data_5I8H
# 
_entry.id   5I8H 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.285 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   5I8H         
WWPDB D_1000218462 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'related structure.' 5I8C unspecified 
PDB .                    5I8E unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5I8H 
_pdbx_database_status.recvd_initial_deposition_date   2016-02-18 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Xu, K.'      1 
'Zhou, T.'    2 
'Kwong, P.D.' 3 
# 
_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            Science 
_citation.journal_id_ASTM           SCIEAS 
_citation.journal_id_CSD            0038 
_citation.journal_id_ISSN           1095-9203 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            352 
_citation.language                  ? 
_citation.page_first                828 
_citation.page_last                 833 
_citation.title                     'Fusion peptide of HIV-1 as a site of vulnerability to neutralizing antibody.' 
_citation.year                      2016 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1126/science.aae0474 
_citation.pdbx_database_id_PubMed   27174988 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Kong, R.'         1  
primary 'Xu, K.'           2  
primary 'Zhou, T.'         3  
primary 'Acharya, P.'      4  
primary 'Lemmin, T.'       5  
primary 'Liu, K.'          6  
primary 'Ozorowski, G.'    7  
primary 'Soto, C.'         8  
primary 'Taft, J.D.'       9  
primary 'Bailer, R.T.'     10 
primary 'Cale, E.M.'       11 
primary 'Chen, L.'         12 
primary 'Choi, C.W.'       13 
primary 'Chuang, G.Y.'     14 
primary 'Doria-Rose, N.A.' 15 
primary 'Druz, A.'         16 
primary 'Georgiev, I.S.'   17 
primary 'Gorman, J.'       18 
primary 'Huang, J.'        19 
primary 'Joyce, M.G.'      20 
primary 'Louder, M.K.'     21 
primary 'Ma, X.'           22 
primary 'McKee, K.'        23 
primary 
;O'Dell, S.
;
24 
primary 'Pancera, M.'      25 
primary 'Yang, Y.'         26 
primary 'Blanchard, S.C.'  27 
primary 'Mothes, W.'       28 
primary 'Burton, D.R.'     29 
primary 'Koff, W.C.'       30 
primary 'Connors, M.'      31 
primary 'Ward, A.B.'       32 
primary 'Kwong, P.D.'      33 
primary 'Mascola, J.R.'    34 
# 
_cell.length_a           252.296 
_cell.length_b           252.296 
_cell.length_c           561.202 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        120.000 
_cell.entry_id           5I8H 
_cell.Z_PDB              36 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.space_group_name_H-M             'H 3 2' 
_symmetry.entry_id                         5I8H 
_symmetry.Int_Tables_number                155 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
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 'BG505 SOSIP.664 gp120'    54064.277 2  ? ? ? ? 
2 polymer     man 'BG505 SOSIP.664 gp41'     17162.525 2  ? ? ? ? 
3 polymer     man 'PGT122 Fab light chain'   22560.941 2  ? ? ? ? 
4 polymer     man 'VRC34.01 Fab heavy chain' 23797.615 2  ? ? ? ? 
5 polymer     man 'VRC34.01 Fab light chain' 23138.766 2  ? ? ? ? 
6 polymer     man 'PGT122 Fab heavy chain'   25434.691 2  ? ? ? ? 
7 non-polymer man N-ACETYL-D-GLUCOSAMINE     221.208   70 ? ? ? ? 
8 non-polymer man BETA-D-MANNOSE             180.156   13 ? ? ? ? 
9 non-polymer man ALPHA-D-MANNOSE            180.156   33 ? ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 
;Endogenous retrovirus group K member 113 Env polyprotein,Endogenous retrovirus group K member 13-1 Env polyprotein,Endogenous retrovirus group K member 18 Env polyprotein,Endogenous retrovirus group K member 19 Env polyprotein,Endogenous retrovirus group K member 21 Env polyprotein,Endogenous retrovirus group K member 24 Env polyprotein,Endogenous retrovirus group K member 25 Env polyprotein,Endogenous retrovirus group K member 6 Env polyprotein,Endogenous retrovirus group K member 8 Env polyprotein,Endogenous retrovirus group K member 9 Env polyprotein
;
2 
;Endogenous retrovirus group K member 113 Env polyprotein,Endogenous retrovirus group K member 13-1 Env polyprotein,Endogenous retrovirus group K member 18 Env polyprotein,Endogenous retrovirus group K member 19 Env polyprotein,Endogenous retrovirus group K member 21 Env polyprotein,Endogenous retrovirus group K member 24 Env polyprotein,Endogenous retrovirus group K member 25 Env polyprotein,Endogenous retrovirus group K member 6 Env polyprotein,Endogenous retrovirus group K member 8 Env polyprotein,Endogenous retrovirus group K member 9 Env polyprotein
;
# 
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 no 
;AENLWVTVYYGVPVWKDAETTLFCASDAKAYETEKHNVWATHACVPTDPNPQEIHLENVTEEFNMWKNNMVEQMHTDIIS
LWDQSLKPCVKLTPLCVTLQCTNVTNNITDDMRGELKNCSFNMTTELRDKKQKVYSLFYRLDVVQINENQGNRSNNSNKE
YRLINCNTSAITQACPKVSFEPIPIHYCAPAGFAILKCKDKKFNGTGPCPSVSTVQCTHGIKPVVSTQLLLNGSLAEEEV
MIRSENITNNAKNILVQFNTPVQINCTRPNNNTRKSIRIGPGQAFYATGDIIGDIRQAHCNVSKATWNETLGKVVKQLRK
HFGNNTIIRFANSSGGDLEVTTHSFNCGGEFFYCNTSGLFNSTWISNTSVQGSNSTGSNDSITLPCRIKQIINMWQRIGQ
AMYAPPIQGVIRCVSNITGLILTRDGGSTNSTTETFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTRCKRRVVGRRRRR
R
;
;AENLWVTVYYGVPVWKDAETTLFCASDAKAYETEKHNVWATHACVPTDPNPQEIHLENVTEEFNMWKNNMVEQMHTDIIS
LWDQSLKPCVKLTPLCVTLQCTNVTNNITDDMRGELKNCSFNMTTELRDKKQKVYSLFYRLDVVQINENQGNRSNNSNKE
YRLINCNTSAITQACPKVSFEPIPIHYCAPAGFAILKCKDKKFNGTGPCPSVSTVQCTHGIKPVVSTQLLLNGSLAEEEV
MIRSENITNNAKNILVQFNTPVQINCTRPNNNTRKSIRIGPGQAFYATGDIIGDIRQAHCNVSKATWNETLGKVVKQLRK
HFGNNTIIRFANSSGGDLEVTTHSFNCGGEFFYCNTSGLFNSTWISNTSVQGSNSTGSNDSITLPCRIKQIINMWQRIGQ
AMYAPPIQGVIRCVSNITGLILTRDGGSTNSTTETFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTRCKRRVVGRRRRR
R
;
A,C ? 
2 'polypeptide(L)' no no 
;AVGIGAVFLGFLGAAGSTMGAASMTLTVQARNLLSGIVQQQSNLLRAIEAQQHLLKLTVWGIKQLQARVLAVERYLRDQQ
LLGIWGCSGKLICCTNVPWNSSWSNRNLSEIWDNMTWLQWDKEISNYTQIIYGLLEESQNQQEKNEQDLLALD
;
;AVGIGAVFLGFLGAAGSTMGAASMTLTVQARNLLSGIVQQQSNLLRAIEAQQHLLKLTVWGIKQLQARVLAVERYLRDQQ
LLGIWGCSGKLICCTNVPWNSSWSNRNLSEIWDNMTWLQWDKEISNYTQIIYGLLEESQNQQEKNEQDLLALD
;
B,D ? 
3 'polypeptide(L)' no no 
;APTFVSVAPGQTARITCGEESLGSRSVIWYQQRPGQAPSLIIYNNNDRPSGIPDRFSGSPGSTFGTTATLTITSVEAGDE
ADYYCHIWDSRRPTNWVFGEGTTLIVLSQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGV
ETTTPSKQSNNKYAASSYLSLTPEQWKSHKSYSCQVTHEGSTVEKTVAPT
;
;APTFVSVAPGQTARITCGEESLGSRSVIWYQQRPGQAPSLIIYNNNDRPSGIPDRFSGSPGSTFGTTATLTITSVEAGDE
ADYYCHIWDSRRPTNWVFGEGTTLIVLSQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGV
ETTTPSKQSNNKYAASSYLSLTPEQWKSHKSYSCQVTHEGSTVEKTVAPT
;
L,J ? 
4 'polypeptide(L)' no no 
;QEVLVQSGAEVKKPGASVKVSCRAFGYTFTGNALHWVRQAPGQGLEWLGWINPHSGDTTTSQKFQGRVYMTRDKSINTAF
LDVTRLTSDDTGIYYCARDKYYGNEAVGMDVWGQGTSVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVT
VSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPK
;
;QEVLVQSGAEVKKPGASVKVSCRAFGYTFTGNALHWVRQAPGQGLEWLGWINPHSGDTTTSQKFQGRVYMTRDKSINTAF
LDVTRLTSDDTGIYYCARDKYYGNEAVGMDVWGQGTSVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVT
VSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPK
;
E,G ? 
5 'polypeptide(L)' no no 
;DIQLTQSPSFLSASVGDKVTITCRASQGVRNELAWYQQKPGKAPNLLIYYASTLQSGVPSRFSATGSGTHFTLTVSSLQP
EDFATYFCQHMSSYPLTFGGGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQ
ESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRG
;
;DIQLTQSPSFLSASVGDKVTITCRASQGVRNELAWYQQKPGKAPNLLIYYASTLQSGVPSRFSATGSGTHFTLTVSSLQP
EDFATYFCQHMSSYPLTFGGGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQ
ESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRG
;
F,H ? 
6 'polypeptide(L)' no no 
;QVHLQESGPGLVKPSETLSLTCNVSGTLVRDNYWSWIRQPLGKQPEWIGYVHDSGDTNYNPSLKSRVHLSLDKSKNLVSL
RLTGVTAADSAIYYCATTKHGRRIYGVVAFKEWFTYFYMDVWGKGTSVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCL
VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSC
;
;QVHLQESGPGLVKPSETLSLTCNVSGTLVRDNYWSWIRQPLGKQPEWIGYVHDSGDTNYNPSLKSRVHLSLDKSKNLVSL
RLTGVTAADSAIYYCATTKHGRRIYGVVAFKEWFTYFYMDVWGKGTSVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCL
VKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSC
;
I,K ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   GLU n 
1 3   ASN n 
1 4   LEU n 
1 5   TRP n 
1 6   VAL n 
1 7   THR n 
1 8   VAL n 
1 9   TYR n 
1 10  TYR n 
1 11  GLY n 
1 12  VAL n 
1 13  PRO n 
1 14  VAL n 
1 15  TRP n 
1 16  LYS n 
1 17  ASP n 
1 18  ALA n 
1 19  GLU n 
1 20  THR n 
1 21  THR n 
1 22  LEU n 
1 23  PHE n 
1 24  CYS n 
1 25  ALA n 
1 26  SER n 
1 27  ASP n 
1 28  ALA n 
1 29  LYS n 
1 30  ALA n 
1 31  TYR n 
1 32  GLU n 
1 33  THR n 
1 34  GLU n 
1 35  LYS n 
1 36  HIS n 
1 37  ASN n 
1 38  VAL n 
1 39  TRP n 
1 40  ALA n 
1 41  THR n 
1 42  HIS n 
1 43  ALA n 
1 44  CYS n 
1 45  VAL n 
1 46  PRO n 
1 47  THR n 
1 48  ASP n 
1 49  PRO n 
1 50  ASN n 
1 51  PRO n 
1 52  GLN n 
1 53  GLU n 
1 54  ILE n 
1 55  HIS n 
1 56  LEU n 
1 57  GLU n 
1 58  ASN n 
1 59  VAL n 
1 60  THR n 
1 61  GLU n 
1 62  GLU n 
1 63  PHE n 
1 64  ASN n 
1 65  MET n 
1 66  TRP n 
1 67  LYS n 
1 68  ASN n 
1 69  ASN n 
1 70  MET n 
1 71  VAL n 
1 72  GLU n 
1 73  GLN n 
1 74  MET n 
1 75  HIS n 
1 76  THR n 
1 77  ASP n 
1 78  ILE n 
1 79  ILE n 
1 80  SER n 
1 81  LEU n 
1 82  TRP n 
1 83  ASP n 
1 84  GLN n 
1 85  SER n 
1 86  LEU n 
1 87  LYS n 
1 88  PRO n 
1 89  CYS n 
1 90  VAL n 
1 91  LYS n 
1 92  LEU n 
1 93  THR n 
1 94  PRO n 
1 95  LEU n 
1 96  CYS n 
1 97  VAL n 
1 98  THR n 
1 99  LEU n 
1 100 GLN n 
1 101 CYS n 
1 102 THR n 
1 103 ASN n 
1 104 VAL n 
1 105 THR n 
1 106 ASN n 
1 107 ASN n 
1 108 ILE n 
1 109 THR n 
1 110 ASP n 
1 111 ASP n 
1 112 MET n 
1 113 ARG n 
1 114 GLY n 
1 115 GLU n 
1 116 LEU n 
1 117 LYS n 
1 118 ASN n 
1 119 CYS n 
1 120 SER n 
1 121 PHE n 
1 122 ASN n 
1 123 MET n 
1 124 THR n 
1 125 THR n 
1 126 GLU n 
1 127 LEU n 
1 128 ARG n 
1 129 ASP n 
1 130 LYS n 
1 131 LYS n 
1 132 GLN n 
1 133 LYS n 
1 134 VAL n 
1 135 TYR n 
1 136 SER n 
1 137 LEU n 
1 138 PHE n 
1 139 TYR n 
1 140 ARG n 
1 141 LEU n 
1 142 ASP n 
1 143 VAL n 
1 144 VAL n 
1 145 GLN n 
1 146 ILE n 
1 147 ASN n 
1 148 GLU n 
1 149 ASN n 
1 150 GLN n 
1 151 GLY n 
1 152 ASN n 
1 153 ARG n 
1 154 SER n 
1 155 ASN n 
1 156 ASN n 
1 157 SER n 
1 158 ASN n 
1 159 LYS n 
1 160 GLU n 
1 161 TYR n 
1 162 ARG n 
1 163 LEU n 
1 164 ILE n 
1 165 ASN n 
1 166 CYS n 
1 167 ASN n 
1 168 THR n 
1 169 SER n 
1 170 ALA n 
1 171 ILE n 
1 172 THR n 
1 173 GLN n 
1 174 ALA n 
1 175 CYS n 
1 176 PRO n 
1 177 LYS n 
1 178 VAL n 
1 179 SER n 
1 180 PHE n 
1 181 GLU n 
1 182 PRO n 
1 183 ILE n 
1 184 PRO n 
1 185 ILE n 
1 186 HIS n 
1 187 TYR n 
1 188 CYS n 
1 189 ALA n 
1 190 PRO n 
1 191 ALA n 
1 192 GLY n 
1 193 PHE n 
1 194 ALA n 
1 195 ILE n 
1 196 LEU n 
1 197 LYS n 
1 198 CYS n 
1 199 LYS n 
1 200 ASP n 
1 201 LYS n 
1 202 LYS n 
1 203 PHE n 
1 204 ASN n 
1 205 GLY n 
1 206 THR n 
1 207 GLY n 
1 208 PRO n 
1 209 CYS n 
1 210 PRO n 
1 211 SER n 
1 212 VAL n 
1 213 SER n 
1 214 THR n 
1 215 VAL n 
1 216 GLN n 
1 217 CYS n 
1 218 THR n 
1 219 HIS n 
1 220 GLY n 
1 221 ILE n 
1 222 LYS n 
1 223 PRO n 
1 224 VAL n 
1 225 VAL n 
1 226 SER n 
1 227 THR n 
1 228 GLN n 
1 229 LEU n 
1 230 LEU n 
1 231 LEU n 
1 232 ASN n 
1 233 GLY n 
1 234 SER n 
1 235 LEU n 
1 236 ALA n 
1 237 GLU n 
1 238 GLU n 
1 239 GLU n 
1 240 VAL n 
1 241 MET n 
1 242 ILE n 
1 243 ARG n 
1 244 SER n 
1 245 GLU n 
1 246 ASN n 
1 247 ILE n 
1 248 THR n 
1 249 ASN n 
1 250 ASN n 
1 251 ALA n 
1 252 LYS n 
1 253 ASN n 
1 254 ILE n 
1 255 LEU n 
1 256 VAL n 
1 257 GLN n 
1 258 PHE n 
1 259 ASN n 
1 260 THR n 
1 261 PRO n 
1 262 VAL n 
1 263 GLN n 
1 264 ILE n 
1 265 ASN n 
1 266 CYS n 
1 267 THR n 
1 268 ARG n 
1 269 PRO n 
1 270 ASN n 
1 271 ASN n 
1 272 ASN n 
1 273 THR n 
1 274 ARG n 
1 275 LYS n 
1 276 SER n 
1 277 ILE n 
1 278 ARG n 
1 279 ILE n 
1 280 GLY n 
1 281 PRO n 
1 282 GLY n 
1 283 GLN n 
1 284 ALA n 
1 285 PHE n 
1 286 TYR n 
1 287 ALA n 
1 288 THR n 
1 289 GLY n 
1 290 ASP n 
1 291 ILE n 
1 292 ILE n 
1 293 GLY n 
1 294 ASP n 
1 295 ILE n 
1 296 ARG n 
1 297 GLN n 
1 298 ALA n 
1 299 HIS n 
1 300 CYS n 
1 301 ASN n 
1 302 VAL n 
1 303 SER n 
1 304 LYS n 
1 305 ALA n 
1 306 THR n 
1 307 TRP n 
1 308 ASN n 
1 309 GLU n 
1 310 THR n 
1 311 LEU n 
1 312 GLY n 
1 313 LYS n 
1 314 VAL n 
1 315 VAL n 
1 316 LYS n 
1 317 GLN n 
1 318 LEU n 
1 319 ARG n 
1 320 LYS n 
1 321 HIS n 
1 322 PHE n 
1 323 GLY n 
1 324 ASN n 
1 325 ASN n 
1 326 THR n 
1 327 ILE n 
1 328 ILE n 
1 329 ARG n 
1 330 PHE n 
1 331 ALA n 
1 332 ASN n 
1 333 SER n 
1 334 SER n 
1 335 GLY n 
1 336 GLY n 
1 337 ASP n 
1 338 LEU n 
1 339 GLU n 
1 340 VAL n 
1 341 THR n 
1 342 THR n 
1 343 HIS n 
1 344 SER n 
1 345 PHE n 
1 346 ASN n 
1 347 CYS n 
1 348 GLY n 
1 349 GLY n 
1 350 GLU n 
1 351 PHE n 
1 352 PHE n 
1 353 TYR n 
1 354 CYS n 
1 355 ASN n 
1 356 THR n 
1 357 SER n 
1 358 GLY n 
1 359 LEU n 
1 360 PHE n 
1 361 ASN n 
1 362 SER n 
1 363 THR n 
1 364 TRP n 
1 365 ILE n 
1 366 SER n 
1 367 ASN n 
1 368 THR n 
1 369 SER n 
1 370 VAL n 
1 371 GLN n 
1 372 GLY n 
1 373 SER n 
1 374 ASN n 
1 375 SER n 
1 376 THR n 
1 377 GLY n 
1 378 SER n 
1 379 ASN n 
1 380 ASP n 
1 381 SER n 
1 382 ILE n 
1 383 THR n 
1 384 LEU n 
1 385 PRO n 
1 386 CYS n 
1 387 ARG n 
1 388 ILE n 
1 389 LYS n 
1 390 GLN n 
1 391 ILE n 
1 392 ILE n 
1 393 ASN n 
1 394 MET n 
1 395 TRP n 
1 396 GLN n 
1 397 ARG n 
1 398 ILE n 
1 399 GLY n 
1 400 GLN n 
1 401 ALA n 
1 402 MET n 
1 403 TYR n 
1 404 ALA n 
1 405 PRO n 
1 406 PRO n 
1 407 ILE n 
1 408 GLN n 
1 409 GLY n 
1 410 VAL n 
1 411 ILE n 
1 412 ARG n 
1 413 CYS n 
1 414 VAL n 
1 415 SER n 
1 416 ASN n 
1 417 ILE n 
1 418 THR n 
1 419 GLY n 
1 420 LEU n 
1 421 ILE n 
1 422 LEU n 
1 423 THR n 
1 424 ARG n 
1 425 ASP n 
1 426 GLY n 
1 427 GLY n 
1 428 SER n 
1 429 THR n 
1 430 ASN n 
1 431 SER n 
1 432 THR n 
1 433 THR n 
1 434 GLU n 
1 435 THR n 
1 436 PHE n 
1 437 ARG n 
1 438 PRO n 
1 439 GLY n 
1 440 GLY n 
1 441 GLY n 
1 442 ASP n 
1 443 MET n 
1 444 ARG n 
1 445 ASP n 
1 446 ASN n 
1 447 TRP n 
1 448 ARG n 
1 449 SER n 
1 450 GLU n 
1 451 LEU n 
1 452 TYR n 
1 453 LYS n 
1 454 TYR n 
1 455 LYS n 
1 456 VAL n 
1 457 VAL n 
1 458 LYS n 
1 459 ILE n 
1 460 GLU n 
1 461 PRO n 
1 462 LEU n 
1 463 GLY n 
1 464 VAL n 
1 465 ALA n 
1 466 PRO n 
1 467 THR n 
1 468 ARG n 
1 469 CYS n 
1 470 LYS n 
1 471 ARG n 
1 472 ARG n 
1 473 VAL n 
1 474 VAL n 
1 475 GLY n 
1 476 ARG n 
1 477 ARG n 
1 478 ARG n 
1 479 ARG n 
1 480 ARG n 
1 481 ARG n 
2 1   ALA n 
2 2   VAL n 
2 3   GLY n 
2 4   ILE n 
2 5   GLY n 
2 6   ALA n 
2 7   VAL n 
2 8   PHE n 
2 9   LEU n 
2 10  GLY n 
2 11  PHE n 
2 12  LEU n 
2 13  GLY n 
2 14  ALA n 
2 15  ALA n 
2 16  GLY n 
2 17  SER n 
2 18  THR n 
2 19  MET n 
2 20  GLY n 
2 21  ALA n 
2 22  ALA n 
2 23  SER n 
2 24  MET n 
2 25  THR n 
2 26  LEU n 
2 27  THR n 
2 28  VAL n 
2 29  GLN n 
2 30  ALA n 
2 31  ARG n 
2 32  ASN n 
2 33  LEU n 
2 34  LEU n 
2 35  SER n 
2 36  GLY n 
2 37  ILE n 
2 38  VAL n 
2 39  GLN n 
2 40  GLN n 
2 41  GLN n 
2 42  SER n 
2 43  ASN n 
2 44  LEU n 
2 45  LEU n 
2 46  ARG n 
2 47  ALA n 
2 48  ILE n 
2 49  GLU n 
2 50  ALA n 
2 51  GLN n 
2 52  GLN n 
2 53  HIS n 
2 54  LEU n 
2 55  LEU n 
2 56  LYS n 
2 57  LEU n 
2 58  THR n 
2 59  VAL n 
2 60  TRP n 
2 61  GLY n 
2 62  ILE n 
2 63  LYS n 
2 64  GLN n 
2 65  LEU n 
2 66  GLN n 
2 67  ALA n 
2 68  ARG n 
2 69  VAL n 
2 70  LEU n 
2 71  ALA n 
2 72  VAL n 
2 73  GLU n 
2 74  ARG n 
2 75  TYR n 
2 76  LEU n 
2 77  ARG n 
2 78  ASP n 
2 79  GLN n 
2 80  GLN n 
2 81  LEU n 
2 82  LEU n 
2 83  GLY n 
2 84  ILE n 
2 85  TRP n 
2 86  GLY n 
2 87  CYS n 
2 88  SER n 
2 89  GLY n 
2 90  LYS n 
2 91  LEU n 
2 92  ILE n 
2 93  CYS n 
2 94  CYS n 
2 95  THR n 
2 96  ASN n 
2 97  VAL n 
2 98  PRO n 
2 99  TRP n 
2 100 ASN n 
2 101 SER n 
2 102 SER n 
2 103 TRP n 
2 104 SER n 
2 105 ASN n 
2 106 ARG n 
2 107 ASN n 
2 108 LEU n 
2 109 SER n 
2 110 GLU n 
2 111 ILE n 
2 112 TRP n 
2 113 ASP n 
2 114 ASN n 
2 115 MET n 
2 116 THR n 
2 117 TRP n 
2 118 LEU n 
2 119 GLN n 
2 120 TRP n 
2 121 ASP n 
2 122 LYS n 
2 123 GLU n 
2 124 ILE n 
2 125 SER n 
2 126 ASN n 
2 127 TYR n 
2 128 THR n 
2 129 GLN n 
2 130 ILE n 
2 131 ILE n 
2 132 TYR n 
2 133 GLY n 
2 134 LEU n 
2 135 LEU n 
2 136 GLU n 
2 137 GLU n 
2 138 SER n 
2 139 GLN n 
2 140 ASN n 
2 141 GLN n 
2 142 GLN n 
2 143 GLU n 
2 144 LYS n 
2 145 ASN n 
2 146 GLU n 
2 147 GLN n 
2 148 ASP n 
2 149 LEU n 
2 150 LEU n 
2 151 ALA n 
2 152 LEU n 
2 153 ASP n 
3 1   ALA n 
3 2   PRO n 
3 3   THR n 
3 4   PHE n 
3 5   VAL n 
3 6   SER n 
3 7   VAL n 
3 8   ALA n 
3 9   PRO n 
3 10  GLY n 
3 11  GLN n 
3 12  THR n 
3 13  ALA n 
3 14  ARG n 
3 15  ILE n 
3 16  THR n 
3 17  CYS n 
3 18  GLY n 
3 19  GLU n 
3 20  GLU n 
3 21  SER n 
3 22  LEU n 
3 23  GLY n 
3 24  SER n 
3 25  ARG n 
3 26  SER n 
3 27  VAL n 
3 28  ILE n 
3 29  TRP n 
3 30  TYR n 
3 31  GLN n 
3 32  GLN n 
3 33  ARG n 
3 34  PRO n 
3 35  GLY n 
3 36  GLN n 
3 37  ALA n 
3 38  PRO n 
3 39  SER n 
3 40  LEU n 
3 41  ILE n 
3 42  ILE n 
3 43  TYR n 
3 44  ASN n 
3 45  ASN n 
3 46  ASN n 
3 47  ASP n 
3 48  ARG n 
3 49  PRO n 
3 50  SER n 
3 51  GLY n 
3 52  ILE n 
3 53  PRO n 
3 54  ASP n 
3 55  ARG n 
3 56  PHE n 
3 57  SER n 
3 58  GLY n 
3 59  SER n 
3 60  PRO n 
3 61  GLY n 
3 62  SER n 
3 63  THR n 
3 64  PHE n 
3 65  GLY n 
3 66  THR n 
3 67  THR n 
3 68  ALA n 
3 69  THR n 
3 70  LEU n 
3 71  THR n 
3 72  ILE n 
3 73  THR n 
3 74  SER n 
3 75  VAL n 
3 76  GLU n 
3 77  ALA n 
3 78  GLY n 
3 79  ASP n 
3 80  GLU n 
3 81  ALA n 
3 82  ASP n 
3 83  TYR n 
3 84  TYR n 
3 85  CYS n 
3 86  HIS n 
3 87  ILE n 
3 88  TRP n 
3 89  ASP n 
3 90  SER n 
3 91  ARG n 
3 92  ARG n 
3 93  PRO n 
3 94  THR n 
3 95  ASN n 
3 96  TRP n 
3 97  VAL n 
3 98  PHE n 
3 99  GLY n 
3 100 GLU n 
3 101 GLY n 
3 102 THR n 
3 103 THR n 
3 104 LEU n 
3 105 ILE n 
3 106 VAL n 
3 107 LEU n 
3 108 SER n 
3 109 GLN n 
3 110 PRO n 
3 111 LYS n 
3 112 ALA n 
3 113 ALA n 
3 114 PRO n 
3 115 SER n 
3 116 VAL n 
3 117 THR n 
3 118 LEU n 
3 119 PHE n 
3 120 PRO n 
3 121 PRO n 
3 122 SER n 
3 123 SER n 
3 124 GLU n 
3 125 GLU n 
3 126 LEU n 
3 127 GLN n 
3 128 ALA n 
3 129 ASN n 
3 130 LYS n 
3 131 ALA n 
3 132 THR n 
3 133 LEU n 
3 134 VAL n 
3 135 CYS n 
3 136 LEU n 
3 137 ILE n 
3 138 SER n 
3 139 ASP n 
3 140 PHE n 
3 141 TYR n 
3 142 PRO n 
3 143 GLY n 
3 144 ALA n 
3 145 VAL n 
3 146 THR n 
3 147 VAL n 
3 148 ALA n 
3 149 TRP n 
3 150 LYS n 
3 151 ALA n 
3 152 ASP n 
3 153 SER n 
3 154 SER n 
3 155 PRO n 
3 156 VAL n 
3 157 LYS n 
3 158 ALA n 
3 159 GLY n 
3 160 VAL n 
3 161 GLU n 
3 162 THR n 
3 163 THR n 
3 164 THR n 
3 165 PRO n 
3 166 SER n 
3 167 LYS n 
3 168 GLN n 
3 169 SER n 
3 170 ASN n 
3 171 ASN n 
3 172 LYS n 
3 173 TYR n 
3 174 ALA n 
3 175 ALA n 
3 176 SER n 
3 177 SER n 
3 178 TYR n 
3 179 LEU n 
3 180 SER n 
3 181 LEU n 
3 182 THR n 
3 183 PRO n 
3 184 GLU n 
3 185 GLN n 
3 186 TRP n 
3 187 LYS n 
3 188 SER n 
3 189 HIS n 
3 190 LYS n 
3 191 SER n 
3 192 TYR n 
3 193 SER n 
3 194 CYS n 
3 195 GLN n 
3 196 VAL n 
3 197 THR n 
3 198 HIS n 
3 199 GLU n 
3 200 GLY n 
3 201 SER n 
3 202 THR n 
3 203 VAL n 
3 204 GLU n 
3 205 LYS n 
3 206 THR n 
3 207 VAL n 
3 208 ALA n 
3 209 PRO n 
3 210 THR n 
4 1   GLN n 
4 2   GLU n 
4 3   VAL n 
4 4   LEU n 
4 5   VAL n 
4 6   GLN n 
4 7   SER n 
4 8   GLY n 
4 9   ALA n 
4 10  GLU n 
4 11  VAL n 
4 12  LYS n 
4 13  LYS n 
4 14  PRO n 
4 15  GLY n 
4 16  ALA n 
4 17  SER n 
4 18  VAL n 
4 19  LYS n 
4 20  VAL n 
4 21  SER n 
4 22  CYS n 
4 23  ARG n 
4 24  ALA n 
4 25  PHE n 
4 26  GLY n 
4 27  TYR n 
4 28  THR n 
4 29  PHE n 
4 30  THR n 
4 31  GLY n 
4 32  ASN n 
4 33  ALA n 
4 34  LEU n 
4 35  HIS n 
4 36  TRP n 
4 37  VAL n 
4 38  ARG n 
4 39  GLN n 
4 40  ALA n 
4 41  PRO n 
4 42  GLY n 
4 43  GLN n 
4 44  GLY n 
4 45  LEU n 
4 46  GLU n 
4 47  TRP n 
4 48  LEU n 
4 49  GLY n 
4 50  TRP n 
4 51  ILE n 
4 52  ASN n 
4 53  PRO n 
4 54  HIS n 
4 55  SER n 
4 56  GLY n 
4 57  ASP n 
4 58  THR n 
4 59  THR n 
4 60  THR n 
4 61  SER n 
4 62  GLN n 
4 63  LYS n 
4 64  PHE n 
4 65  GLN n 
4 66  GLY n 
4 67  ARG n 
4 68  VAL n 
4 69  TYR n 
4 70  MET n 
4 71  THR n 
4 72  ARG n 
4 73  ASP n 
4 74  LYS n 
4 75  SER n 
4 76  ILE n 
4 77  ASN n 
4 78  THR n 
4 79  ALA n 
4 80  PHE n 
4 81  LEU n 
4 82  ASP n 
4 83  VAL n 
4 84  THR n 
4 85  ARG n 
4 86  LEU n 
4 87  THR n 
4 88  SER n 
4 89  ASP n 
4 90  ASP n 
4 91  THR n 
4 92  GLY n 
4 93  ILE n 
4 94  TYR n 
4 95  TYR n 
4 96  CYS n 
4 97  ALA n 
4 98  ARG n 
4 99  ASP n 
4 100 LYS n 
4 101 TYR n 
4 102 TYR n 
4 103 GLY n 
4 104 ASN n 
4 105 GLU n 
4 106 ALA n 
4 107 VAL n 
4 108 GLY n 
4 109 MET n 
4 110 ASP n 
4 111 VAL n 
4 112 TRP n 
4 113 GLY n 
4 114 GLN n 
4 115 GLY n 
4 116 THR n 
4 117 SER n 
4 118 VAL n 
4 119 THR n 
4 120 VAL n 
4 121 SER n 
4 122 SER n 
4 123 ALA n 
4 124 SER n 
4 125 THR n 
4 126 LYS n 
4 127 GLY n 
4 128 PRO n 
4 129 SER n 
4 130 VAL n 
4 131 PHE n 
4 132 PRO n 
4 133 LEU n 
4 134 ALA n 
4 135 PRO n 
4 136 SER n 
4 137 SER n 
4 138 LYS n 
4 139 SER n 
4 140 THR n 
4 141 SER n 
4 142 GLY n 
4 143 GLY n 
4 144 THR n 
4 145 ALA n 
4 146 ALA n 
4 147 LEU n 
4 148 GLY n 
4 149 CYS n 
4 150 LEU n 
4 151 VAL n 
4 152 LYS n 
4 153 ASP n 
4 154 TYR n 
4 155 PHE n 
4 156 PRO n 
4 157 GLU n 
4 158 PRO n 
4 159 VAL n 
4 160 THR n 
4 161 VAL n 
4 162 SER n 
4 163 TRP n 
4 164 ASN n 
4 165 SER n 
4 166 GLY n 
4 167 ALA n 
4 168 LEU n 
4 169 THR n 
4 170 SER n 
4 171 GLY n 
4 172 VAL n 
4 173 HIS n 
4 174 THR n 
4 175 PHE n 
4 176 PRO n 
4 177 ALA n 
4 178 VAL n 
4 179 LEU n 
4 180 GLN n 
4 181 SER n 
4 182 SER n 
4 183 GLY n 
4 184 LEU n 
4 185 TYR n 
4 186 SER n 
4 187 LEU n 
4 188 SER n 
4 189 SER n 
4 190 VAL n 
4 191 VAL n 
4 192 THR n 
4 193 VAL n 
4 194 PRO n 
4 195 SER n 
4 196 SER n 
4 197 SER n 
4 198 LEU n 
4 199 GLY n 
4 200 THR n 
4 201 GLN n 
4 202 THR n 
4 203 TYR n 
4 204 ILE n 
4 205 CYS n 
4 206 ASN n 
4 207 VAL n 
4 208 ASN n 
4 209 HIS n 
4 210 LYS n 
4 211 PRO n 
4 212 SER n 
4 213 ASN n 
4 214 THR n 
4 215 LYS n 
4 216 VAL n 
4 217 ASP n 
4 218 LYS n 
4 219 LYS n 
4 220 VAL n 
4 221 GLU n 
4 222 PRO n 
4 223 LYS n 
5 1   ASP n 
5 2   ILE n 
5 3   GLN n 
5 4   LEU n 
5 5   THR n 
5 6   GLN n 
5 7   SER n 
5 8   PRO n 
5 9   SER n 
5 10  PHE n 
5 11  LEU n 
5 12  SER n 
5 13  ALA n 
5 14  SER n 
5 15  VAL n 
5 16  GLY n 
5 17  ASP n 
5 18  LYS n 
5 19  VAL n 
5 20  THR n 
5 21  ILE n 
5 22  THR n 
5 23  CYS n 
5 24  ARG n 
5 25  ALA n 
5 26  SER n 
5 27  GLN n 
5 28  GLY n 
5 29  VAL n 
5 30  ARG n 
5 31  ASN n 
5 32  GLU n 
5 33  LEU n 
5 34  ALA n 
5 35  TRP n 
5 36  TYR n 
5 37  GLN n 
5 38  GLN n 
5 39  LYS n 
5 40  PRO n 
5 41  GLY n 
5 42  LYS n 
5 43  ALA n 
5 44  PRO n 
5 45  ASN n 
5 46  LEU n 
5 47  LEU n 
5 48  ILE n 
5 49  TYR n 
5 50  TYR n 
5 51  ALA n 
5 52  SER n 
5 53  THR n 
5 54  LEU n 
5 55  GLN n 
5 56  SER n 
5 57  GLY n 
5 58  VAL n 
5 59  PRO n 
5 60  SER n 
5 61  ARG n 
5 62  PHE n 
5 63  SER n 
5 64  ALA n 
5 65  THR n 
5 66  GLY n 
5 67  SER n 
5 68  GLY n 
5 69  THR n 
5 70  HIS n 
5 71  PHE n 
5 72  THR n 
5 73  LEU n 
5 74  THR n 
5 75  VAL n 
5 76  SER n 
5 77  SER n 
5 78  LEU n 
5 79  GLN n 
5 80  PRO n 
5 81  GLU n 
5 82  ASP n 
5 83  PHE n 
5 84  ALA n 
5 85  THR n 
5 86  TYR n 
5 87  PHE n 
5 88  CYS n 
5 89  GLN n 
5 90  HIS n 
5 91  MET n 
5 92  SER n 
5 93  SER n 
5 94  TYR n 
5 95  PRO n 
5 96  LEU n 
5 97  THR n 
5 98  PHE n 
5 99  GLY n 
5 100 GLY n 
5 101 GLY n 
5 102 THR n 
5 103 LYS n 
5 104 VAL n 
5 105 GLU n 
5 106 ILE n 
5 107 LYS n 
5 108 ARG n 
5 109 THR n 
5 110 VAL n 
5 111 ALA n 
5 112 ALA n 
5 113 PRO n 
5 114 SER n 
5 115 VAL n 
5 116 PHE n 
5 117 ILE n 
5 118 PHE n 
5 119 PRO n 
5 120 PRO n 
5 121 SER n 
5 122 ASP n 
5 123 GLU n 
5 124 GLN n 
5 125 LEU n 
5 126 LYS n 
5 127 SER n 
5 128 GLY n 
5 129 THR n 
5 130 ALA n 
5 131 SER n 
5 132 VAL n 
5 133 VAL n 
5 134 CYS n 
5 135 LEU n 
5 136 LEU n 
5 137 ASN n 
5 138 ASN n 
5 139 PHE n 
5 140 TYR n 
5 141 PRO n 
5 142 ARG n 
5 143 GLU n 
5 144 ALA n 
5 145 LYS n 
5 146 VAL n 
5 147 GLN n 
5 148 TRP n 
5 149 LYS n 
5 150 VAL n 
5 151 ASP n 
5 152 ASN n 
5 153 ALA n 
5 154 LEU n 
5 155 GLN n 
5 156 SER n 
5 157 GLY n 
5 158 ASN n 
5 159 SER n 
5 160 GLN n 
5 161 GLU n 
5 162 SER n 
5 163 VAL n 
5 164 THR n 
5 165 GLU n 
5 166 GLN n 
5 167 ASP n 
5 168 SER n 
5 169 LYS n 
5 170 ASP n 
5 171 SER n 
5 172 THR n 
5 173 TYR n 
5 174 SER n 
5 175 LEU n 
5 176 SER n 
5 177 SER n 
5 178 THR n 
5 179 LEU n 
5 180 THR n 
5 181 LEU n 
5 182 SER n 
5 183 LYS n 
5 184 ALA n 
5 185 ASP n 
5 186 TYR n 
5 187 GLU n 
5 188 LYS n 
5 189 HIS n 
5 190 LYS n 
5 191 VAL n 
5 192 TYR n 
5 193 ALA n 
5 194 CYS n 
5 195 GLU n 
5 196 VAL n 
5 197 THR n 
5 198 HIS n 
5 199 GLN n 
5 200 GLY n 
5 201 LEU n 
5 202 SER n 
5 203 SER n 
5 204 PRO n 
5 205 VAL n 
5 206 THR n 
5 207 LYS n 
5 208 SER n 
5 209 PHE n 
5 210 ASN n 
5 211 ARG n 
5 212 GLY n 
6 1   GLN n 
6 2   VAL n 
6 3   HIS n 
6 4   LEU n 
6 5   GLN n 
6 6   GLU n 
6 7   SER n 
6 8   GLY n 
6 9   PRO n 
6 10  GLY n 
6 11  LEU n 
6 12  VAL n 
6 13  LYS n 
6 14  PRO n 
6 15  SER n 
6 16  GLU n 
6 17  THR n 
6 18  LEU n 
6 19  SER n 
6 20  LEU n 
6 21  THR n 
6 22  CYS n 
6 23  ASN n 
6 24  VAL n 
6 25  SER n 
6 26  GLY n 
6 27  THR n 
6 28  LEU n 
6 29  VAL n 
6 30  ARG n 
6 31  ASP n 
6 32  ASN n 
6 33  TYR n 
6 34  TRP n 
6 35  SER n 
6 36  TRP n 
6 37  ILE n 
6 38  ARG n 
6 39  GLN n 
6 40  PRO n 
6 41  LEU n 
6 42  GLY n 
6 43  LYS n 
6 44  GLN n 
6 45  PRO n 
6 46  GLU n 
6 47  TRP n 
6 48  ILE n 
6 49  GLY n 
6 50  TYR n 
6 51  VAL n 
6 52  HIS n 
6 53  ASP n 
6 54  SER n 
6 55  GLY n 
6 56  ASP n 
6 57  THR n 
6 58  ASN n 
6 59  TYR n 
6 60  ASN n 
6 61  PRO n 
6 62  SER n 
6 63  LEU n 
6 64  LYS n 
6 65  SER n 
6 66  ARG n 
6 67  VAL n 
6 68  HIS n 
6 69  LEU n 
6 70  SER n 
6 71  LEU n 
6 72  ASP n 
6 73  LYS n 
6 74  SER n 
6 75  LYS n 
6 76  ASN n 
6 77  LEU n 
6 78  VAL n 
6 79  SER n 
6 80  LEU n 
6 81  ARG n 
6 82  LEU n 
6 83  THR n 
6 84  GLY n 
6 85  VAL n 
6 86  THR n 
6 87  ALA n 
6 88  ALA n 
6 89  ASP n 
6 90  SER n 
6 91  ALA n 
6 92  ILE n 
6 93  TYR n 
6 94  TYR n 
6 95  CYS n 
6 96  ALA n 
6 97  THR n 
6 98  THR n 
6 99  LYS n 
6 100 HIS n 
6 101 GLY n 
6 102 ARG n 
6 103 ARG n 
6 104 ILE n 
6 105 TYR n 
6 106 GLY n 
6 107 VAL n 
6 108 VAL n 
6 109 ALA n 
6 110 PHE n 
6 111 LYS n 
6 112 GLU n 
6 113 TRP n 
6 114 PHE n 
6 115 THR n 
6 116 TYR n 
6 117 PHE n 
6 118 TYR n 
6 119 MET n 
6 120 ASP n 
6 121 VAL n 
6 122 TRP n 
6 123 GLY n 
6 124 LYS n 
6 125 GLY n 
6 126 THR n 
6 127 SER n 
6 128 VAL n 
6 129 THR n 
6 130 VAL n 
6 131 SER n 
6 132 SER n 
6 133 ALA n 
6 134 SER n 
6 135 THR n 
6 136 LYS n 
6 137 GLY n 
6 138 PRO n 
6 139 SER n 
6 140 VAL n 
6 141 PHE n 
6 142 PRO n 
6 143 LEU n 
6 144 ALA n 
6 145 PRO n 
6 146 SER n 
6 147 SER n 
6 148 LYS n 
6 149 SER n 
6 150 THR n 
6 151 SER n 
6 152 GLY n 
6 153 GLY n 
6 154 THR n 
6 155 ALA n 
6 156 ALA n 
6 157 LEU n 
6 158 GLY n 
6 159 CYS n 
6 160 LEU n 
6 161 VAL n 
6 162 LYS n 
6 163 ASP n 
6 164 TYR n 
6 165 PHE n 
6 166 PRO n 
6 167 GLU n 
6 168 PRO n 
6 169 VAL n 
6 170 THR n 
6 171 VAL n 
6 172 SER n 
6 173 TRP n 
6 174 ASN n 
6 175 SER n 
6 176 GLY n 
6 177 ALA n 
6 178 LEU n 
6 179 THR n 
6 180 SER n 
6 181 GLY n 
6 182 VAL n 
6 183 HIS n 
6 184 THR n 
6 185 PHE n 
6 186 PRO n 
6 187 ALA n 
6 188 VAL n 
6 189 LEU n 
6 190 GLN n 
6 191 SER n 
6 192 SER n 
6 193 GLY n 
6 194 LEU n 
6 195 TYR n 
6 196 SER n 
6 197 LEU n 
6 198 SER n 
6 199 SER n 
6 200 VAL n 
6 201 VAL n 
6 202 THR n 
6 203 VAL n 
6 204 PRO n 
6 205 SER n 
6 206 SER n 
6 207 SER n 
6 208 LEU n 
6 209 GLY n 
6 210 THR n 
6 211 GLN n 
6 212 THR n 
6 213 TYR n 
6 214 ILE n 
6 215 CYS n 
6 216 ASN n 
6 217 VAL n 
6 218 ASN n 
6 219 HIS n 
6 220 LYS n 
6 221 PRO n 
6 222 SER n 
6 223 ASN n 
6 224 THR n 
6 225 LYS n 
6 226 VAL n 
6 227 ASP n 
6 228 LYS n 
6 229 ARG n 
6 230 VAL n 
6 231 GLU n 
6 232 PRO n 
6 233 LYS n 
6 234 SER n 
6 235 CYS 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' 1 481 ? ? env ? ? ? ? ? ? 'Human immunodeficiency virus 1' 11676 ? ? ? ? ? ? ? ? 'Homo sapiens' 
9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 153 ? ? env ? ? ? ? ? ? 'Human immunodeficiency virus 1' 11676 ? ? ? ? ? ? ? ? 'Homo sapiens' 
9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 210 ? ? ?   ? ? ? ? ? ? 'Homo sapiens'                   9606  ? ? ? ? ? ? ? ? 'Homo sapiens' 
9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 223 ? ? ?   ? ? ? ? ? ? 'Homo sapiens'                   9606  ? ? ? ? ? ? ? ? 'Homo sapiens' 
9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
5 1 sample 'Biological sequence' 1 212 ? ? ?   ? ? ? ? ? ? 'Homo sapiens'                   9606  ? ? ? ? ? ? ? ? 'Homo sapiens' 
9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
6 1 sample 'Biological sequence' 1 235 ? ? ?   ? ? ? ? ? ? 'Homo sapiens'                   9606  ? ? ? ? ? ? ? ? 'Homo sapiens' 
9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 Q2N0S6_9HIV1 Q2N0S6 ? 1 
;AENLWVTVYYGVPVWKDAETTLFCASDAKAYETEKHNVWATHACVPTDPNPQEIHLENVTEEFNMWKNNMVEQMHTDIIS
LWDQSLKPCVKLTPLCVTLQCTNVTNNITDDMRGELKNCSFNMTTELRDKKQKVYSLFYRLDVVQINENQGNRSNNSNKE
YRLINCNTSAITQACPKVSFEPIPIHYCAPAGFAILKCKDKKFNGTGPCPSVSTVQCTHGIKPVVSTQLLLNGSLAEEEV
MIRSENITNNAKNILVQFNTPVQINCTRPNNNTRKSIRIGPGQAFYATGDIIGDIRQAHCTVSKATWNETLGKVVKQLRK
HFGNNTIIRFANSSGGDLEVTTHSFNCGGEFFYCNTSGLFNSTWISNTSVQGSNSTGSNDSITLPCRIKQIINMWQRIGQ
AMYAPPIQGVIRCVSNITGLILTRDGGSTNSTTETFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTRAKRRVVGREKR
;
30  
2 UNP Q2N0S6_9HIV1 Q2N0S6 ? 2 
;AVGIGAVFLGFLGAAGSTMGAASMTLTVQARNLLSGIVQQQSNLLRAIEAQQHLLKLTVWGIKQLQARVLAVERYLRDQQ
LLGIWGCSGKLICTTNVPWNSSWSNRNLSEIWDNMTWLQWDKEISNYTQIIYGLLEESQNQQEKNEQDLLALD
;
509 
3 PDB 5I8H         5I8H   ? 3 ? 1   
4 PDB 5I8H         5I8H   ? 4 ? 1   
5 PDB 5I8H         5I8H   ? 5 ? 1   
6 PDB 5I8H         5I8H   ? 6 ? 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 5I8H A 1 ? 479 ? Q2N0S6 30  ? 508 ? 31  511 
2  2 5I8H B 1 ? 153 ? Q2N0S6 509 ? 661 ? 512 664 
3  1 5I8H C 1 ? 479 ? Q2N0S6 30  ? 508 ? 31  511 
4  3 5I8H L 1 ? 210 ? 5I8H   6   ? 210 ? 6   210 
5  4 5I8H E 1 ? 223 ? 5I8H   1   ? 214 ? 1   214 
6  5 5I8H F 1 ? 212 ? 5I8H   1   ? 212 ? 1   212 
7  4 5I8H G 1 ? 223 ? 5I8H   1   ? 214 ? 1   214 
8  2 5I8H D 1 ? 153 ? Q2N0S6 509 ? 661 ? 512 664 
9  5 5I8H H 1 ? 212 ? 5I8H   1   ? 212 ? 1   212 
10 6 5I8H I 1 ? 235 ? 5I8H   1   ? 214 ? 1   214 
11 3 5I8H J 1 ? 210 ? 5I8H   6   ? 210 ? 6   210 
12 6 5I8H K 1 ? 235 ? 5I8H   1   ? 214 ? 1   214 
# 
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 5I8H ASN A 301 ? UNP Q2N0S6 THR 330 conflict         332 1  
1 5I8H CYS A 469 ? UNP Q2N0S6 ALA 498 conflict         501 2  
1 5I8H ARG A 477 ? UNP Q2N0S6 GLU 506 conflict         509 3  
1 5I8H ARG A 478 ? UNP Q2N0S6 LYS 507 conflict         510 4  
1 5I8H ARG A 480 ? UNP Q2N0S6 ?   ?   'expression tag' 512 5  
1 5I8H ARG A 481 ? UNP Q2N0S6 ?   ?   'expression tag' 513 6  
2 5I8H CYS B 94  ? UNP Q2N0S6 THR 602 conflict         605 7  
3 5I8H ASN C 301 ? UNP Q2N0S6 THR 330 conflict         332 8  
3 5I8H CYS C 469 ? UNP Q2N0S6 ALA 498 conflict         501 9  
3 5I8H ARG C 477 ? UNP Q2N0S6 GLU 506 conflict         509 10 
3 5I8H ARG C 478 ? UNP Q2N0S6 LYS 507 conflict         510 11 
3 5I8H ARG C 480 ? UNP Q2N0S6 ?   ?   'expression tag' 512 12 
3 5I8H ARG C 481 ? UNP Q2N0S6 ?   ?   'expression tag' 513 13 
8 5I8H CYS D 94  ? UNP Q2N0S6 THR 602 conflict         605 14 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE               ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE             ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'        ? 'C4 H7 N O4'     133.103 
BMA D-saccharide        . BETA-D-MANNOSE         ? 'C6 H12 O6'      180.156 
CYS 'L-peptide linking' y CYSTEINE               ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE              ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'        ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE              ? 'C6 H10 N3 O2 1' 156.162 
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 
MAN D-saccharide        . ALPHA-D-MANNOSE        ? 'C6 H12 O6'      180.156 
MET 'L-peptide linking' y METHIONINE             ? 'C5 H11 N O2 S'  149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6'    221.208 
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 
# 
_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                   5I8H 
_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            5.17 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         76.22 
_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_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.5M Sodium Chloride, 0.1M Tris-HCl pH8.5, 5% PEG 8000 and 20% 2-methyl-2, 4- pentanediol' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_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_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MARMOSAIC 300 mm CCD' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2015-03-15 
# 
_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   1 
_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                        'APS BEAMLINE 22-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   22-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.d_resolution_high            4.300 
_reflns.d_resolution_low             50.000 
_reflns.pdbx_number_measured_all     182597 
_reflns.number_obs                   39396 
_reflns.pdbx_Rmerge_I_obs            0.132 
_reflns.pdbx_netI_over_av_sigmaI     9.812 
_reflns.pdbx_netI_over_sigmaI        3.700 
_reflns.pdbx_chi_squared             0.766 
_reflns.pdbx_redundancy              4.600 
_reflns.percent_possible_obs         82.700 
_reflns.pdbx_Rrim_I_all              0.140 
_reflns.pdbx_Rpim_I_all              0.063 
_reflns.B_iso_Wilson_estimate        127.240 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     5I8H 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1  4.300 4.450  ? ? ? 0 0.903 ? ? 0.663 4.200 ? ? ? 2382 ? ? ? ? 50.700 ?     0.435 0.824 
1 2  4.450 4.630  ? ? ? 0 0.809 ? ? 0.696 4.300 ? ? ? 2654 ? ? ? ? 56.100 0.901 0.386 0.878 
1 3  4.630 4.840  ? ? ? 0 0.756 ? ? 0.686 4.300 ? ? ? 3143 ? ? ? ? 66.800 0.840 0.358 0.921 
1 4  4.840 5.100  ? ? ? 0 0.599 ? ? 0.672 4.400 ? ? ? 3773 ? ? ? ? 79.800 0.666 0.284 0.943 
1 5  5.100 5.420  ? ? ? 0 0.625 ? ? 0.676 4.700 ? ? ? 4247 ? ? ? ? 89.800 0.694 0.296 0.946 
1 6  5.420 5.830  ? ? ? 0 0.502 ? ? 0.686 4.900 ? ? ? 4540 ? ? ? ? 95.700 0.557 0.237 0.954 
1 7  5.830 6.420  ? ? ? 0 0.373 ? ? 0.704 4.800 ? ? ? 4654 ? ? ? ? 97.900 0.415 0.177 0.969 
1 8  6.420 7.350  ? ? ? 0 0.214 ? ? 0.758 4.800 ? ? ? 4669 ? ? ? ? 97.900 0.238 0.101 0.987 
1 9  7.350 9.250  ? ? ? 0 0.093 ? ? 0.872 4.800 ? ? ? 4649 ? ? ? ? 96.600 0.104 0.044 0.996 
1 10 9.250 50.000 ? ? ? 0 0.054 ? ? 1.095 4.600 ? ? ? 4685 ? ? ? ? 94.300 0.060 0.026 0.997 
# 
_refine.entry_id                                 5I8H 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            4.3010 
_refine.ls_d_res_low                             48.3430 
_refine.pdbx_ls_sigma_F                          2.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    54.9000 
_refine.ls_number_reflns_obs                     25786 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.ls_matrix_type                           ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.details                                  ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2825 
_refine.ls_R_factor_R_work                       0.2811 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.3090 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.1000 
_refine.ls_number_reflns_R_free                  1315 
_refine.ls_number_reflns_R_work                  24471 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               215.7774 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.7100 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                423.480 
_refine.B_iso_min                                102.560 
_refine.pdbx_overall_phase_error                 43.8700 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       4.3010 
_refine_hist.d_res_low                        48.3430 
_refine_hist.pdbx_number_atoms_ligand         1486 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               23938 
_refine_hist.pdbx_number_residues_total       2915 
_refine_hist.pdbx_B_iso_mean_ligand           231.65 
_refine_hist.pdbx_number_atoms_protein        22452 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' f_bond_d           24611 0.006  ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          33715 1.196  ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     4125  0.067  ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      4109  0.005  ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 14633 12.800 ? ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.pdbx_ens_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.weight_B_iso 
1  'X-RAY DIFFRACTION' 1 1 TORSIONAL A 4884 5.236 ? ? ? ? ? 
2  'X-RAY DIFFRACTION' 1 2 TORSIONAL C 4884 5.236 ? ? ? ? ? 
3  'X-RAY DIFFRACTION' 2 1 TORSIONAL L 1826 5.236 ? ? ? ? ? 
4  'X-RAY DIFFRACTION' 2 2 TORSIONAL J 1826 5.236 ? ? ? ? ? 
5  'X-RAY DIFFRACTION' 3 1 TORSIONAL B 1158 5.236 ? ? ? ? ? 
6  'X-RAY DIFFRACTION' 3 2 TORSIONAL D 1158 5.236 ? ? ? ? ? 
7  'X-RAY DIFFRACTION' 4 1 TORSIONAL G 4117 5.236 ? ? ? ? ? 
8  'X-RAY DIFFRACTION' 4 2 TORSIONAL E 4117 5.236 ? ? ? ? ? 
9  'X-RAY DIFFRACTION' 5 1 TORSIONAL K 2036 5.236 ? ? ? ? ? 
10 'X-RAY DIFFRACTION' 5 2 TORSIONAL I 2036 5.236 ? ? ? ? ? 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.R_factor_obs 
4.3010 4.4731  9 3.0000  164  . 0.3523 0.3529 . 13  . 177  . 'X-RAY DIFFRACTION' . 
4.4731 4.6765  9 10.0000 470  . 0.3218 0.3542 . 33  . 503  . 'X-RAY DIFFRACTION' . 
4.6765 4.9229  9 18.0000 865  . 0.3220 0.3672 . 45  . 910  . 'X-RAY DIFFRACTION' . 
4.9229 5.2309  9 30.0000 1463 . 0.3025 0.3006 . 61  . 1524 . 'X-RAY DIFFRACTION' . 
5.2309 5.6343  9 50.0000 2485 . 0.3185 0.3319 . 132 . 2617 . 'X-RAY DIFFRACTION' . 
5.6343 6.2002  9 92.0000 4580 . 0.3433 0.3602 . 232 . 4812 . 'X-RAY DIFFRACTION' . 
6.2002 7.0950  9 98.0000 4845 . 0.3337 0.3613 . 271 . 5116 . 'X-RAY DIFFRACTION' . 
7.0950 8.9297  9 97.0000 4819 . 0.2824 0.3124 . 273 . 5092 . 'X-RAY DIFFRACTION' . 
8.9297 48.3461 9 93.0000 4780 . 0.2272 0.2601 . 255 . 5035 . 'X-RAY DIFFRACTION' . 
# 
loop_
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.id 
_struct_ncs_dom.details 
1 1 
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
1 2 
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
2 1 'chain L' 
2 2 'chain J' 
3 1 '(chain B and (resseq 512:519 or resseq 521:547 or resseq 569:664))' 
3 2 '(chain D and (resseq 512:519 or resseq 521:547 or resseq 569:664))' 
4 1 'chain G or chain H' 
4 2 'chain E or chain F' 
5 1 'chain K' 
5 2 'chain I' 
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.selection_details 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
1 1 1  ? A 31   A 141  
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 2  ? A 150  A 184  
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 3  ? A 190  A 309  
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 4  ? A 312  A 320  
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 5  ? A 321  A 321  
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 6  ? A 321  A 321  
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 7  ? A 322  A 398  
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 8  ? A 411  A 504  
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 9  ? A 1088 A 1092 
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 10 ? A 1133 A 1133 
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 11 ? A 1137 A 1137 
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 12 ? A 1157 A 1161 
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 13 ? A 1169 A 1169 
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 14 ? A 1197 A 1198 
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 15 ? A 1234 A 1235 
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 16 ? A 1262 A 1265 
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 17 ? A 1268 A 1269 
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 18 ? A 1276 A 1276 
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 19 ? A 1295 A 1296 
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 20 ? A 1301 A 1302 
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 21 ? A 1331 A 1340 
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 22 ? A 1355 A 1355 
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 23 ? A 1363 A 1364 
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 24 ? A 1386 A 1387 
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 1 25 ? A 1392 A 1393 
;(chain A and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 1  ? C 31   C 141  
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 2  ? C 150  C 184  
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 3  ? C 190  C 309  
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 4  ? C 312  C 320  
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 5  ? C 321  C 321  
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 6  ? C 321  C 321  
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 7  ? C 322  C 398  
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 8  ? C 411  C 504  
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 9  ? C 1088 C 1092 
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 10 ? C 1133 C 1133 
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 11 ? C 1137 C 1137 
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 12 ? C 1157 C 1161 
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 13 ? C 1169 C 1169 
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 14 ? C 1197 C 1198 
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 15 ? C 1234 C 1235 
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 16 ? C 1262 C 1265 
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 17 ? C 1268 C 1269 
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 18 ? C 1276 C 1276 
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 19 ? C 1295 C 1296 
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 20 ? C 1301 C 1302 
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 21 ? C 1331 C 1340 
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 22 ? C 1355 C 1355 
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 23 ? C 1363 C 1364 
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 24 ? C 1386 C 1387 
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
1 2 25 ? C 1392 C 1393 
;(chain C and (resseq 31:141 or resseq 150:184 or resseq 190:309 or resseq 312:320 or resid 321 or resid 321A or resseq 322:398 or resseq 411:504 or resseq 1088:1092 or resseq 1133 or resseq 1137 or resseq 1157:1161 or resseq 1169 or resseq 1197:1198 or resseq 1234:1235 or resseq 1262:1265 or resseq 1268:1269 or resseq 1276 or resseq 1295:1296 or resseq 1301:1302 or resseq 1331:1340 or resseq 1355 or resseq 1363:1364 or resseq 1386:1387 or resseq 1392:1393))
;
? ? ? ? ? ? ? ? 
2 1 1  ? L 6    L 210  'chain L' ? ? ? ? ? ? ? ? 
2 2 1  ? J 6    J 210  'chain J' ? ? ? ? ? ? ? ? 
3 1 1  ? B 512  B 519  '(chain B and (resseq 512:519 or resseq 521:547 or resseq 569:664))' ? ? ? ? ? ? ? ? 
3 1 2  ? B 521  B 547  '(chain B and (resseq 512:519 or resseq 521:547 or resseq 569:664))' ? ? ? ? ? ? ? ? 
3 1 3  ? B 569  B 664  '(chain B and (resseq 512:519 or resseq 521:547 or resseq 569:664))' ? ? ? ? ? ? ? ? 
3 2 1  ? D 512  D 519  '(chain D and (resseq 512:519 or resseq 521:547 or resseq 569:664))' ? ? ? ? ? ? ? ? 
3 2 2  ? D 521  D 547  '(chain D and (resseq 512:519 or resseq 521:547 or resseq 569:664))' ? ? ? ? ? ? ? ? 
3 2 3  ? D 569  D 664  '(chain D and (resseq 512:519 or resseq 521:547 or resseq 569:664))' ? ? ? ? ? ? ? ? 
4 1 1  ? G 1    G 214  'chain G or chain H' ? ? ? ? ? ? ? ? 
4 1 2  ? H 1    H 212  'chain G or chain H' ? ? ? ? ? ? ? ? 
4 2 1  ? E 1    E 214  'chain E or chain F' ? ? ? ? ? ? ? ? 
4 2 2  ? F 1    F 212  'chain E or chain F' ? ? ? ? ? ? ? ? 
5 1 1  ? K 1    K 211  'chain K' ? ? ? ? ? ? ? ? 
5 2 1  ? I 1    I 211  'chain I' ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ncs_ens.id 
_struct_ncs_ens.details 
1 ? 
2 ? 
3 ? 
4 ? 
5 ? 
# 
_struct.entry_id                     5I8H 
_struct.title                        
;Crystal Structure of HIV-1 BG505 SOSIP.664 Prefusion Env Trimer in Complex with V3 Loop-targeting Antibody PGT122 Fab and Fusion Peptide-targeting Antibody VRC34.01 Fab
;
_struct.pdbx_descriptor              
;BG505 SOSIP.664 gp120, BG505 SOSIP.664 gp41, PGT122 Fab light chain, VRC34.01 Fab heavy chain, VRC34.01 Fab light chain, PGT122 Fab heavy chain
;
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        5I8H 
_struct_keywords.text            'HIV-1, envelope, trimer, fusion peptide, antibody, neutralizing, IMMUNE SYSTEM' 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
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 1 ? 
D  N N 3 ? 
E  N N 4 ? 
F  N N 5 ? 
G  N N 4 ? 
H  N N 2 ? 
I  N N 5 ? 
J  N N 6 ? 
K  N N 3 ? 
L  N N 6 ? 
M  N N 7 ? 
N  N N 7 ? 
O  N N 8 ? 
P  N N 9 ? 
Q  N N 9 ? 
R  N N 9 ? 
S  N N 9 ? 
T  N N 7 ? 
U  N N 7 ? 
V  N N 7 ? 
W  N N 8 ? 
X  N N 9 ? 
Y  N N 9 ? 
Z  N N 7 ? 
AA N N 7 ? 
BA N N 7 ? 
CA N N 7 ? 
DA N N 7 ? 
EA N N 7 ? 
FA N N 7 ? 
GA N N 7 ? 
HA N N 8 ? 
IA N N 9 ? 
JA N N 9 ? 
KA N N 9 ? 
LA N N 7 ? 
MA N N 7 ? 
NA N N 7 ? 
OA N N 8 ? 
PA N N 7 ? 
QA N N 7 ? 
RA N N 7 ? 
SA N N 7 ? 
TA N N 8 ? 
UA N N 9 ? 
VA N N 9 ? 
WA N N 9 ? 
XA N N 9 ? 
YA N N 9 ? 
ZA N N 9 ? 
AB N N 9 ? 
BB N N 7 ? 
CB N N 7 ? 
DB N N 7 ? 
EB N N 7 ? 
FB N N 7 ? 
GB N N 7 ? 
HB N N 7 ? 
IB N N 7 ? 
JB N N 7 ? 
KB N N 8 ? 
LB N N 7 ? 
MB N N 7 ? 
NB N N 7 ? 
OB N N 7 ? 
PB N N 7 ? 
QB N N 7 ? 
RB N N 8 ? 
SB N N 9 ? 
TB N N 9 ? 
UB N N 9 ? 
VB N N 9 ? 
WB N N 7 ? 
XB N N 7 ? 
YB N N 7 ? 
ZB N N 7 ? 
AC N N 8 ? 
BC N N 9 ? 
CC N N 9 ? 
DC N N 7 ? 
EC N N 7 ? 
FC N N 7 ? 
GC N N 7 ? 
HC N N 7 ? 
IC N N 7 ? 
JC N N 7 ? 
KC N N 7 ? 
LC N N 8 ? 
MC N N 9 ? 
NC N N 9 ? 
OC N N 9 ? 
PC N N 7 ? 
QC N N 7 ? 
RC N N 7 ? 
SC N N 7 ? 
TC N N 7 ? 
UC N N 7 ? 
VC N N 7 ? 
WC N N 8 ? 
XC N N 9 ? 
YC N N 9 ? 
ZC N N 9 ? 
AD N N 9 ? 
BD N N 9 ? 
CD N N 9 ? 
DD N N 9 ? 
ED N N 7 ? 
FD N N 7 ? 
GD N N 7 ? 
HD N N 7 ? 
ID N N 7 ? 
JD N N 7 ? 
KD N N 7 ? 
LD N N 8 ? 
MD N N 7 ? 
ND N N 7 ? 
OD N N 8 ? 
PD N N 7 ? 
QD N N 7 ? 
RD N N 7 ? 
SD N N 7 ? 
TD N N 7 ? 
UD N N 8 ? 
VD N N 9 ? 
WD N N 7 ? 
XD N N 7 ? 
# 
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 LYS A 29  ? GLU A 34  ? LYS A 59  GLU A 64  5 ? 6  
HELX_P HELX_P2  AA2 ASN A 68  ? LYS A 87  ? ASN A 98  LYS A 117 1 ? 20 
HELX_P HELX_P3  AA3 LEU A 92  ? CYS A 96  ? LEU A 122 CYS A 126 5 ? 5  
HELX_P HELX_P4  AA4 LYS A 304 ? ARG A 319 ? LYS A 335 ARG A 350 1 ? 16 
HELX_P HELX_P5  AA5 ASP A 337 ? THR A 341 ? ASP A 368 THR A 372 1 ? 5  
HELX_P HELX_P6  AA6 MET A 443 ? SER A 449 ? MET A 475 SER A 481 1 ? 7  
HELX_P HELX_P7  AA7 LEU B 12  ? GLY B 16  ? LEU B 523 GLY B 527 5 ? 5  
HELX_P HELX_P8  AA8 THR B 18  ? SER B 23  ? THR B 529 SER B 534 1 ? 6  
HELX_P HELX_P9  AA9 THR B 25  ? ALA B 30  ? THR B 536 ALA B 541 1 ? 6  
HELX_P HELX_P10 AB1 ARG B 31  ? LEU B 34  ? ARG B 542 LEU B 545 5 ? 4  
HELX_P HELX_P11 AB2 GLY B 61  ? TRP B 85  ? GLY B 572 TRP B 596 1 ? 25 
HELX_P HELX_P12 AB3 ASN B 107 ? TRP B 112 ? ASN B 618 TRP B 623 1 ? 6  
HELX_P HELX_P13 AB4 THR B 116 ? SER B 125 ? THR B 627 SER B 636 1 ? 10 
HELX_P HELX_P14 AB5 TYR B 127 ? GLU B 137 ? TYR B 638 GLU B 648 1 ? 11 
HELX_P HELX_P15 AB6 GLN B 142 ? ALA B 151 ? GLN B 653 ALA B 662 1 ? 10 
HELX_P HELX_P16 AB7 LYS C 29  ? GLU C 34  ? LYS C 59  GLU C 64  5 ? 6  
HELX_P HELX_P17 AB8 ASN C 68  ? SER C 85  ? ASN C 98  SER C 115 1 ? 18 
HELX_P HELX_P18 AB9 LEU C 92  ? CYS C 96  ? LEU C 122 CYS C 126 5 ? 5  
HELX_P HELX_P19 AC1 THR C 109 ? ARG C 113 ? THR C 139 ARG C 151 5 ? 5  
HELX_P HELX_P20 AC2 LYS C 304 ? ARG C 319 ? LYS C 335 ARG C 350 1 ? 16 
HELX_P HELX_P21 AC3 ASP C 337 ? THR C 342 ? ASP C 368 THR C 373 1 ? 6  
HELX_P HELX_P22 AC4 MET C 443 ? SER C 449 ? MET C 475 SER C 481 1 ? 7  
HELX_P HELX_P23 AC5 GLU D 76  ? GLU D 80  ? GLU L 79  GLU L 83  5 ? 5  
HELX_P HELX_P24 AC6 SER D 122 ? GLN D 127 ? SER L 122 GLN L 127 1 ? 6  
HELX_P HELX_P25 AC7 THR D 182 ? LYS D 187 ? THR L 182 LYS L 187 1 ? 6  
HELX_P HELX_P26 AC8 THR E 28  ? ASN E 32  ? THR E 28  ASN E 32  5 ? 5  
HELX_P HELX_P27 AC9 GLN E 62  ? GLN E 65  ? GLN E 61  GLN E 64  5 ? 4  
HELX_P HELX_P28 AD1 LYS E 74  ? ILE E 76  ? LYS E 73  ILE E 75  5 ? 3  
HELX_P HELX_P29 AD2 THR E 87  ? THR E 91  ? THR E 83  THR E 87  5 ? 5  
HELX_P HELX_P30 AD3 TYR E 101 ? GLU E 105 A TYR E 97  GLU E 100 5 ? 5  
HELX_P HELX_P31 AD4 SER E 165 ? ALA E 167 ? SER E 156 ALA E 158 5 ? 3  
HELX_P HELX_P32 AD5 SER E 196 ? LEU E 198 ? SER E 187 LEU E 189 5 ? 3  
HELX_P HELX_P33 AD6 GLN F 79  ? PHE F 83  ? GLN F 79  PHE F 83  5 ? 5  
HELX_P HELX_P34 AD7 SER F 121 ? SER F 127 ? SER F 121 SER F 127 1 ? 7  
HELX_P HELX_P35 AD8 LYS F 183 ? LYS F 188 ? LYS F 183 LYS F 188 1 ? 6  
HELX_P HELX_P36 AD9 THR G 28  ? ASN G 32  ? THR G 28  ASN G 32  5 ? 5  
HELX_P HELX_P37 AE1 LYS G 74  ? ILE G 76  ? LYS G 73  ILE G 75  5 ? 3  
HELX_P HELX_P38 AE2 THR G 87  ? THR G 91  ? THR G 83  THR G 87  5 ? 5  
HELX_P HELX_P39 AE3 TYR G 101 ? GLU G 105 A TYR G 97  GLU G 100 5 ? 5  
HELX_P HELX_P40 AE4 SER G 165 ? ALA G 167 ? SER G 156 ALA G 158 5 ? 3  
HELX_P HELX_P41 AE5 SER G 196 ? LEU G 198 ? SER G 187 LEU G 189 5 ? 3  
HELX_P HELX_P42 AE6 LEU H 12  ? GLY H 16  ? LEU D 523 GLY D 527 5 ? 5  
HELX_P HELX_P43 AE7 THR H 18  ? SER H 23  ? THR D 529 SER D 534 1 ? 6  
HELX_P HELX_P44 AE8 THR H 25  ? ALA H 30  ? THR D 536 ALA D 541 1 ? 6  
HELX_P HELX_P45 AE9 ARG H 31  ? LEU H 34  ? ARG D 542 LEU D 545 5 ? 4  
HELX_P HELX_P46 AF1 GLY H 61  ? TRP H 85  ? GLY D 572 TRP D 596 1 ? 25 
HELX_P HELX_P47 AF2 ASN H 107 ? TRP H 112 ? ASN D 618 TRP D 623 1 ? 6  
HELX_P HELX_P48 AF3 THR H 116 ? SER H 125 ? THR D 627 SER D 636 1 ? 10 
HELX_P HELX_P49 AF4 TYR H 127 ? GLU H 137 ? TYR D 638 GLU D 648 1 ? 11 
HELX_P HELX_P50 AF5 GLN H 139 ? ALA H 151 ? GLN D 650 ALA D 662 1 ? 13 
HELX_P HELX_P51 AF6 GLN I 79  ? PHE I 83  ? GLN H 79  PHE H 83  5 ? 5  
HELX_P HELX_P52 AF7 SER I 121 ? SER I 127 ? SER H 121 SER H 127 1 ? 7  
HELX_P HELX_P53 AF8 LYS I 183 ? LYS I 188 ? LYS H 183 LYS H 188 1 ? 6  
HELX_P HELX_P54 AF9 PRO J 61  ? LYS J 64  ? PRO I 61  LYS I 64  5 ? 4  
HELX_P HELX_P55 AG1 THR J 86  ? SER J 90  ? THR I 83  SER I 87  5 ? 5  
HELX_P HELX_P56 AG2 SER J 175 ? ALA J 177 ? SER I 154 ALA I 156 5 ? 3  
HELX_P HELX_P57 AG3 LYS J 220 ? ASN J 223 ? LYS I 199 ASN I 202 5 ? 4  
HELX_P HELX_P58 AG4 GLU K 76  ? GLU K 80  ? GLU J 79  GLU J 83  5 ? 5  
HELX_P HELX_P59 AG5 GLU K 125 ? ASN K 129 ? GLU J 125 ASN J 129 5 ? 5  
HELX_P HELX_P60 AG6 THR K 182 ? HIS K 189 ? THR J 182 HIS J 189 1 ? 8  
HELX_P HELX_P61 AG7 PRO L 61  ? LYS L 64  ? PRO K 61  LYS K 64  5 ? 4  
HELX_P HELX_P62 AG8 THR L 86  ? SER L 90  ? THR K 83  SER K 87  5 ? 5  
HELX_P HELX_P63 AG9 SER L 175 ? ALA L 177 ? SER K 154 ALA K 156 5 ? 3  
HELX_P HELX_P64 AH1 LYS L 220 ? ASN L 223 ? LYS K 199 ASN K 202 5 ? 4  
# 
_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 
disulf1   disulf ?    ? A  CYS 24  SG  ? ? ? 1_555 A  CYS 44  SG ? ? A CYS 54  A CYS 74  1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf2   disulf ?    ? A  CYS 89  SG  ? ? ? 1_555 A  CYS 175 SG ? ? A CYS 119 A CYS 205 1_555 ? ? ? ? ? ? ? 2.028 ? 
disulf3   disulf ?    ? A  CYS 96  SG  ? ? ? 1_555 A  CYS 166 SG ? ? A CYS 126 A CYS 196 1_555 ? ? ? ? ? ? ? 2.011 ? 
disulf4   disulf ?    ? A  CYS 101 SG  ? ? ? 1_555 A  CYS 119 SG ? ? A CYS 131 A CYS 157 1_555 ? ? ? ? ? ? ? 2.024 ? 
disulf5   disulf ?    ? A  CYS 188 SG  ? ? ? 1_555 A  CYS 217 SG ? ? A CYS 218 A CYS 247 1_555 ? ? ? ? ? ? ? 2.024 ? 
disulf6   disulf ?    ? A  CYS 198 SG  ? ? ? 1_555 A  CYS 209 SG ? ? A CYS 228 A CYS 239 1_555 ? ? ? ? ? ? ? 2.057 ? 
disulf7   disulf ?    ? A  CYS 266 SG  ? ? ? 1_555 A  CYS 300 SG ? ? A CYS 296 A CYS 331 1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf8   disulf ?    ? A  CYS 347 SG  ? ? ? 1_555 A  CYS 413 SG ? ? A CYS 378 A CYS 445 1_555 ? ? ? ? ? ? ? 2.015 ? 
disulf9   disulf ?    ? A  CYS 354 SG  ? ? ? 1_555 A  CYS 386 SG ? ? A CYS 385 A CYS 418 1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf10  disulf ?    ? A  CYS 469 SG  ? ? ? 1_555 B  CYS 94  SG ? ? A CYS 501 B CYS 605 1_555 ? ? ? ? ? ? ? 2.027 ? 
disulf11  disulf ?    ? B  CYS 87  SG  ? ? ? 1_555 B  CYS 93  SG ? ? B CYS 598 B CYS 604 1_555 ? ? ? ? ? ? ? 2.055 ? 
disulf12  disulf ?    ? C  CYS 24  SG  ? ? ? 1_555 C  CYS 44  SG ? ? C CYS 54  C CYS 74  1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf13  disulf ?    ? C  CYS 89  SG  ? ? ? 1_555 C  CYS 175 SG ? ? C CYS 119 C CYS 205 1_555 ? ? ? ? ? ? ? 2.029 ? 
disulf14  disulf ?    ? C  CYS 96  SG  ? ? ? 1_555 C  CYS 166 SG ? ? C CYS 126 C CYS 196 1_555 ? ? ? ? ? ? ? 2.011 ? 
disulf15  disulf ?    ? C  CYS 101 SG  ? ? ? 1_555 C  CYS 119 SG ? ? C CYS 131 C CYS 157 1_555 ? ? ? ? ? ? ? 2.029 ? 
disulf16  disulf ?    ? C  CYS 188 SG  ? ? ? 1_555 C  CYS 217 SG ? ? C CYS 218 C CYS 247 1_555 ? ? ? ? ? ? ? 2.029 ? 
disulf17  disulf ?    ? C  CYS 198 SG  ? ? ? 1_555 C  CYS 209 SG ? ? C CYS 228 C CYS 239 1_555 ? ? ? ? ? ? ? 2.048 ? 
disulf18  disulf ?    ? C  CYS 266 SG  ? ? ? 1_555 C  CYS 300 SG ? ? C CYS 296 C CYS 331 1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf19  disulf ?    ? C  CYS 347 SG  ? ? ? 1_555 C  CYS 413 SG ? ? C CYS 378 C CYS 445 1_555 ? ? ? ? ? ? ? 2.015 ? 
disulf20  disulf ?    ? C  CYS 354 SG  ? ? ? 1_555 C  CYS 386 SG ? ? C CYS 385 C CYS 418 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf21  disulf ?    ? C  CYS 469 SG  ? ? ? 1_555 H  CYS 94  SG ? ? C CYS 501 D CYS 605 1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf22  disulf ?    ? D  CYS 17  SG  ? ? ? 1_555 D  CYS 85  SG ? ? L CYS 23  L CYS 88  1_555 ? ? ? ? ? ? ? 2.017 ? 
disulf23  disulf ?    ? D  CYS 135 SG  ? ? ? 1_555 D  CYS 194 SG ? ? L CYS 135 L CYS 194 1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf24  disulf ?    ? E  CYS 22  SG  ? ? ? 1_555 E  CYS 96  SG ? ? E CYS 22  E CYS 92  1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf25  disulf ?    ? E  CYS 149 SG  ? ? ? 1_555 E  CYS 205 SG ? ? E CYS 140 E CYS 196 1_555 ? ? ? ? ? ? ? 2.034 ? 
disulf26  disulf ?    ? F  CYS 23  SG  ? ? ? 1_555 F  CYS 88  SG ? ? F CYS 23  F CYS 88  1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf27  disulf ?    ? F  CYS 134 SG  ? ? ? 1_555 F  CYS 194 SG ? ? F CYS 134 F CYS 194 1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf28  disulf ?    ? G  CYS 22  SG  ? ? ? 1_555 G  CYS 96  SG ? ? G CYS 22  G CYS 92  1_555 ? ? ? ? ? ? ? 2.034 ? 
disulf29  disulf ?    ? G  CYS 149 SG  ? ? ? 1_555 G  CYS 205 SG ? ? G CYS 140 G CYS 196 1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf30  disulf ?    ? H  CYS 87  SG  ? ? ? 1_555 H  CYS 93  SG ? ? D CYS 598 D CYS 604 1_555 ? ? ? ? ? ? ? 2.057 ? 
disulf31  disulf ?    ? I  CYS 23  SG  ? ? ? 1_555 I  CYS 88  SG ? ? H CYS 23  H CYS 88  1_555 ? ? ? ? ? ? ? 2.042 ? 
disulf32  disulf ?    ? I  CYS 134 SG  ? ? ? 1_555 I  CYS 194 SG ? ? H CYS 134 H CYS 194 1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf33  disulf ?    ? J  CYS 22  SG  ? ? ? 1_555 J  CYS 95  SG ? ? I CYS 22  I CYS 92  1_555 ? ? ? ? ? ? ? 2.033 ? 
disulf34  disulf ?    ? J  CYS 159 SG  ? ? ? 1_555 J  CYS 215 SG ? ? I CYS 138 I CYS 194 1_555 ? ? ? ? ? ? ? 2.048 ? 
disulf35  disulf ?    ? K  CYS 17  SG  ? ? ? 1_555 K  CYS 85  SG ? ? J CYS 23  J CYS 88  1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf36  disulf ?    ? K  CYS 135 SG  ? ? ? 1_555 K  CYS 194 SG ? ? J CYS 135 J CYS 194 1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf37  disulf ?    ? L  CYS 22  SG  ? ? ? 1_555 L  CYS 95  SG ? ? K CYS 22  K CYS 92  1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf38  disulf ?    ? L  CYS 159 SG  ? ? ? 1_555 L  CYS 215 SG ? ? K CYS 138 K CYS 194 1_555 ? ? ? ? ? ? ? 2.055 ? 
covale1   covale one  ? A  ASN 58  ND2 ? ? ? 1_555 M  NAG .   C1 ? ? A ASN 88  A NAG 901 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale2   covale one  ? A  ASN 103 ND2 ? ? ? 1_555 T  NAG .   C1 ? ? A ASN 133 A NAG 908 1_555 ? ? ? ? ? ? ? 1.448 ? 
covale3   covale one  ? A  ASN 107 ND2 ? ? ? 1_555 SD NAG .   C1 ? ? A ASN 137 I NAG 301 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale4   covale one  ? A  ASN 118 ND2 ? ? ? 1_555 U  NAG .   C1 ? ? A ASN 156 A NAG 909 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale5   covale one  ? A  ASN 122 ND2 ? ? ? 1_555 Z  NAG .   C1 ? ? A ASN 160 A NAG 914 1_555 ? ? ? ? ? ? ? 1.433 ? 
covale6   covale one  ? A  ASN 167 ND2 ? ? ? 1_555 BA NAG .   C1 ? ? A ASN 197 A NAG 916 1_555 ? ? ? ? ? ? ? 1.445 ? 
covale7   covale one  ? A  ASN 204 ND2 ? ? ? 1_555 DA NAG .   C1 ? ? A ASN 234 A NAG 918 1_555 ? ? ? ? ? ? ? 1.440 ? 
covale8   covale one  ? A  ASN 246 ND2 ? ? ? 1_555 LA NAG .   C1 ? ? A ASN 276 A NAG 926 1_555 ? ? ? ? ? ? ? 1.438 ? 
covale9   covale one  ? A  ASN 265 ND2 ? ? ? 1_555 MA NAG .   C1 ? ? A ASN 295 A NAG 927 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale10  covale one  ? A  ASN 271 ND2 ? ? ? 1_555 PA NAG .   C1 ? ? A ASN 301 A NAG 930 1_555 ? ? ? ? ? ? ? 1.455 ? 
covale11  covale one  ? A  ASN 301 ND2 ? ? ? 1_555 RA NAG .   C1 ? ? A ASN 332 A NAG 932 1_555 ? ? ? ? ? ? ? 1.423 ? 
covale12  covale one  ? A  ASN 308 ND2 ? ? ? 1_555 LB NAG .   C1 ? ? A ASN 339 A NAG 952 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale13  covale one  ? A  ASN 324 ND2 ? ? ? 1_555 BB NAG .   C1 ? ? A ASN 355 A NAG 942 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale14  covale one  ? A  ASN 355 ND2 ? ? ? 1_555 EB NAG .   C1 ? ? A ASN 386 A NAG 945 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale15  covale one  ? A  ASN 361 ND2 ? ? ? 1_555 GB NAG .   C1 ? ? A ASN 392 A NAG 947 1_555 ? ? ? ? ? ? ? 1.440 ? 
covale16  covale one  ? A  ASN 416 ND2 ? ? ? 1_555 IB NAG .   C1 ? ? A ASN 448 A NAG 949 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale17  covale one  ? B  ASN 100 ND2 ? ? ? 1_555 MB NAG .   C1 ? ? B ASN 611 B NAG 901 1_555 ? ? ? ? ? ? ? 1.445 ? 
covale18  covale one  ? B  ASN 107 ND2 ? ? ? 1_555 NB NAG .   C1 ? ? B ASN 618 B NAG 902 1_555 ? ? ? ? ? ? ? 1.434 ? 
covale19  covale one  ? B  ASN 126 ND2 ? ? ? 1_555 OB NAG .   C1 ? ? B ASN 637 B NAG 903 1_555 ? ? ? ? ? ? ? 1.426 ? 
covale20  covale one  ? C  ASN 58  ND2 ? ? ? 1_555 PB NAG .   C1 ? ? C ASN 88  C NAG 901 1_555 ? ? ? ? ? ? ? 1.449 ? 
covale21  covale one  ? C  ASN 103 ND2 ? ? ? 1_555 WB NAG .   C1 ? ? C ASN 133 C NAG 908 1_555 ? ? ? ? ? ? ? 1.436 ? 
covale22  covale one  ? C  ASN 107 ND2 ? ? ? 1_555 XB NAG .   C1 ? ? C ASN 137 C NAG 909 1_555 ? ? ? ? ? ? ? 1.436 ? 
covale23  covale one  ? C  ASN 118 ND2 ? ? ? 1_555 YB NAG .   C1 ? ? C ASN 156 C NAG 910 1_555 ? ? ? ? ? ? ? 1.445 ? 
covale24  covale one  ? C  ASN 122 ND2 ? ? ? 1_555 DC NAG .   C1 ? ? C ASN 160 C NAG 915 1_555 ? ? ? ? ? ? ? 1.436 ? 
covale25  covale one  ? C  ASN 167 ND2 ? ? ? 1_555 FC NAG .   C1 ? ? C ASN 197 C NAG 917 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale26  covale one  ? C  ASN 204 ND2 ? ? ? 1_555 HC NAG .   C1 ? ? C ASN 234 C NAG 919 1_555 ? ? ? ? ? ? ? 1.444 ? 
covale27  covale one  ? C  ASN 232 ND2 ? ? ? 1_555 JC NAG .   C1 ? ? C ASN 262 C NAG 921 1_555 ? ? ? ? ? ? ? 1.477 ? 
covale28  covale one  ? C  ASN 246 ND2 ? ? ? 1_555 PC NAG .   C1 ? ? C ASN 276 C NAG 927 1_555 ? ? ? ? ? ? ? 1.438 ? 
covale29  covale one  ? C  ASN 265 ND2 ? ? ? 1_555 QC NAG .   C1 ? ? C ASN 295 C NAG 928 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale30  covale one  ? C  ASN 271 ND2 ? ? ? 1_555 SC NAG .   C1 ? ? C ASN 301 C NAG 930 1_555 ? ? ? ? ? ? ? 1.455 ? 
covale31  covale one  ? C  ASN 301 ND2 ? ? ? 1_555 UC NAG .   C1 ? ? C ASN 332 C NAG 932 1_555 ? ? ? ? ? ? ? 1.431 ? 
covale32  covale one  ? C  ASN 308 ND2 ? ? ? 1_555 PD NAG .   C1 ? ? C ASN 339 C NAG 953 1_555 ? ? ? ? ? ? ? 1.440 ? 
covale33  covale one  ? C  ASN 324 ND2 ? ? ? 1_555 ED NAG .   C1 ? ? C ASN 355 C NAG 942 1_555 ? ? ? ? ? ? ? 1.459 ? 
covale34  covale one  ? C  ASN 332 ND2 ? ? ? 1_555 FD NAG .   C1 ? ? C ASN 363 C NAG 943 1_555 ? ? ? ? ? ? ? 1.454 ? 
covale35  covale one  ? C  ASN 355 ND2 ? ? ? 1_555 HD NAG .   C1 ? ? C ASN 386 C NAG 945 1_555 ? ? ? ? ? ? ? 1.447 ? 
covale36  covale one  ? C  ASN 361 ND2 ? ? ? 1_555 JD NAG .   C1 ? ? C ASN 392 C NAG 947 1_555 ? ? ? ? ? ? ? 1.427 ? 
covale37  covale one  ? C  ASN 416 ND2 ? ? ? 1_555 MD NAG .   C1 ? ? C ASN 448 C NAG 950 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale38  covale one  ? H  ASN 100 ND2 ? ? ? 1_555 QD NAG .   C1 ? ? D ASN 611 D NAG 901 1_555 ? ? ? ? ? ? ? 1.450 ? 
covale39  covale one  ? H  ASN 126 ND2 ? ? ? 1_555 RD NAG .   C1 ? ? D ASN 637 D NAG 902 1_555 ? ? ? ? ? ? ? 1.426 ? 
covale40  covale one  ? J  ASN 23  ND2 ? ? ? 1_555 WD NAG .   C1 ? ? I ASN 23  I NAG 305 1_555 ? ? ? ? ? ? ? 1.462 ? 
covale41  covale none ? J  ARG 102 NH2 ? ? ? 1_555 VD MAN .   C4 ? ? I ARG 99  I MAN 304 1_555 ? ? ? ? ? ? ? 1.435 ? 
covale42  covale one  ? L  ASN 23  ND2 ? ? ? 1_555 XD NAG .   C1 ? ? K ASN 23  K NAG 301 1_555 ? ? ? ? ? ? ? 1.454 ? 
covale43  covale both ? M  NAG .   O4  ? ? ? 1_555 N  NAG .   C1 ? ? A NAG 901 A NAG 902 1_555 ? ? ? ? ? ? ? 1.440 ? 
covale44  covale both ? N  NAG .   O4  ? ? ? 1_555 O  BMA .   C1 ? ? A NAG 902 A BMA 903 1_555 ? ? ? ? ? ? ? 1.425 ? 
covale45  covale one  ? O  BMA .   O3  ? ? ? 1_555 P  MAN .   C1 ? ? A BMA 903 A MAN 904 1_555 ? ? ? ? ? ? ? 1.431 ? 
covale46  covale one  ? O  BMA .   O6  ? ? ? 1_555 Q  MAN .   C1 ? ? A BMA 903 A MAN 905 1_555 ? ? ? ? ? ? ? 1.434 ? 
covale47  covale one  ? Q  MAN .   O3  ? ? ? 1_555 S  MAN .   C1 ? ? A MAN 905 A MAN 907 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale48  covale one  ? Q  MAN .   O6  ? ? ? 1_555 R  MAN .   C1 ? ? A MAN 905 A MAN 906 1_555 ? ? ? ? ? ? ? 1.452 ? 
covale49  covale both ? U  NAG .   O4  ? ? ? 1_555 V  NAG .   C1 ? ? A NAG 909 A NAG 910 1_555 ? ? ? ? ? ? ? 1.447 ? 
covale50  covale both ? V  NAG .   O4  ? ? ? 1_555 W  BMA .   C1 ? ? A NAG 910 A BMA 911 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale51  covale one  ? W  BMA .   O3  ? ? ? 1_555 X  MAN .   C1 ? ? A BMA 911 A MAN 912 1_555 ? ? ? ? ? ? ? 1.449 ? 
covale52  covale one  ? W  BMA .   O6  ? ? ? 1_555 Y  MAN .   C1 ? ? A BMA 911 A MAN 913 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale53  covale both ? Z  NAG .   O4  ? ? ? 1_555 AA NAG .   C1 ? ? A NAG 914 A NAG 915 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale54  covale both ? BA NAG .   O4  ? ? ? 1_555 CA NAG .   C1 ? ? A NAG 916 A NAG 917 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale55  covale both ? DA NAG .   O4  ? ? ? 1_555 EA NAG .   C1 ? ? A NAG 918 A NAG 919 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale56  covale both ? FA NAG .   O4  ? ? ? 1_555 GA NAG .   C1 ? ? A NAG 920 A NAG 921 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale57  covale both ? GA NAG .   O4  ? ? ? 1_555 HA BMA .   C1 ? ? A NAG 921 A BMA 922 1_555 ? ? ? ? ? ? ? 1.436 ? 
covale58  covale one  ? HA BMA .   O3  ? ? ? 1_555 JA MAN .   C1 ? ? A BMA 922 A MAN 924 1_555 ? ? ? ? ? ? ? 1.450 ? 
covale59  covale one  ? HA BMA .   O6  ? ? ? 1_555 IA MAN .   C1 ? ? A BMA 922 A MAN 923 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale60  covale one  ? JA MAN .   O2  ? ? ? 1_555 KA MAN .   C1 ? ? A MAN 924 A MAN 925 1_555 ? ? ? ? ? ? ? 1.447 ? 
covale61  covale both ? MA NAG .   O4  ? ? ? 1_555 NA NAG .   C1 ? ? A NAG 927 A NAG 928 1_555 ? ? ? ? ? ? ? 1.451 ? 
covale62  covale both ? NA NAG .   O4  ? ? ? 1_555 OA BMA .   C1 ? ? A NAG 928 A BMA 929 1_555 ? ? ? ? ? ? ? 1.465 ? 
covale63  covale both ? PA NAG .   O4  ? ? ? 1_555 QA NAG .   C1 ? ? A NAG 930 A NAG 931 1_555 ? ? ? ? ? ? ? 1.445 ? 
covale64  covale both ? RA NAG .   O4  ? ? ? 1_555 SA NAG .   C1 ? ? A NAG 932 A NAG 933 1_555 ? ? ? ? ? ? ? 1.436 ? 
covale65  covale both ? SA NAG .   O4  ? ? ? 1_555 TA BMA .   C1 ? ? A NAG 933 A BMA 934 1_555 ? ? ? ? ? ? ? 1.433 ? 
covale66  covale one  ? TA BMA .   O3  ? ? ? 1_555 XA MAN .   C1 ? ? A BMA 934 A MAN 938 1_555 ? ? ? ? ? ? ? 1.447 ? 
covale67  covale one  ? TA BMA .   O6  ? ? ? 1_555 UA MAN .   C1 ? ? A BMA 934 A MAN 935 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale68  covale one  ? UA MAN .   O3  ? ? ? 1_555 WA MAN .   C1 ? ? A MAN 935 A MAN 937 1_555 ? ? ? ? ? ? ? 1.445 ? 
covale69  covale one  ? UA MAN .   O6  ? ? ? 1_555 VA MAN .   C1 ? ? A MAN 935 A MAN 936 1_555 ? ? ? ? ? ? ? 1.447 ? 
covale70  covale one  ? WA MAN .   O2  ? ? ? 1_555 AB MAN .   C1 ? ? A MAN 937 A MAN 941 1_555 ? ? ? ? ? ? ? 1.450 ? 
covale71  covale one  ? XA MAN .   O2  ? ? ? 1_555 YA MAN .   C1 ? ? A MAN 938 A MAN 939 1_555 ? ? ? ? ? ? ? 1.447 ? 
covale72  covale one  ? YA MAN .   O2  ? ? ? 1_555 ZA MAN .   C1 ? ? A MAN 939 A MAN 940 1_555 ? ? ? ? ? ? ? 1.450 ? 
covale73  covale both ? CB NAG .   O4  ? ? ? 1_555 DB NAG .   C1 ? ? A NAG 943 A NAG 944 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale74  covale both ? EB NAG .   O4  ? ? ? 1_555 FB NAG .   C1 ? ? A NAG 945 A NAG 946 1_555 ? ? ? ? ? ? ? 1.450 ? 
covale75  covale both ? GB NAG .   O4  ? ? ? 1_555 HB NAG .   C1 ? ? A NAG 947 A NAG 948 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale76  covale both ? IB NAG .   O4  ? ? ? 1_555 JB NAG .   C1 ? ? A NAG 949 A NAG 950 1_555 ? ? ? ? ? ? ? 1.444 ? 
covale77  covale both ? JB NAG .   O4  ? ? ? 1_555 KB BMA .   C1 ? ? A NAG 950 A BMA 951 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale78  covale both ? PB NAG .   O4  ? ? ? 1_555 QB NAG .   C1 ? ? C NAG 901 C NAG 902 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale79  covale both ? QB NAG .   O4  ? ? ? 1_555 RB BMA .   C1 ? ? C NAG 902 C BMA 903 1_555 ? ? ? ? ? ? ? 1.402 ? 
covale80  covale one  ? RB BMA .   O3  ? ? ? 1_555 SB MAN .   C1 ? ? C BMA 903 C MAN 904 1_555 ? ? ? ? ? ? ? 1.414 ? 
covale81  covale one  ? RB BMA .   O6  ? ? ? 1_555 TB MAN .   C1 ? ? C BMA 903 C MAN 905 1_555 ? ? ? ? ? ? ? 1.448 ? 
covale82  covale one  ? TB MAN .   O3  ? ? ? 1_555 VB MAN .   C1 ? ? C MAN 905 C MAN 907 1_555 ? ? ? ? ? ? ? 1.469 ? 
covale83  covale one  ? TB MAN .   O6  ? ? ? 1_555 UB MAN .   C1 ? ? C MAN 905 C MAN 906 1_555 ? ? ? ? ? ? ? 1.467 ? 
covale84  covale both ? YB NAG .   O4  ? ? ? 1_555 ZB NAG .   C1 ? ? C NAG 910 C NAG 911 1_555 ? ? ? ? ? ? ? 1.447 ? 
covale85  covale both ? ZB NAG .   O4  ? ? ? 1_555 AC BMA .   C1 ? ? C NAG 911 C BMA 912 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale86  covale one  ? AC BMA .   O3  ? ? ? 1_555 BC MAN .   C1 ? ? C BMA 912 C MAN 913 1_555 ? ? ? ? ? ? ? 1.449 ? 
covale87  covale one  ? AC BMA .   O6  ? ? ? 1_555 CC MAN .   C1 ? ? C BMA 912 C MAN 914 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale88  covale both ? DC NAG .   O4  ? ? ? 1_555 EC NAG .   C1 ? ? C NAG 915 C NAG 916 1_555 ? ? ? ? ? ? ? 1.445 ? 
covale89  covale both ? FC NAG .   O4  ? ? ? 1_555 GC NAG .   C1 ? ? C NAG 917 C NAG 918 1_555 ? ? ? ? ? ? ? 1.440 ? 
covale90  covale both ? HC NAG .   O4  ? ? ? 1_555 IC NAG .   C1 ? ? C NAG 919 C NAG 920 1_555 ? ? ? ? ? ? ? 1.445 ? 
covale91  covale both ? JC NAG .   O4  ? ? ? 1_555 KC NAG .   C1 ? ? C NAG 921 C NAG 922 1_555 ? ? ? ? ? ? ? 1.451 ? 
covale92  covale both ? KC NAG .   O4  ? ? ? 1_555 LC BMA .   C1 ? ? C NAG 922 C BMA 923 1_555 ? ? ? ? ? ? ? 1.447 ? 
covale93  covale one  ? LC BMA .   O3  ? ? ? 1_555 NC MAN .   C1 ? ? C BMA 923 C MAN 925 1_555 ? ? ? ? ? ? ? 1.450 ? 
covale94  covale one  ? LC BMA .   O6  ? ? ? 1_555 MC MAN .   C1 ? ? C BMA 923 C MAN 924 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale95  covale one  ? NC MAN .   O2  ? ? ? 1_555 OC MAN .   C1 ? ? C MAN 925 C MAN 926 1_555 ? ? ? ? ? ? ? 1.450 ? 
covale96  covale both ? QC NAG .   O4  ? ? ? 1_555 RC NAG .   C1 ? ? C NAG 928 C NAG 929 1_555 ? ? ? ? ? ? ? 1.448 ? 
covale97  covale both ? SC NAG .   O4  ? ? ? 1_555 TC NAG .   C1 ? ? C NAG 930 C NAG 931 1_555 ? ? ? ? ? ? ? 1.445 ? 
covale98  covale both ? UC NAG .   O4  ? ? ? 1_555 VC NAG .   C1 ? ? C NAG 932 C NAG 933 1_555 ? ? ? ? ? ? ? 1.440 ? 
covale99  covale both ? VC NAG .   O4  ? ? ? 1_555 WC BMA .   C1 ? ? C NAG 933 C BMA 934 1_555 ? ? ? ? ? ? ? 1.437 ? 
covale100 covale one  ? WC BMA .   O3  ? ? ? 1_555 AD MAN .   C1 ? ? C BMA 934 C MAN 938 1_555 ? ? ? ? ? ? ? 1.444 ? 
covale101 covale one  ? WC BMA .   O6  ? ? ? 1_555 XC MAN .   C1 ? ? C BMA 934 C MAN 935 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale102 covale one  ? XC MAN .   O3  ? ? ? 1_555 ZC MAN .   C1 ? ? C MAN 935 C MAN 937 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale103 covale one  ? XC MAN .   O6  ? ? ? 1_555 YC MAN .   C1 ? ? C MAN 935 C MAN 936 1_555 ? ? ? ? ? ? ? 1.448 ? 
covale104 covale one  ? ZC MAN .   O2  ? ? ? 1_555 DD MAN .   C1 ? ? C MAN 937 C MAN 941 1_555 ? ? ? ? ? ? ? 1.448 ? 
covale105 covale one  ? AD MAN .   O2  ? ? ? 1_555 BD MAN .   C1 ? ? C MAN 938 C MAN 939 1_555 ? ? ? ? ? ? ? 1.452 ? 
covale106 covale one  ? BD MAN .   O2  ? ? ? 1_555 CD MAN .   C1 ? ? C MAN 939 C MAN 940 1_555 ? ? ? ? ? ? ? 1.452 ? 
covale107 covale both ? FD NAG .   O4  ? ? ? 1_555 GD NAG .   C1 ? ? C NAG 943 C NAG 944 1_555 ? ? ? ? ? ? ? 1.445 ? 
covale108 covale both ? HD NAG .   O4  ? ? ? 1_555 ID NAG .   C1 ? ? C NAG 945 C NAG 946 1_555 ? ? ? ? ? ? ? 1.448 ? 
covale109 covale both ? JD NAG .   O4  ? ? ? 1_555 KD NAG .   C1 ? ? C NAG 947 C NAG 948 1_555 ? ? ? ? ? ? ? 1.436 ? 
covale110 covale both ? KD NAG .   O4  ? ? ? 1_555 LD BMA .   C1 ? ? C NAG 948 C BMA 949 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale111 covale both ? MD NAG .   O4  ? ? ? 1_555 ND NAG .   C1 ? ? C NAG 950 C NAG 951 1_555 ? ? ? ? ? ? ? 1.453 ? 
covale112 covale both ? ND NAG .   O4  ? ? ? 1_555 OD BMA .   C1 ? ? C NAG 951 C BMA 952 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale113 covale both ? SD NAG .   O4  ? ? ? 1_555 TD NAG .   C1 ? ? I NAG 301 I NAG 302 1_555 ? ? ? ? ? ? ? 1.450 ? 
covale114 covale both ? TD NAG .   O4  ? ? ? 1_555 UD BMA .   C1 ? ? I NAG 302 I BMA 303 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale115 covale one  ? UD BMA .   O3  ? ? ? 1_555 VD MAN .   C1 ? ? I BMA 303 I MAN 304 1_555 ? ? ? ? ? ? ? 1.455 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
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  ILE 108 A . ? ILE 138 A THR 109 A ? THR 139 A 1 -5.12  
2  GLY 280 A . ? GLY 312 A PRO 281 A ? PRO 313 A 1 -0.48  
3  SER 428 A . ? SER 460 A THR 429 A ? THR 461 A 1 -3.87  
4  ILE 108 C . ? ILE 138 C THR 109 C ? THR 139 C 1 -5.72  
5  GLY 280 C . ? GLY 312 C PRO 281 C ? PRO 313 C 1 -0.63  
6  SER 428 C . ? SER 460 C THR 429 C ? THR 461 C 1 -4.38  
7  GLN 109 D . ? GLN 109 L PRO 110 D ? PRO 110 L 1 -9.81  
8  TYR 141 D . ? TYR 141 L PRO 142 D ? PRO 142 L 1 -0.90  
9  PHE 155 E . ? PHE 146 E PRO 156 E ? PRO 147 E 1 -11.73 
10 GLU 157 E . ? GLU 148 E PRO 158 E ? PRO 149 E 1 -9.31  
11 SER 7   F . ? SER 7   F PRO 8   F ? PRO 8   F 1 -7.08  
12 TYR 94  F . ? TYR 94  F PRO 95  F ? PRO 95  F 1 -5.65  
13 TYR 140 F . ? TYR 140 F PRO 141 F ? PRO 141 F 1 -1.16  
14 PHE 155 G . ? PHE 146 G PRO 156 G ? PRO 147 G 1 -10.72 
15 GLU 157 G . ? GLU 148 G PRO 158 G ? PRO 149 G 1 -6.93  
16 SER 7   I . ? SER 7   H PRO 8   I ? PRO 8   H 1 -6.01  
17 TYR 94  I . ? TYR 94  H PRO 95  I ? PRO 95  H 1 -6.30  
18 TYR 140 I . ? TYR 140 H PRO 141 I ? PRO 141 H 1 -0.15  
19 PHE 165 J . ? PHE 144 I PRO 166 J ? PRO 145 I 1 -3.61  
20 GLU 167 J . ? GLU 146 I PRO 168 J ? PRO 147 I 1 -3.20  
21 GLY 209 J . ? GLY 188 I THR 210 J ? THR 189 I 1 4.72   
22 GLN 109 K . ? GLN 109 J PRO 110 K ? PRO 110 J 1 -10.72 
23 TYR 141 K . ? TYR 141 J PRO 142 K ? PRO 142 J 1 -1.31  
24 PHE 165 L . ? PHE 144 K PRO 166 L ? PRO 145 K 1 -2.74  
25 GLU 167 L . ? GLU 146 K PRO 168 L ? PRO 147 K 1 -3.50  
26 GLY 209 L . ? GLY 188 K THR 210 L ? THR 189 K 1 4.61   
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 2 ? 
AA6 ? 3 ? 
AA7 ? 7 ? 
AA8 ? 6 ? 
AA9 ? 2 ? 
AB1 ? 3 ? 
AB2 ? 5 ? 
AB3 ? 2 ? 
AB4 ? 2 ? 
AB5 ? 2 ? 
AB6 ? 3 ? 
AB7 ? 7 ? 
AB8 ? 6 ? 
AB9 ? 2 ? 
AC1 ? 5 ? 
AC2 ? 3 ? 
AC3 ? 4 ? 
AC4 ? 4 ? 
AC5 ? 4 ? 
AC6 ? 6 ? 
AC7 ? 4 ? 
AC8 ? 4 ? 
AC9 ? 4 ? 
AD1 ? 3 ? 
AD2 ? 4 ? 
AD3 ? 6 ? 
AD4 ? 4 ? 
AD5 ? 4 ? 
AD6 ? 4 ? 
AD7 ? 4 ? 
AD8 ? 6 ? 
AD9 ? 4 ? 
AE1 ? 4 ? 
AE2 ? 4 ? 
AE3 ? 3 ? 
AE4 ? 4 ? 
AE5 ? 6 ? 
AE6 ? 4 ? 
AE7 ? 4 ? 
AE8 ? 4 ? 
AE9 ? 4 ? 
AF1 ? 6 ? 
AF2 ? 4 ? 
AF3 ? 4 ? 
AF4 ? 3 ? 
AF5 ? 5 ? 
AF6 ? 3 ? 
AF7 ? 4 ? 
AF8 ? 4 ? 
AF9 ? 4 ? 
AG1 ? 6 ? 
AG2 ? 4 ? 
AG3 ? 4 ? 
AG4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA7 6 7 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? parallel      
AA8 5 6 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB2 4 5 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB6 1 2 ? parallel      
AB6 2 3 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB7 4 5 ? anti-parallel 
AB7 5 6 ? anti-parallel 
AB7 6 7 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB8 4 5 ? parallel      
AB8 5 6 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AC1 1 2 ? parallel      
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC1 4 5 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC3 2 3 ? anti-parallel 
AC3 3 4 ? anti-parallel 
AC4 1 2 ? anti-parallel 
AC4 2 3 ? anti-parallel 
AC4 3 4 ? anti-parallel 
AC5 1 2 ? anti-parallel 
AC5 2 3 ? anti-parallel 
AC5 3 4 ? anti-parallel 
AC6 1 2 ? parallel      
AC6 2 3 ? anti-parallel 
AC6 3 4 ? anti-parallel 
AC6 4 5 ? anti-parallel 
AC6 5 6 ? anti-parallel 
AC7 1 2 ? parallel      
AC7 2 3 ? anti-parallel 
AC7 3 4 ? anti-parallel 
AC8 1 2 ? anti-parallel 
AC8 2 3 ? anti-parallel 
AC8 3 4 ? anti-parallel 
AC9 1 2 ? anti-parallel 
AC9 2 3 ? anti-parallel 
AC9 3 4 ? anti-parallel 
AD1 1 2 ? anti-parallel 
AD1 2 3 ? anti-parallel 
AD2 1 2 ? anti-parallel 
AD2 2 3 ? anti-parallel 
AD2 3 4 ? anti-parallel 
AD3 1 2 ? parallel      
AD3 2 3 ? anti-parallel 
AD3 3 4 ? anti-parallel 
AD3 4 5 ? anti-parallel 
AD3 5 6 ? anti-parallel 
AD4 1 2 ? parallel      
AD4 2 3 ? anti-parallel 
AD4 3 4 ? anti-parallel 
AD5 1 2 ? anti-parallel 
AD5 2 3 ? anti-parallel 
AD5 3 4 ? anti-parallel 
AD6 1 2 ? anti-parallel 
AD6 2 3 ? anti-parallel 
AD6 3 4 ? anti-parallel 
AD7 1 2 ? anti-parallel 
AD7 2 3 ? anti-parallel 
AD7 3 4 ? anti-parallel 
AD8 1 2 ? parallel      
AD8 2 3 ? anti-parallel 
AD8 3 4 ? anti-parallel 
AD8 4 5 ? anti-parallel 
AD8 5 6 ? anti-parallel 
AD9 1 2 ? parallel      
AD9 2 3 ? anti-parallel 
AD9 3 4 ? anti-parallel 
AE1 1 2 ? anti-parallel 
AE1 2 3 ? anti-parallel 
AE1 3 4 ? anti-parallel 
AE2 1 2 ? anti-parallel 
AE2 2 3 ? anti-parallel 
AE2 3 4 ? anti-parallel 
AE3 1 2 ? anti-parallel 
AE3 2 3 ? anti-parallel 
AE4 1 2 ? anti-parallel 
AE4 2 3 ? anti-parallel 
AE4 3 4 ? anti-parallel 
AE5 1 2 ? parallel      
AE5 2 3 ? anti-parallel 
AE5 3 4 ? anti-parallel 
AE5 4 5 ? anti-parallel 
AE5 5 6 ? anti-parallel 
AE6 1 2 ? parallel      
AE6 2 3 ? anti-parallel 
AE6 3 4 ? anti-parallel 
AE7 1 2 ? anti-parallel 
AE7 2 3 ? anti-parallel 
AE7 3 4 ? anti-parallel 
AE8 1 2 ? anti-parallel 
AE8 2 3 ? anti-parallel 
AE8 3 4 ? anti-parallel 
AE9 1 2 ? anti-parallel 
AE9 2 3 ? anti-parallel 
AE9 3 4 ? anti-parallel 
AF1 1 2 ? parallel      
AF1 2 3 ? anti-parallel 
AF1 3 4 ? anti-parallel 
AF1 4 5 ? anti-parallel 
AF1 5 6 ? anti-parallel 
AF2 1 2 ? parallel      
AF2 2 3 ? anti-parallel 
AF2 3 4 ? anti-parallel 
AF3 1 2 ? anti-parallel 
AF3 2 3 ? anti-parallel 
AF3 3 4 ? anti-parallel 
AF4 1 2 ? anti-parallel 
AF4 2 3 ? anti-parallel 
AF5 1 2 ? parallel      
AF5 2 3 ? anti-parallel 
AF5 3 4 ? anti-parallel 
AF5 4 5 ? anti-parallel 
AF6 1 2 ? anti-parallel 
AF6 2 3 ? anti-parallel 
AF7 1 2 ? anti-parallel 
AF7 2 3 ? anti-parallel 
AF7 3 4 ? anti-parallel 
AF8 1 2 ? anti-parallel 
AF8 2 3 ? anti-parallel 
AF8 3 4 ? anti-parallel 
AF9 1 2 ? anti-parallel 
AF9 2 3 ? anti-parallel 
AF9 3 4 ? anti-parallel 
AG1 1 2 ? parallel      
AG1 2 3 ? anti-parallel 
AG1 3 4 ? anti-parallel 
AG1 4 5 ? anti-parallel 
AG1 5 6 ? anti-parallel 
AG2 1 2 ? parallel      
AG2 2 3 ? anti-parallel 
AG2 3 4 ? anti-parallel 
AG3 1 2 ? anti-parallel 
AG3 2 3 ? anti-parallel 
AG3 3 4 ? anti-parallel 
AG4 1 2 ? anti-parallel 
AG4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 462 ? THR A 467 ? LEU A 494 THR A 499 
AA1 2 TRP A 5   ? TYR A 10  ? TRP A 35  TYR A 40  
AA1 3 ILE B 92  ? PRO B 98  ? ILE B 603 PRO B 609 
AA2 1 TRP A 15  ? ASP A 17  ? TRP A 45  ASP A 47  
AA2 2 TYR A 454 ? ILE A 459 ? TYR A 486 ILE A 491 
AA2 3 PHE A 193 ? CYS A 198 ? PHE A 223 CYS A 228 
AA2 4 VAL A 212 ? VAL A 215 ? VAL A 242 VAL A 245 
AA2 5 ILE A 54  ? LEU A 56  ? ILE A 84  LEU A 86  
AA3 1 GLU A 61  ? ASN A 64  ? GLU A 91  ASN A 94  
AA3 2 THR A 206 ? CYS A 209 ? THR A 236 CYS A 239 
AA4 1 LEU A 99  ? GLN A 100 ? LEU A 129 GLN A 130 
AA4 2 GLU A 160 ? LEU A 163 ? GLU A 190 LEU A 193 
AA4 3 VAL A 143 ? GLN A 145 ? VAL A 181 GLN A 183 
AA5 1 LEU A 116 ? ASN A 122 ? LEU A 154 ASN A 160 
AA5 2 LYS A 133 ? TYR A 139 ? LYS A 171 TYR A 177 
AA6 1 ALA A 170 ? GLN A 173 ? ALA A 200 GLN A 203 
AA6 2 GLN A 400 ? TYR A 403 ? GLN A 432 TYR A 435 
AA6 3 ILE A 391 ? ILE A 392 ? ILE A 423 ILE A 424 
AA7 1 LEU A 229 ? LEU A 231 ? LEU A 259 LEU A 261 
AA7 2 ILE A 411 ? ARG A 424 ? ILE A 443 ARG A 456 
AA7 3 ILE A 254 ? ARG A 268 ? ILE A 284 ARG A 298 
AA7 4 HIS A 299 ? SER A 303 ? HIS A 330 SER A 334 
AA7 5 SER A 381 ? LYS A 389 ? SER A 413 LYS A 421 
AA7 6 GLU A 350 ? ASN A 355 ? GLU A 381 ASN A 386 
AA7 7 THR A 342 ? CYS A 347 ? THR A 373 CYS A 378 
AA8 1 MET A 241 ? SER A 244 ? MET A 271 SER A 274 
AA8 2 ILE A 254 ? ARG A 268 ? ILE A 284 ARG A 298 
AA8 3 ILE A 411 ? ARG A 424 ? ILE A 443 ARG A 456 
AA8 4 THR A 433 ? PRO A 438 ? THR A 465 PRO A 470 
AA8 5 ILE A 327 ? PHE A 330 ? ILE A 358 PHE A 361 
AA8 6 SER A 362 ? TRP A 364 ? SER A 393 TRP A 395 
AA9 1 ARG A 274 ? ILE A 277 ? ARG A 304 ILE A 307 
AA9 2 PHE A 285 ? THR A 288 ? PHE A 317 THR A 320 
AB1 1 LEU C 462 ? THR C 467 ? LEU C 494 THR C 499 
AB1 2 TRP C 5   ? TYR C 10  ? TRP C 35  TYR C 40  
AB1 3 ILE H 92  ? PRO H 98  ? ILE D 603 PRO D 609 
AB2 1 TRP C 15  ? ASP C 17  ? TRP C 45  ASP C 47  
AB2 2 TYR C 454 ? ILE C 459 ? TYR C 486 ILE C 491 
AB2 3 PHE C 193 ? CYS C 198 ? PHE C 223 CYS C 228 
AB2 4 VAL C 212 ? VAL C 215 ? VAL C 242 VAL C 245 
AB2 5 GLU C 53  ? LEU C 56  ? GLU C 83  LEU C 86  
AB3 1 GLU C 61  ? ASN C 64  ? GLU C 91  ASN C 94  
AB3 2 THR C 206 ? CYS C 209 ? THR C 236 CYS C 239 
AB4 1 LEU C 116 ? ASN C 122 ? LEU C 154 ASN C 160 
AB4 2 LYS C 133 ? TYR C 139 ? LYS C 171 TYR C 177 
AB5 1 VAL C 143 ? GLN C 145 ? VAL C 181 GLN C 183 
AB5 2 TYR C 161 ? LEU C 163 ? TYR C 191 LEU C 193 
AB6 1 ALA C 170 ? GLN C 173 ? ALA C 200 GLN C 203 
AB6 2 GLN C 400 ? TYR C 403 ? GLN C 432 TYR C 435 
AB6 3 ILE C 391 ? ILE C 392 ? ILE C 423 ILE C 424 
AB7 1 LEU C 229 ? LEU C 231 ? LEU C 259 LEU C 261 
AB7 2 ILE C 411 ? ARG C 424 ? ILE C 443 ARG C 456 
AB7 3 ILE C 254 ? ARG C 268 ? ILE C 284 ARG C 298 
AB7 4 ALA C 298 ? SER C 303 ? ALA C 329 SER C 334 
AB7 5 SER C 381 ? LYS C 389 ? SER C 413 LYS C 421 
AB7 6 GLU C 350 ? CYS C 354 ? GLU C 381 CYS C 385 
AB7 7 HIS C 343 ? CYS C 347 ? HIS C 374 CYS C 378 
AB8 1 MET C 241 ? SER C 244 ? MET C 271 SER C 274 
AB8 2 ILE C 254 ? ARG C 268 ? ILE C 284 ARG C 298 
AB8 3 ILE C 411 ? ARG C 424 ? ILE C 443 ARG C 456 
AB8 4 THR C 433 ? PRO C 438 ? THR C 465 PRO C 470 
AB8 5 ILE C 327 ? PHE C 330 ? ILE C 358 PHE C 361 
AB8 6 SER C 362 ? TRP C 364 ? SER C 393 TRP C 395 
AB9 1 ARG C 274 ? ILE C 277 ? ARG C 304 ILE C 307 
AB9 2 PHE C 285 ? THR C 288 ? PHE C 317 THR C 320 
AC1 1 THR D 3   ? VAL D 7   ? THR L 8   VAL L 13  
AC1 2 THR D 102 ? VAL D 106 ? THR L 102 VAL L 106 
AC1 3 ASP D 82  ? HIS D 86  ? ASP L 85  HIS L 89  
AC1 4 ILE D 28  ? GLN D 32  ? ILE L 34  GLN L 38  
AC1 5 SER D 39  ? ILE D 42  ? SER L 45  ILE L 48  
AC2 1 THR D 12  ? GLU D 20  ? THR L 18  GLU L 26  
AC2 2 THR D 67  ? THR D 73  ? THR L 70  THR L 76  
AC2 3 PHE D 56  ? GLY D 58  ? PHE L 62  GLY L 64  
AC3 1 SER D 115 ? PHE D 119 ? SER L 115 PHE L 119 
AC3 2 ALA D 131 ? PHE D 140 ? ALA L 131 PHE L 140 
AC3 3 TYR D 173 ? LEU D 181 ? TYR L 173 LEU L 181 
AC3 4 VAL D 160 ? THR D 162 ? VAL L 160 THR L 162 
AC4 1 SER D 154 ? PRO D 155 ? SER L 154 PRO L 155 
AC4 2 VAL D 145 ? ALA D 151 ? VAL L 145 ALA L 151 
AC4 3 TYR D 192 ? HIS D 198 ? TYR L 192 HIS L 198 
AC4 4 SER D 201 ? VAL D 207 ? SER L 201 VAL L 207 
AC5 1 VAL E 3   ? GLN E 6   ? VAL E 3   GLN E 6   
AC5 2 VAL E 18  ? PHE E 25  ? VAL E 18  PHE E 25  
AC5 3 THR E 78  ? VAL E 83  ? THR E 77  VAL E 82  
AC5 4 VAL E 68  ? ASP E 73  ? VAL E 67  ASP E 72  
AC6 1 GLU E 10  ? LYS E 12  ? GLU E 10  LYS E 12  
AC6 2 THR E 116 ? VAL E 120 ? THR E 107 VAL E 111 
AC6 3 GLY E 92  ? ASP E 99  ? GLY E 88  ASP E 95  
AC6 4 LEU E 34  ? GLN E 39  ? LEU E 34  GLN E 39  
AC6 5 LEU E 45  ? ILE E 51  ? LEU E 45  ILE E 51  
AC6 6 THR E 58  ? THR E 60  ? THR E 57  THR E 59  
AC7 1 GLU E 10  ? LYS E 12  ? GLU E 10  LYS E 12  
AC7 2 THR E 116 ? VAL E 120 ? THR E 107 VAL E 111 
AC7 3 GLY E 92  ? ASP E 99  ? GLY E 88  ASP E 95  
AC7 4 MET E 109 E TRP E 112 ? MET E 100 TRP E 103 
AC8 1 SER E 129 ? LEU E 133 ? SER E 120 LEU E 124 
AC8 2 THR E 144 ? TYR E 154 ? THR E 135 TYR E 145 
AC8 3 TYR E 185 ? PRO E 194 ? TYR E 176 PRO E 185 
AC8 4 VAL E 172 ? THR E 174 ? VAL E 163 THR E 165 
AC9 1 SER E 129 ? LEU E 133 ? SER E 120 LEU E 124 
AC9 2 THR E 144 ? TYR E 154 ? THR E 135 TYR E 145 
AC9 3 TYR E 185 ? PRO E 194 ? TYR E 176 PRO E 185 
AC9 4 VAL E 178 ? LEU E 179 ? VAL E 169 LEU E 170 
AD1 1 THR E 160 ? TRP E 163 ? THR E 151 TRP E 154 
AD1 2 ILE E 204 ? HIS E 209 ? ILE E 195 HIS E 200 
AD1 3 THR E 214 ? LYS E 219 ? THR E 205 LYS E 210 
AD2 1 LEU F 4   ? SER F 7   ? LEU F 4   SER F 7   
AD2 2 VAL F 19  ? ALA F 25  ? VAL F 19  ALA F 25  
AD2 3 HIS F 70  ? VAL F 75  ? HIS F 70  VAL F 75  
AD2 4 PHE F 62  ? SER F 67  ? PHE F 62  SER F 67  
AD3 1 PHE F 10  ? ALA F 13  ? PHE F 10  ALA F 13  
AD3 2 THR F 102 ? ILE F 106 ? THR F 102 ILE F 106 
AD3 3 THR F 85  ? HIS F 90  ? THR F 85  HIS F 90  
AD3 4 LEU F 33  ? GLN F 38  ? LEU F 33  GLN F 38  
AD3 5 ASN F 45  ? TYR F 49  ? ASN F 45  TYR F 49  
AD3 6 THR F 53  ? LEU F 54  ? THR F 53  LEU F 54  
AD4 1 PHE F 10  ? ALA F 13  ? PHE F 10  ALA F 13  
AD4 2 THR F 102 ? ILE F 106 ? THR F 102 ILE F 106 
AD4 3 THR F 85  ? HIS F 90  ? THR F 85  HIS F 90  
AD4 4 THR F 97  ? PHE F 98  ? THR F 97  PHE F 98  
AD5 1 SER F 114 ? PHE F 118 ? SER F 114 PHE F 118 
AD5 2 THR F 129 ? PHE F 139 ? THR F 129 PHE F 139 
AD5 3 TYR F 173 ? SER F 182 ? TYR F 173 SER F 182 
AD5 4 SER F 159 ? VAL F 163 ? SER F 159 VAL F 163 
AD6 1 ALA F 153 ? LEU F 154 ? ALA F 153 LEU F 154 
AD6 2 LYS F 145 ? VAL F 150 ? LYS F 145 VAL F 150 
AD6 3 VAL F 191 ? THR F 197 ? VAL F 191 THR F 197 
AD6 4 VAL F 205 ? ASN F 210 ? VAL F 205 ASN F 210 
AD7 1 VAL G 3   ? GLN G 6   ? VAL G 3   GLN G 6   
AD7 2 VAL G 18  ? PHE G 25  ? VAL G 18  PHE G 25  
AD7 3 THR G 78  ? VAL G 83  ? THR G 77  VAL G 82  
AD7 4 VAL G 68  ? ASP G 73  ? VAL G 67  ASP G 72  
AD8 1 GLU G 10  ? LYS G 12  ? GLU G 10  LYS G 12  
AD8 2 THR G 116 ? VAL G 120 ? THR G 107 VAL G 111 
AD8 3 GLY G 92  ? ASP G 99  ? GLY G 88  ASP G 95  
AD8 4 LEU G 34  ? GLN G 39  ? LEU G 34  GLN G 39  
AD8 5 LEU G 45  ? ILE G 51  ? LEU G 45  ILE G 51  
AD8 6 THR G 58  ? THR G 60  ? THR G 57  THR G 59  
AD9 1 GLU G 10  ? LYS G 12  ? GLU G 10  LYS G 12  
AD9 2 THR G 116 ? VAL G 120 ? THR G 107 VAL G 111 
AD9 3 GLY G 92  ? ASP G 99  ? GLY G 88  ASP G 95  
AD9 4 MET G 109 E TRP G 112 ? MET G 100 TRP G 103 
AE1 1 SER G 129 ? LEU G 133 ? SER G 120 LEU G 124 
AE1 2 THR G 144 ? TYR G 154 ? THR G 135 TYR G 145 
AE1 3 TYR G 185 ? PRO G 194 ? TYR G 176 PRO G 185 
AE1 4 VAL G 172 ? THR G 174 ? VAL G 163 THR G 165 
AE2 1 SER G 129 ? LEU G 133 ? SER G 120 LEU G 124 
AE2 2 THR G 144 ? TYR G 154 ? THR G 135 TYR G 145 
AE2 3 TYR G 185 ? PRO G 194 ? TYR G 176 PRO G 185 
AE2 4 VAL G 178 ? LEU G 179 ? VAL G 169 LEU G 170 
AE3 1 THR G 160 ? TRP G 163 ? THR G 151 TRP G 154 
AE3 2 ILE G 204 ? HIS G 209 ? ILE G 195 HIS G 200 
AE3 3 THR G 214 ? LYS G 219 ? THR G 205 LYS G 210 
AE4 1 LEU I 4   ? SER I 7   ? LEU H 4   SER H 7   
AE4 2 VAL I 19  ? ALA I 25  ? VAL H 19  ALA H 25  
AE4 3 HIS I 70  ? VAL I 75  ? HIS H 70  VAL H 75  
AE4 4 PHE I 62  ? SER I 67  ? PHE H 62  SER H 67  
AE5 1 PHE I 10  ? ALA I 13  ? PHE H 10  ALA H 13  
AE5 2 THR I 102 ? ILE I 106 ? THR H 102 ILE H 106 
AE5 3 THR I 85  ? HIS I 90  ? THR H 85  HIS H 90  
AE5 4 LEU I 33  ? GLN I 38  ? LEU H 33  GLN H 38  
AE5 5 ASN I 45  ? TYR I 49  ? ASN H 45  TYR H 49  
AE5 6 THR I 53  ? LEU I 54  ? THR H 53  LEU H 54  
AE6 1 PHE I 10  ? ALA I 13  ? PHE H 10  ALA H 13  
AE6 2 THR I 102 ? ILE I 106 ? THR H 102 ILE H 106 
AE6 3 THR I 85  ? HIS I 90  ? THR H 85  HIS H 90  
AE6 4 THR I 97  ? PHE I 98  ? THR H 97  PHE H 98  
AE7 1 SER I 114 ? PHE I 118 ? SER H 114 PHE H 118 
AE7 2 THR I 129 ? PHE I 139 ? THR H 129 PHE H 139 
AE7 3 TYR I 173 ? SER I 182 ? TYR H 173 SER H 182 
AE7 4 SER I 159 ? VAL I 163 ? SER H 159 VAL H 163 
AE8 1 ALA I 153 ? LEU I 154 ? ALA H 153 LEU H 154 
AE8 2 LYS I 145 ? VAL I 150 ? LYS H 145 VAL H 150 
AE8 3 VAL I 191 ? THR I 197 ? VAL H 191 THR H 197 
AE8 4 VAL I 205 ? ASN I 210 ? VAL H 205 ASN H 210 
AE9 1 HIS J 3   ? SER J 7   ? HIS I 3   SER I 7   
AE9 2 THR J 17  ? SER J 25  ? THR I 17  SER I 25  
AE9 3 LEU J 77  ? THR J 83  A LEU I 77  THR I 82  
AE9 4 VAL J 67  ? ASP J 72  ? VAL I 67  ASP I 72  
AF1 1 LEU J 11  ? VAL J 12  ? LEU I 11  VAL I 12  
AF1 2 THR J 126 ? VAL J 130 ? THR I 105 VAL I 109 
AF1 3 ALA J 91  ? ILE J 104 A ALA I 88  ILE I 100 
AF1 4 TYR J 33  ? ARG J 38  ? TYR I 33  ARG I 38  
AF1 5 GLU J 46  ? VAL J 51  ? GLU I 46  VAL I 51  
AF1 6 THR J 57  ? TYR J 59  ? THR I 57  TYR I 59  
AF2 1 LEU J 11  ? VAL J 12  ? LEU I 11  VAL I 12  
AF2 2 THR J 126 ? VAL J 130 ? THR I 105 VAL I 109 
AF2 3 ALA J 91  ? ILE J 104 A ALA I 88  ILE I 100 
AF2 4 TRP J 113 J MET J 119 P TRP I 100 MET I 100 
AF3 1 SER J 139 ? LEU J 143 ? SER I 118 LEU I 122 
AF3 2 THR J 154 ? TYR J 164 ? THR I 133 TYR I 143 
AF3 3 TYR J 195 ? PRO J 204 ? TYR I 174 PRO I 183 
AF3 4 VAL J 182 ? PHE J 185 ? VAL I 161 PHE I 164 
AF4 1 THR J 170 ? TRP J 173 ? THR I 149 TRP I 152 
AF4 2 ILE J 214 ? HIS J 219 ? ILE I 193 HIS I 198 
AF4 3 THR J 224 ? ARG J 229 ? THR I 203 ARG I 208 
AF5 1 THR K 3   ? VAL K 7   ? THR J 8   VAL J 13  
AF5 2 THR K 102 ? VAL K 106 ? THR J 102 VAL J 106 
AF5 3 ASP K 82  ? HIS K 86  ? ASP J 85  HIS J 89  
AF5 4 ILE K 28  ? GLN K 32  ? ILE J 34  GLN J 38  
AF5 5 SER K 39  ? ILE K 42  ? SER J 45  ILE J 48  
AF6 1 THR K 12  ? GLU K 20  ? THR J 18  GLU J 26  
AF6 2 THR K 67  ? THR K 73  ? THR J 70  THR J 76  
AF6 3 PHE K 56  ? GLY K 58  ? PHE J 62  GLY J 64  
AF7 1 SER K 115 ? PHE K 119 ? SER J 115 PHE J 119 
AF7 2 ALA K 131 ? PHE K 140 ? ALA J 131 PHE J 140 
AF7 3 TYR K 173 ? LEU K 181 ? TYR J 173 LEU J 181 
AF7 4 VAL K 160 ? THR K 162 ? VAL J 160 THR J 162 
AF8 1 SER K 154 ? PRO K 155 ? SER J 154 PRO J 155 
AF8 2 VAL K 145 ? ALA K 151 ? VAL J 145 ALA J 151 
AF8 3 TYR K 192 ? HIS K 198 ? TYR J 192 HIS J 198 
AF8 4 SER K 201 ? VAL K 207 ? SER J 201 VAL J 207 
AF9 1 HIS L 3   ? SER L 7   ? HIS K 3   SER K 7   
AF9 2 THR L 17  ? SER L 25  ? THR K 17  SER K 25  
AF9 3 LEU L 77  ? THR L 83  A LEU K 77  THR K 82  
AF9 4 VAL L 67  ? ASP L 72  ? VAL K 67  ASP K 72  
AG1 1 LEU L 11  ? VAL L 12  ? LEU K 11  VAL K 12  
AG1 2 THR L 126 ? VAL L 130 ? THR K 105 VAL K 109 
AG1 3 ALA L 91  ? ILE L 104 A ALA K 88  ILE K 100 
AG1 4 TYR L 33  ? ARG L 38  ? TYR K 33  ARG K 38  
AG1 5 GLU L 46  ? VAL L 51  ? GLU K 46  VAL K 51  
AG1 6 THR L 57  ? TYR L 59  ? THR K 57  TYR K 59  
AG2 1 LEU L 11  ? VAL L 12  ? LEU K 11  VAL K 12  
AG2 2 THR L 126 ? VAL L 130 ? THR K 105 VAL K 109 
AG2 3 ALA L 91  ? ILE L 104 A ALA K 88  ILE K 100 
AG2 4 TRP L 113 J MET L 119 P TRP K 100 MET K 100 
AG3 1 SER L 139 ? LEU L 143 ? SER K 118 LEU K 122 
AG3 2 THR L 154 ? TYR L 164 ? THR K 133 TYR K 143 
AG3 3 TYR L 195 ? PRO L 204 ? TYR K 174 PRO K 183 
AG3 4 VAL L 182 ? PHE L 185 ? VAL K 161 PHE K 164 
AG4 1 THR L 170 ? TRP L 173 ? THR K 149 TRP K 152 
AG4 2 ILE L 214 ? HIS L 219 ? ILE K 193 HIS K 198 
AG4 3 THR L 224 ? ARG L 229 ? THR K 203 ARG K 208 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O THR A 467 ? O THR A 499 N TRP A 5   ? N TRP A 35  
AA1 2 3 N VAL A 6   ? N VAL A 36  O VAL B 97  ? O VAL B 608 
AA2 1 2 N LYS A 16  ? N LYS A 46  O LYS A 458 ? O LYS A 490 
AA2 2 3 O VAL A 457 ? O VAL A 489 N ALA A 194 ? N ALA A 224 
AA2 3 4 N LYS A 197 ? N LYS A 227 O SER A 213 ? O SER A 243 
AA2 4 5 O THR A 214 ? O THR A 244 N ILE A 54  ? N ILE A 84  
AA3 1 2 N PHE A 63  ? N PHE A 93  O GLY A 207 ? O GLY A 237 
AA4 1 2 N LEU A 99  ? N LEU A 129 O TYR A 161 ? O TYR A 191 
AA4 2 3 O ARG A 162 ? O ARG A 192 N VAL A 144 ? N VAL A 182 
AA5 1 2 N CYS A 119 ? N CYS A 157 O SER A 136 ? O SER A 174 
AA6 1 2 N THR A 172 ? N THR A 202 O ALA A 401 ? O ALA A 433 
AA6 2 3 O MET A 402 ? O MET A 434 N ILE A 392 ? N ILE A 424 
AA7 1 2 N LEU A 230 ? N LEU A 260 O GLY A 419 ? O GLY A 451 
AA7 2 3 O LEU A 422 ? O LEU A 454 N ILE A 254 ? N ILE A 284 
AA7 3 4 N ASN A 265 ? N ASN A 295 O ASN A 301 ? O ASN A 332 
AA7 4 5 N VAL A 302 ? N VAL A 333 O ILE A 382 ? O ILE A 414 
AA7 5 6 O PRO A 385 ? O PRO A 417 N ASN A 355 ? N ASN A 386 
AA7 6 7 O CYS A 354 ? O CYS A 385 N HIS A 343 ? N HIS A 374 
AA8 1 2 N ARG A 243 ? N ARG A 273 O LEU A 255 ? O LEU A 285 
AA8 2 3 N ILE A 254 ? N ILE A 284 O LEU A 422 ? O LEU A 454 
AA8 3 4 N THR A 423 ? N THR A 455 O ARG A 437 ? O ARG A 469 
AA8 4 5 O GLU A 434 ? O GLU A 466 N ARG A 329 ? N ARG A 360 
AA8 5 6 N ILE A 328 ? N ILE A 359 O TRP A 364 ? O TRP A 395 
AA9 1 2 N LYS A 275 ? N LYS A 305 O ALA A 287 ? O ALA A 319 
AB1 1 2 O THR C 467 ? O THR C 499 N TRP C 5   ? N TRP C 35  
AB1 2 3 N VAL C 6   ? N VAL C 36  O VAL H 97  ? O VAL D 608 
AB2 1 2 N LYS C 16  ? N LYS C 46  O LYS C 458 ? O LYS C 490 
AB2 2 3 O VAL C 457 ? O VAL C 489 N ALA C 194 ? N ALA C 224 
AB2 3 4 N LYS C 197 ? N LYS C 227 O SER C 213 ? O SER C 243 
AB2 4 5 O THR C 214 ? O THR C 244 N ILE C 54  ? N ILE C 84  
AB3 1 2 N PHE C 63  ? N PHE C 93  O GLY C 207 ? O GLY C 237 
AB4 1 2 N LYS C 117 ? N LYS C 155 O PHE C 138 ? O PHE C 176 
AB5 1 2 N VAL C 144 ? N VAL C 182 O ARG C 162 ? O ARG C 192 
AB6 1 2 N THR C 172 ? N THR C 202 O ALA C 401 ? O ALA C 433 
AB6 2 3 O MET C 402 ? O MET C 434 N ILE C 392 ? N ILE C 424 
AB7 1 2 N LEU C 230 ? N LEU C 260 O GLY C 419 ? O GLY C 451 
AB7 2 3 O LEU C 420 ? O LEU C 452 N VAL C 256 ? N VAL C 286 
AB7 3 4 N ASN C 265 ? N ASN C 295 O ASN C 301 ? O ASN C 332 
AB7 4 5 N VAL C 302 ? N VAL C 333 O ILE C 382 ? O ILE C 414 
AB7 5 6 O ARG C 387 ? O ARG C 419 N TYR C 353 ? N TYR C 384 
AB7 6 7 O CYS C 354 ? O CYS C 385 N HIS C 343 ? N HIS C 374 
AB8 1 2 N ARG C 243 ? N ARG C 273 O LEU C 255 ? O LEU C 285 
AB8 2 3 N VAL C 256 ? N VAL C 286 O LEU C 420 ? O LEU C 452 
AB8 3 4 N THR C 423 ? N THR C 455 O ARG C 437 ? O ARG C 469 
AB8 4 5 O PHE C 436 ? O PHE C 468 N ARG C 329 ? N ARG C 360 
AB8 5 6 N ILE C 328 ? N ILE C 359 O TRP C 364 ? O TRP C 395 
AB9 1 2 N LYS C 275 ? N LYS C 305 O ALA C 287 ? O ALA C 319 
AC1 1 2 N VAL D 5   ? N VAL L 11  O ILE D 105 ? O ILE L 105 
AC1 2 3 O THR D 102 ? O THR L 102 N TYR D 83  ? N TYR L 86  
AC1 3 4 O HIS D 86  ? O HIS L 89  N ILE D 28  ? N ILE L 34  
AC1 4 5 N TRP D 29  ? N TRP L 35  O ILE D 42  ? O ILE L 48  
AC2 1 2 N ALA D 13  ? N ALA L 19  O ILE D 72  ? O ILE L 75  
AC2 2 3 O THR D 71  ? O THR L 74  N SER D 57  ? N SER L 63  
AC3 1 2 N SER D 115 ? N SER L 115 O SER D 138 ? O SER L 138 
AC3 2 3 N ILE D 137 ? N ILE L 137 O ALA D 175 ? O ALA L 175 
AC3 3 4 O TYR D 178 ? O TYR L 178 N GLU D 161 ? N GLU L 161 
AC4 1 2 O SER D 154 ? O SER L 154 N ALA D 151 ? N ALA L 151 
AC4 2 3 N THR D 146 ? N THR L 146 O THR D 197 ? O THR L 197 
AC4 3 4 N VAL D 196 ? N VAL L 196 O VAL D 203 ? O VAL L 203 
AC5 1 2 N VAL E 5   ? N VAL E 5   O ARG E 23  ? O ARG E 23  
AC5 2 3 N CYS E 22  ? N CYS E 22  O ALA E 79  ? O ALA E 78  
AC5 3 4 O ASP E 82  ? O ASP E 81  N TYR E 69  ? N TYR E 68  
AC6 1 2 N GLU E 10  ? N GLU E 10  O SER E 117 ? O SER E 108 
AC6 2 3 O VAL E 118 ? O VAL E 109 N GLY E 92  ? N GLY E 88  
AC6 3 4 O TYR E 95  ? O TYR E 91  N VAL E 37  ? N VAL E 37  
AC6 4 5 N LEU E 34  ? N LEU E 34  O ILE E 51  ? O ILE E 51  
AC6 5 6 N TRP E 50  ? N TRP E 50  O THR E 59  ? O THR E 58  
AC7 1 2 N GLU E 10  ? N GLU E 10  O SER E 117 ? O SER E 108 
AC7 2 3 O VAL E 118 ? O VAL E 109 N GLY E 92  ? N GLY E 88  
AC7 3 4 N ARG E 98  ? N ARG E 94  O VAL E 111 ? O VAL E 102 
AC8 1 2 N SER E 129 ? N SER E 120 O LYS E 152 ? O LYS E 143 
AC8 2 3 N VAL E 151 ? N VAL E 142 O LEU E 187 ? O LEU E 178 
AC8 3 4 O VAL E 190 ? O VAL E 181 N HIS E 173 ? N HIS E 164 
AC9 1 2 N SER E 129 ? N SER E 120 O LYS E 152 ? O LYS E 143 
AC9 2 3 N VAL E 151 ? N VAL E 142 O LEU E 187 ? O LEU E 178 
AC9 3 4 O SER E 186 ? O SER E 177 N VAL E 178 ? N VAL E 169 
AD1 1 2 N SER E 162 ? N SER E 153 O ASN E 206 ? O ASN E 197 
AD1 2 3 N VAL E 207 ? N VAL E 198 O VAL E 216 ? O VAL E 207 
AD2 1 2 N THR F 5   ? N THR F 5   O ARG F 24  ? O ARG F 24  
AD2 2 3 N CYS F 23  ? N CYS F 23  O PHE F 71  ? O PHE F 71  
AD2 3 4 O THR F 74  ? O THR F 74  N SER F 63  ? N SER F 63  
AD3 1 2 N LEU F 11  ? N LEU F 11  O LYS F 103 ? O LYS F 103 
AD3 2 3 O THR F 102 ? O THR F 102 N TYR F 86  ? N TYR F 86  
AD3 3 4 O GLN F 89  ? O GLN F 89  N ALA F 34  ? N ALA F 34  
AD3 4 5 N TRP F 35  ? N TRP F 35  O LEU F 47  ? O LEU F 47  
AD3 5 6 N TYR F 49  ? N TYR F 49  O THR F 53  ? O THR F 53  
AD4 1 2 N LEU F 11  ? N LEU F 11  O LYS F 103 ? O LYS F 103 
AD4 2 3 O THR F 102 ? O THR F 102 N TYR F 86  ? N TYR F 86  
AD4 3 4 N HIS F 90  ? N HIS F 90  O THR F 97  ? O THR F 97  
AD5 1 2 N PHE F 116 ? N PHE F 116 O LEU F 135 ? O LEU F 135 
AD5 2 3 N LEU F 136 ? N LEU F 136 O LEU F 175 ? O LEU F 175 
AD5 3 4 O THR F 178 ? O THR F 178 N GLN F 160 ? N GLN F 160 
AD6 1 2 O ALA F 153 ? O ALA F 153 N VAL F 150 ? N VAL F 150 
AD6 2 3 N LYS F 149 ? N LYS F 149 O ALA F 193 ? O ALA F 193 
AD6 3 4 N VAL F 196 ? N VAL F 196 O VAL F 205 ? O VAL F 205 
AD7 1 2 N VAL G 5   ? N VAL G 5   O ARG G 23  ? O ARG G 23  
AD7 2 3 N CYS G 22  ? N CYS G 22  O ALA G 79  ? O ALA G 78  
AD7 3 4 O THR G 78  ? O THR G 77  N ASP G 73  ? N ASP G 72  
AD8 1 2 N GLU G 10  ? N GLU G 10  O SER G 117 ? O SER G 108 
AD8 2 3 O VAL G 118 ? O VAL G 109 N GLY G 92  ? N GLY G 88  
AD8 3 4 O TYR G 95  ? O TYR G 91  N VAL G 37  ? N VAL G 37  
AD8 4 5 N LEU G 34  ? N LEU G 34  O ILE G 51  ? O ILE G 51  
AD8 5 6 N TRP G 50  ? N TRP G 50  O THR G 59  ? O THR G 58  
AD9 1 2 N GLU G 10  ? N GLU G 10  O SER G 117 ? O SER G 108 
AD9 2 3 O VAL G 118 ? O VAL G 109 N GLY G 92  ? N GLY G 88  
AD9 3 4 N ARG G 98  ? N ARG G 94  O VAL G 111 ? O VAL G 102 
AE1 1 2 N SER G 129 ? N SER G 120 O LYS G 152 ? O LYS G 143 
AE1 2 3 N VAL G 151 ? N VAL G 142 O LEU G 187 ? O LEU G 178 
AE1 3 4 O VAL G 190 ? O VAL G 181 N HIS G 173 ? N HIS G 164 
AE2 1 2 N SER G 129 ? N SER G 120 O LYS G 152 ? O LYS G 143 
AE2 2 3 N VAL G 151 ? N VAL G 142 O LEU G 187 ? O LEU G 178 
AE2 3 4 O SER G 186 ? O SER G 177 N VAL G 178 ? N VAL G 169 
AE3 1 2 N THR G 160 ? N THR G 151 O ASN G 208 ? O ASN G 199 
AE3 2 3 N VAL G 207 ? N VAL G 198 O VAL G 216 ? O VAL G 207 
AE4 1 2 N SER I 7   ? N SER H 7   O THR I 22  ? O THR H 22  
AE4 2 3 N CYS I 23  ? N CYS H 23  O PHE I 71  ? O PHE H 71  
AE4 3 4 O THR I 74  ? O THR H 74  N SER I 63  ? N SER H 63  
AE5 1 2 N ALA I 13  ? N ALA H 13  O GLU I 105 ? O GLU H 105 
AE5 2 3 O THR I 102 ? O THR H 102 N TYR I 86  ? N TYR H 86  
AE5 3 4 O THR I 85  ? O THR H 85  N GLN I 38  ? N GLN H 38  
AE5 4 5 N GLN I 37  ? N GLN H 37  O ASN I 45  ? O ASN H 45  
AE5 5 6 N TYR I 49  ? N TYR H 49  O THR I 53  ? O THR H 53  
AE6 1 2 N ALA I 13  ? N ALA H 13  O GLU I 105 ? O GLU H 105 
AE6 2 3 O THR I 102 ? O THR H 102 N TYR I 86  ? N TYR H 86  
AE6 3 4 N HIS I 90  ? N HIS H 90  O THR I 97  ? O THR H 97  
AE7 1 2 N PHE I 116 ? N PHE H 116 O LEU I 135 ? O LEU H 135 
AE7 2 3 N ALA I 130 ? N ALA H 130 O LEU I 181 ? O LEU H 181 
AE7 3 4 O THR I 178 ? O THR H 178 N GLN I 160 ? N GLN H 160 
AE8 1 2 O ALA I 153 ? O ALA H 153 N VAL I 150 ? N VAL H 150 
AE8 2 3 N LYS I 149 ? N LYS H 149 O ALA I 193 ? O ALA H 193 
AE8 3 4 N VAL I 196 ? N VAL H 196 O VAL I 205 ? O VAL H 205 
AE9 1 2 N GLN J 5   ? N GLN I 5   O ASN J 23  ? O ASN I 23  
AE9 2 3 N LEU J 18  ? N LEU I 18  O LEU J 82  ? O LEU I 82  
AE9 3 4 O LEU J 77  ? O LEU I 77  N ASP J 72  ? N ASP I 72  
AF1 1 2 N VAL J 12  ? N VAL I 12  O THR J 129 ? O THR I 108 
AF1 2 3 O VAL J 128 ? O VAL I 107 N ALA J 91  ? N ALA I 88  
AF1 3 4 O TYR J 94  ? O TYR I 91  N ILE J 37  ? N ILE I 37  
AF1 4 5 N ARG J 38  ? N ARG I 38  O GLU J 46  ? O GLU I 46  
AF1 5 6 N TYR J 50  ? N TYR I 50  O ASN J 58  ? O ASN I 58  
AF2 1 2 N VAL J 12  ? N VAL I 12  O THR J 129 ? O THR I 108 
AF2 2 3 O VAL J 128 ? O VAL I 107 N ALA J 91  ? N ALA I 88  
AF2 3 4 N ARG J 103 ? N ARG I 100 O PHE J 114 K O PHE I 100 
AF3 1 2 N PHE J 141 ? N PHE I 120 O LEU J 160 ? O LEU I 139 
AF3 2 3 N LEU J 157 ? N LEU I 136 O VAL J 201 ? O VAL I 180 
AF3 3 4 O VAL J 200 ? O VAL I 179 N HIS J 183 ? N HIS I 162 
AF4 1 2 N SER J 172 ? N SER I 151 O ASN J 216 ? O ASN I 195 
AF4 2 3 N VAL J 217 ? N VAL I 196 O VAL J 226 ? O VAL I 205 
AF5 1 2 N VAL K 5   ? N VAL J 11  O ILE K 105 ? O ILE J 105 
AF5 2 3 O THR K 102 ? O THR J 102 N TYR K 83  ? N TYR J 86  
AF5 3 4 O ASP K 82  ? O ASP J 85  N GLN K 32  ? N GLN J 38  
AF5 4 5 N TRP K 29  ? N TRP J 35  O ILE K 42  ? O ILE J 48  
AF6 1 2 N ALA K 13  ? N ALA J 19  O ILE K 72  ? O ILE J 75  
AF6 2 3 O THR K 71  ? O THR J 74  N SER K 57  ? N SER J 63  
AF7 1 2 N SER K 115 ? N SER J 115 O SER K 138 ? O SER J 138 
AF7 2 3 N ILE K 137 ? N ILE J 137 O ALA K 175 ? O ALA J 175 
AF7 3 4 O TYR K 178 ? O TYR J 178 N GLU K 161 ? N GLU J 161 
AF8 1 2 O SER K 154 ? O SER J 154 N ALA K 151 ? N ALA J 151 
AF8 2 3 N THR K 146 ? N THR J 146 O THR K 197 ? O THR J 197 
AF8 3 4 N VAL K 196 ? N VAL J 196 O VAL K 203 ? O VAL J 203 
AF9 1 2 N HIS L 3   ? N HIS K 3   O SER L 25  ? O SER K 25  
AF9 2 3 N LEU L 18  ? N LEU K 18  O LEU L 82  ? O LEU K 82  
AF9 3 4 O SER L 79  ? O SER K 79  N SER L 70  ? N SER K 70  
AG1 1 2 N VAL L 12  ? N VAL K 12  O THR L 129 ? O THR K 108 
AG1 2 3 O VAL L 128 ? O VAL K 107 N ALA L 91  ? N ALA K 88  
AG1 3 4 O TYR L 94  ? O TYR K 91  N ILE L 37  ? N ILE K 37  
AG1 4 5 N ARG L 38  ? N ARG K 38  O GLU L 46  ? O GLU K 46  
AG1 5 6 N TYR L 50  ? N TYR K 50  O ASN L 58  ? O ASN K 58  
AG2 1 2 N VAL L 12  ? N VAL K 12  O THR L 129 ? O THR K 108 
AG2 2 3 O VAL L 128 ? O VAL K 107 N ALA L 91  ? N ALA K 88  
AG2 3 4 N ARG L 103 ? N ARG K 100 O PHE L 114 K O PHE K 100 
AG3 1 2 N PHE L 141 ? N PHE K 120 O LEU L 160 ? O LEU K 139 
AG3 2 3 N LEU L 157 ? N LEU K 136 O VAL L 201 ? O VAL K 180 
AG3 3 4 O SER L 198 ? O SER K 177 N PHE L 185 ? N PHE K 164 
AG4 1 2 N SER L 172 ? N SER K 151 O ASN L 216 ? O ASN K 195 
AG4 2 3 N VAL L 217 ? N VAL K 196 O VAL L 226 ? O VAL K 205 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ASN 88  ? 6  'binding site for Poly-Saccharide residues NAG A 901 through MAN A 907 bound to ASN A 88'  
AC2 Software A NAG 908 ? 4  'binding site for Mono-Saccharide NAG A 908 bound to ASN A 133'                            
AC3 Software A ASN 137 ? 10 'binding site for Poly-Saccharide residues ARG I 99 through MAN I 304 bound to ASN A 137'  
AC4 Software A ASN 156 ? 3  'binding site for Poly-Saccharide residues NAG A 909 through MAN A 913 bound to ASN A 156' 
AC5 Software A ASN 160 ? 5  'binding site for Poly-Saccharide residues NAG A 914 through NAG A 915 bound to ASN A 160' 
AC6 Software A ASN 197 ? 3  'binding site for Poly-Saccharide residues NAG A 916 through NAG A 917 bound to ASN A 197' 
AC7 Software A ASN 234 ? 3  'binding site for Poly-Saccharide residues NAG A 918 through NAG A 919 bound to ASN A 234' 
AC8 Software A NAG 926 ? 2  'binding site for Mono-Saccharide NAG A 926 bound to ASN A 276'                            
AC9 Software A ASN 295 ? 3  'binding site for Poly-Saccharide residues NAG A 927 through BMA A 929 bound to ASN A 295' 
AD1 Software A ASN 301 ? 2  'binding site for Poly-Saccharide residues NAG A 930 through NAG A 931 bound to ASN A 301' 
AD2 Software A ASN 332 ? 14 'binding site for Poly-Saccharide residues NAG A 932 through MAN A 941 bound to ASN A 332' 
AD3 Software A NAG 952 ? 1  'binding site for Mono-Saccharide NAG A 952 bound to ASN A 339'                            
AD4 Software A NAG 942 ? 1  'binding site for Mono-Saccharide NAG A 942 bound to ASN A 355'                            
AD5 Software A ASN 386 ? 4  'binding site for Poly-Saccharide residues NAG A 945 through NAG A 946 bound to ASN A 386' 
AD6 Software A ASN 392 ? 2  'binding site for Poly-Saccharide residues NAG A 947 through NAG A 948 bound to ASN A 392' 
AD7 Software A ASN 448 ? 4  'binding site for Poly-Saccharide residues NAG A 949 through BMA A 951 bound to ASN A 448' 
AD8 Software B NAG 901 ? 2  'binding site for Mono-Saccharide NAG B 901 bound to ASN B 611'                            
AD9 Software B NAG 902 ? 1  'binding site for Mono-Saccharide NAG B 902 bound to ASN B 618'                            
AE1 Software B NAG 903 ? 1  'binding site for Mono-Saccharide NAG B 903 bound to ASN B 637'                            
AE2 Software C ASN 88  ? 8  'binding site for Poly-Saccharide residues NAG C 901 through MAN C 907 bound to ASN C 88'  
AE3 Software C NAG 908 ? 2  'binding site for Mono-Saccharide NAG C 908 bound to ASN C 133'                            
AE4 Software C NAG 909 ? 4  'binding site for Mono-Saccharide NAG C 909 bound to ASN C 137'                            
AE5 Software C ASN 156 ? 4  'binding site for Poly-Saccharide residues NAG C 910 through MAN C 914 bound to ASN C 156' 
AE6 Software C ASN 160 ? 5  'binding site for Poly-Saccharide residues NAG C 915 through NAG C 916 bound to ASN C 160' 
AE7 Software C ASN 197 ? 4  'binding site for Poly-Saccharide residues NAG C 917 through NAG C 918 bound to ASN C 197' 
AE8 Software C ASN 234 ? 4  'binding site for Poly-Saccharide residues NAG C 919 through NAG C 920 bound to ASN C 234' 
AE9 Software C ASN 262 ? 10 'binding site for Poly-Saccharide residues NAG C 921 through MAN C 926 bound to ASN C 262' 
AF1 Software C NAG 927 ? 2  'binding site for Mono-Saccharide NAG C 927 bound to ASN C 276'                            
AF2 Software C ASN 295 ? 3  'binding site for Poly-Saccharide residues NAG C 928 through NAG C 929 bound to ASN C 295' 
AF3 Software C ASN 301 ? 2  'binding site for Poly-Saccharide residues NAG C 930 through NAG C 931 bound to ASN C 301' 
AF4 Software C ASN 332 ? 15 'binding site for Poly-Saccharide residues NAG C 932 through MAN C 941 bound to ASN C 332' 
AF5 Software C NAG 953 ? 1  'binding site for Mono-Saccharide NAG C 953 bound to ASN C 339'                            
AF6 Software C NAG 942 ? 1  'binding site for Mono-Saccharide NAG C 942 bound to ASN C 355'                            
AF7 Software C ASN 363 ? 4  'binding site for Poly-Saccharide residues NAG C 943 through NAG C 944 bound to ASN C 363' 
AF8 Software C ASN 386 ? 4  'binding site for Poly-Saccharide residues NAG C 945 through NAG C 946 bound to ASN C 386' 
AF9 Software C ASN 392 ? 1  'binding site for Poly-Saccharide residues NAG C 947 through BMA C 949 bound to ASN C 392' 
AG1 Software C ASN 448 ? 4  'binding site for Poly-Saccharide residues NAG C 950 through BMA C 952 bound to ASN C 448' 
AG2 Software D NAG 901 ? 2  'binding site for Mono-Saccharide NAG D 901 bound to ASN D 611'                            
AG3 Software D NAG 902 ? 1  'binding site for Mono-Saccharide NAG D 902 bound to ASN D 637'                            
AG4 Software I NAG 305 ? 2  'binding site for Mono-Saccharide NAG I 305 bound to ASN I 23'                             
AG5 Software K NAG 301 ? 2  'binding site for Mono-Saccharide NAG K 301 bound to ASN K 23'                             
AG6 Software A NAG 920 ? 10 'binding site for Poly-Saccharide residues NAG A 920 through MAN A 925'                    
AG7 Software A NAG 943 ? 10 'binding site for Poly-Saccharide residues NAG A 943 through NAG A 944'                    
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 6  ASN A  58  ? ASN A 88  . ? 1_555  ? 
2   AC1 6  SER B  17  ? SER B 528 . ? 1_555  ? 
3   AC1 6  TYR E  102 ? TYR E 98  . ? 1_555  ? 
4   AC1 6  ASN F  31  ? ASN F 31  . ? 1_555  ? 
5   AC1 6  TYR F  50  ? TYR F 50  . ? 1_555  ? 
6   AC1 6  ARG I  30  ? ARG H 30  . ? 15_554 ? 
7   AC2 4  ASN A  103 ? ASN A 133 . ? 1_555  ? 
8   AC2 4  ASP A  110 ? ASP A 140 . ? 1_555  ? 
9   AC2 4  LYS A  117 ? LYS A 155 . ? 1_555  ? 
10  AC2 4  LYS A  159 ? LYS A 189 . ? 1_555  ? 
11  AC3 10 ASN A  107 ? ASN A 137 . ? 1_555  ? 
12  AC3 10 TYR J  33  ? TYR I 33  . ? 1_555  ? 
13  AC3 10 ASN J  58  ? ASN I 58  . ? 1_555  ? 
14  AC3 10 HIS J  100 ? HIS I 97  . ? 1_555  ? 
15  AC3 10 GLY J  101 ? GLY I 98  . ? 1_555  ? 
16  AC3 10 ARG J  103 ? ARG I 100 . ? 1_555  ? 
17  AC3 10 ILE J  104 A ILE I 100 . ? 1_555  ? 
18  AC3 10 TRP J  113 J TRP I 100 . ? 1_555  ? 
19  AC3 10 PHE J  114 K PHE I 100 . ? 1_555  ? 
20  AC3 10 THR J  115 L THR I 100 . ? 1_555  ? 
21  AC4 3  THR A  105 ? THR A 135 . ? 1_555  ? 
22  AC4 3  ASN A  118 ? ASN A 156 . ? 1_555  ? 
23  AC4 3  TYR A  135 ? TYR A 173 . ? 1_555  ? 
24  AC5 5  THR A  98  ? THR A 128 . ? 1_555  ? 
25  AC5 5  GLN A  100 ? GLN A 130 . ? 1_555  ? 
26  AC5 5  ASN A  122 ? ASN A 160 . ? 1_555  ? 
27  AC5 5  LYS A  131 ? LYS A 169 . ? 1_555  ? 
28  AC5 5  LYS A  133 ? LYS A 171 . ? 1_555  ? 
29  AC6 3  ARG A  162 ? ARG A 192 . ? 1_555  ? 
30  AC6 3  ASN A  167 ? ASN A 197 . ? 1_555  ? 
31  AC6 3  ARG A  278 ? ARG A 308 . ? 2_555  ? 
32  AC7 3  ASN A  204 ? ASN A 234 . ? 1_555  ? 
33  AC7 3  THR A  206 ? THR A 236 . ? 1_555  ? 
34  AC7 3  SER A  244 ? SER A 274 . ? 1_555  ? 
35  AC8 2  ASN A  246 ? ASN A 276 . ? 1_555  ? 
36  AC8 2  THR A  248 ? THR A 278 . ? 1_555  ? 
37  AC9 3  ASN A  265 ? ASN A 295 . ? 1_555  ? 
38  AC9 3  SER A  303 ? SER A 334 . ? 1_555  ? 
39  AC9 3  SER A  381 ? SER A 413 . ? 1_555  ? 
40  AD1 2  ASN A  271 ? ASN A 301 . ? 1_555  ? 
41  AD1 2  ILE A  292 ? ILE A 323 . ? 1_555  ? 
42  AD2 14 THR A  267 ? THR A 297 . ? 1_555  ? 
43  AD2 14 HIS A  299 ? HIS A 330 . ? 1_555  ? 
44  AD2 14 ASN A  301 ? ASN A 332 . ? 1_555  ? 
45  AD2 14 ASP A  380 ? ASP A 412 . ? 1_555  ? 
46  AD2 14 THR A  383 ? THR A 415 . ? 1_555  ? 
47  AD2 14 ARG J  103 ? ARG I 100 . ? 1_555  ? 
48  AD2 14 ILE J  104 A ILE I 100 . ? 1_555  ? 
49  AD2 14 GLY J  106 C GLY I 100 . ? 1_555  ? 
50  AD2 14 VAL J  107 D VAL I 100 . ? 1_555  ? 
51  AD2 14 ASN K  44  ? ASN J 50  . ? 1_555  ? 
52  AD2 14 ASN K  45  ? ASN J 51  . ? 1_555  ? 
53  AD2 14 ASN K  46  ? ASN J 52  . ? 1_555  ? 
54  AD2 14 PRO K  60  ? PRO J 66  . ? 1_555  ? 
55  AD2 14 GLY K  61  ? GLY J 67  . ? 1_555  ? 
56  AD3 1  ASN A  308 ? ASN A 339 . ? 1_555  ? 
57  AD4 1  ASN A  324 ? ASN A 355 . ? 1_555  ? 
58  AD5 4  ASN A  355 ? ASN A 386 . ? 1_555  ? 
59  AD5 4  SER A  357 ? SER A 388 . ? 1_555  ? 
60  AD5 4  NAG CB .   ? NAG A 943 . ? 1_555  ? 
61  AD5 4  NAG DB .   ? NAG A 944 . ? 1_555  ? 
62  AD6 2  ASN A  361 ? ASN A 392 . ? 1_555  ? 
63  AD6 2  NAG CB .   ? NAG A 943 . ? 1_555  ? 
64  AD7 4  ASN A  232 ? ASN A 262 . ? 1_555  ? 
65  AD7 4  PRO A  261 ? PRO A 291 . ? 1_555  ? 
66  AD7 4  ASN A  416 ? ASN A 448 . ? 1_555  ? 
67  AD7 4  NAG FA .   ? NAG A 920 . ? 1_555  ? 
68  AD8 2  ASN B  100 ? ASN B 611 . ? 1_555  ? 
69  AD8 2  SER B  102 ? SER B 613 . ? 1_555  ? 
70  AD9 1  ASN B  107 ? ASN B 618 . ? 1_555  ? 
71  AE1 1  ASN B  126 ? ASN B 637 . ? 1_555  ? 
72  AE2 8  GLU C  57  ? GLU C 87  . ? 1_555  ? 
73  AE2 8  ASN C  58  ? ASN C 88  . ? 1_555  ? 
74  AE2 8  SER H  17  ? SER D 528 . ? 1_555  ? 
75  AE2 8  GLN F  27  ? GLN F 27  . ? 8_555  ? 
76  AE2 8  TYR G  102 ? TYR G 98  . ? 1_555  ? 
77  AE2 8  ASN I  31  ? ASN H 31  . ? 1_555  ? 
78  AE2 8  TYR I  50  ? TYR H 50  . ? 1_555  ? 
79  AE2 8  SER I  67  ? SER H 67  . ? 1_555  ? 
80  AE3 2  ASN C  103 ? ASN C 133 . ? 1_555  ? 
81  AE3 2  ASP C  110 ? ASP C 140 . ? 1_555  ? 
82  AE4 4  ASN C  107 ? ASN C 137 . ? 1_555  ? 
83  AE4 4  PHE L  114 K PHE K 100 . ? 1_555  ? 
84  AE4 4  ASP D  89  ? ASP L 92  . ? 1_555  ? 
85  AE4 4  THR D  94  B THR L 95  . ? 1_555  ? 
86  AE5 4  THR C  105 ? THR C 135 . ? 1_555  ? 
87  AE5 4  ASN C  118 ? ASN C 156 . ? 1_555  ? 
88  AE5 4  SER C  120 ? SER C 158 . ? 1_555  ? 
89  AE5 4  TYR C  135 ? TYR C 173 . ? 1_555  ? 
90  AE6 5  THR C  98  ? THR C 128 . ? 1_555  ? 
91  AE6 5  GLN C  100 ? GLN C 130 . ? 1_555  ? 
92  AE6 5  ASN C  122 ? ASN C 160 . ? 1_555  ? 
93  AE6 5  LYS C  131 ? LYS C 169 . ? 1_555  ? 
94  AE6 5  LYS C  133 ? LYS C 171 . ? 1_555  ? 
95  AE7 4  VAL C  144 ? VAL C 182 . ? 1_555  ? 
96  AE7 4  ARG C  162 ? ARG C 192 . ? 1_555  ? 
97  AE7 4  ASN C  167 ? ASN C 197 . ? 1_555  ? 
98  AE7 4  ARG C  278 ? ARG C 308 . ? 3_665  ? 
99  AE8 4  ASN C  204 ? ASN C 234 . ? 1_555  ? 
100 AE8 4  THR C  206 ? THR C 236 . ? 1_555  ? 
101 AE8 4  SER C  244 ? SER C 274 . ? 1_555  ? 
102 AE8 4  ILE C  247 ? ILE C 277 . ? 1_555  ? 
103 AE9 10 LYS C  35  ? LYS C 65  . ? 1_555  ? 
104 AE9 10 SER C  179 ? SER C 209 . ? 1_555  ? 
105 AE9 10 GLU C  181 ? GLU C 211 . ? 1_555  ? 
106 AE9 10 ASN C  232 ? ASN C 262 . ? 1_555  ? 
107 AE9 10 ASN C  346 ? ASN C 377 . ? 1_555  ? 
108 AE9 10 GLY C  348 ? GLY C 379 . ? 1_555  ? 
109 AE9 10 GLN C  408 ? GLN C 440 . ? 1_555  ? 
110 AE9 10 VAL C  414 ? VAL C 446 . ? 1_555  ? 
111 AE9 10 SER C  415 ? SER C 447 . ? 1_555  ? 
112 AE9 10 NAG MD .   ? NAG C 950 . ? 1_555  ? 
113 AF1 2  ASN C  246 ? ASN C 276 . ? 1_555  ? 
114 AF1 2  THR C  248 ? THR C 278 . ? 1_555  ? 
115 AF2 3  ASN C  265 ? ASN C 295 . ? 1_555  ? 
116 AF2 3  SER C  303 ? SER C 334 . ? 1_555  ? 
117 AF2 3  SER C  381 ? SER C 413 . ? 1_555  ? 
118 AF3 2  ASN C  271 ? ASN C 301 . ? 1_555  ? 
119 AF3 2  ILE C  292 ? ILE C 323 . ? 1_555  ? 
120 AF4 15 THR C  267 ? THR C 297 . ? 1_555  ? 
121 AF4 15 ARG C  296 ? ARG C 327 . ? 1_555  ? 
122 AF4 15 HIS C  299 ? HIS C 330 . ? 1_555  ? 
123 AF4 15 ASN C  301 ? ASN C 332 . ? 1_555  ? 
124 AF4 15 THR C  383 ? THR C 415 . ? 1_555  ? 
125 AF4 15 ARG L  103 ? ARG K 100 . ? 1_555  ? 
126 AF4 15 ILE L  104 A ILE K 100 . ? 1_555  ? 
127 AF4 15 GLY L  106 C GLY K 100 . ? 1_555  ? 
128 AF4 15 VAL L  107 D VAL K 100 . ? 1_555  ? 
129 AF4 15 SER D  24  ? SER L 30  . ? 1_555  ? 
130 AF4 15 ASN D  44  ? ASN L 50  . ? 1_555  ? 
131 AF4 15 ASN D  45  ? ASN L 51  . ? 1_555  ? 
132 AF4 15 PRO D  60  ? PRO L 66  . ? 1_555  ? 
133 AF4 15 GLY D  61  ? GLY L 67  . ? 1_555  ? 
134 AF4 15 SER D  62  A SER L 67  . ? 1_555  ? 
135 AF5 1  ASN C  308 ? ASN C 339 . ? 1_555  ? 
136 AF6 1  ASN C  324 ? ASN C 355 . ? 1_555  ? 
137 AF7 4  ASN C  332 ? ASN C 363 . ? 1_555  ? 
138 AF7 4  SER C  333 ? SER C 364 . ? 1_555  ? 
139 AF7 4  NAG HD .   ? NAG C 945 . ? 1_555  ? 
140 AF7 4  NAG ID .   ? NAG C 946 . ? 1_555  ? 
141 AF8 4  ASN C  355 ? ASN C 386 . ? 1_555  ? 
142 AF8 4  SER C  357 ? SER C 388 . ? 1_555  ? 
143 AF8 4  NAG FD .   ? NAG C 943 . ? 1_555  ? 
144 AF8 4  NAG GD .   ? NAG C 944 . ? 1_555  ? 
145 AF9 1  ASN C  361 ? ASN C 392 . ? 1_555  ? 
146 AG1 4  ASN C  232 ? ASN C 262 . ? 1_555  ? 
147 AG1 4  PRO C  261 ? PRO C 291 . ? 1_555  ? 
148 AG1 4  ASN C  416 ? ASN C 448 . ? 1_555  ? 
149 AG1 4  NAG JC .   ? NAG C 921 . ? 1_555  ? 
150 AG2 2  ASN H  100 ? ASN D 611 . ? 1_555  ? 
151 AG2 2  SER H  102 ? SER D 613 . ? 1_555  ? 
152 AG3 1  ASN H  126 ? ASN D 637 . ? 1_555  ? 
153 AG4 2  SER J  7   ? SER I 7   . ? 1_555  ? 
154 AG4 2  ASN J  23  ? ASN I 23  . ? 1_555  ? 
155 AG5 2  SER L  7   ? SER K 7   . ? 1_555  ? 
156 AG5 2  ASN L  23  ? ASN K 23  . ? 1_555  ? 
157 AG6 10 LYS A  35  ? LYS A 65  . ? 1_555  ? 
158 AG6 10 SER A  179 ? SER A 209 . ? 1_555  ? 
159 AG6 10 PRO A  182 ? PRO A 212 . ? 1_555  ? 
160 AG6 10 ASN A  232 ? ASN A 262 . ? 1_555  ? 
161 AG6 10 ASN A  346 ? ASN A 377 . ? 1_555  ? 
162 AG6 10 GLY A  348 ? GLY A 379 . ? 1_555  ? 
163 AG6 10 GLN A  408 ? GLN A 440 . ? 1_555  ? 
164 AG6 10 VAL A  414 ? VAL A 446 . ? 1_555  ? 
165 AG6 10 SER A  415 ? SER A 447 . ? 1_555  ? 
166 AG6 10 NAG IB .   ? NAG A 949 . ? 1_555  ? 
167 AG7 10 LYS A  35  ? LYS A 65  . ? 1_555  ? 
168 AG7 10 SER A  179 ? SER A 209 . ? 1_555  ? 
169 AG7 10 ASN A  332 ? ASN A 363 . ? 1_555  ? 
170 AG7 10 GLY A  348 ? GLY A 379 . ? 1_555  ? 
171 AG7 10 SER A  357 ? SER A 388 . ? 1_555  ? 
172 AG7 10 GLN A  408 ? GLN A 440 . ? 1_555  ? 
173 AG7 10 NAG FA .   ? NAG A 920 . ? 1_555  ? 
174 AG7 10 NAG EB .   ? NAG A 945 . ? 1_555  ? 
175 AG7 10 NAG FB .   ? NAG A 946 . ? 1_555  ? 
176 AG7 10 NAG GB .   ? NAG A 947 . ? 1_555  ? 
# 
_atom_sites.entry_id                    5I8H 
_atom_sites.fract_transf_matrix[1][1]   0.003964 
_atom_sites.fract_transf_matrix[1][2]   0.002288 
_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]   0.004577 
_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]   0.001782 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C 
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   . ALA A  1 1   ? -6.640  21.131  133.306 1.00 259.92 ?  31  ALA A N   1 
ATOM   2     C CA  . ALA A  1 1   ? -5.951  22.310  132.797 1.00 258.13 ?  31  ALA A CA  1 
ATOM   3     C C   . ALA A  1 1   ? -5.974  23.447  133.821 1.00 257.67 ?  31  ALA A C   1 
ATOM   4     O O   . ALA A  1 1   ? -5.368  23.346  134.890 1.00 253.98 ?  31  ALA A O   1 
ATOM   5     C CB  . ALA A  1 1   ? -6.572  22.762  131.479 1.00 257.57 ?  31  ALA A CB  1 
ATOM   6     N N   . GLU A  1 2   ? -6.693  24.521  133.487 1.00 262.94 ?  32  GLU A N   1 
ATOM   7     C CA  . GLU A  1 2   ? -6.793  25.680  134.372 1.00 255.93 ?  32  GLU A CA  1 
ATOM   8     C C   . GLU A  1 2   ? -7.693  25.417  135.573 1.00 252.30 ?  32  GLU A C   1 
ATOM   9     O O   . GLU A  1 2   ? -7.490  26.015  136.637 1.00 246.31 ?  32  GLU A O   1 
ATOM   10    C CB  . GLU A  1 2   ? -7.255  26.922  133.612 1.00 264.72 ?  32  GLU A CB  1 
ATOM   11    C CG  . GLU A  1 2   ? -7.083  28.182  134.455 1.00 264.87 ?  32  GLU A CG  1 
ATOM   12    C CD  . GLU A  1 2   ? -6.586  29.377  133.673 1.00 266.76 ?  32  GLU A CD  1 
ATOM   13    O OE1 . GLU A  1 2   ? -5.788  29.187  132.731 1.00 273.83 ?  32  GLU A OE1 1 
ATOM   14    O OE2 . GLU A  1 2   ? -6.968  30.512  134.027 1.00 258.36 -1 32  GLU A OE2 1 
ATOM   15    N N   . ASN A  1 3   ? -8.666  24.521  135.450 1.00 231.80 ?  33  ASN A N   1 
ATOM   16    C CA  . ASN A  1 3   ? -9.494  24.198  136.603 1.00 232.67 ?  33  ASN A CA  1 
ATOM   17    C C   . ASN A  1 3   ? -8.706  23.217  137.462 1.00 225.66 ?  33  ASN A C   1 
ATOM   18    O O   . ASN A  1 3   ? -8.321  22.135  137.006 1.00 223.17 ?  33  ASN A O   1 
ATOM   19    C CB  . ASN A  1 3   ? -10.842 23.627  136.156 1.00 241.17 ?  33  ASN A CB  1 
ATOM   20    C CG  . ASN A  1 3   ? -10.700 22.472  135.173 1.00 241.51 ?  33  ASN A CG  1 
ATOM   21    O OD1 . ASN A  1 3   ? -9.701  22.364  134.462 1.00 240.71 ?  33  ASN A OD1 1 
ATOM   22    N ND2 . ASN A  1 3   ? -11.709 21.608  135.125 1.00 248.27 ?  33  ASN A ND2 1 
ATOM   23    N N   . LEU A  1 4   ? -8.480  23.615  138.712 1.00 210.82 ?  34  LEU A N   1 
ATOM   24    C CA  . LEU A  1 4   ? -7.633  22.932  139.676 1.00 202.46 ?  34  LEU A CA  1 
ATOM   25    C C   . LEU A  1 4   ? -8.277  21.678  140.250 1.00 201.16 ?  34  LEU A C   1 
ATOM   26    O O   . LEU A  1 4   ? -9.494  21.476  140.201 1.00 205.77 ?  34  LEU A O   1 
ATOM   27    C CB  . LEU A  1 4   ? -7.256  23.884  140.810 1.00 199.38 ?  34  LEU A CB  1 
ATOM   28    C CG  . LEU A  1 4   ? -6.613  25.182  140.318 1.00 199.69 ?  34  LEU A CG  1 
ATOM   29    C CD1 . LEU A  1 4   ? -6.279  26.100  141.480 1.00 196.39 ?  34  LEU A CD1 1 
ATOM   30    C CD2 . LEU A  1 4   ? -5.373  24.881  139.489 1.00 192.41 ?  34  LEU A CD2 1 
ATOM   31    N N   . TRP A  1 5   ? -7.411  20.834  140.811 1.00 190.96 ?  35  TRP A N   1 
ATOM   32    C CA  . TRP A  1 5   ? -7.770  19.587  141.464 1.00 190.80 ?  35  TRP A CA  1 
ATOM   33    C C   . TRP A  1 5   ? -6.990  19.493  142.767 1.00 186.86 ?  35  TRP A C   1 
ATOM   34    O O   . TRP A  1 5   ? -5.833  19.918  142.834 1.00 180.54 ?  35  TRP A O   1 
ATOM   35    C CB  . TRP A  1 5   ? -7.419  18.390  140.574 1.00 193.90 ?  35  TRP A CB  1 
ATOM   36    C CG  . TRP A  1 5   ? -8.029  18.470  139.214 1.00 198.90 ?  35  TRP A CG  1 
ATOM   37    C CD1 . TRP A  1 5   ? -7.493  19.079  138.116 1.00 194.13 ?  35  TRP A CD1 1 
ATOM   38    C CD2 . TRP A  1 5   ? -9.297  17.951  138.804 1.00 209.65 ?  35  TRP A CD2 1 
ATOM   39    N NE1 . TRP A  1 5   ? -8.343  18.961  137.046 1.00 203.46 ?  35  TRP A NE1 1 
ATOM   40    C CE2 . TRP A  1 5   ? -9.459  18.273  137.442 1.00 212.37 ?  35  TRP A CE2 1 
ATOM   41    C CE3 . TRP A  1 5   ? -10.309 17.243  139.455 1.00 217.93 ?  35  TRP A CE3 1 
ATOM   42    C CZ2 . TRP A  1 5   ? -10.593 17.910  136.720 1.00 222.42 ?  35  TRP A CZ2 1 
ATOM   43    C CZ3 . TRP A  1 5   ? -11.434 16.882  138.736 1.00 225.51 ?  35  TRP A CZ3 1 
ATOM   44    C CH2 . TRP A  1 5   ? -11.567 17.216  137.383 1.00 226.21 ?  35  TRP A CH2 1 
ATOM   45    N N   . VAL A  1 6   ? -7.626  18.946  143.803 1.00 171.87 ?  36  VAL A N   1 
ATOM   46    C CA  . VAL A  1 6   ? -6.977  18.832  145.103 1.00 170.30 ?  36  VAL A CA  1 
ATOM   47    C C   . VAL A  1 6   ? -5.878  17.771  145.050 1.00 165.93 ?  36  VAL A C   1 
ATOM   48    O O   . VAL A  1 6   ? -5.952  16.803  144.280 1.00 166.67 ?  36  VAL A O   1 
ATOM   49    C CB  . VAL A  1 6   ? -8.023  18.494  146.183 1.00 177.41 ?  36  VAL A CB  1 
ATOM   50    C CG1 . VAL A  1 6   ? -9.146  19.516  146.173 1.00 182.67 ?  36  VAL A CG1 1 
ATOM   51    C CG2 . VAL A  1 6   ? -8.589  17.101  145.957 1.00 180.72 ?  36  VAL A CG2 1 
ATOM   52    N N   . THR A  1 7   ? -4.832  17.969  145.858 1.00 166.29 ?  37  THR A N   1 
ATOM   53    C CA  . THR A  1 7   ? -3.734  17.011  145.973 1.00 160.85 ?  37  THR A CA  1 
ATOM   54    C C   . THR A  1 7   ? -3.272  16.916  147.423 1.00 159.94 ?  37  THR A C   1 
ATOM   55    O O   . THR A  1 7   ? -2.973  17.933  148.057 1.00 158.61 ?  37  THR A O   1 
ATOM   56    C CB  . THR A  1 7   ? -2.571  17.392  145.051 1.00 152.70 ?  37  THR A CB  1 
ATOM   57    O OG1 . THR A  1 7   ? -2.412  18.817  145.047 1.00 150.78 ?  37  THR A OG1 1 
ATOM   58    C CG2 . THR A  1 7   ? -2.823  16.879  143.631 1.00 153.86 ?  37  THR A CG2 1 
ATOM   59    N N   . VAL A  1 8   ? -3.227  15.684  147.932 1.00 147.71 ?  38  VAL A N   1 
ATOM   60    C CA  . VAL A  1 8   ? -2.862  15.380  149.315 1.00 147.48 ?  38  VAL A CA  1 
ATOM   61    C C   . VAL A  1 8   ? -1.350  15.341  149.510 1.00 138.24 ?  38  VAL A C   1 
ATOM   62    O O   . VAL A  1 8   ? -0.634  14.657  148.769 1.00 136.60 ?  38  VAL A O   1 
ATOM   63    C CB  . VAL A  1 8   ? -3.489  14.045  149.748 1.00 152.87 ?  38  VAL A CB  1 
ATOM   64    C CG1 . VAL A  1 8   ? -3.166  13.752  151.204 1.00 152.55 ?  38  VAL A CG1 1 
ATOM   65    C CG2 . VAL A  1 8   ? -4.991  14.056  149.516 1.00 162.40 ?  38  VAL A CG2 1 
ATOM   66    N N   . TYR A  1 9   ? -0.859  16.106  150.484 1.00 152.08 ?  39  TYR A N   1 
ATOM   67    C CA  . TYR A  1 9   ? 0.552   16.124  150.857 1.00 143.22 ?  39  TYR A CA  1 
ATOM   68    C C   . TYR A  1 9   ? 0.705   15.535  152.256 1.00 143.20 ?  39  TYR A C   1 
ATOM   69    O O   . TYR A  1 9   ? -0.036  15.904  153.174 1.00 147.67 ?  39  TYR A O   1 
ATOM   70    C CB  . TYR A  1 9   ? 1.135   17.533  150.756 1.00 138.33 ?  39  TYR A CB  1 
ATOM   71    C CG  . TYR A  1 9   ? 1.298   17.928  149.312 1.00 136.11 ?  39  TYR A CG  1 
ATOM   72    C CD1 . TYR A  1 9   ? 0.241   18.452  148.583 1.00 141.91 ?  39  TYR A CD1 1 
ATOM   73    C CD2 . TYR A  1 9   ? 2.501   17.715  148.658 1.00 128.42 ?  39  TYR A CD2 1 
ATOM   74    C CE1 . TYR A  1 9   ? 0.391   18.782  147.246 1.00 139.65 ?  39  TYR A CE1 1 
ATOM   75    C CE2 . TYR A  1 9   ? 2.663   18.040  147.327 1.00 130.28 ?  39  TYR A CE2 1 
ATOM   76    C CZ  . TYR A  1 9   ? 1.607   18.575  146.623 1.00 133.31 ?  39  TYR A CZ  1 
ATOM   77    O OH  . TYR A  1 9   ? 1.770   18.900  145.294 1.00 135.28 ?  39  TYR A OH  1 
ATOM   78    N N   . TYR A  1 10  ? 1.669   14.625  152.413 1.00 129.96 ?  40  TYR A N   1 
ATOM   79    C CA  . TYR A  1 10  ? 1.962   13.956  153.681 1.00 128.52 ?  40  TYR A CA  1 
ATOM   80    C C   . TYR A  1 10  ? 3.389   14.261  154.111 1.00 125.76 ?  40  TYR A C   1 
ATOM   81    O O   . TYR A  1 10  ? 4.346   13.818  153.467 1.00 124.56 ?  40  TYR A O   1 
ATOM   82    C CB  . TYR A  1 10  ? 1.752   12.449  153.551 1.00 130.82 ?  40  TYR A CB  1 
ATOM   83    C CG  . TYR A  1 10  ? 1.979   11.650  154.818 1.00 128.74 ?  40  TYR A CG  1 
ATOM   84    C CD1 . TYR A  1 10  ? 1.172   11.813  155.936 1.00 133.13 ?  40  TYR A CD1 1 
ATOM   85    C CD2 . TYR A  1 10  ? 2.997   10.707  154.878 1.00 126.48 ?  40  TYR A CD2 1 
ATOM   86    C CE1 . TYR A  1 10  ? 1.387   11.065  157.087 1.00 130.64 ?  40  TYR A CE1 1 
ATOM   87    C CE2 . TYR A  1 10  ? 3.216   9.958   156.013 1.00 125.72 ?  40  TYR A CE2 1 
ATOM   88    C CZ  . TYR A  1 10  ? 2.412   10.138  157.115 1.00 126.50 ?  40  TYR A CZ  1 
ATOM   89    O OH  . TYR A  1 10  ? 2.644   9.382   158.242 1.00 125.87 ?  40  TYR A OH  1 
ATOM   90    N N   . GLY A  1 11  ? 3.524   15.010  155.200 1.00 121.89 ?  41  GLY A N   1 
ATOM   91    C CA  . GLY A  1 11  ? 4.821   15.390  155.714 1.00 119.43 ?  41  GLY A CA  1 
ATOM   92    C C   . GLY A  1 11  ? 5.009   16.882  155.580 1.00 119.20 ?  41  GLY A C   1 
ATOM   93    O O   . GLY A  1 11  ? 6.127   17.352  155.353 1.00 117.51 ?  41  GLY A O   1 
ATOM   94    N N   . VAL A  1 12  ? 3.928   17.640  155.734 1.00 121.02 ?  42  VAL A N   1 
ATOM   95    C CA  . VAL A  1 12  ? 4.012   19.092  155.612 1.00 121.12 ?  42  VAL A CA  1 
ATOM   96    C C   . VAL A  1 12  ? 4.309   19.746  156.955 1.00 119.98 ?  42  VAL A C   1 
ATOM   97    O O   . VAL A  1 12  ? 3.813   19.296  157.998 1.00 120.24 ?  42  VAL A O   1 
ATOM   98    C CB  . VAL A  1 12  ? 2.722   19.672  155.007 1.00 123.86 ?  42  VAL A CB  1 
ATOM   99    C CG1 . VAL A  1 12  ? 2.555   19.188  153.586 1.00 124.99 ?  42  VAL A CG1 1 
ATOM   100   C CG2 . VAL A  1 12  ? 1.499   19.323  155.855 1.00 125.50 ?  42  VAL A CG2 1 
ATOM   101   N N   . PRO A  1 13  ? 5.131   20.789  156.973 1.00 129.56 ?  43  PRO A N   1 
ATOM   102   C CA  . PRO A  1 13  ? 5.418   21.498  158.226 1.00 128.28 ?  43  PRO A CA  1 
ATOM   103   C C   . PRO A  1 13  ? 4.207   22.260  158.742 1.00 136.03 ?  43  PRO A C   1 
ATOM   104   O O   . PRO A  1 13  ? 4.160   23.488  158.616 1.00 136.52 ?  43  PRO A O   1 
ATOM   105   C CB  . PRO A  1 13  ? 6.559   22.448  157.840 1.00 121.52 ?  43  PRO A CB  1 
ATOM   106   C CG  . PRO A  1 13  ? 7.152   21.861  156.599 1.00 118.32 ?  43  PRO A CG  1 
ATOM   107   C CD  . PRO A  1 13  ? 5.998   21.244  155.873 1.00 123.75 ?  43  PRO A CD  1 
ATOM   108   N N   . VAL A  1 14  ? 3.228   21.566  159.317 1.00 128.17 ?  44  VAL A N   1 
ATOM   109   C CA  . VAL A  1 14  ? 2.027   22.201  159.849 1.00 130.25 ?  44  VAL A CA  1 
ATOM   110   C C   . VAL A  1 14  ? 1.851   21.720  161.279 1.00 129.85 ?  44  VAL A C   1 
ATOM   111   O O   . VAL A  1 14  ? 1.713   20.515  161.520 1.00 130.03 ?  44  VAL A O   1 
ATOM   112   C CB  . VAL A  1 14  ? 0.777   21.872  159.013 1.00 135.31 ?  44  VAL A CB  1 
ATOM   113   C CG1 . VAL A  1 14  ? -0.478  22.371  159.707 1.00 143.24 ?  44  VAL A CG1 1 
ATOM   114   C CG2 . VAL A  1 14  ? 0.885   22.474  157.626 1.00 134.51 ?  44  VAL A CG2 1 
ATOM   115   N N   . TRP A  1 15  ? 1.852   22.658  162.221 1.00 136.11 ?  45  TRP A N   1 
ATOM   116   C CA  . TRP A  1 15  ? 1.684   22.336  163.624 1.00 137.39 ?  45  TRP A CA  1 
ATOM   117   C C   . TRP A  1 15  ? 0.676   23.275  164.261 1.00 143.74 ?  45  TRP A C   1 
ATOM   118   O O   . TRP A  1 15  ? 0.434   24.384  163.782 1.00 145.51 ?  45  TRP A O   1 
ATOM   119   C CB  . TRP A  1 15  ? 3.003   22.392  164.405 1.00 129.59 ?  45  TRP A CB  1 
ATOM   120   C CG  . TRP A  1 15  ? 3.600   23.739  164.511 1.00 126.74 ?  45  TRP A CG  1 
ATOM   121   C CD1 . TRP A  1 15  ? 3.215   24.748  165.345 1.00 129.83 ?  45  TRP A CD1 1 
ATOM   122   C CD2 . TRP A  1 15  ? 4.728   24.225  163.786 1.00 120.11 ?  45  TRP A CD2 1 
ATOM   123   N NE1 . TRP A  1 15  ? 4.022   25.842  165.166 1.00 125.69 ?  45  TRP A NE1 1 
ATOM   124   C CE2 . TRP A  1 15  ? 4.962   25.546  164.215 1.00 119.65 ?  45  TRP A CE2 1 
ATOM   125   C CE3 . TRP A  1 15  ? 5.560   23.674  162.806 1.00 114.55 ?  45  TRP A CE3 1 
ATOM   126   C CZ2 . TRP A  1 15  ? 5.994   26.326  163.698 1.00 113.90 ?  45  TRP A CZ2 1 
ATOM   127   C CZ3 . TRP A  1 15  ? 6.582   24.448  162.295 1.00 108.71 ?  45  TRP A CZ3 1 
ATOM   128   C CH2 . TRP A  1 15  ? 6.792   25.760  162.741 1.00 108.46 ?  45  TRP A CH2 1 
ATOM   129   N N   . LYS A  1 16  ? 0.081   22.813  165.357 1.00 128.08 ?  46  LYS A N   1 
ATOM   130   C CA  . LYS A  1 16  ? -0.838  23.645  166.111 1.00 130.50 ?  46  LYS A CA  1 
ATOM   131   C C   . LYS A  1 16  ? -0.530  23.457  167.590 1.00 128.98 ?  46  LYS A C   1 
ATOM   132   O O   . LYS A  1 16  ? -0.104  22.378  168.006 1.00 127.83 ?  46  LYS A O   1 
ATOM   133   C CB  . LYS A  1 16  ? -2.275  23.235  165.764 1.00 138.59 ?  46  LYS A CB  1 
ATOM   134   C CG  . LYS A  1 16  ? -2.676  23.693  164.367 1.00 141.41 ?  46  LYS A CG  1 
ATOM   135   C CD  . LYS A  1 16  ? -4.140  23.485  164.050 1.00 149.19 ?  46  LYS A CD  1 
ATOM   136   C CE  . LYS A  1 16  ? -4.467  24.072  162.685 1.00 150.52 ?  46  LYS A CE  1 
ATOM   137   N NZ  . LYS A  1 16  ? -4.164  25.531  162.569 1.00 147.77 1  46  LYS A NZ  1 
ATOM   138   N N   . ASP A  1 17  ? -0.735  24.507  168.383 1.00 130.14 ?  47  ASP A N   1 
ATOM   139   C CA  . ASP A  1 17  ? -0.451  24.417  169.814 1.00 128.99 ?  47  ASP A CA  1 
ATOM   140   C C   . ASP A  1 17  ? -1.347  23.387  170.495 1.00 133.29 ?  47  ASP A C   1 
ATOM   141   O O   . ASP A  1 17  ? -2.569  23.396  170.322 1.00 139.72 ?  47  ASP A O   1 
ATOM   142   C CB  . ASP A  1 17  ? -0.605  25.779  170.494 1.00 130.90 ?  47  ASP A CB  1 
ATOM   143   C CG  . ASP A  1 17  ? 0.323   26.835  169.914 1.00 126.25 ?  47  ASP A CG  1 
ATOM   144   O OD1 . ASP A  1 17  ? 0.550   26.823  168.685 1.00 123.95 ?  47  ASP A OD1 1 
ATOM   145   O OD2 . ASP A  1 17  ? 0.843   27.666  170.693 1.00 124.83 -1 47  ASP A OD2 1 
ATOM   146   N N   . ALA A  1 18  ? -0.738  22.510  171.293 1.00 134.42 ?  48  ALA A N   1 
ATOM   147   C CA  . ALA A  1 18  ? -1.487  21.488  172.016 1.00 135.60 ?  48  ALA A CA  1 
ATOM   148   C C   . ALA A  1 18  ? -0.682  21.080  173.246 1.00 134.18 ?  48  ALA A C   1 
ATOM   149   O O   . ALA A  1 18  ? 0.415   21.589  173.493 1.00 132.36 ?  48  ALA A O   1 
ATOM   150   C CB  . ALA A  1 18  ? -1.796  20.289  171.115 1.00 135.94 ?  48  ALA A CB  1 
ATOM   151   N N   . GLU A  1 19  ? -1.243  20.153  174.021 1.00 162.74 ?  49  GLU A N   1 
ATOM   152   C CA  . GLU A  1 19  ? -0.633  19.625  175.236 1.00 157.51 ?  49  GLU A CA  1 
ATOM   153   C C   . GLU A  1 19  ? -0.602  18.105  175.190 1.00 152.63 ?  49  GLU A C   1 
ATOM   154   O O   . GLU A  1 19  ? -1.590  17.472  174.806 1.00 155.82 ?  49  GLU A O   1 
ATOM   155   C CB  . GLU A  1 19  ? -1.370  20.112  176.484 1.00 166.30 ?  49  GLU A CB  1 
ATOM   156   C CG  . GLU A  1 19  ? -1.353  21.619  176.615 1.00 169.53 ?  49  GLU A CG  1 
ATOM   157   C CD  . GLU A  1 19  ? -2.709  22.199  176.938 1.00 182.80 ?  49  GLU A CD  1 
ATOM   158   O OE1 . GLU A  1 19  ? -3.698  21.434  176.990 1.00 189.87 ?  49  GLU A OE1 1 
ATOM   159   O OE2 . GLU A  1 19  ? -2.781  23.426  177.157 1.00 194.38 -1 49  GLU A OE2 1 
ATOM   160   N N   . THR A  1 20  ? 0.538   17.526  175.570 1.00 150.39 ?  50  THR A N   1 
ATOM   161   C CA  . THR A  1 20  ? 0.723   16.080  175.564 1.00 146.28 ?  50  THR A CA  1 
ATOM   162   C C   . THR A  1 20  ? 1.521   15.654  176.784 1.00 142.71 ?  50  THR A C   1 
ATOM   163   O O   . THR A  1 20  ? 1.897   16.466  177.636 1.00 144.73 ?  50  THR A O   1 
ATOM   164   C CB  . THR A  1 20  ? 1.472   15.597  174.321 1.00 143.02 ?  50  THR A CB  1 
ATOM   165   O OG1 . THR A  1 20  ? 1.571   14.166  174.343 1.00 142.54 ?  50  THR A OG1 1 
ATOM   166   C CG2 . THR A  1 20  ? 2.882   16.171  174.312 1.00 134.83 ?  50  THR A CG2 1 
ATOM   167   N N   . THR A  1 21  ? 1.772   14.353  176.849 1.00 140.07 ?  51  THR A N   1 
ATOM   168   C CA  . THR A  1 21  ? 2.516   13.740  177.937 1.00 138.92 ?  51  THR A CA  1 
ATOM   169   C C   . THR A  1 21  ? 3.998   13.688  177.578 1.00 135.34 ?  51  THR A C   1 
ATOM   170   O O   . THR A  1 21  ? 4.408   12.918  176.703 1.00 135.07 ?  51  THR A O   1 
ATOM   171   C CB  . THR A  1 21  ? 1.971   12.344  178.204 1.00 141.71 ?  51  THR A CB  1 
ATOM   172   O OG1 . THR A  1 21  ? 0.541   12.400  178.308 1.00 145.35 ?  51  THR A OG1 1 
ATOM   173   C CG2 . THR A  1 21  ? 2.542   11.823  179.458 1.00 141.07 ?  51  THR A CG2 1 
ATOM   174   N N   . LEU A  1 22  ? 4.796   14.503  178.261 1.00 137.17 ?  52  LEU A N   1 
ATOM   175   C CA  . LEU A  1 22  ? 6.232   14.588  178.038 1.00 133.84 ?  52  LEU A CA  1 
ATOM   176   C C   . LEU A  1 22  ? 6.962   13.557  178.889 1.00 133.51 ?  52  LEU A C   1 
ATOM   177   O O   . LEU A  1 22  ? 6.562   13.278  180.024 1.00 134.99 ?  52  LEU A O   1 
ATOM   178   C CB  . LEU A  1 22  ? 6.746   15.993  178.354 1.00 131.59 ?  52  LEU A CB  1 
ATOM   179   C CG  . LEU A  1 22  ? 6.061   17.117  177.572 1.00 132.07 ?  52  LEU A CG  1 
ATOM   180   C CD1 . LEU A  1 22  ? 6.579   18.477  178.009 1.00 130.18 ?  52  LEU A CD1 1 
ATOM   181   C CD2 . LEU A  1 22  ? 6.230   16.930  176.073 1.00 131.58 ?  52  LEU A CD2 1 
ATOM   182   N N   . PHE A  1 23  ? 8.031   12.989  178.341 1.00 131.63 ?  53  PHE A N   1 
ATOM   183   C CA  . PHE A  1 23  ? 8.857   12.057  179.095 1.00 131.44 ?  53  PHE A CA  1 
ATOM   184   C C   . PHE A  1 23  ? 10.197  12.700  179.447 1.00 129.79 ?  53  PHE A C   1 
ATOM   185   O O   . PHE A  1 23  ? 10.500  13.826  179.045 1.00 128.74 ?  53  PHE A O   1 
ATOM   186   C CB  . PHE A  1 23  ? 9.034   10.752  178.316 1.00 131.46 ?  53  PHE A CB  1 
ATOM   187   C CG  . PHE A  1 23  ? 9.703   10.915  176.979 1.00 129.92 ?  53  PHE A CG  1 
ATOM   188   C CD1 . PHE A  1 23  ? 8.955   11.215  175.854 1.00 130.14 ?  53  PHE A CD1 1 
ATOM   189   C CD2 . PHE A  1 23  ? 11.068  10.727  176.839 1.00 128.43 ?  53  PHE A CD2 1 
ATOM   190   C CE1 . PHE A  1 23  ? 9.555   11.348  174.618 1.00 128.87 ?  53  PHE A CE1 1 
ATOM   191   C CE2 . PHE A  1 23  ? 11.675  10.856  175.602 1.00 127.12 ?  53  PHE A CE2 1 
ATOM   192   C CZ  . PHE A  1 23  ? 10.915  11.162  174.490 1.00 127.34 ?  53  PHE A CZ  1 
ATOM   193   N N   . CYS A  1 24  ? 11.012  11.959  180.196 1.00 162.28 ?  54  CYS A N   1 
ATOM   194   C CA  . CYS A  1 24  ? 12.246  12.488  180.762 1.00 159.78 ?  54  CYS A CA  1 
ATOM   195   C C   . CYS A  1 24  ? 13.473  12.049  179.974 1.00 158.24 ?  54  CYS A C   1 
ATOM   196   O O   . CYS A  1 24  ? 13.409  11.251  179.036 1.00 159.17 ?  54  CYS A O   1 
ATOM   197   C CB  . CYS A  1 24  ? 12.415  12.059  182.227 1.00 167.61 ?  54  CYS A CB  1 
ATOM   198   S SG  . CYS A  1 24  ? 12.780  10.300  182.442 1.00 189.22 ?  54  CYS A SG  1 
ATOM   199   N N   . ALA A  1 25  ? 14.610  12.604  180.387 1.00 171.58 ?  55  ALA A N   1 
ATOM   200   C CA  . ALA A  1 25  ? 15.923  12.276  179.856 1.00 170.16 ?  55  ALA A CA  1 
ATOM   201   C C   . ALA A  1 25  ? 16.968  12.833  180.812 1.00 168.48 ?  55  ALA A C   1 
ATOM   202   O O   . ALA A  1 25  ? 16.850  13.981  181.251 1.00 167.32 ?  55  ALA A O   1 
ATOM   203   C CB  . ALA A  1 25  ? 16.104  12.839  178.446 1.00 168.72 ?  55  ALA A CB  1 
ATOM   204   N N   . SER A  1 26  ? 17.981  12.046  181.159 1.00 192.34 ?  56  SER A N   1 
ATOM   205   C CA  . SER A  1 26  ? 18.941  12.527  182.140 1.00 194.39 ?  56  SER A CA  1 
ATOM   206   C C   . SER A  1 26  ? 20.302  11.868  181.933 1.00 204.16 ?  56  SER A C   1 
ATOM   207   O O   . SER A  1 26  ? 20.820  11.154  182.793 1.00 199.96 ?  56  SER A O   1 
ATOM   208   C CB  . SER A  1 26  ? 18.420  12.267  183.553 1.00 191.83 ?  56  SER A CB  1 
ATOM   209   O OG  . SER A  1 26  ? 18.093  10.897  183.729 1.00 195.77 ?  56  SER A OG  1 
ATOM   210   N N   . ASP A  1 27  ? 20.894  12.122  180.761 1.00 209.86 ?  57  ASP A N   1 
ATOM   211   C CA  . ASP A  1 27  ? 22.250  11.676  180.467 1.00 214.05 ?  57  ASP A CA  1 
ATOM   212   C C   . ASP A  1 27  ? 22.445  10.185  180.706 1.00 216.83 ?  57  ASP A C   1 
ATOM   213   O O   . ASP A  1 27  ? 21.485  9.407   180.746 1.00 214.96 ?  57  ASP A O   1 
ATOM   214   C CB  . ASP A  1 27  ? 23.253  12.478  181.298 1.00 214.43 ?  57  ASP A CB  1 
ATOM   215   C CG  . ASP A  1 27  ? 23.207  13.961  180.988 1.00 209.21 ?  57  ASP A CG  1 
ATOM   216   O OD1 . ASP A  1 27  ? 23.031  14.311  179.802 1.00 208.78 ?  57  ASP A OD1 1 
ATOM   217   O OD2 . ASP A  1 27  ? 23.339  14.775  181.926 1.00 209.03 -1 57  ASP A OD2 1 
ATOM   218   N N   . ALA A  1 28  ? 23.707  9.801   180.860 1.00 228.35 ?  58  ALA A N   1 
ATOM   219   C CA  . ALA A  1 28  ? 24.099  8.435   181.160 1.00 233.27 ?  58  ALA A CA  1 
ATOM   220   C C   . ALA A  1 28  ? 25.021  8.396   182.363 1.00 238.61 ?  58  ALA A C   1 
ATOM   221   O O   . ALA A  1 28  ? 25.124  7.346   183.009 1.00 245.61 ?  58  ALA A O   1 
ATOM   222   C CB  . ALA A  1 28  ? 24.795  7.781   179.955 1.00 227.46 ?  58  ALA A CB  1 
ATOM   223   N N   . LYS A  1 29  ? 25.681  9.513   182.691 1.00 241.29 ?  59  LYS A N   1 
ATOM   224   C CA  . LYS A  1 29  ? 26.518  9.612   183.879 1.00 242.17 ?  59  LYS A CA  1 
ATOM   225   C C   . LYS A  1 29  ? 25.655  9.861   185.107 1.00 244.99 ?  59  LYS A C   1 
ATOM   226   O O   . LYS A  1 29  ? 26.035  9.489   186.223 1.00 246.90 ?  59  LYS A O   1 
ATOM   227   C CB  . LYS A  1 29  ? 27.587  10.699  183.752 1.00 236.38 ?  59  LYS A CB  1 
ATOM   228   C CG  . LYS A  1 29  ? 28.474  10.738  184.999 1.00 233.53 ?  59  LYS A CG  1 
ATOM   229   C CD  . LYS A  1 29  ? 29.811  11.407  184.824 1.00 222.33 ?  59  LYS A CD  1 
ATOM   230   C CE  . LYS A  1 29  ? 30.890  10.467  185.332 1.00 222.19 ?  59  LYS A CE  1 
ATOM   231   N NZ  . LYS A  1 29  ? 32.049  11.193  185.909 1.00 213.81 1  59  LYS A NZ  1 
ATOM   232   N N   . ALA A  1 30  ? 24.476  10.457  184.909 1.00 243.88 ?  60  ALA A N   1 
ATOM   233   C CA  . ALA A  1 30  ? 23.588  10.720  186.032 1.00 244.01 ?  60  ALA A CA  1 
ATOM   234   C C   . ALA A  1 30  ? 23.065  9.411   186.595 1.00 251.68 ?  60  ALA A C   1 
ATOM   235   O O   . ALA A  1 30  ? 22.692  9.342   187.772 1.00 254.34 ?  60  ALA A O   1 
ATOM   236   C CB  . ALA A  1 30  ? 22.436  11.627  185.599 1.00 240.01 ?  60  ALA A CB  1 
ATOM   237   N N   . TYR A  1 31  ? 23.016  8.376   185.761 1.00 244.71 ?  61  TYR A N   1 
ATOM   238   C CA  . TYR A  1 31  ? 22.581  7.060   186.192 1.00 248.23 ?  61  TYR A CA  1 
ATOM   239   C C   . TYR A  1 31  ? 23.712  6.335   186.924 1.00 250.45 ?  61  TYR A C   1 
ATOM   240   O O   . TYR A  1 31  ? 23.446  5.388   187.674 1.00 254.35 ?  61  TYR A O   1 
ATOM   241   C CB  . TYR A  1 31  ? 22.099  6.262   184.975 1.00 250.98 ?  61  TYR A CB  1 
ATOM   242   C CG  . TYR A  1 31  ? 21.521  4.898   185.276 1.00 256.65 ?  61  TYR A CG  1 
ATOM   243   C CD1 . TYR A  1 31  ? 20.217  4.771   185.735 1.00 257.00 ?  61  TYR A CD1 1 
ATOM   244   C CD2 . TYR A  1 31  ? 22.260  3.739   185.072 1.00 260.15 ?  61  TYR A CD2 1 
ATOM   245   C CE1 . TYR A  1 31  ? 19.669  3.532   186.004 1.00 260.20 ?  61  TYR A CE1 1 
ATOM   246   C CE2 . TYR A  1 31  ? 21.718  2.492   185.339 1.00 264.42 ?  61  TYR A CE2 1 
ATOM   247   C CZ  . TYR A  1 31  ? 20.423  2.396   185.805 1.00 265.00 ?  61  TYR A CZ  1 
ATOM   248   O OH  . TYR A  1 31  ? 19.881  1.159   186.071 1.00 267.37 ?  61  TYR A OH  1 
ATOM   249   N N   . GLU A  1 32  ? 24.966  6.783   186.728 1.00 253.97 ?  62  GLU A N   1 
ATOM   250   C CA  . GLU A  1 32  ? 26.168  6.223   187.351 1.00 252.96 ?  62  GLU A CA  1 
ATOM   251   C C   . GLU A  1 32  ? 26.402  6.723   188.772 1.00 250.95 ?  62  GLU A C   1 
ATOM   252   O O   . GLU A  1 32  ? 27.312  6.231   189.447 1.00 251.17 ?  62  GLU A O   1 
ATOM   253   C CB  . GLU A  1 32  ? 27.408  6.524   186.507 1.00 249.38 ?  62  GLU A CB  1 
ATOM   254   C CG  . GLU A  1 32  ? 27.334  6.007   185.087 1.00 249.50 ?  62  GLU A CG  1 
ATOM   255   C CD  . GLU A  1 32  ? 28.570  6.354   184.290 1.00 245.93 ?  62  GLU A CD  1 
ATOM   256   O OE1 . GLU A  1 32  ? 29.566  6.787   184.907 1.00 243.70 ?  62  GLU A OE1 1 
ATOM   257   O OE2 . GLU A  1 32  ? 28.548  6.190   183.053 1.00 247.49 -1 62  GLU A OE2 1 
ATOM   258   N N   . THR A  1 33  ? 25.608  7.685   189.231 1.00 247.06 ?  63  THR A N   1 
ATOM   259   C CA  . THR A  1 33  ? 25.703  8.206   190.588 1.00 247.03 ?  63  THR A CA  1 
ATOM   260   C C   . THR A  1 33  ? 25.196  7.166   191.571 1.00 246.98 ?  63  THR A C   1 
ATOM   261   O O   . THR A  1 33  ? 25.536  7.215   192.758 1.00 246.37 ?  63  THR A O   1 
ATOM   262   C CB  . THR A  1 33  ? 24.926  9.515   190.737 1.00 243.41 ?  63  THR A CB  1 
ATOM   263   O OG1 . THR A  1 33  ? 25.209  10.366  189.621 1.00 241.54 ?  63  THR A OG1 1 
ATOM   264   C CG2 . THR A  1 33  ? 25.335  10.238  192.023 1.00 241.27 ?  63  THR A CG2 1 
ATOM   265   N N   . GLU A  1 34  ? 24.431  6.202   191.056 1.00 242.76 ?  64  GLU A N   1 
ATOM   266   C CA  . GLU A  1 34  ? 23.762  5.115   191.751 1.00 244.06 ?  64  GLU A CA  1 
ATOM   267   C C   . GLU A  1 34  ? 23.238  5.551   193.103 1.00 242.24 ?  64  GLU A C   1 
ATOM   268   O O   . GLU A  1 34  ? 22.318  6.370   193.194 1.00 238.27 ?  64  GLU A O   1 
ATOM   269   C CB  . GLU A  1 34  ? 24.788  4.015   192.069 1.00 248.48 ?  64  GLU A CB  1 
ATOM   270   C CG  . GLU A  1 34  ? 25.327  3.115   190.984 1.00 249.26 ?  64  GLU A CG  1 
ATOM   271   C CD  . GLU A  1 34  ? 26.563  2.364   191.488 1.00 250.60 ?  64  GLU A CD  1 
ATOM   272   O OE1 . GLU A  1 34  ? 27.518  3.033   191.942 1.00 246.19 ?  64  GLU A OE1 1 
ATOM   273   O OE2 . GLU A  1 34  ? 26.582  1.116   191.444 1.00 256.20 -1 64  GLU A OE2 1 
ATOM   274   N N   . LYS A  1 35  ? 23.837  4.997   194.147 1.00 246.92 ?  65  LYS A N   1 
ATOM   275   C CA  . LYS A  1 35  ? 23.438  5.230   195.525 1.00 246.17 ?  65  LYS A CA  1 
ATOM   276   C C   . LYS A  1 35  ? 21.957  4.892   195.723 1.00 250.08 ?  65  LYS A C   1 
ATOM   277   O O   . LYS A  1 35  ? 21.210  5.665   196.326 1.00 251.65 ?  65  LYS A O   1 
ATOM   278   C CB  . LYS A  1 35  ? 23.714  6.681   195.918 1.00 239.76 ?  65  LYS A CB  1 
ATOM   279   C CG  . LYS A  1 35  ? 25.182  7.071   195.968 1.00 237.70 ?  65  LYS A CG  1 
ATOM   280   C CD  . LYS A  1 35  ? 26.073  6.174   196.801 1.00 239.03 ?  65  LYS A CD  1 
ATOM   281   C CE  . LYS A  1 35  ? 27.531  6.587   196.583 1.00 235.40 ?  65  LYS A CE  1 
ATOM   282   N NZ  . LYS A  1 35  ? 28.429  5.455   196.236 1.00 240.31 1  65  LYS A NZ  1 
ATOM   283   N N   . HIS A  1 36  ? 21.524  3.730   195.215 1.00 248.65 ?  66  HIS A N   1 
ATOM   284   C CA  . HIS A  1 36  ? 20.129  3.293   195.383 1.00 251.01 ?  66  HIS A CA  1 
ATOM   285   C C   . HIS A  1 36  ? 19.110  4.325   194.890 1.00 243.56 ?  66  HIS A C   1 
ATOM   286   O O   . HIS A  1 36  ? 18.267  4.813   195.648 1.00 235.52 ?  66  HIS A O   1 
ATOM   287   C CB  . HIS A  1 36  ? 19.828  2.809   196.800 1.00 251.99 ?  66  HIS A CB  1 
ATOM   288   C CG  . HIS A  1 36  ? 20.551  1.548   197.157 1.00 258.19 ?  66  HIS A CG  1 
ATOM   289   N ND1 . HIS A  1 36  ? 20.804  1.167   198.456 1.00 262.39 ?  66  HIS A ND1 1 
ATOM   290   C CD2 . HIS A  1 36  ? 21.019  0.545   196.374 1.00 260.44 ?  66  HIS A CD2 1 
ATOM   291   C CE1 . HIS A  1 36  ? 21.423  -0.000  198.458 1.00 267.39 ?  66  HIS A CE1 1 
ATOM   292   N NE2 . HIS A  1 36  ? 21.566  -0.399  197.207 1.00 265.81 ?  66  HIS A NE2 1 
ATOM   293   N N   . ASN A  1 37  ? 19.224  4.671   193.603 1.00 248.50 ?  67  ASN A N   1 
ATOM   294   C CA  . ASN A  1 37  ? 18.301  5.618   192.986 1.00 240.34 ?  67  ASN A CA  1 
ATOM   295   C C   . ASN A  1 37  ? 18.287  6.973   193.664 1.00 231.70 ?  67  ASN A C   1 
ATOM   296   O O   . ASN A  1 37  ? 17.488  7.214   194.575 1.00 225.12 ?  67  ASN A O   1 
ATOM   297   C CB  . ASN A  1 37  ? 16.871  5.058   193.041 1.00 240.53 ?  67  ASN A CB  1 
ATOM   298   C CG  . ASN A  1 37  ? 16.103  5.257   191.766 1.00 238.82 ?  67  ASN A CG  1 
ATOM   299   O OD1 . ASN A  1 37  ? 16.561  5.933   190.849 1.00 235.45 ?  67  ASN A OD1 1 
ATOM   300   N ND2 . ASN A  1 37  ? 14.882  4.728   191.732 1.00 240.15 ?  67  ASN A ND2 1 
ATOM   301   N N   . VAL A  1 38  ? 19.159  7.871   193.222 1.00 227.12 ?  68  VAL A N   1 
ATOM   302   C CA  . VAL A  1 38  ? 19.154  9.208   193.785 1.00 216.43 ?  68  VAL A CA  1 
ATOM   303   C C   . VAL A  1 38  ? 18.089  10.006  193.049 1.00 212.89 ?  68  VAL A C   1 
ATOM   304   O O   . VAL A  1 38  ? 18.025  9.992   191.814 1.00 212.47 ?  68  VAL A O   1 
ATOM   305   C CB  . VAL A  1 38  ? 20.543  9.853   193.645 1.00 215.76 ?  68  VAL A CB  1 
ATOM   306   C CG1 . VAL A  1 38  ? 21.506  9.240   194.646 1.00 216.93 ?  68  VAL A CG1 1 
ATOM   307   C CG2 . VAL A  1 38  ? 21.076  9.683   192.227 1.00 215.96 ?  68  VAL A CG2 1 
ATOM   308   N N   . TRP A  1 39  ? 17.236  10.686  193.810 1.00 195.17 ?  69  TRP A N   1 
ATOM   309   C CA  . TRP A  1 39  ? 16.158  11.491  193.251 1.00 194.28 ?  69  TRP A CA  1 
ATOM   310   C C   . TRP A  1 39  ? 15.216  10.677  192.366 1.00 194.72 ?  69  TRP A C   1 
ATOM   311   O O   . TRP A  1 39  ? 14.349  9.958   192.873 1.00 190.85 ?  69  TRP A O   1 
ATOM   312   C CB  . TRP A  1 39  ? 16.704  12.714  192.517 1.00 192.87 ?  69  TRP A CB  1 
ATOM   313   C CG  . TRP A  1 39  ? 15.641  13.736  192.236 1.00 196.63 ?  69  TRP A CG  1 
ATOM   314   C CD1 . TRP A  1 39  ? 15.370  14.316  191.034 1.00 191.62 ?  69  TRP A CD1 1 
ATOM   315   C CD2 . TRP A  1 39  ? 14.640  14.223  193.150 1.00 200.64 ?  69  TRP A CD2 1 
ATOM   316   N NE1 . TRP A  1 39  ? 14.308  15.179  191.151 1.00 194.49 ?  69  TRP A NE1 1 
ATOM   317   C CE2 . TRP A  1 39  ? 13.836  15.134  192.436 1.00 199.32 ?  69  TRP A CE2 1 
ATOM   318   C CE3 . TRP A  1 39  ? 14.361  13.995  194.505 1.00 197.54 ?  69  TRP A CE3 1 
ATOM   319   C CZ2 . TRP A  1 39  ? 12.774  15.816  193.028 1.00 197.76 ?  69  TRP A CZ2 1 
ATOM   320   C CZ3 . TRP A  1 39  ? 13.304  14.672  195.090 1.00 192.15 ?  69  TRP A CZ3 1 
ATOM   321   C CH2 . TRP A  1 39  ? 12.524  15.572  194.352 1.00 197.69 ?  69  TRP A CH2 1 
ATOM   322   N N   . ALA A  1 40  ? 15.384  10.779  191.041 1.00 180.59 ?  70  ALA A N   1 
ATOM   323   C CA  . ALA A  1 40  ? 14.451  10.172  190.094 1.00 184.99 ?  70  ALA A CA  1 
ATOM   324   C C   . ALA A  1 40  ? 15.046  9.162   189.124 1.00 192.35 ?  70  ALA A C   1 
ATOM   325   O O   . ALA A  1 40  ? 14.413  8.137   188.858 1.00 197.78 ?  70  ALA A O   1 
ATOM   326   C CB  . ALA A  1 40  ? 13.781  11.271  189.264 1.00 180.13 ?  70  ALA A CB  1 
ATOM   327   N N   . THR A  1 41  ? 16.233  9.424   188.577 1.00 209.65 ?  71  THR A N   1 
ATOM   328   C CA  . THR A  1 41  ? 16.813  8.606   187.511 1.00 213.52 ?  71  THR A CA  1 
ATOM   329   C C   . THR A  1 41  ? 16.924  7.116   187.808 1.00 216.93 ?  71  THR A C   1 
ATOM   330   O O   . THR A  1 41  ? 17.942  6.651   188.332 1.00 219.99 ?  71  THR A O   1 
ATOM   331   C CB  . THR A  1 41  ? 18.197  9.128   187.124 1.00 213.21 ?  71  THR A CB  1 
ATOM   332   O OG1 . THR A  1 41  ? 18.135  10.545  186.932 1.00 214.35 ?  71  THR A OG1 1 
ATOM   333   C CG2 . THR A  1 41  ? 18.661  8.475   185.820 1.00 213.16 ?  71  THR A CG2 1 
ATOM   334   N N   . HIS A  1 42  ? 15.874  6.366   187.477 1.00 230.20 ?  72  HIS A N   1 
ATOM   335   C CA  . HIS A  1 42  ? 15.873  4.915   187.613 1.00 239.98 ?  72  HIS A CA  1 
ATOM   336   C C   . HIS A  1 42  ? 15.568  4.294   186.256 1.00 242.49 ?  72  HIS A C   1 
ATOM   337   O O   . HIS A  1 42  ? 16.418  3.591   185.699 1.00 247.16 ?  72  HIS A O   1 
ATOM   338   C CB  . HIS A  1 42  ? 14.879  4.445   188.678 1.00 245.11 ?  72  HIS A CB  1 
ATOM   339   C CG  . HIS A  1 42  ? 14.959  2.978   188.956 1.00 250.82 ?  72  HIS A CG  1 
ATOM   340   N ND1 . HIS A  1 42  ? 14.400  2.031   188.127 1.00 258.83 ?  72  HIS A ND1 1 
ATOM   341   C CD2 . HIS A  1 42  ? 15.541  2.294   189.972 1.00 253.20 ?  72  HIS A CD2 1 
ATOM   342   C CE1 . HIS A  1 42  ? 14.641  0.826   188.615 1.00 263.77 ?  72  HIS A CE1 1 
ATOM   343   N NE2 . HIS A  1 42  ? 15.326  0.958   189.737 1.00 260.95 ?  72  HIS A NE2 1 
ATOM   344   N N   . ALA A  1 43  ? 14.381  4.541   185.698 1.00 218.19 ?  73  ALA A N   1 
ATOM   345   C CA  . ALA A  1 43  ? 14.016  4.052   184.375 1.00 212.70 ?  73  ALA A CA  1 
ATOM   346   C C   . ALA A  1 43  ? 13.881  5.223   183.404 1.00 208.99 ?  73  ALA A C   1 
ATOM   347   O O   . ALA A  1 43  ? 13.053  5.197   182.490 1.00 210.46 ?  73  ALA A O   1 
ATOM   348   C CB  . ALA A  1 43  ? 12.726  3.233   184.410 1.00 216.28 ?  73  ALA A CB  1 
ATOM   349   N N   . CYS A  1 44  ? 14.691  6.265   183.605 1.00 202.04 ?  74  CYS A N   1 
ATOM   350   C CA  . CYS A  1 44  ? 14.646  7.440   182.745 1.00 198.29 ?  74  CYS A CA  1 
ATOM   351   C C   . CYS A  1 44  ? 15.502  7.188   181.505 1.00 192.26 ?  74  CYS A C   1 
ATOM   352   O O   . CYS A  1 44  ? 16.569  6.572   181.583 1.00 192.53 ?  74  CYS A O   1 
ATOM   353   C CB  . CYS A  1 44  ? 15.114  8.683   183.493 1.00 194.30 ?  74  CYS A CB  1 
ATOM   354   S SG  . CYS A  1 44  ? 14.814  10.199  182.563 1.00 193.44 ?  74  CYS A SG  1 
ATOM   355   N N   . VAL A  1 45  ? 15.031  7.677   180.367 1.00 183.16 ?  75  VAL A N   1 
ATOM   356   C CA  . VAL A  1 45  ? 15.696  7.462   179.071 1.00 182.42 ?  75  VAL A CA  1 
ATOM   357   C C   . VAL A  1 45  ? 17.022  8.218   178.984 1.00 179.54 ?  75  VAL A C   1 
ATOM   358   O O   . VAL A  1 45  ? 17.072  9.425   179.281 1.00 177.41 ?  75  VAL A O   1 
ATOM   359   C CB  . VAL A  1 45  ? 14.766  7.873   177.933 1.00 182.54 ?  75  VAL A CB  1 
ATOM   360   C CG1 . VAL A  1 45  ? 15.455  7.679   176.585 1.00 181.89 ?  75  VAL A CG1 1 
ATOM   361   C CG2 . VAL A  1 45  ? 13.468  7.082   178.010 1.00 185.75 ?  75  VAL A CG2 1 
ATOM   362   N N   . PRO A  1 46  ? 18.116  7.541   178.624 1.00 190.22 ?  76  PRO A N   1 
ATOM   363   C CA  . PRO A  1 46  ? 19.404  8.223   178.421 1.00 185.59 ?  76  PRO A CA  1 
ATOM   364   C C   . PRO A  1 46  ? 19.311  9.294   177.335 1.00 182.08 ?  76  PRO A C   1 
ATOM   365   O O   . PRO A  1 46  ? 18.703  9.086   176.282 1.00 181.94 ?  76  PRO A O   1 
ATOM   366   C CB  . PRO A  1 46  ? 20.350  7.084   178.021 1.00 188.58 ?  76  PRO A CB  1 
ATOM   367   C CG  . PRO A  1 46  ? 19.727  5.859   178.617 1.00 195.67 ?  76  PRO A CG  1 
ATOM   368   C CD  . PRO A  1 46  ? 18.244  6.077   178.519 1.00 197.67 ?  76  PRO A CD  1 
ATOM   369   N N   . THR A  1 47  ? 19.930  10.442  177.600 1.00 192.94 ?  77  THR A N   1 
ATOM   370   C CA  . THR A  1 47  ? 19.904  11.572  176.675 1.00 193.52 ?  77  THR A CA  1 
ATOM   371   C C   . THR A  1 47  ? 20.660  11.277  175.382 1.00 196.21 ?  77  THR A C   1 
ATOM   372   O O   . THR A  1 47  ? 21.706  10.623  175.388 1.00 197.62 ?  77  THR A O   1 
ATOM   373   C CB  . THR A  1 47  ? 20.505  12.813  177.334 1.00 192.25 ?  77  THR A CB  1 
ATOM   374   O OG1 . THR A  1 47  ? 19.886  13.024  178.608 1.00 189.83 ?  77  THR A OG1 1 
ATOM   375   C CG2 . THR A  1 47  ? 20.300  14.046  176.455 1.00 188.02 ?  77  THR A CG2 1 
ATOM   376   N N   . ASP A  1 48  ? 20.100  11.750  174.267 1.00 210.54 ?  78  ASP A N   1 
ATOM   377   C CA  . ASP A  1 48  ? 20.710  11.618  172.947 1.00 214.77 ?  78  ASP A CA  1 
ATOM   378   C C   . ASP A  1 48  ? 22.097  12.261  172.956 1.00 213.58 ?  78  ASP A C   1 
ATOM   379   O O   . ASP A  1 48  ? 22.219  13.457  173.268 1.00 210.12 ?  78  ASP A O   1 
ATOM   380   C CB  . ASP A  1 48  ? 19.813  12.270  171.888 1.00 212.99 ?  78  ASP A CB  1 
ATOM   381   C CG  . ASP A  1 48  ? 20.134  11.812  170.465 1.00 211.64 ?  78  ASP A CG  1 
ATOM   382   O OD1 . ASP A  1 48  ? 21.324  11.629  170.135 1.00 212.09 ?  78  ASP A OD1 1 
ATOM   383   O OD2 . ASP A  1 48  ? 19.184  11.636  169.671 1.00 209.42 -1 78  ASP A OD2 1 
ATOM   384   N N   . PRO A  1 49  ? 23.156  11.510  172.633 1.00 214.27 ?  79  PRO A N   1 
ATOM   385   C CA  . PRO A  1 49  ? 24.525  12.070  172.642 1.00 211.87 ?  79  PRO A CA  1 
ATOM   386   C C   . PRO A  1 49  ? 24.749  13.344  171.835 1.00 210.06 ?  79  PRO A C   1 
ATOM   387   O O   . PRO A  1 49  ? 25.500  14.218  172.286 1.00 207.73 ?  79  PRO A O   1 
ATOM   388   C CB  . PRO A  1 49  ? 25.361  10.911  172.080 1.00 214.18 ?  79  PRO A CB  1 
ATOM   389   C CG  . PRO A  1 49  ? 24.598  9.684   172.454 1.00 215.27 ?  79  PRO A CG  1 
ATOM   390   C CD  . PRO A  1 49  ? 23.148  10.064  172.347 1.00 217.08 ?  79  PRO A CD  1 
ATOM   391   N N   . ASN A  1 50  ? 24.126  13.483  170.663 1.00 211.55 ?  80  ASN A N   1 
ATOM   392   C CA  . ASN A  1 50  ? 24.264  14.662  169.806 1.00 210.22 ?  80  ASN A CA  1 
ATOM   393   C C   . ASN A  1 50  ? 22.891  15.271  169.552 1.00 207.75 ?  80  ASN A C   1 
ATOM   394   O O   . ASN A  1 50  ? 22.258  14.997  168.520 1.00 209.70 ?  80  ASN A O   1 
ATOM   395   C CB  . ASN A  1 50  ? 24.953  14.340  168.477 1.00 213.87 ?  80  ASN A CB  1 
ATOM   396   C CG  . ASN A  1 50  ? 26.375  13.826  168.648 1.00 219.29 ?  80  ASN A CG  1 
ATOM   397   O OD1 . ASN A  1 50  ? 26.680  13.079  169.578 1.00 223.61 ?  80  ASN A OD1 1 
ATOM   398   N ND2 . ASN A  1 50  ? 27.260  14.248  167.751 1.00 220.27 ?  80  ASN A ND2 1 
ATOM   399   N N   . PRO A  1 51  ? 22.388  16.083  170.483 1.00 199.07 ?  81  PRO A N   1 
ATOM   400   C CA  . PRO A  1 51  ? 21.069  16.687  170.286 1.00 195.10 ?  81  PRO A CA  1 
ATOM   401   C C   . PRO A  1 51  ? 21.106  17.582  169.057 1.00 192.39 ?  81  PRO A C   1 
ATOM   402   O O   . PRO A  1 51  ? 22.135  18.169  168.716 1.00 193.00 ?  81  PRO A O   1 
ATOM   403   C CB  . PRO A  1 51  ? 20.845  17.488  171.575 1.00 192.79 ?  81  PRO A CB  1 
ATOM   404   C CG  . PRO A  1 51  ? 21.807  16.882  172.578 1.00 196.55 ?  81  PRO A CG  1 
ATOM   405   C CD  . PRO A  1 51  ? 22.992  16.467  171.769 1.00 196.60 ?  81  PRO A CD  1 
ATOM   406   N N   . GLN A  1 52  ? 19.961  17.683  168.393 1.00 193.16 ?  82  GLN A N   1 
ATOM   407   C CA  . GLN A  1 52  ? 19.818  18.467  167.175 1.00 188.03 ?  82  GLN A CA  1 
ATOM   408   C C   . GLN A  1 52  ? 18.874  19.644  167.364 1.00 182.46 ?  82  GLN A C   1 
ATOM   409   O O   . GLN A  1 52  ? 17.793  19.494  167.944 1.00 180.04 ?  82  GLN A O   1 
ATOM   410   C CB  . GLN A  1 52  ? 19.322  17.582  166.026 1.00 189.81 ?  82  GLN A CB  1 
ATOM   411   C CG  . GLN A  1 52  ? 20.314  16.511  165.597 1.00 192.00 ?  82  GLN A CG  1 
ATOM   412   C CD  . GLN A  1 52  ? 21.564  17.095  164.973 1.00 187.53 ?  82  GLN A CD  1 
ATOM   413   O OE1 . GLN A  1 52  ? 21.561  18.231  164.497 1.00 183.78 ?  82  GLN A OE1 1 
ATOM   414   N NE2 . GLN A  1 52  ? 22.644  16.323  164.976 1.00 186.51 ?  82  GLN A NE2 1 
ATOM   415   N N   . GLU A  1 53  ? 19.295  20.813  166.870 1.00 169.84 ?  83  GLU A N   1 
ATOM   416   C CA  . GLU A  1 53  ? 18.511  22.043  166.911 1.00 168.97 ?  83  GLU A CA  1 
ATOM   417   C C   . GLU A  1 53  ? 18.385  22.548  165.485 1.00 169.09 ?  83  GLU A C   1 
ATOM   418   O O   . GLU A  1 53  ? 19.362  23.039  164.909 1.00 167.74 ?  83  GLU A O   1 
ATOM   419   C CB  . GLU A  1 53  ? 19.155  23.161  167.737 1.00 167.49 ?  83  GLU A CB  1 
ATOM   420   C CG  . GLU A  1 53  ? 19.139  23.059  169.230 1.00 170.87 ?  83  GLU A CG  1 
ATOM   421   C CD  . GLU A  1 53  ? 19.873  24.223  169.860 1.00 175.91 ?  83  GLU A CD  1 
ATOM   422   O OE1 . GLU A  1 53  ? 19.876  25.306  169.239 1.00 171.77 ?  83  GLU A OE1 1 
ATOM   423   O OE2 . GLU A  1 53  ? 20.410  24.078  170.978 1.00 181.69 -1 83  GLU A OE2 1 
ATOM   424   N N   . ILE A  1 54  ? 17.190  22.430  164.919 1.00 161.12 ?  84  ILE A N   1 
ATOM   425   C CA  . ILE A  1 54  ? 16.954  22.850  163.546 1.00 161.60 ?  84  ILE A CA  1 
ATOM   426   C C   . ILE A  1 54  ? 16.437  24.271  163.684 1.00 161.78 ?  84  ILE A C   1 
ATOM   427   O O   . ILE A  1 54  ? 15.351  24.494  164.228 1.00 163.31 ?  84  ILE A O   1 
ATOM   428   C CB  . ILE A  1 54  ? 15.938  21.940  162.830 1.00 164.41 ?  84  ILE A CB  1 
ATOM   429   C CG1 . ILE A  1 54  ? 16.500  20.528  162.606 1.00 165.22 ?  84  ILE A CG1 1 
ATOM   430   C CG2 . ILE A  1 54  ? 15.492  22.553  161.497 1.00 166.94 ?  84  ILE A CG2 1 
ATOM   431   C CD1 . ILE A  1 54  ? 16.271  19.564  163.771 1.00 164.65 ?  84  ILE A CD1 1 
ATOM   432   N N   . HIS A  1 55  ? 17.201  25.233  163.180 1.00 164.70 ?  85  HIS A N   1 
ATOM   433   C CA  . HIS A  1 55  ? 16.793  26.628  163.245 1.00 166.77 ?  85  HIS A CA  1 
ATOM   434   C C   . HIS A  1 55  ? 15.760  26.875  162.158 1.00 171.81 ?  85  HIS A C   1 
ATOM   435   O O   . HIS A  1 55  ? 16.078  26.832  160.966 1.00 173.67 ?  85  HIS A O   1 
ATOM   436   C CB  . HIS A  1 55  ? 18.005  27.538  163.098 1.00 166.12 ?  85  HIS A CB  1 
ATOM   437   C CG  . HIS A  1 55  ? 17.670  28.993  163.096 1.00 170.69 ?  85  HIS A CG  1 
ATOM   438   N ND1 . HIS A  1 55  ? 16.949  29.585  164.110 1.00 171.55 ?  85  HIS A ND1 1 
ATOM   439   C CD2 . HIS A  1 55  ? 17.961  29.979  162.215 1.00 170.64 ?  85  HIS A CD2 1 
ATOM   440   C CE1 . HIS A  1 55  ? 16.806  30.872  163.852 1.00 173.04 ?  85  HIS A CE1 1 
ATOM   441   N NE2 . HIS A  1 55  ? 17.411  31.137  162.707 1.00 173.05 ?  85  HIS A NE2 1 
ATOM   442   N N   . LEU A  1 56  ? 14.522  27.132  162.568 1.00 152.04 ?  86  LEU A N   1 
ATOM   443   C CA  . LEU A  1 56  ? 13.435  27.353  161.621 1.00 159.91 ?  86  LEU A CA  1 
ATOM   444   C C   . LEU A  1 56  ? 13.514  28.773  161.074 1.00 166.27 ?  86  LEU A C   1 
ATOM   445   O O   . LEU A  1 56  ? 13.030  29.730  161.681 1.00 163.44 ?  86  LEU A O   1 
ATOM   446   C CB  . LEU A  1 56  ? 12.096  27.084  162.293 1.00 156.62 ?  86  LEU A CB  1 
ATOM   447   C CG  . LEU A  1 56  ? 12.012  25.788  163.100 1.00 154.22 ?  86  LEU A CG  1 
ATOM   448   C CD1 . LEU A  1 56  ? 10.592  25.555  163.582 1.00 155.76 ?  86  LEU A CD1 1 
ATOM   449   C CD2 . LEU A  1 56  ? 12.494  24.613  162.266 1.00 154.58 ?  86  LEU A CD2 1 
ATOM   450   N N   . GLU A  1 57  ? 14.162  28.909  159.921 1.00 178.28 ?  87  GLU A N   1 
ATOM   451   C CA  . GLU A  1 57  ? 14.316  30.210  159.291 1.00 177.09 ?  87  GLU A CA  1 
ATOM   452   C C   . GLU A  1 57  ? 12.944  30.745  158.881 1.00 178.52 ?  87  GLU A C   1 
ATOM   453   O O   . GLU A  1 57  ? 12.034  29.978  158.555 1.00 176.18 ?  87  GLU A O   1 
ATOM   454   C CB  . GLU A  1 57  ? 15.237  30.092  158.074 1.00 172.00 ?  87  GLU A CB  1 
ATOM   455   C CG  . GLU A  1 57  ? 15.724  31.406  157.484 1.00 169.20 ?  87  GLU A CG  1 
ATOM   456   C CD  . GLU A  1 57  ? 16.660  32.157  158.411 1.00 163.49 ?  87  GLU A CD  1 
ATOM   457   O OE1 . GLU A  1 57  ? 17.248  31.522  159.312 1.00 161.01 ?  87  GLU A OE1 1 
ATOM   458   O OE2 . GLU A  1 57  ? 16.814  33.384  158.232 1.00 165.00 -1 87  GLU A OE2 1 
ATOM   459   N N   . ASN A  1 58  ? 12.795  32.070  158.907 1.00 171.25 ?  88  ASN A N   1 
ATOM   460   C CA  . ASN A  1 58  ? 11.568  32.758  158.505 1.00 173.18 ?  88  ASN A CA  1 
ATOM   461   C C   . ASN A  1 58  ? 10.352  32.426  159.374 1.00 173.70 ?  88  ASN A C   1 
ATOM   462   O O   . ASN A  1 58  ? 9.240   32.870  159.061 1.00 171.79 ?  88  ASN A O   1 
ATOM   463   C CB  . ASN A  1 58  ? 11.217  32.461  157.036 1.00 176.63 ?  88  ASN A CB  1 
ATOM   464   C CG  . ASN A  1 58  ? 12.087  33.220  156.042 1.00 176.12 ?  88  ASN A CG  1 
ATOM   465   O OD1 . ASN A  1 58  ? 12.641  34.275  156.352 1.00 181.53 ?  88  ASN A OD1 1 
ATOM   466   N ND2 . ASN A  1 58  ? 12.195  32.681  154.826 1.00 164.42 ?  88  ASN A ND2 1 
ATOM   467   N N   . VAL A  1 59  ? 10.516  31.656  160.449 1.00 175.50 ?  89  VAL A N   1 
ATOM   468   C CA  . VAL A  1 59  ? 9.394   31.212  161.274 1.00 172.71 ?  89  VAL A CA  1 
ATOM   469   C C   . VAL A  1 59  ? 9.270   32.107  162.500 1.00 167.22 ?  89  VAL A C   1 
ATOM   470   O O   . VAL A  1 59  ? 10.250  32.323  163.225 1.00 163.36 ?  89  VAL A O   1 
ATOM   471   C CB  . VAL A  1 59  ? 9.561   29.740  161.683 1.00 166.31 ?  89  VAL A CB  1 
ATOM   472   C CG1 . VAL A  1 59  ? 8.452   29.330  162.626 1.00 164.20 ?  89  VAL A CG1 1 
ATOM   473   C CG2 . VAL A  1 59  ? 9.575   28.848  160.449 1.00 170.48 ?  89  VAL A CG2 1 
ATOM   474   N N   . THR A  1 60  ? 8.065   32.634  162.725 1.00 163.62 ?  90  THR A N   1 
ATOM   475   C CA  . THR A  1 60  ? 7.750   33.466  163.885 1.00 163.52 ?  90  THR A CA  1 
ATOM   476   C C   . THR A  1 60  ? 6.580   32.868  164.663 1.00 165.67 ?  90  THR A C   1 
ATOM   477   O O   . THR A  1 60  ? 5.439   32.901  164.189 1.00 169.72 ?  90  THR A O   1 
ATOM   478   C CB  . THR A  1 60  ? 7.422   34.889  163.444 1.00 166.98 ?  90  THR A CB  1 
ATOM   479   O OG1 . THR A  1 60  ? 8.552   35.444  162.759 1.00 168.82 ?  90  THR A OG1 1 
ATOM   480   C CG2 . THR A  1 60  ? 7.083   35.751  164.650 1.00 168.53 ?  90  THR A CG2 1 
ATOM   481   N N   . GLU A  1 61  ? 6.858   32.310  165.844 1.00 145.04 ?  91  GLU A N   1 
ATOM   482   C CA  . GLU A  1 61  ? 5.845   31.674  166.680 1.00 147.14 ?  91  GLU A CA  1 
ATOM   483   C C   . GLU A  1 61  ? 5.671   32.403  168.008 1.00 148.16 ?  91  GLU A C   1 
ATOM   484   O O   . GLU A  1 61  ? 6.652   32.836  168.620 1.00 145.98 ?  91  GLU A O   1 
ATOM   485   C CB  . GLU A  1 61  ? 6.197   30.207  166.956 1.00 145.17 ?  91  GLU A CB  1 
ATOM   486   C CG  . GLU A  1 61  ? 5.083   29.418  167.637 1.00 147.57 ?  91  GLU A CG  1 
ATOM   487   C CD  . GLU A  1 61  ? 3.955   29.019  166.706 1.00 150.56 ?  91  GLU A CD  1 
ATOM   488   O OE1 . GLU A  1 61  ? 4.057   29.279  165.490 1.00 150.67 ?  91  GLU A OE1 1 
ATOM   489   O OE2 . GLU A  1 61  ? 2.954   28.455  167.200 1.00 152.97 -1 91  GLU A OE2 1 
ATOM   490   N N   . GLU A  1 62  ? 4.415   32.534  168.448 1.00 150.81 ?  92  GLU A N   1 
ATOM   491   C CA  . GLU A  1 62  ? 4.085   33.217  169.696 1.00 154.98 ?  92  GLU A CA  1 
ATOM   492   C C   . GLU A  1 62  ? 4.157   32.247  170.870 1.00 152.46 ?  92  GLU A C   1 
ATOM   493   O O   . GLU A  1 62  ? 3.532   31.181  170.846 1.00 150.61 ?  92  GLU A O   1 
ATOM   494   C CB  . GLU A  1 62  ? 2.702   33.869  169.658 1.00 162.30 ?  92  GLU A CB  1 
ATOM   495   C CG  . GLU A  1 62  ? 2.501   34.912  168.579 1.00 168.08 ?  92  GLU A CG  1 
ATOM   496   C CD  . GLU A  1 62  ? 1.125   35.545  168.659 1.00 186.76 ?  92  GLU A CD  1 
ATOM   497   O OE1 . GLU A  1 62  ? 0.426   35.306  169.668 1.00 192.03 ?  92  GLU A OE1 1 
ATOM   498   O OE2 . GLU A  1 62  ? 0.742   36.278  167.723 1.00 197.06 -1 92  GLU A OE2 1 
ATOM   499   N N   . PHE A  1 63  ? 4.917   32.624  171.888 1.00 156.70 ?  93  PHE A N   1 
ATOM   500   C CA  . PHE A  1 63  ? 5.075   31.861  173.116 1.00 156.38 ?  93  PHE A CA  1 
ATOM   501   C C   . PHE A  1 63  ? 4.275   32.512  174.243 1.00 161.80 ?  93  PHE A C   1 
ATOM   502   O O   . PHE A  1 63  ? 3.833   33.660  174.148 1.00 165.46 ?  93  PHE A O   1 
ATOM   503   C CB  . PHE A  1 63  ? 6.555   31.751  173.493 1.00 150.71 ?  93  PHE A CB  1 
ATOM   504   C CG  . PHE A  1 63  ? 7.325   30.762  172.657 1.00 144.30 ?  93  PHE A CG  1 
ATOM   505   C CD1 . PHE A  1 63  ? 7.873   31.137  171.440 1.00 145.71 ?  93  PHE A CD1 1 
ATOM   506   C CD2 . PHE A  1 63  ? 7.503   29.459  173.091 1.00 140.88 ?  93  PHE A CD2 1 
ATOM   507   C CE1 . PHE A  1 63  ? 8.584   30.228  170.673 1.00 143.96 ?  93  PHE A CE1 1 
ATOM   508   C CE2 . PHE A  1 63  ? 8.214   28.547  172.328 1.00 138.10 ?  93  PHE A CE2 1 
ATOM   509   C CZ  . PHE A  1 63  ? 8.754   28.932  171.118 1.00 136.89 ?  93  PHE A CZ  1 
ATOM   510   N N   . ASN A  1 64  ? 4.085   31.755  175.326 1.00 157.82 ?  94  ASN A N   1 
ATOM   511   C CA  . ASN A  1 64  ? 3.369   32.268  176.495 1.00 162.19 ?  94  ASN A CA  1 
ATOM   512   C C   . ASN A  1 64  ? 3.861   31.506  177.724 1.00 159.76 ?  94  ASN A C   1 
ATOM   513   O O   . ASN A  1 64  ? 3.372   30.411  178.017 1.00 174.11 ?  94  ASN A O   1 
ATOM   514   C CB  . ASN A  1 64  ? 1.865   32.125  176.316 1.00 167.08 ?  94  ASN A CB  1 
ATOM   515   C CG  . ASN A  1 64  ? 1.081   32.998  177.271 1.00 171.05 ?  94  ASN A CG  1 
ATOM   516   O OD1 . ASN A  1 64  ? 1.544   33.305  178.369 1.00 169.31 ?  94  ASN A OD1 1 
ATOM   517   N ND2 . ASN A  1 64  ? -0.118  33.394  176.863 1.00 177.21 ?  94  ASN A ND2 1 
ATOM   518   N N   . MET A  1 65  ? 4.829   32.096  178.432 1.00 167.32 ?  95  MET A N   1 
ATOM   519   C CA  . MET A  1 65  ? 5.422   31.452  179.600 1.00 161.51 ?  95  MET A CA  1 
ATOM   520   C C   . MET A  1 65  ? 4.453   31.331  180.769 1.00 169.98 ?  95  MET A C   1 
ATOM   521   O O   . MET A  1 65  ? 4.673   30.492  181.649 1.00 169.62 ?  95  MET A O   1 
ATOM   522   C CB  . MET A  1 65  ? 6.661   32.218  180.067 1.00 157.52 ?  95  MET A CB  1 
ATOM   523   C CG  . MET A  1 65  ? 6.379   33.657  180.470 1.00 166.33 ?  95  MET A CG  1 
ATOM   524   S SD  . MET A  1 65  ? 7.826   34.488  181.151 1.00 161.49 ?  95  MET A SD  1 
ATOM   525   C CE  . MET A  1 65  ? 8.179   33.435  182.555 1.00 154.63 ?  95  MET A CE  1 
ATOM   526   N N   . TRP A  1 66  ? 3.396   32.143  180.807 1.00 170.37 ?  96  TRP A N   1 
ATOM   527   C CA  . TRP A  1 66  ? 2.473   32.114  181.934 1.00 173.96 ?  96  TRP A CA  1 
ATOM   528   C C   . TRP A  1 66  ? 1.300   31.175  181.713 1.00 175.08 ?  96  TRP A C   1 
ATOM   529   O O   . TRP A  1 66  ? 0.609   30.828  182.678 1.00 177.94 ?  96  TRP A O   1 
ATOM   530   C CB  . TRP A  1 66  ? 1.948   33.529  182.195 1.00 176.77 ?  96  TRP A CB  1 
ATOM   531   C CG  . TRP A  1 66  ? 3.044   34.525  182.373 1.00 174.40 ?  96  TRP A CG  1 
ATOM   532   C CD1 . TRP A  1 66  ? 3.420   35.498  181.493 1.00 174.31 ?  96  TRP A CD1 1 
ATOM   533   C CD2 . TRP A  1 66  ? 3.905   34.656  183.508 1.00 170.55 ?  96  TRP A CD2 1 
ATOM   534   N NE1 . TRP A  1 66  ? 4.469   36.220  182.006 1.00 170.85 ?  96  TRP A NE1 1 
ATOM   535   C CE2 . TRP A  1 66  ? 4.783   35.725  183.244 1.00 167.37 ?  96  TRP A CE2 1 
ATOM   536   C CE3 . TRP A  1 66  ? 4.019   33.973  184.721 1.00 170.32 ?  96  TRP A CE3 1 
ATOM   537   C CZ2 . TRP A  1 66  ? 5.764   36.121  184.145 1.00 164.92 ?  96  TRP A CZ2 1 
ATOM   538   C CZ3 . TRP A  1 66  ? 4.991   34.373  185.616 1.00 170.49 ?  96  TRP A CZ3 1 
ATOM   539   C CH2 . TRP A  1 66  ? 5.849   35.438  185.325 1.00 168.07 ?  96  TRP A CH2 1 
ATOM   540   N N   . LYS A  1 67  ? 1.078   30.749  180.479 1.00 166.60 ?  97  LYS A N   1 
ATOM   541   C CA  . LYS A  1 67  ? 0.048   29.789  180.118 1.00 166.84 ?  97  LYS A CA  1 
ATOM   542   C C   . LYS A  1 67  ? 0.682   28.616  179.390 1.00 167.06 ?  97  LYS A C   1 
ATOM   543   O O   . LYS A  1 67  ? 0.116   28.056  178.450 1.00 173.08 ?  97  LYS A O   1 
ATOM   544   C CB  . LYS A  1 67  ? -1.060  30.438  179.292 1.00 177.68 ?  97  LYS A CB  1 
ATOM   545   C CG  . LYS A  1 67  ? -1.746  31.588  180.008 1.00 186.64 ?  97  LYS A CG  1 
ATOM   546   C CD  . LYS A  1 67  ? -2.337  31.118  181.334 1.00 195.22 ?  97  LYS A CD  1 
ATOM   547   C CE  . LYS A  1 67  ? -2.968  32.274  182.091 1.00 202.90 ?  97  LYS A CE  1 
ATOM   548   N NZ  . LYS A  1 67  ? -3.525  31.863  183.410 1.00 213.34 1  97  LYS A NZ  1 
ATOM   549   N N   . ASN A  1 68  ? 1.870   28.220  179.830 1.00 158.15 ?  98  ASN A N   1 
ATOM   550   C CA  . ASN A  1 68  ? 2.577   27.106  179.225 1.00 155.06 ?  98  ASN A CA  1 
ATOM   551   C C   . ASN A  1 68  ? 2.330   25.906  180.124 1.00 155.30 ?  98  ASN A C   1 
ATOM   552   O O   . ASN A  1 68  ? 2.531   25.979  181.341 1.00 155.28 ?  98  ASN A O   1 
ATOM   553   C CB  . ASN A  1 68  ? 4.070   27.419  179.074 1.00 150.86 ?  98  ASN A CB  1 
ATOM   554   C CG  . ASN A  1 68  ? 4.856   26.284  178.442 1.00 148.11 ?  98  ASN A CG  1 
ATOM   555   O OD1 . ASN A  1 68  ? 5.660   25.629  179.100 1.00 146.12 ?  98  ASN A OD1 1 
ATOM   556   N ND2 . ASN A  1 68  ? 4.639   26.063  177.148 1.00 148.22 ?  98  ASN A ND2 1 
ATOM   557   N N   . ASN A  1 69  ? 1.909   24.801  179.516 1.00 142.33 ?  99  ASN A N   1 
ATOM   558   C CA  . ASN A  1 69  ? 1.492   23.629  180.267 1.00 152.17 ?  99  ASN A CA  1 
ATOM   559   C C   . ASN A  1 69  ? 2.660   22.750  180.681 1.00 146.81 ?  99  ASN A C   1 
ATOM   560   O O   . ASN A  1 69  ? 2.476   21.850  181.508 1.00 150.82 ?  99  ASN A O   1 
ATOM   561   C CB  . ASN A  1 69  ? 0.475   22.836  179.447 1.00 162.69 ?  99  ASN A CB  1 
ATOM   562   C CG  . ASN A  1 69  ? -0.230  21.778  180.263 1.00 171.60 ?  99  ASN A CG  1 
ATOM   563   O OD1 . ASN A  1 69  ? 0.087   20.595  180.175 1.00 172.37 ?  99  ASN A OD1 1 
ATOM   564   N ND2 . ASN A  1 69  ? -1.199  22.204  181.068 1.00 173.70 ?  99  ASN A ND2 1 
ATOM   565   N N   . MET A  1 70  ? 3.850   22.990  180.131 1.00 163.05 ?  100 MET A N   1 
ATOM   566   C CA  . MET A  1 70  ? 5.013   22.201  180.515 1.00 155.83 ?  100 MET A CA  1 
ATOM   567   C C   . MET A  1 70  ? 5.330   22.415  181.988 1.00 154.19 ?  100 MET A C   1 
ATOM   568   O O   . MET A  1 70  ? 5.881   21.528  182.650 1.00 153.32 ?  100 MET A O   1 
ATOM   569   C CB  . MET A  1 70  ? 6.193   22.608  179.640 1.00 141.35 ?  100 MET A CB  1 
ATOM   570   C CG  . MET A  1 70  ? 5.876   22.512  178.158 1.00 140.95 ?  100 MET A CG  1 
ATOM   571   S SD  . MET A  1 70  ? 7.229   22.977  177.064 1.00 122.81 ?  100 MET A SD  1 
ATOM   572   C CE  . MET A  1 70  ? 8.431   21.707  177.436 1.00 115.10 ?  100 MET A CE  1 
ATOM   573   N N   . VAL A  1 71  ? 4.985   23.594  182.507 1.00 150.01 ?  101 VAL A N   1 
ATOM   574   C CA  . VAL A  1 71  ? 5.196   23.914  183.915 1.00 148.41 ?  101 VAL A CA  1 
ATOM   575   C C   . VAL A  1 71  ? 4.231   23.118  184.785 1.00 156.67 ?  101 VAL A C   1 
ATOM   576   O O   . VAL A  1 71  ? 4.626   22.498  185.779 1.00 153.54 ?  101 VAL A O   1 
ATOM   577   C CB  . VAL A  1 71  ? 5.041   25.427  184.146 1.00 146.25 ?  101 VAL A CB  1 
ATOM   578   C CG1 . VAL A  1 71  ? 5.176   25.749  185.618 1.00 144.95 ?  101 VAL A CG1 1 
ATOM   579   C CG2 . VAL A  1 71  ? 6.061   26.196  183.327 1.00 134.96 ?  101 VAL A CG2 1 
ATOM   580   N N   . GLU A  1 72  ? 2.948   23.123  184.413 1.00 154.26 ?  102 GLU A N   1 
ATOM   581   C CA  . GLU A  1 72  ? 1.922   22.418  185.170 1.00 158.16 ?  102 GLU A CA  1 
ATOM   582   C C   . GLU A  1 72  ? 2.141   20.914  185.153 1.00 156.80 ?  102 GLU A C   1 
ATOM   583   O O   . GLU A  1 72  ? 1.650   20.213  186.045 1.00 153.77 ?  102 GLU A O   1 
ATOM   584   C CB  . GLU A  1 72  ? 0.544   22.747  184.595 1.00 166.29 ?  102 GLU A CB  1 
ATOM   585   C CG  . GLU A  1 72  ? 0.227   24.235  184.573 1.00 167.00 ?  102 GLU A CG  1 
ATOM   586   C CD  . GLU A  1 72  ? 0.135   24.846  185.957 1.00 163.22 ?  102 GLU A CD  1 
ATOM   587   O OE1 . GLU A  1 72  ? -0.203  24.121  186.915 1.00 167.00 ?  102 GLU A OE1 1 
ATOM   588   O OE2 . GLU A  1 72  ? 0.407   26.059  186.086 1.00 162.81 -1 102 GLU A OE2 1 
ATOM   589   N N   . GLN A  1 73  ? 2.856   20.409  184.150 1.00 161.75 ?  103 GLN A N   1 
ATOM   590   C CA  . GLN A  1 73  ? 3.181   18.991  184.075 1.00 159.38 ?  103 GLN A CA  1 
ATOM   591   C C   . GLN A  1 73  ? 4.377   18.663  184.960 1.00 150.81 ?  103 GLN A C   1 
ATOM   592   O O   . GLN A  1 73  ? 4.378   17.648  185.666 1.00 147.41 ?  103 GLN A O   1 
ATOM   593   C CB  . GLN A  1 73  ? 3.485   18.609  182.626 1.00 166.29 ?  103 GLN A CB  1 
ATOM   594   C CG  . GLN A  1 73  ? 2.288   18.613  181.697 1.00 177.10 ?  103 GLN A CG  1 
ATOM   595   C CD  . GLN A  1 73  ? 2.642   18.120  180.309 1.00 180.22 ?  103 GLN A CD  1 
ATOM   596   O OE1 . GLN A  1 73  ? 3.691   17.508  180.105 1.00 169.70 ?  103 GLN A OE1 1 
ATOM   597   N NE2 . GLN A  1 73  ? 1.779   18.405  179.341 1.00 184.16 ?  103 GLN A NE2 1 
ATOM   598   N N   . MET A  1 74  ? 5.399   19.520  184.931 1.00 159.46 ?  104 MET A N   1 
ATOM   599   C CA  . MET A  1 74  ? 6.587   19.311  185.751 1.00 150.72 ?  104 MET A CA  1 
ATOM   600   C C   . MET A  1 74  ? 6.279   19.388  187.243 1.00 148.21 ?  104 MET A C   1 
ATOM   601   O O   . MET A  1 74  ? 6.811   18.599  188.032 1.00 143.82 ?  104 MET A O   1 
ATOM   602   C CB  . MET A  1 74  ? 7.661   20.331  185.381 1.00 142.16 ?  104 MET A CB  1 
ATOM   603   C CG  . MET A  1 74  ? 8.897   20.232  186.246 1.00 132.20 ?  104 MET A CG  1 
ATOM   604   S SD  . MET A  1 74  ? 10.154  21.427  185.790 1.00 121.80 ?  104 MET A SD  1 
ATOM   605   C CE  . MET A  1 74  ? 11.540  20.829  186.751 1.00 121.06 ?  104 MET A CE  1 
ATOM   606   N N   . HIS A  1 75  ? 5.429   20.333  187.654 1.00 159.17 ?  105 HIS A N   1 
ATOM   607   C CA  . HIS A  1 75  ? 5.113   20.482  189.073 1.00 156.47 ?  105 HIS A CA  1 
ATOM   608   C C   . HIS A  1 75  ? 4.462   19.220  189.631 1.00 155.41 ?  105 HIS A C   1 
ATOM   609   O O   . HIS A  1 75  ? 4.833   18.741  190.709 1.00 150.56 ?  105 HIS A O   1 
ATOM   610   C CB  . HIS A  1 75  ? 4.200   21.697  189.262 1.00 160.56 ?  105 HIS A CB  1 
ATOM   611   C CG  . HIS A  1 75  ? 3.907   22.030  190.693 1.00 158.80 ?  105 HIS A CG  1 
ATOM   612   N ND1 . HIS A  1 75  ? 4.894   22.303  191.617 1.00 158.99 ?  105 HIS A ND1 1 
ATOM   613   C CD2 . HIS A  1 75  ? 2.733   22.119  191.362 1.00 164.52 ?  105 HIS A CD2 1 
ATOM   614   C CE1 . HIS A  1 75  ? 4.340   22.558  192.789 1.00 158.90 ?  105 HIS A CE1 1 
ATOM   615   N NE2 . HIS A  1 75  ? 3.030   22.449  192.662 1.00 163.56 ?  105 HIS A NE2 1 
ATOM   616   N N   . THR A  1 76  ? 3.502   18.654  188.898 1.00 153.26 ?  106 THR A N   1 
ATOM   617   C CA  . THR A  1 76  ? 2.834   17.428  189.324 1.00 152.09 ?  106 THR A CA  1 
ATOM   618   C C   . THR A  1 76  ? 3.746   16.211  189.230 1.00 146.78 ?  106 THR A C   1 
ATOM   619   O O   . THR A  1 76  ? 3.462   15.184  189.856 1.00 147.09 ?  106 THR A O   1 
ATOM   620   C CB  . THR A  1 76  ? 1.577   17.202  188.490 1.00 159.38 ?  106 THR A CB  1 
ATOM   621   O OG1 . THR A  1 76  ? 1.915   17.277  187.101 1.00 172.55 ?  106 THR A OG1 1 
ATOM   622   C CG2 . THR A  1 76  ? 0.534   18.267  188.805 1.00 162.19 ?  106 THR A CG2 1 
ATOM   623   N N   . ASP A  1 77  ? 4.832   16.305  188.463 1.00 148.39 ?  107 ASP A N   1 
ATOM   624   C CA  . ASP A  1 77  ? 5.774   15.199  188.343 1.00 146.04 ?  107 ASP A CA  1 
ATOM   625   C C   . ASP A  1 77  ? 6.690   15.144  189.560 1.00 141.92 ?  107 ASP A C   1 
ATOM   626   O O   . ASP A  1 77  ? 6.931   14.068  190.120 1.00 139.79 ?  107 ASP A O   1 
ATOM   627   C CB  . ASP A  1 77  ? 6.578   15.331  187.045 1.00 152.34 ?  107 ASP A CB  1 
ATOM   628   C CG  . ASP A  1 77  ? 5.793   14.864  185.826 1.00 160.17 ?  107 ASP A CG  1 
ATOM   629   O OD1 . ASP A  1 77  ? 4.551   14.797  185.927 1.00 161.64 ?  107 ASP A OD1 1 
ATOM   630   O OD2 . ASP A  1 77  ? 6.403   14.570  184.772 1.00 161.00 -1 107 ASP A OD2 1 
ATOM   631   N N   . ILE A  1 78  ? 7.225   16.295  189.967 1.00 154.86 ?  108 ILE A N   1 
ATOM   632   C CA  . ILE A  1 78  ? 8.116   16.344  191.120 1.00 149.82 ?  108 ILE A CA  1 
ATOM   633   C C   . ILE A  1 78  ? 7.360   15.974  192.393 1.00 147.61 ?  108 ILE A C   1 
ATOM   634   O O   . ILE A  1 78  ? 7.914   15.333  193.295 1.00 145.69 ?  108 ILE A O   1 
ATOM   635   C CB  . ILE A  1 78  ? 8.775   17.732  191.213 1.00 148.83 ?  108 ILE A CB  1 
ATOM   636   C CG1 . ILE A  1 78  ? 9.378   18.103  189.857 1.00 148.71 ?  108 ILE A CG1 1 
ATOM   637   C CG2 . ILE A  1 78  ? 9.855   17.746  192.281 1.00 143.17 ?  108 ILE A CG2 1 
ATOM   638   C CD1 . ILE A  1 78  ? 10.082  19.437  189.829 1.00 144.18 ?  108 ILE A CD1 1 
ATOM   639   N N   . ILE A  1 79  ? 6.086   16.368  192.490 1.00 152.54 ?  109 ILE A N   1 
ATOM   640   C CA  . ILE A  1 79  ? 5.285   16.020  193.665 1.00 158.17 ?  109 ILE A CA  1 
ATOM   641   C C   . ILE A  1 79  ? 5.073   14.511  193.744 1.00 157.76 ?  109 ILE A C   1 
ATOM   642   O O   . ILE A  1 79  ? 5.273   13.898  194.799 1.00 162.47 ?  109 ILE A O   1 
ATOM   643   C CB  . ILE A  1 79  ? 3.942   16.774  193.670 1.00 162.07 ?  109 ILE A CB  1 
ATOM   644   C CG1 . ILE A  1 79  ? 4.135   18.270  193.927 1.00 160.51 ?  109 ILE A CG1 1 
ATOM   645   C CG2 . ILE A  1 79  ? 3.016   16.194  194.722 1.00 170.39 ?  109 ILE A CG2 1 
ATOM   646   C CD1 . ILE A  1 79  ? 2.819   19.038  193.975 1.00 162.54 ?  109 ILE A CD1 1 
ATOM   647   N N   . SER A  1 80  ? 4.684   13.882  192.633 1.00 155.94 ?  110 SER A N   1 
ATOM   648   C CA  . SER A  1 80  ? 4.506   12.436  192.671 1.00 159.04 ?  110 SER A CA  1 
ATOM   649   C C   . SER A  1 80  ? 5.839   11.750  192.919 1.00 155.10 ?  110 SER A C   1 
ATOM   650   O O   . SER A  1 80  ? 5.884   10.656  193.494 1.00 158.59 ?  110 SER A O   1 
ATOM   651   C CB  . SER A  1 80  ? 3.879   11.954  191.368 1.00 159.36 ?  110 SER A CB  1 
ATOM   652   O OG  . SER A  1 80  ? 4.746   12.247  190.292 1.00 158.61 ?  110 SER A OG  1 
ATOM   653   N N   . LEU A  1 81  ? 6.931   12.371  192.475 1.00 157.56 ?  111 LEU A N   1 
ATOM   654   C CA  . LEU A  1 81  ? 8.250   11.822  192.748 1.00 157.34 ?  111 LEU A CA  1 
ATOM   655   C C   . LEU A  1 81  ? 8.519   11.828  194.248 1.00 158.21 ?  111 LEU A C   1 
ATOM   656   O O   . LEU A  1 81  ? 9.085   10.874  194.793 1.00 159.42 ?  111 LEU A O   1 
ATOM   657   C CB  . LEU A  1 81  ? 9.302   12.644  192.009 1.00 157.04 ?  111 LEU A CB  1 
ATOM   658   C CG  . LEU A  1 81  ? 10.551  11.989  191.434 1.00 164.65 ?  111 LEU A CG  1 
ATOM   659   C CD1 . LEU A  1 81  ? 11.299  13.080  190.707 1.00 158.57 ?  111 LEU A CD1 1 
ATOM   660   C CD2 . LEU A  1 81  ? 11.424  11.336  192.500 1.00 176.30 ?  111 LEU A CD2 1 
ATOM   661   N N   . TRP A  1 82  ? 8.100   12.902  194.931 1.00 165.84 ?  112 TRP A N   1 
ATOM   662   C CA  . TRP A  1 82  ? 8.320   13.031  196.368 1.00 164.38 ?  112 TRP A CA  1 
ATOM   663   C C   . TRP A  1 82  ? 7.548   11.973  197.143 1.00 169.76 ?  112 TRP A C   1 
ATOM   664   O O   . TRP A  1 82  ? 8.070   11.394  198.103 1.00 177.36 ?  112 TRP A O   1 
ATOM   665   C CB  . TRP A  1 82  ? 7.875   14.424  196.817 1.00 169.86 ?  112 TRP A CB  1 
ATOM   666   C CG  . TRP A  1 82  ? 8.420   14.919  198.121 1.00 178.38 ?  112 TRP A CG  1 
ATOM   667   C CD1 . TRP A  1 82  ? 7.767   14.947  199.323 1.00 183.45 ?  112 TRP A CD1 1 
ATOM   668   C CD2 . TRP A  1 82  ? 9.678   15.566  198.337 1.00 180.17 ?  112 TRP A CD2 1 
ATOM   669   N NE1 . TRP A  1 82  ? 8.565   15.515  200.284 1.00 186.08 ?  112 TRP A NE1 1 
ATOM   670   C CE2 . TRP A  1 82  ? 9.741   15.912  199.703 1.00 186.58 ?  112 TRP A CE2 1 
ATOM   671   C CE3 . TRP A  1 82  ? 10.766  15.870  197.512 1.00 173.83 ?  112 TRP A CE3 1 
ATOM   672   C CZ2 . TRP A  1 82  ? 10.848  16.540  200.262 1.00 185.28 ?  112 TRP A CZ2 1 
ATOM   673   C CZ3 . TRP A  1 82  ? 11.863  16.494  198.068 1.00 175.18 ?  112 TRP A CZ3 1 
ATOM   674   C CH2 . TRP A  1 82  ? 11.898  16.822  199.431 1.00 181.34 ?  112 TRP A CH2 1 
ATOM   675   N N   . ASP A  1 83  ? 6.312   11.684  196.720 1.00 147.29 ?  113 ASP A N   1 
ATOM   676   C CA  . ASP A  1 83  ? 5.498   10.716  197.447 1.00 154.70 ?  113 ASP A CA  1 
ATOM   677   C C   . ASP A  1 83  ? 6.003   9.309   197.179 1.00 151.62 ?  113 ASP A C   1 
ATOM   678   O O   . ASP A  1 83  ? 6.046   8.469   198.084 1.00 157.22 ?  113 ASP A O   1 
ATOM   679   C CB  . ASP A  1 83  ? 4.015   10.862  197.085 1.00 156.74 ?  113 ASP A CB  1 
ATOM   680   C CG  . ASP A  1 83  ? 3.450   12.229  197.463 1.00 162.58 ?  113 ASP A CG  1 
ATOM   681   O OD1 . ASP A  1 83  ? 4.233   13.201  197.513 1.00 164.42 ?  113 ASP A OD1 1 
ATOM   682   O OD2 . ASP A  1 83  ? 2.233   12.333  197.740 1.00 172.47 -1 113 ASP A OD2 1 
ATOM   683   N N   . GLN A  1 84  ? 6.376   9.037   195.931 1.00 160.73 ?  114 GLN A N   1 
ATOM   684   C CA  . GLN A  1 84  ? 6.872   7.718   195.578 1.00 165.94 ?  114 GLN A CA  1 
ATOM   685   C C   . GLN A  1 84  ? 8.209   7.446   196.259 1.00 166.35 ?  114 GLN A C   1 
ATOM   686   O O   . GLN A  1 84  ? 8.534   6.291   196.557 1.00 167.53 ?  114 GLN A O   1 
ATOM   687   C CB  . GLN A  1 84  ? 6.988   7.608   194.058 1.00 172.85 ?  114 GLN A CB  1 
ATOM   688   C CG  . GLN A  1 84  ? 6.666   6.231   193.504 1.00 182.46 ?  114 GLN A CG  1 
ATOM   689   C CD  . GLN A  1 84  ? 5.165   6.017   193.283 1.00 186.72 ?  114 GLN A CD  1 
ATOM   690   O OE1 . GLN A  1 84  ? 4.327   6.752   193.813 1.00 191.88 ?  114 GLN A OE1 1 
ATOM   691   N NE2 . GLN A  1 84  ? 4.828   5.008   192.487 1.00 189.62 ?  114 GLN A NE2 1 
ATOM   692   N N   . SER A  1 85  ? 8.985   8.500   196.529 1.00 160.92 ?  115 SER A N   1 
ATOM   693   C CA  . SER A  1 85  ? 10.297  8.357   197.145 1.00 158.63 ?  115 SER A CA  1 
ATOM   694   C C   . SER A  1 85  ? 10.223  8.166   198.653 1.00 158.85 ?  115 SER A C   1 
ATOM   695   O O   . SER A  1 85  ? 11.220  7.764   199.263 1.00 157.98 ?  115 SER A O   1 
ATOM   696   C CB  . SER A  1 85  ? 11.153  9.579   196.827 1.00 158.57 ?  115 SER A CB  1 
ATOM   697   O OG  . SER A  1 85  ? 12.416  9.457   197.446 1.00 171.22 ?  115 SER A OG  1 
ATOM   698   N N   . LEU A  1 86  ? 9.063   8.424   199.251 1.00 152.86 ?  116 LEU A N   1 
ATOM   699   C CA  . LEU A  1 86  ? 8.829   8.304   200.683 1.00 157.26 ?  116 LEU A CA  1 
ATOM   700   C C   . LEU A  1 86  ? 7.926   7.120   200.973 1.00 162.21 ?  116 LEU A C   1 
ATOM   701   O O   . LEU A  1 86  ? 7.647   6.828   202.141 1.00 168.59 ?  116 LEU A O   1 
ATOM   702   C CB  . LEU A  1 86  ? 8.239   9.593   201.275 1.00 153.31 ?  116 LEU A CB  1 
ATOM   703   C CG  . LEU A  1 86  ? 9.160   10.816  201.257 1.00 149.01 ?  116 LEU A CG  1 
ATOM   704   C CD1 . LEU A  1 86  ? 8.498   11.995  201.951 1.00 149.74 ?  116 LEU A CD1 1 
ATOM   705   C CD2 . LEU A  1 86  ? 10.506  10.489  201.904 1.00 148.07 ?  116 LEU A CD2 1 
ATOM   706   N N   . LYS A  1 87  ? 7.471   6.426   199.925 1.00 176.93 ?  117 LYS A N   1 
ATOM   707   C CA  . LYS A  1 87  ? 6.611   5.262   200.124 1.00 177.79 ?  117 LYS A CA  1 
ATOM   708   C C   . LYS A  1 87  ? 7.359   4.095   200.758 1.00 174.37 ?  117 LYS A C   1 
ATOM   709   O O   . LYS A  1 87  ? 6.858   3.544   201.755 1.00 174.89 ?  117 LYS A O   1 
ATOM   710   C CB  . LYS A  1 87  ? 5.988   4.873   198.779 1.00 178.41 ?  117 LYS A CB  1 
ATOM   711   C CG  . LYS A  1 87  ? 5.142   3.625   198.769 1.00 188.62 ?  117 LYS A CG  1 
ATOM   712   C CD  . LYS A  1 87  ? 4.635   3.383   197.354 1.00 177.30 ?  117 LYS A CD  1 
ATOM   713   C CE  . LYS A  1 87  ? 3.358   2.581   197.346 1.00 186.54 ?  117 LYS A CE  1 
ATOM   714   N NZ  . LYS A  1 87  ? 2.270   3.328   198.024 1.00 198.04 1  117 LYS A NZ  1 
ATOM   715   N N   . PRO A  1 88  ? 8.526   3.669   200.274 1.00 164.24 ?  118 PRO A N   1 
ATOM   716   C CA  . PRO A  1 88  ? 9.230   2.552   200.922 1.00 163.27 ?  118 PRO A CA  1 
ATOM   717   C C   . PRO A  1 88  ? 10.143  2.973   202.064 1.00 169.96 ?  118 PRO A C   1 
ATOM   718   O O   . PRO A  1 88  ? 10.974  2.169   202.500 1.00 173.19 ?  118 PRO A O   1 
ATOM   719   C CB  . PRO A  1 88  ? 10.050  1.970   199.763 1.00 164.50 ?  118 PRO A CB  1 
ATOM   720   C CG  . PRO A  1 88  ? 10.398  3.154   198.943 1.00 163.64 ?  118 PRO A CG  1 
ATOM   721   C CD  . PRO A  1 88  ? 9.218   4.089   199.036 1.00 165.30 ?  118 PRO A CD  1 
ATOM   722   N N   . CYS A  1 89  ? 9.992   4.201   202.548 1.00 158.18 ?  119 CYS A N   1 
ATOM   723   C CA  . CYS A  1 89  ? 10.810  4.764   203.606 1.00 162.03 ?  119 CYS A CA  1 
ATOM   724   C C   . CYS A  1 89  ? 10.223  4.497   204.996 1.00 161.09 ?  119 CYS A C   1 
ATOM   725   O O   . CYS A  1 89  ? 9.066   4.099   205.154 1.00 159.93 ?  119 CYS A O   1 
ATOM   726   C CB  . CYS A  1 89  ? 11.026  6.257   203.361 1.00 164.74 ?  119 CYS A CB  1 
ATOM   727   S SG  . CYS A  1 89  ? 12.280  6.551   202.064 1.00 182.49 ?  119 CYS A SG  1 
ATOM   728   N N   . VAL A  1 90  ? 11.055  4.721   206.013 1.00 152.22 ?  120 VAL A N   1 
ATOM   729   C CA  . VAL A  1 90  ? 10.669  4.471   207.399 1.00 152.78 ?  120 VAL A CA  1 
ATOM   730   C C   . VAL A  1 90  ? 9.669   5.522   207.873 1.00 150.85 ?  120 VAL A C   1 
ATOM   731   O O   . VAL A  1 90  ? 9.928   6.729   207.800 1.00 152.72 ?  120 VAL A O   1 
ATOM   732   C CB  . VAL A  1 90  ? 11.908  4.460   208.304 1.00 153.73 ?  120 VAL A CB  1 
ATOM   733   C CG1 . VAL A  1 90  ? 11.506  4.456   209.774 1.00 154.28 ?  120 VAL A CG1 1 
ATOM   734   C CG2 . VAL A  1 90  ? 12.800  3.280   207.966 1.00 151.88 ?  120 VAL A CG2 1 
ATOM   735   N N   . LYS A  1 91  ? 8.513   5.060   208.348 1.00 152.09 ?  121 LYS A N   1 
ATOM   736   C CA  . LYS A  1 91  ? 7.463   5.921   208.888 1.00 152.45 ?  121 LYS A CA  1 
ATOM   737   C C   . LYS A  1 91  ? 7.680   6.151   210.380 1.00 155.12 ?  121 LYS A C   1 
ATOM   738   O O   . LYS A  1 91  ? 7.854   5.190   211.137 1.00 155.49 ?  121 LYS A O   1 
ATOM   739   C CB  . LYS A  1 91  ? 6.079   5.321   208.661 1.00 150.83 ?  121 LYS A CB  1 
ATOM   740   C CG  . LYS A  1 91  ? 6.018   3.822   208.826 1.00 151.21 ?  121 LYS A CG  1 
ATOM   741   C CD  . LYS A  1 91  ? 4.734   3.278   208.230 1.00 158.47 ?  121 LYS A CD  1 
ATOM   742   C CE  . LYS A  1 91  ? 4.708   1.758   208.234 1.00 163.75 ?  121 LYS A CE  1 
ATOM   743   N NZ  . LYS A  1 91  ? 3.482   1.228   207.566 1.00 167.73 1  121 LYS A NZ  1 
ATOM   744   N N   . LEU A  1 92  ? 7.688   7.415   210.800 1.00 141.32 ?  122 LEU A N   1 
ATOM   745   C CA  . LEU A  1 92  ? 7.934   7.764   212.201 1.00 144.31 ?  122 LEU A CA  1 
ATOM   746   C C   . LEU A  1 92  ? 6.646   7.948   213.006 1.00 144.68 ?  122 LEU A C   1 
ATOM   747   O O   . LEU A  1 92  ? 6.542   8.877   213.812 1.00 146.75 ?  122 LEU A O   1 
ATOM   748   C CB  . LEU A  1 92  ? 8.783   9.029   212.263 1.00 146.52 ?  122 LEU A CB  1 
ATOM   749   C CG  . LEU A  1 92  ? 10.120  8.907   211.528 1.00 146.52 ?  122 LEU A CG  1 
ATOM   750   C CD1 . LEU A  1 92  ? 10.960  10.161  211.703 1.00 148.93 ?  122 LEU A CD1 1 
ATOM   751   C CD2 . LEU A  1 92  ? 10.889  7.665   211.968 1.00 146.90 ?  122 LEU A CD2 1 
ATOM   752   N N   . THR A  1 93  ? 5.652   7.079   212.823 1.00 146.15 ?  123 THR A N   1 
ATOM   753   C CA  . THR A  1 93  ? 4.422   7.185   213.610 1.00 146.43 ?  123 THR A CA  1 
ATOM   754   C C   . THR A  1 93  ? 4.607   7.158   215.129 1.00 149.25 ?  123 THR A C   1 
ATOM   755   O O   . THR A  1 93  ? 3.957   7.977   215.804 1.00 150.57 ?  123 THR A O   1 
ATOM   756   C CB  . THR A  1 93  ? 3.413   6.116   213.171 1.00 143.94 ?  123 THR A CB  1 
ATOM   757   O OG1 . THR A  1 93  ? 3.611   4.911   213.916 1.00 144.91 ?  123 THR A OG1 1 
ATOM   758   C CG2 . THR A  1 93  ? 3.540   5.850   211.694 1.00 141.14 ?  123 THR A CG2 1 
ATOM   759   N N   . PRO A  1 94  ? 5.453   6.274   215.742 1.00 146.22 ?  124 PRO A N   1 
ATOM   760   C CA  . PRO A  1 94  ? 5.560   6.302   217.209 1.00 148.80 ?  124 PRO A CA  1 
ATOM   761   C C   . PRO A  1 94  ? 6.662   7.204   217.754 1.00 151.79 ?  124 PRO A C   1 
ATOM   762   O O   . PRO A  1 94  ? 7.394   6.826   218.677 1.00 154.07 ?  124 PRO A O   1 
ATOM   763   C CB  . PRO A  1 94  ? 5.816   4.820   217.561 1.00 148.50 ?  124 PRO A CB  1 
ATOM   764   C CG  . PRO A  1 94  ? 6.416   4.205   216.323 1.00 146.81 ?  124 PRO A CG  1 
ATOM   765   C CD  . PRO A  1 94  ? 6.284   5.188   215.175 1.00 145.53 ?  124 PRO A CD  1 
ATOM   766   N N   . LEU A  1 95  ? 6.759   8.405   217.187 1.00 132.11 ?  125 LEU A N   1 
ATOM   767   C CA  . LEU A  1 95  ? 7.695   9.432   217.624 1.00 132.53 ?  125 LEU A CA  1 
ATOM   768   C C   . LEU A  1 95  ? 6.957   10.606  218.245 1.00 132.63 ?  125 LEU A C   1 
ATOM   769   O O   . LEU A  1 95  ? 7.579   11.626  218.561 1.00 132.87 ?  125 LEU A O   1 
ATOM   770   C CB  . LEU A  1 95  ? 8.573   9.936   216.480 1.00 131.26 ?  125 LEU A CB  1 
ATOM   771   C CG  . LEU A  1 95  ? 10.093  9.997   216.731 1.00 132.16 ?  125 LEU A CG  1 
ATOM   772   C CD1 . LEU A  1 95  ? 10.653  8.720   217.363 1.00 133.70 ?  125 LEU A CD1 1 
ATOM   773   C CD2 . LEU A  1 95  ? 10.853  10.371  215.492 1.00 130.98 ?  125 LEU A CD2 1 
ATOM   774   N N   . CYS A  1 96  ? 5.634   10.510  218.397 1.00 151.77 ?  126 CYS A N   1 
ATOM   775   C CA  . CYS A  1 96  ? 4.856   11.601  218.969 1.00 152.66 ?  126 CYS A CA  1 
ATOM   776   C C   . CYS A  1 96  ? 4.741   11.470  220.480 1.00 155.00 ?  126 CYS A C   1 
ATOM   777   O O   . CYS A  1 96  ? 3.781   11.964  221.084 1.00 155.07 ?  126 CYS A O   1 
ATOM   778   C CB  . CYS A  1 96  ? 3.466   11.664  218.315 1.00 149.94 ?  126 CYS A CB  1 
ATOM   779   S SG  . CYS A  1 96  ? 3.447   12.093  216.528 1.00 147.24 ?  126 CYS A SG  1 
ATOM   780   N N   . VAL A  1 97  ? 5.720   10.799  221.098 1.00 162.15 ?  127 VAL A N   1 
ATOM   781   C CA  . VAL A  1 97  ? 5.753   10.646  222.540 1.00 164.59 ?  127 VAL A CA  1 
ATOM   782   C C   . VAL A  1 97  ? 6.144   11.973  223.191 1.00 167.01 ?  127 VAL A C   1 
ATOM   783   O O   . VAL A  1 97  ? 6.769   12.843  222.575 1.00 167.28 ?  127 VAL A O   1 
ATOM   784   C CB  . VAL A  1 97  ? 6.720   9.510   222.918 1.00 165.95 ?  127 VAL A CB  1 
ATOM   785   C CG1 . VAL A  1 97  ? 6.508   9.037   224.359 1.00 167.70 ?  127 VAL A CG1 1 
ATOM   786   C CG2 . VAL A  1 97  ? 6.579   8.342   221.937 1.00 163.20 ?  127 VAL A CG2 1 
ATOM   787   N N   . THR A  1 98  ? 5.738   12.139  224.450 1.00 162.02 ?  128 THR A N   1 
ATOM   788   C CA  . THR A  1 98  ? 6.085   13.335  225.215 1.00 164.24 ?  128 THR A CA  1 
ATOM   789   C C   . THR A  1 98  ? 7.597   13.507  225.355 1.00 166.85 ?  128 THR A C   1 
ATOM   790   O O   . THR A  1 98  ? 8.302   12.581  225.767 1.00 168.21 ?  128 THR A O   1 
ATOM   791   C CB  . THR A  1 98  ? 5.435   13.247  226.595 1.00 165.34 ?  128 THR A CB  1 
ATOM   792   O OG1 . THR A  1 98  ? 5.895   12.061  227.257 1.00 166.22 ?  128 THR A OG1 1 
ATOM   793   C CG2 . THR A  1 98  ? 3.912   13.198  226.469 1.00 163.22 ?  128 THR A CG2 1 
ATOM   794   N N   . LEU A  1 99  ? 8.097   14.694  224.995 1.00 160.78 ?  129 LEU A N   1 
ATOM   795   C CA  . LEU A  1 99  ? 9.527   14.995  225.021 1.00 163.31 ?  129 LEU A CA  1 
ATOM   796   C C   . LEU A  1 99  ? 9.860   15.923  226.191 1.00 165.52 ?  129 LEU A C   1 
ATOM   797   O O   . LEU A  1 99  ? 9.407   17.072  226.213 1.00 164.88 ?  129 LEU A O   1 
ATOM   798   C CB  . LEU A  1 99  ? 9.931   15.650  223.702 1.00 162.31 ?  129 LEU A CB  1 
ATOM   799   C CG  . LEU A  1 99  ? 9.446   14.906  222.454 1.00 159.08 ?  129 LEU A CG  1 
ATOM   800   C CD1 . LEU A  1 99  ? 9.865   15.629  221.186 1.00 157.78 ?  129 LEU A CD1 1 
ATOM   801   C CD2 . LEU A  1 99  ? 9.929   13.473  222.440 1.00 159.14 ?  129 LEU A CD2 1 
ATOM   802   N N   . GLN A  1 100 ? 10.650  15.437  227.151 1.00 174.38 ?  130 GLN A N   1 
ATOM   803   C CA  . GLN A  1 100 ? 11.161  16.236  228.276 1.00 175.79 ?  130 GLN A CA  1 
ATOM   804   C C   . GLN A  1 100 ? 12.513  16.854  227.904 1.00 177.36 ?  130 GLN A C   1 
ATOM   805   O O   . GLN A  1 100 ? 13.570  16.275  228.164 1.00 179.09 ?  130 GLN A O   1 
ATOM   806   C CB  . GLN A  1 100 ? 11.176  15.416  229.562 1.00 176.53 ?  130 GLN A CB  1 
ATOM   807   C CG  . GLN A  1 100 ? 9.774   14.878  229.861 1.00 174.80 ?  130 GLN A CG  1 
ATOM   808   C CD  . GLN A  1 100 ? 9.620   14.275  231.241 1.00 180.55 ?  130 GLN A CD  1 
ATOM   809   O OE1 . GLN A  1 100 ? 9.715   14.979  232.249 1.00 188.39 ?  130 GLN A OE1 1 
ATOM   810   N NE2 . GLN A  1 100 ? 9.328   12.981  231.296 1.00 182.64 ?  130 GLN A NE2 1 
ATOM   811   N N   . CYS A  1 101 ? 12.485  18.037  227.281 1.00 175.95 ?  131 CYS A N   1 
ATOM   812   C CA  . CYS A  1 101 ? 13.665  18.686  226.717 1.00 176.96 ?  131 CYS A CA  1 
ATOM   813   C C   . CYS A  1 101 ? 14.258  19.734  227.663 1.00 177.39 ?  131 CYS A C   1 
ATOM   814   O O   . CYS A  1 101 ? 13.623  20.168  228.629 1.00 177.04 ?  131 CYS A O   1 
ATOM   815   C CB  . CYS A  1 101 ? 13.330  19.396  225.406 1.00 176.11 ?  131 CYS A CB  1 
ATOM   816   S SG  . CYS A  1 101 ? 12.632  18.264  224.235 1.00 174.38 ?  131 CYS A SG  1 
ATOM   817   N N   . THR A  1 102 ? 15.506  20.122  227.373 1.00 183.39 ?  132 THR A N   1 
ATOM   818   C CA  . THR A  1 102 ? 16.236  21.155  228.106 1.00 183.60 ?  132 THR A CA  1 
ATOM   819   C C   . THR A  1 102 ? 17.202  21.837  227.138 1.00 183.46 ?  132 THR A C   1 
ATOM   820   O O   . THR A  1 102 ? 17.408  21.362  226.018 1.00 183.32 ?  132 THR A O   1 
ATOM   821   C CB  . THR A  1 102 ? 17.013  20.570  229.293 1.00 184.46 ?  132 THR A CB  1 
ATOM   822   O OG1 . THR A  1 102 ? 17.770  21.606  229.930 1.00 184.73 ?  132 THR A OG1 1 
ATOM   823   C CG2 . THR A  1 102 ? 17.969  19.484  228.820 1.00 184.98 ?  132 THR A CG2 1 
ATOM   824   N N   . ASN A  1 103 ? 17.832  22.937  227.581 1.00 195.97 ?  133 ASN A N   1 
ATOM   825   C CA  . ASN A  1 103 ? 18.783  23.612  226.696 1.00 194.13 ?  133 ASN A CA  1 
ATOM   826   C C   . ASN A  1 103 ? 19.991  22.750  226.388 1.00 196.63 ?  133 ASN A C   1 
ATOM   827   O O   . ASN A  1 103 ? 20.402  21.894  227.172 1.00 197.83 ?  133 ASN A O   1 
ATOM   828   C CB  . ASN A  1 103 ? 19.362  24.945  227.217 1.00 199.67 ?  133 ASN A CB  1 
ATOM   829   C CG  . ASN A  1 103 ? 18.410  26.121  227.159 1.00 207.16 ?  133 ASN A CG  1 
ATOM   830   O OD1 . ASN A  1 103 ? 18.509  26.919  226.226 1.00 199.93 ?  133 ASN A OD1 1 
ATOM   831   N ND2 . ASN A  1 103 ? 17.587  26.313  228.173 1.00 225.68 ?  133 ASN A ND2 1 
ATOM   832   N N   . VAL A  1 104 ? 20.554  23.002  225.211 1.00 184.71 ?  134 VAL A N   1 
ATOM   833   C CA  . VAL A  1 104 ? 21.758  22.313  224.802 1.00 184.50 ?  134 VAL A CA  1 
ATOM   834   C C   . VAL A  1 104 ? 22.904  22.816  225.673 1.00 184.92 ?  134 VAL A C   1 
ATOM   835   O O   . VAL A  1 104 ? 22.866  23.931  226.213 1.00 185.13 ?  134 VAL A O   1 
ATOM   836   C CB  . VAL A  1 104 ? 22.027  22.553  223.305 1.00 183.44 ?  134 VAL A CB  1 
ATOM   837   C CG1 . VAL A  1 104 ? 22.456  23.994  223.068 1.00 183.08 ?  134 VAL A CG1 1 
ATOM   838   C CG2 . VAL A  1 104 ? 23.060  21.574  222.776 1.00 182.76 ?  134 VAL A CG2 1 
ATOM   839   N N   . THR A  1 105 ? 23.919  21.981  225.836 1.00 194.65 ?  135 THR A N   1 
ATOM   840   C CA  . THR A  1 105 ? 25.054  22.300  226.694 1.00 197.13 ?  135 THR A CA  1 
ATOM   841   C C   . THR A  1 105 ? 25.867  23.441  226.094 1.00 198.33 ?  135 THR A C   1 
ATOM   842   O O   . THR A  1 105 ? 26.585  23.257  225.106 1.00 194.77 ?  135 THR A O   1 
ATOM   843   C CB  . THR A  1 105 ? 25.925  21.069  226.921 1.00 195.09 ?  135 THR A CB  1 
ATOM   844   O OG1 . THR A  1 105 ? 25.115  20.004  227.432 1.00 196.85 ?  135 THR A OG1 1 
ATOM   845   C CG2 . THR A  1 105 ? 27.023  21.389  227.931 1.00 189.29 ?  135 THR A CG2 1 
ATOM   846   N N   . ASN A  1 106 ? 25.751  24.623  226.692 1.00 206.51 ?  136 ASN A N   1 
ATOM   847   C CA  . ASN A  1 106 ? 26.514  25.789  226.268 1.00 207.04 ?  136 ASN A CA  1 
ATOM   848   C C   . ASN A  1 106 ? 26.598  26.726  227.462 1.00 213.53 ?  136 ASN A C   1 
ATOM   849   O O   . ASN A  1 106 ? 26.127  26.406  228.557 1.00 214.11 ?  136 ASN A O   1 
ATOM   850   C CB  . ASN A  1 106 ? 25.863  26.488  225.066 1.00 200.85 ?  136 ASN A CB  1 
ATOM   851   C CG  . ASN A  1 106 ? 24.515  27.115  225.406 1.00 204.82 ?  136 ASN A CG  1 
ATOM   852   O OD1 . ASN A  1 106 ? 23.817  26.664  226.315 1.00 208.93 ?  136 ASN A OD1 1 
ATOM   853   N ND2 . ASN A  1 106 ? 24.143  28.158  224.668 1.00 202.86 ?  136 ASN A ND2 1 
ATOM   854   N N   . ASN A  1 107 ? 27.184  27.897  227.248 1.00 223.76 ?  137 ASN A N   1 
ATOM   855   C CA  . ASN A  1 107 ? 27.346  28.851  228.334 1.00 230.15 ?  137 ASN A CA  1 
ATOM   856   C C   . ASN A  1 107 ? 26.655  30.158  227.967 1.00 235.72 ?  137 ASN A C   1 
ATOM   857   O O   . ASN A  1 107 ? 27.299  31.070  227.440 1.00 241.25 ?  137 ASN A O   1 
ATOM   858   C CB  . ASN A  1 107 ? 28.866  29.058  228.610 1.00 226.67 ?  137 ASN A CB  1 
ATOM   859   C CG  . ASN A  1 107 ? 29.139  30.229  229.522 1.00 236.42 ?  137 ASN A CG  1 
ATOM   860   O OD1 . ASN A  1 107 ? 29.005  30.132  230.741 1.00 242.59 ?  137 ASN A OD1 1 
ATOM   861   N ND2 . ASN A  1 107 ? 29.502  31.359  228.928 1.00 244.62 ?  137 ASN A ND2 1 
ATOM   862   N N   . ILE A  1 108 ? 25.366  30.261  228.318 1.00 246.65 ?  138 ILE A N   1 
ATOM   863   C CA  . ILE A  1 108 ? 24.576  31.495  228.216 1.00 247.56 ?  138 ILE A CA  1 
ATOM   864   C C   . ILE A  1 108 ? 24.846  32.098  226.765 1.00 242.25 ?  138 ILE A C   1 
ATOM   865   O O   . ILE A  1 108 ? 25.312  31.338  225.911 1.00 237.28 ?  138 ILE A O   1 
ATOM   866   C CB  . ILE A  1 108 ? 24.908  32.351  229.506 1.00 247.26 ?  138 ILE A CB  1 
ATOM   867   C CG1 . ILE A  1 108 ? 24.828  31.460  230.749 1.00 245.44 ?  138 ILE A CG1 1 
ATOM   868   C CG2 . ILE A  1 108 ? 23.754  33.188  229.988 1.00 244.54 ?  138 ILE A CG2 1 
ATOM   869   C CD1 . ILE A  1 108 ? 26.113  30.854  231.242 1.00 243.67 ?  138 ILE A CD1 1 
ATOM   870   N N   . THR A  1 109 ? 24.487  33.327  226.363 1.00 247.09 ?  139 THR A N   1 
ATOM   871   C CA  . THR A  1 109 ? 23.713  34.323  227.073 1.00 246.44 ?  139 THR A CA  1 
ATOM   872   C C   . THR A  1 109 ? 22.219  34.049  227.070 1.00 249.16 ?  139 THR A C   1 
ATOM   873   O O   . THR A  1 109 ? 21.768  32.982  226.647 1.00 249.15 ?  139 THR A O   1 
ATOM   874   C CB  . THR A  1 109 ? 23.957  35.709  226.449 1.00 239.95 ?  139 THR A CB  1 
ATOM   875   O OG1 . THR A  1 109 ? 23.624  35.667  225.055 1.00 238.04 ?  139 THR A OG1 1 
ATOM   876   C CG2 . THR A  1 109 ? 25.418  36.092  226.580 1.00 238.75 ?  139 THR A CG2 1 
ATOM   877   N N   . ASP A  1 110 ? 21.448  35.027  227.549 1.00 264.12 ?  140 ASP A N   1 
ATOM   878   C CA  . ASP A  1 110 ? 20.003  34.870  227.578 1.00 266.16 ?  140 ASP A CA  1 
ATOM   879   C C   . ASP A  1 110 ? 19.386  35.179  226.225 1.00 263.45 ?  140 ASP A C   1 
ATOM   880   O O   . ASP A  1 110 ? 18.187  34.952  226.034 1.00 261.91 ?  140 ASP A O   1 
ATOM   881   C CB  . ASP A  1 110 ? 19.371  35.753  228.656 1.00 267.65 ?  140 ASP A CB  1 
ATOM   882   C CG  . ASP A  1 110 ? 18.128  35.123  229.271 1.00 266.90 ?  140 ASP A CG  1 
ATOM   883   O OD1 . ASP A  1 110 ? 17.440  34.341  228.579 1.00 268.01 ?  140 ASP A OD1 1 
ATOM   884   O OD2 . ASP A  1 110 ? 17.828  35.422  230.446 1.00 265.99 -1 140 ASP A OD2 1 
ATOM   885   N N   . ASP A  1 111 ? 20.186  35.672  225.285 1.00 264.71 ?  141 ASP A N   1 
ATOM   886   C CA  . ASP A  1 111 ? 19.717  36.001  223.952 1.00 259.09 ?  141 ASP A CA  1 
ATOM   887   C C   . ASP A  1 111 ? 19.946  34.846  222.997 1.00 256.00 ?  141 ASP A C   1 
ATOM   888   O O   . ASP A  1 111 ? 19.593  34.948  221.816 1.00 249.78 ?  141 ASP A O   1 
ATOM   889   C CB  . ASP A  1 111 ? 20.374  37.289  223.450 1.00 257.66 ?  141 ASP A CB  1 
ATOM   890   C CG  . ASP A  1 111 ? 20.072  38.477  224.349 1.00 259.83 ?  141 ASP A CG  1 
ATOM   891   O OD1 . ASP A  1 111 ? 18.985  38.490  224.968 1.00 261.58 ?  141 ASP A OD1 1 
ATOM   892   O OD2 . ASP A  1 111 ? 20.908  39.400  224.430 1.00 261.26 -1 141 ASP A OD2 1 
ATOM   893   N N   . MET A  1 112 ? 20.528  33.745  223.487 1.00 251.67 ?  150 MET A N   1 
ATOM   894   C CA  . MET A  1 112 ? 20.742  32.610  222.612 1.00 259.31 ?  150 MET A CA  1 
ATOM   895   C C   . MET A  1 112 ? 19.423  31.899  222.391 1.00 257.34 ?  150 MET A C   1 
ATOM   896   O O   . MET A  1 112 ? 19.319  31.073  221.478 1.00 257.24 ?  150 MET A O   1 
ATOM   897   C CB  . MET A  1 112 ? 21.731  31.618  223.237 1.00 262.70 ?  150 MET A CB  1 
ATOM   898   C CG  . MET A  1 112 ? 23.134  32.133  223.516 1.00 260.16 ?  150 MET A CG  1 
ATOM   899   S SD  . MET A  1 112 ? 24.086  32.572  222.054 1.00 273.05 ?  150 MET A SD  1 
ATOM   900   C CE  . MET A  1 112 ? 25.748  32.479  222.719 1.00 244.27 ?  150 MET A CE  1 
ATOM   901   N N   . ARG A  1 113 ? 18.417  32.249  223.208 1.00 249.86 ?  151 ARG A N   1 
ATOM   902   C CA  . ARG A  1 113 ? 17.050  31.741  223.183 1.00 245.97 ?  151 ARG A CA  1 
ATOM   903   C C   . ARG A  1 113 ? 16.980  30.275  222.767 1.00 249.83 ?  151 ARG A C   1 
ATOM   904   O O   . ARG A  1 113 ? 16.067  29.853  222.048 1.00 246.10 ?  151 ARG A O   1 
ATOM   905   C CB  . ARG A  1 113 ? 16.203  32.702  222.345 1.00 243.59 ?  151 ARG A CB  1 
ATOM   906   C CG  . ARG A  1 113 ? 16.687  32.957  220.935 1.00 239.54 ?  151 ARG A CG  1 
ATOM   907   C CD  . ARG A  1 113 ? 15.735  33.903  220.233 1.00 242.11 ?  151 ARG A CD  1 
ATOM   908   N NE  . ARG A  1 113 ? 14.434  33.300  219.998 1.00 235.95 ?  151 ARG A NE  1 
ATOM   909   C CZ  . ARG A  1 113 ? 14.140  32.569  218.930 1.00 236.05 ?  151 ARG A CZ  1 
ATOM   910   N NH1 . ARG A  1 113 ? 15.060  32.351  217.999 1.00 241.65 1  151 ARG A NH1 1 
ATOM   911   N NH2 . ARG A  1 113 ? 12.927  32.052  218.797 1.00 231.47 ?  151 ARG A NH2 1 
ATOM   912   N N   . GLY A  1 114 ? 17.958  29.507  223.248 1.00 216.41 ?  152 GLY A N   1 
ATOM   913   C CA  . GLY A  1 114 ? 18.091  28.075  223.070 1.00 214.14 ?  152 GLY A CA  1 
ATOM   914   C C   . GLY A  1 114 ? 18.262  27.562  221.656 1.00 215.44 ?  152 GLY A C   1 
ATOM   915   O O   . GLY A  1 114 ? 19.342  27.078  221.301 1.00 218.32 ?  152 GLY A O   1 
ATOM   916   N N   . GLU A  1 115 ? 17.199  27.624  220.855 1.00 204.26 ?  153 GLU A N   1 
ATOM   917   C CA  . GLU A  1 115 ? 17.190  27.109  219.487 1.00 200.82 ?  153 GLU A CA  1 
ATOM   918   C C   . GLU A  1 115 ? 17.406  25.602  219.416 1.00 198.93 ?  153 GLU A C   1 
ATOM   919   O O   . GLU A  1 115 ? 16.588  24.889  218.827 1.00 193.00 ?  153 GLU A O   1 
ATOM   920   C CB  . GLU A  1 115 ? 18.251  27.780  218.617 1.00 201.96 ?  153 GLU A CB  1 
ATOM   921   C CG  . GLU A  1 115 ? 18.286  27.204  217.207 1.00 201.90 ?  153 GLU A CG  1 
ATOM   922   C CD  . GLU A  1 115 ? 19.248  27.928  216.292 1.00 210.85 ?  153 GLU A CD  1 
ATOM   923   O OE1 . GLU A  1 115 ? 19.731  29.013  216.675 1.00 211.99 ?  153 GLU A OE1 1 
ATOM   924   O OE2 . GLU A  1 115 ? 19.543  27.394  215.201 1.00 212.20 -1 153 GLU A OE2 1 
ATOM   925   N N   . LEU A  1 116 ? 18.505  25.103  219.985 1.00 186.87 ?  154 LEU A N   1 
ATOM   926   C CA  . LEU A  1 116 ? 18.770  23.672  220.004 1.00 182.21 ?  154 LEU A CA  1 
ATOM   927   C C   . LEU A  1 116 ? 18.295  23.118  221.344 1.00 182.42 ?  154 LEU A C   1 
ATOM   928   O O   . LEU A  1 116 ? 18.664  23.648  222.397 1.00 186.17 ?  154 LEU A O   1 
ATOM   929   C CB  . LEU A  1 116 ? 20.276  23.460  219.831 1.00 175.25 ?  154 LEU A CB  1 
ATOM   930   C CG  . LEU A  1 116 ? 20.832  23.902  218.469 1.00 172.67 ?  154 LEU A CG  1 
ATOM   931   C CD1 . LEU A  1 116 ? 22.354  23.885  218.437 1.00 162.44 ?  154 LEU A CD1 1 
ATOM   932   C CD2 . LEU A  1 116 ? 20.284  23.073  217.352 1.00 167.29 ?  154 LEU A CD2 1 
ATOM   933   N N   . LYS A  1 117 ? 17.483  22.059  221.310 1.00 183.51 ?  155 LYS A N   1 
ATOM   934   C CA  . LYS A  1 117 ? 16.936  21.459  222.525 1.00 182.46 ?  155 LYS A CA  1 
ATOM   935   C C   . LYS A  1 117 ? 17.382  20.006  222.712 1.00 176.31 ?  155 LYS A C   1 
ATOM   936   O O   . LYS A  1 117 ? 17.355  19.217  221.763 1.00 168.01 ?  155 LYS A O   1 
ATOM   937   C CB  . LYS A  1 117 ? 15.425  21.643  222.586 1.00 177.81 ?  155 LYS A CB  1 
ATOM   938   C CG  . LYS A  1 117 ? 15.171  23.110  222.966 1.00 176.10 ?  155 LYS A CG  1 
ATOM   939   C CD  . LYS A  1 117 ? 15.671  23.403  224.383 1.00 172.34 ?  155 LYS A CD  1 
ATOM   940   C CE  . LYS A  1 117 ? 15.343  24.816  224.852 1.00 173.27 ?  155 LYS A CE  1 
ATOM   941   N NZ  . LYS A  1 117 ? 15.797  25.070  226.255 1.00 174.53 1  155 LYS A NZ  1 
ATOM   942   N N   . ASN A  1 118 ? 17.781  19.655  223.940 1.00 188.55 ?  156 ASN A N   1 
ATOM   943   C CA  . ASN A  1 118 ? 18.196  18.293  224.315 1.00 179.16 ?  156 ASN A CA  1 
ATOM   944   C C   . ASN A  1 118 ? 17.060  17.474  224.947 1.00 179.25 ?  156 ASN A C   1 
ATOM   945   O O   . ASN A  1 118 ? 16.864  17.480  226.163 1.00 184.12 ?  156 ASN A O   1 
ATOM   946   C CB  . ASN A  1 118 ? 19.396  18.370  225.251 1.00 176.63 ?  156 ASN A CB  1 
ATOM   947   C CG  . ASN A  1 118 ? 20.040  17.028  225.470 1.00 163.72 ?  156 ASN A CG  1 
ATOM   948   O OD1 . ASN A  1 118 ? 19.686  16.050  224.815 1.00 157.44 ?  156 ASN A OD1 1 
ATOM   949   N ND2 . ASN A  1 118 ? 20.991  16.966  226.393 1.00 162.70 ?  156 ASN A ND2 1 
ATOM   950   N N   . CYS A  1 119 ? 16.305  16.774  224.089 1.00 173.43 ?  157 CYS A N   1 
ATOM   951   C CA  . CYS A  1 119 ? 15.093  16.016  224.428 1.00 170.81 ?  157 CYS A CA  1 
ATOM   952   C C   . CYS A  1 119 ? 15.283  14.543  224.796 1.00 163.33 ?  157 CYS A C   1 
ATOM   953   O O   . CYS A  1 119 ? 15.982  13.805  224.095 1.00 154.31 ?  157 CYS A O   1 
ATOM   954   C CB  . CYS A  1 119 ? 14.095  16.113  223.275 1.00 166.12 ?  157 CYS A CB  1 
ATOM   955   S SG  . CYS A  1 119 ? 13.857  17.785  222.697 1.00 203.55 ?  157 CYS A SG  1 
ATOM   956   N N   . SER A  1 120 ? 14.663  14.132  225.912 1.00 165.51 ?  158 SER A N   1 
ATOM   957   C CA  . SER A  1 120 ? 14.606  12.745  226.377 1.00 159.05 ?  158 SER A CA  1 
ATOM   958   C C   . SER A  1 120 ? 13.170  12.208  226.351 1.00 155.03 ?  158 SER A C   1 
ATOM   959   O O   . SER A  1 120 ? 12.229  12.928  226.707 1.00 157.77 ?  158 SER A O   1 
ATOM   960   C CB  . SER A  1 120 ? 15.159  12.640  227.803 1.00 164.40 ?  158 SER A CB  1 
ATOM   961   O OG  . SER A  1 120 ? 16.524  13.017  227.866 1.00 166.95 ?  158 SER A OG  1 
ATOM   962   N N   . PHE A  1 121 ? 12.997  10.945  225.930 1.00 162.52 ?  159 PHE A N   1 
ATOM   963   C CA  . PHE A  1 121 ? 11.662  10.359  225.775 1.00 159.03 ?  159 PHE A CA  1 
ATOM   964   C C   . PHE A  1 121 ? 11.727  8.829   225.782 1.00 159.91 ?  159 PHE A C   1 
ATOM   965   O O   . PHE A  1 121 ? 12.801  8.232   225.681 1.00 159.90 ?  159 PHE A O   1 
ATOM   966   C CB  . PHE A  1 121 ? 11.010  10.833  224.479 1.00 157.45 ?  159 PHE A CB  1 
ATOM   967   C CG  . PHE A  1 121 ? 11.863  10.606  223.267 1.00 155.81 ?  159 PHE A CG  1 
ATOM   968   C CD1 . PHE A  1 121 ? 12.778  11.557  222.843 1.00 154.68 ?  159 PHE A CD1 1 
ATOM   969   C CD2 . PHE A  1 121 ? 11.746  9.429   222.549 1.00 155.66 ?  159 PHE A CD2 1 
ATOM   970   C CE1 . PHE A  1 121 ? 13.560  11.330  221.726 1.00 153.40 ?  159 PHE A CE1 1 
ATOM   971   C CE2 . PHE A  1 121 ? 12.520  9.197   221.437 1.00 154.40 ?  159 PHE A CE2 1 
ATOM   972   C CZ  . PHE A  1 121 ? 13.428  10.147  221.023 1.00 153.26 ?  159 PHE A CZ  1 
ATOM   973   N N   . ASN A  1 122 ? 10.547  8.203   225.920 1.00 165.44 ?  160 ASN A N   1 
ATOM   974   C CA  . ASN A  1 122 ? 10.365  6.754   225.828 1.00 166.47 ?  160 ASN A CA  1 
ATOM   975   C C   . ASN A  1 122 ? 10.271  6.306   224.367 1.00 165.04 ?  160 ASN A C   1 
ATOM   976   O O   . ASN A  1 122 ? 9.873   7.072   223.485 1.00 163.52 ?  160 ASN A O   1 
ATOM   977   C CB  . ASN A  1 122 ? 9.103   6.306   226.566 1.00 168.39 ?  160 ASN A CB  1 
ATOM   978   C CG  . ASN A  1 122 ? 9.335   6.083   228.046 1.00 174.23 ?  160 ASN A CG  1 
ATOM   979   O OD1 . ASN A  1 122 ? 9.916   5.077   228.458 1.00 172.03 ?  160 ASN A OD1 1 
ATOM   980   N ND2 . ASN A  1 122 ? 8.869   7.016   228.856 1.00 171.20 ?  160 ASN A ND2 1 
ATOM   981   N N   . MET A  1 123 ? 10.623  5.041   224.116 1.00 166.69 ?  161 MET A N   1 
ATOM   982   C CA  . MET A  1 123 ? 10.590  4.533   222.750 1.00 167.63 ?  161 MET A CA  1 
ATOM   983   C C   . MET A  1 123 ? 10.404  3.019   222.687 1.00 171.37 ?  161 MET A C   1 
ATOM   984   O O   . MET A  1 123 ? 10.839  2.286   223.578 1.00 173.42 ?  161 MET A O   1 
ATOM   985   C CB  . MET A  1 123 ? 11.839  4.953   221.975 1.00 165.11 ?  161 MET A CB  1 
ATOM   986   C CG  . MET A  1 123 ? 11.753  4.577   220.518 1.00 165.56 ?  161 MET A CG  1 
ATOM   987   S SD  . MET A  1 123 ? 10.121  5.031   219.891 1.00 189.02 ?  161 MET A SD  1 
ATOM   988   C CE  . MET A  1 123 ? 10.152  6.799   220.137 1.00 161.76 ?  161 MET A CE  1 
ATOM   989   N N   . THR A  1 124 ? 9.702   2.570   221.640 1.00 158.86 ?  162 THR A N   1 
ATOM   990   C CA  . THR A  1 124 ? 9.451   1.151   221.407 1.00 162.07 ?  162 THR A CA  1 
ATOM   991   C C   . THR A  1 124 ? 10.656  0.489   220.745 1.00 164.27 ?  162 THR A C   1 
ATOM   992   O O   . THR A  1 124 ? 11.138  0.956   219.708 1.00 162.76 ?  162 THR A O   1 
ATOM   993   C CB  . THR A  1 124 ? 8.231   0.962   220.507 1.00 161.04 ?  162 THR A CB  1 
ATOM   994   O OG1 . THR A  1 124 ? 7.098   1.629   221.074 1.00 157.68 ?  162 THR A OG1 1 
ATOM   995   C CG2 . THR A  1 124 ? 7.926   -0.521  220.322 1.00 163.87 ?  162 THR A CG2 1 
ATOM   996   N N   . THR A  1 125 ? 11.135  -0.601  221.345 1.00 168.46 ?  163 THR A N   1 
ATOM   997   C CA  . THR A  1 125 ? 12.258  -1.370  220.817 1.00 170.48 ?  163 THR A CA  1 
ATOM   998   C C   . THR A  1 125 ? 11.779  -2.353  219.757 1.00 173.13 ?  163 THR A C   1 
ATOM   999   O O   . THR A  1 125 ? 10.671  -2.218  219.226 1.00 172.20 ?  163 THR A O   1 
ATOM   1000  C CB  . THR A  1 125 ? 12.970  -2.140  221.933 1.00 172.72 ?  163 THR A CB  1 
ATOM   1001  O OG1 . THR A  1 125 ? 12.047  -3.039  222.562 1.00 175.56 ?  163 THR A OG1 1 
ATOM   1002  C CG2 . THR A  1 125 ? 13.517  -1.189  222.977 1.00 169.75 ?  163 THR A CG2 1 
ATOM   1003  N N   . GLU A  1 126 ? 12.612  -3.348  219.442 1.00 167.58 ?  164 GLU A N   1 
ATOM   1004  C CA  . GLU A  1 126 ? 12.195  -4.368  218.487 1.00 170.28 ?  164 GLU A CA  1 
ATOM   1005  C C   . GLU A  1 126 ? 11.047  -5.180  219.065 1.00 171.49 ?  164 GLU A C   1 
ATOM   1006  O O   . GLU A  1 126 ? 10.096  -5.526  218.355 1.00 171.12 ?  164 GLU A O   1 
ATOM   1007  C CB  . GLU A  1 126 ? 13.345  -5.306  218.113 1.00 172.75 ?  164 GLU A CB  1 
ATOM   1008  C CG  . GLU A  1 126 ? 14.552  -4.683  217.441 1.00 170.19 ?  164 GLU A CG  1 
ATOM   1009  C CD  . GLU A  1 126 ? 15.516  -4.065  218.428 1.00 167.18 ?  164 GLU A CD  1 
ATOM   1010  O OE1 . GLU A  1 126 ? 15.189  -4.012  219.634 1.00 167.56 ?  164 GLU A OE1 1 
ATOM   1011  O OE2 . GLU A  1 126 ? 16.618  -3.665  217.999 1.00 164.09 -1 164 GLU A OE2 1 
ATOM   1012  N N   . LEU A  1 127 ? 11.123  -5.483  220.355 1.00 169.24 ?  165 LEU A N   1 
ATOM   1013  C CA  . LEU A  1 127 ? 10.099  -6.228  221.063 1.00 169.81 ?  165 LEU A CA  1 
ATOM   1014  C C   . LEU A  1 127 ? 8.941   -5.324  221.485 1.00 166.22 ?  165 LEU A C   1 
ATOM   1015  O O   . LEU A  1 127 ? 9.078   -4.106  221.642 1.00 163.69 ?  165 LEU A O   1 
ATOM   1016  C CB  . LEU A  1 127 ? 10.698  -6.920  222.290 1.00 172.25 ?  165 LEU A CB  1 
ATOM   1017  C CG  . LEU A  1 127 ? 11.661  -8.081  222.010 1.00 175.49 ?  165 LEU A CG  1 
ATOM   1018  C CD1 . LEU A  1 127 ? 13.072  -7.600  221.662 1.00 175.42 ?  165 LEU A CD1 1 
ATOM   1019  C CD2 . LEU A  1 127 ? 11.685  -9.043  223.191 1.00 177.60 ?  165 LEU A CD2 1 
ATOM   1020  N N   . ARG A  1 128 ? 7.785   -5.962  221.678 1.00 183.98 ?  166 ARG A N   1 
ATOM   1021  C CA  . ARG A  1 128 ? 6.516   -5.332  222.015 1.00 181.24 ?  166 ARG A CA  1 
ATOM   1022  C C   . ARG A  1 128 ? 6.271   -5.306  223.521 1.00 183.53 ?  166 ARG A C   1 
ATOM   1023  O O   . ARG A  1 128 ? 5.119   -5.262  223.977 1.00 184.93 ?  166 ARG A O   1 
ATOM   1024  C CB  . ARG A  1 128 ? 5.448   -6.180  221.310 1.00 179.61 ?  166 ARG A CB  1 
ATOM   1025  C CG  . ARG A  1 128 ? 4.090   -5.717  220.852 1.00 181.83 ?  166 ARG A CG  1 
ATOM   1026  C CD  . ARG A  1 128 ? 3.869   -4.310  220.483 1.00 184.89 ?  166 ARG A CD  1 
ATOM   1027  N NE  . ARG A  1 128 ? 2.488   -4.271  220.038 1.00 186.52 ?  166 ARG A NE  1 
ATOM   1028  C CZ  . ARG A  1 128 ? 1.452   -4.300  220.853 1.00 185.63 ?  166 ARG A CZ  1 
ATOM   1029  N NH1 . ARG A  1 128 ? 1.636   -4.370  222.155 1.00 185.11 1  166 ARG A NH1 1 
ATOM   1030  N NH2 . ARG A  1 128 ? 0.233   -4.287  220.366 1.00 187.40 ?  166 ARG A NH2 1 
ATOM   1031  N N   . ASP A  1 129 ? 7.338   -5.319  224.315 1.00 166.50 ?  167 ASP A N   1 
ATOM   1032  C CA  . ASP A  1 129 ? 7.233   -5.327  225.772 1.00 166.77 ?  167 ASP A CA  1 
ATOM   1033  C C   . ASP A  1 129 ? 7.896   -4.155  226.484 1.00 180.65 ?  167 ASP A C   1 
ATOM   1034  O O   . ASP A  1 129 ? 7.306   -3.085  226.676 1.00 168.38 ?  167 ASP A O   1 
ATOM   1035  C CB  . ASP A  1 129 ? 7.748   -6.652  226.320 1.00 169.45 ?  167 ASP A CB  1 
ATOM   1036  C CG  . ASP A  1 129 ? 6.946   -7.826  225.806 1.00 168.53 ?  167 ASP A CG  1 
ATOM   1037  O OD1 . ASP A  1 129 ? 6.850   -7.959  224.572 1.00 169.98 ?  167 ASP A OD1 1 
ATOM   1038  O OD2 . ASP A  1 129 ? 6.416   -8.609  226.625 1.00 169.34 -1 167 ASP A OD2 1 
ATOM   1039  N N   . LYS A  1 130 ? 9.147   -4.412  226.873 1.00 181.43 ?  168 LYS A N   1 
ATOM   1040  C CA  . LYS A  1 130 ? 10.002  -3.504  227.629 1.00 186.75 ?  168 LYS A CA  1 
ATOM   1041  C C   . LYS A  1 130 ? 10.246  -2.227  226.827 1.00 177.85 ?  168 LYS A C   1 
ATOM   1042  O O   . LYS A  1 130 ? 10.370  -2.262  225.599 1.00 171.96 ?  168 LYS A O   1 
ATOM   1043  C CB  . LYS A  1 130 ? 11.317  -4.227  227.952 1.00 195.77 ?  168 LYS A CB  1 
ATOM   1044  C CG  . LYS A  1 130 ? 11.125  -5.490  228.817 1.00 196.90 ?  168 LYS A CG  1 
ATOM   1045  C CD  . LYS A  1 130 ? 12.437  -6.189  229.173 1.00 199.74 ?  168 LYS A CD  1 
ATOM   1046  C CE  . LYS A  1 130 ? 12.192  -7.414  230.053 1.00 205.79 ?  168 LYS A CE  1 
ATOM   1047  N NZ  . LYS A  1 130 ? 13.456  -8.110  230.423 1.00 206.46 1  168 LYS A NZ  1 
ATOM   1048  N N   . LYS A  1 131 ? 10.300  -1.086  227.529 1.00 193.44 ?  169 LYS A N   1 
ATOM   1049  C CA  . LYS A  1 131 ? 10.451  0.199   226.847 1.00 182.21 ?  169 LYS A CA  1 
ATOM   1050  C C   . LYS A  1 131 ? 11.877  0.619   226.482 1.00 177.35 ?  169 LYS A C   1 
ATOM   1051  O O   . LYS A  1 131 ? 12.779  -0.222  226.402 1.00 180.41 ?  169 LYS A O   1 
ATOM   1052  C CB  . LYS A  1 131 ? 9.923   1.263   227.818 1.00 184.78 ?  169 LYS A CB  1 
ATOM   1053  C CG  . LYS A  1 131 ? 8.484   1.108   228.316 1.00 177.63 ?  169 LYS A CG  1 
ATOM   1054  C CD  . LYS A  1 131 ? 8.526   0.368   229.667 1.00 176.96 ?  169 LYS A CD  1 
ATOM   1055  C CE  . LYS A  1 131 ? 9.340   1.117   230.712 1.00 171.83 ?  169 LYS A CE  1 
ATOM   1056  N NZ  . LYS A  1 131 ? 9.373   0.382   232.012 1.00 178.90 1  169 LYS A NZ  1 
ATOM   1057  N N   . GLN A  1 132 ? 12.090  1.924   226.268 1.00 155.36 ?  170 GLN A N   1 
ATOM   1058  C CA  . GLN A  1 132 ? 13.412  2.435   225.891 1.00 154.83 ?  170 GLN A CA  1 
ATOM   1059  C C   . GLN A  1 132 ? 13.527  3.926   226.196 1.00 153.98 ?  170 GLN A C   1 
ATOM   1060  O O   . GLN A  1 132 ? 12.791  4.725   225.611 1.00 151.94 ?  170 GLN A O   1 
ATOM   1061  C CB  . GLN A  1 132 ? 13.723  2.158   224.433 1.00 152.83 ?  170 GLN A CB  1 
ATOM   1062  C CG  . GLN A  1 132 ? 15.166  2.428   224.101 1.00 152.85 ?  170 GLN A CG  1 
ATOM   1063  C CD  . GLN A  1 132 ? 15.493  2.114   222.666 1.00 151.11 ?  170 GLN A CD  1 
ATOM   1064  O OE1 . GLN A  1 132 ? 14.632  1.679   221.902 1.00 150.74 ?  170 GLN A OE1 1 
ATOM   1065  N NE2 . GLN A  1 132 ? 16.749  2.307   222.293 1.00 151.18 ?  170 GLN A NE2 1 
ATOM   1066  N N   . LYS A  1 133 ? 14.422  4.300   227.113 1.00 161.60 ?  171 LYS A N   1 
ATOM   1067  C CA  . LYS A  1 133 ? 14.667  5.695   227.513 1.00 163.16 ?  171 LYS A CA  1 
ATOM   1068  C C   . LYS A  1 133 ? 15.800  6.309   226.671 1.00 161.21 ?  171 LYS A C   1 
ATOM   1069  O O   . LYS A  1 133 ? 16.956  6.360   227.095 1.00 162.52 ?  171 LYS A O   1 
ATOM   1070  C CB  . LYS A  1 133 ? 14.968  5.758   229.008 1.00 164.98 ?  171 LYS A CB  1 
ATOM   1071  C CG  . LYS A  1 133 ? 13.741  5.608   229.936 1.00 160.23 ?  171 LYS A CG  1 
ATOM   1072  C CD  . LYS A  1 133 ? 12.868  6.863   230.018 1.00 158.27 ?  171 LYS A CD  1 
ATOM   1073  C CE  . LYS A  1 133 ? 13.517  7.962   230.861 1.00 162.70 ?  171 LYS A CE  1 
ATOM   1074  N NZ  . LYS A  1 133 ? 12.598  9.121   231.065 1.00 159.44 1  171 LYS A NZ  1 
ATOM   1075  N N   . VAL A  1 134 ? 15.485  6.772   225.451 1.00 155.50 ?  172 VAL A N   1 
ATOM   1076  C CA  . VAL A  1 134 ? 16.511  7.371   224.584 1.00 152.72 ?  172 VAL A CA  1 
ATOM   1077  C C   . VAL A  1 134 ? 16.314  8.878   224.407 1.00 151.68 ?  172 VAL A C   1 
ATOM   1078  O O   . VAL A  1 134 ? 15.208  9.409   224.546 1.00 150.60 ?  172 VAL A O   1 
ATOM   1079  C CB  . VAL A  1 134 ? 16.512  6.694   223.198 1.00 152.52 ?  172 VAL A CB  1 
ATOM   1080  C CG1 . VAL A  1 134 ? 17.164  5.335   223.274 1.00 154.16 ?  172 VAL A CG1 1 
ATOM   1081  C CG2 . VAL A  1 134 ? 15.086  6.606   222.648 1.00 151.04 ?  172 VAL A CG2 1 
ATOM   1082  N N   . TYR A  1 135 ? 17.422  9.577   224.087 1.00 157.83 ?  173 TYR A N   1 
ATOM   1083  C CA  . TYR A  1 135 ? 17.418  11.029  223.906 1.00 158.05 ?  173 TYR A CA  1 
ATOM   1084  C C   . TYR A  1 135 ? 17.821  11.426  222.485 1.00 163.83 ?  173 TYR A C   1 
ATOM   1085  O O   . TYR A  1 135 ? 18.537  10.688  221.801 1.00 165.26 ?  173 TYR A O   1 
ATOM   1086  C CB  . TYR A  1 135 ? 18.356  11.748  224.909 1.00 164.62 ?  173 TYR A CB  1 
ATOM   1087  C CG  . TYR A  1 135 ? 19.866  11.684  224.673 1.00 175.98 ?  173 TYR A CG  1 
ATOM   1088  C CD1 . TYR A  1 135 ? 20.631  10.574  225.027 1.00 180.96 ?  173 TYR A CD1 1 
ATOM   1089  C CD2 . TYR A  1 135 ? 20.532  12.789  224.147 1.00 179.85 ?  173 TYR A CD2 1 
ATOM   1090  C CE1 . TYR A  1 135 ? 22.015  10.562  224.823 1.00 185.84 ?  173 TYR A CE1 1 
ATOM   1091  C CE2 . TYR A  1 135 ? 21.901  12.784  223.943 1.00 185.85 ?  173 TYR A CE2 1 
ATOM   1092  C CZ  . TYR A  1 135 ? 22.639  11.672  224.281 1.00 191.27 ?  173 TYR A CZ  1 
ATOM   1093  O OH  . TYR A  1 135 ? 24.004  11.666  224.078 1.00 197.60 ?  173 TYR A OH  1 
ATOM   1094  N N   . SER A  1 136 ? 17.353  12.601  222.043 1.00 163.72 ?  174 SER A N   1 
ATOM   1095  C CA  . SER A  1 136 ? 17.704  13.161  220.731 1.00 161.63 ?  174 SER A CA  1 
ATOM   1096  C C   . SER A  1 136 ? 18.017  14.657  220.867 1.00 164.00 ?  174 SER A C   1 
ATOM   1097  O O   . SER A  1 136 ? 18.068  15.208  221.972 1.00 164.00 ?  174 SER A O   1 
ATOM   1098  C CB  . SER A  1 136 ? 16.588  12.907  219.711 1.00 155.87 ?  174 SER A CB  1 
ATOM   1099  O OG  . SER A  1 136 ? 16.921  13.473  218.456 1.00 156.38 ?  174 SER A OG  1 
ATOM   1100  N N   . LEU A  1 137 ? 18.236  15.313  219.716 1.00 158.15 ?  175 LEU A N   1 
ATOM   1101  C CA  . LEU A  1 137 ? 18.559  16.746  219.625 1.00 160.36 ?  175 LEU A CA  1 
ATOM   1102  C C   . LEU A  1 137 ? 17.775  17.386  218.475 1.00 157.15 ?  175 LEU A C   1 
ATOM   1103  O O   . LEU A  1 137 ? 18.127  17.196  217.306 1.00 155.72 ?  175 LEU A O   1 
ATOM   1104  C CB  . LEU A  1 137 ? 20.055  16.967  219.455 1.00 161.85 ?  175 LEU A CB  1 
ATOM   1105  C CG  . LEU A  1 137 ? 20.528  18.338  219.951 1.00 159.89 ?  175 LEU A CG  1 
ATOM   1106  C CD1 . LEU A  1 137 ? 20.442  18.436  221.470 1.00 163.53 ?  175 LEU A CD1 1 
ATOM   1107  C CD2 . LEU A  1 137 ? 21.930  18.659  219.460 1.00 166.25 ?  175 LEU A CD2 1 
ATOM   1108  N N   . PHE A  1 138 ? 16.721  18.135  218.794 1.00 156.42 ?  176 PHE A N   1 
ATOM   1109  C CA  . PHE A  1 138 ? 15.863  18.774  217.801 1.00 150.73 ?  176 PHE A CA  1 
ATOM   1110  C C   . PHE A  1 138 ? 16.011  20.292  217.749 1.00 150.65 ?  176 PHE A C   1 
ATOM   1111  O O   . PHE A  1 138 ? 16.392  20.937  218.730 1.00 153.47 ?  176 PHE A O   1 
ATOM   1112  C CB  . PHE A  1 138 ? 14.403  18.414  218.048 1.00 151.06 ?  176 PHE A CB  1 
ATOM   1113  C CG  . PHE A  1 138 ? 14.163  16.948  218.058 1.00 151.33 ?  176 PHE A CG  1 
ATOM   1114  C CD1 . PHE A  1 138 ? 14.136  16.244  216.869 1.00 152.88 ?  176 PHE A CD1 1 
ATOM   1115  C CD2 . PHE A  1 138 ? 14.001  16.263  219.247 1.00 151.44 ?  176 PHE A CD2 1 
ATOM   1116  C CE1 . PHE A  1 138 ? 13.931  14.887  216.862 1.00 153.11 ?  176 PHE A CE1 1 
ATOM   1117  C CE2 . PHE A  1 138 ? 13.792  14.902  219.248 1.00 146.94 ?  176 PHE A CE2 1 
ATOM   1118  C CZ  . PHE A  1 138 ? 13.758  14.212  218.053 1.00 148.62 ?  176 PHE A CZ  1 
ATOM   1119  N N   . TYR A  1 139 ? 15.704  20.849  216.576 1.00 143.50 ?  177 TYR A N   1 
ATOM   1120  C CA  . TYR A  1 139 ? 15.712  22.287  216.369 1.00 146.66 ?  177 TYR A CA  1 
ATOM   1121  C C   . TYR A  1 139 ? 14.462  22.892  217.009 1.00 149.31 ?  177 TYR A C   1 
ATOM   1122  O O   . TYR A  1 139 ? 13.463  22.206  217.243 1.00 147.41 ?  177 TYR A O   1 
ATOM   1123  C CB  . TYR A  1 139 ? 15.787  22.564  214.870 1.00 144.64 ?  177 TYR A CB  1 
ATOM   1124  C CG  . TYR A  1 139 ? 17.066  22.015  214.261 1.00 146.37 ?  177 TYR A CG  1 
ATOM   1125  C CD1 . TYR A  1 139 ? 17.089  21.497  212.976 1.00 148.92 ?  177 TYR A CD1 1 
ATOM   1126  C CD2 . TYR A  1 139 ? 18.258  22.043  214.964 1.00 147.80 ?  177 TYR A CD2 1 
ATOM   1127  C CE1 . TYR A  1 139 ? 18.258  21.001  212.420 1.00 148.19 ?  177 TYR A CE1 1 
ATOM   1128  C CE2 . TYR A  1 139 ? 19.436  21.555  214.412 1.00 147.89 ?  177 TYR A CE2 1 
ATOM   1129  C CZ  . TYR A  1 139 ? 19.431  21.039  213.140 1.00 147.18 ?  177 TYR A CZ  1 
ATOM   1130  O OH  . TYR A  1 139 ? 20.599  20.551  212.595 1.00 144.72 ?  177 TYR A OH  1 
ATOM   1131  N N   . ARG A  1 140 ? 14.515  24.200  217.280 1.00 177.82 ?  178 ARG A N   1 
ATOM   1132  C CA  . ARG A  1 140 ? 13.374  24.848  217.925 1.00 178.15 ?  178 ARG A CA  1 
ATOM   1133  C C   . ARG A  1 140 ? 12.124  24.876  217.042 1.00 174.13 ?  178 ARG A C   1 
ATOM   1134  O O   . ARG A  1 140 ? 11.002  24.806  217.560 1.00 170.54 ?  178 ARG A O   1 
ATOM   1135  C CB  . ARG A  1 140 ? 13.792  26.249  218.380 1.00 177.48 ?  178 ARG A CB  1 
ATOM   1136  C CG  . ARG A  1 140 ? 12.737  27.069  219.097 1.00 169.90 ?  178 ARG A CG  1 
ATOM   1137  C CD  . ARG A  1 140 ? 12.557  26.362  220.458 1.00 175.95 ?  178 ARG A CD  1 
ATOM   1138  N NE  . ARG A  1 140 ? 11.989  27.146  221.556 1.00 184.21 ?  178 ARG A NE  1 
ATOM   1139  C CZ  . ARG A  1 140 ? 12.710  27.928  222.358 1.00 190.08 ?  178 ARG A CZ  1 
ATOM   1140  N NH1 . ARG A  1 140 ? 12.130  28.601  223.343 1.00 194.23 1  178 ARG A NH1 1 
ATOM   1141  N NH2 . ARG A  1 140 ? 14.024  28.010  222.197 1.00 197.19 ?  178 ARG A NH2 1 
ATOM   1142  N N   . LEU A  1 141 ? 12.291  24.984  215.720 1.00 157.68 ?  179 LEU A N   1 
ATOM   1143  C CA  . LEU A  1 141 ? 11.179  25.004  214.767 1.00 153.01 ?  179 LEU A CA  1 
ATOM   1144  C C   . LEU A  1 141 ? 10.492  23.658  214.603 1.00 152.96 ?  179 LEU A C   1 
ATOM   1145  O O   . LEU A  1 141 ? 9.393   23.606  214.042 1.00 152.66 ?  179 LEU A O   1 
ATOM   1146  C CB  . LEU A  1 141 ? 11.632  25.517  213.406 1.00 155.16 ?  179 LEU A CB  1 
ATOM   1147  C CG  . LEU A  1 141 ? 12.275  26.896  213.490 1.00 156.11 ?  179 LEU A CG  1 
ATOM   1148  C CD1 . LEU A  1 141 ? 13.542  26.890  212.697 1.00 160.31 ?  179 LEU A CD1 1 
ATOM   1149  C CD2 . LEU A  1 141 ? 11.326  27.971  212.998 1.00 158.06 ?  179 LEU A CD2 1 
ATOM   1150  N N   . ASP A  1 142 ? 11.109  22.579  215.070 1.00 162.44 ?  180 ASP A N   1 
ATOM   1151  C CA  . ASP A  1 142 ? 10.558  21.237  214.941 1.00 161.05 ?  180 ASP A CA  1 
ATOM   1152  C C   . ASP A  1 142 ? 9.709   20.822  216.127 1.00 158.45 ?  180 ASP A C   1 
ATOM   1153  O O   . ASP A  1 142 ? 8.902   19.893  215.995 1.00 157.18 ?  180 ASP A O   1 
ATOM   1154  C CB  . ASP A  1 142 ? 11.686  20.214  214.772 1.00 163.05 ?  180 ASP A CB  1 
ATOM   1155  C CG  . ASP A  1 142 ? 12.447  20.388  213.477 1.00 166.23 ?  180 ASP A CG  1 
ATOM   1156  O OD1 . ASP A  1 142 ? 11.805  20.694  212.455 1.00 164.84 ?  180 ASP A OD1 1 
ATOM   1157  O OD2 . ASP A  1 142 ? 13.687  20.230  213.486 1.00 173.10 -1 180 ASP A OD2 1 
ATOM   1158  N N   . VAL A  1 143 ? 9.877   21.467  217.275 1.00 151.10 ?  181 VAL A N   1 
ATOM   1159  C CA  . VAL A  1 143 ? 9.174   21.089  218.489 1.00 145.76 ?  181 VAL A CA  1 
ATOM   1160  C C   . VAL A  1 143 ? 8.238   22.221  218.902 1.00 142.35 ?  181 VAL A C   1 
ATOM   1161  O O   . VAL A  1 143 ? 8.309   23.342  218.397 1.00 142.00 ?  181 VAL A O   1 
ATOM   1162  C CB  . VAL A  1 143 ? 10.150  20.753  219.629 1.00 145.62 ?  181 VAL A CB  1 
ATOM   1163  C CG1 . VAL A  1 143 ? 10.960  19.517  219.277 1.00 150.96 ?  181 VAL A CG1 1 
ATOM   1164  C CG2 . VAL A  1 143 ? 11.071  21.942  219.892 1.00 149.43 ?  181 VAL A CG2 1 
ATOM   1165  N N   . VAL A  1 144 ? 7.351   21.904  219.842 1.00 150.15 ?  182 VAL A N   1 
ATOM   1166  C CA  . VAL A  1 144 ? 6.417   22.878  220.393 1.00 152.45 ?  182 VAL A CA  1 
ATOM   1167  C C   . VAL A  1 144 ? 5.940   22.374  221.749 1.00 157.25 ?  182 VAL A C   1 
ATOM   1168  O O   . VAL A  1 144 ? 5.474   21.238  221.879 1.00 158.17 ?  182 VAL A O   1 
ATOM   1169  C CB  . VAL A  1 144 ? 5.235   23.133  219.439 1.00 150.62 ?  182 VAL A CB  1 
ATOM   1170  C CG1 . VAL A  1 144 ? 4.663   21.815  218.947 1.00 148.03 ?  182 VAL A CG1 1 
ATOM   1171  C CG2 . VAL A  1 144 ? 4.161   23.959  220.135 1.00 153.87 ?  182 VAL A CG2 1 
ATOM   1172  N N   . GLN A  1 145 ? 6.081   23.218  222.766 1.00 145.47 ?  183 GLN A N   1 
ATOM   1173  C CA  . GLN A  1 145 ? 5.730   22.862  224.129 1.00 152.62 ?  183 GLN A CA  1 
ATOM   1174  C C   . GLN A  1 145 ? 4.216   22.738  224.293 1.00 155.45 ?  183 GLN A C   1 
ATOM   1175  O O   . GLN A  1 145 ? 3.429   23.252  223.493 1.00 153.69 ?  183 GLN A O   1 
ATOM   1176  C CB  . GLN A  1 145 ? 6.318   23.888  225.096 1.00 161.78 ?  183 GLN A CB  1 
ATOM   1177  C CG  . GLN A  1 145 ? 5.905   25.321  224.804 1.00 163.61 ?  183 GLN A CG  1 
ATOM   1178  C CD  . GLN A  1 145 ? 6.535   26.321  225.755 1.00 166.67 ?  183 GLN A CD  1 
ATOM   1179  O OE1 . GLN A  1 145 ? 7.215   25.945  226.710 1.00 166.25 ?  183 GLN A OE1 1 
ATOM   1180  N NE2 . GLN A  1 145 ? 6.326   27.605  225.485 1.00 174.58 ?  183 GLN A NE2 1 
ATOM   1181  N N   . ILE A  1 146 ? 3.811   22.041  225.351 1.00 153.55 ?  184 ILE A N   1 
ATOM   1182  C CA  . ILE A  1 146 ? 2.393   21.843  225.642 1.00 155.09 ?  184 ILE A CA  1 
ATOM   1183  C C   . ILE A  1 146 ? 2.215   21.734  227.152 1.00 165.32 ?  184 ILE A C   1 
ATOM   1184  O O   . ILE A  1 146 ? 2.925   20.973  227.817 1.00 163.34 ?  184 ILE A O   1 
ATOM   1185  C CB  . ILE A  1 146 ? 1.834   20.602  224.912 1.00 153.32 ?  184 ILE A CB  1 
ATOM   1186  C CG1 . ILE A  1 146 ? 0.410   20.295  225.379 1.00 155.79 ?  184 ILE A CG1 1 
ATOM   1187  C CG2 . ILE A  1 146 ? 2.756   19.395  225.093 1.00 151.40 ?  184 ILE A CG2 1 
ATOM   1188  C CD1 . ILE A  1 146 ? -0.598  21.369  225.013 1.00 157.80 ?  184 ILE A CD1 1 
ATOM   1189  N N   . ASN A  1 147 ? 1.273   22.503  227.692 1.00 176.20 ?  185 ASN A N   1 
ATOM   1190  C CA  . ASN A  1 147 ? 0.982   22.485  229.123 1.00 184.48 ?  185 ASN A CA  1 
ATOM   1191  C C   . ASN A  1 147 ? -0.414  21.921  229.400 1.00 189.28 ?  185 ASN A C   1 
ATOM   1192  O O   . ASN A  1 147 ? -0.685  20.741  229.165 1.00 188.32 ?  185 ASN A O   1 
ATOM   1193  C CB  . ASN A  1 147 ? 1.106   23.896  229.708 1.00 192.40 ?  185 ASN A CB  1 
ATOM   1194  C CG  . ASN A  1 147 ? 0.900   23.927  231.210 1.00 200.59 ?  185 ASN A CG  1 
ATOM   1195  O OD1 . ASN A  1 147 ? 1.111   22.929  231.899 1.00 202.51 ?  185 ASN A OD1 1 
ATOM   1196  N ND2 . ASN A  1 147 ? 0.475   25.076  231.725 1.00 206.94 ?  185 ASN A ND2 1 
ATOM   1197  N N   . SER A  1 157 ? 8.005   19.909  238.055 1.00 249.99 ?  187 SER A N   1 
ATOM   1198  C CA  . SER A  1 157 ? 7.864   19.264  236.753 1.00 253.35 ?  187 SER A CA  1 
ATOM   1199  C C   . SER A  1 157 ? 8.688   19.987  235.680 1.00 257.30 ?  187 SER A C   1 
ATOM   1200  O O   . SER A  1 157 ? 8.846   21.207  235.726 1.00 261.13 ?  187 SER A O   1 
ATOM   1201  C CB  . SER A  1 157 ? 6.387   19.207  236.349 1.00 254.11 ?  187 SER A CB  1 
ATOM   1202  O OG  . SER A  1 157 ? 6.158   18.228  235.350 1.00 252.79 ?  187 SER A OG  1 
ATOM   1203  N N   . ASN A  1 158 ? 9.209   19.228  234.716 1.00 254.35 ?  188 ASN A N   1 
ATOM   1204  C CA  . ASN A  1 158 ? 10.053  19.781  233.666 1.00 247.29 ?  188 ASN A CA  1 
ATOM   1205  C C   . ASN A  1 158 ? 9.196   20.485  232.614 1.00 241.35 ?  188 ASN A C   1 
ATOM   1206  O O   . ASN A  1 158 ? 7.965   20.526  232.699 1.00 248.17 ?  188 ASN A O   1 
ATOM   1207  C CB  . ASN A  1 158 ? 10.902  18.681  233.029 1.00 235.58 ?  188 ASN A CB  1 
ATOM   1208  C CG  . ASN A  1 158 ? 11.408  17.663  234.042 1.00 235.29 ?  188 ASN A CG  1 
ATOM   1209  O OD1 . ASN A  1 158 ? 11.767  18.011  235.169 1.00 236.29 ?  188 ASN A OD1 1 
ATOM   1210  N ND2 . ASN A  1 158 ? 11.426  16.394  233.646 1.00 226.60 ?  188 ASN A ND2 1 
ATOM   1211  N N   . LYS A  1 159 ? 9.853   21.059  231.610 1.00 213.79 ?  189 LYS A N   1 
ATOM   1212  C CA  . LYS A  1 159 ? 9.153   21.659  230.483 1.00 208.86 ?  189 LYS A CA  1 
ATOM   1213  C C   . LYS A  1 159 ? 8.955   20.615  229.385 1.00 199.96 ?  189 LYS A C   1 
ATOM   1214  O O   . LYS A  1 159 ? 9.903   19.927  228.994 1.00 192.76 ?  189 LYS A O   1 
ATOM   1215  C CB  . LYS A  1 159 ? 9.906   22.897  229.977 1.00 211.74 ?  189 LYS A CB  1 
ATOM   1216  C CG  . LYS A  1 159 ? 11.339  22.676  229.494 1.00 203.91 ?  189 LYS A CG  1 
ATOM   1217  C CD  . LYS A  1 159 ? 11.851  23.909  228.733 1.00 202.20 ?  189 LYS A CD  1 
ATOM   1218  C CE  . LYS A  1 159 ? 12.369  25.016  229.652 1.00 202.32 ?  189 LYS A CE  1 
ATOM   1219  N NZ  . LYS A  1 159 ? 12.704  26.274  228.908 1.00 204.93 1  189 LYS A NZ  1 
ATOM   1220  N N   . GLU A  1 160 ? 7.712   20.494  228.909 1.00 185.67 ?  190 GLU A N   1 
ATOM   1221  C CA  . GLU A  1 160 ? 7.252   19.371  228.095 1.00 179.22 ?  190 GLU A CA  1 
ATOM   1222  C C   . GLU A  1 160 ? 7.003   19.815  226.659 1.00 172.01 ?  190 GLU A C   1 
ATOM   1223  O O   . GLU A  1 160 ? 6.334   20.829  226.435 1.00 171.14 ?  190 GLU A O   1 
ATOM   1224  C CB  . GLU A  1 160 ? 5.930   18.827  228.650 1.00 178.73 ?  190 GLU A CB  1 
ATOM   1225  C CG  . GLU A  1 160 ? 5.972   18.077  229.969 1.00 187.04 ?  190 GLU A CG  1 
ATOM   1226  C CD  . GLU A  1 160 ? 4.611   17.489  230.315 1.00 192.53 ?  190 GLU A CD  1 
ATOM   1227  O OE1 . GLU A  1 160 ? 3.659   17.722  229.539 1.00 194.86 ?  190 GLU A OE1 1 
ATOM   1228  O OE2 . GLU A  1 160 ? 4.485   16.813  231.358 1.00 193.52 -1 190 GLU A OE2 1 
ATOM   1229  N N   . TYR A  1 161 ? 7.529   19.068  225.689 1.00 163.98 ?  191 TYR A N   1 
ATOM   1230  C CA  . TYR A  1 161 ? 7.350   19.454  224.294 1.00 154.97 ?  191 TYR A CA  1 
ATOM   1231  C C   . TYR A  1 161 ? 6.689   18.325  223.495 1.00 150.53 ?  191 TYR A C   1 
ATOM   1232  O O   . TYR A  1 161 ? 6.282   17.296  224.042 1.00 148.68 ?  191 TYR A O   1 
ATOM   1233  C CB  . TYR A  1 161 ? 8.699   19.836  223.681 1.00 152.54 ?  191 TYR A CB  1 
ATOM   1234  C CG  . TYR A  1 161 ? 9.307   21.095  224.254 1.00 158.93 ?  191 TYR A CG  1 
ATOM   1235  C CD1 . TYR A  1 161 ? 10.003  21.078  225.456 1.00 169.41 ?  191 TYR A CD1 1 
ATOM   1236  C CD2 . TYR A  1 161 ? 9.190   22.303  223.583 1.00 156.87 ?  191 TYR A CD2 1 
ATOM   1237  C CE1 . TYR A  1 161 ? 10.561  22.236  225.976 1.00 177.13 ?  191 TYR A CE1 1 
ATOM   1238  C CE2 . TYR A  1 161 ? 9.743   23.464  224.093 1.00 164.06 ?  191 TYR A CE2 1 
ATOM   1239  C CZ  . TYR A  1 161 ? 10.427  23.427  225.289 1.00 175.30 ?  191 TYR A CZ  1 
ATOM   1240  O OH  . TYR A  1 161 ? 10.976  24.588  225.790 1.00 183.46 ?  191 TYR A OH  1 
ATOM   1241  N N   . ARG A  1 162 ? 6.601   18.534  222.180 1.00 152.49 ?  192 ARG A N   1 
ATOM   1242  C CA  . ARG A  1 162 ? 6.086   17.550  221.233 1.00 145.02 ?  192 ARG A CA  1 
ATOM   1243  C C   . ARG A  1 162 ? 6.560   17.954  219.841 1.00 139.14 ?  192 ARG A C   1 
ATOM   1244  O O   . ARG A  1 162 ? 7.012   19.080  219.629 1.00 139.01 ?  192 ARG A O   1 
ATOM   1245  C CB  . ARG A  1 162 ? 4.561   17.454  221.224 1.00 148.10 ?  192 ARG A CB  1 
ATOM   1246  C CG  . ARG A  1 162 ? 3.925   18.580  220.441 1.00 145.41 ?  192 ARG A CG  1 
ATOM   1247  C CD  . ARG A  1 162 ? 2.474   18.295  220.111 1.00 145.90 ?  192 ARG A CD  1 
ATOM   1248  N NE  . ARG A  1 162 ? 1.971   19.269  219.149 1.00 141.62 ?  192 ARG A NE  1 
ATOM   1249  C CZ  . ARG A  1 162 ? 1.401   20.422  219.478 1.00 149.78 ?  192 ARG A CZ  1 
ATOM   1250  N NH1 . ARG A  1 162 ? 1.255   20.748  220.754 1.00 160.50 1  192 ARG A NH1 1 
ATOM   1251  N NH2 . ARG A  1 162 ? 0.981   21.251  218.532 1.00 148.49 ?  192 ARG A NH2 1 
ATOM   1252  N N   . LEU A  1 163 ? 6.454   17.025  218.892 1.00 134.46 ?  193 LEU A N   1 
ATOM   1253  C CA  . LEU A  1 163 ? 6.779   17.344  217.505 1.00 138.03 ?  193 LEU A CA  1 
ATOM   1254  C C   . LEU A  1 163 ? 5.722   18.270  216.910 1.00 139.52 ?  193 LEU A C   1 
ATOM   1255  O O   . LEU A  1 163 ? 4.523   18.108  217.156 1.00 139.73 ?  193 LEU A O   1 
ATOM   1256  C CB  . LEU A  1 163 ? 6.891   16.078  216.660 1.00 135.49 ?  193 LEU A CB  1 
ATOM   1257  C CG  . LEU A  1 163 ? 8.094   15.192  216.964 1.00 132.26 ?  193 LEU A CG  1 
ATOM   1258  C CD1 . LEU A  1 163 ? 8.139   14.008  216.013 1.00 133.87 ?  193 LEU A CD1 1 
ATOM   1259  C CD2 . LEU A  1 163 ? 9.373   16.014  216.871 1.00 128.47 ?  193 LEU A CD2 1 
ATOM   1260  N N   . ILE A  1 164 ? 6.171   19.252  216.121 1.00 147.79 ?  194 ILE A N   1 
ATOM   1261  C CA  . ILE A  1 164 ? 5.268   20.278  215.603 1.00 146.05 ?  194 ILE A CA  1 
ATOM   1262  C C   . ILE A  1 164 ? 4.256   19.742  214.601 1.00 142.42 ?  194 ILE A C   1 
ATOM   1263  O O   . ILE A  1 164 ? 3.276   20.433  214.297 1.00 143.24 ?  194 ILE A O   1 
ATOM   1264  C CB  . ILE A  1 164 ? 6.079   21.419  214.953 1.00 143.53 ?  194 ILE A CB  1 
ATOM   1265  C CG1 . ILE A  1 164 ? 5.262   22.716  214.891 1.00 142.35 ?  194 ILE A CG1 1 
ATOM   1266  C CG2 . ILE A  1 164 ? 6.540   21.017  213.560 1.00 139.59 ?  194 ILE A CG2 1 
ATOM   1267  C CD1 . ILE A  1 164 ? 6.021   23.894  214.298 1.00 137.41 ?  194 ILE A CD1 1 
ATOM   1268  N N   . ASN A  1 165 ? 4.441   18.521  214.100 1.00 141.74 ?  195 ASN A N   1 
ATOM   1269  C CA  . ASN A  1 165 ? 3.550   17.976  213.086 1.00 147.41 ?  195 ASN A CA  1 
ATOM   1270  C C   . ASN A  1 165 ? 2.587   16.944  213.646 1.00 146.70 ?  195 ASN A C   1 
ATOM   1271  O O   . ASN A  1 165 ? 1.677   16.513  212.929 1.00 152.73 ?  195 ASN A O   1 
ATOM   1272  C CB  . ASN A  1 165 ? 4.351   17.337  211.950 1.00 144.44 ?  195 ASN A CB  1 
ATOM   1273  C CG  . ASN A  1 165 ? 4.981   16.033  212.360 1.00 138.84 ?  195 ASN A CG  1 
ATOM   1274  O OD1 . ASN A  1 165 ? 4.430   14.966  212.100 1.00 138.87 ?  195 ASN A OD1 1 
ATOM   1275  N ND2 . ASN A  1 165 ? 6.134   16.105  213.012 1.00 139.03 ?  195 ASN A ND2 1 
ATOM   1276  N N   . CYS A  1 166 ? 2.770   16.536  214.903 1.00 138.65 ?  196 CYS A N   1 
ATOM   1277  C CA  . CYS A  1 166 ? 1.928   15.504  215.492 1.00 143.92 ?  196 CYS A CA  1 
ATOM   1278  C C   . CYS A  1 166 ? 0.473   15.937  215.562 1.00 143.20 ?  196 CYS A C   1 
ATOM   1279  O O   . CYS A  1 166 ? -0.418  15.084  215.619 1.00 142.92 ?  196 CYS A O   1 
ATOM   1280  C CB  . CYS A  1 166 ? 2.440   15.127  216.881 1.00 152.50 ?  196 CYS A CB  1 
ATOM   1281  S SG  . CYS A  1 166 ? 3.873   14.027  216.878 1.00 165.96 ?  196 CYS A SG  1 
ATOM   1282  N N   . ASN A  1 167 ? 0.210   17.237  215.564 1.00 149.11 ?  197 ASN A N   1 
ATOM   1283  C CA  . ASN A  1 167 ? -1.150  17.741  215.616 1.00 153.84 ?  197 ASN A CA  1 
ATOM   1284  C C   . ASN A  1 167 ? -1.628  18.224  214.255 1.00 151.86 ?  197 ASN A C   1 
ATOM   1285  O O   . ASN A  1 167 ? -2.689  18.851  214.167 1.00 155.56 ?  197 ASN A O   1 
ATOM   1286  C CB  . ASN A  1 167 ? -1.238  18.863  216.652 1.00 161.59 ?  197 ASN A CB  1 
ATOM   1287  C CG  . ASN A  1 167 ? -0.632  20.165  216.159 1.00 160.52 ?  197 ASN A CG  1 
ATOM   1288  O OD1 . ASN A  1 167 ? 0.583   20.266  215.988 1.00 152.56 ?  197 ASN A OD1 1 
ATOM   1289  N ND2 . ASN A  1 167 ? -1.471  21.176  215.961 1.00 166.33 ?  197 ASN A ND2 1 
ATOM   1290  N N   . THR A  1 168 ? -0.868  17.947  213.191 1.00 149.17 ?  198 THR A N   1 
ATOM   1291  C CA  . THR A  1 168 ? -1.229  18.359  211.839 1.00 149.45 ?  198 THR A CA  1 
ATOM   1292  C C   . THR A  1 168 ? -1.429  17.194  210.880 1.00 146.78 ?  198 THR A C   1 
ATOM   1293  O O   . THR A  1 168 ? -2.473  17.117  210.222 1.00 148.36 ?  198 THR A O   1 
ATOM   1294  C CB  . THR A  1 168 ? -0.152  19.302  211.265 1.00 151.84 ?  198 THR A CB  1 
ATOM   1295  O OG1 . THR A  1 168 ? 1.056   18.572  211.020 1.00 153.89 ?  198 THR A OG1 1 
ATOM   1296  C CG2 . THR A  1 168 ? 0.149   20.424  212.242 1.00 161.17 ?  198 THR A CG2 1 
ATOM   1297  N N   . SER A  1 169 ? -0.467  16.276  210.785 1.00 154.21 ?  199 SER A N   1 
ATOM   1298  C CA  . SER A  1 169 ? -0.557  15.165  209.842 1.00 151.16 ?  199 SER A CA  1 
ATOM   1299  C C   . SER A  1 169 ? 0.412   14.060  210.255 1.00 149.24 ?  199 SER A C   1 
ATOM   1300  O O   . SER A  1 169 ? 1.113   14.170  211.263 1.00 152.14 ?  199 SER A O   1 
ATOM   1301  C CB  . SER A  1 169 ? -0.275  15.655  208.427 1.00 153.03 ?  199 SER A CB  1 
ATOM   1302  O OG  . SER A  1 169 ? 1.028   16.199  208.338 1.00 152.36 ?  199 SER A OG  1 
ATOM   1303  N N   . ALA A  1 170 ? 0.476   13.004  209.440 1.00 151.43 ?  200 ALA A N   1 
ATOM   1304  C CA  . ALA A  1 170 ? 1.419   11.925  209.698 1.00 146.28 ?  200 ALA A CA  1 
ATOM   1305  C C   . ALA A  1 170 ? 2.826   12.383  209.310 1.00 145.20 ?  200 ALA A C   1 
ATOM   1306  O O   . ALA A  1 170 ? 3.006   13.447  208.722 1.00 148.68 ?  200 ALA A O   1 
ATOM   1307  C CB  . ALA A  1 170 ? 1.012   10.668  208.930 1.00 139.64 ?  200 ALA A CB  1 
ATOM   1308  N N   . ILE A  1 171 ? 3.833   11.559  209.605 1.00 144.82 ?  201 ILE A N   1 
ATOM   1309  C CA  . ILE A  1 171 ? 5.226   11.923  209.342 1.00 147.00 ?  201 ILE A CA  1 
ATOM   1310  C C   . ILE A  1 171 ? 6.034   10.714  208.877 1.00 147.00 ?  201 ILE A C   1 
ATOM   1311  O O   . ILE A  1 171 ? 5.901   9.618   209.430 1.00 149.51 ?  201 ILE A O   1 
ATOM   1312  C CB  . ILE A  1 171 ? 5.859   12.565  210.593 1.00 146.28 ?  201 ILE A CB  1 
ATOM   1313  C CG1 . ILE A  1 171 ? 7.334   12.884  210.351 1.00 146.25 ?  201 ILE A CG1 1 
ATOM   1314  C CG2 . ILE A  1 171 ? 5.645   11.674  211.810 1.00 146.40 ?  201 ILE A CG2 1 
ATOM   1315  C CD1 . ILE A  1 171 ? 7.991   13.551  211.518 1.00 144.82 ?  201 ILE A CD1 1 
ATOM   1316  N N   . THR A  1 172 ? 6.855   10.910  207.835 1.00 151.11 ?  202 THR A N   1 
ATOM   1317  C CA  . THR A  1 172 ? 7.733   9.865   207.315 1.00 148.76 ?  202 THR A CA  1 
ATOM   1318  C C   . THR A  1 172 ? 9.185   10.315  207.185 1.00 147.72 ?  202 THR A C   1 
ATOM   1319  O O   . THR A  1 172 ? 9.465   11.442  206.766 1.00 147.23 ?  202 THR A O   1 
ATOM   1320  C CB  . THR A  1 172 ? 7.266   9.395   205.936 1.00 147.28 ?  202 THR A CB  1 
ATOM   1321  O OG1 . THR A  1 172 ? 8.296   8.601   205.330 1.00 144.04 ?  202 THR A OG1 1 
ATOM   1322  C CG2 . THR A  1 172 ? 6.958   10.592  205.046 1.00 143.61 ?  202 THR A CG2 1 
ATOM   1323  N N   . GLN A  1 173 ? 10.102  9.424   207.569 1.00 141.30 ?  203 GLN A N   1 
ATOM   1324  C CA  . GLN A  1 173 ? 11.532  9.707   207.514 1.00 143.89 ?  203 GLN A CA  1 
ATOM   1325  C C   . GLN A  1 173 ? 12.083  9.416   206.127 1.00 144.40 ?  203 GLN A C   1 
ATOM   1326  O O   . GLN A  1 173 ? 11.796  8.365   205.546 1.00 143.47 ?  203 GLN A O   1 
ATOM   1327  C CB  . GLN A  1 173 ? 12.320  8.862   208.515 1.00 143.67 ?  203 GLN A CB  1 
ATOM   1328  C CG  . GLN A  1 173 ? 13.821  9.198   208.498 1.00 142.92 ?  203 GLN A CG  1 
ATOM   1329  C CD  . GLN A  1 173 ? 14.675  8.280   209.357 1.00 145.73 ?  203 GLN A CD  1 
ATOM   1330  O OE1 . GLN A  1 173 ? 15.639  8.720   209.985 1.00 146.23 ?  203 GLN A OE1 1 
ATOM   1331  N NE2 . GLN A  1 173 ? 14.352  6.990   209.351 1.00 147.61 ?  203 GLN A NE2 1 
ATOM   1332  N N   . ALA A  1 174 ? 12.876  10.335  205.595 1.00 143.53 ?  204 ALA A N   1 
ATOM   1333  C CA  . ALA A  1 174 ? 13.516  10.085  204.315 1.00 141.05 ?  204 ALA A CA  1 
ATOM   1334  C C   . ALA A  1 174 ? 14.568  8.993   204.458 1.00 147.04 ?  204 ALA A C   1 
ATOM   1335  O O   . ALA A  1 174 ? 15.338  8.975   205.423 1.00 147.61 ?  204 ALA A O   1 
ATOM   1336  C CB  . ALA A  1 174 ? 14.169  11.350  203.774 1.00 137.79 ?  204 ALA A CB  1 
ATOM   1337  N N   . CYS A  1 175 ? 14.600  8.081   203.498 1.00 146.46 ?  205 CYS A N   1 
ATOM   1338  C CA  . CYS A  1 175 ? 15.586  7.015   203.539 1.00 148.18 ?  205 CYS A CA  1 
ATOM   1339  C C   . CYS A  1 175 ? 16.970  7.616   203.327 1.00 149.69 ?  205 CYS A C   1 
ATOM   1340  O O   . CYS A  1 175 ? 17.136  8.504   202.486 1.00 150.05 ?  205 CYS A O   1 
ATOM   1341  C CB  . CYS A  1 175 ? 15.317  5.951   202.481 1.00 150.42 ?  205 CYS A CB  1 
ATOM   1342  S SG  . CYS A  1 175 ? 13.702  5.207   202.599 1.00 197.72 ?  205 CYS A SG  1 
ATOM   1343  N N   . PRO A  1 176 ? 17.981  7.155   204.064 1.00 162.36 ?  206 PRO A N   1 
ATOM   1344  C CA  . PRO A  1 176 ? 19.324  7.730   203.907 1.00 167.22 ?  206 PRO A CA  1 
ATOM   1345  C C   . PRO A  1 176 ? 20.014  7.297   202.630 1.00 173.84 ?  206 PRO A C   1 
ATOM   1346  O O   . PRO A  1 176 ? 21.077  7.838   202.301 1.00 179.56 ?  206 PRO A O   1 
ATOM   1347  C CB  . PRO A  1 176 ? 20.071  7.209   205.139 1.00 169.06 ?  206 PRO A CB  1 
ATOM   1348  C CG  . PRO A  1 176 ? 19.408  5.902   205.439 1.00 167.93 ?  206 PRO A CG  1 
ATOM   1349  C CD  . PRO A  1 176 ? 17.948  6.092   205.088 1.00 164.21 ?  206 PRO A CD  1 
ATOM   1350  N N   . LYS A  1 177 ? 19.437  6.338   201.908 1.00 187.47 ?  207 LYS A N   1 
ATOM   1351  C CA  . LYS A  1 177 ? 20.022  5.847   200.666 1.00 190.48 ?  207 LYS A CA  1 
ATOM   1352  C C   . LYS A  1 177 ? 19.866  6.855   199.533 1.00 191.50 ?  207 LYS A C   1 
ATOM   1353  O O   . LYS A  1 177 ? 20.794  7.051   198.738 1.00 198.68 ?  207 LYS A O   1 
ATOM   1354  C CB  . LYS A  1 177 ? 19.380  4.514   200.286 1.00 195.45 ?  207 LYS A CB  1 
ATOM   1355  C CG  . LYS A  1 177 ? 18.805  3.726   201.463 1.00 192.11 ?  207 LYS A CG  1 
ATOM   1356  C CD  . LYS A  1 177 ? 19.889  3.301   202.447 1.00 197.88 ?  207 LYS A CD  1 
ATOM   1357  C CE  . LYS A  1 177 ? 20.686  2.122   201.922 1.00 216.47 ?  207 LYS A CE  1 
ATOM   1358  N NZ  . LYS A  1 177 ? 21.660  1.634   202.935 1.00 217.51 1  207 LYS A NZ  1 
ATOM   1359  N N   . VAL A  1 178 ? 18.712  7.508   199.442 1.00 186.99 ?  208 VAL A N   1 
ATOM   1360  C CA  . VAL A  1 178 ? 18.481  8.465   198.370 1.00 186.24 ?  208 VAL A CA  1 
ATOM   1361  C C   . VAL A  1 178 ? 19.117  9.806   198.725 1.00 182.41 ?  208 VAL A C   1 
ATOM   1362  O O   . VAL A  1 178 ? 19.433  10.096  199.881 1.00 180.07 ?  208 VAL A O   1 
ATOM   1363  C CB  . VAL A  1 178 ? 16.974  8.626   198.095 1.00 183.80 ?  208 VAL A CB  1 
ATOM   1364  C CG1 . VAL A  1 178 ? 16.337  7.279   197.774 1.00 187.08 ?  208 VAL A CG1 1 
ATOM   1365  C CG2 . VAL A  1 178 ? 16.286  9.296   199.277 1.00 177.29 ?  208 VAL A CG2 1 
ATOM   1366  N N   . SER A  1 179 ? 19.305  10.635  197.702 1.00 169.54 ?  209 SER A N   1 
ATOM   1367  C CA  . SER A  1 179 ? 19.880  11.956  197.881 1.00 166.13 ?  209 SER A CA  1 
ATOM   1368  C C   . SER A  1 179 ? 18.996  12.986  197.207 1.00 165.54 ?  209 SER A C   1 
ATOM   1369  O O   . SER A  1 179 ? 18.288  12.697  196.237 1.00 166.81 ?  209 SER A O   1 
ATOM   1370  C CB  . SER A  1 179 ? 21.294  12.063  197.298 1.00 164.21 ?  209 SER A CB  1 
ATOM   1371  O OG  . SER A  1 179 ? 21.273  11.971  195.887 1.00 169.23 ?  209 SER A OG  1 
ATOM   1372  N N   . PHE A  1 180 ? 19.051  14.199  197.747 1.00 162.24 ?  210 PHE A N   1 
ATOM   1373  C CA  . PHE A  1 180 ? 18.283  15.342  197.268 1.00 162.71 ?  210 PHE A CA  1 
ATOM   1374  C C   . PHE A  1 180 ? 19.130  16.228  196.362 1.00 167.48 ?  210 PHE A C   1 
ATOM   1375  O O   . PHE A  1 180 ? 18.994  17.452  196.351 1.00 168.73 ?  210 PHE A O   1 
ATOM   1376  C CB  . PHE A  1 180 ? 17.721  16.131  198.454 1.00 161.50 ?  210 PHE A CB  1 
ATOM   1377  C CG  . PHE A  1 180 ? 16.980  15.279  199.470 1.00 160.30 ?  210 PHE A CG  1 
ATOM   1378  C CD1 . PHE A  1 180 ? 16.507  14.012  199.140 1.00 158.20 ?  210 PHE A CD1 1 
ATOM   1379  C CD2 . PHE A  1 180 ? 16.786  15.736  200.761 1.00 159.40 ?  210 PHE A CD2 1 
ATOM   1380  C CE1 . PHE A  1 180 ? 15.847  13.235  200.072 1.00 151.30 ?  210 PHE A CE1 1 
ATOM   1381  C CE2 . PHE A  1 180 ? 16.125  14.962  201.698 1.00 153.39 ?  210 PHE A CE2 1 
ATOM   1382  C CZ  . PHE A  1 180 ? 15.655  13.709  201.352 1.00 149.08 ?  210 PHE A CZ  1 
ATOM   1383  N N   . GLU A  1 181 ? 20.012  15.620  195.576 1.00 164.50 ?  211 GLU A N   1 
ATOM   1384  C CA  . GLU A  1 181 ? 20.871  16.383  194.683 1.00 165.73 ?  211 GLU A CA  1 
ATOM   1385  C C   . GLU A  1 181 ? 20.150  16.654  193.374 1.00 158.48 ?  211 GLU A C   1 
ATOM   1386  O O   . GLU A  1 181 ? 19.846  15.703  192.639 1.00 153.70 ?  211 GLU A O   1 
ATOM   1387  C CB  . GLU A  1 181 ? 22.154  15.626  194.398 1.00 163.04 ?  211 GLU A CB  1 
ATOM   1388  C CG  . GLU A  1 181 ? 23.262  16.454  193.752 1.00 169.18 ?  211 GLU A CG  1 
ATOM   1389  C CD  . GLU A  1 181 ? 23.922  17.481  194.657 1.00 177.89 ?  211 GLU A CD  1 
ATOM   1390  O OE1 . GLU A  1 181 ? 23.803  17.366  195.895 1.00 185.75 ?  211 GLU A OE1 1 
ATOM   1391  O OE2 . GLU A  1 181 ? 24.625  18.366  194.121 1.00 180.85 -1 211 GLU A OE2 1 
ATOM   1392  N N   . PRO A  1 182 ? 19.850  17.909  193.044 1.00 166.89 ?  212 PRO A N   1 
ATOM   1393  C CA  . PRO A  1 182 ? 19.138  18.215  191.787 1.00 165.57 ?  212 PRO A CA  1 
ATOM   1394  C C   . PRO A  1 182 ? 19.980  17.845  190.574 1.00 168.55 ?  212 PRO A C   1 
ATOM   1395  O O   . PRO A  1 182 ? 21.044  18.424  190.340 1.00 170.88 ?  212 PRO A O   1 
ATOM   1396  C CB  . PRO A  1 182 ? 18.897  19.729  191.871 1.00 166.22 ?  212 PRO A CB  1 
ATOM   1397  C CG  . PRO A  1 182 ? 19.040  20.067  193.317 1.00 167.00 ?  212 PRO A CG  1 
ATOM   1398  C CD  . PRO A  1 182 ? 20.082  19.124  193.841 1.00 172.07 ?  212 PRO A CD  1 
ATOM   1399  N N   . ILE A  1 183 ? 19.502  16.883  189.790 1.00 169.70 ?  213 ILE A N   1 
ATOM   1400  C CA  . ILE A  1 183 ? 20.246  16.491  188.594 1.00 167.04 ?  213 ILE A CA  1 
ATOM   1401  C C   . ILE A  1 183 ? 19.544  16.924  187.305 1.00 161.97 ?  213 ILE A C   1 
ATOM   1402  O O   . ILE A  1 183 ? 18.306  16.960  187.244 1.00 159.22 ?  213 ILE A O   1 
ATOM   1403  C CB  . ILE A  1 183 ? 20.501  14.973  188.617 1.00 169.67 ?  213 ILE A CB  1 
ATOM   1404  C CG1 . ILE A  1 183 ? 19.193  14.219  188.868 1.00 169.47 ?  213 ILE A CG1 1 
ATOM   1405  C CG2 . ILE A  1 183 ? 21.526  14.618  189.708 1.00 173.35 ?  213 ILE A CG2 1 
ATOM   1406  C CD1 . ILE A  1 183 ? 19.361  12.716  188.978 1.00 174.36 ?  213 ILE A CD1 1 
ATOM   1407  N N   . PRO A  1 184 ? 20.303  17.281  186.263 1.00 154.55 ?  214 PRO A N   1 
ATOM   1408  C CA  . PRO A  1 184 ? 19.703  17.747  184.998 1.00 155.09 ?  214 PRO A CA  1 
ATOM   1409  C C   . PRO A  1 184 ? 18.708  16.757  184.401 1.00 154.14 ?  214 PRO A C   1 
ATOM   1410  O O   . PRO A  1 184 ? 19.003  15.571  184.246 1.00 154.73 ?  214 PRO A O   1 
ATOM   1411  C CB  . PRO A  1 184 ? 20.923  17.941  184.088 1.00 157.97 ?  214 PRO A CB  1 
ATOM   1412  C CG  . PRO A  1 184 ? 22.060  18.219  185.046 1.00 159.42 ?  214 PRO A CG  1 
ATOM   1413  C CD  . PRO A  1 184 ? 21.776  17.367  186.248 1.00 159.13 ?  214 PRO A CD  1 
ATOM   1414  N N   . ILE A  1 185 ? 17.514  17.253  184.072 1.00 153.55 ?  215 ILE A N   1 
ATOM   1415  C CA  . ILE A  1 185 ? 16.457  16.436  183.478 1.00 153.27 ?  215 ILE A CA  1 
ATOM   1416  C C   . ILE A  1 185 ? 15.979  17.071  182.177 1.00 154.26 ?  215 ILE A C   1 
ATOM   1417  O O   . ILE A  1 185 ? 15.469  18.196  182.184 1.00 154.16 ?  215 ILE A O   1 
ATOM   1418  C CB  . ILE A  1 185 ? 15.273  16.258  184.438 1.00 151.73 ?  215 ILE A CB  1 
ATOM   1419  C CG1 . ILE A  1 185 ? 15.726  15.522  185.697 1.00 150.94 ?  215 ILE A CG1 1 
ATOM   1420  C CG2 . ILE A  1 185 ? 14.136  15.530  183.742 1.00 151.74 ?  215 ILE A CG2 1 
ATOM   1421  C CD1 . ILE A  1 185 ? 14.621  15.286  186.682 1.00 155.84 ?  215 ILE A CD1 1 
ATOM   1422  N N   . HIS A  1 186 ? 16.154  16.364  181.064 1.00 149.65 ?  216 HIS A N   1 
ATOM   1423  C CA  . HIS A  1 186 ? 15.699  16.838  179.759 1.00 149.54 ?  216 HIS A CA  1 
ATOM   1424  C C   . HIS A  1 186 ? 14.269  16.372  179.492 1.00 144.38 ?  216 HIS A C   1 
ATOM   1425  O O   . HIS A  1 186 ? 13.978  15.173  179.569 1.00 145.01 ?  216 HIS A O   1 
ATOM   1426  C CB  . HIS A  1 186 ? 16.601  16.373  178.614 1.00 159.24 ?  216 HIS A CB  1 
ATOM   1427  C CG  . HIS A  1 186 ? 18.052  16.708  178.776 1.00 163.08 ?  216 HIS A CG  1 
ATOM   1428  N ND1 . HIS A  1 186 ? 18.660  17.736  178.083 1.00 159.08 ?  216 HIS A ND1 1 
ATOM   1429  C CD2 . HIS A  1 186 ? 19.021  16.138  179.529 1.00 170.27 ?  216 HIS A CD2 1 
ATOM   1430  C CE1 . HIS A  1 186 ? 19.943  17.778  178.400 1.00 161.27 ?  216 HIS A CE1 1 
ATOM   1431  N NE2 . HIS A  1 186 ? 20.185  16.824  179.280 1.00 170.31 ?  216 HIS A NE2 1 
ATOM   1432  N N   . TYR A  1 187 ? 13.380  17.312  179.190 1.00 129.43 ?  217 TYR A N   1 
ATOM   1433  C CA  . TYR A  1 187 ? 12.002  16.987  178.834 1.00 129.41 ?  217 TYR A CA  1 
ATOM   1434  C C   . TYR A  1 187 ? 11.885  16.844  177.323 1.00 133.33 ?  217 TYR A C   1 
ATOM   1435  O O   . TYR A  1 187 ? 12.305  17.733  176.576 1.00 137.68 ?  217 TYR A O   1 
ATOM   1436  C CB  . TYR A  1 187 ? 11.030  18.042  179.342 1.00 128.56 ?  217 TYR A CB  1 
ATOM   1437  C CG  . TYR A  1 187 ? 10.588  17.810  180.761 1.00 132.30 ?  217 TYR A CG  1 
ATOM   1438  C CD1 . TYR A  1 187 ? 11.352  18.245  181.836 1.00 136.44 ?  217 TYR A CD1 1 
ATOM   1439  C CD2 . TYR A  1 187 ? 9.397   17.151  181.025 1.00 129.84 ?  217 TYR A CD2 1 
ATOM   1440  C CE1 . TYR A  1 187 ? 10.931  18.028  183.141 1.00 133.82 ?  217 TYR A CE1 1 
ATOM   1441  C CE2 . TYR A  1 187 ? 8.969   16.930  182.319 1.00 126.56 ?  217 TYR A CE2 1 
ATOM   1442  C CZ  . TYR A  1 187 ? 9.738   17.370  183.375 1.00 129.73 ?  217 TYR A CZ  1 
ATOM   1443  O OH  . TYR A  1 187 ? 9.307   17.149  184.663 1.00 130.61 ?  217 TYR A OH  1 
ATOM   1444  N N   . CYS A  1 188 ? 11.320  15.723  176.877 1.00 130.11 ?  218 CYS A N   1 
ATOM   1445  C CA  . CYS A  1 188 ? 11.216  15.433  175.457 1.00 131.75 ?  218 CYS A CA  1 
ATOM   1446  C C   . CYS A  1 188 ? 9.756   15.215  175.075 1.00 130.58 ?  218 CYS A C   1 
ATOM   1447  O O   . CYS A  1 188 ? 8.913   14.912  175.924 1.00 130.48 ?  218 CYS A O   1 
ATOM   1448  C CB  . CYS A  1 188 ? 12.032  14.204  175.074 1.00 131.75 ?  218 CYS A CB  1 
ATOM   1449  S SG  . CYS A  1 188 ? 13.714  14.387  175.624 1.00 128.47 ?  218 CYS A SG  1 
ATOM   1450  N N   . ALA A  1 189 ? 9.457   15.382  173.761 1.00 121.60 ?  219 ALA A N   1 
ATOM   1451  C CA  . ALA A  1 189 ? 8.116   15.207  173.209 1.00 121.17 ?  219 ALA A CA  1 
ATOM   1452  C C   . ALA A  1 189 ? 8.014   13.921  172.393 1.00 121.89 ?  219 ALA A C   1 
ATOM   1453  O O   . ALA A  1 189 ? 8.961   13.553  171.691 1.00 123.86 ?  219 ALA A O   1 
ATOM   1454  C CB  . ALA A  1 189 ? 7.739   16.394  172.315 1.00 123.75 ?  219 ALA A CB  1 
ATOM   1455  N N   . PRO A  1 190 ? 6.875   13.207  172.480 1.00 118.00 ?  220 PRO A N   1 
ATOM   1456  C CA  . PRO A  1 190 ? 6.722   11.947  171.735 1.00 121.06 ?  220 PRO A CA  1 
ATOM   1457  C C   . PRO A  1 190 ? 6.689   12.119  170.227 1.00 126.10 ?  220 PRO A C   1 
ATOM   1458  O O   . PRO A  1 190 ? 6.715   13.244  169.718 1.00 126.90 ?  220 PRO A O   1 
ATOM   1459  C CB  . PRO A  1 190 ? 5.380   11.403  172.243 1.00 118.67 ?  220 PRO A CB  1 
ATOM   1460  C CG  . PRO A  1 190 ? 4.640   12.615  172.704 1.00 117.73 ?  220 PRO A CG  1 
ATOM   1461  C CD  . PRO A  1 190 ? 5.681   13.526  173.279 1.00 120.40 ?  220 PRO A CD  1 
ATOM   1462  N N   . ALA A  1 191 ? 6.626   10.997  169.510 1.00 129.54 ?  221 ALA A N   1 
ATOM   1463  C CA  . ALA A  1 191 ? 6.607   11.038  168.055 1.00 128.91 ?  221 ALA A CA  1 
ATOM   1464  C C   . ALA A  1 191 ? 5.379   11.784  167.555 1.00 126.61 ?  221 ALA A C   1 
ATOM   1465  O O   . ALA A  1 191 ? 4.282   11.653  168.106 1.00 125.70 ?  221 ALA A O   1 
ATOM   1466  C CB  . ALA A  1 191 ? 6.629   9.621   167.485 1.00 137.03 ?  221 ALA A CB  1 
ATOM   1467  N N   . GLY A  1 192 ? 5.566   12.577  166.504 1.00 131.43 ?  222 GLY A N   1 
ATOM   1468  C CA  . GLY A  1 192 ? 4.480   13.351  165.962 1.00 134.23 ?  222 GLY A CA  1 
ATOM   1469  C C   . GLY A  1 192 ? 4.338   14.717  166.584 1.00 135.03 ?  222 GLY A C   1 
ATOM   1470  O O   . GLY A  1 192 ? 3.525   15.516  166.111 1.00 137.26 ?  222 GLY A O   1 
ATOM   1471  N N   . PHE A  1 193 ? 5.016   14.960  167.701 1.00 124.80 ?  223 PHE A N   1 
ATOM   1472  C CA  . PHE A  1 193 ? 5.020   16.227  168.415 1.00 121.21 ?  223 PHE A CA  1 
ATOM   1473  C C   . PHE A  1 193 ? 6.420   16.836  168.347 1.00 121.63 ?  223 PHE A C   1 
ATOM   1474  O O   . PHE A  1 193 ? 7.384   16.183  167.941 1.00 122.40 ?  223 PHE A O   1 
ATOM   1475  C CB  . PHE A  1 193 ? 4.531   16.034  169.860 1.00 117.52 ?  223 PHE A CB  1 
ATOM   1476  C CG  . PHE A  1 193 ? 3.065   15.607  169.971 1.00 115.90 ?  223 PHE A CG  1 
ATOM   1477  C CD1 . PHE A  1 193 ? 2.500   14.727  169.059 1.00 123.03 ?  223 PHE A CD1 1 
ATOM   1478  C CD2 . PHE A  1 193 ? 2.247   16.117  170.961 1.00 116.27 ?  223 PHE A CD2 1 
ATOM   1479  C CE1 . PHE A  1 193 ? 1.178   14.341  169.144 1.00 129.32 ?  223 PHE A CE1 1 
ATOM   1480  C CE2 . PHE A  1 193 ? 0.909   15.734  171.047 1.00 119.96 ?  223 PHE A CE2 1 
ATOM   1481  C CZ  . PHE A  1 193 ? 0.381   14.844  170.138 1.00 126.25 ?  223 PHE A CZ  1 
ATOM   1482  N N   . ALA A  1 194 ? 6.535   18.097  168.758 1.00 115.84 ?  224 ALA A N   1 
ATOM   1483  C CA  . ALA A  1 194 ? 7.832   18.766  168.751 1.00 117.68 ?  224 ALA A CA  1 
ATOM   1484  C C   . ALA A  1 194 ? 7.826   19.893  169.771 1.00 117.58 ?  224 ALA A C   1 
ATOM   1485  O O   . ALA A  1 194 ? 6.770   20.391  170.167 1.00 116.72 ?  224 ALA A O   1 
ATOM   1486  C CB  . ALA A  1 194 ? 8.181   19.304  167.360 1.00 120.42 ?  224 ALA A CB  1 
ATOM   1487  N N   . ILE A  1 195 ? 9.027   20.277  170.200 1.00 139.91 ?  225 ILE A N   1 
ATOM   1488  C CA  . ILE A  1 195 ? 9.222   21.355  171.163 1.00 137.41 ?  225 ILE A CA  1 
ATOM   1489  C C   . ILE A  1 195 ? 9.966   22.503  170.496 1.00 141.02 ?  225 ILE A C   1 
ATOM   1490  O O   . ILE A  1 195 ? 11.093  22.328  170.017 1.00 150.79 ?  225 ILE A O   1 
ATOM   1491  C CB  . ILE A  1 195 ? 10.013  20.862  172.383 1.00 129.20 ?  225 ILE A CB  1 
ATOM   1492  C CG1 . ILE A  1 195 ? 9.304   19.683  173.053 1.00 128.66 ?  225 ILE A CG1 1 
ATOM   1493  C CG2 . ILE A  1 195 ? 10.236  22.001  173.364 1.00 131.57 ?  225 ILE A CG2 1 
ATOM   1494  C CD1 . ILE A  1 195 ? 10.028  19.162  174.276 1.00 131.44 ?  225 ILE A CD1 1 
ATOM   1495  N N   . LEU A  1 196 ? 9.334   23.675  170.465 1.00 129.85 ?  226 LEU A N   1 
ATOM   1496  C CA  . LEU A  1 196 ? 9.919   24.870  169.872 1.00 132.72 ?  226 LEU A CA  1 
ATOM   1497  C C   . LEU A  1 196 ? 10.742  25.625  170.909 1.00 133.09 ?  226 LEU A C   1 
ATOM   1498  O O   . LEU A  1 196 ? 10.387  25.659  172.091 1.00 131.25 ?  226 LEU A O   1 
ATOM   1499  C CB  . LEU A  1 196 ? 8.829   25.771  169.296 1.00 133.76 ?  226 LEU A CB  1 
ATOM   1500  C CG  . LEU A  1 196 ? 7.908   25.025  168.334 1.00 133.27 ?  226 LEU A CG  1 
ATOM   1501  C CD1 . LEU A  1 196 ? 6.880   25.964  167.724 1.00 135.36 ?  226 LEU A CD1 1 
ATOM   1502  C CD2 . LEU A  1 196 ? 8.733   24.328  167.259 1.00 134.61 ?  226 LEU A CD2 1 
ATOM   1503  N N   . LYS A  1 197 ? 11.851  26.221  170.459 1.00 143.72 ?  227 LYS A N   1 
ATOM   1504  C CA  . LYS A  1 197 ? 12.781  26.944  171.323 1.00 144.73 ?  227 LYS A CA  1 
ATOM   1505  C C   . LYS A  1 197 ? 13.036  28.350  170.792 1.00 150.82 ?  227 LYS A C   1 
ATOM   1506  O O   . LYS A  1 197 ? 13.436  28.520  169.635 1.00 162.30 ?  227 LYS A O   1 
ATOM   1507  C CB  . LYS A  1 197 ? 14.105  26.180  171.472 1.00 145.81 ?  227 LYS A CB  1 
ATOM   1508  C CG  . LYS A  1 197 ? 15.106  26.841  172.410 1.00 143.22 ?  227 LYS A CG  1 
ATOM   1509  C CD  . LYS A  1 197 ? 16.345  25.983  172.598 1.00 143.40 ?  227 LYS A CD  1 
ATOM   1510  C CE  . LYS A  1 197 ? 17.293  26.627  173.591 1.00 140.92 ?  227 LYS A CE  1 
ATOM   1511  N NZ  . LYS A  1 197 ? 18.493  25.786  173.838 1.00 141.84 1  227 LYS A NZ  1 
ATOM   1512  N N   . CYS A  1 198 ? 12.808  29.349  171.645 1.00 140.21 ?  228 CYS A N   1 
ATOM   1513  C CA  . CYS A  1 198 ? 13.023  30.755  171.311 1.00 143.08 ?  228 CYS A CA  1 
ATOM   1514  C C   . CYS A  1 198 ? 14.492  31.130  171.478 1.00 144.91 ?  228 CYS A C   1 
ATOM   1515  O O   . CYS A  1 198 ? 15.066  30.958  172.560 1.00 143.66 ?  228 CYS A O   1 
ATOM   1516  C CB  . CYS A  1 198 ? 12.124  31.642  172.154 1.00 142.44 ?  228 CYS A CB  1 
ATOM   1517  S SG  . CYS A  1 198 ? 11.819  33.267  171.454 1.00 165.10 ?  228 CYS A SG  1 
ATOM   1518  N N   . LYS A  1 199 ? 15.097  31.652  170.404 1.00 174.22 ?  229 LYS A N   1 
ATOM   1519  C CA  . LYS A  1 199 ? 16.523  31.955  170.376 1.00 176.73 ?  229 LYS A CA  1 
ATOM   1520  C C   . LYS A  1 199 ? 16.815  33.447  170.265 1.00 184.85 ?  229 LYS A C   1 
ATOM   1521  O O   . LYS A  1 199 ? 17.871  33.827  169.760 1.00 189.06 ?  229 LYS A O   1 
ATOM   1522  C CB  . LYS A  1 199 ? 17.186  31.279  169.173 1.00 179.49 ?  229 LYS A CB  1 
ATOM   1523  C CG  . LYS A  1 199 ? 17.423  29.790  169.202 1.00 171.06 ?  229 LYS A CG  1 
ATOM   1524  C CD  . LYS A  1 199 ? 18.516  29.477  168.184 1.00 175.00 ?  229 LYS A CD  1 
ATOM   1525  C CE  . LYS A  1 199 ? 18.768  27.995  168.028 1.00 166.11 ?  229 LYS A CE  1 
ATOM   1526  N NZ  . LYS A  1 199 ? 19.776  27.731  166.963 1.00 169.68 1  229 LYS A NZ  1 
ATOM   1527  N N   . ASP A  1 200 ? 15.934  34.311  170.749 1.00 199.39 ?  230 ASP A N   1 
ATOM   1528  C CA  . ASP A  1 200 ? 16.283  35.724  170.769 1.00 206.52 ?  230 ASP A CA  1 
ATOM   1529  C C   . ASP A  1 200 ? 16.972  36.080  172.080 1.00 199.03 ?  230 ASP A C   1 
ATOM   1530  O O   . ASP A  1 200 ? 16.705  35.486  173.128 1.00 186.69 ?  230 ASP A O   1 
ATOM   1531  C CB  . ASP A  1 200 ? 15.053  36.611  170.569 1.00 204.56 ?  230 ASP A CB  1 
ATOM   1532  C CG  . ASP A  1 200 ? 13.889  36.191  171.432 1.00 196.67 ?  230 ASP A CG  1 
ATOM   1533  O OD1 . ASP A  1 200 ? 14.084  35.295  172.279 1.00 192.15 ?  230 ASP A OD1 1 
ATOM   1534  O OD2 . ASP A  1 200 ? 12.787  36.758  171.272 1.00 192.29 -1 230 ASP A OD2 1 
ATOM   1535  N N   . LYS A  1 201 ? 17.876  37.052  172.016 1.00 203.75 ?  231 LYS A N   1 
ATOM   1536  C CA  . LYS A  1 201 ? 18.613  37.409  173.219 1.00 199.05 ?  231 LYS A CA  1 
ATOM   1537  C C   . LYS A  1 201 ? 17.776  38.258  174.170 1.00 195.85 ?  231 LYS A C   1 
ATOM   1538  O O   . LYS A  1 201 ? 18.101  38.341  175.360 1.00 190.65 ?  231 LYS A O   1 
ATOM   1539  C CB  . LYS A  1 201 ? 19.937  38.087  172.854 1.00 204.18 ?  231 LYS A CB  1 
ATOM   1540  C CG  . LYS A  1 201 ? 21.074  37.077  172.633 1.00 202.17 ?  231 LYS A CG  1 
ATOM   1541  C CD  . LYS A  1 201 ? 21.344  36.724  171.179 1.00 208.76 ?  231 LYS A CD  1 
ATOM   1542  C CE  . LYS A  1 201 ? 22.592  35.846  171.071 1.00 206.12 ?  231 LYS A CE  1 
ATOM   1543  N NZ  . LYS A  1 201 ? 22.330  34.431  171.468 1.00 197.94 1  231 LYS A NZ  1 
ATOM   1544  N N   . LYS A  1 202 ? 16.723  38.901  173.663 1.00 183.93 ?  232 LYS A N   1 
ATOM   1545  C CA  . LYS A  1 202 ? 15.801  39.722  174.445 1.00 180.10 ?  232 LYS A CA  1 
ATOM   1546  C C   . LYS A  1 202 ? 14.375  39.214  174.234 1.00 177.74 ?  232 LYS A C   1 
ATOM   1547  O O   . LYS A  1 202 ? 13.809  39.377  173.147 1.00 181.71 ?  232 LYS A O   1 
ATOM   1548  C CB  . LYS A  1 202 ? 15.946  41.186  174.038 1.00 184.12 ?  232 LYS A CB  1 
ATOM   1549  C CG  . LYS A  1 202 ? 17.317  41.760  174.371 1.00 185.43 ?  232 LYS A CG  1 
ATOM   1550  C CD  . LYS A  1 202 ? 17.398  43.223  173.987 1.00 189.92 ?  232 LYS A CD  1 
ATOM   1551  C CE  . LYS A  1 202 ? 17.235  43.385  172.478 1.00 196.55 ?  232 LYS A CE  1 
ATOM   1552  N NZ  . LYS A  1 202 ? 17.345  44.803  172.033 1.00 200.21 1  232 LYS A NZ  1 
ATOM   1553  N N   . PHE A  1 203 ? 13.795  38.601  175.266 1.00 180.79 ?  233 PHE A N   1 
ATOM   1554  C CA  . PHE A  1 203 ? 12.449  38.028  175.177 1.00 179.59 ?  233 PHE A CA  1 
ATOM   1555  C C   . PHE A  1 203 ? 11.826  37.920  176.557 1.00 170.41 ?  233 PHE A C   1 
ATOM   1556  O O   . PHE A  1 203 ? 12.367  37.228  177.425 1.00 166.14 ?  233 PHE A O   1 
ATOM   1557  C CB  . PHE A  1 203 ? 12.481  36.660  174.518 1.00 181.62 ?  233 PHE A CB  1 
ATOM   1558  C CG  . PHE A  1 203 ? 11.123  36.086  174.269 1.00 179.60 ?  233 PHE A CG  1 
ATOM   1559  C CD1 . PHE A  1 203 ? 10.200  36.758  173.488 1.00 180.93 ?  233 PHE A CD1 1 
ATOM   1560  C CD2 . PHE A  1 203 ? 10.771  34.864  174.817 1.00 171.65 ?  233 PHE A CD2 1 
ATOM   1561  C CE1 . PHE A  1 203 ? 8.947   36.225  173.264 1.00 171.49 ?  233 PHE A CE1 1 
ATOM   1562  C CE2 . PHE A  1 203 ? 9.526   34.322  174.590 1.00 168.19 ?  233 PHE A CE2 1 
ATOM   1563  C CZ  . PHE A  1 203 ? 8.610   35.005  173.816 1.00 167.13 ?  233 PHE A CZ  1 
ATOM   1564  N N   . ASN A  1 204 ? 10.687  38.590  176.752 1.00 187.98 ?  234 ASN A N   1 
ATOM   1565  C CA  . ASN A  1 204 ? 10.005  38.612  178.038 1.00 181.44 ?  234 ASN A CA  1 
ATOM   1566  C C   . ASN A  1 204 ? 9.044   37.443  178.225 1.00 174.66 ?  234 ASN A C   1 
ATOM   1567  O O   . ASN A  1 204 ? 8.152   37.525  179.077 1.00 170.19 ?  234 ASN A O   1 
ATOM   1568  C CB  . ASN A  1 204 ? 9.210   39.908  178.203 1.00 187.67 ?  234 ASN A CB  1 
ATOM   1569  C CG  . ASN A  1 204 ? 8.253   40.157  177.047 1.00 188.80 ?  234 ASN A CG  1 
ATOM   1570  O OD1 . ASN A  1 204 ? 8.131   39.339  176.133 1.00 186.74 ?  234 ASN A OD1 1 
ATOM   1571  N ND2 . ASN A  1 204 ? 7.541   41.273  177.105 1.00 189.62 ?  234 ASN A ND2 1 
ATOM   1572  N N   . GLY A  1 205 ? 9.183   36.369  177.450 1.00 165.54 ?  235 GLY A N   1 
ATOM   1573  C CA  . GLY A  1 205 ? 8.346   35.203  177.643 1.00 161.48 ?  235 GLY A CA  1 
ATOM   1574  C C   . GLY A  1 205 ? 6.985   35.238  176.980 1.00 160.71 ?  235 GLY A C   1 
ATOM   1575  O O   . GLY A  1 205 ? 6.333   34.189  176.896 1.00 158.70 ?  235 GLY A O   1 
ATOM   1576  N N   . THR A  1 206 ? 6.514   36.396  176.523 1.00 159.40 ?  236 THR A N   1 
ATOM   1577  C CA  . THR A  1 206 ? 5.196   36.494  175.914 1.00 161.79 ?  236 THR A CA  1 
ATOM   1578  C C   . THR A  1 206 ? 5.298   37.233  174.590 1.00 163.39 ?  236 THR A C   1 
ATOM   1579  O O   . THR A  1 206 ? 5.963   38.270  174.507 1.00 164.90 ?  236 THR A O   1 
ATOM   1580  C CB  . THR A  1 206 ? 4.226   37.239  176.837 1.00 165.28 ?  236 THR A CB  1 
ATOM   1581  O OG1 . THR A  1 206 ? 4.850   38.441  177.308 1.00 167.11 ?  236 THR A OG1 1 
ATOM   1582  C CG2 . THR A  1 206 ? 3.859   36.375  178.024 1.00 164.01 ?  236 THR A CG2 1 
ATOM   1583  N N   . GLY A  1 207 ? 4.638   36.705  173.561 1.00 158.67 ?  237 GLY A N   1 
ATOM   1584  C CA  . GLY A  1 207 ? 4.652   37.333  172.261 1.00 160.23 ?  237 GLY A CA  1 
ATOM   1585  C C   . GLY A  1 207 ? 5.312   36.525  171.160 1.00 157.36 ?  237 GLY A C   1 
ATOM   1586  O O   . GLY A  1 207 ? 5.781   35.401  171.357 1.00 154.17 ?  237 GLY A O   1 
ATOM   1587  N N   . PRO A  1 208 ? 5.348   37.106  169.962 1.00 145.05 ?  238 PRO A N   1 
ATOM   1588  C CA  . PRO A  1 208 ? 5.981   36.434  168.819 1.00 145.06 ?  238 PRO A CA  1 
ATOM   1589  C C   . PRO A  1 208 ? 7.500   36.414  168.960 1.00 150.71 ?  238 PRO A C   1 
ATOM   1590  O O   . PRO A  1 208 ? 8.105   37.366  169.458 1.00 153.51 ?  238 PRO A O   1 
ATOM   1591  C CB  . PRO A  1 208 ? 5.523   37.275  167.622 1.00 146.40 ?  238 PRO A CB  1 
ATOM   1592  C CG  . PRO A  1 208 ? 5.289   38.633  168.196 1.00 149.10 ?  238 PRO A CG  1 
ATOM   1593  C CD  . PRO A  1 208 ? 4.756   38.402  169.587 1.00 149.16 ?  238 PRO A CD  1 
ATOM   1594  N N   . CYS A  1 209 ? 8.117   35.310  168.520 1.00 158.69 ?  239 CYS A N   1 
ATOM   1595  C CA  . CYS A  1 209 ? 9.569   35.127  168.598 1.00 164.68 ?  239 CYS A CA  1 
ATOM   1596  C C   . CYS A  1 209 ? 10.208  35.141  167.214 1.00 169.91 ?  239 CYS A C   1 
ATOM   1597  O O   . CYS A  1 209 ? 9.833   34.333  166.350 1.00 167.68 ?  239 CYS A O   1 
ATOM   1598  C CB  . CYS A  1 209 ? 9.884   33.812  169.317 1.00 162.71 ?  239 CYS A CB  1 
ATOM   1599  S SG  . CYS A  1 209 ? 11.641  33.408  169.410 1.00 170.34 ?  239 CYS A SG  1 
ATOM   1600  N N   . PRO A  1 210 ? 11.164  36.047  166.955 1.00 154.75 ?  240 PRO A N   1 
ATOM   1601  C CA  . PRO A  1 210 ? 11.804  36.112  165.628 1.00 160.66 ?  240 PRO A CA  1 
ATOM   1602  C C   . PRO A  1 210 ? 12.643  34.907  165.209 1.00 164.22 ?  240 PRO A C   1 
ATOM   1603  O O   . PRO A  1 210 ? 12.464  34.393  164.099 1.00 163.79 ?  240 PRO A O   1 
ATOM   1604  C CB  . PRO A  1 210 ? 12.680  37.369  165.732 1.00 165.20 ?  240 PRO A CB  1 
ATOM   1605  C CG  . PRO A  1 210 ? 12.071  38.176  166.841 1.00 160.25 ?  240 PRO A CG  1 
ATOM   1606  C CD  . PRO A  1 210 ? 11.568  37.167  167.822 1.00 155.64 ?  240 PRO A CD  1 
ATOM   1607  N N   . SER A  1 211 ? 13.563  34.452  166.068 1.00 167.50 ?  241 SER A N   1 
ATOM   1608  C CA  . SER A  1 211 ? 14.453  33.328  165.763 1.00 163.22 ?  241 SER A CA  1 
ATOM   1609  C C   . SER A  1 211 ? 14.008  32.113  166.569 1.00 152.88 ?  241 SER A C   1 
ATOM   1610  O O   . SER A  1 211 ? 14.389  31.950  167.732 1.00 147.99 ?  241 SER A O   1 
ATOM   1611  C CB  . SER A  1 211 ? 15.907  33.686  166.067 1.00 163.59 ?  241 SER A CB  1 
ATOM   1612  O OG  . SER A  1 211 ? 16.322  34.823  165.330 1.00 171.76 ?  241 SER A OG  1 
ATOM   1613  N N   . VAL A  1 212 ? 13.215  31.255  165.933 1.00 154.31 ?  242 VAL A N   1 
ATOM   1614  C CA  . VAL A  1 212 ? 12.667  30.051  166.545 1.00 151.31 ?  242 VAL A CA  1 
ATOM   1615  C C   . VAL A  1 212 ? 13.345  28.822  165.957 1.00 150.41 ?  242 VAL A C   1 
ATOM   1616  O O   . VAL A  1 212 ? 13.559  28.737  164.741 1.00 154.43 ?  242 VAL A O   1 
ATOM   1617  C CB  . VAL A  1 212 ? 11.140  29.964  166.355 1.00 151.79 ?  242 VAL A CB  1 
ATOM   1618  C CG1 . VAL A  1 212 ? 10.568  28.751  167.095 1.00 150.28 ?  242 VAL A CG1 1 
ATOM   1619  C CG2 . VAL A  1 212 ? 10.474  31.247  166.818 1.00 154.14 ?  242 VAL A CG2 1 
ATOM   1620  N N   . SER A  1 213 ? 13.688  27.876  166.827 1.00 143.64 ?  243 SER A N   1 
ATOM   1621  C CA  . SER A  1 213 ? 14.266  26.604  166.432 1.00 142.13 ?  243 SER A CA  1 
ATOM   1622  C C   . SER A  1 213 ? 13.500  25.503  167.148 1.00 141.09 ?  243 SER A C   1 
ATOM   1623  O O   . SER A  1 213 ? 12.895  25.724  168.200 1.00 141.19 ?  243 SER A O   1 
ATOM   1624  C CB  . SER A  1 213 ? 15.762  26.508  166.770 1.00 141.18 ?  243 SER A CB  1 
ATOM   1625  O OG  . SER A  1 213 ? 15.991  26.624  168.165 1.00 140.51 ?  243 SER A OG  1 
ATOM   1626  N N   . THR A  1 214 ? 13.527  24.310  166.572 1.00 148.17 ?  244 THR A N   1 
ATOM   1627  C CA  . THR A  1 214 ? 12.837  23.171  167.151 1.00 147.36 ?  244 THR A CA  1 
ATOM   1628  C C   . THR A  1 214 ? 13.838  22.171  167.707 1.00 145.86 ?  244 THR A C   1 
ATOM   1629  O O   . THR A  1 214 ? 14.939  21.996  167.175 1.00 145.59 ?  244 THR A O   1 
ATOM   1630  C CB  . THR A  1 214 ? 11.924  22.472  166.141 1.00 148.05 ?  244 THR A CB  1 
ATOM   1631  O OG1 . THR A  1 214 ? 11.345  21.312  166.755 1.00 147.32 ?  244 THR A OG1 1 
ATOM   1632  C CG2 . THR A  1 214 ? 12.707  22.041  164.913 1.00 148.14 ?  244 THR A CG2 1 
ATOM   1633  N N   . VAL A  1 215 ? 13.440  21.521  168.797 1.00 143.72 ?  245 VAL A N   1 
ATOM   1634  C CA  . VAL A  1 215 ? 14.247  20.492  169.430 1.00 140.09 ?  245 VAL A CA  1 
ATOM   1635  C C   . VAL A  1 215 ? 13.320  19.370  169.853 1.00 139.85 ?  245 VAL A C   1 
ATOM   1636  O O   . VAL A  1 215 ? 12.103  19.537  169.963 1.00 140.55 ?  245 VAL A O   1 
ATOM   1637  C CB  . VAL A  1 215 ? 15.021  20.993  170.668 1.00 139.38 ?  245 VAL A CB  1 
ATOM   1638  C CG1 . VAL A  1 215 ? 16.134  21.921  170.265 1.00 144.00 ?  245 VAL A CG1 1 
ATOM   1639  C CG2 . VAL A  1 215 ? 14.073  21.661  171.650 1.00 139.71 ?  245 VAL A CG2 1 
ATOM   1640  N N   . GLN A  1 216 ? 13.921  18.216  170.089 1.00 137.84 ?  246 GLN A N   1 
ATOM   1641  C CA  . GLN A  1 216 ? 13.164  17.073  170.558 1.00 137.72 ?  246 GLN A CA  1 
ATOM   1642  C C   . GLN A  1 216 ? 13.185  17.043  172.078 1.00 136.94 ?  246 GLN A C   1 
ATOM   1643  O O   . GLN A  1 216 ? 12.174  16.719  172.709 1.00 137.16 ?  246 GLN A O   1 
ATOM   1644  C CB  . GLN A  1 216 ? 13.721  15.777  169.974 1.00 137.66 ?  246 GLN A CB  1 
ATOM   1645  C CG  . GLN A  1 216 ? 12.850  14.584  170.286 1.00 137.93 ?  246 GLN A CG  1 
ATOM   1646  C CD  . GLN A  1 216 ? 11.485  14.698  169.612 1.00 140.00 ?  246 GLN A CD  1 
ATOM   1647  O OE1 . GLN A  1 216 ? 11.346  15.346  168.571 1.00 142.24 ?  246 GLN A OE1 1 
ATOM   1648  N NE2 . GLN A  1 216 ? 10.477  14.070  170.202 1.00 139.36 ?  246 GLN A NE2 1 
ATOM   1649  N N   . CYS A  1 217 ? 14.330  17.402  172.663 1.00 136.92 ?  247 CYS A N   1 
ATOM   1650  C CA  . CYS A  1 217 ? 14.547  17.443  174.104 1.00 136.50 ?  247 CYS A CA  1 
ATOM   1651  C C   . CYS A  1 217 ? 15.139  18.772  174.540 1.00 135.90 ?  247 CYS A C   1 
ATOM   1652  O O   . CYS A  1 217 ? 16.071  19.285  173.914 1.00 136.40 ?  247 CYS A O   1 
ATOM   1653  C CB  . CYS A  1 217 ? 15.466  16.315  174.571 1.00 136.31 ?  247 CYS A CB  1 
ATOM   1654  S SG  . CYS A  1 217 ? 14.954  14.691  174.054 1.00 150.71 ?  247 CYS A SG  1 
ATOM   1655  N N   . THR A  1 218 ? 14.573  19.321  175.613 1.00 127.70 ?  248 THR A N   1 
ATOM   1656  C CA  . THR A  1 218 ? 15.030  20.564  176.205 1.00 127.88 ?  248 THR A CA  1 
ATOM   1657  C C   . THR A  1 218 ? 16.385  20.374  176.879 1.00 127.01 ?  248 THR A C   1 
ATOM   1658  O O   . THR A  1 218 ? 16.863  19.256  177.085 1.00 126.31 ?  248 THR A O   1 
ATOM   1659  C CB  . THR A  1 218 ? 14.026  21.058  177.244 1.00 128.39 ?  248 THR A CB  1 
ATOM   1660  O OG1 . THR A  1 218 ? 14.011  20.148  178.351 1.00 127.58 ?  248 THR A OG1 1 
ATOM   1661  C CG2 . THR A  1 218 ? 12.631  21.129  176.646 1.00 129.48 ?  248 THR A CG2 1 
ATOM   1662  N N   . HIS A  1 219 ? 17.009  21.496  177.223 1.00 141.51 ?  249 HIS A N   1 
ATOM   1663  C CA  . HIS A  1 219 ? 18.292  21.448  177.902 1.00 140.96 ?  249 HIS A CA  1 
ATOM   1664  C C   . HIS A  1 219 ? 18.123  20.887  179.319 1.00 140.28 ?  249 HIS A C   1 
ATOM   1665  O O   . HIS A  1 219 ? 17.010  20.750  179.837 1.00 140.42 ?  249 HIS A O   1 
ATOM   1666  C CB  . HIS A  1 219 ? 18.937  22.836  177.899 1.00 141.74 ?  249 HIS A CB  1 
ATOM   1667  C CG  . HIS A  1 219 ? 18.195  23.858  178.703 1.00 142.49 ?  249 HIS A CG  1 
ATOM   1668  N ND1 . HIS A  1 219 ? 17.200  24.647  178.165 1.00 144.00 ?  249 HIS A ND1 1 
ATOM   1669  C CD2 . HIS A  1 219 ? 18.314  24.236  179.997 1.00 142.60 ?  249 HIS A CD2 1 
ATOM   1670  C CE1 . HIS A  1 219 ? 16.732  25.459  179.096 1.00 146.66 ?  249 HIS A CE1 1 
ATOM   1671  N NE2 . HIS A  1 219 ? 17.391  25.230  180.217 1.00 145.73 ?  249 HIS A NE2 1 
ATOM   1672  N N   . GLY A  1 220 ? 19.250  20.538  179.942 1.00 145.22 ?  250 GLY A N   1 
ATOM   1673  C CA  . GLY A  1 220 ? 19.239  19.982  181.286 1.00 144.67 ?  250 GLY A CA  1 
ATOM   1674  C C   . GLY A  1 220 ? 18.728  20.937  182.347 1.00 145.04 ?  250 GLY A C   1 
ATOM   1675  O O   . GLY A  1 220 ? 19.448  21.850  182.763 1.00 145.41 ?  250 GLY A O   1 
ATOM   1676  N N   . ILE A  1 221 ? 17.495  20.735  182.802 1.00 145.79 ?  251 ILE A N   1 
ATOM   1677  C CA  . ILE A  1 221 ? 16.875  21.581  183.819 1.00 146.15 ?  251 ILE A CA  1 
ATOM   1678  C C   . ILE A  1 221 ? 16.851  20.864  185.170 1.00 148.19 ?  251 ILE A C   1 
ATOM   1679  O O   . ILE A  1 221 ? 16.097  19.904  185.366 1.00 147.67 ?  251 ILE A O   1 
ATOM   1680  C CB  . ILE A  1 221 ? 15.472  22.024  183.387 1.00 146.48 ?  251 ILE A CB  1 
ATOM   1681  C CG1 . ILE A  1 221 ? 15.557  22.818  182.079 1.00 149.70 ?  251 ILE A CG1 1 
ATOM   1682  C CG2 . ILE A  1 221 ? 14.825  22.858  184.466 1.00 145.82 ?  251 ILE A CG2 1 
ATOM   1683  C CD1 . ILE A  1 221 ? 14.229  23.359  181.600 1.00 148.23 ?  251 ILE A CD1 1 
ATOM   1684  N N   . LYS A  1 222 ? 17.684  21.328  186.097 1.00 154.92 ?  252 LYS A N   1 
ATOM   1685  C CA  . LYS A  1 222 ? 17.762  20.760  187.445 1.00 154.62 ?  252 LYS A CA  1 
ATOM   1686  C C   . LYS A  1 222 ? 16.574  21.213  188.291 1.00 155.06 ?  252 LYS A C   1 
ATOM   1687  O O   . LYS A  1 222 ? 16.357  22.421  188.437 1.00 157.26 ?  252 LYS A O   1 
ATOM   1688  C CB  . LYS A  1 222 ? 19.073  21.141  188.119 1.00 153.12 ?  252 LYS A CB  1 
ATOM   1689  C CG  . LYS A  1 222 ? 20.298  20.554  187.438 1.00 151.70 ?  252 LYS A CG  1 
ATOM   1690  C CD  . LYS A  1 222 ? 21.583  21.048  188.078 1.00 149.29 ?  252 LYS A CD  1 
ATOM   1691  C CE  . LYS A  1 222 ? 21.781  22.534  187.847 1.00 156.47 ?  252 LYS A CE  1 
ATOM   1692  N NZ  . LYS A  1 222 ? 21.875  22.837  186.391 1.00 157.36 1  252 LYS A NZ  1 
ATOM   1693  N N   . PRO A  1 223 ? 15.791  20.292  188.866 1.00 149.69 ?  253 PRO A N   1 
ATOM   1694  C CA  . PRO A  1 223 ? 14.639  20.689  189.696 1.00 150.12 ?  253 PRO A CA  1 
ATOM   1695  C C   . PRO A  1 223 ? 15.021  21.227  191.069 1.00 154.43 ?  253 PRO A C   1 
ATOM   1696  O O   . PRO A  1 223 ? 14.848  20.544  192.084 1.00 155.54 ?  253 PRO A O   1 
ATOM   1697  C CB  . PRO A  1 223 ? 13.840  19.385  189.819 1.00 153.00 ?  253 PRO A CB  1 
ATOM   1698  C CG  . PRO A  1 223 ? 14.876  18.307  189.709 1.00 151.69 ?  253 PRO A CG  1 
ATOM   1699  C CD  . PRO A  1 223 ? 15.908  18.827  188.739 1.00 148.68 ?  253 PRO A CD  1 
ATOM   1700  N N   . VAL A  1 224 ? 15.541  22.452  191.112 1.00 159.98 ?  254 VAL A N   1 
ATOM   1701  C CA  . VAL A  1 224 ? 15.950  23.089  192.361 1.00 165.06 ?  254 VAL A CA  1 
ATOM   1702  C C   . VAL A  1 224 ? 14.751  23.778  193.008 1.00 169.96 ?  254 VAL A C   1 
ATOM   1703  O O   . VAL A  1 224 ? 14.232  24.772  192.493 1.00 171.48 ?  254 VAL A O   1 
ATOM   1704  C CB  . VAL A  1 224 ? 17.083  24.092  192.118 1.00 165.64 ?  254 VAL A CB  1 
ATOM   1705  C CG1 . VAL A  1 224 ? 17.445  24.805  193.408 1.00 173.13 ?  254 VAL A CG1 1 
ATOM   1706  C CG2 . VAL A  1 224 ? 18.294  23.394  191.521 1.00 162.88 ?  254 VAL A CG2 1 
ATOM   1707  N N   . VAL A  1 225 ? 14.313  23.237  194.143 1.00 159.66 ?  255 VAL A N   1 
ATOM   1708  C CA  . VAL A  1 225 ? 13.186  23.765  194.908 1.00 158.33 ?  255 VAL A CA  1 
ATOM   1709  C C   . VAL A  1 225 ? 13.712  24.840  195.855 1.00 156.76 ?  255 VAL A C   1 
ATOM   1710  O O   . VAL A  1 225 ? 14.449  24.534  196.797 1.00 156.60 ?  255 VAL A O   1 
ATOM   1711  C CB  . VAL A  1 225 ? 12.466  22.656  195.681 1.00 159.55 ?  255 VAL A CB  1 
ATOM   1712  C CG1 . VAL A  1 225 ? 11.269  23.226  196.416 1.00 171.16 ?  255 VAL A CG1 1 
ATOM   1713  C CG2 . VAL A  1 225 ? 12.050  21.545  194.742 1.00 155.04 ?  255 VAL A CG2 1 
ATOM   1714  N N   . SER A  1 226 ? 13.348  26.099  195.612 1.00 138.16 ?  256 SER A N   1 
ATOM   1715  C CA  . SER A  1 226 ? 13.798  27.191  196.468 1.00 140.57 ?  256 SER A CA  1 
ATOM   1716  C C   . SER A  1 226 ? 12.798  28.341  196.413 1.00 141.94 ?  256 SER A C   1 
ATOM   1717  O O   . SER A  1 226 ? 11.911  28.376  195.557 1.00 144.33 ?  256 SER A O   1 
ATOM   1718  C CB  . SER A  1 226 ? 15.192  27.680  196.058 1.00 140.15 ?  256 SER A CB  1 
ATOM   1719  O OG  . SER A  1 226 ? 15.194  28.152  194.721 1.00 138.51 ?  256 SER A OG  1 
ATOM   1720  N N   . THR A  1 227 ? 12.942  29.283  197.355 1.00 147.06 ?  257 THR A N   1 
ATOM   1721  C CA  . THR A  1 227 ? 12.083  30.460  197.421 1.00 147.75 ?  257 THR A CA  1 
ATOM   1722  C C   . THR A  1 227 ? 12.938  31.722  197.412 1.00 149.64 ?  257 THR A C   1 
ATOM   1723  O O   . THR A  1 227 ? 14.135  31.689  197.706 1.00 149.17 ?  257 THR A O   1 
ATOM   1724  C CB  . THR A  1 227 ? 11.205  30.475  198.688 1.00 150.14 ?  257 THR A CB  1 
ATOM   1725  O OG1 . THR A  1 227 ? 12.035  30.384  199.853 1.00 145.77 ?  257 THR A OG1 1 
ATOM   1726  C CG2 . THR A  1 227 ? 10.235  29.311  198.686 1.00 153.22 ?  257 THR A CG2 1 
ATOM   1727  N N   . GLN A  1 228 ? 12.294  32.845  197.088 1.00 150.55 ?  258 GLN A N   1 
ATOM   1728  C CA  . GLN A  1 228 ? 12.929  34.162  197.046 1.00 155.57 ?  258 GLN A CA  1 
ATOM   1729  C C   . GLN A  1 228 ? 14.122  34.252  196.093 1.00 153.34 ?  258 GLN A C   1 
ATOM   1730  O O   . GLN A  1 228 ? 14.097  35.056  195.155 1.00 153.38 ?  258 GLN A O   1 
ATOM   1731  C CB  . GLN A  1 228 ? 13.327  34.622  198.452 1.00 158.89 ?  258 GLN A CB  1 
ATOM   1732  C CG  . GLN A  1 228 ? 12.135  34.805  199.378 1.00 163.66 ?  258 GLN A CG  1 
ATOM   1733  C CD  . GLN A  1 228 ? 12.528  35.297  200.752 1.00 167.90 ?  258 GLN A CD  1 
ATOM   1734  O OE1 . GLN A  1 228 ? 13.710  35.429  201.062 1.00 168.40 ?  258 GLN A OE1 1 
ATOM   1735  N NE2 . GLN A  1 228 ? 11.533  35.600  201.577 1.00 172.82 ?  258 GLN A NE2 1 
ATOM   1736  N N   . LEU A  1 229 ? 15.163  33.442  196.306 1.00 160.25 ?  259 LEU A N   1 
ATOM   1737  C CA  . LEU A  1 229 ? 16.362  33.469  195.473 1.00 157.26 ?  259 LEU A CA  1 
ATOM   1738  C C   . LEU A  1 229 ? 16.397  32.270  194.531 1.00 155.88 ?  259 LEU A C   1 
ATOM   1739  O O   . LEU A  1 229 ? 16.433  31.121  194.985 1.00 152.89 ?  259 LEU A O   1 
ATOM   1740  C CB  . LEU A  1 229 ? 17.612  33.455  196.352 1.00 155.82 ?  259 LEU A CB  1 
ATOM   1741  C CG  . LEU A  1 229 ? 17.658  34.457  197.503 1.00 160.17 ?  259 LEU A CG  1 
ATOM   1742  C CD1 . LEU A  1 229 ? 18.955  34.305  198.279 1.00 163.42 ?  259 LEU A CD1 1 
ATOM   1743  C CD2 . LEU A  1 229 ? 17.494  35.881  196.995 1.00 163.88 ?  259 LEU A CD2 1 
ATOM   1744  N N   . LEU A  1 230 ? 16.390  32.542  193.224 1.00 170.07 ?  260 LEU A N   1 
ATOM   1745  C CA  . LEU A  1 230 ? 16.500  31.496  192.213 1.00 165.21 ?  260 LEU A CA  1 
ATOM   1746  C C   . LEU A  1 230 ? 17.952  31.039  192.118 1.00 164.67 ?  260 LEU A C   1 
ATOM   1747  O O   . LEU A  1 230 ? 18.840  31.845  191.816 1.00 166.29 ?  260 LEU A O   1 
ATOM   1748  C CB  . LEU A  1 230 ? 16.014  32.012  190.862 1.00 163.47 ?  260 LEU A CB  1 
ATOM   1749  C CG  . LEU A  1 230 ? 14.554  32.462  190.813 1.00 162.48 ?  260 LEU A CG  1 
ATOM   1750  C CD1 . LEU A  1 230 ? 14.205  32.998  189.430 1.00 162.11 ?  260 LEU A CD1 1 
ATOM   1751  C CD2 . LEU A  1 230 ? 13.624  31.327  191.219 1.00 156.31 ?  260 LEU A CD2 1 
ATOM   1752  N N   . LEU A  1 231 ? 18.198  29.762  192.387 1.00 166.01 ?  261 LEU A N   1 
ATOM   1753  C CA  . LEU A  1 231 ? 19.546  29.216  192.427 1.00 167.15 ?  261 LEU A CA  1 
ATOM   1754  C C   . LEU A  1 231 ? 19.799  28.260  191.262 1.00 165.74 ?  261 LEU A C   1 
ATOM   1755  O O   . LEU A  1 231 ? 18.915  27.488  190.878 1.00 164.08 ?  261 LEU A O   1 
ATOM   1756  C CB  . LEU A  1 231 ? 19.794  28.521  193.770 1.00 173.04 ?  261 LEU A CB  1 
ATOM   1757  C CG  . LEU A  1 231 ? 19.589  29.455  194.978 1.00 175.62 ?  261 LEU A CG  1 
ATOM   1758  C CD1 . LEU A  1 231 ? 19.937  28.785  196.308 1.00 178.49 ?  261 LEU A CD1 1 
ATOM   1759  C CD2 . LEU A  1 231 ? 20.351  30.771  194.819 1.00 174.67 ?  261 LEU A CD2 1 
ATOM   1760  N N   . ASN A  1 232 ? 21.024  28.307  190.728 1.00 171.80 ?  262 ASN A N   1 
ATOM   1761  C CA  . ASN A  1 232 ? 21.508  27.433  189.646 1.00 168.73 ?  262 ASN A CA  1 
ATOM   1762  C C   . ASN A  1 232 ? 20.618  27.364  188.405 1.00 166.61 ?  262 ASN A C   1 
ATOM   1763  O O   . ASN A  1 232 ? 20.335  26.284  187.881 1.00 163.35 ?  262 ASN A O   1 
ATOM   1764  C CB  . ASN A  1 232 ? 21.778  26.021  190.160 1.00 169.53 ?  262 ASN A CB  1 
ATOM   1765  C CG  . ASN A  1 232 ? 23.084  25.919  190.894 1.00 177.17 ?  262 ASN A CG  1 
ATOM   1766  O OD1 . ASN A  1 232 ? 23.352  26.675  191.829 1.00 180.91 ?  262 ASN A OD1 1 
ATOM   1767  N ND2 . ASN A  1 232 ? 23.937  25.005  190.442 1.00 182.23 ?  262 ASN A ND2 1 
ATOM   1768  N N   . GLY A  1 233 ? 20.177  28.519  187.910 1.00 163.30 ?  263 GLY A N   1 
ATOM   1769  C CA  . GLY A  1 233 ? 19.340  28.551  186.736 1.00 162.06 ?  263 GLY A CA  1 
ATOM   1770  C C   . GLY A  1 233 ? 20.149  29.010  185.531 1.00 161.14 ?  263 GLY A C   1 
ATOM   1771  O O   . GLY A  1 233 ? 21.357  29.226  185.602 1.00 160.61 ?  263 GLY A O   1 
ATOM   1772  N N   . SER A  1 234 ? 19.455  29.131  184.400 1.00 156.94 ?  264 SER A N   1 
ATOM   1773  C CA  . SER A  1 234 ? 20.113  29.580  183.180 1.00 155.96 ?  264 SER A CA  1 
ATOM   1774  C C   . SER A  1 234 ? 20.174  31.100  183.183 1.00 158.13 ?  264 SER A C   1 
ATOM   1775  O O   . SER A  1 234 ? 19.157  31.773  183.378 1.00 157.67 ?  264 SER A O   1 
ATOM   1776  C CB  . SER A  1 234 ? 19.387  29.073  181.932 1.00 153.97 ?  264 SER A CB  1 
ATOM   1777  O OG  . SER A  1 234 ? 19.352  27.657  181.877 1.00 150.50 ?  264 SER A OG  1 
ATOM   1778  N N   . LEU A  1 235 ? 21.368  31.637  182.969 1.00 158.25 ?  265 LEU A N   1 
ATOM   1779  C CA  . LEU A  1 235 ? 21.555  33.079  182.955 1.00 161.60 ?  265 LEU A CA  1 
ATOM   1780  C C   . LEU A  1 235 ? 21.001  33.692  181.670 1.00 162.47 ?  265 LEU A C   1 
ATOM   1781  O O   . LEU A  1 235 ? 21.017  33.077  180.600 1.00 158.84 ?  265 LEU A O   1 
ATOM   1782  C CB  . LEU A  1 235 ? 23.029  33.426  183.147 1.00 164.63 ?  265 LEU A CB  1 
ATOM   1783  C CG  . LEU A  1 235 ? 23.573  32.889  184.477 1.00 159.51 ?  265 LEU A CG  1 
ATOM   1784  C CD1 . LEU A  1 235 ? 24.569  31.747  184.263 1.00 155.14 ?  265 LEU A CD1 1 
ATOM   1785  C CD2 . LEU A  1 235 ? 24.152  34.000  185.335 1.00 164.44 ?  265 LEU A CD2 1 
ATOM   1786  N N   . ALA A  1 236 ? 20.511  34.923  181.786 1.00 158.85 ?  266 ALA A N   1 
ATOM   1787  C CA  . ALA A  1 236 ? 19.943  35.615  180.641 1.00 161.01 ?  266 ALA A CA  1 
ATOM   1788  C C   . ALA A  1 236 ? 21.057  36.190  179.773 1.00 164.13 ?  266 ALA A C   1 
ATOM   1789  O O   . ALA A  1 236 ? 22.232  36.209  180.149 1.00 163.56 ?  266 ALA A O   1 
ATOM   1790  C CB  . ALA A  1 236 ? 18.996  36.727  181.091 1.00 163.78 ?  266 ALA A CB  1 
ATOM   1791  N N   . GLU A  1 237 ? 20.676  36.663  178.593 1.00 178.29 ?  267 GLU A N   1 
ATOM   1792  C CA  . GLU A  1 237 ? 21.621  37.233  177.644 1.00 186.20 ?  267 GLU A CA  1 
ATOM   1793  C C   . GLU A  1 237 ? 21.643  38.753  177.676 1.00 193.78 ?  267 GLU A C   1 
ATOM   1794  O O   . GLU A  1 237 ? 20.610  39.412  177.836 1.00 196.73 ?  267 GLU A O   1 
ATOM   1795  C CB  . GLU A  1 237 ? 21.350  36.738  176.225 1.00 185.90 ?  267 GLU A CB  1 
ATOM   1796  C CG  . GLU A  1 237 ? 21.068  35.259  176.151 1.00 182.05 ?  267 GLU A CG  1 
ATOM   1797  C CD  . GLU A  1 237 ? 22.361  34.456  176.105 1.00 182.99 ?  267 GLU A CD  1 
ATOM   1798  O OE1 . GLU A  1 237 ? 23.436  35.035  176.383 1.00 188.26 ?  267 GLU A OE1 1 
ATOM   1799  O OE2 . GLU A  1 237 ? 22.310  33.255  175.775 1.00 183.39 -1 267 GLU A OE2 1 
ATOM   1800  N N   . GLU A  1 238 ? 22.854  39.284  177.516 1.00 196.77 ?  268 GLU A N   1 
ATOM   1801  C CA  . GLU A  1 238 ? 23.200  40.698  177.486 1.00 199.53 ?  268 GLU A CA  1 
ATOM   1802  C C   . GLU A  1 238 ? 22.706  41.375  178.756 1.00 204.12 ?  268 GLU A C   1 
ATOM   1803  O O   . GLU A  1 238 ? 23.205  41.084  179.848 1.00 207.61 ?  268 GLU A O   1 
ATOM   1804  C CB  . GLU A  1 238 ? 22.591  41.375  176.254 1.00 201.40 ?  268 GLU A CB  1 
ATOM   1805  C CG  . GLU A  1 238 ? 22.681  40.571  174.959 1.00 199.11 ?  268 GLU A CG  1 
ATOM   1806  C CD  . GLU A  1 238 ? 23.293  41.365  173.820 1.00 207.61 ?  268 GLU A CD  1 
ATOM   1807  O OE1 . GLU A  1 238 ? 23.010  42.578  173.716 1.00 220.48 ?  268 GLU A OE1 1 
ATOM   1808  O OE2 . GLU A  1 238 ? 24.050  40.772  173.021 1.00 211.56 -1 268 GLU A OE2 1 
ATOM   1809  N N   . GLU A  1 239 ? 21.734  42.271  178.633 1.00 202.45 ?  269 GLU A N   1 
ATOM   1810  C CA  . GLU A  1 239 ? 21.171  42.912  179.810 1.00 200.69 ?  269 GLU A CA  1 
ATOM   1811  C C   . GLU A  1 239 ? 20.185  41.972  180.504 1.00 191.22 ?  269 GLU A C   1 
ATOM   1812  O O   . GLU A  1 239 ? 19.539  41.129  179.870 1.00 185.15 ?  269 GLU A O   1 
ATOM   1813  C CB  . GLU A  1 239 ? 20.602  44.287  179.448 1.00 202.12 ?  269 GLU A CB  1 
ATOM   1814  C CG  . GLU A  1 239 ? 19.534  44.375  178.390 1.00 205.70 ?  269 GLU A CG  1 
ATOM   1815  C CD  . GLU A  1 239 ? 19.101  45.819  178.198 1.00 210.84 ?  269 GLU A CD  1 
ATOM   1816  O OE1 . GLU A  1 239 ? 19.432  46.646  179.075 1.00 216.93 ?  269 GLU A OE1 1 
ATOM   1817  O OE2 . GLU A  1 239 ? 18.463  46.136  177.174 1.00 215.71 -1 269 GLU A OE2 1 
ATOM   1818  N N   . VAL A  1 240 ? 20.076  42.132  181.826 1.00 182.24 ?  270 VAL A N   1 
ATOM   1819  C CA  . VAL A  1 240 ? 19.148  41.335  182.617 1.00 177.56 ?  270 VAL A CA  1 
ATOM   1820  C C   . VAL A  1 240 ? 17.691  41.599  182.249 1.00 179.66 ?  270 VAL A C   1 
ATOM   1821  O O   . VAL A  1 240 ? 17.293  42.720  181.905 1.00 189.60 ?  270 VAL A O   1 
ATOM   1822  C CB  . VAL A  1 240 ? 19.390  41.599  184.112 1.00 179.76 ?  270 VAL A CB  1 
ATOM   1823  C CG1 . VAL A  1 240 ? 20.749  41.041  184.532 1.00 173.11 ?  270 VAL A CG1 1 
ATOM   1824  C CG2 . VAL A  1 240 ? 19.307  43.086  184.400 1.00 190.63 ?  270 VAL A CG2 1 
ATOM   1825  N N   . MET A  1 241 ? 16.894  40.537  182.323 1.00 171.29 ?  271 MET A N   1 
ATOM   1826  C CA  . MET A  1 241 ? 15.501  40.519  181.910 1.00 172.62 ?  271 MET A CA  1 
ATOM   1827  C C   . MET A  1 241 ? 14.560  40.616  183.105 1.00 176.40 ?  271 MET A C   1 
ATOM   1828  O O   . MET A  1 241 ? 14.861  40.140  184.204 1.00 175.05 ?  271 MET A O   1 
ATOM   1829  C CB  . MET A  1 241 ? 15.189  39.250  181.119 1.00 167.15 ?  271 MET A CB  1 
ATOM   1830  C CG  . MET A  1 241 ? 14.148  39.467  180.053 1.00 168.40 ?  271 MET A CG  1 
ATOM   1831  S SD  . MET A  1 241 ? 14.741  40.640  178.819 1.00 170.98 ?  271 MET A SD  1 
ATOM   1832  C CE  . MET A  1 241 ? 16.200  39.799  178.204 1.00 171.41 ?  271 MET A CE  1 
ATOM   1833  N N   . ILE A  1 242 ? 13.409  41.240  182.870 1.00 163.33 ?  272 ILE A N   1 
ATOM   1834  C CA  . ILE A  1 242 ? 12.346  41.388  183.858 1.00 168.07 ?  272 ILE A CA  1 
ATOM   1835  C C   . ILE A  1 242 ? 11.072  40.825  183.238 1.00 165.77 ?  272 ILE A C   1 
ATOM   1836  O O   . ILE A  1 242 ? 10.615  41.328  182.205 1.00 168.13 ?  272 ILE A O   1 
ATOM   1837  C CB  . ILE A  1 242 ? 12.144  42.859  184.262 1.00 177.86 ?  272 ILE A CB  1 
ATOM   1838  C CG1 . ILE A  1 242 ? 13.434  43.464  184.826 1.00 175.50 ?  272 ILE A CG1 1 
ATOM   1839  C CG2 . ILE A  1 242 ? 11.029  42.980  185.277 1.00 183.31 ?  272 ILE A CG2 1 
ATOM   1840  C CD1 . ILE A  1 242 ? 13.937  42.787  186.081 1.00 174.21 ?  272 ILE A CD1 1 
ATOM   1841  N N   . ARG A  1 243 ? 10.490  39.796  183.861 1.00 159.01 ?  273 ARG A N   1 
ATOM   1842  C CA  . ARG A  1 243 ? 9.306   39.152  183.303 1.00 157.54 ?  273 ARG A CA  1 
ATOM   1843  C C   . ARG A  1 243 ? 8.172   39.137  184.316 1.00 159.85 ?  273 ARG A C   1 
ATOM   1844  O O   . ARG A  1 243 ? 8.384   38.840  185.496 1.00 160.04 ?  273 ARG A O   1 
ATOM   1845  C CB  . ARG A  1 243 ? 9.605   37.711  182.855 1.00 152.14 ?  273 ARG A CB  1 
ATOM   1846  C CG  . ARG A  1 243 ? 10.691  37.594  181.795 1.00 153.22 ?  273 ARG A CG  1 
ATOM   1847  C CD  . ARG A  1 243 ? 11.015  36.139  181.487 1.00 148.67 ?  273 ARG A CD  1 
ATOM   1848  N NE  . ARG A  1 243 ? 12.002  36.004  180.417 1.00 143.83 ?  273 ARG A NE  1 
ATOM   1849  C CZ  . ARG A  1 243 ? 13.313  35.907  180.610 1.00 142.95 ?  273 ARG A CZ  1 
ATOM   1850  N NH1 . ARG A  1 243 ? 13.809  35.928  181.838 1.00 146.89 1  273 ARG A NH1 1 
ATOM   1851  N NH2 . ARG A  1 243 ? 14.130  35.787  179.572 1.00 142.84 ?  273 ARG A NH2 1 
ATOM   1852  N N   . SER A  1 244 ? 6.964   39.449  183.844 1.00 164.00 ?  274 SER A N   1 
ATOM   1853  C CA  . SER A  1 244 ? 5.784   39.448  184.699 1.00 170.44 ?  274 SER A CA  1 
ATOM   1854  C C   . SER A  1 244 ? 4.530   39.246  183.862 1.00 173.99 ?  274 SER A C   1 
ATOM   1855  O O   . SER A  1 244 ? 4.447   39.726  182.729 1.00 175.10 ?  274 SER A O   1 
ATOM   1856  C CB  . SER A  1 244 ? 5.663   40.756  185.493 1.00 178.94 ?  274 SER A CB  1 
ATOM   1857  O OG  . SER A  1 244 ? 4.490   40.770  186.294 1.00 185.24 ?  274 SER A OG  1 
ATOM   1858  N N   . GLU A  1 245 ? 3.564   38.524  184.435 1.00 161.68 ?  275 GLU A N   1 
ATOM   1859  C CA  . GLU A  1 245 ? 2.293   38.281  183.760 1.00 166.03 ?  275 GLU A CA  1 
ATOM   1860  C C   . GLU A  1 245 ? 1.470   39.563  183.663 1.00 176.51 ?  275 GLU A C   1 
ATOM   1861  O O   . GLU A  1 245 ? 0.764   39.778  182.671 1.00 182.35 ?  275 GLU A O   1 
ATOM   1862  C CB  . GLU A  1 245 ? 1.512   37.173  184.469 1.00 166.25 ?  275 GLU A CB  1 
ATOM   1863  C CG  . GLU A  1 245 ? 0.220   36.780  183.760 1.00 170.88 ?  275 GLU A CG  1 
ATOM   1864  C CD  . GLU A  1 245 ? -0.501  35.642  184.448 1.00 171.01 ?  275 GLU A CD  1 
ATOM   1865  O OE1 . GLU A  1 245 ? -0.046  35.229  185.533 1.00 169.61 ?  275 GLU A OE1 1 
ATOM   1866  O OE2 . GLU A  1 245 ? -1.524  35.167  183.910 1.00 172.49 -1 275 GLU A OE2 1 
ATOM   1867  N N   . ASN A  1 246 ? 1.548   40.431  184.682 1.00 176.10 ?  276 ASN A N   1 
ATOM   1868  C CA  . ASN A  1 246 ? 0.826   41.709  184.667 1.00 184.10 ?  276 ASN A CA  1 
ATOM   1869  C C   . ASN A  1 246 ? 1.572   42.706  185.554 1.00 188.61 ?  276 ASN A C   1 
ATOM   1870  O O   . ASN A  1 246 ? 1.471   42.647  186.784 1.00 191.33 ?  276 ASN A O   1 
ATOM   1871  C CB  . ASN A  1 246 ? -0.615  41.544  185.133 1.00 192.45 ?  276 ASN A CB  1 
ATOM   1872  C CG  . ASN A  1 246 ? -1.494  42.724  184.740 1.00 206.34 ?  276 ASN A CG  1 
ATOM   1873  O OD1 . ASN A  1 246 ? -1.002  43.818  184.455 1.00 208.39 ?  276 ASN A OD1 1 
ATOM   1874  N ND2 . ASN A  1 246 ? -2.800  42.510  184.733 1.00 223.72 ?  276 ASN A ND2 1 
ATOM   1875  N N   . ILE A  1 247 ? 2.322   43.610  184.915 1.00 185.50 ?  277 ILE A N   1 
ATOM   1876  C CA  . ILE A  1 247 ? 3.117   44.594  185.646 1.00 187.40 ?  277 ILE A CA  1 
ATOM   1877  C C   . ILE A  1 247 ? 2.217   45.554  186.419 1.00 199.12 ?  277 ILE A C   1 
ATOM   1878  O O   . ILE A  1 247 ? 2.539   45.963  187.542 1.00 204.00 ?  277 ILE A O   1 
ATOM   1879  C CB  . ILE A  1 247 ? 4.030   45.356  184.665 1.00 178.60 ?  277 ILE A CB  1 
ATOM   1880  C CG1 . ILE A  1 247 ? 4.799   44.384  183.768 1.00 168.88 ?  277 ILE A CG1 1 
ATOM   1881  C CG2 . ILE A  1 247 ? 4.999   46.264  185.412 1.00 181.18 ?  277 ILE A CG2 1 
ATOM   1882  C CD1 . ILE A  1 247 ? 5.721   45.070  182.774 1.00 169.06 ?  277 ILE A CD1 1 
ATOM   1883  N N   . THR A  1 248 ? 1.074   45.924  185.835 1.00 204.21 ?  278 THR A N   1 
ATOM   1884  C CA  . THR A  1 248 ? 0.134   46.830  186.494 1.00 213.97 ?  278 THR A CA  1 
ATOM   1885  C C   . THR A  1 248 ? -0.503  46.215  187.737 1.00 215.51 ?  278 THR A C   1 
ATOM   1886  O O   . THR A  1 248 ? -0.889  46.943  188.659 1.00 222.00 ?  278 THR A O   1 
ATOM   1887  C CB  . THR A  1 248 ? -0.954  47.257  185.507 1.00 215.97 ?  278 THR A CB  1 
ATOM   1888  O OG1 . THR A  1 248 ? -1.629  46.094  185.011 1.00 211.33 ?  278 THR A OG1 1 
ATOM   1889  C CG2 . THR A  1 248 ? -0.348  48.022  184.333 1.00 211.43 ?  278 THR A CG2 1 
ATOM   1890  N N   . ASN A  1 249 ? -0.620  44.892  187.782 1.00 202.15 ?  279 ASN A N   1 
ATOM   1891  C CA  . ASN A  1 249 ? -1.195  44.182  188.918 1.00 200.87 ?  279 ASN A CA  1 
ATOM   1892  C C   . ASN A  1 249 ? -0.138  43.917  189.985 1.00 196.83 ?  279 ASN A C   1 
ATOM   1893  O O   . ASN A  1 249 ? 0.857   43.232  189.722 1.00 186.83 ?  279 ASN A O   1 
ATOM   1894  C CB  . ASN A  1 249 ? -1.822  42.868  188.457 1.00 194.52 ?  279 ASN A CB  1 
ATOM   1895  C CG  . ASN A  1 249 ? -2.803  42.304  189.464 1.00 194.77 ?  279 ASN A CG  1 
ATOM   1896  O OD1 . ASN A  1 249 ? -2.822  42.701  190.629 1.00 197.52 ?  279 ASN A OD1 1 
ATOM   1897  N ND2 . ASN A  1 249 ? -3.626  41.366  189.016 1.00 192.99 ?  279 ASN A ND2 1 
ATOM   1898  N N   . ASN A  1 250 ? -0.355  44.457  191.186 1.00 214.37 ?  280 ASN A N   1 
ATOM   1899  C CA  . ASN A  1 250 ? 0.604   44.265  192.264 1.00 214.84 ?  280 ASN A CA  1 
ATOM   1900  C C   . ASN A  1 250 ? 0.452   42.904  192.927 1.00 209.54 ?  280 ASN A C   1 
ATOM   1901  O O   . ASN A  1 250 ? 1.196   42.602  193.867 1.00 205.13 ?  280 ASN A O   1 
ATOM   1902  C CB  . ASN A  1 250 ? 0.399   45.327  193.347 1.00 225.35 ?  280 ASN A CB  1 
ATOM   1903  C CG  . ASN A  1 250 ? -0.977  45.227  194.000 1.00 232.01 ?  280 ASN A CG  1 
ATOM   1904  O OD1 . ASN A  1 250 ? -1.968  45.752  193.489 1.00 235.96 ?  280 ASN A OD1 1 
ATOM   1905  N ND2 . ASN A  1 250 ? -1.042  44.518  195.124 1.00 232.22 ?  280 ASN A ND2 1 
ATOM   1906  N N   . ALA A  1 251 ? -0.485  42.083  192.449 1.00 211.00 ?  281 ALA A N   1 
ATOM   1907  C CA  . ALA A  1 251 ? -0.733  40.744  192.963 1.00 206.29 ?  281 ALA A CA  1 
ATOM   1908  C C   . ALA A  1 251 ? -0.015  39.663  192.169 1.00 194.46 ?  281 ALA A C   1 
ATOM   1909  O O   . ALA A  1 251 ? 0.078   38.525  192.642 1.00 191.20 ?  281 ALA A O   1 
ATOM   1910  C CB  . ALA A  1 251 ? -2.240  40.449  192.983 1.00 208.63 ?  281 ALA A CB  1 
ATOM   1911  N N   . LYS A  1 252 ? 0.504   39.992  190.989 1.00 190.45 ?  282 LYS A N   1 
ATOM   1912  C CA  . LYS A  1 252 ? 1.226   39.037  190.163 1.00 177.42 ?  282 LYS A CA  1 
ATOM   1913  C C   . LYS A  1 252 ? 2.719   39.141  190.455 1.00 171.14 ?  282 LYS A C   1 
ATOM   1914  O O   . LYS A  1 252 ? 3.266   40.246  190.535 1.00 170.17 ?  282 LYS A O   1 
ATOM   1915  C CB  . LYS A  1 252 ? 0.926   39.294  188.688 1.00 179.64 ?  282 LYS A CB  1 
ATOM   1916  C CG  . LYS A  1 252 ? 0.382   38.072  187.975 1.00 178.09 ?  282 LYS A CG  1 
ATOM   1917  C CD  . LYS A  1 252 ? -0.954  37.663  188.591 1.00 187.66 ?  282 LYS A CD  1 
ATOM   1918  C CE  . LYS A  1 252 ? -1.521  36.430  187.921 1.00 186.12 ?  282 LYS A CE  1 
ATOM   1919  N NZ  . LYS A  1 252 ? -2.817  36.005  188.506 1.00 187.85 1  282 LYS A NZ  1 
ATOM   1920  N N   . ASN A  1 253 ? 3.372   37.987  190.610 1.00 164.03 ?  283 ASN A N   1 
ATOM   1921  C CA  . ASN A  1 253 ? 4.793   37.949  190.924 1.00 158.28 ?  283 ASN A CA  1 
ATOM   1922  C C   . ASN A  1 253 ? 5.622   38.431  189.734 1.00 154.36 ?  283 ASN A C   1 
ATOM   1923  O O   . ASN A  1 253 ? 5.189   38.381  188.580 1.00 155.17 ?  283 ASN A O   1 
ATOM   1924  C CB  . ASN A  1 253 ? 5.183   36.527  191.319 1.00 153.71 ?  283 ASN A CB  1 
ATOM   1925  C CG  . ASN A  1 253 ? 4.482   36.076  192.588 1.00 157.16 ?  283 ASN A CG  1 
ATOM   1926  O OD1 . ASN A  1 253 ? 3.492   36.679  193.007 1.00 157.50 ?  283 ASN A OD1 1 
ATOM   1927  N ND2 . ASN A  1 253 ? 4.966   34.989  193.176 1.00 157.82 ?  283 ASN A ND2 1 
ATOM   1928  N N   . ILE A  1 254 ? 6.832   38.910  190.035 1.00 143.62 ?  284 ILE A N   1 
ATOM   1929  C CA  . ILE A  1 254 ? 7.766   39.434  189.036 1.00 142.27 ?  284 ILE A CA  1 
ATOM   1930  C C   . ILE A  1 254 ? 9.039   38.593  188.995 1.00 136.52 ?  284 ILE A C   1 
ATOM   1931  O O   . ILE A  1 254 ? 9.904   38.720  189.870 1.00 136.80 ?  284 ILE A O   1 
ATOM   1932  C CB  . ILE A  1 254 ? 8.094   40.904  189.311 1.00 149.16 ?  284 ILE A CB  1 
ATOM   1933  C CG1 . ILE A  1 254 ? 6.805   41.731  189.400 1.00 159.98 ?  284 ILE A CG1 1 
ATOM   1934  C CG2 . ILE A  1 254 ? 9.022   41.445  188.249 1.00 144.00 ?  284 ILE A CG2 1 
ATOM   1935  C CD1 . ILE A  1 254 ? 7.028   43.203  189.699 1.00 166.84 ?  284 ILE A CD1 1 
ATOM   1936  N N   . LEU A  1 255 ? 9.155   37.717  187.998 1.00 141.48 ?  285 LEU A N   1 
ATOM   1937  C CA  . LEU A  1 255 ? 10.327  36.862  187.845 1.00 139.31 ?  285 LEU A CA  1 
ATOM   1938  C C   . LEU A  1 255 ? 11.480  37.632  187.194 1.00 138.94 ?  285 LEU A C   1 
ATOM   1939  O O   . LEU A  1 255 ? 11.328  38.171  186.092 1.00 138.46 ?  285 LEU A O   1 
ATOM   1940  C CB  . LEU A  1 255 ? 9.957   35.623  187.037 1.00 136.74 ?  285 LEU A CB  1 
ATOM   1941  C CG  . LEU A  1 255 ? 8.856   34.824  187.743 1.00 137.16 ?  285 LEU A CG  1 
ATOM   1942  C CD1 . LEU A  1 255 ? 8.567   33.514  187.029 1.00 134.60 ?  285 LEU A CD1 1 
ATOM   1943  C CD2 . LEU A  1 255 ? 9.195   34.586  189.212 1.00 138.53 ?  285 LEU A CD2 1 
ATOM   1944  N N   . VAL A  1 256 ? 12.625  37.688  187.874 1.00 151.97 ?  286 VAL A N   1 
ATOM   1945  C CA  . VAL A  1 256 ? 13.822  38.378  187.396 1.00 150.27 ?  286 VAL A CA  1 
ATOM   1946  C C   . VAL A  1 256 ? 14.856  37.339  186.983 1.00 145.33 ?  286 VAL A C   1 
ATOM   1947  O O   . VAL A  1 256 ? 15.010  36.313  187.653 1.00 149.65 ?  286 VAL A O   1 
ATOM   1948  C CB  . VAL A  1 256 ? 14.400  39.319  188.468 1.00 153.99 ?  286 VAL A CB  1 
ATOM   1949  C CG1 . VAL A  1 256 ? 15.588  40.081  187.911 1.00 156.53 ?  286 VAL A CG1 1 
ATOM   1950  C CG2 . VAL A  1 256 ? 13.331  40.269  188.946 1.00 158.58 ?  286 VAL A CG2 1 
ATOM   1951  N N   . GLN A  1 257 ? 15.561  37.597  185.880 1.00 159.93 ?  287 GLN A N   1 
ATOM   1952  C CA  . GLN A  1 257 ? 16.629  36.717  185.413 1.00 158.34 ?  287 GLN A CA  1 
ATOM   1953  C C   . GLN A  1 257 ? 17.936  37.492  185.283 1.00 159.79 ?  287 GLN A C   1 
ATOM   1954  O O   . GLN A  1 257 ? 17.965  38.574  184.686 1.00 159.37 ?  287 GLN A O   1 
ATOM   1955  C CB  . GLN A  1 257 ? 16.277  36.057  184.078 1.00 157.41 ?  287 GLN A CB  1 
ATOM   1956  C CG  . GLN A  1 257 ? 17.274  34.973  183.674 1.00 152.35 ?  287 GLN A CG  1 
ATOM   1957  C CD  . GLN A  1 257 ? 16.890  34.254  182.395 1.00 149.99 ?  287 GLN A CD  1 
ATOM   1958  O OE1 . GLN A  1 257 ? 15.984  34.678  181.677 1.00 152.90 ?  287 GLN A OE1 1 
ATOM   1959  N NE2 . GLN A  1 257 ? 17.587  33.163  182.099 1.00 143.38 ?  287 GLN A NE2 1 
ATOM   1960  N N   . PHE A  1 258 ? 19.006  36.934  185.848 1.00 163.54 ?  288 PHE A N   1 
ATOM   1961  C CA  . PHE A  1 258 ? 20.327  37.546  185.912 1.00 163.25 ?  288 PHE A CA  1 
ATOM   1962  C C   . PHE A  1 258 ? 21.183  37.207  184.695 1.00 161.17 ?  288 PHE A C   1 
ATOM   1963  O O   . PHE A  1 258 ? 20.967  36.210  184.001 1.00 160.36 ?  288 PHE A O   1 
ATOM   1964  C CB  . PHE A  1 258 ? 21.080  37.093  187.163 1.00 164.44 ?  288 PHE A CB  1 
ATOM   1965  C CG  . PHE A  1 258 ? 20.527  37.640  188.437 1.00 169.53 ?  288 PHE A CG  1 
ATOM   1966  C CD1 . PHE A  1 258 ? 19.834  38.835  188.451 1.00 173.56 ?  288 PHE A CD1 1 
ATOM   1967  C CD2 . PHE A  1 258 ? 20.719  36.967  189.630 1.00 167.57 ?  288 PHE A CD2 1 
ATOM   1968  C CE1 . PHE A  1 258 ? 19.324  39.337  189.629 1.00 173.78 ?  288 PHE A CE1 1 
ATOM   1969  C CE2 . PHE A  1 258 ? 20.215  37.463  190.812 1.00 168.95 ?  288 PHE A CE2 1 
ATOM   1970  C CZ  . PHE A  1 258 ? 19.517  38.650  190.813 1.00 171.34 ?  288 PHE A CZ  1 
ATOM   1971  N N   . ASN A  1 259 ? 22.165  38.072  184.441 1.00 165.29 ?  289 ASN A N   1 
ATOM   1972  C CA  . ASN A  1 259 ? 23.171  37.882  183.404 1.00 166.43 ?  289 ASN A CA  1 
ATOM   1973  C C   . ASN A  1 259 ? 24.467  37.301  183.965 1.00 169.05 ?  289 ASN A C   1 
ATOM   1974  O O   . ASN A  1 259 ? 25.018  36.353  183.402 1.00 169.02 ?  289 ASN A O   1 
ATOM   1975  C CB  . ASN A  1 259 ? 23.456  39.204  182.678 1.00 167.50 ?  289 ASN A CB  1 
ATOM   1976  C CG  . ASN A  1 259 ? 24.597  39.088  181.678 1.00 175.56 ?  289 ASN A CG  1 
ATOM   1977  O OD1 . ASN A  1 259 ? 25.754  39.342  182.010 1.00 181.86 ?  289 ASN A OD1 1 
ATOM   1978  N ND2 . ASN A  1 259 ? 24.272  38.712  180.443 1.00 179.79 ?  289 ASN A ND2 1 
ATOM   1979  N N   . THR A  1 260 ? 24.982  37.877  185.078 1.00 167.56 ?  290 THR A N   1 
ATOM   1980  C CA  . THR A  1 260 ? 26.157  37.450  185.842 1.00 167.02 ?  290 THR A CA  1 
ATOM   1981  C C   . THR A  1 260 ? 25.770  36.760  187.145 1.00 161.72 ?  290 THR A C   1 
ATOM   1982  O O   . THR A  1 260 ? 24.990  37.318  187.931 1.00 160.55 ?  290 THR A O   1 
ATOM   1983  C CB  . THR A  1 260 ? 27.054  38.645  186.145 1.00 174.54 ?  290 THR A CB  1 
ATOM   1984  O OG1 . THR A  1 260 ? 26.337  39.586  186.956 1.00 179.53 ?  290 THR A OG1 1 
ATOM   1985  C CG2 . THR A  1 260 ? 27.510  39.313  184.853 1.00 176.15 ?  290 THR A CG2 1 
ATOM   1986  N N   . PRO A  1 261 ? 26.273  35.545  187.383 1.00 164.38 ?  291 PRO A N   1 
ATOM   1987  C CA  . PRO A  1 261 ? 25.900  34.796  188.594 1.00 162.98 ?  291 PRO A CA  1 
ATOM   1988  C C   . PRO A  1 261 ? 26.472  35.425  189.860 1.00 168.41 ?  291 PRO A C   1 
ATOM   1989  O O   . PRO A  1 261 ? 27.591  35.942  189.867 1.00 172.78 ?  291 PRO A O   1 
ATOM   1990  C CB  . PRO A  1 261 ? 26.504  33.410  188.347 1.00 160.87 ?  291 PRO A CB  1 
ATOM   1991  C CG  . PRO A  1 261 ? 27.677  33.688  187.465 1.00 161.07 ?  291 PRO A CG  1 
ATOM   1992  C CD  . PRO A  1 261 ? 27.268  34.825  186.571 1.00 164.19 ?  291 PRO A CD  1 
ATOM   1993  N N   . VAL A  1 262 ? 25.688  35.378  190.937 1.00 162.10 ?  292 VAL A N   1 
ATOM   1994  C CA  . VAL A  1 262 ? 26.093  35.891  192.246 1.00 165.12 ?  292 VAL A CA  1 
ATOM   1995  C C   . VAL A  1 262 ? 26.583  34.748  193.133 1.00 164.56 ?  292 VAL A C   1 
ATOM   1996  O O   . VAL A  1 262 ? 25.811  33.853  193.497 1.00 163.62 ?  292 VAL A O   1 
ATOM   1997  C CB  . VAL A  1 262 ? 24.947  36.649  192.930 1.00 167.81 ?  292 VAL A CB  1 
ATOM   1998  C CG1 . VAL A  1 262 ? 25.384  37.162  194.298 1.00 171.05 ?  292 VAL A CG1 1 
ATOM   1999  C CG2 . VAL A  1 262 ? 24.445  37.795  192.053 1.00 168.76 ?  292 VAL A CG2 1 
ATOM   2000  N N   . GLN A  1 263 ? 27.873  34.772  193.466 1.00 168.61 ?  293 GLN A N   1 
ATOM   2001  C CA  . GLN A  1 263 ? 28.476  33.727  194.285 1.00 171.02 ?  293 GLN A CA  1 
ATOM   2002  C C   . GLN A  1 263 ? 27.854  33.749  195.678 1.00 177.69 ?  293 GLN A C   1 
ATOM   2003  O O   . GLN A  1 263 ? 27.920  34.766  196.376 1.00 180.32 ?  293 GLN A O   1 
ATOM   2004  C CB  . GLN A  1 263 ? 29.989  33.949  194.378 1.00 170.89 ?  293 GLN A CB  1 
ATOM   2005  C CG  . GLN A  1 263 ? 30.819  32.767  194.875 1.00 172.47 ?  293 GLN A CG  1 
ATOM   2006  C CD  . GLN A  1 263 ? 31.122  31.737  193.805 1.00 173.01 ?  293 GLN A CD  1 
ATOM   2007  O OE1 . GLN A  1 263 ? 30.443  31.660  192.781 1.00 167.98 ?  293 GLN A OE1 1 
ATOM   2008  N NE2 . GLN A  1 263 ? 32.159  30.940  194.038 1.00 184.63 ?  293 GLN A NE2 1 
ATOM   2009  N N   . ILE A  1 264 ? 27.262  32.631  196.090 1.00 175.94 ?  294 ILE A N   1 
ATOM   2010  C CA  . ILE A  1 264 ? 26.656  32.497  197.411 1.00 175.38 ?  294 ILE A CA  1 
ATOM   2011  C C   . ILE A  1 264 ? 27.322  31.313  198.093 1.00 175.45 ?  294 ILE A C   1 
ATOM   2012  O O   . ILE A  1 264 ? 27.509  30.257  197.474 1.00 173.24 ?  294 ILE A O   1 
ATOM   2013  C CB  . ILE A  1 264 ? 25.126  32.322  197.353 1.00 170.95 ?  294 ILE A CB  1 
ATOM   2014  C CG1 . ILE A  1 264 ? 24.558  32.232  198.771 1.00 172.04 ?  294 ILE A CG1 1 
ATOM   2015  C CG2 . ILE A  1 264 ? 24.735  31.096  196.554 1.00 169.08 ?  294 ILE A CG2 1 
ATOM   2016  C CD1 . ILE A  1 264 ? 23.058  32.100  198.827 1.00 165.67 ?  294 ILE A CD1 1 
ATOM   2017  N N   . ASN A  1 265 ? 27.698  31.495  199.358 1.00 178.00 ?  295 ASN A N   1 
ATOM   2018  C CA  . ASN A  1 265 ? 28.380  30.462  200.124 1.00 177.38 ?  295 ASN A CA  1 
ATOM   2019  C C   . ASN A  1 265 ? 27.553  30.163  201.365 1.00 180.97 ?  295 ASN A C   1 
ATOM   2020  O O   . ASN A  1 265 ? 27.311  31.064  202.174 1.00 185.01 ?  295 ASN A O   1 
ATOM   2021  C CB  . ASN A  1 265 ? 29.756  30.999  200.521 1.00 180.78 ?  295 ASN A CB  1 
ATOM   2022  C CG  . ASN A  1 265 ? 30.653  31.221  199.321 1.00 173.75 ?  295 ASN A CG  1 
ATOM   2023  O OD1 . ASN A  1 265 ? 30.193  31.710  198.292 1.00 171.58 ?  295 ASN A OD1 1 
ATOM   2024  N ND2 . ASN A  1 265 ? 31.929  30.932  199.454 1.00 183.06 ?  295 ASN A ND2 1 
ATOM   2025  N N   . CYS A  1 266 ? 27.153  28.901  201.534 1.00 167.83 ?  296 CYS A N   1 
ATOM   2026  C CA  . CYS A  1 266 ? 26.363  28.453  202.676 1.00 169.80 ?  296 CYS A CA  1 
ATOM   2027  C C   . CYS A  1 266 ? 27.043  27.300  203.401 1.00 170.58 ?  296 CYS A C   1 
ATOM   2028  O O   . CYS A  1 266 ? 27.514  26.344  202.776 1.00 172.75 ?  296 CYS A O   1 
ATOM   2029  C CB  . CYS A  1 266 ? 24.940  28.058  202.247 1.00 171.87 ?  296 CYS A CB  1 
ATOM   2030  S SG  . CYS A  1 266 ? 24.030  29.374  201.353 1.00 202.22 ?  296 CYS A SG  1 
ATOM   2031  N N   . THR A  1 267 ? 27.048  27.381  204.727 1.00 159.05 ?  297 THR A N   1 
ATOM   2032  C CA  . THR A  1 267 ? 27.663  26.364  205.561 1.00 162.02 ?  297 THR A CA  1 
ATOM   2033  C C   . THR A  1 267 ? 26.754  26.029  206.730 1.00 158.84 ?  297 THR A C   1 
ATOM   2034  O O   . THR A  1 267 ? 25.847  26.787  207.087 1.00 160.56 ?  297 THR A O   1 
ATOM   2035  C CB  . THR A  1 267 ? 29.044  26.791  206.062 1.00 169.03 ?  297 THR A CB  1 
ATOM   2036  O OG1 . THR A  1 267 ? 29.005  28.158  206.492 1.00 171.75 ?  297 THR A OG1 1 
ATOM   2037  C CG2 . THR A  1 267 ? 30.063  26.619  204.961 1.00 172.91 ?  297 THR A CG2 1 
ATOM   2038  N N   . ARG A  1 268 ? 27.031  24.871  207.328 1.00 143.16 ?  298 ARG A N   1 
ATOM   2039  C CA  . ARG A  1 268 ? 26.332  24.369  208.508 1.00 144.93 ?  298 ARG A CA  1 
ATOM   2040  C C   . ARG A  1 268 ? 27.396  24.105  209.564 1.00 151.33 ?  298 ARG A C   1 
ATOM   2041  O O   . ARG A  1 268 ? 27.855  22.964  209.729 1.00 162.98 ?  298 ARG A O   1 
ATOM   2042  C CB  . ARG A  1 268 ? 25.528  23.111  208.184 1.00 143.73 ?  298 ARG A CB  1 
ATOM   2043  C CG  . ARG A  1 268 ? 24.359  22.877  209.129 1.00 144.41 ?  298 ARG A CG  1 
ATOM   2044  C CD  . ARG A  1 268 ? 24.740  22.197  210.435 1.00 146.94 ?  298 ARG A CD  1 
ATOM   2045  N NE  . ARG A  1 268 ? 25.237  20.847  210.201 1.00 152.65 ?  298 ARG A NE  1 
ATOM   2046  C CZ  . ARG A  1 268 ? 24.463  19.767  210.141 1.00 152.16 ?  298 ARG A CZ  1 
ATOM   2047  N NH1 . ARG A  1 268 ? 23.149  19.874  210.298 1.00 144.63 1  298 ARG A NH1 1 
ATOM   2048  N NH2 . ARG A  1 268 ? 25.002  18.578  209.914 1.00 158.69 ?  298 ARG A NH2 1 
ATOM   2049  N N   . PRO A  1 269 ? 27.790  25.125  210.330 1.00 149.77 ?  299 PRO A N   1 
ATOM   2050  C CA  . PRO A  1 269 ? 28.875  24.961  211.310 1.00 152.40 ?  299 PRO A CA  1 
ATOM   2051  C C   . PRO A  1 269 ? 28.494  24.110  212.512 1.00 155.31 ?  299 PRO A C   1 
ATOM   2052  O O   . PRO A  1 269 ? 28.523  24.598  213.646 1.00 158.85 ?  299 PRO A O   1 
ATOM   2053  C CB  . PRO A  1 269 ? 29.182  26.405  211.728 1.00 154.34 ?  299 PRO A CB  1 
ATOM   2054  C CG  . PRO A  1 269 ? 27.890  27.131  211.526 1.00 153.64 ?  299 PRO A CG  1 
ATOM   2055  C CD  . PRO A  1 269 ? 27.261  26.501  210.311 1.00 150.32 ?  299 PRO A CD  1 
ATOM   2056  N N   . ASN A  1 270 ? 28.148  22.842  212.290 1.00 154.22 ?  300 ASN A N   1 
ATOM   2057  C CA  . ASN A  1 270 ? 27.798  21.951  213.396 1.00 158.68 ?  300 ASN A CA  1 
ATOM   2058  C C   . ASN A  1 270 ? 28.136  20.516  213.009 1.00 166.26 ?  300 ASN A C   1 
ATOM   2059  O O   . ASN A  1 270 ? 27.436  19.916  212.187 1.00 167.26 ?  300 ASN A O   1 
ATOM   2060  C CB  . ASN A  1 270 ? 26.307  22.072  213.733 1.00 154.32 ?  300 ASN A CB  1 
ATOM   2061  C CG  . ASN A  1 270 ? 25.985  23.249  214.655 1.00 153.28 ?  300 ASN A CG  1 
ATOM   2062  O OD1 . ASN A  1 270 ? 26.737  23.570  215.574 1.00 158.39 ?  300 ASN A OD1 1 
ATOM   2063  N ND2 . ASN A  1 270 ? 24.853  23.899  214.397 1.00 150.69 ?  300 ASN A ND2 1 
ATOM   2064  N N   . ASN A  1 271 ? 29.211  19.970  213.586 1.00 162.48 ?  301 ASN A N   1 
ATOM   2065  C CA  . ASN A  1 271 ? 29.594  18.586  213.323 1.00 168.36 ?  301 ASN A CA  1 
ATOM   2066  C C   . ASN A  1 271 ? 28.606  17.652  214.010 1.00 173.72 ?  301 ASN A C   1 
ATOM   2067  O O   . ASN A  1 271 ? 28.836  17.227  215.147 1.00 178.77 ?  301 ASN A O   1 
ATOM   2068  C CB  . ASN A  1 271 ? 31.024  18.296  213.809 1.00 169.71 ?  301 ASN A CB  1 
ATOM   2069  C CG  . ASN A  1 271 ? 31.586  16.987  213.250 1.00 168.46 ?  301 ASN A CG  1 
ATOM   2070  O OD1 . ASN A  1 271 ? 30.988  16.379  212.369 1.00 168.39 ?  301 ASN A OD1 1 
ATOM   2071  N ND2 . ASN A  1 271 ? 32.738  16.546  213.775 1.00 181.03 ?  301 ASN A ND2 1 
ATOM   2072  N N   . ASN A  1 272 ? 27.498  17.343  213.344 1.00 170.01 ?  302 ASN A N   1 
ATOM   2073  C CA  . ASN A  1 272 ? 26.474  16.515  213.959 1.00 169.74 ?  302 ASN A CA  1 
ATOM   2074  C C   . ASN A  1 272 ? 26.906  15.051  213.973 1.00 172.46 ?  302 ASN A C   1 
ATOM   2075  O O   . ASN A  1 272 ? 27.772  14.619  213.207 1.00 172.12 ?  302 ASN A O   1 
ATOM   2076  C CB  . ASN A  1 272 ? 25.139  16.658  213.219 1.00 164.82 ?  302 ASN A CB  1 
ATOM   2077  C CG  . ASN A  1 272 ? 24.514  18.040  213.377 1.00 160.91 ?  302 ASN A CG  1 
ATOM   2078  O OD1 . ASN A  1 272 ? 25.170  18.989  213.808 1.00 162.61 ?  302 ASN A OD1 1 
ATOM   2079  N ND2 . ASN A  1 272 ? 23.238  18.157  213.016 1.00 152.19 ?  302 ASN A ND2 1 
ATOM   2080  N N   . THR A  1 273 ? 26.275  14.288  214.858 1.00 159.53 ?  303 THR A N   1 
ATOM   2081  C CA  . THR A  1 273 ? 26.511  12.858  215.010 1.00 161.53 ?  303 THR A CA  1 
ATOM   2082  C C   . THR A  1 273 ? 25.185  12.153  214.774 1.00 160.03 ?  303 THR A C   1 
ATOM   2083  O O   . THR A  1 273 ? 24.145  12.594  215.276 1.00 158.89 ?  303 THR A O   1 
ATOM   2084  C CB  . THR A  1 273 ? 27.062  12.506  216.390 1.00 167.16 ?  303 THR A CB  1 
ATOM   2085  O OG1 . THR A  1 273 ? 28.243  13.275  216.631 1.00 177.40 ?  303 THR A OG1 1 
ATOM   2086  C CG2 . THR A  1 273 ? 27.429  11.028  216.447 1.00 167.38 ?  303 THR A CG2 1 
ATOM   2087  N N   . ARG A  1 274 ? 25.220  11.070  214.003 1.00 165.75 ?  304 ARG A N   1 
ATOM   2088  C CA  . ARG A  1 274 ? 24.024  10.310  213.667 1.00 163.99 ?  304 ARG A CA  1 
ATOM   2089  C C   . ARG A  1 274 ? 23.846  9.108   214.588 1.00 165.59 ?  304 ARG A C   1 
ATOM   2090  O O   . ARG A  1 274 ? 24.571  8.110   214.476 1.00 166.12 ?  304 ARG A O   1 
ATOM   2091  C CB  . ARG A  1 274 ? 24.103  9.857   212.216 1.00 161.76 ?  304 ARG A CB  1 
ATOM   2092  C CG  . ARG A  1 274 ? 22.993  8.967   211.785 1.00 159.61 ?  304 ARG A CG  1 
ATOM   2093  C CD  . ARG A  1 274 ? 23.282  8.495   210.404 1.00 157.35 ?  304 ARG A CD  1 
ATOM   2094  N NE  . ARG A  1 274 ? 22.324  9.090   209.484 1.00 152.31 ?  304 ARG A NE  1 
ATOM   2095  C CZ  . ARG A  1 274 ? 22.271  8.822   208.186 1.00 148.65 ?  304 ARG A CZ  1 
ATOM   2096  N NH1 . ARG A  1 274 ? 23.130  7.963   207.647 1.00 150.15 1  304 ARG A NH1 1 
ATOM   2097  N NH2 . ARG A  1 274 ? 21.368  9.421   207.431 1.00 142.93 ?  304 ARG A NH2 1 
ATOM   2098  N N   . LYS A  1 275 ? 22.900  9.226   215.512 1.00 158.18 ?  305 LYS A N   1 
ATOM   2099  C CA  . LYS A  1 275 ? 22.494  8.134   216.381 1.00 159.47 ?  305 LYS A CA  1 
ATOM   2100  C C   . LYS A  1 275 ? 21.419  7.334   215.654 1.00 157.36 ?  305 LYS A C   1 
ATOM   2101  O O   . LYS A  1 275 ? 20.387  7.892   215.263 1.00 154.92 ?  305 LYS A O   1 
ATOM   2102  C CB  . LYS A  1 275 ? 21.994  8.690   217.711 1.00 161.72 ?  305 LYS A CB  1 
ATOM   2103  C CG  . LYS A  1 275 ? 23.133  8.931   218.680 1.00 164.89 ?  305 LYS A CG  1 
ATOM   2104  C CD  . LYS A  1 275 ? 22.681  9.148   220.103 1.00 168.20 ?  305 LYS A CD  1 
ATOM   2105  C CE  . LYS A  1 275 ? 23.893  9.310   221.007 1.00 171.35 ?  305 LYS A CE  1 
ATOM   2106  N NZ  . LYS A  1 275 ? 23.536  9.826   222.354 1.00 174.65 1  305 LYS A NZ  1 
ATOM   2107  N N   . SER A  1 276 ? 21.656  6.035   215.477 1.00 167.31 ?  306 SER A N   1 
ATOM   2108  C CA  . SER A  1 276 ? 20.733  5.146   214.769 1.00 165.27 ?  306 SER A CA  1 
ATOM   2109  C C   . SER A  1 276 ? 19.979  4.272   215.771 1.00 166.56 ?  306 SER A C   1 
ATOM   2110  O O   . SER A  1 276 ? 20.271  3.088   215.935 1.00 167.13 ?  306 SER A O   1 
ATOM   2111  C CB  . SER A  1 276 ? 21.489  4.298   213.744 1.00 164.31 ?  306 SER A CB  1 
ATOM   2112  O OG  . SER A  1 276 ? 22.542  3.560   214.347 1.00 165.65 ?  306 SER A OG  1 
ATOM   2113  N N   . ILE A  1 277 ? 18.993  4.865   216.454 1.00 170.48 ?  307 ILE A N   1 
ATOM   2114  C CA  . ILE A  1 277 ? 18.176  4.093   217.392 1.00 171.75 ?  307 ILE A CA  1 
ATOM   2115  C C   . ILE A  1 277 ? 17.265  3.145   216.618 1.00 169.16 ?  307 ILE A C   1 
ATOM   2116  O O   . ILE A  1 277 ? 16.771  3.474   215.530 1.00 165.26 ?  307 ILE A O   1 
ATOM   2117  C CB  . ILE A  1 277 ? 17.355  5.019   218.309 1.00 172.23 ?  307 ILE A CB  1 
ATOM   2118  C CG1 . ILE A  1 277 ? 16.434  5.926   217.492 1.00 167.81 ?  307 ILE A CG1 1 
ATOM   2119  C CG2 . ILE A  1 277 ? 18.259  5.862   219.194 1.00 174.71 ?  307 ILE A CG2 1 
ATOM   2120  C CD1 . ILE A  1 277 ? 15.554  6.822   218.342 1.00 166.58 ?  307 ILE A CD1 1 
ATOM   2121  N N   . ARG A  1 278 ? 17.042  1.952   217.182 1.00 164.57 ?  308 ARG A N   1 
ATOM   2122  C CA  . ARG A  1 278 ? 16.334  0.863   216.511 1.00 162.27 ?  308 ARG A CA  1 
ATOM   2123  C C   . ARG A  1 278 ? 14.895  0.743   217.009 1.00 160.92 ?  308 ARG A C   1 
ATOM   2124  O O   . ARG A  1 278 ? 14.656  0.291   218.133 1.00 164.03 ?  308 ARG A O   1 
ATOM   2125  C CB  . ARG A  1 278 ? 17.098  -0.433  216.773 1.00 163.48 ?  308 ARG A CB  1 
ATOM   2126  C CG  . ARG A  1 278 ? 18.562  -0.365  216.361 1.00 161.15 ?  308 ARG A CG  1 
ATOM   2127  C CD  . ARG A  1 278 ? 19.323  -1.598  216.807 1.00 161.70 ?  308 ARG A CD  1 
ATOM   2128  N NE  . ARG A  1 278 ? 18.827  -2.837  216.229 1.00 157.99 ?  308 ARG A NE  1 
ATOM   2129  C CZ  . ARG A  1 278 ? 19.370  -4.024  216.471 1.00 157.40 ?  308 ARG A CZ  1 
ATOM   2130  N NH1 . ARG A  1 278 ? 20.421  -4.122  217.277 1.00 160.05 1  308 ARG A NH1 1 
ATOM   2131  N NH2 . ARG A  1 278 ? 18.859  -5.111  215.914 1.00 153.97 ?  308 ARG A NH2 1 
ATOM   2132  N N   . ILE A  1 279 ? 13.938  1.158   216.180 1.00 153.29 ?  309 ILE A N   1 
ATOM   2133  C CA  . ILE A  1 279 ? 12.521  0.947   216.459 1.00 152.37 ?  309 ILE A CA  1 
ATOM   2134  C C   . ILE A  1 279 ? 12.097  -0.277  215.659 1.00 150.11 ?  309 ILE A C   1 
ATOM   2135  O O   . ILE A  1 279 ? 11.272  -0.175  214.744 1.00 147.69 ?  309 ILE A O   1 
ATOM   2136  C CB  . ILE A  1 279 ? 11.650  2.175   216.137 1.00 151.56 ?  309 ILE A CB  1 
ATOM   2137  C CG1 . ILE A  1 279 ? 12.356  3.464   216.564 1.00 153.05 ?  309 ILE A CG1 1 
ATOM   2138  C CG2 . ILE A  1 279 ? 10.285  2.055   216.818 1.00 152.88 ?  309 ILE A CG2 1 
ATOM   2139  C CD1 . ILE A  1 279 ? 11.571  4.721   216.252 1.00 152.44 ?  309 ILE A CD1 1 
ATOM   2140  N N   . GLY A  1 280 ? 12.658  -1.436  215.982 1.00 181.21 ?  312 GLY A N   1 
ATOM   2141  C CA  . GLY A  1 280 ? 12.372  -2.635  215.214 1.00 179.72 ?  312 GLY A CA  1 
ATOM   2142  C C   . GLY A  1 280 ? 10.954  -3.152  215.358 1.00 178.99 ?  312 GLY A C   1 
ATOM   2143  O O   . GLY A  1 280 ? 10.150  -2.567  216.084 1.00 179.56 ?  312 GLY A O   1 
ATOM   2144  N N   . PRO A  1 281 ? 10.634  -4.256  214.661 1.00 176.11 ?  313 PRO A N   1 
ATOM   2145  C CA  . PRO A  1 281 ? 11.559  -4.973  213.775 1.00 173.67 ?  313 PRO A CA  1 
ATOM   2146  C C   . PRO A  1 281 ? 11.647  -4.402  212.361 1.00 172.25 ?  313 PRO A C   1 
ATOM   2147  O O   . PRO A  1 281 ? 10.625  -4.192  211.708 1.00 171.17 ?  313 PRO A O   1 
ATOM   2148  C CB  . PRO A  1 281 ? 10.962  -6.381  213.734 1.00 174.98 ?  313 PRO A CB  1 
ATOM   2149  C CG  . PRO A  1 281 ? 9.501   -6.165  213.908 1.00 173.10 ?  313 PRO A CG  1 
ATOM   2150  C CD  . PRO A  1 281 ? 9.348   -4.963  214.805 1.00 175.57 ?  313 PRO A CD  1 
ATOM   2151  N N   . GLY A  1 282 ? 12.867  -4.157  211.893 1.00 169.98 ?  314 GLY A N   1 
ATOM   2152  C CA  . GLY A  1 282 ? 13.047  -3.654  210.547 1.00 167.48 ?  314 GLY A CA  1 
ATOM   2153  C C   . GLY A  1 282 ? 13.354  -2.174  210.473 1.00 167.61 ?  314 GLY A C   1 
ATOM   2154  O O   . GLY A  1 282 ? 14.423  -1.774  210.001 1.00 166.16 ?  314 GLY A O   1 
ATOM   2155  N N   . GLN A  1 283 ? 12.407  -1.356  210.928 1.00 168.70 ?  315 GLN A N   1 
ATOM   2156  C CA  . GLN A  1 283 ? 12.543  0.093   210.890 1.00 169.23 ?  315 GLN A CA  1 
ATOM   2157  C C   . GLN A  1 283 ? 13.664  0.573   211.809 1.00 171.11 ?  315 GLN A C   1 
ATOM   2158  O O   . GLN A  1 283 ? 14.010  -0.080  212.798 1.00 172.64 ?  315 GLN A O   1 
ATOM   2159  C CB  . GLN A  1 283 ? 11.223  0.747   211.308 1.00 170.37 ?  315 GLN A CB  1 
ATOM   2160  C CG  . GLN A  1 283 ? 10.126  0.689   210.254 1.00 168.77 ?  315 GLN A CG  1 
ATOM   2161  C CD  . GLN A  1 283 ? 9.469   -0.682  210.180 1.00 167.98 ?  315 GLN A CD  1 
ATOM   2162  O OE1 . GLN A  1 283 ? 9.754   -1.566  210.991 1.00 168.71 ?  315 GLN A OE1 1 
ATOM   2163  N NE2 . GLN A  1 283 ? 8.588   -0.865  209.203 1.00 166.57 ?  315 GLN A NE2 1 
ATOM   2164  N N   . ALA A  1 284 ? 14.241  1.727   211.460 1.00 170.10 ?  316 ALA A N   1 
ATOM   2165  C CA  . ALA A  1 284 ? 15.318  2.331   212.239 1.00 171.61 ?  316 ALA A CA  1 
ATOM   2166  C C   . ALA A  1 284 ? 15.294  3.844   212.059 1.00 172.29 ?  316 ALA A C   1 
ATOM   2167  O O   . ALA A  1 284 ? 15.282  4.332   210.924 1.00 170.11 ?  316 ALA A O   1 
ATOM   2168  C CB  . ALA A  1 284 ? 16.682  1.771   211.818 1.00 169.74 ?  316 ALA A CB  1 
ATOM   2169  N N   . PHE A  1 285 ? 15.282  4.575   213.176 1.00 150.94 ?  317 PHE A N   1 
ATOM   2170  C CA  . PHE A  1 285 ? 15.238  6.034   213.185 1.00 152.25 ?  317 PHE A CA  1 
ATOM   2171  C C   . PHE A  1 285 ? 16.633  6.617   213.383 1.00 153.11 ?  317 PHE A C   1 
ATOM   2172  O O   . PHE A  1 285 ? 17.399  6.141   214.226 1.00 154.36 ?  317 PHE A O   1 
ATOM   2173  C CB  . PHE A  1 285 ? 14.300  6.559   214.273 1.00 154.73 ?  317 PHE A CB  1 
ATOM   2174  C CG  . PHE A  1 285 ? 14.360  8.047   214.442 1.00 156.60 ?  317 PHE A CG  1 
ATOM   2175  C CD1 . PHE A  1 285 ? 13.822  8.883   213.482 1.00 155.91 ?  317 PHE A CD1 1 
ATOM   2176  C CD2 . PHE A  1 285 ? 14.954  8.611   215.554 1.00 159.13 ?  317 PHE A CD2 1 
ATOM   2177  C CE1 . PHE A  1 285 ? 13.883  10.251  213.625 1.00 157.82 ?  317 PHE A CE1 1 
ATOM   2178  C CE2 . PHE A  1 285 ? 15.009  9.978   215.705 1.00 161.01 ?  317 PHE A CE2 1 
ATOM   2179  C CZ  . PHE A  1 285 ? 14.475  10.800  214.738 1.00 160.40 ?  317 PHE A CZ  1 
ATOM   2180  N N   . TYR A  1 286 ? 16.962  7.646   212.599 1.00 167.77 ?  318 TYR A N   1 
ATOM   2181  C CA  . TYR A  1 286 ? 18.259  8.317   212.677 1.00 168.32 ?  318 TYR A CA  1 
ATOM   2182  C C   . TYR A  1 286 ? 18.121  9.621   213.463 1.00 171.76 ?  318 TYR A C   1 
ATOM   2183  O O   . TYR A  1 286 ? 17.697  10.644  212.919 1.00 171.81 ?  318 TYR A O   1 
ATOM   2184  C CB  . TYR A  1 286 ? 18.799  8.549   211.271 1.00 164.54 ?  318 TYR A CB  1 
ATOM   2185  C CG  . TYR A  1 286 ? 19.003  7.248   210.527 1.00 160.80 ?  318 TYR A CG  1 
ATOM   2186  C CD1 . TYR A  1 286 ? 20.042  6.392   210.867 1.00 160.29 ?  318 TYR A CD1 1 
ATOM   2187  C CD2 . TYR A  1 286 ? 18.141  6.864   209.506 1.00 157.82 ?  318 TYR A CD2 1 
ATOM   2188  C CE1 . TYR A  1 286 ? 20.227  5.194   210.202 1.00 156.81 ?  318 TYR A CE1 1 
ATOM   2189  C CE2 . TYR A  1 286 ? 18.319  5.667   208.834 1.00 154.35 ?  318 TYR A CE2 1 
ATOM   2190  C CZ  . TYR A  1 286 ? 19.363  4.837   209.185 1.00 153.82 ?  318 TYR A CZ  1 
ATOM   2191  O OH  . TYR A  1 286 ? 19.536  3.647   208.514 1.00 150.22 ?  318 TYR A OH  1 
ATOM   2192  N N   . ALA A  1 287 ? 18.458  9.571   214.752 1.00 158.61 ?  319 ALA A N   1 
ATOM   2193  C CA  . ALA A  1 287 ? 18.395  10.714  215.650 1.00 161.93 ?  319 ALA A CA  1 
ATOM   2194  C C   . ALA A  1 287 ? 19.666  11.553  215.550 1.00 162.72 ?  319 ALA A C   1 
ATOM   2195  O O   . ALA A  1 287 ? 20.647  11.174  214.902 1.00 160.51 ?  319 ALA A O   1 
ATOM   2196  C CB  . ALA A  1 287 ? 18.184  10.255  217.092 1.00 164.22 ?  319 ALA A CB  1 
ATOM   2197  N N   . THR A  1 288 ? 19.647  12.706  216.214 1.00 165.57 ?  320 THR A N   1 
ATOM   2198  C CA  . THR A  1 288 ? 20.812  13.581  216.269 1.00 166.97 ?  320 THR A CA  1 
ATOM   2199  C C   . THR A  1 288 ? 21.499  13.449  217.621 1.00 169.89 ?  320 THR A C   1 
ATOM   2200  O O   . THR A  1 288 ? 20.909  13.772  218.658 1.00 172.27 ?  320 THR A O   1 
ATOM   2201  C CB  . THR A  1 288 ? 20.444  15.046  216.033 1.00 168.54 ?  320 THR A CB  1 
ATOM   2202  O OG1 . THR A  1 288 ? 19.504  15.148  214.960 1.00 166.27 ?  320 THR A OG1 1 
ATOM   2203  C CG2 . THR A  1 288 ? 21.695  15.853  215.700 1.00 168.88 ?  320 THR A CG2 1 
ATOM   2204  N N   . GLY A  1 289 ? 22.737  12.975  217.603 1.00 177.82 ?  321 GLY A N   1 
ATOM   2205  C CA  . GLY A  1 289 ? 23.527  12.805  218.799 1.00 180.63 ?  321 GLY A CA  1 
ATOM   2206  C C   . GLY A  1 289 ? 24.058  14.152  219.244 1.00 183.64 ?  321 GLY A C   1 
ATOM   2207  O O   . GLY A  1 289 ? 23.555  15.209  218.859 1.00 184.15 ?  321 GLY A O   1 
ATOM   2208  N N   . ASP A  1 290 A 25.090  14.107  220.078 1.00 182.73 ?  321 ASP A N   1 
ATOM   2209  C CA  . ASP A  1 290 A 25.722  15.335  220.540 1.00 190.89 ?  321 ASP A CA  1 
ATOM   2210  C C   . ASP A  1 290 A 26.506  15.989  219.395 1.00 183.33 ?  321 ASP A C   1 
ATOM   2211  O O   . ASP A  1 290 A 26.899  15.327  218.427 1.00 177.06 ?  321 ASP A O   1 
ATOM   2212  C CB  . ASP A  1 290 A 26.601  15.033  221.755 1.00 199.72 ?  321 ASP A CB  1 
ATOM   2213  C CG  . ASP A  1 290 A 27.606  13.935  221.472 1.00 198.83 ?  321 ASP A CG  1 
ATOM   2214  O OD1 . ASP A  1 290 A 27.248  12.953  220.804 1.00 191.71 ?  321 ASP A OD1 1 
ATOM   2215  O OD2 . ASP A  1 290 A 28.739  14.024  222.010 1.00 203.82 -1 321 ASP A OD2 1 
ATOM   2216  N N   . ILE A  1 291 ? 26.726  17.306  219.512 1.00 174.94 ?  322 ILE A N   1 
ATOM   2217  C CA  . ILE A  1 291 ? 27.422  18.125  218.513 1.00 173.83 ?  322 ILE A CA  1 
ATOM   2218  C C   . ILE A  1 291 ? 28.892  18.278  218.886 1.00 175.24 ?  322 ILE A C   1 
ATOM   2219  O O   . ILE A  1 291 ? 29.215  18.694  220.006 1.00 179.23 ?  322 ILE A O   1 
ATOM   2220  C CB  . ILE A  1 291 ? 26.763  19.508  218.360 1.00 175.63 ?  322 ILE A CB  1 
ATOM   2221  C CG1 . ILE A  1 291 ? 25.286  19.362  217.993 1.00 173.94 ?  322 ILE A CG1 1 
ATOM   2222  C CG2 . ILE A  1 291 ? 27.486  20.336  217.296 1.00 173.98 ?  322 ILE A CG2 1 
ATOM   2223  C CD1 . ILE A  1 291 ? 24.572  20.691  217.791 1.00 174.30 ?  322 ILE A CD1 1 
ATOM   2224  N N   . ILE A  1 292 ? 29.780  17.952  217.947 1.00 179.02 ?  323 ILE A N   1 
ATOM   2225  C CA  . ILE A  1 292 ? 31.222  18.042  218.153 1.00 178.66 ?  323 ILE A CA  1 
ATOM   2226  C C   . ILE A  1 292 ? 31.708  19.446  217.804 1.00 180.70 ?  323 ILE A C   1 
ATOM   2227  O O   . ILE A  1 292 ? 31.730  19.839  216.634 1.00 178.74 ?  323 ILE A O   1 
ATOM   2228  C CB  . ILE A  1 292 ? 31.971  16.994  217.321 1.00 170.91 ?  323 ILE A CB  1 
ATOM   2229  C CG1 . ILE A  1 292 ? 31.421  15.593  217.580 1.00 165.39 ?  323 ILE A CG1 1 
ATOM   2230  C CG2 . ILE A  1 292 ? 33.464  17.046  217.606 1.00 171.76 ?  323 ILE A CG2 1 
ATOM   2231  C CD1 . ILE A  1 292 ? 30.847  14.951  216.342 1.00 161.81 ?  323 ILE A CD1 1 
ATOM   2232  N N   . GLY A  1 293 ? 32.093  20.205  218.833 1.00 197.28 ?  324 GLY A N   1 
ATOM   2233  C CA  . GLY A  1 293 ? 32.637  21.541  218.677 1.00 198.79 ?  324 GLY A CA  1 
ATOM   2234  C C   . GLY A  1 293 ? 31.773  22.601  219.347 1.00 203.47 ?  324 GLY A C   1 
ATOM   2235  O O   . GLY A  1 293 ? 31.176  22.362  220.402 1.00 213.12 ?  324 GLY A O   1 
ATOM   2236  N N   . ASP A  1 294 ? 31.716  23.769  218.715 1.00 194.94 ?  325 ASP A N   1 
ATOM   2237  C CA  . ASP A  1 294 ? 31.005  24.943  219.199 1.00 199.43 ?  325 ASP A CA  1 
ATOM   2238  C C   . ASP A  1 294 ? 29.590  25.007  218.638 1.00 195.07 ?  325 ASP A C   1 
ATOM   2239  O O   . ASP A  1 294 ? 29.324  24.560  217.517 1.00 188.41 ?  325 ASP A O   1 
ATOM   2240  C CB  . ASP A  1 294 ? 31.800  26.202  218.860 1.00 200.51 ?  325 ASP A CB  1 
ATOM   2241  C CG  . ASP A  1 294 ? 33.196  26.175  219.467 1.00 205.68 ?  325 ASP A CG  1 
ATOM   2242  O OD1 . ASP A  1 294 ? 33.337  25.695  220.613 1.00 211.74 ?  325 ASP A OD1 1 
ATOM   2243  O OD2 . ASP A  1 294 ? 34.153  26.619  218.800 1.00 204.62 -1 325 ASP A OD2 1 
ATOM   2244  N N   . ILE A  1 295 ? 28.681  25.579  219.428 1.00 189.86 ?  326 ILE A N   1 
ATOM   2245  C CA  . ILE A  1 295 ? 27.292  25.760  219.008 1.00 187.70 ?  326 ILE A CA  1 
ATOM   2246  C C   . ILE A  1 295 ? 27.192  27.024  218.159 1.00 185.77 ?  326 ILE A C   1 
ATOM   2247  O O   . ILE A  1 295 ? 27.097  28.136  218.683 1.00 188.42 ?  326 ILE A O   1 
ATOM   2248  C CB  . ILE A  1 295 ? 26.334  25.831  220.203 1.00 190.81 ?  326 ILE A CB  1 
ATOM   2249  C CG1 . ILE A  1 295 ? 26.386  24.576  221.092 1.00 192.13 ?  326 ILE A CG1 1 
ATOM   2250  C CG2 . ILE A  1 295 ? 24.917  26.101  219.726 1.00 188.41 ?  326 ILE A CG2 1 
ATOM   2251  C CD1 . ILE A  1 295 ? 27.530  24.524  222.105 1.00 195.60 ?  326 ILE A CD1 1 
ATOM   2252  N N   . ARG A  1 296 ? 27.233  26.855  216.838 1.00 188.30 ?  327 ARG A N   1 
ATOM   2253  C CA  . ARG A  1 296 ? 27.111  27.943  215.881 1.00 185.65 ?  327 ARG A CA  1 
ATOM   2254  C C   . ARG A  1 296 ? 25.898  27.668  215.004 1.00 181.85 ?  327 ARG A C   1 
ATOM   2255  O O   . ARG A  1 296 ? 25.426  26.531  214.905 1.00 180.39 ?  327 ARG A O   1 
ATOM   2256  C CB  . ARG A  1 296 ? 28.364  28.110  215.009 1.00 182.68 ?  327 ARG A CB  1 
ATOM   2257  C CG  . ARG A  1 296 ? 29.576  28.619  215.758 1.00 185.87 ?  327 ARG A CG  1 
ATOM   2258  C CD  . ARG A  1 296 ? 30.830  28.598  214.894 1.00 182.46 ?  327 ARG A CD  1 
ATOM   2259  N NE  . ARG A  1 296 ? 30.619  29.223  213.592 1.00 177.19 ?  327 ARG A NE  1 
ATOM   2260  C CZ  . ARG A  1 296 ? 31.552  29.326  212.650 1.00 172.84 ?  327 ARG A CZ  1 
ATOM   2261  N NH1 . ARG A  1 296 ? 31.265  29.910  211.495 1.00 167.81 1  327 ARG A NH1 1 
ATOM   2262  N NH2 . ARG A  1 296 ? 32.772  28.850  212.861 1.00 173.28 ?  327 ARG A NH2 1 
ATOM   2263  N N   . GLN A  1 297 ? 25.386  28.721  214.379 1.00 184.89 ?  328 GLN A N   1 
ATOM   2264  C CA  . GLN A  1 297 ? 24.223  28.634  213.511 1.00 181.50 ?  328 GLN A CA  1 
ATOM   2265  C C   . GLN A  1 297 ? 24.641  28.741  212.052 1.00 175.91 ?  328 GLN A C   1 
ATOM   2266  O O   . GLN A  1 297 ? 25.650  29.367  211.720 1.00 175.02 ?  328 GLN A O   1 
ATOM   2267  C CB  . GLN A  1 297 ? 23.201  29.725  213.826 1.00 183.89 ?  328 GLN A CB  1 
ATOM   2268  C CG  . GLN A  1 297 ? 23.811  31.071  214.125 1.00 186.24 ?  328 GLN A CG  1 
ATOM   2269  C CD  . GLN A  1 297 ? 22.791  32.029  214.690 1.00 189.94 ?  328 GLN A CD  1 
ATOM   2270  O OE1 . GLN A  1 297 ? 23.048  32.726  215.670 1.00 193.31 ?  328 GLN A OE1 1 
ATOM   2271  N NE2 . GLN A  1 297 ? 21.628  32.094  214.051 1.00 189.31 ?  328 GLN A NE2 1 
ATOM   2272  N N   . ALA A  1 298 ? 23.843  28.129  211.188 1.00 178.63 ?  329 ALA A N   1 
ATOM   2273  C CA  . ALA A  1 298 ? 24.121  28.144  209.763 1.00 172.67 ?  329 ALA A CA  1 
ATOM   2274  C C   . ALA A  1 298 ? 24.001  29.564  209.218 1.00 171.83 ?  329 ALA A C   1 
ATOM   2275  O O   . ALA A  1 298 ? 23.245  30.389  209.737 1.00 175.28 ?  329 ALA A O   1 
ATOM   2276  C CB  . ALA A  1 298 ? 23.161  27.215  209.028 1.00 169.12 ?  329 ALA A CB  1 
ATOM   2277  N N   . HIS A  1 299 ? 24.772  29.854  208.172 1.00 180.77 ?  330 HIS A N   1 
ATOM   2278  C CA  . HIS A  1 299 ? 24.763  31.182  207.573 1.00 179.59 ?  330 HIS A CA  1 
ATOM   2279  C C   . HIS A  1 299 ? 25.158  31.061  206.106 1.00 172.31 ?  330 HIS A C   1 
ATOM   2280  O O   . HIS A  1 299 ? 25.771  30.072  205.691 1.00 168.48 ?  330 HIS A O   1 
ATOM   2281  C CB  . HIS A  1 299 ? 25.684  32.149  208.331 1.00 183.68 ?  330 HIS A CB  1 
ATOM   2282  C CG  . HIS A  1 299 ? 27.131  31.775  208.279 1.00 182.03 ?  330 HIS A CG  1 
ATOM   2283  N ND1 . HIS A  1 299 ? 27.690  30.841  209.124 1.00 180.84 ?  330 HIS A ND1 1 
ATOM   2284  C CD2 . HIS A  1 299 ? 28.137  32.217  207.488 1.00 181.50 ?  330 HIS A CD2 1 
ATOM   2285  C CE1 . HIS A  1 299 ? 28.976  30.716  208.850 1.00 179.46 ?  330 HIS A CE1 1 
ATOM   2286  N NE2 . HIS A  1 299 ? 29.273  31.541  207.862 1.00 179.87 ?  330 HIS A NE2 1 
ATOM   2287  N N   . CYS A  1 300 ? 24.798  32.089  205.325 1.00 182.69 ?  331 CYS A N   1 
ATOM   2288  C CA  . CYS A  1 300 ? 25.116  32.179  203.901 1.00 175.48 ?  331 CYS A CA  1 
ATOM   2289  C C   . CYS A  1 300 ? 25.796  33.518  203.629 1.00 174.62 ?  331 CYS A C   1 
ATOM   2290  O O   . CYS A  1 300 ? 25.330  34.556  204.109 1.00 178.28 ?  331 CYS A O   1 
ATOM   2291  C CB  . CYS A  1 300 ? 23.838  32.069  203.049 1.00 172.40 ?  331 CYS A CB  1 
ATOM   2292  S SG  . CYS A  1 300 ? 23.126  30.384  202.875 1.00 170.81 ?  331 CYS A SG  1 
ATOM   2293  N N   . ASN A  1 301 ? 26.890  33.499  202.861 1.00 173.48 ?  332 ASN A N   1 
ATOM   2294  C CA  . ASN A  1 301 ? 27.648  34.703  202.528 1.00 172.10 ?  332 ASN A CA  1 
ATOM   2295  C C   . ASN A  1 301 ? 27.476  35.139  201.077 1.00 168.94 ?  332 ASN A C   1 
ATOM   2296  O O   . ASN A  1 301 ? 27.567  34.311  200.163 1.00 165.76 ?  332 ASN A O   1 
ATOM   2297  C CB  . ASN A  1 301 ? 29.142  34.481  202.752 1.00 171.42 ?  332 ASN A CB  1 
ATOM   2298  C CG  . ASN A  1 301 ? 29.527  34.499  204.187 1.00 178.75 ?  332 ASN A CG  1 
ATOM   2299  O OD1 . ASN A  1 301 ? 28.723  34.808  205.063 1.00 184.57 ?  332 ASN A OD1 1 
ATOM   2300  N ND2 . ASN A  1 301 ? 30.780  34.189  204.446 1.00 178.52 ?  332 ASN A ND2 1 
ATOM   2301  N N   . VAL A  1 302 ? 27.226  36.435  200.870 1.00 175.80 ?  333 VAL A N   1 
ATOM   2302  C CA  . VAL A  1 302 ? 27.159  37.037  199.537 1.00 174.44 ?  333 VAL A CA  1 
ATOM   2303  C C   . VAL A  1 302 ? 28.085  38.255  199.494 1.00 176.97 ?  333 VAL A C   1 
ATOM   2304  O O   . VAL A  1 302 ? 27.929  39.185  200.295 1.00 180.51 ?  333 VAL A O   1 
ATOM   2305  C CB  . VAL A  1 302 ? 25.725  37.422  199.138 1.00 174.46 ?  333 VAL A CB  1 
ATOM   2306  C CG1 . VAL A  1 302 ? 25.734  38.223  197.845 1.00 173.76 ?  333 VAL A CG1 1 
ATOM   2307  C CG2 . VAL A  1 302 ? 24.875  36.170  198.968 1.00 171.65 ?  333 VAL A CG2 1 
ATOM   2308  N N   . SER A  1 303 ? 29.032  38.247  198.557 1.00 178.47 ?  334 SER A N   1 
ATOM   2309  C CA  . SER A  1 303 ? 30.003  39.326  198.349 1.00 182.51 ?  334 SER A CA  1 
ATOM   2310  C C   . SER A  1 303 ? 29.336  40.675  198.051 1.00 189.60 ?  334 SER A C   1 
ATOM   2311  O O   . SER A  1 303 ? 28.616  40.807  197.056 1.00 187.42 ?  334 SER A O   1 
ATOM   2312  C CB  . SER A  1 303 ? 30.973  38.942  197.231 1.00 178.05 ?  334 SER A CB  1 
ATOM   2313  O OG  . SER A  1 303 ? 30.316  38.256  196.181 1.00 174.47 ?  334 SER A OG  1 
ATOM   2314  N N   . LYS A  1 304 ? 29.559  41.669  198.924 1.00 179.45 ?  335 LYS A N   1 
ATOM   2315  C CA  . LYS A  1 304 ? 28.935  42.987  198.767 1.00 182.26 ?  335 LYS A CA  1 
ATOM   2316  C C   . LYS A  1 304 ? 29.202  43.593  197.393 1.00 181.03 ?  335 LYS A C   1 
ATOM   2317  O O   . LYS A  1 304 ? 28.338  44.277  196.829 1.00 183.64 ?  335 LYS A O   1 
ATOM   2318  C CB  . LYS A  1 304 ? 29.458  43.976  199.816 1.00 186.88 ?  335 LYS A CB  1 
ATOM   2319  C CG  . LYS A  1 304 ? 29.495  43.547  201.269 1.00 188.75 ?  335 LYS A CG  1 
ATOM   2320  C CD  . LYS A  1 304 ? 29.992  44.715  202.138 1.00 193.60 ?  335 LYS A CD  1 
ATOM   2321  C CE  . LYS A  1 304 ? 29.335  46.049  201.768 1.00 196.46 ?  335 LYS A CE  1 
ATOM   2322  N NZ  . LYS A  1 304 ? 29.865  47.193  202.574 1.00 201.24 1  335 LYS A NZ  1 
ATOM   2323  N N   . ALA A  1 305 ? 30.389  43.349  196.835 1.00 201.36 ?  336 ALA A N   1 
ATOM   2324  C CA  . ALA A  1 305 ? 30.731  43.918  195.533 1.00 200.21 ?  336 ALA A CA  1 
ATOM   2325  C C   . ALA A  1 305 ? 29.872  43.339  194.414 1.00 196.30 ?  336 ALA A C   1 
ATOM   2326  O O   . ALA A  1 305 ? 29.393  44.083  193.549 1.00 198.77 ?  336 ALA A O   1 
ATOM   2327  C CB  . ALA A  1 305 ? 32.216  43.691  195.247 1.00 198.17 ?  336 ALA A CB  1 
ATOM   2328  N N   . THR A  1 306 ? 29.670  42.023  194.400 1.00 184.30 ?  337 THR A N   1 
ATOM   2329  C CA  . THR A  1 306 ? 28.874  41.415  193.337 1.00 180.12 ?  337 THR A CA  1 
ATOM   2330  C C   . THR A  1 306 ? 27.407  41.831  193.446 1.00 189.64 ?  337 THR A C   1 
ATOM   2331  O O   . THR A  1 306 ? 26.755  42.113  192.433 1.00 195.72 ?  337 THR A O   1 
ATOM   2332  C CB  . THR A  1 306 ? 29.017  39.891  193.376 1.00 173.65 ?  337 THR A CB  1 
ATOM   2333  O OG1 . THR A  1 306 ? 30.405  39.534  193.354 1.00 170.97 ?  337 THR A OG1 1 
ATOM   2334  C CG2 . THR A  1 306 ? 28.331  39.261  192.174 1.00 165.03 ?  337 THR A CG2 1 
ATOM   2335  N N   . TRP A  1 307 ? 26.880  41.880  194.674 1.00 164.08 ?  338 TRP A N   1 
ATOM   2336  C CA  . TRP A  1 307 ? 25.473  42.192  194.930 1.00 172.90 ?  338 TRP A CA  1 
ATOM   2337  C C   . TRP A  1 307 ? 25.120  43.649  194.614 1.00 183.80 ?  338 TRP A C   1 
ATOM   2338  O O   . TRP A  1 307 ? 23.980  43.937  194.227 1.00 192.03 ?  338 TRP A O   1 
ATOM   2339  C CB  . TRP A  1 307 ? 25.144  41.840  196.380 1.00 170.96 ?  338 TRP A CB  1 
ATOM   2340  C CG  . TRP A  1 307 ? 23.707  41.959  196.707 1.00 178.01 ?  338 TRP A CG  1 
ATOM   2341  C CD1 . TRP A  1 307 ? 23.115  42.912  197.475 1.00 184.60 ?  338 TRP A CD1 1 
ATOM   2342  C CD2 . TRP A  1 307 ? 22.661  41.083  196.273 1.00 178.51 ?  338 TRP A CD2 1 
ATOM   2343  N NE1 . TRP A  1 307 ? 21.762  42.687  197.548 1.00 188.54 ?  338 TRP A NE1 1 
ATOM   2344  C CE2 . TRP A  1 307 ? 21.458  41.569  196.817 1.00 185.38 ?  338 TRP A CE2 1 
ATOM   2345  C CE3 . TRP A  1 307 ? 22.626  39.935  195.475 1.00 173.10 ?  338 TRP A CE3 1 
ATOM   2346  C CZ2 . TRP A  1 307 ? 20.232  40.950  196.591 1.00 187.19 ?  338 TRP A CZ2 1 
ATOM   2347  C CZ3 . TRP A  1 307 ? 21.409  39.320  195.251 1.00 175.29 ?  338 TRP A CZ3 1 
ATOM   2348  C CH2 . TRP A  1 307 ? 20.228  39.829  195.807 1.00 182.62 ?  338 TRP A CH2 1 
ATOM   2349  N N   . ASN A  1 308 ? 26.076  44.568  194.760 1.00 187.36 ?  339 ASN A N   1 
ATOM   2350  C CA  . ASN A  1 308 ? 25.837  45.987  194.497 1.00 197.79 ?  339 ASN A CA  1 
ATOM   2351  C C   . ASN A  1 308 ? 25.605  46.240  193.019 1.00 204.82 ?  339 ASN A C   1 
ATOM   2352  O O   . ASN A  1 308 ? 24.735  47.031  192.634 1.00 215.08 ?  339 ASN A O   1 
ATOM   2353  C CB  . ASN A  1 308 ? 27.096  46.753  194.886 1.00 201.22 ?  339 ASN A CB  1 
ATOM   2354  C CG  . ASN A  1 308 ? 26.847  48.085  195.526 1.00 219.06 ?  339 ASN A CG  1 
ATOM   2355  O OD1 . ASN A  1 308 ? 25.734  48.462  195.894 1.00 225.63 ?  339 ASN A OD1 1 
ATOM   2356  N ND2 . ASN A  1 308 ? 27.938  48.840  195.607 1.00 234.25 ?  339 ASN A ND2 1 
ATOM   2357  N N   . GLU A  1 309 ? 26.372  45.546  192.187 1.00 214.92 ?  340 GLU A N   1 
ATOM   2358  C CA  . GLU A  1 309 ? 26.289  45.667  190.742 1.00 218.98 ?  340 GLU A CA  1 
ATOM   2359  C C   . GLU A  1 309 ? 25.040  44.984  190.207 1.00 221.02 ?  340 GLU A C   1 
ATOM   2360  O O   . GLU A  1 309 ? 24.399  45.480  189.272 1.00 230.01 ?  340 GLU A O   1 
ATOM   2361  C CB  . GLU A  1 309 ? 27.571  45.084  190.165 1.00 210.60 ?  340 GLU A CB  1 
ATOM   2362  C CG  . GLU A  1 309 ? 28.775  45.824  190.749 1.00 210.46 ?  340 GLU A CG  1 
ATOM   2363  C CD  . GLU A  1 309 ? 30.102  45.361  190.202 1.00 202.85 ?  340 GLU A CD  1 
ATOM   2364  O OE1 . GLU A  1 309 ? 30.111  44.705  189.141 1.00 197.24 ?  340 GLU A OE1 1 
ATOM   2365  O OE2 . GLU A  1 309 ? 31.136  45.641  190.850 1.00 206.06 -1 340 GLU A OE2 1 
ATOM   2366  N N   . THR A  1 310 ? 24.680  43.846  190.795 1.00 189.86 ?  341 THR A N   1 
ATOM   2367  C CA  . THR A  1 310 ? 23.514  43.103  190.339 1.00 191.22 ?  341 THR A CA  1 
ATOM   2368  C C   . THR A  1 310 ? 22.236  43.880  190.625 1.00 204.00 ?  341 THR A C   1 
ATOM   2369  O O   . THR A  1 310 ? 21.351  43.982  189.768 1.00 211.41 ?  341 THR A O   1 
ATOM   2370  C CB  . THR A  1 310 ? 23.486  41.743  191.026 1.00 182.70 ?  341 THR A CB  1 
ATOM   2371  O OG1 . THR A  1 310 ? 24.699  41.041  190.731 1.00 170.93 ?  341 THR A OG1 1 
ATOM   2372  C CG2 . THR A  1 310 ? 22.310  40.938  190.545 1.00 184.51 ?  341 THR A CG2 1 
ATOM   2373  N N   . LEU A  1 311 ? 22.127  44.436  191.832 1.00 191.55 ?  342 LEU A N   1 
ATOM   2374  C CA  . LEU A  1 311 ? 20.954  45.225  192.186 1.00 201.24 ?  342 LEU A CA  1 
ATOM   2375  C C   . LEU A  1 311 ? 20.858  46.487  191.340 1.00 210.21 ?  342 LEU A C   1 
ATOM   2376  O O   . LEU A  1 311 ? 19.759  46.885  190.936 1.00 215.44 ?  342 LEU A O   1 
ATOM   2377  C CB  . LEU A  1 311 ? 20.978  45.579  193.670 1.00 198.72 ?  342 LEU A CB  1 
ATOM   2378  C CG  . LEU A  1 311 ? 19.906  44.876  194.501 1.00 195.20 ?  342 LEU A CG  1 
ATOM   2379  C CD1 . LEU A  1 311 ? 19.872  45.437  195.912 1.00 192.46 ?  342 LEU A CD1 1 
ATOM   2380  C CD2 . LEU A  1 311 ? 18.547  45.009  193.828 1.00 196.84 ?  342 LEU A CD2 1 
ATOM   2381  N N   . GLY A  1 312 ? 21.995  47.126  191.051 1.00 205.40 ?  343 GLY A N   1 
ATOM   2382  C CA  . GLY A  1 312 ? 21.955  48.325  190.234 1.00 215.66 ?  343 GLY A CA  1 
ATOM   2383  C C   . GLY A  1 312 ? 21.619  48.047  188.788 1.00 219.29 ?  343 GLY A C   1 
ATOM   2384  O O   . GLY A  1 312 ? 21.182  48.957  188.075 1.00 230.93 ?  343 GLY A O   1 
ATOM   2385  N N   . LYS A  1 313 ? 21.810  46.810  188.338 1.00 201.22 ?  344 LYS A N   1 
ATOM   2386  C CA  . LYS A  1 313 ? 21.454  46.486  186.968 1.00 204.14 ?  344 LYS A CA  1 
ATOM   2387  C C   . LYS A  1 313 ? 19.973  46.169  186.877 1.00 213.04 ?  344 LYS A C   1 
ATOM   2388  O O   . LYS A  1 313 ? 19.372  46.320  185.809 1.00 211.87 ?  344 LYS A O   1 
ATOM   2389  C CB  . LYS A  1 313 ? 22.262  45.301  186.437 1.00 191.29 ?  344 LYS A CB  1 
ATOM   2390  C CG  . LYS A  1 313 ? 23.714  45.586  186.108 1.00 182.82 ?  344 LYS A CG  1 
ATOM   2391  C CD  . LYS A  1 313 ? 24.468  44.276  185.911 1.00 169.30 ?  344 LYS A CD  1 
ATOM   2392  C CE  . LYS A  1 313 ? 23.769  43.405  184.859 1.00 169.50 ?  344 LYS A CE  1 
ATOM   2393  N NZ  . LYS A  1 313 ? 24.418  42.079  184.639 1.00 156.52 1  344 LYS A NZ  1 
ATOM   2394  N N   . VAL A  1 314 ? 19.376  45.724  187.984 1.00 210.22 ?  345 VAL A N   1 
ATOM   2395  C CA  . VAL A  1 314 ? 17.954  45.416  187.975 1.00 197.62 ?  345 VAL A CA  1 
ATOM   2396  C C   . VAL A  1 314 ? 17.125  46.685  188.093 1.00 196.65 ?  345 VAL A C   1 
ATOM   2397  O O   . VAL A  1 314 ? 16.154  46.874  187.353 1.00 191.74 ?  345 VAL A O   1 
ATOM   2398  C CB  . VAL A  1 314 ? 17.633  44.439  189.122 1.00 190.54 ?  345 VAL A CB  1 
ATOM   2399  C CG1 . VAL A  1 314 ? 16.137  44.240  189.253 1.00 177.96 ?  345 VAL A CG1 1 
ATOM   2400  C CG2 . VAL A  1 314 ? 18.351  43.117  188.925 1.00 189.65 ?  345 VAL A CG2 1 
ATOM   2401  N N   . VAL A  1 315 ? 17.506  47.586  189.006 1.00 210.66 ?  346 VAL A N   1 
ATOM   2402  C CA  . VAL A  1 315 ? 16.720  48.803  189.192 1.00 213.23 ?  346 VAL A CA  1 
ATOM   2403  C C   . VAL A  1 315 ? 16.750  49.672  187.939 1.00 223.21 ?  346 VAL A C   1 
ATOM   2404  O O   . VAL A  1 315 ? 15.794  50.408  187.662 1.00 220.87 ?  346 VAL A O   1 
ATOM   2405  C CB  . VAL A  1 315 ? 17.214  49.568  190.439 1.00 219.23 ?  346 VAL A CB  1 
ATOM   2406  C CG1 . VAL A  1 315 ? 18.626  50.076  190.234 1.00 231.56 ?  346 VAL A CG1 1 
ATOM   2407  C CG2 . VAL A  1 315 ? 16.282  50.717  190.777 1.00 216.67 ?  346 VAL A CG2 1 
ATOM   2408  N N   . LYS A  1 316 ? 17.831  49.592  187.153 1.00 204.97 ?  347 LYS A N   1 
ATOM   2409  C CA  . LYS A  1 316 ? 17.894  50.343  185.903 1.00 210.51 ?  347 LYS A CA  1 
ATOM   2410  C C   . LYS A  1 316 ? 16.962  49.754  184.856 1.00 202.41 ?  347 LYS A C   1 
ATOM   2411  O O   . LYS A  1 316 ? 16.553  50.468  183.938 1.00 202.44 ?  347 LYS A O   1 
ATOM   2412  C CB  . LYS A  1 316 ? 19.333  50.443  185.394 1.00 221.30 ?  347 LYS A CB  1 
ATOM   2413  C CG  . LYS A  1 316 ? 19.737  51.883  185.055 1.00 228.39 ?  347 LYS A CG  1 
ATOM   2414  C CD  . LYS A  1 316 ? 20.417  52.575  186.234 1.00 229.49 ?  347 LYS A CD  1 
ATOM   2415  C CE  . LYS A  1 316 ? 20.770  54.022  185.909 1.00 233.51 ?  347 LYS A CE  1 
ATOM   2416  N NZ  . LYS A  1 316 ? 21.768  54.597  186.855 1.00 230.56 1  347 LYS A NZ  1 
ATOM   2417  N N   . GLN A  1 317 ? 16.605  48.474  184.994 1.00 207.54 ?  348 GLN A N   1 
ATOM   2418  C CA  . GLN A  1 317 ? 15.672  47.802  184.103 1.00 197.14 ?  348 GLN A CA  1 
ATOM   2419  C C   . GLN A  1 317 ? 14.254  47.974  184.598 1.00 186.54 ?  348 GLN A C   1 
ATOM   2420  O O   . GLN A  1 317 ? 13.304  47.880  183.811 1.00 176.95 ?  348 GLN A O   1 
ATOM   2421  C CB  . GLN A  1 317 ? 15.975  46.305  184.030 1.00 191.80 ?  348 GLN A CB  1 
ATOM   2422  C CG  . GLN A  1 317 ? 17.317  45.902  183.454 1.00 199.68 ?  348 GLN A CG  1 
ATOM   2423  C CD  . GLN A  1 317 ? 17.456  46.149  181.966 1.00 198.89 ?  348 GLN A CD  1 
ATOM   2424  O OE1 . GLN A  1 317 ? 17.024  47.172  181.437 1.00 200.94 ?  348 GLN A OE1 1 
ATOM   2425  N NE2 . GLN A  1 317 ? 18.046  45.184  181.275 1.00 194.59 ?  348 GLN A NE2 1 
ATOM   2426  N N   . LEU A  1 318 ? 14.111  48.223  185.897 1.00 197.47 ?  349 LEU A N   1 
ATOM   2427  C CA  . LEU A  1 318 ? 12.806  48.430  186.499 1.00 185.56 ?  349 LEU A CA  1 
ATOM   2428  C C   . LEU A  1 318 ? 12.282  49.805  186.131 1.00 187.28 ?  349 LEU A C   1 
ATOM   2429  O O   . LEU A  1 318 ? 11.061  50.012  186.071 1.00 176.95 ?  349 LEU A O   1 
ATOM   2430  C CB  . LEU A  1 318 ? 12.897  48.272  188.016 1.00 183.82 ?  349 LEU A CB  1 
ATOM   2431  C CG  . LEU A  1 318 ? 13.327  46.900  188.541 1.00 183.34 ?  349 LEU A CG  1 
ATOM   2432  C CD1 . LEU A  1 318 ? 13.327  46.867  190.060 1.00 182.36 ?  349 LEU A CD1 1 
ATOM   2433  C CD2 . LEU A  1 318 ? 12.459  45.798  187.975 1.00 172.20 ?  349 LEU A CD2 1 
ATOM   2434  N N   . ARG A  1 319 ? 13.192  50.755  185.871 1.00 195.64 ?  350 ARG A N   1 
ATOM   2435  C CA  . ARG A  1 319 ? 12.789  52.113  185.477 1.00 197.80 ?  350 ARG A CA  1 
ATOM   2436  C C   . ARG A  1 319 ? 12.271  52.162  184.053 1.00 194.93 ?  350 ARG A C   1 
ATOM   2437  O O   . ARG A  1 319 ? 11.680  53.176  183.681 1.00 200.48 ?  350 ARG A O   1 
ATOM   2438  C CB  . ARG A  1 319 ? 13.944  53.113  185.607 1.00 212.63 ?  350 ARG A CB  1 
ATOM   2439  C CG  . ARG A  1 319 ? 14.457  53.369  187.006 1.00 218.63 ?  350 ARG A CG  1 
ATOM   2440  C CD  . ARG A  1 319 ? 15.476  54.502  187.024 1.00 234.12 ?  350 ARG A CD  1 
ATOM   2441  N NE  . ARG A  1 319 ? 16.000  54.748  188.362 1.00 236.27 ?  350 ARG A NE  1 
ATOM   2442  C CZ  . ARG A  1 319 ? 17.221  54.356  188.713 1.00 243.62 ?  350 ARG A CZ  1 
ATOM   2443  N NH1 . ARG A  1 319 ? 17.973  53.728  187.819 1.00 254.66 1  350 ARG A NH1 1 
ATOM   2444  N NH2 . ARG A  1 319 ? 17.704  54.596  189.916 1.00 243.03 ?  350 ARG A NH2 1 
ATOM   2445  N N   . LYS A  1 320 ? 12.469  51.102  183.268 1.00 213.39 ?  351 LYS A N   1 
ATOM   2446  C CA  . LYS A  1 320 ? 11.940  51.071  181.909 1.00 205.13 ?  351 LYS A CA  1 
ATOM   2447  C C   . LYS A  1 320 ? 10.455  50.774  181.918 1.00 191.13 ?  351 LYS A C   1 
ATOM   2448  O O   . LYS A  1 320 ? 9.814   50.853  180.865 1.00 182.10 ?  351 LYS A O   1 
ATOM   2449  C CB  . LYS A  1 320 ? 12.545  49.957  181.030 1.00 202.24 ?  351 LYS A CB  1 
ATOM   2450  C CG  . LYS A  1 320 ? 13.990  49.957  180.531 1.00 213.70 ?  351 LYS A CG  1 
ATOM   2451  C CD  . LYS A  1 320 ? 15.043  50.632  181.357 1.00 230.93 ?  351 LYS A CD  1 
ATOM   2452  C CE  . LYS A  1 320 ? 16.410  50.327  180.721 1.00 240.63 ?  351 LYS A CE  1 
ATOM   2453  N NZ  . LYS A  1 320 ? 17.541  51.179  181.185 1.00 256.40 1  351 LYS A NZ  1 
ATOM   2454  N N   . HIS A  1 321 ? 9.909   50.445  183.086 1.00 199.28 ?  352 HIS A N   1 
ATOM   2455  C CA  . HIS A  1 321 ? 8.512   50.094  183.230 1.00 200.24 ?  352 HIS A CA  1 
ATOM   2456  C C   . HIS A  1 321 ? 7.786   50.961  184.243 1.00 205.35 ?  352 HIS A C   1 
ATOM   2457  O O   . HIS A  1 321 ? 6.557   51.055  184.181 1.00 207.89 ?  352 HIS A O   1 
ATOM   2458  C CB  . HIS A  1 321 ? 8.410   48.635  183.700 1.00 195.24 ?  352 HIS A CB  1 
ATOM   2459  C CG  . HIS A  1 321 ? 9.088   47.663  182.784 1.00 190.26 ?  352 HIS A CG  1 
ATOM   2460  N ND1 . HIS A  1 321 ? 10.454  47.472  182.801 1.00 187.56 ?  352 HIS A ND1 1 
ATOM   2461  C CD2 . HIS A  1 321 ? 8.606   46.836  181.827 1.00 187.77 ?  352 HIS A CD2 1 
ATOM   2462  C CE1 . HIS A  1 321 ? 10.783  46.566  181.899 1.00 183.67 ?  352 HIS A CE1 1 
ATOM   2463  N NE2 . HIS A  1 321 ? 9.680   46.164  181.293 1.00 183.68 ?  352 HIS A NE2 1 
ATOM   2464  N N   . PHE A  1 322 ? 8.514   51.592  185.168 1.00 203.30 ?  353 PHE A N   1 
ATOM   2465  C CA  . PHE A  1 322 ? 7.956   52.410  186.241 1.00 212.66 ?  353 PHE A CA  1 
ATOM   2466  C C   . PHE A  1 322 ? 8.410   53.867  186.160 1.00 222.89 ?  353 PHE A C   1 
ATOM   2467  O O   . PHE A  1 322 ? 8.483   54.559  187.178 1.00 231.51 ?  353 PHE A O   1 
ATOM   2468  C CB  . PHE A  1 322 ? 8.297   51.788  187.593 1.00 210.06 ?  353 PHE A CB  1 
ATOM   2469  C CG  . PHE A  1 322 ? 7.614   50.469  187.822 1.00 206.24 ?  353 PHE A CG  1 
ATOM   2470  C CD1 . PHE A  1 322 ? 6.353   50.418  188.389 1.00 212.30 ?  353 PHE A CD1 1 
ATOM   2471  C CD2 . PHE A  1 322 ? 8.193   49.286  187.386 1.00 196.83 ?  353 PHE A CD2 1 
ATOM   2472  C CE1 . PHE A  1 322 ? 5.702   49.212  188.572 1.00 206.68 ?  353 PHE A CE1 1 
ATOM   2473  C CE2 . PHE A  1 322 ? 7.542   48.078  187.560 1.00 193.80 ?  353 PHE A CE2 1 
ATOM   2474  C CZ  . PHE A  1 322 ? 6.298   48.041  188.154 1.00 197.56 ?  353 PHE A CZ  1 
ATOM   2475  N N   . GLY A  1 323 ? 8.718   54.344  184.957 1.00 215.53 ?  354 GLY A N   1 
ATOM   2476  C CA  . GLY A  1 323 ? 9.178   55.710  184.782 1.00 224.98 ?  354 GLY A CA  1 
ATOM   2477  C C   . GLY A  1 323 ? 10.685  55.866  184.814 1.00 228.26 ?  354 GLY A C   1 
ATOM   2478  O O   . GLY A  1 323 ? 11.363  55.239  185.633 1.00 222.69 ?  354 GLY A O   1 
ATOM   2479  N N   . ASN A  1 324 ? 11.216  56.713  183.929 1.00 232.64 ?  355 ASN A N   1 
ATOM   2480  C CA  . ASN A  1 324 ? 12.663  56.887  183.829 1.00 233.78 ?  355 ASN A CA  1 
ATOM   2481  C C   . ASN A  1 324 ? 13.256  57.494  185.092 1.00 236.94 ?  355 ASN A C   1 
ATOM   2482  O O   . ASN A  1 324 ? 14.301  57.045  185.578 1.00 231.86 ?  355 ASN A O   1 
ATOM   2483  C CB  . ASN A  1 324 ? 13.003  57.781  182.636 1.00 238.33 ?  355 ASN A CB  1 
ATOM   2484  C CG  . ASN A  1 324 ? 14.227  57.314  181.894 1.00 242.77 ?  355 ASN A CG  1 
ATOM   2485  O OD1 . ASN A  1 324 ? 15.352  57.550  182.333 1.00 245.44 ?  355 ASN A OD1 1 
ATOM   2486  N ND2 . ASN A  1 324 ? 14.024  56.667  180.760 1.00 254.44 ?  355 ASN A ND2 1 
ATOM   2487  N N   . ASN A  1 325 ? 12.607  58.519  185.631 1.00 223.35 ?  356 ASN A N   1 
ATOM   2488  C CA  . ASN A  1 325 ? 13.072  59.223  186.817 1.00 224.77 ?  356 ASN A CA  1 
ATOM   2489  C C   . ASN A  1 325 ? 12.181  58.872  188.007 1.00 221.81 ?  356 ASN A C   1 
ATOM   2490  O O   . ASN A  1 325 ? 11.342  59.667  188.432 1.00 229.09 ?  356 ASN A O   1 
ATOM   2491  C CB  . ASN A  1 325 ? 13.092  60.733  186.531 1.00 234.60 ?  356 ASN A CB  1 
ATOM   2492  C CG  . ASN A  1 325 ? 14.029  61.095  185.388 1.00 235.76 ?  356 ASN A CG  1 
ATOM   2493  O OD1 . ASN A  1 325 ? 13.702  61.927  184.540 1.00 241.25 ?  356 ASN A OD1 1 
ATOM   2494  N ND2 . ASN A  1 325 ? 15.194  60.457  185.352 1.00 230.03 ?  356 ASN A ND2 1 
ATOM   2495  N N   . THR A  1 326 ? 12.354  57.665  188.542 1.00 222.56 ?  357 THR A N   1 
ATOM   2496  C CA  . THR A  1 326 ? 11.557  57.243  189.682 1.00 221.64 ?  357 THR A CA  1 
ATOM   2497  C C   . THR A  1 326 ? 12.460  56.634  190.743 1.00 217.78 ?  357 THR A C   1 
ATOM   2498  O O   . THR A  1 326 ? 13.589  56.218  190.466 1.00 215.56 ?  357 THR A O   1 
ATOM   2499  C CB  . THR A  1 326 ? 10.500  56.212  189.257 1.00 216.10 ?  357 THR A CB  1 
ATOM   2500  O OG1 . THR A  1 326 ? 9.621   55.930  190.352 1.00 217.98 ?  357 THR A OG1 1 
ATOM   2501  C CG2 . THR A  1 326 ? 11.178  54.925  188.822 1.00 205.47 ?  357 THR A CG2 1 
ATOM   2502  N N   . ILE A  1 327 ? 11.948  56.594  191.973 1.00 228.26 ?  358 ILE A N   1 
ATOM   2503  C CA  . ILE A  1 327 ? 12.676  56.044  193.109 1.00 226.32 ?  358 ILE A CA  1 
ATOM   2504  C C   . ILE A  1 327 ? 12.166  54.635  193.375 1.00 220.88 ?  358 ILE A C   1 
ATOM   2505  O O   . ILE A  1 327 ? 10.961  54.427  193.569 1.00 222.23 ?  358 ILE A O   1 
ATOM   2506  C CB  . ILE A  1 327 ? 12.527  56.941  194.346 1.00 227.53 ?  358 ILE A CB  1 
ATOM   2507  C CG1 . ILE A  1 327 ? 13.053  58.342  194.025 1.00 229.47 ?  358 ILE A CG1 1 
ATOM   2508  C CG2 . ILE A  1 327 ? 13.275  56.343  195.523 1.00 220.30 ?  358 ILE A CG2 1 
ATOM   2509  C CD1 . ILE A  1 327 ? 12.994  59.305  195.183 1.00 238.36 ?  358 ILE A CD1 1 
ATOM   2510  N N   . ILE A  1 328 ? 13.080  53.672  193.383 1.00 222.84 ?  359 ILE A N   1 
ATOM   2511  C CA  . ILE A  1 328 ? 12.781  52.269  193.643 1.00 211.87 ?  359 ILE A CA  1 
ATOM   2512  C C   . ILE A  1 328 ? 13.412  51.857  194.969 1.00 206.48 ?  359 ILE A C   1 
ATOM   2513  O O   . ILE A  1 328 ? 14.635  51.951  195.134 1.00 202.43 ?  359 ILE A O   1 
ATOM   2514  C CB  . ILE A  1 328 ? 13.234  51.389  192.474 1.00 205.31 ?  359 ILE A CB  1 
ATOM   2515  C CG1 . ILE A  1 328 ? 12.493  51.859  191.219 1.00 208.25 ?  359 ILE A CG1 1 
ATOM   2516  C CG2 . ILE A  1 328 ? 12.936  49.932  192.760 1.00 197.28 ?  359 ILE A CG2 1 
ATOM   2517  C CD1 . ILE A  1 328 ? 12.842  51.132  189.968 1.00 195.40 ?  359 ILE A CD1 1 
ATOM   2518  N N   . ARG A  1 329 ? 12.588  51.396  195.910 1.00 202.16 ?  360 ARG A N   1 
ATOM   2519  C CA  . ARG A  1 329 ? 13.048  50.988  197.232 1.00 203.50 ?  360 ARG A CA  1 
ATOM   2520  C C   . ARG A  1 329 ? 12.812  49.494  197.406 1.00 197.33 ?  360 ARG A C   1 
ATOM   2521  O O   . ARG A  1 329 ? 11.758  48.971  197.026 1.00 196.18 ?  360 ARG A O   1 
ATOM   2522  C CB  . ARG A  1 329 ? 12.320  51.746  198.346 1.00 211.47 ?  360 ARG A CB  1 
ATOM   2523  C CG  . ARG A  1 329 ? 12.869  51.450  199.742 1.00 214.33 ?  360 ARG A CG  1 
ATOM   2524  C CD  . ARG A  1 329 ? 11.879  50.708  200.630 1.00 212.79 ?  360 ARG A CD  1 
ATOM   2525  N NE  . ARG A  1 329 ? 10.660  51.463  200.894 1.00 220.93 ?  360 ARG A NE  1 
ATOM   2526  C CZ  . ARG A  1 329 ? 9.895   51.289  201.967 1.00 225.54 ?  360 ARG A CZ  1 
ATOM   2527  N NH1 . ARG A  1 329 ? 10.222  50.386  202.883 1.00 218.18 1  360 ARG A NH1 1 
ATOM   2528  N NH2 . ARG A  1 329 ? 8.800   52.020  202.125 1.00 236.62 ?  360 ARG A NH2 1 
ATOM   2529  N N   . PHE A  1 330 ? 13.800  48.810  197.978 1.00 216.04 ?  361 PHE A N   1 
ATOM   2530  C CA  . PHE A  1 330 ? 13.719  47.382  198.243 1.00 211.99 ?  361 PHE A CA  1 
ATOM   2531  C C   . PHE A  1 330 ? 13.491  47.131  199.726 1.00 214.39 ?  361 PHE A C   1 
ATOM   2532  O O   . PHE A  1 330 ? 14.196  47.693  200.572 1.00 218.10 ?  361 PHE A O   1 
ATOM   2533  C CB  . PHE A  1 330 ? 15.009  46.706  197.782 1.00 207.13 ?  361 PHE A CB  1 
ATOM   2534  C CG  . PHE A  1 330 ? 15.219  46.791  196.304 1.00 204.38 ?  361 PHE A CG  1 
ATOM   2535  C CD1 . PHE A  1 330 ? 14.580  45.913  195.448 1.00 201.00 ?  361 PHE A CD1 1 
ATOM   2536  C CD2 . PHE A  1 330 ? 16.031  47.779  195.767 1.00 205.44 ?  361 PHE A CD2 1 
ATOM   2537  C CE1 . PHE A  1 330 ? 14.763  46.005  194.083 1.00 198.63 ?  361 PHE A CE1 1 
ATOM   2538  C CE2 . PHE A  1 330 ? 16.219  47.877  194.403 1.00 203.07 ?  361 PHE A CE2 1 
ATOM   2539  C CZ  . PHE A  1 330 ? 15.583  46.988  193.559 1.00 199.65 ?  361 PHE A CZ  1 
ATOM   2540  N N   . ALA A  1 331 ? 12.515  46.280  200.035 1.00 195.98 ?  362 ALA A N   1 
ATOM   2541  C CA  . ALA A  1 331 ? 12.209  45.928  201.410 1.00 198.07 ?  362 ALA A CA  1 
ATOM   2542  C C   . ALA A  1 331 ? 11.976  44.427  201.490 1.00 193.94 ?  362 ALA A C   1 
ATOM   2543  O O   . ALA A  1 331 ? 11.597  43.783  200.511 1.00 190.72 ?  362 ALA A O   1 
ATOM   2544  C CB  . ALA A  1 331 ? 10.986  46.695  201.932 1.00 203.64 ?  362 ALA A CB  1 
ATOM   2545  N N   . ASN A  1 332 ? 12.202  43.883  202.681 1.00 198.30 ?  363 ASN A N   1 
ATOM   2546  C CA  . ASN A  1 332 ? 12.050  42.460  202.949 1.00 194.88 ?  363 ASN A CA  1 
ATOM   2547  C C   . ASN A  1 332 ? 10.566  42.057  202.959 1.00 195.92 ?  363 ASN A C   1 
ATOM   2548  O O   . ASN A  1 332 ? 9.666   42.883  202.784 1.00 199.48 ?  363 ASN A O   1 
ATOM   2549  C CB  . ASN A  1 332 ? 12.873  42.112  204.187 1.00 195.20 ?  363 ASN A CB  1 
ATOM   2550  C CG  . ASN A  1 332 ? 12.530  42.958  205.379 1.00 200.72 ?  363 ASN A CG  1 
ATOM   2551  O OD1 . ASN A  1 332 ? 11.428  43.495  205.500 1.00 202.14 ?  363 ASN A OD1 1 
ATOM   2552  N ND2 . ASN A  1 332 ? 13.541  43.203  206.203 1.00 204.03 ?  363 ASN A ND2 1 
ATOM   2553  N N   . SER A  1 333 ? 10.315  40.762  203.178 1.00 187.15 ?  364 SER A N   1 
ATOM   2554  C CA  . SER A  1 333 ? 8.968   40.193  203.115 1.00 187.63 ?  364 SER A CA  1 
ATOM   2555  C C   . SER A  1 333 ? 7.990   40.792  204.127 1.00 193.96 ?  364 SER A C   1 
ATOM   2556  O O   . SER A  1 333 ? 8.366   41.327  205.174 1.00 196.31 ?  364 SER A O   1 
ATOM   2557  C CB  . SER A  1 333 ? 9.032   38.680  203.332 1.00 184.91 ?  364 SER A CB  1 
ATOM   2558  O OG  . SER A  1 333 ? 7.740   38.103  203.258 1.00 188.39 ?  364 SER A OG  1 
ATOM   2559  N N   . SER A  1 334 ? 6.698   40.688  203.771 1.00 187.70 ?  365 SER A N   1 
ATOM   2560  C CA  . SER A  1 334 ? 5.594   41.195  204.584 1.00 194.86 ?  365 SER A CA  1 
ATOM   2561  C C   . SER A  1 334 ? 5.265   40.286  205.767 1.00 197.88 ?  365 SER A C   1 
ATOM   2562  O O   . SER A  1 334 ? 5.026   40.772  206.878 1.00 202.68 ?  365 SER A O   1 
ATOM   2563  C CB  . SER A  1 334 ? 4.352   41.384  203.703 1.00 197.58 ?  365 SER A CB  1 
ATOM   2564  O OG  . SER A  1 334 ? 4.590   42.310  202.652 1.00 195.38 ?  365 SER A OG  1 
ATOM   2565  N N   . GLY A  1 335 ? 5.266   38.972  205.558 1.00 190.00 ?  366 GLY A N   1 
ATOM   2566  C CA  . GLY A  1 335 ? 4.970   38.047  206.634 1.00 192.40 ?  366 GLY A CA  1 
ATOM   2567  C C   . GLY A  1 335 ? 4.211   36.816  206.185 1.00 191.65 ?  366 GLY A C   1 
ATOM   2568  O O   . GLY A  1 335 ? 3.797   36.710  205.027 1.00 189.72 ?  366 GLY A O   1 
ATOM   2569  N N   . GLY A  1 336 ? 4.021   35.879  207.114 1.00 197.83 ?  367 GLY A N   1 
ATOM   2570  C CA  . GLY A  1 336 ? 3.304   34.648  206.854 1.00 197.23 ?  367 GLY A CA  1 
ATOM   2571  C C   . GLY A  1 336 ? 4.066   33.415  207.296 1.00 193.83 ?  367 GLY A C   1 
ATOM   2572  O O   . GLY A  1 336 ? 4.645   33.374  208.387 1.00 194.83 ?  367 GLY A O   1 
ATOM   2573  N N   . ASP A  1 337 ? 4.052   32.392  206.450 1.00 185.70 ?  368 ASP A N   1 
ATOM   2574  C CA  . ASP A  1 337 ? 4.739   31.148  206.748 1.00 182.34 ?  368 ASP A CA  1 
ATOM   2575  C C   . ASP A  1 337 ? 6.250   31.352  206.691 1.00 178.04 ?  368 ASP A C   1 
ATOM   2576  O O   . ASP A  1 337 ? 6.759   32.321  206.117 1.00 176.40 ?  368 ASP A O   1 
ATOM   2577  C CB  . ASP A  1 337 ? 4.314   30.029  205.794 1.00 179.14 ?  368 ASP A CB  1 
ATOM   2578  C CG  . ASP A  1 337 ? 2.809   29.795  205.790 1.00 183.10 ?  368 ASP A CG  1 
ATOM   2579  O OD1 . ASP A  1 337 ? 2.052   30.756  206.035 1.00 187.85 ?  368 ASP A OD1 1 
ATOM   2580  O OD2 . ASP A  1 337 ? 2.384   28.643  205.550 1.00 181.56 -1 368 ASP A OD2 1 
ATOM   2581  N N   . LEU A  1 338 ? 6.972   30.406  207.287 1.00 176.12 ?  369 LEU A N   1 
ATOM   2582  C CA  . LEU A  1 338 ? 8.425   30.489  207.307 1.00 173.57 ?  369 LEU A CA  1 
ATOM   2583  C C   . LEU A  1 338 ? 8.997   30.238  205.922 1.00 166.39 ?  369 LEU A C   1 
ATOM   2584  O O   . LEU A  1 338 ? 10.079  30.737  205.596 1.00 162.31 ?  369 LEU A O   1 
ATOM   2585  C CB  . LEU A  1 338 ? 8.999   29.478  208.298 1.00 169.67 ?  369 LEU A CB  1 
ATOM   2586  C CG  . LEU A  1 338 ? 10.496  29.580  208.604 1.00 168.90 ?  369 LEU A CG  1 
ATOM   2587  C CD1 . LEU A  1 338 ? 10.828  30.897  209.293 1.00 180.82 ?  369 LEU A CD1 1 
ATOM   2588  C CD2 . LEU A  1 338 ? 10.978  28.385  209.420 1.00 163.86 ?  369 LEU A CD2 1 
ATOM   2589  N N   . GLU A  1 339 ? 8.282   29.476  205.098 1.00 181.27 ?  370 GLU A N   1 
ATOM   2590  C CA  . GLU A  1 339 ? 8.734   29.157  203.752 1.00 179.68 ?  370 GLU A CA  1 
ATOM   2591  C C   . GLU A  1 339 ? 8.600   30.336  202.797 1.00 182.15 ?  370 GLU A C   1 
ATOM   2592  O O   . GLU A  1 339 ? 9.174   30.294  201.704 1.00 177.73 ?  370 GLU A O   1 
ATOM   2593  C CB  . GLU A  1 339 ? 7.936   27.963  203.232 1.00 174.99 ?  370 GLU A CB  1 
ATOM   2594  C CG  . GLU A  1 339 ? 8.296   26.650  203.910 1.00 170.96 ?  370 GLU A CG  1 
ATOM   2595  C CD  . GLU A  1 339 ? 7.190   26.145  204.822 1.00 172.44 ?  370 GLU A CD  1 
ATOM   2596  O OE1 . GLU A  1 339 ? 6.078   26.712  204.780 1.00 174.76 ?  370 GLU A OE1 1 
ATOM   2597  O OE2 . GLU A  1 339 ? 7.432   25.185  205.585 1.00 173.04 -1 370 GLU A OE2 1 
ATOM   2598  N N   . VAL A  1 340 ? 7.863   31.375  203.176 1.00 176.75 ?  371 VAL A N   1 
ATOM   2599  C CA  . VAL A  1 340 ? 7.640   32.534  202.322 1.00 178.92 ?  371 VAL A CA  1 
ATOM   2600  C C   . VAL A  1 340 ? 8.517   33.709  202.738 1.00 182.06 ?  371 VAL A C   1 
ATOM   2601  O O   . VAL A  1 340 ? 8.991   34.466  201.890 1.00 179.71 ?  371 VAL A O   1 
ATOM   2602  C CB  . VAL A  1 340 ? 6.148   32.929  202.326 1.00 182.62 ?  371 VAL A CB  1 
ATOM   2603  C CG1 . VAL A  1 340 ? 5.882   34.043  201.316 1.00 181.21 ?  371 VAL A CG1 1 
ATOM   2604  C CG2 . VAL A  1 340 ? 5.283   31.717  202.030 1.00 176.46 ?  371 VAL A CG2 1 
ATOM   2605  N N   . THR A  1 341 ? 8.744   33.869  204.041 1.00 181.84 ?  372 THR A N   1 
ATOM   2606  C CA  . THR A  1 341 ? 9.513   34.992  204.561 1.00 182.81 ?  372 THR A CA  1 
ATOM   2607  C C   . THR A  1 341 ? 11.021  34.767  204.526 1.00 174.70 ?  372 THR A C   1 
ATOM   2608  O O   . THR A  1 341 ? 11.774  35.737  204.678 1.00 173.65 ?  372 THR A O   1 
ATOM   2609  C CB  . THR A  1 341 ? 9.089   35.288  206.004 1.00 191.85 ?  372 THR A CB  1 
ATOM   2610  O OG1 . THR A  1 341 ? 9.320   34.133  206.820 1.00 188.28 ?  372 THR A OG1 1 
ATOM   2611  C CG2 . THR A  1 341 ? 7.611   35.635  206.061 1.00 198.59 ?  372 THR A CG2 1 
ATOM   2612  N N   . THR A  1 342 ? 11.479  33.532  204.330 1.00 172.91 ?  373 THR A N   1 
ATOM   2613  C CA  . THR A  1 342 ? 12.896  33.199  204.333 1.00 169.10 ?  373 THR A CA  1 
ATOM   2614  C C   . THR A  1 342 ? 13.299  32.504  203.037 1.00 163.01 ?  373 THR A C   1 
ATOM   2615  O O   . THR A  1 342 ? 12.463  31.996  202.286 1.00 160.66 ?  373 THR A O   1 
ATOM   2616  C CB  . THR A  1 342 ? 13.252  32.301  205.527 1.00 167.76 ?  373 THR A CB  1 
ATOM   2617  O OG1 . THR A  1 342 ? 12.504  31.081  205.448 1.00 163.08 ?  373 THR A OG1 1 
ATOM   2618  C CG2 . THR A  1 342 ? 12.948  33.007  206.848 1.00 173.74 ?  373 THR A CG2 1 
ATOM   2619  N N   . HIS A  1 343 ? 14.606  32.503  202.782 1.00 163.51 ?  374 HIS A N   1 
ATOM   2620  C CA  . HIS A  1 343 ? 15.200  31.835  201.625 1.00 154.71 ?  374 HIS A CA  1 
ATOM   2621  C C   . HIS A  1 343 ? 15.300  30.344  201.918 1.00 150.23 ?  374 HIS A C   1 
ATOM   2622  O O   . HIS A  1 343 ? 16.277  29.861  202.492 1.00 148.67 ?  374 HIS A O   1 
ATOM   2623  C CB  . HIS A  1 343 ? 16.566  32.422  201.303 1.00 153.02 ?  374 HIS A CB  1 
ATOM   2624  C CG  . HIS A  1 343 ? 17.319  31.644  200.273 1.00 146.78 ?  374 HIS A CG  1 
ATOM   2625  N ND1 . HIS A  1 343 ? 16.720  31.133  199.142 1.00 143.65 ?  374 HIS A ND1 1 
ATOM   2626  C CD2 . HIS A  1 343 ? 18.618  31.266  200.214 1.00 143.10 ?  374 HIS A CD2 1 
ATOM   2627  C CE1 . HIS A  1 343 ? 17.621  30.485  198.425 1.00 138.32 ?  374 HIS A CE1 1 
ATOM   2628  N NE2 . HIS A  1 343 ? 18.781  30.551  199.054 1.00 137.87 ?  374 HIS A NE2 1 
ATOM   2629  N N   . SER A  1 344 ? 14.265  29.608  201.530 1.00 159.29 ?  375 SER A N   1 
ATOM   2630  C CA  . SER A  1 344 ? 14.215  28.173  201.769 1.00 153.93 ?  375 SER A CA  1 
ATOM   2631  C C   . SER A  1 344 ? 15.002  27.431  200.696 1.00 148.03 ?  375 SER A C   1 
ATOM   2632  O O   . SER A  1 344 ? 14.824  27.685  199.501 1.00 147.01 ?  375 SER A O   1 
ATOM   2633  C CB  . SER A  1 344 ? 12.763  27.692  201.781 1.00 153.28 ?  375 SER A CB  1 
ATOM   2634  O OG  . SER A  1 344 ? 11.962  28.480  202.647 1.00 158.50 ?  375 SER A OG  1 
ATOM   2635  N N   . PHE A  1 345 ? 15.873  26.515  201.117 1.00 145.80 ?  376 PHE A N   1 
ATOM   2636  C CA  . PHE A  1 345 ? 16.621  25.700  200.168 1.00 142.50 ?  376 PHE A CA  1 
ATOM   2637  C C   . PHE A  1 345 ? 17.184  24.478  200.881 1.00 141.89 ?  376 PHE A C   1 
ATOM   2638  O O   . PHE A  1 345 ? 17.064  24.328  202.099 1.00 143.92 ?  376 PHE A O   1 
ATOM   2639  C CB  . PHE A  1 345 ? 17.729  26.515  199.475 1.00 141.74 ?  376 PHE A CB  1 
ATOM   2640  C CG  . PHE A  1 345 ? 18.876  26.893  200.374 1.00 143.30 ?  376 PHE A CG  1 
ATOM   2641  C CD1 . PHE A  1 345 ? 18.798  28.023  201.168 1.00 147.22 ?  376 PHE A CD1 1 
ATOM   2642  C CD2 . PHE A  1 345 ? 20.036  26.134  200.411 1.00 141.95 ?  376 PHE A CD2 1 
ATOM   2643  C CE1 . PHE A  1 345 ? 19.845  28.386  201.990 1.00 149.00 ?  376 PHE A CE1 1 
ATOM   2644  C CE2 . PHE A  1 345 ? 21.088  26.491  201.236 1.00 143.60 ?  376 PHE A CE2 1 
ATOM   2645  C CZ  . PHE A  1 345 ? 20.991  27.618  202.025 1.00 146.57 ?  376 PHE A CZ  1 
ATOM   2646  N N   . ASN A  1 346 ? 17.788  23.595  200.087 1.00 142.16 ?  377 ASN A N   1 
ATOM   2647  C CA  . ASN A  1 346 ? 18.387  22.349  200.551 1.00 141.43 ?  377 ASN A CA  1 
ATOM   2648  C C   . ASN A  1 346 ? 19.868  22.330  200.227 1.00 140.44 ?  377 ASN A C   1 
ATOM   2649  O O   . ASN A  1 346 ? 20.271  22.659  199.108 1.00 140.50 ?  377 ASN A O   1 
ATOM   2650  C CB  . ASN A  1 346 ? 17.728  21.117  199.924 1.00 139.44 ?  377 ASN A CB  1 
ATOM   2651  C CG  . ASN A  1 346 ? 18.089  19.828  200.654 1.00 139.47 ?  377 ASN A CG  1 
ATOM   2652  O OD1 . ASN A  1 346 ? 19.197  19.682  201.175 1.00 139.98 ?  377 ASN A OD1 1 
ATOM   2653  N ND2 . ASN A  1 346 ? 17.161  18.882  200.679 1.00 139.32 ?  377 ASN A ND2 1 
ATOM   2654  N N   . CYS A  1 347 ? 20.668  21.933  201.206 1.00 150.09 ?  378 CYS A N   1 
ATOM   2655  C CA  . CYS A  1 347 ? 22.108  21.833  201.020 1.00 149.60 ?  378 CYS A CA  1 
ATOM   2656  C C   . CYS A  1 347 ? 22.683  20.749  201.921 1.00 150.35 ?  378 CYS A C   1 
ATOM   2657  O O   . CYS A  1 347 ? 22.756  20.912  203.143 1.00 152.64 ?  378 CYS A O   1 
ATOM   2658  C CB  . CYS A  1 347 ? 22.777  23.185  201.221 1.00 151.58 ?  378 CYS A CB  1 
ATOM   2659  S SG  . CYS A  1 347 ? 24.495  22.993  200.976 1.00 176.00 ?  378 CYS A SG  1 
ATOM   2660  N N   . GLY A  1 348 ? 23.075  19.635  201.297 1.00 153.82 ?  379 GLY A N   1 
ATOM   2661  C CA  . GLY A  1 348 ? 23.657  18.511  201.996 1.00 154.61 ?  379 GLY A CA  1 
ATOM   2662  C C   . GLY A  1 348 ? 22.640  17.626  202.672 1.00 152.73 ?  379 GLY A C   1 
ATOM   2663  O O   . GLY A  1 348 ? 23.020  16.780  203.489 1.00 153.57 ?  379 GLY A O   1 
ATOM   2664  N N   . GLY A  1 349 ? 21.360  17.790  202.349 1.00 144.36 ?  380 GLY A N   1 
ATOM   2665  C CA  . GLY A  1 349 ? 20.285  17.016  202.922 1.00 144.94 ?  380 GLY A CA  1 
ATOM   2666  C C   . GLY A  1 349 ? 19.480  17.801  203.934 1.00 147.18 ?  380 GLY A C   1 
ATOM   2667  O O   . GLY A  1 349 ? 18.308  17.477  204.169 1.00 147.59 ?  380 GLY A O   1 
ATOM   2668  N N   . GLU A  1 350 ? 20.081  18.825  204.536 1.00 143.86 ?  381 GLU A N   1 
ATOM   2669  C CA  . GLU A  1 350 ? 19.414  19.679  205.503 1.00 146.32 ?  381 GLU A CA  1 
ATOM   2670  C C   . GLU A  1 350 ? 18.627  20.760  204.771 1.00 146.04 ?  381 GLU A C   1 
ATOM   2671  O O   . GLU A  1 350 ? 18.934  21.122  203.631 1.00 144.22 ?  381 GLU A O   1 
ATOM   2672  C CB  . GLU A  1 350 ? 20.423  20.303  206.468 1.00 148.47 ?  381 GLU A CB  1 
ATOM   2673  C CG  . GLU A  1 350 ? 21.219  19.289  207.282 1.00 150.00 ?  381 GLU A CG  1 
ATOM   2674  C CD  . GLU A  1 350 ? 20.493  18.823  208.533 1.00 155.16 ?  381 GLU A CD  1 
ATOM   2675  O OE1 . GLU A  1 350 ? 19.243  18.839  208.543 1.00 162.13 ?  381 GLU A OE1 1 
ATOM   2676  O OE2 . GLU A  1 350 ? 21.174  18.438  209.509 1.00 154.81 -1 381 GLU A OE2 1 
ATOM   2677  N N   . PHE A  1 351 ? 17.606  21.289  205.445 1.00 144.54 ?  382 PHE A N   1 
ATOM   2678  C CA  . PHE A  1 351 ? 16.749  22.338  204.892 1.00 144.94 ?  382 PHE A CA  1 
ATOM   2679  C C   . PHE A  1 351 ? 16.983  23.676  205.590 1.00 147.68 ?  382 PHE A C   1 
ATOM   2680  O O   . PHE A  1 351 ? 16.524  23.889  206.716 1.00 150.33 ?  382 PHE A O   1 
ATOM   2681  C CB  . PHE A  1 351 ? 15.283  21.921  204.992 1.00 145.47 ?  382 PHE A CB  1 
ATOM   2682  C CG  . PHE A  1 351 ? 14.948  20.716  204.165 1.00 142.95 ?  382 PHE A CG  1 
ATOM   2683  C CD1 . PHE A  1 351 ? 14.548  20.861  202.847 1.00 141.00 ?  382 PHE A CD1 1 
ATOM   2684  C CD2 . PHE A  1 351 ? 15.042  19.440  204.695 1.00 142.68 ?  382 PHE A CD2 1 
ATOM   2685  C CE1 . PHE A  1 351 ? 14.251  19.756  202.072 1.00 138.84 ?  382 PHE A CE1 1 
ATOM   2686  C CE2 . PHE A  1 351 ? 14.743  18.332  203.922 1.00 140.59 ?  382 PHE A CE2 1 
ATOM   2687  C CZ  . PHE A  1 351 ? 14.348  18.489  202.612 1.00 138.67 ?  382 PHE A CZ  1 
ATOM   2688  N N   . PHE A  1 352 ? 17.710  24.567  204.914 1.00 130.74 ?  383 PHE A N   1 
ATOM   2689  C CA  . PHE A  1 352 ? 18.043  25.867  205.469 1.00 133.36 ?  383 PHE A CA  1 
ATOM   2690  C C   . PHE A  1 352 ? 16.868  26.823  205.291 1.00 134.99 ?  383 PHE A C   1 
ATOM   2691  O O   . PHE A  1 352 ? 16.029  26.661  204.401 1.00 133.55 ?  383 PHE A O   1 
ATOM   2692  C CB  . PHE A  1 352 ? 19.282  26.446  204.782 1.00 132.31 ?  383 PHE A CB  1 
ATOM   2693  C CG  . PHE A  1 352 ? 20.537  25.666  205.032 1.00 131.38 ?  383 PHE A CG  1 
ATOM   2694  C CD1 . PHE A  1 352 ? 20.869  24.592  204.228 1.00 128.49 ?  383 PHE A CD1 1 
ATOM   2695  C CD2 . PHE A  1 352 ? 21.404  26.027  206.047 1.00 133.65 ?  383 PHE A CD2 1 
ATOM   2696  C CE1 . PHE A  1 352 ? 22.021  23.870  204.456 1.00 127.98 ?  383 PHE A CE1 1 
ATOM   2697  C CE2 . PHE A  1 352 ? 22.564  25.309  206.273 1.00 133.08 ?  383 PHE A CE2 1 
ATOM   2698  C CZ  . PHE A  1 352 ? 22.872  24.231  205.476 1.00 130.30 ?  383 PHE A CZ  1 
ATOM   2699  N N   . TYR A  1 353 ? 16.824  27.836  206.155 1.00 135.71 ?  384 TYR A N   1 
ATOM   2700  C CA  . TYR A  1 353 ? 15.828  28.909  206.087 1.00 136.64 ?  384 TYR A CA  1 
ATOM   2701  C C   . TYR A  1 353 ? 16.538  30.203  206.481 1.00 141.84 ?  384 TYR A C   1 
ATOM   2702  O O   . TYR A  1 353 ? 16.653  30.504  207.673 1.00 144.94 ?  384 TYR A O   1 
ATOM   2703  C CB  . TYR A  1 353 ? 14.630  28.613  206.984 1.00 138.21 ?  384 TYR A CB  1 
ATOM   2704  C CG  . TYR A  1 353 ? 13.831  27.399  206.547 1.00 136.32 ?  384 TYR A CG  1 
ATOM   2705  C CD1 . TYR A  1 353 ? 12.778  27.514  205.648 1.00 134.91 ?  384 TYR A CD1 1 
ATOM   2706  C CD2 . TYR A  1 353 ? 14.133  26.135  207.038 1.00 136.06 ?  384 TYR A CD2 1 
ATOM   2707  C CE1 . TYR A  1 353 ? 12.050  26.398  205.249 1.00 133.23 ?  384 TYR A CE1 1 
ATOM   2708  C CE2 . TYR A  1 353 ? 13.416  25.020  206.647 1.00 134.38 ?  384 TYR A CE2 1 
ATOM   2709  C CZ  . TYR A  1 353 ? 12.375  25.153  205.755 1.00 132.95 ?  384 TYR A CZ  1 
ATOM   2710  O OH  . TYR A  1 353 ? 11.665  24.036  205.372 1.00 131.33 ?  384 TYR A OH  1 
ATOM   2711  N N   . CYS A  1 354 ? 17.000  30.969  205.494 1.00 146.62 ?  385 CYS A N   1 
ATOM   2712  C CA  . CYS A  1 354 ? 17.870  32.113  205.738 1.00 148.18 ?  385 CYS A CA  1 
ATOM   2713  C C   . CYS A  1 354 ? 17.089  33.422  205.754 1.00 149.64 ?  385 CYS A C   1 
ATOM   2714  O O   . CYS A  1 354 ? 16.130  33.614  205.001 1.00 148.59 ?  385 CYS A O   1 
ATOM   2715  C CB  . CYS A  1 354 ? 18.963  32.185  204.667 1.00 146.22 ?  385 CYS A CB  1 
ATOM   2716  S SG  . CYS A  1 354 ? 20.037  30.719  204.591 1.00 144.67 ?  385 CYS A SG  1 
ATOM   2717  N N   . ASN A  1 355 ? 17.543  34.331  206.615 1.00 164.66 ?  386 ASN A N   1 
ATOM   2718  C CA  . ASN A  1 355 ? 16.955  35.656  206.773 1.00 169.20 ?  386 ASN A CA  1 
ATOM   2719  C C   . ASN A  1 355 ? 17.424  36.572  205.656 1.00 166.79 ?  386 ASN A C   1 
ATOM   2720  O O   . ASN A  1 355 ? 18.615  36.888  205.565 1.00 164.51 ?  386 ASN A O   1 
ATOM   2721  C CB  . ASN A  1 355 ? 17.340  36.252  208.126 1.00 173.57 ?  386 ASN A CB  1 
ATOM   2722  C CG  . ASN A  1 355 ? 16.456  37.431  208.533 1.00 178.75 ?  386 ASN A CG  1 
ATOM   2723  O OD1 . ASN A  1 355 ? 15.798  38.052  207.699 1.00 178.90 ?  386 ASN A OD1 1 
ATOM   2724  N ND2 . ASN A  1 355 ? 16.470  37.757  209.824 1.00 194.50 ?  386 ASN A ND2 1 
ATOM   2725  N N   . THR A  1 356 ? 16.494  37.008  204.812 1.00 170.17 ?  387 THR A N   1 
ATOM   2726  C CA  . THR A  1 356 ? 16.850  37.870  203.692 1.00 167.88 ?  387 THR A CA  1 
ATOM   2727  C C   . THR A  1 356 ? 16.476  39.315  203.967 1.00 172.16 ?  387 THR A C   1 
ATOM   2728  O O   . THR A  1 356 ? 15.925  40.011  203.111 1.00 172.10 ?  387 THR A O   1 
ATOM   2729  C CB  . THR A  1 356 ? 16.183  37.378  202.414 1.00 165.12 ?  387 THR A CB  1 
ATOM   2730  O OG1 . THR A  1 356 ? 14.774  37.228  202.636 1.00 168.76 ?  387 THR A OG1 1 
ATOM   2731  C CG2 . THR A  1 356 ? 16.775  36.051  202.002 1.00 160.17 ?  387 THR A CG2 1 
ATOM   2732  N N   . SER A  1 357 ? 16.769  39.784  205.177 1.00 175.26 ?  388 SER A N   1 
ATOM   2733  C CA  . SER A  1 357 ? 16.524  41.169  205.543 1.00 181.55 ?  388 SER A CA  1 
ATOM   2734  C C   . SER A  1 357 ? 17.740  42.040  205.283 1.00 179.38 ?  388 SER A C   1 
ATOM   2735  O O   . SER A  1 357 ? 17.637  43.269  205.367 1.00 183.46 ?  388 SER A O   1 
ATOM   2736  C CB  . SER A  1 357 ? 16.114  41.275  207.015 1.00 191.13 ?  388 SER A CB  1 
ATOM   2737  O OG  . SER A  1 357 ? 14.887  40.607  207.249 1.00 190.14 ?  388 SER A OG  1 
ATOM   2738  N N   . GLY A  1 358 ? 18.879  41.422  204.970 1.00 185.66 ?  389 GLY A N   1 
ATOM   2739  C CA  . GLY A  1 358 ? 20.137  42.095  204.713 1.00 183.02 ?  389 GLY A CA  1 
ATOM   2740  C C   . GLY A  1 358 ? 20.395  42.249  203.230 1.00 179.46 ?  389 GLY A C   1 
ATOM   2741  O O   . GLY A  1 358 ? 21.365  42.891  202.814 1.00 177.69 ?  389 GLY A O   1 
ATOM   2742  N N   . LEU A  1 359 ? 19.522  41.646  202.426 1.00 186.82 ?  390 LEU A N   1 
ATOM   2743  C CA  . LEU A  1 359 ? 19.596  41.691  200.971 1.00 179.57 ?  390 LEU A CA  1 
ATOM   2744  C C   . LEU A  1 359 ? 18.624  42.685  200.360 1.00 183.14 ?  390 LEU A C   1 
ATOM   2745  O O   . LEU A  1 359 ? 18.925  43.265  199.312 1.00 181.79 ?  390 LEU A O   1 
ATOM   2746  C CB  . LEU A  1 359 ? 19.327  40.308  200.364 1.00 175.84 ?  390 LEU A CB  1 
ATOM   2747  C CG  . LEU A  1 359 ? 20.271  39.168  200.732 1.00 172.51 ?  390 LEU A CG  1 
ATOM   2748  C CD1 . LEU A  1 359 ? 19.807  37.891  200.057 1.00 169.20 ?  390 LEU A CD1 1 
ATOM   2749  C CD2 . LEU A  1 359 ? 21.703  39.508  200.335 1.00 168.78 ?  390 LEU A CD2 1 
ATOM   2750  N N   . PHE A  1 360 ? 17.469  42.889  200.989 1.00 182.85 ?  391 PHE A N   1 
ATOM   2751  C CA  . PHE A  1 360 ? 16.432  43.768  200.468 1.00 188.64 ?  391 PHE A CA  1 
ATOM   2752  C C   . PHE A  1 360 ? 16.268  45.009  201.342 1.00 193.76 ?  391 PHE A C   1 
ATOM   2753  O O   . PHE A  1 360 ? 15.150  45.356  201.730 1.00 195.64 ?  391 PHE A O   1 
ATOM   2754  C CB  . PHE A  1 360 ? 15.132  42.964  200.401 1.00 189.55 ?  391 PHE A CB  1 
ATOM   2755  C CG  . PHE A  1 360 ? 15.254  41.706  199.580 1.00 182.19 ?  391 PHE A CG  1 
ATOM   2756  C CD1 . PHE A  1 360 ? 15.743  41.754  198.287 1.00 176.99 ?  391 PHE A CD1 1 
ATOM   2757  C CD2 . PHE A  1 360 ? 14.945  40.468  200.128 1.00 181.26 ?  391 PHE A CD2 1 
ATOM   2758  C CE1 . PHE A  1 360 ? 15.879  40.603  197.540 1.00 172.29 ?  391 PHE A CE1 1 
ATOM   2759  C CE2 . PHE A  1 360 ? 15.083  39.310  199.382 1.00 176.57 ?  391 PHE A CE2 1 
ATOM   2760  C CZ  . PHE A  1 360 ? 15.550  39.380  198.087 1.00 172.08 ?  391 PHE A CZ  1 
ATOM   2761  N N   . ASN A  1 361 ? 17.382  45.638  201.715 1.00 196.66 ?  392 ASN A N   1 
ATOM   2762  C CA  . ASN A  1 361 ? 17.409  46.870  202.513 1.00 212.16 ?  392 ASN A CA  1 
ATOM   2763  C C   . ASN A  1 361 ? 18.090  48.022  201.755 1.00 214.24 ?  392 ASN A C   1 
ATOM   2764  O O   . ASN A  1 361 ? 19.219  48.387  202.097 1.00 220.35 ?  392 ASN A O   1 
ATOM   2765  C CB  . ASN A  1 361 ? 18.134  46.549  203.840 1.00 217.99 ?  392 ASN A CB  1 
ATOM   2766  C CG  . ASN A  1 361 ? 18.254  47.738  204.765 1.00 228.90 ?  392 ASN A CG  1 
ATOM   2767  O OD1 . ASN A  1 361 ? 17.406  48.629  204.774 1.00 238.25 ?  392 ASN A OD1 1 
ATOM   2768  N ND2 . ASN A  1 361 ? 19.324  47.754  205.558 1.00 240.59 ?  392 ASN A ND2 1 
ATOM   2769  N N   . SER A  1 362 ? 17.447  48.587  200.727 1.00 210.48 ?  393 SER A N   1 
ATOM   2770  C CA  . SER A  1 362 ? 18.127  49.632  199.962 1.00 212.35 ?  393 SER A CA  1 
ATOM   2771  C C   . SER A  1 362 ? 17.146  50.678  199.439 1.00 221.34 ?  393 SER A C   1 
ATOM   2772  O O   . SER A  1 362 ? 15.926  50.502  199.503 1.00 224.01 ?  393 SER A O   1 
ATOM   2773  C CB  . SER A  1 362 ? 18.885  49.023  198.780 1.00 204.99 ?  393 SER A CB  1 
ATOM   2774  O OG  . SER A  1 362 ? 19.779  48.016  199.215 1.00 201.76 ?  393 SER A OG  1 
ATOM   2775  N N   . THR A  1 363 ? 17.698  51.782  198.910 1.00 224.33 ?  394 THR A N   1 
ATOM   2776  C CA  . THR A  1 363 ? 16.873  52.823  198.292 1.00 229.35 ?  394 THR A CA  1 
ATOM   2777  C C   . THR A  1 363 ? 17.677  53.553  197.219 1.00 225.00 ?  394 THR A C   1 
ATOM   2778  O O   . THR A  1 363 ? 18.560  54.357  197.532 1.00 227.52 ?  394 THR A O   1 
ATOM   2779  C CB  . THR A  1 363 ? 16.375  53.817  199.339 1.00 239.19 ?  394 THR A CB  1 
ATOM   2780  O OG1 . THR A  1 363 ? 15.580  53.142  200.323 1.00 238.61 ?  394 THR A OG1 1 
ATOM   2781  C CG2 . THR A  1 363 ? 15.562  54.919  198.685 1.00 238.50 ?  394 THR A CG2 1 
ATOM   2782  N N   . TRP A  1 364 ? 17.363  53.259  195.965 1.00 231.97 ?  395 TRP A N   1 
ATOM   2783  C CA  . TRP A  1 364 ? 18.026  53.791  194.776 1.00 232.85 ?  395 TRP A CA  1 
ATOM   2784  C C   . TRP A  1 364 ? 17.224  54.882  194.069 1.00 237.91 ?  395 TRP A C   1 
ATOM   2785  O O   . TRP A  1 364 ? 16.049  54.684  193.743 1.00 238.52 ?  395 TRP A O   1 
ATOM   2786  C CB  . TRP A  1 364 ? 18.495  52.649  193.886 1.00 226.71 ?  395 TRP A CB  1 
ATOM   2787  C CG  . TRP A  1 364 ? 19.605  51.975  194.649 1.00 223.78 ?  395 TRP A CG  1 
ATOM   2788  C CD1 . TRP A  1 364 ? 19.502  51.020  195.620 1.00 218.29 ?  395 TRP A CD1 1 
ATOM   2789  C CD2 . TRP A  1 364 ? 21.005  52.240  194.491 1.00 222.67 ?  395 TRP A CD2 1 
ATOM   2790  N NE1 . TRP A  1 364 ? 20.757  50.685  196.085 1.00 217.00 ?  395 TRP A NE1 1 
ATOM   2791  C CE2 . TRP A  1 364 ? 21.695  51.414  195.399 1.00 216.82 ?  395 TRP A CE2 1 
ATOM   2792  C CE3 . TRP A  1 364 ? 21.740  53.094  193.659 1.00 221.96 ?  395 TRP A CE3 1 
ATOM   2793  C CZ2 . TRP A  1 364 ? 23.087  51.416  195.498 1.00 215.80 ?  395 TRP A CZ2 1 
ATOM   2794  C CZ3 . TRP A  1 364 ? 23.117  53.096  193.758 1.00 218.05 ?  395 TRP A CZ3 1 
ATOM   2795  C CH2 . TRP A  1 364 ? 23.777  52.263  194.671 1.00 216.03 ?  395 TRP A CH2 1 
ATOM   2796  N N   . ILE A  1 365 ? 17.868  56.029  193.841 1.00 225.03 ?  396 ILE A N   1 
ATOM   2797  C CA  . ILE A  1 365 ? 17.295  57.179  193.142 1.00 229.79 ?  396 ILE A CA  1 
ATOM   2798  C C   . ILE A  1 365 ? 17.514  57.019  191.645 1.00 227.38 ?  396 ILE A C   1 
ATOM   2799  O O   . ILE A  1 365 ? 18.210  56.098  191.208 1.00 222.29 ?  396 ILE A O   1 
ATOM   2800  C CB  . ILE A  1 365 ? 17.941  58.493  193.617 1.00 235.68 ?  396 ILE A CB  1 
ATOM   2801  C CG1 . ILE A  1 365 ? 18.382  58.383  195.074 1.00 236.07 ?  396 ILE A CG1 1 
ATOM   2802  C CG2 . ILE A  1 365 ? 16.988  59.671  193.437 1.00 242.03 ?  396 ILE A CG2 1 
ATOM   2803  C CD1 . ILE A  1 365 ? 17.239  58.334  196.048 1.00 238.82 ?  396 ILE A CD1 1 
ATOM   2804  N N   . SER A  1 366 ? 16.949  57.936  190.852 1.00 242.81 ?  397 SER A N   1 
ATOM   2805  C CA  . SER A  1 366 ? 17.057  57.866  189.396 1.00 245.08 ?  397 SER A CA  1 
ATOM   2806  C C   . SER A  1 366 ? 18.513  57.845  188.951 1.00 243.53 ?  397 SER A C   1 
ATOM   2807  O O   . SER A  1 366 ? 18.833  57.292  187.892 1.00 237.46 ?  397 SER A O   1 
ATOM   2808  C CB  . SER A  1 366 ? 16.323  59.040  188.747 1.00 253.12 ?  397 SER A CB  1 
ATOM   2809  O OG  . SER A  1 366 ? 16.938  60.270  189.082 1.00 263.00 ?  397 SER A OG  1 
ATOM   2810  N N   . ASN A  1 367 ? 19.396  58.453  189.734 1.00 233.98 ?  398 ASN A N   1 
ATOM   2811  C CA  . ASN A  1 367 ? 20.817  58.491  189.436 1.00 232.97 ?  398 ASN A CA  1 
ATOM   2812  C C   . ASN A  1 367 ? 21.609  58.732  190.712 1.00 234.63 ?  398 ASN A C   1 
ATOM   2813  O O   . ASN A  1 367 ? 22.172  57.796  191.282 1.00 230.55 ?  398 ASN A O   1 
ATOM   2814  C CB  . ASN A  1 367 ? 21.107  59.609  188.446 1.00 237.11 ?  398 ASN A CB  1 
ATOM   2815  C CG  . ASN A  1 367 ? 20.588  60.946  188.936 1.00 244.11 ?  398 ASN A CG  1 
ATOM   2816  O OD1 . ASN A  1 367 ? 19.452  61.322  188.652 1.00 247.04 ?  398 ASN A OD1 1 
ATOM   2817  N ND2 . ASN A  1 367 ? 21.407  61.657  189.705 1.00 248.95 ?  398 ASN A ND2 1 
ATOM   2818  N N   . ASN A  1 379 ? 35.125  46.054  201.537 1.00 249.68 ?  411 ASN A N   1 
ATOM   2819  C CA  . ASN A  1 379 ? 35.394  44.854  200.751 1.00 241.45 ?  411 ASN A CA  1 
ATOM   2820  C C   . ASN A  1 379 ? 35.304  43.586  201.594 1.00 235.85 ?  411 ASN A C   1 
ATOM   2821  O O   . ASN A  1 379 ? 36.312  43.125  202.132 1.00 234.44 ?  411 ASN A O   1 
ATOM   2822  C CB  . ASN A  1 379 ? 36.772  44.933  200.091 1.00 239.57 ?  411 ASN A CB  1 
ATOM   2823  C CG  . ASN A  1 379 ? 37.056  43.740  199.193 1.00 231.44 ?  411 ASN A CG  1 
ATOM   2824  O OD1 . ASN A  1 379 ? 36.138  43.077  198.708 1.00 227.74 ?  411 ASN A OD1 1 
ATOM   2825  N ND2 . ASN A  1 379 ? 38.335  43.452  198.982 1.00 228.10 ?  411 ASN A ND2 1 
ATOM   2826  N N   . ASP A  1 380 ? 34.100  43.026  201.721 1.00 232.44 ?  412 ASP A N   1 
ATOM   2827  C CA  . ASP A  1 380 ? 33.949  41.806  202.504 1.00 222.30 ?  412 ASP A CA  1 
ATOM   2828  C C   . ASP A  1 380 ? 32.763  40.972  202.023 1.00 214.57 ?  412 ASP A C   1 
ATOM   2829  O O   . ASP A  1 380 ? 32.494  40.913  200.818 1.00 212.85 ?  412 ASP A O   1 
ATOM   2830  C CB  . ASP A  1 380 ? 33.804  42.151  203.988 1.00 219.62 ?  412 ASP A CB  1 
ATOM   2831  C CG  . ASP A  1 380 ? 34.271  41.028  204.894 1.00 212.32 ?  412 ASP A CG  1 
ATOM   2832  O OD1 . ASP A  1 380 ? 35.083  40.196  204.436 1.00 211.81 ?  412 ASP A OD1 1 
ATOM   2833  O OD2 . ASP A  1 380 ? 33.824  40.973  206.060 1.00 213.48 -1 412 ASP A OD2 1 
ATOM   2834  N N   . SER A  1 381 ? 32.049  40.323  202.947 1.00 205.69 ?  413 SER A N   1 
ATOM   2835  C CA  . SER A  1 381 ? 30.919  39.471  202.603 1.00 201.50 ?  413 SER A CA  1 
ATOM   2836  C C   . SER A  1 381 ? 29.710  39.761  203.490 1.00 201.63 ?  413 SER A C   1 
ATOM   2837  O O   . SER A  1 381 ? 29.849  40.103  204.668 1.00 204.83 ?  413 SER A O   1 
ATOM   2838  C CB  . SER A  1 381 ? 31.315  37.998  202.708 1.00 196.85 ?  413 SER A CB  1 
ATOM   2839  O OG  . SER A  1 381 ? 30.307  37.171  202.171 1.00 193.77 ?  413 SER A OG  1 
ATOM   2840  N N   . ILE A  1 382 ? 28.519  39.621  202.906 1.00 180.56 ?  414 ILE A N   1 
ATOM   2841  C CA  . ILE A  1 382 ? 27.248  39.832  203.604 1.00 182.19 ?  414 ILE A CA  1 
ATOM   2842  C C   . ILE A  1 382 ? 26.746  38.519  204.205 1.00 180.53 ?  414 ILE A C   1 
ATOM   2843  O O   . ILE A  1 382 ? 26.241  37.652  203.493 1.00 177.19 ?  414 ILE A O   1 
ATOM   2844  C CB  . ILE A  1 382 ? 26.195  40.432  202.674 1.00 181.85 ?  414 ILE A CB  1 
ATOM   2845  C CG1 . ILE A  1 382 ? 26.704  41.722  202.037 1.00 187.06 ?  414 ILE A CG1 1 
ATOM   2846  C CG2 . ILE A  1 382 ? 24.903  40.670  203.431 1.00 184.10 ?  414 ILE A CG2 1 
ATOM   2847  C CD1 . ILE A  1 382 ? 25.726  42.346  201.073 1.00 189.50 ?  414 ILE A CD1 1 
ATOM   2848  N N   . THR A  1 383 ? 26.895  38.364  205.517 1.00 177.54 ?  415 THR A N   1 
ATOM   2849  C CA  . THR A  1 383 ? 26.458  37.152  206.203 1.00 176.39 ?  415 THR A CA  1 
ATOM   2850  C C   . THR A  1 383 ? 24.953  37.199  206.476 1.00 177.21 ?  415 THR A C   1 
ATOM   2851  O O   . THR A  1 383 ? 24.418  38.240  206.869 1.00 180.45 ?  415 THR A O   1 
ATOM   2852  C CB  . THR A  1 383 ? 27.220  36.977  207.516 1.00 178.76 ?  415 THR A CB  1 
ATOM   2853  O OG1 . THR A  1 383 ? 28.627  37.103  207.272 1.00 178.64 ?  415 THR A OG1 1 
ATOM   2854  C CG2 . THR A  1 383 ? 26.931  35.608  208.127 1.00 177.28 ?  415 THR A CG2 1 
ATOM   2855  N N   . LEU A  1 384 ? 24.263  36.074  206.264 1.00 171.63 ?  416 LEU A N   1 
ATOM   2856  C CA  . LEU A  1 384 ? 22.818  36.007  206.477 1.00 172.25 ?  416 LEU A CA  1 
ATOM   2857  C C   . LEU A  1 384 ? 22.473  34.918  207.486 1.00 172.17 ?  416 LEU A C   1 
ATOM   2858  O O   . LEU A  1 384 ? 22.923  33.773  207.341 1.00 169.48 ?  416 LEU A O   1 
ATOM   2859  C CB  . LEU A  1 384 ? 22.054  35.764  205.170 1.00 169.37 ?  416 LEU A CB  1 
ATOM   2860  C CG  . LEU A  1 384 ? 22.330  36.766  204.058 1.00 169.27 ?  416 LEU A CG  1 
ATOM   2861  C CD1 . LEU A  1 384 ? 21.554  36.385  202.822 1.00 166.35 ?  416 LEU A CD1 1 
ATOM   2862  C CD2 . LEU A  1 384 ? 21.928  38.148  204.533 1.00 173.48 ?  416 LEU A CD2 1 
ATOM   2863  N N   . PRO A  1 385 ? 21.678  35.237  208.510 1.00 175.73 ?  417 PRO A N   1 
ATOM   2864  C CA  . PRO A  1 385 ? 21.277  34.243  209.529 1.00 176.04 ?  417 PRO A CA  1 
ATOM   2865  C C   . PRO A  1 385 ? 20.426  33.112  208.969 1.00 172.86 ?  417 PRO A C   1 
ATOM   2866  O O   . PRO A  1 385 ? 19.339  33.348  208.434 1.00 172.67 ?  417 PRO A O   1 
ATOM   2867  C CB  . PRO A  1 385 ? 20.468  35.083  210.527 1.00 181.22 ?  417 PRO A CB  1 
ATOM   2868  C CG  . PRO A  1 385 ? 20.865  36.512  210.270 1.00 182.82 ?  417 PRO A CG  1 
ATOM   2869  C CD  . PRO A  1 385 ? 21.144  36.578  208.799 1.00 179.51 ?  417 PRO A CD  1 
ATOM   2870  N N   . CYS A  1 386 ? 20.919  31.874  209.078 1.00 164.49 ?  418 CYS A N   1 
ATOM   2871  C CA  . CYS A  1 386 ? 20.188  30.735  208.534 1.00 162.10 ?  418 CYS A CA  1 
ATOM   2872  C C   . CYS A  1 386 ? 19.823  29.760  209.650 1.00 159.57 ?  418 CYS A C   1 
ATOM   2873  O O   . CYS A  1 386 ? 20.679  29.365  210.449 1.00 159.40 ?  418 CYS A O   1 
ATOM   2874  C CB  . CYS A  1 386 ? 21.033  30.016  207.471 1.00 162.31 ?  418 CYS A CB  1 
ATOM   2875  S SG  . CYS A  1 386 ? 21.417  31.075  206.037 1.00 174.30 ?  418 CYS A SG  1 
ATOM   2876  N N   . ARG A  1 387 ? 18.548  29.398  209.706 1.00 156.12 ?  419 ARG A N   1 
ATOM   2877  C CA  . ARG A  1 387 ? 18.000  28.407  210.620 1.00 156.67 ?  419 ARG A CA  1 
ATOM   2878  C C   . ARG A  1 387 ? 17.809  27.101  209.855 1.00 153.13 ?  419 ARG A C   1 
ATOM   2879  O O   . ARG A  1 387 ? 17.768  27.085  208.622 1.00 150.71 ?  419 ARG A O   1 
ATOM   2880  C CB  . ARG A  1 387 ? 16.717  28.867  211.307 1.00 159.64 ?  419 ARG A CB  1 
ATOM   2881  C CG  . ARG A  1 387 ? 16.624  28.211  212.684 1.00 172.85 ?  419 ARG A CG  1 
ATOM   2882  C CD  . ARG A  1 387 ? 16.973  29.155  213.830 1.00 193.65 ?  419 ARG A CD  1 
ATOM   2883  N NE  . ARG A  1 387 ? 15.940  30.154  214.071 1.00 204.76 ?  419 ARG A NE  1 
ATOM   2884  C CZ  . ARG A  1 387 ? 14.916  29.963  214.896 1.00 207.53 ?  419 ARG A CZ  1 
ATOM   2885  N NH1 . ARG A  1 387 ? 14.009  30.915  215.067 1.00 212.29 1  419 ARG A NH1 1 
ATOM   2886  N NH2 . ARG A  1 387 ? 14.804  28.817  215.557 1.00 204.93 ?  419 ARG A NH2 1 
ATOM   2887  N N   . ILE A  1 388 ? 17.699  25.998  210.588 1.00 136.38 ?  420 ILE A N   1 
ATOM   2888  C CA  . ILE A  1 388 ? 17.541  24.687  209.973 1.00 134.06 ?  420 ILE A CA  1 
ATOM   2889  C C   . ILE A  1 388 ? 16.354  23.936  210.553 1.00 134.59 ?  420 ILE A C   1 
ATOM   2890  O O   . ILE A  1 388 ? 16.175  23.897  211.774 1.00 137.12 ?  420 ILE A O   1 
ATOM   2891  C CB  . ILE A  1 388 ? 18.802  23.838  210.160 1.00 133.96 ?  420 ILE A CB  1 
ATOM   2892  C CG1 . ILE A  1 388 ? 19.980  24.493  209.485 1.00 133.25 ?  420 ILE A CG1 1 
ATOM   2893  C CG2 . ILE A  1 388 ? 18.622  22.507  209.502 1.00 131.60 ?  420 ILE A CG2 1 
ATOM   2894  C CD1 . ILE A  1 388 ? 21.146  23.633  209.568 1.00 133.07 ?  420 ILE A CD1 1 
ATOM   2895  N N   . LYS A  1 389 ? 15.490  23.432  209.669 1.00 134.99 ?  421 LYS A N   1 
ATOM   2896  C CA  . LYS A  1 389 ? 14.322  22.652  210.054 1.00 135.53 ?  421 LYS A CA  1 
ATOM   2897  C C   . LYS A  1 389 ? 14.423  21.274  209.409 1.00 132.54 ?  421 LYS A C   1 
ATOM   2898  O O   . LYS A  1 389 ? 14.818  21.146  208.245 1.00 129.82 ?  421 LYS A O   1 
ATOM   2899  C CB  . LYS A  1 389 ? 13.008  23.338  209.635 1.00 136.58 ?  421 LYS A CB  1 
ATOM   2900  C CG  . LYS A  1 389 ? 11.757  22.672  210.217 1.00 137.96 ?  421 LYS A CG  1 
ATOM   2901  C CD  . LYS A  1 389 ? 10.451  23.391  209.899 1.00 139.60 ?  421 LYS A CD  1 
ATOM   2902  C CE  . LYS A  1 389 ? 10.223  23.489  208.407 1.00 137.06 ?  421 LYS A CE  1 
ATOM   2903  N NZ  . LYS A  1 389 ? 8.958   24.203  208.100 1.00 140.16 1  421 LYS A NZ  1 
ATOM   2904  N N   . GLN A  1 390 ? 14.079  20.242  210.176 1.00 140.44 ?  422 GLN A N   1 
ATOM   2905  C CA  . GLN A  1 390 ? 14.136  18.858  209.716 1.00 138.14 ?  422 GLN A CA  1 
ATOM   2906  C C   . GLN A  1 390 ? 12.786  18.300  209.269 1.00 137.68 ?  422 GLN A C   1 
ATOM   2907  O O   . GLN A  1 390 ? 12.728  17.551  208.289 1.00 135.21 ?  422 GLN A O   1 
ATOM   2908  C CB  . GLN A  1 390 ? 14.764  17.963  210.792 1.00 139.10 ?  422 GLN A CB  1 
ATOM   2909  C CG  . GLN A  1 390 ? 16.264  18.247  210.991 1.00 139.04 ?  422 GLN A CG  1 
ATOM   2910  C CD  . GLN A  1 390 ? 16.906  17.453  212.127 1.00 140.46 ?  422 GLN A CD  1 
ATOM   2911  O OE1 . GLN A  1 390 ? 16.275  17.169  213.146 1.00 142.52 ?  422 GLN A OE1 1 
ATOM   2912  N NE2 . GLN A  1 390 ? 18.179  17.106  211.954 1.00 139.55 ?  422 GLN A NE2 1 
ATOM   2913  N N   . ILE A  1 391 ? 11.713  18.623  209.989 1.00 137.08 ?  423 ILE A N   1 
ATOM   2914  C CA  . ILE A  1 391 ? 10.351  18.184  209.679 1.00 137.26 ?  423 ILE A CA  1 
ATOM   2915  C C   . ILE A  1 391 ? 9.671   19.193  208.755 1.00 137.16 ?  423 ILE A C   1 
ATOM   2916  O O   . ILE A  1 391 ? 9.333   20.300  209.182 1.00 139.55 ?  423 ILE A O   1 
ATOM   2917  C CB  . ILE A  1 391 ? 9.530   17.990  210.958 1.00 140.44 ?  423 ILE A CB  1 
ATOM   2918  C CG1 . ILE A  1 391 ? 10.291  17.124  211.958 1.00 140.94 ?  423 ILE A CG1 1 
ATOM   2919  C CG2 . ILE A  1 391 ? 8.169   17.385  210.640 1.00 140.66 ?  423 ILE A CG2 1 
ATOM   2920  C CD1 . ILE A  1 391 ? 9.616   17.047  213.307 1.00 144.28 ?  423 ILE A CD1 1 
ATOM   2921  N N   . ILE A  1 392 ? 9.466   18.821  207.487 1.00 139.38 ?  424 ILE A N   1 
ATOM   2922  C CA  . ILE A  1 392 ? 8.927   19.748  206.498 1.00 138.29 ?  424 ILE A CA  1 
ATOM   2923  C C   . ILE A  1 392 ? 7.596   19.250  205.930 1.00 137.12 ?  424 ILE A C   1 
ATOM   2924  O O   . ILE A  1 392 ? 7.255   18.067  206.004 1.00 136.39 ?  424 ILE A O   1 
ATOM   2925  C CB  . ILE A  1 392 ? 9.930   19.977  205.351 1.00 136.03 ?  424 ILE A CB  1 
ATOM   2926  C CG1 . ILE A  1 392 ? 10.081  18.691  204.533 1.00 133.39 ?  424 ILE A CG1 1 
ATOM   2927  C CG2 . ILE A  1 392 ? 11.279  20.446  205.896 1.00 137.23 ?  424 ILE A CG2 1 
ATOM   2928  C CD1 . ILE A  1 392 ? 10.896  18.856  203.277 1.00 131.01 ?  424 ILE A CD1 1 
ATOM   2929  N N   . ASN A  1 393 ? 6.861   20.189  205.317 1.00 149.48 ?  425 ASN A N   1 
ATOM   2930  C CA  . ASN A  1 393 ? 5.563   19.967  204.651 1.00 154.74 ?  425 ASN A CA  1 
ATOM   2931  C C   . ASN A  1 393 ? 5.510   20.853  203.409 1.00 158.78 ?  425 ASN A C   1 
ATOM   2932  O O   . ASN A  1 393 ? 4.685   21.750  203.276 1.00 163.50 ?  425 ASN A O   1 
ATOM   2933  C CB  . ASN A  1 393 ? 4.356   20.278  205.536 1.00 161.56 ?  425 ASN A CB  1 
ATOM   2934  C CG  . ASN A  1 393 ? 4.070   19.203  206.544 1.00 167.64 ?  425 ASN A CG  1 
ATOM   2935  O OD1 . ASN A  1 393 ? 4.194   18.023  206.240 1.00 171.04 ?  425 ASN A OD1 1 
ATOM   2936  N ND2 . ASN A  1 393 ? 3.654   19.598  207.742 1.00 178.27 ?  425 ASN A ND2 1 
ATOM   2937  N N   . MET A  1 394 ? 6.413   20.586  202.478 1.00 196.73 ?  426 MET A N   1 
ATOM   2938  C CA  . MET A  1 394 ? 6.554   21.394  201.280 1.00 201.23 ?  426 MET A CA  1 
ATOM   2939  C C   . MET A  1 394 ? 5.359   21.202  200.331 1.00 201.73 ?  426 MET A C   1 
ATOM   2940  O O   . MET A  1 394 ? 4.549   20.281  200.479 1.00 201.22 ?  426 MET A O   1 
ATOM   2941  C CB  . MET A  1 394 ? 7.879   21.010  200.618 1.00 194.69 ?  426 MET A CB  1 
ATOM   2942  C CG  . MET A  1 394 ? 8.251   21.658  199.317 1.00 192.63 ?  426 MET A CG  1 
ATOM   2943  S SD  . MET A  1 394 ? 10.033  21.932  199.370 1.00 197.51 ?  426 MET A SD  1 
ATOM   2944  C CE  . MET A  1 394 ? 10.623  20.303  199.852 1.00 180.01 ?  426 MET A CE  1 
ATOM   2945  N N   . TRP A  1 395 ? 5.263   22.103  199.341 1.00 211.02 ?  427 TRP A N   1 
ATOM   2946  C CA  . TRP A  1 395 ? 4.198   22.105  198.327 1.00 209.50 ?  427 TRP A CA  1 
ATOM   2947  C C   . TRP A  1 395 ? 2.793   22.257  198.898 1.00 213.75 ?  427 TRP A C   1 
ATOM   2948  O O   . TRP A  1 395 ? 1.829   21.781  198.290 1.00 216.55 ?  427 TRP A O   1 
ATOM   2949  C CB  . TRP A  1 395 ? 4.271   20.847  197.469 1.00 203.01 ?  427 TRP A CB  1 
ATOM   2950  C CG  . TRP A  1 395 ? 5.492   20.845  196.660 1.00 199.92 ?  427 TRP A CG  1 
ATOM   2951  C CD1 . TRP A  1 395 ? 5.858   21.759  195.718 1.00 198.97 ?  427 TRP A CD1 1 
ATOM   2952  C CD2 . TRP A  1 395 ? 6.551   19.894  196.737 1.00 196.19 ?  427 TRP A CD2 1 
ATOM   2953  N NE1 . TRP A  1 395 ? 7.083   21.428  195.194 1.00 197.42 ?  427 TRP A NE1 1 
ATOM   2954  C CE2 . TRP A  1 395 ? 7.529   20.283  195.803 1.00 194.27 ?  427 TRP A CE2 1 
ATOM   2955  C CE3 . TRP A  1 395 ? 6.764   18.744  197.501 1.00 190.47 ?  427 TRP A CE3 1 
ATOM   2956  C CZ2 . TRP A  1 395 ? 8.703   19.562  195.611 1.00 191.27 ?  427 TRP A CZ2 1 
ATOM   2957  C CZ3 . TRP A  1 395 ? 7.925   18.033  197.311 1.00 187.05 ?  427 TRP A CZ3 1 
ATOM   2958  C CH2 . TRP A  1 395 ? 8.882   18.441  196.373 1.00 188.22 ?  427 TRP A CH2 1 
ATOM   2959  N N   . GLN A  1 396 ? 2.650   22.909  200.053 1.00 198.83 ?  428 GLN A N   1 
ATOM   2960  C CA  . GLN A  1 396 ? 1.337   23.110  200.670 1.00 205.12 ?  428 GLN A CA  1 
ATOM   2961  C C   . GLN A  1 396 ? 0.621   21.782  200.835 1.00 205.37 ?  428 GLN A C   1 
ATOM   2962  O O   . GLN A  1 396 ? -0.596  21.680  200.658 1.00 207.38 ?  428 GLN A O   1 
ATOM   2963  C CB  . GLN A  1 396 ? 0.462   24.019  199.801 1.00 209.48 ?  428 GLN A CB  1 
ATOM   2964  C CG  . GLN A  1 396 ? 0.652   25.506  199.815 1.00 213.42 ?  428 GLN A CG  1 
ATOM   2965  C CD  . GLN A  1 396 ? -0.646  26.204  200.197 1.00 224.03 ?  428 GLN A CD  1 
ATOM   2966  O OE1 . GLN A  1 396 ? -1.699  25.922  199.614 1.00 226.97 ?  428 GLN A OE1 1 
ATOM   2967  N NE2 . GLN A  1 396 ? -0.580  27.125  201.145 1.00 229.50 ?  428 GLN A NE2 1 
ATOM   2968  N N   . ARG A  1 397 ? 1.372   20.751  201.189 1.00 192.67 ?  429 ARG A N   1 
ATOM   2969  C CA  . ARG A  1 397 ? 0.787   19.431  201.308 1.00 191.92 ?  429 ARG A CA  1 
ATOM   2970  C C   . ARG A  1 397 ? 0.523   19.136  202.774 1.00 197.56 ?  429 ARG A C   1 
ATOM   2971  O O   . ARG A  1 397 ? 1.412   19.300  203.618 1.00 194.99 ?  429 ARG A O   1 
ATOM   2972  C CB  . ARG A  1 397 ? 1.699   18.385  200.672 1.00 179.83 ?  429 ARG A CB  1 
ATOM   2973  C CG  . ARG A  1 397 ? 1.818   18.599  199.164 1.00 174.84 ?  429 ARG A CG  1 
ATOM   2974  C CD  . ARG A  1 397 ? 2.556   17.482  198.476 1.00 164.84 ?  429 ARG A CD  1 
ATOM   2975  N NE  . ARG A  1 397 ? 1.951   16.196  198.786 1.00 162.05 ?  429 ARG A NE  1 
ATOM   2976  C CZ  . ARG A  1 397 ? 2.495   15.289  199.586 1.00 164.49 ?  429 ARG A CZ  1 
ATOM   2977  N NH1 . ARG A  1 397 ? 3.664   15.528  200.168 1.00 161.76 1  429 ARG A NH1 1 
ATOM   2978  N NH2 . ARG A  1 397 ? 1.864   14.145  199.805 1.00 168.29 ?  429 ARG A NH2 1 
ATOM   2979  N N   . ILE A  1 398 ? -0.684  18.678  203.065 1.00 196.59 ?  430 ILE A N   1 
ATOM   2980  C CA  . ILE A  1 398 ? -1.079  18.275  204.405 1.00 199.97 ?  430 ILE A CA  1 
ATOM   2981  C C   . ILE A  1 398 ? -1.387  16.792  204.334 1.00 198.59 ?  430 ILE A C   1 
ATOM   2982  O O   . ILE A  1 398 ? -2.105  16.344  203.432 1.00 201.96 ?  430 ILE A O   1 
ATOM   2983  C CB  . ILE A  1 398 ? -2.258  19.098  204.955 1.00 208.43 ?  430 ILE A CB  1 
ATOM   2984  C CG1 . ILE A  1 398 ? -1.938  20.594  204.871 1.00 205.25 ?  430 ILE A CG1 1 
ATOM   2985  C CG2 . ILE A  1 398 ? -2.545  18.712  206.393 1.00 209.84 ?  430 ILE A CG2 1 
ATOM   2986  C CD1 . ILE A  1 398 ? -2.371  21.270  203.607 1.00 204.62 ?  430 ILE A CD1 1 
ATOM   2987  N N   . GLY A  1 399 ? -0.848  16.036  205.290 1.00 180.38 ?  431 GLY A N   1 
ATOM   2988  C CA  . GLY A  1 399 ? -1.006  14.594  205.349 1.00 175.20 ?  431 GLY A CA  1 
ATOM   2989  C C   . GLY A  1 399 ? 0.315   13.858  205.250 1.00 172.55 ?  431 GLY A C   1 
ATOM   2990  O O   . GLY A  1 399 ? 0.448   12.754  205.790 1.00 171.50 ?  431 GLY A O   1 
ATOM   2991  N N   . GLN A  1 400 ? 1.284   14.445  204.545 1.00 172.41 ?  432 GLN A N   1 
ATOM   2992  C CA  . GLN A  1 400 ? 2.606   13.866  204.324 1.00 164.12 ?  432 GLN A CA  1 
ATOM   2993  C C   . GLN A  1 400 ? 3.675   14.817  204.865 1.00 159.69 ?  432 GLN A C   1 
ATOM   2994  O O   . GLN A  1 400 ? 3.989   15.831  204.231 1.00 161.39 ?  432 GLN A O   1 
ATOM   2995  C CB  . GLN A  1 400 ? 2.799   13.589  202.839 1.00 166.23 ?  432 GLN A CB  1 
ATOM   2996  C CG  . GLN A  1 400 ? 3.477   12.291  202.611 1.00 164.40 ?  432 GLN A CG  1 
ATOM   2997  C CD  . GLN A  1 400 ? 2.599   11.173  203.120 1.00 167.78 ?  432 GLN A CD  1 
ATOM   2998  O OE1 . GLN A  1 400 ? 2.967   10.464  204.053 1.00 167.96 ?  432 GLN A OE1 1 
ATOM   2999  N NE2 . GLN A  1 400 ? 1.420   11.018  202.520 1.00 168.51 ?  432 GLN A NE2 1 
ATOM   3000  N N   . ALA A  1 401 ? 4.210   14.499  206.045 1.00 147.79 ?  433 ALA A N   1 
ATOM   3001  C CA  . ALA A  1 401 ? 5.271   15.265  206.690 1.00 150.35 ?  433 ALA A CA  1 
ATOM   3002  C C   . ALA A  1 401 ? 6.569   14.475  206.633 1.00 148.29 ?  433 ALA A C   1 
ATOM   3003  O O   . ALA A  1 401 ? 6.599   13.296  206.997 1.00 147.09 ?  433 ALA A O   1 
ATOM   3004  C CB  . ALA A  1 401 ? 4.927   15.601  208.145 1.00 155.13 ?  433 ALA A CB  1 
ATOM   3005  N N   . MET A  1 402 ? 7.623   15.113  206.137 1.00 147.13 ?  434 MET A N   1 
ATOM   3006  C CA  . MET A  1 402 ? 8.923   14.477  205.976 1.00 145.27 ?  434 MET A CA  1 
ATOM   3007  C C   . MET A  1 402 ? 9.939   14.917  207.018 1.00 148.92 ?  434 MET A C   1 
ATOM   3008  O O   . MET A  1 402 ? 10.164  16.116  207.210 1.00 151.96 ?  434 MET A O   1 
ATOM   3009  C CB  . MET A  1 402 ? 9.510   14.781  204.602 1.00 141.59 ?  434 MET A CB  1 
ATOM   3010  C CG  . MET A  1 402 ? 10.753  13.968  204.341 1.00 139.79 ?  434 MET A CG  1 
ATOM   3011  S SD  . MET A  1 402 ? 11.723  14.640  202.989 1.00 138.61 ?  434 MET A SD  1 
ATOM   3012  C CE  . MET A  1 402 ? 13.326  14.759  203.777 1.00 139.41 ?  434 MET A CE  1 
ATOM   3013  N N   . TYR A  1 403 ? 10.553  13.939  207.678 1.00 135.41 ?  435 TYR A N   1 
ATOM   3014  C CA  . TYR A  1 403 ? 11.638  14.164  208.627 1.00 138.69 ?  435 TYR A CA  1 
ATOM   3015  C C   . TYR A  1 403 ? 12.969  13.979  207.911 1.00 136.53 ?  435 TYR A C   1 
ATOM   3016  O O   . TYR A  1 403 ? 13.349  12.850  207.584 1.00 133.73 ?  435 TYR A O   1 
ATOM   3017  C CB  . TYR A  1 403 ? 11.572  13.246  209.842 1.00 140.54 ?  435 TYR A CB  1 
ATOM   3018  C CG  . TYR A  1 403 ? 12.764  13.464  210.759 1.00 143.83 ?  435 TYR A CG  1 
ATOM   3019  C CD1 . TYR A  1 403 ? 12.757  14.448  211.740 1.00 148.49 ?  435 TYR A CD1 1 
ATOM   3020  C CD2 . TYR A  1 403 ? 13.910  12.681  210.629 1.00 143.38 ?  435 TYR A CD2 1 
ATOM   3021  C CE1 . TYR A  1 403 ? 13.862  14.643  212.566 1.00 151.50 ?  435 TYR A CE1 1 
ATOM   3022  C CE2 . TYR A  1 403 ? 15.010  12.868  211.442 1.00 147.61 ?  435 TYR A CE2 1 
ATOM   3023  C CZ  . TYR A  1 403 ? 14.984  13.846  212.411 1.00 149.91 ?  435 TYR A CZ  1 
ATOM   3024  O OH  . TYR A  1 403 ? 16.088  14.020  213.218 1.00 152.38 ?  435 TYR A OH  1 
ATOM   3025  N N   . ALA A  1 404 ? 13.659  15.071  207.649 1.00 132.54 ?  436 ALA A N   1 
ATOM   3026  C CA  . ALA A  1 404 ? 14.951  14.970  206.993 1.00 131.25 ?  436 ALA A CA  1 
ATOM   3027  C C   . ALA A  1 404 ? 15.946  14.383  207.982 1.00 133.12 ?  436 ALA A C   1 
ATOM   3028  O O   . ALA A  1 404 ? 16.158  14.971  209.051 1.00 135.72 ?  436 ALA A O   1 
ATOM   3029  C CB  . ALA A  1 404 ? 15.417  16.334  206.518 1.00 131.16 ?  436 ALA A CB  1 
ATOM   3030  N N   . PRO A  1 405 ? 16.574  13.251  207.685 1.00 137.11 ?  437 PRO A N   1 
ATOM   3031  C CA  . PRO A  1 405 ? 17.531  12.665  208.627 1.00 139.54 ?  437 PRO A CA  1 
ATOM   3032  C C   . PRO A  1 405 ? 18.749  13.553  208.804 1.00 142.28 ?  437 PRO A C   1 
ATOM   3033  O O   . PRO A  1 405 ? 19.194  14.218  207.857 1.00 140.72 ?  437 PRO A O   1 
ATOM   3034  C CB  . PRO A  1 405 ? 17.900  11.328  207.967 1.00 135.85 ?  437 PRO A CB  1 
ATOM   3035  C CG  . PRO A  1 405 ? 17.648  11.549  206.512 1.00 131.67 ?  437 PRO A CG  1 
ATOM   3036  C CD  . PRO A  1 405 ? 16.451  12.455  206.451 1.00 132.11 ?  437 PRO A CD  1 
ATOM   3037  N N   . PRO A  1 406 ? 19.306  13.594  210.014 1.00 144.78 ?  438 PRO A N   1 
ATOM   3038  C CA  . PRO A  1 406 ? 20.487  14.428  210.268 1.00 146.06 ?  438 PRO A CA  1 
ATOM   3039  C C   . PRO A  1 406 ? 21.657  14.016  209.390 1.00 143.87 ?  438 PRO A C   1 
ATOM   3040  O O   . PRO A  1 406 ? 21.779  12.859  208.983 1.00 142.36 ?  438 PRO A O   1 
ATOM   3041  C CB  . PRO A  1 406 ? 20.784  14.179  211.751 1.00 146.85 ?  438 PRO A CB  1 
ATOM   3042  C CG  . PRO A  1 406 ? 19.493  13.688  212.316 1.00 148.83 ?  438 PRO A CG  1 
ATOM   3043  C CD  . PRO A  1 406 ? 18.841  12.909  211.229 1.00 146.40 ?  438 PRO A CD  1 
ATOM   3044  N N   . ILE A  1 407 ? 22.527  14.981  209.099 1.00 151.79 ?  439 ILE A N   1 
ATOM   3045  C CA  . ILE A  1 407 ? 23.701  14.753  208.265 1.00 149.20 ?  439 ILE A CA  1 
ATOM   3046  C C   . ILE A  1 407 ? 24.955  14.968  209.099 1.00 147.80 ?  439 ILE A C   1 
ATOM   3047  O O   . ILE A  1 407 ? 25.104  16.007  209.753 1.00 149.73 ?  439 ILE A O   1 
ATOM   3048  C CB  . ILE A  1 407 ? 23.707  15.674  207.034 1.00 146.81 ?  439 ILE A CB  1 
ATOM   3049  C CG1 . ILE A  1 407 ? 22.346  15.622  206.341 1.00 148.33 ?  439 ILE A CG1 1 
ATOM   3050  C CG2 . ILE A  1 407 ? 24.832  15.287  206.081 1.00 143.96 ?  439 ILE A CG2 1 
ATOM   3051  C CD1 . ILE A  1 407 ? 21.986  14.249  205.819 1.00 145.44 ?  439 ILE A CD1 1 
ATOM   3052  N N   . GLN A  1 408 ? 25.851  13.983  209.065 1.00 171.00 ?  440 GLN A N   1 
ATOM   3053  C CA  . GLN A  1 408 ? 27.096  14.037  209.820 1.00 173.62 ?  440 GLN A CA  1 
ATOM   3054  C C   . GLN A  1 408 ? 28.071  15.031  209.200 1.00 169.60 ?  440 GLN A C   1 
ATOM   3055  O O   . GLN A  1 408 ? 28.167  15.153  207.976 1.00 168.25 ?  440 GLN A O   1 
ATOM   3056  C CB  . GLN A  1 408 ? 27.742  12.650  209.887 1.00 173.53 ?  440 GLN A CB  1 
ATOM   3057  C CG  . GLN A  1 408 ? 26.768  11.507  210.141 1.00 175.92 ?  440 GLN A CG  1 
ATOM   3058  C CD  . GLN A  1 408 ? 26.198  10.927  208.859 1.00 176.02 ?  440 GLN A CD  1 
ATOM   3059  O OE1 . GLN A  1 408 ? 25.884  11.659  207.918 1.00 175.81 ?  440 GLN A OE1 1 
ATOM   3060  N NE2 . GLN A  1 408 ? 26.049  9.607   208.820 1.00 179.86 ?  440 GLN A NE2 1 
ATOM   3061  N N   . GLY A  1 409 ? 28.796  15.746  210.057 1.00 171.43 ?  441 GLY A N   1 
ATOM   3062  C CA  . GLY A  1 409 ? 29.819  16.668  209.614 1.00 166.93 ?  441 GLY A CA  1 
ATOM   3063  C C   . GLY A  1 409 ? 29.285  18.013  209.163 1.00 163.02 ?  441 GLY A C   1 
ATOM   3064  O O   . GLY A  1 409 ? 28.091  18.218  208.939 1.00 161.20 ?  441 GLY A O   1 
ATOM   3065  N N   . VAL A  1 410 ? 30.216  18.956  209.042 1.00 162.88 ?  442 VAL A N   1 
ATOM   3066  C CA  . VAL A  1 410 ? 29.885  20.297  208.587 1.00 164.78 ?  442 VAL A CA  1 
ATOM   3067  C C   . VAL A  1 410 ? 29.564  20.246  207.101 1.00 163.08 ?  442 VAL A C   1 
ATOM   3068  O O   . VAL A  1 410 ? 30.326  19.684  206.304 1.00 161.88 ?  442 VAL A O   1 
ATOM   3069  C CB  . VAL A  1 410 ? 31.038  21.265  208.884 1.00 168.23 ?  442 VAL A CB  1 
ATOM   3070  C CG1 . VAL A  1 410 ? 30.754  22.621  208.272 1.00 168.79 ?  442 VAL A CG1 1 
ATOM   3071  C CG2 . VAL A  1 410 ? 31.262  21.381  210.387 1.00 169.09 ?  442 VAL A CG2 1 
ATOM   3072  N N   . ILE A  1 411 ? 28.428  20.820  206.719 1.00 151.02 ?  443 ILE A N   1 
ATOM   3073  C CA  . ILE A  1 411 ? 27.979  20.820  205.334 1.00 148.15 ?  443 ILE A CA  1 
ATOM   3074  C C   . ILE A  1 411 ? 28.378  22.143  204.698 1.00 148.11 ?  443 ILE A C   1 
ATOM   3075  O O   . ILE A  1 411 ? 28.092  23.213  205.247 1.00 149.85 ?  443 ILE A O   1 
ATOM   3076  C CB  . ILE A  1 411 ? 26.456  20.616  205.253 1.00 147.11 ?  443 ILE A CB  1 
ATOM   3077  C CG1 . ILE A  1 411 ? 26.029  19.390  206.066 1.00 147.68 ?  443 ILE A CG1 1 
ATOM   3078  C CG2 . ILE A  1 411 ? 26.021  20.494  203.810 1.00 144.20 ?  443 ILE A CG2 1 
ATOM   3079  C CD1 . ILE A  1 411 ? 24.542  19.114  206.022 1.00 146.89 ?  443 ILE A CD1 1 
ATOM   3080  N N   . ARG A  1 412 ? 29.035  22.074  203.537 1.00 171.66 ?  444 ARG A N   1 
ATOM   3081  C CA  . ARG A  1 412 ? 29.417  23.270  202.800 1.00 168.25 ?  444 ARG A CA  1 
ATOM   3082  C C   . ARG A  1 412 ? 28.923  23.173  201.366 1.00 167.73 ?  444 ARG A C   1 
ATOM   3083  O O   . ARG A  1 412 ? 28.995  22.111  200.741 1.00 165.89 ?  444 ARG A O   1 
ATOM   3084  C CB  . ARG A  1 412 ? 30.945  23.438  202.807 1.00 173.06 ?  444 ARG A CB  1 
ATOM   3085  C CG  . ARG A  1 412 ? 31.453  24.719  202.176 1.00 178.89 ?  444 ARG A CG  1 
ATOM   3086  C CD  . ARG A  1 412 ? 32.927  24.594  201.807 1.00 183.72 ?  444 ARG A CD  1 
ATOM   3087  N NE  . ARG A  1 412 ? 33.097  24.352  200.373 1.00 185.24 ?  444 ARG A NE  1 
ATOM   3088  C CZ  . ARG A  1 412 ? 34.270  24.333  199.745 1.00 189.56 ?  444 ARG A CZ  1 
ATOM   3089  N NH1 . ARG A  1 412 ? 35.391  24.547  200.423 1.00 191.08 1  444 ARG A NH1 1 
ATOM   3090  N NH2 . ARG A  1 412 ? 34.321  24.101  198.440 1.00 189.37 ?  444 ARG A NH2 1 
ATOM   3091  N N   . CYS A  1 413 ? 28.394  24.287  200.865 1.00 171.66 ?  445 CYS A N   1 
ATOM   3092  C CA  . CYS A  1 413 ? 27.902  24.412  199.499 1.00 170.60 ?  445 CYS A CA  1 
ATOM   3093  C C   . CYS A  1 413 ? 28.050  25.815  198.930 1.00 170.91 ?  445 CYS A C   1 
ATOM   3094  O O   . CYS A  1 413 ? 27.827  26.813  199.622 1.00 171.19 ?  445 CYS A O   1 
ATOM   3095  C CB  . CYS A  1 413 ? 26.484  23.876  199.411 1.00 171.56 ?  445 CYS A CB  1 
ATOM   3096  S SG  . CYS A  1 413 ? 25.254  24.745  200.333 1.00 181.26 ?  445 CYS A SG  1 
ATOM   3097  N N   . VAL A  1 414 ? 28.429  25.864  197.656 1.00 174.78 ?  446 VAL A N   1 
ATOM   3098  C CA  . VAL A  1 414 ? 28.589  27.091  196.886 1.00 173.49 ?  446 VAL A CA  1 
ATOM   3099  C C   . VAL A  1 414 ? 27.626  27.045  195.700 1.00 172.80 ?  446 VAL A C   1 
ATOM   3100  O O   . VAL A  1 414 ? 27.689  26.118  194.881 1.00 172.75 ?  446 VAL A O   1 
ATOM   3101  C CB  . VAL A  1 414 ? 30.045  27.277  196.428 1.00 174.83 ?  446 VAL A CB  1 
ATOM   3102  C CG1 . VAL A  1 414 ? 30.898  27.728  197.603 1.00 171.00 ?  446 VAL A CG1 1 
ATOM   3103  C CG2 . VAL A  1 414 ? 30.607  25.967  195.857 1.00 178.41 ?  446 VAL A CG2 1 
ATOM   3104  N N   . SER A  1 415 ? 26.713  28.014  195.624 1.00 175.66 ?  447 SER A N   1 
ATOM   3105  C CA  . SER A  1 415 ? 25.700  28.022  194.575 1.00 172.63 ?  447 SER A CA  1 
ATOM   3106  C C   . SER A  1 415 ? 25.770  29.323  193.776 1.00 168.42 ?  447 SER A C   1 
ATOM   3107  O O   . SER A  1 415 ? 26.526  30.242  194.097 1.00 169.04 ?  447 SER A O   1 
ATOM   3108  C CB  . SER A  1 415 ? 24.299  27.825  195.169 1.00 172.41 ?  447 SER A CB  1 
ATOM   3109  O OG  . SER A  1 415 ? 23.432  27.205  194.236 1.00 171.24 ?  447 SER A OG  1 
ATOM   3110  N N   . ASN A  1 416 ? 24.976  29.384  192.710 1.00 169.88 ?  448 ASN A N   1 
ATOM   3111  C CA  . ASN A  1 416 ? 24.875  30.551  191.840 1.00 166.34 ?  448 ASN A CA  1 
ATOM   3112  C C   . ASN A  1 416 ? 23.496  31.186  192.034 1.00 167.68 ?  448 ASN A C   1 
ATOM   3113  O O   . ASN A  1 416 ? 22.477  30.517  191.832 1.00 167.25 ?  448 ASN A O   1 
ATOM   3114  C CB  . ASN A  1 416 ? 25.120  30.097  190.402 1.00 163.55 ?  448 ASN A CB  1 
ATOM   3115  C CG  . ASN A  1 416 ? 26.607  29.962  190.078 1.00 163.01 ?  448 ASN A CG  1 
ATOM   3116  O OD1 . ASN A  1 416 ? 27.475  30.455  190.808 1.00 164.91 ?  448 ASN A OD1 1 
ATOM   3117  N ND2 . ASN A  1 416 ? 26.903  29.217  189.015 1.00 165.11 ?  448 ASN A ND2 1 
ATOM   3118  N N   . ILE A  1 417 ? 23.459  32.462  192.425 1.00 159.23 ?  449 ILE A N   1 
ATOM   3119  C CA  . ILE A  1 417 ? 22.214  33.244  192.500 1.00 160.98 ?  449 ILE A CA  1 
ATOM   3120  C C   . ILE A  1 417 ? 21.885  33.782  191.107 1.00 161.92 ?  449 ILE A C   1 
ATOM   3121  O O   . ILE A  1 417 ? 22.517  34.727  190.631 1.00 163.92 ?  449 ILE A O   1 
ATOM   3122  C CB  . ILE A  1 417 ? 22.310  34.375  193.527 1.00 161.66 ?  449 ILE A CB  1 
ATOM   3123  C CG1 . ILE A  1 417 ? 22.659  33.827  194.913 1.00 162.30 ?  449 ILE A CG1 1 
ATOM   3124  C CG2 . ILE A  1 417 ? 21.006  35.164  193.579 1.00 161.22 ?  449 ILE A CG2 1 
ATOM   3125  C CD1 . ILE A  1 417 ? 22.698  34.885  196.000 1.00 165.93 ?  449 ILE A CD1 1 
ATOM   3126  N N   . THR A  1 418 ? 20.902  33.170  190.440 1.00 159.41 ?  450 THR A N   1 
ATOM   3127  C CA  . THR A  1 418 ? 20.580  33.498  189.055 1.00 156.44 ?  450 THR A CA  1 
ATOM   3128  C C   . THR A  1 418 ? 19.214  34.170  188.846 1.00 159.88 ?  450 THR A C   1 
ATOM   3129  O O   . THR A  1 418 ? 18.798  34.325  187.694 1.00 163.58 ?  450 THR A O   1 
ATOM   3130  C CB  . THR A  1 418 ? 20.673  32.231  188.195 1.00 153.31 ?  450 THR A CB  1 
ATOM   3131  O OG1 . THR A  1 418 ? 19.691  31.285  188.627 1.00 152.39 ?  450 THR A OG1 1 
ATOM   3132  C CG2 . THR A  1 418 ? 22.062  31.578  188.317 1.00 152.80 ?  450 THR A CG2 1 
ATOM   3133  N N   . GLY A  1 419 ? 18.500  34.572  189.901 1.00 158.07 ?  451 GLY A N   1 
ATOM   3134  C CA  . GLY A  1 419 ? 17.209  35.219  189.688 1.00 158.74 ?  451 GLY A CA  1 
ATOM   3135  C C   . GLY A  1 419 ? 16.391  35.468  190.943 1.00 161.05 ?  451 GLY A C   1 
ATOM   3136  O O   . GLY A  1 419 ? 16.681  34.886  191.992 1.00 161.10 ?  451 GLY A O   1 
ATOM   3137  N N   . LEU A  1 420 ? 15.366  36.327  190.851 1.00 141.75 ?  452 LEU A N   1 
ATOM   3138  C CA  . LEU A  1 420 ? 14.514  36.675  191.985 1.00 144.79 ?  452 LEU A CA  1 
ATOM   3139  C C   . LEU A  1 420 ? 13.029  36.517  191.660 1.00 149.42 ?  452 LEU A C   1 
ATOM   3140  O O   . LEU A  1 420 ? 12.624  36.520  190.494 1.00 154.13 ?  452 LEU A O   1 
ATOM   3141  C CB  . LEU A  1 420 ? 14.786  38.116  192.417 1.00 146.56 ?  452 LEU A CB  1 
ATOM   3142  C CG  . LEU A  1 420 ? 16.273  38.450  192.537 1.00 146.92 ?  452 LEU A CG  1 
ATOM   3143  C CD1 . LEU A  1 420 ? 16.480  39.907  192.901 1.00 158.26 ?  452 LEU A CD1 1 
ATOM   3144  C CD2 . LEU A  1 420 ? 16.937  37.549  193.567 1.00 148.28 ?  452 LEU A CD2 1 
ATOM   3145  N N   . ILE A  1 421 ? 12.216  36.390  192.723 1.00 138.51 ?  453 ILE A N   1 
ATOM   3146  C CA  . ILE A  1 421 ? 10.748  36.370  192.641 1.00 142.16 ?  453 ILE A CA  1 
ATOM   3147  C C   . ILE A  1 421 ? 10.192  37.514  193.491 1.00 150.32 ?  453 ILE A C   1 
ATOM   3148  O O   . ILE A  1 421 ? 10.070  37.378  194.715 1.00 155.80 ?  453 ILE A O   1 
ATOM   3149  C CB  . ILE A  1 421 ? 10.167  35.029  193.107 1.00 140.12 ?  453 ILE A CB  1 
ATOM   3150  C CG1 . ILE A  1 421 ? 10.735  33.873  192.289 1.00 134.28 ?  453 ILE A CG1 1 
ATOM   3151  C CG2 . ILE A  1 421 ? 8.644   35.033  193.006 1.00 145.06 ?  453 ILE A CG2 1 
ATOM   3152  C CD1 . ILE A  1 421 ? 10.151  32.526  192.657 1.00 133.25 ?  453 ILE A CD1 1 
ATOM   3153  N N   . LEU A  1 422 ? 9.846   38.638  192.863 1.00 142.39 ?  454 LEU A N   1 
ATOM   3154  C CA  . LEU A  1 422 ? 9.404   39.837  193.567 1.00 149.51 ?  454 LEU A CA  1 
ATOM   3155  C C   . LEU A  1 422 ? 7.903   40.087  193.461 1.00 152.64 ?  454 LEU A C   1 
ATOM   3156  O O   . LEU A  1 422 ? 7.242   39.661  192.507 1.00 151.17 ?  454 LEU A O   1 
ATOM   3157  C CB  . LEU A  1 422 ? 10.146  41.091  193.095 1.00 155.45 ?  454 LEU A CB  1 
ATOM   3158  C CG  . LEU A  1 422 ? 11.666  41.048  193.162 1.00 154.71 ?  454 LEU A CG  1 
ATOM   3159  C CD1 . LEU A  1 422 ? 12.236  42.364  192.667 1.00 165.26 ?  454 LEU A CD1 1 
ATOM   3160  C CD2 . LEU A  1 422 ? 12.086  40.780  194.603 1.00 153.18 ?  454 LEU A CD2 1 
ATOM   3161  N N   . THR A  1 423 ? 7.378   40.783  194.474 1.00 158.25 ?  455 THR A N   1 
ATOM   3162  C CA  . THR A  1 423 ? 5.989   41.216  194.545 1.00 166.33 ?  455 THR A CA  1 
ATOM   3163  C C   . THR A  1 423 ? 5.987   42.701  194.890 1.00 176.29 ?  455 THR A C   1 
ATOM   3164  O O   . THR A  1 423 ? 6.841   43.184  195.638 1.00 178.70 ?  455 THR A O   1 
ATOM   3165  C CB  . THR A  1 423 ? 5.153   40.416  195.573 1.00 163.89 ?  455 THR A CB  1 
ATOM   3166  O OG1 . THR A  1 423 ? 5.744   40.507  196.876 1.00 169.01 ?  455 THR A OG1 1 
ATOM   3167  C CG2 . THR A  1 423 ? 5.038   38.960  195.160 1.00 161.57 ?  455 THR A CG2 1 
ATOM   3168  N N   . ARG A  1 424 ? 5.014   43.419  194.339 1.00 186.73 ?  456 ARG A N   1 
ATOM   3169  C CA  . ARG A  1 424 ? 4.883   44.859  194.506 1.00 194.25 ?  456 ARG A CA  1 
ATOM   3170  C C   . ARG A  1 424 ? 3.715   45.198  195.420 1.00 205.00 ?  456 ARG A C   1 
ATOM   3171  O O   . ARG A  1 424 ? 2.691   44.509  195.417 1.00 207.10 ?  456 ARG A O   1 
ATOM   3172  C CB  . ARG A  1 424 ? 4.707   45.541  193.150 1.00 189.96 ?  456 ARG A CB  1 
ATOM   3173  C CG  . ARG A  1 424 ? 4.801   47.050  193.183 1.00 199.12 ?  456 ARG A CG  1 
ATOM   3174  C CD  . ARG A  1 424 ? 4.925   47.580  191.774 1.00 200.86 ?  456 ARG A CD  1 
ATOM   3175  N NE  . ARG A  1 424 ? 3.809   47.142  190.942 1.00 195.60 ?  456 ARG A NE  1 
ATOM   3176  C CZ  . ARG A  1 424 ? 2.679   47.818  190.766 1.00 201.22 ?  456 ARG A CZ  1 
ATOM   3177  N NH1 . ARG A  1 424 ? 2.488   48.987  191.365 1.00 211.60 1  456 ARG A NH1 1 
ATOM   3178  N NH2 . ARG A  1 424 ? 1.733   47.318  189.984 1.00 204.61 ?  456 ARG A NH2 1 
ATOM   3179  N N   . ASP A  1 425 ? 3.882   46.251  196.216 1.00 201.41 ?  457 ASP A N   1 
ATOM   3180  C CA  . ASP A  1 425 ? 2.848   46.651  197.153 1.00 210.68 ?  457 ASP A CA  1 
ATOM   3181  C C   . ASP A  1 425 ? 1.738   47.406  196.420 1.00 218.69 ?  457 ASP A C   1 
ATOM   3182  O O   . ASP A  1 425 ? 1.894   47.846  195.279 1.00 213.88 ?  457 ASP A O   1 
ATOM   3183  C CB  . ASP A  1 425 ? 3.450   47.519  198.258 1.00 215.27 ?  457 ASP A CB  1 
ATOM   3184  C CG  . ASP A  1 425 ? 4.456   46.764  199.103 1.00 208.80 ?  457 ASP A CG  1 
ATOM   3185  O OD1 . ASP A  1 425 ? 4.047   46.131  200.098 1.00 211.96 ?  457 ASP A OD1 1 
ATOM   3186  O OD2 . ASP A  1 425 ? 5.658   46.793  198.761 1.00 203.11 -1 457 ASP A OD2 1 
ATOM   3187  N N   . GLY A  1 426 ? 0.604   47.561  197.101 1.00 223.54 ?  458 GLY A N   1 
ATOM   3188  C CA  . GLY A  1 426 ? -0.549  48.237  196.534 1.00 232.73 ?  458 GLY A CA  1 
ATOM   3189  C C   . GLY A  1 426 ? -0.717  49.666  197.005 1.00 249.05 ?  458 GLY A C   1 
ATOM   3190  O O   . GLY A  1 426 ? -1.523  50.423  196.457 1.00 256.82 ?  458 GLY A O   1 
ATOM   3191  N N   . GLY A  1 427 ? 0.055   50.042  198.018 1.00 260.64 ?  459 GLY A N   1 
ATOM   3192  C CA  . GLY A  1 427 ? 0.037   51.386  198.560 1.00 267.97 ?  459 GLY A CA  1 
ATOM   3193  C C   . GLY A  1 427 ? 0.464   52.427  197.551 1.00 275.12 ?  459 GLY A C   1 
ATOM   3194  O O   . GLY A  1 427 ? 1.637   52.481  197.167 1.00 268.81 ?  459 GLY A O   1 
ATOM   3195  N N   . SER A  1 428 ? -0.477  53.251  197.096 1.00 270.46 ?  460 SER A N   1 
ATOM   3196  C CA  . SER A  1 428 ? -0.185  54.184  196.018 1.00 272.74 ?  460 SER A CA  1 
ATOM   3197  C C   . SER A  1 428 ? -1.109  55.409  195.975 1.00 284.91 ?  460 SER A C   1 
ATOM   3198  O O   . SER A  1 428 ? -2.316  55.261  196.170 1.00 289.82 ?  460 SER A O   1 
ATOM   3199  C CB  . SER A  1 428 ? -0.299  53.452  194.671 1.00 263.28 ?  460 SER A CB  1 
ATOM   3200  O OG  . SER A  1 428 ? 0.231   52.138  194.713 1.00 251.79 ?  460 SER A OG  1 
ATOM   3201  N N   . THR A  1 429 ? -0.589  56.627  195.739 1.00 272.97 ?  461 THR A N   1 
ATOM   3202  C CA  . THR A  1 429 ? 0.837   57.004  195.576 1.00 270.06 ?  461 THR A CA  1 
ATOM   3203  C C   . THR A  1 429 ? 1.582   56.137  194.538 1.00 263.17 ?  461 THR A C   1 
ATOM   3204  O O   . THR A  1 429 ? 2.583   55.476  194.844 1.00 259.65 ?  461 THR A O   1 
ATOM   3205  C CB  . THR A  1 429 ? 1.542   56.956  196.976 1.00 268.17 ?  461 THR A CB  1 
ATOM   3206  O OG1 . THR A  1 429 ? 0.797   57.745  197.902 1.00 274.92 ?  461 THR A OG1 1 
ATOM   3207  C CG2 . THR A  1 429 ? 2.893   57.588  196.920 1.00 263.17 ?  461 THR A CG2 1 
ATOM   3208  N N   . ASN A  1 430 ? 1.054   56.088  193.313 1.00 283.43 ?  462 ASN A N   1 
ATOM   3209  C CA  . ASN A  1 430 ? 1.617   55.164  192.336 1.00 265.21 ?  462 ASN A CA  1 
ATOM   3210  C C   . ASN A  1 430 ? 2.704   55.813  191.487 1.00 263.85 ?  462 ASN A C   1 
ATOM   3211  O O   . ASN A  1 430 ? 3.742   55.195  191.225 1.00 256.50 ?  462 ASN A O   1 
ATOM   3212  C CB  . ASN A  1 430 ? 0.494   54.619  191.443 1.00 263.02 ?  462 ASN A CB  1 
ATOM   3213  C CG  . ASN A  1 430 ? 0.965   53.511  190.509 1.00 254.17 ?  462 ASN A CG  1 
ATOM   3214  O OD1 . ASN A  1 430 ? 1.713   52.621  190.913 1.00 244.96 ?  462 ASN A OD1 1 
ATOM   3215  N ND2 . ASN A  1 430 ? 0.485   53.533  189.268 1.00 252.69 ?  462 ASN A ND2 1 
ATOM   3216  N N   . SER A  1 431 ? 2.484   57.053  191.053 1.00 263.90 ?  463 SER A N   1 
ATOM   3217  C CA  . SER A  1 431 ? 3.404   57.775  190.179 1.00 261.56 ?  463 SER A CA  1 
ATOM   3218  C C   . SER A  1 431 ? 4.633   58.326  190.895 1.00 262.93 ?  463 SER A C   1 
ATOM   3219  O O   . SER A  1 431 ? 5.422   59.029  190.256 1.00 263.09 ?  463 SER A O   1 
ATOM   3220  C CB  . SER A  1 431 ? 2.668   58.908  189.461 1.00 262.84 ?  463 SER A CB  1 
ATOM   3221  O OG  . SER A  1 431 ? 1.613   58.409  188.656 1.00 258.10 ?  463 SER A OG  1 
ATOM   3222  N N   . THR A  1 432 ? 4.823   58.037  192.185 1.00 242.21 ?  464 THR A N   1 
ATOM   3223  C CA  . THR A  1 432 ? 5.973   58.561  192.918 1.00 237.10 ?  464 THR A CA  1 
ATOM   3224  C C   . THR A  1 432 ? 7.051   57.494  193.055 1.00 229.97 ?  464 THR A C   1 
ATOM   3225  O O   . THR A  1 432 ? 7.977   57.425  192.240 1.00 225.92 ?  464 THR A O   1 
ATOM   3226  C CB  . THR A  1 432 ? 5.556   59.037  194.312 1.00 242.75 ?  464 THR A CB  1 
ATOM   3227  O OG1 . THR A  1 432 ? 5.274   57.898  195.132 1.00 241.85 ?  464 THR A OG1 1 
ATOM   3228  C CG2 . THR A  1 432 ? 4.292   59.888  194.232 1.00 249.65 ?  464 THR A CG2 1 
ATOM   3229  N N   . THR A  1 433 ? 6.948   56.663  194.083 1.00 236.62 ?  465 THR A N   1 
ATOM   3230  C CA  . THR A  1 433 ? 7.936   55.630  194.336 1.00 225.88 ?  465 THR A CA  1 
ATOM   3231  C C   . THR A  1 433 ? 7.226   54.284  194.350 1.00 221.54 ?  465 THR A C   1 
ATOM   3232  O O   . THR A  1 433 ? 6.012   54.204  194.558 1.00 227.95 ?  465 THR A O   1 
ATOM   3233  C CB  . THR A  1 433 ? 8.672   55.866  195.660 1.00 224.12 ?  465 THR A CB  1 
ATOM   3234  O OG1 . THR A  1 433 ? 9.569   54.776  195.911 1.00 212.79 ?  465 THR A OG1 1 
ATOM   3235  C CG2 . THR A  1 433 ? 7.676   55.986  196.808 1.00 225.45 ?  465 THR A CG2 1 
ATOM   3236  N N   . GLU A  1 434 ? 7.996   53.221  194.128 1.00 225.66 ?  466 GLU A N   1 
ATOM   3237  C CA  . GLU A  1 434 ? 7.465   51.866  194.115 1.00 216.79 ?  466 GLU A CA  1 
ATOM   3238  C C   . GLU A  1 434 ? 8.337   50.985  194.998 1.00 208.91 ?  466 GLU A C   1 
ATOM   3239  O O   . GLU A  1 434 ? 9.568   51.087  194.968 1.00 206.27 ?  466 GLU A O   1 
ATOM   3240  C CB  . GLU A  1 434 ? 7.423   51.317  192.683 1.00 210.12 ?  466 GLU A CB  1 
ATOM   3241  C CG  . GLU A  1 434 ? 6.512   52.095  191.724 1.00 218.31 ?  466 GLU A CG  1 
ATOM   3242  C CD  . GLU A  1 434 ? 5.026   51.921  191.993 1.00 225.39 ?  466 GLU A CD  1 
ATOM   3243  O OE1 . GLU A  1 434 ? 4.644   51.010  192.758 1.00 222.12 ?  466 GLU A OE1 1 
ATOM   3244  O OE2 . GLU A  1 434 ? 4.233   52.700  191.423 1.00 234.98 -1 466 GLU A OE2 1 
ATOM   3245  N N   . THR A  1 435 ? 7.693   50.119  195.777 1.00 208.96 ?  467 THR A N   1 
ATOM   3246  C CA  . THR A  1 435 ? 8.376   49.216  196.695 1.00 203.81 ?  467 THR A CA  1 
ATOM   3247  C C   . THR A  1 435 ? 8.215   47.770  196.249 1.00 195.18 ?  467 THR A C   1 
ATOM   3248  O O   . THR A  1 435 ? 7.107   47.335  195.920 1.00 195.60 ?  467 THR A O   1 
ATOM   3249  C CB  . THR A  1 435 ? 7.830   49.386  198.112 1.00 210.68 ?  467 THR A CB  1 
ATOM   3250  O OG1 . THR A  1 435 ? 7.976   50.754  198.508 1.00 222.68 ?  467 THR A OG1 1 
ATOM   3251  C CG2 . THR A  1 435 ? 8.593   48.504  199.086 1.00 206.85 ?  467 THR A CG2 1 
ATOM   3252  N N   . PHE A  1 436 ? 9.323   47.036  196.244 1.00 195.50 ?  468 PHE A N   1 
ATOM   3253  C CA  . PHE A  1 436 ? 9.359   45.638  195.843 1.00 186.47 ?  468 PHE A CA  1 
ATOM   3254  C C   . PHE A  1 436 ? 9.834   44.775  197.005 1.00 186.94 ?  468 PHE A C   1 
ATOM   3255  O O   . PHE A  1 436 ? 10.799  45.126  197.694 1.00 188.85 ?  468 PHE A O   1 
ATOM   3256  C CB  . PHE A  1 436 ? 10.252  45.469  194.624 1.00 181.76 ?  468 PHE A CB  1 
ATOM   3257  C CG  . PHE A  1 436 ? 9.749   46.207  193.420 1.00 183.70 ?  468 PHE A CG  1 
ATOM   3258  C CD1 . PHE A  1 436 ? 8.844   45.614  192.557 1.00 182.26 ?  468 PHE A CD1 1 
ATOM   3259  C CD2 . PHE A  1 436 ? 10.153  47.509  193.173 1.00 192.14 ?  468 PHE A CD2 1 
ATOM   3260  C CE1 . PHE A  1 436 ? 8.370   46.297  191.453 1.00 185.71 ?  468 PHE A CE1 1 
ATOM   3261  C CE2 . PHE A  1 436 ? 9.682   48.198  192.071 1.00 197.88 ?  468 PHE A CE2 1 
ATOM   3262  C CZ  . PHE A  1 436 ? 8.789   47.591  191.210 1.00 193.87 ?  468 PHE A CZ  1 
ATOM   3263  N N   . ARG A  1 437 ? 9.153   43.649  197.219 1.00 185.91 ?  469 ARG A N   1 
ATOM   3264  C CA  . ARG A  1 437 ? 9.437   42.716  198.300 1.00 184.29 ?  469 ARG A CA  1 
ATOM   3265  C C   . ARG A  1 437 ? 9.569   41.287  197.792 1.00 176.69 ?  469 ARG A C   1 
ATOM   3266  O O   . ARG A  1 437 ? 8.969   40.922  196.775 1.00 173.33 ?  469 ARG A O   1 
ATOM   3267  C CB  . ARG A  1 437 ? 8.345   42.774  199.379 1.00 187.05 ?  469 ARG A CB  1 
ATOM   3268  C CG  . ARG A  1 437 ? 8.130   44.158  199.948 1.00 194.67 ?  469 ARG A CG  1 
ATOM   3269  C CD  . ARG A  1 437 ? 6.935   44.203  200.870 1.00 201.66 ?  469 ARG A CD  1 
ATOM   3270  N NE  . ARG A  1 437 ? 6.642   45.572  201.276 1.00 216.35 ?  469 ARG A NE  1 
ATOM   3271  C CZ  . ARG A  1 437 ? 7.102   46.123  202.394 1.00 223.85 ?  469 ARG A CZ  1 
ATOM   3272  N NH1 . ARG A  1 437 ? 7.874   45.419  203.212 1.00 218.03 1  469 ARG A NH1 1 
ATOM   3273  N NH2 . ARG A  1 437 ? 6.793   47.377  202.697 1.00 234.28 ?  469 ARG A NH2 1 
ATOM   3274  N N   . PRO A  1 438 ? 10.349  40.455  198.488 1.00 175.16 ?  470 PRO A N   1 
ATOM   3275  C CA  . PRO A  1 438 ? 10.493  39.055  198.072 1.00 165.65 ?  470 PRO A CA  1 
ATOM   3276  C C   . PRO A  1 438 ? 9.225   38.253  198.316 1.00 165.50 ?  470 PRO A C   1 
ATOM   3277  O O   . PRO A  1 438 ? 8.557   38.400  199.341 1.00 167.52 ?  470 PRO A O   1 
ATOM   3278  C CB  . PRO A  1 438 ? 11.643  38.544  198.948 1.00 158.81 ?  470 PRO A CB  1 
ATOM   3279  C CG  . PRO A  1 438 ? 11.586  39.407  200.164 1.00 168.76 ?  470 PRO A CG  1 
ATOM   3280  C CD  . PRO A  1 438 ? 11.185  40.764  199.662 1.00 176.37 ?  470 PRO A CD  1 
ATOM   3281  N N   . GLY A  1 439 ? 8.898   37.398  197.353 1.00 172.38 ?  471 GLY A N   1 
ATOM   3282  C CA  . GLY A  1 439 ? 7.722   36.562  197.465 1.00 171.84 ?  471 GLY A CA  1 
ATOM   3283  C C   . GLY A  1 439 ? 8.003   35.122  197.095 1.00 165.31 ?  471 GLY A C   1 
ATOM   3284  O O   . GLY A  1 439 ? 9.153   34.675  197.110 1.00 162.48 ?  471 GLY A O   1 
ATOM   3285  N N   . GLY A  1 440 ? 6.955   34.381  196.766 1.00 161.45 ?  472 GLY A N   1 
ATOM   3286  C CA  . GLY A  1 440 ? 7.135   32.997  196.397 1.00 157.41 ?  472 GLY A CA  1 
ATOM   3287  C C   . GLY A  1 440 ? 5.879   32.193  196.630 1.00 158.32 ?  472 GLY A C   1 
ATOM   3288  O O   . GLY A  1 440 ? 4.833   32.461  196.033 1.00 159.78 ?  472 GLY A O   1 
ATOM   3289  N N   . GLY A  1 441 ? 5.984   31.199  197.505 1.00 186.61 ?  473 GLY A N   1 
ATOM   3290  C CA  . GLY A  1 441 ? 4.880   30.327  197.838 1.00 187.36 ?  473 GLY A CA  1 
ATOM   3291  C C   . GLY A  1 441 ? 4.645   29.288  196.766 1.00 183.91 ?  473 GLY A C   1 
ATOM   3292  O O   . GLY A  1 441 ? 5.000   28.117  196.935 1.00 183.11 ?  473 GLY A O   1 
ATOM   3293  N N   . ASP A  1 442 ? 4.027   29.703  195.665 1.00 187.48 ?  474 ASP A N   1 
ATOM   3294  C CA  . ASP A  1 442 ? 3.762   28.797  194.555 1.00 184.36 ?  474 ASP A CA  1 
ATOM   3295  C C   . ASP A  1 442 ? 5.064   28.411  193.863 1.00 180.30 ?  474 ASP A C   1 
ATOM   3296  O O   . ASP A  1 442 ? 5.712   29.253  193.232 1.00 179.86 ?  474 ASP A O   1 
ATOM   3297  C CB  . ASP A  1 442 ? 2.801   29.451  193.568 1.00 185.85 ?  474 ASP A CB  1 
ATOM   3298  C CG  . ASP A  1 442 ? 2.128   28.446  192.658 1.00 183.75 ?  474 ASP A CG  1 
ATOM   3299  O OD1 . ASP A  1 442 ? 1.957   27.282  193.083 1.00 182.58 ?  474 ASP A OD1 1 
ATOM   3300  O OD2 . ASP A  1 442 ? 1.770   28.819  191.521 1.00 183.57 -1 474 ASP A OD2 1 
ATOM   3301  N N   . MET A  1 443 ? 5.451   27.142  193.977 1.00 180.77 ?  475 MET A N   1 
ATOM   3302  C CA  . MET A  1 443 ? 6.692   26.671  193.377 1.00 174.25 ?  475 MET A CA  1 
ATOM   3303  C C   . MET A  1 443 ? 6.559   26.515  191.870 1.00 168.60 ?  475 MET A C   1 
ATOM   3304  O O   . MET A  1 443 ? 7.558   26.237  191.198 1.00 161.75 ?  475 MET A O   1 
ATOM   3305  C CB  . MET A  1 443 ? 7.154   25.350  193.998 1.00 170.30 ?  475 MET A CB  1 
ATOM   3306  C CG  . MET A  1 443 ? 7.230   25.326  195.517 1.00 169.27 ?  475 MET A CG  1 
ATOM   3307  S SD  . MET A  1 443 ? 8.357   26.587  196.147 1.00 191.25 ?  475 MET A SD  1 
ATOM   3308  C CE  . MET A  1 443 ? 8.212   26.359  197.921 1.00 193.80 ?  475 MET A CE  1 
ATOM   3309  N N   . ARG A  1 444 ? 5.344   26.673  191.336 1.00 166.65 ?  476 ARG A N   1 
ATOM   3310  C CA  . ARG A  1 444 ? 5.123   26.558  189.898 1.00 154.86 ?  476 ARG A CA  1 
ATOM   3311  C C   . ARG A  1 444 ? 5.836   27.677  189.162 1.00 154.71 ?  476 ARG A C   1 
ATOM   3312  O O   . ARG A  1 444 ? 6.188   27.532  187.987 1.00 151.86 ?  476 ARG A O   1 
ATOM   3313  C CB  . ARG A  1 444 ? 3.627   26.608  189.612 1.00 153.58 ?  476 ARG A CB  1 
ATOM   3314  C CG  . ARG A  1 444 ? 2.859   25.422  190.143 1.00 158.59 ?  476 ARG A CG  1 
ATOM   3315  C CD  . ARG A  1 444 ? 1.378   25.665  189.972 1.00 167.29 ?  476 ARG A CD  1 
ATOM   3316  N NE  . ARG A  1 444 ? 0.579   24.592  190.545 1.00 179.32 ?  476 ARG A NE  1 
ATOM   3317  C CZ  . ARG A  1 444 ? -0.316  24.784  191.511 1.00 186.64 ?  476 ARG A CZ  1 
ATOM   3318  N NH1 . ARG A  1 444 ? -0.511  26.002  191.998 1.00 185.95 1  476 ARG A NH1 1 
ATOM   3319  N NH2 . ARG A  1 444 ? -1.010  23.761  191.994 1.00 191.44 ?  476 ARG A NH2 1 
ATOM   3320  N N   . ASP A  1 445 ? 6.064   28.791  189.852 1.00 161.15 ?  477 ASP A N   1 
ATOM   3321  C CA  . ASP A  1 445 ? 6.778   29.916  189.274 1.00 163.00 ?  477 ASP A CA  1 
ATOM   3322  C C   . ASP A  1 445 ? 8.230   29.537  189.014 1.00 156.63 ?  477 ASP A C   1 
ATOM   3323  O O   . ASP A  1 445 ? 8.841   30.014  188.051 1.00 155.21 ?  477 ASP A O   1 
ATOM   3324  C CB  . ASP A  1 445 ? 6.712   31.115  190.221 1.00 172.69 ?  477 ASP A CB  1 
ATOM   3325  C CG  . ASP A  1 445 ? 5.287   31.512  190.575 1.00 177.68 ?  477 ASP A CG  1 
ATOM   3326  O OD1 . ASP A  1 445 ? 4.397   31.433  189.701 1.00 174.99 ?  477 ASP A OD1 1 
ATOM   3327  O OD2 . ASP A  1 445 ? 5.061   31.911  191.738 1.00 180.13 -1 477 ASP A OD2 1 
ATOM   3328  N N   . ASN A  1 446 ? 8.786   28.674  189.870 1.00 160.90 ?  478 ASN A N   1 
ATOM   3329  C CA  . ASN A  1 446 ? 10.179  28.253  189.761 1.00 156.40 ?  478 ASN A CA  1 
ATOM   3330  C C   . ASN A  1 446 ? 10.470  27.509  188.465 1.00 148.90 ?  478 ASN A C   1 
ATOM   3331  O O   . ASN A  1 446 ? 11.592  27.576  187.951 1.00 146.45 ?  478 ASN A O   1 
ATOM   3332  C CB  . ASN A  1 446 ? 10.513  27.325  190.925 1.00 157.83 ?  478 ASN A CB  1 
ATOM   3333  C CG  . ASN A  1 446 ? 10.341  27.985  192.264 1.00 165.93 ?  478 ASN A CG  1 
ATOM   3334  O OD1 . ASN A  1 446 ? 9.650   28.997  192.386 1.00 167.97 ?  478 ASN A OD1 1 
ATOM   3335  N ND2 . ASN A  1 446 ? 10.918  27.383  193.293 1.00 169.97 ?  478 ASN A ND2 1 
ATOM   3336  N N   . TRP A  1 447 ? 9.478   26.811  187.915 1.00 149.21 ?  479 TRP A N   1 
ATOM   3337  C CA  . TRP A  1 447 ? 9.674   26.069  186.675 1.00 148.55 ?  479 TRP A CA  1 
ATOM   3338  C C   . TRP A  1 447 ? 9.548   26.988  185.473 1.00 146.05 ?  479 TRP A C   1 
ATOM   3339  O O   . TRP A  1 447 ? 10.137  26.730  184.418 1.00 143.57 ?  479 TRP A O   1 
ATOM   3340  C CB  . TRP A  1 447 ? 8.655   24.931  186.580 1.00 150.80 ?  479 TRP A CB  1 
ATOM   3341  C CG  . TRP A  1 447 ? 8.351   24.307  187.909 1.00 152.85 ?  479 TRP A CG  1 
ATOM   3342  C CD1 . TRP A  1 447 ? 7.123   24.202  188.493 1.00 155.19 ?  479 TRP A CD1 1 
ATOM   3343  C CD2 . TRP A  1 447 ? 9.289   23.786  188.859 1.00 149.24 ?  479 TRP A CD2 1 
ATOM   3344  N NE1 . TRP A  1 447 ? 7.231   23.615  189.727 1.00 153.31 ?  479 TRP A NE1 1 
ATOM   3345  C CE2 . TRP A  1 447 ? 8.551   23.352  189.978 1.00 151.03 ?  479 TRP A CE2 1 
ATOM   3346  C CE3 . TRP A  1 447 ? 10.678  23.628  188.866 1.00 144.91 ?  479 TRP A CE3 1 
ATOM   3347  C CZ2 . TRP A  1 447 ? 9.153   22.772  191.090 1.00 154.65 ?  479 TRP A CZ2 1 
ATOM   3348  C CZ3 . TRP A  1 447 ? 11.273  23.053  189.969 1.00 146.55 ?  479 TRP A CZ3 1 
ATOM   3349  C CH2 . TRP A  1 447 ? 10.512  22.633  191.067 1.00 153.14 ?  479 TRP A CH2 1 
ATOM   3350  N N   . ARG A  1 448 ? 8.785   28.062  185.634 1.00 142.58 ?  480 ARG A N   1 
ATOM   3351  C CA  . ARG A  1 448 ? 8.521   29.021  184.577 1.00 145.29 ?  480 ARG A CA  1 
ATOM   3352  C C   . ARG A  1 448 ? 9.776   29.790  184.190 1.00 145.55 ?  480 ARG A C   1 
ATOM   3353  O O   . ARG A  1 448 ? 9.835   30.344  183.087 1.00 148.23 ?  480 ARG A O   1 
ATOM   3354  C CB  . ARG A  1 448 ? 7.447   29.966  185.094 1.00 150.14 ?  480 ARG A CB  1 
ATOM   3355  C CG  . ARG A  1 448 ? 6.154   29.226  185.347 1.00 151.60 ?  480 ARG A CG  1 
ATOM   3356  C CD  . ARG A  1 448 ? 4.995   30.125  185.701 1.00 159.15 ?  480 ARG A CD  1 
ATOM   3357  N NE  . ARG A  1 448 ? 3.803   29.325  185.971 1.00 161.07 ?  480 ARG A NE  1 
ATOM   3358  C CZ  . ARG A  1 448 ? 2.765   29.739  186.692 1.00 168.07 ?  480 ARG A CZ  1 
ATOM   3359  N NH1 . ARG A  1 448 ? 2.758   30.955  187.225 1.00 173.24 1  480 ARG A NH1 1 
ATOM   3360  N NH2 . ARG A  1 448 ? 1.733   28.932  186.891 1.00 169.30 ?  480 ARG A NH2 1 
ATOM   3361  N N   . SER A  1 449 ? 10.779  29.822  185.074 1.00 152.37 ?  481 SER A N   1 
ATOM   3362  C CA  . SER A  1 449 ? 12.031  30.530  184.836 1.00 154.87 ?  481 SER A CA  1 
ATOM   3363  C C   . SER A  1 449 ? 12.963  29.779  183.897 1.00 152.79 ?  481 SER A C   1 
ATOM   3364  O O   . SER A  1 449 ? 13.986  30.335  183.482 1.00 155.66 ?  481 SER A O   1 
ATOM   3365  C CB  . SER A  1 449 ? 12.747  30.771  186.166 1.00 155.29 ?  481 SER A CB  1 
ATOM   3366  O OG  . SER A  1 449 ? 13.096  29.539  186.776 1.00 150.71 ?  481 SER A OG  1 
ATOM   3367  N N   . GLU A  1 450 ? 12.626  28.542  183.551 1.00 150.36 ?  482 GLU A N   1 
ATOM   3368  C CA  . GLU A  1 450 ? 13.423  27.713  182.664 1.00 148.70 ?  482 GLU A CA  1 
ATOM   3369  C C   . GLU A  1 450 ? 12.625  27.240  181.469 1.00 145.22 ?  482 GLU A C   1 
ATOM   3370  O O   . GLU A  1 450 ? 13.223  26.886  180.447 1.00 143.41 ?  482 GLU A O   1 
ATOM   3371  C CB  . GLU A  1 450 ? 13.996  26.498  183.409 1.00 146.24 ?  482 GLU A CB  1 
ATOM   3372  C CG  . GLU A  1 450 ? 14.884  26.871  184.581 1.00 145.80 ?  482 GLU A CG  1 
ATOM   3373  C CD  . GLU A  1 450 ? 16.135  27.620  184.153 1.00 151.00 ?  482 GLU A CD  1 
ATOM   3374  O OE1 . GLU A  1 450 ? 16.615  27.395  183.020 1.00 154.11 ?  482 GLU A OE1 1 
ATOM   3375  O OE2 . GLU A  1 450 ? 16.629  28.448  184.948 1.00 150.34 -1 482 GLU A OE2 1 
ATOM   3376  N N   . LEU A  1 451 ? 11.298  27.223  181.575 1.00 136.80 ?  483 LEU A N   1 
ATOM   3377  C CA  . LEU A  1 451 ? 10.412  26.783  180.514 1.00 136.36 ?  483 LEU A CA  1 
ATOM   3378  C C   . LEU A  1 451 ? 9.802   27.968  179.782 1.00 138.13 ?  483 LEU A C   1 
ATOM   3379  O O   . LEU A  1 451 ? 8.792   27.817  179.084 1.00 138.73 ?  483 LEU A O   1 
ATOM   3380  C CB  . LEU A  1 451 ? 9.311   25.900  181.100 1.00 132.81 ?  483 LEU A CB  1 
ATOM   3381  C CG  . LEU A  1 451 ? 9.785   24.557  181.650 1.00 129.44 ?  483 LEU A CG  1 
ATOM   3382  C CD1 . LEU A  1 451 ? 8.638   23.816  182.315 1.00 129.97 ?  483 LEU A CD1 1 
ATOM   3383  C CD2 . LEU A  1 451 ? 10.411  23.717  180.554 1.00 130.89 ?  483 LEU A CD2 1 
ATOM   3384  N N   . TYR A  1 452 ? 10.400  29.152  179.935 1.00 136.08 ?  484 TYR A N   1 
ATOM   3385  C CA  . TYR A  1 452 ? 9.865   30.340  179.292 1.00 138.61 ?  484 TYR A CA  1 
ATOM   3386  C C   . TYR A  1 452 ? 10.148  30.342  177.802 1.00 138.39 ?  484 TYR A C   1 
ATOM   3387  O O   . TYR A  1 452 ? 9.445   31.016  177.044 1.00 140.40 ?  484 TYR A O   1 
ATOM   3388  C CB  . TYR A  1 452 ? 10.479  31.578  179.957 1.00 140.01 ?  484 TYR A CB  1 
ATOM   3389  C CG  . TYR A  1 452 ? 11.950  31.778  179.622 1.00 138.79 ?  484 TYR A CG  1 
ATOM   3390  C CD1 . TYR A  1 452 ? 12.933  31.128  180.360 1.00 136.69 ?  484 TYR A CD1 1 
ATOM   3391  C CD2 . TYR A  1 452 ? 12.358  32.617  178.591 1.00 139.96 ?  484 TYR A CD2 1 
ATOM   3392  C CE1 . TYR A  1 452 ? 14.276  31.290  180.074 1.00 135.86 ?  484 TYR A CE1 1 
ATOM   3393  C CE2 . TYR A  1 452 ? 13.705  32.787  178.297 1.00 140.78 ?  484 TYR A CE2 1 
ATOM   3394  C CZ  . TYR A  1 452 ? 14.657  32.122  179.042 1.00 137.08 ?  484 TYR A CZ  1 
ATOM   3395  O OH  . TYR A  1 452 ? 15.991  32.294  178.747 1.00 137.76 ?  484 TYR A OH  1 
ATOM   3396  N N   . LYS A  1 453 ? 11.158  29.592  177.371 1.00 132.51 ?  485 LYS A N   1 
ATOM   3397  C CA  . LYS A  1 453 ? 11.573  29.530  175.978 1.00 130.00 ?  485 LYS A CA  1 
ATOM   3398  C C   . LYS A  1 453 ? 11.176  28.221  175.294 1.00 127.08 ?  485 LYS A C   1 
ATOM   3399  O O   . LYS A  1 453 ? 11.734  27.888  174.245 1.00 134.35 ?  485 LYS A O   1 
ATOM   3400  C CB  . LYS A  1 453 ? 13.066  29.848  175.857 1.00 131.86 ?  485 LYS A CB  1 
ATOM   3401  C CG  . LYS A  1 453 ? 14.031  29.036  176.690 1.00 129.20 ?  485 LYS A CG  1 
ATOM   3402  C CD  . LYS A  1 453 ? 15.449  29.408  176.261 1.00 129.87 ?  485 LYS A CD  1 
ATOM   3403  C CE  . LYS A  1 453 ? 16.534  28.751  177.097 1.00 130.79 ?  485 LYS A CE  1 
ATOM   3404  N NZ  . LYS A  1 453 ? 17.886  29.157  176.608 1.00 128.52 1  485 LYS A NZ  1 
ATOM   3405  N N   . TYR A  1 454 ? 10.232  27.464  175.870 1.00 124.74 ?  486 TYR A N   1 
ATOM   3406  C CA  . TYR A  1 454 ? 9.784   26.197  175.296 1.00 123.98 ?  486 TYR A CA  1 
ATOM   3407  C C   . TYR A  1 454 ? 8.264   26.119  175.263 1.00 127.69 ?  486 TYR A C   1 
ATOM   3408  O O   . TYR A  1 454 ? 7.575   26.674  176.126 1.00 128.31 ?  486 TYR A O   1 
ATOM   3409  C CB  . TYR A  1 454 ? 10.292  24.979  176.094 1.00 121.93 ?  486 TYR A CB  1 
ATOM   3410  C CG  . TYR A  1 454 ? 11.791  24.829  176.184 1.00 121.37 ?  486 TYR A CG  1 
ATOM   3411  C CD1 . TYR A  1 454 ? 12.526  24.419  175.083 1.00 127.49 ?  486 TYR A CD1 1 
ATOM   3412  C CD2 . TYR A  1 454 ? 12.468  25.060  177.375 1.00 124.25 ?  486 TYR A CD2 1 
ATOM   3413  C CE1 . TYR A  1 454 ? 13.901  24.264  175.155 1.00 131.10 ?  486 TYR A CE1 1 
ATOM   3414  C CE2 . TYR A  1 454 ? 13.846  24.907  177.458 1.00 125.49 ?  486 TYR A CE2 1 
ATOM   3415  C CZ  . TYR A  1 454 ? 14.557  24.508  176.343 1.00 129.12 ?  486 TYR A CZ  1 
ATOM   3416  O OH  . TYR A  1 454 ? 15.925  24.352  176.409 1.00 136.63 ?  486 TYR A OH  1 
ATOM   3417  N N   . LYS A  1 455 ? 7.748   25.421  174.247 1.00 126.05 ?  487 LYS A N   1 
ATOM   3418  C CA  . LYS A  1 455 ? 6.318   25.159  174.135 1.00 125.93 ?  487 LYS A CA  1 
ATOM   3419  C C   . LYS A  1 455 ? 6.077   23.923  173.275 1.00 123.19 ?  487 LYS A C   1 
ATOM   3420  O O   . LYS A  1 455 ? 6.887   23.574  172.410 1.00 120.58 ?  487 LYS A O   1 
ATOM   3421  C CB  . LYS A  1 455 ? 5.529   26.353  173.588 1.00 130.43 ?  487 LYS A CB  1 
ATOM   3422  C CG  . LYS A  1 455 ? 5.394   26.440  172.091 1.00 127.91 ?  487 LYS A CG  1 
ATOM   3423  C CD  . LYS A  1 455 ? 4.352   27.498  171.777 1.00 136.07 ?  487 LYS A CD  1 
ATOM   3424  C CE  . LYS A  1 455 ? 3.925   27.479  170.329 1.00 134.41 ?  487 LYS A CE  1 
ATOM   3425  N NZ  . LYS A  1 455 ? 2.827   28.459  170.097 1.00 137.48 1  487 LYS A NZ  1 
ATOM   3426  N N   . VAL A  1 456 ? 4.952   23.267  173.543 1.00 118.48 ?  488 VAL A N   1 
ATOM   3427  C CA  . VAL A  1 456 ? 4.558   22.003  172.934 1.00 118.01 ?  488 VAL A CA  1 
ATOM   3428  C C   . VAL A  1 456 ? 3.645   22.304  171.751 1.00 119.73 ?  488 VAL A C   1 
ATOM   3429  O O   . VAL A  1 456 ? 2.712   23.108  171.863 1.00 135.63 ?  488 VAL A O   1 
ATOM   3430  C CB  . VAL A  1 456 ? 3.861   21.085  173.950 1.00 130.57 ?  488 VAL A CB  1 
ATOM   3431  C CG1 . VAL A  1 456 ? 3.499   19.764  173.303 1.00 131.11 ?  488 VAL A CG1 1 
ATOM   3432  C CG2 . VAL A  1 456 ? 4.763   20.858  175.142 1.00 126.44 ?  488 VAL A CG2 1 
ATOM   3433  N N   . VAL A  1 457 ? 3.923   21.671  170.614 1.00 118.59 ?  489 VAL A N   1 
ATOM   3434  C CA  . VAL A  1 457 ? 3.130   21.799  169.398 1.00 119.40 ?  489 VAL A CA  1 
ATOM   3435  C C   . VAL A  1 457 ? 2.783   20.424  168.859 1.00 118.10 ?  489 VAL A C   1 
ATOM   3436  O O   . VAL A  1 457 ? 3.476   19.438  169.119 1.00 116.61 ?  489 VAL A O   1 
ATOM   3437  C CB  . VAL A  1 457 ? 3.848   22.615  168.304 1.00 120.36 ?  489 VAL A CB  1 
ATOM   3438  C CG1 . VAL A  1 457 ? 4.000   24.036  168.746 1.00 121.92 ?  489 VAL A CG1 1 
ATOM   3439  C CG2 . VAL A  1 457 ? 5.189   21.995  167.951 1.00 119.16 ?  489 VAL A CG2 1 
ATOM   3440  N N   . LYS A  1 458 ? 1.687   20.360  168.109 1.00 125.64 ?  490 LYS A N   1 
ATOM   3441  C CA  . LYS A  1 458 ? 1.225   19.124  167.507 1.00 126.97 ?  490 LYS A CA  1 
ATOM   3442  C C   . LYS A  1 458 ? 1.500   19.178  166.011 1.00 118.59 ?  490 LYS A C   1 
ATOM   3443  O O   . LYS A  1 458 ? 1.202   20.184  165.375 1.00 113.98 ?  490 LYS A O   1 
ATOM   3444  C CB  . LYS A  1 458 ? -0.304  19.127  167.603 1.00 134.79 ?  490 LYS A CB  1 
ATOM   3445  C CG  . LYS A  1 458 ? -1.202  17.991  167.992 1.00 138.12 ?  490 LYS A CG  1 
ATOM   3446  C CD  . LYS A  1 458 ? -2.585  18.683  167.907 1.00 137.47 ?  490 LYS A CD  1 
ATOM   3447  C CE  . LYS A  1 458 ? -3.767  17.840  168.267 1.00 142.41 ?  490 LYS A CE  1 
ATOM   3448  N NZ  . LYS A  1 458 ? -4.381  18.298  169.517 1.00 142.73 1  490 LYS A NZ  1 
ATOM   3449  N N   . ILE A  1 459 ? 1.952   18.073  165.429 1.00 119.50 ?  491 ILE A N   1 
ATOM   3450  C CA  . ILE A  1 459 ? 2.250   18.038  163.996 1.00 119.80 ?  491 ILE A CA  1 
ATOM   3451  C C   . ILE A  1 459 ? 1.032   17.508  163.254 1.00 121.75 ?  491 ILE A C   1 
ATOM   3452  O O   . ILE A  1 459 ? 0.526   16.428  163.579 1.00 121.92 ?  491 ILE A O   1 
ATOM   3453  C CB  . ILE A  1 459 ? 3.512   17.217  163.688 1.00 118.00 ?  491 ILE A CB  1 
ATOM   3454  C CG1 . ILE A  1 459 ? 4.704   17.827  164.422 1.00 116.28 ?  491 ILE A CG1 1 
ATOM   3455  C CG2 . ILE A  1 459 ? 3.790   17.197  162.197 1.00 118.60 ?  491 ILE A CG2 1 
ATOM   3456  C CD1 . ILE A  1 459 ? 4.983   19.270  164.033 1.00 116.83 ?  491 ILE A CD1 1 
ATOM   3457  N N   . GLU A  1 460 ? 0.560   18.247  162.254 1.00 119.75 ?  492 GLU A N   1 
ATOM   3458  C CA  . GLU A  1 460 ? -0.547  17.773  161.427 1.00 119.77 ?  492 GLU A CA  1 
ATOM   3459  C C   . GLU A  1 460 ? 0.008   17.662  160.014 1.00 115.61 ?  492 GLU A C   1 
ATOM   3460  O O   . GLU A  1 460 ? -0.105  18.595  159.202 1.00 118.52 ?  492 GLU A O   1 
ATOM   3461  C CB  . GLU A  1 460 ? -1.770  18.680  161.527 1.00 124.32 ?  492 GLU A CB  1 
ATOM   3462  C CG  . GLU A  1 460 ? -2.314  18.728  162.955 1.00 132.41 ?  492 GLU A CG  1 
ATOM   3463  C CD  . GLU A  1 460 ? -3.532  19.612  163.114 1.00 134.47 ?  492 GLU A CD  1 
ATOM   3464  O OE1 . GLU A  1 460 ? -3.936  20.259  162.127 1.00 141.89 ?  492 GLU A OE1 1 
ATOM   3465  O OE2 . GLU A  1 460 ? -4.093  19.648  164.231 1.00 132.51 -1 492 GLU A OE2 1 
ATOM   3466  N N   . PRO A  1 461 ? 0.626   16.524  159.686 1.00 119.36 ?  493 PRO A N   1 
ATOM   3467  C CA  . PRO A  1 461 ? 1.329   16.387  158.405 1.00 122.24 ?  493 PRO A CA  1 
ATOM   3468  C C   . PRO A  1 461 ? 0.405   16.325  157.214 1.00 125.56 ?  493 PRO A C   1 
ATOM   3469  O O   . PRO A  1 461 ? 0.890   16.298  156.078 1.00 123.27 ?  493 PRO A O   1 
ATOM   3470  C CB  . PRO A  1 461 ? 2.096   15.072  158.575 1.00 119.47 ?  493 PRO A CB  1 
ATOM   3471  C CG  . PRO A  1 461 ? 1.226   14.275  159.503 1.00 120.20 ?  493 PRO A CG  1 
ATOM   3472  C CD  . PRO A  1 461 ? 0.658   15.278  160.473 1.00 121.81 ?  493 PRO A CD  1 
ATOM   3473  N N   . LEU A  1 462 ? -0.900  16.269  157.436 1.00 119.18 ?  494 LEU A N   1 
ATOM   3474  C CA  . LEU A  1 462 ? -1.875  16.199  156.358 1.00 123.20 ?  494 LEU A CA  1 
ATOM   3475  C C   . LEU A  1 462 ? -2.282  17.604  155.930 1.00 126.53 ?  494 LEU A C   1 
ATOM   3476  O O   . LEU A  1 462 ? -2.955  18.322  156.676 1.00 131.35 ?  494 LEU A O   1 
ATOM   3477  C CB  . LEU A  1 462 ? -3.081  15.380  156.805 1.00 128.89 ?  494 LEU A CB  1 
ATOM   3478  C CG  . LEU A  1 462 ? -2.816  13.881  156.662 1.00 130.48 ?  494 LEU A CG  1 
ATOM   3479  C CD1 . LEU A  1 462 ? -4.018  13.067  157.103 1.00 134.10 ?  494 LEU A CD1 1 
ATOM   3480  C CD2 . LEU A  1 462 ? -2.404  13.532  155.241 1.00 127.81 ?  494 LEU A CD2 1 
ATOM   3481  N N   . GLY A  1 463 ? -1.851  18.000  154.736 1.00 156.08 ?  495 GLY A N   1 
ATOM   3482  C CA  . GLY A  1 463 ? -2.194  19.293  154.183 1.00 159.02 ?  495 GLY A CA  1 
ATOM   3483  C C   . GLY A  1 463 ? -2.584  19.110  152.731 1.00 164.20 ?  495 GLY A C   1 
ATOM   3484  O O   . GLY A  1 463 ? -1.855  18.486  151.954 1.00 164.72 ?  495 GLY A O   1 
ATOM   3485  N N   . VAL A  1 464 ? -3.740  19.650  152.360 1.00 171.49 ?  496 VAL A N   1 
ATOM   3486  C CA  . VAL A  1 464 ? -4.273  19.567  151.004 1.00 171.17 ?  496 VAL A CA  1 
ATOM   3487  C C   . VAL A  1 464 ? -3.974  20.856  150.254 1.00 172.61 ?  496 VAL A C   1 
ATOM   3488  O O   . VAL A  1 464 ? -3.972  21.947  150.840 1.00 171.90 ?  496 VAL A O   1 
ATOM   3489  C CB  . VAL A  1 464 ? -5.784  19.274  151.024 1.00 175.91 ?  496 VAL A CB  1 
ATOM   3490  C CG1 . VAL A  1 464 ? -6.037  17.869  151.549 1.00 173.50 ?  496 VAL A CG1 1 
ATOM   3491  C CG2 . VAL A  1 464 ? -6.510  20.303  151.872 1.00 180.93 ?  496 VAL A CG2 1 
ATOM   3492  N N   . ALA A  1 465 ? -3.708  20.729  148.952 1.00 175.77 ?  497 ALA A N   1 
ATOM   3493  C CA  . ALA A  1 465 ? -3.379  21.883  148.137 1.00 179.49 ?  497 ALA A CA  1 
ATOM   3494  C C   . ALA A  1 465 ? -3.779  21.651  146.687 1.00 185.25 ?  497 ALA A C   1 
ATOM   3495  O O   . ALA A  1 465 ? -3.671  20.520  146.190 1.00 183.72 ?  497 ALA A O   1 
ATOM   3496  C CB  . ALA A  1 465 ? -1.884  22.202  148.213 1.00 176.12 ?  497 ALA A CB  1 
ATOM   3497  N N   . PRO A  1 466 ? -4.246  22.690  145.998 1.00 178.97 ?  498 PRO A N   1 
ATOM   3498  C CA  . PRO A  1 466 ? -4.683  22.534  144.606 1.00 183.90 ?  498 PRO A CA  1 
ATOM   3499  C C   . PRO A  1 466 ? -3.529  22.596  143.617 1.00 184.70 ?  498 PRO A C   1 
ATOM   3500  O O   . PRO A  1 466 ? -2.558  23.333  143.805 1.00 182.81 ?  498 PRO A O   1 
ATOM   3501  C CB  . PRO A  1 466 ? -5.635  23.719  144.413 1.00 187.83 ?  498 PRO A CB  1 
ATOM   3502  C CG  . PRO A  1 466 ? -5.071  24.771  145.313 1.00 183.31 ?  498 PRO A CG  1 
ATOM   3503  C CD  . PRO A  1 466 ? -4.526  24.041  146.517 1.00 179.98 ?  498 PRO A CD  1 
ATOM   3504  N N   . THR A  1 467 ? -3.645  21.806  142.553 1.00 183.38 ?  499 THR A N   1 
ATOM   3505  C CA  . THR A  1 467 ? -2.673  21.841  141.471 1.00 186.98 ?  499 THR A CA  1 
ATOM   3506  C C   . THR A  1 467 ? -3.311  21.202  140.251 1.00 195.34 ?  499 THR A C   1 
ATOM   3507  O O   . THR A  1 467 ? -4.292  20.458  140.345 1.00 197.63 ?  499 THR A O   1 
ATOM   3508  C CB  . THR A  1 467 ? -1.353  21.136  141.817 1.00 182.34 ?  499 THR A CB  1 
ATOM   3509  O OG1 . THR A  1 467 ? -0.486  21.136  140.674 1.00 188.15 ?  499 THR A OG1 1 
ATOM   3510  C CG2 . THR A  1 467 ? -1.613  19.719  142.182 1.00 177.41 ?  499 THR A CG2 1 
ATOM   3511  N N   . ARG A  1 468 ? -2.726  21.511  139.104 1.00 193.28 ?  500 ARG A N   1 
ATOM   3512  C CA  . ARG A  1 468 ? -3.184  21.061  137.800 1.00 195.92 ?  500 ARG A CA  1 
ATOM   3513  C C   . ARG A  1 468 ? -2.806  19.612  137.488 1.00 197.43 ?  500 ARG A C   1 
ATOM   3514  O O   . ARG A  1 468 ? -2.254  19.312  136.425 1.00 199.53 ?  500 ARG A O   1 
ATOM   3515  C CB  . ARG A  1 468 ? -2.669  22.109  136.800 1.00 200.78 ?  500 ARG A CB  1 
ATOM   3516  C CG  . ARG A  1 468 ? -1.175  22.436  136.968 1.00 199.23 ?  500 ARG A CG  1 
ATOM   3517  C CD  . ARG A  1 468 ? -0.672  23.471  135.960 1.00 199.57 ?  500 ARG A CD  1 
ATOM   3518  N NE  . ARG A  1 468 ? 0.771   23.686  136.055 1.00 195.37 ?  500 ARG A NE  1 
ATOM   3519  C CZ  . ARG A  1 468 ? 1.417   24.680  135.450 1.00 195.47 ?  500 ARG A CZ  1 
ATOM   3520  N NH1 . ARG A  1 468 ? 0.746   25.554  134.711 1.00 199.68 1  500 ARG A NH1 1 
ATOM   3521  N NH2 . ARG A  1 468 ? 2.728   24.814  135.598 1.00 195.63 ?  500 ARG A NH2 1 
ATOM   3522  N N   . CYS A  1 469 ? -3.120  18.713  138.432 1.00 183.61 ?  501 CYS A N   1 
ATOM   3523  C CA  . CYS A  1 469 ? -2.856  17.274  138.362 1.00 185.82 ?  501 CYS A CA  1 
ATOM   3524  C C   . CYS A  1 469 ? -4.139  16.476  138.550 1.00 190.00 ?  501 CYS A C   1 
ATOM   3525  O O   . CYS A  1 469 ? -4.871  16.699  139.521 1.00 190.55 ?  501 CYS A O   1 
ATOM   3526  C CB  . CYS A  1 469 ? -1.861  16.757  139.401 1.00 181.54 ?  501 CYS A CB  1 
ATOM   3527  S SG  . CYS A  1 469 ? -1.687  14.938  139.268 1.00 230.82 ?  501 CYS A SG  1 
ATOM   3528  N N   . LYS A  1 470 ? -4.411  15.553  137.628 1.00 177.01 ?  502 LYS A N   1 
ATOM   3529  C CA  . LYS A  1 470 ? -5.578  14.680  137.687 1.00 179.73 ?  502 LYS A CA  1 
ATOM   3530  C C   . LYS A  1 470 ? -5.092  13.239  137.620 1.00 182.61 ?  502 LYS A C   1 
ATOM   3531  O O   . LYS A  1 470 ? -4.086  12.945  136.963 1.00 179.12 ?  502 LYS A O   1 
ATOM   3532  C CB  . LYS A  1 470 ? -6.530  14.946  136.506 1.00 190.56 ?  502 LYS A CB  1 
ATOM   3533  C CG  . LYS A  1 470 ? -7.868  14.197  136.512 1.00 207.63 ?  502 LYS A CG  1 
ATOM   3534  C CD  . LYS A  1 470 ? -8.588  14.502  135.196 1.00 214.23 ?  502 LYS A CD  1 
ATOM   3535  C CE  . LYS A  1 470 ? -9.900  13.759  135.032 1.00 220.20 ?  502 LYS A CE  1 
ATOM   3536  N NZ  . LYS A  1 470 ? -10.693 13.759  136.282 1.00 222.78 1  502 LYS A NZ  1 
ATOM   3537  N N   . ARG A  1 471 ? -5.801  12.321  138.288 1.00 167.02 ?  503 ARG A N   1 
ATOM   3538  C CA  . ARG A  1 471 ? -5.290  10.959  138.200 1.00 169.63 ?  503 ARG A CA  1 
ATOM   3539  C C   . ARG A  1 471 ? -5.703  10.271  136.913 1.00 178.65 ?  503 ARG A C   1 
ATOM   3540  O O   . ARG A  1 471 ? -6.147  10.908  135.952 1.00 181.90 ?  503 ARG A O   1 
ATOM   3541  C CB  . ARG A  1 471 ? -5.677  10.064  139.383 1.00 169.30 ?  503 ARG A CB  1 
ATOM   3542  C CG  . ARG A  1 471 ? -4.609  10.041  140.491 1.00 161.85 ?  503 ARG A CG  1 
ATOM   3543  C CD  . ARG A  1 471 ? -4.856  8.909   141.460 1.00 156.86 ?  503 ARG A CD  1 
ATOM   3544  N NE  . ARG A  1 471 ? -6.076  9.075   142.224 1.00 163.22 ?  503 ARG A NE  1 
ATOM   3545  C CZ  . ARG A  1 471 ? -6.594  8.117   142.979 1.00 166.22 ?  503 ARG A CZ  1 
ATOM   3546  N NH1 . ARG A  1 471 ? -5.991  6.936   143.053 1.00 163.06 1  503 ARG A NH1 1 
ATOM   3547  N NH2 . ARG A  1 471 ? -7.724  8.331   143.630 1.00 172.33 ?  503 ARG A NH2 1 
ATOM   3548  N N   . ARG A  1 472 ? -5.594  8.953   136.920 1.00 160.16 ?  504 ARG A N   1 
ATOM   3549  C CA  . ARG A  1 472 ? -5.888  8.153   135.749 1.00 175.36 ?  504 ARG A CA  1 
ATOM   3550  C C   . ARG A  1 472 ? -7.323  7.635   135.744 1.00 187.19 ?  504 ARG A C   1 
ATOM   3551  O O   . ARG A  1 472 ? -8.217  8.121   136.444 1.00 187.06 ?  504 ARG A O   1 
ATOM   3552  C CB  . ARG A  1 472 ? -4.890  6.998   135.639 1.00 175.24 ?  504 ARG A CB  1 
ATOM   3553  C CG  . ARG A  1 472 ? -4.875  6.055   136.832 1.00 173.59 ?  504 ARG A CG  1 
ATOM   3554  C CD  . ARG A  1 472 ? -3.535  5.339   136.902 1.00 173.03 ?  504 ARG A CD  1 
ATOM   3555  N NE  . ARG A  1 472 ? -2.433  6.296   136.829 1.00 169.16 ?  504 ARG A NE  1 
ATOM   3556  C CZ  . ARG A  1 472 ? -1.640  6.623   137.846 1.00 160.49 ?  504 ARG A CZ  1 
ATOM   3557  N NH1 . ARG A  1 472 ? -0.666  7.504   137.664 1.00 156.01 1  504 ARG A NH1 1 
ATOM   3558  N NH2 . ARG A  1 472 ? -1.832  6.091   139.045 1.00 153.48 ?  504 ARG A NH2 1 
ATOM   3559  N N   . VAL A  1 473 ? -7.502  6.588   134.954 1.00 205.30 ?  505 VAL A N   1 
ATOM   3560  C CA  . VAL A  1 473 ? -8.748  5.956   134.561 1.00 215.22 ?  505 VAL A CA  1 
ATOM   3561  C C   . VAL A  1 473 ? -8.375  4.504   134.294 1.00 220.24 ?  505 VAL A C   1 
ATOM   3562  O O   . VAL A  1 473 ? -9.160  3.723   133.746 1.00 226.95 ?  505 VAL A O   1 
ATOM   3563  C CB  . VAL A  1 473 ? -9.376  6.692   133.359 1.00 223.01 ?  505 VAL A CB  1 
ATOM   3564  C CG1 . VAL A  1 473 ? -8.727  6.249   132.002 1.00 221.66 ?  505 VAL A CG1 1 
ATOM   3565  C CG2 . VAL A  1 473 ? -10.957 6.539   133.383 1.00 214.27 ?  505 VAL A CG2 1 
ATOM   3566  N N   . VAL A  1 474 ? -7.174  4.148   134.762 1.00 200.88 ?  506 VAL A N   1 
ATOM   3567  C CA  . VAL A  1 474 ? -6.507  2.862   134.581 1.00 201.48 ?  506 VAL A CA  1 
ATOM   3568  C C   . VAL A  1 474 ? -6.462  2.535   133.092 1.00 206.43 ?  506 VAL A C   1 
ATOM   3569  O O   . VAL A  1 474 ? -6.821  1.432   132.666 1.00 205.59 ?  506 VAL A O   1 
ATOM   3570  C CB  . VAL A  1 474 ? -7.191  1.759   135.408 1.00 196.48 ?  506 VAL A CB  1 
ATOM   3571  C CG1 . VAL A  1 474 ? -6.296  0.529   135.503 1.00 189.86 ?  506 VAL A CG1 1 
ATOM   3572  C CG2 . VAL A  1 474 ? -7.537  2.285   136.796 1.00 192.55 ?  506 VAL A CG2 1 
ATOM   3573  N N   . GLY A  1 475 ? -6.009  3.494   132.290 1.00 186.65 ?  507 GLY A N   1 
ATOM   3574  C CA  . GLY A  1 475 ? -5.908  3.294   130.855 1.00 186.73 ?  507 GLY A CA  1 
ATOM   3575  C C   . GLY A  1 475 ? -4.927  2.213   130.444 1.00 179.61 ?  507 GLY A C   1 
ATOM   3576  O O   . GLY A  1 475 ? -4.077  2.428   129.580 1.00 177.02 ?  507 GLY A O   1 
ATOM   3577  N N   . ALA B  2 1   ? 23.983  31.588  138.478 1.00 192.15 ?  512 ALA B N   1 
ATOM   3578  C CA  . ALA B  2 1   ? 25.151  31.619  139.352 1.00 191.74 ?  512 ALA B CA  1 
ATOM   3579  C C   . ALA B  2 1   ? 25.697  30.212  139.591 1.00 190.35 ?  512 ALA B C   1 
ATOM   3580  O O   . ALA B  2 1   ? 25.061  29.221  139.230 1.00 189.00 ?  512 ALA B O   1 
ATOM   3581  C CB  . ALA B  2 1   ? 24.806  32.288  140.671 1.00 188.42 ?  512 ALA B CB  1 
ATOM   3582  N N   . VAL B  2 2   ? 26.882  30.132  140.199 1.00 176.44 ?  513 VAL B N   1 
ATOM   3583  C CA  . VAL B  2 2   ? 27.477  28.836  140.500 1.00 175.61 ?  513 VAL B CA  1 
ATOM   3584  C C   . VAL B  2 2   ? 26.741  28.186  141.665 1.00 169.98 ?  513 VAL B C   1 
ATOM   3585  O O   . VAL B  2 2   ? 26.195  28.862  142.548 1.00 167.07 ?  513 VAL B O   1 
ATOM   3586  C CB  . VAL B  2 2   ? 28.980  28.986  140.804 1.00 178.58 ?  513 VAL B CB  1 
ATOM   3587  C CG1 . VAL B  2 2   ? 29.737  29.434  139.560 1.00 184.88 ?  513 VAL B CG1 1 
ATOM   3588  C CG2 . VAL B  2 2   ? 29.193  29.970  141.944 1.00 176.79 ?  513 VAL B CG2 1 
ATOM   3589  N N   . GLY B  2 3   ? 26.725  26.861  141.670 1.00 169.95 ?  514 GLY B N   1 
ATOM   3590  C CA  . GLY B  2 3   ? 26.066  26.115  142.727 1.00 165.03 ?  514 GLY B CA  1 
ATOM   3591  C C   . GLY B  2 3   ? 26.816  24.834  143.004 1.00 165.17 ?  514 GLY B C   1 
ATOM   3592  O O   . GLY B  2 3   ? 27.493  24.289  142.127 1.00 169.04 ?  514 GLY B O   1 
ATOM   3593  N N   . ILE B  2 4   ? 26.687  24.346  144.236 1.00 151.09 ?  515 ILE B N   1 
ATOM   3594  C CA  . ILE B  2 4   ? 27.412  23.155  144.665 1.00 150.64 ?  515 ILE B CA  1 
ATOM   3595  C C   . ILE B  2 4   ? 26.411  22.112  145.152 1.00 150.32 ?  515 ILE B C   1 
ATOM   3596  O O   . ILE B  2 4   ? 26.736  21.241  145.968 1.00 149.80 ?  515 ILE B O   1 
ATOM   3597  C CB  . ILE B  2 4   ? 28.467  23.516  145.733 1.00 150.18 ?  515 ILE B CB  1 
ATOM   3598  C CG1 . ILE B  2 4   ? 29.495  22.390  145.906 1.00 150.22 ?  515 ILE B CG1 1 
ATOM   3599  C CG2 . ILE B  2 4   ? 27.807  23.916  147.050 1.00 149.74 ?  515 ILE B CG2 1 
ATOM   3600  C CD1 . ILE B  2 4   ? 30.797  22.851  146.512 1.00 152.56 ?  515 ILE B CD1 1 
ATOM   3601  N N   . GLY B  2 5   ? 25.187  22.183  144.639 1.00 168.40 ?  516 GLY B N   1 
ATOM   3602  C CA  . GLY B  2 5   ? 24.214  21.124  144.824 1.00 166.46 ?  516 GLY B CA  1 
ATOM   3603  C C   . GLY B  2 5   ? 23.186  21.436  145.894 1.00 161.25 ?  516 GLY B C   1 
ATOM   3604  O O   . GLY B  2 5   ? 23.154  22.512  146.497 1.00 159.96 ?  516 GLY B O   1 
ATOM   3605  N N   . ALA B  2 6   ? 22.319  20.450  146.111 1.00 166.39 ?  517 ALA B N   1 
ATOM   3606  C CA  . ALA B  2 6   ? 21.235  20.586  147.070 1.00 162.77 ?  517 ALA B CA  1 
ATOM   3607  C C   . ALA B  2 6   ? 21.767  20.635  148.496 1.00 159.47 ?  517 ALA B C   1 
ATOM   3608  O O   . ALA B  2 6   ? 22.826  20.087  148.811 1.00 162.13 ?  517 ALA B O   1 
ATOM   3609  C CB  . ALA B  2 6   ? 20.250  19.428  146.926 1.00 164.47 ?  517 ALA B CB  1 
ATOM   3610  N N   . VAL B  2 7   ? 21.005  21.288  149.370 1.00 167.66 ?  518 VAL B N   1 
ATOM   3611  C CA  . VAL B  2 7   ? 21.350  21.339  150.785 1.00 164.53 ?  518 VAL B CA  1 
ATOM   3612  C C   . VAL B  2 7   ? 20.230  20.685  151.582 1.00 164.32 ?  518 VAL B C   1 
ATOM   3613  O O   . VAL B  2 7   ? 19.271  20.160  151.004 1.00 165.86 ?  518 VAL B O   1 
ATOM   3614  C CB  . VAL B  2 7   ? 21.624  22.778  151.253 1.00 165.80 ?  518 VAL B CB  1 
ATOM   3615  C CG1 . VAL B  2 7   ? 23.009  23.209  150.803 1.00 169.14 ?  518 VAL B CG1 1 
ATOM   3616  C CG2 . VAL B  2 7   ? 20.568  23.717  150.696 1.00 165.90 ?  518 VAL B CG2 1 
ATOM   3617  N N   . PHE B  2 8   ? 20.334  20.716  152.909 1.00 168.12 ?  519 PHE B N   1 
ATOM   3618  C CA  . PHE B  2 8   ? 19.335  20.115  153.781 1.00 168.37 ?  519 PHE B CA  1 
ATOM   3619  C C   . PHE B  2 8   ? 18.959  21.038  154.932 1.00 171.79 ?  519 PHE B C   1 
ATOM   3620  O O   . PHE B  2 8   ? 19.832  21.668  155.535 1.00 171.90 ?  519 PHE B O   1 
ATOM   3621  C CB  . PHE B  2 8   ? 19.894  18.785  154.303 1.00 169.47 ?  519 PHE B CB  1 
ATOM   3622  C CG  . PHE B  2 8   ? 18.955  18.014  155.174 1.00 171.47 ?  519 PHE B CG  1 
ATOM   3623  C CD1 . PHE B  2 8   ? 17.895  17.312  154.624 1.00 174.99 ?  519 PHE B CD1 1 
ATOM   3624  C CD2 . PHE B  2 8   ? 19.180  17.921  156.536 1.00 170.63 ?  519 PHE B CD2 1 
ATOM   3625  C CE1 . PHE B  2 8   ? 17.042  16.577  155.425 1.00 174.70 ?  519 PHE B CE1 1 
ATOM   3626  C CE2 . PHE B  2 8   ? 18.340  17.179  157.339 1.00 171.61 ?  519 PHE B CE2 1 
ATOM   3627  C CZ  . PHE B  2 8   ? 17.265  16.509  156.785 1.00 171.17 ?  519 PHE B CZ  1 
ATOM   3628  N N   . LEU B  2 9   ? 17.656  21.121  155.240 1.00 177.82 ?  520 LEU B N   1 
ATOM   3629  C CA  . LEU B  2 9   ? 17.206  22.010  156.304 1.00 162.76 ?  520 LEU B CA  1 
ATOM   3630  C C   . LEU B  2 9   ? 16.801  21.284  157.582 1.00 163.63 ?  520 LEU B C   1 
ATOM   3631  O O   . LEU B  2 9   ? 16.813  21.903  158.650 1.00 162.10 ?  520 LEU B O   1 
ATOM   3632  C CB  . LEU B  2 9   ? 16.022  22.857  155.813 1.00 161.96 ?  520 LEU B CB  1 
ATOM   3633  C CG  . LEU B  2 9   ? 16.322  23.678  154.554 1.00 166.92 ?  520 LEU B CG  1 
ATOM   3634  C CD1 . LEU B  2 9   ? 15.135  24.540  154.154 1.00 166.33 ?  520 LEU B CD1 1 
ATOM   3635  C CD2 . LEU B  2 9   ? 17.578  24.529  154.721 1.00 170.08 ?  520 LEU B CD2 1 
ATOM   3636  N N   . GLY B  2 10  ? 16.447  20.006  157.503 1.00 183.82 ?  521 GLY B N   1 
ATOM   3637  C CA  . GLY B  2 10  ? 16.096  19.207  158.664 1.00 178.72 ?  521 GLY B CA  1 
ATOM   3638  C C   . GLY B  2 10  ? 14.609  19.038  158.895 1.00 172.93 ?  521 GLY B C   1 
ATOM   3639  O O   . GLY B  2 10  ? 13.757  19.381  158.068 1.00 175.34 ?  521 GLY B O   1 
ATOM   3640  N N   . PHE B  2 11  ? 14.315  18.455  160.062 1.00 160.22 ?  522 PHE B N   1 
ATOM   3641  C CA  . PHE B  2 11  ? 12.938  18.237  160.485 1.00 159.26 ?  522 PHE B CA  1 
ATOM   3642  C C   . PHE B  2 11  ? 12.250  19.583  160.610 1.00 160.33 ?  522 PHE B C   1 
ATOM   3643  O O   . PHE B  2 11  ? 12.761  20.486  161.282 1.00 161.00 ?  522 PHE B O   1 
ATOM   3644  C CB  . PHE B  2 11  ? 12.889  17.480  161.811 1.00 160.27 ?  522 PHE B CB  1 
ATOM   3645  C CG  . PHE B  2 11  ? 11.502  17.061  162.225 1.00 162.16 ?  522 PHE B CG  1 
ATOM   3646  C CD1 . PHE B  2 11  ? 10.816  16.070  161.543 1.00 161.56 ?  522 PHE B CD1 1 
ATOM   3647  C CD2 . PHE B  2 11  ? 10.895  17.651  163.323 1.00 161.95 ?  522 PHE B CD2 1 
ATOM   3648  C CE1 . PHE B  2 11  ? 9.542   15.691  161.940 1.00 162.58 ?  522 PHE B CE1 1 
ATOM   3649  C CE2 . PHE B  2 11  ? 9.626   17.273  163.726 1.00 161.95 ?  522 PHE B CE2 1 
ATOM   3650  C CZ  . PHE B  2 11  ? 8.949   16.291  163.033 1.00 162.33 ?  522 PHE B CZ  1 
ATOM   3651  N N   . LEU B  2 12  ? 11.093  19.718  159.967 1.00 163.35 ?  523 LEU B N   1 
ATOM   3652  C CA  . LEU B  2 12  ? 10.357  20.977  159.969 1.00 166.11 ?  523 LEU B CA  1 
ATOM   3653  C C   . LEU B  2 12  ? 11.216  22.105  159.406 1.00 170.97 ?  523 LEU B C   1 
ATOM   3654  O O   . LEU B  2 12  ? 11.027  23.276  159.743 1.00 173.82 ?  523 LEU B O   1 
ATOM   3655  C CB  . LEU B  2 12  ? 9.843   21.327  161.369 1.00 163.84 ?  523 LEU B CB  1 
ATOM   3656  C CG  . LEU B  2 12  ? 8.829   20.334  161.942 1.00 163.79 ?  523 LEU B CG  1 
ATOM   3657  C CD1 . LEU B  2 12  ? 8.417   20.722  163.349 1.00 165.25 ?  523 LEU B CD1 1 
ATOM   3658  C CD2 . LEU B  2 12  ? 7.615   20.240  161.039 1.00 158.85 ?  523 LEU B CD2 1 
ATOM   3659  N N   . GLY B  2 13  ? 12.182  21.747  158.561 1.00 161.63 ?  524 GLY B N   1 
ATOM   3660  C CA  . GLY B  2 13  ? 13.122  22.696  158.000 1.00 157.48 ?  524 GLY B CA  1 
ATOM   3661  C C   . GLY B  2 13  ? 12.428  23.801  157.239 1.00 157.37 ?  524 GLY B C   1 
ATOM   3662  O O   . GLY B  2 13  ? 12.589  24.986  157.550 1.00 156.14 ?  524 GLY B O   1 
ATOM   3663  N N   . ALA B  2 14  ? 11.666  23.419  156.220 1.00 148.94 ?  525 ALA B N   1 
ATOM   3664  C CA  . ALA B  2 14  ? 10.972  24.381  155.367 1.00 154.49 ?  525 ALA B CA  1 
ATOM   3665  C C   . ALA B  2 14  ? 9.605   24.762  155.933 1.00 162.16 ?  525 ALA B C   1 
ATOM   3666  O O   . ALA B  2 14  ? 8.594   24.747  155.231 1.00 168.42 ?  525 ALA B O   1 
ATOM   3667  C CB  . ALA B  2 14  ? 10.846  23.820  153.957 1.00 158.14 ?  525 ALA B CB  1 
ATOM   3668  N N   . ALA B  2 15  ? 9.560   25.096  157.224 1.00 145.09 ?  526 ALA B N   1 
ATOM   3669  C CA  . ALA B  2 15  ? 8.291   25.488  157.823 1.00 147.31 ?  526 ALA B CA  1 
ATOM   3670  C C   . ALA B  2 15  ? 7.901   26.903  157.424 1.00 147.39 ?  526 ALA B C   1 
ATOM   3671  O O   . ALA B  2 15  ? 6.712   27.196  157.260 1.00 161.92 ?  526 ALA B O   1 
ATOM   3672  C CB  . ALA B  2 15  ? 8.368   25.372  159.345 1.00 144.26 ?  526 ALA B CB  1 
ATOM   3673  N N   . GLY B  2 16  ? 8.884   27.783  157.273 1.00 154.81 ?  527 GLY B N   1 
ATOM   3674  C CA  . GLY B  2 16  ? 8.693   29.156  156.868 1.00 159.97 ?  527 GLY B CA  1 
ATOM   3675  C C   . GLY B  2 16  ? 8.854   29.385  155.386 1.00 160.37 ?  527 GLY B C   1 
ATOM   3676  O O   . GLY B  2 16  ? 8.696   30.515  154.914 1.00 161.36 ?  527 GLY B O   1 
ATOM   3677  N N   . SER B  2 17  ? 9.182   28.335  154.638 1.00 153.15 ?  528 SER B N   1 
ATOM   3678  C CA  . SER B  2 17  ? 9.351   28.423  153.199 1.00 153.19 ?  528 SER B CA  1 
ATOM   3679  C C   . SER B  2 17  ? 8.003   28.277  152.501 1.00 160.43 ?  528 SER B C   1 
ATOM   3680  O O   . SER B  2 17  ? 7.002   27.862  153.094 1.00 165.59 ?  528 SER B O   1 
ATOM   3681  C CB  . SER B  2 17  ? 10.326  27.351  152.708 1.00 151.10 ?  528 SER B CB  1 
ATOM   3682  O OG  . SER B  2 17  ? 11.601  27.495  153.310 1.00 149.19 ?  528 SER B OG  1 
ATOM   3683  N N   . THR B  2 18  ? 7.983   28.635  151.221 1.00 150.93 ?  529 THR B N   1 
ATOM   3684  C CA  . THR B  2 18  ? 6.769   28.503  150.436 1.00 156.11 ?  529 THR B CA  1 
ATOM   3685  C C   . THR B  2 18  ? 6.353   27.040  150.331 1.00 158.10 ?  529 THR B C   1 
ATOM   3686  O O   . THR B  2 18  ? 7.152   26.120  150.527 1.00 156.63 ?  529 THR B O   1 
ATOM   3687  C CB  . THR B  2 18  ? 6.978   29.081  149.037 1.00 154.51 ?  529 THR B CB  1 
ATOM   3688  O OG1 . THR B  2 18  ? 8.315   28.802  148.604 1.00 150.44 ?  529 THR B OG1 1 
ATOM   3689  C CG2 . THR B  2 18  ? 6.767   30.583  149.048 1.00 155.13 ?  529 THR B CG2 1 
ATOM   3690  N N   . MET B  2 19  ? 5.076   26.832  150.012 1.00 157.65 ?  530 MET B N   1 
ATOM   3691  C CA  . MET B  2 19  ? 4.565   25.472  149.884 1.00 154.34 ?  530 MET B CA  1 
ATOM   3692  C C   . MET B  2 19  ? 5.271   24.726  148.760 1.00 152.35 ?  530 MET B C   1 
ATOM   3693  O O   . MET B  2 19  ? 5.521   23.520  148.866 1.00 149.07 ?  530 MET B O   1 
ATOM   3694  C CB  . MET B  2 19  ? 3.055   25.501  149.671 1.00 154.74 ?  530 MET B CB  1 
ATOM   3695  C CG  . MET B  2 19  ? 2.314   26.054  150.869 1.00 156.59 ?  530 MET B CG  1 
ATOM   3696  S SD  . MET B  2 19  ? 0.540   26.217  150.617 1.00 160.68 ?  530 MET B SD  1 
ATOM   3697  C CE  . MET B  2 19  ? 0.075   24.553  150.156 1.00 161.05 ?  530 MET B CE  1 
ATOM   3698  N N   . GLY B  2 20  ? 5.591   25.427  147.670 1.00 161.99 ?  531 GLY B N   1 
ATOM   3699  C CA  . GLY B  2 20  ? 6.303   24.792  146.573 1.00 160.00 ?  531 GLY B CA  1 
ATOM   3700  C C   . GLY B  2 20  ? 7.705   24.367  146.964 1.00 157.75 ?  531 GLY B C   1 
ATOM   3701  O O   . GLY B  2 20  ? 8.185   23.310  146.544 1.00 154.72 ?  531 GLY B O   1 
ATOM   3702  N N   . ALA B  2 21  ? 8.379   25.182  147.776 1.00 151.64 ?  532 ALA B N   1 
ATOM   3703  C CA  . ALA B  2 21  ? 9.726   24.855  148.221 1.00 146.83 ?  532 ALA B CA  1 
ATOM   3704  C C   . ALA B  2 21  ? 9.684   23.789  149.310 1.00 145.52 ?  532 ALA B C   1 
ATOM   3705  O O   . ALA B  2 21  ? 10.550  22.910  149.357 1.00 147.16 ?  532 ALA B O   1 
ATOM   3706  C CB  . ALA B  2 21  ? 10.440  26.118  148.705 1.00 138.25 ?  532 ALA B CB  1 
ATOM   3707  N N   . ALA B  2 22  ? 8.676   23.851  150.184 1.00 150.24 ?  533 ALA B N   1 
ATOM   3708  C CA  . ALA B  2 22  ? 8.527   22.902  151.283 1.00 151.59 ?  533 ALA B CA  1 
ATOM   3709  C C   . ALA B  2 22  ? 8.054   21.533  150.807 1.00 148.59 ?  533 ALA B C   1 
ATOM   3710  O O   . ALA B  2 22  ? 8.127   20.568  151.576 1.00 147.74 ?  533 ALA B O   1 
ATOM   3711  C CB  . ALA B  2 22  ? 7.558   23.452  152.332 1.00 150.06 ?  533 ALA B CB  1 
ATOM   3712  N N   . SER B  2 23  ? 7.587   21.424  149.562 1.00 135.52 ?  534 SER B N   1 
ATOM   3713  C CA  . SER B  2 23  ? 7.138   20.150  149.019 1.00 135.84 ?  534 SER B CA  1 
ATOM   3714  C C   . SER B  2 23  ? 8.300   19.218  148.708 1.00 136.56 ?  534 SER B C   1 
ATOM   3715  O O   . SER B  2 23  ? 8.074   18.034  148.439 1.00 136.94 ?  534 SER B O   1 
ATOM   3716  C CB  . SER B  2 23  ? 6.305   20.384  147.758 1.00 135.92 ?  534 SER B CB  1 
ATOM   3717  O OG  . SER B  2 23  ? 5.163   21.173  148.042 1.00 135.44 ?  534 SER B OG  1 
ATOM   3718  N N   . MET B  2 24  ? 9.529   19.721  148.758 1.00 140.17 ?  535 MET B N   1 
ATOM   3719  C CA  . MET B  2 24  ? 10.719  18.923  148.529 1.00 146.12 ?  535 MET B CA  1 
ATOM   3720  C C   . MET B  2 24  ? 11.189  18.246  149.808 1.00 142.82 ?  535 MET B C   1 
ATOM   3721  O O   . MET B  2 24  ? 11.999  17.311  149.741 1.00 142.83 ?  535 MET B O   1 
ATOM   3722  C CB  . MET B  2 24  ? 11.842  19.804  147.976 1.00 153.89 ?  535 MET B CB  1 
ATOM   3723  C CG  . MET B  2 24  ? 11.393  20.792  146.906 1.00 151.63 ?  535 MET B CG  1 
ATOM   3724  S SD  . MET B  2 24  ? 10.664  20.067  145.426 1.00 160.81 ?  535 MET B SD  1 
ATOM   3725  C CE  . MET B  2 24  ? 10.431  21.538  144.427 1.00 159.27 ?  535 MET B CE  1 
ATOM   3726  N N   . THR B  2 25  ? 10.674  18.697  150.953 1.00 144.45 ?  536 THR B N   1 
ATOM   3727  C CA  . THR B  2 25  ? 11.067  18.218  152.265 1.00 146.38 ?  536 THR B CA  1 
ATOM   3728  C C   . THR B  2 25  ? 10.003  17.313  152.872 1.00 143.90 ?  536 THR B C   1 
ATOM   3729  O O   . THR B  2 25  ? 9.961   17.131  154.092 1.00 146.26 ?  536 THR B O   1 
ATOM   3730  C CB  . THR B  2 25  ? 11.327  19.398  153.194 1.00 151.11 ?  536 THR B CB  1 
ATOM   3731  O OG1 . THR B  2 25  ? 12.013  20.404  152.528 1.00 157.68 ?  536 THR B OG1 1 
ATOM   3732  C CG2 . THR B  2 25  ? 12.146  18.992  154.348 1.00 149.29 ?  536 THR B CG2 1 
ATOM   3733  N N   . LEU B  2 26  ? 9.148   16.727  152.032 1.00 126.99 ?  537 LEU B N   1 
ATOM   3734  C CA  . LEU B  2 26  ? 8.063   15.884  152.534 1.00 126.81 ?  537 LEU B CA  1 
ATOM   3735  C C   . LEU B  2 26  ? 8.619   14.617  153.155 1.00 127.54 ?  537 LEU B C   1 
ATOM   3736  O O   . LEU B  2 26  ? 8.080   14.108  154.142 1.00 127.46 ?  537 LEU B O   1 
ATOM   3737  C CB  . LEU B  2 26  ? 7.071   15.537  151.426 1.00 126.78 ?  537 LEU B CB  1 
ATOM   3738  C CG  . LEU B  2 26  ? 6.208   16.652  150.849 1.00 126.18 ?  537 LEU B CG  1 
ATOM   3739  C CD1 . LEU B  2 26  ? 5.332   16.092  149.753 1.00 126.42 ?  537 LEU B CD1 1 
ATOM   3740  C CD2 . LEU B  2 26  ? 5.358   17.270  151.939 1.00 125.56 ?  537 LEU B CD2 1 
ATOM   3741  N N   . THR B  2 27  ? 9.700   14.094  152.584 1.00 132.95 ?  538 THR B N   1 
ATOM   3742  C CA  . THR B  2 27  ? 10.270  12.850  153.069 1.00 135.42 ?  538 THR B CA  1 
ATOM   3743  C C   . THR B  2 27  ? 11.088  13.036  154.333 1.00 136.17 ?  538 THR B C   1 
ATOM   3744  O O   . THR B  2 27  ? 11.650  12.058  154.815 1.00 136.02 ?  538 THR B O   1 
ATOM   3745  C CB  . THR B  2 27  ? 11.146  12.215  151.992 1.00 140.72 ?  538 THR B CB  1 
ATOM   3746  O OG1 . THR B  2 27  ? 11.582  10.924  152.438 1.00 140.57 ?  538 THR B OG1 1 
ATOM   3747  C CG2 . THR B  2 27  ? 12.358  13.081  151.729 1.00 142.56 ?  538 THR B CG2 1 
ATOM   3748  N N   . VAL B  2 28  ? 11.147  14.243  154.883 1.00 133.71 ?  539 VAL B N   1 
ATOM   3749  C CA  . VAL B  2 28  ? 11.891  14.523  156.103 1.00 133.98 ?  539 VAL B CA  1 
ATOM   3750  C C   . VAL B  2 28  ? 10.957  14.528  157.303 1.00 133.41 ?  539 VAL B C   1 
ATOM   3751  O O   . VAL B  2 28  ? 11.262  13.950  158.346 1.00 133.94 ?  539 VAL B O   1 
ATOM   3752  C CB  . VAL B  2 28  ? 12.664  15.854  155.980 1.00 133.83 ?  539 VAL B CB  1 
ATOM   3753  C CG1 . VAL B  2 28  ? 13.367  16.181  157.284 1.00 134.17 ?  539 VAL B CG1 1 
ATOM   3754  C CG2 . VAL B  2 28  ? 13.668  15.771  154.842 1.00 136.19 ?  539 VAL B CG2 1 
ATOM   3755  N N   . GLN B  2 29  ? 9.807   15.189  157.160 1.00 136.85 ?  540 GLN B N   1 
ATOM   3756  C CA  . GLN B  2 29  ? 8.802   15.219  158.213 1.00 134.72 ?  540 GLN B CA  1 
ATOM   3757  C C   . GLN B  2 29  ? 8.089   13.876  158.336 1.00 132.33 ?  540 GLN B C   1 
ATOM   3758  O O   . GLN B  2 29  ? 7.476   13.598  159.372 1.00 130.58 ?  540 GLN B O   1 
ATOM   3759  C CB  . GLN B  2 29  ? 7.813   16.356  157.947 1.00 135.19 ?  540 GLN B CB  1 
ATOM   3760  C CG  . GLN B  2 29  ? 8.397   17.742  158.229 1.00 137.66 ?  540 GLN B CG  1 
ATOM   3761  C CD  . GLN B  2 29  ? 9.219   18.277  157.070 1.00 140.43 ?  540 GLN B CD  1 
ATOM   3762  O OE1 . GLN B  2 29  ? 10.183  19.020  157.261 1.00 141.76 ?  540 GLN B OE1 1 
ATOM   3763  N NE2 . GLN B  2 29  ? 8.836   17.903  155.857 1.00 140.34 ?  540 GLN B NE2 1 
ATOM   3764  N N   . ALA B  2 30  ? 8.154   13.048  157.294 1.00 122.56 ?  541 ALA B N   1 
ATOM   3765  C CA  . ALA B  2 30  ? 7.541   11.724  157.295 1.00 123.05 ?  541 ALA B CA  1 
ATOM   3766  C C   . ALA B  2 30  ? 8.431   10.728  158.026 1.00 124.07 ?  541 ALA B C   1 
ATOM   3767  O O   . ALA B  2 30  ? 7.942   9.741   158.591 1.00 124.51 ?  541 ALA B O   1 
ATOM   3768  C CB  . ALA B  2 30  ? 7.274   11.259  155.868 1.00 123.22 ?  541 ALA B CB  1 
ATOM   3769  N N   . ARG B  2 31  ? 9.739   10.995  158.013 1.00 132.34 ?  542 ARG B N   1 
ATOM   3770  C CA  . ARG B  2 31  ? 10.751  10.137  158.629 1.00 135.04 ?  542 ARG B CA  1 
ATOM   3771  C C   . ARG B  2 31  ? 10.692  10.191  160.147 1.00 130.47 ?  542 ARG B C   1 
ATOM   3772  O O   . ARG B  2 31  ? 10.642  9.152   160.816 1.00 129.45 ?  542 ARG B O   1 
ATOM   3773  C CB  . ARG B  2 31  ? 12.110  10.647  158.142 1.00 139.01 ?  542 ARG B CB  1 
ATOM   3774  C CG  . ARG B  2 31  ? 12.633  10.115  156.837 1.00 145.25 ?  542 ARG B CG  1 
ATOM   3775  C CD  . ARG B  2 31  ? 13.865  10.924  156.411 1.00 157.29 ?  542 ARG B CD  1 
ATOM   3776  N NE  . ARG B  2 31  ? 15.073  10.886  157.217 1.00 160.38 ?  542 ARG B NE  1 
ATOM   3777  C CZ  . ARG B  2 31  ? 15.972  11.867  157.171 1.00 158.83 ?  542 ARG B CZ  1 
ATOM   3778  N NH1 . ARG B  2 31  ? 15.768  12.911  156.370 1.00 158.25 1  542 ARG B NH1 1 
ATOM   3779  N NH2 . ARG B  2 31  ? 17.059  11.821  157.922 1.00 155.51 ?  542 ARG B NH2 1 
ATOM   3780  N N   . ASN B  2 32  ? 10.666  11.395  160.709 1.00 150.41 ?  543 ASN B N   1 
ATOM   3781  C CA  . ASN B  2 32  ? 10.644  11.579  162.153 1.00 149.27 ?  543 ASN B CA  1 
ATOM   3782  C C   . ASN B  2 32  ? 9.236   11.618  162.722 1.00 149.87 ?  543 ASN B C   1 
ATOM   3783  O O   . ASN B  2 32  ? 9.020   12.233  163.775 1.00 151.55 ?  543 ASN B O   1 
ATOM   3784  C CB  . ASN B  2 32  ? 11.427  12.830  162.538 1.00 150.37 ?  543 ASN B CB  1 
ATOM   3785  C CG  . ASN B  2 32  ? 12.831  12.818  161.982 1.00 152.24 ?  543 ASN B CG  1 
ATOM   3786  O OD1 . ASN B  2 32  ? 13.224  13.716  161.240 1.00 156.22 ?  543 ASN B OD1 1 
ATOM   3787  N ND2 . ASN B  2 32  ? 13.602  11.796  162.345 1.00 156.28 ?  543 ASN B ND2 1 
ATOM   3788  N N   . LEU B  2 33  ? 8.265   10.994  162.058 1.00 137.57 ?  544 LEU B N   1 
ATOM   3789  C CA  . LEU B  2 33  ? 6.901   11.049  162.561 1.00 140.55 ?  544 LEU B CA  1 
ATOM   3790  C C   . LEU B  2 33  ? 6.620   9.860   163.465 1.00 142.25 ?  544 LEU B C   1 
ATOM   3791  O O   . LEU B  2 33  ? 5.768   9.949   164.358 1.00 141.69 ?  544 LEU B O   1 
ATOM   3792  C CB  . LEU B  2 33  ? 5.907   11.094  161.394 1.00 140.04 ?  544 LEU B CB  1 
ATOM   3793  C CG  . LEU B  2 33  ? 4.446   11.462  161.673 1.00 142.21 ?  544 LEU B CG  1 
ATOM   3794  C CD1 . LEU B  2 33  ? 4.363   12.837  162.313 1.00 141.84 ?  544 LEU B CD1 1 
ATOM   3795  C CD2 . LEU B  2 33  ? 3.640   11.439  160.387 1.00 143.86 ?  544 LEU B CD2 1 
ATOM   3796  N N   . LEU B  2 34  ? 7.316   8.749   163.238 1.00 146.40 ?  545 LEU B N   1 
ATOM   3797  C CA  . LEU B  2 34  ? 7.202   7.543   164.046 1.00 145.79 ?  545 LEU B CA  1 
ATOM   3798  C C   . LEU B  2 34  ? 8.436   7.295   164.902 1.00 145.88 ?  545 LEU B C   1 
ATOM   3799  O O   . LEU B  2 34  ? 8.310   6.864   166.050 1.00 145.44 ?  545 LEU B O   1 
ATOM   3800  C CB  . LEU B  2 34  ? 6.934   6.329   163.154 1.00 145.57 ?  545 LEU B CB  1 
ATOM   3801  C CG  . LEU B  2 34  ? 6.736   5.003   163.880 1.00 144.93 ?  545 LEU B CG  1 
ATOM   3802  C CD1 . LEU B  2 34  ? 5.568   5.130   164.837 1.00 144.40 ?  545 LEU B CD1 1 
ATOM   3803  C CD2 . LEU B  2 34  ? 6.499   3.875   162.884 1.00 144.82 ?  545 LEU B CD2 1 
ATOM   3804  N N   . SER B  2 35  ? 9.629   7.568   164.359 1.00 179.86 ?  546 SER B N   1 
ATOM   3805  C CA  . SER B  2 35  ? 10.912  7.441   165.051 1.00 183.27 ?  546 SER B CA  1 
ATOM   3806  C C   . SER B  2 35  ? 11.131  6.064   165.669 1.00 186.96 ?  546 SER B C   1 
ATOM   3807  O O   . SER B  2 35  ? 10.990  5.892   166.885 1.00 188.05 ?  546 SER B O   1 
ATOM   3808  C CB  . SER B  2 35  ? 11.055  8.523   166.126 1.00 183.02 ?  546 SER B CB  1 
ATOM   3809  O OG  . SER B  2 35  ? 10.982  9.819   165.556 1.00 179.65 ?  546 SER B OG  1 
ATOM   3810  N N   . GLY B  2 36  ? 11.493  5.084   164.847 1.00 169.23 ?  547 GLY B N   1 
ATOM   3811  C CA  . GLY B  2 36  ? 11.735  3.739   165.336 1.00 166.83 ?  547 GLY B CA  1 
ATOM   3812  C C   . GLY B  2 36  ? 10.479  2.997   165.747 1.00 164.17 ?  547 GLY B C   1 
ATOM   3813  O O   . GLY B  2 36  ? 10.120  2.982   166.925 1.00 164.73 ?  547 GLY B O   1 
ATOM   3814  N N   . THR B  2 58  ? 5.631   -0.126  187.663 1.00 168.15 ?  569 THR B N   1 
ATOM   3815  C CA  . THR B  2 58  ? 6.269   1.054   188.235 1.00 172.65 ?  569 THR B CA  1 
ATOM   3816  C C   . THR B  2 58  ? 5.880   2.294   187.430 1.00 172.72 ?  569 THR B C   1 
ATOM   3817  O O   . THR B  2 58  ? 5.949   2.286   186.200 1.00 170.82 ?  569 THR B O   1 
ATOM   3818  C CB  . THR B  2 58  ? 7.801   0.896   188.260 1.00 170.04 ?  569 THR B CB  1 
ATOM   3819  O OG1 . THR B  2 58  ? 8.284   0.695   186.925 1.00 165.42 ?  569 THR B OG1 1 
ATOM   3820  C CG2 . THR B  2 58  ? 8.193   -0.306  189.102 1.00 171.83 ?  569 THR B CG2 1 
ATOM   3821  N N   . VAL B  2 59  ? 5.480   3.367   188.114 1.00 177.81 ?  570 VAL B N   1 
ATOM   3822  C CA  . VAL B  2 59  ? 5.050   4.568   187.407 1.00 178.37 ?  570 VAL B CA  1 
ATOM   3823  C C   . VAL B  2 59  ? 6.262   5.286   186.816 1.00 174.30 ?  570 VAL B C   1 
ATOM   3824  O O   . VAL B  2 59  ? 7.392   4.801   186.925 1.00 164.96 ?  570 VAL B O   1 
ATOM   3825  C CB  . VAL B  2 59  ? 4.264   5.483   188.357 1.00 184.93 ?  570 VAL B CB  1 
ATOM   3826  C CG1 . VAL B  2 59  ? 3.481   6.479   187.589 1.00 183.17 ?  570 VAL B CG1 1 
ATOM   3827  C CG2 . VAL B  2 59  ? 3.356   4.682   189.202 1.00 190.03 ?  570 VAL B CG2 1 
ATOM   3828  N N   . TRP B  2 60  ? 6.036   6.448   186.196 1.00 173.77 ?  571 TRP B N   1 
ATOM   3829  C CA  . TRP B  2 60  ? 7.046   7.291   185.560 1.00 171.03 ?  571 TRP B CA  1 
ATOM   3830  C C   . TRP B  2 60  ? 7.649   6.588   184.352 1.00 165.51 ?  571 TRP B C   1 
ATOM   3831  O O   . TRP B  2 60  ? 8.187   7.236   183.447 1.00 161.39 ?  571 TRP B O   1 
ATOM   3832  C CB  . TRP B  2 60  ? 8.143   7.683   186.551 1.00 177.92 ?  571 TRP B CB  1 
ATOM   3833  C CG  . TRP B  2 60  ? 8.911   8.901   186.148 1.00 182.21 ?  571 TRP B CG  1 
ATOM   3834  C CD1 . TRP B  2 60  ? 8.404   10.103  185.753 1.00 186.81 ?  571 TRP B CD1 1 
ATOM   3835  C CD2 . TRP B  2 60  ? 10.340  9.036   186.110 1.00 182.82 ?  571 TRP B CD2 1 
ATOM   3836  N NE1 . TRP B  2 60  ? 9.425   10.976  185.462 1.00 187.09 ?  571 TRP B NE1 1 
ATOM   3837  C CE2 . TRP B  2 60  ? 10.624  10.346  185.676 1.00 184.21 ?  571 TRP B CE2 1 
ATOM   3838  C CE3 . TRP B  2 60  ? 11.406  8.176   186.400 1.00 182.26 ?  571 TRP B CE3 1 
ATOM   3839  C CZ2 . TRP B  2 60  ? 11.926  10.820  185.533 1.00 183.27 ?  571 TRP B CZ2 1 
ATOM   3840  C CZ3 . TRP B  2 60  ? 12.700  8.647   186.249 1.00 182.36 ?  571 TRP B CZ3 1 
ATOM   3841  C CH2 . TRP B  2 60  ? 12.948  9.956   185.819 1.00 182.65 ?  571 TRP B CH2 1 
ATOM   3842  N N   . GLY B  2 61  ? 7.573   5.260   184.342 1.00 183.70 ?  572 GLY B N   1 
ATOM   3843  C CA  . GLY B  2 61  ? 7.988   4.492   183.194 1.00 177.67 ?  572 GLY B CA  1 
ATOM   3844  C C   . GLY B  2 61  ? 6.741   4.183   182.402 1.00 175.43 ?  572 GLY B C   1 
ATOM   3845  O O   . GLY B  2 61  ? 6.799   3.871   181.209 1.00 175.64 ?  572 GLY B O   1 
ATOM   3846  N N   . ILE B  2 62  ? 5.592   4.251   183.082 1.00 162.74 ?  573 ILE B N   1 
ATOM   3847  C CA  . ILE B  2 62  ? 4.328   4.069   182.387 1.00 159.07 ?  573 ILE B CA  1 
ATOM   3848  C C   . ILE B  2 62  ? 3.861   5.354   181.733 1.00 160.36 ?  573 ILE B C   1 
ATOM   3849  O O   . ILE B  2 62  ? 2.961   5.330   180.885 1.00 161.13 ?  573 ILE B O   1 
ATOM   3850  C CB  . ILE B  2 62  ? 3.277   3.637   183.422 1.00 160.55 ?  573 ILE B CB  1 
ATOM   3851  C CG1 . ILE B  2 62  ? 2.024   3.060   182.765 1.00 160.17 ?  573 ILE B CG1 1 
ATOM   3852  C CG2 . ILE B  2 62  ? 2.926   4.827   184.346 1.00 167.25 ?  573 ILE B CG2 1 
ATOM   3853  C CD1 . ILE B  2 62  ? 0.981   2.633   183.775 1.00 165.20 ?  573 ILE B CD1 1 
ATOM   3854  N N   . LYS B  2 63  ? 4.470   6.474   182.107 1.00 162.01 ?  574 LYS B N   1 
ATOM   3855  C CA  . LYS B  2 63  ? 4.131   7.761   181.519 1.00 162.35 ?  574 LYS B CA  1 
ATOM   3856  C C   . LYS B  2 63  ? 4.521   7.813   180.045 1.00 158.71 ?  574 LYS B C   1 
ATOM   3857  O O   . LYS B  2 63  ? 3.817   8.417   179.227 1.00 158.69 ?  574 LYS B O   1 
ATOM   3858  C CB  . LYS B  2 63  ? 4.624   8.923   182.369 1.00 163.95 ?  574 LYS B CB  1 
ATOM   3859  C CG  . LYS B  2 63  ? 3.723   10.085  182.003 1.00 166.60 ?  574 LYS B CG  1 
ATOM   3860  C CD  . LYS B  2 63  ? 2.309   9.818   182.620 1.00 171.49 ?  574 LYS B CD  1 
ATOM   3861  C CE  . LYS B  2 63  ? 1.296   10.966  182.499 1.00 175.54 ?  574 LYS B CE  1 
ATOM   3862  N NZ  . LYS B  2 63  ? -0.017  10.657  183.159 1.00 181.12 1  574 LYS B NZ  1 
ATOM   3863  N N   . GLN B  2 64  ? 5.644   7.182   179.691 1.00 162.34 ?  575 GLN B N   1 
ATOM   3864  C CA  . GLN B  2 64  ? 6.138   7.199   178.321 1.00 162.56 ?  575 GLN B CA  1 
ATOM   3865  C C   . GLN B  2 64  ? 5.447   6.132   177.491 1.00 161.99 ?  575 GLN B C   1 
ATOM   3866  O O   . GLN B  2 64  ? 5.407   6.248   176.261 1.00 162.12 ?  575 GLN B O   1 
ATOM   3867  C CB  . GLN B  2 64  ? 7.649   6.936   178.275 1.00 162.97 ?  575 GLN B CB  1 
ATOM   3868  C CG  . GLN B  2 64  ? 8.111   5.635   178.971 1.00 162.59 ?  575 GLN B CG  1 
ATOM   3869  C CD  . GLN B  2 64  ? 8.051   4.405   178.051 1.00 162.16 ?  575 GLN B CD  1 
ATOM   3870  O OE1 . GLN B  2 64  ? 7.974   4.535   176.828 1.00 162.27 ?  575 GLN B OE1 1 
ATOM   3871  N NE2 . GLN B  2 64  ? 8.085   3.212   178.643 1.00 161.69 ?  575 GLN B NE2 1 
ATOM   3872  N N   . LEU B  2 65  ? 4.939   5.083   178.133 1.00 126.26 ?  576 LEU B N   1 
ATOM   3873  C CA  . LEU B  2 65  ? 4.242   4.028   177.410 1.00 125.33 ?  576 LEU B CA  1 
ATOM   3874  C C   . LEU B  2 65  ? 2.981   4.595   176.767 1.00 125.21 ?  576 LEU B C   1 
ATOM   3875  O O   . LEU B  2 65  ? 2.738   4.397   175.571 1.00 124.21 ?  576 LEU B O   1 
ATOM   3876  C CB  . LEU B  2 65  ? 3.925   2.858   178.337 1.00 126.41 ?  576 LEU B CB  1 
ATOM   3877  C CG  . LEU B  2 65  ? 3.317   1.646   177.635 1.00 125.67 ?  576 LEU B CG  1 
ATOM   3878  C CD1 . LEU B  2 65  ? 3.862   0.374   178.248 1.00 126.28 ?  576 LEU B CD1 1 
ATOM   3879  C CD2 . LEU B  2 65  ? 1.806   1.680   177.743 1.00 128.40 ?  576 LEU B CD2 1 
ATOM   3880  N N   . GLN B  2 66  ? 2.153   5.294   177.560 1.00 130.12 ?  577 GLN B N   1 
ATOM   3881  C CA  . GLN B  2 66  ? 0.906   5.887   177.071 1.00 139.08 ?  577 GLN B CA  1 
ATOM   3882  C C   . GLN B  2 66  ? 1.160   6.936   175.998 1.00 137.88 ?  577 GLN B C   1 
ATOM   3883  O O   . GLN B  2 66  ? 0.269   7.220   175.188 1.00 144.46 ?  577 GLN B O   1 
ATOM   3884  C CB  . GLN B  2 66  ? 0.162   6.571   178.214 1.00 150.15 ?  577 GLN B CB  1 
ATOM   3885  C CG  . GLN B  2 66  ? -1.260  6.992   177.877 1.00 163.26 ?  577 GLN B CG  1 
ATOM   3886  C CD  . GLN B  2 66  ? -2.220  6.780   179.022 1.00 177.97 ?  577 GLN B CD  1 
ATOM   3887  O OE1 . GLN B  2 66  ? -1.837  6.289   180.083 1.00 185.04 ?  577 GLN B OE1 1 
ATOM   3888  N NE2 . GLN B  2 66  ? -3.475  7.170   178.823 1.00 185.18 ?  577 GLN B NE2 1 
ATOM   3889  N N   . ALA B  2 67  ? 2.372   7.481   175.954 1.00 141.38 ?  578 ALA B N   1 
ATOM   3890  C CA  . ALA B  2 67  ? 2.756   8.474   174.961 1.00 139.39 ?  578 ALA B CA  1 
ATOM   3891  C C   . ALA B  2 67  ? 3.108   7.747   173.677 1.00 131.39 ?  578 ALA B C   1 
ATOM   3892  O O   . ALA B  2 67  ? 2.752   8.190   172.579 1.00 129.95 ?  578 ALA B O   1 
ATOM   3893  C CB  . ALA B  2 67  ? 3.919   9.328   175.464 1.00 134.49 ?  578 ALA B CB  1 
ATOM   3894  N N   . ARG B  2 68  ? 3.794   6.613   173.818 1.00 138.59 ?  579 ARG B N   1 
ATOM   3895  C CA  . ARG B  2 68  ? 4.230   5.820   172.687 1.00 131.47 ?  579 ARG B CA  1 
ATOM   3896  C C   . ARG B  2 68  ? 3.076   5.017   172.096 1.00 132.93 ?  579 ARG B C   1 
ATOM   3897  O O   . ARG B  2 68  ? 3.188   4.524   170.967 1.00 127.09 ?  579 ARG B O   1 
ATOM   3898  C CB  . ARG B  2 68  ? 5.323   4.882   173.236 1.00 129.41 ?  579 ARG B CB  1 
ATOM   3899  C CG  . ARG B  2 68  ? 6.504   4.461   172.383 1.00 127.20 ?  579 ARG B CG  1 
ATOM   3900  C CD  . ARG B  2 68  ? 7.481   3.632   173.254 1.00 128.16 ?  579 ARG B CD  1 
ATOM   3901  N NE  . ARG B  2 68  ? 6.954   2.344   173.708 1.00 132.42 ?  579 ARG B NE  1 
ATOM   3902  C CZ  . ARG B  2 68  ? 7.666   1.450   174.389 1.00 134.36 ?  579 ARG B CZ  1 
ATOM   3903  N NH1 . ARG B  2 68  ? 8.932   1.705   174.692 1.00 131.89 1  579 ARG B NH1 1 
ATOM   3904  N NH2 . ARG B  2 68  ? 7.118   0.303   174.770 1.00 139.69 ?  579 ARG B NH2 1 
ATOM   3905  N N   . VAL B  2 69  ? 1.966   4.884   172.829 1.00 115.44 ?  580 VAL B N   1 
ATOM   3906  C CA  . VAL B  2 69  ? 0.762   4.286   172.262 1.00 115.35 ?  580 VAL B CA  1 
ATOM   3907  C C   . VAL B  2 69  ? -0.007  5.285   171.399 1.00 115.30 ?  580 VAL B C   1 
ATOM   3908  O O   . VAL B  2 69  ? -0.447  4.959   170.293 1.00 114.64 ?  580 VAL B O   1 
ATOM   3909  C CB  . VAL B  2 69  ? -0.118  3.708   173.384 1.00 116.40 ?  580 VAL B CB  1 
ATOM   3910  C CG1 . VAL B  2 69  ? -1.539  3.490   172.891 1.00 116.61 ?  580 VAL B CG1 1 
ATOM   3911  C CG2 . VAL B  2 69  ? 0.475   2.401   173.894 1.00 116.40 ?  580 VAL B CG2 1 
ATOM   3912  N N   . LEU B  2 70  ? -0.145  6.532   171.869 1.00 120.91 ?  581 LEU B N   1 
ATOM   3913  C CA  . LEU B  2 70  ? -0.825  7.565   171.089 1.00 122.56 ?  581 LEU B CA  1 
ATOM   3914  C C   . LEU B  2 70  ? -0.041  7.975   169.851 1.00 118.19 ?  581 LEU B C   1 
ATOM   3915  O O   . LEU B  2 70  ? -0.637  8.467   168.885 1.00 119.55 ?  581 LEU B O   1 
ATOM   3916  C CB  . LEU B  2 70  ? -1.129  8.772   171.983 1.00 125.59 ?  581 LEU B CB  1 
ATOM   3917  C CG  . LEU B  2 70  ? -1.912  9.960   171.413 1.00 134.34 ?  581 LEU B CG  1 
ATOM   3918  C CD1 . LEU B  2 70  ? -2.881  10.497  172.461 1.00 149.91 ?  581 LEU B CD1 1 
ATOM   3919  C CD2 . LEU B  2 70  ? -0.977  11.063  170.930 1.00 131.04 ?  581 LEU B CD2 1 
ATOM   3920  N N   . ALA B  2 71  ? 1.275   7.768   169.854 1.00 129.30 ?  582 ALA B N   1 
ATOM   3921  C CA  . ALA B  2 71  ? 2.088   8.140   168.703 1.00 123.13 ?  582 ALA B CA  1 
ATOM   3922  C C   . ALA B  2 71  ? 1.738   7.262   167.515 1.00 119.23 ?  582 ALA B C   1 
ATOM   3923  O O   . ALA B  2 71  ? 1.602   7.747   166.385 1.00 120.05 ?  582 ALA B O   1 
ATOM   3924  C CB  . ALA B  2 71  ? 3.573   8.047   169.045 1.00 122.33 ?  582 ALA B CB  1 
ATOM   3925  N N   . VAL B  2 72  ? 1.552   5.966   167.763 1.00 112.93 ?  583 VAL B N   1 
ATOM   3926  C CA  . VAL B  2 72  ? 1.227   5.048   166.685 1.00 113.45 ?  583 VAL B CA  1 
ATOM   3927  C C   . VAL B  2 72  ? -0.255  5.135   166.360 1.00 118.28 ?  583 VAL B C   1 
ATOM   3928  O O   . VAL B  2 72  ? -0.657  4.820   165.235 1.00 119.35 ?  583 VAL B O   1 
ATOM   3929  C CB  . VAL B  2 72  ? 1.625   3.608   167.043 1.00 113.42 ?  583 VAL B CB  1 
ATOM   3930  C CG1 . VAL B  2 72  ? 3.136   3.515   167.307 1.00 109.67 ?  583 VAL B CG1 1 
ATOM   3931  C CG2 . VAL B  2 72  ? 0.819   3.119   168.219 1.00 117.39 ?  583 VAL B CG2 1 
ATOM   3932  N N   . GLU B  2 73  ? -1.083  5.561   167.316 1.00 115.14 ?  584 GLU B N   1 
ATOM   3933  C CA  . GLU B  2 73  ? -2.491  5.743   167.002 1.00 120.35 ?  584 GLU B CA  1 
ATOM   3934  C C   . GLU B  2 73  ? -2.650  6.948   166.095 1.00 120.38 ?  584 GLU B C   1 
ATOM   3935  O O   . GLU B  2 73  ? -3.521  6.964   165.219 1.00 123.49 ?  584 GLU B O   1 
ATOM   3936  C CB  . GLU B  2 73  ? -3.298  5.947   168.281 1.00 124.76 ?  584 GLU B CB  1 
ATOM   3937  C CG  . GLU B  2 73  ? -3.428  4.725   169.161 1.00 126.54 ?  584 GLU B CG  1 
ATOM   3938  C CD  . GLU B  2 73  ? -4.231  5.013   170.416 1.00 131.63 ?  584 GLU B CD  1 
ATOM   3939  O OE1 . GLU B  2 73  ? -4.425  6.205   170.743 1.00 133.08 ?  584 GLU B OE1 1 
ATOM   3940  O OE2 . GLU B  2 73  ? -4.657  4.049   171.083 1.00 135.88 -1 584 GLU B OE2 1 
ATOM   3941  N N   . ARG B  2 74  ? -1.811  7.963   166.302 1.00 118.88 ?  585 ARG B N   1 
ATOM   3942  C CA  . ARG B  2 74  ? -1.825  9.135   165.443 1.00 119.11 ?  585 ARG B CA  1 
ATOM   3943  C C   . ARG B  2 74  ? -1.261  8.798   164.068 1.00 116.37 ?  585 ARG B C   1 
ATOM   3944  O O   . ARG B  2 74  ? -1.684  9.379   163.062 1.00 118.51 ?  585 ARG B O   1 
ATOM   3945  C CB  . ARG B  2 74  ? -1.066  10.279  166.108 1.00 117.25 ?  585 ARG B CB  1 
ATOM   3946  C CG  . ARG B  2 74  ? -1.029  11.521  165.266 1.00 118.10 ?  585 ARG B CG  1 
ATOM   3947  C CD  . ARG B  2 74  ? -1.184  12.724  166.149 1.00 120.44 ?  585 ARG B CD  1 
ATOM   3948  N NE  . ARG B  2 74  ? -1.198  13.964  165.389 1.00 122.33 ?  585 ARG B NE  1 
ATOM   3949  C CZ  . ARG B  2 74  ? -1.228  15.161  165.955 1.00 124.78 ?  585 ARG B CZ  1 
ATOM   3950  N NH1 . ARG B  2 74  ? -1.251  15.249  167.275 1.00 131.47 1  585 ARG B NH1 1 
ATOM   3951  N NH2 . ARG B  2 74  ? -1.247  16.259  165.211 1.00 127.85 ?  585 ARG B NH2 1 
ATOM   3952  N N   . TYR B  2 75  ? -0.313  7.859   164.005 1.00 117.79 ?  586 TYR B N   1 
ATOM   3953  C CA  . TYR B  2 75  ? 0.274   7.482   162.725 1.00 115.65 ?  586 TYR B CA  1 
ATOM   3954  C C   . TYR B  2 75  ? -0.715  6.667   161.900 1.00 119.34 ?  586 TYR B C   1 
ATOM   3955  O O   . TYR B  2 75  ? -0.957  6.977   160.728 1.00 120.54 ?  586 TYR B O   1 
ATOM   3956  C CB  . TYR B  2 75  ? 1.572   6.708   162.961 1.00 111.40 ?  586 TYR B CB  1 
ATOM   3957  C CG  . TYR B  2 75  ? 2.211   6.168   161.705 1.00 110.29 ?  586 TYR B CG  1 
ATOM   3958  C CD1 . TYR B  2 75  ? 2.952   6.987   160.865 1.00 113.40 ?  586 TYR B CD1 1 
ATOM   3959  C CD2 . TYR B  2 75  ? 2.091   4.825   161.374 1.00 111.20 ?  586 TYR B CD2 1 
ATOM   3960  C CE1 . TYR B  2 75  ? 3.539   6.484   159.714 1.00 116.01 ?  586 TYR B CE1 1 
ATOM   3961  C CE2 . TYR B  2 75  ? 2.674   4.313   160.232 1.00 110.64 ?  586 TYR B CE2 1 
ATOM   3962  C CZ  . TYR B  2 75  ? 3.397   5.145   159.403 1.00 116.07 ?  586 TYR B CZ  1 
ATOM   3963  O OH  . TYR B  2 75  ? 3.979   4.637   158.262 1.00 117.35 ?  586 TYR B OH  1 
ATOM   3964  N N   . LEU B  2 76  ? -1.306  5.625   162.494 1.00 119.09 ?  587 LEU B N   1 
ATOM   3965  C CA  . LEU B  2 76  ? -2.262  4.818   161.744 1.00 119.61 ?  587 LEU B CA  1 
ATOM   3966  C C   . LEU B  2 76  ? -3.517  5.614   161.433 1.00 120.83 ?  587 LEU B C   1 
ATOM   3967  O O   . LEU B  2 76  ? -4.214  5.298   160.463 1.00 121.53 ?  587 LEU B O   1 
ATOM   3968  C CB  . LEU B  2 76  ? -2.588  3.517   162.474 1.00 119.38 ?  587 LEU B CB  1 
ATOM   3969  C CG  . LEU B  2 76  ? -1.367  2.600   162.530 1.00 118.41 ?  587 LEU B CG  1 
ATOM   3970  C CD1 . LEU B  2 76  ? -1.726  1.271   163.174 1.00 118.50 ?  587 LEU B CD1 1 
ATOM   3971  C CD2 . LEU B  2 76  ? -0.803  2.406   161.119 1.00 118.27 ?  587 LEU B CD2 1 
ATOM   3972  N N   . ARG B  2 77  ? -3.821  6.634   162.240 1.00 126.77 ?  588 ARG B N   1 
ATOM   3973  C CA  . ARG B  2 77  ? -4.966  7.481   161.939 1.00 132.01 ?  588 ARG B CA  1 
ATOM   3974  C C   . ARG B  2 77  ? -4.721  8.183   160.615 1.00 131.56 ?  588 ARG B C   1 
ATOM   3975  O O   . ARG B  2 77  ? -5.585  8.197   159.732 1.00 138.92 ?  588 ARG B O   1 
ATOM   3976  C CB  . ARG B  2 77  ? -5.200  8.505   163.055 1.00 133.45 ?  588 ARG B CB  1 
ATOM   3977  C CG  . ARG B  2 77  ? -6.360  9.468   162.781 1.00 139.48 ?  588 ARG B CG  1 
ATOM   3978  C CD  . ARG B  2 77  ? -6.293  10.754  163.620 1.00 141.37 ?  588 ARG B CD  1 
ATOM   3979  N NE  . ARG B  2 77  ? -4.954  11.343  163.711 1.00 134.70 ?  588 ARG B NE  1 
ATOM   3980  C CZ  . ARG B  2 77  ? -4.571  12.450  163.074 1.00 133.96 ?  588 ARG B CZ  1 
ATOM   3981  N NH1 . ARG B  2 77  ? -5.422  13.103  162.293 1.00 143.98 1  588 ARG B NH1 1 
ATOM   3982  N NH2 . ARG B  2 77  ? -3.334  12.909  163.220 1.00 129.73 ?  588 ARG B NH2 1 
ATOM   3983  N N   . ASP B  2 78  ? -3.534  8.777   160.467 1.00 130.27 ?  589 ASP B N   1 
ATOM   3984  C CA  . ASP B  2 78  ? -3.194  9.426   159.210 1.00 131.58 ?  589 ASP B CA  1 
ATOM   3985  C C   . ASP B  2 78  ? -3.008  8.392   158.103 1.00 129.02 ?  589 ASP B C   1 
ATOM   3986  O O   . ASP B  2 78  ? -3.375  8.640   156.949 1.00 133.21 ?  589 ASP B O   1 
ATOM   3987  C CB  . ASP B  2 78  ? -1.913  10.248  159.386 1.00 125.41 ?  589 ASP B CB  1 
ATOM   3988  C CG  . ASP B  2 78  ? -2.110  11.483  160.263 1.00 131.17 ?  589 ASP B CG  1 
ATOM   3989  O OD1 . ASP B  2 78  ? -3.219  12.059  160.270 1.00 141.31 ?  589 ASP B OD1 1 
ATOM   3990  O OD2 . ASP B  2 78  ? -1.144  11.872  160.957 1.00 125.59 -1 589 ASP B OD2 1 
ATOM   3991  N N   . GLN B  2 79  ? -2.453  7.219   158.436 1.00 128.97 ?  590 GLN B N   1 
ATOM   3992  C CA  . GLN B  2 79  ? -2.270  6.180   157.425 1.00 129.40 ?  590 GLN B CA  1 
ATOM   3993  C C   . GLN B  2 79  ? -3.592  5.582   156.976 1.00 135.39 ?  590 GLN B C   1 
ATOM   3994  O O   . GLN B  2 79  ? -3.725  5.183   155.814 1.00 141.47 ?  590 GLN B O   1 
ATOM   3995  C CB  . GLN B  2 79  ? -1.347  5.083   157.944 1.00 126.01 ?  590 GLN B CB  1 
ATOM   3996  C CG  . GLN B  2 79  ? 0.102   5.497   157.968 1.00 120.76 ?  590 GLN B CG  1 
ATOM   3997  C CD  . GLN B  2 79  ? 0.639   5.764   156.576 1.00 120.33 ?  590 GLN B CD  1 
ATOM   3998  O OE1 . GLN B  2 79  ? 0.242   5.111   155.607 1.00 123.35 ?  590 GLN B OE1 1 
ATOM   3999  N NE2 . GLN B  2 79  ? 1.547   6.726   156.467 1.00 119.60 ?  590 GLN B NE2 1 
ATOM   4000  N N   . GLN B  2 80  ? -4.575  5.500   157.872 1.00 128.22 ?  591 GLN B N   1 
ATOM   4001  C CA  . GLN B  2 80  ? -5.875  4.984   157.462 1.00 134.55 ?  591 GLN B CA  1 
ATOM   4002  C C   . GLN B  2 80  ? -6.551  5.978   156.534 1.00 138.28 ?  591 GLN B C   1 
ATOM   4003  O O   . GLN B  2 80  ? -7.142  5.591   155.520 1.00 142.38 ?  591 GLN B O   1 
ATOM   4004  C CB  . GLN B  2 80  ? -6.755  4.666   158.666 1.00 137.65 ?  591 GLN B CB  1 
ATOM   4005  C CG  . GLN B  2 80  ? -8.055  3.964   158.281 1.00 144.48 ?  591 GLN B CG  1 
ATOM   4006  C CD  . GLN B  2 80  ? -8.975  3.748   159.464 1.00 148.59 ?  591 GLN B CD  1 
ATOM   4007  O OE1 . GLN B  2 80  ? -8.818  4.383   160.505 1.00 153.56 ?  591 GLN B OE1 1 
ATOM   4008  N NE2 . GLN B  2 80  ? -9.933  2.837   159.316 1.00 157.60 ?  591 GLN B NE2 1 
ATOM   4009  N N   . LEU B  2 81  ? -6.492  7.265   156.886 1.00 135.76 ?  592 LEU B N   1 
ATOM   4010  C CA  . LEU B  2 81  ? -7.023  8.299   156.010 1.00 139.39 ?  592 LEU B CA  1 
ATOM   4011  C C   . LEU B  2 81  ? -6.262  8.300   154.695 1.00 138.82 ?  592 LEU B C   1 
ATOM   4012  O O   . LEU B  2 81  ? -6.852  8.456   153.620 1.00 144.38 ?  592 LEU B O   1 
ATOM   4013  C CB  . LEU B  2 81  ? -6.899  9.662   156.687 1.00 138.57 ?  592 LEU B CB  1 
ATOM   4014  C CG  . LEU B  2 81  ? -7.653  9.896   157.995 1.00 141.36 ?  592 LEU B CG  1 
ATOM   4015  C CD1 . LEU B  2 81  ? -7.429  11.315  158.494 1.00 141.34 ?  592 LEU B CD1 1 
ATOM   4016  C CD2 . LEU B  2 81  ? -9.129  9.617   157.815 1.00 149.54 ?  592 LEU B CD2 1 
ATOM   4017  N N   . LEU B  2 82  ? -4.941  8.123   154.767 1.00 148.39 ?  593 LEU B N   1 
ATOM   4018  C CA  . LEU B  2 82  ? -4.108  8.090   153.573 1.00 143.62 ?  593 LEU B CA  1 
ATOM   4019  C C   . LEU B  2 82  ? -4.377  6.855   152.724 1.00 149.85 ?  593 LEU B C   1 
ATOM   4020  O O   . LEU B  2 82  ? -4.047  6.852   151.534 1.00 152.14 ?  593 LEU B O   1 
ATOM   4021  C CB  . LEU B  2 82  ? -2.634  8.136   153.973 1.00 131.50 ?  593 LEU B CB  1 
ATOM   4022  C CG  . LEU B  2 82  ? -1.620  8.639   152.954 1.00 130.34 ?  593 LEU B CG  1 
ATOM   4023  C CD1 . LEU B  2 82  ? -1.946  10.069  152.576 1.00 129.36 ?  593 LEU B CD1 1 
ATOM   4024  C CD2 . LEU B  2 82  ? -0.223  8.540   153.536 1.00 124.36 ?  593 LEU B CD2 1 
ATOM   4025  N N   . GLY B  2 83  ? -4.971  5.815   153.310 1.00 160.61 ?  594 GLY B N   1 
ATOM   4026  C CA  . GLY B  2 83  ? -5.267  4.576   152.617 1.00 162.85 ?  594 GLY B CA  1 
ATOM   4027  C C   . GLY B  2 83  ? -6.665  4.562   152.034 1.00 171.93 ?  594 GLY B C   1 
ATOM   4028  O O   . GLY B  2 83  ? -6.864  4.119   150.899 1.00 180.78 ?  594 GLY B O   1 
ATOM   4029  N N   . ILE B  2 84  ? -7.647  5.046   152.800 1.00 151.55 ?  595 ILE B N   1 
ATOM   4030  C CA  . ILE B  2 84  ? -9.024  5.052   152.320 1.00 157.79 ?  595 ILE B CA  1 
ATOM   4031  C C   . ILE B  2 84  ? -9.207  6.060   151.201 1.00 163.52 ?  595 ILE B C   1 
ATOM   4032  O O   . ILE B  2 84  ? -10.167 5.955   150.428 1.00 176.39 ?  595 ILE B O   1 
ATOM   4033  C CB  . ILE B  2 84  ? -10.025 5.367   153.444 1.00 159.34 ?  595 ILE B CB  1 
ATOM   4034  C CG1 . ILE B  2 84  ? -9.728  6.746   154.035 1.00 159.92 ?  595 ILE B CG1 1 
ATOM   4035  C CG2 . ILE B  2 84  ? -9.984  4.289   154.512 1.00 164.21 ?  595 ILE B CG2 1 
ATOM   4036  C CD1 . ILE B  2 84  ? -10.566 7.089   155.237 1.00 164.21 ?  595 ILE B CD1 1 
ATOM   4037  N N   . TRP B  2 85  ? -8.316  7.042   151.095 1.00 175.09 ?  596 TRP B N   1 
ATOM   4038  C CA  . TRP B  2 85  ? -8.388  7.958   149.973 1.00 180.02 ?  596 TRP B CA  1 
ATOM   4039  C C   . TRP B  2 85  ? -7.759  7.273   148.765 1.00 184.46 ?  596 TRP B C   1 
ATOM   4040  O O   . TRP B  2 85  ? -7.269  6.144   148.851 1.00 184.74 ?  596 TRP B O   1 
ATOM   4041  C CB  . TRP B  2 85  ? -7.678  9.265   150.325 1.00 173.68 ?  596 TRP B CB  1 
ATOM   4042  C CG  . TRP B  2 85  ? -8.316  9.979   151.487 1.00 175.02 ?  596 TRP B CG  1 
ATOM   4043  C CD1 . TRP B  2 85  ? -9.551  9.736   152.014 1.00 180.80 ?  596 TRP B CD1 1 
ATOM   4044  C CD2 . TRP B  2 85  ? -7.743  11.031  152.280 1.00 172.90 ?  596 TRP B CD2 1 
ATOM   4045  N NE1 . TRP B  2 85  ? -9.786  10.573  153.076 1.00 180.67 ?  596 TRP B NE1 1 
ATOM   4046  C CE2 . TRP B  2 85  ? -8.695  11.379  153.260 1.00 176.32 ?  596 TRP B CE2 1 
ATOM   4047  C CE3 . TRP B  2 85  ? -6.524  11.714  152.253 1.00 171.51 ?  596 TRP B CE3 1 
ATOM   4048  C CZ2 . TRP B  2 85  ? -8.467  12.380  154.203 1.00 173.81 ?  596 TRP B CZ2 1 
ATOM   4049  C CZ3 . TRP B  2 85  ? -6.300  12.710  153.193 1.00 173.76 ?  596 TRP B CZ3 1 
ATOM   4050  C CH2 . TRP B  2 85  ? -7.268  13.032  154.153 1.00 172.68 ?  596 TRP B CH2 1 
ATOM   4051  N N   . GLY B  2 86  ? -7.739  7.945   147.624 1.00 177.20 ?  597 GLY B N   1 
ATOM   4052  C CA  . GLY B  2 86  ? -7.088  7.310   146.498 1.00 182.80 ?  597 GLY B CA  1 
ATOM   4053  C C   . GLY B  2 86  ? -5.592  7.481   146.501 1.00 180.69 ?  597 GLY B C   1 
ATOM   4054  O O   . GLY B  2 86  ? -5.012  7.905   145.498 1.00 185.20 ?  597 GLY B O   1 
ATOM   4055  N N   . CYS B  2 87  ? -4.945  7.131   147.610 1.00 158.81 ?  598 CYS B N   1 
ATOM   4056  C CA  . CYS B  2 87  ? -3.508  7.342   147.709 1.00 160.56 ?  598 CYS B CA  1 
ATOM   4057  C C   . CYS B  2 87  ? -2.811  6.092   148.219 1.00 162.13 ?  598 CYS B C   1 
ATOM   4058  O O   . CYS B  2 87  ? -2.204  5.370   147.424 1.00 164.16 ?  598 CYS B O   1 
ATOM   4059  C CB  . CYS B  2 87  ? -3.183  8.588   148.517 1.00 159.45 ?  598 CYS B CB  1 
ATOM   4060  S SG  . CYS B  2 87  ? -4.043  9.952   147.718 1.00 157.90 ?  598 CYS B SG  1 
ATOM   4061  N N   . SER B  2 88  ? -2.892  5.826   149.528 1.00 147.47 ?  599 SER B N   1 
ATOM   4062  C CA  . SER B  2 88  ? -2.143  4.734   150.143 1.00 149.05 ?  599 SER B CA  1 
ATOM   4063  C C   . SER B  2 88  ? -0.652  4.982   149.960 1.00 151.17 ?  599 SER B C   1 
ATOM   4064  O O   . SER B  2 88  ? 0.076   5.130   150.948 1.00 151.48 ?  599 SER B O   1 
ATOM   4065  C CB  . SER B  2 88  ? -2.567  3.379   149.562 1.00 149.97 ?  599 SER B CB  1 
ATOM   4066  O OG  . SER B  2 88  ? -1.888  2.307   150.191 1.00 151.51 ?  599 SER B OG  1 
ATOM   4067  N N   . GLY B  2 89  ? -0.173  4.992   148.720 1.00 152.75 ?  600 GLY B N   1 
ATOM   4068  C CA  . GLY B  2 89  ? 1.193   5.416   148.497 1.00 154.69 ?  600 GLY B CA  1 
ATOM   4069  C C   . GLY B  2 89  ? 1.371   6.840   149.001 1.00 153.42 ?  600 GLY B C   1 
ATOM   4070  O O   . GLY B  2 89  ? 0.702   7.774   148.549 1.00 151.97 ?  600 GLY B O   1 
ATOM   4071  N N   . LYS B  2 90  ? 2.289   7.011   149.948 1.00 154.04 ?  601 LYS B N   1 
ATOM   4072  C CA  . LYS B  2 90  ? 2.472   8.254   150.690 1.00 152.74 ?  601 LYS B CA  1 
ATOM   4073  C C   . LYS B  2 90  ? 3.083   9.406   149.893 1.00 153.39 ?  601 LYS B C   1 
ATOM   4074  O O   . LYS B  2 90  ? 3.028   9.422   148.658 1.00 154.27 ?  601 LYS B O   1 
ATOM   4075  C CB  . LYS B  2 90  ? 3.326   7.958   151.928 1.00 153.47 ?  601 LYS B CB  1 
ATOM   4076  C CG  . LYS B  2 90  ? 2.828   6.767   152.753 1.00 153.15 ?  601 LYS B CG  1 
ATOM   4077  C CD  . LYS B  2 90  ? 3.873   6.319   153.765 1.00 154.61 ?  601 LYS B CD  1 
ATOM   4078  C CE  . LYS B  2 90  ? 3.424   5.036   154.449 1.00 154.67 ?  601 LYS B CE  1 
ATOM   4079  N NZ  . LYS B  2 90  ? 4.429   4.529   155.421 1.00 156.26 1  601 LYS B NZ  1 
ATOM   4080  N N   . LEU B  2 91  ? 3.655   10.381  150.614 1.00 152.96 ?  602 LEU B N   1 
ATOM   4081  C CA  . LEU B  2 91  ? 4.277   11.573  150.036 1.00 153.50 ?  602 LEU B CA  1 
ATOM   4082  C C   . LEU B  2 91  ? 3.324   12.438  149.220 1.00 151.98 ?  602 LEU B C   1 
ATOM   4083  O O   . LEU B  2 91  ? 2.783   13.422  149.737 1.00 149.94 ?  602 LEU B O   1 
ATOM   4084  C CB  . LEU B  2 91  ? 5.494   11.194  149.195 1.00 156.53 ?  602 LEU B CB  1 
ATOM   4085  C CG  . LEU B  2 91  ? 6.586   10.483  149.988 1.00 158.32 ?  602 LEU B CG  1 
ATOM   4086  C CD1 . LEU B  2 91  ? 7.830   10.282  149.136 1.00 161.38 ?  602 LEU B CD1 1 
ATOM   4087  C CD2 . LEU B  2 91  ? 6.905   11.298  151.238 1.00 157.19 ?  602 LEU B CD2 1 
ATOM   4088  N N   . ILE B  2 92  ? 3.120   12.098  147.949 1.00 153.00 ?  603 ILE B N   1 
ATOM   4089  C CA  . ILE B  2 92  ? 2.253   12.880  147.078 1.00 151.84 ?  603 ILE B CA  1 
ATOM   4090  C C   . ILE B  2 92  ? 1.273   11.958  146.371 1.00 151.58 ?  603 ILE B C   1 
ATOM   4091  O O   . ILE B  2 92  ? 1.560   10.784  146.120 1.00 153.07 ?  603 ILE B O   1 
ATOM   4092  C CB  . ILE B  2 92  ? 3.071   13.671  146.032 1.00 153.58 ?  603 ILE B CB  1 
ATOM   4093  C CG1 . ILE B  2 92  ? 3.940   12.714  145.201 1.00 156.43 ?  603 ILE B CG1 1 
ATOM   4094  C CG2 . ILE B  2 92  ? 3.914   14.723  146.726 1.00 153.58 ?  603 ILE B CG2 1 
ATOM   4095  C CD1 . ILE B  2 92  ? 3.373   12.396  143.804 1.00 157.06 ?  603 ILE B CD1 1 
ATOM   4096  N N   . CYS B  2 93  ? 0.100   12.506  146.059 1.00 158.20 ?  604 CYS B N   1 
ATOM   4097  C CA  . CYS B  2 93  ? -0.925  11.802  145.302 1.00 157.83 ?  604 CYS B CA  1 
ATOM   4098  C C   . CYS B  2 93  ? -1.971  12.768  144.762 1.00 156.18 ?  604 CYS B C   1 
ATOM   4099  O O   . CYS B  2 93  ? -2.299  13.769  145.402 1.00 154.49 ?  604 CYS B O   1 
ATOM   4100  C CB  . CYS B  2 93  ? -1.562  10.771  146.235 1.00 156.75 ?  604 CYS B CB  1 
ATOM   4101  S SG  . CYS B  2 93  ? -3.207  10.277  145.869 1.00 155.05 ?  604 CYS B SG  1 
ATOM   4102  N N   . CYS B  2 94  ? -2.507  12.439  143.586 1.00 162.21 ?  605 CYS B N   1 
ATOM   4103  C CA  . CYS B  2 94  ? -3.522  13.256  142.938 1.00 160.93 ?  605 CYS B CA  1 
ATOM   4104  C C   . CYS B  2 94  ? -4.949  12.730  143.155 1.00 159.08 ?  605 CYS B C   1 
ATOM   4105  O O   . CYS B  2 94  ? -5.166  11.573  143.530 1.00 159.12 ?  605 CYS B O   1 
ATOM   4106  C CB  . CYS B  2 94  ? -3.174  13.399  141.453 1.00 162.83 ?  605 CYS B CB  1 
ATOM   4107  S SG  . CYS B  2 94  ? -1.606  14.330  141.200 1.00 164.83 ?  605 CYS B SG  1 
ATOM   4108  N N   . THR B  2 95  ? -5.931  13.609  142.915 1.00 177.69 ?  606 THR B N   1 
ATOM   4109  C CA  . THR B  2 95  ? -7.341  13.263  143.057 1.00 175.95 ?  606 THR B CA  1 
ATOM   4110  C C   . THR B  2 95  ? -8.168  13.957  141.984 1.00 175.61 ?  606 THR B C   1 
ATOM   4111  O O   . THR B  2 95  ? -7.765  14.981  141.421 1.00 176.16 ?  606 THR B O   1 
ATOM   4112  C CB  . THR B  2 95  ? -7.878  13.676  144.435 1.00 173.75 ?  606 THR B CB  1 
ATOM   4113  O OG1 . THR B  2 95  ? -6.853  13.523  145.411 1.00 174.20 ?  606 THR B OG1 1 
ATOM   4114  C CG2 . THR B  2 95  ? -9.067  12.826  144.837 1.00 172.45 ?  606 THR B CG2 1 
ATOM   4115  N N   . ASN B  2 96  ? -9.328  13.377  141.699 1.00 197.38 ?  607 ASN B N   1 
ATOM   4116  C CA  . ASN B  2 96  ? -10.282 13.901  140.720 1.00 206.85 ?  607 ASN B CA  1 
ATOM   4117  C C   . ASN B  2 96  ? -11.365 14.724  141.414 1.00 207.49 ?  607 ASN B C   1 
ATOM   4118  O O   . ASN B  2 96  ? -12.555 14.456  141.253 1.00 213.72 ?  607 ASN B O   1 
ATOM   4119  C CB  . ASN B  2 96  ? -10.886 12.775  139.884 1.00 215.81 ?  607 ASN B CB  1 
ATOM   4120  C CG  . ASN B  2 96  ? -9.837  11.969  139.122 1.00 218.20 ?  607 ASN B CG  1 
ATOM   4121  O OD1 . ASN B  2 96  ? -8.653  11.946  139.472 1.00 217.07 ?  607 ASN B OD1 1 
ATOM   4122  N ND2 . ASN B  2 96  ? -10.273 11.335  138.042 1.00 225.68 ?  607 ASN B ND2 1 
ATOM   4123  N N   . VAL B  2 97  ? -10.996 15.726  142.205 1.00 198.30 ?  608 VAL B N   1 
ATOM   4124  C CA  . VAL B  2 97  ? -11.969 16.562  142.896 1.00 199.89 ?  608 VAL B CA  1 
ATOM   4125  C C   . VAL B  2 97  ? -11.748 18.019  142.506 1.00 201.35 ?  608 VAL B C   1 
ATOM   4126  O O   . VAL B  2 97  ? -10.667 18.568  142.741 1.00 196.11 ?  608 VAL B O   1 
ATOM   4127  C CB  . VAL B  2 97  ? -11.889 16.394  144.421 1.00 196.90 ?  608 VAL B CB  1 
ATOM   4128  C CG1 . VAL B  2 97  ? -12.803 17.390  145.101 1.00 199.96 ?  608 VAL B CG1 1 
ATOM   4129  C CG2 . VAL B  2 97  ? -12.258 14.979  144.805 1.00 198.09 ?  608 VAL B CG2 1 
ATOM   4130  N N   . PRO B  2 98  ? -12.736 18.679  141.899 1.00 204.37 ?  609 PRO B N   1 
ATOM   4131  C CA  . PRO B  2 98  ? -12.583 20.095  141.524 1.00 208.16 ?  609 PRO B CA  1 
ATOM   4132  C C   . PRO B  2 98  ? -12.495 21.006  142.743 1.00 208.27 ?  609 PRO B C   1 
ATOM   4133  O O   . PRO B  2 98  ? -13.286 20.891  143.682 1.00 212.54 ?  609 PRO B O   1 
ATOM   4134  C CB  . PRO B  2 98  ? -13.844 20.379  140.699 1.00 218.01 ?  609 PRO B CB  1 
ATOM   4135  C CG  . PRO B  2 98  ? -14.838 19.377  141.187 1.00 222.53 ?  609 PRO B CG  1 
ATOM   4136  C CD  . PRO B  2 98  ? -14.051 18.142  141.511 1.00 212.76 ?  609 PRO B CD  1 
ATOM   4137  N N   . TRP B  2 99  ? -11.520 21.913  142.720 1.00 215.67 ?  610 TRP B N   1 
ATOM   4138  C CA  . TRP B  2 99  ? -11.298 22.842  143.824 1.00 219.08 ?  610 TRP B CA  1 
ATOM   4139  C C   . TRP B  2 99  ? -12.395 23.909  143.803 1.00 231.51 ?  610 TRP B C   1 
ATOM   4140  O O   . TRP B  2 99  ? -12.443 24.733  142.884 1.00 238.46 ?  610 TRP B O   1 
ATOM   4141  C CB  . TRP B  2 99  ? -9.927  23.495  143.697 1.00 212.07 ?  610 TRP B CB  1 
ATOM   4142  C CG  . TRP B  2 99  ? -9.617  24.407  144.833 1.00 218.58 ?  610 TRP B CG  1 
ATOM   4143  C CD1 . TRP B  2 99  ? -9.834  25.751  144.914 1.00 228.49 ?  610 TRP B CD1 1 
ATOM   4144  C CD2 . TRP B  2 99  ? -8.923  24.037  146.030 1.00 211.51 ?  610 TRP B CD2 1 
ATOM   4145  N NE1 . TRP B  2 99  ? -9.374  26.228  146.123 1.00 229.20 ?  610 TRP B NE1 1 
ATOM   4146  C CE2 . TRP B  2 99  ? -8.801  25.194  146.820 1.00 217.08 ?  610 TRP B CE2 1 
ATOM   4147  C CE3 . TRP B  2 99  ? -8.411  22.830  146.516 1.00 195.81 ?  610 TRP B CE3 1 
ATOM   4148  C CZ2 . TRP B  2 99  ? -8.188  25.179  148.074 1.00 206.12 ?  610 TRP B CZ2 1 
ATOM   4149  C CZ3 . TRP B  2 99  ? -7.806  22.814  147.757 1.00 188.44 ?  610 TRP B CZ3 1 
ATOM   4150  C CH2 . TRP B  2 99  ? -7.698  23.981  148.523 1.00 193.25 ?  610 TRP B CH2 1 
ATOM   4151  N N   . ASN B  2 100 ? -13.277 23.905  144.804 1.00 224.16 ?  611 ASN B N   1 
ATOM   4152  C CA  . ASN B  2 100 ? -14.353 24.893  144.878 1.00 233.82 ?  611 ASN B CA  1 
ATOM   4153  C C   . ASN B  2 100 ? -13.782 26.286  145.157 1.00 233.59 ?  611 ASN B C   1 
ATOM   4154  O O   . ASN B  2 100 ? -12.967 26.465  146.067 1.00 228.51 ?  611 ASN B O   1 
ATOM   4155  C CB  . ASN B  2 100 ? -15.356 24.470  145.956 1.00 239.82 ?  611 ASN B CB  1 
ATOM   4156  C CG  . ASN B  2 100 ? -16.742 25.074  145.760 1.00 251.50 ?  611 ASN B CG  1 
ATOM   4157  O OD1 . ASN B  2 100 ? -17.005 25.762  144.774 1.00 255.44 ?  611 ASN B OD1 1 
ATOM   4158  N ND2 . ASN B  2 100 ? -17.646 24.782  146.700 1.00 257.47 ?  611 ASN B ND2 1 
ATOM   4159  N N   . SER B  2 101 ? -14.216 27.276  144.364 1.00 234.76 ?  612 SER B N   1 
ATOM   4160  C CA  . SER B  2 101 ? -13.698 28.643  144.457 1.00 235.32 ?  612 SER B CA  1 
ATOM   4161  C C   . SER B  2 101 ? -13.982 29.317  145.796 1.00 239.53 ?  612 SER B C   1 
ATOM   4162  O O   . SER B  2 101 ? -13.274 30.262  146.162 1.00 238.13 ?  612 SER B O   1 
ATOM   4163  C CB  . SER B  2 101 ? -14.272 29.500  143.327 1.00 242.08 ?  612 SER B CB  1 
ATOM   4164  O OG  . SER B  2 101 ? -13.870 30.853  143.462 1.00 243.64 ?  612 SER B OG  1 
ATOM   4165  N N   . SER B  2 102 ? -15.001 28.868  146.527 1.00 232.48 ?  613 SER B N   1 
ATOM   4166  C CA  . SER B  2 102 ? -15.346 29.470  147.811 1.00 237.45 ?  613 SER B CA  1 
ATOM   4167  C C   . SER B  2 102 ? -14.269 29.244  148.865 1.00 229.30 ?  613 SER B C   1 
ATOM   4168  O O   . SER B  2 102 ? -14.250 29.949  149.879 1.00 231.87 ?  613 SER B O   1 
ATOM   4169  C CB  . SER B  2 102 ? -16.683 28.924  148.311 1.00 245.47 ?  613 SER B CB  1 
ATOM   4170  O OG  . SER B  2 102 ? -16.644 27.513  148.426 1.00 249.59 ?  613 SER B OG  1 
ATOM   4171  N N   . TRP B  2 103 ? -13.379 28.277  148.643 1.00 240.35 ?  614 TRP B N   1 
ATOM   4172  C CA  . TRP B  2 103 ? -12.303 27.937  149.574 1.00 232.24 ?  614 TRP B CA  1 
ATOM   4173  C C   . TRP B  2 103 ? -11.078 28.835  149.374 1.00 226.74 ?  614 TRP B C   1 
ATOM   4174  O O   . TRP B  2 103 ? -9.981  28.379  149.052 1.00 218.15 ?  614 TRP B O   1 
ATOM   4175  C CB  . TRP B  2 103 ? -11.925 26.476  149.374 1.00 225.24 ?  614 TRP B CB  1 
ATOM   4176  C CG  . TRP B  2 103 ? -13.076 25.529  149.486 1.00 230.47 ?  614 TRP B CG  1 
ATOM   4177  C CD1 . TRP B  2 103 ? -14.267 25.747  150.114 1.00 239.69 ?  614 TRP B CD1 1 
ATOM   4178  C CD2 . TRP B  2 103 ? -13.166 24.229  148.893 1.00 227.33 ?  614 TRP B CD2 1 
ATOM   4179  N NE1 . TRP B  2 103 ? -15.082 24.648  149.974 1.00 242.46 ?  614 TRP B NE1 1 
ATOM   4180  C CE2 . TRP B  2 103 ? -14.428 23.703  149.227 1.00 234.89 ?  614 TRP B CE2 1 
ATOM   4181  C CE3 . TRP B  2 103 ? -12.293 23.452  148.124 1.00 219.32 ?  614 TRP B CE3 1 
ATOM   4182  C CZ2 . TRP B  2 103 ? -14.841 22.436  148.818 1.00 234.55 ?  614 TRP B CZ2 1 
ATOM   4183  C CZ3 . TRP B  2 103 ? -12.703 22.196  147.720 1.00 219.07 ?  614 TRP B CZ3 1 
ATOM   4184  C CH2 . TRP B  2 103 ? -13.965 21.701  148.067 1.00 226.55 ?  614 TRP B CH2 1 
ATOM   4185  N N   . SER B  2 104 ? -11.288 30.139  149.579 1.00 240.36 ?  615 SER B N   1 
ATOM   4186  C CA  . SER B  2 104 ? -10.240 31.143  149.400 1.00 236.58 ?  615 SER B CA  1 
ATOM   4187  C C   . SER B  2 104 ? -9.659  31.093  147.992 1.00 232.21 ?  615 SER B C   1 
ATOM   4188  O O   . SER B  2 104 ? -8.635  30.444  147.758 1.00 223.68 ?  615 SER B O   1 
ATOM   4189  C CB  . SER B  2 104 ? -9.128  30.959  150.439 1.00 229.25 ?  615 SER B CB  1 
ATOM   4190  O OG  . SER B  2 104 ? -8.102  31.925  150.273 1.00 225.95 ?  615 SER B OG  1 
ATOM   4191  N N   . ASN B  2 105 ? -10.299 31.785  147.056 1.00 231.60 ?  616 ASN B N   1 
ATOM   4192  C CA  . ASN B  2 105 ? -9.892  31.788  145.651 1.00 227.44 ?  616 ASN B CA  1 
ATOM   4193  C C   . ASN B  2 105 ? -8.541  32.481  145.491 1.00 219.68 ?  616 ASN B C   1 
ATOM   4194  O O   . ASN B  2 105 ? -8.457  33.707  145.389 1.00 224.51 ?  616 ASN B O   1 
ATOM   4195  C CB  . ASN B  2 105 ? -10.977 32.451  144.810 1.00 236.73 ?  616 ASN B CB  1 
ATOM   4196  C CG  . ASN B  2 105 ? -11.405 33.795  145.368 1.00 248.05 ?  616 ASN B CG  1 
ATOM   4197  O OD1 . ASN B  2 105 ? -12.319 33.866  146.189 1.00 259.36 ?  616 ASN B OD1 1 
ATOM   4198  N ND2 . ASN B  2 105 ? -10.761 34.866  144.917 1.00 246.80 ?  616 ASN B ND2 1 
ATOM   4199  N N   . ARG B  2 106 ? -7.473  31.682  145.480 1.00 222.09 ?  617 ARG B N   1 
ATOM   4200  C CA  . ARG B  2 106 ? -6.104  32.130  145.267 1.00 215.92 ?  617 ARG B CA  1 
ATOM   4201  C C   . ARG B  2 106 ? -5.574  31.504  143.980 1.00 211.16 ?  617 ARG B C   1 
ATOM   4202  O O   . ARG B  2 106 ? -6.153  30.552  143.452 1.00 211.49 ?  617 ARG B O   1 
ATOM   4203  C CB  . ARG B  2 106 ? -5.204  31.787  146.461 1.00 209.76 ?  617 ARG B CB  1 
ATOM   4204  C CG  . ARG B  2 106 ? -4.213  32.889  146.811 1.00 208.13 ?  617 ARG B CG  1 
ATOM   4205  C CD  . ARG B  2 106 ? -4.943  34.159  147.222 1.00 216.59 ?  617 ARG B CD  1 
ATOM   4206  N NE  . ARG B  2 106 ? -5.351  34.138  148.623 1.00 218.92 ?  617 ARG B NE  1 
ATOM   4207  C CZ  . ARG B  2 106 ? -4.660  34.700  149.609 1.00 217.41 ?  617 ARG B CZ  1 
ATOM   4208  N NH1 . ARG B  2 106 ? -3.523  35.329  149.348 1.00 213.69 1  617 ARG B NH1 1 
ATOM   4209  N NH2 . ARG B  2 106 ? -5.107  34.634  150.856 1.00 220.05 ?  617 ARG B NH2 1 
ATOM   4210  N N   . ASN B  2 107 ? -4.464  32.045  143.470 1.00 234.92 ?  618 ASN B N   1 
ATOM   4211  C CA  . ASN B  2 107 ? -3.874  31.531  142.240 1.00 233.14 ?  618 ASN B CA  1 
ATOM   4212  C C   . ASN B  2 107 ? -2.791  30.473  142.462 1.00 222.76 ?  618 ASN B C   1 
ATOM   4213  O O   . ASN B  2 107 ? -2.262  30.295  143.561 1.00 218.75 ?  618 ASN B O   1 
ATOM   4214  C CB  . ASN B  2 107 ? -3.233  32.706  141.499 1.00 234.11 ?  618 ASN B CB  1 
ATOM   4215  C CG  . ASN B  2 107 ? -3.071  32.474  140.020 1.00 238.03 ?  618 ASN B CG  1 
ATOM   4216  O OD1 . ASN B  2 107 ? -2.701  31.389  139.571 1.00 235.77 ?  618 ASN B OD1 1 
ATOM   4217  N ND2 . ASN B  2 107 ? -3.309  33.524  139.250 1.00 254.01 ?  618 ASN B ND2 1 
ATOM   4218  N N   . LEU B  2 108 ? -2.462  29.770  141.364 1.00 224.92 ?  619 LEU B N   1 
ATOM   4219  C CA  . LEU B  2 108 ? -1.452  28.713  141.404 1.00 215.42 ?  619 LEU B CA  1 
ATOM   4220  C C   . LEU B  2 108 ? -0.096  29.280  141.794 1.00 206.97 ?  619 LEU B C   1 
ATOM   4221  O O   . LEU B  2 108 ? 0.634   28.694  142.603 1.00 201.65 ?  619 LEU B O   1 
ATOM   4222  C CB  . LEU B  2 108 ? -1.370  28.005  140.050 1.00 210.94 ?  619 LEU B CB  1 
ATOM   4223  C CG  . LEU B  2 108 ? -0.150  27.122  139.747 1.00 196.24 ?  619 LEU B CG  1 
ATOM   4224  C CD1 . LEU B  2 108 ? 0.013   25.994  140.753 1.00 186.89 ?  619 LEU B CD1 1 
ATOM   4225  C CD2 . LEU B  2 108 ? -0.225  26.556  138.343 1.00 201.63 ?  619 LEU B CD2 1 
ATOM   4226  N N   . SER B  2 109 ? 0.249   30.434  141.223 1.00 191.44 ?  620 SER B N   1 
ATOM   4227  C CA  . SER B  2 109 ? 1.519   31.091  141.469 1.00 190.45 ?  620 SER B CA  1 
ATOM   4228  C C   . SER B  2 109 ? 1.462   31.923  142.734 1.00 191.55 ?  620 SER B C   1 
ATOM   4229  O O   . SER B  2 109 ? 2.497   32.425  143.186 1.00 190.85 ?  620 SER B O   1 
ATOM   4230  C CB  . SER B  2 109 ? 1.895   31.964  140.268 1.00 189.92 ?  620 SER B CB  1 
ATOM   4231  O OG  . SER B  2 109 ? 3.197   32.501  140.410 1.00 188.79 ?  620 SER B OG  1 
ATOM   4232  N N   . GLU B  2 110 ? 0.264   32.081  143.291 1.00 191.71 ?  621 GLU B N   1 
ATOM   4233  C CA  . GLU B  2 110 ? 0.026   32.854  144.492 1.00 194.62 ?  621 GLU B CA  1 
ATOM   4234  C C   . GLU B  2 110 ? -0.032  31.980  145.741 1.00 191.64 ?  621 GLU B C   1 
ATOM   4235  O O   . GLU B  2 110 ? -0.096  32.521  146.851 1.00 193.21 ?  621 GLU B O   1 
ATOM   4236  C CB  . GLU B  2 110 ? -1.312  33.591  144.326 1.00 205.29 ?  621 GLU B CB  1 
ATOM   4237  C CG  . GLU B  2 110 ? -1.245  35.073  144.000 1.00 210.93 ?  621 GLU B CG  1 
ATOM   4238  C CD  . GLU B  2 110 ? -2.631  35.689  143.852 1.00 217.84 ?  621 GLU B CD  1 
ATOM   4239  O OE1 . GLU B  2 110 ? -3.623  35.024  144.223 1.00 222.35 ?  621 GLU B OE1 1 
ATOM   4240  O OE2 . GLU B  2 110 ? -2.732  36.826  143.343 1.00 221.54 -1 621 GLU B OE2 1 
ATOM   4241  N N   . ILE B  2 111 ? -0.012  30.652  145.583 1.00 194.59 ?  622 ILE B N   1 
ATOM   4242  C CA  . ILE B  2 111 ? -0.056  29.703  146.700 1.00 191.64 ?  622 ILE B CA  1 
ATOM   4243  C C   . ILE B  2 111 ? 1.305   29.053  146.942 1.00 184.13 ?  622 ILE B C   1 
ATOM   4244  O O   . ILE B  2 111 ? 1.850   29.119  148.045 1.00 181.96 ?  622 ILE B O   1 
ATOM   4245  C CB  . ILE B  2 111 ? -1.146  28.631  146.473 1.00 193.41 ?  622 ILE B CB  1 
ATOM   4246  C CG1 . ILE B  2 111 ? -2.543  29.250  146.514 1.00 201.40 ?  622 ILE B CG1 1 
ATOM   4247  C CG2 . ILE B  2 111 ? -1.013  27.497  147.491 1.00 189.68 ?  622 ILE B CG2 1 
ATOM   4248  C CD1 . ILE B  2 111 ? -3.635  28.272  146.159 1.00 204.15 ?  622 ILE B CD1 1 
ATOM   4249  N N   . TRP B  2 112 ? 1.883   28.440  145.903 1.00 181.30 ?  623 TRP B N   1 
ATOM   4250  C CA  . TRP B  2 112 ? 3.133   27.688  145.978 1.00 180.87 ?  623 TRP B CA  1 
ATOM   4251  C C   . TRP B  2 112 ? 4.363   28.580  145.966 1.00 193.49 ?  623 TRP B C   1 
ATOM   4252  O O   . TRP B  2 112 ? 5.462   28.098  146.259 1.00 196.22 ?  623 TRP B O   1 
ATOM   4253  C CB  . TRP B  2 112 ? 3.207   26.693  144.811 1.00 174.03 ?  623 TRP B CB  1 
ATOM   4254  C CG  . TRP B  2 112 ? 2.057   25.722  144.730 1.00 173.30 ?  623 TRP B CG  1 
ATOM   4255  C CD1 . TRP B  2 112 ? 0.979   25.808  143.905 1.00 180.50 ?  623 TRP B CD1 1 
ATOM   4256  C CD2 . TRP B  2 112 ? 1.961   24.439  145.373 1.00 173.52 ?  623 TRP B CD2 1 
ATOM   4257  N NE1 . TRP B  2 112 ? 0.163   24.716  144.066 1.00 181.03 ?  623 TRP B NE1 1 
ATOM   4258  C CE2 . TRP B  2 112 ? 0.750   23.853  144.952 1.00 179.08 ?  623 TRP B CE2 1 
ATOM   4259  C CE3 . TRP B  2 112 ? 2.759   23.750  146.291 1.00 168.91 ?  623 TRP B CE3 1 
ATOM   4260  C CZ2 . TRP B  2 112 ? 0.319   22.612  145.414 1.00 179.05 ?  623 TRP B CZ2 1 
ATOM   4261  C CZ3 . TRP B  2 112 ? 2.327   22.515  146.751 1.00 166.43 ?  623 TRP B CZ3 1 
ATOM   4262  C CH2 . TRP B  2 112 ? 1.119   21.961  146.311 1.00 171.68 ?  623 TRP B CH2 1 
ATOM   4263  N N   . ASP B  2 113 ? 4.201   29.865  145.654 1.00 185.14 ?  624 ASP B N   1 
ATOM   4264  C CA  . ASP B  2 113 ? 5.319   30.792  145.546 1.00 196.93 ?  624 ASP B CA  1 
ATOM   4265  C C   . ASP B  2 113 ? 5.024   32.060  146.333 1.00 199.83 ?  624 ASP B C   1 
ATOM   4266  O O   . ASP B  2 113 ? 5.631   33.106  146.079 1.00 205.21 ?  624 ASP B O   1 
ATOM   4267  C CB  . ASP B  2 113 ? 5.591   31.134  144.078 1.00 205.44 ?  624 ASP B CB  1 
ATOM   4268  C CG  . ASP B  2 113 ? 6.066   29.935  143.273 1.00 213.97 ?  624 ASP B CG  1 
ATOM   4269  O OD1 . ASP B  2 113 ? 6.794   29.088  143.832 1.00 213.36 ?  624 ASP B OD1 1 
ATOM   4270  O OD2 . ASP B  2 113 ? 5.700   29.838  142.081 1.00 215.89 -1 624 ASP B OD2 1 
ATOM   4271  N N   . ASN B  2 114 ? 4.093   31.977  147.288 1.00 194.95 ?  625 ASN B N   1 
ATOM   4272  C CA  . ASN B  2 114 ? 3.755   33.149  148.100 1.00 197.70 ?  625 ASN B CA  1 
ATOM   4273  C C   . ASN B  2 114 ? 3.037   32.763  149.388 1.00 193.11 ?  625 ASN B C   1 
ATOM   4274  O O   . ASN B  2 114 ? 2.350   33.617  149.956 1.00 199.46 ?  625 ASN B O   1 
ATOM   4275  C CB  . ASN B  2 114 ? 2.894   34.114  147.267 1.00 198.08 ?  625 ASN B CB  1 
ATOM   4276  C CG  . ASN B  2 114 ? 2.831   35.512  147.859 1.00 206.62 ?  625 ASN B CG  1 
ATOM   4277  O OD1 . ASN B  2 114 ? 3.697   35.906  148.639 1.00 215.12 ?  625 ASN B OD1 1 
ATOM   4278  N ND2 . ASN B  2 114 ? 1.814   36.276  147.473 1.00 207.99 ?  625 ASN B ND2 1 
ATOM   4279  N N   . MET B  2 115 ? 3.154   31.527  149.868 1.00 195.57 ?  626 MET B N   1 
ATOM   4280  C CA  . MET B  2 115 ? 2.425   31.132  151.064 1.00 188.90 ?  626 MET B CA  1 
ATOM   4281  C C   . MET B  2 115 ? 3.087   29.944  151.743 1.00 185.19 ?  626 MET B C   1 
ATOM   4282  O O   . MET B  2 115 ? 3.547   29.018  151.070 1.00 182.38 ?  626 MET B O   1 
ATOM   4283  C CB  . MET B  2 115 ? 0.985   30.760  150.704 1.00 179.10 ?  626 MET B CB  1 
ATOM   4284  C CG  . MET B  2 115 ? -0.033  31.001  151.789 1.00 178.67 ?  626 MET B CG  1 
ATOM   4285  S SD  . MET B  2 115 ? -1.693  30.925  151.099 1.00 185.05 ?  626 MET B SD  1 
ATOM   4286  C CE  . MET B  2 115 ? -2.670  31.257  152.554 1.00 188.80 ?  626 MET B CE  1 
ATOM   4287  N N   . THR B  2 116 ? 3.137   29.981  153.072 1.00 178.79 ?  627 THR B N   1 
ATOM   4288  C CA  . THR B  2 116 ? 3.692   28.874  153.834 1.00 172.89 ?  627 THR B CA  1 
ATOM   4289  C C   . THR B  2 116 ? 2.575   27.900  154.194 1.00 159.50 ?  627 THR B C   1 
ATOM   4290  O O   . THR B  2 116 ? 1.389   28.234  154.158 1.00 161.88 ?  627 THR B O   1 
ATOM   4291  C CB  . THR B  2 116 ? 4.376   29.362  155.112 1.00 177.50 ?  627 THR B CB  1 
ATOM   4292  O OG1 . THR B  2 116 ? 3.401   29.941  155.988 1.00 176.06 ?  627 THR B OG1 1 
ATOM   4293  C CG2 . THR B  2 116 ? 5.430   30.401  154.788 1.00 184.24 ?  627 THR B CG2 1 
ATOM   4294  N N   . TRP B  2 117 ? 2.970   26.677  154.543 1.00 160.14 ?  628 TRP B N   1 
ATOM   4295  C CA  . TRP B  2 117 ? 1.981   25.666  154.897 1.00 162.81 ?  628 TRP B CA  1 
ATOM   4296  C C   . TRP B  2 117 ? 1.235   26.032  156.176 1.00 167.14 ?  628 TRP B C   1 
ATOM   4297  O O   . TRP B  2 117 ? 0.044   25.726  156.311 1.00 172.05 ?  628 TRP B O   1 
ATOM   4298  C CB  . TRP B  2 117 ? 2.663   24.309  155.025 1.00 158.98 ?  628 TRP B CB  1 
ATOM   4299  C CG  . TRP B  2 117 ? 2.848   23.613  153.705 1.00 156.74 ?  628 TRP B CG  1 
ATOM   4300  C CD1 . TRP B  2 117 ? 3.984   23.593  152.947 1.00 156.85 ?  628 TRP B CD1 1 
ATOM   4301  C CD2 . TRP B  2 117 ? 1.878   22.833  152.993 1.00 160.13 ?  628 TRP B CD2 1 
ATOM   4302  N NE1 . TRP B  2 117 ? 3.781   22.852  151.808 1.00 156.93 ?  628 TRP B NE1 1 
ATOM   4303  C CE2 . TRP B  2 117 ? 2.497   22.374  151.812 1.00 159.47 ?  628 TRP B CE2 1 
ATOM   4304  C CE3 . TRP B  2 117 ? 0.547   22.479  153.238 1.00 162.04 ?  628 TRP B CE3 1 
ATOM   4305  C CZ2 . TRP B  2 117 ? 1.832   21.578  150.879 1.00 160.07 ?  628 TRP B CZ2 1 
ATOM   4306  C CZ3 . TRP B  2 117 ? -0.112  21.690  152.311 1.00 164.34 ?  628 TRP B CZ3 1 
ATOM   4307  C CH2 . TRP B  2 117 ? 0.532   21.247  151.146 1.00 164.35 ?  628 TRP B CH2 1 
ATOM   4308  N N   . LEU B  2 118 ? 1.922   26.686  157.117 1.00 162.58 ?  629 LEU B N   1 
ATOM   4309  C CA  . LEU B  2 118 ? 1.292   27.134  158.356 1.00 165.52 ?  629 LEU B CA  1 
ATOM   4310  C C   . LEU B  2 118 ? 0.262   28.222  158.091 1.00 171.83 ?  629 LEU B C   1 
ATOM   4311  O O   . LEU B  2 118 ? -0.834  28.209  158.665 1.00 175.83 ?  629 LEU B O   1 
ATOM   4312  C CB  . LEU B  2 118 ? 2.369   27.656  159.302 1.00 163.98 ?  629 LEU B CB  1 
ATOM   4313  C CG  . LEU B  2 118 ? 3.295   26.614  159.911 1.00 158.17 ?  629 LEU B CG  1 
ATOM   4314  C CD1 . LEU B  2 118 ? 4.363   27.312  160.727 1.00 161.22 ?  629 LEU B CD1 1 
ATOM   4315  C CD2 . LEU B  2 118 ? 2.503   25.640  160.765 1.00 158.16 ?  629 LEU B CD2 1 
ATOM   4316  N N   . GLN B  2 119 ? 0.598   29.163  157.210 1.00 163.96 ?  630 GLN B N   1 
ATOM   4317  C CA  . GLN B  2 119 ? -0.313  30.250  156.886 1.00 170.20 ?  630 GLN B CA  1 
ATOM   4318  C C   . GLN B  2 119 ? -1.479  29.721  156.071 1.00 173.15 ?  630 GLN B C   1 
ATOM   4319  O O   . GLN B  2 119 ? -2.601  30.231  156.177 1.00 179.14 ?  630 GLN B O   1 
ATOM   4320  C CB  . GLN B  2 119 ? 0.450   31.343  156.142 1.00 174.76 ?  630 GLN B CB  1 
ATOM   4321  C CG  . GLN B  2 119 ? -0.312  32.616  155.862 1.00 185.65 ?  630 GLN B CG  1 
ATOM   4322  C CD  . GLN B  2 119 ? 0.546   33.617  155.116 1.00 200.17 ?  630 GLN B CD  1 
ATOM   4323  O OE1 . GLN B  2 119 ? 1.728   33.786  155.421 1.00 200.83 ?  630 GLN B OE1 1 
ATOM   4324  N NE2 . GLN B  2 119 ? -0.041  34.280  154.126 1.00 206.08 ?  630 GLN B NE2 1 
ATOM   4325  N N   . TRP B  2 120 ? -1.220  28.700  155.258 1.00 171.82 ?  631 TRP B N   1 
ATOM   4326  C CA  . TRP B  2 120 ? -2.258  28.120  154.421 1.00 174.42 ?  631 TRP B CA  1 
ATOM   4327  C C   . TRP B  2 120 ? -3.227  27.304  155.264 1.00 176.29 ?  631 TRP B C   1 
ATOM   4328  O O   . TRP B  2 120 ? -4.446  27.418  155.099 1.00 182.97 ?  631 TRP B O   1 
ATOM   4329  C CB  . TRP B  2 120 ? -1.594  27.276  153.331 1.00 169.98 ?  631 TRP B CB  1 
ATOM   4330  C CG  . TRP B  2 120 ? -2.500  26.424  152.519 1.00 171.71 ?  631 TRP B CG  1 
ATOM   4331  C CD1 . TRP B  2 120 ? -2.758  25.097  152.700 1.00 169.79 ?  631 TRP B CD1 1 
ATOM   4332  C CD2 . TRP B  2 120 ? -3.292  26.840  151.407 1.00 176.77 ?  631 TRP B CD2 1 
ATOM   4333  N NE1 . TRP B  2 120 ? -3.648  24.656  151.753 1.00 173.08 ?  631 TRP B NE1 1 
ATOM   4334  C CE2 . TRP B  2 120 ? -3.994  25.710  150.948 1.00 177.44 ?  631 TRP B CE2 1 
ATOM   4335  C CE3 . TRP B  2 120 ? -3.472  28.060  150.749 1.00 181.35 ?  631 TRP B CE3 1 
ATOM   4336  C CZ2 . TRP B  2 120 ? -4.865  25.764  149.866 1.00 182.27 ?  631 TRP B CZ2 1 
ATOM   4337  C CZ3 . TRP B  2 120 ? -4.334  28.112  149.675 1.00 188.75 ?  631 TRP B CZ3 1 
ATOM   4338  C CH2 . TRP B  2 120 ? -5.020  26.972  149.243 1.00 187.52 ?  631 TRP B CH2 1 
ATOM   4339  N N   . ASP B  2 121 ? -2.708  26.494  156.192 1.00 171.12 ?  632 ASP B N   1 
ATOM   4340  C CA  . ASP B  2 121 ? -3.590  25.679  157.017 1.00 172.84 ?  632 ASP B CA  1 
ATOM   4341  C C   . ASP B  2 121 ? -4.485  26.532  157.910 1.00 178.91 ?  632 ASP B C   1 
ATOM   4342  O O   . ASP B  2 121 ? -5.529  26.050  158.359 1.00 182.68 ?  632 ASP B O   1 
ATOM   4343  C CB  . ASP B  2 121 ? -2.776  24.706  157.871 1.00 167.97 ?  632 ASP B CB  1 
ATOM   4344  C CG  . ASP B  2 121 ? -3.651  23.733  158.636 1.00 168.99 ?  632 ASP B CG  1 
ATOM   4345  O OD1 . ASP B  2 121 ? -3.974  22.658  158.087 1.00 168.19 ?  632 ASP B OD1 1 
ATOM   4346  O OD2 . ASP B  2 121 ? -4.031  24.052  159.782 1.00 173.27 -1 632 ASP B OD2 1 
ATOM   4347  N N   . LYS B  2 122 ? -4.103  27.787  158.175 1.00 175.54 ?  633 LYS B N   1 
ATOM   4348  C CA  . LYS B  2 122 ? -4.921  28.638  159.034 1.00 186.56 ?  633 LYS B CA  1 
ATOM   4349  C C   . LYS B  2 122 ? -6.178  29.089  158.311 1.00 197.39 ?  633 LYS B C   1 
ATOM   4350  O O   . LYS B  2 122 ? -7.223  29.293  158.940 1.00 207.64 ?  633 LYS B O   1 
ATOM   4351  C CB  . LYS B  2 122 ? -4.130  29.851  159.521 1.00 184.90 ?  633 LYS B CB  1 
ATOM   4352  C CG  . LYS B  2 122 ? -3.543  29.682  160.911 1.00 187.44 ?  633 LYS B CG  1 
ATOM   4353  C CD  . LYS B  2 122 ? -3.293  31.033  161.566 1.00 194.26 ?  633 LYS B CD  1 
ATOM   4354  C CE  . LYS B  2 122 ? -4.599  31.722  161.945 1.00 206.75 ?  633 LYS B CE  1 
ATOM   4355  N NZ  . LYS B  2 122 ? -5.372  30.936  162.946 1.00 209.87 1  633 LYS B NZ  1 
ATOM   4356  N N   . GLU B  2 123 ? -6.092  29.237  156.991 1.00 189.42 ?  634 GLU B N   1 
ATOM   4357  C CA  . GLU B  2 123 ? -7.201  29.689  156.167 1.00 199.26 ?  634 GLU B CA  1 
ATOM   4358  C C   . GLU B  2 123 ? -8.092  28.521  155.776 1.00 196.90 ?  634 GLU B C   1 
ATOM   4359  O O   . GLU B  2 123 ? -9.320  28.625  155.858 1.00 204.23 ?  634 GLU B O   1 
ATOM   4360  C CB  . GLU B  2 123 ? -6.668  30.370  154.908 1.00 203.63 ?  634 GLU B CB  1 
ATOM   4361  C CG  . GLU B  2 123 ? -5.948  31.667  155.152 1.00 198.02 ?  634 GLU B CG  1 
ATOM   4362  C CD  . GLU B  2 123 ? -5.553  32.336  153.859 1.00 201.16 ?  634 GLU B CD  1 
ATOM   4363  O OE1 . GLU B  2 123 ? -5.807  31.753  152.781 1.00 204.78 ?  634 GLU B OE1 1 
ATOM   4364  O OE2 . GLU B  2 123 ? -4.957  33.429  153.924 1.00 200.62 -1 634 GLU B OE2 1 
ATOM   4365  N N   . ILE B  2 124 ? -7.492  27.399  155.363 1.00 197.95 ?  635 ILE B N   1 
ATOM   4366  C CA  . ILE B  2 124 ? -8.276  26.258  154.896 1.00 200.55 ?  635 ILE B CA  1 
ATOM   4367  C C   . ILE B  2 124 ? -8.768  25.408  156.053 1.00 200.91 ?  635 ILE B C   1 
ATOM   4368  O O   . ILE B  2 124 ? -9.496  24.432  155.830 1.00 205.11 ?  635 ILE B O   1 
ATOM   4369  C CB  . ILE B  2 124 ? -7.441  25.400  153.924 1.00 193.12 ?  635 ILE B CB  1 
ATOM   4370  C CG1 . ILE B  2 124 ? -6.529  26.296  153.088 1.00 183.46 ?  635 ILE B CG1 1 
ATOM   4371  C CG2 . ILE B  2 124 ? -8.334  24.575  153.001 1.00 196.15 ?  635 ILE B CG2 1 
ATOM   4372  C CD1 . ILE B  2 124 ? -7.264  27.204  152.133 1.00 190.53 ?  635 ILE B CD1 1 
ATOM   4373  N N   . SER B  2 125 ? -8.397  25.761  157.288 1.00 206.98 ?  636 SER B N   1 
ATOM   4374  C CA  . SER B  2 125 ? -8.832  25.006  158.459 1.00 213.92 ?  636 SER B CA  1 
ATOM   4375  C C   . SER B  2 125 ? -10.348 24.915  158.529 1.00 227.88 ?  636 SER B C   1 
ATOM   4376  O O   . SER B  2 125 ? -10.893 23.939  159.058 1.00 232.28 ?  636 SER B O   1 
ATOM   4377  C CB  . SER B  2 125 ? -8.281  25.647  159.734 1.00 212.65 ?  636 SER B CB  1 
ATOM   4378  O OG  . SER B  2 125 ? -8.755  26.975  159.886 1.00 220.38 ?  636 SER B OG  1 
ATOM   4379  N N   . ASN B  2 126 ? -11.039 25.932  158.008 1.00 219.24 ?  637 ASN B N   1 
ATOM   4380  C CA  . ASN B  2 126 ? -12.495 25.949  158.005 1.00 228.05 ?  637 ASN B CA  1 
ATOM   4381  C C   . ASN B  2 126 ? -13.096 24.925  157.053 1.00 225.79 ?  637 ASN B C   1 
ATOM   4382  O O   . ASN B  2 126 ? -14.195 24.420  157.309 1.00 228.91 ?  637 ASN B O   1 
ATOM   4383  C CB  . ASN B  2 126 ? -12.959 27.335  157.583 1.00 237.13 ?  637 ASN B CB  1 
ATOM   4384  C CG  . ASN B  2 126 ? -12.913 28.323  158.701 1.00 240.34 ?  637 ASN B CG  1 
ATOM   4385  O OD1 . ASN B  2 126 ? -12.296 28.091  159.741 1.00 240.23 ?  637 ASN B OD1 1 
ATOM   4386  N ND2 . ASN B  2 126 ? -13.542 29.455  158.486 1.00 257.56 ?  637 ASN B ND2 1 
ATOM   4387  N N   . TYR B  2 127 ? -12.400 24.595  155.967 1.00 218.62 ?  638 TYR B N   1 
ATOM   4388  C CA  . TYR B  2 127 ? -12.941 23.697  154.955 1.00 219.31 ?  638 TYR B CA  1 
ATOM   4389  C C   . TYR B  2 127 ? -12.186 22.379  154.878 1.00 212.93 ?  638 TYR B C   1 
ATOM   4390  O O   . TYR B  2 127 ? -12.448 21.575  153.980 1.00 213.13 ?  638 TYR B O   1 
ATOM   4391  C CB  . TYR B  2 127 ? -12.968 24.385  153.586 1.00 218.16 ?  638 TYR B CB  1 
ATOM   4392  C CG  . TYR B  2 127 ? -13.498 25.810  153.609 1.00 224.09 ?  638 TYR B CG  1 
ATOM   4393  C CD1 . TYR B  2 127 ? -14.867 26.058  153.654 1.00 234.35 ?  638 TYR B CD1 1 
ATOM   4394  C CD2 . TYR B  2 127 ? -12.639 26.902  153.586 1.00 224.01 ?  638 TYR B CD2 1 
ATOM   4395  C CE1 . TYR B  2 127 ? -15.365 27.353  153.675 1.00 245.84 ?  638 TYR B CE1 1 
ATOM   4396  C CE2 . TYR B  2 127 ? -13.129 28.205  153.607 1.00 234.81 ?  638 TYR B CE2 1 
ATOM   4397  C CZ  . TYR B  2 127 ? -14.495 28.421  153.652 1.00 245.30 ?  638 TYR B CZ  1 
ATOM   4398  O OH  . TYR B  2 127 ? -15.008 29.701  153.674 1.00 256.75 ?  638 TYR B OH  1 
ATOM   4399  N N   . THR B  2 128 ? -11.253 22.147  155.797 1.00 221.44 ?  639 THR B N   1 
ATOM   4400  C CA  . THR B  2 128 ? -10.485 20.908  155.796 1.00 215.58 ?  639 THR B CA  1 
ATOM   4401  C C   . THR B  2 128 ? -11.393 19.695  155.964 1.00 220.39 ?  639 THR B C   1 
ATOM   4402  O O   . THR B  2 128 ? -11.259 18.695  155.249 1.00 218.39 ?  639 THR B O   1 
ATOM   4403  C CB  . THR B  2 128 ? -9.439  20.940  156.907 1.00 211.10 ?  639 THR B CB  1 
ATOM   4404  O OG1 . THR B  2 128 ? -10.003 21.565  158.067 1.00 217.09 ?  639 THR B OG1 1 
ATOM   4405  C CG2 . THR B  2 128 ? -8.185  21.697  156.472 1.00 203.92 ?  639 THR B CG2 1 
ATOM   4406  N N   . GLN B  2 129 ? -12.336 19.774  156.904 1.00 195.21 ?  640 GLN B N   1 
ATOM   4407  C CA  . GLN B  2 129 ? -13.232 18.656  157.172 1.00 197.43 ?  640 GLN B CA  1 
ATOM   4408  C C   . GLN B  2 129 ? -14.180 18.384  156.008 1.00 197.23 ?  640 GLN B C   1 
ATOM   4409  O O   . GLN B  2 129 ? -14.583 17.235  155.790 1.00 198.50 ?  640 GLN B O   1 
ATOM   4410  C CB  . GLN B  2 129 ? -14.019 18.958  158.443 1.00 199.49 ?  640 GLN B CB  1 
ATOM   4411  C CG  . GLN B  2 129 ? -14.837 17.810  158.956 1.00 202.10 ?  640 GLN B CG  1 
ATOM   4412  C CD  . GLN B  2 129 ? -13.936 16.690  159.457 1.00 202.96 ?  640 GLN B CD  1 
ATOM   4413  O OE1 . GLN B  2 129 ? -12.755 16.912  159.745 1.00 201.93 ?  640 GLN B OE1 1 
ATOM   4414  N NE2 . GLN B  2 129 ? -14.482 15.488  159.562 1.00 204.94 ?  640 GLN B NE2 1 
ATOM   4415  N N   . ILE B  2 130 ? -14.546 19.418  155.251 1.00 202.97 ?  641 ILE B N   1 
ATOM   4416  C CA  . ILE B  2 130 ? -15.436 19.240  154.107 1.00 202.77 ?  641 ILE B CA  1 
ATOM   4417  C C   . ILE B  2 130 ? -14.714 18.511  152.987 1.00 201.42 ?  641 ILE B C   1 
ATOM   4418  O O   . ILE B  2 130 ? -15.260 17.592  152.367 1.00 202.16 ?  641 ILE B O   1 
ATOM   4419  C CB  . ILE B  2 130 ? -15.982 20.595  153.632 1.00 202.47 ?  641 ILE B CB  1 
ATOM   4420  C CG1 . ILE B  2 130 ? -16.612 21.354  154.798 1.00 209.57 ?  641 ILE B CG1 1 
ATOM   4421  C CG2 . ILE B  2 130 ? -16.981 20.392  152.513 1.00 208.20 ?  641 ILE B CG2 1 
ATOM   4422  C CD1 . ILE B  2 130 ? -16.700 22.848  154.571 1.00 209.21 ?  641 ILE B CD1 1 
ATOM   4423  N N   . ILE B  2 131 ? -13.476 18.919  152.712 1.00 214.97 ?  642 ILE B N   1 
ATOM   4424  C CA  . ILE B  2 131 ? -12.695 18.316  151.641 1.00 208.48 ?  642 ILE B CA  1 
ATOM   4425  C C   . ILE B  2 131 ? -12.458 16.843  151.928 1.00 206.70 ?  642 ILE B C   1 
ATOM   4426  O O   . ILE B  2 131 ? -12.514 16.000  151.024 1.00 206.42 ?  642 ILE B O   1 
ATOM   4427  C CB  . ILE B  2 131 ? -11.361 19.074  151.504 1.00 200.14 ?  642 ILE B CB  1 
ATOM   4428  C CG1 . ILE B  2 131 ? -11.600 20.545  151.149 1.00 201.87 ?  642 ILE B CG1 1 
ATOM   4429  C CG2 . ILE B  2 131 ? -10.457 18.398  150.498 1.00 193.70 ?  642 ILE B CG2 1 
ATOM   4430  C CD1 . ILE B  2 131 ? -10.319 21.339  151.001 1.00 194.45 ?  642 ILE B CD1 1 
ATOM   4431  N N   . TYR B  2 132 ? -12.200 16.509  153.191 1.00 213.37 ?  643 TYR B N   1 
ATOM   4432  C CA  . TYR B  2 132 ? -11.951 15.121  153.553 1.00 212.16 ?  643 TYR B CA  1 
ATOM   4433  C C   . TYR B  2 132 ? -13.133 14.234  153.172 1.00 219.40 ?  643 TYR B C   1 
ATOM   4434  O O   . TYR B  2 132 ? -12.946 13.098  152.723 1.00 218.38 ?  643 TYR B O   1 
ATOM   4435  C CB  . TYR B  2 132 ? -11.684 15.036  155.055 1.00 212.24 ?  643 TYR B CB  1 
ATOM   4436  C CG  . TYR B  2 132 ? -10.367 15.650  155.494 1.00 204.91 ?  643 TYR B CG  1 
ATOM   4437  C CD1 . TYR B  2 132 ? -9.404  16.040  154.566 1.00 198.11 ?  643 TYR B CD1 1 
ATOM   4438  C CD2 . TYR B  2 132 ? -10.113 15.891  156.838 1.00 205.64 ?  643 TYR B CD2 1 
ATOM   4439  C CE1 . TYR B  2 132 ? -8.209  16.624  154.973 1.00 194.01 ?  643 TYR B CE1 1 
ATOM   4440  C CE2 . TYR B  2 132 ? -8.923  16.473  157.254 1.00 199.61 ?  643 TYR B CE2 1 
ATOM   4441  C CZ  . TYR B  2 132 ? -7.974  16.838  156.317 1.00 195.26 ?  643 TYR B CZ  1 
ATOM   4442  O OH  . TYR B  2 132 ? -6.789  17.418  156.719 1.00 194.30 ?  643 TYR B OH  1 
ATOM   4443  N N   . GLY B  2 133 ? -14.359 14.755  153.305 1.00 210.09 ?  644 GLY B N   1 
ATOM   4444  C CA  . GLY B  2 133 ? -15.539 13.974  152.970 1.00 218.05 ?  644 GLY B CA  1 
ATOM   4445  C C   . GLY B  2 133 ? -15.713 13.716  151.487 1.00 218.00 ?  644 GLY B C   1 
ATOM   4446  O O   . GLY B  2 133 ? -16.262 12.684  151.093 1.00 221.91 ?  644 GLY B O   1 
ATOM   4447  N N   . LEU B  2 134 ? -15.260 14.644  150.649 1.00 206.58 ?  645 LEU B N   1 
ATOM   4448  C CA  . LEU B  2 134 ? -15.376 14.509  149.202 1.00 206.44 ?  645 LEU B CA  1 
ATOM   4449  C C   . LEU B  2 134 ? -14.317 13.580  148.622 1.00 199.18 ?  645 LEU B C   1 
ATOM   4450  O O   . LEU B  2 134 ? -14.393 13.241  147.436 1.00 199.15 ?  645 LEU B O   1 
ATOM   4451  C CB  . LEU B  2 134 ? -15.345 15.880  148.523 1.00 205.94 ?  645 LEU B CB  1 
ATOM   4452  C CG  . LEU B  2 134 ? -16.721 16.550  148.405 1.00 215.59 ?  645 LEU B CG  1 
ATOM   4453  C CD1 . LEU B  2 134 ? -17.682 15.644  147.632 1.00 222.02 ?  645 LEU B CD1 1 
ATOM   4454  C CD2 . LEU B  2 134 ? -17.308 16.933  149.763 1.00 220.90 ?  645 LEU B CD2 1 
ATOM   4455  N N   . LEU B  2 135 ? -13.351 13.163  149.435 1.00 182.81 ?  646 LEU B N   1 
ATOM   4456  C CA  . LEU B  2 135 ? -12.237 12.319  149.040 1.00 182.03 ?  646 LEU B CA  1 
ATOM   4457  C C   . LEU B  2 135 ? -12.502 10.853  149.348 1.00 184.14 ?  646 LEU B C   1 
ATOM   4458  O O   . LEU B  2 135 ? -12.220 9.991   148.511 1.00 183.80 ?  646 LEU B O   1 
ATOM   4459  C CB  . LEU B  2 135 ? -10.955 12.764  149.755 1.00 181.08 ?  646 LEU B CB  1 
ATOM   4460  C CG  . LEU B  2 135 ? -10.469 14.201  149.580 1.00 179.04 ?  646 LEU B CG  1 
ATOM   4461  C CD1 . LEU B  2 135 ? -9.195  14.427  150.384 1.00 178.53 ?  646 LEU B CD1 1 
ATOM   4462  C CD2 . LEU B  2 135 ? -10.268 14.536  148.110 1.00 176.98 ?  646 LEU B CD2 1 
ATOM   4463  N N   . GLU B  2 136 ? -13.059 10.541  150.523 1.00 217.54 ?  647 GLU B N   1 
ATOM   4464  C CA  . GLU B  2 136 ? -13.275 9.144   150.904 1.00 220.62 ?  647 GLU B CA  1 
ATOM   4465  C C   . GLU B  2 136 ? -14.533 8.553   150.282 1.00 229.89 ?  647 GLU B C   1 
ATOM   4466  O O   . GLU B  2 136 ? -14.545 7.380   149.892 1.00 232.93 ?  647 GLU B O   1 
ATOM   4467  C CB  . GLU B  2 136 ? -13.476 9.006   152.412 1.00 223.51 ?  647 GLU B CB  1 
ATOM   4468  C CG  . GLU B  2 136 ? -12.851 10.030  153.312 1.00 220.02 ?  647 GLU B CG  1 
ATOM   4469  C CD  . GLU B  2 136 ? -13.253 9.803   154.754 1.00 224.54 ?  647 GLU B CD  1 
ATOM   4470  O OE1 . GLU B  2 136 ? -14.429 9.467   154.985 1.00 232.95 ?  647 GLU B OE1 1 
ATOM   4471  O OE2 . GLU B  2 136 ? -12.410 9.976   155.659 1.00 220.22 -1 647 GLU B OE2 1 
ATOM   4472  N N   . GLU B  2 137 ? -15.593 9.352   150.175 1.00 224.52 ?  648 GLU B N   1 
ATOM   4473  C CA  . GLU B  2 137 ? -16.888 8.864   149.711 1.00 234.52 ?  648 GLU B CA  1 
ATOM   4474  C C   . GLU B  2 137 ? -17.055 8.982   148.200 1.00 235.35 ?  648 GLU B C   1 
ATOM   4475  O O   . GLU B  2 137 ? -17.309 7.982   147.524 1.00 238.43 ?  648 GLU B O   1 
ATOM   4476  C CB  . GLU B  2 137 ? -17.989 9.617   150.468 1.00 242.75 ?  648 GLU B CB  1 
ATOM   4477  C CG  . GLU B  2 137 ? -19.387 9.497   149.911 1.00 253.94 ?  648 GLU B CG  1 
ATOM   4478  C CD  . GLU B  2 137 ? -20.246 10.684  150.306 1.00 260.38 ?  648 GLU B CD  1 
ATOM   4479  O OE1 . GLU B  2 137 ? -21.046 11.144  149.465 1.00 265.76 ?  648 GLU B OE1 1 
ATOM   4480  O OE2 . GLU B  2 137 ? -20.119 11.156  151.458 1.00 260.43 -1 648 GLU B OE2 1 
ATOM   4481  N N   . SER B  2 138 ? -16.917 10.187  147.657 1.00 221.96 ?  649 SER B N   1 
ATOM   4482  C CA  . SER B  2 138 ? -17.197 10.356  146.239 1.00 223.88 ?  649 SER B CA  1 
ATOM   4483  C C   . SER B  2 138 ? -16.190 9.620   145.364 1.00 217.06 ?  649 SER B C   1 
ATOM   4484  O O   . SER B  2 138 ? -16.514 9.281   144.220 1.00 219.83 ?  649 SER B O   1 
ATOM   4485  C CB  . SER B  2 138 ? -17.235 11.841  145.881 1.00 223.10 ?  649 SER B CB  1 
ATOM   4486  O OG  . SER B  2 138 ? -15.930 12.384  145.828 1.00 213.00 ?  649 SER B OG  1 
ATOM   4487  N N   . GLN B  2 139 ? -14.982 9.365   145.866 1.00 205.99 ?  650 GLN B N   1 
ATOM   4488  C CA  . GLN B  2 139 ? -13.931 8.784   145.038 1.00 199.70 ?  650 GLN B CA  1 
ATOM   4489  C C   . GLN B  2 139 ? -13.795 7.268   145.144 1.00 200.95 ?  650 GLN B C   1 
ATOM   4490  O O   . GLN B  2 139 ? -14.469 6.535   144.414 1.00 206.47 ?  650 GLN B O   1 
ATOM   4491  C CB  . GLN B  2 139 ? -12.591 9.443   145.367 1.00 196.82 ?  650 GLN B CB  1 
ATOM   4492  C CG  . GLN B  2 139 ? -12.470 10.938  145.033 1.00 194.86 ?  650 GLN B CG  1 
ATOM   4493  C CD  . GLN B  2 139 ? -12.671 11.286  143.552 1.00 193.30 ?  650 GLN B CD  1 
ATOM   4494  O OE1 . GLN B  2 139 ? -13.493 10.702  142.843 1.00 194.68 ?  650 GLN B OE1 1 
ATOM   4495  N NE2 . GLN B  2 139 ? -11.882 12.239  143.079 1.00 191.13 ?  650 GLN B NE2 1 
ATOM   4496  N N   . ASN B  2 140 ? -12.934 6.787   146.050 1.00 189.16 ?  651 ASN B N   1 
ATOM   4497  C CA  . ASN B  2 140 ? -12.603 5.363   146.087 1.00 189.15 ?  651 ASN B CA  1 
ATOM   4498  C C   . ASN B  2 140 ? -13.786 4.444   146.360 1.00 193.73 ?  651 ASN B C   1 
ATOM   4499  O O   . ASN B  2 140 ? -13.618 3.224   146.266 1.00 194.47 ?  651 ASN B O   1 
ATOM   4500  C CB  . ASN B  2 140 ? -11.525 5.093   147.135 1.00 189.45 ?  651 ASN B CB  1 
ATOM   4501  C CG  . ASN B  2 140 ? -10.179 5.634   146.729 1.00 189.68 ?  651 ASN B CG  1 
ATOM   4502  O OD1 . ASN B  2 140 ? -10.092 6.596   145.969 1.00 189.67 ?  651 ASN B OD1 1 
ATOM   4503  N ND2 . ASN B  2 140 ? -9.115  4.999   147.212 1.00 189.99 ?  651 ASN B ND2 1 
ATOM   4504  N N   . GLN B  2 141 ? -14.964 4.972   146.676 1.00 188.40 ?  652 GLN B N   1 
ATOM   4505  C CA  . GLN B  2 141 ? -16.133 4.110   146.792 1.00 188.42 ?  652 GLN B CA  1 
ATOM   4506  C C   . GLN B  2 141 ? -16.855 4.018   145.462 1.00 189.94 ?  652 GLN B C   1 
ATOM   4507  O O   . GLN B  2 141 ? -17.475 2.991   145.157 1.00 194.48 ?  652 GLN B O   1 
ATOM   4508  C CB  . GLN B  2 141 ? -17.081 4.581   147.899 1.00 188.69 ?  652 GLN B CB  1 
ATOM   4509  C CG  . GLN B  2 141 ? -18.285 3.652   148.068 1.00 189.33 ?  652 GLN B CG  1 
ATOM   4510  C CD  . GLN B  2 141 ? -17.873 2.228   148.392 1.00 196.96 ?  652 GLN B CD  1 
ATOM   4511  O OE1 . GLN B  2 141 ? -16.901 1.999   149.110 1.00 200.16 ?  652 GLN B OE1 1 
ATOM   4512  N NE2 . GLN B  2 141 ? -18.593 1.262   147.832 1.00 200.16 ?  652 GLN B NE2 1 
ATOM   4513  N N   . GLN B  2 142 ? -16.735 5.066   144.654 1.00 201.47 ?  653 GLN B N   1 
ATOM   4514  C CA  . GLN B  2 142 ? -17.335 5.129   143.337 1.00 206.89 ?  653 GLN B CA  1 
ATOM   4515  C C   . GLN B  2 142 ? -16.321 4.788   142.266 1.00 202.55 ?  653 GLN B C   1 
ATOM   4516  O O   . GLN B  2 142 ? -16.693 4.221   141.242 1.00 206.53 ?  653 GLN B O   1 
ATOM   4517  C CB  . GLN B  2 142 ? -17.900 6.534   143.091 1.00 209.66 ?  653 GLN B CB  1 
ATOM   4518  C CG  . GLN B  2 142 ? -18.677 6.716   141.802 1.00 216.72 ?  653 GLN B CG  1 
ATOM   4519  C CD  . GLN B  2 142 ? -19.207 8.130   141.648 1.00 220.00 ?  653 GLN B CD  1 
ATOM   4520  O OE1 . GLN B  2 142 ? -19.931 8.628   142.511 1.00 223.44 ?  653 GLN B OE1 1 
ATOM   4521  N NE2 . GLN B  2 142 ? -18.849 8.786   140.549 1.00 218.83 ?  653 GLN B NE2 1 
ATOM   4522  N N   . GLU B  2 143 ? -15.038 5.026   142.541 1.00 200.38 ?  654 GLU B N   1 
ATOM   4523  C CA  . GLU B  2 143 ? -13.974 4.746   141.584 1.00 197.20 ?  654 GLU B CA  1 
ATOM   4524  C C   . GLU B  2 143 ? -13.648 3.256   141.579 1.00 197.38 ?  654 GLU B C   1 
ATOM   4525  O O   . GLU B  2 143 ? -13.543 2.639   140.514 1.00 200.00 ?  654 GLU B O   1 
ATOM   4526  C CB  . GLU B  2 143 ? -12.744 5.589   141.924 1.00 190.44 ?  654 GLU B CB  1 
ATOM   4527  C CG  . GLU B  2 143 ? -11.520 5.319   141.083 1.00 189.35 ?  654 GLU B CG  1 
ATOM   4528  C CD  . GLU B  2 143 ? -10.348 6.170   141.518 1.00 189.58 ?  654 GLU B CD  1 
ATOM   4529  O OE1 . GLU B  2 143 ? -9.210  5.874   141.103 1.00 189.72 ?  654 GLU B OE1 1 
ATOM   4530  O OE2 . GLU B  2 143 ? -10.589 7.240   142.114 1.00 189.70 -1 654 GLU B OE2 1 
ATOM   4531  N N   . LYS B  2 144 ? -13.488 2.660   142.766 1.00 198.46 ?  655 LYS B N   1 
ATOM   4532  C CA  . LYS B  2 144 ? -13.177 1.235   142.840 1.00 198.94 ?  655 LYS B CA  1 
ATOM   4533  C C   . LYS B  2 144 ? -14.374 0.405   142.397 1.00 206.39 ?  655 LYS B C   1 
ATOM   4534  O O   . LYS B  2 144 ? -14.208 -0.650  141.773 1.00 208.49 ?  655 LYS B O   1 
ATOM   4535  C CB  . LYS B  2 144 ? -12.719 0.831   144.241 1.00 195.69 ?  655 LYS B CB  1 
ATOM   4536  C CG  . LYS B  2 144 ? -11.348 1.357   144.640 1.00 193.20 ?  655 LYS B CG  1 
ATOM   4537  C CD  . LYS B  2 144 ? -10.944 0.795   145.995 1.00 193.51 ?  655 LYS B CD  1 
ATOM   4538  C CE  . LYS B  2 144 ? -9.553  1.244   146.407 1.00 193.76 ?  655 LYS B CE  1 
ATOM   4539  N NZ  . LYS B  2 144 ? -9.152  0.661   147.719 1.00 194.23 1  655 LYS B NZ  1 
ATOM   4540  N N   . ASN B  2 145 ? -15.590 0.856   142.723 1.00 209.48 ?  656 ASN B N   1 
ATOM   4541  C CA  . ASN B  2 145 ? -16.771 0.141   142.254 1.00 217.32 ?  656 ASN B CA  1 
ATOM   4542  C C   . ASN B  2 145 ? -16.847 0.220   140.736 1.00 220.29 ?  656 ASN B C   1 
ATOM   4543  O O   . ASN B  2 145 ? -17.321 -0.720  140.087 1.00 225.29 ?  656 ASN B O   1 
ATOM   4544  C CB  . ASN B  2 145 ? -18.033 0.706   142.905 1.00 222.08 ?  656 ASN B CB  1 
ATOM   4545  C CG  . ASN B  2 145 ? -19.199 -0.268  142.862 1.00 230.27 ?  656 ASN B CG  1 
ATOM   4546  O OD1 . ASN B  2 145 ? -19.300 -1.101  141.961 1.00 233.74 ?  656 ASN B OD1 1 
ATOM   4547  N ND2 . ASN B  2 145 ? -20.087 -0.165  143.845 1.00 233.89 ?  656 ASN B ND2 1 
ATOM   4548  N N   . GLU B  2 146 ? -16.376 1.328   140.153 1.00 230.60 ?  657 GLU B N   1 
ATOM   4549  C CA  . GLU B  2 146 ? -16.331 1.408   138.699 1.00 232.95 ?  657 GLU B CA  1 
ATOM   4550  C C   . GLU B  2 146 ? -15.333 0.390   138.180 1.00 230.60 ?  657 GLU B C   1 
ATOM   4551  O O   . GLU B  2 146 ? -15.540 -0.199  137.115 1.00 236.66 ?  657 GLU B O   1 
ATOM   4552  C CB  . GLU B  2 146 ? -15.945 2.804   138.200 1.00 229.86 ?  657 GLU B CB  1 
ATOM   4553  C CG  . GLU B  2 146 ? -16.929 3.922   138.476 1.00 232.64 ?  657 GLU B CG  1 
ATOM   4554  C CD  . GLU B  2 146 ? -18.259 3.764   137.781 1.00 246.36 ?  657 GLU B CD  1 
ATOM   4555  O OE1 . GLU B  2 146 ? -18.348 2.993   136.803 1.00 255.95 ?  657 GLU B OE1 1 
ATOM   4556  O OE2 . GLU B  2 146 ? -19.220 4.431   138.218 1.00 248.65 -1 657 GLU B OE2 1 
ATOM   4557  N N   . GLN B  2 147 ? -14.252 0.164   138.933 1.00 231.28 ?  658 GLN B N   1 
ATOM   4558  C CA  . GLN B  2 147 ? -13.232 -0.772  138.488 1.00 229.13 ?  658 GLN B CA  1 
ATOM   4559  C C   . GLN B  2 147 ? -13.752 -2.203  138.551 1.00 234.40 ?  658 GLN B C   1 
ATOM   4560  O O   . GLN B  2 147 ? -13.348 -3.039  137.736 1.00 236.15 ?  658 GLN B O   1 
ATOM   4561  C CB  . GLN B  2 147 ? -11.985 -0.592  139.362 1.00 221.81 ?  658 GLN B CB  1 
ATOM   4562  C CG  . GLN B  2 147 ? -10.735 -1.335  138.930 1.00 220.43 ?  658 GLN B CG  1 
ATOM   4563  C CD  . GLN B  2 147 ? -9.546  -1.011  139.824 1.00 215.45 ?  658 GLN B CD  1 
ATOM   4564  O OE1 . GLN B  2 147 ? -9.664  -0.242  140.780 1.00 209.67 ?  658 GLN B OE1 1 
ATOM   4565  N NE2 . GLN B  2 147 ? -8.391  -1.587  139.508 1.00 217.49 ?  658 GLN B NE2 1 
ATOM   4566  N N   . ASP B  2 148 ? -14.639 -2.509  139.507 1.00 217.94 ?  659 ASP B N   1 
ATOM   4567  C CA  . ASP B  2 148 ? -15.213 -3.850  139.550 1.00 218.31 ?  659 ASP B CA  1 
ATOM   4568  C C   . ASP B  2 148 ? -16.096 -4.122  138.343 1.00 223.98 ?  659 ASP B C   1 
ATOM   4569  O O   . ASP B  2 148 ? -16.236 -5.275  137.921 1.00 228.24 ?  659 ASP B O   1 
ATOM   4570  C CB  . ASP B  2 148 ? -16.043 -4.052  140.813 1.00 219.00 ?  659 ASP B CB  1 
ATOM   4571  C CG  . ASP B  2 148 ? -16.627 -5.450  140.896 1.00 225.74 ?  659 ASP B CG  1 
ATOM   4572  O OD1 . ASP B  2 148 ? -15.937 -6.364  141.391 1.00 225.00 ?  659 ASP B OD1 1 
ATOM   4573  O OD2 . ASP B  2 148 ? -17.773 -5.638  140.429 1.00 232.57 -1 659 ASP B OD2 1 
ATOM   4574  N N   . LEU B  2 149 ? -16.694 -3.076  137.777 1.00 221.50 ?  660 LEU B N   1 
ATOM   4575  C CA  . LEU B  2 149 ? -17.512 -3.251  136.586 1.00 228.79 ?  660 LEU B CA  1 
ATOM   4576  C C   . LEU B  2 149 ? -16.661 -3.301  135.326 1.00 229.20 ?  660 LEU B C   1 
ATOM   4577  O O   . LEU B  2 149 ? -17.070 -3.908  134.330 1.00 237.39 ?  660 LEU B O   1 
ATOM   4578  C CB  . LEU B  2 149 ? -18.564 -2.140  136.506 1.00 231.99 ?  660 LEU B CB  1 
ATOM   4579  C CG  . LEU B  2 149 ? -19.886 -2.386  137.253 1.00 237.89 ?  660 LEU B CG  1 
ATOM   4580  C CD1 . LEU B  2 149 ? -19.664 -2.664  138.737 1.00 233.86 ?  660 LEU B CD1 1 
ATOM   4581  C CD2 . LEU B  2 149 ? -20.845 -1.217  137.076 1.00 241.82 ?  660 LEU B CD2 1 
ATOM   4582  N N   . LEU B  2 150 ? -15.487 -2.666  135.354 1.00 249.04 ?  661 LEU B N   1 
ATOM   4583  C CA  . LEU B  2 150 ? -14.597 -2.600  134.203 1.00 249.72 ?  661 LEU B CA  1 
ATOM   4584  C C   . LEU B  2 150 ? -13.617 -3.767  134.133 1.00 247.75 ?  661 LEU B C   1 
ATOM   4585  O O   . LEU B  2 150 ? -13.034 -4.006  133.070 1.00 247.68 ?  661 LEU B O   1 
ATOM   4586  C CB  . LEU B  2 150 ? -13.818 -1.285  134.193 1.00 243.87 ?  661 LEU B CB  1 
ATOM   4587  C CG  . LEU B  2 150 ? -14.750 -0.067  134.146 1.00 238.96 ?  661 LEU B CG  1 
ATOM   4588  C CD1 . LEU B  2 150 ? -14.007 1.264   134.347 1.00 232.96 ?  661 LEU B CD1 1 
ATOM   4589  C CD2 . LEU B  2 150 ? -15.761 -0.049  133.035 1.00 248.53 ?  661 LEU B CD2 1 
ATOM   4590  N N   . ALA B  2 151 ? -13.415 -4.490  135.237 1.00 231.57 ?  662 ALA B N   1 
ATOM   4591  C CA  . ALA B  2 151 ? -12.435 -5.566  135.307 1.00 230.29 ?  662 ALA B CA  1 
ATOM   4592  C C   . ALA B  2 151 ? -13.051 -6.931  135.044 1.00 237.51 ?  662 ALA B C   1 
ATOM   4593  O O   . ALA B  2 151 ? -12.311 -7.906  134.869 1.00 238.41 ?  662 ALA B O   1 
ATOM   4594  C CB  . ALA B  2 151 ? -11.743 -5.575  136.678 1.00 224.77 ?  662 ALA B CB  1 
ATOM   4595  N N   . LEU B  2 152 ? -14.381 -7.021  135.017 1.00 239.16 ?  663 LEU B N   1 
ATOM   4596  C CA  . LEU B  2 152 ? -15.064 -8.282  134.770 1.00 246.21 ?  663 LEU B CA  1 
ATOM   4597  C C   . LEU B  2 152 ? -15.138 -8.617  133.284 1.00 250.08 ?  663 LEU B C   1 
ATOM   4598  O O   . LEU B  2 152 ? -15.287 -9.792  132.934 1.00 252.39 ?  663 LEU B O   1 
ATOM   4599  C CB  . LEU B  2 152 ? -16.474 -8.240  135.373 1.00 241.67 ?  663 LEU B CB  1 
ATOM   4600  C CG  . LEU B  2 152 ? -17.476 -7.237  134.785 1.00 243.79 ?  663 LEU B CG  1 
ATOM   4601  C CD1 . LEU B  2 152 ? -18.285 -7.814  133.622 1.00 246.02 ?  663 LEU B CD1 1 
ATOM   4602  C CD2 . LEU B  2 152 ? -18.401 -6.705  135.871 1.00 240.23 ?  663 LEU B CD2 1 
ATOM   4603  N N   . ASP B  2 153 ? -15.037 -7.620  132.408 1.00 261.27 ?  664 ASP B N   1 
ATOM   4604  C CA  . ASP B  2 153 ? -15.091 -7.857  130.967 1.00 257.92 ?  664 ASP B CA  1 
ATOM   4605  C C   . ASP B  2 153 ? -13.695 -8.046  130.374 1.00 253.99 ?  664 ASP B C   1 
ATOM   4606  O O   . ASP B  2 153 ? -13.470 -7.790  129.190 1.00 251.09 ?  664 ASP B O   1 
ATOM   4607  C CB  . ASP B  2 153 ? -15.819 -6.705  130.258 1.00 257.49 ?  664 ASP B CB  1 
ATOM   4608  C CG  . ASP B  2 153 ? -15.192 -5.344  130.532 1.00 256.07 ?  664 ASP B CG  1 
ATOM   4609  O OD1 . ASP B  2 153 ? -13.994 -5.275  130.877 1.00 254.55 ?  664 ASP B OD1 1 
ATOM   4610  O OD2 . ASP B  2 153 ? -15.910 -4.331  130.398 1.00 256.92 -1 664 ASP B OD2 1 
ATOM   4611  N N   . ALA C  1 1   ? 110.618 88.513  317.303 1.00 221.70 ?  31  ALA C N   1 
ATOM   4612  C CA  . ALA C  1 1   ? 109.318 88.762  317.913 1.00 227.26 ?  31  ALA C CA  1 
ATOM   4613  C C   . ALA C  1 1   ? 108.415 89.558  316.978 1.00 229.05 ?  31  ALA C C   1 
ATOM   4614  O O   . ALA C  1 1   ? 107.998 89.064  315.931 1.00 229.28 ?  31  ALA C O   1 
ATOM   4615  C CB  . ALA C  1 1   ? 109.483 89.491  319.238 1.00 217.86 ?  31  ALA C CB  1 
ATOM   4616  N N   . GLU C  1 2   ? 108.108 90.797  317.369 1.00 241.82 ?  32  GLU C N   1 
ATOM   4617  C CA  . GLU C  1 2   ? 107.242 91.636  316.546 1.00 240.61 ?  32  GLU C CA  1 
ATOM   4618  C C   . GLU C  1 2   ? 107.946 92.168  315.304 1.00 236.25 ?  32  GLU C C   1 
ATOM   4619  O O   . GLU C  1 2   ? 107.290 92.411  314.285 1.00 235.84 ?  32  GLU C O   1 
ATOM   4620  C CB  . GLU C  1 2   ? 106.699 92.800  317.376 1.00 238.68 ?  32  GLU C CB  1 
ATOM   4621  C CG  . GLU C  1 2   ? 105.443 92.470  318.158 1.00 240.06 ?  32  GLU C CG  1 
ATOM   4622  C CD  . GLU C  1 2   ? 104.277 92.124  317.255 1.00 246.82 ?  32  GLU C CD  1 
ATOM   4623  O OE1 . GLU C  1 2   ? 104.247 92.617  316.107 1.00 245.48 ?  32  GLU C OE1 1 
ATOM   4624  O OE2 . GLU C  1 2   ? 103.396 91.354  317.690 1.00 251.08 -1 32  GLU C OE2 1 
ATOM   4625  N N   . ASN C  1 3   ? 109.263 92.360  315.355 1.00 226.88 ?  33  ASN C N   1 
ATOM   4626  C CA  . ASN C  1 3   ? 109.998 92.797  314.175 1.00 225.41 ?  33  ASN C CA  1 
ATOM   4627  C C   . ASN C  1 3   ? 110.313 91.609  313.270 1.00 224.89 ?  33  ASN C C   1 
ATOM   4628  O O   . ASN C  1 3   ? 110.964 90.648  313.695 1.00 224.08 ?  33  ASN C O   1 
ATOM   4629  C CB  . ASN C  1 3   ? 111.274 93.530  314.589 1.00 221.29 ?  33  ASN C CB  1 
ATOM   4630  C CG  . ASN C  1 3   ? 112.117 92.735  315.568 1.00 221.44 ?  33  ASN C CG  1 
ATOM   4631  O OD1 . ASN C  1 3   ? 111.606 91.887  316.300 1.00 224.47 ?  33  ASN C OD1 1 
ATOM   4632  N ND2 . ASN C  1 3   ? 113.416 93.014  315.594 1.00 222.78 ?  33  ASN C ND2 1 
ATOM   4633  N N   . LEU C  1 4   ? 109.843 91.677  312.028 1.00 205.05 ?  34  LEU C N   1 
ATOM   4634  C CA  . LEU C  1 4   ? 109.957 90.584  311.075 1.00 202.79 ?  34  LEU C CA  1 
ATOM   4635  C C   . LEU C  1 4   ? 111.373 90.483  310.514 1.00 198.73 ?  34  LEU C C   1 
ATOM   4636  O O   . LEU C  1 4   ? 112.169 91.423  310.572 1.00 195.21 ?  34  LEU C O   1 
ATOM   4637  C CB  . LEU C  1 4   ? 108.940 90.732  309.943 1.00 202.00 ?  34  LEU C CB  1 
ATOM   4638  C CG  . LEU C  1 4   ? 107.492 90.869  310.409 1.00 202.70 ?  34  LEU C CG  1 
ATOM   4639  C CD1 . LEU C  1 4   ? 106.557 91.030  309.221 1.00 202.41 ?  34  LEU C CD1 1 
ATOM   4640  C CD2 . LEU C  1 4   ? 107.102 89.663  311.253 1.00 204.42 ?  34  LEU C CD2 1 
ATOM   4641  N N   . TRP C  1 5   ? 111.670 89.314  309.956 1.00 199.46 ?  35  TRP C N   1 
ATOM   4642  C CA  . TRP C  1 5   ? 112.944 89.023  309.318 1.00 197.41 ?  35  TRP C CA  1 
ATOM   4643  C C   . TRP C  1 5   ? 112.675 88.311  308.006 1.00 197.69 ?  35  TRP C C   1 
ATOM   4644  O O   . TRP C  1 5   ? 111.752 87.498  307.912 1.00 197.96 ?  35  TRP C O   1 
ATOM   4645  C CB  . TRP C  1 5   ? 113.841 88.150  310.202 1.00 198.17 ?  35  TRP C CB  1 
ATOM   4646  C CG  . TRP C  1 5   ? 114.094 88.725  311.543 1.00 197.27 ?  35  TRP C CG  1 
ATOM   4647  C CD1 . TRP C  1 5   ? 113.336 88.571  312.665 1.00 199.93 ?  35  TRP C CD1 1 
ATOM   4648  C CD2 . TRP C  1 5   ? 115.204 89.544  311.913 1.00 197.72 ?  35  TRP C CD2 1 
ATOM   4649  N NE1 . TRP C  1 5   ? 113.904 89.257  313.713 1.00 202.10 ?  35  TRP C NE1 1 
ATOM   4650  C CE2 . TRP C  1 5   ? 115.053 89.861  313.275 1.00 200.56 ?  35  TRP C CE2 1 
ATOM   4651  C CE3 . TRP C  1 5   ? 116.310 90.044  311.221 1.00 199.70 ?  35  TRP C CE3 1 
ATOM   4652  C CZ2 . TRP C  1 5   ? 115.968 90.657  313.959 1.00 200.44 ?  35  TRP C CZ2 1 
ATOM   4653  C CZ3 . TRP C  1 5   ? 117.216 90.832  311.899 1.00 198.28 ?  35  TRP C CZ3 1 
ATOM   4654  C CH2 . TRP C  1 5   ? 117.041 91.132  313.254 1.00 196.66 ?  35  TRP C CH2 1 
ATOM   4655  N N   . VAL C  1 6   ? 113.486 88.616  306.995 1.00 186.73 ?  36  VAL C N   1 
ATOM   4656  C CA  . VAL C  1 6   ? 113.281 88.002  305.694 1.00 187.32 ?  36  VAL C CA  1 
ATOM   4657  C C   . VAL C  1 6   ? 113.665 86.530  305.762 1.00 192.57 ?  36  VAL C C   1 
ATOM   4658  O O   . VAL C  1 6   ? 114.542 86.121  306.537 1.00 191.59 ?  36  VAL C O   1 
ATOM   4659  C CB  . VAL C  1 6   ? 114.104 88.739  304.623 1.00 186.22 ?  36  VAL C CB  1 
ATOM   4660  C CG1 . VAL C  1 6   ? 113.773 90.212  304.634 1.00 186.10 ?  36  VAL C CG1 1 
ATOM   4661  C CG2 . VAL C  1 6   ? 115.587 88.535  304.864 1.00 186.58 ?  36  VAL C CG2 1 
ATOM   4662  N N   . THR C  1 7   ? 112.989 85.719  304.953 1.00 186.60 ?  37  THR C N   1 
ATOM   4663  C CA  . THR C  1 7   ? 113.287 84.298  304.852 1.00 185.75 ?  37  THR C CA  1 
ATOM   4664  C C   . THR C  1 7   ? 113.153 83.883  303.396 1.00 183.18 ?  37  THR C C   1 
ATOM   4665  O O   . THR C  1 7   ? 112.126 84.144  302.761 1.00 182.47 ?  37  THR C O   1 
ATOM   4666  C CB  . THR C  1 7   ? 112.362 83.470  305.749 1.00 183.89 ?  37  THR C CB  1 
ATOM   4667  O OG1 . THR C  1 7   ? 111.041 84.026  305.716 1.00 185.07 ?  37  THR C OG1 1 
ATOM   4668  C CG2 . THR C  1 7   ? 112.885 83.460  307.177 1.00 183.15 ?  37  THR C CG2 1 
ATOM   4669  N N   . VAL C  1 8   ? 114.202 83.250  302.880 1.00 160.16 ?  38  VAL C N   1 
ATOM   4670  C CA  . VAL C  1 8   ? 114.275 82.823  301.486 1.00 161.14 ?  38  VAL C CA  1 
ATOM   4671  C C   . VAL C  1 8   ? 113.546 81.502  301.285 1.00 162.48 ?  38  VAL C C   1 
ATOM   4672  O O   . VAL C  1 8   ? 113.790 80.524  302.003 1.00 162.98 ?  38  VAL C O   1 
ATOM   4673  C CB  . VAL C  1 8   ? 115.739 82.715  301.034 1.00 161.17 ?  38  VAL C CB  1 
ATOM   4674  C CG1 . VAL C  1 8   ? 115.818 82.331  299.562 1.00 162.13 ?  38  VAL C CG1 1 
ATOM   4675  C CG2 . VAL C  1 8   ? 116.479 84.027  301.296 1.00 160.10 ?  38  VAL C CG2 1 
ATOM   4676  N N   . TYR C  1 9   ? 112.627 81.478  300.327 1.00 163.53 ?  39  TYR C N   1 
ATOM   4677  C CA  . TYR C  1 9   ? 111.899 80.271  299.968 1.00 166.94 ?  39  TYR C CA  1 
ATOM   4678  C C   . TYR C  1 9   ? 112.327 79.854  298.565 1.00 171.36 ?  39  TYR C C   1 
ATOM   4679  O O   . TYR C  1 9   ? 112.372 80.685  297.650 1.00 169.64 ?  39  TYR C O   1 
ATOM   4680  C CB  . TYR C  1 9   ? 110.394 80.496  300.098 1.00 164.89 ?  39  TYR C CB  1 
ATOM   4681  C CG  . TYR C  1 9   ? 110.007 80.570  301.559 1.00 167.37 ?  39  TYR C CG  1 
ATOM   4682  C CD1 . TYR C  1 9   ? 110.121 81.758  302.272 1.00 167.07 ?  39  TYR C CD1 1 
ATOM   4683  C CD2 . TYR C  1 9   ? 109.592 79.437  302.242 1.00 170.69 ?  39  TYR C CD2 1 
ATOM   4684  C CE1 . TYR C  1 9   ? 109.795 81.820  303.614 1.00 165.44 ?  39  TYR C CE1 1 
ATOM   4685  C CE2 . TYR C  1 9   ? 109.264 79.489  303.581 1.00 169.51 ?  39  TYR C CE2 1 
ATOM   4686  C CZ  . TYR C  1 9   ? 109.367 80.682  304.262 1.00 164.65 ?  39  TYR C CZ  1 
ATOM   4687  O OH  . TYR C  1 9   ? 109.040 80.735  305.597 1.00 162.28 ?  39  TYR C OH  1 
ATOM   4688  N N   . TYR C  1 10  ? 112.635 78.567  298.403 1.00 140.58 ?  40  TYR C N   1 
ATOM   4689  C CA  . TYR C  1 10  ? 113.074 77.984  297.138 1.00 135.02 ?  40  TYR C CA  1 
ATOM   4690  C C   . TYR C  1 10  ? 112.103 76.898  296.698 1.00 133.97 ?  40  TYR C C   1 
ATOM   4691  O O   . TYR C  1 10  ? 111.987 75.856  297.353 1.00 136.18 ?  40  TYR C O   1 
ATOM   4692  C CB  . TYR C  1 10  ? 114.488 77.423  297.278 1.00 131.40 ?  40  TYR C CB  1 
ATOM   4693  C CG  . TYR C  1 10  ? 115.086 76.842  296.013 1.00 132.11 ?  40  TYR C CG  1 
ATOM   4694  C CD1 . TYR C  1 10  ? 115.352 77.640  294.907 1.00 136.25 ?  40  TYR C CD1 1 
ATOM   4695  C CD2 . TYR C  1 10  ? 115.415 75.493  295.940 1.00 134.41 ?  40  TYR C CD2 1 
ATOM   4696  C CE1 . TYR C  1 10  ? 115.911 77.101  293.754 1.00 136.49 ?  40  TYR C CE1 1 
ATOM   4697  C CE2 . TYR C  1 10  ? 115.974 74.949  294.799 1.00 138.35 ?  40  TYR C CE2 1 
ATOM   4698  C CZ  . TYR C  1 10  ? 116.221 75.755  293.709 1.00 137.12 ?  40  TYR C CZ  1 
ATOM   4699  O OH  . TYR C  1 10  ? 116.777 75.205  292.576 1.00 131.47 ?  40  TYR C OH  1 
ATOM   4700  N N   . GLY C  1 11  ? 111.402 77.155  295.601 1.00 132.48 ?  41  GLY C N   1 
ATOM   4701  C CA  . GLY C  1 11  ? 110.431 76.221  295.076 1.00 133.87 ?  41  GLY C CA  1 
ATOM   4702  C C   . GLY C  1 11  ? 109.039 76.796  295.177 1.00 134.67 ?  41  GLY C C   1 
ATOM   4703  O O   . GLY C  1 11  ? 108.071 76.064  295.399 1.00 136.06 ?  41  GLY C O   1 
ATOM   4704  N N   . VAL C  1 12  ? 108.924 78.109  295.011 1.00 134.82 ?  42  VAL C N   1 
ATOM   4705  C CA  . VAL C  1 12  ? 107.618 78.751  295.097 1.00 135.67 ?  42  VAL C CA  1 
ATOM   4706  C C   . VAL C  1 12  ? 106.951 78.798  293.727 1.00 136.24 ?  42  VAL C C   1 
ATOM   4707  O O   . VAL C  1 12  ? 107.624 78.993  292.703 1.00 135.47 ?  42  VAL C O   1 
ATOM   4708  C CB  . VAL C  1 12  ? 107.734 80.163  295.700 1.00 134.83 ?  42  VAL C CB  1 
ATOM   4709  C CG1 . VAL C  1 12  ? 108.203 80.091  297.151 1.00 134.41 ?  42  VAL C CG1 1 
ATOM   4710  C CG2 . VAL C  1 12  ? 108.673 81.036  294.874 1.00 133.52 ?  42  VAL C CG2 1 
ATOM   4711  N N   . PRO C  1 13  ? 105.642 78.587  293.665 1.00 136.28 ?  43  PRO C N   1 
ATOM   4712  C CA  . PRO C  1 13  ? 104.921 78.672  292.388 1.00 136.73 ?  43  PRO C CA  1 
ATOM   4713  C C   . PRO C  1 13  ? 104.859 80.101  291.865 1.00 136.46 ?  43  PRO C C   1 
ATOM   4714  O O   . PRO C  1 13  ? 103.806 80.738  291.964 1.00 137.51 ?  43  PRO C O   1 
ATOM   4715  C CB  . PRO C  1 13  ? 103.530 78.123  292.731 1.00 140.57 ?  43  PRO C CB  1 
ATOM   4716  C CG  . PRO C  1 13  ? 103.728 77.318  293.991 1.00 143.46 ?  43  PRO C CG  1 
ATOM   4717  C CD  . PRO C  1 13  ? 104.798 78.045  294.743 1.00 138.45 ?  43  PRO C CD  1 
ATOM   4718  N N   . VAL C  1 14  ? 105.952 80.631  291.321 1.00 139.18 ?  44  VAL C N   1 
ATOM   4719  C CA  . VAL C  1 14  ? 105.966 81.992  290.795 1.00 138.78 ?  44  VAL C CA  1 
ATOM   4720  C C   . VAL C  1 14  ? 106.504 81.942  289.377 1.00 138.36 ?  44  VAL C C   1 
ATOM   4721  O O   . VAL C  1 14  ? 107.643 81.515  289.154 1.00 137.42 ?  44  VAL C O   1 
ATOM   4722  C CB  . VAL C  1 14  ? 106.820 82.942  291.654 1.00 137.61 ?  44  VAL C CB  1 
ATOM   4723  C CG1 . VAL C  1 14  ? 106.983 84.288  290.965 1.00 137.24 ?  44  VAL C CG1 1 
ATOM   4724  C CG2 . VAL C  1 14  ? 106.203 83.128  293.020 1.00 138.07 ?  44  VAL C CG2 1 
ATOM   4725  N N   . TRP C  1 15  ? 105.691 82.389  288.423 1.00 131.97 ?  45  TRP C N   1 
ATOM   4726  C CA  . TRP C  1 15  ? 106.068 82.417  287.022 1.00 131.49 ?  45  TRP C CA  1 
ATOM   4727  C C   . TRP C  1 15  ? 105.701 83.762  286.413 1.00 134.64 ?  45  TRP C C   1 
ATOM   4728  O O   . TRP C  1 15  ? 104.806 84.462  286.892 1.00 135.29 ?  45  TRP C O   1 
ATOM   4729  C CB  . TRP C  1 15  ? 105.393 81.286  286.229 1.00 131.01 ?  45  TRP C CB  1 
ATOM   4730  C CG  . TRP C  1 15  ? 103.912 81.421  286.139 1.00 132.46 ?  45  TRP C CG  1 
ATOM   4731  C CD1 . TRP C  1 15  ? 103.211 82.255  285.318 1.00 135.60 ?  45  TRP C CD1 1 
ATOM   4732  C CD2 . TRP C  1 15  ? 102.943 80.703  286.904 1.00 133.56 ?  45  TRP C CD2 1 
ATOM   4733  N NE1 . TRP C  1 15  ? 101.864 82.100  285.524 1.00 139.15 ?  45  TRP C NE1 1 
ATOM   4734  C CE2 . TRP C  1 15  ? 101.673 81.152  286.494 1.00 137.04 ?  45  TRP C CE2 1 
ATOM   4735  C CE3 . TRP C  1 15  ? 103.025 79.723  287.896 1.00 133.76 ?  45  TRP C CE3 1 
ATOM   4736  C CZ2 . TRP C  1 15  ? 100.495 80.654  287.041 1.00 139.51 ?  45  TRP C CZ2 1 
ATOM   4737  C CZ3 . TRP C  1 15  ? 101.857 79.231  288.437 1.00 139.04 ?  45  TRP C CZ3 1 
ATOM   4738  C CH2 . TRP C  1 15  ? 100.608 79.696  288.009 1.00 140.04 ?  45  TRP C CH2 1 
ATOM   4739  N N   . LYS C  1 16  ? 106.404 84.111  285.338 1.00 137.86 ?  46  LYS C N   1 
ATOM   4740  C CA  . LYS C  1 16  ? 106.121 85.318  284.581 1.00 140.45 ?  46  LYS C CA  1 
ATOM   4741  C C   . LYS C  1 16  ? 106.202 84.970  283.102 1.00 143.98 ?  46  LYS C C   1 
ATOM   4742  O O   . LYS C  1 16  ? 106.969 84.090  282.700 1.00 142.22 ?  46  LYS C O   1 
ATOM   4743  C CB  . LYS C  1 16  ? 107.080 86.450  284.979 1.00 140.92 ?  46  LYS C CB  1 
ATOM   4744  C CG  . LYS C  1 16  ? 106.728 87.015  286.353 1.00 140.74 ?  46  LYS C CG  1 
ATOM   4745  C CD  . LYS C  1 16  ? 107.500 88.259  286.736 1.00 147.13 ?  46  LYS C CD  1 
ATOM   4746  C CE  . LYS C  1 16  ? 106.972 88.806  288.059 1.00 150.99 ?  46  LYS C CE  1 
ATOM   4747  N NZ  . LYS C  1 16  ? 107.786 89.937  288.580 1.00 153.29 1  46  LYS C NZ  1 
ATOM   4748  N N   . ASP C  1 17  ? 105.401 85.661  282.296 1.00 149.16 ?  47  ASP C N   1 
ATOM   4749  C CA  . ASP C  1 17  ? 105.373 85.396  280.864 1.00 152.74 ?  47  ASP C CA  1 
ATOM   4750  C C   . ASP C  1 17  ? 106.718 85.684  280.210 1.00 149.70 ?  47  ASP C C   1 
ATOM   4751  O O   . ASP C  1 17  ? 107.312 86.746  280.416 1.00 148.54 ?  47  ASP C O   1 
ATOM   4752  C CB  . ASP C  1 17  ? 104.292 86.247  280.191 1.00 154.55 ?  47  ASP C CB  1 
ATOM   4753  C CG  . ASP C  1 17  ? 102.903 85.986  280.744 1.00 157.20 ?  47  ASP C CG  1 
ATOM   4754  O OD1 . ASP C  1 17  ? 102.769 85.756  281.965 1.00 154.68 ?  47  ASP C OD1 1 
ATOM   4755  O OD2 . ASP C  1 17  ? 101.939 86.019  279.948 1.00 157.91 -1 47  ASP C OD2 1 
ATOM   4756  N N   . ALA C  1 18  ? 107.196 84.732  279.416 1.00 153.16 ?  48  ALA C N   1 
ATOM   4757  C CA  . ALA C  1 18  ? 108.454 84.896  278.704 1.00 154.69 ?  48  ALA C CA  1 
ATOM   4758  C C   . ALA C  1 18  ? 108.403 83.984  277.486 1.00 157.99 ?  48  ALA C C   1 
ATOM   4759  O O   . ALA C  1 18  ? 107.420 83.270  277.267 1.00 158.85 ?  48  ALA C O   1 
ATOM   4760  C CB  . ALA C  1 18  ? 109.651 84.583  279.605 1.00 148.18 ?  48  ALA C CB  1 
ATOM   4761  N N   . GLU C  1 19  ? 109.471 84.018  276.686 1.00 159.99 ?  49  GLU C N   1 
ATOM   4762  C CA  . GLU C  1 19  ? 109.596 83.204  275.482 1.00 157.65 ?  49  GLU C CA  1 
ATOM   4763  C C   . GLU C  1 19  ? 110.914 82.437  275.452 1.00 154.27 ?  49  GLU C C   1 
ATOM   4764  O O   . GLU C  1 19  ? 111.975 83.005  275.731 1.00 153.12 ?  49  GLU C O   1 
ATOM   4765  C CB  . GLU C  1 19  ? 109.402 84.090  274.254 1.00 162.58 ?  49  GLU C CB  1 
ATOM   4766  C CG  . GLU C  1 19  ? 108.005 84.709  274.311 1.00 167.33 ?  49  GLU C CG  1 
ATOM   4767  C CD  . GLU C  1 19  ? 107.703 85.687  273.207 1.00 178.69 ?  49  GLU C CD  1 
ATOM   4768  O OE1 . GLU C  1 19  ? 108.603 85.973  272.395 1.00 185.98 ?  49  GLU C OE1 1 
ATOM   4769  O OE2 . GLU C  1 19  ? 106.543 86.153  273.140 1.00 189.34 -1 49  GLU C OE2 1 
ATOM   4770  N N   . THR C  1 20  ? 110.847 81.149  275.097 1.00 144.04 ?  50  THR C N   1 
ATOM   4771  C CA  . THR C  1 20  ? 112.027 80.290  275.033 1.00 140.77 ?  50  THR C CA  1 
ATOM   4772  C C   . THR C  1 20  ? 111.921 79.354  273.832 1.00 141.41 ?  50  THR C C   1 
ATOM   4773  O O   . THR C  1 20  ? 110.961 79.404  273.056 1.00 143.42 ?  50  THR C O   1 
ATOM   4774  C CB  . THR C  1 20  ? 112.198 79.473  276.320 1.00 140.71 ?  50  THR C CB  1 
ATOM   4775  O OG1 . THR C  1 20  ? 113.397 78.694  276.233 1.00 139.42 ?  50  THR C OG1 1 
ATOM   4776  C CG2 . THR C  1 20  ? 111.026 78.524  276.504 1.00 140.05 ?  50  THR C CG2 1 
ATOM   4777  N N   . THR C  1 21  ? 112.931 78.495  273.683 1.00 140.64 ?  51  THR C N   1 
ATOM   4778  C CA  . THR C  1 21  ? 113.001 77.528  272.590 1.00 146.14 ?  51  THR C CA  1 
ATOM   4779  C C   . THR C  1 21  ? 112.358 76.212  273.037 1.00 144.01 ?  51  THR C C   1 
ATOM   4780  O O   . THR C  1 21  ? 112.904 75.499  273.886 1.00 139.73 ?  51  THR C O   1 
ATOM   4781  C CB  . THR C  1 21  ? 114.449 77.334  272.140 1.00 151.85 ?  51  THR C CB  1 
ATOM   4782  O OG1 . THR C  1 21  ? 115.204 76.720  273.191 1.00 163.90 ?  51  THR C OG1 1 
ATOM   4783  C CG2 . THR C  1 21  ? 115.089 78.675  271.779 1.00 154.42 ?  51  THR C CG2 1 
ATOM   4784  N N   . LEU C  1 22  ? 111.199 75.903  272.460 1.00 142.96 ?  52  LEU C N   1 
ATOM   4785  C CA  . LEU C  1 22  ? 110.407 74.711  272.746 1.00 140.02 ?  52  LEU C CA  1 
ATOM   4786  C C   . LEU C  1 22  ? 110.860 73.549  271.871 1.00 135.55 ?  52  LEU C C   1 
ATOM   4787  O O   . LEU C  1 22  ? 111.242 73.748  270.715 1.00 142.86 ?  52  LEU C O   1 
ATOM   4788  C CB  . LEU C  1 22  ? 108.920 74.981  272.516 1.00 144.42 ?  52  LEU C CB  1 
ATOM   4789  C CG  . LEU C  1 22  ? 108.304 76.143  273.298 1.00 151.17 ?  52  LEU C CG  1 
ATOM   4790  C CD1 . LEU C  1 22  ? 106.848 76.336  272.907 1.00 152.65 ?  52  LEU C CD1 1 
ATOM   4791  C CD2 . LEU C  1 22  ? 108.433 75.928  274.797 1.00 152.36 ?  52  LEU C CD2 1 
ATOM   4792  N N   . PHE C  1 23  ? 110.825 72.334  272.420 1.00 141.09 ?  53  PHE C N   1 
ATOM   4793  C CA  . PHE C  1 23  ? 111.161 71.158  271.625 1.00 145.68 ?  53  PHE C CA  1 
ATOM   4794  C C   . PHE C  1 23  ? 109.905 70.344  271.308 1.00 150.73 ?  53  PHE C C   1 
ATOM   4795  O O   . PHE C  1 23  ? 108.799 70.659  271.757 1.00 145.64 ?  53  PHE C O   1 
ATOM   4796  C CB  . PHE C  1 23  ? 112.221 70.310  272.340 1.00 147.65 ?  53  PHE C CB  1 
ATOM   4797  C CG  . PHE C  1 23  ? 111.799 69.783  273.692 1.00 150.78 ?  53  PHE C CG  1 
ATOM   4798  C CD1 . PHE C  1 23  ? 111.982 70.546  274.835 1.00 147.62 ?  53  PHE C CD1 1 
ATOM   4799  C CD2 . PHE C  1 23  ? 111.266 68.508  273.826 1.00 155.57 ?  53  PHE C CD2 1 
ATOM   4800  C CE1 . PHE C  1 23  ? 111.616 70.062  276.082 1.00 147.82 ?  53  PHE C CE1 1 
ATOM   4801  C CE2 . PHE C  1 23  ? 110.899 68.017  275.073 1.00 155.98 ?  53  PHE C CE2 1 
ATOM   4802  C CZ  . PHE C  1 23  ? 111.076 68.796  276.201 1.00 149.28 ?  53  PHE C CZ  1 
ATOM   4803  N N   . CYS C  1 24  ? 110.098 69.274  270.525 1.00 166.97 ?  54  CYS C N   1 
ATOM   4804  C CA  . CYS C  1 24  ? 109.021 68.472  269.956 1.00 167.69 ?  54  CYS C CA  1 
ATOM   4805  C C   . CYS C  1 24  ? 108.807 67.173  270.727 1.00 166.18 ?  54  CYS C C   1 
ATOM   4806  O O   . CYS C  1 24  ? 109.550 66.818  271.645 1.00 168.10 ?  54  CYS C O   1 
ATOM   4807  C CB  . CYS C  1 24  ? 109.286 68.136  268.483 1.00 175.10 ?  54  CYS C CB  1 
ATOM   4808  S SG  . CYS C  1 24  ? 110.624 66.948  268.224 1.00 196.64 ?  54  CYS C SG  1 
ATOM   4809  N N   . ALA C  1 25  ? 107.762 66.454  270.310 1.00 174.04 ?  55  ALA C N   1 
ATOM   4810  C CA  . ALA C  1 25  ? 107.388 65.143  270.820 1.00 175.01 ?  55  ALA C CA  1 
ATOM   4811  C C   . ALA C  1 25  ? 106.393 64.504  269.853 1.00 178.12 ?  55  ALA C C   1 
ATOM   4812  O O   . ALA C  1 25  ? 105.455 65.167  269.400 1.00 176.23 ?  55  ALA C O   1 
ATOM   4813  C CB  . ALA C  1 25  ? 106.798 65.271  272.225 1.00 175.99 ?  55  ALA C CB  1 
ATOM   4814  N N   . SER C  1 26  ? 106.580 63.234  269.508 1.00 193.59 ?  56  SER C N   1 
ATOM   4815  C CA  . SER C  1 26  ? 105.696 62.645  268.513 1.00 197.28 ?  56  SER C CA  1 
ATOM   4816  C C   . SER C  1 26  ? 105.575 61.137  268.712 1.00 211.89 ?  56  SER C C   1 
ATOM   4817  O O   . SER C  1 26  ? 105.957 60.332  267.861 1.00 203.21 ?  56  SER C O   1 
ATOM   4818  C CB  . SER C  1 26  ? 106.207 62.973  267.111 1.00 192.90 ?  56  SER C CB  1 
ATOM   4819  O OG  . SER C  1 26  ? 107.559 62.568  266.963 1.00 195.18 ?  56  SER C OG  1 
ATOM   4820  N N   . ASP C  1 27  ? 105.037 60.750  269.873 1.00 216.14 ?  57  ASP C N   1 
ATOM   4821  C CA  . ASP C  1 27  ? 104.732 59.352  270.150 1.00 219.58 ?  57  ASP C CA  1 
ATOM   4822  C C   . ASP C  1 27  ? 105.913 58.419  269.931 1.00 220.16 ?  57  ASP C C   1 
ATOM   4823  O O   . ASP C  1 27  ? 107.076 58.838  269.920 1.00 218.65 ?  57  ASP C O   1 
ATOM   4824  C CB  . ASP C  1 27  ? 103.556 58.896  269.283 1.00 222.45 ?  57  ASP C CB  1 
ATOM   4825  C CG  . ASP C  1 27  ? 102.294 59.679  269.563 1.00 223.73 ?  57  ASP C CG  1 
ATOM   4826  O OD1 . ASP C  1 27  ? 102.044 60.001  270.744 1.00 224.64 ?  57  ASP C OD1 1 
ATOM   4827  O OD2 . ASP C  1 27  ? 101.556 59.976  268.601 1.00 228.64 -1 57  ASP C OD2 1 
ATOM   4828  N N   . ALA C  1 28  ? 105.589 57.142  269.762 1.00 231.38 ?  58  ALA C N   1 
ATOM   4829  C CA  . ALA C  1 28  ? 106.554 56.097  269.474 1.00 234.49 ?  58  ALA C CA  1 
ATOM   4830  C C   . ALA C  1 28  ? 106.121 55.309  268.255 1.00 241.51 ?  58  ALA C C   1 
ATOM   4831  O O   . ALA C  1 28  ? 106.967 54.672  267.616 1.00 245.20 ?  58  ALA C O   1 
ATOM   4832  C CB  . ALA C  1 28  ? 106.716 55.144  270.668 1.00 234.42 ?  58  ALA C CB  1 
ATOM   4833  N N   . LYS C  1 29  ? 104.828 55.339  267.912 1.00 256.71 ?  59  LYS C N   1 
ATOM   4834  C CA  . LYS C  1 29  ? 104.327 54.702  266.703 1.00 262.62 ?  59  LYS C CA  1 
ATOM   4835  C C   . LYS C  1 29  ? 104.578 55.597  265.500 1.00 265.53 ?  59  LYS C C   1 
ATOM   4836  O O   . LYS C  1 29  ? 104.720 55.105  264.375 1.00 267.67 ?  59  LYS C O   1 
ATOM   4837  C CB  . LYS C  1 29  ? 102.841 54.352  266.805 1.00 261.55 ?  59  LYS C CB  1 
ATOM   4838  C CG  . LYS C  1 29  ? 102.351 53.644  265.542 1.00 259.38 ?  59  LYS C CG  1 
ATOM   4839  C CD  . LYS C  1 29  ? 101.082 52.849  265.708 1.00 252.23 ?  59  LYS C CD  1 
ATOM   4840  C CE  . LYS C  1 29  ? 101.396 51.369  265.572 1.00 248.33 ?  59  LYS C CE  1 
ATOM   4841  N NZ  . LYS C  1 29  ? 100.236 50.595  265.056 1.00 242.15 1  59  LYS C NZ  1 
ATOM   4842  N N   . ALA C  1 30  ? 104.664 56.913  265.726 1.00 270.43 ?  60  ALA C N   1 
ATOM   4843  C CA  . ALA C  1 30  ? 104.916 57.823  264.617 1.00 268.96 ?  60  ALA C CA  1 
ATOM   4844  C C   . ALA C  1 30  ? 106.322 57.618  264.086 1.00 268.75 ?  60  ALA C C   1 
ATOM   4845  O O   . ALA C  1 30  ? 106.597 57.914  262.916 1.00 268.69 ?  60  ALA C O   1 
ATOM   4846  C CB  . ALA C  1 30  ? 104.710 59.275  265.056 1.00 260.16 ?  60  ALA C CB  1 
ATOM   4847  N N   . TYR C  1 31  ? 107.223 57.136  264.938 1.00 275.42 ?  61  TYR C N   1 
ATOM   4848  C CA  . TYR C  1 31  ? 108.575 56.850  264.509 1.00 278.42 ?  61  TYR C CA  1 
ATOM   4849  C C   . TYR C  1 31  ? 108.600 55.508  263.776 1.00 279.43 ?  61  TYR C C   1 
ATOM   4850  O O   . TYR C  1 31  ? 109.549 55.243  263.031 1.00 281.29 ?  61  TYR C O   1 
ATOM   4851  C CB  . TYR C  1 31  ? 109.513 56.865  265.732 1.00 281.44 ?  61  TYR C CB  1 
ATOM   4852  C CG  . TYR C  1 31  ? 110.983 56.677  265.422 1.00 286.20 ?  61  TYR C CG  1 
ATOM   4853  C CD1 . TYR C  1 31  ? 111.747 57.738  264.951 1.00 282.07 ?  61  TYR C CD1 1 
ATOM   4854  C CD2 . TYR C  1 31  ? 111.626 55.470  265.675 1.00 290.27 ?  61  TYR C CD2 1 
ATOM   4855  C CE1 . TYR C  1 31  ? 113.096 57.588  264.683 1.00 284.67 ?  61  TYR C CE1 1 
ATOM   4856  C CE2 . TYR C  1 31  ? 112.980 55.313  265.413 1.00 292.44 ?  61  TYR C CE2 1 
ATOM   4857  C CZ  . TYR C  1 31  ? 113.709 56.376  264.919 1.00 289.85 ?  61  TYR C CZ  1 
ATOM   4858  O OH  . TYR C  1 31  ? 115.052 56.213  264.658 1.00 287.36 ?  61  TYR C OH  1 
ATOM   4859  N N   . GLU C  1 32  ? 107.572 54.673  263.981 1.00 268.38 ?  62  GLU C N   1 
ATOM   4860  C CA  . GLU C  1 32  ? 107.459 53.379  263.333 1.00 266.93 ?  62  GLU C CA  1 
ATOM   4861  C C   . GLU C  1 32  ? 106.910 53.490  261.914 1.00 265.44 ?  62  GLU C C   1 
ATOM   4862  O O   . GLU C  1 32  ? 106.865 52.475  261.203 1.00 264.78 ?  62  GLU C O   1 
ATOM   4863  C CB  . GLU C  1 32  ? 106.587 52.419  264.146 1.00 263.70 ?  62  GLU C CB  1 
ATOM   4864  C CG  . GLU C  1 32  ? 107.171 52.092  265.511 1.00 264.92 ?  62  GLU C CG  1 
ATOM   4865  C CD  . GLU C  1 32  ? 106.298 51.162  266.328 1.00 265.82 ?  62  GLU C CD  1 
ATOM   4866  O OE1 . GLU C  1 32  ? 105.351 50.596  265.747 1.00 260.00 ?  62  GLU C OE1 1 
ATOM   4867  O OE2 . GLU C  1 32  ? 106.546 51.010  267.547 1.00 272.71 -1 62  GLU C OE2 1 
ATOM   4868  N N   . THR C  1 33  ? 106.468 54.676  261.507 1.00 267.90 ?  63  THR C N   1 
ATOM   4869  C CA  . THR C  1 33  ? 105.986 54.864  260.145 1.00 265.32 ?  63  THR C CA  1 
ATOM   4870  C C   . THR C  1 33  ? 107.166 54.835  259.193 1.00 265.81 ?  63  THR C C   1 
ATOM   4871  O O   . THR C  1 33  ? 106.994 54.569  258.000 1.00 263.81 ?  63  THR C O   1 
ATOM   4872  C CB  . THR C  1 33  ? 105.204 56.175  259.998 1.00 261.41 ?  63  THR C CB  1 
ATOM   4873  O OG1 . THR C  1 33  ? 104.297 56.329  261.095 1.00 262.38 ?  63  THR C OG1 1 
ATOM   4874  C CG2 . THR C  1 33  ? 104.411 56.193  258.692 1.00 260.55 ?  63  THR C CG2 1 
ATOM   4875  N N   . GLU C  1 34  ? 108.365 55.077  259.744 1.00 254.78 ?  64  GLU C N   1 
ATOM   4876  C CA  . GLU C  1 34  ? 109.665 55.148  259.087 1.00 252.81 ?  64  GLU C CA  1 
ATOM   4877  C C   . GLU C  1 34  ? 109.558 55.745  257.695 1.00 248.19 ?  64  GLU C C   1 
ATOM   4878  O O   . GLU C  1 34  ? 109.283 56.940  257.543 1.00 243.13 ?  64  GLU C O   1 
ATOM   4879  C CB  . GLU C  1 34  ? 110.312 53.754  259.008 1.00 255.01 ?  64  GLU C CB  1 
ATOM   4880  C CG  . GLU C  1 34  ? 109.357 52.585  258.677 1.00 253.50 ?  64  GLU C CG  1 
ATOM   4881  C CD  . GLU C  1 34  ? 110.073 51.305  258.284 1.00 253.36 ?  64  GLU C CD  1 
ATOM   4882  O OE1 . GLU C  1 34  ? 111.294 51.210  258.519 1.00 258.43 ?  64  GLU C OE1 1 
ATOM   4883  O OE2 . GLU C  1 34  ? 109.412 50.394  257.736 1.00 247.29 -1 64  GLU C OE2 1 
ATOM   4884  N N   . LYS C  1 35  ? 109.787 54.913  256.686 1.00 245.75 ?  65  LYS C N   1 
ATOM   4885  C CA  . LYS C  1 35  ? 109.803 55.325  255.288 1.00 244.40 ?  65  LYS C CA  1 
ATOM   4886  C C   . LYS C  1 35  ? 110.820 56.441  255.033 1.00 245.89 ?  65  LYS C C   1 
ATOM   4887  O O   . LYS C  1 35  ? 110.507 57.450  254.396 1.00 245.86 ?  65  LYS C O   1 
ATOM   4888  C CB  . LYS C  1 35  ? 108.405 55.767  254.855 1.00 239.58 ?  65  LYS C CB  1 
ATOM   4889  C CG  . LYS C  1 35  ? 107.363 54.661  254.816 1.00 239.48 ?  65  LYS C CG  1 
ATOM   4890  C CD  . LYS C  1 35  ? 107.764 53.447  254.015 1.00 240.94 ?  65  LYS C CD  1 
ATOM   4891  C CE  . LYS C  1 35  ? 106.729 52.351  254.223 1.00 240.97 ?  65  LYS C CE  1 
ATOM   4892  N NZ  . LYS C  1 35  ? 107.089 51.076  253.555 1.00 242.79 1  65  LYS C NZ  1 
ATOM   4893  N N   . HIS C  1 36  ? 112.047 56.263  255.540 1.00 251.13 ?  66  HIS C N   1 
ATOM   4894  C CA  . HIS C  1 36  ? 113.120 57.241  255.323 1.00 250.67 ?  66  HIS C CA  1 
ATOM   4895  C C   . HIS C  1 36  ? 112.732 58.652  255.772 1.00 244.38 ?  66  HIS C C   1 
ATOM   4896  O O   . HIS C  1 36  ? 112.726 59.606  254.987 1.00 234.84 ?  66  HIS C O   1 
ATOM   4897  C CB  . HIS C  1 36  ? 113.625 57.210  253.880 1.00 248.17 ?  66  HIS C CB  1 
ATOM   4898  C CG  . HIS C  1 36  ? 114.309 55.927  253.525 1.00 252.57 ?  66  HIS C CG  1 
ATOM   4899  N ND1 . HIS C  1 36  ? 114.442 55.478  252.230 1.00 250.94 ?  66  HIS C ND1 1 
ATOM   4900  C CD2 . HIS C  1 36  ? 114.925 55.008  254.307 1.00 255.76 ?  66  HIS C CD2 1 
ATOM   4901  C CE1 . HIS C  1 36  ? 115.098 54.331  252.229 1.00 255.18 ?  66  HIS C CE1 1 
ATOM   4902  N NE2 . HIS C  1 36  ? 115.403 54.024  253.477 1.00 256.60 ?  66  HIS C NE2 1 
ATOM   4903  N N   . ASN C  1 37  ? 112.385 58.758  257.057 1.00 244.27 ?  67  ASN C N   1 
ATOM   4904  C CA  . ASN C  1 37  ? 112.015 60.030  257.666 1.00 234.57 ?  67  ASN C CA  1 
ATOM   4905  C C   . ASN C  1 37  ? 110.834 60.710  257.003 1.00 224.22 ?  67  ASN C C   1 
ATOM   4906  O O   . ASN C  1 37  ? 111.006 61.535  256.099 1.00 218.66 ?  67  ASN C O   1 
ATOM   4907  C CB  . ASN C  1 37  ? 113.207 60.997  257.585 1.00 229.93 ?  67  ASN C CB  1 
ATOM   4908  C CG  . ASN C  1 37  ? 113.460 61.742  258.864 1.00 226.77 ?  67  ASN C CG  1 
ATOM   4909  O OD1 . ASN C  1 37  ? 112.686 61.656  259.812 1.00 226.71 ?  67  ASN C OD1 1 
ATOM   4910  N ND2 . ASN C  1 37  ? 114.520 62.549  258.868 1.00 222.34 ?  67  ASN C ND2 1 
ATOM   4911  N N   . VAL C  1 38  ? 109.628 60.387  257.455 1.00 216.23 ?  68  VAL C N   1 
ATOM   4912  C CA  . VAL C  1 38  ? 108.454 61.050  256.919 1.00 210.11 ?  68  VAL C CA  1 
ATOM   4913  C C   . VAL C  1 38  ? 108.276 62.353  257.679 1.00 208.54 ?  68  VAL C C   1 
ATOM   4914  O O   . VAL C  1 38  ? 108.341 62.381  258.914 1.00 209.13 ?  68  VAL C O   1 
ATOM   4915  C CB  . VAL C  1 38  ? 107.215 60.153  257.044 1.00 210.88 ?  68  VAL C CB  1 
ATOM   4916  C CG1 . VAL C  1 38  ? 107.274 59.045  256.012 1.00 211.62 ?  68  VAL C CG1 1 
ATOM   4917  C CG2 . VAL C  1 38  ? 107.120 59.578  258.447 1.00 212.40 ?  68  VAL C CG2 1 
ATOM   4918  N N   . TRP C  1 39  ? 108.077 63.439  256.940 1.00 188.66 ?  69  TRP C N   1 
ATOM   4919  C CA  . TRP C  1 39  ? 107.893 64.757  257.528 1.00 186.73 ?  69  TRP C CA  1 
ATOM   4920  C C   . TRP C  1 39  ? 109.081 65.162  258.397 1.00 186.62 ?  69  TRP C C   1 
ATOM   4921  O O   . TRP C  1 39  ? 110.123 65.585  257.887 1.00 185.61 ?  69  TRP C O   1 
ATOM   4922  C CB  . TRP C  1 39  ? 106.596 64.860  258.329 1.00 186.77 ?  69  TRP C CB  1 
ATOM   4923  C CG  . TRP C  1 39  ? 106.240 66.299  258.604 1.00 184.53 ?  69  TRP C CG  1 
ATOM   4924  C CD1 . TRP C  1 39  ? 105.943 66.861  259.811 1.00 183.92 ?  69  TRP C CD1 1 
ATOM   4925  C CD2 . TRP C  1 39  ? 106.134 67.355  257.634 1.00 182.42 ?  69  TRP C CD2 1 
ATOM   4926  N NE1 . TRP C  1 39  ? 105.667 68.200  259.656 1.00 181.56 ?  69  TRP C NE1 1 
ATOM   4927  C CE2 . TRP C  1 39  ? 105.775 68.527  258.329 1.00 180.67 ?  69  TRP C CE2 1 
ATOM   4928  C CE3 . TRP C  1 39  ? 106.308 67.422  256.246 1.00 181.74 ?  69  TRP C CE3 1 
ATOM   4929  C CZ2 . TRP C  1 39  ? 105.589 69.749  257.686 1.00 178.42 ?  69  TRP C CZ2 1 
ATOM   4930  C CZ3 . TRP C  1 39  ? 106.125 68.634  255.612 1.00 179.50 ?  69  TRP C CZ3 1 
ATOM   4931  C CH2 . TRP C  1 39  ? 105.768 69.782  256.330 1.00 177.95 ?  69  TRP C CH2 1 
ATOM   4932  N N   . ALA C  1 40  ? 108.923 65.009  259.720 1.00 183.93 ?  70  ALA C N   1 
ATOM   4933  C CA  . ALA C  1 40  ? 109.870 65.484  260.723 1.00 183.42 ?  70  ALA C CA  1 
ATOM   4934  C C   . ALA C  1 40  ? 110.461 64.427  261.636 1.00 186.23 ?  70  ALA C C   1 
ATOM   4935  O O   . ALA C  1 40  ? 111.657 64.487  261.941 1.00 186.86 ?  70  ALA C O   1 
ATOM   4936  C CB  . ALA C  1 40  ? 109.159 66.490  261.631 1.00 182.57 ?  70  ALA C CB  1 
ATOM   4937  N N   . THR C  1 41  ? 109.657 63.473  262.096 1.00 206.36 ?  71  THR C N   1 
ATOM   4938  C CA  . THR C  1 41  ? 110.104 62.525  263.108 1.00 215.61 ?  71  THR C CA  1 
ATOM   4939  C C   . THR C  1 41  ? 111.380 61.768  262.767 1.00 221.40 ?  71  THR C C   1 
ATOM   4940  O O   . THR C  1 41  ? 111.330 60.678  262.187 1.00 223.19 ?  71  THR C O   1 
ATOM   4941  C CB  . THR C  1 41  ? 108.992 61.520  263.413 1.00 222.12 ?  71  THR C CB  1 
ATOM   4942  O OG1 . THR C  1 41  ? 107.761 62.222  263.624 1.00 222.20 ?  71  THR C OG1 1 
ATOM   4943  C CG2 . THR C  1 41  ? 109.335 60.728  264.668 1.00 228.04 ?  71  THR C CG2 1 
ATOM   4944  N N   . HIS C  1 42  ? 112.528 62.345  263.128 1.00 228.13 ?  72  HIS C N   1 
ATOM   4945  C CA  . HIS C  1 42  ? 113.820 61.687  262.960 1.00 231.99 ?  72  HIS C CA  1 
ATOM   4946  C C   . HIS C  1 42  ? 114.504 61.619  264.316 1.00 234.58 ?  72  HIS C C   1 
ATOM   4947  O O   . HIS C  1 42  ? 114.732 60.522  264.836 1.00 240.07 ?  72  HIS C O   1 
ATOM   4948  C CB  . HIS C  1 42  ? 114.708 62.415  261.940 1.00 228.30 ?  72  HIS C CB  1 
ATOM   4949  C CG  . HIS C  1 42  ? 115.987 61.694  261.622 1.00 229.25 ?  72  HIS C CG  1 
ATOM   4950  N ND1 . HIS C  1 42  ? 116.458 60.639  262.374 1.00 235.77 ?  72  HIS C ND1 1 
ATOM   4951  C CD2 . HIS C  1 42  ? 116.881 61.864  260.618 1.00 229.96 ?  72  HIS C CD2 1 
ATOM   4952  C CE1 . HIS C  1 42  ? 117.590 60.198  261.856 1.00 235.87 ?  72  HIS C CE1 1 
ATOM   4953  N NE2 . HIS C  1 42  ? 117.869 60.924  260.789 1.00 233.42 ?  72  HIS C NE2 1 
ATOM   4954  N N   . ALA C  1 43  ? 114.837 62.768  264.905 1.00 210.02 ?  73  ALA C N   1 
ATOM   4955  C CA  . ALA C  1 43  ? 115.429 62.836  266.231 1.00 206.22 ?  73  ALA C CA  1 
ATOM   4956  C C   . ALA C  1 43  ? 114.463 63.501  267.206 1.00 206.11 ?  73  ALA C C   1 
ATOM   4957  O O   . ALA C  1 43  ? 114.883 64.189  268.140 1.00 205.67 ?  73  ALA C O   1 
ATOM   4958  C CB  . ALA C  1 43  ? 116.763 63.580  266.198 1.00 206.36 ?  73  ALA C CB  1 
ATOM   4959  N N   . CYS C  1 44  ? 113.161 63.307  266.993 1.00 204.95 ?  74  CYS C N   1 
ATOM   4960  C CA  . CYS C  1 44  ? 112.166 63.908  267.865 1.00 204.45 ?  74  CYS C CA  1 
ATOM   4961  C C   . CYS C  1 44  ? 111.972 63.004  269.080 1.00 200.02 ?  74  CYS C C   1 
ATOM   4962  O O   . CYS C  1 44  ? 111.975 61.775  268.965 1.00 202.51 ?  74  CYS C O   1 
ATOM   4963  C CB  . CYS C  1 44  ? 110.853 64.141  267.122 1.00 204.16 ?  74  CYS C CB  1 
ATOM   4964  S SG  . CYS C  1 44  ? 109.695 65.134  268.087 1.00 201.13 ?  74  CYS C SG  1 
ATOM   4965  N N   . VAL C  1 45  ? 111.795 63.622  270.239 1.00 183.81 ?  75  VAL C N   1 
ATOM   4966  C CA  . VAL C  1 45  ? 111.659 62.899  271.512 1.00 187.32 ?  75  VAL C CA  1 
ATOM   4967  C C   . VAL C  1 45  ? 110.337 62.136  271.580 1.00 190.32 ?  75  VAL C C   1 
ATOM   4968  O O   . VAL C  1 45  ? 109.273 62.711  271.293 1.00 189.59 ?  75  VAL C O   1 
ATOM   4969  C CB  . VAL C  1 45  ? 111.783 63.872  272.683 1.00 186.68 ?  75  VAL C CB  1 
ATOM   4970  C CG1 . VAL C  1 45  ? 111.616 63.135  274.005 1.00 190.24 ?  75  VAL C CG1 1 
ATOM   4971  C CG2 . VAL C  1 45  ? 113.123 64.587  272.630 1.00 183.85 ?  75  VAL C CG2 1 
ATOM   4972  N N   . PRO C  1 46  ? 110.364 60.840  271.896 1.00 198.06 ?  76  PRO C N   1 
ATOM   4973  C CA  . PRO C  1 46  ? 109.119 60.078  272.076 1.00 203.96 ?  76  PRO C CA  1 
ATOM   4974  C C   . PRO C  1 46  ? 108.255 60.677  273.185 1.00 207.44 ?  76  PRO C C   1 
ATOM   4975  O O   . PRO C  1 46  ? 108.754 61.064  274.245 1.00 209.33 ?  76  PRO C O   1 
ATOM   4976  C CB  . PRO C  1 46  ? 109.611 58.669  272.426 1.00 206.80 ?  76  PRO C CB  1 
ATOM   4977  C CG  . PRO C  1 46  ? 110.981 58.596  271.824 1.00 203.04 ?  76  PRO C CG  1 
ATOM   4978  C CD  . PRO C  1 46  ? 111.555 59.976  271.968 1.00 197.48 ?  76  PRO C CD  1 
ATOM   4979  N N   . THR C  1 47  ? 106.950 60.749  272.932 1.00 208.02 ?  77  THR C N   1 
ATOM   4980  C CA  . THR C  1 47  ? 106.005 61.328  273.885 1.00 208.89 ?  77  THR C CA  1 
ATOM   4981  C C   . THR C  1 47  ? 105.877 60.488  275.154 1.00 213.10 ?  77  THR C C   1 
ATOM   4982  O O   . THR C  1 47  ? 105.891 59.255  275.111 1.00 218.35 ?  77  THR C O   1 
ATOM   4983  C CB  . THR C  1 47  ? 104.627 61.490  273.240 1.00 207.54 ?  77  THR C CB  1 
ATOM   4984  O OG1 . THR C  1 47  ? 104.761 62.174  271.989 1.00 203.82 ?  77  THR C OG1 1 
ATOM   4985  C CG2 . THR C  1 47  ? 103.693 62.285  274.151 1.00 200.95 ?  77  THR C CG2 1 
ATOM   4986  N N   . ASP C  1 48  ? 105.770 61.178  276.291 1.00 214.47 ?  78  ASP C N   1 
ATOM   4987  C CA  . ASP C  1 48  ? 105.580 60.552  277.598 1.00 222.12 ?  78  ASP C CA  1 
ATOM   4988  C C   . ASP C  1 48  ? 104.323 59.687  277.587 1.00 225.71 ?  78  ASP C C   1 
ATOM   4989  O O   . ASP C  1 48  ? 103.231 60.193  277.285 1.00 223.62 ?  78  ASP C O   1 
ATOM   4990  C CB  . ASP C  1 48  ? 105.480 61.621  278.692 1.00 219.69 ?  78  ASP C CB  1 
ATOM   4991  C CG  . ASP C  1 48  ? 105.714 61.062  280.095 1.00 217.77 ?  78  ASP C CG  1 
ATOM   4992  O OD1 . ASP C  1 48  ? 105.262 59.935  280.384 1.00 221.13 ?  78  ASP C OD1 1 
ATOM   4993  O OD2 . ASP C  1 48  ? 106.358 61.755  280.913 1.00 212.63 -1 78  ASP C OD2 1 
ATOM   4994  N N   . PRO C  1 49  ? 104.435 58.388  277.885 1.00 219.85 ?  79  PRO C N   1 
ATOM   4995  C CA  . PRO C  1 49  ? 103.255 57.500  277.875 1.00 220.76 ?  79  PRO C CA  1 
ATOM   4996  C C   . PRO C  1 49  ? 102.065 57.959  278.709 1.00 222.60 ?  79  PRO C C   1 
ATOM   4997  O O   . PRO C  1 49  ? 100.923 57.770  278.272 1.00 222.48 ?  79  PRO C O   1 
ATOM   4998  C CB  . PRO C  1 49  ? 103.828 56.178  278.404 1.00 222.75 ?  79  PRO C CB  1 
ATOM   4999  C CG  . PRO C  1 49  ? 105.266 56.212  278.011 1.00 219.41 ?  79  PRO C CG  1 
ATOM   5000  C CD  . PRO C  1 49  ? 105.685 57.649  278.139 1.00 219.25 ?  79  PRO C CD  1 
ATOM   5001  N N   . ASN C  1 50  ? 102.281 58.547  279.889 1.00 219.88 ?  80  ASN C N   1 
ATOM   5002  C CA  . ASN C  1 50  ? 101.197 59.027  280.749 1.00 218.15 ?  80  ASN C CA  1 
ATOM   5003  C C   . ASN C  1 50  ? 101.403 60.513  281.018 1.00 209.55 ?  80  ASN C C   1 
ATOM   5004  O O   . ASN C  1 50  ? 101.944 60.896  282.067 1.00 206.79 ?  80  ASN C O   1 
ATOM   5005  C CB  . ASN C  1 50  ? 101.130 58.258  282.071 1.00 224.46 ?  80  ASN C CB  1 
ATOM   5006  C CG  . ASN C  1 50  ? 100.851 56.772  281.889 1.00 234.56 ?  80  ASN C CG  1 
ATOM   5007  O OD1 . ASN C  1 50  ? 101.349 56.136  280.961 1.00 238.49 ?  80  ASN C OD1 1 
ATOM   5008  N ND2 . ASN C  1 50  ? 100.038 56.217  282.782 1.00 239.34 ?  80  ASN C ND2 1 
ATOM   5009  N N   . PRO C  1 51  ? 100.997 61.378  280.087 1.00 208.97 ?  81  PRO C N   1 
ATOM   5010  C CA  . PRO C  1 51  ? 101.178 62.817  280.303 1.00 202.30 ?  81  PRO C CA  1 
ATOM   5011  C C   . PRO C  1 51  ? 100.365 63.278  281.503 1.00 199.38 ?  81  PRO C C   1 
ATOM   5012  O O   . PRO C  1 51  ? 99.303  62.731  281.808 1.00 203.89 ?  81  PRO C O   1 
ATOM   5013  C CB  . PRO C  1 51  ? 100.664 63.440  278.997 1.00 202.53 ?  81  PRO C CB  1 
ATOM   5014  C CG  . PRO C  1 51  ? 100.701 62.308  277.983 1.00 206.95 ?  81  PRO C CG  1 
ATOM   5015  C CD  . PRO C  1 51  ? 100.393 61.079  278.778 1.00 212.90 ?  81  PRO C CD  1 
ATOM   5016  N N   . GLN C  1 52  ? 100.877 64.294  282.190 1.00 201.60 ?  82  GLN C N   1 
ATOM   5017  C CA  . GLN C  1 52  ? 100.218 64.842  283.366 1.00 198.26 ?  82  GLN C CA  1 
ATOM   5018  C C   . GLN C  1 52  ? 99.787  66.281  283.136 1.00 187.01 ?  82  GLN C C   1 
ATOM   5019  O O   . GLN C  1 52  ? 100.563 67.095  282.622 1.00 180.67 ?  82  GLN C O   1 
ATOM   5020  C CB  . GLN C  1 52  ? 101.126 64.755  284.596 1.00 199.75 ?  82  GLN C CB  1 
ATOM   5021  C CG  . GLN C  1 52  ? 101.414 63.334  285.047 1.00 208.17 ?  82  GLN C CG  1 
ATOM   5022  C CD  . GLN C  1 52  ? 100.172 62.633  285.567 1.00 209.35 ?  82  GLN C CD  1 
ATOM   5023  O OE1 . GLN C  1 52  ? 99.200  63.278  285.963 1.00 204.71 ?  82  GLN C OE1 1 
ATOM   5024  N NE2 . GLN C  1 52  ? 100.202 61.306  285.575 1.00 211.11 ?  82  GLN C NE2 1 
ATOM   5025  N N   . GLU C  1 53  ? 98.546  66.580  283.513 1.00 174.94 ?  83  GLU C N   1 
ATOM   5026  C CA  . GLU C  1 53  ? 97.970  67.917  283.425 1.00 170.05 ?  83  GLU C CA  1 
ATOM   5027  C C   . GLU C  1 53  ? 97.468  68.247  284.824 1.00 168.50 ?  83  GLU C C   1 
ATOM   5028  O O   . GLU C  1 53  ? 96.510  67.638  285.312 1.00 171.16 ?  83  GLU C O   1 
ATOM   5029  C CB  . GLU C  1 53  ? 96.873  68.043  282.357 1.00 172.88 ?  83  GLU C CB  1 
ATOM   5030  C CG  . GLU C  1 53  ? 95.546  67.328  282.575 1.00 181.50 ?  83  GLU C CG  1 
ATOM   5031  C CD  . GLU C  1 53  ? 94.556  67.634  281.464 1.00 189.74 ?  83  GLU C CD  1 
ATOM   5032  O OE1 . GLU C  1 53  ? 95.004  67.920  280.333 1.00 187.85 ?  83  GLU C OE1 1 
ATOM   5033  O OE2 . GLU C  1 53  ? 93.333  67.601  281.721 1.00 193.11 -1 83  GLU C OE2 1 
ATOM   5034  N N   . ILE C  1 54  ? 98.155  69.161  285.491 1.00 165.42 ?  84  ILE C N   1 
ATOM   5035  C CA  . ILE C  1 54  ? 97.824  69.530  286.858 1.00 165.47 ?  84  ILE C CA  1 
ATOM   5036  C C   . ILE C  1 54  ? 96.900  70.732  286.760 1.00 164.52 ?  84  ILE C C   1 
ATOM   5037  O O   . ILE C  1 54  ? 97.308  71.806  286.304 1.00 161.72 ?  84  ILE C O   1 
ATOM   5038  C CB  . ILE C  1 54  ? 99.098  69.856  287.649 1.00 162.87 ?  84  ILE C CB  1 
ATOM   5039  C CG1 . ILE C  1 54  ? 99.929  68.589  287.834 1.00 164.57 ?  84  ILE C CG1 1 
ATOM   5040  C CG2 . ILE C  1 54  ? 98.764  70.467  288.992 1.00 162.27 ?  84  ILE C CG2 1 
ATOM   5041  C CD1 . ILE C  1 54  ? 101.364 68.864  288.140 1.00 161.95 ?  84  ILE C CD1 1 
ATOM   5042  N N   . HIS C  1 55  ? 95.657  70.555  287.200 1.00 172.61 ?  85  HIS C N   1 
ATOM   5043  C CA  . HIS C  1 55  ? 94.671  71.627  287.173 1.00 172.39 ?  85  HIS C CA  1 
ATOM   5044  C C   . HIS C  1 55  ? 94.936  72.570  288.343 1.00 170.08 ?  85  HIS C C   1 
ATOM   5045  O O   . HIS C  1 55  ? 94.756  72.194  289.507 1.00 170.93 ?  85  HIS C O   1 
ATOM   5046  C CB  . HIS C  1 55  ? 93.276  71.010  287.211 1.00 176.07 ?  85  HIS C CB  1 
ATOM   5047  C CG  . HIS C  1 55  ? 92.163  72.006  287.230 1.00 181.60 ?  85  HIS C CG  1 
ATOM   5048  N ND1 . HIS C  1 55  ? 92.044  72.992  286.274 1.00 182.07 ?  85  HIS C ND1 1 
ATOM   5049  C CD2 . HIS C  1 55  ? 91.092  72.140  288.047 1.00 184.06 ?  85  HIS C CD2 1 
ATOM   5050  C CE1 . HIS C  1 55  ? 90.964  73.711  286.521 1.00 183.15 ?  85  HIS C CE1 1 
ATOM   5051  N NE2 . HIS C  1 55  ? 90.367  73.214  287.590 1.00 186.31 ?  85  HIS C NE2 1 
ATOM   5052  N N   . LEU C  1 56  ? 95.375  73.791  288.029 1.00 158.42 ?  86  LEU C N   1 
ATOM   5053  C CA  . LEU C  1 56  ? 95.710  74.819  289.019 1.00 155.84 ?  86  LEU C CA  1 
ATOM   5054  C C   . LEU C  1 56  ? 94.474  75.525  289.568 1.00 157.10 ?  86  LEU C C   1 
ATOM   5055  O O   . LEU C  1 56  ? 93.959  76.470  288.965 1.00 157.15 ?  86  LEU C O   1 
ATOM   5056  C CB  . LEU C  1 56  ? 96.692  75.826  288.430 1.00 152.59 ?  86  LEU C CB  1 
ATOM   5057  C CG  . LEU C  1 56  ? 97.899  75.254  287.686 1.00 151.39 ?  86  LEU C CG  1 
ATOM   5058  C CD1 . LEU C  1 56  ? 98.861  76.366  287.304 1.00 148.08 ?  86  LEU C CD1 1 
ATOM   5059  C CD2 . LEU C  1 56  ? 98.606  74.203  288.532 1.00 151.55 ?  86  LEU C CD2 1 
ATOM   5060  N N   . GLU C  1 57  ? 93.988  75.047  290.709 1.00 175.00 ?  87  GLU C N   1 
ATOM   5061  C CA  . GLU C  1 57  ? 92.813  75.617  291.355 1.00 170.07 ?  87  GLU C CA  1 
ATOM   5062  C C   . GLU C  1 57  ? 93.089  77.052  291.807 1.00 164.28 ?  87  GLU C C   1 
ATOM   5063  O O   . GLU C  1 57  ? 94.222  77.411  292.143 1.00 159.26 ?  87  GLU C O   1 
ATOM   5064  C CB  . GLU C  1 57  ? 92.405  74.758  292.552 1.00 167.40 ?  87  GLU C CB  1 
ATOM   5065  C CG  . GLU C  1 57  ? 91.038  75.084  293.133 1.00 169.58 ?  87  GLU C CG  1 
ATOM   5066  C CD  . GLU C  1 57  ? 89.899  74.750  292.193 1.00 175.69 ?  87  GLU C CD  1 
ATOM   5067  O OE1 . GLU C  1 57  ? 90.100  73.922  291.279 1.00 182.06 ?  87  GLU C OE1 1 
ATOM   5068  O OE2 . GLU C  1 57  ? 88.799  75.314  292.372 1.00 177.31 -1 87  GLU C OE2 1 
ATOM   5069  N N   . ASN C  1 58  ? 92.037  77.877  291.815 1.00 190.19 ?  88  ASN C N   1 
ATOM   5070  C CA  . ASN C  1 58  ? 92.065  79.276  292.250 1.00 186.59 ?  88  ASN C CA  1 
ATOM   5071  C C   . ASN C  1 58  ? 92.948  80.190  291.395 1.00 185.46 ?  88  ASN C C   1 
ATOM   5072  O O   . ASN C  1 58  ? 93.129  81.365  291.745 1.00 182.65 ?  88  ASN C O   1 
ATOM   5073  C CB  . ASN C  1 58  ? 92.502  79.387  293.725 1.00 186.39 ?  88  ASN C CB  1 
ATOM   5074  C CG  . ASN C  1 58  ? 91.400  79.002  294.718 1.00 186.20 ?  88  ASN C CG  1 
ATOM   5075  O OD1 . ASN C  1 58  ? 90.209  79.080  294.405 1.00 194.70 ?  88  ASN C OD1 1 
ATOM   5076  N ND2 . ASN C  1 58  ? 91.800  78.593  295.929 1.00 181.69 ?  88  ASN C ND2 1 
ATOM   5077  N N   . VAL C  1 59  ? 93.516  79.698  290.296 1.00 179.28 ?  89  VAL C N   1 
ATOM   5078  C CA  . VAL C  1 59  ? 94.445  80.468  289.469 1.00 175.14 ?  89  VAL C CA  1 
ATOM   5079  C C   . VAL C  1 59  ? 93.710  81.054  288.267 1.00 173.05 ?  89  VAL C C   1 
ATOM   5080  O O   . VAL C  1 59  ? 93.007  80.330  287.549 1.00 174.66 ?  89  VAL C O   1 
ATOM   5081  C CB  . VAL C  1 59  ? 95.635  79.606  289.014 1.00 171.54 ?  89  VAL C CB  1 
ATOM   5082  C CG1 . VAL C  1 59  ? 96.523  80.398  288.066 1.00 165.79 ?  89  VAL C CG1 1 
ATOM   5083  C CG2 . VAL C  1 59  ? 96.433  79.117  290.215 1.00 168.47 ?  89  VAL C CG2 1 
ATOM   5084  N N   . THR C  1 60  ? 93.862  82.369  288.057 1.00 170.75 ?  90  THR C N   1 
ATOM   5085  C CA  . THR C  1 60  ? 93.283  83.080  286.915 1.00 175.91 ?  90  THR C CA  1 
ATOM   5086  C C   . THR C  1 60  ? 94.399  83.775  286.134 1.00 173.77 ?  90  THR C C   1 
ATOM   5087  O O   . THR C  1 60  ? 94.961  84.778  286.594 1.00 169.92 ?  90  THR C O   1 
ATOM   5088  C CB  . THR C  1 60  ? 92.232  84.093  287.382 1.00 177.84 ?  90  THR C CB  1 
ATOM   5089  O OG1 . THR C  1 60  ? 91.178  83.424  288.082 1.00 180.02 ?  90  THR C OG1 1 
ATOM   5090  C CG2 . THR C  1 60  ? 91.636  84.806  286.211 1.00 178.89 ?  90  THR C CG2 1 
ATOM   5091  N N   . GLU C  1 61  ? 94.714  83.240  284.953 1.00 166.84 ?  91  GLU C N   1 
ATOM   5092  C CA  . GLU C  1 61  ? 95.778  83.757  284.103 1.00 164.60 ?  91  GLU C CA  1 
ATOM   5093  C C   . GLU C  1 61  ? 95.246  84.276  282.774 1.00 166.79 ?  91  GLU C C   1 
ATOM   5094  O O   . GLU C  1 61  ? 94.369  83.659  282.158 1.00 169.67 ?  91  GLU C O   1 
ATOM   5095  C CB  . GLU C  1 61  ? 96.833  82.681  283.839 1.00 162.53 ?  91  GLU C CB  1 
ATOM   5096  C CG  . GLU C  1 61  ? 98.090  83.210  283.147 1.00 159.72 ?  91  GLU C CG  1 
ATOM   5097  C CD  . GLU C  1 61  ? 99.028  83.972  284.083 1.00 156.54 ?  91  GLU C CD  1 
ATOM   5098  O OE1 . GLU C  1 61  ? 98.756  84.030  285.300 1.00 156.20 ?  91  GLU C OE1 1 
ATOM   5099  O OE2 . GLU C  1 61  ? 100.050 84.511  283.603 1.00 154.34 -1 91  GLU C OE2 1 
ATOM   5100  N N   . GLU C  1 62  ? 95.797  85.405  282.329 1.00 164.85 ?  92  GLU C N   1 
ATOM   5101  C CA  . GLU C  1 62  ? 95.389  86.031  281.079 1.00 166.72 ?  92  GLU C CA  1 
ATOM   5102  C C   . GLU C  1 62  ? 96.176  85.453  279.908 1.00 165.12 ?  92  GLU C C   1 
ATOM   5103  O O   . GLU C  1 62  ? 97.412  85.441  279.924 1.00 161.89 ?  92  GLU C O   1 
ATOM   5104  C CB  . GLU C  1 62  ? 95.559  87.551  281.125 1.00 166.50 ?  92  GLU C CB  1 
ATOM   5105  C CG  . GLU C  1 62  ? 94.765  88.248  282.215 1.00 168.26 ?  92  GLU C CG  1 
ATOM   5106  C CD  . GLU C  1 62  ? 94.923  89.759  282.175 1.00 174.49 ?  92  GLU C CD  1 
ATOM   5107  O OE1 . GLU C  1 62  ? 95.487  90.275  281.186 1.00 175.95 ?  92  GLU C OE1 1 
ATOM   5108  O OE2 . GLU C  1 62  ? 94.490  90.432  283.134 1.00 182.28 -1 92  GLU C OE2 1 
ATOM   5109  N N   . PHE C  1 63  ? 95.459  84.990  278.892 1.00 155.78 ?  93  PHE C N   1 
ATOM   5110  C CA  . PHE C  1 63  ? 96.039  84.451  277.670 1.00 154.35 ?  93  PHE C CA  1 
ATOM   5111  C C   . PHE C  1 63  ? 95.902  85.456  276.528 1.00 154.99 ?  93  PHE C C   1 
ATOM   5112  O O   . PHE C  1 63  ? 95.144  86.425  276.607 1.00 157.47 ?  93  PHE C O   1 
ATOM   5113  C CB  . PHE C  1 63  ? 95.369  83.126  277.297 1.00 156.04 ?  93  PHE C CB  1 
ATOM   5114  C CG  . PHE C  1 63  ? 95.809  81.967  278.141 1.00 155.18 ?  93  PHE C CG  1 
ATOM   5115  C CD1 . PHE C  1 63  ? 95.194  81.706  279.352 1.00 156.90 ?  93  PHE C CD1 1 
ATOM   5116  C CD2 . PHE C  1 63  ? 96.833  81.135  277.721 1.00 152.88 ?  93  PHE C CD2 1 
ATOM   5117  C CE1 . PHE C  1 63  ? 95.594  80.640  280.131 1.00 156.25 ?  93  PHE C CE1 1 
ATOM   5118  C CE2 . PHE C  1 63  ? 97.237  80.065  278.497 1.00 152.53 ?  93  PHE C CE2 1 
ATOM   5119  C CZ  . PHE C  1 63  ? 96.617  79.818  279.703 1.00 154.22 ?  93  PHE C CZ  1 
ATOM   5120  N N   . ASN C  1 64  ? 96.657  85.220  275.452 1.00 174.89 ?  94  ASN C N   1 
ATOM   5121  C CA  . ASN C  1 64  ? 96.577  86.092  274.277 1.00 177.40 ?  94  ASN C CA  1 
ATOM   5122  C C   . ASN C  1 64  ? 96.986  85.290  273.044 1.00 175.88 ?  94  ASN C C   1 
ATOM   5123  O O   . ASN C  1 64  ? 98.178  85.171  272.743 1.00 185.88 ?  94  ASN C O   1 
ATOM   5124  C CB  . ASN C  1 64  ? 97.451  87.328  274.444 1.00 176.03 ?  94  ASN C CB  1 
ATOM   5125  C CG  . ASN C  1 64  ? 97.083  88.438  273.472 1.00 179.26 ?  94  ASN C CG  1 
ATOM   5126  O OD1 . ASN C  1 64  ? 96.589  88.178  272.374 1.00 177.84 ?  94  ASN C OD1 1 
ATOM   5127  N ND2 . ASN C  1 64  ? 97.331  89.681  273.869 1.00 178.44 ?  94  ASN C ND2 1 
ATOM   5128  N N   . MET C  1 65  ? 95.989  84.751  272.334 1.00 167.48 ?  95  MET C N   1 
ATOM   5129  C CA  . MET C  1 65  ? 96.257  83.928  271.160 1.00 166.19 ?  95  MET C CA  1 
ATOM   5130  C C   . MET C  1 65  ? 96.843  84.741  270.015 1.00 167.51 ?  95  MET C C   1 
ATOM   5131  O O   . MET C  1 65  ? 97.480  84.166  269.126 1.00 166.37 ?  95  MET C O   1 
ATOM   5132  C CB  . MET C  1 65  ? 94.981  83.230  270.690 1.00 168.66 ?  95  MET C CB  1 
ATOM   5133  C CG  . MET C  1 65  ? 93.873  84.190  270.303 1.00 172.67 ?  95  MET C CG  1 
ATOM   5134  S SD  . MET C  1 65  ? 92.428  83.362  269.618 1.00 174.32 ?  95  MET C SD  1 
ATOM   5135  C CE  . MET C  1 65  ? 93.152  82.547  268.199 1.00 171.45 ?  95  MET C CE  1 
ATOM   5136  N N   . TRP C  1 66  ? 96.647  86.062  270.016 1.00 178.95 ?  96  TRP C N   1 
ATOM   5137  C CA  . TRP C  1 66  ? 97.124  86.904  268.929 1.00 178.93 ?  96  TRP C CA  1 
ATOM   5138  C C   . TRP C  1 66  ? 98.512  87.467  269.197 1.00 172.93 ?  96  TRP C C   1 
ATOM   5139  O O   . TRP C  1 66  ? 99.156  87.959  268.265 1.00 166.76 ?  96  TRP C O   1 
ATOM   5140  C CB  . TRP C  1 66  ? 96.129  88.045  268.677 1.00 183.97 ?  96  TRP C CB  1 
ATOM   5141  C CG  . TRP C  1 66  ? 94.735  87.540  268.449 1.00 187.50 ?  96  TRP C CG  1 
ATOM   5142  C CD1 . TRP C  1 66  ? 93.675  87.639  269.304 1.00 188.81 ?  96  TRP C CD1 1 
ATOM   5143  C CD2 . TRP C  1 66  ? 94.259  86.825  267.302 1.00 186.60 ?  96  TRP C CD2 1 
ATOM   5144  N NE1 . TRP C  1 66  ? 92.566  87.042  268.754 1.00 189.44 ?  96  TRP C NE1 1 
ATOM   5145  C CE2 . TRP C  1 66  ? 92.898  86.534  267.526 1.00 186.90 ?  96  TRP C CE2 1 
ATOM   5146  C CE3 . TRP C  1 66  ? 94.849  86.408  266.104 1.00 182.66 ?  96  TRP C CE3 1 
ATOM   5147  C CZ2 . TRP C  1 66  ? 92.121  85.842  266.600 1.00 184.19 ?  96  TRP C CZ2 1 
ATOM   5148  C CZ3 . TRP C  1 66  ? 94.072  85.724  265.183 1.00 183.06 ?  96  TRP C CZ3 1 
ATOM   5149  C CH2 . TRP C  1 66  ? 92.723  85.451  265.436 1.00 184.39 ?  96  TRP C CH2 1 
ATOM   5150  N N   . LYS C  1 67  ? 98.981  87.394  270.439 1.00 182.51 ?  97  LYS C N   1 
ATOM   5151  C CA  . LYS C  1 67  ? 100.317 87.809  270.843 1.00 180.73 ?  97  LYS C CA  1 
ATOM   5152  C C   . LYS C  1 67  ? 101.039 86.655  271.524 1.00 178.56 ?  97  LYS C C   1 
ATOM   5153  O O   . LYS C  1 67  ? 101.775 86.833  272.498 1.00 181.17 ?  97  LYS C O   1 
ATOM   5154  C CB  . LYS C  1 67  ? 100.278 89.060  271.719 1.00 183.27 ?  97  LYS C CB  1 
ATOM   5155  C CG  . LYS C  1 67  ? 99.634  90.237  271.014 1.00 186.48 ?  97  LYS C CG  1 
ATOM   5156  C CD  . LYS C  1 67  ? 100.433 90.489  269.735 1.00 190.04 ?  97  LYS C CD  1 
ATOM   5157  C CE  . LYS C  1 67  ? 99.875  91.607  268.875 1.00 192.90 ?  97  LYS C CE  1 
ATOM   5158  N NZ  . LYS C  1 67  ? 99.183  92.649  269.672 1.00 193.35 1  97  LYS C NZ  1 
ATOM   5159  N N   . ASN C  1 68  ? 100.807 85.447  271.017 1.00 174.97 ?  98  ASN C N   1 
ATOM   5160  C CA  . ASN C  1 68  ? 101.430 84.240  271.536 1.00 171.70 ?  98  ASN C CA  1 
ATOM   5161  C C   . ASN C  1 68  ? 102.588 83.862  270.623 1.00 168.88 ?  98  ASN C C   1 
ATOM   5162  O O   . ASN C  1 68  ? 102.427 83.801  269.398 1.00 168.81 ?  98  ASN C O   1 
ATOM   5163  C CB  . ASN C  1 68  ? 100.418 83.098  271.632 1.00 173.15 ?  98  ASN C CB  1 
ATOM   5164  C CG  . ASN C  1 68  ? 101.030 81.819  272.160 1.00 171.82 ?  98  ASN C CG  1 
ATOM   5165  O OD1 . ASN C  1 68  ? 101.183 80.846  271.425 1.00 171.22 ?  98  ASN C OD1 1 
ATOM   5166  N ND2 . ASN C  1 68  ? 101.386 81.815  273.440 1.00 171.46 ?  98  ASN C ND2 1 
ATOM   5167  N N   . ASN C  1 69  ? 103.752 83.625  271.218 1.00 170.88 ?  99  ASN C N   1 
ATOM   5168  C CA  . ASN C  1 69  ? 104.960 83.379  270.447 1.00 163.81 ?  99  ASN C CA  1 
ATOM   5169  C C   . ASN C  1 69  ? 105.108 81.929  270.015 1.00 159.07 ?  99  ASN C C   1 
ATOM   5170  O O   . ASN C  1 69  ? 105.958 81.632  269.169 1.00 158.96 ?  99  ASN C O   1 
ATOM   5171  C CB  . ASN C  1 69  ? 106.178 83.797  271.252 1.00 168.56 ?  99  ASN C CB  1 
ATOM   5172  C CG  . ASN C  1 69  ? 107.432 83.850  270.419 1.00 164.44 ?  99  ASN C CG  1 
ATOM   5173  O OD1 . ASN C  1 69  ? 108.264 82.948  270.472 1.00 159.46 ?  99  ASN C OD1 1 
ATOM   5174  N ND2 . ASN C  1 69  ? 107.581 84.919  269.643 1.00 165.63 ?  99  ASN C ND2 1 
ATOM   5175  N N   . MET C  1 70  ? 104.305 81.024  270.573 1.00 163.42 ?  100 MET C N   1 
ATOM   5176  C CA  . MET C  1 70  ? 104.392 79.625  270.175 1.00 160.48 ?  100 MET C CA  1 
ATOM   5177  C C   . MET C  1 70  ? 104.028 79.468  268.708 1.00 164.59 ?  100 MET C C   1 
ATOM   5178  O O   . MET C  1 70  ? 104.510 78.549  268.036 1.00 160.81 ?  100 MET C O   1 
ATOM   5179  C CB  . MET C  1 70  ? 103.465 78.793  271.055 1.00 159.01 ?  100 MET C CB  1 
ATOM   5180  C CG  . MET C  1 70  ? 103.714 78.979  272.540 1.00 159.07 ?  100 MET C CG  1 
ATOM   5181  S SD  . MET C  1 70  ? 102.611 77.981  273.553 1.00 160.71 ?  100 MET C SD  1 
ATOM   5182  C CE  . MET C  1 70  ? 103.126 76.331  273.101 1.00 156.46 ?  100 MET C CE  1 
ATOM   5183  N N   . VAL C  1 71  ? 103.180 80.364  268.202 1.00 166.74 ?  101 VAL C N   1 
ATOM   5184  C CA  . VAL C  1 71  ? 102.780 80.338  266.799 1.00 167.15 ?  101 VAL C CA  1 
ATOM   5185  C C   . VAL C  1 71  ? 103.945 80.760  265.909 1.00 165.20 ?  101 VAL C C   1 
ATOM   5186  O O   . VAL C  1 71  ? 104.266 80.097  264.915 1.00 161.72 ?  101 VAL C O   1 
ATOM   5187  C CB  . VAL C  1 71  ? 101.551 81.238  266.579 1.00 172.88 ?  101 VAL C CB  1 
ATOM   5188  C CG1 . VAL C  1 71  ? 101.178 81.277  265.107 1.00 175.10 ?  101 VAL C CG1 1 
ATOM   5189  C CG2 . VAL C  1 71  ? 100.380 80.769  267.433 1.00 173.56 ?  101 VAL C CG2 1 
ATOM   5190  N N   . GLU C  1 72  ? 104.598 81.869  266.264 1.00 163.71 ?  102 GLU C N   1 
ATOM   5191  C CA  . GLU C  1 72  ? 105.713 82.396  265.488 1.00 160.90 ?  102 GLU C CA  1 
ATOM   5192  C C   . GLU C  1 72  ? 106.903 81.445  265.490 1.00 154.02 ?  102 GLU C C   1 
ATOM   5193  O O   . GLU C  1 72  ? 107.727 81.489  264.569 1.00 154.28 ?  102 GLU C O   1 
ATOM   5194  C CB  . GLU C  1 72  ? 106.141 83.736  266.085 1.00 166.48 ?  102 GLU C CB  1 
ATOM   5195  C CG  . GLU C  1 72  ? 105.030 84.782  266.175 1.00 177.08 ?  102 GLU C CG  1 
ATOM   5196  C CD  . GLU C  1 72  ? 104.488 85.236  264.838 1.00 186.81 ?  102 GLU C CD  1 
ATOM   5197  O OE1 . GLU C  1 72  ? 105.232 85.190  263.837 1.00 191.80 ?  102 GLU C OE1 1 
ATOM   5198  O OE2 . GLU C  1 72  ? 103.311 85.658  264.799 1.00 190.54 -1 102 GLU C OE2 1 
ATOM   5199  N N   . GLN C  1 73  ? 106.997 80.581  266.502 1.00 156.27 ?  103 GLN C N   1 
ATOM   5200  C CA  . GLN C  1 73  ? 108.057 79.585  266.574 1.00 152.01 ?  103 GLN C CA  1 
ATOM   5201  C C   . GLN C  1 73  ? 107.726 78.375  265.714 1.00 151.36 ?  103 GLN C C   1 
ATOM   5202  O O   . GLN C  1 73  ? 108.593 77.858  265.001 1.00 154.40 ?  103 GLN C O   1 
ATOM   5203  C CB  . GLN C  1 73  ? 108.262 79.153  268.023 1.00 149.68 ?  103 GLN C CB  1 
ATOM   5204  C CG  . GLN C  1 73  ? 108.880 80.209  268.906 1.00 155.16 ?  103 GLN C CG  1 
ATOM   5205  C CD  . GLN C  1 73  ? 109.159 79.689  270.296 1.00 152.17 ?  103 GLN C CD  1 
ATOM   5206  O OE1 . GLN C  1 73  ? 109.165 78.480  270.527 1.00 155.18 ?  103 GLN C OE1 1 
ATOM   5207  N NE2 . GLN C  1 73  ? 109.362 80.600  271.240 1.00 157.69 ?  103 GLN C NE2 1 
ATOM   5208  N N   . MET C  1 74  ? 106.472 77.923  265.765 1.00 135.81 ?  104 MET C N   1 
ATOM   5209  C CA  . MET C  1 74  ? 106.054 76.782  264.960 1.00 135.82 ?  104 MET C CA  1 
ATOM   5210  C C   . MET C  1 74  ? 106.144 77.100  263.476 1.00 136.02 ?  104 MET C C   1 
ATOM   5211  O O   . MET C  1 74  ? 106.548 76.251  262.674 1.00 135.64 ?  104 MET C O   1 
ATOM   5212  C CB  . MET C  1 74  ? 104.634 76.367  265.332 1.00 136.52 ?  104 MET C CB  1 
ATOM   5213  C CG  . MET C  1 74  ? 104.096 75.240  264.485 1.00 136.62 ?  104 MET C CG  1 
ATOM   5214  S SD  . MET C  1 74  ? 102.431 74.772  264.962 1.00 137.62 ?  104 MET C SD  1 
ATOM   5215  C CE  . MET C  1 74  ? 102.249 73.262  264.021 1.00 137.42 ?  104 MET C CE  1 
ATOM   5216  N N   . HIS C  1 75  ? 105.753 78.316  263.088 1.00 142.54 ?  105 HIS C N   1 
ATOM   5217  C CA  . HIS C  1 75  ? 105.797 78.683  261.679 1.00 145.20 ?  105 HIS C CA  1 
ATOM   5218  C C   . HIS C  1 75  ? 107.225 78.620  261.150 1.00 143.61 ?  105 HIS C C   1 
ATOM   5219  O O   . HIS C  1 75  ? 107.466 78.084  260.063 1.00 144.18 ?  105 HIS C O   1 
ATOM   5220  C CB  . HIS C  1 75  ? 105.215 80.083  261.499 1.00 151.92 ?  105 HIS C CB  1 
ATOM   5221  C CG  . HIS C  1 75  ? 105.094 80.512  260.072 1.00 158.30 ?  105 HIS C CG  1 
ATOM   5222  N ND1 . HIS C  1 75  ? 104.373 79.801  259.138 1.00 162.29 ?  105 HIS C ND1 1 
ATOM   5223  C CD2 . HIS C  1 75  ? 105.611 81.578  259.416 1.00 165.86 ?  105 HIS C CD2 1 
ATOM   5224  C CE1 . HIS C  1 75  ? 104.444 80.414  257.970 1.00 169.19 ?  105 HIS C CE1 1 
ATOM   5225  N NE2 . HIS C  1 75  ? 105.190 81.495  258.111 1.00 171.14 ?  105 HIS C NE2 1 
ATOM   5226  N N   . THR C  1 76  ? 108.186 79.155  261.908 1.00 149.62 ?  106 THR C N   1 
ATOM   5227  C CA  . THR C  1 76  ? 109.585 79.110  261.498 1.00 147.90 ?  106 THR C CA  1 
ATOM   5228  C C   . THR C  1 76  ? 110.161 77.701  261.589 1.00 142.66 ?  106 THR C C   1 
ATOM   5229  O O   . THR C  1 76  ? 111.194 77.423  260.969 1.00 144.24 ?  106 THR C O   1 
ATOM   5230  C CB  . THR C  1 76  ? 110.422 80.055  262.357 1.00 151.03 ?  106 THR C CB  1 
ATOM   5231  O OG1 . THR C  1 76  ? 110.175 79.774  263.739 1.00 158.84 ?  106 THR C OG1 1 
ATOM   5232  C CG2 . THR C  1 76  ? 110.051 81.506  262.079 1.00 155.97 ?  106 THR C CG2 1 
ATOM   5233  N N   . ASP C  1 77  ? 109.514 76.812  262.348 1.00 147.96 ?  107 ASP C N   1 
ATOM   5234  C CA  . ASP C  1 77  ? 109.964 75.428  262.476 1.00 145.39 ?  107 ASP C CA  1 
ATOM   5235  C C   . ASP C  1 77  ? 109.547 74.610  261.262 1.00 143.41 ?  107 ASP C C   1 
ATOM   5236  O O   . ASP C  1 77  ? 110.348 73.846  260.710 1.00 143.83 ?  107 ASP C O   1 
ATOM   5237  C CB  . ASP C  1 77  ? 109.418 74.820  263.771 1.00 155.93 ?  107 ASP C CB  1 
ATOM   5238  C CG  . ASP C  1 77  ? 110.215 75.249  264.995 1.00 161.13 ?  107 ASP C CG  1 
ATOM   5239  O OD1 . ASP C  1 77  ? 110.927 76.271  264.898 1.00 163.00 ?  107 ASP C OD1 1 
ATOM   5240  O OD2 . ASP C  1 77  ? 110.117 74.590  266.055 1.00 165.22 -1 107 ASP C OD2 1 
ATOM   5241  N N   . ILE C  1 78  ? 108.289 74.745  260.846 1.00 152.48 ?  108 ILE C N   1 
ATOM   5242  C CA  . ILE C  1 78  ? 107.810 74.001  259.689 1.00 152.80 ?  108 ILE C CA  1 
ATOM   5243  C C   . ILE C  1 78  ? 108.542 74.470  258.438 1.00 151.92 ?  108 ILE C C   1 
ATOM   5244  O O   . ILE C  1 78  ? 108.830 73.677  257.532 1.00 152.23 ?  108 ILE C O   1 
ATOM   5245  C CB  . ILE C  1 78  ? 106.284 74.156  259.545 1.00 152.84 ?  108 ILE C CB  1 
ATOM   5246  C CG1 . ILE C  1 78  ? 105.576 73.851  260.867 1.00 151.61 ?  108 ILE C CG1 1 
ATOM   5247  C CG2 . ILE C  1 78  ? 105.756 73.256  258.446 1.00 147.63 ?  108 ILE C CG2 1 
ATOM   5248  C CD1 . ILE C  1 78  ? 105.800 72.446  261.374 1.00 148.37 ?  108 ILE C CD1 1 
ATOM   5249  N N   . ILE C  1 79  ? 108.849 75.768  258.367 1.00 142.74 ?  109 ILE C N   1 
ATOM   5250  C CA  . ILE C  1 79  ? 109.574 76.300  257.219 1.00 144.29 ?  109 ILE C CA  1 
ATOM   5251  C C   . ILE C  1 79  ? 110.991 75.734  257.144 1.00 142.96 ?  109 ILE C C   1 
ATOM   5252  O O   . ILE C  1 79  ? 111.405 75.218  256.101 1.00 148.86 ?  109 ILE C O   1 
ATOM   5253  C CB  . ILE C  1 79  ? 109.603 77.840  257.287 1.00 147.80 ?  109 ILE C CB  1 
ATOM   5254  C CG1 . ILE C  1 79  ? 108.219 78.447  257.048 1.00 160.36 ?  109 ILE C CG1 1 
ATOM   5255  C CG2 . ILE C  1 79  ? 110.603 78.406  256.293 1.00 154.44 ?  109 ILE C CG2 1 
ATOM   5256  C CD1 . ILE C  1 79  ? 108.224 79.969  257.080 1.00 167.10 ?  109 ILE C CD1 1 
ATOM   5257  N N   . SER C  1 80  ? 111.740 75.760  258.251 1.00 147.22 ?  110 SER C N   1 
ATOM   5258  C CA  . SER C  1 80  ? 113.092 75.203  258.191 1.00 146.78 ?  110 SER C CA  1 
ATOM   5259  C C   . SER C  1 80  ? 113.099 73.697  257.971 1.00 145.05 ?  110 SER C C   1 
ATOM   5260  O O   . SER C  1 80  ? 114.032 73.165  257.358 1.00 144.80 ?  110 SER C O   1 
ATOM   5261  C CB  . SER C  1 80  ? 113.859 75.554  259.461 1.00 147.29 ?  110 SER C CB  1 
ATOM   5262  O OG  . SER C  1 80  ? 113.233 74.982  260.592 1.00 146.28 ?  110 SER C OG  1 
ATOM   5263  N N   . LEU C  1 81  ? 112.077 72.998  258.459 1.00 151.35 ?  111 LEU C N   1 
ATOM   5264  C CA  . LEU C  1 81  ? 111.980 71.565  258.227 1.00 150.84 ?  111 LEU C CA  1 
ATOM   5265  C C   . LEU C  1 81  ? 111.807 71.310  256.739 1.00 150.48 ?  111 LEU C C   1 
ATOM   5266  O O   . LEU C  1 81  ? 112.390 70.378  256.170 1.00 148.04 ?  111 LEU C O   1 
ATOM   5267  C CB  . LEU C  1 81  ? 110.825 71.026  259.049 1.00 153.36 ?  111 LEU C CB  1 
ATOM   5268  C CG  . LEU C  1 81  ? 110.958 69.646  259.645 1.00 160.26 ?  111 LEU C CG  1 
ATOM   5269  C CD1 . LEU C  1 81  ? 109.699 69.524  260.444 1.00 162.52 ?  111 LEU C CD1 1 
ATOM   5270  C CD2 . LEU C  1 81  ? 111.108 68.547  258.597 1.00 159.20 ?  111 LEU C CD2 1 
ATOM   5271  N N   . TRP C  1 82  ? 111.009 72.161  256.099 1.00 159.81 ?  112 TRP C N   1 
ATOM   5272  C CA  . TRP C  1 82  ? 110.743 72.056  254.674 1.00 157.78 ?  112 TRP C CA  1 
ATOM   5273  C C   . TRP C  1 82  ? 111.998 72.297  253.849 1.00 159.08 ?  112 TRP C C   1 
ATOM   5274  O O   . TRP C  1 82  ? 112.200 71.634  252.828 1.00 161.13 ?  112 TRP C O   1 
ATOM   5275  C CB  . TRP C  1 82  ? 109.679 73.086  254.281 1.00 161.50 ?  112 TRP C CB  1 
ATOM   5276  C CG  . TRP C  1 82  ? 108.955 72.885  252.965 1.00 164.97 ?  112 TRP C CG  1 
ATOM   5277  C CD1 . TRP C  1 82  ? 109.212 73.562  251.802 1.00 166.72 ?  112 TRP C CD1 1 
ATOM   5278  C CD2 . TRP C  1 82  ? 107.841 72.029  252.685 1.00 165.17 ?  112 TRP C CD2 1 
ATOM   5279  N NE1 . TRP C  1 82  ? 108.352 73.161  250.814 1.00 165.75 ?  112 TRP C NE1 1 
ATOM   5280  C CE2 . TRP C  1 82  ? 107.499 72.221  251.327 1.00 166.63 ?  112 TRP C CE2 1 
ATOM   5281  C CE3 . TRP C  1 82  ? 107.109 71.109  253.439 1.00 161.54 ?  112 TRP C CE3 1 
ATOM   5282  C CZ2 . TRP C  1 82  ? 106.461 71.528  250.713 1.00 165.37 ?  112 TRP C CZ2 1 
ATOM   5283  C CZ3 . TRP C  1 82  ? 106.079 70.423  252.825 1.00 161.29 ?  112 TRP C CZ3 1 
ATOM   5284  C CH2 . TRP C  1 82  ? 105.765 70.636  251.478 1.00 163.48 ?  112 TRP C CH2 1 
ATOM   5285  N N   . ASP C  1 83  ? 112.850 73.250  254.253 1.00 154.66 ?  113 ASP C N   1 
ATOM   5286  C CA  . ASP C  1 83  ? 114.015 73.545  253.417 1.00 157.43 ?  113 ASP C CA  1 
ATOM   5287  C C   . ASP C  1 83  ? 115.095 72.470  253.507 1.00 155.17 ?  113 ASP C C   1 
ATOM   5288  O O   . ASP C  1 83  ? 115.662 72.077  252.482 1.00 156.95 ?  113 ASP C O   1 
ATOM   5289  C CB  . ASP C  1 83  ? 114.582 74.897  253.838 1.00 162.04 ?  113 ASP C CB  1 
ATOM   5290  C CG  . ASP C  1 83  ? 113.592 76.034  253.643 1.00 168.67 ?  113 ASP C CG  1 
ATOM   5291  O OD1 . ASP C  1 83  ? 112.371 75.775  253.672 1.00 172.26 ?  113 ASP C OD1 1 
ATOM   5292  O OD2 . ASP C  1 83  ? 114.030 77.202  253.564 1.00 177.36 -1 113 ASP C OD2 1 
ATOM   5293  N N   . GLN C  1 84  ? 115.405 71.982  254.706 1.00 151.68 ?  114 GLN C N   1 
ATOM   5294  C CA  . GLN C  1 84  ? 116.412 70.925  254.829 1.00 148.88 ?  114 GLN C CA  1 
ATOM   5295  C C   . GLN C  1 84  ? 115.917 69.616  254.237 1.00 147.67 ?  114 GLN C C   1 
ATOM   5296  O O   . GLN C  1 84  ? 116.736 68.765  253.887 1.00 147.22 ?  114 GLN C O   1 
ATOM   5297  C CB  . GLN C  1 84  ? 117.078 70.762  256.197 1.00 158.52 ?  114 GLN C CB  1 
ATOM   5298  C CG  . GLN C  1 84  ? 116.419 71.062  257.466 1.00 165.44 ?  114 GLN C CG  1 
ATOM   5299  C CD  . GLN C  1 84  ? 117.504 71.453  258.469 1.00 177.37 ?  114 GLN C CD  1 
ATOM   5300  O OE1 . GLN C  1 84  ? 118.062 70.596  259.155 1.00 184.37 ?  114 GLN C OE1 1 
ATOM   5301  N NE2 . GLN C  1 84  ? 117.885 72.721  258.469 1.00 182.00 ?  114 GLN C NE2 1 
ATOM   5302  N N   . SER C  1 85  ? 114.603 69.414  254.161 1.00 154.30 ?  115 SER C N   1 
ATOM   5303  C CA  . SER C  1 85  ? 114.062 68.156  253.663 1.00 150.63 ?  115 SER C CA  1 
ATOM   5304  C C   . SER C  1 85  ? 114.177 68.080  252.151 1.00 154.76 ?  115 SER C C   1 
ATOM   5305  O O   . SER C  1 85  ? 113.960 67.007  251.575 1.00 152.35 ?  115 SER C O   1 
ATOM   5306  C CB  . SER C  1 85  ? 112.593 67.994  254.090 1.00 151.00 ?  115 SER C CB  1 
ATOM   5307  O OG  . SER C  1 85  ? 112.022 66.789  253.598 1.00 149.09 ?  115 SER C OG  1 
ATOM   5308  N N   . LEU C  1 86  ? 114.507 69.201  251.511 1.00 143.48 ?  116 LEU C N   1 
ATOM   5309  C CA  . LEU C  1 86  ? 114.665 69.313  250.072 1.00 146.76 ?  116 LEU C CA  1 
ATOM   5310  C C   . LEU C  1 86  ? 116.135 69.487  249.693 1.00 154.15 ?  116 LEU C C   1 
ATOM   5311  O O   . LEU C  1 86  ? 116.457 69.534  248.501 1.00 159.57 ?  116 LEU C O   1 
ATOM   5312  C CB  . LEU C  1 86  ? 113.830 70.476  249.529 1.00 146.46 ?  116 LEU C CB  1 
ATOM   5313  C CG  . LEU C  1 86  ? 112.323 70.269  249.665 1.00 143.07 ?  116 LEU C CG  1 
ATOM   5314  C CD1 . LEU C  1 86  ? 111.575 71.425  249.023 1.00 146.22 ?  116 LEU C CD1 1 
ATOM   5315  C CD2 . LEU C  1 86  ? 111.930 68.928  249.038 1.00 140.64 ?  116 LEU C CD2 1 
ATOM   5316  N N   . LYS C  1 87  ? 117.048 69.566  250.677 1.00 144.85 ?  117 LYS C N   1 
ATOM   5317  C CA  . LYS C  1 87  ? 118.464 69.699  250.330 1.00 148.67 ?  117 LYS C CA  1 
ATOM   5318  C C   . LYS C  1 87  ? 119.003 68.425  249.698 1.00 143.71 ?  117 LYS C C   1 
ATOM   5319  O O   . LYS C  1 87  ? 119.637 68.515  248.633 1.00 145.74 ?  117 LYS C O   1 
ATOM   5320  C CB  . LYS C  1 87  ? 119.303 70.140  251.534 1.00 151.20 ?  117 LYS C CB  1 
ATOM   5321  C CG  . LYS C  1 87  ? 120.795 70.174  251.163 1.00 153.88 ?  117 LYS C CG  1 
ATOM   5322  C CD  . LYS C  1 87  ? 121.717 70.590  252.298 1.00 160.21 ?  117 LYS C CD  1 
ATOM   5323  C CE  . LYS C  1 87  ? 121.506 72.040  252.700 1.00 162.92 ?  117 LYS C CE  1 
ATOM   5324  N NZ  . LYS C  1 87  ? 121.841 72.960  251.568 1.00 164.53 1  117 LYS C NZ  1 
ATOM   5325  N N   . PRO C  1 88  ? 118.788 67.233  250.252 1.00 154.82 ?  118 PRO C N   1 
ATOM   5326  C CA  . PRO C  1 88  ? 119.318 66.028  249.605 1.00 149.57 ?  118 PRO C CA  1 
ATOM   5327  C C   . PRO C  1 88  ? 118.406 65.467  248.526 1.00 151.37 ?  118 PRO C C   1 
ATOM   5328  O O   . PRO C  1 88  ? 118.593 64.320  248.104 1.00 149.75 ?  118 PRO C O   1 
ATOM   5329  C CB  . PRO C  1 88  ? 119.432 65.054  250.786 1.00 143.92 ?  118 PRO C CB  1 
ATOM   5330  C CG  . PRO C  1 88  ? 118.288 65.424  251.671 1.00 141.61 ?  118 PRO C CG  1 
ATOM   5331  C CD  . PRO C  1 88  ? 118.137 66.917  251.541 1.00 149.78 ?  118 PRO C CD  1 
ATOM   5332  N N   . CYS C  1 89  ? 117.432 66.258  248.090 1.00 155.17 ?  119 CYS C N   1 
ATOM   5333  C CA  . CYS C  1 89  ? 116.507 65.824  247.065 1.00 153.66 ?  119 CYS C CA  1 
ATOM   5334  C C   . CYS C  1 89  ? 117.066 66.205  245.698 1.00 153.89 ?  119 CYS C C   1 
ATOM   5335  O O   . CYS C  1 89  ? 117.985 67.022  245.579 1.00 154.99 ?  119 CYS C O   1 
ATOM   5336  C CB  . CYS C  1 89  ? 115.116 66.424  247.282 1.00 154.00 ?  119 CYS C CB  1 
ATOM   5337  S SG  . CYS C  1 89  ? 114.190 65.579  248.590 1.00 162.42 ?  119 CYS C SG  1 
ATOM   5338  N N   . VAL C  1 90  ? 116.498 65.601  244.657 1.00 157.15 ?  120 VAL C N   1 
ATOM   5339  C CA  . VAL C  1 90  ? 116.966 65.852  243.298 1.00 152.48 ?  120 VAL C CA  1 
ATOM   5340  C C   . VAL C  1 90  ? 116.534 67.240  242.833 1.00 158.67 ?  120 VAL C C   1 
ATOM   5341  O O   . VAL C  1 90  ? 115.342 67.573  242.854 1.00 160.94 ?  120 VAL C O   1 
ATOM   5342  C CB  . VAL C  1 90  ? 116.465 64.766  242.339 1.00 137.86 ?  120 VAL C CB  1 
ATOM   5343  C CG1 . VAL C  1 90  ? 116.740 65.175  240.904 1.00 137.34 ?  120 VAL C CG1 1 
ATOM   5344  C CG2 . VAL C  1 90  ? 117.125 63.425  242.661 1.00 126.52 ?  120 VAL C CG2 1 
ATOM   5345  N N   . LYS C  1 91  ? 117.507 68.055  242.418 1.00 155.52 ?  121 LYS C N   1 
ATOM   5346  C CA  . LYS C  1 91  ? 117.254 69.393  241.891 1.00 153.16 ?  121 LYS C CA  1 
ATOM   5347  C C   . LYS C  1 91  ? 117.015 69.297  240.388 1.00 149.61 ?  121 LYS C C   1 
ATOM   5348  O O   . LYS C  1 91  ? 117.826 68.718  239.656 1.00 145.15 ?  121 LYS C O   1 
ATOM   5349  C CB  . LYS C  1 91  ? 118.398 70.348  242.236 1.00 152.49 ?  121 LYS C CB  1 
ATOM   5350  C CG  . LYS C  1 91  ? 119.777 69.743  242.180 1.00 156.00 ?  121 LYS C CG  1 
ATOM   5351  C CD  . LYS C  1 91  ? 120.756 70.657  242.903 1.00 152.31 ?  121 LYS C CD  1 
ATOM   5352  C CE  . LYS C  1 91  ? 122.132 70.028  243.030 1.00 156.12 ?  121 LYS C CE  1 
ATOM   5353  N NZ  . LYS C  1 91  ? 123.063 70.887  243.820 1.00 155.84 1  121 LYS C NZ  1 
ATOM   5354  N N   . LEU C  1 92  ? 115.899 69.868  239.938 1.00 142.11 ?  122 LEU C N   1 
ATOM   5355  C CA  . LEU C  1 92  ? 115.464 69.820  238.540 1.00 142.25 ?  122 LEU C CA  1 
ATOM   5356  C C   . LEU C  1 92  ? 115.885 71.032  237.706 1.00 143.41 ?  122 LEU C C   1 
ATOM   5357  O O   . LEU C  1 92  ? 115.101 71.533  236.893 1.00 143.73 ?  122 LEU C O   1 
ATOM   5358  C CB  . LEU C  1 92  ? 113.948 69.666  238.535 1.00 141.70 ?  122 LEU C CB  1 
ATOM   5359  C CG  . LEU C  1 92  ? 113.295 68.476  239.247 1.00 140.70 ?  122 LEU C CG  1 
ATOM   5360  C CD1 . LEU C  1 92  ? 111.775 68.489  239.026 1.00 140.42 ?  122 LEU C CD1 1 
ATOM   5361  C CD2 . LEU C  1 92  ? 113.916 67.160  238.788 1.00 140.21 ?  122 LEU C CD2 1 
ATOM   5362  N N   . THR C  1 93  ? 117.119 71.510  237.849 1.00 162.10 ?  123 THR C N   1 
ATOM   5363  C CA  . THR C  1 93  ? 117.584 72.636  237.038 1.00 160.18 ?  123 THR C CA  1 
ATOM   5364  C C   . THR C  1 93  ? 117.503 72.482  235.512 1.00 159.12 ?  123 THR C C   1 
ATOM   5365  O O   . THR C  1 93  ? 117.073 73.450  234.859 1.00 153.84 ?  123 THR C O   1 
ATOM   5366  C CB  . THR C  1 93  ? 118.994 73.071  237.470 1.00 152.80 ?  123 THR C CB  1 
ATOM   5367  O OG1 . THR C  1 93  ? 119.521 73.987  236.507 1.00 159.37 ?  123 THR C OG1 1 
ATOM   5368  C CG2 . THR C  1 93  ? 119.938 71.916  237.659 1.00 155.23 ?  123 THR C CG2 1 
ATOM   5369  N N   . PRO C  1 94  ? 117.863 71.332  234.867 1.00 166.32 ?  124 PRO C N   1 
ATOM   5370  C CA  . PRO C  1 94  ? 117.789 71.307  233.397 1.00 158.76 ?  124 PRO C CA  1 
ATOM   5371  C C   . PRO C  1 94  ? 116.488 70.828  232.768 1.00 158.25 ?  124 PRO C C   1 
ATOM   5372  O O   . PRO C  1 94  ? 116.489 70.065  231.795 1.00 161.72 ?  124 PRO C O   1 
ATOM   5373  C CB  . PRO C  1 94  ? 118.942 70.366  233.019 1.00 159.97 ?  124 PRO C CB  1 
ATOM   5374  C CG  . PRO C  1 94  ? 119.158 69.488  234.239 1.00 159.69 ?  124 PRO C CG  1 
ATOM   5375  C CD  . PRO C  1 94  ? 118.368 70.053  235.391 1.00 168.19 ?  124 PRO C CD  1 
ATOM   5376  N N   . LEU C  1 95  ? 115.365 71.298  233.301 1.00 141.84 ?  125 LEU C N   1 
ATOM   5377  C CA  . LEU C  1 95  ? 114.056 71.003  232.737 1.00 141.26 ?  125 LEU C CA  1 
ATOM   5378  C C   . LEU C  1 95  ? 113.428 72.255  232.162 1.00 142.36 ?  125 LEU C C   1 
ATOM   5379  O O   . LEU C  1 95  ? 112.265 72.218  231.757 1.00 142.10 ?  125 LEU C O   1 
ATOM   5380  C CB  . LEU C  1 95  ? 113.067 70.330  233.680 1.00 140.14 ?  125 LEU C CB  1 
ATOM   5381  C CG  . LEU C  1 95  ? 113.393 69.248  234.679 1.00 139.18 ?  125 LEU C CG  1 
ATOM   5382  C CD1 . LEU C  1 95  ? 112.280 69.281  235.630 1.00 138.72 ?  125 LEU C CD1 1 
ATOM   5383  C CD2 . LEU C  1 95  ? 113.419 67.924  234.020 1.00 138.36 ?  125 LEU C CD2 1 
ATOM   5384  N N   . CYS C  1 96  ? 114.162 73.369  232.123 1.00 151.85 ?  126 CYS C N   1 
ATOM   5385  C CA  . CYS C  1 96  ? 113.612 74.614  231.603 1.00 154.09 ?  126 CYS C CA  1 
ATOM   5386  C C   . CYS C  1 96  ? 113.828 74.717  230.109 1.00 153.89 ?  126 CYS C C   1 
ATOM   5387  O O   . CYS C  1 96  ? 113.901 75.815  229.548 1.00 158.86 ?  126 CYS C O   1 
ATOM   5388  C CB  . CYS C  1 96  ? 114.239 75.829  232.309 1.00 161.05 ?  126 CYS C CB  1 
ATOM   5389  S SG  . CYS C  1 96  ? 113.890 76.047  234.093 1.00 158.92 ?  126 CYS C SG  1 
ATOM   5390  N N   . VAL C  1 97  ? 113.938 73.556  229.465 1.00 163.13 ?  127 VAL C N   1 
ATOM   5391  C CA  . VAL C  1 97  ? 114.091 73.445  228.032 1.00 167.53 ?  127 VAL C CA  1 
ATOM   5392  C C   . VAL C  1 97  ? 112.761 73.774  227.356 1.00 170.01 ?  127 VAL C C   1 
ATOM   5393  O O   . VAL C  1 97  ? 111.686 73.689  227.960 1.00 168.01 ?  127 VAL C O   1 
ATOM   5394  C CB  . VAL C  1 97  ? 114.572 72.023  227.691 1.00 164.09 ?  127 VAL C CB  1 
ATOM   5395  C CG1 . VAL C  1 97  ? 115.118 71.940  226.286 1.00 166.21 ?  127 VAL C CG1 1 
ATOM   5396  C CG2 . VAL C  1 97  ? 115.621 71.555  228.712 1.00 158.22 ?  127 VAL C CG2 1 
ATOM   5397  N N   . THR C  1 98  ? 112.837 74.194  226.096 1.00 176.66 ?  128 THR C N   1 
ATOM   5398  C CA  . THR C  1 98  ? 111.627 74.483  225.333 1.00 175.76 ?  128 THR C CA  1 
ATOM   5399  C C   . THR C  1 98  ? 110.733 73.246  225.240 1.00 171.21 ?  128 THR C C   1 
ATOM   5400  O O   . THR C  1 98  ? 111.189 72.158  224.877 1.00 169.42 ?  128 THR C O   1 
ATOM   5401  C CB  . THR C  1 98  ? 112.001 74.993  223.943 1.00 182.87 ?  128 THR C CB  1 
ATOM   5402  O OG1 . THR C  1 98  ? 112.794 74.007  223.271 1.00 185.44 ?  128 THR C OG1 1 
ATOM   5403  C CG2 . THR C  1 98  ? 112.780 76.306  224.051 1.00 187.35 ?  128 THR C CG2 1 
ATOM   5404  N N   . LEU C  1 99  ? 109.459 73.418  225.591 1.00 156.99 ?  129 LEU C N   1 
ATOM   5405  C CA  . LEU C  1 99  ? 108.477 72.337  225.634 1.00 161.06 ?  129 LEU C CA  1 
ATOM   5406  C C   . LEU C  1 99  ? 107.523 72.431  224.445 1.00 161.13 ?  129 LEU C C   1 
ATOM   5407  O O   . LEU C  1 99  ? 106.777 73.407  224.322 1.00 161.25 ?  129 LEU C O   1 
ATOM   5408  C CB  . LEU C  1 99  ? 107.699 72.403  226.947 1.00 167.19 ?  129 LEU C CB  1 
ATOM   5409  C CG  . LEU C  1 99  ? 108.593 72.520  228.182 1.00 167.27 ?  129 LEU C CG  1 
ATOM   5410  C CD1 . LEU C  1 99  ? 107.767 72.606  229.452 1.00 171.67 ?  129 LEU C CD1 1 
ATOM   5411  C CD2 . LEU C  1 99  ? 109.553 71.348  228.244 1.00 166.87 ?  129 LEU C CD2 1 
ATOM   5412  N N   . GLN C  1 100 ? 107.544 71.415  223.580 1.00 166.74 ?  130 GLN C N   1 
ATOM   5413  C CA  . GLN C  1 100 ? 106.619 71.302  222.446 1.00 166.29 ?  130 GLN C CA  1 
ATOM   5414  C C   . GLN C  1 100 ? 105.373 70.552  222.907 1.00 171.33 ?  130 GLN C C   1 
ATOM   5415  O O   . GLN C  1 100 ? 105.287 69.329  222.785 1.00 169.89 ?  130 GLN C O   1 
ATOM   5416  C CB  . GLN C  1 100 ? 107.296 70.595  221.277 1.00 162.42 ?  130 GLN C CB  1 
ATOM   5417  C CG  . GLN C  1 100 ? 108.587 71.246  220.807 1.00 161.47 ?  130 GLN C CG  1 
ATOM   5418  C CD  . GLN C  1 100 ? 108.341 72.585  220.157 1.00 165.64 ?  130 GLN C CD  1 
ATOM   5419  O OE1 . GLN C  1 100 ? 107.299 72.798  219.537 1.00 170.03 ?  130 GLN C OE1 1 
ATOM   5420  N NE2 . GLN C  1 100 ? 109.292 73.500  220.299 1.00 167.54 ?  130 GLN C NE2 1 
ATOM   5421  N N   . CYS C  1 101 ? 104.399 71.278  223.464 1.00 161.44 ?  131 CYS C N   1 
ATOM   5422  C CA  . CYS C  1 101 ? 103.240 70.639  224.075 1.00 160.50 ?  131 CYS C CA  1 
ATOM   5423  C C   . CYS C  1 101 ? 102.042 70.610  223.128 1.00 160.64 ?  131 CYS C C   1 
ATOM   5424  O O   . CYS C  1 101 ? 101.988 71.328  222.126 1.00 161.73 ?  131 CYS C O   1 
ATOM   5425  C CB  . CYS C  1 101 ? 102.820 71.347  225.366 1.00 161.15 ?  131 CYS C CB  1 
ATOM   5426  S SG  . CYS C  1 101 ? 104.202 71.379  226.497 1.00 160.96 ?  131 CYS C SG  1 
ATOM   5427  N N   . THR C  1 102 ? 101.078 69.750  223.463 1.00 170.41 ?  132 THR C N   1 
ATOM   5428  C CA  . THR C  1 102 ? 99.832  69.632  222.719 1.00 172.38 ?  132 THR C CA  1 
ATOM   5429  C C   . THR C  1 102 ? 98.741  69.192  223.687 1.00 172.24 ?  132 THR C C   1 
ATOM   5430  O O   . THR C  1 102 ? 99.015  68.839  224.836 1.00 171.92 ?  132 THR C O   1 
ATOM   5431  C CB  . THR C  1 102 ? 99.943  68.630  221.567 1.00 172.50 ?  132 THR C CB  1 
ATOM   5432  O OG1 . THR C  1 102 ? 98.666  68.506  220.931 1.00 176.35 ?  132 THR C OG1 1 
ATOM   5433  C CG2 . THR C  1 102 ? 100.374 67.262  222.087 1.00 156.58 ?  132 THR C CG2 1 
ATOM   5434  N N   . ASN C  1 103 ? 97.494  69.218  223.214 1.00 200.26 ?  133 ASN C N   1 
ATOM   5435  C CA  . ASN C  1 103 ? 96.377  68.796  224.052 1.00 198.11 ?  133 ASN C CA  1 
ATOM   5436  C C   . ASN C  1 103 ? 96.451  67.314  224.380 1.00 195.88 ?  133 ASN C C   1 
ATOM   5437  O O   . ASN C  1 103 ? 96.986  66.505  223.618 1.00 194.99 ?  133 ASN C O   1 
ATOM   5438  C CB  . ASN C  1 103 ? 95.018  69.091  223.417 1.00 202.29 ?  133 ASN C CB  1 
ATOM   5439  C CG  . ASN C  1 103 ? 94.665  70.556  223.448 1.00 203.95 ?  133 ASN C CG  1 
ATOM   5440  O OD1 . ASN C  1 103 ? 95.221  71.325  224.232 1.00 198.57 ?  133 ASN C OD1 1 
ATOM   5441  N ND2 . ASN C  1 103 ? 93.698  70.945  222.634 1.00 221.98 ?  133 ASN C ND2 1 
ATOM   5442  N N   . VAL C  1 104 ? 95.893  66.966  225.537 1.00 194.34 ?  134 VAL C N   1 
ATOM   5443  C CA  . VAL C  1 104 ? 95.837  65.574  225.946 1.00 192.68 ?  134 VAL C CA  1 
ATOM   5444  C C   . VAL C  1 104 ? 94.849  64.825  225.057 1.00 194.75 ?  134 VAL C C   1 
ATOM   5445  O O   . VAL C  1 104 ? 93.920  65.408  224.480 1.00 202.33 ?  134 VAL C O   1 
ATOM   5446  C CB  . VAL C  1 104 ? 95.448  65.471  227.432 1.00 193.47 ?  134 VAL C CB  1 
ATOM   5447  C CG1 . VAL C  1 104 ? 93.986  65.857  227.633 1.00 195.25 ?  134 VAL C CG1 1 
ATOM   5448  C CG2 . VAL C  1 104 ? 95.730  64.074  227.974 1.00 189.45 ?  134 VAL C CG2 1 
ATOM   5449  N N   . THR C  1 105 ? 95.068  63.520  224.928 1.00 211.07 ?  135 THR C N   1 
ATOM   5450  C CA  . THR C  1 105 ? 94.250  62.667  224.074 1.00 205.19 ?  135 THR C CA  1 
ATOM   5451  C C   . THR C  1 105 ? 92.849  62.543  224.656 1.00 209.45 ?  135 THR C C   1 
ATOM   5452  O O   . THR C  1 105 ? 92.638  61.846  225.655 1.00 201.59 ?  135 THR C O   1 
ATOM   5453  C CB  . THR C  1 105 ? 94.891  61.294  223.901 1.00 185.35 ?  135 THR C CB  1 
ATOM   5454  O OG1 . THR C  1 105 ? 95.397  60.830  225.159 1.00 183.63 ?  135 THR C OG1 1 
ATOM   5455  C CG2 . THR C  1 105 ? 96.012  61.355  222.879 1.00 176.06 ?  135 THR C CG2 1 
ATOM   5456  N N   . ASN C  1 106 ? 91.894  63.223  224.032 1.00 218.69 ?  136 ASN C N   1 
ATOM   5457  C CA  . ASN C  1 106 ? 90.493  63.163  224.421 1.00 215.82 ?  136 ASN C CA  1 
ATOM   5458  C C   . ASN C  1 106 ? 89.680  63.558  223.200 1.00 223.23 ?  136 ASN C C   1 
ATOM   5459  O O   . ASN C  1 106 ? 90.223  63.783  222.115 1.00 225.40 ?  136 ASN C O   1 
ATOM   5460  C CB  . ASN C  1 106 ? 90.170  64.083  225.605 1.00 218.21 ?  136 ASN C CB  1 
ATOM   5461  C CG  . ASN C  1 106 ? 90.309  65.562  225.260 1.00 227.69 ?  136 ASN C CG  1 
ATOM   5462  O OD1 . ASN C  1 106 ? 91.077  65.943  224.376 1.00 230.88 ?  136 ASN C OD1 1 
ATOM   5463  N ND2 . ASN C  1 106 ? 89.547  66.401  225.956 1.00 234.01 ?  136 ASN C ND2 1 
ATOM   5464  N N   . ASN C  1 107 ? 88.371  63.659  223.382 1.00 225.19 ?  137 ASN C N   1 
ATOM   5465  C CA  . ASN C  1 107 ? 87.492  64.003  222.277 1.00 231.68 ?  137 ASN C CA  1 
ATOM   5466  C C   . ASN C  1 107 ? 86.724  65.274  222.630 1.00 241.09 ?  137 ASN C C   1 
ATOM   5467  O O   . ASN C  1 107 ? 85.602  65.198  223.137 1.00 247.15 ?  137 ASN C O   1 
ATOM   5468  C CB  . ASN C  1 107 ? 86.547  62.803  221.995 1.00 224.22 ?  137 ASN C CB  1 
ATOM   5469  C CG  . ASN C  1 107 ? 85.416  63.159  221.069 1.00 233.57 ?  137 ASN C CG  1 
ATOM   5470  O OD1 . ASN C  1 107 ? 85.580  63.224  219.852 1.00 238.01 ?  137 ASN C OD1 1 
ATOM   5471  N ND2 . ASN C  1 107 ? 84.252  63.414  221.651 1.00 243.41 ?  137 ASN C ND2 1 
ATOM   5472  N N   . ILE C  1 108 ? 87.311  66.430  222.286 1.00 245.20 ?  138 ILE C N   1 
ATOM   5473  C CA  . ILE C  1 108 ? 86.679  67.758  222.370 1.00 248.74 ?  138 ILE C CA  1 
ATOM   5474  C C   . ILE C  1 108 ? 86.005  67.845  223.809 1.00 245.76 ?  138 ILE C C   1 
ATOM   5475  O O   . ILE C  1 108 ? 86.399  67.047  224.659 1.00 239.88 ?  138 ILE C O   1 
ATOM   5476  C CB  . ILE C  1 108 ? 85.782  67.916  221.080 1.00 246.85 ?  138 ILE C CB  1 
ATOM   5477  C CG1 . ILE C  1 108 ? 86.594  67.532  219.836 1.00 238.43 ?  138 ILE C CG1 1 
ATOM   5478  C CG2 . ILE C  1 108 ? 85.607  69.339  220.645 1.00 247.43 ?  138 ILE C CG2 1 
ATOM   5479  C CD1 . ILE C  1 108 ? 86.454  66.108  219.343 1.00 229.24 ?  138 ILE C CD1 1 
ATOM   5480  N N   . THR C  1 109 ? 85.147  68.795  224.218 1.00 248.77 ?  139 THR C N   1 
ATOM   5481  C CA  . THR C  1 109 ? 84.703  70.005  223.551 1.00 253.77 ?  139 THR C CA  1 
ATOM   5482  C C   . THR C  1 109 ? 85.712  71.144  223.608 1.00 256.42 ?  139 THR C C   1 
ATOM   5483  O O   . THR C  1 109 ? 86.856  70.953  224.029 1.00 257.05 ?  139 THR C O   1 
ATOM   5484  C CB  . THR C  1 109 ? 83.390  70.485  224.175 1.00 259.50 ?  139 THR C CB  1 
ATOM   5485  O OG1 . THR C  1 109 ? 83.584  70.686  225.582 1.00 262.19 ?  139 THR C OG1 1 
ATOM   5486  C CG2 . THR C  1 109 ? 82.306  69.441  223.969 1.00 255.54 ?  139 THR C CG2 1 
ATOM   5487  N N   . ASP C  1 110 ? 85.279  72.332  223.173 1.00 260.43 ?  140 ASP C N   1 
ATOM   5488  C CA  . ASP C  1 110 ? 86.156  73.495  223.193 1.00 259.75 ?  140 ASP C CA  1 
ATOM   5489  C C   . ASP C  1 110 ? 86.211  74.158  224.563 1.00 267.38 ?  140 ASP C C   1 
ATOM   5490  O O   . ASP C  1 110 ? 87.034  75.057  224.767 1.00 270.28 ?  140 ASP C O   1 
ATOM   5491  C CB  . ASP C  1 110 ? 85.723  74.513  222.132 1.00 265.62 ?  140 ASP C CB  1 
ATOM   5492  C CG  . ASP C  1 110 ? 86.900  75.282  221.541 1.00 262.39 ?  140 ASP C CG  1 
ATOM   5493  O OD1 . ASP C  1 110 ? 87.911  75.466  222.248 1.00 258.95 ?  140 ASP C OD1 1 
ATOM   5494  O OD2 . ASP C  1 110 ? 86.820  75.702  220.366 1.00 266.81 -1 140 ASP C OD2 1 
ATOM   5495  N N   . ASP C  1 111 ? 85.373  73.732  225.507 1.00 264.64 ?  141 ASP C N   1 
ATOM   5496  C CA  . ASP C  1 111 ? 85.367  74.302  226.846 1.00 265.02 ?  141 ASP C CA  1 
ATOM   5497  C C   . ASP C  1 111 ? 86.227  73.484  227.789 1.00 253.50 ?  141 ASP C C   1 
ATOM   5498  O O   . ASP C  1 111 ? 86.351  73.826  228.970 1.00 249.43 ?  141 ASP C O   1 
ATOM   5499  C CB  . ASP C  1 111 ? 83.938  74.469  227.371 1.00 272.59 ?  141 ASP C CB  1 
ATOM   5500  C CG  . ASP C  1 111 ? 83.106  75.388  226.489 1.00 279.84 ?  141 ASP C CG  1 
ATOM   5501  O OD1 . ASP C  1 111 ? 83.691  76.303  225.867 1.00 283.01 ?  141 ASP C OD1 1 
ATOM   5502  O OD2 . ASP C  1 111 ? 81.872  75.217  226.435 1.00 276.53 -1 141 ASP C OD2 1 
ATOM   5503  N N   . MET C  1 112 ? 86.822  72.410  227.277 1.00 260.16 ?  150 MET C N   1 
ATOM   5504  C CA  . MET C  1 112 ? 87.686  71.559  228.068 1.00 253.00 ?  150 MET C CA  1 
ATOM   5505  C C   . MET C  1 112 ? 89.029  72.230  228.278 1.00 248.71 ?  150 MET C C   1 
ATOM   5506  O O   . MET C  1 112 ? 89.822  71.750  229.094 1.00 242.54 ?  150 MET C O   1 
ATOM   5507  C CB  . MET C  1 112 ? 87.903  70.212  227.375 1.00 248.55 ?  150 MET C CB  1 
ATOM   5508  C CG  . MET C  1 112 ? 86.658  69.379  227.153 1.00 247.16 ?  150 MET C CG  1 
ATOM   5509  S SD  . MET C  1 112 ? 85.899  68.825  228.686 1.00 247.40 ?  150 MET C SD  1 
ATOM   5510  C CE  . MET C  1 112 ? 87.212  67.796  229.338 1.00 230.73 ?  150 MET C CE  1 
ATOM   5511  N N   . ARG C  1 113 ? 89.283  73.320  227.538 1.00 238.84 ?  151 ARG C N   1 
ATOM   5512  C CA  . ARG C  1 113 ? 90.491  74.140  227.569 1.00 238.38 ?  151 ARG C CA  1 
ATOM   5513  C C   . ARG C  1 113 ? 91.749  73.328  227.826 1.00 226.43 ?  151 ARG C C   1 
ATOM   5514  O O   . ARG C  1 113 ? 92.664  73.805  228.504 1.00 226.82 ?  151 ARG C O   1 
ATOM   5515  C CB  . ARG C  1 113 ? 90.375  75.229  228.645 1.00 238.42 ?  151 ARG C CB  1 
ATOM   5516  C CG  . ARG C  1 113 ? 90.082  74.656  230.025 1.00 233.01 ?  151 ARG C CG  1 
ATOM   5517  C CD  . ARG C  1 113 ? 90.013  75.660  231.139 1.00 238.29 ?  151 ARG C CD  1 
ATOM   5518  N NE  . ARG C  1 113 ? 91.326  76.232  231.403 1.00 234.73 ?  151 ARG C NE  1 
ATOM   5519  C CZ  . ARG C  1 113 ? 91.664  76.817  232.546 1.00 236.77 ?  151 ARG C CZ  1 
ATOM   5520  N NH1 . ARG C  1 113 ? 90.781  76.896  233.531 1.00 240.72 1  151 ARG C NH1 1 
ATOM   5521  N NH2 . ARG C  1 113 ? 92.880  77.324  232.705 1.00 231.20 ?  151 ARG C NH2 1 
ATOM   5522  N N   . GLY C  1 114 ? 91.830  72.127  227.264 1.00 220.42 ?  152 GLY C N   1 
ATOM   5523  C CA  . GLY C  1 114 ? 93.030  71.330  227.408 1.00 209.56 ?  152 GLY C CA  1 
ATOM   5524  C C   . GLY C  1 114 ? 93.319  70.984  228.858 1.00 208.72 ?  152 GLY C C   1 
ATOM   5525  O O   . GLY C  1 114 ? 93.178  69.829  229.270 1.00 204.84 ?  152 GLY C O   1 
ATOM   5526  N N   . GLU C  1 115 ? 93.726  71.992  229.638 1.00 209.79 ?  153 GLU C N   1 
ATOM   5527  C CA  . GLU C  1 115 ? 94.116  71.854  231.040 1.00 201.17 ?  153 GLU C CA  1 
ATOM   5528  C C   . GLU C  1 115 ? 95.343  70.965  231.193 1.00 188.96 ?  153 GLU C C   1 
ATOM   5529  O O   . GLU C  1 115 ? 96.341  71.378  231.792 1.00 184.89 ?  153 GLU C O   1 
ATOM   5530  C CB  . GLU C  1 115 ? 92.977  71.296  231.893 1.00 200.02 ?  153 GLU C CB  1 
ATOM   5531  C CG  . GLU C  1 115 ? 93.377  71.088  233.346 1.00 192.05 ?  153 GLU C CG  1 
ATOM   5532  C CD  . GLU C  1 115 ? 92.220  70.649  234.215 1.00 199.00 ?  153 GLU C CD  1 
ATOM   5533  O OE1 . GLU C  1 115 ? 91.067  70.719  233.743 1.00 207.49 ?  153 GLU C OE1 1 
ATOM   5534  O OE2 . GLU C  1 115 ? 92.465  70.222  235.365 1.00 201.04 -1 153 GLU C OE2 1 
ATOM   5535  N N   . LEU C  1 116 ? 95.270  69.739  230.680 1.00 177.10 ?  154 LEU C N   1 
ATOM   5536  C CA  . LEU C  1 116 ? 96.391  68.812  230.706 1.00 165.84 ?  154 LEU C CA  1 
ATOM   5537  C C   . LEU C  1 116 ? 97.101  68.917  229.362 1.00 169.16 ?  154 LEU C C   1 
ATOM   5538  O O   . LEU C  1 116 ? 96.456  68.843  228.311 1.00 174.71 ?  154 LEU C O   1 
ATOM   5539  C CB  . LEU C  1 116 ? 95.874  67.396  230.956 1.00 158.96 ?  154 LEU C CB  1 
ATOM   5540  C CG  . LEU C  1 116 ? 95.261  67.247  232.351 1.00 159.90 ?  154 LEU C CG  1 
ATOM   5541  C CD1 . LEU C  1 116 ? 94.542  65.919  232.519 1.00 157.63 ?  154 LEU C CD1 1 
ATOM   5542  C CD2 . LEU C  1 116 ? 96.343  67.393  233.388 1.00 159.65 ?  154 LEU C CD2 1 
ATOM   5543  N N   . LYS C  1 117 ? 98.418  69.100  229.389 1.00 159.07 ?  155 LYS C N   1 
ATOM   5544  C CA  . LYS C  1 117 ? 99.213  69.259  228.176 1.00 159.47 ?  155 LYS C CA  1 
ATOM   5545  C C   . LYS C  1 117 ? 100.235 68.135  228.009 1.00 153.70 ?  155 LYS C C   1 
ATOM   5546  O O   . LYS C  1 117 ? 100.915 67.760  228.969 1.00 152.13 ?  155 LYS C O   1 
ATOM   5547  C CB  . LYS C  1 117 ? 99.825  70.653  228.132 1.00 163.19 ?  155 LYS C CB  1 
ATOM   5548  C CG  . LYS C  1 117 ? 98.697  71.609  227.758 1.00 167.92 ?  155 LYS C CG  1 
ATOM   5549  C CD  . LYS C  1 117 ? 98.893  72.379  226.479 1.00 175.00 ?  155 LYS C CD  1 
ATOM   5550  C CE  . LYS C  1 117 ? 97.741  73.361  226.318 1.00 184.38 ?  155 LYS C CE  1 
ATOM   5551  N NZ  . LYS C  1 117 ? 97.828  74.228  225.112 1.00 192.50 1  155 LYS C NZ  1 
ATOM   5552  N N   . ASN C  1 118 ? 100.337 67.604  226.784 1.00 173.28 ?  156 ASN C N   1 
ATOM   5553  C CA  . ASN C  1 118 ? 101.293 66.548  226.419 1.00 168.46 ?  156 ASN C CA  1 
ATOM   5554  C C   . ASN C  1 118 ? 102.576 67.121  225.803 1.00 170.96 ?  156 ASN C C   1 
ATOM   5555  O O   . ASN C  1 118 ? 102.687 67.279  224.586 1.00 174.42 ?  156 ASN C O   1 
ATOM   5556  C CB  . ASN C  1 118 ? 100.623 65.580  225.445 1.00 164.50 ?  156 ASN C CB  1 
ATOM   5557  C CG  . ASN C  1 118 ? 101.438 64.328  225.211 1.00 159.33 ?  156 ASN C CG  1 
ATOM   5558  O OD1 . ASN C  1 118 ? 102.443 64.103  225.880 1.00 159.60 ?  156 ASN C OD1 1 
ATOM   5559  N ND2 . ASN C  1 118 ? 101.018 63.512  224.245 1.00 165.23 ?  156 ASN C ND2 1 
ATOM   5560  N N   . CYS C  1 119 ? 103.550 67.426  226.676 1.00 157.60 ?  157 CYS C N   1 
ATOM   5561  C CA  . CYS C  1 119 ? 104.816 68.089  226.337 1.00 160.22 ?  157 CYS C CA  1 
ATOM   5562  C C   . CYS C  1 119 ? 105.966 67.143  225.994 1.00 154.51 ?  157 CYS C C   1 
ATOM   5563  O O   . CYS C  1 119 ? 106.236 66.191  226.730 1.00 149.99 ?  157 CYS C O   1 
ATOM   5564  C CB  . CYS C  1 119 ? 105.262 69.019  227.469 1.00 165.78 ?  157 CYS C CB  1 
ATOM   5565  S SG  . CYS C  1 119 ? 103.987 70.120  228.073 1.00 207.39 ?  157 CYS C SG  1 
ATOM   5566  N N   . SER C  1 120 ? 106.637 67.423  224.871 1.00 146.12 ?  158 SER C N   1 
ATOM   5567  C CA  . SER C  1 120 ? 107.844 66.735  224.419 1.00 145.74 ?  158 SER C CA  1 
ATOM   5568  C C   . SER C  1 120 ? 109.031 67.700  224.423 1.00 147.01 ?  158 SER C C   1 
ATOM   5569  O O   . SER C  1 120 ? 108.883 68.867  224.044 1.00 149.60 ?  158 SER C O   1 
ATOM   5570  C CB  . SER C  1 120 ? 107.651 66.156  223.015 1.00 145.28 ?  158 SER C CB  1 
ATOM   5571  O OG  . SER C  1 120 ? 106.622 65.182  223.001 1.00 144.07 ?  158 SER C OG  1 
ATOM   5572  N N   . PHE C  1 121 ? 110.209 67.228  224.845 1.00 140.67 ?  159 PHE C N   1 
ATOM   5573  C CA  . PHE C  1 121 ? 111.365 68.118  224.969 1.00 141.93 ?  159 PHE C CA  1 
ATOM   5574  C C   . PHE C  1 121 ? 112.666 67.319  224.951 1.00 141.69 ?  159 PHE C C   1 
ATOM   5575  O O   . PHE C  1 121 ? 112.669 66.092  225.071 1.00 140.55 ?  159 PHE C O   1 
ATOM   5576  C CB  . PHE C  1 121 ? 111.299 68.942  226.253 1.00 143.17 ?  159 PHE C CB  1 
ATOM   5577  C CG  . PHE C  1 121 ? 111.113 68.114  227.488 1.00 141.34 ?  159 PHE C CG  1 
ATOM   5578  C CD1 . PHE C  1 121 ? 109.848 67.793  227.942 1.00 140.60 ?  159 PHE C CD1 1 
ATOM   5579  C CD2 . PHE C  1 121 ? 112.212 67.651  228.194 1.00 141.18 ?  159 PHE C CD2 1 
ATOM   5580  C CE1 . PHE C  1 121 ? 109.682 67.028  229.080 1.00 139.73 ?  159 PHE C CE1 1 
ATOM   5581  C CE2 . PHE C  1 121 ? 112.052 66.886  229.330 1.00 140.29 ?  159 PHE C CE2 1 
ATOM   5582  C CZ  . PHE C  1 121 ? 110.787 66.575  229.775 1.00 139.58 ?  159 PHE C CZ  1 
ATOM   5583  N N   . ASN C  1 122 ? 113.779 68.045  224.792 1.00 146.66 ?  160 ASN C N   1 
ATOM   5584  C CA  . ASN C  1 122 ? 115.122 67.471  224.866 1.00 149.83 ?  160 ASN C CA  1 
ATOM   5585  C C   . ASN C  1 122 ? 115.567 67.316  226.320 1.00 152.77 ?  160 ASN C C   1 
ATOM   5586  O O   . ASN C  1 122 ? 115.110 68.039  227.210 1.00 154.59 ?  160 ASN C O   1 
ATOM   5587  C CB  . ASN C  1 122 ? 116.132 68.346  224.119 1.00 159.13 ?  160 ASN C CB  1 
ATOM   5588  C CG  . ASN C  1 122 ? 116.193 68.048  222.627 1.00 159.76 ?  160 ASN C CG  1 
ATOM   5589  O OD1 . ASN C  1 122 ? 116.774 67.048  222.197 1.00 158.01 ?  160 ASN C OD1 1 
ATOM   5590  N ND2 . ASN C  1 122 ? 115.599 68.923  221.830 1.00 160.80 ?  160 ASN C ND2 1 
ATOM   5591  N N   . MET C  1 123 ? 116.485 66.375  226.556 1.00 156.91 ?  161 MET C N   1 
ATOM   5592  C CA  . MET C  1 123 ? 116.956 66.123  227.913 1.00 160.37 ?  161 MET C CA  1 
ATOM   5593  C C   . MET C  1 123 ? 118.361 65.529  227.928 1.00 162.39 ?  161 MET C C   1 
ATOM   5594  O O   . MET C  1 123 ? 118.754 64.791  227.021 1.00 170.10 ?  161 MET C O   1 
ATOM   5595  C CB  . MET C  1 123 ? 115.994 65.208  228.678 1.00 152.02 ?  161 MET C CB  1 
ATOM   5596  C CG  . MET C  1 123 ? 116.365 65.058  230.137 1.00 148.92 ?  161 MET C CG  1 
ATOM   5597  S SD  . MET C  1 123 ? 116.748 66.673  230.849 1.00 188.58 ?  161 MET C SD  1 
ATOM   5598  C CE  . MET C  1 123 ? 115.181 67.518  230.651 1.00 153.89 ?  161 MET C CE  1 
ATOM   5599  N N   . THR C  1 124 ? 119.121 65.886  228.965 1.00 169.13 ?  162 THR C N   1 
ATOM   5600  C CA  . THR C  1 124 ? 120.480 65.393  229.154 1.00 174.59 ?  162 THR C CA  1 
ATOM   5601  C C   . THR C  1 124 ? 120.441 64.000  229.770 1.00 173.62 ?  162 THR C C   1 
ATOM   5602  O O   . THR C  1 124 ? 119.785 63.784  230.793 1.00 170.82 ?  162 THR C O   1 
ATOM   5603  C CB  . THR C  1 124 ? 121.276 66.328  230.064 1.00 174.80 ?  162 THR C CB  1 
ATOM   5604  O OG1 . THR C  1 124 ? 121.248 67.658  229.536 1.00 183.78 ?  162 THR C OG1 1 
ATOM   5605  C CG2 . THR C  1 124 ? 122.722 65.856  230.193 1.00 180.82 ?  162 THR C CG2 1 
ATOM   5606  N N   . THR C  1 125 ? 121.134 63.052  229.139 1.00 161.95 ?  163 THR C N   1 
ATOM   5607  C CA  . THR C  1 125 ? 121.194 61.688  229.653 1.00 169.86 ?  163 THR C CA  1 
ATOM   5608  C C   . THR C  1 125 ? 122.263 61.581  230.732 1.00 178.29 ?  163 THR C C   1 
ATOM   5609  O O   . THR C  1 125 ? 122.714 62.599  231.268 1.00 175.65 ?  163 THR C O   1 
ATOM   5610  C CB  . THR C  1 125 ? 121.494 60.696  228.526 1.00 178.81 ?  163 THR C CB  1 
ATOM   5611  O OG1 . THR C  1 125 ? 122.751 61.024  227.920 1.00 185.77 ?  163 THR C OG1 1 
ATOM   5612  C CG2 . THR C  1 125 ? 120.409 60.743  227.469 1.00 175.78 ?  163 THR C CG2 1 
ATOM   5613  N N   . GLU C  1 126 ? 122.680 60.352  231.055 1.00 165.62 ?  164 GLU C N   1 
ATOM   5614  C CA  . GLU C  1 126 ? 123.742 60.179  232.042 1.00 168.45 ?  164 GLU C CA  1 
ATOM   5615  C C   . GLU C  1 126 ? 125.039 60.753  231.505 1.00 172.12 ?  164 GLU C C   1 
ATOM   5616  O O   . GLU C  1 126 ? 125.808 61.384  232.242 1.00 171.00 ?  164 GLU C O   1 
ATOM   5617  C CB  . GLU C  1 126 ? 123.924 58.706  232.413 1.00 175.15 ?  164 GLU C CB  1 
ATOM   5618  C CG  . GLU C  1 126 ? 122.709 58.041  233.050 1.00 173.24 ?  164 GLU C CG  1 
ATOM   5619  C CD  . GLU C  1 126 ? 121.689 57.571  232.036 1.00 173.46 ?  164 GLU C CD  1 
ATOM   5620  O OE1 . GLU C  1 126 ? 121.862 57.866  230.835 1.00 178.99 ?  164 GLU C OE1 1 
ATOM   5621  O OE2 . GLU C  1 126 ? 120.710 56.911  232.443 1.00 171.71 -1 164 GLU C OE2 1 
ATOM   5622  N N   . LEU C  1 127 ? 125.290 60.539  230.225 1.00 180.82 ?  165 LEU C N   1 
ATOM   5623  C CA  . LEU C  1 127 ? 126.465 61.071  229.583 1.00 180.39 ?  165 LEU C CA  1 
ATOM   5624  C C   . LEU C  1 127 ? 126.201 62.522  229.206 1.00 172.69 ?  165 LEU C C   1 
ATOM   5625  O O   . LEU C  1 127 ? 125.055 62.951  229.035 1.00 167.52 ?  165 LEU C O   1 
ATOM   5626  C CB  . LEU C  1 127 ? 126.795 60.260  228.324 1.00 186.21 ?  165 LEU C CB  1 
ATOM   5627  C CG  . LEU C  1 127 ? 127.298 58.819  228.476 1.00 191.09 ?  165 LEU C CG  1 
ATOM   5628  C CD1 . LEU C  1 127 ? 126.146 57.846  228.715 1.00 192.32 ?  165 LEU C CD1 1 
ATOM   5629  C CD2 . LEU C  1 127 ? 128.088 58.388  227.248 1.00 197.46 ?  165 LEU C CD2 1 
ATOM   5630  N N   . ARG C  1 128 ? 127.281 63.284  229.072 1.00 190.05 ?  166 ARG C N   1 
ATOM   5631  C CA  . ARG C  1 128 ? 127.179 64.704  228.767 1.00 182.91 ?  166 ARG C CA  1 
ATOM   5632  C C   . ARG C  1 128 ? 127.267 64.971  227.283 1.00 187.60 ?  166 ARG C C   1 
ATOM   5633  O O   . ARG C  1 128 ? 127.692 66.060  226.872 1.00 188.72 ?  166 ARG C O   1 
ATOM   5634  C CB  . ARG C  1 128 ? 128.309 65.484  229.421 1.00 184.09 ?  166 ARG C CB  1 
ATOM   5635  C CG  . ARG C  1 128 ? 127.937 66.893  229.706 1.00 182.82 ?  166 ARG C CG  1 
ATOM   5636  C CD  . ARG C  1 128 ? 129.012 67.569  230.485 1.00 192.14 ?  166 ARG C CD  1 
ATOM   5637  N NE  . ARG C  1 128 ? 129.077 68.959  230.023 1.00 197.30 ?  166 ARG C NE  1 
ATOM   5638  C CZ  . ARG C  1 128 ? 130.194 69.670  229.889 1.00 205.19 ?  166 ARG C CZ  1 
ATOM   5639  N NH1 . ARG C  1 128 ? 131.371 69.132  230.175 1.00 205.31 1  166 ARG C NH1 1 
ATOM   5640  N NH2 . ARG C  1 128 ? 130.134 70.923  229.458 1.00 213.35 ?  166 ARG C NH2 1 
ATOM   5641  N N   . ASP C  1 129 ? 126.857 64.009  226.469 1.00 181.12 ?  167 ASP C N   1 
ATOM   5642  C CA  . ASP C  1 129 ? 126.924 64.089  225.018 1.00 176.71 ?  167 ASP C CA  1 
ATOM   5643  C C   . ASP C  1 129 ? 125.552 64.004  224.377 1.00 184.77 ?  167 ASP C C   1 
ATOM   5644  O O   . ASP C  1 129 ? 124.858 65.017  224.245 1.00 172.47 ?  167 ASP C O   1 
ATOM   5645  C CB  . ASP C  1 129 ? 127.858 63.007  224.495 1.00 182.39 ?  167 ASP C CB  1 
ATOM   5646  C CG  . ASP C  1 129 ? 129.257 63.176  225.026 1.00 183.80 ?  167 ASP C CG  1 
ATOM   5647  O OD1 . ASP C  1 129 ? 129.530 64.254  225.599 1.00 183.40 ?  167 ASP C OD1 1 
ATOM   5648  O OD2 . ASP C  1 129 ? 130.068 62.238  224.905 1.00 187.94 -1 167 ASP C OD2 1 
ATOM   5649  N N   . LYS C  1 130 ? 125.145 62.796  223.999 1.00 193.15 ?  168 LYS C N   1 
ATOM   5650  C CA  . LYS C  1 130 ? 123.874 62.623  223.316 1.00 195.70 ?  168 LYS C CA  1 
ATOM   5651  C C   . LYS C  1 130 ? 122.739 63.080  224.230 1.00 181.39 ?  168 LYS C C   1 
ATOM   5652  O O   . LYS C  1 130 ? 122.771 62.851  225.442 1.00 175.06 ?  168 LYS C O   1 
ATOM   5653  C CB  . LYS C  1 130 ? 123.726 61.132  223.009 1.00 202.24 ?  168 LYS C CB  1 
ATOM   5654  C CG  . LYS C  1 130 ? 124.821 60.570  222.103 1.00 197.00 ?  168 LYS C CG  1 
ATOM   5655  C CD  . LYS C  1 130 ? 124.598 59.093  221.807 1.00 199.16 ?  168 LYS C CD  1 
ATOM   5656  C CE  . LYS C  1 130 ? 125.670 58.530  220.881 1.00 195.59 ?  168 LYS C CE  1 
ATOM   5657  N NZ  . LYS C  1 130 ? 125.443 57.086  220.584 1.00 192.94 1  168 LYS C NZ  1 
ATOM   5658  N N   . LYS C  1 131 ? 121.739 63.749  223.644 1.00 202.16 ?  169 LYS C N   1 
ATOM   5659  C CA  . LYS C  1 131 ? 120.612 64.270  224.410 1.00 185.24 ?  169 LYS C CA  1 
ATOM   5660  C C   . LYS C  1 131 ? 119.537 63.190  224.578 1.00 181.22 ?  169 LYS C C   1 
ATOM   5661  O O   . LYS C  1 131 ? 119.820 61.994  224.471 1.00 191.99 ?  169 LYS C O   1 
ATOM   5662  C CB  . LYS C  1 131 ? 120.099 65.560  223.758 1.00 180.75 ?  169 LYS C CB  1 
ATOM   5663  C CG  . LYS C  1 131 ? 121.162 66.658  223.642 1.00 180.25 ?  169 LYS C CG  1 
ATOM   5664  C CD  . LYS C  1 131 ? 121.842 66.655  222.280 1.00 178.63 ?  169 LYS C CD  1 
ATOM   5665  C CE  . LYS C  1 131 ? 120.833 66.881  221.168 1.00 170.93 ?  169 LYS C CE  1 
ATOM   5666  N NZ  . LYS C  1 131 ? 121.471 66.880  219.825 1.00 176.83 1  169 LYS C NZ  1 
ATOM   5667  N N   . GLN C  1 132 ? 118.289 63.602  224.822 1.00 166.37 ?  170 GLN C N   1 
ATOM   5668  C CA  . GLN C  1 132 ? 117.195 62.655  225.038 1.00 157.35 ?  170 GLN C CA  1 
ATOM   5669  C C   . GLN C  1 132 ? 115.853 63.318  224.755 1.00 142.02 ?  170 GLN C C   1 
ATOM   5670  O O   . GLN C  1 132 ? 115.489 64.275  225.445 1.00 142.41 ?  170 GLN C O   1 
ATOM   5671  C CB  . GLN C  1 132 ? 117.243 62.124  226.463 1.00 162.27 ?  170 GLN C CB  1 
ATOM   5672  C CG  . GLN C  1 132 ? 116.336 60.964  226.725 1.00 154.00 ?  170 GLN C CG  1 
ATOM   5673  C CD  . GLN C  1 132 ? 116.466 60.465  228.141 1.00 151.92 ?  170 GLN C CD  1 
ATOM   5674  O OE1 . GLN C  1 132 ? 117.254 60.991  228.930 1.00 151.67 ?  170 GLN C OE1 1 
ATOM   5675  N NE2 . GLN C  1 132 ? 115.690 59.447  228.477 1.00 148.78 ?  170 GLN C NE2 1 
ATOM   5676  N N   . LYS C  1 133 ? 115.129 62.841  223.739 1.00 144.86 ?  171 LYS C N   1 
ATOM   5677  C CA  . LYS C  1 133 ? 113.813 63.389  223.382 1.00 144.80 ?  171 LYS C CA  1 
ATOM   5678  C C   . LYS C  1 133 ? 112.707 62.620  224.111 1.00 140.62 ?  171 LYS C C   1 
ATOM   5679  O O   . LYS C  1 133 ? 112.073 61.718  223.562 1.00 141.29 ?  171 LYS C O   1 
ATOM   5680  C CB  . LYS C  1 133 ? 113.592 63.361  221.872 1.00 147.96 ?  171 LYS C CB  1 
ATOM   5681  C CG  . LYS C  1 133 ? 114.127 64.552  221.074 1.00 148.05 ?  171 LYS C CG  1 
ATOM   5682  C CD  . LYS C  1 133 ? 113.238 64.758  219.842 1.00 148.23 ?  171 LYS C CD  1 
ATOM   5683  C CE  . LYS C  1 133 ? 112.655 66.161  219.772 1.00 152.49 ?  171 LYS C CE  1 
ATOM   5684  N NZ  . LYS C  1 133 ? 111.461 66.229  218.879 1.00 157.21 1  171 LYS C NZ  1 
ATOM   5685  N N   . VAL C  1 134 ? 112.482 62.969  225.379 1.00 145.22 ?  172 VAL C N   1 
ATOM   5686  C CA  . VAL C  1 134 ? 111.441 62.320  226.173 1.00 144.25 ?  172 VAL C CA  1 
ATOM   5687  C C   . VAL C  1 134 ? 110.310 63.312  226.448 1.00 144.52 ?  172 VAL C C   1 
ATOM   5688  O O   . VAL C  1 134 ? 110.498 64.533  226.436 1.00 145.52 ?  172 VAL C O   1 
ATOM   5689  C CB  . VAL C  1 134 ? 111.999 61.731  227.485 1.00 144.07 ?  172 VAL C CB  1 
ATOM   5690  C CG1 . VAL C  1 134 ? 112.764 60.448  227.199 1.00 143.65 ?  172 VAL C CG1 1 
ATOM   5691  C CG2 . VAL C  1 134 ? 112.897 62.738  228.179 1.00 145.08 ?  172 VAL C CG2 1 
ATOM   5692  N N   . TYR C  1 135 ? 109.116 62.768  226.706 1.00 158.93 ?  173 TYR C N   1 
ATOM   5693  C CA  . TYR C  1 135 ? 107.906 63.550  226.950 1.00 161.11 ?  173 TYR C CA  1 
ATOM   5694  C C   . TYR C  1 135 ? 107.318 63.337  228.345 1.00 161.10 ?  173 TYR C C   1 
ATOM   5695  O O   . TYR C  1 135 ? 107.525 62.292  228.970 1.00 158.94 ?  173 TYR C O   1 
ATOM   5696  C CB  . TYR C  1 135 ? 106.839 63.224  225.900 1.00 163.27 ?  173 TYR C CB  1 
ATOM   5697  C CG  . TYR C  1 135 ? 106.165 61.885  226.092 1.00 165.08 ?  173 TYR C CG  1 
ATOM   5698  C CD1 . TYR C  1 135 ? 106.775 60.708  225.679 1.00 163.26 ?  173 TYR C CD1 1 
ATOM   5699  C CD2 . TYR C  1 135 ? 104.908 61.802  226.675 1.00 166.27 ?  173 TYR C CD2 1 
ATOM   5700  C CE1 . TYR C  1 135 ? 106.152 59.482  225.850 1.00 164.37 ?  173 TYR C CE1 1 
ATOM   5701  C CE2 . TYR C  1 135 ? 104.278 60.585  226.850 1.00 166.07 ?  173 TYR C CE2 1 
ATOM   5702  C CZ  . TYR C  1 135 ? 104.903 59.427  226.436 1.00 166.71 ?  173 TYR C CZ  1 
ATOM   5703  O OH  . TYR C  1 135 ? 104.276 58.213  226.608 1.00 163.78 ?  173 TYR C OH  1 
ATOM   5704  N N   . SER C  1 136 ? 106.578 64.345  228.822 1.00 147.73 ?  174 SER C N   1 
ATOM   5705  C CA  . SER C  1 136 ? 105.879 64.308  230.113 1.00 148.28 ?  174 SER C CA  1 
ATOM   5706  C C   . SER C  1 136 ? 104.457 64.860  229.938 1.00 154.48 ?  174 SER C C   1 
ATOM   5707  O O   . SER C  1 136 ? 104.016 65.160  228.824 1.00 157.37 ?  174 SER C O   1 
ATOM   5708  C CB  . SER C  1 136 ? 106.662 65.074  231.186 1.00 150.52 ?  174 SER C CB  1 
ATOM   5709  O OG  . SER C  1 136 ? 105.972 65.058  232.424 1.00 150.96 ?  174 SER C OG  1 
ATOM   5710  N N   . LEU C  1 137 ? 103.740 65.010  231.062 1.00 143.46 ?  175 LEU C N   1 
ATOM   5711  C CA  . LEU C  1 137 ? 102.353 65.502  231.095 1.00 154.46 ?  175 LEU C CA  1 
ATOM   5712  C C   . LEU C  1 137 ? 102.166 66.509  232.230 1.00 158.84 ?  175 LEU C C   1 
ATOM   5713  O O   . LEU C  1 137 ? 102.082 66.119  233.399 1.00 154.66 ?  175 LEU C O   1 
ATOM   5714  C CB  . LEU C  1 137 ? 101.365 64.353  231.251 1.00 153.79 ?  175 LEU C CB  1 
ATOM   5715  C CG  . LEU C  1 137 ? 99.955  64.629  230.722 1.00 157.54 ?  175 LEU C CG  1 
ATOM   5716  C CD1 . LEU C  1 137 ? 99.927  64.722  229.206 1.00 160.48 ?  175 LEU C CD1 1 
ATOM   5717  C CD2 . LEU C  1 137 ? 98.965  63.593  231.230 1.00 154.66 ?  175 LEU C CD2 1 
ATOM   5718  N N   . PHE C  1 138 ? 102.102 67.797  231.894 1.00 155.73 ?  176 PHE C N   1 
ATOM   5719  C CA  . PHE C  1 138 ? 101.959 68.857  232.884 1.00 157.66 ?  176 PHE C CA  1 
ATOM   5720  C C   . PHE C  1 138 ? 100.580 69.510  232.841 1.00 168.31 ?  176 PHE C C   1 
ATOM   5721  O O   . PHE C  1 138 ? 99.908  69.524  231.805 1.00 175.17 ?  176 PHE C O   1 
ATOM   5722  C CB  . PHE C  1 138 ? 103.033 69.916  232.664 1.00 156.56 ?  176 PHE C CB  1 
ATOM   5723  C CG  . PHE C  1 138 ? 104.408 69.353  232.687 1.00 147.62 ?  176 PHE C CG  1 
ATOM   5724  C CD1 . PHE C  1 138 ? 105.000 69.002  233.884 1.00 143.84 ?  176 PHE C CD1 1 
ATOM   5725  C CD2 . PHE C  1 138 ? 105.086 69.110  231.506 1.00 143.63 ?  176 PHE C CD2 1 
ATOM   5726  C CE1 . PHE C  1 138 ? 106.261 68.456  233.909 1.00 135.58 ?  176 PHE C CE1 1 
ATOM   5727  C CE2 . PHE C  1 138 ? 106.348 68.563  231.522 1.00 134.53 ?  176 PHE C CE2 1 
ATOM   5728  C CZ  . PHE C  1 138 ? 106.938 68.235  232.727 1.00 131.01 ?  176 PHE C CZ  1 
ATOM   5729  N N   . TYR C  1 139 ? 100.169 70.050  233.990 1.00 150.72 ?  177 TYR C N   1 
ATOM   5730  C CA  . TYR C  1 139 ? 98.921  70.789  234.108 1.00 156.80 ?  177 TYR C CA  1 
ATOM   5731  C C   . TYR C  1 139 ? 99.083  72.188  233.517 1.00 160.24 ?  177 TYR C C   1 
ATOM   5732  O O   . TYR C  1 139 ? 100.196 72.699  233.365 1.00 158.22 ?  177 TYR C O   1 
ATOM   5733  C CB  . TYR C  1 139 ? 98.482  70.856  235.572 1.00 157.87 ?  177 TYR C CB  1 
ATOM   5734  C CG  . TYR C  1 139 ? 98.196  69.495  236.179 1.00 153.59 ?  177 TYR C CG  1 
ATOM   5735  C CD1 . TYR C  1 139 ? 99.224  68.701  236.675 1.00 148.70 ?  177 TYR C CD1 1 
ATOM   5736  C CD2 . TYR C  1 139 ? 96.895  69.020  236.286 1.00 154.62 ?  177 TYR C CD2 1 
ATOM   5737  C CE1 . TYR C  1 139 ? 98.966  67.457  237.234 1.00 147.88 ?  177 TYR C CE1 1 
ATOM   5738  C CE2 . TYR C  1 139 ? 96.627  67.776  236.846 1.00 150.29 ?  177 TYR C CE2 1 
ATOM   5739  C CZ  . TYR C  1 139 ? 97.667  67.001  237.320 1.00 148.05 ?  177 TYR C CZ  1 
ATOM   5740  O OH  . TYR C  1 139 ? 97.406  65.768  237.877 1.00 147.39 ?  177 TYR C OH  1 
ATOM   5741  N N   . ARG C  1 140 ? 97.949  72.811  233.183 1.00 179.03 ?  178 ARG C N   1 
ATOM   5742  C CA  . ARG C  1 140 ? 97.989  74.149  232.596 1.00 184.87 ?  178 ARG C CA  1 
ATOM   5743  C C   . ARG C  1 140 ? 98.529  75.181  233.581 1.00 186.30 ?  178 ARG C C   1 
ATOM   5744  O O   . ARG C  1 140 ? 99.178  76.151  233.172 1.00 186.19 ?  178 ARG C O   1 
ATOM   5745  C CB  . ARG C  1 140 ? 96.601  74.527  232.080 1.00 188.63 ?  178 ARG C CB  1 
ATOM   5746  C CG  . ARG C  1 140 ? 96.499  75.895  231.443 1.00 191.22 ?  178 ARG C CG  1 
ATOM   5747  C CD  . ARG C  1 140 ? 95.124  76.058  230.820 1.00 198.51 ?  178 ARG C CD  1 
ATOM   5748  N NE  . ARG C  1 140 ? 94.869  75.060  229.777 1.00 203.00 ?  178 ARG C NE  1 
ATOM   5749  C CZ  . ARG C  1 140 ? 95.239  75.175  228.503 1.00 205.98 ?  178 ARG C CZ  1 
ATOM   5750  N NH1 . ARG C  1 140 ? 95.893  76.250  228.092 1.00 205.16 1  178 ARG C NH1 1 
ATOM   5751  N NH2 . ARG C  1 140 ? 94.948  74.211  227.636 1.00 211.15 ?  178 ARG C NH2 1 
ATOM   5752  N N   . LEU C  1 141 ? 98.275  74.983  234.875 1.00 174.90 ?  179 LEU C N   1 
ATOM   5753  C CA  . LEU C  1 141 ? 98.750  75.893  235.910 1.00 169.26 ?  179 LEU C CA  1 
ATOM   5754  C C   . LEU C  1 141 ? 100.259 75.810  236.106 1.00 162.08 ?  179 LEU C C   1 
ATOM   5755  O O   . LEU C  1 141 ? 100.839 76.689  236.752 1.00 160.49 ?  179 LEU C O   1 
ATOM   5756  C CB  . LEU C  1 141 ? 98.037  75.592  237.228 1.00 169.95 ?  179 LEU C CB  1 
ATOM   5757  C CG  . LEU C  1 141 ? 96.512  75.638  237.153 1.00 175.71 ?  179 LEU C CG  1 
ATOM   5758  C CD1 . LEU C  1 141 ? 95.882  75.142  238.447 1.00 171.16 ?  179 LEU C CD1 1 
ATOM   5759  C CD2 . LEU C  1 141 ? 96.061  77.056  236.836 1.00 179.76 ?  179 LEU C CD2 1 
ATOM   5760  N N   . ASP C  1 142 ? 100.895 74.766  235.581 1.00 173.58 ?  180 ASP C N   1 
ATOM   5761  C CA  . ASP C  1 142 ? 102.329 74.545  235.709 1.00 167.40 ?  180 ASP C CA  1 
ATOM   5762  C C   . ASP C  1 142 ? 103.140 75.122  234.557 1.00 166.01 ?  180 ASP C C   1 
ATOM   5763  O O   . ASP C  1 142 ? 104.348 75.338  234.714 1.00 159.77 ?  180 ASP C O   1 
ATOM   5764  C CB  . ASP C  1 142 ? 102.608 73.041  235.784 1.00 161.95 ?  180 ASP C CB  1 
ATOM   5765  C CG  . ASP C  1 142 ? 102.037 72.400  237.031 1.00 159.70 ?  180 ASP C CG  1 
ATOM   5766  O OD1 . ASP C  1 142 ? 102.089 73.034  238.102 1.00 160.27 ?  180 ASP C OD1 1 
ATOM   5767  O OD2 . ASP C  1 142 ? 101.499 71.276  236.930 1.00 164.50 -1 180 ASP C OD2 1 
ATOM   5768  N N   . VAL C  1 143 ? 102.509 75.355  233.408 1.00 156.35 ?  181 VAL C N   1 
ATOM   5769  C CA  . VAL C  1 143 ? 103.183 75.813  232.203 1.00 157.60 ?  181 VAL C CA  1 
ATOM   5770  C C   . VAL C  1 143 ? 102.702 77.208  231.805 1.00 162.40 ?  181 VAL C C   1 
ATOM   5771  O O   . VAL C  1 143 ? 101.716 77.734  232.326 1.00 164.66 ?  181 VAL C O   1 
ATOM   5772  C CB  . VAL C  1 143 ? 102.979 74.823  231.041 1.00 154.68 ?  181 VAL C CB  1 
ATOM   5773  C CG1 . VAL C  1 143 ? 103.657 73.488  231.358 1.00 151.08 ?  181 VAL C CG1 1 
ATOM   5774  C CG2 . VAL C  1 143 ? 101.485 74.625  230.786 1.00 154.89 ?  181 VAL C CG2 1 
ATOM   5775  N N   . VAL C  1 144 ? 103.440 77.806  230.869 1.00 159.27 ?  182 VAL C N   1 
ATOM   5776  C CA  . VAL C  1 144 ? 103.129 79.115  230.304 1.00 164.20 ?  182 VAL C CA  1 
ATOM   5777  C C   . VAL C  1 144 ? 103.817 79.257  228.947 1.00 164.81 ?  182 VAL C C   1 
ATOM   5778  O O   . VAL C  1 144 ? 105.014 78.977  228.798 1.00 163.42 ?  182 VAL C O   1 
ATOM   5779  C CB  . VAL C  1 144 ? 103.497 80.253  231.281 1.00 167.95 ?  182 VAL C CB  1 
ATOM   5780  C CG1 . VAL C  1 144 ? 104.992 80.556  231.277 1.00 169.54 ?  182 VAL C CG1 1 
ATOM   5781  C CG2 . VAL C  1 144 ? 102.695 81.504  230.950 1.00 172.70 ?  182 VAL C CG2 1 
ATOM   5782  N N   . GLN C  1 145 ? 103.039 79.604  227.925 1.00 158.87 ?  183 GLN C N   1 
ATOM   5783  C CA  . GLN C  1 145 ? 103.537 79.718  226.566 1.00 159.53 ?  183 GLN C CA  1 
ATOM   5784  C C   . GLN C  1 145 ? 104.463 80.923  226.425 1.00 164.72 ?  183 GLN C C   1 
ATOM   5785  O O   . GLN C  1 145 ? 104.442 81.854  227.232 1.00 169.54 ?  183 GLN C O   1 
ATOM   5786  C CB  . GLN C  1 145 ? 102.375 79.823  225.581 1.00 160.65 ?  183 GLN C CB  1 
ATOM   5787  C CG  . GLN C  1 145 ? 101.417 80.956  225.888 1.00 166.11 ?  183 GLN C CG  1 
ATOM   5788  C CD  . GLN C  1 145 ? 100.260 81.023  224.907 1.00 167.30 ?  183 GLN C CD  1 
ATOM   5789  O OE1 . GLN C  1 145 ? 100.212 80.275  223.925 1.00 163.94 ?  183 GLN C OE1 1 
ATOM   5790  N NE2 . GLN C  1 145 ? 99.336  81.949  225.153 1.00 172.34 ?  183 GLN C NE2 1 
ATOM   5791  N N   . ILE C  1 146 ? 105.275 80.908  225.372 1.00 155.06 ?  184 ILE C N   1 
ATOM   5792  C CA  . ILE C  1 146 ? 106.200 82.013  225.140 1.00 156.96 ?  184 ILE C CA  1 
ATOM   5793  C C   . ILE C  1 146 ? 106.416 82.180  223.640 1.00 158.06 ?  184 ILE C C   1 
ATOM   5794  O O   . ILE C  1 146 ? 106.637 81.202  222.920 1.00 156.81 ?  184 ILE C O   1 
ATOM   5795  C CB  . ILE C  1 146 ? 107.539 81.796  225.875 1.00 156.25 ?  184 ILE C CB  1 
ATOM   5796  C CG1 . ILE C  1 146 ? 108.557 82.858  225.459 1.00 158.29 ?  184 ILE C CG1 1 
ATOM   5797  C CG2 . ILE C  1 146 ? 108.071 80.380  225.645 1.00 154.17 ?  184 ILE C CG2 1 
ATOM   5798  C CD1 . ILE C  1 146 ? 108.178 84.260  225.878 1.00 160.37 ?  184 ILE C CD1 1 
ATOM   5799  N N   . ASN C  1 147 ? 106.331 83.428  223.174 1.00 180.79 ?  185 ASN C N   1 
ATOM   5800  C CA  . ASN C  1 147 ? 106.660 83.796  221.792 1.00 184.93 ?  185 ASN C CA  1 
ATOM   5801  C C   . ASN C  1 147 ? 107.920 84.672  221.711 1.00 191.93 ?  185 ASN C C   1 
ATOM   5802  O O   . ASN C  1 147 ? 109.057 84.190  221.763 1.00 189.04 ?  185 ASN C O   1 
ATOM   5803  C CB  . ASN C  1 147 ? 105.486 84.540  221.142 1.00 189.94 ?  185 ASN C CB  1 
ATOM   5804  C CG  . ASN C  1 147 ? 104.830 83.745  220.033 1.00 184.83 ?  185 ASN C CG  1 
ATOM   5805  O OD1 . ASN C  1 147 ? 105.192 82.598  219.781 1.00 177.28 ?  185 ASN C OD1 1 
ATOM   5806  N ND2 . ASN C  1 147 ? 103.844 84.348  219.373 1.00 188.54 ?  185 ASN C ND2 1 
ATOM   5807  N N   . GLU C  1 160 ? 104.422 76.744  221.790 1.00 151.17 ?  190 GLU C N   1 
ATOM   5808  C CA  . GLU C  1 160 ? 105.631 76.588  222.590 1.00 152.52 ?  190 GLU C CA  1 
ATOM   5809  C C   . GLU C  1 160 ? 105.400 76.986  224.043 1.00 156.48 ?  190 GLU C C   1 
ATOM   5810  O O   . GLU C  1 160 ? 104.851 78.055  224.294 1.00 160.76 ?  190 GLU C O   1 
ATOM   5811  C CB  . GLU C  1 160 ? 106.738 77.487  222.032 1.00 154.84 ?  190 GLU C CB  1 
ATOM   5812  C CG  . GLU C  1 160 ? 107.375 77.073  220.728 1.00 147.58 ?  190 GLU C CG  1 
ATOM   5813  C CD  . GLU C  1 160 ? 108.542 77.982  220.369 1.00 155.81 ?  190 GLU C CD  1 
ATOM   5814  O OE1 . GLU C  1 160 ? 108.788 78.953  221.117 1.00 163.06 ?  190 GLU C OE1 1 
ATOM   5815  O OE2 . GLU C  1 160 ? 109.211 77.733  219.344 1.00 158.80 -1 190 GLU C OE2 1 
ATOM   5816  N N   . TYR C  1 161 ? 105.805 76.152  225.001 1.00 161.37 ?  191 TYR C N   1 
ATOM   5817  C CA  . TYR C  1 161 ? 105.586 76.470  226.408 1.00 158.61 ?  191 TYR C CA  1 
ATOM   5818  C C   . TYR C  1 161 ? 106.906 76.472  227.186 1.00 158.88 ?  191 TYR C C   1 
ATOM   5819  O O   . TYR C  1 161 ? 107.996 76.339  226.622 1.00 155.81 ?  191 TYR C O   1 
ATOM   5820  C CB  . TYR C  1 161 ? 104.587 75.487  227.028 1.00 154.28 ?  191 TYR C CB  1 
ATOM   5821  C CG  . TYR C  1 161 ? 103.165 75.603  226.510 1.00 157.25 ?  191 TYR C CG  1 
ATOM   5822  C CD1 . TYR C  1 161 ? 102.782 75.026  225.304 1.00 157.68 ?  191 TYR C CD1 1 
ATOM   5823  C CD2 . TYR C  1 161 ? 102.191 76.258  227.258 1.00 161.34 ?  191 TYR C CD2 1 
ATOM   5824  C CE1 . TYR C  1 161 ? 101.466 75.129  224.842 1.00 157.44 ?  191 TYR C CE1 1 
ATOM   5825  C CE2 . TYR C  1 161 ? 100.882 76.362  226.810 1.00 163.84 ?  191 TYR C CE2 1 
ATOM   5826  C CZ  . TYR C  1 161 ? 100.521 75.800  225.607 1.00 161.34 ?  191 TYR C CZ  1 
ATOM   5827  O OH  . TYR C  1 161 ? 99.212  75.923  225.187 1.00 165.08 ?  191 TYR C OH  1 
ATOM   5828  N N   . ARG C  1 162 ? 106.783 76.625  228.504 1.00 152.05 ?  192 ARG C N   1 
ATOM   5829  C CA  . ARG C  1 162 ? 107.900 76.573  229.440 1.00 154.05 ?  192 ARG C CA  1 
ATOM   5830  C C   . ARG C  1 162 ? 107.327 76.332  230.830 1.00 148.07 ?  192 ARG C C   1 
ATOM   5831  O O   . ARG C  1 162 ? 106.124 76.482  231.056 1.00 146.90 ?  192 ARG C O   1 
ATOM   5832  C CB  . ARG C  1 162 ? 108.745 77.849  229.433 1.00 162.56 ?  192 ARG C CB  1 
ATOM   5833  C CG  . ARG C  1 162 ? 108.126 79.001  230.202 1.00 163.26 ?  192 ARG C CG  1 
ATOM   5834  C CD  . ARG C  1 162 ? 109.149 80.093  230.478 1.00 166.48 ?  192 ARG C CD  1 
ATOM   5835  N NE  . ARG C  1 162 ? 108.637 81.084  231.419 1.00 167.86 ?  192 ARG C NE  1 
ATOM   5836  C CZ  . ARG C  1 162 ? 107.972 82.176  231.057 1.00 176.76 ?  192 ARG C CZ  1 
ATOM   5837  N NH1 . ARG C  1 162 ? 107.744 82.417  229.774 1.00 183.07 1  192 ARG C NH1 1 
ATOM   5838  N NH2 . ARG C  1 162 ? 107.531 83.025  231.973 1.00 176.17 ?  192 ARG C NH2 1 
ATOM   5839  N N   . LEU C  1 163 ? 108.196 75.952  231.761 1.00 150.26 ?  193 LEU C N   1 
ATOM   5840  C CA  . LEU C  1 163 ? 107.747 75.802  233.137 1.00 150.99 ?  193 LEU C CA  1 
ATOM   5841  C C   . LEU C  1 163 ? 107.455 77.180  233.724 1.00 154.04 ?  193 LEU C C   1 
ATOM   5842  O O   . LEU C  1 163 ? 108.192 78.142  233.486 1.00 156.66 ?  193 LEU C O   1 
ATOM   5843  C CB  . LEU C  1 163 ? 108.797 75.073  233.974 1.00 151.14 ?  193 LEU C CB  1 
ATOM   5844  C CG  . LEU C  1 163 ? 108.982 73.594  233.629 1.00 147.89 ?  193 LEU C CG  1 
ATOM   5845  C CD1 . LEU C  1 163 ? 109.991 72.931  234.557 1.00 147.72 ?  193 LEU C CD1 1 
ATOM   5846  C CD2 . LEU C  1 163 ? 107.639 72.876  233.687 1.00 145.67 ?  193 LEU C CD2 1 
ATOM   5847  N N   . ILE C  1 164 ? 106.370 77.276  234.496 1.00 161.59 ?  194 ILE C N   1 
ATOM   5848  C CA  . ILE C  1 164 ? 105.920 78.573  234.994 1.00 163.86 ?  194 ILE C CA  1 
ATOM   5849  C C   . ILE C  1 164 ? 106.876 79.195  236.002 1.00 165.58 ?  194 ILE C C   1 
ATOM   5850  O O   . ILE C  1 164 ? 106.765 80.393  236.287 1.00 171.83 ?  194 ILE C O   1 
ATOM   5851  C CB  . ILE C  1 164 ? 104.511 78.441  235.611 1.00 162.60 ?  194 ILE C CB  1 
ATOM   5852  C CG1 . ILE C  1 164 ? 103.797 79.797  235.640 1.00 166.31 ?  194 ILE C CG1 1 
ATOM   5853  C CG2 . ILE C  1 164 ? 104.596 77.848  237.010 1.00 159.40 ?  194 ILE C CG2 1 
ATOM   5854  C CD1 . ILE C  1 164 ? 102.386 79.739  236.195 1.00 163.86 ?  194 ILE C CD1 1 
ATOM   5855  N N   . ASN C  1 165 ? 107.840 78.431  236.518 1.00 152.97 ?  195 ASN C N   1 
ATOM   5856  C CA  . ASN C  1 165 ? 108.751 78.925  237.541 1.00 158.71 ?  195 ASN C CA  1 
ATOM   5857  C C   . ASN C  1 165 ? 110.133 79.245  236.997 1.00 158.61 ?  195 ASN C C   1 
ATOM   5858  O O   . ASN C  1 165 ? 110.950 79.820  237.725 1.00 166.41 ?  195 ASN C O   1 
ATOM   5859  C CB  . ASN C  1 165 ? 108.902 77.898  238.663 1.00 156.87 ?  195 ASN C CB  1 
ATOM   5860  C CG  . ASN C  1 165 ? 109.721 76.710  238.235 1.00 150.60 ?  195 ASN C CG  1 
ATOM   5861  O OD1 . ASN C  1 165 ? 110.922 76.649  238.494 1.00 150.93 ?  195 ASN C OD1 1 
ATOM   5862  N ND2 . ASN C  1 165 ? 109.085 75.763  237.557 1.00 149.01 ?  195 ASN C ND2 1 
ATOM   5863  N N   . CYS C  1 166 ? 110.404 78.890  235.739 1.00 156.06 ?  196 CYS C N   1 
ATOM   5864  C CA  . CYS C  1 166 ? 111.721 79.099  235.155 1.00 158.09 ?  196 CYS C CA  1 
ATOM   5865  C C   . CYS C  1 166 ? 112.077 80.577  235.102 1.00 161.62 ?  196 CYS C C   1 
ATOM   5866  O O   . CYS C  1 166 ? 113.262 80.921  235.059 1.00 163.96 ?  196 CYS C O   1 
ATOM   5867  C CB  . CYS C  1 166 ? 111.785 78.465  233.764 1.00 156.04 ?  196 CYS C CB  1 
ATOM   5868  S SG  . CYS C  1 166 ? 112.007 76.662  233.749 1.00 156.51 ?  196 CYS C SG  1 
ATOM   5869  N N   . ASN C  1 167 ? 111.081 81.457  235.107 1.00 158.59 ?  197 ASN C N   1 
ATOM   5870  C CA  . ASN C  1 167 ? 111.325 82.888  235.080 1.00 165.03 ?  197 ASN C CA  1 
ATOM   5871  C C   . ASN C  1 167 ? 111.131 83.513  236.455 1.00 167.09 ?  197 ASN C C   1 
ATOM   5872  O O   . ASN C  1 167 ? 111.107 84.742  236.573 1.00 171.90 ?  197 ASN C O   1 
ATOM   5873  C CB  . ASN C  1 167 ? 110.420 83.559  234.044 1.00 165.13 ?  197 ASN C CB  1 
ATOM   5874  C CG  . ASN C  1 167 ? 108.986 83.693  234.513 1.00 161.76 ?  197 ASN C CG  1 
ATOM   5875  O OD1 . ASN C  1 167 ? 108.273 82.700  234.655 1.00 157.22 ?  197 ASN C OD1 1 
ATOM   5876  N ND2 . ASN C  1 167 ? 108.543 84.934  234.715 1.00 176.37 ?  197 ASN C ND2 1 
ATOM   5877  N N   . THR C  1 168 ? 110.984 82.689  237.497 1.00 161.30 ?  198 THR C N   1 
ATOM   5878  C CA  . THR C  1 168 ? 110.796 83.173  238.860 1.00 159.83 ?  198 THR C CA  1 
ATOM   5879  C C   . THR C  1 168 ? 111.907 82.740  239.805 1.00 158.68 ?  198 THR C C   1 
ATOM   5880  O O   . THR C  1 168 ? 112.495 83.588  240.485 1.00 161.88 ?  198 THR C O   1 
ATOM   5881  C CB  . THR C  1 168 ? 109.442 82.689  239.410 1.00 161.35 ?  198 THR C CB  1 
ATOM   5882  O OG1 . THR C  1 168 ? 109.486 81.271  239.617 1.00 160.61 ?  198 THR C OG1 1 
ATOM   5883  C CG2 . THR C  1 168 ? 108.324 83.012  238.436 1.00 169.84 ?  198 THR C CG2 1 
ATOM   5884  N N   . SER C  1 169 ? 112.225 81.448  239.864 1.00 166.63 ?  199 SER C N   1 
ATOM   5885  C CA  . SER C  1 169 ? 113.244 80.954  240.785 1.00 164.99 ?  199 SER C CA  1 
ATOM   5886  C C   . SER C  1 169 ? 113.706 79.573  240.330 1.00 162.84 ?  199 SER C C   1 
ATOM   5887  O O   . SER C  1 169 ? 113.264 79.057  239.299 1.00 162.76 ?  199 SER C O   1 
ATOM   5888  C CB  . SER C  1 169 ? 112.706 80.913  242.214 1.00 162.89 ?  199 SER C CB  1 
ATOM   5889  O OG  . SER C  1 169 ? 111.593 80.044  242.298 1.00 160.43 ?  199 SER C OG  1 
ATOM   5890  N N   . ALA C  1 170 ? 114.603 78.973  241.116 1.00 160.00 ?  200 ALA C N   1 
ATOM   5891  C CA  . ALA C  1 170 ? 115.081 77.622  240.860 1.00 157.30 ?  200 ALA C CA  1 
ATOM   5892  C C   . ALA C  1 170 ? 114.002 76.621  241.272 1.00 154.37 ?  200 ALA C C   1 
ATOM   5893  O O   . ALA C  1 170 ? 112.981 76.987  241.855 1.00 154.16 ?  200 ALA C O   1 
ATOM   5894  C CB  . ALA C  1 170 ? 116.384 77.358  241.611 1.00 155.58 ?  200 ALA C CB  1 
ATOM   5895  N N   . ILE C  1 171 ? 114.232 75.339  240.986 1.00 148.00 ?  201 ILE C N   1 
ATOM   5896  C CA  . ILE C  1 171 ? 113.241 74.305  241.281 1.00 145.64 ?  201 ILE C CA  1 
ATOM   5897  C C   . ILE C  1 171 ? 113.909 73.016  241.751 1.00 144.67 ?  201 ILE C C   1 
ATOM   5898  O O   . ILE C  1 171 ? 114.917 72.583  241.183 1.00 144.75 ?  201 ILE C O   1 
ATOM   5899  C CB  . ILE C  1 171 ? 112.339 74.042  240.057 1.00 146.42 ?  201 ILE C CB  1 
ATOM   5900  C CG1 . ILE C  1 171 ? 111.353 72.912  240.352 1.00 144.60 ?  201 ILE C CG1 1 
ATOM   5901  C CG2 . ILE C  1 171 ? 113.178 73.753  238.815 1.00 146.55 ?  201 ILE C CG2 1 
ATOM   5902  C CD1 . ILE C  1 171 ? 110.407 72.622  239.219 1.00 144.57 ?  201 ILE C CD1 1 
ATOM   5903  N N   . THR C  1 172 ? 113.358 72.413  242.813 1.00 154.56 ?  202 THR C N   1 
ATOM   5904  C CA  . THR C  1 172 ? 113.841 71.140  243.338 1.00 149.12 ?  202 THR C CA  1 
ATOM   5905  C C   . THR C  1 172 ? 112.695 70.145  243.486 1.00 148.46 ?  202 THR C C   1 
ATOM   5906  O O   . THR C  1 172 ? 111.597 70.507  243.915 1.00 151.23 ?  202 THR C O   1 
ATOM   5907  C CB  . THR C  1 172 ? 114.518 71.322  244.696 1.00 145.94 ?  202 THR C CB  1 
ATOM   5908  O OG1 . THR C  1 172 ? 114.708 70.038  245.308 1.00 141.33 ?  202 THR C OG1 1 
ATOM   5909  C CG2 . THR C  1 172 ? 113.662 72.206  245.599 1.00 142.09 ?  202 THR C CG2 1 
ATOM   5910  N N   . GLN C  1 173 ? 112.954 68.891  243.106 1.00 150.17 ?  203 GLN C N   1 
ATOM   5911  C CA  . GLN C  1 173 ? 111.948 67.836  243.171 1.00 150.82 ?  203 GLN C CA  1 
ATOM   5912  C C   . GLN C  1 173 ? 111.899 67.213  244.557 1.00 149.01 ?  203 GLN C C   1 
ATOM   5913  O O   . GLN C  1 173 ? 112.939 66.900  245.141 1.00 143.17 ?  203 GLN C O   1 
ATOM   5914  C CB  . GLN C  1 173 ? 112.225 66.733  242.152 1.00 145.98 ?  203 GLN C CB  1 
ATOM   5915  C CG  . GLN C  1 173 ? 111.156 65.644  242.152 1.00 144.27 ?  203 GLN C CG  1 
ATOM   5916  C CD  . GLN C  1 173 ? 111.498 64.473  241.254 1.00 141.95 ?  203 GLN C CD  1 
ATOM   5917  O OE1 . GLN C  1 173 ? 110.622 63.897  240.610 1.00 143.95 ?  203 GLN C OE1 1 
ATOM   5918  N NE2 . GLN C  1 173 ? 112.771 64.097  241.229 1.00 137.39 ?  203 GLN C NE2 1 
ATOM   5919  N N   . ALA C  1 174 ? 110.694 67.033  245.083 1.00 157.88 ?  204 ALA C N   1 
ATOM   5920  C CA  . ALA C  1 174 ? 110.548 66.366  246.365 1.00 151.73 ?  204 ALA C CA  1 
ATOM   5921  C C   . ALA C  1 174 ? 110.913 64.892  246.237 1.00 148.82 ?  204 ALA C C   1 
ATOM   5922  O O   . ALA C  1 174 ? 110.536 64.222  245.272 1.00 151.03 ?  204 ALA C O   1 
ATOM   5923  C CB  . ALA C  1 174 ? 109.118 66.499  246.881 1.00 154.69 ?  204 ALA C CB  1 
ATOM   5924  N N   . CYS C  1 175 ? 111.657 64.390  247.210 1.00 156.06 ?  205 CYS C N   1 
ATOM   5925  C CA  . CYS C  1 175 ? 112.045 62.989  247.185 1.00 150.84 ?  205 CYS C CA  1 
ATOM   5926  C C   . CYS C  1 175 ? 110.824 62.100  247.396 1.00 152.59 ?  205 CYS C C   1 
ATOM   5927  O O   . CYS C  1 175 ? 109.962 62.410  248.223 1.00 156.96 ?  205 CYS C O   1 
ATOM   5928  C CB  . CYS C  1 175 ? 113.096 62.674  248.240 1.00 147.60 ?  205 CYS C CB  1 
ATOM   5929  S SG  . CYS C  1 175 ? 114.589 63.649  248.109 1.00 196.66 ?  205 CYS C SG  1 
ATOM   5930  N N   . PRO C  1 176 ? 110.721 60.991  246.661 1.00 161.06 ?  206 PRO C N   1 
ATOM   5931  C CA  . PRO C  1 176 ? 109.554 60.109  246.810 1.00 164.00 ?  206 PRO C CA  1 
ATOM   5932  C C   . PRO C  1 176 ? 109.585 59.287  248.082 1.00 165.58 ?  206 PRO C C   1 
ATOM   5933  O O   . PRO C  1 176 ? 108.586 58.631  248.402 1.00 171.77 ?  206 PRO C O   1 
ATOM   5934  C CB  . PRO C  1 176 ? 109.668 59.179  245.602 1.00 160.81 ?  206 PRO C CB  1 
ATOM   5935  C CG  . PRO C  1 176 ? 111.148 59.110  245.360 1.00 154.48 ?  206 PRO C CG  1 
ATOM   5936  C CD  . PRO C  1 176 ? 111.695 60.468  245.690 1.00 156.92 ?  206 PRO C CD  1 
ATOM   5937  N N   . LYS C  1 177 ? 110.707 59.294  248.802 1.00 195.82 ?  207 LYS C N   1 
ATOM   5938  C CA  . LYS C  1 177 ? 110.843 58.527  250.037 1.00 193.72 ?  207 LYS C CA  1 
ATOM   5939  C C   . LYS C  1 177 ? 110.062 59.161  251.181 1.00 195.76 ?  207 LYS C C   1 
ATOM   5940  O O   . LYS C  1 177 ? 109.433 58.457  251.979 1.00 197.05 ?  207 LYS C O   1 
ATOM   5941  C CB  . LYS C  1 177 ? 112.325 58.377  250.379 1.00 189.73 ?  207 LYS C CB  1 
ATOM   5942  C CG  . LYS C  1 177 ? 113.232 58.407  249.143 1.00 184.30 ?  207 LYS C CG  1 
ATOM   5943  C CD  . LYS C  1 177 ? 112.949 57.224  248.215 1.00 184.43 ?  207 LYS C CD  1 
ATOM   5944  C CE  . LYS C  1 177 ? 113.528 55.930  248.746 1.00 193.52 ?  207 LYS C CE  1 
ATOM   5945  N NZ  . LYS C  1 177 ? 113.328 54.811  247.784 1.00 192.79 1  207 LYS C NZ  1 
ATOM   5946  N N   . VAL C  1 178 ? 110.089 60.481  251.277 1.00 175.24 ?  208 VAL C N   1 
ATOM   5947  C CA  . VAL C  1 178 ? 109.386 61.167  252.349 1.00 177.55 ?  208 VAL C CA  1 
ATOM   5948  C C   . VAL C  1 178 ? 107.914 61.298  251.978 1.00 180.01 ?  208 VAL C C   1 
ATOM   5949  O O   . VAL C  1 178 ? 107.512 61.137  250.822 1.00 181.64 ?  208 VAL C O   1 
ATOM   5950  C CB  . VAL C  1 178 ? 110.004 62.547  252.633 1.00 178.21 ?  208 VAL C CB  1 
ATOM   5951  C CG1 . VAL C  1 178 ? 111.499 62.431  252.955 1.00 173.86 ?  208 VAL C CG1 1 
ATOM   5952  C CG2 . VAL C  1 178 ? 109.738 63.493  251.474 1.00 175.92 ?  208 VAL C CG2 1 
ATOM   5953  N N   . SER C  1 179 ? 107.092 61.568  252.982 1.00 179.91 ?  209 SER C N   1 
ATOM   5954  C CA  . SER C  1 179 ? 105.670 61.737  252.755 1.00 183.39 ?  209 SER C CA  1 
ATOM   5955  C C   . SER C  1 179 ? 105.210 63.036  253.387 1.00 186.34 ?  209 SER C C   1 
ATOM   5956  O O   . SER C  1 179 ? 105.778 63.506  254.378 1.00 183.25 ?  209 SER C O   1 
ATOM   5957  C CB  . SER C  1 179 ? 104.856 60.581  253.353 1.00 182.91 ?  209 SER C CB  1 
ATOM   5958  O OG  . SER C  1 179 ? 104.910 60.589  254.771 1.00 181.93 ?  209 SER C OG  1 
ATOM   5959  N N   . PHE C  1 180 ? 104.158 63.606  252.804 1.00 177.10 ?  210 PHE C N   1 
ATOM   5960  C CA  . PHE C  1 180 ? 103.593 64.856  253.286 1.00 176.63 ?  210 PHE C CA  1 
ATOM   5961  C C   . PHE C  1 180 ? 102.382 64.616  254.173 1.00 184.30 ?  210 PHE C C   1 
ATOM   5962  O O   . PHE C  1 180 ? 101.418 65.387  254.141 1.00 187.52 ?  210 PHE C O   1 
ATOM   5963  C CB  . PHE C  1 180 ? 103.248 65.790  252.122 1.00 178.13 ?  210 PHE C CB  1 
ATOM   5964  C CG  . PHE C  1 180 ? 104.386 66.017  251.152 1.00 175.07 ?  210 PHE C CG  1 
ATOM   5965  C CD1 . PHE C  1 180 ? 105.706 65.892  251.564 1.00 171.31 ?  210 PHE C CD1 1 
ATOM   5966  C CD2 . PHE C  1 180 ? 104.138 66.393  249.841 1.00 172.96 ?  210 PHE C CD2 1 
ATOM   5967  C CE1 . PHE C  1 180 ? 106.748 66.111  250.684 1.00 170.94 ?  210 PHE C CE1 1 
ATOM   5968  C CE2 . PHE C  1 180 ? 105.177 66.618  248.955 1.00 170.66 ?  210 PHE C CE2 1 
ATOM   5969  C CZ  . PHE C  1 180 ? 106.483 66.475  249.378 1.00 173.10 ?  210 PHE C CZ  1 
ATOM   5970  N N   . GLU C  1 181 ? 102.410 63.533  254.949 1.00 171.34 ?  211 GLU C N   1 
ATOM   5971  C CA  . GLU C  1 181 ? 101.312 63.211  255.843 1.00 179.51 ?  211 GLU C CA  1 
ATOM   5972  C C   . GLU C  1 181 ? 101.495 63.932  257.169 1.00 177.37 ?  211 GLU C C   1 
ATOM   5973  O O   . GLU C  1 181 ? 102.471 63.658  257.883 1.00 173.27 ?  211 GLU C O   1 
ATOM   5974  C CB  . GLU C  1 181 ? 101.199 61.715  256.080 1.00 183.29 ?  211 GLU C CB  1 
ATOM   5975  C CG  . GLU C  1 181 ? 99.869  61.318  256.738 1.00 190.12 ?  211 GLU C CG  1 
ATOM   5976  C CD  . GLU C  1 181 ? 98.659  61.450  255.827 1.00 198.75 ?  211 GLU C CD  1 
ATOM   5977  O OE1 . GLU C  1 181 ? 98.831  61.504  254.592 1.00 196.03 ?  211 GLU C OE1 1 
ATOM   5978  O OE2 . GLU C  1 181 ? 97.527  61.513  256.357 1.00 206.58 -1 211 GLU C OE2 1 
ATOM   5979  N N   . PRO C  1 182 ? 100.607 64.856  257.523 1.00 167.05 ?  212 PRO C N   1 
ATOM   5980  C CA  . PRO C  1 182 ? 100.748 65.597  258.784 1.00 166.69 ?  212 PRO C CA  1 
ATOM   5981  C C   . PRO C  1 182 ? 100.627 64.635  259.954 1.00 172.61 ?  212 PRO C C   1 
ATOM   5982  O O   . PRO C  1 182 ? 99.584  64.012  260.164 1.00 176.54 ?  212 PRO C O   1 
ATOM   5983  C CB  . PRO C  1 182 ? 99.595  66.607  258.734 1.00 164.59 ?  212 PRO C CB  1 
ATOM   5984  C CG  . PRO C  1 182 ? 99.211  66.683  257.284 1.00 159.25 ?  212 PRO C CG  1 
ATOM   5985  C CD  . PRO C  1 182 ? 99.447  65.313  256.744 1.00 169.22 ?  212 PRO C CD  1 
ATOM   5986  N N   . ILE C  1 183 ? 101.707 64.506  260.717 1.00 164.34 ?  213 ILE C N   1 
ATOM   5987  C CA  . ILE C  1 183 ? 101.681 63.614  261.872 1.00 168.43 ?  213 ILE C CA  1 
ATOM   5988  C C   . ILE C  1 183 ? 101.679 64.420  263.168 1.00 168.58 ?  213 ILE C C   1 
ATOM   5989  O O   . ILE C  1 183 ? 102.287 65.498  263.239 1.00 167.45 ?  213 ILE C O   1 
ATOM   5990  C CB  . ILE C  1 183 ? 102.864 62.632  261.810 1.00 165.08 ?  213 ILE C CB  1 
ATOM   5991  C CG1 . ILE C  1 183 ? 104.180 63.383  261.589 1.00 163.56 ?  213 ILE C CG1 1 
ATOM   5992  C CG2 . ILE C  1 183 ? 102.651 61.620  260.687 1.00 167.95 ?  213 ILE C CG2 1 
ATOM   5993  C CD1 . ILE C  1 183 ? 105.383 62.473  261.445 1.00 167.49 ?  213 ILE C CD1 1 
ATOM   5994  N N   . PRO C  1 184 ? 100.996 63.928  264.207 1.00 150.39 ?  214 PRO C N   1 
ATOM   5995  C CA  . PRO C  1 184 ? 100.892 64.664  265.481 1.00 149.56 ?  214 PRO C CA  1 
ATOM   5996  C C   . PRO C  1 184 ? 102.232 65.047  266.099 1.00 149.14 ?  214 PRO C C   1 
ATOM   5997  O O   . PRO C  1 184 ? 103.122 64.210  266.264 1.00 148.89 ?  214 PRO C O   1 
ATOM   5998  C CB  . PRO C  1 184 ? 100.126 63.685  266.379 1.00 151.83 ?  214 PRO C CB  1 
ATOM   5999  C CG  . PRO C  1 184 ? 99.327  62.850  265.428 1.00 151.30 ?  214 PRO C CG  1 
ATOM   6000  C CD  . PRO C  1 184 ? 100.198 62.689  264.215 1.00 152.91 ?  214 PRO C CD  1 
ATOM   6001  N N   . ILE C  1 185 ? 102.368 66.333  266.440 1.00 147.95 ?  215 ILE C N   1 
ATOM   6002  C CA  . ILE C  1 185 ? 103.580 66.863  267.059 1.00 147.25 ?  215 ILE C CA  1 
ATOM   6003  C C   . ILE C  1 185 ? 103.257 67.595  268.362 1.00 147.61 ?  215 ILE C C   1 
ATOM   6004  O O   . ILE C  1 185 ? 102.543 68.606  268.348 1.00 147.89 ?  215 ILE C O   1 
ATOM   6005  C CB  . ILE C  1 185 ? 104.320 67.814  266.103 1.00 146.43 ?  215 ILE C CB  1 
ATOM   6006  C CG1 . ILE C  1 185 ? 104.769 67.066  264.849 1.00 146.05 ?  215 ILE C CG1 1 
ATOM   6007  C CG2 . ILE C  1 185 ? 105.505 68.461  266.797 1.00 145.82 ?  215 ILE C CG2 1 
ATOM   6008  C CD1 . ILE C  1 185 ? 105.528 67.923  263.859 1.00 145.38 ?  215 ILE C CD1 1 
ATOM   6009  N N   . HIS C  1 186 ? 103.773 67.086  269.483 1.00 156.67 ?  216 HIS C N   1 
ATOM   6010  C CA  . HIS C  1 186 ? 103.600 67.718  270.790 1.00 155.94 ?  216 HIS C CA  1 
ATOM   6011  C C   . HIS C  1 186 ? 104.738 68.697  271.070 1.00 153.39 ?  216 HIS C C   1 
ATOM   6012  O O   . HIS C  1 186 ? 105.912 68.315  271.024 1.00 153.54 ?  216 HIS C O   1 
ATOM   6013  C CB  . HIS C  1 186 ? 103.508 66.710  271.942 1.00 158.10 ?  216 HIS C CB  1 
ATOM   6014  C CG  . HIS C  1 186 ? 102.444 65.670  271.781 1.00 159.85 ?  216 HIS C CG  1 
ATOM   6015  N ND1 . HIS C  1 186 ? 101.258 65.723  272.482 1.00 159.92 ?  216 HIS C ND1 1 
ATOM   6016  C CD2 . HIS C  1 186 ? 102.383 64.552  271.022 1.00 162.58 ?  216 HIS C CD2 1 
ATOM   6017  C CE1 . HIS C  1 186 ? 100.511 64.683  272.161 1.00 161.22 ?  216 HIS C CE1 1 
ATOM   6018  N NE2 . HIS C  1 186 ? 101.167 63.959  271.272 1.00 163.22 ?  216 HIS C NE2 1 
ATOM   6019  N N   . TYR C  1 187 ? 104.400 69.946  271.368 1.00 151.82 ?  217 TYR C N   1 
ATOM   6020  C CA  . TYR C  1 187 ? 105.404 70.942  271.734 1.00 148.58 ?  217 TYR C CA  1 
ATOM   6021  C C   . TYR C  1 187 ? 105.563 70.957  273.253 1.00 150.53 ?  217 TYR C C   1 
ATOM   6022  O O   . TYR C  1 187 ? 104.570 71.085  273.975 1.00 150.41 ?  217 TYR C O   1 
ATOM   6023  C CB  . TYR C  1 187 ? 105.033 72.331  271.206 1.00 147.76 ?  217 TYR C CB  1 
ATOM   6024  C CG  . TYR C  1 187 ? 105.480 72.579  269.780 1.00 149.23 ?  217 TYR C CG  1 
ATOM   6025  C CD1 . TYR C  1 187 ? 104.717 72.157  268.701 1.00 155.58 ?  217 TYR C CD1 1 
ATOM   6026  C CD2 . TYR C  1 187 ? 106.666 73.260  269.517 1.00 144.36 ?  217 TYR C CD2 1 
ATOM   6027  C CE1 . TYR C  1 187 ? 105.131 72.388  267.399 1.00 151.57 ?  217 TYR C CE1 1 
ATOM   6028  C CE2 . TYR C  1 187 ? 107.087 73.498  268.217 1.00 140.22 ?  217 TYR C CE2 1 
ATOM   6029  C CZ  . TYR C  1 187 ? 106.314 73.060  267.163 1.00 144.78 ?  217 TYR C CZ  1 
ATOM   6030  O OH  . TYR C  1 187 ? 106.722 73.290  265.869 1.00 146.62 ?  217 TYR C OH  1 
ATOM   6031  N N   . CYS C  1 188 ? 106.811 70.834  273.735 1.00 145.34 ?  218 CYS C N   1 
ATOM   6032  C CA  . CYS C  1 188 ? 107.098 70.761  275.167 1.00 145.80 ?  218 CYS C CA  1 
ATOM   6033  C C   . CYS C  1 188 ? 108.046 71.876  275.588 1.00 143.45 ?  218 CYS C C   1 
ATOM   6034  O O   . CYS C  1 188 ? 108.781 72.436  274.770 1.00 145.59 ?  218 CYS C O   1 
ATOM   6035  C CB  . CYS C  1 188 ? 107.748 69.429  275.574 1.00 149.03 ?  218 CYS C CB  1 
ATOM   6036  S SG  . CYS C  1 188 ? 106.752 68.057  275.037 1.00 159.59 ?  218 CYS C SG  1 
ATOM   6037  N N   . ALA C  1 189 ? 108.017 72.201  276.919 1.00 140.25 ?  219 ALA C N   1 
ATOM   6038  C CA  . ALA C  1 189 ? 108.876 73.239  277.482 1.00 137.80 ?  219 ALA C CA  1 
ATOM   6039  C C   . ALA C  1 189 ? 109.998 72.659  278.343 1.00 137.87 ?  219 ALA C C   1 
ATOM   6040  O O   . ALA C  1 189 ? 109.787 71.680  279.066 1.00 139.76 ?  219 ALA C O   1 
ATOM   6041  C CB  . ALA C  1 189 ? 108.059 74.218  278.336 1.00 136.78 ?  219 ALA C CB  1 
ATOM   6042  N N   . PRO C  1 190 ? 111.212 73.243  278.265 1.00 135.44 ?  220 PRO C N   1 
ATOM   6043  C CA  . PRO C  1 190 ? 112.354 72.746  279.053 1.00 136.80 ?  220 PRO C CA  1 
ATOM   6044  C C   . PRO C  1 190 ? 112.217 72.932  280.557 1.00 135.83 ?  220 PRO C C   1 
ATOM   6045  O O   . PRO C  1 190 ? 111.237 73.510  281.038 1.00 134.17 ?  220 PRO C O   1 
ATOM   6046  C CB  . PRO C  1 190 ? 113.531 73.568  278.513 1.00 132.91 ?  220 PRO C CB  1 
ATOM   6047  C CG  . PRO C  1 190 ? 112.909 74.807  277.976 1.00 127.93 ?  220 PRO C CG  1 
ATOM   6048  C CD  . PRO C  1 190 ? 111.590 74.376  277.405 1.00 134.30 ?  220 PRO C CD  1 
ATOM   6049  N N   . ALA C  1 191 ? 113.204 72.433  281.303 1.00 145.59 ?  221 ALA C N   1 
ATOM   6050  C CA  . ALA C  1 191 ? 113.185 72.539  282.757 1.00 140.24 ?  221 ALA C CA  1 
ATOM   6051  C C   . ALA C  1 191 ? 113.193 74.000  283.185 1.00 134.70 ?  221 ALA C C   1 
ATOM   6052  O O   . ALA C  1 191 ? 113.879 74.837  282.591 1.00 133.61 ?  221 ALA C O   1 
ATOM   6053  C CB  . ALA C  1 191 ? 114.387 71.814  283.361 1.00 140.89 ?  221 ALA C CB  1 
ATOM   6054  N N   . GLY C  1 192 ? 112.428 74.306  284.230 1.00 151.82 ?  222 GLY C N   1 
ATOM   6055  C CA  . GLY C  1 192 ? 112.324 75.660  284.719 1.00 144.06 ?  222 GLY C CA  1 
ATOM   6056  C C   . GLY C  1 192 ? 111.211 76.454  284.081 1.00 144.64 ?  222 GLY C C   1 
ATOM   6057  O O   . GLY C  1 192 ? 110.894 77.549  284.558 1.00 141.53 ?  222 GLY C O   1 
ATOM   6058  N N   . PHE C  1 193 ? 110.646 75.948  282.992 1.00 145.44 ?  223 PHE C N   1 
ATOM   6059  C CA  . PHE C  1 193 ? 109.542 76.538  282.255 1.00 141.16 ?  223 PHE C CA  1 
ATOM   6060  C C   . PHE C  1 193 ? 108.318 75.634  282.370 1.00 144.18 ?  223 PHE C C   1 
ATOM   6061  O O   . PHE C  1 193 ? 108.405 74.492  282.826 1.00 150.57 ?  223 PHE C O   1 
ATOM   6062  C CB  . PHE C  1 193 ? 109.952 76.752  280.795 1.00 138.48 ?  223 PHE C CB  1 
ATOM   6063  C CG  . PHE C  1 193 ? 111.049 77.770  280.624 1.00 136.34 ?  223 PHE C CG  1 
ATOM   6064  C CD1 . PHE C  1 193 ? 112.382 77.396  280.739 1.00 136.31 ?  223 PHE C CD1 1 
ATOM   6065  C CD2 . PHE C  1 193 ? 110.753 79.094  280.349 1.00 130.23 ?  223 PHE C CD2 1 
ATOM   6066  C CE1 . PHE C  1 193 ? 113.396 78.326  280.591 1.00 135.56 ?  223 PHE C CE1 1 
ATOM   6067  C CE2 . PHE C  1 193 ? 111.764 80.029  280.195 1.00 131.29 ?  223 PHE C CE2 1 
ATOM   6068  C CZ  . PHE C  1 193 ? 113.087 79.643  280.317 1.00 131.08 ?  223 PHE C CZ  1 
ATOM   6069  N N   . ALA C  1 194 ? 107.167 76.154  281.944 1.00 129.56 ?  224 ALA C N   1 
ATOM   6070  C CA  . ALA C  1 194 ? 105.929 75.384  281.967 1.00 130.75 ?  224 ALA C CA  1 
ATOM   6071  C C   . ALA C  1 194 ? 104.977 75.961  280.929 1.00 131.31 ?  224 ALA C C   1 
ATOM   6072  O O   . ALA C  1 194 ? 105.097 77.123  280.535 1.00 130.96 ?  224 ALA C O   1 
ATOM   6073  C CB  . ALA C  1 194 ? 105.285 75.395  283.358 1.00 131.39 ?  224 ALA C CB  1 
ATOM   6074  N N   . ILE C  1 195 ? 104.032 75.130  280.486 1.00 135.44 ?  225 ILE C N   1 
ATOM   6075  C CA  . ILE C  1 195 ? 103.022 75.534  279.512 1.00 135.98 ?  225 ILE C CA  1 
ATOM   6076  C C   . ILE C  1 195 ? 101.652 75.472  280.168 1.00 137.35 ?  225 ILE C C   1 
ATOM   6077  O O   . ILE C  1 195 ? 101.227 74.402  280.625 1.00 147.57 ?  225 ILE C O   1 
ATOM   6078  C CB  . ILE C  1 195 ? 103.042 74.619  278.276 1.00 137.64 ?  225 ILE C CB  1 
ATOM   6079  C CG1 . ILE C  1 195 ? 104.422 74.622  277.621 1.00 136.86 ?  225 ILE C CG1 1 
ATOM   6080  C CG2 . ILE C  1 195 ? 101.971 75.045  277.277 1.00 136.79 ?  225 ILE C CG2 1 
ATOM   6081  C CD1 . ILE C  1 195 ? 104.502 73.754  276.386 1.00 139.02 ?  225 ILE C CD1 1 
ATOM   6082  N N   . LEU C  1 196 ? 100.968 76.611  280.228 1.00 131.63 ?  226 LEU C N   1 
ATOM   6083  C CA  . LEU C  1 196 ? 99.638  76.671  280.815 1.00 133.08 ?  226 LEU C CA  1 
ATOM   6084  C C   . LEU C  1 196 ? 98.596  76.388  279.739 1.00 134.11 ?  226 LEU C C   1 
ATOM   6085  O O   . LEU C  1 196 ? 98.764  76.793  278.586 1.00 133.75 ?  226 LEU C O   1 
ATOM   6086  C CB  . LEU C  1 196 ? 99.400  78.044  281.441 1.00 133.24 ?  226 LEU C CB  1 
ATOM   6087  C CG  . LEU C  1 196 ? 100.510 78.427  282.420 1.00 132.06 ?  226 LEU C CG  1 
ATOM   6088  C CD1 . LEU C  1 196 ? 100.235 79.760  283.090 1.00 132.26 ?  226 LEU C CD1 1 
ATOM   6089  C CD2 . LEU C  1 196 ? 100.700 77.333  283.450 1.00 132.12 ?  226 LEU C CD2 1 
ATOM   6090  N N   . LYS C  1 197 ? 97.524  75.685  280.112 1.00 139.03 ?  227 LYS C N   1 
ATOM   6091  C CA  . LYS C  1 197 ? 96.469  75.314  279.170 1.00 140.00 ?  227 LYS C CA  1 
ATOM   6092  C C   . LYS C  1 197 ? 95.099  75.729  279.703 1.00 143.61 ?  227 LYS C C   1 
ATOM   6093  O O   . LYS C  1 197 ? 94.720  75.319  280.806 1.00 152.75 ?  227 LYS C O   1 
ATOM   6094  C CB  . LYS C  1 197 ? 96.509  73.808  278.886 1.00 144.00 ?  227 LYS C CB  1 
ATOM   6095  C CG  . LYS C  1 197 ? 95.483  73.340  277.873 1.00 155.02 ?  227 LYS C CG  1 
ATOM   6096  C CD  . LYS C  1 197 ? 95.643  71.866  277.557 1.00 157.89 ?  227 LYS C CD  1 
ATOM   6097  C CE  . LYS C  1 197 ? 94.518  71.056  278.158 1.00 155.79 ?  227 LYS C CE  1 
ATOM   6098  N NZ  . LYS C  1 197 ? 94.103  69.979  277.222 1.00 166.45 1  227 LYS C NZ  1 
ATOM   6099  N N   . CYS C  1 198 ? 94.351  76.523  278.919 1.00 142.70 ?  228 CYS C N   1 
ATOM   6100  C CA  . CYS C  1 198 ? 93.006  76.953  279.306 1.00 144.53 ?  228 CYS C CA  1 
ATOM   6101  C C   . CYS C  1 198 ? 91.993  75.870  278.943 1.00 145.87 ?  228 CYS C C   1 
ATOM   6102  O O   . CYS C  1 198 ? 91.886  75.497  277.769 1.00 145.74 ?  228 CYS C O   1 
ATOM   6103  C CB  . CYS C  1 198 ? 92.654  78.238  278.566 1.00 144.91 ?  228 CYS C CB  1 
ATOM   6104  S SG  . CYS C  1 198 ? 91.399  79.326  279.254 1.00 146.88 ?  228 CYS C SG  1 
ATOM   6105  N N   . LYS C  1 199 ? 91.248  75.354  279.932 1.00 166.39 ?  229 LYS C N   1 
ATOM   6106  C CA  . LYS C  1 199 ? 90.307  74.258  279.691 1.00 168.19 ?  229 LYS C CA  1 
ATOM   6107  C C   . LYS C  1 199 ? 88.857  74.663  279.962 1.00 171.84 ?  229 LYS C C   1 
ATOM   6108  O O   . LYS C  1 199 ? 88.047  73.819  280.359 1.00 173.79 ?  229 LYS C O   1 
ATOM   6109  C CB  . LYS C  1 199 ? 90.644  72.946  280.405 1.00 167.46 ?  229 LYS C CB  1 
ATOM   6110  C CG  . LYS C  1 199 ? 91.091  72.886  281.832 1.00 167.00 ?  229 LYS C CG  1 
ATOM   6111  C CD  . LYS C  1 199 ? 91.795  71.537  281.968 1.00 165.73 ?  229 LYS C CD  1 
ATOM   6112  C CE  . LYS C  1 199 ? 92.085  71.159  283.400 1.00 165.86 ?  229 LYS C CE  1 
ATOM   6113  N NZ  . LYS C  1 199 ? 90.834  71.071  284.200 1.00 168.95 1  229 LYS C NZ  1 
ATOM   6114  N N   . ASP C  1 200 ? 88.502  75.932  279.764 1.00 193.43 ?  230 ASP C N   1 
ATOM   6115  C CA  . ASP C  1 200 ? 87.107  76.326  279.899 1.00 199.31 ?  230 ASP C CA  1 
ATOM   6116  C C   . ASP C  1 200 ? 86.431  76.108  278.559 1.00 198.66 ?  230 ASP C C   1 
ATOM   6117  O O   . ASP C  1 200 ? 87.050  76.191  277.497 1.00 196.82 ?  230 ASP C O   1 
ATOM   6118  C CB  . ASP C  1 200 ? 86.913  77.779  280.344 1.00 199.27 ?  230 ASP C CB  1 
ATOM   6119  C CG  . ASP C  1 200 ? 87.765  78.762  279.570 1.00 197.24 ?  230 ASP C CG  1 
ATOM   6120  O OD1 . ASP C  1 200 ? 88.424  78.361  278.590 1.00 195.19 ?  230 ASP C OD1 1 
ATOM   6121  O OD2 . ASP C  1 200 ? 87.725  79.962  279.919 1.00 199.96 -1 230 ASP C OD2 1 
ATOM   6122  N N   . LYS C  1 201 ? 85.149  75.818  278.621 1.00 202.04 ?  231 LYS C N   1 
ATOM   6123  C CA  . LYS C  1 201 ? 84.453  75.470  277.402 1.00 203.49 ?  231 LYS C CA  1 
ATOM   6124  C C   . LYS C  1 201 ? 84.137  76.674  276.515 1.00 205.04 ?  231 LYS C C   1 
ATOM   6125  O O   . LYS C  1 201 ? 83.873  76.485  275.324 1.00 208.20 ?  231 LYS C O   1 
ATOM   6126  C CB  . LYS C  1 201 ? 83.213  74.706  277.837 1.00 207.00 ?  231 LYS C CB  1 
ATOM   6127  C CG  . LYS C  1 201 ? 83.651  73.572  278.772 1.00 205.64 ?  231 LYS C CG  1 
ATOM   6128  C CD  . LYS C  1 201 ? 83.166  72.195  278.472 1.00 206.77 ?  231 LYS C CD  1 
ATOM   6129  C CE  . LYS C  1 201 ? 83.859  71.248  279.435 1.00 204.30 ?  231 LYS C CE  1 
ATOM   6130  N NZ  . LYS C  1 201 ? 85.306  71.152  279.135 1.00 200.24 1  231 LYS C NZ  1 
ATOM   6131  N N   . LYS C  1 202 ? 84.112  77.895  277.057 1.00 201.13 ?  232 LYS C N   1 
ATOM   6132  C CA  . LYS C  1 202 ? 83.878  79.095  276.253 1.00 202.93 ?  232 LYS C CA  1 
ATOM   6133  C C   . LYS C  1 202 ? 85.028  80.070  276.481 1.00 200.69 ?  232 LYS C C   1 
ATOM   6134  O O   . LYS C  1 202 ? 85.172  80.622  277.578 1.00 200.93 ?  232 LYS C O   1 
ATOM   6135  C CB  . LYS C  1 202 ? 82.521  79.764  276.503 1.00 209.90 ?  232 LYS C CB  1 
ATOM   6136  C CG  . LYS C  1 202 ? 82.114  80.121  277.911 1.00 211.10 ?  232 LYS C CG  1 
ATOM   6137  C CD  . LYS C  1 202 ? 80.711  80.727  277.831 1.00 218.55 ?  232 LYS C CD  1 
ATOM   6138  C CE  . LYS C  1 202 ? 79.655  79.905  278.540 1.00 218.71 ?  232 LYS C CE  1 
ATOM   6139  N NZ  . LYS C  1 202 ? 79.867  79.889  280.007 1.00 224.89 1  232 LYS C NZ  1 
ATOM   6140  N N   . PHE C  1 203 ? 85.861  80.259  275.460 1.00 193.57 ?  233 PHE C N   1 
ATOM   6141  C CA  . PHE C  1 203 ? 87.029  81.132  275.564 1.00 191.48 ?  233 PHE C CA  1 
ATOM   6142  C C   . PHE C  1 203 ? 87.436  81.615  274.184 1.00 191.23 ?  233 PHE C C   1 
ATOM   6143  O O   . PHE C  1 203 ? 87.775  80.800  273.319 1.00 189.26 ?  233 PHE C O   1 
ATOM   6144  C CB  . PHE C  1 203 ? 88.190  80.397  276.221 1.00 187.41 ?  233 PHE C CB  1 
ATOM   6145  C CG  . PHE C  1 203 ? 89.378  81.268  276.494 1.00 185.43 ?  233 PHE C CG  1 
ATOM   6146  C CD1 . PHE C  1 203 ? 89.266  82.390  277.296 1.00 187.03 ?  233 PHE C CD1 1 
ATOM   6147  C CD2 . PHE C  1 203 ? 90.613  80.962  275.942 1.00 182.08 ?  233 PHE C CD2 1 
ATOM   6148  C CE1 . PHE C  1 203 ? 90.364  83.193  277.543 1.00 185.25 ?  233 PHE C CE1 1 
ATOM   6149  C CE2 . PHE C  1 203 ? 91.715  81.758  276.188 1.00 180.43 ?  233 PHE C CE2 1 
ATOM   6150  C CZ  . PHE C  1 203 ? 91.590  82.877  276.988 1.00 181.98 ?  233 PHE C CZ  1 
ATOM   6151  N N   . ASN C  1 204 ? 87.420  82.938  273.984 1.00 193.58 ?  234 ASN C N   1 
ATOM   6152  C CA  . ASN C  1 204 ? 87.742  83.537  272.697 1.00 194.01 ?  234 ASN C CA  1 
ATOM   6153  C C   . ASN C  1 204 ? 89.235  83.790  272.516 1.00 190.65 ?  234 ASN C C   1 
ATOM   6154  O O   . ASN C  1 204 ? 89.610  84.598  271.659 1.00 191.44 ?  234 ASN C O   1 
ATOM   6155  C CB  . ASN C  1 204 ? 87.007  84.868  272.509 1.00 198.55 ?  234 ASN C CB  1 
ATOM   6156  C CG  . ASN C  1 204 ? 87.248  85.842  273.656 1.00 199.37 ?  234 ASN C CG  1 
ATOM   6157  O OD1 . ASN C  1 204 ? 88.008  85.559  274.583 1.00 196.40 ?  234 ASN C OD1 1 
ATOM   6158  N ND2 . ASN C  1 204 ? 86.630  87.017  273.569 1.00 203.56 ?  234 ASN C ND2 1 
ATOM   6159  N N   . GLY C  1 205 ? 90.093  83.137  273.298 1.00 176.70 ?  235 GLY C N   1 
ATOM   6160  C CA  . GLY C  1 205 ? 91.520  83.285  273.114 1.00 173.65 ?  235 GLY C CA  1 
ATOM   6161  C C   . GLY C  1 205 ? 92.150  84.488  273.782 1.00 174.03 ?  235 GLY C C   1 
ATOM   6162  O O   . GLY C  1 205 ? 93.383  84.541  273.882 1.00 171.42 ?  235 GLY C O   1 
ATOM   6163  N N   . THR C  1 206 ? 91.361  85.464  274.232 1.00 178.64 ?  236 THR C N   1 
ATOM   6164  C CA  . THR C  1 206 ? 91.905  86.667  274.846 1.00 179.25 ?  236 THR C CA  1 
ATOM   6165  C C   . THR C  1 206 ? 91.202  86.938  276.167 1.00 180.71 ?  236 THR C C   1 
ATOM   6166  O O   . THR C  1 206 ? 89.972  86.861  276.247 1.00 183.67 ?  236 THR C O   1 
ATOM   6167  C CB  . THR C  1 206 ? 91.726  87.878  273.918 1.00 182.61 ?  236 THR C CB  1 
ATOM   6168  O OG1 . THR C  1 206 ? 90.377  87.917  273.431 1.00 186.18 ?  236 THR C OG1 1 
ATOM   6169  C CG2 . THR C  1 206 ? 92.668  87.791  272.735 1.00 181.06 ?  236 THR C CG2 1 
ATOM   6170  N N   . GLY C  1 207 ? 91.980  87.263  277.196 1.00 162.33 ?  237 GLY C N   1 
ATOM   6171  C CA  . GLY C  1 207 ? 91.422  87.558  278.493 1.00 163.19 ?  237 GLY C CA  1 
ATOM   6172  C C   . GLY C  1 207 ? 91.809  86.586  279.590 1.00 162.08 ?  237 GLY C C   1 
ATOM   6173  O O   . GLY C  1 207 ? 92.569  85.633  279.391 1.00 160.59 ?  237 GLY C O   1 
ATOM   6174  N N   . PRO C  1 208 ? 91.286  86.836  280.786 1.00 160.49 ?  238 PRO C N   1 
ATOM   6175  C CA  . PRO C  1 208 ? 91.565  85.955  281.928 1.00 158.04 ?  238 PRO C CA  1 
ATOM   6176  C C   . PRO C  1 208 ? 90.840  84.621  281.788 1.00 158.18 ?  238 PRO C C   1 
ATOM   6177  O O   . PRO C  1 208 ? 89.717  84.559  281.283 1.00 161.17 ?  238 PRO C O   1 
ATOM   6178  C CB  . PRO C  1 208 ? 91.057  86.766  283.125 1.00 159.92 ?  238 PRO C CB  1 
ATOM   6179  C CG  . PRO C  1 208 ? 89.988  87.635  282.554 1.00 164.25 ?  238 PRO C CG  1 
ATOM   6180  C CD  . PRO C  1 208 ? 90.448  87.986  281.163 1.00 164.27 ?  238 PRO C CD  1 
ATOM   6181  N N   . CYS C  1 209 ? 91.497  83.541  282.225 1.00 168.48 ?  239 CYS C N   1 
ATOM   6182  C CA  . CYS C  1 209 ? 90.911  82.202  282.137 1.00 168.57 ?  239 CYS C CA  1 
ATOM   6183  C C   . CYS C  1 209 ? 90.581  81.656  283.521 1.00 168.62 ?  239 CYS C C   1 
ATOM   6184  O O   . CYS C  1 209 ? 91.473  81.561  284.379 1.00 166.23 ?  239 CYS C O   1 
ATOM   6185  C CB  . CYS C  1 209 ? 91.872  81.256  281.408 1.00 165.59 ?  239 CYS C CB  1 
ATOM   6186  S SG  . CYS C  1 209 ? 91.318  79.523  281.291 1.00 165.69 ?  239 CYS C SG  1 
ATOM   6187  N N   . PRO C  1 210 ? 89.310  81.300  283.788 1.00 178.50 ?  240 PRO C N   1 
ATOM   6188  C CA  . PRO C  1 210 ? 88.938  80.774  285.114 1.00 178.98 ?  240 PRO C CA  1 
ATOM   6189  C C   . PRO C  1 210 ? 89.554  79.429  285.491 1.00 176.61 ?  240 PRO C C   1 
ATOM   6190  O O   . PRO C  1 210 ? 90.120  79.294  286.583 1.00 175.10 ?  240 PRO C O   1 
ATOM   6191  C CB  . PRO C  1 210 ? 87.407  80.674  285.028 1.00 183.07 ?  240 PRO C CB  1 
ATOM   6192  C CG  . PRO C  1 210 ? 87.019  81.623  283.934 1.00 184.97 ?  240 PRO C CG  1 
ATOM   6193  C CD  . PRO C  1 210 ? 88.132  81.542  282.938 1.00 181.91 ?  240 PRO C CD  1 
ATOM   6194  N N   . SER C  1 211 ? 89.456  78.428  284.605 1.00 179.14 ?  241 SER C N   1 
ATOM   6195  C CA  . SER C  1 211 ? 89.969  77.077  284.860 1.00 177.44 ?  241 SER C CA  1 
ATOM   6196  C C   . SER C  1 211 ? 91.229  76.834  284.030 1.00 174.25 ?  241 SER C C   1 
ATOM   6197  O O   . SER C  1 211 ? 91.151  76.447  282.860 1.00 174.15 ?  241 SER C O   1 
ATOM   6198  C CB  . SER C  1 211 ? 88.898  76.035  284.546 1.00 179.88 ?  241 SER C CB  1 
ATOM   6199  O OG  . SER C  1 211 ? 87.726  76.252  285.314 1.00 181.21 ?  241 SER C OG  1 
ATOM   6200  N N   . VAL C  1 212 ? 92.386  77.049  284.655 1.00 155.94 ?  242 VAL C N   1 
ATOM   6201  C CA  . VAL C  1 212 ? 93.700  76.900  284.035 1.00 153.94 ?  242 VAL C CA  1 
ATOM   6202  C C   . VAL C  1 212 ? 94.424  75.680  284.589 1.00 153.33 ?  242 VAL C C   1 
ATOM   6203  O O   . VAL C  1 212 ? 94.394  75.425  285.799 1.00 153.76 ?  242 VAL C O   1 
ATOM   6204  C CB  . VAL C  1 212 ? 94.565  78.160  284.240 1.00 152.61 ?  242 VAL C CB  1 
ATOM   6205  C CG1 . VAL C  1 212 ? 95.900  78.033  283.495 1.00 150.71 ?  242 VAL C CG1 1 
ATOM   6206  C CG2 . VAL C  1 212 ? 93.810  79.398  283.800 1.00 153.48 ?  242 VAL C CG2 1 
ATOM   6207  N N   . SER C  1 213 ? 95.061  74.922  283.698 1.00 145.47 ?  243 SER C N   1 
ATOM   6208  C CA  . SER C  1 213 ? 95.874  73.780  284.083 1.00 144.86 ?  243 SER C CA  1 
ATOM   6209  C C   . SER C  1 213 ? 97.209  73.898  283.363 1.00 142.99 ?  243 SER C C   1 
ATOM   6210  O O   . SER C  1 213 ? 97.321  74.544  282.319 1.00 142.41 ?  243 SER C O   1 
ATOM   6211  C CB  . SER C  1 213 ? 95.207  72.439  283.750 1.00 146.08 ?  243 SER C CB  1 
ATOM   6212  O OG  . SER C  1 213 ? 94.974  72.291  282.360 1.00 145.96 ?  243 SER C OG  1 
ATOM   6213  N N   . THR C  1 214 ? 98.227  73.276  283.939 1.00 141.89 ?  244 THR C N   1 
ATOM   6214  C CA  . THR C  1 214 ? 99.568  73.292  283.381 1.00 140.24 ?  244 THR C CA  1 
ATOM   6215  C C   . THR C  1 214 ? 99.943  71.924  282.838 1.00 140.24 ?  244 THR C C   1 
ATOM   6216  O O   . THR C  1 214 ? 99.531  70.884  283.363 1.00 141.29 ?  244 THR C O   1 
ATOM   6217  C CB  . THR C  1 214 ? 100.619 73.736  284.399 1.00 139.18 ?  244 THR C CB  1 
ATOM   6218  O OG1 . THR C  1 214 ? 101.919 73.644  283.801 1.00 137.76 ?  244 THR C OG1 1 
ATOM   6219  C CG2 . THR C  1 214 ? 100.578 72.850  285.623 1.00 139.89 ?  244 THR C CG2 1 
ATOM   6220  N N   . VAL C  1 215 ? 100.732 71.940  281.770 1.00 146.47 ?  245 VAL C N   1 
ATOM   6221  C CA  . VAL C  1 215 ? 101.228 70.722  281.157 1.00 147.44 ?  245 VAL C CA  1 
ATOM   6222  C C   . VAL C  1 215 ? 102.677 70.957  280.780 1.00 148.02 ?  245 VAL C C   1 
ATOM   6223  O O   . VAL C  1 215 ? 103.147 72.093  280.674 1.00 146.38 ?  245 VAL C O   1 
ATOM   6224  C CB  . VAL C  1 215 ? 100.444 70.305  279.890 1.00 148.00 ?  245 VAL C CB  1 
ATOM   6225  C CG1 . VAL C  1 215 ? 99.061  69.817  280.244 1.00 147.86 ?  245 VAL C CG1 1 
ATOM   6226  C CG2 . VAL C  1 215 ? 100.392 71.451  278.882 1.00 146.40 ?  245 VAL C CG2 1 
ATOM   6227  N N   . GLN C  1 216 ? 103.379 69.853  280.569 1.00 156.53 ?  246 GLN C N   1 
ATOM   6228  C CA  . GLN C  1 216 ? 104.763 69.914  280.143 1.00 157.47 ?  246 GLN C CA  1 
ATOM   6229  C C   . GLN C  1 216 ? 104.780 69.876  278.622 1.00 158.94 ?  246 GLN C C   1 
ATOM   6230  O O   . GLN C  1 216 ? 105.571 70.586  277.992 1.00 156.93 ?  246 GLN C O   1 
ATOM   6231  C CB  . GLN C  1 216 ? 105.566 68.759  280.746 1.00 160.04 ?  246 GLN C CB  1 
ATOM   6232  C CG  . GLN C  1 216 ? 107.070 68.842  280.514 1.00 160.04 ?  246 GLN C CG  1 
ATOM   6233  C CD  . GLN C  1 216 ? 107.700 70.038  281.231 1.00 158.78 ?  246 GLN C CD  1 
ATOM   6234  O OE1 . GLN C  1 216 ? 107.189 70.503  282.253 1.00 161.08 ?  246 GLN C OE1 1 
ATOM   6235  N NE2 . GLN C  1 216 ? 108.829 70.515  280.717 1.00 154.69 ?  246 GLN C NE2 1 
ATOM   6236  N N   . CYS C  1 217 ? 103.878 69.065  278.045 1.00 165.51 ?  247 CYS C N   1 
ATOM   6237  C CA  . CYS C  1 217 ? 103.695 68.882  276.607 1.00 165.30 ?  247 CYS C CA  1 
ATOM   6238  C C   . CYS C  1 217 ? 102.239 69.034  276.205 1.00 163.74 ?  247 CYS C C   1 
ATOM   6239  O O   . CYS C  1 217 ? 101.340 68.487  276.855 1.00 164.33 ?  247 CYS C O   1 
ATOM   6240  C CB  . CYS C  1 217 ? 104.178 67.507  276.124 1.00 165.02 ?  247 CYS C CB  1 
ATOM   6241  S SG  . CYS C  1 217 ? 105.852 67.147  276.611 1.00 176.97 ?  247 CYS C SG  1 
ATOM   6242  N N   . THR C  1 218 ? 102.027 69.799  275.138 1.00 138.18 ?  248 THR C N   1 
ATOM   6243  C CA  . THR C  1 218 ? 100.721 70.026  274.554 1.00 139.07 ?  248 THR C CA  1 
ATOM   6244  C C   . THR C  1 218 ? 100.222 68.758  273.864 1.00 139.68 ?  248 THR C C   1 
ATOM   6245  O O   . THR C  1 218 ? 100.970 67.801  273.642 1.00 139.28 ?  248 THR C O   1 
ATOM   6246  C CB  . THR C  1 218 ? 100.792 71.161  273.535 1.00 138.52 ?  248 THR C CB  1 
ATOM   6247  O OG1 . THR C  1 218 ? 101.585 70.739  272.419 1.00 137.70 ?  248 THR C OG1 1 
ATOM   6248  C CG2 . THR C  1 218 ? 101.447 72.388  274.143 1.00 137.86 ?  248 THR C CG2 1 
ATOM   6249  N N   . HIS C  1 219 ? 98.934  68.761  273.524 1.00 154.11 ?  249 HIS C N   1 
ATOM   6250  C CA  . HIS C  1 219 ? 98.324  67.645  272.816 1.00 154.07 ?  249 HIS C CA  1 
ATOM   6251  C C   . HIS C  1 219 ? 98.880  67.574  271.388 1.00 153.49 ?  249 HIS C C   1 
ATOM   6252  O O   . HIS C  1 219 ? 99.534  68.501  270.903 1.00 154.44 ?  249 HIS C O   1 
ATOM   6253  C CB  . HIS C  1 219 ? 96.800  67.775  272.808 1.00 153.84 ?  249 HIS C CB  1 
ATOM   6254  C CG  . HIS C  1 219 ? 96.293  68.941  272.017 1.00 152.79 ?  249 HIS C CG  1 
ATOM   6255  N ND1 . HIS C  1 219 ? 96.099  70.188  272.570 1.00 151.14 ?  249 HIS C ND1 1 
ATOM   6256  C CD2 . HIS C  1 219 ? 95.952  69.053  270.711 1.00 152.39 ?  249 HIS C CD2 1 
ATOM   6257  C CE1 . HIS C  1 219 ? 95.649  71.015  271.643 1.00 149.79 ?  249 HIS C CE1 1 
ATOM   6258  N NE2 . HIS C  1 219 ? 95.554  70.352  270.505 1.00 150.53 ?  249 HIS C NE2 1 
ATOM   6259  N N   . GLY C  1 220 ? 98.616  66.454  270.711 1.00 160.29 ?  250 GLY C N   1 
ATOM   6260  C CA  . GLY C  1 220 ? 99.080  66.231  269.346 1.00 157.46 ?  250 GLY C CA  1 
ATOM   6261  C C   . GLY C  1 220 ? 98.512  67.175  268.298 1.00 160.76 ?  250 GLY C C   1 
ATOM   6262  O O   . GLY C  1 220 ? 97.355  67.027  267.891 1.00 161.58 ?  250 GLY C O   1 
ATOM   6263  N N   . ILE C  1 221 ? 99.318  68.141  267.851 1.00 144.99 ?  251 ILE C N   1 
ATOM   6264  C CA  . ILE C  1 221 ? 98.933  69.138  266.849 1.00 144.93 ?  251 ILE C CA  1 
ATOM   6265  C C   . ILE C  1 221 ? 99.564  68.805  265.497 1.00 144.12 ?  251 ILE C C   1 
ATOM   6266  O O   . ILE C  1 221 ? 100.779 68.935  265.310 1.00 143.17 ?  251 ILE C O   1 
ATOM   6267  C CB  . ILE C  1 221 ? 99.283  70.563  267.299 1.00 144.69 ?  251 ILE C CB  1 
ATOM   6268  C CG1 . ILE C  1 221 ? 98.546  70.888  268.602 1.00 145.60 ?  251 ILE C CG1 1 
ATOM   6269  C CG2 . ILE C  1 221 ? 98.910  71.566  266.221 1.00 144.82 ?  251 ILE C CG2 1 
ATOM   6270  C CD1 . ILE C  1 221 ? 98.759  72.301  269.116 1.00 145.50 ?  251 ILE C CD1 1 
ATOM   6271  N N   . LYS C  1 222 ? 98.726  68.379  264.557 1.00 147.88 ?  252 LYS C N   1 
ATOM   6272  C CA  . LYS C  1 222 ? 99.155  68.022  263.206 1.00 147.21 ?  252 LYS C CA  1 
ATOM   6273  C C   . LYS C  1 222 ? 99.446  69.276  262.387 1.00 147.60 ?  252 LYS C C   1 
ATOM   6274  O O   . LYS C  1 222 ? 98.567  70.135  262.259 1.00 147.56 ?  252 LYS C O   1 
ATOM   6275  C CB  . LYS C  1 222 ? 98.060  67.231  262.504 1.00 147.85 ?  252 LYS C CB  1 
ATOM   6276  C CG  . LYS C  1 222 ? 97.726  65.882  263.104 1.00 148.37 ?  252 LYS C CG  1 
ATOM   6277  C CD  . LYS C  1 222 ? 96.543  65.270  262.364 1.00 149.10 ?  252 LYS C CD  1 
ATOM   6278  C CE  . LYS C  1 222 ? 95.613  64.532  263.316 1.00 150.34 ?  252 LYS C CE  1 
ATOM   6279  N NZ  . LYS C  1 222 ? 94.924  65.473  264.249 1.00 151.22 1  252 LYS C NZ  1 
ATOM   6280  N N   . PRO C  1 223 ? 100.649 69.428  261.823 1.00 149.44 ?  253 PRO C N   1 
ATOM   6281  C CA  . PRO C  1 223 ? 100.939 70.623  261.015 1.00 149.04 ?  253 PRO C CA  1 
ATOM   6282  C C   . PRO C  1 223 ? 100.268 70.571  259.649 1.00 149.99 ?  253 PRO C C   1 
ATOM   6283  O O   . PRO C  1 223 ? 100.933 70.362  258.629 1.00 150.18 ?  253 PRO C O   1 
ATOM   6284  C CB  . PRO C  1 223 ? 102.466 70.592  260.887 1.00 147.79 ?  253 PRO C CB  1 
ATOM   6285  C CG  . PRO C  1 223 ? 102.807 69.133  260.970 1.00 144.50 ?  253 PRO C CG  1 
ATOM   6286  C CD  . PRO C  1 223 ? 101.814 68.532  261.931 1.00 145.22 ?  253 PRO C CD  1 
ATOM   6287  N N   . VAL C  1 224 ? 98.952  70.763  259.617 1.00 165.21 ?  254 VAL C N   1 
ATOM   6288  C CA  . VAL C  1 224 ? 98.190  70.743  258.373 1.00 161.90 ?  254 VAL C CA  1 
ATOM   6289  C C   . VAL C  1 224 ? 98.220  72.131  257.743 1.00 162.39 ?  254 VAL C C   1 
ATOM   6290  O O   . VAL C  1 224 ? 97.637  73.082  258.272 1.00 159.11 ?  254 VAL C O   1 
ATOM   6291  C CB  . VAL C  1 224 ? 96.749  70.281  258.612 1.00 157.95 ?  254 VAL C CB  1 
ATOM   6292  C CG1 . VAL C  1 224 ? 95.954  70.344  257.319 1.00 159.09 ?  254 VAL C CG1 1 
ATOM   6293  C CG2 . VAL C  1 224 ? 96.735  68.875  259.194 1.00 156.89 ?  254 VAL C CG2 1 
ATOM   6294  N N   . VAL C  1 225 ? 98.907  72.247  256.611 1.00 155.54 ?  255 VAL C N   1 
ATOM   6295  C CA  . VAL C  1 225 ? 99.017  73.505  255.884 1.00 153.01 ?  255 VAL C CA  1 
ATOM   6296  C C   . VAL C  1 225 ? 97.815  73.611  254.954 1.00 152.58 ?  255 VAL C C   1 
ATOM   6297  O O   . VAL C  1 225 ? 97.700  72.846  253.993 1.00 152.38 ?  255 VAL C O   1 
ATOM   6298  C CB  . VAL C  1 225 ? 100.330 73.588  255.098 1.00 156.52 ?  255 VAL C CB  1 
ATOM   6299  C CG1 . VAL C  1 225 ? 100.434 74.930  254.403 1.00 160.69 ?  255 VAL C CG1 1 
ATOM   6300  C CG2 . VAL C  1 225 ? 101.516 73.357  256.016 1.00 156.57 ?  255 VAL C CG2 1 
ATOM   6301  N N   . SER C  1 226 ? 96.910  74.545  255.238 1.00 138.96 ?  256 SER C N   1 
ATOM   6302  C CA  . SER C  1 226 ? 95.736  74.722  254.396 1.00 139.97 ?  256 SER C CA  1 
ATOM   6303  C C   . SER C  1 226 ? 95.234  76.154  254.507 1.00 141.29 ?  256 SER C C   1 
ATOM   6304  O O   . SER C  1 226 ? 95.640  76.914  255.391 1.00 141.43 ?  256 SER C O   1 
ATOM   6305  C CB  . SER C  1 226 ? 94.629  73.732  254.780 1.00 140.39 ?  256 SER C CB  1 
ATOM   6306  O OG  . SER C  1 226 ? 94.226  73.912  256.128 1.00 140.98 ?  256 SER C OG  1 
ATOM   6307  N N   . THR C  1 227 ? 94.351  76.522  253.578 1.00 133.20 ?  257 THR C N   1 
ATOM   6308  C CA  . THR C  1 227 ? 93.742  77.842  253.554 1.00 134.72 ?  257 THR C CA  1 
ATOM   6309  C C   . THR C  1 227 ? 92.229  77.680  253.538 1.00 136.07 ?  257 THR C C   1 
ATOM   6310  O O   . THR C  1 227 ? 91.700  76.613  253.217 1.00 135.78 ?  257 THR C O   1 
ATOM   6311  C CB  . THR C  1 227 ? 94.193  78.674  252.342 1.00 135.02 ?  257 THR C CB  1 
ATOM   6312  O OG1 . THR C  1 227 ? 93.913  77.959  251.133 1.00 134.74 ?  257 THR C OG1 1 
ATOM   6313  C CG2 . THR C  1 227 ? 95.681  78.974  252.419 1.00 133.96 ?  257 THR C CG2 1 
ATOM   6314  N N   . GLN C  1 228 ? 91.539  78.762  253.889 1.00 145.81 ?  258 GLN C N   1 
ATOM   6315  C CA  . GLN C  1 228 ? 90.080  78.824  253.914 1.00 145.97 ?  258 GLN C CA  1 
ATOM   6316  C C   . GLN C  1 228 ? 89.418  77.789  254.827 1.00 146.34 ?  258 GLN C C   1 
ATOM   6317  O O   . GLN C  1 228 ? 88.720  78.166  255.773 1.00 148.93 ?  258 GLN C O   1 
ATOM   6318  C CB  . GLN C  1 228 ? 89.531  78.680  252.491 1.00 147.05 ?  258 GLN C CB  1 
ATOM   6319  C CG  . GLN C  1 228 ? 89.950  79.796  251.545 1.00 150.10 ?  258 GLN C CG  1 
ATOM   6320  C CD  . GLN C  1 228 ? 89.360  79.636  250.155 1.00 152.22 ?  258 GLN C CD  1 
ATOM   6321  O OE1 . GLN C  1 228 ? 88.697  78.641  249.858 1.00 152.79 ?  258 GLN C OE1 1 
ATOM   6322  N NE2 . GLN C  1 228 ? 89.600  80.619  249.294 1.00 153.80 ?  258 GLN C NE2 1 
ATOM   6323  N N   . LEU C  1 229 ? 89.625  76.493  254.566 1.00 147.50 ?  259 LEU C N   1 
ATOM   6324  C CA  . LEU C  1 229 ? 89.030  75.406  255.348 1.00 147.74 ?  259 LEU C CA  1 
ATOM   6325  C C   . LEU C  1 229 ? 90.062  74.737  256.253 1.00 151.28 ?  259 LEU C C   1 
ATOM   6326  O O   . LEU C  1 229 ? 91.051  74.180  255.763 1.00 152.04 ?  259 LEU C O   1 
ATOM   6327  C CB  . LEU C  1 229 ? 88.395  74.366  254.425 1.00 145.90 ?  259 LEU C CB  1 
ATOM   6328  C CG  . LEU C  1 229 ? 87.463  74.903  253.339 1.00 144.72 ?  259 LEU C CG  1 
ATOM   6329  C CD1 . LEU C  1 229 ? 86.921  73.758  252.505 1.00 143.67 ?  259 LEU C CD1 1 
ATOM   6330  C CD2 . LEU C  1 229 ? 86.329  75.713  253.941 1.00 143.22 ?  259 LEU C CD2 1 
ATOM   6331  N N   . LEU C  1 230 ? 89.828  74.789  257.566 1.00 154.05 ?  260 LEU C N   1 
ATOM   6332  C CA  . LEU C  1 230 ? 90.686  74.129  258.550 1.00 155.46 ?  260 LEU C CA  1 
ATOM   6333  C C   . LEU C  1 230 ? 90.405  72.622  258.568 1.00 155.19 ?  260 LEU C C   1 
ATOM   6334  O O   . LEU C  1 230 ? 89.272  72.203  258.832 1.00 153.32 ?  260 LEU C O   1 
ATOM   6335  C CB  . LEU C  1 230 ? 90.463  74.757  259.924 1.00 154.61 ?  260 LEU C CB  1 
ATOM   6336  C CG  . LEU C  1 230 ? 90.802  76.254  259.965 1.00 154.20 ?  260 LEU C CG  1 
ATOM   6337  C CD1 . LEU C  1 230 ? 90.524  76.859  261.333 1.00 153.03 ?  260 LEU C CD1 1 
ATOM   6338  C CD2 . LEU C  1 230 ? 92.242  76.516  259.540 1.00 156.38 ?  260 LEU C CD2 1 
ATOM   6339  N N   . LEU C  1 231 ? 91.428  71.817  258.274 1.00 152.82 ?  261 LEU C N   1 
ATOM   6340  C CA  . LEU C  1 231 ? 91.337  70.364  258.140 1.00 151.33 ?  261 LEU C CA  1 
ATOM   6341  C C   . LEU C  1 231 ? 92.058  69.656  259.290 1.00 149.95 ?  261 LEU C C   1 
ATOM   6342  O O   . LEU C  1 231 ? 93.113  70.116  259.739 1.00 149.87 ?  261 LEU C O   1 
ATOM   6343  C CB  . LEU C  1 231 ? 91.882  69.929  256.782 1.00 151.14 ?  261 LEU C CB  1 
ATOM   6344  C CG  . LEU C  1 231 ? 91.094  70.640  255.672 1.00 152.66 ?  261 LEU C CG  1 
ATOM   6345  C CD1 . LEU C  1 231 ? 91.515  70.178  254.287 1.00 152.46 ?  261 LEU C CD1 1 
ATOM   6346  C CD2 . LEU C  1 231 ? 89.585  70.484  255.866 1.00 153.43 ?  261 LEU C CD2 1 
ATOM   6347  N N   . ASN C  1 232 ? 91.501  68.522  259.748 1.00 160.44 ?  262 ASN C N   1 
ATOM   6348  C CA  . ASN C  1 232 ? 92.087  67.706  260.833 1.00 159.39 ?  262 ASN C CA  1 
ATOM   6349  C C   . ASN C  1 232 ? 92.412  68.522  262.086 1.00 159.44 ?  262 ASN C C   1 
ATOM   6350  O O   . ASN C  1 232 ? 93.477  68.366  262.686 1.00 158.85 ?  262 ASN C O   1 
ATOM   6351  C CB  . ASN C  1 232 ? 93.372  66.952  260.427 1.00 158.67 ?  262 ASN C CB  1 
ATOM   6352  C CG  . ASN C  1 232 ? 93.168  65.646  259.635 1.00 158.30 ?  262 ASN C CG  1 
ATOM   6353  O OD1 . ASN C  1 232 ? 93.440  64.600  260.218 1.00 157.80 ?  262 ASN C OD1 1 
ATOM   6354  N ND2 . ASN C  1 232 ? 92.810  65.677  258.343 1.00 158.75 ?  262 ASN C ND2 1 
ATOM   6355  N N   . GLY C  1 233 ? 91.486  69.376  262.519 1.00 157.09 ?  263 GLY C N   1 
ATOM   6356  C CA  . GLY C  1 233 ? 91.727  70.175  263.695 1.00 159.44 ?  263 GLY C CA  1 
ATOM   6357  C C   . GLY C  1 233 ? 90.964  69.726  264.932 1.00 162.04 ?  263 GLY C C   1 
ATOM   6358  O O   . GLY C  1 233 ? 90.250  68.725  264.950 1.00 160.42 ?  263 GLY C O   1 
ATOM   6359  N N   . SER C  1 234 ? 91.169  70.501  265.999 1.00 169.32 ?  264 SER C N   1 
ATOM   6360  C CA  . SER C  1 234 ? 90.514  70.268  267.280 1.00 172.26 ?  264 SER C CA  1 
ATOM   6361  C C   . SER C  1 234 ? 89.132  70.909  267.294 1.00 173.90 ?  264 SER C C   1 
ATOM   6362  O O   . SER C  1 234 ? 88.990  72.098  266.987 1.00 174.46 ?  264 SER C O   1 
ATOM   6363  C CB  . SER C  1 234 ? 91.359  70.806  268.435 1.00 170.13 ?  264 SER C CB  1 
ATOM   6364  O OG  . SER C  1 234 ? 92.624  70.171  268.485 1.00 167.77 ?  264 SER C OG  1 
ATOM   6365  N N   . LEU C  1 235 ? 88.121  70.129  267.652 1.00 165.14 ?  265 LEU C N   1 
ATOM   6366  C CA  . LEU C  1 235 ? 86.755  70.632  267.709 1.00 166.76 ?  265 LEU C CA  1 
ATOM   6367  C C   . LEU C  1 235 ? 86.546  71.527  268.930 1.00 167.62 ?  265 LEU C C   1 
ATOM   6368  O O   . LEU C  1 235 ? 87.160  71.334  269.983 1.00 166.70 ?  265 LEU C O   1 
ATOM   6369  C CB  . LEU C  1 235 ? 85.752  69.480  267.720 1.00 166.92 ?  265 LEU C CB  1 
ATOM   6370  C CG  . LEU C  1 235 ? 85.769  68.530  266.521 1.00 166.45 ?  265 LEU C CG  1 
ATOM   6371  C CD1 . LEU C  1 235 ? 84.845  67.342  266.766 1.00 166.85 ?  265 LEU C CD1 1 
ATOM   6372  C CD2 . LEU C  1 235 ? 85.374  69.278  265.251 1.00 167.74 ?  265 LEU C CD2 1 
ATOM   6373  N N   . ALA C  1 236 ? 85.671  72.520  268.780 1.00 163.50 ?  266 ALA C N   1 
ATOM   6374  C CA  . ALA C  1 236 ? 85.404  73.425  269.885 1.00 164.63 ?  266 ALA C CA  1 
ATOM   6375  C C   . ALA C  1 236 ? 84.435  72.766  270.863 1.00 164.83 ?  266 ALA C C   1 
ATOM   6376  O O   . ALA C  1 236 ? 83.838  71.724  270.580 1.00 164.54 ?  266 ALA C O   1 
ATOM   6377  C CB  . ALA C  1 236 ? 84.826  74.747  269.383 1.00 167.08 ?  266 ALA C CB  1 
ATOM   6378  N N   . GLU C  1 237 ? 84.275  73.388  272.025 1.00 184.40 ?  267 GLU C N   1 
ATOM   6379  C CA  . GLU C  1 237 ? 83.388  72.866  273.053 1.00 184.82 ?  267 GLU C CA  1 
ATOM   6380  C C   . GLU C  1 237 ? 82.052  73.597  273.047 1.00 189.82 ?  267 GLU C C   1 
ATOM   6381  O O   . GLU C  1 237 ? 81.998  74.816  272.859 1.00 193.62 ?  267 GLU C O   1 
ATOM   6382  C CB  . GLU C  1 237 ? 84.049  72.988  274.427 1.00 184.60 ?  267 GLU C CB  1 
ATOM   6383  C CG  . GLU C  1 237 ? 85.528  72.602  274.431 1.00 186.96 ?  267 GLU C CG  1 
ATOM   6384  C CD  . GLU C  1 237 ? 85.766  71.106  274.562 1.00 187.50 ?  267 GLU C CD  1 
ATOM   6385  O OE1 . GLU C  1 237 ? 84.805  70.323  274.403 1.00 188.17 ?  267 GLU C OE1 1 
ATOM   6386  O OE2 . GLU C  1 237 ? 86.924  70.712  274.817 1.00 186.12 -1 267 GLU C OE2 1 
ATOM   6387  N N   . GLU C  1 238 ? 80.978  72.834  273.273 1.00 198.05 ?  268 GLU C N   1 
ATOM   6388  C CA  . GLU C  1 238 ? 79.612  73.346  273.338 1.00 205.24 ?  268 GLU C CA  1 
ATOM   6389  C C   . GLU C  1 238 ? 79.263  74.123  272.074 1.00 208.93 ?  268 GLU C C   1 
ATOM   6390  O O   . GLU C  1 238 ? 79.141  73.535  270.994 1.00 208.27 ?  268 GLU C O   1 
ATOM   6391  C CB  . GLU C  1 238 ? 79.405  74.196  274.597 1.00 204.14 ?  268 GLU C CB  1 
ATOM   6392  C CG  . GLU C  1 238 ? 80.039  73.610  275.860 1.00 202.97 ?  268 GLU C CG  1 
ATOM   6393  C CD  . GLU C  1 238 ? 79.052  73.504  277.013 1.00 211.71 ?  268 GLU C CD  1 
ATOM   6394  O OE1 . GLU C  1 238 ? 79.441  73.776  278.169 1.00 210.35 ?  268 GLU C OE1 1 
ATOM   6395  O OE2 . GLU C  1 238 ? 77.881  73.147  276.760 1.00 219.46 -1 268 GLU C OE2 1 
ATOM   6396  N N   . GLU C  1 239 ? 79.088  75.436  272.194 1.00 187.96 ?  269 GLU C N   1 
ATOM   6397  C CA  . GLU C  1 239 ? 78.805  76.260  271.029 1.00 182.50 ?  269 GLU C CA  1 
ATOM   6398  C C   . GLU C  1 239 ? 80.078  76.513  270.230 1.00 175.47 ?  269 GLU C C   1 
ATOM   6399  O O   . GLU C  1 239 ? 81.186  76.550  270.775 1.00 170.59 ?  269 GLU C O   1 
ATOM   6400  C CB  . GLU C  1 239 ? 78.164  77.590  271.428 1.00 182.60 ?  269 GLU C CB  1 
ATOM   6401  C CG  . GLU C  1 239 ? 76.795  77.454  272.077 1.00 188.86 ?  269 GLU C CG  1 
ATOM   6402  C CD  . GLU C  1 239 ? 76.207  78.794  272.479 1.00 193.26 ?  269 GLU C CD  1 
ATOM   6403  O OE1 . GLU C  1 239 ? 76.961  79.789  272.517 1.00 188.86 ?  269 GLU C OE1 1 
ATOM   6404  O OE2 . GLU C  1 239 ? 74.989  78.854  272.751 1.00 200.46 -1 269 GLU C OE2 1 
ATOM   6405  N N   . VAL C  1 240 ? 79.904  76.687  268.917 1.00 161.36 ?  270 VAL C N   1 
ATOM   6406  C CA  . VAL C  1 240 ? 81.039  76.997  268.065 1.00 160.18 ?  270 VAL C CA  1 
ATOM   6407  C C   . VAL C  1 240 ? 81.607  78.356  268.457 1.00 161.51 ?  270 VAL C C   1 
ATOM   6408  O O   . VAL C  1 240 ? 80.879  79.276  268.853 1.00 164.24 ?  270 VAL C O   1 
ATOM   6409  C CB  . VAL C  1 240 ? 80.630  76.973  266.582 1.00 161.31 ?  270 VAL C CB  1 
ATOM   6410  C CG1 . VAL C  1 240 ? 80.291  75.551  266.152 1.00 159.84 ?  270 VAL C CG1 1 
ATOM   6411  C CG2 . VAL C  1 240 ? 79.456  77.904  266.340 1.00 165.05 ?  270 VAL C CG2 1 
ATOM   6412  N N   . MET C  1 241 ? 82.923  78.479  268.353 1.00 169.83 ?  271 MET C N   1 
ATOM   6413  C CA  . MET C  1 241 ? 83.633  79.664  268.803 1.00 168.53 ?  271 MET C CA  1 
ATOM   6414  C C   . MET C  1 241 ? 83.992  80.575  267.637 1.00 171.13 ?  271 MET C C   1 
ATOM   6415  O O   . MET C  1 241 ? 84.236  80.123  266.515 1.00 168.05 ?  271 MET C O   1 
ATOM   6416  C CB  . MET C  1 241 ? 84.900  79.283  269.569 1.00 164.30 ?  271 MET C CB  1 
ATOM   6417  C CG  . MET C  1 241 ? 85.261  80.262  270.675 1.00 163.65 ?  271 MET C CG  1 
ATOM   6418  S SD  . MET C  1 241 ? 84.052  80.380  272.002 1.00 172.07 ?  271 MET C SD  1 
ATOM   6419  C CE  . MET C  1 241 ? 84.069  78.688  272.578 1.00 172.28 ?  271 MET C CE  1 
ATOM   6420  N N   . ILE C  1 242 ? 84.013  81.873  267.923 1.00 160.61 ?  272 ILE C N   1 
ATOM   6421  C CA  . ILE C  1 242 ? 84.391  82.900  266.964 1.00 162.89 ?  272 ILE C CA  1 
ATOM   6422  C C   . ILE C  1 242 ? 85.512  83.712  267.600 1.00 163.23 ?  272 ILE C C   1 
ATOM   6423  O O   . ILE C  1 242 ? 85.310  84.320  268.658 1.00 164.69 ?  272 ILE C O   1 
ATOM   6424  C CB  . ILE C  1 242 ? 83.199  83.805  266.611 1.00 167.10 ?  272 ILE C CB  1 
ATOM   6425  C CG1 . ILE C  1 242 ? 82.034  82.988  266.040 1.00 166.99 ?  272 ILE C CG1 1 
ATOM   6426  C CG2 . ILE C  1 242 ? 83.619  84.875  265.633 1.00 169.70 ?  272 ILE C CG2 1 
ATOM   6427  C CD1 . ILE C  1 242 ? 82.354  82.263  264.760 1.00 166.14 ?  272 ILE C CD1 1 
ATOM   6428  N N   . ARG C  1 243 ? 86.686  83.726  266.969 1.00 156.62 ?  273 ARG C N   1 
ATOM   6429  C CA  . ARG C  1 243 ? 87.837  84.421  267.531 1.00 156.93 ?  273 ARG C CA  1 
ATOM   6430  C C   . ARG C  1 243 ? 88.406  85.414  266.533 1.00 159.50 ?  273 ARG C C   1 
ATOM   6431  O O   . ARG C  1 243 ? 88.546  85.108  265.345 1.00 159.22 ?  273 ARG C O   1 
ATOM   6432  C CB  . ARG C  1 243 ? 88.929  83.437  267.963 1.00 153.29 ?  273 ARG C CB  1 
ATOM   6433  C CG  . ARG C  1 243 ? 88.463  82.445  269.013 1.00 150.93 ?  273 ARG C CG  1 
ATOM   6434  C CD  . ARG C  1 243 ? 89.523  81.409  269.337 1.00 147.64 ?  273 ARG C CD  1 
ATOM   6435  N NE  . ARG C  1 243 ? 89.088  80.510  270.403 1.00 145.77 ?  273 ARG C NE  1 
ATOM   6436  C CZ  . ARG C  1 243 ? 88.473  79.349  270.204 1.00 144.14 ?  273 ARG C CZ  1 
ATOM   6437  N NH1 . ARG C  1 243 ? 88.214  78.934  268.972 1.00 144.03 1  273 ARG C NH1 1 
ATOM   6438  N NH2 . ARG C  1 243 ? 88.114  78.601  271.239 1.00 142.82 ?  273 ARG C NH2 1 
ATOM   6439  N N   . SER C  1 244 ? 88.740  86.603  267.028 1.00 166.61 ?  274 SER C N   1 
ATOM   6440  C CA  . SER C  1 244 ? 89.324  87.636  266.189 1.00 175.02 ?  274 SER C CA  1 
ATOM   6441  C C   . SER C  1 244 ? 90.124  88.592  267.058 1.00 180.23 ?  274 SER C C   1 
ATOM   6442  O O   . SER C  1 244 ? 89.753  88.856  268.204 1.00 180.69 ?  274 SER C O   1 
ATOM   6443  C CB  . SER C  1 244 ? 88.253  88.413  265.416 1.00 183.10 ?  274 SER C CB  1 
ATOM   6444  O OG  . SER C  1 244 ? 88.836  89.445  264.635 1.00 187.01 ?  274 SER C OG  1 
ATOM   6445  N N   . GLU C  1 245 ? 91.233  89.084  266.505 1.00 186.33 ?  275 GLU C N   1 
ATOM   6446  C CA  . GLU C  1 245 ? 92.077  90.039  267.215 1.00 192.14 ?  275 GLU C CA  1 
ATOM   6447  C C   . GLU C  1 245 ? 91.373  91.388  267.352 1.00 202.27 ?  275 GLU C C   1 
ATOM   6448  O O   . GLU C  1 245 ? 91.550  92.080  268.362 1.00 207.26 ?  275 GLU C O   1 
ATOM   6449  C CB  . GLU C  1 245 ? 93.433  90.185  266.524 1.00 190.57 ?  275 GLU C CB  1 
ATOM   6450  C CG  . GLU C  1 245 ? 94.420  91.070  267.279 1.00 194.86 ?  275 GLU C CG  1 
ATOM   6451  C CD  . GLU C  1 245 ? 95.773  91.153  266.597 1.00 190.33 ?  275 GLU C CD  1 
ATOM   6452  O OE1 . GLU C  1 245 ? 95.915  90.611  265.480 1.00 188.11 ?  275 GLU C OE1 1 
ATOM   6453  O OE2 . GLU C  1 245 ? 96.697  91.753  267.182 1.00 191.36 -1 275 GLU C OE2 1 
ATOM   6454  N N   . ASN C  1 246 ? 90.577  91.776  266.347 1.00 195.45 ?  276 ASN C N   1 
ATOM   6455  C CA  . ASN C  1 246 ? 89.815  93.030  266.366 1.00 201.55 ?  276 ASN C CA  1 
ATOM   6456  C C   . ASN C  1 246 ? 88.592  92.821  265.474 1.00 204.20 ?  276 ASN C C   1 
ATOM   6457  O O   . ASN C  1 246 ? 88.696  92.857  264.243 1.00 207.88 ?  276 ASN C O   1 
ATOM   6458  C CB  . ASN C  1 246 ? 90.647  94.215  265.893 1.00 209.62 ?  276 ASN C CB  1 
ATOM   6459  C CG  . ASN C  1 246 ? 90.040  95.557  266.296 1.00 218.70 ?  276 ASN C CG  1 
ATOM   6460  O OD1 . ASN C  1 246 ? 88.848  95.653  266.595 1.00 220.25 ?  276 ASN C OD1 1 
ATOM   6461  N ND2 . ASN C  1 246 ? 90.860  96.597  266.300 1.00 236.25 ?  276 ASN C ND2 1 
ATOM   6462  N N   . ILE C  1 247 ? 87.441  92.592  266.118 1.00 194.21 ?  277 ILE C N   1 
ATOM   6463  C CA  . ILE C  1 247 ? 86.195  92.317  265.404 1.00 195.36 ?  277 ILE C CA  1 
ATOM   6464  C C   . ILE C  1 247 ? 85.745  93.524  264.587 1.00 200.66 ?  277 ILE C C   1 
ATOM   6465  O O   . ILE C  1 247 ? 85.226  93.380  263.473 1.00 201.93 ?  277 ILE C O   1 
ATOM   6466  C CB  . ILE C  1 247 ? 85.117  91.896  266.422 1.00 194.27 ?  277 ILE C CB  1 
ATOM   6467  C CG1 . ILE C  1 247 ? 85.660  90.805  267.348 1.00 191.16 ?  277 ILE C CG1 1 
ATOM   6468  C CG2 . ILE C  1 247 ? 83.860  91.410  265.718 1.00 196.58 ?  277 ILE C CG2 1 
ATOM   6469  C CD1 . ILE C  1 247 ? 84.669  90.324  268.387 1.00 190.17 ?  277 ILE C CD1 1 
ATOM   6470  N N   . THR C  1 248 ? 85.932  94.730  265.127 1.00 207.32 ?  278 THR C N   1 
ATOM   6471  C CA  . THR C  1 248 ? 85.559  95.959  264.427 1.00 215.61 ?  278 THR C CA  1 
ATOM   6472  C C   . THR C  1 248 ? 86.417  96.211  263.187 1.00 216.38 ?  278 THR C C   1 
ATOM   6473  O O   . THR C  1 248 ? 85.960  96.856  262.236 1.00 220.08 ?  278 THR C O   1 
ATOM   6474  C CB  . THR C  1 248 ? 85.657  97.150  265.381 1.00 220.97 ?  278 THR C CB  1 
ATOM   6475  O OG1 . THR C  1 248 ? 86.993  97.236  265.890 1.00 222.23 ?  278 THR C OG1 1 
ATOM   6476  C CG2 . THR C  1 248 ? 84.686  96.994  266.549 1.00 217.18 ?  278 THR C CG2 1 
ATOM   6477  N N   . ASN C  1 249 ? 87.650  95.706  263.184 1.00 217.21 ?  279 ASN C N   1 
ATOM   6478  C CA  . ASN C  1 249 ? 88.603  95.854  262.083 1.00 215.17 ?  279 ASN C CA  1 
ATOM   6479  C C   . ASN C  1 249 ? 88.451  94.807  260.987 1.00 209.16 ?  279 ASN C C   1 
ATOM   6480  O O   . ASN C  1 249 ? 88.558  93.603  261.246 1.00 204.76 ?  279 ASN C O   1 
ATOM   6481  C CB  . ASN C  1 249 ? 90.038  95.807  262.599 1.00 210.75 ?  279 ASN C CB  1 
ATOM   6482  C CG  . ASN C  1 249 ? 91.032  96.383  261.601 1.00 211.75 ?  279 ASN C CG  1 
ATOM   6483  O OD1 . ASN C  1 249 ? 90.726  96.548  260.417 1.00 213.97 ?  279 ASN C OD1 1 
ATOM   6484  N ND2 . ASN C  1 249 ? 92.232  96.684  262.076 1.00 211.52 ?  279 ASN C ND2 1 
ATOM   6485  N N   . ASN C  1 250 ? 88.180  95.271  259.769 1.00 218.32 ?  280 ASN C N   1 
ATOM   6486  C CA  . ASN C  1 250 ? 88.009  94.366  258.645 1.00 218.38 ?  280 ASN C CA  1 
ATOM   6487  C C   . ASN C  1 250 ? 89.327  93.872  258.048 1.00 214.77 ?  280 ASN C C   1 
ATOM   6488  O O   . ASN C  1 250 ? 89.272  93.115  257.073 1.00 211.36 ?  280 ASN C O   1 
ATOM   6489  C CB  . ASN C  1 250 ? 87.239  95.062  257.516 1.00 226.11 ?  280 ASN C CB  1 
ATOM   6490  C CG  . ASN C  1 250 ? 87.990  96.268  256.957 1.00 233.46 ?  280 ASN C CG  1 
ATOM   6491  O OD1 . ASN C  1 250 ? 87.916  97.369  257.502 1.00 239.21 ?  280 ASN C OD1 1 
ATOM   6492  N ND2 . ASN C  1 250 ? 88.723  96.057  255.864 1.00 238.68 ?  280 ASN C ND2 1 
ATOM   6493  N N   . ALA C  1 251 ? 90.506  94.252  258.577 1.00 206.63 ?  281 ALA C N   1 
ATOM   6494  C CA  . ALA C  1 251 ? 91.736  93.735  257.975 1.00 204.29 ?  281 ALA C CA  1 
ATOM   6495  C C   . ALA C  1 251 ? 92.308  92.497  258.660 1.00 198.94 ?  281 ALA C C   1 
ATOM   6496  O O   . ALA C  1 251 ? 93.145  91.813  258.062 1.00 197.12 ?  281 ALA C O   1 
ATOM   6497  C CB  . ALA C  1 251 ? 92.815  94.830  257.966 1.00 207.41 ?  281 ALA C CB  1 
ATOM   6498  N N   . LYS C  1 252 ? 91.876  92.178  259.872 1.00 185.21 ?  282 LYS C N   1 
ATOM   6499  C CA  . LYS C  1 252 ? 92.317  90.980  260.578 1.00 180.35 ?  282 LYS C CA  1 
ATOM   6500  C C   . LYS C  1 252 ? 91.305  89.862  260.354 1.00 177.96 ?  282 LYS C C   1 
ATOM   6501  O O   . LYS C  1 252 ? 90.092  90.076  260.453 1.00 179.25 ?  282 LYS C O   1 
ATOM   6502  C CB  . LYS C  1 252 ? 92.679  91.217  262.046 1.00 179.08 ?  282 LYS C CB  1 
ATOM   6503  C CG  . LYS C  1 252 ? 93.960  92.080  262.122 1.00 182.51 ?  282 LYS C CG  1 
ATOM   6504  C CD  . LYS C  1 252 ? 95.143  91.322  261.435 1.00 183.56 ?  282 LYS C CD  1 
ATOM   6505  C CE  . LYS C  1 252 ? 96.484  92.073  261.465 1.00 183.47 ?  282 LYS C CE  1 
ATOM   6506  N NZ  . LYS C  1 252 ? 97.578  91.293  260.794 1.00 184.54 1  282 LYS C NZ  1 
ATOM   6507  N N   . ASN C  1 253 ? 91.820  88.662  260.092 1.00 160.58 ?  283 ASN C N   1 
ATOM   6508  C CA  . ASN C  1 253 ? 91.008  87.491  259.803 1.00 158.35 ?  283 ASN C CA  1 
ATOM   6509  C C   . ASN C  1 253 ? 90.207  87.063  261.028 1.00 156.54 ?  283 ASN C C   1 
ATOM   6510  O O   . ASN C  1 253 ? 90.556  87.364  262.170 1.00 155.88 ?  283 ASN C O   1 
ATOM   6511  C CB  . ASN C  1 253 ? 91.917  86.338  259.367 1.00 155.27 ?  283 ASN C CB  1 
ATOM   6512  C CG  . ASN C  1 253 ? 92.638  86.634  258.081 1.00 156.49 ?  283 ASN C CG  1 
ATOM   6513  O OD1 . ASN C  1 253 ? 91.995  86.954  257.094 1.00 158.46 ?  283 ASN C OD1 1 
ATOM   6514  N ND2 . ASN C  1 253 ? 93.971  86.537  258.076 1.00 155.54 ?  283 ASN C ND2 1 
ATOM   6515  N N   . ILE C  1 254 ? 89.115  86.341  260.771 1.00 141.73 ?  284 ILE C N   1 
ATOM   6516  C CA  . ILE C  1 254 ? 88.208  85.861  261.814 1.00 140.32 ?  284 ILE C CA  1 
ATOM   6517  C C   . ILE C  1 254 ? 88.268  84.342  261.812 1.00 136.11 ?  284 ILE C C   1 
ATOM   6518  O O   . ILE C  1 254 ? 87.665  83.679  260.960 1.00 135.38 ?  284 ILE C O   1 
ATOM   6519  C CB  . ILE C  1 254 ? 86.766  86.341  261.598 1.00 143.17 ?  284 ILE C CB  1 
ATOM   6520  C CG1 . ILE C  1 254 ? 86.694  87.866  261.466 1.00 148.09 ?  284 ILE C CG1 1 
ATOM   6521  C CG2 . ILE C  1 254 ? 85.847  85.821  262.716 1.00 141.93 ?  284 ILE C CG2 1 
ATOM   6522  C CD1 . ILE C  1 254 ? 85.284  88.388  261.227 1.00 151.50 ?  284 ILE C CD1 1 
ATOM   6523  N N   . LEU C  1 255 ? 88.997  83.788  262.772 1.00 143.92 ?  285 LEU C N   1 
ATOM   6524  C CA  . LEU C  1 255 ? 89.156  82.348  262.890 1.00 140.14 ?  285 LEU C CA  1 
ATOM   6525  C C   . LEU C  1 255 ? 87.922  81.732  263.547 1.00 139.39 ?  285 LEU C C   1 
ATOM   6526  O O   . LEU C  1 255 ? 87.548  82.110  264.663 1.00 140.01 ?  285 LEU C O   1 
ATOM   6527  C CB  . LEU C  1 255 ? 90.423  82.053  263.686 1.00 138.12 ?  285 LEU C CB  1 
ATOM   6528  C CG  . LEU C  1 255 ? 91.656  82.646  262.987 1.00 139.19 ?  285 LEU C CG  1 
ATOM   6529  C CD1 . LEU C  1 255 ? 92.948  82.257  263.680 1.00 137.27 ?  285 LEU C CD1 1 
ATOM   6530  C CD2 . LEU C  1 255 ? 91.709  82.284  261.507 1.00 139.29 ?  285 LEU C CD2 1 
ATOM   6531  N N   . VAL C  1 256 ? 87.288  80.790  262.852 1.00 140.99 ?  286 VAL C N   1 
ATOM   6532  C CA  . VAL C  1 256 ? 86.094  80.102  263.331 1.00 140.49 ?  286 VAL C CA  1 
ATOM   6533  C C   . VAL C  1 256 ? 86.473  78.680  263.711 1.00 137.03 ?  286 VAL C C   1 
ATOM   6534  O O   . VAL C  1 256 ? 87.276  78.039  263.023 1.00 135.33 ?  286 VAL C O   1 
ATOM   6535  C CB  . VAL C  1 256 ? 84.971  80.107  262.277 1.00 142.28 ?  286 VAL C CB  1 
ATOM   6536  C CG1 . VAL C  1 256 ? 83.710  79.457  262.838 1.00 142.24 ?  286 VAL C CG1 1 
ATOM   6537  C CG2 . VAL C  1 256 ? 84.699  81.524  261.830 1.00 146.07 ?  286 VAL C CG2 1 
ATOM   6538  N N   . GLN C  1 257 ? 85.906  78.187  264.808 1.00 153.32 ?  287 GLN C N   1 
ATOM   6539  C CA  . GLN C  1 257 ? 86.132  76.816  265.247 1.00 150.83 ?  287 GLN C CA  1 
ATOM   6540  C C   . GLN C  1 257 ? 84.792  76.103  265.359 1.00 153.03 ?  287 GLN C C   1 
ATOM   6541  O O   . GLN C  1 257 ? 83.851  76.625  265.968 1.00 152.66 ?  287 GLN C O   1 
ATOM   6542  C CB  . GLN C  1 257 ? 86.880  76.750  266.581 1.00 149.12 ?  287 GLN C CB  1 
ATOM   6543  C CG  . GLN C  1 257 ? 87.310  75.326  266.939 1.00 146.89 ?  287 GLN C CG  1 
ATOM   6544  C CD  . GLN C  1 257 ? 88.127  75.243  268.215 1.00 145.23 ?  287 GLN C CD  1 
ATOM   6545  O OE1 . GLN C  1 257 ? 88.225  76.210  268.968 1.00 146.35 ?  287 GLN C OE1 1 
ATOM   6546  N NE2 . GLN C  1 257 ? 88.717  74.077  268.465 1.00 143.18 ?  287 GLN C NE2 1 
ATOM   6547  N N   . PHE C  1 258 ? 84.719  74.914  264.772 1.00 158.22 ?  288 PHE C N   1 
ATOM   6548  C CA  . PHE C  1 258 ? 83.504  74.120  264.691 1.00 156.26 ?  288 PHE C CA  1 
ATOM   6549  C C   . PHE C  1 258 ? 83.338  73.206  265.899 1.00 157.14 ?  288 PHE C C   1 
ATOM   6550  O O   . PHE C  1 258 ? 84.297  72.855  266.589 1.00 159.74 ?  288 PHE C O   1 
ATOM   6551  C CB  . PHE C  1 258 ? 83.510  73.250  263.436 1.00 154.83 ?  288 PHE C CB  1 
ATOM   6552  C CG  . PHE C  1 258 ? 83.353  74.013  262.164 1.00 158.75 ?  288 PHE C CG  1 
ATOM   6553  C CD1 . PHE C  1 258 ? 82.698  75.229  262.142 1.00 164.14 ?  288 PHE C CD1 1 
ATOM   6554  C CD2 . PHE C  1 258 ? 83.844  73.498  260.979 1.00 154.45 ?  288 PHE C CD2 1 
ATOM   6555  C CE1 . PHE C  1 258 ? 82.550  75.923  260.962 1.00 163.07 ?  288 PHE C CE1 1 
ATOM   6556  C CE2 . PHE C  1 258 ? 83.700  74.184  259.798 1.00 153.08 ?  288 PHE C CE2 1 
ATOM   6557  C CZ  . PHE C  1 258 ? 83.051  75.398  259.788 1.00 156.84 ?  288 PHE C CZ  1 
ATOM   6558  N N   . ASN C  1 259 ? 82.085  72.827  266.143 1.00 156.46 ?  289 ASN C N   1 
ATOM   6559  C CA  . ASN C  1 259 ? 81.724  71.863  267.172 1.00 159.87 ?  289 ASN C CA  1 
ATOM   6560  C C   . ASN C  1 259 ? 81.556  70.474  266.574 1.00 159.78 ?  289 ASN C C   1 
ATOM   6561  O O   . ASN C  1 259 ? 82.104  69.497  267.093 1.00 158.72 ?  289 ASN C O   1 
ATOM   6562  C CB  . ASN C  1 259 ? 80.431  72.289  267.881 1.00 163.52 ?  289 ASN C CB  1 
ATOM   6563  C CG  . ASN C  1 259 ? 79.933  71.243  268.865 1.00 168.55 ?  289 ASN C CG  1 
ATOM   6564  O OD1 . ASN C  1 259 ? 79.128  70.380  268.514 1.00 171.66 ?  289 ASN C OD1 1 
ATOM   6565  N ND2 . ASN C  1 259 ? 80.409  71.317  270.104 1.00 172.91 ?  289 ASN C ND2 1 
ATOM   6566  N N   . THR C  1 260 ? 80.814  70.375  265.482 1.00 172.89 ?  290 THR C N   1 
ATOM   6567  C CA  . THR C  1 260 ? 80.637  69.140  264.736 1.00 175.43 ?  290 THR C CA  1 
ATOM   6568  C C   . THR C  1 260 ? 81.454  69.175  263.453 1.00 170.10 ?  290 THR C C   1 
ATOM   6569  O O   . THR C  1 260 ? 81.332  70.129  262.670 1.00 168.36 ?  290 THR C O   1 
ATOM   6570  C CB  . THR C  1 260 ? 79.164  68.923  264.406 1.00 182.07 ?  290 THR C CB  1 
ATOM   6571  O OG1 . THR C  1 260 ? 78.701  69.993  263.572 1.00 186.58 ?  290 THR C OG1 1 
ATOM   6572  C CG2 . THR C  1 260 ? 78.333  68.873  265.685 1.00 182.59 ?  290 THR C CG2 1 
ATOM   6573  N N   . PRO C  1 261 ? 82.305  68.177  263.225 1.00 177.47 ?  291 PRO C N   1 
ATOM   6574  C CA  . PRO C  1 261 ? 83.154  68.179  262.028 1.00 172.89 ?  291 PRO C CA  1 
ATOM   6575  C C   . PRO C  1 261 ? 82.318  67.966  260.776 1.00 176.68 ?  291 PRO C C   1 
ATOM   6576  O O   . PRO C  1 261 ? 81.337  67.220  260.787 1.00 181.58 ?  291 PRO C O   1 
ATOM   6577  C CB  . PRO C  1 261 ? 84.111  67.008  262.270 1.00 172.07 ?  291 PRO C CB  1 
ATOM   6578  C CG  . PRO C  1 261 ? 83.321  66.079  263.135 1.00 175.69 ?  291 PRO C CG  1 
ATOM   6579  C CD  . PRO C  1 261 ? 82.488  66.958  264.030 1.00 179.21 ?  291 PRO C CD  1 
ATOM   6580  N N   . VAL C  1 262 ? 82.702  68.641  259.697 1.00 165.47 ?  292 VAL C N   1 
ATOM   6581  C CA  . VAL C  1 262 ? 82.025  68.502  258.413 1.00 166.65 ?  292 VAL C CA  1 
ATOM   6582  C C   . VAL C  1 262 ? 82.817  67.528  257.547 1.00 165.00 ?  292 VAL C C   1 
ATOM   6583  O O   . VAL C  1 262 ? 83.962  67.799  257.167 1.00 163.93 ?  292 VAL C O   1 
ATOM   6584  C CB  . VAL C  1 262 ? 81.861  69.854  257.707 1.00 168.34 ?  292 VAL C CB  1 
ATOM   6585  C CG1 . VAL C  1 262 ? 81.164  69.665  256.368 1.00 169.64 ?  292 VAL C CG1 1 
ATOM   6586  C CG2 . VAL C  1 262 ? 81.102  70.836  258.592 1.00 170.28 ?  292 VAL C CG2 1 
ATOM   6587  N N   . GLN C  1 263 ? 82.200  66.383  257.257 1.00 165.67 ?  293 GLN C N   1 
ATOM   6588  C CA  . GLN C  1 263 ? 82.830  65.329  256.473 1.00 163.90 ?  293 GLN C CA  1 
ATOM   6589  C C   . GLN C  1 263 ? 83.092  65.846  255.064 1.00 164.86 ?  293 GLN C C   1 
ATOM   6590  O O   . GLN C  1 263 ? 82.161  66.248  254.359 1.00 165.83 ?  293 GLN C O   1 
ATOM   6591  C CB  . GLN C  1 263 ? 81.923  64.091  256.452 1.00 164.66 ?  293 GLN C CB  1 
ATOM   6592  C CG  . GLN C  1 263 ? 82.562  62.766  256.000 1.00 163.54 ?  293 GLN C CG  1 
ATOM   6593  C CD  . GLN C  1 263 ? 83.349  62.054  257.092 1.00 162.72 ?  293 GLN C CD  1 
ATOM   6594  O OE1 . GLN C  1 263 ? 83.759  62.665  258.077 1.00 168.48 ?  293 GLN C OE1 1 
ATOM   6595  N NE2 . GLN C  1 263 ? 83.579  60.756  256.907 1.00 162.78 ?  293 GLN C NE2 1 
ATOM   6596  N N   . ILE C  1 264 ? 84.352  65.820  254.643 1.00 173.69 ?  294 ILE C N   1 
ATOM   6597  C CA  . ILE C  1 264 ? 84.740  66.264  253.310 1.00 172.93 ?  294 ILE C CA  1 
ATOM   6598  C C   . ILE C  1 264 ? 85.439  65.095  252.634 1.00 174.96 ?  294 ILE C C   1 
ATOM   6599  O O   . ILE C  1 264 ? 86.280  64.425  253.247 1.00 174.40 ?  294 ILE C O   1 
ATOM   6600  C CB  . ILE C  1 264 ? 85.634  67.518  253.352 1.00 167.58 ?  294 ILE C CB  1 
ATOM   6601  C CG1 . ILE C  1 264 ? 85.974  67.964  251.933 1.00 166.57 ?  294 ILE C CG1 1 
ATOM   6602  C CG2 . ILE C  1 264 ? 86.890  67.283  254.176 1.00 166.02 ?  294 ILE C CG2 1 
ATOM   6603  C CD1 . ILE C  1 264 ? 86.805  69.202  251.878 1.00 161.66 ?  294 ILE C CD1 1 
ATOM   6604  N N   . ASN C  1 265 ? 85.068  64.841  251.377 1.00 182.98 ?  295 ASN C N   1 
ATOM   6605  C CA  . ASN C  1 265 ? 85.603  63.730  250.602 1.00 180.37 ?  295 ASN C CA  1 
ATOM   6606  C C   . ASN C  1 265 ? 86.244  64.291  249.339 1.00 180.59 ?  295 ASN C C   1 
ATOM   6607  O O   . ASN C  1 265 ? 85.566  64.954  248.549 1.00 181.78 ?  295 ASN C O   1 
ATOM   6608  C CB  . ASN C  1 265 ? 84.431  62.822  250.226 1.00 181.52 ?  295 ASN C CB  1 
ATOM   6609  C CG  . ASN C  1 265 ? 83.787  62.164  251.437 1.00 176.66 ?  295 ASN C CG  1 
ATOM   6610  O OD1 . ASN C  1 265 ? 83.625  62.804  252.476 1.00 178.14 ?  295 ASN C OD1 1 
ATOM   6611  N ND2 . ASN C  1 265 ? 83.340  60.933  251.290 1.00 174.16 ?  295 ASN C ND2 1 
ATOM   6612  N N   . CYS C  1 266 ? 87.532  64.006  249.138 1.00 153.74 ?  296 CYS C N   1 
ATOM   6613  C CA  . CYS C  1 266 ? 88.292  64.458  247.974 1.00 152.65 ?  296 CYS C CA  1 
ATOM   6614  C C   . CYS C  1 266 ? 88.952  63.304  247.225 1.00 156.00 ?  296 CYS C C   1 
ATOM   6615  O O   . CYS C  1 266 ? 89.557  62.417  247.836 1.00 158.70 ?  296 CYS C O   1 
ATOM   6616  C CB  . CYS C  1 266 ? 89.322  65.513  248.389 1.00 150.70 ?  296 CYS C CB  1 
ATOM   6617  S SG  . CYS C  1 266 ? 88.601  66.946  249.273 1.00 184.19 ?  296 CYS C SG  1 
ATOM   6618  N N   . THR C  1 267 ? 88.864  63.341  245.896 1.00 161.98 ?  297 THR C N   1 
ATOM   6619  C CA  . THR C  1 267 ? 89.440  62.303  245.050 1.00 160.46 ?  297 THR C CA  1 
ATOM   6620  C C   . THR C  1 267 ? 90.175  62.907  243.864 1.00 155.66 ?  297 THR C C   1 
ATOM   6621  O O   . THR C  1 267 ? 89.976  64.070  243.499 1.00 154.24 ?  297 THR C O   1 
ATOM   6622  C CB  . THR C  1 267 ? 88.384  61.323  244.539 1.00 162.18 ?  297 THR C CB  1 
ATOM   6623  O OG1 . THR C  1 267 ? 87.222  62.049  244.116 1.00 165.15 ?  297 THR C OG1 1 
ATOM   6624  C CG2 . THR C  1 267 ? 88.023  60.329  245.620 1.00 163.90 ?  297 THR C CG2 1 
ATOM   6625  N N   . ARG C  1 268 ? 91.033  62.079  243.263 1.00 142.89 ?  298 ARG C N   1 
ATOM   6626  C CA  . ARG C  1 268 ? 91.802  62.416  242.067 1.00 143.14 ?  298 ARG C CA  1 
ATOM   6627  C C   . ARG C  1 268 ? 91.489  61.351  241.023 1.00 143.34 ?  298 ARG C C   1 
ATOM   6628  O O   . ARG C  1 268 ? 92.241  60.379  240.864 1.00 143.02 ?  298 ARG C O   1 
ATOM   6629  C CB  . ARG C  1 268 ? 93.300  62.499  242.363 1.00 142.67 ?  298 ARG C CB  1 
ATOM   6630  C CG  . ARG C  1 268 ? 94.070  63.381  241.384 1.00 143.28 ?  298 ARG C CG  1 
ATOM   6631  C CD  . ARG C  1 268 ? 94.463  62.690  240.079 1.00 143.49 ?  298 ARG C CD  1 
ATOM   6632  N NE  . ARG C  1 268 ? 95.405  61.601  240.320 1.00 143.03 ?  298 ARG C NE  1 
ATOM   6633  C CZ  . ARG C  1 268 ? 96.726  61.754  240.358 1.00 143.21 ?  298 ARG C CZ  1 
ATOM   6634  N NH1 . ARG C  1 268 ? 97.266  62.952  240.171 1.00 143.80 1  298 ARG C NH1 1 
ATOM   6635  N NH2 . ARG C  1 268 ? 97.509  60.710  240.594 1.00 143.09 ?  298 ARG C NH2 1 
ATOM   6636  N N   . PRO C  1 269 ? 90.392  61.518  240.273 1.00 150.82 ?  299 PRO C N   1 
ATOM   6637  C CA  . PRO C  1 269 ? 89.967  60.497  239.301 1.00 151.26 ?  299 PRO C CA  1 
ATOM   6638  C C   . PRO C  1 269 ? 90.861  60.396  238.074 1.00 151.36 ?  299 PRO C C   1 
ATOM   6639  O O   . PRO C  1 269 ? 90.391  60.615  236.953 1.00 152.05 ?  299 PRO C O   1 
ATOM   6640  C CB  . PRO C  1 269 ? 88.557  60.959  238.914 1.00 152.37 ?  299 PRO C CB  1 
ATOM   6641  C CG  . PRO C  1 269 ? 88.586  62.435  239.115 1.00 152.73 ?  299 PRO C CG  1 
ATOM   6642  C CD  . PRO C  1 269 ? 89.471  62.667  240.309 1.00 151.69 ?  299 PRO C CD  1 
ATOM   6643  N N   . ASN C  1 270 ? 92.137  60.062  238.253 1.00 155.46 ?  300 ASN C N   1 
ATOM   6644  C CA  . ASN C  1 270 ? 93.054  59.919  237.123 1.00 154.21 ?  300 ASN C CA  1 
ATOM   6645  C C   . ASN C  1 270 ? 94.131  58.907  237.494 1.00 155.87 ?  300 ASN C C   1 
ATOM   6646  O O   . ASN C  1 270 ? 95.009  59.221  238.301 1.00 157.58 ?  300 ASN C O   1 
ATOM   6647  C CB  . ASN C  1 270 ? 93.703  61.263  236.763 1.00 154.75 ?  300 ASN C CB  1 
ATOM   6648  C CG  . ASN C  1 270 ? 92.840  62.144  235.859 1.00 155.29 ?  300 ASN C CG  1 
ATOM   6649  O OD1 . ASN C  1 270 ? 93.295  62.592  234.810 1.00 156.07 ?  300 ASN C OD1 1 
ATOM   6650  N ND2 . ASN C  1 270 ? 91.630  62.458  236.299 1.00 155.52 ?  300 ASN C ND2 1 
ATOM   6651  N N   . ASN C  1 271 ? 94.069  57.696  236.928 1.00 157.40 ?  301 ASN C N   1 
ATOM   6652  C CA  . ASN C  1 271 ? 95.103  56.704  237.217 1.00 157.48 ?  301 ASN C CA  1 
ATOM   6653  C C   . ASN C  1 271 ? 96.408  57.098  236.535 1.00 157.77 ?  301 ASN C C   1 
ATOM   6654  O O   . ASN C  1 271 ? 96.686  56.657  235.416 1.00 158.40 ?  301 ASN C O   1 
ATOM   6655  C CB  . ASN C  1 271 ? 94.666  55.308  236.738 1.00 158.16 ?  301 ASN C CB  1 
ATOM   6656  C CG  . ASN C  1 271 ? 95.530  54.178  237.306 1.00 158.62 ?  301 ASN C CG  1 
ATOM   6657  O OD1 . ASN C  1 271 ? 96.349  54.399  238.191 1.00 158.32 ?  301 ASN C OD1 1 
ATOM   6658  N ND2 . ASN C  1 271 ? 95.357  52.960  236.773 1.00 159.61 ?  301 ASN C ND2 1 
ATOM   6659  N N   . ASN C  1 272 ? 97.202  57.945  237.190 1.00 155.93 ?  302 ASN C N   1 
ATOM   6660  C CA  . ASN C  1 272 ? 98.432  58.422  236.579 1.00 156.56 ?  302 ASN C CA  1 
ATOM   6661  C C   . ASN C  1 272 ? 99.523  57.351  236.634 1.00 157.17 ?  302 ASN C C   1 
ATOM   6662  O O   . ASN C  1 272 ? 99.484  56.422  237.445 1.00 157.10 ?  302 ASN C O   1 
ATOM   6663  C CB  . ASN C  1 272 ? 98.915  59.694  237.288 1.00 156.45 ?  302 ASN C CB  1 
ATOM   6664  C CG  . ASN C  1 272 ? 97.989  60.885  237.060 1.00 156.39 ?  302 ASN C CG  1 
ATOM   6665  O OD1 . ASN C  1 272 ? 96.859  60.722  236.603 1.00 156.28 ?  302 ASN C OD1 1 
ATOM   6666  N ND2 . ASN C  1 272 ? 98.460  62.085  237.397 1.00 156.74 ?  302 ASN C ND2 1 
ATOM   6667  N N   . THR C  1 273 ? 100.500 57.489  235.746 1.00 151.14 ?  303 THR C N   1 
ATOM   6668  C CA  . THR C  1 273 ? 101.656 56.605  235.676 1.00 152.19 ?  303 THR C CA  1 
ATOM   6669  C C   . THR C  1 273 ? 102.912 57.458  235.819 1.00 152.89 ?  303 THR C C   1 
ATOM   6670  O O   . THR C  1 273 ? 102.991 58.553  235.253 1.00 153.12 ?  303 THR C O   1 
ATOM   6671  C CB  . THR C  1 273 ? 101.668 55.735  234.409 1.00 153.04 ?  303 THR C CB  1 
ATOM   6672  O OG1 . THR C  1 273 ? 102.498 54.587  234.636 1.00 154.27 ?  303 THR C OG1 1 
ATOM   6673  C CG2 . THR C  1 273 ? 102.180 56.482  233.219 1.00 153.64 ?  303 THR C CG2 1 
ATOM   6674  N N   . ARG C  1 274 ? 103.867 56.997  236.620 1.00 161.34 ?  304 ARG C N   1 
ATOM   6675  C CA  . ARG C  1 274 ? 105.113 57.728  236.851 1.00 162.49 ?  304 ARG C CA  1 
ATOM   6676  C C   . ARG C  1 274 ? 106.213 57.203  235.929 1.00 159.18 ?  304 ARG C C   1 
ATOM   6677  O O   . ARG C  1 274 ? 106.736 56.102  236.133 1.00 155.26 ?  304 ARG C O   1 
ATOM   6678  C CB  . ARG C  1 274 ? 105.551 57.655  238.312 1.00 164.00 ?  304 ARG C CB  1 
ATOM   6679  C CG  . ARG C  1 274 ? 106.916 58.300  238.536 1.00 163.49 ?  304 ARG C CG  1 
ATOM   6680  C CD  . ARG C  1 274 ? 107.430 58.117  239.952 1.00 163.08 ?  304 ARG C CD  1 
ATOM   6681  N NE  . ARG C  1 274 ? 106.763 59.028  240.877 1.00 159.60 ?  304 ARG C NE  1 
ATOM   6682  C CZ  . ARG C  1 274 ? 107.060 59.143  242.168 1.00 163.86 ?  304 ARG C CZ  1 
ATOM   6683  N NH1 . ARG C  1 274 ? 108.022 58.403  242.703 1.00 168.28 1  304 ARG C NH1 1 
ATOM   6684  N NH2 . ARG C  1 274 ? 106.394 60.003  242.926 1.00 162.21 ?  304 ARG C NH2 1 
ATOM   6685  N N   . LYS C  1 275 ? 106.545 57.993  234.905 1.00 146.86 ?  305 LYS C N   1 
ATOM   6686  C CA  . LYS C  1 275 ? 107.658 57.715  234.001 1.00 149.46 ?  305 LYS C CA  1 
ATOM   6687  C C   . LYS C  1 275 ? 108.929 58.273  234.636 1.00 149.62 ?  305 LYS C C   1 
ATOM   6688  O O   . LYS C  1 275 ? 109.003 59.468  234.943 1.00 148.37 ?  305 LYS C O   1 
ATOM   6689  C CB  . LYS C  1 275 ? 107.406 58.343  232.630 1.00 150.40 ?  305 LYS C CB  1 
ATOM   6690  C CG  . LYS C  1 275 ? 106.582 57.485  231.675 1.00 151.53 ?  305 LYS C CG  1 
ATOM   6691  C CD  . LYS C  1 275 ? 106.671 58.001  230.245 1.00 153.07 ?  305 LYS C CD  1 
ATOM   6692  C CE  . LYS C  1 275 ? 105.911 57.101  229.280 1.00 154.44 ?  305 LYS C CE  1 
ATOM   6693  N NZ  . LYS C  1 275 ? 104.443 57.099  229.541 1.00 152.58 1  305 LYS C NZ  1 
ATOM   6694  N N   . SER C  1 276 ? 109.930 57.403  234.818 1.00 154.76 ?  306 SER C N   1 
ATOM   6695  C CA  . SER C  1 276 ? 111.208 57.735  235.462 1.00 155.85 ?  306 SER C CA  1 
ATOM   6696  C C   . SER C  1 276 ? 112.378 57.901  234.487 1.00 160.99 ?  306 SER C C   1 
ATOM   6697  O O   . SER C  1 276 ? 113.235 57.027  234.350 1.00 164.68 ?  306 SER C O   1 
ATOM   6698  C CB  . SER C  1 276 ? 111.529 56.666  236.507 1.00 155.67 ?  306 SER C CB  1 
ATOM   6699  O OG  . SER C  1 276 ? 111.541 55.369  235.927 1.00 162.97 ?  306 SER C OG  1 
ATOM   6700  N N   . ILE C  1 277 ? 112.409 59.044  233.793 1.00 153.31 ?  307 ILE C N   1 
ATOM   6701  C CA  . ILE C  1 277 ? 113.518 59.345  232.888 1.00 153.12 ?  307 ILE C CA  1 
ATOM   6702  C C   . ILE C  1 277 ? 114.773 59.650  233.700 1.00 153.06 ?  307 ILE C C   1 
ATOM   6703  O O   . ILE C  1 277 ? 114.703 60.241  234.787 1.00 155.14 ?  307 ILE C O   1 
ATOM   6704  C CB  . ILE C  1 277 ? 113.174 60.530  231.968 1.00 152.84 ?  307 ILE C CB  1 
ATOM   6705  C CG1 . ILE C  1 277 ? 112.854 61.777  232.800 1.00 150.13 ?  307 ILE C CG1 1 
ATOM   6706  C CG2 . ILE C  1 277 ? 112.023 60.178  231.037 1.00 152.81 ?  307 ILE C CG2 1 
ATOM   6707  C CD1 . ILE C  1 277 ? 112.562 63.011  231.974 1.00 152.10 ?  307 ILE C CD1 1 
ATOM   6708  N N   . ARG C  1 278 ? 115.936 59.238  233.183 1.00 148.23 ?  308 ARG C N   1 
ATOM   6709  C CA  . ARG C  1 278 ? 117.198 59.321  233.919 1.00 149.12 ?  308 ARG C CA  1 
ATOM   6710  C C   . ARG C  1 278 ? 118.028 60.511  233.439 1.00 150.19 ?  308 ARG C C   1 
ATOM   6711  O O   . ARG C  1 278 ? 118.574 60.485  232.331 1.00 152.55 ?  308 ARG C O   1 
ATOM   6712  C CB  . ARG C  1 278 ? 118.010 58.035  233.761 1.00 151.61 ?  308 ARG C CB  1 
ATOM   6713  C CG  . ARG C  1 278 ? 117.307 56.745  234.148 1.00 151.13 ?  308 ARG C CG  1 
ATOM   6714  C CD  . ARG C  1 278 ? 118.177 55.555  233.778 1.00 154.12 ?  308 ARG C CD  1 
ATOM   6715  N NE  . ARG C  1 278 ? 119.451 55.576  234.491 1.00 155.17 ?  308 ARG C NE  1 
ATOM   6716  C CZ  . ARG C  1 278 ? 120.388 54.641  234.374 1.00 157.82 ?  308 ARG C CZ  1 
ATOM   6717  N NH1 . ARG C  1 278 ? 120.196 53.605  233.569 1.00 159.72 1  308 ARG C NH1 1 
ATOM   6718  N NH2 . ARG C  1 278 ? 121.516 54.743  235.063 1.00 158.69 ?  308 ARG C NH2 1 
ATOM   6719  N N   . ILE C  1 279 ? 118.110 61.558  234.262 1.00 152.28 ?  309 ILE C N   1 
ATOM   6720  C CA  . ILE C  1 279 ? 119.006 62.677  233.985 1.00 153.45 ?  309 ILE C CA  1 
ATOM   6721  C C   . ILE C  1 279 ? 120.261 62.441  234.814 1.00 154.61 ?  309 ILE C C   1 
ATOM   6722  O O   . ILE C  1 279 ? 120.578 63.218  235.722 1.00 153.62 ?  309 ILE C O   1 
ATOM   6723  C CB  . ILE C  1 279 ? 118.375 64.047  234.294 1.00 151.36 ?  309 ILE C CB  1 
ATOM   6724  C CG1 . ILE C  1 279 ? 116.910 64.077  233.857 1.00 149.58 ?  309 ILE C CG1 1 
ATOM   6725  C CG2 . ILE C  1 279 ? 119.166 65.166  233.616 1.00 153.04 ?  309 ILE C CG2 1 
ATOM   6726  C CD1 . ILE C  1 279 ? 116.215 65.387  234.159 1.00 147.60 ?  309 ILE C CD1 1 
ATOM   6727  N N   . GLY C  1 280 ? 120.974 61.361  234.512 1.00 175.37 ?  312 GLY C N   1 
ATOM   6728  C CA  . GLY C  1 280 ? 122.148 60.975  235.272 1.00 177.00 ?  312 GLY C CA  1 
ATOM   6729  C C   . GLY C  1 280 ? 123.327 61.912  235.106 1.00 179.94 ?  312 GLY C C   1 
ATOM   6730  O O   . GLY C  1 280 ? 123.240 62.894  234.369 1.00 182.58 ?  312 GLY C O   1 
ATOM   6731  N N   . PRO C  1 281 ? 124.442 61.611  235.792 1.00 173.30 ?  313 PRO C N   1 
ATOM   6732  C CA  . PRO C  1 281 ? 124.560 60.451  236.683 1.00 171.64 ?  313 PRO C CA  1 
ATOM   6733  C C   . PRO C  1 281 ? 124.042 60.680  238.101 1.00 168.11 ?  313 PRO C C   1 
ATOM   6734  O O   . PRO C  1 281 ? 124.400 61.661  238.751 1.00 165.56 ?  313 PRO C O   1 
ATOM   6735  C CB  . PRO C  1 281 ? 126.067 60.197  236.712 1.00 172.52 ?  313 PRO C CB  1 
ATOM   6736  C CG  . PRO C  1 281 ? 126.669 61.541  236.523 1.00 172.03 ?  313 PRO C CG  1 
ATOM   6737  C CD  . PRO C  1 281 ? 125.728 62.311  235.627 1.00 174.67 ?  313 PRO C CD  1 
ATOM   6738  N N   . GLY C  1 282 ? 123.193 59.770  238.566 1.00 167.87 ?  314 GLY C N   1 
ATOM   6739  C CA  . GLY C  1 282 ? 122.660 59.841  239.910 1.00 164.08 ?  314 GLY C CA  1 
ATOM   6740  C C   . GLY C  1 282 ? 121.236 60.349  239.964 1.00 163.38 ?  314 GLY C C   1 
ATOM   6741  O O   . GLY C  1 282 ? 120.331 59.616  240.372 1.00 163.04 ?  314 GLY C O   1 
ATOM   6742  N N   . GLN C  1 283 ? 121.022 61.594  239.546 1.00 171.47 ?  315 GLN C N   1 
ATOM   6743  C CA  . GLN C  1 283 ? 119.690 62.182  239.585 1.00 171.05 ?  315 GLN C CA  1 
ATOM   6744  C C   . GLN C  1 283 ? 118.750 61.470  238.617 1.00 175.38 ?  315 GLN C C   1 
ATOM   6745  O O   . GLN C  1 283 ? 119.174 60.894  237.610 1.00 175.30 ?  315 GLN C O   1 
ATOM   6746  C CB  . GLN C  1 283 ? 119.750 63.679  239.273 1.00 165.93 ?  315 GLN C CB  1 
ATOM   6747  C CG  . GLN C  1 283 ? 120.284 64.543  240.416 1.00 164.99 ?  315 GLN C CG  1 
ATOM   6748  C CD  . GLN C  1 283 ? 121.793 64.488  240.563 1.00 157.69 ?  315 GLN C CD  1 
ATOM   6749  O OE1 . GLN C  1 283 ? 122.490 63.888  239.743 1.00 163.53 ?  315 GLN C OE1 1 
ATOM   6750  N NE2 . GLN C  1 283 ? 122.306 65.117  241.617 1.00 152.93 ?  315 GLN C NE2 1 
ATOM   6751  N N   . ALA C  1 284 ? 117.457 61.514  238.938 1.00 171.47 ?  316 ALA C N   1 
ATOM   6752  C CA  . ALA C  1 284 ? 116.420 60.892  238.123 1.00 167.25 ?  316 ALA C CA  1 
ATOM   6753  C C   . ALA C  1 284 ? 115.121 61.663  238.308 1.00 165.15 ?  316 ALA C C   1 
ATOM   6754  O O   . ALA C  1 284 ? 114.693 61.890  239.444 1.00 163.31 ?  316 ALA C O   1 
ATOM   6755  C CB  . ALA C  1 284 ? 116.230 59.417  238.501 1.00 164.84 ?  316 ALA C CB  1 
ATOM   6756  N N   . PHE C  1 285 ? 114.501 62.056  237.197 1.00 163.43 ?  317 PHE C N   1 
ATOM   6757  C CA  . PHE C  1 285 ? 113.266 62.831  237.204 1.00 161.95 ?  317 PHE C CA  1 
ATOM   6758  C C   . PHE C  1 285 ? 112.056 61.928  237.019 1.00 161.32 ?  317 PHE C C   1 
ATOM   6759  O O   . PHE C  1 285 ? 112.065 61.015  236.187 1.00 161.36 ?  317 PHE C O   1 
ATOM   6760  C CB  . PHE C  1 285 ? 113.274 63.918  236.127 1.00 160.21 ?  317 PHE C CB  1 
ATOM   6761  C CG  . PHE C  1 285 ? 111.953 64.616  235.974 1.00 156.23 ?  317 PHE C CG  1 
ATOM   6762  C CD1 . PHE C  1 285 ? 111.501 65.488  236.950 1.00 150.95 ?  317 PHE C CD1 1 
ATOM   6763  C CD2 . PHE C  1 285 ? 111.178 64.423  234.844 1.00 152.21 ?  317 PHE C CD2 1 
ATOM   6764  C CE1 . PHE C  1 285 ? 110.288 66.126  236.817 1.00 145.41 ?  317 PHE C CE1 1 
ATOM   6765  C CE2 . PHE C  1 285 ? 109.971 65.071  234.700 1.00 146.49 ?  317 PHE C CE2 1 
ATOM   6766  C CZ  . PHE C  1 285 ? 109.523 65.920  235.690 1.00 143.81 ?  317 PHE C CZ  1 
ATOM   6767  N N   . TYR C  1 286 ? 111.020 62.185  237.818 1.00 159.48 ?  318 TYR C N   1 
ATOM   6768  C CA  . TYR C  1 286 ? 109.773 61.426  237.787 1.00 159.46 ?  318 TYR C CA  1 
ATOM   6769  C C   . TYR C  1 286 ? 108.741 62.223  236.998 1.00 155.53 ?  318 TYR C C   1 
ATOM   6770  O O   . TYR C  1 286 ? 108.091 63.124  237.536 1.00 151.92 ?  318 TYR C O   1 
ATOM   6771  C CB  . TYR C  1 286 ? 109.296 61.174  239.213 1.00 160.36 ?  318 TYR C CB  1 
ATOM   6772  C CG  . TYR C  1 286 ? 110.264 60.375  240.054 1.00 165.64 ?  318 TYR C CG  1 
ATOM   6773  C CD1 . TYR C  1 286 ? 111.385 59.771  239.493 1.00 166.54 ?  318 TYR C CD1 1 
ATOM   6774  C CD2 . TYR C  1 286 ? 110.099 60.289  241.423 1.00 166.30 ?  318 TYR C CD2 1 
ATOM   6775  C CE1 . TYR C  1 286 ? 112.283 59.064  240.271 1.00 166.73 ?  318 TYR C CE1 1 
ATOM   6776  C CE2 . TYR C  1 286 ? 110.986 59.591  242.200 1.00 166.27 ?  318 TYR C CE2 1 
ATOM   6777  C CZ  . TYR C  1 286 ? 112.078 58.980  241.629 1.00 165.51 ?  318 TYR C CZ  1 
ATOM   6778  O OH  . TYR C  1 286 ? 112.955 58.282  242.431 1.00 163.85 ?  318 TYR C OH  1 
ATOM   6779  N N   . ALA C  1 287 ? 108.592 61.884  235.720 1.00 157.81 ?  319 ALA C N   1 
ATOM   6780  C CA  . ALA C  1 287 ? 107.648 62.549  234.838 1.00 153.45 ?  319 ALA C CA  1 
ATOM   6781  C C   . ALA C  1 287 ? 106.261 61.935  234.986 1.00 151.94 ?  319 ALA C C   1 
ATOM   6782  O O   . ALA C  1 287 ? 106.072 60.919  235.659 1.00 154.66 ?  319 ALA C O   1 
ATOM   6783  C CB  . ALA C  1 287 ? 108.113 62.452  233.386 1.00 151.65 ?  319 ALA C CB  1 
ATOM   6784  N N   . THR C  1 288 ? 105.278 62.565  234.348 1.00 154.79 ?  320 THR C N   1 
ATOM   6785  C CA  . THR C  1 288 ? 103.918 62.046  234.346 1.00 152.74 ?  320 THR C CA  1 
ATOM   6786  C C   . THR C  1 288 ? 103.649 61.390  232.997 1.00 154.57 ?  320 THR C C   1 
ATOM   6787  O O   . THR C  1 288 ? 103.681 62.060  231.959 1.00 150.62 ?  320 THR C O   1 
ATOM   6788  C CB  . THR C  1 288 ? 102.895 63.156  234.593 1.00 148.03 ?  320 THR C CB  1 
ATOM   6789  O OG1 . THR C  1 288 ? 103.356 64.028  235.630 1.00 148.44 ?  320 THR C OG1 1 
ATOM   6790  C CG2 . THR C  1 288 ? 101.558 62.559  235.008 1.00 148.42 ?  320 THR C CG2 1 
ATOM   6791  N N   . GLY C  1 289 ? 103.413 60.085  233.013 1.00 169.68 ?  321 GLY C N   1 
ATOM   6792  C CA  . GLY C  1 289 ? 103.128 59.337  231.808 1.00 165.92 ?  321 GLY C CA  1 
ATOM   6793  C C   . GLY C  1 289 ? 101.694 59.548  231.364 1.00 161.32 ?  321 GLY C C   1 
ATOM   6794  O O   . GLY C  1 289 ? 101.020 60.502  231.761 1.00 159.87 ?  321 GLY C O   1 
ATOM   6795  N N   . ASP C  1 290 A 101.223 58.630  230.523 1.00 171.98 ?  321 ASP C N   1 
ATOM   6796  C CA  . ASP C  1 290 A 99.847  58.674  230.052 1.00 170.88 ?  321 ASP C CA  1 
ATOM   6797  C C   . ASP C  1 290 A 98.876  58.294  231.180 1.00 168.85 ?  321 ASP C C   1 
ATOM   6798  O O   . ASP C  1 290 A 99.241  57.630  232.156 1.00 168.12 ?  321 ASP C O   1 
ATOM   6799  C CB  . ASP C  1 290 A 99.678  57.772  228.827 1.00 170.25 ?  321 ASP C CB  1 
ATOM   6800  C CG  . ASP C  1 290 A 99.966  56.316  229.125 1.00 175.48 ?  321 ASP C CG  1 
ATOM   6801  O OD1 . ASP C  1 290 A 101.148 55.915  229.048 1.00 180.11 ?  321 ASP C OD1 1 
ATOM   6802  O OD2 . ASP C  1 290 A 99.011  55.571  229.426 1.00 173.88 -1 321 ASP C OD2 1 
ATOM   6803  N N   . ILE C  1 291 ? 97.624  58.739  231.034 1.00 164.28 ?  322 ILE C N   1 
ATOM   6804  C CA  . ILE C  1 291 ? 96.561  58.515  232.017 1.00 166.14 ?  322 ILE C CA  1 
ATOM   6805  C C   . ILE C  1 291 ? 95.713  57.306  231.634 1.00 164.38 ?  322 ILE C C   1 
ATOM   6806  O O   . ILE C  1 291 ? 95.189  57.228  230.514 1.00 159.23 ?  322 ILE C O   1 
ATOM   6807  C CB  . ILE C  1 291 ? 95.681  59.767  232.167 1.00 163.08 ?  322 ILE C CB  1 
ATOM   6808  C CG1 . ILE C  1 291 ? 96.538  60.973  232.554 1.00 164.24 ?  322 ILE C CG1 1 
ATOM   6809  C CG2 . ILE C  1 291 ? 94.583  59.531  233.198 1.00 164.99 ?  322 ILE C CG2 1 
ATOM   6810  C CD1 . ILE C  1 291 ? 95.746  62.246  232.756 1.00 160.63 ?  322 ILE C CD1 1 
ATOM   6811  N N   . ILE C  1 292 ? 95.582  56.368  232.570 1.00 168.03 ?  323 ILE C N   1 
ATOM   6812  C CA  . ILE C  1 292 ? 94.804  55.143  232.398 1.00 166.14 ?  323 ILE C CA  1 
ATOM   6813  C C   . ILE C  1 292 ? 93.348  55.375  232.802 1.00 162.70 ?  323 ILE C C   1 
ATOM   6814  O O   . ILE C  1 292 ? 93.043  55.542  233.986 1.00 165.25 ?  323 ILE C O   1 
ATOM   6815  C CB  . ILE C  1 292 ? 95.404  53.980  233.197 1.00 170.25 ?  323 ILE C CB  1 
ATOM   6816  C CG1 . ILE C  1 292 ? 96.884  53.798  232.856 1.00 172.08 ?  323 ILE C CG1 1 
ATOM   6817  C CG2 . ILE C  1 292 ? 94.614  52.696  232.947 1.00 168.94 ?  323 ILE C CG2 1 
ATOM   6818  C CD1 . ILE C  1 292 ? 97.816  53.990  234.036 1.00 175.48 ?  323 ILE C CD1 1 
ATOM   6819  N N   . GLY C  1 293 ? 92.447  55.387  231.817 1.00 169.38 ?  324 GLY C N   1 
ATOM   6820  C CA  . GLY C  1 293 ? 91.023  55.537  232.056 1.00 168.32 ?  324 GLY C CA  1 
ATOM   6821  C C   . GLY C  1 293 ? 90.462  56.796  231.411 1.00 167.59 ?  324 GLY C C   1 
ATOM   6822  O O   . GLY C  1 293 ? 90.903  57.201  230.330 1.00 168.73 ?  324 GLY C O   1 
ATOM   6823  N N   . ASP C  1 294 ? 89.499  57.413  232.091 1.00 179.37 ?  325 ASP C N   1 
ATOM   6824  C CA  . ASP C  1 294 ? 88.817  58.594  231.583 1.00 175.17 ?  325 ASP C CA  1 
ATOM   6825  C C   . ASP C  1 294 ? 89.503  59.859  232.077 1.00 175.53 ?  325 ASP C C   1 
ATOM   6826  O O   . ASP C  1 294 ? 90.057  59.904  233.183 1.00 177.27 ?  325 ASP C O   1 
ATOM   6827  C CB  . ASP C  1 294 ? 87.339  58.586  231.984 1.00 174.71 ?  325 ASP C CB  1 
ATOM   6828  C CG  . ASP C  1 294 ? 86.601  57.354  231.470 1.00 174.61 ?  325 ASP C CG  1 
ATOM   6829  O OD1 . ASP C  1 294 ? 86.883  56.927  230.332 1.00 173.91 ?  325 ASP C OD1 1 
ATOM   6830  O OD2 . ASP C  1 294 ? 85.728  56.826  232.193 1.00 175.82 -1 325 ASP C OD2 1 
ATOM   6831  N N   . ILE C  1 295 ? 89.454  60.901  231.247 1.00 176.79 ?  326 ILE C N   1 
ATOM   6832  C CA  . ILE C  1 295 ? 90.025  62.203  231.605 1.00 176.70 ?  326 ILE C CA  1 
ATOM   6833  C C   . ILE C  1 295 ? 89.011  62.974  232.447 1.00 178.27 ?  326 ILE C C   1 
ATOM   6834  O O   . ILE C  1 295 ? 88.091  63.610  231.923 1.00 181.91 ?  326 ILE C O   1 
ATOM   6835  C CB  . ILE C  1 295 ? 90.439  62.988  230.359 1.00 178.04 ?  326 ILE C CB  1 
ATOM   6836  C CG1 . ILE C  1 295 ? 91.458  62.191  229.545 1.00 176.22 ?  326 ILE C CG1 1 
ATOM   6837  C CG2 . ILE C  1 295 ? 90.998  64.328  230.758 1.00 176.66 ?  326 ILE C CG2 1 
ATOM   6838  C CD1 . ILE C  1 295 ? 92.743  61.897  230.297 1.00 172.85 ?  326 ILE C CD1 1 
ATOM   6839  N N   . ARG C  1 296 ? 89.169  62.892  233.762 1.00 176.75 ?  327 ARG C N   1 
ATOM   6840  C CA  . ARG C  1 296 ? 88.327  63.570  234.727 1.00 177.64 ?  327 ARG C CA  1 
ATOM   6841  C C   . ARG C  1 296 ? 89.174  64.508  235.582 1.00 176.06 ?  327 ARG C C   1 
ATOM   6842  O O   . ARG C  1 296 ? 90.396  64.364  235.677 1.00 173.28 ?  327 ARG C O   1 
ATOM   6843  C CB  . ARG C  1 296 ? 87.587  62.548  235.588 1.00 174.96 ?  327 ARG C CB  1 
ATOM   6844  C CG  . ARG C  1 296 ? 86.350  61.987  234.916 1.00 178.78 ?  327 ARG C CG  1 
ATOM   6845  C CD  . ARG C  1 296 ? 85.749  60.836  235.707 1.00 175.48 ?  327 ARG C CD  1 
ATOM   6846  N NE  . ARG C  1 296 ? 85.564  61.116  237.130 1.00 173.28 ?  327 ARG C NE  1 
ATOM   6847  C CZ  . ARG C  1 296 ? 85.062  60.227  237.983 1.00 175.58 ?  327 ARG C CZ  1 
ATOM   6848  N NH1 . ARG C  1 296 ? 84.903  60.521  239.271 1.00 173.25 1  327 ARG C NH1 1 
ATOM   6849  N NH2 . ARG C  1 296 ? 84.692  59.039  237.525 1.00 181.23 ?  327 ARG C NH2 1 
ATOM   6850  N N   . GLN C  1 297 ? 88.507  65.479  236.203 1.00 169.78 ?  328 GLN C N   1 
ATOM   6851  C CA  . GLN C  1 297 ? 89.138  66.476  237.057 1.00 168.64 ?  328 GLN C CA  1 
ATOM   6852  C C   . GLN C  1 297 ? 88.846  66.172  238.521 1.00 164.74 ?  328 GLN C C   1 
ATOM   6853  O O   . GLN C  1 297 ? 87.820  65.570  238.852 1.00 164.18 ?  328 GLN C O   1 
ATOM   6854  C CB  . GLN C  1 297 ? 88.641  67.877  236.703 1.00 173.61 ?  328 GLN C CB  1 
ATOM   6855  C CG  . GLN C  1 297 ? 87.150  67.928  236.408 1.00 181.09 ?  328 GLN C CG  1 
ATOM   6856  C CD  . GLN C  1 297 ? 86.726  69.246  235.791 1.00 188.37 ?  328 GLN C CD  1 
ATOM   6857  O OE1 . GLN C  1 297 ? 85.942  69.278  234.844 1.00 186.93 ?  328 GLN C OE1 1 
ATOM   6858  N NE2 . GLN C  1 297 ? 87.254  70.345  236.321 1.00 194.22 ?  328 GLN C NE2 1 
ATOM   6859  N N   . ALA C  1 298 ? 89.759  66.588  239.389 1.00 174.51 ?  329 ALA C N   1 
ATOM   6860  C CA  . ALA C  1 298 ? 89.604  66.355  240.816 1.00 166.58 ?  329 ALA C CA  1 
ATOM   6861  C C   . ALA C  1 298 ? 88.410  67.134  241.367 1.00 165.39 ?  329 ALA C C   1 
ATOM   6862  O O   . ALA C  1 298 ? 88.045  68.195  240.857 1.00 169.80 ?  329 ALA C O   1 
ATOM   6863  C CB  . ALA C  1 298 ? 90.886  66.752  241.549 1.00 164.48 ?  329 ALA C CB  1 
ATOM   6864  N N   . HIS C  1 299 ? 87.788  66.585  242.414 1.00 165.87 ?  330 HIS C N   1 
ATOM   6865  C CA  . HIS C  1 299 ? 86.620  67.216  243.021 1.00 167.28 ?  330 HIS C CA  1 
ATOM   6866  C C   . HIS C  1 299 ? 86.524  66.809  244.490 1.00 168.40 ?  330 HIS C C   1 
ATOM   6867  O O   . HIS C  1 299 ? 87.085  65.790  244.905 1.00 166.70 ?  330 HIS C O   1 
ATOM   6868  C CB  . HIS C  1 299 ? 85.349  66.842  242.249 1.00 173.10 ?  330 HIS C CB  1 
ATOM   6869  C CG  . HIS C  1 299 ? 85.027  65.382  242.300 1.00 174.86 ?  330 HIS C CG  1 
ATOM   6870  N ND1 . HIS C  1 299 ? 85.615  64.461  241.458 1.00 184.86 ?  330 HIS C ND1 1 
ATOM   6871  C CD2 . HIS C  1 299 ? 84.194  64.679  243.102 1.00 168.31 ?  330 HIS C CD2 1 
ATOM   6872  C CE1 . HIS C  1 299 ? 85.154  63.255  241.736 1.00 177.62 ?  330 HIS C CE1 1 
ATOM   6873  N NE2 . HIS C  1 299 ? 84.289  63.359  242.730 1.00 169.18 ?  330 HIS C NE2 1 
ATOM   6874  N N   . CYS C  1 300 ? 85.796  67.619  245.275 1.00 172.64 ?  331 CYS C N   1 
ATOM   6875  C CA  . CYS C  1 300 ? 85.554  67.376  246.698 1.00 169.14 ?  331 CYS C CA  1 
ATOM   6876  C C   . CYS C  1 300 ? 84.050  67.452  246.998 1.00 171.16 ?  331 CYS C C   1 
ATOM   6877  O O   . CYS C  1 300 ? 83.382  68.377  246.528 1.00 174.64 ?  331 CYS C O   1 
ATOM   6878  C CB  . CYS C  1 300 ? 86.312  68.416  247.548 1.00 166.74 ?  331 CYS C CB  1 
ATOM   6879  S SG  . CYS C  1 300 ? 88.143  68.212  247.742 1.00 164.25 ?  331 CYS C SG  1 
ATOM   6880  N N   . ASN C  1 301 ? 83.513  66.491  247.767 1.00 170.44 ?  332 ASN C N   1 
ATOM   6881  C CA  . ASN C  1 301 ? 82.090  66.448  248.134 1.00 172.26 ?  332 ASN C CA  1 
ATOM   6882  C C   . ASN C  1 301 ? 81.857  66.797  249.603 1.00 171.00 ?  332 ASN C C   1 
ATOM   6883  O O   . ASN C  1 301 ? 82.568  66.299  250.482 1.00 169.32 ?  332 ASN C O   1 
ATOM   6884  C CB  . ASN C  1 301 ? 81.436  65.090  247.868 1.00 172.19 ?  332 ASN C CB  1 
ATOM   6885  C CG  . ASN C  1 301 ? 81.143  64.852  246.414 1.00 175.79 ?  332 ASN C CG  1 
ATOM   6886  O OD1 . ASN C  1 301 ? 80.676  65.742  245.705 1.00 179.83 ?  332 ASN C OD1 1 
ATOM   6887  N ND2 . ASN C  1 301 ? 81.356  63.631  245.974 1.00 174.49 ?  332 ASN C ND2 1 
ATOM   6888  N N   . VAL C  1 302 ? 80.865  67.658  249.859 1.00 169.28 ?  333 VAL C N   1 
ATOM   6889  C CA  . VAL C  1 302 ? 80.416  68.041  251.203 1.00 169.79 ?  333 VAL C CA  1 
ATOM   6890  C C   . VAL C  1 302 ? 78.907  67.813  251.309 1.00 172.12 ?  333 VAL C C   1 
ATOM   6891  O O   . VAL C  1 302 ? 78.139  68.352  250.504 1.00 174.42 ?  333 VAL C O   1 
ATOM   6892  C CB  . VAL C  1 302 ? 80.771  69.500  251.540 1.00 170.51 ?  333 VAL C CB  1 
ATOM   6893  C CG1 . VAL C  1 302 ? 80.116  69.923  252.848 1.00 171.48 ?  333 VAL C CG1 1 
ATOM   6894  C CG2 . VAL C  1 302 ? 82.283  69.659  251.636 1.00 168.36 ?  333 VAL C CG2 1 
ATOM   6895  N N   . SER C  1 303 ? 78.489  67.016  252.302 1.00 172.80 ?  334 SER C N   1 
ATOM   6896  C CA  . SER C  1 303 ? 77.079  66.690  252.534 1.00 179.10 ?  334 SER C CA  1 
ATOM   6897  C C   . SER C  1 303 ? 76.215  67.934  252.749 1.00 184.39 ?  334 SER C C   1 
ATOM   6898  O O   . SER C  1 303 ? 76.402  68.683  253.711 1.00 186.39 ?  334 SER C O   1 
ATOM   6899  C CB  . SER C  1 303 ? 76.962  65.750  253.732 1.00 177.63 ?  334 SER C CB  1 
ATOM   6900  O OG  . SER C  1 303 ? 77.879  66.098  254.753 1.00 177.31 ?  334 SER C OG  1 
ATOM   6901  N N   . LYS C  1 304 ? 75.263  68.128  251.826 1.00 182.83 ?  335 LYS C N   1 
ATOM   6902  C CA  . LYS C  1 304 ? 74.372  69.289  251.818 1.00 186.01 ?  335 LYS C CA  1 
ATOM   6903  C C   . LYS C  1 304 ? 73.608  69.470  253.126 1.00 187.41 ?  335 LYS C C   1 
ATOM   6904  O O   . LYS C  1 304 ? 73.384  70.605  253.567 1.00 189.03 ?  335 LYS C O   1 
ATOM   6905  C CB  . LYS C  1 304 ? 73.427  69.159  250.618 1.00 188.72 ?  335 LYS C CB  1 
ATOM   6906  C CG  . LYS C  1 304 ? 72.690  70.419  250.182 1.00 191.66 ?  335 LYS C CG  1 
ATOM   6907  C CD  . LYS C  1 304 ? 71.754  70.098  249.020 1.00 194.41 ?  335 LYS C CD  1 
ATOM   6908  C CE  . LYS C  1 304 ? 70.923  71.301  248.566 1.00 197.89 ?  335 LYS C CE  1 
ATOM   6909  N NZ  . LYS C  1 304 ? 69.921  71.820  249.562 1.00 201.10 1  335 LYS C NZ  1 
ATOM   6910  N N   . ALA C  1 305 ? 73.202  68.370  253.765 1.00 202.18 ?  336 ALA C N   1 
ATOM   6911  C CA  . ALA C  1 305 ? 72.461  68.475  255.018 1.00 202.76 ?  336 ALA C CA  1 
ATOM   6912  C C   . ALA C  1 305 ? 73.343  69.018  256.135 1.00 200.93 ?  336 ALA C C   1 
ATOM   6913  O O   . ALA C  1 305 ? 72.950  69.943  256.853 1.00 205.86 ?  336 ALA C O   1 
ATOM   6914  C CB  . ALA C  1 305 ? 71.880  67.115  255.399 1.00 199.43 ?  336 ALA C CB  1 
ATOM   6915  N N   . THR C  1 306 ? 74.568  68.502  256.245 1.00 177.86 ?  337 THR C N   1 
ATOM   6916  C CA  . THR C  1 306 ? 75.469  68.937  257.307 1.00 175.86 ?  337 THR C CA  1 
ATOM   6917  C C   . THR C  1 306 ? 75.898  70.383  257.104 1.00 176.42 ?  337 THR C C   1 
ATOM   6918  O O   . THR C  1 306 ? 75.991  71.150  258.068 1.00 176.79 ?  337 THR C O   1 
ATOM   6919  C CB  . THR C  1 306 ? 76.682  68.008  257.383 1.00 172.54 ?  337 THR C CB  1 
ATOM   6920  O OG1 . THR C  1 306 ? 76.236  66.652  257.498 1.00 171.72 ?  337 THR C OG1 1 
ATOM   6921  C CG2 . THR C  1 306 ? 77.547  68.350  258.588 1.00 171.43 ?  337 THR C CG2 1 
ATOM   6922  N N   . TRP C  1 307 ? 76.181  70.770  255.861 1.00 166.80 ?  338 TRP C N   1 
ATOM   6923  C CA  . TRP C  1 307 ? 76.656  72.124  255.610 1.00 167.60 ?  338 TRP C CA  1 
ATOM   6924  C C   . TRP C  1 307 ? 75.560  73.162  255.848 1.00 171.26 ?  338 TRP C C   1 
ATOM   6925  O O   . TRP C  1 307 ? 75.860  74.296  256.241 1.00 172.19 ?  338 TRP C O   1 
ATOM   6926  C CB  . TRP C  1 307 ? 77.187  72.226  254.184 1.00 167.36 ?  338 TRP C CB  1 
ATOM   6927  C CG  . TRP C  1 307 ? 77.840  73.528  253.898 1.00 168.21 ?  338 TRP C CG  1 
ATOM   6928  C CD1 . TRP C  1 307 ? 77.356  74.536  253.124 1.00 171.24 ?  338 TRP C CD1 1 
ATOM   6929  C CD2 . TRP C  1 307 ? 79.133  73.951  254.350 1.00 166.31 ?  338 TRP C CD2 1 
ATOM   6930  N NE1 . TRP C  1 307 ? 78.254  75.576  253.086 1.00 171.49 ?  338 TRP C NE1 1 
ATOM   6931  C CE2 . TRP C  1 307 ? 79.356  75.239  253.827 1.00 168.45 ?  338 TRP C CE2 1 
ATOM   6932  C CE3 . TRP C  1 307 ? 80.118  73.367  255.152 1.00 163.30 ?  338 TRP C CE3 1 
ATOM   6933  C CZ2 . TRP C  1 307 ? 80.523  75.955  254.080 1.00 167.71 ?  338 TRP C CZ2 1 
ATOM   6934  C CZ3 . TRP C  1 307 ? 81.277  74.080  255.402 1.00 162.49 ?  338 TRP C CZ3 1 
ATOM   6935  C CH2 . TRP C  1 307 ? 81.469  75.360  254.867 1.00 164.69 ?  338 TRP C CH2 1 
ATOM   6936  N N   . ASN C  1 308 ? 74.292  72.799  255.615 1.00 184.75 ?  339 ASN C N   1 
ATOM   6937  C CA  . ASN C  1 308 ? 73.194  73.745  255.810 1.00 188.68 ?  339 ASN C CA  1 
ATOM   6938  C C   . ASN C  1 308 ? 72.974  74.068  257.282 1.00 189.34 ?  339 ASN C C   1 
ATOM   6939  O O   . ASN C  1 308 ? 72.736  75.227  257.642 1.00 191.43 ?  339 ASN C O   1 
ATOM   6940  C CB  . ASN C  1 308 ? 71.919  73.120  255.265 1.00 191.12 ?  339 ASN C CB  1 
ATOM   6941  C CG  . ASN C  1 308 ? 71.016  74.096  254.574 1.00 202.78 ?  339 ASN C CG  1 
ATOM   6942  O OD1 . ASN C  1 308 ? 71.365  75.245  254.300 1.00 202.17 ?  339 ASN C OD1 1 
ATOM   6943  N ND2 . ASN C  1 308 ? 69.803  73.628  254.322 1.00 224.60 ?  339 ASN C ND2 1 
ATOM   6944  N N   . GLU C  1 309 ? 73.056  73.057  258.147 1.00 193.51 ?  340 GLU C N   1 
ATOM   6945  C CA  . GLU C  1 309 ? 72.879  73.278  259.581 1.00 192.24 ?  340 GLU C CA  1 
ATOM   6946  C C   . GLU C  1 309 ? 74.115  73.949  260.163 1.00 187.00 ?  340 GLU C C   1 
ATOM   6947  O O   . GLU C  1 309 ? 74.009  74.780  261.072 1.00 189.78 ?  340 GLU C O   1 
ATOM   6948  C CB  . GLU C  1 309 ? 72.445  71.994  260.296 1.00 196.45 ?  340 GLU C CB  1 
ATOM   6949  C CG  . GLU C  1 309 ? 72.922  70.707  259.697 1.00 200.30 ?  340 GLU C CG  1 
ATOM   6950  C CD  . GLU C  1 309 ? 72.364  69.489  260.414 1.00 205.93 ?  340 GLU C CD  1 
ATOM   6951  O OE1 . GLU C  1 309 ? 72.844  69.131  261.510 1.00 205.45 ?  340 GLU C OE1 1 
ATOM   6952  O OE2 . GLU C  1 309 ? 71.404  68.901  259.869 1.00 212.33 -1 340 GLU C OE2 1 
ATOM   6953  N N   . THR C  1 310 ? 75.296  73.582  259.660 1.00 176.34 ?  341 THR C N   1 
ATOM   6954  C CA  . THR C  1 310 ? 76.544  74.148  260.160 1.00 172.04 ?  341 THR C CA  1 
ATOM   6955  C C   . THR C  1 310 ? 76.613  75.633  259.824 1.00 172.53 ?  341 THR C C   1 
ATOM   6956  O O   . THR C  1 310 ? 77.000  76.447  260.670 1.00 175.29 ?  341 THR C O   1 
ATOM   6957  C CB  . THR C  1 310 ? 77.736  73.405  259.557 1.00 166.84 ?  341 THR C CB  1 
ATOM   6958  O OG1 . THR C  1 310 ? 77.649  72.012  259.882 1.00 168.94 ?  341 THR C OG1 1 
ATOM   6959  C CG2 . THR C  1 310 ? 79.042  73.961  260.087 1.00 163.52 ?  341 THR C CG2 1 
ATOM   6960  N N   . LEU C  1 311 ? 76.252  76.005  258.593 1.00 171.88 ?  342 LEU C N   1 
ATOM   6961  C CA  . LEU C  1 311 ? 76.259  77.420  258.240 1.00 174.79 ?  342 LEU C CA  1 
ATOM   6962  C C   . LEU C  1 311 ? 75.232  78.165  259.078 1.00 184.71 ?  342 LEU C C   1 
ATOM   6963  O O   . LEU C  1 311 ? 75.475  79.296  259.516 1.00 187.54 ?  342 LEU C O   1 
ATOM   6964  C CB  . LEU C  1 311 ? 75.976  77.613  256.753 1.00 176.42 ?  342 LEU C CB  1 
ATOM   6965  C CG  . LEU C  1 311 ? 77.169  78.118  255.946 1.00 175.38 ?  342 LEU C CG  1 
ATOM   6966  C CD1 . LEU C  1 311 ? 76.737  78.474  254.536 1.00 177.79 ?  342 LEU C CD1 1 
ATOM   6967  C CD2 . LEU C  1 311 ? 77.792  79.319  256.641 1.00 177.65 ?  342 LEU C CD2 1 
ATOM   6968  N N   . GLY C  1 312 ? 74.080  77.538  259.322 1.00 193.82 ?  343 GLY C N   1 
ATOM   6969  C CA  . GLY C  1 312 ? 73.061  78.157  260.145 1.00 201.24 ?  343 GLY C CA  1 
ATOM   6970  C C   . GLY C  1 312 ? 73.477  78.203  261.597 1.00 198.17 ?  343 GLY C C   1 
ATOM   6971  O O   . GLY C  1 312 ? 72.925  78.988  262.375 1.00 200.17 ?  343 GLY C O   1 
ATOM   6972  N N   . LYS C  1 313 ? 74.442  77.362  261.971 1.00 194.08 ?  344 LYS C N   1 
ATOM   6973  C CA  . LYS C  1 313 ? 74.962  77.321  263.328 1.00 189.58 ?  344 LYS C CA  1 
ATOM   6974  C C   . LYS C  1 313 ? 76.018  78.397  263.532 1.00 188.31 ?  344 LYS C C   1 
ATOM   6975  O O   . LYS C  1 313 ? 76.225  78.857  264.661 1.00 187.04 ?  344 LYS C O   1 
ATOM   6976  C CB  . LYS C  1 313 ? 75.567  75.936  263.578 1.00 185.91 ?  344 LYS C CB  1 
ATOM   6977  C CG  . LYS C  1 313 ? 76.014  75.617  264.990 1.00 181.61 ?  344 LYS C CG  1 
ATOM   6978  C CD  . LYS C  1 313 ? 76.272  74.117  265.129 1.00 176.63 ?  344 LYS C CD  1 
ATOM   6979  C CE  . LYS C  1 313 ? 77.258  73.632  264.069 1.00 171.87 ?  344 LYS C CE  1 
ATOM   6980  N NZ  . LYS C  1 313 ? 77.512  72.164  264.128 1.00 168.54 1  344 LYS C NZ  1 
ATOM   6981  N N   . VAL C  1 314 ? 76.688  78.810  262.455 1.00 176.50 ?  345 VAL C N   1 
ATOM   6982  C CA  . VAL C  1 314 ? 77.693  79.859  262.567 1.00 176.67 ?  345 VAL C CA  1 
ATOM   6983  C C   . VAL C  1 314 ? 77.038  81.233  262.603 1.00 181.01 ?  345 VAL C C   1 
ATOM   6984  O O   . VAL C  1 314 ? 77.392  82.083  263.426 1.00 181.85 ?  345 VAL C O   1 
ATOM   6985  C CB  . VAL C  1 314 ? 78.695  79.746  261.405 1.00 175.19 ?  345 VAL C CB  1 
ATOM   6986  C CG1 . VAL C  1 314 ? 79.635  80.935  261.406 1.00 176.25 ?  345 VAL C CG1 1 
ATOM   6987  C CG2 . VAL C  1 314 ? 79.464  78.434  261.482 1.00 170.95 ?  345 VAL C CG2 1 
ATOM   6988  N N   . VAL C  1 315 ? 76.057  81.457  261.723 1.00 191.17 ?  346 VAL C N   1 
ATOM   6989  C CA  . VAL C  1 315 ? 75.390  82.753  261.630 1.00 195.89 ?  346 VAL C CA  1 
ATOM   6990  C C   . VAL C  1 315 ? 74.641  83.087  262.912 1.00 197.93 ?  346 VAL C C   1 
ATOM   6991  O O   . VAL C  1 315 ? 74.469  84.266  263.248 1.00 201.12 ?  346 VAL C O   1 
ATOM   6992  C CB  . VAL C  1 315 ? 74.463  82.786  260.397 1.00 198.85 ?  346 VAL C CB  1 
ATOM   6993  C CG1 . VAL C  1 315 ? 73.326  81.803  260.562 1.00 199.02 ?  346 VAL C CG1 1 
ATOM   6994  C CG2 . VAL C  1 315 ? 73.936  84.191  260.156 1.00 204.02 ?  346 VAL C CG2 1 
ATOM   6995  N N   . LYS C  1 316 ? 74.203  82.072  263.663 1.00 199.52 ?  347 LYS C N   1 
ATOM   6996  C CA  . LYS C  1 316 ? 73.528  82.356  264.923 1.00 202.23 ?  347 LYS C CA  1 
ATOM   6997  C C   . LYS C  1 316 ? 74.510  82.892  265.955 1.00 196.46 ?  347 LYS C C   1 
ATOM   6998  O O   . LYS C  1 316 ? 74.094  83.568  266.902 1.00 198.89 ?  347 LYS C O   1 
ATOM   6999  C CB  . LYS C  1 316 ? 72.796  81.110  265.423 1.00 201.55 ?  347 LYS C CB  1 
ATOM   7000  C CG  . LYS C  1 316 ? 71.521  80.824  264.618 1.00 214.36 ?  347 LYS C CG  1 
ATOM   7001  C CD  . LYS C  1 316 ? 70.487  81.943  264.738 1.00 223.54 ?  347 LYS C CD  1 
ATOM   7002  C CE  . LYS C  1 316 ? 69.203  81.620  263.968 1.00 230.57 ?  347 LYS C CE  1 
ATOM   7003  N NZ  . LYS C  1 316 ? 69.427  81.445  262.499 1.00 230.08 1  347 LYS C NZ  1 
ATOM   7004  N N   . GLN C  1 317 ? 75.800  82.602  265.787 1.00 185.71 ?  348 GLN C N   1 
ATOM   7005  C CA  . GLN C  1 317 ? 76.844  83.123  266.656 1.00 184.31 ?  348 GLN C CA  1 
ATOM   7006  C C   . GLN C  1 317 ? 77.365  84.449  266.134 1.00 186.95 ?  348 GLN C C   1 
ATOM   7007  O O   . GLN C  1 317 ? 77.896  85.251  266.911 1.00 187.80 ?  348 GLN C O   1 
ATOM   7008  C CB  . GLN C  1 317 ? 78.011  82.137  266.761 1.00 179.48 ?  348 GLN C CB  1 
ATOM   7009  C CG  . GLN C  1 317 ? 77.680  80.803  267.395 1.00 176.72 ?  348 GLN C CG  1 
ATOM   7010  C CD  . GLN C  1 317 ? 77.394  80.914  268.879 1.00 176.97 ?  348 GLN C CD  1 
ATOM   7011  O OE1 . GLN C  1 317 ? 77.835  81.855  269.541 1.00 177.99 ?  348 GLN C OE1 1 
ATOM   7012  N NE2 . GLN C  1 317 ? 76.680  79.934  269.418 1.00 176.10 ?  348 GLN C NE2 1 
ATOM   7013  N N   . LEU C  1 318 ? 77.207  84.685  264.828 1.00 186.10 ?  349 LEU C N   1 
ATOM   7014  C CA  . LEU C  1 318 ? 77.659  85.923  264.208 1.00 189.01 ?  349 LEU C CA  1 
ATOM   7015  C C   . LEU C  1 318 ? 76.736  87.081  264.554 1.00 194.23 ?  349 LEU C C   1 
ATOM   7016  O O   . LEU C  1 318 ? 77.176  88.234  264.591 1.00 196.80 ?  349 LEU C O   1 
ATOM   7017  C CB  . LEU C  1 318 ? 77.735  85.740  262.694 1.00 189.17 ?  349 LEU C CB  1 
ATOM   7018  C CG  . LEU C  1 318 ? 78.722  84.682  262.200 1.00 184.55 ?  349 LEU C CG  1 
ATOM   7019  C CD1 . LEU C  1 318 ? 78.744  84.627  260.682 1.00 185.28 ?  349 LEU C CD1 1 
ATOM   7020  C CD2 . LEU C  1 318 ? 80.112  84.933  262.755 1.00 182.30 ?  349 LEU C CD2 1 
ATOM   7021  N N   . ARG C  1 319 ? 75.459  86.796  264.818 1.00 204.69 ?  350 ARG C N   1 
ATOM   7022  C CA  . ARG C  1 319 ? 74.515  87.844  265.182 1.00 214.87 ?  350 ARG C CA  1 
ATOM   7023  C C   . ARG C  1 319 ? 74.737  88.322  266.604 1.00 214.44 ?  350 ARG C C   1 
ATOM   7024  O O   . ARG C  1 319 ? 74.182  89.351  266.995 1.00 223.86 ?  350 ARG C O   1 
ATOM   7025  C CB  . ARG C  1 319 ? 73.063  87.384  265.034 1.00 218.16 ?  350 ARG C CB  1 
ATOM   7026  C CG  . ARG C  1 319 ? 72.624  87.056  263.620 1.00 220.02 ?  350 ARG C CG  1 
ATOM   7027  C CD  . ARG C  1 319 ? 71.119  86.817  263.560 1.00 227.06 ?  350 ARG C CD  1 
ATOM   7028  N NE  . ARG C  1 319 ? 70.657  86.476  262.220 1.00 226.15 ?  350 ARG C NE  1 
ATOM   7029  C CZ  . ARG C  1 319 ? 70.490  85.225  261.807 1.00 223.80 ?  350 ARG C CZ  1 
ATOM   7030  N NH1 . ARG C  1 319 ? 70.743  84.223  262.634 1.00 221.14 1  350 ARG C NH1 1 
ATOM   7031  N NH2 . ARG C  1 319 ? 70.072  84.969  260.579 1.00 222.66 ?  350 ARG C NH2 1 
ATOM   7032  N N   . LYS C  1 320 ? 75.530  87.597  267.386 1.00 214.24 ?  351 LYS C N   1 
ATOM   7033  C CA  . LYS C  1 320 ? 75.834  87.994  268.750 1.00 213.06 ?  351 LYS C CA  1 
ATOM   7034  C C   . LYS C  1 320 ? 76.873  89.101  268.804 1.00 213.49 ?  351 LYS C C   1 
ATOM   7035  O O   . LYS C  1 320 ? 77.131  89.639  269.886 1.00 215.06 ?  351 LYS C O   1 
ATOM   7036  C CB  . LYS C  1 320 ? 76.341  86.782  269.530 1.00 207.08 ?  351 LYS C CB  1 
ATOM   7037  C CG  . LYS C  1 320 ? 75.285  85.727  269.796 1.00 206.75 ?  351 LYS C CG  1 
ATOM   7038  C CD  . LYS C  1 320 ? 75.849  84.588  270.620 1.00 197.92 ?  351 LYS C CD  1 
ATOM   7039  C CE  . LYS C  1 320 ? 74.754  83.619  271.016 1.00 197.06 ?  351 LYS C CE  1 
ATOM   7040  N NZ  . LYS C  1 320 ? 74.083  83.035  269.818 1.00 204.68 1  351 LYS C NZ  1 
ATOM   7041  N N   . HIS C  1 321 ? 77.468  89.452  267.665 1.00 212.43 ?  352 HIS C N   1 
ATOM   7042  C CA  . HIS C  1 321 ? 78.491  90.479  267.599 1.00 213.81 ?  352 HIS C CA  1 
ATOM   7043  C C   . HIS C  1 321 ? 78.153  91.592  266.621 1.00 219.01 ?  352 HIS C C   1 
ATOM   7044  O O   . HIS C  1 321 ? 78.718  92.684  266.733 1.00 221.71 ?  352 HIS C O   1 
ATOM   7045  C CB  . HIS C  1 321 ? 79.836  89.857  267.189 1.00 209.38 ?  352 HIS C CB  1 
ATOM   7046  C CG  . HIS C  1 321 ? 80.309  88.780  268.115 1.00 204.50 ?  352 HIS C CG  1 
ATOM   7047  N ND1 . HIS C  1 321 ? 79.816  87.492  268.072 1.00 201.38 ?  352 HIS C ND1 1 
ATOM   7048  C CD2 . HIS C  1 321 ? 81.218  88.800  269.118 1.00 202.47 ?  352 HIS C CD2 1 
ATOM   7049  C CE1 . HIS C  1 321 ? 80.411  86.763  268.999 1.00 197.69 ?  352 HIS C CE1 1 
ATOM   7050  N NE2 . HIS C  1 321 ? 81.265  87.533  269.649 1.00 198.21 ?  352 HIS C NE2 1 
ATOM   7051  N N   . PHE C  1 322 ? 77.274  91.336  265.659 1.00 221.75 ?  353 PHE C N   1 
ATOM   7052  C CA  . PHE C  1 322 ? 76.903  92.289  264.624 1.00 226.73 ?  353 PHE C CA  1 
ATOM   7053  C C   . PHE C  1 322 ? 75.416  92.614  264.708 1.00 231.38 ?  353 PHE C C   1 
ATOM   7054  O O   . PHE C  1 322 ? 74.782  92.965  263.710 1.00 235.53 ?  353 PHE C O   1 
ATOM   7055  C CB  . PHE C  1 322 ? 77.290  91.730  263.261 1.00 224.89 ?  353 PHE C CB  1 
ATOM   7056  C CG  . PHE C  1 322 ? 78.777  91.597  263.079 1.00 221.42 ?  353 PHE C CG  1 
ATOM   7057  C CD1 . PHE C  1 322 ? 79.538  92.655  262.615 1.00 224.16 ?  353 PHE C CD1 1 
ATOM   7058  C CD2 . PHE C  1 322 ? 79.420  90.411  263.413 1.00 215.75 ?  353 PHE C CD2 1 
ATOM   7059  C CE1 . PHE C  1 322 ? 80.906  92.525  262.461 1.00 221.21 ?  353 PHE C CE1 1 
ATOM   7060  C CE2 . PHE C  1 322 ? 80.786  90.276  263.261 1.00 212.83 ?  353 PHE C CE2 1 
ATOM   7061  C CZ  . PHE C  1 322 ? 81.530  91.334  262.785 1.00 215.53 ?  353 PHE C CZ  1 
ATOM   7062  N N   . GLY C  1 323 ? 74.856  92.515  265.907 1.00 231.06 ?  354 GLY C N   1 
ATOM   7063  C CA  . GLY C  1 323 ? 73.442  92.764  266.089 1.00 242.31 ?  354 GLY C CA  1 
ATOM   7064  C C   . GLY C  1 323 ? 72.585  91.515  266.010 1.00 244.89 ?  354 GLY C C   1 
ATOM   7065  O O   . GLY C  1 323 ? 72.773  90.665  265.127 1.00 239.34 ?  354 GLY C O   1 
ATOM   7066  N N   . ASN C  1 324 ? 71.581  91.455  266.903 1.00 243.59 ?  355 ASN C N   1 
ATOM   7067  C CA  . ASN C  1 324 ? 70.713  90.281  267.015 1.00 240.15 ?  355 ASN C CA  1 
ATOM   7068  C C   . ASN C  1 324 ? 69.912  90.031  265.770 1.00 243.43 ?  355 ASN C C   1 
ATOM   7069  O O   . ASN C  1 324 ? 69.799  88.887  265.317 1.00 238.35 ?  355 ASN C O   1 
ATOM   7070  C CB  . ASN C  1 324 ? 69.669  90.469  268.130 1.00 243.36 ?  355 ASN C CB  1 
ATOM   7071  C CG  . ASN C  1 324 ? 69.395  89.192  268.950 1.00 249.47 ?  355 ASN C CG  1 
ATOM   7072  O OD1 . ASN C  1 324 ? 68.658  88.315  268.471 1.00 255.76 ?  355 ASN C OD1 1 
ATOM   7073  N ND2 . ASN C  1 324 ? 69.960  89.098  270.176 1.00 262.76 ?  355 ASN C ND2 1 
ATOM   7074  N N   . ASN C  1 325 ? 69.334  91.089  265.219 1.00 238.83 ?  356 ASN C N   1 
ATOM   7075  C CA  . ASN C  1 325 ? 68.490  91.061  264.037 1.00 234.78 ?  356 ASN C CA  1 
ATOM   7076  C C   . ASN C  1 325 ? 69.217  91.678  262.845 1.00 229.63 ?  356 ASN C C   1 
ATOM   7077  O O   . ASN C  1 325 ? 68.925  92.804  262.443 1.00 233.15 ?  356 ASN C O   1 
ATOM   7078  C CB  . ASN C  1 325 ? 67.162  91.799  264.331 1.00 243.85 ?  356 ASN C CB  1 
ATOM   7079  C CG  . ASN C  1 325 ? 66.365  91.158  265.459 1.00 247.55 ?  356 ASN C CG  1 
ATOM   7080  O OD1 . ASN C  1 325 ? 66.906  90.422  266.283 1.00 245.76 ?  356 ASN C OD1 1 
ATOM   7081  N ND2 . ASN C  1 325 ? 65.062  91.421  265.482 1.00 252.51 ?  356 ASN C ND2 1 
ATOM   7082  N N   . THR C  1 326 ? 70.167  90.941  262.278 1.00 237.22 ?  357 THR C N   1 
ATOM   7083  C CA  . THR C  1 326 ? 70.925  91.419  261.132 1.00 237.28 ?  357 THR C CA  1 
ATOM   7084  C C   . THR C  1 326 ? 70.978  90.341  260.061 1.00 232.95 ?  357 THR C C   1 
ATOM   7085  O O   . THR C  1 326 ? 70.758  89.155  260.328 1.00 226.66 ?  357 THR C O   1 
ATOM   7086  C CB  . THR C  1 326 ? 72.353  91.792  261.535 1.00 232.76 ?  357 THR C CB  1 
ATOM   7087  O OG1 . THR C  1 326 ? 73.038  92.407  260.434 1.00 236.75 ?  357 THR C OG1 1 
ATOM   7088  C CG2 . THR C  1 326 ? 73.088  90.548  261.980 1.00 224.93 ?  357 THR C CG2 1 
ATOM   7089  N N   . ILE C  1 327 ? 71.270  90.782  258.838 1.00 224.05 ?  358 ILE C N   1 
ATOM   7090  C CA  . ILE C  1 327 ? 71.370  89.914  257.671 1.00 221.50 ?  358 ILE C CA  1 
ATOM   7091  C C   . ILE C  1 327 ? 72.840  89.632  257.394 1.00 216.81 ?  358 ILE C C   1 
ATOM   7092  O O   . ILE C  1 327 ? 73.643  90.561  257.241 1.00 218.26 ?  358 ILE C O   1 
ATOM   7093  C CB  . ILE C  1 327 ? 70.686  90.550  256.450 1.00 226.66 ?  358 ILE C CB  1 
ATOM   7094  C CG1 . ILE C  1 327 ? 69.209  90.819  256.752 1.00 231.68 ?  358 ILE C CG1 1 
ATOM   7095  C CG2 . ILE C  1 327 ? 70.817  89.649  255.242 1.00 223.84 ?  358 ILE C CG2 1 
ATOM   7096  C CD1 . ILE C  1 327 ? 68.438  91.409  255.589 1.00 237.11 ?  358 ILE C CD1 1 
ATOM   7097  N N   . ILE C  1 328 ? 73.189  88.352  257.332 1.00 220.33 ?  359 ILE C N   1 
ATOM   7098  C CA  . ILE C  1 328 ? 74.543  87.888  257.058 1.00 212.91 ?  359 ILE C CA  1 
ATOM   7099  C C   . ILE C  1 328 ? 74.565  87.212  255.693 1.00 207.09 ?  359 ILE C C   1 
ATOM   7100  O O   . ILE C  1 328 ? 73.828  86.244  255.467 1.00 204.80 ?  359 ILE C O   1 
ATOM   7101  C CB  . ILE C  1 328 ? 75.039  86.938  258.154 1.00 208.35 ?  359 ILE C CB  1 
ATOM   7102  C CG1 . ILE C  1 328 ? 75.025  87.661  259.502 1.00 208.25 ?  359 ILE C CG1 1 
ATOM   7103  C CG2 . ILE C  1 328 ? 76.428  86.421  257.821 1.00 200.45 ?  359 ILE C CG2 1 
ATOM   7104  C CD1 . ILE C  1 328 ? 75.877  88.906  259.532 1.00 207.41 ?  359 ILE C CD1 1 
ATOM   7105  N N   . ARG C  1 329 ? 75.394  87.719  254.780 1.00 203.23 ?  360 ARG C N   1 
ATOM   7106  C CA  . ARG C  1 329 ? 75.494  87.172  253.432 1.00 200.91 ?  360 ARG C CA  1 
ATOM   7107  C C   . ARG C  1 329 ? 76.892  86.600  253.248 1.00 193.25 ?  360 ARG C C   1 
ATOM   7108  O O   . ARG C  1 329 ? 77.884  87.212  253.661 1.00 194.14 ?  360 ARG C O   1 
ATOM   7109  C CB  . ARG C  1 329 ? 75.233  88.238  252.355 1.00 207.91 ?  360 ARG C CB  1 
ATOM   7110  C CG  . ARG C  1 329 ? 75.185  87.673  250.934 1.00 206.96 ?  360 ARG C CG  1 
ATOM   7111  C CD  . ARG C  1 329 ? 74.928  88.736  249.871 1.00 215.55 ?  360 ARG C CD  1 
ATOM   7112  N NE  . ARG C  1 329 ? 76.045  89.664  249.717 1.00 218.50 ?  360 ARG C NE  1 
ATOM   7113  C CZ  . ARG C  1 329 ? 77.029  89.492  248.838 1.00 217.53 ?  360 ARG C CZ  1 
ATOM   7114  N NH1 . ARG C  1 329 ? 77.026  88.429  248.043 1.00 214.40 1  360 ARG C NH1 1 
ATOM   7115  N NH2 . ARG C  1 329 ? 78.011  90.378  248.750 1.00 217.89 ?  360 ARG C NH2 1 
ATOM   7116  N N   . PHE C  1 330 ? 76.964  85.421  252.635 1.00 201.30 ?  361 PHE C N   1 
ATOM   7117  C CA  . PHE C  1 330 ? 78.224  84.749  252.346 1.00 195.50 ?  361 PHE C CA  1 
ATOM   7118  C C   . PHE C  1 330 ? 78.518  84.882  250.854 1.00 191.36 ?  361 PHE C C   1 
ATOM   7119  O O   . PHE C  1 330 ? 77.650  84.606  250.019 1.00 194.60 ?  361 PHE C O   1 
ATOM   7120  C CB  . PHE C  1 330 ? 78.144  83.291  252.803 1.00 193.07 ?  361 PHE C CB  1 
ATOM   7121  C CG  . PHE C  1 330 ? 77.990  83.153  254.299 1.00 192.88 ?  361 PHE C CG  1 
ATOM   7122  C CD1 . PHE C  1 330 ? 79.089  83.245  255.138 1.00 188.15 ?  361 PHE C CD1 1 
ATOM   7123  C CD2 . PHE C  1 330 ? 76.736  82.970  254.866 1.00 192.36 ?  361 PHE C CD2 1 
ATOM   7124  C CE1 . PHE C  1 330 ? 78.942  83.141  256.512 1.00 185.13 ?  361 PHE C CE1 1 
ATOM   7125  C CE2 . PHE C  1 330 ? 76.584  82.864  256.239 1.00 191.59 ?  361 PHE C CE2 1 
ATOM   7126  C CZ  . PHE C  1 330 ? 77.690  82.949  257.062 1.00 187.55 ?  361 PHE C CZ  1 
ATOM   7127  N N   . ALA C  1 331 ? 79.748  85.286  250.530 1.00 182.61 ?  362 ALA C N   1 
ATOM   7128  C CA  . ALA C  1 331 ? 80.209  85.470  249.157 1.00 189.04 ?  362 ALA C CA  1 
ATOM   7129  C C   . ALA C  1 331 ? 81.608  84.891  248.987 1.00 184.34 ?  362 ALA C C   1 
ATOM   7130  O O   . ALA C  1 331 ? 82.360  84.744  249.952 1.00 179.72 ?  362 ALA C O   1 
ATOM   7131  C CB  . ALA C  1 331 ? 80.201  86.949  248.754 1.00 199.52 ?  362 ALA C CB  1 
ATOM   7132  N N   . ASN C  1 332 ? 81.945  84.551  247.741 1.00 190.84 ?  363 ASN C N   1 
ATOM   7133  C CA  . ASN C  1 332 ? 83.244  83.961  247.448 1.00 183.65 ?  363 ASN C CA  1 
ATOM   7134  C C   . ASN C  1 332 ? 84.353  85.009  247.613 1.00 184.09 ?  363 ASN C C   1 
ATOM   7135  O O   . ASN C  1 332 ? 84.106  86.182  247.912 1.00 190.84 ?  363 ASN C O   1 
ATOM   7136  C CB  . ASN C  1 332 ? 83.241  83.369  246.034 1.00 187.43 ?  363 ASN C CB  1 
ATOM   7137  C CG  . ASN C  1 332 ? 82.863  84.396  244.966 1.00 199.38 ?  363 ASN C CG  1 
ATOM   7138  O OD1 . ASN C  1 332 ? 82.301  85.445  245.280 1.00 208.61 ?  363 ASN C OD1 1 
ATOM   7139  N ND2 . ASN C  1 332 ? 83.171  84.095  243.698 1.00 203.51 ?  363 ASN C ND2 1 
ATOM   7140  N N   . SER C  1 333 ? 85.595  84.569  247.406 1.00 179.45 ?  364 SER C N   1 
ATOM   7141  C CA  . SER C  1 333 ? 86.781  85.401  247.599 1.00 182.47 ?  364 SER C CA  1 
ATOM   7142  C C   . SER C  1 333 ? 86.808  86.618  246.674 1.00 191.76 ?  364 SER C C   1 
ATOM   7143  O O   . SER C  1 333 ? 86.135  86.669  245.641 1.00 199.82 ?  364 SER C O   1 
ATOM   7144  C CB  . SER C  1 333 ? 88.047  84.571  247.390 1.00 177.03 ?  364 SER C CB  1 
ATOM   7145  O OG  . SER C  1 333 ? 89.211  85.355  247.592 1.00 179.54 ?  364 SER C OG  1 
ATOM   7146  N N   . SER C  1 334 ? 87.548  87.647  247.105 1.00 180.03 ?  365 SER C N   1 
ATOM   7147  C CA  . SER C  1 334 ? 87.648  88.855  246.293 1.00 184.96 ?  365 SER C CA  1 
ATOM   7148  C C   . SER C  1 334 ? 88.611  88.684  245.116 1.00 184.64 ?  365 SER C C   1 
ATOM   7149  O O   . SER C  1 334 ? 88.312  89.136  244.004 1.00 190.67 ?  365 SER C O   1 
ATOM   7150  C CB  . SER C  1 334 ? 88.084  90.032  247.167 1.00 191.45 ?  365 SER C CB  1 
ATOM   7151  O OG  . SER C  1 334 ? 87.154  90.275  248.209 1.00 194.31 ?  365 SER C OG  1 
ATOM   7152  N N   . GLY C  1 335 ? 89.769  88.046  245.329 1.00 189.83 ?  366 GLY C N   1 
ATOM   7153  C CA  . GLY C  1 335 ? 90.720  87.837  244.244 1.00 190.70 ?  366 GLY C CA  1 
ATOM   7154  C C   . GLY C  1 335 ? 92.209  87.906  244.557 1.00 191.18 ?  366 GLY C C   1 
ATOM   7155  O O   . GLY C  1 335 ? 92.610  88.250  245.673 1.00 189.50 ?  366 GLY C O   1 
ATOM   7156  N N   . GLY C  1 336 ? 93.038  87.583  243.557 1.00 193.32 ?  367 GLY C N   1 
ATOM   7157  C CA  . GLY C  1 336 ? 94.492  87.609  243.639 1.00 194.75 ?  367 GLY C CA  1 
ATOM   7158  C C   . GLY C  1 336 ? 95.137  86.318  243.172 1.00 193.64 ?  367 GLY C C   1 
ATOM   7159  O O   . GLY C  1 336 ? 94.735  85.743  242.155 1.00 192.56 ?  367 GLY C O   1 
ATOM   7160  N N   . ASP C  1 337 ? 96.148  85.860  243.908 1.00 186.21 ?  368 ASP C N   1 
ATOM   7161  C CA  . ASP C  1 337 ? 96.850  84.625  243.583 1.00 184.99 ?  368 ASP C CA  1 
ATOM   7162  C C   . ASP C  1 337 ? 95.938  83.426  243.858 1.00 182.18 ?  368 ASP C C   1 
ATOM   7163  O O   . ASP C  1 337 ? 94.925  83.523  244.556 1.00 181.28 ?  368 ASP C O   1 
ATOM   7164  C CB  . ASP C  1 337 ? 98.221  84.528  244.267 1.00 185.51 ?  368 ASP C CB  1 
ATOM   7165  C CG  . ASP C  1 337 ? 98.192  84.879  245.726 1.00 184.52 ?  368 ASP C CG  1 
ATOM   7166  O OD1 . ASP C  1 337 ? 97.141  85.341  246.205 1.00 184.58 ?  368 ASP C OD1 1 
ATOM   7167  O OD2 . ASP C  1 337 ? 99.240  84.705  246.388 1.00 184.67 -1 368 ASP C OD2 1 
ATOM   7168  N N   . LEU C  1 338 ? 96.321  82.282  243.296 1.00 182.63 ?  369 LEU C N   1 
ATOM   7169  C CA  . LEU C  1 338 ? 95.542  81.053  243.425 1.00 170.56 ?  369 LEU C CA  1 
ATOM   7170  C C   . LEU C  1 338 ? 95.556  80.452  244.829 1.00 168.73 ?  369 LEU C C   1 
ATOM   7171  O O   . LEU C  1 338 ? 94.595  79.774  245.207 1.00 163.65 ?  369 LEU C O   1 
ATOM   7172  C CB  . LEU C  1 338 ? 96.071  80.017  242.437 1.00 162.67 ?  369 LEU C CB  1 
ATOM   7173  C CG  . LEU C  1 338 ? 95.261  78.734  242.255 1.00 159.66 ?  369 LEU C CG  1 
ATOM   7174  C CD1 . LEU C  1 338 ? 93.893  79.029  241.660 1.00 162.23 ?  369 LEU C CD1 1 
ATOM   7175  C CD2 . LEU C  1 338 ? 96.027  77.725  241.417 1.00 157.86 ?  369 LEU C CD2 1 
ATOM   7176  N N   . GLU C  1 339 ? 96.597  80.686  245.624 1.00 165.26 ?  370 GLU C N   1 
ATOM   7177  C CA  . GLU C  1 339 ? 96.626  80.091  246.959 1.00 161.04 ?  370 GLU C CA  1 
ATOM   7178  C C   . GLU C  1 339 ? 95.670  80.757  247.943 1.00 163.21 ?  370 GLU C C   1 
ATOM   7179  O O   . GLU C  1 339 ? 95.420  80.193  249.014 1.00 158.73 ?  370 GLU C O   1 
ATOM   7180  C CB  . GLU C  1 339 ? 98.056  80.117  247.492 1.00 161.26 ?  370 GLU C CB  1 
ATOM   7181  C CG  . GLU C  1 339 ? 98.950  79.123  246.775 1.00 155.44 ?  370 GLU C CG  1 
ATOM   7182  C CD  . GLU C  1 339 ? 99.965  79.796  245.880 1.00 159.86 ?  370 GLU C CD  1 
ATOM   7183  O OE1 . GLU C  1 339 ? 100.100 81.034  245.963 1.00 169.30 ?  370 GLU C OE1 1 
ATOM   7184  O OE2 . GLU C  1 339 ? 100.617 79.091  245.081 1.00 157.41 -1 370 GLU C OE2 1 
ATOM   7185  N N   . VAL C  1 340 ? 95.131  81.925  247.614 1.00 172.28 ?  371 VAL C N   1 
ATOM   7186  C CA  . VAL C  1 340 ? 94.234  82.660  248.497 1.00 170.56 ?  371 VAL C CA  1 
ATOM   7187  C C   . VAL C  1 340 ? 92.776  82.492  248.082 1.00 170.78 ?  371 VAL C C   1 
ATOM   7188  O O   . VAL C  1 340 ? 91.888  82.441  248.934 1.00 168.22 ?  371 VAL C O   1 
ATOM   7189  C CB  . VAL C  1 340 ? 94.628  84.152  248.565 1.00 174.73 ?  371 VAL C CB  1 
ATOM   7190  C CG1 . VAL C  1 340 ? 93.783  84.871  249.600 1.00 170.46 ?  371 VAL C CG1 1 
ATOM   7191  C CG2 . VAL C  1 340 ? 96.097  84.282  248.935 1.00 174.65 ?  371 VAL C CG2 1 
ATOM   7192  N N   . THR C  1 341 ? 92.512  82.402  246.773 1.00 181.17 ?  372 THR C N   1 
ATOM   7193  C CA  . THR C  1 341 ? 91.151  82.306  246.254 1.00 177.72 ?  372 THR C CA  1 
ATOM   7194  C C   . THR C  1 341 ? 90.583  80.889  246.275 1.00 167.10 ?  372 THR C C   1 
ATOM   7195  O O   . THR C  1 341 ? 89.364  80.731  246.135 1.00 163.94 ?  372 THR C O   1 
ATOM   7196  C CB  . THR C  1 341 ? 91.113  82.816  244.806 1.00 178.28 ?  372 THR C CB  1 
ATOM   7197  O OG1 . THR C  1 341 ? 91.990  82.025  243.994 1.00 173.51 ?  372 THR C OG1 1 
ATOM   7198  C CG2 . THR C  1 341 ? 91.578  84.263  244.729 1.00 185.04 ?  372 THR C CG2 1 
ATOM   7199  N N   . THR C  1 342 ? 91.411  79.862  246.454 1.00 162.84 ?  373 THR C N   1 
ATOM   7200  C CA  . THR C  1 342 ? 90.954  78.480  246.441 1.00 159.76 ?  373 THR C CA  1 
ATOM   7201  C C   . THR C  1 342 ? 91.359  77.765  247.724 1.00 157.03 ?  373 THR C C   1 
ATOM   7202  O O   . THR C  1 342 ? 92.255  78.202  248.451 1.00 157.05 ?  373 THR C O   1 
ATOM   7203  C CB  . THR C  1 342 ? 91.510  77.719  245.233 1.00 158.58 ?  373 THR C CB  1 
ATOM   7204  O OG1 . THR C  1 342 ? 92.942  77.715  245.290 1.00 158.01 ?  373 THR C OG1 1 
ATOM   7205  C CG2 . THR C  1 342 ? 91.037  78.362  243.930 1.00 161.27 ?  373 THR C CG2 1 
ATOM   7206  N N   . HIS C  1 343 ? 90.684  76.650  247.996 1.00 146.49 ?  374 HIS C N   1 
ATOM   7207  C CA  . HIS C  1 343 ? 91.004  75.823  249.158 1.00 143.97 ?  374 HIS C CA  1 
ATOM   7208  C C   . HIS C  1 343 ? 92.224  74.977  248.816 1.00 142.07 ?  374 HIS C C   1 
ATOM   7209  O O   . HIS C  1 343 ? 92.120  73.881  248.262 1.00 140.62 ?  374 HIS C O   1 
ATOM   7210  C CB  . HIS C  1 343 ? 89.821  74.956  249.564 1.00 142.72 ?  374 HIS C CB  1 
ATOM   7211  C CG  . HIS C  1 343 ? 90.159  73.944  250.614 1.00 140.18 ?  374 HIS C CG  1 
ATOM   7212  N ND1 . HIS C  1 343 ? 90.954  74.239  251.700 1.00 139.72 ?  374 HIS C ND1 1 
ATOM   7213  C CD2 . HIS C  1 343 ? 89.841  72.633  250.724 1.00 138.26 ?  374 HIS C CD2 1 
ATOM   7214  C CE1 . HIS C  1 343 ? 91.094  73.158  252.446 1.00 137.55 ?  374 HIS C CE1 1 
ATOM   7215  N NE2 . HIS C  1 343 ? 90.430  72.169  251.875 1.00 136.72 ?  374 HIS C NE2 1 
ATOM   7216  N N   . SER C  1 344 ? 93.399  75.507  249.141 1.00 145.55 ?  375 SER C N   1 
ATOM   7217  C CA  . SER C  1 344 ? 94.662  74.838  248.863 1.00 144.22 ?  375 SER C CA  1 
ATOM   7218  C C   . SER C  1 344 ? 94.955  73.809  249.946 1.00 141.76 ?  375 SER C C   1 
ATOM   7219  O O   . SER C  1 344 ? 94.864  74.113  251.139 1.00 141.55 ?  375 SER C O   1 
ATOM   7220  C CB  . SER C  1 344 ? 95.795  75.860  248.790 1.00 145.98 ?  375 SER C CB  1 
ATOM   7221  O OG  . SER C  1 344 ? 97.048  75.255  249.070 1.00 144.70 ?  375 SER C OG  1 
ATOM   7222  N N   . PHE C  1 345 ? 95.308  72.593  249.537 1.00 140.96 ?  376 PHE C N   1 
ATOM   7223  C CA  . PHE C  1 345 ? 95.672  71.558  250.497 1.00 138.96 ?  376 PHE C CA  1 
ATOM   7224  C C   . PHE C  1 345 ? 96.438  70.451  249.788 1.00 137.94 ?  376 PHE C C   1 
ATOM   7225  O O   . PHE C  1 345 ? 96.597  70.453  248.564 1.00 138.51 ?  376 PHE C O   1 
ATOM   7226  C CB  . PHE C  1 345 ? 94.441  70.983  251.211 1.00 137.98 ?  376 PHE C CB  1 
ATOM   7227  C CG  . PHE C  1 345 ? 93.556  70.135  250.330 1.00 137.64 ?  376 PHE C CG  1 
ATOM   7228  C CD1 . PHE C  1 345 ? 92.588  70.718  249.532 1.00 139.04 ?  376 PHE C CD1 1 
ATOM   7229  C CD2 . PHE C  1 345 ? 93.694  68.752  250.301 1.00 136.16 ?  376 PHE C CD2 1 
ATOM   7230  C CE1 . PHE C  1 345 ? 91.768  69.943  248.726 1.00 138.87 ?  376 PHE C CE1 1 
ATOM   7231  C CE2 . PHE C  1 345 ? 92.880  67.972  249.491 1.00 136.04 ?  376 PHE C CE2 1 
ATOM   7232  C CZ  . PHE C  1 345 ? 91.917  68.568  248.705 1.00 137.33 ?  376 PHE C CZ  1 
ATOM   7233  N N   . ASN C  1 346 ? 96.913  69.500  250.587 1.00 145.32 ?  377 ASN C N   1 
ATOM   7234  C CA  . ASN C  1 346 ? 97.683  68.352  250.132 1.00 144.58 ?  377 ASN C CA  1 
ATOM   7235  C C   . ASN C  1 346 ? 96.935  67.081  250.492 1.00 143.32 ?  377 ASN C C   1 
ATOM   7236  O O   . ASN C  1 346 ? 96.450  66.933  251.619 1.00 142.75 ?  377 ASN C O   1 
ATOM   7237  C CB  . ASN C  1 346 ? 99.081  68.314  250.757 1.00 144.69 ?  377 ASN C CB  1 
ATOM   7238  C CG  . ASN C  1 346 ? 100.020 67.350  250.040 1.00 144.62 ?  377 ASN C CG  1 
ATOM   7239  O OD1 . ASN C  1 346 ? 99.594  66.311  249.533 1.00 143.95 ?  377 ASN C OD1 1 
ATOM   7240  N ND2 . ASN C  1 346 ? 101.306 67.670  250.034 1.00 145.52 ?  377 ASN C ND2 1 
ATOM   7241  N N   . CYS C  1 347 ? 96.852  66.173  249.530 1.00 156.89 ?  378 CYS C N   1 
ATOM   7242  C CA  . CYS C  1 347 ? 96.196  64.884  249.712 1.00 156.13 ?  378 CYS C CA  1 
ATOM   7243  C C   . CYS C  1 347 ? 96.816  63.814  248.824 1.00 156.10 ?  378 CYS C C   1 
ATOM   7244  O O   . CYS C  1 347 ? 96.639  63.819  247.600 1.00 156.50 ?  378 CYS C O   1 
ATOM   7245  C CB  . CYS C  1 347 ? 94.695  65.010  249.507 1.00 156.23 ?  378 CYS C CB  1 
ATOM   7246  S SG  . CYS C  1 347 ? 93.988  63.432  249.730 1.00 155.93 ?  378 CYS C SG  1 
ATOM   7247  N N   . GLY C  1 348 ? 97.558  62.905  249.462 1.00 164.85 ?  379 GLY C N   1 
ATOM   7248  C CA  . GLY C  1 348 ? 98.205  61.811  248.776 1.00 160.81 ?  379 GLY C CA  1 
ATOM   7249  C C   . GLY C  1 348 ? 99.486  62.221  248.096 1.00 162.05 ?  379 GLY C C   1 
ATOM   7250  O O   . GLY C  1 348 ? 100.004 61.465  247.266 1.00 158.77 ?  379 GLY C O   1 
ATOM   7251  N N   . GLY C  1 349 ? 100.003 63.408  248.415 1.00 156.48 ?  380 GLY C N   1 
ATOM   7252  C CA  . GLY C  1 349 ? 101.213 63.936  247.839 1.00 155.47 ?  380 GLY C CA  1 
ATOM   7253  C C   . GLY C  1 349 ? 100.946 65.030  246.826 1.00 155.03 ?  380 GLY C C   1 
ATOM   7254  O O   . GLY C  1 349 ? 101.820 65.874  246.590 1.00 154.57 ?  380 GLY C O   1 
ATOM   7255  N N   . GLU C  1 350 ? 99.753  65.034  246.233 1.00 150.29 ?  381 GLU C N   1 
ATOM   7256  C CA  . GLU C  1 350 ? 99.343  66.031  245.259 1.00 150.97 ?  381 GLU C CA  1 
ATOM   7257  C C   . GLU C  1 350 ? 98.816  67.271  245.975 1.00 155.39 ?  381 GLU C C   1 
ATOM   7258  O O   . GLU C  1 350 ? 98.352  67.212  247.117 1.00 156.98 ?  381 GLU C O   1 
ATOM   7259  C CB  . GLU C  1 350 ? 98.259  65.465  244.340 1.00 146.60 ?  381 GLU C CB  1 
ATOM   7260  C CG  . GLU C  1 350 ? 98.675  64.236  243.534 1.00 145.82 ?  381 GLU C CG  1 
ATOM   7261  C CD  . GLU C  1 350 ? 99.403  64.575  242.245 1.00 147.14 ?  381 GLU C CD  1 
ATOM   7262  O OE1 . GLU C  1 350 ? 100.042 65.645  242.181 1.00 157.40 ?  381 GLU C OE1 1 
ATOM   7263  O OE2 . GLU C  1 350 ? 99.331  63.769  241.291 1.00 140.03 -1 381 GLU C OE2 1 
ATOM   7264  N N   . PHE C  1 351 ? 98.881  68.405  245.285 1.00 135.97 ?  382 PHE C N   1 
ATOM   7265  C CA  . PHE C  1 351 ? 98.403  69.675  245.827 1.00 140.05 ?  382 PHE C CA  1 
ATOM   7266  C C   . PHE C  1 351 ? 97.142  70.136  245.105 1.00 138.98 ?  382 PHE C C   1 
ATOM   7267  O O   . PHE C  1 351 ? 97.206  70.633  243.978 1.00 138.51 ?  382 PHE C O   1 
ATOM   7268  C CB  . PHE C  1 351 ? 99.509  70.722  245.750 1.00 143.75 ?  382 PHE C CB  1 
ATOM   7269  C CG  . PHE C  1 351 ? 100.693 70.394  246.606 1.00 148.05 ?  382 PHE C CG  1 
ATOM   7270  C CD1 . PHE C  1 351 ? 100.736 70.818  247.924 1.00 152.29 ?  382 PHE C CD1 1 
ATOM   7271  C CD2 . PHE C  1 351 ? 101.742 69.634  246.115 1.00 146.61 ?  382 PHE C CD2 1 
ATOM   7272  C CE1 . PHE C  1 351 ? 101.814 70.514  248.731 1.00 153.51 ?  382 PHE C CE1 1 
ATOM   7273  C CE2 . PHE C  1 351 ? 102.825 69.324  246.921 1.00 150.02 ?  382 PHE C CE2 1 
ATOM   7274  C CZ  . PHE C  1 351 ? 102.860 69.763  248.230 1.00 153.54 ?  382 PHE C CZ  1 
ATOM   7275  N N   . PHE C  1 352 ? 95.996  69.953  245.757 1.00 131.13 ?  383 PHE C N   1 
ATOM   7276  C CA  . PHE C  1 352 ? 94.716  70.313  245.172 1.00 130.12 ?  383 PHE C CA  1 
ATOM   7277  C C   . PHE C  1 352 ? 94.473  71.810  245.350 1.00 134.15 ?  383 PHE C C   1 
ATOM   7278  O O   . PHE C  1 352 ? 95.016  72.446  246.256 1.00 137.56 ?  383 PHE C O   1 
ATOM   7279  C CB  . PHE C  1 352 ? 93.593  69.514  245.827 1.00 127.64 ?  383 PHE C CB  1 
ATOM   7280  C CG  . PHE C  1 352 ? 93.672  68.043  245.567 1.00 125.69 ?  383 PHE C CG  1 
ATOM   7281  C CD1 . PHE C  1 352 ? 94.432  67.226  246.387 1.00 125.51 ?  383 PHE C CD1 1 
ATOM   7282  C CD2 . PHE C  1 352 ? 92.976  67.471  244.520 1.00 126.36 ?  383 PHE C CD2 1 
ATOM   7283  C CE1 . PHE C  1 352 ? 94.511  65.870  246.154 1.00 126.06 ?  383 PHE C CE1 1 
ATOM   7284  C CE2 . PHE C  1 352 ? 93.048  66.114  244.285 1.00 126.94 ?  383 PHE C CE2 1 
ATOM   7285  C CZ  . PHE C  1 352 ? 93.816  65.312  245.104 1.00 126.81 ?  383 PHE C CZ  1 
ATOM   7286  N N   . TYR C  1 353 ? 93.637  72.372  244.477 1.00 129.67 ?  384 TYR C N   1 
ATOM   7287  C CA  . TYR C  1 353 ? 93.231  73.777  244.576 1.00 132.80 ?  384 TYR C CA  1 
ATOM   7288  C C   . TYR C  1 353 ? 91.760  73.839  244.170 1.00 130.67 ?  384 TYR C C   1 
ATOM   7289  O O   . TYR C  1 353 ? 91.450  73.927  242.979 1.00 129.19 ?  384 TYR C O   1 
ATOM   7290  C CB  . TYR C  1 353 ? 94.109  74.668  243.703 1.00 135.36 ?  384 TYR C CB  1 
ATOM   7291  C CG  . TYR C  1 353 ? 95.562  74.705  244.147 1.00 137.53 ?  384 TYR C CG  1 
ATOM   7292  C CD1 . TYR C  1 353 ? 96.015  75.637  245.074 1.00 141.42 ?  384 TYR C CD1 1 
ATOM   7293  C CD2 . TYR C  1 353 ? 96.480  73.796  243.636 1.00 135.34 ?  384 TYR C CD2 1 
ATOM   7294  C CE1 . TYR C  1 353 ? 97.347  75.657  245.477 1.00 143.40 ?  384 TYR C CE1 1 
ATOM   7295  C CE2 . TYR C  1 353 ? 97.804  73.808  244.032 1.00 137.13 ?  384 TYR C CE2 1 
ATOM   7296  C CZ  . TYR C  1 353 ? 98.235  74.739  244.949 1.00 141.24 ?  384 TYR C CZ  1 
ATOM   7297  O OH  . TYR C  1 353 ? 99.556  74.745  245.337 1.00 142.87 ?  384 TYR C OH  1 
ATOM   7298  N N   . CYS C  1 354 ? 90.858  73.808  245.150 1.00 151.67 ?  385 CYS C N   1 
ATOM   7299  C CA  . CYS C  1 354 ? 89.432  73.650  244.889 1.00 153.01 ?  385 CYS C CA  1 
ATOM   7300  C C   . CYS C  1 354 ? 88.665  74.967  244.899 1.00 157.43 ?  385 CYS C C   1 
ATOM   7301  O O   . CYS C  1 354 ? 88.947  75.882  245.678 1.00 159.19 ?  385 CYS C O   1 
ATOM   7302  C CB  . CYS C  1 354 ? 88.811  72.700  245.918 1.00 148.52 ?  385 CYS C CB  1 
ATOM   7303  S SG  . CYS C  1 354 ? 89.523  71.022  245.935 1.00 150.09 ?  385 CYS C SG  1 
ATOM   7304  N N   . ASN C  1 355 ? 87.661  75.021  244.029 1.00 167.27 ?  386 ASN C N   1 
ATOM   7305  C CA  . ASN C  1 355 ? 86.765  76.161  243.874 1.00 171.14 ?  386 ASN C CA  1 
ATOM   7306  C C   . ASN C  1 355 ? 85.725  76.142  244.986 1.00 171.89 ?  386 ASN C C   1 
ATOM   7307  O O   . ASN C  1 355 ? 84.900  75.225  245.055 1.00 170.57 ?  386 ASN C O   1 
ATOM   7308  C CB  . ASN C  1 355 ? 86.094  76.099  242.501 1.00 173.47 ?  386 ASN C CB  1 
ATOM   7309  C CG  . ASN C  1 355 ? 85.446  77.415  242.077 1.00 178.24 ?  386 ASN C CG  1 
ATOM   7310  O OD1 . ASN C  1 355 ? 85.157  78.280  242.904 1.00 180.88 ?  386 ASN C OD1 1 
ATOM   7311  N ND2 . ASN C  1 355 ? 85.179  77.546  240.773 1.00 189.17 ?  386 ASN C ND2 1 
ATOM   7312  N N   . THR C  1 356 ? 85.758  77.153  245.853 1.00 164.88 ?  387 THR C N   1 
ATOM   7313  C CA  . THR C  1 356 ? 84.842  77.241  246.988 1.00 164.27 ?  387 THR C CA  1 
ATOM   7314  C C   . THR C  1 356 ? 83.730  78.248  246.740 1.00 169.60 ?  387 THR C C   1 
ATOM   7315  O O   . THR C  1 356 ? 83.393  79.062  247.605 1.00 170.97 ?  387 THR C O   1 
ATOM   7316  C CB  . THR C  1 356 ? 85.604  77.595  248.260 1.00 158.83 ?  387 THR C CB  1 
ATOM   7317  O OG1 . THR C  1 356 ? 86.395  78.768  248.031 1.00 159.96 ?  387 THR C OG1 1 
ATOM   7318  C CG2 . THR C  1 356 ? 86.503  76.444  248.669 1.00 152.53 ?  387 THR C CG2 1 
ATOM   7319  N N   . SER C  1 357 ? 83.147  78.206  245.549 1.00 173.03 ?  388 SER C N   1 
ATOM   7320  C CA  . SER C  1 357 ? 82.034  79.072  245.202 1.00 179.54 ?  388 SER C CA  1 
ATOM   7321  C C   . SER C  1 357 ? 80.691  78.430  245.511 1.00 180.11 ?  388 SER C C   1 
ATOM   7322  O O   . SER C  1 357 ? 79.663  79.111  245.439 1.00 188.98 ?  388 SER C O   1 
ATOM   7323  C CB  . SER C  1 357 ? 82.100  79.456  243.721 1.00 183.01 ?  388 SER C CB  1 
ATOM   7324  O OG  . SER C  1 357 ? 83.267  80.211  243.441 1.00 179.25 ?  388 SER C OG  1 
ATOM   7325  N N   . GLY C  1 358 ? 80.684  77.141  245.854 1.00 182.94 ?  389 GLY C N   1 
ATOM   7326  C CA  . GLY C  1 358 ? 79.467  76.412  246.150 1.00 179.13 ?  389 GLY C CA  1 
ATOM   7327  C C   . GLY C  1 358 ? 79.247  76.323  247.646 1.00 177.37 ?  389 GLY C C   1 
ATOM   7328  O O   . GLY C  1 358 ? 78.211  75.836  248.110 1.00 178.16 ?  389 GLY C O   1 
ATOM   7329  N N   . LEU C  1 359 ? 80.236  76.789  248.407 1.00 172.52 ?  390 LEU C N   1 
ATOM   7330  C CA  . LEU C  1 359 ? 80.183  76.799  249.863 1.00 172.11 ?  390 LEU C CA  1 
ATOM   7331  C C   . LEU C  1 359 ? 79.855  78.167  250.439 1.00 176.74 ?  390 LEU C C   1 
ATOM   7332  O O   . LEU C  1 359 ? 79.202  78.243  251.484 1.00 177.62 ?  390 LEU C O   1 
ATOM   7333  C CB  . LEU C  1 359 ? 81.509  76.328  250.473 1.00 164.19 ?  390 LEU C CB  1 
ATOM   7334  C CG  . LEU C  1 359 ? 82.002  74.919  250.160 1.00 157.70 ?  390 LEU C CG  1 
ATOM   7335  C CD1 . LEU C  1 359 ? 83.339  74.689  250.837 1.00 152.13 ?  390 LEU C CD1 1 
ATOM   7336  C CD2 . LEU C  1 359 ? 80.986  73.874  250.596 1.00 160.31 ?  390 LEU C CD2 1 
ATOM   7337  N N   . PHE C  1 360 ? 80.279  79.246  249.778 1.00 173.39 ?  391 PHE C N   1 
ATOM   7338  C CA  . PHE C  1 360 ? 80.068  80.598  250.283 1.00 176.78 ?  391 PHE C CA  1 
ATOM   7339  C C   . PHE C  1 360 ? 79.091  81.381  249.415 1.00 182.27 ?  391 PHE C C   1 
ATOM   7340  O O   . PHE C  1 360 ? 79.358  82.524  249.034 1.00 183.92 ?  391 PHE C O   1 
ATOM   7341  C CB  . PHE C  1 360 ? 81.421  81.304  250.356 1.00 176.38 ?  391 PHE C CB  1 
ATOM   7342  C CG  . PHE C  1 360 ? 82.422  80.567  251.194 1.00 172.44 ?  391 PHE C CG  1 
ATOM   7343  C CD1 . PHE C  1 360 ? 82.107  80.190  252.485 1.00 171.15 ?  391 PHE C CD1 1 
ATOM   7344  C CD2 . PHE C  1 360 ? 83.652  80.200  250.672 1.00 170.15 ?  391 PHE C CD2 1 
ATOM   7345  C CE1 . PHE C  1 360 ? 83.009  79.493  253.256 1.00 167.68 ?  391 PHE C CE1 1 
ATOM   7346  C CE2 . PHE C  1 360 ? 84.561  79.500  251.441 1.00 166.78 ?  391 PHE C CE2 1 
ATOM   7347  C CZ  . PHE C  1 360 ? 84.237  79.147  252.735 1.00 165.55 ?  391 PHE C CZ  1 
ATOM   7348  N N   . ASN C  1 361 ? 77.982  80.746  249.062 1.00 188.89 ?  392 ASN C N   1 
ATOM   7349  C CA  . ASN C  1 361 ? 76.892  81.333  248.282 1.00 204.37 ?  392 ASN C CA  1 
ATOM   7350  C C   . ASN C  1 361 ? 75.582  81.323  249.080 1.00 211.65 ?  392 ASN C C   1 
ATOM   7351  O O   . ASN C  1 361 ? 74.692  80.515  248.792 1.00 216.70 ?  392 ASN C O   1 
ATOM   7352  C CB  . ASN C  1 361 ? 76.737  80.593  246.961 1.00 205.96 ?  392 ASN C CB  1 
ATOM   7353  C CG  . ASN C  1 361 ? 75.601  81.131  246.138 1.00 214.94 ?  392 ASN C CG  1 
ATOM   7354  O OD1 . ASN C  1 361 ? 75.262  82.314  246.179 1.00 217.06 ?  392 ASN C OD1 1 
ATOM   7355  N ND2 . ASN C  1 361 ? 74.949  80.227  245.442 1.00 228.25 ?  392 ASN C ND2 1 
ATOM   7356  N N   . SER C  1 362 ? 75.453  82.182  250.092 1.00 202.27 ?  393 SER C N   1 
ATOM   7357  C CA  . SER C  1 362 ? 74.243  82.131  250.905 1.00 206.52 ?  393 SER C CA  1 
ATOM   7358  C C   . SER C  1 362 ? 73.855  83.528  251.382 1.00 212.52 ?  393 SER C C   1 
ATOM   7359  O O   . SER C  1 362 ? 74.612  84.493  251.240 1.00 211.86 ?  393 SER C O   1 
ATOM   7360  C CB  . SER C  1 362 ? 74.428  81.185  252.097 1.00 195.56 ?  393 SER C CB  1 
ATOM   7361  O OG  . SER C  1 362 ? 74.825  79.895  251.663 1.00 182.96 ?  393 SER C OG  1 
ATOM   7362  N N   . THR C  1 363 ? 72.649  83.616  251.957 1.00 207.13 ?  394 THR C N   1 
ATOM   7363  C CA  . THR C  1 363 ? 72.119  84.854  252.532 1.00 211.98 ?  394 THR C CA  1 
ATOM   7364  C C   . THR C  1 363 ? 71.148  84.503  253.652 1.00 212.99 ?  394 THR C C   1 
ATOM   7365  O O   . THR C  1 363 ? 70.042  84.022  253.385 1.00 215.01 ?  394 THR C O   1 
ATOM   7366  C CB  . THR C  1 363 ? 71.423  85.703  251.470 1.00 214.79 ?  394 THR C CB  1 
ATOM   7367  O OG1 . THR C  1 363 ? 72.353  86.051  250.438 1.00 217.82 ?  394 THR C OG1 1 
ATOM   7368  C CG2 . THR C  1 363 ? 70.865  86.969  252.090 1.00 221.58 ?  394 THR C CG2 1 
ATOM   7369  N N   . TRP C  1 364 ? 71.555  84.737  254.895 1.00 215.80 ?  395 TRP C N   1 
ATOM   7370  C CA  . TRP C  1 364 ? 70.760  84.380  256.063 1.00 215.97 ?  395 TRP C CA  1 
ATOM   7371  C C   . TRP C  1 364 ? 70.034  85.592  256.632 1.00 223.45 ?  395 TRP C C   1 
ATOM   7372  O O   . TRP C  1 364 ? 70.661  86.617  256.923 1.00 225.95 ?  395 TRP C O   1 
ATOM   7373  C CB  . TRP C  1 364 ? 71.628  83.723  257.133 1.00 207.79 ?  395 TRP C CB  1 
ATOM   7374  C CG  . TRP C  1 364 ? 72.141  82.407  256.676 1.00 201.01 ?  395 TRP C CG  1 
ATOM   7375  C CD1 . TRP C  1 364 ? 73.260  82.173  255.934 1.00 195.44 ?  395 TRP C CD1 1 
ATOM   7376  C CD2 . TRP C  1 364 ? 71.509  81.136  256.863 1.00 197.88 ?  395 TRP C CD2 1 
ATOM   7377  N NE1 . TRP C  1 364 ? 73.387  80.828  255.681 1.00 189.44 ?  395 TRP C NE1 1 
ATOM   7378  C CE2 . TRP C  1 364 ? 72.322  80.170  256.238 1.00 190.12 ?  395 TRP C CE2 1 
ATOM   7379  C CE3 . TRP C  1 364 ? 70.343  80.719  257.513 1.00 198.72 ?  395 TRP C CE3 1 
ATOM   7380  C CZ2 . TRP C  1 364 ? 72.007  78.812  256.245 1.00 187.71 ?  395 TRP C CZ2 1 
ATOM   7381  C CZ3 . TRP C  1 364 ? 70.032  79.372  257.519 1.00 193.56 ?  395 TRP C CZ3 1 
ATOM   7382  C CH2 . TRP C  1 364 ? 70.861  78.434  256.889 1.00 189.52 ?  395 TRP C CH2 1 
ATOM   7383  N N   . ILE C  1 365 ? 68.715  85.474  256.783 1.00 229.06 ?  396 ILE C N   1 
ATOM   7384  C CA  . ILE C  1 365 ? 67.913  86.539  257.374 1.00 236.32 ?  396 ILE C CA  1 
ATOM   7385  C C   . ILE C  1 365 ? 67.948  86.279  258.878 1.00 235.91 ?  396 ILE C C   1 
ATOM   7386  O O   . ILE C  1 365 ? 68.438  85.231  259.309 1.00 232.41 ?  396 ILE C O   1 
ATOM   7387  C CB  . ILE C  1 365 ? 66.490  86.535  256.757 1.00 241.87 ?  396 ILE C CB  1 
ATOM   7388  C CG1 . ILE C  1 365 ? 66.419  87.470  255.546 1.00 244.99 ?  396 ILE C CG1 1 
ATOM   7389  C CG2 . ILE C  1 365 ? 65.359  86.866  257.739 1.00 246.92 ?  396 ILE C CG2 1 
ATOM   7390  C CD1 . ILE C  1 365 ? 67.293  87.062  254.388 1.00 236.42 ?  396 ILE C CD1 1 
ATOM   7391  N N   . SER C  1 366 ? 67.407  87.195  259.686 1.00 244.36 ?  397 SER C N   1 
ATOM   7392  C CA  . SER C  1 366 ? 67.437  87.035  261.138 1.00 247.04 ?  397 SER C CA  1 
ATOM   7393  C C   . SER C  1 366 ? 66.768  85.741  261.585 1.00 246.05 ?  397 SER C C   1 
ATOM   7394  O O   . SER C  1 366 ? 67.139  85.176  262.620 1.00 239.86 ?  397 SER C O   1 
ATOM   7395  C CB  . SER C  1 366 ? 66.777  88.232  261.816 1.00 255.53 ?  397 SER C CB  1 
ATOM   7396  O OG  . SER C  1 366 ? 65.397  88.284  261.509 1.00 264.85 ?  397 SER C OG  1 
ATOM   7397  N N   . ASN C  1 367 ? 65.784  85.265  260.831 1.00 241.64 ?  398 ASN C N   1 
ATOM   7398  C CA  . ASN C  1 367 ? 65.086  84.032  261.160 1.00 239.44 ?  398 ASN C CA  1 
ATOM   7399  C C   . ASN C  1 367 ? 64.429  83.428  259.933 1.00 236.63 ?  398 ASN C C   1 
ATOM   7400  O O   . ASN C  1 367 ? 64.872  82.391  259.444 1.00 231.75 ?  398 ASN C O   1 
ATOM   7401  C CB  . ASN C  1 367 ? 64.027  84.319  262.217 1.00 244.49 ?  398 ASN C CB  1 
ATOM   7402  C CG  . ASN C  1 367 ? 63.085  85.425  261.787 1.00 253.32 ?  398 ASN C CG  1 
ATOM   7403  O OD1 . ASN C  1 367 ? 63.332  86.598  262.065 1.00 258.99 ?  398 ASN C OD1 1 
ATOM   7404  N ND2 . ASN C  1 367 ? 62.013  85.064  261.088 1.00 260.60 ?  398 ASN C ND2 1 
ATOM   7405  N N   . ASN C  1 379 ? 68.594  65.675  249.417 1.00 229.24 ?  411 ASN C N   1 
ATOM   7406  C CA  . ASN C  1 379 ? 69.538  64.893  250.204 1.00 222.69 ?  411 ASN C CA  1 
ATOM   7407  C C   . ASN C  1 379 ? 70.719  64.415  249.361 1.00 214.02 ?  411 ASN C C   1 
ATOM   7408  O O   . ASN C  1 379 ? 70.686  63.300  248.835 1.00 209.76 ?  411 ASN C O   1 
ATOM   7409  C CB  . ASN C  1 379 ? 68.817  63.687  250.829 1.00 221.09 ?  411 ASN C CB  1 
ATOM   7410  C CG  . ASN C  1 379 ? 69.715  62.861  251.736 1.00 212.95 ?  411 ASN C CG  1 
ATOM   7411  O OD1 . ASN C  1 379 ? 70.719  63.349  252.254 1.00 209.86 ?  411 ASN C OD1 1 
ATOM   7412  N ND2 . ASN C  1 379 ? 69.356  61.595  251.925 1.00 208.55 ?  411 ASN C ND2 1 
ATOM   7413  N N   . ASP C  1 380 ? 71.764  65.243  249.228 1.00 214.03 ?  412 ASP C N   1 
ATOM   7414  C CA  . ASP C  1 380 ? 72.921  64.813  248.447 1.00 201.52 ?  412 ASP C CA  1 
ATOM   7415  C C   . ASP C  1 380 ? 74.231  65.481  248.876 1.00 198.94 ?  412 ASP C C   1 
ATOM   7416  O O   . ASP C  1 380 ? 74.431  65.729  250.070 1.00 203.25 ?  412 ASP C O   1 
ATOM   7417  C CB  . ASP C  1 380 ? 72.654  65.075  246.964 1.00 200.67 ?  412 ASP C CB  1 
ATOM   7418  C CG  . ASP C  1 380 ? 73.434  64.147  246.061 1.00 197.90 ?  412 ASP C CG  1 
ATOM   7419  O OD1 . ASP C  1 380 ? 73.826  63.054  246.522 1.00 196.43 ?  412 ASP C OD1 1 
ATOM   7420  O OD2 . ASP C  1 380 ? 73.672  64.523  244.896 1.00 200.73 -1 412 ASP C OD2 1 
ATOM   7421  N N   . SER C  1 381 ? 75.134  65.770  247.924 1.00 187.99 ?  413 SER C N   1 
ATOM   7422  C CA  . SER C  1 381 ? 76.433  66.380  248.212 1.00 186.22 ?  413 SER C CA  1 
ATOM   7423  C C   . SER C  1 381 ? 76.765  67.532  247.261 1.00 182.25 ?  413 SER C C   1 
ATOM   7424  O O   . SER C  1 381 ? 76.382  67.507  246.088 1.00 177.77 ?  413 SER C O   1 
ATOM   7425  C CB  . SER C  1 381 ? 77.542  65.317  248.140 1.00 179.61 ?  413 SER C CB  1 
ATOM   7426  O OG  . SER C  1 381 ? 77.277  64.245  249.032 1.00 180.45 ?  413 SER C OG  1 
ATOM   7427  N N   . ILE C  1 382 ? 77.466  68.548  247.777 1.00 185.40 ?  414 ILE C N   1 
ATOM   7428  C CA  . ILE C  1 382 ? 77.907  69.708  246.989 1.00 182.75 ?  414 ILE C CA  1 
ATOM   7429  C C   . ILE C  1 382 ? 79.312  69.464  246.430 1.00 172.98 ?  414 ILE C C   1 
ATOM   7430  O O   . ILE C  1 382 ? 80.299  69.518  247.167 1.00 170.86 ?  414 ILE C O   1 
ATOM   7431  C CB  . ILE C  1 382 ? 77.868  71.017  247.779 1.00 186.37 ?  414 ILE C CB  1 
ATOM   7432  C CG1 . ILE C  1 382 ? 76.482  71.290  248.362 1.00 191.59 ?  414 ILE C CG1 1 
ATOM   7433  C CG2 . ILE C  1 382 ? 78.357  72.174  246.894 1.00 183.29 ?  414 ILE C CG2 1 
ATOM   7434  C CD1 . ILE C  1 382 ? 76.377  70.904  249.802 1.00 196.62 ?  414 ILE C CD1 1 
ATOM   7435  N N   . THR C  1 383 ? 79.407  69.168  245.136 1.00 183.34 ?  415 THR C N   1 
ATOM   7436  C CA  . THR C  1 383 ? 80.686  68.905  244.477 1.00 176.36 ?  415 THR C CA  1 
ATOM   7437  C C   . THR C  1 383 ? 81.398  70.217  244.136 1.00 175.32 ?  415 THR C C   1 
ATOM   7438  O O   . THR C  1 383 ? 80.764  71.182  243.702 1.00 177.54 ?  415 THR C O   1 
ATOM   7439  C CB  . THR C  1 383 ? 80.475  68.079  243.209 1.00 171.45 ?  415 THR C CB  1 
ATOM   7440  O OG1 . THR C  1 383 ? 79.667  66.938  243.520 1.00 172.54 ?  415 THR C OG1 1 
ATOM   7441  C CG2 . THR C  1 383 ? 81.809  67.611  242.645 1.00 167.25 ?  415 THR C CG2 1 
ATOM   7442  N N   . LEU C  1 384 ? 82.717  70.260  244.352 1.00 173.41 ?  416 LEU C N   1 
ATOM   7443  C CA  . LEU C  1 384 ? 83.518  71.460  244.101 1.00 171.00 ?  416 LEU C CA  1 
ATOM   7444  C C   . LEU C  1 384 ? 84.646  71.201  243.106 1.00 168.37 ?  416 LEU C C   1 
ATOM   7445  O O   . LEU C  1 384 ? 85.408  70.236  243.260 1.00 165.12 ?  416 LEU C O   1 
ATOM   7446  C CB  . LEU C  1 384 ? 84.095  72.034  245.401 1.00 169.91 ?  416 LEU C CB  1 
ATOM   7447  C CG  . LEU C  1 384 ? 83.067  72.345  246.483 1.00 176.75 ?  416 LEU C CG  1 
ATOM   7448  C CD1 . LEU C  1 384 ? 83.758  72.858  247.724 1.00 177.77 ?  416 LEU C CD1 1 
ATOM   7449  C CD2 . LEU C  1 384 ? 82.080  73.371  245.960 1.00 179.97 ?  416 LEU C CD2 1 
ATOM   7450  N N   . PRO C  1 385 ? 84.777  72.048  242.081 1.00 168.01 ?  417 PRO C N   1 
ATOM   7451  C CA  . PRO C  1 385 ? 85.837  71.914  241.058 1.00 164.26 ?  417 PRO C CA  1 
ATOM   7452  C C   . PRO C  1 385 ? 87.248  72.069  241.612 1.00 161.84 ?  417 PRO C C   1 
ATOM   7453  O O   . PRO C  1 385 ? 87.601  73.114  242.160 1.00 168.89 ?  417 PRO C O   1 
ATOM   7454  C CB  . PRO C  1 385 ? 85.522  73.059  240.088 1.00 168.56 ?  417 PRO C CB  1 
ATOM   7455  C CG  . PRO C  1 385 ? 84.092  73.433  240.356 1.00 173.13 ?  417 PRO C CG  1 
ATOM   7456  C CD  . PRO C  1 385 ? 83.892  73.192  241.815 1.00 173.93 ?  417 PRO C CD  1 
ATOM   7457  N N   . CYS C  1 386 ? 88.067  71.021  241.461 1.00 162.69 ?  418 CYS C N   1 
ATOM   7458  C CA  . CYS C  1 386 ? 89.431  71.012  241.990 1.00 164.15 ?  418 CYS C CA  1 
ATOM   7459  C C   . CYS C  1 386 ? 90.454  70.877  240.862 1.00 161.26 ?  418 CYS C C   1 
ATOM   7460  O O   . CYS C  1 386 ? 90.333  69.999  239.999 1.00 159.10 ?  418 CYS C O   1 
ATOM   7461  C CB  . CYS C  1 386 ? 89.617  69.870  242.998 1.00 165.15 ?  418 CYS C CB  1 
ATOM   7462  S SG  . CYS C  1 386 ? 88.531  70.055  244.449 1.00 182.37 ?  418 CYS C SG  1 
ATOM   7463  N N   . ARG C  1 387 ? 91.447  71.768  240.882 1.00 159.20 ?  419 ARG C N   1 
ATOM   7464  C CA  . ARG C  1 387 ? 92.609  71.853  240.002 1.00 157.19 ?  419 ARG C CA  1 
ATOM   7465  C C   . ARG C  1 387 ? 93.811  71.237  240.719 1.00 152.12 ?  419 ARG C C   1 
ATOM   7466  O O   . ARG C  1 387 ? 93.818  71.111  241.947 1.00 156.01 ?  419 ARG C O   1 
ATOM   7467  C CB  . ARG C  1 387 ? 92.885  73.327  239.673 1.00 161.55 ?  419 ARG C CB  1 
ATOM   7468  C CG  . ARG C  1 387 ? 91.740  74.142  239.019 1.00 170.65 ?  419 ARG C CG  1 
ATOM   7469  C CD  . ARG C  1 387 ? 91.468  73.734  237.580 1.00 179.16 ?  419 ARG C CD  1 
ATOM   7470  N NE  . ARG C  1 387 ? 92.715  73.949  236.849 1.00 185.05 ?  419 ARG C NE  1 
ATOM   7471  C CZ  . ARG C  1 387 ? 92.824  74.143  235.537 1.00 187.90 ?  419 ARG C CZ  1 
ATOM   7472  N NH1 . ARG C  1 387 ? 91.744  74.160  234.769 1.00 188.27 1  419 ARG C NH1 1 
ATOM   7473  N NH2 . ARG C  1 387 ? 94.029  74.319  234.993 1.00 188.07 ?  419 ARG C NH2 1 
ATOM   7474  N N   . ILE C  1 388 ? 94.829  70.836  239.953 1.00 126.59 ?  420 ILE C N   1 
ATOM   7475  C CA  . ILE C  1 388 ? 96.023  70.228  240.537 1.00 126.77 ?  420 ILE C CA  1 
ATOM   7476  C C   . ILE C  1 388 ? 97.282  70.904  240.019 1.00 128.05 ?  420 ILE C C   1 
ATOM   7477  O O   . ILE C  1 388 ? 97.461  71.042  238.805 1.00 129.34 ?  420 ILE C O   1 
ATOM   7478  C CB  . ILE C  1 388 ? 96.102  68.722  240.223 1.00 127.29 ?  420 ILE C CB  1 
ATOM   7479  C CG1 . ILE C  1 388 ? 94.926  67.975  240.827 1.00 126.16 ?  420 ILE C CG1 1 
ATOM   7480  C CG2 . ILE C  1 388 ? 97.409  68.138  240.734 1.00 127.73 ?  420 ILE C CG2 1 
ATOM   7481  C CD1 . ILE C  1 388 ? 95.046  66.510  240.626 1.00 126.78 ?  420 ILE C CD1 1 
ATOM   7482  N N   . LYS C  1 389 ? 98.146  71.333  240.936 1.00 128.70 ?  421 LYS C N   1 
ATOM   7483  C CA  . LYS C  1 389 ? 99.409  71.960  240.578 1.00 129.73 ?  421 LYS C CA  1 
ATOM   7484  C C   . LYS C  1 389 ? 100.559 71.164  241.183 1.00 132.15 ?  421 LYS C C   1 
ATOM   7485  O O   . LYS C  1 389 ? 100.474 70.712  242.329 1.00 133.75 ?  421 LYS C O   1 
ATOM   7486  C CB  . LYS C  1 389 ? 99.455  73.415  241.035 1.00 131.75 ?  421 LYS C CB  1 
ATOM   7487  C CG  . LYS C  1 389 ? 100.642 74.185  240.498 1.00 134.00 ?  421 LYS C CG  1 
ATOM   7488  C CD  . LYS C  1 389 ? 100.592 75.651  240.887 1.00 136.49 ?  421 LYS C CD  1 
ATOM   7489  C CE  . LYS C  1 389 ? 100.569 75.844  242.394 1.00 136.76 ?  421 LYS C CE  1 
ATOM   7490  N NZ  . LYS C  1 389 ? 100.501 77.288  242.765 1.00 141.22 1  421 LYS C NZ  1 
ATOM   7491  N N   . GLN C  1 390 ? 101.626 70.979  240.407 1.00 127.23 ?  422 GLN C N   1 
ATOM   7492  C CA  . GLN C  1 390 ? 102.797 70.231  240.854 1.00 127.85 ?  422 GLN C CA  1 
ATOM   7493  C C   . GLN C  1 390 ? 103.943 71.122  241.327 1.00 128.47 ?  422 GLN C C   1 
ATOM   7494  O O   . GLN C  1 390 ? 104.625 70.780  242.298 1.00 131.24 ?  422 GLN C O   1 
ATOM   7495  C CB  . GLN C  1 390 ? 103.276 69.260  239.765 1.00 129.44 ?  422 GLN C CB  1 
ATOM   7496  C CG  . GLN C  1 390 ? 102.300 68.096  239.530 1.00 128.95 ?  422 GLN C CG  1 
ATOM   7497  C CD  . GLN C  1 390 ? 102.700 67.173  238.382 1.00 130.71 ?  422 GLN C CD  1 
ATOM   7498  O OE1 . GLN C  1 390 ? 103.271 67.607  237.380 1.00 132.20 ?  422 GLN C OE1 1 
ATOM   7499  N NE2 . GLN C  1 390 ? 102.400 65.886  238.532 1.00 130.66 ?  422 GLN C NE2 1 
ATOM   7500  N N   . ILE C  1 391 ? 104.195 72.232  240.634 1.00 130.60 ?  423 ILE C N   1 
ATOM   7501  C CA  . ILE C  1 391 ? 105.244 73.190  240.985 1.00 131.45 ?  423 ILE C CA  1 
ATOM   7502  C C   . ILE C  1 391 ? 104.667 74.248  241.925 1.00 130.21 ?  423 ILE C C   1 
ATOM   7503  O O   . ILE C  1 391 ? 103.880 75.096  241.497 1.00 130.04 ?  423 ILE C O   1 
ATOM   7504  C CB  . ILE C  1 391 ? 105.825 73.848  239.729 1.00 133.37 ?  423 ILE C CB  1 
ATOM   7505  C CG1 . ILE C  1 391 ? 106.209 72.790  238.695 1.00 134.64 ?  423 ILE C CG1 1 
ATOM   7506  C CG2 . ILE C  1 391 ? 107.026 74.715  240.082 1.00 134.54 ?  423 ILE C CG2 1 
ATOM   7507  C CD1 . ILE C  1 391 ? 106.616 73.376  237.362 1.00 136.51 ?  423 ILE C CD1 1 
ATOM   7508  N N   . ILE C  1 392 ? 105.050 74.206  243.207 1.00 126.42 ?  424 ILE C N   1 
ATOM   7509  C CA  . ILE C  1 392 ? 104.477 75.098  244.210 1.00 125.24 ?  424 ILE C CA  1 
ATOM   7510  C C   . ILE C  1 392 ? 105.540 75.988  244.855 1.00 126.09 ?  424 ILE C C   1 
ATOM   7511  O O   . ILE C  1 392 ? 106.740 75.704  244.818 1.00 127.29 ?  424 ILE C O   1 
ATOM   7512  C CB  . ILE C  1 392 ? 103.754 74.289  245.304 1.00 123.38 ?  424 ILE C CB  1 
ATOM   7513  C CG1 . ILE C  1 392 ? 104.786 73.500  246.113 1.00 123.51 ?  424 ILE C CG1 1 
ATOM   7514  C CG2 . ILE C  1 392 ? 102.707 73.357  244.705 1.00 122.68 ?  424 ILE C CG2 1 
ATOM   7515  C CD1 . ILE C  1 392 ? 104.224 72.815  247.320 1.00 121.83 ?  424 ILE C CD1 1 
ATOM   7516  N N   . ASN C  1 393 ? 105.062 77.072  245.482 1.00 153.10 ?  425 ASN C N   1 
ATOM   7517  C CA  . ASN C  1 393 ? 105.883 78.045  246.218 1.00 160.44 ?  425 ASN C CA  1 
ATOM   7518  C C   . ASN C  1 393 ? 105.129 78.552  247.451 1.00 166.53 ?  425 ASN C C   1 
ATOM   7519  O O   . ASN C  1 393 ? 104.818 79.732  247.581 1.00 172.61 ?  425 ASN C O   1 
ATOM   7520  C CB  . ASN C  1 393 ? 106.296 79.234  245.353 1.00 165.03 ?  425 ASN C CB  1 
ATOM   7521  C CG  . ASN C  1 393 ? 107.411 78.901  244.413 1.00 172.01 ?  425 ASN C CG  1 
ATOM   7522  O OD1 . ASN C  1 393 ? 108.327 78.174  244.779 1.00 177.37 ?  425 ASN C OD1 1 
ATOM   7523  N ND2 . ASN C  1 393 ? 107.365 79.449  243.204 1.00 173.79 ?  425 ASN C ND2 1 
ATOM   7524  N N   . MET C  1 394 ? 104.826 77.650  248.378 1.00 190.74 ?  426 MET C N   1 
ATOM   7525  C CA  . MET C  1 394 ? 104.044 78.003  249.558 1.00 191.97 ?  426 MET C CA  1 
ATOM   7526  C C   . MET C  1 394 ? 104.844 78.884  250.522 1.00 191.55 ?  426 MET C C   1 
ATOM   7527  O O   . MET C  1 394 ? 106.060 79.059  250.396 1.00 195.28 ?  426 MET C O   1 
ATOM   7528  C CB  . MET C  1 394 ? 103.549 76.751  250.285 1.00 188.17 ?  426 MET C CB  1 
ATOM   7529  C CG  . MET C  1 394 ? 104.579 75.652  250.459 1.00 185.51 ?  426 MET C CG  1 
ATOM   7530  S SD  . MET C  1 394 ? 103.921 74.251  251.393 1.00 173.15 ?  426 MET C SD  1 
ATOM   7531  C CE  . MET C  1 394 ? 102.390 73.919  250.525 1.00 170.03 ?  426 MET C CE  1 
ATOM   7532  N N   . TRP C  1 395 ? 104.120 79.448  251.498 1.00 204.47 ?  427 TRP C N   1 
ATOM   7533  C CA  . TRP C  1 395 ? 104.671 80.335  252.531 1.00 210.77 ?  427 TRP C CA  1 
ATOM   7534  C C   . TRP C  1 395 ? 105.301 81.607  251.978 1.00 219.59 ?  427 TRP C C   1 
ATOM   7535  O O   . TRP C  1 395 ? 106.206 82.166  252.606 1.00 221.51 ?  427 TRP C O   1 
ATOM   7536  C CB  . TRP C  1 395 ? 105.721 79.604  253.366 1.00 205.19 ?  427 TRP C CB  1 
ATOM   7537  C CG  . TRP C  1 395 ? 105.160 78.504  254.162 1.00 198.92 ?  427 TRP C CG  1 
ATOM   7538  C CD1 . TRP C  1 395 ? 104.206 78.575  255.132 1.00 193.69 ?  427 TRP C CD1 1 
ATOM   7539  C CD2 . TRP C  1 395 ? 105.528 77.128  254.053 1.00 198.44 ?  427 TRP C CD2 1 
ATOM   7540  N NE1 . TRP C  1 395 ? 103.948 77.317  255.627 1.00 197.33 ?  427 TRP C NE1 1 
ATOM   7541  C CE2 . TRP C  1 395 ? 104.752 76.412  254.982 1.00 199.29 ?  427 TRP C CE2 1 
ATOM   7542  C CE3 . TRP C  1 395 ? 106.444 76.432  253.256 1.00 197.16 ?  427 TRP C CE3 1 
ATOM   7543  C CZ2 . TRP C  1 395 ? 104.862 75.031  255.137 1.00 197.82 ?  427 TRP C CZ2 1 
ATOM   7544  C CZ3 . TRP C  1 395 ? 106.552 75.065  253.410 1.00 197.57 ?  427 TRP C CZ3 1 
ATOM   7545  C CH2 . TRP C  1 395 ? 105.766 74.377  254.343 1.00 198.12 ?  427 TRP C CH2 1 
ATOM   7546  N N   . GLN C  1 396 ? 104.843 82.089  250.821 1.00 206.15 ?  428 GLN C N   1 
ATOM   7547  C CA  . GLN C  1 396 ? 105.395 83.315  250.241 1.00 212.19 ?  428 GLN C CA  1 
ATOM   7548  C C   . GLN C  1 396 ? 106.909 83.213  250.092 1.00 211.89 ?  428 GLN C C   1 
ATOM   7549  O O   . GLN C  1 396 ? 107.647 84.168  250.343 1.00 216.68 ?  428 GLN C O   1 
ATOM   7550  C CB  . GLN C  1 396 ? 105.046 84.538  251.097 1.00 218.58 ?  428 GLN C CB  1 
ATOM   7551  C CG  . GLN C  1 396 ? 103.647 85.099  250.980 1.00 220.62 ?  428 GLN C CG  1 
ATOM   7552  C CD  . GLN C  1 396 ? 103.663 86.542  250.501 1.00 228.43 ?  428 GLN C CD  1 
ATOM   7553  O OE1 . GLN C  1 396 ? 104.357 87.386  251.076 1.00 235.75 ?  428 GLN C OE1 1 
ATOM   7554  N NE2 . GLN C  1 396 ? 102.895 86.837  249.462 1.00 226.34 ?  428 GLN C NE2 1 
ATOM   7555  N N   . ARG C  1 397 ? 107.383 82.041  249.679 1.00 194.77 ?  429 ARG C N   1 
ATOM   7556  C CA  . ARG C  1 397 ? 108.813 81.807  249.563 1.00 193.31 ?  429 ARG C CA  1 
ATOM   7557  C C   . ARG C  1 397 ? 109.217 81.986  248.109 1.00 198.21 ?  429 ARG C C   1 
ATOM   7558  O O   . ARG C  1 397 ? 108.589 81.414  247.212 1.00 197.73 ?  429 ARG C O   1 
ATOM   7559  C CB  . ARG C  1 397 ? 109.149 80.384  250.010 1.00 186.27 ?  429 ARG C CB  1 
ATOM   7560  C CG  . ARG C  1 397 ? 108.917 80.072  251.473 1.00 185.16 ?  429 ARG C CG  1 
ATOM   7561  C CD  . ARG C  1 397 ? 110.131 80.430  252.290 1.00 181.62 ?  429 ARG C CD  1 
ATOM   7562  N NE  . ARG C  1 397 ? 111.341 79.934  251.640 1.00 182.58 ?  429 ARG C NE  1 
ATOM   7563  C CZ  . ARG C  1 397 ? 111.680 78.649  251.581 1.00 177.61 ?  429 ARG C CZ  1 
ATOM   7564  N NH1 . ARG C  1 397 ? 110.896 77.728  252.128 1.00 168.37 1  429 ARG C NH1 1 
ATOM   7565  N NH2 . ARG C  1 397 ? 112.800 78.284  250.972 1.00 182.72 ?  429 ARG C NH2 1 
ATOM   7566  N N   . ILE C  1 398 ? 110.268 82.770  247.880 1.00 195.75 ?  430 ILE C N   1 
ATOM   7567  C CA  . ILE C  1 398 ? 110.821 82.976  246.548 1.00 201.76 ?  430 ILE C CA  1 
ATOM   7568  C C   . ILE C  1 398 ? 112.242 82.438  246.556 1.00 203.57 ?  430 ILE C C   1 
ATOM   7569  O O   . ILE C  1 398 ? 113.017 82.747  247.470 1.00 208.81 ?  430 ILE C O   1 
ATOM   7570  C CB  . ILE C  1 398 ? 110.783 84.459  246.134 1.00 205.27 ?  430 ILE C CB  1 
ATOM   7571  C CG1 . ILE C  1 398 ? 109.361 85.000  246.286 1.00 203.58 ?  430 ILE C CG1 1 
ATOM   7572  C CG2 . ILE C  1 398 ? 111.282 84.637  244.699 1.00 207.55 ?  430 ILE C CG2 1 
ATOM   7573  C CD1 . ILE C  1 398 ? 108.343 84.268  245.439 1.00 197.84 ?  430 ILE C CD1 1 
ATOM   7574  N N   . GLY C  1 399 ? 112.585 81.637  245.546 1.00 189.63 ?  431 GLY C N   1 
ATOM   7575  C CA  . GLY C  1 399 ? 113.903 81.038  245.431 1.00 189.43 ?  431 GLY C CA  1 
ATOM   7576  C C   . GLY C  1 399 ? 113.889 79.523  245.477 1.00 181.20 ?  431 GLY C C   1 
ATOM   7577  O O   . GLY C  1 399 ? 114.747 78.878  244.864 1.00 183.32 ?  431 GLY C O   1 
ATOM   7578  N N   . GLN C  1 400 ? 112.928 78.945  246.194 1.00 177.34 ?  432 GLN C N   1 
ATOM   7579  C CA  . GLN C  1 400 ? 112.814 77.503  246.365 1.00 168.15 ?  432 GLN C CA  1 
ATOM   7580  C C   . GLN C  1 400 ? 111.456 77.033  245.848 1.00 159.40 ?  432 GLN C C   1 
ATOM   7581  O O   . GLN C  1 400 ? 110.435 77.207  246.523 1.00 159.07 ?  432 GLN C O   1 
ATOM   7582  C CB  . GLN C  1 400 ? 112.991 77.159  247.843 1.00 171.10 ?  432 GLN C CB  1 
ATOM   7583  C CG  . GLN C  1 400 ? 113.833 75.944  248.086 1.00 174.95 ?  432 GLN C CG  1 
ATOM   7584  C CD  . GLN C  1 400 ? 115.242 76.173  247.578 1.00 176.33 ?  432 GLN C CD  1 
ATOM   7585  O OE1 . GLN C  1 400 ? 115.703 75.494  246.673 1.00 172.54 ?  432 GLN C OE1 1 
ATOM   7586  N NE2 . GLN C  1 400 ? 115.934 77.137  248.164 1.00 181.86 ?  432 GLN C NE2 1 
ATOM   7587  N N   . ALA C  1 401 ? 111.440 76.454  244.649 1.00 146.89 ?  433 ALA C N   1 
ATOM   7588  C CA  . ALA C  1 401 ? 110.229 75.917  244.044 1.00 145.64 ?  433 ALA C CA  1 
ATOM   7589  C C   . ALA C  1 401 ? 110.318 74.400  244.061 1.00 147.19 ?  433 ALA C C   1 
ATOM   7590  O O   . ALA C  1 401 ? 111.313 73.826  243.607 1.00 149.34 ?  433 ALA C O   1 
ATOM   7591  C CB  . ALA C  1 401 ? 110.043 76.427  242.614 1.00 146.86 ?  433 ALA C CB  1 
ATOM   7592  N N   . MET C  1 402 ? 109.290 73.757  244.602 1.00 138.01 ?  434 MET C N   1 
ATOM   7593  C CA  . MET C  1 402 ? 109.254 72.310  244.736 1.00 140.63 ?  434 MET C CA  1 
ATOM   7594  C C   . MET C  1 402 ? 108.322 71.670  243.719 1.00 140.25 ?  434 MET C C   1 
ATOM   7595  O O   . MET C  1 402 ? 107.160 72.069  243.595 1.00 136.90 ?  434 MET C O   1 
ATOM   7596  C CB  . MET C  1 402 ? 108.826 71.884  246.138 1.00 140.43 ?  434 MET C CB  1 
ATOM   7597  C CG  . MET C  1 402 ? 109.004 70.390  246.346 1.00 143.42 ?  434 MET C CG  1 
ATOM   7598  S SD  . MET C  1 402 ? 108.104 69.717  247.751 1.00 143.51 ?  434 MET C SD  1 
ATOM   7599  C CE  . MET C  1 402 ? 106.413 69.839  247.171 1.00 140.44 ?  434 MET C CE  1 
ATOM   7600  N N   . TYR C  1 403 ? 108.841 70.679  243.002 1.00 144.60 ?  435 TYR C N   1 
ATOM   7601  C CA  . TYR C  1 403 ? 108.060 69.883  242.063 1.00 142.08 ?  435 TYR C CA  1 
ATOM   7602  C C   . TYR C  1 403 ? 107.577 68.624  242.767 1.00 142.95 ?  435 TYR C C   1 
ATOM   7603  O O   . TYR C  1 403 ? 108.367 67.714  243.036 1.00 147.43 ?  435 TYR C O   1 
ATOM   7604  C CB  . TYR C  1 403 ? 108.853 69.511  240.812 1.00 142.78 ?  435 TYR C CB  1 
ATOM   7605  C CG  . TYR C  1 403 ? 108.054 68.603  239.881 1.00 138.43 ?  435 TYR C CG  1 
ATOM   7606  C CD1 . TYR C  1 403 ? 107.179 69.112  238.929 1.00 133.49 ?  435 TYR C CD1 1 
ATOM   7607  C CD2 . TYR C  1 403 ? 108.185 67.216  239.969 1.00 139.28 ?  435 TYR C CD2 1 
ATOM   7608  C CE1 . TYR C  1 403 ? 106.447 68.255  238.096 1.00 129.69 ?  435 TYR C CE1 1 
ATOM   7609  C CE2 . TYR C  1 403 ? 107.464 66.362  239.147 1.00 135.10 ?  435 TYR C CE2 1 
ATOM   7610  C CZ  . TYR C  1 403 ? 106.599 66.882  238.211 1.00 130.42 ?  435 TYR C CZ  1 
ATOM   7611  O OH  . TYR C  1 403 ? 105.890 66.020  237.398 1.00 130.38 ?  435 TYR C OH  1 
ATOM   7612  N N   . ALA C  1 404 ? 106.289 68.583  243.079 1.00 133.87 ?  436 ALA C N   1 
ATOM   7613  C CA  . ALA C  1 404 ? 105.719 67.417  243.733 1.00 132.82 ?  436 ALA C CA  1 
ATOM   7614  C C   . ALA C  1 404 ? 105.685 66.296  242.709 1.00 134.01 ?  436 ALA C C   1 
ATOM   7615  O O   . ALA C  1 404 ? 105.056 66.450  241.654 1.00 134.38 ?  436 ALA C O   1 
ATOM   7616  C CB  . ALA C  1 404 ? 104.316 67.693  244.259 1.00 130.89 ?  436 ALA C CB  1 
ATOM   7617  N N   . PRO C  1 405 ? 106.340 65.166  242.968 1.00 134.47 ?  437 PRO C N   1 
ATOM   7618  C CA  . PRO C  1 405 ? 106.330 64.082  241.993 1.00 135.83 ?  437 PRO C CA  1 
ATOM   7619  C C   . PRO C  1 405 ? 104.943 63.509  241.809 1.00 134.86 ?  437 PRO C C   1 
ATOM   7620  O O   . PRO C  1 405 ? 104.135 63.461  242.756 1.00 133.13 ?  437 PRO C O   1 
ATOM   7621  C CB  . PRO C  1 405 ? 107.299 63.054  242.605 1.00 136.67 ?  437 PRO C CB  1 
ATOM   7622  C CG  . PRO C  1 405 ? 107.264 63.337  244.076 1.00 135.02 ?  437 PRO C CG  1 
ATOM   7623  C CD  . PRO C  1 405 ? 107.106 64.828  244.180 1.00 134.38 ?  437 PRO C CD  1 
ATOM   7624  N N   . PRO C  1 406 ? 104.597 63.085  240.590 1.00 139.02 ?  438 PRO C N   1 
ATOM   7625  C CA  . PRO C  1 406 ? 103.268 62.519  240.333 1.00 134.99 ?  438 PRO C CA  1 
ATOM   7626  C C   . PRO C  1 406 ? 103.020 61.289  241.192 1.00 136.30 ?  438 PRO C C   1 
ATOM   7627  O O   . PRO C  1 406 ? 103.951 60.578  241.575 1.00 139.89 ?  438 PRO C O   1 
ATOM   7628  C CB  . PRO C  1 406 ? 103.318 62.159  238.844 1.00 136.23 ?  438 PRO C CB  1 
ATOM   7629  C CG  . PRO C  1 406 ? 104.415 63.011  238.284 1.00 137.43 ?  438 PRO C CG  1 
ATOM   7630  C CD  . PRO C  1 406 ? 105.425 63.138  239.373 1.00 138.43 ?  438 PRO C CD  1 
ATOM   7631  N N   . ILE C  1 407 ? 101.746 61.036  241.492 1.00 141.71 ?  439 ILE C N   1 
ATOM   7632  C CA  . ILE C  1 407 ? 101.345 59.900  242.315 1.00 142.58 ?  439 ILE C CA  1 
ATOM   7633  C C   . ILE C  1 407 ? 100.511 58.942  241.476 1.00 141.70 ?  439 ILE C C   1 
ATOM   7634  O O   . ILE C  1 407 ? 99.541  59.354  240.830 1.00 141.36 ?  439 ILE C O   1 
ATOM   7635  C CB  . ILE C  1 407 ? 100.555 60.357  243.554 1.00 142.72 ?  439 ILE C CB  1 
ATOM   7636  C CG1 . ILE C  1 407 ? 101.287 61.497  244.264 1.00 145.60 ?  439 ILE C CG1 1 
ATOM   7637  C CG2 . ILE C  1 407 ? 100.321 59.187  244.506 1.00 143.93 ?  439 ILE C CG2 1 
ATOM   7638  C CD1 . ILE C  1 407 ? 102.647 61.116  244.785 1.00 150.41 ?  439 ILE C CD1 1 
ATOM   7639  N N   . GLN C  1 408 ? 100.897 57.665  241.494 1.00 158.84 ?  440 GLN C N   1 
ATOM   7640  C CA  . GLN C  1 408 ? 100.210 56.629  240.733 1.00 158.30 ?  440 GLN C CA  1 
ATOM   7641  C C   . GLN C  1 408 ? 98.857  56.292  241.353 1.00 158.06 ?  440 GLN C C   1 
ATOM   7642  O O   . GLN C  1 408 ? 98.706  56.255  242.577 1.00 161.87 ?  440 GLN C O   1 
ATOM   7643  C CB  . GLN C  1 408 ? 101.069 55.362  240.653 1.00 160.37 ?  440 GLN C CB  1 
ATOM   7644  C CG  . GLN C  1 408 ? 102.560 55.594  240.401 1.00 163.33 ?  440 GLN C CG  1 
ATOM   7645  C CD  . GLN C  1 408 ? 103.353 55.764  241.688 1.00 172.70 ?  440 GLN C CD  1 
ATOM   7646  O OE1 . GLN C  1 408 ? 102.891 56.406  242.632 1.00 169.81 ?  440 GLN C OE1 1 
ATOM   7647  N NE2 . GLN C  1 408 ? 104.551 55.191  241.728 1.00 180.97 ?  440 GLN C NE2 1 
ATOM   7648  N N   . GLY C  1 409 ? 97.871  56.045  240.495 1.00 152.41 ?  441 GLY C N   1 
ATOM   7649  C CA  . GLY C  1 409 ? 96.554  55.629  240.928 1.00 151.03 ?  441 GLY C CA  1 
ATOM   7650  C C   . GLY C  1 409 ? 95.666  56.764  241.396 1.00 149.10 ?  441 GLY C C   1 
ATOM   7651  O O   . GLY C  1 409 ? 96.096  57.891  241.646 1.00 147.94 ?  441 GLY C O   1 
ATOM   7652  N N   . VAL C  1 410 ? 94.379  56.442  241.503 1.00 156.29 ?  442 VAL C N   1 
ATOM   7653  C CA  . VAL C  1 410 ? 93.401  57.409  241.973 1.00 157.05 ?  442 VAL C CA  1 
ATOM   7654  C C   . VAL C  1 410 ? 93.600  57.626  243.466 1.00 157.30 ?  442 VAL C C   1 
ATOM   7655  O O   . VAL C  1 410 ? 93.658  56.666  244.246 1.00 157.99 ?  442 VAL C O   1 
ATOM   7656  C CB  . VAL C  1 410 ? 91.981  56.924  241.654 1.00 158.95 ?  442 VAL C CB  1 
ATOM   7657  C CG1 . VAL C  1 410 ? 90.963  57.849  242.280 1.00 160.10 ?  442 VAL C CG1 1 
ATOM   7658  C CG2 . VAL C  1 410 ? 91.788  56.834  240.148 1.00 158.75 ?  442 VAL C CG2 1 
ATOM   7659  N N   . ILE C  1 411 ? 93.704  58.887  243.873 1.00 151.27 ?  443 ILE C N   1 
ATOM   7660  C CA  . ILE C  1 411 ? 93.926  59.250  245.267 1.00 151.40 ?  443 ILE C CA  1 
ATOM   7661  C C   . ILE C  1 411 ? 92.602  59.614  245.921 1.00 153.11 ?  443 ILE C C   1 
ATOM   7662  O O   . ILE C  1 411 ? 91.839  60.424  245.381 1.00 153.64 ?  443 ILE C O   1 
ATOM   7663  C CB  . ILE C  1 411 ? 94.924  60.413  245.385 1.00 149.98 ?  443 ILE C CB  1 
ATOM   7664  C CG1 . ILE C  1 411 ? 96.196  60.108  244.599 1.00 148.42 ?  443 ILE C CG1 1 
ATOM   7665  C CG2 . ILE C  1 411 ? 95.242  60.706  246.842 1.00 149.97 ?  443 ILE C CG2 1 
ATOM   7666  C CD1 . ILE C  1 411 ? 97.221  61.199  244.689 1.00 147.22 ?  443 ILE C CD1 1 
ATOM   7667  N N   . ARG C  1 412 ? 92.321  59.007  247.077 1.00 171.16 ?  444 ARG C N   1 
ATOM   7668  C CA  . ARG C  1 412 ? 91.124  59.312  247.848 1.00 174.56 ?  444 ARG C CA  1 
ATOM   7669  C C   . ARG C  1 412 ? 91.511  59.642  249.283 1.00 176.22 ?  444 ARG C C   1 
ATOM   7670  O O   . ARG C  1 412 ? 92.393  59.003  249.866 1.00 173.75 ?  444 ARG C O   1 
ATOM   7671  C CB  . ARG C  1 412 ? 90.122  58.154  247.831 1.00 175.68 ?  444 ARG C CB  1 
ATOM   7672  C CG  . ARG C  1 412 ? 88.799  58.467  248.522 1.00 180.70 ?  444 ARG C CG  1 
ATOM   7673  C CD  . ARG C  1 412 ? 88.059  57.193  248.872 1.00 183.88 ?  444 ARG C CD  1 
ATOM   7674  N NE  . ARG C  1 412 ? 88.742  56.422  249.905 1.00 186.35 ?  444 ARG C NE  1 
ATOM   7675  C CZ  . ARG C  1 412 ? 88.234  55.338  250.482 1.00 189.75 ?  444 ARG C CZ  1 
ATOM   7676  N NH1 . ARG C  1 412 ? 87.036  54.896  250.126 1.00 196.03 1  444 ARG C NH1 1 
ATOM   7677  N NH2 . ARG C  1 412 ? 88.922  54.700  251.419 1.00 191.81 ?  444 ARG C NH2 1 
ATOM   7678  N N   . CYS C  1 413 ? 90.856  60.665  249.827 1.00 174.96 ?  445 CYS C N   1 
ATOM   7679  C CA  . CYS C  1 413 ? 91.034  61.138  251.194 1.00 173.81 ?  445 CYS C CA  1 
ATOM   7680  C C   . CYS C  1 413 ? 89.762  61.713  251.795 1.00 171.75 ?  445 CYS C C   1 
ATOM   7681  O O   . CYS C  1 413 ? 88.995  62.420  251.134 1.00 170.42 ?  445 CYS C O   1 
ATOM   7682  C CB  . CYS C  1 413 ? 92.217  62.099  251.274 1.00 173.83 ?  445 CYS C CB  1 
ATOM   7683  S SG  . CYS C  1 413 ? 92.091  63.633  250.378 1.00 177.41 ?  445 CYS C SG  1 
ATOM   7684  N N   . VAL C  1 414 ? 89.572  61.402  253.069 1.00 170.87 ?  446 VAL C N   1 
ATOM   7685  C CA  . VAL C  1 414 ? 88.451  61.869  253.863 1.00 172.52 ?  446 VAL C CA  1 
ATOM   7686  C C   . VAL C  1 414 ? 89.026  62.688  255.007 1.00 172.18 ?  446 VAL C C   1 
ATOM   7687  O O   . VAL C  1 414 ? 89.817  62.173  255.808 1.00 171.57 ?  446 VAL C O   1 
ATOM   7688  C CB  . VAL C  1 414 ? 87.613  60.698  254.395 1.00 174.30 ?  446 VAL C CB  1 
ATOM   7689  C CG1 . VAL C  1 414 ? 86.450  61.215  255.215 1.00 174.05 ?  446 VAL C CG1 1 
ATOM   7690  C CG2 . VAL C  1 414 ? 87.146  59.812  253.244 1.00 174.52 ?  446 VAL C CG2 1 
ATOM   7691  N N   . SER C  1 415 ? 88.643  63.959  255.080 1.00 165.83 ?  447 SER C N   1 
ATOM   7692  C CA  . SER C  1 415 ? 89.185  64.866  256.076 1.00 161.33 ?  447 SER C CA  1 
ATOM   7693  C C   . SER C  1 415 ? 88.046  65.437  256.910 1.00 162.18 ?  447 SER C C   1 
ATOM   7694  O O   . SER C  1 415 ? 86.864  65.204  256.640 1.00 163.25 ?  447 SER C O   1 
ATOM   7695  C CB  . SER C  1 415 ? 89.996  65.991  255.418 1.00 160.04 ?  447 SER C CB  1 
ATOM   7696  O OG  . SER C  1 415 ? 91.098  65.474  254.690 1.00 159.24 ?  447 SER C OG  1 
ATOM   7697  N N   . ASN C  1 416 ? 88.419  66.186  257.939 1.00 162.68 ?  448 ASN C N   1 
ATOM   7698  C CA  . ASN C  1 416 ? 87.471  66.830  258.834 1.00 161.87 ?  448 ASN C CA  1 
ATOM   7699  C C   . ASN C  1 416 ? 87.534  68.334  258.596 1.00 161.76 ?  448 ASN C C   1 
ATOM   7700  O O   . ASN C  1 416 ? 88.597  68.942  258.758 1.00 163.98 ?  448 ASN C O   1 
ATOM   7701  C CB  . ASN C  1 416 ? 87.840  66.470  260.271 1.00 161.16 ?  448 ASN C CB  1 
ATOM   7702  C CG  . ASN C  1 416 ? 87.322  65.094  260.677 1.00 160.00 ?  448 ASN C CG  1 
ATOM   7703  O OD1 . ASN C  1 416 ? 87.113  64.229  259.826 1.00 160.51 ?  448 ASN C OD1 1 
ATOM   7704  N ND2 . ASN C  1 416 ? 87.172  64.865  261.975 1.00 166.45 ?  448 ASN C ND2 1 
ATOM   7705  N N   . ILE C  1 417 ? 86.407  68.941  258.232 1.00 154.23 ?  449 ILE C N   1 
ATOM   7706  C CA  . ILE C  1 417 ? 86.330  70.400  258.151 1.00 155.38 ?  449 ILE C CA  1 
ATOM   7707  C C   . ILE C  1 417 ? 86.064  70.916  259.563 1.00 155.94 ?  449 ILE C C   1 
ATOM   7708  O O   . ILE C  1 417 ? 84.944  70.809  260.066 1.00 156.38 ?  449 ILE C O   1 
ATOM   7709  C CB  . ILE C  1 417 ? 85.257  70.864  257.167 1.00 156.88 ?  449 ILE C CB  1 
ATOM   7710  C CG1 . ILE C  1 417 ? 85.510  70.281  255.777 1.00 156.05 ?  449 ILE C CG1 1 
ATOM   7711  C CG2 . ILE C  1 417 ? 85.215  72.374  257.121 1.00 158.44 ?  449 ILE C CG2 1 
ATOM   7712  C CD1 . ILE C  1 417 ? 84.526  70.761  254.745 1.00 157.54 ?  449 ILE C CD1 1 
ATOM   7713  N N   . THR C  1 418 ? 87.095  71.458  260.218 1.00 150.58 ?  450 THR C N   1 
ATOM   7714  C CA  . THR C  1 418 ? 87.000  71.864  261.617 1.00 150.64 ?  450 THR C CA  1 
ATOM   7715  C C   . THR C  1 418 ? 87.088  73.377  261.846 1.00 152.27 ?  450 THR C C   1 
ATOM   7716  O O   . THR C  1 418 ? 87.182  73.809  263.000 1.00 151.97 ?  450 THR C O   1 
ATOM   7717  C CB  . THR C  1 418 ? 88.090  71.154  262.432 1.00 149.02 ?  450 THR C CB  1 
ATOM   7718  O OG1 . THR C  1 418 ? 89.379  71.572  261.974 1.00 148.71 ?  450 THR C OG1 1 
ATOM   7719  C CG2 . THR C  1 418 ? 87.997  69.630  262.265 1.00 147.61 ?  450 THR C CG2 1 
ATOM   7720  N N   . GLY C  1 419 ? 87.066  74.198  260.797 1.00 150.25 ?  451 GLY C N   1 
ATOM   7721  C CA  . GLY C  1 419 ? 87.136  75.634  261.013 1.00 150.90 ?  451 GLY C CA  1 
ATOM   7722  C C   . GLY C  1 419 ? 87.301  76.449  259.747 1.00 150.19 ?  451 GLY C C   1 
ATOM   7723  O O   . GLY C  1 419 ? 87.661  75.904  258.700 1.00 148.67 ?  451 GLY C O   1 
ATOM   7724  N N   . LEU C  1 420 ? 87.052  77.759  259.837 1.00 143.80 ?  452 LEU C N   1 
ATOM   7725  C CA  . LEU C  1 420 ? 87.149  78.668  258.701 1.00 143.88 ?  452 LEU C CA  1 
ATOM   7726  C C   . LEU C  1 420 ? 88.016  79.880  259.032 1.00 146.61 ?  452 LEU C C   1 
ATOM   7727  O O   . LEU C  1 420 ? 88.222  80.221  260.200 1.00 153.64 ?  452 LEU C O   1 
ATOM   7728  C CB  . LEU C  1 420 ? 85.757  79.141  258.275 1.00 146.64 ?  452 LEU C CB  1 
ATOM   7729  C CG  . LEU C  1 420 ? 84.713  78.030  258.160 1.00 147.25 ?  452 LEU C CG  1 
ATOM   7730  C CD1 . LEU C  1 420 ? 83.351  78.598  257.798 1.00 156.76 ?  452 LEU C CD1 1 
ATOM   7731  C CD2 . LEU C  1 420 ? 85.147  76.978  257.149 1.00 146.40 ?  452 LEU C CD2 1 
ATOM   7732  N N   . ILE C  1 421 ? 88.518  80.532  257.974 1.00 132.05 ?  453 ILE C N   1 
ATOM   7733  C CA  . ILE C  1 421 ? 89.251  81.801  258.063 1.00 133.23 ?  453 ILE C CA  1 
ATOM   7734  C C   . ILE C  1 421 ? 88.500  82.831  257.220 1.00 136.66 ?  453 ILE C C   1 
ATOM   7735  O O   . ILE C  1 421 ? 88.663  82.874  255.994 1.00 136.69 ?  453 ILE C O   1 
ATOM   7736  C CB  . ILE C  1 421 ? 90.704  81.659  257.591 1.00 133.75 ?  453 ILE C CB  1 
ATOM   7737  C CG1 . ILE C  1 421 ? 91.431  80.589  258.405 1.00 132.81 ?  453 ILE C CG1 1 
ATOM   7738  C CG2 . ILE C  1 421 ? 91.444  82.986  257.712 1.00 135.14 ?  453 ILE C CG2 1 
ATOM   7739  C CD1 . ILE C  1 421 ? 92.901  80.424  258.051 1.00 133.42 ?  453 ILE C CD1 1 
ATOM   7740  N N   . LEU C  1 422 ? 87.685  83.667  257.861 1.00 138.96 ?  454 LEU C N   1 
ATOM   7741  C CA  . LEU C  1 422 ? 86.823  84.623  257.176 1.00 148.18 ?  454 LEU C CA  1 
ATOM   7742  C C   . LEU C  1 422 ? 87.325  86.060  257.274 1.00 153.19 ?  454 LEU C C   1 
ATOM   7743  O O   . LEU C  1 422 ? 88.033  86.435  258.215 1.00 154.24 ?  454 LEU C O   1 
ATOM   7744  C CB  . LEU C  1 422 ? 85.382  84.545  257.689 1.00 153.64 ?  454 LEU C CB  1 
ATOM   7745  C CG  . LEU C  1 422 ? 84.747  83.158  257.626 1.00 148.97 ?  454 LEU C CG  1 
ATOM   7746  C CD1 . LEU C  1 422 ? 83.323  83.208  258.154 1.00 160.05 ?  454 LEU C CD1 1 
ATOM   7747  C CD2 . LEU C  1 422 ? 84.777  82.651  256.187 1.00 145.98 ?  454 LEU C CD2 1 
ATOM   7748  N N   . THR C  1 423 ? 86.946  86.856  256.270 1.00 159.21 ?  455 THR C N   1 
ATOM   7749  C CA  . THR C  1 423 ? 87.240  88.281  256.191 1.00 162.04 ?  455 THR C CA  1 
ATOM   7750  C C   . THR C  1 423 ? 85.956  89.040  255.878 1.00 169.86 ?  455 THR C C   1 
ATOM   7751  O O   . THR C  1 423 ? 85.085  88.551  255.152 1.00 172.07 ?  455 THR C O   1 
ATOM   7752  C CB  . THR C  1 423 ? 88.297  88.611  255.122 1.00 159.97 ?  455 THR C CB  1 
ATOM   7753  O OG1 . THR C  1 423 ? 87.862  88.135  253.843 1.00 167.19 ?  455 THR C OG1 1 
ATOM   7754  C CG2 . THR C  1 423 ? 89.622  87.979  255.466 1.00 148.65 ?  455 THR C CG2 1 
ATOM   7755  N N   . ARG C  1 424 ? 85.852  90.243  256.433 1.00 179.64 ?  456 ARG C N   1 
ATOM   7756  C CA  . ARG C  1 424 ? 84.680  91.093  256.285 1.00 184.18 ?  456 ARG C CA  1 
ATOM   7757  C C   . ARG C  1 424 ? 84.978  92.265  255.361 1.00 191.66 ?  456 ARG C C   1 
ATOM   7758  O O   . ARG C  1 424 ? 86.088  92.805  255.366 1.00 191.10 ?  456 ARG C O   1 
ATOM   7759  C CB  . ARG C  1 424 ? 84.231  91.632  257.640 1.00 186.79 ?  456 ARG C CB  1 
ATOM   7760  C CG  . ARG C  1 424 ? 82.892  92.326  257.625 1.00 194.21 ?  456 ARG C CG  1 
ATOM   7761  C CD  . ARG C  1 424 ? 82.436  92.536  259.041 1.00 197.29 ?  456 ARG C CD  1 
ATOM   7762  N NE  . ARG C  1 424 ? 83.448  93.295  259.766 1.00 195.79 ?  456 ARG C NE  1 
ATOM   7763  C CZ  . ARG C  1 424 ? 83.473  94.618  259.871 1.00 203.28 ?  456 ARG C CZ  1 
ATOM   7764  N NH1 . ARG C  1 424 ? 82.534  95.359  259.295 1.00 210.66 1  456 ARG C NH1 1 
ATOM   7765  N NH2 . ARG C  1 424 ? 84.448  95.203  260.550 1.00 206.11 ?  456 ARG C NH2 1 
ATOM   7766  N N   . ASP C  1 425 ? 83.982  92.653  254.571 1.00 187.02 ?  457 ASP C N   1 
ATOM   7767  C CA  . ASP C  1 425 ? 84.181  93.745  253.635 1.00 190.58 ?  457 ASP C CA  1 
ATOM   7768  C C   . ASP C  1 425 ? 84.099  95.088  254.355 1.00 195.47 ?  457 ASP C C   1 
ATOM   7769  O O   . ASP C  1 425 ? 83.618  95.194  255.487 1.00 196.46 ?  457 ASP C O   1 
ATOM   7770  C CB  . ASP C  1 425 ? 83.140  93.687  252.516 1.00 191.91 ?  457 ASP C CB  1 
ATOM   7771  C CG  . ASP C  1 425 ? 83.273  92.440  251.661 1.00 187.42 ?  457 ASP C CG  1 
ATOM   7772  O OD1 . ASP C  1 425 ? 84.037  92.467  250.673 1.00 186.32 ?  457 ASP C OD1 1 
ATOM   7773  O OD2 . ASP C  1 425 ? 82.623  91.425  251.987 1.00 185.06 -1 457 ASP C OD2 1 
ATOM   7774  N N   . GLY C  1 426 ? 84.566  96.126  253.667 1.00 211.57 ?  458 GLY C N   1 
ATOM   7775  C CA  . GLY C  1 426 ? 84.565  97.462  254.222 1.00 220.84 ?  458 GLY C CA  1 
ATOM   7776  C C   . GLY C  1 426 ? 83.436  98.319  253.693 1.00 233.15 ?  458 GLY C C   1 
ATOM   7777  O O   . GLY C  1 426 ? 83.175  99.401  254.230 1.00 241.28 ?  458 GLY C O   1 
ATOM   7778  N N   . GLY C  1 427 ? 82.748  97.845  252.652 1.00 250.06 ?  459 GLY C N   1 
ATOM   7779  C CA  . GLY C  1 427 ? 81.631  98.595  252.114 1.00 256.35 ?  459 GLY C CA  1 
ATOM   7780  C C   . GLY C  1 427 ? 80.542  98.728  253.150 1.00 265.29 ?  459 GLY C C   1 
ATOM   7781  O O   . GLY C  1 427 ? 79.854  97.757  253.485 1.00 259.92 ?  459 GLY C O   1 
ATOM   7782  N N   . SER C  1 428 ? 80.381  99.938  253.666 1.00 255.80 ?  460 SER C N   1 
ATOM   7783  C CA  . SER C  1 428 ? 79.465  100.145 254.764 1.00 259.55 ?  460 SER C CA  1 
ATOM   7784  C C   . SER C  1 428 ? 78.981  101.589 254.900 1.00 271.34 ?  460 SER C C   1 
ATOM   7785  O O   . SER C  1 428 ? 79.802  102.498 254.772 1.00 272.68 ?  460 SER C O   1 
ATOM   7786  C CB  . SER C  1 428 ? 80.134  99.690  256.062 1.00 251.33 ?  460 SER C CB  1 
ATOM   7787  O OG  . SER C  1 428 ? 81.336  100.399 256.298 1.00 249.54 ?  460 SER C OG  1 
ATOM   7788  N N   . THR C  1 429 ? 77.693  101.853 255.172 1.00 265.60 ?  461 THR C N   1 
ATOM   7789  C CA  . THR C  1 429 ? 76.535  100.934 255.299 1.00 267.23 ?  461 THR C CA  1 
ATOM   7790  C C   . THR C  1 429 ? 76.806  99.736  256.237 1.00 263.08 ?  461 THR C C   1 
ATOM   7791  O O   . THR C  1 429 ? 76.623  98.568  255.888 1.00 259.80 ?  461 THR C O   1 
ATOM   7792  C CB  . THR C  1 429 ? 75.953  100.519 253.872 1.00 263.74 ?  461 THR C CB  1 
ATOM   7793  O OG1 . THR C  1 429 ? 74.617  100.031 254.026 1.00 264.69 ?  461 THR C OG1 1 
ATOM   7794  C CG2 . THR C  1 429 ? 76.769  99.495  253.087 1.00 250.65 ?  461 THR C CG2 1 
ATOM   7795  N N   . ASN C  1 430 ? 77.198  100.062 257.466 1.00 274.40 ?  462 ASN C N   1 
ATOM   7796  C CA  . ASN C  1 430 ? 77.642  99.050  258.415 1.00 258.90 ?  462 ASN C CA  1 
ATOM   7797  C C   . ASN C  1 430 ? 76.504  98.526  259.274 1.00 259.05 ?  462 ASN C C   1 
ATOM   7798  O O   . ASN C  1 430 ? 76.430  97.319  259.530 1.00 251.62 ?  462 ASN C O   1 
ATOM   7799  C CB  . ASN C  1 430 ? 78.755  99.612  259.303 1.00 257.17 ?  462 ASN C CB  1 
ATOM   7800  C CG  . ASN C  1 430 ? 79.374  98.557  260.188 1.00 253.55 ?  462 ASN C CG  1 
ATOM   7801  O OD1 . ASN C  1 430 ? 80.286  97.847  259.767 1.00 245.32 ?  462 ASN C OD1 1 
ATOM   7802  N ND2 . ASN C  1 430 ? 78.898  98.457  261.425 1.00 257.20 ?  462 ASN C ND2 1 
ATOM   7803  N N   . SER C  1 431 ? 75.616  99.405  259.724 1.00 271.24 ?  463 SER C N   1 
ATOM   7804  C CA  . SER C  1 431 ? 74.533  99.004  260.610 1.00 270.19 ?  463 SER C CA  1 
ATOM   7805  C C   . SER C  1 431 ? 73.410  98.271  259.883 1.00 265.99 ?  463 SER C C   1 
ATOM   7806  O O   . SER C  1 431 ? 72.396  97.951  260.513 1.00 266.93 ?  463 SER C O   1 
ATOM   7807  C CB  . SER C  1 431 ? 73.975  100.228 261.344 1.00 275.40 ?  463 SER C CB  1 
ATOM   7808  O OG  . SER C  1 431 ? 74.971  100.848 262.143 1.00 272.40 ?  463 SER C OG  1 
ATOM   7809  N N   . THR C  1 432 ? 73.562  97.991  258.586 1.00 246.24 ?  464 THR C N   1 
ATOM   7810  C CA  . THR C  1 432 ? 72.534  97.297  257.818 1.00 236.63 ?  464 THR C CA  1 
ATOM   7811  C C   . THR C  1 432 ? 72.927  95.833  257.649 1.00 230.32 ?  464 THR C C   1 
ATOM   7812  O O   . THR C  1 432 ? 72.522  94.983  258.448 1.00 226.95 ?  464 THR C O   1 
ATOM   7813  C CB  . THR C  1 432 ? 72.326  97.967  256.457 1.00 240.82 ?  464 THR C CB  1 
ATOM   7814  O OG1 . THR C  1 432 ? 73.451  97.700  255.610 1.00 238.37 ?  464 THR C OG1 1 
ATOM   7815  C CG2 . THR C  1 432 ? 72.162  99.473  256.624 1.00 244.40 ?  464 THR C CG2 1 
ATOM   7816  N N   . THR C  1 433 ? 73.712  95.521  256.622 1.00 233.56 ?  465 THR C N   1 
ATOM   7817  C CA  . THR C  1 433 ? 74.112  94.148  256.355 1.00 224.61 ?  465 THR C CA  1 
ATOM   7818  C C   . THR C  1 433 ? 75.633  94.051  256.340 1.00 225.24 ?  465 THR C C   1 
ATOM   7819  O O   . THR C  1 433 ? 76.338  95.046  256.149 1.00 231.56 ?  465 THR C O   1 
ATOM   7820  C CB  . THR C  1 433 ? 73.545  93.639  255.029 1.00 218.97 ?  465 THR C CB  1 
ATOM   7821  O OG1 . THR C  1 433 ? 74.046  92.321  254.776 1.00 211.41 ?  465 THR C OG1 1 
ATOM   7822  C CG2 . THR C  1 433 ? 73.955  94.562  253.895 1.00 220.09 ?  465 THR C CG2 1 
ATOM   7823  N N   . GLU C  1 434 ? 76.133  92.832  256.546 1.00 222.23 ?  466 GLU C N   1 
ATOM   7824  C CA  . GLU C  1 434 ? 77.563  92.552  256.553 1.00 215.42 ?  466 GLU C CA  1 
ATOM   7825  C C   . GLU C  1 434 ? 77.845  91.350  255.661 1.00 203.75 ?  466 GLU C C   1 
ATOM   7826  O O   . GLU C  1 434 ? 77.101  90.364  255.677 1.00 201.34 ?  466 GLU C O   1 
ATOM   7827  C CB  . GLU C  1 434 ? 78.074  92.325  257.980 1.00 211.32 ?  466 GLU C CB  1 
ATOM   7828  C CG  . GLU C  1 434 ? 77.902  93.557  258.874 1.00 215.53 ?  466 GLU C CG  1 
ATOM   7829  C CD  . GLU C  1 434 ? 78.841  94.705  258.518 1.00 225.59 ?  466 GLU C CD  1 
ATOM   7830  O OE1 . GLU C  1 434 ? 79.803  94.487  257.751 1.00 224.01 ?  466 GLU C OE1 1 
ATOM   7831  O OE2 . GLU C  1 434 ? 78.599  95.837  258.991 1.00 233.24 -1 466 GLU C OE2 1 
ATOM   7832  N N   . THR C  1 435 ? 78.929  91.439  254.890 1.00 202.02 ?  467 THR C N   1 
ATOM   7833  C CA  . THR C  1 435 ? 79.344  90.402  253.952 1.00 195.51 ?  467 THR C CA  1 
ATOM   7834  C C   . THR C  1 435 ? 80.644  89.746  254.400 1.00 188.43 ?  467 THR C C   1 
ATOM   7835  O O   . THR C  1 435 ? 81.599  90.438  254.771 1.00 188.27 ?  467 THR C O   1 
ATOM   7836  C CB  . THR C  1 435 ? 79.528  90.997  252.555 1.00 199.25 ?  467 THR C CB  1 
ATOM   7837  O OG1 . THR C  1 435 ? 78.308  91.623  252.141 1.00 208.65 ?  467 THR C OG1 1 
ATOM   7838  C CG2 . THR C  1 435 ? 79.900  89.917  251.557 1.00 194.14 ?  467 THR C CG2 1 
ATOM   7839  N N   . PHE C  1 436 ? 80.674  88.415  254.360 1.00 187.01 ?  468 PHE C N   1 
ATOM   7840  C CA  . PHE C  1 436 ? 81.832  87.632  254.764 1.00 179.56 ?  468 PHE C CA  1 
ATOM   7841  C C   . PHE C  1 436 ? 82.361  86.812  253.593 1.00 178.09 ?  468 PHE C C   1 
ATOM   7842  O O   . PHE C  1 436 ? 81.586  86.186  252.861 1.00 179.07 ?  468 PHE C O   1 
ATOM   7843  C CB  . PHE C  1 436 ? 81.444  86.710  255.914 1.00 173.17 ?  468 PHE C CB  1 
ATOM   7844  C CG  . PHE C  1 436 ? 81.016  87.444  257.147 1.00 179.05 ?  468 PHE C CG  1 
ATOM   7845  C CD1 . PHE C  1 436 ? 81.603  88.648  257.490 1.00 183.33 ?  468 PHE C CD1 1 
ATOM   7846  C CD2 . PHE C  1 436 ? 79.994  86.951  257.939 1.00 182.81 ?  468 PHE C CD2 1 
ATOM   7847  C CE1 . PHE C  1 436 ? 81.206  89.329  258.621 1.00 190.27 ?  468 PHE C CE1 1 
ATOM   7848  C CE2 . PHE C  1 436 ? 79.589  87.633  259.068 1.00 187.87 ?  468 PHE C CE2 1 
ATOM   7849  C CZ  . PHE C  1 436 ? 80.196  88.822  259.409 1.00 193.30 ?  468 PHE C CZ  1 
ATOM   7850  N N   . ARG C  1 437 ? 83.682  86.820  253.420 1.00 180.41 ?  469 ARG C N   1 
ATOM   7851  C CA  . ARG C  1 437 ? 84.371  86.121  252.346 1.00 175.41 ?  469 ARG C CA  1 
ATOM   7852  C C   . ARG C  1 437 ? 85.521  85.282  252.885 1.00 170.55 ?  469 ARG C C   1 
ATOM   7853  O O   . ARG C  1 437 ? 86.097  85.608  253.929 1.00 171.39 ?  469 ARG C O   1 
ATOM   7854  C CB  . ARG C  1 437 ? 84.898  87.109  251.294 1.00 175.47 ?  469 ARG C CB  1 
ATOM   7855  C CG  . ARG C  1 437 ? 83.825  88.008  250.710 1.00 180.06 ?  469 ARG C CG  1 
ATOM   7856  C CD  . ARG C  1 437 ? 84.413  89.081  249.814 1.00 183.97 ?  469 ARG C CD  1 
ATOM   7857  N NE  . ARG C  1 437 ? 83.391  90.038  249.401 1.00 194.70 ?  469 ARG C NE  1 
ATOM   7858  C CZ  . ARG C  1 437 ? 82.706  89.947  248.266 1.00 200.12 ?  469 ARG C CZ  1 
ATOM   7859  N NH1 . ARG C  1 437 ? 82.936  88.943  247.430 1.00 193.28 1  469 ARG C NH1 1 
ATOM   7860  N NH2 . ARG C  1 437 ? 81.790  90.858  247.964 1.00 208.31 ?  469 ARG C NH2 1 
ATOM   7861  N N   . PRO C  1 438 ? 85.874  84.193  252.199 1.00 165.06 ?  470 PRO C N   1 
ATOM   7862  C CA  . PRO C  1 438 ? 87.007  83.370  252.649 1.00 161.42 ?  470 PRO C CA  1 
ATOM   7863  C C   . PRO C  1 438 ? 88.344  84.067  252.437 1.00 161.25 ?  470 PRO C C   1 
ATOM   7864  O O   . PRO C  1 438 ? 88.576  84.710  251.411 1.00 162.65 ?  470 PRO C O   1 
ATOM   7865  C CB  . PRO C  1 438 ? 86.896  82.112  251.780 1.00 158.60 ?  470 PRO C CB  1 
ATOM   7866  C CG  . PRO C  1 438 ? 86.204  82.582  250.542 1.00 160.70 ?  470 PRO C CG  1 
ATOM   7867  C CD  . PRO C  1 438 ? 85.214  83.613  251.016 1.00 164.62 ?  470 PRO C CD  1 
ATOM   7868  N N   . GLY C  1 439 ? 89.231  83.930  253.418 1.00 164.01 ?  471 GLY C N   1 
ATOM   7869  C CA  . GLY C  1 439 ? 90.541  84.539  253.309 1.00 165.24 ?  471 GLY C CA  1 
ATOM   7870  C C   . GLY C  1 439 ? 91.650  83.582  253.693 1.00 162.26 ?  471 GLY C C   1 
ATOM   7871  O O   . GLY C  1 439 ? 91.452  82.363  253.688 1.00 157.47 ?  471 GLY C O   1 
ATOM   7872  N N   . GLY C  1 440 ? 92.823  84.109  254.025 1.00 162.73 ?  472 GLY C N   1 
ATOM   7873  C CA  . GLY C  1 440 ? 93.919  83.242  254.401 1.00 153.42 ?  472 GLY C CA  1 
ATOM   7874  C C   . GLY C  1 440 ? 95.269  83.882  254.177 1.00 157.63 ?  472 GLY C C   1 
ATOM   7875  O O   . GLY C  1 440 ? 95.591  84.908  254.784 1.00 160.78 ?  472 GLY C O   1 
ATOM   7876  N N   . GLY C  1 441 ? 96.073  83.272  253.310 1.00 168.40 ?  473 GLY C N   1 
ATOM   7877  C CA  . GLY C  1 441 ? 97.393  83.787  253.017 1.00 167.69 ?  473 GLY C CA  1 
ATOM   7878  C C   . GLY C  1 441 ? 98.404  83.467  254.096 1.00 164.35 ?  473 GLY C C   1 
ATOM   7879  O O   . GLY C  1 441 ? 99.239  82.572  253.938 1.00 164.67 ?  473 GLY C O   1 
ATOM   7880  N N   . ASP C  1 442 ? 98.327  84.196  255.203 1.00 171.88 ?  474 ASP C N   1 
ATOM   7881  C CA  . ASP C  1 442 ? 99.229  83.993  256.329 1.00 164.64 ?  474 ASP C CA  1 
ATOM   7882  C C   . ASP C  1 442 ? 98.960  82.657  257.008 1.00 157.04 ?  474 ASP C C   1 
ATOM   7883  O O   . ASP C  1 442 ? 97.895  82.457  257.601 1.00 154.44 ?  474 ASP C O   1 
ATOM   7884  C CB  . ASP C  1 442 ? 99.085  85.132  257.331 1.00 165.33 ?  474 ASP C CB  1 
ATOM   7885  C CG  . ASP C  1 442 ? 100.269 85.228  258.261 1.00 162.50 ?  474 ASP C CG  1 
ATOM   7886  O OD1 . ASP C  1 442 ? 101.376 84.823  257.846 1.00 159.56 ?  474 ASP C OD1 1 
ATOM   7887  O OD2 . ASP C  1 442 ? 100.089 85.682  259.412 1.00 168.77 -1 474 ASP C OD2 1 
ATOM   7888  N N   . MET C  1 443 ? 99.926  81.736  256.911 1.00 169.34 ?  475 MET C N   1 
ATOM   7889  C CA  . MET C  1 443 ? 99.771  80.411  257.493 1.00 161.34 ?  475 MET C CA  1 
ATOM   7890  C C   . MET C  1 443 ? 99.918  80.473  259.003 1.00 159.49 ?  475 MET C C   1 
ATOM   7891  O O   . MET C  1 443 ? 99.677  79.469  259.685 1.00 156.63 ?  475 MET C O   1 
ATOM   7892  C CB  . MET C  1 443 ? 100.799 79.440  256.904 1.00 157.68 ?  475 MET C CB  1 
ATOM   7893  C CG  . MET C  1 443 ? 100.837 79.446  255.387 1.00 167.85 ?  475 MET C CG  1 
ATOM   7894  S SD  . MET C  1 443 ? 99.248  79.026  254.650 1.00 179.03 ?  475 MET C SD  1 
ATOM   7895  C CE  . MET C  1 443 ? 99.622  79.175  252.900 1.00 169.28 ?  475 MET C CE  1 
ATOM   7896  N N   . ARG C  1 444 ? 100.310 81.637  259.524 1.00 160.91 ?  476 ARG C N   1 
ATOM   7897  C CA  . ARG C  1 444 ? 100.458 81.822  260.957 1.00 157.62 ?  476 ARG C CA  1 
ATOM   7898  C C   . ARG C  1 444 ? 99.104  81.733  261.641 1.00 159.08 ?  476 ARG C C   1 
ATOM   7899  O O   . ARG C  1 444 ? 99.025  81.358  262.815 1.00 159.83 ?  476 ARG C O   1 
ATOM   7900  C CB  . ARG C  1 444 ? 101.146 83.167  261.177 1.00 163.15 ?  476 ARG C CB  1 
ATOM   7901  C CG  . ARG C  1 444 ? 102.638 83.012  261.211 1.00 164.64 ?  476 ARG C CG  1 
ATOM   7902  C CD  . ARG C  1 444 ? 103.380 84.317  261.217 1.00 175.99 ?  476 ARG C CD  1 
ATOM   7903  N NE  . ARG C  1 444 ? 104.166 84.292  259.985 1.00 180.32 ?  476 ARG C NE  1 
ATOM   7904  C CZ  . ARG C  1 444 ? 104.891 85.289  259.494 1.00 186.10 ?  476 ARG C CZ  1 
ATOM   7905  N NH1 . ARG C  1 444 ? 104.959 86.452  260.124 1.00 189.64 1  476 ARG C NH1 1 
ATOM   7906  N NH2 . ARG C  1 444 ? 105.541 85.111  258.348 1.00 191.46 ?  476 ARG C NH2 1 
ATOM   7907  N N   . ASP C  1 445 ? 98.038  82.049  260.911 1.00 158.05 ?  477 ASP C N   1 
ATOM   7908  C CA  . ASP C  1 445 ? 96.693  81.934  261.457 1.00 159.49 ?  477 ASP C CA  1 
ATOM   7909  C C   . ASP C  1 445 ? 96.345  80.468  261.686 1.00 153.08 ?  477 ASP C C   1 
ATOM   7910  O O   . ASP C  1 445 ? 95.610  80.138  262.622 1.00 151.17 ?  477 ASP C O   1 
ATOM   7911  C CB  . ASP C  1 445 ? 95.680  82.608  260.529 1.00 167.81 ?  477 ASP C CB  1 
ATOM   7912  C CG  . ASP C  1 445 ? 96.013  84.072  260.263 1.00 175.33 ?  477 ASP C CG  1 
ATOM   7913  O OD1 . ASP C  1 445 ? 96.489  84.764  261.192 1.00 174.71 ?  477 ASP C OD1 1 
ATOM   7914  O OD2 . ASP C  1 445 ? 95.816  84.527  259.117 1.00 179.89 -1 477 ASP C OD2 1 
ATOM   7915  N N   . ASN C  1 446 ? 96.868  79.583  260.825 1.00 155.25 ?  478 ASN C N   1 
ATOM   7916  C CA  . ASN C  1 446 ? 96.589  78.152  260.910 1.00 152.87 ?  478 ASN C CA  1 
ATOM   7917  C C   . ASN C  1 446 ? 97.098  77.539  262.205 1.00 148.65 ?  478 ASN C C   1 
ATOM   7918  O O   . ASN C  1 446 ? 96.513  76.573  262.706 1.00 148.88 ?  478 ASN C O   1 
ATOM   7919  C CB  . ASN C  1 446 ? 97.274  77.433  259.750 1.00 153.38 ?  478 ASN C CB  1 
ATOM   7920  C CG  . ASN C  1 446 ? 96.795  77.902  258.404 1.00 156.07 ?  478 ASN C CG  1 
ATOM   7921  O OD1 . ASN C  1 446 ? 96.225  78.985  258.276 1.00 159.25 ?  478 ASN C OD1 1 
ATOM   7922  N ND2 . ASN C  1 446 ? 97.073  77.111  257.376 1.00 154.67 ?  478 ASN C ND2 1 
ATOM   7923  N N   . TRP C  1 447 ? 98.174  78.084  262.761 1.00 150.75 ?  479 TRP C N   1 
ATOM   7924  C CA  . TRP C  1 447 ? 98.723  77.562  264.003 1.00 148.33 ?  479 TRP C CA  1 
ATOM   7925  C C   . TRP C  1 447 ? 97.966  78.112  265.198 1.00 150.32 ?  479 TRP C C   1 
ATOM   7926  O O   . TRP C  1 447 ? 97.914  77.476  266.258 1.00 151.18 ?  479 TRP C O   1 
ATOM   7927  C CB  . TRP C  1 447 ? 100.208 77.901  264.090 1.00 148.06 ?  479 TRP C CB  1 
ATOM   7928  C CG  . TRP C  1 447 ? 100.895 77.842  262.757 1.00 148.69 ?  479 TRP C CG  1 
ATOM   7929  C CD1 . TRP C  1 447 ? 101.575 78.853  262.148 1.00 151.78 ?  479 TRP C CD1 1 
ATOM   7930  C CD2 . TRP C  1 447 ? 100.943 76.729  261.856 1.00 146.23 ?  479 TRP C CD2 1 
ATOM   7931  N NE1 . TRP C  1 447 ? 102.055 78.439  260.931 1.00 148.96 ?  479 TRP C NE1 1 
ATOM   7932  C CE2 . TRP C  1 447 ? 101.680 77.138  260.728 1.00 146.17 ?  479 TRP C CE2 1 
ATOM   7933  C CE3 . TRP C  1 447 ? 100.440 75.426  261.895 1.00 144.59 ?  479 TRP C CE3 1 
ATOM   7934  C CZ2 . TRP C  1 447 ? 101.927 76.293  259.652 1.00 144.38 ?  479 TRP C CZ2 1 
ATOM   7935  C CZ3 . TRP C  1 447 ? 100.686 74.590  260.828 1.00 142.29 ?  479 TRP C CZ3 1 
ATOM   7936  C CH2 . TRP C  1 447 ? 101.423 75.025  259.722 1.00 142.70 ?  479 TRP C CH2 1 
ATOM   7937  N N   . ARG C  1 448 ? 97.388  79.299  265.031 1.00 142.85 ?  480 ARG C N   1 
ATOM   7938  C CA  . ARG C  1 448 ? 96.658  79.992  266.079 1.00 150.22 ?  480 ARG C CA  1 
ATOM   7939  C C   . ARG C  1 448 ? 95.372  79.262  266.444 1.00 151.26 ?  480 ARG C C   1 
ATOM   7940  O O   . ARG C  1 448 ? 94.840  79.474  267.538 1.00 154.41 ?  480 ARG C O   1 
ATOM   7941  C CB  . ARG C  1 448 ? 96.357  81.393  265.556 1.00 154.38 ?  480 ARG C CB  1 
ATOM   7942  C CG  . ARG C  1 448 ? 97.627  82.183  265.322 1.00 152.21 ?  480 ARG C CG  1 
ATOM   7943  C CD  . ARG C  1 448 ? 97.403  83.631  264.961 1.00 163.98 ?  480 ARG C CD  1 
ATOM   7944  N NE  . ARG C  1 448 ? 98.690  84.275  264.716 1.00 163.81 ?  480 ARG C NE  1 
ATOM   7945  C CZ  . ARG C  1 448 ? 98.853  85.374  263.987 1.00 170.89 ?  480 ARG C CZ  1 
ATOM   7946  N NH1 . ARG C  1 448 ? 97.807  85.964  263.423 1.00 171.08 1  480 ARG C NH1 1 
ATOM   7947  N NH2 . ARG C  1 448 ? 100.066 85.876  263.809 1.00 172.27 ?  480 ARG C NH2 1 
ATOM   7948  N N   . SER C  1 449 ? 94.866  78.407  265.546 1.00 143.30 ?  481 SER C N   1 
ATOM   7949  C CA  . SER C  1 449 ? 93.641  77.651  265.776 1.00 146.30 ?  481 SER C CA  1 
ATOM   7950  C C   . SER C  1 449 ? 93.850  76.459  266.695 1.00 142.96 ?  481 SER C C   1 
ATOM   7951  O O   . SER C  1 449 ? 92.871  75.817  267.092 1.00 143.49 ?  481 SER C O   1 
ATOM   7952  C CB  . SER C  1 449 ? 93.080  77.154  264.444 1.00 149.96 ?  481 SER C CB  1 
ATOM   7953  O OG  . SER C  1 449 ? 93.991  76.257  263.830 1.00 147.87 ?  481 SER C OG  1 
ATOM   7954  N N   . GLU C  1 450 ? 95.098  76.148  267.029 1.00 148.71 ?  482 GLU C N   1 
ATOM   7955  C CA  . GLU C  1 450 ? 95.436  75.031  267.893 1.00 147.15 ?  482 GLU C CA  1 
ATOM   7956  C C   . GLU C  1 450 ? 96.251  75.453  269.097 1.00 144.70 ?  482 GLU C C   1 
ATOM   7957  O O   . GLU C  1 450 ? 96.267  74.728  270.097 1.00 138.19 ?  482 GLU C O   1 
ATOM   7958  C CB  . GLU C  1 450 ? 96.187  73.946  267.110 1.00 143.39 ?  482 GLU C CB  1 
ATOM   7959  C CG  . GLU C  1 450 ? 95.363  73.417  265.955 1.00 147.00 ?  482 GLU C CG  1 
ATOM   7960  C CD  . GLU C  1 450 ? 94.097  72.723  266.420 1.00 154.21 ?  482 GLU C CD  1 
ATOM   7961  O OE1 . GLU C  1 450 ? 94.094  72.163  267.539 1.00 155.88 ?  482 GLU C OE1 1 
ATOM   7962  O OE2 . GLU C  1 450 ? 93.095  72.764  265.676 1.00 157.32 -1 482 GLU C OE2 1 
ATOM   7963  N N   . LEU C  1 451 ? 96.923  76.601  269.025 1.00 147.50 ?  483 LEU C N   1 
ATOM   7964  C CA  . LEU C  1 451 ? 97.759  77.127  270.089 1.00 140.77 ?  483 LEU C CA  1 
ATOM   7965  C C   . LEU C  1 451 ? 97.038  78.218  270.869 1.00 141.79 ?  483 LEU C C   1 
ATOM   7966  O O   . LEU C  1 451 ? 97.677  79.005  271.577 1.00 140.91 ?  483 LEU C O   1 
ATOM   7967  C CB  . LEU C  1 451 ? 99.060  77.670  269.498 1.00 139.83 ?  483 LEU C CB  1 
ATOM   7968  C CG  . LEU C  1 451 ? 99.996  76.621  268.899 1.00 137.76 ?  483 LEU C CG  1 
ATOM   7969  C CD1 . LEU C  1 451 ? 101.189 77.283  268.235 1.00 138.39 ?  483 LEU C CD1 1 
ATOM   7970  C CD2 . LEU C  1 451 ? 100.448 75.626  269.950 1.00 134.34 ?  483 LEU C CD2 1 
ATOM   7971  N N   . TYR C  1 452 ? 95.709  78.272  270.747 1.00 139.53 ?  484 TYR C N   1 
ATOM   7972  C CA  . TYR C  1 452 ? 94.917  79.290  271.422 1.00 141.15 ?  484 TYR C CA  1 
ATOM   7973  C C   . TYR C  1 452 ? 94.803  79.016  272.910 1.00 139.84 ?  484 TYR C C   1 
ATOM   7974  O O   . TYR C  1 452 ? 94.516  79.940  273.679 1.00 143.36 ?  484 TYR C O   1 
ATOM   7975  C CB  . TYR C  1 452 ? 93.535  79.372  270.769 1.00 146.72 ?  484 TYR C CB  1 
ATOM   7976  C CG  . TYR C  1 452 ? 92.639  78.184  271.056 1.00 147.13 ?  484 TYR C CG  1 
ATOM   7977  C CD1 . TYR C  1 452 ? 92.722  77.037  270.274 1.00 146.14 ?  484 TYR C CD1 1 
ATOM   7978  C CD2 . TYR C  1 452 ? 91.695  78.211  272.077 1.00 149.01 ?  484 TYR C CD2 1 
ATOM   7979  C CE1 . TYR C  1 452 ? 91.910  75.945  270.510 1.00 143.83 ?  484 TYR C CE1 1 
ATOM   7980  C CE2 . TYR C  1 452 ? 90.874  77.118  272.319 1.00 146.57 ?  484 TYR C CE2 1 
ATOM   7981  C CZ  . TYR C  1 452 ? 90.987  75.990  271.531 1.00 145.05 ?  484 TYR C CZ  1 
ATOM   7982  O OH  . TYR C  1 452 ? 90.176  74.903  271.768 1.00 142.91 ?  484 TYR C OH  1 
ATOM   7983  N N   . LYS C  1 453 ? 95.019  77.769  273.330 1.00 138.63 ?  485 LYS C N   1 
ATOM   7984  C CA  . LYS C  1 453 ? 94.897  77.381  274.726 1.00 134.95 ?  485 LYS C CA  1 
ATOM   7985  C C   . LYS C  1 453 ? 96.258  77.177  275.379 1.00 131.36 ?  485 LYS C C   1 
ATOM   7986  O O   . LYS C  1 453 ? 96.331  76.567  276.446 1.00 132.99 ?  485 LYS C O   1 
ATOM   7987  C CB  . LYS C  1 453 ? 94.083  76.095  274.887 1.00 136.07 ?  485 LYS C CB  1 
ATOM   7988  C CG  . LYS C  1 453 ? 94.608  74.920  274.070 1.00 134.53 ?  485 LYS C CG  1 
ATOM   7989  C CD  . LYS C  1 453 ? 93.899  73.613  274.419 1.00 129.63 ?  485 LYS C CD  1 
ATOM   7990  C CE  . LYS C  1 453 ? 92.407  73.653  274.181 1.00 130.04 ?  485 LYS C CE  1 
ATOM   7991  N NZ  . LYS C  1 453 ? 91.794  72.340  274.536 1.00 129.72 1  485 LYS C NZ  1 
ATOM   7992  N N   . TYR C  1 454 ? 97.341  77.674  274.780 1.00 137.68 ?  486 TYR C N   1 
ATOM   7993  C CA  . TYR C  1 454 ? 98.659  77.485  275.370 1.00 135.18 ?  486 TYR C CA  1 
ATOM   7994  C C   . TYR C  1 454 ? 99.462  78.779  275.404 1.00 136.99 ?  486 TYR C C   1 
ATOM   7995  O O   . TYR C  1 454 ? 99.325  79.641  274.531 1.00 139.01 ?  486 TYR C O   1 
ATOM   7996  C CB  . TYR C  1 454 ? 99.477  76.443  274.576 1.00 135.61 ?  486 TYR C CB  1 
ATOM   7997  C CG  . TYR C  1 454 ? 98.873  75.056  274.499 1.00 136.53 ?  486 TYR C CG  1 
ATOM   7998  C CD1 . TYR C  1 454 ? 98.870  74.213  275.601 1.00 137.14 ?  486 TYR C CD1 1 
ATOM   7999  C CD2 . TYR C  1 454 ? 98.333  74.578  273.310 1.00 139.56 ?  486 TYR C CD2 1 
ATOM   8000  C CE1 . TYR C  1 454 ? 98.327  72.940  275.527 1.00 138.14 ?  486 TYR C CE1 1 
ATOM   8001  C CE2 . TYR C  1 454 ? 97.789  73.308  273.226 1.00 139.35 ?  486 TYR C CE2 1 
ATOM   8002  C CZ  . TYR C  1 454 ? 97.789  72.494  274.337 1.00 136.71 ?  486 TYR C CZ  1 
ATOM   8003  O OH  . TYR C  1 454 ? 97.250  71.230  274.262 1.00 143.97 ?  486 TYR C OH  1 
ATOM   8004  N N   . LYS C  1 455 ? 100.305 78.898  276.432 1.00 144.15 ?  487 LYS C N   1 
ATOM   8005  C CA  . LYS C  1 455 ? 101.241 80.008  276.546 1.00 149.50 ?  487 LYS C CA  1 
ATOM   8006  C C   . LYS C  1 455 ? 102.400 79.574  277.437 1.00 146.40 ?  487 LYS C C   1 
ATOM   8007  O O   . LYS C  1 455 ? 102.243 78.724  278.319 1.00 138.45 ?  487 LYS C O   1 
ATOM   8008  C CB  . LYS C  1 455 ? 100.559 81.280  277.067 1.00 152.25 ?  487 LYS C CB  1 
ATOM   8009  C CG  . LYS C  1 455 ? 100.500 81.453  278.565 1.00 147.22 ?  487 LYS C CG  1 
ATOM   8010  C CD  . LYS C  1 455 ? 100.058 82.874  278.867 1.00 152.51 ?  487 LYS C CD  1 
ATOM   8011  C CE  . LYS C  1 455 ? 100.234 83.232  280.324 1.00 150.48 ?  487 LYS C CE  1 
ATOM   8012  N NZ  . LYS C  1 455 ? 99.892  84.662  280.559 1.00 157.51 1  487 LYS C NZ  1 
ATOM   8013  N N   . VAL C  1 456 ? 103.562 80.168  277.179 1.00 150.26 ?  488 VAL C N   1 
ATOM   8014  C CA  . VAL C  1 456 ? 104.826 79.827  277.827 1.00 142.55 ?  488 VAL C CA  1 
ATOM   8015  C C   . VAL C  1 456 ? 105.100 80.778  278.984 1.00 141.03 ?  488 VAL C C   1 
ATOM   8016  O O   . VAL C  1 456 ? 104.973 81.999  278.834 1.00 146.34 ?  488 VAL C O   1 
ATOM   8017  C CB  . VAL C  1 456 ? 105.986 79.848  276.819 1.00 146.61 ?  488 VAL C CB  1 
ATOM   8018  C CG1 . VAL C  1 456 ? 107.285 79.449  277.500 1.00 144.09 ?  488 VAL C CG1 1 
ATOM   8019  C CG2 . VAL C  1 456 ? 105.688 78.926  275.649 1.00 147.03 ?  488 VAL C CG2 1 
ATOM   8020  N N   . VAL C  1 457 ? 105.455 80.223  280.144 1.00 133.81 ?  489 VAL C N   1 
ATOM   8021  C CA  . VAL C  1 457 ? 105.828 81.018  281.308 1.00 135.28 ?  489 VAL C CA  1 
ATOM   8022  C C   . VAL C  1 457 ? 107.142 80.486  281.864 1.00 135.63 ?  489 VAL C C   1 
ATOM   8023  O O   . VAL C  1 457 ? 107.471 79.306  281.701 1.00 134.21 ?  489 VAL C O   1 
ATOM   8024  C CB  . VAL C  1 457 ? 104.735 80.986  282.399 1.00 134.13 ?  489 VAL C CB  1 
ATOM   8025  C CG1 . VAL C  1 457 ? 103.484 81.672  281.905 1.00 134.51 ?  489 VAL C CG1 1 
ATOM   8026  C CG2 . VAL C  1 457 ? 104.439 79.553  282.835 1.00 131.58 ?  489 VAL C CG2 1 
ATOM   8027  N N   . LYS C  1 458 ? 107.899 81.364  282.524 1.00 138.73 ?  490 LYS C N   1 
ATOM   8028  C CA  . LYS C  1 458 ? 109.160 80.991  283.149 1.00 140.96 ?  490 LYS C CA  1 
ATOM   8029  C C   . LYS C  1 458 ? 108.973 81.015  284.659 1.00 142.64 ?  490 LYS C C   1 
ATOM   8030  O O   . LYS C  1 458 ? 108.319 81.909  285.196 1.00 142.77 ?  490 LYS C O   1 
ATOM   8031  C CB  . LYS C  1 458 ? 110.329 81.915  282.782 1.00 148.49 ?  490 LYS C CB  1 
ATOM   8032  C CG  . LYS C  1 458 ? 110.170 83.386  283.135 1.00 152.44 ?  490 LYS C CG  1 
ATOM   8033  C CD  . LYS C  1 458 ? 111.438 84.145  282.763 1.00 159.44 ?  490 LYS C CD  1 
ATOM   8034  C CE  . LYS C  1 458 ? 111.322 85.624  283.073 1.00 166.89 ?  490 LYS C CE  1 
ATOM   8035  N NZ  . LYS C  1 458 ? 111.743 86.460  281.921 1.00 163.61 1  490 LYS C NZ  1 
ATOM   8036  N N   . ILE C  1 459 ? 109.604 80.074  285.336 1.00 130.26 ?  491 ILE C N   1 
ATOM   8037  C CA  . ILE C  1 459 ? 109.500 79.923  286.783 1.00 130.15 ?  491 ILE C CA  1 
ATOM   8038  C C   . ILE C  1 459 ? 110.603 80.710  287.477 1.00 132.34 ?  491 ILE C C   1 
ATOM   8039  O O   . ILE C  1 459 ? 111.787 80.568  287.146 1.00 133.45 ?  491 ILE C O   1 
ATOM   8040  C CB  . ILE C  1 459 ? 109.544 78.441  287.187 1.00 128.65 ?  491 ILE C CB  1 
ATOM   8041  C CG1 . ILE C  1 459 ? 108.397 77.672  286.530 1.00 126.64 ?  491 ILE C CG1 1 
ATOM   8042  C CG2 . ILE C  1 459 ? 109.483 78.303  288.689 1.00 128.66 ?  491 ILE C CG2 1 
ATOM   8043  C CD1 . ILE C  1 459 ? 107.033 78.191  286.905 1.00 125.89 ?  491 ILE C CD1 1 
ATOM   8044  N N   . GLU C  1 460 ? 110.216 81.545  288.444 1.00 140.37 ?  492 GLU C N   1 
ATOM   8045  C CA  . GLU C  1 460 ? 111.163 82.309  289.254 1.00 141.47 ?  492 GLU C CA  1 
ATOM   8046  C C   . GLU C  1 460 ? 110.955 81.779  290.665 1.00 137.76 ?  492 GLU C C   1 
ATOM   8047  O O   . GLU C  1 460 ? 110.177 82.335  291.456 1.00 138.44 ?  492 GLU C O   1 
ATOM   8048  C CB  . GLU C  1 460 ? 110.911 83.816  289.197 1.00 144.13 ?  492 GLU C CB  1 
ATOM   8049  C CG  . GLU C  1 460 ? 111.039 84.462  287.830 1.00 153.01 ?  492 GLU C CG  1 
ATOM   8050  C CD  . GLU C  1 460 ? 110.770 85.956  287.876 1.00 154.85 ?  492 GLU C CD  1 
ATOM   8051  O OE1 . GLU C  1 460 ? 110.419 86.461  288.964 1.00 160.35 ?  492 GLU C OE1 1 
ATOM   8052  O OE2 . GLU C  1 460 ? 110.921 86.626  286.832 1.00 151.30 -1 492 GLU C OE2 1 
ATOM   8053  N N   . PRO C  1 461 ? 111.643 80.685  291.007 1.00 133.81 ?  493 PRO C N   1 
ATOM   8054  C CA  . PRO C  1 461 ? 111.408 79.994  292.285 1.00 133.01 ?  493 PRO C CA  1 
ATOM   8055  C C   . PRO C  1 461 ? 111.899 80.758  293.491 1.00 134.82 ?  493 PRO C C   1 
ATOM   8056  O O   . PRO C  1 461 ? 111.696 80.292  294.619 1.00 134.34 ?  493 PRO C O   1 
ATOM   8057  C CB  . PRO C  1 461 ? 112.187 78.687  292.117 1.00 132.33 ?  493 PRO C CB  1 
ATOM   8058  C CG  . PRO C  1 461 ? 113.311 79.063  291.208 1.00 133.87 ?  493 PRO C CG  1 
ATOM   8059  C CD  . PRO C  1 461 ? 112.726 80.053  290.233 1.00 134.13 ?  493 PRO C CD  1 
ATOM   8060  N N   . LEU C  1 462 ? 112.577 81.880  293.286 1.00 147.45 ?  494 LEU C N   1 
ATOM   8061  C CA  . LEU C  1 462 ? 113.118 82.694  294.364 1.00 153.14 ?  494 LEU C CA  1 
ATOM   8062  C C   . LEU C  1 462 ? 112.098 83.724  294.832 1.00 154.80 ?  494 LEU C C   1 
ATOM   8063  O O   . LEU C  1 462 ? 111.775 84.672  294.109 1.00 158.65 ?  494 LEU C O   1 
ATOM   8064  C CB  . LEU C  1 462 ? 114.398 83.372  293.891 1.00 159.43 ?  494 LEU C CB  1 
ATOM   8065  C CG  . LEU C  1 462 ? 115.594 82.430  293.994 1.00 161.04 ?  494 LEU C CG  1 
ATOM   8066  C CD1 . LEU C  1 462 ? 116.867 83.112  293.523 1.00 165.69 ?  494 LEU C CD1 1 
ATOM   8067  C CD2 . LEU C  1 462 ? 115.738 81.888  295.411 1.00 155.96 ?  494 LEU C CD2 1 
ATOM   8068  N N   . GLY C  1 463 ? 111.579 83.516  296.037 1.00 171.78 ?  495 GLY C N   1 
ATOM   8069  C CA  . GLY C  1 463 ? 110.628 84.418  296.648 1.00 173.94 ?  495 GLY C CA  1 
ATOM   8070  C C   . GLY C  1 463 ? 111.034 84.629  298.091 1.00 181.08 ?  495 GLY C C   1 
ATOM   8071  O O   . GLY C  1 463 ? 111.271 83.670  298.832 1.00 175.67 ?  495 GLY C O   1 
ATOM   8072  N N   . VAL C  1 464 ? 111.127 85.889  298.492 1.00 190.51 ?  496 VAL C N   1 
ATOM   8073  C CA  . VAL C  1 464 ? 111.509 86.279  299.844 1.00 187.04 ?  496 VAL C CA  1 
ATOM   8074  C C   . VAL C  1 464 ? 110.258 86.604  300.644 1.00 187.68 ?  496 VAL C C   1 
ATOM   8075  O O   . VAL C  1 464 ? 109.284 87.144  300.101 1.00 186.32 ?  496 VAL C O   1 
ATOM   8076  C CB  . VAL C  1 464 ? 112.469 87.485  299.807 1.00 190.79 ?  496 VAL C CB  1 
ATOM   8077  C CG1 . VAL C  1 464 ? 113.134 87.697  301.163 1.00 198.12 ?  496 VAL C CG1 1 
ATOM   8078  C CG2 . VAL C  1 464 ? 113.506 87.310  298.703 1.00 194.42 ?  496 VAL C CG2 1 
ATOM   8079  N N   . ALA C  1 465 ? 110.271 86.274  301.939 1.00 191.28 ?  497 ALA C N   1 
ATOM   8080  C CA  . ALA C  1 465 ? 109.089 86.547  302.733 1.00 191.24 ?  497 ALA C CA  1 
ATOM   8081  C C   . ALA C  1 465 ? 109.449 86.770  304.194 1.00 191.26 ?  497 ALA C C   1 
ATOM   8082  O O   . ALA C  1 465 ? 110.357 86.107  304.717 1.00 191.53 ?  497 ALA C O   1 
ATOM   8083  C CB  . ALA C  1 465 ? 108.082 85.398  302.618 1.00 186.52 ?  497 ALA C CB  1 
ATOM   8084  N N   . PRO C  1 466 ? 108.761 87.692  304.863 1.00 183.83 ?  498 PRO C N   1 
ATOM   8085  C CA  . PRO C  1 466 ? 109.066 87.993  306.266 1.00 188.95 ?  498 PRO C CA  1 
ATOM   8086  C C   . PRO C  1 466 ? 108.401 87.044  307.252 1.00 188.53 ?  498 PRO C C   1 
ATOM   8087  O O   . PRO C  1 466 ? 107.275 86.586  307.044 1.00 186.49 ?  498 PRO C O   1 
ATOM   8088  C CB  . PRO C  1 466 ? 108.529 89.419  306.433 1.00 194.48 ?  498 PRO C CB  1 
ATOM   8089  C CG  . PRO C  1 466 ? 107.373 89.470  305.491 1.00 190.95 ?  498 PRO C CG  1 
ATOM   8090  C CD  . PRO C  1 466 ? 107.765 88.623  304.304 1.00 186.06 ?  498 PRO C CD  1 
ATOM   8091  N N   . THR C  1 467 ? 109.115 86.759  308.337 1.00 188.67 ?  499 THR C N   1 
ATOM   8092  C CA  . THR C  1 467 ? 108.574 85.966  309.431 1.00 192.60 ?  499 THR C CA  1 
ATOM   8093  C C   . THR C  1 467 ? 109.445 86.220  310.649 1.00 197.69 ?  499 THR C C   1 
ATOM   8094  O O   . THR C  1 467 ? 110.592 86.666  310.544 1.00 199.98 ?  499 THR C O   1 
ATOM   8095  C CB  . THR C  1 467 ? 108.501 84.463  309.115 1.00 184.55 ?  499 THR C CB  1 
ATOM   8096  O OG1 . THR C  1 467 ? 108.047 83.743  310.270 1.00 187.31 ?  499 THR C OG1 1 
ATOM   8097  C CG2 . THR C  1 467 ? 109.851 83.938  308.743 1.00 181.45 ?  499 THR C CG2 1 
ATOM   8098  N N   . ARG C  1 468 ? 108.876 85.913  311.807 1.00 194.61 ?  500 ARG C N   1 
ATOM   8099  C CA  . ARG C  1 468 ? 109.499 86.111  313.106 1.00 196.85 ?  500 ARG C CA  1 
ATOM   8100  C C   . ARG C  1 468 ? 110.531 85.031  313.430 1.00 203.94 ?  500 ARG C C   1 
ATOM   8101  O O   . ARG C  1 468 ? 110.506 84.435  314.510 1.00 205.69 ?  500 ARG C O   1 
ATOM   8102  C CB  . ARG C  1 468 ? 108.354 86.234  314.121 1.00 197.84 ?  500 ARG C CB  1 
ATOM   8103  C CG  . ARG C  1 468 ? 107.341 85.107  313.967 1.00 195.96 ?  500 ARG C CG  1 
ATOM   8104  C CD  . ARG C  1 468 ? 106.187 85.156  314.952 1.00 197.24 ?  500 ARG C CD  1 
ATOM   8105  N NE  . ARG C  1 468 ? 105.346 83.972  314.793 1.00 197.14 ?  500 ARG C NE  1 
ATOM   8106  C CZ  . ARG C  1 468 ? 104.159 83.807  315.367 1.00 198.24 ?  500 ARG C CZ  1 
ATOM   8107  N NH1 . ARG C  1 468 ? 103.656 84.757  316.143 1.00 201.57 1  500 ARG C NH1 1 
ATOM   8108  N NH2 . ARG C  1 468 ? 103.467 82.698  315.149 1.00 200.51 ?  500 ARG C NH2 1 
ATOM   8109  N N   . CYS C  1 469 ? 111.450 84.805  312.482 1.00 193.53 ?  501 CYS C N   1 
ATOM   8110  C CA  . CYS C  1 469 ? 112.535 83.825  312.553 1.00 193.81 ?  501 CYS C CA  1 
ATOM   8111  C C   . CYS C  1 469 ? 113.891 84.470  312.354 1.00 189.10 ?  501 CYS C C   1 
ATOM   8112  O O   . CYS C  1 469 ? 114.099 85.175  311.361 1.00 184.27 ?  501 CYS C O   1 
ATOM   8113  C CB  . CYS C  1 469 ? 112.456 82.742  311.477 1.00 196.25 ?  501 CYS C CB  1 
ATOM   8114  S SG  . CYS C  1 469 ? 113.913 81.627  311.532 1.00 235.33 ?  501 CYS C SG  1 
ATOM   8115  N N   . LYS C  1 470 ? 114.808 84.231  313.290 1.00 190.71 ?  502 LYS C N   1 
ATOM   8116  C CA  . LYS C  1 470 ? 116.161 84.754  313.180 1.00 189.29 ?  502 LYS C CA  1 
ATOM   8117  C C   . LYS C  1 470 ? 117.127 83.579  313.319 1.00 185.73 ?  502 LYS C C   1 
ATOM   8118  O O   . LYS C  1 470 ? 116.844 82.605  314.025 1.00 186.16 ?  502 LYS C O   1 
ATOM   8119  C CB  . LYS C  1 470 ? 116.473 85.862  314.191 1.00 199.62 ?  502 LYS C CB  1 
ATOM   8120  C CG  . LYS C  1 470 ? 117.830 86.502  313.918 1.00 207.66 ?  502 LYS C CG  1 
ATOM   8121  C CD  . LYS C  1 470 ? 118.236 87.506  314.968 1.00 204.67 ?  502 LYS C CD  1 
ATOM   8122  C CE  . LYS C  1 470 ? 119.617 88.044  314.646 1.00 211.77 ?  502 LYS C CE  1 
ATOM   8123  N NZ  . LYS C  1 470 ? 120.093 89.005  315.675 1.00 211.56 1  502 LYS C NZ  1 
ATOM   8124  N N   . ARG C  1 471 ? 118.280 83.675  312.649 1.00 186.90 ?  503 ARG C N   1 
ATOM   8125  C CA  . ARG C  1 471 ? 119.260 82.595  312.704 1.00 195.88 ?  503 ARG C CA  1 
ATOM   8126  C C   . ARG C  1 471 ? 120.074 82.656  313.992 1.00 206.84 ?  503 ARG C C   1 
ATOM   8127  O O   . ARG C  1 471 ? 119.665 83.317  314.952 1.00 213.41 ?  503 ARG C O   1 
ATOM   8128  C CB  . ARG C  1 471 ? 120.184 82.692  311.481 1.00 194.80 ?  503 ARG C CB  1 
ATOM   8129  C CG  . ARG C  1 471 ? 119.773 81.853  310.267 1.00 187.48 ?  503 ARG C CG  1 
ATOM   8130  C CD  . ARG C  1 471 ? 120.910 81.791  309.254 1.00 182.78 ?  503 ARG C CD  1 
ATOM   8131  N NE  . ARG C  1 471 ? 121.148 83.113  308.677 1.00 181.72 ?  503 ARG C NE  1 
ATOM   8132  C CZ  . ARG C  1 471 ? 122.190 83.429  307.916 1.00 186.30 ?  503 ARG C CZ  1 
ATOM   8133  N NH1 . ARG C  1 471 ? 123.112 82.518  307.634 1.00 191.48 1  503 ARG C NH1 1 
ATOM   8134  N NH2 . ARG C  1 471 ? 122.314 84.662  307.445 1.00 186.44 ?  503 ARG C NH2 1 
ATOM   8135  N N   . ARG C  1 472 ? 121.216 81.973  314.033 1.00 210.28 ?  504 ARG C N   1 
ATOM   8136  C CA  . ARG C  1 472 ? 122.039 81.929  315.236 1.00 219.09 ?  504 ARG C CA  1 
ATOM   8137  C C   . ARG C  1 472 ? 123.127 83.001  315.188 1.00 223.37 ?  504 ARG C C   1 
ATOM   8138  O O   . ARG C  1 472 ? 123.078 83.937  314.384 1.00 218.64 ?  504 ARG C O   1 
ATOM   8139  C CB  . ARG C  1 472 ? 122.625 80.528  315.451 1.00 219.10 ?  504 ARG C CB  1 
ATOM   8140  C CG  . ARG C  1 472 ? 121.599 79.432  315.686 1.00 213.42 ?  504 ARG C CG  1 
ATOM   8141  C CD  . ARG C  1 472 ? 122.152 78.073  315.292 1.00 214.74 ?  504 ARG C CD  1 
ATOM   8142  N NE  . ARG C  1 472 ? 122.333 77.962  313.849 1.00 215.36 ?  504 ARG C NE  1 
ATOM   8143  C CZ  . ARG C  1 472 ? 121.398 77.513  313.019 1.00 216.49 ?  504 ARG C CZ  1 
ATOM   8144  N NH1 . ARG C  1 472 ? 120.220 77.132  313.495 1.00 215.88 1  504 ARG C NH1 1 
ATOM   8145  N NH2 . ARG C  1 472 ? 121.637 77.444  311.717 1.00 220.99 ?  504 ARG C NH2 1 
ATOM   8146  N N   . VAL C  1 473 ? 124.138 82.839  316.032 1.00 226.97 ?  505 VAL C N   1 
ATOM   8147  C CA  . VAL C  1 473 ? 125.234 83.778  316.136 1.00 229.41 ?  505 VAL C CA  1 
ATOM   8148  C C   . VAL C  1 473 ? 126.524 83.042  315.788 1.00 230.54 ?  505 VAL C C   1 
ATOM   8149  O O   . VAL C  1 473 ? 126.543 81.810  315.721 1.00 229.83 ?  505 VAL C O   1 
ATOM   8150  C CB  . VAL C  1 473 ? 125.299 84.405  317.547 1.00 228.77 ?  505 VAL C CB  1 
ATOM   8151  C CG1 . VAL C  1 473 ? 126.686 84.828  317.872 1.00 234.36 ?  505 VAL C CG1 1 
ATOM   8152  C CG2 . VAL C  1 473 ? 124.403 85.596  317.632 1.00 226.67 ?  505 VAL C CG2 1 
ATOM   8153  N N   . ALA D  3 1   ? 93.106  41.057  206.680 1.00 283.28 ?  6   ALA L N   1 
ATOM   8154  C CA  . ALA D  3 1   ? 91.977  41.842  207.180 1.00 283.56 ?  6   ALA L CA  1 
ATOM   8155  C C   . ALA D  3 1   ? 90.807  40.985  207.729 1.00 288.16 ?  6   ALA L C   1 
ATOM   8156  O O   . ALA D  3 1   ? 90.327  41.255  208.828 1.00 277.55 ?  6   ALA L O   1 
ATOM   8157  C CB  . ALA D  3 1   ? 91.482  42.800  206.088 1.00 272.25 ?  6   ALA L CB  1 
ATOM   8158  N N   . PRO D  3 2   ? 90.347  39.966  206.998 1.00 293.35 ?  7   PRO L N   1 
ATOM   8159  C CA  . PRO D  3 2   ? 89.239  39.150  207.509 1.00 282.87 ?  7   PRO L CA  1 
ATOM   8160  C C   . PRO D  3 2   ? 89.711  38.137  208.542 1.00 273.59 ?  7   PRO L C   1 
ATOM   8161  O O   . PRO D  3 2   ? 90.843  37.649  208.497 1.00 281.14 ?  7   PRO L O   1 
ATOM   8162  C CB  . PRO D  3 2   ? 88.711  38.449  206.252 1.00 280.08 ?  7   PRO L CB  1 
ATOM   8163  C CG  . PRO D  3 2   ? 89.912  38.306  205.394 1.00 282.99 ?  7   PRO L CG  1 
ATOM   8164  C CD  . PRO D  3 2   ? 90.736  39.541  205.636 1.00 286.13 ?  7   PRO L CD  1 
ATOM   8165  N N   . THR D  3 3   ? 88.827  37.830  209.494 1.00 262.73 ?  8   THR L N   1 
ATOM   8166  C CA  . THR D  3 3   ? 89.130  36.857  210.535 1.00 263.38 ?  8   THR L CA  1 
ATOM   8167  C C   . THR D  3 3   ? 88.025  35.808  210.597 1.00 265.19 ?  8   THR L C   1 
ATOM   8168  O O   . THR D  3 3   ? 86.884  36.055  210.199 1.00 265.86 ?  8   THR L O   1 
ATOM   8169  C CB  . THR D  3 3   ? 89.271  37.547  211.906 1.00 262.68 ?  8   THR L CB  1 
ATOM   8170  O OG1 . THR D  3 3   ? 88.081  38.296  212.190 1.00 262.99 ?  8   THR L OG1 1 
ATOM   8171  C CG2 . THR D  3 3   ? 90.459  38.498  211.910 1.00 260.89 ?  8   THR L CG2 1 
ATOM   8172  N N   . PHE D  3 4   ? 88.378  34.624  211.108 1.00 266.21 ?  9   PHE L N   1 
ATOM   8173  C CA  . PHE D  3 4   ? 87.449  33.503  211.196 1.00 267.99 ?  9   PHE L CA  1 
ATOM   8174  C C   . PHE D  3 4   ? 87.536  32.799  212.544 1.00 268.59 ?  9   PHE L C   1 
ATOM   8175  O O   . PHE D  3 4   ? 88.622  32.672  213.116 1.00 267.86 ?  9   PHE L O   1 
ATOM   8176  C CB  . PHE D  3 4   ? 87.719  32.492  210.077 1.00 268.69 ?  9   PHE L CB  1 
ATOM   8177  C CG  . PHE D  3 4   ? 87.355  32.989  208.711 1.00 268.50 ?  9   PHE L CG  1 
ATOM   8178  C CD1 . PHE D  3 4   ? 88.264  33.700  207.945 1.00 267.12 ?  9   PHE L CD1 1 
ATOM   8179  C CD2 . PHE D  3 4   ? 86.107  32.720  208.183 1.00 269.73 ?  9   PHE L CD2 1 
ATOM   8180  C CE1 . PHE D  3 4   ? 87.922  34.151  206.684 1.00 266.98 ?  9   PHE L CE1 1 
ATOM   8181  C CE2 . PHE D  3 4   ? 85.760  33.165  206.925 1.00 269.61 ?  9   PHE L CE2 1 
ATOM   8182  C CZ  . PHE D  3 4   ? 86.668  33.881  206.174 1.00 268.24 ?  9   PHE L CZ  1 
ATOM   8183  N N   . VAL D  3 5   ? 86.383  32.349  213.044 1.00 258.56 ?  11  VAL L N   1 
ATOM   8184  C CA  . VAL D  3 5   ? 86.270  31.583  214.287 1.00 271.44 ?  11  VAL L CA  1 
ATOM   8185  C C   . VAL D  3 5   ? 85.303  30.422  214.048 1.00 279.48 ?  11  VAL L C   1 
ATOM   8186  O O   . VAL D  3 5   ? 84.112  30.647  213.805 1.00 277.54 ?  11  VAL L O   1 
ATOM   8187  C CB  . VAL D  3 5   ? 85.820  32.435  215.483 1.00 260.31 ?  11  VAL L CB  1 
ATOM   8188  C CG1 . VAL D  3 5   ? 87.003  33.208  216.048 1.00 245.81 ?  11  VAL L CG1 1 
ATOM   8189  C CG2 . VAL D  3 5   ? 84.711  33.387  215.080 1.00 251.46 ?  11  VAL L CG2 1 
ATOM   8190  N N   . SER D  3 6   ? 85.808  29.188  214.099 1.00 273.68 ?  12  SER L N   1 
ATOM   8191  C CA  . SER D  3 6   ? 84.991  27.994  213.886 1.00 277.65 ?  12  SER L CA  1 
ATOM   8192  C C   . SER D  3 6   ? 84.688  27.363  215.243 1.00 285.56 ?  12  SER L C   1 
ATOM   8193  O O   . SER D  3 6   ? 85.609  27.039  216.000 1.00 286.26 ?  12  SER L O   1 
ATOM   8194  C CB  . SER D  3 6   ? 85.695  26.996  212.965 1.00 278.25 ?  12  SER L CB  1 
ATOM   8195  O OG  . SER D  3 6   ? 86.936  26.572  213.505 1.00 283.91 ?  12  SER L OG  1 
ATOM   8196  N N   . VAL D  3 7   ? 83.397  27.175  215.537 1.00 294.56 ?  13  VAL L N   1 
ATOM   8197  C CA  . VAL D  3 7   ? 82.927  26.622  216.806 1.00 302.99 ?  13  VAL L CA  1 
ATOM   8198  C C   . VAL D  3 7   ? 81.904  25.519  216.552 1.00 315.57 ?  13  VAL L C   1 
ATOM   8199  O O   . VAL D  3 7   ? 80.976  25.696  215.755 1.00 313.48 ?  13  VAL L O   1 
ATOM   8200  C CB  . VAL D  3 7   ? 82.320  27.716  217.706 1.00 287.33 ?  13  VAL L CB  1 
ATOM   8201  C CG1 . VAL D  3 7   ? 81.749  27.107  218.974 1.00 288.59 ?  13  VAL L CG1 1 
ATOM   8202  C CG2 . VAL D  3 7   ? 83.364  28.766  218.046 1.00 277.49 ?  13  VAL L CG2 1 
ATOM   8203  N N   . ALA D  3 8   ? 82.084  24.384  217.229 1.00 302.73 ?  14  ALA L N   1 
ATOM   8204  C CA  . ALA D  3 8   ? 81.169  23.255  217.119 1.00 307.96 ?  14  ALA L CA  1 
ATOM   8205  C C   . ALA D  3 8   ? 79.763  23.623  217.605 1.00 306.89 ?  14  ALA L C   1 
ATOM   8206  O O   . ALA D  3 8   ? 79.601  24.439  218.518 1.00 298.91 ?  14  ALA L O   1 
ATOM   8207  C CB  . ALA D  3 8   ? 81.704  22.064  217.912 1.00 304.41 ?  14  ALA L CB  1 
ATOM   8208  N N   . PRO D  3 9   ? 78.729  23.045  216.988 1.00 301.98 ?  15  PRO L N   1 
ATOM   8209  C CA  . PRO D  3 9   ? 77.343  23.347  217.382 1.00 299.64 ?  15  PRO L CA  1 
ATOM   8210  C C   . PRO D  3 9   ? 77.069  23.046  218.847 1.00 297.76 ?  15  PRO L C   1 
ATOM   8211  O O   . PRO D  3 9   ? 77.450  21.995  219.369 1.00 303.53 ?  15  PRO L O   1 
ATOM   8212  C CB  . PRO D  3 9   ? 76.514  22.440  216.466 1.00 304.47 ?  15  PRO L CB  1 
ATOM   8213  C CG  . PRO D  3 9   ? 77.379  22.210  215.289 1.00 298.99 ?  15  PRO L CG  1 
ATOM   8214  C CD  . PRO D  3 9   ? 78.782  22.150  215.821 1.00 301.15 ?  15  PRO L CD  1 
ATOM   8215  N N   . GLY D  3 10  ? 76.402  23.987  219.513 1.00 288.71 ?  16  GLY L N   1 
ATOM   8216  C CA  . GLY D  3 10  ? 76.056  23.817  220.902 1.00 284.19 ?  16  GLY L CA  1 
ATOM   8217  C C   . GLY D  3 10  ? 77.092  24.348  221.861 1.00 283.00 ?  16  GLY L C   1 
ATOM   8218  O O   . GLY D  3 10  ? 76.817  24.433  223.064 1.00 281.57 ?  16  GLY L O   1 
ATOM   8219  N N   . GLN D  3 11  ? 78.269  24.714  221.359 1.00 288.96 ?  17  GLN L N   1 
ATOM   8220  C CA  . GLN D  3 11  ? 79.368  25.212  222.171 1.00 281.53 ?  17  GLN L CA  1 
ATOM   8221  C C   . GLN D  3 11  ? 79.258  26.722  222.358 1.00 266.43 ?  17  GLN L C   1 
ATOM   8222  O O   . GLN D  3 11  ? 78.154  27.277  222.336 1.00 261.38 ?  17  GLN L O   1 
ATOM   8223  C CB  . GLN D  3 11  ? 80.700  24.832  221.521 1.00 282.25 ?  17  GLN L CB  1 
ATOM   8224  C CG  . GLN D  3 11  ? 80.880  23.325  221.291 1.00 292.13 ?  17  GLN L CG  1 
ATOM   8225  C CD  . GLN D  3 11  ? 80.993  22.515  222.570 1.00 297.46 ?  17  GLN L CD  1 
ATOM   8226  O OE1 . GLN D  3 11  ? 80.043  22.412  223.347 1.00 307.71 ?  17  GLN L OE1 1 
ATOM   8227  N NE2 . GLN D  3 11  ? 82.158  21.918  222.785 1.00 290.07 ?  17  GLN L NE2 1 
ATOM   8228  N N   . THR D  3 12  ? 80.394  27.388  222.552 1.00 262.19 ?  18  THR L N   1 
ATOM   8229  C CA  . THR D  3 12  ? 80.460  28.825  222.796 1.00 260.45 ?  18  THR L CA  1 
ATOM   8230  C C   . THR D  3 12  ? 81.384  29.496  221.790 1.00 258.67 ?  18  THR L C   1 
ATOM   8231  O O   . THR D  3 12  ? 82.516  29.047  221.584 1.00 258.18 ?  18  THR L O   1 
ATOM   8232  C CB  . THR D  3 12  ? 80.932  29.120  224.223 1.00 259.93 ?  18  THR L CB  1 
ATOM   8233  O OG1 . THR D  3 12  ? 80.044  28.491  225.154 1.00 261.62 ?  18  THR L OG1 1 
ATOM   8234  C CG2 . THR D  3 12  ? 80.931  30.614  224.481 1.00 258.18 ?  18  THR L CG2 1 
ATOM   8235  N N   . ALA D  3 13  ? 80.892  30.562  221.164 1.00 274.88 ?  19  ALA L N   1 
ATOM   8236  C CA  . ALA D  3 13  ? 81.638  31.328  220.175 1.00 271.99 ?  19  ALA L CA  1 
ATOM   8237  C C   . ALA D  3 13  ? 82.124  32.620  220.819 1.00 268.67 ?  19  ALA L C   1 
ATOM   8238  O O   . ALA D  3 13  ? 81.425  33.212  221.646 1.00 263.58 ?  19  ALA L O   1 
ATOM   8239  C CB  . ALA D  3 13  ? 80.766  31.643  218.957 1.00 262.57 ?  19  ALA L CB  1 
ATOM   8240  N N   . ARG D  3 14  ? 83.324  33.057  220.432 1.00 269.33 ?  20  ARG L N   1 
ATOM   8241  C CA  . ARG D  3 14  ? 83.927  34.275  220.959 1.00 258.02 ?  20  ARG L CA  1 
ATOM   8242  C C   . ARG D  3 14  ? 84.408  35.136  219.803 1.00 254.23 ?  20  ARG L C   1 
ATOM   8243  O O   . ARG D  3 14  ? 85.073  34.634  218.891 1.00 255.69 ?  20  ARG L O   1 
ATOM   8244  C CB  . ARG D  3 14  ? 85.129  33.924  221.844 1.00 254.24 ?  20  ARG L CB  1 
ATOM   8245  C CG  . ARG D  3 14  ? 84.840  33.002  223.010 1.00 261.34 ?  20  ARG L CG  1 
ATOM   8246  C CD  . ARG D  3 14  ? 84.342  33.733  224.226 1.00 269.72 ?  20  ARG L CD  1 
ATOM   8247  N NE  . ARG D  3 14  ? 84.193  32.809  225.344 1.00 280.63 ?  20  ARG L NE  1 
ATOM   8248  C CZ  . ARG D  3 14  ? 84.204  33.173  226.619 1.00 277.40 ?  20  ARG L CZ  1 
ATOM   8249  N NH1 . ARG D  3 14  ? 84.358  34.450  226.942 1.00 271.10 1  20  ARG L NH1 1 
ATOM   8250  N NH2 . ARG D  3 14  ? 84.063  32.262  227.572 1.00 285.15 ?  20  ARG L NH2 1 
ATOM   8251  N N   . ILE D  3 15  ? 84.074  36.425  219.838 1.00 272.64 ?  21  ILE L N   1 
ATOM   8252  C CA  . ILE D  3 15  ? 84.371  37.340  218.742 1.00 260.90 ?  21  ILE L CA  1 
ATOM   8253  C C   . ILE D  3 15  ? 85.133  38.552  219.257 1.00 247.30 ?  21  ILE L C   1 
ATOM   8254  O O   . ILE D  3 15  ? 84.694  39.205  220.209 1.00 242.04 ?  21  ILE L O   1 
ATOM   8255  C CB  . ILE D  3 15  ? 83.077  37.793  218.039 1.00 252.75 ?  21  ILE L CB  1 
ATOM   8256  C CG1 . ILE D  3 15  ? 82.400  36.591  217.384 1.00 253.30 ?  21  ILE L CG1 1 
ATOM   8257  C CG2 . ILE D  3 15  ? 83.362  38.910  217.039 1.00 239.37 ?  21  ILE L CG2 1 
ATOM   8258  C CD1 . ILE D  3 15  ? 81.061  36.896  216.798 1.00 249.49 ?  21  ILE L CD1 1 
ATOM   8259  N N   . THR D  3 16  ? 86.258  38.863  218.622 1.00 230.75 ?  22  THR L N   1 
ATOM   8260  C CA  . THR D  3 16  ? 87.071  40.016  218.978 1.00 228.78 ?  22  THR L CA  1 
ATOM   8261  C C   . THR D  3 16  ? 86.938  41.013  217.839 1.00 227.57 ?  22  THR L C   1 
ATOM   8262  O O   . THR D  3 16  ? 87.124  40.651  216.673 1.00 228.94 ?  22  THR L O   1 
ATOM   8263  C CB  . THR D  3 16  ? 88.540  39.656  219.210 1.00 227.98 ?  22  THR L CB  1 
ATOM   8264  O OG1 . THR D  3 16  ? 89.079  39.029  218.039 1.00 228.05 ?  22  THR L OG1 1 
ATOM   8265  C CG2 . THR D  3 16  ? 88.681  38.737  220.409 1.00 229.13 ?  22  THR L CG2 1 
ATOM   8266  N N   . CYS D  3 17  ? 86.631  42.261  218.170 1.00 234.50 ?  23  CYS L N   1 
ATOM   8267  C CA  . CYS D  3 17  ? 86.491  43.267  217.134 1.00 232.02 ?  23  CYS L CA  1 
ATOM   8268  C C   . CYS D  3 17  ? 86.972  44.604  217.663 1.00 229.64 ?  23  CYS L C   1 
ATOM   8269  O O   . CYS D  3 17  ? 86.877  44.884  218.860 1.00 224.53 ?  23  CYS L O   1 
ATOM   8270  C CB  . CYS D  3 17  ? 85.022  43.430  216.720 1.00 227.55 ?  23  CYS L CB  1 
ATOM   8271  S SG  . CYS D  3 17  ? 84.665  44.775  215.541 1.00 259.69 ?  23  CYS L SG  1 
ATOM   8272  N N   . GLY D  3 18  ? 87.480  45.432  216.758 1.00 241.45 ?  24  GLY L N   1 
ATOM   8273  C CA  . GLY D  3 18  ? 87.925  46.748  217.156 1.00 230.65 ?  24  GLY L CA  1 
ATOM   8274  C C   . GLY D  3 18  ? 89.230  46.709  217.917 1.00 231.48 ?  24  GLY L C   1 
ATOM   8275  O O   . GLY D  3 18  ? 89.702  45.637  218.299 1.00 240.12 ?  24  GLY L O   1 
ATOM   8276  N N   . GLU D  3 19  ? 89.824  47.876  218.136 1.00 240.56 ?  25  GLU L N   1 
ATOM   8277  C CA  . GLU D  3 19  ? 91.070  47.980  218.876 1.00 238.52 ?  25  GLU L CA  1 
ATOM   8278  C C   . GLU D  3 19  ? 90.808  47.757  220.369 1.00 239.04 ?  25  GLU L C   1 
ATOM   8279  O O   . GLU D  3 19  ? 89.683  47.478  220.797 1.00 239.03 ?  25  GLU L O   1 
ATOM   8280  C CB  . GLU D  3 19  ? 91.699  49.340  218.609 1.00 227.90 ?  25  GLU L CB  1 
ATOM   8281  C CG  . GLU D  3 19  ? 90.850  50.477  219.144 1.00 221.05 ?  25  GLU L CG  1 
ATOM   8282  C CD  . GLU D  3 19  ? 91.517  51.824  219.015 1.00 212.72 ?  25  GLU L CD  1 
ATOM   8283  O OE1 . GLU D  3 19  ? 92.506  51.922  218.261 1.00 214.46 ?  25  GLU L OE1 1 
ATOM   8284  O OE2 . GLU D  3 19  ? 91.049  52.785  219.662 1.00 213.04 -1 25  GLU L OE2 1 
ATOM   8285  N N   . GLU D  3 20  ? 91.861  47.874  221.177 1.00 237.18 ?  26  GLU L N   1 
ATOM   8286  C CA  . GLU D  3 20  ? 91.708  47.740  222.619 1.00 240.37 ?  26  GLU L CA  1 
ATOM   8287  C C   . GLU D  3 20  ? 91.076  48.992  223.216 1.00 230.91 ?  26  GLU L C   1 
ATOM   8288  O O   . GLU D  3 20  ? 91.284  50.112  222.742 1.00 223.62 ?  26  GLU L O   1 
ATOM   8289  C CB  . GLU D  3 20  ? 93.025  47.444  223.341 1.00 242.15 ?  26  GLU L CB  1 
ATOM   8290  C CG  . GLU D  3 20  ? 93.688  46.135  222.975 1.00 246.81 ?  26  GLU L CG  1 
ATOM   8291  C CD  . GLU D  3 20  ? 95.181  46.263  222.805 1.00 255.82 ?  26  GLU L CD  1 
ATOM   8292  O OE1 . GLU D  3 20  ? 95.703  47.389  222.945 1.00 259.69 ?  26  GLU L OE1 1 
ATOM   8293  O OE2 . GLU D  3 20  ? 95.840  45.226  222.577 1.00 261.69 -1 26  GLU L OE2 1 
ATOM   8294  N N   . SER D  3 21  ? 90.291  48.778  224.265 1.00 237.18 ?  27  SER L N   1 
ATOM   8295  C CA  . SER D  3 21  ? 89.592  49.857  224.951 1.00 230.10 ?  27  SER L CA  1 
ATOM   8296  C C   . SER D  3 21  ? 90.565  50.822  225.617 1.00 229.13 ?  27  SER L C   1 
ATOM   8297  O O   . SER D  3 21  ? 91.541  50.412  226.250 1.00 231.08 ?  27  SER L O   1 
ATOM   8298  C CB  . SER D  3 21  ? 88.641  49.287  226.001 1.00 238.50 ?  27  SER L CB  1 
ATOM   8299  O OG  . SER D  3 21  ? 88.231  50.293  226.911 1.00 226.23 ?  27  SER L OG  1 
ATOM   8300  N N   . LEU D  3 22  ? 90.285  52.118  225.458 1.00 228.55 ?  28  LEU L N   1 
ATOM   8301  C CA  . LEU D  3 22  ? 91.065  53.205  226.038 1.00 225.93 ?  28  LEU L CA  1 
ATOM   8302  C C   . LEU D  3 22  ? 90.328  53.902  227.166 1.00 215.86 ?  28  LEU L C   1 
ATOM   8303  O O   . LEU D  3 22  ? 90.967  54.439  228.074 1.00 212.78 ?  28  LEU L O   1 
ATOM   8304  C CB  . LEU D  3 22  ? 91.404  54.254  224.969 1.00 223.16 ?  28  LEU L CB  1 
ATOM   8305  C CG  . LEU D  3 22  ? 92.432  55.331  225.333 1.00 214.76 ?  28  LEU L CG  1 
ATOM   8306  C CD1 . LEU D  3 22  ? 93.724  54.707  225.852 1.00 226.33 ?  28  LEU L CD1 1 
ATOM   8307  C CD2 . LEU D  3 22  ? 92.685  56.267  224.157 1.00 212.83 ?  28  LEU L CD2 1 
ATOM   8308  N N   . GLY D  3 23  ? 89.001  53.897  227.124 1.00 213.79 ?  29  GLY L N   1 
ATOM   8309  C CA  . GLY D  3 23  ? 88.174  54.476  228.159 1.00 208.41 ?  29  GLY L CA  1 
ATOM   8310  C C   . GLY D  3 23  ? 86.911  53.655  228.311 1.00 216.70 ?  29  GLY L C   1 
ATOM   8311  O O   . GLY D  3 23  ? 86.849  52.511  227.850 1.00 226.12 ?  29  GLY L O   1 
ATOM   8312  N N   . SER D  3 24  ? 85.901  54.223  228.958 1.00 217.35 ?  30  SER L N   1 
ATOM   8313  C CA  . SER D  3 24  ? 84.623  53.543  229.098 1.00 217.29 ?  30  SER L CA  1 
ATOM   8314  C C   . SER D  3 24  ? 83.958  53.452  227.732 1.00 211.23 ?  30  SER L C   1 
ATOM   8315  O O   . SER D  3 24  ? 83.786  54.464  227.046 1.00 197.13 ?  30  SER L O   1 
ATOM   8316  C CB  . SER D  3 24  ? 83.727  54.281  230.089 1.00 210.52 ?  30  SER L CB  1 
ATOM   8317  O OG  . SER D  3 24  ? 83.550  55.626  229.692 1.00 212.49 ?  30  SER L OG  1 
ATOM   8318  N N   . ARG D  3 25  ? 83.596  52.244  227.327 1.00 219.00 ?  31  ARG L N   1 
ATOM   8319  C CA  . ARG D  3 25  ? 83.053  52.026  225.998 1.00 212.24 ?  31  ARG L CA  1 
ATOM   8320  C C   . ARG D  3 25  ? 81.562  51.739  226.065 1.00 209.40 ?  31  ARG L C   1 
ATOM   8321  O O   . ARG D  3 25  ? 80.993  51.467  227.125 1.00 211.62 ?  31  ARG L O   1 
ATOM   8322  C CB  . ARG D  3 25  ? 83.756  50.860  225.288 1.00 219.60 ?  31  ARG L CB  1 
ATOM   8323  C CG  . ARG D  3 25  ? 85.137  51.156  224.732 1.00 217.08 ?  31  ARG L CG  1 
ATOM   8324  C CD  . ARG D  3 25  ? 85.652  49.971  223.923 1.00 225.28 ?  31  ARG L CD  1 
ATOM   8325  N NE  . ARG D  3 25  ? 86.858  50.297  223.169 1.00 222.29 ?  31  ARG L NE  1 
ATOM   8326  C CZ  . ARG D  3 25  ? 87.445  49.472  222.306 1.00 237.62 ?  31  ARG L CZ  1 
ATOM   8327  N NH1 . ARG D  3 25  ? 86.934  48.269  222.087 1.00 244.92 1  31  ARG L NH1 1 
ATOM   8328  N NH2 . ARG D  3 25  ? 88.536  49.854  221.657 1.00 241.67 ?  31  ARG L NH2 1 
ATOM   8329  N N   . SER D  3 26  ? 80.938  51.808  224.884 1.00 207.05 ?  32  SER L N   1 
ATOM   8330  C CA  . SER D  3 26  ? 79.550  51.447  224.684 1.00 207.44 ?  32  SER L CA  1 
ATOM   8331  C C   . SER D  3 26  ? 79.530  50.707  223.348 1.00 210.90 ?  32  SER L C   1 
ATOM   8332  O O   . SER D  3 26  ? 79.059  51.198  222.321 1.00 208.82 ?  32  SER L O   1 
ATOM   8333  C CB  . SER D  3 26  ? 78.637  52.678  224.674 1.00 201.54 ?  32  SER L CB  1 
ATOM   8334  O OG  . SER D  3 26  ? 77.274  52.314  224.537 1.00 202.02 ?  32  SER L OG  1 
ATOM   8335  N N   . VAL D  3 27  ? 80.081  49.492  223.368 1.00 212.98 ?  33  VAL L N   1 
ATOM   8336  C CA  . VAL D  3 27  ? 80.239  48.730  222.140 1.00 220.19 ?  33  VAL L CA  1 
ATOM   8337  C C   . VAL D  3 27  ? 78.873  48.261  221.664 1.00 224.59 ?  33  VAL L C   1 
ATOM   8338  O O   . VAL D  3 27  ? 78.119  47.626  222.414 1.00 228.29 ?  33  VAL L O   1 
ATOM   8339  C CB  . VAL D  3 27  ? 81.196  47.549  222.363 1.00 228.24 ?  33  VAL L CB  1 
ATOM   8340  C CG1 . VAL D  3 27  ? 81.436  46.802  221.056 1.00 233.08 ?  33  VAL L CG1 1 
ATOM   8341  C CG2 . VAL D  3 27  ? 82.514  48.035  222.973 1.00 229.56 ?  33  VAL L CG2 1 
ATOM   8342  N N   . ILE D  3 28  ? 78.543  48.580  220.418 1.00 215.79 ?  34  ILE L N   1 
ATOM   8343  C CA  . ILE D  3 28  ? 77.309  48.134  219.787 1.00 217.06 ?  34  ILE L CA  1 
ATOM   8344  C C   . ILE D  3 28  ? 77.678  47.094  218.742 1.00 222.51 ?  34  ILE L C   1 
ATOM   8345  O O   . ILE D  3 28  ? 78.471  47.374  217.833 1.00 222.22 ?  34  ILE L O   1 
ATOM   8346  C CB  . ILE D  3 28  ? 76.516  49.310  219.208 1.00 211.34 ?  34  ILE L CB  1 
ATOM   8347  C CG1 . ILE D  3 28  ? 76.544  50.436  220.241 1.00 206.84 ?  34  ILE L CG1 1 
ATOM   8348  C CG2 . ILE D  3 28  ? 75.088  48.883  218.886 1.00 212.43 ?  34  ILE L CG2 1 
ATOM   8349  C CD1 . ILE D  3 28  ? 75.982  51.716  219.781 1.00 200.68 ?  34  ILE L CD1 1 
ATOM   8350  N N   . TRP D  3 29  ? 77.100  45.906  218.862 1.00 215.64 ?  35  TRP L N   1 
ATOM   8351  C CA  . TRP D  3 29  ? 77.379  44.806  217.956 1.00 222.84 ?  35  TRP L CA  1 
ATOM   8352  C C   . TRP D  3 29  ? 76.269  44.677  216.922 1.00 220.46 ?  35  TRP L C   1 
ATOM   8353  O O   . TRP D  3 29  ? 75.107  44.996  217.187 1.00 217.12 ?  35  TRP L O   1 
ATOM   8354  C CB  . TRP D  3 29  ? 77.513  43.497  218.742 1.00 226.49 ?  35  TRP L CB  1 
ATOM   8355  C CG  . TRP D  3 29  ? 78.721  43.459  219.627 1.00 225.11 ?  35  TRP L CG  1 
ATOM   8356  C CD1 . TRP D  3 29  ? 78.786  43.819  220.943 1.00 221.55 ?  35  TRP L CD1 1 
ATOM   8357  C CD2 . TRP D  3 29  ? 80.033  43.018  219.267 1.00 227.33 ?  35  TRP L CD2 1 
ATOM   8358  N NE1 . TRP D  3 29  ? 80.062  43.644  221.419 1.00 223.86 ?  35  TRP L NE1 1 
ATOM   8359  C CE2 . TRP D  3 29  ? 80.846  43.150  220.409 1.00 228.65 ?  35  TRP L CE2 1 
ATOM   8360  C CE3 . TRP D  3 29  ? 80.600  42.528  218.088 1.00 228.87 ?  35  TRP L CE3 1 
ATOM   8361  C CZ2 . TRP D  3 29  ? 82.195  42.810  220.406 1.00 234.41 ?  35  TRP L CZ2 1 
ATOM   8362  C CZ3 . TRP D  3 29  ? 81.939  42.191  218.088 1.00 232.42 ?  35  TRP L CZ3 1 
ATOM   8363  C CH2 . TRP D  3 29  ? 82.721  42.334  219.237 1.00 236.23 ?  35  TRP L CH2 1 
ATOM   8364  N N   . TYR D  3 30  ? 76.641  44.196  215.739 1.00 230.79 ?  36  TYR L N   1 
ATOM   8365  C CA  . TYR D  3 30  ? 75.703  43.987  214.650 1.00 233.10 ?  36  TYR L CA  1 
ATOM   8366  C C   . TYR D  3 30  ? 76.060  42.671  213.978 1.00 245.21 ?  36  TYR L C   1 
ATOM   8367  O O   . TYR D  3 30  ? 77.229  42.280  213.940 1.00 253.40 ?  36  TYR L O   1 
ATOM   8368  C CB  . TYR D  3 30  ? 75.742  45.147  213.648 1.00 222.22 ?  36  TYR L CB  1 
ATOM   8369  C CG  . TYR D  3 30  ? 75.227  46.443  214.222 1.00 215.15 ?  36  TYR L CG  1 
ATOM   8370  C CD1 . TYR D  3 30  ? 73.867  46.709  214.275 1.00 213.52 ?  36  TYR L CD1 1 
ATOM   8371  C CD2 . TYR D  3 30  ? 76.105  47.403  214.707 1.00 210.26 ?  36  TYR L CD2 1 
ATOM   8372  C CE1 . TYR D  3 30  ? 73.396  47.890  214.798 1.00 207.19 ?  36  TYR L CE1 1 
ATOM   8373  C CE2 . TYR D  3 30  ? 75.646  48.586  215.230 1.00 203.96 ?  36  TYR L CE2 1 
ATOM   8374  C CZ  . TYR D  3 30  ? 74.292  48.826  215.273 1.00 202.43 ?  36  TYR L CZ  1 
ATOM   8375  O OH  . TYR D  3 30  ? 73.845  50.013  215.800 1.00 196.25 ?  36  TYR L OH  1 
ATOM   8376  N N   . GLN D  3 31  ? 75.043  41.988  213.457 1.00 227.40 ?  37  GLN L N   1 
ATOM   8377  C CA  . GLN D  3 31  ? 75.201  40.728  212.740 1.00 234.53 ?  37  GLN L CA  1 
ATOM   8378  C C   . GLN D  3 31  ? 74.689  40.837  211.318 1.00 235.34 ?  37  GLN L C   1 
ATOM   8379  O O   . GLN D  3 31  ? 73.580  41.335  211.093 1.00 232.85 ?  37  GLN L O   1 
ATOM   8380  C CB  . GLN D  3 31  ? 74.418  39.624  213.429 1.00 239.22 ?  37  GLN L CB  1 
ATOM   8381  C CG  . GLN D  3 31  ? 74.485  38.276  212.798 1.00 246.85 ?  37  GLN L CG  1 
ATOM   8382  C CD  . GLN D  3 31  ? 73.541  37.342  213.493 1.00 251.06 ?  37  GLN L CD  1 
ATOM   8383  O OE1 . GLN D  3 31  ? 73.935  36.284  213.973 1.00 251.77 ?  37  GLN L OE1 1 
ATOM   8384  N NE2 . GLN D  3 31  ? 72.267  37.723  213.546 1.00 254.00 ?  37  GLN L NE2 1 
ATOM   8385  N N   . GLN D  3 32  ? 75.480  40.371  210.360 1.00 220.89 ?  38  GLN L N   1 
ATOM   8386  C CA  . GLN D  3 32  ? 75.056  40.435  208.971 1.00 222.41 ?  38  GLN L CA  1 
ATOM   8387  C C   . GLN D  3 32  ? 75.080  39.030  208.382 1.00 230.44 ?  38  GLN L C   1 
ATOM   8388  O O   . GLN D  3 32  ? 76.139  38.509  208.022 1.00 233.68 ?  38  GLN L O   1 
ATOM   8389  C CB  . GLN D  3 32  ? 75.954  41.376  208.179 1.00 219.31 ?  38  GLN L CB  1 
ATOM   8390  C CG  . GLN D  3 32  ? 75.458  41.659  206.782 1.00 219.54 ?  38  GLN L CG  1 
ATOM   8391  C CD  . GLN D  3 32  ? 76.396  42.556  206.006 1.00 220.15 ?  38  GLN L CD  1 
ATOM   8392  O OE1 . GLN D  3 32  ? 77.594  42.614  206.286 1.00 221.21 ?  38  GLN L OE1 1 
ATOM   8393  N NE2 . GLN D  3 32  ? 75.857  43.253  205.013 1.00 219.52 ?  38  GLN L NE2 1 
ATOM   8394  N N   . ARG D  3 33  ? 73.916  38.416  208.308 1.00 243.23 ?  39  ARG L N   1 
ATOM   8395  C CA  . ARG D  3 33  ? 73.792  37.128  207.654 1.00 257.14 ?  39  ARG L CA  1 
ATOM   8396  C C   . ARG D  3 33  ? 74.003  37.339  206.155 1.00 259.02 ?  39  ARG L C   1 
ATOM   8397  O O   . ARG D  3 33  ? 73.574  38.361  205.614 1.00 250.39 ?  39  ARG L O   1 
ATOM   8398  C CB  . ARG D  3 33  ? 72.475  36.457  208.036 1.00 262.65 ?  39  ARG L CB  1 
ATOM   8399  C CG  . ARG D  3 33  ? 72.603  34.946  208.119 1.00 258.50 ?  39  ARG L CG  1 
ATOM   8400  C CD  . ARG D  3 33  ? 73.326  34.544  209.379 1.00 264.96 ?  39  ARG L CD  1 
ATOM   8401  N NE  . ARG D  3 33  ? 72.746  34.817  210.685 1.00 258.69 ?  39  ARG L NE  1 
ATOM   8402  C CZ  . ARG D  3 33  ? 73.331  34.402  211.802 1.00 262.42 ?  39  ARG L CZ  1 
ATOM   8403  N NH1 . ARG D  3 33  ? 74.464  33.730  211.708 1.00 269.01 1  39  ARG L NH1 1 
ATOM   8404  N NH2 . ARG D  3 33  ? 72.800  34.627  212.995 1.00 261.47 ?  39  ARG L NH2 1 
ATOM   8405  N N   . PRO D  3 34  ? 74.663  36.416  205.463 1.00 251.27 ?  40  PRO L N   1 
ATOM   8406  C CA  . PRO D  3 34  ? 74.925  36.620  204.028 1.00 251.99 ?  40  PRO L CA  1 
ATOM   8407  C C   . PRO D  3 34  ? 73.700  36.918  203.172 1.00 243.17 ?  40  PRO L C   1 
ATOM   8408  O O   . PRO D  3 34  ? 72.729  36.155  203.123 1.00 250.78 ?  40  PRO L O   1 
ATOM   8409  C CB  . PRO D  3 34  ? 75.585  35.299  203.605 1.00 262.53 ?  40  PRO L CB  1 
ATOM   8410  C CG  . PRO D  3 34  ? 75.255  34.321  204.686 1.00 260.46 ?  40  PRO L CG  1 
ATOM   8411  C CD  . PRO D  3 34  ? 75.204  35.133  205.938 1.00 250.76 ?  40  PRO L CD  1 
ATOM   8412  N N   . GLY D  3 35  ? 73.771  38.069  202.490 1.00 234.17 ?  41  GLY L N   1 
ATOM   8413  C CA  . GLY D  3 35  ? 72.723  38.562  201.616 1.00 229.20 ?  41  GLY L CA  1 
ATOM   8414  C C   . GLY D  3 35  ? 71.626  39.388  202.259 1.00 223.86 ?  41  GLY L C   1 
ATOM   8415  O O   . GLY D  3 35  ? 70.620  39.663  201.594 1.00 222.99 ?  41  GLY L O   1 
ATOM   8416  N N   . GLN D  3 36  ? 71.787  39.808  203.517 1.00 250.53 ?  42  GLN L N   1 
ATOM   8417  C CA  . GLN D  3 36  ? 70.763  40.581  204.213 1.00 244.79 ?  42  GLN L CA  1 
ATOM   8418  C C   . GLN D  3 36  ? 71.312  41.891  204.769 1.00 227.71 ?  42  GLN L C   1 
ATOM   8419  O O   . GLN D  3 36  ? 72.442  42.285  204.462 1.00 214.93 ?  42  GLN L O   1 
ATOM   8420  C CB  . GLN D  3 36  ? 70.152  39.785  205.364 1.00 253.93 ?  42  GLN L CB  1 
ATOM   8421  C CG  . GLN D  3 36  ? 69.521  38.478  204.974 1.00 259.74 ?  42  GLN L CG  1 
ATOM   8422  C CD  . GLN D  3 36  ? 68.932  37.765  206.168 1.00 265.73 ?  42  GLN L CD  1 
ATOM   8423  O OE1 . GLN D  3 36  ? 68.803  38.344  207.248 1.00 272.46 ?  42  GLN L OE1 1 
ATOM   8424  N NE2 . GLN D  3 36  ? 68.570  36.502  205.985 1.00 272.73 ?  42  GLN L NE2 1 
ATOM   8425  N N   . ALA D  3 37  ? 70.486  42.602  205.597 1.00 246.36 ?  43  ALA L N   1 
ATOM   8426  C CA  . ALA D  3 37  ? 70.869  43.876  206.185 1.00 230.37 ?  43  ALA L CA  1 
ATOM   8427  C C   . ALA D  3 37  ? 71.318  43.694  207.629 1.00 232.77 ?  43  ALA L C   1 
ATOM   8428  O O   . ALA D  3 37  ? 70.826  42.809  208.335 1.00 238.96 ?  43  ALA L O   1 
ATOM   8429  C CB  . ALA D  3 37  ? 69.698  44.863  206.159 1.00 217.57 ?  43  ALA L CB  1 
ATOM   8430  N N   . PRO D  3 38  ? 72.267  44.517  208.076 1.00 230.18 ?  44  PRO L N   1 
ATOM   8431  C CA  . PRO D  3 38  ? 72.740  44.430  209.468 1.00 225.86 ?  44  PRO L CA  1 
ATOM   8432  C C   . PRO D  3 38  ? 71.616  44.589  210.486 1.00 224.13 ?  44  PRO L C   1 
ATOM   8433  O O   . PRO D  3 38  ? 70.778  45.485  210.378 1.00 224.47 ?  44  PRO L O   1 
ATOM   8434  C CB  . PRO D  3 38  ? 73.750  45.579  209.559 1.00 219.20 ?  44  PRO L CB  1 
ATOM   8435  C CG  . PRO D  3 38  ? 74.228  45.763  208.148 1.00 219.82 ?  44  PRO L CG  1 
ATOM   8436  C CD  . PRO D  3 38  ? 73.042  45.484  207.280 1.00 224.05 ?  44  PRO L CD  1 
ATOM   8437  N N   . SER D  3 39  ? 71.596  43.697  211.477 1.00 217.96 ?  45  SER L N   1 
ATOM   8438  C CA  . SER D  3 39  ? 70.593  43.716  212.533 1.00 216.07 ?  45  SER L CA  1 
ATOM   8439  C C   . SER D  3 39  ? 71.234  43.932  213.899 1.00 215.51 ?  45  SER L C   1 
ATOM   8440  O O   . SER D  3 39  ? 72.389  43.566  214.118 1.00 219.57 ?  45  SER L O   1 
ATOM   8441  C CB  . SER D  3 39  ? 69.799  42.410  212.554 1.00 222.13 ?  45  SER L CB  1 
ATOM   8442  O OG  . SER D  3 39  ? 70.658  41.313  212.810 1.00 228.99 ?  45  SER L OG  1 
ATOM   8443  N N   . LEU D  3 40  ? 70.515  44.629  214.780 1.00 220.20 ?  46  LEU L N   1 
ATOM   8444  C CA  . LEU D  3 40  ? 71.004  44.907  216.127 1.00 214.80 ?  46  LEU L CA  1 
ATOM   8445  C C   . LEU D  3 40  ? 70.903  43.686  217.042 1.00 229.18 ?  46  LEU L C   1 
ATOM   8446  O O   . LEU D  3 40  ? 69.847  43.053  217.130 1.00 238.18 ?  46  LEU L O   1 
ATOM   8447  C CB  . LEU D  3 40  ? 70.239  46.074  216.751 1.00 207.19 ?  46  LEU L CB  1 
ATOM   8448  C CG  . LEU D  3 40  ? 70.641  46.418  218.193 1.00 204.01 ?  46  LEU L CG  1 
ATOM   8449  C CD1 . LEU D  3 40  ? 72.101  46.842  218.279 1.00 201.21 ?  46  LEU L CD1 1 
ATOM   8450  C CD2 . LEU D  3 40  ? 69.734  47.493  218.778 1.00 197.59 ?  46  LEU L CD2 1 
ATOM   8451  N N   . ILE D  3 41  ? 72.004  43.357  217.717 1.00 220.81 ?  47  ILE L N   1 
ATOM   8452  C CA  . ILE D  3 41  ? 72.065  42.249  218.679 1.00 221.49 ?  47  ILE L CA  1 
ATOM   8453  C C   . ILE D  3 41  ? 72.284  42.771  220.083 1.00 220.16 ?  47  ILE L C   1 
ATOM   8454  O O   . ILE D  3 41  ? 71.510  42.481  220.995 1.00 219.27 ?  47  ILE L O   1 
ATOM   8455  C CB  . ILE D  3 41  ? 73.131  41.192  218.310 1.00 224.12 ?  47  ILE L CB  1 
ATOM   8456  C CG1 . ILE D  3 41  ? 72.812  40.501  216.996 1.00 226.15 ?  47  ILE L CG1 1 
ATOM   8457  C CG2 . ILE D  3 41  ? 73.271  40.165  219.424 1.00 226.55 ?  47  ILE L CG2 1 
ATOM   8458  C CD1 . ILE D  3 41  ? 73.034  41.325  215.846 1.00 225.61 ?  47  ILE L CD1 1 
ATOM   8459  N N   . ILE D  3 42  ? 73.364  43.509  220.289 1.00 234.49 ?  48  ILE L N   1 
ATOM   8460  C CA  . ILE D  3 42  ? 73.692  44.030  221.602 1.00 226.44 ?  48  ILE L CA  1 
ATOM   8461  C C   . ILE D  3 42  ? 74.152  45.468  221.458 1.00 211.17 ?  48  ILE L C   1 
ATOM   8462  O O   . ILE D  3 42  ? 75.135  45.742  220.762 1.00 211.75 ?  48  ILE L O   1 
ATOM   8463  C CB  . ILE D  3 42  ? 74.794  43.211  222.287 1.00 225.24 ?  48  ILE L CB  1 
ATOM   8464  C CG1 . ILE D  3 42  ? 74.321  41.800  222.634 1.00 233.59 ?  48  ILE L CG1 1 
ATOM   8465  C CG2 . ILE D  3 42  ? 75.325  43.975  223.476 1.00 210.99 ?  48  ILE L CG2 1 
ATOM   8466  C CD1 . ILE D  3 42  ? 75.401  41.024  223.280 1.00 245.90 ?  48  ILE L CD1 1 
ATOM   8467  N N   . TYR D  3 43  ? 73.433  46.383  222.091 1.00 219.95 ?  49  TYR L N   1 
ATOM   8468  C CA  . TYR D  3 43  ? 73.804  47.783  222.162 1.00 213.60 ?  49  TYR L CA  1 
ATOM   8469  C C   . TYR D  3 43  ? 74.239  48.066  223.593 1.00 212.12 ?  49  TYR L C   1 
ATOM   8470  O O   . TYR D  3 43  ? 73.890  47.330  224.514 1.00 215.19 ?  49  TYR L O   1 
ATOM   8471  C CB  . TYR D  3 43  ? 72.637  48.684  221.720 1.00 209.01 ?  49  TYR L CB  1 
ATOM   8472  C CG  . TYR D  3 43  ? 71.431  48.652  222.648 1.00 208.57 ?  49  TYR L CG  1 
ATOM   8473  C CD1 . TYR D  3 43  ? 70.468  47.658  222.513 1.00 212.87 ?  49  TYR L CD1 1 
ATOM   8474  C CD2 . TYR D  3 43  ? 71.247  49.604  223.646 1.00 204.04 ?  49  TYR L CD2 1 
ATOM   8475  C CE1 . TYR D  3 43  ? 69.362  47.600  223.351 1.00 212.70 ?  49  TYR L CE1 1 
ATOM   8476  C CE2 . TYR D  3 43  ? 70.136  49.556  224.491 1.00 203.81 ?  49  TYR L CE2 1 
ATOM   8477  C CZ  . TYR D  3 43  ? 69.199  48.552  224.337 1.00 208.15 ?  49  TYR L CZ  1 
ATOM   8478  O OH  . TYR D  3 43  ? 68.102  48.502  225.173 1.00 208.15 ?  49  TYR L OH  1 
ATOM   8479  N N   . ASN D  3 44  ? 75.041  49.110  223.773 1.00 213.10 ?  50  ASN L N   1 
ATOM   8480  C CA  . ASN D  3 44  ? 75.570  49.454  225.094 1.00 211.66 ?  50  ASN L CA  1 
ATOM   8481  C C   . ASN D  3 44  ? 76.277  48.258  225.744 1.00 217.34 ?  50  ASN L C   1 
ATOM   8482  O O   . ASN D  3 44  ? 75.865  47.748  226.788 1.00 219.37 ?  50  ASN L O   1 
ATOM   8483  C CB  . ASN D  3 44  ? 74.476  50.006  226.012 1.00 208.52 ?  50  ASN L CB  1 
ATOM   8484  C CG  . ASN D  3 44  ? 75.042  50.608  227.289 1.00 206.29 ?  50  ASN L CG  1 
ATOM   8485  O OD1 . ASN D  3 44  ? 76.226  50.939  227.362 1.00 205.56 ?  50  ASN L OD1 1 
ATOM   8486  N ND2 . ASN D  3 44  ? 74.201  50.733  228.308 1.00 205.44 ?  50  ASN L ND2 1 
ATOM   8487  N N   . ASN D  3 45  ? 77.334  47.787  225.077 1.00 213.65 ?  51  ASN L N   1 
ATOM   8488  C CA  . ASN D  3 45  ? 78.177  46.706  225.587 1.00 221.83 ?  51  ASN L CA  1 
ATOM   8489  C C   . ASN D  3 45  ? 77.481  45.362  225.778 1.00 234.81 ?  51  ASN L C   1 
ATOM   8490  O O   . ASN D  3 45  ? 77.917  44.360  225.201 1.00 240.23 ?  51  ASN L O   1 
ATOM   8491  C CB  . ASN D  3 45  ? 78.795  47.145  226.912 1.00 221.45 ?  51  ASN L CB  1 
ATOM   8492  C CG  . ASN D  3 45  ? 79.646  48.379  226.765 1.00 213.99 ?  51  ASN L CG  1 
ATOM   8493  O OD1 . ASN D  3 45  ? 80.371  48.539  225.783 1.00 212.21 ?  51  ASN L OD1 1 
ATOM   8494  N ND2 . ASN D  3 45  ? 79.515  49.296  227.717 1.00 199.99 ?  51  ASN L ND2 1 
ATOM   8495  N N   . ASN D  3 46  ? 76.424  45.305  226.594 1.00 220.90 ?  52  ASN L N   1 
ATOM   8496  C CA  . ASN D  3 46  ? 75.777  44.021  226.859 1.00 227.92 ?  52  ASN L CA  1 
ATOM   8497  C C   . ASN D  3 46  ? 74.278  44.198  227.047 1.00 224.68 ?  52  ASN L C   1 
ATOM   8498  O O   . ASN D  3 46  ? 73.655  43.522  227.872 1.00 234.58 ?  52  ASN L O   1 
ATOM   8499  C CB  . ASN D  3 46  ? 76.380  43.341  228.092 1.00 231.85 ?  52  ASN L CB  1 
ATOM   8500  C CG  . ASN D  3 46  ? 76.160  41.840  228.103 1.00 244.00 ?  52  ASN L CG  1 
ATOM   8501  O OD1 . ASN D  3 46  ? 75.903  41.233  227.069 1.00 252.53 ?  52  ASN L OD1 1 
ATOM   8502  N ND2 . ASN D  3 46  ? 76.254  41.236  229.286 1.00 241.65 ?  52  ASN L ND2 1 
ATOM   8503  N N   . ASP D  3 47  ? 73.679  45.110  226.293 1.00 234.31 ?  53  ASP L N   1 
ATOM   8504  C CA  . ASP D  3 47  ? 72.232  45.325  226.317 1.00 230.11 ?  53  ASP L CA  1 
ATOM   8505  C C   . ASP D  3 47  ? 71.609  44.957  224.976 1.00 228.03 ?  53  ASP L C   1 
ATOM   8506  O O   . ASP D  3 47  ? 71.930  45.566  223.950 1.00 224.60 ?  53  ASP L O   1 
ATOM   8507  C CB  . ASP D  3 47  ? 71.901  46.775  226.669 1.00 221.23 ?  53  ASP L CB  1 
ATOM   8508  C CG  . ASP D  3 47  ? 72.299  47.132  228.081 1.00 214.56 ?  53  ASP L CG  1 
ATOM   8509  O OD1 . ASP D  3 47  ? 72.391  46.225  228.932 1.00 224.74 ?  53  ASP L OD1 1 
ATOM   8510  O OD2 . ASP D  3 47  ? 72.539  48.329  228.326 1.00 211.58 -1 53  ASP L OD2 1 
ATOM   8511  N N   . ARG D  3 48  ? 70.834  44.009  224.976 1.00 218.20 ?  54  ARG L N   1 
ATOM   8512  C CA  . ARG D  3 48  ? 70.108  43.428  223.864 1.00 221.93 ?  54  ARG L CA  1 
ATOM   8513  C C   . ARG D  3 48  ? 68.657  43.922  223.808 1.00 218.70 ?  54  ARG L C   1 
ATOM   8514  O O   . ARG D  3 48  ? 67.965  43.945  224.827 1.00 218.29 ?  54  ARG L O   1 
ATOM   8515  C CB  . ARG D  3 48  ? 70.189  41.907  223.963 1.00 229.08 ?  54  ARG L CB  1 
ATOM   8516  C CG  . ARG D  3 48  ? 71.277  41.513  224.853 1.00 231.16 ?  54  ARG L CG  1 
ATOM   8517  C CD  . ARG D  3 48  ? 71.036  40.063  225.303 1.00 241.76 ?  54  ARG L CD  1 
ATOM   8518  N NE  . ARG D  3 48  ? 69.809  40.156  225.834 1.00 246.67 ?  54  ARG L NE  1 
ATOM   8519  C CZ  . ARG D  3 48  ? 69.137  39.246  226.258 1.00 251.45 ?  54  ARG L CZ  1 
ATOM   8520  N NH1 . ARG D  3 48  ? 69.551  38.141  226.220 1.00 259.43 1  54  ARG L NH1 1 
ATOM   8521  N NH2 . ARG D  3 48  ? 68.010  39.444  226.719 1.00 254.09 ?  54  ARG L NH2 1 
ATOM   8522  N N   . PRO D  3 49  ? 68.213  44.265  222.604 1.00 230.18 ?  55  PRO L N   1 
ATOM   8523  C CA  . PRO D  3 49  ? 66.827  44.698  222.381 1.00 227.87 ?  55  PRO L CA  1 
ATOM   8524  C C   . PRO D  3 49  ? 65.838  43.551  222.397 1.00 233.62 ?  55  PRO L C   1 
ATOM   8525  O O   . PRO D  3 49  ? 66.197  42.409  222.691 1.00 239.11 ?  55  PRO L O   1 
ATOM   8526  C CB  . PRO D  3 49  ? 66.890  45.359  220.999 1.00 225.22 ?  55  PRO L CB  1 
ATOM   8527  C CG  . PRO D  3 49  ? 68.010  44.641  220.307 1.00 229.42 ?  55  PRO L CG  1 
ATOM   8528  C CD  . PRO D  3 49  ? 69.019  44.330  221.374 1.00 230.59 ?  55  PRO L CD  1 
ATOM   8529  N N   . SER D  3 50  ? 64.589  43.851  222.071 1.00 252.59 ?  56  SER L N   1 
ATOM   8530  C CA  . SER D  3 50  ? 63.558  42.825  222.056 1.00 265.91 ?  56  SER L CA  1 
ATOM   8531  C C   . SER D  3 50  ? 63.793  41.921  220.855 1.00 278.71 ?  56  SER L C   1 
ATOM   8532  O O   . SER D  3 50  ? 63.996  42.400  219.734 1.00 274.07 ?  56  SER L O   1 
ATOM   8533  C CB  . SER D  3 50  ? 62.176  43.463  221.990 1.00 256.17 ?  56  SER L CB  1 
ATOM   8534  O OG  . SER D  3 50  ? 62.066  44.300  220.850 1.00 246.35 ?  56  SER L OG  1 
ATOM   8535  N N   . GLY D  3 51  ? 63.775  40.609  221.086 1.00 243.95 ?  57  GLY L N   1 
ATOM   8536  C CA  . GLY D  3 51  ? 63.991  39.678  220.004 1.00 251.06 ?  57  GLY L CA  1 
ATOM   8537  C C   . GLY D  3 51  ? 65.327  38.968  220.059 1.00 258.70 ?  57  GLY L C   1 
ATOM   8538  O O   . GLY D  3 51  ? 65.520  38.002  219.311 1.00 266.47 ?  57  GLY L O   1 
ATOM   8539  N N   . ILE D  3 52  ? 66.255  39.409  220.899 1.00 247.67 ?  58  ILE L N   1 
ATOM   8540  C CA  . ILE D  3 52  ? 67.587  38.817  220.982 1.00 245.03 ?  58  ILE L CA  1 
ATOM   8541  C C   . ILE D  3 52  ? 67.674  37.857  222.167 1.00 247.13 ?  58  ILE L C   1 
ATOM   8542  O O   . ILE D  3 52  ? 67.400  38.265  223.306 1.00 244.42 ?  58  ILE L O   1 
ATOM   8543  C CB  . ILE D  3 52  ? 68.663  39.905  221.094 1.00 237.23 ?  58  ILE L CB  1 
ATOM   8544  C CG1 . ILE D  3 52  ? 68.502  40.924  219.965 1.00 232.89 ?  58  ILE L CG1 1 
ATOM   8545  C CG2 . ILE D  3 52  ? 70.052  39.287  221.080 1.00 240.27 ?  58  ILE L CG2 1 
ATOM   8546  C CD1 . ILE D  3 52  ? 68.632  40.324  218.577 1.00 237.26 ?  58  ILE L CD1 1 
ATOM   8547  N N   . PRO D  3 53  ? 68.049  36.594  221.935 1.00 243.33 ?  59  PRO L N   1 
ATOM   8548  C CA  . PRO D  3 53  ? 68.179  35.577  222.991 1.00 253.33 ?  59  PRO L CA  1 
ATOM   8549  C C   . PRO D  3 53  ? 69.297  35.880  223.979 1.00 251.80 ?  59  PRO L C   1 
ATOM   8550  O O   . PRO D  3 53  ? 70.150  36.746  223.765 1.00 240.69 ?  59  PRO L O   1 
ATOM   8551  C CB  . PRO D  3 53  ? 68.457  34.290  222.211 1.00 255.07 ?  59  PRO L CB  1 
ATOM   8552  C CG  . PRO D  3 53  ? 69.038  34.756  220.924 1.00 250.59 ?  59  PRO L CG  1 
ATOM   8553  C CD  . PRO D  3 53  ? 68.340  36.046  220.605 1.00 241.56 ?  59  PRO L CD  1 
ATOM   8554  N N   . ASP D  3 54  ? 69.289  35.142  225.104 1.00 259.59 ?  60  ASP L N   1 
ATOM   8555  C CA  . ASP D  3 54  ? 70.309  35.380  226.123 1.00 262.73 ?  60  ASP L CA  1 
ATOM   8556  C C   . ASP D  3 54  ? 71.629  34.717  225.771 1.00 267.35 ?  60  ASP L C   1 
ATOM   8557  O O   . ASP D  3 54  ? 72.566  34.767  226.570 1.00 270.12 ?  60  ASP L O   1 
ATOM   8558  C CB  . ASP D  3 54  ? 69.883  34.779  227.476 1.00 272.66 ?  60  ASP L CB  1 
ATOM   8559  C CG  . ASP D  3 54  ? 68.408  34.898  227.736 1.00 265.26 ?  60  ASP L CG  1 
ATOM   8560  O OD1 . ASP D  3 54  ? 67.834  35.934  227.381 1.00 258.87 ?  60  ASP L OD1 1 
ATOM   8561  O OD2 . ASP D  3 54  ? 67.838  33.962  228.357 1.00 265.18 -1 60  ASP L OD2 1 
ATOM   8562  N N   . ARG D  3 55  ? 71.705  34.091  224.589 1.00 263.25 ?  61  ARG L N   1 
ATOM   8563  C CA  . ARG D  3 55  ? 72.934  33.469  224.095 1.00 267.22 ?  61  ARG L CA  1 
ATOM   8564  C C   . ARG D  3 55  ? 73.978  34.504  223.699 1.00 265.42 ?  61  ARG L C   1 
ATOM   8565  O O   . ARG D  3 55  ? 75.182  34.230  223.747 1.00 269.95 ?  61  ARG L O   1 
ATOM   8566  C CB  . ARG D  3 55  ? 72.568  32.548  222.931 1.00 263.95 ?  61  ARG L CB  1 
ATOM   8567  C CG  . ARG D  3 55  ? 71.537  31.504  223.367 1.00 265.36 ?  61  ARG L CG  1 
ATOM   8568  C CD  . ARG D  3 55  ? 71.209  30.446  222.325 1.00 277.08 ?  61  ARG L CD  1 
ATOM   8569  N NE  . ARG D  3 55  ? 70.628  31.010  221.110 1.00 277.56 ?  61  ARG L NE  1 
ATOM   8570  C CZ  . ARG D  3 55  ? 71.257  31.205  219.958 1.00 277.42 ?  61  ARG L CZ  1 
ATOM   8571  N NH1 . ARG D  3 55  ? 72.538  30.883  219.819 1.00 271.79 1  61  ARG L NH1 1 
ATOM   8572  N NH2 . ARG D  3 55  ? 70.587  31.714  218.929 1.00 283.55 ?  61  ARG L NH2 1 
ATOM   8573  N N   . PHE D  3 56  ? 73.529  35.693  223.324 1.00 271.23 ?  62  PHE L N   1 
ATOM   8574  C CA  . PHE D  3 56  ? 74.412  36.769  222.902 1.00 266.20 ?  62  PHE L CA  1 
ATOM   8575  C C   . PHE D  3 56  ? 74.754  37.690  224.065 1.00 259.92 ?  62  PHE L C   1 
ATOM   8576  O O   . PHE D  3 56  ? 73.873  38.364  224.612 1.00 249.89 ?  62  PHE L O   1 
ATOM   8577  C CB  . PHE D  3 56  ? 73.768  37.535  221.753 1.00 250.37 ?  62  PHE L CB  1 
ATOM   8578  C CG  . PHE D  3 56  ? 73.507  36.672  220.569 1.00 262.11 ?  62  PHE L CG  1 
ATOM   8579  C CD1 . PHE D  3 56  ? 72.303  36.006  220.450 1.00 265.40 ?  62  PHE L CD1 1 
ATOM   8580  C CD2 . PHE D  3 56  ? 74.503  36.419  219.643 1.00 266.09 ?  62  PHE L CD2 1 
ATOM   8581  C CE1 . PHE D  3 56  ? 72.057  35.175  219.382 1.00 274.03 ?  62  PHE L CE1 1 
ATOM   8582  C CE2 . PHE D  3 56  ? 74.267  35.579  218.573 1.00 274.67 ?  62  PHE L CE2 1 
ATOM   8583  C CZ  . PHE D  3 56  ? 73.041  34.956  218.443 1.00 280.53 ?  62  PHE L CZ  1 
ATOM   8584  N N   . SER D  3 57  ? 76.033  37.729  224.425 1.00 263.53 ?  63  SER L N   1 
ATOM   8585  C CA  . SER D  3 57  ? 76.517  38.579  225.497 1.00 245.92 ?  63  SER L CA  1 
ATOM   8586  C C   . SER D  3 57  ? 77.731  39.328  224.974 1.00 244.56 ?  63  SER L C   1 
ATOM   8587  O O   . SER D  3 57  ? 78.493  38.817  224.149 1.00 251.85 ?  63  SER L O   1 
ATOM   8588  C CB  . SER D  3 57  ? 76.889  37.784  226.754 1.00 247.07 ?  63  SER L CB  1 
ATOM   8589  O OG  . SER D  3 57  ? 75.855  36.885  227.108 1.00 257.97 ?  63  SER L OG  1 
ATOM   8590  N N   . GLY D  3 58  ? 77.921  40.535  225.486 1.00 243.34 ?  64  GLY L N   1 
ATOM   8591  C CA  . GLY D  3 58  ? 79.034  41.354  225.059 1.00 242.80 ?  64  GLY L CA  1 
ATOM   8592  C C   . GLY D  3 58  ? 79.923  41.767  226.204 1.00 244.01 ?  64  GLY L C   1 
ATOM   8593  O O   . GLY D  3 58  ? 79.473  41.822  227.352 1.00 242.97 ?  64  GLY L O   1 
ATOM   8594  N N   . SER D  3 59  ? 81.183  42.058  225.913 1.00 246.04 ?  65  SER L N   1 
ATOM   8595  C CA  . SER D  3 59  ? 82.076  42.482  226.974 1.00 239.68 ?  65  SER L CA  1 
ATOM   8596  C C   . SER D  3 59  ? 81.647  43.835  227.538 1.00 228.14 ?  65  SER L C   1 
ATOM   8597  O O   . SER D  3 59  ? 81.276  44.742  226.785 1.00 214.60 ?  65  SER L O   1 
ATOM   8598  C CB  . SER D  3 59  ? 83.509  42.574  226.456 1.00 239.76 ?  65  SER L CB  1 
ATOM   8599  O OG  . SER D  3 59  ? 84.296  43.409  227.288 1.00 231.89 ?  65  SER L OG  1 
ATOM   8600  N N   . PRO D  3 60  ? 81.675  43.988  228.860 1.00 238.25 ?  66  PRO L N   1 
ATOM   8601  C CA  . PRO D  3 60  ? 81.281  45.259  229.477 1.00 231.67 ?  66  PRO L CA  1 
ATOM   8602  C C   . PRO D  3 60  ? 82.223  46.380  229.068 1.00 225.89 ?  66  PRO L C   1 
ATOM   8603  O O   . PRO D  3 60  ? 83.431  46.181  228.924 1.00 231.69 ?  66  PRO L O   1 
ATOM   8604  C CB  . PRO D  3 60  ? 81.359  44.963  230.978 1.00 235.29 ?  66  PRO L CB  1 
ATOM   8605  C CG  . PRO D  3 60  ? 82.315  43.823  231.090 1.00 236.85 ?  66  PRO L CG  1 
ATOM   8606  C CD  . PRO D  3 60  ? 82.078  42.989  229.864 1.00 240.42 ?  66  PRO L CD  1 
ATOM   8607  N N   . GLY D  3 61  ? 81.661  47.566  228.874 1.00 214.22 ?  67  GLY L N   1 
ATOM   8608  C CA  . GLY D  3 61  ? 82.484  48.692  228.491 1.00 214.22 ?  67  GLY L CA  1 
ATOM   8609  C C   . GLY D  3 61  ? 83.053  49.383  229.709 1.00 213.44 ?  67  GLY L C   1 
ATOM   8610  O O   . GLY D  3 61  ? 83.138  50.614  229.758 1.00 212.25 ?  67  GLY L O   1 
ATOM   8611  N N   . SER D  3 62  A 83.448  48.587  230.704 1.00 221.15 ?  67  SER L N   1 
ATOM   8612  C CA  . SER D  3 62  A 84.042  49.103  231.924 1.00 224.00 ?  67  SER L CA  1 
ATOM   8613  C C   . SER D  3 62  A 85.455  48.597  232.139 1.00 230.58 ?  67  SER L C   1 
ATOM   8614  O O   . SER D  3 62  A 86.116  49.038  233.087 1.00 224.40 ?  67  SER L O   1 
ATOM   8615  C CB  . SER D  3 62  A 83.192  48.712  233.142 1.00 221.97 ?  67  SER L CB  1 
ATOM   8616  O OG  . SER D  3 62  A 81.823  48.997  232.924 1.00 216.57 ?  67  SER L OG  1 
ATOM   8617  N N   . THR D  3 63  B 85.924  47.674  231.303 1.00 229.98 ?  67  THR L N   1 
ATOM   8618  C CA  . THR D  3 63  B 87.276  47.143  231.388 1.00 238.04 ?  67  THR L CA  1 
ATOM   8619  C C   . THR D  3 63  B 88.185  47.979  230.494 1.00 231.98 ?  67  THR L C   1 
ATOM   8620  O O   . THR D  3 63  B 87.938  48.094  229.288 1.00 226.53 ?  67  THR L O   1 
ATOM   8621  C CB  . THR D  3 63  B 87.301  45.672  230.971 1.00 241.33 ?  67  THR L CB  1 
ATOM   8622  O OG1 . THR D  3 63  B 86.308  44.952  231.710 1.00 246.20 ?  67  THR L OG1 1 
ATOM   8623  C CG2 . THR D  3 63  B 88.653  45.059  231.269 1.00 242.61 ?  67  THR L CG2 1 
ATOM   8624  N N   . PHE D  3 64  C 89.228  48.560  231.077 1.00 235.33 ?  67  PHE L N   1 
ATOM   8625  C CA  . PHE D  3 64  C 90.143  49.434  230.354 1.00 224.31 ?  67  PHE L CA  1 
ATOM   8626  C C   . PHE D  3 64  C 91.363  48.631  229.928 1.00 227.68 ?  67  PHE L C   1 
ATOM   8627  O O   . PHE D  3 64  C 92.091  48.102  230.776 1.00 232.81 ?  67  PHE L O   1 
ATOM   8628  C CB  . PHE D  3 64  C 90.538  50.651  231.188 1.00 222.01 ?  67  PHE L CB  1 
ATOM   8629  C CG  . PHE D  3 64  C 89.364  51.418  231.724 1.00 214.29 ?  67  PHE L CG  1 
ATOM   8630  C CD1 . PHE D  3 64  C 88.229  51.593  230.947 1.00 209.48 ?  67  PHE L CD1 1 
ATOM   8631  C CD2 . PHE D  3 64  C 89.402  51.991  232.983 1.00 208.26 ?  67  PHE L CD2 1 
ATOM   8632  C CE1 . PHE D  3 64  C 87.143  52.305  231.423 1.00 201.13 ?  67  PHE L CE1 1 
ATOM   8633  C CE2 . PHE D  3 64  C 88.319  52.709  233.465 1.00 202.41 ?  67  PHE L CE2 1 
ATOM   8634  C CZ  . PHE D  3 64  C 87.189  52.865  232.683 1.00 196.53 ?  67  PHE L CZ  1 
ATOM   8635  N N   . GLY D  3 65  ? 91.583  48.549  228.625 1.00 222.49 ?  68  GLY L N   1 
ATOM   8636  C CA  . GLY D  3 65  ? 92.712  47.844  228.072 1.00 230.51 ?  68  GLY L CA  1 
ATOM   8637  C C   . GLY D  3 65  ? 92.381  46.517  227.415 1.00 240.40 ?  68  GLY L C   1 
ATOM   8638  O O   . GLY D  3 65  ? 93.293  45.706  227.216 1.00 249.50 ?  68  GLY L O   1 
ATOM   8639  N N   . THR D  3 66  ? 91.117  46.276  227.072 1.00 242.06 ?  69  THR L N   1 
ATOM   8640  C CA  . THR D  3 66  ? 90.678  45.040  226.444 1.00 243.00 ?  69  THR L CA  1 
ATOM   8641  C C   . THR D  3 66  ? 89.896  45.358  225.176 1.00 236.71 ?  69  THR L C   1 
ATOM   8642  O O   . THR D  3 66  ? 89.389  46.467  224.994 1.00 228.45 ?  69  THR L O   1 
ATOM   8643  C CB  . THR D  3 66  ? 89.804  44.202  227.391 1.00 244.01 ?  69  THR L CB  1 
ATOM   8644  O OG1 . THR D  3 66  ? 88.731  45.010  227.891 1.00 242.68 ?  69  THR L OG1 1 
ATOM   8645  C CG2 . THR D  3 66  ? 90.627  43.680  228.562 1.00 239.33 ?  69  THR L CG2 1 
ATOM   8646  N N   . THR D  3 67  ? 89.803  44.368  224.297 1.00 241.53 ?  70  THR L N   1 
ATOM   8647  C CA  . THR D  3 67  ? 89.078  44.524  223.047 1.00 236.67 ?  70  THR L CA  1 
ATOM   8648  C C   . THR D  3 67  ? 87.619  44.134  223.246 1.00 236.99 ?  70  THR L C   1 
ATOM   8649  O O   . THR D  3 67  ? 87.264  43.415  224.184 1.00 242.11 ?  70  THR L O   1 
ATOM   8650  C CB  . THR D  3 67  ? 89.695  43.662  221.942 1.00 235.71 ?  70  THR L CB  1 
ATOM   8651  O OG1 . THR D  3 67  ? 89.685  42.287  222.345 1.00 241.54 ?  70  THR L OG1 1 
ATOM   8652  C CG2 . THR D  3 67  ? 91.126  44.089  221.657 1.00 235.98 ?  70  THR L CG2 1 
ATOM   8653  N N   . ALA D  3 68  ? 86.767  44.627  222.352 1.00 233.87 ?  71  ALA L N   1 
ATOM   8654  C CA  . ALA D  3 68  ? 85.354  44.289  222.424 1.00 233.66 ?  71  ALA L CA  1 
ATOM   8655  C C   . ALA D  3 68  ? 85.177  42.812  222.100 1.00 243.34 ?  71  ALA L C   1 
ATOM   8656  O O   . ALA D  3 68  ? 85.651  42.332  221.066 1.00 248.06 ?  71  ALA L O   1 
ATOM   8657  C CB  . ALA D  3 68  ? 84.558  45.156  221.451 1.00 223.69 ?  71  ALA L CB  1 
ATOM   8658  N N   . THR D  3 69  ? 84.497  42.089  222.989 1.00 228.78 ?  72  THR L N   1 
ATOM   8659  C CA  . THR D  3 69  ? 84.308  40.651  222.850 1.00 233.09 ?  72  THR L CA  1 
ATOM   8660  C C   . THR D  3 69  ? 82.826  40.305  222.868 1.00 237.41 ?  72  THR L C   1 
ATOM   8661  O O   . THR D  3 69  ? 82.094  40.727  223.770 1.00 241.67 ?  72  THR L O   1 
ATOM   8662  C CB  . THR D  3 69  ? 85.040  39.897  223.963 1.00 236.74 ?  72  THR L CB  1 
ATOM   8663  O OG1 . THR D  3 69  ? 86.427  40.254  223.944 1.00 236.45 ?  72  THR L OG1 1 
ATOM   8664  C CG2 . THR D  3 69  ? 84.913  38.392  223.766 1.00 243.67 ?  72  THR L CG2 1 
ATOM   8665  N N   . LEU D  3 70  ? 82.396  39.540  221.865 1.00 242.80 ?  73  LEU L N   1 
ATOM   8666  C CA  . LEU D  3 70  ? 81.023  39.064  221.721 1.00 247.94 ?  73  LEU L CA  1 
ATOM   8667  C C   . LEU D  3 70  ? 80.982  37.563  221.990 1.00 261.19 ?  73  LEU L C   1 
ATOM   8668  O O   . LEU D  3 70  ? 81.557  36.778  221.228 1.00 270.04 ?  73  LEU L O   1 
ATOM   8669  C CB  . LEU D  3 70  ? 80.474  39.381  220.332 1.00 241.70 ?  73  LEU L CB  1 
ATOM   8670  C CG  . LEU D  3 70  ? 79.030  38.934  220.089 1.00 240.40 ?  73  LEU L CG  1 
ATOM   8671  C CD1 . LEU D  3 70  ? 78.083  39.620  221.061 1.00 235.18 ?  73  LEU L CD1 1 
ATOM   8672  C CD2 . LEU D  3 70  ? 78.611  39.200  218.658 1.00 240.44 ?  73  LEU L CD2 1 
ATOM   8673  N N   . THR D  3 71  ? 80.315  37.165  223.070 1.00 245.53 ?  74  THR L N   1 
ATOM   8674  C CA  . THR D  3 71  ? 80.225  35.765  223.466 1.00 252.13 ?  74  THR L CA  1 
ATOM   8675  C C   . THR D  3 71  ? 78.890  35.211  222.985 1.00 254.54 ?  74  THR L C   1 
ATOM   8676  O O   . THR D  3 71  ? 77.838  35.802  223.251 1.00 251.24 ?  74  THR L O   1 
ATOM   8677  C CB  . THR D  3 71  ? 80.337  35.621  224.986 1.00 252.34 ?  74  THR L CB  1 
ATOM   8678  O OG1 . THR D  3 71  ? 81.591  36.149  225.433 1.00 249.64 ?  74  THR L OG1 1 
ATOM   8679  C CG2 . THR D  3 71  ? 80.232  34.169  225.396 1.00 259.14 ?  74  THR L CG2 1 
ATOM   8680  N N   . ILE D  3 72  ? 78.929  34.079  222.285 1.00 263.01 ?  75  ILE L N   1 
ATOM   8681  C CA  . ILE D  3 72  ? 77.720  33.449  221.766 1.00 262.47 ?  75  ILE L CA  1 
ATOM   8682  C C   . ILE D  3 72  ? 77.641  32.036  222.329 1.00 272.61 ?  75  ILE L C   1 
ATOM   8683  O O   . ILE D  3 72  ? 78.313  31.121  221.838 1.00 280.88 ?  75  ILE L O   1 
ATOM   8684  C CB  . ILE D  3 72  ? 77.701  33.425  220.234 1.00 252.53 ?  75  ILE L CB  1 
ATOM   8685  C CG1 . ILE D  3 72  ? 77.905  34.832  219.669 1.00 229.55 ?  75  ILE L CG1 1 
ATOM   8686  C CG2 . ILE D  3 72  ? 76.413  32.797  219.725 1.00 253.22 ?  75  ILE L CG2 1 
ATOM   8687  C CD1 . ILE D  3 72  ? 77.963  34.863  218.166 1.00 228.63 ?  75  ILE L CD1 1 
ATOM   8688  N N   . THR D  3 73  ? 76.824  31.856  223.361 1.00 260.46 ?  76  THR L N   1 
ATOM   8689  C CA  . THR D  3 73  ? 76.619  30.550  223.966 1.00 270.58 ?  76  THR L CA  1 
ATOM   8690  C C   . THR D  3 73  ? 75.586  29.769  223.157 1.00 283.23 ?  76  THR L C   1 
ATOM   8691  O O   . THR D  3 73  ? 74.730  30.355  222.489 1.00 277.76 ?  76  THR L O   1 
ATOM   8692  C CB  . THR D  3 73  ? 76.160  30.692  225.419 1.00 261.38 ?  76  THR L CB  1 
ATOM   8693  O OG1 . THR D  3 73  ? 74.893  31.358  225.457 1.00 257.12 ?  76  THR L OG1 1 
ATOM   8694  C CG2 . THR D  3 73  ? 77.167  31.507  226.228 1.00 247.12 ?  76  THR L CG2 1 
ATOM   8695  N N   . SER D  3 74  ? 75.672  28.440  223.214 1.00 275.22 ?  77  SER L N   1 
ATOM   8696  C CA  . SER D  3 74  ? 74.761  27.561  222.474 1.00 282.32 ?  77  SER L CA  1 
ATOM   8697  C C   . SER D  3 74  ? 74.751  27.906  220.981 1.00 273.80 ?  77  SER L C   1 
ATOM   8698  O O   . SER D  3 74  ? 73.749  28.341  220.410 1.00 271.80 ?  77  SER L O   1 
ATOM   8699  C CB  . SER D  3 74  ? 73.353  27.607  223.076 1.00 281.28 ?  77  SER L CB  1 
ATOM   8700  O OG  . SER D  3 74  ? 72.507  26.626  222.501 1.00 283.58 ?  77  SER L OG  1 
ATOM   8701  N N   . VAL D  3 75  ? 75.913  27.708  220.363 1.00 269.22 ?  78  VAL L N   1 
ATOM   8702  C CA  . VAL D  3 75  ? 76.113  28.033  218.955 1.00 268.56 ?  78  VAL L CA  1 
ATOM   8703  C C   . VAL D  3 75  ? 75.240  27.135  218.089 1.00 273.93 ?  78  VAL L C   1 
ATOM   8704  O O   . VAL D  3 75  ? 75.251  25.905  218.232 1.00 280.65 ?  78  VAL L O   1 
ATOM   8705  C CB  . VAL D  3 75  ? 77.595  27.898  218.578 1.00 270.00 ?  78  VAL L CB  1 
ATOM   8706  C CG1 . VAL D  3 75  ? 77.799  28.317  217.141 1.00 269.61 ?  78  VAL L CG1 1 
ATOM   8707  C CG2 . VAL D  3 75  ? 78.454  28.739  219.508 1.00 264.66 ?  78  VAL L CG2 1 
ATOM   8708  N N   . GLU D  3 76  ? 74.479  27.746  217.184 1.00 269.48 ?  79  GLU L N   1 
ATOM   8709  C CA  . GLU D  3 76  ? 73.608  27.013  216.279 1.00 282.92 ?  79  GLU L CA  1 
ATOM   8710  C C   . GLU D  3 76  ? 73.985  27.280  214.831 1.00 287.07 ?  79  GLU L C   1 
ATOM   8711  O O   . GLU D  3 76  ? 74.750  28.195  214.516 1.00 283.52 ?  79  GLU L O   1 
ATOM   8712  C CB  . GLU D  3 76  ? 72.150  27.475  216.419 1.00 275.75 ?  79  GLU L CB  1 
ATOM   8713  C CG  . GLU D  3 76  ? 71.617  27.764  217.799 1.00 280.26 ?  79  GLU L CG  1 
ATOM   8714  C CD  . GLU D  3 76  ? 70.105  27.927  217.779 1.00 283.25 ?  79  GLU L CD  1 
ATOM   8715  O OE1 . GLU D  3 76  ? 69.523  27.934  216.671 1.00 283.25 ?  79  GLU L OE1 1 
ATOM   8716  O OE2 . GLU D  3 76  ? 69.500  28.071  218.860 1.00 283.52 -1 79  GLU L OE2 1 
ATOM   8717  N N   . ALA D  3 77  ? 73.440  26.438  213.944 1.00 290.41 ?  80  ALA L N   1 
ATOM   8718  C CA  . ALA D  3 77  ? 73.727  26.567  212.519 1.00 285.46 ?  80  ALA L CA  1 
ATOM   8719  C C   . ALA D  3 77  ? 73.210  27.897  211.995 1.00 278.69 ?  80  ALA L C   1 
ATOM   8720  O O   . ALA D  3 77  ? 73.722  28.426  211.001 1.00 273.38 ?  80  ALA L O   1 
ATOM   8721  C CB  . ALA D  3 77  ? 73.118  25.402  211.741 1.00 286.41 ?  80  ALA L CB  1 
ATOM   8722  N N   . GLY D  3 78  ? 72.192  28.444  212.663 1.00 300.89 ?  81  GLY L N   1 
ATOM   8723  C CA  . GLY D  3 78  ? 71.589  29.712  212.307 1.00 282.58 ?  81  GLY L CA  1 
ATOM   8724  C C   . GLY D  3 78  ? 72.486  30.887  212.607 1.00 267.44 ?  81  GLY L C   1 
ATOM   8725  O O   . GLY D  3 78  ? 72.254  31.975  212.081 1.00 248.33 ?  81  GLY L O   1 
ATOM   8726  N N   . ASP D  3 79  ? 73.484  30.687  213.467 1.00 283.96 ?  82  ASP L N   1 
ATOM   8727  C CA  . ASP D  3 79  ? 74.460  31.673  213.923 1.00 275.88 ?  82  ASP L CA  1 
ATOM   8728  C C   . ASP D  3 79  ? 75.605  31.888  212.936 1.00 276.29 ?  82  ASP L C   1 
ATOM   8729  O O   . ASP D  3 79  ? 76.475  32.722  213.202 1.00 272.00 ?  82  ASP L O   1 
ATOM   8730  C CB  . ASP D  3 79  ? 75.031  31.281  215.292 1.00 276.52 ?  82  ASP L CB  1 
ATOM   8731  C CG  . ASP D  3 79  ? 73.968  31.209  216.373 1.00 275.01 ?  82  ASP L CG  1 
ATOM   8732  O OD1 . ASP D  3 79  ? 72.932  31.894  216.236 1.00 270.67 ?  82  ASP L OD1 1 
ATOM   8733  O OD2 . ASP D  3 79  ? 74.169  30.470  217.360 1.00 278.68 -1 82  ASP L OD2 1 
ATOM   8734  N N   . GLU D  3 80  ? 75.619  31.174  211.811 1.00 280.66 ?  83  GLU L N   1 
ATOM   8735  C CA  . GLU D  3 80  ? 76.668  31.269  210.795 1.00 281.98 ?  83  GLU L CA  1 
ATOM   8736  C C   . GLU D  3 80  ? 76.580  32.613  210.073 1.00 267.60 ?  83  GLU L C   1 
ATOM   8737  O O   . GLU D  3 80  ? 75.817  32.770  209.119 1.00 264.36 ?  83  GLU L O   1 
ATOM   8738  C CB  . GLU D  3 80  ? 76.452  30.126  209.806 1.00 291.97 ?  83  GLU L CB  1 
ATOM   8739  C CG  . GLU D  3 80  ? 77.426  29.992  208.663 1.00 292.57 ?  83  GLU L CG  1 
ATOM   8740  C CD  . GLU D  3 80  ? 78.463  28.920  208.919 1.00 297.26 ?  83  GLU L CD  1 
ATOM   8741  O OE1 . GLU D  3 80  ? 78.158  27.949  209.646 1.00 298.86 ?  83  GLU L OE1 1 
ATOM   8742  O OE2 . GLU D  3 80  ? 79.580  29.038  208.378 1.00 290.23 -1 83  GLU L OE2 1 
ATOM   8743  N N   . ALA D  3 81  ? 77.374  33.595  210.510 1.00 267.40 ?  84  ALA L N   1 
ATOM   8744  C CA  . ALA D  3 81  ? 77.346  34.911  209.877 1.00 260.97 ?  84  ALA L CA  1 
ATOM   8745  C C   . ALA D  3 81  ? 78.579  35.716  210.246 1.00 256.77 ?  84  ALA L C   1 
ATOM   8746  O O   . ALA D  3 81  ? 79.496  35.236  210.918 1.00 259.07 ?  84  ALA L O   1 
ATOM   8747  C CB  . ALA D  3 81  ? 76.126  35.715  210.306 1.00 256.04 ?  84  ALA L CB  1 
ATOM   8748  N N   . ASP D  3 82  ? 78.573  36.965  209.783 1.00 246.82 ?  85  ASP L N   1 
ATOM   8749  C CA  . ASP D  3 82  ? 79.583  37.977  210.047 1.00 245.00 ?  85  ASP L CA  1 
ATOM   8750  C C   . ASP D  3 82  ? 79.109  38.857  211.203 1.00 240.98 ?  85  ASP L C   1 
ATOM   8751  O O   . ASP D  3 82  ? 77.912  39.114  211.351 1.00 238.33 ?  85  ASP L O   1 
ATOM   8752  C CB  . ASP D  3 82  ? 79.823  38.838  208.806 1.00 234.93 ?  85  ASP L CB  1 
ATOM   8753  C CG  . ASP D  3 82  ? 80.569  38.099  207.720 1.00 244.23 ?  85  ASP L CG  1 
ATOM   8754  O OD1 . ASP D  3 82  ? 81.350  37.185  208.052 1.00 254.63 ?  85  ASP L OD1 1 
ATOM   8755  O OD2 . ASP D  3 82  ? 80.352  38.417  206.532 1.00 241.41 -1 85  ASP L OD2 1 
ATOM   8756  N N   . TYR D  3 83  ? 80.051  39.318  212.026 1.00 246.79 ?  86  TYR L N   1 
ATOM   8757  C CA  . TYR D  3 83  ? 79.745  40.154  213.187 1.00 240.37 ?  86  TYR L CA  1 
ATOM   8758  C C   . TYR D  3 83  ? 80.635  41.388  213.229 1.00 238.20 ?  86  TYR L C   1 
ATOM   8759  O O   . TYR D  3 83  ? 81.864  41.270  213.251 1.00 240.44 ?  86  TYR L O   1 
ATOM   8760  C CB  . TYR D  3 83  ? 79.833  39.373  214.502 1.00 237.51 ?  86  TYR L CB  1 
ATOM   8761  C CG  . TYR D  3 83  ? 78.773  38.304  214.632 1.00 242.60 ?  86  TYR L CG  1 
ATOM   8762  C CD1 . TYR D  3 83  ? 78.949  37.033  214.105 1.00 250.85 ?  86  TYR L CD1 1 
ATOM   8763  C CD2 . TYR D  3 83  ? 77.585  38.576  215.302 1.00 243.20 ?  86  TYR L CD2 1 
ATOM   8764  C CE1 . TYR D  3 83  ? 77.961  36.064  214.234 1.00 258.04 ?  86  TYR L CE1 1 
ATOM   8765  C CE2 . TYR D  3 83  ? 76.601  37.620  215.440 1.00 253.24 ?  86  TYR L CE2 1 
ATOM   8766  C CZ  . TYR D  3 83  ? 76.789  36.366  214.905 1.00 259.97 ?  86  TYR L CZ  1 
ATOM   8767  O OH  . TYR D  3 83  ? 75.794  35.422  215.047 1.00 270.97 ?  86  TYR L OH  1 
ATOM   8768  N N   . TYR D  3 84  ? 80.009  42.564  213.256 1.00 252.29 ?  87  TYR L N   1 
ATOM   8769  C CA  . TYR D  3 84  ? 80.690  43.846  213.338 1.00 243.74 ?  87  TYR L CA  1 
ATOM   8770  C C   . TYR D  3 84  ? 80.423  44.470  214.702 1.00 240.21 ?  87  TYR L C   1 
ATOM   8771  O O   . TYR D  3 84  ? 79.464  44.121  215.395 1.00 241.01 ?  87  TYR L O   1 
ATOM   8772  C CB  . TYR D  3 84  ? 80.221  44.787  212.218 1.00 230.51 ?  87  TYR L CB  1 
ATOM   8773  C CG  . TYR D  3 84  ? 80.544  44.277  210.833 1.00 230.49 ?  87  TYR L CG  1 
ATOM   8774  C CD1 . TYR D  3 84  ? 81.811  43.815  210.530 1.00 234.85 ?  87  TYR L CD1 1 
ATOM   8775  C CD2 . TYR D  3 84  ? 79.572  44.209  209.844 1.00 228.29 ?  87  TYR L CD2 1 
ATOM   8776  C CE1 . TYR D  3 84  ? 82.120  43.330  209.277 1.00 237.12 ?  87  TYR L CE1 1 
ATOM   8777  C CE2 . TYR D  3 84  ? 79.872  43.719  208.582 1.00 230.75 ?  87  TYR L CE2 1 
ATOM   8778  C CZ  . TYR D  3 84  ? 81.151  43.281  208.307 1.00 235.16 ?  87  TYR L CZ  1 
ATOM   8779  O OH  . TYR D  3 84  ? 81.470  42.795  207.061 1.00 234.76 ?  87  TYR L OH  1 
ATOM   8780  N N   . CYS D  3 85  ? 81.290  45.403  215.085 1.00 232.57 ?  88  CYS L N   1 
ATOM   8781  C CA  . CYS D  3 85  ? 81.158  46.101  216.353 1.00 224.81 ?  88  CYS L CA  1 
ATOM   8782  C C   . CYS D  3 85  ? 81.335  47.598  216.154 1.00 220.22 ?  88  CYS L C   1 
ATOM   8783  O O   . CYS D  3 85  ? 82.111  48.038  215.302 1.00 219.43 ?  88  CYS L O   1 
ATOM   8784  C CB  . CYS D  3 85  ? 82.186  45.607  217.369 1.00 229.28 ?  88  CYS L CB  1 
ATOM   8785  S SG  . CYS D  3 85  ? 83.896  45.995  216.951 1.00 243.87 ?  88  CYS L SG  1 
ATOM   8786  N N   . HIS D  3 86  ? 80.611  48.376  216.953 1.00 221.53 ?  89  HIS L N   1 
ATOM   8787  C CA  . HIS D  3 86  ? 80.691  49.834  216.911 1.00 217.09 ?  89  HIS L CA  1 
ATOM   8788  C C   . HIS D  3 86  ? 81.268  50.342  218.230 1.00 216.05 ?  89  HIS L C   1 
ATOM   8789  O O   . HIS D  3 86  ? 80.556  50.447  219.233 1.00 215.49 ?  89  HIS L O   1 
ATOM   8790  C CB  . HIS D  3 86  ? 79.340  50.481  216.633 1.00 214.34 ?  89  HIS L CB  1 
ATOM   8791  C CG  . HIS D  3 86  ? 79.461  51.891  216.149 1.00 210.19 ?  89  HIS L CG  1 
ATOM   8792  N ND1 . HIS D  3 86  ? 78.375  52.715  215.946 1.00 207.33 ?  89  HIS L ND1 1 
ATOM   8793  C CD2 . HIS D  3 86  ? 80.555  52.628  215.844 1.00 208.55 ?  89  HIS L CD2 1 
ATOM   8794  C CE1 . HIS D  3 86  ? 78.796  53.897  215.532 1.00 204.11 ?  89  HIS L CE1 1 
ATOM   8795  N NE2 . HIS D  3 86  ? 80.115  53.870  215.461 1.00 204.73 ?  89  HIS L NE2 1 
ATOM   8796  N N   . ILE D  3 87  ? 82.565  50.644  218.221 1.00 216.20 ?  90  ILE L N   1 
ATOM   8797  C CA  . ILE D  3 87  ? 83.280  51.057  219.424 1.00 212.80 ?  90  ILE L CA  1 
ATOM   8798  C C   . ILE D  3 87  ? 82.896  52.491  219.774 1.00 206.45 ?  90  ILE L C   1 
ATOM   8799  O O   . ILE D  3 87  ? 83.044  53.403  218.952 1.00 196.43 ?  90  ILE L O   1 
ATOM   8800  C CB  . ILE D  3 87  ? 84.798  50.934  219.227 1.00 218.73 ?  90  ILE L CB  1 
ATOM   8801  C CG1 . ILE D  3 87  ? 85.190  49.497  218.867 1.00 216.59 ?  90  ILE L CG1 1 
ATOM   8802  C CG2 . ILE D  3 87  ? 85.544  51.447  220.450 1.00 223.24 ?  90  ILE L CG2 1 
ATOM   8803  C CD1 . ILE D  3 87  ? 84.818  48.481  219.912 1.00 210.25 ?  90  ILE L CD1 1 
ATOM   8804  N N   . TRP D  3 88  ? 82.393  52.699  220.989 1.00 214.23 ?  91  TRP L N   1 
ATOM   8805  C CA  . TRP D  3 88  ? 82.082  54.041  221.484 1.00 209.57 ?  91  TRP L CA  1 
ATOM   8806  C C   . TRP D  3 88  ? 82.984  54.340  222.673 1.00 213.97 ?  91  TRP L C   1 
ATOM   8807  O O   . TRP D  3 88  ? 82.614  54.098  223.823 1.00 217.85 ?  91  TRP L O   1 
ATOM   8808  C CB  . TRP D  3 88  ? 80.615  54.216  221.881 1.00 203.34 ?  91  TRP L CB  1 
ATOM   8809  C CG  . TRP D  3 88  ? 79.688  54.374  220.744 1.00 206.09 ?  91  TRP L CG  1 
ATOM   8810  C CD1 . TRP D  3 88  ? 79.017  53.399  220.072 1.00 210.52 ?  91  TRP L CD1 1 
ATOM   8811  C CD2 . TRP D  3 88  ? 79.381  55.603  220.089 1.00 199.13 ?  91  TRP L CD2 1 
ATOM   8812  N NE1 . TRP D  3 88  ? 78.271  53.956  219.060 1.00 204.09 ?  91  TRP L NE1 1 
ATOM   8813  C CE2 . TRP D  3 88  ? 78.484  55.310  219.046 1.00 196.78 ?  91  TRP L CE2 1 
ATOM   8814  C CE3 . TRP D  3 88  ? 79.769  56.930  220.294 1.00 193.22 ?  91  TRP L CE3 1 
ATOM   8815  C CZ2 . TRP D  3 88  ? 77.968  56.295  218.210 1.00 190.85 ?  91  TRP L CZ2 1 
ATOM   8816  C CZ3 . TRP D  3 88  ? 79.258  57.903  219.467 1.00 187.18 ?  91  TRP L CZ3 1 
ATOM   8817  C CH2 . TRP D  3 88  ? 78.367  57.584  218.437 1.00 187.79 ?  91  TRP L CH2 1 
ATOM   8818  N N   . ASP D  3 89  ? 84.156  54.900  222.394 1.00 204.13 ?  92  ASP L N   1 
ATOM   8819  C CA  . ASP D  3 89  ? 85.138  55.192  223.425 1.00 207.61 ?  92  ASP L CA  1 
ATOM   8820  C C   . ASP D  3 89  ? 85.058  56.675  223.769 1.00 209.26 ?  92  ASP L C   1 
ATOM   8821  O O   . ASP D  3 89  ? 84.857  57.516  222.886 1.00 202.36 ?  92  ASP L O   1 
ATOM   8822  C CB  . ASP D  3 89  ? 86.537  54.808  222.943 1.00 200.88 ?  92  ASP L CB  1 
ATOM   8823  C CG  . ASP D  3 89  ? 87.489  54.531  224.078 1.00 209.86 ?  92  ASP L CG  1 
ATOM   8824  O OD1 . ASP D  3 89  ? 87.282  55.089  225.175 1.00 214.52 ?  92  ASP L OD1 1 
ATOM   8825  O OD2 . ASP D  3 89  ? 88.433  53.738  223.878 1.00 205.34 -1 92  ASP L OD2 1 
ATOM   8826  N N   . SER D  3 90  ? 85.223  56.992  225.056 1.00 210.44 ?  93  SER L N   1 
ATOM   8827  C CA  . SER D  3 90  ? 85.151  58.371  225.531 1.00 202.61 ?  93  SER L CA  1 
ATOM   8828  C C   . SER D  3 90  ? 86.414  59.190  225.293 1.00 206.69 ?  93  SER L C   1 
ATOM   8829  O O   . SER D  3 90  ? 86.387  60.404  225.518 1.00 202.57 ?  93  SER L O   1 
ATOM   8830  C CB  . SER D  3 90  ? 84.838  58.384  227.028 1.00 192.52 ?  93  SER L CB  1 
ATOM   8831  O OG  . SER D  3 90  ? 85.876  57.751  227.755 1.00 189.96 ?  93  SER L OG  1 
ATOM   8832  N N   . ARG D  3 91  ? 87.504  58.583  224.833 1.00 185.49 ?  94  ARG L N   1 
ATOM   8833  C CA  . ARG D  3 91  ? 88.737  59.313  224.573 1.00 186.11 ?  94  ARG L CA  1 
ATOM   8834  C C   . ARG D  3 91  ? 89.049  59.445  223.097 1.00 186.77 ?  94  ARG L C   1 
ATOM   8835  O O   . ARG D  3 91  ? 89.925  60.235  222.731 1.00 187.15 ?  94  ARG L O   1 
ATOM   8836  C CB  . ARG D  3 91  ? 89.920  58.676  225.303 1.00 187.22 ?  94  ARG L CB  1 
ATOM   8837  C CG  . ARG D  3 91  ? 89.696  58.624  226.788 1.00 186.65 ?  94  ARG L CG  1 
ATOM   8838  C CD  . ARG D  3 91  ? 90.892  58.069  227.488 1.00 187.80 ?  94  ARG L CD  1 
ATOM   8839  N NE  . ARG D  3 91  ? 92.119  58.709  227.029 1.00 188.58 ?  94  ARG L NE  1 
ATOM   8840  C CZ  . ARG D  3 91  ? 93.300  58.540  227.609 1.00 189.57 ?  94  ARG L CZ  1 
ATOM   8841  N NH1 . ARG D  3 91  ? 93.407  57.753  228.669 1.00 189.91 1  94  ARG L NH1 1 
ATOM   8842  N NH2 . ARG D  3 91  ? 94.370  59.165  227.140 1.00 190.28 ?  94  ARG L NH2 1 
ATOM   8843  N N   . ARG D  3 92  ? 88.372  58.715  222.267 1.00 196.32 ?  95  ARG L N   1 
ATOM   8844  C CA  . ARG D  3 92  ? 88.598  58.729  220.843 1.00 193.44 ?  95  ARG L CA  1 
ATOM   8845  C C   . ARG D  3 92  ? 87.394  59.347  220.157 1.00 197.04 ?  95  ARG L C   1 
ATOM   8846  O O   . ARG D  3 92  ? 86.261  59.221  220.619 1.00 193.38 ?  95  ARG L O   1 
ATOM   8847  C CB  . ARG D  3 92  ? 88.869  57.329  220.280 1.00 194.41 ?  95  ARG L CB  1 
ATOM   8848  C CG  . ARG D  3 92  ? 90.101  56.672  220.884 1.00 196.66 ?  95  ARG L CG  1 
ATOM   8849  C CD  . ARG D  3 92  ? 91.370  57.422  220.472 1.00 210.50 ?  95  ARG L CD  1 
ATOM   8850  N NE  . ARG D  3 92  ? 92.600  56.729  220.851 1.00 225.57 ?  95  ARG L NE  1 
ATOM   8851  C CZ  . ARG D  3 92  ? 93.821  57.192  220.597 1.00 237.80 ?  95  ARG L CZ  1 
ATOM   8852  N NH1 . ARG D  3 92  ? 94.894  56.506  220.972 1.00 248.29 1  95  ARG L NH1 1 
ATOM   8853  N NH2 . ARG D  3 92  ? 93.969  58.350  219.971 1.00 232.66 ?  95  ARG L NH2 1 
ATOM   8854  N N   . PRO D  3 93  A 87.622  60.035  219.049 1.00 222.24 ?  95  PRO L N   1 
ATOM   8855  C CA  . PRO D  3 93  A 86.510  60.625  218.293 1.00 217.38 ?  95  PRO L CA  1 
ATOM   8856  C C   . PRO D  3 93  A 85.526  59.565  217.827 1.00 219.27 ?  95  PRO L C   1 
ATOM   8857  O O   . PRO D  3 93  A 85.776  58.359  217.866 1.00 220.53 ?  95  PRO L O   1 
ATOM   8858  C CB  . PRO D  3 93  A 87.214  61.331  217.120 1.00 205.40 ?  95  PRO L CB  1 
ATOM   8859  C CG  . PRO D  3 93  A 88.601  61.605  217.638 1.00 203.34 ?  95  PRO L CG  1 
ATOM   8860  C CD  . PRO D  3 93  A 88.939  60.441  218.507 1.00 212.83 ?  95  PRO L CD  1 
ATOM   8861  N N   . THR D  3 94  B 84.380  60.052  217.378 1.00 221.05 ?  95  THR L N   1 
ATOM   8862  C CA  . THR D  3 94  B 83.321  59.174  216.922 1.00 219.54 ?  95  THR L CA  1 
ATOM   8863  C C   . THR D  3 94  B 83.779  58.347  215.733 1.00 224.35 ?  95  THR L C   1 
ATOM   8864  O O   . THR D  3 94  B 84.148  58.888  214.688 1.00 223.92 ?  95  THR L O   1 
ATOM   8865  C CB  . THR D  3 94  B 82.103  60.017  216.546 1.00 210.05 ?  95  THR L CB  1 
ATOM   8866  O OG1 . THR D  3 94  B 81.731  60.880  217.633 1.00 190.78 ?  95  THR L OG1 1 
ATOM   8867  C CG2 . THR D  3 94  B 80.962  59.161  216.143 1.00 211.00 ?  95  THR L CG2 1 
ATOM   8868  N N   . ASN D  3 95  C 83.771  57.027  215.910 1.00 216.45 ?  95  ASN L N   1 
ATOM   8869  C CA  . ASN D  3 95  C 84.172  56.113  214.856 1.00 217.54 ?  95  ASN L CA  1 
ATOM   8870  C C   . ASN D  3 95  C 83.017  55.957  213.883 1.00 215.58 ?  95  ASN L C   1 
ATOM   8871  O O   . ASN D  3 95  C 81.977  55.385  214.223 1.00 209.42 ?  95  ASN L O   1 
ATOM   8872  C CB  . ASN D  3 95  C 84.596  54.754  215.409 1.00 216.69 ?  95  ASN L CB  1 
ATOM   8873  C CG  . ASN D  3 95  C 85.806  54.830  216.312 1.00 214.28 ?  95  ASN L CG  1 
ATOM   8874  O OD1 . ASN D  3 95  C 86.132  55.881  216.847 1.00 210.62 ?  95  ASN L OD1 1 
ATOM   8875  N ND2 . ASN D  3 95  C 86.496  53.701  216.466 1.00 206.99 ?  95  ASN L ND2 1 
ATOM   8876  N N   . TRP D  3 96  ? 83.216  56.454  212.672 1.00 235.86 ?  96  TRP L N   1 
ATOM   8877  C CA  . TRP D  3 96  ? 82.234  56.401  211.602 1.00 232.12 ?  96  TRP L CA  1 
ATOM   8878  C C   . TRP D  3 96  ? 82.409  55.163  210.745 1.00 230.55 ?  96  TRP L C   1 
ATOM   8879  O O   . TRP D  3 96  ? 81.777  55.048  209.686 1.00 227.40 ?  96  TRP L O   1 
ATOM   8880  C CB  . TRP D  3 96  ? 82.317  57.670  210.747 1.00 225.19 ?  96  TRP L CB  1 
ATOM   8881  C CG  . TRP D  3 96  ? 81.921  58.917  211.484 1.00 225.00 ?  96  TRP L CG  1 
ATOM   8882  C CD1 . TRP D  3 96  ? 82.734  59.751  212.190 1.00 223.31 ?  96  TRP L CD1 1 
ATOM   8883  C CD2 . TRP D  3 96  ? 80.609  59.501  211.534 1.00 225.82 ?  96  TRP L CD2 1 
ATOM   8884  N NE1 . TRP D  3 96  ? 82.006  60.798  212.707 1.00 222.12 ?  96  TRP L NE1 1 
ATOM   8885  C CE2 . TRP D  3 96  ? 80.701  60.671  212.311 1.00 223.78 ?  96  TRP L CE2 1 
ATOM   8886  C CE3 . TRP D  3 96  ? 79.365  59.140  211.003 1.00 226.82 ?  96  TRP L CE3 1 
ATOM   8887  C CZ2 . TRP D  3 96  ? 79.598  61.483  212.574 1.00 224.12 ?  96  TRP L CZ2 1 
ATOM   8888  C CZ3 . TRP D  3 96  ? 78.271  59.948  211.266 1.00 221.21 ?  96  TRP L CZ3 1 
ATOM   8889  C CH2 . TRP D  3 96  ? 78.395  61.105  212.043 1.00 221.97 ?  96  TRP L CH2 1 
ATOM   8890  N N   . VAL D  3 97  ? 83.276  54.249  211.176 1.00 206.45 ?  97  VAL L N   1 
ATOM   8891  C CA  . VAL D  3 97  ? 83.528  52.991  210.493 1.00 209.67 ?  97  VAL L CA  1 
ATOM   8892  C C   . VAL D  3 97  ? 83.540  51.862  211.521 1.00 212.18 ?  97  VAL L C   1 
ATOM   8893  O O   . VAL D  3 97  ? 84.297  51.917  212.499 1.00 212.21 ?  97  VAL L O   1 
ATOM   8894  C CB  . VAL D  3 97  ? 84.866  53.036  209.739 1.00 210.36 ?  97  VAL L CB  1 
ATOM   8895  C CG1 . VAL D  3 97  ? 85.177  51.679  209.170 1.00 213.46 ?  97  VAL L CG1 1 
ATOM   8896  C CG2 . VAL D  3 97  ? 84.867  54.157  208.653 1.00 207.66 ?  97  VAL L CG2 1 
ATOM   8897  N N   . PHE D  3 98  ? 82.693  50.856  211.311 1.00 203.94 ?  98  PHE L N   1 
ATOM   8898  C CA  . PHE D  3 98  ? 82.649  49.717  212.212 1.00 211.73 ?  98  PHE L CA  1 
ATOM   8899  C C   . PHE D  3 98  ? 83.991  48.985  212.202 1.00 214.59 ?  98  PHE L C   1 
ATOM   8900  O O   . PHE D  3 98  ? 84.735  49.024  211.217 1.00 207.17 ?  98  PHE L O   1 
ATOM   8901  C CB  . PHE D  3 98  ? 81.521  48.762  211.813 1.00 216.82 ?  98  PHE L CB  1 
ATOM   8902  C CG  . PHE D  3 98  ? 80.130  49.304  212.060 1.00 219.66 ?  98  PHE L CG  1 
ATOM   8903  C CD1 . PHE D  3 98  ? 79.925  50.452  212.811 1.00 217.13 ?  98  PHE L CD1 1 
ATOM   8904  C CD2 . PHE D  3 98  ? 79.023  48.627  211.572 1.00 223.49 ?  98  PHE L CD2 1 
ATOM   8905  C CE1 . PHE D  3 98  ? 78.646  50.927  213.043 1.00 216.76 ?  98  PHE L CE1 1 
ATOM   8906  C CE2 . PHE D  3 98  ? 77.744  49.094  211.805 1.00 223.39 ?  98  PHE L CE2 1 
ATOM   8907  C CZ  . PHE D  3 98  ? 77.556  50.246  212.542 1.00 219.98 ?  98  PHE L CZ  1 
ATOM   8908  N N   . GLY D  3 99  ? 84.295  48.307  213.314 1.00 213.33 ?  99  GLY L N   1 
ATOM   8909  C CA  . GLY D  3 99  ? 85.525  47.538  213.415 1.00 222.30 ?  99  GLY L CA  1 
ATOM   8910  C C   . GLY D  3 99  ? 85.525  46.344  212.479 1.00 227.32 ?  99  GLY L C   1 
ATOM   8911  O O   . GLY D  3 99  ? 84.481  45.911  211.987 1.00 223.72 ?  99  GLY L O   1 
ATOM   8912  N N   . GLU D  3 100 ? 86.713  45.796  212.214 1.00 223.42 ?  100 GLU L N   1 
ATOM   8913  C CA  . GLU D  3 100 ? 86.794  44.639  211.324 1.00 232.47 ?  100 GLU L CA  1 
ATOM   8914  C C   . GLU D  3 100 ? 86.036  43.437  211.855 1.00 228.46 ?  100 GLU L C   1 
ATOM   8915  O O   . GLU D  3 100 ? 86.269  42.972  212.977 1.00 231.54 ?  100 GLU L O   1 
ATOM   8916  C CB  . GLU D  3 100 ? 88.229  44.213  211.023 1.00 246.37 ?  100 GLU L CB  1 
ATOM   8917  C CG  . GLU D  3 100 ? 89.078  45.170  210.225 1.00 257.54 ?  100 GLU L CG  1 
ATOM   8918  C CD  . GLU D  3 100 ? 90.455  44.594  209.967 1.00 268.55 ?  100 GLU L CD  1 
ATOM   8919  O OE1 . GLU D  3 100 ? 90.669  43.424  210.336 1.00 269.57 ?  100 GLU L OE1 1 
ATOM   8920  O OE2 . GLU D  3 100 ? 91.315  45.287  209.380 1.00 272.60 -1 100 GLU L OE2 1 
ATOM   8921  N N   . GLY D  3 101 ? 85.126  42.947  211.019 1.00 232.05 ?  101 GLY L N   1 
ATOM   8922  C CA  . GLY D  3 101 ? 84.251  41.847  211.381 1.00 234.36 ?  101 GLY L CA  1 
ATOM   8923  C C   . GLY D  3 101 ? 84.965  40.523  211.576 1.00 238.65 ?  101 GLY L C   1 
ATOM   8924  O O   . GLY D  3 101 ? 86.125  40.331  211.204 1.00 240.30 ?  101 GLY L O   1 
ATOM   8925  N N   . THR D  3 102 ? 84.234  39.604  212.208 1.00 242.45 ?  102 THR L N   1 
ATOM   8926  C CA  . THR D  3 102 ? 84.701  38.248  212.473 1.00 246.74 ?  102 THR L CA  1 
ATOM   8927  C C   . THR D  3 102 ? 83.642  37.257  211.991 1.00 248.61 ?  102 THR L C   1 
ATOM   8928  O O   . THR D  3 102 ? 82.478  37.344  212.400 1.00 247.53 ?  102 THR L O   1 
ATOM   8929  C CB  . THR D  3 102 ? 84.970  38.061  213.973 1.00 247.74 ?  102 THR L CB  1 
ATOM   8930  O OG1 . THR D  3 102 ? 85.854  39.092  214.433 1.00 245.49 ?  102 THR L OG1 1 
ATOM   8931  C CG2 . THR D  3 102 ? 85.626  36.725  214.241 1.00 252.37 ?  102 THR L CG2 1 
ATOM   8932  N N   . THR D  3 103 ? 84.042  36.335  211.112 1.00 262.15 ?  103 THR L N   1 
ATOM   8933  C CA  . THR D  3 103 ? 83.139  35.349  210.523 1.00 263.97 ?  103 THR L CA  1 
ATOM   8934  C C   . THR D  3 103 ? 83.021  34.121  211.422 1.00 267.65 ?  103 THR L C   1 
ATOM   8935  O O   . THR D  3 103 ? 84.036  33.528  211.803 1.00 270.50 ?  103 THR L O   1 
ATOM   8936  C CB  . THR D  3 103 ? 83.627  34.929  209.136 1.00 265.27 ?  103 THR L CB  1 
ATOM   8937  O OG1 . THR D  3 103 ? 83.754  36.085  208.301 1.00 262.10 ?  103 THR L OG1 1 
ATOM   8938  C CG2 . THR D  3 103 ? 82.640  33.960  208.501 1.00 267.16 ?  103 THR L CG2 1 
ATOM   8939  N N   . LEU D  3 104 ? 81.787  33.735  211.750 1.00 267.42 ?  104 LEU L N   1 
ATOM   8940  C CA  . LEU D  3 104 ? 81.517  32.560  212.576 1.00 274.74 ?  104 LEU L CA  1 
ATOM   8941  C C   . LEU D  3 104 ? 81.227  31.332  211.714 1.00 286.17 ?  104 LEU L C   1 
ATOM   8942  O O   . LEU D  3 104 ? 80.267  31.326  210.936 1.00 284.18 ?  104 LEU L O   1 
ATOM   8943  C CB  . LEU D  3 104 ? 80.348  32.826  213.525 1.00 266.38 ?  104 LEU L CB  1 
ATOM   8944  C CG  . LEU D  3 104 ? 79.948  31.634  214.398 1.00 268.52 ?  104 LEU L CG  1 
ATOM   8945  C CD1 . LEU D  3 104 ? 81.126  31.161  215.232 1.00 275.69 ?  104 LEU L CD1 1 
ATOM   8946  C CD2 . LEU D  3 104 ? 78.771  31.970  215.296 1.00 269.06 ?  104 LEU L CD2 1 
ATOM   8947  N N   . ILE D  3 105 ? 82.059  30.302  211.857 1.00 285.41 ?  105 ILE L N   1 
ATOM   8948  C CA  . ILE D  3 105 ? 81.938  29.048  211.114 1.00 291.58 ?  105 ILE L CA  1 
ATOM   8949  C C   . ILE D  3 105 ? 81.369  27.980  212.043 1.00 302.59 ?  105 ILE L C   1 
ATOM   8950  O O   . ILE D  3 105 ? 82.004  27.612  213.037 1.00 305.74 ?  105 ILE L O   1 
ATOM   8951  C CB  . ILE D  3 105 ? 83.287  28.610  210.525 1.00 286.77 ?  105 ILE L CB  1 
ATOM   8952  C CG1 . ILE D  3 105 ? 83.828  29.677  209.573 1.00 274.66 ?  105 ILE L CG1 1 
ATOM   8953  C CG2 . ILE D  3 105 ? 83.143  27.279  209.811 1.00 288.30 ?  105 ILE L CG2 1 
ATOM   8954  C CD1 . ILE D  3 105 ? 85.167  29.323  208.964 1.00 272.34 ?  105 ILE L CD1 1 
ATOM   8955  N N   . VAL D  3 106 ? 80.178  27.476  211.736 1.00 295.31 ?  106 VAL L N   1 
ATOM   8956  C CA  . VAL D  3 106 ? 79.557  26.416  212.527 1.00 299.60 ?  106 VAL L CA  1 
ATOM   8957  C C   . VAL D  3 106 ? 80.018  25.071  211.973 1.00 311.65 ?  106 VAL L C   1 
ATOM   8958  O O   . VAL D  3 106 ? 79.610  24.669  210.881 1.00 313.15 ?  106 VAL L O   1 
ATOM   8959  C CB  . VAL D  3 106 ? 78.029  26.526  212.519 1.00 288.09 ?  106 VAL L CB  1 
ATOM   8960  C CG1 . VAL D  3 106 ? 77.428  25.444  213.376 1.00 292.71 ?  106 VAL L CG1 1 
ATOM   8961  C CG2 . VAL D  3 106 ? 77.601  27.875  213.026 1.00 278.57 ?  106 VAL L CG2 1 
ATOM   8962  N N   . LEU D  3 107 ? 80.876  24.377  212.724 1.00 296.56 ?  107 LEU L N   1 
ATOM   8963  C CA  . LEU D  3 107 ? 81.436  23.106  212.283 1.00 305.10 ?  107 LEU L CA  1 
ATOM   8964  C C   . LEU D  3 107 ? 80.355  22.026  212.222 1.00 312.29 ?  107 LEU L C   1 
ATOM   8965  O O   . LEU D  3 107 ? 79.212  22.227  212.643 1.00 311.72 ?  107 LEU L O   1 
ATOM   8966  C CB  . LEU D  3 107 ? 82.549  22.668  213.234 1.00 301.04 ?  107 LEU L CB  1 
ATOM   8967  C CG  . LEU D  3 107 ? 83.820  23.514  213.210 1.00 299.63 ?  107 LEU L CG  1 
ATOM   8968  C CD1 . LEU D  3 107 ? 84.815  23.019  214.247 1.00 299.71 ?  107 LEU L CD1 1 
ATOM   8969  C CD2 . LEU D  3 107 ? 84.433  23.498  211.820 1.00 299.89 ?  107 LEU L CD2 1 
ATOM   8970  N N   . SER D  3 108 ? 80.735  20.858  211.689 1.00 322.88 ?  108 SER L N   1 
ATOM   8971  C CA  . SER D  3 108 ? 79.836  19.705  211.575 1.00 323.68 ?  108 SER L CA  1 
ATOM   8972  C C   . SER D  3 108 ? 78.573  20.077  210.797 1.00 317.15 ?  108 SER L C   1 
ATOM   8973  O O   . SER D  3 108 ? 77.450  19.767  211.203 1.00 314.20 ?  108 SER L O   1 
ATOM   8974  C CB  . SER D  3 108 ? 79.490  19.137  212.956 1.00 324.71 ?  108 SER L CB  1 
ATOM   8975  O OG  . SER D  3 108 ? 78.627  18.017  212.853 1.00 329.75 ?  108 SER L OG  1 
ATOM   8976  N N   . GLN D  3 109 ? 78.767  20.752  209.665 1.00 328.86 ?  109 GLN L N   1 
ATOM   8977  C CA  . GLN D  3 109 ? 77.653  21.096  208.778 1.00 325.78 ?  109 GLN L CA  1 
ATOM   8978  C C   . GLN D  3 109 ? 76.885  19.882  208.221 1.00 330.65 ?  109 GLN L C   1 
ATOM   8979  O O   . GLN D  3 109 ? 75.657  19.884  208.250 1.00 330.60 ?  109 GLN L O   1 
ATOM   8980  C CB  . GLN D  3 109 ? 78.169  21.965  207.626 1.00 317.46 ?  109 GLN L CB  1 
ATOM   8981  C CG  . GLN D  3 109 ? 77.118  22.831  206.959 1.00 307.78 ?  109 GLN L CG  1 
ATOM   8982  C CD  . GLN D  3 109 ? 76.765  24.058  207.781 1.00 305.22 ?  109 GLN L CD  1 
ATOM   8983  O OE1 . GLN D  3 109 ? 77.567  24.530  208.590 1.00 303.75 ?  109 GLN L OE1 1 
ATOM   8984  N NE2 . GLN D  3 109 ? 75.566  24.588  207.570 1.00 299.70 ?  109 GLN L NE2 1 
ATOM   8985  N N   . PRO D  3 110 ? 77.581  18.844  207.712 1.00 324.37 ?  110 PRO L N   1 
ATOM   8986  C CA  . PRO D  3 110 ? 79.003  18.680  207.394 1.00 326.60 ?  110 PRO L CA  1 
ATOM   8987  C C   . PRO D  3 110 ? 79.287  18.580  205.883 1.00 322.21 ?  110 PRO L C   1 
ATOM   8988  O O   . PRO D  3 110 ? 80.203  19.232  205.381 1.00 317.45 ?  110 PRO L O   1 
ATOM   8989  C CB  . PRO D  3 110 ? 79.356  17.372  208.099 1.00 327.54 ?  110 PRO L CB  1 
ATOM   8990  C CG  . PRO D  3 110 ? 78.083  16.569  208.042 1.00 331.15 ?  110 PRO L CG  1 
ATOM   8991  C CD  . PRO D  3 110 ? 76.923  17.537  207.892 1.00 324.52 ?  110 PRO L CD  1 
ATOM   8992  N N   . LYS D  3 111 ? 78.500  17.764  205.180 1.00 316.33 ?  111 LYS L N   1 
ATOM   8993  C CA  . LYS D  3 111 ? 78.622  17.538  203.746 1.00 309.93 ?  111 LYS L CA  1 
ATOM   8994  C C   . LYS D  3 111 ? 77.306  17.816  203.032 1.00 298.43 ?  111 LYS L C   1 
ATOM   8995  O O   . LYS D  3 111 ? 76.228  17.779  203.632 1.00 301.11 ?  111 LYS L O   1 
ATOM   8996  C CB  . LYS D  3 111 ? 79.038  16.097  203.450 1.00 313.54 ?  111 LYS L CB  1 
ATOM   8997  C CG  . LYS D  3 111 ? 79.957  15.514  204.494 1.00 310.66 ?  111 LYS L CG  1 
ATOM   8998  C CD  . LYS D  3 111 ? 79.832  14.006  204.534 1.00 306.49 ?  111 LYS L CD  1 
ATOM   8999  C CE  . LYS D  3 111 ? 80.743  13.408  205.587 1.00 310.34 ?  111 LYS L CE  1 
ATOM   9000  N NZ  . LYS D  3 111 ? 80.616  11.927  205.628 1.00 309.64 1  111 LYS L NZ  1 
ATOM   9001  N N   . ALA D  3 112 ? 77.411  18.112  201.738 1.00 301.16 ?  112 ALA L N   1 
ATOM   9002  C CA  . ALA D  3 112 ? 76.238  18.395  200.918 1.00 294.97 ?  112 ALA L CA  1 
ATOM   9003  C C   . ALA D  3 112 ? 76.557  18.022  199.477 1.00 297.58 ?  112 ALA L C   1 
ATOM   9004  O O   . ALA D  3 112 ? 77.504  18.554  198.890 1.00 298.03 ?  112 ALA L O   1 
ATOM   9005  C CB  . ALA D  3 112 ? 75.822  19.861  201.023 1.00 281.38 ?  112 ALA L CB  1 
ATOM   9006  N N   . ALA D  3 113 ? 75.768  17.111  198.921 1.00 294.95 ?  113 ALA L N   1 
ATOM   9007  C CA  . ALA D  3 113 ? 75.956  16.672  197.540 1.00 293.85 ?  113 ALA L CA  1 
ATOM   9008  C C   . ALA D  3 113 ? 75.483  17.750  196.569 1.00 292.74 ?  113 ALA L C   1 
ATOM   9009  O O   . ALA D  3 113 ? 74.341  18.210  196.676 1.00 283.23 ?  113 ALA L O   1 
ATOM   9010  C CB  . ALA D  3 113 ? 75.202  15.369  197.295 1.00 300.99 ?  113 ALA L CB  1 
ATOM   9011  N N   . PRO D  3 114 ? 76.307  18.163  195.604 1.00 292.83 ?  114 PRO L N   1 
ATOM   9012  C CA  . PRO D  3 114 ? 75.881  19.223  194.675 1.00 282.29 ?  114 PRO L CA  1 
ATOM   9013  C C   . PRO D  3 114 ? 74.742  18.751  193.779 1.00 284.89 ?  114 PRO L C   1 
ATOM   9014  O O   . PRO D  3 114 ? 74.781  17.645  193.236 1.00 287.02 ?  114 PRO L O   1 
ATOM   9015  C CB  . PRO D  3 114 ? 77.149  19.509  193.861 1.00 279.48 ?  114 PRO L CB  1 
ATOM   9016  C CG  . PRO D  3 114 ? 77.933  18.227  193.934 1.00 288.87 ?  114 PRO L CG  1 
ATOM   9017  C CD  . PRO D  3 114 ? 77.664  17.670  195.303 1.00 290.09 ?  114 PRO L CD  1 
ATOM   9018  N N   . SER D  3 115 ? 73.721  19.602  193.630 1.00 280.86 ?  115 SER L N   1 
ATOM   9019  C CA  . SER D  3 115 ? 72.567  19.323  192.770 1.00 275.27 ?  115 SER L CA  1 
ATOM   9020  C C   . SER D  3 115 ? 72.735  20.096  191.463 1.00 274.93 ?  115 SER L C   1 
ATOM   9021  O O   . SER D  3 115 ? 72.345  21.260  191.355 1.00 266.54 ?  115 SER L O   1 
ATOM   9022  C CB  . SER D  3 115 ? 71.274  19.701  193.485 1.00 268.70 ?  115 SER L CB  1 
ATOM   9023  O OG  . SER D  3 115 ? 71.127  18.978  194.696 1.00 278.29 ?  115 SER L OG  1 
ATOM   9024  N N   . VAL D  3 116 ? 73.333  19.439  190.457 1.00 280.88 ?  116 VAL L N   1 
ATOM   9025  C CA  . VAL D  3 116 ? 73.606  20.064  189.165 1.00 281.70 ?  116 VAL L CA  1 
ATOM   9026  C C   . VAL D  3 116 ? 72.420  19.898  188.218 1.00 281.11 ?  116 VAL L C   1 
ATOM   9027  O O   . VAL D  3 116 ? 71.677  18.912  188.274 1.00 281.51 ?  116 VAL L O   1 
ATOM   9028  C CB  . VAL D  3 116 ? 74.909  19.498  188.565 1.00 282.82 ?  116 VAL L CB  1 
ATOM   9029  C CG1 . VAL D  3 116 ? 76.099  19.884  189.443 1.00 283.71 ?  116 VAL L CG1 1 
ATOM   9030  C CG2 . VAL D  3 116 ? 74.813  17.995  188.429 1.00 286.71 ?  116 VAL L CG2 1 
ATOM   9031  N N   . THR D  3 117 ? 72.238  20.890  187.343 1.00 287.35 ?  117 THR L N   1 
ATOM   9032  C CA  . THR D  3 117 ? 71.176  20.892  186.336 1.00 287.80 ?  117 THR L CA  1 
ATOM   9033  C C   . THR D  3 117 ? 71.682  21.611  185.092 1.00 288.20 ?  117 THR L C   1 
ATOM   9034  O O   . THR D  3 117 ? 72.109  22.766  185.187 1.00 286.75 ?  117 THR L O   1 
ATOM   9035  C CB  . THR D  3 117 ? 69.898  21.551  186.859 1.00 280.43 ?  117 THR L CB  1 
ATOM   9036  O OG1 . THR D  3 117 ? 69.523  20.946  188.102 1.00 283.43 ?  117 THR L OG1 1 
ATOM   9037  C CG2 . THR D  3 117 ? 68.764  21.371  185.858 1.00 271.05 ?  117 THR L CG2 1 
ATOM   9038  N N   . LEU D  3 118 ? 71.636  20.947  183.940 1.00 270.76 ?  118 LEU L N   1 
ATOM   9039  C CA  . LEU D  3 118 ? 72.150  21.490  182.684 1.00 275.06 ?  118 LEU L CA  1 
ATOM   9040  C C   . LEU D  3 118 ? 70.998  21.810  181.737 1.00 284.18 ?  118 LEU L C   1 
ATOM   9041  O O   . LEU D  3 118 ? 70.226  20.917  181.368 1.00 292.81 ?  118 LEU L O   1 
ATOM   9042  C CB  . LEU D  3 118 ? 73.114  20.503  182.023 1.00 278.00 ?  118 LEU L CB  1 
ATOM   9043  C CG  . LEU D  3 118 ? 73.778  20.982  180.726 1.00 281.59 ?  118 LEU L CG  1 
ATOM   9044  C CD1 . LEU D  3 118 ? 74.567  22.262  180.932 1.00 280.41 ?  118 LEU L CD1 1 
ATOM   9045  C CD2 . LEU D  3 118 ? 74.649  19.880  180.110 1.00 288.54 ?  118 LEU L CD2 1 
ATOM   9046  N N   . PHE D  3 119 ? 70.882  23.081  181.340 1.00 279.35 ?  119 PHE L N   1 
ATOM   9047  C CA  . PHE D  3 119 ? 69.827  23.494  180.419 1.00 280.55 ?  119 PHE L CA  1 
ATOM   9048  C C   . PHE D  3 119 ? 70.386  23.821  179.043 1.00 281.69 ?  119 PHE L C   1 
ATOM   9049  O O   . PHE D  3 119 ? 71.402  24.520  178.929 1.00 277.73 ?  119 PHE L O   1 
ATOM   9050  C CB  . PHE D  3 119 ? 69.026  24.685  180.959 1.00 273.67 ?  119 PHE L CB  1 
ATOM   9051  C CG  . PHE D  3 119 ? 67.995  24.304  181.983 1.00 271.92 ?  119 PHE L CG  1 
ATOM   9052  C CD1 . PHE D  3 119 ? 66.777  23.776  181.578 1.00 275.28 ?  119 PHE L CD1 1 
ATOM   9053  C CD2 . PHE D  3 119 ? 68.228  24.471  183.334 1.00 262.81 ?  119 PHE L CD2 1 
ATOM   9054  C CE1 . PHE D  3 119 ? 65.813  23.424  182.501 1.00 267.36 ?  119 PHE L CE1 1 
ATOM   9055  C CE2 . PHE D  3 119 ? 67.265  24.118  184.263 1.00 251.63 ?  119 PHE L CE2 1 
ATOM   9056  C CZ  . PHE D  3 119 ? 66.057  23.593  183.844 1.00 251.32 ?  119 PHE L CZ  1 
ATOM   9057  N N   . PRO D  3 120 ? 69.732  23.337  177.991 1.00 267.05 ?  120 PRO L N   1 
ATOM   9058  C CA  . PRO D  3 120 ? 70.142  23.648  176.613 1.00 278.10 ?  120 PRO L CA  1 
ATOM   9059  C C   . PRO D  3 120 ? 69.756  25.058  176.207 1.00 278.87 ?  120 PRO L C   1 
ATOM   9060  O O   . PRO D  3 120 ? 68.910  25.691  176.857 1.00 268.87 ?  120 PRO L O   1 
ATOM   9061  C CB  . PRO D  3 120 ? 69.372  22.609  175.785 1.00 282.13 ?  120 PRO L CB  1 
ATOM   9062  C CG  . PRO D  3 120 ? 68.147  22.348  176.585 1.00 271.92 ?  120 PRO L CG  1 
ATOM   9063  C CD  . PRO D  3 120 ? 68.567  22.435  178.031 1.00 262.30 ?  120 PRO L CD  1 
ATOM   9064  N N   . PRO D  3 121 ? 70.365  25.593  175.144 1.00 268.80 ?  121 PRO L N   1 
ATOM   9065  C CA  . PRO D  3 121 ? 70.007  26.945  174.704 1.00 268.40 ?  121 PRO L CA  1 
ATOM   9066  C C   . PRO D  3 121 ? 68.555  26.969  174.262 1.00 266.80 ?  121 PRO L C   1 
ATOM   9067  O O   . PRO D  3 121 ? 68.049  26.014  173.669 1.00 268.44 ?  121 PRO L O   1 
ATOM   9068  C CB  . PRO D  3 121 ? 70.957  27.204  173.528 1.00 273.80 ?  121 PRO L CB  1 
ATOM   9069  C CG  . PRO D  3 121 ? 71.332  25.856  173.044 1.00 277.15 ?  121 PRO L CG  1 
ATOM   9070  C CD  . PRO D  3 121 ? 71.387  24.993  174.269 1.00 274.19 ?  121 PRO L CD  1 
ATOM   9071  N N   . SER D  3 122 ? 67.882  28.071  174.560 1.00 261.08 ?  122 SER L N   1 
ATOM   9072  C CA  . SER D  3 122 ? 66.476  28.167  174.224 1.00 260.61 ?  122 SER L CA  1 
ATOM   9073  C C   . SER D  3 122 ? 66.274  28.287  172.720 1.00 261.87 ?  122 SER L C   1 
ATOM   9074  O O   . SER D  3 122 ? 67.162  28.693  171.966 1.00 262.97 ?  122 SER L O   1 
ATOM   9075  C CB  . SER D  3 122 ? 65.836  29.373  174.911 1.00 259.35 ?  122 SER L CB  1 
ATOM   9076  O OG  . SER D  3 122 ? 66.368  29.566  176.207 1.00 258.40 ?  122 SER L OG  1 
ATOM   9077  N N   . SER D  3 123 ? 65.073  27.914  172.290 1.00 271.93 ?  123 SER L N   1 
ATOM   9078  C CA  . SER D  3 123 ? 64.742  28.005  170.879 1.00 278.75 ?  123 SER L CA  1 
ATOM   9079  C C   . SER D  3 123 ? 64.620  29.468  170.474 1.00 278.95 ?  123 SER L C   1 
ATOM   9080  O O   . SER D  3 123 ? 64.790  29.805  169.298 1.00 287.11 ?  123 SER L O   1 
ATOM   9081  C CB  . SER D  3 123 ? 63.466  27.216  170.577 1.00 278.13 ?  123 SER L CB  1 
ATOM   9082  O OG  . SER D  3 123 ? 62.314  27.901  171.026 1.00 265.45 ?  123 SER L OG  1 
ATOM   9083  N N   . GLU D  3 124 ? 64.306  30.336  171.444 1.00 284.40 ?  124 GLU L N   1 
ATOM   9084  C CA  . GLU D  3 124 ? 64.127  31.768  171.226 1.00 281.43 ?  124 GLU L CA  1 
ATOM   9085  C C   . GLU D  3 124 ? 65.430  32.539  171.027 1.00 288.18 ?  124 GLU L C   1 
ATOM   9086  O O   . GLU D  3 124 ? 65.435  33.551  170.320 1.00 285.32 ?  124 GLU L O   1 
ATOM   9087  C CB  . GLU D  3 124 ? 63.456  32.357  172.465 1.00 267.97 ?  124 GLU L CB  1 
ATOM   9088  C CG  . GLU D  3 124 ? 63.044  33.799  172.381 1.00 266.59 ?  124 GLU L CG  1 
ATOM   9089  C CD  . GLU D  3 124 ? 62.321  34.245  173.632 1.00 260.79 ?  124 GLU L CD  1 
ATOM   9090  O OE1 . GLU D  3 124 ? 62.649  33.724  174.722 1.00 261.11 ?  124 GLU L OE1 1 
ATOM   9091  O OE2 . GLU D  3 124 ? 61.444  35.123  173.535 1.00 257.93 -1 124 GLU L OE2 1 
ATOM   9092  N N   . GLU D  3 125 ? 66.513  32.139  171.689 1.00 282.00 ?  125 GLU L N   1 
ATOM   9093  C CA  . GLU D  3 125 ? 67.801  32.824  171.557 1.00 289.14 ?  125 GLU L CA  1 
ATOM   9094  C C   . GLU D  3 125 ? 68.551  32.450  170.281 1.00 299.74 ?  125 GLU L C   1 
ATOM   9095  O O   . GLU D  3 125 ? 69.299  33.274  169.746 1.00 308.09 ?  125 GLU L O   1 
ATOM   9096  C CB  . GLU D  3 125 ? 68.714  32.667  172.777 1.00 280.90 ?  125 GLU L CB  1 
ATOM   9097  C CG  . GLU D  3 125 ? 69.714  31.552  172.772 1.00 279.69 ?  125 GLU L CG  1 
ATOM   9098  C CD  . GLU D  3 125 ? 70.554  31.589  174.031 1.00 275.05 ?  125 GLU L CD  1 
ATOM   9099  O OE1 . GLU D  3 125 ? 70.821  32.716  174.505 1.00 274.79 ?  125 GLU L OE1 1 
ATOM   9100  O OE2 . GLU D  3 125 ? 70.973  30.525  174.527 1.00 273.58 -1 125 GLU L OE2 1 
ATOM   9101  N N   . LEU D  3 126 ? 68.359  31.224  169.784 1.00 277.76 ?  126 LEU L N   1 
ATOM   9102  C CA  . LEU D  3 126 ? 69.072  30.744  168.599 1.00 288.57 ?  126 LEU L CA  1 
ATOM   9103  C C   . LEU D  3 126 ? 68.792  31.586  167.354 1.00 303.67 ?  126 LEU L C   1 
ATOM   9104  O O   . LEU D  3 126 ? 69.661  31.692  166.482 1.00 313.53 ?  126 LEU L O   1 
ATOM   9105  C CB  . LEU D  3 126 ? 68.658  29.295  168.345 1.00 278.62 ?  126 LEU L CB  1 
ATOM   9106  C CG  . LEU D  3 126 ? 69.117  28.199  169.319 1.00 262.23 ?  126 LEU L CG  1 
ATOM   9107  C CD1 . LEU D  3 126 ? 68.581  26.838  168.888 1.00 261.94 ?  126 LEU L CD1 1 
ATOM   9108  C CD2 . LEU D  3 126 ? 70.631  28.159  169.495 1.00 269.47 ?  126 LEU L CD2 1 
ATOM   9109  N N   . GLN D  3 127 ? 67.616  32.200  167.249 1.00 302.55 ?  127 GLN L N   1 
ATOM   9110  C CA  . GLN D  3 127 ? 67.308  33.082  166.126 1.00 306.97 ?  127 GLN L CA  1 
ATOM   9111  C C   . GLN D  3 127 ? 68.042  34.406  166.216 1.00 301.82 ?  127 GLN L C   1 
ATOM   9112  O O   . GLN D  3 127 ? 68.112  35.136  165.221 1.00 302.12 ?  127 GLN L O   1 
ATOM   9113  C CB  . GLN D  3 127 ? 65.855  33.438  166.091 1.00 304.78 ?  127 GLN L CB  1 
ATOM   9114  C CG  . GLN D  3 127 ? 65.475  33.760  167.463 1.00 278.45 ?  127 GLN L CG  1 
ATOM   9115  C CD  . GLN D  3 127 ? 64.071  34.125  167.565 1.00 272.91 ?  127 GLN L CD  1 
ATOM   9116  O OE1 . GLN D  3 127 ? 63.405  34.268  166.550 1.00 283.50 ?  127 GLN L OE1 1 
ATOM   9117  N NE2 . GLN D  3 127 ? 63.554  34.141  168.781 1.00 265.22 ?  127 GLN L NE2 1 
ATOM   9118  N N   . ALA D  3 128 ? 68.594  34.728  167.375 1.00 288.72 ?  128 ALA L N   1 
ATOM   9119  C CA  . ALA D  3 128 ? 69.344  35.953  167.528 1.00 287.16 ?  128 ALA L CA  1 
ATOM   9120  C C   . ALA D  3 128 ? 70.806  35.665  167.333 1.00 306.26 ?  128 ALA L C   1 
ATOM   9121  O O   . ALA D  3 128 ? 71.668  36.443  167.759 1.00 310.52 ?  128 ALA L O   1 
ATOM   9122  C CB  . ALA D  3 128 ? 69.084  36.577  168.902 1.00 275.00 ?  128 ALA L CB  1 
ATOM   9123  N N   . ASN D  3 129 ? 71.076  34.534  166.674 1.00 295.29 ?  129 ASN L N   1 
ATOM   9124  C CA  . ASN D  3 129 ? 72.409  34.058  166.352 1.00 302.82 ?  129 ASN L CA  1 
ATOM   9125  C C   . ASN D  3 129 ? 73.246  33.922  167.618 1.00 300.34 ?  129 ASN L C   1 
ATOM   9126  O O   . ASN D  3 129 ? 74.440  34.226  167.636 1.00 305.47 ?  129 ASN L O   1 
ATOM   9127  C CB  . ASN D  3 129 ? 73.065  34.964  165.310 1.00 308.48 ?  129 ASN L CB  1 
ATOM   9128  C CG  . ASN D  3 129 ? 74.204  34.287  164.594 1.00 311.10 ?  129 ASN L CG  1 
ATOM   9129  O OD1 . ASN D  3 129 ? 74.282  33.059  164.559 1.00 311.47 ?  129 ASN L OD1 1 
ATOM   9130  N ND2 . ASN D  3 129 ? 75.063  35.077  163.968 1.00 317.93 ?  129 ASN L ND2 1 
ATOM   9131  N N   . LYS D  3 130 ? 72.604  33.452  168.690 1.00 314.24 ?  130 LYS L N   1 
ATOM   9132  C CA  . LYS D  3 130 ? 73.273  33.278  169.966 1.00 305.65 ?  130 LYS L CA  1 
ATOM   9133  C C   . LYS D  3 130 ? 72.845  31.949  170.572 1.00 296.83 ?  130 LYS L C   1 
ATOM   9134  O O   . LYS D  3 130 ? 71.731  31.471  170.340 1.00 291.15 ?  130 LYS L O   1 
ATOM   9135  C CB  . LYS D  3 130 ? 72.856  34.415  170.911 1.00 288.25 ?  130 LYS L CB  1 
ATOM   9136  C CG  . LYS D  3 130 ? 73.258  35.804  170.442 1.00 292.32 ?  130 LYS L CG  1 
ATOM   9137  C CD  . LYS D  3 130 ? 72.705  36.887  171.354 1.00 271.08 ?  130 LYS L CD  1 
ATOM   9138  C CE  . LYS D  3 130 ? 73.051  38.269  170.825 1.00 273.66 ?  130 LYS L CE  1 
ATOM   9139  N NZ  . LYS D  3 130 ? 72.484  39.344  171.681 1.00 266.55 1  130 LYS L NZ  1 
ATOM   9140  N N   . ALA D  3 131 ? 73.750  31.363  171.355 1.00 299.61 ?  131 ALA L N   1 
ATOM   9141  C CA  . ALA D  3 131 ? 73.536  30.105  172.060 1.00 286.95 ?  131 ALA L CA  1 
ATOM   9142  C C   . ALA D  3 131 ? 74.283  30.142  173.386 1.00 275.48 ?  131 ALA L C   1 
ATOM   9143  O O   . ALA D  3 131 ? 75.376  30.710  173.463 1.00 279.95 ?  131 ALA L O   1 
ATOM   9144  C CB  . ALA D  3 131 ? 73.985  28.900  171.226 1.00 290.48 ?  131 ALA L CB  1 
ATOM   9145  N N   . THR D  3 132 ? 73.701  29.546  174.426 1.00 283.83 ?  132 THR L N   1 
ATOM   9146  C CA  . THR D  3 132 ? 74.342  29.558  175.738 1.00 271.06 ?  132 THR L CA  1 
ATOM   9147  C C   . THR D  3 132 ? 73.894  28.341  176.536 1.00 268.37 ?  132 THR L C   1 
ATOM   9148  O O   . THR D  3 132 ? 72.694  28.139  176.742 1.00 264.96 ?  132 THR L O   1 
ATOM   9149  C CB  . THR D  3 132 ? 74.014  30.845  176.503 1.00 267.38 ?  132 THR L CB  1 
ATOM   9150  O OG1 . THR D  3 132 ? 74.515  31.980  175.784 1.00 270.07 ?  132 THR L OG1 1 
ATOM   9151  C CG2 . THR D  3 132 ? 74.655  30.818  177.877 1.00 265.33 ?  132 THR L CG2 1 
ATOM   9152  N N   . LEU D  3 133 ? 74.865  27.538  176.976 1.00 283.87 ?  133 LEU L N   1 
ATOM   9153  C CA  . LEU D  3 133 ? 74.627  26.376  177.824 1.00 278.74 ?  133 LEU L CA  1 
ATOM   9154  C C   . LEU D  3 133 ? 74.707  26.823  179.282 1.00 268.16 ?  133 LEU L C   1 
ATOM   9155  O O   . LEU D  3 133 ? 75.613  27.572  179.655 1.00 267.35 ?  133 LEU L O   1 
ATOM   9156  C CB  . LEU D  3 133 ? 75.666  25.294  177.527 1.00 293.69 ?  133 LEU L CB  1 
ATOM   9157  C CG  . LEU D  3 133 ? 75.573  24.611  176.157 1.00 303.24 ?  133 LEU L CG  1 
ATOM   9158  C CD1 . LEU D  3 133 ? 76.736  23.653  175.933 1.00 316.29 ?  133 LEU L CD1 1 
ATOM   9159  C CD2 . LEU D  3 133 ? 74.254  23.887  175.999 1.00 282.98 ?  133 LEU L CD2 1 
ATOM   9160  N N   . VAL D  3 134 ? 73.758  26.369  180.104 1.00 291.08 ?  134 VAL L N   1 
ATOM   9161  C CA  . VAL D  3 134 ? 73.667  26.763  181.511 1.00 286.23 ?  134 VAL L CA  1 
ATOM   9162  C C   . VAL D  3 134 ? 73.807  25.553  182.438 1.00 282.44 ?  134 VAL L C   1 
ATOM   9163  O O   . VAL D  3 134 ? 73.088  24.563  182.271 1.00 281.00 ?  134 VAL L O   1 
ATOM   9164  C CB  . VAL D  3 134 ? 72.325  27.473  181.768 1.00 278.63 ?  134 VAL L CB  1 
ATOM   9165  C CG1 . VAL D  3 134 ? 72.307  28.124  183.125 1.00 275.01 ?  134 VAL L CG1 1 
ATOM   9166  C CG2 . VAL D  3 134 ? 72.027  28.469  180.668 1.00 280.31 ?  134 VAL L CG2 1 
ATOM   9167  N N   . CYS D  3 135 ? 74.707  25.639  183.431 1.00 298.08 ?  135 CYS L N   1 
ATOM   9168  C CA  . CYS D  3 135 ? 74.938  24.556  184.403 1.00 300.86 ?  135 CYS L CA  1 
ATOM   9169  C C   . CYS D  3 135 ? 74.710  25.090  185.821 1.00 284.51 ?  135 CYS L C   1 
ATOM   9170  O O   . CYS D  3 135 ? 75.577  25.786  186.361 1.00 280.90 ?  135 CYS L O   1 
ATOM   9171  C CB  . CYS D  3 135 ? 76.359  24.005  184.328 1.00 321.75 ?  135 CYS L CB  1 
ATOM   9172  S SG  . CYS D  3 135 ? 76.685  22.416  185.177 1.00 320.65 ?  135 CYS L SG  1 
ATOM   9173  N N   . LEU D  3 136 ? 73.553  24.801  186.419 1.00 296.10 ?  136 LEU L N   1 
ATOM   9174  C CA  . LEU D  3 136 ? 73.208  25.274  187.764 1.00 287.49 ?  136 LEU L CA  1 
ATOM   9175  C C   . LEU D  3 136 ? 73.674  24.275  188.822 1.00 284.55 ?  136 LEU L C   1 
ATOM   9176  O O   . LEU D  3 136 ? 73.361  23.085  188.729 1.00 283.79 ?  136 LEU L O   1 
ATOM   9177  C CB  . LEU D  3 136 ? 71.710  25.539  187.911 1.00 285.91 ?  136 LEU L CB  1 
ATOM   9178  C CG  . LEU D  3 136 ? 71.101  26.662  187.069 1.00 284.47 ?  136 LEU L CG  1 
ATOM   9179  C CD1 . LEU D  3 136 ? 72.076  27.827  186.998 1.00 282.11 ?  136 LEU L CD1 1 
ATOM   9180  C CD2 . LEU D  3 136 ? 70.695  26.193  185.681 1.00 291.07 ?  136 LEU L CD2 1 
ATOM   9181  N N   . ILE D  3 137 ? 74.411  24.758  189.824 1.00 288.28 ?  137 ILE L N   1 
ATOM   9182  C CA  . ILE D  3 137 ? 74.951  23.934  190.909 1.00 285.67 ?  137 ILE L CA  1 
ATOM   9183  C C   . ILE D  3 137 ? 74.461  24.482  192.244 1.00 278.57 ?  137 ILE L C   1 
ATOM   9184  O O   . ILE D  3 137 ? 74.725  25.645  192.570 1.00 279.42 ?  137 ILE L O   1 
ATOM   9185  C CB  . ILE D  3 137 ? 76.486  23.919  190.897 1.00 291.38 ?  137 ILE L CB  1 
ATOM   9186  C CG1 . ILE D  3 137 ? 77.016  23.779  189.474 1.00 298.50 ?  137 ILE L CG1 1 
ATOM   9187  C CG2 . ILE D  3 137 ? 77.014  22.805  191.792 1.00 287.96 ?  137 ILE L CG2 1 
ATOM   9188  C CD1 . ILE D  3 137 ? 78.499  23.961  189.391 1.00 295.35 ?  137 ILE L CD1 1 
ATOM   9189  N N   . SER D  3 138 ? 73.772  23.645  193.027 1.00 283.93 ?  138 SER L N   1 
ATOM   9190  C CA  . SER D  3 138 ? 73.237  24.082  194.311 1.00 284.62 ?  138 SER L CA  1 
ATOM   9191  C C   . SER D  3 138 ? 73.315  22.966  195.347 1.00 292.63 ?  138 SER L C   1 
ATOM   9192  O O   . SER D  3 138 ? 73.627  21.812  195.037 1.00 294.79 ?  138 SER L O   1 
ATOM   9193  C CB  . SER D  3 138 ? 71.775  24.524  194.173 1.00 277.56 ?  138 SER L CB  1 
ATOM   9194  O OG  . SER D  3 138 ? 70.972  23.447  193.710 1.00 279.87 ?  138 SER L OG  1 
ATOM   9195  N N   . ASP D  3 139 ? 73.018  23.344  196.598 1.00 292.44 ?  139 ASP L N   1 
ATOM   9196  C CA  . ASP D  3 139 ? 72.973  22.432  197.746 1.00 286.20 ?  139 ASP L CA  1 
ATOM   9197  C C   . ASP D  3 139 ? 74.286  21.670  197.949 1.00 290.27 ?  139 ASP L C   1 
ATOM   9198  O O   . ASP D  3 139 ? 74.294  20.460  198.177 1.00 293.88 ?  139 ASP L O   1 
ATOM   9199  C CB  . ASP D  3 139 ? 71.789  21.469  197.623 1.00 279.86 ?  139 ASP L CB  1 
ATOM   9200  C CG  . ASP D  3 139 ? 70.449  22.177  197.741 1.00 272.87 ?  139 ASP L CG  1 
ATOM   9201  O OD1 . ASP D  3 139 ? 70.322  23.093  198.583 1.00 271.60 ?  139 ASP L OD1 1 
ATOM   9202  O OD2 . ASP D  3 139 ? 69.524  21.821  196.983 1.00 260.66 -1 139 ASP L OD2 1 
ATOM   9203  N N   . PHE D  3 140 ? 75.409  22.387  197.890 1.00 289.33 ?  140 PHE L N   1 
ATOM   9204  C CA  . PHE D  3 140 ? 76.709  21.759  198.094 1.00 292.51 ?  140 PHE L CA  1 
ATOM   9205  C C   . PHE D  3 140 ? 77.510  22.486  199.164 1.00 291.07 ?  140 PHE L C   1 
ATOM   9206  O O   . PHE D  3 140 ? 77.509  23.719  199.229 1.00 290.64 ?  140 PHE L O   1 
ATOM   9207  C CB  . PHE D  3 140 ? 77.522  21.708  196.789 1.00 298.26 ?  140 PHE L CB  1 
ATOM   9208  C CG  . PHE D  3 140 ? 77.845  23.062  196.208 1.00 294.61 ?  140 PHE L CG  1 
ATOM   9209  C CD1 . PHE D  3 140 ? 76.957  23.700  195.356 1.00 285.57 ?  140 PHE L CD1 1 
ATOM   9210  C CD2 . PHE D  3 140 ? 79.044  23.690  196.506 1.00 299.41 ?  140 PHE L CD2 1 
ATOM   9211  C CE1 . PHE D  3 140 ? 77.258  24.940  194.817 1.00 284.72 ?  140 PHE L CE1 1 
ATOM   9212  C CE2 . PHE D  3 140 ? 79.348  24.930  195.973 1.00 297.25 ?  140 PHE L CE2 1 
ATOM   9213  C CZ  . PHE D  3 140 ? 78.455  25.554  195.127 1.00 290.00 ?  140 PHE L CZ  1 
ATOM   9214  N N   . TYR D  3 141 ? 78.183  21.709  200.009 1.00 294.95 ?  141 TYR L N   1 
ATOM   9215  C CA  . TYR D  3 141 ? 79.009  22.256  201.076 1.00 301.15 ?  141 TYR L CA  1 
ATOM   9216  C C   . TYR D  3 141 ? 80.298  21.440  201.152 1.00 308.49 ?  141 TYR L C   1 
ATOM   9217  O O   . TYR D  3 141 ? 80.255  20.209  201.117 1.00 309.64 ?  141 TYR L O   1 
ATOM   9218  C CB  . TYR D  3 141 ? 78.265  22.211  202.412 1.00 297.68 ?  141 TYR L CB  1 
ATOM   9219  C CG  . TYR D  3 141 ? 78.959  22.923  203.551 1.00 299.42 ?  141 TYR L CG  1 
ATOM   9220  C CD1 . TYR D  3 141 ? 78.711  24.267  203.795 1.00 294.48 ?  141 TYR L CD1 1 
ATOM   9221  C CD2 . TYR D  3 141 ? 79.896  22.275  204.347 1.00 301.43 ?  141 TYR L CD2 1 
ATOM   9222  C CE1 . TYR D  3 141 ? 79.340  24.936  204.821 1.00 296.95 ?  141 TYR L CE1 1 
ATOM   9223  C CE2 . TYR D  3 141 ? 80.537  22.941  205.379 1.00 299.34 ?  141 TYR L CE2 1 
ATOM   9224  C CZ  . TYR D  3 141 ? 80.253  24.272  205.610 1.00 298.68 ?  141 TYR L CZ  1 
ATOM   9225  O OH  . TYR D  3 141 ? 80.881  24.944  206.633 1.00 299.04 ?  141 TYR L OH  1 
ATOM   9226  N N   . PRO D  3 142 ? 81.452  22.115  201.255 1.00 302.99 ?  142 PRO L N   1 
ATOM   9227  C CA  . PRO D  3 142 ? 81.580  23.575  201.282 1.00 298.91 ?  142 PRO L CA  1 
ATOM   9228  C C   . PRO D  3 142 ? 81.533  24.182  199.881 1.00 292.92 ?  142 PRO L C   1 
ATOM   9229  O O   . PRO D  3 142 ? 81.538  23.452  198.891 1.00 294.41 ?  142 PRO L O   1 
ATOM   9230  C CB  . PRO D  3 142 ? 82.950  23.789  201.923 1.00 303.81 ?  142 PRO L CB  1 
ATOM   9231  C CG  . PRO D  3 142 ? 83.730  22.592  201.509 1.00 310.77 ?  142 PRO L CG  1 
ATOM   9232  C CD  . PRO D  3 142 ? 82.750  21.448  201.466 1.00 308.20 ?  142 PRO L CD  1 
ATOM   9233  N N   . GLY D  3 143 ? 81.496  25.510  199.813 1.00 293.11 ?  143 GLY L N   1 
ATOM   9234  C CA  . GLY D  3 143 ? 81.410  26.218  198.551 1.00 294.57 ?  143 GLY L CA  1 
ATOM   9235  C C   . GLY D  3 143 ? 82.737  26.294  197.832 1.00 304.71 ?  143 GLY L C   1 
ATOM   9236  O O   . GLY D  3 143 ? 83.449  27.299  197.919 1.00 310.74 ?  143 GLY L O   1 
ATOM   9237  N N   . ALA D  3 144 ? 83.073  25.226  197.112 1.00 290.87 ?  144 ALA L N   1 
ATOM   9238  C CA  . ALA D  3 144 ? 84.319  25.177  196.348 1.00 296.53 ?  144 ALA L CA  1 
ATOM   9239  C C   . ALA D  3 144 ? 84.131  24.124  195.251 1.00 296.46 ?  144 ALA L C   1 
ATOM   9240  O O   . ALA D  3 144 ? 84.387  22.939  195.467 1.00 296.50 ?  144 ALA L O   1 
ATOM   9241  C CB  . ALA D  3 144 ? 85.509  24.859  197.230 1.00 297.62 ?  144 ALA L CB  1 
ATOM   9242  N N   . VAL D  3 145 ? 83.675  24.576  194.084 1.00 297.36 ?  145 VAL L N   1 
ATOM   9243  C CA  . VAL D  3 145 ? 83.404  23.692  192.959 1.00 307.14 ?  145 VAL L CA  1 
ATOM   9244  C C   . VAL D  3 145 ? 84.186  24.181  191.751 1.00 319.66 ?  145 VAL L C   1 
ATOM   9245  O O   . VAL D  3 145 ? 84.531  25.361  191.637 1.00 322.11 ?  145 VAL L O   1 
ATOM   9246  C CB  . VAL D  3 145 ? 81.899  23.622  192.622 1.00 300.42 ?  145 VAL L CB  1 
ATOM   9247  C CG1 . VAL D  3 145 ? 81.139  22.964  193.747 1.00 288.77 ?  145 VAL L CG1 1 
ATOM   9248  C CG2 . VAL D  3 145 ? 81.349  25.013  192.333 1.00 294.29 ?  145 VAL L CG2 1 
ATOM   9249  N N   . THR D  3 146 ? 84.472  23.245  190.849 1.00 298.85 ?  146 THR L N   1 
ATOM   9250  C CA  . THR D  3 146 ? 85.159  23.520  189.597 1.00 305.60 ?  146 THR L CA  1 
ATOM   9251  C C   . THR D  3 146 ? 84.357  22.901  188.463 1.00 307.74 ?  146 THR L C   1 
ATOM   9252  O O   . THR D  3 146 ? 84.050  21.705  188.500 1.00 307.41 ?  146 THR L O   1 
ATOM   9253  C CB  . THR D  3 146 ? 86.580  22.944  189.611 1.00 307.01 ?  146 THR L CB  1 
ATOM   9254  O OG1 . THR D  3 146 ? 86.520  21.542  189.894 1.00 305.14 ?  146 THR L OG1 1 
ATOM   9255  C CG2 . THR D  3 146 ? 87.423  23.618  190.684 1.00 308.76 ?  146 THR L CG2 1 
ATOM   9256  N N   . VAL D  3 147 ? 84.013  23.709  187.464 1.00 299.78 ?  147 VAL L N   1 
ATOM   9257  C CA  . VAL D  3 147 ? 83.179  23.267  186.355 1.00 299.81 ?  147 VAL L CA  1 
ATOM   9258  C C   . VAL D  3 147 ? 84.060  23.110  185.125 1.00 306.16 ?  147 VAL L C   1 
ATOM   9259  O O   . VAL D  3 147 ? 84.843  24.011  184.800 1.00 314.17 ?  147 VAL L O   1 
ATOM   9260  C CB  . VAL D  3 147 ? 82.049  24.274  186.076 1.00 295.79 ?  147 VAL L CB  1 
ATOM   9261  C CG1 . VAL D  3 147 ? 81.138  23.754  184.986 1.00 298.43 ?  147 VAL L CG1 1 
ATOM   9262  C CG2 . VAL D  3 147 ? 81.286  24.594  187.347 1.00 290.14 ?  147 VAL L CG2 1 
ATOM   9263  N N   . ALA D  3 148 ? 83.935  21.970  184.444 1.00 302.93 ?  148 ALA L N   1 
ATOM   9264  C CA  . ALA D  3 148 ? 84.669  21.714  183.211 1.00 315.38 ?  148 ALA L CA  1 
ATOM   9265  C C   . ALA D  3 148 ? 83.704  21.243  182.134 1.00 319.87 ?  148 ALA L C   1 
ATOM   9266  O O   . ALA D  3 148 ? 83.073  20.191  182.288 1.00 318.04 ?  148 ALA L O   1 
ATOM   9267  C CB  . ALA D  3 148 ? 85.763  20.664  183.427 1.00 320.34 ?  148 ALA L CB  1 
ATOM   9268  N N   . TRP D  3 149 ? 83.586  22.008  181.054 1.00 325.25 ?  149 TRP L N   1 
ATOM   9269  C CA  . TRP D  3 149 ? 82.676  21.633  179.984 1.00 326.72 ?  149 TRP L CA  1 
ATOM   9270  C C   . TRP D  3 149 ? 83.374  20.661  179.038 1.00 337.86 ?  149 TRP L C   1 
ATOM   9271  O O   . TRP D  3 149 ? 84.604  20.625  178.947 1.00 347.08 ?  149 TRP L O   1 
ATOM   9272  C CB  . TRP D  3 149 ? 82.192  22.877  179.237 1.00 318.61 ?  149 TRP L CB  1 
ATOM   9273  C CG  . TRP D  3 149 ? 81.364  23.796  180.089 1.00 304.72 ?  149 TRP L CG  1 
ATOM   9274  C CD1 . TRP D  3 149 ? 81.813  24.757  180.944 1.00 290.80 ?  149 TRP L CD1 1 
ATOM   9275  C CD2 . TRP D  3 149 ? 79.935  23.891  180.096 1.00 292.15 ?  149 TRP L CD2 1 
ATOM   9276  N NE1 . TRP D  3 149 ? 80.752  25.411  181.523 1.00 273.75 ?  149 TRP L NE1 1 
ATOM   9277  C CE2 . TRP D  3 149 ? 79.587  24.901  181.012 1.00 278.41 ?  149 TRP L CE2 1 
ATOM   9278  C CE3 . TRP D  3 149 ? 78.916  23.205  179.429 1.00 290.23 ?  149 TRP L CE3 1 
ATOM   9279  C CZ2 . TRP D  3 149 ? 78.264  25.242  181.277 1.00 272.21 ?  149 TRP L CZ2 1 
ATOM   9280  C CZ3 . TRP D  3 149 ? 77.606  23.543  179.696 1.00 276.67 ?  149 TRP L CZ3 1 
ATOM   9281  C CH2 . TRP D  3 149 ? 77.290  24.553  180.611 1.00 272.16 ?  149 TRP L CH2 1 
ATOM   9282  N N   . LYS D  3 150 ? 82.574  19.874  178.322 1.00 314.87 ?  150 LYS L N   1 
ATOM   9283  C CA  . LYS D  3 150 ? 83.106  18.861  177.417 1.00 326.41 ?  150 LYS L CA  1 
ATOM   9284  C C   . LYS D  3 150 ? 82.294  18.876  176.127 1.00 327.27 ?  150 LYS L C   1 
ATOM   9285  O O   . LYS D  3 150 ? 81.060  18.840  176.168 1.00 318.28 ?  150 LYS L O   1 
ATOM   9286  C CB  . LYS D  3 150 ? 83.134  17.475  178.080 1.00 318.30 ?  150 LYS L CB  1 
ATOM   9287  C CG  . LYS D  3 150 ? 84.234  17.389  179.154 1.00 322.64 ?  150 LYS L CG  1 
ATOM   9288  C CD  . LYS D  3 150 ? 85.617  17.486  178.520 1.00 324.47 ?  150 LYS L CD  1 
ATOM   9289  C CE  . LYS D  3 150 ? 86.770  17.278  179.501 1.00 318.38 ?  150 LYS L CE  1 
ATOM   9290  N NZ  . LYS D  3 150 ? 86.815  15.940  180.140 1.00 324.65 1  150 LYS L NZ  1 
ATOM   9291  N N   . ALA D  3 151 ? 82.990  18.923  174.991 1.00 321.28 ?  151 ALA L N   1 
ATOM   9292  C CA  . ALA D  3 151 ? 82.400  18.765  173.662 1.00 317.60 ?  151 ALA L CA  1 
ATOM   9293  C C   . ALA D  3 151 ? 82.651  17.350  173.146 1.00 324.94 ?  151 ALA L C   1 
ATOM   9294  O O   . ALA D  3 151 ? 83.778  17.014  172.767 1.00 333.82 ?  151 ALA L O   1 
ATOM   9295  C CB  . ALA D  3 151 ? 82.970  19.803  172.699 1.00 314.43 ?  151 ALA L CB  1 
ATOM   9296  N N   . ASP D  3 152 ? 81.594  16.526  173.136 1.00 326.69 ?  152 ASP L N   1 
ATOM   9297  C CA  . ASP D  3 152 ? 81.673  15.092  172.861 1.00 329.19 ?  152 ASP L CA  1 
ATOM   9298  C C   . ASP D  3 152 ? 82.602  14.447  173.874 1.00 330.77 ?  152 ASP L C   1 
ATOM   9299  O O   . ASP D  3 152 ? 82.206  14.168  175.011 1.00 320.89 ?  152 ASP L O   1 
ATOM   9300  C CB  . ASP D  3 152 ? 82.186  14.819  171.438 1.00 333.24 ?  152 ASP L CB  1 
ATOM   9301  C CG  . ASP D  3 152 ? 81.204  15.244  170.361 1.00 326.85 ?  152 ASP L CG  1 
ATOM   9302  O OD1 . ASP D  3 152 ? 79.990  15.276  170.643 1.00 323.62 ?  152 ASP L OD1 1 
ATOM   9303  O OD2 . ASP D  3 152 ? 81.648  15.567  169.236 1.00 333.75 -1 152 ASP L OD2 1 
ATOM   9304  N N   . SER D  3 153 ? 83.835  14.190  173.458 1.00 320.66 ?  153 SER L N   1 
ATOM   9305  C CA  . SER D  3 153 ? 84.849  13.660  174.348 1.00 318.77 ?  153 SER L CA  1 
ATOM   9306  C C   . SER D  3 153 ? 86.019  14.619  174.484 1.00 322.23 ?  153 SER L C   1 
ATOM   9307  O O   . SER D  3 153 ? 86.964  14.324  175.224 1.00 314.93 ?  153 SER L O   1 
ATOM   9308  C CB  . SER D  3 153 ? 85.348  12.298  173.842 1.00 321.49 ?  153 SER L CB  1 
ATOM   9309  O OG  . SER D  3 153 ? 84.276  11.394  173.627 1.00 315.05 ?  153 SER L OG  1 
ATOM   9310  N N   . SER D  3 154 ? 85.969  15.781  173.790 1.00 332.93 ?  154 SER L N   1 
ATOM   9311  C CA  . SER D  3 154 ? 86.952  16.855  173.740 1.00 333.58 ?  154 SER L CA  1 
ATOM   9312  C C   . SER D  3 154 ? 86.581  18.004  174.663 1.00 327.96 ?  154 SER L C   1 
ATOM   9313  O O   . SER D  3 154 ? 85.428  18.458  174.652 1.00 323.83 ?  154 SER L O   1 
ATOM   9314  C CB  . SER D  3 154 ? 87.080  17.370  172.312 1.00 336.37 ?  154 SER L CB  1 
ATOM   9315  O OG  . SER D  3 154 ? 87.441  16.313  171.443 1.00 331.99 ?  154 SER L OG  1 
ATOM   9316  N N   . PRO D  3 155 ? 87.523  18.470  175.476 1.00 326.53 ?  155 PRO L N   1 
ATOM   9317  C CA  . PRO D  3 155 ? 87.247  19.580  176.396 1.00 323.01 ?  155 PRO L CA  1 
ATOM   9318  C C   . PRO D  3 155 ? 87.055  20.895  175.658 1.00 325.83 ?  155 PRO L C   1 
ATOM   9319  O O   . PRO D  3 155 ? 87.567  21.095  174.554 1.00 324.65 ?  155 PRO L O   1 
ATOM   9320  C CB  . PRO D  3 155 ? 88.493  19.620  177.285 1.00 322.19 ?  155 PRO L CB  1 
ATOM   9321  C CG  . PRO D  3 155 ? 89.571  19.035  176.424 1.00 325.93 ?  155 PRO L CG  1 
ATOM   9322  C CD  . PRO D  3 155 ? 88.902  17.972  175.605 1.00 325.93 ?  155 PRO L CD  1 
ATOM   9323  N N   . VAL D  3 156 ? 86.300  21.797  176.276 1.00 327.21 ?  156 VAL L N   1 
ATOM   9324  C CA  . VAL D  3 156 ? 86.052  23.120  175.718 1.00 325.07 ?  156 VAL L CA  1 
ATOM   9325  C C   . VAL D  3 156 ? 86.994  24.078  176.438 1.00 327.58 ?  156 VAL L C   1 
ATOM   9326  O O   . VAL D  3 156 ? 86.985  24.157  177.671 1.00 321.84 ?  156 VAL L O   1 
ATOM   9327  C CB  . VAL D  3 156 ? 84.585  23.544  175.899 1.00 311.02 ?  156 VAL L CB  1 
ATOM   9328  C CG1 . VAL D  3 156 ? 84.385  24.938  175.387 1.00 305.13 ?  156 VAL L CG1 1 
ATOM   9329  C CG2 . VAL D  3 156 ? 83.651  22.591  175.187 1.00 303.76 ?  156 VAL L CG2 1 
ATOM   9330  N N   . LYS D  3 157 ? 87.806  24.810  175.674 1.00 317.39 ?  157 LYS L N   1 
ATOM   9331  C CA  . LYS D  3 157 ? 88.829  25.688  176.239 1.00 318.59 ?  157 LYS L CA  1 
ATOM   9332  C C   . LYS D  3 157 ? 88.276  27.073  176.566 1.00 312.94 ?  157 LYS L C   1 
ATOM   9333  O O   . LYS D  3 157 ? 88.382  27.541  177.706 1.00 300.65 ?  157 LYS L O   1 
ATOM   9334  C CB  . LYS D  3 157 ? 90.024  25.792  175.284 1.00 317.80 ?  157 LYS L CB  1 
ATOM   9335  C CG  . LYS D  3 157 ? 90.745  24.474  175.017 1.00 320.79 ?  157 LYS L CG  1 
ATOM   9336  C CD  . LYS D  3 157 ? 91.875  24.686  174.019 1.00 330.36 ?  157 LYS L CD  1 
ATOM   9337  C CE  . LYS D  3 157 ? 92.677  23.423  173.805 1.00 338.14 ?  157 LYS L CE  1 
ATOM   9338  N NZ  . LYS D  3 157 ? 92.083  22.279  174.544 1.00 335.31 1  157 LYS L NZ  1 
ATOM   9339  N N   . ALA D  3 158 ? 87.682  27.738  175.585 1.00 323.77 ?  158 ALA L N   1 
ATOM   9340  C CA  . ALA D  3 158 ? 87.204  29.090  175.801 1.00 315.12 ?  158 ALA L CA  1 
ATOM   9341  C C   . ALA D  3 158 ? 85.685  29.118  175.828 1.00 301.20 ?  158 ALA L C   1 
ATOM   9342  O O   . ALA D  3 158 ? 84.999  28.166  175.444 1.00 301.30 ?  158 ALA L O   1 
ATOM   9343  C CB  . ALA D  3 158 ? 87.729  30.034  174.714 1.00 315.42 ?  158 ALA L CB  1 
ATOM   9344  N N   . GLY D  3 159 ? 85.177  30.247  176.303 1.00 327.44 ?  159 GLY L N   1 
ATOM   9345  C CA  . GLY D  3 159 ? 83.764  30.487  176.413 1.00 315.62 ?  159 GLY L CA  1 
ATOM   9346  C C   . GLY D  3 159 ? 83.180  30.056  177.735 1.00 307.12 ?  159 GLY L C   1 
ATOM   9347  O O   . GLY D  3 159 ? 81.961  30.166  177.918 1.00 295.74 ?  159 GLY L O   1 
ATOM   9348  N N   . VAL D  3 160 ? 84.005  29.564  178.659 1.00 321.87 ?  160 VAL L N   1 
ATOM   9349  C CA  . VAL D  3 160 ? 83.517  29.090  179.947 1.00 307.77 ?  160 VAL L CA  1 
ATOM   9350  C C   . VAL D  3 160 ? 83.600  30.243  180.939 1.00 300.28 ?  160 VAL L C   1 
ATOM   9351  O O   . VAL D  3 160 ? 84.667  30.830  181.150 1.00 305.57 ?  160 VAL L O   1 
ATOM   9352  C CB  . VAL D  3 160 ? 84.317  27.869  180.425 1.00 302.51 ?  160 VAL L CB  1 
ATOM   9353  C CG1 . VAL D  3 160 ? 84.009  26.685  179.539 1.00 293.42 ?  160 VAL L CG1 1 
ATOM   9354  C CG2 . VAL D  3 160 ? 85.814  28.148  180.388 1.00 312.99 ?  160 VAL L CG2 1 
ATOM   9355  N N   . GLU D  3 161 ? 82.456  30.586  181.517 1.00 308.76 ?  161 GLU L N   1 
ATOM   9356  C CA  . GLU D  3 161 ? 82.328  31.627  182.529 1.00 295.02 ?  161 GLU L CA  1 
ATOM   9357  C C   . GLU D  3 161 ? 81.637  31.009  183.735 1.00 280.05 ?  161 GLU L C   1 
ATOM   9358  O O   . GLU D  3 161 ? 80.500  30.538  183.623 1.00 272.47 ?  161 GLU L O   1 
ATOM   9359  C CB  . GLU D  3 161 ? 81.639  32.863  181.955 1.00 289.51 ?  161 GLU L CB  1 
ATOM   9360  C CG  . GLU D  3 161 ? 82.415  33.274  180.693 1.00 300.21 ?  161 GLU L CG  1 
ATOM   9361  C CD  . GLU D  3 161 ? 82.869  34.707  180.683 1.00 310.50 ?  161 GLU L CD  1 
ATOM   9362  O OE1 . GLU D  3 161 ? 82.022  35.591  180.770 1.00 309.42 ?  161 GLU L OE1 1 
ATOM   9363  O OE2 . GLU D  3 161 ? 84.095  34.945  180.589 1.00 327.29 -1 161 GLU L OE2 1 
ATOM   9364  N N   . THR D  3 162 ? 82.309  31.013  184.882 1.00 295.49 ?  162 THR L N   1 
ATOM   9365  C CA  . THR D  3 162 ? 81.822  30.351  186.084 1.00 291.16 ?  162 THR L CA  1 
ATOM   9366  C C   . THR D  3 162 ? 81.739  31.317  187.255 1.00 287.72 ?  162 THR L C   1 
ATOM   9367  O O   . THR D  3 162 ? 82.649  32.119  187.484 1.00 290.00 ?  162 THR L O   1 
ATOM   9368  C CB  . THR D  3 162 ? 82.753  29.190  186.468 1.00 293.80 ?  162 THR L CB  1 
ATOM   9369  O OG1 . THR D  3 162 ? 82.918  28.307  185.351 1.00 298.90 ?  162 THR L OG1 1 
ATOM   9370  C CG2 . THR D  3 162 ? 82.196  28.416  187.653 1.00 289.70 ?  162 THR L CG2 1 
ATOM   9371  N N   . THR D  3 163 ? 80.624  31.234  187.984 1.00 304.41 ?  163 THR L N   1 
ATOM   9372  C CA  . THR D  3 163 ? 80.403  32.089  189.135 1.00 292.21 ?  163 THR L CA  1 
ATOM   9373  C C   . THR D  3 163 ? 81.167  31.554  190.340 1.00 291.29 ?  163 THR L C   1 
ATOM   9374  O O   . THR D  3 163 ? 81.602  30.400  190.375 1.00 292.67 ?  163 THR L O   1 
ATOM   9375  C CB  . THR D  3 163 ? 78.908  32.133  189.474 1.00 276.69 ?  163 THR L CB  1 
ATOM   9376  O OG1 . THR D  3 163 ? 78.136  32.070  188.268 1.00 286.97 ?  163 THR L OG1 1 
ATOM   9377  C CG2 . THR D  3 163 ? 78.544  33.402  190.238 1.00 254.54 ?  163 THR L CG2 1 
ATOM   9378  N N   . THR D  3 164 ? 81.323  32.381  191.295 1.00 287.61 ?  164 THR L N   1 
ATOM   9379  C CA  . THR D  3 164 ? 81.958  32.045  192.561 1.00 289.11 ?  164 THR L CA  1 
ATOM   9380  C C   . THR D  3 164 ? 80.932  31.594  193.604 1.00 282.45 ?  164 THR L C   1 
ATOM   9381  O O   . THR D  3 164 ? 79.824  32.135  193.658 1.00 280.68 ?  164 THR L O   1 
ATOM   9382  C CB  . THR D  3 164 ? 82.759  33.233  193.086 1.00 296.53 ?  164 THR L CB  1 
ATOM   9383  O OG1 . THR D  3 164 ? 83.171  32.980  194.434 1.00 290.37 ?  164 THR L OG1 1 
ATOM   9384  C CG2 . THR D  3 164 ? 81.938  34.513  193.023 1.00 293.66 ?  164 THR L CG2 1 
ATOM   9385  N N   . PRO D  3 165 ? 81.290  30.581  194.399 1.00 279.51 ?  165 PRO L N   1 
ATOM   9386  C CA  . PRO D  3 165 ? 80.383  30.066  195.440 1.00 274.64 ?  165 PRO L CA  1 
ATOM   9387  C C   . PRO D  3 165 ? 79.836  31.186  196.324 1.00 271.03 ?  165 PRO L C   1 
ATOM   9388  O O   . PRO D  3 165 ? 80.522  32.170  196.609 1.00 272.83 ?  165 PRO L O   1 
ATOM   9389  C CB  . PRO D  3 165 ? 81.265  29.082  196.216 1.00 276.47 ?  165 PRO L CB  1 
ATOM   9390  C CG  . PRO D  3 165 ? 82.258  28.601  195.171 1.00 281.91 ?  165 PRO L CG  1 
ATOM   9391  C CD  . PRO D  3 165 ? 82.531  29.791  194.296 1.00 284.21 ?  165 PRO L CD  1 
ATOM   9392  N N   . SER D  3 166 ? 78.584  31.031  196.767 1.00 287.45 ?  166 SER L N   1 
ATOM   9393  C CA  . SER D  3 166 ? 77.939  32.068  197.579 1.00 286.18 ?  166 SER L CA  1 
ATOM   9394  C C   . SER D  3 166 ? 76.807  31.491  198.425 1.00 282.54 ?  166 SER L C   1 
ATOM   9395  O O   . SER D  3 166 ? 75.787  31.066  197.874 1.00 282.83 ?  166 SER L O   1 
ATOM   9396  C CB  . SER D  3 166 ? 77.416  33.174  196.675 1.00 283.95 ?  166 SER L CB  1 
ATOM   9397  O OG  . SER D  3 166 ? 76.539  32.630  195.708 1.00 275.23 ?  166 SER L OG  1 
ATOM   9398  N N   . LYS D  3 167 ? 76.988  31.467  199.750 1.00 287.41 ?  167 LYS L N   1 
ATOM   9399  C CA  . LYS D  3 167 ? 75.979  30.911  200.646 1.00 282.26 ?  167 LYS L CA  1 
ATOM   9400  C C   . LYS D  3 167 ? 74.723  31.766  200.732 1.00 285.80 ?  167 LYS L C   1 
ATOM   9401  O O   . LYS D  3 167 ? 74.768  32.992  200.601 1.00 287.04 ?  167 LYS L O   1 
ATOM   9402  C CB  . LYS D  3 167 ? 76.536  30.917  202.076 1.00 282.01 ?  167 LYS L CB  1 
ATOM   9403  C CG  . LYS D  3 167 ? 77.396  29.797  202.530 1.00 274.95 ?  167 LYS L CG  1 
ATOM   9404  C CD  . LYS D  3 167 ? 77.973  30.031  203.939 1.00 273.21 ?  167 LYS L CD  1 
ATOM   9405  C CE  . LYS D  3 167 ? 77.920  31.493  204.374 1.00 271.01 ?  167 LYS L CE  1 
ATOM   9406  N NZ  . LYS D  3 167 ? 78.385  31.680  205.777 1.00 268.44 1  167 LYS L NZ  1 
ATOM   9407  N N   . GLN D  3 168 ? 73.566  31.083  200.953 1.00 280.16 ?  168 GLN L N   1 
ATOM   9408  C CA  . GLN D  3 168 ? 72.256  31.743  201.076 1.00 278.86 ?  168 GLN L CA  1 
ATOM   9409  C C   . GLN D  3 168 ? 71.485  31.143  202.263 1.00 280.09 ?  168 GLN L C   1 
ATOM   9410  O O   . GLN D  3 168 ? 70.656  30.245  202.087 1.00 271.58 ?  168 GLN L O   1 
ATOM   9411  C CB  . GLN D  3 168 ? 71.436  31.688  199.787 1.00 273.37 ?  168 GLN L CB  1 
ATOM   9412  C CG  . GLN D  3 168 ? 72.034  32.480  198.634 1.00 275.92 ?  168 GLN L CG  1 
ATOM   9413  C CD  . GLN D  3 168 ? 71.240  32.332  197.352 1.00 277.47 ?  168 GLN L CD  1 
ATOM   9414  O OE1 . GLN D  3 168 ? 70.556  31.330  197.145 1.00 277.56 ?  168 GLN L OE1 1 
ATOM   9415  N NE2 . GLN D  3 168 ? 71.316  33.339  196.489 1.00 284.22 ?  168 GLN L NE2 1 
ATOM   9416  N N   . SER D  3 169 ? 71.753  31.638  203.470 1.00 279.99 ?  169 SER L N   1 
ATOM   9417  C CA  . SER D  3 169 ? 71.029  31.210  204.674 1.00 278.01 ?  169 SER L CA  1 
ATOM   9418  C C   . SER D  3 169 ? 71.016  29.690  204.867 1.00 275.36 ?  169 SER L C   1 
ATOM   9419  O O   . SER D  3 169 ? 70.068  29.145  205.436 1.00 270.24 ?  169 SER L O   1 
ATOM   9420  C CB  . SER D  3 169 ? 69.596  31.751  204.665 1.00 269.50 ?  169 SER L CB  1 
ATOM   9421  O OG  . SER D  3 169 ? 68.886  31.343  205.822 1.00 273.41 ?  169 SER L OG  1 
ATOM   9422  N N   . ASN D  3 170 ? 72.046  28.979  204.428 1.00 278.61 ?  170 ASN L N   1 
ATOM   9423  C CA  . ASN D  3 170 ? 72.019  27.523  204.563 1.00 272.65 ?  170 ASN L CA  1 
ATOM   9424  C C   . ASN D  3 170 ? 73.417  26.989  204.284 1.00 269.00 ?  170 ASN L C   1 
ATOM   9425  O O   . ASN D  3 170 ? 74.388  27.752  204.207 1.00 263.62 ?  170 ASN L O   1 
ATOM   9426  C CB  . ASN D  3 170 ? 71.019  26.915  203.575 1.00 269.83 ?  170 ASN L CB  1 
ATOM   9427  C CG  . ASN D  3 170 ? 69.892  26.170  204.252 1.00 267.63 ?  170 ASN L CG  1 
ATOM   9428  O OD1 . ASN D  3 170 ? 70.026  25.685  205.376 1.00 269.86 ?  170 ASN L OD1 1 
ATOM   9429  N ND2 . ASN D  3 170 ? 68.755  26.098  203.571 1.00 262.53 ?  170 ASN L ND2 1 
ATOM   9430  N N   . ASN D  3 171 ? 73.524  25.666  204.149 1.00 277.32 ?  171 ASN L N   1 
ATOM   9431  C CA  . ASN D  3 171 ? 74.761  25.063  203.677 1.00 282.28 ?  171 ASN L CA  1 
ATOM   9432  C C   . ASN D  3 171 ? 74.845  25.147  202.165 1.00 281.38 ?  171 ASN L C   1 
ATOM   9433  O O   . ASN D  3 171 ? 75.917  24.920  201.593 1.00 286.81 ?  171 ASN L O   1 
ATOM   9434  C CB  . ASN D  3 171 ? 74.898  23.607  204.150 1.00 293.86 ?  171 ASN L CB  1 
ATOM   9435  C CG  . ASN D  3 171 ? 73.832  22.675  203.579 1.00 294.00 ?  171 ASN L CG  1 
ATOM   9436  O OD1 . ASN D  3 171 ? 73.491  22.721  202.395 1.00 302.31 ?  171 ASN L OD1 1 
ATOM   9437  N ND2 . ASN D  3 171 ? 73.320  21.799  204.431 1.00 283.64 ?  171 ASN L ND2 1 
ATOM   9438  N N   . LYS D  3 172 ? 73.715  25.463  201.532 1.00 288.89 ?  172 LYS L N   1 
ATOM   9439  C CA  . LYS D  3 172 ? 73.565  25.570  200.088 1.00 290.93 ?  172 LYS L CA  1 
ATOM   9440  C C   . LYS D  3 172 ? 74.381  26.734  199.559 1.00 289.45 ?  172 LYS L C   1 
ATOM   9441  O O   . LYS D  3 172 ? 74.077  27.898  199.845 1.00 282.15 ?  172 LYS L O   1 
ATOM   9442  C CB  . LYS D  3 172 ? 72.103  25.782  199.715 1.00 285.54 ?  172 LYS L CB  1 
ATOM   9443  C CG  . LYS D  3 172 ? 71.952  26.161  198.251 1.00 286.36 ?  172 LYS L CG  1 
ATOM   9444  C CD  . LYS D  3 172 ? 70.538  26.537  197.884 1.00 276.62 ?  172 LYS L CD  1 
ATOM   9445  C CE  . LYS D  3 172 ? 70.284  27.989  198.273 1.00 269.71 ?  172 LYS L CE  1 
ATOM   9446  N NZ  . LYS D  3 172 ? 69.594  28.747  197.195 1.00 273.63 1  172 LYS L NZ  1 
ATOM   9447  N N   . TYR D  3 173 ? 75.428  26.427  198.811 1.00 288.97 ?  173 TYR L N   1 
ATOM   9448  C CA  . TYR D  3 173 ? 76.167  27.460  198.114 1.00 285.53 ?  173 TYR L CA  1 
ATOM   9449  C C   . TYR D  3 173 ? 75.590  27.475  196.700 1.00 284.13 ?  173 TYR L C   1 
ATOM   9450  O O   . TYR D  3 173 ? 75.003  26.488  196.249 1.00 282.54 ?  173 TYR L O   1 
ATOM   9451  C CB  . TYR D  3 173 ? 77.653  27.104  198.096 1.00 287.58 ?  173 TYR L CB  1 
ATOM   9452  C CG  . TYR D  3 173 ? 78.407  27.460  199.362 1.00 286.18 ?  173 TYR L CG  1 
ATOM   9453  C CD1 . TYR D  3 173 ? 78.304  26.632  200.474 1.00 289.07 ?  173 TYR L CD1 1 
ATOM   9454  C CD2 . TYR D  3 173 ? 79.243  28.568  199.446 1.00 287.05 ?  173 TYR L CD2 1 
ATOM   9455  C CE1 . TYR D  3 173 ? 78.979  26.900  201.639 1.00 285.71 ?  173 TYR L CE1 1 
ATOM   9456  C CE2 . TYR D  3 173 ? 79.943  28.839  200.619 1.00 291.67 ?  173 TYR L CE2 1 
ATOM   9457  C CZ  . TYR D  3 173 ? 79.805  27.996  201.709 1.00 285.44 ?  173 TYR L CZ  1 
ATOM   9458  O OH  . TYR D  3 173 ? 80.475  28.257  202.882 1.00 269.23 ?  173 TYR L OH  1 
ATOM   9459  N N   . ALA D  3 174 ? 75.736  28.593  195.999 1.00 283.51 ?  174 ALA L N   1 
ATOM   9460  C CA  . ALA D  3 174 ? 75.174  28.704  194.659 1.00 283.58 ?  174 ALA L CA  1 
ATOM   9461  C C   . ALA D  3 174 ? 76.261  28.959  193.622 1.00 288.92 ?  174 ALA L C   1 
ATOM   9462  O O   . ALA D  3 174 ? 77.198  29.724  193.870 1.00 298.30 ?  174 ALA L O   1 
ATOM   9463  C CB  . ALA D  3 174 ? 74.119  29.803  194.615 1.00 278.91 ?  174 ALA L CB  1 
ATOM   9464  N N   . ALA D  3 175 ? 76.122  28.336  192.451 1.00 281.36 ?  175 ALA L N   1 
ATOM   9465  C CA  . ALA D  3 175 ? 77.106  28.529  191.393 1.00 285.54 ?  175 ALA L CA  1 
ATOM   9466  C C   . ALA D  3 175 ? 76.514  28.207  190.027 1.00 292.34 ?  175 ALA L C   1 
ATOM   9467  O O   . ALA D  3 175 ? 75.942  27.128  189.840 1.00 292.52 ?  175 ALA L O   1 
ATOM   9468  C CB  . ALA D  3 175 ? 78.341  27.659  191.650 1.00 289.63 ?  175 ALA L CB  1 
ATOM   9469  N N   . SER D  3 176 ? 76.665  29.132  189.077 1.00 289.85 ?  176 SER L N   1 
ATOM   9470  C CA  . SER D  3 176 ? 76.176  28.958  187.713 1.00 286.31 ?  176 SER L CA  1 
ATOM   9471  C C   . SER D  3 176 ? 77.364  29.105  186.766 1.00 296.13 ?  176 SER L C   1 
ATOM   9472  O O   . SER D  3 176 ? 78.133  30.066  186.874 1.00 306.85 ?  176 SER L O   1 
ATOM   9473  C CB  . SER D  3 176 ? 75.069  29.966  187.374 1.00 268.40 ?  176 SER L CB  1 
ATOM   9474  O OG  . SER D  3 176 ? 75.403  31.275  187.796 1.00 267.95 ?  176 SER L OG  1 
ATOM   9475  N N   . SER D  3 177 ? 77.491  28.164  185.830 1.00 281.34 ?  177 SER L N   1 
ATOM   9476  C CA  . SER D  3 177 ? 78.545  28.132  184.819 1.00 291.22 ?  177 SER L CA  1 
ATOM   9477  C C   . SER D  3 177 ? 77.919  28.210  183.432 1.00 291.96 ?  177 SER L C   1 
ATOM   9478  O O   . SER D  3 177 ? 77.027  27.419  183.111 1.00 289.99 ?  177 SER L O   1 
ATOM   9479  C CB  . SER D  3 177 ? 79.411  26.875  184.950 1.00 297.57 ?  177 SER L CB  1 
ATOM   9480  O OG  . SER D  3 177 ? 78.926  25.831  184.129 1.00 301.63 ?  177 SER L OG  1 
ATOM   9481  N N   . TYR D  3 178 ? 78.375  29.163  182.619 1.00 290.82 ?  178 TYR L N   1 
ATOM   9482  C CA  . TYR D  3 178 ? 77.835  29.390  181.285 1.00 287.87 ?  178 TYR L CA  1 
ATOM   9483  C C   . TYR D  3 178 ? 78.866  29.062  180.214 1.00 295.25 ?  178 TYR L C   1 
ATOM   9484  O O   . TYR D  3 178 ? 80.074  29.217  180.416 1.00 305.31 ?  178 TYR L O   1 
ATOM   9485  C CB  . TYR D  3 178 ? 77.413  30.857  181.127 1.00 285.06 ?  178 TYR L CB  1 
ATOM   9486  C CG  . TYR D  3 178 ? 76.284  31.257  182.041 1.00 282.73 ?  178 TYR L CG  1 
ATOM   9487  C CD1 . TYR D  3 178 ? 76.548  31.680  183.335 1.00 272.97 ?  178 TYR L CD1 1 
ATOM   9488  C CD2 . TYR D  3 178 ? 74.964  31.237  181.613 1.00 280.17 ?  178 TYR L CD2 1 
ATOM   9489  C CE1 . TYR D  3 178 ? 75.531  32.042  184.189 1.00 264.13 ?  178 TYR L CE1 1 
ATOM   9490  C CE2 . TYR D  3 178 ? 73.935  31.607  182.462 1.00 274.67 ?  178 TYR L CE2 1 
ATOM   9491  C CZ  . TYR D  3 178 ? 74.228  32.011  183.749 1.00 270.82 ?  178 TYR L CZ  1 
ATOM   9492  O OH  . TYR D  3 178 ? 73.210  32.377  184.600 1.00 263.97 ?  178 TYR L OH  1 
ATOM   9493  N N   . LEU D  3 179 ? 78.366  28.607  179.062 1.00 276.09 ?  179 LEU L N   1 
ATOM   9494  C CA  . LEU D  3 179 ? 79.203  28.277  177.909 1.00 284.29 ?  179 LEU L CA  1 
ATOM   9495  C C   . LEU D  3 179 ? 78.523  28.870  176.680 1.00 292.34 ?  179 LEU L C   1 
ATOM   9496  O O   . LEU D  3 179 ? 77.531  28.330  176.182 1.00 291.93 ?  179 LEU L O   1 
ATOM   9497  C CB  . LEU D  3 179 ? 79.382  26.768  177.766 1.00 287.49 ?  179 LEU L CB  1 
ATOM   9498  C CG  . LEU D  3 179 ? 80.245  26.288  176.594 1.00 295.25 ?  179 LEU L CG  1 
ATOM   9499  C CD1 . LEU D  3 179 ? 81.625  26.922  176.641 1.00 304.05 ?  179 LEU L CD1 1 
ATOM   9500  C CD2 . LEU D  3 179 ? 80.340  24.766  176.553 1.00 294.65 ?  179 LEU L CD2 1 
ATOM   9501  N N   . SER D  3 180 ? 79.071  29.984  176.202 1.00 277.61 ?  180 SER L N   1 
ATOM   9502  C CA  . SER D  3 180 ? 78.538  30.694  175.047 1.00 279.62 ?  180 SER L CA  1 
ATOM   9503  C C   . SER D  3 180 ? 78.999  29.999  173.773 1.00 296.69 ?  180 SER L C   1 
ATOM   9504  O O   . SER D  3 180 ? 80.204  29.887  173.526 1.00 306.80 ?  180 SER L O   1 
ATOM   9505  C CB  . SER D  3 180 ? 78.976  32.157  175.074 1.00 273.10 ?  180 SER L CB  1 
ATOM   9506  O OG  . SER D  3 180 ? 78.517  32.799  176.253 1.00 261.94 ?  180 SER L OG  1 
ATOM   9507  N N   . LEU D  3 181 ? 78.051  29.535  172.965 1.00 282.49 ?  181 LEU L N   1 
ATOM   9508  C CA  . LEU D  3 181 ? 78.365  28.865  171.713 1.00 288.94 ?  181 LEU L CA  1 
ATOM   9509  C C   . LEU D  3 181 ? 77.586  29.504  170.576 1.00 296.10 ?  181 LEU L C   1 
ATOM   9510  O O   . LEU D  3 181 ? 76.744  30.383  170.777 1.00 294.91 ?  181 LEU L O   1 
ATOM   9511  C CB  . LEU D  3 181 ? 78.041  27.364  171.768 1.00 288.34 ?  181 LEU L CB  1 
ATOM   9512  C CG  . LEU D  3 181 ? 78.828  26.462  172.714 1.00 291.66 ?  181 LEU L CG  1 
ATOM   9513  C CD1 . LEU D  3 181 ? 78.339  25.028  172.587 1.00 292.28 ?  181 LEU L CD1 1 
ATOM   9514  C CD2 . LEU D  3 181 ? 80.312  26.547  172.405 1.00 298.25 ?  181 LEU L CD2 1 
ATOM   9515  N N   . THR D  3 182 ? 77.890  29.054  169.372 1.00 297.47 ?  182 THR L N   1 
ATOM   9516  C CA  . THR D  3 182 ? 77.196  29.526  168.191 1.00 300.49 ?  182 THR L CA  1 
ATOM   9517  C C   . THR D  3 182 ? 76.194  28.482  167.722 1.00 302.14 ?  182 THR L C   1 
ATOM   9518  O O   . THR D  3 182 ? 76.371  27.286  167.967 1.00 304.17 ?  182 THR L O   1 
ATOM   9519  C CB  . THR D  3 182 ? 78.184  29.823  167.060 1.00 298.66 ?  182 THR L CB  1 
ATOM   9520  O OG1 . THR D  3 182 ? 78.803  28.603  166.631 1.00 305.53 ?  182 THR L OG1 1 
ATOM   9521  C CG2 . THR D  3 182 ? 79.246  30.798  167.537 1.00 294.71 ?  182 THR L CG2 1 
ATOM   9522  N N   . PRO D  3 183 ? 75.120  28.917  167.068 1.00 308.79 ?  183 PRO L N   1 
ATOM   9523  C CA  . PRO D  3 183 ? 74.131  27.957  166.553 1.00 309.33 ?  183 PRO L CA  1 
ATOM   9524  C C   . PRO D  3 183 ? 74.708  26.863  165.665 1.00 317.13 ?  183 PRO L C   1 
ATOM   9525  O O   . PRO D  3 183 ? 74.114  25.781  165.582 1.00 314.84 ?  183 PRO L O   1 
ATOM   9526  C CB  . PRO D  3 183 ? 73.160  28.855  165.778 1.00 307.39 ?  183 PRO L CB  1 
ATOM   9527  C CG  . PRO D  3 183 ? 73.242  30.170  166.475 1.00 300.07 ?  183 PRO L CG  1 
ATOM   9528  C CD  . PRO D  3 183 ? 74.677  30.313  166.900 1.00 302.54 ?  183 PRO L CD  1 
ATOM   9529  N N   . GLU D  3 184 ? 75.834  27.107  164.986 1.00 313.33 ?  184 GLU L N   1 
ATOM   9530  C CA  . GLU D  3 184 ? 76.435  26.060  164.167 1.00 317.42 ?  184 GLU L CA  1 
ATOM   9531  C C   . GLU D  3 184 ? 77.220  25.051  165.000 1.00 317.17 ?  184 GLU L C   1 
ATOM   9532  O O   . GLU D  3 184 ? 77.212  23.853  164.695 1.00 321.31 ?  184 GLU L O   1 
ATOM   9533  C CB  . GLU D  3 184 ? 77.356  26.711  163.138 1.00 321.39 ?  184 GLU L CB  1 
ATOM   9534  C CG  . GLU D  3 184 ? 76.661  27.750  162.279 1.00 323.83 ?  184 GLU L CG  1 
ATOM   9535  C CD  . GLU D  3 184 ? 77.627  28.515  161.397 1.00 339.41 ?  184 GLU L CD  1 
ATOM   9536  O OE1 . GLU D  3 184 ? 78.851  28.298  161.526 1.00 344.52 ?  184 GLU L OE1 1 
ATOM   9537  O OE2 . GLU D  3 184 ? 77.163  29.346  160.586 1.00 349.92 -1 184 GLU L OE2 1 
ATOM   9538  N N   . GLN D  3 185 ? 77.894  25.510  166.056 1.00 318.17 ?  185 GLN L N   1 
ATOM   9539  C CA  . GLN D  3 185 ? 78.657  24.592  166.897 1.00 317.09 ?  185 GLN L CA  1 
ATOM   9540  C C   . GLN D  3 185 ? 77.727  23.668  167.674 1.00 312.59 ?  185 GLN L C   1 
ATOM   9541  O O   . GLN D  3 185 ? 78.057  22.501  167.916 1.00 312.11 ?  185 GLN L O   1 
ATOM   9542  C CB  . GLN D  3 185 ? 79.627  25.320  167.824 1.00 312.45 ?  185 GLN L CB  1 
ATOM   9543  C CG  . GLN D  3 185 ? 80.445  24.309  168.630 1.00 312.41 ?  185 GLN L CG  1 
ATOM   9544  C CD  . GLN D  3 185 ? 81.875  24.722  168.863 1.00 314.10 ?  185 GLN L CD  1 
ATOM   9545  O OE1 . GLN D  3 185 ? 82.249  25.872  168.646 1.00 316.65 ?  185 GLN L OE1 1 
ATOM   9546  N NE2 . GLN D  3 185 ? 82.700  23.778  169.327 1.00 317.77 ?  185 GLN L NE2 1 
ATOM   9547  N N   . TRP D  3 186 ? 76.568  24.183  168.089 1.00 322.02 ?  186 TRP L N   1 
ATOM   9548  C CA  . TRP D  3 186 ? 75.641  23.391  168.890 1.00 313.39 ?  186 TRP L CA  1 
ATOM   9549  C C   . TRP D  3 186 ? 75.103  22.209  168.104 1.00 315.29 ?  186 TRP L C   1 
ATOM   9550  O O   . TRP D  3 186 ? 74.989  21.100  168.639 1.00 311.27 ?  186 TRP L O   1 
ATOM   9551  C CB  . TRP D  3 186 ? 74.492  24.279  169.366 1.00 301.90 ?  186 TRP L CB  1 
ATOM   9552  C CG  . TRP D  3 186 ? 73.357  23.513  169.929 1.00 302.46 ?  186 TRP L CG  1 
ATOM   9553  C CD1 . TRP D  3 186 ? 72.102  23.421  169.403 1.00 298.66 ?  186 TRP L CD1 1 
ATOM   9554  C CD2 . TRP D  3 186 ? 73.373  22.669  171.080 1.00 301.86 ?  186 TRP L CD2 1 
ATOM   9555  N NE1 . TRP D  3 186 ? 71.323  22.603  170.178 1.00 296.34 ?  186 TRP L NE1 1 
ATOM   9556  C CE2 . TRP D  3 186 ? 72.081  22.124  171.214 1.00 294.58 ?  186 TRP L CE2 1 
ATOM   9557  C CE3 . TRP D  3 186 ? 74.349  22.333  172.022 1.00 293.22 ?  186 TRP L CE3 1 
ATOM   9558  C CZ2 . TRP D  3 186 ? 71.740  21.263  172.249 1.00 284.40 ?  186 TRP L CZ2 1 
ATOM   9559  C CZ3 . TRP D  3 186 ? 74.009  21.479  173.048 1.00 288.93 ?  186 TRP L CZ3 1 
ATOM   9560  C CH2 . TRP D  3 186 ? 72.716  20.953  173.154 1.00 285.79 ?  186 TRP L CH2 1 
ATOM   9561  N N   . LYS D  3 187 ? 74.741  22.421  166.850 1.00 309.16 ?  187 LYS L N   1 
ATOM   9562  C CA  . LYS D  3 187 ? 74.223  21.315  166.065 1.00 310.28 ?  187 LYS L CA  1 
ATOM   9563  C C   . LYS D  3 187 ? 75.343  20.428  165.528 1.00 314.50 ?  187 LYS L C   1 
ATOM   9564  O O   . LYS D  3 187 ? 75.054  19.396  164.912 1.00 315.57 ?  187 LYS L O   1 
ATOM   9565  C CB  . LYS D  3 187 ? 73.378  21.847  164.909 1.00 308.19 ?  187 LYS L CB  1 
ATOM   9566  C CG  . LYS D  3 187 ? 72.095  22.543  165.338 1.00 304.74 ?  187 LYS L CG  1 
ATOM   9567  C CD  . LYS D  3 187 ? 71.135  21.598  166.038 1.00 303.47 ?  187 LYS L CD  1 
ATOM   9568  C CE  . LYS D  3 187 ? 69.845  22.317  166.404 1.00 300.07 ?  187 LYS L CE  1 
ATOM   9569  N NZ  . LYS D  3 187 ? 68.875  21.421  167.089 1.00 300.34 1  187 LYS L NZ  1 
ATOM   9570  N N   . SER D  3 188 ? 76.608  20.805  165.753 1.00 311.14 ?  188 SER L N   1 
ATOM   9571  C CA  . SER D  3 188 ? 77.769  20.070  165.259 1.00 314.13 ?  188 SER L CA  1 
ATOM   9572  C C   . SER D  3 188 ? 78.019  18.784  166.037 1.00 312.77 ?  188 SER L C   1 
ATOM   9573  O O   . SER D  3 188 ? 77.721  17.688  165.553 1.00 313.70 ?  188 SER L O   1 
ATOM   9574  C CB  . SER D  3 188 ? 79.016  20.953  165.329 1.00 313.54 ?  188 SER L CB  1 
ATOM   9575  O OG  . SER D  3 188 ? 78.858  22.124  164.549 1.00 315.45 ?  188 SER L OG  1 
ATOM   9576  N N   . HIS D  3 189 ? 78.566  18.907  167.242 1.00 315.95 ?  189 HIS L N   1 
ATOM   9577  C CA  . HIS D  3 189 ? 78.894  17.735  168.039 1.00 318.32 ?  189 HIS L CA  1 
ATOM   9578  C C   . HIS D  3 189 ? 77.642  16.980  168.475 1.00 311.07 ?  189 HIS L C   1 
ATOM   9579  O O   . HIS D  3 189 ? 76.516  17.483  168.429 1.00 300.52 ?  189 HIS L O   1 
ATOM   9580  C CB  . HIS D  3 189 ? 79.774  18.091  169.235 1.00 320.65 ?  189 HIS L CB  1 
ATOM   9581  C CG  . HIS D  3 189 ? 81.081  18.717  168.860 1.00 318.92 ?  189 HIS L CG  1 
ATOM   9582  N ND1 . HIS D  3 189 ? 82.274  18.036  168.972 1.00 326.45 ?  189 HIS L ND1 1 
ATOM   9583  C CD2 . HIS D  3 189 ? 81.391  19.940  168.369 1.00 310.27 ?  189 HIS L CD2 1 
ATOM   9584  C CE1 . HIS D  3 189 ? 83.264  18.814  168.574 1.00 324.91 ?  189 HIS L CE1 1 
ATOM   9585  N NE2 . HIS D  3 189 ? 82.755  19.976  168.203 1.00 317.39 ?  189 HIS L NE2 1 
ATOM   9586  N N   . LYS D  3 190 ? 77.873  15.744  168.917 1.00 295.88 ?  190 LYS L N   1 
ATOM   9587  C CA  . LYS D  3 190 ? 76.785  14.863  169.318 1.00 294.27 ?  190 LYS L CA  1 
ATOM   9588  C C   . LYS D  3 190 ? 76.120  15.351  170.594 1.00 292.67 ?  190 LYS L C   1 
ATOM   9589  O O   . LYS D  3 190 ? 74.889  15.454  170.667 1.00 290.71 ?  190 LYS L O   1 
ATOM   9590  C CB  . LYS D  3 190 ? 77.353  13.473  169.592 1.00 296.82 ?  190 LYS L CB  1 
ATOM   9591  C CG  . LYS D  3 190 ? 78.003  12.753  168.442 1.00 298.69 ?  190 LYS L CG  1 
ATOM   9592  C CD  . LYS D  3 190 ? 78.439  11.378  168.922 1.00 301.03 ?  190 LYS L CD  1 
ATOM   9593  C CE  . LYS D  3 190 ? 79.275  10.667  167.884 1.00 303.17 ?  190 LYS L CE  1 
ATOM   9594  N NZ  . LYS D  3 190 ? 80.558  11.407  167.687 1.00 304.20 1  190 LYS L NZ  1 
ATOM   9595  N N   . SER D  3 191 ? 76.919  15.670  171.608 1.00 312.55 ?  191 SER L N   1 
ATOM   9596  C CA  . SER D  3 191 ? 76.383  16.112  172.885 1.00 306.87 ?  191 SER L CA  1 
ATOM   9597  C C   . SER D  3 191 ? 77.449  16.887  173.643 1.00 307.62 ?  191 SER L C   1 
ATOM   9598  O O   . SER D  3 191 ? 78.648  16.728  173.403 1.00 313.35 ?  191 SER L O   1 
ATOM   9599  C CB  . SER D  3 191 ? 75.902  14.924  173.732 1.00 303.66 ?  191 SER L CB  1 
ATOM   9600  O OG  . SER D  3 191 ? 75.254  13.938  172.946 1.00 302.43 ?  191 SER L OG  1 
ATOM   9601  N N   . TYR D  3 192 ? 76.987  17.743  174.547 1.00 310.25 ?  192 TYR L N   1 
ATOM   9602  C CA  . TYR D  3 192 ? 77.847  18.518  175.427 1.00 309.76 ?  192 TYR L CA  1 
ATOM   9603  C C   . TYR D  3 192 ? 77.610  18.030  176.849 1.00 306.68 ?  192 TYR L C   1 
ATOM   9604  O O   . TYR D  3 192 ? 76.521  17.559  177.183 1.00 303.13 ?  192 TYR L O   1 
ATOM   9605  C CB  . TYR D  3 192 ? 77.575  20.020  175.283 1.00 306.07 ?  192 TYR L CB  1 
ATOM   9606  C CG  . TYR D  3 192 ? 78.236  20.600  174.056 1.00 310.07 ?  192 TYR L CG  1 
ATOM   9607  C CD1 . TYR D  3 192 ? 77.603  20.587  172.817 1.00 310.58 ?  192 TYR L CD1 1 
ATOM   9608  C CD2 . TYR D  3 192 ? 79.498  21.165  174.141 1.00 312.79 ?  192 TYR L CD2 1 
ATOM   9609  C CE1 . TYR D  3 192 ? 78.227  21.111  171.697 1.00 311.00 ?  192 TYR L CE1 1 
ATOM   9610  C CE2 . TYR D  3 192 ? 80.120  21.694  173.037 1.00 316.57 ?  192 TYR L CE2 1 
ATOM   9611  C CZ  . TYR D  3 192 ? 79.485  21.664  171.819 1.00 314.04 ?  192 TYR L CZ  1 
ATOM   9612  O OH  . TYR D  3 192 ? 80.122  22.190  170.725 1.00 314.39 ?  192 TYR L OH  1 
ATOM   9613  N N   . SER D  3 193 ? 78.634  18.136  177.687 1.00 329.03 ?  193 SER L N   1 
ATOM   9614  C CA  . SER D  3 193 ? 78.555  17.655  179.059 1.00 320.58 ?  193 SER L CA  1 
ATOM   9615  C C   . SER D  3 193 ? 78.988  18.730  180.042 1.00 304.88 ?  193 SER L C   1 
ATOM   9616  O O   . SER D  3 193 ? 79.745  19.637  179.692 1.00 312.45 ?  193 SER L O   1 
ATOM   9617  C CB  . SER D  3 193 ? 79.438  16.419  179.245 1.00 317.21 ?  193 SER L CB  1 
ATOM   9618  O OG  . SER D  3 193 ? 79.094  15.399  178.324 1.00 320.85 ?  193 SER L OG  1 
ATOM   9619  N N   . CYS D  3 194 ? 78.488  18.637  181.276 1.00 312.80 ?  194 CYS L N   1 
ATOM   9620  C CA  . CYS D  3 194 ? 78.856  19.576  182.337 1.00 308.88 ?  194 CYS L CA  1 
ATOM   9621  C C   . CYS D  3 194 ? 79.396  18.769  183.530 1.00 309.32 ?  194 CYS L C   1 
ATOM   9622  O O   . CYS D  3 194 ? 78.624  18.334  184.388 1.00 300.08 ?  194 CYS L O   1 
ATOM   9623  C CB  . CYS D  3 194 ? 77.666  20.522  182.772 1.00 298.11 ?  194 CYS L CB  1 
ATOM   9624  S SG  . CYS D  3 194 ? 78.225  21.623  184.102 1.00 303.82 ?  194 CYS L SG  1 
ATOM   9625  N N   . GLN D  3 195 ? 80.717  18.541  183.575 1.00 302.06 ?  195 GLN L N   1 
ATOM   9626  C CA  . GLN D  3 195 ? 81.330  17.777  184.663 1.00 303.91 ?  195 GLN L CA  1 
ATOM   9627  C C   . GLN D  3 195 ? 81.671  18.738  185.796 1.00 299.82 ?  195 GLN L C   1 
ATOM   9628  O O   . GLN D  3 195 ? 82.518  19.624  185.629 1.00 301.94 ?  195 GLN L O   1 
ATOM   9629  C CB  . GLN D  3 195 ? 82.607  17.037  184.252 1.00 321.34 ?  195 GLN L CB  1 
ATOM   9630  C CG  . GLN D  3 195 ? 82.503  15.968  183.188 1.00 330.05 ?  195 GLN L CG  1 
ATOM   9631  C CD  . GLN D  3 195 ? 83.858  15.338  182.915 1.00 334.41 ?  195 GLN L CD  1 
ATOM   9632  O OE1 . GLN D  3 195 ? 84.860  15.722  183.519 1.00 339.04 ?  195 GLN L OE1 1 
ATOM   9633  N NE2 . GLN D  3 195 ? 83.895  14.364  182.013 1.00 333.99 ?  195 GLN L NE2 1 
ATOM   9634  N N   . VAL D  3 196 ? 81.011  18.568  186.939 1.00 315.88 ?  196 VAL L N   1 
ATOM   9635  C CA  . VAL D  3 196 ? 81.225  19.416  188.106 1.00 313.24 ?  196 VAL L CA  1 
ATOM   9636  C C   . VAL D  3 196 ? 81.994  18.624  189.157 1.00 312.06 ?  196 VAL L C   1 
ATOM   9637  O O   . VAL D  3 196 ? 81.507  17.604  189.661 1.00 309.38 ?  196 VAL L O   1 
ATOM   9638  C CB  . VAL D  3 196 ? 79.894  19.934  188.674 1.00 301.84 ?  196 VAL L CB  1 
ATOM   9639  C CG1 . VAL D  3 196 ? 80.135  20.760  189.924 1.00 283.84 ?  196 VAL L CG1 1 
ATOM   9640  C CG2 . VAL D  3 196 ? 79.133  20.743  187.623 1.00 290.32 ?  196 VAL L CG2 1 
ATOM   9641  N N   . THR D  3 197 ? 83.189  19.106  189.487 1.00 300.79 ?  197 THR L N   1 
ATOM   9642  C CA  . THR D  3 197 ? 84.074  18.495  190.474 1.00 307.22 ?  197 THR L CA  1 
ATOM   9643  C C   . THR D  3 197 ? 83.901  19.211  191.811 1.00 300.47 ?  197 THR L C   1 
ATOM   9644  O O   . THR D  3 197 ? 84.303  20.371  191.952 1.00 301.99 ?  197 THR L O   1 
ATOM   9645  C CB  . THR D  3 197 ? 85.527  18.548  190.015 1.00 315.14 ?  197 THR L CB  1 
ATOM   9646  O OG1 . THR D  3 197 ? 85.654  17.876  188.757 1.00 322.61 ?  197 THR L OG1 1 
ATOM   9647  C CG2 . THR D  3 197 ? 86.419  17.872  191.041 1.00 310.99 ?  197 THR L CG2 1 
ATOM   9648  N N   . HIS D  3 198 ? 83.309  18.526  192.788 1.00 307.59 ?  198 HIS L N   1 
ATOM   9649  C CA  . HIS D  3 198 ? 83.102  19.070  194.126 1.00 303.12 ?  198 HIS L CA  1 
ATOM   9650  C C   . HIS D  3 198 ? 83.803  18.182  195.143 1.00 320.84 ?  198 HIS L C   1 
ATOM   9651  O O   . HIS D  3 198 ? 83.536  16.976  195.200 1.00 329.56 ?  198 HIS L O   1 
ATOM   9652  C CB  . HIS D  3 198 ? 81.606  19.157  194.442 1.00 289.25 ?  198 HIS L CB  1 
ATOM   9653  C CG  . HIS D  3 198 ? 81.307  19.561  195.853 1.00 289.09 ?  198 HIS L CG  1 
ATOM   9654  N ND1 . HIS D  3 198 ? 80.719  18.709  196.763 1.00 289.77 ?  198 HIS L ND1 1 
ATOM   9655  C CD2 . HIS D  3 198 ? 81.530  20.721  196.513 1.00 287.96 ?  198 HIS L CD2 1 
ATOM   9656  C CE1 . HIS D  3 198 ? 80.583  19.331  197.920 1.00 286.67 ?  198 HIS L CE1 1 
ATOM   9657  N NE2 . HIS D  3 198 ? 81.069  20.553  197.796 1.00 285.02 ?  198 HIS L NE2 1 
ATOM   9658  N N   . GLU D  3 199 ? 84.694  18.779  195.944 1.00 295.59 ?  199 GLU L N   1 
ATOM   9659  C CA  . GLU D  3 199 ? 85.453  18.043  196.953 1.00 303.87 ?  199 GLU L CA  1 
ATOM   9660  C C   . GLU D  3 199 ? 86.215  16.889  196.320 1.00 315.94 ?  199 GLU L C   1 
ATOM   9661  O O   . GLU D  3 199 ? 87.339  17.056  195.837 1.00 326.98 ?  199 GLU L O   1 
ATOM   9662  C CB  . GLU D  3 199 ? 84.556  17.536  198.088 1.00 293.75 ?  199 GLU L CB  1 
ATOM   9663  C CG  . GLU D  3 199 ? 83.987  18.622  198.992 1.00 288.84 ?  199 GLU L CG  1 
ATOM   9664  C CD  . GLU D  3 199 ? 85.065  19.370  199.764 1.00 291.12 ?  199 GLU L CD  1 
ATOM   9665  O OE1 . GLU D  3 199 ? 85.574  18.815  200.761 1.00 293.49 ?  199 GLU L OE1 1 
ATOM   9666  O OE2 . GLU D  3 199 ? 85.395  20.513  199.383 1.00 290.70 -1 199 GLU L OE2 1 
ATOM   9667  N N   . GLY D  3 200 ? 85.591  15.714  196.315 1.00 309.98 ?  200 GLY L N   1 
ATOM   9668  C CA  . GLY D  3 200 ? 86.203  14.519  195.780 1.00 313.48 ?  200 GLY L CA  1 
ATOM   9669  C C   . GLY D  3 200 ? 85.406  13.840  194.686 1.00 306.05 ?  200 GLY L C   1 
ATOM   9670  O O   . GLY D  3 200 ? 85.943  12.987  193.974 1.00 312.85 ?  200 GLY L O   1 
ATOM   9671  N N   . SER D  3 201 ? 84.134  14.191  194.533 1.00 315.04 ?  201 SER L N   1 
ATOM   9672  C CA  . SER D  3 201 ? 83.308  13.555  193.520 1.00 306.17 ?  201 SER L CA  1 
ATOM   9673  C C   . SER D  3 201 ? 83.156  14.466  192.310 1.00 305.92 ?  201 SER L C   1 
ATOM   9674  O O   . SER D  3 201 ? 83.428  15.668  192.364 1.00 303.74 ?  201 SER L O   1 
ATOM   9675  C CB  . SER D  3 201 ? 81.926  13.215  194.085 1.00 300.23 ?  201 SER L CB  1 
ATOM   9676  O OG  . SER D  3 201 ? 81.264  14.386  194.534 1.00 286.08 ?  201 SER L OG  1 
ATOM   9677  N N   . THR D  3 202 ? 82.714  13.869  191.205 1.00 296.18 ?  202 THR L N   1 
ATOM   9678  C CA  . THR D  3 202 ? 82.505  14.600  189.960 1.00 296.60 ?  202 THR L CA  1 
ATOM   9679  C C   . THR D  3 202 ? 81.231  14.081  189.308 1.00 292.65 ?  202 THR L C   1 
ATOM   9680  O O   . THR D  3 202 ? 81.189  12.932  188.856 1.00 296.76 ?  202 THR L O   1 
ATOM   9681  C CB  . THR D  3 202 ? 83.703  14.440  189.025 1.00 304.83 ?  202 THR L CB  1 
ATOM   9682  O OG1 . THR D  3 202 ? 84.878  14.955  189.663 1.00 314.13 ?  202 THR L OG1 1 
ATOM   9683  C CG2 . THR D  3 202 ? 83.467  15.195  187.730 1.00 302.89 ?  202 THR L CG2 1 
ATOM   9684  N N   . VAL D  3 203 ? 80.201  14.921  189.266 1.00 308.74 ?  203 VAL L N   1 
ATOM   9685  C CA  . VAL D  3 203 ? 78.908  14.589  188.674 1.00 299.34 ?  203 VAL L CA  1 
ATOM   9686  C C   . VAL D  3 203 ? 78.886  15.099  187.240 1.00 307.40 ?  203 VAL L C   1 
ATOM   9687  O O   . VAL D  3 203 ? 79.308  16.231  186.971 1.00 310.66 ?  203 VAL L O   1 
ATOM   9688  C CB  . VAL D  3 203 ? 77.754  15.187  189.500 1.00 283.01 ?  203 VAL L CB  1 
ATOM   9689  C CG1 . VAL D  3 203 ? 76.409  14.720  188.962 1.00 277.33 ?  203 VAL L CG1 1 
ATOM   9690  C CG2 . VAL D  3 203 ? 77.914  14.834  190.977 1.00 276.06 ?  203 VAL L CG2 1 
ATOM   9691  N N   . GLU D  3 204 ? 78.408  14.272  186.309 1.00 287.77 ?  204 GLU L N   1 
ATOM   9692  C CA  . GLU D  3 204 ? 78.366  14.652  184.900 1.00 295.54 ?  204 GLU L CA  1 
ATOM   9693  C C   . GLU D  3 204 ? 76.957  14.477  184.342 1.00 289.25 ?  204 GLU L C   1 
ATOM   9694  O O   . GLU D  3 204 ? 76.381  13.387  184.428 1.00 285.13 ?  204 GLU L O   1 
ATOM   9695  C CB  . GLU D  3 204 ? 79.384  13.832  184.099 1.00 311.24 ?  204 GLU L CB  1 
ATOM   9696  C CG  . GLU D  3 204 ? 79.308  13.992  182.595 1.00 320.93 ?  204 GLU L CG  1 
ATOM   9697  C CD  . GLU D  3 204 ? 80.326  13.125  181.877 1.00 336.48 ?  204 GLU L CD  1 
ATOM   9698  O OE1 . GLU D  3 204 ? 81.215  12.567  182.556 1.00 347.13 ?  204 GLU L OE1 1 
ATOM   9699  O OE2 . GLU D  3 204 ? 80.249  13.016  180.636 1.00 335.62 -1 204 GLU L OE2 1 
ATOM   9700  N N   . LYS D  3 205 ? 76.411  15.555  183.772 1.00 289.97 ?  205 LYS L N   1 
ATOM   9701  C CA  . LYS D  3 205 ? 75.121  15.560  183.091 1.00 286.73 ?  205 LYS L CA  1 
ATOM   9702  C C   . LYS D  3 205 ? 75.338  16.079  181.671 1.00 289.26 ?  205 LYS L C   1 
ATOM   9703  O O   . LYS D  3 205 ? 76.096  17.035  181.464 1.00 290.31 ?  205 LYS L O   1 
ATOM   9704  C CB  . LYS D  3 205 ? 74.089  16.411  183.855 1.00 279.82 ?  205 LYS L CB  1 
ATOM   9705  C CG  . LYS D  3 205 ? 73.534  15.727  185.116 1.00 276.90 ?  205 LYS L CG  1 
ATOM   9706  C CD  . LYS D  3 205 ? 72.381  16.505  185.743 1.00 270.19 ?  205 LYS L CD  1 
ATOM   9707  C CE  . LYS D  3 205 ? 71.175  15.615  186.019 1.00 266.93 ?  205 LYS L CE  1 
ATOM   9708  N NZ  . LYS D  3 205 ? 71.104  15.190  187.448 1.00 264.78 1  205 LYS L NZ  1 
ATOM   9709  N N   . THR D  3 206 ? 74.672  15.457  180.699 1.00 286.99 ?  206 THR L N   1 
ATOM   9710  C CA  . THR D  3 206 ? 74.841  15.748  179.277 1.00 290.27 ?  206 THR L CA  1 
ATOM   9711  C C   . THR D  3 206 ? 73.598  16.405  178.668 1.00 286.40 ?  206 THR L C   1 
ATOM   9712  O O   . THR D  3 206 ? 72.579  16.615  179.335 1.00 281.24 ?  206 THR L O   1 
ATOM   9713  C CB  . THR D  3 206 ? 75.201  14.464  178.524 1.00 296.07 ?  206 THR L CB  1 
ATOM   9714  O OG1 . THR D  3 206 ? 74.099  13.552  178.575 1.00 294.31 ?  206 THR L OG1 1 
ATOM   9715  C CG2 . THR D  3 206 ? 76.417  13.801  179.159 1.00 300.17 ?  206 THR L CG2 1 
ATOM   9716  N N   . VAL D  3 207 ? 73.705  16.732  177.377 1.00 297.47 ?  207 VAL L N   1 
ATOM   9717  C CA  . VAL D  3 207 ? 72.623  17.354  176.610 1.00 295.35 ?  207 VAL L CA  1 
ATOM   9718  C C   . VAL D  3 207 ? 72.849  17.074  175.125 1.00 310.78 ?  207 VAL L C   1 
ATOM   9719  O O   . VAL D  3 207 ? 73.968  17.192  174.620 1.00 317.75 ?  207 VAL L O   1 
ATOM   9720  C CB  . VAL D  3 207 ? 72.538  18.875  176.890 1.00 279.37 ?  207 VAL L CB  1 
ATOM   9721  C CG1 . VAL D  3 207 ? 73.888  19.558  176.628 1.00 283.04 ?  207 VAL L CG1 1 
ATOM   9722  C CG2 . VAL D  3 207 ? 71.429  19.512  176.058 1.00 275.17 ?  207 VAL L CG2 1 
ATOM   9723  N N   . ALA D  3 208 ? 71.765  16.716  174.427 1.00 300.64 ?  208 ALA L N   1 
ATOM   9724  C CA  . ALA D  3 208 ? 71.756  16.370  173.010 1.00 302.28 ?  208 ALA L CA  1 
ATOM   9725  C C   . ALA D  3 208 ? 70.728  17.198  172.249 1.00 298.44 ?  208 ALA L C   1 
ATOM   9726  O O   . ALA D  3 208 ? 69.621  17.427  172.751 1.00 291.31 ?  208 ALA L O   1 
ATOM   9727  C CB  . ALA D  3 208 ? 71.455  14.879  172.803 1.00 302.40 ?  208 ALA L CB  1 
ATOM   9728  N N   . PRO D  3 209 ? 71.060  17.663  171.046 1.00 303.09 ?  209 PRO L N   1 
ATOM   9729  C CA  . PRO D  3 209 ? 70.088  18.426  170.254 1.00 304.56 ?  209 PRO L CA  1 
ATOM   9730  C C   . PRO D  3 209 ? 68.910  17.552  169.845 1.00 309.19 ?  209 PRO L C   1 
ATOM   9731  O O   . PRO D  3 209 ? 68.930  16.324  169.958 1.00 311.51 ?  209 PRO L O   1 
ATOM   9732  C CB  . PRO D  3 209 ? 70.895  18.882  169.033 1.00 306.78 ?  209 PRO L CB  1 
ATOM   9733  C CG  . PRO D  3 209 ? 72.329  18.783  169.461 1.00 306.90 ?  209 PRO L CG  1 
ATOM   9734  C CD  . PRO D  3 209 ? 72.379  17.613  170.394 1.00 308.09 ?  209 PRO L CD  1 
ATOM   9735  N N   . THR D  3 210 ? 67.865  18.211  169.352 1.00 312.87 ?  210 THR L N   1 
ATOM   9736  C CA  . THR D  3 210 ? 66.657  17.511  168.923 1.00 309.74 ?  210 THR L CA  1 
ATOM   9737  C C   . THR D  3 210 ? 66.365  17.724  167.438 1.00 310.87 ?  210 THR L C   1 
ATOM   9738  O O   . THR D  3 210 ? 66.858  18.668  166.819 1.00 309.75 ?  210 THR L O   1 
ATOM   9739  C CB  . THR D  3 210 ? 65.426  17.957  169.737 1.00 293.88 ?  210 THR L CB  1 
ATOM   9740  O OG1 . THR D  3 210 ? 65.657  17.722  171.132 1.00 288.48 ?  210 THR L OG1 1 
ATOM   9741  C CG2 . THR D  3 210 ? 64.195  17.184  169.295 1.00 287.96 ?  210 THR L CG2 1 
ATOM   9742  N N   . GLN E  4 1   ? 22.158  35.460  166.758 1.00 183.02 ?  1   GLN E N   1 
ATOM   9743  C CA  . GLN E  4 1   ? 22.315  34.034  167.040 1.00 179.31 ?  1   GLN E CA  1 
ATOM   9744  C C   . GLN E  4 1   ? 23.130  33.321  165.959 1.00 178.67 ?  1   GLN E C   1 
ATOM   9745  O O   . GLN E  4 1   ? 23.832  32.359  166.254 1.00 176.45 ?  1   GLN E O   1 
ATOM   9746  C CB  . GLN E  4 1   ? 20.974  33.314  167.170 1.00 183.88 ?  1   GLN E CB  1 
ATOM   9747  C CG  . GLN E  4 1   ? 19.888  34.057  167.989 1.00 189.69 ?  1   GLN E CG  1 
ATOM   9748  C CD  . GLN E  4 1   ? 19.599  35.540  167.539 1.00 198.55 ?  1   GLN E CD  1 
ATOM   9749  O OE1 . GLN E  4 1   ? 19.672  35.838  166.401 1.00 206.71 ?  1   GLN E OE1 1 
ATOM   9750  N NE2 . GLN E  4 1   ? 19.263  36.357  168.435 1.00 192.58 ?  1   GLN E NE2 1 
ATOM   9751  N N   . GLU E  4 2   ? 23.024  33.747  164.697 1.00 149.45 ?  2   GLU E N   1 
ATOM   9752  C CA  . GLU E  4 2   ? 23.625  33.000  163.595 1.00 148.90 ?  2   GLU E CA  1 
ATOM   9753  C C   . GLU E  4 2   ? 25.056  33.498  163.441 1.00 145.45 ?  2   GLU E C   1 
ATOM   9754  O O   . GLU E  4 2   ? 25.290  34.625  163.002 1.00 146.92 ?  2   GLU E O   1 
ATOM   9755  C CB  . GLU E  4 2   ? 22.829  33.232  162.314 1.00 154.07 ?  2   GLU E CB  1 
ATOM   9756  C CG  . GLU E  4 2   ? 21.342  32.974  162.467 1.00 159.35 ?  2   GLU E CG  1 
ATOM   9757  C CD  . GLU E  4 2   ? 20.618  32.973  161.146 1.00 164.97 ?  2   GLU E CD  1 
ATOM   9758  O OE1 . GLU E  4 2   ? 19.509  33.542  161.081 1.00 169.41 ?  2   GLU E OE1 1 
ATOM   9759  O OE2 . GLU E  4 2   ? 21.158  32.404  160.177 1.00 165.42 -1 2   GLU E OE2 1 
ATOM   9760  N N   . VAL E  4 3   ? 26.012  32.647  163.825 1.00 141.08 ?  3   VAL E N   1 
ATOM   9761  C CA  . VAL E  4 3   ? 27.411  33.026  163.947 1.00 139.51 ?  3   VAL E CA  1 
ATOM   9762  C C   . VAL E  4 3   ? 28.291  31.857  163.531 1.00 138.49 ?  3   VAL E C   1 
ATOM   9763  O O   . VAL E  4 3   ? 27.890  30.691  163.582 1.00 138.54 ?  3   VAL E O   1 
ATOM   9764  C CB  . VAL E  4 3   ? 27.786  33.475  165.380 1.00 139.43 ?  3   VAL E CB  1 
ATOM   9765  C CG1 . VAL E  4 3   ? 26.976  34.686  165.806 1.00 140.61 ?  3   VAL E CG1 1 
ATOM   9766  C CG2 . VAL E  4 3   ? 27.591  32.334  166.370 1.00 139.35 ?  3   VAL E CG2 1 
ATOM   9767  N N   . LEU E  4 4   ? 29.507  32.191  163.119 1.00 145.95 ?  4   LEU E N   1 
ATOM   9768  C CA  . LEU E  4 4   ? 30.553  31.224  162.829 1.00 144.85 ?  4   LEU E CA  1 
ATOM   9769  C C   . LEU E  4 4   ? 31.730  31.559  163.732 1.00 142.22 ?  4   LEU E C   1 
ATOM   9770  O O   . LEU E  4 4   ? 32.165  32.714  163.785 1.00 141.03 ?  4   LEU E O   1 
ATOM   9771  C CB  . LEU E  4 4   ? 30.958  31.248  161.353 1.00 145.49 ?  4   LEU E CB  1 
ATOM   9772  C CG  . LEU E  4 4   ? 29.878  30.817  160.354 1.00 148.20 ?  4   LEU E CG  1 
ATOM   9773  C CD1 . LEU E  4 4   ? 30.242  31.244  158.940 1.00 148.64 ?  4   LEU E CD1 1 
ATOM   9774  C CD2 . LEU E  4 4   ? 29.654  29.316  160.422 1.00 148.98 ?  4   LEU E CD2 1 
ATOM   9775  N N   . VAL E  4 5   ? 32.224  30.561  164.459 1.00 147.40 ?  5   VAL E N   1 
ATOM   9776  C CA  . VAL E  4 5   ? 33.348  30.733  165.371 1.00 145.37 ?  5   VAL E CA  1 
ATOM   9777  C C   . VAL E  4 5   ? 34.530  29.933  164.847 1.00 145.82 ?  5   VAL E C   1 
ATOM   9778  O O   . VAL E  4 5   ? 34.423  28.720  164.626 1.00 147.28 ?  5   VAL E O   1 
ATOM   9779  C CB  . VAL E  4 5   ? 32.981  30.288  166.795 1.00 144.68 ?  5   VAL E CB  1 
ATOM   9780  C CG1 . VAL E  4 5   ? 34.131  30.555  167.749 1.00 142.83 ?  5   VAL E CG1 1 
ATOM   9781  C CG2 . VAL E  4 5   ? 31.708  30.980  167.261 1.00 144.44 ?  5   VAL E CG2 1 
ATOM   9782  N N   . GLN E  4 6   ? 35.656  30.614  164.659 1.00 148.69 ?  6   GLN E N   1 
ATOM   9783  C CA  . GLN E  4 6   ? 36.854  30.046  164.064 1.00 149.77 ?  6   GLN E CA  1 
ATOM   9784  C C   . GLN E  4 6   ? 37.915  29.779  165.125 1.00 149.48 ?  6   GLN E C   1 
ATOM   9785  O O   . GLN E  4 6   ? 37.918  30.380  166.203 1.00 147.69 ?  6   GLN E O   1 
ATOM   9786  C CB  . GLN E  4 6   ? 37.414  30.973  162.983 1.00 149.79 ?  6   GLN E CB  1 
ATOM   9787  C CG  . GLN E  4 6   ? 36.475  31.169  161.810 1.00 150.37 ?  6   GLN E CG  1 
ATOM   9788  C CD  . GLN E  4 6   ? 37.093  32.001  160.711 1.00 150.60 ?  6   GLN E CD  1 
ATOM   9789  O OE1 . GLN E  4 6   ? 36.498  32.970  160.239 1.00 150.38 ?  6   GLN E OE1 1 
ATOM   9790  N NE2 . GLN E  4 6   ? 38.295  31.624  160.292 1.00 151.52 ?  6   GLN E NE2 1 
ATOM   9791  N N   . SER E  4 7   ? 38.820  28.859  164.801 1.00 146.83 ?  7   SER E N   1 
ATOM   9792  C CA  . SER E  4 7   ? 39.929  28.539  165.685 1.00 147.41 ?  7   SER E CA  1 
ATOM   9793  C C   . SER E  4 7   ? 40.899  29.712  165.786 1.00 146.43 ?  7   SER E C   1 
ATOM   9794  O O   . SER E  4 7   ? 40.872  30.655  164.989 1.00 145.86 ?  7   SER E O   1 
ATOM   9795  C CB  . SER E  4 7   ? 40.667  27.294  165.194 1.00 150.17 ?  7   SER E CB  1 
ATOM   9796  O OG  . SER E  4 7   ? 41.044  27.436  163.841 1.00 151.03 ?  7   SER E OG  1 
ATOM   9797  N N   . GLY E  4 8   ? 41.756  29.649  166.798 1.00 156.04 ?  8   GLY E N   1 
ATOM   9798  C CA  . GLY E  4 8   ? 42.642  30.753  167.092 1.00 155.18 ?  8   GLY E CA  1 
ATOM   9799  C C   . GLY E  4 8   ? 43.792  30.859  166.111 1.00 157.57 ?  8   GLY E C   1 
ATOM   9800  O O   . GLY E  4 8   ? 44.045  29.980  165.286 1.00 159.90 ?  8   GLY E O   1 
ATOM   9801  N N   . ALA E  4 9   ? 44.517  31.967  166.238 1.00 168.47 ?  9   ALA E N   1 
ATOM   9802  C CA  . ALA E  4 9   ? 45.642  32.256  165.360 1.00 171.07 ?  9   ALA E CA  1 
ATOM   9803  C C   . ALA E  4 9   ? 46.663  31.121  165.380 1.00 174.66 ?  9   ALA E C   1 
ATOM   9804  O O   . ALA E  4 9   ? 46.836  30.428  166.386 1.00 175.16 ?  9   ALA E O   1 
ATOM   9805  C CB  . ALA E  4 9   ? 46.302  33.572  165.769 1.00 170.35 ?  9   ALA E CB  1 
ATOM   9806  N N   . GLU E  4 10  ? 47.348  30.936  164.247 1.00 169.76 ?  10  GLU E N   1 
ATOM   9807  C CA  . GLU E  4 10  ? 48.346  29.882  164.117 1.00 173.52 ?  10  GLU E CA  1 
ATOM   9808  C C   . GLU E  4 10  ? 49.596  30.413  163.422 1.00 176.79 ?  10  GLU E C   1 
ATOM   9809  O O   . GLU E  4 10  ? 49.524  31.305  162.573 1.00 176.65 ?  10  GLU E O   1 
ATOM   9810  C CB  . GLU E  4 10  ? 47.767  28.703  163.320 1.00 174.33 ?  10  GLU E CB  1 
ATOM   9811  C CG  . GLU E  4 10  ? 46.554  28.052  163.975 1.00 172.04 ?  10  GLU E CG  1 
ATOM   9812  C CD  . GLU E  4 10  ? 46.510  26.550  163.794 1.00 174.21 ?  10  GLU E CD  1 
ATOM   9813  O OE1 . GLU E  4 10  ? 47.584  25.933  163.638 1.00 176.99 ?  10  GLU E OE1 1 
ATOM   9814  O OE2 . GLU E  4 10  ? 45.394  25.987  163.797 1.00 172.74 -1 10  GLU E OE2 1 
ATOM   9815  N N   . VAL E  4 11  ? 50.744  29.841  163.788 1.00 182.09 ?  11  VAL E N   1 
ATOM   9816  C CA  . VAL E  4 11  ? 52.012  30.045  163.093 1.00 185.43 ?  11  VAL E CA  1 
ATOM   9817  C C   . VAL E  4 11  ? 52.492  28.699  162.565 1.00 188.60 ?  11  VAL E C   1 
ATOM   9818  O O   . VAL E  4 11  ? 52.462  27.699  163.293 1.00 189.51 ?  11  VAL E O   1 
ATOM   9819  C CB  . VAL E  4 11  ? 53.065  30.685  164.017 1.00 187.80 ?  11  VAL E CB  1 
ATOM   9820  C CG1 . VAL E  4 11  ? 54.433  30.683  163.354 1.00 194.37 ?  11  VAL E CG1 1 
ATOM   9821  C CG2 . VAL E  4 11  ? 52.645  32.099  164.408 1.00 185.86 ?  11  VAL E CG2 1 
ATOM   9822  N N   . LYS E  4 12  ? 52.944  28.674  161.310 1.00 196.00 ?  12  LYS E N   1 
ATOM   9823  C CA  . LYS E  4 12  ? 53.589  27.496  160.745 1.00 199.41 ?  12  LYS E CA  1 
ATOM   9824  C C   . LYS E  4 12  ? 54.800  27.916  159.917 1.00 203.76 ?  12  LYS E C   1 
ATOM   9825  O O   . LYS E  4 12  ? 54.885  29.048  159.436 1.00 204.13 ?  12  LYS E O   1 
ATOM   9826  C CB  . LYS E  4 12  ? 52.607  26.688  159.886 1.00 198.48 ?  12  LYS E CB  1 
ATOM   9827  C CG  . LYS E  4 12  ? 51.551  25.947  160.700 1.00 194.89 ?  12  LYS E CG  1 
ATOM   9828  C CD  . LYS E  4 12  ? 52.116  24.827  161.556 1.00 197.15 ?  12  LYS E CD  1 
ATOM   9829  C CE  . LYS E  4 12  ? 50.983  24.028  162.189 1.00 196.41 ?  12  LYS E CE  1 
ATOM   9830  N NZ  . LYS E  4 12  ? 51.476  22.940  163.076 1.00 197.95 1  12  LYS E NZ  1 
ATOM   9831  N N   . LYS E  4 13  ? 55.747  26.987  159.762 1.00 197.83 ?  13  LYS E N   1 
ATOM   9832  C CA  . LYS E  4 13  ? 56.914  27.215  158.921 1.00 202.44 ?  13  LYS E CA  1 
ATOM   9833  C C   . LYS E  4 13  ? 56.605  26.892  157.459 1.00 203.21 ?  13  LYS E C   1 
ATOM   9834  O O   . LYS E  4 13  ? 55.670  26.145  157.164 1.00 200.70 ?  13  LYS E O   1 
ATOM   9835  C CB  . LYS E  4 13  ? 58.086  26.363  159.403 1.00 206.02 ?  13  LYS E CB  1 
ATOM   9836  C CG  . LYS E  4 13  ? 57.920  24.872  159.157 1.00 206.22 ?  13  LYS E CG  1 
ATOM   9837  C CD  . LYS E  4 13  ? 58.937  24.064  159.945 1.00 208.90 ?  13  LYS E CD  1 
ATOM   9838  C CE  . LYS E  4 13  ? 58.849  22.587  159.597 1.00 209.57 ?  13  LYS E CE  1 
ATOM   9839  N NZ  . LYS E  4 13  ? 59.589  21.741  160.571 1.00 211.31 1  13  LYS E NZ  1 
ATOM   9840  N N   . PRO E  4 14  ? 57.372  27.458  156.522 1.00 192.96 ?  14  PRO E N   1 
ATOM   9841  C CA  . PRO E  4 14  ? 57.154  27.142  155.102 1.00 194.23 ?  14  PRO E CA  1 
ATOM   9842  C C   . PRO E  4 14  ? 57.246  25.651  154.810 1.00 195.08 ?  14  PRO E C   1 
ATOM   9843  O O   . PRO E  4 14  ? 58.093  24.936  155.350 1.00 197.26 ?  14  PRO E O   1 
ATOM   9844  C CB  . PRO E  4 14  ? 58.264  27.924  154.391 1.00 198.97 ?  14  PRO E CB  1 
ATOM   9845  C CG  . PRO E  4 14  ? 58.589  29.037  155.319 1.00 198.64 ?  14  PRO E CG  1 
ATOM   9846  C CD  . PRO E  4 14  ? 58.390  28.507  156.705 1.00 196.00 ?  14  PRO E CD  1 
ATOM   9847  N N   . GLY E  4 15  ? 56.360  25.193  153.927 1.00 196.20 ?  15  GLY E N   1 
ATOM   9848  C CA  . GLY E  4 15  ? 56.307  23.814  153.509 1.00 196.69 ?  15  GLY E CA  1 
ATOM   9849  C C   . GLY E  4 15  ? 55.378  22.945  154.329 1.00 192.90 ?  15  GLY E C   1 
ATOM   9850  O O   . GLY E  4 15  ? 54.984  21.870  153.863 1.00 192.46 ?  15  GLY E O   1 
ATOM   9851  N N   . ALA E  4 16  ? 55.019  23.383  155.533 1.00 201.41 ?  16  ALA E N   1 
ATOM   9852  C CA  . ALA E  4 16  ? 54.151  22.638  156.436 1.00 198.09 ?  16  ALA E CA  1 
ATOM   9853  C C   . ALA E  4 16  ? 52.684  22.848  156.051 1.00 194.35 ?  16  ALA E C   1 
ATOM   9854  O O   . ALA E  4 16  ? 52.363  23.467  155.032 1.00 194.40 ?  16  ALA E O   1 
ATOM   9855  C CB  . ALA E  4 16  ? 54.434  23.038  157.882 1.00 197.38 ?  16  ALA E CB  1 
ATOM   9856  N N   . SER E  4 17  ? 51.775  22.308  156.864 1.00 196.76 ?  17  SER E N   1 
ATOM   9857  C CA  . SER E  4 17  ? 50.339  22.445  156.665 1.00 193.30 ?  17  SER E CA  1 
ATOM   9858  C C   . SER E  4 17  ? 49.687  22.997  157.925 1.00 190.26 ?  17  SER E C   1 
ATOM   9859  O O   . SER E  4 17  ? 50.167  22.780  159.041 1.00 190.54 ?  17  SER E O   1 
ATOM   9860  C CB  . SER E  4 17  ? 49.692  21.104  156.302 1.00 192.78 ?  17  SER E CB  1 
ATOM   9861  O OG  . SER E  4 17  ? 50.256  20.585  155.114 1.00 195.40 ?  17  SER E OG  1 
ATOM   9862  N N   . VAL E  4 18  ? 48.597  23.736  157.729 1.00 191.01 ?  18  VAL E N   1 
ATOM   9863  C CA  . VAL E  4 18  ? 47.792  24.273  158.818 1.00 187.93 ?  18  VAL E CA  1 
ATOM   9864  C C   . VAL E  4 18  ? 46.347  23.839  158.605 1.00 185.36 ?  18  VAL E C   1 
ATOM   9865  O O   . VAL E  4 18  ? 45.854  23.819  157.471 1.00 185.14 ?  18  VAL E O   1 
ATOM   9866  C CB  . VAL E  4 18  ? 47.914  25.813  158.918 1.00 186.81 ?  18  VAL E CB  1 
ATOM   9867  C CG1 . VAL E  4 18  ? 47.322  26.501  157.691 1.00 185.92 ?  18  VAL E CG1 1 
ATOM   9868  C CG2 . VAL E  4 18  ? 47.261  26.322  160.194 1.00 183.84 ?  18  VAL E CG2 1 
ATOM   9869  N N   . LYS E  4 19  ? 45.675  23.469  159.694 1.00 173.17 ?  19  LYS E N   1 
ATOM   9870  C CA  . LYS E  4 19  ? 44.264  23.102  159.672 1.00 171.15 ?  19  LYS E CA  1 
ATOM   9871  C C   . LYS E  4 19  ? 43.530  24.092  160.555 1.00 168.48 ?  19  LYS E C   1 
ATOM   9872  O O   . LYS E  4 19  ? 43.810  24.189  161.754 1.00 168.29 ?  19  LYS E O   1 
ATOM   9873  C CB  . LYS E  4 19  ? 44.040  21.675  160.177 1.00 171.97 ?  19  LYS E CB  1 
ATOM   9874  C CG  . LYS E  4 19  ? 42.594  21.215  160.075 1.00 170.52 ?  19  LYS E CG  1 
ATOM   9875  C CD  . LYS E  4 19  ? 42.402  19.821  160.637 1.00 172.41 ?  19  LYS E CD  1 
ATOM   9876  C CE  . LYS E  4 19  ? 42.126  18.831  159.523 1.00 175.19 ?  19  LYS E CE  1 
ATOM   9877  N NZ  . LYS E  4 19  ? 40.989  17.932  159.849 1.00 178.44 1  19  LYS E NZ  1 
ATOM   9878  N N   . VAL E  4 20  ? 42.591  24.815  159.972 1.00 165.41 ?  20  VAL E N   1 
ATOM   9879  C CA  . VAL E  4 20  ? 41.824  25.787  160.727 1.00 162.87 ?  20  VAL E CA  1 
ATOM   9880  C C   . VAL E  4 20  ? 40.367  25.322  160.751 1.00 161.86 ?  20  VAL E C   1 
ATOM   9881  O O   . VAL E  4 20  ? 39.892  24.709  159.789 1.00 162.50 ?  20  VAL E O   1 
ATOM   9882  C CB  . VAL E  4 20  ? 42.051  27.173  160.072 1.00 161.58 ?  20  VAL E CB  1 
ATOM   9883  C CG1 . VAL E  4 20  ? 41.537  27.202  158.650 1.00 161.61 ?  20  VAL E CG1 1 
ATOM   9884  C CG2 . VAL E  4 20  ? 41.522  28.315  160.917 1.00 162.00 ?  20  VAL E CG2 1 
ATOM   9885  N N   . SER E  4 21  ? 39.651  25.605  161.848 1.00 153.29 ?  21  SER E N   1 
ATOM   9886  C CA  . SER E  4 21  ? 38.266  25.158  161.975 1.00 152.92 ?  21  SER E CA  1 
ATOM   9887  C C   . SER E  4 21  ? 37.276  26.307  162.138 1.00 150.84 ?  21  SER E C   1 
ATOM   9888  O O   . SER E  4 21  ? 37.622  27.407  162.579 1.00 149.34 ?  21  SER E O   1 
ATOM   9889  C CB  . SER E  4 21  ? 38.096  24.189  163.160 1.00 153.75 ?  21  SER E CB  1 
ATOM   9890  O OG  . SER E  4 21  ? 38.341  24.826  164.403 1.00 152.49 ?  21  SER E OG  1 
ATOM   9891  N N   . CYS E  4 22  ? 36.024  26.013  161.773 1.00 153.65 ?  22  CYS E N   1 
ATOM   9892  C CA  . CYS E  4 22  ? 34.917  26.968  161.803 1.00 152.57 ?  22  CYS E CA  1 
ATOM   9893  C C   . CYS E  4 22  ? 33.636  26.244  162.214 1.00 153.53 ?  22  CYS E C   1 
ATOM   9894  O O   . CYS E  4 22  ? 33.169  25.361  161.487 1.00 154.80 ?  22  CYS E O   1 
ATOM   9895  C CB  . CYS E  4 22  ? 34.781  27.632  160.422 1.00 152.41 ?  22  CYS E CB  1 
ATOM   9896  S SG  . CYS E  4 22  ? 33.266  28.558  160.034 1.00 152.64 ?  22  CYS E SG  1 
ATOM   9897  N N   . ARG E  4 23  ? 33.053  26.605  163.359 1.00 145.46 ?  23  ARG E N   1 
ATOM   9898  C CA  . ARG E  4 23  ? 31.852  25.935  163.853 1.00 146.73 ?  23  ARG E CA  1 
ATOM   9899  C C   . ARG E  4 23  ? 30.649  26.866  163.755 1.00 146.90 ?  23  ARG E C   1 
ATOM   9900  O O   . ARG E  4 23  ? 30.722  28.036  164.147 1.00 145.37 ?  23  ARG E O   1 
ATOM   9901  C CB  . ARG E  4 23  ? 32.023  25.451  165.297 1.00 146.49 ?  23  ARG E CB  1 
ATOM   9902  C CG  . ARG E  4 23  ? 30.777  24.749  165.839 1.00 148.18 ?  23  ARG E CG  1 
ATOM   9903  C CD  . ARG E  4 23  ? 31.030  23.997  167.136 1.00 148.66 ?  23  ARG E CD  1 
ATOM   9904  N NE  . ARG E  4 23  ? 29.839  23.264  167.568 1.00 150.31 ?  23  ARG E NE  1 
ATOM   9905  C CZ  . ARG E  4 23  ? 29.861  22.127  168.257 1.00 151.70 ?  23  ARG E CZ  1 
ATOM   9906  N NH1 . ARG E  4 23  ? 28.725  21.520  168.575 1.00 153.23 1  23  ARG E NH1 1 
ATOM   9907  N NH2 . ARG E  4 23  ? 31.018  21.591  168.622 1.00 151.87 ?  23  ARG E NH2 1 
ATOM   9908  N N   . ALA E  4 24  ? 29.546  26.331  163.236 1.00 140.79 ?  24  ALA E N   1 
ATOM   9909  C CA  . ALA E  4 24  ? 28.314  27.075  163.009 1.00 141.64 ?  24  ALA E CA  1 
ATOM   9910  C C   . ALA E  4 24  ? 27.399  26.969  164.222 1.00 142.27 ?  24  ALA E C   1 
ATOM   9911  O O   . ALA E  4 24  ? 27.173  25.870  164.739 1.00 142.38 ?  24  ALA E O   1 
ATOM   9912  C CB  . ALA E  4 24  ? 27.603  26.548  161.763 1.00 142.24 ?  24  ALA E CB  1 
ATOM   9913  N N   . PHE E  4 25  ? 26.871  28.109  164.669 1.00 135.79 ?  25  PHE E N   1 
ATOM   9914  C CA  . PHE E  4 25  ? 25.888  28.144  165.742 1.00 136.74 ?  25  PHE E CA  1 
ATOM   9915  C C   . PHE E  4 25  ? 24.646  28.897  165.286 1.00 138.08 ?  25  PHE E C   1 
ATOM   9916  O O   . PHE E  4 25  ? 24.729  29.828  164.479 1.00 138.12 ?  25  PHE E O   1 
ATOM   9917  C CB  . PHE E  4 25  ? 26.450  28.814  167.006 1.00 136.45 ?  25  PHE E CB  1 
ATOM   9918  C CG  . PHE E  4 25  ? 27.627  28.102  167.587 1.00 135.36 ?  25  PHE E CG  1 
ATOM   9919  C CD1 . PHE E  4 25  ? 27.459  27.221  168.637 1.00 135.53 ?  25  PHE E CD1 1 
ATOM   9920  C CD2 . PHE E  4 25  ? 28.906  28.342  167.116 1.00 134.37 ?  25  PHE E CD2 1 
ATOM   9921  C CE1 . PHE E  4 25  ? 28.535  26.559  169.179 1.00 134.67 ?  25  PHE E CE1 1 
ATOM   9922  C CE2 . PHE E  4 25  ? 29.989  27.686  167.658 1.00 133.63 ?  25  PHE E CE2 1 
ATOM   9923  C CZ  . PHE E  4 25  ? 29.803  26.795  168.694 1.00 133.76 ?  25  PHE E CZ  1 
ATOM   9924  N N   . GLY E  4 26  ? 23.491  28.488  165.814 1.00 148.08 ?  26  GLY E N   1 
ATOM   9925  C CA  . GLY E  4 26  ? 22.272  29.250  165.631 1.00 150.33 ?  26  GLY E CA  1 
ATOM   9926  C C   . GLY E  4 26  ? 21.565  29.032  164.315 1.00 155.96 ?  26  GLY E C   1 
ATOM   9927  O O   . GLY E  4 26  ? 20.598  29.746  164.026 1.00 159.32 ?  26  GLY E O   1 
ATOM   9928  N N   . TYR E  4 27  ? 21.998  28.058  163.518 1.00 155.42 ?  27  TYR E N   1 
ATOM   9929  C CA  . TYR E  4 27  ? 21.294  27.683  162.300 1.00 158.73 ?  27  TYR E CA  1 
ATOM   9930  C C   . TYR E  4 27  ? 21.679  26.255  161.951 1.00 158.18 ?  27  TYR E C   1 
ATOM   9931  O O   . TYR E  4 27  ? 22.526  25.641  162.605 1.00 156.37 ?  27  TYR E O   1 
ATOM   9932  C CB  . TYR E  4 27  ? 21.608  28.633  161.136 1.00 160.73 ?  27  TYR E CB  1 
ATOM   9933  C CG  . TYR E  4 27  ? 22.969  28.431  160.497 1.00 156.59 ?  27  TYR E CG  1 
ATOM   9934  C CD1 . TYR E  4 27  ? 24.121  28.977  161.051 1.00 153.44 ?  27  TYR E CD1 1 
ATOM   9935  C CD2 . TYR E  4 27  ? 23.093  27.712  159.316 1.00 157.02 ?  27  TYR E CD2 1 
ATOM   9936  C CE1 . TYR E  4 27  ? 25.362  28.792  160.451 1.00 150.38 ?  27  TYR E CE1 1 
ATOM   9937  C CE2 . TYR E  4 27  ? 24.324  27.519  158.713 1.00 154.35 ?  27  TYR E CE2 1 
ATOM   9938  C CZ  . TYR E  4 27  ? 25.455  28.060  159.283 1.00 150.76 ?  27  TYR E CZ  1 
ATOM   9939  O OH  . TYR E  4 27  ? 26.678  27.868  158.677 1.00 148.38 ?  27  TYR E OH  1 
ATOM   9940  N N   . THR E  4 28  ? 21.033  25.724  160.916 1.00 157.08 ?  28  THR E N   1 
ATOM   9941  C CA  . THR E  4 28  ? 21.292  24.351  160.506 1.00 156.47 ?  28  THR E CA  1 
ATOM   9942  C C   . THR E  4 28  ? 22.534  24.361  159.626 1.00 154.49 ?  28  THR E C   1 
ATOM   9943  O O   . THR E  4 28  ? 22.519  24.901  158.515 1.00 155.92 ?  28  THR E O   1 
ATOM   9944  C CB  . THR E  4 28  ? 20.089  23.784  159.757 1.00 159.96 ?  28  THR E CB  1 
ATOM   9945  O OG1 . THR E  4 28  ? 18.947  23.757  160.623 1.00 161.76 ?  28  THR E OG1 1 
ATOM   9946  C CG2 . THR E  4 28  ? 20.385  22.383  159.275 1.00 159.08 ?  28  THR E CG2 1 
ATOM   9947  N N   . PHE E  4 29  ? 23.604  23.745  160.136 1.00 160.51 ?  29  PHE E N   1 
ATOM   9948  C CA  . PHE E  4 29  ? 24.903  23.757  159.469 1.00 158.28 ?  29  PHE E CA  1 
ATOM   9949  C C   . PHE E  4 29  ? 24.822  23.268  158.028 1.00 159.56 ?  29  PHE E C   1 
ATOM   9950  O O   . PHE E  4 29  ? 25.495  23.805  157.141 1.00 158.54 ?  29  PHE E O   1 
ATOM   9951  C CB  . PHE E  4 29  ? 25.882  22.906  160.278 1.00 156.13 ?  29  PHE E CB  1 
ATOM   9952  C CG  . PHE E  4 29  ? 27.229  22.764  159.647 1.00 154.31 ?  29  PHE E CG  1 
ATOM   9953  C CD1 . PHE E  4 29  ? 28.021  23.874  159.409 1.00 152.52 ?  29  PHE E CD1 1 
ATOM   9954  C CD2 . PHE E  4 29  ? 27.705  21.516  159.289 1.00 154.54 ?  29  PHE E CD2 1 
ATOM   9955  C CE1 . PHE E  4 29  ? 29.267  23.740  158.826 1.00 151.06 ?  29  PHE E CE1 1 
ATOM   9956  C CE2 . PHE E  4 29  ? 28.947  21.374  158.706 1.00 153.26 ?  29  PHE E CE2 1 
ATOM   9957  C CZ  . PHE E  4 29  ? 29.730  22.487  158.473 1.00 151.54 ?  29  PHE E CZ  1 
ATOM   9958  N N   . THR E  4 30  ? 23.998  22.258  157.777 1.00 167.61 ?  30  THR E N   1 
ATOM   9959  C CA  . THR E  4 30  ? 23.897  21.637  156.463 1.00 168.45 ?  30  THR E CA  1 
ATOM   9960  C C   . THR E  4 30  ? 22.983  22.386  155.503 1.00 172.14 ?  30  THR E C   1 
ATOM   9961  O O   . THR E  4 30  ? 22.767  21.908  154.384 1.00 174.32 ?  30  THR E O   1 
ATOM   9962  C CB  . THR E  4 30  ? 23.403  20.202  156.618 1.00 170.20 ?  30  THR E CB  1 
ATOM   9963  O OG1 . THR E  4 30  ? 22.221  20.200  157.428 1.00 173.06 ?  30  THR E OG1 1 
ATOM   9964  C CG2 . THR E  4 30  ? 24.468  19.368  157.300 1.00 168.08 ?  30  THR E CG2 1 
ATOM   9965  N N   . GLY E  4 31  ? 22.444  23.532  155.901 1.00 161.09 ?  31  GLY E N   1 
ATOM   9966  C CA  . GLY E  4 31  ? 21.500  24.256  155.081 1.00 165.28 ?  31  GLY E CA  1 
ATOM   9967  C C   . GLY E  4 31  ? 22.071  25.311  154.169 1.00 164.95 ?  31  GLY E C   1 
ATOM   9968  O O   . GLY E  4 31  ? 21.318  25.899  153.386 1.00 168.73 ?  31  GLY E O   1 
ATOM   9969  N N   . ASN E  4 32  ? 23.373  25.581  154.238 1.00 161.33 ?  32  ASN E N   1 
ATOM   9970  C CA  . ASN E  4 32  ? 23.965  26.647  153.446 1.00 160.14 ?  32  ASN E CA  1 
ATOM   9971  C C   . ASN E  4 32  ? 25.369  26.254  153.019 1.00 155.85 ?  32  ASN E C   1 
ATOM   9972  O O   . ASN E  4 32  ? 26.132  25.698  153.813 1.00 153.17 ?  32  ASN E O   1 
ATOM   9973  C CB  . ASN E  4 32  ? 24.035  27.959  154.232 1.00 159.89 ?  32  ASN E CB  1 
ATOM   9974  C CG  . ASN E  4 32  ? 22.681  28.436  154.705 1.00 164.53 ?  32  ASN E CG  1 
ATOM   9975  O OD1 . ASN E  4 32  ? 22.128  27.902  155.665 1.00 165.21 ?  32  ASN E OD1 1 
ATOM   9976  N ND2 . ASN E  4 32  ? 22.144  29.452  154.042 1.00 167.87 ?  32  ASN E ND2 1 
ATOM   9977  N N   . ALA E  4 33  ? 25.702  26.558  151.766 1.00 159.98 ?  33  ALA E N   1 
ATOM   9978  C CA  . ALA E  4 33  ? 27.076  26.414  151.314 1.00 156.52 ?  33  ALA E CA  1 
ATOM   9979  C C   . ALA E  4 33  ? 27.968  27.338  152.132 1.00 153.99 ?  33  ALA E C   1 
ATOM   9980  O O   . ALA E  4 33  ? 27.526  28.373  152.639 1.00 154.70 ?  33  ALA E O   1 
ATOM   9981  C CB  . ALA E  4 33  ? 27.186  26.727  149.823 1.00 157.07 ?  33  ALA E CB  1 
ATOM   9982  N N   . LEU E  4 34  ? 29.238  26.970  152.258 1.00 160.64 ?  34  LEU E N   1 
ATOM   9983  C CA  . LEU E  4 34  ? 30.161  27.743  153.073 1.00 158.64 ?  34  LEU E CA  1 
ATOM   9984  C C   . LEU E  4 34  ? 31.422  28.077  152.295 1.00 159.41 ?  34  LEU E C   1 
ATOM   9985  O O   . LEU E  4 34  ? 32.053  27.187  151.716 1.00 159.35 ?  34  LEU E O   1 
ATOM   9986  C CB  . LEU E  4 34  ? 30.523  26.977  154.348 1.00 156.58 ?  34  LEU E CB  1 
ATOM   9987  C CG  . LEU E  4 34  ? 31.342  27.765  155.368 1.00 154.46 ?  34  LEU E CG  1 
ATOM   9988  C CD1 . LEU E  4 34  ? 30.425  28.620  156.225 1.00 152.53 ?  34  LEU E CD1 1 
ATOM   9989  C CD2 . LEU E  4 34  ? 32.168  26.834  156.230 1.00 152.24 ?  34  LEU E CD2 1 
ATOM   9990  N N   . HIS E  4 35  ? 31.791  29.356  152.305 1.00 163.03 ?  35  HIS E N   1 
ATOM   9991  C CA  . HIS E  4 35  ? 32.961  29.865  151.606 1.00 163.83 ?  35  HIS E CA  1 
ATOM   9992  C C   . HIS E  4 35  ? 34.123  30.010  152.581 1.00 161.56 ?  35  HIS E C   1 
ATOM   9993  O O   . HIS E  4 35  ? 33.927  30.212  153.783 1.00 159.90 ?  35  HIS E O   1 
ATOM   9994  C CB  . HIS E  4 35  ? 32.689  31.235  150.975 1.00 164.98 ?  35  HIS E CB  1 
ATOM   9995  C CG  . HIS E  4 35  ? 31.554  31.258  150.000 1.00 166.46 ?  35  HIS E CG  1 
ATOM   9996  N ND1 . HIS E  4 35  ? 31.728  31.046  148.650 1.00 169.11 ?  35  HIS E ND1 1 
ATOM   9997  C CD2 . HIS E  4 35  ? 30.234  31.501  150.175 1.00 165.10 ?  35  HIS E CD2 1 
ATOM   9998  C CE1 . HIS E  4 35  ? 30.563  31.148  148.036 1.00 169.78 ?  35  HIS E CE1 1 
ATOM   9999  N NE2 . HIS E  4 35  ? 29.639  31.418  148.940 1.00 167.03 ?  35  HIS E NE2 1 
ATOM   10000 N N   . TRP E  4 36  ? 35.338  29.907  152.046 1.00 176.96 ?  36  TRP E N   1 
ATOM   10001 C CA  . TRP E  4 36  ? 36.557  30.338  152.720 1.00 175.18 ?  36  TRP E CA  1 
ATOM   10002 C C   . TRP E  4 36  ? 37.211  31.449  151.910 1.00 177.16 ?  36  TRP E C   1 
ATOM   10003 O O   . TRP E  4 36  ? 37.403  31.311  150.697 1.00 178.74 ?  36  TRP E O   1 
ATOM   10004 C CB  . TRP E  4 36  ? 37.540  29.174  152.928 1.00 171.93 ?  36  TRP E CB  1 
ATOM   10005 C CG  . TRP E  4 36  ? 37.045  28.097  153.864 1.00 169.44 ?  36  TRP E CG  1 
ATOM   10006 C CD1 . TRP E  4 36  ? 36.268  27.020  153.547 1.00 169.21 ?  36  TRP E CD1 1 
ATOM   10007 C CD2 . TRP E  4 36  ? 37.314  27.995  155.271 1.00 166.96 ?  36  TRP E CD2 1 
ATOM   10008 N NE1 . TRP E  4 36  ? 36.026  26.262  154.670 1.00 166.62 ?  36  TRP E NE1 1 
ATOM   10009 C CE2 . TRP E  4 36  ? 36.658  26.839  155.740 1.00 165.24 ?  36  TRP E CE2 1 
ATOM   10010 C CE3 . TRP E  4 36  ? 38.040  28.774  156.179 1.00 166.17 ?  36  TRP E CE3 1 
ATOM   10011 C CZ2 . TRP E  4 36  ? 36.708  26.443  157.077 1.00 162.76 ?  36  TRP E CZ2 1 
ATOM   10012 C CZ3 . TRP E  4 36  ? 38.089  28.378  157.505 1.00 163.83 ?  36  TRP E CZ3 1 
ATOM   10013 C CH2 . TRP E  4 36  ? 37.427  27.224  157.941 1.00 162.15 ?  36  TRP E CH2 1 
ATOM   10014 N N   . VAL E  4 37  ? 37.543  32.546  152.587 1.00 176.01 ?  37  VAL E N   1 
ATOM   10015 C CA  . VAL E  4 37  ? 38.079  33.757  151.976 1.00 178.08 ?  37  VAL E CA  1 
ATOM   10016 C C   . VAL E  4 37  ? 39.262  34.205  152.823 1.00 176.96 ?  37  VAL E C   1 
ATOM   10017 O O   . VAL E  4 37  ? 39.178  34.195  154.056 1.00 175.23 ?  37  VAL E O   1 
ATOM   10018 C CB  . VAL E  4 37  ? 37.013  34.871  151.883 1.00 179.31 ?  37  VAL E CB  1 
ATOM   10019 C CG1 . VAL E  4 37  ? 37.617  36.152  151.326 1.00 181.18 ?  37  VAL E CG1 1 
ATOM   10020 C CG2 . VAL E  4 37  ? 35.828  34.413  151.045 1.00 180.15 ?  37  VAL E CG2 1 
ATOM   10021 N N   . ARG E  4 38  ? 40.358  34.612  152.177 1.00 184.50 ?  38  ARG E N   1 
ATOM   10022 C CA  . ARG E  4 38  ? 41.510  35.088  152.929 1.00 183.60 ?  38  ARG E CA  1 
ATOM   10023 C C   . ARG E  4 38  ? 41.861  36.518  152.542 1.00 186.75 ?  38  ARG E C   1 
ATOM   10024 O O   . ARG E  4 38  ? 41.497  37.012  151.470 1.00 189.42 ?  38  ARG E O   1 
ATOM   10025 C CB  . ARG E  4 38  ? 42.759  34.211  152.728 1.00 183.31 ?  38  ARG E CB  1 
ATOM   10026 C CG  . ARG E  4 38  ? 43.442  34.308  151.366 1.00 187.42 ?  38  ARG E CG  1 
ATOM   10027 C CD  . ARG E  4 38  ? 44.703  33.447  151.366 1.00 188.48 ?  38  ARG E CD  1 
ATOM   10028 N NE  . ARG E  4 38  ? 45.486  33.575  150.141 1.00 192.91 ?  38  ARG E NE  1 
ATOM   10029 C CZ  . ARG E  4 38  ? 46.612  32.906  149.906 1.00 194.84 ?  38  ARG E CZ  1 
ATOM   10030 N NH1 . ARG E  4 38  ? 47.074  32.051  150.808 1.00 192.76 1  38  ARG E NH1 1 
ATOM   10031 N NH2 . ARG E  4 38  ? 47.269  33.082  148.767 1.00 199.21 ?  38  ARG E NH2 1 
ATOM   10032 N N   . GLN E  4 39  ? 42.594  37.167  153.445 1.00 190.14 ?  39  GLN E N   1 
ATOM   10033 C CA  . GLN E  4 39  ? 43.019  38.554  153.284 1.00 194.40 ?  39  GLN E CA  1 
ATOM   10034 C C   . GLN E  4 39  ? 44.461  38.707  153.749 1.00 196.64 ?  39  GLN E C   1 
ATOM   10035 O O   . GLN E  4 39  ? 44.743  38.562  154.943 1.00 194.92 ?  39  GLN E O   1 
ATOM   10036 C CB  . GLN E  4 39  ? 42.095  39.474  154.085 1.00 193.64 ?  39  GLN E CB  1 
ATOM   10037 C CG  . GLN E  4 39  ? 42.341  40.960  153.928 1.00 198.15 ?  39  GLN E CG  1 
ATOM   10038 C CD  . GLN E  4 39  ? 41.177  41.783  154.447 1.00 197.52 ?  39  GLN E CD  1 
ATOM   10039 O OE1 . GLN E  4 39  ? 40.540  41.418  155.435 1.00 193.79 ?  39  GLN E OE1 1 
ATOM   10040 N NE2 . GLN E  4 39  ? 40.902  42.903  153.791 1.00 201.52 ?  39  GLN E NE2 1 
ATOM   10041 N N   . ALA E  4 40  ? 45.372  38.993  152.819 1.00 199.90 ?  40  ALA E N   1 
ATOM   10042 C CA  . ALA E  4 40  ? 46.751  39.240  153.205 1.00 203.00 ?  40  ALA E CA  1 
ATOM   10043 C C   . ALA E  4 40  ? 46.817  40.616  153.868 1.00 205.54 ?  40  ALA E C   1 
ATOM   10044 O O   . ALA E  4 40  ? 45.973  41.475  153.599 1.00 206.39 ?  40  ALA E O   1 
ATOM   10045 C CB  . ALA E  4 40  ? 47.678  39.179  151.994 1.00 207.32 ?  40  ALA E CB  1 
ATOM   10046 N N   . PRO E  4 41  ? 47.785  40.848  154.754 1.00 211.86 ?  41  PRO E N   1 
ATOM   10047 C CA  . PRO E  4 41  ? 47.798  42.122  155.490 1.00 214.21 ?  41  PRO E CA  1 
ATOM   10048 C C   . PRO E  4 41  ? 47.874  43.321  154.553 1.00 219.52 ?  41  PRO E C   1 
ATOM   10049 O O   . PRO E  4 41  ? 48.750  43.406  153.690 1.00 223.66 ?  41  PRO E O   1 
ATOM   10050 C CB  . PRO E  4 41  ? 49.047  42.018  156.375 1.00 215.97 ?  41  PRO E CB  1 
ATOM   10051 C CG  . PRO E  4 41  ? 49.811  40.824  155.891 1.00 215.74 ?  41  PRO E CG  1 
ATOM   10052 C CD  . PRO E  4 41  ? 48.858  39.933  155.179 1.00 211.74 ?  41  PRO E CD  1 
ATOM   10053 N N   . GLY E  4 42  ? 46.936  44.253  154.733 1.00 208.91 ?  42  GLY E N   1 
ATOM   10054 C CA  . GLY E  4 42  ? 46.862  45.440  153.908 1.00 214.08 ?  42  GLY E CA  1 
ATOM   10055 C C   . GLY E  4 42  ? 46.276  45.247  152.526 1.00 214.79 ?  42  GLY E C   1 
ATOM   10056 O O   . GLY E  4 42  ? 46.227  46.214  151.755 1.00 219.39 ?  42  GLY E O   1 
ATOM   10057 N N   . GLN E  4 43  ? 45.822  44.043  152.186 1.00 205.48 ?  43  GLN E N   1 
ATOM   10058 C CA  . GLN E  4 43  ? 45.374  43.699  150.843 1.00 206.08 ?  43  GLN E CA  1 
ATOM   10059 C C   . GLN E  4 43  ? 43.865  43.452  150.832 1.00 202.35 ?  43  GLN E C   1 
ATOM   10060 O O   . GLN E  4 43  ? 43.171  43.635  151.836 1.00 199.91 ?  43  GLN E O   1 
ATOM   10061 C CB  . GLN E  4 43  ? 46.132  42.470  150.333 1.00 205.00 ?  43  GLN E CB  1 
ATOM   10062 C CG  . GLN E  4 43  ? 47.648  42.581  150.443 1.00 208.60 ?  43  GLN E CG  1 
ATOM   10063 C CD  . GLN E  4 43  ? 48.187  43.878  149.887 1.00 215.10 ?  43  GLN E CD  1 
ATOM   10064 O OE1 . GLN E  4 43  ? 47.893  44.249  148.753 1.00 218.05 ?  43  GLN E OE1 1 
ATOM   10065 N NE2 . GLN E  4 43  ? 48.983  44.578  150.686 1.00 217.69 ?  43  GLN E NE2 1 
ATOM   10066 N N   . GLY E  4 44  ? 43.355  43.046  149.668 1.00 195.97 ?  44  GLY E N   1 
ATOM   10067 C CA  . GLY E  4 44  ? 41.944  42.772  149.487 1.00 193.03 ?  44  GLY E CA  1 
ATOM   10068 C C   . GLY E  4 44  ? 41.594  41.322  149.763 1.00 187.66 ?  44  GLY E C   1 
ATOM   10069 O O   . GLY E  4 44  ? 42.343  40.583  150.406 1.00 185.72 ?  44  GLY E O   1 
ATOM   10070 N N   . LEU E  4 45  ? 40.435  40.911  149.252 1.00 204.17 ?  45  LEU E N   1 
ATOM   10071 C CA  . LEU E  4 45  ? 39.856  39.603  149.540 1.00 199.25 ?  45  LEU E CA  1 
ATOM   10072 C C   . LEU E  4 45  ? 40.075  38.621  148.391 1.00 199.41 ?  45  LEU E C   1 
ATOM   10073 O O   . LEU E  4 45  ? 39.891  38.969  147.221 1.00 202.73 ?  45  LEU E O   1 
ATOM   10074 C CB  . LEU E  4 45  ? 38.359  39.746  149.826 1.00 197.11 ?  45  LEU E CB  1 
ATOM   10075 C CG  . LEU E  4 45  ? 37.993  40.633  151.022 1.00 196.64 ?  45  LEU E CG  1 
ATOM   10076 C CD1 . LEU E  4 45  ? 36.529  41.046  150.967 1.00 196.48 ?  45  LEU E CD1 1 
ATOM   10077 C CD2 . LEU E  4 45  ? 38.309  39.945  152.345 1.00 192.54 ?  45  LEU E CD2 1 
ATOM   10078 N N   . GLU E  4 46  ? 40.473  37.391  148.733 1.00 192.70 ?  46  GLU E N   1 
ATOM   10079 C CA  . GLU E  4 46  ? 40.749  36.343  147.751 1.00 193.11 ?  46  GLU E CA  1 
ATOM   10080 C C   . GLU E  4 46  ? 39.973  35.073  148.094 1.00 190.84 ?  46  GLU E C   1 
ATOM   10081 O O   . GLU E  4 46  ? 40.116  34.535  149.197 1.00 188.16 ?  46  GLU E O   1 
ATOM   10082 C CB  . GLU E  4 46  ? 42.252  36.060  147.678 1.00 194.95 ?  46  GLU E CB  1 
ATOM   10083 C CG  . GLU E  4 46  ? 42.644  35.020  146.649 1.00 195.89 ?  46  GLU E CG  1 
ATOM   10084 C CD  . GLU E  4 46  ? 44.145  34.885  146.511 1.00 198.89 ?  46  GLU E CD  1 
ATOM   10085 O OE1 . GLU E  4 46  ? 44.617  34.592  145.392 1.00 201.90 ?  46  GLU E OE1 1 
ATOM   10086 O OE2 . GLU E  4 46  ? 44.859  35.127  147.506 1.00 198.84 -1 46  GLU E OE2 1 
ATOM   10087 N N   . TRP E  4 47  ? 39.155  34.602  147.146 1.00 176.81 ?  47  TRP E N   1 
ATOM   10088 C CA  . TRP E  4 47  ? 38.326  33.405  147.302 1.00 175.39 ?  47  TRP E CA  1 
ATOM   10089 C C   . TRP E  4 47  ? 39.144  32.128  147.095 1.00 173.51 ?  47  TRP E C   1 
ATOM   10090 O O   . TRP E  4 47  ? 39.786  31.965  146.052 1.00 174.88 ?  47  TRP E O   1 
ATOM   10091 C CB  . TRP E  4 47  ? 37.173  33.460  146.299 1.00 177.95 ?  47  TRP E CB  1 
ATOM   10092 C CG  . TRP E  4 47  ? 36.158  32.349  146.394 1.00 177.31 ?  47  TRP E CG  1 
ATOM   10093 C CD1 . TRP E  4 47  ? 35.150  32.233  147.307 1.00 175.89 ?  47  TRP E CD1 1 
ATOM   10094 C CD2 . TRP E  4 47  ? 36.047  31.209  145.529 1.00 177.98 ?  47  TRP E CD2 1 
ATOM   10095 N NE1 . TRP E  4 47  ? 34.422  31.092  147.068 1.00 176.12 ?  47  TRP E NE1 1 
ATOM   10096 C CE2 . TRP E  4 47  ? 34.953  30.445  145.983 1.00 177.37 ?  47  TRP E CE2 1 
ATOM   10097 C CE3 . TRP E  4 47  ? 36.769  30.758  144.419 1.00 178.94 ?  47  TRP E CE3 1 
ATOM   10098 C CZ2 . TRP E  4 47  ? 34.562  29.259  145.364 1.00 177.88 ?  47  TRP E CZ2 1 
ATOM   10099 C CZ3 . TRP E  4 47  ? 36.381  29.578  143.809 1.00 178.97 ?  47  TRP E CZ3 1 
ATOM   10100 C CH2 . TRP E  4 47  ? 35.289  28.842  144.284 1.00 178.52 ?  47  TRP E CH2 1 
ATOM   10101 N N   . LEU E  4 48  ? 39.124  31.223  148.082 1.00 181.82 ?  48  LEU E N   1 
ATOM   10102 C CA  . LEU E  4 48  ? 39.800  29.929  147.963 1.00 178.87 ?  48  LEU E CA  1 
ATOM   10103 C C   . LEU E  4 48  ? 38.912  28.823  147.393 1.00 178.91 ?  48  LEU E C   1 
ATOM   10104 O O   . LEU E  4 48  ? 39.373  28.017  146.577 1.00 178.19 ?  48  LEU E O   1 
ATOM   10105 C CB  . LEU E  4 48  ? 40.335  29.472  149.324 1.00 174.85 ?  48  LEU E CB  1 
ATOM   10106 C CG  . LEU E  4 48  ? 41.244  30.389  150.138 1.00 174.98 ?  48  LEU E CG  1 
ATOM   10107 C CD1 . LEU E  4 48  ? 41.550  29.753  151.486 1.00 172.04 ?  48  LEU E CD1 1 
ATOM   10108 C CD2 . LEU E  4 48  ? 42.523  30.666  149.377 1.00 179.09 ?  48  LEU E CD2 1 
ATOM   10109 N N   . GLY E  4 49  ? 37.656  28.771  147.811 1.00 173.32 ?  49  GLY E N   1 
ATOM   10110 C CA  . GLY E  4 49  ? 36.745  27.722  147.398 1.00 173.72 ?  49  GLY E CA  1 
ATOM   10111 C C   . GLY E  4 49  ? 35.548  27.691  148.324 1.00 173.75 ?  49  GLY E C   1 
ATOM   10112 O O   . GLY E  4 49  ? 35.434  28.489  149.254 1.00 173.34 ?  49  GLY E O   1 
ATOM   10113 N N   . TRP E  4 50  ? 34.646  26.749  148.051 1.00 159.96 ?  50  TRP E N   1 
ATOM   10114 C CA  . TRP E  4 50  ? 33.523  26.552  148.956 1.00 159.98 ?  50  TRP E CA  1 
ATOM   10115 C C   . TRP E  4 50  ? 33.154  25.076  149.022 1.00 158.23 ?  50  TRP E C   1 
ATOM   10116 O O   . TRP E  4 50  ? 33.532  24.277  148.160 1.00 157.60 ?  50  TRP E O   1 
ATOM   10117 C CB  . TRP E  4 50  ? 32.329  27.438  148.560 1.00 163.71 ?  50  TRP E CB  1 
ATOM   10118 C CG  . TRP E  4 50  ? 31.630  27.121  147.271 1.00 166.87 ?  50  TRP E CG  1 
ATOM   10119 C CD1 . TRP E  4 50  ? 32.131  26.449  146.194 1.00 167.61 ?  50  TRP E CD1 1 
ATOM   10120 C CD2 . TRP E  4 50  ? 30.318  27.557  146.895 1.00 169.21 ?  50  TRP E CD2 1 
ATOM   10121 N NE1 . TRP E  4 50  ? 31.191  26.396  145.191 1.00 171.21 ?  50  TRP E NE1 1 
ATOM   10122 C CE2 . TRP E  4 50  ? 30.071  27.075  145.595 1.00 172.14 ?  50  TRP E CE2 1 
ATOM   10123 C CE3 . TRP E  4 50  ? 29.319  28.291  147.542 1.00 167.92 ?  50  TRP E CE3 1 
ATOM   10124 C CZ2 . TRP E  4 50  ? 28.867  27.306  144.930 1.00 174.34 ?  50  TRP E CZ2 1 
ATOM   10125 C CZ3 . TRP E  4 50  ? 28.128  28.522  146.881 1.00 168.74 ?  50  TRP E CZ3 1 
ATOM   10126 C CH2 . TRP E  4 50  ? 27.910  28.030  145.590 1.00 172.17 ?  50  TRP E CH2 1 
ATOM   10127 N N   . ILE E  4 51  ? 32.402  24.730  150.066 1.00 160.10 ?  51  ILE E N   1 
ATOM   10128 C CA  . ILE E  4 51  ? 31.991  23.360  150.343 1.00 157.84 ?  51  ILE E CA  1 
ATOM   10129 C C   . ILE E  4 51  ? 30.495  23.344  150.628 1.00 160.96 ?  51  ILE E C   1 
ATOM   10130 O O   . ILE E  4 51  ? 29.954  24.279  151.229 1.00 162.76 ?  51  ILE E O   1 
ATOM   10131 C CB  . ILE E  4 51  ? 32.788  22.770  151.529 1.00 152.61 ?  51  ILE E CB  1 
ATOM   10132 C CG1 . ILE E  4 51  ? 32.401  21.312  151.788 1.00 148.98 ?  51  ILE E CG1 1 
ATOM   10133 C CG2 . ILE E  4 51  ? 32.600  23.613  152.778 1.00 153.30 ?  51  ILE E CG2 1 
ATOM   10134 C CD1 . ILE E  4 51  ? 33.352  20.588  152.711 1.00 143.44 ?  51  ILE E CD1 1 
ATOM   10135 N N   . ASN E  4 52  ? 29.830  22.275  150.187 1.00 156.18 ?  52  ASN E N   1 
ATOM   10136 C CA  . ASN E  4 52  ? 28.452  21.998  150.567 1.00 158.63 ?  52  ASN E CA  1 
ATOM   10137 C C   . ASN E  4 52  ? 28.484  21.133  151.818 1.00 154.02 ?  52  ASN E C   1 
ATOM   10138 O O   . ASN E  4 52  ? 28.912  19.971  151.741 1.00 149.13 ?  52  ASN E O   1 
ATOM   10139 C CB  . ASN E  4 52  ? 27.707  21.287  149.443 1.00 160.99 ?  52  ASN E CB  1 
ATOM   10140 C CG  . ASN E  4 52  ? 26.238  21.027  149.772 1.00 164.52 ?  52  ASN E CG  1 
ATOM   10141 O OD1 . ASN E  4 52  ? 25.870  20.736  150.909 1.00 163.22 ?  52  ASN E OD1 1 
ATOM   10142 N ND2 . ASN E  4 52  ? 25.389  21.152  148.761 1.00 169.12 ?  52  ASN E ND2 1 
ATOM   10143 N N   . PRO E  4 53  A 28.056  21.636  152.977 1.00 157.96 ?  52  PRO E N   1 
ATOM   10144 C CA  . PRO E  4 53  A 28.197  20.846  154.207 1.00 153.60 ?  52  PRO E CA  1 
ATOM   10145 C C   . PRO E  4 53  A 27.296  19.630  154.236 1.00 151.47 ?  52  PRO E C   1 
ATOM   10146 O O   . PRO E  4 53  A 27.573  18.691  154.991 1.00 145.69 ?  52  PRO E O   1 
ATOM   10147 C CB  . PRO E  4 53  A 27.812  21.844  155.308 1.00 156.53 ?  52  PRO E CB  1 
ATOM   10148 C CG  . PRO E  4 53  A 28.077  23.187  154.698 1.00 158.43 ?  52  PRO E CG  1 
ATOM   10149 C CD  . PRO E  4 53  A 27.653  23.021  153.266 1.00 161.14 ?  52  PRO E CD  1 
ATOM   10150 N N   . HIS E  4 54  ? 26.228  19.619  153.441 1.00 170.24 ?  53  HIS E N   1 
ATOM   10151 C CA  . HIS E  4 54  ? 25.343  18.462  153.391 1.00 166.93 ?  53  HIS E CA  1 
ATOM   10152 C C   . HIS E  4 54  ? 26.009  17.278  152.696 1.00 161.37 ?  53  HIS E C   1 
ATOM   10153 O O   . HIS E  4 54  ? 26.158  16.199  153.281 1.00 154.88 ?  53  HIS E O   1 
ATOM   10154 C CB  . HIS E  4 54  ? 24.052  18.852  152.670 1.00 171.92 ?  53  HIS E CB  1 
ATOM   10155 C CG  . HIS E  4 54  ? 23.137  17.702  152.397 1.00 167.40 ?  53  HIS E CG  1 
ATOM   10156 N ND1 . HIS E  4 54  ? 22.649  16.879  153.388 1.00 161.54 ?  53  HIS E ND1 1 
ATOM   10157 C CD2 . HIS E  4 54  ? 22.627  17.234  151.233 1.00 169.50 ?  53  HIS E CD2 1 
ATOM   10158 C CE1 . HIS E  4 54  ? 21.876  15.955  152.847 1.00 159.06 ?  53  HIS E CE1 1 
ATOM   10159 N NE2 . HIS E  4 54  ? 21.846  16.149  151.541 1.00 164.68 ?  53  HIS E NE2 1 
ATOM   10160 N N   . SER E  4 55  ? 26.420  17.467  151.444 1.00 167.45 ?  54  SER E N   1 
ATOM   10161 C CA  . SER E  4 55  ? 26.994  16.386  150.652 1.00 163.12 ?  54  SER E CA  1 
ATOM   10162 C C   . SER E  4 55  ? 28.485  16.187  150.883 1.00 158.32 ?  54  SER E C   1 
ATOM   10163 O O   . SER E  4 55  ? 28.988  15.072  150.697 1.00 155.52 ?  54  SER E O   1 
ATOM   10164 C CB  . SER E  4 55  ? 26.745  16.635  149.161 1.00 167.94 ?  54  SER E CB  1 
ATOM   10165 O OG  . SER E  4 55  ? 27.423  17.796  148.712 1.00 172.29 ?  54  SER E OG  1 
ATOM   10166 N N   . GLY E  4 56  ? 29.200  17.231  151.288 1.00 171.63 ?  55  GLY E N   1 
ATOM   10167 C CA  . GLY E  4 56  ? 30.644  17.192  151.340 1.00 168.24 ?  55  GLY E CA  1 
ATOM   10168 C C   . GLY E  4 56  ? 31.327  17.555  150.038 1.00 170.63 ?  55  GLY E C   1 
ATOM   10169 O O   . GLY E  4 56  ? 32.562  17.639  150.008 1.00 168.77 ?  55  GLY E O   1 
ATOM   10170 N N   . ASP E  4 57  ? 30.566  17.774  148.964 1.00 170.92 ?  56  ASP E N   1 
ATOM   10171 C CA  . ASP E  4 57  ? 31.146  18.147  147.681 1.00 173.81 ?  56  ASP E CA  1 
ATOM   10172 C C   . ASP E  4 57  ? 31.851  19.494  147.786 1.00 176.63 ?  56  ASP E C   1 
ATOM   10173 O O   . ASP E  4 57  ? 31.420  20.390  148.517 1.00 178.40 ?  56  ASP E O   1 
ATOM   10174 C CB  . ASP E  4 57  ? 30.065  18.212  146.598 1.00 180.58 ?  56  ASP E CB  1 
ATOM   10175 C CG  . ASP E  4 57  ? 29.480  16.850  146.267 1.00 180.82 ?  56  ASP E CG  1 
ATOM   10176 O OD1 . ASP E  4 57  ? 30.065  15.830  146.686 1.00 175.71 ?  56  ASP E OD1 1 
ATOM   10177 O OD2 . ASP E  4 57  ? 28.435  16.800  145.583 1.00 187.29 -1 56  ASP E OD2 1 
ATOM   10178 N N   . THR E  4 58  ? 32.946  19.638  147.046 1.00 165.01 ?  57  THR E N   1 
ATOM   10179 C CA  . THR E  4 58  ? 33.741  20.853  147.091 1.00 165.91 ?  57  THR E CA  1 
ATOM   10180 C C   . THR E  4 58  ? 34.067  21.303  145.676 1.00 168.57 ?  57  THR E C   1 
ATOM   10181 O O   . THR E  4 58  ? 34.133  20.494  144.746 1.00 170.34 ?  57  THR E O   1 
ATOM   10182 C CB  . THR E  4 58  ? 35.051  20.647  147.867 1.00 166.86 ?  57  THR E CB  1 
ATOM   10183 O OG1 . THR E  4 58  ? 35.823  19.627  147.223 1.00 169.36 ?  57  THR E OG1 1 
ATOM   10184 C CG2 . THR E  4 58  ? 34.772  20.232  149.306 1.00 164.43 ?  57  THR E CG2 1 
ATOM   10185 N N   . THR E  4 59  ? 34.254  22.612  145.526 1.00 169.77 ?  58  THR E N   1 
ATOM   10186 C CA  . THR E  4 59  ? 34.875  23.199  144.347 1.00 172.85 ?  58  THR E CA  1 
ATOM   10187 C C   . THR E  4 59  ? 35.926  24.187  144.824 1.00 174.05 ?  58  THR E C   1 
ATOM   10188 O O   . THR E  4 59  ? 35.613  25.101  145.595 1.00 172.47 ?  58  THR E O   1 
ATOM   10189 C CB  . THR E  4 59  ? 33.840  23.899  143.463 1.00 172.88 ?  58  THR E CB  1 
ATOM   10190 O OG1 . THR E  4 59  ? 32.868  22.944  143.022 1.00 172.07 ?  58  THR E OG1 1 
ATOM   10191 C CG2 . THR E  4 59  ? 34.512  24.524  142.254 1.00 176.33 ?  58  THR E CG2 1 
ATOM   10192 N N   . THR E  4 60  ? 37.161  24.008  144.369 1.00 182.90 ?  59  THR E N   1 
ATOM   10193 C CA  . THR E  4 60  ? 38.283  24.836  144.784 1.00 184.70 ?  59  THR E CA  1 
ATOM   10194 C C   . THR E  4 60  ? 38.693  25.767  143.651 1.00 187.93 ?  59  THR E C   1 
ATOM   10195 O O   . THR E  4 60  ? 38.681  25.372  142.480 1.00 189.91 ?  59  THR E O   1 
ATOM   10196 C CB  . THR E  4 60  ? 39.481  23.970  145.199 1.00 186.58 ?  59  THR E CB  1 
ATOM   10197 O OG1 . THR E  4 60  ? 39.071  23.020  146.189 1.00 183.85 ?  59  THR E OG1 1 
ATOM   10198 C CG2 . THR E  4 60  ? 40.594  24.826  145.773 1.00 188.38 ?  59  THR E CG2 1 
ATOM   10199 N N   . SER E  4 61  ? 39.018  27.014  143.998 1.00 190.20 ?  60  SER E N   1 
ATOM   10200 C CA  . SER E  4 61  ? 39.607  27.914  143.018 1.00 193.93 ?  60  SER E CA  1 
ATOM   10201 C C   . SER E  4 61  ? 40.826  27.228  142.418 1.00 197.70 ?  60  SER E C   1 
ATOM   10202 O O   . SER E  4 61  ? 41.630  26.626  143.133 1.00 198.08 ?  60  SER E O   1 
ATOM   10203 C CB  . SER E  4 61  ? 39.992  29.244  143.668 1.00 194.54 ?  60  SER E CB  1 
ATOM   10204 O OG  . SER E  4 61  ? 40.517  30.148  142.713 1.00 198.51 ?  60  SER E OG  1 
ATOM   10205 N N   . GLN E  4 62  ? 40.962  27.314  141.096 1.00 196.89 ?  61  GLN E N   1 
ATOM   10206 C CA  . GLN E  4 62  ? 41.973  26.500  140.438 1.00 200.52 ?  61  GLN E CA  1 
ATOM   10207 C C   . GLN E  4 62  ? 43.397  26.913  140.795 1.00 204.03 ?  61  GLN E C   1 
ATOM   10208 O O   . GLN E  4 62  ? 44.309  26.088  140.678 1.00 206.78 ?  61  GLN E O   1 
ATOM   10209 C CB  . GLN E  4 62  ? 41.755  26.530  138.930 1.00 203.04 ?  61  GLN E CB  1 
ATOM   10210 C CG  . GLN E  4 62  ? 40.593  25.645  138.529 1.00 200.29 ?  61  GLN E CG  1 
ATOM   10211 C CD  . GLN E  4 62  ? 41.022  24.222  138.264 1.00 201.59 ?  61  GLN E CD  1 
ATOM   10212 O OE1 . GLN E  4 62  ? 41.811  23.954  137.360 1.00 206.27 ?  61  GLN E OE1 1 
ATOM   10213 N NE2 . GLN E  4 62  ? 40.522  23.298  139.077 1.00 198.43 ?  61  GLN E NE2 1 
ATOM   10214 N N   . LYS E  4 63  ? 43.612  28.166  141.202 1.00 198.28 ?  62  LYS E N   1 
ATOM   10215 C CA  . LYS E  4 63  ? 44.918  28.573  141.716 1.00 201.38 ?  62  LYS E CA  1 
ATOM   10216 C C   . LYS E  4 63  ? 45.372  27.706  142.886 1.00 199.85 ?  62  LYS E C   1 
ATOM   10217 O O   . LYS E  4 63  ? 46.572  27.450  143.044 1.00 203.30 ?  62  LYS E O   1 
ATOM   10218 C CB  . LYS E  4 63  ? 44.879  30.041  142.148 1.00 201.66 ?  62  LYS E CB  1 
ATOM   10219 C CG  . LYS E  4 63  ? 46.185  30.557  142.740 1.00 207.98 ?  62  LYS E CG  1 
ATOM   10220 C CD  . LYS E  4 63  ? 46.081  32.016  143.147 1.00 206.17 ?  62  LYS E CD  1 
ATOM   10221 C CE  . LYS E  4 63  ? 47.296  32.443  143.953 1.00 213.85 ?  62  LYS E CE  1 
ATOM   10222 N NZ  . LYS E  4 63  ? 47.167  33.828  144.480 1.00 209.85 1  62  LYS E NZ  1 
ATOM   10223 N N   . PHE E  4 64  ? 44.432  27.233  143.701 1.00 203.86 ?  63  PHE E N   1 
ATOM   10224 C CA  . PHE E  4 64  ? 44.735  26.450  144.890 1.00 202.10 ?  63  PHE E CA  1 
ATOM   10225 C C   . PHE E  4 64  ? 44.443  24.963  144.750 1.00 201.13 ?  63  PHE E C   1 
ATOM   10226 O O   . PHE E  4 64  ? 44.629  24.221  145.722 1.00 199.70 ?  63  PHE E O   1 
ATOM   10227 C CB  . PHE E  4 64  ? 43.952  27.033  146.067 1.00 197.63 ?  63  PHE E CB  1 
ATOM   10228 C CG  . PHE E  4 64  ? 44.236  28.488  146.301 1.00 198.60 ?  63  PHE E CG  1 
ATOM   10229 C CD1 . PHE E  4 64  ? 45.427  28.898  146.877 1.00 201.11 ?  63  PHE E CD1 1 
ATOM   10230 C CD2 . PHE E  4 64  ? 43.328  29.451  145.893 1.00 197.50 ?  63  PHE E CD2 1 
ATOM   10231 C CE1 . PHE E  4 64  ? 45.688  30.242  147.076 1.00 202.34 ?  63  PHE E CE1 1 
ATOM   10232 C CE2 . PHE E  4 64  ? 43.584  30.794  146.084 1.00 198.88 ?  63  PHE E CE2 1 
ATOM   10233 C CZ  . PHE E  4 64  ? 44.766  31.191  146.677 1.00 201.27 ?  63  PHE E CZ  1 
ATOM   10234 N N   . GLN E  4 65  ? 43.973  24.514  143.587 1.00 202.38 ?  64  GLN E N   1 
ATOM   10235 C CA  . GLN E  4 65  ? 43.582  23.121  143.405 1.00 201.57 ?  64  GLN E CA  1 
ATOM   10236 C C   . GLN E  4 65  ? 44.731  22.188  143.768 1.00 204.61 ?  64  GLN E C   1 
ATOM   10237 O O   . GLN E  4 65  ? 45.864  22.368  143.313 1.00 209.16 ?  64  GLN E O   1 
ATOM   10238 C CB  . GLN E  4 65  ? 43.130  22.874  141.968 1.00 203.00 ?  64  GLN E CB  1 
ATOM   10239 C CG  . GLN E  4 65  ? 42.776  21.426  141.707 1.00 204.43 ?  64  GLN E CG  1 
ATOM   10240 C CD  . GLN E  4 65  ? 41.574  20.986  142.516 1.00 205.33 ?  64  GLN E CD  1 
ATOM   10241 O OE1 . GLN E  4 65  ? 40.602  21.729  142.655 1.00 205.06 ?  64  GLN E OE1 1 
ATOM   10242 N NE2 . GLN E  4 65  ? 41.638  19.778  143.065 1.00 205.75 ?  64  GLN E NE2 1 
ATOM   10243 N N   . GLY E  4 66  ? 44.434  21.196  144.606 1.00 199.36 ?  65  GLY E N   1 
ATOM   10244 C CA  . GLY E  4 66  ? 45.407  20.213  145.029 1.00 202.21 ?  65  GLY E CA  1 
ATOM   10245 C C   . GLY E  4 66  ? 46.291  20.666  146.167 1.00 202.84 ?  65  GLY E C   1 
ATOM   10246 O O   . GLY E  4 66  ? 47.131  19.884  146.632 1.00 205.35 ?  65  GLY E O   1 
ATOM   10247 N N   . ARG E  4 67  ? 46.139  21.905  146.617 1.00 203.79 ?  66  ARG E N   1 
ATOM   10248 C CA  . ARG E  4 67  ? 46.915  22.484  147.705 1.00 204.07 ?  66  ARG E CA  1 
ATOM   10249 C C   . ARG E  4 67  ? 46.025  22.821  148.893 1.00 198.73 ?  66  ARG E C   1 
ATOM   10250 O O   . ARG E  4 67  ? 46.399  22.555  150.038 1.00 197.78 ?  66  ARG E O   1 
ATOM   10251 C CB  . ARG E  4 67  ? 47.726  23.710  147.214 1.00 207.41 ?  66  ARG E CB  1 
ATOM   10252 C CG  . ARG E  4 67  ? 48.945  24.022  148.108 1.00 209.30 ?  66  ARG E CG  1 
ATOM   10253 C CD  . ARG E  4 67  ? 49.922  25.071  147.528 1.00 213.72 ?  66  ARG E CD  1 
ATOM   10254 N NE  . ARG E  4 67  ? 49.449  26.449  147.430 1.00 212.53 ?  66  ARG E NE  1 
ATOM   10255 C CZ  . ARG E  4 67  ? 49.589  27.350  148.399 1.00 211.09 ?  66  ARG E CZ  1 
ATOM   10256 N NH1 . ARG E  4 67  ? 50.134  27.000  149.557 1.00 210.53 1  66  ARG E NH1 1 
ATOM   10257 N NH2 . ARG E  4 67  ? 49.151  28.590  148.228 1.00 210.50 ?  66  ARG E NH2 1 
ATOM   10258 N N   . VAL E  4 68  ? 44.852  23.410  148.639 1.00 205.19 ?  67  VAL E N   1 
ATOM   10259 C CA  . VAL E  4 68  ? 43.843  23.709  149.655 1.00 200.34 ?  67  VAL E CA  1 
ATOM   10260 C C   . VAL E  4 68  ? 42.743  22.648  149.623 1.00 197.20 ?  67  VAL E C   1 
ATOM   10261 O O   . VAL E  4 68  ? 42.237  22.300  148.548 1.00 197.41 ?  67  VAL E O   1 
ATOM   10262 C CB  . VAL E  4 68  ? 43.250  25.111  149.429 1.00 199.15 ?  67  VAL E CB  1 
ATOM   10263 C CG1 . VAL E  4 68  ? 42.078  25.363  150.359 1.00 196.27 ?  67  VAL E CG1 1 
ATOM   10264 C CG2 . VAL E  4 68  ? 44.320  26.172  149.610 1.00 201.95 ?  67  VAL E CG2 1 
ATOM   10265 N N   . TYR E  4 69  ? 42.371  22.135  150.807 1.00 188.53 ?  68  TYR E N   1 
ATOM   10266 C CA  . TYR E  4 69  ? 41.389  21.062  150.972 1.00 185.93 ?  68  TYR E CA  1 
ATOM   10267 C C   . TYR E  4 69  ? 40.311  21.430  151.984 1.00 181.61 ?  68  TYR E C   1 
ATOM   10268 O O   . TYR E  4 69  ? 40.618  21.865  153.099 1.00 180.47 ?  68  TYR E O   1 
ATOM   10269 C CB  . TYR E  4 69  ? 42.043  19.746  151.408 1.00 187.52 ?  68  TYR E CB  1 
ATOM   10270 C CG  . TYR E  4 69  ? 42.965  19.162  150.377 1.00 191.98 ?  68  TYR E CG  1 
ATOM   10271 C CD1 . TYR E  4 69  ? 42.482  18.259  149.441 1.00 192.66 ?  68  TYR E CD1 1 
ATOM   10272 C CD2 . TYR E  4 69  ? 44.309  19.499  150.335 1.00 195.76 ?  68  TYR E CD2 1 
ATOM   10273 C CE1 . TYR E  4 69  ? 43.306  17.714  148.485 1.00 197.01 ?  68  TYR E CE1 1 
ATOM   10274 C CE2 . TYR E  4 69  ? 45.147  18.957  149.379 1.00 200.30 ?  68  TYR E CE2 1 
ATOM   10275 C CZ  . TYR E  4 69  ? 44.638  18.065  148.457 1.00 200.91 ?  68  TYR E CZ  1 
ATOM   10276 O OH  . TYR E  4 69  ? 45.468  17.523  147.503 1.00 205.68 ?  68  TYR E OH  1 
ATOM   10277 N N   . MET E  4 70  ? 39.053  21.231  151.592 1.00 176.58 ?  69  MET E N   1 
ATOM   10278 C CA  . MET E  4 70  ? 37.889  21.542  152.412 1.00 172.90 ?  69  MET E CA  1 
ATOM   10279 C C   . MET E  4 70  ? 37.189  20.255  152.828 1.00 171.41 ?  69  MET E C   1 
ATOM   10280 O O   . MET E  4 70  ? 36.913  19.394  151.985 1.00 172.16 ?  69  MET E O   1 
ATOM   10281 C CB  . MET E  4 70  ? 36.916  22.440  151.647 1.00 172.01 ?  69  MET E CB  1 
ATOM   10282 C CG  . MET E  4 70  ? 37.444  23.835  151.395 1.00 173.33 ?  69  MET E CG  1 
ATOM   10283 S SD  . MET E  4 70  ? 36.498  24.702  150.135 1.00 173.82 ?  69  MET E SD  1 
ATOM   10284 C CE  . MET E  4 70  ? 37.080  23.870  148.661 1.00 177.23 ?  69  MET E CE  1 
ATOM   10285 N N   . THR E  4 71  ? 36.893  20.133  154.122 1.00 184.70 ?  70  THR E N   1 
ATOM   10286 C CA  . THR E  4 71  ? 36.180  18.986  154.669 1.00 183.31 ?  70  THR E CA  1 
ATOM   10287 C C   . THR E  4 71  ? 35.147  19.499  155.662 1.00 180.33 ?  70  THR E C   1 
ATOM   10288 O O   . THR E  4 71  ? 35.137  20.678  156.022 1.00 179.48 ?  70  THR E O   1 
ATOM   10289 C CB  . THR E  4 71  ? 37.124  17.985  155.355 1.00 184.73 ?  70  THR E CB  1 
ATOM   10290 O OG1 . THR E  4 71  ? 37.915  18.658  156.345 1.00 184.61 ?  70  THR E OG1 1 
ATOM   10291 C CG2 . THR E  4 71  ? 38.035  17.314  154.340 1.00 188.24 ?  70  THR E CG2 1 
ATOM   10292 N N   . ARG E  4 72  ? 34.271  18.603  156.112 1.00 159.69 ?  71  ARG E N   1 
ATOM   10293 C CA  . ARG E  4 72  ? 33.314  18.962  157.147 1.00 157.29 ?  71  ARG E CA  1 
ATOM   10294 C C   . ARG E  4 72  ? 33.040  17.774  158.059 1.00 156.70 ?  71  ARG E C   1 
ATOM   10295 O O   . ARG E  4 72  ? 33.155  16.615  157.649 1.00 157.84 ?  71  ARG E O   1 
ATOM   10296 C CB  . ARG E  4 72  ? 32.019  19.486  156.509 1.00 156.33 ?  71  ARG E CB  1 
ATOM   10297 C CG  . ARG E  4 72  ? 31.490  18.606  155.384 1.00 157.18 ?  71  ARG E CG  1 
ATOM   10298 C CD  . ARG E  4 72  ? 30.482  17.573  155.841 1.00 156.45 ?  71  ARG E CD  1 
ATOM   10299 N NE  . ARG E  4 72  ? 30.001  16.789  154.706 1.00 157.54 ?  71  ARG E NE  1 
ATOM   10300 C CZ  . ARG E  4 72  ? 29.672  15.503  154.766 1.00 158.05 ?  71  ARG E CZ  1 
ATOM   10301 N NH1 . ARG E  4 72  ? 29.245  14.874  153.679 1.00 159.19 1  71  ARG E NH1 1 
ATOM   10302 N NH2 . ARG E  4 72  ? 29.769  14.844  155.911 1.00 157.59 ?  71  ARG E NH2 1 
ATOM   10303 N N   . ASP E  4 73  ? 32.672  18.084  159.306 1.00 175.83 ?  72  ASP E N   1 
ATOM   10304 C CA  . ASP E  4 73  ? 32.130  17.121  160.261 1.00 175.26 ?  72  ASP E CA  1 
ATOM   10305 C C   . ASP E  4 73  ? 30.742  17.616  160.660 1.00 173.54 ?  72  ASP E C   1 
ATOM   10306 O O   . ASP E  4 73  ? 30.620  18.582  161.422 1.00 172.06 ?  72  ASP E O   1 
ATOM   10307 C CB  . ASP E  4 73  ? 33.064  16.993  161.472 1.00 175.40 ?  72  ASP E CB  1 
ATOM   10308 C CG  . ASP E  4 73  ? 32.632  15.911  162.455 1.00 175.35 ?  72  ASP E CG  1 
ATOM   10309 O OD1 . ASP E  4 73  ? 31.482  15.436  162.368 1.00 174.84 ?  72  ASP E OD1 1 
ATOM   10310 O OD2 . ASP E  4 73  ? 33.454  15.529  163.319 1.00 176.04 -1 72  ASP E OD2 1 
ATOM   10311 N N   . LYS E  4 74  ? 29.698  16.957  160.145 1.00 178.13 ?  73  LYS E N   1 
ATOM   10312 C CA  . LYS E  4 74  ? 28.329  17.410  160.391 1.00 177.11 ?  73  LYS E CA  1 
ATOM   10313 C C   . LYS E  4 74  ? 27.922  17.311  161.860 1.00 174.61 ?  73  LYS E C   1 
ATOM   10314 O O   . LYS E  4 74  ? 27.138  18.141  162.338 1.00 169.92 ?  73  LYS E O   1 
ATOM   10315 C CB  . LYS E  4 74  ? 27.351  16.627  159.514 1.00 177.94 ?  73  LYS E CB  1 
ATOM   10316 C CG  . LYS E  4 74  ? 27.511  16.912  158.027 1.00 178.59 ?  73  LYS E CG  1 
ATOM   10317 C CD  . LYS E  4 74  ? 26.333  16.392  157.217 1.00 178.93 ?  73  LYS E CD  1 
ATOM   10318 C CE  . LYS E  4 74  ? 26.400  14.897  156.992 1.00 179.77 ?  73  LYS E CE  1 
ATOM   10319 N NZ  . LYS E  4 74  ? 25.408  14.479  155.963 1.00 180.19 1  73  LYS E NZ  1 
ATOM   10320 N N   . SER E  4 75  ? 28.428  16.305  162.582 1.00 175.75 ?  74  SER E N   1 
ATOM   10321 C CA  . SER E  4 75  ? 27.987  16.064  163.956 1.00 171.63 ?  74  SER E CA  1 
ATOM   10322 C C   . SER E  4 75  ? 28.289  17.242  164.876 1.00 167.66 ?  74  SER E C   1 
ATOM   10323 O O   . SER E  4 75  ? 27.506  17.543  165.785 1.00 162.73 ?  74  SER E O   1 
ATOM   10324 C CB  . SER E  4 75  ? 28.637  14.791  164.504 1.00 174.63 ?  74  SER E CB  1 
ATOM   10325 O OG  . SER E  4 75  ? 30.041  14.935  164.647 1.00 176.94 ?  74  SER E OG  1 
ATOM   10326 N N   . ILE E  4 76  ? 29.420  17.914  164.666 1.00 165.21 ?  75  ILE E N   1 
ATOM   10327 C CA  . ILE E  4 76  ? 29.802  19.064  165.477 1.00 161.96 ?  75  ILE E CA  1 
ATOM   10328 C C   . ILE E  4 76  ? 29.595  20.391  164.751 1.00 161.49 ?  75  ILE E C   1 
ATOM   10329 O O   . ILE E  4 76  ? 30.099  21.422  165.208 1.00 160.64 ?  75  ILE E O   1 
ATOM   10330 C CB  . ILE E  4 76  ? 31.256  18.922  165.953 1.00 164.28 ?  75  ILE E CB  1 
ATOM   10331 C CG1 . ILE E  4 76  ? 32.176  18.651  164.758 1.00 169.13 ?  75  ILE E CG1 1 
ATOM   10332 C CG2 . ILE E  4 76  ? 31.368  17.806  166.984 1.00 163.60 ?  75  ILE E CG2 1 
ATOM   10333 C CD1 . ILE E  4 76  ? 33.655  18.760  165.072 1.00 170.78 ?  75  ILE E CD1 1 
ATOM   10334 N N   . ASN E  4 77  ? 28.872  20.391  163.628 1.00 154.04 ?  76  ASN E N   1 
ATOM   10335 C CA  . ASN E  4 77  ? 28.528  21.621  162.906 1.00 155.05 ?  76  ASN E CA  1 
ATOM   10336 C C   . ASN E  4 77  ? 29.780  22.404  162.515 1.00 155.03 ?  76  ASN E C   1 
ATOM   10337 O O   . ASN E  4 77  ? 29.797  23.635  162.559 1.00 155.38 ?  76  ASN E O   1 
ATOM   10338 C CB  . ASN E  4 77  ? 27.585  22.515  163.721 1.00 155.20 ?  76  ASN E CB  1 
ATOM   10339 C CG  . ASN E  4 77  ? 26.298  21.822  164.107 1.00 155.81 ?  76  ASN E CG  1 
ATOM   10340 O OD1 . ASN E  4 77  ? 25.819  20.938  163.400 1.00 156.69 ?  76  ASN E OD1 1 
ATOM   10341 N ND2 . ASN E  4 77  ? 25.718  22.235  165.228 1.00 155.73 ?  76  ASN E ND2 1 
ATOM   10342 N N   . THR E  4 78  ? 30.841  21.689  162.138 1.00 159.10 ?  77  THR E N   1 
ATOM   10343 C CA  . THR E  4 78  ? 32.152  22.297  161.957 1.00 159.37 ?  77  THR E CA  1 
ATOM   10344 C C   . THR E  4 78  ? 32.717  21.961  160.579 1.00 160.95 ?  77  THR E C   1 
ATOM   10345 O O   . THR E  4 78  ? 32.646  20.812  160.131 1.00 161.36 ?  77  THR E O   1 
ATOM   10346 C CB  . THR E  4 78  ? 33.122  21.850  163.069 1.00 158.27 ?  77  THR E CB  1 
ATOM   10347 O OG1 . THR E  4 78  ? 32.635  22.307  164.337 1.00 157.05 ?  77  THR E OG1 1 
ATOM   10348 C CG2 . THR E  4 78  ? 34.502  22.443  162.852 1.00 159.11 ?  77  THR E CG2 1 
ATOM   10349 N N   . ALA E  4 79  ? 33.277  22.975  159.918 1.00 167.40 ?  78  ALA E N   1 
ATOM   10350 C CA  . ALA E  4 79  ? 34.015  22.853  158.666 1.00 169.26 ?  78  ALA E CA  1 
ATOM   10351 C C   . ALA E  4 79  ? 35.510  23.044  158.912 1.00 169.87 ?  78  ALA E C   1 
ATOM   10352 O O   . ALA E  4 79  ? 35.912  23.796  159.805 1.00 169.33 ?  78  ALA E O   1 
ATOM   10353 C CB  . ALA E  4 79  ? 33.525  23.875  157.635 1.00 170.87 ?  78  ALA E CB  1 
ATOM   10354 N N   . PHE E  4 80  ? 36.335  22.360  158.110 1.00 173.46 ?  79  PHE E N   1 
ATOM   10355 C CA  . PHE E  4 80  ? 37.790  22.449  158.207 1.00 174.71 ?  79  PHE E CA  1 
ATOM   10356 C C   . PHE E  4 80  ? 38.397  22.872  156.875 1.00 177.43 ?  79  PHE E C   1 
ATOM   10357 O O   . PHE E  4 80  ? 37.923  22.475  155.805 1.00 178.54 ?  79  PHE E O   1 
ATOM   10358 C CB  . PHE E  4 80  ? 38.444  21.115  158.619 1.00 174.70 ?  79  PHE E CB  1 
ATOM   10359 C CG  . PHE E  4 80  ? 37.911  20.530  159.892 1.00 172.41 ?  79  PHE E CG  1 
ATOM   10360 C CD1 . PHE E  4 80  ? 38.444  20.913  161.112 1.00 171.50 ?  79  PHE E CD1 1 
ATOM   10361 C CD2 . PHE E  4 80  ? 36.920  19.563  159.871 1.00 171.51 ?  79  PHE E CD2 1 
ATOM   10362 C CE1 . PHE E  4 80  ? 37.970  20.375  162.292 1.00 169.62 ?  79  PHE E CE1 1 
ATOM   10363 C CE2 . PHE E  4 80  ? 36.442  19.016  161.050 1.00 169.73 ?  79  PHE E CE2 1 
ATOM   10364 C CZ  . PHE E  4 80  ? 36.969  19.423  162.262 1.00 168.74 ?  79  PHE E CZ  1 
ATOM   10365 N N   . LEU E  4 81  ? 39.453  23.679  156.966 1.00 165.85 ?  80  LEU E N   1 
ATOM   10366 C CA  . LEU E  4 81  ? 40.259  24.120  155.833 1.00 168.90 ?  80  LEU E CA  1 
ATOM   10367 C C   . LEU E  4 81  ? 41.695  23.669  156.060 1.00 170.62 ?  80  LEU E C   1 
ATOM   10368 O O   . LEU E  4 81  ? 42.315  24.056  157.057 1.00 170.30 ?  80  LEU E O   1 
ATOM   10369 C CB  . LEU E  4 81  ? 40.195  25.641  155.689 1.00 169.85 ?  80  LEU E CB  1 
ATOM   10370 C CG  . LEU E  4 81  ? 40.918  26.280  154.508 1.00 173.34 ?  80  LEU E CG  1 
ATOM   10371 C CD1 . LEU E  4 81  ? 40.138  26.016  153.238 1.00 174.19 ?  80  LEU E CD1 1 
ATOM   10372 C CD2 . LEU E  4 81  ? 41.107  27.766  154.741 1.00 174.60 ?  80  LEU E CD2 1 
ATOM   10373 N N   . ASP E  4 82  ? 42.219  22.848  155.150 1.00 169.87 ?  81  ASP E N   1 
ATOM   10374 C CA  . ASP E  4 82  ? 43.622  22.445  155.167 1.00 172.40 ?  81  ASP E CA  1 
ATOM   10375 C C   . ASP E  4 82  ? 44.378  23.200  154.080 1.00 175.95 ?  81  ASP E C   1 
ATOM   10376 O O   . ASP E  4 82  ? 44.092  23.026  152.891 1.00 177.44 ?  81  ASP E O   1 
ATOM   10377 C CB  . ASP E  4 82  ? 43.753  20.938  154.943 1.00 172.96 ?  81  ASP E CB  1 
ATOM   10378 C CG  . ASP E  4 82  ? 43.227  20.124  156.106 1.00 170.14 ?  81  ASP E CG  1 
ATOM   10379 O OD1 . ASP E  4 82  ? 43.853  20.161  157.185 1.00 170.72 ?  81  ASP E OD1 1 
ATOM   10380 O OD2 . ASP E  4 82  ? 42.188  19.449  155.940 1.00 174.30 -1 81  ASP E OD2 1 
ATOM   10381 N N   . VAL E  4 83  ? 45.336  24.031  154.482 1.00 182.74 ?  82  VAL E N   1 
ATOM   10382 C CA  . VAL E  4 83  ? 46.219  24.733  153.554 1.00 186.72 ?  82  VAL E CA  1 
ATOM   10383 C C   . VAL E  4 83  ? 47.614  24.127  153.659 1.00 189.83 ?  82  VAL E C   1 
ATOM   10384 O O   . VAL E  4 83  ? 48.241  24.184  154.725 1.00 189.67 ?  82  VAL E O   1 
ATOM   10385 C CB  . VAL E  4 83  ? 46.247  26.242  153.836 1.00 187.31 ?  82  VAL E CB  1 
ATOM   10386 C CG1 . VAL E  4 83  ? 46.998  26.971  152.737 1.00 191.70 ?  82  VAL E CG1 1 
ATOM   10387 C CG2 . VAL E  4 83  ? 44.831  26.777  153.971 1.00 184.29 ?  82  VAL E CG2 1 
ATOM   10388 N N   . THR E  4 84  A 48.101  23.546  152.563 1.00 196.30 ?  82  THR E N   1 
ATOM   10389 C CA  . THR E  4 84  A 49.335  22.769  152.563 1.00 199.59 ?  82  THR E CA  1 
ATOM   10390 C C   . THR E  4 84  A 50.421  23.468  151.747 1.00 204.28 ?  82  THR E C   1 
ATOM   10391 O O   . THR E  4 84  A 50.174  24.454  151.046 1.00 205.46 ?  82  THR E O   1 
ATOM   10392 C CB  . THR E  4 84  A 49.084  21.355  152.019 1.00 199.33 ?  82  THR E CB  1 
ATOM   10393 O OG1 . THR E  4 84  A 48.887  21.407  150.600 1.00 203.00 ?  82  THR E OG1 1 
ATOM   10394 C CG2 . THR E  4 84  A 47.849  20.736  152.669 1.00 195.88 ?  82  THR E CG2 1 
ATOM   10395 N N   . ARG E  4 85  B 51.637  22.920  151.841 1.00 190.80 ?  82  ARG E N   1 
ATOM   10396 C CA  . ARG E  4 85  B 52.820  23.412  151.124 1.00 196.18 ?  82  ARG E CA  1 
ATOM   10397 C C   . ARG E  4 85  B 52.971  24.928  151.262 1.00 197.11 ?  82  ARG E C   1 
ATOM   10398 O O   . ARG E  4 85  B 53.114  25.663  150.282 1.00 200.00 ?  82  ARG E O   1 
ATOM   10399 C CB  . ARG E  4 85  B 52.803  22.975  149.656 1.00 198.93 ?  82  ARG E CB  1 
ATOM   10400 C CG  . ARG E  4 85  B 52.537  21.481  149.462 1.00 198.14 ?  82  ARG E CG  1 
ATOM   10401 C CD  . ARG E  4 85  B 52.902  21.020  148.054 1.00 202.30 ?  82  ARG E CD  1 
ATOM   10402 N NE  . ARG E  4 85  B 52.182  21.733  147.003 1.00 202.35 ?  82  ARG E NE  1 
ATOM   10403 C CZ  . ARG E  4 85  B 50.993  21.371  146.532 1.00 199.64 ?  82  ARG E CZ  1 
ATOM   10404 N NH1 . ARG E  4 85  B 50.373  20.315  147.038 1.00 196.64 1  82  ARG E NH1 1 
ATOM   10405 N NH2 . ARG E  4 85  B 50.415  22.077  145.569 1.00 200.24 ?  82  ARG E NH2 1 
ATOM   10406 N N   . LEU E  4 86  C 52.936  25.388  152.509 1.00 203.01 ?  82  LEU E N   1 
ATOM   10407 C CA  . LEU E  4 86  C 52.864  26.810  152.817 1.00 203.23 ?  82  LEU E CA  1 
ATOM   10408 C C   . LEU E  4 86  C 54.117  27.562  152.381 1.00 208.94 ?  82  LEU E C   1 
ATOM   10409 O O   . LEU E  4 86  C 55.232  27.032  152.401 1.00 212.47 ?  82  LEU E O   1 
ATOM   10410 C CB  . LEU E  4 86  C 52.643  27.023  154.314 1.00 200.00 ?  82  LEU E CB  1 
ATOM   10411 C CG  . LEU E  4 86  C 51.268  26.638  154.856 1.00 194.32 ?  82  LEU E CG  1 
ATOM   10412 C CD1 . LEU E  4 86  C 51.288  26.567  156.371 1.00 191.96 ?  82  LEU E CD1 1 
ATOM   10413 C CD2 . LEU E  4 86  C 50.224  27.631  154.388 1.00 192.73 ?  82  LEU E CD2 1 
ATOM   10414 N N   . THR E  4 87  ? 53.914  28.813  151.969 1.00 207.16 ?  83  THR E N   1 
ATOM   10415 C CA  . THR E  4 87  ? 54.982  29.787  151.782 1.00 212.41 ?  83  THR E CA  1 
ATOM   10416 C C   . THR E  4 87  ? 54.562  31.083  152.468 1.00 211.15 ?  83  THR E C   1 
ATOM   10417 O O   . THR E  4 87  ? 53.445  31.203  152.979 1.00 206.42 ?  83  THR E O   1 
ATOM   10418 C CB  . THR E  4 87  ? 55.284  30.040  150.297 1.00 216.79 ?  83  THR E CB  1 
ATOM   10419 O OG1 . THR E  4 87  ? 54.303  30.933  149.752 1.00 215.40 ?  83  THR E OG1 1 
ATOM   10420 C CG2 . THR E  4 87  ? 55.287  28.743  149.509 1.00 217.08 ?  83  THR E CG2 1 
ATOM   10421 N N   . SER E  4 88  ? 55.466  32.067  152.478 1.00 221.73 ?  84  SER E N   1 
ATOM   10422 C CA  . SER E  4 88  ? 55.173  33.340  153.132 1.00 221.44 ?  84  SER E CA  1 
ATOM   10423 C C   . SER E  4 88  ? 54.011  34.079  152.480 1.00 219.81 ?  84  SER E C   1 
ATOM   10424 O O   . SER E  4 88  ? 53.396  34.936  153.124 1.00 218.28 ?  84  SER E O   1 
ATOM   10425 C CB  . SER E  4 88  ? 56.417  34.227  153.146 1.00 227.56 ?  84  SER E CB  1 
ATOM   10426 O OG  . SER E  4 88  ? 56.918  34.427  151.838 1.00 232.50 ?  84  SER E OG  1 
ATOM   10427 N N   . ASP E  4 89  ? 53.700  33.769  151.222 1.00 214.11 ?  85  ASP E N   1 
ATOM   10428 C CA  . ASP E  4 89  ? 52.584  34.391  150.524 1.00 212.87 ?  85  ASP E CA  1 
ATOM   10429 C C   . ASP E  4 89  ? 51.234  34.002  151.111 1.00 206.74 ?  85  ASP E C   1 
ATOM   10430 O O   . ASP E  4 89  ? 50.230  34.653  150.802 1.00 205.40 ?  85  ASP E O   1 
ATOM   10431 C CB  . ASP E  4 89  ? 52.626  34.006  149.047 1.00 215.25 ?  85  ASP E CB  1 
ATOM   10432 C CG  . ASP E  4 89  ? 51.738  34.878  148.196 1.00 218.82 ?  85  ASP E CG  1 
ATOM   10433 O OD1 . ASP E  4 89  ? 51.834  36.118  148.312 1.00 225.74 ?  85  ASP E OD1 1 
ATOM   10434 O OD2 . ASP E  4 89  ? 50.933  34.320  147.423 1.00 219.20 -1 85  ASP E OD2 1 
ATOM   10435 N N   . ASP E  4 90  ? 51.188  32.968  151.943 1.00 205.19 ?  86  ASP E N   1 
ATOM   10436 C CA  . ASP E  4 90  ? 49.950  32.491  152.539 1.00 199.59 ?  86  ASP E CA  1 
ATOM   10437 C C   . ASP E  4 90  ? 49.632  33.158  153.873 1.00 197.27 ?  86  ASP E C   1 
ATOM   10438 O O   . ASP E  4 90  ? 48.600  32.844  154.475 1.00 192.81 ?  86  ASP E O   1 
ATOM   10439 C CB  . ASP E  4 90  ? 50.030  30.972  152.717 1.00 197.39 ?  86  ASP E CB  1 
ATOM   10440 C CG  . ASP E  4 90  ? 50.124  30.240  151.392 1.00 199.33 ?  86  ASP E CG  1 
ATOM   10441 O OD1 . ASP E  4 90  ? 49.334  30.559  150.480 1.00 199.31 ?  86  ASP E OD1 1 
ATOM   10442 O OD2 . ASP E  4 90  ? 51.002  29.362  151.253 1.00 201.17 -1 86  ASP E OD2 1 
ATOM   10443 N N   . THR E  4 91  ? 50.497  34.054  154.350 1.00 196.57 ?  87  THR E N   1 
ATOM   10444 C CA  . THR E  4 91  ? 50.231  34.808  155.571 1.00 195.08 ?  87  THR E CA  1 
ATOM   10445 C C   . THR E  4 91  ? 49.012  35.710  155.394 1.00 193.55 ?  87  THR E C   1 
ATOM   10446 O O   . THR E  4 91  ? 48.892  36.417  154.388 1.00 196.46 ?  87  THR E O   1 
ATOM   10447 C CB  . THR E  4 91  ? 51.460  35.637  155.948 1.00 199.79 ?  87  THR E CB  1 
ATOM   10448 O OG1 . THR E  4 91  ? 52.524  34.763  156.346 1.00 200.83 ?  87  THR E OG1 1 
ATOM   10449 C CG2 . THR E  4 91  ? 51.142  36.579  157.101 1.00 198.93 ?  87  THR E CG2 1 
ATOM   10450 N N   . GLY E  4 92  ? 48.117  35.689  156.374 1.00 186.15 ?  88  GLY E N   1 
ATOM   10451 C CA  . GLY E  4 92  ? 46.937  36.528  156.337 1.00 185.56 ?  88  GLY E CA  1 
ATOM   10452 C C   . GLY E  4 92  ? 45.872  36.028  157.298 1.00 180.75 ?  88  GLY E C   1 
ATOM   10453 O O   . GLY E  4 92  ? 46.092  35.098  158.073 1.00 178.18 ?  88  GLY E O   1 
ATOM   10454 N N   . ILE E  4 93  ? 44.710  36.686  157.230 1.00 174.39 ?  89  ILE E N   1 
ATOM   10455 C CA  . ILE E  4 93  ? 43.529  36.320  158.011 1.00 170.46 ?  89  ILE E CA  1 
ATOM   10456 C C   . ILE E  4 93  ? 42.599  35.489  157.136 1.00 167.74 ?  89  ILE E C   1 
ATOM   10457 O O   . ILE E  4 93  ? 42.253  35.898  156.019 1.00 170.15 ?  89  ILE E O   1 
ATOM   10458 C CB  . ILE E  4 93  ? 42.808  37.570  158.543 1.00 171.16 ?  89  ILE E CB  1 
ATOM   10459 C CG1 . ILE E  4 93  ? 43.707  38.328  159.519 1.00 175.92 ?  89  ILE E CG1 1 
ATOM   10460 C CG2 . ILE E  4 93  ? 41.503  37.189  159.231 1.00 168.51 ?  89  ILE E CG2 1 
ATOM   10461 C CD1 . ILE E  4 93  ? 43.056  39.550  160.123 1.00 182.05 ?  89  ILE E CD1 1 
ATOM   10462 N N   . TYR E  4 94  ? 42.187  34.328  157.649 1.00 174.99 ?  90  TYR E N   1 
ATOM   10463 C CA  . TYR E  4 94  ? 41.313  33.388  156.953 1.00 172.51 ?  90  TYR E CA  1 
ATOM   10464 C C   . TYR E  4 94  ? 39.914  33.427  157.559 1.00 170.33 ?  90  TYR E C   1 
ATOM   10465 O O   . TYR E  4 94  ? 39.749  33.206  158.765 1.00 169.09 ?  90  TYR E O   1 
ATOM   10466 C CB  . TYR E  4 94  ? 41.885  31.971  157.028 1.00 172.12 ?  90  TYR E CB  1 
ATOM   10467 C CG  . TYR E  4 94  ? 43.123  31.770  156.176 1.00 174.94 ?  90  TYR E CG  1 
ATOM   10468 C CD1 . TYR E  4 94  ? 44.336  32.348  156.534 1.00 178.29 ?  90  TYR E CD1 1 
ATOM   10469 C CD2 . TYR E  4 94  ? 43.075  31.023  155.005 1.00 175.59 ?  90  TYR E CD2 1 
ATOM   10470 C CE1 . TYR E  4 94  ? 45.471  32.175  155.758 1.00 181.07 ?  90  TYR E CE1 1 
ATOM   10471 C CE2 . TYR E  4 94  ? 44.206  30.847  154.220 1.00 178.56 ?  90  TYR E CE2 1 
ATOM   10472 C CZ  . TYR E  4 94  ? 45.400  31.425  154.602 1.00 181.40 ?  90  TYR E CZ  1 
ATOM   10473 O OH  . TYR E  4 94  ? 46.522  31.252  153.823 1.00 186.19 ?  90  TYR E OH  1 
ATOM   10474 N N   . TYR E  4 95  ? 38.912  33.684  156.719 1.00 161.85 ?  91  TYR E N   1 
ATOM   10475 C CA  . TYR E  4 95  ? 37.513  33.734  157.124 1.00 159.59 ?  91  TYR E CA  1 
ATOM   10476 C C   . TYR E  4 95  ? 36.728  32.562  156.553 1.00 158.41 ?  91  TYR E C   1 
ATOM   10477 O O   . TYR E  4 95  ? 36.958  32.144  155.414 1.00 159.50 ?  91  TYR E O   1 
ATOM   10478 C CB  . TYR E  4 95  ? 36.827  35.022  156.655 1.00 163.14 ?  91  TYR E CB  1 
ATOM   10479 C CG  . TYR E  4 95  ? 37.404  36.307  157.189 1.00 165.24 ?  91  TYR E CG  1 
ATOM   10480 C CD1 . TYR E  4 95  ? 37.039  36.777  158.443 1.00 164.16 ?  91  TYR E CD1 1 
ATOM   10481 C CD2 . TYR E  4 95  ? 38.270  37.076  156.425 1.00 170.07 ?  91  TYR E CD2 1 
ATOM   10482 C CE1 . TYR E  4 95  ? 37.546  37.961  158.937 1.00 167.65 ?  91  TYR E CE1 1 
ATOM   10483 C CE2 . TYR E  4 95  ? 38.782  38.263  156.909 1.00 172.72 ?  91  TYR E CE2 1 
ATOM   10484 C CZ  . TYR E  4 95  ? 38.416  38.701  158.164 1.00 172.43 ?  91  TYR E CZ  1 
ATOM   10485 O OH  . TYR E  4 95  ? 38.931  39.882  158.647 1.00 177.69 ?  91  TYR E OH  1 
ATOM   10486 N N   . CYS E  4 96  ? 35.799  32.039  157.346 1.00 150.37 ?  92  CYS E N   1 
ATOM   10487 C CA  . CYS E  4 96  ? 34.700  31.257  156.806 1.00 149.37 ?  92  CYS E CA  1 
ATOM   10488 C C   . CYS E  4 96  ? 33.492  32.176  156.696 1.00 150.51 ?  92  CYS E C   1 
ATOM   10489 O O   . CYS E  4 96  ? 33.279  33.037  157.556 1.00 151.11 ?  92  CYS E O   1 
ATOM   10490 C CB  . CYS E  4 96  ? 34.368  30.048  157.682 1.00 146.98 ?  92  CYS E CB  1 
ATOM   10491 S SG  . CYS E  4 96  ? 33.947  30.371  159.406 1.00 145.92 ?  92  CYS E SG  1 
ATOM   10492 N N   . ALA E  4 97  ? 32.693  31.984  155.650 1.00 149.48 ?  93  ALA E N   1 
ATOM   10493 C CA  . ALA E  4 97  ? 31.535  32.842  155.438 1.00 151.11 ?  93  ALA E CA  1 
ATOM   10494 C C   . ALA E  4 97  ? 30.401  32.039  154.827 1.00 150.98 ?  93  ALA E C   1 
ATOM   10495 O O   . ALA E  4 97  ? 30.584  31.393  153.793 1.00 151.71 ?  93  ALA E O   1 
ATOM   10496 C CB  . ALA E  4 97  ? 31.885  34.029  154.533 1.00 154.55 ?  93  ALA E CB  1 
ATOM   10497 N N   . ARG E  4 98  ? 29.238  32.085  155.468 1.00 162.17 ?  94  ARG E N   1 
ATOM   10498 C CA  . ARG E  4 98  ? 28.066  31.383  154.967 1.00 162.47 ?  94  ARG E CA  1 
ATOM   10499 C C   . ARG E  4 98  ? 27.479  32.121  153.771 1.00 165.86 ?  94  ARG E C   1 
ATOM   10500 O O   . ARG E  4 98  ? 27.399  33.351  153.772 1.00 167.98 ?  94  ARG E O   1 
ATOM   10501 C CB  . ARG E  4 98  ? 27.013  31.275  156.065 1.00 161.40 ?  94  ARG E CB  1 
ATOM   10502 C CG  . ARG E  4 98  ? 25.787  30.504  155.661 1.00 161.97 ?  94  ARG E CG  1 
ATOM   10503 C CD  . ARG E  4 98  ? 24.730  30.579  156.739 1.00 161.73 ?  94  ARG E CD  1 
ATOM   10504 N NE  . ARG E  4 98  ? 24.004  31.844  156.667 1.00 164.66 ?  94  ARG E NE  1 
ATOM   10505 C CZ  . ARG E  4 98  ? 23.041  32.206  157.508 1.00 165.51 ?  94  ARG E CZ  1 
ATOM   10506 N NH1 . ARG E  4 98  ? 22.695  31.405  158.506 1.00 163.67 1  94  ARG E NH1 1 
ATOM   10507 N NH2 . ARG E  4 98  ? 22.435  33.377  157.362 1.00 168.69 ?  94  ARG E NH2 1 
ATOM   10508 N N   . ASP E  4 99  ? 27.046  31.369  152.759 1.00 156.75 ?  95  ASP E N   1 
ATOM   10509 C CA  . ASP E  4 99  ? 26.283  31.948  151.661 1.00 160.14 ?  95  ASP E CA  1 
ATOM   10510 C C   . ASP E  4 99  ? 24.790  31.813  151.937 1.00 160.92 ?  95  ASP E C   1 
ATOM   10511 O O   . ASP E  4 99  ? 24.335  30.786  152.446 1.00 159.05 ?  95  ASP E O   1 
ATOM   10512 C CB  . ASP E  4 99  ? 26.637  31.275  150.334 1.00 161.25 ?  95  ASP E CB  1 
ATOM   10513 C CG  . ASP E  4 99  ? 26.416  32.189  149.140 1.00 165.15 ?  95  ASP E CG  1 
ATOM   10514 O OD1 . ASP E  4 99  ? 25.242  32.480  148.828 1.00 167.23 ?  95  ASP E OD1 1 
ATOM   10515 O OD2 . ASP E  4 99  ? 27.411  32.611  148.511 1.00 166.44 -1 95  ASP E OD2 1 
ATOM   10516 N N   . LYS E  4 100 ? 24.033  32.865  151.606 1.00 156.73 ?  96  LYS E N   1 
ATOM   10517 C CA  . LYS E  4 100 ? 22.574  32.780  151.648 1.00 158.52 ?  96  LYS E CA  1 
ATOM   10518 C C   . LYS E  4 100 ? 22.065  31.591  150.841 1.00 158.71 ?  96  LYS E C   1 
ATOM   10519 O O   . LYS E  4 100 ? 21.113  30.914  151.247 1.00 158.63 ?  96  LYS E O   1 
ATOM   10520 C CB  . LYS E  4 100 ? 21.961  34.095  151.165 1.00 162.69 ?  96  LYS E CB  1 
ATOM   10521 C CG  . LYS E  4 100 ? 22.341  35.277  152.054 1.00 163.00 ?  96  LYS E CG  1 
ATOM   10522 C CD  . LYS E  4 100 ? 21.902  36.603  151.462 1.00 167.55 ?  96  LYS E CD  1 
ATOM   10523 C CE  . LYS E  4 100 ? 20.389  36.715  151.458 1.00 170.44 ?  96  LYS E CE  1 
ATOM   10524 N NZ  . LYS E  4 100 ? 19.850  36.900  152.835 1.00 169.56 1  96  LYS E NZ  1 
ATOM   10525 N N   . TYR E  4 101 ? 22.686  31.332  149.689 1.00 167.65 ?  97  TYR E N   1 
ATOM   10526 C CA  . TYR E  4 101 ? 22.457  30.124  148.894 1.00 167.68 ?  97  TYR E CA  1 
ATOM   10527 C C   . TYR E  4 101 ? 21.014  29.989  148.397 1.00 170.64 ?  97  TYR E C   1 
ATOM   10528 O O   . TYR E  4 101 ? 20.520  28.873  148.207 1.00 170.35 ?  97  TYR E O   1 
ATOM   10529 C CB  . TYR E  4 101 ? 22.890  28.876  149.672 1.00 164.00 ?  97  TYR E CB  1 
ATOM   10530 C CG  . TYR E  4 101 ? 23.364  27.742  148.791 1.00 163.77 ?  97  TYR E CG  1 
ATOM   10531 C CD1 . TYR E  4 101 ? 24.385  27.932  147.866 1.00 164.62 ?  97  TYR E CD1 1 
ATOM   10532 C CD2 . TYR E  4 101 ? 22.798  26.479  148.889 1.00 163.08 ?  97  TYR E CD2 1 
ATOM   10533 C CE1 . TYR E  4 101 ? 24.828  26.894  147.062 1.00 164.79 ?  97  TYR E CE1 1 
ATOM   10534 C CE2 . TYR E  4 101 ? 23.230  25.437  148.087 1.00 163.26 ?  97  TYR E CE2 1 
ATOM   10535 C CZ  . TYR E  4 101 ? 24.245  25.650  147.175 1.00 164.11 ?  97  TYR E CZ  1 
ATOM   10536 O OH  . TYR E  4 101 ? 24.670  24.619  146.366 1.00 164.71 ?  97  TYR E OH  1 
ATOM   10537 N N   . TYR E  4 102 ? 20.309  31.108  148.209 1.00 172.12 ?  98  TYR E N   1 
ATOM   10538 C CA  . TYR E  4 102 ? 18.986  31.045  147.595 1.00 176.78 ?  98  TYR E CA  1 
ATOM   10539 C C   . TYR E  4 102 ? 19.056  30.319  146.260 1.00 177.39 ?  98  TYR E C   1 
ATOM   10540 O O   . TYR E  4 102 ? 19.980  30.526  145.468 1.00 178.09 ?  98  TYR E O   1 
ATOM   10541 C CB  . TYR E  4 102 ? 18.402  32.443  147.385 1.00 179.57 ?  98  TYR E CB  1 
ATOM   10542 C CG  . TYR E  4 102 ? 18.121  33.212  148.654 1.00 180.43 ?  98  TYR E CG  1 
ATOM   10543 C CD1 . TYR E  4 102 ? 18.000  32.564  149.879 1.00 178.70 ?  98  TYR E CD1 1 
ATOM   10544 C CD2 . TYR E  4 102 ? 17.945  34.588  148.623 1.00 184.61 ?  98  TYR E CD2 1 
ATOM   10545 C CE1 . TYR E  4 102 ? 17.736  33.274  151.045 1.00 180.04 ?  98  TYR E CE1 1 
ATOM   10546 C CE2 . TYR E  4 102 ? 17.675  35.305  149.779 1.00 184.73 ?  98  TYR E CE2 1 
ATOM   10547 C CZ  . TYR E  4 102 ? 17.573  34.644  150.990 1.00 183.30 ?  98  TYR E CZ  1 
ATOM   10548 O OH  . TYR E  4 102 ? 17.303  35.348  152.145 1.00 185.87 ?  98  TYR E OH  1 
ATOM   10549 N N   . GLY E  4 103 ? 18.062  29.470  146.010 1.00 174.23 ?  99  GLY E N   1 
ATOM   10550 C CA  . GLY E  4 103 ? 18.047  28.734  144.764 1.00 175.94 ?  99  GLY E CA  1 
ATOM   10551 C C   . GLY E  4 103 ? 19.186  27.754  144.620 1.00 172.86 ?  99  GLY E C   1 
ATOM   10552 O O   . GLY E  4 103 ? 19.471  27.314  143.504 1.00 175.52 ?  99  GLY E O   1 
ATOM   10553 N N   . ASN E  4 104 ? 19.844  27.401  145.728 1.00 161.79 ?  100 ASN E N   1 
ATOM   10554 C CA  . ASN E  4 104 ? 21.001  26.504  145.729 1.00 158.92 ?  100 ASN E CA  1 
ATOM   10555 C C   . ASN E  4 104 ? 22.112  27.035  144.826 1.00 159.67 ?  100 ASN E C   1 
ATOM   10556 O O   . ASN E  4 104 ? 22.807  26.276  144.148 1.00 159.40 ?  100 ASN E O   1 
ATOM   10557 C CB  . ASN E  4 104 ? 20.608  25.078  145.329 1.00 159.31 ?  100 ASN E CB  1 
ATOM   10558 C CG  . ASN E  4 104 ? 19.543  24.485  146.238 1.00 158.93 ?  100 ASN E CG  1 
ATOM   10559 O OD1 . ASN E  4 104 ? 19.726  24.375  147.452 1.00 156.10 ?  100 ASN E OD1 1 
ATOM   10560 N ND2 . ASN E  4 104 ? 18.422  24.094  145.646 1.00 162.08 ?  100 ASN E ND2 1 
ATOM   10561 N N   . GLU E  4 105 A 22.298  28.354  144.838 1.00 166.76 ?  100 GLU E N   1 
ATOM   10562 C CA  . GLU E  4 105 A 23.397  28.985  144.125 1.00 168.02 ?  100 GLU E CA  1 
ATOM   10563 C C   . GLU E  4 105 A 23.943  30.121  144.973 1.00 166.68 ?  100 GLU E C   1 
ATOM   10564 O O   . GLU E  4 105 A 23.295  30.589  145.911 1.00 165.92 ?  100 GLU E O   1 
ATOM   10565 C CB  . GLU E  4 105 A 22.948  29.512  142.755 1.00 174.74 ?  100 GLU E CB  1 
ATOM   10566 C CG  . GLU E  4 105 A 21.845  30.554  142.829 1.00 179.47 ?  100 GLU E CG  1 
ATOM   10567 C CD  . GLU E  4 105 A 21.429  31.059  141.463 1.00 185.97 ?  100 GLU E CD  1 
ATOM   10568 O OE1 . GLU E  4 105 A 20.602  31.993  141.406 1.00 191.98 ?  100 GLU E OE1 1 
ATOM   10569 O OE2 . GLU E  4 105 A 21.933  30.530  140.450 1.00 185.74 -1 100 GLU E OE2 1 
ATOM   10570 N N   . ALA E  4 106 B 25.140  30.576  144.615 1.00 168.55 ?  100 ALA E N   1 
ATOM   10571 C CA  . ALA E  4 106 B 25.764  31.678  145.333 1.00 168.05 ?  100 ALA E CA  1 
ATOM   10572 C C   . ALA E  4 106 B 24.959  32.961  145.165 1.00 171.30 ?  100 ALA E C   1 
ATOM   10573 O O   . ALA E  4 106 B 24.575  33.329  144.051 1.00 174.77 ?  100 ALA E O   1 
ATOM   10574 C CB  . ALA E  4 106 B 27.200  31.875  144.847 1.00 168.36 ?  100 ALA E CB  1 
ATOM   10575 N N   . VAL E  4 107 C 24.686  33.629  146.285 1.00 171.17 ?  100 VAL E N   1 
ATOM   10576 C CA  . VAL E  4 107 C 23.903  34.861  146.293 1.00 174.36 ?  100 VAL E CA  1 
ATOM   10577 C C   . VAL E  4 107 C 24.688  35.932  147.045 1.00 174.16 ?  100 VAL E C   1 
ATOM   10578 O O   . VAL E  4 107 C 24.856  37.055  146.555 1.00 177.49 ?  100 VAL E O   1 
ATOM   10579 C CB  . VAL E  4 107 C 22.507  34.641  146.905 1.00 174.47 ?  100 VAL E CB  1 
ATOM   10580 C CG1 . VAL E  4 107 C 21.769  35.957  147.004 1.00 178.13 ?  100 VAL E CG1 1 
ATOM   10581 C CG2 . VAL E  4 107 C 21.705  33.656  146.058 1.00 175.54 ?  100 VAL E CG2 1 
ATOM   10582 N N   . GLY E  4 108 D 25.161  35.595  148.239 1.00 175.86 ?  100 GLY E N   1 
ATOM   10583 C CA  . GLY E  4 108 D 25.967  36.519  149.020 1.00 175.55 ?  100 GLY E CA  1 
ATOM   10584 C C   . GLY E  4 108 D 26.336  35.902  150.353 1.00 171.42 ?  100 GLY E C   1 
ATOM   10585 O O   . GLY E  4 108 D 25.673  34.981  150.843 1.00 169.14 ?  100 GLY E O   1 
ATOM   10586 N N   . MET E  4 109 E 27.412  36.435  150.936 1.00 161.65 ?  100 MET E N   1 
ATOM   10587 C CA  . MET E  4 109 E 27.994  35.890  152.163 1.00 157.73 ?  100 MET E CA  1 
ATOM   10588 C C   . MET E  4 109 E 27.473  36.736  153.321 1.00 158.53 ?  100 MET E C   1 
ATOM   10589 O O   . MET E  4 109 E 27.979  37.830  153.584 1.00 160.13 ?  100 MET E O   1 
ATOM   10590 C CB  . MET E  4 109 E 29.517  35.896  152.081 1.00 157.77 ?  100 MET E CB  1 
ATOM   10591 C CG  . MET E  4 109 E 30.062  35.148  150.869 1.00 158.69 ?  100 MET E CG  1 
ATOM   10592 S SD  . MET E  4 109 E 31.862  35.127  150.767 1.00 159.43 ?  100 MET E SD  1 
ATOM   10593 C CE  . MET E  4 109 E 32.086  34.492  149.107 1.00 160.86 ?  100 MET E CE  1 
ATOM   10594 N N   . ASP E  4 110 ? 26.460  36.219  154.018 1.00 167.62 ?  101 ASP E N   1 
ATOM   10595 C CA  . ASP E  4 110 ? 25.724  37.011  154.996 1.00 168.86 ?  101 ASP E CA  1 
ATOM   10596 C C   . ASP E  4 110 ? 26.200  36.875  156.438 1.00 167.59 ?  101 ASP E C   1 
ATOM   10597 O O   . ASP E  4 110 ? 25.902  37.759  157.249 1.00 169.97 ?  101 ASP E O   1 
ATOM   10598 C CB  . ASP E  4 110 ? 24.237  36.642  154.945 1.00 170.31 ?  101 ASP E CB  1 
ATOM   10599 C CG  . ASP E  4 110 ? 23.980  35.208  155.365 1.00 168.31 ?  101 ASP E CG  1 
ATOM   10600 O OD1 . ASP E  4 110 ? 24.940  34.407  155.382 1.00 165.08 ?  101 ASP E OD1 1 
ATOM   10601 O OD2 . ASP E  4 110 ? 22.820  34.885  155.693 1.00 170.37 -1 101 ASP E OD2 1 
ATOM   10602 N N   . VAL E  4 111 ? 26.925  35.813  156.785 1.00 160.74 ?  102 VAL E N   1 
ATOM   10603 C CA  . VAL E  4 111 ? 27.465  35.643  158.131 1.00 158.18 ?  102 VAL E CA  1 
ATOM   10604 C C   . VAL E  4 111 ? 28.928  35.246  158.028 1.00 156.49 ?  102 VAL E C   1 
ATOM   10605 O O   . VAL E  4 111 ? 29.265  34.259  157.365 1.00 155.39 ?  102 VAL E O   1 
ATOM   10606 C CB  . VAL E  4 111 ? 26.674  34.600  158.944 1.00 155.73 ?  102 VAL E CB  1 
ATOM   10607 C CG1 . VAL E  4 111 ? 27.382  34.314  160.263 1.00 153.14 ?  102 VAL E CG1 1 
ATOM   10608 C CG2 . VAL E  4 111 ? 25.247  35.087  159.194 1.00 157.94 ?  102 VAL E CG2 1 
ATOM   10609 N N   . TRP E  4 112 ? 29.792  36.009  158.685 1.00 161.54 ?  103 TRP E N   1 
ATOM   10610 C CA  . TRP E  4 112 ? 31.221  35.758  158.653 1.00 160.62 ?  103 TRP E CA  1 
ATOM   10611 C C   . TRP E  4 112 ? 31.742  35.381  160.029 1.00 158.05 ?  103 TRP E C   1 
ATOM   10612 O O   . TRP E  4 112 ? 31.314  35.939  161.045 1.00 158.06 ?  103 TRP E O   1 
ATOM   10613 C CB  . TRP E  4 112 ? 31.964  36.988  158.159 1.00 163.88 ?  103 TRP E CB  1 
ATOM   10614 C CG  . TRP E  4 112 ? 31.711  37.301  156.731 1.00 166.57 ?  103 TRP E CG  1 
ATOM   10615 C CD1 . TRP E  4 112 ? 30.526  37.678  156.168 1.00 168.43 ?  103 TRP E CD1 1 
ATOM   10616 C CD2 . TRP E  4 112 ? 32.675  37.298  155.675 1.00 168.20 ?  103 TRP E CD2 1 
ATOM   10617 N NE1 . TRP E  4 112 ? 30.691  37.894  154.821 1.00 170.96 ?  103 TRP E NE1 1 
ATOM   10618 C CE2 . TRP E  4 112 ? 32.002  37.669  154.494 1.00 170.86 ?  103 TRP E CE2 1 
ATOM   10619 C CE3 . TRP E  4 112 ? 34.041  37.011  155.613 1.00 168.00 ?  103 TRP E CE3 1 
ATOM   10620 C CZ2 . TRP E  4 112 ? 32.650  37.761  153.266 1.00 173.20 ?  103 TRP E CZ2 1 
ATOM   10621 C CZ3 . TRP E  4 112 ? 34.682  37.103  154.395 1.00 170.46 ?  103 TRP E CZ3 1 
ATOM   10622 C CH2 . TRP E  4 112 ? 33.987  37.474  153.236 1.00 172.96 ?  103 TRP E CH2 1 
ATOM   10623 N N   . GLY E  4 113 ? 32.663  34.429  160.046 1.00 152.40 ?  104 GLY E N   1 
ATOM   10624 C CA  . GLY E  4 113 ? 33.443  34.167  161.231 1.00 150.56 ?  104 GLY E CA  1 
ATOM   10625 C C   . GLY E  4 113 ? 34.341  35.340  161.565 1.00 152.68 ?  104 GLY E C   1 
ATOM   10626 O O   . GLY E  4 113 ? 34.488  36.299  160.806 1.00 155.58 ?  104 GLY E O   1 
ATOM   10627 N N   . GLN E  4 114 ? 34.966  35.257  162.735 1.00 155.73 ?  105 GLN E N   1 
ATOM   10628 C CA  . GLN E  4 114 ? 35.806  36.359  163.173 1.00 157.97 ?  105 GLN E CA  1 
ATOM   10629 C C   . GLN E  4 114 ? 37.177  36.350  162.514 1.00 159.69 ?  105 GLN E C   1 
ATOM   10630 O O   . GLN E  4 114 ? 37.920  37.328  162.649 1.00 162.51 ?  105 GLN E O   1 
ATOM   10631 C CB  . GLN E  4 114 ? 35.997  36.276  164.689 1.00 156.37 ?  105 GLN E CB  1 
ATOM   10632 C CG  . GLN E  4 114 ? 37.130  35.321  165.083 1.00 154.85 ?  105 GLN E CG  1 
ATOM   10633 C CD  . GLN E  4 114 ? 36.708  33.856  165.088 1.00 151.80 ?  105 GLN E CD  1 
ATOM   10634 O OE1 . GLN E  4 114 ? 35.688  33.486  164.504 1.00 150.97 ?  105 GLN E OE1 1 
ATOM   10635 N NE2 . GLN E  4 114 ? 37.517  33.011  165.720 1.00 150.55 ?  105 GLN E NE2 1 
ATOM   10636 N N   . GLY E  4 115 ? 37.520  35.290  161.801 1.00 148.46 ?  106 GLY E N   1 
ATOM   10637 C CA  . GLY E  4 115 ? 38.800  35.198  161.121 1.00 148.58 ?  106 GLY E CA  1 
ATOM   10638 C C   . GLY E  4 115 ? 39.840  34.501  161.973 1.00 148.54 ?  106 GLY E C   1 
ATOM   10639 O O   . GLY E  4 115 ? 39.831  34.567  163.201 1.00 148.51 ?  106 GLY E O   1 
ATOM   10640 N N   . THR E  4 116 ? 40.752  33.803  161.307 1.00 158.95 ?  107 THR E N   1 
ATOM   10641 C CA  . THR E  4 116 ? 41.874  33.154  161.973 1.00 158.78 ?  107 THR E CA  1 
ATOM   10642 C C   . THR E  4 116 ? 43.159  33.649  161.333 1.00 162.62 ?  107 THR E C   1 
ATOM   10643 O O   . THR E  4 116 ? 43.368  33.453  160.131 1.00 164.17 ?  107 THR E O   1 
ATOM   10644 C CB  . THR E  4 116 ? 41.798  31.635  161.900 1.00 156.49 ?  107 THR E CB  1 
ATOM   10645 O OG1 . THR E  4 116 ? 40.608  31.181  162.555 1.00 153.22 ?  107 THR E OG1 1 
ATOM   10646 C CG2 . THR E  4 116 ? 43.018  31.037  162.583 1.00 156.97 ?  107 THR E CG2 1 
ATOM   10647 N N   . SER E  4 117 ? 44.018  34.274  162.128 1.00 173.59 ?  108 SER E N   1 
ATOM   10648 C CA  . SER E  4 117 ? 45.314  34.719  161.638 1.00 177.71 ?  108 SER E CA  1 
ATOM   10649 C C   . SER E  4 117 ? 46.291  33.553  161.492 1.00 178.18 ?  108 SER E C   1 
ATOM   10650 O O   . SER E  4 117 ? 46.509  32.794  162.440 1.00 176.18 ?  108 SER E O   1 
ATOM   10651 C CB  . SER E  4 117 ? 45.887  35.762  162.593 1.00 179.93 ?  108 SER E CB  1 
ATOM   10652 O OG  . SER E  4 117 ? 47.146  36.216  162.142 1.00 184.46 ?  108 SER E OG  1 
ATOM   10653 N N   . VAL E  4 118 ? 46.858  33.399  160.294 1.00 183.32 ?  109 VAL E N   1 
ATOM   10654 C CA  . VAL E  4 118 ? 47.889  32.401  160.000 1.00 184.78 ?  109 VAL E CA  1 
ATOM   10655 C C   . VAL E  4 118 ? 49.148  33.122  159.521 1.00 189.97 ?  109 VAL E C   1 
ATOM   10656 O O   . VAL E  4 118 ? 49.100  33.873  158.538 1.00 192.55 ?  109 VAL E O   1 
ATOM   10657 C CB  . VAL E  4 118 ? 47.415  31.374  158.959 1.00 183.48 ?  109 VAL E CB  1 
ATOM   10658 C CG1 . VAL E  4 118 ? 48.544  30.412  158.598 1.00 186.65 ?  109 VAL E CG1 1 
ATOM   10659 C CG2 . VAL E  4 118 ? 46.203  30.611  159.482 1.00 178.76 ?  109 VAL E CG2 1 
ATOM   10660 N N   . THR E  4 119 ? 50.267  32.906  160.214 1.00 196.08 ?  110 THR E N   1 
ATOM   10661 C CA  . THR E  4 119 ? 51.559  33.475  159.836 1.00 201.89 ?  110 THR E CA  1 
ATOM   10662 C C   . THR E  4 119 ? 52.525  32.377  159.395 1.00 203.64 ?  110 THR E C   1 
ATOM   10663 O O   . THR E  4 119 ? 52.809  31.452  160.165 1.00 202.46 ?  110 THR E O   1 
ATOM   10664 C CB  . THR E  4 119 ? 52.152  34.270  160.999 1.00 203.60 ?  110 THR E CB  1 
ATOM   10665 O OG1 . THR E  4 119 ? 51.247  35.318  161.367 1.00 203.41 ?  110 THR E OG1 1 
ATOM   10666 C CG2 . THR E  4 119 ? 53.488  34.878  160.606 1.00 210.57 ?  110 THR E CG2 1 
ATOM   10667 N N   . VAL E  4 120 ? 53.027  32.483  158.162 1.00 192.47 ?  111 VAL E N   1 
ATOM   10668 C CA  . VAL E  4 120 ? 54.007  31.552  157.601 1.00 195.56 ?  111 VAL E CA  1 
ATOM   10669 C C   . VAL E  4 120 ? 55.349  32.269  157.512 1.00 201.89 ?  111 VAL E C   1 
ATOM   10670 O O   . VAL E  4 120 ? 55.490  33.251  156.773 1.00 205.97 ?  111 VAL E O   1 
ATOM   10671 C CB  . VAL E  4 120 ? 53.579  31.007  156.234 1.00 195.21 ?  111 VAL E CB  1 
ATOM   10672 C CG1 . VAL E  4 120 ? 54.623  30.025  155.732 1.00 199.24 ?  111 VAL E CG1 1 
ATOM   10673 C CG2 . VAL E  4 120 ? 52.232  30.327  156.348 1.00 189.65 ?  111 VAL E CG2 1 
ATOM   10674 N N   . SER E  4 121 ? 56.335  31.761  158.244 1.00 216.87 ?  112 SER E N   1 
ATOM   10675 C CA  . SER E  4 121 ? 57.645  32.385  158.360 1.00 222.31 ?  112 SER E CA  1 
ATOM   10676 C C   . SER E  4 121 ? 58.623  31.334  158.857 1.00 221.92 ?  112 SER E C   1 
ATOM   10677 O O   . SER E  4 121 ? 58.224  30.336  159.461 1.00 217.93 ?  112 SER E O   1 
ATOM   10678 C CB  . SER E  4 121 ? 57.622  33.596  159.300 1.00 223.40 ?  112 SER E CB  1 
ATOM   10679 O OG  . SER E  4 121 ? 58.919  34.154  159.429 1.00 228.75 ?  112 SER E OG  1 
ATOM   10680 N N   . SER E  4 122 ? 59.910  31.558  158.600 1.00 218.70 ?  113 SER E N   1 
ATOM   10681 C CA  . SER E  4 122 ? 60.872  30.678  159.243 1.00 217.31 ?  113 SER E CA  1 
ATOM   10682 C C   . SER E  4 122 ? 61.313  31.259  160.570 1.00 216.30 ?  113 SER E C   1 
ATOM   10683 O O   . SER E  4 122 ? 62.101  30.631  161.285 1.00 215.05 ?  113 SER E O   1 
ATOM   10684 C CB  . SER E  4 122 ? 62.095  30.447  158.345 1.00 218.05 ?  113 SER E CB  1 
ATOM   10685 O OG  . SER E  4 122 ? 61.763  29.665  157.214 1.00 218.77 ?  113 SER E OG  1 
ATOM   10686 N N   . ALA E  4 123 ? 60.829  32.455  160.895 1.00 244.77 ?  114 ALA E N   1 
ATOM   10687 C CA  . ALA E  4 123 ? 61.092  33.041  162.195 1.00 244.60 ?  114 ALA E CA  1 
ATOM   10688 C C   . ALA E  4 123 ? 60.460  32.139  163.252 1.00 237.51 ?  114 ALA E C   1 
ATOM   10689 O O   . ALA E  4 123 ? 59.446  31.478  163.006 1.00 235.77 ?  114 ALA E O   1 
ATOM   10690 C CB  . ALA E  4 123 ? 60.537  34.462  162.284 1.00 245.49 ?  114 ALA E CB  1 
ATOM   10691 N N   . SER E  4 124 ? 61.051  32.136  164.436 1.00 239.35 ?  115 SER E N   1 
ATOM   10692 C CA  . SER E  4 124 ? 60.561  31.422  165.610 1.00 234.21 ?  115 SER E CA  1 
ATOM   10693 C C   . SER E  4 124 ? 60.483  32.419  166.762 1.00 233.96 ?  115 SER E C   1 
ATOM   10694 O O   . SER E  4 124 ? 61.256  33.367  166.833 1.00 238.49 ?  115 SER E O   1 
ATOM   10695 C CB  . SER E  4 124 ? 61.367  30.145  165.926 1.00 233.84 ?  115 SER E CB  1 
ATOM   10696 O OG  . SER E  4 124 ? 62.750  30.294  165.692 1.00 239.21 ?  115 SER E OG  1 
ATOM   10697 N N   . THR E  4 125 ? 59.534  32.188  167.663 1.00 251.56 ?  116 THR E N   1 
ATOM   10698 C CA  . THR E  4 125 ? 59.081  33.168  168.651 1.00 250.00 ?  116 THR E CA  1 
ATOM   10699 C C   . THR E  4 125 ? 60.189  33.825  169.477 1.00 253.77 ?  116 THR E C   1 
ATOM   10700 O O   . THR E  4 125 ? 61.067  33.157  170.031 1.00 255.67 ?  116 THR E O   1 
ATOM   10701 C CB  . THR E  4 125 ? 58.099  32.463  169.596 1.00 246.33 ?  116 THR E CB  1 
ATOM   10702 O OG1 . THR E  4 125 ? 56.917  32.076  168.881 1.00 245.12 ?  116 THR E OG1 1 
ATOM   10703 C CG2 . THR E  4 125 ? 57.713  33.361  170.750 1.00 245.34 ?  116 THR E CG2 1 
ATOM   10704 N N   . LYS E  4 126 ? 60.126  35.168  169.521 1.00 240.84 ?  117 LYS E N   1 
ATOM   10705 C CA  . LYS E  4 126 ? 61.066  36.088  170.166 1.00 245.51 ?  117 LYS E CA  1 
ATOM   10706 C C   . LYS E  4 126 ? 60.324  37.309  170.688 1.00 245.08 ?  117 LYS E C   1 
ATOM   10707 O O   . LYS E  4 126 ? 59.509  37.893  169.965 1.00 244.78 ?  117 LYS E O   1 
ATOM   10708 C CB  . LYS E  4 126 ? 62.130  36.587  169.184 1.00 252.91 ?  117 LYS E CB  1 
ATOM   10709 C CG  . LYS E  4 126 ? 63.150  37.565  169.773 1.00 260.39 ?  117 LYS E CG  1 
ATOM   10710 C CD  . LYS E  4 126 ? 63.979  36.966  170.893 1.00 262.18 ?  117 LYS E CD  1 
ATOM   10711 C CE  . LYS E  4 126 ? 65.028  37.956  171.384 1.00 267.43 ?  117 LYS E CE  1 
ATOM   10712 N NZ  . LYS E  4 126 ? 64.420  39.137  172.062 1.00 268.01 1  117 LYS E NZ  1 
ATOM   10713 N N   . GLY E  4 127 ? 60.600  37.682  171.940 1.00 238.56 ?  118 GLY E N   1 
ATOM   10714 C CA  . GLY E  4 127 ? 60.095  38.915  172.499 1.00 238.98 ?  118 GLY E CA  1 
ATOM   10715 C C   . GLY E  4 127 ? 60.825  40.152  172.006 1.00 244.63 ?  118 GLY E C   1 
ATOM   10716 O O   . GLY E  4 127 ? 62.004  40.111  171.640 1.00 249.18 ?  118 GLY E O   1 
ATOM   10717 N N   . PRO E  4 128 ? 60.127  41.285  172.002 1.00 220.95 ?  119 PRO E N   1 
ATOM   10718 C CA  . PRO E  4 128 ? 60.726  42.525  171.499 1.00 226.95 ?  119 PRO E CA  1 
ATOM   10719 C C   . PRO E  4 128 ? 61.813  43.089  172.399 1.00 230.51 ?  119 PRO E C   1 
ATOM   10720 O O   . PRO E  4 128 ? 61.821  42.894  173.617 1.00 228.88 ?  119 PRO E O   1 
ATOM   10721 C CB  . PRO E  4 128 ? 59.533  43.480  171.423 1.00 228.06 ?  119 PRO E CB  1 
ATOM   10722 C CG  . PRO E  4 128 ? 58.623  42.995  172.483 1.00 223.23 ?  119 PRO E CG  1 
ATOM   10723 C CD  . PRO E  4 128 ? 58.740  41.495  172.450 1.00 217.80 ?  119 PRO E CD  1 
ATOM   10724 N N   . SER E  4 129 ? 62.741  43.801  171.769 1.00 223.82 ?  120 SER E N   1 
ATOM   10725 C CA  . SER E  4 129 ? 63.637  44.713  172.463 1.00 228.14 ?  120 SER E CA  1 
ATOM   10726 C C   . SER E  4 129 ? 62.953  46.074  172.520 1.00 230.91 ?  120 SER E C   1 
ATOM   10727 O O   . SER E  4 129 ? 62.514  46.592  171.488 1.00 235.05 ?  120 SER E O   1 
ATOM   10728 C CB  . SER E  4 129 ? 64.989  44.809  171.760 1.00 235.48 ?  120 SER E CB  1 
ATOM   10729 O OG  . SER E  4 129 ? 65.619  43.543  171.696 1.00 237.78 ?  120 SER E OG  1 
ATOM   10730 N N   . VAL E  4 130 ? 62.862  46.653  173.714 1.00 229.69 ?  121 VAL E N   1 
ATOM   10731 C CA  . VAL E  4 130 ? 62.152  47.913  173.915 1.00 232.04 ?  121 VAL E CA  1 
ATOM   10732 C C   . VAL E  4 130 ? 63.155  49.002  174.260 1.00 238.61 ?  121 VAL E C   1 
ATOM   10733 O O   . VAL E  4 130 ? 63.877  48.902  175.260 1.00 238.82 ?  121 VAL E O   1 
ATOM   10734 C CB  . VAL E  4 130 ? 61.090  47.796  175.017 1.00 226.93 ?  121 VAL E CB  1 
ATOM   10735 C CG1 . VAL E  4 130 ? 60.339  49.112  175.157 1.00 229.85 ?  121 VAL E CG1 1 
ATOM   10736 C CG2 . VAL E  4 130 ? 60.141  46.652  174.715 1.00 222.90 ?  121 VAL E CG2 1 
ATOM   10737 N N   . PHE E  4 131 ? 63.194  50.044  173.426 1.00 237.62 ?  122 PHE E N   1 
ATOM   10738 C CA  . PHE E  4 131 ? 64.136  51.136  173.554 1.00 244.78 ?  122 PHE E CA  1 
ATOM   10739 C C   . PHE E  4 131 ? 63.388  52.453  173.717 1.00 247.90 ?  122 PHE E C   1 
ATOM   10740 O O   . PHE E  4 131 ? 62.323  52.643  173.118 1.00 246.48 ?  122 PHE E O   1 
ATOM   10741 C CB  . PHE E  4 131 ? 65.057  51.211  172.327 1.00 250.16 ?  122 PHE E CB  1 
ATOM   10742 C CG  . PHE E  4 131 ? 65.772  49.922  172.036 1.00 247.61 ?  122 PHE E CG  1 
ATOM   10743 C CD1 . PHE E  4 131 ? 66.683  49.401  172.940 1.00 246.77 ?  122 PHE E CD1 1 
ATOM   10744 C CD2 . PHE E  4 131 ? 65.528  49.227  170.862 1.00 246.36 ?  122 PHE E CD2 1 
ATOM   10745 C CE1 . PHE E  4 131 ? 67.334  48.209  172.681 1.00 244.75 ?  122 PHE E CE1 1 
ATOM   10746 C CE2 . PHE E  4 131 ? 66.180  48.036  170.595 1.00 244.33 ?  122 PHE E CE2 1 
ATOM   10747 C CZ  . PHE E  4 131 ? 67.086  47.529  171.506 1.00 243.59 ?  122 PHE E CZ  1 
ATOM   10748 N N   . PRO E  4 132 ? 63.918  53.379  174.511 1.00 250.25 ?  123 PRO E N   1 
ATOM   10749 C CA  . PRO E  4 132 ? 63.245  54.668  174.691 1.00 253.80 ?  123 PRO E CA  1 
ATOM   10750 C C   . PRO E  4 132 ? 63.348  55.548  173.457 1.00 260.40 ?  123 PRO E C   1 
ATOM   10751 O O   . PRO E  4 132 ? 64.376  55.589  172.776 1.00 265.20 ?  123 PRO E O   1 
ATOM   10752 C CB  . PRO E  4 132 ? 63.982  55.281  175.885 1.00 256.92 ?  123 PRO E CB  1 
ATOM   10753 C CG  . PRO E  4 132 ? 65.351  54.716  175.776 1.00 258.69 ?  123 PRO E CG  1 
ATOM   10754 C CD  . PRO E  4 132 ? 65.141  53.288  175.327 1.00 252.25 ?  123 PRO E CD  1 
ATOM   10755 N N   . LEU E  4 133 ? 62.258  56.253  173.179 1.00 256.52 ?  124 LEU E N   1 
ATOM   10756 C CA  . LEU E  4 133 ? 62.259  57.401  172.278 1.00 264.44 ?  124 LEU E CA  1 
ATOM   10757 C C   . LEU E  4 133 ? 62.187  58.620  173.186 1.00 269.03 ?  124 LEU E C   1 
ATOM   10758 O O   . LEU E  4 133 ? 61.112  58.993  173.665 1.00 267.48 ?  124 LEU E O   1 
ATOM   10759 C CB  . LEU E  4 133 ? 61.090  57.343  171.301 1.00 263.40 ?  124 LEU E CB  1 
ATOM   10760 C CG  . LEU E  4 133 ? 61.039  56.122  170.382 1.00 258.77 ?  124 LEU E CG  1 
ATOM   10761 C CD1 . LEU E  4 133 ? 59.682  56.017  169.697 1.00 256.58 ?  124 LEU E CD1 1 
ATOM   10762 C CD2 . LEU E  4 133 ? 62.166  56.186  169.364 1.00 264.84 ?  124 LEU E CD2 1 
ATOM   10763 N N   . ALA E  4 134 ? 63.334  59.233  173.428 1.00 259.15 ?  125 ALA E N   1 
ATOM   10764 C CA  . ALA E  4 134 ? 63.399  60.185  174.522 1.00 262.75 ?  125 ALA E CA  1 
ATOM   10765 C C   . ALA E  4 134 ? 62.841  61.535  174.082 1.00 273.00 ?  125 ALA E C   1 
ATOM   10766 O O   . ALA E  4 134 ? 63.052  61.953  172.940 1.00 279.92 ?  125 ALA E O   1 
ATOM   10767 C CB  . ALA E  4 134 ? 64.840  60.350  175.000 1.00 264.20 ?  125 ALA E CB  1 
ATOM   10768 N N   . PRO E  4 135 ? 62.139  62.236  174.969 1.00 281.83 ?  126 PRO E N   1 
ATOM   10769 C CA  . PRO E  4 135 ? 61.601  63.546  174.601 1.00 291.34 ?  126 PRO E CA  1 
ATOM   10770 C C   . PRO E  4 135 ? 62.728  64.523  174.332 1.00 302.02 ?  126 PRO E C   1 
ATOM   10771 O O   . PRO E  4 135 ? 63.744  64.542  175.029 1.00 303.00 ?  126 PRO E O   1 
ATOM   10772 C CB  . PRO E  4 135 ? 60.777  63.948  175.830 1.00 289.64 ?  126 PRO E CB  1 
ATOM   10773 C CG  . PRO E  4 135 ? 61.418  63.209  176.956 1.00 282.36 ?  126 PRO E CG  1 
ATOM   10774 C CD  . PRO E  4 135 ? 61.829  61.888  176.367 1.00 274.65 ?  126 PRO E CD  1 
ATOM   10775 N N   . SER E  4 136 ? 62.544  65.324  173.293 1.00 295.02 ?  127 SER E N   1 
ATOM   10776 C CA  . SER E  4 136 ? 63.534  66.330  172.952 1.00 308.04 ?  127 SER E CA  1 
ATOM   10777 C C   . SER E  4 136 ? 63.722  67.302  174.105 1.00 312.70 ?  127 SER E C   1 
ATOM   10778 O O   . SER E  4 136 ? 62.756  67.733  174.744 1.00 312.43 ?  127 SER E O   1 
ATOM   10779 C CB  . SER E  4 136 ? 63.110  67.092  171.696 1.00 317.22 ?  127 SER E CB  1 
ATOM   10780 O OG  . SER E  4 136 ? 63.973  68.187  171.431 1.00 329.29 ?  127 SER E OG  1 
ATOM   10781 N N   . SER E  4 137 ? 64.985  67.642  174.370 1.00 303.07 ?  128 SER E N   1 
ATOM   10782 C CA  . SER E  4 137 ? 65.258  68.672  175.361 1.00 308.56 ?  128 SER E CA  1 
ATOM   10783 C C   . SER E  4 137 ? 64.848  70.043  174.852 1.00 319.47 ?  128 SER E C   1 
ATOM   10784 O O   . SER E  4 137 ? 64.836  71.001  175.636 1.00 325.80 ?  128 SER E O   1 
ATOM   10785 C CB  . SER E  4 137 ? 66.744  68.657  175.748 1.00 312.96 ?  128 SER E CB  1 
ATOM   10786 O OG  . SER E  4 137 ? 67.572  68.878  174.630 1.00 315.92 ?  128 SER E OG  1 
ATOM   10787 N N   . LYS E  4 138 ? 64.544  70.156  173.560 1.00 321.51 ?  129 LYS E N   1 
ATOM   10788 C CA  . LYS E  4 138 ? 64.131  71.406  172.932 1.00 327.25 ?  129 LYS E CA  1 
ATOM   10789 C C   . LYS E  4 138 ? 62.621  71.572  172.901 1.00 329.10 ?  129 LYS E C   1 
ATOM   10790 O O   . LYS E  4 138 ? 62.117  72.490  172.232 1.00 333.73 ?  129 LYS E O   1 
ATOM   10791 C CB  . LYS E  4 138 ? 64.731  71.505  171.521 1.00 329.04 ?  129 LYS E CB  1 
ATOM   10792 C CG  . LYS E  4 138 ? 66.254  71.457  171.442 1.00 327.36 ?  129 LYS E CG  1 
ATOM   10793 C CD  . LYS E  4 138 ? 67.082  71.540  172.748 1.00 326.36 ?  129 LYS E CD  1 
ATOM   10794 C CE  . LYS E  4 138 ? 67.019  72.924  173.404 1.00 338.76 ?  129 LYS E CE  1 
ATOM   10795 N NZ  . LYS E  4 138 ? 67.629  72.854  174.758 1.00 337.75 1  129 LYS E NZ  1 
ATOM   10796 N N   . SER E  4 139 ? 61.905  70.677  173.571 1.00 333.92 ?  130 SER E N   1 
ATOM   10797 C CA  . SER E  4 139 ? 60.452  70.708  173.609 1.00 332.68 ?  130 SER E CA  1 
ATOM   10798 C C   . SER E  4 139 ? 59.940  72.094  173.979 1.00 339.70 ?  130 SER E C   1 
ATOM   10799 O O   . SER E  4 139 ? 60.505  72.787  174.831 1.00 339.57 ?  130 SER E O   1 
ATOM   10800 C CB  . SER E  4 139 ? 59.939  69.674  174.618 1.00 319.36 ?  130 SER E CB  1 
ATOM   10801 O OG  . SER E  4 139 ? 60.227  68.363  174.169 1.00 310.26 ?  130 SER E OG  1 
ATOM   10802 N N   . THR E  4 140 ? 58.863  72.489  173.308 1.00 317.20 ?  131 THR E N   1 
ATOM   10803 C CA  . THR E  4 140 ? 58.364  73.856  173.358 1.00 321.93 ?  131 THR E CA  1 
ATOM   10804 C C   . THR E  4 140 ? 57.924  74.237  174.767 1.00 320.96 ?  131 THR E C   1 
ATOM   10805 O O   . THR E  4 140 ? 57.161  73.514  175.412 1.00 317.53 ?  131 THR E O   1 
ATOM   10806 C CB  . THR E  4 140 ? 57.195  74.006  172.384 1.00 324.41 ?  131 THR E CB  1 
ATOM   10807 O OG1 . THR E  4 140 ? 57.589  73.522  171.094 1.00 324.73 ?  131 THR E OG1 1 
ATOM   10808 C CG2 . THR E  4 140 ? 56.793  75.453  172.275 1.00 329.52 ?  131 THR E CG2 1 
ATOM   10809 N N   . SER E  4 141 ? 58.437  75.372  175.251 1.00 323.11 ?  132 SER E N   1 
ATOM   10810 C CA  . SER E  4 141 ? 58.113  75.853  176.590 1.00 321.34 ?  132 SER E CA  1 
ATOM   10811 C C   . SER E  4 141 ? 56.623  76.145  176.703 1.00 323.74 ?  132 SER E C   1 
ATOM   10812 O O   . SER E  4 141 ? 56.070  76.937  175.931 1.00 326.66 ?  132 SER E O   1 
ATOM   10813 C CB  . SER E  4 141 ? 58.930  77.107  176.904 1.00 326.85 ?  132 SER E CB  1 
ATOM   10814 O OG  . SER E  4 141 ? 58.496  77.730  178.101 1.00 333.46 ?  132 SER E OG  1 
ATOM   10815 N N   . GLY E  4 142 ? 55.978  75.500  177.674 1.00 332.91 ?  133 GLY E N   1 
ATOM   10816 C CA  . GLY E  4 142 ? 54.536  75.539  177.791 1.00 332.41 ?  133 GLY E CA  1 
ATOM   10817 C C   . GLY E  4 142 ? 53.808  74.853  176.660 1.00 329.93 ?  133 GLY E C   1 
ATOM   10818 O O   . GLY E  4 142 ? 52.577  74.913  176.601 1.00 333.44 ?  133 GLY E O   1 
ATOM   10819 N N   . GLY E  4 143 ? 54.539  74.190  175.776 1.00 328.81 ?  134 GLY E N   1 
ATOM   10820 C CA  . GLY E  4 143 ? 54.056  73.537  174.581 1.00 326.91 ?  134 GLY E CA  1 
ATOM   10821 C C   . GLY E  4 143 ? 53.871  72.048  174.767 1.00 315.13 ?  134 GLY E C   1 
ATOM   10822 O O   . GLY E  4 143 ? 53.632  71.558  175.878 1.00 307.51 ?  134 GLY E O   1 
ATOM   10823 N N   . THR E  4 144 ? 53.979  71.317  173.663 1.00 302.66 ?  135 THR E N   1 
ATOM   10824 C CA  . THR E  4 144 ? 53.739  69.884  173.631 1.00 292.20 ?  135 THR E CA  1 
ATOM   10825 C C   . THR E  4 144 ? 55.037  69.154  173.318 1.00 289.25 ?  135 THR E C   1 
ATOM   10826 O O   . THR E  4 144 ? 55.778  69.550  172.411 1.00 295.76 ?  135 THR E O   1 
ATOM   10827 C CB  . THR E  4 144 ? 52.684  69.537  172.575 1.00 292.23 ?  135 THR E CB  1 
ATOM   10828 O OG1 . THR E  4 144 ? 51.412  70.066  172.970 1.00 293.21 ?  135 THR E OG1 1 
ATOM   10829 C CG2 . THR E  4 144 ? 52.572  68.034  172.390 1.00 282.24 ?  135 THR E CG2 1 
ATOM   10830 N N   . ALA E  4 145 ? 55.307  68.096  174.076 1.00 299.20 ?  136 ALA E N   1 
ATOM   10831 C CA  . ALA E  4 145 ? 56.464  67.240  173.884 1.00 294.88 ?  136 ALA E CA  1 
ATOM   10832 C C   . ALA E  4 145 ? 55.977  65.872  173.433 1.00 285.93 ?  136 ALA E C   1 
ATOM   10833 O O   . ALA E  4 145 ? 54.881  65.436  173.796 1.00 280.20 ?  136 ALA E O   1 
ATOM   10834 C CB  . ALA E  4 145 ? 57.289  67.107  175.167 1.00 290.64 ?  136 ALA E CB  1 
ATOM   10835 N N   . ALA E  4 146 ? 56.798  65.197  172.638 1.00 289.54 ?  137 ALA E N   1 
ATOM   10836 C CA  . ALA E  4 146 ? 56.527  63.835  172.211 1.00 280.60 ?  137 ALA E CA  1 
ATOM   10837 C C   . ALA E  4 146 ? 57.586  62.888  172.757 1.00 272.80 ?  137 ALA E C   1 
ATOM   10838 O O   . ALA E  4 146 ? 58.771  63.233  172.817 1.00 276.35 ?  137 ALA E O   1 
ATOM   10839 C CB  . ALA E  4 146 ? 56.472  63.746  170.682 1.00 284.76 ?  137 ALA E CB  1 
ATOM   10840 N N   . LEU E  4 147 ? 57.145  61.696  173.158 1.00 268.58 ?  138 LEU E N   1 
ATOM   10841 C CA  . LEU E  4 147 ? 58.032  60.642  173.626 1.00 261.62 ?  138 LEU E CA  1 
ATOM   10842 C C   . LEU E  4 147 ? 57.389  59.312  173.264 1.00 260.09 ?  138 LEU E C   1 
ATOM   10843 O O   . LEU E  4 147 ? 56.247  59.261  172.801 1.00 261.14 ?  138 LEU E O   1 
ATOM   10844 C CB  . LEU E  4 147 ? 58.277  60.743  175.135 1.00 260.28 ?  138 LEU E CB  1 
ATOM   10845 C CG  . LEU E  4 147 ? 57.017  60.745  176.005 1.00 260.29 ?  138 LEU E CG  1 
ATOM   10846 C CD1 . LEU E  4 147 ? 56.837  59.391  176.669 1.00 257.54 ?  138 LEU E CD1 1 
ATOM   10847 C CD2 . LEU E  4 147 ? 57.057  61.862  177.038 1.00 261.28 ?  138 LEU E CD2 1 
ATOM   10848 N N   . GLY E  4 148 ? 58.117  58.228  173.483 1.00 269.53 ?  139 GLY E N   1 
ATOM   10849 C CA  . GLY E  4 148 ? 57.576  56.948  173.083 1.00 260.89 ?  139 GLY E CA  1 
ATOM   10850 C C   . GLY E  4 148 ? 58.507  55.807  173.413 1.00 253.12 ?  139 GLY E C   1 
ATOM   10851 O O   . GLY E  4 148 ? 59.497  55.965  174.129 1.00 253.08 ?  139 GLY E O   1 
ATOM   10852 N N   . CYS E  4 149 ? 58.154  54.647  172.860 1.00 260.89 ?  140 CYS E N   1 
ATOM   10853 C CA  . CYS E  4 149 ? 58.948  53.427  172.924 1.00 253.61 ?  140 CYS E CA  1 
ATOM   10854 C C   . CYS E  4 149 ? 59.013  52.780  171.550 1.00 253.47 ?  140 CYS E C   1 
ATOM   10855 O O   . CYS E  4 149 ? 57.998  52.679  170.854 1.00 253.62 ?  140 CYS E O   1 
ATOM   10856 C CB  . CYS E  4 149 ? 58.376  52.422  173.928 1.00 243.81 ?  140 CYS E CB  1 
ATOM   10857 S SG  . CYS E  4 149 ? 58.622  52.841  175.647 1.00 241.74 ?  140 CYS E SG  1 
ATOM   10858 N N   . LEU E  4 150 ? 60.214  52.357  171.169 1.00 257.75 ?  141 LEU E N   1 
ATOM   10859 C CA  . LEU E  4 150 ? 60.436  51.561  169.970 1.00 256.97 ?  141 LEU E CA  1 
ATOM   10860 C C   . LEU E  4 150 ? 60.368  50.089  170.357 1.00 247.25 ?  141 LEU E C   1 
ATOM   10861 O O   . LEU E  4 150 ? 61.152  49.628  171.194 1.00 242.53 ?  141 LEU E O   1 
ATOM   10862 C CB  . LEU E  4 150 ? 61.789  51.892  169.347 1.00 262.95 ?  141 LEU E CB  1 
ATOM   10863 C CG  . LEU E  4 150 ? 62.209  51.025  168.162 1.00 262.15 ?  141 LEU E CG  1 
ATOM   10864 C CD1 . LEU E  4 150 ? 61.220  51.146  167.012 1.00 266.23 ?  141 LEU E CD1 1 
ATOM   10865 C CD2 . LEU E  4 150 ? 63.604  51.395  167.730 1.00 269.11 ?  141 LEU E CD2 1 
ATOM   10866 N N   . VAL E  4 151 ? 59.440  49.356  169.755 1.00 231.58 ?  142 VAL E N   1 
ATOM   10867 C CA  . VAL E  4 151 ? 59.213  47.956  170.089 1.00 229.93 ?  142 VAL E CA  1 
ATOM   10868 C C   . VAL E  4 151 ? 59.678  47.132  168.895 1.00 229.95 ?  142 VAL E C   1 
ATOM   10869 O O   . VAL E  4 151 ? 58.967  47.008  167.892 1.00 230.70 ?  142 VAL E O   1 
ATOM   10870 C CB  . VAL E  4 151 ? 57.739  47.693  170.415 1.00 229.64 ?  142 VAL E CB  1 
ATOM   10871 C CG1 . VAL E  4 151 ? 57.522  46.249  170.802 1.00 227.97 ?  142 VAL E CG1 1 
ATOM   10872 C CG2 . VAL E  4 151 ? 57.267  48.632  171.517 1.00 229.90 ?  142 VAL E CG2 1 
ATOM   10873 N N   . LYS E  4 152 ? 60.882  46.575  169.000 1.00 230.36 ?  143 LYS E N   1 
ATOM   10874 C CA  . LYS E  4 152 ? 61.629  46.104  167.844 1.00 232.59 ?  143 LYS E CA  1 
ATOM   10875 C C   . LYS E  4 152 ? 61.958  44.620  167.963 1.00 229.13 ?  143 LYS E C   1 
ATOM   10876 O O   . LYS E  4 152 ? 62.229  44.117  169.059 1.00 226.17 ?  143 LYS E O   1 
ATOM   10877 C CB  . LYS E  4 152 ? 62.918  46.915  167.671 1.00 241.35 ?  143 LYS E CB  1 
ATOM   10878 C CG  . LYS E  4 152 ? 63.694  46.594  166.407 1.00 247.74 ?  143 LYS E CG  1 
ATOM   10879 C CD  . LYS E  4 152 ? 64.761  47.635  166.136 1.00 255.56 ?  143 LYS E CD  1 
ATOM   10880 C CE  . LYS E  4 152 ? 65.816  47.092  165.191 1.00 260.87 ?  143 LYS E CE  1 
ATOM   10881 N NZ  . LYS E  4 152 ? 65.223  46.699  163.882 1.00 263.06 1  143 LYS E NZ  1 
ATOM   10882 N N   . ASP E  4 153 ? 61.929  43.933  166.818 1.00 242.01 ?  144 ASP E N   1 
ATOM   10883 C CA  . ASP E  4 153 ? 62.403  42.556  166.652 1.00 239.57 ?  144 ASP E CA  1 
ATOM   10884 C C   . ASP E  4 153 ? 61.637  41.539  167.506 1.00 232.57 ?  144 ASP E C   1 
ATOM   10885 O O   . ASP E  4 153 ? 62.204  40.863  168.368 1.00 230.98 ?  144 ASP E O   1 
ATOM   10886 C CB  . ASP E  4 153 ? 63.907  42.470  166.945 1.00 243.60 ?  144 ASP E CB  1 
ATOM   10887 C CG  . ASP E  4 153 ? 64.754  43.155  165.886 1.00 252.10 ?  144 ASP E CG  1 
ATOM   10888 O OD1 . ASP E  4 153 ? 64.252  43.380  164.765 1.00 253.99 ?  144 ASP E OD1 1 
ATOM   10889 O OD2 . ASP E  4 153 ? 65.931  43.458  166.175 1.00 259.04 -1 144 ASP E OD2 1 
ATOM   10890 N N   . TYR E  4 154 ? 60.333  41.430  167.259 1.00 232.18 ?  145 TYR E N   1 
ATOM   10891 C CA  . TYR E  4 154 ? 59.547  40.398  167.918 1.00 225.34 ?  145 TYR E CA  1 
ATOM   10892 C C   . TYR E  4 154 ? 58.856  39.529  166.874 1.00 222.29 ?  145 TYR E C   1 
ATOM   10893 O O   . TYR E  4 154 ? 58.632  39.947  165.734 1.00 226.32 ?  145 TYR E O   1 
ATOM   10894 C CB  . TYR E  4 154 ? 58.522  40.994  168.894 1.00 222.84 ?  145 TYR E CB  1 
ATOM   10895 C CG  . TYR E  4 154 ? 57.465  41.873  168.273 1.00 223.73 ?  145 TYR E CG  1 
ATOM   10896 C CD1 . TYR E  4 154 ? 57.686  43.230  168.080 1.00 229.65 ?  145 TYR E CD1 1 
ATOM   10897 C CD2 . TYR E  4 154 ? 56.232  41.351  167.911 1.00 219.71 ?  145 TYR E CD2 1 
ATOM   10898 C CE1 . TYR E  4 154 ? 56.715  44.037  167.524 1.00 230.97 ?  145 TYR E CE1 1 
ATOM   10899 C CE2 . TYR E  4 154 ? 55.256  42.149  167.356 1.00 221.41 ?  145 TYR E CE2 1 
ATOM   10900 C CZ  . TYR E  4 154 ? 55.503  43.490  167.165 1.00 227.27 ?  145 TYR E CZ  1 
ATOM   10901 O OH  . TYR E  4 154 ? 54.535  44.291  166.616 1.00 234.52 ?  145 TYR E OH  1 
ATOM   10902 N N   . PHE E  4 155 ? 58.515  38.308  167.278 1.00 230.26 ?  146 PHE E N   1 
ATOM   10903 C CA  . PHE E  4 155 ? 57.752  37.404  166.424 1.00 227.80 ?  146 PHE E CA  1 
ATOM   10904 C C   . PHE E  4 155 ? 56.985  36.393  167.270 1.00 221.82 ?  146 PHE E C   1 
ATOM   10905 O O   . PHE E  4 155 ? 57.487  35.941  168.298 1.00 219.56 ?  146 PHE E O   1 
ATOM   10906 C CB  . PHE E  4 155 ? 58.675  36.683  165.435 1.00 230.38 ?  146 PHE E CB  1 
ATOM   10907 C CG  . PHE E  4 155 ? 57.958  35.723  164.523 1.00 227.96 ?  146 PHE E CG  1 
ATOM   10908 C CD1 . PHE E  4 155 ? 57.765  34.400  164.890 1.00 223.69 ?  146 PHE E CD1 1 
ATOM   10909 C CD2 . PHE E  4 155 ? 57.464  36.151  163.302 1.00 230.50 ?  146 PHE E CD2 1 
ATOM   10910 C CE1 . PHE E  4 155 ? 57.100  33.524  164.053 1.00 222.06 ?  146 PHE E CE1 1 
ATOM   10911 C CE2 . PHE E  4 155 ? 56.799  35.280  162.461 1.00 228.89 ?  146 PHE E CE2 1 
ATOM   10912 C CZ  . PHE E  4 155 ? 56.618  33.966  162.837 1.00 224.74 ?  146 PHE E CZ  1 
ATOM   10913 N N   . PRO E  4 156 ? 55.759  36.041  166.852 1.00 214.55 ?  147 PRO E N   1 
ATOM   10914 C CA  . PRO E  4 156 ? 54.945  36.667  165.809 1.00 216.02 ?  147 PRO E CA  1 
ATOM   10915 C C   . PRO E  4 156 ? 54.176  37.852  166.376 1.00 217.45 ?  147 PRO E C   1 
ATOM   10916 O O   . PRO E  4 156 ? 54.412  38.227  167.523 1.00 217.30 ?  147 PRO E O   1 
ATOM   10917 C CB  . PRO E  4 156 ? 54.006  35.540  165.391 1.00 212.80 ?  147 PRO E CB  1 
ATOM   10918 C CG  . PRO E  4 156 ? 53.755  34.821  166.670 1.00 208.64 ?  147 PRO E CG  1 
ATOM   10919 C CD  . PRO E  4 156 ? 55.069  34.874  167.434 1.00 209.45 ?  147 PRO E CD  1 
ATOM   10920 N N   . GLU E  4 157 ? 53.277  38.439  165.596 1.00 201.65 ?  148 GLU E N   1 
ATOM   10921 C CA  . GLU E  4 157 ? 52.325  39.378  166.173 1.00 202.19 ?  148 GLU E CA  1 
ATOM   10922 C C   . GLU E  4 157 ? 51.363  38.616  167.079 1.00 201.08 ?  148 GLU E C   1 
ATOM   10923 O O   . GLU E  4 157 ? 51.237  37.397  166.964 1.00 200.19 ?  148 GLU E O   1 
ATOM   10924 C CB  . GLU E  4 157 ? 51.535  40.128  165.095 1.00 203.89 ?  148 GLU E CB  1 
ATOM   10925 C CG  . GLU E  4 157 ? 52.327  41.076  164.229 1.00 208.51 ?  148 GLU E CG  1 
ATOM   10926 C CD  . GLU E  4 157 ? 51.434  42.142  163.619 1.00 211.71 ?  148 GLU E CD  1 
ATOM   10927 O OE1 . GLU E  4 157 ? 51.015  41.978  162.455 1.00 213.13 ?  148 GLU E OE1 1 
ATOM   10928 O OE2 . GLU E  4 157 ? 51.161  43.152  164.303 1.00 213.44 -1 148 GLU E OE2 1 
ATOM   10929 N N   . PRO E  4 158 ? 50.670  39.332  167.980 1.00 215.08 ?  149 PRO E N   1 
ATOM   10930 C CA  . PRO E  4 158 ? 50.849  40.740  168.340 1.00 219.03 ?  149 PRO E CA  1 
ATOM   10931 C C   . PRO E  4 158 ? 51.630  40.992  169.626 1.00 219.55 ?  149 PRO E C   1 
ATOM   10932 O O   . PRO E  4 158 ? 51.975  40.072  170.367 1.00 216.76 ?  149 PRO E O   1 
ATOM   10933 C CB  . PRO E  4 158 ? 49.410  41.216  168.499 1.00 218.81 ?  149 PRO E CB  1 
ATOM   10934 C CG  . PRO E  4 158 ? 48.734  40.028  169.121 1.00 213.88 ?  149 PRO E CG  1 
ATOM   10935 C CD  . PRO E  4 158 ? 49.444  38.787  168.590 1.00 212.13 ?  149 PRO E CD  1 
ATOM   10936 N N   . VAL E  4 159 ? 51.897  42.269  169.867 1.00 228.54 ?  150 VAL E N   1 
ATOM   10937 C CA  . VAL E  4 159 ? 52.267  42.772  171.179 1.00 227.78 ?  150 VAL E CA  1 
ATOM   10938 C C   . VAL E  4 159 ? 51.104  43.629  171.656 1.00 228.17 ?  150 VAL E C   1 
ATOM   10939 O O   . VAL E  4 159 ? 50.311  44.143  170.860 1.00 232.46 ?  150 VAL E O   1 
ATOM   10940 C CB  . VAL E  4 159 ? 53.585  43.574  171.171 1.00 232.94 ?  150 VAL E CB  1 
ATOM   10941 C CG1 . VAL E  4 159 ? 54.774  42.654  170.923 1.00 233.41 ?  150 VAL E CG1 1 
ATOM   10942 C CG2 . VAL E  4 159 ? 53.529  44.684  170.132 1.00 238.70 ?  150 VAL E CG2 1 
ATOM   10943 N N   . THR E  4 160 ? 50.999  43.788  172.969 1.00 236.44 ?  151 THR E N   1 
ATOM   10944 C CA  . THR E  4 160 ? 50.145  44.816  173.541 1.00 237.42 ?  151 THR E CA  1 
ATOM   10945 C C   . THR E  4 160 ? 51.014  45.891  174.170 1.00 241.55 ?  151 THR E C   1 
ATOM   10946 O O   . THR E  4 160 ? 52.030  45.591  174.805 1.00 241.74 ?  151 THR E O   1 
ATOM   10947 C CB  . THR E  4 160 ? 49.194  44.233  174.590 1.00 234.93 ?  151 THR E CB  1 
ATOM   10948 O OG1 . THR E  4 160 ? 49.953  43.611  175.634 1.00 235.61 ?  151 THR E OG1 1 
ATOM   10949 C CG2 . THR E  4 160 ? 48.281  43.202  173.957 1.00 232.17 ?  151 THR E CG2 1 
ATOM   10950 N N   . VAL E  4 161 ? 50.609  47.144  173.986 1.00 231.52 ?  152 VAL E N   1 
ATOM   10951 C CA  . VAL E  4 161 ? 51.321  48.290  174.533 1.00 235.81 ?  152 VAL E CA  1 
ATOM   10952 C C   . VAL E  4 161 ? 50.341  49.139  175.326 1.00 237.57 ?  152 VAL E C   1 
ATOM   10953 O O   . VAL E  4 161 ? 49.273  49.503  174.821 1.00 239.70 ?  152 VAL E O   1 
ATOM   10954 C CB  . VAL E  4 161 ? 51.985  49.131  173.425 1.00 242.38 ?  152 VAL E CB  1 
ATOM   10955 C CG1 . VAL E  4 161 ? 52.758  50.298  174.032 1.00 249.02 ?  152 VAL E CG1 1 
ATOM   10956 C CG2 . VAL E  4 161 ? 52.895  48.262  172.564 1.00 243.10 ?  152 VAL E CG2 1 
ATOM   10957 N N   . SER E  4 162 ? 50.706  49.452  176.563 1.00 230.24 ?  153 SER E N   1 
ATOM   10958 C CA  . SER E  4 162 ? 50.010  50.439  177.368 1.00 232.68 ?  153 SER E CA  1 
ATOM   10959 C C   . SER E  4 162 ? 51.024  51.447  177.881 1.00 237.62 ?  153 SER E C   1 
ATOM   10960 O O   . SER E  4 162 ? 52.238  51.228  177.823 1.00 238.20 ?  153 SER E O   1 
ATOM   10961 C CB  . SER E  4 162 ? 49.262  49.790  178.539 1.00 227.22 ?  153 SER E CB  1 
ATOM   10962 O OG  . SER E  4 162 ? 50.163  49.127  179.408 1.00 224.22 ?  153 SER E OG  1 
ATOM   10963 N N   . TRP E  4 163 ? 50.515  52.565  178.384 1.00 228.33 ?  154 TRP E N   1 
ATOM   10964 C CA  . TRP E  4 163 ? 51.343  53.574  179.023 1.00 233.15 ?  154 TRP E CA  1 
ATOM   10965 C C   . TRP E  4 163 ? 50.882  53.716  180.464 1.00 231.16 ?  154 TRP E C   1 
ATOM   10966 O O   . TRP E  4 163 ? 49.680  53.842  180.725 1.00 230.22 ?  154 TRP E O   1 
ATOM   10967 C CB  . TRP E  4 163 ? 51.272  54.911  178.280 1.00 240.86 ?  154 TRP E CB  1 
ATOM   10968 C CG  . TRP E  4 163 ? 52.048  54.900  176.994 1.00 243.84 ?  154 TRP E CG  1 
ATOM   10969 C CD1 . TRP E  4 163 ? 51.598  54.520  175.763 1.00 243.47 ?  154 TRP E CD1 1 
ATOM   10970 C CD2 . TRP E  4 163 ? 53.428  55.252  176.824 1.00 247.79 ?  154 TRP E CD2 1 
ATOM   10971 N NE1 . TRP E  4 163 ? 52.605  54.632  174.835 1.00 246.99 ?  154 TRP E NE1 1 
ATOM   10972 C CE2 . TRP E  4 163 ? 53.739  55.077  175.461 1.00 249.75 ?  154 TRP E CE2 1 
ATOM   10973 C CE3 . TRP E  4 163 ? 54.427  55.705  177.692 1.00 250.13 ?  154 TRP E CE3 1 
ATOM   10974 C CZ2 . TRP E  4 163 ? 55.007  55.340  174.946 1.00 254.01 ?  154 TRP E CZ2 1 
ATOM   10975 C CZ3 . TRP E  4 163 ? 55.685  55.965  177.178 1.00 254.36 ?  154 TRP E CZ3 1 
ATOM   10976 C CH2 . TRP E  4 163 ? 55.964  55.781  175.820 1.00 256.29 ?  154 TRP E CH2 1 
ATOM   10977 N N   . ASN E  4 164 ? 51.845  53.717  181.385 1.00 236.88 ?  155 ASN E N   1 
ATOM   10978 C CA  . ASN E  4 164 ? 51.582  53.813  182.820 1.00 235.28 ?  155 ASN E CA  1 
ATOM   10979 C C   . ASN E  4 164 ? 50.499  52.826  183.257 1.00 229.01 ?  155 ASN E C   1 
ATOM   10980 O O   . ASN E  4 164 ? 49.593  53.161  184.024 1.00 228.72 ?  155 ASN E O   1 
ATOM   10981 C CB  . ASN E  4 164 ? 51.213  55.246  183.211 1.00 241.15 ?  155 ASN E CB  1 
ATOM   10982 C CG  . ASN E  4 164 ? 52.362  56.220  183.010 1.00 247.82 ?  155 ASN E CG  1 
ATOM   10983 O OD1 . ASN E  4 164 ? 53.502  55.816  182.775 1.00 247.71 ?  155 ASN E OD1 1 
ATOM   10984 N ND2 . ASN E  4 164 ? 52.067  57.511  183.109 1.00 253.97 ?  155 ASN E ND2 1 
ATOM   10985 N N   . SER E  4 165 ? 50.602  51.588  182.759 1.00 239.38 ?  156 SER E N   1 
ATOM   10986 C CA  . SER E  4 165 ? 49.698  50.488  183.119 1.00 232.71 ?  156 SER E CA  1 
ATOM   10987 C C   . SER E  4 165 ? 48.232  50.804  182.813 1.00 233.18 ?  156 SER E C   1 
ATOM   10988 O O   . SER E  4 165 ? 47.323  50.285  183.467 1.00 232.36 ?  156 SER E O   1 
ATOM   10989 C CB  . SER E  4 165 ? 49.874  50.090  184.588 1.00 231.91 ?  156 SER E CB  1 
ATOM   10990 O OG  . SER E  4 165 ? 51.174  49.568  184.821 1.00 233.53 ?  156 SER E OG  1 
ATOM   10991 N N   . GLY E  4 166 ? 47.984  51.647  181.814 1.00 218.93 ?  157 GLY E N   1 
ATOM   10992 C CA  . GLY E  4 166 ? 46.644  51.986  181.387 1.00 220.84 ?  157 GLY E CA  1 
ATOM   10993 C C   . GLY E  4 166 ? 46.135  53.319  181.891 1.00 222.89 ?  157 GLY E C   1 
ATOM   10994 O O   . GLY E  4 166 ? 45.037  53.733  181.498 1.00 224.72 ?  157 GLY E O   1 
ATOM   10995 N N   . ALA E  4 167 ? 46.892  53.998  182.751 1.00 236.92 ?  158 ALA E N   1 
ATOM   10996 C CA  . ALA E  4 167 ? 46.440  55.265  183.309 1.00 242.22 ?  158 ALA E CA  1 
ATOM   10997 C C   . ALA E  4 167 ? 46.611  56.413  182.325 1.00 249.47 ?  158 ALA E C   1 
ATOM   10998 O O   . ALA E  4 167 ? 46.000  57.471  182.513 1.00 254.51 ?  158 ALA E O   1 
ATOM   10999 C CB  . ALA E  4 167 ? 47.186  55.582  184.605 1.00 242.63 ?  158 ALA E CB  1 
ATOM   11000 N N   . LEU E  4 168 ? 47.421  56.220  181.284 1.00 235.82 ?  159 LEU E N   1 
ATOM   11001 C CA  . LEU E  4 168 ? 47.636  57.205  180.230 1.00 242.58 ?  159 LEU E CA  1 
ATOM   11002 C C   . LEU E  4 168 ? 47.172  56.626  178.905 1.00 241.16 ?  159 LEU E C   1 
ATOM   11003 O O   . LEU E  4 168 ? 47.741  55.641  178.422 1.00 237.22 ?  159 LEU E O   1 
ATOM   11004 C CB  . LEU E  4 168 ? 49.115  57.582  180.130 1.00 246.01 ?  159 LEU E CB  1 
ATOM   11005 C CG  . LEU E  4 168 ? 49.500  58.557  179.016 1.00 253.32 ?  159 LEU E CG  1 
ATOM   11006 C CD1 . LEU E  4 168 ? 48.826  59.902  179.211 1.00 259.97 ?  159 LEU E CD1 1 
ATOM   11007 C CD2 . LEU E  4 168 ? 51.009  58.703  178.941 1.00 255.88 ?  159 LEU E CD2 1 
ATOM   11008 N N   . THR E  4 169 ? 46.142  57.230  178.331 1.00 245.66 ?  160 THR E N   1 
ATOM   11009 C CA  . THR E  4 169 ? 45.562  56.786  177.068 1.00 244.93 ?  160 THR E CA  1 
ATOM   11010 C C   . THR E  4 169 ? 45.404  57.907  176.050 1.00 252.47 ?  160 THR E C   1 
ATOM   11011 O O   . THR E  4 169 ? 45.668  57.695  174.863 1.00 253.34 ?  160 THR E O   1 
ATOM   11012 C CB  . THR E  4 169 ? 44.196  56.132  177.337 1.00 240.39 ?  160 THR E CB  1 
ATOM   11013 O OG1 . THR E  4 169 ? 43.358  57.051  178.049 1.00 243.73 ?  160 THR E OG1 1 
ATOM   11014 C CG2 . THR E  4 169 ? 44.360  54.863  178.167 1.00 232.77 ?  160 THR E CG2 1 
ATOM   11015 N N   . SER E  4 170 ? 44.966  59.088  176.484 1.00 241.45 ?  161 SER E N   1 
ATOM   11016 C CA  . SER E  4 170 ? 44.796  60.227  175.588 1.00 249.28 ?  161 SER E CA  1 
ATOM   11017 C C   . SER E  4 170 ? 46.100  60.620  174.906 1.00 253.68 ?  161 SER E C   1 
ATOM   11018 O O   . SER E  4 170 ? 47.149  60.719  175.548 1.00 254.19 ?  161 SER E O   1 
ATOM   11019 C CB  . SER E  4 170 ? 44.236  61.418  176.360 1.00 254.39 ?  161 SER E CB  1 
ATOM   11020 O OG  . SER E  4 170 ? 42.996  61.083  176.954 1.00 250.80 ?  161 SER E OG  1 
ATOM   11021 N N   . GLY E  4 171 ? 46.023  60.848  173.597 1.00 248.78 ?  162 GLY E N   1 
ATOM   11022 C CA  . GLY E  4 171 ? 47.172  61.269  172.823 1.00 255.63 ?  162 GLY E CA  1 
ATOM   11023 C C   . GLY E  4 171 ? 48.157  60.180  172.472 1.00 252.35 ?  162 GLY E C   1 
ATOM   11024 O O   . GLY E  4 171 ? 49.211  60.483  171.901 1.00 257.72 ?  162 GLY E O   1 
ATOM   11025 N N   . VAL E  4 172 ? 47.844  58.927  172.780 1.00 247.70 ?  163 VAL E N   1 
ATOM   11026 C CA  . VAL E  4 172 ? 48.710  57.799  172.465 1.00 245.49 ?  163 VAL E CA  1 
ATOM   11027 C C   . VAL E  4 172 ? 48.432  57.347  171.040 1.00 246.27 ?  163 VAL E C   1 
ATOM   11028 O O   . VAL E  4 172 ? 47.272  57.162  170.652 1.00 247.20 ?  163 VAL E O   1 
ATOM   11029 C CB  . VAL E  4 172 ? 48.496  56.649  173.462 1.00 242.90 ?  163 VAL E CB  1 
ATOM   11030 C CG1 . VAL E  4 172 ? 49.292  55.429  173.040 1.00 240.74 ?  163 VAL E CG1 1 
ATOM   11031 C CG2 . VAL E  4 172 ? 48.890  57.077  174.866 1.00 242.06 ?  163 VAL E CG2 1 
ATOM   11032 N N   . HIS E  4 173 ? 49.496  57.172  170.259 1.00 250.22 ?  164 HIS E N   1 
ATOM   11033 C CA  . HIS E  4 173 ? 49.436  56.496  168.967 1.00 254.16 ?  164 HIS E CA  1 
ATOM   11034 C C   . HIS E  4 173 ? 50.356  55.285  169.016 1.00 243.41 ?  164 HIS E C   1 
ATOM   11035 O O   . HIS E  4 173 ? 51.581  55.434  169.089 1.00 242.03 ?  164 HIS E O   1 
ATOM   11036 C CB  . HIS E  4 173 ? 49.850  57.433  167.831 1.00 267.34 ?  164 HIS E CB  1 
ATOM   11037 C CG  . HIS E  4 173 ? 48.894  58.558  167.588 1.00 278.89 ?  164 HIS E CG  1 
ATOM   11038 N ND1 . HIS E  4 173 ? 47.595  58.355  167.175 1.00 283.57 ?  164 HIS E ND1 1 
ATOM   11039 C CD2 . HIS E  4 173 ? 49.048  59.898  167.698 1.00 286.11 ?  164 HIS E CD2 1 
ATOM   11040 C CE1 . HIS E  4 173 ? 46.990  59.522  167.043 1.00 293.54 ?  164 HIS E CE1 1 
ATOM   11041 N NE2 . HIS E  4 173 ? 47.850  60.474  167.355 1.00 294.76 ?  164 HIS E NE2 1 
ATOM   11042 N N   . THR E  4 174 ? 49.773  54.090  168.976 1.00 263.77 ?  165 THR E N   1 
ATOM   11043 C CA  . THR E  4 174 ? 50.540  52.856  168.867 1.00 253.75 ?  165 THR E CA  1 
ATOM   11044 C C   . THR E  4 174 ? 50.445  52.437  167.408 1.00 258.62 ?  165 THR E C   1 
ATOM   11045 O O   . THR E  4 174 ? 49.373  52.048  166.932 1.00 261.50 ?  165 THR E O   1 
ATOM   11046 C CB  . THR E  4 174 ? 50.008  51.770  169.800 1.00 241.75 ?  165 THR E CB  1 
ATOM   11047 O OG1 . THR E  4 174 ? 50.183  52.174  171.164 1.00 239.49 ?  165 THR E OG1 1 
ATOM   11048 C CG2 . THR E  4 174 ? 50.752  50.464  169.568 1.00 235.75 ?  165 THR E CG2 1 
ATOM   11049 N N   . PHE E  4 175 ? 51.567  52.519  166.705 1.00 253.88 ?  166 PHE E N   1 
ATOM   11050 C CA  . PHE E  4 175 ? 51.552  52.319  165.271 1.00 259.68 ?  166 PHE E CA  1 
ATOM   11051 C C   . PHE E  4 175 ? 51.366  50.845  164.923 1.00 248.91 ?  166 PHE E C   1 
ATOM   11052 O O   . PHE E  4 175 ? 51.767  49.960  165.683 1.00 238.41 ?  166 PHE E O   1 
ATOM   11053 C CB  . PHE E  4 175 ? 52.835  52.858  164.646 1.00 262.95 ?  166 PHE E CB  1 
ATOM   11054 C CG  . PHE E  4 175 ? 52.885  54.357  164.586 1.00 275.99 ?  166 PHE E CG  1 
ATOM   11055 C CD1 . PHE E  4 175 ? 52.303  55.042  163.532 1.00 288.80 ?  166 PHE E CD1 1 
ATOM   11056 C CD2 . PHE E  4 175 ? 53.492  55.083  165.596 1.00 276.46 ?  166 PHE E CD2 1 
ATOM   11057 C CE1 . PHE E  4 175 ? 52.338  56.422  163.481 1.00 301.73 ?  166 PHE E CE1 1 
ATOM   11058 C CE2 . PHE E  4 175 ? 53.530  56.464  165.550 1.00 288.20 ?  166 PHE E CE2 1 
ATOM   11059 C CZ  . PHE E  4 175 ? 52.953  57.135  164.491 1.00 301.91 ?  166 PHE E CZ  1 
ATOM   11060 N N   . PRO E  4 176 ? 50.744  50.563  163.781 1.00 252.52 ?  167 PRO E N   1 
ATOM   11061 C CA  . PRO E  4 176 ? 50.661  49.181  163.304 1.00 242.59 ?  167 PRO E CA  1 
ATOM   11062 C C   . PRO E  4 176 ? 52.051  48.587  163.177 1.00 236.92 ?  167 PRO E C   1 
ATOM   11063 O O   . PRO E  4 176 ? 53.004  49.269  162.791 1.00 242.69 ?  167 PRO E O   1 
ATOM   11064 C CB  . PRO E  4 176 ? 49.973  49.312  161.942 1.00 252.15 ?  167 PRO E CB  1 
ATOM   11065 C CG  . PRO E  4 176 ? 49.214  50.588  162.022 1.00 266.04 ?  167 PRO E CG  1 
ATOM   11066 C CD  . PRO E  4 176 ? 50.012  51.498  162.909 1.00 267.24 ?  167 PRO E CD  1 
ATOM   11067 N N   . ALA E  4 177 ? 52.173  47.310  163.526 1.00 232.74 ?  168 ALA E N   1 
ATOM   11068 C CA  . ALA E  4 177 ? 53.474  46.684  163.399 1.00 231.17 ?  168 ALA E CA  1 
ATOM   11069 C C   . ALA E  4 177 ? 53.845  46.671  161.930 1.00 235.19 ?  168 ALA E C   1 
ATOM   11070 O O   . ALA E  4 177 ? 52.990  46.541  161.051 1.00 235.19 ?  168 ALA E O   1 
ATOM   11071 C CB  . ALA E  4 177 ? 53.443  45.256  163.937 1.00 228.47 ?  168 ALA E CB  1 
ATOM   11072 N N   . VAL E  4 178 ? 55.131  46.802  161.660 1.00 223.86 ?  169 VAL E N   1 
ATOM   11073 C CA  . VAL E  4 178 ? 55.635  46.640  160.312 1.00 226.64 ?  169 VAL E CA  1 
ATOM   11074 C C   . VAL E  4 178 ? 56.511  45.393  160.314 1.00 223.17 ?  169 VAL E C   1 
ATOM   11075 O O   . VAL E  4 178 ? 57.214  45.127  161.296 1.00 221.83 ?  169 VAL E O   1 
ATOM   11076 C CB  . VAL E  4 178 ? 56.383  47.937  159.925 1.00 234.85 ?  169 VAL E CB  1 
ATOM   11077 C CG1 . VAL E  4 178 ? 57.665  48.124  160.707 1.00 236.17 ?  169 VAL E CG1 1 
ATOM   11078 C CG2 . VAL E  4 178 ? 56.546  48.112  158.432 1.00 238.16 ?  169 VAL E CG2 1 
ATOM   11079 N N   . LEU E  4 179 ? 56.459  44.614  159.230 1.00 225.11 ?  170 LEU E N   1 
ATOM   11080 C CA  . LEU E  4 179 ? 57.368  43.482  159.074 1.00 223.61 ?  170 LEU E CA  1 
ATOM   11081 C C   . LEU E  4 179 ? 58.678  43.959  158.459 1.00 231.49 ?  170 LEU E C   1 
ATOM   11082 O O   . LEU E  4 179 ? 58.706  44.419  157.312 1.00 237.11 ?  170 LEU E O   1 
ATOM   11083 C CB  . LEU E  4 179 ? 56.728  42.369  158.238 1.00 221.38 ?  170 LEU E CB  1 
ATOM   11084 C CG  . LEU E  4 179 ? 57.526  41.069  158.046 1.00 219.25 ?  170 LEU E CG  1 
ATOM   11085 C CD1 . LEU E  4 179 ? 57.845  40.428  159.397 1.00 214.50 ?  170 LEU E CD1 1 
ATOM   11086 C CD2 . LEU E  4 179 ? 56.791  40.073  157.157 1.00 219.01 ?  170 LEU E CD2 1 
ATOM   11087 N N   . GLN E  4 180 ? 59.757  43.831  159.220 1.00 242.92 ?  171 GLN E N   1 
ATOM   11088 C CA  . GLN E  4 180 ? 61.073  44.251  158.777 1.00 248.85 ?  171 GLN E CA  1 
ATOM   11089 C C   . GLN E  4 180 ? 61.646  43.264  157.766 1.00 252.26 ?  171 GLN E C   1 
ATOM   11090 O O   . GLN E  4 180 ? 61.188  42.125  157.635 1.00 246.28 ?  171 GLN E O   1 
ATOM   11091 C CB  . GLN E  4 180 ? 62.005  44.412  159.975 1.00 250.16 ?  171 GLN E CB  1 
ATOM   11092 C CG  . GLN E  4 180 ? 61.536  45.497  160.935 1.00 250.96 ?  171 GLN E CG  1 
ATOM   11093 C CD  . GLN E  4 180 ? 62.304  45.509  162.240 1.00 250.25 ?  171 GLN E CD  1 
ATOM   11094 O OE1 . GLN E  4 180 ? 63.036  46.456  162.533 1.00 257.52 ?  171 GLN E OE1 1 
ATOM   11095 N NE2 . GLN E  4 180 ? 62.144  44.455  163.033 1.00 242.83 ?  171 GLN E NE2 1 
ATOM   11096 N N   . SER E  4 181 ? 62.662  43.725  157.034 1.00 256.41 ?  172 SER E N   1 
ATOM   11097 C CA  . SER E  4 181 ? 63.314  42.865  156.054 1.00 258.77 ?  172 SER E CA  1 
ATOM   11098 C C   . SER E  4 181 ? 63.916  41.617  156.689 1.00 255.60 ?  172 SER E C   1 
ATOM   11099 O O   . SER E  4 181 ? 64.153  40.630  155.986 1.00 256.07 ?  172 SER E O   1 
ATOM   11100 C CB  . SER E  4 181 ? 64.400  43.646  155.319 1.00 267.99 ?  172 SER E CB  1 
ATOM   11101 O OG  . SER E  4 181 ? 65.409  44.069  156.220 1.00 273.88 ?  172 SER E OG  1 
ATOM   11102 N N   . SER E  4 182 ? 64.176  41.644  157.995 1.00 249.90 ?  173 SER E N   1 
ATOM   11103 C CA  . SER E  4 182 ? 64.722  40.493  158.704 1.00 246.83 ?  173 SER E CA  1 
ATOM   11104 C C   . SER E  4 182 ? 63.694  39.392  158.943 1.00 238.85 ?  173 SER E C   1 
ATOM   11105 O O   . SER E  4 182 ? 64.084  38.250  159.216 1.00 236.75 ?  173 SER E O   1 
ATOM   11106 C CB  . SER E  4 182 ? 65.322  40.940  160.035 1.00 247.31 ?  173 SER E CB  1 
ATOM   11107 O OG  . SER E  4 182 ? 64.312  41.441  160.890 1.00 241.45 ?  173 SER E OG  1 
ATOM   11108 N N   . GLY E  4 183 ? 62.401  39.696  158.839 1.00 257.49 ?  174 GLY E N   1 
ATOM   11109 C CA  . GLY E  4 183 ? 61.365  38.736  159.157 1.00 249.08 ?  174 GLY E CA  1 
ATOM   11110 C C   . GLY E  4 183 ? 60.787  38.862  160.550 1.00 244.27 ?  174 GLY E C   1 
ATOM   11111 O O   . GLY E  4 183 ? 59.900  38.076  160.907 1.00 239.12 ?  174 GLY E O   1 
ATOM   11112 N N   . LEU E  4 184 ? 61.259  39.821  161.344 1.00 231.32 ?  175 LEU E N   1 
ATOM   11113 C CA  . LEU E  4 184 ? 60.705  40.133  162.653 1.00 227.60 ?  175 LEU E CA  1 
ATOM   11114 C C   . LEU E  4 184 ? 59.897  41.423  162.567 1.00 229.43 ?  175 LEU E C   1 
ATOM   11115 O O   . LEU E  4 184 ? 60.189  42.305  161.754 1.00 234.95 ?  175 LEU E O   1 
ATOM   11116 C CB  . LEU E  4 184 ? 61.809  40.260  163.706 1.00 228.93 ?  175 LEU E CB  1 
ATOM   11117 C CG  . LEU E  4 184 ? 62.773  39.074  163.796 1.00 228.16 ?  175 LEU E CG  1 
ATOM   11118 C CD1 . LEU E  4 184 ? 63.801  39.299  164.891 1.00 229.70 ?  175 LEU E CD1 1 
ATOM   11119 C CD2 . LEU E  4 184 ? 62.012  37.776  164.031 1.00 221.69 ?  175 LEU E CD2 1 
ATOM   11120 N N   . TYR E  4 185 ? 58.880  41.528  163.420 1.00 228.89 ?  176 TYR E N   1 
ATOM   11121 C CA  . TYR E  4 185 ? 58.028  42.706  163.451 1.00 230.42 ?  176 TYR E CA  1 
ATOM   11122 C C   . TYR E  4 185 ? 58.640  43.827  164.287 1.00 233.99 ?  176 TYR E C   1 
ATOM   11123 O O   . TYR E  4 185 ? 59.481  43.605  165.162 1.00 233.65 ?  176 TYR E O   1 
ATOM   11124 C CB  . TYR E  4 185 ? 56.653  42.336  164.010 1.00 224.47 ?  176 TYR E CB  1 
ATOM   11125 C CG  . TYR E  4 185 ? 55.933  41.311  163.168 1.00 221.33 ?  176 TYR E CG  1 
ATOM   11126 C CD1 . TYR E  4 185 ? 55.132  41.695  162.103 1.00 223.05 ?  176 TYR E CD1 1 
ATOM   11127 C CD2 . TYR E  4 185 ? 56.068  39.954  163.432 1.00 216.91 ?  176 TYR E CD2 1 
ATOM   11128 C CE1 . TYR E  4 185 ? 54.481  40.757  161.328 1.00 220.42 ?  176 TYR E CE1 1 
ATOM   11129 C CE2 . TYR E  4 185 ? 55.422  39.009  162.663 1.00 214.34 ?  176 TYR E CE2 1 
ATOM   11130 C CZ  . TYR E  4 185 ? 54.630  39.415  161.613 1.00 216.08 ?  176 TYR E CZ  1 
ATOM   11131 O OH  . TYR E  4 185 ? 53.986  38.472  160.847 1.00 213.69 ?  176 TYR E OH  1 
ATOM   11132 N N   . SER E  4 186 ? 58.199  45.052  163.995 1.00 230.71 ?  177 SER E N   1 
ATOM   11133 C CA  . SER E  4 186 ? 58.568  46.234  164.759 1.00 234.32 ?  177 SER E CA  1 
ATOM   11134 C C   . SER E  4 186 ? 57.443  47.256  164.690 1.00 235.48 ?  177 SER E C   1 
ATOM   11135 O O   . SER E  4 186 ? 56.725  47.348  163.691 1.00 236.65 ?  177 SER E O   1 
ATOM   11136 C CB  . SER E  4 186 ? 59.871  46.861  164.247 1.00 241.32 ?  177 SER E CB  1 
ATOM   11137 O OG  . SER E  4 186 ? 60.286  47.939  165.071 1.00 244.91 ?  177 SER E OG  1 
ATOM   11138 N N   . LEU E  4 187 ? 57.293  48.014  165.772 1.00 238.75 ?  178 LEU E N   1 
ATOM   11139 C CA  . LEU E  4 187 ? 56.408  49.167  165.797 1.00 242.81 ?  178 LEU E CA  1 
ATOM   11140 C C   . LEU E  4 187 ? 56.965  50.170  166.794 1.00 245.97 ?  178 LEU E C   1 
ATOM   11141 O O   . LEU E  4 187 ? 57.841  49.852  167.603 1.00 244.23 ?  178 LEU E O   1 
ATOM   11142 C CB  . LEU E  4 187 ? 54.966  48.759  166.141 1.00 236.89 ?  178 LEU E CB  1 
ATOM   11143 C CG  . LEU E  4 187 ? 54.603  48.145  167.503 1.00 231.19 ?  178 LEU E CG  1 
ATOM   11144 C CD1 . LEU E  4 187 ? 54.567  49.159  168.650 1.00 234.07 ?  178 LEU E CD1 1 
ATOM   11145 C CD2 . LEU E  4 187 ? 53.277  47.400  167.408 1.00 226.50 ?  178 LEU E CD2 1 
ATOM   11146 N N   . SER E  4 188 ? 56.449  51.391  166.729 1.00 258.13 ?  179 SER E N   1 
ATOM   11147 C CA  . SER E  4 188 ? 56.677  52.374  167.773 1.00 260.74 ?  179 SER E CA  1 
ATOM   11148 C C   . SER E  4 188 ? 55.346  52.742  168.409 1.00 258.55 ?  179 SER E C   1 
ATOM   11149 O O   . SER E  4 188 ? 54.302  52.742  167.749 1.00 258.27 ?  179 SER E O   1 
ATOM   11150 C CB  . SER E  4 188 ? 57.351  53.634  167.223 1.00 271.59 ?  179 SER E CB  1 
ATOM   11151 O OG  . SER E  4 188 ? 58.718  53.395  166.948 1.00 274.08 ?  179 SER E OG  1 
ATOM   11152 N N   . SER E  4 189 ? 55.393  53.062  169.697 1.00 248.86 ?  180 SER E N   1 
ATOM   11153 C CA  . SER E  4 189 ? 54.267  53.657  170.400 1.00 248.46 ?  180 SER E CA  1 
ATOM   11154 C C   . SER E  4 189 ? 54.707  55.010  170.929 1.00 254.87 ?  180 SER E C   1 
ATOM   11155 O O   . SER E  4 189 ? 55.699  55.099  171.657 1.00 255.49 ?  180 SER E O   1 
ATOM   11156 C CB  . SER E  4 189 ? 53.789  52.761  171.542 1.00 240.94 ?  180 SER E CB  1 
ATOM   11157 O OG  . SER E  4 189 ? 52.691  53.348  172.219 1.00 240.86 ?  180 SER E OG  1 
ATOM   11158 N N   . VAL E  4 190 ? 53.971  56.054  170.565 1.00 247.60 ?  181 VAL E N   1 
ATOM   11159 C CA  . VAL E  4 190 ? 54.290  57.412  170.975 1.00 254.46 ?  181 VAL E CA  1 
ATOM   11160 C C   . VAL E  4 190 ? 53.093  57.995  171.713 1.00 254.47 ?  181 VAL E C   1 
ATOM   11161 O O   . VAL E  4 190 ? 51.963  57.514  171.606 1.00 250.56 ?  181 VAL E O   1 
ATOM   11162 C CB  . VAL E  4 190 ? 54.690  58.310  169.787 1.00 262.70 ?  181 VAL E CB  1 
ATOM   11163 C CG1 . VAL E  4 190 ? 55.908  57.737  169.078 1.00 263.19 ?  181 VAL E CG1 1 
ATOM   11164 C CG2 . VAL E  4 190 ? 53.525  58.478  168.824 1.00 272.49 ?  181 VAL E CG2 1 
ATOM   11165 N N   . VAL E  4 191 ? 53.365  59.044  172.478 1.00 267.33 ?  182 VAL E N   1 
ATOM   11166 C CA  . VAL E  4 191 ? 52.333  59.781  173.194 1.00 268.61 ?  182 VAL E CA  1 
ATOM   11167 C C   . VAL E  4 191 ? 52.770  61.234  173.232 1.00 277.48 ?  182 VAL E C   1 
ATOM   11168 O O   . VAL E  4 191 ? 53.963  61.530  173.339 1.00 280.86 ?  182 VAL E O   1 
ATOM   11169 C CB  . VAL E  4 191 ? 52.111  59.214  174.613 1.00 262.54 ?  182 VAL E CB  1 
ATOM   11170 C CG1 . VAL E  4 191 ? 53.405  59.256  175.407 1.00 263.20 ?  182 VAL E CG1 1 
ATOM   11171 C CG2 . VAL E  4 191 ? 51.018  59.985  175.336 1.00 263.98 ?  182 VAL E CG2 1 
ATOM   11172 N N   . THR E  4 192 ? 51.811  62.144  173.118 1.00 267.67 ?  183 THR E N   1 
ATOM   11173 C CA  . THR E  4 192 ? 52.107  63.557  173.277 1.00 276.20 ?  183 THR E CA  1 
ATOM   11174 C C   . THR E  4 192 ? 51.598  64.030  174.629 1.00 275.84 ?  183 THR E C   1 
ATOM   11175 O O   . THR E  4 192 ? 50.486  63.688  175.045 1.00 271.71 ?  183 THR E O   1 
ATOM   11176 C CB  . THR E  4 192 ? 51.469  64.376  172.154 1.00 282.52 ?  183 THR E CB  1 
ATOM   11177 O OG1 . THR E  4 192 ? 50.076  64.053  172.059 1.00 279.79 ?  183 THR E OG1 1 
ATOM   11178 C CG2 . THR E  4 192 ? 52.150  64.066  170.831 1.00 286.08 ?  183 THR E CG2 1 
ATOM   11179 N N   . VAL E  4 193 ? 52.420  64.826  175.305 1.00 284.11 ?  184 VAL E N   1 
ATOM   11180 C CA  . VAL E  4 193 ? 52.149  65.243  176.679 1.00 283.97 ?  184 VAL E CA  1 
ATOM   11181 C C   . VAL E  4 193 ? 52.620  66.677  176.857 1.00 293.40 ?  184 VAL E C   1 
ATOM   11182 O O   . VAL E  4 193 ? 53.442  67.180  176.078 1.00 299.27 ?  184 VAL E O   1 
ATOM   11183 C CB  . VAL E  4 193 ? 52.851  64.324  177.703 1.00 277.28 ?  184 VAL E CB  1 
ATOM   11184 C CG1 . VAL E  4 193 ? 52.351  62.888  177.584 1.00 267.94 ?  184 VAL E CG1 1 
ATOM   11185 C CG2 . VAL E  4 193 ? 54.355  64.375  177.507 1.00 280.19 ?  184 VAL E CG2 1 
ATOM   11186 N N   . PRO E  4 194 ? 52.110  67.367  177.878 1.00 297.06 ?  185 PRO E N   1 
ATOM   11187 C CA  . PRO E  4 194 ? 52.610  68.718  178.168 1.00 306.67 ?  185 PRO E CA  1 
ATOM   11188 C C   . PRO E  4 194 ? 54.084  68.712  178.552 1.00 307.53 ?  185 PRO E C   1 
ATOM   11189 O O   . PRO E  4 194 ? 54.548  67.854  179.306 1.00 301.68 ?  185 PRO E O   1 
ATOM   11190 C CB  . PRO E  4 194 ? 51.721  69.189  179.326 1.00 306.97 ?  185 PRO E CB  1 
ATOM   11191 C CG  . PRO E  4 194 ? 50.508  68.317  179.261 1.00 300.76 ?  185 PRO E CG  1 
ATOM   11192 C CD  . PRO E  4 194 ? 50.967  67.003  178.734 1.00 292.44 ?  185 PRO E CD  1 
ATOM   11193 N N   . SER E  4 195 ? 54.824  69.684  178.010 1.00 303.01 ?  186 SER E N   1 
ATOM   11194 C CA  . SER E  4 195 ? 56.237  69.823  178.350 1.00 305.90 ?  186 SER E CA  1 
ATOM   11195 C C   . SER E  4 195 ? 56.448  70.075  179.838 1.00 305.28 ?  186 SER E C   1 
ATOM   11196 O O   . SER E  4 195 ? 57.475  69.671  180.394 1.00 304.80 ?  186 SER E O   1 
ATOM   11197 C CB  . SER E  4 195 ? 56.872  70.943  177.528 1.00 320.19 ?  186 SER E CB  1 
ATOM   11198 O OG  . SER E  4 195 ? 56.783  70.657  176.145 1.00 323.96 ?  186 SER E OG  1 
ATOM   11199 N N   . SER E  4 196 ? 55.505  70.759  180.493 1.00 304.99 ?  187 SER E N   1 
ATOM   11200 C CA  . SER E  4 196 ? 55.602  70.976  181.933 1.00 304.40 ?  187 SER E CA  1 
ATOM   11201 C C   . SER E  4 196 ? 55.650  69.677  182.728 1.00 294.30 ?  187 SER E C   1 
ATOM   11202 O O   . SER E  4 196 ? 56.122  69.682  183.870 1.00 293.42 ?  187 SER E O   1 
ATOM   11203 C CB  . SER E  4 196 ? 54.421  71.826  182.412 1.00 307.50 ?  187 SER E CB  1 
ATOM   11204 O OG  . SER E  4 196 ? 53.185  71.167  182.191 1.00 301.31 ?  187 SER E OG  1 
ATOM   11205 N N   . SER E  4 197 ? 55.163  68.575  182.165 1.00 305.95 ?  188 SER E N   1 
ATOM   11206 C CA  . SER E  4 197 ? 55.124  67.302  182.871 1.00 295.76 ?  188 SER E CA  1 
ATOM   11207 C C   . SER E  4 197 ? 56.413  66.489  182.781 1.00 293.18 ?  188 SER E C   1 
ATOM   11208 O O   . SER E  4 197 ? 56.532  65.484  183.490 1.00 286.21 ?  188 SER E O   1 
ATOM   11209 C CB  . SER E  4 197 ? 53.956  66.459  182.357 1.00 289.51 ?  188 SER E CB  1 
ATOM   11210 O OG  . SER E  4 197 ? 54.254  65.909  181.088 1.00 289.08 ?  188 SER E OG  1 
ATOM   11211 N N   . LEU E  4 198 ? 57.372  66.873  181.937 1.00 288.36 ?  189 LEU E N   1 
ATOM   11212 C CA  . LEU E  4 198 ? 58.599  66.092  181.815 1.00 285.78 ?  189 LEU E CA  1 
ATOM   11213 C C   . LEU E  4 198 ? 59.391  66.151  183.117 1.00 285.73 ?  189 LEU E C   1 
ATOM   11214 O O   . LEU E  4 198 ? 59.688  67.234  183.629 1.00 292.82 ?  189 LEU E O   1 
ATOM   11215 C CB  . LEU E  4 198 ? 59.452  66.590  180.647 1.00 292.51 ?  189 LEU E CB  1 
ATOM   11216 C CG  . LEU E  4 198 ? 58.860  66.510  179.236 1.00 293.24 ?  189 LEU E CG  1 
ATOM   11217 C CD1 . LEU E  4 198 ? 59.823  67.094  178.212 1.00 300.78 ?  189 LEU E CD1 1 
ATOM   11218 C CD2 . LEU E  4 198 ? 58.497  65.079  178.872 1.00 284.15 ?  189 LEU E CD2 1 
ATOM   11219 N N   . GLY E  4 199 ? 59.742  64.977  183.644 1.00 277.31 ?  190 GLY E N   1 
ATOM   11220 C CA  . GLY E  4 199 ? 60.481  64.854  184.881 1.00 278.48 ?  190 GLY E CA  1 
ATOM   11221 C C   . GLY E  4 199 ? 59.611  64.846  186.124 1.00 277.47 ?  190 GLY E C   1 
ATOM   11222 O O   . GLY E  4 199 ? 59.987  64.239  187.132 1.00 283.29 ?  190 GLY E O   1 
ATOM   11223 N N   . THR E  4 200 ? 58.452  65.507  186.069 1.00 278.37 ?  191 THR E N   1 
ATOM   11224 C CA  . THR E  4 200 ? 57.508  65.545  187.182 1.00 275.10 ?  191 THR E CA  1 
ATOM   11225 C C   . THR E  4 200 ? 56.590  64.328  187.175 1.00 266.26 ?  191 THR E C   1 
ATOM   11226 O O   . THR E  4 200 ? 56.302  63.754  188.232 1.00 264.32 ?  191 THR E O   1 
ATOM   11227 C CB  . THR E  4 200 ? 56.682  66.833  187.130 1.00 282.50 ?  191 THR E CB  1 
ATOM   11228 O OG1 . THR E  4 200 ? 57.545  67.964  187.299 1.00 291.84 ?  191 THR E OG1 1 
ATOM   11229 C CG2 . THR E  4 200 ? 55.627  66.845  188.234 1.00 279.34 ?  191 THR E CG2 1 
ATOM   11230 N N   . GLN E  4 201 ? 56.146  63.913  185.993 1.00 280.11 ?  192 GLN E N   1 
ATOM   11231 C CA  . GLN E  4 201 ? 55.340  62.715  185.812 1.00 271.88 ?  192 GLN E CA  1 
ATOM   11232 C C   . GLN E  4 201 ? 56.203  61.643  185.164 1.00 266.75 ?  192 GLN E C   1 
ATOM   11233 O O   . GLN E  4 201 ? 56.835  61.887  184.130 1.00 270.74 ?  192 GLN E O   1 
ATOM   11234 C CB  . GLN E  4 201 ? 54.120  63.021  184.935 1.00 272.36 ?  192 GLN E CB  1 
ATOM   11235 C CG  . GLN E  4 201 ? 53.271  61.823  184.512 1.00 264.47 ?  192 GLN E CG  1 
ATOM   11236 C CD  . GLN E  4 201 ? 52.558  61.164  185.673 1.00 259.08 ?  192 GLN E CD  1 
ATOM   11237 O OE1 . GLN E  4 201 ? 51.841  61.821  186.427 1.00 262.24 ?  192 GLN E OE1 1 
ATOM   11238 N NE2 . GLN E  4 201 ? 52.726  59.854  185.806 1.00 251.45 ?  192 GLN E NE2 1 
ATOM   11239 N N   . THR E  4 202 ? 56.231  60.465  185.782 1.00 264.78 ?  193 THR E N   1 
ATOM   11240 C CA  . THR E  4 202 ? 56.964  59.331  185.241 1.00 261.01 ?  193 THR E CA  1 
ATOM   11241 C C   . THR E  4 202 ? 56.180  58.696  184.100 1.00 256.79 ?  193 THR E C   1 
ATOM   11242 O O   . THR E  4 202 ? 54.956  58.549  184.172 1.00 254.16 ?  193 THR E O   1 
ATOM   11243 C CB  . THR E  4 202 ? 57.225  58.299  186.347 1.00 255.35 ?  193 THR E CB  1 
ATOM   11244 O OG1 . THR E  4 202 ? 58.134  58.842  187.313 1.00 261.19 ?  193 THR E OG1 1 
ATOM   11245 C CG2 . THR E  4 202 ? 57.822  57.020  185.780 1.00 252.21 ?  193 THR E CG2 1 
ATOM   11246 N N   . TYR E  4 203 ? 56.895  58.319  183.040 1.00 254.77 ?  194 TYR E N   1 
ATOM   11247 C CA  . TYR E  4 203 ? 56.302  57.668  181.879 1.00 252.06 ?  194 TYR E CA  1 
ATOM   11248 C C   . TYR E  4 203 ? 56.968  56.320  181.659 1.00 247.15 ?  194 TYR E C   1 
ATOM   11249 O O   . TYR E  4 203 ? 58.186  56.243  181.464 1.00 249.90 ?  194 TYR E O   1 
ATOM   11250 C CB  . TYR E  4 203 ? 56.429  58.534  180.623 1.00 258.44 ?  194 TYR E CB  1 
ATOM   11251 C CG  . TYR E  4 203 ? 55.626  59.809  180.672 1.00 264.52 ?  194 TYR E CG  1 
ATOM   11252 C CD1 . TYR E  4 203 ? 54.242  59.768  180.595 1.00 262.15 ?  194 TYR E CD1 1 
ATOM   11253 C CD2 . TYR E  4 203 ? 56.242  61.049  180.774 1.00 272.52 ?  194 TYR E CD2 1 
ATOM   11254 C CE1 . TYR E  4 203 ? 53.490  60.919  180.628 1.00 267.61 ?  194 TYR E CE1 1 
ATOM   11255 C CE2 . TYR E  4 203 ? 55.495  62.213  180.809 1.00 278.10 ?  194 TYR E CE2 1 
ATOM   11256 C CZ  . TYR E  4 203 ? 54.119  62.139  180.734 1.00 275.18 ?  194 TYR E CZ  1 
ATOM   11257 O OH  . TYR E  4 203 ? 53.364  63.287  180.772 1.00 281.24 ?  194 TYR E OH  1 
ATOM   11258 N N   . ILE E  4 204 ? 56.158  55.267  181.696 1.00 243.21 ?  195 ILE E N   1 
ATOM   11259 C CA  . ILE E  4 204 ? 56.598  53.892  181.526 1.00 237.99 ?  195 ILE E CA  1 
ATOM   11260 C C   . ILE E  4 204 ? 55.696  53.256  180.481 1.00 237.33 ?  195 ILE E C   1 
ATOM   11261 O O   . ILE E  4 204 ? 54.469  53.281  180.626 1.00 237.68 ?  195 ILE E O   1 
ATOM   11262 C CB  . ILE E  4 204 ? 56.524  53.111  182.852 1.00 235.98 ?  195 ILE E CB  1 
ATOM   11263 C CG1 . ILE E  4 204 ? 57.461  53.735  183.887 1.00 236.59 ?  195 ILE E CG1 1 
ATOM   11264 C CG2 . ILE E  4 204 ? 56.858  51.648  182.629 1.00 234.34 ?  195 ILE E CG2 1 
ATOM   11265 C CD1 . ILE E  4 204 ? 57.268  53.204  185.288 1.00 235.01 ?  195 ILE E CD1 1 
ATOM   11266 N N   . CYS E  4 205 ? 56.289  52.689  179.435 1.00 260.04 ?  196 CYS E N   1 
ATOM   11267 C CA  . CYS E  4 205 ? 55.522  51.894  178.488 1.00 256.55 ?  196 CYS E CA  1 
ATOM   11268 C C   . CYS E  4 205 ? 55.586  50.425  178.881 1.00 249.74 ?  196 CYS E C   1 
ATOM   11269 O O   . CYS E  4 205 ? 56.652  49.903  179.215 1.00 249.98 ?  196 CYS E O   1 
ATOM   11270 C CB  . CYS E  4 205 ? 56.036  52.101  177.057 1.00 261.84 ?  196 CYS E CB  1 
ATOM   11271 S SG  . CYS E  4 205 ? 57.661  51.375  176.678 1.00 264.14 ?  196 CYS E SG  1 
ATOM   11272 N N   . ASN E  4 206 ? 54.432  49.768  178.845 1.00 247.33 ?  197 ASN E N   1 
ATOM   11273 C CA  . ASN E  4 206 ? 54.292  48.370  179.229 1.00 241.19 ?  197 ASN E CA  1 
ATOM   11274 C C   . ASN E  4 206 ? 54.014  47.572  177.967 1.00 239.12 ?  197 ASN E C   1 
ATOM   11275 O O   . ASN E  4 206 ? 52.978  47.770  177.323 1.00 238.70 ?  197 ASN E O   1 
ATOM   11276 C CB  . ASN E  4 206 ? 53.176  48.187  180.256 1.00 237.30 ?  197 ASN E CB  1 
ATOM   11277 C CG  . ASN E  4 206 ? 53.087  49.347  181.219 1.00 240.60 ?  197 ASN E CG  1 
ATOM   11278 O OD1 . ASN E  4 206 ? 52.164  50.155  181.150 1.00 242.35 ?  197 ASN E OD1 1 
ATOM   11279 N ND2 . ASN E  4 206 ? 54.051  49.435  182.128 1.00 241.47 ?  197 ASN E ND2 1 
ATOM   11280 N N   . VAL E  4 207 ? 54.935  46.679  177.617 1.00 253.26 ?  198 VAL E N   1 
ATOM   11281 C CA  . VAL E  4 207 ? 54.895  45.953  176.352 1.00 251.99 ?  198 VAL E CA  1 
ATOM   11282 C C   . VAL E  4 207 ? 54.850  44.471  176.690 1.00 246.79 ?  198 VAL E C   1 
ATOM   11283 O O   . VAL E  4 207 ? 55.814  43.919  177.237 1.00 247.70 ?  198 VAL E O   1 
ATOM   11284 C CB  . VAL E  4 207 ? 56.102  46.279  175.459 1.00 257.52 ?  198 VAL E CB  1 
ATOM   11285 C CG1 . VAL E  4 207 ? 56.006  45.527  174.137 1.00 257.60 ?  198 VAL E CG1 1 
ATOM   11286 C CG2 . VAL E  4 207 ? 56.221  47.788  175.228 1.00 266.19 ?  198 VAL E CG2 1 
ATOM   11287 N N   . ASN E  4 208 ? 53.728  43.832  176.375 1.00 255.51 ?  199 ASN E N   1 
ATOM   11288 C CA  . ASN E  4 208 ? 53.529  42.411  176.608 1.00 250.75 ?  199 ASN E CA  1 
ATOM   11289 C C   . ASN E  4 208 ? 53.467  41.665  175.280 1.00 249.60 ?  199 ASN E C   1 
ATOM   11290 O O   . ASN E  4 208 ? 52.860  42.142  174.315 1.00 252.02 ?  199 ASN E O   1 
ATOM   11291 C CB  . ASN E  4 208 ? 52.246  42.184  177.414 1.00 249.27 ?  199 ASN E CB  1 
ATOM   11292 C CG  . ASN E  4 208 ? 52.296  42.845  178.788 1.00 253.61 ?  199 ASN E CG  1 
ATOM   11293 O OD1 . ASN E  4 208 ? 53.345  43.323  179.224 1.00 256.88 ?  199 ASN E OD1 1 
ATOM   11294 N ND2 . ASN E  4 208 ? 51.159  42.873  179.473 1.00 254.34 ?  199 ASN E ND2 1 
ATOM   11295 N N   . HIS E  4 209 ? 54.095  40.492  175.237 1.00 232.33 ?  200 HIS E N   1 
ATOM   11296 C CA  . HIS E  4 209 ? 54.086  39.626  174.060 1.00 232.26 ?  200 HIS E CA  1 
ATOM   11297 C C   . HIS E  4 209 ? 53.777  38.210  174.526 1.00 230.84 ?  200 HIS E C   1 
ATOM   11298 O O   . HIS E  4 209 ? 54.641  37.535  175.092 1.00 229.66 ?  200 HIS E O   1 
ATOM   11299 C CB  . HIS E  4 209 ? 55.420  39.684  173.333 1.00 232.40 ?  200 HIS E CB  1 
ATOM   11300 C CG  . HIS E  4 209 ? 55.443  38.916  172.053 1.00 232.56 ?  200 HIS E CG  1 
ATOM   11301 N ND1 . HIS E  4 209 ? 56.257  37.821  171.864 1.00 231.55 ?  200 HIS E ND1 1 
ATOM   11302 C CD2 . HIS E  4 209 ? 54.752  39.077  170.900 1.00 233.66 ?  200 HIS E CD2 1 
ATOM   11303 C CE1 . HIS E  4 209 ? 56.069  37.341  170.648 1.00 232.05 ?  200 HIS E CE1 1 
ATOM   11304 N NE2 . HIS E  4 209 ? 55.162  38.085  170.042 1.00 233.32 ?  200 HIS E NE2 1 
ATOM   11305 N N   . LYS E  4 210 ? 52.552  37.769  174.290 1.00 241.93 ?  201 LYS E N   1 
ATOM   11306 C CA  . LYS E  4 210 ? 52.110  36.482  174.810 1.00 237.16 ?  201 LYS E CA  1 
ATOM   11307 C C   . LYS E  4 210 ? 52.795  35.259  174.197 1.00 236.16 ?  201 LYS E C   1 
ATOM   11308 O O   . LYS E  4 210 ? 53.053  34.298  174.934 1.00 233.42 ?  201 LYS E O   1 
ATOM   11309 C CB  . LYS E  4 210 ? 50.595  36.333  174.669 1.00 234.50 ?  201 LYS E CB  1 
ATOM   11310 C CG  . LYS E  4 210 ? 50.066  35.118  175.431 1.00 229.84 ?  201 LYS E CG  1 
ATOM   11311 C CD  . LYS E  4 210 ? 48.561  34.943  175.328 1.00 229.06 ?  201 LYS E CD  1 
ATOM   11312 C CE  . LYS E  4 210 ? 48.078  33.885  176.316 1.00 230.22 ?  201 LYS E CE  1 
ATOM   11313 N NZ  . LYS E  4 210 ? 48.191  32.505  175.764 1.00 228.06 1  201 LYS E NZ  1 
ATOM   11314 N N   . PRO E  4 211 ? 53.073  35.207  172.879 1.00 231.34 ?  202 PRO E N   1 
ATOM   11315 C CA  . PRO E  4 211 ? 53.709  33.983  172.357 1.00 230.49 ?  202 PRO E CA  1 
ATOM   11316 C C   . PRO E  4 211 ? 55.008  33.664  173.064 1.00 231.34 ?  202 PRO E C   1 
ATOM   11317 O O   . PRO E  4 211 ? 55.302  32.488  173.314 1.00 229.14 ?  202 PRO E O   1 
ATOM   11318 C CB  . PRO E  4 211 ? 53.918  34.306  170.874 1.00 234.05 ?  202 PRO E CB  1 
ATOM   11319 C CG  . PRO E  4 211 ? 52.824  35.255  170.561 1.00 234.77 ?  202 PRO E CG  1 
ATOM   11320 C CD  . PRO E  4 211 ? 52.693  36.119  171.784 1.00 234.60 ?  202 PRO E CD  1 
ATOM   11321 N N   . SER E  4 212 ? 55.800  34.678  173.397 1.00 244.29 ?  203 SER E N   1 
ATOM   11322 C CA  . SER E  4 212 ? 57.023  34.428  174.133 1.00 245.08 ?  203 SER E CA  1 
ATOM   11323 C C   . SER E  4 212 ? 56.777  34.648  175.612 1.00 244.72 ?  203 SER E C   1 
ATOM   11324 O O   . SER E  4 212 ? 57.690  34.463  176.422 1.00 246.24 ?  203 SER E O   1 
ATOM   11325 C CB  . SER E  4 212 ? 58.171  35.312  173.638 1.00 251.09 ?  203 SER E CB  1 
ATOM   11326 O OG  . SER E  4 212 ? 57.871  36.683  173.799 1.00 252.28 ?  203 SER E OG  1 
ATOM   11327 N N   . ASN E  4 213 ? 55.538  35.003  175.969 1.00 256.93 ?  204 ASN E N   1 
ATOM   11328 C CA  . ASN E  4 213 ? 55.158  35.329  177.340 1.00 255.51 ?  204 ASN E CA  1 
ATOM   11329 C C   . ASN E  4 213 ? 56.090  36.354  177.973 1.00 261.45 ?  204 ASN E C   1 
ATOM   11330 O O   . ASN E  4 213 ? 56.737  36.068  178.966 1.00 262.25 ?  204 ASN E O   1 
ATOM   11331 C CB  . ASN E  4 213 ? 54.995  34.108  178.235 1.00 253.20 ?  204 ASN E CB  1 
ATOM   11332 C CG  . ASN E  4 213 ? 54.088  34.414  179.432 1.00 256.87 ?  204 ASN E CG  1 
ATOM   11333 O OD1 . ASN E  4 213 ? 54.505  34.427  180.596 1.00 256.30 ?  204 ASN E OD1 1 
ATOM   11334 N ND2 . ASN E  4 213 ? 52.848  34.766  179.118 1.00 261.47 ?  204 ASN E ND2 1 
ATOM   11335 N N   . THR E  4 214 ? 56.343  37.453  177.282 1.00 245.31 ?  205 THR E N   1 
ATOM   11336 C CA  . THR E  4 214 ? 57.229  38.471  177.828 1.00 250.44 ?  205 THR E CA  1 
ATOM   11337 C C   . THR E  4 214 ? 56.411  39.724  178.126 1.00 250.05 ?  205 THR E C   1 
ATOM   11338 O O   . THR E  4 214 ? 55.428  40.024  177.444 1.00 249.13 ?  205 THR E O   1 
ATOM   11339 C CB  . THR E  4 214 ? 58.384  38.814  176.883 1.00 254.24 ?  205 THR E CB  1 
ATOM   11340 O OG1 . THR E  4 214 ? 57.860  39.163  175.597 1.00 255.76 ?  205 THR E OG1 1 
ATOM   11341 C CG2 . THR E  4 214 ? 59.363  37.640  176.756 1.00 254.77 ?  205 THR E CG2 1 
ATOM   11342 N N   . LYS E  4 215 ? 56.818  40.434  179.180 1.00 262.55 ?  206 LYS E N   1 
ATOM   11343 C CA  . LYS E  4 215 ? 56.241  41.710  179.589 1.00 265.22 ?  206 LYS E CA  1 
ATOM   11344 C C   . LYS E  4 215 ? 57.388  42.660  179.867 1.00 270.98 ?  206 LYS E C   1 
ATOM   11345 O O   . LYS E  4 215 ? 58.363  42.262  180.495 1.00 273.04 ?  206 LYS E O   1 
ATOM   11346 C CB  . LYS E  4 215 ? 55.421  41.582  180.881 1.00 263.41 ?  206 LYS E CB  1 
ATOM   11347 C CG  . LYS E  4 215 ? 54.200  40.692  180.825 1.00 261.08 ?  206 LYS E CG  1 
ATOM   11348 C CD  . LYS E  4 215 ? 53.494  40.706  182.176 1.00 260.13 ?  206 LYS E CD  1 
ATOM   11349 C CE  . LYS E  4 215 ? 52.179  39.941  182.162 1.00 259.10 ?  206 LYS E CE  1 
ATOM   11350 N NZ  . LYS E  4 215 ? 52.375  38.508  181.784 1.00 261.03 1  206 LYS E NZ  1 
ATOM   11351 N N   . VAL E  4 216 ? 57.389  43.819  179.223 1.00 245.61 ?  207 VAL E N   1 
ATOM   11352 C CA  . VAL E  4 216 ? 58.447  44.804  179.417 1.00 251.10 ?  207 VAL E CA  1 
ATOM   11353 C C   . VAL E  4 216 ? 57.850  46.133  179.859 1.00 253.98 ?  207 VAL E C   1 
ATOM   11354 O O   . VAL E  4 216 ? 56.834  46.578  179.317 1.00 254.05 ?  207 VAL E O   1 
ATOM   11355 C CB  . VAL E  4 216 ? 59.308  44.978  178.155 1.00 255.40 ?  207 VAL E CB  1 
ATOM   11356 C CG1 . VAL E  4 216 ? 60.318  46.096  178.355 1.00 261.57 ?  207 VAL E CG1 1 
ATOM   11357 C CG2 . VAL E  4 216 ? 60.022  43.686  177.855 1.00 253.15 ?  207 VAL E CG2 1 
ATOM   11358 N N   . ASP E  4 217 ? 58.469  46.749  180.864 1.00 260.64 ?  208 ASP E N   1 
ATOM   11359 C CA  . ASP E  4 217 ? 58.137  48.094  181.332 1.00 264.22 ?  208 ASP E CA  1 
ATOM   11360 C C   . ASP E  4 217 ? 59.378  48.950  181.125 1.00 270.44 ?  208 ASP E C   1 
ATOM   11361 O O   . ASP E  4 217 ? 60.475  48.520  181.482 1.00 270.89 ?  208 ASP E O   1 
ATOM   11362 C CB  . ASP E  4 217 ? 57.694  48.134  182.793 1.00 262.50 ?  208 ASP E CB  1 
ATOM   11363 C CG  . ASP E  4 217 ? 56.431  47.337  183.054 1.00 256.55 ?  208 ASP E CG  1 
ATOM   11364 O OD1 . ASP E  4 217 ? 55.407  47.534  182.359 1.00 255.41 ?  208 ASP E OD1 1 
ATOM   11365 O OD2 . ASP E  4 217 ? 56.459  46.525  183.997 1.00 253.36 -1 208 ASP E OD2 1 
ATOM   11366 N N   . LYS E  4 218 ? 59.302  49.932  180.244 1.00 245.74 ?  209 LYS E N   1 
ATOM   11367 C CA  . LYS E  4 218 ? 60.474  50.754  179.975 1.00 252.23 ?  209 LYS E CA  1 
ATOM   11368 C C   . LYS E  4 218 ? 60.207  52.205  180.379 1.00 257.29 ?  209 LYS E C   1 
ATOM   11369 O O   . LYS E  4 218 ? 59.309  52.849  179.823 1.00 258.45 ?  209 LYS E O   1 
ATOM   11370 C CB  . LYS E  4 218 ? 60.899  50.645  178.518 1.00 254.37 ?  209 LYS E CB  1 
ATOM   11371 C CG  . LYS E  4 218 ? 62.269  51.241  178.258 1.00 260.83 ?  209 LYS E CG  1 
ATOM   11372 C CD  . LYS E  4 218 ? 63.333  50.314  178.840 1.00 259.52 ?  209 LYS E CD  1 
ATOM   11373 C CE  . LYS E  4 218 ? 64.715  50.710  178.393 1.00 268.08 ?  209 LYS E CE  1 
ATOM   11374 N NZ  . LYS E  4 218 ? 65.683  49.643  178.757 1.00 268.30 1  209 LYS E NZ  1 
ATOM   11375 N N   . LYS E  4 219 ? 60.968  52.719  181.341 1.00 243.03 ?  210 LYS E N   1 
ATOM   11376 C CA  . LYS E  4 219 ? 60.835  54.124  181.702 1.00 248.57 ?  210 LYS E CA  1 
ATOM   11377 C C   . LYS E  4 219 ? 61.531  55.001  180.666 1.00 255.61 ?  210 LYS E C   1 
ATOM   11378 O O   . LYS E  4 219 ? 62.669  54.730  180.267 1.00 258.09 ?  210 LYS E O   1 
ATOM   11379 C CB  . LYS E  4 219 ? 61.422  54.374  183.090 1.00 249.62 ?  210 LYS E CB  1 
ATOM   11380 C CG  . LYS E  4 219 ? 61.230  55.791  183.596 1.00 255.20 ?  210 LYS E CG  1 
ATOM   11381 C CD  . LYS E  4 219 ? 61.684  55.958  185.041 1.00 255.52 ?  210 LYS E CD  1 
ATOM   11382 C CE  . LYS E  4 219 ? 61.675  57.428  185.455 1.00 262.20 ?  210 LYS E CE  1 
ATOM   11383 N NZ  . LYS E  4 219 ? 62.089  57.633  186.875 1.00 262.72 1  210 LYS E NZ  1 
ATOM   11384 N N   . VAL E  4 220 ? 60.835  56.046  180.227 1.00 246.52 ?  211 VAL E N   1 
ATOM   11385 C CA  . VAL E  4 220 ? 61.298  56.946  179.176 1.00 253.43 ?  211 VAL E CA  1 
ATOM   11386 C C   . VAL E  4 220 ? 61.431  58.337  179.782 1.00 259.78 ?  211 VAL E C   1 
ATOM   11387 O O   . VAL E  4 220 ? 60.431  58.930  180.204 1.00 259.47 ?  211 VAL E O   1 
ATOM   11388 C CB  . VAL E  4 220 ? 60.347  56.952  177.971 1.00 252.80 ?  211 VAL E CB  1 
ATOM   11389 C CG1 . VAL E  4 220 ? 60.902  57.830  176.877 1.00 260.61 ?  211 VAL E CG1 1 
ATOM   11390 C CG2 . VAL E  4 220 ? 60.140  55.536  177.458 1.00 246.24 ?  211 VAL E CG2 1 
ATOM   11391 N N   . GLU E  4 221 ? 62.651  58.851  179.833 1.00 256.88 ?  212 GLU E N   1 
ATOM   11392 C CA  . GLU E  4 221 ? 62.940  60.105  180.508 1.00 265.92 ?  212 GLU E CA  1 
ATOM   11393 C C   . GLU E  4 221 ? 63.860  60.946  179.638 1.00 273.64 ?  212 GLU E C   1 
ATOM   11394 O O   . GLU E  4 221 ? 64.513  60.423  178.729 1.00 271.56 ?  212 GLU E O   1 
ATOM   11395 C CB  . GLU E  4 221 ? 63.554  59.848  181.891 1.00 265.23 ?  212 GLU E CB  1 
ATOM   11396 C CG  . GLU E  4 221 ? 64.770  58.952  181.881 1.00 261.43 ?  212 GLU E CG  1 
ATOM   11397 C CD  . GLU E  4 221 ? 65.081  58.425  183.263 1.00 261.42 ?  212 GLU E CD  1 
ATOM   11398 O OE1 . GLU E  4 221 ? 65.703  57.348  183.367 1.00 262.23 ?  212 GLU E OE1 1 
ATOM   11399 O OE2 . GLU E  4 221 ? 64.666  59.071  184.248 1.00 266.38 -1 212 GLU E OE2 1 
ATOM   11400 N N   . PRO E  4 222 ? 63.922  62.258  179.883 1.00 267.51 ?  213 PRO E N   1 
ATOM   11401 C CA  . PRO E  4 222 ? 64.888  63.103  179.170 1.00 275.99 ?  213 PRO E CA  1 
ATOM   11402 C C   . PRO E  4 222 ? 66.318  62.596  179.302 1.00 275.17 ?  213 PRO E C   1 
ATOM   11403 O O   . PRO E  4 222 ? 66.769  62.214  180.384 1.00 273.47 ?  213 PRO E O   1 
ATOM   11404 C CB  . PRO E  4 222 ? 64.712  64.475  179.831 1.00 282.60 ?  213 PRO E CB  1 
ATOM   11405 C CG  . PRO E  4 222 ? 63.322  64.460  180.359 1.00 278.64 ?  213 PRO E CG  1 
ATOM   11406 C CD  . PRO E  4 222 ? 63.044  63.046  180.767 1.00 268.74 ?  213 PRO E CD  1 
ATOM   11407 N N   . LYS E  4 223 ? 67.032  62.599  178.180 1.00 287.06 ?  214 LYS E N   1 
ATOM   11408 C CA  . LYS E  4 223 ? 68.394  62.084  178.129 1.00 286.68 ?  214 LYS E CA  1 
ATOM   11409 C C   . LYS E  4 223 ? 69.404  63.118  178.625 1.00 298.12 ?  214 LYS E C   1 
ATOM   11410 O O   . LYS E  4 223 ? 69.209  64.324  178.464 1.00 307.65 ?  214 LYS E O   1 
ATOM   11411 C CB  . LYS E  4 223 ? 68.740  61.647  176.702 1.00 286.29 ?  214 LYS E CB  1 
ATOM   11412 C CG  . LYS E  4 223 ? 70.103  60.994  176.565 1.00 291.18 ?  214 LYS E CG  1 
ATOM   11413 C CD  . LYS E  4 223 ? 70.425  60.668  175.118 1.00 293.14 ?  214 LYS E CD  1 
ATOM   11414 C CE  . LYS E  4 223 ? 71.798  60.032  175.007 1.00 294.79 ?  214 LYS E CE  1 
ATOM   11415 N NZ  . LYS E  4 223 ? 72.205  59.826  173.593 1.00 299.34 1  214 LYS E NZ  1 
ATOM   11416 N N   . ASP F  5 1   ? 39.736  34.469  134.506 1.00 209.11 ?  1   ASP F N   1 
ATOM   11417 C CA  . ASP F  5 1   ? 38.877  35.042  135.536 1.00 204.44 ?  1   ASP F CA  1 
ATOM   11418 C C   . ASP F  5 1   ? 38.252  36.355  135.075 1.00 208.85 ?  1   ASP F C   1 
ATOM   11419 O O   . ASP F  5 1   ? 38.623  36.904  134.037 1.00 215.56 ?  1   ASP F O   1 
ATOM   11420 C CB  . ASP F  5 1   ? 39.663  35.263  136.829 1.00 208.13 ?  1   ASP F CB  1 
ATOM   11421 C CG  . ASP F  5 1   ? 40.479  34.053  137.230 1.00 205.29 ?  1   ASP F CG  1 
ATOM   11422 O OD1 . ASP F  5 1   ? 40.292  32.974  136.630 1.00 198.94 ?  1   ASP F OD1 1 
ATOM   11423 O OD2 . ASP F  5 1   ? 41.311  34.185  138.148 1.00 208.83 -1 1   ASP F OD2 1 
ATOM   11424 N N   . ILE F  5 2   ? 37.291  36.842  135.855 1.00 221.89 ?  2   ILE F N   1 
ATOM   11425 C CA  . ILE F  5 2   ? 36.660  38.139  135.639 1.00 226.21 ?  2   ILE F CA  1 
ATOM   11426 C C   . ILE F  5 2   ? 37.243  39.124  136.645 1.00 233.25 ?  2   ILE F C   1 
ATOM   11427 O O   . ILE F  5 2   ? 37.326  38.819  137.842 1.00 228.57 ?  2   ILE F O   1 
ATOM   11428 C CB  . ILE F  5 2   ? 35.131  38.044  135.781 1.00 215.96 ?  2   ILE F CB  1 
ATOM   11429 C CG1 . ILE F  5 2   ? 34.540  37.180  134.662 1.00 209.55 ?  2   ILE F CG1 1 
ATOM   11430 C CG2 . ILE F  5 2   ? 34.502  39.436  135.770 1.00 220.37 ?  2   ILE F CG2 1 
ATOM   11431 C CD1 . ILE F  5 2   ? 33.074  36.837  134.864 1.00 200.92 ?  2   ILE F CD1 1 
ATOM   11432 N N   . GLN F  5 3   ? 37.655  40.297  136.165 1.00 214.98 ?  3   GLN F N   1 
ATOM   11433 C CA  . GLN F  5 3   ? 38.210  41.341  137.018 1.00 221.30 ?  3   GLN F CA  1 
ATOM   11434 C C   . GLN F  5 3   ? 37.140  42.384  137.324 1.00 219.17 ?  3   GLN F C   1 
ATOM   11435 O O   . GLN F  5 3   ? 36.457  42.865  136.413 1.00 221.02 ?  3   GLN F O   1 
ATOM   11436 C CB  . GLN F  5 3   ? 39.410  42.023  136.352 1.00 234.00 ?  3   GLN F CB  1 
ATOM   11437 C CG  . GLN F  5 3   ? 40.702  41.207  136.294 1.00 238.01 ?  3   GLN F CG  1 
ATOM   11438 C CD  . GLN F  5 3   ? 40.714  40.179  135.175 1.00 236.23 ?  3   GLN F CD  1 
ATOM   11439 O OE1 . GLN F  5 3   ? 40.395  40.489  134.026 1.00 239.02 ?  3   GLN F OE1 1 
ATOM   11440 N NE2 . GLN F  5 3   ? 41.101  38.951  135.503 1.00 231.07 ?  3   GLN F NE2 1 
ATOM   11441 N N   . LEU F  5 4   ? 37.005  42.728  138.605 1.00 224.79 ?  4   LEU F N   1 
ATOM   11442 C CA  . LEU F  5 4   ? 36.133  43.802  139.067 1.00 222.87 ?  4   LEU F CA  1 
ATOM   11443 C C   . LEU F  5 4   ? 36.990  44.997  139.461 1.00 232.15 ?  4   LEU F C   1 
ATOM   11444 O O   . LEU F  5 4   ? 37.889  44.869  140.301 1.00 233.88 ?  4   LEU F O   1 
ATOM   11445 C CB  . LEU F  5 4   ? 35.283  43.349  140.256 1.00 210.49 ?  4   LEU F CB  1 
ATOM   11446 C CG  . LEU F  5 4   ? 34.370  42.136  140.075 1.00 199.11 ?  4   LEU F CG  1 
ATOM   11447 C CD1 . LEU F  5 4   ? 33.631  41.816  141.365 1.00 187.58 ?  4   LEU F CD1 1 
ATOM   11448 C CD2 . LEU F  5 4   ? 33.382  42.395  138.957 1.00 198.94 ?  4   LEU F CD2 1 
ATOM   11449 N N   . THR F  5 5   ? 36.708  46.151  138.863 1.00 225.49 ?  5   THR F N   1 
ATOM   11450 C CA  . THR F  5 5   ? 37.442  47.384  139.123 1.00 234.10 ?  5   THR F CA  1 
ATOM   11451 C C   . THR F  5 5   ? 36.539  48.389  139.825 1.00 230.79 ?  5   THR F C   1 
ATOM   11452 O O   . THR F  5 5   ? 35.500  48.778  139.280 1.00 228.95 ?  5   THR F O   1 
ATOM   11453 C CB  . THR F  5 5   ? 37.975  47.983  137.822 1.00 244.61 ?  5   THR F CB  1 
ATOM   11454 O OG1 . THR F  5 5   ? 38.803  47.025  137.151 1.00 247.53 ?  5   THR F OG1 1 
ATOM   11455 C CG2 . THR F  5 5   ? 38.780  49.236  138.114 1.00 253.42 ?  5   THR F CG2 1 
ATOM   11456 N N   . GLN F  5 6   ? 36.931  48.807  141.026 1.00 238.60 ?  6   GLN F N   1 
ATOM   11457 C CA  . GLN F  5 6   ? 36.162  49.775  141.795 1.00 235.70 ?  6   GLN F CA  1 
ATOM   11458 C C   . GLN F  5 6   ? 36.778  51.161  141.654 1.00 244.74 ?  6   GLN F C   1 
ATOM   11459 O O   . GLN F  5 6   ? 38.003  51.306  141.604 1.00 251.66 ?  6   GLN F O   1 
ATOM   11460 C CB  . GLN F  5 6   ? 36.072  49.380  143.271 1.00 228.01 ?  6   GLN F CB  1 
ATOM   11461 C CG  . GLN F  5 6   ? 35.219  48.143  143.509 1.00 216.92 ?  6   GLN F CG  1 
ATOM   11462 C CD  . GLN F  5 6   ? 35.042  47.810  144.978 1.00 208.39 ?  6   GLN F CD  1 
ATOM   11463 O OE1 . GLN F  5 6   ? 35.469  46.754  145.446 1.00 203.15 ?  6   GLN F OE1 1 
ATOM   11464 N NE2 . GLN F  5 6   ? 34.402  48.712  145.714 1.00 206.78 ?  6   GLN F NE2 1 
ATOM   11465 N N   . SER F  5 7   ? 35.924  52.179  141.593 1.00 239.54 ?  7   SER F N   1 
ATOM   11466 C CA  . SER F  5 7   ? 36.395  53.560  141.532 1.00 246.70 ?  7   SER F CA  1 
ATOM   11467 C C   . SER F  5 7   ? 35.498  54.507  142.324 1.00 242.44 ?  7   SER F C   1 
ATOM   11468 O O   . SER F  5 7   ? 34.278  54.344  142.338 1.00 236.72 ?  7   SER F O   1 
ATOM   11469 C CB  . SER F  5 7   ? 36.484  54.022  140.081 1.00 254.58 ?  7   SER F CB  1 
ATOM   11470 O OG  . SER F  5 7   ? 35.236  53.875  139.430 1.00 250.57 ?  7   SER F OG  1 
ATOM   11471 N N   . PRO F  5 8   ? 36.099  55.509  142.985 1.00 257.55 ?  8   PRO F N   1 
ATOM   11472 C CA  . PRO F  5 8   ? 37.545  55.706  143.144 1.00 263.58 ?  8   PRO F CA  1 
ATOM   11473 C C   . PRO F  5 8   ? 38.140  54.738  144.160 1.00 259.58 ?  8   PRO F C   1 
ATOM   11474 O O   . PRO F  5 8   ? 37.385  54.089  144.884 1.00 251.97 ?  8   PRO F O   1 
ATOM   11475 C CB  . PRO F  5 8   ? 37.641  57.152  143.622 1.00 265.71 ?  8   PRO F CB  1 
ATOM   11476 C CG  . PRO F  5 8   ? 36.399  57.345  144.417 1.00 257.71 ?  8   PRO F CG  1 
ATOM   11477 C CD  . PRO F  5 8   ? 35.331  56.551  143.692 1.00 254.60 ?  8   PRO F CD  1 
ATOM   11478 N N   . SER F  5 9   ? 39.471  54.635  144.216 1.00 264.12 ?  9   SER F N   1 
ATOM   11479 C CA  . SER F  5 9   ? 40.076  53.801  145.249 1.00 261.08 ?  9   SER F CA  1 
ATOM   11480 C C   . SER F  5 9   ? 39.972  54.442  146.624 1.00 255.93 ?  9   SER F C   1 
ATOM   11481 O O   . SER F  5 9   ? 39.856  53.730  147.627 1.00 249.74 ?  9   SER F O   1 
ATOM   11482 C CB  . SER F  5 9   ? 41.539  53.518  144.912 1.00 268.88 ?  9   SER F CB  1 
ATOM   11483 O OG  . SER F  5 9   ? 41.648  52.605  143.835 1.00 272.32 ?  9   SER F OG  1 
ATOM   11484 N N   . PHE F  5 10  ? 40.019  55.770  146.699 1.00 263.33 ?  10  PHE F N   1 
ATOM   11485 C CA  . PHE F  5 10  ? 39.920  56.477  147.971 1.00 257.48 ?  10  PHE F CA  1 
ATOM   11486 C C   . PHE F  5 10  ? 39.007  57.674  147.779 1.00 256.81 ?  10  PHE F C   1 
ATOM   11487 O O   . PHE F  5 10  ? 39.312  58.568  146.985 1.00 263.25 ?  10  PHE F O   1 
ATOM   11488 C CB  . PHE F  5 10  ? 41.295  56.911  148.488 1.00 260.51 ?  10  PHE F CB  1 
ATOM   11489 C CG  . PHE F  5 10  ? 42.234  55.766  148.728 1.00 261.34 ?  10  PHE F CG  1 
ATOM   11490 C CD1 . PHE F  5 10  ? 43.112  55.345  147.743 1.00 270.24 ?  10  PHE F CD1 1 
ATOM   11491 C CD2 . PHE F  5 10  ? 42.224  55.098  149.942 1.00 253.14 ?  10  PHE F CD2 1 
ATOM   11492 C CE1 . PHE F  5 10  ? 43.969  54.283  147.969 1.00 271.73 ?  10  PHE F CE1 1 
ATOM   11493 C CE2 . PHE F  5 10  ? 43.077  54.038  150.175 1.00 253.95 ?  10  PHE F CE2 1 
ATOM   11494 C CZ  . PHE F  5 10  ? 43.951  53.629  149.188 1.00 263.84 ?  10  PHE F CZ  1 
ATOM   11495 N N   . LEU F  5 11  ? 37.893  57.692  148.505 1.00 259.12 ?  11  LEU F N   1 
ATOM   11496 C CA  . LEU F  5 11  ? 36.886  58.733  148.364 1.00 258.19 ?  11  LEU F CA  1 
ATOM   11497 C C   . LEU F  5 11  ? 36.839  59.503  149.672 1.00 252.41 ?  11  LEU F C   1 
ATOM   11498 O O   . LEU F  5 11  ? 36.643  58.911  150.739 1.00 245.07 ?  11  LEU F O   1 
ATOM   11499 C CB  . LEU F  5 11  ? 35.516  58.140  148.019 1.00 254.28 ?  11  LEU F CB  1 
ATOM   11500 C CG  . LEU F  5 11  ? 34.475  59.063  147.377 1.00 255.88 ?  11  LEU F CG  1 
ATOM   11501 C CD1 . LEU F  5 11  ? 33.484  58.256  146.550 1.00 254.72 ?  11  LEU F CD1 1 
ATOM   11502 C CD2 . LEU F  5 11  ? 33.744  59.884  148.428 1.00 252.32 ?  11  LEU F CD2 1 
ATOM   11503 N N   . SER F  5 12  ? 37.021  60.813  149.588 1.00 260.43 ?  12  SER F N   1 
ATOM   11504 C CA  . SER F  5 12  ? 36.914  61.700  150.734 1.00 262.45 ?  12  SER F CA  1 
ATOM   11505 C C   . SER F  5 12  ? 35.563  62.395  150.696 1.00 264.74 ?  12  SER F C   1 
ATOM   11506 O O   . SER F  5 12  ? 35.160  62.922  149.654 1.00 269.55 ?  12  SER F O   1 
ATOM   11507 C CB  . SER F  5 12  ? 38.045  62.729  150.743 1.00 269.70 ?  12  SER F CB  1 
ATOM   11508 O OG  . SER F  5 12  ? 39.304  62.091  150.856 1.00 267.79 ?  12  SER F OG  1 
ATOM   11509 N N   . ALA F  5 13  ? 34.861  62.383  151.822 1.00 265.74 ?  13  ALA F N   1 
ATOM   11510 C CA  . ALA F  5 13  ? 33.555  63.011  151.878 1.00 267.92 ?  13  ALA F CA  1 
ATOM   11511 C C   . ALA F  5 13  ? 33.295  63.472  153.299 1.00 267.51 ?  13  ALA F C   1 
ATOM   11512 O O   . ALA F  5 13  ? 33.957  63.047  154.248 1.00 263.53 ?  13  ALA F O   1 
ATOM   11513 C CB  . ALA F  5 13  ? 32.442  62.063  151.414 1.00 262.39 ?  13  ALA F CB  1 
ATOM   11514 N N   . SER F  5 14  ? 32.308  64.341  153.424 1.00 266.18 ?  14  SER F N   1 
ATOM   11515 C CA  . SER F  5 14  ? 31.878  64.890  154.695 1.00 266.90 ?  14  SER F CA  1 
ATOM   11516 C C   . SER F  5 14  ? 30.630  64.165  155.165 1.00 261.04 ?  14  SER F C   1 
ATOM   11517 O O   . SER F  5 14  ? 29.858  63.639  154.358 1.00 258.47 ?  14  SER F O   1 
ATOM   11518 C CB  . SER F  5 14  ? 31.603  66.389  154.584 1.00 276.00 ?  14  SER F CB  1 
ATOM   11519 O OG  . SER F  5 14  ? 32.771  67.083  154.187 1.00 281.75 ?  14  SER F OG  1 
ATOM   11520 N N   . VAL F  5 15  ? 30.464  64.101  156.485 1.00 248.07 ?  15  VAL F N   1 
ATOM   11521 C CA  . VAL F  5 15  ? 29.202  63.630  157.033 1.00 243.92 ?  15  VAL F CA  1 
ATOM   11522 C C   . VAL F  5 15  ? 28.073  64.403  156.371 1.00 249.09 ?  15  VAL F C   1 
ATOM   11523 O O   . VAL F  5 15  ? 28.104  65.636  156.294 1.00 256.68 ?  15  VAL F O   1 
ATOM   11524 C CB  . VAL F  5 15  ? 29.194  63.798  158.563 1.00 243.18 ?  15  VAL F CB  1 
ATOM   11525 C CG1 . VAL F  5 15  ? 27.807  63.511  159.135 1.00 240.03 ?  15  VAL F CG1 1 
ATOM   11526 C CG2 . VAL F  5 15  ? 30.251  62.905  159.202 1.00 237.79 ?  15  VAL F CG2 1 
ATOM   11527 N N   . GLY F  5 16  ? 27.065  63.673  155.890 1.00 248.32 ?  16  GLY F N   1 
ATOM   11528 C CA  . GLY F  5 16  ? 25.927  64.247  155.209 1.00 252.56 ?  16  GLY F CA  1 
ATOM   11529 C C   . GLY F  5 16  ? 25.968  64.180  153.691 1.00 254.39 ?  16  GLY F C   1 
ATOM   11530 O O   . GLY F  5 16  ? 24.929  64.398  153.056 1.00 256.62 ?  16  GLY F O   1 
ATOM   11531 N N   . ASP F  5 17  ? 27.124  63.901  153.088 1.00 249.20 ?  17  ASP F N   1 
ATOM   11532 C CA  . ASP F  5 17  ? 27.207  63.853  151.632 1.00 251.60 ?  17  ASP F CA  1 
ATOM   11533 C C   . ASP F  5 17  ? 26.480  62.635  151.065 1.00 245.27 ?  17  ASP F C   1 
ATOM   11534 O O   . ASP F  5 17  ? 26.424  61.571  151.686 1.00 237.77 ?  17  ASP F O   1 
ATOM   11535 C CB  . ASP F  5 17  ? 28.668  63.791  151.175 1.00 252.84 ?  17  ASP F CB  1 
ATOM   11536 C CG  . ASP F  5 17  ? 29.381  65.119  151.285 1.00 261.06 ?  17  ASP F CG  1 
ATOM   11537 O OD1 . ASP F  5 17  ? 28.725  66.125  151.621 1.00 266.19 ?  17  ASP F OD1 1 
ATOM   11538 O OD2 . ASP F  5 17  ? 30.602  65.156  151.018 1.00 262.48 -1 17  ASP F OD2 1 
ATOM   11539 N N   . LYS F  5 18  ? 25.915  62.805  149.868 1.00 260.67 ?  18  LYS F N   1 
ATOM   11540 C CA  . LYS F  5 18  ? 25.479  61.682  149.046 1.00 255.60 ?  18  LYS F CA  1 
ATOM   11541 C C   . LYS F  5 18  ? 26.665  61.281  148.177 1.00 255.67 ?  18  LYS F C   1 
ATOM   11542 O O   . LYS F  5 18  ? 27.236  62.126  147.479 1.00 262.52 ?  18  LYS F O   1 
ATOM   11543 C CB  . LYS F  5 18  ? 24.264  62.048  148.189 1.00 259.31 ?  18  LYS F CB  1 
ATOM   11544 C CG  . LYS F  5 18  ? 23.801  60.929  147.256 1.00 254.74 ?  18  LYS F CG  1 
ATOM   11545 C CD  . LYS F  5 18  ? 22.586  61.333  146.423 1.00 258.84 ?  18  LYS F CD  1 
ATOM   11546 C CE  . LYS F  5 18  ? 22.144  60.203  145.496 1.00 254.32 ?  18  LYS F CE  1 
ATOM   11547 N NZ  . LYS F  5 18  ? 20.850  60.493  144.812 1.00 261.10 1  18  LYS F NZ  1 
ATOM   11548 N N   . VAL F  5 19  ? 27.033  60.001  148.205 1.00 252.44 ?  19  VAL F N   1 
ATOM   11549 C CA  . VAL F  5 19  ? 28.139  59.513  147.390 1.00 253.28 ?  19  VAL F CA  1 
ATOM   11550 C C   . VAL F  5 19  ? 27.771  58.215  146.686 1.00 247.50 ?  19  VAL F C   1 
ATOM   11551 O O   . VAL F  5 19  ? 26.952  57.426  147.168 1.00 240.23 ?  19  VAL F O   1 
ATOM   11552 C CB  . VAL F  5 19  ? 29.422  59.314  148.232 1.00 251.95 ?  19  VAL F CB  1 
ATOM   11553 C CG1 . VAL F  5 19  ? 29.908  60.639  148.806 1.00 259.34 ?  19  VAL F CG1 1 
ATOM   11554 C CG2 . VAL F  5 19  ? 29.170  58.319  149.347 1.00 241.17 ?  19  VAL F CG2 1 
ATOM   11555 N N   . THR F  5 20  ? 28.384  58.013  145.519 1.00 245.38 ?  20  THR F N   1 
ATOM   11556 C CA  . THR F  5 20  ? 28.198  56.826  144.697 1.00 240.98 ?  20  THR F CA  1 
ATOM   11557 C C   . THR F  5 20  ? 29.564  56.266  144.326 1.00 241.01 ?  20  THR F C   1 
ATOM   11558 O O   . THR F  5 20  ? 30.429  57.007  143.848 1.00 248.63 ?  20  THR F O   1 
ATOM   11559 C CB  . THR F  5 20  ? 27.401  57.148  143.428 1.00 246.59 ?  20  THR F CB  1 
ATOM   11560 O OG1 . THR F  5 20  ? 26.102  57.636  143.785 1.00 246.17 ?  20  THR F OG1 1 
ATOM   11561 C CG2 . THR F  5 20  ? 27.253  55.910  142.560 1.00 241.99 ?  20  THR F CG2 1 
ATOM   11562 N N   . ILE F  5 21  ? 29.759  54.967  144.548 1.00 236.77 ?  21  ILE F N   1 
ATOM   11563 C CA  . ILE F  5 21  ? 30.992  54.280  144.182 1.00 236.18 ?  21  ILE F CA  1 
ATOM   11564 C C   . ILE F  5 21  ? 30.651  53.265  143.102 1.00 233.83 ?  21  ILE F C   1 
ATOM   11565 O O   . ILE F  5 21  ? 29.517  52.780  143.013 1.00 229.12 ?  21  ILE F O   1 
ATOM   11566 C CB  . ILE F  5 21  ? 31.683  53.595  145.382 1.00 228.51 ?  21  ILE F CB  1 
ATOM   11567 C CG1 . ILE F  5 21  ? 30.802  52.484  145.955 1.00 218.51 ?  21  ILE F CG1 1 
ATOM   11568 C CG2 . ILE F  5 21  ? 32.010  54.608  146.461 1.00 230.60 ?  21  ILE F CG2 1 
ATOM   11569 C CD1 . ILE F  5 21  ? 31.439  51.716  147.093 1.00 211.16 ?  21  ILE F CD1 1 
ATOM   11570 N N   . THR F  5 22  ? 31.641  52.945  142.275 1.00 240.35 ?  22  THR F N   1 
ATOM   11571 C CA  . THR F  5 22  ? 31.418  52.200  141.046 1.00 240.89 ?  22  THR F CA  1 
ATOM   11572 C C   . THR F  5 22  ? 32.203  50.896  141.067 1.00 234.86 ?  22  THR F C   1 
ATOM   11573 O O   . THR F  5 22  ? 33.333  50.850  141.560 1.00 234.35 ?  22  THR F O   1 
ATOM   11574 C CB  . THR F  5 22  ? 31.835  53.046  139.834 1.00 252.49 ?  22  THR F CB  1 
ATOM   11575 O OG1 . THR F  5 22  ? 30.970  54.184  139.728 1.00 259.48 ?  22  THR F OG1 1 
ATOM   11576 C CG2 . THR F  5 22  ? 31.754  52.243  138.550 1.00 254.48 ?  22  THR F CG2 1 
ATOM   11577 N N   . CYS F  5 23  ? 31.588  49.842  140.531 1.00 244.96 ?  23  CYS F N   1 
ATOM   11578 C CA  . CYS F  5 23  ? 32.221  48.541  140.347 1.00 239.47 ?  23  CYS F CA  1 
ATOM   11579 C C   . CYS F  5 23  ? 31.979  48.132  138.899 1.00 241.98 ?  23  CYS F C   1 
ATOM   11580 O O   . CYS F  5 23  ? 30.826  48.052  138.462 1.00 240.28 ?  23  CYS F O   1 
ATOM   11581 C CB  . CYS F  5 23  ? 31.639  47.511  141.330 1.00 228.08 ?  23  CYS F CB  1 
ATOM   11582 S SG  . CYS F  5 23  ? 32.282  45.810  141.217 1.00 220.32 ?  23  CYS F SG  1 
ATOM   11583 N N   . ARG F  5 24  ? 33.053  47.882  138.153 1.00 227.05 ?  24  ARG F N   1 
ATOM   11584 C CA  . ARG F  5 24  ? 32.952  47.442  136.767 1.00 229.33 ?  24  ARG F CA  1 
ATOM   11585 C C   . ARG F  5 24  ? 33.513  46.040  136.602 1.00 222.52 ?  24  ARG F C   1 
ATOM   11586 O O   . ARG F  5 24  ? 34.585  45.723  137.125 1.00 221.33 ?  24  ARG F O   1 
ATOM   11587 C CB  . ARG F  5 24  ? 33.679  48.395  135.818 1.00 240.85 ?  24  ARG F CB  1 
ATOM   11588 C CG  . ARG F  5 24  ? 33.129  49.800  135.828 1.00 248.68 ?  24  ARG F CG  1 
ATOM   11589 C CD  . ARG F  5 24  ? 33.679  50.584  134.662 1.00 258.73 ?  24  ARG F CD  1 
ATOM   11590 N NE  . ARG F  5 24  ? 32.895  50.314  133.462 1.00 262.18 ?  24  ARG F NE  1 
ATOM   11591 C CZ  . ARG F  5 24  ? 32.011  51.156  132.940 1.00 264.10 ?  24  ARG F CZ  1 
ATOM   11592 N NH1 . ARG F  5 24  ? 31.824  52.350  133.486 1.00 269.37 1  24  ARG F NH1 1 
ATOM   11593 N NH2 . ARG F  5 24  ? 31.337  50.817  131.849 1.00 267.23 ?  24  ARG F NH2 1 
ATOM   11594 N N   . ALA F  5 25  ? 32.789  45.208  135.860 1.00 211.30 ?  25  ALA F N   1 
ATOM   11595 C CA  . ALA F  5 25  ? 33.208  43.843  135.585 1.00 210.52 ?  25  ALA F CA  1 
ATOM   11596 C C   . ALA F  5 25  ? 33.775  43.723  134.178 1.00 211.96 ?  25  ALA F C   1 
ATOM   11597 O O   . ALA F  5 25  ? 33.278  44.353  133.240 1.00 213.14 ?  25  ALA F O   1 
ATOM   11598 C CB  . ALA F  5 25  ? 32.034  42.877  135.739 1.00 208.93 ?  25  ALA F CB  1 
ATOM   11599 N N   . SER F  5 26  ? 34.825  42.909  134.045 1.00 218.97 ?  26  SER F N   1 
ATOM   11600 C CA  . SER F  5 26  ? 35.468  42.709  132.752 1.00 224.65 ?  26  SER F CA  1 
ATOM   11601 C C   . SER F  5 26  ? 34.603  41.882  131.809 1.00 222.46 ?  26  SER F C   1 
ATOM   11602 O O   . SER F  5 26  ? 34.810  41.934  130.592 1.00 227.56 ?  26  SER F O   1 
ATOM   11603 C CB  . SER F  5 26  ? 36.834  42.043  132.926 1.00 222.80 ?  26  SER F CB  1 
ATOM   11604 O OG  . SER F  5 26  ? 36.715  40.772  133.538 1.00 212.23 ?  26  SER F OG  1 
ATOM   11605 N N   . GLN F  5 27  ? 33.651  41.116  132.346 1.00 221.86 ?  27  GLN F N   1 
ATOM   11606 C CA  . GLN F  5 27  ? 32.672  40.393  131.545 1.00 218.06 ?  27  GLN F CA  1 
ATOM   11607 C C   . GLN F  5 27  ? 31.301  40.556  132.193 1.00 213.99 ?  27  GLN F C   1 
ATOM   11608 O O   . GLN F  5 27  ? 31.191  40.947  133.357 1.00 211.99 ?  27  GLN F O   1 
ATOM   11609 C CB  . GLN F  5 27  ? 33.037  38.903  131.439 1.00 210.95 ?  27  GLN F CB  1 
ATOM   11610 C CG  . GLN F  5 27  ? 34.233  38.599  130.540 1.00 216.66 ?  27  GLN F CG  1 
ATOM   11611 C CD  . GLN F  5 27  ? 33.918  38.730  129.064 1.00 223.34 ?  27  GLN F CD  1 
ATOM   11612 O OE1 . GLN F  5 27  ? 32.762  38.882  128.674 1.00 222.98 ?  27  GLN F OE1 1 
ATOM   11613 N NE2 . GLN F  5 27  ? 34.953  38.676  128.232 1.00 231.43 ?  27  GLN F NE2 1 
ATOM   11614 N N   . GLY F  5 28  ? 30.251  40.255  131.432 1.00 202.27 ?  28  GLY F N   1 
ATOM   11615 C CA  . GLY F  5 28  ? 28.900  40.368  131.968 1.00 201.25 ?  28  GLY F CA  1 
ATOM   11616 C C   . GLY F  5 28  ? 28.651  39.357  133.074 1.00 199.25 ?  28  GLY F C   1 
ATOM   11617 O O   . GLY F  5 28  ? 28.843  38.150  132.886 1.00 198.52 ?  28  GLY F O   1 
ATOM   11618 N N   . VAL F  5 29  ? 28.220  39.844  134.238 1.00 214.12 ?  29  VAL F N   1 
ATOM   11619 C CA  . VAL F  5 29  ? 27.849  38.984  135.356 1.00 204.30 ?  29  VAL F CA  1 
ATOM   11620 C C   . VAL F  5 29  ? 26.351  39.021  135.660 1.00 200.87 ?  29  VAL F C   1 
ATOM   11621 O O   . VAL F  5 29  ? 25.936  38.555  136.726 1.00 193.99 ?  29  VAL F O   1 
ATOM   11622 C CB  . VAL F  5 29  ? 28.674  39.315  136.610 1.00 203.52 ?  29  VAL F CB  1 
ATOM   11623 C CG1 . VAL F  5 29  ? 30.157  39.117  136.335 1.00 206.23 ?  29  VAL F CG1 1 
ATOM   11624 C CG2 . VAL F  5 29  ? 28.411  40.733  137.045 1.00 210.02 ?  29  VAL F CG2 1 
ATOM   11625 N N   . ARG F  5 30  ? 25.531  39.564  134.759 1.00 220.04 ?  30  ARG F N   1 
ATOM   11626 C CA  . ARG F  5 30  ? 24.068  39.690  134.944 1.00 217.40 ?  30  ARG F CA  1 
ATOM   11627 C C   . ARG F  5 30  ? 23.791  40.504  136.210 1.00 217.03 ?  30  ARG F C   1 
ATOM   11628 O O   . ARG F  5 30  ? 24.406  41.567  136.389 1.00 223.78 ?  30  ARG F O   1 
ATOM   11629 C CB  . ARG F  5 30  ? 23.457  38.296  134.911 1.00 210.60 ?  30  ARG F CB  1 
ATOM   11630 C CG  . ARG F  5 30  ? 23.691  37.550  133.611 1.00 213.17 ?  30  ARG F CG  1 
ATOM   11631 C CD  . ARG F  5 30  ? 23.148  36.143  133.713 1.00 206.97 ?  30  ARG F CD  1 
ATOM   11632 N NE  . ARG F  5 30  ? 24.010  35.318  134.555 1.00 201.88 ?  30  ARG F NE  1 
ATOM   11633 C CZ  . ARG F  5 30  ? 25.083  34.678  134.108 1.00 203.43 ?  30  ARG F CZ  1 
ATOM   11634 N NH1 . ARG F  5 30  ? 25.423  34.785  132.831 1.00 212.45 1  30  ARG F NH1 1 
ATOM   11635 N NH2 . ARG F  5 30  ? 25.822  33.946  134.931 1.00 198.56 ?  30  ARG F NH2 1 
ATOM   11636 N N   . ASN F  5 31  ? 22.887  40.066  137.095 1.00 219.63 ?  31  ASN F N   1 
ATOM   11637 C CA  . ASN F  5 31  ? 22.641  40.721  138.376 1.00 218.70 ?  31  ASN F CA  1 
ATOM   11638 C C   . ASN F  5 31  ? 23.312  40.014  139.551 1.00 211.83 ?  31  ASN F C   1 
ATOM   11639 O O   . ASN F  5 31  ? 22.957  40.274  140.706 1.00 209.20 ?  31  ASN F O   1 
ATOM   11640 C CB  . ASN F  5 31  ? 21.137  40.829  138.647 1.00 216.19 ?  31  ASN F CB  1 
ATOM   11641 C CG  . ASN F  5 31  ? 20.481  39.474  138.873 1.00 207.58 ?  31  ASN F CG  1 
ATOM   11642 O OD1 . ASN F  5 31  ? 21.016  38.437  138.480 1.00 205.38 ?  31  ASN F OD1 1 
ATOM   11643 N ND2 . ASN F  5 31  ? 19.335  39.477  139.545 1.00 206.88 ?  31  ASN F ND2 1 
ATOM   11644 N N   . GLU F  5 32  ? 24.264  39.119  139.291 1.00 209.67 ?  32  GLU F N   1 
ATOM   11645 C CA  . GLU F  5 32  ? 24.743  38.201  140.330 1.00 202.81 ?  32  GLU F CA  1 
ATOM   11646 C C   . GLU F  5 32  ? 25.964  38.823  141.002 1.00 205.62 ?  32  GLU F C   1 
ATOM   11647 O O   . GLU F  5 32  ? 27.117  38.482  140.738 1.00 205.89 ?  32  GLU F O   1 
ATOM   11648 C CB  . GLU F  5 32  ? 25.034  36.832  139.728 1.00 200.22 ?  32  GLU F CB  1 
ATOM   11649 C CG  . GLU F  5 32  ? 23.790  36.174  139.134 1.00 198.43 ?  32  GLU F CG  1 
ATOM   11650 C CD  . GLU F  5 32  ? 24.102  34.979  138.256 1.00 197.90 ?  32  GLU F CD  1 
ATOM   11651 O OE1 . GLU F  5 32  ? 23.150  34.293  137.830 1.00 197.98 ?  32  GLU F OE1 1 
ATOM   11652 O OE2 . GLU F  5 32  ? 25.296  34.720  138.001 1.00 199.97 -1 32  GLU F OE2 1 
ATOM   11653 N N   . LEU F  5 33  ? 25.682  39.773  141.892 1.00 188.53 ?  33  LEU F N   1 
ATOM   11654 C CA  . LEU F  5 33  ? 26.697  40.668  142.422 1.00 193.57 ?  33  LEU F CA  1 
ATOM   11655 C C   . LEU F  5 33  ? 26.266  41.105  143.819 1.00 191.21 ?  33  LEU F C   1 
ATOM   11656 O O   . LEU F  5 33  ? 25.081  41.399  144.057 1.00 190.56 ?  33  LEU F O   1 
ATOM   11657 C CB  . LEU F  5 33  ? 26.898  41.905  141.556 1.00 203.87 ?  33  LEU F CB  1 
ATOM   11658 C CG  . LEU F  5 33  ? 28.078  42.779  141.987 1.00 209.98 ?  33  LEU F CG  1 
ATOM   11659 C CD1 . LEU F  5 33  ? 29.283  42.602  141.089 1.00 216.19 ?  33  LEU F CD1 1 
ATOM   11660 C CD2 . LEU F  5 33  ? 27.661  44.179  142.030 1.00 215.91 ?  33  LEU F CD2 1 
ATOM   11661 N N   . ALA F  5 34  ? 27.223  41.134  144.747 1.00 186.08 ?  34  ALA F N   1 
ATOM   11662 C CA  . ALA F  5 34  ? 26.983  41.534  146.126 1.00 183.95 ?  34  ALA F CA  1 
ATOM   11663 C C   . ALA F  5 34  ? 27.930  42.655  146.530 1.00 190.60 ?  34  ALA F C   1 
ATOM   11664 O O   . ALA F  5 34  ? 29.017  42.808  145.961 1.00 194.97 ?  34  ALA F O   1 
ATOM   11665 C CB  . ALA F  5 34  ? 27.163  40.346  147.078 1.00 174.92 ?  34  ALA F CB  1 
ATOM   11666 N N   . TRP F  5 35  ? 27.503  43.439  147.516 1.00 176.56 ?  35  TRP F N   1 
ATOM   11667 C CA  . TRP F  5 35  ? 28.328  44.467  148.132 1.00 178.53 ?  35  TRP F CA  1 
ATOM   11668 C C   . TRP F  5 35  ? 28.504  44.168  149.615 1.00 176.70 ?  35  TRP F C   1 
ATOM   11669 O O   . TRP F  5 35  ? 27.583  43.682  150.278 1.00 175.67 ?  35  TRP F O   1 
ATOM   11670 C CB  . TRP F  5 35  ? 27.710  45.863  147.957 1.00 186.00 ?  35  TRP F CB  1 
ATOM   11671 C CG  . TRP F  5 35  ? 27.687  46.383  146.544 1.00 193.42 ?  35  TRP F CG  1 
ATOM   11672 C CD1 . TRP F  5 35  ? 26.706  46.198  145.611 1.00 193.87 ?  35  TRP F CD1 1 
ATOM   11673 C CD2 . TRP F  5 35  ? 28.672  47.221  145.930 1.00 201.85 ?  35  TRP F CD2 1 
ATOM   11674 N NE1 . TRP F  5 35  ? 27.036  46.849  144.445 1.00 202.05 ?  35  TRP F NE1 1 
ATOM   11675 C CE2 . TRP F  5 35  ? 28.237  47.486  144.617 1.00 207.16 ?  35  TRP F CE2 1 
ATOM   11676 C CE3 . TRP F  5 35  ? 29.886  47.763  146.361 1.00 205.49 ?  35  TRP F CE3 1 
ATOM   11677 C CZ2 . TRP F  5 35  ? 28.975  48.271  143.734 1.00 216.18 ?  35  TRP F CZ2 1 
ATOM   11678 C CZ3 . TRP F  5 35  ? 30.615  48.540  145.484 1.00 214.25 ?  35  TRP F CZ3 1 
ATOM   11679 C CH2 . TRP F  5 35  ? 30.158  48.788  144.187 1.00 219.67 ?  35  TRP F CH2 1 
ATOM   11680 N N   . TYR F  5 36  ? 29.696  44.473  150.124 1.00 193.57 ?  36  TYR F N   1 
ATOM   11681 C CA  . TYR F  5 36  ? 30.062  44.268  151.517 1.00 189.27 ?  36  TYR F CA  1 
ATOM   11682 C C   . TYR F  5 36  ? 30.671  45.528  152.109 1.00 195.25 ?  36  TYR F C   1 
ATOM   11683 O O   . TYR F  5 36  ? 31.234  46.366  151.399 1.00 202.57 ?  36  TYR F O   1 
ATOM   11684 C CB  . TYR F  5 36  ? 31.045  43.099  151.689 1.00 183.99 ?  36  TYR F CB  1 
ATOM   11685 C CG  . TYR F  5 36  ? 30.545  41.783  151.148 1.00 177.45 ?  36  TYR F CG  1 
ATOM   11686 C CD1 . TYR F  5 36  ? 30.691  41.453  149.809 1.00 179.54 ?  36  TYR F CD1 1 
ATOM   11687 C CD2 . TYR F  5 36  ? 29.947  40.857  151.992 1.00 169.21 ?  36  TYR F CD2 1 
ATOM   11688 C CE1 . TYR F  5 36  ? 30.235  40.245  149.321 1.00 173.39 ?  36  TYR F CE1 1 
ATOM   11689 C CE2 . TYR F  5 36  ? 29.493  39.649  151.517 1.00 163.08 ?  36  TYR F CE2 1 
ATOM   11690 C CZ  . TYR F  5 36  ? 29.638  39.345  150.182 1.00 165.09 ?  36  TYR F CZ  1 
ATOM   11691 O OH  . TYR F  5 36  ? 29.181  38.138  149.708 1.00 158.98 ?  36  TYR F OH  1 
ATOM   11692 N N   . GLN F  5 37  ? 30.534  45.644  153.425 1.00 195.30 ?  37  GLN F N   1 
ATOM   11693 C CA  . GLN F  5 37  ? 31.220  46.641  154.232 1.00 199.41 ?  37  GLN F CA  1 
ATOM   11694 C C   . GLN F  5 37  ? 32.253  45.930  155.092 1.00 194.85 ?  37  GLN F C   1 
ATOM   11695 O O   . GLN F  5 37  ? 31.966  44.877  155.670 1.00 187.52 ?  37  GLN F O   1 
ATOM   11696 C CB  . GLN F  5 37  ? 30.220  47.380  155.127 1.00 199.81 ?  37  GLN F CB  1 
ATOM   11697 C CG  . GLN F  5 37  ? 30.785  48.513  155.956 1.00 203.91 ?  37  GLN F CG  1 
ATOM   11698 C CD  . GLN F  5 37  ? 29.800  48.984  157.008 1.00 202.43 ?  37  GLN F CD  1 
ATOM   11699 O OE1 . GLN F  5 37  ? 29.563  48.305  158.010 1.00 196.04 ?  37  GLN F OE1 1 
ATOM   11700 N NE2 . GLN F  5 37  ? 29.207  50.146  156.776 1.00 208.52 ?  37  GLN F NE2 1 
ATOM   11701 N N   . GLN F  5 38  ? 33.452  46.504  155.182 1.00 196.34 ?  38  GLN F N   1 
ATOM   11702 C CA  . GLN F  5 38  ? 34.478  46.001  156.084 1.00 194.23 ?  38  GLN F CA  1 
ATOM   11703 C C   . GLN F  5 38  ? 35.120  47.157  156.830 1.00 198.54 ?  38  GLN F C   1 
ATOM   11704 O O   . GLN F  5 38  ? 35.460  48.182  156.229 1.00 206.12 ?  38  GLN F O   1 
ATOM   11705 C CB  . GLN F  5 38  ? 35.562  45.218  155.332 1.00 193.61 ?  38  GLN F CB  1 
ATOM   11706 C CG  . GLN F  5 38  ? 36.557  44.537  156.263 1.00 188.94 ?  38  GLN F CG  1 
ATOM   11707 C CD  . GLN F  5 38  ? 37.616  43.736  155.532 1.00 188.35 ?  38  GLN F CD  1 
ATOM   11708 O OE1 . GLN F  5 38  ? 38.107  44.141  154.480 1.00 194.08 ?  38  GLN F OE1 1 
ATOM   11709 N NE2 . GLN F  5 38  ? 37.971  42.585  156.091 1.00 182.22 ?  38  GLN F NE2 1 
ATOM   11710 N N   . LYS F  5 39  ? 35.290  46.981  158.127 1.00 197.75 ?  39  LYS F N   1 
ATOM   11711 C CA  . LYS F  5 39  ? 35.953  47.942  158.975 1.00 200.62 ?  39  LYS F CA  1 
ATOM   11712 C C   . LYS F  5 39  ? 37.267  47.351  159.472 1.00 196.19 ?  39  LYS F C   1 
ATOM   11713 O O   . LYS F  5 39  ? 37.408  46.125  159.521 1.00 189.94 ?  39  LYS F O   1 
ATOM   11714 C CB  . LYS F  5 39  ? 35.042  48.276  160.160 1.00 200.61 ?  39  LYS F CB  1 
ATOM   11715 C CG  . LYS F  5 39  ? 33.794  49.048  159.749 1.00 207.59 ?  39  LYS F CG  1 
ATOM   11716 C CD  . LYS F  5 39  ? 32.883  49.346  160.927 1.00 211.67 ?  39  LYS F CD  1 
ATOM   11717 C CE  . LYS F  5 39  ? 31.665  50.139  160.479 1.00 224.52 ?  39  LYS F CE  1 
ATOM   11718 N NZ  . LYS F  5 39  ? 30.750  50.450  161.611 1.00 230.21 1  39  LYS F NZ  1 
ATOM   11719 N N   . PRO F  5 40  ? 38.258  48.175  159.811 1.00 211.76 ?  40  PRO F N   1 
ATOM   11720 C CA  . PRO F  5 40  ? 39.554  47.621  160.224 1.00 208.81 ?  40  PRO F CA  1 
ATOM   11721 C C   . PRO F  5 40  ? 39.392  46.646  161.383 1.00 201.99 ?  40  PRO F C   1 
ATOM   11722 O O   . PRO F  5 40  ? 38.737  46.948  162.384 1.00 203.44 ?  40  PRO F O   1 
ATOM   11723 C CB  . PRO F  5 40  ? 40.352  48.865  160.626 1.00 215.58 ?  40  PRO F CB  1 
ATOM   11724 C CG  . PRO F  5 40  ? 39.798  49.925  159.741 1.00 223.40 ?  40  PRO F CG  1 
ATOM   11725 C CD  . PRO F  5 40  ? 38.318  49.641  159.668 1.00 221.81 ?  40  PRO F CD  1 
ATOM   11726 N N   . GLY F  5 41  ? 39.999  45.470  161.245 1.00 211.68 ?  41  GLY F N   1 
ATOM   11727 C CA  . GLY F  5 41  ? 39.967  44.488  162.307 1.00 207.84 ?  41  GLY F CA  1 
ATOM   11728 C C   . GLY F  5 41  ? 38.719  43.634  162.387 1.00 202.22 ?  41  GLY F C   1 
ATOM   11729 O O   . GLY F  5 41  ? 38.630  42.792  163.291 1.00 200.84 ?  41  GLY F O   1 
ATOM   11730 N N   . LYS F  5 42  ? 37.754  43.817  161.487 1.00 198.36 ?  42  LYS F N   1 
ATOM   11731 C CA  . LYS F  5 42  ? 36.489  43.096  161.526 1.00 194.71 ?  42  LYS F CA  1 
ATOM   11732 C C   . LYS F  5 42  ? 36.263  42.330  160.229 1.00 192.90 ?  42  LYS F C   1 
ATOM   11733 O O   . LYS F  5 42  ? 36.827  42.654  159.180 1.00 195.61 ?  42  LYS F O   1 
ATOM   11734 C CB  . LYS F  5 42  ? 35.306  44.047  161.765 1.00 199.27 ?  42  LYS F CB  1 
ATOM   11735 C CG  . LYS F  5 42  ? 35.413  44.884  163.026 1.00 205.08 ?  42  LYS F CG  1 
ATOM   11736 C CD  . LYS F  5 42  ? 35.512  43.997  164.255 1.00 202.41 ?  42  LYS F CD  1 
ATOM   11737 C CE  . LYS F  5 42  ? 35.328  44.799  165.530 1.00 210.44 ?  42  LYS F CE  1 
ATOM   11738 N NZ  . LYS F  5 42  ? 35.271  43.917  166.727 1.00 209.83 1  42  LYS F NZ  1 
ATOM   11739 N N   . ALA F  5 43  ? 35.432  41.295  160.322 1.00 189.27 ?  43  ALA F N   1 
ATOM   11740 C CA  . ALA F  5 43  ? 34.993  40.590  159.134 1.00 188.48 ?  43  ALA F CA  1 
ATOM   11741 C C   . ALA F  5 43  ? 34.047  41.474  158.323 1.00 194.44 ?  43  ALA F C   1 
ATOM   11742 O O   . ALA F  5 43  ? 33.386  42.360  158.873 1.00 197.41 ?  43  ALA F O   1 
ATOM   11743 C CB  . ALA F  5 43  ? 34.298  39.285  159.512 1.00 182.37 ?  43  ALA F CB  1 
ATOM   11744 N N   . PRO F  5 44  ? 33.968  41.256  157.012 1.00 182.46 ?  44  PRO F N   1 
ATOM   11745 C CA  . PRO F  5 44  ? 32.976  41.972  156.203 1.00 188.16 ?  44  PRO F CA  1 
ATOM   11746 C C   . PRO F  5 44  ? 31.545  41.684  156.639 1.00 186.73 ?  44  PRO F C   1 
ATOM   11747 O O   . PRO F  5 44  ? 31.234  40.648  157.233 1.00 180.91 ?  44  PRO F O   1 
ATOM   11748 C CB  . PRO F  5 44  ? 33.247  41.465  154.780 1.00 189.51 ?  44  PRO F CB  1 
ATOM   11749 C CG  . PRO F  5 44  ? 34.666  40.966  154.826 1.00 186.66 ?  44  PRO F CG  1 
ATOM   11750 C CD  . PRO F  5 44  ? 34.828  40.389  156.190 1.00 180.42 ?  44  PRO F CD  1 
ATOM   11751 N N   . ASN F  5 45  ? 30.666  42.634  156.324 1.00 180.21 ?  45  ASN F N   1 
ATOM   11752 C CA  . ASN F  5 45  ? 29.228  42.503  156.516 1.00 184.67 ?  45  ASN F CA  1 
ATOM   11753 C C   . ASN F  5 45  ? 28.545  42.662  155.164 1.00 193.14 ?  45  ASN F C   1 
ATOM   11754 O O   . ASN F  5 45  ? 28.888  43.562  154.392 1.00 200.44 ?  45  ASN F O   1 
ATOM   11755 C CB  . ASN F  5 45  ? 28.715  43.550  157.509 1.00 191.23 ?  45  ASN F CB  1 
ATOM   11756 C CG  . ASN F  5 45  ? 28.806  43.077  158.945 1.00 183.01 ?  45  ASN F CG  1 
ATOM   11757 O OD1 . ASN F  5 45  ? 29.338  42.001  159.219 1.00 172.43 ?  45  ASN F OD1 1 
ATOM   11758 N ND2 . ASN F  5 45  ? 28.296  43.880  159.872 1.00 188.09 ?  45  ASN F ND2 1 
ATOM   11759 N N   . LEU F  5 46  ? 27.579  41.788  154.877 1.00 165.21 ?  46  LEU F N   1 
ATOM   11760 C CA  . LEU F  5 46  ? 26.839  41.864  153.620 1.00 168.26 ?  46  LEU F CA  1 
ATOM   11761 C C   . LEU F  5 46  ? 25.850  43.025  153.586 1.00 177.17 ?  46  LEU F C   1 
ATOM   11762 O O   . LEU F  5 46  ? 25.016  43.174  154.484 1.00 177.39 ?  46  LEU F O   1 
ATOM   11763 C CB  . LEU F  5 46  ? 26.094  40.551  153.383 1.00 168.06 ?  46  LEU F CB  1 
ATOM   11764 C CG  . LEU F  5 46  ? 25.251  40.431  152.111 1.00 171.31 ?  46  LEU F CG  1 
ATOM   11765 C CD1 . LEU F  5 46  ? 26.128  40.459  150.870 1.00 171.64 ?  46  LEU F CD1 1 
ATOM   11766 C CD2 . LEU F  5 46  ? 24.415  39.162  152.152 1.00 171.14 ?  46  LEU F CD2 1 
ATOM   11767 N N   . LEU F  5 47  ? 25.940  43.841  152.532 1.00 168.95 ?  47  LEU F N   1 
ATOM   11768 C CA  . LEU F  5 47  ? 25.043  44.970  152.298 1.00 180.66 ?  47  LEU F CA  1 
ATOM   11769 C C   . LEU F  5 47  ? 23.983  44.685  151.237 1.00 186.01 ?  47  LEU F C   1 
ATOM   11770 O O   . LEU F  5 47  ? 22.790  44.896  151.477 1.00 187.83 ?  47  LEU F O   1 
ATOM   11771 C CB  . LEU F  5 47  ? 25.839  46.218  151.895 1.00 188.44 ?  47  LEU F CB  1 
ATOM   11772 C CG  . LEU F  5 47  ? 26.888  46.761  152.861 1.00 184.89 ?  47  LEU F CG  1 
ATOM   11773 C CD1 . LEU F  5 47  ? 27.649  47.905  152.215 1.00 193.07 ?  47  LEU F CD1 1 
ATOM   11774 C CD2 . LEU F  5 47  ? 26.220  47.216  154.145 1.00 184.70 ?  47  LEU F CD2 1 
ATOM   11775 N N   . ILE F  5 48  ? 24.409  44.226  150.057 1.00 177.56 ?  48  ILE F N   1 
ATOM   11776 C CA  . ILE F  5 48  ? 23.575  44.144  148.859 1.00 184.69 ?  48  ILE F CA  1 
ATOM   11777 C C   . ILE F  5 48  ? 23.807  42.796  148.191 1.00 177.96 ?  48  ILE F C   1 
ATOM   11778 O O   . ILE F  5 48  ? 24.937  42.304  148.155 1.00 170.19 ?  48  ILE F O   1 
ATOM   11779 C CB  . ILE F  5 48  ? 23.896  45.283  147.864 1.00 196.00 ?  48  ILE F CB  1 
ATOM   11780 C CG1 . ILE F  5 48  ? 23.623  46.649  148.491 1.00 202.63 ?  48  ILE F CG1 1 
ATOM   11781 C CG2 . ILE F  5 48  ? 23.107  45.123  146.561 1.00 203.24 ?  48  ILE F CG2 1 
ATOM   11782 C CD1 . ILE F  5 48  ? 22.165  47.002  148.569 1.00 205.04 ?  48  ILE F CD1 1 
ATOM   11783 N N   . TYR F  5 49  ? 22.734  42.175  147.701 1.00 183.47 ?  49  TYR F N   1 
ATOM   11784 C CA  . TYR F  5 49  ? 22.852  40.997  146.852 1.00 179.32 ?  49  TYR F CA  1 
ATOM   11785 C C   . TYR F  5 49  ? 21.883  41.157  145.688 1.00 189.11 ?  49  TYR F C   1 
ATOM   11786 O O   . TYR F  5 49  ? 21.014  42.034  145.694 1.00 197.21 ?  49  TYR F O   1 
ATOM   11787 C CB  . TYR F  5 49  ? 22.596  39.686  147.606 1.00 173.84 ?  49  TYR F CB  1 
ATOM   11788 C CG  . TYR F  5 49  ? 21.243  39.575  148.263 1.00 175.38 ?  49  TYR F CG  1 
ATOM   11789 C CD1 . TYR F  5 49  ? 20.174  39.007  147.583 1.00 178.33 ?  49  TYR F CD1 1 
ATOM   11790 C CD2 . TYR F  5 49  ? 21.034  40.012  149.563 1.00 174.07 ?  49  TYR F CD2 1 
ATOM   11791 C CE1 . TYR F  5 49  ? 18.929  38.888  148.170 1.00 179.95 ?  49  TYR F CE1 1 
ATOM   11792 C CE2 . TYR F  5 49  ? 19.787  39.898  150.163 1.00 175.68 ?  49  TYR F CE2 1 
ATOM   11793 C CZ  . TYR F  5 49  ? 18.739  39.333  149.459 1.00 178.61 ?  49  TYR F CZ  1 
ATOM   11794 O OH  . TYR F  5 49  ? 17.495  39.212  150.040 1.00 180.43 ?  49  TYR F OH  1 
ATOM   11795 N N   . TYR F  5 50  ? 22.047  40.300  144.677 1.00 177.81 ?  50  TYR F N   1 
ATOM   11796 C CA  . TYR F  5 50  ? 21.309  40.412  143.415 1.00 183.61 ?  50  TYR F CA  1 
ATOM   11797 C C   . TYR F  5 50  ? 21.465  41.812  142.830 1.00 194.91 ?  50  TYR F C   1 
ATOM   11798 O O   . TYR F  5 50  ? 20.563  42.334  142.168 1.00 204.94 ?  50  TYR F O   1 
ATOM   11799 C CB  . TYR F  5 50  ? 19.826  40.058  143.576 1.00 185.72 ?  50  TYR F CB  1 
ATOM   11800 C CG  . TYR F  5 50  ? 19.535  38.601  143.885 1.00 182.96 ?  50  TYR F CG  1 
ATOM   11801 C CD1 . TYR F  5 50  ? 20.320  37.581  143.358 1.00 180.95 ?  50  TYR F CD1 1 
ATOM   11802 C CD2 . TYR F  5 50  ? 18.449  38.246  144.676 1.00 183.33 ?  50  TYR F CD2 1 
ATOM   11803 C CE1 . TYR F  5 50  ? 20.045  36.250  143.637 1.00 179.23 ?  50  TYR F CE1 1 
ATOM   11804 C CE2 . TYR F  5 50  ? 18.165  36.921  144.956 1.00 181.72 ?  50  TYR F CE2 1 
ATOM   11805 C CZ  . TYR F  5 50  ? 18.966  35.928  144.435 1.00 179.64 ?  50  TYR F CZ  1 
ATOM   11806 O OH  . TYR F  5 50  ? 18.682  34.610  144.710 1.00 178.13 ?  50  TYR F OH  1 
ATOM   11807 N N   . ALA F  5 51  ? 22.622  42.419  143.097 1.00 188.99 ?  51  ALA F N   1 
ATOM   11808 C CA  . ALA F  5 51  ? 23.018  43.743  142.630 1.00 191.29 ?  51  ALA F CA  1 
ATOM   11809 C C   . ALA F  5 51  ? 22.183  44.897  143.179 1.00 193.57 ?  51  ALA F C   1 
ATOM   11810 O O   . ALA F  5 51  ? 22.704  46.007  143.313 1.00 193.94 ?  51  ALA F O   1 
ATOM   11811 C CB  . ALA F  5 51  ? 22.996  43.791  141.098 1.00 195.19 ?  51  ALA F CB  1 
ATOM   11812 N N   . SER F  5 52  ? 20.900  44.685  143.492 1.00 196.33 ?  52  SER F N   1 
ATOM   11813 C CA  . SER F  5 52  ? 20.105  45.777  144.043 1.00 201.20 ?  52  SER F CA  1 
ATOM   11814 C C   . SER F  5 52  ? 19.328  45.489  145.326 1.00 192.21 ?  52  SER F C   1 
ATOM   11815 O O   . SER F  5 52  ? 18.675  46.405  145.835 1.00 194.02 ?  52  SER F O   1 
ATOM   11816 C CB  . SER F  5 52  ? 19.116  46.283  142.983 1.00 212.06 ?  52  SER F CB  1 
ATOM   11817 O OG  . SER F  5 52  ? 18.324  45.219  142.487 1.00 209.89 ?  52  SER F OG  1 
ATOM   11818 N N   . THR F  5 53  ? 19.357  44.270  145.858 1.00 188.28 ?  53  THR F N   1 
ATOM   11819 C CA  . THR F  5 53  ? 18.501  43.917  146.988 1.00 187.38 ?  53  THR F CA  1 
ATOM   11820 C C   . THR F  5 53  ? 19.224  44.134  148.315 1.00 183.38 ?  53  THR F C   1 
ATOM   11821 O O   . THR F  5 53  ? 20.341  43.643  148.505 1.00 179.77 ?  53  THR F O   1 
ATOM   11822 C CB  . THR F  5 53  ? 18.018  42.472  146.873 1.00 186.67 ?  53  THR F CB  1 
ATOM   11823 O OG1 . THR F  5 53  ? 17.266  42.320  145.662 1.00 190.83 ?  53  THR F OG1 1 
ATOM   11824 C CG2 . THR F  5 53  ? 17.122  42.121  148.054 1.00 185.99 ?  53  THR F CG2 1 
ATOM   11825 N N   . LEU F  5 54  ? 18.582  44.869  149.226 1.00 200.42 ?  54  LEU F N   1 
ATOM   11826 C CA  . LEU F  5 54  ? 19.156  45.132  150.544 1.00 193.92 ?  54  LEU F CA  1 
ATOM   11827 C C   . LEU F  5 54  ? 19.122  43.896  151.436 1.00 182.70 ?  54  LEU F C   1 
ATOM   11828 O O   . LEU F  5 54  ? 18.072  43.268  151.608 1.00 178.61 ?  54  LEU F O   1 
ATOM   11829 C CB  . LEU F  5 54  ? 18.411  46.272  151.240 1.00 195.44 ?  54  LEU F CB  1 
ATOM   11830 C CG  . LEU F  5 54  ? 18.891  47.705  151.019 1.00 203.74 ?  54  LEU F CG  1 
ATOM   11831 C CD1 . LEU F  5 54  ? 20.286  47.874  151.610 1.00 201.49 ?  54  LEU F CD1 1 
ATOM   11832 C CD2 . LEU F  5 54  ? 18.880  48.079  149.546 1.00 214.20 ?  54  LEU F CD2 1 
ATOM   11833 N N   . GLN F  5 55  ? 20.276  43.556  152.011 1.00 196.30 ?  55  GLN F N   1 
ATOM   11834 C CA  . GLN F  5 55  ? 20.345  42.513  153.028 1.00 185.71 ?  55  GLN F CA  1 
ATOM   11835 C C   . GLN F  5 55  ? 19.568  42.928  154.277 1.00 181.35 ?  55  GLN F C   1 
ATOM   11836 O O   . GLN F  5 55  ? 19.515  44.107  154.639 1.00 185.23 ?  55  GLN F O   1 
ATOM   11837 C CB  . GLN F  5 55  ? 21.810  42.220  153.377 1.00 182.11 ?  55  GLN F CB  1 
ATOM   11838 C CG  . GLN F  5 55  ? 22.042  41.289  154.568 1.00 171.27 ?  55  GLN F CG  1 
ATOM   11839 C CD  . GLN F  5 55  ? 21.513  39.877  154.351 1.00 165.18 ?  55  GLN F CD  1 
ATOM   11840 O OE1 . GLN F  5 55  ? 21.098  39.512  153.251 1.00 168.76 ?  55  GLN F OE1 1 
ATOM   11841 N NE2 . GLN F  5 55  ? 21.531  39.074  155.410 1.00 156.20 ?  55  GLN F NE2 1 
ATOM   11842 N N   . SER F  5 56  ? 18.944  41.941  154.923 1.00 188.65 ?  56  SER F N   1 
ATOM   11843 C CA  . SER F  5 56  ? 18.180  42.173  156.146 1.00 183.97 ?  56  SER F CA  1 
ATOM   11844 C C   . SER F  5 56  ? 18.987  42.939  157.187 1.00 182.52 ?  56  SER F C   1 
ATOM   11845 O O   . SER F  5 56  ? 20.116  42.564  157.518 1.00 179.88 ?  56  SER F O   1 
ATOM   11846 C CB  . SER F  5 56  ? 17.711  40.838  156.729 1.00 175.27 ?  56  SER F CB  1 
ATOM   11847 O OG  . SER F  5 56  ? 16.877  41.039  157.859 1.00 176.01 ?  56  SER F OG  1 
ATOM   11848 N N   . GLY F  5 57  ? 18.393  44.011  157.714 1.00 190.14 ?  57  GLY F N   1 
ATOM   11849 C CA  . GLY F  5 57  ? 19.014  44.806  158.750 1.00 190.69 ?  57  GLY F CA  1 
ATOM   11850 C C   . GLY F  5 57  ? 19.909  45.927  158.269 1.00 195.93 ?  57  GLY F C   1 
ATOM   11851 O O   . GLY F  5 57  ? 20.318  46.764  159.084 1.00 197.17 ?  57  GLY F O   1 
ATOM   11852 N N   . VAL F  5 58  ? 20.229  45.976  156.981 1.00 186.67 ?  58  VAL F N   1 
ATOM   11853 C CA  . VAL F  5 58  ? 21.069  47.042  156.441 1.00 194.62 ?  58  VAL F CA  1 
ATOM   11854 C C   . VAL F  5 58  ? 20.233  48.312  156.330 1.00 200.71 ?  58  VAL F C   1 
ATOM   11855 O O   . VAL F  5 58  ? 19.083  48.254  155.871 1.00 202.55 ?  58  VAL F O   1 
ATOM   11856 C CB  . VAL F  5 58  ? 21.668  46.634  155.088 1.00 199.86 ?  58  VAL F CB  1 
ATOM   11857 C CG1 . VAL F  5 58  ? 22.449  47.779  154.485 1.00 208.81 ?  58  VAL F CG1 1 
ATOM   11858 C CG2 . VAL F  5 58  ? 22.550  45.415  155.261 1.00 193.64 ?  58  VAL F CG2 1 
ATOM   11859 N N   . PRO F  5 59  ? 20.761  49.469  156.737 1.00 194.84 ?  59  PRO F N   1 
ATOM   11860 C CA  . PRO F  5 59  ? 19.964  50.704  156.702 1.00 200.76 ?  59  PRO F CA  1 
ATOM   11861 C C   . PRO F  5 59  ? 19.526  51.088  155.294 1.00 209.83 ?  59  PRO F C   1 
ATOM   11862 O O   . PRO F  5 59  ? 20.230  50.853  154.309 1.00 214.02 ?  59  PRO F O   1 
ATOM   11863 C CB  . PRO F  5 59  ? 20.909  51.755  157.297 1.00 203.28 ?  59  PRO F CB  1 
ATOM   11864 C CG  . PRO F  5 59  ? 21.886  50.979  158.114 1.00 195.64 ?  59  PRO F CG  1 
ATOM   11865 C CD  . PRO F  5 59  ? 22.047  49.654  157.432 1.00 192.88 ?  59  PRO F CD  1 
ATOM   11866 N N   . SER F  5 60  ? 18.334  51.691  155.217 1.00 207.60 ?  60  SER F N   1 
ATOM   11867 C CA  . SER F  5 60  ? 17.719  52.067  153.948 1.00 216.07 ?  60  SER F CA  1 
ATOM   11868 C C   . SER F  5 60  ? 18.509  53.125  153.186 1.00 224.70 ?  60  SER F C   1 
ATOM   11869 O O   . SER F  5 60  ? 18.246  53.329  151.995 1.00 233.28 ?  60  SER F O   1 
ATOM   11870 C CB  . SER F  5 60  ? 16.293  52.570  154.189 1.00 221.89 ?  60  SER F CB  1 
ATOM   11871 O OG  . SER F  5 60  ? 16.278  53.658  155.098 1.00 229.17 ?  60  SER F OG  1 
ATOM   11872 N N   . ARG F  5 61  ? 19.458  53.804  153.830 1.00 214.66 ?  61  ARG F N   1 
ATOM   11873 C CA  . ARG F  5 61  ? 20.250  54.806  153.129 1.00 224.21 ?  61  ARG F CA  1 
ATOM   11874 C C   . ARG F  5 61  ? 21.209  54.181  152.123 1.00 226.72 ?  61  ARG F C   1 
ATOM   11875 O O   . ARG F  5 61  ? 21.768  54.908  151.293 1.00 234.64 ?  61  ARG F O   1 
ATOM   11876 C CB  . ARG F  5 61  ? 21.008  55.673  154.136 1.00 221.90 ?  61  ARG F CB  1 
ATOM   11877 C CG  . ARG F  5 61  ? 22.050  54.919  154.933 1.00 214.01 ?  61  ARG F CG  1 
ATOM   11878 C CD  . ARG F  5 61  ? 22.731  55.820  155.948 1.00 214.37 ?  61  ARG F CD  1 
ATOM   11879 N NE  . ARG F  5 61  ? 23.680  55.086  156.780 1.00 206.82 ?  61  ARG F NE  1 
ATOM   11880 C CZ  . ARG F  5 61  ? 23.338  54.396  157.862 1.00 198.01 ?  61  ARG F CZ  1 
ATOM   11881 N NH1 . ARG F  5 61  ? 22.072  54.368  158.254 1.00 199.85 1  61  ARG F NH1 1 
ATOM   11882 N NH2 . ARG F  5 61  ? 24.260  53.754  158.568 1.00 194.45 ?  61  ARG F NH2 1 
ATOM   11883 N N   . PHE F  5 62  ? 21.406  52.862  152.181 1.00 218.02 ?  62  PHE F N   1 
ATOM   11884 C CA  . PHE F  5 62  ? 22.182  52.119  151.195 1.00 220.73 ?  62  PHE F CA  1 
ATOM   11885 C C   . PHE F  5 62  ? 21.269  51.668  150.061 1.00 224.94 ?  62  PHE F C   1 
ATOM   11886 O O   . PHE F  5 62  ? 20.168  51.166  150.306 1.00 222.42 ?  62  PHE F O   1 
ATOM   11887 C CB  . PHE F  5 62  ? 22.852  50.894  151.826 1.00 210.78 ?  62  PHE F CB  1 
ATOM   11888 C CG  . PHE F  5 62  ? 23.962  51.226  152.776 1.00 207.98 ?  62  PHE F CG  1 
ATOM   11889 C CD1 . PHE F  5 62  ? 25.254  51.397  152.311 1.00 212.24 ?  62  PHE F CD1 1 
ATOM   11890 C CD2 . PHE F  5 62  ? 23.719  51.354  154.134 1.00 202.86 ?  62  PHE F CD2 1 
ATOM   11891 C CE1 . PHE F  5 62  ? 26.280  51.706  153.177 1.00 210.28 ?  62  PHE F CE1 1 
ATOM   11892 C CE2 . PHE F  5 62  ? 24.744  51.661  155.008 1.00 200.16 ?  62  PHE F CE2 1 
ATOM   11893 C CZ  . PHE F  5 62  ? 26.027  51.838  154.528 1.00 204.61 ?  62  PHE F CZ  1 
ATOM   11894 N N   . SER F  5 63  ? 21.723  51.861  148.825 1.00 204.91 ?  63  SER F N   1 
ATOM   11895 C CA  . SER F  5 63  ? 21.036  51.321  147.662 1.00 209.45 ?  63  SER F CA  1 
ATOM   11896 C C   . SER F  5 63  ? 22.070  50.996  146.597 1.00 214.81 ?  63  SER F C   1 
ATOM   11897 O O   . SER F  5 63  ? 23.212  51.458  146.654 1.00 217.11 ?  63  SER F O   1 
ATOM   11898 C CB  . SER F  5 63  ? 19.995  52.308  147.117 1.00 218.18 ?  63  SER F CB  1 
ATOM   11899 O OG  . SER F  5 63  ? 20.619  53.460  146.574 1.00 227.74 ?  63  SER F OG  1 
ATOM   11900 N N   . ALA F  5 64  ? 21.658  50.198  145.616 1.00 214.11 ?  64  ALA F N   1 
ATOM   11901 C CA  . ALA F  5 64  ? 22.579  49.783  144.571 1.00 218.27 ?  64  ALA F CA  1 
ATOM   11902 C C   . ALA F  5 64  ? 21.798  49.495  143.300 1.00 225.32 ?  64  ALA F C   1 
ATOM   11903 O O   . ALA F  5 64  ? 20.614  49.148  143.343 1.00 223.94 ?  64  ALA F O   1 
ATOM   11904 C CB  . ALA F  5 64  ? 23.388  48.553  144.998 1.00 206.91 ?  64  ALA F CB  1 
ATOM   11905 N N   . THR F  5 65  ? 22.481  49.643  142.167 1.00 215.17 ?  65  THR F N   1 
ATOM   11906 C CA  . THR F  5 65  ? 21.882  49.503  140.848 1.00 223.13 ?  65  THR F CA  1 
ATOM   11907 C C   . THR F  5 65  ? 22.838  48.765  139.924 1.00 218.71 ?  65  THR F C   1 
ATOM   11908 O O   . THR F  5 65  ? 24.006  48.536  140.249 1.00 209.85 ?  65  THR F O   1 
ATOM   11909 C CB  . THR F  5 65  ? 21.527  50.864  140.229 1.00 240.69 ?  65  THR F CB  1 
ATOM   11910 O OG1 . THR F  5 65  ? 22.729  51.568  139.889 1.00 248.31 ?  65  THR F OG1 1 
ATOM   11911 C CG2 . THR F  5 65  ? 20.695  51.705  141.180 1.00 243.94 ?  65  THR F CG2 1 
ATOM   11912 N N   . GLY F  5 66  ? 22.318  48.386  138.758 1.00 221.91 ?  66  GLY F N   1 
ATOM   11913 C CA  . GLY F  5 66  ? 23.142  47.864  137.689 1.00 218.35 ?  66  GLY F CA  1 
ATOM   11914 C C   . GLY F  5 66  ? 22.894  46.443  137.231 1.00 211.59 ?  66  GLY F C   1 
ATOM   11915 O O   . GLY F  5 66  ? 22.262  45.634  137.917 1.00 207.11 ?  66  GLY F O   1 
ATOM   11916 N N   . SER F  5 67  ? 23.412  46.144  136.046 1.00 218.43 ?  67  SER F N   1 
ATOM   11917 C CA  . SER F  5 67  ? 23.358  44.819  135.450 1.00 218.12 ?  67  SER F CA  1 
ATOM   11918 C C   . SER F  5 67  ? 24.508  44.735  134.462 1.00 218.61 ?  67  SER F C   1 
ATOM   11919 O O   . SER F  5 67  ? 25.107  45.749  134.095 1.00 220.28 ?  67  SER F O   1 
ATOM   11920 C CB  . SER F  5 67  ? 22.015  44.552  134.760 1.00 222.71 ?  67  SER F CB  1 
ATOM   11921 O OG  . SER F  5 67  ? 21.072  43.978  135.649 1.00 222.98 ?  67  SER F OG  1 
ATOM   11922 N N   . GLY F  5 68  ? 24.815  43.520  134.031 1.00 220.78 ?  68  GLY F N   1 
ATOM   11923 C CA  . GLY F  5 68  ? 25.842  43.389  133.023 1.00 221.69 ?  68  GLY F CA  1 
ATOM   11924 C C   . GLY F  5 68  ? 27.244  43.675  133.519 1.00 217.86 ?  68  GLY F C   1 
ATOM   11925 O O   . GLY F  5 68  ? 27.782  42.937  134.349 1.00 213.01 ?  68  GLY F O   1 
ATOM   11926 N N   . THR F  5 69  ? 27.855  44.739  132.999 1.00 225.43 ?  69  THR F N   1 
ATOM   11927 C CA  . THR F  5 69  ? 29.213  45.122  133.362 1.00 222.81 ?  69  THR F CA  1 
ATOM   11928 C C   . THR F  5 69  ? 29.326  46.356  134.251 1.00 223.65 ?  69  THR F C   1 
ATOM   11929 O O   . THR F  5 69  ? 30.442  46.687  134.667 1.00 221.63 ?  69  THR F O   1 
ATOM   11930 C CB  . THR F  5 69  ? 30.028  45.369  132.088 1.00 232.14 ?  69  THR F CB  1 
ATOM   11931 O OG1 . THR F  5 69  ? 29.424  46.434  131.342 1.00 243.00 ?  69  THR F OG1 1 
ATOM   11932 C CG2 . THR F  5 69  ? 30.065  44.117  131.223 1.00 231.76 ?  69  THR F CG2 1 
ATOM   11933 N N   . HIS F  5 70  ? 28.231  47.046  134.562 1.00 233.60 ?  70  HIS F N   1 
ATOM   11934 C CA  . HIS F  5 70  ? 28.316  48.312  135.285 1.00 240.04 ?  70  HIS F CA  1 
ATOM   11935 C C   . HIS F  5 70  ? 27.396  48.325  136.498 1.00 239.49 ?  70  HIS F C   1 
ATOM   11936 O O   . HIS F  5 70  ? 26.185  48.116  136.366 1.00 244.82 ?  70  HIS F O   1 
ATOM   11937 C CB  . HIS F  5 70  ? 27.979  49.475  134.346 1.00 255.10 ?  70  HIS F CB  1 
ATOM   11938 C CG  . HIS F  5 70  ? 28.025  50.820  135.000 1.00 264.06 ?  70  HIS F CG  1 
ATOM   11939 N ND1 . HIS F  5 70  ? 26.897  51.464  135.459 1.00 276.03 ?  70  HIS F ND1 1 
ATOM   11940 C CD2 . HIS F  5 70  ? 29.064  51.649  135.260 1.00 265.02 ?  70  HIS F CD2 1 
ATOM   11941 C CE1 . HIS F  5 70  ? 27.239  52.629  135.979 1.00 279.13 ?  70  HIS F CE1 1 
ATOM   11942 N NE2 . HIS F  5 70  ? 28.548  52.766  135.870 1.00 273.16 ?  70  HIS F NE2 1 
ATOM   11943 N N   . PHE F  5 71  ? 27.978  48.561  137.678 1.00 237.16 ?  71  PHE F N   1 
ATOM   11944 C CA  . PHE F  5 71  ? 27.268  48.512  138.949 1.00 235.42 ?  71  PHE F CA  1 
ATOM   11945 C C   . PHE F  5 71  ? 27.652  49.719  139.796 1.00 239.33 ?  71  PHE F C   1 
ATOM   11946 O O   . PHE F  5 71  ? 28.797  50.179  139.761 1.00 237.49 ?  71  PHE F O   1 
ATOM   11947 C CB  . PHE F  5 71  ? 27.579  47.223  139.722 1.00 221.03 ?  71  PHE F CB  1 
ATOM   11948 C CG  . PHE F  5 71  ? 27.269  45.971  138.955 1.00 216.78 ?  71  PHE F CG  1 
ATOM   11949 C CD1 . PHE F  5 71  ? 28.211  45.421  138.102 1.00 211.83 ?  71  PHE F CD1 1 
ATOM   11950 C CD2 . PHE F  5 71  ? 26.033  45.355  139.069 1.00 217.47 ?  71  PHE F CD2 1 
ATOM   11951 C CE1 . PHE F  5 71  ? 27.933  44.275  137.387 1.00 207.52 ?  71  PHE F CE1 1 
ATOM   11952 C CE2 . PHE F  5 71  ? 25.748  44.207  138.352 1.00 214.70 ?  71  PHE F CE2 1 
ATOM   11953 C CZ  . PHE F  5 71  ? 26.700  43.668  137.511 1.00 209.05 ?  71  PHE F CZ  1 
ATOM   11954 N N   . THR F  5 72  ? 26.688  50.233  140.560 1.00 219.93 ?  72  THR F N   1 
ATOM   11955 C CA  . THR F  5 72  ? 26.954  51.301  141.513 1.00 219.00 ?  72  THR F CA  1 
ATOM   11956 C C   . THR F  5 72  ? 26.307  51.009  142.858 1.00 216.27 ?  72  THR F C   1 
ATOM   11957 O O   . THR F  5 72  ? 25.299  50.303  142.945 1.00 216.62 ?  72  THR F O   1 
ATOM   11958 C CB  . THR F  5 72  ? 26.437  52.660  141.013 1.00 234.62 ?  72  THR F CB  1 
ATOM   11959 O OG1 . THR F  5 72  ? 25.019  52.593  140.819 1.00 242.38 ?  72  THR F OG1 1 
ATOM   11960 C CG2 . THR F  5 72  ? 27.110  53.047  139.710 1.00 239.06 ?  72  THR F CG2 1 
ATOM   11961 N N   . LEU F  5 73  ? 26.906  51.569  143.907 1.00 231.95 ?  73  LEU F N   1 
ATOM   11962 C CA  . LEU F  5 73  ? 26.349  51.561  145.253 1.00 229.86 ?  73  LEU F CA  1 
ATOM   11963 C C   . LEU F  5 73  ? 26.249  53.013  145.699 1.00 240.62 ?  73  LEU F C   1 
ATOM   11964 O O   . LEU F  5 73  ? 27.214  53.771  145.558 1.00 242.32 ?  73  LEU F O   1 
ATOM   11965 C CB  . LEU F  5 73  ? 27.217  50.745  146.218 1.00 215.93 ?  73  LEU F CB  1 
ATOM   11966 C CG  . LEU F  5 73  ? 26.847  50.781  147.704 1.00 212.21 ?  73  LEU F CG  1 
ATOM   11967 C CD1 . LEU F  5 73  ? 25.647  49.886  147.986 1.00 211.42 ?  73  LEU F CD1 1 
ATOM   11968 C CD2 . LEU F  5 73  ? 28.027  50.378  148.577 1.00 204.94 ?  73  LEU F CD2 1 
ATOM   11969 N N   . THR F  5 74  ? 25.101  53.400  146.247 1.00 225.69 ?  74  THR F N   1 
ATOM   11970 C CA  . THR F  5 74  ? 24.877  54.780  146.656 1.00 229.72 ?  74  THR F CA  1 
ATOM   11971 C C   . THR F  5 74  ? 24.484  54.833  148.126 1.00 221.97 ?  74  THR F C   1 
ATOM   11972 O O   . THR F  5 74  ? 23.672  54.026  148.588 1.00 221.05 ?  74  THR F O   1 
ATOM   11973 C CB  . THR F  5 74  ? 23.776  55.423  145.799 1.00 238.27 ?  74  THR F CB  1 
ATOM   11974 O OG1 . THR F  5 74  ? 24.203  55.479  144.432 1.00 249.62 ?  74  THR F OG1 1 
ATOM   11975 C CG2 . THR F  5 74  ? 23.470  56.831  146.282 1.00 243.46 ?  74  THR F CG2 1 
ATOM   11976 N N   . VAL F  5 75  ? 25.054  55.792  148.855 1.00 237.97 ?  75  VAL F N   1 
ATOM   11977 C CA  . VAL F  5 75  ? 24.587  56.155  150.189 1.00 231.86 ?  75  VAL F CA  1 
ATOM   11978 C C   . VAL F  5 75  ? 23.922  57.522  150.118 1.00 239.09 ?  75  VAL F C   1 
ATOM   11979 O O   . VAL F  5 75  ? 24.553  58.510  149.722 1.00 247.38 ?  75  VAL F O   1 
ATOM   11980 C CB  . VAL F  5 75  ? 25.736  56.157  151.210 1.00 225.68 ?  75  VAL F CB  1 
ATOM   11981 C CG1 . VAL F  5 75  ? 25.198  56.364  152.622 1.00 219.21 ?  75  VAL F CG1 1 
ATOM   11982 C CG2 . VAL F  5 75  ? 26.532  54.854  151.127 1.00 222.52 ?  75  VAL F CG2 1 
ATOM   11983 N N   . SER F  5 76  ? 22.643  57.578  150.493 1.00 227.57 ?  76  SER F N   1 
ATOM   11984 C CA  . SER F  5 76  ? 21.885  58.809  150.299 1.00 237.67 ?  76  SER F CA  1 
ATOM   11985 C C   . SER F  5 76  ? 22.391  59.919  151.215 1.00 240.80 ?  76  SER F C   1 
ATOM   11986 O O   . SER F  5 76  ? 22.499  61.077  150.794 1.00 249.87 ?  76  SER F O   1 
ATOM   11987 C CB  . SER F  5 76  ? 20.395  58.548  150.517 1.00 238.30 ?  76  SER F CB  1 
ATOM   11988 O OG  . SER F  5 76  ? 20.149  58.071  151.826 1.00 231.51 ?  76  SER F OG  1 
ATOM   11989 N N   . SER F  5 77  ? 22.698  59.590  152.474 1.00 252.47 ?  77  SER F N   1 
ATOM   11990 C CA  . SER F  5 77  ? 23.342  60.537  153.386 1.00 254.71 ?  77  SER F CA  1 
ATOM   11991 C C   . SER F  5 77  ? 24.301  59.800  154.317 1.00 245.52 ?  77  SER F C   1 
ATOM   11992 O O   . SER F  5 77  ? 23.857  58.998  155.146 1.00 238.89 ?  77  SER F O   1 
ATOM   11993 C CB  . SER F  5 77  ? 22.288  61.303  154.184 1.00 259.48 ?  77  SER F CB  1 
ATOM   11994 O OG  . SER F  5 77  ? 22.854  62.388  154.899 1.00 263.89 ?  77  SER F OG  1 
ATOM   11995 N N   . LEU F  5 78  ? 25.604  60.055  154.176 1.00 251.71 ?  78  LEU F N   1 
ATOM   11996 C CA  . LEU F  5 78  ? 26.608  59.349  154.969 1.00 243.23 ?  78  LEU F CA  1 
ATOM   11997 C C   . LEU F  5 78  ? 26.497  59.687  156.453 1.00 241.75 ?  78  LEU F C   1 
ATOM   11998 O O   . LEU F  5 78  ? 26.341  60.852  156.832 1.00 248.84 ?  78  LEU F O   1 
ATOM   11999 C CB  . LEU F  5 78  ? 28.022  59.686  154.488 1.00 244.49 ?  78  LEU F CB  1 
ATOM   12000 C CG  . LEU F  5 78  ? 28.562  59.069  153.200 1.00 243.18 ?  78  LEU F CG  1 
ATOM   12001 C CD1 . LEU F  5 78  ? 29.773  59.850  152.719 1.00 248.13 ?  78  LEU F CD1 1 
ATOM   12002 C CD2 . LEU F  5 78  ? 28.926  57.614  153.444 1.00 232.55 ?  78  LEU F CD2 1 
ATOM   12003 N N   . GLN F  5 79  ? 26.587  58.661  157.292 1.00 241.89 ?  79  GLN F N   1 
ATOM   12004 C CA  . GLN F  5 79  ? 26.680  58.776  158.739 1.00 239.46 ?  79  GLN F CA  1 
ATOM   12005 C C   . GLN F  5 79  ? 28.065  58.346  159.206 1.00 233.63 ?  79  GLN F C   1 
ATOM   12006 O O   . GLN F  5 79  ? 28.786  57.657  158.476 1.00 229.85 ?  79  GLN F O   1 
ATOM   12007 C CB  . GLN F  5 79  ? 25.599  57.941  159.440 1.00 234.67 ?  79  GLN F CB  1 
ATOM   12008 C CG  . GLN F  5 79  ? 24.190  58.249  158.973 1.00 240.22 ?  79  GLN F CG  1 
ATOM   12009 C CD  . GLN F  5 79  ? 23.139  57.569  159.824 1.00 236.50 ?  79  GLN F CD  1 
ATOM   12010 O OE1 . GLN F  5 79  ? 23.462  56.835  160.759 1.00 229.71 ?  79  GLN F OE1 1 
ATOM   12011 N NE2 . GLN F  5 79  ? 21.873  57.822  159.515 1.00 241.47 ?  79  GLN F NE2 1 
ATOM   12012 N N   . PRO F  5 80  ? 28.494  58.771  160.402 1.00 245.00 ?  80  PRO F N   1 
ATOM   12013 C CA  . PRO F  5 80  ? 29.863  58.443  160.842 1.00 240.39 ?  80  PRO F CA  1 
ATOM   12014 C C   . PRO F  5 80  ? 30.225  56.967  160.760 1.00 230.66 ?  80  PRO F C   1 
ATOM   12015 O O   . PRO F  5 80  ? 31.375  56.645  160.440 1.00 227.98 ?  80  PRO F O   1 
ATOM   12016 C CB  . PRO F  5 80  ? 29.879  58.947  162.290 1.00 241.30 ?  80  PRO F CB  1 
ATOM   12017 C CG  . PRO F  5 80  ? 28.926  60.083  162.284 1.00 250.00 ?  80  PRO F CG  1 
ATOM   12018 C CD  . PRO F  5 80  ? 27.818  59.670  161.355 1.00 250.24 ?  80  PRO F CD  1 
ATOM   12019 N N   . GLU F  5 81  ? 29.287  56.057  161.043 1.00 245.43 ?  81  GLU F N   1 
ATOM   12020 C CA  . GLU F  5 81  ? 29.619  54.636  160.988 1.00 236.43 ?  81  GLU F CA  1 
ATOM   12021 C C   . GLU F  5 81  ? 29.785  54.117  159.564 1.00 235.69 ?  81  GLU F C   1 
ATOM   12022 O O   . GLU F  5 81  ? 30.209  52.968  159.392 1.00 228.80 ?  81  GLU F O   1 
ATOM   12023 C CB  . GLU F  5 81  ? 28.586  53.781  161.737 1.00 231.50 ?  81  GLU F CB  1 
ATOM   12024 C CG  . GLU F  5 81  ? 27.151  53.841  161.236 1.00 234.70 ?  81  GLU F CG  1 
ATOM   12025 C CD  . GLU F  5 81  ? 26.313  54.868  161.973 1.00 242.34 ?  81  GLU F CD  1 
ATOM   12026 O OE1 . GLU F  5 81  ? 26.868  55.893  162.419 1.00 245.74 ?  81  GLU F OE1 1 
ATOM   12027 O OE2 . GLU F  5 81  ? 25.094  54.636  162.122 1.00 246.91 -1 81  GLU F OE2 1 
ATOM   12028 N N   . ASP F  5 82  ? 29.466  54.918  158.545 1.00 220.29 ?  82  ASP F N   1 
ATOM   12029 C CA  . ASP F  5 82  ? 29.555  54.459  157.164 1.00 220.48 ?  82  ASP F CA  1 
ATOM   12030 C C   . ASP F  5 82  ? 30.926  54.659  156.533 1.00 221.66 ?  82  ASP F C   1 
ATOM   12031 O O   . ASP F  5 82  ? 31.144  54.183  155.413 1.00 221.65 ?  82  ASP F O   1 
ATOM   12032 C CB  . ASP F  5 82  ? 28.498  55.159  156.305 1.00 228.08 ?  82  ASP F CB  1 
ATOM   12033 C CG  . ASP F  5 82  ? 27.087  54.920  156.807 1.00 227.39 ?  82  ASP F CG  1 
ATOM   12034 O OD1 . ASP F  5 82  ? 26.848  53.881  157.460 1.00 220.04 ?  82  ASP F OD1 1 
ATOM   12035 O OD2 . ASP F  5 82  ? 26.213  55.770  156.540 1.00 234.56 -1 82  ASP F OD2 1 
ATOM   12036 N N   . PHE F  5 83  ? 31.856  55.333  157.203 1.00 231.54 ?  83  PHE F N   1 
ATOM   12037 C CA  . PHE F  5 83  ? 33.182  55.527  156.627 1.00 233.01 ?  83  PHE F CA  1 
ATOM   12038 C C   . PHE F  5 83  ? 33.995  54.270  156.904 1.00 224.29 ?  83  PHE F C   1 
ATOM   12039 O O   . PHE F  5 83  ? 34.306  53.959  158.058 1.00 219.66 ?  83  PHE F O   1 
ATOM   12040 C CB  . PHE F  5 83  ? 33.847  56.784  157.179 1.00 238.91 ?  83  PHE F CB  1 
ATOM   12041 C CG  . PHE F  5 83  ? 33.198  58.058  156.718 1.00 248.47 ?  83  PHE F CG  1 
ATOM   12042 C CD1 . PHE F  5 83  ? 32.091  58.578  157.369 1.00 251.21 ?  83  PHE F CD1 1 
ATOM   12043 C CD2 . PHE F  5 83  ? 33.690  58.725  155.608 1.00 255.13 ?  83  PHE F CD2 1 
ATOM   12044 C CE1 . PHE F  5 83  ? 31.497  59.750  156.924 1.00 260.44 ?  83  PHE F CE1 1 
ATOM   12045 C CE2 . PHE F  5 83  ? 33.104  59.893  155.159 1.00 264.31 ?  83  PHE F CE2 1 
ATOM   12046 C CZ  . PHE F  5 83  ? 32.007  60.406  155.817 1.00 266.94 ?  83  PHE F CZ  1 
ATOM   12047 N N   . ALA F  5 84  ? 34.341  53.558  155.842 1.00 220.21 ?  84  ALA F N   1 
ATOM   12048 C CA  . ALA F  5 84  ? 34.823  52.183  155.906 1.00 211.94 ?  84  ALA F CA  1 
ATOM   12049 C C   . ALA F  5 84  ? 35.286  51.817  154.504 1.00 213.40 ?  84  ALA F C   1 
ATOM   12050 O O   . ALA F  5 84  ? 35.257  52.646  153.589 1.00 220.67 ?  84  ALA F O   1 
ATOM   12051 C CB  . ALA F  5 84  ? 33.748  51.220  156.416 1.00 205.91 ?  84  ALA F CB  1 
ATOM   12052 N N   . THR F  5 85  ? 35.714  50.572  154.334 1.00 200.89 ?  85  THR F N   1 
ATOM   12053 C CA  . THR F  5 85  ? 36.045  50.072  153.011 1.00 202.04 ?  85  THR F CA  1 
ATOM   12054 C C   . THR F  5 85  ? 34.874  49.231  152.519 1.00 199.92 ?  85  THR F C   1 
ATOM   12055 O O   . THR F  5 85  ? 34.255  48.494  153.292 1.00 197.92 ?  85  THR F O   1 
ATOM   12056 C CB  . THR F  5 85  ? 37.333  49.240  153.040 1.00 197.28 ?  85  THR F CB  1 
ATOM   12057 O OG1 . THR F  5 85  ? 38.437  50.065  153.434 1.00 200.19 ?  85  THR F OG1 1 
ATOM   12058 C CG2 . THR F  5 85  ? 37.634  48.658  151.672 1.00 198.84 ?  85  THR F CG2 1 
ATOM   12059 N N   . TYR F  5 86  ? 34.575  49.355  151.227 1.00 197.31 ?  86  TYR F N   1 
ATOM   12060 C CA  . TYR F  5 86  ? 33.485  48.647  150.569 1.00 196.12 ?  86  TYR F CA  1 
ATOM   12061 C C   . TYR F  5 86  ? 34.022  47.790  149.428 1.00 195.47 ?  86  TYR F C   1 
ATOM   12062 O O   . TYR F  5 86  ? 34.857  48.246  148.638 1.00 200.67 ?  86  TYR F O   1 
ATOM   12063 C CB  . TYR F  5 86  ? 32.432  49.639  150.039 1.00 203.82 ?  86  TYR F CB  1 
ATOM   12064 C CG  . TYR F  5 86  ? 31.694  50.413  151.119 1.00 208.13 ?  86  TYR F CG  1 
ATOM   12065 C CD1 . TYR F  5 86  ? 32.224  51.586  151.643 1.00 211.89 ?  86  TYR F CD1 1 
ATOM   12066 C CD2 . TYR F  5 86  ? 30.463  49.981  151.600 1.00 202.55 ?  86  TYR F CD2 1 
ATOM   12067 C CE1 . TYR F  5 86  ? 31.561  52.296  152.626 1.00 213.20 ?  86  TYR F CE1 1 
ATOM   12068 C CE2 . TYR F  5 86  ? 29.789  50.690  152.582 1.00 203.56 ?  86  TYR F CE2 1 
ATOM   12069 C CZ  . TYR F  5 86  ? 30.344  51.845  153.090 1.00 208.02 ?  86  TYR F CZ  1 
ATOM   12070 O OH  . TYR F  5 86  ? 29.677  52.553  154.064 1.00 210.05 ?  86  TYR F OH  1 
ATOM   12071 N N   . PHE F  5 87  ? 33.544  46.549  149.350 1.00 202.84 ?  87  PHE F N   1 
ATOM   12072 C CA  . PHE F  5 87  ? 33.933  45.606  148.309 1.00 201.96 ?  87  PHE F CA  1 
ATOM   12073 C C   . PHE F  5 87  ? 32.711  45.164  147.517 1.00 203.34 ?  87  PHE F C   1 
ATOM   12074 O O   . PHE F  5 87  ? 31.619  45.008  148.074 1.00 200.83 ?  87  PHE F O   1 
ATOM   12075 C CB  . PHE F  5 87  ? 34.627  44.361  148.886 1.00 193.37 ?  87  PHE F CB  1 
ATOM   12076 C CG  . PHE F  5 87  ? 35.945  44.644  149.538 1.00 192.03 ?  87  PHE F CG  1 
ATOM   12077 C CD1 . PHE F  5 87  ? 37.109  44.677  148.788 1.00 194.94 ?  87  PHE F CD1 1 
ATOM   12078 C CD2 . PHE F  5 87  ? 36.025  44.863  150.902 1.00 188.35 ?  87  PHE F CD2 1 
ATOM   12079 C CE1 . PHE F  5 87  ? 38.328  44.940  149.384 1.00 194.07 ?  87  PHE F CE1 1 
ATOM   12080 C CE2 . PHE F  5 87  ? 37.242  45.123  151.506 1.00 187.47 ?  87  PHE F CE2 1 
ATOM   12081 C CZ  . PHE F  5 87  ? 38.395  45.163  150.745 1.00 190.29 ?  87  PHE F CZ  1 
ATOM   12082 N N   . CYS F  5 88  ? 32.906  44.950  146.219 1.00 198.23 ?  88  CYS F N   1 
ATOM   12083 C CA  . CYS F  5 88  ? 31.929  44.258  145.397 1.00 198.72 ?  88  CYS F CA  1 
ATOM   12084 C C   . CYS F  5 88  ? 32.449  42.860  145.087 1.00 193.19 ?  88  CYS F C   1 
ATOM   12085 O O   . CYS F  5 88  ? 33.656  42.604  145.103 1.00 191.79 ?  88  CYS F O   1 
ATOM   12086 C CB  . CYS F  5 88  ? 31.645  45.034  144.103 1.00 208.49 ?  88  CYS F CB  1 
ATOM   12087 S SG  . CYS F  5 88  ? 33.081  45.349  143.040 1.00 214.47 ?  88  CYS F SG  1 
ATOM   12088 N N   . GLN F  5 89  ? 31.517  41.952  144.801 1.00 200.01 ?  89  GLN F N   1 
ATOM   12089 C CA  . GLN F  5 89  ? 31.849  40.558  144.543 1.00 194.66 ?  89  GLN F CA  1 
ATOM   12090 C C   . GLN F  5 89  ? 30.863  39.989  143.533 1.00 197.23 ?  89  GLN F C   1 
ATOM   12091 O O   . GLN F  5 89  ? 29.656  40.218  143.646 1.00 198.41 ?  89  GLN F O   1 
ATOM   12092 C CB  . GLN F  5 89  ? 31.834  39.743  145.845 1.00 185.26 ?  89  GLN F CB  1 
ATOM   12093 C CG  . GLN F  5 89  ? 32.093  38.251  145.679 1.00 179.30 ?  89  GLN F CG  1 
ATOM   12094 C CD  . GLN F  5 89  ? 31.087  37.391  146.426 1.00 172.97 ?  89  GLN F CD  1 
ATOM   12095 O OE1 . GLN F  5 89  ? 30.603  37.764  147.494 1.00 170.53 ?  89  GLN F OE1 1 
ATOM   12096 N NE2 . GLN F  5 89  ? 30.778  36.226  145.871 1.00 170.64 ?  89  GLN F NE2 1 
ATOM   12097 N N   . HIS F  5 90  ? 31.374  39.249  142.553 1.00 199.76 ?  90  HIS F N   1 
ATOM   12098 C CA  . HIS F  5 90  ? 30.523  38.542  141.608 1.00 201.75 ?  90  HIS F CA  1 
ATOM   12099 C C   . HIS F  5 90  ? 30.563  37.049  141.906 1.00 193.92 ?  90  HIS F C   1 
ATOM   12100 O O   . HIS F  5 90  ? 31.558  36.525  142.417 1.00 188.63 ?  90  HIS F O   1 
ATOM   12101 C CB  . HIS F  5 90  ? 30.959  38.787  140.164 1.00 210.02 ?  90  HIS F CB  1 
ATOM   12102 C CG  . HIS F  5 90  ? 32.009  37.835  139.687 1.00 208.08 ?  90  HIS F CG  1 
ATOM   12103 N ND1 . HIS F  5 90  ? 31.702  36.667  139.023 1.00 206.93 ?  90  HIS F ND1 1 
ATOM   12104 C CD2 . HIS F  5 90  ? 33.357  37.864  139.794 1.00 207.29 ?  90  HIS F CD2 1 
ATOM   12105 C CE1 . HIS F  5 90  ? 32.817  36.022  138.732 1.00 205.65 ?  90  HIS F CE1 1 
ATOM   12106 N NE2 . HIS F  5 90  ? 33.836  36.727  139.189 1.00 205.83 ?  90  HIS F NE2 1 
ATOM   12107 N N   . MET F  5 91  ? 29.463  36.367  141.584 1.00 195.78 ?  91  MET F N   1 
ATOM   12108 C CA  . MET F  5 91  ? 29.369  34.916  141.696 1.00 189.45 ?  91  MET F CA  1 
ATOM   12109 C C   . MET F  5 91  ? 28.959  34.224  140.397 1.00 193.53 ?  91  MET F C   1 
ATOM   12110 O O   . MET F  5 91  ? 28.447  33.101  140.438 1.00 189.36 ?  91  MET F O   1 
ATOM   12111 C CB  . MET F  5 91  ? 28.392  34.584  142.821 1.00 183.43 ?  91  MET F CB  1 
ATOM   12112 C CG  . MET F  5 91  ? 27.024  35.203  142.602 1.00 188.12 ?  91  MET F CG  1 
ATOM   12113 S SD  . MET F  5 91  ? 26.401  35.972  144.103 1.00 184.86 ?  91  MET F SD  1 
ATOM   12114 C CE  . MET F  5 91  ? 27.349  37.490  144.115 1.00 190.11 ?  91  MET F CE  1 
ATOM   12115 N N   . SER F  5 92  ? 29.164  34.862  139.242 1.00 184.63 ?  92  SER F N   1 
ATOM   12116 C CA  . SER F  5 92  ? 28.603  34.347  137.994 1.00 189.85 ?  92  SER F CA  1 
ATOM   12117 C C   . SER F  5 92  ? 29.344  33.135  137.430 1.00 187.93 ?  92  SER F C   1 
ATOM   12118 O O   . SER F  5 92  ? 28.779  32.426  136.590 1.00 190.47 ?  92  SER F O   1 
ATOM   12119 C CB  . SER F  5 92  ? 28.566  35.455  136.941 1.00 200.29 ?  92  SER F CB  1 
ATOM   12120 O OG  . SER F  5 92  ? 29.874  35.878  136.606 1.00 203.30 ?  92  SER F OG  1 
ATOM   12121 N N   . SER F  5 93  ? 30.573  32.872  137.868 1.00 188.68 ?  93  SER F N   1 
ATOM   12122 C CA  . SER F  5 93  ? 31.382  31.783  137.327 1.00 187.45 ?  93  SER F CA  1 
ATOM   12123 C C   . SER F  5 93  ? 32.633  31.661  138.185 1.00 181.93 ?  93  SER F C   1 
ATOM   12124 O O   . SER F  5 93  ? 32.956  32.555  138.970 1.00 180.72 ?  93  SER F O   1 
ATOM   12125 C CB  . SER F  5 93  ? 31.746  32.011  135.859 1.00 196.80 ?  93  SER F CB  1 
ATOM   12126 O OG  . SER F  5 93  ? 32.436  33.236  135.701 1.00 202.69 ?  93  SER F OG  1 
ATOM   12127 N N   . TYR F  5 94  ? 33.337  30.544  138.026 1.00 190.78 ?  94  TYR F N   1 
ATOM   12128 C CA  . TYR F  5 94  ? 34.509  30.286  138.856 1.00 185.39 ?  94  TYR F CA  1 
ATOM   12129 C C   . TYR F  5 94  ? 35.779  30.874  138.253 1.00 191.04 ?  94  TYR F C   1 
ATOM   12130 O O   . TYR F  5 94  ? 35.950  30.858  137.034 1.00 198.11 ?  94  TYR F O   1 
ATOM   12131 C CB  . TYR F  5 94  ? 34.723  28.777  139.028 1.00 179.56 ?  94  TYR F CB  1 
ATOM   12132 C CG  . TYR F  5 94  ? 33.651  28.028  139.787 1.00 172.94 ?  94  TYR F CG  1 
ATOM   12133 C CD1 . TYR F  5 94  ? 33.370  28.322  141.115 1.00 166.96 ?  94  TYR F CD1 1 
ATOM   12134 C CD2 . TYR F  5 94  ? 32.936  27.003  139.179 1.00 173.00 ?  94  TYR F CD2 1 
ATOM   12135 C CE1 . TYR F  5 94  ? 32.393  27.629  141.811 1.00 161.36 ?  94  TYR F CE1 1 
ATOM   12136 C CE2 . TYR F  5 94  ? 31.962  26.302  139.868 1.00 167.28 ?  94  TYR F CE2 1 
ATOM   12137 C CZ  . TYR F  5 94  ? 31.693  26.620  141.183 1.00 161.53 ?  94  TYR F CZ  1 
ATOM   12138 O OH  . TYR F  5 94  ? 30.729  25.923  141.875 1.00 156.26 ?  94  TYR F OH  1 
ATOM   12139 N N   . PRO F  5 95  ? 36.687  31.379  139.109 1.00 191.54 ?  95  PRO F N   1 
ATOM   12140 C CA  . PRO F  5 95  ? 36.563  31.541  140.564 1.00 184.20 ?  95  PRO F CA  1 
ATOM   12141 C C   . PRO F  5 95  ? 35.802  32.817  140.964 1.00 186.47 ?  95  PRO F C   1 
ATOM   12142 O O   . PRO F  5 95  ? 35.813  33.783  140.202 1.00 194.05 ?  95  PRO F O   1 
ATOM   12143 C CB  . PRO F  5 95  ? 38.019  31.592  141.020 1.00 182.63 ?  95  PRO F CB  1 
ATOM   12144 C CG  . PRO F  5 95  ? 38.703  32.288  139.903 1.00 191.38 ?  95  PRO F CG  1 
ATOM   12145 C CD  . PRO F  5 95  ? 38.013  31.816  138.636 1.00 196.32 ?  95  PRO F CD  1 
ATOM   12146 N N   . LEU F  5 96  ? 35.154  32.811  142.131 1.00 191.02 ?  96  LEU F N   1 
ATOM   12147 C CA  . LEU F  5 96  ? 34.594  34.034  142.699 1.00 192.62 ?  96  LEU F CA  1 
ATOM   12148 C C   . LEU F  5 96  ? 35.706  35.052  142.938 1.00 195.46 ?  96  LEU F C   1 
ATOM   12149 O O   . LEU F  5 96  ? 36.791  34.702  143.410 1.00 192.27 ?  96  LEU F O   1 
ATOM   12150 C CB  . LEU F  5 96  ? 33.862  33.727  144.009 1.00 185.26 ?  96  LEU F CB  1 
ATOM   12151 C CG  . LEU F  5 96  ? 32.381  33.331  143.965 1.00 184.11 ?  96  LEU F CG  1 
ATOM   12152 C CD1 . LEU F  5 96  ? 32.132  32.157  143.027 1.00 184.26 ?  96  LEU F CD1 1 
ATOM   12153 C CD2 . LEU F  5 96  ? 31.879  33.012  145.365 1.00 176.83 ?  96  LEU F CD2 1 
ATOM   12154 N N   . THR F  5 97  ? 35.448  36.318  142.598 1.00 192.68 ?  97  THR F N   1 
ATOM   12155 C CA  . THR F  5 97  ? 36.415  37.381  142.852 1.00 195.91 ?  97  THR F CA  1 
ATOM   12156 C C   . THR F  5 97  ? 35.773  38.625  143.459 1.00 198.21 ?  97  THR F C   1 
ATOM   12157 O O   . THR F  5 97  ? 34.571  38.873  143.324 1.00 199.83 ?  97  THR F O   1 
ATOM   12158 C CB  . THR F  5 97  ? 37.145  37.796  141.562 1.00 204.24 ?  97  THR F CB  1 
ATOM   12159 O OG1 . THR F  5 97  ? 36.196  38.320  140.626 1.00 210.91 ?  97  THR F OG1 1 
ATOM   12160 C CG2 . THR F  5 97  ? 37.873  36.612  140.933 1.00 202.86 ?  97  THR F CG2 1 
ATOM   12161 N N   . PHE F  5 98  ? 36.625  39.399  144.136 1.00 204.54 ?  98  PHE F N   1 
ATOM   12162 C CA  . PHE F  5 98  ? 36.306  40.647  144.817 1.00 206.88 ?  98  PHE F CA  1 
ATOM   12163 C C   . PHE F  5 98  ? 37.007  41.807  144.116 1.00 215.50 ?  98  PHE F C   1 
ATOM   12164 O O   . PHE F  5 98  ? 38.069  41.635  143.509 1.00 217.91 ?  98  PHE F O   1 
ATOM   12165 C CB  . PHE F  5 98  ? 36.729  40.611  146.293 1.00 200.21 ?  98  PHE F CB  1 
ATOM   12166 C CG  . PHE F  5 98  ? 35.922  39.663  147.139 1.00 192.40 ?  98  PHE F CG  1 
ATOM   12167 C CD1 . PHE F  5 98  ? 36.216  38.310  147.168 1.00 186.56 ?  98  PHE F CD1 1 
ATOM   12168 C CD2 . PHE F  5 98  ? 34.876  40.133  147.920 1.00 191.29 ?  98  PHE F CD2 1 
ATOM   12169 C CE1 . PHE F  5 98  ? 35.471  37.438  147.948 1.00 179.77 ?  98  PHE F CE1 1 
ATOM   12170 C CE2 . PHE F  5 98  ? 34.129  39.267  148.704 1.00 184.61 ?  98  PHE F CE2 1 
ATOM   12171 C CZ  . PHE F  5 98  ? 34.427  37.918  148.717 1.00 178.82 ?  98  PHE F CZ  1 
ATOM   12172 N N   . GLY F  5 99  ? 36.410  42.992  144.208 1.00 193.67 ?  99  GLY F N   1 
ATOM   12173 C CA  . GLY F  5 99  ? 37.090  44.205  143.804 1.00 195.82 ?  99  GLY F CA  1 
ATOM   12174 C C   . GLY F  5 99  ? 38.219  44.586  144.744 1.00 193.23 ?  99  GLY F C   1 
ATOM   12175 O O   . GLY F  5 99  ? 38.413  44.009  145.815 1.00 189.83 ?  99  GLY F O   1 
ATOM   12176 N N   . GLY F  5 100 ? 38.987  45.595  144.324 1.00 205.63 ?  100 GLY F N   1 
ATOM   12177 C CA  . GLY F  5 100 ? 40.149  46.019  145.086 1.00 204.67 ?  100 GLY F CA  1 
ATOM   12178 C C   . GLY F  5 100 ? 39.850  46.876  146.295 1.00 203.49 ?  100 GLY F C   1 
ATOM   12179 O O   . GLY F  5 100 ? 40.768  47.196  147.058 1.00 202.16 ?  100 GLY F O   1 
ATOM   12180 N N   . GLY F  5 101 ? 38.600  47.268  146.472 1.00 208.15 ?  101 GLY F N   1 
ATOM   12181 C CA  . GLY F  5 101 ? 38.111  48.042  147.601 1.00 207.40 ?  101 GLY F CA  1 
ATOM   12182 C C   . GLY F  5 101 ? 38.096  49.536  147.345 1.00 216.21 ?  101 GLY F C   1 
ATOM   12183 O O   . GLY F  5 101 ? 38.916  50.088  146.611 1.00 222.56 ?  101 GLY F O   1 
ATOM   12184 N N   . THR F  5 102 ? 37.123  50.198  147.971 1.00 209.70 ?  102 THR F N   1 
ATOM   12185 C CA  . THR F  5 102 ? 36.994  51.650  147.990 1.00 217.57 ?  102 THR F CA  1 
ATOM   12186 C C   . THR F  5 102 ? 36.955  52.089  149.448 1.00 214.39 ?  102 THR F C   1 
ATOM   12187 O O   . THR F  5 102 ? 36.033  51.714  150.182 1.00 209.81 ?  102 THR F O   1 
ATOM   12188 C CB  . THR F  5 102 ? 35.726  52.099  147.254 1.00 223.14 ?  102 THR F CB  1 
ATOM   12189 O OG1 . THR F  5 102 ? 35.854  51.837  145.850 1.00 227.32 ?  102 THR F OG1 1 
ATOM   12190 C CG2 . THR F  5 102 ? 35.480  53.581  147.465 1.00 230.91 ?  102 THR F CG2 1 
ATOM   12191 N N   . LYS F  5 103 ? 37.945  52.871  149.870 1.00 219.26 ?  103 LYS F N   1 
ATOM   12192 C CA  . LYS F  5 103 ? 37.990  53.383  151.234 1.00 217.17 ?  103 LYS F CA  1 
ATOM   12193 C C   . LYS F  5 103 ? 37.359  54.772  151.277 1.00 225.12 ?  103 LYS F C   1 
ATOM   12194 O O   . LYS F  5 103 ? 37.772  55.670  150.533 1.00 233.12 ?  103 LYS F O   1 
ATOM   12195 C CB  . LYS F  5 103 ? 39.428  53.405  151.751 1.00 215.59 ?  103 LYS F CB  1 
ATOM   12196 C CG  . LYS F  5 103 ? 39.567  53.800  153.208 1.00 213.03 ?  103 LYS F CG  1 
ATOM   12197 C CD  . LYS F  5 103 ? 40.996  53.630  153.693 1.00 210.88 ?  103 LYS F CD  1 
ATOM   12198 C CE  . LYS F  5 103 ? 41.068  53.754  155.202 1.00 207.06 ?  103 LYS F CE  1 
ATOM   12199 N NZ  . LYS F  5 103 ? 42.363  53.247  155.724 1.00 203.24 1  103 LYS F NZ  1 
ATOM   12200 N N   . VAL F  5 104 ? 36.363  54.945  152.141 1.00 236.40 ?  104 VAL F N   1 
ATOM   12201 C CA  . VAL F  5 104 ? 35.656  56.208  152.307 1.00 243.70 ?  104 VAL F CA  1 
ATOM   12202 C C   . VAL F  5 104 ? 36.144  56.872  153.589 1.00 243.61 ?  104 VAL F C   1 
ATOM   12203 O O   . VAL F  5 104 ? 35.967  56.327  154.684 1.00 237.15 ?  104 VAL F O   1 
ATOM   12204 C CB  . VAL F  5 104 ? 34.136  55.998  152.337 1.00 242.97 ?  104 VAL F CB  1 
ATOM   12205 C CG1 . VAL F  5 104 ? 33.406  57.328  152.383 1.00 251.48 ?  104 VAL F CG1 1 
ATOM   12206 C CG2 . VAL F  5 104 ? 33.688  55.179  151.136 1.00 242.30 ?  104 VAL F CG2 1 
ATOM   12207 N N   . GLU F  5 105 ? 36.760  58.043  153.457 1.00 259.18 ?  105 GLU F N   1 
ATOM   12208 C CA  . GLU F  5 105 ? 37.325  58.754  154.595 1.00 260.15 ?  105 GLU F CA  1 
ATOM   12209 C C   . GLU F  5 105 ? 36.617  60.091  154.802 1.00 268.33 ?  105 GLU F C   1 
ATOM   12210 O O   . GLU F  5 105 ? 35.984  60.633  153.892 1.00 274.91 ?  105 GLU F O   1 
ATOM   12211 C CB  . GLU F  5 105 ? 38.843  58.946  154.425 1.00 261.78 ?  105 GLU F CB  1 
ATOM   12212 C CG  . GLU F  5 105 ? 39.264  59.848  153.269 1.00 275.39 ?  105 GLU F CG  1 
ATOM   12213 C CD  . GLU F  5 105 ? 40.452  60.706  153.640 1.00 282.30 ?  105 GLU F CD  1 
ATOM   12214 O OE1 . GLU F  5 105 ? 41.458  60.168  154.121 1.00 281.90 ?  105 GLU F OE1 1 
ATOM   12215 O OE2 . GLU F  5 105 ? 40.378  61.937  153.431 1.00 291.04 -1 105 GLU F OE2 1 
ATOM   12216 N N   . ILE F  5 106 ? 36.728  60.618  156.023 1.00 272.12 ?  106 ILE F N   1 
ATOM   12217 C CA  . ILE F  5 106 ? 36.049  61.854  156.413 1.00 279.58 ?  106 ILE F CA  1 
ATOM   12218 C C   . ILE F  5 106 ? 36.909  63.062  156.057 1.00 288.23 ?  106 ILE F C   1 
ATOM   12219 O O   . ILE F  5 106 ? 38.112  63.088  156.342 1.00 287.29 ?  106 ILE F O   1 
ATOM   12220 C CB  . ILE F  5 106 ? 35.730  61.854  157.921 1.00 276.29 ?  106 ILE F CB  1 
ATOM   12221 C CG1 . ILE F  5 106 ? 34.842  60.669  158.303 1.00 269.47 ?  106 ILE F CG1 1 
ATOM   12222 C CG2 . ILE F  5 106 ? 35.070  63.158  158.339 1.00 287.32 ?  106 ILE F CG2 1 
ATOM   12223 C CD1 . ILE F  5 106 ? 34.416  60.683  159.761 1.00 269.23 ?  106 ILE F CD1 1 
ATOM   12224 N N   . LYS F  5 107 ? 36.296  64.062  155.423 1.00 277.24 ?  107 LYS F N   1 
ATOM   12225 C CA  . LYS F  5 107 ? 36.964  65.337  155.201 1.00 286.53 ?  107 LYS F CA  1 
ATOM   12226 C C   . LYS F  5 107 ? 36.969  66.156  156.485 1.00 288.91 ?  107 LYS F C   1 
ATOM   12227 O O   . LYS F  5 107 ? 36.000  66.143  157.251 1.00 287.53 ?  107 LYS F O   1 
ATOM   12228 C CB  . LYS F  5 107 ? 36.288  66.132  154.083 1.00 295.68 ?  107 LYS F CB  1 
ATOM   12229 C CG  . LYS F  5 107 ? 36.382  65.497  152.710 1.00 297.00 ?  107 LYS F CG  1 
ATOM   12230 C CD  . LYS F  5 107 ? 35.602  66.315  151.696 1.00 313.75 ?  107 LYS F CD  1 
ATOM   12231 C CE  . LYS F  5 107 ? 36.394  67.544  151.266 1.00 327.43 ?  107 LYS F CE  1 
ATOM   12232 N NZ  . LYS F  5 107 ? 36.480  67.697  149.787 1.00 339.89 1  107 LYS F NZ  1 
ATOM   12233 N N   . ARG F  5 108 ? 38.067  66.870  156.718 1.00 296.41 ?  108 ARG F N   1 
ATOM   12234 C CA  . ARG F  5 108 ? 38.138  67.855  157.788 1.00 300.89 ?  108 ARG F CA  1 
ATOM   12235 C C   . ARG F  5 108 ? 39.041  68.991  157.332 1.00 310.14 ?  108 ARG F C   1 
ATOM   12236 O O   . ARG F  5 108 ? 39.593  68.968  156.228 1.00 312.79 ?  108 ARG F O   1 
ATOM   12237 C CB  . ARG F  5 108 ? 38.662  67.249  159.093 1.00 293.44 ?  108 ARG F CB  1 
ATOM   12238 C CG  . ARG F  5 108 ? 39.993  66.531  158.952 1.00 288.44 ?  108 ARG F CG  1 
ATOM   12239 C CD  . ARG F  5 108 ? 40.799  66.591  160.242 1.00 286.16 ?  108 ARG F CD  1 
ATOM   12240 N NE  . ARG F  5 108 ? 41.248  67.951  160.533 1.00 295.36 ?  108 ARG F NE  1 
ATOM   12241 C CZ  . ARG F  5 108 ? 41.532  68.406  161.749 1.00 296.43 ?  108 ARG F CZ  1 
ATOM   12242 N NH1 . ARG F  5 108 ? 41.397  67.617  162.805 1.00 288.95 1  108 ARG F NH1 1 
ATOM   12243 N NH2 . ARG F  5 108 ? 41.939  69.658  161.909 1.00 305.39 ?  108 ARG F NH2 1 
ATOM   12244 N N   . THR F  5 109 ? 39.179  69.997  158.190 1.00 307.15 ?  109 THR F N   1 
ATOM   12245 C CA  . THR F  5 109 ? 40.047  71.117  157.872 1.00 316.26 ?  109 THR F CA  1 
ATOM   12246 C C   . THR F  5 109 ? 41.502  70.661  157.824 1.00 313.10 ?  109 THR F C   1 
ATOM   12247 O O   . THR F  5 109 ? 41.907  69.722  158.514 1.00 304.55 ?  109 THR F O   1 
ATOM   12248 C CB  . THR F  5 109 ? 39.883  72.229  158.908 1.00 322.27 ?  109 THR F CB  1 
ATOM   12249 O OG1 . THR F  5 109 ? 40.264  71.739  160.200 1.00 315.62 ?  109 THR F OG1 1 
ATOM   12250 C CG2 . THR F  5 109 ? 38.432  72.693  158.967 1.00 326.01 ?  109 THR F CG2 1 
ATOM   12251 N N   . VAL F  5 110 ? 42.289  71.338  156.986 1.00 315.47 ?  110 VAL F N   1 
ATOM   12252 C CA  . VAL F  5 110 ? 43.704  71.014  156.862 1.00 313.08 ?  110 VAL F CA  1 
ATOM   12253 C C   . VAL F  5 110 ? 44.402  71.251  158.194 1.00 311.76 ?  110 VAL F C   1 
ATOM   12254 O O   . VAL F  5 110 ? 44.192  72.281  158.848 1.00 315.68 ?  110 VAL F O   1 
ATOM   12255 C CB  . VAL F  5 110 ? 44.331  71.834  155.725 1.00 317.94 ?  110 VAL F CB  1 
ATOM   12256 C CG1 . VAL F  5 110 ? 45.830  71.686  155.737 1.00 316.33 ?  110 VAL F CG1 1 
ATOM   12257 C CG2 . VAL F  5 110 ? 43.759  71.391  154.387 1.00 318.65 ?  110 VAL F CG2 1 
ATOM   12258 N N   . ALA F  5 111 ? 45.241  70.298  158.603 1.00 326.73 ?  111 ALA F N   1 
ATOM   12259 C CA  . ALA F  5 111 ? 46.011  70.394  159.840 1.00 325.19 ?  111 ALA F CA  1 
ATOM   12260 C C   . ALA F  5 111 ? 47.452  69.983  159.574 1.00 323.62 ?  111 ALA F C   1 
ATOM   12261 O O   . ALA F  5 111 ? 47.703  68.863  159.118 1.00 316.59 ?  111 ALA F O   1 
ATOM   12262 C CB  . ALA F  5 111 ? 45.398  69.523  160.941 1.00 316.31 ?  111 ALA F CB  1 
ATOM   12263 N N   . ALA F  5 112 ? 48.392  70.885  159.854 1.00 320.12 ?  112 ALA F N   1 
ATOM   12264 C CA  . ALA F  5 112 ? 49.800  70.573  159.673 1.00 318.53 ?  112 ALA F CA  1 
ATOM   12265 C C   . ALA F  5 112 ? 50.291  69.606  160.753 1.00 312.98 ?  112 ALA F C   1 
ATOM   12266 O O   . ALA F  5 112 ? 49.825  69.646  161.895 1.00 311.55 ?  112 ALA F O   1 
ATOM   12267 C CB  . ALA F  5 112 ? 50.632  71.851  159.707 1.00 323.88 ?  112 ALA F CB  1 
ATOM   12268 N N   . PRO F  5 113 ? 51.235  68.728  160.414 1.00 313.01 ?  113 PRO F N   1 
ATOM   12269 C CA  . PRO F  5 113 ? 51.788  67.808  161.414 1.00 305.16 ?  113 PRO F CA  1 
ATOM   12270 C C   . PRO F  5 113 ? 52.712  68.503  162.401 1.00 309.34 ?  113 PRO F C   1 
ATOM   12271 O O   . PRO F  5 113 ? 53.410  69.463  162.065 1.00 314.07 ?  113 PRO F O   1 
ATOM   12272 C CB  . PRO F  5 113 ? 52.567  66.794  160.569 1.00 301.19 ?  113 PRO F CB  1 
ATOM   12273 C CG  . PRO F  5 113 ? 52.954  67.558  159.347 1.00 309.67 ?  113 PRO F CG  1 
ATOM   12274 C CD  . PRO F  5 113 ? 51.825  68.516  159.080 1.00 313.88 ?  113 PRO F CD  1 
ATOM   12275 N N   . SER F  5 114 ? 52.714  68.002  163.635 1.00 293.28 ?  114 SER F N   1 
ATOM   12276 C CA  . SER F  5 114 ? 53.776  68.327  164.575 1.00 295.93 ?  114 SER F CA  1 
ATOM   12277 C C   . SER F  5 114 ? 54.863  67.278  164.390 1.00 290.85 ?  114 SER F C   1 
ATOM   12278 O O   . SER F  5 114 ? 54.574  66.076  164.397 1.00 282.05 ?  114 SER F O   1 
ATOM   12279 C CB  . SER F  5 114 ? 53.263  68.322  166.016 1.00 292.97 ?  114 SER F CB  1 
ATOM   12280 O OG  . SER F  5 114 ? 52.254  69.296  166.212 1.00 298.03 ?  114 SER F OG  1 
ATOM   12281 N N   . VAL F  5 115 ? 56.108  67.720  164.232 1.00 284.29 ?  115 VAL F N   1 
ATOM   12282 C CA  . VAL F  5 115 ? 57.192  66.826  163.845 1.00 281.43 ?  115 VAL F CA  1 
ATOM   12283 C C   . VAL F  5 115 ? 58.202  66.725  164.979 1.00 280.57 ?  115 VAL F C   1 
ATOM   12284 O O   . VAL F  5 115 ? 58.599  67.739  165.568 1.00 284.49 ?  115 VAL F O   1 
ATOM   12285 C CB  . VAL F  5 115 ? 57.868  67.304  162.549 1.00 285.06 ?  115 VAL F CB  1 
ATOM   12286 C CG1 . VAL F  5 115 ? 58.908  66.295  162.088 1.00 282.19 ?  115 VAL F CG1 1 
ATOM   12287 C CG2 . VAL F  5 115 ? 56.820  67.545  161.467 1.00 286.64 ?  115 VAL F CG2 1 
ATOM   12288 N N   . PHE F  5 116 ? 58.605  65.494  165.282 1.00 275.46 ?  116 PHE F N   1 
ATOM   12289 C CA  . PHE F  5 116 ? 59.560  65.182  166.331 1.00 274.31 ?  116 PHE F CA  1 
ATOM   12290 C C   . PHE F  5 116 ? 60.539  64.151  165.792 1.00 270.65 ?  116 PHE F C   1 
ATOM   12291 O O   . PHE F  5 116 ? 60.138  63.231  165.073 1.00 264.58 ?  116 PHE F O   1 
ATOM   12292 C CB  . PHE F  5 116 ? 58.852  64.690  167.595 1.00 268.03 ?  116 PHE F CB  1 
ATOM   12293 C CG  . PHE F  5 116 ? 57.783  65.630  168.087 1.00 271.37 ?  116 PHE F CG  1 
ATOM   12294 C CD1 . PHE F  5 116 ? 56.488  65.555  167.594 1.00 268.59 ?  116 PHE F CD1 1 
ATOM   12295 C CD2 . PHE F  5 116 ? 58.080  66.609  169.021 1.00 277.77 ?  116 PHE F CD2 1 
ATOM   12296 C CE1 . PHE F  5 116 ? 55.507  66.422  168.040 1.00 272.07 ?  116 PHE F CE1 1 
ATOM   12297 C CE2 . PHE F  5 116 ? 57.103  67.480  169.470 1.00 281.31 ?  116 PHE F CE2 1 
ATOM   12298 C CZ  . PHE F  5 116 ? 55.815  67.387  168.978 1.00 278.47 ?  116 PHE F CZ  1 
ATOM   12299 N N   . ILE F  5 117 ? 61.815  64.295  166.135 1.00 274.22 ?  117 ILE F N   1 
ATOM   12300 C CA  . ILE F  5 117 ? 62.824  63.298  165.798 1.00 270.89 ?  117 ILE F CA  1 
ATOM   12301 C C   . ILE F  5 117 ? 63.378  62.720  167.093 1.00 267.06 ?  117 ILE F C   1 
ATOM   12302 O O   . ILE F  5 117 ? 63.570  63.441  168.080 1.00 270.90 ?  117 ILE F O   1 
ATOM   12303 C CB  . ILE F  5 117 ? 63.945  63.884  164.910 1.00 276.05 ?  117 ILE F CB  1 
ATOM   12304 C CG1 . ILE F  5 117 ? 64.873  62.772  164.413 1.00 274.68 ?  117 ILE F CG1 1 
ATOM   12305 C CG2 . ILE F  5 117 ? 64.728  64.962  165.649 1.00 280.53 ?  117 ILE F CG2 1 
ATOM   12306 C CD1 . ILE F  5 117 ? 65.774  63.191  163.271 1.00 279.07 ?  117 ILE F CD1 1 
ATOM   12307 N N   . PHE F  5 118 ? 63.596  61.408  167.096 1.00 275.46 ?  118 PHE F N   1 
ATOM   12308 C CA  . PHE F  5 118 ? 64.135  60.697  168.245 1.00 271.91 ?  118 PHE F CA  1 
ATOM   12309 C C   . PHE F  5 118 ? 65.409  59.963  167.857 1.00 273.03 ?  118 PHE F C   1 
ATOM   12310 O O   . PHE F  5 118 ? 65.365  59.072  166.989 1.00 270.31 ?  118 PHE F O   1 
ATOM   12311 C CB  . PHE F  5 118 ? 63.090  59.729  168.781 1.00 263.48 ?  118 PHE F CB  1 
ATOM   12312 C CG  . PHE F  5 118 ? 61.810  60.402  169.158 1.00 262.53 ?  118 PHE F CG  1 
ATOM   12313 C CD1 . PHE F  5 118 ? 61.676  61.012  170.389 1.00 264.23 ?  118 PHE F CD1 1 
ATOM   12314 C CD2 . PHE F  5 118 ? 60.750  60.453  168.268 1.00 260.56 ?  118 PHE F CD2 1 
ATOM   12315 C CE1 . PHE F  5 118 ? 60.504  61.644  170.738 1.00 265.04 ?  118 PHE F CE1 1 
ATOM   12316 C CE2 . PHE F  5 118 ? 59.572  61.085  168.610 1.00 260.03 ?  118 PHE F CE2 1 
ATOM   12317 C CZ  . PHE F  5 118 ? 59.450  61.681  169.849 1.00 262.85 ?  118 PHE F CZ  1 
ATOM   12318 N N   . PRO F  5 119 ? 66.549  60.289  168.455 1.00 270.23 ?  119 PRO F N   1 
ATOM   12319 C CA  . PRO F  5 119 ? 67.766  59.518  168.206 1.00 271.15 ?  119 PRO F CA  1 
ATOM   12320 C C   . PRO F  5 119 ? 67.643  58.116  168.771 1.00 263.52 ?  119 PRO F C   1 
ATOM   12321 O O   . PRO F  5 119 ? 66.768  57.848  169.609 1.00 258.26 ?  119 PRO F O   1 
ATOM   12322 C CB  . PRO F  5 119 ? 68.845  60.319  168.949 1.00 277.13 ?  119 PRO F CB  1 
ATOM   12323 C CG  . PRO F  5 119 ? 68.096  61.016  170.036 1.00 276.90 ?  119 PRO F CG  1 
ATOM   12324 C CD  . PRO F  5 119 ? 66.749  61.342  169.464 1.00 274.12 ?  119 PRO F CD  1 
ATOM   12325 N N   . PRO F  5 120 ? 68.490  57.190  168.330 1.00 277.71 ?  120 PRO F N   1 
ATOM   12326 C CA  . PRO F  5 120 ? 68.513  55.864  168.951 1.00 271.64 ?  120 PRO F CA  1 
ATOM   12327 C C   . PRO F  5 120 ? 69.004  55.932  170.386 1.00 274.85 ?  120 PRO F C   1 
ATOM   12328 O O   . PRO F  5 120 ? 69.859  56.745  170.745 1.00 281.25 ?  120 PRO F O   1 
ATOM   12329 C CB  . PRO F  5 120 ? 69.481  55.071  168.066 1.00 274.87 ?  120 PRO F CB  1 
ATOM   12330 C CG  . PRO F  5 120 ? 70.333  56.110  167.416 1.00 284.47 ?  120 PRO F CG  1 
ATOM   12331 C CD  . PRO F  5 120 ? 69.437  57.292  167.207 1.00 285.43 ?  120 PRO F CD  1 
ATOM   12332 N N   . SER F  5 121 ? 68.444  55.064  171.214 1.00 272.55 ?  121 SER F N   1 
ATOM   12333 C CA  . SER F  5 121 ? 68.905  54.962  172.586 1.00 273.59 ?  121 SER F CA  1 
ATOM   12334 C C   . SER F  5 121 ? 70.302  54.353  172.634 1.00 277.95 ?  121 SER F C   1 
ATOM   12335 O O   . SER F  5 121 ? 70.718  53.617  171.734 1.00 278.14 ?  121 SER F O   1 
ATOM   12336 C CB  . SER F  5 121 ? 67.934  54.134  173.417 1.00 266.44 ?  121 SER F CB  1 
ATOM   12337 O OG  . SER F  5 121 ? 67.909  52.796  172.967 1.00 261.98 ?  121 SER F OG  1 
ATOM   12338 N N   . ASP F  5 122 ? 71.033  54.681  173.701 1.00 280.81 ?  122 ASP F N   1 
ATOM   12339 C CA  . ASP F  5 122 ? 72.338  54.066  173.910 1.00 285.98 ?  122 ASP F CA  1 
ATOM   12340 C C   . ASP F  5 122 ? 72.209  52.563  174.108 1.00 280.83 ?  122 ASP F C   1 
ATOM   12341 O O   . ASP F  5 122 ? 73.110  51.806  173.730 1.00 282.57 ?  122 ASP F O   1 
ATOM   12342 C CB  . ASP F  5 122 ? 73.032  54.695  175.118 1.00 291.68 ?  122 ASP F CB  1 
ATOM   12343 C CG  . ASP F  5 122 ? 73.456  56.125  174.867 1.00 301.65 ?  122 ASP F CG  1 
ATOM   12344 O OD1 . ASP F  5 122 ? 73.569  56.516  173.687 1.00 301.42 ?  122 ASP F OD1 1 
ATOM   12345 O OD2 . ASP F  5 122 ? 73.689  56.854  175.854 1.00 307.60 -1 122 ASP F OD2 1 
ATOM   12346 N N   . GLU F  5 123 ? 71.098  52.116  174.698 1.00 289.40 ?  123 GLU F N   1 
ATOM   12347 C CA  . GLU F  5 123 ? 70.876  50.688  174.894 1.00 284.45 ?  123 GLU F CA  1 
ATOM   12348 C C   . GLU F  5 123 ? 70.830  49.947  173.566 1.00 282.18 ?  123 GLU F C   1 
ATOM   12349 O O   . GLU F  5 123 ? 71.398  48.856  173.433 1.00 281.95 ?  123 GLU F O   1 
ATOM   12350 C CB  . GLU F  5 123 ? 69.580  50.464  175.662 1.00 278.17 ?  123 GLU F CB  1 
ATOM   12351 C CG  . GLU F  5 123 ? 69.368  49.039  176.105 1.00 273.73 ?  123 GLU F CG  1 
ATOM   12352 C CD  . GLU F  5 123 ? 68.008  48.849  176.728 1.00 267.66 ?  123 GLU F CD  1 
ATOM   12353 O OE1 . GLU F  5 123 ? 67.314  49.862  176.944 1.00 267.42 ?  123 GLU F OE1 1 
ATOM   12354 O OE2 . GLU F  5 123 ? 67.625  47.691  176.979 1.00 264.09 -1 123 GLU F OE2 1 
ATOM   12355 N N   . GLN F  5 124 ? 70.149  50.519  172.571 1.00 286.25 ?  124 GLN F N   1 
ATOM   12356 C CA  . GLN F  5 124 ? 70.073  49.863  171.272 1.00 284.19 ?  124 GLN F CA  1 
ATOM   12357 C C   . GLN F  5 124 ? 71.436  49.850  170.604 1.00 293.07 ?  124 GLN F C   1 
ATOM   12358 O O   . GLN F  5 124 ? 71.812  48.863  169.961 1.00 293.72 ?  124 GLN F O   1 
ATOM   12359 C CB  . GLN F  5 124 ? 69.056  50.571  170.377 1.00 280.45 ?  124 GLN F CB  1 
ATOM   12360 C CG  . GLN F  5 124 ? 68.824  49.871  169.046 1.00 278.33 ?  124 GLN F CG  1 
ATOM   12361 C CD  . GLN F  5 124 ? 67.997  50.695  168.078 1.00 277.10 ?  124 GLN F CD  1 
ATOM   12362 O OE1 . GLN F  5 124 ? 67.845  51.906  168.244 1.00 280.59 ?  124 GLN F OE1 1 
ATOM   12363 N NE2 . GLN F  5 124 ? 67.466  50.040  167.053 1.00 274.44 ?  124 GLN F NE2 1 
ATOM   12364 N N   . LEU F  5 125 ? 72.179  50.948  170.732 1.00 283.79 ?  125 LEU F N   1 
ATOM   12365 C CA  . LEU F  5 125 ? 73.485  51.041  170.098 1.00 291.89 ?  125 LEU F CA  1 
ATOM   12366 C C   . LEU F  5 125 ? 74.428  49.948  170.595 1.00 295.01 ?  125 LEU F C   1 
ATOM   12367 O O   . LEU F  5 125 ? 75.266  49.457  169.831 1.00 300.93 ?  125 LEU F O   1 
ATOM   12368 C CB  . LEU F  5 125 ? 74.060  52.430  170.369 1.00 296.98 ?  125 LEU F CB  1 
ATOM   12369 C CG  . LEU F  5 125 ? 73.396  53.541  169.552 1.00 298.95 ?  125 LEU F CG  1 
ATOM   12370 C CD1 . LEU F  5 125 ? 73.817  54.920  170.043 1.00 310.08 ?  125 LEU F CD1 1 
ATOM   12371 C CD2 . LEU F  5 125 ? 73.716  53.369  168.084 1.00 303.41 ?  125 LEU F CD2 1 
ATOM   12372 N N   . LYS F  5 126 ? 74.318  49.572  171.874 1.00 283.27 ?  126 LYS F N   1 
ATOM   12373 C CA  . LYS F  5 126 ? 75.136  48.494  172.427 1.00 284.18 ?  126 LYS F CA  1 
ATOM   12374 C C   . LYS F  5 126 ? 74.937  47.178  171.685 1.00 280.39 ?  126 LYS F C   1 
ATOM   12375 O O   . LYS F  5 126 ? 75.855  46.352  171.630 1.00 286.05 ?  126 LYS F O   1 
ATOM   12376 C CB  . LYS F  5 126 ? 74.854  48.338  173.917 1.00 282.42 ?  126 LYS F CB  1 
ATOM   12377 C CG  . LYS F  5 126 ? 75.404  49.508  174.709 1.00 289.43 ?  126 LYS F CG  1 
ATOM   12378 C CD  . LYS F  5 126 ? 75.269  49.317  176.197 1.00 292.52 ?  126 LYS F CD  1 
ATOM   12379 C CE  . LYS F  5 126 ? 73.879  48.872  176.570 1.00 280.74 ?  126 LYS F CE  1 
ATOM   12380 N NZ  . LYS F  5 126 ? 73.736  48.893  178.047 1.00 285.32 1  126 LYS F NZ  1 
ATOM   12381 N N   . SER F  5 127 ? 73.752  46.959  171.121 1.00 301.22 ?  127 SER F N   1 
ATOM   12382 C CA  . SER F  5 127 ? 73.409  45.684  170.508 1.00 297.36 ?  127 SER F CA  1 
ATOM   12383 C C   . SER F  5 127 ? 73.812  45.613  169.043 1.00 301.51 ?  127 SER F C   1 
ATOM   12384 O O   . SER F  5 127 ? 73.703  44.541  168.438 1.00 302.65 ?  127 SER F O   1 
ATOM   12385 C CB  . SER F  5 127 ? 71.907  45.406  170.639 1.00 289.92 ?  127 SER F CB  1 
ATOM   12386 O OG  . SER F  5 127 ? 71.154  46.203  169.741 1.00 289.55 ?  127 SER F OG  1 
ATOM   12387 N N   . GLY F  5 128 ? 74.271  46.722  168.463 1.00 294.31 ?  128 GLY F N   1 
ATOM   12388 C CA  . GLY F  5 128 ? 74.798  46.739  167.114 1.00 299.16 ?  128 GLY F CA  1 
ATOM   12389 C C   . GLY F  5 128 ? 73.908  47.373  166.068 1.00 295.75 ?  128 GLY F C   1 
ATOM   12390 O O   . GLY F  5 128 ? 74.280  47.369  164.888 1.00 300.90 ?  128 GLY F O   1 
ATOM   12391 N N   . THR F  5 129 ? 72.752  47.916  166.444 1.00 283.11 ?  129 THR F N   1 
ATOM   12392 C CA  . THR F  5 129 ? 71.890  48.608  165.499 1.00 281.56 ?  129 THR F CA  1 
ATOM   12393 C C   . THR F  5 129 ? 71.502  49.972  166.053 1.00 276.84 ?  129 THR F C   1 
ATOM   12394 O O   . THR F  5 129 ? 71.535  50.210  167.264 1.00 274.95 ?  129 THR F O   1 
ATOM   12395 C CB  . THR F  5 129 ? 70.616  47.800  165.199 1.00 283.86 ?  129 THR F CB  1 
ATOM   12396 O OG1 . THR F  5 129 ? 69.821  47.698  166.387 1.00 282.65 ?  129 THR F OG1 1 
ATOM   12397 C CG2 . THR F  5 129 ? 70.965  46.402  164.715 1.00 288.84 ?  129 THR F CG2 1 
ATOM   12398 N N   . ALA F  5 130 ? 71.134  50.870  165.140 1.00 287.50 ?  130 ALA F N   1 
ATOM   12399 C CA  . ALA F  5 130 ? 70.680  52.214  165.477 1.00 284.15 ?  130 ALA F CA  1 
ATOM   12400 C C   . ALA F  5 130 ? 69.391  52.478  164.718 1.00 280.52 ?  130 ALA F C   1 
ATOM   12401 O O   . ALA F  5 130 ? 69.374  52.418  163.484 1.00 283.47 ?  130 ALA F O   1 
ATOM   12402 C CB  . ALA F  5 130 ? 71.737  53.263  165.122 1.00 288.56 ?  130 ALA F CB  1 
ATOM   12403 N N   . SER F  5 131 ? 68.319  52.769  165.447 1.00 278.28 ?  131 SER F N   1 
ATOM   12404 C CA  . SER F  5 131 ? 67.058  53.191  164.855 1.00 276.74 ?  131 SER F CA  1 
ATOM   12405 C C   . SER F  5 131 ? 66.806  54.664  165.140 1.00 276.07 ?  131 SER F C   1 
ATOM   12406 O O   . SER F  5 131 ? 66.850  55.094  166.297 1.00 273.23 ?  131 SER F O   1 
ATOM   12407 C CB  . SER F  5 131 ? 65.898  52.348  165.384 1.00 272.60 ?  131 SER F CB  1 
ATOM   12408 O OG  . SER F  5 131 ? 66.077  50.976  165.076 1.00 276.79 ?  131 SER F OG  1 
ATOM   12409 N N   . VAL F  5 132 ? 66.537  55.427  164.086 1.00 269.83 ?  132 VAL F N   1 
ATOM   12410 C CA  . VAL F  5 132 ? 66.202  56.841  164.189 1.00 266.36 ?  132 VAL F CA  1 
ATOM   12411 C C   . VAL F  5 132 ? 64.746  56.972  163.771 1.00 266.72 ?  132 VAL F C   1 
ATOM   12412 O O   . VAL F  5 132 ? 64.357  56.490  162.701 1.00 269.56 ?  132 VAL F O   1 
ATOM   12413 C CB  . VAL F  5 132 ? 67.121  57.707  163.311 1.00 265.75 ?  132 VAL F CB  1 
ATOM   12414 C CG1 . VAL F  5 132 ? 66.986  59.173  163.688 1.00 262.06 ?  132 VAL F CG1 1 
ATOM   12415 C CG2 . VAL F  5 132 ? 68.571  57.237  163.424 1.00 266.79 ?  132 VAL F CG2 1 
ATOM   12416 N N   . VAL F  5 133 ? 63.942  57.618  164.612 1.00 267.13 ?  133 VAL F N   1 
ATOM   12417 C CA  . VAL F  5 133 ? 62.502  57.712  164.407 1.00 267.46 ?  133 VAL F CA  1 
ATOM   12418 C C   . VAL F  5 133 ? 62.101  59.160  164.164 1.00 264.79 ?  133 VAL F C   1 
ATOM   12419 O O   . VAL F  5 133 ? 62.497  60.059  164.917 1.00 261.61 ?  133 VAL F O   1 
ATOM   12420 C CB  . VAL F  5 133 ? 61.742  57.133  165.612 1.00 267.02 ?  133 VAL F CB  1 
ATOM   12421 C CG1 . VAL F  5 133 ? 60.248  57.364  165.465 1.00 267.11 ?  133 VAL F CG1 1 
ATOM   12422 C CG2 . VAL F  5 133 ? 62.060  55.650  165.776 1.00 270.22 ?  133 VAL F CG2 1 
ATOM   12423 N N   . CYS F  5 134 ? 61.323  59.378  163.107 1.00 273.01 ?  134 CYS F N   1 
ATOM   12424 C CA  . CYS F  5 134 ? 60.696  60.657  162.805 1.00 271.17 ?  134 CYS F CA  1 
ATOM   12425 C C   . CYS F  5 134 ? 59.188  60.478  162.940 1.00 271.91 ?  134 CYS F C   1 
ATOM   12426 O O   . CYS F  5 134 ? 58.608  59.589  162.305 1.00 275.21 ?  134 CYS F O   1 
ATOM   12427 C CB  . CYS F  5 134 ? 61.083  61.133  161.406 1.00 272.67 ?  134 CYS F CB  1 
ATOM   12428 S SG  . CYS F  5 134 ? 60.562  62.804  161.010 1.00 270.58 ?  134 CYS F SG  1 
ATOM   12429 N N   . LEU F  5 135 ? 58.564  61.306  163.776 1.00 275.48 ?  135 LEU F N   1 
ATOM   12430 C CA  . LEU F  5 135 ? 57.133  61.245  164.050 1.00 275.81 ?  135 LEU F CA  1 
ATOM   12431 C C   . LEU F  5 135 ? 56.415  62.444  163.443 1.00 275.12 ?  135 LEU F C   1 
ATOM   12432 O O   . LEU F  5 135 ? 56.838  63.590  163.638 1.00 272.41 ?  135 LEU F O   1 
ATOM   12433 C CB  . LEU F  5 135 ? 56.870  61.189  165.556 1.00 273.25 ?  135 LEU F CB  1 
ATOM   12434 C CG  . LEU F  5 135 ? 55.425  61.445  165.987 1.00 272.73 ?  135 LEU F CG  1 
ATOM   12435 C CD1 . LEU F  5 135 ? 54.517  60.332  165.493 1.00 276.51 ?  135 LEU F CD1 1 
ATOM   12436 C CD2 . LEU F  5 135 ? 55.322  61.594  167.496 1.00 269.72 ?  135 LEU F CD2 1 
ATOM   12437 N N   . LEU F  5 136 ? 55.337  62.173  162.708 1.00 285.69 ?  136 LEU F N   1 
ATOM   12438 C CA  . LEU F  5 136 ? 54.412  63.183  162.199 1.00 289.15 ?  136 LEU F CA  1 
ATOM   12439 C C   . LEU F  5 136 ? 53.088  62.980  162.927 1.00 285.64 ?  136 LEU F C   1 
ATOM   12440 O O   . LEU F  5 136 ? 52.439  61.943  162.753 1.00 283.74 ?  136 LEU F O   1 
ATOM   12441 C CB  . LEU F  5 136 ? 54.227  63.052  160.688 1.00 294.21 ?  136 LEU F CB  1 
ATOM   12442 C CG  . LEU F  5 136 ? 55.324  63.472  159.703 1.00 299.53 ?  136 LEU F CG  1 
ATOM   12443 C CD1 . LEU F  5 136 ? 56.643  62.732  159.931 1.00 297.96 ?  136 LEU F CD1 1 
ATOM   12444 C CD2 . LEU F  5 136 ? 54.828  63.263  158.279 1.00 304.32 ?  136 LEU F CD2 1 
ATOM   12445 N N   . ASN F  5 137 ? 52.680  63.956  163.735 1.00 286.51 ?  137 ASN F N   1 
ATOM   12446 C CA  . ASN F  5 137 ? 51.518  63.799  164.602 1.00 282.83 ?  137 ASN F CA  1 
ATOM   12447 C C   . ASN F  5 137 ? 50.328  64.637  164.148 1.00 286.09 ?  137 ASN F C   1 
ATOM   12448 O O   . ASN F  5 137 ? 50.460  65.842  163.909 1.00 290.06 ?  137 ASN F O   1 
ATOM   12449 C CB  . ASN F  5 137 ? 51.873  64.165  166.043 1.00 279.26 ?  137 ASN F CB  1 
ATOM   12450 C CG  . ASN F  5 137 ? 51.077  63.370  167.048 1.00 276.97 ?  137 ASN F CG  1 
ATOM   12451 O OD1 . ASN F  5 137 ? 50.904  62.161  166.898 1.00 279.74 ?  137 ASN F OD1 1 
ATOM   12452 N ND2 . ASN F  5 137 ? 50.566  64.045  168.068 1.00 274.08 ?  137 ASN F ND2 1 
ATOM   12453 N N   . ASN F  5 138 ? 49.169  63.980  164.048 1.00 287.36 ?  138 ASN F N   1 
ATOM   12454 C CA  . ASN F  5 138 ? 47.848  64.600  163.907 1.00 289.48 ?  138 ASN F CA  1 
ATOM   12455 C C   . ASN F  5 138 ? 47.737  65.534  162.697 1.00 296.11 ?  138 ASN F C   1 
ATOM   12456 O O   . ASN F  5 138 ? 47.530  66.740  162.837 1.00 299.12 ?  138 ASN F O   1 
ATOM   12457 C CB  . ASN F  5 138 ? 47.476  65.348  165.192 1.00 287.52 ?  138 ASN F CB  1 
ATOM   12458 C CG  . ASN F  5 138 ? 47.299  64.422  166.374 1.00 281.49 ?  138 ASN F CG  1 
ATOM   12459 O OD1 . ASN F  5 138 ? 47.329  63.199  166.230 1.00 278.82 ?  138 ASN F OD1 1 
ATOM   12460 N ND2 . ASN F  5 138 ? 47.110  64.999  167.555 1.00 279.71 ?  138 ASN F ND2 1 
ATOM   12461 N N   . PHE F  5 139 ? 47.875  64.964  161.498 1.00 293.36 ?  139 PHE F N   1 
ATOM   12462 C CA  . PHE F  5 139 ? 47.810  65.757  160.276 1.00 300.15 ?  139 PHE F CA  1 
ATOM   12463 C C   . PHE F  5 139 ? 46.669  65.295  159.368 1.00 302.92 ?  139 PHE F C   1 
ATOM   12464 O O   . PHE F  5 139 ? 46.187  64.163  159.460 1.00 299.68 ?  139 PHE F O   1 
ATOM   12465 C CB  . PHE F  5 139 ? 49.139  65.724  159.500 1.00 302.84 ?  139 PHE F CB  1 
ATOM   12466 C CG  . PHE F  5 139 ? 49.567  64.351  159.067 1.00 300.79 ?  139 PHE F CG  1 
ATOM   12467 C CD1 . PHE F  5 139 ? 50.375  63.574  159.878 1.00 295.66 ?  139 PHE F CD1 1 
ATOM   12468 C CD2 . PHE F  5 139 ? 49.191  63.853  157.828 1.00 304.68 ?  139 PHE F CD2 1 
ATOM   12469 C CE1 . PHE F  5 139 ? 50.779  62.315  159.476 1.00 294.40 ?  139 PHE F CE1 1 
ATOM   12470 C CE2 . PHE F  5 139 ? 49.591  62.595  157.420 1.00 303.40 ?  139 PHE F CE2 1 
ATOM   12471 C CZ  . PHE F  5 139 ? 50.387  61.825  158.245 1.00 298.27 ?  139 PHE F CZ  1 
ATOM   12472 N N   . TYR F  5 140 ? 46.244  66.205  158.490 1.00 297.16 ?  140 TYR F N   1 
ATOM   12473 C CA  . TYR F  5 140 ? 45.264  65.945  157.424 1.00 301.52 ?  140 TYR F CA  1 
ATOM   12474 C C   . TYR F  5 140 ? 45.519  66.879  156.240 1.00 309.45 ?  140 TYR F C   1 
ATOM   12475 O O   . TYR F  5 140 ? 45.828  68.054  156.439 1.00 312.21 ?  140 TYR F O   1 
ATOM   12476 C CB  . TYR F  5 140 ? 43.821  66.117  157.923 1.00 300.86 ?  140 TYR F CB  1 
ATOM   12477 C CG  . TYR F  5 140 ? 42.764  65.773  156.884 1.00 305.35 ?  140 TYR F CG  1 
ATOM   12478 C CD1 . TYR F  5 140 ? 42.279  66.746  156.013 1.00 312.85 ?  140 TYR F CD1 1 
ATOM   12479 C CD2 . TYR F  5 140 ? 42.274  64.479  156.753 1.00 302.68 ?  140 TYR F CD2 1 
ATOM   12480 C CE1 . TYR F  5 140 ? 41.330  66.448  155.061 1.00 317.51 ?  140 TYR F CE1 1 
ATOM   12481 C CE2 . TYR F  5 140 ? 41.322  64.172  155.797 1.00 307.27 ?  140 TYR F CE2 1 
ATOM   12482 C CZ  . TYR F  5 140 ? 40.856  65.162  154.956 1.00 314.67 ?  140 TYR F CZ  1 
ATOM   12483 O OH  . TYR F  5 140 ? 39.911  64.875  154.002 1.00 319.73 ?  140 TYR F OH  1 
ATOM   12484 N N   . PRO F  5 141 ? 45.377  66.374  155.000 1.00 308.75 ?  141 PRO F N   1 
ATOM   12485 C CA  . PRO F  5 141 ? 45.025  65.016  154.558 1.00 307.02 ?  141 PRO F CA  1 
ATOM   12486 C C   . PRO F  5 141 ? 46.161  63.998  154.692 1.00 302.91 ?  141 PRO F C   1 
ATOM   12487 O O   . PRO F  5 141 ? 47.252  64.341  155.150 1.00 301.35 ?  141 PRO F O   1 
ATOM   12488 C CB  . PRO F  5 141 ? 44.652  65.215  153.087 1.00 315.00 ?  141 PRO F CB  1 
ATOM   12489 C CG  . PRO F  5 141 ? 45.416  66.401  152.667 1.00 320.13 ?  141 PRO F CG  1 
ATOM   12490 C CD  . PRO F  5 141 ? 45.489  67.303  153.862 1.00 317.01 ?  141 PRO F CD  1 
ATOM   12491 N N   . ARG F  5 142 ? 45.887  62.753  154.289 1.00 308.59 ?  142 ARG F N   1 
ATOM   12492 C CA  . ARG F  5 142 ? 46.831  61.660  154.513 1.00 304.45 ?  142 ARG F CA  1 
ATOM   12493 C C   . ARG F  5 142 ? 48.135  61.836  153.747 1.00 307.90 ?  142 ARG F C   1 
ATOM   12494 O O   . ARG F  5 142 ? 49.182  61.357  154.200 1.00 304.48 ?  142 ARG F O   1 
ATOM   12495 C CB  . ARG F  5 142 ? 46.199  60.324  154.116 1.00 303.68 ?  142 ARG F CB  1 
ATOM   12496 C CG  . ARG F  5 142 ? 46.953  59.099  154.627 1.00 302.11 ?  142 ARG F CG  1 
ATOM   12497 C CD  . ARG F  5 142 ? 46.323  57.809  154.120 1.00 307.37 ?  142 ARG F CD  1 
ATOM   12498 N NE  . ARG F  5 142 ? 46.876  56.626  154.772 1.00 307.29 ?  142 ARG F NE  1 
ATOM   12499 C CZ  . ARG F  5 142 ? 47.956  55.977  154.344 1.00 308.21 ?  142 ARG F CZ  1 
ATOM   12500 N NH1 . ARG F  5 142 ? 48.609  56.406  153.273 1.00 309.08 1  142 ARG F NH1 1 
ATOM   12501 N NH2 . ARG F  5 142 ? 48.391  54.906  154.994 1.00 308.35 ?  142 ARG F NH2 1 
ATOM   12502 N N   . GLU F  5 143 ? 48.106  62.502  152.596 1.00 308.27 ?  143 GLU F N   1 
ATOM   12503 C CA  . GLU F  5 143 ? 49.300  62.552  151.763 1.00 312.27 ?  143 GLU F CA  1 
ATOM   12504 C C   . GLU F  5 143 ? 50.417  63.304  152.476 1.00 310.48 ?  143 GLU F C   1 
ATOM   12505 O O   . GLU F  5 143 ? 50.256  64.469  152.852 1.00 311.72 ?  143 GLU F O   1 
ATOM   12506 C CB  . GLU F  5 143 ? 48.975  63.216  150.425 1.00 320.83 ?  143 GLU F CB  1 
ATOM   12507 C CG  . GLU F  5 143 ? 50.200  63.600  149.612 1.00 325.82 ?  143 GLU F CG  1 
ATOM   12508 C CD  . GLU F  5 143 ? 51.058  62.399  149.238 1.00 324.70 ?  143 GLU F CD  1 
ATOM   12509 O OE1 . GLU F  5 143 ? 50.514  61.277  149.140 1.00 322.66 ?  143 GLU F OE1 1 
ATOM   12510 O OE2 . GLU F  5 143 ? 52.279  62.576  149.046 1.00 326.22 -1 143 GLU F OE2 1 
ATOM   12511 N N   . ALA F  5 144 ? 51.552  62.630  152.659 1.00 314.53 ?  144 ALA F N   1 
ATOM   12512 C CA  . ALA F  5 144 ? 52.725  63.223  153.284 1.00 313.18 ?  144 ALA F CA  1 
ATOM   12513 C C   . ALA F  5 144 ? 53.964  62.523  152.747 1.00 314.76 ?  144 ALA F C   1 
ATOM   12514 O O   . ALA F  5 144 ? 53.925  61.335  152.417 1.00 313.83 ?  144 ALA F O   1 
ATOM   12515 C CB  . ALA F  5 144 ? 52.665  63.121  154.813 1.00 305.62 ?  144 ALA F CB  1 
ATOM   12516 N N   . LYS F  5 145 ? 55.065  63.266  152.660 1.00 315.32 ?  145 LYS F N   1 
ATOM   12517 C CA  . LYS F  5 145 ? 56.344  62.720  152.224 1.00 316.17 ?  145 LYS F CA  1 
ATOM   12518 C C   . LYS F  5 145 ? 57.391  62.919  153.311 1.00 311.62 ?  145 LYS F C   1 
ATOM   12519 O O   . LYS F  5 145 ? 57.553  64.031  153.825 1.00 309.47 ?  145 LYS F O   1 
ATOM   12520 C CB  . LYS F  5 145 ? 56.790  63.371  150.913 1.00 320.01 ?  145 LYS F CB  1 
ATOM   12521 C CG  . LYS F  5 145 ? 58.123  62.877  150.398 1.00 323.71 ?  145 LYS F CG  1 
ATOM   12522 C CD  . LYS F  5 145 ? 58.238  63.117  148.904 1.00 332.80 ?  145 LYS F CD  1 
ATOM   12523 C CE  . LYS F  5 145 ? 58.334  64.596  148.572 1.00 334.77 ?  145 LYS F CE  1 
ATOM   12524 N NZ  . LYS F  5 145 ? 58.738  64.808  147.153 1.00 342.53 1  145 LYS F NZ  1 
ATOM   12525 N N   . VAL F  5 146 ? 58.097  61.843  153.658 1.00 319.69 ?  146 VAL F N   1 
ATOM   12526 C CA  . VAL F  5 146 ? 59.203  61.881  154.612 1.00 316.78 ?  146 VAL F CA  1 
ATOM   12527 C C   . VAL F  5 146 ? 60.467  61.416  153.899 1.00 318.86 ?  146 VAL F C   1 
ATOM   12528 O O   . VAL F  5 146 ? 60.492  60.319  153.326 1.00 324.30 ?  146 VAL F O   1 
ATOM   12529 C CB  . VAL F  5 146 ? 58.924  61.008  155.847 1.00 311.16 ?  146 VAL F CB  1 
ATOM   12530 C CG1 . VAL F  5 146 ? 60.068  61.112  156.839 1.00 308.29 ?  146 VAL F CG1 1 
ATOM   12531 C CG2 . VAL F  5 146 ? 57.614  61.410  156.506 1.00 306.42 ?  146 VAL F CG2 1 
ATOM   12532 N N   . GLN F  5 147 ? 61.509  62.244  153.934 1.00 306.72 ?  147 GLN F N   1 
ATOM   12533 C CA  . GLN F  5 147 ? 62.800  61.922  153.340 1.00 308.46 ?  147 GLN F CA  1 
ATOM   12534 C C   . GLN F  5 147 ? 63.878  61.993  154.413 1.00 305.04 ?  147 GLN F C   1 
ATOM   12535 O O   . GLN F  5 147 ? 63.924  62.956  155.186 1.00 302.22 ?  147 GLN F O   1 
ATOM   12536 C CB  . GLN F  5 147 ? 63.125  62.877  152.188 1.00 311.55 ?  147 GLN F CB  1 
ATOM   12537 C CG  . GLN F  5 147 ? 62.110  62.832  151.057 1.00 321.33 ?  147 GLN F CG  1 
ATOM   12538 C CD  . GLN F  5 147 ? 62.589  63.536  149.806 1.00 328.48 ?  147 GLN F CD  1 
ATOM   12539 O OE1 . GLN F  5 147 ? 63.756  63.432  149.430 1.00 335.10 ?  147 GLN F OE1 1 
ATOM   12540 N NE2 . GLN F  5 147 ? 61.685  64.252  149.147 1.00 335.55 ?  147 GLN F NE2 1 
ATOM   12541 N N   . TRP F  5 148 ? 64.740  60.977  154.459 1.00 299.67 ?  148 TRP F N   1 
ATOM   12542 C CA  . TRP F  5 148 ? 65.861  60.925  155.389 1.00 297.15 ?  148 TRP F CA  1 
ATOM   12543 C C   . TRP F  5 148 ? 67.134  61.425  154.717 1.00 299.09 ?  148 TRP F C   1 
ATOM   12544 O O   . TRP F  5 148 ? 67.417  61.077  153.567 1.00 302.93 ?  148 TRP F O   1 
ATOM   12545 C CB  . TRP F  5 148 ? 66.070  59.496  155.897 1.00 296.97 ?  148 TRP F CB  1 
ATOM   12546 C CG  . TRP F  5 148 ? 65.050  59.044  156.898 1.00 294.23 ?  148 TRP F CG  1 
ATOM   12547 C CD1 . TRP F  5 148 ? 63.916  58.322  156.653 1.00 291.92 ?  148 TRP F CD1 1 
ATOM   12548 C CD2 . TRP F  5 148 ? 65.108  59.231  158.317 1.00 289.11 ?  148 TRP F CD2 1 
ATOM   12549 N NE1 . TRP F  5 148 ? 63.246  58.082  157.831 1.00 285.69 ?  148 TRP F NE1 1 
ATOM   12550 C CE2 . TRP F  5 148 ? 63.961  58.626  158.867 1.00 283.87 ?  148 TRP F CE2 1 
ATOM   12551 C CE3 . TRP F  5 148 ? 66.013  59.864  159.174 1.00 287.59 ?  148 TRP F CE3 1 
ATOM   12552 C CZ2 . TRP F  5 148 ? 63.696  58.636  160.235 1.00 278.43 ?  148 TRP F CZ2 1 
ATOM   12553 C CZ3 . TRP F  5 148 ? 65.749  59.874  160.529 1.00 283.49 ?  148 TRP F CZ3 1 
ATOM   12554 C CH2 . TRP F  5 148 ? 64.600  59.264  161.047 1.00 278.34 ?  148 TRP F CH2 1 
ATOM   12555 N N   . LYS F  5 149 ? 67.900  62.241  155.441 1.00 294.74 ?  149 LYS F N   1 
ATOM   12556 C CA  . LYS F  5 149 ? 69.200  62.716  154.983 1.00 297.16 ?  149 LYS F CA  1 
ATOM   12557 C C   . LYS F  5 149 ? 70.266  62.424  156.030 1.00 294.68 ?  149 LYS F C   1 
ATOM   12558 O O   . LYS F  5 149 ? 70.080  62.740  157.211 1.00 291.57 ?  149 LYS F O   1 
ATOM   12559 C CB  . LYS F  5 149 ? 69.137  64.216  154.682 1.00 298.00 ?  149 LYS F CB  1 
ATOM   12560 C CG  . LYS F  5 149 ? 68.233  64.537  153.506 1.00 302.80 ?  149 LYS F CG  1 
ATOM   12561 C CD  . LYS F  5 149 ? 67.899  66.012  153.428 1.00 304.68 ?  149 LYS F CD  1 
ATOM   12562 C CE  . LYS F  5 149 ? 66.885  66.265  152.329 1.00 312.04 ?  149 LYS F CE  1 
ATOM   12563 N NZ  . LYS F  5 149 ? 66.558  67.709  152.198 1.00 312.01 1  149 LYS F NZ  1 
ATOM   12564 N N   . VAL F  5 150 ? 71.370  61.812  155.603 1.00 290.60 ?  150 VAL F N   1 
ATOM   12565 C CA  . VAL F  5 150 ? 72.509  61.527  156.472 1.00 289.52 ?  150 VAL F CA  1 
ATOM   12566 C C   . VAL F  5 150 ? 73.746  62.204  155.883 1.00 291.90 ?  150 VAL F C   1 
ATOM   12567 O O   . VAL F  5 150 ? 74.231  61.803  154.817 1.00 295.61 ?  150 VAL F O   1 
ATOM   12568 C CB  . VAL F  5 150 ? 72.723  60.017  156.640 1.00 290.71 ?  150 VAL F CB  1 
ATOM   12569 C CG1 . VAL F  5 150 ? 73.886  59.751  157.554 1.00 289.90 ?  150 VAL F CG1 1 
ATOM   12570 C CG2 . VAL F  5 150 ? 71.458  59.364  157.183 1.00 288.69 ?  150 VAL F CG2 1 
ATOM   12571 N N   . ASP F  5 151 ? 74.264  63.218  156.582 1.00 287.76 ?  151 ASP F N   1 
ATOM   12572 C CA  . ASP F  5 151 ? 75.320  64.105  156.071 1.00 289.13 ?  151 ASP F CA  1 
ATOM   12573 C C   . ASP F  5 151 ? 74.974  64.683  154.700 1.00 289.85 ?  151 ASP F C   1 
ATOM   12574 O O   . ASP F  5 151 ? 75.772  64.647  153.761 1.00 289.83 ?  151 ASP F O   1 
ATOM   12575 C CB  . ASP F  5 151 ? 76.685  63.416  156.043 1.00 296.07 ?  151 ASP F CB  1 
ATOM   12576 C CG  . ASP F  5 151 ? 77.298  63.291  157.420 1.00 294.49 ?  151 ASP F CG  1 
ATOM   12577 O OD1 . ASP F  5 151 ? 76.958  64.113  158.298 1.00 290.15 ?  151 ASP F OD1 1 
ATOM   12578 O OD2 . ASP F  5 151 ? 78.144  62.395  157.614 1.00 301.46 -1 151 ASP F OD2 1 
ATOM   12579 N N   . ASN F  5 152 ? 73.758  65.217  154.595 1.00 290.94 ?  152 ASN F N   1 
ATOM   12580 C CA  . ASN F  5 152 ? 73.225  65.825  153.377 1.00 289.98 ?  152 ASN F CA  1 
ATOM   12581 C C   . ASN F  5 152 ? 73.183  64.864  152.186 1.00 295.44 ?  152 ASN F C   1 
ATOM   12582 O O   . ASN F  5 152 ? 73.128  65.311  151.035 1.00 299.47 ?  152 ASN F O   1 
ATOM   12583 C CB  . ASN F  5 152 ? 74.022  67.082  153.006 1.00 291.42 ?  152 ASN F CB  1 
ATOM   12584 C CG  . ASN F  5 152 ? 73.720  68.255  153.920 1.00 285.47 ?  152 ASN F CG  1 
ATOM   12585 O OD1 . ASN F  5 152 ? 72.627  68.820  153.889 1.00 283.30 ?  152 ASN F OD1 1 
ATOM   12586 N ND2 . ASN F  5 152 ? 74.688  68.613  154.756 1.00 288.13 ?  152 ASN F ND2 1 
ATOM   12587 N N   . ALA F  5 153 ? 73.213  63.554  152.424 1.00 283.65 ?  153 ALA F N   1 
ATOM   12588 C CA  . ALA F  5 153 ? 73.054  62.554  151.373 1.00 287.15 ?  153 ALA F CA  1 
ATOM   12589 C C   . ALA F  5 153 ? 71.666  61.942  151.500 1.00 287.93 ?  153 ALA F C   1 
ATOM   12590 O O   . ALA F  5 153 ? 71.306  61.434  152.568 1.00 286.74 ?  153 ALA F O   1 
ATOM   12591 C CB  . ALA F  5 153 ? 74.134  61.475  151.458 1.00 288.76 ?  153 ALA F CB  1 
ATOM   12592 N N   . LEU F  5 154 ? 70.893  61.986  150.417 1.00 291.59 ?  154 LEU F N   1 
ATOM   12593 C CA  . LEU F  5 154 ? 69.549  61.423  150.437 1.00 289.61 ?  154 LEU F CA  1 
ATOM   12594 C C   . LEU F  5 154 ? 69.595  59.905  150.577 1.00 295.65 ?  154 LEU F C   1 
ATOM   12595 O O   . LEU F  5 154 ? 70.345  59.225  149.869 1.00 299.40 ?  154 LEU F O   1 
ATOM   12596 C CB  . LEU F  5 154 ? 68.792  61.817  149.169 1.00 287.99 ?  154 LEU F CB  1 
ATOM   12597 C CG  . LEU F  5 154 ? 67.334  61.362  149.091 1.00 290.87 ?  154 LEU F CG  1 
ATOM   12598 C CD1 . LEU F  5 154 ? 66.551  61.888  150.288 1.00 286.36 ?  154 LEU F CD1 1 
ATOM   12599 C CD2 . LEU F  5 154 ? 66.700  61.819  147.787 1.00 288.79 ?  154 LEU F CD2 1 
ATOM   12600 N N   . GLN F  5 155 ? 68.789  59.377  151.497 1.00 283.53 ?  155 GLN F N   1 
ATOM   12601 C CA  . GLN F  5 155 ? 68.738  57.951  151.790 1.00 285.71 ?  155 GLN F CA  1 
ATOM   12602 C C   . GLN F  5 155 ? 67.603  57.284  151.023 1.00 289.04 ?  155 GLN F C   1 
ATOM   12603 O O   . GLN F  5 155 ? 66.535  57.874  150.832 1.00 288.73 ?  155 GLN F O   1 
ATOM   12604 C CB  . GLN F  5 155 ? 68.551  57.705  153.289 1.00 283.30 ?  155 GLN F CB  1 
ATOM   12605 C CG  . GLN F  5 155 ? 69.588  58.368  154.173 1.00 280.08 ?  155 GLN F CG  1 
ATOM   12606 C CD  . GLN F  5 155 ? 70.974  57.788  153.977 1.00 281.45 ?  155 GLN F CD  1 
ATOM   12607 O OE1 . GLN F  5 155 ? 71.237  56.643  154.345 1.00 283.16 ?  155 GLN F OE1 1 
ATOM   12608 N NE2 . GLN F  5 155 ? 71.872  58.579  153.402 1.00 280.89 ?  155 GLN F NE2 1 
ATOM   12609 N N   . SER F  5 156 ? 67.841  56.046  150.591 1.00 275.48 ?  156 SER F N   1 
ATOM   12610 C CA  . SER F  5 156 ? 66.814  55.212  149.983 1.00 279.09 ?  156 SER F CA  1 
ATOM   12611 C C   . SER F  5 156 ? 66.980  53.769  150.442 1.00 281.33 ?  156 SER F C   1 
ATOM   12612 O O   . SER F  5 156 ? 68.106  53.286  150.599 1.00 281.62 ?  156 SER F O   1 
ATOM   12613 C CB  . SER F  5 156 ? 66.860  55.286  148.449 1.00 282.25 ?  156 SER F CB  1 
ATOM   12614 O OG  . SER F  5 156 ? 66.910  56.629  147.998 1.00 280.37 ?  156 SER F OG  1 
ATOM   12615 N N   . GLY F  5 157 ? 65.852  53.086  150.655 1.00 283.13 ?  157 GLY F N   1 
ATOM   12616 C CA  . GLY F  5 157 ? 65.847  51.667  150.951 1.00 286.04 ?  157 GLY F CA  1 
ATOM   12617 C C   . GLY F  5 157 ? 66.075  51.260  152.394 1.00 284.02 ?  157 GLY F C   1 
ATOM   12618 O O   . GLY F  5 157 ? 65.810  50.101  152.738 1.00 286.56 ?  157 GLY F O   1 
ATOM   12619 N N   . ASN F  5 158 ? 66.563  52.153  153.254 1.00 283.56 ?  158 ASN F N   1 
ATOM   12620 C CA  . ASN F  5 158 ? 66.832  51.811  154.646 1.00 281.68 ?  158 ASN F CA  1 
ATOM   12621 C C   . ASN F  5 158 ? 65.771  52.315  155.624 1.00 278.97 ?  158 ASN F C   1 
ATOM   12622 O O   . ASN F  5 158 ? 65.997  52.258  156.837 1.00 276.83 ?  158 ASN F O   1 
ATOM   12623 C CB  . ASN F  5 158 ? 68.226  52.295  155.071 1.00 279.25 ?  158 ASN F CB  1 
ATOM   12624 C CG  . ASN F  5 158 ? 68.495  53.740  154.712 1.00 276.26 ?  158 ASN F CG  1 
ATOM   12625 O OD1 . ASN F  5 158 ? 67.597  54.474  154.300 1.00 275.52 ?  158 ASN F OD1 1 
ATOM   12626 N ND2 . ASN F  5 158 ? 69.745  54.161  154.876 1.00 274.73 ?  158 ASN F ND2 1 
ATOM   12627 N N   . SER F  5 159 ? 64.626  52.800  155.142 1.00 276.56 ?  159 SER F N   1 
ATOM   12628 C CA  . SER F  5 159 ? 63.565  53.248  156.034 1.00 274.24 ?  159 SER F CA  1 
ATOM   12629 C C   . SER F  5 159 ? 62.252  52.533  155.730 1.00 277.39 ?  159 SER F C   1 
ATOM   12630 O O   . SER F  5 159 ? 62.012  52.062  154.615 1.00 281.03 ?  159 SER F O   1 
ATOM   12631 C CB  . SER F  5 159 ? 63.358  54.768  155.931 1.00 270.84 ?  159 SER F CB  1 
ATOM   12632 O OG  . SER F  5 159 ? 62.962  55.159  154.626 1.00 272.78 ?  159 SER F OG  1 
ATOM   12633 N N   . GLN F  5 160 ? 61.401  52.461  156.757 1.00 274.89 ?  160 GLN F N   1 
ATOM   12634 C CA  . GLN F  5 160 ? 60.044  51.942  156.652 1.00 277.40 ?  160 GLN F CA  1 
ATOM   12635 C C   . GLN F  5 160 ? 59.071  52.912  157.308 1.00 274.25 ?  160 GLN F C   1 
ATOM   12636 O O   . GLN F  5 160 ? 59.398  53.538  158.321 1.00 270.35 ?  160 GLN F O   1 
ATOM   12637 C CB  . GLN F  5 160 ? 59.936  50.564  157.318 1.00 279.88 ?  160 GLN F CB  1 
ATOM   12638 C CG  . GLN F  5 160 ? 60.648  49.453  156.567 1.00 283.99 ?  160 GLN F CG  1 
ATOM   12639 C CD  . GLN F  5 160 ? 60.420  48.092  157.191 1.00 286.92 ?  160 GLN F CD  1 
ATOM   12640 O OE1 . GLN F  5 160 ? 60.967  47.780  158.249 1.00 285.48 ?  160 GLN F OE1 1 
ATOM   12641 N NE2 . GLN F  5 160 ? 59.603  47.274  156.540 1.00 291.30 ?  160 GLN F NE2 1 
ATOM   12642 N N   . GLU F  5 161 ? 57.880  53.034  156.728 1.00 300.61 ?  161 GLU F N   1 
ATOM   12643 C CA  . GLU F  5 161 ? 56.828  53.885  157.266 1.00 293.86 ?  161 GLU F CA  1 
ATOM   12644 C C   . GLU F  5 161 ? 55.673  53.061  157.826 1.00 292.58 ?  161 GLU F C   1 
ATOM   12645 O O   . GLU F  5 161 ? 55.380  51.963  157.345 1.00 296.83 ?  161 GLU F O   1 
ATOM   12646 C CB  . GLU F  5 161 ? 56.301  54.830  156.184 1.00 292.59 ?  161 GLU F CB  1 
ATOM   12647 C CG  . GLU F  5 161 ? 57.295  55.893  155.767 1.00 297.48 ?  161 GLU F CG  1 
ATOM   12648 C CD  . GLU F  5 161 ? 56.700  56.900  154.810 1.00 295.69 ?  161 GLU F CD  1 
ATOM   12649 O OE1 . GLU F  5 161 ? 55.556  56.688  154.356 1.00 291.86 ?  161 GLU F OE1 1 
ATOM   12650 O OE2 . GLU F  5 161 ? 57.381  57.902  154.508 1.00 299.19 -1 161 GLU F OE2 1 
ATOM   12651 N N   . SER F  5 162 ? 55.025  53.605  158.857 1.00 296.98 ?  162 SER F N   1 
ATOM   12652 C CA  . SER F  5 162 ? 53.761  53.088  159.368 1.00 292.66 ?  162 SER F CA  1 
ATOM   12653 C C   . SER F  5 162 ? 52.815  54.263  159.566 1.00 290.18 ?  162 SER F C   1 
ATOM   12654 O O   . SER F  5 162 ? 53.216  55.292  160.119 1.00 285.97 ?  162 SER F O   1 
ATOM   12655 C CB  . SER F  5 162 ? 53.962  52.333  160.689 1.00 291.67 ?  162 SER F CB  1 
ATOM   12656 O OG  . SER F  5 162 ? 52.750  51.767  161.153 1.00 293.48 ?  162 SER F OG  1 
ATOM   12657 N N   . VAL F  5 163 ? 51.566  54.114  159.128 1.00 305.92 ?  163 VAL F N   1 
ATOM   12658 C CA  . VAL F  5 163 ? 50.563  55.163  159.266 1.00 300.49 ?  163 VAL F CA  1 
ATOM   12659 C C   . VAL F  5 163 ? 49.381  54.629  160.061 1.00 294.51 ?  163 VAL F C   1 
ATOM   12660 O O   . VAL F  5 163 ? 48.955  53.486  159.864 1.00 297.24 ?  163 VAL F O   1 
ATOM   12661 C CB  . VAL F  5 163 ? 50.093  55.676  157.889 1.00 300.94 ?  163 VAL F CB  1 
ATOM   12662 C CG1 . VAL F  5 163 ? 49.224  56.911  158.047 1.00 295.97 ?  163 VAL F CG1 1 
ATOM   12663 C CG2 . VAL F  5 163 ? 51.282  55.960  156.990 1.00 307.00 ?  163 VAL F CG2 1 
ATOM   12664 N N   . THR F  5 164 ? 48.853  55.456  160.959 1.00 306.13 ?  164 THR F N   1 
ATOM   12665 C CA  . THR F  5 164 ? 47.670  55.073  161.711 1.00 299.37 ?  164 THR F CA  1 
ATOM   12666 C C   . THR F  5 164 ? 46.424  55.186  160.836 1.00 297.95 ?  164 THR F C   1 
ATOM   12667 O O   . THR F  5 164 ? 46.398  55.906  159.833 1.00 300.63 ?  164 THR F O   1 
ATOM   12668 C CB  . THR F  5 164 ? 47.505  55.945  162.957 1.00 293.59 ?  164 THR F CB  1 
ATOM   12669 O OG1 . THR F  5 164 ? 47.393  57.320  162.571 1.00 294.20 ?  164 THR F OG1 1 
ATOM   12670 C CG2 . THR F  5 164 ? 48.697  55.778  163.886 1.00 294.70 ?  164 THR F CG2 1 
ATOM   12671 N N   . GLU F  5 165 ? 45.380  54.463  161.230 1.00 309.54 ?  165 GLU F N   1 
ATOM   12672 C CA  . GLU F  5 165 ? 44.059  54.706  160.672 1.00 307.26 ?  165 GLU F CA  1 
ATOM   12673 C C   . GLU F  5 165 ? 43.582  56.092  161.089 1.00 303.35 ?  165 GLU F C   1 
ATOM   12674 O O   . GLU F  5 165 ? 44.005  56.630  162.117 1.00 301.10 ?  165 GLU F O   1 
ATOM   12675 C CB  . GLU F  5 165 ? 43.064  53.637  161.129 1.00 304.05 ?  165 GLU F CB  1 
ATOM   12676 C CG  . GLU F  5 165 ? 43.338  52.235  160.592 1.00 308.81 ?  165 GLU F CG  1 
ATOM   12677 C CD  . GLU F  5 165 ? 43.297  52.165  159.072 1.00 313.62 ?  165 GLU F CD  1 
ATOM   12678 O OE1 . GLU F  5 165 ? 42.320  52.665  158.476 1.00 314.95 ?  165 GLU F OE1 1 
ATOM   12679 O OE2 . GLU F  5 165 ? 44.238  51.602  158.472 1.00 327.66 -1 165 GLU F OE2 1 
ATOM   12680 N N   . GLN F  5 166 ? 42.729  56.691  160.258 1.00 301.49 ?  166 GLN F N   1 
ATOM   12681 C CA  . GLN F  5 166 ? 42.177  58.001  160.580 1.00 298.13 ?  166 GLN F CA  1 
ATOM   12682 C C   . GLN F  5 166 ? 41.580  57.977  161.982 1.00 292.92 ?  166 GLN F C   1 
ATOM   12683 O O   . GLN F  5 166 ? 40.793  57.088  162.318 1.00 295.53 ?  166 GLN F O   1 
ATOM   12684 C CB  . GLN F  5 166 ? 41.107  58.366  159.548 1.00 302.77 ?  166 GLN F CB  1 
ATOM   12685 C CG  . GLN F  5 166 ? 40.534  59.768  159.658 1.00 305.68 ?  166 GLN F CG  1 
ATOM   12686 C CD  . GLN F  5 166 ? 39.676  60.133  158.457 1.00 312.42 ?  166 GLN F CD  1 
ATOM   12687 O OE1 . GLN F  5 166 ? 38.949  59.295  157.922 1.00 313.90 ?  166 GLN F OE1 1 
ATOM   12688 N NE2 . GLN F  5 166 ? 39.757  61.388  158.029 1.00 316.95 ?  166 GLN F NE2 1 
ATOM   12689 N N   . ASP F  5 167 ? 41.967  58.954  162.803 1.00 296.61 ?  167 ASP F N   1 
ATOM   12690 C CA  . ASP F  5 167 ? 41.520  58.976  164.190 1.00 292.38 ?  167 ASP F CA  1 
ATOM   12691 C C   . ASP F  5 167 ? 40.005  59.147  164.254 1.00 294.12 ?  167 ASP F C   1 
ATOM   12692 O O   . ASP F  5 167 ? 39.431  59.997  163.568 1.00 298.79 ?  167 ASP F O   1 
ATOM   12693 C CB  . ASP F  5 167 ? 42.235  60.080  164.967 1.00 291.29 ?  167 ASP F CB  1 
ATOM   12694 C CG  . ASP F  5 167 ? 41.965  60.010  166.459 1.00 286.62 ?  167 ASP F CG  1 
ATOM   12695 O OD1 . ASP F  5 167 ? 42.461  59.059  167.103 1.00 282.46 ?  167 ASP F OD1 1 
ATOM   12696 O OD2 . ASP F  5 167 ? 41.274  60.902  166.990 1.00 287.46 -1 167 ASP F OD2 1 
ATOM   12697 N N   . SER F  5 168 ? 39.361  58.328  165.086 1.00 285.91 ?  168 SER F N   1 
ATOM   12698 C CA  . SER F  5 168 ? 37.904  58.332  165.186 1.00 288.24 ?  168 SER F CA  1 
ATOM   12699 C C   . SER F  5 168 ? 37.343  59.657  165.696 1.00 289.21 ?  168 SER F C   1 
ATOM   12700 O O   . SER F  5 168 ? 36.208  60.016  165.359 1.00 292.88 ?  168 SER F O   1 
ATOM   12701 C CB  . SER F  5 168 ? 37.448  57.190  166.092 1.00 289.51 ?  168 SER F CB  1 
ATOM   12702 O OG  . SER F  5 168 ? 37.796  57.452  167.440 1.00 284.84 ?  168 SER F OG  1 
ATOM   12703 N N   . LYS F  5 169 ? 38.108  60.400  166.494 1.00 286.81 ?  169 LYS F N   1 
ATOM   12704 C CA  . LYS F  5 169 ? 37.618  61.649  167.074 1.00 288.62 ?  169 LYS F CA  1 
ATOM   12705 C C   . LYS F  5 169 ? 37.937  62.885  166.233 1.00 293.80 ?  169 LYS F C   1 
ATOM   12706 O O   . LYS F  5 169 ? 37.028  63.601  165.802 1.00 298.40 ?  169 LYS F O   1 
ATOM   12707 C CB  . LYS F  5 169 ? 38.204  61.805  168.481 1.00 285.50 ?  169 LYS F CB  1 
ATOM   12708 C CG  . LYS F  5 169 ? 37.670  60.797  169.484 1.00 281.31 ?  169 LYS F CG  1 
ATOM   12709 C CD  . LYS F  5 169 ? 37.801  61.306  170.910 1.00 281.12 ?  169 LYS F CD  1 
ATOM   12710 C CE  . LYS F  5 169 ? 39.087  62.098  171.101 1.00 283.66 ?  169 LYS F CE  1 
ATOM   12711 N NZ  . LYS F  5 169 ? 39.422  62.283  172.539 1.00 277.81 1  169 LYS F NZ  1 
ATOM   12712 N N   . ASP F  5 170 ? 39.217  63.143  165.986 1.00 287.91 ?  170 ASP F N   1 
ATOM   12713 C CA  . ASP F  5 170 ? 39.649  64.387  165.362 1.00 292.71 ?  170 ASP F CA  1 
ATOM   12714 C C   . ASP F  5 170 ? 39.926  64.250  163.871 1.00 297.06 ?  170 ASP F C   1 
ATOM   12715 O O   . ASP F  5 170 ? 40.293  65.240  163.230 1.00 301.63 ?  170 ASP F O   1 
ATOM   12716 C CB  . ASP F  5 170 ? 40.870  64.952  166.108 1.00 290.41 ?  170 ASP F CB  1 
ATOM   12717 C CG  . ASP F  5 170 ? 42.110  64.068  166.005 1.00 286.98 ?  170 ASP F CG  1 
ATOM   12718 O OD1 . ASP F  5 170 ? 42.299  63.350  165.002 1.00 288.19 ?  170 ASP F OD1 1 
ATOM   12719 O OD2 . ASP F  5 170 ? 42.908  64.093  166.965 1.00 283.22 -1 170 ASP F OD2 1 
ATOM   12720 N N   . SER F  5 171 ? 39.767  63.049  163.315 1.00 289.16 ?  171 SER F N   1 
ATOM   12721 C CA  . SER F  5 171 ? 39.882  62.780  161.882 1.00 293.51 ?  171 SER F CA  1 
ATOM   12722 C C   . SER F  5 171 ? 41.279  63.047  161.329 1.00 294.66 ?  171 SER F C   1 
ATOM   12723 O O   . SER F  5 171 ? 41.434  63.282  160.125 1.00 300.02 ?  171 SER F O   1 
ATOM   12724 C CB  . SER F  5 171 ? 38.845  63.585  161.086 1.00 300.05 ?  171 SER F CB  1 
ATOM   12725 O OG  . SER F  5 171 ? 37.522  63.228  161.451 1.00 299.63 ?  171 SER F OG  1 
ATOM   12726 N N   . THR F  5 172 ? 42.308  63.027  162.170 1.00 299.45 ?  172 THR F N   1 
ATOM   12727 C CA  . THR F  5 172 ? 43.671  63.178  161.686 1.00 300.41 ?  172 THR F CA  1 
ATOM   12728 C C   . THR F  5 172 ? 44.350  61.816  161.538 1.00 298.28 ?  172 THR F C   1 
ATOM   12729 O O   . THR F  5 172 ? 43.819  60.771  161.924 1.00 296.36 ?  172 THR F O   1 
ATOM   12730 C CB  . THR F  5 172 ? 44.482  64.085  162.620 1.00 298.88 ?  172 THR F CB  1 
ATOM   12731 O OG1 . THR F  5 172 ? 44.568  63.492  163.922 1.00 292.87 ?  172 THR F OG1 1 
ATOM   12732 C CG2 . THR F  5 172 ? 43.832  65.459  162.735 1.00 302.84 ?  172 THR F CG2 1 
ATOM   12733 N N   . TYR F  5 173 ? 45.552  61.854  160.971 1.00 293.47 ?  173 TYR F N   1 
ATOM   12734 C CA  . TYR F  5 173 ? 46.443  60.714  160.816 1.00 296.92 ?  173 TYR F CA  1 
ATOM   12735 C C   . TYR F  5 173 ? 47.739  60.976  161.570 1.00 298.82 ?  173 TYR F C   1 
ATOM   12736 O O   . TYR F  5 173 ? 48.115  62.125  161.817 1.00 298.82 ?  173 TYR F O   1 
ATOM   12737 C CB  . TYR F  5 173 ? 46.769  60.422  159.342 1.00 301.57 ?  173 TYR F CB  1 
ATOM   12738 C CG  . TYR F  5 173 ? 45.586  60.074  158.462 1.00 299.35 ?  173 TYR F CG  1 
ATOM   12739 C CD1 . TYR F  5 173 ? 44.872  61.063  157.798 1.00 300.72 ?  173 TYR F CD1 1 
ATOM   12740 C CD2 . TYR F  5 173 ? 45.201  58.752  158.275 1.00 298.82 ?  173 TYR F CD2 1 
ATOM   12741 C CE1 . TYR F  5 173 ? 43.798  60.747  156.983 1.00 304.35 ?  173 TYR F CE1 1 
ATOM   12742 C CE2 . TYR F  5 173 ? 44.129  58.426  157.463 1.00 298.40 ?  173 TYR F CE2 1 
ATOM   12743 C CZ  . TYR F  5 173 ? 43.431  59.427  156.820 1.00 302.63 ?  173 TYR F CZ  1 
ATOM   12744 O OH  . TYR F  5 173 ? 42.363  59.108  156.011 1.00 306.76 ?  173 TYR F OH  1 
ATOM   12745 N N   . SER F  5 174 ? 48.426  59.897  161.934 1.00 300.90 ?  174 SER F N   1 
ATOM   12746 C CA  . SER F  5 174 ? 49.797  60.006  162.401 1.00 304.44 ?  174 SER F CA  1 
ATOM   12747 C C   . SER F  5 174 ? 50.661  59.012  161.642 1.00 310.71 ?  174 SER F C   1 
ATOM   12748 O O   . SER F  5 174 ? 50.182  57.977  161.171 1.00 311.07 ?  174 SER F O   1 
ATOM   12749 C CB  . SER F  5 174 ? 49.900  59.734  163.911 1.00 299.82 ?  174 SER F CB  1 
ATOM   12750 O OG  . SER F  5 174 ? 49.242  60.739  164.662 1.00 294.29 ?  174 SER F OG  1 
ATOM   12751 N N   . LEU F  5 175 ? 51.947  59.340  161.533 1.00 292.37 ?  175 LEU F N   1 
ATOM   12752 C CA  . LEU F  5 175 ? 52.871  58.561  160.724 1.00 294.31 ?  175 LEU F CA  1 
ATOM   12753 C C   . LEU F  5 175 ? 54.226  58.497  161.407 1.00 292.51 ?  175 LEU F C   1 
ATOM   12754 O O   . LEU F  5 175 ? 54.717  59.500  161.935 1.00 292.77 ?  175 LEU F O   1 
ATOM   12755 C CB  . LEU F  5 175 ? 53.012  59.164  159.313 1.00 300.63 ?  175 LEU F CB  1 
ATOM   12756 C CG  . LEU F  5 175 ? 53.932  58.534  158.258 1.00 304.17 ?  175 LEU F CG  1 
ATOM   12757 C CD1 . LEU F  5 175 ? 53.443  58.916  156.870 1.00 310.11 ?  175 LEU F CD1 1 
ATOM   12758 C CD2 . LEU F  5 175 ? 55.390  58.959  158.421 1.00 305.29 ?  175 LEU F CD2 1 
ATOM   12759 N N   . SER F  5 176 ? 54.823  57.312  161.384 1.00 290.90 ?  176 SER F N   1 
ATOM   12760 C CA  . SER F  5 176 ? 56.190  57.099  161.823 1.00 290.39 ?  176 SER F CA  1 
ATOM   12761 C C   . SER F  5 176 ? 57.026  56.693  160.618 1.00 294.98 ?  176 SER F C   1 
ATOM   12762 O O   . SER F  5 176 ? 56.583  55.895  159.786 1.00 296.51 ?  176 SER F O   1 
ATOM   12763 C CB  . SER F  5 176 ? 56.271  56.031  162.919 1.00 285.59 ?  176 SER F CB  1 
ATOM   12764 O OG  . SER F  5 176 ? 55.991  54.738  162.412 1.00 285.62 ?  176 SER F OG  1 
ATOM   12765 N N   . SER F  5 177 ? 58.229  57.243  160.527 1.00 270.41 ?  177 SER F N   1 
ATOM   12766 C CA  . SER F  5 177 ? 59.223  56.792  159.567 1.00 272.70 ?  177 SER F CA  1 
ATOM   12767 C C   . SER F  5 177 ? 60.436  56.366  160.374 1.00 271.42 ?  177 SER F C   1 
ATOM   12768 O O   . SER F  5 177 ? 60.933  57.135  161.204 1.00 267.88 ?  177 SER F O   1 
ATOM   12769 C CB  . SER F  5 177 ? 59.574  57.889  158.560 1.00 272.07 ?  177 SER F CB  1 
ATOM   12770 O OG  . SER F  5 177 ? 60.525  57.423  157.620 1.00 274.40 ?  177 SER F OG  1 
ATOM   12771 N N   . THR F  5 178 ? 60.913  55.149  160.131 1.00 262.91 ?  178 THR F N   1 
ATOM   12772 C CA  . THR F  5 178 ? 61.996  54.569  160.912 1.00 262.41 ?  178 THR F CA  1 
ATOM   12773 C C   . THR F  5 178 ? 63.186  54.247  160.023 1.00 264.32 ?  178 THR F C   1 
ATOM   12774 O O   . THR F  5 178 ? 63.077  53.435  159.100 1.00 268.04 ?  178 THR F O   1 
ATOM   12775 C CB  . THR F  5 178 ? 61.522  53.302  161.630 1.00 264.55 ?  178 THR F CB  1 
ATOM   12776 O OG1 . THR F  5 178 ? 60.356  53.595  162.410 1.00 262.95 ?  178 THR F OG1 1 
ATOM   12777 C CG2 . THR F  5 178 ? 62.609  52.765  162.541 1.00 264.03 ?  178 THR F CG2 1 
ATOM   12778 N N   . LEU F  5 179 ? 64.318  54.874  160.322 1.00 276.95 ?  179 LEU F N   1 
ATOM   12779 C CA  . LEU F  5 179 ? 65.566  54.679  159.601 1.00 278.34 ?  179 LEU F CA  1 
ATOM   12780 C C   . LEU F  5 179 ? 66.394  53.677  160.390 1.00 279.36 ?  179 LEU F C   1 
ATOM   12781 O O   . LEU F  5 179 ? 66.646  53.886  161.581 1.00 276.95 ?  179 LEU F O   1 
ATOM   12782 C CB  . LEU F  5 179 ? 66.323  56.001  159.464 1.00 275.32 ?  179 LEU F CB  1 
ATOM   12783 C CG  . LEU F  5 179 ? 67.745  55.970  158.901 1.00 276.15 ?  179 LEU F CG  1 
ATOM   12784 C CD1 . LEU F  5 179 ? 67.729  55.679  157.413 1.00 279.33 ?  179 LEU F CD1 1 
ATOM   12785 C CD2 . LEU F  5 179 ? 68.473  57.273  159.197 1.00 272.73 ?  179 LEU F CD2 1 
ATOM   12786 N N   . THR F  5 180 ? 66.818  52.594  159.742 1.00 274.92 ?  180 THR F N   1 
ATOM   12787 C CA  . THR F  5 180 ? 67.573  51.557  160.434 1.00 276.50 ?  180 THR F CA  1 
ATOM   12788 C C   . THR F  5 180 ? 68.959  51.448  159.820 1.00 277.66 ?  180 THR F C   1 
ATOM   12789 O O   . THR F  5 180 ? 69.094  51.215  158.614 1.00 280.11 ?  180 THR F O   1 
ATOM   12790 C CB  . THR F  5 180 ? 66.846  50.212  160.341 1.00 280.40 ?  180 THR F CB  1 
ATOM   12791 O OG1 . THR F  5 180 ? 65.486  50.368  160.767 1.00 279.53 ?  180 THR F OG1 1 
ATOM   12792 C CG2 . THR F  5 180 ? 67.531  49.170  161.208 1.00 282.02 ?  180 THR F CG2 1 
ATOM   12793 N N   . LEU F  5 181 ? 69.983  51.616  160.657 1.00 292.09 ?  181 LEU F N   1 
ATOM   12794 C CA  . LEU F  5 181 ? 71.376  51.517  160.251 1.00 297.50 ?  181 LEU F CA  1 
ATOM   12795 C C   . LEU F  5 181 ? 72.128  50.598  161.203 1.00 297.90 ?  181 LEU F C   1 
ATOM   12796 O O   . LEU F  5 181 ? 71.736  50.430  162.362 1.00 293.65 ?  181 LEU F O   1 
ATOM   12797 C CB  . LEU F  5 181 ? 72.046  52.898  160.228 1.00 303.30 ?  181 LEU F CB  1 
ATOM   12798 C CG  . LEU F  5 181 ? 71.359  53.985  159.396 1.00 312.10 ?  181 LEU F CG  1 
ATOM   12799 C CD1 . LEU F  5 181 ? 71.857  55.361  159.799 1.00 316.69 ?  181 LEU F CD1 1 
ATOM   12800 C CD2 . LEU F  5 181 ? 71.576  53.753  157.908 1.00 321.20 ?  181 LEU F CD2 1 
ATOM   12801 N N   . SER F  5 182 ? 73.204  49.989  160.707 1.00 308.15 ?  182 SER F N   1 
ATOM   12802 C CA  . SER F  5 182 ? 74.134  49.319  161.603 1.00 310.57 ?  182 SER F CA  1 
ATOM   12803 C C   . SER F  5 182 ? 74.847  50.355  162.474 1.00 310.98 ?  182 SER F C   1 
ATOM   12804 O O   . SER F  5 182 ? 74.929  51.539  162.133 1.00 311.17 ?  182 SER F O   1 
ATOM   12805 C CB  . SER F  5 182 ? 75.142  48.481  160.816 1.00 317.43 ?  182 SER F CB  1 
ATOM   12806 O OG  . SER F  5 182 ? 75.991  49.292  160.023 1.00 322.28 ?  182 SER F OG  1 
ATOM   12807 N N   . LYS F  5 183 ? 75.356  49.900  163.623 1.00 303.64 ?  183 LYS F N   1 
ATOM   12808 C CA  . LYS F  5 183 ? 76.124  50.790  164.494 1.00 304.81 ?  183 LYS F CA  1 
ATOM   12809 C C   . LYS F  5 183 ? 77.327  51.399  163.776 1.00 311.38 ?  183 LYS F C   1 
ATOM   12810 O O   . LYS F  5 183 ? 77.609  52.593  163.931 1.00 309.37 ?  183 LYS F O   1 
ATOM   12811 C CB  . LYS F  5 183 ? 76.572  50.038  165.749 1.00 305.41 ?  183 LYS F CB  1 
ATOM   12812 C CG  . LYS F  5 183 ? 77.387  50.876  166.732 1.00 306.82 ?  183 LYS F CG  1 
ATOM   12813 C CD  . LYS F  5 183 ? 77.911  50.018  167.880 1.00 308.56 ?  183 LYS F CD  1 
ATOM   12814 C CE  . LYS F  5 183 ? 78.292  50.852  169.098 1.00 308.07 ?  183 LYS F CE  1 
ATOM   12815 N NZ  . LYS F  5 183 ? 79.365  51.840  168.797 1.00 311.34 1  183 LYS F NZ  1 
ATOM   12816 N N   . ALA F  5 184 ? 78.059  50.588  163.002 1.00 312.50 ?  184 ALA F N   1 
ATOM   12817 C CA  . ALA F  5 184 ? 79.212  51.089  162.254 1.00 315.63 ?  184 ALA F CA  1 
ATOM   12818 C C   . ALA F  5 184 ? 78.837  52.245  161.331 1.00 312.52 ?  184 ALA F C   1 
ATOM   12819 O O   . ALA F  5 184 ? 79.473  53.305  161.355 1.00 311.50 ?  184 ALA F O   1 
ATOM   12820 C CB  . ALA F  5 184 ? 79.854  49.950  161.460 1.00 321.88 ?  184 ALA F CB  1 
ATOM   12821 N N   . ASP F  5 185 ? 77.811  52.052  160.498 1.00 321.09 ?  185 ASP F N   1 
ATOM   12822 C CA  . ASP F  5 185 ? 77.393  53.104  159.574 1.00 321.04 ?  185 ASP F CA  1 
ATOM   12823 C C   . ASP F  5 185 ? 76.882  54.326  160.322 1.00 319.18 ?  185 ASP F C   1 
ATOM   12824 O O   . ASP F  5 185 ? 77.132  55.466  159.909 1.00 323.13 ?  185 ASP F O   1 
ATOM   12825 C CB  . ASP F  5 185 ? 76.329  52.579  158.611 1.00 321.89 ?  185 ASP F CB  1 
ATOM   12826 C CG  . ASP F  5 185 ? 76.920  51.781  157.465 1.00 327.30 ?  185 ASP F CG  1 
ATOM   12827 O OD1 . ASP F  5 185 ? 78.149  51.857  157.249 1.00 330.59 ?  185 ASP F OD1 1 
ATOM   12828 O OD2 . ASP F  5 185 ? 76.149  51.087  156.770 1.00 328.39 -1 185 ASP F OD2 1 
ATOM   12829 N N   . TYR F  5 186 ? 76.144  54.107  161.414 1.00 312.05 ?  186 TYR F N   1 
ATOM   12830 C CA  . TYR F  5 186 ? 75.608  55.219  162.192 1.00 309.87 ?  186 TYR F CA  1 
ATOM   12831 C C   . TYR F  5 186 ? 76.731  56.127  162.681 1.00 310.94 ?  186 TYR F C   1 
ATOM   12832 O O   . TYR F  5 186 ? 76.650  57.355  162.561 1.00 313.12 ?  186 TYR F O   1 
ATOM   12833 C CB  . TYR F  5 186 ? 74.779  54.686  163.362 1.00 302.89 ?  186 TYR F CB  1 
ATOM   12834 C CG  . TYR F  5 186 ? 74.198  55.765  164.240 1.00 300.44 ?  186 TYR F CG  1 
ATOM   12835 C CD1 . TYR F  5 186 ? 73.212  56.613  163.757 1.00 302.78 ?  186 TYR F CD1 1 
ATOM   12836 C CD2 . TYR F  5 186 ? 74.626  55.933  165.549 1.00 295.97 ?  186 TYR F CD2 1 
ATOM   12837 C CE1 . TYR F  5 186 ? 72.674  57.601  164.545 1.00 300.88 ?  186 TYR F CE1 1 
ATOM   12838 C CE2 . TYR F  5 186 ? 74.091  56.920  166.349 1.00 293.90 ?  186 TYR F CE2 1 
ATOM   12839 C CZ  . TYR F  5 186 ? 73.115  57.751  165.840 1.00 296.43 ?  186 TYR F CZ  1 
ATOM   12840 O OH  . TYR F  5 186 ? 72.572  58.739  166.624 1.00 294.66 ?  186 TYR F OH  1 
ATOM   12841 N N   . GLU F  5 187 ? 77.792  55.539  163.235 1.00 299.80 ?  187 GLU F N   1 
ATOM   12842 C CA  . GLU F  5 187 ? 78.880  56.339  163.779 1.00 300.60 ?  187 GLU F CA  1 
ATOM   12843 C C   . GLU F  5 187 ? 79.797  56.892  162.694 1.00 307.16 ?  187 GLU F C   1 
ATOM   12844 O O   . GLU F  5 187 ? 80.691  57.685  163.008 1.00 308.75 ?  187 GLU F O   1 
ATOM   12845 C CB  . GLU F  5 187 ? 79.679  55.524  164.798 1.00 301.42 ?  187 GLU F CB  1 
ATOM   12846 C CG  . GLU F  5 187 ? 78.799  54.937  165.887 1.00 298.93 ?  187 GLU F CG  1 
ATOM   12847 C CD  . GLU F  5 187 ? 79.586  54.381  167.052 1.00 301.34 ?  187 GLU F CD  1 
ATOM   12848 O OE1 . GLU F  5 187 ? 80.419  53.477  166.834 1.00 306.47 ?  187 GLU F OE1 1 
ATOM   12849 O OE2 . GLU F  5 187 ? 79.368  54.851  168.188 1.00 298.32 -1 187 GLU F OE2 1 
ATOM   12850 N N   . LYS F  5 188 ? 79.599  56.492  161.437 1.00 297.41 ?  188 LYS F N   1 
ATOM   12851 C CA  . LYS F  5 188 ? 80.392  56.975  160.314 1.00 298.21 ?  188 LYS F CA  1 
ATOM   12852 C C   . LYS F  5 188 ? 79.829  58.276  159.743 1.00 295.71 ?  188 LYS F C   1 
ATOM   12853 O O   . LYS F  5 188 ? 80.372  58.803  158.767 1.00 296.23 ?  188 LYS F O   1 
ATOM   12854 C CB  . LYS F  5 188 ? 80.464  55.893  159.218 1.00 301.78 ?  188 LYS F CB  1 
ATOM   12855 C CG  . LYS F  5 188 ? 81.509  56.128  158.119 1.00 303.33 ?  188 LYS F CG  1 
ATOM   12856 C CD  . LYS F  5 188 ? 81.416  55.098  156.997 1.00 306.79 ?  188 LYS F CD  1 
ATOM   12857 C CE  . LYS F  5 188 ? 81.489  53.679  157.526 1.00 309.49 ?  188 LYS F CE  1 
ATOM   12858 N NZ  . LYS F  5 188 ? 81.527  52.693  156.412 1.00 313.14 1  188 LYS F NZ  1 
ATOM   12859 N N   . HIS F  5 189 ? 78.768  58.813  160.349 1.00 291.39 ?  189 HIS F N   1 
ATOM   12860 C CA  . HIS F  5 189 ? 78.151  60.060  159.917 1.00 294.19 ?  189 HIS F CA  1 
ATOM   12861 C C   . HIS F  5 189 ? 77.721  60.860  161.143 1.00 290.45 ?  189 HIS F C   1 
ATOM   12862 O O   . HIS F  5 189 ? 77.595  60.322  162.246 1.00 285.19 ?  189 HIS F O   1 
ATOM   12863 C CB  . HIS F  5 189 ? 76.946  59.799  159.007 1.00 297.05 ?  189 HIS F CB  1 
ATOM   12864 C CG  . HIS F  5 189 ? 77.267  58.991  157.787 1.00 301.48 ?  189 HIS F CG  1 
ATOM   12865 N ND1 . HIS F  5 189 ? 76.803  57.705  157.603 1.00 299.92 ?  189 HIS F ND1 1 
ATOM   12866 C CD2 . HIS F  5 189 ? 78.000  59.286  156.687 1.00 307.44 ?  189 HIS F CD2 1 
ATOM   12867 C CE1 . HIS F  5 189 ? 77.241  57.242  156.446 1.00 304.98 ?  189 HIS F CE1 1 
ATOM   12868 N NE2 . HIS F  5 189 ? 77.969  58.181  155.870 1.00 309.59 ?  189 HIS F NE2 1 
ATOM   12869 N N   . LYS F  5 190 ? 77.501  62.162  160.939 1.00 288.20 ?  190 LYS F N   1 
ATOM   12870 C CA  . LYS F  5 190 ? 77.140  63.071  162.022 1.00 285.37 ?  190 LYS F CA  1 
ATOM   12871 C C   . LYS F  5 190 ? 75.690  63.544  161.986 1.00 286.34 ?  190 LYS F C   1 
ATOM   12872 O O   . LYS F  5 190 ? 74.930  63.280  162.921 1.00 281.59 ?  190 LYS F O   1 
ATOM   12873 C CB  . LYS F  5 190 ? 78.070  64.293  162.012 1.00 288.28 ?  190 LYS F CB  1 
ATOM   12874 C CG  . LYS F  5 190 ? 77.577  65.404  162.928 1.00 286.40 ?  190 LYS F CG  1 
ATOM   12875 C CD  . LYS F  5 190 ? 78.553  66.558  163.047 1.00 288.62 ?  190 LYS F CD  1 
ATOM   12876 C CE  . LYS F  5 190 ? 78.637  67.342  161.749 1.00 295.84 ?  190 LYS F CE  1 
ATOM   12877 N NZ  . LYS F  5 190 ? 79.372  68.625  161.924 1.00 297.66 1  190 LYS F NZ  1 
ATOM   12878 N N   . VAL F  5 191 ? 75.279  64.231  160.921 1.00 287.57 ?  191 VAL F N   1 
ATOM   12879 C CA  . VAL F  5 191 ? 73.985  64.909  160.874 1.00 289.24 ?  191 VAL F CA  1 
ATOM   12880 C C   . VAL F  5 191 ? 72.879  63.974  160.397 1.00 289.22 ?  191 VAL F C   1 
ATOM   12881 O O   . VAL F  5 191 ? 72.947  63.431  159.289 1.00 292.39 ?  191 VAL F O   1 
ATOM   12882 C CB  . VAL F  5 191 ? 74.061  66.149  159.969 1.00 295.29 ?  191 VAL F CB  1 
ATOM   12883 C CG1 . VAL F  5 191 ? 72.801  66.992  160.107 1.00 296.45 ?  191 VAL F CG1 1 
ATOM   12884 C CG2 . VAL F  5 191 ? 75.312  66.959  160.275 1.00 295.90 ?  191 VAL F CG2 1 
ATOM   12885 N N   . TYR F  5 192 ? 71.858  63.787  161.238 1.00 299.47 ?  192 TYR F N   1 
ATOM   12886 C CA  . TYR F  5 192 ? 70.685  62.987  160.902 1.00 299.28 ?  192 TYR F CA  1 
ATOM   12887 C C   . TYR F  5 192 ? 69.456  63.887  160.914 1.00 301.74 ?  192 TYR F C   1 
ATOM   12888 O O   . TYR F  5 192 ? 69.166  64.529  161.929 1.00 299.15 ?  192 TYR F O   1 
ATOM   12889 C CB  . TYR F  5 192 ? 70.525  61.822  161.880 1.00 291.90 ?  192 TYR F CB  1 
ATOM   12890 C CG  . TYR F  5 192 ? 71.589  60.777  161.689 1.00 289.91 ?  192 TYR F CG  1 
ATOM   12891 C CD1 . TYR F  5 192 ? 72.824  60.886  162.316 1.00 287.11 ?  192 TYR F CD1 1 
ATOM   12892 C CD2 . TYR F  5 192 ? 71.372  59.698  160.847 1.00 291.15 ?  192 TYR F CD2 1 
ATOM   12893 C CE1 . TYR F  5 192 ? 73.801  59.939  162.123 1.00 285.68 ?  192 TYR F CE1 1 
ATOM   12894 C CE2 . TYR F  5 192 ? 72.339  58.749  160.649 1.00 289.70 ?  192 TYR F CE2 1 
ATOM   12895 C CZ  . TYR F  5 192 ? 73.551  58.874  161.288 1.00 287.07 ?  192 TYR F CZ  1 
ATOM   12896 O OH  . TYR F  5 192 ? 74.518  57.925  161.088 1.00 285.95 ?  192 TYR F OH  1 
ATOM   12897 N N   . ALA F  5 193 ? 68.730  63.917  159.795 1.00 300.89 ?  193 ALA F N   1 
ATOM   12898 C CA  . ALA F  5 193 ? 67.605  64.823  159.585 1.00 304.51 ?  193 ALA F CA  1 
ATOM   12899 C C   . ALA F  5 193 ? 66.482  64.110  158.846 1.00 307.10 ?  193 ALA F C   1 
ATOM   12900 O O   . ALA F  5 193 ? 66.745  63.322  157.934 1.00 309.38 ?  193 ALA F O   1 
ATOM   12901 C CB  . ALA F  5 193 ? 68.026  66.071  158.795 1.00 309.32 ?  193 ALA F CB  1 
ATOM   12902 N N   . CYS F  5 194 ? 65.236  64.372  159.244 1.00 318.03 ?  194 CYS F N   1 
ATOM   12903 C CA  . CYS F  5 194 ? 64.071  63.996  158.450 1.00 319.66 ?  194 CYS F CA  1 
ATOM   12904 C C   . CYS F  5 194 ? 63.362  65.266  157.989 1.00 319.03 ?  194 CYS F C   1 
ATOM   12905 O O   . CYS F  5 194 ? 63.123  66.177  158.790 1.00 315.85 ?  194 CYS F O   1 
ATOM   12906 C CB  . CYS F  5 194 ? 63.121  63.081  159.245 1.00 308.87 ?  194 CYS F CB  1 
ATOM   12907 S SG  . CYS F  5 194 ? 62.299  63.821  160.704 1.00 302.58 ?  194 CYS F SG  1 
ATOM   12908 N N   . GLU F  5 195 ? 63.043  65.324  156.696 1.00 311.03 ?  195 GLU F N   1 
ATOM   12909 C CA  . GLU F  5 195 ? 62.373  66.461  156.074 1.00 305.92 ?  195 GLU F CA  1 
ATOM   12910 C C   . GLU F  5 195 ? 60.960  66.041  155.685 1.00 302.27 ?  195 GLU F C   1 
ATOM   12911 O O   . GLU F  5 195 ? 60.779  65.022  155.007 1.00 305.39 ?  195 GLU F O   1 
ATOM   12912 C CB  . GLU F  5 195 ? 63.171  66.976  154.873 1.00 311.13 ?  195 GLU F CB  1 
ATOM   12913 C CG  . GLU F  5 195 ? 62.760  68.359  154.407 1.00 311.94 ?  195 GLU F CG  1 
ATOM   12914 C CD  . GLU F  5 195 ? 63.452  68.774  153.129 1.00 323.76 ?  195 GLU F CD  1 
ATOM   12915 O OE1 . GLU F  5 195 ? 64.167  67.941  152.533 1.00 330.22 ?  195 GLU F OE1 1 
ATOM   12916 O OE2 . GLU F  5 195 ? 63.295  69.947  152.733 1.00 324.37 -1 195 GLU F OE2 1 
ATOM   12917 N N   . VAL F  5 196 ? 59.968  66.818  156.118 1.00 330.39 ?  196 VAL F N   1 
ATOM   12918 C CA  . VAL F  5 196 ? 58.554  66.485  155.963 1.00 319.79 ?  196 VAL F CA  1 
ATOM   12919 C C   . VAL F  5 196 ? 57.876  67.484  155.033 1.00 315.91 ?  196 VAL F C   1 
ATOM   12920 O O   . VAL F  5 196 ? 57.982  68.700  155.231 1.00 316.25 ?  196 VAL F O   1 
ATOM   12921 C CB  . VAL F  5 196 ? 57.846  66.464  157.329 1.00 312.51 ?  196 VAL F CB  1 
ATOM   12922 C CG1 . VAL F  5 196 ? 56.342  66.317  157.159 1.00 301.36 ?  196 VAL F CG1 1 
ATOM   12923 C CG2 . VAL F  5 196 ? 58.411  65.359  158.204 1.00 314.16 ?  196 VAL F CG2 1 
ATOM   12924 N N   . THR F  5 197 ? 57.185  66.966  154.018 1.00 310.21 ?  197 THR F N   1 
ATOM   12925 C CA  . THR F  5 197 ? 56.414  67.771  153.079 1.00 311.67 ?  197 THR F CA  1 
ATOM   12926 C C   . THR F  5 197 ? 54.932  67.464  153.244 1.00 313.19 ?  197 THR F C   1 
ATOM   12927 O O   . THR F  5 197 ? 54.526  66.301  153.159 1.00 315.43 ?  197 THR F O   1 
ATOM   12928 C CB  . THR F  5 197 ? 56.832  67.478  151.639 1.00 315.38 ?  197 THR F CB  1 
ATOM   12929 O OG1 . THR F  5 197 ? 58.243  67.676  151.498 1.00 319.26 ?  197 THR F OG1 1 
ATOM   12930 C CG2 . THR F  5 197 ? 56.079  68.382  150.677 1.00 318.26 ?  197 THR F CG2 1 
ATOM   12931 N N   . HIS F  5 198 ? 54.129  68.503  153.472 1.00 321.00 ?  198 HIS F N   1 
ATOM   12932 C CA  . HIS F  5 198 ? 52.684  68.349  153.583 1.00 322.32 ?  198 HIS F CA  1 
ATOM   12933 C C   . HIS F  5 198 ? 52.045  69.683  153.213 1.00 324.90 ?  198 HIS F C   1 
ATOM   12934 O O   . HIS F  5 198 ? 52.609  70.745  153.490 1.00 323.75 ?  198 HIS F O   1 
ATOM   12935 C CB  . HIS F  5 198 ? 52.286  67.893  154.995 1.00 318.08 ?  198 HIS F CB  1 
ATOM   12936 C CG  . HIS F  5 198 ? 50.822  67.624  155.165 1.00 319.43 ?  198 HIS F CG  1 
ATOM   12937 N ND1 . HIS F  5 198 ? 49.912  68.603  155.499 1.00 319.96 ?  198 HIS F ND1 1 
ATOM   12938 C CD2 . HIS F  5 198 ? 50.116  66.473  155.066 1.00 318.25 ?  198 HIS F CD2 1 
ATOM   12939 C CE1 . HIS F  5 198 ? 48.707  68.069  155.587 1.00 321.13 ?  198 HIS F CE1 1 
ATOM   12940 N NE2 . HIS F  5 198 ? 48.803  66.778  155.329 1.00 318.11 ?  198 HIS F NE2 1 
ATOM   12941 N N   . GLN F  5 199 ? 50.870  69.630  152.576 1.00 316.93 ?  199 GLN F N   1 
ATOM   12942 C CA  . GLN F  5 199 ? 50.281  70.864  152.061 1.00 320.30 ?  199 GLN F CA  1 
ATOM   12943 C C   . GLN F  5 199 ? 49.803  71.807  153.161 1.00 317.93 ?  199 GLN F C   1 
ATOM   12944 O O   . GLN F  5 199 ? 49.573  72.989  152.884 1.00 320.16 ?  199 GLN F O   1 
ATOM   12945 C CB  . GLN F  5 199 ? 49.107  70.561  151.127 1.00 325.42 ?  199 GLN F CB  1 
ATOM   12946 C CG  . GLN F  5 199 ? 47.867  70.029  151.821 1.00 324.87 ?  199 GLN F CG  1 
ATOM   12947 C CD  . GLN F  5 199 ? 46.641  70.085  150.930 1.00 330.51 ?  199 GLN F CD  1 
ATOM   12948 O OE1 . GLN F  5 199 ? 45.934  71.092  150.894 1.00 332.68 ?  199 GLN F OE1 1 
ATOM   12949 N NE2 . GLN F  5 199 ? 46.382  69.002  150.207 1.00 333.26 ?  199 GLN F NE2 1 
ATOM   12950 N N   . GLY F  5 200 ? 49.647  71.324  154.393 1.00 343.21 ?  200 GLY F N   1 
ATOM   12951 C CA  . GLY F  5 200 ? 49.260  72.204  155.482 1.00 340.81 ?  200 GLY F CA  1 
ATOM   12952 C C   . GLY F  5 200 ? 50.368  73.071  156.027 1.00 337.94 ?  200 GLY F C   1 
ATOM   12953 O O   . GLY F  5 200 ? 50.099  74.010  156.783 1.00 336.72 ?  200 GLY F O   1 
ATOM   12954 N N   . LEU F  5 201 ? 51.608  72.764  155.668 1.00 333.85 ?  201 LEU F N   1 
ATOM   12955 C CA  . LEU F  5 201 ? 52.777  73.499  156.125 1.00 331.34 ?  201 LEU F CA  1 
ATOM   12956 C C   . LEU F  5 201 ? 53.066  74.658  155.181 1.00 336.55 ?  201 LEU F C   1 
ATOM   12957 O O   . LEU F  5 201 ? 53.047  74.490  153.958 1.00 341.67 ?  201 LEU F O   1 
ATOM   12958 C CB  . LEU F  5 201 ? 53.992  72.575  156.223 1.00 328.77 ?  201 LEU F CB  1 
ATOM   12959 C CG  . LEU F  5 201 ? 53.933  71.452  157.261 1.00 324.87 ?  201 LEU F CG  1 
ATOM   12960 C CD1 . LEU F  5 201 ? 55.053  70.454  157.036 1.00 323.82 ?  201 LEU F CD1 1 
ATOM   12961 C CD2 . LEU F  5 201 ? 54.031  72.033  158.657 1.00 320.99 ?  201 LEU F CD2 1 
ATOM   12962 N N   . SER F  5 202 ? 53.309  75.840  155.752 1.00 331.66 ?  202 SER F N   1 
ATOM   12963 C CA  . SER F  5 202 ? 53.710  76.970  154.923 1.00 336.35 ?  202 SER F CA  1 
ATOM   12964 C C   . SER F  5 202 ? 55.016  76.677  154.195 1.00 337.84 ?  202 SER F C   1 
ATOM   12965 O O   . SER F  5 202 ? 55.224  77.161  153.076 1.00 341.55 ?  202 SER F O   1 
ATOM   12966 C CB  . SER F  5 202 ? 53.843  78.230  155.779 1.00 337.30 ?  202 SER F CB  1 
ATOM   12967 O OG  . SER F  5 202 ? 54.857  78.078  156.756 1.00 338.58 ?  202 SER F OG  1 
ATOM   12968 N N   . SER F  5 203 ? 55.903  75.897  154.808 1.00 340.82 ?  203 SER F N   1 
ATOM   12969 C CA  . SER F  5 203 ? 57.167  75.503  154.204 1.00 339.38 ?  203 SER F CA  1 
ATOM   12970 C C   . SER F  5 203 ? 57.532  74.115  154.707 1.00 335.38 ?  203 SER F C   1 
ATOM   12971 O O   . SER F  5 203 ? 57.164  73.753  155.831 1.00 332.01 ?  203 SER F O   1 
ATOM   12972 C CB  . SER F  5 203 ? 58.289  76.498  154.537 1.00 340.37 ?  203 SER F CB  1 
ATOM   12973 O OG  . SER F  5 203 ? 59.469  76.211  153.805 1.00 342.22 ?  203 SER F OG  1 
ATOM   12974 N N   . PRO F  5 204 ? 58.224  73.311  153.897 1.00 324.10 ?  204 PRO F N   1 
ATOM   12975 C CA  . PRO F  5 204 ? 58.733  72.021  154.384 1.00 323.81 ?  204 PRO F CA  1 
ATOM   12976 C C   . PRO F  5 204 ? 59.518  72.179  155.681 1.00 320.16 ?  204 PRO F C   1 
ATOM   12977 O O   . PRO F  5 204 ? 60.226  73.168  155.883 1.00 320.10 ?  204 PRO F O   1 
ATOM   12978 C CB  . PRO F  5 204 ? 59.624  71.547  153.233 1.00 327.91 ?  204 PRO F CB  1 
ATOM   12979 C CG  . PRO F  5 204 ? 58.974  72.133  152.019 1.00 332.69 ?  204 PRO F CG  1 
ATOM   12980 C CD  . PRO F  5 204 ? 58.430  73.475  152.446 1.00 333.59 ?  204 PRO F CD  1 
ATOM   12981 N N   . VAL F  5 205 ? 59.400  71.186  156.565 1.00 315.11 ?  205 VAL F N   1 
ATOM   12982 C CA  . VAL F  5 205 ? 59.985  71.246  157.903 1.00 311.22 ?  205 VAL F CA  1 
ATOM   12983 C C   . VAL F  5 205 ? 61.079  70.193  158.043 1.00 310.46 ?  205 VAL F C   1 
ATOM   12984 O O   . VAL F  5 205 ? 60.872  69.022  157.701 1.00 311.42 ?  205 VAL F O   1 
ATOM   12985 C CB  . VAL F  5 205 ? 58.905  71.042  158.981 1.00 309.65 ?  205 VAL F CB  1 
ATOM   12986 C CG1 . VAL F  5 205 ? 59.538  70.708  160.325 1.00 306.40 ?  205 VAL F CG1 1 
ATOM   12987 C CG2 . VAL F  5 205 ? 58.014  72.269  159.087 1.00 311.13 ?  205 VAL F CG2 1 
ATOM   12988 N N   . THR F  5 206 ? 62.245  70.619  158.535 1.00 280.13 ?  206 THR F N   1 
ATOM   12989 C CA  . THR F  5 206 ? 63.371  69.742  158.845 1.00 280.06 ?  206 THR F CA  1 
ATOM   12990 C C   . THR F  5 206 ? 63.584  69.687  160.357 1.00 277.07 ?  206 THR F C   1 
ATOM   12991 O O   . THR F  5 206 ? 63.710  70.732  161.006 1.00 274.65 ?  206 THR F O   1 
ATOM   12992 C CB  . THR F  5 206 ? 64.650  70.216  158.145 1.00 280.64 ?  206 THR F CB  1 
ATOM   12993 O OG1 . THR F  5 206 ? 64.474  70.168  156.724 1.00 283.67 ?  206 THR F OG1 1 
ATOM   12994 C CG2 . THR F  5 206 ? 65.819  69.324  158.515 1.00 280.67 ?  206 THR F CG2 1 
ATOM   12995 N N   . LYS F  5 207 ? 63.621  68.475  160.913 1.00 288.21 ?  207 LYS F N   1 
ATOM   12996 C CA  . LYS F  5 207 ? 64.047  68.223  162.289 1.00 284.70 ?  207 LYS F CA  1 
ATOM   12997 C C   . LYS F  5 207 ? 65.298  67.356  162.246 1.00 285.90 ?  207 LYS F C   1 
ATOM   12998 O O   . LYS F  5 207 ? 65.332  66.350  161.529 1.00 286.98 ?  207 LYS F O   1 
ATOM   12999 C CB  . LYS F  5 207 ? 62.946  67.542  163.114 1.00 282.81 ?  207 LYS F CB  1 
ATOM   13000 C CG  . LYS F  5 207 ? 61.666  68.359  163.312 1.00 283.50 ?  207 LYS F CG  1 
ATOM   13001 C CD  . LYS F  5 207 ? 61.906  69.579  164.200 1.00 283.19 ?  207 LYS F CD  1 
ATOM   13002 C CE  . LYS F  5 207 ? 60.614  70.347  164.471 1.00 284.55 ?  207 LYS F CE  1 
ATOM   13003 N NZ  . LYS F  5 207 ? 60.809  71.466  165.438 1.00 288.74 1  207 LYS F NZ  1 
ATOM   13004 N N   . SER F  5 208 ? 66.323  67.740  163.006 1.00 283.62 ?  208 SER F N   1 
ATOM   13005 C CA  . SER F  5 208 ? 67.600  67.044  162.942 1.00 283.79 ?  208 SER F CA  1 
ATOM   13006 C C   . SER F  5 208 ? 68.259  67.008  164.314 1.00 280.49 ?  208 SER F C   1 
ATOM   13007 O O   . SER F  5 208 ? 67.866  67.723  165.240 1.00 279.78 ?  208 SER F O   1 
ATOM   13008 C CB  . SER F  5 208 ? 68.533  67.704  161.923 1.00 287.03 ?  208 SER F CB  1 
ATOM   13009 O OG  . SER F  5 208 ? 68.840  69.028  162.316 1.00 288.74 ?  208 SER F OG  1 
ATOM   13010 N N   . PHE F  5 209 ? 69.273  66.147  164.429 1.00 283.38 ?  209 PHE F N   1 
ATOM   13011 C CA  . PHE F  5 209 ? 70.197  66.145  165.554 1.00 281.71 ?  209 PHE F CA  1 
ATOM   13012 C C   . PHE F  5 209 ? 71.586  65.787  165.043 1.00 284.78 ?  209 PHE F C   1 
ATOM   13013 O O   . PHE F  5 209 ? 71.743  65.215  163.961 1.00 287.38 ?  209 PHE F O   1 
ATOM   13014 C CB  . PHE F  5 209 ? 69.765  65.154  166.650 1.00 278.99 ?  209 PHE F CB  1 
ATOM   13015 C CG  . PHE F  5 209 ? 69.788  63.708  166.214 1.00 280.65 ?  209 PHE F CG  1 
ATOM   13016 C CD1 . PHE F  5 209 ? 70.929  62.935  166.377 1.00 280.81 ?  209 PHE F CD1 1 
ATOM   13017 C CD2 . PHE F  5 209 ? 68.674  63.128  165.631 1.00 280.74 ?  209 PHE F CD2 1 
ATOM   13018 C CE1 . PHE F  5 209 ? 70.954  61.611  165.976 1.00 284.16 ?  209 PHE F CE1 1 
ATOM   13019 C CE2 . PHE F  5 209 ? 68.694  61.804  165.229 1.00 281.00 ?  209 PHE F CE2 1 
ATOM   13020 C CZ  . PHE F  5 209 ? 69.836  61.046  165.402 1.00 283.50 ?  209 PHE F CZ  1 
ATOM   13021 N N   . ASN F  5 210 ? 72.595  66.123  165.842 1.00 271.72 ?  210 ASN F N   1 
ATOM   13022 C CA  . ASN F  5 210 ? 73.971  65.704  165.606 1.00 274.03 ?  210 ASN F CA  1 
ATOM   13023 C C   . ASN F  5 210 ? 74.328  64.544  166.526 1.00 273.22 ?  210 ASN F C   1 
ATOM   13024 O O   . ASN F  5 210 ? 74.153  64.641  167.746 1.00 270.59 ?  210 ASN F O   1 
ATOM   13025 C CB  . ASN F  5 210 ? 74.933  66.873  165.821 1.00 274.49 ?  210 ASN F CB  1 
ATOM   13026 C CG  . ASN F  5 210 ? 74.716  67.993  164.822 1.00 276.00 ?  210 ASN F CG  1 
ATOM   13027 O OD1 . ASN F  5 210 ? 74.649  67.757  163.615 1.00 279.17 ?  210 ASN F OD1 1 
ATOM   13028 N ND2 . ASN F  5 210 ? 74.601  69.218  165.321 1.00 275.93 ?  210 ASN F ND2 1 
ATOM   13029 N N   . ARG F  5 211 ? 74.813  63.450  165.937 1.00 261.24 ?  211 ARG F N   1 
ATOM   13030 C CA  . ARG F  5 211 ? 75.177  62.268  166.711 1.00 262.74 ?  211 ARG F CA  1 
ATOM   13031 C C   . ARG F  5 211 ? 76.181  62.624  167.802 1.00 268.28 ?  211 ARG F C   1 
ATOM   13032 O O   . ARG F  5 211 ? 77.234  63.208  167.530 1.00 269.59 ?  211 ARG F O   1 
ATOM   13033 C CB  . ARG F  5 211 ? 75.750  61.183  165.795 1.00 267.57 ?  211 ARG F CB  1 
ATOM   13034 C CG  . ARG F  5 211 ? 76.315  59.981  166.549 1.00 269.60 ?  211 ARG F CG  1 
ATOM   13035 C CD  . ARG F  5 211 ? 76.954  58.951  165.621 1.00 275.88 ?  211 ARG F CD  1 
ATOM   13036 N NE  . ARG F  5 211 ? 78.126  59.450  164.906 1.00 280.69 ?  211 ARG F NE  1 
ATOM   13037 C CZ  . ARG F  5 211 ? 79.358  59.457  165.406 1.00 284.46 ?  211 ARG F CZ  1 
ATOM   13038 N NH1 . ARG F  5 211 ? 80.364  59.932  164.685 1.00 289.51 1  211 ARG F NH1 1 
ATOM   13039 N NH2 . ARG F  5 211 ? 79.588  58.980  166.623 1.00 285.23 ?  211 ARG F NH2 1 
ATOM   13040 N N   . GLY F  5 212 ? 75.847  62.269  169.038 1.00 246.51 ?  212 GLY F N   1 
ATOM   13041 C CA  . GLY F  5 212 ? 76.682  62.586  170.182 1.00 245.82 ?  212 GLY F CA  1 
ATOM   13042 C C   . GLY F  5 212 ? 76.127  63.718  171.024 1.00 242.60 ?  212 GLY F C   1 
ATOM   13043 O O   . GLY F  5 212 ? 75.809  64.789  170.508 1.00 240.92 ?  212 GLY F O   1 
ATOM   13044 N N   . GLN G  4 1   ? 84.466  70.591  283.975 1.00 195.26 ?  1   GLN G N   1 
ATOM   13045 C CA  . GLN G  4 1   ? 85.660  69.830  283.612 1.00 192.74 ?  1   GLN G CA  1 
ATOM   13046 C C   . GLN G  4 1   ? 85.928  68.748  284.640 1.00 193.26 ?  1   GLN G C   1 
ATOM   13047 O O   . GLN G  4 1   ? 86.353  67.648  284.289 1.00 196.46 ?  1   GLN G O   1 
ATOM   13048 C CB  . GLN G  4 1   ? 86.903  70.729  283.478 1.00 190.00 ?  1   GLN G CB  1 
ATOM   13049 C CG  . GLN G  4 1   ? 86.657  72.175  283.079 1.00 190.11 ?  1   GLN G CG  1 
ATOM   13050 C CD  . GLN G  4 1   ? 86.207  73.026  284.234 1.00 190.82 ?  1   GLN G CD  1 
ATOM   13051 O OE1 . GLN G  4 1   ? 86.826  73.047  285.286 1.00 193.39 ?  1   GLN G OE1 1 
ATOM   13052 N NE2 . GLN G  4 1   ? 85.116  73.730  284.049 1.00 183.86 ?  1   GLN G NE2 1 
ATOM   13053 N N   . GLU G  4 2   ? 85.636  69.054  285.902 1.00 165.56 ?  2   GLU G N   1 
ATOM   13054 C CA  . GLU G  4 2   ? 85.982  68.188  287.023 1.00 164.86 ?  2   GLU G CA  1 
ATOM   13055 C C   . GLU G  4 2   ? 84.866  67.168  287.202 1.00 169.64 ?  2   GLU G C   1 
ATOM   13056 O O   . GLU G  4 2   ? 83.788  67.493  287.710 1.00 169.22 ?  2   GLU G O   1 
ATOM   13057 C CB  . GLU G  4 2   ? 86.195  69.023  288.281 1.00 159.25 ?  2   GLU G CB  1 
ATOM   13058 C CG  . GLU G  4 2   ? 87.161  70.177  288.055 1.00 156.24 ?  2   GLU G CG  1 
ATOM   13059 C CD  . GLU G  4 2   ? 87.585  70.852  289.339 1.00 151.56 ?  2   GLU G CD  1 
ATOM   13060 O OE1 . GLU G  4 2   ? 87.642  72.101  289.362 1.00 148.10 ?  2   GLU G OE1 1 
ATOM   13061 O OE2 . GLU G  4 2   ? 87.856  70.135  290.324 1.00 152.02 -1 2   GLU G OE2 1 
ATOM   13062 N N   . VAL G  4 3   ? 85.131  65.928  286.792 1.00 142.91 ?  3   VAL G N   1 
ATOM   13063 C CA  . VAL G  4 3   ? 84.110  64.894  286.704 1.00 146.79 ?  3   VAL G CA  1 
ATOM   13064 C C   . VAL G  4 3   ? 84.718  63.554  287.084 1.00 149.63 ?  3   VAL G C   1 
ATOM   13065 O O   . VAL G  4 3   ? 85.930  63.341  286.998 1.00 148.82 ?  3   VAL G O   1 
ATOM   13066 C CB  . VAL G  4 3   ? 83.487  64.791  285.294 1.00 146.68 ?  3   VAL G CB  1 
ATOM   13067 C CG1 . VAL G  4 3   ? 82.776  66.077  284.913 1.00 143.97 ?  3   VAL G CG1 1 
ATOM   13068 C CG2 . VAL G  4 3   ? 84.562  64.457  284.278 1.00 147.86 ?  3   VAL G CG2 1 
ATOM   13069 N N   . LEU G  4 4   ? 83.844  62.645  287.503 1.00 140.96 ?  4   LEU G N   1 
ATOM   13070 C CA  . LEU G  4 4   ? 84.190  61.259  287.771 1.00 143.64 ?  4   LEU G CA  1 
ATOM   13071 C C   . LEU G  4 4   ? 83.347  60.379  286.860 1.00 145.00 ?  4   LEU G C   1 
ATOM   13072 O O   . LEU G  4 4   ? 82.125  60.543  286.793 1.00 143.94 ?  4   LEU G O   1 
ATOM   13073 C CB  . LEU G  4 4   ? 83.952  60.903  289.242 1.00 143.29 ?  4   LEU G CB  1 
ATOM   13074 C CG  . LEU G  4 4   ? 84.818  61.631  290.273 1.00 139.32 ?  4   LEU G CG  1 
ATOM   13075 C CD1 . LEU G  4 4   ? 84.237  61.476  291.674 1.00 138.46 ?  4   LEU G CD1 1 
ATOM   13076 C CD2 . LEU G  4 4   ? 86.253  61.131  290.220 1.00 139.84 ?  4   LEU G CD2 1 
ATOM   13077 N N   . VAL G  4 5   ? 84.000  59.465  286.150 1.00 142.94 ?  5   VAL G N   1 
ATOM   13078 C CA  . VAL G  4 5   ? 83.337  58.568  285.211 1.00 145.08 ?  5   VAL G CA  1 
ATOM   13079 C C   . VAL G  4 5   ? 83.454  57.149  285.752 1.00 149.61 ?  5   VAL G C   1 
ATOM   13080 O O   . VAL G  4 5   ? 84.563  56.656  285.990 1.00 151.47 ?  5   VAL G O   1 
ATOM   13081 C CB  . VAL G  4 5   ? 83.945  58.678  283.804 1.00 144.95 ?  5   VAL G CB  1 
ATOM   13082 C CG1 . VAL G  4 5   ? 83.193  57.791  282.824 1.00 147.49 ?  5   VAL G CG1 1 
ATOM   13083 C CG2 . VAL G  4 5   ? 83.948  60.132  283.329 1.00 141.05 ?  5   VAL G CG2 1 
ATOM   13084 N N   . GLN G  4 6   ? 82.314  56.494  285.939 1.00 144.38 ?  6   GLN G N   1 
ATOM   13085 C CA  . GLN G  4 6   ? 82.257  55.171  286.539 1.00 145.09 ?  6   GLN G CA  1 
ATOM   13086 C C   . GLN G  4 6   ? 81.967  54.111  285.485 1.00 147.40 ?  6   GLN G C   1 
ATOM   13087 O O   . GLN G  4 6   ? 81.433  54.397  284.410 1.00 148.49 ?  6   GLN G O   1 
ATOM   13088 C CB  . GLN G  4 6   ? 81.193  55.108  287.637 1.00 144.32 ?  6   GLN G CB  1 
ATOM   13089 C CG  . GLN G  4 6   ? 81.456  56.025  288.805 1.00 142.22 ?  6   GLN G CG  1 
ATOM   13090 C CD  . GLN G  4 6   ? 80.447  55.827  289.910 1.00 141.80 ?  6   GLN G CD  1 
ATOM   13091 O OE1 . GLN G  4 6   ? 79.847  56.782  290.399 1.00 140.64 ?  6   GLN G OE1 1 
ATOM   13092 N NE2 . GLN G  4 6   ? 80.251  54.576  290.309 1.00 142.86 ?  6   GLN G NE2 1 
ATOM   13093 N N   . SER G  4 7   ? 82.328  52.875  285.816 1.00 145.66 ?  7   SER G N   1 
ATOM   13094 C CA  . SER G  4 7   ? 82.077  51.747  284.936 1.00 149.60 ?  7   SER G CA  1 
ATOM   13095 C C   . SER G  4 7   ? 80.580  51.466  284.823 1.00 150.75 ?  7   SER G C   1 
ATOM   13096 O O   . SER G  4 7   ? 79.765  51.931  285.625 1.00 149.26 ?  7   SER G O   1 
ATOM   13097 C CB  . SER G  4 7   ? 82.804  50.502  285.441 1.00 154.70 ?  7   SER G CB  1 
ATOM   13098 O OG  . SER G  4 7   ? 82.462  50.233  286.789 1.00 157.26 ?  7   SER G OG  1 
ATOM   13099 N N   . GLY G  4 8   ? 80.229  50.684  283.808 1.00 159.26 ?  8   GLY G N   1 
ATOM   13100 C CA  . GLY G  4 8   ? 78.839  50.422  283.504 1.00 160.40 ?  8   GLY G CA  1 
ATOM   13101 C C   . GLY G  4 8   ? 78.193  49.454  284.477 1.00 164.85 ?  8   GLY G C   1 
ATOM   13102 O O   . GLY G  4 8   ? 78.836  48.847  285.336 1.00 167.90 ?  8   GLY G O   1 
ATOM   13103 N N   . ALA G  4 9   ? 76.874  49.326  284.329 1.00 170.67 ?  9   ALA G N   1 
ATOM   13104 C CA  . ALA G  4 9   ? 76.080  48.460  285.191 1.00 174.96 ?  9   ALA G CA  1 
ATOM   13105 C C   . ALA G  4 9   ? 76.580  47.020  285.143 1.00 181.44 ?  9   ALA G C   1 
ATOM   13106 O O   . ALA G  4 9   ? 77.099  46.551  284.125 1.00 182.43 ?  9   ALA G O   1 
ATOM   13107 C CB  . ALA G  4 9   ? 74.606  48.518  284.786 1.00 174.44 ?  9   ALA G CB  1 
ATOM   13108 N N   . GLU G  4 10  ? 76.413  46.312  286.263 1.00 164.00 ?  10  GLU G N   1 
ATOM   13109 C CA  . GLU G  4 10  ? 76.868  44.934  286.392 1.00 170.84 ?  10  GLU G CA  1 
ATOM   13110 C C   . GLU G  4 10  ? 75.810  44.086  287.088 1.00 176.53 ?  10  GLU G C   1 
ATOM   13111 O O   . GLU G  4 10  ? 75.061  44.573  287.941 1.00 175.46 ?  10  GLU G O   1 
ATOM   13112 C CB  . GLU G  4 10  ? 78.188  44.851  287.175 1.00 172.22 ?  10  GLU G CB  1 
ATOM   13113 C CG  . GLU G  4 10  ? 79.343  45.598  286.528 1.00 167.23 ?  10  GLU G CG  1 
ATOM   13114 C CD  . GLU G  4 10  ? 80.673  44.894  286.716 1.00 169.90 ?  10  GLU G CD  1 
ATOM   13115 O OE1 . GLU G  4 10  ? 80.676  43.656  286.883 1.00 175.59 ?  10  GLU G OE1 1 
ATOM   13116 O OE2 . GLU G  4 10  ? 81.717  45.579  286.690 1.00 165.96 -1 10  GLU G OE2 1 
ATOM   13117 N N   . VAL G  4 11  ? 75.757  42.809  286.710 1.00 174.05 ?  11  VAL G N   1 
ATOM   13118 C CA  . VAL G  4 11  ? 74.953  41.798  287.389 1.00 179.73 ?  11  VAL G CA  1 
ATOM   13119 C C   . VAL G  4 11  ? 75.888  40.702  287.886 1.00 185.75 ?  11  VAL G C   1 
ATOM   13120 O O   . VAL G  4 11  ? 76.756  40.235  287.139 1.00 186.54 ?  11  VAL G O   1 
ATOM   13121 C CB  . VAL G  4 11  ? 73.865  41.219  286.463 1.00 182.66 ?  11  VAL G CB  1 
ATOM   13122 C CG1 . VAL G  4 11  ? 73.198  40.020  287.112 1.00 192.22 ?  11  VAL G CG1 1 
ATOM   13123 C CG2 . VAL G  4 11  ? 72.830  42.285  286.112 1.00 178.46 ?  11  VAL G CG2 1 
ATOM   13124 N N   . LYS G  4 12  ? 75.710  40.292  289.142 1.00 194.43 ?  12  LYS G N   1 
ATOM   13125 C CA  . LYS G  4 12  ? 76.457  39.180  289.715 1.00 200.61 ?  12  LYS G CA  1 
ATOM   13126 C C   . LYS G  4 12  ? 75.522  38.325  290.561 1.00 207.64 ?  12  LYS G C   1 
ATOM   13127 O O   . LYS G  4 12  ? 74.474  38.782  291.021 1.00 209.69 ?  12  LYS G O   1 
ATOM   13128 C CB  . LYS G  4 12  ? 77.638  39.673  290.567 1.00 199.71 ?  12  LYS G CB  1 
ATOM   13129 C CG  . LYS G  4 12  ? 78.786  40.284  289.773 1.00 192.52 ?  12  LYS G CG  1 
ATOM   13130 C CD  . LYS G  4 12  ? 79.504  39.252  288.921 1.00 194.06 ?  12  LYS G CD  1 
ATOM   13131 C CE  . LYS G  4 12  ? 80.747  39.848  288.280 1.00 190.35 ?  12  LYS G CE  1 
ATOM   13132 N NZ  . LYS G  4 12  ? 81.460  38.868  287.418 1.00 191.25 1  12  LYS G NZ  1 
ATOM   13133 N N   . LYS G  4 13  ? 75.907  37.063  290.745 1.00 199.64 ?  13  LYS G N   1 
ATOM   13134 C CA  . LYS G  4 13  ? 75.178  36.136  291.597 1.00 205.50 ?  13  LYS G CA  1 
ATOM   13135 C C   . LYS G  4 13  ? 75.642  36.250  293.044 1.00 205.15 ?  13  LYS G C   1 
ATOM   13136 O O   . LYS G  4 13  ? 76.751  36.717  293.319 1.00 200.63 ?  13  LYS G O   1 
ATOM   13137 C CB  . LYS G  4 13  ? 75.363  34.706  291.092 1.00 209.07 ?  13  LYS G CB  1 
ATOM   13138 C CG  . LYS G  4 13  ? 76.762  34.146  291.277 1.00 209.86 ?  13  LYS G CG  1 
ATOM   13139 C CD  . LYS G  4 13  ? 76.941  32.862  290.483 1.00 215.53 ?  13  LYS G CD  1 
ATOM   13140 C CE  . LYS G  4 13  ? 78.289  32.218  290.759 1.00 216.17 ?  13  LYS G CE  1 
ATOM   13141 N NZ  . LYS G  4 13  ? 78.602  31.149  289.771 1.00 218.42 1  13  LYS G NZ  1 
ATOM   13142 N N   . PRO G  4 14  ? 74.804  35.840  294.000 1.00 192.02 ?  14  PRO G N   1 
ATOM   13143 C CA  . PRO G  4 14  ? 75.212  35.889  295.410 1.00 189.55 ?  14  PRO G CA  1 
ATOM   13144 C C   . PRO G  4 14  ? 76.476  35.083  295.677 1.00 190.97 ?  14  PRO G C   1 
ATOM   13145 O O   . PRO G  4 14  ? 76.685  34.006  295.114 1.00 195.49 ?  14  PRO G O   1 
ATOM   13146 C CB  . PRO G  4 14  ? 74.005  35.301  296.149 1.00 192.76 ?  14  PRO G CB  1 
ATOM   13147 C CG  . PRO G  4 14  ? 72.850  35.563  295.245 1.00 194.04 ?  14  PRO G CG  1 
ATOM   13148 C CD  . PRO G  4 14  ? 73.387  35.461  293.847 1.00 195.68 ?  14  PRO G CD  1 
ATOM   13149 N N   . GLY G  4 15  ? 77.323  35.622  296.552 1.00 186.77 ?  15  GLY G N   1 
ATOM   13150 C CA  . GLY G  4 15  ? 78.555  34.980  296.939 1.00 187.50 ?  15  GLY G CA  1 
ATOM   13151 C C   . GLY G  4 15  ? 79.769  35.376  296.126 1.00 184.39 ?  15  GLY G C   1 
ATOM   13152 O O   . GLY G  4 15  ? 80.897  35.176  296.591 1.00 183.22 ?  15  GLY G O   1 
ATOM   13153 N N   . ALA G  4 16  ? 79.574  35.931  294.933 1.00 196.17 ?  16  ALA G N   1 
ATOM   13154 C CA  . ALA G  4 16  ? 80.678  36.332  294.071 1.00 192.69 ?  16  ALA G CA  1 
ATOM   13155 C C   . ALA G  4 16  ? 81.185  37.715  294.482 1.00 186.04 ?  16  ALA G C   1 
ATOM   13156 O O   . ALA G  4 16  ? 80.769  38.285  295.494 1.00 183.50 ?  16  ALA G O   1 
ATOM   13157 C CB  . ALA G  4 16  ? 80.243  36.289  292.608 1.00 193.55 ?  16  ALA G CB  1 
ATOM   13158 N N   . SER G  4 17  ? 82.109  38.264  293.694 1.00 195.18 ?  17  SER G N   1 
ATOM   13159 C CA  . SER G  4 17  ? 82.664  39.590  293.919 1.00 188.66 ?  17  SER G CA  1 
ATOM   13160 C C   . SER G  4 17  ? 82.526  40.409  292.643 1.00 186.18 ?  17  SER G C   1 
ATOM   13161 O O   . SER G  4 17  ? 82.536  39.864  291.534 1.00 187.65 ?  17  SER G O   1 
ATOM   13162 C CB  . SER G  4 17  ? 84.138  39.516  294.342 1.00 185.53 ?  17  SER G CB  1 
ATOM   13163 O OG  . SER G  4 17  ? 84.284  38.743  295.521 1.00 187.80 ?  17  SER G OG  1 
ATOM   13164 N N   . VAL G  4 18  ? 82.384  41.724  292.809 1.00 186.24 ?  18  VAL G N   1 
ATOM   13165 C CA  . VAL G  4 18  ? 82.294  42.664  291.697 1.00 183.28 ?  18  VAL G CA  1 
ATOM   13166 C C   . VAL G  4 18  ? 83.338  43.757  291.889 1.00 176.29 ?  18  VAL G C   1 
ATOM   13167 O O   . VAL G  4 18  ? 83.598  44.194  293.017 1.00 173.01 ?  18  VAL G O   1 
ATOM   13168 C CB  . VAL G  4 18  ? 80.876  43.265  291.569 1.00 185.42 ?  18  VAL G CB  1 
ATOM   13169 C CG1 . VAL G  4 18  ? 80.534  44.112  292.791 1.00 180.94 ?  18  VAL G CG1 1 
ATOM   13170 C CG2 . VAL G  4 18  ? 80.731  44.068  290.268 1.00 180.15 ?  18  VAL G CG2 1 
ATOM   13171 N N   . LYS G  4 19  ? 83.958  44.176  290.787 1.00 175.07 ?  19  LYS G N   1 
ATOM   13172 C CA  . LYS G  4 19  ? 84.945  45.248  290.791 1.00 168.43 ?  19  LYS G CA  1 
ATOM   13173 C C   . LYS G  4 19  ? 84.429  46.402  289.946 1.00 164.59 ?  19  LYS G C   1 
ATOM   13174 O O   . LYS G  4 19  ? 84.183  46.242  288.745 1.00 163.82 ?  19  LYS G O   1 
ATOM   13175 C CB  . LYS G  4 19  ? 86.299  44.768  290.271 1.00 166.83 ?  19  LYS G CB  1 
ATOM   13176 C CG  . LYS G  4 19  ? 87.375  45.834  290.361 1.00 160.43 ?  19  LYS G CG  1 
ATOM   13177 C CD  . LYS G  4 19  ? 88.706  45.379  289.789 1.00 159.89 ?  19  LYS G CD  1 
ATOM   13178 C CE  . LYS G  4 19  ? 89.713  45.159  290.909 1.00 158.95 ?  19  LYS G CE  1 
ATOM   13179 N NZ  . LYS G  4 19  ? 91.045  45.747  290.591 1.00 154.82 1  19  LYS G NZ  1 
ATOM   13180 N N   . VAL G  4 20  ? 84.295  47.562  290.572 1.00 161.44 ?  20  VAL G N   1 
ATOM   13181 C CA  . VAL G  4 20  ? 83.751  48.754  289.945 1.00 156.60 ?  20  VAL G CA  1 
ATOM   13182 C C   . VAL G  4 20  ? 84.853  49.811  289.897 1.00 150.54 ?  20  VAL G C   1 
ATOM   13183 O O   . VAL G  4 20  ? 85.651  49.928  290.831 1.00 148.78 ?  20  VAL G O   1 
ATOM   13184 C CB  . VAL G  4 20  ? 82.504  49.234  290.726 1.00 155.44 ?  20  VAL G CB  1 
ATOM   13185 C CG1 . VAL G  4 20  ? 82.299  50.713  290.533 1.00 153.18 ?  20  VAL G CG1 1 
ATOM   13186 C CG2 . VAL G  4 20  ? 81.207  48.424  290.338 1.00 159.52 ?  20  VAL G CG2 1 
ATOM   13187 N N   . SER G  4 21  ? 84.904  50.582  288.812 1.00 157.73 ?  21  SER G N   1 
ATOM   13188 C CA  . SER G  4 21  ? 85.964  51.565  288.633 1.00 152.29 ?  21  SER G CA  1 
ATOM   13189 C C   . SER G  4 21  ? 85.388  52.971  288.513 1.00 148.17 ?  21  SER G C   1 
ATOM   13190 O O   . SER G  4 21  ? 84.213  53.164  288.189 1.00 148.42 ?  21  SER G O   1 
ATOM   13191 C CB  . SER G  4 21  ? 86.816  51.239  287.403 1.00 151.34 ?  21  SER G CB  1 
ATOM   13192 O OG  . SER G  4 21  ? 86.034  51.349  286.231 1.00 151.21 ?  21  SER G OG  1 
ATOM   13193 N N   . CYS G  4 22  ? 86.237  53.947  288.825 1.00 160.97 ?  22  CYS G N   1 
ATOM   13194 C CA  . CYS G  4 22  ? 85.874  55.359  288.806 1.00 156.72 ?  22  CYS G CA  1 
ATOM   13195 C C   . CYS G  4 22  ? 87.112  56.148  288.409 1.00 151.81 ?  22  CYS G C   1 
ATOM   13196 O O   . CYS G  4 22  ? 88.099  56.152  289.150 1.00 149.42 ?  22  CYS G O   1 
ATOM   13197 C CB  . CYS G  4 22  ? 85.352  55.788  290.181 1.00 156.49 ?  22  CYS G CB  1 
ATOM   13198 S SG  . CYS G  4 22  ? 85.226  57.563  290.542 1.00 149.62 ?  22  CYS G SG  1 
ATOM   13199 N N   . ARG G  4 23  ? 87.071  56.808  287.254 1.00 148.50 ?  23  ARG G N   1 
ATOM   13200 C CA  . ARG G  4 23  ? 88.214  57.555  286.742 1.00 144.70 ?  23  ARG G CA  1 
ATOM   13201 C C   . ARG G  4 23  ? 87.965  59.054  286.849 1.00 140.32 ?  23  ARG G C   1 
ATOM   13202 O O   . ARG G  4 23  ? 86.893  59.543  286.477 1.00 140.30 ?  23  ARG G O   1 
ATOM   13203 C CB  . ARG G  4 23  ? 88.528  57.181  285.291 1.00 145.91 ?  23  ARG G CB  1 
ATOM   13204 C CG  . ARG G  4 23  ? 89.710  57.966  284.742 1.00 142.79 ?  23  ARG G CG  1 
ATOM   13205 C CD  . ARG G  4 23  ? 90.263  57.414  283.444 1.00 144.90 ?  23  ARG G CD  1 
ATOM   13206 N NE  . ARG G  4 23  ? 91.423  58.187  283.008 1.00 142.49 ?  23  ARG G NE  1 
ATOM   13207 C CZ  . ARG G  4 23  ? 92.414  57.705  282.266 1.00 144.31 ?  23  ARG G CZ  1 
ATOM   13208 N NH1 . ARG G  4 23  ? 93.430  58.487  281.926 1.00 142.41 1  23  ARG G NH1 1 
ATOM   13209 N NH2 . ARG G  4 23  ? 92.387  56.445  281.858 1.00 148.34 ?  23  ARG G NH2 1 
ATOM   13210 N N   . ALA G  4 24  ? 88.967  59.773  287.352 1.00 146.98 ?  24  ALA G N   1 
ATOM   13211 C CA  . ALA G  4 24  ? 88.887  61.209  287.572 1.00 144.60 ?  24  ALA G CA  1 
ATOM   13212 C C   . ALA G  4 24  ? 89.406  61.959  286.354 1.00 145.31 ?  24  ALA G C   1 
ATOM   13213 O O   . ALA G  4 24  ? 90.449  61.604  285.795 1.00 146.56 ?  24  ALA G O   1 
ATOM   13214 C CB  . ALA G  4 24  ? 89.688  61.604  288.812 1.00 143.25 ?  24  ALA G CB  1 
ATOM   13215 N N   . PHE G  4 25  ? 88.671  62.985  285.939 1.00 152.19 ?  25  PHE G N   1 
ATOM   13216 C CA  . PHE G  4 25  ? 89.104  63.857  284.861 1.00 150.67 ?  25  PHE G CA  1 
ATOM   13217 C C   . PHE G  4 25  ? 89.070  65.309  285.315 1.00 146.36 ?  25  PHE G C   1 
ATOM   13218 O O   . PHE G  4 25  ? 88.217  65.709  286.113 1.00 145.31 ?  25  PHE G O   1 
ATOM   13219 C CB  . PHE G  4 25  ? 88.232  63.690  283.618 1.00 153.43 ?  25  PHE G CB  1 
ATOM   13220 C CG  . PHE G  4 25  ? 88.282  62.318  283.028 1.00 157.21 ?  25  PHE G CG  1 
ATOM   13221 C CD1 . PHE G  4 25  ? 89.179  62.026  282.017 1.00 158.30 ?  25  PHE G CD1 1 
ATOM   13222 C CD2 . PHE G  4 25  ? 87.447  61.316  283.489 1.00 159.85 ?  25  PHE G CD2 1 
ATOM   13223 C CE1 . PHE G  4 25  ? 89.235  60.767  281.465 1.00 161.84 ?  25  PHE G CE1 1 
ATOM   13224 C CE2 . PHE G  4 25  ? 87.498  60.052  282.941 1.00 163.30 ?  25  PHE G CE2 1 
ATOM   13225 C CZ  . PHE G  4 25  ? 88.393  59.778  281.926 1.00 164.92 ?  25  PHE G CZ  1 
ATOM   13226 N N   . GLY G  4 26  ? 90.008  66.092  284.784 1.00 159.50 ?  26  GLY G N   1 
ATOM   13227 C CA  . GLY G  4 26  ? 90.012  67.530  284.954 1.00 154.94 ?  26  GLY G CA  1 
ATOM   13228 C C   . GLY G  4 26  ? 90.581  68.038  286.257 1.00 151.99 ?  26  GLY G C   1 
ATOM   13229 O O   . GLY G  4 26  ? 90.501  69.244  286.517 1.00 148.22 ?  26  GLY G O   1 
ATOM   13230 N N   . TYR G  4 27  ? 91.158  67.169  287.083 1.00 148.23 ?  27  TYR G N   1 
ATOM   13231 C CA  . TYR G  4 27  ? 91.813  67.600  288.307 1.00 143.85 ?  27  TYR G CA  1 
ATOM   13232 C C   . TYR G  4 27  ? 92.857  66.558  288.674 1.00 145.27 ?  27  TYR G C   1 
ATOM   13233 O O   . TYR G  4 27  ? 92.972  65.512  288.029 1.00 150.19 ?  27  TYR G O   1 
ATOM   13234 C CB  . TYR G  4 27  ? 90.812  67.805  289.451 1.00 142.54 ?  27  TYR G CB  1 
ATOM   13235 C CG  . TYR G  4 27  ? 90.337  66.529  290.123 1.00 144.02 ?  27  TYR G CG  1 
ATOM   13236 C CD1 . TYR G  4 27  ? 89.317  65.763  289.577 1.00 149.10 ?  27  TYR G CD1 1 
ATOM   13237 C CD2 . TYR G  4 27  ? 90.899  66.108  291.322 1.00 141.72 ?  27  TYR G CD2 1 
ATOM   13238 C CE1 . TYR G  4 27  ? 88.882  64.602  290.201 1.00 151.41 ?  27  TYR G CE1 1 
ATOM   13239 C CE2 . TYR G  4 27  ? 90.475  64.950  291.949 1.00 144.57 ?  27  TYR G CE2 1 
ATOM   13240 C CZ  . TYR G  4 27  ? 89.468  64.201  291.386 1.00 148.90 ?  27  TYR G CZ  1 
ATOM   13241 O OH  . TYR G  4 27  ? 89.046  63.050  292.015 1.00 151.96 ?  27  TYR G OH  1 
ATOM   13242 N N   . THR G  4 28  ? 93.617  66.848  289.726 1.00 161.64 ?  28  THR G N   1 
ATOM   13243 C CA  . THR G  4 28  ? 94.683  65.957  290.170 1.00 163.10 ?  28  THR G CA  1 
ATOM   13244 C C   . THR G  4 28  ? 94.077  64.847  291.020 1.00 164.48 ?  28  THR G C   1 
ATOM   13245 O O   . THR G  4 28  ? 93.594  65.097  292.130 1.00 162.52 ?  28  THR G O   1 
ATOM   13246 C CB  . THR G  4 28  ? 95.743  66.731  290.947 1.00 162.19 ?  28  THR G CB  1 
ATOM   13247 O OG1 . THR G  4 28  ? 96.306  67.749  290.108 1.00 161.88 ?  28  THR G OG1 1 
ATOM   13248 C CG2 . THR G  4 28  ? 96.852  65.793  291.404 1.00 164.64 ?  28  THR G CG2 1 
ATOM   13249 N N   . PHE G  4 29  ? 94.117  63.620  290.494 1.00 144.94 ?  29  PHE G N   1 
ATOM   13250 C CA  . PHE G  4 29  ? 93.491  62.477  291.153 1.00 147.62 ?  29  PHE G CA  1 
ATOM   13251 C C   . PHE G  4 29  ? 93.973  62.315  292.590 1.00 145.64 ?  29  PHE G C   1 
ATOM   13252 O O   . PHE G  4 29  ? 93.189  61.975  293.484 1.00 145.73 ?  29  PHE G O   1 
ATOM   13253 C CB  . PHE G  4 29  ? 93.769  61.212  290.338 1.00 152.79 ?  29  PHE G CB  1 
ATOM   13254 C CG  . PHE G  4 29  ? 93.271  59.949  290.975 1.00 156.33 ?  29  PHE G CG  1 
ATOM   13255 C CD1 . PHE G  4 29  ? 91.924  59.775  291.250 1.00 157.49 ?  29  PHE G CD1 1 
ATOM   13256 C CD2 . PHE G  4 29  ? 94.150  58.924  291.280 1.00 159.00 ?  29  PHE G CD2 1 
ATOM   13257 C CE1 . PHE G  4 29  ? 91.466  58.605  291.832 1.00 161.26 ?  29  PHE G CE1 1 
ATOM   13258 C CE2 . PHE G  4 29  ? 93.699  57.752  291.860 1.00 162.61 ?  29  PHE G CE2 1 
ATOM   13259 C CZ  . PHE G  4 29  ? 92.356  57.592  292.136 1.00 163.77 ?  29  PHE G CZ  1 
ATOM   13260 N N   . THR G  4 30  ? 95.254  62.575  292.833 1.00 166.26 ?  30  THR G N   1 
ATOM   13261 C CA  . THR G  4 30  ? 95.853  62.364  294.144 1.00 165.18 ?  30  THR G CA  1 
ATOM   13262 C C   . THR G  4 30  ? 95.612  63.514  295.113 1.00 160.19 ?  30  THR G C   1 
ATOM   13263 O O   . THR G  4 30  ? 96.142  63.477  296.229 1.00 160.39 ?  30  THR G O   1 
ATOM   13264 C CB  . THR G  4 30  ? 97.357  62.145  293.993 1.00 166.61 ?  30  THR G CB  1 
ATOM   13265 O OG1 . THR G  4 30  ? 97.915  63.220  293.224 1.00 164.30 ?  30  THR G OG1 1 
ATOM   13266 C CG2 . THR G  4 30  ? 97.619  60.837  293.283 1.00 171.97 ?  30  THR G CG2 1 
ATOM   13267 N N   . GLY G  4 31  ? 94.839  64.523  294.722 1.00 163.66 ?  31  GLY G N   1 
ATOM   13268 C CA  . GLY G  4 31  ? 94.655  65.694  295.552 1.00 160.76 ?  31  GLY G CA  1 
ATOM   13269 C C   . GLY G  4 31  ? 93.457  65.699  296.472 1.00 160.21 ?  31  GLY G C   1 
ATOM   13270 O O   . GLY G  4 31  ? 93.304  66.642  297.254 1.00 159.29 ?  31  GLY G O   1 
ATOM   13271 N N   . ASN G  4 32  ? 92.591  64.688  296.406 1.00 152.61 ?  32  ASN G N   1 
ATOM   13272 C CA  . ASN G  4 32  ? 91.384  64.692  297.220 1.00 152.00 ?  32  ASN G CA  1 
ATOM   13273 C C   . ASN G  4 32  ? 91.049  63.277  297.657 1.00 155.92 ?  32  ASN G C   1 
ATOM   13274 O O   . ASN G  4 32  ? 91.107  62.346  296.850 1.00 160.09 ?  32  ASN G O   1 
ATOM   13275 C CB  . ASN G  4 32  ? 90.189  65.263  296.453 1.00 151.78 ?  32  ASN G CB  1 
ATOM   13276 C CG  . ASN G  4 32  ? 90.424  66.672  295.962 1.00 148.19 ?  32  ASN G CG  1 
ATOM   13277 O OD1 . ASN G  4 32  ? 91.131  66.884  294.977 1.00 148.79 ?  32  ASN G OD1 1 
ATOM   13278 N ND2 . ASN G  4 32  ? 89.829  67.646  296.641 1.00 146.41 ?  32  ASN G ND2 1 
ATOM   13279 N N   . ALA G  4 33  ? 90.667  63.131  298.924 1.00 148.88 ?  33  ALA G N   1 
ATOM   13280 C CA  . ALA G  4 33  ? 90.134  61.863  299.394 1.00 153.34 ?  33  ALA G CA  1 
ATOM   13281 C C   . ALA G  4 33  ? 88.873  61.524  298.609 1.00 155.14 ?  33  ALA G C   1 
ATOM   13282 O O   . ALA G  4 33  ? 88.158  62.409  298.132 1.00 153.57 ?  33  ALA G O   1 
ATOM   13283 C CB  . ALA G  4 33  ? 89.836  61.933  300.892 1.00 152.86 ?  33  ALA G CB  1 
ATOM   13284 N N   . LEU G  4 34  ? 88.599  60.231  298.468 1.00 155.96 ?  34  LEU G N   1 
ATOM   13285 C CA  . LEU G  4 34  ? 87.485  59.784  297.645 1.00 155.30 ?  34  LEU G CA  1 
ATOM   13286 C C   . LEU G  4 34  ? 86.603  58.834  298.436 1.00 157.79 ?  34  LEU G C   1 
ATOM   13287 O O   . LEU G  4 34  ? 87.093  57.852  299.000 1.00 160.49 ?  34  LEU G O   1 
ATOM   13288 C CB  . LEU G  4 34  ? 87.986  59.099  296.372 1.00 155.21 ?  34  LEU G CB  1 
ATOM   13289 C CG  . LEU G  4 34  ? 86.892  58.774  295.358 1.00 154.53 ?  34  LEU G CG  1 
ATOM   13290 C CD1 . LEU G  4 34  ? 86.570  60.006  294.527 1.00 151.84 ?  34  LEU G CD1 1 
ATOM   13291 C CD2 . LEU G  4 34  ? 87.316  57.625  294.471 1.00 156.07 ?  34  LEU G CD2 1 
ATOM   13292 N N   . HIS G  4 35  ? 85.303  59.120  298.450 1.00 153.72 ?  35  HIS G N   1 
ATOM   13293 C CA  . HIS G  4 35  ? 84.305  58.321  299.144 1.00 156.39 ?  35  HIS G CA  1 
ATOM   13294 C C   . HIS G  4 35  ? 83.636  57.365  298.165 1.00 157.02 ?  35  HIS G C   1 
ATOM   13295 O O   . HIS G  4 35  ? 83.569  57.626  296.962 1.00 154.98 ?  35  HIS G O   1 
ATOM   13296 C CB  . HIS G  4 35  ? 83.224  59.201  299.782 1.00 156.36 ?  35  HIS G CB  1 
ATOM   13297 C CG  . HIS G  4 35  ? 83.744  60.208  300.760 1.00 156.13 ?  35  HIS G CG  1 
ATOM   13298 N ND1 . HIS G  4 35  ? 83.837  59.957  302.112 1.00 159.11 ?  35  HIS G ND1 1 
ATOM   13299 C CD2 . HIS G  4 35  ? 84.184  61.476  300.583 1.00 153.71 ?  35  HIS G CD2 1 
ATOM   13300 C CE1 . HIS G  4 35  ? 84.313  61.026  302.725 1.00 158.49 ?  35  HIS G CE1 1 
ATOM   13301 N NE2 . HIS G  4 35  ? 84.537  61.960  301.819 1.00 155.18 ?  35  HIS G NE2 1 
ATOM   13302 N N   . TRP G  4 36  ? 83.143  56.249  298.696 1.00 153.54 ?  36  TRP G N   1 
ATOM   13303 C CA  . TRP G  4 36  ? 82.198  55.395  297.990 1.00 154.79 ?  36  TRP G CA  1 
ATOM   13304 C C   . TRP G  4 36  ? 80.899  55.348  298.781 1.00 157.16 ?  36  TRP G C   1 
ATOM   13305 O O   . TRP G  4 36  ? 80.908  55.058  299.982 1.00 159.86 ?  36  TRP G O   1 
ATOM   13306 C CB  . TRP G  4 36  ? 82.757  53.983  297.771 1.00 157.19 ?  36  TRP G CB  1 
ATOM   13307 C CG  . TRP G  4 36  ? 83.918  53.935  296.817 1.00 155.56 ?  36  TRP G CG  1 
ATOM   13308 C CD1 . TRP G  4 36  ? 85.240  54.100  297.117 1.00 155.35 ?  36  TRP G CD1 1 
ATOM   13309 C CD2 . TRP G  4 36  ? 83.852  53.724  295.400 1.00 154.55 ?  36  TRP G CD2 1 
ATOM   13310 N NE1 . TRP G  4 36  ? 86.001  53.994  295.975 1.00 154.37 ?  36  TRP G NE1 1 
ATOM   13311 C CE2 . TRP G  4 36  ? 85.172  53.766  294.909 1.00 153.85 ?  36  TRP G CE2 1 
ATOM   13312 C CE3 . TRP G  4 36  ? 82.804  53.502  294.500 1.00 154.61 ?  36  TRP G CE3 1 
ATOM   13313 C CZ2 . TRP G  4 36  ? 85.472  53.593  293.558 1.00 153.31 ?  36  TRP G CZ2 1 
ATOM   13314 C CZ3 . TRP G  4 36  ? 83.104  53.331  293.160 1.00 153.96 ?  36  TRP G CZ3 1 
ATOM   13315 C CH2 . TRP G  4 36  ? 84.426  53.377  292.702 1.00 153.34 ?  36  TRP G CH2 1 
ATOM   13316 N N   . VAL G  4 37  ? 79.789  55.635  298.101 1.00 155.95 ?  37  VAL G N   1 
ATOM   13317 C CA  . VAL G  4 37  ? 78.464  55.734  298.704 1.00 158.36 ?  37  VAL G CA  1 
ATOM   13318 C C   . VAL G  4 37  ? 77.495  54.960  297.822 1.00 160.05 ?  37  VAL G C   1 
ATOM   13319 O O   . VAL G  4 37  ? 77.532  55.086  296.593 1.00 158.02 ?  37  VAL G O   1 
ATOM   13320 C CB  . VAL G  4 37  ? 78.016  57.209  298.852 1.00 156.36 ?  37  VAL G CB  1 
ATOM   13321 C CG1 . VAL G  4 37  ? 76.598  57.301  299.403 1.00 159.50 ?  37  VAL G CG1 1 
ATOM   13322 C CG2 . VAL G  4 37  ? 78.990  57.989  299.731 1.00 155.01 ?  37  VAL G CG2 1 
ATOM   13323 N N   . ARG G  4 38  ? 76.620  54.168  298.441 1.00 158.84 ?  38  ARG G N   1 
ATOM   13324 C CA  . ARG G  4 38  ? 75.661  53.373  297.692 1.00 160.99 ?  38  ARG G CA  1 
ATOM   13325 C C   . ARG G  4 38  ? 74.237  53.756  298.069 1.00 163.64 ?  38  ARG G C   1 
ATOM   13326 O O   . ARG G  4 38  ? 73.978  54.341  299.124 1.00 164.94 ?  38  ARG G O   1 
ATOM   13327 C CB  . ARG G  4 38  ? 75.860  51.868  297.913 1.00 164.42 ?  38  ARG G CB  1 
ATOM   13328 C CG  . ARG G  4 38  ? 75.388  51.352  299.256 1.00 168.94 ?  38  ARG G CG  1 
ATOM   13329 C CD  . ARG G  4 38  ? 75.519  49.842  299.306 1.00 172.75 ?  38  ARG G CD  1 
ATOM   13330 N NE  . ARG G  4 38  ? 74.975  49.281  300.538 1.00 177.87 ?  38  ARG G NE  1 
ATOM   13331 C CZ  . ARG G  4 38  ? 74.987  47.986  300.835 1.00 182.24 ?  38  ARG G CZ  1 
ATOM   13332 N NH1 . ARG G  4 38  ? 75.518  47.115  299.986 1.00 182.06 1  38  ARG G NH1 1 
ATOM   13333 N NH2 . ARG G  4 38  ? 74.470  47.560  301.980 1.00 187.27 ?  38  ARG G NH2 1 
ATOM   13334 N N   . GLN G  4 39  ? 73.313  53.415  297.174 1.00 174.81 ?  39  GLN G N   1 
ATOM   13335 C CA  . GLN G  4 39  ? 71.901  53.754  297.318 1.00 177.89 ?  39  GLN G CA  1 
ATOM   13336 C C   . GLN G  4 39  ? 71.074  52.563  296.853 1.00 181.89 ?  39  GLN G C   1 
ATOM   13337 O O   . GLN G  4 39  ? 71.040  52.263  295.656 1.00 181.01 ?  39  GLN G O   1 
ATOM   13338 C CB  . GLN G  4 39  ? 71.569  55.001  296.499 1.00 175.10 ?  39  GLN G CB  1 
ATOM   13339 C CG  . GLN G  4 39  ? 70.166  55.546  296.661 1.00 178.20 ?  39  GLN G CG  1 
ATOM   13340 C CD  . GLN G  4 39  ? 70.044  56.955  296.112 1.00 175.32 ?  39  GLN G CD  1 
ATOM   13341 O OE1 . GLN G  4 39  ? 70.693  57.305  295.125 1.00 171.60 ?  39  GLN G OE1 1 
ATOM   13342 N NE2 . GLN G  4 39  ? 69.214  57.771  296.747 1.00 177.54 ?  39  GLN G NE2 1 
ATOM   13343 N N   . ALA G  4 40  ? 70.404  51.895  297.788 1.00 184.51 ?  40  ALA G N   1 
ATOM   13344 C CA  . ALA G  4 40  ? 69.508  50.815  297.416 1.00 189.06 ?  40  ALA G CA  1 
ATOM   13345 C C   . ALA G  4 40  ? 68.255  51.397  296.761 1.00 190.48 ?  40  ALA G C   1 
ATOM   13346 O O   . ALA G  4 40  ? 67.898  52.551  297.016 1.00 189.44 ?  40  ALA G O   1 
ATOM   13347 C CB  . ALA G  4 40  ? 69.139  49.982  298.642 1.00 194.47 ?  40  ALA G CB  1 
ATOM   13348 N N   . PRO G  4 41  ? 67.587  50.635  295.893 1.00 187.04 ?  41  PRO G N   1 
ATOM   13349 C CA  . PRO G  4 41  ? 66.455  51.198  295.142 1.00 188.56 ?  41  PRO G CA  1 
ATOM   13350 C C   . PRO G  4 41  ? 65.365  51.708  296.073 1.00 192.75 ?  41  PRO G C   1 
ATOM   13351 O O   . PRO G  4 41  ? 64.856  50.977  296.926 1.00 197.71 ?  41  PRO G O   1 
ATOM   13352 C CB  . PRO G  4 41  ? 65.964  50.023  294.286 1.00 192.05 ?  41  PRO G CB  1 
ATOM   13353 C CG  . PRO G  4 41  ? 66.635  48.808  294.822 1.00 193.41 ?  41  PRO G CG  1 
ATOM   13354 C CD  . PRO G  4 41  ? 67.881  49.244  295.508 1.00 188.99 ?  41  PRO G CD  1 
ATOM   13355 N N   . GLY G  4 42  ? 65.011  52.980  295.899 1.00 195.73 ?  42  GLY G N   1 
ATOM   13356 C CA  . GLY G  4 42  ? 64.010  53.611  296.728 1.00 201.41 ?  42  GLY G CA  1 
ATOM   13357 C C   . GLY G  4 42  ? 64.471  53.991  298.119 1.00 201.88 ?  42  GLY G C   1 
ATOM   13358 O O   . GLY G  4 42  ? 63.655  54.490  298.905 1.00 205.42 ?  42  GLY G O   1 
ATOM   13359 N N   . GLN G  4 43  ? 65.747  53.782  298.449 1.00 211.51 ?  43  GLN G N   1 
ATOM   13360 C CA  . GLN G  4 43  ? 66.284  53.974  299.789 1.00 210.50 ?  43  GLN G CA  1 
ATOM   13361 C C   . GLN G  4 43  ? 67.211  55.192  299.820 1.00 204.74 ?  43  GLN G C   1 
ATOM   13362 O O   . GLN G  4 43  ? 67.351  55.921  298.832 1.00 200.27 ?  43  GLN G O   1 
ATOM   13363 C CB  . GLN G  4 43  ? 67.014  52.708  300.251 1.00 213.49 ?  43  GLN G CB  1 
ATOM   13364 C CG  . GLN G  4 43  ? 66.207  51.424  300.142 1.00 219.82 ?  43  GLN G CG  1 
ATOM   13365 C CD  . GLN G  4 43  ? 64.838  51.534  300.778 1.00 230.45 ?  43  GLN G CD  1 
ATOM   13366 O OE1 . GLN G  4 43  ? 64.706  51.961  301.925 1.00 235.75 ?  43  GLN G OE1 1 
ATOM   13367 N NE2 . GLN G  4 43  ? 63.810  51.133  300.041 1.00 234.90 ?  43  GLN G NE2 1 
ATOM   13368 N N   . GLY G  4 44  ? 67.844  55.411  300.972 1.00 195.27 ?  44  GLY G N   1 
ATOM   13369 C CA  . GLY G  4 44  ? 68.749  56.525  301.169 1.00 190.58 ?  44  GLY G CA  1 
ATOM   13370 C C   . GLY G  4 44  ? 70.192  56.181  300.863 1.00 185.90 ?  44  GLY G C   1 
ATOM   13371 O O   . GLY G  4 44  ? 70.500  55.195  300.188 1.00 185.36 ?  44  GLY G O   1 
ATOM   13372 N N   . LEU G  4 45  ? 71.090  57.017  301.381 1.00 188.49 ?  45  LEU G N   1 
ATOM   13373 C CA  . LEU G  4 45  ? 72.516  56.942  301.092 1.00 183.68 ?  45  LEU G CA  1 
ATOM   13374 C C   . LEU G  4 45  ? 73.259  56.282  302.248 1.00 186.10 ?  45  LEU G C   1 
ATOM   13375 O O   . LEU G  4 45  ? 72.999  56.580  303.418 1.00 189.98 ?  45  LEU G O   1 
ATOM   13376 C CB  . LEU G  4 45  ? 73.080  58.339  300.832 1.00 179.03 ?  45  LEU G CB  1 
ATOM   13377 C CG  . LEU G  4 45  ? 72.457  59.095  299.654 1.00 177.18 ?  45  LEU G CG  1 
ATOM   13378 C CD1 . LEU G  4 45  ? 72.773  60.579  299.746 1.00 176.19 ?  45  LEU G CD1 1 
ATOM   13379 C CD2 . LEU G  4 45  ? 72.931  58.526  298.320 1.00 175.60 ?  45  LEU G CD2 1 
ATOM   13380 N N   . GLU G  4 46  ? 74.185  55.381  301.913 1.00 172.12 ?  46  GLU G N   1 
ATOM   13381 C CA  . GLU G  4 46  ? 74.945  54.617  302.897 1.00 174.30 ?  46  GLU G CA  1 
ATOM   13382 C C   . GLU G  4 46  ? 76.433  54.720  302.590 1.00 170.39 ?  46  GLU G C   1 
ATOM   13383 O O   . GLU G  4 46  ? 76.864  54.400  301.476 1.00 167.79 ?  46  GLU G O   1 
ATOM   13384 C CB  . GLU G  4 46  ? 74.495  53.153  302.910 1.00 178.59 ?  46  GLU G CB  1 
ATOM   13385 C CG  . GLU G  4 46  ? 75.191  52.291  303.946 1.00 181.83 ?  46  GLU G CG  1 
ATOM   13386 C CD  . GLU G  4 46  ? 74.616  50.889  304.008 1.00 186.81 ?  46  GLU G CD  1 
ATOM   13387 O OE1 . GLU G  4 46  ? 74.689  50.258  305.085 1.00 191.49 ?  46  GLU G OE1 1 
ATOM   13388 O OE2 . GLU G  4 46  ? 74.098  50.415  302.977 1.00 186.60 -1 46  GLU G OE2 1 
ATOM   13389 N N   . TRP G  4 47  ? 77.210  55.162  303.578 1.00 162.04 ?  47  TRP G N   1 
ATOM   13390 C CA  . TRP G  4 47  ? 78.652  55.338  303.438 1.00 158.95 ?  47  TRP G CA  1 
ATOM   13391 C C   . TRP G  4 47  ? 79.358  53.994  303.609 1.00 161.38 ?  47  TRP G C   1 
ATOM   13392 O O   . TRP G  4 47  ? 79.182  53.320  304.630 1.00 165.90 ?  47  TRP G O   1 
ATOM   13393 C CB  . TRP G  4 47  ? 79.139  56.359  304.468 1.00 158.76 ?  47  TRP G CB  1 
ATOM   13394 C CG  . TRP G  4 47  ? 80.582  56.762  304.353 1.00 155.88 ?  47  TRP G CG  1 
ATOM   13395 C CD1 . TRP G  4 47  ? 81.116  57.657  303.472 1.00 152.62 ?  47  TRP G CD1 1 
ATOM   13396 C CD2 . TRP G  4 47  ? 81.668  56.311  305.172 1.00 157.85 ?  47  TRP G CD2 1 
ATOM   13397 N NE1 . TRP G  4 47  ? 82.469  57.776  303.678 1.00 152.20 ?  47  TRP G NE1 1 
ATOM   13398 C CE2 . TRP G  4 47  ? 82.832  56.961  304.716 1.00 154.32 ?  47  TRP G CE2 1 
ATOM   13399 C CE3 . TRP G  4 47  ? 81.770  55.414  306.239 1.00 162.73 ?  47  TRP G CE3 1 
ATOM   13400 C CZ2 . TRP G  4 47  ? 84.081  56.742  305.290 1.00 155.53 ?  47  TRP G CZ2 1 
ATOM   13401 C CZ3 . TRP G  4 47  ? 83.010  55.198  306.806 1.00 163.88 ?  47  TRP G CZ3 1 
ATOM   13402 C CH2 . TRP G  4 47  ? 84.149  55.858  306.331 1.00 160.30 ?  47  TRP G CH2 1 
ATOM   13403 N N   . LEU G  4 48  ? 80.153  53.601  302.607 1.00 163.66 ?  48  LEU G N   1 
ATOM   13404 C CA  . LEU G  4 48  ? 80.933  52.366  302.653 1.00 166.10 ?  48  LEU G CA  1 
ATOM   13405 C C   . LEU G  4 48  ? 82.340  52.578  303.201 1.00 165.80 ?  48  LEU G C   1 
ATOM   13406 O O   . LEU G  4 48  ? 82.837  51.752  303.975 1.00 169.59 ?  48  LEU G O   1 
ATOM   13407 C CB  . LEU G  4 48  ? 81.029  51.747  301.255 1.00 164.52 ?  48  LEU G CB  1 
ATOM   13408 C CG  . LEU G  4 48  ? 79.737  51.471  300.485 1.00 164.93 ?  48  LEU G CG  1 
ATOM   13409 C CD1 . LEU G  4 48  ? 80.054  50.952  299.089 1.00 163.34 ?  48  LEU G CD1 1 
ATOM   13410 C CD2 . LEU G  4 48  ? 78.865  50.485  301.239 1.00 170.21 ?  48  LEU G CD2 1 
ATOM   13411 N N   . GLY G  4 49  ? 82.990  53.658  302.801 1.00 161.47 ?  49  GLY G N   1 
ATOM   13412 C CA  . GLY G  4 49  ? 84.354  53.930  303.201 1.00 161.10 ?  49  GLY G CA  1 
ATOM   13413 C C   . GLY G  4 49  ? 84.950  54.972  302.282 1.00 156.41 ?  49  GLY G C   1 
ATOM   13414 O O   . GLY G  4 49  ? 84.312  55.438  301.338 1.00 153.49 ?  49  GLY G O   1 
ATOM   13415 N N   . TRP G  4 50  ? 86.201  55.325  302.566 1.00 159.14 ?  50  TRP G N   1 
ATOM   13416 C CA  . TRP G  4 50  ? 86.891  56.255  301.685 1.00 155.25 ?  50  TRP G CA  1 
ATOM   13417 C C   . TRP G  4 50  ? 88.369  55.900  301.609 1.00 156.25 ?  50  TRP G C   1 
ATOM   13418 O O   . TRP G  4 50  ? 88.905  55.184  302.459 1.00 159.87 ?  50  TRP G O   1 
ATOM   13419 C CB  . TRP G  4 50  ? 86.677  57.714  302.122 1.00 153.04 ?  50  TRP G CB  1 
ATOM   13420 C CG  . TRP G  4 50  ? 87.311  58.125  303.415 1.00 155.05 ?  50  TRP G CG  1 
ATOM   13421 C CD1 . TRP G  4 50  ? 87.696  57.316  304.444 1.00 159.22 ?  50  TRP G CD1 1 
ATOM   13422 C CD2 . TRP G  4 50  ? 87.612  59.465  303.823 1.00 153.45 ?  50  TRP G CD2 1 
ATOM   13423 N NE1 . TRP G  4 50  ? 88.230  58.070  305.463 1.00 160.33 ?  50  TRP G NE1 1 
ATOM   13424 C CE2 . TRP G  4 50  ? 88.188  59.393  305.106 1.00 156.79 ?  50  TRP G CE2 1 
ATOM   13425 C CE3 . TRP G  4 50  ? 87.456  60.718  303.224 1.00 149.89 ?  50  TRP G CE3 1 
ATOM   13426 C CZ2 . TRP G  4 50  ? 88.606  60.527  305.801 1.00 156.61 ?  50  TRP G CZ2 1 
ATOM   13427 C CZ3 . TRP G  4 50  ? 87.869  61.843  303.915 1.00 149.69 ?  50  TRP G CZ3 1 
ATOM   13428 C CH2 . TRP G  4 50  ? 88.439  61.740  305.189 1.00 152.99 ?  50  TRP G CH2 1 
ATOM   13429 N N   . ILE G  4 51  ? 89.016  56.413  300.565 1.00 156.72 ?  51  ILE G N   1 
ATOM   13430 C CA  . ILE G  4 51  ? 90.404  56.105  300.245 1.00 157.87 ?  51  ILE G CA  1 
ATOM   13431 C C   . ILE G  4 51  ? 91.151  57.404  299.967 1.00 155.25 ?  51  ILE G C   1 
ATOM   13432 O O   . ILE G  4 51  ? 90.593  58.338  299.381 1.00 151.94 ?  51  ILE G O   1 
ATOM   13433 C CB  . ILE G  4 51  ? 90.487  55.148  299.033 1.00 158.30 ?  51  ILE G CB  1 
ATOM   13434 C CG1 . ILE G  4 51  ? 91.938  54.820  298.680 1.00 160.01 ?  51  ILE G CG1 1 
ATOM   13435 C CG2 . ILE G  4 51  ? 89.738  55.721  297.829 1.00 154.71 ?  51  ILE G CG2 1 
ATOM   13436 C CD1 . ILE G  4 51  ? 92.074  53.677  297.705 1.00 161.82 ?  51  ILE G CD1 1 
ATOM   13437 N N   . ASN G  4 52  ? 92.414  57.466  300.401 1.00 155.09 ?  52  ASN G N   1 
ATOM   13438 C CA  . ASN G  4 52  ? 93.297  58.561  300.025 1.00 153.39 ?  52  ASN G CA  1 
ATOM   13439 C C   . ASN G  4 52  ? 94.024  58.148  298.755 1.00 153.63 ?  52  ASN G C   1 
ATOM   13440 O O   . ASN G  4 52  ? 94.859  57.233  298.806 1.00 157.03 ?  52  ASN G O   1 
ATOM   13441 C CB  . ASN G  4 52  ? 94.293  58.871  301.136 1.00 155.91 ?  52  ASN G CB  1 
ATOM   13442 C CG  . ASN G  4 52  ? 95.170  60.079  300.824 1.00 154.46 ?  52  ASN G CG  1 
ATOM   13443 O OD1 . ASN G  4 52  ? 95.555  60.312  299.679 1.00 153.10 ?  52  ASN G OD1 1 
ATOM   13444 N ND2 . ASN G  4 52  ? 95.482  60.858  301.852 1.00 155.22 ?  52  ASN G ND2 1 
ATOM   13445 N N   . PRO G  4 53  A 93.757  58.777  297.610 1.00 154.50 ?  52  PRO G N   1 
ATOM   13446 C CA  . PRO G  4 53  A 94.377  58.313  296.362 1.00 155.14 ?  52  PRO G CA  1 
ATOM   13447 C C   . PRO G  4 53  A 95.874  58.524  296.328 1.00 157.34 ?  52  PRO G C   1 
ATOM   13448 O O   . PRO G  4 53  A 96.564  57.833  295.569 1.00 159.60 ?  52  PRO G O   1 
ATOM   13449 C CB  . PRO G  4 53  A 93.673  59.154  295.288 1.00 151.62 ?  52  PRO G CB  1 
ATOM   13450 C CG  . PRO G  4 53  A 92.388  59.588  295.934 1.00 149.52 ?  52  PRO G CG  1 
ATOM   13451 C CD  . PRO G  4 53  A 92.761  59.830  297.366 1.00 150.92 ?  52  PRO G CD  1 
ATOM   13452 N N   . HIS G  4 54  ? 96.396  59.448  297.134 1.00 163.43 ?  53  HIS G N   1 
ATOM   13453 C CA  . HIS G  4 54  ? 97.833  59.685  297.174 1.00 166.06 ?  53  HIS G CA  1 
ATOM   13454 C C   . HIS G  4 54  ? 98.560  58.520  297.839 1.00 171.60 ?  53  HIS G C   1 
ATOM   13455 O O   . HIS G  4 54  ? 99.425  57.879  297.231 1.00 175.89 ?  53  HIS G O   1 
ATOM   13456 C CB  . HIS G  4 54  ? 98.111  61.001  297.906 1.00 165.00 ?  53  HIS G CB  1 
ATOM   13457 C CG  . HIS G  4 54  ? 99.562  61.259  298.167 1.00 170.68 ?  53  HIS G CG  1 
ATOM   13458 N ND1 . HIS G  4 54  ? 100.503 61.307  297.161 1.00 174.10 ?  53  HIS G ND1 1 
ATOM   13459 C CD2 . HIS G  4 54  ? 100.234 61.480  299.322 1.00 174.97 ?  53  HIS G CD2 1 
ATOM   13460 C CE1 . HIS G  4 54  ? 101.692 61.548  297.685 1.00 177.88 ?  53  HIS G CE1 1 
ATOM   13461 N NE2 . HIS G  4 54  ? 101.556 61.657  298.994 1.00 179.23 ?  53  HIS G NE2 1 
ATOM   13462 N N   . SER G  4 55  ? 98.212  58.227  299.091 1.00 166.05 ?  54  SER G N   1 
ATOM   13463 C CA  . SER G  4 55  ? 98.894  57.194  299.861 1.00 172.18 ?  54  SER G CA  1 
ATOM   13464 C C   . SER G  4 55  ? 98.328  55.799  299.633 1.00 173.81 ?  54  SER G C   1 
ATOM   13465 O O   . SER G  4 55  ? 99.057  54.811  299.788 1.00 179.51 ?  54  SER G O   1 
ATOM   13466 C CB  . SER G  4 55  ? 98.827  57.531  301.352 1.00 173.60 ?  54  SER G CB  1 
ATOM   13467 O OG  . SER G  4 55  ? 97.483  57.552  301.802 1.00 170.32 ?  54  SER G OG  1 
ATOM   13468 N N   . GLY G  4 56  ? 97.056  55.691  299.264 1.00 169.29 ?  55  GLY G N   1 
ATOM   13469 C CA  . GLY G  4 56  ? 96.394  54.408  299.206 1.00 171.10 ?  55  GLY G CA  1 
ATOM   13470 C C   . GLY G  4 56  ? 95.739  53.966  300.496 1.00 172.83 ?  55  GLY G C   1 
ATOM   13471 O O   . GLY G  4 56  ? 95.094  52.910  300.508 1.00 174.58 ?  55  GLY G O   1 
ATOM   13472 N N   . ASP G  4 57  ? 95.881  54.733  301.577 1.00 166.68 ?  56  ASP G N   1 
ATOM   13473 C CA  . ASP G  4 57  ? 95.248  54.377  302.840 1.00 168.86 ?  56  ASP G CA  1 
ATOM   13474 C C   . ASP G  4 57  ? 93.731  54.364  302.702 1.00 166.16 ?  56  ASP G C   1 
ATOM   13475 O O   . ASP G  4 57  ? 93.144  55.140  301.942 1.00 161.85 ?  56  ASP G O   1 
ATOM   13476 C CB  . ASP G  4 57  ? 95.652  55.353  303.949 1.00 169.51 ?  56  ASP G CB  1 
ATOM   13477 C CG  . ASP G  4 57  ? 97.098  55.194  304.368 1.00 174.13 ?  56  ASP G CG  1 
ATOM   13478 O OD1 . ASP G  4 57  ? 97.719  54.185  303.977 1.00 178.18 ?  56  ASP G OD1 1 
ATOM   13479 O OD2 . ASP G  4 57  ? 97.610  56.069  305.099 1.00 177.33 -1 56  ASP G OD2 1 
ATOM   13480 N N   . THR G  4 58  ? 93.097  53.462  303.447 1.00 162.76 ?  57  THR G N   1 
ATOM   13481 C CA  . THR G  4 58  ? 91.654  53.302  303.425 1.00 161.30 ?  57  THR G CA  1 
ATOM   13482 C C   . THR G  4 58  ? 91.127  53.259  304.849 1.00 164.23 ?  57  THR G C   1 
ATOM   13483 O O   . THR G  4 58  ? 91.821  52.834  305.778 1.00 168.55 ?  57  THR G O   1 
ATOM   13484 C CB  . THR G  4 58  ? 91.223  52.016  302.693 1.00 162.89 ?  57  THR G CB  1 
ATOM   13485 O OG1 . THR G  4 58  ? 91.771  50.872  303.361 1.00 168.41 ?  57  THR G OG1 1 
ATOM   13486 C CG2 . THR G  4 58  ? 91.701  52.035  301.252 1.00 160.57 ?  57  THR G CG2 1 
ATOM   13487 N N   . THR G  4 59  ? 89.893  53.720  305.010 1.00 163.18 ?  58  THR G N   1 
ATOM   13488 C CA  . THR G  4 59  ? 89.108  53.471  306.210 1.00 166.61 ?  58  THR G CA  1 
ATOM   13489 C C   . THR G  4 59  ? 87.739  53.005  305.749 1.00 166.00 ?  58  THR G C   1 
ATOM   13490 O O   . THR G  4 59  ? 87.050  53.726  305.020 1.00 162.00 ?  58  THR G O   1 
ATOM   13491 C CB  . THR G  4 59  ? 88.995  54.720  307.088 1.00 165.88 ?  58  THR G CB  1 
ATOM   13492 O OG1 . THR G  4 59  ? 90.302  55.148  307.492 1.00 166.75 ?  58  THR G OG1 1 
ATOM   13493 C CG2 . THR G  4 59  ? 88.166  54.418  308.322 1.00 170.19 ?  58  THR G CG2 1 
ATOM   13494 N N   . THR G  4 60  ? 87.348  51.808  306.171 1.00 172.84 ?  59  THR G N   1 
ATOM   13495 C CA  . THR G  4 60  ? 86.096  51.198  305.752 1.00 173.23 ?  59  THR G CA  1 
ATOM   13496 C C   . THR G  4 60  ? 85.104  51.270  306.902 1.00 176.48 ?  59  THR G C   1 
ATOM   13497 O O   . THR G  4 60  ? 85.476  51.076  308.065 1.00 181.46 ?  59  THR G O   1 
ATOM   13498 C CB  . THR G  4 60  ? 86.305  49.737  305.324 1.00 177.04 ?  59  THR G CB  1 
ATOM   13499 O OG1 . THR G  4 60  ? 87.358  49.663  304.355 1.00 175.64 ?  59  THR G OG1 1 
ATOM   13500 C CG2 . THR G  4 60  ? 85.036  49.165  304.710 1.00 176.92 ?  59  THR G CG2 1 
ATOM   13501 N N   . SER G  4 61  ? 83.851  51.582  306.576 1.00 171.93 ?  60  SER G N   1 
ATOM   13502 C CA  . SER G  4 61  ? 82.793  51.501  307.570 1.00 175.79 ?  60  SER G CA  1 
ATOM   13503 C C   . SER G  4 61  ? 82.800  50.112  308.188 1.00 181.87 ?  60  SER G C   1 
ATOM   13504 O O   . SER G  4 61  ? 82.924  49.104  307.487 1.00 182.59 ?  60  SER G O   1 
ATOM   13505 C CB  . SER G  4 61  ? 81.434  51.805  306.939 1.00 174.05 ?  60  SER G CB  1 
ATOM   13506 O OG  . SER G  4 61  ? 80.405  51.775  307.912 1.00 178.35 ?  60  SER G OG  1 
ATOM   13507 N N   . GLN G  4 62  ? 82.680  50.067  309.514 1.00 180.91 ?  61  GLN G N   1 
ATOM   13508 C CA  . GLN G  4 62  ? 82.920  48.819  310.222 1.00 187.16 ?  61  GLN G CA  1 
ATOM   13509 C C   . GLN G  4 62  ? 81.888  47.755  309.873 1.00 190.05 ?  61  GLN G C   1 
ATOM   13510 O O   . GLN G  4 62  ? 82.163  46.563  310.044 1.00 194.62 ?  61  GLN G O   1 
ATOM   13511 C CB  . GLN G  4 62  ? 82.956  49.081  311.725 1.00 192.12 ?  61  GLN G CB  1 
ATOM   13512 C CG  . GLN G  4 62  ? 84.216  49.815  312.153 1.00 190.60 ?  61  GLN G CG  1 
ATOM   13513 C CD  . GLN G  4 62  ? 85.385  48.883  312.344 1.00 194.20 ?  61  GLN G CD  1 
ATOM   13514 O OE1 . GLN G  4 62  ? 85.368  48.013  313.213 1.00 201.62 ?  61  GLN G OE1 1 
ATOM   13515 N NE2 . GLN G  4 62  ? 86.408  49.047  311.514 1.00 190.34 ?  61  GLN G NE2 1 
ATOM   13516 N N   . LYS G  4 63  ? 80.707  48.158  309.400 1.00 177.86 ?  62  LYS G N   1 
ATOM   13517 C CA  . LYS G  4 63  ? 79.749  47.195  308.868 1.00 180.08 ?  62  LYS G CA  1 
ATOM   13518 C C   . LYS G  4 63  ? 80.330  46.404  307.699 1.00 178.05 ?  62  LYS G C   1 
ATOM   13519 O O   . LYS G  4 63  ? 79.993  45.229  307.514 1.00 181.88 ?  62  LYS G O   1 
ATOM   13520 C CB  . LYS G  4 63  ? 78.473  47.920  308.436 1.00 177.87 ?  62  LYS G CB  1 
ATOM   13521 C CG  . LYS G  4 63  ? 77.405  47.025  307.827 1.00 180.17 ?  62  LYS G CG  1 
ATOM   13522 C CD  . LYS G  4 63  ? 76.178  47.828  307.422 1.00 178.43 ?  62  LYS G CD  1 
ATOM   13523 C CE  . LYS G  4 63  ? 75.212  46.976  306.615 1.00 180.21 ?  62  LYS G CE  1 
ATOM   13524 N NZ  . LYS G  4 63  ? 74.050  47.753  306.105 1.00 178.65 1  62  LYS G NZ  1 
ATOM   13525 N N   . PHE G  4 64  ? 81.200  47.023  306.904 1.00 184.44 ?  63  PHE G N   1 
ATOM   13526 C CA  . PHE G  4 64  ? 81.721  46.414  305.688 1.00 182.36 ?  63  PHE G CA  1 
ATOM   13527 C C   . PHE G  4 64  ? 83.170  45.963  305.797 1.00 183.45 ?  63  PHE G C   1 
ATOM   13528 O O   . PHE G  4 64  ? 83.730  45.494  304.801 1.00 182.05 ?  63  PHE G O   1 
ATOM   13529 C CB  . PHE G  4 64  ? 81.568  47.396  304.526 1.00 175.83 ?  63  PHE G CB  1 
ATOM   13530 C CG  . PHE G  4 64  ? 80.155  47.848  304.311 1.00 175.05 ?  63  PHE G CG  1 
ATOM   13531 C CD1 . PHE G  4 64  ? 79.231  47.013  303.706 1.00 177.12 ?  63  PHE G CD1 1 
ATOM   13532 C CD2 . PHE G  4 64  ? 79.739  49.094  304.750 1.00 172.94 ?  63  PHE G CD2 1 
ATOM   13533 C CE1 . PHE G  4 64  ? 77.923  47.423  303.515 1.00 177.05 ?  63  PHE G CE1 1 
ATOM   13534 C CE2 . PHE G  4 64  ? 78.432  49.509  304.567 1.00 172.91 ?  63  PHE G CE2 1 
ATOM   13535 C CZ  . PHE G  4 64  ? 77.523  48.672  303.948 1.00 175.02 ?  63  PHE G CZ  1 
ATOM   13536 N N   . GLN G  4 65  ? 83.794  46.116  306.963 1.00 184.27 ?  64  GLN G N   1 
ATOM   13537 C CA  . GLN G  4 65  ? 85.203  45.780  307.121 1.00 185.77 ?  64  GLN G CA  1 
ATOM   13538 C C   . GLN G  4 65  ? 85.470  44.327  306.745 1.00 189.96 ?  64  GLN G C   1 
ATOM   13539 O O   . GLN G  4 65  ? 84.757  43.416  307.177 1.00 194.89 ?  64  GLN G O   1 
ATOM   13540 C CB  . GLN G  4 65  ? 85.648  46.041  308.558 1.00 189.60 ?  64  GLN G CB  1 
ATOM   13541 C CG  . GLN G  4 65  ? 87.102  45.699  308.800 1.00 192.00 ?  64  GLN G CG  1 
ATOM   13542 C CD  . GLN G  4 65  ? 88.037  46.586  308.002 1.00 186.38 ?  64  GLN G CD  1 
ATOM   13543 O OE1 . GLN G  4 65  ? 87.822  47.794  307.891 1.00 183.01 ?  64  GLN G OE1 1 
ATOM   13544 N NE2 . GLN G  4 65  ? 89.076  45.988  307.429 1.00 187.25 ?  64  GLN G NE2 1 
ATOM   13545 N N   . GLY G  4 66  ? 86.499  44.115  305.927 1.00 183.32 ?  65  GLY G N   1 
ATOM   13546 C CA  . GLY G  4 66  ? 86.876  42.787  305.497 1.00 187.44 ?  65  GLY G CA  1 
ATOM   13547 C C   . GLY G  4 66  ? 86.060  42.241  304.351 1.00 186.28 ?  65  GLY G C   1 
ATOM   13548 O O   . GLY G  4 66  ? 86.374  41.154  303.849 1.00 189.56 ?  65  GLY G O   1 
ATOM   13549 N N   . ARG G  4 67  ? 85.035  42.962  303.916 1.00 184.14 ?  66  ARG G N   1 
ATOM   13550 C CA  . ARG G  4 67  ? 84.180  42.575  302.803 1.00 182.98 ?  66  ARG G CA  1 
ATOM   13551 C C   . ARG G  4 67  ? 84.258  43.558  301.647 1.00 176.38 ?  66  ARG G C   1 
ATOM   13552 O O   . ARG G  4 67  ? 84.271  43.141  300.485 1.00 175.45 ?  66  ARG G O   1 
ATOM   13553 C CB  . ARG G  4 67  ? 82.726  42.432  303.283 1.00 185.18 ?  66  ARG G CB  1 
ATOM   13554 C CG  . ARG G  4 67  ? 81.863  41.537  302.407 1.00 186.80 ?  66  ARG G CG  1 
ATOM   13555 C CD  . ARG G  4 67  ? 80.542  41.188  303.083 1.00 190.65 ?  66  ARG G CD  1 
ATOM   13556 N NE  . ARG G  4 67  ? 79.643  42.331  303.202 1.00 187.24 ?  66  ARG G NE  1 
ATOM   13557 C CZ  . ARG G  4 67  ? 78.773  42.691  302.265 1.00 184.22 ?  66  ARG G CZ  1 
ATOM   13558 N NH1 . ARG G  4 67  ? 78.700  42.011  301.128 1.00 183.96 1  66  ARG G NH1 1 
ATOM   13559 N NH2 . ARG G  4 67  ? 77.987  43.742  302.454 1.00 181.87 ?  66  ARG G NH2 1 
ATOM   13560 N N   . VAL G  4 68  ? 84.301  44.857  301.940 1.00 179.09 ?  67  VAL G N   1 
ATOM   13561 C CA  . VAL G  4 68  ? 84.467  45.905  300.939 1.00 173.14 ?  67  VAL G CA  1 
ATOM   13562 C C   . VAL G  4 68  ? 85.920  46.365  300.956 1.00 171.53 ?  67  VAL G C   1 
ATOM   13563 O O   . VAL G  4 68  ? 86.479  46.639  302.026 1.00 172.77 ?  67  VAL G O   1 
ATOM   13564 C CB  . VAL G  4 68  ? 83.508  47.077  301.210 1.00 169.84 ?  67  VAL G CB  1 
ATOM   13565 C CG1 . VAL G  4 68  ? 83.819  48.245  300.298 1.00 164.11 ?  67  VAL G CG1 1 
ATOM   13566 C CG2 . VAL G  4 68  ? 82.066  46.635  301.030 1.00 171.58 ?  67  VAL G CG2 1 
ATOM   13567 N N   . TYR G  4 69  ? 86.531  46.456  299.773 1.00 164.41 ?  68  TYR G N   1 
ATOM   13568 C CA  . TYR G  4 69  ? 87.940  46.808  299.629 1.00 163.54 ?  68  TYR G CA  1 
ATOM   13569 C C   . TYR G  4 69  ? 88.103  47.935  298.619 1.00 158.20 ?  68  TYR G C   1 
ATOM   13570 O O   . TYR G  4 69  ? 87.544  47.873  297.519 1.00 156.44 ?  68  TYR G O   1 
ATOM   13571 C CB  . TYR G  4 69  ? 88.770  45.595  299.192 1.00 167.68 ?  68  TYR G CB  1 
ATOM   13572 C CG  . TYR G  4 69  ? 88.812  44.487  300.216 1.00 173.64 ?  68  TYR G CG  1 
ATOM   13573 C CD1 . TYR G  4 69  ? 89.789  44.469  301.202 1.00 176.52 ?  68  TYR G CD1 1 
ATOM   13574 C CD2 . TYR G  4 69  ? 87.881  43.457  300.196 1.00 176.87 ?  68  TYR G CD2 1 
ATOM   13575 C CE1 . TYR G  4 69  ? 89.835  43.459  302.145 1.00 182.52 ?  68  TYR G CE1 1 
ATOM   13576 C CE2 . TYR G  4 69  ? 87.920  42.440  301.135 1.00 182.83 ?  68  TYR G CE2 1 
ATOM   13577 C CZ  . TYR G  4 69  ? 88.900  42.447  302.106 1.00 185.66 ?  68  TYR G CZ  1 
ATOM   13578 O OH  . TYR G  4 69  ? 88.944  41.439  303.043 1.00 192.09 ?  68  TYR G OH  1 
ATOM   13579 N N   . MET G  4 70  ? 88.875  48.954  298.993 1.00 169.14 ?  69  MET G N   1 
ATOM   13580 C CA  . MET G  4 70  ? 89.139  50.112  298.148 1.00 164.50 ?  69  MET G CA  1 
ATOM   13581 C C   . MET G  4 70  ? 90.605  50.119  297.732 1.00 165.28 ?  69  MET G C   1 
ATOM   13582 O O   . MET G  4 70  ? 91.496  49.987  298.577 1.00 167.84 ?  69  MET G O   1 
ATOM   13583 C CB  . MET G  4 70  ? 88.792  51.410  298.882 1.00 161.55 ?  69  MET G CB  1 
ATOM   13584 C CG  . MET G  4 70  ? 87.304  51.610  299.127 1.00 160.58 ?  69  MET G CG  1 
ATOM   13585 S SD  . MET G  4 70  ? 86.970  52.865  300.380 1.00 159.20 ?  69  MET G SD  1 
ATOM   13586 C CE  . MET G  4 70  ? 87.422  51.983  301.870 1.00 164.60 ?  69  MET G CE  1 
ATOM   13587 N N   . THR G  4 71  ? 90.848  50.281  296.433 1.00 172.29 ?  70  THR G N   1 
ATOM   13588 C CA  . THR G  4 71  ? 92.189  50.375  295.872 1.00 173.26 ?  70  THR G CA  1 
ATOM   13589 C C   . THR G  4 71  ? 92.216  51.523  294.875 1.00 169.16 ?  70  THR G C   1 
ATOM   13590 O O   . THR G  4 71  ? 91.181  52.104  294.538 1.00 165.92 ?  70  THR G O   1 
ATOM   13591 C CB  . THR G  4 71  ? 92.623  49.067  295.189 1.00 177.32 ?  70  THR G CB  1 
ATOM   13592 O OG1 . THR G  4 71  ? 91.661  48.698  294.193 1.00 176.25 ?  70  THR G OG1 1 
ATOM   13593 C CG2 . THR G  4 71  ? 92.767  47.945  296.206 1.00 182.19 ?  70  THR G CG2 1 
ATOM   13594 N N   . ARG G  4 72  ? 93.416  51.860  294.408 1.00 158.34 ?  71  ARG G N   1 
ATOM   13595 C CA  . ARG G  4 72  ? 93.555  52.898  293.399 1.00 155.26 ?  71  ARG G CA  1 
ATOM   13596 C C   . ARG G  4 72  ? 94.724  52.579  292.478 1.00 157.89 ?  71  ARG G C   1 
ATOM   13597 O O   . ARG G  4 72  ? 95.683  51.910  292.870 1.00 161.76 ?  71  ARG G O   1 
ATOM   13598 C CB  . ARG G  4 72  ? 93.724  54.278  294.049 1.00 152.27 ?  71  ARG G CB  1 
ATOM   13599 C CG  . ARG G  4 72  ? 94.728  54.326  295.191 1.00 154.60 ?  71  ARG G CG  1 
ATOM   13600 C CD  . ARG G  4 72  ? 96.124  54.687  294.719 1.00 156.09 ?  71  ARG G CD  1 
ATOM   13601 N NE  . ARG G  4 72  ? 97.066  54.750  295.833 1.00 158.73 ?  71  ARG G NE  1 
ATOM   13602 C CZ  . ARG G  4 72  ? 98.354  54.429  295.749 1.00 162.58 ?  71  ARG G CZ  1 
ATOM   13603 N NH1 . ARG G  4 72  ? 99.132  54.521  296.819 1.00 165.21 1  71  ARG G NH1 1 
ATOM   13604 N NH2 . ARG G  4 72  ? 98.866  54.015  294.599 1.00 164.51 ?  71  ARG G NH2 1 
ATOM   13605 N N   . ASP G  4 73  ? 94.618  53.065  291.240 1.00 167.84 ?  72  ASP G N   1 
ATOM   13606 C CA  . ASP G  4 73  ? 95.697  53.041  290.256 1.00 170.25 ?  72  ASP G CA  1 
ATOM   13607 C C   . ASP G  4 73  ? 95.970  54.489  289.866 1.00 167.26 ?  72  ASP G C   1 
ATOM   13608 O O   . ASP G  4 73  ? 95.188  55.093  289.122 1.00 164.42 ?  72  ASP G O   1 
ATOM   13609 C CB  . ASP G  4 73  ? 95.307  52.190  289.045 1.00 172.14 ?  72  ASP G CB  1 
ATOM   13610 C CG  . ASP G  4 73  ? 96.458  51.968  288.076 1.00 176.12 ?  72  ASP G CG  1 
ATOM   13611 O OD1 . ASP G  4 73  ? 97.478  52.683  288.165 1.00 177.13 ?  72  ASP G OD1 1 
ATOM   13612 O OD2 . ASP G  4 73  ? 96.341  51.065  287.219 1.00 179.49 -1 72  ASP G OD2 1 
ATOM   13613 N N   . LYS G  4 74  ? 97.077  55.045  290.370 1.00 174.49 ?  73  LYS G N   1 
ATOM   13614 C CA  . LYS G  4 74  ? 97.357  56.466  290.172 1.00 171.93 ?  73  LYS G CA  1 
ATOM   13615 C C   . LYS G  4 74  ? 97.653  56.798  288.714 1.00 172.57 ?  73  LYS G C   1 
ATOM   13616 O O   . LYS G  4 74  ? 97.290  57.880  288.236 1.00 169.78 ?  73  LYS G O   1 
ATOM   13617 C CB  . LYS G  4 74  ? 98.524  56.904  291.060 1.00 173.66 ?  73  LYS G CB  1 
ATOM   13618 C CG  . LYS G  4 74  ? 98.216  56.883  292.551 1.00 172.81 ?  73  LYS G CG  1 
ATOM   13619 C CD  . LYS G  4 74  ? 99.248  57.672  293.347 1.00 173.93 ?  73  LYS G CD  1 
ATOM   13620 C CE  . LYS G  4 74  ? 100.545 56.908  293.522 1.00 179.34 ?  73  LYS G CE  1 
ATOM   13621 N NZ  . LYS G  4 74  ? 101.417 57.577  294.526 1.00 180.58 1  73  LYS G NZ  1 
ATOM   13622 N N   . SER G  4 75  ? 98.313  55.887  287.992 1.00 164.14 ?  74  SER G N   1 
ATOM   13623 C CA  . SER G  4 75  ? 98.741  56.192  286.629 1.00 165.86 ?  74  SER G CA  1 
ATOM   13624 C C   . SER G  4 75  ? 97.559  56.486  285.715 1.00 163.04 ?  74  SER G C   1 
ATOM   13625 O O   . SER G  4 75  ? 97.673  57.311  284.801 1.00 162.74 ?  74  SER G O   1 
ATOM   13626 C CB  . SER G  4 75  ? 99.572  55.037  286.065 1.00 171.49 ?  74  SER G CB  1 
ATOM   13627 O OG  . SER G  4 75  ? 98.786  53.870  285.898 1.00 172.26 ?  74  SER G OG  1 
ATOM   13628 N N   . ILE G  4 76  ? 96.425  55.827  285.940 1.00 161.84 ?  75  ILE G N   1 
ATOM   13629 C CA  . ILE G  4 76  ? 95.236  56.002  285.116 1.00 159.64 ?  75  ILE G CA  1 
ATOM   13630 C C   . ILE G  4 76  ? 94.163  56.828  285.820 1.00 154.98 ?  75  ILE G C   1 
ATOM   13631 O O   . ILE G  4 76  ? 93.015  56.860  285.361 1.00 153.38 ?  75  ILE G O   1 
ATOM   13632 C CB  . ILE G  4 76  ? 94.675  54.642  284.667 1.00 161.99 ?  75  ILE G CB  1 
ATOM   13633 C CG1 . ILE G  4 76  ? 94.504  53.720  285.874 1.00 162.65 ?  75  ILE G CG1 1 
ATOM   13634 C CG2 . ILE G  4 76  ? 95.593  53.997  283.627 1.00 166.78 ?  75  ILE G CG2 1 
ATOM   13635 C CD1 . ILE G  4 76  ? 93.761  52.437  285.572 1.00 164.64 ?  75  ILE G CD1 1 
ATOM   13636 N N   . ASN G  4 77  ? 94.504  57.497  286.925 1.00 155.52 ?  76  ASN G N   1 
ATOM   13637 C CA  . ASN G  4 77  ? 93.576  58.389  287.630 1.00 151.63 ?  76  ASN G CA  1 
ATOM   13638 C C   . ASN G  4 77  ? 92.293  57.662  288.035 1.00 150.68 ?  76  ASN G C   1 
ATOM   13639 O O   . ASN G  4 77  ? 91.197  58.221  287.965 1.00 148.19 ?  76  ASN G O   1 
ATOM   13640 C CB  . ASN G  4 77  ? 93.243  59.625  286.785 1.00 149.55 ?  76  ASN G CB  1 
ATOM   13641 C CG  . ASN G  4 77  ? 94.475  60.422  286.387 1.00 150.73 ?  76  ASN G CG  1 
ATOM   13642 O OD1 . ASN G  4 77  ? 95.482  60.428  287.095 1.00 152.00 ?  76  ASN G OD1 1 
ATOM   13643 N ND2 . ASN G  4 77  ? 94.394  61.108  285.251 1.00 150.70 ?  76  ASN G ND2 1 
ATOM   13644 N N   . THR G  4 78  ? 92.420  56.402  288.450 1.00 157.78 ?  77  THR G N   1 
ATOM   13645 C CA  . THR G  4 78  ? 91.260  55.545  288.654 1.00 157.23 ?  77  THR G CA  1 
ATOM   13646 C C   . THR G  4 78  ? 91.301  54.887  290.029 1.00 159.15 ?  77  THR G C   1 
ATOM   13647 O O   . THR G  4 78  ? 92.355  54.424  290.475 1.00 161.76 ?  77  THR G O   1 
ATOM   13648 C CB  . THR G  4 78  ? 91.181  54.471  287.557 1.00 160.92 ?  77  THR G CB  1 
ATOM   13649 O OG1 . THR G  4 78  ? 91.043  55.106  286.280 1.00 161.43 ?  77  THR G OG1 1 
ATOM   13650 C CG2 . THR G  4 78  ? 89.988  53.547  287.782 1.00 161.63 ?  77  THR G CG2 1 
ATOM   13651 N N   . ALA G  4 79  ? 90.148  54.862  290.698 1.00 152.43 ?  78  ALA G N   1 
ATOM   13652 C CA  . ALA G  4 79  ? 89.948  54.131  291.942 1.00 154.03 ?  78  ALA G CA  1 
ATOM   13653 C C   . ALA G  4 79  ? 89.070  52.910  291.692 1.00 156.18 ?  78  ALA G C   1 
ATOM   13654 O O   . ALA G  4 79  ? 88.205  52.920  290.811 1.00 155.57 ?  78  ALA G O   1 
ATOM   13655 C CB  . ALA G  4 79  ? 89.309  55.018  293.014 1.00 151.70 ?  78  ALA G CB  1 
ATOM   13656 N N   . PHE G  4 80  ? 89.292  51.856  292.482 1.00 148.24 ?  79  PHE G N   1 
ATOM   13657 C CA  . PHE G  4 80  ? 88.543  50.610  292.364 1.00 157.57 ?  79  PHE G CA  1 
ATOM   13658 C C   . PHE G  4 80  ? 87.829  50.283  293.670 1.00 160.73 ?  79  PHE G C   1 
ATOM   13659 O O   . PHE G  4 80  ? 88.352  50.532  294.761 1.00 159.94 ?  79  PHE G O   1 
ATOM   13660 C CB  . PHE G  4 80  ? 89.452  49.426  291.987 1.00 166.21 ?  79  PHE G CB  1 
ATOM   13661 C CG  . PHE G  4 80  ? 90.241  49.632  290.725 1.00 164.36 ?  79  PHE G CG  1 
ATOM   13662 C CD1 . PHE G  4 80  ? 89.688  49.337  289.490 1.00 166.51 ?  79  PHE G CD1 1 
ATOM   13663 C CD2 . PHE G  4 80  ? 91.549  50.085  290.777 1.00 160.90 ?  79  PHE G CD2 1 
ATOM   13664 C CE1 . PHE G  4 80  ? 90.416  49.517  288.328 1.00 165.17 ?  79  PHE G CE1 1 
ATOM   13665 C CE2 . PHE G  4 80  ? 92.282  50.264  289.620 1.00 159.54 ?  79  PHE G CE2 1 
ATOM   13666 C CZ  . PHE G  4 80  ? 91.715  49.980  288.394 1.00 161.47 ?  79  PHE G CZ  1 
ATOM   13667 N N   . LEU G  4 81  ? 86.627  49.722  293.543 1.00 149.12 ?  80  LEU G N   1 
ATOM   13668 C CA  . LEU G  4 81  ? 85.842  49.232  294.669 1.00 153.45 ?  80  LEU G CA  1 
ATOM   13669 C C   . LEU G  4 81  ? 85.544  47.755  294.446 1.00 163.76 ?  80  LEU G C   1 
ATOM   13670 O O   . LEU G  4 81  ? 84.891  47.395  293.460 1.00 165.81 ?  80  LEU G O   1 
ATOM   13671 C CB  . LEU G  4 81  ? 84.542  50.027  294.812 1.00 147.98 ?  80  LEU G CB  1 
ATOM   13672 C CG  . LEU G  4 81  ? 83.644  49.687  296.002 1.00 151.16 ?  80  LEU G CG  1 
ATOM   13673 C CD1 . LEU G  4 81  ? 84.240  50.229  297.287 1.00 148.24 ?  80  LEU G CD1 1 
ATOM   13674 C CD2 . LEU G  4 81  ? 82.240  50.225  295.792 1.00 147.75 ?  80  LEU G CD2 1 
ATOM   13675 N N   . ASP G  4 82  ? 86.018  46.904  295.355 1.00 147.00 ?  81  ASP G N   1 
ATOM   13676 C CA  . ASP G  4 82  ? 85.714  45.476  295.341 1.00 156.23 ?  81  ASP G CA  1 
ATOM   13677 C C   . ASP G  4 82  ? 84.715  45.165  296.448 1.00 158.60 ?  81  ASP G C   1 
ATOM   13678 O O   . ASP G  4 82  ? 85.022  45.350  297.630 1.00 158.45 ?  81  ASP G O   1 
ATOM   13679 C CB  . ASP G  4 82  ? 86.978  44.635  295.520 1.00 162.22 ?  81  ASP G CB  1 
ATOM   13680 C CG  . ASP G  4 82  ? 87.892  44.689  294.318 1.00 161.93 ?  81  ASP G CG  1 
ATOM   13681 O OD1 . ASP G  4 82  ? 87.509  44.146  293.261 1.00 164.77 ?  81  ASP G OD1 1 
ATOM   13682 O OD2 . ASP G  4 82  ? 88.994  45.264  294.435 1.00 158.91 -1 81  ASP G OD2 1 
ATOM   13683 N N   . VAL G  4 83  ? 83.527  44.701  296.067 1.00 154.01 ?  82  VAL G N   1 
ATOM   13684 C CA  . VAL G  4 83  ? 82.510  44.239  297.010 1.00 157.24 ?  82  VAL G CA  1 
ATOM   13685 C C   . VAL G  4 83  ? 82.386  42.727  296.860 1.00 165.47 ?  82  VAL G C   1 
ATOM   13686 O O   . VAL G  4 83  ? 82.021  42.229  295.788 1.00 167.35 ?  82  VAL G O   1 
ATOM   13687 C CB  . VAL G  4 83  ? 81.159  44.939  296.784 1.00 153.01 ?  82  VAL G CB  1 
ATOM   13688 C CG1 . VAL G  4 83  ? 80.179  44.599  297.904 1.00 156.09 ?  82  VAL G CG1 1 
ATOM   13689 C CG2 . VAL G  4 83  ? 81.347  46.450  296.683 1.00 147.99 ?  82  VAL G CG2 1 
ATOM   13690 N N   . THR G  4 84  A 82.685  42.000  297.932 1.00 172.16 ?  82  THR G N   1 
ATOM   13691 C CA  . THR G  4 84  A 82.783  40.548  297.904 1.00 179.27 ?  82  THR G CA  1 
ATOM   13692 C C   . THR G  4 84  A 81.668  39.916  298.730 1.00 183.07 ?  82  THR G C   1 
ATOM   13693 O O   . THR G  4 84  A 80.947  40.592  299.469 1.00 180.95 ?  82  THR G O   1 
ATOM   13694 C CB  . THR G  4 84  A 84.151  40.090  298.425 1.00 182.69 ?  82  THR G CB  1 
ATOM   13695 O OG1 . THR G  4 84  A 84.221  40.299  299.841 1.00 183.97 ?  82  THR G OG1 1 
ATOM   13696 C CG2 . THR G  4 84  A 85.267  40.877  297.752 1.00 178.73 ?  82  THR G CG2 1 
ATOM   13697 N N   . ARG G  4 85  B 81.555  38.592  298.598 1.00 181.66 ?  82  ARG G N   1 
ATOM   13698 C CA  . ARG G  4 85  B 80.570  37.782  299.322 1.00 186.57 ?  82  ARG G CA  1 
ATOM   13699 C C   . ARG G  4 85  B 79.167  38.386  299.212 1.00 183.66 ?  82  ARG G C   1 
ATOM   13700 O O   . ARG G  4 85  B 78.470  38.602  300.206 1.00 185.29 ?  82  ARG G O   1 
ATOM   13701 C CB  . ARG G  4 85  B 80.993  37.602  300.783 1.00 190.37 ?  82  ARG G CB  1 
ATOM   13702 C CG  . ARG G  4 85  B 82.451  37.164  300.946 1.00 192.18 ?  82  ARG G CG  1 
ATOM   13703 C CD  . ARG G  4 85  B 82.743  36.617  302.342 1.00 198.41 ?  82  ARG G CD  1 
ATOM   13704 N NE  . ARG G  4 85  B 82.501  37.587  303.409 1.00 197.70 ?  82  ARG G NE  1 
ATOM   13705 C CZ  . ARG G  4 85  B 83.410  38.444  303.864 1.00 194.66 ?  82  ARG G CZ  1 
ATOM   13706 N NH1 . ARG G  4 85  B 84.628  38.463  303.342 1.00 194.97 1  82  ARG G NH1 1 
ATOM   13707 N NH2 . ARG G  4 85  B 83.099  39.287  304.840 1.00 194.47 ?  82  ARG G NH2 1 
ATOM   13708 N N   . LEU G  4 86  C 78.758  38.649  297.973 1.00 191.43 ?  82  LEU G N   1 
ATOM   13709 C CA  . LEU G  4 86  C 77.552  39.420  297.688 1.00 188.91 ?  82  LEU G CA  1 
ATOM   13710 C C   . LEU G  4 86  C 76.273  38.696  298.106 1.00 193.83 ?  82  LEU G C   1 
ATOM   13711 O O   . LEU G  4 86  C 76.181  37.465  298.067 1.00 199.27 ?  82  LEU G O   1 
ATOM   13712 C CB  . LEU G  4 86  C 77.484  39.749  296.197 1.00 185.50 ?  82  LEU G CB  1 
ATOM   13713 C CG  . LEU G  4 86  C 78.503  40.758  295.669 1.00 179.77 ?  82  LEU G CG  1 
ATOM   13714 C CD1 . LEU G  4 86  C 78.551  40.721  294.147 1.00 178.93 ?  82  LEU G CD1 1 
ATOM   13715 C CD2 . LEU G  4 86  C 78.159  42.148  296.169 1.00 174.46 ?  82  LEU G CD2 1 
ATOM   13716 N N   . THR G  4 87  ? 75.280  39.489  298.517 1.00 188.63 ?  83  THR G N   1 
ATOM   13717 C CA  . THR G  4 87  ? 73.895  39.062  298.695 1.00 192.02 ?  83  THR G CA  1 
ATOM   13718 C C   . THR G  4 87  ? 72.972  40.078  298.027 1.00 187.55 ?  83  THR G C   1 
ATOM   13719 O O   . THR G  4 87  ? 73.414  41.115  297.524 1.00 181.71 ?  83  THR G O   1 
ATOM   13720 C CB  . THR G  4 87  ? 73.517  38.914  300.175 1.00 195.48 ?  83  THR G CB  1 
ATOM   13721 O OG1 . THR G  4 87  ? 73.294  40.211  300.744 1.00 190.68 ?  83  THR G OG1 1 
ATOM   13722 C CG2 . THR G  4 87  ? 74.609  38.202  300.947 1.00 199.03 ?  83  THR G CG2 1 
ATOM   13723 N N   . SER G  4 88  ? 71.670  39.773  298.031 1.00 205.33 ?  84  SER G N   1 
ATOM   13724 C CA  . SER G  4 88  ? 70.685  40.656  297.412 1.00 201.92 ?  84  SER G CA  1 
ATOM   13725 C C   . SER G  4 88  ? 70.585  42.006  298.112 1.00 195.99 ?  84  SER G C   1 
ATOM   13726 O O   . SER G  4 88  ? 70.099  42.970  297.510 1.00 192.04 ?  84  SER G O   1 
ATOM   13727 C CB  . SER G  4 88  ? 69.314  39.979  297.391 1.00 210.18 ?  84  SER G CB  1 
ATOM   13728 O OG  . SER G  4 88  ? 68.926  39.585  298.694 1.00 216.39 ?  84  SER G OG  1 
ATOM   13729 N N   . ASP G  4 89  ? 71.023  42.094  299.369 1.00 199.36 ?  85  ASP G N   1 
ATOM   13730 C CA  . ASP G  4 89  ? 71.011  43.368  300.077 1.00 193.85 ?  85  ASP G CA  1 
ATOM   13731 C C   . ASP G  4 89  ? 71.979  44.374  299.469 1.00 185.44 ?  85  ASP G C   1 
ATOM   13732 O O   . ASP G  4 89  ? 71.886  45.569  299.771 1.00 180.18 ?  85  ASP G O   1 
ATOM   13733 C CB  . ASP G  4 89  ? 71.349  43.146  301.552 1.00 198.28 ?  85  ASP G CB  1 
ATOM   13734 C CG  . ASP G  4 89  ? 71.044  44.356  302.409 1.00 196.30 ?  85  ASP G CG  1 
ATOM   13735 O OD1 . ASP G  4 89  ? 69.929  44.906  302.287 1.00 198.85 ?  85  ASP G OD1 1 
ATOM   13736 O OD2 . ASP G  4 89  ? 71.921  44.757  303.204 1.00 196.64 -1 85  ASP G OD2 1 
ATOM   13737 N N   . ASP G  4 90  ? 72.894  43.920  298.617 1.00 181.88 ?  86  ASP G N   1 
ATOM   13738 C CA  . ASP G  4 90  ? 73.910  44.766  298.010 1.00 175.61 ?  86  ASP G CA  1 
ATOM   13739 C C   . ASP G  4 90  ? 73.461  45.378  296.686 1.00 171.63 ?  86  ASP G C   1 
ATOM   13740 O O   . ASP G  4 90  ? 74.227  46.129  296.073 1.00 166.69 ?  86  ASP G O   1 
ATOM   13741 C CB  . ASP G  4 90  ? 75.191  43.949  297.806 1.00 179.00 ?  86  ASP G CB  1 
ATOM   13742 C CG  . ASP G  4 90  ? 75.773  43.442  299.117 1.00 182.68 ?  86  ASP G CG  1 
ATOM   13743 O OD1 . ASP G  4 90  ? 75.884  44.239  300.072 1.00 179.22 ?  86  ASP G OD1 1 
ATOM   13744 O OD2 . ASP G  4 90  ? 76.103  42.240  299.199 1.00 189.03 -1 86  ASP G OD2 1 
ATOM   13745 N N   . THR G  4 91  ? 72.248  45.072  296.233 1.00 182.59 ?  87  THR G N   1 
ATOM   13746 C CA  . THR G  4 91  ? 71.716  45.677  295.020 1.00 179.12 ?  87  THR G CA  1 
ATOM   13747 C C   . THR G  4 91  ? 71.507  47.175  295.220 1.00 171.56 ?  87  THR G C   1 
ATOM   13748 O O   . THR G  4 91  ? 70.957  47.604  296.239 1.00 171.14 ?  87  THR G O   1 
ATOM   13749 C CB  . THR G  4 91  ? 70.400  45.004  294.635 1.00 186.51 ?  87  THR G CB  1 
ATOM   13750 O OG1 . THR G  4 91  ? 70.660  43.657  294.219 1.00 192.89 ?  87  THR G OG1 1 
ATOM   13751 C CG2 . THR G  4 91  ? 69.721  45.756  293.497 1.00 182.65 ?  87  THR G CG2 1 
ATOM   13752 N N   . GLY G  4 92  ? 71.947  47.964  294.250 1.00 179.01 ?  88  GLY G N   1 
ATOM   13753 C CA  . GLY G  4 92  ? 71.780  49.400  294.313 1.00 175.62 ?  88  GLY G CA  1 
ATOM   13754 C C   . GLY G  4 92  ? 72.714  50.095  293.339 1.00 170.63 ?  88  GLY G C   1 
ATOM   13755 O O   . GLY G  4 92  ? 73.393  49.459  292.535 1.00 169.99 ?  88  GLY G O   1 
ATOM   13756 N N   . ILE G  4 93  ? 72.717  51.424  293.429 1.00 170.84 ?  89  ILE G N   1 
ATOM   13757 C CA  . ILE G  4 93  ? 73.598  52.274  292.636 1.00 166.27 ?  89  ILE G CA  1 
ATOM   13758 C C   . ILE G  4 93  ? 74.789  52.664  293.499 1.00 163.58 ?  89  ILE G C   1 
ATOM   13759 O O   . ILE G  4 93  ? 74.617  53.148  294.624 1.00 163.82 ?  89  ILE G O   1 
ATOM   13760 C CB  . ILE G  4 93  ? 72.857  53.522  292.123 1.00 164.79 ?  89  ILE G CB  1 
ATOM   13761 C CG1 . ILE G  4 93  ? 71.729  53.126  291.170 1.00 167.72 ?  89  ILE G CG1 1 
ATOM   13762 C CG2 . ILE G  4 93  ? 73.819  54.461  291.417 1.00 160.39 ?  89  ILE G CG2 1 
ATOM   13763 C CD1 . ILE G  4 93  ? 70.994  54.309  290.578 1.00 166.96 ?  89  ILE G CD1 1 
ATOM   13764 N N   . TYR G  4 94  ? 75.995  52.459  292.976 1.00 165.48 ?  90  TYR G N   1 
ATOM   13765 C CA  . TYR G  4 94  ? 77.234  52.761  293.685 1.00 163.40 ?  90  TYR G CA  1 
ATOM   13766 C C   . TYR G  4 94  ? 77.870  54.010  293.092 1.00 159.32 ?  90  TYR G C   1 
ATOM   13767 O O   . TYR G  4 94  ? 78.142  54.060  291.887 1.00 158.13 ?  90  TYR G O   1 
ATOM   13768 C CB  . TYR G  4 94  ? 78.205  51.581  293.622 1.00 164.84 ?  90  TYR G CB  1 
ATOM   13769 C CG  . TYR G  4 94  ? 77.791  50.410  294.481 1.00 169.13 ?  90  TYR G CG  1 
ATOM   13770 C CD1 . TYR G  4 94  ? 76.729  49.593  294.117 1.00 172.42 ?  90  TYR G CD1 1 
ATOM   13771 C CD2 . TYR G  4 94  ? 78.457  50.133  295.667 1.00 170.37 ?  90  TYR G CD2 1 
ATOM   13772 C CE1 . TYR G  4 94  ? 76.346  48.527  294.910 1.00 176.81 ?  90  TYR G CE1 1 
ATOM   13773 C CE2 . TYR G  4 94  ? 78.084  49.072  296.466 1.00 174.82 ?  90  TYR G CE2 1 
ATOM   13774 C CZ  . TYR G  4 94  ? 77.028  48.272  296.083 1.00 178.02 ?  90  TYR G CZ  1 
ATOM   13775 O OH  . TYR G  4 94  ? 76.652  47.212  296.877 1.00 182.89 ?  90  TYR G OH  1 
ATOM   13776 N N   . TYR G  4 95  ? 78.116  55.005  293.940 1.00 152.64 ?  91  TYR G N   1 
ATOM   13777 C CA  . TYR G  4 95  ? 78.748  56.253  293.543 1.00 149.09 ?  91  TYR G CA  1 
ATOM   13778 C C   . TYR G  4 95  ? 80.144  56.343  294.140 1.00 147.92 ?  91  TYR G C   1 
ATOM   13779 O O   . TYR G  4 95  ? 80.371  55.927  295.280 1.00 149.36 ?  91  TYR G O   1 
ATOM   13780 C CB  . TYR G  4 95  ? 77.941  57.472  294.014 1.00 148.40 ?  91  TYR G CB  1 
ATOM   13781 C CG  . TYR G  4 95  ? 76.518  57.539  293.513 1.00 150.10 ?  91  TYR G CG  1 
ATOM   13782 C CD1 . TYR G  4 95  ? 76.226  58.043  292.253 1.00 149.10 ?  91  TYR G CD1 1 
ATOM   13783 C CD2 . TYR G  4 95  ? 75.461  57.117  294.310 1.00 153.37 ?  91  TYR G CD2 1 
ATOM   13784 C CE1 . TYR G  4 95  ? 74.922  58.109  291.793 1.00 151.14 ?  91  TYR G CE1 1 
ATOM   13785 C CE2 . TYR G  4 95  ? 74.153  57.180  293.859 1.00 155.53 ?  91  TYR G CE2 1 
ATOM   13786 C CZ  . TYR G  4 95  ? 73.889  57.678  292.600 1.00 154.40 ?  91  TYR G CZ  1 
ATOM   13787 O OH  . TYR G  4 95  ? 72.589  57.741  292.148 1.00 157.14 ?  91  TYR G OH  1 
ATOM   13788 N N   . CYS G  4 96  ? 81.072  56.888  293.365 1.00 144.27 ?  92  CYS G N   1 
ATOM   13789 C CA  . CYS G  4 96  ? 82.291  57.464  293.905 1.00 142.83 ?  92  CYS G CA  1 
ATOM   13790 C C   . CYS G  4 96  ? 82.070  58.963  294.019 1.00 140.53 ?  92  CYS G C   1 
ATOM   13791 O O   . CYS G  4 96  ? 81.436  59.570  293.151 1.00 139.59 ?  92  CYS G O   1 
ATOM   13792 C CB  . CYS G  4 96  ? 83.500  57.160  293.019 1.00 142.33 ?  92  CYS G CB  1 
ATOM   13793 S SG  . CYS G  4 96  ? 83.351  57.737  291.312 1.00 140.73 ?  92  CYS G SG  1 
ATOM   13794 N N   . ALA G  4 97  ? 82.588  59.561  295.088 1.00 150.54 ?  93  ALA G N   1 
ATOM   13795 C CA  . ALA G  4 97  ? 82.357  60.977  295.340 1.00 148.77 ?  93  ALA G CA  1 
ATOM   13796 C C   . ALA G  4 97  ? 83.601  61.587  295.959 1.00 147.82 ?  93  ALA G C   1 
ATOM   13797 O O   . ALA G  4 97  ? 84.077  61.125  297.002 1.00 150.46 ?  93  ALA G O   1 
ATOM   13798 C CB  . ALA G  4 97  ? 81.146  61.180  296.253 1.00 150.30 ?  93  ALA G CB  1 
ATOM   13799 N N   . ARG G  4 98  ? 84.113  62.626  295.313 1.00 153.93 ?  94  ARG G N   1 
ATOM   13800 C CA  . ARG G  4 98  ? 85.288  63.332  295.792 1.00 156.74 ?  94  ARG G CA  1 
ATOM   13801 C C   . ARG G  4 98  ? 84.925  64.241  296.957 1.00 160.15 ?  94  ARG G C   1 
ATOM   13802 O O   . ARG G  4 98  ? 83.883  64.901  296.945 1.00 159.60 ?  94  ARG G O   1 
ATOM   13803 C CB  . ARG G  4 98  ? 85.892  64.156  294.660 1.00 154.91 ?  94  ARG G CB  1 
ATOM   13804 C CG  . ARG G  4 98  ? 87.150  64.879  295.045 1.00 157.81 ?  94  ARG G CG  1 
ATOM   13805 C CD  . ARG G  4 98  ? 87.561  65.854  293.964 1.00 156.48 ?  94  ARG G CD  1 
ATOM   13806 N NE  . ARG G  4 98  ? 86.751  67.067  294.026 1.00 156.28 ?  94  ARG G NE  1 
ATOM   13807 C CZ  . ARG G  4 98  ? 86.855  68.085  293.179 1.00 155.37 ?  94  ARG G CZ  1 
ATOM   13808 N NH1 . ARG G  4 98  ? 87.736  68.041  292.190 1.00 154.62 1  94  ARG G NH1 1 
ATOM   13809 N NH2 . ARG G  4 98  ? 86.073  69.147  293.317 1.00 155.65 ?  94  ARG G NH2 1 
ATOM   13810 N N   . ASP G  4 99  ? 85.794  64.278  297.961 1.00 155.02 ?  95  ASP G N   1 
ATOM   13811 C CA  . ASP G  4 99  ? 85.661  65.213  299.069 1.00 158.70 ?  95  ASP G CA  1 
ATOM   13812 C C   . ASP G  4 99  ? 86.502  66.457  298.812 1.00 159.74 ?  95  ASP G C   1 
ATOM   13813 O O   . ASP G  4 99  ? 87.624  66.370  298.304 1.00 159.74 ?  95  ASP G O   1 
ATOM   13814 C CB  . ASP G  4 99  ? 86.077  64.562  300.392 1.00 162.95 ?  95  ASP G CB  1 
ATOM   13815 C CG  . ASP G  4 99  ? 85.401  65.200  301.601 1.00 166.72 ?  95  ASP G CG  1 
ATOM   13816 O OD1 . ASP G  4 99  ? 85.732  66.360  301.925 1.00 168.94 ?  95  ASP G OD1 1 
ATOM   13817 O OD2 . ASP G  4 99  ? 84.547  64.542  302.236 1.00 167.74 -1 95  ASP G OD2 1 
ATOM   13818 N N   . LYS G  4 100 ? 85.940  67.619  299.159 1.00 162.52 ?  96  LYS G N   1 
ATOM   13819 C CA  . LYS G  4 100 ? 86.701  68.864  299.117 1.00 164.11 ?  96  LYS G CA  1 
ATOM   13820 C C   . LYS G  4 100 ? 87.982  68.755  299.936 1.00 168.18 ?  96  LYS G C   1 
ATOM   13821 O O   . LYS G  4 100 ? 89.030  69.278  299.539 1.00 168.96 ?  96  LYS G O   1 
ATOM   13822 C CB  . LYS G  4 100 ? 85.829  70.017  299.619 1.00 165.71 ?  96  LYS G CB  1 
ATOM   13823 C CG  . LYS G  4 100 ? 84.586  70.254  298.771 1.00 162.33 ?  96  LYS G CG  1 
ATOM   13824 C CD  . LYS G  4 100 ? 83.650  71.266  299.412 1.00 164.74 ?  96  LYS G CD  1 
ATOM   13825 C CE  . LYS G  4 100 ? 84.269  72.649  299.428 1.00 166.51 ?  96  LYS G CE  1 
ATOM   13826 N NZ  . LYS G  4 100 ? 84.324  73.257  298.070 1.00 163.17 1  96  LYS G NZ  1 
ATOM   13827 N N   . TYR G  4 101 ? 87.909  68.088  301.089 1.00 159.13 ?  97  TYR G N   1 
ATOM   13828 C CA  . TYR G  4 101 ? 89.082  67.714  301.880 1.00 163.29 ?  97  TYR G CA  1 
ATOM   13829 C C   . TYR G  4 101 ? 89.882  68.928  302.355 1.00 166.83 ?  97  TYR G C   1 
ATOM   13830 O O   . TYR G  4 101 ? 91.107  68.855  302.491 1.00 169.41 ?  97  TYR G O   1 
ATOM   13831 C CB  . TYR G  4 101 ? 89.976  66.735  301.107 1.00 161.66 ?  97  TYR G CB  1 
ATOM   13832 C CG  . TYR G  4 101 ? 90.751  65.777  301.991 1.00 165.71 ?  97  TYR G CG  1 
ATOM   13833 C CD1 . TYR G  4 101 ? 90.098  64.989  302.933 1.00 167.56 ?  97  TYR G CD1 1 
ATOM   13834 C CD2 . TYR G  4 101 ? 92.128  65.637  301.865 1.00 168.05 ?  97  TYR G CD2 1 
ATOM   13835 C CE1 . TYR G  4 101 ? 90.797  64.106  303.741 1.00 171.57 ?  97  TYR G CE1 1 
ATOM   13836 C CE2 . TYR G  4 101 ? 92.835  64.751  302.666 1.00 172.24 ?  97  TYR G CE2 1 
ATOM   13837 C CZ  . TYR G  4 101 ? 92.163  63.992  303.604 1.00 173.94 ?  97  TYR G CZ  1 
ATOM   13838 O OH  . TYR G  4 101 ? 92.855  63.114  304.406 1.00 178.34 ?  97  TYR G OH  1 
ATOM   13839 N N   . TYR G  4 102 ? 89.207  70.059  302.584 1.00 171.92 ?  98  TYR G N   1 
ATOM   13840 C CA  . TYR G  4 102 ? 89.864  71.203  303.205 1.00 175.56 ?  98  TYR G CA  1 
ATOM   13841 C C   . TYR G  4 102 ? 90.497  70.787  304.525 1.00 180.96 ?  98  TYR G C   1 
ATOM   13842 O O   . TYR G  4 102 ? 89.892  70.064  305.320 1.00 182.75 ?  98  TYR G O   1 
ATOM   13843 C CB  . TYR G  4 102 ? 88.877  72.348  303.459 1.00 175.73 ?  98  TYR G CB  1 
ATOM   13844 C CG  . TYR G  4 102 ? 88.290  72.997  302.228 1.00 171.41 ?  98  TYR G CG  1 
ATOM   13845 C CD1 . TYR G  4 102 ? 88.866  72.823  300.978 1.00 167.90 ?  98  TYR G CD1 1 
ATOM   13846 C CD2 . TYR G  4 102 ? 87.175  73.819  302.327 1.00 171.42 ?  98  TYR G CD2 1 
ATOM   13847 C CE1 . TYR G  4 102 ? 88.329  73.429  299.854 1.00 164.41 ?  98  TYR G CE1 1 
ATOM   13848 C CE2 . TYR G  4 102 ? 86.635  74.431  301.215 1.00 168.01 ?  98  TYR G CE2 1 
ATOM   13849 C CZ  . TYR G  4 102 ? 87.214  74.234  299.981 1.00 164.50 ?  98  TYR G CZ  1 
ATOM   13850 O OH  . TYR G  4 102 ? 86.665  74.847  298.877 1.00 161.49 ?  98  TYR G OH  1 
ATOM   13851 N N   . GLY G  4 103 ? 91.719  71.258  304.760 1.00 177.36 ?  99  GLY G N   1 
ATOM   13852 C CA  . GLY G  4 103 ? 92.416  70.896  305.978 1.00 183.18 ?  99  GLY G CA  1 
ATOM   13853 C C   . GLY G  4 103 ? 92.735  69.424  306.090 1.00 183.57 ?  99  GLY G C   1 
ATOM   13854 O O   . GLY G  4 103 ? 93.003  68.939  307.193 1.00 188.16 ?  99  GLY G O   1 
ATOM   13855 N N   . ASN G  4 104 ? 92.705  68.698  304.971 1.00 163.71 ?  100 ASN G N   1 
ATOM   13856 C CA  . ASN G  4 104 ? 92.928  67.251  304.944 1.00 163.65 ?  100 ASN G CA  1 
ATOM   13857 C C   . ASN G  4 104 ? 91.938  66.513  305.842 1.00 164.69 ?  100 ASN G C   1 
ATOM   13858 O O   . ASN G  4 104 ? 92.269  65.498  306.458 1.00 167.12 ?  100 ASN G O   1 
ATOM   13859 C CB  . ASN G  4 104 ? 94.367  66.901  305.321 1.00 168.38 ?  100 ASN G CB  1 
ATOM   13860 C CG  . ASN G  4 104 ? 95.375  67.582  304.431 1.00 167.90 ?  100 ASN G CG  1 
ATOM   13861 O OD1 . ASN G  4 104 ? 95.362  67.405  303.215 1.00 163.66 ?  100 ASN G OD1 1 
ATOM   13862 N ND2 . ASN G  4 104 ? 96.255  68.371  305.031 1.00 172.42 ?  100 ASN G ND2 1 
ATOM   13863 N N   . GLU G  4 105 A 90.702  67.011  305.892 1.00 167.11 ?  100 GLU G N   1 
ATOM   13864 C CA  . GLU G  4 105 A 89.625  66.359  306.625 1.00 167.84 ?  100 GLU G CA  1 
ATOM   13865 C C   . GLU G  4 105 A 88.341  66.454  305.813 1.00 162.86 ?  100 GLU G C   1 
ATOM   13866 O O   . GLU G  4 105 A 88.218  67.278  304.904 1.00 159.72 ?  100 GLU G O   1 
ATOM   13867 C CB  . GLU G  4 105 A 89.415  66.978  308.017 1.00 173.22 ?  100 GLU G CB  1 
ATOM   13868 C CG  . GLU G  4 105 A 89.007  68.443  308.011 1.00 173.17 ?  100 GLU G CG  1 
ATOM   13869 C CD  . GLU G  4 105 A 88.811  68.999  309.411 1.00 179.02 ?  100 GLU G CD  1 
ATOM   13870 O OE1 . GLU G  4 105 A 88.389  70.168  309.530 1.00 179.63 ?  100 GLU G OE1 1 
ATOM   13871 O OE2 . GLU G  4 105 A 89.075  68.269  310.391 1.00 183.02 -1 100 GLU G OE2 1 
ATOM   13872 N N   . ALA G  4 106 B 87.370  65.614  306.171 1.00 169.98 ?  100 ALA G N   1 
ATOM   13873 C CA  . ALA G  4 106 B 86.103  65.583  305.451 1.00 165.73 ?  100 ALA G CA  1 
ATOM   13874 C C   . ALA G  4 106 B 85.365  66.907  305.601 1.00 166.43 ?  100 ALA G C   1 
ATOM   13875 O O   . ALA G  4 106 B 85.223  67.434  306.709 1.00 171.16 ?  100 ALA G O   1 
ATOM   13876 C CB  . ALA G  4 106 B 85.233  64.431  305.954 1.00 166.13 ?  100 ALA G CB  1 
ATOM   13877 N N   . VAL G  4 107 C 84.908  67.450  304.474 1.00 170.20 ?  100 VAL G N   1 
ATOM   13878 C CA  . VAL G  4 107 C 84.203  68.727  304.451 1.00 170.50 ?  100 VAL G CA  1 
ATOM   13879 C C   . VAL G  4 107 C 82.893  68.561  303.687 1.00 166.95 ?  100 VAL G C   1 
ATOM   13880 O O   . VAL G  4 107 C 81.830  68.984  304.156 1.00 168.91 ?  100 VAL G O   1 
ATOM   13881 C CB  . VAL G  4 107 C 85.079  69.837  303.839 1.00 169.57 ?  100 VAL G CB  1 
ATOM   13882 C CG1 . VAL G  4 107 C 84.297  71.124  303.736 1.00 169.57 ?  100 VAL G CG1 1 
ATOM   13883 C CG2 . VAL G  4 107 C 86.333  70.057  304.682 1.00 173.87 ?  100 VAL G CG2 1 
ATOM   13884 N N   . GLY G  4 108 D 82.963  67.952  302.509 1.00 174.96 ?  100 GLY G N   1 
ATOM   13885 C CA  . GLY G  4 108 D 81.767  67.692  301.727 1.00 171.58 ?  100 GLY G CA  1 
ATOM   13886 C C   . GLY G  4 108 D 82.128  67.048  300.404 1.00 166.53 ?  100 GLY G C   1 
ATOM   13887 O O   . GLY G  4 108 D 83.253  67.175  299.911 1.00 165.38 ?  100 GLY G O   1 
ATOM   13888 N N   . MET G  4 109 E 81.138  66.358  299.834 1.00 158.58 ?  100 MET G N   1 
ATOM   13889 C CA  . MET G  4 109 E 81.304  65.599  298.593 1.00 157.03 ?  100 MET G CA  1 
ATOM   13890 C C   . MET G  4 109 E 80.800  66.472  297.448 1.00 155.45 ?  100 MET G C   1 
ATOM   13891 O O   . MET G  4 109 E 79.595  66.558  297.201 1.00 156.63 ?  100 MET G O   1 
ATOM   13892 C CB  . MET G  4 109 E 80.557  64.270  298.660 1.00 159.04 ?  100 MET G CB  1 
ATOM   13893 C CG  . MET G  4 109 E 80.936  63.389  299.847 1.00 161.42 ?  100 MET G CG  1 
ATOM   13894 S SD  . MET G  4 109 E 80.063  61.807  299.854 1.00 164.34 ?  100 MET G SD  1 
ATOM   13895 C CE  . MET G  4 109 E 80.464  61.200  301.490 1.00 167.76 ?  100 MET G CE  1 
ATOM   13896 N N   . ASP G  4 110 ? 81.732  67.117  296.745 1.00 170.80 ?  101 ASP G N   1 
ATOM   13897 C CA  . ASP G  4 110 ? 81.391  68.150  295.776 1.00 169.74 ?  101 ASP G CA  1 
ATOM   13898 C C   . ASP G  4 110 ? 81.311  67.658  294.337 1.00 168.97 ?  101 ASP G C   1 
ATOM   13899 O O   . ASP G  4 110 ? 80.668  68.319  293.513 1.00 168.96 ?  101 ASP G O   1 
ATOM   13900 C CB  . ASP G  4 110 ? 82.407  69.296  295.852 1.00 168.45 ?  101 ASP G CB  1 
ATOM   13901 C CG  . ASP G  4 110 ? 83.804  68.865  295.444 1.00 167.23 ?  101 ASP G CG  1 
ATOM   13902 O OD1 . ASP G  4 110 ? 84.078  67.646  295.444 1.00 167.58 ?  101 ASP G OD1 1 
ATOM   13903 O OD2 . ASP G  4 110 ? 84.625  69.746  295.111 1.00 166.33 -1 101 ASP G OD2 1 
ATOM   13904 N N   . VAL G  4 111 ? 81.934  66.528  294.009 1.00 157.48 ?  102 VAL G N   1 
ATOM   13905 C CA  . VAL G  4 111 ? 81.888  65.968  292.663 1.00 157.31 ?  102 VAL G CA  1 
ATOM   13906 C C   . VAL G  4 111 ? 81.531  64.494  292.766 1.00 158.69 ?  102 VAL G C   1 
ATOM   13907 O O   . VAL G  4 111 ? 82.209  63.732  293.465 1.00 159.09 ?  102 VAL G O   1 
ATOM   13908 C CB  . VAL G  4 111 ? 83.223  66.146  291.915 1.00 156.02 ?  102 VAL G CB  1 
ATOM   13909 C CG1 . VAL G  4 111 ? 83.187  65.413  290.579 1.00 156.47 ?  102 VAL G CG1 1 
ATOM   13910 C CG2 . VAL G  4 111 ? 83.519  67.621  291.711 1.00 155.02 ?  102 VAL G CG2 1 
ATOM   13911 N N   . TRP G  4 112 ? 80.470  64.098  292.071 1.00 151.11 ?  103 TRP G N   1 
ATOM   13912 C CA  . TRP G  4 112 ? 79.975  62.732  292.098 1.00 152.88 ?  103 TRP G CA  1 
ATOM   13913 C C   . TRP G  4 112 ? 80.065  62.105  290.718 1.00 153.17 ?  103 TRP G C   1 
ATOM   13914 O O   . TRP G  4 112 ? 79.787  62.756  289.705 1.00 152.82 ?  103 TRP G O   1 
ATOM   13915 C CB  . TRP G  4 112 ? 78.527  62.680  292.579 1.00 154.96 ?  103 TRP G CB  1 
ATOM   13916 C CG  . TRP G  4 112 ? 78.370  63.047  294.011 1.00 155.62 ?  103 TRP G CG  1 
ATOM   13917 C CD1 . TRP G  4 112 ? 78.613  64.263  294.577 1.00 154.59 ?  103 TRP G CD1 1 
ATOM   13918 C CD2 . TRP G  4 112 ? 77.943  62.187  295.072 1.00 158.00 ?  103 TRP G CD2 1 
ATOM   13919 N NE1 . TRP G  4 112 ? 78.359  64.217  295.925 1.00 156.19 ?  103 TRP G NE1 1 
ATOM   13920 C CE2 . TRP G  4 112 ? 77.947  62.952  296.254 1.00 158.36 ?  103 TRP G CE2 1 
ATOM   13921 C CE3 . TRP G  4 112 ? 77.557  60.845  295.137 1.00 160.24 ?  103 TRP G CE3 1 
ATOM   13922 C CZ2 . TRP G  4 112 ? 77.578  62.421  297.488 1.00 161.02 ?  103 TRP G CZ2 1 
ATOM   13923 C CZ3 . TRP G  4 112 ? 77.192  60.319  296.362 1.00 162.84 ?  103 TRP G CZ3 1 
ATOM   13924 C CH2 . TRP G  4 112 ? 77.206  61.105  297.521 1.00 163.26 ?  103 TRP G CH2 1 
ATOM   13925 N N   . GLY G  4 113 ? 80.446  60.836  290.691 1.00 144.50 ?  104 GLY G N   1 
ATOM   13926 C CA  . GLY G  4 113 ? 80.300  60.049  289.491 1.00 146.28 ?  104 GLY G CA  1 
ATOM   13927 C C   . GLY G  4 113 ? 78.839  59.844  289.153 1.00 147.34 ?  104 GLY G C   1 
ATOM   13928 O O   . GLY G  4 113 ? 77.929  60.177  289.915 1.00 146.79 ?  104 GLY G O   1 
ATOM   13929 N N   . GLN G  4 114 ? 78.612  59.272  287.975 1.00 142.99 ?  105 GLN G N   1 
ATOM   13930 C CA  . GLN G  4 114 ? 77.249  59.064  287.510 1.00 145.27 ?  105 GLN G CA  1 
ATOM   13931 C C   . GLN G  4 114 ? 76.578  57.866  288.163 1.00 147.84 ?  105 GLN G C   1 
ATOM   13932 O O   . GLN G  4 114 ? 75.358  57.711  288.031 1.00 150.22 ?  105 GLN G O   1 
ATOM   13933 C CB  . GLN G  4 114 ? 77.238  58.892  285.986 1.00 146.25 ?  105 GLN G CB  1 
ATOM   13934 C CG  . GLN G  4 114 ? 77.549  57.475  285.502 1.00 148.17 ?  105 GLN G CG  1 
ATOM   13935 C CD  . GLN G  4 114 ? 79.037  57.163  285.482 1.00 146.94 ?  105 GLN G CD  1 
ATOM   13936 O OE1 . GLN G  4 114 ? 79.842  57.863  286.097 1.00 144.64 ?  105 GLN G OE1 1 
ATOM   13937 N NE2 . GLN G  4 114 ? 79.408  56.101  284.775 1.00 148.96 ?  105 GLN G NE2 1 
ATOM   13938 N N   . GLY G  4 115 ? 77.328  57.038  288.872 1.00 139.10 ?  106 GLY G N   1 
ATOM   13939 C CA  . GLY G  4 115 ? 76.780  55.864  289.526 1.00 140.05 ?  106 GLY G CA  1 
ATOM   13940 C C   . GLY G  4 115 ? 76.884  54.624  288.664 1.00 142.03 ?  106 GLY G C   1 
ATOM   13941 O O   . GLY G  4 115 ? 76.775  54.663  287.440 1.00 143.19 ?  106 GLY G O   1 
ATOM   13942 N N   . THR G  4 116 ? 77.084  53.490  289.329 1.00 152.11 ?  107 THR G N   1 
ATOM   13943 C CA  . THR G  4 116 ? 77.143  52.188  288.679 1.00 154.84 ?  107 THR G CA  1 
ATOM   13944 C C   . THR G  4 116 ? 76.074  51.301  289.298 1.00 158.44 ?  107 THR G C   1 
ATOM   13945 O O   . THR G  4 116 ? 76.120  51.017  290.500 1.00 159.32 ?  107 THR G O   1 
ATOM   13946 C CB  . THR G  4 116 ? 78.527  51.554  288.838 1.00 154.69 ?  107 THR G CB  1 
ATOM   13947 O OG1 . THR G  4 116 ? 79.518  52.387  288.221 1.00 151.86 ?  107 THR G OG1 1 
ATOM   13948 C CG2 . THR G  4 116 ? 78.551  50.181  288.205 1.00 158.09 ?  107 THR G CG2 1 
ATOM   13949 N N   . SER G  4 117 ? 75.118  50.866  288.481 1.00 159.88 ?  108 SER G N   1 
ATOM   13950 C CA  . SER G  4 117 ? 74.062  49.983  288.954 1.00 163.96 ?  108 SER G CA  1 
ATOM   13951 C C   . SER G  4 117 ? 74.603  48.569  289.120 1.00 166.66 ?  108 SER G C   1 
ATOM   13952 O O   . SER G  4 117 ? 75.200  48.010  288.196 1.00 167.12 ?  108 SER G O   1 
ATOM   13953 C CB  . SER G  4 117 ? 72.882  49.995  287.983 1.00 166.32 ?  108 SER G CB  1 
ATOM   13954 O OG  . SER G  4 117 ? 71.833  49.168  288.453 1.00 170.72 ?  108 SER G OG  1 
ATOM   13955 N N   . VAL G  4 118 ? 74.406  47.998  290.305 1.00 175.16 ?  109 VAL G N   1 
ATOM   13956 C CA  . VAL G  4 118 ? 74.810  46.629  290.605 1.00 178.53 ?  109 VAL G CA  1 
ATOM   13957 C C   . VAL G  4 118 ? 73.569  45.848  291.016 1.00 183.42 ?  109 VAL G C   1 
ATOM   13958 O O   . VAL G  4 118 ? 72.865  46.240  291.955 1.00 184.40 ?  109 VAL G O   1 
ATOM   13959 C CB  . VAL G  4 118 ? 75.879  46.577  291.708 1.00 177.60 ?  109 VAL G CB  1 
ATOM   13960 C CG1 . VAL G  4 118 ? 76.187  45.135  292.088 1.00 182.00 ?  109 VAL G CG1 1 
ATOM   13961 C CG2 . VAL G  4 118 ? 77.141  47.296  291.258 1.00 173.44 ?  109 VAL G CG2 1 
ATOM   13962 N N   . THR G  4 119 ? 73.300  44.751  290.309 1.00 185.89 ?  110 THR G N   1 
ATOM   13963 C CA  . THR G  4 119 ? 72.191  43.854  290.619 1.00 191.26 ?  110 THR G CA  1 
ATOM   13964 C C   . THR G  4 119 ? 72.748  42.505  291.056 1.00 195.02 ?  110 THR G C   1 
ATOM   13965 O O   . THR G  4 119 ? 73.447  41.839  290.284 1.00 195.70 ?  110 THR G O   1 
ATOM   13966 C CB  . THR G  4 119 ? 71.270  43.681  289.410 1.00 193.40 ?  110 THR G CB  1 
ATOM   13967 O OG1 . THR G  4 119 ? 70.758  44.957  289.002 1.00 190.42 ?  110 THR G OG1 1 
ATOM   13968 C CG2 . THR G  4 119 ? 70.111  42.768  289.756 1.00 199.38 ?  110 THR G CG2 1 
ATOM   13969 N N   . VAL G  4 120 ? 72.429  42.101  292.284 1.00 183.99 ?  111 VAL G N   1 
ATOM   13970 C CA  . VAL G  4 120 ? 72.834  40.809  292.826 1.00 188.42 ?  111 VAL G CA  1 
ATOM   13971 C C   . VAL G  4 120 ? 71.596  39.935  292.938 1.00 194.46 ?  111 VAL G C   1 
ATOM   13972 O O   . VAL G  4 120 ? 70.672  40.250  293.699 1.00 196.35 ?  111 VAL G O   1 
ATOM   13973 C CB  . VAL G  4 120 ? 73.527  40.946  294.188 1.00 188.22 ?  111 VAL G CB  1 
ATOM   13974 C CG1 . VAL G  4 120 ? 73.935  39.572  294.704 1.00 193.42 ?  111 VAL G CG1 1 
ATOM   13975 C CG2 . VAL G  4 120 ? 74.733  41.863  294.079 1.00 182.61 ?  111 VAL G CG2 1 
ATOM   13976 N N   . SER G  4 121 ? 71.577  38.840  292.186 1.00 202.44 ?  112 SER G N   1 
ATOM   13977 C CA  . SER G  4 121 ? 70.417  37.965  292.168 1.00 207.17 ?  112 SER G CA  1 
ATOM   13978 C C   . SER G  4 121 ? 70.818  36.619  291.588 1.00 210.04 ?  112 SER G C   1 
ATOM   13979 O O   . SER G  4 121 ? 71.790  36.508  290.836 1.00 207.63 ?  112 SER G O   1 
ATOM   13980 C CB  . SER G  4 121 ? 69.270  38.576  291.357 1.00 205.80 ?  112 SER G CB  1 
ATOM   13981 O OG  . SER G  4 121 ? 68.149  37.711  291.326 1.00 210.64 ?  112 SER G OG  1 
ATOM   13982 N N   . SER G  4 122 ? 70.042  35.599  291.941 1.00 211.93 ?  113 SER G N   1 
ATOM   13983 C CA  . SER G  4 122 ? 70.144  34.312  291.276 1.00 215.15 ?  113 SER G CA  1 
ATOM   13984 C C   . SER G  4 122 ? 69.239  34.247  290.056 1.00 214.87 ?  113 SER G C   1 
ATOM   13985 O O   . SER G  4 122 ? 69.284  33.255  289.317 1.00 217.11 ?  113 SER G O   1 
ATOM   13986 C CB  . SER G  4 122 ? 69.797  33.179  292.248 1.00 221.73 ?  113 SER G CB  1 
ATOM   13987 O OG  . SER G  4 122 ? 70.804  33.028  293.234 1.00 222.58 ?  113 SER G OG  1 
ATOM   13988 N N   . ALA G  4 123 ? 68.426  35.284  289.841 1.00 241.25 ?  114 ALA G N   1 
ATOM   13989 C CA  . ALA G  4 123 ? 67.654  35.412  288.615 1.00 241.33 ?  114 ALA G CA  1 
ATOM   13990 C C   . ALA G  4 123 ? 68.605  35.555  287.437 1.00 237.06 ?  114 ALA G C   1 
ATOM   13991 O O   . ALA G  4 123 ? 69.745  36.008  287.576 1.00 235.33 ?  114 ALA G O   1 
ATOM   13992 C CB  . ALA G  4 123 ? 66.705  36.610  288.683 1.00 237.97 ?  114 ALA G CB  1 
ATOM   13993 N N   . SER G  4 124 ? 68.147  35.128  286.274 1.00 243.85 ?  115 SER G N   1 
ATOM   13994 C CA  . SER G  4 124 ? 68.996  35.147  285.103 1.00 241.08 ?  115 SER G CA  1 
ATOM   13995 C C   . SER G  4 124 ? 68.250  35.717  283.900 1.00 238.67 ?  115 SER G C   1 
ATOM   13996 O O   . SER G  4 124 ? 67.017  35.722  283.843 1.00 240.93 ?  115 SER G O   1 
ATOM   13997 C CB  . SER G  4 124 ? 69.547  33.745  284.856 1.00 244.97 ?  115 SER G CB  1 
ATOM   13998 O OG  . SER G  4 124 ? 70.288  33.244  285.957 1.00 246.09 ?  115 SER G OG  1 
ATOM   13999 N N   . THR G  4 125 ? 69.041  36.220  282.951 1.00 258.27 ?  116 THR G N   1 
ATOM   14000 C CA  . THR G  4 125 ? 68.585  37.117  281.890 1.00 255.15 ?  116 THR G CA  1 
ATOM   14001 C C   . THR G  4 125 ? 67.379  36.579  281.117 1.00 259.46 ?  116 THR G C   1 
ATOM   14002 O O   . THR G  4 125 ? 67.413  35.483  280.553 1.00 263.95 ?  116 THR G O   1 
ATOM   14003 C CB  . THR G  4 125 ? 69.755  37.385  280.933 1.00 253.66 ?  116 THR G CB  1 
ATOM   14004 O OG1 . THR G  4 125 ? 70.850  37.975  281.652 1.00 251.92 ?  116 THR G OG1 1 
ATOM   14005 C CG2 . THR G  4 125 ? 69.336  38.321  279.829 1.00 251.62 ?  116 THR G CG2 1 
ATOM   14006 N N   . LYS G  4 126 ? 66.321  37.379  281.049 1.00 242.69 ?  117 LYS G N   1 
ATOM   14007 C CA  . LYS G  4 126 ? 65.114  36.956  280.351 1.00 247.22 ?  117 LYS G CA  1 
ATOM   14008 C C   . LYS G  4 126 ? 64.444  38.166  279.726 1.00 244.45 ?  117 LYS G C   1 
ATOM   14009 O O   . LYS G  4 126 ? 64.296  39.201  280.382 1.00 241.62 ?  117 LYS G O   1 
ATOM   14010 C CB  . LYS G  4 126 ? 64.139  36.240  281.292 1.00 253.33 ?  117 LYS G CB  1 
ATOM   14011 C CG  . LYS G  4 126 ? 62.823  35.818  280.635 1.00 260.49 ?  117 LYS G CG  1 
ATOM   14012 C CD  . LYS G  4 126 ? 63.032  34.817  279.509 1.00 265.57 ?  117 LYS G CD  1 
ATOM   14013 C CE  . LYS G  4 126 ? 61.698  34.351  278.939 1.00 270.50 ?  117 LYS G CE  1 
ATOM   14014 N NZ  . LYS G  4 126 ? 60.963  35.436  278.235 1.00 269.35 1  117 LYS G NZ  1 
ATOM   14015 N N   . GLY G  4 127 ? 64.040  38.034  278.467 1.00 240.06 ?  118 GLY G N   1 
ATOM   14016 C CA  . GLY G  4 127 ? 63.254  39.061  277.835 1.00 238.42 ?  118 GLY G CA  1 
ATOM   14017 C C   . GLY G  4 127 ? 61.837  39.029  278.368 1.00 241.83 ?  118 GLY G C   1 
ATOM   14018 O O   . GLY G  4 127 ? 61.315  37.974  278.742 1.00 246.98 ?  118 GLY G O   1 
ATOM   14019 N N   . PRO G  4 128 ? 61.181  40.185  278.408 1.00 230.26 ?  119 PRO G N   1 
ATOM   14020 C CA  . PRO G  4 128 ? 59.843  40.247  279.001 1.00 233.96 ?  119 PRO G CA  1 
ATOM   14021 C C   . PRO G  4 128 ? 58.781  39.593  278.135 1.00 238.83 ?  119 PRO G C   1 
ATOM   14022 O O   . PRO G  4 128 ? 58.899  39.511  276.910 1.00 239.46 ?  119 PRO G O   1 
ATOM   14023 C CB  . PRO G  4 128 ? 59.589  41.751  279.133 1.00 232.43 ?  119 PRO G CB  1 
ATOM   14024 C CG  . PRO G  4 128 ? 60.393  42.350  278.032 1.00 229.16 ?  119 PRO G CG  1 
ATOM   14025 C CD  . PRO G  4 128 ? 61.645  41.511  277.962 1.00 226.25 ?  119 PRO G CD  1 
ATOM   14026 N N   . SER G  4 129 ? 57.732  39.117  278.799 1.00 227.76 ?  120 SER G N   1 
ATOM   14027 C CA  . SER G  4 129 ? 56.481  38.784  278.137 1.00 232.70 ?  120 SER G CA  1 
ATOM   14028 C C   . SER G  4 129 ? 55.608  40.032  278.112 1.00 232.98 ?  120 SER G C   1 
ATOM   14029 O O   . SER G  4 129 ? 55.390  40.661  279.152 1.00 232.72 ?  120 SER G O   1 
ATOM   14030 C CB  . SER G  4 129 ? 55.768  37.641  278.860 1.00 238.40 ?  120 SER G CB  1 
ATOM   14031 O OG  . SER G  4 129 ? 56.588  36.487  278.922 1.00 238.63 ?  120 SER G OG  1 
ATOM   14032 N N   . VAL G  4 130 ? 55.122  40.393  276.927 1.00 238.32 ?  121 VAL G N   1 
ATOM   14033 C CA  . VAL G  4 130 ? 54.360  41.622  276.726 1.00 238.81 ?  121 VAL G CA  1 
ATOM   14034 C C   . VAL G  4 130 ? 52.923  41.254  276.381 1.00 245.24 ?  121 VAL G C   1 
ATOM   14035 O O   . VAL G  4 130 ? 52.671  40.571  275.381 1.00 247.46 ?  121 VAL G O   1 
ATOM   14036 C CB  . VAL G  4 130 ? 54.984  42.500  275.631 1.00 234.62 ?  121 VAL G CB  1 
ATOM   14037 C CG1 . VAL G  4 130 ? 54.200  43.795  275.481 1.00 235.46 ?  121 VAL G CG1 1 
ATOM   14038 C CG2 . VAL G  4 130 ? 56.445  42.780  275.952 1.00 228.65 ?  121 VAL G CG2 1 
ATOM   14039 N N   . PHE G  4 131 ? 51.984  41.713  277.207 1.00 243.35 ?  122 PHE G N   1 
ATOM   14040 C CA  . PHE G  4 131 ? 50.570  41.413  277.063 1.00 250.12 ?  122 PHE G CA  1 
ATOM   14041 C C   . PHE G  4 131 ? 49.762  42.697  276.929 1.00 251.68 ?  122 PHE G C   1 
ATOM   14042 O O   . PHE G  4 131 ? 50.107  43.722  277.526 1.00 248.62 ?  122 PHE G O   1 
ATOM   14043 C CB  . PHE G  4 131 ? 50.049  40.604  278.256 1.00 254.53 ?  122 PHE G CB  1 
ATOM   14044 C CG  . PHE G  4 131 ? 50.833  39.352  278.525 1.00 253.67 ?  122 PHE G CG  1 
ATOM   14045 C CD1 . PHE G  4 131 ? 50.860  38.325  277.596 1.00 255.29 ?  122 PHE G CD1 1 
ATOM   14046 C CD2 . PHE G  4 131 ? 51.548  39.204  279.703 1.00 251.60 ?  122 PHE G CD2 1 
ATOM   14047 C CE1 . PHE G  4 131 ? 51.585  37.170  277.837 1.00 254.93 ?  122 PHE G CE1 1 
ATOM   14048 C CE2 . PHE G  4 131 ? 52.274  38.052  279.951 1.00 251.26 ?  122 PHE G CE2 1 
ATOM   14049 C CZ  . PHE G  4 131 ? 52.292  37.034  279.017 1.00 252.97 ?  122 PHE G CZ  1 
ATOM   14050 N N   . PRO G  4 132 ? 48.688  42.675  276.145 1.00 251.19 ?  123 PRO G N   1 
ATOM   14051 C CA  . PRO G  4 132 ? 47.877  43.883  275.982 1.00 253.41 ?  123 PRO G CA  1 
ATOM   14052 C C   . PRO G  4 132 ? 47.032  44.177  277.209 1.00 257.64 ?  123 PRO G C   1 
ATOM   14053 O O   . PRO G  4 132 ? 46.475  43.275  277.842 1.00 262.22 ?  123 PRO G O   1 
ATOM   14054 C CB  . PRO G  4 132 ? 46.997  43.551  274.773 1.00 258.25 ?  123 PRO G CB  1 
ATOM   14055 C CG  . PRO G  4 132 ? 46.841  42.077  274.853 1.00 261.24 ?  123 PRO G CG  1 
ATOM   14056 C CD  . PRO G  4 132 ? 48.183  41.567  275.316 1.00 255.31 ?  123 PRO G CD  1 
ATOM   14057 N N   . LEU G  4 133 ? 46.938  45.460  277.534 1.00 259.40 ?  124 LEU G N   1 
ATOM   14058 C CA  . LEU G  4 133 ? 45.910  45.976  278.431 1.00 265.05 ?  124 LEU G CA  1 
ATOM   14059 C C   . LEU G  4 133 ? 44.876  46.631  277.526 1.00 269.27 ?  124 LEU G C   1 
ATOM   14060 O O   . LEU G  4 133 ? 45.043  47.775  277.097 1.00 266.58 ?  124 LEU G O   1 
ATOM   14061 C CB  . LEU G  4 133 ? 46.484  46.955  279.451 1.00 261.20 ?  124 LEU G CB  1 
ATOM   14062 C CG  . LEU G  4 133 ? 47.530  46.419  280.431 1.00 256.65 ?  124 LEU G CG  1 
ATOM   14063 C CD1 . LEU G  4 133 ? 48.192  47.557  281.200 1.00 252.78 ?  124 LEU G CD1 1 
ATOM   14064 C CD2 . LEU G  4 133 ? 46.900  45.416  281.387 1.00 263.54 ?  124 LEU G CD2 1 
ATOM   14065 N N   . ALA G  4 134 ? 43.816  45.909  277.241 1.00 256.64 ?  125 ALA G N   1 
ATOM   14066 C CA  . ALA G  4 134 ? 42.956  46.355  276.161 1.00 259.74 ?  125 ALA G CA  1 
ATOM   14067 C C   . ALA G  4 134 ? 42.069  47.502  276.636 1.00 265.83 ?  125 ALA G C   1 
ATOM   14068 O O   . ALA G  4 134 ? 41.575  47.476  277.766 1.00 275.35 ?  125 ALA G O   1 
ATOM   14069 C CB  . ALA G  4 134 ? 42.089  45.203  275.663 1.00 268.18 ?  125 ALA G CB  1 
ATOM   14070 N N   . PRO G  4 135 ? 41.845  48.511  275.795 1.00 266.82 ?  126 PRO G N   1 
ATOM   14071 C CA  . PRO G  4 135 ? 40.975  49.619  276.200 1.00 271.28 ?  126 PRO G CA  1 
ATOM   14072 C C   . PRO G  4 135 ? 39.561  49.117  276.435 1.00 287.98 ?  126 PRO G C   1 
ATOM   14073 O O   . PRO G  4 135 ? 39.047  48.284  275.685 1.00 294.71 ?  126 PRO G O   1 
ATOM   14074 C CB  . PRO G  4 135 ? 41.045  50.581  275.009 1.00 270.49 ?  126 PRO G CB  1 
ATOM   14075 C CG  . PRO G  4 135 ? 41.395  49.704  273.850 1.00 269.40 ?  126 PRO G CG  1 
ATOM   14076 C CD  . PRO G  4 135 ? 42.326  48.666  274.412 1.00 263.75 ?  126 PRO G CD  1 
ATOM   14077 N N   . SER G  4 136 ? 38.943  49.617  277.501 1.00 278.31 ?  127 SER G N   1 
ATOM   14078 C CA  . SER G  4 136 ? 37.582  49.213  277.819 1.00 297.55 ?  127 SER G CA  1 
ATOM   14079 C C   . SER G  4 136 ? 36.645  49.554  276.667 1.00 301.13 ?  127 SER G C   1 
ATOM   14080 O O   . SER G  4 136 ? 36.708  50.645  276.093 1.00 294.64 ?  127 SER G O   1 
ATOM   14081 C CB  . SER G  4 136 ? 37.115  49.897  279.106 1.00 304.94 ?  127 SER G CB  1 
ATOM   14082 O OG  . SER G  4 136 ? 35.739  49.657  279.351 1.00 323.19 ?  127 SER G OG  1 
ATOM   14083 N N   . SER G  4 137 ? 35.768  48.606  276.326 1.00 286.36 ?  128 SER G N   1 
ATOM   14084 C CA  . SER G  4 137 ? 34.739  48.875  275.330 1.00 289.98 ?  128 SER G CA  1 
ATOM   14085 C C   . SER G  4 137 ? 33.696  49.851  275.846 1.00 298.12 ?  128 SER G C   1 
ATOM   14086 O O   . SER G  4 137 ? 32.880  50.342  275.055 1.00 301.23 ?  128 SER G O   1 
ATOM   14087 C CB  . SER G  4 137 ? 34.065  47.572  274.895 1.00 297.70 ?  128 SER G CB  1 
ATOM   14088 O OG  . SER G  4 137 ? 33.475  46.911  276.001 1.00 306.55 ?  128 SER G OG  1 
ATOM   14089 N N   . LYS G  4 138 ? 33.716  50.146  277.145 1.00 305.49 ?  129 LYS G N   1 
ATOM   14090 C CA  . LYS G  4 138 ? 32.805  51.093  277.768 1.00 311.71 ?  129 LYS G CA  1 
ATOM   14091 C C   . LYS G  4 138 ? 33.399  52.497  277.803 1.00 299.05 ?  129 LYS G C   1 
ATOM   14092 O O   . LYS G  4 138 ? 32.858  53.371  278.488 1.00 303.36 ?  129 LYS G O   1 
ATOM   14093 C CB  . LYS G  4 138 ? 32.455  50.647  279.202 1.00 323.20 ?  129 LYS G CB  1 
ATOM   14094 C CG  . LYS G  4 138 ? 31.938  49.194  279.427 1.00 331.10 ?  129 LYS G CG  1 
ATOM   14095 C CD  . LYS G  4 138 ? 31.426  48.469  278.178 1.00 329.58 ?  129 LYS G CD  1 
ATOM   14096 C CE  . LYS G  4 138 ? 30.013  48.875  277.789 1.00 338.40 ?  129 LYS G CE  1 
ATOM   14097 N NZ  . LYS G  4 138 ? 29.543  48.116  276.595 1.00 335.98 1  129 LYS G NZ  1 
ATOM   14098 N N   . SER G  4 139 ? 34.509  52.714  277.093 1.00 316.26 ?  130 SER G N   1 
ATOM   14099 C CA  . SER G  4 139 ? 35.193  54.000  277.080 1.00 306.85 ?  130 SER G CA  1 
ATOM   14100 C C   . SER G  4 139 ? 34.230  55.138  276.763 1.00 314.93 ?  130 SER G C   1 
ATOM   14101 O O   . SER G  4 139 ? 33.334  55.006  275.925 1.00 320.16 ?  130 SER G O   1 
ATOM   14102 C CB  . SER G  4 139 ? 36.338  53.976  276.063 1.00 296.77 ?  130 SER G CB  1 
ATOM   14103 O OG  . SER G  4 139 ? 37.371  53.097  276.480 1.00 288.02 ?  130 SER G OG  1 
ATOM   14104 N N   . THR G  4 140 ? 34.427  56.259  277.451 1.00 307.11 ?  131 THR G N   1 
ATOM   14105 C CA  . THR G  4 140 ? 33.474  57.361  277.404 1.00 314.52 ?  131 THR G CA  1 
ATOM   14106 C C   . THR G  4 140 ? 33.357  57.944  276.002 1.00 315.55 ?  131 THR G C   1 
ATOM   14107 O O   . THR G  4 140 ? 34.362  58.258  275.360 1.00 307.43 ?  131 THR G O   1 
ATOM   14108 C CB  . THR G  4 140 ? 33.896  58.454  278.382 1.00 313.14 ?  131 THR G CB  1 
ATOM   14109 O OG1 . THR G  4 140 ? 34.163  57.869  279.662 1.00 314.75 ?  131 THR G OG1 1 
ATOM   14110 C CG2 . THR G  4 140 ? 32.801  59.498  278.511 1.00 322.96 ?  131 THR G CG2 1 
ATOM   14111 N N   . SER G  4 141 ? 32.122  58.090  275.534 1.00 302.37 ?  132 SER G N   1 
ATOM   14112 C CA  . SER G  4 141 ? 31.869  58.690  274.230 1.00 303.40 ?  132 SER G CA  1 
ATOM   14113 C C   . SER G  4 141 ? 32.394  60.117  274.171 1.00 302.86 ?  132 SER G C   1 
ATOM   14114 O O   . SER G  4 141 ? 32.001  60.965  274.978 1.00 305.98 ?  132 SER G O   1 
ATOM   14115 C CB  . SER G  4 141 ? 30.373  58.684  273.945 1.00 316.18 ?  132 SER G CB  1 
ATOM   14116 O OG  . SER G  4 141 ? 30.070  59.555  272.876 1.00 322.49 ?  132 SER G OG  1 
ATOM   14117 N N   . GLY G  4 142 ? 33.276  60.380  273.206 1.00 313.68 ?  133 GLY G N   1 
ATOM   14118 C CA  . GLY G  4 142 ? 33.932  61.669  273.097 1.00 310.66 ?  133 GLY G CA  1 
ATOM   14119 C C   . GLY G  4 142 ? 34.842  61.946  274.273 1.00 302.06 ?  133 GLY G C   1 
ATOM   14120 O O   . GLY G  4 142 ? 35.366  63.052  274.427 1.00 304.70 ?  133 GLY G O   1 
ATOM   14121 N N   . GLY G  4 143 ? 35.009  60.942  275.120 1.00 318.98 ?  134 GLY G N   1 
ATOM   14122 C CA  . GLY G  4 143 ? 35.766  61.036  276.342 1.00 313.40 ?  134 GLY G CA  1 
ATOM   14123 C C   . GLY G  4 143 ? 37.166  60.490  276.183 1.00 305.27 ?  134 GLY G C   1 
ATOM   14124 O O   . GLY G  4 143 ? 37.758  60.537  275.098 1.00 298.22 ?  134 GLY G O   1 
ATOM   14125 N N   . THR G  4 144 ? 37.709  59.967  277.278 1.00 287.97 ?  135 THR G N   1 
ATOM   14126 C CA  . THR G  4 144 ? 39.081  59.482  277.319 1.00 277.21 ?  135 THR G CA  1 
ATOM   14127 C C   . THR G  4 144 ? 39.097  57.971  277.520 1.00 275.67 ?  135 THR G C   1 
ATOM   14128 O O   . THR G  4 144 ? 38.401  57.449  278.399 1.00 280.86 ?  135 THR G O   1 
ATOM   14129 C CB  . THR G  4 144 ? 39.870  60.169  278.439 1.00 272.54 ?  135 THR G CB  1 
ATOM   14130 O OG1 . THR G  4 144 ? 39.983  61.571  278.164 1.00 276.02 ?  135 THR G OG1 1 
ATOM   14131 C CG2 . THR G  4 144 ? 41.266  59.578  278.558 1.00 263.73 ?  135 THR G CG2 1 
ATOM   14132 N N   . ALA G  4 145 ? 39.889  57.276  276.705 1.00 282.03 ?  136 ALA G N   1 
ATOM   14133 C CA  . ALA G  4 145 ? 40.110  55.844  276.829 1.00 281.22 ?  136 ALA G CA  1 
ATOM   14134 C C   . ALA G  4 145 ? 41.559  55.593  277.224 1.00 271.36 ?  136 ALA G C   1 
ATOM   14135 O O   . ALA G  4 145 ? 42.467  56.321  276.812 1.00 266.69 ?  136 ALA G O   1 
ATOM   14136 C CB  . ALA G  4 145 ? 39.781  55.112  275.521 1.00 282.95 ?  136 ALA G CB  1 
ATOM   14137 N N   . ALA G  4 146 ? 41.771  54.555  278.026 1.00 278.21 ?  137 ALA G N   1 
ATOM   14138 C CA  . ALA G  4 146 ? 43.102  54.158  278.456 1.00 270.14 ?  137 ALA G CA  1 
ATOM   14139 C C   . ALA G  4 146 ? 43.421  52.765  277.934 1.00 267.71 ?  137 ALA G C   1 
ATOM   14140 O O   . ALA G  4 146 ? 42.554  51.885  277.909 1.00 272.96 ?  137 ALA G O   1 
ATOM   14141 C CB  . ALA G  4 146 ? 43.221  54.197  279.984 1.00 270.51 ?  137 ALA G CB  1 
ATOM   14142 N N   . LEU G  4 147 ? 44.670  52.579  277.512 1.00 259.98 ?  138 LEU G N   1 
ATOM   14143 C CA  . LEU G  4 147 ? 45.173  51.294  277.054 1.00 257.39 ?  138 LEU G CA  1 
ATOM   14144 C C   . LEU G  4 147 ? 46.652  51.231  277.399 1.00 249.28 ?  138 LEU G C   1 
ATOM   14145 O O   . LEU G  4 147 ? 47.252  52.224  277.814 1.00 245.64 ?  138 LEU G O   1 
ATOM   14146 C CB  . LEU G  4 147 ? 44.934  51.111  275.552 1.00 258.60 ?  138 LEU G CB  1 
ATOM   14147 C CG  . LEU G  4 147 ? 45.501  52.222  274.666 1.00 255.01 ?  138 LEU G CG  1 
ATOM   14148 C CD1 . LEU G  4 147 ? 46.770  51.760  273.972 1.00 248.93 ?  138 LEU G CD1 1 
ATOM   14149 C CD2 . LEU G  4 147 ? 44.461  52.695  273.660 1.00 263.67 ?  138 LEU G CD2 1 
ATOM   14150 N N   . GLY G  4 148 ? 47.251  50.063  277.215 1.00 249.22 ?  139 GLY G N   1 
ATOM   14151 C CA  . GLY G  4 148 ? 48.641  49.931  277.594 1.00 242.43 ?  139 GLY G CA  1 
ATOM   14152 C C   . GLY G  4 148 ? 49.191  48.561  277.279 1.00 240.25 ?  139 GLY G C   1 
ATOM   14153 O O   . GLY G  4 148 ? 48.551  47.747  276.611 1.00 244.19 ?  139 GLY G O   1 
ATOM   14154 N N   . CYS G  4 149 ? 50.401  48.327  277.793 1.00 230.15 ?  140 CYS G N   1 
ATOM   14155 C CA  . CYS G  4 149 ? 51.109  47.057  277.688 1.00 229.64 ?  140 CYS G CA  1 
ATOM   14156 C C   . CYS G  4 149 ? 51.664  46.662  279.045 1.00 229.15 ?  140 CYS G C   1 
ATOM   14157 O O   . CYS G  4 149 ? 52.259  47.489  279.743 1.00 228.50 ?  140 CYS G O   1 
ATOM   14158 C CB  . CYS G  4 149 ? 52.260  47.132  276.682 1.00 228.68 ?  140 CYS G CB  1 
ATOM   14159 S SG  . CYS G  4 149 ? 51.755  47.128  274.969 1.00 229.28 ?  140 CYS G SG  1 
ATOM   14160 N N   . LEU G  4 150 ? 51.473  45.395  279.407 1.00 239.88 ?  141 LEU G N   1 
ATOM   14161 C CA  . LEU G  4 150 ? 52.072  44.815  280.603 1.00 239.27 ?  141 LEU G CA  1 
ATOM   14162 C C   . LEU G  4 150 ? 53.391  44.149  280.222 1.00 235.01 ?  141 LEU G C   1 
ATOM   14163 O O   . LEU G  4 150 ? 53.415  43.244  279.381 1.00 235.46 ?  141 LEU G O   1 
ATOM   14164 C CB  . LEU G  4 150 ? 51.114  43.814  281.247 1.00 245.52 ?  141 LEU G CB  1 
ATOM   14165 C CG  . LEU G  4 150 ? 51.580  43.012  282.463 1.00 246.81 ?  141 LEU G CG  1 
ATOM   14166 C CD1 . LEU G  4 150 ? 51.952  43.940  283.611 1.00 246.36 ?  141 LEU G CD1 1 
ATOM   14167 C CD2 . LEU G  4 150 ? 50.488  42.045  282.887 1.00 255.15 ?  141 LEU G CD2 1 
ATOM   14168 N N   . VAL G  4 151 ? 54.479  44.596  280.838 1.00 224.33 ?  142 VAL G N   1 
ATOM   14169 C CA  . VAL G  4 151 ? 55.826  44.126  280.533 1.00 223.36 ?  142 VAL G CA  1 
ATOM   14170 C C   . VAL G  4 151 ? 56.294  43.316  281.736 1.00 223.23 ?  142 VAL G C   1 
ATOM   14171 O O   . VAL G  4 151 ? 56.726  43.880  282.748 1.00 222.82 ?  142 VAL G O   1 
ATOM   14172 C CB  . VAL G  4 151 ? 56.772  45.292  280.225 1.00 222.38 ?  142 VAL G CB  1 
ATOM   14173 C CG1 . VAL G  4 151 ? 58.151  44.785  279.878 1.00 221.46 ?  142 VAL G CG1 1 
ATOM   14174 C CG2 . VAL G  4 151 ? 56.214  46.144  279.092 1.00 222.65 ?  142 VAL G CG2 1 
ATOM   14175 N N   . LYS G  4 152 ? 56.212  41.989  281.635 1.00 227.39 ?  143 LYS G N   1 
ATOM   14176 C CA  . LYS G  4 152 ? 56.272  41.110  282.796 1.00 229.59 ?  143 LYS G CA  1 
ATOM   14177 C C   . LYS G  4 152 ? 57.397  40.089  282.672 1.00 228.73 ?  143 LYS G C   1 
ATOM   14178 O O   . LYS G  4 152 ? 57.693  39.601  281.576 1.00 228.13 ?  143 LYS G O   1 
ATOM   14179 C CB  . LYS G  4 152 ? 54.932  40.386  282.986 1.00 238.07 ?  143 LYS G CB  1 
ATOM   14180 C CG  . LYS G  4 152 ? 54.840  39.543  284.248 1.00 244.23 ?  143 LYS G CG  1 
ATOM   14181 C CD  . LYS G  4 152 ? 53.411  39.103  284.511 1.00 251.24 ?  143 LYS G CD  1 
ATOM   14182 C CE  . LYS G  4 152 ? 53.366  37.930  285.474 1.00 257.18 ?  143 LYS G CE  1 
ATOM   14183 N NZ  . LYS G  4 152 ? 53.975  38.280  286.787 1.00 258.35 1  143 LYS G NZ  1 
ATOM   14184 N N   . ASP G  4 153 ? 58.017  39.778  283.815 1.00 240.93 ?  144 ASP G N   1 
ATOM   14185 C CA  . ASP G  4 153 ? 58.981  38.684  283.960 1.00 240.87 ?  144 ASP G CA  1 
ATOM   14186 C C   . ASP G  4 153 ? 60.217  38.879  283.080 1.00 235.82 ?  144 ASP G C   1 
ATOM   14187 O O   . ASP G  4 153 ? 60.532  38.057  282.217 1.00 236.86 ?  144 ASP G O   1 
ATOM   14188 C CB  . ASP G  4 153 ? 58.325  37.328  283.674 1.00 246.70 ?  144 ASP G CB  1 
ATOM   14189 C CG  . ASP G  4 153 ? 57.377  36.890  284.770 1.00 253.72 ?  144 ASP G CG  1 
ATOM   14190 O OD1 . ASP G  4 153 ? 57.461  37.430  285.895 1.00 253.62 ?  144 ASP G OD1 1 
ATOM   14191 O OD2 . ASP G  4 153 ? 56.556  35.986  284.507 1.00 261.60 -1 144 ASP G OD2 1 
ATOM   14192 N N   . TYR G  4 154 ? 60.934  39.974  283.324 1.00 240.99 ?  145 TYR G N   1 
ATOM   14193 C CA  . TYR G  4 154 ? 62.208  40.195  282.659 1.00 235.96 ?  145 TYR G CA  1 
ATOM   14194 C C   . TYR G  4 154 ? 63.308  40.409  283.690 1.00 232.59 ?  145 TYR G C   1 
ATOM   14195 O O   . TYR G  4 154 ? 63.058  40.805  284.833 1.00 234.58 ?  145 TYR G O   1 
ATOM   14196 C CB  . TYR G  4 154 ? 62.163  41.389  281.692 1.00 232.72 ?  145 TYR G CB  1 
ATOM   14197 C CG  . TYR G  4 154 ? 61.934  42.745  282.326 1.00 230.35 ?  145 TYR G CG  1 
ATOM   14198 C CD1 . TYR G  4 154 ? 60.651  43.237  282.532 1.00 233.99 ?  145 TYR G CD1 1 
ATOM   14199 C CD2 . TYR G  4 154 ? 63.008  43.547  282.692 1.00 225.71 ?  145 TYR G CD2 1 
ATOM   14200 C CE1 . TYR G  4 154 ? 60.447  44.484  283.102 1.00 232.48 ?  145 TYR G CE1 1 
ATOM   14201 C CE2 . TYR G  4 154 ? 62.814  44.792  283.262 1.00 224.51 ?  145 TYR G CE2 1 
ATOM   14202 C CZ  . TYR G  4 154 ? 61.533  45.256  283.463 1.00 228.16 ?  145 TYR G CZ  1 
ATOM   14203 O OH  . TYR G  4 154 ? 61.335  46.495  284.027 1.00 228.32 ?  145 TYR G OH  1 
ATOM   14204 N N   . PHE G  4 155 ? 64.538  40.139  283.265 1.00 245.92 ?  146 PHE G N   1 
ATOM   14205 C CA  . PHE G  4 155 ? 65.715  40.362  284.092 1.00 241.31 ?  146 PHE G CA  1 
ATOM   14206 C C   . PHE G  4 155 ? 66.956  40.539  283.226 1.00 236.99 ?  146 PHE G C   1 
ATOM   14207 O O   . PHE G  4 155 ? 67.088  39.884  282.194 1.00 240.59 ?  146 PHE G O   1 
ATOM   14208 C CB  . PHE G  4 155 ? 65.914  39.198  285.068 1.00 241.64 ?  146 PHE G CB  1 
ATOM   14209 C CG  . PHE G  4 155 ? 67.114  39.350  285.956 1.00 232.73 ?  146 PHE G CG  1 
ATOM   14210 C CD1 . PHE G  4 155 ? 68.350  38.855  285.568 1.00 227.35 ?  146 PHE G CD1 1 
ATOM   14211 C CD2 . PHE G  4 155 ? 67.012  40.004  287.171 1.00 229.06 ?  146 PHE G CD2 1 
ATOM   14212 C CE1 . PHE G  4 155 ? 69.455  39.001  286.380 1.00 217.37 ?  146 PHE G CE1 1 
ATOM   14213 C CE2 . PHE G  4 155 ? 68.114  40.154  287.988 1.00 219.37 ?  146 PHE G CE2 1 
ATOM   14214 C CZ  . PHE G  4 155 ? 69.338  39.651  287.592 1.00 213.05 ?  146 PHE G CZ  1 
ATOM   14215 N N   . PRO G  4 156 ? 67.865  41.438  283.634 1.00 228.90 ?  147 PRO G N   1 
ATOM   14216 C CA  . PRO G  4 156 ? 67.706  42.428  284.702 1.00 221.01 ?  147 PRO G CA  1 
ATOM   14217 C C   . PRO G  4 156 ? 67.047  43.691  284.175 1.00 218.32 ?  147 PRO G C   1 
ATOM   14218 O O   . PRO G  4 156 ? 66.570  43.682  283.042 1.00 222.84 ?  147 PRO G O   1 
ATOM   14219 C CB  . PRO G  4 156 ? 69.144  42.696  285.130 1.00 207.34 ?  147 PRO G CB  1 
ATOM   14220 C CG  . PRO G  4 156 ? 69.902  42.586  283.854 1.00 205.64 ?  147 PRO G CG  1 
ATOM   14221 C CD  . PRO G  4 156 ? 69.225  41.480  283.067 1.00 220.24 ?  147 PRO G CD  1 
ATOM   14222 N N   . GLU G  4 157 ? 67.004  44.752  284.976 1.00 210.66 ?  148 GLU G N   1 
ATOM   14223 C CA  . GLU G  4 157 ? 66.655  46.056  284.433 1.00 203.67 ?  148 GLU G CA  1 
ATOM   14224 C C   . GLU G  4 157 ? 67.776  46.520  283.509 1.00 201.19 ?  148 GLU G C   1 
ATOM   14225 O O   . GLU G  4 157 ? 68.900  46.026  283.601 1.00 200.77 ?  148 GLU G O   1 
ATOM   14226 C CB  . GLU G  4 157 ? 66.407  47.083  285.544 1.00 203.76 ?  148 GLU G CB  1 
ATOM   14227 C CG  . GLU G  4 157 ? 65.142  46.857  286.341 1.00 209.52 ?  148 GLU G CG  1 
ATOM   14228 C CD  . GLU G  4 157 ? 64.613  48.148  286.930 1.00 217.90 ?  148 GLU G CD  1 
ATOM   14229 O OE1 . GLU G  4 157 ? 64.958  48.467  288.087 1.00 219.10 ?  148 GLU G OE1 1 
ATOM   14230 O OE2 . GLU G  4 157 ? 63.884  48.866  286.213 1.00 215.77 -1 148 GLU G OE2 1 
ATOM   14231 N N   . PRO G  4 158 ? 67.479  47.474  282.614 1.00 217.94 ?  149 PRO G N   1 
ATOM   14232 C CA  . PRO G  4 158 ? 66.156  48.032  282.322 1.00 220.23 ?  149 PRO G CA  1 
ATOM   14233 C C   . PRO G  4 158 ? 65.507  47.506  281.046 1.00 222.82 ?  149 PRO G C   1 
ATOM   14234 O O   . PRO G  4 158 ? 66.123  46.767  280.277 1.00 222.94 ?  149 PRO G O   1 
ATOM   14235 C CB  . PRO G  4 158 ? 66.459  49.517  282.177 1.00 218.05 ?  149 PRO G CB  1 
ATOM   14236 C CG  . PRO G  4 158 ? 67.807  49.515  281.500 1.00 215.29 ?  149 PRO G CG  1 
ATOM   14237 C CD  . PRO G  4 158 ? 68.541  48.269  281.974 1.00 215.56 ?  149 PRO G CD  1 
ATOM   14238 N N   . VAL G  4 159 ? 64.253  47.898  280.844 1.00 228.82 ?  150 VAL G N   1 
ATOM   14239 C CA  . VAL G  4 159 ? 63.596  47.827  279.548 1.00 229.57 ?  150 VAL G CA  1 
ATOM   14240 C C   . VAL G  4 159 ? 63.359  49.250  279.070 1.00 228.51 ?  150 VAL G C   1 
ATOM   14241 O O   . VAL G  4 159 ? 63.265  50.189  279.869 1.00 229.98 ?  150 VAL G O   1 
ATOM   14242 C CB  . VAL G  4 159 ? 62.268  47.041  279.602 1.00 234.67 ?  150 VAL G CB  1 
ATOM   14243 C CG1 . VAL G  4 159 ? 62.532  45.567  279.845 1.00 241.77 ?  150 VAL G CG1 1 
ATOM   14244 C CG2 . VAL G  4 159 ? 61.354  47.613  280.678 1.00 237.34 ?  150 VAL G CG2 1 
ATOM   14245 N N   . THR G  4 160 ? 63.266  49.410  277.755 1.00 237.68 ?  151 THR G N   1 
ATOM   14246 C CA  . THR G  4 160 ? 62.794  50.645  277.149 1.00 237.47 ?  151 THR G CA  1 
ATOM   14247 C C   . THR G  4 160 ? 61.431  50.395  276.525 1.00 241.91 ?  151 THR G C   1 
ATOM   14248 O O   . THR G  4 160 ? 61.207  49.352  275.902 1.00 244.33 ?  151 THR G O   1 
ATOM   14249 C CB  . THR G  4 160 ? 63.769  51.159  276.087 1.00 236.69 ?  151 THR G CB  1 
ATOM   14250 O OG1 . THR G  4 160 ? 63.923  50.173  275.061 1.00 240.56 ?  151 THR G OG1 1 
ATOM   14251 C CG2 . THR G  4 160 ? 65.128  51.446  276.707 1.00 233.66 ?  151 THR G CG2 1 
ATOM   14252 N N   . VAL G  4 161 ? 60.521  51.348  276.703 1.00 227.42 ?  152 VAL G N   1 
ATOM   14253 C CA  . VAL G  4 161 ? 59.168  51.255  276.172 1.00 231.80 ?  152 VAL G CA  1 
ATOM   14254 C C   . VAL G  4 161 ? 58.874  52.517  275.375 1.00 232.62 ?  152 VAL G C   1 
ATOM   14255 O O   . VAL G  4 161 ? 59.065  53.632  275.873 1.00 231.90 ?  152 VAL G O   1 
ATOM   14256 C CB  . VAL G  4 161 ? 58.122  51.064  277.289 1.00 235.73 ?  152 VAL G CB  1 
ATOM   14257 C CG1 . VAL G  4 161 ? 56.736  50.859  276.687 1.00 242.65 ?  152 VAL G CG1 1 
ATOM   14258 C CG2 . VAL G  4 161 ? 58.505  49.895  278.201 1.00 237.28 ?  152 VAL G CG2 1 
ATOM   14259 N N   . SER G  4 162 ? 58.415  52.339  274.140 1.00 225.12 ?  153 SER G N   1 
ATOM   14260 C CA  . SER G  4 162 ? 57.898  53.422  273.322 1.00 225.60 ?  153 SER G CA  1 
ATOM   14261 C C   . SER G  4 162 ? 56.518  53.033  272.814 1.00 226.85 ?  153 SER G C   1 
ATOM   14262 O O   . SER G  4 162 ? 56.114  51.868  272.872 1.00 227.24 ?  153 SER G O   1 
ATOM   14263 C CB  . SER G  4 162 ? 58.830  53.737  272.144 1.00 225.12 ?  153 SER G CB  1 
ATOM   14264 O OG  . SER G  4 162 ? 58.964  52.618  271.286 1.00 225.30 ?  153 SER G OG  1 
ATOM   14265 N N   . TRP G  4 163 ? 55.792  54.025  272.312 1.00 225.03 ?  154 TRP G N   1 
ATOM   14266 C CA  . TRP G  4 163 ? 54.500  53.800  271.685 1.00 226.29 ?  154 TRP G CA  1 
ATOM   14267 C C   . TRP G  4 163 ? 54.574  54.235  270.232 1.00 226.60 ?  154 TRP G C   1 
ATOM   14268 O O   . TRP G  4 163 ? 54.986  55.363  269.939 1.00 226.33 ?  154 TRP G O   1 
ATOM   14269 C CB  . TRP G  4 163 ? 53.383  54.552  272.413 1.00 228.48 ?  154 TRP G CB  1 
ATOM   14270 C CG  . TRP G  4 163 ? 52.998  53.913  273.708 1.00 229.66 ?  154 TRP G CG  1 
ATOM   14271 C CD1 . TRP G  4 163 ? 53.499  54.193  274.944 1.00 226.95 ?  154 TRP G CD1 1 
ATOM   14272 C CD2 . TRP G  4 163 ? 52.070  52.836  273.885 1.00 234.02 ?  154 TRP G CD2 1 
ATOM   14273 N NE1 . TRP G  4 163 ? 52.914  53.381  275.887 1.00 229.67 ?  154 TRP G NE1 1 
ATOM   14274 C CE2 . TRP G  4 163 ? 52.037  52.536  275.261 1.00 234.02 ?  154 TRP G CE2 1 
ATOM   14275 C CE3 . TRP G  4 163 ? 51.255  52.106  273.015 1.00 238.31 ?  154 TRP G CE3 1 
ATOM   14276 C CZ2 . TRP G  4 163 ? 51.220  51.537  275.786 1.00 238.22 ?  154 TRP G CZ2 1 
ATOM   14277 C CZ3 . TRP G  4 163 ? 50.444  51.115  273.539 1.00 242.33 ?  154 TRP G CZ3 1 
ATOM   14278 C CH2 . TRP G  4 163 ? 50.435  50.839  274.910 1.00 242.32 ?  154 TRP G CH2 1 
ATOM   14279 N N   . ASN G  4 164 ? 54.149  53.342  269.337 1.00 237.07 ?  155 ASN G N   1 
ATOM   14280 C CA  . ASN G  4 164 ? 54.178  53.570  267.893 1.00 238.46 ?  155 ASN G CA  1 
ATOM   14281 C C   . ASN G  4 164 ? 55.545  54.079  267.432 1.00 233.35 ?  155 ASN G C   1 
ATOM   14282 O O   . ASN G  4 164 ? 55.650  55.013  266.633 1.00 234.04 ?  155 ASN G O   1 
ATOM   14283 C CB  . ASN G  4 164 ? 53.054  54.520  267.473 1.00 243.63 ?  155 ASN G CB  1 
ATOM   14284 C CG  . ASN G  4 164 ? 51.671  53.925  267.706 1.00 249.50 ?  155 ASN G CG  1 
ATOM   14285 O OD1 . ASN G  4 164 ? 51.530  52.729  267.970 1.00 249.93 ?  155 ASN G OD1 1 
ATOM   14286 N ND2 . ASN G  4 164 ? 50.644  54.762  267.612 1.00 254.40 ?  155 ASN G ND2 1 
ATOM   14287 N N   . SER G  4 165 ? 56.604  53.450  267.951 1.00 237.14 ?  156 SER G N   1 
ATOM   14288 C CA  . SER G  4 165 ? 57.989  53.744  267.571 1.00 232.35 ?  156 SER G CA  1 
ATOM   14289 C C   . SER G  4 165 ? 58.380  55.198  267.844 1.00 230.23 ?  156 SER G C   1 
ATOM   14290 O O   . SER G  4 165 ? 59.253  55.755  267.174 1.00 229.16 ?  156 SER G O   1 
ATOM   14291 C CB  . SER G  4 165 ? 58.248  53.376  266.105 1.00 233.61 ?  156 SER G CB  1 
ATOM   14292 O OG  . SER G  4 165 ? 58.120  51.977  265.897 1.00 236.25 ?  156 SER G OG  1 
ATOM   14293 N N   . GLY G  4 166 ? 57.763  55.827  268.842 1.00 227.47 ?  157 GLY G N   1 
ATOM   14294 C CA  . GLY G  4 166 ? 58.117  57.174  269.233 1.00 225.88 ?  157 GLY G CA  1 
ATOM   14295 C C   . GLY G  4 166 ? 57.179  58.256  268.745 1.00 230.25 ?  157 GLY G C   1 
ATOM   14296 O O   . GLY G  4 166 ? 57.340  59.416  269.144 1.00 229.49 ?  157 GLY G O   1 
ATOM   14297 N N   . ALA G  4 167 ? 56.202  57.919  267.904 1.00 227.75 ?  158 ALA G N   1 
ATOM   14298 C CA  . ALA G  4 167 ? 55.272  58.926  267.413 1.00 232.67 ?  158 ALA G CA  1 
ATOM   14299 C C   . ALA G  4 167 ? 54.194  59.268  268.431 1.00 236.20 ?  158 ALA G C   1 
ATOM   14300 O O   . ALA G  4 167 ? 53.527  60.298  268.284 1.00 240.22 ?  158 ALA G O   1 
ATOM   14301 C CB  . ALA G  4 167 ? 54.622  58.457  266.111 1.00 236.94 ?  158 ALA G CB  1 
ATOM   14302 N N   . LEU G  4 168 ? 54.005  58.427  269.447 1.00 233.77 ?  159 LEU G N   1 
ATOM   14303 C CA  . LEU G  4 168 ? 53.043  58.656  270.519 1.00 237.07 ?  159 LEU G CA  1 
ATOM   14304 C C   . LEU G  4 168 ? 53.793  58.762  271.837 1.00 232.68 ?  159 LEU G C   1 
ATOM   14305 O O   . LEU G  4 168 ? 54.406  57.787  272.284 1.00 229.39 ?  159 LEU G O   1 
ATOM   14306 C CB  . LEU G  4 168 ? 52.009  57.532  270.584 1.00 241.33 ?  159 LEU G CB  1 
ATOM   14307 C CG  . LEU G  4 168 ? 51.023  57.630  271.750 1.00 245.29 ?  159 LEU G CG  1 
ATOM   14308 C CD1 . LEU G  4 168 ? 50.167  58.879  271.630 1.00 250.30 ?  159 LEU G CD1 1 
ATOM   14309 C CD2 . LEU G  4 168 ? 50.158  56.383  271.825 1.00 248.99 ?  159 LEU G CD2 1 
ATOM   14310 N N   . THR G  4 169 ? 53.749  59.935  272.444 1.00 241.38 ?  160 THR G N   1 
ATOM   14311 C CA  . THR G  4 169 ? 54.421  60.209  273.710 1.00 237.64 ?  160 THR G CA  1 
ATOM   14312 C C   . THR G  4 169 ? 53.514  60.888  274.723 1.00 241.66 ?  160 THR G C   1 
ATOM   14313 O O   . THR G  4 169 ? 53.573  60.558  275.910 1.00 240.71 ?  160 THR G O   1 
ATOM   14314 C CB  . THR G  4 169 ? 55.672  61.079  273.475 1.00 232.80 ?  160 THR G CB  1 
ATOM   14315 O OG1 . THR G  4 169 ? 55.303  62.271  272.769 1.00 235.77 ?  160 THR G OG1 1 
ATOM   14316 C CG2 . THR G  4 169 ? 56.715  60.319  272.669 1.00 228.50 ?  160 THR G CG2 1 
ATOM   14317 N N   . SER G  4 170 ? 52.690  61.839  274.287 1.00 232.68 ?  161 SER G N   1 
ATOM   14318 C CA  . SER G  4 170 ? 51.803  62.551  275.198 1.00 237.40 ?  161 SER G CA  1 
ATOM   14319 C C   . SER G  4 170 ? 50.825  61.600  275.879 1.00 241.44 ?  161 SER G C   1 
ATOM   14320 O O   . SER G  4 170 ? 50.243  60.715  275.244 1.00 244.00 ?  161 SER G O   1 
ATOM   14321 C CB  . SER G  4 170 ? 51.041  63.642  274.445 1.00 242.61 ?  161 SER G CB  1 
ATOM   14322 O OG  . SER G  4 170 ? 51.935  64.570  273.856 1.00 239.35 ?  161 SER G OG  1 
ATOM   14323 N N   . GLY G  4 171 ? 50.654  61.786  277.186 1.00 234.55 ?  162 GLY G N   1 
ATOM   14324 C CA  . GLY G  4 171 ? 49.741  60.976  277.962 1.00 238.86 ?  162 GLY G CA  1 
ATOM   14325 C C   . GLY G  4 171 ? 50.254  59.601  278.318 1.00 235.34 ?  162 GLY G C   1 
ATOM   14326 O O   . GLY G  4 171 ? 49.509  58.817  278.919 1.00 238.87 ?  162 GLY G O   1 
ATOM   14327 N N   . VAL G  4 172 ? 51.498  59.288  277.983 1.00 241.96 ?  163 VAL G N   1 
ATOM   14328 C CA  . VAL G  4 172 ? 52.070  57.987  278.302 1.00 238.63 ?  163 VAL G CA  1 
ATOM   14329 C C   . VAL G  4 172 ? 52.630  58.020  279.716 1.00 236.16 ?  163 VAL G C   1 
ATOM   14330 O O   . VAL G  4 172 ? 53.375  58.938  280.082 1.00 232.83 ?  163 VAL G O   1 
ATOM   14331 C CB  . VAL G  4 172 ? 53.158  57.613  277.286 1.00 233.17 ?  163 VAL G CB  1 
ATOM   14332 C CG1 . VAL G  4 172 ? 53.849  56.338  277.711 1.00 229.74 ?  163 VAL G CG1 1 
ATOM   14333 C CG2 . VAL G  4 172 ? 52.559  57.464  275.903 1.00 235.96 ?  163 VAL G CG2 1 
ATOM   14334 N N   . HIS G  4 173 ? 52.270  57.020  280.519 1.00 232.05 ?  164 HIS G N   1 
ATOM   14335 C CA  . HIS G  4 173 ? 52.895  56.778  281.815 1.00 229.50 ?  164 HIS G CA  1 
ATOM   14336 C C   . HIS G  4 173 ? 53.486  55.375  281.794 1.00 226.75 ?  164 HIS G C   1 
ATOM   14337 O O   . HIS G  4 173 ? 52.745  54.386  281.766 1.00 230.42 ?  164 HIS G O   1 
ATOM   14338 C CB  . HIS G  4 173 ? 51.890  56.931  282.958 1.00 235.18 ?  164 HIS G CB  1 
ATOM   14339 C CG  . HIS G  4 173 ? 51.388  58.330  283.143 1.00 238.09 ?  164 HIS G CG  1 
ATOM   14340 N ND1 . HIS G  4 173 ? 52.206  59.374  283.517 1.00 234.54 ?  164 HIS G ND1 1 
ATOM   14341 C CD2 . HIS G  4 173 ? 50.148  58.856  283.001 1.00 244.62 ?  164 HIS G CD2 1 
ATOM   14342 C CE1 . HIS G  4 173 ? 51.492  60.482  283.600 1.00 238.76 ?  164 HIS G CE1 1 
ATOM   14343 N NE2 . HIS G  4 173 ? 50.240  60.195  283.291 1.00 244.98 ?  164 HIS G NE2 1 
ATOM   14344 N N   . THR G  4 174 ? 54.813  55.289  281.800 1.00 242.11 ?  165 THR G N   1 
ATOM   14345 C CA  . THR G  4 174 ? 55.518  54.019  281.924 1.00 239.61 ?  165 THR G CA  1 
ATOM   14346 C C   . THR G  4 174 ? 55.972  53.898  283.373 1.00 238.63 ?  165 THR G C   1 
ATOM   14347 O O   . THR G  4 174 ? 56.858  54.636  283.819 1.00 234.86 ?  165 THR G O   1 
ATOM   14348 C CB  . THR G  4 174 ? 56.699  53.937  280.959 1.00 234.18 ?  165 THR G CB  1 
ATOM   14349 O OG1 . THR G  4 174 ? 56.220  53.986  279.609 1.00 235.67 ?  165 THR G OG1 1 
ATOM   14350 C CG2 . THR G  4 174 ? 57.457  52.635  281.164 1.00 232.04 ?  165 THR G CG2 1 
ATOM   14351 N N   . PHE G  4 175 ? 55.361  52.971  284.103 1.00 227.05 ?  166 PHE G N   1 
ATOM   14352 C CA  . PHE G  4 175 ? 55.559  52.902  285.539 1.00 227.58 ?  166 PHE G CA  1 
ATOM   14353 C C   . PHE G  4 175 ? 56.943  52.353  285.878 1.00 222.51 ?  166 PHE G C   1 
ATOM   14354 O O   . PHE G  4 175 ? 57.524  51.585  285.107 1.00 220.09 ?  166 PHE G O   1 
ATOM   14355 C CB  . PHE G  4 175 ? 54.478  52.040  286.183 1.00 233.72 ?  166 PHE G CB  1 
ATOM   14356 C CG  . PHE G  4 175 ? 53.143  52.719  286.267 1.00 239.51 ?  166 PHE G CG  1 
ATOM   14357 C CD1 . PHE G  4 175 ? 52.845  53.556  287.329 1.00 241.80 ?  166 PHE G CD1 1 
ATOM   14358 C CD2 . PHE G  4 175 ? 52.190  52.531  285.280 1.00 243.13 ?  166 PHE G CD2 1 
ATOM   14359 C CE1 . PHE G  4 175 ? 51.620  54.189  287.408 1.00 247.69 ?  166 PHE G CE1 1 
ATOM   14360 C CE2 . PHE G  4 175 ? 50.961  53.161  285.354 1.00 248.97 ?  166 PHE G CE2 1 
ATOM   14361 C CZ  . PHE G  4 175 ? 50.675  53.990  286.421 1.00 251.34 ?  166 PHE G CZ  1 
ATOM   14362 N N   . PRO G  4 176 ? 57.498  52.757  287.021 1.00 221.64 ?  167 PRO G N   1 
ATOM   14363 C CA  . PRO G  4 176 ? 58.769  52.180  287.468 1.00 217.71 ?  167 PRO G CA  1 
ATOM   14364 C C   . PRO G  4 176 ? 58.668  50.667  287.567 1.00 219.84 ?  167 PRO G C   1 
ATOM   14365 O O   . PRO G  4 176 ? 57.629  50.120  287.946 1.00 225.11 ?  167 PRO G O   1 
ATOM   14366 C CB  . PRO G  4 176 ? 58.987  52.823  288.843 1.00 218.24 ?  167 PRO G CB  1 
ATOM   14367 C CG  . PRO G  4 176 ? 58.191  54.086  288.806 1.00 220.27 ?  167 PRO G CG  1 
ATOM   14368 C CD  . PRO G  4 176 ? 57.005  53.802  287.934 1.00 224.09 ?  167 PRO G CD  1 
ATOM   14369 N N   . ALA G  4 177 ? 59.757  49.992  287.202 1.00 218.96 ?  168 ALA G N   1 
ATOM   14370 C CA  . ALA G  4 177 ? 59.781  48.541  287.286 1.00 221.15 ?  168 ALA G CA  1 
ATOM   14371 C C   . ALA G  4 177 ? 59.592  48.119  288.730 1.00 224.21 ?  168 ALA G C   1 
ATOM   14372 O O   . ALA G  4 177 ? 60.105  48.751  289.656 1.00 222.40 ?  168 ALA G O   1 
ATOM   14373 C CB  . ALA G  4 177 ? 61.104  47.985  286.766 1.00 216.88 ?  168 ALA G CB  1 
ATOM   14374 N N   . VAL G  4 178 ? 58.878  47.022  288.915 1.00 210.55 ?  169 VAL G N   1 
ATOM   14375 C CA  . VAL G  4 178 ? 58.612  46.473  290.231 1.00 213.89 ?  169 VAL G CA  1 
ATOM   14376 C C   . VAL G  4 178 ? 59.315  45.122  290.319 1.00 213.72 ?  169 VAL G C   1 
ATOM   14377 O O   . VAL G  4 178 ? 59.196  44.297  289.407 1.00 214.09 ?  169 VAL G O   1 
ATOM   14378 C CB  . VAL G  4 178 ? 57.091  46.354  290.466 1.00 220.77 ?  169 VAL G CB  1 
ATOM   14379 C CG1 . VAL G  4 178 ? 56.811  45.267  291.465 1.00 224.29 ?  169 VAL G CG1 1 
ATOM   14380 C CG2 . VAL G  4 178 ? 56.435  47.736  290.893 1.00 221.57 ?  169 VAL G CG2 1 
ATOM   14381 N N   . LEU G  4 179 ? 60.023  44.876  291.421 1.00 221.52 ?  170 LEU G N   1 
ATOM   14382 C CA  . LEU G  4 179 ? 60.660  43.578  291.621 1.00 222.53 ?  170 LEU G CA  1 
ATOM   14383 C C   . LEU G  4 179 ? 59.627  42.649  292.241 1.00 229.41 ?  170 LEU G C   1 
ATOM   14384 O O   . LEU G  4 179 ? 59.242  42.827  293.400 1.00 232.70 ?  170 LEU G O   1 
ATOM   14385 C CB  . LEU G  4 179 ? 61.899  43.689  292.504 1.00 219.79 ?  170 LEU G CB  1 
ATOM   14386 C CG  . LEU G  4 179 ? 62.645  42.364  292.665 1.00 220.79 ?  170 LEU G CG  1 
ATOM   14387 C CD1 . LEU G  4 179 ? 63.070  41.833  291.300 1.00 218.27 ?  170 LEU G CD1 1 
ATOM   14388 C CD2 . LEU G  4 179 ? 63.843  42.550  293.577 1.00 218.43 ?  170 LEU G CD2 1 
ATOM   14389 N N   . GLN G  4 180 ? 59.192  41.656  291.473 1.00 230.20 ?  171 GLN G N   1 
ATOM   14390 C CA  . GLN G  4 180 ? 58.183  40.715  291.930 1.00 237.07 ?  171 GLN G CA  1 
ATOM   14391 C C   . GLN G  4 180 ? 58.787  39.713  292.910 1.00 239.47 ?  171 GLN G C   1 
ATOM   14392 O O   . GLN G  4 180 ? 60.007  39.579  293.033 1.00 235.67 ?  171 GLN G O   1 
ATOM   14393 C CB  . GLN G  4 180 ? 57.564  39.982  290.743 1.00 238.85 ?  171 GLN G CB  1 
ATOM   14394 C CG  . GLN G  4 180 ? 56.875  40.899  289.759 1.00 237.49 ?  171 GLN G CG  1 
ATOM   14395 C CD  . GLN G  4 180 ? 56.518  40.197  288.470 1.00 238.43 ?  171 GLN G CD  1 
ATOM   14396 O OE1 . GLN G  4 180 ? 55.341  40.006  288.158 1.00 243.10 ?  171 GLN G OE1 1 
ATOM   14397 N NE2 . GLN G  4 180 ? 57.532  39.804  287.711 1.00 234.45 ?  171 GLN G NE2 1 
ATOM   14398 N N   . SER G  4 181 ? 57.906  39.008  293.625 1.00 241.81 ?  172 SER G N   1 
ATOM   14399 C CA  . SER G  4 181 ? 58.346  37.981  294.564 1.00 245.25 ?  172 SER G CA  1 
ATOM   14400 C C   . SER G  4 181 ? 59.122  36.858  293.883 1.00 244.20 ?  172 SER G C   1 
ATOM   14401 O O   . SER G  4 181 ? 59.875  36.142  294.554 1.00 245.61 ?  172 SER G O   1 
ATOM   14402 C CB  . SER G  4 181 ? 57.137  37.409  295.308 1.00 253.35 ?  172 SER G CB  1 
ATOM   14403 O OG  . SER G  4 181 ? 56.216  36.822  294.405 1.00 259.47 ?  172 SER G OG  1 
ATOM   14404 N N   . SER G  4 182 ? 58.958  36.685  292.570 1.00 246.06 ?  173 SER G N   1 
ATOM   14405 C CA  . SER G  4 182 ? 59.668  35.640  291.841 1.00 245.24 ?  173 SER G CA  1 
ATOM   14406 C C   . SER G  4 182 ? 61.128  35.982  291.568 1.00 238.88 ?  173 SER G C   1 
ATOM   14407 O O   . SER G  4 182 ? 61.909  35.079  291.247 1.00 238.78 ?  173 SER G O   1 
ATOM   14408 C CB  . SER G  4 182 ? 58.963  35.357  290.514 1.00 245.89 ?  173 SER G CB  1 
ATOM   14409 O OG  . SER G  4 182 ? 59.019  36.488  289.663 1.00 240.76 ?  173 SER G OG  1 
ATOM   14410 N N   . GLY G  4 183 ? 61.510  37.252  291.675 1.00 248.67 ?  174 GLY G N   1 
ATOM   14411 C CA  . GLY G  4 183 ? 62.843  37.688  291.317 1.00 242.66 ?  174 GLY G CA  1 
ATOM   14412 C C   . GLY G  4 183 ? 62.956  38.283  289.932 1.00 238.16 ?  174 GLY G C   1 
ATOM   14413 O O   . GLY G  4 183 ? 64.058  38.680  289.533 1.00 233.19 ?  174 GLY G O   1 
ATOM   14414 N N   . LEU G  4 184 ? 61.857  38.349  289.187 1.00 227.75 ?  175 LEU G N   1 
ATOM   14415 C CA  . LEU G  4 184 ? 61.812  38.998  287.889 1.00 224.04 ?  175 LEU G CA  1 
ATOM   14416 C C   . LEU G  4 184 ? 61.078  40.328  288.006 1.00 222.97 ?  175 LEU G C   1 
ATOM   14417 O O   . LEU G  4 184 ? 60.174  40.488  288.832 1.00 226.79 ?  175 LEU G O   1 
ATOM   14418 C CB  . LEU G  4 184 ? 61.122  38.096  286.861 1.00 227.21 ?  175 LEU G CB  1 
ATOM   14419 C CG  . LEU G  4 184 ? 61.679  36.671  286.781 1.00 229.53 ?  175 LEU G CG  1 
ATOM   14420 C CD1 . LEU G  4 184 ? 60.956  35.861  285.720 1.00 232.74 ?  175 LEU G CD1 1 
ATOM   14421 C CD2 . LEU G  4 184 ? 63.175  36.690  286.510 1.00 224.88 ?  175 LEU G CD2 1 
ATOM   14422 N N   . TYR G  4 185 ? 61.476  41.284  287.173 1.00 231.38 ?  176 TYR G N   1 
ATOM   14423 C CA  . TYR G  4 185 ? 60.864  42.603  287.199 1.00 230.31 ?  176 TYR G CA  1 
ATOM   14424 C C   . TYR G  4 185 ? 59.592  42.636  286.357 1.00 233.42 ?  176 TYR G C   1 
ATOM   14425 O O   . TYR G  4 185 ? 59.379  41.809  285.468 1.00 234.94 ?  176 TYR G O   1 
ATOM   14426 C CB  . TYR G  4 185 ? 61.843  43.663  286.700 1.00 224.23 ?  176 TYR G CB  1 
ATOM   14427 C CG  . TYR G  4 185 ? 63.075  43.808  287.555 1.00 221.23 ?  176 TYR G CG  1 
ATOM   14428 C CD1 . TYR G  4 185 ? 63.088  44.671  288.640 1.00 220.86 ?  176 TYR G CD1 1 
ATOM   14429 C CD2 . TYR G  4 185 ? 64.228  43.084  287.277 1.00 219.06 ?  176 TYR G CD2 1 
ATOM   14430 C CE1 . TYR G  4 185 ? 64.211  44.813  289.425 1.00 218.38 ?  176 TYR G CE1 1 
ATOM   14431 C CE2 . TYR G  4 185 ? 65.357  43.219  288.057 1.00 216.68 ?  176 TYR G CE2 1 
ATOM   14432 C CZ  . TYR G  4 185 ? 65.343  44.084  289.129 1.00 216.28 ?  176 TYR G CZ  1 
ATOM   14433 O OH  . TYR G  4 185 ? 66.466  44.222  289.911 1.00 214.18 ?  176 TYR G OH  1 
ATOM   14434 N N   . SER G  4 186 ? 58.739  43.613  286.660 1.00 218.46 ?  177 SER G N   1 
ATOM   14435 C CA  . SER G  4 186 ? 57.538  43.856  285.877 1.00 221.42 ?  177 SER G CA  1 
ATOM   14436 C C   . SER G  4 186 ? 57.178  45.331  285.961 1.00 220.23 ?  177 SER G C   1 
ATOM   14437 O O   . SER G  4 186 ? 57.405  45.986  286.982 1.00 219.61 ?  177 SER G O   1 
ATOM   14438 C CB  . SER G  4 186 ? 56.361  42.998  286.354 1.00 228.22 ?  177 SER G CB  1 
ATOM   14439 O OG  . SER G  4 186 ? 55.231  43.168  285.515 1.00 231.35 ?  177 SER G OG  1 
ATOM   14440 N N   . LEU G  4 187 ? 56.612  45.845  284.872 1.00 223.62 ?  178 LEU G N   1 
ATOM   14441 C CA  . LEU G  4 187 ? 56.046  47.184  284.852 1.00 223.76 ?  178 LEU G CA  1 
ATOM   14442 C C   . LEU G  4 187 ? 54.901  47.200  283.853 1.00 224.62 ?  178 LEU G C   1 
ATOM   14443 O O   . LEU G  4 187 ? 54.746  46.288  283.036 1.00 224.87 ?  178 LEU G O   1 
ATOM   14444 C CB  . LEU G  4 187 ? 57.106  48.246  284.513 1.00 222.66 ?  178 LEU G CB  1 
ATOM   14445 C CG  . LEU G  4 187 ? 57.820  48.291  283.154 1.00 222.01 ?  178 LEU G CG  1 
ATOM   14446 C CD1 . LEU G  4 187 ? 56.955  48.879  282.037 1.00 222.55 ?  178 LEU G CD1 1 
ATOM   14447 C CD2 . LEU G  4 187 ? 59.119  49.070  283.280 1.00 220.86 ?  178 LEU G CD2 1 
ATOM   14448 N N   . SER G  4 188 ? 54.097  48.252  283.927 1.00 236.65 ?  179 SER G N   1 
ATOM   14449 C CA  . SER G  4 188 ? 53.098  48.538  282.914 1.00 239.77 ?  179 SER G CA  1 
ATOM   14450 C C   . SER G  4 188 ? 53.417  49.875  282.266 1.00 236.50 ?  179 SER G C   1 
ATOM   14451 O O   . SER G  4 188 ? 53.946  50.786  282.910 1.00 233.63 ?  179 SER G O   1 
ATOM   14452 C CB  . SER G  4 188 ? 51.689  48.571  283.513 1.00 246.83 ?  179 SER G CB  1 
ATOM   14453 O OG  . SER G  4 188 ? 51.253  47.267  283.851 1.00 250.82 ?  179 SER G OG  1 
ATOM   14454 N N   . SER G  4 189 ? 53.103  49.979  280.981 1.00 234.49 ?  180 SER G N   1 
ATOM   14455 C CA  . SER G  4 189 ? 53.135  51.244  280.262 1.00 233.03 ?  180 SER G CA  1 
ATOM   14456 C C   . SER G  4 189 ? 51.738  51.507  279.735 1.00 239.10 ?  180 SER G C   1 
ATOM   14457 O O   . SER G  4 189 ? 51.192  50.690  278.988 1.00 241.86 ?  180 SER G O   1 
ATOM   14458 C CB  . SER G  4 189 ? 54.145  51.213  279.117 1.00 228.05 ?  180 SER G CB  1 
ATOM   14459 O OG  . SER G  4 189 ? 54.150  52.449  278.425 1.00 227.21 ?  180 SER G OG  1 
ATOM   14460 N N   . VAL G  4 190 ? 51.166  52.645  280.116 1.00 235.94 ?  181 VAL G N   1 
ATOM   14461 C CA  . VAL G  4 190 ? 49.817  53.000  279.713 1.00 242.30 ?  181 VAL G CA  1 
ATOM   14462 C C   . VAL G  4 190 ? 49.862  54.319  278.960 1.00 241.65 ?  181 VAL G C   1 
ATOM   14463 O O   . VAL G  4 190 ? 50.817  55.094  279.053 1.00 236.72 ?  181 VAL G O   1 
ATOM   14464 C CB  . VAL G  4 190 ? 48.850  53.096  280.914 1.00 248.03 ?  181 VAL G CB  1 
ATOM   14465 C CG1 . VAL G  4 190 ? 48.782  51.770  281.658 1.00 249.62 ?  181 VAL G CG1 1 
ATOM   14466 C CG2 . VAL G  4 190 ? 49.266  54.224  281.851 1.00 246.26 ?  181 VAL G CG2 1 
ATOM   14467 N N   . VAL G  4 191 ? 48.804  54.563  278.199 1.00 246.65 ?  182 VAL G N   1 
ATOM   14468 C CA  . VAL G  4 191 ? 48.625  55.826  277.500 1.00 247.46 ?  182 VAL G CA  1 
ATOM   14469 C C   . VAL G  4 191 ? 47.137  56.122  277.475 1.00 255.62 ?  182 VAL G C   1 
ATOM   14470 O O   . VAL G  4 191 ? 46.313  55.216  277.315 1.00 260.07 ?  182 VAL G O   1 
ATOM   14471 C CB  . VAL G  4 191 ? 49.221  55.781  276.076 1.00 244.28 ?  182 VAL G CB  1 
ATOM   14472 C CG1 . VAL G  4 191 ? 48.587  54.660  275.272 1.00 247.59 ?  182 VAL G CG1 1 
ATOM   14473 C CG2 . VAL G  4 191 ? 49.026  57.117  275.375 1.00 245.39 ?  182 VAL G CG2 1 
ATOM   14474 N N   . THR G  4 192 ? 46.791  57.389  277.650 1.00 253.17 ?  183 THR G N   1 
ATOM   14475 C CA  . THR G  4 192 ? 45.413  57.826  277.515 1.00 261.24 ?  183 THR G CA  1 
ATOM   14476 C C   . THR G  4 192 ? 45.258  58.506  276.166 1.00 262.19 ?  183 THR G C   1 
ATOM   14477 O O   . THR G  4 192 ? 46.082  59.343  275.782 1.00 257.93 ?  183 THR G O   1 
ATOM   14478 C CB  . THR G  4 192 ? 45.004  58.769  278.647 1.00 264.58 ?  183 THR G CB  1 
ATOM   14479 O OG1 . THR G  4 192 ? 45.985  59.804  278.797 1.00 259.48 ?  183 THR G OG1 1 
ATOM   14480 C CG2 . THR G  4 192 ? 44.860  57.999  279.953 1.00 265.25 ?  183 THR G CG2 1 
ATOM   14481 N N   . VAL G  4 193 ? 44.195  58.142  275.457 1.00 269.17 ?  184 VAL G N   1 
ATOM   14482 C CA  . VAL G  4 193 ? 43.963  58.569  274.080 1.00 270.91 ?  184 VAL G CA  1 
ATOM   14483 C C   . VAL G  4 193 ? 42.479  58.851  273.917 1.00 280.25 ?  184 VAL G C   1 
ATOM   14484 O O   . VAL G  4 193 ? 41.656  58.394  274.722 1.00 284.95 ?  184 VAL G O   1 
ATOM   14485 C CB  . VAL G  4 193 ? 44.412  57.499  273.063 1.00 267.77 ?  184 VAL G CB  1 
ATOM   14486 C CG1 . VAL G  4 193 ? 45.909  57.237  273.173 1.00 258.91 ?  184 VAL G CG1 1 
ATOM   14487 C CG2 . VAL G  4 193 ? 43.622  56.217  273.264 1.00 271.96 ?  184 VAL G CG2 1 
ATOM   14488 N N   . PRO G  4 194 ? 42.106  59.620  272.894 1.00 277.31 ?  185 PRO G N   1 
ATOM   14489 C CA  . PRO G  4 194 ? 40.678  59.857  272.662 1.00 287.36 ?  185 PRO G CA  1 
ATOM   14490 C C   . PRO G  4 194 ? 39.952  58.549  272.395 1.00 290.30 ?  185 PRO G C   1 
ATOM   14491 O O   . PRO G  4 194 ? 40.426  57.689  271.651 1.00 287.35 ?  185 PRO G O   1 
ATOM   14492 C CB  . PRO G  4 194 ? 40.661  60.782  271.439 1.00 289.60 ?  185 PRO G CB  1 
ATOM   14493 C CG  . PRO G  4 194 ? 42.007  61.417  271.422 1.00 282.44 ?  185 PRO G CG  1 
ATOM   14494 C CD  . PRO G  4 194 ? 42.953  60.402  271.974 1.00 273.96 ?  185 PRO G CD  1 
ATOM   14495 N N   . SER G  4 195 ? 38.793  58.399  273.039 1.00 290.74 ?  186 SER G N   1 
ATOM   14496 C CA  . SER G  4 195 ? 37.988  57.201  272.831 1.00 295.56 ?  186 SER G CA  1 
ATOM   14497 C C   . SER G  4 195 ? 37.554  57.070  271.381 1.00 298.62 ?  186 SER G C   1 
ATOM   14498 O O   . SER G  4 195 ? 37.300  55.956  270.909 1.00 300.67 ?  186 SER G O   1 
ATOM   14499 C CB  . SER G  4 195 ? 36.773  57.213  273.755 1.00 307.26 ?  186 SER G CB  1 
ATOM   14500 O OG  . SER G  4 195 ? 37.169  57.175  275.116 1.00 306.39 ?  186 SER G OG  1 
ATOM   14501 N N   . SER G  4 196 ? 37.422  58.194  270.673 1.00 289.54 ?  187 SER G N   1 
ATOM   14502 C CA  . SER G  4 196 ? 37.077  58.142  269.258 1.00 292.52 ?  187 SER G CA  1 
ATOM   14503 C C   . SER G  4 196 ? 38.150  57.434  268.440 1.00 284.96 ?  187 SER G C   1 
ATOM   14504 O O   . SER G  4 196 ? 37.838  56.711  267.486 1.00 286.85 ?  187 SER G O   1 
ATOM   14505 C CB  . SER G  4 196 ? 36.885  59.557  268.716 1.00 295.10 ?  187 SER G CB  1 
ATOM   14506 O OG  . SER G  4 196 ? 38.098  60.292  268.810 1.00 287.12 ?  187 SER G OG  1 
ATOM   14507 N N   . SER G  4 197 ? 39.418  57.579  268.835 1.00 293.85 ?  188 SER G N   1 
ATOM   14508 C CA  . SER G  4 197 ? 40.522  57.099  268.010 1.00 286.08 ?  188 SER G CA  1 
ATOM   14509 C C   . SER G  4 197 ? 40.708  55.594  268.089 1.00 284.46 ?  188 SER G C   1 
ATOM   14510 O O   . SER G  4 197 ? 41.546  55.052  267.361 1.00 279.69 ?  188 SER G O   1 
ATOM   14511 C CB  . SER G  4 197 ? 41.819  57.817  268.391 1.00 278.31 ?  188 SER G CB  1 
ATOM   14512 O OG  . SER G  4 197 ? 42.339  57.330  269.615 1.00 275.27 ?  188 SER G OG  1 
ATOM   14513 N N   . LEU G  4 198 ? 39.959  54.914  268.953 1.00 275.73 ?  189 LEU G N   1 
ATOM   14514 C CA  . LEU G  4 198 ? 40.054  53.466  269.040 1.00 274.37 ?  189 LEU G CA  1 
ATOM   14515 C C   . LEU G  4 198 ? 39.580  52.852  267.728 1.00 278.12 ?  189 LEU G C   1 
ATOM   14516 O O   . LEU G  4 198 ? 38.471  53.130  267.262 1.00 285.76 ?  189 LEU G O   1 
ATOM   14517 C CB  . LEU G  4 198 ? 39.206  52.958  270.205 1.00 278.84 ?  189 LEU G CB  1 
ATOM   14518 C CG  . LEU G  4 198 ? 39.573  53.435  271.614 1.00 276.20 ?  189 LEU G CG  1 
ATOM   14519 C CD1 . LEU G  4 198 ? 38.590  52.887  272.637 1.00 282.22 ?  189 LEU G CD1 1 
ATOM   14520 C CD2 . LEU G  4 198 ? 40.994  53.042  271.984 1.00 267.08 ?  189 LEU G CD2 1 
ATOM   14521 N N   . GLY G  4 199 ? 40.425  52.015  267.130 1.00 278.69 ?  190 GLY G N   1 
ATOM   14522 C CA  . GLY G  4 199 ? 40.129  51.384  265.865 1.00 281.66 ?  190 GLY G CA  1 
ATOM   14523 C C   . GLY G  4 199 ? 40.554  52.174  264.641 1.00 281.35 ?  190 GLY G C   1 
ATOM   14524 O O   . GLY G  4 199 ? 40.854  51.573  263.605 1.00 290.50 ?  190 GLY G O   1 
ATOM   14525 N N   . THR G  4 200 ? 40.590  53.505  264.733 1.00 286.60 ?  191 THR G N   1 
ATOM   14526 C CA  . THR G  4 200 ? 41.040  54.340  263.624 1.00 285.40 ?  191 THR G CA  1 
ATOM   14527 C C   . THR G  4 200 ? 42.554  54.523  263.623 1.00 276.69 ?  191 THR G C   1 
ATOM   14528 O O   . THR G  4 200 ? 43.183  54.517  262.558 1.00 277.86 ?  191 THR G O   1 
ATOM   14529 C CB  . THR G  4 200 ? 40.343  55.705  263.678 1.00 291.17 ?  191 THR G CB  1 
ATOM   14530 O OG1 . THR G  4 200 ? 38.939  55.531  263.452 1.00 301.09 ?  191 THR G OG1 1 
ATOM   14531 C CG2 . THR G  4 200 ? 40.904  56.650  262.619 1.00 289.99 ?  191 THR G CG2 1 
ATOM   14532 N N   . GLN G  4 201 ? 43.150  54.676  264.802 1.00 277.09 ?  192 GLN G N   1 
ATOM   14533 C CA  . GLN G  4 201 ? 44.591  54.802  264.964 1.00 268.67 ?  192 GLN G CA  1 
ATOM   14534 C C   . GLN G  4 201 ? 45.147  53.513  265.554 1.00 264.48 ?  192 GLN G C   1 
ATOM   14535 O O   . GLN G  4 201 ? 44.665  53.041  266.589 1.00 265.74 ?  192 GLN G O   1 
ATOM   14536 C CB  . GLN G  4 201 ? 44.930  55.989  265.871 1.00 266.19 ?  192 GLN G CB  1 
ATOM   14537 C CG  . GLN G  4 201 ? 46.402  56.121  266.239 1.00 257.79 ?  192 GLN G CG  1 
ATOM   14538 C CD  . GLN G  4 201 ? 47.270  56.484  265.052 1.00 254.94 ?  192 GLN G CD  1 
ATOM   14539 O OE1 . GLN G  4 201 ? 47.002  57.455  264.345 1.00 257.99 ?  192 GLN G OE1 1 
ATOM   14540 N NE2 . GLN G  4 201 ? 48.320  55.703  264.828 1.00 249.43 ?  192 GLN G NE2 1 
ATOM   14541 N N   . THR G  4 202 ? 46.157  52.950  264.898 1.00 260.86 ?  193 THR G N   1 
ATOM   14542 C CA  . THR G  4 202 ? 46.800  51.747  265.405 1.00 256.95 ?  193 THR G CA  1 
ATOM   14543 C C   . THR G  4 202 ? 47.733  52.111  266.554 1.00 250.82 ?  193 THR G C   1 
ATOM   14544 O O   . THR G  4 202 ? 48.477  53.093  266.480 1.00 246.97 ?  193 THR G O   1 
ATOM   14545 C CB  . THR G  4 202 ? 47.577  51.044  264.288 1.00 254.45 ?  193 THR G CB  1 
ATOM   14546 O OG1 . THR G  4 202 ? 46.666  50.575  263.285 1.00 260.49 ?  193 THR G OG1 1 
ATOM   14547 C CG2 . THR G  4 202 ? 48.360  49.866  264.835 1.00 250.23 ?  193 THR G CG2 1 
ATOM   14548 N N   . TYR G  4 203 ? 47.696  51.309  267.617 1.00 257.18 ?  194 TYR G N   1 
ATOM   14549 C CA  . TYR G  4 203 ? 48.534  51.519  268.792 1.00 251.79 ?  194 TYR G CA  1 
ATOM   14550 C C   . TYR G  4 203 ? 49.424  50.303  268.998 1.00 247.82 ?  194 TYR G C   1 
ATOM   14551 O O   . TYR G  4 203 ? 48.927  49.187  269.182 1.00 250.58 ?  194 TYR G O   1 
ATOM   14552 C CB  . TYR G  4 203 ? 47.685  51.790  270.037 1.00 254.96 ?  194 TYR G CB  1 
ATOM   14553 C CG  . TYR G  4 203 ? 46.966  53.118  269.997 1.00 258.61 ?  194 TYR G CG  1 
ATOM   14554 C CD1 . TYR G  4 203 ? 47.676  54.305  270.097 1.00 254.87 ?  194 TYR G CD1 1 
ATOM   14555 C CD2 . TYR G  4 203 ? 45.585  53.188  269.869 1.00 266.17 ?  194 TYR G CD2 1 
ATOM   14556 C CE1 . TYR G  4 203 ? 47.038  55.524  270.065 1.00 258.51 ?  194 TYR G CE1 1 
ATOM   14557 C CE2 . TYR G  4 203 ? 44.936  54.407  269.835 1.00 269.99 ?  194 TYR G CE2 1 
ATOM   14558 C CZ  . TYR G  4 203 ? 45.667  55.570  269.934 1.00 266.09 ?  194 TYR G CZ  1 
ATOM   14559 O OH  . TYR G  4 203 ? 45.021  56.783  269.900 1.00 270.03 ?  194 TYR G OH  1 
ATOM   14560 N N   . ILE G  4 204 ? 50.737  50.528  268.963 1.00 245.33 ?  195 ILE G N   1 
ATOM   14561 C CA  . ILE G  4 204 ? 51.744  49.485  269.110 1.00 241.21 ?  195 ILE G CA  1 
ATOM   14562 C C   . ILE G  4 204 ? 52.766  49.961  270.132 1.00 235.58 ?  195 ILE G C   1 
ATOM   14563 O O   . ILE G  4 204 ? 53.328  51.052  269.986 1.00 232.62 ?  195 ILE G O   1 
ATOM   14564 C CB  . ILE G  4 204 ? 52.433  49.168  267.768 1.00 239.59 ?  195 ILE G CB  1 
ATOM   14565 C CG1 . ILE G  4 204 ? 51.403  48.697  266.741 1.00 245.42 ?  195 ILE G CG1 1 
ATOM   14566 C CG2 . ILE G  4 204 ? 53.519  48.114  267.951 1.00 235.51 ?  195 ILE G CG2 1 
ATOM   14567 C CD1 . ILE G  4 204 ? 51.936  48.627  265.331 1.00 244.71 ?  195 ILE G CD1 1 
ATOM   14568 N N   . CYS G  4 205 ? 53.001  49.157  271.166 1.00 251.66 ?  196 CYS G N   1 
ATOM   14569 C CA  . CYS G  4 205 ? 54.059  49.425  272.132 1.00 246.28 ?  196 CYS G CA  1 
ATOM   14570 C C   . CYS G  4 205 ? 55.311  48.645  271.749 1.00 242.08 ?  196 CYS G C   1 
ATOM   14571 O O   . CYS G  4 205 ? 55.234  47.458  271.418 1.00 243.68 ?  196 CYS G O   1 
ATOM   14572 C CB  . CYS G  4 205 ? 53.611  49.074  273.556 1.00 247.54 ?  196 CYS G CB  1 
ATOM   14573 S SG  . CYS G  4 205 ? 53.499  47.309  273.946 1.00 249.72 ?  196 CYS G SG  1 
ATOM   14574 N N   . ASN G  4 206 ? 56.457  49.317  271.784 1.00 243.70 ?  197 ASN G N   1 
ATOM   14575 C CA  . ASN G  4 206 ? 57.743  48.724  271.434 1.00 239.74 ?  197 ASN G CA  1 
ATOM   14576 C C   . ASN G  4 206 ? 58.573  48.586  272.701 1.00 236.16 ?  197 ASN G C   1 
ATOM   14577 O O   . ASN G  4 206 ? 58.907  49.592  273.335 1.00 233.56 ?  197 ASN G O   1 
ATOM   14578 C CB  . ASN G  4 206 ? 58.475  49.572  270.398 1.00 237.19 ?  197 ASN G CB  1 
ATOM   14579 C CG  . ASN G  4 206 ? 57.538  50.178  269.388 1.00 240.89 ?  197 ASN G CG  1 
ATOM   14580 O OD1 . ASN G  4 206 ? 57.255  51.372  269.429 1.00 240.99 ?  197 ASN G OD1 1 
ATOM   14581 N ND2 . ASN G  4 206 ? 57.058  49.358  268.462 1.00 244.16 ?  197 ASN G ND2 1 
ATOM   14582 N N   . VAL G  4 207 ? 58.904  47.349  273.063 1.00 251.45 ?  198 VAL G N   1 
ATOM   14583 C CA  . VAL G  4 207 ? 59.579  47.041  274.321 1.00 248.90 ?  198 VAL G CA  1 
ATOM   14584 C C   . VAL G  4 207 ? 60.918  46.398  273.977 1.00 246.22 ?  198 VAL G C   1 
ATOM   14585 O O   . VAL G  4 207 ? 60.959  45.283  273.440 1.00 249.60 ?  198 VAL G O   1 
ATOM   14586 C CB  . VAL G  4 207 ? 58.737  46.121  275.218 1.00 253.48 ?  198 VAL G CB  1 
ATOM   14587 C CG1 . VAL G  4 207 ? 59.445  45.862  276.543 1.00 252.45 ?  198 VAL G CG1 1 
ATOM   14588 C CG2 . VAL G  4 207 ? 57.350  46.711  275.454 1.00 259.98 ?  198 VAL G CG2 1 
ATOM   14589 N N   . ASN G  4 208 ? 62.010  47.095  274.285 1.00 248.69 ?  199 ASN G N   1 
ATOM   14590 C CA  . ASN G  4 208 ? 63.359  46.613  274.023 1.00 246.28 ?  199 ASN G CA  1 
ATOM   14591 C C   . ASN G  4 208 ? 64.060  46.294  275.338 1.00 244.05 ?  199 ASN G C   1 
ATOM   14592 O O   . ASN G  4 208 ? 63.943  47.041  276.314 1.00 243.61 ?  199 ASN G O   1 
ATOM   14593 C CB  . ASN G  4 208 ? 64.171  47.648  273.235 1.00 245.49 ?  199 ASN G CB  1 
ATOM   14594 C CG  . ASN G  4 208 ? 63.552  47.976  271.888 1.00 251.23 ?  199 ASN G CG  1 
ATOM   14595 O OD1 . ASN G  4 208 ? 62.634  47.294  271.432 1.00 255.40 ?  199 ASN G OD1 1 
ATOM   14596 N ND2 . ASN G  4 208 ? 64.051  49.027  271.244 1.00 252.17 ?  199 ASN G ND2 1 
ATOM   14597 N N   . HIS G  4 209 ? 64.789  45.180  275.354 1.00 237.79 ?  200 HIS G N   1 
ATOM   14598 C CA  . HIS G  4 209 ? 65.541  44.726  276.524 1.00 236.67 ?  200 HIS G CA  1 
ATOM   14599 C C   . HIS G  4 209 ? 66.933  44.317  276.055 1.00 234.15 ?  200 HIS G C   1 
ATOM   14600 O O   . HIS G  4 209 ? 67.101  43.248  275.462 1.00 237.32 ?  200 HIS G O   1 
ATOM   14601 C CB  . HIS G  4 209 ? 64.826  43.572  277.215 1.00 239.91 ?  200 HIS G CB  1 
ATOM   14602 C CG  . HIS G  4 209 ? 65.483  43.125  278.482 1.00 239.27 ?  200 HIS G CG  1 
ATOM   14603 N ND1 . HIS G  4 209 ? 66.014  41.864  278.638 1.00 240.99 ?  200 HIS G ND1 1 
ATOM   14604 C CD2 . HIS G  4 209 ? 65.695  43.771  279.653 1.00 237.91 ?  200 HIS G CD2 1 
ATOM   14605 C CE1 . HIS G  4 209 ? 66.525  41.751  279.851 1.00 239.55 ?  200 HIS G CE1 1 
ATOM   14606 N NE2 . HIS G  4 209 ? 66.345  42.894  280.487 1.00 237.65 ?  200 HIS G NE2 1 
ATOM   14607 N N   . LYS G  4 210 ? 67.927  45.159  276.326 1.00 233.76 ?  201 LYS G N   1 
ATOM   14608 C CA  . LYS G  4 210 ? 69.273  44.938  275.804 1.00 232.75 ?  201 LYS G CA  1 
ATOM   14609 C C   . LYS G  4 210 ? 70.000  43.727  276.395 1.00 234.10 ?  201 LYS G C   1 
ATOM   14610 O O   . LYS G  4 210 ? 70.687  43.021  275.645 1.00 232.96 ?  201 LYS G O   1 
ATOM   14611 C CB  . LYS G  4 210 ? 70.137  46.183  276.008 1.00 226.39 ?  201 LYS G CB  1 
ATOM   14612 C CG  . LYS G  4 210 ? 71.454  46.095  275.252 1.00 225.68 ?  201 LYS G CG  1 
ATOM   14613 C CD  . LYS G  4 210 ? 72.322  47.326  275.422 1.00 221.16 ?  201 LYS G CD  1 
ATOM   14614 C CE  . LYS G  4 210 ? 73.513  47.281  274.471 1.00 219.31 ?  201 LYS G CE  1 
ATOM   14615 N NZ  . LYS G  4 210 ? 74.633  46.461  275.015 1.00 215.07 1  201 LYS G NZ  1 
ATOM   14616 N N   . PRO G  4 211 ? 69.905  43.449  277.706 1.00 234.71 ?  202 PRO G N   1 
ATOM   14617 C CA  . PRO G  4 211 ? 70.661  42.301  278.248 1.00 227.93 ?  202 PRO G CA  1 
ATOM   14618 C C   . PRO G  4 211 ? 70.346  40.986  277.557 1.00 236.44 ?  202 PRO G C   1 
ATOM   14619 O O   . PRO G  4 211 ? 71.257  40.188  277.299 1.00 231.31 ?  202 PRO G O   1 
ATOM   14620 C CB  . PRO G  4 211 ? 70.244  42.284  279.722 1.00 220.23 ?  202 PRO G CB  1 
ATOM   14621 C CG  . PRO G  4 211 ? 69.945  43.701  280.023 1.00 220.17 ?  202 PRO G CG  1 
ATOM   14622 C CD  . PRO G  4 211 ? 69.285  44.235  278.790 1.00 230.44 ?  202 PRO G CD  1 
ATOM   14623 N N   . SER G  4 212 ? 69.080  40.746  277.234 1.00 243.60 ?  203 SER G N   1 
ATOM   14624 C CA  . SER G  4 212 ? 68.688  39.579  276.466 1.00 249.32 ?  203 SER G CA  1 
ATOM   14625 C C   . SER G  4 212 ? 68.593  39.895  274.987 1.00 252.11 ?  203 SER G C   1 
ATOM   14626 O O   . SER G  4 212 ? 68.353  38.992  274.179 1.00 256.81 ?  203 SER G O   1 
ATOM   14627 C CB  . SER G  4 212 ? 67.339  39.048  276.964 1.00 250.13 ?  203 SER G CB  1 
ATOM   14628 O OG  . SER G  4 212 ? 66.315  40.017  276.843 1.00 248.21 ?  203 SER G OG  1 
ATOM   14629 N N   . ASN G  4 213 ? 68.808  41.158  274.629 1.00 258.47 ?  204 ASN G N   1 
ATOM   14630 C CA  . ASN G  4 213 ? 68.681  41.667  273.269 1.00 257.01 ?  204 ASN G CA  1 
ATOM   14631 C C   . ASN G  4 213 ? 67.388  41.176  272.621 1.00 264.03 ?  204 ASN G C   1 
ATOM   14632 O O   . ASN G  4 213 ? 67.388  40.422  271.653 1.00 268.03 ?  204 ASN G O   1 
ATOM   14633 C CB  . ASN G  4 213 ? 69.893  41.338  272.404 1.00 255.66 ?  204 ASN G CB  1 
ATOM   14634 C CG  . ASN G  4 213 ? 70.073  42.349  271.288 1.00 256.55 ?  204 ASN G CG  1 
ATOM   14635 O OD1 . ASN G  4 213 ? 70.105  41.997  270.113 1.00 255.35 ?  204 ASN G OD1 1 
ATOM   14636 N ND2 . ASN G  4 213 ? 70.179  43.624  271.657 1.00 259.45 ?  204 ASN G ND2 1 
ATOM   14637 N N   . THR G  4 214 ? 66.278  41.533  273.253 1.00 249.97 ?  205 THR G N   1 
ATOM   14638 C CA  . THR G  4 214 ? 64.957  41.286  272.705 1.00 254.50 ?  205 THR G CA  1 
ATOM   14639 C C   . THR G  4 214 ? 64.300  42.624  272.393 1.00 249.96 ?  205 THR G C   1 
ATOM   14640 O O   . THR G  4 214 ? 64.549  43.629  273.064 1.00 245.76 ?  205 THR G O   1 
ATOM   14641 C CB  . THR G  4 214 ? 64.073  40.487  273.668 1.00 256.80 ?  205 THR G CB  1 
ATOM   14642 O OG1 . THR G  4 214 ? 64.091  41.101  274.963 1.00 254.15 ?  205 THR G OG1 1 
ATOM   14643 C CG2 . THR G  4 214 ? 64.556  39.054  273.783 1.00 261.70 ?  205 THR G CG2 1 
ATOM   14644 N N   . LYS G  4 215 ? 63.472  42.628  271.358 1.00 267.30 ?  206 LYS G N   1 
ATOM   14645 C CA  . LYS G  4 215 ? 62.647  43.774  271.002 1.00 266.20 ?  206 LYS G CA  1 
ATOM   14646 C C   . LYS G  4 215 ? 61.246  43.229  270.800 1.00 271.31 ?  206 LYS G C   1 
ATOM   14647 O O   . LYS G  4 215 ? 61.085  42.210  270.137 1.00 276.50 ?  206 LYS G O   1 
ATOM   14648 C CB  . LYS G  4 215 ? 63.139  44.463  269.721 1.00 265.19 ?  206 LYS G CB  1 
ATOM   14649 C CG  . LYS G  4 215 ? 64.533  45.061  269.809 1.00 262.61 ?  206 LYS G CG  1 
ATOM   14650 C CD  . LYS G  4 215 ? 64.899  45.754  268.507 1.00 261.55 ?  206 LYS G CD  1 
ATOM   14651 C CE  . LYS G  4 215 ? 66.235  46.474  268.599 1.00 258.79 ?  206 LYS G CE  1 
ATOM   14652 N NZ  . LYS G  4 215 ? 67.354  45.545  268.933 1.00 262.92 1  206 LYS G NZ  1 
ATOM   14653 N N   . VAL G  4 216 ? 60.242  43.818  271.434 1.00 254.66 ?  207 VAL G N   1 
ATOM   14654 C CA  . VAL G  4 216 ? 58.876  43.346  271.243 1.00 259.17 ?  207 VAL G CA  1 
ATOM   14655 C C   . VAL G  4 216 ? 58.008  44.518  270.812 1.00 257.34 ?  207 VAL G C   1 
ATOM   14656 O O   . VAL G  4 216 ? 58.077  45.605  271.398 1.00 255.82 ?  207 VAL G O   1 
ATOM   14657 C CB  . VAL G  4 216 ? 58.318  42.658  272.506 1.00 261.70 ?  207 VAL G CB  1 
ATOM   14658 C CG1 . VAL G  4 216 ? 56.856  42.293  272.323 1.00 267.87 ?  207 VAL G CG1 1 
ATOM   14659 C CG2 . VAL G  4 216 ? 59.124  41.401  272.824 1.00 265.91 ?  207 VAL G CG2 1 
ATOM   14660 N N   . ASP G  4 217 ? 57.203  44.290  269.784 1.00 261.78 ?  208 ASP G N   1 
ATOM   14661 C CA  . ASP G  4 217 ? 56.163  45.206  269.344 1.00 261.64 ?  208 ASP G CA  1 
ATOM   14662 C C   . ASP G  4 217 ? 54.837  44.498  269.581 1.00 266.19 ?  208 ASP G C   1 
ATOM   14663 O O   . ASP G  4 217 ? 54.732  43.297  269.327 1.00 272.63 ?  208 ASP G O   1 
ATOM   14664 C CB  . ASP G  4 217 ? 56.339  45.587  267.869 1.00 261.26 ?  208 ASP G CB  1 
ATOM   14665 C CG  . ASP G  4 217 ? 57.658  46.291  267.602 1.00 258.91 ?  208 ASP G CG  1 
ATOM   14666 O OD1 . ASP G  4 217 ? 57.967  47.252  268.335 1.00 255.70 ?  208 ASP G OD1 1 
ATOM   14667 O OD2 . ASP G  4 217 ? 58.382  45.891  266.665 1.00 261.12 -1 208 ASP G OD2 1 
ATOM   14668 N N   . LYS G  4 218 ? 53.907  45.168  270.260 1.00 251.16 ?  209 LYS G N   1 
ATOM   14669 C CA  . LYS G  4 218 ? 52.611  44.565  270.550 1.00 254.56 ?  209 LYS G CA  1 
ATOM   14670 C C   . LYS G  4 218 ? 51.514  45.564  270.203 1.00 254.91 ?  209 LYS G C   1 
ATOM   14671 O O   . LYS G  4 218 ? 51.463  46.650  270.787 1.00 252.47 ?  209 LYS G O   1 
ATOM   14672 C CB  . LYS G  4 218 ? 52.528  44.137  272.020 1.00 254.20 ?  209 LYS G CB  1 
ATOM   14673 C CG  . LYS G  4 218 ? 51.374  43.211  272.347 1.00 257.97 ?  209 LYS G CG  1 
ATOM   14674 C CD  . LYS G  4 218 ? 51.681  41.827  271.793 1.00 261.32 ?  209 LYS G CD  1 
ATOM   14675 C CE  . LYS G  4 218 ? 50.691  40.798  272.294 1.00 264.67 ?  209 LYS G CE  1 
ATOM   14676 N NZ  . LYS G  4 218 ? 51.110  39.407  271.962 1.00 267.66 1  209 LYS G NZ  1 
ATOM   14677 N N   . LYS G  4 219 ? 50.651  45.220  269.246 1.00 243.21 ?  210 LYS G N   1 
ATOM   14678 C CA  . LYS G  4 219 ? 49.493  46.057  268.945 1.00 244.17 ?  210 LYS G CA  1 
ATOM   14679 C C   . LYS G  4 219 ? 48.403  45.823  269.983 1.00 247.34 ?  210 LYS G C   1 
ATOM   14680 O O   . LYS G  4 219 ? 48.092  44.676  270.325 1.00 250.00 ?  210 LYS G O   1 
ATOM   14681 C CB  . LYS G  4 219 ? 48.959  45.765  267.546 1.00 246.88 ?  210 LYS G CB  1 
ATOM   14682 C CG  . LYS G  4 219 ? 47.789  46.619  267.062 1.00 251.70 ?  210 LYS G CG  1 
ATOM   14683 C CD  . LYS G  4 219 ? 47.499  46.282  265.604 1.00 254.94 ?  210 LYS G CD  1 
ATOM   14684 C CE  . LYS G  4 219 ? 46.208  46.907  265.115 1.00 261.30 ?  210 LYS G CE  1 
ATOM   14685 N NZ  . LYS G  4 219 ? 45.956  46.600  263.678 1.00 264.63 1  210 LYS G NZ  1 
ATOM   14686 N N   . VAL G  4 220 ? 47.827  46.912  270.481 1.00 254.18 ?  211 VAL G N   1 
ATOM   14687 C CA  . VAL G  4 220 ? 46.802  46.878  271.518 1.00 258.80 ?  211 VAL G CA  1 
ATOM   14688 C C   . VAL G  4 220 ? 45.521  47.426  270.911 1.00 265.31 ?  211 VAL G C   1 
ATOM   14689 O O   . VAL G  4 220 ? 45.471  48.595  270.508 1.00 264.97 ?  211 VAL G O   1 
ATOM   14690 C CB  . VAL G  4 220 ? 47.212  47.691  272.755 1.00 255.65 ?  211 VAL G CB  1 
ATOM   14691 C CG1 . VAL G  4 220 ? 46.154  47.578  273.834 1.00 261.12 ?  211 VAL G CG1 1 
ATOM   14692 C CG2 . VAL G  4 220 ? 48.559  47.224  273.269 1.00 249.07 ?  211 VAL G CG2 1 
ATOM   14693 N N   . GLU G  4 221 ? 44.495  46.588  270.842 1.00 255.65 ?  212 GLU G N   1 
ATOM   14694 C CA  . GLU G  4 221 ? 43.245  46.907  270.173 1.00 262.59 ?  212 GLU G CA  1 
ATOM   14695 C C   . GLU G  4 221 ? 42.080  46.458  271.042 1.00 269.15 ?  212 GLU G C   1 
ATOM   14696 O O   . GLU G  4 221 ? 42.254  45.630  271.943 1.00 268.49 ?  212 GLU G O   1 
ATOM   14697 C CB  . GLU G  4 221 ? 43.181  46.238  268.793 1.00 264.20 ?  212 GLU G CB  1 
ATOM   14698 C CG  . GLU G  4 221 ? 43.430  44.743  268.812 1.00 264.29 ?  212 GLU G CG  1 
ATOM   14699 C CD  . GLU G  4 221 ? 43.734  44.195  267.434 1.00 264.15 ?  212 GLU G CD  1 
ATOM   14700 O OE1 . GLU G  4 221 ? 44.344  43.109  267.351 1.00 265.13 ?  212 GLU G OE1 1 
ATOM   14701 O OE2 . GLU G  4 221 ? 43.359  44.845  266.435 1.00 266.30 -1 212 GLU G OE2 1 
ATOM   14702 N N   . PRO G  4 222 ? 40.885  47.007  270.812 1.00 254.91 ?  213 PRO G N   1 
ATOM   14703 C CA  . PRO G  4 222 ? 39.705  46.548  271.558 1.00 262.29 ?  213 PRO G CA  1 
ATOM   14704 C C   . PRO G  4 222 ? 39.491  45.045  271.429 1.00 264.98 ?  213 PRO G C   1 
ATOM   14705 O O   . PRO G  4 222 ? 39.633  44.465  270.350 1.00 265.00 ?  213 PRO G O   1 
ATOM   14706 C CB  . PRO G  4 222 ? 38.556  47.340  270.923 1.00 269.10 ?  213 PRO G CB  1 
ATOM   14707 C CG  . PRO G  4 222 ? 39.208  48.581  270.395 1.00 264.69 ?  213 PRO G CG  1 
ATOM   14708 C CD  . PRO G  4 222 ? 40.582  48.167  269.952 1.00 256.47 ?  213 PRO G CD  1 
ATOM   14709 N N   . LYS G  4 223 ? 39.149  44.416  272.549 1.00 287.13 ?  214 LYS G N   1 
ATOM   14710 C CA  . LYS G  4 223 ? 38.957  42.971  272.588 1.00 290.01 ?  214 LYS G CA  1 
ATOM   14711 C C   . LYS G  4 223 ? 37.582  42.581  272.048 1.00 300.79 ?  214 LYS G C   1 
ATOM   14712 O O   . LYS G  4 223 ? 36.611  43.328  272.182 1.00 307.07 ?  214 LYS G O   1 
ATOM   14713 C CB  . LYS G  4 223 ? 39.128  42.443  274.017 1.00 290.52 ?  214 LYS G CB  1 
ATOM   14714 C CG  . LYS G  4 223 ? 39.040  40.927  274.123 1.00 296.40 ?  214 LYS G CG  1 
ATOM   14715 C CD  . LYS G  4 223 ? 39.109  40.445  275.565 1.00 297.08 ?  214 LYS G CD  1 
ATOM   14716 C CE  . LYS G  4 223 ? 38.974  38.930  275.632 1.00 299.85 ?  214 LYS G CE  1 
ATOM   14717 N NZ  . LYS G  4 223 ? 38.903  38.428  277.032 1.00 303.31 1  214 LYS G NZ  1 
ATOM   14718 N N   . ALA H  2 1   ? 87.031  67.044  312.306 1.00 189.63 ?  512 ALA D N   1 
ATOM   14719 C CA  . ALA H  2 1   ? 86.433  66.045  311.427 1.00 184.09 ?  512 ALA D CA  1 
ATOM   14720 C C   . ALA H  2 1   ? 87.398  64.887  311.182 1.00 178.56 ?  512 ALA D C   1 
ATOM   14721 O O   . ALA H  2 1   ? 88.570  64.961  311.550 1.00 176.44 ?  512 ALA D O   1 
ATOM   14722 C CB  . ALA H  2 1   ? 86.019  66.681  310.112 1.00 181.85 ?  512 ALA D CB  1 
ATOM   14723 N N   . VAL H  2 2   ? 86.892  63.813  310.569 1.00 169.23 ?  513 VAL D N   1 
ATOM   14724 C CA  . VAL H  2 2   ? 87.729  62.665  310.245 1.00 169.79 ?  513 VAL D CA  1 
ATOM   14725 C C   . VAL H  2 2   ? 88.631  62.995  309.059 1.00 168.54 ?  513 VAL D C   1 
ATOM   14726 O O   . VAL H  2 2   ? 88.294  63.817  308.197 1.00 167.87 ?  513 VAL D O   1 
ATOM   14727 C CB  . VAL H  2 2   ? 86.860  61.425  309.961 1.00 172.04 ?  513 VAL D CB  1 
ATOM   14728 C CG1 . VAL H  2 2   ? 86.123  60.991  311.224 1.00 173.26 ?  513 VAL D CG1 1 
ATOM   14729 C CG2 . VAL H  2 2   ? 85.869  61.718  308.840 1.00 172.60 ?  513 VAL D CG2 1 
ATOM   14730 N N   . GLY H  2 3   ? 89.793  62.357  309.019 1.00 185.31 ?  514 GLY D N   1 
ATOM   14731 C CA  . GLY H  2 3   ? 90.743  62.582  307.943 1.00 178.43 ?  514 GLY D CA  1 
ATOM   14732 C C   . GLY H  2 3   ? 91.500  61.314  307.629 1.00 179.21 ?  514 GLY D C   1 
ATOM   14733 O O   . GLY H  2 3   ? 91.652  60.433  308.482 1.00 180.13 ?  514 GLY D O   1 
ATOM   14734 N N   . ILE H  2 4   ? 91.982  61.221  306.390 1.00 165.29 ?  515 ILE D N   1 
ATOM   14735 C CA  . ILE H  2 4   ? 92.686  60.026  305.936 1.00 166.03 ?  515 ILE D CA  1 
ATOM   14736 C C   . ILE H  2 4   ? 94.083  60.404  305.445 1.00 164.30 ?  515 ILE D C   1 
ATOM   14737 O O   . ILE H  2 4   ? 94.687  59.700  304.628 1.00 164.55 ?  515 ILE D O   1 
ATOM   14738 C CB  . ILE H  2 4   ? 91.864  59.289  304.858 1.00 167.63 ?  515 ILE D CB  1 
ATOM   14739 C CG1 . ILE H  2 4   ? 92.371  57.854  304.662 1.00 168.86 ?  515 ILE D CG1 1 
ATOM   14740 C CG2 . ILE H  2 4   ? 91.828  60.080  303.560 1.00 166.71 ?  515 ILE D CG2 1 
ATOM   14741 C CD1 . ILE H  2 4   ? 91.352  56.924  304.062 1.00 170.88 ?  515 ILE D CD1 1 
ATOM   14742 N N   . GLY H  2 5   ? 94.615  61.509  305.960 1.00 176.99 ?  516 GLY D N   1 
ATOM   14743 C CA  . GLY H  2 5   ? 96.016  61.843  305.778 1.00 175.31 ?  516 GLY D CA  1 
ATOM   14744 C C   . GLY H  2 5   ? 96.256  62.884  304.700 1.00 173.85 ?  516 GLY D C   1 
ATOM   14745 O O   . GLY H  2 5   ? 95.337  63.437  304.087 1.00 174.02 ?  516 GLY D O   1 
ATOM   14746 N N   . ALA H  2 6   ? 97.544  63.151  304.488 1.00 177.02 ?  517 ALA D N   1 
ATOM   14747 C CA  . ALA H  2 6   ? 97.978  64.148  303.521 1.00 177.81 ?  517 ALA D CA  1 
ATOM   14748 C C   . ALA H  2 6   ? 97.697  63.698  302.092 1.00 175.89 ?  517 ALA D C   1 
ATOM   14749 O O   . ALA H  2 6   ? 97.646  62.503  301.788 1.00 177.32 ?  517 ALA D O   1 
ATOM   14750 C CB  . ALA H  2 6   ? 99.470  64.436  303.688 1.00 174.51 ?  517 ALA D CB  1 
ATOM   14751 N N   . VAL H  2 7   ? 97.523  64.680  301.208 1.00 169.73 ?  518 VAL D N   1 
ATOM   14752 C CA  . VAL H  2 7   ? 97.319  64.437  299.784 1.00 170.17 ?  518 VAL D CA  1 
ATOM   14753 C C   . VAL H  2 7   ? 98.447  65.118  299.012 1.00 168.34 ?  518 VAL D C   1 
ATOM   14754 O O   . VAL H  2 7   ? 99.392  65.641  299.614 1.00 166.89 ?  518 VAL D O   1 
ATOM   14755 C CB  . VAL H  2 7   ? 95.922  64.896  299.328 1.00 170.91 ?  518 VAL D CB  1 
ATOM   14756 C CG1 . VAL H  2 7   ? 94.873  63.865  299.751 1.00 173.07 ?  518 VAL D CG1 1 
ATOM   14757 C CG2 . VAL H  2 7   ? 95.586  66.256  299.921 1.00 177.05 ?  518 VAL D CG2 1 
ATOM   14758 N N   . PHE H  2 8   ? 98.362  65.127  297.683 1.00 180.13 ?  519 PHE D N   1 
ATOM   14759 C CA  . PHE H  2 8   ? 99.391  65.735  296.848 1.00 174.18 ?  519 PHE D CA  1 
ATOM   14760 C C   . PHE H  2 8   ? 98.779  66.608  295.760 1.00 174.59 ?  519 PHE D C   1 
ATOM   14761 O O   . PHE H  2 8   ? 97.754  66.247  295.174 1.00 174.29 ?  519 PHE D O   1 
ATOM   14762 C CB  . PHE H  2 8   ? 100.238 64.610  296.254 1.00 173.92 ?  519 PHE D CB  1 
ATOM   14763 C CG  . PHE H  2 8   ? 101.380 65.074  295.424 1.00 172.33 ?  519 PHE D CG  1 
ATOM   14764 C CD1 . PHE H  2 8   ? 102.509 65.605  296.019 1.00 170.72 ?  519 PHE D CD1 1 
ATOM   14765 C CD2 . PHE H  2 8   ? 101.363 64.903  294.052 1.00 172.51 ?  519 PHE D CD2 1 
ATOM   14766 C CE1 . PHE H  2 8   ? 103.580 66.014  295.256 1.00 169.27 ?  519 PHE D CE1 1 
ATOM   14767 C CE2 . PHE H  2 8   ? 102.434 65.297  293.284 1.00 171.07 ?  519 PHE D CE2 1 
ATOM   14768 C CZ  . PHE H  2 8   ? 103.544 65.859  293.885 1.00 169.44 ?  519 PHE D CZ  1 
ATOM   14769 N N   . LEU H  2 9   ? 99.413  67.759  295.480 1.00 167.00 ?  520 LEU D N   1 
ATOM   14770 C CA  . LEU H  2 9   ? 98.855  68.670  294.487 1.00 166.46 ?  520 LEU D CA  1 
ATOM   14771 C C   . LEU H  2 9   ? 99.600  68.684  293.157 1.00 165.74 ?  520 LEU D C   1 
ATOM   14772 O O   . LEU H  2 9   ? 99.004  69.044  292.135 1.00 165.87 ?  520 LEU D O   1 
ATOM   14773 C CB  . LEU H  2 9   ? 98.908  70.093  295.054 1.00 164.82 ?  520 LEU D CB  1 
ATOM   14774 C CG  . LEU H  2 9   ? 98.230  70.377  296.393 1.00 165.13 ?  520 LEU D CG  1 
ATOM   14775 C CD1 . LEU H  2 9   ? 98.363  71.861  296.733 1.00 163.36 ?  520 LEU D CD1 1 
ATOM   14776 C CD2 . LEU H  2 9   ? 96.772  69.936  296.366 1.00 166.96 ?  520 LEU D CD2 1 
ATOM   14777 N N   . GLY H  2 10  ? 100.870 68.313  293.145 1.00 176.80 ?  521 GLY D N   1 
ATOM   14778 C CA  . GLY H  2 10  ? 101.675 68.232  291.941 1.00 176.14 ?  521 GLY D CA  1 
ATOM   14779 C C   . GLY H  2 10  ? 102.556 69.445  291.725 1.00 173.98 ?  521 GLY D C   1 
ATOM   14780 O O   . GLY H  2 10  ? 102.700 70.327  292.579 1.00 172.88 ?  521 GLY D O   1 
ATOM   14781 N N   . PHE H  2 11  ? 103.180 69.459  290.545 1.00 170.32 ?  522 PHE D N   1 
ATOM   14782 C CA  . PHE H  2 11  ? 104.032 70.569  290.139 1.00 168.80 ?  522 PHE D CA  1 
ATOM   14783 C C   . PHE H  2 11  ? 103.216 71.851  290.032 1.00 172.02 ?  522 PHE D C   1 
ATOM   14784 O O   . PHE H  2 11  ? 102.188 71.883  289.346 1.00 173.89 ?  522 PHE D O   1 
ATOM   14785 C CB  . PHE H  2 11  ? 104.730 70.272  288.815 1.00 167.90 ?  522 PHE D CB  1 
ATOM   14786 C CG  . PHE H  2 11  ? 105.762 71.299  288.439 1.00 165.85 ?  522 PHE D CG  1 
ATOM   14787 C CD1 . PHE H  2 11  ? 106.948 71.408  289.146 1.00 164.70 ?  522 PHE D CD1 1 
ATOM   14788 C CD2 . PHE H  2 11  ? 105.545 72.154  287.371 1.00 166.28 ?  522 PHE D CD2 1 
ATOM   14789 C CE1 . PHE H  2 11  ? 107.899 72.355  288.797 1.00 163.08 ?  522 PHE D CE1 1 
ATOM   14790 C CE2 . PHE H  2 11  ? 106.493 73.099  287.015 1.00 165.84 ?  522 PHE D CE2 1 
ATOM   14791 C CZ  . PHE H  2 11  ? 107.671 73.200  287.730 1.00 164.30 ?  522 PHE D CZ  1 
ATOM   14792 N N   . LEU H  2 12  ? 103.677 72.909  290.694 1.00 168.78 ?  523 LEU D N   1 
ATOM   14793 C CA  . LEU H  2 12  ? 102.989 74.200  290.715 1.00 168.00 ?  523 LEU D CA  1 
ATOM   14794 C C   . LEU H  2 12  ? 101.564 74.082  291.244 1.00 172.85 ?  523 LEU D C   1 
ATOM   14795 O O   . LEU H  2 12  ? 100.705 74.903  290.908 1.00 179.15 ?  523 LEU D O   1 
ATOM   14796 C CB  . LEU H  2 12  ? 102.990 74.865  289.330 1.00 167.26 ?  523 LEU D CB  1 
ATOM   14797 C CG  . LEU H  2 12  ? 104.356 75.246  288.751 1.00 165.65 ?  523 LEU D CG  1 
ATOM   14798 C CD1 . LEU H  2 12  ? 104.216 75.840  287.362 1.00 165.13 ?  523 LEU D CD1 1 
ATOM   14799 C CD2 . LEU H  2 12  ? 105.094 76.202  289.668 1.00 164.32 ?  523 LEU D CD2 1 
ATOM   14800 N N   . GLY H  2 13  ? 101.305 73.063  292.058 1.00 154.14 ?  524 GLY D N   1 
ATOM   14801 C CA  . GLY H  2 13  ? 99.984  72.779  292.580 1.00 154.67 ?  524 GLY D CA  1 
ATOM   14802 C C   . GLY H  2 13  ? 99.366  73.908  293.372 1.00 159.29 ?  524 GLY D C   1 
ATOM   14803 O O   . GLY H  2 13  ? 98.300  74.428  293.024 1.00 163.09 ?  524 GLY D O   1 
ATOM   14804 N N   . ALA H  2 14  ? 100.054 74.308  294.435 1.00 155.47 ?  525 ALA D N   1 
ATOM   14805 C CA  . ALA H  2 14  ? 99.571  75.346  295.341 1.00 161.00 ?  525 ALA D CA  1 
ATOM   14806 C C   . ALA H  2 14  ? 99.947  76.750  294.875 1.00 164.14 ?  525 ALA D C   1 
ATOM   14807 O O   . ALA H  2 14  ? 100.459 77.561  295.643 1.00 166.70 ?  525 ALA D O   1 
ATOM   14808 C CB  . ALA H  2 14  ? 100.101 75.079  296.744 1.00 160.65 ?  525 ALA D CB  1 
ATOM   14809 N N   . ALA H  2 15  ? 99.700  77.044  293.597 1.00 145.54 ?  526 ALA D N   1 
ATOM   14810 C CA  . ALA H  2 15  ? 100.005 78.373  293.081 1.00 148.93 ?  526 ALA D CA  1 
ATOM   14811 C C   . ALA H  2 15  ? 98.960  79.371  293.550 1.00 155.64 ?  526 ALA D C   1 
ATOM   14812 O O   . ALA H  2 15  ? 99.282  80.535  293.818 1.00 159.89 ?  526 ALA D O   1 
ATOM   14813 C CB  . ALA H  2 15  ? 100.088 78.351  291.555 1.00 146.97 ?  526 ALA D CB  1 
ATOM   14814 N N   . GLY H  2 16  ? 97.717  78.917  293.670 1.00 148.11 ?  527 GLY D N   1 
ATOM   14815 C CA  . GLY H  2 16  ? 96.574  79.671  294.124 1.00 154.65 ?  527 GLY D CA  1 
ATOM   14816 C C   . GLY H  2 16  ? 96.306  79.521  295.600 1.00 157.24 ?  527 GLY D C   1 
ATOM   14817 O O   . GLY H  2 16  ? 95.369  80.132  296.121 1.00 163.25 ?  527 GLY D O   1 
ATOM   14818 N N   . SER H  2 17  ? 97.101  78.710  296.295 1.00 156.77 ?  528 SER D N   1 
ATOM   14819 C CA  . SER H  2 17  ? 96.931  78.526  297.725 1.00 160.25 ?  528 SER D CA  1 
ATOM   14820 C C   . SER H  2 17  ? 97.669  79.638  298.467 1.00 163.44 ?  528 SER D C   1 
ATOM   14821 O O   . SER H  2 17  ? 98.490  80.362  297.897 1.00 161.88 ?  528 SER D O   1 
ATOM   14822 C CB  . SER H  2 17  ? 97.429  77.146  298.155 1.00 153.62 ?  528 SER D CB  1 
ATOM   14823 O OG  . SER H  2 17  ? 96.714  76.117  297.490 1.00 154.15 ?  528 SER D OG  1 
ATOM   14824 N N   . THR H  2 18  ? 97.365  79.781  299.753 1.00 168.24 ?  529 THR D N   1 
ATOM   14825 C CA  . THR H  2 18  ? 98.037  80.793  300.553 1.00 171.84 ?  529 THR D CA  1 
ATOM   14826 C C   . THR H  2 18  ? 99.536  80.524  300.642 1.00 166.75 ?  529 THR D C   1 
ATOM   14827 O O   . THR H  2 18  ? 100.010 79.408  300.418 1.00 160.81 ?  529 THR D O   1 
ATOM   14828 C CB  . THR H  2 18  ? 97.447  80.820  301.960 1.00 176.62 ?  529 THR D CB  1 
ATOM   14829 O OG1 . THR H  2 18  ? 97.116  79.483  302.355 1.00 173.21 ?  529 THR D OG1 1 
ATOM   14830 C CG2 . THR H  2 18  ? 96.186  81.664  301.987 1.00 184.20 ?  529 THR D CG2 1 
ATOM   14831 N N   . MET H  2 19  ? 100.289 81.579  300.974 1.00 180.24 ?  530 MET D N   1 
ATOM   14832 C CA  . MET H  2 19  ? 101.736 81.427  301.094 1.00 174.43 ?  530 MET D CA  1 
ATOM   14833 C C   . MET H  2 19  ? 102.079 80.450  302.206 1.00 177.48 ?  530 MET D C   1 
ATOM   14834 O O   . MET H  2 19  ? 103.040 79.680  302.095 1.00 172.61 ?  530 MET D O   1 
ATOM   14835 C CB  . MET H  2 19  ? 102.406 82.779  301.343 1.00 173.92 ?  530 MET D CB  1 
ATOM   14836 C CG  . MET H  2 19  ? 102.287 83.771  300.201 1.00 174.61 ?  530 MET D CG  1 
ATOM   14837 S SD  . MET H  2 19  ? 102.995 85.374  300.621 1.00 175.60 ?  530 MET D SD  1 
ATOM   14838 C CE  . MET H  2 19  ? 104.661 84.905  301.085 1.00 181.13 ?  530 MET D CE  1 
ATOM   14839 N N   . GLY H  2 20  ? 101.308 80.480  303.296 1.00 179.35 ?  531 GLY D N   1 
ATOM   14840 C CA  . GLY H  2 20  ? 101.542 79.544  304.382 1.00 183.34 ?  531 GLY D CA  1 
ATOM   14841 C C   . GLY H  2 20  ? 101.260 78.117  303.958 1.00 183.58 ?  531 GLY D C   1 
ATOM   14842 O O   . GLY H  2 20  ? 101.966 77.186  304.357 1.00 182.91 ?  531 GLY D O   1 
ATOM   14843 N N   . ALA H  2 21  ? 100.220 77.926  303.143 1.00 171.22 ?  532 ALA D N   1 
ATOM   14844 C CA  . ALA H  2 21  ? 99.877  76.595  302.664 1.00 171.49 ?  532 ALA D CA  1 
ATOM   14845 C C   . ALA H  2 21  ? 100.830 76.163  301.558 1.00 163.39 ?  532 ALA D C   1 
ATOM   14846 O O   . ALA H  2 21  ? 101.198 74.986  301.475 1.00 162.39 ?  532 ALA D O   1 
ATOM   14847 C CB  . ALA H  2 21  ? 98.427  76.562  302.183 1.00 174.68 ?  532 ALA D CB  1 
ATOM   14848 N N   . ALA H  2 22  ? 101.238 77.104  300.700 1.00 179.91 ?  533 ALA D N   1 
ATOM   14849 C CA  . ALA H  2 22  ? 102.138 76.795  299.596 1.00 171.22 ?  533 ALA D CA  1 
ATOM   14850 C C   . ALA H  2 22  ? 103.564 76.561  300.073 1.00 166.35 ?  533 ALA D C   1 
ATOM   14851 O O   . ALA H  2 22  ? 104.391 76.069  299.300 1.00 159.42 ?  533 ALA D O   1 
ATOM   14852 C CB  . ALA H  2 22  ? 102.109 77.918  298.556 1.00 166.50 ?  533 ALA D CB  1 
ATOM   14853 N N   . SER H  2 23  ? 103.874 76.918  301.318 1.00 168.87 ?  534 SER D N   1 
ATOM   14854 C CA  . SER H  2 23  ? 105.204 76.698  301.867 1.00 163.87 ?  534 SER D CA  1 
ATOM   14855 C C   . SER H  2 23  ? 105.447 75.232  302.188 1.00 164.47 ?  534 SER D C   1 
ATOM   14856 O O   . SER H  2 23  ? 106.592 74.852  302.453 1.00 157.77 ?  534 SER D O   1 
ATOM   14857 C CB  . SER H  2 23  ? 105.405 77.547  303.123 1.00 168.29 ?  534 SER D CB  1 
ATOM   14858 O OG  . SER H  2 23  ? 105.275 78.927  302.830 1.00 167.71 ?  534 SER D OG  1 
ATOM   14859 N N   . MET H  2 24  ? 104.402 74.405  302.136 1.00 170.58 ?  535 MET D N   1 
ATOM   14860 C CA  . MET H  2 24  ? 104.503 72.976  302.388 1.00 173.24 ?  535 MET D CA  1 
ATOM   14861 C C   . MET H  2 24  ? 104.880 72.185  301.141 1.00 164.84 ?  535 MET D C   1 
ATOM   14862 O O   . MET H  2 24  ? 105.284 71.022  301.259 1.00 163.40 ?  535 MET D O   1 
ATOM   14863 C CB  . MET H  2 24  ? 103.158 72.451  302.910 1.00 188.50 ?  535 MET D CB  1 
ATOM   14864 C CG  . MET H  2 24  ? 102.477 73.341  303.954 1.00 196.83 ?  535 MET D CG  1 
ATOM   14865 S SD  . MET H  2 24  ? 103.383 73.654  305.479 1.00 207.88 ?  535 MET D SD  1 
ATOM   14866 C CE  . MET H  2 24  ? 102.157 74.581  306.403 1.00 212.12 ?  535 MET D CE  1 
ATOM   14867 N N   . THR H  2 25  ? 104.767 72.792  299.959 1.00 173.25 ?  536 THR D N   1 
ATOM   14868 C CA  . THR H  2 25  ? 105.015 72.144  298.675 1.00 168.96 ?  536 THR D CA  1 
ATOM   14869 C C   . THR H  2 25  ? 106.335 72.587  298.043 1.00 156.53 ?  536 THR D C   1 
ATOM   14870 O O   . THR H  2 25  ? 106.509 72.464  296.826 1.00 149.70 ?  536 THR D O   1 
ATOM   14871 C CB  . THR H  2 25  ? 103.840 72.371  297.717 1.00 175.17 ?  536 THR D CB  1 
ATOM   14872 O OG1 . THR H  2 25  ? 104.052 71.637  296.504 1.00 166.33 ?  536 THR D OG1 1 
ATOM   14873 C CG2 . THR H  2 25  ? 103.684 73.834  297.380 1.00 167.29 ?  536 THR D CG2 1 
ATOM   14874 N N   . LEU H  2 26  ? 107.281 73.067  298.853 1.00 153.81 ?  537 LEU D N   1 
ATOM   14875 C CA  . LEU H  2 26  ? 108.548 73.572  298.328 1.00 141.71 ?  537 LEU D CA  1 
ATOM   14876 C C   . LEU H  2 26  ? 109.381 72.464  297.694 1.00 134.78 ?  537 LEU D C   1 
ATOM   14877 O O   . LEU H  2 26  ? 110.075 72.701  296.698 1.00 134.61 ?  537 LEU D O   1 
ATOM   14878 C CB  . LEU H  2 26  ? 109.351 74.253  299.434 1.00 139.95 ?  537 LEU D CB  1 
ATOM   14879 C CG  . LEU H  2 26  ? 108.816 75.560  300.004 1.00 147.20 ?  537 LEU D CG  1 
ATOM   14880 C CD1 . LEU H  2 26  ? 109.750 76.043  301.095 1.00 145.84 ?  537 LEU D CD1 1 
ATOM   14881 C CD2 . LEU H  2 26  ? 108.681 76.595  298.903 1.00 146.98 ?  537 LEU D CD2 1 
ATOM   14882 N N   . THR H  2 27  ? 109.334 71.253  298.244 1.00 158.73 ?  538 THR D N   1 
ATOM   14883 C CA  . THR H  2 27  ? 110.160 70.178  297.706 1.00 150.66 ?  538 THR D CA  1 
ATOM   14884 C C   . THR H  2 27  ? 109.585 69.578  296.427 1.00 148.90 ?  538 THR D C   1 
ATOM   14885 O O   . THR H  2 27  ? 110.172 68.632  295.893 1.00 145.58 ?  538 THR D O   1 
ATOM   14886 C CB  . THR H  2 27  ? 110.361 69.071  298.748 1.00 152.89 ?  538 THR D CB  1 
ATOM   14887 O OG1 . THR H  2 27  ? 111.289 68.102  298.242 1.00 147.63 ?  538 THR D OG1 1 
ATOM   14888 C CG2 . THR H  2 27  ? 109.054 68.371  299.041 1.00 164.51 ?  538 THR D CG2 1 
ATOM   14889 N N   . VAL H  2 28  ? 108.484 70.118  295.916 1.00 134.11 ?  539 VAL D N   1 
ATOM   14890 C CA  . VAL H  2 28  ? 107.845 69.640  294.695 1.00 133.02 ?  539 VAL D CA  1 
ATOM   14891 C C   . VAL H  2 28  ? 108.262 70.491  293.506 1.00 127.54 ?  539 VAL D C   1 
ATOM   14892 O O   . VAL H  2 28  ? 108.591 69.974  292.440 1.00 125.09 ?  539 VAL D O   1 
ATOM   14893 C CB  . VAL H  2 28  ? 106.308 69.625  294.862 1.00 145.25 ?  539 VAL D CB  1 
ATOM   14894 C CG1 . VAL H  2 28  ? 105.631 69.208  293.567 1.00 143.41 ?  539 VAL D CG1 1 
ATOM   14895 C CG2 . VAL H  2 28  ? 105.908 68.712  296.016 1.00 153.22 ?  539 VAL D CG2 1 
ATOM   14896 N N   . GLN H  2 29  ? 108.250 71.811  293.679 1.00 132.62 ?  540 GLN D N   1 
ATOM   14897 C CA  . GLN H  2 29  ? 108.690 72.708  292.624 1.00 132.83 ?  540 GLN D CA  1 
ATOM   14898 C C   . GLN H  2 29  ? 110.204 72.672  292.455 1.00 132.56 ?  540 GLN D C   1 
ATOM   14899 O O   . GLN H  2 29  ? 110.714 73.088  291.410 1.00 132.63 ?  540 GLN D O   1 
ATOM   14900 C CB  . GLN H  2 29  ? 108.215 74.129  292.912 1.00 133.61 ?  540 GLN D CB  1 
ATOM   14901 C CG  . GLN H  2 29  ? 106.724 74.340  292.681 1.00 134.07 ?  540 GLN D CG  1 
ATOM   14902 C CD  . GLN H  2 29  ? 105.881 73.899  293.860 1.00 134.26 ?  540 GLN D CD  1 
ATOM   14903 O OE1 . GLN H  2 29  ? 104.744 73.456  293.697 1.00 134.37 ?  540 GLN D OE1 1 
ATOM   14904 N NE2 . GLN H  2 29  ? 106.440 74.011  295.057 1.00 134.33 ?  540 GLN D NE2 1 
ATOM   14905 N N   . ALA H  2 30  ? 110.930 72.200  293.466 1.00 137.18 ?  541 ALA D N   1 
ATOM   14906 C CA  . ALA H  2 30  ? 112.384 72.103  293.401 1.00 135.42 ?  541 ALA D CA  1 
ATOM   14907 C C   . ALA H  2 30  ? 112.807 70.863  292.629 1.00 131.62 ?  541 ALA D C   1 
ATOM   14908 O O   . ALA H  2 30  ? 113.891 70.829  292.030 1.00 131.22 ?  541 ALA D O   1 
ATOM   14909 C CB  . ALA H  2 30  ? 112.971 72.088  294.811 1.00 135.29 ?  541 ALA D CB  1 
ATOM   14910 N N   . ARG H  2 31  ? 111.948 69.846  292.659 1.00 142.23 ?  542 ARG D N   1 
ATOM   14911 C CA  . ARG H  2 31  ? 112.183 68.556  292.018 1.00 141.52 ?  542 ARG D CA  1 
ATOM   14912 C C   . ARG H  2 31  ? 112.104 68.645  290.498 1.00 141.80 ?  542 ARG D C   1 
ATOM   14913 O O   . ARG H  2 31  ? 113.009 68.179  289.793 1.00 140.01 ?  542 ARG D O   1 
ATOM   14914 C CB  . ARG H  2 31  ? 111.113 67.619  292.572 1.00 138.99 ?  542 ARG D CB  1 
ATOM   14915 C CG  . ARG H  2 31  ? 111.502 66.713  293.709 1.00 139.12 ?  542 ARG D CG  1 
ATOM   14916 C CD  . ARG H  2 31  ? 110.228 66.089  294.239 1.00 148.85 ?  542 ARG D CD  1 
ATOM   14917 N NE  . ARG H  2 31  ? 109.475 65.212  293.357 1.00 151.13 ?  542 ARG D NE  1 
ATOM   14918 C CZ  . ARG H  2 31  ? 108.168 65.029  293.527 1.00 152.05 ?  542 ARG D CZ  1 
ATOM   14919 N NH1 . ARG H  2 31  ? 107.562 65.667  294.522 1.00 159.70 1  542 ARG D NH1 1 
ATOM   14920 N NH2 . ARG H  2 31  ? 107.467 64.241  292.727 1.00 151.21 ?  542 ARG D NH2 1 
ATOM   14921 N N   . ASN H  2 32  ? 111.044 69.253  289.965 1.00 160.91 ?  543 ASN D N   1 
ATOM   14922 C CA  . ASN H  2 32  ? 110.889 69.352  288.520 1.00 160.92 ?  543 ASN D CA  1 
ATOM   14923 C C   . ASN H  2 32  ? 111.529 70.607  287.945 1.00 166.11 ?  543 ASN D C   1 
ATOM   14924 O O   . ASN H  2 32  ? 111.115 71.072  286.874 1.00 169.15 ?  543 ASN D O   1 
ATOM   14925 C CB  . ASN H  2 32  ? 109.415 69.266  288.130 1.00 161.89 ?  543 ASN D CB  1 
ATOM   14926 C CG  . ASN H  2 32  ? 108.744 68.033  288.688 1.00 162.66 ?  543 ASN D CG  1 
ATOM   14927 O OD1 . ASN H  2 32  ? 107.764 68.127  289.425 1.00 161.59 ?  543 ASN D OD1 1 
ATOM   14928 N ND2 . ASN H  2 32  ? 109.271 66.862  288.338 1.00 164.18 ?  543 ASN D ND2 1 
ATOM   14929 N N   . LEU H  2 33  ? 112.536 71.164  288.621 1.00 139.45 ?  544 LEU D N   1 
ATOM   14930 C CA  . LEU H  2 33  ? 113.166 72.384  288.139 1.00 140.31 ?  544 LEU D CA  1 
ATOM   14931 C C   . LEU H  2 33  ? 114.366 72.067  287.269 1.00 139.91 ?  544 LEU D C   1 
ATOM   14932 O O   . LEU H  2 33  ? 114.709 72.852  286.377 1.00 146.26 ?  544 LEU D O   1 
ATOM   14933 C CB  . LEU H  2 33  ? 113.598 73.259  289.318 1.00 145.24 ?  544 LEU D CB  1 
ATOM   14934 C CG  . LEU H  2 33  ? 113.999 74.706  289.023 1.00 155.45 ?  544 LEU D CG  1 
ATOM   14935 C CD1 . LEU H  2 33  ? 112.857 75.469  288.360 1.00 160.93 ?  544 LEU D CD1 1 
ATOM   14936 C CD2 . LEU H  2 33  ? 114.452 75.395  290.300 1.00 159.04 ?  544 LEU D CD2 1 
ATOM   14937 N N   . LEU H  2 34  ? 115.002 70.925  287.513 1.00 153.49 ?  545 LEU D N   1 
ATOM   14938 C CA  . LEU H  2 34  ? 116.138 70.448  286.738 1.00 151.81 ?  545 LEU D CA  1 
ATOM   14939 C C   . LEU H  2 34  ? 115.763 69.245  285.885 1.00 150.59 ?  545 LEU D C   1 
ATOM   14940 O O   . LEU H  2 34  ? 116.210 69.135  284.741 1.00 149.09 ?  545 LEU D O   1 
ATOM   14941 C CB  . LEU H  2 34  ? 117.313 70.113  287.662 1.00 152.06 ?  545 LEU D CB  1 
ATOM   14942 C CG  . LEU H  2 34  ? 118.599 69.665  286.981 1.00 150.50 ?  545 LEU D CG  1 
ATOM   14943 C CD1 . LEU H  2 34  ? 119.045 70.773  286.046 1.00 149.73 ?  545 LEU D CD1 1 
ATOM   14944 C CD2 . LEU H  2 34  ? 119.663 69.404  288.030 1.00 151.05 ?  545 LEU D CD2 1 
ATOM   14945 N N   . SER H  2 35  ? 114.928 68.351  286.431 1.00 178.85 ?  546 SER D N   1 
ATOM   14946 C CA  . SER H  2 35  ? 114.393 67.161  285.768 1.00 182.30 ?  546 SER D CA  1 
ATOM   14947 C C   . SER H  2 35  ? 115.450 66.243  285.159 1.00 182.70 ?  546 SER D C   1 
ATOM   14948 O O   . SER H  2 35  ? 115.659 66.249  283.941 1.00 181.55 ?  546 SER D O   1 
ATOM   14949 C CB  . SER H  2 35  ? 113.384 67.578  284.691 1.00 184.05 ?  546 SER D CB  1 
ATOM   14950 O OG  . SER H  2 35  ? 112.307 68.313  285.256 1.00 186.97 ?  546 SER D OG  1 
ATOM   14951 N N   . GLY H  2 36  ? 116.112 65.443  285.992 1.00 190.64 ?  547 GLY D N   1 
ATOM   14952 C CA  . GLY H  2 36  ? 117.128 64.523  285.512 1.00 184.73 ?  547 GLY D CA  1 
ATOM   14953 C C   . GLY H  2 36  ? 118.419 65.178  285.061 1.00 179.94 ?  547 GLY D C   1 
ATOM   14954 O O   . GLY H  2 36  ? 118.844 64.994  283.919 1.00 175.14 ?  547 GLY D O   1 
ATOM   14955 N N   . THR H  2 58  ? 123.366 68.029  262.674 1.00 179.05 ?  569 THR D N   1 
ATOM   14956 C CA  . THR H  2 58  ? 122.004 68.103  262.160 1.00 180.31 ?  569 THR D CA  1 
ATOM   14957 C C   . THR H  2 58  ? 121.161 69.035  263.019 1.00 181.59 ?  569 THR D C   1 
ATOM   14958 O O   . THR H  2 58  ? 121.169 68.938  264.248 1.00 179.89 ?  569 THR D O   1 
ATOM   14959 C CB  . THR H  2 58  ? 121.352 66.711  262.107 1.00 176.97 ?  569 THR D CB  1 
ATOM   14960 O OG1 . THR H  2 58  ? 121.334 66.138  263.424 1.00 166.60 ?  569 THR D OG1 1 
ATOM   14961 C CG2 . THR H  2 58  ? 122.115 65.796  261.155 1.00 180.68 ?  569 THR D CG2 1 
ATOM   14962 N N   . VAL H  2 59  ? 120.423 69.932  262.367 1.00 195.65 ?  570 VAL D N   1 
ATOM   14963 C CA  . VAL H  2 59  ? 119.603 70.914  263.068 1.00 200.60 ?  570 VAL D CA  1 
ATOM   14964 C C   . VAL H  2 59  ? 118.375 70.229  263.666 1.00 191.73 ?  570 VAL D C   1 
ATOM   14965 O O   . VAL H  2 59  ? 118.235 69.005  263.580 1.00 179.42 ?  570 VAL D O   1 
ATOM   14966 C CB  . VAL H  2 59  ? 119.208 72.049  262.112 1.00 210.01 ?  570 VAL D CB  1 
ATOM   14967 C CG1 . VAL H  2 59  ? 118.739 73.237  262.876 1.00 214.90 ?  570 VAL D CG1 1 
ATOM   14968 C CG2 . VAL H  2 59  ? 120.359 72.423  261.249 1.00 215.75 ?  570 VAL D CG2 1 
ATOM   14969 N N   . TRP H  2 60  ? 117.478 71.014  264.272 1.00 200.55 ?  571 TRP D N   1 
ATOM   14970 C CA  . TRP H  2 60  ? 116.245 70.560  264.912 1.00 194.04 ?  571 TRP D CA  1 
ATOM   14971 C C   . TRP H  2 60  ? 116.526 69.713  266.145 1.00 184.28 ?  571 TRP D C   1 
ATOM   14972 O O   . TRP H  2 60  ? 115.669 69.581  267.026 1.00 175.85 ?  571 TRP D O   1 
ATOM   14973 C CB  . TRP H  2 60  ? 115.374 69.767  263.937 1.00 193.28 ?  571 TRP D CB  1 
ATOM   14974 C CG  . TRP H  2 60  ? 113.943 69.712  264.346 1.00 197.51 ?  571 TRP D CG  1 
ATOM   14975 C CD1 . TRP H  2 60  ? 113.149 70.758  264.706 1.00 203.02 ?  571 TRP D CD1 1 
ATOM   14976 C CD2 . TRP H  2 60  ? 113.137 68.534  264.468 1.00 195.46 ?  571 TRP D CD2 1 
ATOM   14977 N NE1 . TRP H  2 60  ? 111.892 70.308  265.032 1.00 202.30 ?  571 TRP D NE1 1 
ATOM   14978 C CE2 . TRP H  2 60  ? 111.859 68.946  264.894 1.00 197.16 ?  571 TRP D CE2 1 
ATOM   14979 C CE3 . TRP H  2 60  ? 113.369 67.171  264.251 1.00 192.67 ?  571 TRP D CE3 1 
ATOM   14980 C CZ2 . TRP H  2 60  ? 110.818 68.047  265.103 1.00 194.44 ?  571 TRP D CZ2 1 
ATOM   14981 C CZ3 . TRP H  2 60  ? 112.335 66.280  264.464 1.00 190.85 ?  571 TRP D CZ3 1 
ATOM   14982 C CH2 . TRP H  2 60  ? 111.075 66.722  264.883 1.00 191.55 ?  571 TRP D CH2 1 
ATOM   14983 N N   . GLY H  2 61  ? 117.717 69.123  266.210 1.00 191.35 ?  572 GLY D N   1 
ATOM   14984 C CA  . GLY H  2 61  ? 118.140 68.399  267.388 1.00 182.23 ?  572 GLY D CA  1 
ATOM   14985 C C   . GLY H  2 61  ? 118.990 69.318  268.232 1.00 185.93 ?  572 GLY D C   1 
ATOM   14986 O O   . GLY H  2 61  ? 119.194 69.093  269.428 1.00 187.54 ?  572 GLY D O   1 
ATOM   14987 N N   . ILE H  2 62  ? 119.523 70.358  267.579 1.00 161.23 ?  573 ILE D N   1 
ATOM   14988 C CA  . ILE H  2 62  ? 120.288 71.394  268.265 1.00 165.72 ?  573 ILE D CA  1 
ATOM   14989 C C   . ILE H  2 62  ? 119.374 72.433  268.884 1.00 172.49 ?  573 ILE D C   1 
ATOM   14990 O O   . ILE H  2 62  ? 119.819 73.247  269.702 1.00 178.49 ?  573 ILE D O   1 
ATOM   14991 C CB  . ILE H  2 62  ? 121.249 72.055  267.260 1.00 176.02 ?  573 ILE D CB  1 
ATOM   14992 C CG1 . ILE H  2 62  ? 122.334 72.855  267.982 1.00 181.34 ?  573 ILE D CG1 1 
ATOM   14993 C CG2 . ILE H  2 62  ? 120.456 72.955  266.288 1.00 181.25 ?  573 ILE D CG2 1 
ATOM   14994 C CD1 . ILE H  2 62  ? 123.305 73.523  267.040 1.00 183.43 ?  573 ILE D CD1 1 
ATOM   14995 N N   . LYS H  2 63  ? 118.094 72.401  268.527 1.00 166.60 ?  574 LYS D N   1 
ATOM   14996 C CA  . LYS H  2 63  ? 117.131 73.336  269.090 1.00 172.53 ?  574 LYS D CA  1 
ATOM   14997 C C   . LYS H  2 63  ? 116.979 73.109  270.588 1.00 169.96 ?  574 LYS D C   1 
ATOM   14998 O O   . LYS H  2 63  ? 116.817 74.062  271.357 1.00 176.45 ?  574 LYS D O   1 
ATOM   14999 C CB  . LYS H  2 63  ? 115.789 73.219  268.369 1.00 173.58 ?  574 LYS D CB  1 
ATOM   15000 C CG  . LYS H  2 63  ? 114.908 74.472  268.465 1.00 175.26 ?  574 LYS D CG  1 
ATOM   15001 C CD  . LYS H  2 63  ? 115.430 75.615  267.581 1.00 183.61 ?  574 LYS D CD  1 
ATOM   15002 C CE  . LYS H  2 63  ? 114.449 76.788  267.540 1.00 177.03 ?  574 LYS D CE  1 
ATOM   15003 N NZ  . LYS H  2 63  ? 114.910 77.882  266.632 1.00 182.83 1  574 LYS D NZ  1 
ATOM   15004 N N   . GLN H  2 64  ? 117.010 71.847  271.013 1.00 176.08 ?  575 GLN D N   1 
ATOM   15005 C CA  . GLN H  2 64  ? 116.841 71.453  272.407 1.00 171.07 ?  575 GLN D CA  1 
ATOM   15006 C C   . GLN H  2 64  ? 118.130 71.490  273.217 1.00 174.74 ?  575 GLN D C   1 
ATOM   15007 O O   . GLN H  2 64  ? 118.064 71.607  274.447 1.00 178.70 ?  575 GLN D O   1 
ATOM   15008 C CB  . GLN H  2 64  ? 116.267 70.034  272.483 1.00 161.35 ?  575 GLN D CB  1 
ATOM   15009 C CG  . GLN H  2 64  ? 117.079 68.988  271.717 1.00 157.91 ?  575 GLN D CG  1 
ATOM   15010 C CD  . GLN H  2 64  ? 118.214 68.393  272.548 1.00 155.45 ?  575 GLN D CD  1 
ATOM   15011 O OE1 . GLN H  2 64  ? 118.223 68.506  273.773 1.00 157.96 ?  575 GLN D OE1 1 
ATOM   15012 N NE2 . GLN H  2 64  ? 119.179 67.765  271.879 1.00 155.59 ?  575 GLN D NE2 1 
ATOM   15013 N N   . LEU H  2 65  ? 119.290 71.368  272.568 1.00 142.44 ?  576 LEU D N   1 
ATOM   15014 C CA  . LEU H  2 65  ? 120.559 71.378  273.290 1.00 143.10 ?  576 LEU D CA  1 
ATOM   15015 C C   . LEU H  2 65  ? 120.808 72.715  273.981 1.00 149.92 ?  576 LEU D C   1 
ATOM   15016 O O   . LEU H  2 65  ? 121.077 72.761  275.186 1.00 145.27 ?  576 LEU D O   1 
ATOM   15017 C CB  . LEU H  2 65  ? 121.693 71.066  272.314 1.00 146.04 ?  576 LEU D CB  1 
ATOM   15018 C CG  . LEU H  2 65  ? 123.099 70.905  272.887 1.00 143.86 ?  576 LEU D CG  1 
ATOM   15019 C CD1 . LEU H  2 65  ? 123.829 69.806  272.157 1.00 145.28 ?  576 LEU D CD1 1 
ATOM   15020 C CD2 . LEU H  2 65  ? 123.882 72.206  272.778 1.00 148.95 ?  576 LEU D CD2 1 
ATOM   15021 N N   . GLN H  2 66  ? 120.730 73.816  273.235 1.00 148.59 ?  577 GLN D N   1 
ATOM   15022 C CA  . GLN H  2 66  ? 120.955 75.137  273.819 1.00 156.52 ?  577 GLN D CA  1 
ATOM   15023 C C   . GLN H  2 66  ? 119.904 75.499  274.869 1.00 155.76 ?  577 GLN D C   1 
ATOM   15024 O O   . GLN H  2 66  ? 120.152 76.381  275.700 1.00 161.99 ?  577 GLN D O   1 
ATOM   15025 C CB  . GLN H  2 66  ? 121.093 76.202  272.735 1.00 171.48 ?  577 GLN D CB  1 
ATOM   15026 C CG  . GLN H  2 66  ? 119.852 76.771  272.131 1.00 179.56 ?  577 GLN D CG  1 
ATOM   15027 C CD  . GLN H  2 66  ? 120.213 77.905  271.191 1.00 194.17 ?  577 GLN D CD  1 
ATOM   15028 O OE1 . GLN H  2 66  ? 121.390 78.249  271.044 1.00 196.68 ?  577 GLN D OE1 1 
ATOM   15029 N NE2 . GLN H  2 66  ? 119.213 78.479  270.538 1.00 204.40 ?  577 GLN D NE2 1 
ATOM   15030 N N   . ALA H  2 67  ? 118.746 74.833  274.854 1.00 169.81 ?  578 ALA D N   1 
ATOM   15031 C CA  . ALA H  2 67  ? 117.676 75.088  275.816 1.00 161.37 ?  578 ALA D CA  1 
ATOM   15032 C C   . ALA H  2 67  ? 117.999 74.384  277.121 1.00 149.54 ?  578 ALA D C   1 
ATOM   15033 O O   . ALA H  2 67  ? 117.788 74.939  278.206 1.00 150.06 ?  578 ALA D O   1 
ATOM   15034 C CB  . ALA H  2 67  ? 116.334 74.607  275.266 1.00 155.45 ?  578 ALA D CB  1 
ATOM   15035 N N   . ARG H  2 68  ? 118.518 73.165  277.029 1.00 159.92 ?  579 ARG D N   1 
ATOM   15036 C CA  . ARG H  2 68  ? 118.862 72.395  278.208 1.00 150.08 ?  579 ARG D CA  1 
ATOM   15037 C C   . ARG H  2 68  ? 120.169 72.916  278.796 1.00 154.21 ?  579 ARG D C   1 
ATOM   15038 O O   . ARG H  2 68  ? 120.519 72.563  279.929 1.00 150.14 ?  579 ARG D O   1 
ATOM   15039 C CB  . ARG H  2 68  ? 118.833 70.905  277.823 1.00 140.85 ?  579 ARG D CB  1 
ATOM   15040 C CG  . ARG H  2 68  ? 119.917 70.372  276.895 1.00 144.88 ?  579 ARG D CG  1 
ATOM   15041 C CD  . ARG H  2 68  ? 119.729 68.858  276.726 1.00 142.31 ?  579 ARG D CD  1 
ATOM   15042 N NE  . ARG H  2 68  ? 120.760 68.224  275.906 1.00 142.28 ?  579 ARG D NE  1 
ATOM   15043 C CZ  . ARG H  2 68  ? 121.422 67.117  276.224 1.00 130.57 ?  579 ARG D CZ  1 
ATOM   15044 N NH1 . ARG H  2 68  ? 121.171 66.489  277.366 1.00 119.82 1  579 ARG D NH1 1 
ATOM   15045 N NH2 . ARG H  2 68  ? 122.331 66.633  275.385 1.00 130.67 ?  579 ARG D NH2 1 
ATOM   15046 N N   . VAL H  2 69  ? 120.891 73.743  278.030 1.00 132.33 ?  580 VAL D N   1 
ATOM   15047 C CA  . VAL H  2 69  ? 122.050 74.461  278.548 1.00 132.33 ?  580 VAL D CA  1 
ATOM   15048 C C   . VAL H  2 69  ? 121.561 75.645  279.377 1.00 131.16 ?  580 VAL D C   1 
ATOM   15049 O O   . VAL H  2 69  ? 122.087 75.932  280.456 1.00 130.42 ?  580 VAL D O   1 
ATOM   15050 C CB  . VAL H  2 69  ? 122.973 74.913  277.398 1.00 133.96 ?  580 VAL D CB  1 
ATOM   15051 C CG1 . VAL H  2 69  ? 123.910 76.014  277.864 1.00 134.08 ?  580 VAL D CG1 1 
ATOM   15052 C CG2 . VAL H  2 69  ? 123.779 73.738  276.861 1.00 135.10 ?  580 VAL D CG2 1 
ATOM   15053 N N   . LEU H  2 70  ? 120.530 76.344  278.880 1.00 143.48 ?  581 LEU D N   1 
ATOM   15054 C CA  . LEU H  2 70  ? 119.931 77.446  279.624 1.00 148.15 ?  581 LEU D CA  1 
ATOM   15055 C C   . LEU H  2 70  ? 119.207 76.937  280.863 1.00 142.00 ?  581 LEU D C   1 
ATOM   15056 O O   . LEU H  2 70  ? 119.029 77.691  281.827 1.00 144.67 ?  581 LEU D O   1 
ATOM   15057 C CB  . LEU H  2 70  ? 118.972 78.222  278.713 1.00 155.96 ?  581 LEU D CB  1 
ATOM   15058 C CG  . LEU H  2 70  ? 118.261 79.477  279.229 1.00 163.29 ?  581 LEU D CG  1 
ATOM   15059 C CD1 . LEU H  2 70  ? 119.212 80.663  279.312 1.00 177.58 ?  581 LEU D CD1 1 
ATOM   15060 C CD2 . LEU H  2 70  ? 117.049 79.809  278.362 1.00 167.31 ?  581 LEU D CD2 1 
ATOM   15061 N N   . ALA H  2 71  ? 118.796 75.664  280.851 1.00 151.55 ?  582 ALA D N   1 
ATOM   15062 C CA  . ALA H  2 71  ? 118.100 75.079  281.990 1.00 144.60 ?  582 ALA D CA  1 
ATOM   15063 C C   . ALA H  2 71  ? 119.047 74.968  283.172 1.00 140.66 ?  582 ALA D C   1 
ATOM   15064 O O   . ALA H  2 71  ? 118.675 75.262  284.313 1.00 140.38 ?  582 ALA D O   1 
ATOM   15065 C CB  . ALA H  2 71  ? 117.521 73.714  281.628 1.00 136.44 ?  582 ALA D CB  1 
ATOM   15066 N N   . VAL H  2 72  ? 120.287 74.552  282.905 1.00 131.48 ?  583 VAL D N   1 
ATOM   15067 C CA  . VAL H  2 72  ? 121.268 74.401  283.968 1.00 126.50 ?  583 VAL D CA  1 
ATOM   15068 C C   . VAL H  2 72  ? 121.876 75.748  284.320 1.00 133.21 ?  583 VAL D C   1 
ATOM   15069 O O   . VAL H  2 72  ? 122.355 75.925  285.446 1.00 131.75 ?  583 VAL D O   1 
ATOM   15070 C CB  . VAL H  2 72  ? 122.362 73.390  283.588 1.00 119.98 ?  583 VAL D CB  1 
ATOM   15071 C CG1 . VAL H  2 72  ? 121.744 72.026  283.322 1.00 113.52 ?  583 VAL D CG1 1 
ATOM   15072 C CG2 . VAL H  2 72  ? 123.156 73.873  282.392 1.00 125.10 ?  583 VAL D CG2 1 
ATOM   15073 N N   . GLU H  2 73  ? 121.870 76.705  283.386 1.00 124.57 ?  584 GLU D N   1 
ATOM   15074 C CA  . GLU H  2 73  ? 122.358 78.037  283.720 1.00 132.89 ?  584 GLU D CA  1 
ATOM   15075 C C   . GLU H  2 73  ? 121.374 78.730  284.648 1.00 136.77 ?  584 GLU D C   1 
ATOM   15076 O O   . GLU H  2 73  ? 121.772 79.494  285.533 1.00 139.08 ?  584 GLU D O   1 
ATOM   15077 C CB  . GLU H  2 73  ? 122.518 78.887  282.461 1.00 141.96 ?  584 GLU D CB  1 
ATOM   15078 C CG  . GLU H  2 73  ? 123.629 78.526  281.506 1.00 144.80 ?  584 GLU D CG  1 
ATOM   15079 C CD  . GLU H  2 73  ? 123.643 79.456  280.301 1.00 159.58 ?  584 GLU D CD  1 
ATOM   15080 O OE1 . GLU H  2 73  ? 122.629 80.156  280.082 1.00 162.06 ?  584 GLU D OE1 1 
ATOM   15081 O OE2 . GLU H  2 73  ? 124.658 79.487  279.574 1.00 168.11 -1 584 GLU D OE2 1 
ATOM   15082 N N   . ARG H  2 74  ? 120.078 78.472  284.449 1.00 145.78 ?  585 ARG D N   1 
ATOM   15083 C CA  . ARG H  2 74  ? 119.056 79.032  285.323 1.00 148.68 ?  585 ARG D CA  1 
ATOM   15084 C C   . ARG H  2 74  ? 119.091 78.364  286.691 1.00 141.11 ?  585 ARG D C   1 
ATOM   15085 O O   . ARG H  2 74  ? 118.772 78.998  287.703 1.00 144.01 ?  585 ARG D O   1 
ATOM   15086 C CB  . ARG H  2 74  ? 117.683 78.940  284.654 1.00 149.49 ?  585 ARG D CB  1 
ATOM   15087 C CG  . ARG H  2 74  ? 116.550 79.491  285.489 1.00 152.01 ?  585 ARG D CG  1 
ATOM   15088 C CD  . ARG H  2 74  ? 115.610 80.245  284.574 1.00 157.32 ?  585 ARG D CD  1 
ATOM   15089 N NE  . ARG H  2 74  ? 114.499 80.856  285.289 1.00 159.88 ?  585 ARG D NE  1 
ATOM   15090 C CZ  . ARG H  2 74  ? 113.501 81.495  284.690 1.00 163.00 ?  585 ARG D CZ  1 
ATOM   15091 N NH1 . ARG H  2 74  ? 113.488 81.606  283.369 1.00 163.87 1  585 ARG D NH1 1 
ATOM   15092 N NH2 . ARG H  2 74  ? 112.527 82.033  285.409 1.00 164.69 ?  585 ARG D NH2 1 
ATOM   15093 N N   . TYR H  2 75  ? 119.465 77.084  286.740 1.00 157.56 ?  586 TYR D N   1 
ATOM   15094 C CA  . TYR H  2 75  ? 119.521 76.390  288.019 1.00 149.74 ?  586 TYR D CA  1 
ATOM   15095 C C   . TYR H  2 75  ? 120.714 76.862  288.838 1.00 151.14 ?  586 TYR D C   1 
ATOM   15096 O O   . TYR H  2 75  ? 120.568 77.222  290.012 1.00 152.00 ?  586 TYR D O   1 
ATOM   15097 C CB  . TYR H  2 75  ? 119.595 74.880  287.789 1.00 138.55 ?  586 TYR D CB  1 
ATOM   15098 C CG  . TYR H  2 75  ? 119.767 74.068  289.056 1.00 130.49 ?  586 TYR D CG  1 
ATOM   15099 C CD1 . TYR H  2 75  ? 118.688 73.801  289.891 1.00 127.86 ?  586 TYR D CD1 1 
ATOM   15100 C CD2 . TYR H  2 75  ? 121.011 73.557  289.413 1.00 125.38 ?  586 TYR D CD2 1 
ATOM   15101 C CE1 . TYR H  2 75  ? 118.845 73.050  291.057 1.00 120.86 ?  586 TYR D CE1 1 
ATOM   15102 C CE2 . TYR H  2 75  ? 121.179 72.805  290.573 1.00 118.04 ?  586 TYR D CE2 1 
ATOM   15103 C CZ  . TYR H  2 75  ? 120.094 72.554  291.393 1.00 116.03 ?  586 TYR D CZ  1 
ATOM   15104 O OH  . TYR H  2 75  ? 120.263 71.809  292.544 1.00 109.08 ?  586 TYR D OH  1 
ATOM   15105 N N   . LEU H  2 76  ? 121.908 76.872  288.236 1.00 122.90 ?  587 LEU D N   1 
ATOM   15106 C CA  . LEU H  2 76  ? 123.090 77.304  288.976 1.00 123.34 ?  587 LEU D CA  1 
ATOM   15107 C C   . LEU H  2 76  ? 123.048 78.790  289.301 1.00 132.76 ?  587 LEU D C   1 
ATOM   15108 O O   . LEU H  2 76  ? 123.676 79.220  290.276 1.00 132.19 ?  587 LEU D O   1 
ATOM   15109 C CB  . LEU H  2 76  ? 124.360 76.945  288.211 1.00 123.97 ?  587 LEU D CB  1 
ATOM   15110 C CG  . LEU H  2 76  ? 124.534 75.428  288.142 1.00 122.00 ?  587 LEU D CG  1 
ATOM   15111 C CD1 . LEU H  2 76  ? 125.834 75.040  287.471 1.00 122.70 ?  587 LEU D CD1 1 
ATOM   15112 C CD2 . LEU H  2 76  ? 124.454 74.828  289.536 1.00 120.70 ?  587 LEU D CD2 1 
ATOM   15113 N N   . ARG H  2 77  ? 122.329 79.589  288.507 1.00 140.56 ?  588 ARG D N   1 
ATOM   15114 C CA  . ARG H  2 77  ? 122.205 81.007  288.829 1.00 150.31 ?  588 ARG D CA  1 
ATOM   15115 C C   . ARG H  2 77  ? 121.481 81.154  290.160 1.00 149.78 ?  588 ARG D C   1 
ATOM   15116 O O   . ARG H  2 77  ? 121.915 81.901  291.044 1.00 151.47 ?  588 ARG D O   1 
ATOM   15117 C CB  . ARG H  2 77  ? 121.514 81.796  287.702 1.00 159.08 ?  588 ARG D CB  1 
ATOM   15118 C CG  . ARG H  2 77  ? 119.992 81.946  287.778 1.00 160.98 ?  588 ARG D CG  1 
ATOM   15119 C CD  . ARG H  2 77  ? 119.440 82.851  286.680 1.00 174.67 ?  588 ARG D CD  1 
ATOM   15120 N NE  . ARG H  2 77  ? 117.977 82.889  286.685 1.00 179.34 ?  588 ARG D NE  1 
ATOM   15121 C CZ  . ARG H  2 77  ? 117.255 83.884  287.191 1.00 181.89 ?  588 ARG D CZ  1 
ATOM   15122 N NH1 . ARG H  2 77  ? 117.856 84.931  287.737 1.00 189.31 1  588 ARG D NH1 1 
ATOM   15123 N NH2 . ARG H  2 77  ? 115.930 83.834  287.152 1.00 177.25 ?  588 ARG D NH2 1 
ATOM   15124 N N   . ASP H  2 78  ? 120.359 80.445  290.312 1.00 155.95 ?  589 ASP D N   1 
ATOM   15125 C CA  . ASP H  2 78  ? 119.621 80.479  291.564 1.00 154.86 ?  589 ASP D CA  1 
ATOM   15126 C C   . ASP H  2 78  ? 120.410 79.786  292.672 1.00 147.11 ?  589 ASP D C   1 
ATOM   15127 O O   . ASP H  2 78  ? 120.365 80.210  293.832 1.00 147.97 ?  589 ASP D O   1 
ATOM   15128 C CB  . ASP H  2 78  ? 118.256 79.816  291.368 1.00 150.98 ?  589 ASP D CB  1 
ATOM   15129 C CG  . ASP H  2 78  ? 117.316 80.643  290.490 1.00 158.19 ?  589 ASP D CG  1 
ATOM   15130 O OD1 . ASP H  2 78  ? 117.400 81.891  290.495 1.00 166.79 ?  589 ASP D OD1 1 
ATOM   15131 O OD2 . ASP H  2 78  ? 116.492 80.030  289.777 1.00 154.73 -1 589 ASP D OD2 1 
ATOM   15132 N N   . GLN H  2 79  ? 121.147 78.721  292.331 1.00 155.19 ?  590 GLN D N   1 
ATOM   15133 C CA  . GLN H  2 79  ? 121.947 78.020  293.333 1.00 146.83 ?  590 GLN D CA  1 
ATOM   15134 C C   . GLN H  2 79  ? 123.115 78.872  293.807 1.00 149.87 ?  590 GLN D C   1 
ATOM   15135 O O   . GLN H  2 79  ? 123.526 78.773  294.969 1.00 145.99 ?  590 GLN D O   1 
ATOM   15136 C CB  . GLN H  2 79  ? 122.473 76.703  292.767 1.00 137.05 ?  590 GLN D CB  1 
ATOM   15137 C CG  . GLN H  2 79  ? 121.442 75.599  292.649 1.00 127.00 ?  590 GLN D CG  1 
ATOM   15138 C CD  . GLN H  2 79  ? 120.909 75.159  293.997 1.00 128.26 ?  590 GLN D CD  1 
ATOM   15139 O OE1 . GLN H  2 79  ? 119.742 74.785  294.128 1.00 133.27 ?  590 GLN D OE1 1 
ATOM   15140 N NE2 . GLN H  2 79  ? 121.764 75.205  295.013 1.00 123.25 ?  590 GLN D NE2 1 
ATOM   15141 N N   . GLN H  2 80  ? 123.661 79.708  292.922 1.00 135.44 ?  591 GLN D N   1 
ATOM   15142 C CA  . GLN H  2 80  ? 124.750 80.593  293.319 1.00 138.76 ?  591 GLN D CA  1 
ATOM   15143 C C   . GLN H  2 80  ? 124.229 81.664  294.268 1.00 145.33 ?  591 GLN D C   1 
ATOM   15144 O O   . GLN H  2 80  ? 124.883 81.987  295.266 1.00 144.03 ?  591 GLN D O   1 
ATOM   15145 C CB  . GLN H  2 80  ? 125.439 81.190  292.093 1.00 144.40 ?  591 GLN D CB  1 
ATOM   15146 C CG  . GLN H  2 80  ? 126.705 81.984  292.410 1.00 142.23 ?  591 GLN D CG  1 
ATOM   15147 C CD  . GLN H  2 80  ? 127.293 82.640  291.174 1.00 148.05 ?  591 GLN D CD  1 
ATOM   15148 O OE1 . GLN H  2 80  ? 126.614 82.792  290.159 1.00 154.90 ?  591 GLN D OE1 1 
ATOM   15149 N NE2 . GLN H  2 80  ? 128.583 82.980  291.234 1.00 145.65 ?  591 GLN D NE2 1 
ATOM   15150 N N   . LEU H  2 81  ? 123.065 82.245  293.955 1.00 149.09 ?  592 LEU D N   1 
ATOM   15151 C CA  . LEU H  2 81  ? 122.436 83.207  294.856 1.00 155.24 ?  592 LEU D CA  1 
ATOM   15152 C C   . LEU H  2 81  ? 122.087 82.546  296.184 1.00 150.34 ?  592 LEU D C   1 
ATOM   15153 O O   . LEU H  2 81  ? 122.244 83.150  297.252 1.00 153.42 ?  592 LEU D O   1 
ATOM   15154 C CB  . LEU H  2 81  ? 121.174 83.783  294.212 1.00 162.16 ?  592 LEU D CB  1 
ATOM   15155 C CG  . LEU H  2 81  ? 121.306 84.582  292.918 1.00 169.14 ?  592 LEU D CG  1 
ATOM   15156 C CD1 . LEU H  2 81  ? 119.943 85.083  292.478 1.00 175.15 ?  592 LEU D CD1 1 
ATOM   15157 C CD2 . LEU H  2 81  ? 122.254 85.750  293.111 1.00 176.88 ?  592 LEU D CD2 1 
ATOM   15158 N N   . LEU H  2 82  ? 121.599 81.304  296.130 1.00 157.55 ?  593 LEU D N   1 
ATOM   15159 C CA  . LEU H  2 82  ? 121.236 80.561  297.330 1.00 151.14 ?  593 LEU D CA  1 
ATOM   15160 C C   . LEU H  2 82  ? 122.451 80.208  298.177 1.00 145.13 ?  593 LEU D C   1 
ATOM   15161 O O   . LEU H  2 82  ? 122.301 79.942  299.374 1.00 142.06 ?  593 LEU D O   1 
ATOM   15162 C CB  . LEU H  2 82  ? 120.488 79.287  296.937 1.00 143.92 ?  593 LEU D CB  1 
ATOM   15163 C CG  . LEU H  2 82  ? 119.573 78.645  297.976 1.00 139.26 ?  593 LEU D CG  1 
ATOM   15164 C CD1 . LEU H  2 82  ? 118.469 79.604  298.380 1.00 147.07 ?  593 LEU D CD1 1 
ATOM   15165 C CD2 . LEU H  2 82  ? 118.996 77.343  297.434 1.00 131.39 ?  593 LEU D CD2 1 
ATOM   15166 N N   . GLY H  2 83  ? 123.648 80.232  297.591 1.00 161.23 ?  594 GLY D N   1 
ATOM   15167 C CA  . GLY H  2 83  ? 124.874 79.897  298.290 1.00 154.99 ?  594 GLY D CA  1 
ATOM   15168 C C   . GLY H  2 83  ? 125.562 81.109  298.885 1.00 162.76 ?  594 GLY D C   1 
ATOM   15169 O O   . GLY H  2 83  ? 126.051 81.050  300.017 1.00 166.23 ?  594 GLY D O   1 
ATOM   15170 N N   . ILE H  2 84  ? 125.620 82.214  298.134 1.00 147.70 ?  595 ILE D N   1 
ATOM   15171 C CA  . ILE H  2 84  ? 126.282 83.411  298.640 1.00 153.72 ?  595 ILE D CA  1 
ATOM   15172 C C   . ILE H  2 84  ? 125.478 84.038  299.764 1.00 162.75 ?  595 ILE D C   1 
ATOM   15173 O O   . ILE H  2 84  ? 126.026 84.816  300.557 1.00 173.11 ?  595 ILE D O   1 
ATOM   15174 C CB  . ILE H  2 84  ? 126.509 84.429  297.510 1.00 161.95 ?  595 ILE D CB  1 
ATOM   15175 C CG1 . ILE H  2 84  ? 125.172 84.832  296.893 1.00 171.72 ?  595 ILE D CG1 1 
ATOM   15176 C CG2 . ILE H  2 84  ? 127.463 83.875  296.463 1.00 157.32 ?  595 ILE D CG2 1 
ATOM   15177 C CD1 . ILE H  2 84  ? 125.323 85.710  295.691 1.00 181.66 ?  595 ILE D CD1 1 
ATOM   15178 N N   . TRP H  2 85  ? 124.182 83.733  299.848 1.00 162.14 ?  596 TRP D N   1 
ATOM   15179 C CA  . TRP H  2 85  ? 123.381 84.191  300.970 1.00 170.45 ?  596 TRP D CA  1 
ATOM   15180 C C   . TRP H  2 85  ? 123.638 83.262  302.151 1.00 162.33 ?  596 TRP D C   1 
ATOM   15181 O O   . TRP H  2 85  ? 124.389 82.286  302.049 1.00 151.42 ?  596 TRP D O   1 
ATOM   15182 C CB  . TRP H  2 85  ? 121.898 84.210  300.592 1.00 169.83 ?  596 TRP D CB  1 
ATOM   15183 C CG  . TRP H  2 85  ? 121.579 85.145  299.481 1.00 180.54 ?  596 TRP D CG  1 
ATOM   15184 C CD1 . TRP H  2 85  ? 122.368 86.140  299.001 1.00 190.75 ?  596 TRP D CD1 1 
ATOM   15185 C CD2 . TRP H  2 85  ? 120.389 85.155  298.683 1.00 180.93 ?  596 TRP D CD2 1 
ATOM   15186 N NE1 . TRP H  2 85  ? 121.743 86.783  297.961 1.00 195.65 ?  596 TRP D NE1 1 
ATOM   15187 C CE2 . TRP H  2 85  ? 120.526 86.196  297.745 1.00 189.62 ?  596 TRP D CE2 1 
ATOM   15188 C CE3 . TRP H  2 85  ? 119.219 84.389  298.675 1.00 178.22 ?  596 TRP D CE3 1 
ATOM   15189 C CZ2 . TRP H  2 85  ? 119.539 86.494  296.807 1.00 190.56 ?  596 TRP D CZ2 1 
ATOM   15190 C CZ3 . TRP H  2 85  ? 118.238 84.687  297.741 1.00 181.41 ?  596 TRP D CZ3 1 
ATOM   15191 C CH2 . TRP H  2 85  ? 118.405 85.730  296.821 1.00 187.02 ?  596 TRP D CH2 1 
ATOM   15192 N N   . GLY H  2 86  ? 122.993 83.536  303.281 1.00 178.59 ?  597 GLY D N   1 
ATOM   15193 C CA  . GLY H  2 86  ? 123.150 82.645  304.419 1.00 175.11 ?  597 GLY D CA  1 
ATOM   15194 C C   . GLY H  2 86  ? 122.262 81.428  304.362 1.00 166.69 ?  597 GLY D C   1 
ATOM   15195 O O   . GLY H  2 86  ? 121.546 81.129  305.319 1.00 171.27 ?  597 GLY D O   1 
ATOM   15196 N N   . CYS H  2 87  ? 122.323 80.701  303.250 1.00 151.70 ?  598 CYS D N   1 
ATOM   15197 C CA  . CYS H  2 87  ? 121.443 79.553  303.057 1.00 142.14 ?  598 CYS D CA  1 
ATOM   15198 C C   . CYS H  2 87  ? 122.259 78.349  302.586 1.00 130.50 ?  598 CYS D C   1 
ATOM   15199 O O   . CYS H  2 87  ? 122.574 77.452  303.372 1.00 126.20 ?  598 CYS D O   1 
ATOM   15200 C CB  . CYS H  2 87  ? 120.366 79.873  302.017 1.00 147.00 ?  598 CYS D CB  1 
ATOM   15201 S SG  . CYS H  2 87  ? 119.298 81.317  302.250 1.00 159.86 ?  598 CYS D SG  1 
ATOM   15202 N N   . SER H  2 88  ? 122.613 78.341  301.293 1.00 151.63 ?  599 SER D N   1 
ATOM   15203 C CA  . SER H  2 88  ? 123.276 77.209  300.651 1.00 140.55 ?  599 SER D CA  1 
ATOM   15204 C C   . SER H  2 88  ? 122.371 75.982  300.744 1.00 132.30 ?  599 SER D C   1 
ATOM   15205 O O   . SER H  2 88  ? 121.933 75.439  299.721 1.00 128.80 ?  599 SER D O   1 
ATOM   15206 C CB  . SER H  2 88  ? 124.654 76.949  301.269 1.00 138.47 ?  599 SER D CB  1 
ATOM   15207 O OG  . SER H  2 88  ? 125.314 75.886  300.603 1.00 127.11 ?  599 SER D OG  1 
ATOM   15208 N N   . GLY H  2 89  ? 122.118 75.520  301.966 1.00 123.34 ?  600 GLY D N   1 
ATOM   15209 C CA  . GLY H  2 89  ? 121.129 74.490  302.225 1.00 116.37 ?  600 GLY D CA  1 
ATOM   15210 C C   . GLY H  2 89  ? 119.783 74.993  301.739 1.00 123.81 ?  600 GLY D C   1 
ATOM   15211 O O   . GLY H  2 89  ? 119.304 76.035  302.198 1.00 134.11 ?  600 GLY D O   1 
ATOM   15212 N N   . LYS H  2 90  ? 119.159 74.264  300.815 1.00 123.73 ?  601 LYS D N   1 
ATOM   15213 C CA  . LYS H  2 90  ? 117.968 74.749  300.125 1.00 135.70 ?  601 LYS D CA  1 
ATOM   15214 C C   . LYS H  2 90  ? 116.693 74.833  300.966 1.00 135.46 ?  601 LYS D C   1 
ATOM   15215 O O   . LYS H  2 90  ? 116.748 74.864  302.201 1.00 132.10 ?  601 LYS D O   1 
ATOM   15216 C CB  . LYS H  2 90  ? 117.702 73.864  298.901 1.00 129.20 ?  601 LYS D CB  1 
ATOM   15217 C CG  . LYS H  2 90  ? 118.920 73.639  298.001 1.00 120.24 ?  601 LYS D CG  1 
ATOM   15218 C CD  . LYS H  2 90  ? 118.666 72.538  296.981 1.00 113.29 ?  601 LYS D CD  1 
ATOM   15219 C CE  . LYS H  2 90  ? 119.921 72.201  296.189 1.00 108.25 ?  601 LYS D CE  1 
ATOM   15220 N NZ  . LYS H  2 90  ? 121.125 72.017  297.049 1.00 102.56 1  601 LYS D NZ  1 
ATOM   15221 N N   . LEU H  2 91  ? 115.539 74.860  300.281 1.00 144.80 ?  602 LEU D N   1 
ATOM   15222 C CA  . LEU H  2 91  ? 114.196 74.966  300.856 1.00 142.91 ?  602 LEU D CA  1 
ATOM   15223 C C   . LEU H  2 91  ? 113.962 76.237  301.667 1.00 151.14 ?  602 LEU D C   1 
ATOM   15224 O O   . LEU H  2 91  ? 113.415 77.211  301.139 1.00 159.14 ?  602 LEU D O   1 
ATOM   15225 C CB  . LEU H  2 91  ? 113.852 73.731  301.693 1.00 130.86 ?  602 LEU D CB  1 
ATOM   15226 C CG  . LEU H  2 91  ? 113.872 72.456  300.850 1.00 128.58 ?  602 LEU D CG  1 
ATOM   15227 C CD1 . LEU H  2 91  ? 113.371 71.244  301.625 1.00 127.91 ?  602 LEU D CD1 1 
ATOM   15228 C CD2 . LEU H  2 91  ? 113.031 72.665  299.591 1.00 133.19 ?  602 LEU D CD2 1 
ATOM   15229 N N   . ILE H  2 92  ? 114.339 76.251  302.948 1.00 146.31 ?  603 ILE D N   1 
ATOM   15230 C CA  . ILE H  2 92  ? 114.115 77.422  303.795 1.00 153.63 ?  603 ILE D CA  1 
ATOM   15231 C C   . ILE H  2 92  ? 115.384 77.802  304.546 1.00 162.11 ?  603 ILE D C   1 
ATOM   15232 O O   . ILE H  2 92  ? 116.231 76.952  304.838 1.00 161.11 ?  603 ILE D O   1 
ATOM   15233 C CB  . ILE H  2 92  ? 112.953 77.177  304.793 1.00 145.38 ?  603 ILE D CB  1 
ATOM   15234 C CG1 . ILE H  2 92  ? 113.210 75.952  305.672 1.00 136.14 ?  603 ILE D CG1 1 
ATOM   15235 C CG2 . ILE H  2 92  ? 111.657 76.985  304.048 1.00 143.15 ?  603 ILE D CG2 1 
ATOM   15236 C CD1 . ILE H  2 92  ? 113.685 76.299  307.063 1.00 141.82 ?  603 ILE D CD1 1 
ATOM   15237 N N   . CYS H  2 93  ? 115.514 79.099  304.844 1.00 128.48 ?  604 CYS D N   1 
ATOM   15238 C CA  . CYS H  2 93  ? 116.627 79.582  305.644 1.00 137.03 ?  604 CYS D CA  1 
ATOM   15239 C C   . CYS H  2 93  ? 116.262 80.981  306.147 1.00 151.39 ?  604 CYS D C   1 
ATOM   15240 O O   . CYS H  2 93  ? 115.536 81.723  305.485 1.00 156.38 ?  604 CYS D O   1 
ATOM   15241 C CB  . CYS H  2 93  ? 117.931 79.650  304.805 1.00 144.77 ?  604 CYS D CB  1 
ATOM   15242 S SG  . CYS H  2 93  ? 117.968 81.196  303.814 1.00 170.60 ?  604 CYS D SG  1 
ATOM   15243 N N   . CYS H  2 94  ? 116.740 81.325  307.343 1.00 155.65 ?  605 CYS D N   1 
ATOM   15244 C CA  . CYS H  2 94  ? 116.489 82.628  307.951 1.00 165.61 ?  605 CYS D CA  1 
ATOM   15245 C C   . CYS H  2 94  ? 117.696 83.550  307.712 1.00 173.58 ?  605 CYS D C   1 
ATOM   15246 O O   . CYS H  2 94  ? 118.770 83.098  307.310 1.00 168.80 ?  605 CYS D O   1 
ATOM   15247 C CB  . CYS H  2 94  ? 116.100 82.430  309.428 1.00 161.49 ?  605 CYS D CB  1 
ATOM   15248 S SG  . CYS H  2 94  ? 114.476 81.521  309.578 1.00 152.10 ?  605 CYS D SG  1 
ATOM   15249 N N   . THR H  2 95  ? 117.494 84.854  307.890 1.00 165.25 ?  606 THR D N   1 
ATOM   15250 C CA  . THR H  2 95  ? 118.550 85.835  307.691 1.00 172.34 ?  606 THR D CA  1 
ATOM   15251 C C   . THR H  2 95  ? 118.421 86.922  308.741 1.00 180.29 ?  606 THR D C   1 
ATOM   15252 O O   . THR H  2 95  ? 117.356 87.116  309.333 1.00 181.03 ?  606 THR D O   1 
ATOM   15253 C CB  . THR H  2 95  ? 118.497 86.473  306.290 1.00 178.16 ?  606 THR D CB  1 
ATOM   15254 O OG1 . THR H  2 95  ? 118.055 85.506  305.345 1.00 172.24 ?  606 THR D OG1 1 
ATOM   15255 C CG2 . THR H  2 95  ? 119.870 86.972  305.855 1.00 177.69 ?  606 THR D CG2 1 
ATOM   15256 N N   . ASN H  2 96  ? 119.524 87.618  308.984 1.00 196.92 ?  607 ASN D N   1 
ATOM   15257 C CA  . ASN H  2 96  ? 119.552 88.696  309.971 1.00 212.01 ?  607 ASN D CA  1 
ATOM   15258 C C   . ASN H  2 96  ? 119.310 90.040  309.301 1.00 222.73 ?  607 ASN D C   1 
ATOM   15259 O O   . ASN H  2 96  ? 120.104 90.970  309.425 1.00 230.38 ?  607 ASN D O   1 
ATOM   15260 C CB  . ASN H  2 96  ? 120.885 88.683  310.708 1.00 212.93 ?  607 ASN D CB  1 
ATOM   15261 C CG  . ASN H  2 96  ? 121.160 87.360  311.406 1.00 202.19 ?  607 ASN D CG  1 
ATOM   15262 O OD1 . ASN H  2 96  ? 120.588 86.318  311.069 1.00 197.35 ?  607 ASN D OD1 1 
ATOM   15263 N ND2 . ASN H  2 96  ? 122.078 87.396  312.361 1.00 202.39 ?  607 ASN D ND2 1 
ATOM   15264 N N   . VAL H  2 97  ? 118.211 90.154  308.562 1.00 198.40 ?  608 VAL D N   1 
ATOM   15265 C CA  . VAL H  2 97  ? 117.855 91.393  307.884 1.00 205.73 ?  608 VAL D CA  1 
ATOM   15266 C C   . VAL H  2 97  ? 116.468 91.850  308.332 1.00 204.64 ?  608 VAL D C   1 
ATOM   15267 O O   . VAL H  2 97  ? 115.482 91.131  308.141 1.00 196.33 ?  608 VAL D O   1 
ATOM   15268 C CB  . VAL H  2 97  ? 117.902 91.238  306.356 1.00 205.94 ?  608 VAL D CB  1 
ATOM   15269 C CG1 . VAL H  2 97  ? 117.374 92.494  305.695 1.00 210.42 ?  608 VAL D CG1 1 
ATOM   15270 C CG2 . VAL H  2 97  ? 119.331 90.962  305.911 1.00 206.06 ?  608 VAL D CG2 1 
ATOM   15271 N N   . PRO H  2 98  ? 116.352 93.028  308.945 1.00 213.55 ?  609 PRO D N   1 
ATOM   15272 C CA  . PRO H  2 98  ? 115.040 93.545  309.373 1.00 215.70 ?  609 PRO D CA  1 
ATOM   15273 C C   . PRO H  2 98  ? 114.146 93.900  308.190 1.00 215.12 ?  609 PRO D C   1 
ATOM   15274 O O   . PRO H  2 98  ? 114.589 94.545  307.237 1.00 221.27 ?  609 PRO D O   1 
ATOM   15275 C CB  . PRO H  2 98  ? 115.401 94.788  310.198 1.00 232.83 ?  609 PRO D CB  1 
ATOM   15276 C CG  . PRO H  2 98  ? 116.732 95.213  309.667 1.00 239.65 ?  609 PRO D CG  1 
ATOM   15277 C CD  . PRO H  2 98  ? 117.451 93.943  309.305 1.00 222.69 ?  609 PRO D CD  1 
ATOM   15278 N N   . TRP H  2 99  ? 112.885 93.471  308.247 1.00 224.17 ?  610 TRP D N   1 
ATOM   15279 C CA  . TRP H  2 99  ? 111.948 93.745  307.158 1.00 227.86 ?  610 TRP D CA  1 
ATOM   15280 C C   . TRP H  2 99  ? 111.542 95.217  307.184 1.00 244.21 ?  610 TRP D C   1 
ATOM   15281 O O   . TRP H  2 99  ? 110.841 95.658  308.100 1.00 248.15 ?  610 TRP D O   1 
ATOM   15282 C CB  . TRP H  2 99  ? 110.708 92.868  307.294 1.00 213.36 ?  610 TRP D CB  1 
ATOM   15283 C CG  . TRP H  2 99  ? 109.722 93.092  306.195 1.00 214.83 ?  610 TRP D CG  1 
ATOM   15284 C CD1 . TRP H  2 99  ? 108.655 93.946  306.213 1.00 219.47 ?  610 TRP D CD1 1 
ATOM   15285 C CD2 . TRP H  2 99  ? 109.694 92.442  304.922 1.00 205.75 ?  610 TRP D CD2 1 
ATOM   15286 N NE1 . TRP H  2 99  ? 107.975 93.877  305.021 1.00 218.28 ?  610 TRP D NE1 1 
ATOM   15287 C CE2 . TRP H  2 99  ? 108.591 92.958  304.212 1.00 210.14 ?  610 TRP D CE2 1 
ATOM   15288 C CE3 . TRP H  2 99  ? 110.498 91.475  304.310 1.00 193.15 ?  610 TRP D CE3 1 
ATOM   15289 C CZ2 . TRP H  2 99  ? 108.272 92.539  302.922 1.00 202.05 ?  610 TRP D CZ2 1 
ATOM   15290 C CZ3 . TRP H  2 99  ? 110.180 91.061  303.030 1.00 187.77 ?  610 TRP D CZ3 1 
ATOM   15291 C CH2 . TRP H  2 99  ? 109.077 91.592  302.350 1.00 190.74 ?  610 TRP D CH2 1 
ATOM   15292 N N   . ASN H  2 100 ? 111.977 95.979  306.179 1.00 225.55 ?  611 ASN D N   1 
ATOM   15293 C CA  . ASN H  2 100 ? 111.630 97.394  306.097 1.00 236.87 ?  611 ASN D CA  1 
ATOM   15294 C C   . ASN H  2 100 ? 110.135 97.527  305.793 1.00 236.36 ?  611 ASN D C   1 
ATOM   15295 O O   . ASN H  2 100 ? 109.621 96.885  304.871 1.00 229.86 ?  611 ASN D O   1 
ATOM   15296 C CB  . ASN H  2 100 ? 112.513 98.056  305.028 1.00 241.11 ?  611 ASN D CB  1 
ATOM   15297 C CG  . ASN H  2 100 ? 112.671 99.569  305.210 1.00 255.86 ?  611 ASN D CG  1 
ATOM   15298 O OD1 . ASN H  2 100 ? 112.186 100.153 306.178 1.00 261.23 ?  611 ASN D OD1 1 
ATOM   15299 N ND2 . ASN H  2 100 ? 113.421 100.192 304.286 1.00 278.32 ?  611 ASN D ND2 1 
ATOM   15300 N N   . SER H  2 101 ? 109.434 98.358  306.574 1.00 231.43 ?  612 SER D N   1 
ATOM   15301 C CA  . SER H  2 101 ? 107.984 98.515  306.435 1.00 228.09 ?  612 SER D CA  1 
ATOM   15302 C C   . SER H  2 101 ? 107.559 99.093  305.090 1.00 229.54 ?  612 SER D C   1 
ATOM   15303 O O   . SER H  2 101 ? 106.411 98.889  304.678 1.00 224.29 ?  612 SER D O   1 
ATOM   15304 C CB  . SER H  2 101 ? 107.425 99.372  307.571 1.00 232.70 ?  612 SER D CB  1 
ATOM   15305 O OG  . SER H  2 101 ? 107.685 98.770  308.826 1.00 245.93 ?  612 SER D OG  1 
ATOM   15306 N N   . SER H  2 102 ? 108.450 99.804  304.398 1.00 243.50 ?  613 SER D N   1 
ATOM   15307 C CA  . SER H  2 102 ? 108.112 100.409 303.113 1.00 246.62 ?  613 SER D CA  1 
ATOM   15308 C C   . SER H  2 102 ? 107.841 99.362  302.042 1.00 234.48 ?  613 SER D C   1 
ATOM   15309 O O   . SER H  2 102 ? 107.237 99.682  301.012 1.00 234.61 ?  613 SER D O   1 
ATOM   15310 C CB  . SER H  2 102 ? 109.229 101.351 302.663 1.00 259.14 ?  613 SER D CB  1 
ATOM   15311 O OG  . SER H  2 102 ? 110.468 100.671 302.576 1.00 258.53 ?  613 SER D OG  1 
ATOM   15312 N N   . TRP H  2 103 ? 108.280 98.124  302.264 1.00 246.66 ?  614 TRP D N   1 
ATOM   15313 C CA  . TRP H  2 103 ? 108.089 97.021  301.326 1.00 235.59 ?  614 TRP D CA  1 
ATOM   15314 C C   . TRP H  2 103 ? 106.712 96.388  301.546 1.00 228.45 ?  614 TRP D C   1 
ATOM   15315 O O   . TRP H  2 103 ? 106.580 95.216  301.901 1.00 219.20 ?  614 TRP D O   1 
ATOM   15316 C CB  . TRP H  2 103 ? 109.195 95.987  301.502 1.00 227.09 ?  614 TRP D CB  1 
ATOM   15317 C CG  . TRP H  2 103 ? 110.596 96.519  301.382 1.00 234.73 ?  614 TRP D CG  1 
ATOM   15318 C CD1 . TRP H  2 103 ? 110.993 97.668  300.762 1.00 245.70 ?  614 TRP D CD1 1 
ATOM   15319 C CD2 . TRP H  2 103 ? 111.786 95.917  301.910 1.00 232.46 ?  614 TRP D CD2 1 
ATOM   15320 N NE1 . TRP H  2 103 ? 112.357 97.815  300.866 1.00 252.40 ?  614 TRP D NE1 1 
ATOM   15321 C CE2 . TRP H  2 103 ? 112.866 96.753  301.567 1.00 242.69 ?  614 TRP D CE2 1 
ATOM   15322 C CE3 . TRP H  2 103 ? 112.042 94.750  302.638 1.00 221.41 ?  614 TRP D CE3 1 
ATOM   15323 C CZ2 . TRP H  2 103 ? 114.182 96.460  301.926 1.00 240.23 ?  614 TRP D CZ2 1 
ATOM   15324 C CZ3 . TRP H  2 103 ? 113.348 94.461  302.994 1.00 221.30 ?  614 TRP D CZ3 1 
ATOM   15325 C CH2 . TRP H  2 103 ? 114.401 95.312  302.637 1.00 228.78 ?  614 TRP D CH2 1 
ATOM   15326 N N   . SER H  2 104 ? 105.672 97.206  301.338 1.00 242.68 ?  615 SER D N   1 
ATOM   15327 C CA  . SER H  2 104 ? 104.283 96.793  301.536 1.00 234.54 ?  615 SER D CA  1 
ATOM   15328 C C   . SER H  2 104 ? 104.039 96.295  302.956 1.00 230.80 ?  615 SER D C   1 
ATOM   15329 O O   . SER H  2 104 ? 104.110 95.091  303.222 1.00 219.41 ?  615 SER D O   1 
ATOM   15330 C CB  . SER H  2 104 ? 103.886 95.716  300.522 1.00 222.58 ?  615 SER D CB  1 
ATOM   15331 O OG  . SER H  2 104 ? 102.542 95.310  300.713 1.00 218.90 ?  615 SER D OG  1 
ATOM   15332 N N   . ASN H  2 105 ? 103.745 97.220  303.870 1.00 226.96 ?  616 ASN D N   1 
ATOM   15333 C CA  . ASN H  2 105 ? 103.551 96.885  305.275 1.00 225.99 ?  616 ASN D CA  1 
ATOM   15334 C C   . ASN H  2 105 ? 102.309 96.032  305.511 1.00 228.28 ?  616 ASN D C   1 
ATOM   15335 O O   . ASN H  2 105 ? 101.194 96.550  305.640 1.00 236.24 ?  616 ASN D O   1 
ATOM   15336 C CB  . ASN H  2 105 ? 103.456 98.170  306.108 1.00 232.93 ?  616 ASN D CB  1 
ATOM   15337 C CG  . ASN H  2 105 ? 102.449 99.161  305.540 1.00 241.89 ?  616 ASN D CG  1 
ATOM   15338 O OD1 . ASN H  2 105 ? 102.231 99.213  304.329 1.00 243.64 ?  616 ASN D OD1 1 
ATOM   15339 N ND2 . ASN H  2 105 ? 101.820 99.939  306.415 1.00 248.49 ?  616 ASN D ND2 1 
ATOM   15340 N N   . ARG H  2 106 ? 102.499 94.715  305.560 1.00 223.56 ?  617 ARG D N   1 
ATOM   15341 C CA  . ARG H  2 106 ? 101.432 93.776  305.861 1.00 225.00 ?  617 ARG D CA  1 
ATOM   15342 C C   . ARG H  2 106 ? 101.768 93.052  307.159 1.00 220.30 ?  617 ARG D C   1 
ATOM   15343 O O   . ARG H  2 106 ? 102.911 93.069  307.624 1.00 215.88 ?  617 ARG D O   1 
ATOM   15344 C CB  . ARG H  2 106 ? 101.240 92.755  304.729 1.00 221.60 ?  617 ARG D CB  1 
ATOM   15345 C CG  . ARG H  2 106 ? 101.005 93.345  303.346 1.00 225.72 ?  617 ARG D CG  1 
ATOM   15346 C CD  . ARG H  2 106 ? 99.541  93.705  303.146 1.00 234.94 ?  617 ARG D CD  1 
ATOM   15347 N NE  . ARG H  2 106 ? 99.238  94.051  301.760 1.00 238.90 ?  617 ARG D NE  1 
ATOM   15348 C CZ  . ARG H  2 106 ? 98.016  94.320  301.311 1.00 246.96 ?  617 ARG D CZ  1 
ATOM   15349 N NH1 . ARG H  2 106 ? 96.983  94.280  302.142 1.00 251.84 1  617 ARG D NH1 1 
ATOM   15350 N NH2 . ARG H  2 106 ? 97.824  94.628  300.036 1.00 250.27 ?  617 ARG D NH2 1 
ATOM   15351 N N   . ASN H  2 107 ? 100.758 92.420  307.750 1.00 218.35 ?  618 ASN D N   1 
ATOM   15352 C CA  . ASN H  2 107 ? 100.951 91.677  308.986 1.00 214.52 ?  618 ASN D CA  1 
ATOM   15353 C C   . ASN H  2 107 ? 101.215 90.191  308.726 1.00 212.42 ?  618 ASN D C   1 
ATOM   15354 O O   . ASN H  2 107 ? 101.021 89.674  307.624 1.00 212.84 ?  618 ASN D O   1 
ATOM   15355 C CB  . ASN H  2 107 ? 99.752  91.860  309.919 1.00 221.64 ?  618 ASN D CB  1 
ATOM   15356 C CG  . ASN H  2 107 ? 100.103 91.605  311.383 1.00 219.17 ?  618 ASN D CG  1 
ATOM   15357 O OD1 . ASN H  2 107 ? 100.832 90.665  311.703 1.00 213.84 ?  618 ASN D OD1 1 
ATOM   15358 N ND2 . ASN H  2 107 ? 99.582  92.443  312.276 1.00 226.06 ?  618 ASN D ND2 1 
ATOM   15359 N N   . LEU H  2 108 ? 101.663 89.507  309.786 1.00 219.48 ?  619 LEU D N   1 
ATOM   15360 C CA  . LEU H  2 108 ? 101.987 88.085  309.700 1.00 214.19 ?  619 LEU D CA  1 
ATOM   15361 C C   . LEU H  2 108 ? 100.767 87.271  309.291 1.00 215.10 ?  619 LEU D C   1 
ATOM   15362 O O   . LEU H  2 108 ? 100.869 86.348  308.475 1.00 215.33 ?  619 LEU D O   1 
ATOM   15363 C CB  . LEU H  2 108 ? 102.546 87.582  311.030 1.00 213.65 ?  619 LEU D CB  1 
ATOM   15364 C CG  . LEU H  2 108 ? 103.417 86.322  310.953 1.00 213.32 ?  619 LEU D CG  1 
ATOM   15365 C CD1 . LEU H  2 108 ? 104.616 86.509  310.027 1.00 212.78 ?  619 LEU D CD1 1 
ATOM   15366 C CD2 . LEU H  2 108 ? 103.873 85.904  312.339 1.00 212.84 ?  619 LEU D CD2 1 
ATOM   15367 N N   . SER H  2 109 ? 99.601  87.601  309.845 1.00 196.66 ?  620 SER D N   1 
ATOM   15368 C CA  . SER H  2 109 ? 98.395  86.850  309.536 1.00 197.55 ?  620 SER D CA  1 
ATOM   15369 C C   . SER H  2 109 ? 97.770  87.321  308.238 1.00 198.15 ?  620 SER D C   1 
ATOM   15370 O O   . SER H  2 109 ? 96.830  86.688  307.746 1.00 198.92 ?  620 SER D O   1 
ATOM   15371 C CB  . SER H  2 109 ? 97.383  86.980  310.676 1.00 197.90 ?  620 SER D CB  1 
ATOM   15372 O OG  . SER H  2 109 ? 96.266  86.139  310.460 1.00 198.74 ?  620 SER D OG  1 
ATOM   15373 N N   . GLU H  2 110 ? 98.267  88.427  307.691 1.00 200.04 ?  621 GLU D N   1 
ATOM   15374 C CA  . GLU H  2 110 ? 97.774  89.002  306.454 1.00 200.55 ?  621 GLU D CA  1 
ATOM   15375 C C   . GLU H  2 110 ? 98.617  88.593  305.252 1.00 200.35 ?  621 GLU D C   1 
ATOM   15376 O O   . GLU H  2 110 ? 98.242  88.904  304.116 1.00 200.81 ?  621 GLU D O   1 
ATOM   15377 C CB  . GLU H  2 110 ? 97.785  90.532  306.562 1.00 200.33 ?  621 GLU D CB  1 
ATOM   15378 C CG  . GLU H  2 110 ? 96.993  91.099  307.723 1.00 200.49 ?  621 GLU D CG  1 
ATOM   15379 C CD  . GLU H  2 110 ? 97.055  92.615  307.776 1.00 200.27 ?  621 GLU D CD  1 
ATOM   15380 O OE1 . GLU H  2 110 ? 97.517  93.231  306.791 1.00 200.15 ?  621 GLU D OE1 1 
ATOM   15381 O OE2 . GLU H  2 110 ? 96.655  93.190  308.809 1.00 200.22 -1 621 GLU D OE2 1 
ATOM   15382 N N   . ILE H  2 111 ? 99.740  87.905  305.478 1.00 197.50 ?  622 ILE D N   1 
ATOM   15383 C CA  . ILE H  2 111 ? 100.638 87.458  304.412 1.00 197.25 ?  622 ILE D CA  1 
ATOM   15384 C C   . ILE H  2 111 ? 100.519 85.957  304.161 1.00 197.57 ?  622 ILE D C   1 
ATOM   15385 O O   . ILE H  2 111 ? 100.246 85.525  303.040 1.00 198.05 ?  622 ILE D O   1 
ATOM   15386 C CB  . ILE H  2 111 ? 102.099 87.844  304.741 1.00 196.24 ?  622 ILE D CB  1 
ATOM   15387 C CG1 . ILE H  2 111 ? 102.290 89.360  304.726 1.00 195.95 ?  622 ILE D CG1 1 
ATOM   15388 C CG2 . ILE H  2 111 ? 103.082 87.147  303.797 1.00 195.94 ?  622 ILE D CG2 1 
ATOM   15389 C CD1 . ILE H  2 111 ? 103.667 89.792  305.183 1.00 194.97 ?  622 ILE D CD1 1 
ATOM   15390 N N   . TRP H  2 112 ? 100.699 85.145  305.204 1.00 181.96 ?  623 TRP D N   1 
ATOM   15391 C CA  . TRP H  2 112 ? 100.717 83.692  305.080 1.00 180.48 ?  623 TRP D CA  1 
ATOM   15392 C C   . TRP H  2 112 ? 99.333  83.056  305.002 1.00 182.36 ?  623 TRP D C   1 
ATOM   15393 O O   . TRP H  2 112 ? 99.236  81.875  304.656 1.00 181.15 ?  623 TRP D O   1 
ATOM   15394 C CB  . TRP H  2 112 ? 101.524 83.108  306.249 1.00 180.06 ?  623 TRP D CB  1 
ATOM   15395 C CG  . TRP H  2 112 ? 102.940 83.656  306.334 1.00 178.22 ?  623 TRP D CG  1 
ATOM   15396 C CD1 . TRP H  2 112 ? 103.391 84.632  307.177 1.00 179.47 ?  623 TRP D CD1 1 
ATOM   15397 C CD2 . TRP H  2 112 ? 104.095 83.191  305.614 1.00 174.99 ?  623 TRP D CD2 1 
ATOM   15398 N NE1 . TRP H  2 112 ? 104.734 84.847  306.983 1.00 177.25 ?  623 TRP D NE1 1 
ATOM   15399 C CE2 . TRP H  2 112 ? 105.192 83.969  306.037 1.00 174.49 ?  623 TRP D CE2 1 
ATOM   15400 C CE3 . TRP H  2 112 ? 104.303 82.209  304.640 1.00 172.61 ?  623 TRP D CE3 1 
ATOM   15401 C CZ2 . TRP H  2 112 ? 106.475 83.795  305.521 1.00 171.75 ?  623 TRP D CZ2 1 
ATOM   15402 C CZ3 . TRP H  2 112 ? 105.580 82.039  304.129 1.00 169.86 ?  623 TRP D CZ3 1 
ATOM   15403 C CH2 . TRP H  2 112 ? 106.647 82.828  304.571 1.00 169.47 ?  623 TRP D CH2 1 
ATOM   15404 N N   . ASP H  2 113 ? 98.264  83.800  305.296 1.00 194.45 ?  624 ASP D N   1 
ATOM   15405 C CA  . ASP H  2 113 ? 96.912  83.250  305.311 1.00 196.65 ?  624 ASP D CA  1 
ATOM   15406 C C   . ASP H  2 113 ? 95.942  84.135  304.533 1.00 198.27 ?  624 ASP D C   1 
ATOM   15407 O O   . ASP H  2 113 ? 94.729  84.064  304.755 1.00 200.99 ?  624 ASP D O   1 
ATOM   15408 C CB  . ASP H  2 113 ? 96.417  83.045  306.748 1.00 199.42 ?  624 ASP D CB  1 
ATOM   15409 C CG  . ASP H  2 113 ? 97.207  81.977  307.496 1.00 198.02 ?  624 ASP D CG  1 
ATOM   15410 O OD1 . ASP H  2 113 ? 97.619  80.989  306.854 1.00 195.54 ?  624 ASP D OD1 1 
ATOM   15411 O OD2 . ASP H  2 113 ? 97.411  82.120  308.723 1.00 199.47 -1 624 ASP D OD2 1 
ATOM   15412 N N   . ASN H  2 114 ? 96.463  84.970  303.627 1.00 203.42 ?  625 ASN D N   1 
ATOM   15413 C CA  . ASN H  2 114 ? 95.602  85.856  302.834 1.00 208.18 ?  625 ASN D CA  1 
ATOM   15414 C C   . ASN H  2 114 ? 96.316  86.362  301.585 1.00 206.23 ?  625 ASN D C   1 
ATOM   15415 O O   . ASN H  2 114 ? 95.913  87.398  301.047 1.00 215.46 ?  625 ASN D O   1 
ATOM   15416 C CB  . ASN H  2 114 ? 95.086  87.022  303.687 1.00 224.97 ?  625 ASN D CB  1 
ATOM   15417 C CG  . ASN H  2 114 ? 93.889  87.726  303.055 1.00 236.90 ?  625 ASN D CG  1 
ATOM   15418 O OD1 . ASN H  2 114 ? 93.188  87.153  302.217 1.00 230.11 ?  625 ASN D OD1 1 
ATOM   15419 N ND2 . ASN H  2 114 ? 93.654  88.970  303.453 1.00 252.40 ?  625 ASN D ND2 1 
ATOM   15420 N N   . MET H  2 115 ? 97.344  85.671  301.099 1.00 204.27 ?  626 MET D N   1 
ATOM   15421 C CA  . MET H  2 115 ? 98.115  86.127  299.952 1.00 197.67 ?  626 MET D CA  1 
ATOM   15422 C C   . MET H  2 115 ? 98.779  84.949  299.257 1.00 190.56 ?  626 MET D C   1 
ATOM   15423 O O   . MET H  2 115 ? 99.269  84.030  299.914 1.00 189.63 ?  626 MET D O   1 
ATOM   15424 C CB  . MET H  2 115 ? 99.228  87.054  300.473 1.00 198.64 ?  626 MET D CB  1 
ATOM   15425 C CG  . MET H  2 115 ? 99.764  88.167  299.593 1.00 199.79 ?  626 MET D CG  1 
ATOM   15426 S SD  . MET H  2 115 ? 98.751  89.593  299.194 1.00 212.07 ?  626 MET D SD  1 
ATOM   15427 C CE  . MET H  2 115 ? 99.904  90.498  298.152 1.00 209.81 ?  626 MET D CE  1 
ATOM   15428 N N   . THR H  2 116 ? 98.741  84.962  297.924 1.00 185.89 ?  627 THR D N   1 
ATOM   15429 C CA  . THR H  2 116 ? 99.394  83.933  297.129 1.00 183.15 ?  627 THR D CA  1 
ATOM   15430 C C   . THR H  2 116 ? 100.800 84.391  296.765 1.00 180.78 ?  627 THR D C   1 
ATOM   15431 O O   . THR H  2 116 ? 101.123 85.579  296.827 1.00 181.29 ?  627 THR D O   1 
ATOM   15432 C CB  . THR H  2 116 ? 98.607  83.613  295.858 1.00 183.12 ?  627 THR D CB  1 
ATOM   15433 O OG1 . THR H  2 116 ? 98.592  84.762  295.003 1.00 183.27 ?  627 THR D OG1 1 
ATOM   15434 C CG2 . THR H  2 116 ? 97.178  83.208  296.199 1.00 185.72 ?  627 THR D CG2 1 
ATOM   15435 N N   . TRP H  2 117 ? 101.644 83.433  296.389 1.00 178.94 ?  628 TRP D N   1 
ATOM   15436 C CA  . TRP H  2 117 ? 103.008 83.790  296.018 1.00 175.70 ?  628 TRP D CA  1 
ATOM   15437 C C   . TRP H  2 117 ? 103.042 84.631  294.742 1.00 176.95 ?  628 TRP D C   1 
ATOM   15438 O O   . TRP H  2 117 ? 103.889 85.521  294.604 1.00 178.29 ?  628 TRP D O   1 
ATOM   15439 C CB  . TRP H  2 117 ? 103.854 82.529  295.867 1.00 173.26 ?  628 TRP D CB  1 
ATOM   15440 C CG  . TRP H  2 117 ? 104.396 82.007  297.171 1.00 173.13 ?  628 TRP D CG  1 
ATOM   15441 C CD1 . TRP H  2 117 ? 103.870 80.999  297.927 1.00 173.82 ?  628 TRP D CD1 1 
ATOM   15442 C CD2 . TRP H  2 117 ? 105.581 82.442  297.854 1.00 172.33 ?  628 TRP D CD2 1 
ATOM   15443 N NE1 . TRP H  2 117 ? 104.642 80.789  299.043 1.00 173.48 ?  628 TRP D NE1 1 
ATOM   15444 C CE2 . TRP H  2 117 ? 105.700 81.660  299.021 1.00 172.57 ?  628 TRP D CE2 1 
ATOM   15445 C CE3 . TRP H  2 117 ? 106.548 83.418  297.595 1.00 171.55 ?  628 TRP D CE3 1 
ATOM   15446 C CZ2 . TRP H  2 117 ? 106.746 81.824  299.926 1.00 172.05 ?  628 TRP D CZ2 1 
ATOM   15447 C CZ3 . TRP H  2 117 ? 107.585 83.580  298.496 1.00 171.08 ?  628 TRP D CZ3 1 
ATOM   15448 C CH2 . TRP H  2 117 ? 107.676 82.786  299.647 1.00 171.31 ?  628 TRP D CH2 1 
ATOM   15449 N N   . LEU H  2 118 ? 102.121 84.362  293.810 1.00 170.57 ?  629 LEU D N   1 
ATOM   15450 C CA  . LEU H  2 118 ? 102.026 85.133  292.571 1.00 170.41 ?  629 LEU D CA  1 
ATOM   15451 C C   . LEU H  2 118 ? 101.591 86.569  292.826 1.00 172.47 ?  629 LEU D C   1 
ATOM   15452 O O   . LEU H  2 118 ? 102.137 87.507  292.232 1.00 172.01 ?  629 LEU D O   1 
ATOM   15453 C CB  . LEU H  2 118 ? 101.036 84.449  291.633 1.00 170.75 ?  629 LEU D CB  1 
ATOM   15454 C CG  . LEU H  2 118 ? 101.485 83.131  291.011 1.00 168.63 ?  629 LEU D CG  1 
ATOM   15455 C CD1 . LEU H  2 118 ? 100.346 82.537  290.201 1.00 169.51 ?  629 LEU D CD1 1 
ATOM   15456 C CD2 . LEU H  2 118 ? 102.712 83.352  290.146 1.00 166.38 ?  629 LEU D CD2 1 
ATOM   15457 N N   . GLN H  2 119 ? 100.613 86.758  293.709 1.00 183.16 ?  630 GLN D N   1 
ATOM   15458 C CA  . GLN H  2 119 ? 100.127 88.097  294.012 1.00 187.30 ?  630 GLN D CA  1 
ATOM   15459 C C   . GLN H  2 119 ? 101.164 88.866  294.814 1.00 189.13 ?  630 GLN D C   1 
ATOM   15460 O O   . GLN H  2 119 ? 101.288 90.088  294.671 1.00 194.57 ?  630 GLN D O   1 
ATOM   15461 C CB  . GLN H  2 119 ? 98.793  88.010  294.752 1.00 192.46 ?  630 GLN D CB  1 
ATOM   15462 C CG  . GLN H  2 119 ? 98.089  89.335  294.991 1.00 201.76 ?  630 GLN D CG  1 
ATOM   15463 C CD  . GLN H  2 119 ? 96.778  89.158  295.738 1.00 207.03 ?  630 GLN D CD  1 
ATOM   15464 O OE1 . GLN H  2 119 ? 96.327  88.032  295.960 1.00 203.69 ?  630 GLN D OE1 1 
ATOM   15465 N NE2 . GLN H  2 119 ? 96.156  90.268  296.120 1.00 215.66 ?  630 GLN D NE2 1 
ATOM   15466 N N   . TRP H  2 120 ? 101.924 88.153  295.646 1.00 192.35 ?  631 TRP D N   1 
ATOM   15467 C CA  . TRP H  2 120 ? 102.937 88.784  296.479 1.00 193.65 ?  631 TRP D CA  1 
ATOM   15468 C C   . TRP H  2 120 ? 104.124 89.216  295.633 1.00 190.99 ?  631 TRP D C   1 
ATOM   15469 O O   . TRP H  2 120 ? 104.624 90.338  295.779 1.00 195.65 ?  631 TRP D O   1 
ATOM   15470 C CB  . TRP H  2 120 ? 103.401 87.782  297.532 1.00 189.12 ?  631 TRP D CB  1 
ATOM   15471 C CG  . TRP H  2 120 ? 104.586 88.195  298.324 1.00 189.07 ?  631 TRP D CG  1 
ATOM   15472 C CD1 . TRP H  2 120 ? 105.887 87.856  298.086 1.00 183.36 ?  631 TRP D CD1 1 
ATOM   15473 C CD2 . TRP H  2 120 ? 104.576 88.881  299.577 1.00 194.46 ?  631 TRP D CD2 1 
ATOM   15474 N NE1 . TRP H  2 120 ? 106.697 88.372  299.065 1.00 185.21 ?  631 TRP D NE1 1 
ATOM   15475 C CE2 . TRP H  2 120 ? 105.915 88.996  300.001 1.00 191.89 ?  631 TRP D CE2 1 
ATOM   15476 C CE3 . TRP H  2 120 ? 103.567 89.441  300.366 1.00 201.65 ?  631 TRP D CE3 1 
ATOM   15477 C CZ2 . TRP H  2 120 ? 106.271 89.647  301.178 1.00 196.17 ?  631 TRP D CZ2 1 
ATOM   15478 C CZ3 . TRP H  2 120 ? 103.921 90.087  301.535 1.00 206.03 ?  631 TRP D CZ3 1 
ATOM   15479 C CH2 . TRP H  2 120 ? 105.262 90.185  301.930 1.00 203.19 ?  631 TRP D CH2 1 
ATOM   15480 N N   . ASP H  2 121 ? 104.574 88.344  294.724 1.00 196.94 ?  632 ASP D N   1 
ATOM   15481 C CA  . ASP H  2 121 ? 105.721 88.682  293.893 1.00 194.27 ?  632 ASP D CA  1 
ATOM   15482 C C   . ASP H  2 121 ? 105.396 89.862  292.989 1.00 200.04 ?  632 ASP D C   1 
ATOM   15483 O O   . ASP H  2 121 ? 106.314 90.527  292.500 1.00 200.91 ?  632 ASP D O   1 
ATOM   15484 C CB  . ASP H  2 121 ? 106.186 87.466  293.085 1.00 186.12 ?  632 ASP D CB  1 
ATOM   15485 C CG  . ASP H  2 121 ? 107.480 87.728  292.327 1.00 183.54 ?  632 ASP D CG  1 
ATOM   15486 O OD1 . ASP H  2 121 ? 108.563 87.502  292.912 1.00 180.54 ?  632 ASP D OD1 1 
ATOM   15487 O OD2 . ASP H  2 121 ? 107.420 88.146  291.151 1.00 184.91 -1 632 ASP D OD2 1 
ATOM   15488 N N   . LYS H  2 122 ? 104.104 90.128  292.754 1.00 189.43 ?  633 LYS D N   1 
ATOM   15489 C CA  . LYS H  2 122 ? 103.711 91.242  291.899 1.00 195.39 ?  633 LYS D CA  1 
ATOM   15490 C C   . LYS H  2 122 ? 103.943 92.565  292.609 1.00 202.70 ?  633 LYS D C   1 
ATOM   15491 O O   . LYS H  2 122 ? 104.234 93.578  291.962 1.00 206.99 ?  633 LYS D O   1 
ATOM   15492 C CB  . LYS H  2 122 ? 102.241 91.118  291.503 1.00 198.29 ?  633 LYS D CB  1 
ATOM   15493 C CG  . LYS H  2 122 ? 101.806 92.062  290.398 1.00 203.61 ?  633 LYS D CG  1 
ATOM   15494 C CD  . LYS H  2 122 ? 102.539 91.844  289.100 1.00 199.69 ?  633 LYS D CD  1 
ATOM   15495 C CE  . LYS H  2 122 ? 101.959 92.769  288.047 1.00 207.53 ?  633 LYS D CE  1 
ATOM   15496 N NZ  . LYS H  2 122 ? 100.522 92.487  287.774 1.00 210.30 1  633 LYS D NZ  1 
ATOM   15497 N N   . GLU H  2 123 ? 103.814 92.572  293.934 1.00 193.39 ?  634 GLU D N   1 
ATOM   15498 C CA  . GLU H  2 123 ? 103.992 93.783  294.718 1.00 195.11 ?  634 GLU D CA  1 
ATOM   15499 C C   . GLU H  2 123 ? 105.460 93.987  295.059 1.00 193.70 ?  634 GLU D C   1 
ATOM   15500 O O   . GLU H  2 123 ? 105.981 95.098  294.918 1.00 196.52 ?  634 GLU D O   1 
ATOM   15501 C CB  . GLU H  2 123 ? 103.144 93.720  295.989 1.00 197.60 ?  634 GLU D CB  1 
ATOM   15502 C CG  . GLU H  2 123 ? 101.650 93.763  295.719 1.00 201.83 ?  634 GLU D CG  1 
ATOM   15503 C CD  . GLU H  2 123 ? 100.829 93.824  296.988 1.00 207.16 ?  634 GLU D CD  1 
ATOM   15504 O OE1 . GLU H  2 123 ? 101.426 93.785  298.084 1.00 207.09 ?  634 GLU D OE1 1 
ATOM   15505 O OE2 . GLU H  2 123 ? 99.587  93.907  296.889 1.00 212.20 -1 634 GLU D OE2 1 
ATOM   15506 N N   . ILE H  2 124 ? 106.147 92.919  295.483 1.00 202.56 ?  635 ILE D N   1 
ATOM   15507 C CA  . ILE H  2 124 ? 107.541 93.038  295.905 1.00 200.45 ?  635 ILE D CA  1 
ATOM   15508 C C   . ILE H  2 124 ? 108.487 93.006  294.720 1.00 196.85 ?  635 ILE D C   1 
ATOM   15509 O O   . ILE H  2 124 ? 109.703 93.139  294.907 1.00 195.49 ?  635 ILE D O   1 
ATOM   15510 C CB  . ILE H  2 124 ? 107.937 91.935  296.909 1.00 194.67 ?  635 ILE D CB  1 
ATOM   15511 C CG1 . ILE H  2 124 ? 106.759 91.603  297.820 1.00 197.10 ?  635 ILE D CG1 1 
ATOM   15512 C CG2 . ILE H  2 124 ? 109.118 92.379  297.773 1.00 195.49 ?  635 ILE D CG2 1 
ATOM   15513 C CD1 . ILE H  2 124 ? 106.373 92.734  298.747 1.00 205.74 ?  635 ILE D CD1 1 
ATOM   15514 N N   . SER H  2 125 ? 107.966 92.836  293.501 1.00 211.12 ?  636 SER D N   1 
ATOM   15515 C CA  . SER H  2 125 ? 108.833 92.813  292.329 1.00 208.21 ?  636 SER D CA  1 
ATOM   15516 C C   . SER H  2 125 ? 109.663 94.084  292.262 1.00 213.68 ?  636 SER D C   1 
ATOM   15517 O O   . SER H  2 125 ? 110.782 94.077  291.738 1.00 211.20 ?  636 SER D O   1 
ATOM   15518 C CB  . SER H  2 125 ? 108.011 92.650  291.049 1.00 208.51 ?  636 SER D CB  1 
ATOM   15519 O OG  . SER H  2 125 ? 107.110 93.732  290.877 1.00 216.66 ?  636 SER D OG  1 
ATOM   15520 N N   . ASN H  2 126 ? 109.117 95.184  292.789 1.00 211.24 ?  637 ASN D N   1 
ATOM   15521 C CA  . ASN H  2 126 ? 109.814 96.462  292.806 1.00 217.61 ?  637 ASN D CA  1 
ATOM   15522 C C   . ASN H  2 126 ? 111.002 96.479  293.757 1.00 216.10 ?  637 ASN D C   1 
ATOM   15523 O O   . ASN H  2 126 ? 111.982 97.189  293.499 1.00 218.09 ?  637 ASN D O   1 
ATOM   15524 C CB  . ASN H  2 126 ? 108.839 97.541  293.246 1.00 226.48 ?  637 ASN D CB  1 
ATOM   15525 C CG  . ASN H  2 126 ? 107.952 97.999  292.139 1.00 230.44 ?  637 ASN D CG  1 
ATOM   15526 O OD1 . ASN H  2 126 ? 107.871 97.375  291.082 1.00 226.09 ?  637 ASN D OD1 1 
ATOM   15527 N ND2 . ASN H  2 126 ? 107.260 99.091  292.376 1.00 243.08 ?  637 ASN D ND2 1 
ATOM   15528 N N   . TYR H  2 127 ? 110.955 95.702  294.841 1.00 208.54 ?  638 TYR D N   1 
ATOM   15529 C CA  . TYR H  2 127 ? 112.007 95.724  295.851 1.00 207.59 ?  638 TYR D CA  1 
ATOM   15530 C C   . TYR H  2 127 ? 112.776 94.416  295.903 1.00 195.76 ?  638 TYR D C   1 
ATOM   15531 O O   . TYR H  2 127 ? 113.626 94.238  296.782 1.00 194.37 ?  638 TYR D O   1 
ATOM   15532 C CB  . TYR H  2 127 ? 111.435 96.062  297.239 1.00 214.31 ?  638 TYR D CB  1 
ATOM   15533 C CG  . TYR H  2 127 ? 110.419 97.191  297.232 1.00 227.16 ?  638 TYR D CG  1 
ATOM   15534 C CD1 . TYR H  2 127 ? 110.831 98.512  297.140 1.00 235.29 ?  638 TYR D CD1 1 
ATOM   15535 C CD2 . TYR H  2 127 ? 109.057 96.940  297.403 1.00 230.69 ?  638 TYR D CD2 1 
ATOM   15536 C CE1 . TYR H  2 127 ? 109.915 99.554  297.134 1.00 246.63 ?  638 TYR D CE1 1 
ATOM   15537 C CE2 . TYR H  2 127 ? 108.133 97.979  297.411 1.00 241.68 ?  638 TYR D CE2 1 
ATOM   15538 C CZ  . TYR H  2 127 ? 108.565 99.281  297.279 1.00 249.90 ?  638 TYR D CZ  1 
ATOM   15539 O OH  . TYR H  2 127 ? 107.631 100.295 297.287 1.00 261.65 ?  638 TYR D OH  1 
ATOM   15540 N N   . THR H  2 128 ? 112.506 93.501  294.968 1.00 211.01 ?  639 THR D N   1 
ATOM   15541 C CA  . THR H  2 128 ? 113.210 92.223  294.950 1.00 205.74 ?  639 THR D CA  1 
ATOM   15542 C C   . THR H  2 128 ? 114.703 92.443  294.775 1.00 208.78 ?  639 THR D C   1 
ATOM   15543 O O   . THR H  2 128 ? 115.521 91.841  295.478 1.00 207.80 ?  639 THR D O   1 
ATOM   15544 C CB  . THR H  2 128 ? 112.673 91.328  293.830 1.00 199.78 ?  639 THR D CB  1 
ATOM   15545 O OG1 . THR H  2 128 ? 112.403 92.121  292.669 1.00 206.99 ?  639 THR D OG1 1 
ATOM   15546 C CG2 . THR H  2 128 ? 111.401 90.597  294.262 1.00 190.76 ?  639 THR D CG2 1 
ATOM   15547 N N   . GLN H  2 129 ? 115.070 93.322  293.843 1.00 192.16 ?  640 GLN D N   1 
ATOM   15548 C CA  . GLN H  2 129 ? 116.472 93.595  293.574 1.00 194.11 ?  640 GLN D CA  1 
ATOM   15549 C C   . GLN H  2 129 ? 117.143 94.295  294.754 1.00 196.73 ?  640 GLN D C   1 
ATOM   15550 O O   . GLN H  2 129 ? 118.345 94.118  294.976 1.00 196.05 ?  640 GLN D O   1 
ATOM   15551 C CB  . GLN H  2 129 ? 116.564 94.453  292.311 1.00 199.81 ?  640 GLN D CB  1 
ATOM   15552 C CG  . GLN H  2 129 ? 117.952 94.676  291.767 1.00 206.74 ?  640 GLN D CG  1 
ATOM   15553 C CD  . GLN H  2 129 ? 118.548 93.393  291.225 1.00 201.89 ?  640 GLN D CD  1 
ATOM   15554 O OE1 . GLN H  2 129 ? 117.827 92.439  290.929 1.00 194.42 ?  640 GLN D OE1 1 
ATOM   15555 N NE2 . GLN H  2 129 ? 119.866 93.364  291.085 1.00 207.96 ?  640 GLN D NE2 1 
ATOM   15556 N N   . ILE H  2 130 ? 116.387 95.088  295.515 1.00 201.58 ?  641 ILE D N   1 
ATOM   15557 C CA  . ILE H  2 130 ? 116.945 95.792  296.669 1.00 204.77 ?  641 ILE D CA  1 
ATOM   15558 C C   . ILE H  2 130 ? 117.260 94.828  297.809 1.00 199.59 ?  641 ILE D C   1 
ATOM   15559 O O   . ILE H  2 130 ? 118.336 94.884  298.416 1.00 198.99 ?  641 ILE D O   1 
ATOM   15560 C CB  . ILE H  2 130 ? 115.985 96.901  297.133 1.00 209.32 ?  641 ILE D CB  1 
ATOM   15561 C CG1 . ILE H  2 130 ? 115.611 97.816  295.966 1.00 215.41 ?  641 ILE D CG1 1 
ATOM   15562 C CG2 . ILE H  2 130 ? 116.606 97.695  298.266 1.00 209.57 ?  641 ILE D CG2 1 
ATOM   15563 C CD1 . ILE H  2 130 ? 114.658 98.926  296.354 1.00 221.37 ?  641 ILE D CD1 1 
ATOM   15564 N N   . ILE H  2 131 ? 116.325 93.926  298.109 1.00 204.43 ?  642 ILE D N   1 
ATOM   15565 C CA  . ILE H  2 131 ? 116.501 92.970  299.200 1.00 198.23 ?  642 ILE D CA  1 
ATOM   15566 C C   . ILE H  2 131 ? 117.677 92.044  298.930 1.00 194.18 ?  642 ILE D C   1 
ATOM   15567 O O   . ILE H  2 131 ? 118.438 91.696  299.843 1.00 193.61 ?  642 ILE D O   1 
ATOM   15568 C CB  . ILE H  2 131 ? 115.200 92.171  299.405 1.00 190.67 ?  642 ILE D CB  1 
ATOM   15569 C CG1 . ILE H  2 131 ? 114.040 93.092  299.781 1.00 198.25 ?  642 ILE D CG1 1 
ATOM   15570 C CG2 . ILE H  2 131 ? 115.386 91.098  300.459 1.00 184.15 ?  642 ILE D CG2 1 
ATOM   15571 C CD1 . ILE H  2 131 ? 112.740 92.345  299.999 1.00 190.11 ?  642 ILE D CD1 1 
ATOM   15572 N N   . TYR H  2 132 ? 117.843 91.629  297.675 1.00 209.08 ?  643 TYR D N   1 
ATOM   15573 C CA  . TYR H  2 132 ? 118.924 90.715  297.323 1.00 202.25 ?  643 TYR D CA  1 
ATOM   15574 C C   . TYR H  2 132 ? 120.289 91.284  297.700 1.00 207.49 ?  643 TYR D C   1 
ATOM   15575 O O   . TYR H  2 132 ? 121.177 90.542  298.133 1.00 205.83 ?  643 TYR D O   1 
ATOM   15576 C CB  . TYR H  2 132 ? 118.869 90.436  295.822 1.00 197.36 ?  643 TYR D CB  1 
ATOM   15577 C CG  . TYR H  2 132 ? 117.677 89.607  295.390 1.00 194.14 ?  643 TYR D CG  1 
ATOM   15578 C CD1 . TYR H  2 132 ? 116.856 88.978  296.320 1.00 190.79 ?  643 TYR D CD1 1 
ATOM   15579 C CD2 . TYR H  2 132 ? 117.329 89.519  294.049 1.00 197.80 ?  643 TYR D CD2 1 
ATOM   15580 C CE1 . TYR H  2 132 ? 115.743 88.247  295.919 1.00 187.17 ?  643 TYR D CE1 1 
ATOM   15581 C CE2 . TYR H  2 132 ? 116.220 88.792  293.639 1.00 194.22 ?  643 TYR D CE2 1 
ATOM   15582 C CZ  . TYR H  2 132 ? 115.430 88.158  294.577 1.00 184.58 ?  643 TYR D CZ  1 
ATOM   15583 O OH  . TYR H  2 132 ? 114.326 87.433  294.178 1.00 173.51 ?  643 TYR D OH  1 
ATOM   15584 N N   . GLY H  2 133 ? 120.469 92.601  297.565 1.00 202.47 ?  644 GLY D N   1 
ATOM   15585 C CA  . GLY H  2 133 ? 121.750 93.199  297.906 1.00 205.32 ?  644 GLY D CA  1 
ATOM   15586 C C   . GLY H  2 133 ? 122.048 93.204  299.391 1.00 207.97 ?  644 GLY D C   1 
ATOM   15587 O O   . GLY H  2 133 ? 123.212 93.130  299.794 1.00 212.03 ?  644 GLY D O   1 
ATOM   15588 N N   . LEU H  2 134 ? 121.015 93.300  300.225 1.00 205.19 ?  645 LEU D N   1 
ATOM   15589 C CA  . LEU H  2 134 ? 121.222 93.318  301.667 1.00 206.38 ?  645 LEU D CA  1 
ATOM   15590 C C   . LEU H  2 134 ? 121.467 91.932  302.244 1.00 197.72 ?  645 LEU D C   1 
ATOM   15591 O O   . LEU H  2 134 ? 121.825 91.826  303.421 1.00 193.88 ?  645 LEU D O   1 
ATOM   15592 C CB  . LEU H  2 134 ? 120.046 93.994  302.376 1.00 205.99 ?  645 LEU D CB  1 
ATOM   15593 C CG  . LEU H  2 134 ? 120.163 95.518  302.512 1.00 211.39 ?  645 LEU D CG  1 
ATOM   15594 C CD1 . LEU H  2 134 ? 121.441 95.887  303.260 1.00 219.13 ?  645 LEU D CD1 1 
ATOM   15595 C CD2 . LEU H  2 134 ? 120.106 96.226  301.164 1.00 214.47 ?  645 LEU D CD2 1 
ATOM   15596 N N   . LEU H  2 135 ? 121.286 90.876  301.452 1.00 180.86 ?  646 LEU D N   1 
ATOM   15597 C CA  . LEU H  2 135 ? 121.449 89.509  301.926 1.00 180.24 ?  646 LEU D CA  1 
ATOM   15598 C C   . LEU H  2 135 ? 122.824 88.947  301.592 1.00 181.26 ?  646 LEU D C   1 
ATOM   15599 O O   . LEU H  2 135 ? 123.453 88.313  302.443 1.00 181.07 ?  646 LEU D O   1 
ATOM   15600 C CB  . LEU H  2 135 ? 120.375 88.610  301.300 1.00 179.41 ?  646 LEU D CB  1 
ATOM   15601 C CG  . LEU H  2 135 ? 118.905 88.970  301.513 1.00 178.32 ?  646 LEU D CG  1 
ATOM   15602 C CD1 . LEU H  2 135 ? 118.009 87.964  300.801 1.00 177.66 ?  646 LEU D CD1 1 
ATOM   15603 C CD2 . LEU H  2 135 ? 118.590 89.034  302.994 1.00 177.34 ?  646 LEU D CD2 1 
ATOM   15604 N N   . GLU H  2 136 ? 123.304 89.172  300.366 1.00 201.63 ?  647 GLU D N   1 
ATOM   15605 C CA  . GLU H  2 136 ? 124.591 88.628  299.938 1.00 203.88 ?  647 GLU D CA  1 
ATOM   15606 C C   . GLU H  2 136 ? 125.766 89.484  300.404 1.00 216.35 ?  647 GLU D C   1 
ATOM   15607 O O   . GLU H  2 136 ? 126.821 88.951  300.766 1.00 217.14 ?  647 GLU D O   1 
ATOM   15608 C CB  . GLU H  2 136 ? 124.620 88.472  298.415 1.00 197.67 ?  647 GLU D CB  1 
ATOM   15609 C CG  . GLU H  2 136 ? 124.237 89.720  297.634 1.00 200.66 ?  647 GLU D CG  1 
ATOM   15610 C CD  . GLU H  2 136 ? 124.349 89.520  296.135 1.00 202.58 ?  647 GLU D CD  1 
ATOM   15611 O OE1 . GLU H  2 136 ? 123.713 90.282  295.375 1.00 203.93 ?  647 GLU D OE1 1 
ATOM   15612 O OE2 . GLU H  2 136 ? 125.082 88.602  295.716 1.00 203.89 -1 647 GLU D OE2 1 
ATOM   15613 N N   . GLU H  2 137 ? 125.598 90.807  300.408 1.00 221.42 ?  648 GLU D N   1 
ATOM   15614 C CA  . GLU H  2 137 ? 126.678 91.738  300.728 1.00 228.06 ?  648 GLU D CA  1 
ATOM   15615 C C   . GLU H  2 137 ? 126.730 92.068  302.219 1.00 225.90 ?  648 GLU D C   1 
ATOM   15616 O O   . GLU H  2 137 ? 127.758 91.860  302.871 1.00 222.10 ?  648 GLU D O   1 
ATOM   15617 C CB  . GLU H  2 137 ? 126.523 93.007  299.877 1.00 241.72 ?  648 GLU D CB  1 
ATOM   15618 C CG  . GLU H  2 137 ? 127.361 94.201  300.315 1.00 253.81 ?  648 GLU D CG  1 
ATOM   15619 C CD  . GLU H  2 137 ? 126.551 95.260  301.041 1.00 260.61 ?  648 GLU D CD  1 
ATOM   15620 O OE1 . GLU H  2 137 ? 125.422 94.956  301.482 1.00 259.60 ?  648 GLU D OE1 1 
ATOM   15621 O OE2 . GLU H  2 137 ? 127.045 96.401  301.165 1.00 266.61 -1 648 GLU D OE2 1 
ATOM   15622 N N   . SER H  2 138 ? 125.631 92.579  302.771 1.00 226.49 ?  649 SER D N   1 
ATOM   15623 C CA  . SER H  2 138 ? 125.633 93.044  304.153 1.00 225.47 ?  649 SER D CA  1 
ATOM   15624 C C   . SER H  2 138 ? 125.812 91.909  305.156 1.00 213.03 ?  649 SER D C   1 
ATOM   15625 O O   . SER H  2 138 ? 126.245 92.158  306.285 1.00 218.38 ?  649 SER D O   1 
ATOM   15626 C CB  . SER H  2 138 ? 124.345 93.813  304.448 1.00 225.97 ?  649 SER D CB  1 
ATOM   15627 O OG  . SER H  2 138 ? 123.253 92.933  304.631 1.00 214.32 ?  649 SER D OG  1 
ATOM   15628 N N   . GLN H  2 139 ? 125.462 90.682  304.783 1.00 204.25 ?  650 GLN D N   1 
ATOM   15629 C CA  . GLN H  2 139 ? 125.462 89.545  305.699 1.00 203.38 ?  650 GLN D CA  1 
ATOM   15630 C C   . GLN H  2 139 ? 126.725 88.696  305.661 1.00 202.37 ?  650 GLN D C   1 
ATOM   15631 O O   . GLN H  2 139 ? 127.673 88.947  306.413 1.00 208.52 ?  650 GLN D O   1 
ATOM   15632 C CB  . GLN H  2 139 ? 124.239 88.670  305.450 1.00 197.37 ?  650 GLN D CB  1 
ATOM   15633 C CG  . GLN H  2 139 ? 122.946 89.391  305.772 1.00 194.42 ?  650 GLN D CG  1 
ATOM   15634 C CD  . GLN H  2 139 ? 122.897 89.844  307.223 1.00 197.14 ?  650 GLN D CD  1 
ATOM   15635 O OE1 . GLN H  2 139 ? 123.307 89.114  308.124 1.00 201.54 ?  650 GLN D OE1 1 
ATOM   15636 N NE2 . GLN H  2 139 ? 122.414 91.061  307.451 1.00 200.87 ?  650 GLN D NE2 1 
ATOM   15637 N N   . ASN H  2 140 ? 126.732 87.671  304.808 1.00 196.52 ?  651 ASN D N   1 
ATOM   15638 C CA  . ASN H  2 140 ? 127.788 86.665  304.797 1.00 192.14 ?  651 ASN D CA  1 
ATOM   15639 C C   . ASN H  2 140 ? 129.172 87.228  304.524 1.00 194.88 ?  651 ASN D C   1 
ATOM   15640 O O   . ASN H  2 140 ? 130.156 86.486  304.620 1.00 195.37 ?  651 ASN D O   1 
ATOM   15641 C CB  . ASN H  2 140 ? 127.488 85.580  303.769 1.00 191.95 ?  651 ASN D CB  1 
ATOM   15642 C CG  . ASN H  2 140 ? 126.320 84.691  304.156 1.00 192.83 ?  651 ASN D CG  1 
ATOM   15643 O OD1 . ASN H  2 140 ? 126.196 83.599  303.642 1.00 193.02 ?  651 ASN D OD1 1 
ATOM   15644 N ND2 . ASN H  2 140 ? 125.467 85.161  305.041 1.00 193.39 ?  651 ASN D ND2 1 
ATOM   15645 N N   . GLN H  2 141 ? 129.277 88.509  304.219 1.00 194.35 ?  652 GLN D N   1 
ATOM   15646 C CA  . GLN H  2 141 ? 130.570 89.152  304.087 1.00 198.40 ?  652 GLN D CA  1 
ATOM   15647 C C   . GLN H  2 141 ? 130.970 89.696  305.445 1.00 207.28 ?  652 GLN D C   1 
ATOM   15648 O O   . GLN H  2 141 ? 132.164 89.804  305.753 1.00 212.49 ?  652 GLN D O   1 
ATOM   15649 C CB  . GLN H  2 141 ? 130.549 90.249  303.027 1.00 200.46 ?  652 GLN D CB  1 
ATOM   15650 C CG  . GLN H  2 141 ? 131.915 90.867  302.819 1.00 209.32 ?  652 GLN D CG  1 
ATOM   15651 C CD  . GLN H  2 141 ? 132.939 89.823  302.386 1.00 205.36 ?  652 GLN D CD  1 
ATOM   15652 O OE1 . GLN H  2 141 ? 132.621 88.896  301.640 1.00 198.46 ?  652 GLN D OE1 1 
ATOM   15653 N NE2 . GLN H  2 141 ? 134.170 89.966  302.863 1.00 207.35 ?  652 GLN D NE2 1 
ATOM   15654 N N   . GLN H  2 142 ? 129.961 89.996  306.265 1.00 206.06 ?  653 GLN D N   1 
ATOM   15655 C CA  . GLN H  2 142 ? 130.114 90.491  307.620 1.00 207.20 ?  653 GLN D CA  1 
ATOM   15656 C C   . GLN H  2 142 ? 129.980 89.366  308.620 1.00 203.24 ?  653 GLN D C   1 
ATOM   15657 O O   . GLN H  2 142 ? 130.624 89.405  309.666 1.00 210.61 ?  653 GLN D O   1 
ATOM   15658 C CB  . GLN H  2 142 ? 128.962 91.463  307.942 1.00 206.68 ?  653 GLN D CB  1 
ATOM   15659 C CG  . GLN H  2 142 ? 129.027 92.919  307.543 1.00 214.95 ?  653 GLN D CG  1 
ATOM   15660 C CD  . GLN H  2 142 ? 129.600 93.776  308.643 1.00 221.40 ?  653 GLN D CD  1 
ATOM   15661 O OE1 . GLN H  2 142 ? 130.806 93.967  308.737 1.00 228.34 ?  653 GLN D OE1 1 
ATOM   15662 N NE2 . GLN H  2 142 ? 128.717 94.294  309.504 1.00 225.91 ?  653 GLN D NE2 1 
ATOM   15663 N N   . GLU H  2 143 ? 129.222 88.323  308.276 1.00 199.20 ?  654 GLU D N   1 
ATOM   15664 C CA  . GLU H  2 143 ? 129.017 87.189  309.170 1.00 194.08 ?  654 GLU D CA  1 
ATOM   15665 C C   . GLU H  2 143 ? 130.203 86.228  309.133 1.00 199.06 ?  654 GLU D C   1 
ATOM   15666 O O   . GLU H  2 143 ? 130.708 85.807  310.180 1.00 205.14 ?  654 GLU D O   1 
ATOM   15667 C CB  . GLU H  2 143 ? 127.706 86.494  308.796 1.00 194.09 ?  654 GLU D CB  1 
ATOM   15668 C CG  . GLU H  2 143 ? 127.373 85.221  309.537 1.00 194.75 ?  654 GLU D CG  1 
ATOM   15669 C CD  . GLU H  2 143 ? 126.073 84.633  309.038 1.00 195.46 ?  654 GLU D CD  1 
ATOM   15670 O OE1 . GLU H  2 143 ? 126.045 83.429  308.725 1.00 195.66 ?  654 GLU D OE1 1 
ATOM   15671 O OE2 . GLU H  2 143 ? 125.139 85.420  308.767 1.00 195.74 -1 654 GLU D OE2 1 
ATOM   15672 N N   . LYS H  2 144 ? 130.655 85.870  307.927 1.00 201.63 ?  655 LYS D N   1 
ATOM   15673 C CA  . LYS H  2 144 ? 131.782 84.948  307.789 1.00 203.56 ?  655 LYS D CA  1 
ATOM   15674 C C   . LYS H  2 144 ? 133.081 85.606  308.234 1.00 212.48 ?  655 LYS D C   1 
ATOM   15675 O O   . LYS H  2 144 ? 133.950 84.947  308.819 1.00 214.08 ?  655 LYS D O   1 
ATOM   15676 C CB  . LYS H  2 144 ? 131.879 84.436  306.354 1.00 198.80 ?  655 LYS D CB  1 
ATOM   15677 C CG  . LYS H  2 144 ? 130.735 83.497  305.987 1.00 191.30 ?  655 LYS D CG  1 
ATOM   15678 C CD  . LYS H  2 144 ? 130.913 82.910  304.600 1.00 191.07 ?  655 LYS D CD  1 
ATOM   15679 C CE  . LYS H  2 144 ? 129.804 81.928  304.245 1.00 191.80 ?  655 LYS D CE  1 
ATOM   15680 N NZ  . LYS H  2 144 ? 130.045 80.567  304.784 1.00 192.18 1  655 LYS D NZ  1 
ATOM   15681 N N   . ASN H  2 145 ? 133.236 86.905  307.953 1.00 218.16 ?  656 ASN D N   1 
ATOM   15682 C CA  . ASN H  2 145 ? 134.421 87.613  308.422 1.00 227.44 ?  656 ASN D CA  1 
ATOM   15683 C C   . ASN H  2 145 ? 134.425 87.678  309.940 1.00 233.35 ?  656 ASN D C   1 
ATOM   15684 O O   . ASN H  2 145 ? 135.495 87.666  310.559 1.00 234.89 ?  656 ASN D O   1 
ATOM   15685 C CB  . ASN H  2 145 ? 134.497 89.007  307.809 1.00 229.64 ?  656 ASN D CB  1 
ATOM   15686 C CG  . ASN H  2 145 ? 135.900 89.582  307.850 1.00 236.71 ?  656 ASN D CG  1 
ATOM   15687 O OD1 . ASN H  2 145 ? 136.697 89.262  308.732 1.00 238.09 ?  656 ASN D OD1 1 
ATOM   15688 N ND2 . ASN H  2 145 ? 136.217 90.423  306.875 1.00 236.84 ?  656 ASN D ND2 1 
ATOM   15689 N N   . GLU H  2 146 ? 133.244 87.750  310.557 1.00 230.94 ?  657 GLU D N   1 
ATOM   15690 C CA  . GLU H  2 146 ? 133.214 87.712  312.011 1.00 228.31 ?  657 GLU D CA  1 
ATOM   15691 C C   . GLU H  2 146 ? 133.692 86.351  312.480 1.00 227.51 ?  657 GLU D C   1 
ATOM   15692 O O   . GLU H  2 146 ? 134.433 86.268  313.461 1.00 233.17 ?  657 GLU D O   1 
ATOM   15693 C CB  . GLU H  2 146 ? 131.825 88.017  312.583 1.00 225.04 ?  657 GLU D CB  1 
ATOM   15694 C CG  . GLU H  2 146 ? 131.326 89.446  312.397 1.00 229.39 ?  657 GLU D CG  1 
ATOM   15695 C CD  . GLU H  2 146 ? 132.155 90.498  313.111 1.00 243.71 ?  657 GLU D CD  1 
ATOM   15696 O OE1 . GLU H  2 146 ? 132.910 90.152  314.042 1.00 245.83 ?  657 GLU D OE1 1 
ATOM   15697 O OE2 . GLU H  2 146 ? 132.045 91.684  312.732 1.00 247.65 -1 657 GLU D OE2 1 
ATOM   15698 N N   . GLN H  2 147 ? 133.383 85.291  311.719 1.00 232.81 ?  658 GLN D N   1 
ATOM   15699 C CA  . GLN H  2 147 ? 133.779 83.952  312.140 1.00 229.62 ?  658 GLN D CA  1 
ATOM   15700 C C   . GLN H  2 147 ? 135.284 83.772  312.052 1.00 232.23 ?  658 GLN D C   1 
ATOM   15701 O O   . GLN H  2 147 ? 135.853 83.009  312.839 1.00 232.12 ?  658 GLN D O   1 
ATOM   15702 C CB  . GLN H  2 147 ? 133.118 82.884  311.265 1.00 220.22 ?  658 GLN D CB  1 
ATOM   15703 C CG  . GLN H  2 147 ? 132.021 82.061  311.916 1.00 214.75 ?  658 GLN D CG  1 
ATOM   15704 C CD  . GLN H  2 147 ? 131.384 81.083  310.936 1.00 205.10 ?  658 GLN D CD  1 
ATOM   15705 O OE1 . GLN H  2 147 ? 131.777 81.009  309.769 1.00 205.02 ?  658 GLN D OE1 1 
ATOM   15706 N NE2 . GLN H  2 147 ? 130.421 80.303  311.417 1.00 196.92 ?  658 GLN D NE2 1 
ATOM   15707 N N   . ASP H  2 148 ? 135.950 84.439  311.106 1.00 230.25 ?  659 ASP D N   1 
ATOM   15708 C CA  . ASP H  2 148 ? 137.400 84.309  311.078 1.00 232.39 ?  659 ASP D CA  1 
ATOM   15709 C C   . ASP H  2 148 ? 137.990 84.929  312.333 1.00 237.82 ?  659 ASP D C   1 
ATOM   15710 O O   . ASP H  2 148 ? 139.060 84.519  312.797 1.00 238.51 ?  659 ASP D O   1 
ATOM   15711 C CB  . ASP H  2 148 ? 137.968 84.981  309.831 1.00 230.06 ?  659 ASP D CB  1 
ATOM   15712 C CG  . ASP H  2 148 ? 139.470 84.839  309.728 1.00 231.62 ?  659 ASP D CG  1 
ATOM   15713 O OD1 . ASP H  2 148 ? 139.929 83.809  309.194 1.00 226.81 ?  659 ASP D OD1 1 
ATOM   15714 O OD2 . ASP H  2 148 ? 140.190 85.757  310.179 1.00 238.39 -1 659 ASP D OD2 1 
ATOM   15715 N N   . LEU H  2 149 ? 137.294 85.918  312.885 1.00 226.72 ?  660 LEU D N   1 
ATOM   15716 C CA  . LEU H  2 149 ? 137.691 86.553  314.130 1.00 229.11 ?  660 LEU D CA  1 
ATOM   15717 C C   . LEU H  2 149 ? 137.227 85.743  315.332 1.00 231.87 ?  660 LEU D C   1 
ATOM   15718 O O   . LEU H  2 149 ? 137.804 85.861  316.416 1.00 232.92 ?  660 LEU D O   1 
ATOM   15719 C CB  . LEU H  2 149 ? 137.188 87.996  314.214 1.00 231.39 ?  660 LEU D CB  1 
ATOM   15720 C CG  . LEU H  2 149 ? 138.095 89.069  313.594 1.00 230.37 ?  660 LEU D CG  1 
ATOM   15721 C CD1 . LEU H  2 149 ? 138.384 88.796  312.126 1.00 226.21 ?  660 LEU D CD1 1 
ATOM   15722 C CD2 . LEU H  2 149 ? 137.514 90.459  313.783 1.00 233.29 ?  660 LEU D CD2 1 
ATOM   15723 N N   . LEU H  2 150 ? 136.161 84.956  315.173 1.00 230.89 ?  661 LEU D N   1 
ATOM   15724 C CA  . LEU H  2 150 ? 135.616 84.192  316.282 1.00 231.21 ?  661 LEU D CA  1 
ATOM   15725 C C   . LEU H  2 150 ? 136.301 82.836  316.404 1.00 227.39 ?  661 LEU D C   1 
ATOM   15726 O O   . LEU H  2 150 ? 136.206 82.186  317.454 1.00 227.09 ?  661 LEU D O   1 
ATOM   15727 C CB  . LEU H  2 150 ? 134.110 83.994  316.079 1.00 228.02 ?  661 LEU D CB  1 
ATOM   15728 C CG  . LEU H  2 150 ? 133.374 85.347  315.961 1.00 231.20 ?  661 LEU D CG  1 
ATOM   15729 C CD1 . LEU H  2 150 ? 131.888 85.251  315.551 1.00 224.76 ?  661 LEU D CD1 1 
ATOM   15730 C CD2 . LEU H  2 150 ? 133.678 86.461  316.942 1.00 239.14 ?  661 LEU D CD2 1 
ATOM   15731 N N   . ALA H  2 151 ? 136.978 82.408  315.336 1.00 227.24 ?  662 ALA D N   1 
ATOM   15732 C CA  . ALA H  2 151 ? 137.643 81.120  315.207 1.00 223.80 ?  662 ALA D CA  1 
ATOM   15733 C C   . ALA H  2 151 ? 139.133 81.183  315.527 1.00 226.32 ?  662 ALA D C   1 
ATOM   15734 O O   . ALA H  2 151 ? 139.763 80.126  315.651 1.00 224.80 ?  662 ALA D O   1 
ATOM   15735 C CB  . ALA H  2 151 ? 137.449 80.559  313.791 1.00 219.30 ?  662 ALA D CB  1 
ATOM   15736 N N   . LEU H  2 152 ? 139.709 82.386  315.663 1.00 228.71 ?  663 LEU D N   1 
ATOM   15737 C CA  . LEU H  2 152 ? 141.130 82.533  315.957 1.00 229.30 ?  663 LEU D CA  1 
ATOM   15738 C C   . LEU H  2 152 ? 141.449 82.341  317.436 1.00 237.32 ?  663 LEU D C   1 
ATOM   15739 O O   . LEU H  2 152 ? 142.599 82.032  317.771 1.00 235.85 ?  663 LEU D O   1 
ATOM   15740 C CB  . LEU H  2 152 ? 141.628 83.927  315.521 1.00 231.44 ?  663 LEU D CB  1 
ATOM   15741 C CG  . LEU H  2 152 ? 141.009 85.137  316.267 1.00 232.36 ?  663 LEU D CG  1 
ATOM   15742 C CD1 . LEU H  2 152 ? 141.724 85.575  317.531 1.00 230.41 ?  663 LEU D CD1 1 
ATOM   15743 C CD2 . LEU H  2 152 ? 140.919 86.371  315.382 1.00 225.27 ?  663 LEU D CD2 1 
ATOM   15744 N N   . ASP H  2 153 ? 140.483 82.534  318.325 1.00 239.86 ?  664 ASP D N   1 
ATOM   15745 C CA  . ASP H  2 153 ? 140.720 82.354  319.757 1.00 239.51 ?  664 ASP D CA  1 
ATOM   15746 C C   . ASP H  2 153 ? 140.365 80.938  320.240 1.00 236.29 ?  664 ASP D C   1 
ATOM   15747 O O   . ASP H  2 153 ? 140.328 80.659  321.443 1.00 236.09 ?  664 ASP D O   1 
ATOM   15748 C CB  . ASP H  2 153 ? 139.957 83.423  320.544 1.00 240.51 ?  664 ASP D CB  1 
ATOM   15749 C CG  . ASP H  2 153 ? 138.478 83.425  320.239 1.00 240.53 ?  664 ASP D CG  1 
ATOM   15750 O OD1 . ASP H  2 153 ? 137.968 82.391  319.767 1.00 240.02 ?  664 ASP D OD1 1 
ATOM   15751 O OD2 . ASP H  2 153 ? 137.830 84.475  320.439 1.00 246.26 -1 664 ASP D OD2 1 
ATOM   15752 N N   . ASP I  5 1   ? 77.106  54.481  316.220 1.00 209.58 ?  1   ASP H N   1 
ATOM   15753 C CA  . ASP I  5 1   ? 77.004  55.489  315.172 1.00 202.23 ?  1   ASP H CA  1 
ATOM   15754 C C   . ASP I  5 1   ? 76.172  56.674  315.643 1.00 201.60 ?  1   ASP H C   1 
ATOM   15755 O O   . ASP I  5 1   ? 75.541  56.621  316.699 1.00 206.47 ?  1   ASP H O   1 
ATOM   15756 C CB  . ASP I  5 1   ? 76.391  54.890  313.906 1.00 207.03 ?  1   ASP H CB  1 
ATOM   15757 C CG  . ASP I  5 1   ? 77.017  53.565  313.525 1.00 217.18 ?  1   ASP H CG  1 
ATOM   15758 O OD1 . ASP I  5 1   ? 78.055  53.195  314.115 1.00 208.55 ?  1   ASP H OD1 1 
ATOM   15759 O OD2 . ASP I  5 1   ? 76.463  52.891  312.635 1.00 231.00 -1 1   ASP H OD2 1 
ATOM   15760 N N   . ILE I  5 2   ? 76.195  57.751  314.861 1.00 199.31 ?  2   ILE H N   1 
ATOM   15761 C CA  . ILE I  5 2   ? 75.361  58.924  315.092 1.00 198.60 ?  2   ILE H CA  1 
ATOM   15762 C C   . ILE I  5 2   ? 74.216  58.902  314.089 1.00 199.50 ?  2   ILE H C   1 
ATOM   15763 O O   . ILE I  5 2   ? 74.435  58.674  312.892 1.00 198.87 ?  2   ILE H O   1 
ATOM   15764 C CB  . ILE I  5 2   ? 76.182  60.221  314.980 1.00 195.38 ?  2   ILE H CB  1 
ATOM   15765 C CG1 . ILE I  5 2   ? 77.209  60.303  316.113 1.00 194.62 ?  2   ILE H CG1 1 
ATOM   15766 C CG2 . ILE I  5 2   ? 75.277  61.448  315.009 1.00 194.58 ?  2   ILE H CG2 1 
ATOM   15767 C CD1 . ILE I  5 2   ? 78.204  61.441  315.957 1.00 191.41 ?  2   ILE H CD1 1 
ATOM   15768 N N   . GLN I  5 3   ? 72.995  59.117  314.575 1.00 201.03 ?  3   GLN H N   1 
ATOM   15769 C CA  . GLN I  5 3   ? 71.801  59.138  313.740 1.00 202.05 ?  3   GLN H CA  1 
ATOM   15770 C C   . GLN I  5 3   ? 71.374  60.572  313.449 1.00 200.15 ?  3   GLN H C   1 
ATOM   15771 O O   . GLN I  5 3   ? 71.294  61.401  314.363 1.00 199.50 ?  3   GLN H O   1 
ATOM   15772 C CB  . GLN I  5 3   ? 70.646  58.383  314.402 1.00 209.56 ?  3   GLN H CB  1 
ATOM   15773 C CG  . GLN I  5 3   ? 70.786  56.867  314.412 1.00 219.57 ?  3   GLN H CG  1 
ATOM   15774 C CD  . GLN I  5 3   ? 71.671  56.360  315.535 1.00 216.62 ?  3   GLN H CD  1 
ATOM   15775 O OE1 . GLN I  5 3   ? 71.520  56.762  316.688 1.00 212.69 ?  3   GLN H OE1 1 
ATOM   15776 N NE2 . GLN I  5 3   ? 72.593  55.461  315.203 1.00 219.47 ?  3   GLN H NE2 1 
ATOM   15777 N N   . LEU I  5 4   ? 71.104  60.854  312.176 1.00 199.31 ?  4   LEU H N   1 
ATOM   15778 C CA  . LEU I  5 4   ? 70.539  62.119  311.726 1.00 197.81 ?  4   LEU H CA  1 
ATOM   15779 C C   . LEU I  5 4   ? 69.079  61.914  311.343 1.00 199.86 ?  4   LEU H C   1 
ATOM   15780 O O   . LEU I  5 4   ? 68.765  61.054  310.513 1.00 201.14 ?  4   LEU H O   1 
ATOM   15781 C CB  . LEU I  5 4   ? 71.319  62.685  310.537 1.00 195.21 ?  4   LEU H CB  1 
ATOM   15782 C CG  . LEU I  5 4   ? 72.805  62.998  310.728 1.00 192.88 ?  4   LEU H CG  1 
ATOM   15783 C CD1 . LEU I  5 4   ? 73.420  63.520  309.433 1.00 190.55 ?  4   LEU H CD1 1 
ATOM   15784 C CD2 . LEU I  5 4   ? 72.990  64.005  311.854 1.00 191.69 ?  4   LEU H CD2 1 
ATOM   15785 N N   . THR I  5 5   ? 68.196  62.705  311.945 1.00 200.19 ?  5   THR H N   1 
ATOM   15786 C CA  . THR I  5 5   ? 66.760  62.634  311.699 1.00 202.11 ?  5   THR H CA  1 
ATOM   15787 C C   . THR I  5 5   ? 66.302  63.918  311.020 1.00 200.38 ?  5   THR H C   1 
ATOM   15788 O O   . THR I  5 5   ? 66.473  65.011  311.571 1.00 198.81 ?  5   THR H O   1 
ATOM   15789 C CB  . THR I  5 5   ? 65.993  62.416  313.001 1.00 204.29 ?  5   THR H CB  1 
ATOM   15790 O OG1 . THR I  5 5   ? 66.499  61.250  313.664 1.00 205.80 ?  5   THR H OG1 1 
ATOM   15791 C CG2 . THR I  5 5   ? 64.518  62.223  312.708 1.00 206.46 ?  5   THR H CG2 1 
ATOM   15792 N N   . GLN I  5 6   ? 65.722  63.784  309.831 1.00 200.70 ?  6   GLN H N   1 
ATOM   15793 C CA  . GLN I  5 6   ? 65.240  64.924  309.066 1.00 199.22 ?  6   GLN H CA  1 
ATOM   15794 C C   . GLN I  5 6   ? 63.729  65.066  309.187 1.00 201.19 ?  6   GLN H C   1 
ATOM   15795 O O   . GLN I  5 6   ? 62.999  64.072  309.220 1.00 203.73 ?  6   GLN H O   1 
ATOM   15796 C CB  . GLN I  5 6   ? 65.636  64.797  307.595 1.00 198.05 ?  6   GLN H CB  1 
ATOM   15797 C CG  . GLN I  5 6   ? 67.129  64.927  307.375 1.00 195.68 ?  6   GLN H CG  1 
ATOM   15798 C CD  . GLN I  5 6   ? 67.510  64.945  305.913 1.00 194.36 ?  6   GLN H CD  1 
ATOM   15799 O OE1 . GLN I  5 6   ? 68.235  64.071  305.437 1.00 194.45 ?  6   GLN H OE1 1 
ATOM   15800 N NE2 . GLN I  5 6   ? 67.027  65.948  305.190 1.00 193.16 ?  6   GLN H NE2 1 
ATOM   15801 N N   . SER I  5 7   ? 63.269  66.314  309.245 1.00 220.24 ?  7   SER H N   1 
ATOM   15802 C CA  . SER I  5 7   ? 61.842  66.614  309.311 1.00 223.21 ?  7   SER H CA  1 
ATOM   15803 C C   . SER I  5 7   ? 61.489  67.879  308.523 1.00 215.98 ?  7   SER H C   1 
ATOM   15804 O O   . SER I  5 7   ? 62.254  68.845  308.517 1.00 207.68 ?  7   SER H O   1 
ATOM   15805 C CB  . SER I  5 7   ? 61.397  66.766  310.768 1.00 224.40 ?  7   SER H CB  1 
ATOM   15806 O OG  . SER I  5 7   ? 62.131  67.786  311.424 1.00 216.81 ?  7   SER H OG  1 
ATOM   15807 N N   . PRO I  5 8   ? 60.321  67.877  307.854 1.00 215.19 ?  8   PRO H N   1 
ATOM   15808 C CA  . PRO I  5 8   ? 59.436  66.713  307.728 1.00 224.69 ?  8   PRO H CA  1 
ATOM   15809 C C   . PRO I  5 8   ? 59.961  65.699  306.718 1.00 229.02 ?  8   PRO H C   1 
ATOM   15810 O O   . PRO I  5 8   ? 60.878  66.019  305.965 1.00 223.73 ?  8   PRO H O   1 
ATOM   15811 C CB  . PRO I  5 8   ? 58.123  67.331  307.250 1.00 224.23 ?  8   PRO H CB  1 
ATOM   15812 C CG  . PRO I  5 8   ? 58.553  68.507  306.455 1.00 214.86 ?  8   PRO H CG  1 
ATOM   15813 C CD  . PRO I  5 8   ? 59.770  69.056  307.163 1.00 211.19 ?  8   PRO H CD  1 
ATOM   15814 N N   . SER I  5 9   ? 59.394  64.490  306.710 1.00 236.50 ?  9   SER H N   1 
ATOM   15815 C CA  . SER I  5 9   ? 59.787  63.514  305.700 1.00 241.98 ?  9   SER H CA  1 
ATOM   15816 C C   . SER I  5 9   ? 59.233  63.882  304.330 1.00 239.80 ?  9   SER H C   1 
ATOM   15817 O O   . SER I  5 9   ? 59.879  63.615  303.310 1.00 238.99 ?  9   SER H O   1 
ATOM   15818 C CB  . SER I  5 9   ? 59.328  62.113  306.109 1.00 252.97 ?  9   SER H CB  1 
ATOM   15819 O OG  . SER I  5 9   ? 60.121  61.603  307.169 1.00 254.96 ?  9   SER H OG  1 
ATOM   15820 N N   . PHE I  5 10  ? 58.050  64.491  304.287 1.00 231.81 ?  10  PHE H N   1 
ATOM   15821 C CA  . PHE I  5 10  ? 57.444  64.941  303.040 1.00 228.71 ?  10  PHE H CA  1 
ATOM   15822 C C   . PHE I  5 10  ? 56.829  66.313  303.268 1.00 221.21 ?  10  PHE H C   1 
ATOM   15823 O O   . PHE I  5 10  ? 55.901  66.455  304.070 1.00 223.45 ?  10  PHE H O   1 
ATOM   15824 C CB  . PHE I  5 10  ? 56.401  63.939  302.533 1.00 237.47 ?  10  PHE H CB  1 
ATOM   15825 C CG  . PHE I  5 10  ? 56.976  62.588  302.209 1.00 245.50 ?  10  PHE H CG  1 
ATOM   15826 C CD1 . PHE I  5 10  ? 56.996  61.575  303.155 1.00 253.61 ?  10  PHE H CD1 1 
ATOM   15827 C CD2 . PHE I  5 10  ? 57.516  62.339  300.958 1.00 244.35 ?  10  PHE H CD2 1 
ATOM   15828 C CE1 . PHE I  5 10  ? 57.535  60.336  302.852 1.00 261.51 ?  10  PHE H CE1 1 
ATOM   15829 C CE2 . PHE I  5 10  ? 58.056  61.106  300.650 1.00 252.03 ?  10  PHE H CE2 1 
ATOM   15830 C CZ  . PHE I  5 10  ? 58.066  60.103  301.598 1.00 261.32 ?  10  PHE H CZ  1 
ATOM   15831 N N   . LEU I  5 11  ? 57.347  67.311  302.557 1.00 243.08 ?  11  LEU H N   1 
ATOM   15832 C CA  . LEU I  5 11  ? 56.946  68.703  302.703 1.00 235.60 ?  11  LEU H CA  1 
ATOM   15833 C C   . LEU I  5 11  ? 56.259  69.154  301.421 1.00 234.39 ?  11  LEU H C   1 
ATOM   15834 O O   . LEU I  5 11  ? 56.826  69.023  300.331 1.00 229.41 ?  11  LEU H O   1 
ATOM   15835 C CB  . LEU I  5 11  ? 58.163  69.587  303.000 1.00 229.12 ?  11  LEU H CB  1 
ATOM   15836 C CG  . LEU I  5 11  ? 57.960  70.982  303.599 1.00 230.94 ?  11  LEU H CG  1 
ATOM   15837 C CD1 . LEU I  5 11  ? 59.206  71.411  304.356 1.00 226.87 ?  11  LEU H CD1 1 
ATOM   15838 C CD2 . LEU I  5 11  ? 57.617  72.005  302.525 1.00 229.61 ?  11  LEU H CD2 1 
ATOM   15839 N N   . SER I  5 12  ? 55.041  69.672  301.553 1.00 240.82 ?  12  SER H N   1 
ATOM   15840 C CA  . SER I  5 12  ? 54.291  70.211  300.426 1.00 241.36 ?  12  SER H CA  1 
ATOM   15841 C C   . SER I  5 12  ? 54.386  71.732  300.434 1.00 240.78 ?  12  SER H C   1 
ATOM   15842 O O   . SER I  5 12  ? 54.127  72.369  301.461 1.00 244.47 ?  12  SER H O   1 
ATOM   15843 C CB  . SER I  5 12  ? 52.828  69.765  300.490 1.00 248.40 ?  12  SER H CB  1 
ATOM   15844 O OG  . SER I  5 12  ? 52.721  68.351  300.443 1.00 249.05 ?  12  SER H OG  1 
ATOM   15845 N N   . ALA I  5 13  ? 54.755  72.308  299.291 1.00 260.21 ?  13  ALA H N   1 
ATOM   15846 C CA  . ALA I  5 13  ? 54.893  73.753  299.178 1.00 259.59 ?  13  ALA H CA  1 
ATOM   15847 C C   . ALA I  5 13  ? 54.657  74.175  297.735 1.00 257.99 ?  13  ALA H C   1 
ATOM   15848 O O   . ALA I  5 13  ? 54.727  73.364  296.807 1.00 255.41 ?  13  ALA H O   1 
ATOM   15849 C CB  . ALA I  5 13  ? 56.272  74.227  299.654 1.00 254.15 ?  13  ALA H CB  1 
ATOM   15850 N N   . SER I  5 14  ? 54.381  75.463  297.563 1.00 262.76 ?  14  SER H N   1 
ATOM   15851 C CA  . SER I  5 14  ? 54.134  76.070  296.264 1.00 261.99 ?  14  SER H CA  1 
ATOM   15852 C C   . SER I  5 14  ? 55.361  76.837  295.792 1.00 255.69 ?  14  SER H C   1 
ATOM   15853 O O   . SER I  5 14  ? 56.200  77.254  296.594 1.00 252.92 ?  14  SER H O   1 
ATOM   15854 C CB  . SER I  5 14  ? 52.930  77.012  296.319 1.00 268.58 ?  14  SER H CB  1 
ATOM   15855 O OG  . SER I  5 14  ? 51.759  76.317  296.701 1.00 274.48 ?  14  SER H OG  1 
ATOM   15856 N N   . VAL I  5 15  ? 55.473  76.987  294.470 1.00 248.75 ?  15  VAL H N   1 
ATOM   15857 C CA  . VAL I  5 15  ? 56.483  77.873  293.905 1.00 243.74 ?  15  VAL H CA  1 
ATOM   15858 C C   . VAL I  5 15  ? 56.369  79.244  294.554 1.00 246.37 ?  15  VAL H C   1 
ATOM   15859 O O   . VAL I  5 15  ? 55.284  79.835  294.605 1.00 252.26 ?  15  VAL H O   1 
ATOM   15860 C CB  . VAL I  5 15  ? 56.324  77.953  292.376 1.00 242.56 ?  15  VAL H CB  1 
ATOM   15861 C CG1 . VAL I  5 15  ? 57.271  78.993  291.791 1.00 238.30 ?  15  VAL H CG1 1 
ATOM   15862 C CG2 . VAL I  5 15  ? 56.565  76.590  291.749 1.00 239.57 ?  15  VAL H CG2 1 
ATOM   15863 N N   . GLY I  5 16  ? 57.496  79.759  295.047 1.00 248.51 ?  16  GLY H N   1 
ATOM   15864 C CA  . GLY I  5 16  ? 57.535  81.041  295.717 1.00 250.39 ?  16  GLY H CA  1 
ATOM   15865 C C   . GLY I  5 16  ? 57.588  80.985  297.231 1.00 252.22 ?  16  GLY H C   1 
ATOM   15866 O O   . GLY I  5 16  ? 57.895  82.007  297.857 1.00 252.48 ?  16  GLY H O   1 
ATOM   15867 N N   . ASP I  5 17  ? 57.301  79.834  297.835 1.00 245.90 ?  17  ASP H N   1 
ATOM   15868 C CA  . ASP I  5 17  ? 57.301  79.719  299.288 1.00 248.28 ?  17  ASP H CA  1 
ATOM   15869 C C   . ASP I  5 17  ? 58.711  79.786  299.869 1.00 242.32 ?  17  ASP H C   1 
ATOM   15870 O O   . ASP I  5 17  ? 59.690  79.362  299.249 1.00 236.09 ?  17  ASP H O   1 
ATOM   15871 C CB  . ASP I  5 17  ? 56.647  78.406  299.725 1.00 251.63 ?  17  ASP H CB  1 
ATOM   15872 C CG  . ASP I  5 17  ? 55.135  78.453  299.664 1.00 259.11 ?  17  ASP H CG  1 
ATOM   15873 O OD1 . ASP I  5 17  ? 54.577  79.524  299.350 1.00 262.08 ?  17  ASP H OD1 1 
ATOM   15874 O OD2 . ASP I  5 17  ? 54.504  77.415  299.958 1.00 262.21 -1 17  ASP H OD2 1 
ATOM   15875 N N   . LYS I  5 18  ? 58.801  80.339  301.077 1.00 233.67 ?  18  LYS H N   1 
ATOM   15876 C CA  . LYS I  5 18  ? 59.963  80.168  301.939 1.00 229.23 ?  18  LYS H CA  1 
ATOM   15877 C C   . LYS I  5 18  ? 59.731  78.923  302.786 1.00 231.37 ?  18  LYS H C   1 
ATOM   15878 O O   . LYS I  5 18  ? 58.712  78.824  303.477 1.00 237.85 ?  18  LYS H O   1 
ATOM   15879 C CB  . LYS I  5 18  ? 60.170  81.392  302.832 1.00 230.68 ?  18  LYS H CB  1 
ATOM   15880 C CG  . LYS I  5 18  ? 61.303  81.241  303.838 1.00 226.62 ?  18  LYS H CG  1 
ATOM   15881 C CD  . LYS I  5 18  ? 61.454  82.480  304.708 1.00 228.35 ?  18  LYS H CD  1 
ATOM   15882 C CE  . LYS I  5 18  ? 62.592  82.319  305.704 1.00 224.18 ?  18  LYS H CE  1 
ATOM   15883 N NZ  . LYS I  5 18  ? 62.867  83.584  306.435 1.00 224.84 1  18  LYS H NZ  1 
ATOM   15884 N N   . VAL I  5 19  ? 60.666  77.978  302.740 1.00 237.80 ?  19  VAL H N   1 
ATOM   15885 C CA  . VAL I  5 19  ? 60.534  76.740  303.496 1.00 237.30 ?  19  VAL H CA  1 
ATOM   15886 C C   . VAL I  5 19  ? 61.835  76.446  304.227 1.00 233.04 ?  19  VAL H C   1 
ATOM   15887 O O   . VAL I  5 19  ? 62.925  76.815  303.779 1.00 228.63 ?  19  VAL H O   1 
ATOM   15888 C CB  . VAL I  5 19  ? 60.141  75.548  302.592 1.00 237.19 ?  19  VAL H CB  1 
ATOM   15889 C CG1 . VAL I  5 19  ? 58.776  75.775  301.973 1.00 243.23 ?  19  VAL H CG1 1 
ATOM   15890 C CG2 . VAL I  5 19  ? 61.183  75.334  301.510 1.00 230.48 ?  19  VAL H CG2 1 
ATOM   15891 N N   . THR I  5 20  ? 61.705  75.777  305.372 1.00 222.24 ?  20  THR H N   1 
ATOM   15892 C CA  . THR I  5 20  ? 62.831  75.384  306.206 1.00 219.26 ?  20  THR H CA  1 
ATOM   15893 C C   . THR I  5 20  ? 62.689  73.910  306.561 1.00 219.04 ?  20  THR H C   1 
ATOM   15894 O O   . THR I  5 20  ? 61.628  73.483  307.028 1.00 223.76 ?  20  THR H O   1 
ATOM   15895 C CB  . THR I  5 20  ? 62.894  76.237  307.482 1.00 223.25 ?  20  THR H CB  1 
ATOM   15896 O OG1 . THR I  5 20  ? 63.050  77.620  307.137 1.00 223.71 ?  20  THR H OG1 1 
ATOM   15897 C CG2 . THR I  5 20  ? 64.053  75.806  308.357 1.00 220.68 ?  20  THR H CG2 1 
ATOM   15898 N N   . ILE I  5 21  ? 63.748  73.137  306.335 1.00 212.28 ?  21  ILE H N   1 
ATOM   15899 C CA  . ILE I  5 21  ? 63.774  71.725  306.695 1.00 212.20 ?  21  ILE H CA  1 
ATOM   15900 C C   . ILE I  5 21  ? 64.825  71.528  307.776 1.00 211.06 ?  21  ILE H C   1 
ATOM   15901 O O   . ILE I  5 21  ? 65.793  72.289  307.874 1.00 208.09 ?  21  ILE H O   1 
ATOM   15902 C CB  . ILE I  5 21  ? 64.043  70.816  305.475 1.00 208.07 ?  21  ILE H CB  1 
ATOM   15903 C CG1 . ILE I  5 21  ? 65.438  71.074  304.906 1.00 202.14 ?  21  ILE H CG1 1 
ATOM   15904 C CG2 . ILE I  5 21  ? 62.979  71.031  304.407 1.00 209.68 ?  21  ILE H CG2 1 
ATOM   15905 C CD1 . ILE I  5 21  ? 65.801  70.163  303.756 1.00 198.41 ?  21  ILE H CD1 1 
ATOM   15906 N N   . THR I  5 22  ? 64.630  70.498  308.592 1.00 205.79 ?  22  THR H N   1 
ATOM   15907 C CA  . THR I  5 22  ? 65.374  70.329  309.831 1.00 206.58 ?  22  THR H CA  1 
ATOM   15908 C C   . THR I  5 22  ? 66.156  69.024  309.812 1.00 203.94 ?  22  THR H C   1 
ATOM   15909 O O   . THR I  5 22  ? 65.678  68.010  309.295 1.00 204.14 ?  22  THR H O   1 
ATOM   15910 C CB  . THR I  5 22  ? 64.423  70.356  311.031 1.00 213.54 ?  22  THR H CB  1 
ATOM   15911 O OG1 . THR I  5 22  ? 63.799  71.643  311.110 1.00 216.26 ?  22  THR H OG1 1 
ATOM   15912 C CG2 . THR I  5 22  ? 65.169  70.077  312.329 1.00 215.06 ?  22  THR H CG2 1 
ATOM   15913 N N   . CYS I  5 23  ? 67.367  69.067  310.367 1.00 206.13 ?  23  CYS H N   1 
ATOM   15914 C CA  . CYS I  5 23  ? 68.216  67.895  310.539 1.00 204.44 ?  23  CYS H CA  1 
ATOM   15915 C C   . CYS I  5 23  ? 68.689  67.874  311.985 1.00 207.50 ?  23  CYS H C   1 
ATOM   15916 O O   . CYS I  5 23  ? 69.305  68.838  312.451 1.00 206.68 ?  23  CYS H O   1 
ATOM   15917 C CB  . CYS I  5 23  ? 69.401  67.936  309.565 1.00 197.92 ?  23  CYS H CB  1 
ATOM   15918 S SG  . CYS I  5 23  ? 70.594  66.560  309.644 1.00 195.60 ?  23  CYS H SG  1 
ATOM   15919 N N   . ARG I  5 24  ? 68.397  66.786  312.695 1.00 197.71 ?  24  ARG H N   1 
ATOM   15920 C CA  . ARG I  5 24  ? 68.794  66.630  314.087 1.00 201.28 ?  24  ARG H CA  1 
ATOM   15921 C C   . ARG I  5 24  ? 69.782  65.484  314.237 1.00 199.88 ?  24  ARG H C   1 
ATOM   15922 O O   . ARG I  5 24  ? 69.596  64.409  313.661 1.00 199.50 ?  24  ARG H O   1 
ATOM   15923 C CB  . ARG I  5 24  ? 67.584  66.383  314.993 1.00 208.46 ?  24  ARG H CB  1 
ATOM   15924 C CG  . ARG I  5 24  ? 66.564  67.502  314.997 1.00 211.12 ?  24  ARG H CG  1 
ATOM   15925 C CD  . ARG I  5 24  ? 65.613  67.340  316.169 1.00 218.78 ?  24  ARG H CD  1 
ATOM   15926 N NE  . ARG I  5 24  ? 66.207  67.855  317.398 1.00 221.37 ?  24  ARG H NE  1 
ATOM   15927 C CZ  . ARG I  5 24  ? 65.875  69.013  317.958 1.00 224.46 ?  24  ARG H CZ  1 
ATOM   15928 N NH1 . ARG I  5 24  ? 64.939  69.770  317.404 1.00 225.50 1  24  ARG H NH1 1 
ATOM   15929 N NH2 . ARG I  5 24  ? 66.471  69.410  319.076 1.00 226.77 ?  24  ARG H NH2 1 
ATOM   15930 N N   . ALA I  5 25  ? 70.829  65.722  315.019 1.00 196.26 ?  25  ALA H N   1 
ATOM   15931 C CA  . ALA I  5 25  ? 71.843  64.718  315.300 1.00 195.54 ?  25  ALA H CA  1 
ATOM   15932 C C   . ALA I  5 25  ? 71.647  64.144  316.695 1.00 202.18 ?  25  ALA H C   1 
ATOM   15933 O O   . ALA I  5 25  ? 71.310  64.869  317.636 1.00 205.90 ?  25  ALA H O   1 
ATOM   15934 C CB  . ALA I  5 25  ? 73.247  65.307  315.182 1.00 190.45 ?  25  ALA H CB  1 
ATOM   15935 N N   . SER I  5 26  ? 71.868  62.835  316.823 1.00 197.90 ?  26  SER H N   1 
ATOM   15936 C CA  . SER I  5 26  ? 71.747  62.189  318.124 1.00 204.68 ?  26  SER H CA  1 
ATOM   15937 C C   . SER I  5 26  ? 72.902  62.544  319.050 1.00 206.44 ?  26  SER H C   1 
ATOM   15938 O O   . SER I  5 26  ? 72.766  62.404  320.269 1.00 212.83 ?  26  SER H O   1 
ATOM   15939 C CB  . SER I  5 26  ? 71.666  60.670  317.960 1.00 207.16 ?  26  SER H CB  1 
ATOM   15940 O OG  . SER I  5 26  ? 72.864  60.142  317.413 1.00 202.71 ?  26  SER H OG  1 
ATOM   15941 N N   . GLN I  5 27  ? 74.033  62.984  318.498 1.00 197.51 ?  27  GLN H N   1 
ATOM   15942 C CA  . GLN I  5 27  ? 75.163  63.470  319.276 1.00 196.88 ?  27  GLN H CA  1 
ATOM   15943 C C   . GLN I  5 27  ? 75.692  64.738  318.618 1.00 190.43 ?  27  GLN H C   1 
ATOM   15944 O O   . GLN I  5 27  ? 75.398  65.021  317.455 1.00 185.95 ?  27  GLN H O   1 
ATOM   15945 C CB  . GLN I  5 27  ? 76.271  62.411  319.383 1.00 196.64 ?  27  GLN H CB  1 
ATOM   15946 C CG  . GLN I  5 27  ? 75.949  61.254  320.320 1.00 203.94 ?  27  GLN H CG  1 
ATOM   15947 C CD  . GLN I  5 27  ? 76.055  61.632  321.786 1.00 209.45 ?  27  GLN H CD  1 
ATOM   15948 O OE1 . GLN I  5 27  ? 76.530  62.715  322.130 1.00 207.36 ?  27  GLN H OE1 1 
ATOM   15949 N NE2 . GLN I  5 27  ? 75.620  60.731  322.660 1.00 218.66 ?  27  GLN H NE2 1 
ATOM   15950 N N   . GLY I  5 28  ? 76.476  65.503  319.372 1.00 180.68 ?  28  GLY H N   1 
ATOM   15951 C CA  . GLY I  5 28  ? 77.023  66.749  318.848 1.00 179.20 ?  28  GLY H CA  1 
ATOM   15952 C C   . GLY I  5 28  ? 78.022  66.492  317.733 1.00 178.22 ?  28  GLY H C   1 
ATOM   15953 O O   . GLY I  5 28  ? 78.965  65.708  317.893 1.00 179.48 ?  28  GLY H O   1 
ATOM   15954 N N   . VAL I  5 29  ? 77.810  67.140  316.585 1.00 192.91 ?  29  VAL H N   1 
ATOM   15955 C CA  . VAL I  5 29  ? 78.708  67.030  315.443 1.00 186.45 ?  29  VAL H CA  1 
ATOM   15956 C C   . VAL I  5 29  ? 79.384  68.357  315.096 1.00 181.46 ?  29  VAL H C   1 
ATOM   15957 O O   . VAL I  5 29  ? 79.950  68.490  314.009 1.00 176.11 ?  29  VAL H O   1 
ATOM   15958 C CB  . VAL I  5 29  ? 77.980  66.446  314.216 1.00 184.98 ?  29  VAL H CB  1 
ATOM   15959 C CG1 . VAL I  5 29  ? 77.451  65.049  314.524 1.00 189.60 ?  29  VAL H CG1 1 
ATOM   15960 C CG2 . VAL I  5 29  ? 76.851  67.350  313.797 1.00 185.33 ?  29  VAL H CG2 1 
ATOM   15961 N N   . ARG I  5 30  ? 79.333  69.342  315.994 1.00 193.50 ?  30  ARG H N   1 
ATOM   15962 C CA  . ARG I  5 30  ? 79.953  70.675  315.822 1.00 189.09 ?  30  ARG H CA  1 
ATOM   15963 C C   . ARG I  5 30  ? 79.361  71.336  314.577 1.00 185.47 ?  30  ARG H C   1 
ATOM   15964 O O   . ARG I  5 30  ? 78.132  71.304  314.406 1.00 188.83 ?  30  ARG H O   1 
ATOM   15965 C CB  . ARG I  5 30  ? 81.467  70.514  315.814 1.00 185.81 ?  30  ARG H CB  1 
ATOM   15966 C CG  . ARG I  5 30  ? 82.046  69.923  317.076 1.00 192.29 ?  30  ARG H CG  1 
ATOM   15967 C CD  . ARG I  5 30  ? 83.533  69.711  316.906 1.00 189.56 ?  30  ARG H CD  1 
ATOM   15968 N NE  . ARG I  5 30  ? 83.806  68.599  316.001 1.00 189.71 ?  30  ARG H NE  1 
ATOM   15969 C CZ  . ARG I  5 30  ? 83.825  67.331  316.388 1.00 193.82 ?  30  ARG H CZ  1 
ATOM   15970 N NH1 . ARG I  5 30  ? 83.563  67.044  317.648 1.00 202.59 1  30  ARG H NH1 1 
ATOM   15971 N NH2 . ARG I  5 30  ? 84.085  66.359  315.524 1.00 191.95 ?  30  ARG H NH2 1 
ATOM   15972 N N   . ASN I  5 31  ? 80.174  71.939  313.700 1.00 191.07 ?  31  ASN H N   1 
ATOM   15973 C CA  . ASN I  5 31  ? 79.727  72.525  312.439 1.00 187.61 ?  31  ASN H CA  1 
ATOM   15974 C C   . ASN I  5 31  ? 80.031  71.627  311.242 1.00 183.66 ?  31  ASN H C   1 
ATOM   15975 O O   . ASN I  5 31  ? 79.989  72.092  310.097 1.00 180.29 ?  31  ASN H O   1 
ATOM   15976 C CB  . ASN I  5 31  ? 80.365  73.904  312.226 1.00 185.40 ?  31  ASN H CB  1 
ATOM   15977 C CG  . ASN I  5 31  ? 81.865  73.829  311.934 1.00 178.72 ?  31  ASN H CG  1 
ATOM   15978 O OD1 . ASN I  5 31  ? 82.527  72.850  312.274 1.00 181.11 ?  31  ASN H OD1 1 
ATOM   15979 N ND2 . ASN I  5 31  ? 82.400  74.868  311.295 1.00 180.26 ?  31  ASN H ND2 1 
ATOM   15980 N N   . GLU I  5 32  ? 80.336  70.353  311.486 1.00 190.58 ?  32  GLU H N   1 
ATOM   15981 C CA  . GLU I  5 32  ? 80.886  69.467  310.462 1.00 187.03 ?  32  GLU H CA  1 
ATOM   15982 C C   . GLU I  5 32  ? 79.739  68.710  309.796 1.00 189.54 ?  32  GLU H C   1 
ATOM   15983 O O   . GLU I  5 32  ? 79.490  67.529  310.047 1.00 192.63 ?  32  GLU H O   1 
ATOM   15984 C CB  . GLU I  5 32  ? 81.915  68.533  311.086 1.00 188.75 ?  32  GLU H CB  1 
ATOM   15985 C CG  . GLU I  5 32  ? 83.101  69.280  311.686 1.00 185.69 ?  32  GLU H CG  1 
ATOM   15986 C CD  . GLU I  5 32  ? 83.923  68.428  312.627 1.00 190.15 ?  32  GLU H CD  1 
ATOM   15987 O OE1 . GLU I  5 32  ? 84.965  68.917  313.113 1.00 190.24 ?  32  GLU H OE1 1 
ATOM   15988 O OE2 . GLU I  5 32  ? 83.515  67.281  312.900 1.00 194.55 -1 32  GLU H OE2 1 
ATOM   15989 N N   . LEU I  5 33  ? 79.034  69.419  308.918 1.00 167.25 ?  33  LEU H N   1 
ATOM   15990 C CA  . LEU I  5 33  ? 77.787  68.928  308.351 1.00 169.82 ?  33  LEU H CA  1 
ATOM   15991 C C   . LEU I  5 33  ? 77.589  69.543  306.977 1.00 166.52 ?  33  LEU H C   1 
ATOM   15992 O O   . LEU I  5 33  ? 77.887  70.722  306.769 1.00 164.20 ?  33  LEU H O   1 
ATOM   15993 C CB  . LEU I  5 33  ? 76.588  69.248  309.248 1.00 175.00 ?  33  LEU H CB  1 
ATOM   15994 C CG  . LEU I  5 33  ? 75.247  68.675  308.784 1.00 178.05 ?  33  LEU H CG  1 
ATOM   15995 C CD1 . LEU I  5 33  ? 74.660  67.760  309.847 1.00 183.45 ?  33  LEU H CD1 1 
ATOM   15996 C CD2 . LEU I  5 33  ? 74.283  69.800  308.428 1.00 179.15 ?  33  LEU H CD2 1 
ATOM   15997 N N   . ALA I  5 34  ? 77.097  68.733  306.042 1.00 170.03 ?  34  ALA H N   1 
ATOM   15998 C CA  . ALA I  5 34  ? 76.847  69.169  304.678 1.00 167.46 ?  34  ALA H CA  1 
ATOM   15999 C C   . ALA I  5 34  ? 75.403  68.887  304.284 1.00 170.83 ?  34  ALA H C   1 
ATOM   16000 O O   . ALA I  5 34  ? 74.760  67.983  304.825 1.00 174.39 ?  34  ALA H O   1 
ATOM   16001 C CB  . ALA I  5 34  ? 77.796  68.477  303.694 1.00 163.77 ?  34  ALA H CB  1 
ATOM   16002 N N   . TRP I  5 35  ? 74.903  69.667  303.326 1.00 167.07 ?  35  TRP H N   1 
ATOM   16003 C CA  . TRP I  5 35  ? 73.590  69.456  302.728 1.00 167.39 ?  35  TRP H CA  1 
ATOM   16004 C C   . TRP I  5 35  ? 73.740  69.178  301.236 1.00 166.86 ?  35  TRP H C   1 
ATOM   16005 O O   . TRP I  5 35  ? 74.567  69.799  300.560 1.00 166.28 ?  35  TRP H O   1 
ATOM   16006 C CB  . TRP I  5 35  ? 72.668  70.672  302.939 1.00 170.10 ?  35  TRP H CB  1 
ATOM   16007 C CG  . TRP I  5 35  ? 72.235  70.917  304.363 1.00 173.96 ?  35  TRP H CG  1 
ATOM   16008 C CD1 . TRP I  5 35  ? 72.880  71.671  305.300 1.00 173.72 ?  35  TRP H CD1 1 
ATOM   16009 C CD2 . TRP I  5 35  ? 71.038  70.436  304.993 1.00 179.02 ?  35  TRP H CD2 1 
ATOM   16010 N NE1 . TRP I  5 35  ? 72.170  71.674  306.478 1.00 178.48 ?  35  TRP H NE1 1 
ATOM   16011 C CE2 . TRP I  5 35  ? 71.035  70.924  306.314 1.00 181.80 ?  35  TRP H CE2 1 
ATOM   16012 C CE3 . TRP I  5 35  ? 69.974  69.633  304.569 1.00 181.57 ?  35  TRP H CE3 1 
ATOM   16013 C CZ2 . TRP I  5 35  ? 70.010  70.636  307.215 1.00 187.19 ?  35  TRP H CZ2 1 
ATOM   16014 C CZ3 . TRP I  5 35  ? 68.957  69.348  305.466 1.00 186.64 ?  35  TRP H CZ3 1 
ATOM   16015 C CH2 . TRP I  5 35  ? 68.982  69.850  306.771 1.00 189.48 ?  35  TRP H CH2 1 
ATOM   16016 N N   . TYR I  5 36  ? 72.922  68.259  300.722 1.00 180.49 ?  36  TYR H N   1 
ATOM   16017 C CA  . TYR I  5 36  ? 72.954  67.863  299.319 1.00 178.88 ?  36  TYR H CA  1 
ATOM   16018 C C   . TYR I  5 36  ? 71.560  67.920  298.710 1.00 181.83 ?  36  TYR H C   1 
ATOM   16019 O O   . TYR I  5 36  ? 70.548  67.826  299.408 1.00 185.48 ?  36  TYR H O   1 
ATOM   16020 C CB  . TYR I  5 36  ? 73.509  66.445  299.125 1.00 178.23 ?  36  TYR H CB  1 
ATOM   16021 C CG  . TYR I  5 36  ? 74.902  66.221  299.650 1.00 175.61 ?  36  TYR H CG  1 
ATOM   16022 C CD1 . TYR I  5 36  ? 75.122  65.907  300.983 1.00 177.23 ?  36  TYR H CD1 1 
ATOM   16023 C CD2 . TYR I  5 36  ? 76.000  66.290  298.803 1.00 171.88 ?  36  TYR H CD2 1 
ATOM   16024 C CE1 . TYR I  5 36  ? 76.400  65.690  301.464 1.00 175.11 ?  36  TYR H CE1 1 
ATOM   16025 C CE2 . TYR I  5 36  ? 77.281  66.072  299.272 1.00 169.65 ?  36  TYR H CE2 1 
ATOM   16026 C CZ  . TYR I  5 36  ? 77.476  65.772  300.604 1.00 171.25 ?  36  TYR H CZ  1 
ATOM   16027 O OH  . TYR I  5 36  ? 78.751  65.555  301.080 1.00 169.28 ?  36  TYR H OH  1 
ATOM   16028 N N   . GLN I  5 37  ? 71.529  68.081  297.388 1.00 186.41 ?  37  GLN H N   1 
ATOM   16029 C CA  . GLN I  5 37  ? 70.316  67.970  296.585 1.00 189.11 ?  37  GLN H CA  1 
ATOM   16030 C C   . GLN I  5 37  ? 70.413  66.743  295.686 1.00 188.73 ?  37  GLN H C   1 
ATOM   16031 O O   . GLN I  5 37  ? 71.438  66.534  295.030 1.00 185.81 ?  37  GLN H O   1 
ATOM   16032 C CB  . GLN I  5 37  ? 70.115  69.232  295.741 1.00 188.85 ?  37  GLN H CB  1 
ATOM   16033 C CG  . GLN I  5 37  ? 68.837  69.273  294.919 1.00 191.97 ?  37  GLN H CG  1 
ATOM   16034 C CD  . GLN I  5 37  ? 68.831  70.424  293.929 1.00 191.52 ?  37  GLN H CD  1 
ATOM   16035 O OE1 . GLN I  5 37  ? 69.536  70.393  292.920 1.00 189.39 ?  37  GLN H OE1 1 
ATOM   16036 N NE2 . GLN I  5 37  ? 68.043  71.451  294.220 1.00 194.37 ?  37  GLN H NE2 1 
ATOM   16037 N N   . GLN I  5 38  ? 69.342  65.950  295.634 1.00 179.34 ?  38  GLN H N   1 
ATOM   16038 C CA  . GLN I  5 38  ? 69.262  64.811  294.728 1.00 179.58 ?  38  GLN H CA  1 
ATOM   16039 C C   . GLN I  5 38  ? 67.914  64.795  294.026 1.00 182.57 ?  38  GLN H C   1 
ATOM   16040 O O   . GLN I  5 38  ? 66.870  64.949  294.669 1.00 185.61 ?  38  GLN H O   1 
ATOM   16041 C CB  . GLN I  5 38  ? 69.462  63.475  295.457 1.00 180.69 ?  38  GLN H CB  1 
ATOM   16042 C CG  . GLN I  5 38  ? 69.539  62.294  294.492 1.00 180.95 ?  38  GLN H CG  1 
ATOM   16043 C CD  . GLN I  5 38  ? 69.714  60.957  295.181 1.00 182.57 ?  38  GLN H CD  1 
ATOM   16044 O OE1 . GLN I  5 38  ? 69.106  60.695  296.218 1.00 185.11 ?  38  GLN H OE1 1 
ATOM   16045 N NE2 . GLN I  5 38  ? 70.540  60.096  294.597 1.00 181.49 ?  38  GLN H NE2 1 
ATOM   16046 N N   . LYS I  5 39  ? 67.945  64.590  292.714 1.00 188.31 ?  39  LYS H N   1 
ATOM   16047 C CA  . LYS I  5 39  ? 66.790  64.426  291.856 1.00 190.65 ?  39  LYS H CA  1 
ATOM   16048 C C   . LYS I  5 39  ? 66.748  62.991  291.338 1.00 190.75 ?  39  LYS H C   1 
ATOM   16049 O O   . LYS I  5 39  ? 67.791  62.335  291.254 1.00 189.03 ?  39  LYS H O   1 
ATOM   16050 C CB  . LYS I  5 39  ? 66.842  65.407  290.677 1.00 191.19 ?  39  LYS H CB  1 
ATOM   16051 C CG  . LYS I  5 39  ? 66.704  66.866  291.098 1.00 191.76 ?  39  LYS H CG  1 
ATOM   16052 C CD  . LYS I  5 39  ? 66.804  67.817  289.918 1.00 192.59 ?  39  LYS H CD  1 
ATOM   16053 C CE  . LYS I  5 39  ? 66.636  69.259  290.370 1.00 193.52 ?  39  LYS H CE  1 
ATOM   16054 N NZ  . LYS I  5 39  ? 66.732  70.212  289.230 1.00 194.77 1  39  LYS H NZ  1 
ATOM   16055 N N   . PRO I  5 40  ? 65.568  62.466  291.007 1.00 190.95 ?  40  PRO H N   1 
ATOM   16056 C CA  . PRO I  5 40  ? 65.478  61.061  290.587 1.00 191.24 ?  40  PRO H CA  1 
ATOM   16057 C C   . PRO I  5 40  ? 66.399  60.755  289.413 1.00 190.17 ?  40  PRO H C   1 
ATOM   16058 O O   . PRO I  5 40  ? 66.404  61.463  288.403 1.00 190.59 ?  40  PRO H O   1 
ATOM   16059 C CB  . PRO I  5 40  ? 64.002  60.908  290.205 1.00 193.68 ?  40  PRO H CB  1 
ATOM   16060 C CG  . PRO I  5 40  ? 63.306  61.895  291.083 1.00 194.72 ?  40  PRO H CG  1 
ATOM   16061 C CD  . PRO I  5 40  ? 64.234  63.081  291.141 1.00 193.26 ?  40  PRO H CD  1 
ATOM   16062 N N   . GLY I  5 41  ? 67.185  59.689  289.558 1.00 188.06 ?  41  GLY H N   1 
ATOM   16063 C CA  . GLY I  5 41  ? 68.069  59.228  288.508 1.00 187.35 ?  41  GLY H CA  1 
ATOM   16064 C C   . GLY I  5 41  ? 69.404  59.935  288.409 1.00 185.28 ?  41  GLY H C   1 
ATOM   16065 O O   . GLY I  5 41  ? 70.190  59.608  287.510 1.00 184.86 ?  41  GLY H O   1 
ATOM   16066 N N   . LYS I  5 42  ? 69.692  60.888  289.291 1.00 183.63 ?  42  LYS H N   1 
ATOM   16067 C CA  . LYS I  5 42  ? 70.923  61.658  289.232 1.00 181.62 ?  42  LYS H CA  1 
ATOM   16068 C C   . LYS I  5 42  ? 71.711  61.515  290.526 1.00 179.79 ?  42  LYS H C   1 
ATOM   16069 O O   . LYS I  5 42  ? 71.168  61.169  291.579 1.00 180.27 ?  42  LYS H O   1 
ATOM   16070 C CB  . LYS I  5 42  ? 70.644  63.143  288.965 1.00 181.97 ?  42  LYS H CB  1 
ATOM   16071 C CG  . LYS I  5 42  ? 69.884  63.419  287.681 1.00 184.07 ?  42  LYS H CG  1 
ATOM   16072 C CD  . LYS I  5 42  ? 70.649  62.906  286.471 1.00 183.91 ?  42  LYS H CD  1 
ATOM   16073 C CE  . LYS I  5 42  ? 70.027  63.403  285.176 1.00 185.95 ?  42  LYS H CE  1 
ATOM   16074 N NZ  . LYS I  5 42  ? 70.852  63.028  283.996 1.00 186.77 1  42  LYS H NZ  1 
ATOM   16075 N N   . ALA I  5 43  ? 73.011  61.776  290.424 1.00 185.18 ?  43  ALA H N   1 
ATOM   16076 C CA  . ALA I  5 43  ? 73.852  61.844  291.603 1.00 183.34 ?  43  ALA H CA  1 
ATOM   16077 C C   . ALA I  5 43  ? 73.535  63.112  292.397 1.00 183.04 ?  43  ALA H C   1 
ATOM   16078 O O   . ALA I  5 43  ? 73.079  64.111  291.833 1.00 183.73 ?  43  ALA H O   1 
ATOM   16079 C CB  . ALA I  5 43  ? 75.326  61.820  291.209 1.00 181.37 ?  43  ALA H CB  1 
ATOM   16080 N N   . PRO I  5 44  ? 73.747  63.089  293.712 1.00 178.86 ?  44  PRO H N   1 
ATOM   16081 C CA  . PRO I  5 44  ? 73.547  64.300  294.516 1.00 178.51 ?  44  PRO H CA  1 
ATOM   16082 C C   . PRO I  5 44  ? 74.499  65.424  294.128 1.00 176.75 ?  44  PRO H C   1 
ATOM   16083 O O   . PRO I  5 44  ? 75.582  65.206  293.579 1.00 175.16 ?  44  PRO H O   1 
ATOM   16084 C CB  . PRO I  5 44  ? 73.806  63.820  295.949 1.00 177.86 ?  44  PRO H CB  1 
ATOM   16085 C CG  . PRO I  5 44  ? 73.573  62.342  295.897 1.00 178.95 ?  44  PRO H CG  1 
ATOM   16086 C CD  . PRO I  5 44  ? 74.060  61.920  294.548 1.00 178.62 ?  44  PRO H CD  1 
ATOM   16087 N N   . ASN I  5 45  ? 74.073  66.650  294.432 1.00 186.25 ?  45  ASN H N   1 
ATOM   16088 C CA  . ASN I  5 45  ? 74.881  67.850  294.258 1.00 184.76 ?  45  ASN H CA  1 
ATOM   16089 C C   . ASN I  5 45  ? 75.066  68.547  295.599 1.00 183.84 ?  45  ASN H C   1 
ATOM   16090 O O   . ASN I  5 45  ? 74.115  68.688  296.373 1.00 185.44 ?  45  ASN H O   1 
ATOM   16091 C CB  . ASN I  5 45  ? 74.243  68.816  293.256 1.00 186.50 ?  45  ASN H CB  1 
ATOM   16092 C CG  . ASN I  5 45  ? 74.652  68.526  291.826 1.00 186.61 ?  45  ASN H CG  1 
ATOM   16093 O OD1 . ASN I  5 45  ? 75.339  67.543  291.549 1.00 185.52 ?  45  ASN H OD1 1 
ATOM   16094 N ND2 . ASN I  5 45  ? 74.238  69.392  290.908 1.00 189.39 ?  45  ASN H ND2 1 
ATOM   16095 N N   . LEU I  5 46  ? 76.297  68.984  295.862 1.00 176.92 ?  46  LEU H N   1 
ATOM   16096 C CA  . LEU I  5 46  ? 76.618  69.650  297.119 1.00 175.98 ?  46  LEU H CA  1 
ATOM   16097 C C   . LEU I  5 46  ? 76.062  71.069  297.155 1.00 177.21 ?  46  LEU H C   1 
ATOM   16098 O O   . LEU I  5 46  ? 76.299  71.867  296.243 1.00 177.25 ?  46  LEU H O   1 
ATOM   16099 C CB  . LEU I  5 46  ? 78.132  69.676  297.329 1.00 172.93 ?  46  LEU H CB  1 
ATOM   16100 C CG  . LEU I  5 46  ? 78.638  70.320  298.621 1.00 171.32 ?  46  LEU H CG  1 
ATOM   16101 C CD1 . LEU I  5 46  ? 78.175  69.525  299.831 1.00 172.16 ?  46  LEU H CD1 1 
ATOM   16102 C CD2 . LEU I  5 46  ? 80.155  70.429  298.599 1.00 168.22 ?  46  LEU H CD2 1 
ATOM   16103 N N   . LEU I  5 47  ? 75.317  71.378  298.215 1.00 161.06 ?  47  LEU H N   1 
ATOM   16104 C CA  . LEU I  5 47  ? 74.774  72.709  298.450 1.00 160.30 ?  47  LEU H CA  1 
ATOM   16105 C C   . LEU I  5 47  ? 75.509  73.460  299.549 1.00 159.38 ?  47  LEU H C   1 
ATOM   16106 O O   . LEU I  5 47  ? 75.902  74.616  299.357 1.00 159.68 ?  47  LEU H O   1 
ATOM   16107 C CB  . LEU I  5 47  ? 73.283  72.618  298.798 1.00 161.96 ?  47  LEU H CB  1 
ATOM   16108 C CG  . LEU I  5 47  ? 72.376  71.984  297.748 1.00 163.80 ?  47  LEU H CG  1 
ATOM   16109 C CD1 . LEU I  5 47  ? 70.963  71.868  298.286 1.00 166.78 ?  47  LEU H CD1 1 
ATOM   16110 C CD2 . LEU I  5 47  ? 72.403  72.801  296.470 1.00 164.46 ?  47  LEU H CD2 1 
ATOM   16111 N N   . ILE I  5 48  ? 75.691  72.830  300.708 1.00 159.66 ?  48  ILE H N   1 
ATOM   16112 C CA  . ILE I  5 48  ? 76.189  73.478  301.915 1.00 158.50 ?  48  ILE H CA  1 
ATOM   16113 C C   . ILE I  5 48  ? 77.247  72.586  302.544 1.00 158.52 ?  48  ILE H C   1 
ATOM   16114 O O   . ILE I  5 48  ? 77.108  71.359  302.548 1.00 158.59 ?  48  ILE H O   1 
ATOM   16115 C CB  . ILE I  5 48  ? 75.052  73.743  302.926 1.00 156.67 ?  48  ILE H CB  1 
ATOM   16116 C CG1 . ILE I  5 48  ? 74.035  74.726  302.353 1.00 159.12 ?  48  ILE H CG1 1 
ATOM   16117 C CG2 . ILE I  5 48  ? 75.606  74.259  304.245 1.00 155.45 ?  48  ILE H CG2 1 
ATOM   16118 C CD1 . ILE I  5 48  ? 74.521  76.143  302.360 1.00 158.73 ?  48  ILE H CD1 1 
ATOM   16119 N N   . TYR I  5 49  ? 78.320  73.196  303.047 1.00 161.94 ?  49  TYR H N   1 
ATOM   16120 C CA  . TYR I  5 49  ? 79.281  72.508  303.900 1.00 159.75 ?  49  TYR H CA  1 
ATOM   16121 C C   . TYR I  5 49  ? 79.639  73.433  305.055 1.00 159.11 ?  49  TYR H C   1 
ATOM   16122 O O   . TYR I  5 49  ? 79.307  74.622  305.048 1.00 160.01 ?  49  TYR H O   1 
ATOM   16123 C CB  . TYR I  5 49  ? 80.532  72.065  303.131 1.00 156.93 ?  49  TYR H CB  1 
ATOM   16124 C CG  . TYR I  5 49  ? 81.303  73.184  302.470 1.00 157.36 ?  49  TYR H CG  1 
ATOM   16125 C CD1 . TYR I  5 49  ? 82.350  73.814  303.129 1.00 157.16 ?  49  TYR H CD1 1 
ATOM   16126 C CD2 . TYR I  5 49  ? 81.004  73.591  301.178 1.00 158.59 ?  49  TYR H CD2 1 
ATOM   16127 C CE1 . TYR I  5 49  ? 83.069  74.831  302.527 1.00 158.15 ?  49  TYR H CE1 1 
ATOM   16128 C CE2 . TYR I  5 49  ? 81.716  74.611  300.567 1.00 159.58 ?  49  TYR H CE2 1 
ATOM   16129 C CZ  . TYR I  5 49  ? 82.749  75.226  301.244 1.00 159.36 ?  49  TYR H CZ  1 
ATOM   16130 O OH  . TYR I  5 49  ? 83.459  76.238  300.637 1.00 160.36 ?  49  TYR H OH  1 
ATOM   16131 N N   . TYR I  5 50  ? 80.319  72.877  306.061 1.00 162.55 ?  50  TYR H N   1 
ATOM   16132 C CA  . TYR I  5 50  ? 80.563  73.584  307.322 1.00 162.19 ?  50  TYR H CA  1 
ATOM   16133 C C   . TYR I  5 50  ? 79.255  74.099  307.920 1.00 165.61 ?  50  TYR H C   1 
ATOM   16134 O O   . TYR I  5 50  ? 79.224  75.143  308.578 1.00 165.93 ?  50  TYR H O   1 
ATOM   16135 C CB  . TYR I  5 50  ? 81.564  74.733  307.152 1.00 159.58 ?  50  TYR H CB  1 
ATOM   16136 C CG  . TYR I  5 50  ? 82.975  74.295  306.825 1.00 156.06 ?  50  TYR H CG  1 
ATOM   16137 C CD1 . TYR I  5 50  ? 83.484  73.097  307.308 1.00 155.14 ?  50  TYR H CD1 1 
ATOM   16138 C CD2 . TYR I  5 50  ? 83.809  75.097  306.055 1.00 153.92 ?  50  TYR H CD2 1 
ATOM   16139 C CE1 . TYR I  5 50  ? 84.779  72.698  307.013 1.00 152.17 ?  50  TYR H CE1 1 
ATOM   16140 C CE2 . TYR I  5 50  ? 85.104  74.708  305.758 1.00 150.87 ?  50  TYR H CE2 1 
ATOM   16141 C CZ  . TYR I  5 50  ? 85.584  73.510  306.238 1.00 150.00 ?  50  TYR H CZ  1 
ATOM   16142 O OH  . TYR I  5 50  ? 86.873  73.126  305.942 1.00 147.21 ?  50  TYR H OH  1 
ATOM   16143 N N   . ALA I  5 51  ? 78.169  73.363  307.667 1.00 156.48 ?  51  ALA H N   1 
ATOM   16144 C CA  . ALA I  5 51  ? 76.824  73.636  308.167 1.00 160.09 ?  51  ALA H CA  1 
ATOM   16145 C C   . ALA I  5 51  ? 76.181  74.905  307.612 1.00 161.71 ?  51  ALA H C   1 
ATOM   16146 O O   . ALA I  5 51  ? 74.952  74.972  307.518 1.00 164.91 ?  51  ALA H O   1 
ATOM   16147 C CB  . ALA I  5 51  ? 76.827  73.698  309.698 1.00 161.01 ?  51  ALA H CB  1 
ATOM   16148 N N   . SER I  5 52  ? 76.969  75.921  307.248 1.00 165.77 ?  52  SER H N   1 
ATOM   16149 C CA  . SER I  5 52  ? 76.384  77.166  306.766 1.00 167.58 ?  52  SER H CA  1 
ATOM   16150 C C   . SER I  5 52  ? 76.974  77.738  305.480 1.00 165.97 ?  52  SER H C   1 
ATOM   16151 O O   . SER I  5 52  ? 76.457  78.748  304.991 1.00 167.83 ?  52  SER H O   1 
ATOM   16152 C CB  . SER I  5 52  ? 76.482  78.242  307.858 1.00 168.28 ?  52  SER H CB  1 
ATOM   16153 O OG  . SER I  5 52  ? 77.825  78.420  308.274 1.00 164.80 ?  52  SER H OG  1 
ATOM   16154 N N   . THR I  5 53  ? 78.022  77.143  304.916 1.00 161.06 ?  53  THR H N   1 
ATOM   16155 C CA  . THR I  5 53  ? 78.725  77.753  303.791 1.00 159.50 ?  53  THR H CA  1 
ATOM   16156 C C   . THR I  5 53  ? 78.175  77.248  302.460 1.00 160.72 ?  53  THR H C   1 
ATOM   16157 O O   . THR I  5 53  ? 78.050  76.037  302.250 1.00 160.45 ?  53  THR H O   1 
ATOM   16158 C CB  . THR I  5 53  ? 80.228  77.482  303.880 1.00 159.70 ?  53  THR H CB  1 
ATOM   16159 O OG1 . THR I  5 53  ? 80.745  78.032  305.099 1.00 158.59 ?  53  THR H OG1 1 
ATOM   16160 C CG2 . THR I  5 53  ? 80.953  78.117  302.702 1.00 161.39 ?  53  THR H CG2 1 
ATOM   16161 N N   . LEU I  5 54  ? 77.849  78.183  301.566 1.00 174.85 ?  54  LEU H N   1 
ATOM   16162 C CA  . LEU I  5 54  ? 77.320  77.837  300.251 1.00 176.25 ?  54  LEU H CA  1 
ATOM   16163 C C   . LEU I  5 54  ? 78.413  77.277  299.348 1.00 173.59 ?  54  LEU H C   1 
ATOM   16164 O O   . LEU I  5 54  ? 79.487  77.871  299.214 1.00 171.52 ?  54  LEU H O   1 
ATOM   16165 C CB  . LEU I  5 54  ? 76.690  79.059  299.583 1.00 178.99 ?  54  LEU H CB  1 
ATOM   16166 C CG  . LEU I  5 54  ? 75.201  79.327  299.799 1.00 182.92 ?  54  LEU H CG  1 
ATOM   16167 C CD1 . LEU I  5 54  ? 74.394  78.179  299.225 1.00 183.90 ?  54  LEU H CD1 1 
ATOM   16168 C CD2 . LEU I  5 54  ? 74.882  79.517  301.270 1.00 183.74 ?  54  LEU H CD2 1 
ATOM   16169 N N   . GLN I  5 55  ? 78.135  76.130  298.730 1.00 180.24 ?  55  GLN H N   1 
ATOM   16170 C CA  . GLN I  5 55  ? 79.021  75.596  297.703 1.00 178.45 ?  55  GLN H CA  1 
ATOM   16171 C C   . GLN I  5 55  ? 79.046  76.522  296.492 1.00 179.64 ?  55  GLN H C   1 
ATOM   16172 O O   . GLN I  5 55  ? 78.041  77.154  296.152 1.00 182.57 ?  55  GLN H O   1 
ATOM   16173 C CB  . GLN I  5 55  ? 78.572  74.187  297.297 1.00 179.09 ?  55  GLN H CB  1 
ATOM   16174 C CG  . GLN I  5 55  ? 79.279  73.592  296.076 1.00 178.08 ?  55  GLN H CG  1 
ATOM   16175 C CD  . GLN I  5 55  ? 80.765  73.345  296.283 1.00 174.80 ?  55  GLN H CD  1 
ATOM   16176 O OE1 . GLN I  5 55  ? 81.284  73.463  297.393 1.00 173.01 ?  55  GLN H OE1 1 
ATOM   16177 N NE2 . GLN I  5 55  ? 81.458  73.003  295.203 1.00 174.11 ?  55  GLN H NE2 1 
ATOM   16178 N N   . SER I  5 56  ? 80.216  76.618  295.862 1.00 188.59 ?  56  SER H N   1 
ATOM   16179 C CA  . SER I  5 56  ? 80.387  77.440  294.671 1.00 189.88 ?  56  SER H CA  1 
ATOM   16180 C C   . SER I  5 56  ? 79.353  77.090  293.608 1.00 192.68 ?  56  SER H C   1 
ATOM   16181 O O   . SER I  5 56  ? 79.160  75.919  293.269 1.00 192.78 ?  56  SER H O   1 
ATOM   16182 C CB  . SER I  5 56  ? 81.801  77.260  294.114 1.00 187.50 ?  56  SER H CB  1 
ATOM   16183 O OG  . SER I  5 56  ? 82.029  78.129  293.019 1.00 189.38 ?  56  SER H OG  1 
ATOM   16184 N N   . GLY I  5 57  ? 78.688  78.118  293.082 1.00 180.59 ?  57  GLY H N   1 
ATOM   16185 C CA  . GLY I  5 57  ? 77.699  77.943  292.045 1.00 183.66 ?  57  GLY H CA  1 
ATOM   16186 C C   . GLY I  5 57  ? 76.294  77.681  292.541 1.00 186.05 ?  57  GLY H C   1 
ATOM   16187 O O   . GLY I  5 57  ? 75.357  77.709  291.733 1.00 188.94 ?  57  GLY H O   1 
ATOM   16188 N N   . VAL I  5 58  ? 76.119  77.423  293.830 1.00 184.34 ?  58  VAL H N   1 
ATOM   16189 C CA  . VAL I  5 58  ? 74.786  77.196  294.391 1.00 186.71 ?  58  VAL H CA  1 
ATOM   16190 C C   . VAL I  5 58  ? 74.083  78.544  294.541 1.00 189.46 ?  58  VAL H C   1 
ATOM   16191 O O   . VAL I  5 58  ? 74.705  79.508  295.018 1.00 188.55 ?  58  VAL H O   1 
ATOM   16192 C CB  . VAL I  5 58  ? 74.885  76.463  295.729 1.00 185.03 ?  58  VAL H CB  1 
ATOM   16193 C CG1 . VAL I  5 58  ? 73.514  76.290  296.355 1.00 187.77 ?  58  VAL H CG1 1 
ATOM   16194 C CG2 . VAL I  5 58  ? 75.549  75.098  295.541 1.00 182.78 ?  58  VAL H CG2 1 
ATOM   16195 N N   . PRO I  5 59  ? 72.814  78.656  294.141 1.00 204.73 ?  59  PRO H N   1 
ATOM   16196 C CA  . PRO I  5 59  ? 72.133  79.959  294.172 1.00 209.11 ?  59  PRO H CA  1 
ATOM   16197 C C   . PRO I  5 59  ? 72.030  80.550  295.572 1.00 208.85 ?  59  PRO H C   1 
ATOM   16198 O O   . PRO I  5 59  ? 71.961  79.837  296.575 1.00 206.97 ?  59  PRO H O   1 
ATOM   16199 C CB  . PRO I  5 59  ? 70.746  79.646  293.598 1.00 212.71 ?  59  PRO H CB  1 
ATOM   16200 C CG  . PRO I  5 59  ? 70.941  78.415  292.782 1.00 212.37 ?  59  PRO H CG  1 
ATOM   16201 C CD  . PRO I  5 59  ? 72.014  77.624  293.460 1.00 205.88 ?  59  PRO H CD  1 
ATOM   16202 N N   . SER I  5 60  ? 72.032  81.887  295.618 1.00 211.15 ?  60  SER H N   1 
ATOM   16203 C CA  . SER I  5 60  ? 72.016  82.620  296.879 1.00 211.24 ?  60  SER H CA  1 
ATOM   16204 C C   . SER I  5 60  ? 70.731  82.424  297.673 1.00 213.12 ?  60  SER H C   1 
ATOM   16205 O O   . SER I  5 60  ? 70.705  82.743  298.866 1.00 213.98 ?  60  SER H O   1 
ATOM   16206 C CB  . SER I  5 60  ? 72.222  84.112  296.614 1.00 215.00 ?  60  SER H CB  1 
ATOM   16207 O OG  . SER I  5 60  ? 71.207  84.616  295.762 1.00 222.08 ?  60  SER H OG  1 
ATOM   16208 N N   . ARG I  5 61  ? 69.664  81.920  297.049 1.00 208.23 ?  61  ARG H N   1 
ATOM   16209 C CA  . ARG I  5 61  ? 68.425  81.688  297.783 1.00 211.03 ?  61  ARG H CA  1 
ATOM   16210 C C   . ARG I  5 61  ? 68.535  80.532  298.769 1.00 208.77 ?  61  ARG H C   1 
ATOM   16211 O O   . ARG I  5 61  ? 67.651  80.379  299.620 1.00 210.77 ?  61  ARG H O   1 
ATOM   16212 C CB  . ARG I  5 61  ? 67.278  81.442  296.804 1.00 214.09 ?  61  ARG H CB  1 
ATOM   16213 C CG  . ARG I  5 61  ? 67.457  80.196  295.967 1.00 212.07 ?  61  ARG H CG  1 
ATOM   16214 C CD  . ARG I  5 61  ? 66.331  80.036  294.968 1.00 215.29 ?  61  ARG H CD  1 
ATOM   16215 N NE  . ARG I  5 61  ? 66.530  78.864  294.123 1.00 213.43 ?  61  ARG H NE  1 
ATOM   16216 C CZ  . ARG I  5 61  ? 67.289  78.856  293.033 1.00 212.08 ?  61  ARG H CZ  1 
ATOM   16217 N NH1 . ARG I  5 61  ? 67.914  79.962  292.652 1.00 212.23 1  61  ARG H NH1 1 
ATOM   16218 N NH2 . ARG I  5 61  ? 67.420  77.747  292.318 1.00 210.67 ?  61  ARG H NH2 1 
ATOM   16219 N N   . PHE I  5 62  ? 69.588  79.725  298.676 1.00 213.27 ?  62  PHE H N   1 
ATOM   16220 C CA  . PHE I  5 62  ? 69.865  78.680  299.651 1.00 210.80 ?  62  PHE H CA  1 
ATOM   16221 C C   . PHE I  5 62  ? 70.717  79.237  300.785 1.00 208.20 ?  62  PHE H C   1 
ATOM   16222 O O   . PHE I  5 62  ? 71.683  79.968  300.548 1.00 205.00 ?  62  PHE H O   1 
ATOM   16223 C CB  . PHE I  5 62  ? 70.596  77.504  298.998 1.00 206.29 ?  62  PHE H CB  1 
ATOM   16224 C CG  . PHE I  5 62  ? 69.752  76.708  298.044 1.00 208.70 ?  62  PHE H CG  1 
ATOM   16225 C CD1 . PHE I  5 62  ? 68.965  75.664  298.499 1.00 210.87 ?  62  PHE H CD1 1 
ATOM   16226 C CD2 . PHE I  5 62  ? 69.761  76.991  296.686 1.00 208.76 ?  62  PHE H CD2 1 
ATOM   16227 C CE1 . PHE I  5 62  ? 68.192  74.925  297.622 1.00 213.02 ?  62  PHE H CE1 1 
ATOM   16228 C CE2 . PHE I  5 62  ? 68.991  76.255  295.803 1.00 210.96 ?  62  PHE H CE2 1 
ATOM   16229 C CZ  . PHE I  5 62  ? 68.206  75.221  296.271 1.00 213.02 ?  62  PHE H CZ  1 
ATOM   16230 N N   . SER I  5 63  ? 70.345  78.897  302.018 1.00 207.56 ?  63  SER H N   1 
ATOM   16231 C CA  . SER I  5 63  ? 71.164  79.193  303.186 1.00 204.92 ?  63  SER H CA  1 
ATOM   16232 C C   . SER I  5 63  ? 70.951  78.090  304.214 1.00 205.25 ?  63  SER H C   1 
ATOM   16233 O O   . SER I  5 63  ? 69.981  77.333  304.144 1.00 208.59 ?  63  SER H O   1 
ATOM   16234 C CB  . SER I  5 63  ? 70.839  80.568  303.783 1.00 208.33 ?  63  SER H CB  1 
ATOM   16235 O OG  . SER I  5 63  ? 69.544  80.586  304.357 1.00 214.37 ?  63  SER H OG  1 
ATOM   16236 N N   . ALA I  5 64  ? 71.863  78.012  305.180 1.00 197.24 ?  64  ALA H N   1 
ATOM   16237 C CA  . ALA I  5 64  ? 71.800  76.957  306.180 1.00 197.59 ?  64  ALA H CA  1 
ATOM   16238 C C   . ALA I  5 64  ? 72.422  77.451  307.477 1.00 196.62 ?  64  ALA H C   1 
ATOM   16239 O O   . ALA I  5 64  ? 73.289  78.329  307.472 1.00 193.65 ?  64  ALA H O   1 
ATOM   16240 C CB  . ALA I  5 64  ? 72.502  75.684  305.693 1.00 193.45 ?  64  ALA H CB  1 
ATOM   16241 N N   . THR I  5 65  ? 71.959  76.883  308.590 1.00 202.49 ?  65  THR H N   1 
ATOM   16242 C CA  . THR I  5 65  ? 72.357  77.314  309.924 1.00 203.92 ?  65  THR H CA  1 
ATOM   16243 C C   . THR I  5 65  ? 72.540  76.101  310.826 1.00 203.80 ?  65  THR H C   1 
ATOM   16244 O O   . THR I  5 65  ? 72.191  74.972  310.469 1.00 203.90 ?  65  THR H O   1 
ATOM   16245 C CB  . THR I  5 65  ? 71.319  78.257  310.553 1.00 213.80 ?  65  THR H CB  1 
ATOM   16246 O OG1 . THR I  5 65  ? 70.124  77.520  310.846 1.00 223.05 ?  65  THR H OG1 1 
ATOM   16247 C CG2 . THR I  5 65  ? 70.987  79.429  309.631 1.00 218.47 ?  65  THR H CG2 1 
ATOM   16248 N N   . GLY I  5 66  ? 73.094  76.348  312.014 1.00 207.65 ?  66  GLY H N   1 
ATOM   16249 C CA  . GLY I  5 66  ? 73.119  75.346  313.063 1.00 208.31 ?  66  GLY H CA  1 
ATOM   16250 C C   . GLY I  5 66  ? 74.475  74.891  313.569 1.00 203.68 ?  66  GLY H C   1 
ATOM   16251 O O   . GLY I  5 66  ? 75.506  75.098  312.922 1.00 198.83 ?  66  GLY H O   1 
ATOM   16252 N N   . SER I  5 67  ? 74.469  74.270  314.747 1.00 212.07 ?  67  SER H N   1 
ATOM   16253 C CA  . SER I  5 67  ? 75.654  73.674  315.352 1.00 208.76 ?  67  SER H CA  1 
ATOM   16254 C C   . SER I  5 67  ? 75.185  72.601  316.325 1.00 214.39 ?  67  SER H C   1 
ATOM   16255 O O   . SER I  5 67  ? 74.005  72.532  316.679 1.00 219.63 ?  67  SER H O   1 
ATOM   16256 C CB  . SER I  5 67  ? 76.521  74.722  316.064 1.00 210.77 ?  67  SER H CB  1 
ATOM   16257 O OG  . SER I  5 67  ? 77.480  75.300  315.193 1.00 211.72 ?  67  SER H OG  1 
ATOM   16258 N N   . GLY I  5 68  ? 76.123  71.759  316.753 1.00 196.02 ?  68  GLY H N   1 
ATOM   16259 C CA  . GLY I  5 68  ? 75.798  70.754  317.745 1.00 196.06 ?  68  GLY H CA  1 
ATOM   16260 C C   . GLY I  5 68  ? 74.894  69.661  317.214 1.00 197.06 ?  68  GLY H C   1 
ATOM   16261 O O   . GLY I  5 68  ? 75.314  68.837  316.397 1.00 197.27 ?  68  GLY H O   1 
ATOM   16262 N N   . THR I  5 69  ? 73.650  69.634  317.691 1.00 198.53 ?  69  THR H N   1 
ATOM   16263 C CA  . THR I  5 69  ? 72.685  68.614  317.303 1.00 200.54 ?  69  THR H CA  1 
ATOM   16264 C C   . THR I  5 69  ? 71.553  69.122  316.417 1.00 202.85 ?  69  THR H C   1 
ATOM   16265 O O   . THR I  5 69  ? 70.722  68.313  315.991 1.00 206.07 ?  69  THR H O   1 
ATOM   16266 C CB  . THR I  5 69  ? 72.081  67.964  318.553 1.00 206.40 ?  69  THR H CB  1 
ATOM   16267 O OG1 . THR I  5 69  ? 71.404  68.961  319.329 1.00 211.43 ?  69  THR H OG1 1 
ATOM   16268 C CG2 . THR I  5 69  ? 73.167  67.318  319.398 1.00 204.92 ?  69  THR H CG2 1 
ATOM   16269 N N   . HIS I  5 70  ? 71.481  70.422  316.129 1.00 207.52 ?  70  HIS H N   1 
ATOM   16270 C CA  . HIS I  5 70  ? 70.320  71.000  315.455 1.00 211.61 ?  70  HIS H CA  1 
ATOM   16271 C C   . HIS I  5 70  ? 70.758  71.823  314.249 1.00 207.41 ?  70  HIS H C   1 
ATOM   16272 O O   . HIS I  5 70  ? 71.528  72.777  314.394 1.00 204.27 ?  70  HIS H O   1 
ATOM   16273 C CB  . HIS I  5 70  ? 69.513  71.863  316.430 1.00 217.65 ?  70  HIS H CB  1 
ATOM   16274 C CG  . HIS I  5 70  ? 68.286  72.467  315.827 1.00 223.79 ?  70  HIS H CG  1 
ATOM   16275 N ND1 . HIS I  5 70  ? 68.237  73.768  315.375 1.00 226.48 ?  70  HIS H ND1 1 
ATOM   16276 C CD2 . HIS I  5 70  ? 67.061  71.940  315.592 1.00 229.82 ?  70  HIS H CD2 1 
ATOM   16277 C CE1 . HIS I  5 70  ? 67.032  74.019  314.894 1.00 229.13 ?  70  HIS H CE1 1 
ATOM   16278 N NE2 . HIS I  5 70  ? 66.300  72.926  315.012 1.00 231.72 ?  70  HIS H NE2 1 
ATOM   16279 N N   . PHE I  5 71  ? 70.251  71.459  313.066 1.00 213.90 ?  71  PHE H N   1 
ATOM   16280 C CA  . PHE I  5 71  ? 70.619  72.086  311.801 1.00 210.22 ?  71  PHE H CA  1 
ATOM   16281 C C   . PHE I  5 71  ? 69.372  72.314  310.957 1.00 214.02 ?  71  PHE H C   1 
ATOM   16282 O O   . PHE I  5 71  ? 68.431  71.516  310.988 1.00 218.24 ?  71  PHE H O   1 
ATOM   16283 C CB  . PHE I  5 71  ? 71.621  71.228  311.014 1.00 204.86 ?  71  PHE H CB  1 
ATOM   16284 C CG  . PHE I  5 71  ? 72.869  70.896  311.782 1.00 201.39 ?  71  PHE H CG  1 
ATOM   16285 C CD1 . PHE I  5 71  ? 72.911  69.787  312.614 1.00 203.41 ?  71  PHE H CD1 1 
ATOM   16286 C CD2 . PHE I  5 71  ? 74.000  71.688  311.670 1.00 195.46 ?  71  PHE H CD2 1 
ATOM   16287 C CE1 . PHE I  5 71  ? 74.057  69.480  313.325 1.00 199.77 ?  71  PHE H CE1 1 
ATOM   16288 C CE2 . PHE I  5 71  ? 75.151  71.384  312.378 1.00 193.10 ?  71  PHE H CE2 1 
ATOM   16289 C CZ  . PHE I  5 71  ? 75.178  70.280  313.206 1.00 194.59 ?  71  PHE H CZ  1 
ATOM   16290 N N   . THR I  5 72  ? 69.371  73.412  310.197 1.00 205.17 ?  72  THR H N   1 
ATOM   16291 C CA  . THR I  5 72  ? 68.298  73.709  309.257 1.00 208.42 ?  72  THR H CA  1 
ATOM   16292 C C   . THR I  5 72  ? 68.864  74.163  307.918 1.00 204.54 ?  72  THR H C   1 
ATOM   16293 O O   . THR I  5 72  ? 69.968  74.710  307.841 1.00 200.10 ?  72  THR H O   1 
ATOM   16294 C CB  . THR I  5 72  ? 67.342  74.798  309.788 1.00 213.99 ?  72  THR H CB  1 
ATOM   16295 O OG1 . THR I  5 72  ? 68.066  76.015  310.008 1.00 212.14 ?  72  THR H OG1 1 
ATOM   16296 C CG2 . THR I  5 72  ? 66.673  74.359  311.083 1.00 218.58 ?  72  THR H CG2 1 
ATOM   16297 N N   . LEU I  5 73  ? 68.086  73.928  306.863 1.00 206.71 ?  73  LEU H N   1 
ATOM   16298 C CA  . LEU I  5 73  ? 68.354  74.447  305.528 1.00 204.57 ?  73  LEU H CA  1 
ATOM   16299 C C   . LEU I  5 73  ? 67.137  75.244  305.078 1.00 210.26 ?  73  LEU H C   1 
ATOM   16300 O O   . LEU I  5 73  ? 66.001  74.780  305.225 1.00 214.54 ?  73  LEU H O   1 
ATOM   16301 C CB  . LEU I  5 73  ? 68.657  73.322  304.533 1.00 202.48 ?  73  LEU H CB  1 
ATOM   16302 C CG  . LEU I  5 73  ? 68.822  73.742  303.068 1.00 200.61 ?  73  LEU H CG  1 
ATOM   16303 C CD1 . LEU I  5 73  ? 70.181  74.390  302.838 1.00 197.67 ?  73  LEU H CD1 1 
ATOM   16304 C CD2 . LEU I  5 73  ? 68.612  72.563  302.124 1.00 205.32 ?  73  LEU H CD2 1 
ATOM   16305 N N   . THR I  5 74  ? 67.374  76.438  304.538 1.00 211.93 ?  74  THR H N   1 
ATOM   16306 C CA  . THR I  5 74  ? 66.308  77.346  304.143 1.00 217.24 ?  74  THR H CA  1 
ATOM   16307 C C   . THR I  5 74  ? 66.435  77.718  302.671 1.00 216.19 ?  74  THR H C   1 
ATOM   16308 O O   . THR I  5 74  ? 67.530  78.020  302.183 1.00 211.87 ?  74  THR H O   1 
ATOM   16309 C CB  . THR I  5 74  ? 66.328  78.619  305.005 1.00 219.37 ?  74  THR H CB  1 
ATOM   16310 O OG1 . THR I  5 74  ? 66.137  78.269  306.380 1.00 222.18 ?  74  THR H OG1 1 
ATOM   16311 C CG2 . THR I  5 74  ? 65.225  79.573  304.586 1.00 226.15 ?  74  THR H CG2 1 
ATOM   16312 N N   . VAL I  5 75  ? 65.307  77.689  301.967 1.00 216.50 ?  75  VAL H N   1 
ATOM   16313 C CA  . VAL I  5 75  ? 65.185  78.269  300.635 1.00 217.78 ?  75  VAL H CA  1 
ATOM   16314 C C   . VAL I  5 75  ? 64.298  79.497  300.762 1.00 223.75 ?  75  VAL H C   1 
ATOM   16315 O O   . VAL I  5 75  ? 63.132  79.392  301.163 1.00 229.76 ?  75  VAL H O   1 
ATOM   16316 C CB  . VAL I  5 75  ? 64.612  77.268  299.622 1.00 218.04 ?  75  VAL H CB  1 
ATOM   16317 C CG1 . VAL I  5 75  ? 64.638  77.861  298.218 1.00 219.38 ?  75  VAL H CG1 1 
ATOM   16318 C CG2 . VAL I  5 75  ? 65.388  75.964  299.672 1.00 215.19 ?  75  VAL H CG2 1 
ATOM   16319 N N   . SER I  5 76  ? 64.852  80.663  300.423 1.00 220.15 ?  76  SER H N   1 
ATOM   16320 C CA  . SER I  5 76  ? 64.127  81.912  300.635 1.00 225.68 ?  76  SER H CA  1 
ATOM   16321 C C   . SER I  5 76  ? 62.932  82.027  299.695 1.00 231.18 ?  76  SER H C   1 
ATOM   16322 O O   . SER I  5 76  ? 61.869  82.517  300.094 1.00 237.36 ?  76  SER H O   1 
ATOM   16323 C CB  . SER I  5 76  ? 65.072  83.104  300.466 1.00 223.34 ?  76  SER H CB  1 
ATOM   16324 O OG  . SER I  5 76  ? 65.626  83.148  299.163 1.00 220.59 ?  76  SER H OG  1 
ATOM   16325 N N   . SER I  5 77  ? 63.089  81.596  298.444 1.00 230.05 ?  77  SER H N   1 
ATOM   16326 C CA  . SER I  5 77  ? 61.974  81.549  297.501 1.00 234.86 ?  77  SER H CA  1 
ATOM   16327 C C   . SER I  5 77  ? 62.169  80.339  296.597 1.00 231.62 ?  77  SER H C   1 
ATOM   16328 O O   . SER I  5 77  ? 63.106  80.312  295.793 1.00 227.48 ?  77  SER H O   1 
ATOM   16329 C CB  . SER I  5 77  ? 61.890  82.838  296.685 1.00 237.87 ?  77  SER H CB  1 
ATOM   16330 O OG  . SER I  5 77  ? 60.679  82.911  295.953 1.00 243.95 ?  77  SER H OG  1 
ATOM   16331 N N   . LEU I  5 78  ? 61.292  79.345  296.732 1.00 231.58 ?  78  LEU H N   1 
ATOM   16332 C CA  . LEU I  5 78  ? 61.411  78.120  295.951 1.00 228.78 ?  78  LEU H CA  1 
ATOM   16333 C C   . LEU I  5 78  ? 61.162  78.396  294.475 1.00 230.28 ?  78  LEU H C   1 
ATOM   16334 O O   . LEU I  5 78  ? 60.213  79.098  294.113 1.00 235.81 ?  78  LEU H O   1 
ATOM   16335 C CB  . LEU I  5 78  ? 60.426  77.062  296.449 1.00 231.49 ?  78  LEU H CB  1 
ATOM   16336 C CG  . LEU I  5 78  ? 60.717  76.314  297.749 1.00 229.35 ?  78  LEU H CG  1 
ATOM   16337 C CD1 . LEU I  5 78  ? 59.462  75.606  298.237 1.00 234.15 ?  78  LEU H CD1 1 
ATOM   16338 C CD2 . LEU I  5 78  ? 61.848  75.322  297.550 1.00 222.93 ?  78  LEU H CD2 1 
ATOM   16339 N N   . GLN I  5 79  ? 62.014  77.838  293.626 1.00 229.71 ?  79  GLN H N   1 
ATOM   16340 C CA  . GLN I  5 79  ? 61.850  77.838  292.183 1.00 230.82 ?  79  GLN H CA  1 
ATOM   16341 C C   . GLN I  5 79  ? 61.573  76.423  291.688 1.00 229.87 ?  79  GLN H C   1 
ATOM   16342 O O   . GLN I  5 79  ? 61.841  75.447  292.398 1.00 227.26 ?  79  GLN H O   1 
ATOM   16343 C CB  . GLN I  5 79  ? 63.098  78.415  291.496 1.00 226.83 ?  79  GLN H CB  1 
ATOM   16344 C CG  . GLN I  5 79  ? 63.471  79.808  291.984 1.00 227.57 ?  79  GLN H CG  1 
ATOM   16345 C CD  . GLN I  5 79  ? 64.548  80.459  291.139 1.00 224.63 ?  79  GLN H CD  1 
ATOM   16346 O OE1 . GLN I  5 79  ? 65.034  79.873  290.172 1.00 228.75 ?  79  GLN H OE1 1 
ATOM   16347 N NE2 . GLN I  5 79  ? 64.924  81.682  291.498 1.00 225.25 ?  79  GLN H NE2 1 
ATOM   16348 N N   . PRO I  5 80  ? 61.003  76.272  290.485 1.00 226.09 ?  80  PRO H N   1 
ATOM   16349 C CA  . PRO I  5 80  ? 60.621  74.926  290.016 1.00 225.77 ?  80  PRO H CA  1 
ATOM   16350 C C   . PRO I  5 80  ? 61.729  73.884  290.084 1.00 219.62 ?  80  PRO H C   1 
ATOM   16351 O O   . PRO I  5 80  ? 61.450  72.721  290.402 1.00 219.21 ?  80  PRO H O   1 
ATOM   16352 C CB  . PRO I  5 80  ? 60.177  75.187  288.572 1.00 228.52 ?  80  PRO H CB  1 
ATOM   16353 C CG  . PRO I  5 80  ? 59.651  76.580  288.605 1.00 233.02 ?  80  PRO H CG  1 
ATOM   16354 C CD  . PRO I  5 80  ? 60.548  77.323  289.554 1.00 230.10 ?  80  PRO H CD  1 
ATOM   16355 N N   . GLU I  5 81  ? 62.977  74.258  289.798 1.00 234.83 ?  81  GLU H N   1 
ATOM   16356 C CA  . GLU I  5 81  ? 64.053  73.274  289.835 1.00 229.23 ?  81  GLU H CA  1 
ATOM   16357 C C   . GLU I  5 81  ? 64.467  72.891  291.251 1.00 226.65 ?  81  GLU H C   1 
ATOM   16358 O O   . GLU I  5 81  ? 65.277  71.971  291.407 1.00 222.56 ?  81  GLU H O   1 
ATOM   16359 C CB  . GLU I  5 81  ? 65.274  73.780  289.062 1.00 225.46 ?  81  GLU H CB  1 
ATOM   16360 C CG  . GLU I  5 81  ? 65.882  75.060  289.605 1.00 224.32 ?  81  GLU H CG  1 
ATOM   16361 C CD  . GLU I  5 81  ? 65.363  76.297  288.901 1.00 228.53 ?  81  GLU H CD  1 
ATOM   16362 O OE1 . GLU I  5 81  ? 64.205  76.274  288.433 1.00 233.48 ?  81  GLU H OE1 1 
ATOM   16363 O OE2 . GLU I  5 81  ? 66.114  77.292  288.814 1.00 227.04 -1 81  GLU H OE2 1 
ATOM   16364 N N   . ASP I  5 82  ? 63.943  73.561  292.278 1.00 221.90 ?  82  ASP H N   1 
ATOM   16365 C CA  . ASP I  5 82  ? 64.321  73.255  293.652 1.00 219.73 ?  82  ASP H CA  1 
ATOM   16366 C C   . ASP I  5 82  ? 63.498  72.132  294.265 1.00 221.92 ?  82  ASP H C   1 
ATOM   16367 O O   . ASP I  5 82  ? 63.811  71.696  295.379 1.00 220.47 ?  82  ASP H O   1 
ATOM   16368 C CB  . ASP I  5 82  ? 64.204  74.501  294.540 1.00 221.42 ?  82  ASP H CB  1 
ATOM   16369 C CG  . ASP I  5 82  ? 65.107  75.630  294.088 1.00 219.23 ?  82  ASP H CG  1 
ATOM   16370 O OD1 . ASP I  5 82  ? 66.134  75.352  293.434 1.00 214.92 ?  82  ASP H OD1 1 
ATOM   16371 O OD2 . ASP I  5 82  ? 64.796  76.797  294.404 1.00 222.04 -1 82  ASP H OD2 1 
ATOM   16372 N N   . PHE I  5 83  ? 62.465  71.651  293.576 1.00 215.31 ?  83  PHE H N   1 
ATOM   16373 C CA  . PHE I  5 83  ? 61.649  70.560  294.096 1.00 217.68 ?  83  PHE H CA  1 
ATOM   16374 C C   . PHE I  5 83  ? 62.352  69.243  293.792 1.00 213.81 ?  83  PHE H C   1 
ATOM   16375 O O   . PHE I  5 83  ? 62.461  68.835  292.631 1.00 213.06 ?  83  PHE H O   1 
ATOM   16376 C CB  . PHE I  5 83  ? 60.244  70.610  293.504 1.00 223.40 ?  83  PHE H CB  1 
ATOM   16377 C CG  . PHE I  5 83  ? 59.440  71.788  293.978 1.00 227.96 ?  83  PHE H CG  1 
ATOM   16378 C CD1 . PHE I  5 83  ? 59.534  73.011  293.334 1.00 228.97 ?  83  PHE H CD1 1 
ATOM   16379 C CD2 . PHE I  5 83  ? 58.617  71.684  295.089 1.00 231.49 ?  83  PHE H CD2 1 
ATOM   16380 C CE1 . PHE I  5 83  ? 58.804  74.102  293.773 1.00 233.55 ?  83  PHE H CE1 1 
ATOM   16381 C CE2 . PHE I  5 83  ? 57.885  72.772  295.534 1.00 236.01 ?  83  PHE H CE2 1 
ATOM   16382 C CZ  . PHE I  5 83  ? 57.979  73.982  294.875 1.00 237.07 ?  83  PHE H CZ  1 
ATOM   16383 N N   . ALA I  5 84  ? 62.816  68.581  294.843 1.00 219.48 ?  84  ALA H N   1 
ATOM   16384 C CA  . ALA I  5 84  ? 63.762  67.471  294.768 1.00 215.27 ?  84  ALA H CA  1 
ATOM   16385 C C   . ALA I  5 84  ? 63.887  66.888  296.172 1.00 214.97 ?  84  ALA H C   1 
ATOM   16386 O O   . ALA I  5 84  ? 63.145  67.268  297.085 1.00 218.30 ?  84  ALA H O   1 
ATOM   16387 C CB  . ALA I  5 84  ? 65.111  67.926  294.207 1.00 210.41 ?  84  ALA H CB  1 
ATOM   16388 N N   . THR I  5 85  ? 64.816  65.949  296.341 1.00 209.61 ?  85  THR H N   1 
ATOM   16389 C CA  . THR I  5 85  ? 65.131  65.375  297.643 1.00 209.27 ?  85  THR H CA  1 
ATOM   16390 C C   . THR I  5 85  ? 66.404  66.014  298.195 1.00 204.91 ?  85  THR H C   1 
ATOM   16391 O O   . THR I  5 85  ? 67.368  66.235  297.456 1.00 200.99 ?  85  THR H O   1 
ATOM   16392 C CB  . THR I  5 85  ? 65.299  63.854  297.536 1.00 208.76 ?  85  THR H CB  1 
ATOM   16393 O OG1 . THR I  5 85  ? 64.102  63.274  296.999 1.00 212.68 ?  85  THR H OG1 1 
ATOM   16394 C CG2 . THR I  5 85  ? 65.545  63.248  298.898 1.00 208.77 ?  85  THR H CG2 1 
ATOM   16395 N N   . TYR I  5 86  ? 66.398  66.311  299.496 1.00 197.42 ?  86  TYR H N   1 
ATOM   16396 C CA  . TYR I  5 86  ? 67.517  66.953  300.179 1.00 193.54 ?  86  TYR H CA  1 
ATOM   16397 C C   . TYR I  5 86  ? 68.019  66.081  301.326 1.00 192.50 ?  86  TYR H C   1 
ATOM   16398 O O   . TYR I  5 86  ? 67.222  65.544  302.102 1.00 196.26 ?  86  TYR H O   1 
ATOM   16399 C CB  . TYR I  5 86  ? 67.122  68.337  300.722 1.00 195.34 ?  86  TYR H CB  1 
ATOM   16400 C CG  . TYR I  5 86  ? 66.812  69.382  299.667 1.00 196.11 ?  86  TYR H CG  1 
ATOM   16401 C CD1 . TYR I  5 86  ? 65.535  69.505  299.132 1.00 200.88 ?  86  TYR H CD1 1 
ATOM   16402 C CD2 . TYR I  5 86  ? 67.795  70.255  299.219 1.00 192.31 ?  86  TYR H CD2 1 
ATOM   16403 C CE1 . TYR I  5 86  ? 65.250  70.465  298.175 1.00 202.01 ?  86  TYR H CE1 1 
ATOM   16404 C CE2 . TYR I  5 86  ? 67.518  71.216  298.263 1.00 193.45 ?  86  TYR H CE2 1 
ATOM   16405 C CZ  . TYR I  5 86  ? 66.245  71.316  297.744 1.00 198.37 ?  86  TYR H CZ  1 
ATOM   16406 O OH  . TYR I  5 86  ? 65.965  72.270  296.793 1.00 199.87 ?  86  TYR H OH  1 
ATOM   16407 N N   . PHE I  5 87  ? 69.345  65.953  301.432 1.00 177.74 ?  87  PHE H N   1 
ATOM   16408 C CA  . PHE I  5 87  ? 70.000  65.178  302.480 1.00 176.63 ?  87  PHE H CA  1 
ATOM   16409 C C   . PHE I  5 87  ? 70.959  66.039  303.293 1.00 174.91 ?  87  PHE H C   1 
ATOM   16410 O O   . PHE I  5 87  ? 71.606  66.948  302.765 1.00 174.42 ?  87  PHE H O   1 
ATOM   16411 C CB  . PHE I  5 87  ? 70.788  63.993  301.898 1.00 176.78 ?  87  PHE H CB  1 
ATOM   16412 C CG  . PHE I  5 87  ? 69.931  62.957  301.237 1.00 178.46 ?  87  PHE H CG  1 
ATOM   16413 C CD1 . PHE I  5 87  ? 69.369  61.933  301.978 1.00 178.86 ?  87  PHE H CD1 1 
ATOM   16414 C CD2 . PHE I  5 87  ? 69.693  63.002  299.875 1.00 179.70 ?  87  PHE H CD2 1 
ATOM   16415 C CE1 . PHE I  5 87  ? 68.580  60.975  301.376 1.00 180.49 ?  87  PHE H CE1 1 
ATOM   16416 C CE2 . PHE I  5 87  ? 68.905  62.046  299.266 1.00 181.33 ?  87  PHE H CE2 1 
ATOM   16417 C CZ  . PHE I  5 87  ? 68.347  61.032  300.018 1.00 181.74 ?  87  PHE H CZ  1 
ATOM   16418 N N   . CYS I  5 88  ? 71.046  65.737  304.588 1.00 184.32 ?  88  CYS H N   1 
ATOM   16419 C CA  . CYS I  5 88  ? 72.110  66.233  305.449 1.00 182.69 ?  88  CYS H CA  1 
ATOM   16420 C C   . CYS I  5 88  ? 73.071  65.093  305.766 1.00 182.09 ?  88  CYS H C   1 
ATOM   16421 O O   . CYS I  5 88  ? 72.695  63.918  305.740 1.00 182.84 ?  88  CYS H O   1 
ATOM   16422 C CB  . CYS I  5 88  ? 71.555  66.841  306.745 1.00 182.15 ?  88  CYS H CB  1 
ATOM   16423 S SG  . CYS I  5 88  ? 70.570  65.731  307.778 1.00 182.71 ?  88  CYS H SG  1 
ATOM   16424 N N   . GLN I  5 89  ? 74.319  65.450  306.067 1.00 194.86 ?  89  GLN H N   1 
ATOM   16425 C CA  . GLN I  5 89  ? 75.366  64.464  306.301 1.00 192.38 ?  89  GLN H CA  1 
ATOM   16426 C C   . GLN I  5 89  ? 76.360  65.004  307.317 1.00 189.84 ?  89  GLN H C   1 
ATOM   16427 O O   . GLN I  5 89  ? 76.754  66.170  307.239 1.00 187.42 ?  89  GLN H O   1 
ATOM   16428 C CB  . GLN I  5 89  ? 76.093  64.113  304.998 1.00 188.81 ?  89  GLN H CB  1 
ATOM   16429 C CG  . GLN I  5 89  ? 77.279  63.171  305.168 1.00 186.06 ?  89  GLN H CG  1 
ATOM   16430 C CD  . GLN I  5 89  ? 78.527  63.665  304.452 1.00 180.86 ?  89  GLN H CD  1 
ATOM   16431 O OE1 . GLN I  5 89  ? 78.441  64.324  303.417 1.00 179.59 ?  89  GLN H OE1 1 
ATOM   16432 N NE2 . GLN I  5 89  ? 79.694  63.339  304.998 1.00 178.09 ?  89  GLN H NE2 1 
ATOM   16433 N N   . HIS I  5 90  ? 76.770  64.154  308.258 1.00 201.35 ?  90  HIS H N   1 
ATOM   16434 C CA  . HIS I  5 90  ? 77.799  64.505  309.224 1.00 198.73 ?  90  HIS H CA  1 
ATOM   16435 C C   . HIS I  5 90  ? 79.090  63.762  308.901 1.00 194.92 ?  90  HIS H C   1 
ATOM   16436 O O   . HIS I  5 90  ? 79.073  62.660  308.345 1.00 195.73 ?  90  HIS H O   1 
ATOM   16437 C CB  . HIS I  5 90  ? 77.384  64.158  310.656 1.00 202.50 ?  90  HIS H CB  1 
ATOM   16438 C CG  . HIS I  5 90  ? 77.824  62.795  311.095 1.00 203.51 ?  90  HIS H CG  1 
ATOM   16439 N ND1 . HIS I  5 90  ? 79.011  62.583  311.763 1.00 200.90 ?  90  HIS H ND1 1 
ATOM   16440 C CD2 . HIS I  5 90  ? 77.258  61.576  310.939 1.00 206.82 ?  90  HIS H CD2 1 
ATOM   16441 C CE1 . HIS I  5 90  ? 79.149  61.294  312.015 1.00 202.88 ?  90  HIS H CE1 1 
ATOM   16442 N NE2 . HIS I  5 90  ? 78.099  60.660  311.524 1.00 206.47 ?  90  HIS H NE2 1 
ATOM   16443 N N   . MET I  5 91  ? 80.216  64.380  309.265 1.00 202.85 ?  91  MET H N   1 
ATOM   16444 C CA  . MET I  5 91  ? 81.528  63.762  309.120 1.00 199.32 ?  91  MET H CA  1 
ATOM   16445 C C   . MET I  5 91  ? 82.352  63.826  310.404 1.00 198.45 ?  91  MET H C   1 
ATOM   16446 O O   . MET I  5 91  ? 83.585  63.767  310.344 1.00 194.71 ?  91  MET H O   1 
ATOM   16447 C CB  . MET I  5 91  ? 82.284  64.405  307.956 1.00 194.68 ?  91  MET H CB  1 
ATOM   16448 C CG  . MET I  5 91  ? 82.413  65.915  308.059 1.00 192.48 ?  91  MET H CG  1 
ATOM   16449 S SD  . MET I  5 91  ? 82.062  66.723  306.485 1.00 191.19 ?  91  MET H SD  1 
ATOM   16450 C CE  . MET I  5 91  ? 80.277  66.594  306.427 1.00 196.97 ?  91  MET H CE  1 
ATOM   16451 N N   . SER I  5 92  ? 81.703  63.947  311.566 1.00 185.48 ?  92  SER H N   1 
ATOM   16452 C CA  . SER I  5 92  ? 82.424  64.187  312.812 1.00 184.92 ?  92  SER H CA  1 
ATOM   16453 C C   . SER I  5 92  ? 83.109  62.941  313.367 1.00 185.57 ?  92  SER H C   1 
ATOM   16454 O O   . SER I  5 92  ? 83.998  63.073  314.216 1.00 184.24 ?  92  SER H O   1 
ATOM   16455 C CB  . SER I  5 92  ? 81.477  64.765  313.867 1.00 189.03 ?  92  SER H CB  1 
ATOM   16456 O OG  . SER I  5 92  ? 80.466  63.838  314.216 1.00 194.35 ?  92  SER H OG  1 
ATOM   16457 N N   . SER I  5 93  ? 82.729  61.748  312.915 1.00 182.31 ?  93  SER H N   1 
ATOM   16458 C CA  . SER I  5 93  ? 83.302  60.507  313.426 1.00 183.79 ?  93  SER H CA  1 
ATOM   16459 C C   . SER I  5 93  ? 82.812  59.363  312.550 1.00 186.06 ?  93  SER H C   1 
ATOM   16460 O O   . SER I  5 93  ? 81.876  59.517  311.762 1.00 187.23 ?  93  SER H O   1 
ATOM   16461 C CB  . SER I  5 93  ? 82.934  60.269  314.894 1.00 188.14 ?  93  SER H CB  1 
ATOM   16462 O OG  . SER I  5 93  ? 81.529  60.276  315.069 1.00 192.81 ?  93  SER H OG  1 
ATOM   16463 N N   . TYR I  5 94  ? 83.461  58.209  312.698 1.00 184.75 ?  94  TYR H N   1 
ATOM   16464 C CA  . TYR I  5 94  ? 83.141  57.033  311.891 1.00 187.15 ?  94  TYR H CA  1 
ATOM   16465 C C   . TYR I  5 94  ? 82.009  56.226  312.508 1.00 194.05 ?  94  TYR H C   1 
ATOM   16466 O O   . TYR I  5 94  ? 81.941  56.079  313.728 1.00 197.44 ?  94  TYR H O   1 
ATOM   16467 C CB  . TYR I  5 94  ? 84.364  56.120  311.725 1.00 185.89 ?  94  TYR H CB  1 
ATOM   16468 C CG  . TYR I  5 94  ? 85.501  56.695  310.908 1.00 179.59 ?  94  TYR H CG  1 
ATOM   16469 C CD1 . TYR I  5 94  ? 85.319  57.030  309.571 1.00 177.18 ?  94  TYR H CD1 1 
ATOM   16470 C CD2 . TYR I  5 94  ? 86.765  56.867  311.458 1.00 176.79 ?  94  TYR H CD2 1 
ATOM   16471 C CE1 . TYR I  5 94  ? 86.358  57.547  308.811 1.00 172.21 ?  94  TYR H CE1 1 
ATOM   16472 C CE2 . TYR I  5 94  ? 87.812  57.382  310.704 1.00 171.65 ?  94  TYR H CE2 1 
ATOM   16473 C CZ  . TYR I  5 94  ? 87.603  57.721  309.382 1.00 170.53 ?  94  TYR H CZ  1 
ATOM   16474 O OH  . TYR I  5 94  ? 88.645  58.230  308.638 1.00 170.22 ?  94  TYR H OH  1 
ATOM   16475 N N   . PRO I  5 95  ? 81.122  55.682  311.661 1.00 187.84 ?  95  PRO H N   1 
ATOM   16476 C CA  . PRO I  5 95  ? 81.073  55.903  310.212 1.00 184.43 ?  95  PRO H CA  1 
ATOM   16477 C C   . PRO I  5 95  ? 80.292  57.159  309.819 1.00 182.68 ?  95  PRO H C   1 
ATOM   16478 O O   . PRO I  5 95  ? 79.422  57.598  310.571 1.00 185.47 ?  95  PRO H O   1 
ATOM   16479 C CB  . PRO I  5 95  ? 80.372  54.645  309.704 1.00 189.05 ?  95  PRO H CB  1 
ATOM   16480 C CG  . PRO I  5 95  ? 79.428  54.310  310.800 1.00 194.92 ?  95  PRO H CG  1 
ATOM   16481 C CD  . PRO I  5 95  ? 80.139  54.671  312.087 1.00 194.58 ?  95  PRO H CD  1 
ATOM   16482 N N   . LEU I  5 96  ? 80.618  57.730  308.659 1.00 183.44 ?  96  LEU H N   1 
ATOM   16483 C CA  . LEU I  5 96  ? 79.813  58.806  308.093 1.00 182.87 ?  96  LEU H CA  1 
ATOM   16484 C C   . LEU I  5 96  ? 78.394  58.312  307.839 1.00 187.63 ?  96  LEU H C   1 
ATOM   16485 O O   . LEU I  5 96  ? 78.185  57.183  307.386 1.00 189.70 ?  96  LEU H O   1 
ATOM   16486 C CB  . LEU I  5 96  ? 80.432  59.306  306.783 1.00 178.46 ?  96  LEU H CB  1 
ATOM   16487 C CG  . LEU I  5 96  ? 81.480  60.423  306.798 1.00 176.45 ?  96  LEU H CG  1 
ATOM   16488 C CD1 . LEU I  5 96  ? 82.634  60.096  307.731 1.00 175.49 ?  96  LEU H CD1 1 
ATOM   16489 C CD2 . LEU I  5 96  ? 81.990  60.694  305.390 1.00 176.83 ?  96  LEU H CD2 1 
ATOM   16490 N N   . THR I  5 97  ? 77.408  59.156  308.147 1.00 186.05 ?  97  THR H N   1 
ATOM   16491 C CA  . THR I  5 97  ? 76.013  58.800  307.919 1.00 190.51 ?  97  THR H CA  1 
ATOM   16492 C C   . THR I  5 97  ? 75.254  59.960  307.286 1.00 190.36 ?  97  THR H C   1 
ATOM   16493 O O   . THR I  5 97  ? 75.634  61.128  307.403 1.00 187.83 ?  97  THR H O   1 
ATOM   16494 C CB  . THR I  5 97  ? 75.303  58.379  309.218 1.00 195.47 ?  97  THR H CB  1 
ATOM   16495 O OG1 . THR I  5 97  ? 75.309  59.467  310.149 1.00 195.25 ?  97  THR H OG1 1 
ATOM   16496 C CG2 . THR I  5 97  ? 75.983  57.169  309.850 1.00 196.85 ?  97  THR H CG2 1 
ATOM   16497 N N   . PHE I  5 98  ? 74.162  59.605  306.615 1.00 188.90 ?  98  PHE H N   1 
ATOM   16498 C CA  . PHE I  5 98  ? 73.255  60.536  305.962 1.00 189.73 ?  98  PHE H CA  1 
ATOM   16499 C C   . PHE I  5 98  ? 71.901  60.500  306.659 1.00 195.24 ?  98  PHE H C   1 
ATOM   16500 O O   . PHE I  5 98  ? 71.525  59.493  307.267 1.00 198.62 ?  98  PHE H O   1 
ATOM   16501 C CB  . PHE I  5 98  ? 73.065  60.190  304.482 1.00 188.97 ?  98  PHE H CB  1 
ATOM   16502 C CG  . PHE I  5 98  ? 74.290  60.397  303.638 1.00 183.85 ?  98  PHE H CG  1 
ATOM   16503 C CD1 . PHE I  5 98  ? 75.292  59.439  303.594 1.00 181.92 ?  98  PHE H CD1 1 
ATOM   16504 C CD2 . PHE I  5 98  ? 74.424  61.536  302.863 1.00 181.50 ?  98  PHE H CD2 1 
ATOM   16505 C CE1 . PHE I  5 98  ? 76.414  59.624  302.806 1.00 180.93 ?  98  PHE H CE1 1 
ATOM   16506 C CE2 . PHE I  5 98  ? 75.542  61.727  302.073 1.00 181.09 ?  98  PHE H CE2 1 
ATOM   16507 C CZ  . PHE I  5 98  ? 76.539  60.770  302.044 1.00 180.80 ?  98  PHE H CZ  1 
ATOM   16508 N N   . GLY I  5 99  ? 71.171  61.606  306.568 1.00 181.01 ?  99  GLY H N   1 
ATOM   16509 C CA  . GLY I  5 99  ? 69.793  61.619  307.011 1.00 181.92 ?  99  GLY H CA  1 
ATOM   16510 C C   . GLY I  5 99  ? 68.888  60.811  306.099 1.00 183.68 ?  99  GLY H C   1 
ATOM   16511 O O   . GLY I  5 99  ? 69.270  60.352  305.022 1.00 184.26 ?  99  GLY H O   1 
ATOM   16512 N N   . GLY I  5 100 ? 67.645  60.636  306.551 1.00 195.42 ?  100 GLY H N   1 
ATOM   16513 C CA  . GLY I  5 100 ? 66.692  59.845  305.796 1.00 198.29 ?  100 GLY H CA  1 
ATOM   16514 C C   . GLY I  5 100 ? 66.076  60.548  304.608 1.00 198.23 ?  100 GLY H C   1 
ATOM   16515 O O   . GLY I  5 100 ? 65.400  59.901  303.803 1.00 199.96 ?  100 GLY H O   1 
ATOM   16516 N N   . GLY I  5 101 ? 66.307  61.844  304.472 1.00 206.42 ?  101 GLY H N   1 
ATOM   16517 C CA  . GLY I  5 101 ? 65.848  62.605  303.328 1.00 206.39 ?  101 GLY H CA  1 
ATOM   16518 C C   . GLY I  5 101 ? 64.527  63.316  303.566 1.00 211.20 ?  101 GLY H C   1 
ATOM   16519 O O   . GLY I  5 101 ? 63.652  62.846  304.302 1.00 215.65 ?  101 GLY H O   1 
ATOM   16520 N N   . THR I  5 102 ? 64.387  64.481  302.931 1.00 201.97 ?  102 THR H N   1 
ATOM   16521 C CA  . THR I  5 102 ? 63.153  65.258  302.899 1.00 203.05 ?  102 THR H CA  1 
ATOM   16522 C C   . THR I  5 102 ? 62.805  65.521  301.440 1.00 204.48 ?  102 THR H C   1 
ATOM   16523 O O   . THR I  5 102 ? 63.571  66.183  300.732 1.00 203.97 ?  102 THR H O   1 
ATOM   16524 C CB  . THR I  5 102 ? 63.306  66.581  303.663 1.00 201.87 ?  102 THR H CB  1 
ATOM   16525 O OG1 . THR I  5 102 ? 63.488  66.321  305.062 1.00 200.75 ?  102 THR H OG1 1 
ATOM   16526 C CG2 . THR I  5 102 ? 62.087  67.467  303.465 1.00 203.10 ?  102 THR H CG2 1 
ATOM   16527 N N   . LYS I  5 103 ? 61.663  65.002  300.988 1.00 242.68 ?  103 LYS H N   1 
ATOM   16528 C CA  . LYS I  5 103 ? 61.218  65.186  299.609 1.00 241.60 ?  103 LYS H CA  1 
ATOM   16529 C C   . LYS I  5 103 ? 60.271  66.379  299.530 1.00 241.07 ?  103 LYS H C   1 
ATOM   16530 O O   . LYS I  5 103 ? 59.244  66.413  300.218 1.00 241.13 ?  103 LYS H O   1 
ATOM   16531 C CB  . LYS I  5 103 ? 60.541  63.919  299.085 1.00 241.14 ?  103 LYS H CB  1 
ATOM   16532 C CG  . LYS I  5 103 ? 60.168  63.982  297.610 1.00 240.04 ?  103 LYS H CG  1 
ATOM   16533 C CD  . LYS I  5 103 ? 59.665  62.640  297.106 1.00 239.68 ?  103 LYS H CD  1 
ATOM   16534 C CE  . LYS I  5 103 ? 59.568  62.629  295.591 1.00 238.67 ?  103 LYS H CE  1 
ATOM   16535 N NZ  . LYS I  5 103 ? 59.410  61.248  295.065 1.00 238.43 1  103 LYS H NZ  1 
ATOM   16536 N N   . VAL I  5 104 ? 60.612  67.349  298.685 1.00 240.55 ?  104 VAL H N   1 
ATOM   16537 C CA  . VAL I  5 104 ? 59.830  68.569  298.511 1.00 240.03 ?  104 VAL H CA  1 
ATOM   16538 C C   . VAL I  5 104 ? 59.043  68.457  297.211 1.00 238.91 ?  104 VAL H C   1 
ATOM   16539 O O   . VAL I  5 104 ? 59.629  68.328  296.128 1.00 238.44 ?  104 VAL H O   1 
ATOM   16540 C CB  . VAL I  5 104 ? 60.727  69.818  298.515 1.00 240.25 ?  104 VAL H CB  1 
ATOM   16541 C CG1 . VAL I  5 104 ? 59.885  71.079  298.434 1.00 239.76 ?  104 VAL H CG1 1 
ATOM   16542 C CG2 . VAL I  5 104 ? 61.608  69.853  299.763 1.00 241.39 ?  104 VAL H CG2 1 
ATOM   16543 N N   . GLU I  5 105 ? 57.717  68.500  297.318 1.00 252.59 ?  105 GLU H N   1 
ATOM   16544 C CA  . GLU I  5 105 ? 56.808  68.372  296.190 1.00 251.55 ?  105 GLU H CA  1 
ATOM   16545 C C   . GLU I  5 105 ? 55.995  69.650  296.021 1.00 251.02 ?  105 GLU H C   1 
ATOM   16546 O O   . GLU I  5 105 ? 55.859  70.453  296.948 1.00 251.49 ?  105 GLU H O   1 
ATOM   16547 C CB  . GLU I  5 105 ? 55.876  67.168  296.374 1.00 260.32 ?  105 GLU H CB  1 
ATOM   16548 C CG  . GLU I  5 105 ? 55.110  67.182  297.684 1.00 272.24 ?  105 GLU H CG  1 
ATOM   16549 C CD  . GLU I  5 105 ? 53.783  66.479  297.582 1.00 282.71 ?  105 GLU H CD  1 
ATOM   16550 O OE1 . GLU I  5 105 ? 53.754  65.335  297.088 1.00 292.44 ?  105 GLU H OE1 1 
ATOM   16551 O OE2 . GLU I  5 105 ? 52.768  67.068  297.999 1.00 281.69 -1 105 GLU H OE2 1 
ATOM   16552 N N   . ILE I  5 106 ? 55.458  69.833  294.814 1.00 257.36 ?  106 ILE H N   1 
ATOM   16553 C CA  . ILE I  5 106 ? 54.703  71.031  294.458 1.00 253.88 ?  106 ILE H CA  1 
ATOM   16554 C C   . ILE I  5 106 ? 53.241  70.833  294.840 1.00 263.99 ?  106 ILE H C   1 
ATOM   16555 O O   . ILE I  5 106 ? 52.652  69.784  294.556 1.00 272.23 ?  106 ILE H O   1 
ATOM   16556 C CB  . ILE I  5 106 ? 54.837  71.345  292.957 1.00 251.34 ?  106 ILE H CB  1 
ATOM   16557 C CG1 . ILE I  5 106 ? 56.306  71.488  292.556 1.00 251.58 ?  106 ILE H CG1 1 
ATOM   16558 C CG2 . ILE I  5 106 ? 54.071  72.613  292.601 1.00 250.71 ?  106 ILE H CG2 1 
ATOM   16559 C CD1 . ILE I  5 106 ? 56.501  71.893  291.109 1.00 250.70 ?  106 ILE H CD1 1 
ATOM   16560 N N   . LYS I  5 107 ? 52.658  71.838  295.494 1.00 256.09 ?  107 LYS H N   1 
ATOM   16561 C CA  . LYS I  5 107 ? 51.226  71.852  295.761 1.00 265.04 ?  107 LYS H CA  1 
ATOM   16562 C C   . LYS I  5 107 ? 50.449  72.283  294.521 1.00 263.15 ?  107 LYS H C   1 
ATOM   16563 O O   . LYS I  5 107 ? 50.884  73.164  293.773 1.00 256.69 ?  107 LYS H O   1 
ATOM   16564 C CB  . LYS I  5 107 ? 50.904  72.794  296.923 1.00 268.22 ?  107 LYS H CB  1 
ATOM   16565 C CG  . LYS I  5 107 ? 51.442  72.354  298.279 1.00 271.66 ?  107 LYS H CG  1 
ATOM   16566 C CD  . LYS I  5 107 ? 51.142  73.398  299.349 1.00 276.75 ?  107 LYS H CD  1 
ATOM   16567 C CE  . LYS I  5 107 ? 49.689  73.330  299.796 1.00 286.62 ?  107 LYS H CE  1 
ATOM   16568 N NZ  . LYS I  5 107 ? 49.561  73.287  301.278 1.00 292.82 1  107 LYS H NZ  1 
ATOM   16569 N N   . ARG I  5 108 ? 49.291  71.658  294.313 1.00 259.88 ?  108 ARG H N   1 
ATOM   16570 C CA  . ARG I  5 108 ? 48.349  72.076  293.282 1.00 258.87 ?  108 ARG H CA  1 
ATOM   16571 C C   . ARG I  5 108 ? 46.932  71.815  293.778 1.00 267.08 ?  108 ARG H C   1 
ATOM   16572 O O   . ARG I  5 108 ? 46.719  71.319  294.888 1.00 274.18 ?  108 ARG H O   1 
ATOM   16573 C CB  . ARG I  5 108 ? 48.599  71.357  291.950 1.00 258.72 ?  108 ARG H CB  1 
ATOM   16574 C CG  . ARG I  5 108 ? 48.588  69.839  292.041 1.00 267.83 ?  108 ARG H CG  1 
ATOM   16575 C CD  . ARG I  5 108 ? 48.137  69.188  290.737 1.00 268.77 ?  108 ARG H CD  1 
ATOM   16576 N NE  . ARG I  5 108 ? 46.718  69.412  290.468 1.00 272.32 ?  108 ARG H NE  1 
ATOM   16577 C CZ  . ARG I  5 108 ? 46.165  69.344  289.262 1.00 272.80 ?  108 ARG H CZ  1 
ATOM   16578 N NH1 . ARG I  5 108 ? 46.911  69.062  288.203 1.00 269.61 1  108 ARG H NH1 1 
ATOM   16579 N NH2 . ARG I  5 108 ? 44.864  69.560  289.112 1.00 276.70 ?  108 ARG H NH2 1 
ATOM   16580 N N   . THR I  5 109 ? 45.960  72.166  292.942 1.00 263.90 ?  109 THR H N   1 
ATOM   16581 C CA  . THR I  5 109 ? 44.561  71.934  293.266 1.00 271.27 ?  109 THR H CA  1 
ATOM   16582 C C   . THR I  5 109 ? 44.253  70.440  293.297 1.00 280.55 ?  109 THR H C   1 
ATOM   16583 O O   . THR I  5 109 ? 44.893  69.635  292.614 1.00 280.48 ?  109 THR H O   1 
ATOM   16584 C CB  . THR I  5 109 ? 43.654  72.633  292.254 1.00 267.39 ?  109 THR H CB  1 
ATOM   16585 O OG1 . THR I  5 109 ? 43.867  72.070  290.954 1.00 266.56 ?  109 THR H OG1 1 
ATOM   16586 C CG2 . THR I  5 109 ? 43.958  74.126  292.210 1.00 259.38 ?  109 THR H CG2 1 
ATOM   16587 N N   . VAL I  5 110 ? 43.265  70.075  294.118 1.00 275.61 ?  110 VAL H N   1 
ATOM   16588 C CA  . VAL I  5 110 ? 42.858  68.679  294.245 1.00 275.70 ?  110 VAL H CA  1 
ATOM   16589 C C   . VAL I  5 110 ? 42.290  68.178  292.922 1.00 274.74 ?  110 VAL H C   1 
ATOM   16590 O O   . VAL I  5 110 ? 41.465  68.847  292.286 1.00 274.01 ?  110 VAL H O   1 
ATOM   16591 C CB  . VAL I  5 110 ? 41.843  68.537  295.389 1.00 276.10 ?  110 VAL H CB  1 
ATOM   16592 C CG1 . VAL I  5 110 ? 41.267  67.145  295.411 1.00 276.07 ?  110 VAL H CG1 1 
ATOM   16593 C CG2 . VAL I  5 110 ? 42.494  68.870  296.725 1.00 277.11 ?  110 VAL H CG2 1 
ATOM   16594 N N   . ALA I  5 111 ? 42.728  66.987  292.502 1.00 280.07 ?  111 ALA H N   1 
ATOM   16595 C CA  . ALA I  5 111 ? 42.271  66.376  291.255 1.00 280.72 ?  111 ALA H CA  1 
ATOM   16596 C C   . ALA I  5 111 ? 41.979  64.900  291.481 1.00 288.98 ?  111 ALA H C   1 
ATOM   16597 O O   . ALA I  5 111 ? 42.847  64.151  291.939 1.00 289.54 ?  111 ALA H O   1 
ATOM   16598 C CB  . ALA I  5 111 ? 43.305  66.549  290.142 1.00 272.99 ?  111 ALA H CB  1 
ATOM   16599 N N   . ALA I  5 112 ? 40.759  64.482  291.158 1.00 291.00 ?  112 ALA H N   1 
ATOM   16600 C CA  . ALA I  5 112 ? 40.377  63.089  291.322 1.00 290.77 ?  112 ALA H CA  1 
ATOM   16601 C C   . ALA I  5 112 ? 41.000  62.206  290.237 1.00 287.03 ?  112 ALA H C   1 
ATOM   16602 O O   . ALA I  5 112 ? 41.207  62.648  289.104 1.00 288.74 ?  112 ALA H O   1 
ATOM   16603 C CB  . ALA I  5 112 ? 38.859  62.959  291.299 1.00 292.84 ?  112 ALA H CB  1 
ATOM   16604 N N   . PRO I  5 113 ? 41.306  60.950  290.561 1.00 299.26 ?  113 PRO H N   1 
ATOM   16605 C CA  . PRO I  5 113 ? 41.882  60.041  289.565 1.00 295.86 ?  113 PRO H CA  1 
ATOM   16606 C C   . PRO I  5 113 ? 40.866  59.538  288.551 1.00 293.31 ?  113 PRO H C   1 
ATOM   16607 O O   . PRO I  5 113 ? 39.684  59.349  288.851 1.00 292.14 ?  113 PRO H O   1 
ATOM   16608 C CB  . PRO I  5 113 ? 42.406  58.876  290.417 1.00 293.23 ?  113 PRO H CB  1 
ATOM   16609 C CG  . PRO I  5 113 ? 41.512  58.864  291.599 1.00 294.37 ?  113 PRO H CG  1 
ATOM   16610 C CD  . PRO I  5 113 ? 41.168  60.304  291.879 1.00 298.71 ?  113 PRO H CD  1 
ATOM   16611 N N   . SER I  5 114 ? 41.354  59.316  287.331 1.00 289.08 ?  114 SER H N   1 
ATOM   16612 C CA  . SER I  5 114 ? 40.629  58.533  286.340 1.00 290.68 ?  114 SER H CA  1 
ATOM   16613 C C   . SER I  5 114 ? 41.028  57.072  286.505 1.00 289.36 ?  114 SER H C   1 
ATOM   16614 O O   . SER I  5 114 ? 42.217  56.738  286.464 1.00 284.36 ?  114 SER H O   1 
ATOM   16615 C CB  . SER I  5 114 ? 40.936  59.018  284.921 1.00 287.28 ?  114 SER H CB  1 
ATOM   16616 O OG  . SER I  5 114 ? 40.475  60.342  284.709 1.00 291.74 ?  114 SER H OG  1 
ATOM   16617 N N   . VAL I  5 115 ? 40.035  56.205  286.679 1.00 282.97 ?  115 VAL H N   1 
ATOM   16618 C CA  . VAL I  5 115 ? 40.267  54.816  287.059 1.00 282.51 ?  115 VAL H CA  1 
ATOM   16619 C C   . VAL I  5 115 ? 39.839  53.913  285.913 1.00 282.72 ?  115 VAL H C   1 
ATOM   16620 O O   . VAL I  5 115 ? 38.745  54.073  285.355 1.00 286.35 ?  115 VAL H O   1 
ATOM   16621 C CB  . VAL I  5 115 ? 39.528  54.453  288.359 1.00 287.56 ?  115 VAL H CB  1 
ATOM   16622 C CG1 . VAL I  5 115 ? 39.873  53.037  288.784 1.00 285.04 ?  115 VAL H CG1 1 
ATOM   16623 C CG2 . VAL I  5 115 ? 39.877  55.440  289.466 1.00 287.84 ?  115 VAL H CG2 1 
ATOM   16624 N N   . PHE I  5 116 ? 40.704  52.964  285.570 1.00 275.35 ?  116 PHE H N   1 
ATOM   16625 C CA  . PHE I  5 116 ? 40.465  52.001  284.510 1.00 273.79 ?  116 PHE H CA  1 
ATOM   16626 C C   . PHE I  5 116 ? 40.882  50.631  285.020 1.00 271.53 ?  116 PHE H C   1 
ATOM   16627 O O   . PHE I  5 116 ? 41.898  50.503  285.710 1.00 270.24 ?  116 PHE H O   1 
ATOM   16628 C CB  . PHE I  5 116 ? 41.259  52.342  283.245 1.00 269.60 ?  116 PHE H CB  1 
ATOM   16629 C CG  . PHE I  5 116 ? 41.060  53.751  282.760 1.00 271.28 ?  116 PHE H CG  1 
ATOM   16630 C CD1 . PHE I  5 116 ? 41.834  54.785  283.264 1.00 268.75 ?  116 PHE H CD1 1 
ATOM   16631 C CD2 . PHE I  5 116 ? 40.100  54.042  281.808 1.00 273.49 ?  116 PHE H CD2 1 
ATOM   16632 C CE1 . PHE I  5 116 ? 41.661  56.082  282.819 1.00 268.79 ?  116 PHE H CE1 1 
ATOM   16633 C CE2 . PHE I  5 116 ? 39.920  55.339  281.361 1.00 272.97 ?  116 PHE H CE2 1 
ATOM   16634 C CZ  . PHE I  5 116 ? 40.701  56.359  281.868 1.00 270.89 ?  116 PHE H CZ  1 
ATOM   16635 N N   . ILE I  5 117 ? 40.102  49.611  284.679 1.00 288.31 ?  117 ILE H N   1 
ATOM   16636 C CA  . ILE I  5 117 ? 40.433  48.232  285.010 1.00 280.95 ?  117 ILE H CA  1 
ATOM   16637 C C   . ILE I  5 117 ? 40.672  47.477  283.710 1.00 274.81 ?  117 ILE H C   1 
ATOM   16638 O O   . ILE I  5 117 ? 39.949  47.665  282.725 1.00 277.21 ?  117 ILE H O   1 
ATOM   16639 C CB  . ILE I  5 117 ? 39.330  47.566  285.864 1.00 284.29 ?  117 ILE H CB  1 
ATOM   16640 C CG1 . ILE I  5 117 ? 39.790  46.196  286.365 1.00 277.30 ?  117 ILE H CG1 1 
ATOM   16641 C CG2 . ILE I  5 117 ? 38.005  47.462  285.102 1.00 288.43 ?  117 ILE H CG2 1 
ATOM   16642 C CD1 . ILE I  5 117 ? 38.938  45.639  287.480 1.00 280.78 ?  117 ILE H CD1 1 
ATOM   16643 N N   . PHE I  5 118 ? 41.714  46.651  283.698 1.00 277.93 ?  118 PHE H N   1 
ATOM   16644 C CA  . PHE I  5 118 ? 42.074  45.872  282.523 1.00 271.76 ?  118 PHE H CA  1 
ATOM   16645 C C   . PHE I  5 118 ? 42.134  44.397  282.883 1.00 266.11 ?  118 PHE H C   1 
ATOM   16646 O O   . PHE I  5 118 ? 42.953  44.002  283.732 1.00 262.30 ?  118 PHE H O   1 
ATOM   16647 C CB  . PHE I  5 118 ? 43.409  46.347  281.950 1.00 267.43 ?  118 PHE H CB  1 
ATOM   16648 C CG  . PHE I  5 118 ? 43.419  47.803  281.593 1.00 273.06 ?  118 PHE H CG  1 
ATOM   16649 C CD1 . PHE I  5 118 ? 42.881  48.230  280.394 1.00 276.53 ?  118 PHE H CD1 1 
ATOM   16650 C CD2 . PHE I  5 118 ? 43.956  48.744  282.455 1.00 274.79 ?  118 PHE H CD2 1 
ATOM   16651 C CE1 . PHE I  5 118 ? 42.879  49.565  280.054 1.00 282.27 ?  118 PHE H CE1 1 
ATOM   16652 C CE2 . PHE I  5 118 ? 43.958  50.085  282.121 1.00 279.98 ?  118 PHE H CE2 1 
ATOM   16653 C CZ  . PHE I  5 118 ? 43.418  50.495  280.917 1.00 284.00 ?  118 PHE H CZ  1 
ATOM   16654 N N   . PRO I  5 119 ? 41.301  43.557  282.280 1.00 272.34 ?  119 PRO H N   1 
ATOM   16655 C CA  . PRO I  5 119 ? 41.378  42.119  282.530 1.00 272.86 ?  119 PRO H CA  1 
ATOM   16656 C C   . PRO I  5 119 ? 42.659  41.541  281.961 1.00 270.36 ?  119 PRO H C   1 
ATOM   16657 O O   . PRO I  5 119 ? 43.310  42.170  281.111 1.00 268.41 ?  119 PRO H O   1 
ATOM   16658 C CB  . PRO I  5 119 ? 40.142  41.573  281.802 1.00 274.78 ?  119 PRO H CB  1 
ATOM   16659 C CG  . PRO I  5 119 ? 39.909  42.554  280.700 1.00 274.13 ?  119 PRO H CG  1 
ATOM   16660 C CD  . PRO I  5 119 ? 40.292  43.895  281.262 1.00 273.36 ?  119 PRO H CD  1 
ATOM   16661 N N   . PRO I  5 120 ? 43.064  40.353  282.406 1.00 293.53 ?  120 PRO H N   1 
ATOM   16662 C CA  . PRO I  5 120 ? 44.220  39.698  281.784 1.00 286.34 ?  120 PRO H CA  1 
ATOM   16663 C C   . PRO I  5 120 ? 43.908  39.297  280.351 1.00 286.55 ?  120 PRO H C   1 
ATOM   16664 O O   . PRO I  5 120 ? 42.785  38.903  280.026 1.00 289.07 ?  120 PRO H O   1 
ATOM   16665 C CB  . PRO I  5 120 ? 44.459  38.473  282.674 1.00 283.48 ?  120 PRO H CB  1 
ATOM   16666 C CG  . PRO I  5 120 ? 43.135  38.220  283.333 1.00 290.13 ?  120 PRO H CG  1 
ATOM   16667 C CD  . PRO I  5 120 ? 42.525  39.574  283.535 1.00 296.54 ?  120 PRO H CD  1 
ATOM   16668 N N   . SER I  5 121 ? 44.913  39.413  279.490 1.00 281.52 ?  121 SER H N   1 
ATOM   16669 C CA  . SER I  5 121 ? 44.769  38.965  278.115 1.00 279.53 ?  121 SER H CA  1 
ATOM   16670 C C   . SER I  5 121 ? 44.722  37.440  278.054 1.00 275.20 ?  121 SER H C   1 
ATOM   16671 O O   . SER I  5 121 ? 45.206  36.740  278.948 1.00 272.63 ?  121 SER H O   1 
ATOM   16672 C CB  . SER I  5 121 ? 45.913  39.496  277.255 1.00 276.61 ?  121 SER H CB  1 
ATOM   16673 O OG  . SER I  5 121 ? 47.156  38.977  277.691 1.00 271.45 ?  121 SER H OG  1 
ATOM   16674 N N   . ASP I  5 122 ? 44.108  36.928  276.984 1.00 286.21 ?  122 ASP H N   1 
ATOM   16675 C CA  . ASP I  5 122 ? 44.077  35.483  276.771 1.00 283.14 ?  122 ASP H CA  1 
ATOM   16676 C C   . ASP I  5 122 ? 45.474  34.912  276.563 1.00 276.70 ?  122 ASP H C   1 
ATOM   16677 O O   . ASP I  5 122 ? 45.731  33.756  276.921 1.00 273.84 ?  122 ASP H O   1 
ATOM   16678 C CB  . ASP I  5 122 ? 43.182  35.143  275.577 1.00 284.68 ?  122 ASP H CB  1 
ATOM   16679 C CG  . ASP I  5 122 ? 41.710  35.386  275.861 1.00 293.33 ?  122 ASP H CG  1 
ATOM   16680 O OD1 . ASP I  5 122 ? 41.330  35.440  277.049 1.00 293.53 ?  122 ASP H OD1 1 
ATOM   16681 O OD2 . ASP I  5 122 ? 40.932  35.517  274.892 1.00 298.63 -1 122 ASP H OD2 1 
ATOM   16682 N N   . GLU I  5 123 ? 46.385  35.698  275.982 1.00 264.74 ?  123 GLU H N   1 
ATOM   16683 C CA  . GLU I  5 123 ? 47.749  35.221  275.776 1.00 259.23 ?  123 GLU H CA  1 
ATOM   16684 C C   . GLU I  5 123 ? 48.423  34.877  277.097 1.00 257.35 ?  123 GLU H C   1 
ATOM   16685 O O   . GLU I  5 123 ? 49.110  33.854  277.205 1.00 255.62 ?  123 GLU H O   1 
ATOM   16686 C CB  . GLU I  5 123 ? 48.561  36.271  275.023 1.00 258.91 ?  123 GLU H CB  1 
ATOM   16687 C CG  . GLU I  5 123 ? 49.943  35.796  274.621 1.00 253.33 ?  123 GLU H CG  1 
ATOM   16688 C CD  . GLU I  5 123 ? 50.797  36.910  274.055 1.00 253.33 ?  123 GLU H CD  1 
ATOM   16689 O OE1 . GLU I  5 123 ? 50.269  38.026  273.864 1.00 257.92 ?  123 GLU H OE1 1 
ATOM   16690 O OE2 . GLU I  5 123 ? 51.995  36.670  273.797 1.00 249.00 -1 123 GLU H OE2 1 
ATOM   16691 N N   . GLN I  5 124 ? 48.246  35.725  278.112 1.00 270.52 ?  124 GLN H N   1 
ATOM   16692 C CA  . GLN I  5 124 ? 48.839  35.449  279.416 1.00 268.79 ?  124 GLN H CA  1 
ATOM   16693 C C   . GLN I  5 124 ? 48.187  34.239  280.073 1.00 274.42 ?  124 GLN H C   1 
ATOM   16694 O O   . GLN I  5 124 ? 48.868  33.432  280.717 1.00 276.29 ?  124 GLN H O   1 
ATOM   16695 C CB  . GLN I  5 124 ? 48.722  36.678  280.318 1.00 271.24 ?  124 GLN H CB  1 
ATOM   16696 C CG  . GLN I  5 124 ? 49.414  36.523  281.662 1.00 269.63 ?  124 GLN H CG  1 
ATOM   16697 C CD  . GLN I  5 124 ? 49.095  37.649  282.624 1.00 273.56 ?  124 GLN H CD  1 
ATOM   16698 O OE1 . GLN I  5 124 ? 48.135  38.396  282.433 1.00 279.69 ?  124 GLN H OE1 1 
ATOM   16699 N NE2 . GLN I  5 124 ? 49.902  37.776  283.669 1.00 272.05 ?  124 GLN H NE2 1 
ATOM   16700 N N   . LEU I  5 125 ? 46.866  34.105  279.929 1.00 270.09 ?  125 LEU H N   1 
ATOM   16701 C CA  . LEU I  5 125 ? 46.155  32.985  280.538 1.00 275.76 ?  125 LEU H CA  1 
ATOM   16702 C C   . LEU I  5 125 ? 46.651  31.643  280.010 1.00 277.26 ?  125 LEU H C   1 
ATOM   16703 O O   . LEU I  5 125 ? 46.641  30.647  280.743 1.00 282.40 ?  125 LEU H O   1 
ATOM   16704 C CB  . LEU I  5 125 ? 44.652  33.139  280.306 1.00 277.34 ?  125 LEU H CB  1 
ATOM   16705 C CG  . LEU I  5 125 ? 43.960  34.205  281.160 1.00 280.91 ?  125 LEU H CG  1 
ATOM   16706 C CD1 . LEU I  5 125 ? 42.533  34.446  280.687 1.00 289.25 ?  125 LEU H CD1 1 
ATOM   16707 C CD2 . LEU I  5 125 ? 43.987  33.808  282.630 1.00 286.63 ?  125 LEU H CD2 1 
ATOM   16708 N N   . LYS I  5 126 ? 47.067  31.590  278.741 1.00 284.86 ?  126 LYS H N   1 
ATOM   16709 C CA  . LYS I  5 126 ? 47.603  30.352  278.181 1.00 284.37 ?  126 LYS H CA  1 
ATOM   16710 C C   . LYS I  5 126 ? 48.864  29.889  278.905 1.00 283.71 ?  126 LYS H C   1 
ATOM   16711 O O   . LYS I  5 126 ? 49.145  28.686  278.948 1.00 288.23 ?  126 LYS H O   1 
ATOM   16712 C CB  . LYS I  5 126 ? 47.885  30.532  276.691 1.00 281.04 ?  126 LYS H CB  1 
ATOM   16713 C CG  . LYS I  5 126 ? 46.633  30.657  275.841 1.00 283.72 ?  126 LYS H CG  1 
ATOM   16714 C CD  . LYS I  5 126 ? 46.981  30.711  274.363 1.00 284.53 ?  126 LYS H CD  1 
ATOM   16715 C CE  . LYS I  5 126 ? 48.090  31.718  274.088 1.00 275.95 ?  126 LYS H CE  1 
ATOM   16716 N NZ  . LYS I  5 126 ? 48.312  31.912  272.628 1.00 277.79 1  126 LYS H NZ  1 
ATOM   16717 N N   . SER I  5 127 ? 49.640  30.818  279.465 1.00 286.94 ?  127 SER H N   1 
ATOM   16718 C CA  . SER I  5 127 ? 50.914  30.467  280.080 1.00 286.34 ?  127 SER H CA  1 
ATOM   16719 C C   . SER I  5 127 ? 50.794  30.097  281.556 1.00 291.75 ?  127 SER H C   1 
ATOM   16720 O O   . SER I  5 127 ? 51.787  29.660  282.147 1.00 295.21 ?  127 SER H O   1 
ATOM   16721 C CB  . SER I  5 127 ? 51.919  31.613  279.918 1.00 282.12 ?  127 SER H CB  1 
ATOM   16722 O OG  . SER I  5 127 ? 51.613  32.690  280.785 1.00 283.68 ?  127 SER H OG  1 
ATOM   16723 N N   . GLY I  5 128 ? 49.617  30.261  282.165 1.00 276.14 ?  128 GLY H N   1 
ATOM   16724 C CA  . GLY I  5 128 ? 49.375  29.793  283.519 1.00 281.38 ?  128 GLY H CA  1 
ATOM   16725 C C   . GLY I  5 128 ? 49.250  30.852  284.598 1.00 280.58 ?  128 GLY H C   1 
ATOM   16726 O O   . GLY I  5 128 ? 49.101  30.489  285.770 1.00 286.15 ?  128 GLY H O   1 
ATOM   16727 N N   . THR I  5 129 ? 49.302  32.138  284.262 1.00 270.43 ?  129 THR H N   1 
ATOM   16728 C CA  . THR I  5 129 ? 49.117  33.196  285.246 1.00 270.95 ?  129 THR H CA  1 
ATOM   16729 C C   . THR I  5 129 ? 48.091  34.201  284.740 1.00 270.60 ?  129 THR H C   1 
ATOM   16730 O O   . THR I  5 129 ? 47.841  34.315  283.538 1.00 270.18 ?  129 THR H O   1 
ATOM   16731 C CB  . THR I  5 129 ? 50.433  33.916  285.568 1.00 267.94 ?  129 THR H CB  1 
ATOM   16732 O OG1 . THR I  5 129 ? 50.911  34.584  284.395 1.00 269.83 ?  129 THR H OG1 1 
ATOM   16733 C CG2 . THR I  5 129 ? 51.482  32.929  286.067 1.00 267.77 ?  129 THR H CG2 1 
ATOM   16734 N N   . ALA I  5 130 ? 47.493  34.932  285.681 1.00 270.85 ?  130 ALA H N   1 
ATOM   16735 C CA  . ALA I  5 130 ? 46.509  35.965  285.378 1.00 270.38 ?  130 ALA H CA  1 
ATOM   16736 C C   . ALA I  5 130 ? 46.875  37.235  286.131 1.00 269.75 ?  130 ALA H C   1 
ATOM   16737 O O   . ALA I  5 130 ? 46.954  37.226  287.364 1.00 273.63 ?  130 ALA H O   1 
ATOM   16738 C CB  . ALA I  5 130 ? 45.097  35.506  285.751 1.00 277.63 ?  130 ALA H CB  1 
ATOM   16739 N N   . SER I  5 131 ? 47.097  38.320  285.394 1.00 272.50 ?  131 SER H N   1 
ATOM   16740 C CA  . SER I  5 131 ? 47.355  39.633  285.970 1.00 270.49 ?  131 SER H CA  1 
ATOM   16741 C C   . SER I  5 131 ? 46.187  40.568  285.685 1.00 271.95 ?  131 SER H C   1 
ATOM   16742 O O   . SER I  5 131 ? 45.787  40.734  284.528 1.00 271.45 ?  131 SER H O   1 
ATOM   16743 C CB  . SER I  5 131 ? 48.653  40.226  285.417 1.00 264.71 ?  131 SER H CB  1 
ATOM   16744 O OG  . SER I  5 131 ? 49.761  39.387  285.697 1.00 264.54 ?  131 SER H OG  1 
ATOM   16745 N N   . VAL I  5 132 ? 45.654  41.180  286.740 1.00 260.55 ?  132 VAL H N   1 
ATOM   16746 C CA  . VAL I  5 132 ? 44.576  42.159  286.646 1.00 263.36 ?  132 VAL H CA  1 
ATOM   16747 C C   . VAL I  5 132 ? 45.142  43.513  287.050 1.00 261.47 ?  132 VAL H C   1 
ATOM   16748 O O   . VAL I  5 132 ? 45.749  43.644  288.120 1.00 262.06 ?  132 VAL H O   1 
ATOM   16749 C CB  . VAL I  5 132 ? 43.382  41.771  287.535 1.00 269.65 ?  132 VAL H CB  1 
ATOM   16750 C CG1 . VAL I  5 132 ? 42.147  42.561  287.137 1.00 272.65 ?  132 VAL H CG1 1 
ATOM   16751 C CG2 . VAL I  5 132 ? 43.120  40.269  287.457 1.00 273.57 ?  132 VAL H CG2 1 
ATOM   16752 N N   . VAL I  5 133 ? 44.941  44.518  286.201 1.00 257.13 ?  133 VAL H N   1 
ATOM   16753 C CA  . VAL I  5 133 ? 45.559  45.829  286.365 1.00 255.30 ?  133 VAL H CA  1 
ATOM   16754 C C   . VAL I  5 133 ? 44.479  46.869  286.632 1.00 259.04 ?  133 VAL H C   1 
ATOM   16755 O O   . VAL I  5 133 ? 43.490  46.956  285.892 1.00 261.08 ?  133 VAL H O   1 
ATOM   16756 C CB  . VAL I  5 133 ? 46.392  46.206  285.128 1.00 249.15 ?  133 VAL H CB  1 
ATOM   16757 C CG1 . VAL I  5 133 ? 46.914  47.625  285.248 1.00 247.76 ?  133 VAL H CG1 1 
ATOM   16758 C CG2 . VAL I  5 133 ? 47.539  45.224  284.942 1.00 245.69 ?  133 VAL H CG2 1 
ATOM   16759 N N   . CYS I  5 134 ? 44.677  47.658  287.686 1.00 249.15 ?  134 CYS H N   1 
ATOM   16760 C CA  . CYS I  5 134 ? 43.853  48.816  288.011 1.00 250.52 ?  134 CYS H CA  1 
ATOM   16761 C C   . CYS I  5 134 ? 44.722  50.059  287.852 1.00 248.50 ?  134 CYS H C   1 
ATOM   16762 O O   . CYS I  5 134 ? 45.782  50.161  288.480 1.00 247.05 ?  134 CYS H O   1 
ATOM   16763 C CB  . CYS I  5 134 ? 43.293  48.696  289.432 1.00 252.62 ?  134 CYS H CB  1 
ATOM   16764 S SG  . CYS I  5 134 ? 42.084  49.954  289.935 1.00 254.80 ?  134 CYS H SG  1 
ATOM   16765 N N   . LEU I  5 135 ? 44.282  50.989  287.007 1.00 257.55 ?  135 LEU H N   1 
ATOM   16766 C CA  . LEU I  5 135 ? 45.029  52.202  286.695 1.00 255.65 ?  135 LEU H CA  1 
ATOM   16767 C C   . LEU I  5 135 ? 44.343  53.417  287.302 1.00 257.00 ?  135 LEU H C   1 
ATOM   16768 O O   . LEU I  5 135 ? 43.140  53.616  287.107 1.00 258.95 ?  135 LEU H O   1 
ATOM   16769 C CB  . LEU I  5 135 ? 45.158  52.389  285.182 1.00 254.26 ?  135 LEU H CB  1 
ATOM   16770 C CG  . LEU I  5 135 ? 45.618  53.770  284.709 1.00 252.72 ?  135 LEU H CG  1 
ATOM   16771 C CD1 . LEU I  5 135 ? 47.052  54.048  285.138 1.00 250.42 ?  135 LEU H CD1 1 
ATOM   16772 C CD2 . LEU I  5 135 ? 45.468  53.901  283.205 1.00 251.87 ?  135 LEU H CD2 1 
ATOM   16773 N N   . LEU I  5 136 ? 45.113  54.223  288.030 1.00 253.70 ?  136 LEU H N   1 
ATOM   16774 C CA  . LEU I  5 136 ? 44.683  55.518  288.545 1.00 265.05 ?  136 LEU H CA  1 
ATOM   16775 C C   . LEU I  5 136 ? 45.506  56.588  287.841 1.00 260.25 ?  136 LEU H C   1 
ATOM   16776 O O   . LEU I  5 136 ? 46.730  56.638  288.007 1.00 258.95 ?  136 LEU H O   1 
ATOM   16777 C CB  . LEU I  5 136 ? 44.871  55.609  290.063 1.00 282.92 ?  136 LEU H CB  1 
ATOM   16778 C CG  . LEU I  5 136 ? 43.959  54.854  291.041 1.00 287.24 ?  136 LEU H CG  1 
ATOM   16779 C CD1 . LEU I  5 136 ? 43.981  53.343  290.834 1.00 282.34 ?  136 LEU H CD1 1 
ATOM   16780 C CD2 . LEU I  5 136 ? 44.340  55.200  292.476 1.00 298.80 ?  136 LEU H CD2 1 
ATOM   16781 N N   . ASN I  5 137 ? 44.847  57.437  287.058 1.00 269.81 ?  137 ASN H N   1 
ATOM   16782 C CA  . ASN I  5 137 ? 45.541  58.371  286.181 1.00 260.06 ?  137 ASN H CA  1 
ATOM   16783 C C   . ASN I  5 137 ? 45.389  59.813  286.653 1.00 270.66 ?  137 ASN H C   1 
ATOM   16784 O O   . ASN I  5 137 ? 44.268  60.296  286.841 1.00 276.66 ?  137 ASN H O   1 
ATOM   16785 C CB  . ASN I  5 137 ? 45.021  58.238  284.749 1.00 245.35 ?  137 ASN H CB  1 
ATOM   16786 C CG  . ASN I  5 137 ? 46.072  58.581  283.723 1.00 240.26 ?  137 ASN H CG  1 
ATOM   16787 O OD1 . ASN I  5 137 ? 47.220  58.154  283.838 1.00 236.81 ?  137 ASN H OD1 1 
ATOM   16788 N ND2 . ASN I  5 137 ? 45.695  59.363  282.721 1.00 243.66 ?  137 ASN H ND2 1 
ATOM   16789 N N   . ASN I  5 138 ? 46.528  60.494  286.821 1.00 260.36 ?  138 ASN H N   1 
ATOM   16790 C CA  . ASN I  5 138 ? 46.624  61.952  286.954 1.00 266.48 ?  138 ASN H CA  1 
ATOM   16791 C C   . ASN I  5 138 ? 45.807  62.488  288.138 1.00 288.70 ?  138 ASN H C   1 
ATOM   16792 O O   . ASN I  5 138 ? 44.818  63.201  287.968 1.00 295.42 ?  138 ASN H O   1 
ATOM   16793 C CB  . ASN I  5 138 ? 46.193  62.628  285.646 1.00 257.29 ?  138 ASN H CB  1 
ATOM   16794 C CG  . ASN I  5 138 ? 47.115  62.299  284.491 1.00 237.61 ?  138 ASN H CG  1 
ATOM   16795 O OD1 . ASN I  5 138 ? 48.160  61.676  284.675 1.00 230.83 ?  138 ASN H OD1 1 
ATOM   16796 N ND2 . ASN I  5 138 ? 46.732  62.717  283.289 1.00 236.42 ?  138 ASN H ND2 1 
ATOM   16797 N N   . PHE I  5 139 ? 46.246  62.136  289.350 1.00 272.71 ?  139 PHE H N   1 
ATOM   16798 C CA  . PHE I  5 139 ? 45.571  62.574  290.568 1.00 288.32 ?  139 PHE H CA  1 
ATOM   16799 C C   . PHE I  5 139 ? 46.514  63.334  291.502 1.00 285.68 ?  139 PHE H C   1 
ATOM   16800 O O   . PHE I  5 139 ? 47.741  63.244  291.396 1.00 273.70 ?  139 PHE H O   1 
ATOM   16801 C CB  . PHE I  5 139 ? 44.935  61.387  291.315 1.00 293.90 ?  139 PHE H CB  1 
ATOM   16802 C CG  . PHE I  5 139 ? 45.921  60.340  291.757 1.00 285.74 ?  139 PHE H CG  1 
ATOM   16803 C CD1 . PHE I  5 139 ? 46.264  59.293  290.917 1.00 278.77 ?  139 PHE H CD1 1 
ATOM   16804 C CD2 . PHE I  5 139 ? 46.481  60.385  293.025 1.00 286.13 ?  139 PHE H CD2 1 
ATOM   16805 C CE1 . PHE I  5 139 ? 47.169  58.323  291.322 1.00 270.82 ?  139 PHE H CE1 1 
ATOM   16806 C CE2 . PHE I  5 139 ? 47.384  59.418  293.438 1.00 279.53 ?  139 PHE H CE2 1 
ATOM   16807 C CZ  . PHE I  5 139 ? 47.728  58.386  292.585 1.00 271.25 ?  139 PHE H CZ  1 
ATOM   16808 N N   . TYR I  5 140 ? 45.909  64.103  292.412 1.00 276.14 ?  140 TYR H N   1 
ATOM   16809 C CA  . TYR I  5 140 ? 46.597  64.806  293.508 1.00 275.20 ?  140 TYR H CA  1 
ATOM   16810 C C   . TYR I  5 140 ? 45.643  64.984  294.697 1.00 285.82 ?  140 TYR H C   1 
ATOM   16811 O O   . TYR I  5 140 ? 44.465  65.277  294.501 1.00 292.69 ?  140 TYR H O   1 
ATOM   16812 C CB  . TYR I  5 140 ? 47.125  66.173  293.046 1.00 272.08 ?  140 TYR H CB  1 
ATOM   16813 C CG  . TYR I  5 140 ? 47.913  66.927  294.103 1.00 270.09 ?  140 TYR H CG  1 
ATOM   16814 C CD1 . TYR I  5 140 ? 47.276  67.788  294.991 1.00 280.68 ?  140 TYR H CD1 1 
ATOM   16815 C CD2 . TYR I  5 140 ? 49.288  66.765  294.223 1.00 259.00 ?  140 TYR H CD2 1 
ATOM   16816 C CE1 . TYR I  5 140 ? 47.983  68.470  295.960 1.00 278.10 ?  140 TYR H CE1 1 
ATOM   16817 C CE2 . TYR I  5 140 ? 50.005  67.446  295.192 1.00 258.03 ?  140 TYR H CE2 1 
ATOM   16818 C CZ  . TYR I  5 140 ? 49.346  68.296  296.056 1.00 267.43 ?  140 TYR H CZ  1 
ATOM   16819 O OH  . TYR I  5 140 ? 50.051  68.977  297.022 1.00 264.08 ?  140 TYR H OH  1 
ATOM   16820 N N   . PRO I  5 141 ? 46.147  64.839  295.939 1.00 274.42 ?  141 PRO H N   1 
ATOM   16821 C CA  . PRO I  5 141 ? 47.517  64.522  296.373 1.00 265.63 ?  141 PRO H CA  1 
ATOM   16822 C C   . PRO I  5 141 ? 47.925  63.057  296.217 1.00 260.11 ?  141 PRO H C   1 
ATOM   16823 O O   . PRO I  5 141 ? 47.134  62.236  295.753 1.00 263.19 ?  141 PRO H O   1 
ATOM   16824 C CB  . PRO I  5 141 ? 47.510  64.914  297.853 1.00 269.43 ?  141 PRO H CB  1 
ATOM   16825 C CG  . PRO I  5 141 ? 46.101  64.759  298.273 1.00 278.92 ?  141 PRO H CG  1 
ATOM   16826 C CD  . PRO I  5 141 ? 45.267  65.135  297.085 1.00 282.27 ?  141 PRO H CD  1 
ATOM   16827 N N   . ARG I  5 142 ? 49.161  62.749  296.625 1.00 272.33 ?  142 ARG H N   1 
ATOM   16828 C CA  . ARG I  5 142 ? 49.727  61.423  296.393 1.00 265.79 ?  142 ARG H CA  1 
ATOM   16829 C C   . ARG I  5 142 ? 48.971  60.333  297.143 1.00 272.87 ?  142 ARG H C   1 
ATOM   16830 O O   . ARG I  5 142 ? 48.922  59.188  296.681 1.00 270.28 ?  142 ARG H O   1 
ATOM   16831 C CB  . ARG I  5 142 ? 51.202  61.405  296.797 1.00 256.38 ?  142 ARG H CB  1 
ATOM   16832 C CG  . ARG I  5 142 ? 51.960  60.178  296.316 1.00 248.80 ?  142 ARG H CG  1 
ATOM   16833 C CD  . ARG I  5 142 ? 53.379  60.156  296.853 1.00 238.02 ?  142 ARG H CD  1 
ATOM   16834 N NE  . ARG I  5 142 ? 54.189  59.124  296.213 1.00 229.72 ?  142 ARG H NE  1 
ATOM   16835 C CZ  . ARG I  5 142 ? 54.253  57.861  296.623 1.00 232.44 ?  142 ARG H CZ  1 
ATOM   16836 N NH1 . ARG I  5 142 ? 53.547  57.461  297.673 1.00 243.48 1  142 ARG H NH1 1 
ATOM   16837 N NH2 . ARG I  5 142 ? 55.021  56.994  295.977 1.00 219.75 ?  142 ARG H NH2 1 
ATOM   16838 N N   . GLU I  5 143 ? 48.383  60.658  298.292 1.00 255.33 ?  143 GLU H N   1 
ATOM   16839 C CA  . GLU I  5 143 ? 47.755  59.635  299.118 1.00 261.16 ?  143 GLU H CA  1 
ATOM   16840 C C   . GLU I  5 143 ? 46.564  59.020  298.391 1.00 264.16 ?  143 GLU H C   1 
ATOM   16841 O O   . GLU I  5 143 ? 45.620  59.724  298.020 1.00 271.16 ?  143 GLU H O   1 
ATOM   16842 C CB  . GLU I  5 143 ? 47.318  60.239  300.452 1.00 270.04 ?  143 GLU H CB  1 
ATOM   16843 C CG  . GLU I  5 143 ? 46.413  59.340  301.274 1.00 280.46 ?  143 GLU H CG  1 
ATOM   16844 C CD  . GLU I  5 143 ? 47.076  58.026  301.644 1.00 278.86 ?  143 GLU H CD  1 
ATOM   16845 O OE1 . GLU I  5 143 ? 48.321  57.994  301.752 1.00 275.25 ?  143 GLU H OE1 1 
ATOM   16846 O OE2 . GLU I  5 143 ? 46.352  57.025  301.821 1.00 285.33 -1 143 GLU H OE2 1 
ATOM   16847 N N   . ALA I  5 144 ? 46.615  57.705  298.182 1.00 272.38 ?  144 ALA H N   1 
ATOM   16848 C CA  . ALA I  5 144 ? 45.536  56.979  297.526 1.00 274.72 ?  144 ALA H CA  1 
ATOM   16849 C C   . ALA I  5 144 ? 45.535  55.541  298.023 1.00 273.52 ?  144 ALA H C   1 
ATOM   16850 O O   . ALA I  5 144 ? 46.587  54.978  298.338 1.00 268.48 ?  144 ALA H O   1 
ATOM   16851 C CB  . ALA I  5 144 ? 45.674  57.027  295.999 1.00 270.08 ?  144 ALA H CB  1 
ATOM   16852 N N   . LYS I  5 145 ? 44.342  54.953  298.096 1.00 280.89 ?  145 LYS H N   1 
ATOM   16853 C CA  . LYS I  5 145 ? 44.165  53.575  298.536 1.00 279.96 ?  145 LYS H CA  1 
ATOM   16854 C C   . LYS I  5 145 ? 43.477  52.763  297.450 1.00 274.88 ?  145 LYS H C   1 
ATOM   16855 O O   . LYS I  5 145 ? 42.436  53.174  296.926 1.00 276.12 ?  145 LYS H O   1 
ATOM   16856 C CB  . LYS I  5 145 ? 43.350  53.507  299.828 1.00 287.95 ?  145 LYS H CB  1 
ATOM   16857 C CG  . LYS I  5 145 ? 43.121  52.087  300.312 1.00 291.27 ?  145 LYS H CG  1 
ATOM   16858 C CD  . LYS I  5 145 ? 42.828  52.038  301.801 1.00 300.94 ?  145 LYS H CD  1 
ATOM   16859 C CE  . LYS I  5 145 ? 41.476  52.653  302.126 1.00 307.01 ?  145 LYS H CE  1 
ATOM   16860 N NZ  . LYS I  5 145 ? 41.067  52.366  303.530 1.00 314.91 1  145 LYS H NZ  1 
ATOM   16861 N N   . VAL I  5 146 ? 44.063  51.615  297.120 1.00 290.74 ?  146 VAL H N   1 
ATOM   16862 C CA  . VAL I  5 146 ? 43.498  50.663  296.171 1.00 286.83 ?  146 VAL H CA  1 
ATOM   16863 C C   . VAL I  5 146 ? 43.299  49.336  296.893 1.00 287.47 ?  146 VAL H C   1 
ATOM   16864 O O   . VAL I  5 146 ? 44.245  48.794  297.477 1.00 291.04 ?  146 VAL H O   1 
ATOM   16865 C CB  . VAL I  5 146 ? 44.401  50.483  294.937 1.00 283.07 ?  146 VAL H CB  1 
ATOM   16866 C CG1 . VAL I  5 146 ? 43.765  49.516  293.951 1.00 275.60 ?  146 VAL H CG1 1 
ATOM   16867 C CG2 . VAL I  5 146 ? 44.674  51.828  294.274 1.00 282.42 ?  146 VAL H CG2 1 
ATOM   16868 N N   . GLN I  5 147 ? 42.072  48.822  296.856 1.00 282.83 ?  147 GLN H N   1 
ATOM   16869 C CA  . GLN I  5 147 ? 41.727  47.539  297.455 1.00 282.75 ?  147 GLN H CA  1 
ATOM   16870 C C   . GLN I  5 147 ? 41.160  46.623  296.382 1.00 274.74 ?  147 GLN H C   1 
ATOM   16871 O O   . GLN I  5 147 ? 40.301  47.040  295.597 1.00 270.66 ?  147 GLN H O   1 
ATOM   16872 C CB  . GLN I  5 147 ? 40.708  47.709  298.585 1.00 289.19 ?  147 GLN H CB  1 
ATOM   16873 C CG  . GLN I  5 147 ? 41.176  48.588  299.726 1.00 301.45 ?  147 GLN H CG  1 
ATOM   16874 C CD  . GLN I  5 147 ? 40.266  48.492  300.932 1.00 310.69 ?  147 GLN H CD  1 
ATOM   16875 O OE1 . GLN I  5 147 ? 39.793  47.411  301.280 1.00 315.90 ?  147 GLN H OE1 1 
ATOM   16876 N NE2 . GLN I  5 147 ? 40.014  49.625  301.576 1.00 320.69 ?  147 GLN H NE2 1 
ATOM   16877 N N   . TRP I  5 148 ? 41.638  45.380  296.354 1.00 281.09 ?  148 TRP H N   1 
ATOM   16878 C CA  . TRP I  5 148 ? 41.153  44.368  295.425 1.00 273.90 ?  148 TRP H CA  1 
ATOM   16879 C C   . TRP I  5 148 ? 40.086  43.509  296.087 1.00 276.63 ?  148 TRP H C   1 
ATOM   16880 O O   . TRP I  5 148 ? 40.236  43.088  297.238 1.00 284.20 ?  148 TRP H O   1 
ATOM   16881 C CB  . TRP I  5 148 ? 42.295  43.474  294.928 1.00 267.61 ?  148 TRP H CB  1 
ATOM   16882 C CG  . TRP I  5 148 ? 43.156  44.129  293.899 1.00 262.71 ?  148 TRP H CG  1 
ATOM   16883 C CD1 . TRP I  5 148 ? 44.341  44.771  294.108 1.00 265.60 ?  148 TRP H CD1 1 
ATOM   16884 C CD2 . TRP I  5 148 ? 42.887  44.228  292.494 1.00 257.38 ?  148 TRP H CD2 1 
ATOM   16885 N NE1 . TRP I  5 148 ? 44.831  45.256  292.918 1.00 258.54 ?  148 TRP H NE1 1 
ATOM   16886 C CE2 . TRP I  5 148 ? 43.956  44.937  291.912 1.00 254.80 ?  148 TRP H CE2 1 
ATOM   16887 C CE3 . TRP I  5 148 ? 41.846  43.784  291.671 1.00 258.75 ?  148 TRP H CE3 1 
ATOM   16888 C CZ2 . TRP I  5 148 ? 44.016  45.211  290.545 1.00 253.57 ?  148 TRP H CZ2 1 
ATOM   16889 C CZ3 . TRP I  5 148 ? 41.907  44.057  290.314 1.00 257.52 ?  148 TRP H CZ3 1 
ATOM   16890 C CH2 . TRP I  5 148 ? 42.984  44.764  289.765 1.00 254.96 ?  148 TRP H CH2 1 
ATOM   16891 N N   . LYS I  5 149 ? 39.009  43.250  295.349 1.00 278.39 ?  149 LYS H N   1 
ATOM   16892 C CA  . LYS I  5 149 ? 37.941  42.368  295.793 1.00 285.55 ?  149 LYS H CA  1 
ATOM   16893 C C   . LYS I  5 149 ? 37.666  41.340  294.706 1.00 283.06 ?  149 LYS H C   1 
ATOM   16894 O O   . LYS I  5 149 ? 37.447  41.701  293.544 1.00 280.13 ?  149 LYS H O   1 
ATOM   16895 C CB  . LYS I  5 149 ? 36.680  43.169  296.131 1.00 291.93 ?  149 LYS H CB  1 
ATOM   16896 C CG  . LYS I  5 149 ? 36.870  44.080  297.332 1.00 297.00 ?  149 LYS H CG  1 
ATOM   16897 C CD  . LYS I  5 149 ? 35.750  45.088  297.473 1.00 303.76 ?  149 LYS H CD  1 
ATOM   16898 C CE  . LYS I  5 149 ? 36.045  46.038  298.617 1.00 310.77 ?  149 LYS H CE  1 
ATOM   16899 N NZ  . LYS I  5 149 ? 34.958  47.033  298.816 1.00 315.50 1  149 LYS H NZ  1 
ATOM   16900 N N   . VAL I  5 150 ? 37.682  40.065  295.086 1.00 296.38 ?  150 VAL H N   1 
ATOM   16901 C CA  . VAL I  5 150 ? 37.422  38.951  294.179 1.00 295.13 ?  150 VAL H CA  1 
ATOM   16902 C C   . VAL I  5 150 ? 36.246  38.170  294.748 1.00 303.58 ?  150 VAL H C   1 
ATOM   16903 O O   . VAL I  5 150 ? 36.370  37.528  295.799 1.00 308.11 ?  150 VAL H O   1 
ATOM   16904 C CB  . VAL I  5 150 ? 38.655  38.055  294.007 1.00 292.75 ?  150 VAL H CB  1 
ATOM   16905 C CG1 . VAL I  5 150 ? 38.352  36.912  293.064 1.00 291.54 ?  150 VAL H CG1 1 
ATOM   16906 C CG2 . VAL I  5 150 ? 39.834  38.871  293.499 1.00 284.83 ?  150 VAL H CG2 1 
ATOM   16907 N N   . ASP I  5 151 ? 35.111  38.214  294.049 1.00 292.46 ?  151 ASP H N   1 
ATOM   16908 C CA  . ASP I  5 151 ? 33.843  37.697  294.562 1.00 299.40 ?  151 ASP H CA  1 
ATOM   16909 C C   . ASP I  5 151 ? 33.550  38.258  295.951 1.00 307.87 ?  151 ASP H C   1 
ATOM   16910 O O   . ASP I  5 151 ? 33.215  37.531  296.889 1.00 310.61 ?  151 ASP H O   1 
ATOM   16911 C CB  . ASP I  5 151 ? 33.820  36.168  294.568 1.00 302.32 ?  151 ASP H CB  1 
ATOM   16912 C CG  . ASP I  5 151 ? 33.568  35.587  293.195 1.00 295.56 ?  151 ASP H CG  1 
ATOM   16913 O OD1 . ASP I  5 151 ? 32.979  36.293  292.348 1.00 293.01 ?  151 ASP H OD1 1 
ATOM   16914 O OD2 . ASP I  5 151 ? 33.943  34.418  292.968 1.00 298.82 -1 151 ASP H OD2 1 
ATOM   16915 N N   . ASN I  5 152 ? 33.692  39.579  296.072 1.00 296.91 ?  152 ASN H N   1 
ATOM   16916 C CA  . ASN I  5 152 ? 33.435  40.329  297.301 1.00 303.80 ?  152 ASN H CA  1 
ATOM   16917 C C   . ASN I  5 152 ? 34.316  39.885  298.468 1.00 307.95 ?  152 ASN H C   1 
ATOM   16918 O O   . ASN I  5 152 ? 33.965  40.113  299.631 1.00 318.62 ?  152 ASN H O   1 
ATOM   16919 C CB  . ASN I  5 152 ? 31.955  40.250  297.693 1.00 313.50 ?  152 ASN H CB  1 
ATOM   16920 C CG  . ASN I  5 152 ? 31.066  41.071  296.777 1.00 313.05 ?  152 ASN H CG  1 
ATOM   16921 O OD1 . ASN I  5 152 ? 31.088  42.302  296.806 1.00 316.11 ?  152 ASN H OD1 1 
ATOM   16922 N ND2 . ASN I  5 152 ? 30.289  40.389  295.943 1.00 315.33 ?  152 ASN H ND2 1 
ATOM   16923 N N   . ALA I  5 153 ? 35.451  39.248  298.188 1.00 292.04 ?  153 ALA H N   1 
ATOM   16924 C CA  . ALA I  5 153 ? 36.435  38.896  299.205 1.00 296.85 ?  153 ALA H CA  1 
ATOM   16925 C C   . ALA I  5 153 ? 37.641  39.814  299.055 1.00 291.02 ?  153 ALA H C   1 
ATOM   16926 O O   . ALA I  5 153 ? 38.263  39.858  297.987 1.00 285.22 ?  153 ALA H O   1 
ATOM   16927 C CB  . ALA I  5 153 ? 36.852  37.430  299.089 1.00 295.74 ?  153 ALA H CB  1 
ATOM   16928 N N   . LEU I  5 154 ? 37.970  40.537  300.124 1.00 303.93 ?  154 LEU H N   1 
ATOM   16929 C CA  . LEU I  5 154 ? 39.093  41.464  300.095 1.00 298.74 ?  154 LEU H CA  1 
ATOM   16930 C C   . LEU I  5 154 ? 40.408  40.700  299.990 1.00 296.62 ?  154 LEU H C   1 
ATOM   16931 O O   . LEU I  5 154 ? 40.632  39.721  300.709 1.00 300.36 ?  154 LEU H O   1 
ATOM   16932 C CB  . LEU I  5 154 ? 39.081  42.348  301.341 1.00 304.54 ?  154 LEU H CB  1 
ATOM   16933 C CG  . LEU I  5 154 ? 40.154  43.438  301.408 1.00 305.85 ?  154 LEU H CG  1 
ATOM   16934 C CD1 . LEU I  5 154 ? 40.065  44.356  300.196 1.00 299.31 ?  154 LEU H CD1 1 
ATOM   16935 C CD2 . LEU I  5 154 ? 40.034  44.234  302.698 1.00 312.40 ?  154 LEU H CD2 1 
ATOM   16936 N N   . GLN I  5 155 ? 41.273  41.147  299.085 1.00 292.24 ?  155 GLN H N   1 
ATOM   16937 C CA  . GLN I  5 155 ? 42.544  40.489  298.817 1.00 288.54 ?  155 GLN H CA  1 
ATOM   16938 C C   . GLN I  5 155 ? 43.680  41.176  299.563 1.00 288.57 ?  155 GLN H C   1 
ATOM   16939 O O   . GLN I  5 155 ? 43.689  42.401  299.717 1.00 288.30 ?  155 GLN H O   1 
ATOM   16940 C CB  . GLN I  5 155 ? 42.836  40.483  297.316 1.00 281.45 ?  155 GLN H CB  1 
ATOM   16941 C CG  . GLN I  5 155 ? 41.709  39.892  296.492 1.00 281.13 ?  155 GLN H CG  1 
ATOM   16942 C CD  . GLN I  5 155 ? 41.518  38.412  296.749 1.00 283.84 ?  155 GLN H CD  1 
ATOM   16943 O OE1 . GLN I  5 155 ? 42.357  37.592  296.379 1.00 281.14 ?  155 GLN H OE1 1 
ATOM   16944 N NE2 . GLN I  5 155 ? 40.409  38.061  297.393 1.00 290.01 ?  155 GLN H NE2 1 
ATOM   16945 N N   . SER I  5 156 ? 44.639  40.373  300.023 1.00 268.74 ?  156 SER H N   1 
ATOM   16946 C CA  . SER I  5 156 ? 45.863  40.872  300.633 1.00 269.03 ?  156 SER H CA  1 
ATOM   16947 C C   . SER I  5 156 ? 47.035  40.000  300.210 1.00 265.47 ?  156 SER H C   1 
ATOM   16948 O O   . SER I  5 156 ? 46.900  38.778  300.095 1.00 267.09 ?  156 SER H O   1 
ATOM   16949 C CB  . SER I  5 156 ? 45.760  40.897  302.165 1.00 278.25 ?  156 SER H CB  1 
ATOM   16950 O OG  . SER I  5 156 ? 44.573  41.540  302.593 1.00 287.11 ?  156 SER H OG  1 
ATOM   16951 N N   . GLY I  5 157 ? 48.187  40.635  299.988 1.00 266.52 ?  157 GLY H N   1 
ATOM   16952 C CA  . GLY I  5 157 ? 49.425  39.933  299.727 1.00 263.47 ?  157 GLY H CA  1 
ATOM   16953 C C   . GLY I  5 157 ? 49.676  39.531  298.288 1.00 257.43 ?  157 GLY H C   1 
ATOM   16954 O O   . GLY I  5 157 ? 50.813  39.170  297.958 1.00 254.88 ?  157 GLY H O   1 
ATOM   16955 N N   . ASN I  5 158 ? 48.664  39.565  297.423 1.00 260.90 ?  158 ASN H N   1 
ATOM   16956 C CA  . ASN I  5 158 ? 48.833  39.166  296.032 1.00 255.44 ?  158 ASN H CA  1 
ATOM   16957 C C   . ASN I  5 158 ? 48.877  40.346  295.065 1.00 250.38 ?  158 ASN H C   1 
ATOM   16958 O O   . ASN I  5 158 ? 48.799  40.133  293.851 1.00 246.14 ?  158 ASN H O   1 
ATOM   16959 C CB  . ASN I  5 158 ? 47.720  38.202  295.616 1.00 257.07 ?  158 ASN H CB  1 
ATOM   16960 C CG  . ASN I  5 158 ? 46.338  38.705  295.985 1.00 260.77 ?  158 ASN H CG  1 
ATOM   16961 O OD1 . ASN I  5 158 ? 46.163  39.856  296.385 1.00 261.61 ?  158 ASN H OD1 1 
ATOM   16962 N ND2 . ASN I  5 158 ? 45.340  37.842  295.833 1.00 263.24 ?  158 ASN H ND2 1 
ATOM   16963 N N   . SER I  5 159 ? 48.999  41.576  295.564 1.00 245.73 ?  159 SER H N   1 
ATOM   16964 C CA  . SER I  5 159 ? 49.049  42.756  294.714 1.00 241.40 ?  159 SER H CA  1 
ATOM   16965 C C   . SER I  5 159 ? 50.309  43.567  294.985 1.00 239.12 ?  159 SER H C   1 
ATOM   16966 O O   . SER I  5 159 ? 50.861  43.543  296.089 1.00 242.02 ?  159 SER H O   1 
ATOM   16967 C CB  . SER I  5 159 ? 47.810  43.646  294.920 1.00 244.15 ?  159 SER H CB  1 
ATOM   16968 O OG  . SER I  5 159 ? 47.750  44.160  296.240 1.00 248.89 ?  159 SER H OG  1 
ATOM   16969 N N   . GLN I  5 160 ? 50.758  44.289  293.958 1.00 232.28 ?  160 GLN H N   1 
ATOM   16970 C CA  . GLN I  5 160 ? 51.882  45.208  294.060 1.00 229.86 ?  160 GLN H CA  1 
ATOM   16971 C C   . GLN I  5 160 ? 51.511  46.528  293.400 1.00 227.90 ?  160 GLN H C   1 
ATOM   16972 O O   . GLN I  5 160 ? 50.802  46.548  292.390 1.00 225.92 ?  160 GLN H O   1 
ATOM   16973 C CB  . GLN I  5 160 ? 53.138  44.624  293.408 1.00 225.48 ?  160 GLN H CB  1 
ATOM   16974 C CG  . GLN I  5 160 ? 53.737  43.459  294.173 1.00 227.71 ?  160 GLN H CG  1 
ATOM   16975 C CD  . GLN I  5 160 ? 55.050  42.991  293.585 1.00 223.67 ?  160 GLN H CD  1 
ATOM   16976 O OE1 . GLN I  5 160 ? 55.083  42.370  292.522 1.00 220.74 ?  160 GLN H OE1 1 
ATOM   16977 N NE2 . GLN I  5 160 ? 56.143  43.291  294.274 1.00 223.69 ?  160 GLN H NE2 1 
ATOM   16978 N N   . GLU I  5 161 ? 51.992  47.627  293.974 1.00 235.64 ?  161 GLU H N   1 
ATOM   16979 C CA  . GLU I  5 161 ? 51.749  48.963  293.452 1.00 234.23 ?  161 GLU H CA  1 
ATOM   16980 C C   . GLU I  5 161 ? 53.027  49.555  292.871 1.00 229.59 ?  161 GLU H C   1 
ATOM   16981 O O   . GLU I  5 161 ? 54.134  49.267  293.333 1.00 228.64 ?  161 GLU H O   1 
ATOM   16982 C CB  . GLU I  5 161 ? 51.211  49.893  294.544 1.00 239.01 ?  161 GLU H CB  1 
ATOM   16983 C CG  . GLU I  5 161 ? 49.801  49.578  295.010 1.00 243.89 ?  161 GLU H CG  1 
ATOM   16984 C CD  . GLU I  5 161 ? 49.270  50.620  295.975 1.00 248.56 ?  161 GLU H CD  1 
ATOM   16985 O OE1 . GLU I  5 161 ? 50.050  51.510  296.376 1.00 248.15 ?  161 GLU H OE1 1 
ATOM   16986 O OE2 . GLU I  5 161 ? 48.076  50.550  296.335 1.00 252.77 -1 161 GLU H OE2 1 
ATOM   16987 N N   . SER I  5 162 ? 52.855  50.383  291.843 1.00 229.90 ?  162 SER H N   1 
ATOM   16988 C CA  . SER I  5 162 ? 53.920  51.212  291.298 1.00 229.35 ?  162 SER H CA  1 
ATOM   16989 C C   . SER I  5 162 ? 53.362  52.610  291.080 1.00 229.87 ?  162 SER H C   1 
ATOM   16990 O O   . SER I  5 162 ? 52.268  52.763  290.526 1.00 229.55 ?  162 SER H O   1 
ATOM   16991 C CB  . SER I  5 162 ? 54.463  50.633  289.990 1.00 227.42 ?  162 SER H CB  1 
ATOM   16992 O OG  . SER I  5 162 ? 55.553  51.400  289.518 1.00 226.99 ?  162 SER H OG  1 
ATOM   16993 N N   . VAL I  5 163 ? 54.106  53.624  291.519 1.00 237.58 ?  163 VAL H N   1 
ATOM   16994 C CA  . VAL I  5 163 ? 53.681  55.015  291.431 1.00 238.99 ?  163 VAL H CA  1 
ATOM   16995 C C   . VAL I  5 163 ? 54.708  55.807  290.635 1.00 235.13 ?  163 VAL H C   1 
ATOM   16996 O O   . VAL I  5 163 ? 55.919  55.612  290.793 1.00 232.63 ?  163 VAL H O   1 
ATOM   16997 C CB  . VAL I  5 163 ? 53.481  55.638  292.830 1.00 243.71 ?  163 VAL H CB  1 
ATOM   16998 C CG1 . VAL I  5 163 ? 52.869  57.030  292.720 1.00 245.92 ?  163 VAL H CG1 1 
ATOM   16999 C CG2 . VAL I  5 163 ? 52.619  54.736  293.715 1.00 247.78 ?  163 VAL H CG2 1 
ATOM   17000 N N   . THR I  5 164 ? 54.218  56.697  289.777 1.00 245.37 ?  164 THR H N   1 
ATOM   17001 C CA  . THR I  5 164 ? 55.080  57.588  289.023 1.00 242.34 ?  164 THR H CA  1 
ATOM   17002 C C   . THR I  5 164 ? 55.565  58.734  289.905 1.00 244.36 ?  164 THR H C   1 
ATOM   17003 O O   . THR I  5 164 ? 54.936  59.102  290.902 1.00 248.71 ?  164 THR H O   1 
ATOM   17004 C CB  . THR I  5 164 ? 54.344  58.151  287.801 1.00 241.78 ?  164 THR H CB  1 
ATOM   17005 O OG1 . THR I  5 164 ? 53.178  58.871  288.223 1.00 246.29 ?  164 THR H OG1 1 
ATOM   17006 C CG2 . THR I  5 164 ? 53.916  57.027  286.873 1.00 239.49 ?  164 THR H CG2 1 
ATOM   17007 N N   . GLU I  5 165 ? 56.705  59.299  289.523 1.00 245.37 ?  165 GLU H N   1 
ATOM   17008 C CA  . GLU I  5 165 ? 57.132  60.566  290.091 1.00 246.96 ?  165 GLU H CA  1 
ATOM   17009 C C   . GLU I  5 165 ? 56.171  61.669  289.672 1.00 249.76 ?  165 GLU H C   1 
ATOM   17010 O O   . GLU I  5 165 ? 55.483  61.569  288.651 1.00 249.07 ?  165 GLU H O   1 
ATOM   17011 C CB  . GLU I  5 165 ? 58.551  60.909  289.640 1.00 242.93 ?  165 GLU H CB  1 
ATOM   17012 C CG  . GLU I  5 165 ? 59.635  60.009  290.208 1.00 240.56 ?  165 GLU H CG  1 
ATOM   17013 C CD  . GLU I  5 165 ? 59.765  60.118  291.722 1.00 243.94 ?  165 GLU H CD  1 
ATOM   17014 O OE1 . GLU I  5 165 ? 59.821  61.253  292.243 1.00 246.32 ?  165 GLU H OE1 1 
ATOM   17015 O OE2 . GLU I  5 165 ? 59.839  59.066  292.391 1.00 248.61 -1 165 GLU H OE2 1 
ATOM   17016 N N   . GLN I  5 166 ? 56.103  62.714  290.494 1.00 246.00 ?  166 GLN H N   1 
ATOM   17017 C CA  . GLN I  5 166 ? 55.261  63.863  290.186 1.00 249.23 ?  166 GLN H CA  1 
ATOM   17018 C C   . GLN I  5 166 ? 55.573  64.384  288.789 1.00 246.30 ?  166 GLN H C   1 
ATOM   17019 O O   . GLN I  5 166 ? 56.728  64.671  288.462 1.00 243.51 ?  166 GLN H O   1 
ATOM   17020 C CB  . GLN I  5 166 ? 55.481  64.961  291.230 1.00 252.93 ?  166 GLN H CB  1 
ATOM   17021 C CG  . GLN I  5 166 ? 54.522  66.139  291.130 1.00 257.32 ?  166 GLN H CG  1 
ATOM   17022 C CD  . GLN I  5 166 ? 54.607  67.065  292.334 1.00 261.92 ?  166 GLN H CD  1 
ATOM   17023 O OE1 . GLN I  5 166 ? 55.689  67.299  292.873 1.00 260.79 ?  166 GLN H OE1 1 
ATOM   17024 N NE2 . GLN I  5 166 ? 53.465  67.594  292.761 1.00 266.97 ?  166 GLN H NE2 1 
ATOM   17025 N N   . ASP I  5 167 ? 54.534  64.501  287.964 1.00 244.60 ?  167 ASP H N   1 
ATOM   17026 C CA  . ASP I  5 167 ? 54.728  64.905  286.578 1.00 243.44 ?  167 ASP H CA  1 
ATOM   17027 C C   . ASP I  5 167 ? 55.267  66.330  286.515 1.00 244.77 ?  167 ASP H C   1 
ATOM   17028 O O   . ASP I  5 167 ? 54.783  67.222  287.217 1.00 248.60 ?  167 ASP H O   1 
ATOM   17029 C CB  . ASP I  5 167 ? 53.416  64.783  285.806 1.00 245.20 ?  167 ASP H CB  1 
ATOM   17030 C CG  . ASP I  5 167 ? 53.607  64.921  284.309 1.00 244.24 ?  167 ASP H CG  1 
ATOM   17031 O OD1 . ASP I  5 167 ? 54.180  63.995  283.696 1.00 241.36 ?  167 ASP H OD1 1 
ATOM   17032 O OD2 . ASP I  5 167 ? 53.184  65.950  283.745 1.00 246.03 -1 167 ASP H OD2 1 
ATOM   17033 N N   . SER I  5 168 ? 56.286  66.538  285.677 1.00 244.54 ?  168 SER H N   1 
ATOM   17034 C CA  . SER I  5 168 ? 56.962  67.832  285.632 1.00 245.47 ?  168 SER H CA  1 
ATOM   17035 C C   . SER I  5 168 ? 56.050  68.958  285.152 1.00 249.60 ?  168 SER H C   1 
ATOM   17036 O O   . SER I  5 168 ? 56.243  70.114  285.543 1.00 253.54 ?  168 SER H O   1 
ATOM   17037 C CB  . SER I  5 168 ? 58.202  67.739  284.744 1.00 241.51 ?  168 SER H CB  1 
ATOM   17038 O OG  . SER I  5 168 ? 57.838  67.583  283.384 1.00 241.47 ?  168 SER H OG  1 
ATOM   17039 N N   . LYS I  5 169 ? 55.053  68.653  284.321 1.00 231.77 ?  169 LYS H N   1 
ATOM   17040 C CA  . LYS I  5 169 ? 54.203  69.699  283.756 1.00 236.65 ?  169 LYS H CA  1 
ATOM   17041 C C   . LYS I  5 169 ? 52.969  69.975  284.612 1.00 241.55 ?  169 LYS H C   1 
ATOM   17042 O O   . LYS I  5 169 ? 52.774  71.098  285.087 1.00 246.47 ?  169 LYS H O   1 
ATOM   17043 C CB  . LYS I  5 169 ? 53.767  69.322  282.339 1.00 237.23 ?  169 LYS H CB  1 
ATOM   17044 C CG  . LYS I  5 169 ? 54.867  69.328  281.299 1.00 233.23 ?  169 LYS H CG  1 
ATOM   17045 C CD  . LYS I  5 169 ? 54.263  69.493  279.911 1.00 236.34 ?  169 LYS H CD  1 
ATOM   17046 C CE  . LYS I  5 169 ? 52.945  68.729  279.789 1.00 240.51 ?  169 LYS H CE  1 
ATOM   17047 N NZ  . LYS I  5 169 ? 52.488  68.571  278.381 1.00 237.41 1  169 LYS H NZ  1 
ATOM   17048 N N   . ASP I  5 170 ? 52.128  68.960  284.812 1.00 254.88 ?  170 ASP H N   1 
ATOM   17049 C CA  . ASP I  5 170 ? 50.835  69.133  285.461 1.00 260.02 ?  170 ASP H CA  1 
ATOM   17050 C C   . ASP I  5 170 ? 50.850  68.785  286.943 1.00 261.85 ?  170 ASP H C   1 
ATOM   17051 O O   . ASP I  5 170 ? 49.813  68.904  287.602 1.00 266.43 ?  170 ASP H O   1 
ATOM   17052 C CB  . ASP I  5 170 ? 49.762  68.307  284.726 1.00 259.59 ?  170 ASP H CB  1 
ATOM   17053 C CG  . ASP I  5 170 ? 50.012  66.794  284.780 1.00 257.09 ?  170 ASP H CG  1 
ATOM   17054 O OD1 . ASP I  5 170 ? 50.591  66.276  285.760 1.00 254.68 ?  170 ASP H OD1 1 
ATOM   17055 O OD2 . ASP I  5 170 ? 49.621  66.111  283.811 1.00 256.87 -1 170 ASP H OD2 1 
ATOM   17056 N N   . SER I  5 171 ? 51.992  68.346  287.474 1.00 255.93 ?  171 SER H N   1 
ATOM   17057 C CA  . SER I  5 171 ? 52.188  68.090  288.902 1.00 257.60 ?  171 SER H CA  1 
ATOM   17058 C C   . SER I  5 171 ? 51.294  66.975  289.440 1.00 258.78 ?  171 SER H C   1 
ATOM   17059 O O   . SER I  5 171 ? 50.987  66.953  290.637 1.00 262.44 ?  171 SER H O   1 
ATOM   17060 C CB  . SER I  5 171 ? 51.985  69.366  289.729 1.00 262.91 ?  171 SER H CB  1 
ATOM   17061 O OG  . SER I  5 171 ? 52.917  70.370  289.364 1.00 262.11 ?  171 SER H OG  1 
ATOM   17062 N N   . THR I  5 172 ? 50.852  66.051  288.590 1.00 251.35 ?  172 THR H N   1 
ATOM   17063 C CA  . THR I  5 172 ? 50.060  64.916  289.043 1.00 252.23 ?  172 THR H CA  1 
ATOM   17064 C C   . THR I  5 172 ? 50.918  63.659  289.178 1.00 247.83 ?  172 THR H C   1 
ATOM   17065 O O   . THR I  5 172 ? 52.061  63.590  288.720 1.00 243.59 ?  172 THR H O   1 
ATOM   17066 C CB  . THR I  5 172 ? 48.889  64.653  288.086 1.00 252.93 ?  172 THR H CB  1 
ATOM   17067 O OG1 . THR I  5 172 ? 49.385  64.335  286.778 1.00 248.18 ?  172 THR H OG1 1 
ATOM   17068 C CG2 . THR I  5 172 ? 47.995  65.878  287.995 1.00 257.88 ?  172 THR H CG2 1 
ATOM   17069 N N   . TYR I  5 173 ? 50.325  62.648  289.804 1.00 250.28 ?  173 TYR H N   1 
ATOM   17070 C CA  . TYR I  5 173 ? 50.895  61.319  289.943 1.00 246.98 ?  173 TYR H CA  1 
ATOM   17071 C C   . TYR I  5 173 ? 49.990  60.337  289.216 1.00 246.14 ?  173 TYR H C   1 
ATOM   17072 O O   . TYR I  5 173 ? 48.811  60.611  288.977 1.00 249.00 ?  173 TYR H O   1 
ATOM   17073 C CB  . TYR I  5 173 ? 51.013  60.871  291.412 1.00 249.71 ?  173 TYR H CB  1 
ATOM   17074 C CG  . TYR I  5 173 ? 51.869  61.702  292.350 1.00 251.09 ?  173 TYR H CG  1 
ATOM   17075 C CD1 . TYR I  5 173 ? 51.328  62.770  293.059 1.00 256.09 ?  173 TYR H CD1 1 
ATOM   17076 C CD2 . TYR I  5 173 ? 53.199  61.371  292.585 1.00 247.69 ?  173 TYR H CD2 1 
ATOM   17077 C CE1 . TYR I  5 173 ? 52.100  63.511  293.942 1.00 257.54 ?  173 TYR H CE1 1 
ATOM   17078 C CE2 . TYR I  5 173 ? 53.978  62.106  293.466 1.00 249.01 ?  173 TYR H CE2 1 
ATOM   17079 C CZ  . TYR I  5 173 ? 53.422  63.174  294.141 1.00 253.90 ?  173 TYR H CZ  1 
ATOM   17080 O OH  . TYR I  5 173 ? 54.185  63.911  295.019 1.00 255.41 ?  173 TYR H OH  1 
ATOM   17081 N N   . SER I  5 174 ? 50.550  59.187  288.862 1.00 247.33 ?  174 SER H N   1 
ATOM   17082 C CA  . SER I  5 174 ? 49.758  58.059  288.401 1.00 246.84 ?  174 SER H CA  1 
ATOM   17083 C C   . SER I  5 174 ? 50.184  56.809  289.157 1.00 246.21 ?  174 SER H C   1 
ATOM   17084 O O   . SER I  5 174 ? 51.327  56.697  289.607 1.00 244.51 ?  174 SER H O   1 
ATOM   17085 C CB  . SER I  5 174 ? 49.896  57.849  286.889 1.00 242.73 ?  174 SER H CB  1 
ATOM   17086 O OG  . SER I  5 174 ? 49.327  58.934  286.175 1.00 244.10 ?  174 SER H OG  1 
ATOM   17087 N N   . LEU I  5 175 ? 49.255  55.863  289.284 1.00 248.98 ?  175 LEU H N   1 
ATOM   17088 C CA  . LEU I  5 175 ? 49.479  54.670  290.084 1.00 250.32 ?  175 LEU H CA  1 
ATOM   17089 C C   . LEU I  5 175 ? 48.894  53.460  289.373 1.00 248.50 ?  175 LEU H C   1 
ATOM   17090 O O   . LEU I  5 175 ? 47.769  53.504  288.867 1.00 246.76 ?  175 LEU H O   1 
ATOM   17091 C CB  . LEU I  5 175 ? 48.860  54.817  291.487 1.00 252.21 ?  175 LEU H CB  1 
ATOM   17092 C CG  . LEU I  5 175 ? 48.986  53.695  292.526 1.00 253.90 ?  175 LEU H CG  1 
ATOM   17093 C CD1 . LEU I  5 175 ? 48.897  54.288  293.923 1.00 256.31 ?  175 LEU H CD1 1 
ATOM   17094 C CD2 . LEU I  5 175 ? 47.920  52.613  292.358 1.00 252.64 ?  175 LEU H CD2 1 
ATOM   17095 N N   . SER I  5 176 ? 49.667  52.382  289.343 1.00 240.08 ?  176 SER H N   1 
ATOM   17096 C CA  . SER I  5 176 ? 49.201  51.090  288.873 1.00 238.89 ?  176 SER H CA  1 
ATOM   17097 C C   . SER I  5 176 ? 49.212  50.115  290.039 1.00 242.76 ?  176 SER H C   1 
ATOM   17098 O O   . SER I  5 176 ? 50.164  50.085  290.825 1.00 244.34 ?  176 SER H O   1 
ATOM   17099 C CB  . SER I  5 176 ? 50.077  50.563  287.734 1.00 234.30 ?  176 SER H CB  1 
ATOM   17100 O OG  . SER I  5 176 ? 51.353  50.180  288.217 1.00 234.56 ?  176 SER H OG  1 
ATOM   17101 N N   . SER I  5 177 ? 48.149  49.328  290.153 1.00 225.45 ?  177 SER H N   1 
ATOM   17102 C CA  . SER I  5 177 ? 48.084  48.227  291.101 1.00 226.91 ?  177 SER H CA  1 
ATOM   17103 C C   . SER I  5 177 ? 47.863  46.948  290.312 1.00 225.42 ?  177 SER H C   1 
ATOM   17104 O O   . SER I  5 177 ? 46.931  46.865  289.505 1.00 223.40 ?  177 SER H O   1 
ATOM   17105 C CB  . SER I  5 177 ? 46.967  48.441  292.129 1.00 227.78 ?  177 SER H CB  1 
ATOM   17106 O OG  . SER I  5 177 ? 46.971  47.427  293.120 1.00 229.40 ?  177 SER H OG  1 
ATOM   17107 N N   . THR I  5 178 ? 48.718  45.957  290.546 1.00 225.62 ?  178 THR H N   1 
ATOM   17108 C CA  . THR I  5 178 ? 48.732  44.729  289.764 1.00 224.40 ?  178 THR H CA  1 
ATOM   17109 C C   . THR I  5 178 ? 48.422  43.545  290.667 1.00 225.66 ?  178 THR H C   1 
ATOM   17110 O O   . THR I  5 178 ? 49.178  43.256  291.601 1.00 227.75 ?  178 THR H O   1 
ATOM   17111 C CB  . THR I  5 178 ? 50.087  44.535  289.078 1.00 224.37 ?  178 THR H CB  1 
ATOM   17112 O OG1 . THR I  5 178 ? 50.423  45.711  288.328 1.00 223.42 ?  178 THR H OG1 1 
ATOM   17113 C CG2 . THR I  5 178 ? 50.035  43.351  288.145 1.00 222.93 ?  178 THR H CG2 1 
ATOM   17114 N N   . LEU I  5 179 ? 47.318  42.863  290.375 1.00 247.66 ?  179 LEU H N   1 
ATOM   17115 C CA  . LEU I  5 179 ? 46.887  41.678  291.104 1.00 251.66 ?  179 LEU H CA  1 
ATOM   17116 C C   . LEU I  5 179 ? 47.334  40.458  290.310 1.00 249.62 ?  179 LEU H C   1 
ATOM   17117 O O   . LEU I  5 179 ? 46.987  40.322  289.132 1.00 245.94 ?  179 LEU H O   1 
ATOM   17118 C CB  . LEU I  5 179 ? 45.368  41.686  291.292 1.00 253.73 ?  179 LEU H CB  1 
ATOM   17119 C CG  . LEU I  5 179 ? 44.681  40.455  291.883 1.00 257.75 ?  179 LEU H CG  1 
ATOM   17120 C CD1 . LEU I  5 179 ? 44.972  40.348  293.369 1.00 264.60 ?  179 LEU H CD1 1 
ATOM   17121 C CD2 . LEU I  5 179 ? 43.183  40.498  291.626 1.00 258.05 ?  179 LEU H CD2 1 
ATOM   17122 N N   . THR I  5 180 ? 48.097  39.576  290.949 1.00 250.30 ?  180 THR H N   1 
ATOM   17123 C CA  . THR I  5 180 ? 48.660  38.409  290.280 1.00 249.39 ?  180 THR H CA  1 
ATOM   17124 C C   . THR I  5 180 ? 48.093  37.140  290.898 1.00 253.11 ?  180 THR H C   1 
ATOM   17125 O O   . THR I  5 180 ? 48.231  36.914  292.106 1.00 259.76 ?  180 THR H O   1 
ATOM   17126 C CB  . THR I  5 180 ? 50.186  38.404  290.361 1.00 249.67 ?  180 THR H CB  1 
ATOM   17127 O OG1 . THR I  5 180 ? 50.693  39.669  289.916 1.00 249.72 ?  180 THR H OG1 1 
ATOM   17128 C CG2 . THR I  5 180 ? 50.751  37.299  289.488 1.00 248.63 ?  180 THR H CG2 1 
ATOM   17129 N N   . LEU I  5 181 ? 47.457  36.323  290.062 1.00 261.79 ?  181 LEU H N   1 
ATOM   17130 C CA  . LEU I  5 181 ? 46.885  35.046  290.450 1.00 265.50 ?  181 LEU H CA  1 
ATOM   17131 C C   . LEU I  5 181 ? 47.315  33.986  289.446 1.00 263.22 ?  181 LEU H C   1 
ATOM   17132 O O   . LEU I  5 181 ? 47.640  34.289  288.294 1.00 258.26 ?  181 LEU H O   1 
ATOM   17133 C CB  . LEU I  5 181 ? 45.351  35.105  290.507 1.00 266.38 ?  181 LEU H CB  1 
ATOM   17134 C CG  . LEU I  5 181 ? 44.680  36.193  291.350 1.00 270.61 ?  181 LEU H CG  1 
ATOM   17135 C CD1 . LEU I  5 181 ? 43.233  36.385  290.923 1.00 272.97 ?  181 LEU H CD1 1 
ATOM   17136 C CD2 . LEU I  5 181 ? 44.754  35.865  292.831 1.00 279.03 ?  181 LEU H CD2 1 
ATOM   17137 N N   . SER I  5 182 ? 47.328  32.734  289.897 1.00 285.76 ?  182 SER H N   1 
ATOM   17138 C CA  . SER I  5 182 ? 47.452  31.625  288.965 1.00 285.89 ?  182 SER H CA  1 
ATOM   17139 C C   . SER I  5 182 ? 46.171  31.485  288.144 1.00 281.99 ?  182 SER H C   1 
ATOM   17140 O O   . SER I  5 182 ? 45.101  31.974  288.518 1.00 283.23 ?  182 SER H O   1 
ATOM   17141 C CB  . SER I  5 182 ? 47.766  30.321  289.700 1.00 292.49 ?  182 SER H CB  1 
ATOM   17142 O OG  . SER I  5 182 ? 46.701  29.921  290.543 1.00 297.36 ?  182 SER H OG  1 
ATOM   17143 N N   . LYS I  5 183 ? 46.299  30.816  286.995 1.00 280.15 ?  183 LYS H N   1 
ATOM   17144 C CA  . LYS I  5 183 ? 45.144  30.602  286.127 1.00 277.87 ?  183 LYS H CA  1 
ATOM   17145 C C   . LYS I  5 183 ? 44.032  29.843  286.841 1.00 283.77 ?  183 LYS H C   1 
ATOM   17146 O O   . LYS I  5 183 ? 42.851  30.185  286.702 1.00 282.40 ?  183 LYS H O   1 
ATOM   17147 C CB  . LYS I  5 183 ? 45.563  29.857  284.862 1.00 276.89 ?  183 LYS H CB  1 
ATOM   17148 C CG  . LYS I  5 183 ? 44.417  29.630  283.885 1.00 273.05 ?  183 LYS H CG  1 
ATOM   17149 C CD  . LYS I  5 183 ? 44.855  28.766  282.711 1.00 273.91 ?  183 LYS H CD  1 
ATOM   17150 C CE  . LYS I  5 183 ? 43.906  28.889  281.526 1.00 274.29 ?  183 LYS H CE  1 
ATOM   17151 N NZ  . LYS I  5 183 ? 42.534  28.442  281.881 1.00 280.08 1  183 LYS H NZ  1 
ATOM   17152 N N   . ALA I  5 184 ? 44.388  28.796  287.592 1.00 290.72 ?  184 ALA H N   1 
ATOM   17153 C CA  . ALA I  5 184 ? 43.391  28.010  288.316 1.00 296.68 ?  184 ALA H CA  1 
ATOM   17154 C C   . ALA I  5 184 ? 42.583  28.883  289.269 1.00 300.03 ?  184 ALA H C   1 
ATOM   17155 O O   . ALA I  5 184 ? 41.347  28.857  289.257 1.00 301.64 ?  184 ALA H O   1 
ATOM   17156 C CB  . ALA I  5 184 ? 44.074  26.869  289.070 1.00 301.37 ?  184 ALA H CB  1 
ATOM   17157 N N   . ASP I  5 185 ? 43.269  29.660  290.111 1.00 302.45 ?  185 ASP H N   1 
ATOM   17158 C CA  . ASP I  5 185 ? 42.572  30.540  291.043 1.00 306.46 ?  185 ASP H CA  1 
ATOM   17159 C C   . ASP I  5 185 ? 41.759  31.597  290.304 1.00 301.96 ?  185 ASP H C   1 
ATOM   17160 O O   . ASP I  5 185 ? 40.672  31.980  290.752 1.00 303.85 ?  185 ASP H O   1 
ATOM   17161 C CB  . ASP I  5 185 ? 43.572  31.195  291.999 1.00 307.84 ?  185 ASP H CB  1 
ATOM   17162 C CG  . ASP I  5 185 ? 43.963  30.285  293.151 1.00 318.39 ?  185 ASP H CG  1 
ATOM   17163 O OD1 . ASP I  5 185 ? 43.281  29.261  293.365 1.00 325.16 ?  185 ASP H OD1 1 
ATOM   17164 O OD2 . ASP I  5 185 ? 44.950  30.601  293.850 1.00 320.09 -1 185 ASP H OD2 1 
ATOM   17165 N N   . TYR I  5 186 ? 42.282  32.098  289.179 1.00 294.92 ?  186 TYR H N   1 
ATOM   17166 C CA  . TYR I  5 186 ? 41.563  33.107  288.404 1.00 291.38 ?  186 TYR H CA  1 
ATOM   17167 C C   . TYR I  5 186 ? 40.212  32.582  287.929 1.00 294.36 ?  186 TYR H C   1 
ATOM   17168 O O   . TYR I  5 186 ? 39.190  33.270  288.038 1.00 293.02 ?  186 TYR H O   1 
ATOM   17169 C CB  . TYR I  5 186 ? 42.410  33.558  287.214 1.00 283.50 ?  186 TYR H CB  1 
ATOM   17170 C CG  . TYR I  5 186 ? 41.721  34.585  286.349 1.00 277.61 ?  186 TYR H CG  1 
ATOM   17171 C CD1 . TYR I  5 186 ? 41.470  35.864  286.826 1.00 279.43 ?  186 TYR H CD1 1 
ATOM   17172 C CD2 . TYR I  5 186 ? 41.313  34.274  285.059 1.00 274.61 ?  186 TYR H CD2 1 
ATOM   17173 C CE1 . TYR I  5 186 ? 40.836  36.805  286.044 1.00 274.32 ?  186 TYR H CE1 1 
ATOM   17174 C CE2 . TYR I  5 186 ? 40.679  35.209  284.268 1.00 271.14 ?  186 TYR H CE2 1 
ATOM   17175 C CZ  . TYR I  5 186 ? 40.443  36.473  284.766 1.00 270.52 ?  186 TYR H CZ  1 
ATOM   17176 O OH  . TYR I  5 186 ? 39.812  37.413  283.985 1.00 269.97 ?  186 TYR H OH  1 
ATOM   17177 N N   . GLU I  5 187 ? 40.192  31.364  287.391 1.00 280.41 ?  187 GLU H N   1 
ATOM   17178 C CA  . GLU I  5 187 ? 38.966  30.779  286.870 1.00 281.02 ?  187 GLU H CA  1 
ATOM   17179 C C   . GLU I  5 187 ? 38.058  30.217  287.957 1.00 288.13 ?  187 GLU H C   1 
ATOM   17180 O O   . GLU I  5 187 ? 36.940  29.793  287.645 1.00 288.93 ?  187 GLU H O   1 
ATOM   17181 C CB  . GLU I  5 187 ? 39.309  29.691  285.853 1.00 279.03 ?  187 GLU H CB  1 
ATOM   17182 C CG  . GLU I  5 187 ? 40.213  30.193  284.745 1.00 272.00 ?  187 GLU H CG  1 
ATOM   17183 C CD  . GLU I  5 187 ? 40.326  29.223  283.595 1.00 274.93 ?  187 GLU H CD  1 
ATOM   17184 O OE1 . GLU I  5 187 ? 40.729  28.064  283.827 1.00 279.74 ?  187 GLU H OE1 1 
ATOM   17185 O OE2 . GLU I  5 187 ? 40.009  29.624  282.457 1.00 268.62 -1 187 GLU H OE2 1 
ATOM   17186 N N   . LYS I  5 188 ? 38.503  30.202  289.214 1.00 280.12 ?  188 LYS H N   1 
ATOM   17187 C CA  . LYS I  5 188 ? 37.691  29.739  290.333 1.00 289.10 ?  188 LYS H CA  1 
ATOM   17188 C C   . LYS I  5 188 ? 36.804  30.848  290.894 1.00 289.80 ?  188 LYS H C   1 
ATOM   17189 O O   . LYS I  5 188 ? 36.051  30.609  291.845 1.00 296.41 ?  188 LYS H O   1 
ATOM   17190 C CB  . LYS I  5 188 ? 38.605  29.169  291.433 1.00 293.50 ?  188 LYS H CB  1 
ATOM   17191 C CG  . LYS I  5 188 ? 37.920  28.332  292.516 1.00 304.71 ?  188 LYS H CG  1 
ATOM   17192 C CD  . LYS I  5 188 ? 38.901  27.944  293.614 1.00 310.00 ?  188 LYS H CD  1 
ATOM   17193 C CE  . LYS I  5 188 ? 40.122  27.245  293.039 1.00 307.68 ?  188 LYS H CE  1 
ATOM   17194 N NZ  . LYS I  5 188 ? 41.038  26.773  294.111 1.00 315.01 1  188 LYS H NZ  1 
ATOM   17195 N N   . HIS I  5 189 ? 36.856  32.043  290.304 1.00 295.00 ?  189 HIS H N   1 
ATOM   17196 C CA  . HIS I  5 189 ? 36.058  33.185  290.728 1.00 293.65 ?  189 HIS H CA  1 
ATOM   17197 C C   . HIS I  5 189 ? 35.583  33.951  289.499 1.00 285.33 ?  189 HIS H C   1 
ATOM   17198 O O   . HIS I  5 189 ? 36.107  33.783  288.395 1.00 282.45 ?  189 HIS H O   1 
ATOM   17199 C CB  . HIS I  5 189 ? 36.844  34.128  291.652 1.00 295.71 ?  189 HIS H CB  1 
ATOM   17200 C CG  . HIS I  5 189 ? 37.373  33.473  292.893 1.00 302.62 ?  189 HIS H CG  1 
ATOM   17201 N ND1 . HIS I  5 189 ? 38.720  33.286  293.118 1.00 305.51 ?  189 HIS H ND1 1 
ATOM   17202 C CD2 . HIS I  5 189 ? 36.737  32.974  293.979 1.00 310.28 ?  189 HIS H CD2 1 
ATOM   17203 C CE1 . HIS I  5 189 ? 38.891  32.694  294.287 1.00 311.33 ?  189 HIS H CE1 1 
ATOM   17204 N NE2 . HIS I  5 189 ? 37.703  32.494  294.829 1.00 315.26 ?  189 HIS H NE2 1 
ATOM   17205 N N   . LYS I  5 190 ? 34.572  34.798  289.703 1.00 285.51 ?  190 LYS H N   1 
ATOM   17206 C CA  . LYS I  5 190 ? 33.960  35.563  288.622 1.00 281.92 ?  190 LYS H CA  1 
ATOM   17207 C C   . LYS I  5 190 ? 34.248  37.058  288.708 1.00 280.84 ?  190 LYS H C   1 
ATOM   17208 O O   . LYS I  5 190 ? 34.850  37.626  287.792 1.00 276.80 ?  190 LYS H O   1 
ATOM   17209 C CB  . LYS I  5 190 ? 32.446  35.323  288.610 1.00 286.63 ?  190 LYS H CB  1 
ATOM   17210 C CG  . LYS I  5 190 ? 31.692  36.269  287.694 1.00 282.82 ?  190 LYS H CG  1 
ATOM   17211 C CD  . LYS I  5 190 ? 30.216  35.929  287.640 1.00 287.31 ?  190 LYS H CD  1 
ATOM   17212 C CE  . LYS I  5 190 ? 29.532  36.246  288.959 1.00 294.03 ?  190 LYS H CE  1 
ATOM   17213 N NZ  . LYS I  5 190 ? 28.048  36.190  288.846 1.00 295.10 1  190 LYS H NZ  1 
ATOM   17214 N N   . VAL I  5 191 ? 33.828  37.714  289.787 1.00 284.04 ?  191 VAL H N   1 
ATOM   17215 C CA  . VAL I  5 191 ? 33.816  39.172  289.872 1.00 282.77 ?  191 VAL H CA  1 
ATOM   17216 C C   . VAL I  5 191 ? 35.176  39.679  290.340 1.00 281.89 ?  191 VAL H C   1 
ATOM   17217 O O   . VAL I  5 191 ? 35.659  39.293  291.410 1.00 284.80 ?  191 VAL H O   1 
ATOM   17218 C CB  . VAL I  5 191 ? 32.702  39.660  290.811 1.00 286.85 ?  191 VAL H CB  1 
ATOM   17219 C CG1 . VAL I  5 191 ? 32.570  41.171  290.729 1.00 288.26 ?  191 VAL H CG1 1 
ATOM   17220 C CG2 . VAL I  5 191 ? 31.383  38.980  290.481 1.00 291.94 ?  191 VAL H CG2 1 
ATOM   17221 N N   . TYR I  5 192 ? 35.794  40.544  289.536 1.00 282.29 ?  192 TYR H N   1 
ATOM   17222 C CA  . TYR I  5 192 ? 37.061  41.187  289.873 1.00 282.57 ?  192 TYR H CA  1 
ATOM   17223 C C   . TYR I  5 192 ? 36.860  42.695  289.899 1.00 278.88 ?  192 TYR H C   1 
ATOM   17224 O O   . TYR I  5 192 ? 36.436  43.279  288.899 1.00 275.05 ?  192 TYR H O   1 
ATOM   17225 C CB  . TYR I  5 192 ? 38.146  40.800  288.868 1.00 274.47 ?  192 TYR H CB  1 
ATOM   17226 C CG  . TYR I  5 192 ? 38.531  39.350  288.979 1.00 276.63 ?  192 TYR H CG  1 
ATOM   17227 C CD1 . TYR I  5 192 ? 37.819  38.373  288.298 1.00 275.91 ?  192 TYR H CD1 1 
ATOM   17228 C CD2 . TYR I  5 192 ? 39.581  38.954  289.793 1.00 278.50 ?  192 TYR H CD2 1 
ATOM   17229 C CE1 . TYR I  5 192 ? 38.155  37.048  288.407 1.00 277.65 ?  192 TYR H CE1 1 
ATOM   17230 C CE2 . TYR I  5 192 ? 39.924  37.632  289.908 1.00 281.79 ?  192 TYR H CE2 1 
ATOM   17231 C CZ  . TYR I  5 192 ? 39.207  36.684  289.214 1.00 280.21 ?  192 TYR H CZ  1 
ATOM   17232 O OH  . TYR I  5 192 ? 39.547  35.362  289.328 1.00 285.06 ?  192 TYR H OH  1 
ATOM   17233 N N   . ALA I  5 193 ? 37.178  43.319  291.034 1.00 269.23 ?  193 ALA H N   1 
ATOM   17234 C CA  . ALA I  5 193 ? 36.925  44.738  291.251 1.00 271.13 ?  193 ALA H CA  1 
ATOM   17235 C C   . ALA I  5 193 ? 38.074  45.367  292.026 1.00 270.36 ?  193 ALA H C   1 
ATOM   17236 O O   . ALA I  5 193 ? 38.628  44.747  292.938 1.00 274.95 ?  193 ALA H O   1 
ATOM   17237 C CB  . ALA I  5 193 ? 35.614  44.968  292.013 1.00 276.02 ?  193 ALA H CB  1 
ATOM   17238 N N   . CYS I  5 194 ? 38.428  46.595  291.654 1.00 277.28 ?  194 CYS H N   1 
ATOM   17239 C CA  . CYS I  5 194 ? 39.324  47.436  292.438 1.00 279.35 ?  194 CYS H CA  1 
ATOM   17240 C C   . CYS I  5 194 ? 38.556  48.655  292.937 1.00 282.75 ?  194 CYS H C   1 
ATOM   17241 O O   . CYS I  5 194 ? 37.853  49.313  292.163 1.00 281.00 ?  194 CYS H O   1 
ATOM   17242 C CB  . CYS I  5 194 ? 40.565  47.841  291.619 1.00 276.14 ?  194 CYS H CB  1 
ATOM   17243 S SG  . CYS I  5 194 ? 40.319  48.966  290.202 1.00 274.27 ?  194 CYS H SG  1 
ATOM   17244 N N   . GLU I  5 195 ? 38.677  48.936  294.233 1.00 272.68 ?  195 GLU H N   1 
ATOM   17245 C CA  . GLU I  5 195 ? 38.002  50.055  294.877 1.00 277.49 ?  195 GLU H CA  1 
ATOM   17246 C C   . GLU I  5 195 ? 39.041  51.104  295.247 1.00 275.84 ?  195 GLU H C   1 
ATOM   17247 O O   . GLU I  5 195 ? 40.037  50.790  295.908 1.00 277.91 ?  195 GLU H O   1 
ATOM   17248 C CB  . GLU I  5 195 ? 37.235  49.597  296.122 1.00 287.03 ?  195 GLU H CB  1 
ATOM   17249 C CG  . GLU I  5 195 ? 36.198  50.591  296.607 1.00 294.67 ?  195 GLU H CG  1 
ATOM   17250 C CD  . GLU I  5 195 ? 35.557  50.177  297.913 1.00 308.01 ?  195 GLU H CD  1 
ATOM   17251 O OE1 . GLU I  5 195 ? 36.009  49.179  298.513 1.00 311.56 ?  195 GLU H OE1 1 
ATOM   17252 O OE2 . GLU I  5 195 ? 34.593  50.847  298.337 1.00 313.79 -1 195 GLU H OE2 1 
ATOM   17253 N N   . VAL I  5 196 ? 38.809  52.344  294.817 1.00 279.98 ?  196 VAL H N   1 
ATOM   17254 C CA  . VAL I  5 196 ? 39.779  53.429  294.932 1.00 279.50 ?  196 VAL H CA  1 
ATOM   17255 C C   . VAL I  5 196 ? 39.234  54.488  295.879 1.00 285.78 ?  196 VAL H C   1 
ATOM   17256 O O   . VAL I  5 196 ? 38.103  54.961  295.711 1.00 288.15 ?  196 VAL H O   1 
ATOM   17257 C CB  . VAL I  5 196 ? 40.098  54.037  293.555 1.00 273.60 ?  196 VAL H CB  1 
ATOM   17258 C CG1 . VAL I  5 196 ? 40.926  55.308  293.701 1.00 273.53 ?  196 VAL H CG1 1 
ATOM   17259 C CG2 . VAL I  5 196 ? 40.811  53.018  292.676 1.00 269.17 ?  196 VAL H CG2 1 
ATOM   17260 N N   . THR I  5 197 ? 40.040  54.860  296.870 1.00 260.63 ?  197 THR H N   1 
ATOM   17261 C CA  . THR I  5 197 ? 39.710  55.914  297.820 1.00 262.34 ?  197 THR H CA  1 
ATOM   17262 C C   . THR I  5 197 ? 40.681  57.071  297.641 1.00 262.86 ?  197 THR H C   1 
ATOM   17263 O O   . THR I  5 197 ? 41.900  56.874  297.687 1.00 263.68 ?  197 THR H O   1 
ATOM   17264 C CB  . THR I  5 197 ? 39.772  55.398  299.257 1.00 264.91 ?  197 THR H CB  1 
ATOM   17265 O OG1 . THR I  5 197 ? 38.906  54.265  299.394 1.00 264.43 ?  197 THR H OG1 1 
ATOM   17266 C CG2 . THR I  5 197 ? 39.338  56.486  300.230 1.00 266.67 ?  197 THR H CG2 1 
ATOM   17267 N N   . HIS I  5 198 ? 40.140  58.270  297.437 1.00 280.74 ?  198 HIS H N   1 
ATOM   17268 C CA  . HIS I  5 198 ? 40.950  59.473  297.299 1.00 279.83 ?  198 HIS H CA  1 
ATOM   17269 C C   . HIS I  5 198 ? 40.090  60.670  297.686 1.00 284.89 ?  198 HIS H C   1 
ATOM   17270 O O   . HIS I  5 198 ? 38.879  60.675  297.449 1.00 286.85 ?  198 HIS H O   1 
ATOM   17271 C CB  . HIS I  5 198 ? 41.489  59.613  295.870 1.00 272.97 ?  198 HIS H CB  1 
ATOM   17272 C CG  . HIS I  5 198 ? 42.447  60.747  295.690 1.00 271.75 ?  198 HIS H CG  1 
ATOM   17273 N ND1 . HIS I  5 198 ? 42.038  62.027  295.385 1.00 273.21 ?  198 HIS H ND1 1 
ATOM   17274 C CD2 . HIS I  5 198 ? 43.799  60.792  295.764 1.00 269.28 ?  198 HIS H CD2 1 
ATOM   17275 C CE1 . HIS I  5 198 ? 43.095  62.813  295.285 1.00 271.80 ?  198 HIS H CE1 1 
ATOM   17276 N NE2 . HIS I  5 198 ? 44.176  62.088  295.510 1.00 269.28 ?  198 HIS H NE2 1 
ATOM   17277 N N   . GLN I  5 199 ? 40.724  61.683  298.293 1.00 278.61 ?  199 GLN H N   1 
ATOM   17278 C CA  . GLN I  5 199 ? 39.960  62.809  298.827 1.00 284.45 ?  199 GLN H CA  1 
ATOM   17279 C C   . GLN I  5 199 ? 39.359  63.678  297.730 1.00 282.74 ?  199 GLN H C   1 
ATOM   17280 O O   . GLN I  5 199 ? 38.422  64.437  298.006 1.00 287.47 ?  199 GLN H O   1 
ATOM   17281 C CB  . GLN I  5 199 ? 40.825  63.683  299.739 1.00 287.86 ?  199 GLN H CB  1 
ATOM   17282 C CG  . GLN I  5 199 ? 41.849  64.534  299.009 1.00 283.63 ?  199 GLN H CG  1 
ATOM   17283 C CD  . GLN I  5 199 ? 42.392  65.651  299.878 1.00 287.91 ?  199 GLN H CD  1 
ATOM   17284 O OE1 . GLN I  5 199 ? 41.842  66.752  299.907 1.00 291.41 ?  199 GLN H OE1 1 
ATOM   17285 N NE2 . GLN I  5 199 ? 43.471  65.371  300.598 1.00 287.83 ?  199 GLN H NE2 1 
ATOM   17286 N N   . GLY I  5 200 ? 39.862  63.575  296.495 1.00 297.68 ?  200 GLY H N   1 
ATOM   17287 C CA  . GLY I  5 200 ? 39.279  64.321  295.395 1.00 296.38 ?  200 GLY H CA  1 
ATOM   17288 C C   . GLY I  5 200 ? 37.978  63.743  294.899 1.00 296.24 ?  200 GLY H C   1 
ATOM   17289 O O   . GLY I  5 200 ? 37.206  64.451  294.242 1.00 296.32 ?  200 GLY H O   1 
ATOM   17290 N N   . LEU I  5 201 ? 37.707  62.482  295.234 1.00 298.09 ?  201 LEU H N   1 
ATOM   17291 C CA  . LEU I  5 201 ? 36.438  61.841  294.932 1.00 298.34 ?  201 LEU H CA  1 
ATOM   17292 C C   . LEU I  5 201 ? 35.500  62.091  296.103 1.00 305.90 ?  201 LEU H C   1 
ATOM   17293 O O   . LEU I  5 201 ? 35.845  61.805  297.255 1.00 309.16 ?  201 LEU H O   1 
ATOM   17294 C CB  . LEU I  5 201 ? 36.616  60.335  294.717 1.00 294.42 ?  201 LEU H CB  1 
ATOM   17295 C CG  . LEU I  5 201 ? 37.449  59.839  293.530 1.00 287.02 ?  201 LEU H CG  1 
ATOM   17296 C CD1 . LEU I  5 201 ? 37.777  58.366  293.704 1.00 285.18 ?  201 LEU H CD1 1 
ATOM   17297 C CD2 . LEU I  5 201 ? 36.742  60.064  292.189 1.00 283.65 ?  201 LEU H CD2 1 
ATOM   17298 N N   . SER I  5 202 ? 34.318  62.627  295.813 1.00 301.13 ?  202 SER H N   1 
ATOM   17299 C CA  . SER I  5 202 ? 33.329  62.768  296.870 1.00 308.63 ?  202 SER H CA  1 
ATOM   17300 C C   . SER I  5 202 ? 32.878  61.410  297.390 1.00 309.34 ?  202 SER H C   1 
ATOM   17301 O O   . SER I  5 202 ? 32.405  61.319  298.528 1.00 315.61 ?  202 SER H O   1 
ATOM   17302 C CB  . SER I  5 202 ? 32.145  63.605  296.391 1.00 311.51 ?  202 SER H CB  1 
ATOM   17303 O OG  . SER I  5 202 ? 31.479  62.975  295.321 1.00 307.95 ?  202 SER H OG  1 
ATOM   17304 N N   . SER I  5 203 ? 33.011  60.355  296.581 1.00 315.94 ?  203 SER H N   1 
ATOM   17305 C CA  . SER I  5 203 ? 32.655  59.006  296.987 1.00 316.31 ?  203 SER H CA  1 
ATOM   17306 C C   . SER I  5 203 ? 33.629  57.989  296.403 1.00 309.84 ?  203 SER H C   1 
ATOM   17307 O O   . SER I  5 203 ? 34.121  58.175  295.279 1.00 304.34 ?  203 SER H O   1 
ATOM   17308 C CB  . SER I  5 203 ? 31.230  58.660  296.539 1.00 317.34 ?  203 SER H CB  1 
ATOM   17309 O OG  . SER I  5 203 ? 30.830  57.416  297.076 1.00 319.01 ?  203 SER H OG  1 
ATOM   17310 N N   . PRO I  5 204 ? 33.931  56.920  297.148 1.00 310.80 ?  204 PRO H N   1 
ATOM   17311 C CA  . PRO I  5 204 ? 34.790  55.848  296.622 1.00 307.60 ?  204 PRO H CA  1 
ATOM   17312 C C   . PRO I  5 204 ? 34.284  55.269  295.305 1.00 303.04 ?  204 PRO H C   1 
ATOM   17313 O O   . PRO I  5 204 ? 33.079  55.180  295.060 1.00 304.72 ?  204 PRO H O   1 
ATOM   17314 C CB  . PRO I  5 204 ? 34.765  54.802  297.741 1.00 313.15 ?  204 PRO H CB  1 
ATOM   17315 C CG  . PRO I  5 204 ? 34.568  55.609  298.980 1.00 320.04 ?  204 PRO H CG  1 
ATOM   17316 C CD  . PRO I  5 204 ? 33.663  56.753  298.588 1.00 322.25 ?  204 PRO H CD  1 
ATOM   17317 N N   . VAL I  5 205 ? 35.231  54.867  294.457 1.00 303.54 ?  205 VAL H N   1 
ATOM   17318 C CA  . VAL I  5 205 ? 34.953  54.400  293.101 1.00 298.08 ?  205 VAL H CA  1 
ATOM   17319 C C   . VAL I  5 205 ? 35.331  52.928  292.966 1.00 295.30 ?  205 VAL H C   1 
ATOM   17320 O O   . VAL I  5 205 ? 36.423  52.520  293.383 1.00 294.39 ?  205 VAL H O   1 
ATOM   17321 C CB  . VAL I  5 205 ? 35.708  55.236  292.058 1.00 293.27 ?  205 VAL H CB  1 
ATOM   17322 C CG1 . VAL I  5 205 ? 35.712  54.500  290.752 1.00 287.36 ?  205 VAL H CG1 1 
ATOM   17323 C CG2 . VAL I  5 205 ? 35.066  56.598  291.903 1.00 295.65 ?  205 VAL H CG2 1 
ATOM   17324 N N   . THR I  5 206 ? 34.430  52.137  292.382 1.00 278.56 ?  206 THR H N   1 
ATOM   17325 C CA  . THR I  5 206 ? 34.681  50.742  292.038 1.00 275.66 ?  206 THR H CA  1 
ATOM   17326 C C   . THR I  5 206 ? 34.648  50.555  290.521 1.00 269.34 ?  206 THR H C   1 
ATOM   17327 O O   . THR I  5 206 ? 33.684  50.960  289.863 1.00 268.57 ?  206 THR H O   1 
ATOM   17328 C CB  . THR I  5 206 ? 33.650  49.825  292.702 1.00 279.68 ?  206 THR H CB  1 
ATOM   17329 O OG1 . THR I  5 206 ? 33.717  49.973  294.127 1.00 285.83 ?  206 THR H OG1 1 
ATOM   17330 C CG2 . THR I  5 206 ? 33.912  48.373  292.344 1.00 276.87 ?  206 THR H CG2 1 
ATOM   17331 N N   . LYS I  5 207 ? 35.703  49.950  289.972 1.00 279.07 ?  207 LYS H N   1 
ATOM   17332 C CA  . LYS I  5 207 ? 35.732  49.451  288.598 1.00 273.42 ?  207 LYS H CA  1 
ATOM   17333 C C   . LYS I  5 207 ? 35.892  47.937  288.615 1.00 272.45 ?  207 LYS H C   1 
ATOM   17334 O O   . LYS I  5 207 ? 36.755  47.407  289.323 1.00 273.65 ?  207 LYS H O   1 
ATOM   17335 C CB  . LYS I  5 207 ? 36.858  50.091  287.774 1.00 268.97 ?  207 LYS H CB  1 
ATOM   17336 C CG  . LYS I  5 207 ? 36.623  51.528  287.363 1.00 268.70 ?  207 LYS H CG  1 
ATOM   17337 C CD  . LYS I  5 207 ? 35.479  51.558  286.351 1.00 267.33 ?  207 LYS H CD  1 
ATOM   17338 C CE  . LYS I  5 207 ? 35.559  52.766  285.435 1.00 264.58 ?  207 LYS H CE  1 
ATOM   17339 N NZ  . LYS I  5 207 ? 34.243  53.445  285.286 1.00 266.87 1  207 LYS H NZ  1 
ATOM   17340 N N   . SER I  5 208 ? 35.065  47.246  287.834 1.00 287.84 ?  208 SER H N   1 
ATOM   17341 C CA  . SER I  5 208 ? 35.033  45.793  287.887 1.00 287.56 ?  208 SER H CA  1 
ATOM   17342 C C   . SER I  5 208 ? 34.745  45.216  286.509 1.00 282.67 ?  208 SER H C   1 
ATOM   17343 O O   . SER I  5 208 ? 34.353  45.927  285.580 1.00 279.92 ?  208 SER H O   1 
ATOM   17344 C CB  . SER I  5 208 ? 33.987  45.305  288.893 1.00 292.83 ?  208 SER H CB  1 
ATOM   17345 O OG  . SER I  5 208 ? 32.691  45.691  288.481 1.00 293.34 ?  208 SER H OG  1 
ATOM   17346 N N   . PHE I  5 209 ? 34.975  43.907  286.387 1.00 290.32 ?  209 PHE H N   1 
ATOM   17347 C CA  . PHE I  5 209 ? 34.538  43.114  285.245 1.00 286.73 ?  209 PHE H CA  1 
ATOM   17348 C C   . PHE I  5 209 ? 34.178  41.718  285.737 1.00 289.09 ?  209 PHE H C   1 
ATOM   17349 O O   . PHE I  5 209 ? 34.575  41.302  286.829 1.00 292.91 ?  209 PHE H O   1 
ATOM   17350 C CB  . PHE I  5 209 ? 35.615  43.029  284.153 1.00 281.64 ?  209 PHE H CB  1 
ATOM   17351 C CG  . PHE I  5 209 ? 36.859  42.295  284.578 1.00 281.96 ?  209 PHE H CG  1 
ATOM   17352 C CD1 . PHE I  5 209 ? 36.985  40.929  284.365 1.00 281.52 ?  209 PHE H CD1 1 
ATOM   17353 C CD2 . PHE I  5 209 ? 37.900  42.968  285.193 1.00 282.94 ?  209 PHE H CD2 1 
ATOM   17354 C CE1 . PHE I  5 209 ? 38.125  40.251  284.756 1.00 282.22 ?  209 PHE H CE1 1 
ATOM   17355 C CE2 . PHE I  5 209 ? 39.041  42.295  285.586 1.00 283.42 ?  209 PHE H CE2 1 
ATOM   17356 C CZ  . PHE I  5 209 ? 39.154  40.935  285.367 1.00 283.13 ?  209 PHE H CZ  1 
ATOM   17357 N N   . ASN I  5 210 ? 33.413  40.997  284.921 1.00 280.17 ?  210 ASN H N   1 
ATOM   17358 C CA  . ASN I  5 210 ? 33.118  39.589  285.160 1.00 281.74 ?  210 ASN H CA  1 
ATOM   17359 C C   . ASN I  5 210 ? 33.962  38.725  284.231 1.00 277.81 ?  210 ASN H C   1 
ATOM   17360 O O   . ASN I  5 210 ? 33.967  38.938  283.013 1.00 273.33 ?  210 ASN H O   1 
ATOM   17361 C CB  . ASN I  5 210 ? 31.632  39.292  284.962 1.00 282.66 ?  210 ASN H CB  1 
ATOM   17362 C CG  . ASN I  5 210 ? 30.754  40.001  285.979 1.00 287.42 ?  210 ASN H CG  1 
ATOM   17363 O OD1 . ASN I  5 210 ? 31.016  39.957  287.183 1.00 291.91 ?  210 ASN H OD1 1 
ATOM   17364 N ND2 . ASN I  5 210 ? 29.704  40.656  285.499 1.00 286.71 ?  210 ASN H ND2 1 
ATOM   17365 N N   . ARG I  5 211 ? 34.681  37.765  284.813 1.00 280.20 ?  211 ARG H N   1 
ATOM   17366 C CA  . ARG I  5 211 ? 35.544  36.889  284.033 1.00 277.18 ?  211 ARG H CA  1 
ATOM   17367 C C   . ARG I  5 211 ? 34.750  36.189  282.938 1.00 275.87 ?  211 ARG H C   1 
ATOM   17368 O O   . ARG I  5 211 ? 33.746  35.525  283.209 1.00 277.14 ?  211 ARG H O   1 
ATOM   17369 C CB  . ARG I  5 211 ? 36.206  35.852  284.937 1.00 280.82 ?  211 ARG H CB  1 
ATOM   17370 C CG  . ARG I  5 211 ? 37.005  34.808  284.178 1.00 278.50 ?  211 ARG H CG  1 
ATOM   17371 C CD  . ARG I  5 211 ? 37.544  33.742  285.111 1.00 282.78 ?  211 ARG H CD  1 
ATOM   17372 N NE  . ARG I  5 211 ? 36.464  32.991  285.744 1.00 286.86 ?  211 ARG H NE  1 
ATOM   17373 C CZ  . ARG I  5 211 ? 35.858  31.946  285.190 1.00 287.44 ?  211 ARG H CZ  1 
ATOM   17374 N NH1 . ARG I  5 211 ? 34.884  31.322  285.837 1.00 293.43 1  211 ARG H NH1 1 
ATOM   17375 N NH2 . ARG I  5 211 ? 36.225  31.525  283.987 1.00 283.95 ?  211 ARG H NH2 1 
ATOM   17376 N N   . GLY I  5 212 ? 35.208  36.340  281.701 1.00 281.01 ?  212 GLY H N   1 
ATOM   17377 C CA  . GLY I  5 212 ? 34.532  35.758  280.559 1.00 278.33 ?  212 GLY H CA  1 
ATOM   17378 C C   . GLY I  5 212 ? 33.753  36.783  279.761 1.00 275.22 ?  212 GLY H C   1 
ATOM   17379 O O   . GLY I  5 212 ? 32.935  37.516  280.317 1.00 278.04 ?  212 GLY H O   1 
ATOM   17380 N N   . GLN J  6 1   ? 58.053  49.366  237.019 1.00 250.65 ?  1   GLN I N   1 
ATOM   17381 C CA  . GLN J  6 1   ? 57.927  48.100  237.731 1.00 244.82 ?  1   GLN I CA  1 
ATOM   17382 C C   . GLN J  6 1   ? 56.583  48.044  238.455 1.00 241.75 ?  1   GLN I C   1 
ATOM   17383 O O   . GLN J  6 1   ? 56.066  49.073  238.891 1.00 244.75 ?  1   GLN I O   1 
ATOM   17384 C CB  . GLN J  6 1   ? 59.082  47.924  238.719 1.00 245.09 ?  1   GLN I CB  1 
ATOM   17385 C CG  . GLN J  6 1   ? 59.171  49.003  239.789 1.00 251.19 ?  1   GLN I CG  1 
ATOM   17386 C CD  . GLN J  6 1   ? 59.838  50.283  239.311 1.00 264.59 ?  1   GLN I CD  1 
ATOM   17387 O OE1 . GLN J  6 1   ? 60.278  50.387  238.164 1.00 269.83 ?  1   GLN I OE1 1 
ATOM   17388 N NE2 . GLN J  6 1   ? 59.920  51.265  240.200 1.00 270.27 ?  1   GLN I NE2 1 
ATOM   17389 N N   . VAL J  6 2   ? 56.014  46.846  238.570 1.00 248.63 ?  2   VAL I N   1 
ATOM   17390 C CA  . VAL J  6 2   ? 54.729  46.636  239.230 1.00 245.80 ?  2   VAL I CA  1 
ATOM   17391 C C   . VAL J  6 2   ? 54.937  45.793  240.482 1.00 242.35 ?  2   VAL I C   1 
ATOM   17392 O O   . VAL J  6 2   ? 55.314  44.617  240.395 1.00 238.82 ?  2   VAL I O   1 
ATOM   17393 C CB  . VAL J  6 2   ? 53.711  45.973  238.293 1.00 242.95 ?  2   VAL I CB  1 
ATOM   17394 C CG1 . VAL J  6 2   ? 52.399  45.738  239.029 1.00 240.66 ?  2   VAL I CG1 1 
ATOM   17395 C CG2 . VAL J  6 2   ? 53.492  46.831  237.050 1.00 246.68 ?  2   VAL I CG2 1 
ATOM   17396 N N   . HIS J  6 3   ? 54.701  46.384  241.649 1.00 253.89 ?  3   HIS I N   1 
ATOM   17397 C CA  . HIS J  6 3   ? 54.857  45.685  242.916 1.00 247.47 ?  3   HIS I CA  1 
ATOM   17398 C C   . HIS J  6 3   ? 53.522  45.606  243.636 1.00 243.82 ?  3   HIS I C   1 
ATOM   17399 O O   . HIS J  6 3   ? 52.842  46.623  243.813 1.00 248.10 ?  3   HIS I O   1 
ATOM   17400 C CB  . HIS J  6 3   ? 55.871  46.341  243.842 1.00 252.97 ?  3   HIS I CB  1 
ATOM   17401 C CG  . HIS J  6 3   ? 56.102  45.564  245.102 1.00 251.91 ?  3   HIS I CG  1 
ATOM   17402 N ND1 . HIS J  6 3   ? 56.625  44.288  245.105 1.00 250.83 ?  3   HIS I ND1 1 
ATOM   17403 C CD2 . HIS J  6 3   ? 55.841  45.866  246.396 1.00 252.59 ?  3   HIS I CD2 1 
ATOM   17404 C CE1 . HIS J  6 3   ? 56.703  43.850  246.349 1.00 248.36 ?  3   HIS I CE1 1 
ATOM   17405 N NE2 . HIS J  6 3   ? 56.233  44.787  247.152 1.00 248.58 ?  3   HIS I NE2 1 
ATOM   17406 N N   . LEU J  6 4   ? 53.162  44.400  244.054 1.00 241.32 ?  4   LEU I N   1 
ATOM   17407 C CA  . LEU J  6 4   ? 51.929  44.134  244.774 1.00 235.02 ?  4   LEU I CA  1 
ATOM   17408 C C   . LEU J  6 4   ? 52.273  43.549  246.135 1.00 233.17 ?  4   LEU I C   1 
ATOM   17409 O O   . LEU J  6 4   ? 53.144  42.679  246.246 1.00 231.14 ?  4   LEU I O   1 
ATOM   17410 C CB  . LEU J  6 4   ? 51.017  43.187  243.993 1.00 231.07 ?  4   LEU I CB  1 
ATOM   17411 C CG  . LEU J  6 4   ? 50.646  43.651  242.582 1.00 232.22 ?  4   LEU I CG  1 
ATOM   17412 C CD1 . LEU J  6 4   ? 49.711  42.661  241.895 1.00 228.96 ?  4   LEU I CD1 1 
ATOM   17413 C CD2 . LEU J  6 4   ? 50.027  45.037  242.622 1.00 240.62 ?  4   LEU I CD2 1 
ATOM   17414 N N   . GLN J  6 5   ? 51.577  44.017  247.166 1.00 235.47 ?  5   GLN I N   1 
ATOM   17415 C CA  . GLN J  6 5   ? 51.811  43.570  248.531 1.00 235.00 ?  5   GLN I CA  1 
ATOM   17416 C C   . GLN J  6 5   ? 50.474  43.276  249.191 1.00 234.42 ?  5   GLN I C   1 
ATOM   17417 O O   . GLN J  6 5   ? 49.585  44.134  249.209 1.00 236.99 ?  5   GLN I O   1 
ATOM   17418 C CB  . GLN J  6 5   ? 52.568  44.642  249.325 1.00 238.99 ?  5   GLN I CB  1 
ATOM   17419 C CG  . GLN J  6 5   ? 52.838  44.315  250.787 1.00 239.28 ?  5   GLN I CG  1 
ATOM   17420 C CD  . GLN J  6 5   ? 53.816  43.168  250.977 1.00 236.62 ?  5   GLN I CD  1 
ATOM   17421 O OE1 . GLN J  6 5   ? 54.598  42.842  250.082 1.00 235.49 ?  5   GLN I OE1 1 
ATOM   17422 N NE2 . GLN J  6 5   ? 53.802  42.574  252.164 1.00 236.09 ?  5   GLN I NE2 1 
ATOM   17423 N N   . GLU J  6 6   ? 50.336  42.067  249.728 1.00 232.45 ?  6   GLU I N   1 
ATOM   17424 C CA  . GLU J  6 6   ? 49.136  41.638  250.430 1.00 233.19 ?  6   GLU I CA  1 
ATOM   17425 C C   . GLU J  6 6   ? 49.333  41.776  251.932 1.00 237.72 ?  6   GLU I C   1 
ATOM   17426 O O   . GLU J  6 6   ? 50.438  41.603  252.452 1.00 237.74 ?  6   GLU I O   1 
ATOM   17427 C CB  . GLU J  6 6   ? 48.797  40.184  250.092 1.00 227.06 ?  6   GLU I CB  1 
ATOM   17428 C CG  . GLU J  6 6   ? 48.472  39.946  248.636 1.00 225.16 ?  6   GLU I CG  1 
ATOM   17429 C CD  . GLU J  6 6   ? 49.705  39.759  247.775 1.00 223.89 ?  6   GLU I CD  1 
ATOM   17430 O OE1 . GLU J  6 6   ? 50.823  40.013  248.271 1.00 224.92 ?  6   GLU I OE1 1 
ATOM   17431 O OE2 . GLU J  6 6   ? 49.556  39.386  246.593 1.00 222.20 -1 6   GLU I OE2 1 
ATOM   17432 N N   . SER J  6 7   ? 48.244  42.084  252.630 1.00 235.89 ?  7   SER I N   1 
ATOM   17433 C CA  . SER J  6 7   ? 48.310  42.239  254.074 1.00 239.71 ?  7   SER I CA  1 
ATOM   17434 C C   . SER J  6 7   ? 46.952  41.937  254.680 1.00 240.28 ?  7   SER I C   1 
ATOM   17435 O O   . SER J  6 7   ? 45.935  42.467  254.222 1.00 241.36 ?  7   SER I O   1 
ATOM   17436 C CB  . SER J  6 7   ? 48.743  43.659  254.453 1.00 246.39 ?  7   SER I CB  1 
ATOM   17437 O OG  . SER J  6 7   ? 47.849  44.615  253.910 1.00 246.89 ?  7   SER I OG  1 
ATOM   17438 N N   . GLY J  6 8   ? 46.937  41.081  255.695 1.00 236.81 ?  8   GLY I N   1 
ATOM   17439 C CA  . GLY J  6 8   ? 45.702  40.737  256.351 1.00 234.77 ?  8   GLY I CA  1 
ATOM   17440 C C   . GLY J  6 8   ? 45.898  40.409  257.815 1.00 238.20 ?  8   GLY I C   1 
ATOM   17441 O O   . GLY J  6 8   ? 46.977  40.599  258.387 1.00 240.48 ?  8   GLY I O   1 
ATOM   17442 N N   . PRO J  6 9   ? 44.841  39.901  258.451 1.00 241.43 ?  9   PRO I N   1 
ATOM   17443 C CA  . PRO J  6 9   ? 44.954  39.556  259.876 1.00 244.66 ?  9   PRO I CA  1 
ATOM   17444 C C   . PRO J  6 9   ? 45.826  38.342  260.120 1.00 242.44 ?  9   PRO I C   1 
ATOM   17445 O O   . PRO J  6 9   ? 46.653  38.340  261.040 1.00 244.48 ?  9   PRO I O   1 
ATOM   17446 C CB  . PRO J  6 9   ? 43.496  39.298  260.288 1.00 246.84 ?  9   PRO I CB  1 
ATOM   17447 C CG  . PRO J  6 9   ? 42.821  38.897  259.025 1.00 243.06 ?  9   PRO I CG  1 
ATOM   17448 C CD  . PRO J  6 9   ? 43.481  39.683  257.931 1.00 240.83 ?  9   PRO I CD  1 
ATOM   17449 N N   . GLY J  6 10  ? 45.661  37.308  259.297 1.00 253.52 ?  10  GLY I N   1 
ATOM   17450 C CA  . GLY J  6 10  ? 46.365  36.066  259.405 1.00 251.58 ?  10  GLY I CA  1 
ATOM   17451 C C   . GLY J  6 10  ? 45.586  35.004  260.157 1.00 253.06 ?  10  GLY I C   1 
ATOM   17452 O O   . GLY J  6 10  ? 45.702  33.817  259.836 1.00 250.94 ?  10  GLY I O   1 
ATOM   17453 N N   . LEU J  6 11  ? 44.799  35.401  261.152 1.00 247.91 ?  11  LEU I N   1 
ATOM   17454 C CA  . LEU J  6 11  ? 43.983  34.479  261.938 1.00 250.18 ?  11  LEU I CA  1 
ATOM   17455 C C   . LEU J  6 11  ? 42.587  35.080  262.056 1.00 253.03 ?  11  LEU I C   1 
ATOM   17456 O O   . LEU J  6 11  ? 42.439  36.213  262.528 1.00 256.25 ?  11  LEU I O   1 
ATOM   17457 C CB  . LEU J  6 11  ? 44.595  34.204  263.319 1.00 253.87 ?  11  LEU I CB  1 
ATOM   17458 C CG  . LEU J  6 11  ? 44.080  33.010  264.148 1.00 255.70 ?  11  LEU I CG  1 
ATOM   17459 C CD1 . LEU J  6 11  ? 44.904  32.878  265.430 1.00 259.48 ?  11  LEU I CD1 1 
ATOM   17460 C CD2 . LEU J  6 11  ? 42.578  33.018  264.471 1.00 258.60 ?  11  LEU I CD2 1 
ATOM   17461 N N   . VAL J  6 12  ? 41.566  34.338  261.621 1.00 244.97 ?  12  VAL I N   1 
ATOM   17462 C CA  . VAL J  6 12  ? 40.177  34.794  261.660 1.00 247.89 ?  12  VAL I CA  1 
ATOM   17463 C C   . VAL J  6 12  ? 39.327  33.715  262.318 1.00 250.38 ?  12  VAL I C   1 
ATOM   17464 O O   . VAL J  6 12  ? 39.383  32.544  261.924 1.00 247.71 ?  12  VAL I O   1 
ATOM   17465 C CB  . VAL J  6 12  ? 39.627  35.127  260.259 1.00 244.71 ?  12  VAL I CB  1 
ATOM   17466 C CG1 . VAL J  6 12  ? 38.172  35.572  260.355 1.00 248.41 ?  12  VAL I CG1 1 
ATOM   17467 C CG2 . VAL J  6 12  ? 40.457  36.209  259.618 1.00 242.71 ?  12  VAL I CG2 1 
ATOM   17468 N N   . LYS J  6 13  ? 38.539  34.113  263.314 1.00 241.87 ?  13  LYS I N   1 
ATOM   17469 C CA  . LYS J  6 13  ? 37.668  33.180  264.012 1.00 245.29 ?  13  LYS I CA  1 
ATOM   17470 C C   . LYS J  6 13  ? 36.574  32.647  263.087 1.00 243.52 ?  13  LYS I C   1 
ATOM   17471 O O   . LYS J  6 13  ? 36.191  33.303  262.116 1.00 241.37 ?  13  LYS I O   1 
ATOM   17472 C CB  . LYS J  6 13  ? 37.013  33.855  265.214 1.00 252.13 ?  13  LYS I CB  1 
ATOM   17473 C CG  . LYS J  6 13  ? 37.962  34.555  266.164 1.00 254.65 ?  13  LYS I CG  1 
ATOM   17474 C CD  . LYS J  6 13  ? 38.981  33.586  266.730 1.00 253.68 ?  13  LYS I CD  1 
ATOM   17475 C CE  . LYS J  6 13  ? 39.953  34.293  267.655 1.00 256.29 ?  13  LYS I CE  1 
ATOM   17476 N NZ  . LYS J  6 13  ? 40.968  33.350  268.196 1.00 255.63 1  13  LYS I NZ  1 
ATOM   17477 N N   . PRO J  6 14  ? 36.072  31.444  263.363 1.00 254.69 ?  14  PRO I N   1 
ATOM   17478 C CA  . PRO J  6 14  ? 34.976  30.895  262.559 1.00 253.72 ?  14  PRO I CA  1 
ATOM   17479 C C   . PRO J  6 14  ? 33.733  31.771  262.623 1.00 257.82 ?  14  PRO I C   1 
ATOM   17480 O O   . PRO J  6 14  ? 33.482  32.465  263.612 1.00 262.84 ?  14  PRO I O   1 
ATOM   17481 C CB  . PRO J  6 14  ? 34.729  29.519  263.189 1.00 255.84 ?  14  PRO I CB  1 
ATOM   17482 C CG  . PRO J  6 14  ? 36.034  29.164  263.823 1.00 255.02 ?  14  PRO I CG  1 
ATOM   17483 C CD  . PRO J  6 14  ? 36.596  30.459  264.326 1.00 256.49 ?  14  PRO I CD  1 
ATOM   17484 N N   . SER J  6 15  ? 32.953  31.727  261.540 1.00 254.79 ?  15  SER I N   1 
ATOM   17485 C CA  . SER J  6 15  ? 31.715  32.501  261.399 1.00 258.38 ?  15  SER I CA  1 
ATOM   17486 C C   . SER J  6 15  ? 31.946  34.002  261.569 1.00 259.92 ?  15  SER I C   1 
ATOM   17487 O O   . SER J  6 15  ? 31.119  34.714  262.143 1.00 266.47 ?  15  SER I O   1 
ATOM   17488 C CB  . SER J  6 15  ? 30.643  32.013  262.378 1.00 264.92 ?  15  SER I CB  1 
ATOM   17489 O OG  . SER J  6 15  ? 30.993  32.308  263.720 1.00 269.02 ?  15  SER I OG  1 
ATOM   17490 N N   . GLU J  6 16  ? 33.080  34.488  261.073 1.00 249.92 ?  16  GLU I N   1 
ATOM   17491 C CA  . GLU J  6 16  ? 33.416  35.903  261.127 1.00 251.38 ?  16  GLU I CA  1 
ATOM   17492 C C   . GLU J  6 16  ? 33.568  36.428  259.696 1.00 246.76 ?  16  GLU I C   1 
ATOM   17493 O O   . GLU J  6 16  ? 33.264  35.730  258.724 1.00 243.28 ?  16  GLU I O   1 
ATOM   17494 C CB  . GLU J  6 16  ? 34.687  36.097  261.954 1.00 251.26 ?  16  GLU I CB  1 
ATOM   17495 C CG  . GLU J  6 16  ? 34.776  37.393  262.720 1.00 256.05 ?  16  GLU I CG  1 
ATOM   17496 C CD  . GLU J  6 16  ? 36.084  37.506  263.470 1.00 255.64 ?  16  GLU I CD  1 
ATOM   17497 O OE1 . GLU J  6 16  ? 36.902  36.565  263.379 1.00 251.72 ?  16  GLU I OE1 1 
ATOM   17498 O OE2 . GLU J  6 16  ? 36.293  38.528  264.154 1.00 259.56 -1 16  GLU I OE2 1 
ATOM   17499 N N   . THR J  6 17  ? 34.043  37.668  259.567 1.00 258.19 ?  17  THR I N   1 
ATOM   17500 C CA  . THR J  6 17  ? 34.236  38.307  258.266 1.00 257.94 ?  17  THR I CA  1 
ATOM   17501 C C   . THR J  6 17  ? 35.720  38.605  258.052 1.00 252.77 ?  17  THR I C   1 
ATOM   17502 O O   . THR J  6 17  ? 36.291  39.470  258.727 1.00 252.17 ?  17  THR I O   1 
ATOM   17503 C CB  . THR J  6 17  ? 33.371  39.566  258.131 1.00 263.81 ?  17  THR I CB  1 
ATOM   17504 O OG1 . THR J  6 17  ? 33.729  40.282  256.940 1.00 261.48 ?  17  THR I OG1 1 
ATOM   17505 C CG2 . THR J  6 17  ? 33.495  40.469  259.354 1.00 265.10 ?  17  THR I CG2 1 
ATOM   17506 N N   . LEU J  6 18  ? 36.343  37.882  257.121 1.00 251.05 ?  18  LEU I N   1 
ATOM   17507 C CA  . LEU J  6 18  ? 37.746  38.088  256.772 1.00 241.03 ?  18  LEU I CA  1 
ATOM   17508 C C   . LEU J  6 18  ? 37.911  39.331  255.907 1.00 244.37 ?  18  LEU I C   1 
ATOM   17509 O O   . LEU J  6 18  ? 37.180  39.517  254.930 1.00 250.27 ?  18  LEU I O   1 
ATOM   17510 C CB  . LEU J  6 18  ? 38.310  36.869  256.040 1.00 229.56 ?  18  LEU I CB  1 
ATOM   17511 C CG  . LEU J  6 18  ? 39.659  37.076  255.338 1.00 222.07 ?  18  LEU I CG  1 
ATOM   17512 C CD1 . LEU J  6 18  ? 40.771  37.403  256.317 1.00 220.65 ?  18  LEU I CD1 1 
ATOM   17513 C CD2 . LEU J  6 18  ? 40.028  35.851  254.524 1.00 217.46 ?  18  LEU I CD2 1 
ATOM   17514 N N   . SER J  6 19  ? 38.875  40.180  256.263 1.00 215.76 ?  19  SER I N   1 
ATOM   17515 C CA  . SER J  6 19  ? 39.168  41.396  255.512 1.00 223.31 ?  19  SER I CA  1 
ATOM   17516 C C   . SER J  6 19  ? 40.641  41.419  255.133 1.00 220.42 ?  19  SER I C   1 
ATOM   17517 O O   . SER J  6 19  ? 41.511  41.320  256.003 1.00 220.26 ?  19  SER I O   1 
ATOM   17518 C CB  . SER J  6 19  ? 38.813  42.648  256.321 1.00 233.38 ?  19  SER I CB  1 
ATOM   17519 O OG  . SER J  6 19  ? 39.005  43.823  255.550 1.00 245.26 ?  19  SER I OG  1 
ATOM   17520 N N   . LEU J  6 20  ? 40.912  41.547  253.835 1.00 228.83 ?  20  LEU I N   1 
ATOM   17521 C CA  . LEU J  6 20  ? 42.262  41.575  253.293 1.00 228.29 ?  20  LEU I CA  1 
ATOM   17522 C C   . LEU J  6 20  ? 42.454  42.855  252.486 1.00 237.68 ?  20  LEU I C   1 
ATOM   17523 O O   . LEU J  6 20  ? 41.486  43.504  252.078 1.00 244.47 ?  20  LEU I O   1 
ATOM   17524 C CB  . LEU J  6 20  ? 42.540  40.353  252.409 1.00 216.15 ?  20  LEU I CB  1 
ATOM   17525 C CG  . LEU J  6 20  ? 42.448  38.992  253.098 1.00 212.66 ?  20  LEU I CG  1 
ATOM   17526 C CD1 . LEU J  6 20  ? 42.655  37.893  252.085 1.00 210.26 ?  20  LEU I CD1 1 
ATOM   17527 C CD2 . LEU J  6 20  ? 43.480  38.888  254.212 1.00 213.80 ?  20  LEU I CD2 1 
ATOM   17528 N N   . THR J  6 21  ? 43.722  43.221  252.267 1.00 235.06 ?  21  THR I N   1 
ATOM   17529 C CA  . THR J  6 21  ? 44.080  44.436  251.540 1.00 242.94 ?  21  THR I CA  1 
ATOM   17530 C C   . THR J  6 21  ? 45.327  44.197  250.699 1.00 240.94 ?  21  THR I C   1 
ATOM   17531 O O   . THR J  6 21  ? 46.305  43.628  251.194 1.00 237.81 ?  21  THR I O   1 
ATOM   17532 C CB  . THR J  6 21  ? 44.314  45.598  252.513 1.00 254.06 ?  21  THR I CB  1 
ATOM   17533 O OG1 . THR J  6 21  ? 43.147  45.793  253.330 1.00 258.00 ?  21  THR I OG1 1 
ATOM   17534 C CG2 . THR J  6 21  ? 44.588  46.870  251.734 1.00 265.78 ?  21  THR I CG2 1 
ATOM   17535 N N   . CYS J  6 22  ? 45.278  44.596  249.418 1.00 257.58 ?  22  CYS I N   1 
ATOM   17536 C CA  . CYS J  6 22  ? 46.390  44.463  248.458 1.00 252.42 ?  22  CYS I CA  1 
ATOM   17537 C C   . CYS J  6 22  ? 46.969  45.817  248.113 1.00 256.99 ?  22  CYS I C   1 
ATOM   17538 O O   . CYS J  6 22  ? 46.429  46.585  247.309 1.00 261.38 ?  22  CYS I O   1 
ATOM   17539 C CB  . CYS J  6 22  ? 45.887  43.763  247.210 1.00 244.52 ?  22  CYS I CB  1 
ATOM   17540 S SG  . CYS J  6 22  ? 47.124  43.599  245.918 1.00 237.78 ?  22  CYS I SG  1 
ATOM   17541 N N   . ASN J  6 23  ? 48.009  46.154  248.776 1.00 244.88 ?  23  ASN I N   1 
ATOM   17542 C CA  . ASN J  6 23  ? 48.629  47.430  248.507 1.00 248.06 ?  23  ASN I CA  1 
ATOM   17543 C C   . ASN J  6 23  ? 49.375  47.409  247.154 1.00 240.29 ?  23  ASN I C   1 
ATOM   17544 O O   . ASN J  6 23  ? 50.292  46.610  246.910 1.00 236.61 ?  23  ASN I O   1 
ATOM   17545 C CB  . ASN J  6 23  ? 49.365  47.660  249.797 1.00 251.44 ?  23  ASN I CB  1 
ATOM   17546 C CG  . ASN J  6 23  ? 49.207  49.041  250.365 1.00 273.18 ?  23  ASN I CG  1 
ATOM   17547 O OD1 . ASN J  6 23  ? 48.975  50.026  249.662 1.00 276.67 ?  23  ASN I OD1 1 
ATOM   17548 N ND2 . ASN J  6 23  ? 49.232  49.122  251.672 1.00 297.84 ?  23  ASN I ND2 1 
ATOM   17549 N N   . VAL J  6 24  ? 48.934  48.275  246.266 1.00 246.37 ?  24  VAL I N   1 
ATOM   17550 C CA  . VAL J  6 24  ? 49.436  48.331  244.905 1.00 240.29 ?  24  VAL I CA  1 
ATOM   17551 C C   . VAL J  6 24  ? 50.340  49.540  244.743 1.00 242.10 ?  24  VAL I C   1 
ATOM   17552 O O   . VAL J  6 24  ? 49.996  50.653  245.164 1.00 250.68 ?  24  VAL I O   1 
ATOM   17553 C CB  . VAL J  6 24  ? 48.254  48.388  243.930 1.00 242.47 ?  24  VAL I CB  1 
ATOM   17554 C CG1 . VAL J  6 24  ? 48.729  48.441  242.519 1.00 236.45 ?  24  VAL I CG1 1 
ATOM   17555 C CG2 . VAL J  6 24  ? 47.305  47.222  244.178 1.00 240.18 ?  24  VAL I CG2 1 
ATOM   17556 N N   . SER J  6 25  ? 51.497  49.295  244.159 1.00 235.98 ?  25  SER I N   1 
ATOM   17557 C CA  . SER J  6 25  ? 52.475  50.313  243.846 1.00 245.37 ?  25  SER I CA  1 
ATOM   17558 C C   . SER J  6 25  ? 52.958  50.032  242.433 1.00 243.34 ?  25  SER I C   1 
ATOM   17559 O O   . SER J  6 25  ? 53.283  48.885  242.108 1.00 238.03 ?  25  SER I O   1 
ATOM   17560 C CB  . SER J  6 25  ? 53.645  50.291  244.833 1.00 249.97 ?  25  SER I CB  1 
ATOM   17561 O OG  . SER J  6 25  ? 53.210  50.519  246.163 1.00 255.97 ?  25  SER I OG  1 
ATOM   17562 N N   . GLY J  6 26  ? 53.006  51.066  241.600 1.00 238.93 ?  26  GLY I N   1 
ATOM   17563 C CA  . GLY J  6 26  ? 53.470  50.914  240.236 1.00 236.86 ?  26  GLY I CA  1 
ATOM   17564 C C   . GLY J  6 26  ? 52.424  51.105  239.160 1.00 236.83 ?  26  GLY I C   1 
ATOM   17565 O O   . GLY J  6 26  ? 52.791  51.232  237.985 1.00 238.54 ?  26  GLY I O   1 
ATOM   17566 N N   . THR J  6 27  ? 51.142  51.110  239.508 1.00 236.17 ?  27  THR I N   1 
ATOM   17567 C CA  . THR J  6 27  ? 50.090  51.285  238.518 1.00 237.06 ?  27  THR I CA  1 
ATOM   17568 C C   . THR J  6 27  ? 48.839  51.782  239.221 1.00 238.75 ?  27  THR I C   1 
ATOM   17569 O O   . THR J  6 27  ? 48.716  51.699  240.445 1.00 240.34 ?  27  THR I O   1 
ATOM   17570 C CB  . THR J  6 27  ? 49.809  49.979  237.762 1.00 231.61 ?  27  THR I CB  1 
ATOM   17571 O OG1 . THR J  6 27  ? 48.759  50.179  236.804 1.00 232.89 ?  27  THR I OG1 1 
ATOM   17572 C CG2 . THR J  6 27  ? 49.419  48.883  238.734 1.00 229.05 ?  27  THR I CG2 1 
ATOM   17573 N N   . LEU J  6 28  ? 47.912  52.299  238.424 1.00 234.35 ?  28  LEU I N   1 
ATOM   17574 C CA  . LEU J  6 28  ? 46.645  52.803  238.930 1.00 243.04 ?  28  LEU I CA  1 
ATOM   17575 C C   . LEU J  6 28  ? 45.628  51.673  238.997 1.00 240.53 ?  28  LEU I C   1 
ATOM   17576 O O   . LEU J  6 28  ? 45.651  50.742  238.186 1.00 232.84 ?  28  LEU I O   1 
ATOM   17577 C CB  . LEU J  6 28  ? 46.113  53.947  238.065 1.00 249.79 ?  28  LEU I CB  1 
ATOM   17578 C CG  . LEU J  6 28  ? 46.968  55.214  238.013 1.00 254.74 ?  28  LEU I CG  1 
ATOM   17579 C CD1 . LEU J  6 28  ? 46.306  56.283  237.148 1.00 262.82 ?  28  LEU I CD1 1 
ATOM   17580 C CD2 . LEU J  6 28  ? 47.223  55.728  239.421 1.00 260.19 ?  28  LEU I CD2 1 
ATOM   17581 N N   . VAL J  6 29  ? 44.715  51.772  239.971 1.00 250.55 ?  29  VAL I N   1 
ATOM   17582 C CA  . VAL J  6 29  ? 43.738  50.705  240.169 1.00 247.90 ?  29  VAL I CA  1 
ATOM   17583 C C   . VAL J  6 29  ? 42.575  50.820  239.199 1.00 249.54 ?  29  VAL I C   1 
ATOM   17584 O O   . VAL J  6 29  ? 41.763  49.891  239.093 1.00 244.72 ?  29  VAL I O   1 
ATOM   17585 C CB  . VAL J  6 29  ? 43.252  50.770  241.634 1.00 255.42 ?  29  VAL I CB  1 
ATOM   17586 C CG1 . VAL J  6 29  ? 42.500  49.504  242.042 1.00 251.00 ?  29  VAL I CG1 1 
ATOM   17587 C CG2 . VAL J  6 29  ? 44.427  51.069  242.597 1.00 256.94 ?  29  VAL I CG2 1 
ATOM   17588 N N   . ARG J  6 30  ? 42.502  51.917  238.450 1.00 240.06 ?  30  ARG I N   1 
ATOM   17589 C CA  . ARG J  6 30  ? 41.421  52.145  237.507 1.00 242.06 ?  30  ARG I CA  1 
ATOM   17590 C C   . ARG J  6 30  ? 41.764  51.621  236.116 1.00 233.02 ?  30  ARG I C   1 
ATOM   17591 O O   . ARG J  6 30  ? 40.853  51.265  235.359 1.00 230.57 ?  30  ARG I O   1 
ATOM   17592 C CB  . ARG J  6 30  ? 41.043  53.631  237.478 1.00 252.22 ?  30  ARG I CB  1 
ATOM   17593 C CG  . ARG J  6 30  ? 39.858  53.942  236.585 1.00 256.00 ?  30  ARG I CG  1 
ATOM   17594 C CD  . ARG J  6 30  ? 39.295  55.282  236.954 1.00 269.43 ?  30  ARG I CD  1 
ATOM   17595 N NE  . ARG J  6 30  ? 40.338  56.291  236.899 1.00 275.80 ?  30  ARG I NE  1 
ATOM   17596 C CZ  . ARG J  6 30  ? 40.167  57.557  237.251 1.00 287.35 ?  30  ARG I CZ  1 
ATOM   17597 N NH1 . ARG J  6 30  ? 38.985  57.971  237.688 1.00 293.49 1  30  ARG I NH1 1 
ATOM   17598 N NH2 . ARG J  6 30  ? 41.180  58.404  237.168 1.00 292.71 ?  30  ARG I NH2 1 
ATOM   17599 N N   . ASP J  6 31  ? 43.056  51.524  235.781 1.00 242.01 ?  31  ASP I N   1 
ATOM   17600 C CA  . ASP J  6 31  ? 43.505  51.117  234.456 1.00 238.58 ?  31  ASP I CA  1 
ATOM   17601 C C   . ASP J  6 31  ? 43.802  49.620  234.350 1.00 232.19 ?  31  ASP I C   1 
ATOM   17602 O O   . ASP J  6 31  ? 44.436  49.195  233.379 1.00 231.32 ?  31  ASP I O   1 
ATOM   17603 C CB  . ASP J  6 31  ? 44.799  51.862  234.096 1.00 241.57 ?  31  ASP I CB  1 
ATOM   17604 C CG  . ASP J  6 31  ? 44.567  53.290  233.632 1.00 248.73 ?  31  ASP I CG  1 
ATOM   17605 O OD1 . ASP J  6 31  ? 43.592  53.926  234.093 1.00 252.39 ?  31  ASP I OD1 1 
ATOM   17606 O OD2 . ASP J  6 31  ? 45.352  53.764  232.784 1.00 251.03 -1 31  ASP I OD2 1 
ATOM   17607 N N   . ASN J  6 32  ? 43.391  48.813  235.321 1.00 232.40 ?  32  ASN I N   1 
ATOM   17608 C CA  . ASN J  6 32  ? 43.683  47.393  235.214 1.00 228.88 ?  32  ASN I CA  1 
ATOM   17609 C C   . ASN J  6 32  ? 42.544  46.597  235.821 1.00 227.39 ?  32  ASN I C   1 
ATOM   17610 O O   . ASN J  6 32  ? 41.725  47.120  236.581 1.00 228.32 ?  32  ASN I O   1 
ATOM   17611 C CB  . ASN J  6 32  ? 45.009  47.023  235.894 1.00 229.21 ?  32  ASN I CB  1 
ATOM   17612 C CG  . ASN J  6 32  ? 46.207  47.633  235.207 1.00 230.40 ?  32  ASN I CG  1 
ATOM   17613 O OD1 . ASN J  6 32  ? 46.631  48.733  235.546 1.00 232.63 ?  32  ASN I OD1 1 
ATOM   17614 N ND2 . ASN J  6 32  ? 46.761  46.917  234.232 1.00 228.94 ?  32  ASN I ND2 1 
ATOM   17615 N N   . TYR J  6 33  ? 42.512  45.318  235.478 1.00 233.25 ?  33  TYR I N   1 
ATOM   17616 C CA  . TYR J  6 33  ? 41.593  44.384  236.098 1.00 232.98 ?  33  TYR I CA  1 
ATOM   17617 C C   . TYR J  6 33  ? 42.338  43.782  237.282 1.00 235.35 ?  33  TYR I C   1 
ATOM   17618 O O   . TYR J  6 33  ? 43.566  43.665  237.259 1.00 236.13 ?  33  TYR I O   1 
ATOM   17619 C CB  . TYR J  6 33  ? 41.119  43.323  235.104 1.00 230.46 ?  33  TYR I CB  1 
ATOM   17620 C CG  . TYR J  6 33  ? 40.114  43.834  234.081 1.00 227.69 ?  33  TYR I CG  1 
ATOM   17621 C CD1 . TYR J  6 33  ? 40.525  44.574  232.978 1.00 225.34 ?  33  TYR I CD1 1 
ATOM   17622 C CD2 . TYR J  6 33  ? 38.760  43.540  234.200 1.00 227.08 ?  33  TYR I CD2 1 
ATOM   17623 C CE1 . TYR J  6 33  ? 39.613  45.031  232.040 1.00 222.32 ?  33  TYR I CE1 1 
ATOM   17624 C CE2 . TYR J  6 33  ? 37.842  43.989  233.266 1.00 224.30 ?  33  TYR I CE2 1 
ATOM   17625 C CZ  . TYR J  6 33  ? 38.273  44.732  232.188 1.00 221.75 ?  33  TYR I CZ  1 
ATOM   17626 O OH  . TYR J  6 33  ? 37.362  45.181  231.259 1.00 218.68 ?  33  TYR I OH  1 
ATOM   17627 N N   . TRP J  6 34  ? 41.600  43.395  238.318 1.00 229.24 ?  34  TRP I N   1 
ATOM   17628 C CA  . TRP J  6 34  ? 42.223  42.869  239.526 1.00 229.90 ?  34  TRP I CA  1 
ATOM   17629 C C   . TRP J  6 34  ? 41.534  41.592  239.982 1.00 225.64 ?  34  TRP I C   1 
ATOM   17630 O O   . TRP J  6 34  ? 40.308  41.563  240.118 1.00 225.82 ?  34  TRP I O   1 
ATOM   17631 C CB  . TRP J  6 34  ? 42.175  43.934  240.626 1.00 236.54 ?  34  TRP I CB  1 
ATOM   17632 C CG  . TRP J  6 34  ? 42.875  45.197  240.209 1.00 239.40 ?  34  TRP I CG  1 
ATOM   17633 C CD1 . TRP J  6 34  ? 42.287  46.320  239.702 1.00 240.85 ?  34  TRP I CD1 1 
ATOM   17634 C CD2 . TRP J  6 34  ? 44.283  45.466  240.247 1.00 239.80 ?  34  TRP I CD2 1 
ATOM   17635 N NE1 . TRP J  6 34  ? 43.238  47.269  239.419 1.00 243.98 ?  34  TRP I NE1 1 
ATOM   17636 C CE2 . TRP J  6 34  ? 44.471  46.772  239.747 1.00 243.06 ?  34  TRP I CE2 1 
ATOM   17637 C CE3 . TRP J  6 34  ? 45.401  44.734  240.657 1.00 237.73 ?  34  TRP I CE3 1 
ATOM   17638 C CZ2 . TRP J  6 34  ? 45.731  47.359  239.646 1.00 245.48 ?  34  TRP I CZ2 1 
ATOM   17639 C CZ3 . TRP J  6 34  ? 46.649  45.320  240.557 1.00 241.88 ?  34  TRP I CZ3 1 
ATOM   17640 C CH2 . TRP J  6 34  ? 46.805  46.618  240.054 1.00 246.08 ?  34  TRP I CH2 1 
ATOM   17641 N N   . SER J  6 35  ? 42.318  40.536  240.210 1.00 226.08 ?  35  SER I N   1 
ATOM   17642 C CA  . SER J  6 35  ? 41.776  39.251  240.627 1.00 222.98 ?  35  SER I CA  1 
ATOM   17643 C C   . SER J  6 35  ? 42.410  38.770  241.928 1.00 224.89 ?  35  SER I C   1 
ATOM   17644 O O   . SER J  6 35  ? 43.557  39.101  242.244 1.00 227.69 ?  35  SER I O   1 
ATOM   17645 C CB  . SER J  6 35  ? 42.002  38.188  239.546 1.00 215.68 ?  35  SER I CB  1 
ATOM   17646 O OG  . SER J  6 35  ? 41.438  38.592  238.312 1.00 217.70 ?  35  SER I OG  1 
ATOM   17647 N N   . TRP J  6 36  ? 41.638  37.970  242.669 1.00 222.06 ?  36  TRP I N   1 
ATOM   17648 C CA  . TRP J  6 36  ? 42.048  37.334  243.918 1.00 214.88 ?  36  TRP I CA  1 
ATOM   17649 C C   . TRP J  6 36  ? 42.008  35.825  243.723 1.00 210.36 ?  36  TRP I C   1 
ATOM   17650 O O   . TRP J  6 36  ? 41.041  35.285  243.176 1.00 209.14 ?  36  TRP I O   1 
ATOM   17651 C CB  . TRP J  6 36  ? 41.184  37.752  245.121 1.00 217.67 ?  36  TRP I CB  1 
ATOM   17652 C CG  . TRP J  6 36  ? 41.491  39.126  245.686 1.00 226.03 ?  36  TRP I CG  1 
ATOM   17653 C CD1 . TRP J  6 36  ? 41.017  40.333  245.256 1.00 230.58 ?  36  TRP I CD1 1 
ATOM   17654 C CD2 . TRP J  6 36  ? 42.334  39.407  246.814 1.00 230.65 ?  36  TRP I CD2 1 
ATOM   17655 N NE1 . TRP J  6 36  ? 41.525  41.347  246.040 1.00 235.86 ?  36  TRP I NE1 1 
ATOM   17656 C CE2 . TRP J  6 36  ? 42.332  40.803  247.005 1.00 236.75 ?  36  TRP I CE2 1 
ATOM   17657 C CE3 . TRP J  6 36  ? 43.089  38.609  247.682 1.00 226.33 ?  36  TRP I CE3 1 
ATOM   17658 C CZ2 . TRP J  6 36  ? 43.062  41.418  248.024 1.00 240.41 ?  36  TRP I CZ2 1 
ATOM   17659 C CZ3 . TRP J  6 36  ? 43.811  39.221  248.693 1.00 227.40 ?  36  TRP I CZ3 1 
ATOM   17660 C CH2 . TRP J  6 36  ? 43.792  40.611  248.855 1.00 233.90 ?  36  TRP I CH2 1 
ATOM   17661 N N   . ILE J  6 37  ? 43.069  35.158  244.163 1.00 206.23 ?  37  ILE I N   1 
ATOM   17662 C CA  . ILE J  6 37  ? 43.241  33.717  244.036 1.00 204.01 ?  37  ILE I CA  1 
ATOM   17663 C C   . ILE J  6 37  ? 43.608  33.133  245.395 1.00 204.18 ?  37  ILE I C   1 
ATOM   17664 O O   . ILE J  6 37  ? 44.547  33.604  246.047 1.00 205.72 ?  37  ILE I O   1 
ATOM   17665 C CB  . ILE J  6 37  ? 44.293  33.373  242.964 1.00 203.19 ?  37  ILE I CB  1 
ATOM   17666 C CG1 . ILE J  6 37  ? 43.918  34.054  241.636 1.00 203.23 ?  37  ILE I CG1 1 
ATOM   17667 C CG2 . ILE J  6 37  ? 44.425  31.861  242.819 1.00 200.86 ?  37  ILE I CG2 1 
ATOM   17668 C CD1 . ILE J  6 37  ? 44.570  35.428  241.400 1.00 205.45 ?  37  ILE I CD1 1 
ATOM   17669 N N   . ARG J  6 38  ? 42.856  32.119  245.821 1.00 224.61 ?  38  ARG I N   1 
ATOM   17670 C CA  . ARG J  6 38  ? 43.069  31.412  247.074 1.00 219.21 ?  38  ARG I CA  1 
ATOM   17671 C C   . ARG J  6 38  ? 43.589  30.000  246.834 1.00 212.21 ?  38  ARG I C   1 
ATOM   17672 O O   . ARG J  6 38  ? 43.356  29.408  245.777 1.00 209.81 ?  38  ARG I O   1 
ATOM   17673 C CB  . ARG J  6 38  ? 41.716  31.277  247.782 1.00 218.62 ?  38  ARG I CB  1 
ATOM   17674 C CG  . ARG J  6 38  ? 41.692  30.862  249.222 1.00 209.28 ?  38  ARG I CG  1 
ATOM   17675 C CD  . ARG J  6 38  ? 40.243  30.871  249.697 1.00 213.76 ?  38  ARG I CD  1 
ATOM   17676 N NE  . ARG J  6 38  ? 39.598  29.585  249.429 1.00 209.64 ?  38  ARG I NE  1 
ATOM   17677 C CZ  . ARG J  6 38  ? 38.356  29.268  249.784 1.00 214.31 ?  38  ARG I CZ  1 
ATOM   17678 N NH1 . ARG J  6 38  ? 37.597  30.143  250.432 1.00 222.05 1  38  ARG I NH1 1 
ATOM   17679 N NH2 . ARG J  6 38  ? 37.869  28.073  249.482 1.00 208.37 ?  38  ARG I NH2 1 
ATOM   17680 N N   . GLN J  6 39  ? 44.317  29.466  247.828 1.00 223.50 ?  39  GLN I N   1 
ATOM   17681 C CA  . GLN J  6 39  ? 44.879  28.128  247.682 1.00 217.82 ?  39  GLN I CA  1 
ATOM   17682 C C   . GLN J  6 39  ? 45.099  27.397  249.001 1.00 213.37 ?  39  GLN I C   1 
ATOM   17683 O O   . GLN J  6 39  ? 46.006  27.765  249.761 1.00 211.83 ?  39  GLN I O   1 
ATOM   17684 C CB  . GLN J  6 39  ? 46.218  28.167  246.945 1.00 219.08 ?  39  GLN I CB  1 
ATOM   17685 C CG  . GLN J  6 39  ? 46.795  26.768  246.732 1.00 214.28 ?  39  GLN I CG  1 
ATOM   17686 C CD  . GLN J  6 39  ? 48.146  26.766  246.045 1.00 216.52 ?  39  GLN I CD  1 
ATOM   17687 O OE1 . GLN J  6 39  ? 48.744  27.816  245.816 1.00 225.20 ?  39  GLN I OE1 1 
ATOM   17688 N NE2 . GLN J  6 39  ? 48.639  25.575  245.720 1.00 209.13 ?  39  GLN I NE2 1 
ATOM   17689 N N   . PRO J  6 40  ? 44.303  26.384  249.325 1.00 225.14 ?  40  PRO I N   1 
ATOM   17690 C CA  . PRO J  6 40  ? 44.567  25.601  250.536 1.00 220.52 ?  40  PRO I CA  1 
ATOM   17691 C C   . PRO J  6 40  ? 45.883  24.843  250.400 1.00 217.36 ?  40  PRO I C   1 
ATOM   17692 O O   . PRO J  6 40  ? 46.440  24.687  249.311 1.00 218.32 ?  40  PRO I O   1 
ATOM   17693 C CB  . PRO J  6 40  ? 43.358  24.667  250.637 1.00 218.21 ?  40  PRO I CB  1 
ATOM   17694 C CG  . PRO J  6 40  ? 42.289  25.372  249.856 1.00 222.38 ?  40  PRO I CG  1 
ATOM   17695 C CD  . PRO J  6 40  ? 43.001  26.050  248.729 1.00 225.56 ?  40  PRO I CD  1 
ATOM   17696 N N   . LEU J  6 41  ? 46.380  24.356  251.533 1.00 225.06 ?  41  LEU I N   1 
ATOM   17697 C CA  . LEU J  6 41  ? 47.653  23.637  251.563 1.00 223.51 ?  41  LEU I CA  1 
ATOM   17698 C C   . LEU J  6 41  ? 47.518  22.274  250.889 1.00 218.01 ?  41  LEU I C   1 
ATOM   17699 O O   . LEU J  6 41  ? 46.838  21.379  251.403 1.00 217.19 ?  41  LEU I O   1 
ATOM   17700 C CB  . LEU J  6 41  ? 48.163  23.500  252.994 1.00 220.39 ?  41  LEU I CB  1 
ATOM   17701 C CG  . LEU J  6 41  ? 48.413  24.828  253.714 1.00 219.76 ?  41  LEU I CG  1 
ATOM   17702 C CD1 . LEU J  6 41  ? 47.262  25.194  254.637 1.00 216.24 ?  41  LEU I CD1 1 
ATOM   17703 C CD2 . LEU J  6 41  ? 49.738  24.792  254.470 1.00 217.35 ?  41  LEU I CD2 1 
ATOM   17704 N N   . GLY J  6 42  ? 48.167  22.114  249.736 1.00 212.28 ?  42  GLY I N   1 
ATOM   17705 C CA  . GLY J  6 42  ? 48.159  20.851  249.025 1.00 209.35 ?  42  GLY I CA  1 
ATOM   17706 C C   . GLY J  6 42  ? 46.990  20.651  248.093 1.00 210.61 ?  42  GLY I C   1 
ATOM   17707 O O   . GLY J  6 42  ? 46.650  19.503  247.783 1.00 208.72 ?  42  GLY I O   1 
ATOM   17708 N N   . LYS J  6 43  ? 46.366  21.731  247.638 1.00 207.26 ?  43  LYS I N   1 
ATOM   17709 C CA  . LYS J  6 43  ? 45.234  21.694  246.729 1.00 208.36 ?  43  LYS I CA  1 
ATOM   17710 C C   . LYS J  6 43  ? 45.489  22.647  245.570 1.00 213.23 ?  43  LYS I C   1 
ATOM   17711 O O   . LYS J  6 43  ? 46.456  23.413  245.563 1.00 216.37 ?  43  LYS I O   1 
ATOM   17712 C CB  . LYS J  6 43  ? 43.927  22.046  247.447 1.00 208.70 ?  43  LYS I CB  1 
ATOM   17713 C CG  . LYS J  6 43  ? 43.547  21.034  248.508 1.00 204.38 ?  43  LYS I CG  1 
ATOM   17714 C CD  . LYS J  6 43  ? 43.296  19.663  247.900 1.00 200.93 ?  43  LYS I CD  1 
ATOM   17715 C CE  . LYS J  6 43  ? 42.130  19.696  246.927 1.00 202.59 ?  43  LYS I CE  1 
ATOM   17716 N NZ  . LYS J  6 43  ? 41.860  18.356  246.336 1.00 199.26 1  43  LYS I NZ  1 
ATOM   17717 N N   . GLN J  6 44  ? 44.613  22.580  244.572 1.00 223.78 ?  44  GLN I N   1 
ATOM   17718 C CA  . GLN J  6 44  ? 44.766  23.443  243.414 1.00 227.18 ?  44  GLN I CA  1 
ATOM   17719 C C   . GLN J  6 44  ? 44.183  24.836  243.666 1.00 233.13 ?  44  GLN I C   1 
ATOM   17720 O O   . GLN J  6 44  ? 43.205  24.990  244.402 1.00 233.04 ?  44  GLN I O   1 
ATOM   17721 C CB  . GLN J  6 44  ? 44.117  22.816  242.179 1.00 221.30 ?  44  GLN I CB  1 
ATOM   17722 C CG  . GLN J  6 44  ? 42.619  22.563  242.257 1.00 217.37 ?  44  GLN I CG  1 
ATOM   17723 C CD  . GLN J  6 44  ? 42.274  21.248  242.931 1.00 216.16 ?  44  GLN I CD  1 
ATOM   17724 O OE1 . GLN J  6 44  ? 43.068  20.696  243.692 1.00 216.25 ?  44  GLN I OE1 1 
ATOM   17725 N NE2 . GLN J  6 44  ? 41.089  20.726  242.631 1.00 212.36 ?  44  GLN I NE2 1 
ATOM   17726 N N   . PRO J  6 45  ? 44.794  25.862  243.067 1.00 219.51 ?  45  PRO I N   1 
ATOM   17727 C CA  . PRO J  6 45  ? 44.338  27.245  243.268 1.00 222.08 ?  45  PRO I CA  1 
ATOM   17728 C C   . PRO J  6 45  ? 42.881  27.455  242.890 1.00 224.06 ?  45  PRO I C   1 
ATOM   17729 O O   . PRO J  6 45  ? 42.409  26.972  241.858 1.00 223.89 ?  45  PRO I O   1 
ATOM   17730 C CB  . PRO J  6 45  ? 45.267  28.056  242.359 1.00 228.97 ?  45  PRO I CB  1 
ATOM   17731 C CG  . PRO J  6 45  ? 46.484  27.223  242.230 1.00 227.85 ?  45  PRO I CG  1 
ATOM   17732 C CD  . PRO J  6 45  ? 46.000  25.801  242.226 1.00 220.11 ?  45  PRO I CD  1 
ATOM   17733 N N   . GLU J  6 46  ? 42.170  28.192  243.743 1.00 214.14 ?  46  GLU I N   1 
ATOM   17734 C CA  . GLU J  6 46  ? 40.761  28.493  243.533 1.00 218.92 ?  46  GLU I CA  1 
ATOM   17735 C C   . GLU J  6 46  ? 40.582  29.984  243.262 1.00 222.69 ?  46  GLU I C   1 
ATOM   17736 O O   . GLU J  6 46  ? 40.942  30.825  244.095 1.00 223.53 ?  46  GLU I O   1 
ATOM   17737 C CB  . GLU J  6 46  ? 39.956  28.056  244.760 1.00 220.46 ?  46  GLU I CB  1 
ATOM   17738 C CG  . GLU J  6 46  ? 38.451  28.251  244.675 1.00 225.08 ?  46  GLU I CG  1 
ATOM   17739 C CD  . GLU J  6 46  ? 37.742  27.739  245.917 1.00 226.94 ?  46  GLU I CD  1 
ATOM   17740 O OE1 . GLU J  6 46  ? 38.365  26.950  246.659 1.00 223.64 ?  46  GLU I OE1 1 
ATOM   17741 O OE2 . GLU J  6 46  ? 36.567  28.101  246.145 1.00 231.96 -1 46  GLU I OE2 1 
ATOM   17742 N N   . TRP J  6 47  ? 40.023  30.289  242.089 1.00 205.46 ?  47  TRP I N   1 
ATOM   17743 C CA  . TRP J  6 47  ? 39.757  31.657  241.652 1.00 209.66 ?  47  TRP I CA  1 
ATOM   17744 C C   . TRP J  6 47  ? 38.616  32.267  242.458 1.00 214.74 ?  47  TRP I C   1 
ATOM   17745 O O   . TRP J  6 47  ? 37.521  31.699  242.519 1.00 216.85 ?  47  TRP I O   1 
ATOM   17746 C CB  . TRP J  6 47  ? 39.418  31.690  240.162 1.00 211.11 ?  47  TRP I CB  1 
ATOM   17747 C CG  . TRP J  6 47  ? 39.523  33.067  239.548 1.00 214.45 ?  47  TRP I CG  1 
ATOM   17748 C CD1 . TRP J  6 47  ? 40.001  34.203  240.142 1.00 215.74 ?  47  TRP I CD1 1 
ATOM   17749 C CD2 . TRP J  6 47  ? 39.109  33.451  238.231 1.00 217.28 ?  47  TRP I CD2 1 
ATOM   17750 N NE1 . TRP J  6 47  ? 39.930  35.262  239.267 1.00 219.35 ?  47  TRP I NE1 1 
ATOM   17751 C CE2 . TRP J  6 47  ? 39.381  34.827  238.089 1.00 220.26 ?  47  TRP I CE2 1 
ATOM   17752 C CE3 . TRP J  6 47  ? 38.539  32.762  237.156 1.00 217.66 ?  47  TRP I CE3 1 
ATOM   17753 C CZ2 . TRP J  6 47  ? 39.103  35.526  236.914 1.00 223.52 ?  47  TRP I CZ2 1 
ATOM   17754 C CZ3 . TRP J  6 47  ? 38.264  33.457  235.992 1.00 220.62 ?  47  TRP I CZ3 1 
ATOM   17755 C CH2 . TRP J  6 47  ? 38.546  34.824  235.880 1.00 223.43 ?  47  TRP I CH2 1 
ATOM   17756 N N   . ILE J  6 48  ? 38.861  33.417  243.076 1.00 209.53 ?  48  ILE I N   1 
ATOM   17757 C CA  . ILE J  6 48  ? 37.826  34.042  243.898 1.00 210.63 ?  48  ILE I CA  1 
ATOM   17758 C C   . ILE J  6 48  ? 36.920  34.967  243.082 1.00 211.16 ?  48  ILE I C   1 
ATOM   17759 O O   . ILE J  6 48  ? 35.696  34.926  243.227 1.00 210.76 ?  48  ILE I O   1 
ATOM   17760 C CB  . ILE J  6 48  ? 38.472  34.785  245.085 1.00 212.79 ?  48  ILE I CB  1 
ATOM   17761 C CG1 . ILE J  6 48  ? 39.412  33.864  245.868 1.00 212.28 ?  48  ILE I CG1 1 
ATOM   17762 C CG2 . ILE J  6 48  ? 37.412  35.333  246.011 1.00 213.86 ?  48  ILE I CG2 1 
ATOM   17763 C CD1 . ILE J  6 48  ? 40.121  34.562  247.020 1.00 214.40 ?  48  ILE I CD1 1 
ATOM   17764 N N   . GLY J  6 49  ? 37.477  35.792  242.211 1.00 211.45 ?  49  GLY I N   1 
ATOM   17765 C CA  . GLY J  6 49  ? 36.688  36.697  241.399 1.00 212.03 ?  49  GLY I CA  1 
ATOM   17766 C C   . GLY J  6 49  ? 37.531  37.855  240.931 1.00 213.83 ?  49  GLY I C   1 
ATOM   17767 O O   . GLY J  6 49  ? 38.616  38.120  241.451 1.00 214.98 ?  49  GLY I O   1 
ATOM   17768 N N   . TYR J  6 50  ? 37.023  38.561  239.920 1.00 229.17 ?  50  TYR I N   1 
ATOM   17769 C CA  . TYR J  6 50  ? 37.727  39.708  239.364 1.00 230.98 ?  50  TYR I CA  1 
ATOM   17770 C C   . TYR J  6 50  ? 36.914  40.976  239.580 1.00 234.80 ?  50  TYR I C   1 
ATOM   17771 O O   . TYR J  6 50  ? 35.680  40.954  239.504 1.00 234.41 ?  50  TYR I O   1 
ATOM   17772 C CB  . TYR J  6 50  ? 38.002  39.504  237.864 1.00 229.59 ?  50  TYR I CB  1 
ATOM   17773 C CG  . TYR J  6 50  ? 36.775  39.368  236.975 1.00 229.86 ?  50  TYR I CG  1 
ATOM   17774 C CD1 . TYR J  6 50  ? 36.156  38.137  236.778 1.00 227.45 ?  50  TYR I CD1 1 
ATOM   17775 C CD2 . TYR J  6 50  ? 36.270  40.468  236.291 1.00 231.01 ?  50  TYR I CD2 1 
ATOM   17776 C CE1 . TYR J  6 50  ? 35.052  38.016  235.950 1.00 226.29 ?  50  TYR I CE1 1 
ATOM   17777 C CE2 . TYR J  6 50  ? 35.170  40.355  235.461 1.00 229.44 ?  50  TYR I CE2 1 
ATOM   17778 C CZ  . TYR J  6 50  ? 34.566  39.128  235.295 1.00 226.97 ?  50  TYR I CZ  1 
ATOM   17779 O OH  . TYR J  6 50  ? 33.471  39.010  234.471 1.00 225.34 ?  50  TYR I OH  1 
ATOM   17780 N N   . VAL J  6 51  ? 37.618  42.082  239.838 1.00 235.06 ?  51  VAL I N   1 
ATOM   17781 C CA  . VAL J  6 51  ? 37.007  43.385  240.077 1.00 239.36 ?  51  VAL I CA  1 
ATOM   17782 C C   . VAL J  6 51  ? 37.631  44.438  239.164 1.00 240.06 ?  51  VAL I C   1 
ATOM   17783 O O   . VAL J  6 51  ? 38.844  44.433  238.925 1.00 240.35 ?  51  VAL I O   1 
ATOM   17784 C CB  . VAL J  6 51  ? 37.139  43.790  241.565 1.00 242.79 ?  51  VAL I CB  1 
ATOM   17785 C CG1 . VAL J  6 51  ? 38.604  43.810  242.000 1.00 241.17 ?  51  VAL I CG1 1 
ATOM   17786 C CG2 . VAL J  6 51  ? 36.466  45.135  241.833 1.00 248.93 ?  51  VAL I CG2 1 
ATOM   17787 N N   . HIS J  6 52  ? 36.791  45.333  238.646 1.00 235.12 ?  52  HIS I N   1 
ATOM   17788 C CA  . HIS J  6 52  ? 37.220  46.409  237.765 1.00 237.25 ?  52  HIS I CA  1 
ATOM   17789 C C   . HIS J  6 52  ? 36.300  47.606  237.951 1.00 239.50 ?  52  HIS I C   1 
ATOM   17790 O O   . HIS J  6 52  ? 35.214  47.496  238.527 1.00 238.81 ?  52  HIS I O   1 
ATOM   17791 C CB  . HIS J  6 52  ? 37.238  45.985  236.292 1.00 234.72 ?  52  HIS I CB  1 
ATOM   17792 C CG  . HIS J  6 52  ? 37.845  47.008  235.382 1.00 236.85 ?  52  HIS I CG  1 
ATOM   17793 N ND1 . HIS J  6 52  ? 37.083  47.880  234.634 1.00 237.57 ?  52  HIS I ND1 1 
ATOM   17794 C CD2 . HIS J  6 52  ? 39.137  47.314  235.115 1.00 238.82 ?  52  HIS I CD2 1 
ATOM   17795 C CE1 . HIS J  6 52  ? 37.879  48.671  233.938 1.00 239.90 ?  52  HIS I CE1 1 
ATOM   17796 N NE2 . HIS J  6 52  ? 39.130  48.349  234.211 1.00 240.73 ?  52  HIS I NE2 1 
ATOM   17797 N N   . ASP J  6 53  ? 36.758  48.762  237.476 1.00 255.85 ?  53  ASP I N   1 
ATOM   17798 C CA  . ASP J  6 53  ? 35.963  49.976  237.553 1.00 263.67 ?  53  ASP I CA  1 
ATOM   17799 C C   . ASP J  6 53  ? 34.765  49.861  236.606 1.00 265.32 ?  53  ASP I C   1 
ATOM   17800 O O   . ASP J  6 53  ? 34.608  48.883  235.869 1.00 260.73 ?  53  ASP I O   1 
ATOM   17801 C CB  . ASP J  6 53  ? 36.821  51.194  237.211 1.00 269.06 ?  53  ASP I CB  1 
ATOM   17802 C CG  . ASP J  6 53  ? 36.290  52.481  237.824 1.00 277.22 ?  53  ASP I CG  1 
ATOM   17803 O OD1 . ASP J  6 53  ? 35.056  52.619  237.956 1.00 280.93 ?  53  ASP I OD1 1 
ATOM   17804 O OD2 . ASP J  6 53  ? 37.110  53.365  238.153 1.00 278.93 -1 53  ASP I OD2 1 
ATOM   17805 N N   . SER J  6 54  ? 33.911  50.885  236.626 1.00 274.38 ?  54  SER I N   1 
ATOM   17806 C CA  . SER J  6 54  ? 32.705  50.965  235.799 1.00 273.35 ?  54  SER I CA  1 
ATOM   17807 C C   . SER J  6 54  ? 31.721  49.830  236.074 1.00 269.91 ?  54  SER I C   1 
ATOM   17808 O O   . SER J  6 54  ? 30.882  49.513  235.226 1.00 266.39 ?  54  SER I O   1 
ATOM   17809 C CB  . SER J  6 54  ? 33.058  51.005  234.307 1.00 273.70 ?  54  SER I CB  1 
ATOM   17810 O OG  . SER J  6 54  ? 31.892  50.993  233.502 1.00 276.69 ?  54  SER I OG  1 
ATOM   17811 N N   . GLY J  6 55  ? 31.809  49.202  237.245 1.00 283.04 ?  55  GLY I N   1 
ATOM   17812 C CA  . GLY J  6 55  ? 30.870  48.180  237.660 1.00 279.64 ?  55  GLY I CA  1 
ATOM   17813 C C   . GLY J  6 55  ? 31.113  46.777  237.141 1.00 273.19 ?  55  GLY I C   1 
ATOM   17814 O O   . GLY J  6 55  ? 30.343  45.872  237.490 1.00 271.72 ?  55  GLY I O   1 
ATOM   17815 N N   . ASP J  6 56  ? 32.147  46.556  236.331 1.00 267.52 ?  56  ASP I N   1 
ATOM   17816 C CA  . ASP J  6 56  ? 32.454  45.229  235.790 1.00 257.46 ?  56  ASP I CA  1 
ATOM   17817 C C   . ASP J  6 56  ? 33.083  44.382  236.895 1.00 252.66 ?  56  ASP I C   1 
ATOM   17818 O O   . ASP J  6 56  ? 34.297  44.400  237.104 1.00 253.66 ?  56  ASP I O   1 
ATOM   17819 C CB  . ASP J  6 56  ? 33.369  45.346  234.576 1.00 251.72 ?  56  ASP I CB  1 
ATOM   17820 C CG  . ASP J  6 56  ? 33.633  44.010  233.916 1.00 243.55 ?  56  ASP I CG  1 
ATOM   17821 O OD1 . ASP J  6 56  ? 32.749  43.132  233.993 1.00 242.31 ?  56  ASP I OD1 1 
ATOM   17822 O OD2 . ASP J  6 56  ? 34.715  43.841  233.312 1.00 242.60 -1 56  ASP I OD2 1 
ATOM   17823 N N   . THR J  6 57  ? 32.250  43.632  237.618 1.00 247.06 ?  57  THR I N   1 
ATOM   17824 C CA  . THR J  6 57  ? 32.733  42.806  238.720 1.00 241.46 ?  57  THR I CA  1 
ATOM   17825 C C   . THR J  6 57  ? 31.891  41.542  238.826 1.00 237.18 ?  57  THR I C   1 
ATOM   17826 O O   . THR J  6 57  ? 30.664  41.625  238.929 1.00 245.44 ?  57  THR I O   1 
ATOM   17827 C CB  . THR J  6 57  ? 32.681  43.575  240.046 1.00 248.50 ?  57  THR I CB  1 
ATOM   17828 O OG1 . THR J  6 57  ? 33.427  44.793  239.929 1.00 244.18 ?  57  THR I OG1 1 
ATOM   17829 C CG2 . THR J  6 57  ? 33.264  42.737  241.175 1.00 243.85 ?  57  THR I CG2 1 
ATOM   17830 N N   . ASN J  6 58  ? 32.549  40.383  238.795 1.00 235.85 ?  58  ASN I N   1 
ATOM   17831 C CA  . ASN J  6 58  ? 31.882  39.094  238.916 1.00 235.06 ?  58  ASN I CA  1 
ATOM   17832 C C   . ASN J  6 58  ? 32.578  38.270  239.995 1.00 229.17 ?  58  ASN I C   1 
ATOM   17833 O O   . ASN J  6 58  ? 33.776  38.436  240.241 1.00 224.72 ?  58  ASN I O   1 
ATOM   17834 C CB  . ASN J  6 58  ? 31.850  38.348  237.576 1.00 228.01 ?  58  ASN I CB  1 
ATOM   17835 C CG  . ASN J  6 58  ? 30.926  37.150  237.605 1.00 227.16 ?  58  ASN I CG  1 
ATOM   17836 O OD1 . ASN J  6 58  ? 30.065  37.041  238.479 1.00 235.60 ?  58  ASN I OD1 1 
ATOM   17837 N ND2 . ASN J  6 58  ? 31.070  36.263  236.629 1.00 222.02 ?  58  ASN I ND2 1 
ATOM   17838 N N   . TYR J  6 59  ? 31.824  37.370  240.626 1.00 230.83 ?  59  TYR I N   1 
ATOM   17839 C CA  . TYR J  6 59  ? 32.298  36.547  241.739 1.00 225.90 ?  59  TYR I CA  1 
ATOM   17840 C C   . TYR J  6 59  ? 32.259  35.062  241.395 1.00 220.17 ?  59  TYR I C   1 
ATOM   17841 O O   . TYR J  6 59  ? 31.791  34.645  240.333 1.00 217.63 ?  59  TYR I O   1 
ATOM   17842 C CB  . TYR J  6 59  ? 31.475  36.768  243.012 1.00 232.81 ?  59  TYR I CB  1 
ATOM   17843 C CG  . TYR J  6 59  ? 31.488  38.165  243.571 1.00 242.61 ?  59  TYR I CG  1 
ATOM   17844 C CD1 . TYR J  6 59  ? 32.624  38.957  243.485 1.00 243.40 ?  59  TYR I CD1 1 
ATOM   17845 C CD2 . TYR J  6 59  ? 30.383  38.671  244.241 1.00 256.43 ?  59  TYR I CD2 1 
ATOM   17846 C CE1 . TYR J  6 59  ? 32.646  40.233  244.020 1.00 254.29 ?  59  TYR I CE1 1 
ATOM   17847 C CE2 . TYR J  6 59  ? 30.395  39.941  244.780 1.00 266.57 ?  59  TYR I CE2 1 
ATOM   17848 C CZ  . TYR J  6 59  ? 31.526  40.719  244.668 1.00 265.39 ?  59  TYR I CZ  1 
ATOM   17849 O OH  . TYR J  6 59  ? 31.526  41.985  245.209 1.00 272.53 ?  59  TYR I OH  1 
ATOM   17850 N N   . ASN J  6 60  ? 32.767  34.273  242.337 1.00 225.72 ?  60  ASN I N   1 
ATOM   17851 C CA  . ASN J  6 60  ? 32.766  32.822  242.228 1.00 221.11 ?  60  ASN I CA  1 
ATOM   17852 C C   . ASN J  6 60  ? 31.415  32.239  242.620 1.00 225.44 ?  60  ASN I C   1 
ATOM   17853 O O   . ASN J  6 60  ? 30.952  32.474  243.743 1.00 230.78 ?  60  ASN I O   1 
ATOM   17854 C CB  . ASN J  6 60  ? 33.851  32.233  243.129 1.00 217.64 ?  60  ASN I CB  1 
ATOM   17855 C CG  . ASN J  6 60  ? 34.133  30.762  242.841 1.00 212.02 ?  60  ASN I CG  1 
ATOM   17856 O OD1 . ASN J  6 60  ? 33.306  30.051  242.271 1.00 211.84 ?  60  ASN I OD1 1 
ATOM   17857 N ND2 . ASN J  6 60  ? 35.306  30.299  243.258 1.00 207.65 ?  60  ASN I ND2 1 
ATOM   17858 N N   . PRO J  6 61  ? 30.743  31.517  241.722 1.00 226.90 ?  61  PRO I N   1 
ATOM   17859 C CA  . PRO J  6 61  ? 29.440  30.913  242.047 1.00 230.08 ?  61  PRO I CA  1 
ATOM   17860 C C   . PRO J  6 61  ? 29.451  30.120  243.343 1.00 232.78 ?  61  PRO I C   1 
ATOM   17861 O O   . PRO J  6 61  ? 28.414  30.000  244.008 1.00 239.09 ?  61  PRO I O   1 
ATOM   17862 C CB  . PRO J  6 61  ? 29.169  30.018  240.832 1.00 221.27 ?  61  PRO I CB  1 
ATOM   17863 C CG  . PRO J  6 61  ? 29.853  30.724  239.710 1.00 217.90 ?  61  PRO I CG  1 
ATOM   17864 C CD  . PRO J  6 61  ? 31.096  31.334  240.305 1.00 219.28 ?  61  PRO I CD  1 
ATOM   17865 N N   . SER J  6 62  ? 30.606  29.561  243.712 1.00 226.62 ?  62  SER I N   1 
ATOM   17866 C CA  . SER J  6 62  ? 30.730  28.789  244.940 1.00 226.14 ?  62  SER I CA  1 
ATOM   17867 C C   . SER J  6 62  ? 30.769  29.685  246.171 1.00 233.28 ?  62  SER I C   1 
ATOM   17868 O O   . SER J  6 62  ? 30.378  29.252  247.261 1.00 236.73 ?  62  SER I O   1 
ATOM   17869 C CB  . SER J  6 62  ? 31.999  27.929  244.893 1.00 214.21 ?  62  SER I CB  1 
ATOM   17870 O OG  . SER J  6 62  ? 32.159  27.283  243.639 1.00 206.61 ?  62  SER I OG  1 
ATOM   17871 N N   . LEU J  6 63  ? 31.245  30.919  246.024 1.00 216.28 ?  63  LEU I N   1 
ATOM   17872 C CA  . LEU J  6 63  ? 31.344  31.871  247.124 1.00 221.61 ?  63  LEU I CA  1 
ATOM   17873 C C   . LEU J  6 63  ? 30.512  33.132  246.874 1.00 227.68 ?  63  LEU I C   1 
ATOM   17874 O O   . LEU J  6 63  ? 30.856  34.211  247.360 1.00 230.96 ?  63  LEU I O   1 
ATOM   17875 C CB  . LEU J  6 63  ? 32.810  32.218  247.375 1.00 217.95 ?  63  LEU I CB  1 
ATOM   17876 C CG  . LEU J  6 63  ? 33.714  30.980  247.457 1.00 211.72 ?  63  LEU I CG  1 
ATOM   17877 C CD1 . LEU J  6 63  ? 35.177  31.362  247.599 1.00 210.29 ?  63  LEU I CD1 1 
ATOM   17878 C CD2 . LEU J  6 63  ? 33.286  30.066  248.595 1.00 214.52 ?  63  LEU I CD2 1 
ATOM   17879 N N   . LYS J  6 64  ? 29.424  33.011  246.104 1.00 224.04 ?  64  LYS I N   1 
ATOM   17880 C CA  . LYS J  6 64  ? 28.634  34.180  245.708 1.00 223.10 ?  64  LYS I CA  1 
ATOM   17881 C C   . LYS J  6 64  ? 28.067  34.951  246.896 1.00 223.94 ?  64  LYS I C   1 
ATOM   17882 O O   . LYS J  6 64  ? 28.208  36.177  246.973 1.00 222.85 ?  64  LYS I O   1 
ATOM   17883 C CB  . LYS J  6 64  ? 27.467  33.769  244.812 1.00 223.31 ?  64  LYS I CB  1 
ATOM   17884 C CG  . LYS J  6 64  ? 27.462  34.350  243.418 1.00 221.44 ?  64  LYS I CG  1 
ATOM   17885 C CD  . LYS J  6 64  ? 26.226  33.844  242.694 1.00 221.95 ?  64  LYS I CD  1 
ATOM   17886 C CE  . LYS J  6 64  ? 25.584  34.953  241.874 1.00 220.58 ?  64  LYS I CE  1 
ATOM   17887 N NZ  . LYS J  6 64  ? 24.364  34.497  241.152 1.00 221.05 1  64  LYS I NZ  1 
ATOM   17888 N N   . SER J  6 65  ? 27.436  34.256  247.841 1.00 230.19 ?  65  SER I N   1 
ATOM   17889 C CA  . SER J  6 65  ? 26.735  34.929  248.927 1.00 236.84 ?  65  SER I CA  1 
ATOM   17890 C C   . SER J  6 65  ? 27.606  35.163  250.151 1.00 237.94 ?  65  SER I C   1 
ATOM   17891 O O   . SER J  6 65  ? 27.078  35.334  251.256 1.00 242.82 ?  65  SER I O   1 
ATOM   17892 C CB  . SER J  6 65  ? 25.485  34.132  249.315 1.00 239.51 ?  65  SER I CB  1 
ATOM   17893 O OG  . SER J  6 65  ? 25.820  32.822  249.739 1.00 236.37 ?  65  SER I OG  1 
ATOM   17894 N N   . ARG J  6 66  ? 28.924  35.179  249.979 1.00 238.85 ?  66  ARG I N   1 
ATOM   17895 C CA  . ARG J  6 66  ? 29.836  35.404  251.094 1.00 240.30 ?  66  ARG I CA  1 
ATOM   17896 C C   . ARG J  6 66  ? 30.952  36.384  250.774 1.00 240.36 ?  66  ARG I C   1 
ATOM   17897 O O   . ARG J  6 66  ? 31.528  36.947  251.712 1.00 243.01 ?  66  ARG I O   1 
ATOM   17898 C CB  . ARG J  6 66  ? 30.456  34.084  251.578 1.00 235.10 ?  66  ARG I CB  1 
ATOM   17899 C CG  . ARG J  6 66  ? 29.436  33.037  251.998 1.00 236.50 ?  66  ARG I CG  1 
ATOM   17900 C CD  . ARG J  6 66  ? 30.062  31.909  252.807 1.00 233.92 ?  66  ARG I CD  1 
ATOM   17901 N NE  . ARG J  6 66  ? 31.209  31.293  252.146 1.00 227.12 ?  66  ARG I NE  1 
ATOM   17902 C CZ  . ARG J  6 66  ? 32.469  31.455  252.538 1.00 224.38 ?  66  ARG I CZ  1 
ATOM   17903 N NH1 . ARG J  6 66  ? 32.742  32.212  253.591 1.00 228.05 1  66  ARG I NH1 1 
ATOM   17904 N NH2 . ARG J  6 66  ? 33.454  30.855  251.884 1.00 217.84 ?  66  ARG I NH2 1 
ATOM   17905 N N   . VAL J  6 67  ? 31.277  36.622  249.493 1.00 249.72 ?  67  VAL I N   1 
ATOM   17906 C CA  . VAL J  6 67  ? 32.394  37.481  249.119 1.00 248.22 ?  67  VAL I CA  1 
ATOM   17907 C C   . VAL J  6 67  ? 31.902  38.861  248.698 1.00 253.16 ?  67  VAL I C   1 
ATOM   17908 O O   . VAL J  6 67  ? 30.791  39.031  248.179 1.00 255.74 ?  67  VAL I O   1 
ATOM   17909 C CB  . VAL J  6 67  ? 33.213  36.813  247.989 1.00 240.14 ?  67  VAL I CB  1 
ATOM   17910 C CG1 . VAL J  6 67  ? 32.478  36.897  246.651 1.00 238.98 ?  67  VAL I CG1 1 
ATOM   17911 C CG2 . VAL J  6 67  ? 34.591  37.435  247.881 1.00 236.97 ?  67  VAL I CG2 1 
ATOM   17912 N N   . HIS J  6 68  ? 32.747  39.861  248.954 1.00 259.08 ?  68  HIS I N   1 
ATOM   17913 C CA  . HIS J  6 68  ? 32.526  41.256  248.591 1.00 260.37 ?  68  HIS I CA  1 
ATOM   17914 C C   . HIS J  6 68  ? 33.887  41.865  248.270 1.00 255.75 ?  68  HIS I C   1 
ATOM   17915 O O   . HIS J  6 68  ? 34.826  41.728  249.061 1.00 252.62 ?  68  HIS I O   1 
ATOM   17916 C CB  . HIS J  6 68  ? 31.782  42.010  249.701 1.00 265.81 ?  68  HIS I CB  1 
ATOM   17917 C CG  . HIS J  6 68  ? 30.401  41.479  249.961 1.00 270.23 ?  68  HIS I CG  1 
ATOM   17918 N ND1 . HIS J  6 68  ? 29.596  40.985  248.956 1.00 266.76 ?  68  HIS I ND1 1 
ATOM   17919 C CD2 . HIS J  6 68  ? 29.686  41.361  251.106 1.00 272.53 ?  68  HIS I CD2 1 
ATOM   17920 C CE1 . HIS J  6 68  ? 28.444  40.591  249.469 1.00 269.71 ?  68  HIS I CE1 1 
ATOM   17921 N NE2 . HIS J  6 68  ? 28.473  40.808  250.772 1.00 275.63 ?  68  HIS I NE2 1 
ATOM   17922 N N   . LEU J  6 69  ? 33.993  42.526  247.120 1.00 258.81 ?  69  LEU I N   1 
ATOM   17923 C CA  . LEU J  6 69  ? 35.219  43.160  246.646 1.00 253.93 ?  69  LEU I CA  1 
ATOM   17924 C C   . LEU J  6 69  ? 35.044  44.665  246.467 1.00 257.37 ?  69  LEU I C   1 
ATOM   17925 O O   . LEU J  6 69  ? 33.926  45.162  246.310 1.00 263.03 ?  69  LEU I O   1 
ATOM   17926 C CB  . LEU J  6 69  ? 35.680  42.534  245.325 1.00 248.25 ?  69  LEU I CB  1 
ATOM   17927 C CG  . LEU J  6 69  ? 36.125  41.074  245.409 1.00 242.59 ?  69  LEU I CG  1 
ATOM   17928 C CD1 . LEU J  6 69  ? 36.570  40.571  244.047 1.00 236.10 ?  69  LEU I CD1 1 
ATOM   17929 C CD2 . LEU J  6 69  ? 37.238  40.917  246.432 1.00 239.49 ?  69  LEU I CD2 1 
ATOM   17930 N N   . SER J  6 70  ? 36.164  45.395  246.499 1.00 266.27 ?  70  SER I N   1 
ATOM   17931 C CA  . SER J  6 70  ? 36.113  46.846  246.349 1.00 269.18 ?  70  SER I CA  1 
ATOM   17932 C C   . SER J  6 70  ? 37.464  47.371  245.873 1.00 263.64 ?  70  SER I C   1 
ATOM   17933 O O   . SER J  6 70  ? 38.497  46.710  246.011 1.00 258.06 ?  70  SER I O   1 
ATOM   17934 C CB  . SER J  6 70  ? 35.747  47.531  247.674 1.00 271.82 ?  70  SER I CB  1 
ATOM   17935 O OG  . SER J  6 70  ? 34.637  46.913  248.300 1.00 277.77 ?  70  SER I OG  1 
ATOM   17936 N N   . LEU J  6 71  ? 37.428  48.582  245.304 1.00 268.11 ?  71  LEU I N   1 
ATOM   17937 C CA  . LEU J  6 71  ? 38.603  49.279  244.788 1.00 265.30 ?  71  LEU I CA  1 
ATOM   17938 C C   . LEU J  6 71  ? 38.642  50.685  245.369 1.00 271.08 ?  71  LEU I C   1 
ATOM   17939 O O   . LEU J  6 71  ? 37.686  51.450  245.200 1.00 277.53 ?  71  LEU I O   1 
ATOM   17940 C CB  . LEU J  6 71  ? 38.581  49.339  243.259 1.00 262.69 ?  71  LEU I CB  1 
ATOM   17941 C CG  . LEU J  6 71  ? 38.712  48.002  242.528 1.00 255.42 ?  71  LEU I CG  1 
ATOM   17942 C CD1 . LEU J  6 71  ? 38.594  48.195  241.017 1.00 254.93 ?  71  LEU I CD1 1 
ATOM   17943 C CD2 . LEU J  6 71  ? 39.990  47.273  242.905 1.00 247.16 ?  71  LEU I CD2 1 
ATOM   17944 N N   . ASP J  6 72  ? 39.735  51.028  246.049 1.00 263.77 ?  72  ASP I N   1 
ATOM   17945 C CA  . ASP J  6 72  ? 39.931  52.355  246.638 1.00 267.45 ?  72  ASP I CA  1 
ATOM   17946 C C   . ASP J  6 72  ? 40.770  53.239  245.713 1.00 267.20 ?  72  ASP I C   1 
ATOM   17947 O O   . ASP J  6 72  ? 41.996  53.107  245.668 1.00 259.19 ?  72  ASP I O   1 
ATOM   17948 C CB  . ASP J  6 72  ? 40.582  52.220  248.011 1.00 262.74 ?  72  ASP I CB  1 
ATOM   17949 C CG  . ASP J  6 72  ? 40.399  53.453  248.876 1.00 270.22 ?  72  ASP I CG  1 
ATOM   17950 O OD1 . ASP J  6 72  ? 40.229  54.561  248.325 1.00 278.24 ?  72  ASP I OD1 1 
ATOM   17951 O OD2 . ASP J  6 72  ? 40.418  53.308  250.116 1.00 270.88 -1 72  ASP I OD2 1 
ATOM   17952 N N   . LYS J  6 73  ? 40.121  54.138  244.961 1.00 256.08 ?  73  LYS I N   1 
ATOM   17953 C CA  . LYS J  6 73  ? 40.885  54.986  244.048 1.00 253.64 ?  73  LYS I CA  1 
ATOM   17954 C C   . LYS J  6 73  ? 41.600  56.128  244.762 1.00 253.34 ?  73  LYS I C   1 
ATOM   17955 O O   . LYS J  6 73  ? 42.539  56.704  244.198 1.00 251.69 ?  73  LYS I O   1 
ATOM   17956 C CB  . LYS J  6 73  ? 39.988  55.592  242.964 1.00 255.07 ?  73  LYS I CB  1 
ATOM   17957 C CG  . LYS J  6 73  ? 39.259  54.604  242.075 1.00 256.28 ?  73  LYS I CG  1 
ATOM   17958 C CD  . LYS J  6 73  ? 38.404  55.345  241.055 1.00 255.15 ?  73  LYS I CD  1 
ATOM   17959 C CE  . LYS J  6 73  ? 37.359  56.212  241.731 1.00 258.90 ?  73  LYS I CE  1 
ATOM   17960 N NZ  . LYS J  6 73  ? 36.528  56.944  240.738 1.00 260.35 1  73  LYS I NZ  1 
ATOM   17961 N N   . SER J  6 74  ? 41.186  56.454  245.988 1.00 253.63 ?  74  SER I N   1 
ATOM   17962 C CA  . SER J  6 74  ? 41.800  57.530  246.761 1.00 254.36 ?  74  SER I CA  1 
ATOM   17963 C C   . SER J  6 74  ? 43.056  57.042  247.465 1.00 251.71 ?  74  SER I C   1 
ATOM   17964 O O   . SER J  6 74  ? 44.052  57.769  247.549 1.00 250.60 ?  74  SER I O   1 
ATOM   17965 C CB  . SER J  6 74  ? 40.801  58.101  247.770 1.00 260.88 ?  74  SER I CB  1 
ATOM   17966 O OG  . SER J  6 74  ? 40.363  57.109  248.680 1.00 263.76 ?  74  SER I OG  1 
ATOM   17967 N N   . LYS J  6 75  ? 43.019  55.810  247.964 1.00 249.79 ?  75  LYS I N   1 
ATOM   17968 C CA  . LYS J  6 75  ? 44.131  55.213  248.679 1.00 247.88 ?  75  LYS I CA  1 
ATOM   17969 C C   . LYS J  6 75  ? 44.936  54.289  247.781 1.00 243.94 ?  75  LYS I C   1 
ATOM   17970 O O   . LYS J  6 75  ? 45.974  53.772  248.208 1.00 241.95 ?  75  LYS I O   1 
ATOM   17971 C CB  . LYS J  6 75  ? 43.599  54.427  249.881 1.00 250.18 ?  75  LYS I CB  1 
ATOM   17972 C CG  . LYS J  6 75  ? 42.830  55.275  250.879 1.00 254.82 ?  75  LYS I CG  1 
ATOM   17973 C CD  . LYS J  6 75  ? 42.343  54.444  252.059 1.00 256.62 ?  75  LYS I CD  1 
ATOM   17974 C CE  . LYS J  6 75  ? 41.559  55.291  253.052 1.00 261.71 ?  75  LYS I CE  1 
ATOM   17975 N NZ  . LYS J  6 75  ? 42.238  55.395  254.374 1.00 263.41 1  75  LYS I NZ  1 
ATOM   17976 N N   . ASN J  6 76  ? 44.475  54.089  246.548 1.00 258.62 ?  76  ASN I N   1 
ATOM   17977 C CA  . ASN J  6 76  ? 45.130  53.263  245.539 1.00 251.75 ?  76  ASN I CA  1 
ATOM   17978 C C   . ASN J  6 76  ? 45.396  51.849  246.062 1.00 249.38 ?  76  ASN I C   1 
ATOM   17979 O O   . ASN J  6 76  ? 46.539  51.410  246.207 1.00 246.24 ?  76  ASN I O   1 
ATOM   17980 C CB  . ASN J  6 76  ? 46.409  53.951  245.057 1.00 250.46 ?  76  ASN I CB  1 
ATOM   17981 C CG  . ASN J  6 76  ? 46.957  53.334  243.799 1.00 250.37 ?  76  ASN I CG  1 
ATOM   17982 O OD1 . ASN J  6 76  ? 46.555  53.697  242.692 1.00 251.77 ?  76  ASN I OD1 1 
ATOM   17983 N ND2 . ASN J  6 76  ? 47.882  52.399  243.954 1.00 246.86 ?  76  ASN I ND2 1 
ATOM   17984 N N   . LEU J  6 77  ? 44.309  51.130  246.349 1.00 253.52 ?  77  LEU I N   1 
ATOM   17985 C CA  . LEU J  6 77  ? 44.428  49.766  246.846 1.00 253.79 ?  77  LEU I CA  1 
ATOM   17986 C C   . LEU J  6 77  ? 43.177  48.964  246.507 1.00 253.79 ?  77  LEU I C   1 
ATOM   17987 O O   . LEU J  6 77  ? 42.145  49.508  246.105 1.00 255.38 ?  77  LEU I O   1 
ATOM   17988 C CB  . LEU J  6 77  ? 44.685  49.740  248.361 1.00 255.33 ?  77  LEU I CB  1 
ATOM   17989 C CG  . LEU J  6 77  ? 43.787  50.529  249.321 1.00 256.51 ?  77  LEU I CG  1 
ATOM   17990 C CD1 . LEU J  6 77  ? 42.526  49.744  249.671 1.00 255.17 ?  77  LEU I CD1 1 
ATOM   17991 C CD2 . LEU J  6 77  ? 44.549  50.909  250.579 1.00 254.99 ?  77  LEU I CD2 1 
ATOM   17992 N N   . VAL J  6 78  ? 43.295  47.649  246.676 1.00 254.84 ?  78  VAL I N   1 
ATOM   17993 C CA  . VAL J  6 78  ? 42.222  46.693  246.429 1.00 253.37 ?  78  VAL I CA  1 
ATOM   17994 C C   . VAL J  6 78  ? 41.840  46.065  247.761 1.00 255.56 ?  78  VAL I C   1 
ATOM   17995 O O   . VAL J  6 78  ? 42.715  45.702  248.556 1.00 255.38 ?  78  VAL I O   1 
ATOM   17996 C CB  . VAL J  6 78  ? 42.649  45.608  245.422 1.00 247.44 ?  78  VAL I CB  1 
ATOM   17997 C CG1 . VAL J  6 78  ? 41.463  44.737  245.045 1.00 245.38 ?  78  VAL I CG1 1 
ATOM   17998 C CG2 . VAL J  6 78  ? 43.280  46.237  244.198 1.00 248.15 ?  78  VAL I CG2 1 
ATOM   17999 N N   . SER J  6 79  ? 40.539  45.940  248.009 1.00 253.96 ?  79  SER I N   1 
ATOM   18000 C CA  . SER J  6 79  ? 40.039  45.396  249.263 1.00 258.52 ?  79  SER I CA  1 
ATOM   18001 C C   . SER J  6 79  ? 39.321  44.071  249.022 1.00 260.63 ?  79  SER I C   1 
ATOM   18002 O O   . SER J  6 79  ? 38.953  43.736  247.893 1.00 258.40 ?  79  SER I O   1 
ATOM   18003 C CB  . SER J  6 79  ? 39.095  46.397  249.942 1.00 260.36 ?  79  SER I CB  1 
ATOM   18004 O OG  . SER J  6 79  ? 38.522  45.855  251.118 1.00 267.06 ?  79  SER I OG  1 
ATOM   18005 N N   . LEU J  6 80  ? 39.127  43.316  250.106 1.00 250.74 ?  80  LEU I N   1 
ATOM   18006 C CA  . LEU J  6 80  ? 38.438  42.033  250.042 1.00 252.09 ?  80  LEU I CA  1 
ATOM   18007 C C   . LEU J  6 80  ? 37.694  41.778  251.349 1.00 259.13 ?  80  LEU I C   1 
ATOM   18008 O O   . LEU J  6 80  ? 38.209  42.080  252.429 1.00 257.97 ?  80  LEU I O   1 
ATOM   18009 C CB  . LEU J  6 80  ? 39.443  40.908  249.760 1.00 245.00 ?  80  LEU I CB  1 
ATOM   18010 C CG  . LEU J  6 80  ? 38.928  39.471  249.717 1.00 245.26 ?  80  LEU I CG  1 
ATOM   18011 C CD1 . LEU J  6 80  ? 39.593  38.702  248.601 1.00 240.93 ?  80  LEU I CD1 1 
ATOM   18012 C CD2 . LEU J  6 80  ? 39.193  38.778  251.043 1.00 244.28 ?  80  LEU I CD2 1 
ATOM   18013 N N   . ARG J  6 81  ? 36.480  41.226  251.241 1.00 240.54 ?  81  ARG I N   1 
ATOM   18014 C CA  . ARG J  6 81  ? 35.644  40.901  252.395 1.00 246.69 ?  81  ARG I CA  1 
ATOM   18015 C C   . ARG J  6 81  ? 35.000  39.531  252.210 1.00 247.95 ?  81  ARG I C   1 
ATOM   18016 O O   . ARG J  6 81  ? 34.419  39.260  251.155 1.00 247.71 ?  81  ARG I O   1 
ATOM   18017 C CB  . ARG J  6 81  ? 34.586  41.994  252.598 1.00 252.65 ?  81  ARG I CB  1 
ATOM   18018 C CG  . ARG J  6 81  ? 35.195  43.285  253.141 1.00 256.33 ?  81  ARG I CG  1 
ATOM   18019 C CD  . ARG J  6 81  ? 34.185  44.395  253.359 1.00 261.66 ?  81  ARG I CD  1 
ATOM   18020 N NE  . ARG J  6 81  ? 33.141  44.036  254.307 1.00 264.40 ?  81  ARG I NE  1 
ATOM   18021 C CZ  . ARG J  6 81  ? 31.911  43.688  253.949 1.00 265.79 ?  81  ARG I CZ  1 
ATOM   18022 N NH1 . ARG J  6 81  ? 31.014  43.372  254.870 1.00 271.16 1  81  ARG I NH1 1 
ATOM   18023 N NH2 . ARG J  6 81  ? 31.580  43.663  252.666 1.00 264.88 ?  81  ARG I NH2 1 
ATOM   18024 N N   . LEU J  6 82  ? 35.102  38.673  253.230 1.00 226.68 ?  82  LEU I N   1 
ATOM   18025 C CA  . LEU J  6 82  ? 34.524  37.327  253.217 1.00 228.20 ?  82  LEU I CA  1 
ATOM   18026 C C   . LEU J  6 82  ? 33.757  37.073  254.510 1.00 230.18 ?  82  LEU I C   1 
ATOM   18027 O O   . LEU J  6 82  ? 34.371  36.839  255.555 1.00 231.06 ?  82  LEU I O   1 
ATOM   18028 C CB  . LEU J  6 82  ? 35.610  36.266  253.031 1.00 228.30 ?  82  LEU I CB  1 
ATOM   18029 C CG  . LEU J  6 82  ? 35.131  34.812  252.965 1.00 229.82 ?  82  LEU I CG  1 
ATOM   18030 C CD1 . LEU J  6 82  ? 34.148  34.599  251.827 1.00 229.47 ?  82  LEU I CD1 1 
ATOM   18031 C CD2 . LEU J  6 82  ? 36.311  33.856  252.849 1.00 229.85 ?  82  LEU I CD2 1 
ATOM   18032 N N   . THR J  6 83  A 32.427  37.079  254.440 1.00 222.10 ?  82  THR I N   1 
ATOM   18033 C CA  . THR J  6 83  A 31.601  36.868  255.622 1.00 228.79 ?  82  THR I CA  1 
ATOM   18034 C C   . THR J  6 83  A 31.322  35.381  255.826 1.00 231.05 ?  82  THR I C   1 
ATOM   18035 O O   . THR J  6 83  A 31.167  34.622  254.866 1.00 227.78 ?  82  THR I O   1 
ATOM   18036 C CB  . THR J  6 83  A 30.278  37.630  255.501 1.00 231.61 ?  82  THR I CB  1 
ATOM   18037 O OG1 . THR J  6 83  A 29.548  37.149  254.365 1.00 231.13 ?  82  THR I OG1 1 
ATOM   18038 C CG2 . THR J  6 83  A 30.528  39.126  255.340 1.00 233.52 ?  82  THR I CG2 1 
ATOM   18039 N N   . GLY J  6 84  B 31.246  34.972  257.094 1.00 223.72 ?  82  GLY I N   1 
ATOM   18040 C CA  . GLY J  6 84  B 30.983  33.585  257.443 1.00 225.48 ?  82  GLY I CA  1 
ATOM   18041 C C   . GLY J  6 84  B 32.059  32.592  257.043 1.00 225.31 ?  82  GLY I C   1 
ATOM   18042 O O   . GLY J  6 84  B 31.802  31.676  256.257 1.00 225.50 ?  82  GLY I O   1 
ATOM   18043 N N   . VAL J  6 85  C 33.262  32.757  257.585 1.00 225.93 ?  82  VAL I N   1 
ATOM   18044 C CA  . VAL J  6 85  C 34.398  31.900  257.259 1.00 225.69 ?  82  VAL I CA  1 
ATOM   18045 C C   . VAL J  6 85  C 34.354  30.614  258.078 1.00 227.71 ?  82  VAL I C   1 
ATOM   18046 O O   . VAL J  6 85  C 33.819  30.572  259.191 1.00 229.20 ?  82  VAL I O   1 
ATOM   18047 C CB  . VAL J  6 85  C 35.721  32.657  257.481 1.00 224.44 ?  82  VAL I CB  1 
ATOM   18048 C CG1 . VAL J  6 85  C 35.859  33.787  256.470 1.00 222.32 ?  82  VAL I CG1 1 
ATOM   18049 C CG2 . VAL J  6 85  C 35.792  33.184  258.903 1.00 225.36 ?  82  VAL I CG2 1 
ATOM   18050 N N   . THR J  6 86  ? 34.915  29.546  257.510 1.00 235.81 ?  83  THR I N   1 
ATOM   18051 C CA  . THR J  6 86  ? 35.001  28.255  258.184 1.00 239.56 ?  83  THR I CA  1 
ATOM   18052 C C   . THR J  6 86  ? 36.426  27.726  258.093 1.00 234.00 ?  83  THR I C   1 
ATOM   18053 O O   . THR J  6 86  ? 37.335  28.456  257.687 1.00 227.97 ?  83  THR I O   1 
ATOM   18054 C CB  . THR J  6 86  ? 34.036  27.240  257.567 1.00 242.21 ?  83  THR I CB  1 
ATOM   18055 O OG1 . THR J  6 86  ? 34.300  27.121  256.162 1.00 235.44 ?  83  THR I OG1 1 
ATOM   18056 C CG2 . THR J  6 86  ? 32.593  27.664  257.782 1.00 248.83 ?  83  THR I CG2 1 
ATOM   18057 N N   . ALA J  6 87  ? 36.629  26.450  258.428 1.00 246.86 ?  84  ALA I N   1 
ATOM   18058 C CA  . ALA J  6 87  ? 37.970  25.884  258.375 1.00 238.79 ?  84  ALA I CA  1 
ATOM   18059 C C   . ALA J  6 87  ? 38.416  25.614  256.947 1.00 227.71 ?  84  ALA I C   1 
ATOM   18060 O O   . ALA J  6 87  ? 39.614  25.428  256.710 1.00 224.36 ?  84  ALA I O   1 
ATOM   18061 C CB  . ALA J  6 87  ? 38.041  24.592  259.191 1.00 244.04 ?  84  ALA I CB  1 
ATOM   18062 N N   . ALA J  6 88  ? 37.477  25.589  255.998 1.00 239.96 ?  85  ALA I N   1 
ATOM   18063 C CA  . ALA J  6 88  ? 37.805  25.328  254.604 1.00 233.55 ?  85  ALA I CA  1 
ATOM   18064 C C   . ALA J  6 88  ? 38.372  26.563  253.924 1.00 231.05 ?  85  ALA I C   1 
ATOM   18065 O O   . ALA J  6 88  ? 38.987  26.444  252.858 1.00 225.01 ?  85  ALA I O   1 
ATOM   18066 C CB  . ALA J  6 88  ? 36.570  24.840  253.844 1.00 235.86 ?  85  ALA I CB  1 
ATOM   18067 N N   . ASP J  6 89  ? 38.176  27.740  254.519 1.00 236.00 ?  86  ASP I N   1 
ATOM   18068 C CA  . ASP J  6 89  ? 38.652  28.998  253.962 1.00 233.48 ?  86  ASP I CA  1 
ATOM   18069 C C   . ASP J  6 89  ? 40.086  29.304  254.365 1.00 231.02 ?  86  ASP I C   1 
ATOM   18070 O O   . ASP J  6 89  ? 40.638  30.315  253.920 1.00 224.87 ?  86  ASP I O   1 
ATOM   18071 C CB  . ASP J  6 89  ? 37.754  30.155  254.418 1.00 236.10 ?  86  ASP I CB  1 
ATOM   18072 C CG  . ASP J  6 89  ? 36.348  30.058  253.871 1.00 239.15 ?  86  ASP I CG  1 
ATOM   18073 O OD1 . ASP J  6 89  ? 36.177  29.517  252.761 1.00 235.35 ?  86  ASP I OD1 1 
ATOM   18074 O OD2 . ASP J  6 89  ? 35.413  30.531  254.553 1.00 243.06 -1 86  ASP I OD2 1 
ATOM   18075 N N   . SER J  6 90  ? 40.696  28.453  255.185 1.00 241.08 ?  87  SER I N   1 
ATOM   18076 C CA  . SER J  6 90  ? 42.079  28.617  255.630 1.00 235.76 ?  87  SER I CA  1 
ATOM   18077 C C   . SER J  6 90  ? 43.007  28.335  254.455 1.00 227.32 ?  87  SER I C   1 
ATOM   18078 O O   . SER J  6 90  ? 43.236  27.177  254.098 1.00 226.39 ?  87  SER I O   1 
ATOM   18079 C CB  . SER J  6 90  ? 42.372  27.701  256.814 1.00 238.72 ?  87  SER I CB  1 
ATOM   18080 O OG  . SER J  6 90  ? 41.906  26.381  256.586 1.00 241.25 ?  87  SER I OG  1 
ATOM   18081 N N   . ALA J  6 91  ? 43.549  29.386  253.842 1.00 218.37 ?  88  ALA I N   1 
ATOM   18082 C CA  . ALA J  6 91  ? 44.410  29.211  252.676 1.00 214.34 ?  88  ALA I CA  1 
ATOM   18083 C C   . ALA J  6 91  ? 45.318  30.432  252.526 1.00 208.89 ?  88  ALA I C   1 
ATOM   18084 O O   . ALA J  6 91  ? 45.384  31.290  253.414 1.00 206.91 ?  88  ALA I O   1 
ATOM   18085 C CB  . ALA J  6 91  ? 43.560  28.964  251.429 1.00 216.39 ?  88  ALA I CB  1 
ATOM   18086 N N   . ILE J  6 92  ? 46.030  30.501  251.397 1.00 212.52 ?  89  ILE I N   1 
ATOM   18087 C CA  . ILE J  6 92  ? 46.935  31.599  251.053 1.00 206.88 ?  89  ILE I CA  1 
ATOM   18088 C C   . ILE J  6 92  ? 46.317  32.440  249.933 1.00 207.32 ?  89  ILE I C   1 
ATOM   18089 O O   . ILE J  6 92  ? 46.204  31.976  248.792 1.00 207.24 ?  89  ILE I O   1 
ATOM   18090 C CB  . ILE J  6 92  ? 48.311  31.058  250.641 1.00 204.15 ?  89  ILE I CB  1 
ATOM   18091 C CG1 . ILE J  6 92  ? 48.869  30.144  251.735 1.00 206.34 ?  89  ILE I CG1 1 
ATOM   18092 C CG2 . ILE J  6 92  ? 49.280  32.197  250.386 1.00 201.00 ?  89  ILE I CG2 1 
ATOM   18093 C CD1 . ILE J  6 92  ? 50.209  29.525  251.394 1.00 205.03 ?  89  ILE I CD1 1 
ATOM   18094 N N   . TYR J  6 93  ? 45.907  33.669  250.261 1.00 204.93 ?  90  TYR I N   1 
ATOM   18095 C CA  . TYR J  6 93  ? 45.226  34.576  249.334 1.00 208.05 ?  90  TYR I CA  1 
ATOM   18096 C C   . TYR J  6 93  ? 46.178  35.464  248.529 1.00 204.52 ?  90  TYR I C   1 
ATOM   18097 O O   . TYR J  6 93  ? 46.984  36.197  249.114 1.00 203.07 ?  90  TYR I O   1 
ATOM   18098 C CB  . TYR J  6 93  ? 44.272  35.469  250.124 1.00 214.75 ?  90  TYR I CB  1 
ATOM   18099 C CG  . TYR J  6 93  ? 43.136  34.721  250.765 1.00 221.96 ?  90  TYR I CG  1 
ATOM   18100 C CD1 . TYR J  6 93  ? 43.316  34.038  251.963 1.00 220.38 ?  90  TYR I CD1 1 
ATOM   18101 C CD2 . TYR J  6 93  ? 41.882  34.705  250.182 1.00 226.44 ?  90  TYR I CD2 1 
ATOM   18102 C CE1 . TYR J  6 93  ? 42.275  33.348  252.550 1.00 225.54 ?  90  TYR I CE1 1 
ATOM   18103 C CE2 . TYR J  6 93  ? 40.838  34.026  250.761 1.00 232.58 ?  90  TYR I CE2 1 
ATOM   18104 C CZ  . TYR J  6 93  ? 41.037  33.346  251.944 1.00 233.33 ?  90  TYR I CZ  1 
ATOM   18105 O OH  . TYR J  6 93  ? 39.987  32.665  252.516 1.00 239.12 ?  90  TYR I OH  1 
ATOM   18106 N N   . TYR J  6 94  ? 46.088  35.401  247.196 1.00 213.73 ?  91  TYR I N   1 
ATOM   18107 C CA  . TYR J  6 94  ? 46.917  36.209  246.307 1.00 209.77 ?  91  TYR I CA  1 
ATOM   18108 C C   . TYR J  6 94  ? 46.095  37.293  245.610 1.00 213.12 ?  91  TYR I C   1 
ATOM   18109 O O   . TYR J  6 94  ? 44.901  37.119  245.351 1.00 212.45 ?  91  TYR I O   1 
ATOM   18110 C CB  . TYR J  6 94  ? 47.618  35.348  245.252 1.00 204.16 ?  91  TYR I CB  1 
ATOM   18111 C CG  . TYR J  6 94  ? 48.538  34.293  245.816 1.00 199.30 ?  91  TYR I CG  1 
ATOM   18112 C CD1 . TYR J  6 94  ? 49.453  34.616  246.802 1.00 201.45 ?  91  TYR I CD1 1 
ATOM   18113 C CD2 . TYR J  6 94  ? 48.508  32.986  245.355 1.00 200.36 ?  91  TYR I CD2 1 
ATOM   18114 C CE1 . TYR J  6 94  ? 50.311  33.673  247.324 1.00 202.84 ?  91  TYR I CE1 1 
ATOM   18115 C CE2 . TYR J  6 94  ? 49.365  32.027  245.874 1.00 198.05 ?  91  TYR I CE2 1 
ATOM   18116 C CZ  . TYR J  6 94  ? 50.265  32.378  246.860 1.00 200.77 ?  91  TYR I CZ  1 
ATOM   18117 O OH  . TYR J  6 94  ? 51.124  31.437  247.382 1.00 208.64 ?  91  TYR I OH  1 
ATOM   18118 N N   . CYS J  6 95  ? 46.759  38.416  245.312 1.00 222.99 ?  92  CYS I N   1 
ATOM   18119 C CA  . CYS J  6 95  ? 46.220  39.543  244.547 1.00 225.45 ?  92  CYS I CA  1 
ATOM   18120 C C   . CYS J  6 95  ? 47.083  39.752  243.304 1.00 224.77 ?  92  CYS I C   1 
ATOM   18121 O O   . CYS J  6 95  ? 48.290  39.985  243.425 1.00 224.01 ?  92  CYS I O   1 
ATOM   18122 C CB  . CYS J  6 95  ? 46.124  40.819  245.392 1.00 230.08 ?  92  CYS I CB  1 
ATOM   18123 S SG  . CYS J  6 95  ? 47.641  41.633  245.869 1.00 253.69 ?  92  CYS I SG  1 
ATOM   18124 N N   . ALA J  6 96  ? 46.487  39.656  242.116 1.00 216.13 ?  93  ALA I N   1 
ATOM   18125 C CA  . ALA J  6 96  ? 47.254  39.753  240.876 1.00 216.24 ?  93  ALA I CA  1 
ATOM   18126 C C   . ALA J  6 96  ? 46.535  40.597  239.831 1.00 221.40 ?  93  ALA I C   1 
ATOM   18127 O O   . ALA J  6 96  ? 45.303  40.612  239.765 1.00 224.62 ?  93  ALA I O   1 
ATOM   18128 C CB  . ALA J  6 96  ? 47.549  38.369  240.286 1.00 212.89 ?  93  ALA I CB  1 
ATOM   18129 N N   . THR J  6 97  ? 47.324  41.315  239.023 1.00 210.18 ?  94  THR I N   1 
ATOM   18130 C CA  . THR J  6 97  ? 46.751  42.093  237.935 1.00 216.51 ?  94  THR I CA  1 
ATOM   18131 C C   . THR J  6 97  ? 46.143  41.133  236.922 1.00 218.49 ?  94  THR I C   1 
ATOM   18132 O O   . THR J  6 97  ? 46.534  39.966  236.821 1.00 213.45 ?  94  THR I O   1 
ATOM   18133 C CB  . THR J  6 97  ? 47.805  42.956  237.226 1.00 217.02 ?  94  THR I CB  1 
ATOM   18134 O OG1 . THR J  6 97  ? 48.800  42.119  236.626 1.00 215.84 ?  94  THR I OG1 1 
ATOM   18135 C CG2 . THR J  6 97  ? 48.501  43.887  238.195 1.00 217.82 ?  94  THR I CG2 1 
ATOM   18136 N N   . THR J  6 98  ? 45.184  41.634  236.147 1.00 212.66 ?  95  THR I N   1 
ATOM   18137 C CA  . THR J  6 98  ? 44.477  40.798  235.183 1.00 213.21 ?  95  THR I CA  1 
ATOM   18138 C C   . THR J  6 98  ? 44.329  41.473  233.826 1.00 219.38 ?  95  THR I C   1 
ATOM   18139 O O   . THR J  6 98  ? 43.814  42.591  233.735 1.00 224.84 ?  95  THR I O   1 
ATOM   18140 C CB  . THR J  6 98  ? 43.096  40.415  235.733 1.00 211.11 ?  95  THR I CB  1 
ATOM   18141 O OG1 . THR J  6 98  ? 43.242  39.769  237.003 1.00 206.99 ?  95  THR I OG1 1 
ATOM   18142 C CG2 . THR J  6 98  ? 42.393  39.473  234.795 1.00 207.72 ?  95  THR I CG2 1 
ATOM   18143 N N   . LYS J  6 99  ? 44.804  40.803  232.778 1.00 202.88 ?  96  LYS I N   1 
ATOM   18144 C CA  . LYS J  6 99  ? 44.635  41.260  231.408 1.00 209.23 ?  96  LYS I CA  1 
ATOM   18145 C C   . LYS J  6 99  ? 43.589  40.373  230.751 1.00 204.95 ?  96  LYS I C   1 
ATOM   18146 O O   . LYS J  6 99  ? 43.636  39.146  230.888 1.00 194.93 ?  96  LYS I O   1 
ATOM   18147 C CB  . LYS J  6 99  ? 45.916  41.170  230.567 1.00 208.72 ?  96  LYS I CB  1 
ATOM   18148 C CG  . LYS J  6 99  ? 46.951  42.292  230.619 1.00 213.35 ?  96  LYS I CG  1 
ATOM   18149 C CD  . LYS J  6 99  ? 47.737  42.440  231.898 1.00 209.88 ?  96  LYS I CD  1 
ATOM   18150 C CE  . LYS J  6 99  ? 49.012  43.217  231.550 1.00 200.60 ?  96  LYS I CE  1 
ATOM   18151 N NZ  . LYS J  6 99  ? 48.777  44.683  231.310 1.00 209.23 1  96  LYS I NZ  1 
ATOM   18152 N N   . HIS J  6 100 ? 42.641  40.994  230.060 1.00 191.97 ?  97  HIS I N   1 
ATOM   18153 C CA  . HIS J  6 100 ? 41.561  40.265  229.419 1.00 189.82 ?  97  HIS I CA  1 
ATOM   18154 C C   . HIS J  6 100 ? 41.922  39.965  227.973 1.00 191.26 ?  97  HIS I C   1 
ATOM   18155 O O   . HIS J  6 100 ? 42.765  40.631  227.361 1.00 196.18 ?  97  HIS I O   1 
ATOM   18156 C CB  . HIS J  6 100 ? 40.245  41.037  229.455 1.00 193.86 ?  97  HIS I CB  1 
ATOM   18157 C CG  . HIS J  6 100 ? 40.292  42.349  228.742 1.00 201.98 ?  97  HIS I CG  1 
ATOM   18158 N ND1 . HIS J  6 100 ? 40.648  43.522  229.370 1.00 205.23 ?  97  HIS I ND1 1 
ATOM   18159 C CD2 . HIS J  6 100 ? 40.000  42.678  227.461 1.00 207.70 ?  97  HIS I CD2 1 
ATOM   18160 C CE1 . HIS J  6 100 ? 40.595  44.515  228.502 1.00 212.70 ?  97  HIS I CE1 1 
ATOM   18161 N NE2 . HIS J  6 100 ? 40.202  44.031  227.337 1.00 214.47 ?  97  HIS I NE2 1 
ATOM   18162 N N   . GLY J  6 101 ? 41.285  38.930  227.441 1.00 195.50 ?  98  GLY I N   1 
ATOM   18163 C CA  . GLY J  6 101 ? 41.469  38.565  226.052 1.00 196.74 ?  98  GLY I CA  1 
ATOM   18164 C C   . GLY J  6 101 ? 40.161  38.029  225.512 1.00 199.75 ?  98  GLY I C   1 
ATOM   18165 O O   . GLY J  6 101 ? 39.302  37.545  226.257 1.00 200.60 ?  98  GLY I O   1 
ATOM   18166 N N   . ARG J  6 102 ? 40.032  38.104  224.190 1.00 213.09 ?  99  ARG I N   1 
ATOM   18167 C CA  . ARG J  6 102 ? 38.832  37.670  223.493 1.00 220.02 ?  99  ARG I CA  1 
ATOM   18168 C C   . ARG J  6 102 ? 39.137  36.641  222.410 1.00 220.26 ?  99  ARG I C   1 
ATOM   18169 O O   . ARG J  6 102 ? 39.839  36.935  221.435 1.00 220.78 ?  99  ARG I O   1 
ATOM   18170 C CB  . ARG J  6 102 ? 38.062  38.879  222.955 1.00 227.18 ?  99  ARG I CB  1 
ATOM   18171 C CG  . ARG J  6 102 ? 37.514  39.808  224.067 1.00 230.04 ?  99  ARG I CG  1 
ATOM   18172 C CD  . ARG J  6 102 ? 36.814  41.050  223.483 1.00 240.84 ?  99  ARG I CD  1 
ATOM   18173 N NE  . ARG J  6 102 ? 36.186  41.937  224.475 1.00 244.16 ?  99  ARG I NE  1 
ATOM   18174 C CZ  . ARG J  6 102 ? 36.774  42.912  225.168 1.00 250.36 ?  99  ARG I CZ  1 
ATOM   18175 N NH1 . ARG J  6 102 ? 38.054  43.191  225.016 1.00 255.95 1  99  ARG I NH1 1 
ATOM   18176 N NH2 . ARG J  6 102 ? 36.062  43.623  226.030 1.00 251.22 ?  99  ARG I NH2 1 
ATOM   18177 N N   . ARG J  6 103 ? 38.609  35.430  222.604 1.00 200.77 ?  100 ARG I N   1 
ATOM   18178 C CA  . ARG J  6 103 ? 38.767  34.298  221.691 1.00 206.11 ?  100 ARG I CA  1 
ATOM   18179 C C   . ARG J  6 103 ? 37.610  34.200  220.695 1.00 214.42 ?  100 ARG I C   1 
ATOM   18180 O O   . ARG J  6 103 ? 36.471  33.905  221.081 1.00 217.25 ?  100 ARG I O   1 
ATOM   18181 C CB  . ARG J  6 103 ? 38.926  32.988  222.455 1.00 203.94 ?  100 ARG I CB  1 
ATOM   18182 C CG  . ARG J  6 103 ? 39.107  31.855  221.478 1.00 214.27 ?  100 ARG I CG  1 
ATOM   18183 C CD  . ARG J  6 103 ? 40.378  31.994  220.644 1.00 211.50 ?  100 ARG I CD  1 
ATOM   18184 N NE  . ARG J  6 103 ? 40.705  30.752  219.943 1.00 224.80 ?  100 ARG I NE  1 
ATOM   18185 C CZ  . ARG J  6 103 ? 40.211  30.416  218.753 1.00 233.32 ?  100 ARG I CZ  1 
ATOM   18186 N NH1 . ARG J  6 103 ? 40.551  29.268  218.178 1.00 236.32 1  100 ARG I NH1 1 
ATOM   18187 N NH2 . ARG J  6 103 ? 39.380  31.239  218.129 1.00 229.41 ?  100 ARG I NH2 1 
ATOM   18188 N N   . ILE J  6 104 A 37.901  34.447  219.419 1.00 204.52 ?  100 ILE I N   1 
ATOM   18189 C CA  . ILE J  6 104 A 36.906  34.408  218.349 1.00 211.96 ?  100 ILE I CA  1 
ATOM   18190 C C   . ILE J  6 104 A 37.013  33.084  217.598 1.00 215.93 ?  100 ILE I C   1 
ATOM   18191 O O   . ILE J  6 104 A 38.085  32.728  217.088 1.00 216.14 ?  100 ILE I O   1 
ATOM   18192 C CB  . ILE J  6 104 A 37.065  35.582  217.366 1.00 215.71 ?  100 ILE I CB  1 
ATOM   18193 C CG1 . ILE J  6 104 A 36.486  36.898  217.921 1.00 214.42 ?  100 ILE I CG1 1 
ATOM   18194 C CG2 . ILE J  6 104 A 36.482  35.229  215.977 1.00 219.91 ?  100 ILE I CG2 1 
ATOM   18195 C CD1 . ILE J  6 104 A 37.337  37.523  219.023 1.00 212.79 ?  100 ILE I CD1 1 
ATOM   18196 N N   . TYR J  6 105 B 35.894  32.358  217.526 1.00 195.16 ?  100 TYR I N   1 
ATOM   18197 C CA  . TYR J  6 105 B 35.807  31.072  216.846 1.00 198.29 ?  100 TYR I CA  1 
ATOM   18198 C C   . TYR J  6 105 B 34.728  31.044  215.769 1.00 201.62 ?  100 TYR I C   1 
ATOM   18199 O O   . TYR J  6 105 B 34.812  30.219  214.853 1.00 203.99 ?  100 TYR I O   1 
ATOM   18200 C CB  . TYR J  6 105 B 35.536  29.936  217.850 1.00 199.50 ?  100 TYR I CB  1 
ATOM   18201 C CG  . TYR J  6 105 B 34.261  30.087  218.671 1.00 200.65 ?  100 TYR I CG  1 
ATOM   18202 C CD1 . TYR J  6 105 B 33.046  29.597  218.204 1.00 204.32 ?  100 TYR I CD1 1 
ATOM   18203 C CD2 . TYR J  6 105 B 34.281  30.682  219.929 1.00 198.19 ?  100 TYR I CD2 1 
ATOM   18204 C CE1 . TYR J  6 105 B 31.883  29.717  218.951 1.00 205.55 ?  100 TYR I CE1 1 
ATOM   18205 C CE2 . TYR J  6 105 B 33.119  30.800  220.686 1.00 199.39 ?  100 TYR I CE2 1 
ATOM   18206 C CZ  . TYR J  6 105 B 31.924  30.317  220.190 1.00 203.09 ?  100 TYR I CZ  1 
ATOM   18207 O OH  . TYR J  6 105 B 30.768  30.432  220.931 1.00 204.45 ?  100 TYR I OH  1 
ATOM   18208 N N   . GLY J  6 106 C 33.728  31.915  215.856 1.00 196.42 ?  100 GLY I N   1 
ATOM   18209 C CA  . GLY J  6 106 C 32.604  31.951  214.941 1.00 199.65 ?  100 GLY I CA  1 
ATOM   18210 C C   . GLY J  6 106 C 32.656  33.061  213.913 1.00 199.07 ?  100 GLY I C   1 
ATOM   18211 O O   . GLY J  6 106 C 33.648  33.217  213.194 1.00 197.88 ?  100 GLY I O   1 
ATOM   18212 N N   . VAL J  6 107 D 31.579  33.839  213.839 1.00 198.67 ?  100 VAL I N   1 
ATOM   18213 C CA  . VAL J  6 107 D 31.430  34.901  212.855 1.00 198.60 ?  100 VAL I CA  1 
ATOM   18214 C C   . VAL J  6 107 D 31.405  36.271  213.538 1.00 195.62 ?  100 VAL I C   1 
ATOM   18215 O O   . VAL J  6 107 D 30.937  37.254  212.962 1.00 195.83 ?  100 VAL I O   1 
ATOM   18216 C CB  . VAL J  6 107 D 30.168  34.673  212.003 1.00 202.63 ?  100 VAL I CB  1 
ATOM   18217 C CG1 . VAL J  6 107 D 30.180  35.537  210.767 1.00 202.98 ?  100 VAL I CG1 1 
ATOM   18218 C CG2 . VAL J  6 107 D 30.027  33.216  211.631 1.00 205.68 ?  100 VAL I CG2 1 
ATOM   18219 N N   . VAL J  6 108 E 31.900  36.339  214.777 1.00 191.11 ?  100 VAL I N   1 
ATOM   18220 C CA  . VAL J  6 108 E 32.022  37.568  215.561 1.00 187.96 ?  100 VAL I CA  1 
ATOM   18221 C C   . VAL J  6 108 E 30.667  38.227  215.785 1.00 189.74 ?  100 VAL I C   1 
ATOM   18222 O O   . VAL J  6 108 E 30.251  38.451  216.927 1.00 189.74 ?  100 VAL I O   1 
ATOM   18223 C CB  . VAL J  6 108 E 32.990  38.557  214.888 1.00 185.42 ?  100 VAL I CB  1 
ATOM   18224 C CG1 . VAL J  6 108 E 33.196  39.776  215.769 1.00 182.36 ?  100 VAL I CG1 1 
ATOM   18225 C CG2 . VAL J  6 108 E 34.306  37.877  214.571 1.00 184.35 ?  100 VAL I CG2 1 
ATOM   18226 N N   . ALA J  6 109 F 29.977  38.538  214.687 1.00 187.63 ?  100 ALA I N   1 
ATOM   18227 C CA  . ALA J  6 109 F 28.707  39.252  214.747 1.00 190.74 ?  100 ALA I CA  1 
ATOM   18228 C C   . ALA J  6 109 F 27.635  38.477  215.500 1.00 193.37 ?  100 ALA I C   1 
ATOM   18229 O O   . ALA J  6 109 F 26.719  39.083  216.066 1.00 195.18 ?  100 ALA I O   1 
ATOM   18230 C CB  . ALA J  6 109 F 28.219  39.572  213.337 1.00 193.32 ?  100 ALA I CB  1 
ATOM   18231 N N   . PHE J  6 110 G 27.705  37.149  215.507 1.00 194.93 ?  100 PHE I N   1 
ATOM   18232 C CA  . PHE J  6 110 G 26.698  36.362  216.197 1.00 197.54 ?  100 PHE I CA  1 
ATOM   18233 C C   . PHE J  6 110 G 27.090  36.050  217.635 1.00 195.33 ?  100 PHE I C   1 
ATOM   18234 O O   . PHE J  6 110 G 26.597  35.067  218.203 1.00 196.76 ?  100 PHE I O   1 
ATOM   18235 C CB  . PHE J  6 110 G 26.446  35.057  215.444 1.00 200.00 ?  100 PHE I CB  1 
ATOM   18236 C CG  . PHE J  6 110 G 25.489  35.193  214.297 1.00 203.37 ?  100 PHE I CG  1 
ATOM   18237 C CD1 . PHE J  6 110 G 24.121  35.110  214.481 1.00 207.21 ?  100 PHE I CD1 1 
ATOM   18238 C CD2 . PHE J  6 110 G 25.977  35.343  213.011 1.00 203.66 ?  100 PHE I CD2 1 
ATOM   18239 C CE1 . PHE J  6 110 G 23.254  35.214  213.404 1.00 210.76 ?  100 PHE I CE1 1 
ATOM   18240 C CE2 . PHE J  6 110 G 25.121  35.444  211.934 1.00 206.84 ?  100 PHE I CE2 1 
ATOM   18241 C CZ  . PHE J  6 110 G 23.757  35.379  212.130 1.00 210.47 ?  100 PHE I CZ  1 
ATOM   18242 N N   . LYS J  6 111 H 27.957  36.873  218.234 1.00 207.59 ?  100 LYS I N   1 
ATOM   18243 C CA  . LYS J  6 111 H 28.427  36.687  219.607 1.00 205.26 ?  100 LYS I CA  1 
ATOM   18244 C C   . LYS J  6 111 H 29.027  35.299  219.799 1.00 204.54 ?  100 LYS I C   1 
ATOM   18245 O O   . LYS J  6 111 H 28.993  34.733  220.894 1.00 204.33 ?  100 LYS I O   1 
ATOM   18246 C CB  . LYS J  6 111 H 27.299  36.935  220.611 1.00 207.52 ?  100 LYS I CB  1 
ATOM   18247 C CG  . LYS J  6 111 H 26.810  38.371  220.623 1.00 208.28 ?  100 LYS I CG  1 
ATOM   18248 C CD  . LYS J  6 111 H 25.695  38.563  221.630 1.00 212.29 ?  100 LYS I CD  1 
ATOM   18249 C CE  . LYS J  6 111 H 25.230  40.007  221.658 1.00 216.81 ?  100 LYS I CE  1 
ATOM   18250 N NZ  . LYS J  6 111 H 24.336  40.276  222.817 1.00 223.27 1  100 LYS I NZ  1 
ATOM   18251 N N   . GLU J  6 112 I 29.589  34.761  218.720 1.00 194.75 ?  100 GLU I N   1 
ATOM   18252 C CA  . GLU J  6 112 I 30.216  33.442  218.714 1.00 195.57 ?  100 GLU I CA  1 
ATOM   18253 C C   . GLU J  6 112 I 31.672  33.550  219.183 1.00 191.89 ?  100 GLU I C   1 
ATOM   18254 O O   . GLU J  6 112 I 32.622  33.200  218.483 1.00 191.38 ?  100 GLU I O   1 
ATOM   18255 C CB  . GLU J  6 112 I 30.100  32.838  217.318 1.00 198.40 ?  100 GLU I CB  1 
ATOM   18256 C CG  . GLU J  6 112 I 28.649  32.545  216.920 1.00 202.37 ?  100 GLU I CG  1 
ATOM   18257 C CD  . GLU J  6 112 I 28.510  31.964  215.524 1.00 205.26 ?  100 GLU I CD  1 
ATOM   18258 O OE1 . GLU J  6 112 I 29.434  32.150  214.708 1.00 204.03 ?  100 GLU I OE1 1 
ATOM   18259 O OE2 . GLU J  6 112 I 27.464  31.344  215.233 1.00 208.84 -1 100 GLU I OE2 1 
ATOM   18260 N N   . TRP J  6 113 J 31.821  34.047  220.411 1.00 221.12 ?  100 TRP I N   1 
ATOM   18261 C CA  . TRP J  6 113 J 33.115  34.236  221.054 1.00 215.12 ?  100 TRP I CA  1 
ATOM   18262 C C   . TRP J  6 113 J 32.948  34.189  222.570 1.00 209.81 ?  100 TRP I C   1 
ATOM   18263 O O   . TRP J  6 113 J 31.831  34.110  223.088 1.00 214.88 ?  100 TRP I O   1 
ATOM   18264 C CB  . TRP J  6 113 J 33.771  35.561  220.623 1.00 213.57 ?  100 TRP I CB  1 
ATOM   18265 C CG  . TRP J  6 113 J 32.995  36.810  221.012 1.00 220.06 ?  100 TRP I CG  1 
ATOM   18266 C CD1 . TRP J  6 113 J 31.704  36.873  221.459 1.00 225.48 ?  100 TRP I CD1 1 
ATOM   18267 C CD2 . TRP J  6 113 J 33.492  38.156  221.055 1.00 223.62 ?  100 TRP I CD2 1 
ATOM   18268 N NE1 . TRP J  6 113 J 31.354  38.173  221.727 1.00 230.45 ?  100 TRP I NE1 1 
ATOM   18269 C CE2 . TRP J  6 113 J 32.437  38.980  221.496 1.00 228.84 ?  100 TRP I CE2 1 
ATOM   18270 C CE3 . TRP J  6 113 J 34.722  38.746  220.749 1.00 224.77 ?  100 TRP I CE3 1 
ATOM   18271 C CZ2 . TRP J  6 113 J 32.575  40.359  221.638 1.00 234.62 ?  100 TRP I CZ2 1 
ATOM   18272 C CZ3 . TRP J  6 113 J 34.855  40.113  220.888 1.00 228.08 ?  100 TRP I CZ3 1 
ATOM   18273 C CH2 . TRP J  6 113 J 33.790  40.905  221.331 1.00 233.19 ?  100 TRP I CH2 1 
ATOM   18274 N N   . PHE J  6 114 K 34.079  34.238  223.283 1.00 215.61 ?  100 PHE I N   1 
ATOM   18275 C CA  . PHE J  6 114 K 34.058  34.269  224.742 1.00 211.00 ?  100 PHE I CA  1 
ATOM   18276 C C   . PHE J  6 114 K 35.333  34.943  225.234 1.00 201.73 ?  100 PHE I C   1 
ATOM   18277 O O   . PHE J  6 114 K 36.389  34.840  224.602 1.00 197.45 ?  100 PHE I O   1 
ATOM   18278 C CB  . PHE J  6 114 K 33.940  32.877  225.383 1.00 210.78 ?  100 PHE I CB  1 
ATOM   18279 C CG  . PHE J  6 114 K 35.140  31.991  225.176 1.00 203.69 ?  100 PHE I CG  1 
ATOM   18280 C CD1 . PHE J  6 114 K 35.284  31.225  224.033 1.00 205.58 ?  100 PHE I CD1 1 
ATOM   18281 C CD2 . PHE J  6 114 K 36.109  31.897  226.166 1.00 194.55 ?  100 PHE I CD2 1 
ATOM   18282 C CE1 . PHE J  6 114 K 36.391  30.406  223.871 1.00 200.90 ?  100 PHE I CE1 1 
ATOM   18283 C CE2 . PHE J  6 114 K 37.210  31.083  226.010 1.00 193.21 ?  100 PHE I CE2 1 
ATOM   18284 C CZ  . PHE J  6 114 K 37.353  30.336  224.863 1.00 195.60 ?  100 PHE I CZ  1 
ATOM   18285 N N   . THR J  6 115 L 35.220  35.642  226.365 1.00 193.90 ?  100 THR I N   1 
ATOM   18286 C CA  . THR J  6 115 L 36.345  36.358  226.956 1.00 190.00 ?  100 THR I CA  1 
ATOM   18287 C C   . THR J  6 115 L 37.045  35.519  228.019 1.00 189.12 ?  100 THR I C   1 
ATOM   18288 O O   . THR J  6 115 L 36.390  34.971  228.913 1.00 190.49 ?  100 THR I O   1 
ATOM   18289 C CB  . THR J  6 115 L 35.860  37.659  227.595 1.00 189.26 ?  100 THR I CB  1 
ATOM   18290 O OG1 . THR J  6 115 L 34.740  37.381  228.445 1.00 191.74 ?  100 THR I OG1 1 
ATOM   18291 C CG2 . THR J  6 115 L 35.403  38.623  226.534 1.00 190.54 ?  100 THR I CG2 1 
ATOM   18292 N N   . TYR J  6 116 M 38.371  35.415  227.914 1.00 197.49 ?  100 TYR I N   1 
ATOM   18293 C CA  . TYR J  6 116 M 39.189  34.682  228.872 1.00 195.28 ?  100 TYR I CA  1 
ATOM   18294 C C   . TYR J  6 116 M 40.122  35.648  229.606 1.00 191.32 ?  100 TYR I C   1 
ATOM   18295 O O   . TYR J  6 116 M 40.643  36.592  228.999 1.00 189.35 ?  100 TYR I O   1 
ATOM   18296 C CB  . TYR J  6 116 M 39.990  33.571  228.181 1.00 196.44 ?  100 TYR I CB  1 
ATOM   18297 C CG  . TYR J  6 116 M 40.952  34.041  227.114 1.00 194.98 ?  100 TYR I CG  1 
ATOM   18298 C CD1 . TYR J  6 116 M 40.525  34.246  225.807 1.00 196.62 ?  100 TYR I CD1 1 
ATOM   18299 C CD2 . TYR J  6 116 M 42.290  34.254  227.407 1.00 192.14 ?  100 TYR I CD2 1 
ATOM   18300 C CE1 . TYR J  6 116 M 41.403  34.665  224.833 1.00 195.58 ?  100 TYR I CE1 1 
ATOM   18301 C CE2 . TYR J  6 116 M 43.173  34.672  226.440 1.00 190.94 ?  100 TYR I CE2 1 
ATOM   18302 C CZ  . TYR J  6 116 M 42.724  34.875  225.155 1.00 192.61 ?  100 TYR I CZ  1 
ATOM   18303 O OH  . TYR J  6 116 M 43.600  35.293  224.185 1.00 192.61 ?  100 TYR I OH  1 
ATOM   18304 N N   . PHE J  6 117 N 40.339  35.408  230.903 1.00 192.72 ?  100 PHE I N   1 
ATOM   18305 C CA  . PHE J  6 117 N 41.209  36.218  231.736 1.00 189.11 ?  100 PHE I CA  1 
ATOM   18306 C C   . PHE J  6 117 N 42.452  35.447  232.150 1.00 188.04 ?  100 PHE I C   1 
ATOM   18307 O O   . PHE J  6 117 N 42.418  34.232  232.333 1.00 190.11 ?  100 PHE I O   1 
ATOM   18308 C CB  . PHE J  6 117 N 40.479  36.732  232.982 1.00 188.48 ?  100 PHE I CB  1 
ATOM   18309 C CG  . PHE J  6 117 N 39.351  37.676  232.682 1.00 190.46 ?  100 PHE I CG  1 
ATOM   18310 C CD1 . PHE J  6 117 N 39.599  39.027  232.506 1.00 189.38 ?  100 PHE I CD1 1 
ATOM   18311 C CD2 . PHE J  6 117 N 38.047  37.220  232.573 1.00 193.74 ?  100 PHE I CD2 1 
ATOM   18312 C CE1 . PHE J  6 117 N 38.572  39.910  232.238 1.00 191.50 ?  100 PHE I CE1 1 
ATOM   18313 C CE2 . PHE J  6 117 N 37.013  38.101  232.299 1.00 198.23 ?  100 PHE I CE2 1 
ATOM   18314 C CZ  . PHE J  6 117 N 37.277  39.447  232.131 1.00 198.80 ?  100 PHE I CZ  1 
ATOM   18315 N N   . TYR J  6 118 O 43.546  36.168  232.348 1.00 201.39 ?  100 TYR I N   1 
ATOM   18316 C CA  . TYR J  6 118 O 44.785  35.540  232.787 1.00 197.22 ?  100 TYR I CA  1 
ATOM   18317 C C   . TYR J  6 118 O 45.626  36.526  233.577 1.00 198.98 ?  100 TYR I C   1 
ATOM   18318 O O   . TYR J  6 118 O 45.767  37.686  233.179 1.00 198.32 ?  100 TYR I O   1 
ATOM   18319 C CB  . TYR J  6 118 O 45.561  34.995  231.584 1.00 198.31 ?  100 TYR I CB  1 
ATOM   18320 C CG  . TYR J  6 118 O 46.012  36.010  230.540 1.00 204.34 ?  100 TYR I CG  1 
ATOM   18321 C CD1 . TYR J  6 118 O 45.100  36.616  229.668 1.00 209.05 ?  100 TYR I CD1 1 
ATOM   18322 C CD2 . TYR J  6 118 O 47.354  36.352  230.415 1.00 201.25 ?  100 TYR I CD2 1 
ATOM   18323 C CE1 . TYR J  6 118 O 45.520  37.537  228.718 1.00 209.47 ?  100 TYR I CE1 1 
ATOM   18324 C CE2 . TYR J  6 118 O 47.782  37.266  229.463 1.00 202.07 ?  100 TYR I CE2 1 
ATOM   18325 C CZ  . TYR J  6 118 O 46.857  37.859  228.620 1.00 203.53 ?  100 TYR I CZ  1 
ATOM   18326 O OH  . TYR J  6 118 O 47.281  38.754  227.662 1.00 198.12 ?  100 TYR I OH  1 
ATOM   18327 N N   . MET J  6 119 P 46.168  36.063  234.697 1.00 207.32 ?  100 MET I N   1 
ATOM   18328 C CA  . MET J  6 119 P 47.004  36.891  235.563 1.00 200.89 ?  100 MET I CA  1 
ATOM   18329 C C   . MET J  6 119 P 48.465  36.764  235.147 1.00 199.53 ?  100 MET I C   1 
ATOM   18330 O O   . MET J  6 119 P 48.971  35.651  234.972 1.00 202.03 ?  100 MET I O   1 
ATOM   18331 C CB  . MET J  6 119 P 46.856  36.487  237.033 1.00 196.70 ?  100 MET I CB  1 
ATOM   18332 C CG  . MET J  6 119 P 45.500  36.788  237.633 1.00 196.99 ?  100 MET I CG  1 
ATOM   18333 S SD  . MET J  6 119 P 44.187  35.867  236.818 1.00 198.82 ?  100 MET I SD  1 
ATOM   18334 C CE  . MET J  6 119 P 44.662  34.183  237.206 1.00 200.96 ?  100 MET I CE  1 
ATOM   18335 N N   . ASP J  6 120 Q 49.141  37.904  235.001 1.00 207.90 ?  100 ASP I N   1 
ATOM   18336 C CA  . ASP J  6 120 Q 50.534  37.941  234.573 1.00 207.12 ?  100 ASP I CA  1 
ATOM   18337 C C   . ASP J  6 120 Q 51.477  38.380  235.679 1.00 205.07 ?  100 ASP I C   1 
ATOM   18338 O O   . ASP J  6 120 Q 52.573  37.828  235.807 1.00 204.65 ?  100 ASP I O   1 
ATOM   18339 C CB  . ASP J  6 120 Q 50.725  38.881  233.373 1.00 208.48 ?  100 ASP I CB  1 
ATOM   18340 C CG  . ASP J  6 120 Q 50.284  40.311  233.662 1.00 208.56 ?  100 ASP I CG  1 
ATOM   18341 O OD1 . ASP J  6 120 Q 49.281  40.499  234.379 1.00 210.73 ?  100 ASP I OD1 1 
ATOM   18342 O OD2 . ASP J  6 120 Q 50.957  41.250  233.179 1.00 208.68 -1 100 ASP I OD2 1 
ATOM   18343 N N   . VAL J  6 121 R 51.071  39.358  236.485 1.00 215.09 ?  100 VAL I N   1 
ATOM   18344 C CA  . VAL J  6 121 R 51.888  39.895  237.565 1.00 216.17 ?  100 VAL I CA  1 
ATOM   18345 C C   . VAL J  6 121 R 51.208  39.568  238.887 1.00 213.54 ?  100 VAL I C   1 
ATOM   18346 O O   . VAL J  6 121 R 50.170  40.152  239.223 1.00 215.07 ?  100 VAL I O   1 
ATOM   18347 C CB  . VAL J  6 121 R 52.074  41.412  237.413 1.00 218.76 ?  100 VAL I CB  1 
ATOM   18348 C CG1 . VAL J  6 121 R 52.925  41.974  238.538 1.00 216.44 ?  100 VAL I CG1 1 
ATOM   18349 C CG2 . VAL J  6 121 R 52.666  41.750  236.055 1.00 219.19 ?  100 VAL I CG2 1 
ATOM   18350 N N   . TRP J  6 122 ? 51.772  38.616  239.625 1.00 208.70 ?  101 TRP I N   1 
ATOM   18351 C CA  . TRP J  6 122 ? 51.220  38.209  240.906 1.00 208.37 ?  101 TRP I CA  1 
ATOM   18352 C C   . TRP J  6 122 ? 51.909  38.961  242.042 1.00 208.36 ?  101 TRP I C   1 
ATOM   18353 O O   . TRP J  6 122 ? 52.864  39.712  241.833 1.00 210.97 ?  101 TRP I O   1 
ATOM   18354 C CB  . TRP J  6 122 ? 51.388  36.713  241.123 1.00 207.51 ?  101 TRP I CB  1 
ATOM   18355 C CG  . TRP J  6 122 ? 50.585  35.897  240.206 1.00 212.82 ?  101 TRP I CG  1 
ATOM   18356 C CD1 . TRP J  6 122 ? 50.720  35.803  238.852 1.00 213.72 ?  101 TRP I CD1 1 
ATOM   18357 C CD2 . TRP J  6 122 ? 49.437  35.134  240.552 1.00 216.64 ?  101 TRP I CD2 1 
ATOM   18358 N NE1 . TRP J  6 122 ? 49.761  34.965  238.342 1.00 220.60 ?  101 TRP I NE1 1 
ATOM   18359 C CE2 . TRP J  6 122 ? 48.953  34.549  239.367 1.00 222.22 ?  101 TRP I CE2 1 
ATOM   18360 C CE3 . TRP J  6 122 ? 48.784  34.867  241.756 1.00 213.19 ?  101 TRP I CE3 1 
ATOM   18361 C CZ2 . TRP J  6 122 ? 47.845  33.714  239.352 1.00 225.52 ?  101 TRP I CZ2 1 
ATOM   18362 C CZ3 . TRP J  6 122 ? 47.691  34.040  241.742 1.00 214.96 ?  101 TRP I CZ3 1 
ATOM   18363 C CH2 . TRP J  6 122 ? 47.229  33.471  240.548 1.00 222.19 ?  101 TRP I CH2 1 
ATOM   18364 N N   . GLY J  6 123 ? 51.408  38.761  243.262 1.00 217.31 ?  102 GLY I N   1 
ATOM   18365 C CA  . GLY J  6 123 ? 52.015  39.338  244.438 1.00 216.73 ?  102 GLY I CA  1 
ATOM   18366 C C   . GLY J  6 123 ? 52.633  38.251  245.306 1.00 215.20 ?  102 GLY I C   1 
ATOM   18367 O O   . GLY J  6 123 ? 52.537  37.058  245.028 1.00 213.62 ?  102 GLY I O   1 
ATOM   18368 N N   . LYS J  6 124 ? 53.284  38.694  246.383 1.00 217.67 ?  103 LYS I N   1 
ATOM   18369 C CA  . LYS J  6 124 ? 53.901  37.736  247.299 1.00 218.86 ?  103 LYS I CA  1 
ATOM   18370 C C   . LYS J  6 124 ? 52.856  36.893  248.033 1.00 218.34 ?  103 LYS I C   1 
ATOM   18371 O O   . LYS J  6 124 ? 53.083  35.703  248.287 1.00 219.01 ?  103 LYS I O   1 
ATOM   18372 C CB  . LYS J  6 124 ? 54.867  38.455  248.239 1.00 222.40 ?  103 LYS I CB  1 
ATOM   18373 C CG  . LYS J  6 124 ? 56.038  39.052  247.440 1.00 221.36 ?  103 LYS I CG  1 
ATOM   18374 C CD  . LYS J  6 124 ? 57.022  39.852  248.268 1.00 222.89 ?  103 LYS I CD  1 
ATOM   18375 C CE  . LYS J  6 124 ? 57.607  38.995  249.376 1.00 223.96 ?  103 LYS I CE  1 
ATOM   18376 N NZ  . LYS J  6 124 ? 58.350  37.812  248.838 1.00 228.12 1  103 LYS I NZ  1 
ATOM   18377 N N   . GLY J  6 125 ? 51.719  37.480  248.394 1.00 216.40 ?  104 GLY I N   1 
ATOM   18378 C CA  . GLY J  6 125 ? 50.670  36.725  249.060 1.00 218.40 ?  104 GLY I CA  1 
ATOM   18379 C C   . GLY J  6 125 ? 50.673  36.849  250.577 1.00 218.85 ?  104 GLY I C   1 
ATOM   18380 O O   . GLY J  6 125 ? 51.697  37.131  251.209 1.00 217.23 ?  104 GLY I O   1 
ATOM   18381 N N   . THR J  6 126 ? 49.489  36.645  251.173 1.00 217.81 ?  105 THR I N   1 
ATOM   18382 C CA  . THR J  6 126 ? 49.265  36.664  252.615 1.00 222.11 ?  105 THR I CA  1 
ATOM   18383 C C   . THR J  6 126 ? 48.692  35.322  253.070 1.00 220.10 ?  105 THR I C   1 
ATOM   18384 O O   . THR J  6 126 ? 48.007  34.636  252.305 1.00 217.44 ?  105 THR I O   1 
ATOM   18385 C CB  . THR J  6 126 ? 48.297  37.804  253.010 1.00 225.51 ?  105 THR I CB  1 
ATOM   18386 O OG1 . THR J  6 126 ? 48.048  37.781  254.423 1.00 229.59 ?  105 THR I OG1 1 
ATOM   18387 C CG2 . THR J  6 126 ? 46.981  37.676  252.246 1.00 223.85 ?  105 THR I CG2 1 
ATOM   18388 N N   . SER J  6 127 ? 48.984  34.948  254.319 1.00 215.99 ?  106 SER I N   1 
ATOM   18389 C CA  . SER J  6 127 ? 48.532  33.687  254.910 1.00 215.96 ?  106 SER I CA  1 
ATOM   18390 C C   . SER J  6 127 ? 47.338  33.904  255.839 1.00 223.35 ?  106 SER I C   1 
ATOM   18391 O O   . SER J  6 127 ? 47.403  34.743  256.743 1.00 225.74 ?  106 SER I O   1 
ATOM   18392 C CB  . SER J  6 127 ? 49.675  33.023  255.682 1.00 215.43 ?  106 SER I CB  1 
ATOM   18393 O OG  . SER J  6 127 ? 49.272  31.784  256.240 1.00 220.01 ?  106 SER I OG  1 
ATOM   18394 N N   . VAL J  6 128 ? 46.252  33.155  255.617 1.00 212.15 ?  107 VAL I N   1 
ATOM   18395 C CA  . VAL J  6 128 ? 45.040  33.244  256.438 1.00 216.49 ?  107 VAL I CA  1 
ATOM   18396 C C   . VAL J  6 128 ? 44.655  31.864  256.977 1.00 221.83 ?  107 VAL I C   1 
ATOM   18397 O O   . VAL J  6 128 ? 44.361  30.951  256.195 1.00 224.08 ?  107 VAL I O   1 
ATOM   18398 C CB  . VAL J  6 128 ? 43.862  33.855  255.659 1.00 218.93 ?  107 VAL I CB  1 
ATOM   18399 C CG1 . VAL J  6 128 ? 42.592  33.796  256.491 1.00 224.80 ?  107 VAL I CG1 1 
ATOM   18400 C CG2 . VAL J  6 128 ? 44.164  35.300  255.262 1.00 216.60 ?  107 VAL I CG2 1 
ATOM   18401 N N   . THR J  6 129 ? 44.662  31.714  258.305 1.00 217.64 ?  108 THR I N   1 
ATOM   18402 C CA  . THR J  6 129 ? 44.309  30.469  258.987 1.00 223.28 ?  108 THR I CA  1 
ATOM   18403 C C   . THR J  6 129 ? 43.063  30.711  259.834 1.00 228.51 ?  108 THR I C   1 
ATOM   18404 O O   . THR J  6 129 ? 43.026  31.662  260.621 1.00 227.83 ?  108 THR I O   1 
ATOM   18405 C CB  . THR J  6 129 ? 45.456  29.958  259.866 1.00 222.74 ?  108 THR I CB  1 
ATOM   18406 O OG1 . THR J  6 129 ? 46.646  29.830  259.080 1.00 218.53 ?  108 THR I OG1 1 
ATOM   18407 C CG2 . THR J  6 129 ? 45.107  28.604  260.456 1.00 226.44 ?  108 THR I CG2 1 
ATOM   18408 N N   . VAL J  6 130 ? 42.047  29.862  259.678 1.00 219.57 ?  109 VAL I N   1 
ATOM   18409 C CA  . VAL J  6 130 ? 40.799  29.985  260.429 1.00 225.68 ?  109 VAL I CA  1 
ATOM   18410 C C   . VAL J  6 130 ? 40.809  28.998  261.591 1.00 231.23 ?  109 VAL I C   1 
ATOM   18411 O O   . VAL J  6 130 ? 40.755  27.780  261.386 1.00 234.76 ?  109 VAL I O   1 
ATOM   18412 C CB  . VAL J  6 130 ? 39.576  29.756  259.533 1.00 230.48 ?  109 VAL I CB  1 
ATOM   18413 C CG1 . VAL J  6 130 ? 38.305  29.819  260.362 1.00 240.91 ?  109 VAL I CG1 1 
ATOM   18414 C CG2 . VAL J  6 130 ? 39.535  30.781  258.414 1.00 228.38 ?  109 VAL I CG2 1 
ATOM   18415 N N   . SER J  6 131 ? 40.864  29.522  262.814 1.00 232.15 ?  110 SER I N   1 
ATOM   18416 C CA  . SER J  6 131 ? 40.861  28.698  264.013 1.00 239.44 ?  110 SER I CA  1 
ATOM   18417 C C   . SER J  6 131 ? 40.318  29.503  265.183 1.00 247.78 ?  110 SER I C   1 
ATOM   18418 O O   . SER J  6 131 ? 40.512  30.718  265.259 1.00 244.81 ?  110 SER I O   1 
ATOM   18419 C CB  . SER J  6 131 ? 42.258  28.177  264.355 1.00 236.22 ?  110 SER I CB  1 
ATOM   18420 O OG  . SER J  6 131 ? 42.212  27.365  265.514 1.00 241.22 ?  110 SER I OG  1 
ATOM   18421 N N   . SER J  6 132 ? 39.621  28.819  266.085 1.00 242.11 ?  111 SER I N   1 
ATOM   18422 C CA  . SER J  6 132 ? 39.035  29.469  267.250 1.00 252.36 ?  111 SER I CA  1 
ATOM   18423 C C   . SER J  6 132 ? 40.025  29.594  268.406 1.00 252.33 ?  111 SER I C   1 
ATOM   18424 O O   . SER J  6 132 ? 39.632  30.026  269.496 1.00 252.61 ?  111 SER I O   1 
ATOM   18425 C CB  . SER J  6 132 ? 37.788  28.712  267.713 1.00 267.67 ?  111 SER I CB  1 
ATOM   18426 O OG  . SER J  6 132 ? 38.088  27.356  267.988 1.00 277.26 ?  111 SER I OG  1 
ATOM   18427 N N   . ALA J  6 133 ? 41.288  29.236  268.185 1.00 261.33 ?  112 ALA I N   1 
ATOM   18428 C CA  . ALA J  6 133 ? 42.325  29.314  269.203 1.00 260.67 ?  112 ALA I CA  1 
ATOM   18429 C C   . ALA J  6 133 ? 42.947  30.701  269.225 1.00 255.39 ?  112 ALA I C   1 
ATOM   18430 O O   . ALA J  6 133 ? 42.940  31.424  268.226 1.00 249.20 ?  112 ALA I O   1 
ATOM   18431 C CB  . ALA J  6 133 ? 43.415  28.271  268.953 1.00 253.23 ?  112 ALA I CB  1 
ATOM   18432 N N   . SER J  6 134 ? 43.484  31.069  270.384 1.00 278.75 ?  113 SER I N   1 
ATOM   18433 C CA  . SER J  6 134 ? 44.082  32.382  270.522 1.00 269.88 ?  113 SER I CA  1 
ATOM   18434 C C   . SER J  6 134 ? 45.474  32.442  269.896 1.00 262.11 ?  113 SER I C   1 
ATOM   18435 O O   . SER J  6 134 ? 46.096  31.434  269.554 1.00 262.51 ?  113 SER I O   1 
ATOM   18436 C CB  . SER J  6 134 ? 44.156  32.776  271.995 1.00 268.76 ?  113 SER I CB  1 
ATOM   18437 O OG  . SER J  6 134 ? 44.308  34.176  272.137 1.00 255.00 ?  113 SER I OG  1 
ATOM   18438 N N   . THR J  6 135 ? 45.946  33.677  269.766 1.00 276.65 ?  114 THR I N   1 
ATOM   18439 C CA  . THR J  6 135 ? 47.254  34.040  269.229 1.00 267.25 ?  114 THR I CA  1 
ATOM   18440 C C   . THR J  6 135 ? 48.302  34.096  270.339 1.00 266.77 ?  114 THR I C   1 
ATOM   18441 O O   . THR J  6 135 ? 48.045  34.647  271.414 1.00 271.81 ?  114 THR I O   1 
ATOM   18442 C CB  . THR J  6 135 ? 47.164  35.385  268.510 1.00 259.88 ?  114 THR I CB  1 
ATOM   18443 O OG1 . THR J  6 135 ? 46.116  35.332  267.538 1.00 260.04 ?  114 THR I OG1 1 
ATOM   18444 C CG2 . THR J  6 135 ? 48.449  35.666  267.784 1.00 248.70 ?  114 THR I CG2 1 
ATOM   18445 N N   . LYS J  6 136 ? 49.477  33.512  270.087 1.00 270.16 ?  115 LYS I N   1 
ATOM   18446 C CA  . LYS J  6 136 ? 50.568  33.507  271.059 1.00 265.88 ?  115 LYS I CA  1 
ATOM   18447 C C   . LYS J  6 136 ? 51.817  34.229  270.577 1.00 257.82 ?  115 LYS I C   1 
ATOM   18448 O O   . LYS J  6 136 ? 52.283  34.009  269.454 1.00 252.16 ?  115 LYS I O   1 
ATOM   18449 C CB  . LYS J  6 136 ? 51.046  32.087  271.386 1.00 265.92 ?  115 LYS I CB  1 
ATOM   18450 C CG  . LYS J  6 136 ? 52.034  32.099  272.551 1.00 266.54 ?  115 LYS I CG  1 
ATOM   18451 C CD  . LYS J  6 136 ? 52.599  30.755  272.956 1.00 264.05 ?  115 LYS I CD  1 
ATOM   18452 C CE  . LYS J  6 136 ? 53.435  30.965  274.207 1.00 264.50 ?  115 LYS I CE  1 
ATOM   18453 N NZ  . LYS J  6 136 ? 54.657  30.129  274.213 1.00 265.28 1  115 LYS I NZ  1 
ATOM   18454 N N   . GLY J  6 137 ? 52.348  35.102  271.438 1.00 258.50 ?  116 GLY I N   1 
ATOM   18455 C CA  . GLY J  6 137 ? 53.567  35.793  271.116 1.00 253.77 ?  116 GLY I CA  1 
ATOM   18456 C C   . GLY J  6 137 ? 54.702  34.805  271.292 1.00 253.18 ?  116 GLY I C   1 
ATOM   18457 O O   . GLY J  6 137 ? 54.764  34.064  272.278 1.00 257.46 ?  116 GLY I O   1 
ATOM   18458 N N   . PRO J  6 138 ? 55.624  34.779  270.342 1.00 254.08 ?  117 PRO I N   1 
ATOM   18459 C CA  . PRO J  6 138 ? 56.760  33.858  270.434 1.00 250.46 ?  117 PRO I CA  1 
ATOM   18460 C C   . PRO J  6 138 ? 57.772  34.277  271.491 1.00 254.40 ?  117 PRO I C   1 
ATOM   18461 O O   . PRO J  6 138 ? 57.843  35.438  271.901 1.00 256.62 ?  117 PRO I O   1 
ATOM   18462 C CB  . PRO J  6 138 ? 57.368  33.913  269.031 1.00 241.62 ?  117 PRO I CB  1 
ATOM   18463 C CG  . PRO J  6 138 ? 56.991  35.260  268.527 1.00 240.59 ?  117 PRO I CG  1 
ATOM   18464 C CD  . PRO J  6 138 ? 55.628  35.542  269.084 1.00 247.69 ?  117 PRO I CD  1 
ATOM   18465 N N   . SER J  6 139 ? 58.562  33.301  271.940 1.00 257.34 ?  118 SER I N   1 
ATOM   18466 C CA  . SER J  6 139 ? 59.649  33.553  272.883 1.00 261.85 ?  118 SER I CA  1 
ATOM   18467 C C   . SER J  6 139 ? 60.913  33.115  272.145 1.00 262.04 ?  118 SER I C   1 
ATOM   18468 O O   . SER J  6 139 ? 61.145  31.916  271.959 1.00 267.58 ?  118 SER I O   1 
ATOM   18469 C CB  . SER J  6 139 ? 59.451  32.807  274.206 1.00 268.67 ?  118 SER I CB  1 
ATOM   18470 O OG  . SER J  6 139 ? 59.303  31.412  274.016 1.00 277.07 ?  118 SER I OG  1 
ATOM   18471 N N   . VAL J  6 140 ? 61.722  34.096  271.734 1.00 266.13 ?  119 VAL I N   1 
ATOM   18472 C CA  . VAL J  6 140 ? 62.932  33.889  270.932 1.00 263.61 ?  119 VAL I CA  1 
ATOM   18473 C C   . VAL J  6 140 ? 64.144  33.611  271.815 1.00 270.31 ?  119 VAL I C   1 
ATOM   18474 O O   . VAL J  6 140 ? 64.412  34.357  272.765 1.00 270.37 ?  119 VAL I O   1 
ATOM   18475 C CB  . VAL J  6 140 ? 63.184  35.092  270.009 1.00 255.26 ?  119 VAL I CB  1 
ATOM   18476 C CG1 . VAL J  6 140 ? 64.372  34.817  269.097 1.00 253.90 ?  119 VAL I CG1 1 
ATOM   18477 C CG2 . VAL J  6 140 ? 61.936  35.389  269.188 1.00 251.90 ?  119 VAL I CG2 1 
ATOM   18478 N N   . PHE J  6 141 ? 64.880  32.535  271.513 1.00 260.27 ?  120 PHE I N   1 
ATOM   18479 C CA  . PHE J  6 141 ? 66.093  32.228  272.264 1.00 265.57 ?  120 PHE I CA  1 
ATOM   18480 C C   . PHE J  6 141 ? 67.306  32.045  271.350 1.00 263.82 ?  120 PHE I C   1 
ATOM   18481 O O   . PHE J  6 141 ? 67.222  31.337  270.332 1.00 260.06 ?  120 PHE I O   1 
ATOM   18482 C CB  . PHE J  6 141 ? 65.828  30.990  273.128 1.00 273.25 ?  120 PHE I CB  1 
ATOM   18483 C CG  . PHE J  6 141 ? 64.681  31.183  274.101 1.00 276.46 ?  120 PHE I CG  1 
ATOM   18484 C CD1 . PHE J  6 141 ? 64.844  31.894  275.284 1.00 275.81 ?  120 PHE I CD1 1 
ATOM   18485 C CD2 . PHE J  6 141 ? 63.426  30.666  273.812 1.00 276.00 ?  120 PHE I CD2 1 
ATOM   18486 C CE1 . PHE J  6 141 ? 63.774  32.073  276.162 1.00 274.67 ?  120 PHE I CE1 1 
ATOM   18487 C CE2 . PHE J  6 141 ? 62.359  30.839  274.683 1.00 278.53 ?  120 PHE I CE2 1 
ATOM   18488 C CZ  . PHE J  6 141 ? 62.533  31.544  275.858 1.00 279.89 ?  120 PHE I CZ  1 
ATOM   18489 N N   . PRO J  6 142 ? 68.447  32.657  271.689 1.00 266.19 ?  121 PRO I N   1 
ATOM   18490 C CA  . PRO J  6 142 ? 69.661  32.613  270.844 1.00 263.58 ?  121 PRO I CA  1 
ATOM   18491 C C   . PRO J  6 142 ? 70.449  31.301  270.865 1.00 265.64 ?  121 PRO I C   1 
ATOM   18492 O O   . PRO J  6 142 ? 70.669  30.703  271.916 1.00 271.14 ?  121 PRO I O   1 
ATOM   18493 C CB  . PRO J  6 142 ? 70.508  33.759  271.411 1.00 268.57 ?  121 PRO I CB  1 
ATOM   18494 C CG  . PRO J  6 142 ? 70.104  33.839  272.844 1.00 272.50 ?  121 PRO I CG  1 
ATOM   18495 C CD  . PRO J  6 142 ? 68.632  33.507  272.877 1.00 268.54 ?  121 PRO I CD  1 
ATOM   18496 N N   . LEU J  6 143 ? 70.937  30.882  269.690 1.00 259.02 ?  122 LEU I N   1 
ATOM   18497 C CA  . LEU J  6 143 ? 71.757  29.672  269.561 1.00 264.53 ?  122 LEU I CA  1 
ATOM   18498 C C   . LEU J  6 143 ? 73.245  30.038  269.489 1.00 265.54 ?  122 LEU I C   1 
ATOM   18499 O O   . LEU J  6 143 ? 73.719  30.539  268.465 1.00 263.55 ?  122 LEU I O   1 
ATOM   18500 C CB  . LEU J  6 143 ? 71.337  28.900  268.314 1.00 264.84 ?  122 LEU I CB  1 
ATOM   18501 C CG  . LEU J  6 143 ? 69.905  28.365  268.321 1.00 265.04 ?  122 LEU I CG  1 
ATOM   18502 C CD1 . LEU J  6 143 ? 69.612  27.613  267.035 1.00 265.52 ?  122 LEU I CD1 1 
ATOM   18503 C CD2 . LEU J  6 143 ? 69.664  27.488  269.534 1.00 270.65 ?  122 LEU I CD2 1 
ATOM   18504 N N   . ALA J  6 144 ? 73.979  29.735  270.569 1.00 256.99 ?  123 ALA I N   1 
ATOM   18505 C CA  . ALA J  6 144 ? 75.397  30.083  270.694 1.00 262.88 ?  123 ALA I CA  1 
ATOM   18506 C C   . ALA J  6 144 ? 76.285  29.400  269.651 1.00 269.12 ?  123 ALA I C   1 
ATOM   18507 O O   . ALA J  6 144 ? 76.106  28.213  269.356 1.00 272.95 ?  123 ALA I O   1 
ATOM   18508 C CB  . ALA J  6 144 ? 75.900  29.722  272.093 1.00 263.58 ?  123 ALA I CB  1 
ATOM   18509 N N   . PRO J  6 145 ? 77.268  30.121  269.099 1.00 268.48 ?  124 PRO I N   1 
ATOM   18510 C CA  . PRO J  6 145 ? 78.196  29.535  268.115 1.00 272.04 ?  124 PRO I CA  1 
ATOM   18511 C C   . PRO J  6 145 ? 79.094  28.430  268.666 1.00 287.01 ?  124 PRO I C   1 
ATOM   18512 O O   . PRO J  6 145 ? 79.610  28.521  269.783 1.00 291.89 ?  124 PRO I O   1 
ATOM   18513 C CB  . PRO J  6 145 ? 79.041  30.737  267.673 1.00 270.98 ?  124 PRO I CB  1 
ATOM   18514 C CG  . PRO J  6 145 ? 78.230  31.938  268.024 1.00 265.99 ?  124 PRO I CG  1 
ATOM   18515 C CD  . PRO J  6 145 ? 77.491  31.565  269.272 1.00 266.26 ?  124 PRO I CD  1 
ATOM   18516 N N   . SER J  6 146 ? 79.286  27.379  267.861 1.00 272.32 ?  125 SER I N   1 
ATOM   18517 C CA  . SER J  6 146 ? 80.156  26.266  268.254 1.00 283.47 ?  125 SER I CA  1 
ATOM   18518 C C   . SER J  6 146 ? 80.644  25.587  266.973 1.00 286.94 ?  125 SER I C   1 
ATOM   18519 O O   . SER J  6 146 ? 79.886  24.844  266.343 1.00 289.34 ?  125 SER I O   1 
ATOM   18520 C CB  . SER J  6 146 ? 79.447  25.289  269.177 1.00 283.77 ?  125 SER I CB  1 
ATOM   18521 O OG  . SER J  6 146 ? 79.098  25.910  270.403 1.00 276.55 ?  125 SER I OG  1 
ATOM   18522 N N   . SER J  6 147 ? 81.901  25.841  266.610 1.00 274.69 ?  126 SER I N   1 
ATOM   18523 C CA  . SER J  6 147 ? 82.514  25.253  265.415 1.00 278.56 ?  126 SER I CA  1 
ATOM   18524 C C   . SER J  6 147 ? 81.683  25.498  264.163 1.00 273.18 ?  126 SER I C   1 
ATOM   18525 O O   . SER J  6 147 ? 81.487  24.588  263.358 1.00 276.36 ?  126 SER I O   1 
ATOM   18526 C CB  . SER J  6 147 ? 82.745  23.752  265.597 1.00 287.06 ?  126 SER I CB  1 
ATOM   18527 O OG  . SER J  6 147 ? 83.649  23.501  266.656 1.00 293.14 ?  126 SER I OG  1 
ATOM   18528 N N   . GLY J  6 152 ? 88.105  23.907  261.136 1.00 281.59 ?  131 GLY I N   1 
ATOM   18529 C CA  . GLY J  6 152 ? 87.606  23.931  259.773 1.00 275.53 ?  131 GLY I CA  1 
ATOM   18530 C C   . GLY J  6 152 ? 87.625  25.316  259.156 1.00 265.67 ?  131 GLY I C   1 
ATOM   18531 O O   . GLY J  6 152 ? 87.486  25.479  257.943 1.00 265.77 ?  131 GLY I O   1 
ATOM   18532 N N   . GLY J  6 153 ? 87.789  26.324  260.007 1.00 288.67 ?  132 GLY I N   1 
ATOM   18533 C CA  . GLY J  6 153 ? 87.823  27.698  259.562 1.00 284.70 ?  132 GLY I CA  1 
ATOM   18534 C C   . GLY J  6 153 ? 86.461  28.332  259.405 1.00 278.10 ?  132 GLY I C   1 
ATOM   18535 O O   . GLY J  6 153 ? 86.382  29.521  259.068 1.00 270.50 ?  132 GLY I O   1 
ATOM   18536 N N   . THR J  6 154 ? 85.395  27.575  259.640 1.00 276.63 ?  133 THR I N   1 
ATOM   18537 C CA  . THR J  6 154 ? 84.009  28.002  259.545 1.00 269.29 ?  133 THR I CA  1 
ATOM   18538 C C   . THR J  6 154 ? 83.337  27.811  260.899 1.00 270.91 ?  133 THR I C   1 
ATOM   18539 O O   . THR J  6 154 ? 83.867  27.144  261.791 1.00 275.56 ?  133 THR I O   1 
ATOM   18540 C CB  . THR J  6 154 ? 83.269  27.218  258.456 1.00 267.10 ?  133 THR I CB  1 
ATOM   18541 O OG1 . THR J  6 154 ? 83.372  25.814  258.728 1.00 278.74 ?  133 THR I OG1 1 
ATOM   18542 C CG2 . THR J  6 154 ? 83.875  27.510  257.095 1.00 256.80 ?  133 THR I CG2 1 
ATOM   18543 N N   . ALA J  6 155 ? 82.160  28.414  261.057 1.00 259.20 ?  134 ALA I N   1 
ATOM   18544 C CA  . ALA J  6 155 ? 81.419  28.311  262.306 1.00 260.07 ?  134 ALA I CA  1 
ATOM   18545 C C   . ALA J  6 155 ? 79.933  28.466  262.018 1.00 257.82 ?  134 ALA I C   1 
ATOM   18546 O O   . ALA J  6 155 ? 79.535  29.076  261.022 1.00 253.71 ?  134 ALA I O   1 
ATOM   18547 C CB  . ALA J  6 155 ? 81.886  29.356  263.327 1.00 258.59 ?  134 ALA I CB  1 
ATOM   18548 N N   . ALA J  6 156 ? 79.117  27.905  262.906 1.00 265.06 ?  135 ALA I N   1 
ATOM   18549 C CA  . ALA J  6 156 ? 77.668  27.958  262.790 1.00 264.05 ?  135 ALA I CA  1 
ATOM   18550 C C   . ALA J  6 156 ? 77.087  28.933  263.808 1.00 260.54 ?  135 ALA I C   1 
ATOM   18551 O O   . ALA J  6 156 ? 77.627  29.109  264.903 1.00 261.26 ?  135 ALA I O   1 
ATOM   18552 C CB  . ALA J  6 156 ? 77.058  26.567  262.991 1.00 270.60 ?  135 ALA I CB  1 
ATOM   18553 N N   . LEU J  6 157 ? 75.973  29.562  263.432 1.00 272.13 ?  136 LEU I N   1 
ATOM   18554 C CA  . LEU J  6 157 ? 75.297  30.537  264.278 1.00 268.51 ?  136 LEU I CA  1 
ATOM   18555 C C   . LEU J  6 157 ? 73.837  30.652  263.855 1.00 261.21 ?  136 LEU I C   1 
ATOM   18556 O O   . LEU J  6 157 ? 73.538  30.628  262.659 1.00 254.79 ?  136 LEU I O   1 
ATOM   18557 C CB  . LEU J  6 157 ? 76.000  31.900  264.207 1.00 268.22 ?  136 LEU I CB  1 
ATOM   18558 C CG  . LEU J  6 157 ? 75.640  32.965  265.244 1.00 266.67 ?  136 LEU I CG  1 
ATOM   18559 C CD1 . LEU J  6 157 ? 76.802  33.915  265.409 1.00 272.35 ?  136 LEU I CD1 1 
ATOM   18560 C CD2 . LEU J  6 157 ? 74.402  33.749  264.824 1.00 259.94 ?  136 LEU I CD2 1 
ATOM   18561 N N   . GLY J  6 158 ? 72.938  30.777  264.829 1.00 271.10 ?  137 GLY I N   1 
ATOM   18562 C CA  . GLY J  6 158 ? 71.529  30.890  264.507 1.00 268.70 ?  137 GLY I CA  1 
ATOM   18563 C C   . GLY J  6 158 ? 70.702  31.396  265.675 1.00 263.61 ?  137 GLY I C   1 
ATOM   18564 O O   . GLY J  6 158 ? 71.237  31.744  266.731 1.00 263.76 ?  137 GLY I O   1 
ATOM   18565 N N   . CYS J  6 159 ? 69.377  31.407  265.476 1.00 271.37 ?  138 CYS I N   1 
ATOM   18566 C CA  . CYS J  6 159 ? 68.410  31.823  266.482 1.00 266.17 ?  138 CYS I CA  1 
ATOM   18567 C C   . CYS J  6 159 ? 67.359  30.726  266.640 1.00 260.37 ?  138 CYS I C   1 
ATOM   18568 O O   . CYS J  6 159 ? 67.379  29.715  265.936 1.00 259.76 ?  138 CYS I O   1 
ATOM   18569 C CB  . CYS J  6 159 ? 67.761  33.183  266.109 1.00 264.40 ?  138 CYS I CB  1 
ATOM   18570 S SG  . CYS J  6 159 ? 68.931  34.579  266.080 1.00 317.59 ?  138 CYS I SG  1 
ATOM   18571 N N   . LEU J  6 160 ? 66.415  30.926  267.551 1.00 278.32 ?  139 LEU I N   1 
ATOM   18572 C CA  . LEU J  6 160 ? 65.357  29.950  267.803 1.00 267.56 ?  139 LEU I CA  1 
ATOM   18573 C C   . LEU J  6 160 ? 64.080  30.684  268.177 1.00 256.94 ?  139 LEU I C   1 
ATOM   18574 O O   . LEU J  6 160 ? 64.088  31.477  269.127 1.00 252.99 ?  139 LEU I O   1 
ATOM   18575 C CB  . LEU J  6 160 ? 65.730  28.952  268.912 1.00 268.28 ?  139 LEU I CB  1 
ATOM   18576 C CG  . LEU J  6 160 ? 64.571  27.991  269.240 1.00 262.40 ?  139 LEU I CG  1 
ATOM   18577 C CD1 . LEU J  6 160 ? 65.079  26.630  269.491 1.00 267.86 ?  139 LEU I CD1 1 
ATOM   18578 C CD2 . LEU J  6 160 ? 63.754  28.368  270.466 1.00 254.93 ?  139 LEU I CD2 1 
ATOM   18579 N N   . VAL J  6 161 ? 62.998  30.415  267.455 1.00 261.12 ?  140 VAL I N   1 
ATOM   18580 C CA  . VAL J  6 161 ? 61.673  30.973  267.711 1.00 252.21 ?  140 VAL I CA  1 
ATOM   18581 C C   . VAL J  6 161 ? 60.821  29.870  268.327 1.00 252.20 ?  140 VAL I C   1 
ATOM   18582 O O   . VAL J  6 161 ? 60.432  28.919  267.639 1.00 252.86 ?  140 VAL I O   1 
ATOM   18583 C CB  . VAL J  6 161 ? 61.020  31.543  266.443 1.00 248.77 ?  140 VAL I CB  1 
ATOM   18584 C CG1 . VAL J  6 161 ? 59.653  32.128  266.776 1.00 246.36 ?  140 VAL I CG1 1 
ATOM   18585 C CG2 . VAL J  6 161 ? 61.906  32.602  265.820 1.00 255.17 ?  140 VAL I CG2 1 
ATOM   18586 N N   . LYS J  6 162 ? 60.521  29.988  269.615 1.00 254.03 ?  141 LYS I N   1 
ATOM   18587 C CA  . LYS J  6 162 ? 59.823  28.946  270.358 1.00 257.21 ?  141 LYS I CA  1 
ATOM   18588 C C   . LYS J  6 162 ? 58.394  29.340  270.676 1.00 260.24 ?  141 LYS I C   1 
ATOM   18589 O O   . LYS J  6 162 ? 58.137  30.464  271.121 1.00 257.88 ?  141 LYS I O   1 
ATOM   18590 C CB  . LYS J  6 162 ? 60.521  28.663  271.692 1.00 266.51 ?  141 LYS I CB  1 
ATOM   18591 C CG  . LYS J  6 162 ? 59.849  27.591  272.550 1.00 271.53 ?  141 LYS I CG  1 
ATOM   18592 C CD  . LYS J  6 162 ? 60.800  26.581  273.159 1.00 271.07 ?  141 LYS I CD  1 
ATOM   18593 C CE  . LYS J  6 162 ? 60.016  25.617  274.047 1.00 278.39 ?  141 LYS I CE  1 
ATOM   18594 N NZ  . LYS J  6 162 ? 60.867  24.614  274.745 1.00 284.10 1  141 LYS I NZ  1 
ATOM   18595 N N   . ASP J  6 163 ? 57.482  28.397  270.438 1.00 269.64 ?  142 ASP I N   1 
ATOM   18596 C CA  . ASP J  6 163 ? 56.067  28.486  270.773 1.00 273.02 ?  142 ASP I CA  1 
ATOM   18597 C C   . ASP J  6 163 ? 55.335  29.703  270.209 1.00 264.66 ?  142 ASP I C   1 
ATOM   18598 O O   . ASP J  6 163 ? 55.287  30.747  270.867 1.00 262.25 ?  142 ASP I O   1 
ATOM   18599 C CB  . ASP J  6 163 ? 55.938  28.442  272.294 1.00 278.91 ?  142 ASP I CB  1 
ATOM   18600 C CG  . ASP J  6 163 ? 56.211  27.059  272.854 1.00 289.68 ?  142 ASP I CG  1 
ATOM   18601 O OD1 . ASP J  6 163 ? 56.977  26.308  272.212 1.00 290.34 ?  142 ASP I OD1 1 
ATOM   18602 O OD2 . ASP J  6 163 ? 55.683  26.726  273.933 1.00 301.17 -1 142 ASP I OD2 1 
ATOM   18603 N N   . TYR J  6 164 ? 54.765  29.599  269.006 1.00 289.78 ?  143 TYR I N   1 
ATOM   18604 C CA  . TYR J  6 164 ? 53.974  30.705  268.479 1.00 281.46 ?  143 TYR I CA  1 
ATOM   18605 C C   . TYR J  6 164 ? 52.823  30.153  267.652 1.00 279.26 ?  143 TYR I C   1 
ATOM   18606 O O   . TYR J  6 164 ? 52.813  28.986  267.251 1.00 280.99 ?  143 TYR I O   1 
ATOM   18607 C CB  . TYR J  6 164 ? 54.785  31.694  267.620 1.00 274.34 ?  143 TYR I CB  1 
ATOM   18608 C CG  . TYR J  6 164 ? 55.263  31.182  266.272 1.00 266.81 ?  143 TYR I CG  1 
ATOM   18609 C CD1 . TYR J  6 164 ? 56.486  30.541  266.132 1.00 268.11 ?  143 TYR I CD1 1 
ATOM   18610 C CD2 . TYR J  6 164 ? 54.483  31.359  265.131 1.00 261.03 ?  143 TYR I CD2 1 
ATOM   18611 C CE1 . TYR J  6 164 ? 56.918  30.086  264.890 1.00 264.08 ?  143 TYR I CE1 1 
ATOM   18612 C CE2 . TYR J  6 164 ? 54.901  30.905  263.895 1.00 255.85 ?  143 TYR I CE2 1 
ATOM   18613 C CZ  . TYR J  6 164 ? 56.118  30.271  263.777 1.00 257.37 ?  143 TYR I CZ  1 
ATOM   18614 O OH  . TYR J  6 164 ? 56.526  29.825  262.538 1.00 254.40 ?  143 TYR I OH  1 
ATOM   18615 N N   . PHE J  6 165 ? 51.856  31.028  267.397 1.00 274.65 ?  144 PHE I N   1 
ATOM   18616 C CA  . PHE J  6 165 ? 50.653  30.717  266.636 1.00 279.11 ?  144 PHE I CA  1 
ATOM   18617 C C   . PHE J  6 165 ? 49.916  31.974  266.201 1.00 278.77 ?  144 PHE I C   1 
ATOM   18618 O O   . PHE J  6 165 ? 49.710  32.878  267.006 1.00 279.51 ?  144 PHE I O   1 
ATOM   18619 C CB  . PHE J  6 165 ? 49.740  29.847  267.518 1.00 284.97 ?  144 PHE I CB  1 
ATOM   18620 C CG  . PHE J  6 165 ? 48.481  29.373  266.849 1.00 287.86 ?  144 PHE I CG  1 
ATOM   18621 C CD1 . PHE J  6 165 ? 48.462  28.243  266.053 1.00 284.98 ?  144 PHE I CD1 1 
ATOM   18622 C CD2 . PHE J  6 165 ? 47.287  30.038  267.090 1.00 289.13 ?  144 PHE I CD2 1 
ATOM   18623 C CE1 . PHE J  6 165 ? 47.280  27.821  265.465 1.00 281.38 ?  144 PHE I CE1 1 
ATOM   18624 C CE2 . PHE J  6 165 ? 46.108  29.620  266.514 1.00 285.93 ?  144 PHE I CE2 1 
ATOM   18625 C CZ  . PHE J  6 165 ? 46.102  28.511  265.700 1.00 280.62 ?  144 PHE I CZ  1 
ATOM   18626 N N   . PRO J  6 166 ? 49.510  32.037  264.920 1.00 288.45 ?  145 PRO I N   1 
ATOM   18627 C CA  . PRO J  6 166 ? 49.782  31.032  263.891 1.00 282.67 ?  145 PRO I CA  1 
ATOM   18628 C C   . PRO J  6 166 ? 50.914  31.481  262.961 1.00 274.60 ?  145 PRO I C   1 
ATOM   18629 O O   . PRO J  6 166 ? 51.617  32.451  263.260 1.00 273.44 ?  145 PRO I O   1 
ATOM   18630 C CB  . PRO J  6 166 ? 48.459  30.956  263.138 1.00 273.75 ?  145 PRO I CB  1 
ATOM   18631 C CG  . PRO J  6 166 ? 47.969  32.375  263.174 1.00 271.11 ?  145 PRO I CG  1 
ATOM   18632 C CD  . PRO J  6 166 ? 48.480  32.989  264.470 1.00 280.32 ?  145 PRO I CD  1 
ATOM   18633 N N   . GLU J  6 167 ? 51.073  30.778  261.844 1.00 259.19 ?  146 GLU I N   1 
ATOM   18634 C CA  . GLU J  6 167 ? 52.067  31.124  260.834 1.00 254.44 ?  146 GLU I CA  1 
ATOM   18635 C C   . GLU J  6 167 ? 51.669  32.419  260.108 1.00 250.00 ?  146 GLU I C   1 
ATOM   18636 O O   . GLU J  6 167 ? 50.487  32.763  260.064 1.00 249.85 ?  146 GLU I O   1 
ATOM   18637 C CB  . GLU J  6 167 ? 52.248  29.978  259.827 1.00 252.47 ?  146 GLU I CB  1 
ATOM   18638 C CG  . GLU J  6 167 ? 52.943  28.740  260.384 1.00 256.76 ?  146 GLU I CG  1 
ATOM   18639 C CD  . GLU J  6 167 ? 54.286  28.487  259.723 1.00 255.03 ?  146 GLU I CD  1 
ATOM   18640 O OE1 . GLU J  6 167 ? 54.479  28.935  258.576 1.00 250.19 ?  146 GLU I OE1 1 
ATOM   18641 O OE2 . GLU J  6 167 ? 55.153  27.842  260.350 1.00 258.90 -1 146 GLU I OE2 1 
ATOM   18642 N N   . PRO J  6 168 ? 52.651  33.142  259.540 1.00 267.44 ?  147 PRO I N   1 
ATOM   18643 C CA  . PRO J  6 168 ? 54.084  32.845  259.603 1.00 267.14 ?  147 PRO I CA  1 
ATOM   18644 C C   . PRO J  6 168 ? 54.890  33.798  260.476 1.00 265.93 ?  147 PRO I C   1 
ATOM   18645 O O   . PRO J  6 168 ? 54.330  34.610  261.214 1.00 267.10 ?  147 PRO I O   1 
ATOM   18646 C CB  . PRO J  6 168 ? 54.508  32.995  258.147 1.00 264.51 ?  147 PRO I CB  1 
ATOM   18647 C CG  . PRO J  6 168 ? 53.652  34.151  257.665 1.00 261.73 ?  147 PRO I CG  1 
ATOM   18648 C CD  . PRO J  6 168 ? 52.360  34.116  258.474 1.00 265.46 ?  147 PRO I CD  1 
ATOM   18649 N N   . VAL J  6 169 ? 56.214  33.688  260.370 1.00 256.53 ?  148 VAL I N   1 
ATOM   18650 C CA  . VAL J  6 169 ? 57.145  34.573  261.058 1.00 258.39 ?  148 VAL I CA  1 
ATOM   18651 C C   . VAL J  6 169 ? 58.275  34.915  260.095 1.00 258.44 ?  148 VAL I C   1 
ATOM   18652 O O   . VAL J  6 169 ? 58.976  34.017  259.615 1.00 260.70 ?  148 VAL I O   1 
ATOM   18653 C CB  . VAL J  6 169 ? 57.704  33.938  262.342 1.00 265.57 ?  148 VAL I CB  1 
ATOM   18654 C CG1 . VAL J  6 169 ? 58.934  34.679  262.803 1.00 271.61 ?  148 VAL I CG1 1 
ATOM   18655 C CG2 . VAL J  6 169 ? 56.651  33.952  263.434 1.00 267.59 ?  148 VAL I CG2 1 
ATOM   18656 N N   . THR J  6 170 ? 58.452  36.205  259.811 1.00 266.50 ?  149 THR I N   1 
ATOM   18657 C CA  . THR J  6 170 ? 59.512  36.682  258.926 1.00 267.50 ?  149 THR I CA  1 
ATOM   18658 C C   . THR J  6 170 ? 60.771  36.930  259.749 1.00 275.75 ?  149 THR I C   1 
ATOM   18659 O O   . THR J  6 170 ? 60.741  37.695  260.720 1.00 277.37 ?  149 THR I O   1 
ATOM   18660 C CB  . THR J  6 170 ? 59.093  37.942  258.170 1.00 256.47 ?  149 THR I CB  1 
ATOM   18661 O OG1 . THR J  6 170 ? 58.766  38.981  259.096 1.00 253.58 ?  149 THR I OG1 1 
ATOM   18662 C CG2 . THR J  6 170 ? 57.883  37.659  257.296 1.00 247.38 ?  149 THR I CG2 1 
ATOM   18663 N N   . VAL J  6 171 ? 61.873  36.291  259.367 1.00 248.47 ?  150 VAL I N   1 
ATOM   18664 C CA  . VAL J  6 171 ? 63.134  36.402  260.089 1.00 255.64 ?  150 VAL I CA  1 
ATOM   18665 C C   . VAL J  6 171 ? 64.211  36.930  259.155 1.00 254.40 ?  150 VAL I C   1 
ATOM   18666 O O   . VAL J  6 171 ? 64.517  36.306  258.131 1.00 257.93 ?  150 VAL I O   1 
ATOM   18667 C CB  . VAL J  6 171 ? 63.573  35.060  260.694 1.00 265.75 ?  150 VAL I CB  1 
ATOM   18668 C CG1 . VAL J  6 171 ? 64.934  35.214  261.364 1.00 273.73 ?  150 VAL I CG1 1 
ATOM   18669 C CG2 . VAL J  6 171 ? 62.538  34.564  261.688 1.00 268.62 ?  150 VAL I CG2 1 
ATOM   18670 N N   . SER J  6 172 ? 64.782  38.080  259.509 1.00 244.58 ?  151 SER I N   1 
ATOM   18671 C CA  . SER J  6 172 ? 65.860  38.687  258.750 1.00 243.06 ?  151 SER I CA  1 
ATOM   18672 C C   . SER J  6 172 ? 67.062  38.841  259.671 1.00 245.59 ?  151 SER I C   1 
ATOM   18673 O O   . SER J  6 172 ? 66.947  38.763  260.896 1.00 248.25 ?  151 SER I O   1 
ATOM   18674 C CB  . SER J  6 172 ? 65.458  40.053  258.170 1.00 240.68 ?  151 SER I CB  1 
ATOM   18675 O OG  . SER J  6 172 ? 65.099  40.973  259.188 1.00 242.09 ?  151 SER I OG  1 
ATOM   18676 N N   . TRP J  6 173 ? 68.218  39.067  259.067 1.00 242.87 ?  152 TRP I N   1 
ATOM   18677 C CA  . TRP J  6 173 ? 69.475  39.198  259.789 1.00 249.69 ?  152 TRP I CA  1 
ATOM   18678 C C   . TRP J  6 173 ? 70.122  40.550  259.542 1.00 248.49 ?  152 TRP I C   1 
ATOM   18679 O O   . TRP J  6 173 ? 70.287  40.968  258.391 1.00 245.24 ?  152 TRP I O   1 
ATOM   18680 C CB  . TRP J  6 173 ? 70.422  38.050  259.449 1.00 256.62 ?  152 TRP I CB  1 
ATOM   18681 C CG  . TRP J  6 173 ? 69.941  36.739  259.984 1.00 259.40 ?  152 TRP I CG  1 
ATOM   18682 C CD1 . TRP J  6 173 ? 68.995  35.916  259.447 1.00 256.78 ?  152 TRP I CD1 1 
ATOM   18683 C CD2 . TRP J  6 173 ? 70.416  36.088  261.168 1.00 265.68 ?  152 TRP I CD2 1 
ATOM   18684 N NE1 . TRP J  6 173 ? 68.841  34.798  260.237 1.00 261.36 ?  152 TRP I NE1 1 
ATOM   18685 C CE2 . TRP J  6 173 ? 69.707  34.879  261.296 1.00 266.77 ?  152 TRP I CE2 1 
ATOM   18686 C CE3 . TRP J  6 173 ? 71.375  36.415  262.133 1.00 272.01 ?  152 TRP I CE3 1 
ATOM   18687 C CZ2 . TRP J  6 173 ? 69.925  33.995  262.353 1.00 272.61 ?  152 TRP I CZ2 1 
ATOM   18688 C CZ3 . TRP J  6 173 ? 71.590  35.539  263.180 1.00 277.71 ?  152 TRP I CZ3 1 
ATOM   18689 C CH2 . TRP J  6 173 ? 70.870  34.342  263.281 1.00 277.04 ?  152 TRP I CH2 1 
ATOM   18690 N N   . ASN J  6 174 ? 70.474  41.224  260.638 1.00 255.73 ?  153 ASN I N   1 
ATOM   18691 C CA  . ASN J  6 174 ? 71.090  42.548  260.620 1.00 258.66 ?  153 ASN I CA  1 
ATOM   18692 C C   . ASN J  6 174 ? 70.245  43.539  259.817 1.00 248.35 ?  153 ASN I C   1 
ATOM   18693 O O   . ASN J  6 174 ? 70.757  44.325  259.016 1.00 247.28 ?  153 ASN I O   1 
ATOM   18694 C CB  . ASN J  6 174 ? 72.520  42.459  260.071 1.00 265.46 ?  153 ASN I CB  1 
ATOM   18695 C CG  . ASN J  6 174 ? 73.578  42.461  261.172 1.00 270.43 ?  153 ASN I CG  1 
ATOM   18696 O OD1 . ASN J  6 174 ? 73.397  43.072  262.224 1.00 269.75 ?  153 ASN I OD1 1 
ATOM   18697 N ND2 . ASN J  6 174 ? 74.685  41.762  260.931 1.00 270.02 ?  153 ASN I ND2 1 
ATOM   18698 N N   . SER J  6 175 ? 68.928  43.493  260.047 1.00 233.75 ?  154 SER I N   1 
ATOM   18699 C CA  . SER J  6 175 ? 67.948  44.356  259.376 1.00 231.24 ?  154 SER I CA  1 
ATOM   18700 C C   . SER J  6 175 ? 67.988  44.202  257.858 1.00 228.11 ?  154 SER I C   1 
ATOM   18701 O O   . SER J  6 175 ? 67.683  45.139  257.118 1.00 225.80 ?  154 SER I O   1 
ATOM   18702 C CB  . SER J  6 175 ? 68.142  45.822  259.775 1.00 231.28 ?  154 SER I CB  1 
ATOM   18703 O OG  . SER J  6 175 ? 67.361  46.682  258.965 1.00 228.62 ?  154 SER I OG  1 
ATOM   18704 N N   . GLY J  6 176 ? 68.358  43.017  257.393 1.00 228.13 ?  155 GLY I N   1 
ATOM   18705 C CA  . GLY J  6 176 ? 68.405  42.697  255.983 1.00 225.38 ?  155 GLY I CA  1 
ATOM   18706 C C   . GLY J  6 176 ? 69.741  42.933  255.317 1.00 224.58 ?  155 GLY I C   1 
ATOM   18707 O O   . GLY J  6 176 ? 69.810  42.920  254.082 1.00 222.05 ?  155 GLY I O   1 
ATOM   18708 N N   . ALA J  6 177 ? 70.801  43.148  256.095 1.00 238.91 ?  156 ALA I N   1 
ATOM   18709 C CA  . ALA J  6 177 ? 72.149  43.377  255.596 1.00 241.48 ?  156 ALA I CA  1 
ATOM   18710 C C   . ALA J  6 177 ? 72.944  42.082  255.519 1.00 249.76 ?  156 ALA I C   1 
ATOM   18711 O O   . ALA J  6 177 ? 74.179  42.122  255.476 1.00 254.28 ?  156 ALA I O   1 
ATOM   18712 C CB  . ALA J  6 177 ? 72.882  44.396  256.473 1.00 246.47 ?  156 ALA I CB  1 
ATOM   18713 N N   . LEU J  6 178 ? 72.258  40.936  255.495 1.00 241.86 ?  157 LEU I N   1 
ATOM   18714 C CA  . LEU J  6 178 ? 72.936  39.642  255.438 1.00 250.37 ?  157 LEU I CA  1 
ATOM   18715 C C   . LEU J  6 178 ? 71.992  38.611  254.820 1.00 247.44 ?  157 LEU I C   1 
ATOM   18716 O O   . LEU J  6 178 ? 71.107  38.093  255.506 1.00 246.41 ?  157 LEU I O   1 
ATOM   18717 C CB  . LEU J  6 178 ? 73.377  39.211  256.827 1.00 257.57 ?  157 LEU I CB  1 
ATOM   18718 C CG  . LEU J  6 178 ? 74.198  37.927  256.943 1.00 265.20 ?  157 LEU I CG  1 
ATOM   18719 C CD1 . LEU J  6 178 ? 75.459  38.017  256.102 1.00 268.97 ?  157 LEU I CD1 1 
ATOM   18720 C CD2 . LEU J  6 178 ? 74.528  37.643  258.398 1.00 269.29 ?  157 LEU I CD2 1 
ATOM   18721 N N   . THR J  6 179 ? 72.181  38.341  253.528 1.00 245.49 ?  158 THR I N   1 
ATOM   18722 C CA  . THR J  6 179 ? 71.352  37.397  252.794 1.00 242.53 ?  158 THR I CA  1 
ATOM   18723 C C   . THR J  6 179 ? 72.154  36.220  252.258 1.00 249.65 ?  158 THR I C   1 
ATOM   18724 O O   . THR J  6 179 ? 71.582  35.342  251.602 1.00 248.62 ?  158 THR I O   1 
ATOM   18725 C CB  . THR J  6 179 ? 70.644  38.102  251.627 1.00 231.81 ?  158 THR I CB  1 
ATOM   18726 O OG1 . THR J  6 179 ? 69.841  37.158  250.909 1.00 232.46 ?  158 THR I OG1 1 
ATOM   18727 C CG2 . THR J  6 179 ? 71.665  38.703  250.673 1.00 224.63 ?  158 THR I CG2 1 
ATOM   18728 N N   . SER J  6 180 ? 73.456  36.175  252.521 1.00 240.74 ?  159 SER I N   1 
ATOM   18729 C CA  . SER J  6 180 ? 74.335  35.114  252.045 1.00 247.24 ?  159 SER I CA  1 
ATOM   18730 C C   . SER J  6 180 ? 74.606  34.112  253.163 1.00 255.52 ?  159 SER I C   1 
ATOM   18731 O O   . SER J  6 180 ? 75.162  34.474  254.206 1.00 259.31 ?  159 SER I O   1 
ATOM   18732 C CB  . SER J  6 180 ? 75.642  35.702  251.519 1.00 250.78 ?  159 SER I CB  1 
ATOM   18733 O OG  . SER J  6 180 ? 76.287  36.454  252.530 1.00 258.99 ?  159 SER I OG  1 
ATOM   18734 N N   . GLY J  6 181 ? 74.202  32.862  252.950 1.00 249.54 ?  160 GLY I N   1 
ATOM   18735 C CA  . GLY J  6 181 ? 74.416  31.802  253.916 1.00 255.56 ?  160 GLY I CA  1 
ATOM   18736 C C   . GLY J  6 181 ? 73.306  31.610  254.921 1.00 252.47 ?  160 GLY I C   1 
ATOM   18737 O O   . GLY J  6 181 ? 73.500  30.888  255.907 1.00 257.16 ?  160 GLY I O   1 
ATOM   18738 N N   . VAL J  6 182 ? 72.159  32.235  254.708 1.00 258.60 ?  161 VAL I N   1 
ATOM   18739 C CA  . VAL J  6 182 ? 71.022  32.139  255.613 1.00 255.48 ?  161 VAL I CA  1 
ATOM   18740 C C   . VAL J  6 182 ? 70.107  31.016  255.137 1.00 254.77 ?  161 VAL I C   1 
ATOM   18741 O O   . VAL J  6 182 ? 69.710  30.987  253.966 1.00 251.05 ?  161 VAL I O   1 
ATOM   18742 C CB  . VAL J  6 182 ? 70.269  33.477  255.689 1.00 247.60 ?  161 VAL I CB  1 
ATOM   18743 C CG1 . VAL J  6 182 ? 69.161  33.395  256.713 1.00 248.46 ?  161 VAL I CG1 1 
ATOM   18744 C CG2 . VAL J  6 182 ? 71.230  34.617  256.023 1.00 246.12 ?  161 VAL I CG2 1 
ATOM   18745 N N   . HIS J  6 183 ? 69.777  30.085  256.035 1.00 264.57 ?  162 HIS I N   1 
ATOM   18746 C CA  . HIS J  6 183 ? 68.890  28.959  255.728 1.00 266.05 ?  162 HIS I CA  1 
ATOM   18747 C C   . HIS J  6 183 ? 67.834  28.893  256.831 1.00 260.05 ?  162 HIS I C   1 
ATOM   18748 O O   . HIS J  6 183 ? 68.104  28.408  257.934 1.00 262.31 ?  162 HIS I O   1 
ATOM   18749 C CB  . HIS J  6 183 ? 69.652  27.634  255.617 1.00 275.03 ?  162 HIS I CB  1 
ATOM   18750 C CG  . HIS J  6 183 ? 70.524  27.524  254.402 1.00 280.24 ?  162 HIS I CG  1 
ATOM   18751 N ND1 . HIS J  6 183 ? 70.298  28.254  253.255 1.00 277.50 ?  162 HIS I ND1 1 
ATOM   18752 C CD2 . HIS J  6 183 ? 71.594  26.735  254.139 1.00 286.84 ?  162 HIS I CD2 1 
ATOM   18753 C CE1 . HIS J  6 183 ? 71.208  27.942  252.349 1.00 280.94 ?  162 HIS I CE1 1 
ATOM   18754 N NE2 . HIS J  6 183 ? 72.005  27.021  252.859 1.00 285.60 ?  162 HIS I NE2 1 
ATOM   18755 N N   . THR J  6 184 ? 66.635  29.388  256.523 1.00 264.15 ?  163 THR I N   1 
ATOM   18756 C CA  . THR J  6 184 ? 65.508  29.379  257.449 1.00 260.83 ?  163 THR I CA  1 
ATOM   18757 C C   . THR J  6 184 ? 64.689  28.108  257.250 1.00 264.03 ?  163 THR I C   1 
ATOM   18758 O O   . THR J  6 184 ? 64.230  27.829  256.137 1.00 262.47 ?  163 THR I O   1 
ATOM   18759 C CB  . THR J  6 184 ? 64.634  30.614  257.234 1.00 249.77 ?  163 THR I CB  1 
ATOM   18760 O OG1 . THR J  6 184 ? 65.415  31.796  257.453 1.00 249.43 ?  163 THR I OG1 1 
ATOM   18761 C CG2 . THR J  6 184 ? 63.452  30.606  258.191 1.00 241.63 ?  163 THR I CG2 1 
ATOM   18762 N N   . PHE J  6 185 ? 64.521  27.320  258.341 1.00 261.70 ?  164 PHE I N   1 
ATOM   18763 C CA  . PHE J  6 185 ? 63.811  26.049  258.349 1.00 265.31 ?  164 PHE I CA  1 
ATOM   18764 C C   . PHE J  6 185 ? 62.323  26.207  258.663 1.00 257.39 ?  164 PHE I C   1 
ATOM   18765 O O   . PHE J  6 185 ? 61.927  27.108  259.409 1.00 250.70 ?  164 PHE I O   1 
ATOM   18766 C CB  . PHE J  6 185 ? 64.449  25.098  259.357 1.00 273.07 ?  164 PHE I CB  1 
ATOM   18767 C CG  . PHE J  6 185 ? 65.854  24.706  259.003 1.00 278.79 ?  164 PHE I CG  1 
ATOM   18768 C CD1 . PHE J  6 185 ? 66.932  25.469  259.419 1.00 280.28 ?  164 PHE I CD1 1 
ATOM   18769 C CD2 . PHE J  6 185 ? 66.093  23.580  258.233 1.00 283.92 ?  164 PHE I CD2 1 
ATOM   18770 C CE1 . PHE J  6 185 ? 68.226  25.107  259.084 1.00 284.40 ?  164 PHE I CE1 1 
ATOM   18771 C CE2 . PHE J  6 185 ? 67.382  23.213  257.894 1.00 290.74 ?  164 PHE I CE2 1 
ATOM   18772 C CZ  . PHE J  6 185 ? 68.450  23.978  258.320 1.00 290.26 ?  164 PHE I CZ  1 
ATOM   18773 N N   . PRO J  6 186 ? 61.508  25.328  258.081 1.00 248.00 ?  165 PRO I N   1 
ATOM   18774 C CA  . PRO J  6 186 ? 60.066  25.325  258.358 1.00 250.17 ?  165 PRO I CA  1 
ATOM   18775 C C   . PRO J  6 186 ? 59.747  24.958  259.801 1.00 256.82 ?  165 PRO I C   1 
ATOM   18776 O O   . PRO J  6 186 ? 60.430  24.146  260.430 1.00 259.72 ?  165 PRO I O   1 
ATOM   18777 C CB  . PRO J  6 186 ? 59.520  24.279  257.380 1.00 248.59 ?  165 PRO I CB  1 
ATOM   18778 C CG  . PRO J  6 186 ? 60.682  23.404  257.084 1.00 248.44 ?  165 PRO I CG  1 
ATOM   18779 C CD  . PRO J  6 186 ? 61.875  24.306  257.089 1.00 245.70 ?  165 PRO I CD  1 
ATOM   18780 N N   . ALA J  6 187 ? 58.687  25.577  260.322 1.00 258.04 ?  166 ALA I N   1 
ATOM   18781 C CA  . ALA J  6 187 ? 58.266  25.400  261.706 1.00 262.98 ?  166 ALA I CA  1 
ATOM   18782 C C   . ALA J  6 187 ? 57.721  23.996  261.954 1.00 265.69 ?  166 ALA I C   1 
ATOM   18783 O O   . ALA J  6 187 ? 57.477  23.210  261.034 1.00 264.24 ?  166 ALA I O   1 
ATOM   18784 C CB  . ALA J  6 187 ? 57.192  26.422  262.077 1.00 263.71 ?  166 ALA I CB  1 
ATOM   18785 N N   . VAL J  6 188 ? 57.533  23.693  263.238 1.00 271.61 ?  167 VAL I N   1 
ATOM   18786 C CA  . VAL J  6 188 ? 56.991  22.424  263.704 1.00 274.18 ?  167 VAL I CA  1 
ATOM   18787 C C   . VAL J  6 188 ? 55.760  22.680  264.565 1.00 276.71 ?  167 VAL I C   1 
ATOM   18788 O O   . VAL J  6 188 ? 55.786  23.517  265.475 1.00 277.91 ?  167 VAL I O   1 
ATOM   18789 C CB  . VAL J  6 188 ? 58.036  21.592  264.475 1.00 275.36 ?  167 VAL I CB  1 
ATOM   18790 C CG1 . VAL J  6 188 ? 58.699  22.421  265.538 1.00 276.78 ?  167 VAL I CG1 1 
ATOM   18791 C CG2 . VAL J  6 188 ? 57.389  20.353  265.092 1.00 277.64 ?  167 VAL I CG2 1 
ATOM   18792 N N   . LEU J  6 189 ? 54.689  21.948  264.269 1.00 283.96 ?  168 LEU I N   1 
ATOM   18793 C CA  . LEU J  6 189 ? 53.415  21.998  264.985 1.00 289.81 ?  168 LEU I CA  1 
ATOM   18794 C C   . LEU J  6 189 ? 53.556  21.143  266.232 1.00 289.77 ?  168 LEU I C   1 
ATOM   18795 O O   . LEU J  6 189 ? 53.632  19.918  266.138 1.00 286.70 ?  168 LEU I O   1 
ATOM   18796 C CB  . LEU J  6 189 ? 52.255  21.486  264.136 1.00 289.39 ?  168 LEU I CB  1 
ATOM   18797 C CG  . LEU J  6 189 ? 50.939  21.558  264.936 1.00 286.85 ?  168 LEU I CG  1 
ATOM   18798 C CD1 . LEU J  6 189 ? 50.449  22.998  265.106 1.00 286.28 ?  168 LEU I CD1 1 
ATOM   18799 C CD2 . LEU J  6 189 ? 49.821  20.623  264.397 1.00 281.11 ?  168 LEU I CD2 1 
ATOM   18800 N N   . GLN J  6 190 ? 53.588  21.772  267.405 1.00 292.38 ?  169 GLN I N   1 
ATOM   18801 C CA  . GLN J  6 190 ? 53.741  20.964  268.599 1.00 295.95 ?  169 GLN I CA  1 
ATOM   18802 C C   . GLN J  6 190 ? 52.450  20.210  268.890 1.00 298.63 ?  169 GLN I C   1 
ATOM   18803 O O   . GLN J  6 190 ? 51.414  20.414  268.248 1.00 297.37 ?  169 GLN I O   1 
ATOM   18804 C CB  . GLN J  6 190 ? 53.986  21.860  269.812 1.00 296.68 ?  169 GLN I CB  1 
ATOM   18805 C CG  . GLN J  6 190 ? 55.206  22.746  269.808 1.00 284.53 ?  169 GLN I CG  1 
ATOM   18806 C CD  . GLN J  6 190 ? 55.248  23.636  271.041 1.00 285.60 ?  169 GLN I CD  1 
ATOM   18807 O OE1 . GLN J  6 190 ? 54.309  23.656  271.842 1.00 289.80 ?  169 GLN I OE1 1 
ATOM   18808 N NE2 . GLN J  6 190 ? 56.321  24.402  271.180 1.00 282.32 ?  169 GLN I NE2 1 
ATOM   18809 N N   . SER J  6 191 ? 52.510  19.319  269.884 1.00 289.30 ?  170 SER I N   1 
ATOM   18810 C CA  . SER J  6 191 ? 51.307  18.577  270.227 1.00 291.15 ?  170 SER I CA  1 
ATOM   18811 C C   . SER J  6 191 ? 50.320  19.497  270.920 1.00 293.36 ?  170 SER I C   1 
ATOM   18812 O O   . SER J  6 191 ? 49.118  19.214  270.950 1.00 295.12 ?  170 SER I O   1 
ATOM   18813 C CB  . SER J  6 191 ? 51.656  17.369  271.095 1.00 292.21 ?  170 SER I CB  1 
ATOM   18814 O OG  . SER J  6 191 ? 52.273  17.776  272.300 1.00 294.04 ?  170 SER I OG  1 
ATOM   18815 N N   . SER J  6 192 ? 50.834  20.589  271.485 1.00 297.88 ?  171 SER I N   1 
ATOM   18816 C CA  . SER J  6 192 ? 50.074  21.614  272.178 1.00 295.74 ?  171 SER I CA  1 
ATOM   18817 C C   . SER J  6 192 ? 49.348  22.530  271.203 1.00 298.11 ?  171 SER I C   1 
ATOM   18818 O O   . SER J  6 192 ? 48.444  23.266  271.618 1.00 296.17 ?  171 SER I O   1 
ATOM   18819 C CB  . SER J  6 192 ? 51.002  22.428  273.083 1.00 286.99 ?  171 SER I CB  1 
ATOM   18820 O OG  . SER J  6 192 ? 52.029  23.041  272.324 1.00 283.33 ?  171 SER I OG  1 
ATOM   18821 N N   . GLY J  6 193 ? 49.726  22.500  269.924 1.00 310.45 ?  172 GLY I N   1 
ATOM   18822 C CA  . GLY J  6 193 ? 49.105  23.335  268.917 1.00 306.51 ?  172 GLY I CA  1 
ATOM   18823 C C   . GLY J  6 193 ? 49.844  24.626  268.633 1.00 302.79 ?  172 GLY I C   1 
ATOM   18824 O O   . GLY J  6 193 ? 49.218  25.590  268.179 1.00 298.56 ?  172 GLY I O   1 
ATOM   18825 N N   . LEU J  6 194 ? 51.145  24.678  268.917 1.00 295.36 ?  173 LEU I N   1 
ATOM   18826 C CA  . LEU J  6 194 ? 51.986  25.853  268.725 1.00 291.29 ?  173 LEU I CA  1 
ATOM   18827 C C   . LEU J  6 194 ? 53.156  25.575  267.783 1.00 287.27 ?  173 LEU I C   1 
ATOM   18828 O O   . LEU J  6 194 ? 53.736  24.485  267.808 1.00 288.17 ?  173 LEU I O   1 
ATOM   18829 C CB  . LEU J  6 194 ? 52.535  26.285  270.087 1.00 291.61 ?  173 LEU I CB  1 
ATOM   18830 C CG  . LEU J  6 194 ? 51.487  26.717  271.116 1.00 293.65 ?  173 LEU I CG  1 
ATOM   18831 C CD1 . LEU J  6 194 ? 52.126  26.953  272.481 1.00 286.70 ?  173 LEU I CD1 1 
ATOM   18832 C CD2 . LEU J  6 194 ? 50.737  27.948  270.646 1.00 289.39 ?  173 LEU I CD2 1 
ATOM   18833 N N   . TYR J  6 195 ? 53.476  26.543  266.921 1.00 284.38 ?  174 TYR I N   1 
ATOM   18834 C CA  . TYR J  6 195 ? 54.585  26.418  265.979 1.00 278.86 ?  174 TYR I CA  1 
ATOM   18835 C C   . TYR J  6 195 ? 55.908  26.860  266.621 1.00 275.99 ?  174 TYR I C   1 
ATOM   18836 O O   . TYR J  6 195 ? 55.934  27.530  267.655 1.00 279.71 ?  174 TYR I O   1 
ATOM   18837 C CB  . TYR J  6 195 ? 54.332  27.186  264.678 1.00 271.84 ?  174 TYR I CB  1 
ATOM   18838 C CG  . TYR J  6 195 ? 53.139  26.724  263.855 1.00 271.95 ?  174 TYR I CG  1 
ATOM   18839 C CD1 . TYR J  6 195 ? 53.266  25.641  262.988 1.00 273.34 ?  174 TYR I CD1 1 
ATOM   18840 C CD2 . TYR J  6 195 ? 51.921  27.390  263.891 1.00 275.13 ?  174 TYR I CD2 1 
ATOM   18841 C CE1 . TYR J  6 195 ? 52.208  25.213  262.208 1.00 276.45 ?  174 TYR I CE1 1 
ATOM   18842 C CE2 . TYR J  6 195 ? 50.852  26.968  263.107 1.00 280.02 ?  174 TYR I CE2 1 
ATOM   18843 C CZ  . TYR J  6 195 ? 51.004  25.879  262.269 1.00 280.22 ?  174 TYR I CZ  1 
ATOM   18844 O OH  . TYR J  6 195 ? 49.948  25.457  261.492 1.00 282.83 ?  174 TYR I OH  1 
ATOM   18845 N N   . SER J  6 196 ? 57.014  26.464  265.983 1.00 269.13 ?  175 SER I N   1 
ATOM   18846 C CA  . SER J  6 196 ? 58.374  26.761  266.450 1.00 267.87 ?  175 SER I CA  1 
ATOM   18847 C C   . SER J  6 196 ? 59.346  26.616  265.283 1.00 265.77 ?  175 SER I C   1 
ATOM   18848 O O   . SER J  6 196 ? 59.411  25.539  264.682 1.00 266.97 ?  175 SER I O   1 
ATOM   18849 C CB  . SER J  6 196 ? 58.771  25.853  267.616 1.00 270.77 ?  175 SER I CB  1 
ATOM   18850 O OG  . SER J  6 196 ? 59.580  24.778  267.186 1.00 271.00 ?  175 SER I OG  1 
ATOM   18851 N N   . LEU J  6 197 ? 60.103  27.674  264.960 1.00 272.64 ?  176 LEU I N   1 
ATOM   18852 C CA  . LEU J  6 197 ? 61.051  27.654  263.838 1.00 267.35 ?  176 LEU I CA  1 
ATOM   18853 C C   . LEU J  6 197 ? 62.497  27.846  264.296 1.00 273.64 ?  176 LEU I C   1 
ATOM   18854 O O   . LEU J  6 197 ? 62.788  28.010  265.483 1.00 284.41 ?  176 LEU I O   1 
ATOM   18855 C CB  . LEU J  6 197 ? 60.781  28.857  262.924 1.00 259.80 ?  176 LEU I CB  1 
ATOM   18856 C CG  . LEU J  6 197 ? 59.638  29.336  262.035 1.00 250.24 ?  176 LEU I CG  1 
ATOM   18857 C CD1 . LEU J  6 197 ? 59.964  30.765  261.651 1.00 251.49 ?  176 LEU I CD1 1 
ATOM   18858 C CD2 . LEU J  6 197 ? 59.560  28.552  260.769 1.00 238.49 ?  176 LEU I CD2 1 
ATOM   18859 N N   . SER J  6 198 ? 63.408  27.808  263.312 1.00 265.69 ?  177 SER I N   1 
ATOM   18860 C CA  . SER J  6 198 ? 64.839  28.017  263.514 1.00 266.72 ?  177 SER I CA  1 
ATOM   18861 C C   . SER J  6 198 ? 65.456  28.592  262.241 1.00 263.71 ?  177 SER I C   1 
ATOM   18862 O O   . SER J  6 198 ? 64.965  28.340  261.136 1.00 261.17 ?  177 SER I O   1 
ATOM   18863 C CB  . SER J  6 198 ? 65.552  26.708  263.879 1.00 269.01 ?  177 SER I CB  1 
ATOM   18864 O OG  . SER J  6 198 ? 65.024  26.148  265.068 1.00 273.44 ?  177 SER I OG  1 
ATOM   18865 N N   . SER J  6 199 ? 66.536  29.364  262.401 1.00 267.94 ?  178 SER I N   1 
ATOM   18866 C CA  . SER J  6 199 ? 67.249  29.976  261.276 1.00 262.52 ?  178 SER I CA  1 
ATOM   18867 C C   . SER J  6 199 ? 68.750  29.997  261.554 1.00 268.82 ?  178 SER I C   1 
ATOM   18868 O O   . SER J  6 199 ? 69.178  30.650  262.510 1.00 274.24 ?  178 SER I O   1 
ATOM   18869 C CB  . SER J  6 199 ? 66.731  31.391  261.003 1.00 256.90 ?  178 SER I CB  1 
ATOM   18870 O OG  . SER J  6 199 ? 67.365  31.960  259.870 1.00 249.61 ?  178 SER I OG  1 
ATOM   18871 N N   . VAL J  6 200 ? 69.555  29.307  260.739 1.00 258.92 ?  179 VAL I N   1 
ATOM   18872 C CA  . VAL J  6 200 ? 71.003  29.258  260.955 1.00 266.36 ?  179 VAL I CA  1 
ATOM   18873 C C   . VAL J  6 200 ? 71.740  30.002  259.843 1.00 263.01 ?  179 VAL I C   1 
ATOM   18874 O O   . VAL J  6 200 ? 71.250  30.116  258.713 1.00 257.51 ?  179 VAL I O   1 
ATOM   18875 C CB  . VAL J  6 200 ? 71.513  27.807  261.060 1.00 274.31 ?  179 VAL I CB  1 
ATOM   18876 C CG1 . VAL J  6 200 ? 70.901  27.134  262.265 1.00 274.35 ?  179 VAL I CG1 1 
ATOM   18877 C CG2 . VAL J  6 200 ? 71.198  27.035  259.785 1.00 270.72 ?  179 VAL I CG2 1 
ATOM   18878 N N   . VAL J  6 201 ? 72.931  30.518  260.178 1.00 254.86 ?  180 VAL I N   1 
ATOM   18879 C CA  . VAL J  6 201 ? 73.794  31.243  259.244 1.00 253.93 ?  180 VAL I CA  1 
ATOM   18880 C C   . VAL J  6 201 ? 75.216  30.687  259.311 1.00 260.38 ?  180 VAL I C   1 
ATOM   18881 O O   . VAL J  6 201 ? 75.814  30.628  260.392 1.00 265.55 ?  180 VAL I O   1 
ATOM   18882 C CB  . VAL J  6 201 ? 73.807  32.758  259.534 1.00 252.18 ?  180 VAL I CB  1 
ATOM   18883 C CG1 . VAL J  6 201 ? 74.729  33.482  258.554 1.00 251.61 ?  180 VAL I CG1 1 
ATOM   18884 C CG2 . VAL J  6 201 ? 72.387  33.339  259.484 1.00 246.51 ?  180 VAL I CG2 1 
ATOM   18885 N N   . THR J  6 202 ? 75.757  30.294  258.153 1.00 245.26 ?  181 THR I N   1 
ATOM   18886 C CA  . THR J  6 202 ? 77.127  29.792  258.034 1.00 254.85 ?  181 THR I CA  1 
ATOM   18887 C C   . THR J  6 202 ? 78.075  30.986  257.945 1.00 261.10 ?  181 THR I C   1 
ATOM   18888 O O   . THR J  6 202 ? 78.103  31.685  256.927 1.00 255.12 ?  181 THR I O   1 
ATOM   18889 C CB  . THR J  6 202 ? 77.269  28.872  256.822 1.00 249.07 ?  181 THR I CB  1 
ATOM   18890 O OG1 . THR J  6 202 ? 76.909  29.575  255.624 1.00 241.15 ?  181 THR I OG1 1 
ATOM   18891 C CG2 . THR J  6 202 ? 76.385  27.640  256.973 1.00 243.74 ?  181 THR I CG2 1 
ATOM   18892 N N   . VAL J  6 203 ? 78.856  31.226  258.995 1.00 263.60 ?  182 VAL I N   1 
ATOM   18893 C CA  . VAL J  6 203 ? 79.766  32.372  259.004 1.00 265.91 ?  182 VAL I CA  1 
ATOM   18894 C C   . VAL J  6 203 ? 81.210  31.966  259.280 1.00 278.58 ?  182 VAL I C   1 
ATOM   18895 O O   . VAL J  6 203 ? 81.460  30.950  259.946 1.00 282.79 ?  182 VAL I O   1 
ATOM   18896 C CB  . VAL J  6 203 ? 79.316  33.429  260.026 1.00 255.39 ?  182 VAL I CB  1 
ATOM   18897 C CG1 . VAL J  6 203 ? 78.039  34.086  259.575 1.00 241.50 ?  182 VAL I CG1 1 
ATOM   18898 C CG2 . VAL J  6 203 ? 79.132  32.804  261.395 1.00 253.99 ?  182 VAL I CG2 1 
ATOM   18899 N N   . PRO J  6 204 ? 82.182  32.729  258.778 1.00 267.04 ?  183 PRO I N   1 
ATOM   18900 C CA  . PRO J  6 204 ? 83.590  32.436  259.069 1.00 276.11 ?  183 PRO I CA  1 
ATOM   18901 C C   . PRO J  6 204 ? 83.888  32.551  260.556 1.00 282.70 ?  183 PRO I C   1 
ATOM   18902 O O   . PRO J  6 204 ? 83.322  33.387  261.264 1.00 280.08 ?  183 PRO I O   1 
ATOM   18903 C CB  . PRO J  6 204 ? 84.350  33.497  258.263 1.00 272.01 ?  183 PRO I CB  1 
ATOM   18904 C CG  . PRO J  6 204 ? 83.358  34.578  258.017 1.00 258.73 ?  183 PRO I CG  1 
ATOM   18905 C CD  . PRO J  6 204 ? 82.043  33.881  257.871 1.00 257.89 ?  183 PRO I CD  1 
ATOM   18906 N N   . SER J  6 205 ? 84.793  31.687  261.025 1.00 292.23 ?  184 SER I N   1 
ATOM   18907 C CA  . SER J  6 205 ? 85.129  31.648  262.445 1.00 297.26 ?  184 SER I CA  1 
ATOM   18908 C C   . SER J  6 205 ? 85.713  32.974  262.919 1.00 298.31 ?  184 SER I C   1 
ATOM   18909 O O   . SER J  6 205 ? 85.621  33.304  264.107 1.00 299.74 ?  184 SER I O   1 
ATOM   18910 C CB  . SER J  6 205 ? 86.122  30.513  262.721 1.00 306.22 ?  184 SER I CB  1 
ATOM   18911 O OG  . SER J  6 205 ? 85.618  29.253  262.309 1.00 306.02 ?  184 SER I OG  1 
ATOM   18912 N N   . SER J  6 206 ? 86.322  33.738  262.012 1.00 294.60 ?  185 SER I N   1 
ATOM   18913 C CA  . SER J  6 206 ? 86.908  35.041  262.323 1.00 295.71 ?  185 SER I CA  1 
ATOM   18914 C C   . SER J  6 206 ? 85.801  36.054  262.612 1.00 288.47 ?  185 SER I C   1 
ATOM   18915 O O   . SER J  6 206 ? 85.397  36.845  261.756 1.00 283.13 ?  185 SER I O   1 
ATOM   18916 C CB  . SER J  6 206 ? 87.782  35.515  261.167 1.00 297.32 ?  185 SER I CB  1 
ATOM   18917 O OG  . SER J  6 206 ? 87.015  35.650  259.980 1.00 290.45 ?  185 SER I OG  1 
ATOM   18918 N N   . SER J  6 207 ? 85.278  36.019  263.838 1.00 284.22 ?  186 SER I N   1 
ATOM   18919 C CA  . SER J  6 207 ? 84.214  36.952  264.199 1.00 283.37 ?  186 SER I CA  1 
ATOM   18920 C C   . SER J  6 207 ? 84.436  37.507  265.604 1.00 286.14 ?  186 SER I C   1 
ATOM   18921 O O   . SER J  6 207 ? 83.523  37.563  266.429 1.00 287.16 ?  186 SER I O   1 
ATOM   18922 C CB  . SER J  6 207 ? 82.850  36.269  264.105 1.00 282.62 ?  186 SER I CB  1 
ATOM   18923 O OG  . SER J  6 207 ? 82.620  35.758  262.805 1.00 280.05 ?  186 SER I OG  1 
ATOM   18924 N N   . LEU J  6 208 ? 85.675  37.920  265.889 1.00 302.82 ?  187 LEU I N   1 
ATOM   18925 C CA  . LEU J  6 208 ? 85.971  38.581  267.157 1.00 309.63 ?  187 LEU I CA  1 
ATOM   18926 C C   . LEU J  6 208 ? 85.245  39.917  267.248 1.00 307.37 ?  187 LEU I C   1 
ATOM   18927 O O   . LEU J  6 208 ? 84.648  40.251  268.278 1.00 308.93 ?  187 LEU I O   1 
ATOM   18928 C CB  . LEU J  6 208 ? 87.481  38.761  267.332 1.00 315.27 ?  187 LEU I CB  1 
ATOM   18929 C CG  . LEU J  6 208 ? 87.993  39.025  268.756 1.00 314.07 ?  187 LEU I CG  1 
ATOM   18930 C CD1 . LEU J  6 208 ? 87.822  40.482  269.193 1.00 325.06 ?  187 LEU I CD1 1 
ATOM   18931 C CD2 . LEU J  6 208 ? 87.294  38.095  269.740 1.00 312.91 ?  187 LEU I CD2 1 
ATOM   18932 N N   . GLY J  6 209 ? 85.303  40.691  266.167 1.00 313.28 ?  188 GLY I N   1 
ATOM   18933 C CA  . GLY J  6 209 ? 84.575  41.932  265.982 1.00 303.52 ?  188 GLY I CA  1 
ATOM   18934 C C   . GLY J  6 209 ? 84.537  43.007  267.058 1.00 311.18 ?  188 GLY I C   1 
ATOM   18935 O O   . GLY J  6 209 ? 85.514  43.731  267.244 1.00 325.18 ?  188 GLY I O   1 
ATOM   18936 N N   . THR J  6 210 ? 83.411  43.129  267.758 1.00 299.15 ?  189 THR I N   1 
ATOM   18937 C CA  . THR J  6 210 ? 82.290  42.214  267.588 1.00 294.40 ?  189 THR I CA  1 
ATOM   18938 C C   . THR J  6 210 ? 81.460  42.491  266.349 1.00 287.35 ?  189 THR I C   1 
ATOM   18939 O O   . THR J  6 210 ? 80.793  43.520  266.243 1.00 283.72 ?  189 THR I O   1 
ATOM   18940 C CB  . THR J  6 210 ? 81.338  42.279  268.800 1.00 293.75 ?  189 THR I CB  1 
ATOM   18941 O OG1 . THR J  6 210 ? 80.843  43.615  268.952 1.00 291.13 ?  189 THR I OG1 1 
ATOM   18942 C CG2 . THR J  6 210 ? 82.065  41.884  270.063 1.00 300.82 ?  189 THR I CG2 1 
ATOM   18943 N N   . GLN J  6 211 ? 81.519  41.557  265.403 1.00 300.71 ?  190 GLN I N   1 
ATOM   18944 C CA  . GLN J  6 211 ? 80.656  41.640  264.239 1.00 291.62 ?  190 GLN I CA  1 
ATOM   18945 C C   . GLN J  6 211 ? 79.263  41.283  264.736 1.00 289.74 ?  190 GLN I C   1 
ATOM   18946 O O   . GLN J  6 211 ? 78.864  40.114  264.709 1.00 293.35 ?  190 GLN I O   1 
ATOM   18947 C CB  . GLN J  6 211 ? 81.149  40.703  263.133 1.00 290.85 ?  190 GLN I CB  1 
ATOM   18948 C CG  . GLN J  6 211 ? 80.289  40.655  261.882 1.00 284.23 ?  190 GLN I CG  1 
ATOM   18949 C CD  . GLN J  6 211 ? 79.798  42.018  261.443 1.00 280.23 ?  190 GLN I CD  1 
ATOM   18950 O OE1 . GLN J  6 211 ? 78.696  42.439  261.794 1.00 276.27 ?  190 GLN I OE1 1 
ATOM   18951 N NE2 . GLN J  6 211 ? 80.617  42.717  260.665 1.00 281.73 ?  190 GLN I NE2 1 
ATOM   18952 N N   . THR J  6 212 ? 78.535  42.290  265.218 1.00 289.50 ?  191 THR I N   1 
ATOM   18953 C CA  . THR J  6 212 ? 77.246  42.101  265.875 1.00 286.71 ?  191 THR I CA  1 
ATOM   18954 C C   . THR J  6 212 ? 76.228  41.424  264.956 1.00 280.87 ?  191 THR I C   1 
ATOM   18955 O O   . THR J  6 212 ? 75.794  42.008  263.957 1.00 276.19 ?  191 THR I O   1 
ATOM   18956 C CB  . THR J  6 212 ? 76.741  43.451  266.411 1.00 285.85 ?  191 THR I CB  1 
ATOM   18957 O OG1 . THR J  6 212 ? 75.415  43.312  266.935 1.00 283.13 ?  191 THR I OG1 1 
ATOM   18958 C CG2 . THR J  6 212 ? 76.784  44.539  265.334 1.00 282.55 ?  191 THR I CG2 1 
ATOM   18959 N N   . TYR J  6 213 ? 75.861  40.180  265.278 1.00 272.83 ?  192 TYR I N   1 
ATOM   18960 C CA  . TYR J  6 213 ? 74.838  39.421  264.551 1.00 267.90 ?  192 TYR I CA  1 
ATOM   18961 C C   . TYR J  6 213 ? 73.512  39.478  265.302 1.00 265.87 ?  192 TYR I C   1 
ATOM   18962 O O   . TYR J  6 213 ? 73.335  38.809  266.323 1.00 268.96 ?  192 TYR I O   1 
ATOM   18963 C CB  . TYR J  6 213 ? 75.286  37.977  264.351 1.00 270.16 ?  192 TYR I CB  1 
ATOM   18964 C CG  . TYR J  6 213 ? 76.486  37.821  263.455 1.00 271.84 ?  192 TYR I CG  1 
ATOM   18965 C CD1 . TYR J  6 213 ? 76.673  38.667  262.374 1.00 268.67 ?  192 TYR I CD1 1 
ATOM   18966 C CD2 . TYR J  6 213 ? 77.427  36.828  263.684 1.00 277.12 ?  192 TYR I CD2 1 
ATOM   18967 C CE1 . TYR J  6 213 ? 77.756  38.527  261.545 1.00 270.67 ?  192 TYR I CE1 1 
ATOM   18968 C CE2 . TYR J  6 213 ? 78.519  36.682  262.860 1.00 279.26 ?  192 TYR I CE2 1 
ATOM   18969 C CZ  . TYR J  6 213 ? 78.681  37.535  261.794 1.00 276.02 ?  192 TYR I CZ  1 
ATOM   18970 O OH  . TYR J  6 213 ? 79.771  37.386  260.971 1.00 278.57 ?  192 TYR I OH  1 
ATOM   18971 N N   . ILE J  6 214 ? 72.581  40.286  264.795 1.00 267.53 ?  193 ILE I N   1 
ATOM   18972 C CA  . ILE J  6 214 ? 71.254  40.448  265.383 1.00 268.10 ?  193 ILE I CA  1 
ATOM   18973 C C   . ILE J  6 214 ? 70.200  39.980  264.380 1.00 264.32 ?  193 ILE I C   1 
ATOM   18974 O O   . ILE J  6 214 ? 70.003  40.616  263.336 1.00 261.76 ?  193 ILE I O   1 
ATOM   18975 C CB  . ILE J  6 214 ? 71.002  41.902  265.812 1.00 268.88 ?  193 ILE I CB  1 
ATOM   18976 C CG1 . ILE J  6 214 ? 72.018  42.328  266.878 1.00 273.08 ?  193 ILE I CG1 1 
ATOM   18977 C CG2 . ILE J  6 214 ? 69.587  42.083  266.327 1.00 265.79 ?  193 ILE I CG2 1 
ATOM   18978 C CD1 . ILE J  6 214 ? 71.860  43.761  267.356 1.00 273.12 ?  193 ILE I CD1 1 
ATOM   18979 N N   . CYS J  6 215 ? 69.527  38.871  264.690 1.00 277.16 ?  194 CYS I N   1 
ATOM   18980 C CA  . CYS J  6 215 ? 68.460  38.353  263.840 1.00 273.45 ?  194 CYS I CA  1 
ATOM   18981 C C   . CYS J  6 215 ? 67.151  39.077  264.155 1.00 269.61 ?  194 CYS I C   1 
ATOM   18982 O O   . CYS J  6 215 ? 66.811  39.276  265.323 1.00 271.36 ?  194 CYS I O   1 
ATOM   18983 C CB  . CYS J  6 215 ? 68.325  36.837  264.047 1.00 272.37 ?  194 CYS I CB  1 
ATOM   18984 S SG  . CYS J  6 215 ? 67.919  36.331  265.761 1.00 276.07 ?  194 CYS I SG  1 
ATOM   18985 N N   . ASN J  6 216 ? 66.406  39.467  263.113 1.00 272.93 ?  195 ASN I N   1 
ATOM   18986 C CA  . ASN J  6 216 ? 65.142  40.190  263.280 1.00 266.04 ?  195 ASN I CA  1 
ATOM   18987 C C   . ASN J  6 216 ? 63.963  39.251  263.041 1.00 260.89 ?  195 ASN I C   1 
ATOM   18988 O O   . ASN J  6 216 ? 63.749  38.791  261.917 1.00 254.64 ?  195 ASN I O   1 
ATOM   18989 C CB  . ASN J  6 216 ? 65.066  41.400  262.349 1.00 259.27 ?  195 ASN I CB  1 
ATOM   18990 C CG  . ASN J  6 216 ? 66.212  42.373  262.556 1.00 264.48 ?  195 ASN I CG  1 
ATOM   18991 O OD1 . ASN J  6 216 ? 67.155  42.091  263.296 1.00 272.21 ?  195 ASN I OD1 1 
ATOM   18992 N ND2 . ASN J  6 216 ? 66.116  43.543  261.934 1.00 259.80 ?  195 ASN I ND2 1 
ATOM   18993 N N   . VAL J  6 217 ? 63.189  38.995  264.096 1.00 267.14 ?  196 VAL I N   1 
ATOM   18994 C CA  . VAL J  6 217 ? 62.027  38.110  264.067 1.00 263.29 ?  196 VAL I CA  1 
ATOM   18995 C C   . VAL J  6 217 ? 60.755  38.949  264.067 1.00 255.29 ?  196 VAL I C   1 
ATOM   18996 O O   . VAL J  6 217 ? 60.589  39.817  264.929 1.00 256.59 ?  196 VAL I O   1 
ATOM   18997 C CB  . VAL J  6 217 ? 62.047  37.154  265.273 1.00 270.77 ?  196 VAL I CB  1 
ATOM   18998 C CG1 . VAL J  6 217 ? 60.855  36.236  265.258 1.00 267.61 ?  196 VAL I CG1 1 
ATOM   18999 C CG2 . VAL J  6 217 ? 63.341  36.362  265.301 1.00 278.64 ?  196 VAL I CG2 1 
ATOM   19000 N N   . ASN J  6 218 ? 59.856  38.698  263.108 1.00 276.52 ?  197 ASN I N   1 
ATOM   19001 C CA  . ASN J  6 218 ? 58.592  39.424  262.982 1.00 268.53 ?  197 ASN I CA  1 
ATOM   19002 C C   . ASN J  6 218 ? 57.430  38.434  262.941 1.00 263.98 ?  197 ASN I C   1 
ATOM   19003 O O   . ASN J  6 218 ? 57.483  37.431  262.225 1.00 261.60 ?  197 ASN I O   1 
ATOM   19004 C CB  . ASN J  6 218 ? 58.576  40.331  261.740 1.00 259.77 ?  197 ASN I CB  1 
ATOM   19005 C CG  . ASN J  6 218 ? 57.230  41.019  261.520 1.00 250.78 ?  197 ASN I CG  1 
ATOM   19006 O OD1 . ASN J  6 218 ? 56.363  41.025  262.396 1.00 252.47 ?  197 ASN I OD1 1 
ATOM   19007 N ND2 . ASN J  6 218 ? 57.053  41.599  260.338 1.00 241.08 ?  197 ASN I ND2 1 
ATOM   19008 N N   . HIS J  6 219 ? 56.369  38.735  263.692 1.00 264.60 ?  198 HIS I N   1 
ATOM   19009 C CA  . HIS J  6 219 ? 55.157  37.912  263.754 1.00 261.60 ?  198 HIS I CA  1 
ATOM   19010 C C   . HIS J  6 219 ? 53.918  38.782  263.566 1.00 254.02 ?  198 HIS I C   1 
ATOM   19011 O O   . HIS J  6 219 ? 53.454  39.423  264.513 1.00 260.78 ?  198 HIS I O   1 
ATOM   19012 C CB  . HIS J  6 219 ? 55.066  37.152  265.074 1.00 271.60 ?  198 HIS I CB  1 
ATOM   19013 C CG  . HIS J  6 219 ? 53.998  36.101  265.085 1.00 269.61 ?  198 HIS I CG  1 
ATOM   19014 N ND1 . HIS J  6 219 ? 53.367  35.691  266.240 1.00 275.81 ?  198 HIS I ND1 1 
ATOM   19015 C CD2 . HIS J  6 219 ? 53.442  35.386  264.080 1.00 262.02 ?  198 HIS I CD2 1 
ATOM   19016 C CE1 . HIS J  6 219 ? 52.469  34.768  265.945 1.00 272.75 ?  198 HIS I CE1 1 
ATOM   19017 N NE2 . HIS J  6 219 ? 52.494  34.565  264.640 1.00 264.23 ?  198 HIS I NE2 1 
ATOM   19018 N N   . LYS J  6 220 ? 53.396  38.817  262.342 1.00 265.64 ?  199 LYS I N   1 
ATOM   19019 C CA  . LYS J  6 220 ? 52.249  39.673  262.055 1.00 257.84 ?  199 LYS I CA  1 
ATOM   19020 C C   . LYS J  6 220 ? 51.022  39.335  262.904 1.00 259.42 ?  199 LYS I C   1 
ATOM   19021 O O   . LYS J  6 220 ? 50.357  40.273  263.373 1.00 258.88 ?  199 LYS I O   1 
ATOM   19022 C CB  . LYS J  6 220 ? 51.886  39.539  260.570 1.00 245.65 ?  199 LYS I CB  1 
ATOM   19023 C CG  . LYS J  6 220 ? 52.978  39.856  259.567 1.00 243.46 ?  199 LYS I CG  1 
ATOM   19024 C CD  . LYS J  6 220 ? 52.979  41.269  259.035 1.00 237.90 ?  199 LYS I CD  1 
ATOM   19025 C CE  . LYS J  6 220 ? 54.100  41.385  258.010 1.00 232.92 ?  199 LYS I CE  1 
ATOM   19026 N NZ  . LYS J  6 220 ? 53.752  40.661  256.746 1.00 220.86 1  199 LYS I NZ  1 
ATOM   19027 N N   . PRO J  6 221 ? 50.645  38.065  263.114 1.00 256.60 ?  200 PRO I N   1 
ATOM   19028 C CA  . PRO J  6 221 ? 49.447  37.781  263.930 1.00 258.87 ?  200 PRO I CA  1 
ATOM   19029 C C   . PRO J  6 221 ? 49.530  38.227  265.385 1.00 268.65 ?  200 PRO I C   1 
ATOM   19030 O O   . PRO J  6 221 ? 48.478  38.395  266.017 1.00 269.00 ?  200 PRO I O   1 
ATOM   19031 C CB  . PRO J  6 221 ? 49.291  36.262  263.806 1.00 260.42 ?  200 PRO I CB  1 
ATOM   19032 C CG  . PRO J  6 221 ? 49.923  35.942  262.509 1.00 252.98 ?  200 PRO I CG  1 
ATOM   19033 C CD  . PRO J  6 221 ? 51.094  36.857  262.401 1.00 254.60 ?  200 PRO I CD  1 
ATOM   19034 N N   . SER J  6 222 ? 50.727  38.439  265.936 1.00 253.87 ?  201 SER I N   1 
ATOM   19035 C CA  . SER J  6 222 ? 50.868  38.905  267.308 1.00 256.80 ?  201 SER I CA  1 
ATOM   19036 C C   . SER J  6 222 ? 51.506  40.276  267.303 1.00 256.05 ?  201 SER I C   1 
ATOM   19037 O O   . SER J  6 222 ? 51.751  40.849  268.373 1.00 258.24 ?  201 SER I O   1 
ATOM   19038 C CB  . SER J  6 222 ? 51.758  37.956  268.129 1.00 259.55 ?  201 SER I CB  1 
ATOM   19039 O OG  . SER J  6 222 ? 51.207  36.664  268.271 1.00 260.62 ?  201 SER I OG  1 
ATOM   19040 N N   . ASN J  6 223 ? 51.761  40.804  266.105 1.00 279.31 ?  202 ASN I N   1 
ATOM   19041 C CA  . ASN J  6 223 ? 52.382  42.099  265.863 1.00 274.49 ?  202 ASN I CA  1 
ATOM   19042 C C   . ASN J  6 223 ? 53.688  42.219  266.643 1.00 283.29 ?  202 ASN I C   1 
ATOM   19043 O O   . ASN J  6 223 ? 54.102  43.312  267.022 1.00 284.91 ?  202 ASN I O   1 
ATOM   19044 C CB  . ASN J  6 223 ? 51.373  43.184  266.238 1.00 272.22 ?  202 ASN I CB  1 
ATOM   19045 C CG  . ASN J  6 223 ? 50.070  43.061  265.438 1.00 263.45 ?  202 ASN I CG  1 
ATOM   19046 O OD1 . ASN J  6 223 ? 50.076  42.644  264.281 1.00 260.39 ?  202 ASN I OD1 1 
ATOM   19047 N ND2 . ASN J  6 223 ? 48.949  43.220  266.123 1.00 259.83 ?  202 ASN I ND2 1 
ATOM   19048 N N   . THR J  6 224 ? 54.414  41.101  266.719 1.00 262.80 ?  203 THR I N   1 
ATOM   19049 C CA  . THR J  6 224 ? 55.640  40.954  267.501 1.00 271.52 ?  203 THR I CA  1 
ATOM   19050 C C   . THR J  6 224 ? 56.863  40.966  266.590 1.00 271.98 ?  203 THR I C   1 
ATOM   19051 O O   . THR J  6 224 ? 56.983  40.111  265.705 1.00 269.99 ?  203 THR I O   1 
ATOM   19052 C CB  . THR J  6 224 ? 55.602  39.682  268.350 1.00 278.71 ?  203 THR I CB  1 
ATOM   19053 O OG1 . THR J  6 224 ? 54.404  39.673  269.137 1.00 278.94 ?  203 THR I OG1 1 
ATOM   19054 C CG2 . THR J  6 224 ? 56.795  39.650  269.291 1.00 287.57 ?  203 THR I CG2 1 
ATOM   19055 N N   . LYS J  6 225 ? 57.762  41.923  266.809 1.00 265.89 ?  204 LYS I N   1 
ATOM   19056 C CA  . LYS J  6 225 ? 59.020  42.035  266.073 1.00 266.76 ?  204 LYS I CA  1 
ATOM   19057 C C   . LYS J  6 225 ? 60.178  41.967  267.068 1.00 276.34 ?  204 LYS I C   1 
ATOM   19058 O O   . LYS J  6 225 ? 60.430  42.944  267.782 1.00 279.05 ?  204 LYS I O   1 
ATOM   19059 C CB  . LYS J  6 225 ? 59.014  43.336  265.276 1.00 260.41 ?  204 LYS I CB  1 
ATOM   19060 C CG  . LYS J  6 225 ? 60.155  43.572  264.320 1.00 260.27 ?  204 LYS I CG  1 
ATOM   19061 C CD  . LYS J  6 225 ? 59.637  44.392  263.143 1.00 250.85 ?  204 LYS I CD  1 
ATOM   19062 C CE  . LYS J  6 225 ? 58.871  45.622  263.628 1.00 248.23 ?  204 LYS I CE  1 
ATOM   19063 N NZ  . LYS J  6 225 ? 58.294  46.416  262.506 1.00 239.00 1  204 LYS I NZ  1 
ATOM   19064 N N   . VAL J  6 226 ? 60.908  40.835  267.075 1.00 262.06 ?  205 VAL I N   1 
ATOM   19065 C CA  . VAL J  6 226 ? 62.003  40.577  268.023 1.00 264.83 ?  205 VAL I CA  1 
ATOM   19066 C C   . VAL J  6 226 ? 63.356  40.456  267.325 1.00 263.89 ?  205 VAL I C   1 
ATOM   19067 O O   . VAL J  6 226 ? 63.555  39.588  266.463 1.00 263.94 ?  205 VAL I O   1 
ATOM   19068 C CB  . VAL J  6 226 ? 61.744  39.302  268.852 1.00 267.51 ?  205 VAL I CB  1 
ATOM   19069 C CG1 . VAL J  6 226 ? 62.938  38.999  269.794 1.00 271.87 ?  205 VAL I CG1 1 
ATOM   19070 C CG2 . VAL J  6 226 ? 60.387  39.352  269.603 1.00 268.68 ?  205 VAL I CG2 1 
ATOM   19071 N N   . ASP J  6 227 ? 64.292  41.321  267.732 1.00 267.46 ?  206 ASP I N   1 
ATOM   19072 C CA  . ASP J  6 227 ? 65.670  41.338  267.255 1.00 271.14 ?  206 ASP I CA  1 
ATOM   19073 C C   . ASP J  6 227 ? 66.557  40.691  268.327 1.00 278.16 ?  206 ASP I C   1 
ATOM   19074 O O   . ASP J  6 227 ? 66.746  41.279  269.392 1.00 280.38 ?  206 ASP I O   1 
ATOM   19075 C CB  . ASP J  6 227 ? 66.109  42.774  266.968 1.00 269.72 ?  206 ASP I CB  1 
ATOM   19076 C CG  . ASP J  6 227 ? 65.227  43.445  265.924 1.00 261.40 ?  206 ASP I CG  1 
ATOM   19077 O OD1 . ASP J  6 227 ? 64.683  42.711  265.086 1.00 256.13 ?  206 ASP I OD1 1 
ATOM   19078 O OD2 . ASP J  6 227 ? 65.157  44.699  265.866 1.00 259.76 -1 206 ASP I OD2 1 
ATOM   19079 N N   . LYS J  6 228 ? 67.155  39.525  268.039 1.00 275.15 ?  207 LYS I N   1 
ATOM   19080 C CA  . LYS J  6 228 ? 67.997  38.799  269.002 1.00 280.22 ?  207 LYS I CA  1 
ATOM   19081 C C   . LYS J  6 228 ? 69.465  38.735  268.575 1.00 281.49 ?  207 LYS I C   1 
ATOM   19082 O O   . LYS J  6 228 ? 69.766  38.399  267.425 1.00 279.31 ?  207 LYS I O   1 
ATOM   19083 C CB  . LYS J  6 228 ? 67.468  37.366  269.156 1.00 280.60 ?  207 LYS I CB  1 
ATOM   19084 C CG  . LYS J  6 228 ? 68.172  36.450  270.169 1.00 283.85 ?  207 LYS I CG  1 
ATOM   19085 C CD  . LYS J  6 228 ? 68.128  36.905  271.590 1.00 287.25 ?  207 LYS I CD  1 
ATOM   19086 C CE  . LYS J  6 228 ? 66.711  36.910  272.064 1.00 286.81 ?  207 LYS I CE  1 
ATOM   19087 N NZ  . LYS J  6 228 ? 66.471  35.852  273.068 1.00 289.57 1  207 LYS I NZ  1 
ATOM   19088 N N   . ARG J  6 229 ? 70.377  39.046  269.506 1.00 269.02 ?  208 ARG I N   1 
ATOM   19089 C CA  . ARG J  6 229 ? 71.820  38.994  269.260 1.00 269.30 ?  208 ARG I CA  1 
ATOM   19090 C C   . ARG J  6 229 ? 72.445  37.747  269.888 1.00 272.02 ?  208 ARG I C   1 
ATOM   19091 O O   . ARG J  6 229 ? 72.243  37.473  271.078 1.00 274.82 ?  208 ARG I O   1 
ATOM   19092 C CB  . ARG J  6 229 ? 72.556  40.264  269.692 1.00 269.76 ?  208 ARG I CB  1 
ATOM   19093 C CG  . ARG J  6 229 ? 74.052  40.162  269.387 1.00 270.03 ?  208 ARG I CG  1 
ATOM   19094 C CD  . ARG J  6 229 ? 74.832  41.436  269.666 1.00 270.82 ?  208 ARG I CD  1 
ATOM   19095 N NE  . ARG J  6 229 ? 74.828  41.921  271.036 1.00 276.93 ?  208 ARG I NE  1 
ATOM   19096 C CZ  . ARG J  6 229 ? 75.872  42.527  271.589 1.00 284.35 ?  208 ARG I CZ  1 
ATOM   19097 N NH1 . ARG J  6 229 ? 76.975  42.716  270.879 1.00 287.39 1  208 ARG I NH1 1 
ATOM   19098 N NH2 . ARG J  6 229 ? 75.809  42.958  272.841 1.00 288.49 ?  208 ARG I NH2 1 
ATOM   19099 N N   . VAL J  6 230 ? 73.200  37.005  269.085 1.00 286.34 ?  209 VAL I N   1 
ATOM   19100 C CA  . VAL J  6 230 ? 73.860  35.758  269.471 1.00 286.00 ?  209 VAL I CA  1 
ATOM   19101 C C   . VAL J  6 230 ? 75.317  36.005  269.854 1.00 287.94 ?  209 VAL I C   1 
ATOM   19102 O O   . VAL J  6 230 ? 76.091  36.558  269.062 1.00 285.28 ?  209 VAL I O   1 
ATOM   19103 C CB  . VAL J  6 230 ? 73.777  34.711  268.352 1.00 273.54 ?  209 VAL I CB  1 
ATOM   19104 C CG1 . VAL J  6 230 ? 74.533  33.475  268.767 1.00 271.91 ?  209 VAL I CG1 1 
ATOM   19105 C CG2 . VAL J  6 230 ? 72.334  34.363  268.072 1.00 268.97 ?  209 VAL I CG2 1 
ATOM   19106 N N   . GLU J  6 231 ? 75.697  35.605  271.074 1.00 280.85 ?  210 GLU I N   1 
ATOM   19107 C CA  . GLU J  6 231 ? 77.063  35.780  271.547 1.00 278.76 ?  210 GLU I CA  1 
ATOM   19108 C C   . GLU J  6 231 ? 77.564  34.449  272.095 1.00 277.70 ?  210 GLU I C   1 
ATOM   19109 O O   . GLU J  6 231 ? 76.831  33.759  272.816 1.00 280.67 ?  210 GLU I O   1 
ATOM   19110 C CB  . GLU J  6 231 ? 77.106  36.827  272.674 1.00 279.64 ?  210 GLU I CB  1 
ATOM   19111 C CG  . GLU J  6 231 ? 76.645  38.221  272.288 1.00 282.21 ?  210 GLU I CG  1 
ATOM   19112 C CD  . GLU J  6 231 ? 76.574  39.156  273.483 1.00 293.40 ?  210 GLU I CD  1 
ATOM   19113 O OE1 . GLU J  6 231 ? 76.736  38.677  274.626 1.00 295.26 ?  210 GLU I OE1 1 
ATOM   19114 O OE2 . GLU J  6 231 ? 76.325  40.363  273.285 1.00 300.69 -1 210 GLU I OE2 1 
ATOM   19115 N N   . PRO J  6 232 ? 78.816  34.059  271.779 1.00 284.52 ?  211 PRO I N   1 
ATOM   19116 C CA  . PRO J  6 232 ? 79.409  32.801  272.261 1.00 281.59 ?  211 PRO I CA  1 
ATOM   19117 C C   . PRO J  6 232 ? 79.502  32.706  273.783 1.00 283.72 ?  211 PRO I C   1 
ATOM   19118 O O   . PRO J  6 232 ? 80.376  33.346  274.367 1.00 284.01 ?  211 PRO I O   1 
ATOM   19119 C CB  . PRO J  6 232 ? 80.804  32.798  271.622 1.00 274.35 ?  211 PRO I CB  1 
ATOM   19120 C CG  . PRO J  6 232 ? 80.674  33.678  270.426 1.00 268.82 ?  211 PRO I CG  1 
ATOM   19121 C CD  . PRO J  6 232 ? 79.706  34.752  270.831 1.00 278.90 ?  211 PRO I CD  1 
ATOM   19122 N N   . ALA K  3 1   ? 44.660  11.980  243.973 1.00 302.11 ?  6   ALA J N   1 
ATOM   19123 C CA  . ALA K  3 1   ? 44.592  13.354  243.474 1.00 299.78 ?  6   ALA J CA  1 
ATOM   19124 C C   . ALA K  3 1   ? 45.920  13.870  242.855 1.00 299.50 ?  6   ALA J C   1 
ATOM   19125 O O   . ALA K  3 1   ? 45.897  14.423  241.754 1.00 293.91 ?  6   ALA J O   1 
ATOM   19126 C CB  . ALA K  3 1   ? 44.113  14.292  244.592 1.00 293.21 ?  6   ALA J CB  1 
ATOM   19127 N N   . PRO K  3 2   ? 47.059  13.701  243.535 1.00 309.43 ?  7   PRO J N   1 
ATOM   19128 C CA  . PRO K  3 2   ? 48.327  14.181  242.970 1.00 297.22 ?  7   PRO J CA  1 
ATOM   19129 C C   . PRO K  3 2   ? 48.880  13.234  241.915 1.00 285.37 ?  7   PRO J C   1 
ATOM   19130 O O   . PRO K  3 2   ? 48.669  12.020  241.965 1.00 290.33 ?  7   PRO J O   1 
ATOM   19131 C CB  . PRO K  3 2   ? 49.255  14.240  244.189 1.00 295.76 ?  7   PRO J CB  1 
ATOM   19132 C CG  . PRO K  3 2   ? 48.754  13.157  245.067 1.00 299.76 ?  7   PRO J CG  1 
ATOM   19133 C CD  . PRO K  3 2   ? 47.262  13.141  244.889 1.00 305.59 ?  7   PRO J CD  1 
ATOM   19134 N N   . THR K  3 3   ? 49.585  13.808  240.936 1.00 271.81 ?  8   THR J N   1 
ATOM   19135 C CA  . THR K  3 3   ? 50.200  13.025  239.873 1.00 272.84 ?  8   THR J CA  1 
ATOM   19136 C C   . THR K  3 3   ? 51.680  13.384  239.766 1.00 270.63 ?  8   THR J C   1 
ATOM   19137 O O   . THR K  3 3   ? 52.102  14.480  240.148 1.00 268.07 ?  8   THR J O   1 
ATOM   19138 C CB  . THR K  3 3   ? 49.487  13.278  238.528 1.00 273.27 ?  8   THR J CB  1 
ATOM   19139 O OG1 . THR K  3 3   ? 49.485  14.682  238.242 1.00 272.97 ?  8   THR J OG1 1 
ATOM   19140 C CG2 . THR K  3 3   ? 48.044  12.800  238.583 1.00 275.70 ?  8   THR J CG2 1 
ATOM   19141 N N   . PHE K  3 4   ? 52.471  12.447  239.231 1.00 263.08 ?  9   PHE J N   1 
ATOM   19142 C CA  . PHE K  3 4   ? 53.913  12.628  239.105 1.00 261.36 ?  9   PHE J CA  1 
ATOM   19143 C C   . PHE K  3 4   ? 54.428  12.179  237.743 1.00 262.68 ?  9   PHE J C   1 
ATOM   19144 O O   . PHE K  3 4   ? 53.937  11.196  237.180 1.00 265.64 ?  9   PHE J O   1 
ATOM   19145 C CB  . PHE K  3 4   ? 54.652  11.844  240.199 1.00 261.42 ?  9   PHE J CB  1 
ATOM   19146 C CG  . PHE K  3 4   ? 54.472  12.403  241.584 1.00 259.97 ?  9   PHE J CG  1 
ATOM   19147 C CD1 . PHE K  3 4   ? 53.410  12.011  242.384 1.00 261.74 ?  9   PHE J CD1 1 
ATOM   19148 C CD2 . PHE K  3 4   ? 55.382  13.310  242.090 1.00 257.30 ?  9   PHE J CD2 1 
ATOM   19149 C CE1 . PHE K  3 4   ? 53.262  12.527  243.660 1.00 260.94 ?  9   PHE J CE1 1 
ATOM   19150 C CE2 . PHE K  3 4   ? 55.241  13.828  243.358 1.00 256.46 ?  9   PHE J CE2 1 
ATOM   19151 C CZ  . PHE K  3 4   ? 54.181  13.437  244.145 1.00 258.33 ?  9   PHE J CZ  1 
ATOM   19152 N N   . VAL K  3 5   ? 55.415  12.910  237.218 1.00 250.95 ?  11  VAL J N   1 
ATOM   19153 C CA  . VAL K  3 5   ? 56.090  12.595  235.956 1.00 257.05 ?  11  VAL J CA  1 
ATOM   19154 C C   . VAL K  3 5   ? 57.597  12.785  236.141 1.00 259.32 ?  11  VAL J C   1 
ATOM   19155 O O   . VAL K  3 5   ? 58.053  13.914  236.358 1.00 252.35 ?  11  VAL J O   1 
ATOM   19156 C CB  . VAL K  3 5   ? 55.585  13.437  234.776 1.00 251.97 ?  11  VAL J CB  1 
ATOM   19157 C CG1 . VAL K  3 5   ? 56.461  13.197  233.561 1.00 256.99 ?  11  VAL J CG1 1 
ATOM   19158 C CG2 . VAL K  3 5   ? 54.151  13.070  234.444 1.00 241.95 ?  11  VAL J CG2 1 
ATOM   19159 N N   . SER K  3 6   ? 58.369  11.700  236.065 1.00 253.59 ?  12  SER J N   1 
ATOM   19160 C CA  . SER K  3 6   ? 59.821  11.771  236.222 1.00 253.25 ?  12  SER J CA  1 
ATOM   19161 C C   . SER K  3 6   ? 60.452  11.691  234.833 1.00 256.84 ?  12  SER J C   1 
ATOM   19162 O O   . SER K  3 6   ? 60.204  10.735  234.091 1.00 264.04 ?  12  SER J O   1 
ATOM   19163 C CB  . SER K  3 6   ? 60.344  10.653  237.126 1.00 260.59 ?  12  SER J CB  1 
ATOM   19164 O OG  . SER K  3 6   ? 60.040  9.373   236.601 1.00 269.13 ?  12  SER J OG  1 
ATOM   19165 N N   . VAL K  3 7   ? 61.272  12.690  234.491 1.00 267.25 ?  13  VAL J N   1 
ATOM   19166 C CA  . VAL K  3 7   ? 61.928  12.791  233.188 1.00 269.36 ?  13  VAL J CA  1 
ATOM   19167 C C   . VAL K  3 7   ? 63.411  13.090  233.376 1.00 270.60 ?  13  VAL J C   1 
ATOM   19168 O O   . VAL K  3 7   ? 63.777  13.981  234.151 1.00 263.68 ?  13  VAL J O   1 
ATOM   19169 C CB  . VAL K  3 7   ? 61.273  13.875  232.308 1.00 257.86 ?  13  VAL J CB  1 
ATOM   19170 C CG1 . VAL K  3 7   ? 62.029  14.035  230.996 1.00 258.70 ?  13  VAL J CG1 1 
ATOM   19171 C CG2 . VAL K  3 7   ? 59.816  13.537  232.048 1.00 255.70 ?  13  VAL J CG2 1 
ATOM   19172 N N   . ALA K  3 8   ? 64.260  12.341  232.670 1.00 271.62 ?  14  ALA J N   1 
ATOM   19173 C CA  . ALA K  3 8   ? 65.700  12.550  232.733 1.00 271.00 ?  14  ALA J CA  1 
ATOM   19174 C C   . ALA K  3 8   ? 66.082  13.941  232.222 1.00 262.79 ?  14  ALA J C   1 
ATOM   19175 O O   . ALA K  3 8   ? 65.438  14.482  231.317 1.00 258.73 ?  14  ALA J O   1 
ATOM   19176 C CB  . ALA K  3 8   ? 66.428  11.482  231.918 1.00 278.01 ?  14  ALA J CB  1 
ATOM   19177 N N   . PRO K  3 9   ? 67.120  14.546  232.804 1.00 270.48 ?  15  PRO J N   1 
ATOM   19178 C CA  . PRO K  3 9   ? 67.549  15.886  232.378 1.00 262.90 ?  15  PRO J CA  1 
ATOM   19179 C C   . PRO K  3 9   ? 67.911  15.928  230.902 1.00 263.58 ?  15  PRO J C   1 
ATOM   19180 O O   . PRO K  3 9   ? 68.623  15.059  230.392 1.00 269.68 ?  15  PRO J O   1 
ATOM   19181 C CB  . PRO K  3 9   ? 68.772  16.160  233.259 1.00 257.71 ?  15  PRO J CB  1 
ATOM   19182 C CG  . PRO K  3 9   ? 68.563  15.321  234.452 1.00 258.23 ?  15  PRO J CG  1 
ATOM   19183 C CD  . PRO K  3 9   ? 67.894  14.069  233.960 1.00 268.23 ?  15  PRO J CD  1 
ATOM   19184 N N   . GLY K  3 10  ? 67.419  16.954  230.217 1.00 262.55 ?  16  GLY J N   1 
ATOM   19185 C CA  . GLY K  3 10  ? 67.712  17.119  228.817 1.00 259.56 ?  16  GLY J CA  1 
ATOM   19186 C C   . GLY K  3 10  ? 66.716  16.453  227.903 1.00 265.62 ?  16  GLY J C   1 
ATOM   19187 O O   . GLY K  3 10  ? 66.757  16.688  226.689 1.00 267.63 ?  16  GLY J O   1 
ATOM   19188 N N   . GLN K  3 11  ? 65.821  15.630  228.450 1.00 260.81 ?  17  GLN J N   1 
ATOM   19189 C CA  . GLN K  3 11  ? 64.836  14.916  227.655 1.00 265.28 ?  17  GLN J CA  1 
ATOM   19190 C C   . GLN K  3 11  ? 63.600  15.790  227.485 1.00 258.14 ?  17  GLN J C   1 
ATOM   19191 O O   . GLN K  3 11  ? 63.711  17.021  227.499 1.00 250.65 ?  17  GLN J O   1 
ATOM   19192 C CB  . GLN K  3 11  ? 64.488  13.593  228.337 1.00 271.92 ?  17  GLN J CB  1 
ATOM   19193 C CG  . GLN K  3 11  ? 64.425  12.407  227.409 1.00 281.35 ?  17  GLN J CG  1 
ATOM   19194 C CD  . GLN K  3 11  ? 65.774  12.112  226.777 1.00 286.43 ?  17  GLN J CD  1 
ATOM   19195 O OE1 . GLN K  3 11  ? 66.823  12.315  227.393 1.00 290.41 ?  17  GLN J OE1 1 
ATOM   19196 N NE2 . GLN K  3 11  ? 65.753  11.630  225.542 1.00 286.35 ?  17  GLN J NE2 1 
ATOM   19197 N N   . THR K  3 12  ? 62.427  15.185  227.296 1.00 266.01 ?  18  THR J N   1 
ATOM   19198 C CA  . THR K  3 12  ? 61.200  15.945  227.090 1.00 259.35 ?  18  THR J CA  1 
ATOM   19199 C C   . THR K  3 12  ? 60.122  15.530  228.083 1.00 257.53 ?  18  THR J C   1 
ATOM   19200 O O   . THR K  3 12  ? 59.828  14.337  228.212 1.00 264.28 ?  18  THR J O   1 
ATOM   19201 C CB  . THR K  3 12  ? 60.694  15.733  225.659 1.00 262.87 ?  18  THR J CB  1 
ATOM   19202 O OG1 . THR K  3 12  ? 61.710  16.127  224.730 1.00 265.65 ?  18  THR J OG1 1 
ATOM   19203 C CG2 . THR K  3 12  ? 59.449  16.547  225.405 1.00 254.91 ?  18  THR J CG2 1 
ATOM   19204 N N   . ALA K  3 13  ? 59.534  16.504  228.784 1.00 268.77 ?  19  ALA J N   1 
ATOM   19205 C CA  . ALA K  3 13  ? 58.472  16.228  229.741 1.00 269.19 ?  19  ALA J CA  1 
ATOM   19206 C C   . ALA K  3 13  ? 57.126  16.658  229.166 1.00 261.63 ?  19  ALA J C   1 
ATOM   19207 O O   . ALA K  3 13  ? 57.034  17.685  228.489 1.00 255.48 ?  19  ALA J O   1 
ATOM   19208 C CB  . ALA K  3 13  ? 58.731  16.954  231.065 1.00 262.72 ?  19  ALA J CB  1 
ATOM   19209 N N   . ARG K  3 14  ? 56.088  15.867  229.444 1.00 253.83 ?  20  ARG J N   1 
ATOM   19210 C CA  . ARG K  3 14  ? 54.713  16.122  229.011 1.00 248.64 ?  20  ARG J CA  1 
ATOM   19211 C C   . ARG K  3 14  ? 53.783  15.933  230.210 1.00 245.44 ?  20  ARG J C   1 
ATOM   19212 O O   . ARG K  3 14  ? 53.899  14.942  230.937 1.00 251.10 ?  20  ARG J O   1 
ATOM   19213 C CB  . ARG K  3 14  ? 54.408  15.323  227.735 1.00 254.37 ?  20  ARG J CB  1 
ATOM   19214 C CG  . ARG K  3 14  ? 54.765  13.865  227.693 1.00 264.77 ?  20  ARG J CG  1 
ATOM   19215 C CD  . ARG K  3 14  ? 54.444  13.384  226.282 1.00 270.22 ?  20  ARG J CD  1 
ATOM   19216 N NE  . ARG K  3 14  ? 55.605  13.652  225.421 1.00 274.06 ?  20  ARG J NE  1 
ATOM   19217 C CZ  . ARG K  3 14  ? 55.604  14.421  224.332 1.00 272.14 ?  20  ARG J CZ  1 
ATOM   19218 N NH1 . ARG K  3 14  ? 54.495  15.029  223.932 1.00 266.54 1  20  ARG J NH1 1 
ATOM   19219 N NH2 . ARG K  3 14  ? 56.727  14.590  223.639 1.00 275.88 ?  20  ARG J NH2 1 
ATOM   19220 N N   . ILE K  3 15  ? 52.865  16.885  230.407 1.00 254.44 ?  21  ILE J N   1 
ATOM   19221 C CA  . ILE K  3 15  ? 51.987  16.977  231.577 1.00 249.85 ?  21  ILE J CA  1 
ATOM   19222 C C   . ILE K  3 15  ? 50.508  17.031  231.203 1.00 245.72 ?  21  ILE J C   1 
ATOM   19223 O O   . ILE K  3 15  ? 50.107  17.839  230.360 1.00 240.89 ?  21  ILE J O   1 
ATOM   19224 C CB  . ILE K  3 15  ? 52.344  18.216  232.420 1.00 242.04 ?  21  ILE J CB  1 
ATOM   19225 C CG1 . ILE K  3 15  ? 53.754  18.098  233.007 1.00 245.69 ?  21  ILE J CG1 1 
ATOM   19226 C CG2 . ILE K  3 15  ? 51.279  18.486  233.468 1.00 236.33 ?  21  ILE J CG2 1 
ATOM   19227 C CD1 . ILE K  3 15  ? 54.219  19.349  233.724 1.00 238.51 ?  21  ILE J CD1 1 
ATOM   19228 N N   . THR K  3 16  ? 49.697  16.192  231.856 1.00 226.24 ?  22  THR J N   1 
ATOM   19229 C CA  . THR K  3 16  ? 48.256  16.127  231.633 1.00 222.13 ?  22  THR J CA  1 
ATOM   19230 C C   . THR K  3 16  ? 47.566  16.727  232.856 1.00 214.90 ?  22  THR J C   1 
ATOM   19231 O O   . THR K  3 16  ? 47.852  16.343  233.993 1.00 216.61 ?  22  THR J O   1 
ATOM   19232 C CB  . THR K  3 16  ? 47.787  14.680  231.419 1.00 229.31 ?  22  THR J CB  1 
ATOM   19233 O OG1 . THR K  3 16  ? 48.168  13.870  232.541 1.00 234.43 ?  22  THR J OG1 1 
ATOM   19234 C CG2 . THR K  3 16  ? 48.385  14.080  230.145 1.00 236.22 ?  22  THR J CG2 1 
ATOM   19235 N N   . CYS K  3 17  ? 46.645  17.654  232.604 1.00 245.98 ?  23  CYS J N   1 
ATOM   19236 C CA  . CYS K  3 17  ? 45.873  18.372  233.610 1.00 238.77 ?  23  CYS J CA  1 
ATOM   19237 C C   . CYS K  3 17  ? 44.480  18.646  233.070 1.00 233.54 ?  23  CYS J C   1 
ATOM   19238 O O   . CYS K  3 17  ? 44.281  18.738  231.854 1.00 233.50 ?  23  CYS J O   1 
ATOM   19239 C CB  . CYS K  3 17  ? 46.477  19.738  233.969 1.00 233.48 ?  23  CYS J CB  1 
ATOM   19240 S SG  . CYS K  3 17  ? 45.461  20.756  235.102 1.00 223.45 ?  23  CYS J SG  1 
ATOM   19241 N N   . GLY K  3 18  ? 43.511  18.757  233.974 1.00 223.11 ?  24  GLY J N   1 
ATOM   19242 C CA  . GLY K  3 18  ? 42.162  19.061  233.565 1.00 218.03 ?  24  GLY J CA  1 
ATOM   19243 C C   . GLY K  3 18  ? 41.392  17.914  232.951 1.00 222.34 ?  24  GLY J C   1 
ATOM   19244 O O   . GLY K  3 18  ? 41.906  16.833  232.664 1.00 229.83 ?  24  GLY J O   1 
ATOM   19245 N N   . GLU K  3 19  ? 40.100  18.181  232.761 1.00 222.23 ?  25  GLU J N   1 
ATOM   19246 C CA  . GLU K  3 19  ? 39.157  17.225  232.191 1.00 225.28 ?  25  GLU J CA  1 
ATOM   19247 C C   . GLU K  3 19  ? 39.422  17.062  230.690 1.00 228.51 ?  25  GLU J C   1 
ATOM   19248 O O   . GLU K  3 19  ? 40.347  17.655  230.125 1.00 227.37 ?  25  GLU J O   1 
ATOM   19249 C CB  . GLU K  3 19  ? 37.752  17.785  232.493 1.00 218.45 ?  25  GLU J CB  1 
ATOM   19250 C CG  . GLU K  3 19  ? 36.633  17.678  231.464 1.00 219.70 ?  25  GLU J CG  1 
ATOM   19251 C CD  . GLU K  3 19  ? 35.340  18.242  231.969 1.00 218.41 ?  25  GLU J CD  1 
ATOM   19252 O OE1 . GLU K  3 19  ? 35.166  18.346  233.206 1.00 222.19 ?  25  GLU J OE1 1 
ATOM   19253 O OE2 . GLU K  3 19  ? 34.530  18.643  231.117 1.00 218.69 -1 25  GLU J OE2 1 
ATOM   19254 N N   . GLU K  3 20  ? 38.617  16.223  230.047 1.00 232.86 ?  26  GLU J N   1 
ATOM   19255 C CA  . GLU K  3 20  ? 38.727  16.024  228.611 1.00 235.51 ?  26  GLU J CA  1 
ATOM   19256 C C   . GLU K  3 20  ? 38.117  17.200  227.857 1.00 228.34 ?  26  GLU J C   1 
ATOM   19257 O O   . GLU K  3 20  ? 37.118  17.788  228.285 1.00 223.66 ?  26  GLU J O   1 
ATOM   19258 C CB  . GLU K  3 20  ? 38.042  14.730  228.172 1.00 240.90 ?  26  GLU J CB  1 
ATOM   19259 C CG  . GLU K  3 20  ? 38.627  13.446  228.737 1.00 249.53 ?  26  GLU J CG  1 
ATOM   19260 C CD  . GLU K  3 20  ? 38.581  12.314  227.718 1.00 256.97 ?  26  GLU J CD  1 
ATOM   19261 O OE1 . GLU K  3 20  ? 38.072  12.539  226.597 1.00 254.66 ?  26  GLU J OE1 1 
ATOM   19262 O OE2 . GLU K  3 20  ? 39.061  11.204  228.031 1.00 265.30 -1 26  GLU J OE2 1 
ATOM   19263 N N   . SER K  3 21  ? 38.716  17.539  226.716 1.00 220.56 ?  27  SER J N   1 
ATOM   19264 C CA  . SER K  3 21  ? 38.198  18.658  225.938 1.00 217.59 ?  27  SER J CA  1 
ATOM   19265 C C   . SER K  3 21  ? 36.817  18.350  225.368 1.00 219.44 ?  27  SER J C   1 
ATOM   19266 O O   . SER K  3 21  ? 36.586  17.266  224.819 1.00 223.63 ?  27  SER J O   1 
ATOM   19267 C CB  . SER K  3 21  ? 39.152  19.000  224.796 1.00 219.15 ?  27  SER J CB  1 
ATOM   19268 O OG  . SER K  3 21  ? 38.518  19.819  223.828 1.00 218.94 ?  27  SER J OG  1 
ATOM   19269 N N   . LEU K  3 22  ? 35.896  19.305  225.508 1.00 226.84 ?  28  LEU J N   1 
ATOM   19270 C CA  . LEU K  3 22  ? 34.549  19.190  224.962 1.00 228.22 ?  28  LEU J CA  1 
ATOM   19271 C C   . LEU K  3 22  ? 34.284  20.152  223.815 1.00 227.77 ?  28  LEU J C   1 
ATOM   19272 O O   . LEU K  3 22  ? 33.494  19.841  222.922 1.00 230.54 ?  28  LEU J O   1 
ATOM   19273 C CB  . LEU K  3 22  ? 33.502  19.451  226.053 1.00 225.95 ?  28  LEU J CB  1 
ATOM   19274 C CG  . LEU K  3 22  ? 32.050  19.111  225.695 1.00 227.92 ?  28  LEU J CG  1 
ATOM   19275 C CD1 . LEU K  3 22  ? 31.914  17.676  225.183 1.00 233.10 ?  28  LEU J CD1 1 
ATOM   19276 C CD2 . LEU K  3 22  ? 31.101  19.394  226.856 1.00 225.98 ?  28  LEU J CD2 1 
ATOM   19277 N N   . GLY K  3 23  ? 34.951  21.302  223.826 1.00 219.21 ?  29  GLY J N   1 
ATOM   19278 C CA  . GLY K  3 23  ? 34.854  22.332  222.812 1.00 218.69 ?  29  GLY J CA  1 
ATOM   19279 C C   . GLY K  3 23  ? 36.161  23.061  222.594 1.00 217.60 ?  29  GLY J C   1 
ATOM   19280 O O   . GLY K  3 23  ? 37.233  22.579  222.972 1.00 218.01 ?  29  GLY J O   1 
ATOM   19281 N N   . SER K  3 24  ? 36.071  24.232  221.975 1.00 214.66 ?  30  SER J N   1 
ATOM   19282 C CA  . SER K  3 24  ? 37.240  25.071  221.760 1.00 213.81 ?  30  SER J CA  1 
ATOM   19283 C C   . SER K  3 24  ? 37.728  25.574  223.114 1.00 210.30 ?  30  SER J C   1 
ATOM   19284 O O   . SER K  3 24  ? 36.958  26.148  223.890 1.00 207.55 ?  30  SER J O   1 
ATOM   19285 C CB  . SER K  3 24  ? 36.884  26.241  220.847 1.00 213.44 ?  30  SER J CB  1 
ATOM   19286 O OG  . SER K  3 24  ? 35.803  26.973  221.396 1.00 210.55 ?  30  SER J OG  1 
ATOM   19287 N N   . ARG K  3 25  ? 39.001  25.338  223.408 1.00 213.53 ?  31  ARG J N   1 
ATOM   19288 C CA  . ARG K  3 25  ? 39.565  25.655  224.709 1.00 209.51 ?  31  ARG J CA  1 
ATOM   19289 C C   . ARG K  3 25  ? 40.493  26.857  224.631 1.00 208.21 ?  31  ARG J C   1 
ATOM   19290 O O   . ARG K  3 25  ? 40.904  27.293  223.553 1.00 209.97 ?  31  ARG J O   1 
ATOM   19291 C CB  . ARG K  3 25  ? 40.403  24.462  225.187 1.00 211.14 ?  31  ARG J CB  1 
ATOM   19292 C CG  . ARG K  3 25  ? 39.687  23.241  225.712 1.00 212.18 ?  31  ARG J CG  1 
ATOM   19293 C CD  . ARG K  3 25  ? 39.703  23.168  227.212 1.00 209.73 ?  31  ARG J CD  1 
ATOM   19294 N NE  . ARG K  3 25  ? 38.818  22.120  227.709 1.00 210.92 ?  31  ARG J NE  1 
ATOM   19295 C CZ  . ARG K  3 25  ? 39.246  21.062  228.392 1.00 212.08 ?  31  ARG J CZ  1 
ATOM   19296 N NH1 . ARG K  3 25  ? 40.540  20.922  228.651 1.00 211.95 1  31  ARG J NH1 1 
ATOM   19297 N NH2 . ARG K  3 25  ? 38.385  20.152  228.827 1.00 216.20 ?  31  ARG J NH2 1 
ATOM   19298 N N   . SER K  3 26  ? 40.808  27.407  225.820 1.00 215.70 ?  32  SER J N   1 
ATOM   19299 C CA  . SER K  3 26  ? 41.802  28.461  225.976 1.00 213.02 ?  32  SER J CA  1 
ATOM   19300 C C   . SER K  3 26  ? 42.545  28.134  227.277 1.00 211.24 ?  32  SER J C   1 
ATOM   19301 O O   . SER K  3 26  ? 42.415  28.804  228.304 1.00 205.06 ?  32  SER J O   1 
ATOM   19302 C CB  . SER K  3 26  ? 41.163  29.854  226.000 1.00 210.14 ?  32  SER J CB  1 
ATOM   19303 O OG  . SER K  3 26  ? 42.143  30.874  226.090 1.00 206.91 ?  32  SER J OG  1 
ATOM   19304 N N   . VAL K  3 27  ? 43.347  27.071  227.234 1.00 211.46 ?  33  VAL J N   1 
ATOM   19305 C CA  . VAL K  3 27  ? 44.011  26.591  228.439 1.00 211.15 ?  33  VAL J CA  1 
ATOM   19306 C C   . VAL K  3 27  ? 45.114  27.557  228.842 1.00 211.43 ?  33  VAL J C   1 
ATOM   19307 O O   . VAL K  3 27  ? 45.991  27.890  228.033 1.00 213.36 ?  33  VAL J O   1 
ATOM   19308 C CB  . VAL K  3 27  ? 44.552  25.170  228.229 1.00 214.66 ?  33  VAL J CB  1 
ATOM   19309 C CG1 . VAL K  3 27  ? 45.164  24.652  229.520 1.00 214.19 ?  33  VAL J CG1 1 
ATOM   19310 C CG2 . VAL K  3 27  ? 43.433  24.251  227.762 1.00 215.04 ?  33  VAL J CG2 1 
ATOM   19311 N N   . ILE K  3 28  ? 45.078  28.014  230.090 1.00 205.13 ?  34  ILE J N   1 
ATOM   19312 C CA  . ILE K  3 28  ? 46.121  28.874  230.633 1.00 204.62 ?  34  ILE J CA  1 
ATOM   19313 C C   . ILE K  3 28  ? 46.923  28.048  231.625 1.00 204.72 ?  34  ILE J C   1 
ATOM   19314 O O   . ILE K  3 28  ? 46.365  27.502  232.586 1.00 203.50 ?  34  ILE J O   1 
ATOM   19315 C CB  . ILE K  3 28  ? 45.553  30.147  231.272 1.00 202.54 ?  34  ILE J CB  1 
ATOM   19316 C CG1 . ILE K  3 28  ? 44.463  30.722  230.370 1.00 202.50 ?  34  ILE J CG1 1 
ATOM   19317 C CG2 . ILE K  3 28  ? 46.661  31.165  231.505 1.00 202.82 ?  34  ILE J CG2 1 
ATOM   19318 C CD1 . ILE K  3 28  ? 43.698  31.839  230.985 1.00 200.67 ?  34  ILE J CD1 1 
ATOM   19319 N N   . TRP K  3 29  ? 48.228  27.964  231.397 1.00 206.67 ?  35  TRP J N   1 
ATOM   19320 C CA  . TRP K  3 29  ? 49.125  27.190  232.238 1.00 207.08 ?  35  TRP J CA  1 
ATOM   19321 C C   . TRP K  3 29  ? 49.874  28.101  233.202 1.00 206.01 ?  35  TRP J C   1 
ATOM   19322 O O   . TRP K  3 29  ? 50.136  29.270  232.909 1.00 206.02 ?  35  TRP J O   1 
ATOM   19323 C CB  . TRP K  3 29  ? 50.112  26.407  231.371 1.00 213.64 ?  35  TRP J CB  1 
ATOM   19324 C CG  . TRP K  3 29  ? 49.463  25.315  230.571 1.00 217.43 ?  35  TRP J CG  1 
ATOM   19325 C CD1 . TRP K  3 29  ? 48.987  25.408  229.296 1.00 217.12 ?  35  TRP J CD1 1 
ATOM   19326 C CD2 . TRP K  3 29  ? 49.274  23.951  230.970 1.00 222.63 ?  35  TRP J CD2 1 
ATOM   19327 N NE1 . TRP K  3 29  ? 48.480  24.197  228.890 1.00 221.67 ?  35  TRP J NE1 1 
ATOM   19328 C CE2 . TRP K  3 29  ? 48.650  23.285  229.898 1.00 225.27 ?  35  TRP J CE2 1 
ATOM   19329 C CE3 . TRP K  3 29  ? 49.561  23.231  232.135 1.00 225.54 ?  35  TRP J CE3 1 
ATOM   19330 C CZ2 . TRP K  3 29  ? 48.309  21.936  229.954 1.00 230.87 ?  35  TRP J CZ2 1 
ATOM   19331 C CZ3 . TRP K  3 29  ? 49.220  21.890  232.188 1.00 231.18 ?  35  TRP J CZ3 1 
ATOM   19332 C CH2 . TRP K  3 29  ? 48.600  21.258  231.105 1.00 233.86 ?  35  TRP J CH2 1 
ATOM   19333 N N   . TYR K  3 30  ? 50.203  27.545  234.365 1.00 212.40 ?  36  TYR J N   1 
ATOM   19334 C CA  . TYR K  3 30  ? 50.931  28.253  235.403 1.00 212.92 ?  36  TYR J CA  1 
ATOM   19335 C C   . TYR K  3 30  ? 51.946  27.299  236.023 1.00 217.77 ?  36  TYR J C   1 
ATOM   19336 O O   . TYR K  3 30  ? 51.714  26.087  236.082 1.00 224.15 ?  36  TYR J O   1 
ATOM   19337 C CB  . TYR K  3 30  ? 49.968  28.789  236.469 1.00 209.96 ?  36  TYR J CB  1 
ATOM   19338 C CG  . TYR K  3 30  ? 49.048  29.882  235.961 1.00 205.40 ?  36  TYR J CG  1 
ATOM   19339 C CD1 . TYR K  3 30  ? 49.458  31.208  235.884 1.00 205.15 ?  36  TYR J CD1 1 
ATOM   19340 C CD2 . TYR K  3 30  ? 47.758  29.571  235.549 1.00 203.05 ?  36  TYR J CD2 1 
ATOM   19341 C CE1 . TYR K  3 30  ? 48.600  32.193  235.413 1.00 204.18 ?  36  TYR J CE1 1 
ATOM   19342 C CE2 . TYR K  3 30  ? 46.901  30.541  235.080 1.00 202.15 ?  36  TYR J CE2 1 
ATOM   19343 C CZ  . TYR K  3 30  ? 47.323  31.850  235.013 1.00 203.93 ?  36  TYR J CZ  1 
ATOM   19344 O OH  . TYR K  3 30  ? 46.464  32.817  234.545 1.00 205.68 ?  36  TYR J OH  1 
ATOM   19345 N N   . GLN K  3 31  ? 53.073  27.841  236.478 1.00 216.30 ?  37  GLN J N   1 
ATOM   19346 C CA  . GLN K  3 31  ? 54.095  27.046  237.146 1.00 218.23 ?  37  GLN J CA  1 
ATOM   19347 C C   . GLN K  3 31  ? 54.285  27.577  238.558 1.00 213.93 ?  37  GLN J C   1 
ATOM   19348 O O   . GLN K  3 31  ? 54.442  28.787  238.751 1.00 210.20 ?  37  GLN J O   1 
ATOM   19349 C CB  . GLN K  3 31  ? 55.417  27.129  236.386 1.00 221.24 ?  37  GLN J CB  1 
ATOM   19350 C CG  . GLN K  3 31  ? 56.542  26.339  236.989 1.00 227.76 ?  37  GLN J CG  1 
ATOM   19351 C CD  . GLN K  3 31  ? 57.856  26.587  236.280 1.00 230.93 ?  37  GLN J CD  1 
ATOM   19352 O OE1 . GLN K  3 31  ? 58.667  25.677  236.127 1.00 226.66 ?  37  GLN J OE1 1 
ATOM   19353 N NE2 . GLN K  3 31  ? 58.091  27.833  235.878 1.00 238.89 ?  37  GLN J NE2 1 
ATOM   19354 N N   . GLN K  3 32  ? 54.275  26.673  239.541 1.00 214.44 ?  38  GLN J N   1 
ATOM   19355 C CA  . GLN K  3 32  ? 54.439  27.063  240.938 1.00 211.92 ?  38  GLN J CA  1 
ATOM   19356 C C   . GLN K  3 32  ? 55.607  26.335  241.603 1.00 216.67 ?  38  GLN J C   1 
ATOM   19357 O O   . GLN K  3 32  ? 55.479  25.170  241.996 1.00 220.94 ?  38  GLN J O   1 
ATOM   19358 C CB  . GLN K  3 32  ? 53.151  26.824  241.711 1.00 209.09 ?  38  GLN J CB  1 
ATOM   19359 C CG  . GLN K  3 32  ? 53.200  27.395  243.103 1.00 205.98 ?  38  GLN J CG  1 
ATOM   19360 C CD  . GLN K  3 32  ? 52.639  26.448  244.128 1.00 207.83 ?  38  GLN J CD  1 
ATOM   19361 O OE1 . GLN K  3 32  ? 52.625  25.233  243.930 1.00 212.04 ?  38  GLN J OE1 1 
ATOM   19362 N NE2 . GLN K  3 32  ? 52.167  26.999  245.237 1.00 205.21 ?  38  GLN J NE2 1 
ATOM   19363 N N   . ARG K  3 33  ? 56.731  27.034  241.721 1.00 226.87 ?  39  ARG J N   1 
ATOM   19364 C CA  . ARG K  3 33  ? 57.897  26.526  242.437 1.00 230.83 ?  39  ARG J CA  1 
ATOM   19365 C C   . ARG K  3 33  ? 57.584  26.462  243.933 1.00 231.20 ?  39  ARG J C   1 
ATOM   19366 O O   . ARG K  3 33  ? 56.913  27.349  244.466 1.00 228.22 ?  39  ARG J O   1 
ATOM   19367 C CB  . ARG K  3 33  ? 59.143  27.354  242.092 1.00 231.37 ?  39  ARG J CB  1 
ATOM   19368 C CG  . ARG K  3 33  ? 60.428  26.516  242.072 1.00 239.45 ?  39  ARG J CG  1 
ATOM   19369 C CD  . ARG K  3 33  ? 60.502  25.661  240.810 1.00 239.96 ?  39  ARG J CD  1 
ATOM   19370 N NE  . ARG K  3 33  ? 60.586  26.306  239.506 1.00 237.53 ?  39  ARG J NE  1 
ATOM   19371 C CZ  . ARG K  3 33  ? 60.744  25.624  238.373 1.00 238.67 ?  39  ARG J CZ  1 
ATOM   19372 N NH1 . ARG K  3 33  ? 60.832  24.295  238.398 1.00 241.94 1  39  ARG J NH1 1 
ATOM   19373 N NH2 . ARG K  3 33  ? 60.813  26.256  237.209 1.00 238.46 ?  39  ARG J NH2 1 
ATOM   19374 N N   . PRO K  3 34  ? 58.057  25.434  244.635 1.00 219.76 ?  40  PRO J N   1 
ATOM   19375 C CA  . PRO K  3 34  ? 57.752  25.288  246.071 1.00 218.51 ?  40  PRO J CA  1 
ATOM   19376 C C   . PRO K  3 34  ? 58.089  26.454  246.994 1.00 214.50 ?  40  PRO J C   1 
ATOM   19377 O O   . PRO K  3 34  ? 59.242  26.889  247.078 1.00 216.65 ?  40  PRO J O   1 
ATOM   19378 C CB  . PRO K  3 34  ? 58.570  24.052  246.469 1.00 223.01 ?  40  PRO J CB  1 
ATOM   19379 C CG  . PRO K  3 34  ? 59.578  23.867  245.388 1.00 226.06 ?  40  PRO J CG  1 
ATOM   19380 C CD  . PRO K  3 34  ? 58.901  24.333  244.145 1.00 222.03 ?  40  PRO J CD  1 
ATOM   19381 N N   . GLY K  3 35  ? 57.062  26.954  247.696 1.00 213.14 ?  41  GLY J N   1 
ATOM   19382 C CA  . GLY K  3 35  ? 57.184  28.057  248.635 1.00 212.35 ?  41  GLY J CA  1 
ATOM   19383 C C   . GLY K  3 35  ? 57.076  29.436  248.034 1.00 212.34 ?  41  GLY J C   1 
ATOM   19384 O O   . GLY K  3 35  ? 57.352  30.424  248.729 1.00 213.08 ?  41  GLY J O   1 
ATOM   19385 N N   . GLN K  3 36  ? 56.668  29.536  246.773 1.00 231.25 ?  42  GLN J N   1 
ATOM   19386 C CA  . GLN K  3 36  ? 56.568  30.814  246.084 1.00 230.12 ?  42  GLN J CA  1 
ATOM   19387 C C   . GLN K  3 36  ? 55.184  31.041  245.483 1.00 227.13 ?  42  GLN J C   1 
ATOM   19388 O O   . GLN K  3 36  ? 54.250  30.279  245.755 1.00 222.69 ?  42  GLN J O   1 
ATOM   19389 C CB  . GLN K  3 36  ? 57.636  30.860  244.997 1.00 232.26 ?  42  GLN J CB  1 
ATOM   19390 C CG  . GLN K  3 36  ? 59.028  30.661  245.559 1.00 234.57 ?  42  GLN J CG  1 
ATOM   19391 C CD  . GLN K  3 36  ? 60.104  30.714  244.503 1.00 234.51 ?  42  GLN J CD  1 
ATOM   19392 O OE1 . GLN K  3 36  ? 59.858  31.117  243.366 1.00 235.96 ?  42  GLN J OE1 1 
ATOM   19393 N NE2 . GLN K  3 36  ? 61.311  30.300  244.873 1.00 236.27 ?  42  GLN J NE2 1 
ATOM   19394 N N   . ALA K  3 37  ? 55.031  32.154  244.639 1.00 221.64 ?  43  ALA J N   1 
ATOM   19395 C CA  . ALA K  3 37  ? 53.735  32.447  244.041 1.00 217.49 ?  43  ALA J CA  1 
ATOM   19396 C C   . ALA K  3 37  ? 53.675  31.976  242.589 1.00 217.75 ?  43  ALA J C   1 
ATOM   19397 O O   . ALA K  3 37  ? 54.685  31.981  241.879 1.00 221.50 ?  43  ALA J O   1 
ATOM   19398 C CB  . ALA K  3 37  ? 53.434  33.948  244.099 1.00 216.57 ?  43  ALA J CB  1 
ATOM   19399 N N   . PRO K  3 38  ? 52.487  31.557  242.152 1.00 212.52 ?  44  PRO J N   1 
ATOM   19400 C CA  . PRO K  3 38  ? 52.293  31.102  240.763 1.00 210.30 ?  44  PRO J CA  1 
ATOM   19401 C C   . PRO K  3 38  ? 52.675  32.127  239.698 1.00 212.36 ?  44  PRO J C   1 
ATOM   19402 O O   . PRO K  3 38  ? 52.320  33.305  239.783 1.00 215.75 ?  44  PRO J O   1 
ATOM   19403 C CB  . PRO K  3 38  ? 50.794  30.783  240.712 1.00 210.04 ?  44  PRO J CB  1 
ATOM   19404 C CG  . PRO K  3 38  ? 50.437  30.454  242.126 1.00 210.32 ?  44  PRO J CG  1 
ATOM   19405 C CD  . PRO K  3 38  ? 51.284  31.351  242.976 1.00 211.43 ?  44  PRO J CD  1 
ATOM   19406 N N   . SER K  3 39  ? 53.412  31.661  238.686 1.00 212.33 ?  45  SER J N   1 
ATOM   19407 C CA  . SER K  3 39  ? 53.857  32.491  237.575 1.00 213.07 ?  45  SER J CA  1 
ATOM   19408 C C   . SER K  3 39  ? 53.263  31.981  236.265 1.00 212.71 ?  45  SER J C   1 
ATOM   19409 O O   . SER K  3 39  ? 53.065  30.776  236.080 1.00 213.88 ?  45  SER J O   1 
ATOM   19410 C CB  . SER K  3 39  ? 55.387  32.505  237.467 1.00 214.87 ?  45  SER J CB  1 
ATOM   19411 O OG  . SER K  3 39  ? 55.892  31.201  237.226 1.00 215.73 ?  45  SER J OG  1 
ATOM   19412 N N   . LEU K  3 40  ? 52.979  32.913  235.357 1.00 213.73 ?  46  LEU J N   1 
ATOM   19413 C CA  . LEU K  3 40  ? 52.398  32.582  234.060 1.00 208.54 ?  46  LEU J CA  1 
ATOM   19414 C C   . LEU K  3 40  ? 53.452  31.972  233.142 1.00 212.76 ?  46  LEU J C   1 
ATOM   19415 O O   . LEU K  3 40  ? 54.545  32.527  232.988 1.00 216.48 ?  46  LEU J O   1 
ATOM   19416 C CB  . LEU K  3 40  ? 51.787  33.822  233.406 1.00 206.44 ?  46  LEU J CB  1 
ATOM   19417 C CG  . LEU K  3 40  ? 51.184  33.605  232.014 1.00 210.21 ?  46  LEU J CG  1 
ATOM   19418 C CD1 . LEU K  3 40  ? 50.033  32.607  232.062 1.00 207.99 ?  46  LEU J CD1 1 
ATOM   19419 C CD2 . LEU K  3 40  ? 50.733  34.924  231.405 1.00 211.97 ?  46  LEU J CD2 1 
ATOM   19420 N N   . ILE K  3 41  ? 53.126  30.837  232.524 1.00 208.43 ?  47  ILE J N   1 
ATOM   19421 C CA  . ILE K  3 41  ? 54.027  30.156  231.593 1.00 213.58 ?  47  ILE J CA  1 
ATOM   19422 C C   . ILE K  3 41  ? 53.487  30.210  230.172 1.00 216.67 ?  47  ILE J C   1 
ATOM   19423 O O   . ILE K  3 41  ? 54.148  30.722  229.266 1.00 220.08 ?  47  ILE J O   1 
ATOM   19424 C CB  . ILE K  3 41  ? 54.285  28.697  232.031 1.00 212.77 ?  47  ILE J CB  1 
ATOM   19425 C CG1 . ILE K  3 41  ? 54.986  28.662  233.381 1.00 212.99 ?  47  ILE J CG1 1 
ATOM   19426 C CG2 . ILE K  3 41  ? 55.090  27.959  230.972 1.00 219.15 ?  47  ILE J CG2 1 
ATOM   19427 C CD1 . ILE K  3 41  ? 56.325  29.349  233.375 1.00 213.92 ?  47  ILE J CD1 1 
ATOM   19428 N N   . ILE K  3 42  ? 52.285  29.681  229.952 1.00 228.11 ?  48  ILE J N   1 
ATOM   19429 C CA  . ILE K  3 42  ? 51.675  29.658  228.628 1.00 226.28 ?  48  ILE J CA  1 
ATOM   19430 C C   . ILE K  3 42  ? 50.204  30.018  228.772 1.00 219.90 ?  48  ILE J C   1 
ATOM   19431 O O   . ILE K  3 42  ? 49.453  29.309  229.451 1.00 217.70 ?  48  ILE J O   1 
ATOM   19432 C CB  . ILE K  3 42  ? 51.819  28.290  227.937 1.00 227.91 ?  48  ILE J CB  1 
ATOM   19433 C CG1 . ILE K  3 42  ? 53.283  28.006  227.609 1.00 230.46 ?  48  ILE J CG1 1 
ATOM   19434 C CG2 . ILE K  3 42  ? 50.974  28.239  226.681 1.00 227.77 ?  48  ILE J CG2 1 
ATOM   19435 C CD1 . ILE K  3 42  ? 53.500  26.677  226.942 1.00 239.15 ?  48  ILE J CD1 1 
ATOM   19436 N N   . TYR K  3 43  ? 49.795  31.112  228.144 1.00 223.02 ?  49  TYR J N   1 
ATOM   19437 C CA  . TYR K  3 43  ? 48.399  31.507  228.094 1.00 216.72 ?  49  TYR J CA  1 
ATOM   19438 C C   . TYR K  3 43  ? 47.898  31.311  226.671 1.00 224.62 ?  49  TYR J C   1 
ATOM   19439 O O   . TYR K  3 43  ? 48.679  31.297  225.716 1.00 231.76 ?  49  TYR J O   1 
ATOM   19440 C CB  . TYR K  3 43  ? 48.215  32.963  228.544 1.00 209.41 ?  49  TYR J CB  1 
ATOM   19441 C CG  . TYR K  3 43  ? 48.830  33.969  227.597 1.00 214.62 ?  49  TYR J CG  1 
ATOM   19442 C CD1 . TYR K  3 43  ? 50.177  34.301  227.685 1.00 216.23 ?  49  TYR J CD1 1 
ATOM   19443 C CD2 . TYR K  3 43  ? 48.068  34.582  226.610 1.00 217.00 ?  49  TYR J CD2 1 
ATOM   19444 C CE1 . TYR K  3 43  ? 50.747  35.215  226.816 1.00 221.42 ?  49  TYR J CE1 1 
ATOM   19445 C CE2 . TYR K  3 43  ? 48.629  35.496  225.737 1.00 220.28 ?  49  TYR J CE2 1 
ATOM   19446 C CZ  . TYR K  3 43  ? 49.969  35.809  225.844 1.00 221.58 ?  49  TYR J CZ  1 
ATOM   19447 O OH  . TYR K  3 43  ? 50.538  36.718  224.980 1.00 219.51 ?  49  TYR J OH  1 
ATOM   19448 N N   . ASN K  3 44  ? 46.585  31.164  226.537 1.00 218.00 ?  50  ASN J N   1 
ATOM   19449 C CA  . ASN K  3 44  ? 45.947  30.923  225.246 1.00 220.10 ?  50  ASN J CA  1 
ATOM   19450 C C   . ASN K  3 44  ? 46.575  29.717  224.540 1.00 236.80 ?  50  ASN J C   1 
ATOM   19451 O O   . ASN K  3 44  ? 47.162  29.822  223.461 1.00 244.35 ?  50  ASN J O   1 
ATOM   19452 C CB  . ASN K  3 44  ? 45.998  32.174  224.367 1.00 210.52 ?  50  ASN J CB  1 
ATOM   19453 C CG  . ASN K  3 44  ? 45.125  32.054  223.134 1.00 215.52 ?  50  ASN J CG  1 
ATOM   19454 O OD1 . ASN K  3 44  ? 44.219  31.221  223.079 1.00 216.95 ?  50  ASN J OD1 1 
ATOM   19455 N ND2 . ASN K  3 44  ? 45.397  32.884  222.136 1.00 221.42 ?  50  ASN J ND2 1 
ATOM   19456 N N   . ASN K  3 45  ? 46.470  28.565  225.200 1.00 208.73 ?  51  ASN J N   1 
ATOM   19457 C CA  . ASN K  3 45  ? 46.929  27.284  224.666 1.00 222.32 ?  51  ASN J CA  1 
ATOM   19458 C C   . ASN K  3 45  ? 48.428  27.169  224.389 1.00 230.58 ?  51  ASN J C   1 
ATOM   19459 O O   . ASN K  3 45  ? 49.091  26.295  224.953 1.00 237.15 ?  51  ASN J O   1 
ATOM   19460 C CB  . ASN K  3 45  ? 46.170  26.977  223.374 1.00 224.75 ?  51  ASN J CB  1 
ATOM   19461 C CG  . ASN K  3 45  ? 44.674  26.887  223.585 1.00 216.36 ?  51  ASN J CG  1 
ATOM   19462 O OD1 . ASN K  3 45  ? 44.205  26.357  224.591 1.00 214.65 ?  51  ASN J OD1 1 
ATOM   19463 N ND2 . ASN K  3 45  ? 43.913  27.423  222.636 1.00 210.23 ?  51  ASN J ND2 1 
ATOM   19464 N N   . ASN K  3 46  ? 48.981  28.032  223.535 1.00 227.72 ?  52  ASN J N   1 
ATOM   19465 C CA  . ASN K  3 46  ? 50.393  27.916  223.173 1.00 234.38 ?  52  ASN J CA  1 
ATOM   19466 C C   . ASN K  3 46  ? 51.025  29.279  222.922 1.00 228.30 ?  52  ASN J C   1 
ATOM   19467 O O   . ASN K  3 46  ? 51.867  29.427  222.031 1.00 233.27 ?  52  ASN J O   1 
ATOM   19468 C CB  . ASN K  3 46  ? 50.588  27.020  221.946 1.00 245.26 ?  52  ASN J CB  1 
ATOM   19469 C CG  . ASN K  3 46  ? 51.985  26.441  221.864 1.00 254.68 ?  52  ASN J CG  1 
ATOM   19470 O OD1 . ASN K  3 46  ? 52.703  26.373  222.862 1.00 254.10 ?  52  ASN J OD1 1 
ATOM   19471 N ND2 . ASN K  3 46  ? 52.385  26.039  220.665 1.00 263.60 ?  52  ASN J ND2 1 
ATOM   19472 N N   . ASP K  3 47  ? 50.649  30.281  223.701 1.00 237.81 ?  53  ASP J N   1 
ATOM   19473 C CA  . ASP K  3 47  ? 51.241  31.608  223.590 1.00 231.79 ?  53  ASP J CA  1 
ATOM   19474 C C   . ASP K  3 47  ? 52.043  31.916  224.842 1.00 227.94 ?  53  ASP J C   1 
ATOM   19475 O O   . ASP K  3 47  ? 51.490  32.020  225.941 1.00 219.12 ?  53  ASP J O   1 
ATOM   19476 C CB  . ASP K  3 47  ? 50.178  32.678  223.337 1.00 214.87 ?  53  ASP J CB  1 
ATOM   19477 C CG  . ASP K  3 47  ? 49.524  32.525  221.986 1.00 213.40 ?  53  ASP J CG  1 
ATOM   19478 O OD1 . ASP K  3 47  ? 50.160  31.939  221.080 1.00 225.22 ?  53  ASP J OD1 1 
ATOM   19479 O OD2 . ASP K  3 47  ? 48.385  32.993  221.825 1.00 206.13 -1 53  ASP J OD2 1 
ATOM   19480 N N   . ARG K  3 48  ? 53.371  32.081  224.658 1.00 228.59 ?  54  ARG J N   1 
ATOM   19481 C CA  . ARG K  3 48  ? 54.251  32.361  225.787 1.00 225.93 ?  54  ARG J CA  1 
ATOM   19482 C C   . ARG K  3 48  ? 54.516  33.854  225.892 1.00 218.82 ?  54  ARG J C   1 
ATOM   19483 O O   . ARG K  3 48  ? 54.815  34.501  224.876 1.00 221.35 ?  54  ARG J O   1 
ATOM   19484 C CB  . ARG K  3 48  ? 55.573  31.594  225.638 1.00 233.21 ?  54  ARG J CB  1 
ATOM   19485 C CG  . ARG K  3 48  ? 56.102  31.530  224.202 1.00 242.64 ?  54  ARG J CG  1 
ATOM   19486 C CD  . ARG K  3 48  ? 57.600  31.279  224.075 1.00 252.04 ?  54  ARG J CD  1 
ATOM   19487 N NE  . ARG K  3 48  ? 58.386  32.234  224.800 1.00 253.57 ?  54  ARG J NE  1 
ATOM   19488 C CZ  . ARG K  3 48  ? 58.940  33.301  224.250 1.00 249.61 ?  54  ARG J CZ  1 
ATOM   19489 N NH1 . ARG K  3 48  ? 58.784  33.534  222.947 1.00 242.12 1  54  ARG J NH1 1 
ATOM   19490 N NH2 . ARG K  3 48  ? 59.666  34.105  224.993 1.00 257.24 ?  54  ARG J NH2 1 
ATOM   19491 N N   . PRO K  3 49  ? 54.442  34.414  227.102 1.00 222.28 ?  55  PRO J N   1 
ATOM   19492 C CA  . PRO K  3 49  ? 54.742  35.835  227.291 1.00 220.70 ?  55  PRO J CA  1 
ATOM   19493 C C   . PRO K  3 49  ? 56.230  36.120  227.241 1.00 224.26 ?  55  PRO J C   1 
ATOM   19494 O O   . PRO K  3 49  ? 57.034  35.227  226.951 1.00 227.27 ?  55  PRO J O   1 
ATOM   19495 C CB  . PRO K  3 49  ? 54.148  36.138  228.676 1.00 216.85 ?  55  PRO J CB  1 
ATOM   19496 C CG  . PRO K  3 49  ? 54.222  34.846  229.399 1.00 215.27 ?  55  PRO J CG  1 
ATOM   19497 C CD  . PRO K  3 49  ? 53.982  33.778  228.354 1.00 218.04 ?  55  PRO J CD  1 
ATOM   19498 N N   . SER K  3 50  ? 56.617  37.360  227.532 1.00 238.50 ?  56  SER J N   1 
ATOM   19499 C CA  . SER K  3 50  ? 58.029  37.712  227.495 1.00 243.52 ?  56  SER J CA  1 
ATOM   19500 C C   . SER K  3 50  ? 58.710  37.062  228.688 1.00 245.01 ?  56  SER J C   1 
ATOM   19501 O O   . SER K  3 50  ? 58.232  37.171  229.822 1.00 240.66 ?  56  SER J O   1 
ATOM   19502 C CB  . SER K  3 50  ? 58.195  39.231  227.545 1.00 244.42 ?  56  SER J CB  1 
ATOM   19503 O OG  . SER K  3 50  ? 57.579  39.771  228.705 1.00 240.58 ?  56  SER J OG  1 
ATOM   19504 N N   . GLY K  3 51  ? 59.830  36.382  228.437 1.00 242.29 ?  57  GLY J N   1 
ATOM   19505 C CA  . GLY K  3 51  ? 60.555  35.731  229.506 1.00 238.55 ?  57  GLY J CA  1 
ATOM   19506 C C   . GLY K  3 51  ? 60.476  34.215  229.508 1.00 235.63 ?  57  GLY J C   1 
ATOM   19507 O O   . GLY K  3 51  ? 61.253  33.579  230.232 1.00 231.50 ?  57  GLY J O   1 
ATOM   19508 N N   . ILE K  3 52  ? 59.582  33.613  228.731 1.00 232.44 ?  58  ILE J N   1 
ATOM   19509 C CA  . ILE K  3 52  ? 59.402  32.163  228.703 1.00 240.34 ?  58  ILE J CA  1 
ATOM   19510 C C   . ILE K  3 52  ? 60.121  31.561  227.498 1.00 253.51 ?  58  ILE J C   1 
ATOM   19511 O O   . ILE K  3 52  ? 59.886  32.000  226.371 1.00 257.92 ?  58  ILE J O   1 
ATOM   19512 C CB  . ILE K  3 52  ? 57.910  31.803  228.653 1.00 238.71 ?  58  ILE J CB  1 
ATOM   19513 C CG1 . ILE K  3 52  ? 57.167  32.502  229.787 1.00 225.95 ?  58  ILE J CG1 1 
ATOM   19514 C CG2 . ILE K  3 52  ? 57.715  30.295  228.664 1.00 247.25 ?  58  ILE J CG2 1 
ATOM   19515 C CD1 . ILE K  3 52  ? 57.670  32.113  231.151 1.00 221.08 ?  58  ILE J CD1 1 
ATOM   19516 N N   . PRO K  3 53  ? 61.020  30.602  227.698 1.00 246.96 ?  59  PRO J N   1 
ATOM   19517 C CA  . PRO K  3 53  ? 61.740  29.967  226.582 1.00 259.86 ?  59  PRO J CA  1 
ATOM   19518 C C   . PRO K  3 53  ? 60.806  29.159  225.684 1.00 269.47 ?  59  PRO J C   1 
ATOM   19519 O O   . PRO K  3 53  ? 59.649  28.893  226.019 1.00 265.68 ?  59  PRO J O   1 
ATOM   19520 C CB  . PRO K  3 53  ? 62.768  29.074  227.282 1.00 260.54 ?  59  PRO J CB  1 
ATOM   19521 C CG  . PRO K  3 53  ? 62.172  28.809  228.629 1.00 250.67 ?  59  PRO J CG  1 
ATOM   19522 C CD  . PRO K  3 53  ? 61.448  30.065  229.000 1.00 240.59 ?  59  PRO J CD  1 
ATOM   19523 N N   . ASP K  3 54  ? 61.310  28.787  224.498 1.00 269.10 ?  60  ASP J N   1 
ATOM   19524 C CA  . ASP K  3 54  ? 60.478  28.021  223.573 1.00 278.96 ?  60  ASP J CA  1 
ATOM   19525 C C   . ASP K  3 54  ? 60.452  26.547  223.946 1.00 283.80 ?  60  ASP J C   1 
ATOM   19526 O O   . ASP K  3 54  ? 59.849  25.744  223.225 1.00 290.02 ?  60  ASP J O   1 
ATOM   19527 C CB  . ASP K  3 54  ? 61.006  28.110  222.135 1.00 291.27 ?  60  ASP J CB  1 
ATOM   19528 C CG  . ASP K  3 54  ? 62.434  27.578  222.003 1.00 288.95 ?  60  ASP J CG  1 
ATOM   19529 O OD1 . ASP K  3 54  ? 63.174  27.622  223.006 1.00 278.30 ?  60  ASP J OD1 1 
ATOM   19530 O OD2 . ASP K  3 54  ? 62.807  27.078  220.915 1.00 298.26 -1 60  ASP J OD2 1 
ATOM   19531 N N   . ARG K  3 55  ? 61.097  26.180  225.058 1.00 276.86 ?  61  ARG J N   1 
ATOM   19532 C CA  . ARG K  3 55  ? 61.080  24.802  225.528 1.00 280.66 ?  61  ARG J CA  1 
ATOM   19533 C C   . ARG K  3 55  ? 59.706  24.414  226.053 1.00 276.81 ?  61  ARG J C   1 
ATOM   19534 O O   . ARG K  3 55  ? 59.346  23.231  226.040 1.00 283.66 ?  61  ARG J O   1 
ATOM   19535 C CB  . ARG K  3 55  ? 62.138  24.614  226.614 1.00 273.80 ?  61  ARG J CB  1 
ATOM   19536 C CG  . ARG K  3 55  ? 63.540  25.008  226.181 1.00 274.99 ?  61  ARG J CG  1 
ATOM   19537 C CD  . ARG K  3 55  ? 64.586  24.650  227.226 1.00 269.11 ?  61  ARG J CD  1 
ATOM   19538 N NE  . ARG K  3 55  ? 64.334  25.321  228.501 1.00 255.57 ?  61  ARG J NE  1 
ATOM   19539 C CZ  . ARG K  3 55  ? 63.797  24.742  229.570 1.00 250.10 ?  61  ARG J CZ  1 
ATOM   19540 N NH1 . ARG K  3 55  ? 63.447  23.463  229.531 1.00 257.02 1  61  ARG J NH1 1 
ATOM   19541 N NH2 . ARG K  3 55  ? 63.609  25.443  230.680 1.00 237.85 ?  61  ARG J NH2 1 
ATOM   19542 N N   . PHE K  3 56  ? 58.931  25.391  226.517 1.00 289.58 ?  62  PHE J N   1 
ATOM   19543 C CA  . PHE K  3 56  ? 57.600  25.144  227.049 1.00 283.58 ?  62  PHE J CA  1 
ATOM   19544 C C   . PHE K  3 56  ? 56.588  25.330  225.925 1.00 287.82 ?  62  PHE J C   1 
ATOM   19545 O O   . PHE K  3 56  ? 56.430  26.440  225.404 1.00 281.82 ?  62  PHE J O   1 
ATOM   19546 C CB  . PHE K  3 56  ? 57.304  26.092  228.212 1.00 265.87 ?  62  PHE J CB  1 
ATOM   19547 C CG  . PHE K  3 56  ? 58.250  25.938  229.367 1.00 260.94 ?  62  PHE J CG  1 
ATOM   19548 C CD1 . PHE K  3 56  ? 59.420  26.676  229.417 1.00 256.91 ?  62  PHE J CD1 1 
ATOM   19549 C CD2 . PHE K  3 56  ? 57.989  25.037  230.386 1.00 258.56 ?  62  PHE J CD2 1 
ATOM   19550 C CE1 . PHE K  3 56  ? 60.304  26.534  230.467 1.00 249.47 ?  62  PHE J CE1 1 
ATOM   19551 C CE2 . PHE K  3 56  ? 58.872  24.890  231.440 1.00 252.44 ?  62  PHE J CE2 1 
ATOM   19552 C CZ  . PHE K  3 56  ? 60.031  25.640  231.480 1.00 248.22 ?  62  PHE J CZ  1 
ATOM   19553 N N   . SER K  3 57  ? 55.906  24.249  225.553 1.00 257.29 ?  63  SER J N   1 
ATOM   19554 C CA  . SER K  3 57  ? 54.894  24.293  224.510 1.00 260.59 ?  63  SER J CA  1 
ATOM   19555 C C   . SER K  3 57  ? 53.640  23.589  225.004 1.00 257.69 ?  63  SER J C   1 
ATOM   19556 O O   . SER K  3 57  ? 53.710  22.637  225.786 1.00 258.61 ?  63  SER J O   1 
ATOM   19557 C CB  . SER K  3 57  ? 55.403  23.639  223.213 1.00 275.09 ?  63  SER J CB  1 
ATOM   19558 O OG  . SER K  3 57  ? 55.749  22.279  223.423 1.00 279.76 ?  63  SER J OG  1 
ATOM   19559 N N   . GLY K  3 58  ? 52.490  24.057  224.525 1.00 254.58 ?  64  GLY J N   1 
ATOM   19560 C CA  . GLY K  3 58  ? 51.210  23.492  224.903 1.00 251.60 ?  64  GLY J CA  1 
ATOM   19561 C C   . GLY K  3 58  ? 50.404  23.020  223.709 1.00 256.86 ?  64  GLY J C   1 
ATOM   19562 O O   . GLY K  3 58  ? 50.579  23.503  222.588 1.00 259.42 ?  64  GLY J O   1 
ATOM   19563 N N   . SER K  3 59  ? 49.520  22.059  223.963 1.00 234.76 ?  65  SER J N   1 
ATOM   19564 C CA  . SER K  3 59  ? 48.655  21.538  222.917 1.00 238.01 ?  65  SER J CA  1 
ATOM   19565 C C   . SER K  3 59  ? 47.664  22.606  222.454 1.00 227.14 ?  65  SER J C   1 
ATOM   19566 O O   . SER K  3 59  ? 47.107  23.340  223.277 1.00 217.43 ?  65  SER J O   1 
ATOM   19567 C CB  . SER K  3 59  ? 47.900  20.302  223.407 1.00 241.77 ?  65  SER J CB  1 
ATOM   19568 O OG  . SER K  3 59  ? 47.018  20.624  224.467 1.00 231.85 ?  65  SER J OG  1 
ATOM   19569 N N   . PRO K  3 60  ? 47.432  22.716  221.149 1.00 229.36 ?  66  PRO J N   1 
ATOM   19570 C CA  . PRO K  3 60  ? 46.494  23.722  220.635 1.00 218.69 ?  66  PRO J CA  1 
ATOM   19571 C C   . PRO K  3 60  ? 45.077  23.473  221.133 1.00 210.64 ?  66  PRO J C   1 
ATOM   19572 O O   . PRO K  3 60  ? 44.638  22.330  221.278 1.00 215.69 ?  66  PRO J O   1 
ATOM   19573 C CB  . PRO K  3 60  ? 46.608  23.568  219.114 1.00 222.86 ?  66  PRO J CB  1 
ATOM   19574 C CG  . PRO K  3 60  ? 47.095  22.183  218.914 1.00 236.01 ?  66  PRO J CG  1 
ATOM   19575 C CD  . PRO K  3 60  ? 48.017  21.909  220.067 1.00 240.11 ?  66  PRO J CD  1 
ATOM   19576 N N   . GLY K  3 61  ? 44.362  24.561  221.401 1.00 207.93 ?  67  GLY J N   1 
ATOM   19577 C CA  . GLY K  3 61  ? 43.001  24.452  221.887 1.00 207.43 ?  67  GLY J CA  1 
ATOM   19578 C C   . GLY K  3 61  ? 41.968  24.329  220.787 1.00 208.16 ?  67  GLY J C   1 
ATOM   19579 O O   . GLY K  3 61  ? 40.889  24.925  220.853 1.00 207.76 ?  67  GLY J O   1 
ATOM   19580 N N   . SER K  3 62  A 42.314  23.558  219.751 1.00 208.65 ?  67  SER J N   1 
ATOM   19581 C CA  . SER K  3 62  A 41.443  23.292  218.617 1.00 206.33 ?  67  SER J CA  1 
ATOM   19582 C C   . SER K  3 62  A 41.111  21.811  218.450 1.00 214.35 ?  67  SER J C   1 
ATOM   19583 O O   . SER K  3 62  A 40.309  21.469  217.572 1.00 212.68 ?  67  SER J O   1 
ATOM   19584 C CB  . SER K  3 62  A 42.082  23.823  217.322 1.00 209.09 ?  67  SER J CB  1 
ATOM   19585 O OG  . SER K  3 62  A 43.331  23.199  217.066 1.00 222.31 ?  67  SER J OG  1 
ATOM   19586 N N   . THR K  3 63  B 41.722  20.931  219.248 1.00 219.28 ?  67  THR J N   1 
ATOM   19587 C CA  . THR K  3 63  B 41.483  19.489  219.218 1.00 227.30 ?  67  THR J CA  1 
ATOM   19588 C C   . THR K  3 63  B 40.378  19.091  220.195 1.00 221.95 ?  67  THR J C   1 
ATOM   19589 O O   . THR K  3 63  B 40.476  19.366  221.396 1.00 218.70 ?  67  THR J O   1 
ATOM   19590 C CB  . THR K  3 63  B 42.768  18.732  219.550 1.00 240.56 ?  67  THR J CB  1 
ATOM   19591 O OG1 . THR K  3 63  B 43.826  19.200  218.706 1.00 245.92 ?  67  THR J OG1 1 
ATOM   19592 C CG2 . THR K  3 63  B 42.583  17.237  219.334 1.00 248.98 ?  67  THR J CG2 1 
ATOM   19593 N N   . PHE K  3 64  C 39.336  18.444  219.681 1.00 231.86 ?  67  PHE J N   1 
ATOM   19594 C CA  . PHE K  3 64  C 38.171  18.049  220.467 1.00 226.54 ?  67  PHE J CA  1 
ATOM   19595 C C   . PHE K  3 64  C 38.281  16.597  220.921 1.00 236.55 ?  67  PHE J C   1 
ATOM   19596 O O   . PHE K  3 64  C 38.356  15.686  220.089 1.00 243.82 ?  67  PHE J O   1 
ATOM   19597 C CB  . PHE K  3 64  C 36.874  18.257  219.688 1.00 217.50 ?  67  PHE J CB  1 
ATOM   19598 C CG  . PHE K  3 64  C 36.708  19.639  219.145 1.00 207.21 ?  67  PHE J CG  1 
ATOM   19599 C CD1 . PHE K  3 64  C 37.106  20.735  219.894 1.00 201.94 ?  67  PHE J CD1 1 
ATOM   19600 C CD2 . PHE K  3 64  C 36.130  19.851  217.907 1.00 202.62 ?  67  PHE J CD2 1 
ATOM   19601 C CE1 . PHE K  3 64  C 36.942  22.017  219.414 1.00 192.34 ?  67  PHE J CE1 1 
ATOM   19602 C CE2 . PHE K  3 64  C 35.964  21.133  217.419 1.00 194.45 ?  67  PHE J CE2 1 
ATOM   19603 C CZ  . PHE K  3 64  C 36.371  22.218  218.174 1.00 189.68 ?  67  PHE J CZ  1 
ATOM   19604 N N   . GLY K  3 65  ? 38.291  16.392  222.231 1.00 219.20 ?  68  GLY J N   1 
ATOM   19605 C CA  . GLY K  3 65  ? 38.351  15.076  222.825 1.00 227.92 ?  68  GLY J CA  1 
ATOM   19606 C C   . GLY K  3 65  ? 39.667  14.667  223.458 1.00 238.45 ?  68  GLY J C   1 
ATOM   19607 O O   . GLY K  3 65  ? 39.872  13.467  223.682 1.00 247.73 ?  68  GLY J O   1 
ATOM   19608 N N   . THR K  3 66  ? 40.551  15.613  223.758 1.00 230.57 ?  69  THR J N   1 
ATOM   19609 C CA  . THR K  3 66  ? 41.843  15.337  224.366 1.00 237.06 ?  69  THR J CA  1 
ATOM   19610 C C   . THR K  3 66  ? 42.029  16.204  225.605 1.00 228.29 ?  69  THR J C   1 
ATOM   19611 O O   . THR K  3 66  ? 41.373  17.233  225.773 1.00 216.71 ?  69  THR J O   1 
ATOM   19612 C CB  . THR K  3 66  ? 42.989  15.577  223.375 1.00 241.98 ?  69  THR J CB  1 
ATOM   19613 O OG1 . THR K  3 66  ? 42.871  16.894  222.824 1.00 232.84 ?  69  THR J OG1 1 
ATOM   19614 C CG2 . THR K  3 66  ? 42.944  14.553  222.247 1.00 249.70 ?  69  THR J CG2 1 
ATOM   19615 N N   . THR K  3 67  ? 42.934  15.779  226.478 1.00 237.66 ?  70  THR J N   1 
ATOM   19616 C CA  . THR K  3 67  ? 43.221  16.520  227.696 1.00 225.74 ?  70  THR J CA  1 
ATOM   19617 C C   . THR K  3 67  ? 44.334  17.530  227.424 1.00 224.04 ?  70  THR J C   1 
ATOM   19618 O O   . THR K  3 67  ? 45.103  17.400  226.469 1.00 233.18 ?  70  THR J O   1 
ATOM   19619 C CB  . THR K  3 67  ? 43.618  15.576  228.835 1.00 228.11 ?  70  THR J CB  1 
ATOM   19620 O OG1 . THR K  3 67  ? 44.765  14.811  228.447 1.00 240.75 ?  70  THR J OG1 1 
ATOM   19621 C CG2 . THR K  3 67  ? 42.472  14.623  229.175 1.00 228.31 ?  70  THR J CG2 1 
ATOM   19622 N N   . ALA K  3 68  ? 44.406  18.552  228.276 1.00 232.52 ?  71  ALA J N   1 
ATOM   19623 C CA  . ALA K  3 68  ? 45.444  19.566  228.138 1.00 230.30 ?  71  ALA J CA  1 
ATOM   19624 C C   . ALA K  3 68  ? 46.817  18.974  228.436 1.00 238.68 ?  71  ALA J C   1 
ATOM   19625 O O   . ALA K  3 68  ? 47.027  18.365  229.490 1.00 237.82 ?  71  ALA J O   1 
ATOM   19626 C CB  . ALA K  3 68  ? 45.151  20.737  229.075 1.00 216.37 ?  71  ALA J CB  1 
ATOM   19627 N N   . THR K  3 69  ? 47.751  19.156  227.498 1.00 218.13 ?  72  THR J N   1 
ATOM   19628 C CA  . THR K  3 69  ? 49.099  18.603  227.582 1.00 225.79 ?  72  THR J CA  1 
ATOM   19629 C C   . THR K  3 69  ? 50.150  19.701  227.461 1.00 223.41 ?  72  THR J C   1 
ATOM   19630 O O   . THR K  3 69  ? 50.107  20.507  226.526 1.00 223.70 ?  72  THR J O   1 
ATOM   19631 C CB  . THR K  3 69  ? 49.312  17.551  226.489 1.00 240.22 ?  72  THR J CB  1 
ATOM   19632 O OG1 . THR K  3 69  ? 48.308  16.536  226.605 1.00 242.42 ?  72  THR J OG1 1 
ATOM   19633 C CG2 . THR K  3 69  ? 50.681  16.905  226.620 1.00 249.16 ?  72  THR J CG2 1 
ATOM   19634 N N   . LEU K  3 70  ? 51.088  19.727  228.412 1.00 247.92 ?  73  LEU J N   1 
ATOM   19635 C CA  . LEU K  3 70  ? 52.204  20.673  228.451 1.00 244.65 ?  73  LEU J CA  1 
ATOM   19636 C C   . LEU K  3 70  ? 53.520  19.956  228.146 1.00 253.88 ?  73  LEU J C   1 
ATOM   19637 O O   . LEU K  3 70  ? 53.974  19.129  228.943 1.00 252.70 ?  73  LEU J O   1 
ATOM   19638 C CB  . LEU K  3 70  ? 52.268  21.367  229.810 1.00 230.99 ?  73  LEU J CB  1 
ATOM   19639 C CG  . LEU K  3 70  ? 53.393  22.391  229.968 1.00 226.08 ?  73  LEU J CG  1 
ATOM   19640 C CD1 . LEU K  3 70  ? 53.255  23.517  228.958 1.00 225.52 ?  73  LEU J CD1 1 
ATOM   19641 C CD2 . LEU K  3 70  ? 53.438  22.941  231.385 1.00 213.00 ?  73  LEU J CD2 1 
ATOM   19642 N N   . THR K  3 71  ? 54.144  20.287  227.014 1.00 250.07 ?  74  THR J N   1 
ATOM   19643 C CA  . THR K  3 71  ? 55.390  19.654  226.584 1.00 259.69 ?  74  THR J CA  1 
ATOM   19644 C C   . THR K  3 71  ? 56.575  20.546  226.947 1.00 253.22 ?  74  THR J C   1 
ATOM   19645 O O   . THR K  3 71  ? 56.583  21.737  226.618 1.00 248.22 ?  74  THR J O   1 
ATOM   19646 C CB  . THR K  3 71  ? 55.376  19.385  225.078 1.00 272.97 ?  74  THR J CB  1 
ATOM   19647 O OG1 . THR K  3 71  ? 54.281  18.519  224.752 1.00 277.68 ?  74  THR J OG1 1 
ATOM   19648 C CG2 . THR K  3 71  ? 56.674  18.733  224.641 1.00 284.03 ?  74  THR J CG2 1 
ATOM   19649 N N   . ILE K  3 72  ? 57.575  19.966  227.618 1.00 280.33 ?  75  ILE J N   1 
ATOM   19650 C CA  . ILE K  3 72  ? 58.779  20.682  228.046 1.00 273.80 ?  75  ILE J CA  1 
ATOM   19651 C C   . ILE K  3 72  ? 60.005  19.999  227.448 1.00 282.43 ?  75  ILE J C   1 
ATOM   19652 O O   . ILE K  3 72  ? 60.460  18.967  227.956 1.00 282.83 ?  75  ILE J O   1 
ATOM   19653 C CB  . ILE K  3 72  ? 58.892  20.754  229.574 1.00 260.68 ?  75  ILE J CB  1 
ATOM   19654 C CG1 . ILE K  3 72  ? 57.624  21.352  230.187 1.00 251.68 ?  75  ILE J CG1 1 
ATOM   19655 C CG2 . ILE K  3 72  ? 60.122  21.554  229.989 1.00 253.84 ?  75  ILE J CG2 1 
ATOM   19656 C CD1 . ILE K  3 72  ? 57.646  21.389  231.703 1.00 239.33 ?  75  ILE J CD1 1 
ATOM   19657 N N   . THR K  3 73  ? 60.551  20.570  226.377 1.00 271.78 ?  76  THR J N   1 
ATOM   19658 C CA  . THR K  3 73  ? 61.747  20.028  225.748 1.00 279.58 ?  76  THR J CA  1 
ATOM   19659 C C   . THR K  3 73  ? 62.991  20.492  226.502 1.00 270.68 ?  76  THR J C   1 
ATOM   19660 O O   . THR K  3 73  ? 62.992  21.549  227.142 1.00 260.32 ?  76  THR J O   1 
ATOM   19661 C CB  . THR K  3 73  ? 61.834  20.461  224.285 1.00 289.56 ?  76  THR J CB  1 
ATOM   19662 O OG1 . THR K  3 73  ? 61.948  21.888  224.216 1.00 282.76 ?  76  THR J OG1 1 
ATOM   19663 C CG2 . THR K  3 73  ? 60.593  20.020  223.524 1.00 298.90 ?  76  THR J CG2 1 
ATOM   19664 N N   . SER K  3 74  ? 64.058  19.694  226.419 1.00 278.39 ?  77  SER J N   1 
ATOM   19665 C CA  . SER K  3 74  ? 65.323  19.975  227.105 1.00 270.80 ?  77  SER J CA  1 
ATOM   19666 C C   . SER K  3 74  ? 65.096  20.183  228.605 1.00 257.88 ?  77  SER J C   1 
ATOM   19667 O O   . SER K  3 74  ? 65.325  21.258  229.163 1.00 248.68 ?  77  SER J O   1 
ATOM   19668 C CB  . SER K  3 74  ? 66.035  21.175  226.470 1.00 269.93 ?  77  SER J CB  1 
ATOM   19669 O OG  . SER K  3 74  ? 66.287  20.953  225.090 1.00 281.54 ?  77  SER J OG  1 
ATOM   19670 N N   . VAL K  3 75  ? 64.636  19.114  229.255 1.00 269.91 ?  78  VAL J N   1 
ATOM   19671 C CA  . VAL K  3 75  ? 64.313  19.169  230.676 1.00 258.08 ?  78  VAL J CA  1 
ATOM   19672 C C   . VAL K  3 75  ? 65.573  19.402  231.495 1.00 249.32 ?  78  VAL J C   1 
ATOM   19673 O O   . VAL K  3 75  ? 66.581  18.702  231.337 1.00 252.34 ?  78  VAL J O   1 
ATOM   19674 C CB  . VAL K  3 75  ? 63.604  17.882  231.119 1.00 259.73 ?  78  VAL J CB  1 
ATOM   19675 C CG1 . VAL K  3 75  ? 63.204  17.988  232.578 1.00 247.18 ?  78  VAL J CG1 1 
ATOM   19676 C CG2 . VAL K  3 75  ? 62.385  17.633  230.258 1.00 268.61 ?  78  VAL J CG2 1 
ATOM   19677 N N   . GLU K  3 76  ? 65.529  20.406  232.360 1.00 268.25 ?  79  GLU J N   1 
ATOM   19678 C CA  . GLU K  3 76  ? 66.633  20.738  233.242 1.00 259.15 ?  79  GLU J CA  1 
ATOM   19679 C C   . GLU K  3 76  ? 66.158  20.658  234.685 1.00 248.22 ?  79  GLU J C   1 
ATOM   19680 O O   . GLU K  3 76  ? 64.959  20.585  234.966 1.00 246.85 ?  79  GLU J O   1 
ATOM   19681 C CB  . GLU K  3 76  ? 67.176  22.144  232.953 1.00 255.69 ?  79  GLU J CB  1 
ATOM   19682 C CG  . GLU K  3 76  ? 66.143  23.246  233.151 1.00 249.60 ?  79  GLU J CG  1 
ATOM   19683 C CD  . GLU K  3 76  ? 66.585  24.585  232.591 1.00 248.68 ?  79  GLU J CD  1 
ATOM   19684 O OE1 . GLU K  3 76  ? 67.781  24.731  232.261 1.00 250.46 ?  79  GLU J OE1 1 
ATOM   19685 O OE2 . GLU K  3 76  ? 65.734  25.493  232.484 1.00 246.06 -1 79  GLU J OE2 1 
ATOM   19686 N N   . ALA K  3 77  ? 67.123  20.666  235.606 1.00 257.46 ?  80  ALA J N   1 
ATOM   19687 C CA  . ALA K  3 77  ? 66.807  20.567  237.026 1.00 248.09 ?  80  ALA J CA  1 
ATOM   19688 C C   . ALA K  3 77  ? 65.976  21.752  237.491 1.00 244.12 ?  80  ALA J C   1 
ATOM   19689 O O   . ALA K  3 77  ? 65.235  21.637  238.473 1.00 240.81 ?  80  ALA J O   1 
ATOM   19690 C CB  . ALA K  3 77  ? 68.084  20.469  237.859 1.00 249.51 ?  80  ALA J CB  1 
ATOM   19691 N N   . GLY K  3 78  ? 66.084  22.884  236.793 1.00 248.67 ?  81  GLY J N   1 
ATOM   19692 C CA  . GLY K  3 78  ? 65.343  24.079  237.141 1.00 245.59 ?  81  GLY J CA  1 
ATOM   19693 C C   . GLY K  3 78  ? 63.859  23.986  236.864 1.00 242.87 ?  81  GLY J C   1 
ATOM   19694 O O   . GLY K  3 78  ? 63.104  24.808  237.383 1.00 239.89 ?  81  GLY J O   1 
ATOM   19695 N N   . ASP K  3 79  ? 63.434  23.049  236.011 1.00 248.66 ?  82  ASP J N   1 
ATOM   19696 C CA  . ASP K  3 79  ? 62.032  22.855  235.641 1.00 250.29 ?  82  ASP J CA  1 
ATOM   19697 C C   . ASP K  3 79  ? 61.244  22.039  236.664 1.00 245.87 ?  82  ASP J C   1 
ATOM   19698 O O   . ASP K  3 79  ? 60.037  21.845  236.480 1.00 248.03 ?  82  ASP J O   1 
ATOM   19699 C CB  . ASP K  3 79  ? 61.927  22.180  234.269 1.00 263.94 ?  82  ASP J CB  1 
ATOM   19700 C CG  . ASP K  3 79  ? 62.550  23.004  233.159 1.00 268.57 ?  82  ASP J CG  1 
ATOM   19701 O OD1 . ASP K  3 79  ? 62.624  24.243  233.304 1.00 260.73 ?  82  ASP J OD1 1 
ATOM   19702 O OD2 . ASP K  3 79  ? 62.955  22.412  232.136 1.00 280.12 -1 82  ASP J OD2 1 
ATOM   19703 N N   . GLU K  3 80  ? 61.890  21.567  237.727 1.00 255.49 ?  83  GLU J N   1 
ATOM   19704 C CA  . GLU K  3 80  ? 61.272  20.756  238.776 1.00 250.80 ?  83  GLU J CA  1 
ATOM   19705 C C   . GLU K  3 80  ? 60.323  21.603  239.621 1.00 247.25 ?  83  GLU J C   1 
ATOM   19706 O O   . GLU K  3 80  ? 60.750  22.294  240.550 1.00 246.19 ?  83  GLU J O   1 
ATOM   19707 C CB  . GLU K  3 80  ? 62.360  20.139  239.649 1.00 251.96 ?  83  GLU J CB  1 
ATOM   19708 C CG  . GLU K  3 80  ? 61.845  19.254  240.765 1.00 252.64 ?  83  GLU J CG  1 
ATOM   19709 C CD  . GLU K  3 80  ? 62.963  18.571  241.528 1.00 253.04 ?  83  GLU J CD  1 
ATOM   19710 O OE1 . GLU K  3 80  ? 63.999  18.253  240.907 1.00 254.17 ?  83  GLU J OE1 1 
ATOM   19711 O OE2 . GLU K  3 80  ? 62.799  18.333  242.745 1.00 252.43 -1 83  GLU J OE2 1 
ATOM   19712 N N   . ALA K  3 81  ? 59.025  21.550  239.310 1.00 238.16 ?  84  ALA J N   1 
ATOM   19713 C CA  . ALA K  3 81  ? 58.003  22.312  240.030 1.00 234.63 ?  84  ALA J CA  1 
ATOM   19714 C C   . ALA K  3 81  ? 56.630  21.717  239.750 1.00 233.76 ?  84  ALA J C   1 
ATOM   19715 O O   . ALA K  3 81  ? 56.501  20.683  239.085 1.00 242.73 ?  84  ALA J O   1 
ATOM   19716 C CB  . ALA K  3 81  ? 57.997  23.785  239.613 1.00 233.94 ?  84  ALA J CB  1 
ATOM   19717 N N   . ASP K  3 82  ? 55.599  22.383  240.268 1.00 230.93 ?  85  ASP J N   1 
ATOM   19718 C CA  . ASP K  3 82  ? 54.209  22.012  240.066 1.00 234.88 ?  85  ASP J CA  1 
ATOM   19719 C C   . ASP K  3 82  ? 53.631  22.832  238.917 1.00 232.34 ?  85  ASP J C   1 
ATOM   19720 O O   . ASP K  3 82  ? 53.988  23.996  238.723 1.00 224.29 ?  85  ASP J O   1 
ATOM   19721 C CB  . ASP K  3 82  ? 53.398  22.238  241.343 1.00 230.29 ?  85  ASP J CB  1 
ATOM   19722 C CG  . ASP K  3 82  ? 53.717  21.219  242.418 1.00 243.92 ?  85  ASP J CG  1 
ATOM   19723 O OD1 . ASP K  3 82  ? 54.105  20.088  242.060 1.00 253.43 ?  85  ASP J OD1 1 
ATOM   19724 O OD2 . ASP K  3 82  ? 53.574  21.543  243.617 1.00 244.81 -1 85  ASP J OD2 1 
ATOM   19725 N N   . TYR K  3 83  ? 52.730  22.214  238.156 1.00 244.29 ?  86  TYR J N   1 
ATOM   19726 C CA  . TYR K  3 83  ? 52.114  22.852  236.997 1.00 239.00 ?  86  TYR J CA  1 
ATOM   19727 C C   . TYR K  3 83  ? 50.601  22.690  237.043 1.00 238.48 ?  86  TYR J C   1 
ATOM   19728 O O   . TYR K  3 83  ? 50.098  21.564  237.102 1.00 243.41 ?  86  TYR J O   1 
ATOM   19729 C CB  . TYR K  3 83  ? 52.696  22.287  235.701 1.00 240.85 ?  86  TYR J CB  1 
ATOM   19730 C CG  . TYR K  3 83  ? 54.163  22.618  235.520 1.00 241.72 ?  86  TYR J CG  1 
ATOM   19731 C CD1 . TYR K  3 83  ? 55.158  21.822  236.079 1.00 246.88 ?  86  TYR J CD1 1 
ATOM   19732 C CD2 . TYR K  3 83  ? 54.550  23.727  234.781 1.00 235.44 ?  86  TYR J CD2 1 
ATOM   19733 C CE1 . TYR K  3 83  ? 56.497  22.129  235.907 1.00 244.07 ?  86  TYR J CE1 1 
ATOM   19734 C CE2 . TYR K  3 83  ? 55.880  24.037  234.600 1.00 234.34 ?  86  TYR J CE2 1 
ATOM   19735 C CZ  . TYR K  3 83  ? 56.851  23.238  235.165 1.00 239.72 ?  86  TYR J CZ  1 
ATOM   19736 O OH  . TYR K  3 83  ? 58.180  23.550  234.989 1.00 239.68 ?  86  TYR J OH  1 
ATOM   19737 N N   . TYR K  3 84  ? 49.888  23.814  237.013 1.00 230.77 ?  87  TYR J N   1 
ATOM   19738 C CA  . TYR K  3 84  ? 48.432  23.880  237.014 1.00 231.58 ?  87  TYR J CA  1 
ATOM   19739 C C   . TYR K  3 84  ? 47.918  24.377  235.666 1.00 228.16 ?  87  TYR J C   1 
ATOM   19740 O O   . TYR K  3 84  ? 48.649  24.992  234.885 1.00 221.13 ?  87  TYR J O   1 
ATOM   19741 C CB  . TYR K  3 84  ? 47.941  24.798  238.140 1.00 225.06 ?  87  TYR J CB  1 
ATOM   19742 C CG  . TYR K  3 84  ? 48.304  24.295  239.516 1.00 228.02 ?  87  TYR J CG  1 
ATOM   19743 C CD1 . TYR K  3 84  ? 48.110  22.967  239.852 1.00 238.07 ?  87  TYR J CD1 1 
ATOM   19744 C CD2 . TYR K  3 84  ? 48.880  25.132  240.463 1.00 224.51 ?  87  TYR J CD2 1 
ATOM   19745 C CE1 . TYR K  3 84  ? 48.447  22.486  241.100 1.00 241.49 ?  87  TYR J CE1 1 
ATOM   19746 C CE2 . TYR K  3 84  ? 49.224  24.658  241.719 1.00 227.63 ?  87  TYR J CE2 1 
ATOM   19747 C CZ  . TYR K  3 84  ? 49.004  23.333  242.029 1.00 234.87 ?  87  TYR J CZ  1 
ATOM   19748 O OH  . TYR K  3 84  ? 49.337  22.848  243.272 1.00 233.94 ?  87  TYR J OH  1 
ATOM   19749 N N   . CYS K  3 85  ? 46.646  24.096  235.390 1.00 220.04 ?  88  CYS J N   1 
ATOM   19750 C CA  . CYS K  3 85  ? 46.021  24.527  234.149 1.00 216.70 ?  88  CYS J CA  1 
ATOM   19751 C C   . CYS K  3 85  ? 44.661  25.156  234.431 1.00 212.62 ?  88  CYS J C   1 
ATOM   19752 O O   . CYS K  3 85  ? 43.951  24.750  235.356 1.00 215.09 ?  88  CYS J O   1 
ATOM   19753 C CB  . CYS K  3 85  ? 45.896  23.349  233.168 1.00 224.90 ?  88  CYS J CB  1 
ATOM   19754 S SG  . CYS K  3 85  ? 44.769  22.011  233.663 1.00 231.51 ?  88  CYS J SG  1 
ATOM   19755 N N   . HIS K  3 86  ? 44.312  26.159  233.617 1.00 207.58 ?  89  HIS J N   1 
ATOM   19756 C CA  . HIS K  3 86  ? 43.041  26.882  233.704 1.00 205.44 ?  89  HIS J CA  1 
ATOM   19757 C C   . HIS K  3 86  ? 42.233  26.602  232.441 1.00 209.32 ?  89  HIS J C   1 
ATOM   19758 O O   . HIS K  3 86  ? 42.466  27.208  231.391 1.00 203.59 ?  89  HIS J O   1 
ATOM   19759 C CB  . HIS K  3 86  ? 43.266  28.379  233.885 1.00 196.61 ?  89  HIS J CB  1 
ATOM   19760 C CG  . HIS K  3 86  ? 42.069  29.096  234.419 1.00 195.66 ?  89  HIS J CG  1 
ATOM   19761 N ND1 . HIS K  3 86  ? 42.010  30.467  234.548 1.00 188.36 ?  89  HIS J ND1 1 
ATOM   19762 C CD2 . HIS K  3 86  ? 40.872  28.626  234.842 1.00 201.51 ?  89  HIS J CD2 1 
ATOM   19763 C CE1 . HIS K  3 86  ? 40.831  30.809  235.037 1.00 189.73 ?  89  HIS J CE1 1 
ATOM   19764 N NE2 . HIS K  3 86  ? 40.122  29.710  235.224 1.00 197.66 ?  89  HIS J NE2 1 
ATOM   19765 N N   . ILE K  3 87  ? 41.290  25.670  232.552 1.00 206.46 ?  90  ILE J N   1 
ATOM   19766 C CA  . ILE K  3 87  ? 40.499  25.224  231.411 1.00 207.70 ?  90  ILE J CA  1 
ATOM   19767 C C   . ILE K  3 87  ? 39.460  26.277  231.043 1.00 200.42 ?  90  ILE J C   1 
ATOM   19768 O O   . ILE K  3 87  ? 38.624  26.660  231.870 1.00 199.82 ?  90  ILE J O   1 
ATOM   19769 C CB  . ILE K  3 87  ? 39.828  23.880  231.725 1.00 218.77 ?  90  ILE J CB  1 
ATOM   19770 C CG1 . ILE K  3 87  ? 40.880  22.823  232.080 1.00 221.29 ?  90  ILE J CG1 1 
ATOM   19771 C CG2 . ILE K  3 87  ? 38.893  23.473  230.611 1.00 219.00 ?  90  ILE J CG2 1 
ATOM   19772 C CD1 . ILE K  3 87  ? 41.881  22.557  230.976 1.00 213.36 ?  90  ILE J CD1 1 
ATOM   19773 N N   . TRP K  3 88  ? 39.508  26.748  229.797 1.00 213.94 ?  91  TRP J N   1 
ATOM   19774 C CA  . TRP K  3 88  ? 38.522  27.678  229.239 1.00 210.19 ?  91  TRP J CA  1 
ATOM   19775 C C   . TRP K  3 88  ? 37.783  27.029  228.076 1.00 213.72 ?  91  TRP J C   1 
ATOM   19776 O O   . TRP K  3 88  ? 38.173  27.195  226.919 1.00 210.01 ?  91  TRP J O   1 
ATOM   19777 C CB  . TRP K  3 88  ? 39.156  28.991  228.791 1.00 199.29 ?  91  TRP J CB  1 
ATOM   19778 C CG  . TRP K  3 88  ? 39.482  29.927  229.887 1.00 195.57 ?  91  TRP J CG  1 
ATOM   19779 C CD1 . TRP K  3 88  ? 40.643  30.017  230.592 1.00 194.83 ?  91  TRP J CD1 1 
ATOM   19780 C CD2 . TRP K  3 88  ? 38.621  30.952  230.389 1.00 194.32 ?  91  TRP J CD2 1 
ATOM   19781 N NE1 . TRP K  3 88  ? 40.549  31.031  231.520 1.00 193.19 ?  91  TRP J NE1 1 
ATOM   19782 C CE2 . TRP K  3 88  ? 39.317  31.620  231.412 1.00 192.19 ?  91  TRP J CE2 1 
ATOM   19783 C CE3 . TRP K  3 88  ? 37.322  31.365  230.074 1.00 194.66 ?  91  TRP J CE3 1 
ATOM   19784 C CZ2 . TRP K  3 88  ? 38.757  32.681  232.125 1.00 188.15 ?  91  TRP J CZ2 1 
ATOM   19785 C CZ3 . TRP K  3 88  ? 36.769  32.416  230.779 1.00 188.69 ?  91  TRP J CZ3 1 
ATOM   19786 C CH2 . TRP K  3 88  ? 37.484  33.062  231.795 1.00 185.45 ?  91  TRP J CH2 1 
ATOM   19787 N N   . ASP K  3 89  ? 36.690  26.340  228.372 1.00 195.65 ?  92  ASP J N   1 
ATOM   19788 C CA  . ASP K  3 89  ? 35.928  25.640  227.350 1.00 196.50 ?  92  ASP J CA  1 
ATOM   19789 C C   . ASP K  3 89  ? 34.710  26.489  226.994 1.00 196.32 ?  92  ASP J C   1 
ATOM   19790 O O   . ASP K  3 89  ? 34.118  27.129  227.868 1.00 195.45 ?  92  ASP J O   1 
ATOM   19791 C CB  . ASP K  3 89  ? 35.526  24.246  227.830 1.00 199.85 ?  92  ASP J CB  1 
ATOM   19792 C CG  . ASP K  3 89  ? 35.275  23.292  226.686 1.00 204.48 ?  92  ASP J CG  1 
ATOM   19793 O OD1 . ASP K  3 89  ? 34.906  23.761  225.589 1.00 201.22 ?  92  ASP J OD1 1 
ATOM   19794 O OD2 . ASP K  3 89  ? 35.489  22.077  226.873 1.00 211.36 -1 92  ASP J OD2 1 
ATOM   19795 N N   . SER K  3 90  ? 34.338  26.494  225.710 1.00 190.17 ?  93  SER J N   1 
ATOM   19796 C CA  . SER K  3 90  ? 33.202  27.291  225.248 1.00 190.09 ?  93  SER J CA  1 
ATOM   19797 C C   . SER K  3 90  ? 31.847  26.667  225.541 1.00 189.96 ?  93  SER J C   1 
ATOM   19798 O O   . SER K  3 90  ? 30.819  27.319  225.329 1.00 189.77 ?  93  SER J O   1 
ATOM   19799 C CB  . SER K  3 90  ? 33.296  27.508  223.741 1.00 191.08 ?  93  SER J CB  1 
ATOM   19800 O OG  . SER K  3 90  ? 33.228  26.262  223.064 1.00 191.99 ?  93  SER J OG  1 
ATOM   19801 N N   . ARG K  3 91  ? 31.818  25.437  226.025 1.00 184.89 ?  94  ARG J N   1 
ATOM   19802 C CA  . ARG K  3 91  ? 30.584  24.753  226.355 1.00 184.79 ?  94  ARG J CA  1 
ATOM   19803 C C   . ARG K  3 91  ? 30.417  24.593  227.850 1.00 183.82 ?  94  ARG J C   1 
ATOM   19804 O O   . ARG K  3 91  ? 29.323  24.245  228.309 1.00 183.55 ?  94  ARG J O   1 
ATOM   19805 C CB  . ARG K  3 91  ? 30.529  23.388  225.666 1.00 185.77 ?  94  ARG J CB  1 
ATOM   19806 C CG  . ARG K  3 91  ? 30.655  23.523  224.170 1.00 186.77 ?  94  ARG J CG  1 
ATOM   19807 C CD  . ARG K  3 91  ? 30.487  22.208  223.471 1.00 187.75 ?  94  ARG J CD  1 
ATOM   19808 N NE  . ARG K  3 91  ? 29.158  21.662  223.705 1.00 191.82 ?  94  ARG J NE  1 
ATOM   19809 C CZ  . ARG K  3 91  ? 28.691  20.572  223.112 1.00 198.55 ?  94  ARG J CZ  1 
ATOM   19810 N NH1 . ARG K  3 91  ? 29.450  19.914  222.248 1.00 200.35 1  94  ARG J NH1 1 
ATOM   19811 N NH2 . ARG K  3 91  ? 27.470  20.138  223.385 1.00 203.52 ?  94  ARG J NH2 1 
ATOM   19812 N N   . ARG K  3 92  ? 31.466  24.839  228.604 1.00 194.41 ?  95  ARG J N   1 
ATOM   19813 C CA  . ARG K  3 92  ? 31.436  24.675  230.024 1.00 196.34 ?  95  ARG J CA  1 
ATOM   19814 C C   . ARG K  3 92  ? 31.544  26.045  230.682 1.00 188.25 ?  95  ARG J C   1 
ATOM   19815 O O   . ARG K  3 92  ? 32.202  26.947  230.149 1.00 181.19 ?  95  ARG J O   1 
ATOM   19816 C CB  . ARG K  3 92  ? 32.655  23.836  230.429 1.00 199.02 ?  95  ARG J CB  1 
ATOM   19817 C CG  . ARG K  3 92  ? 32.724  22.452  229.779 1.00 204.14 ?  95  ARG J CG  1 
ATOM   19818 C CD  . ARG K  3 92  ? 31.683  21.429  230.157 1.00 212.98 ?  95  ARG J CD  1 
ATOM   19819 N NE  . ARG K  3 92  ? 32.338  20.283  230.777 1.00 218.62 ?  95  ARG J NE  1 
ATOM   19820 C CZ  . ARG K  3 92  ? 31.707  19.203  231.219 1.00 229.73 ?  95  ARG J CZ  1 
ATOM   19821 N NH1 . ARG K  3 92  ? 32.398  18.215  231.768 1.00 236.53 1  95  ARG J NH1 1 
ATOM   19822 N NH2 . ARG K  3 92  ? 30.389  19.108  231.104 1.00 232.89 ?  95  ARG J NH2 1 
ATOM   19823 N N   . PRO K  3 93  A 30.894  26.245  231.822 1.00 196.95 ?  95  PRO J N   1 
ATOM   19824 C CA  . PRO K  3 93  A 31.031  27.516  232.537 1.00 190.69 ?  95  PRO J CA  1 
ATOM   19825 C C   . PRO K  3 93  A 32.473  27.762  232.955 1.00 184.04 ?  95  PRO J C   1 
ATOM   19826 O O   . PRO K  3 93  A 33.337  26.882  232.921 1.00 186.36 ?  95  PRO J O   1 
ATOM   19827 C CB  . PRO K  3 93  A 30.085  27.364  233.731 1.00 196.35 ?  95  PRO J CB  1 
ATOM   19828 C CG  . PRO K  3 93  A 29.077  26.351  233.265 1.00 205.91 ?  95  PRO J CG  1 
ATOM   19829 C CD  . PRO K  3 93  A 29.845  25.394  232.405 1.00 206.52 ?  95  PRO J CD  1 
ATOM   19830 N N   . THR K  3 94  B 32.724  29.000  233.353 1.00 197.96 ?  95  THR J N   1 
ATOM   19831 C CA  . THR K  3 94  B 34.054  29.411  233.773 1.00 191.97 ?  95  THR J CA  1 
ATOM   19832 C C   . THR K  3 94  B 34.495  28.611  234.989 1.00 198.09 ?  95  THR J C   1 
ATOM   19833 O O   . THR K  3 94  B 33.841  28.637  236.034 1.00 203.65 ?  95  THR J O   1 
ATOM   19834 C CB  . THR K  3 94  B 34.060  30.903  234.094 1.00 184.26 ?  95  THR J CB  1 
ATOM   19835 O OG1 . THR K  3 94  B 32.870  31.234  234.820 1.00 186.26 ?  95  THR J OG1 1 
ATOM   19836 C CG2 . THR K  3 94  B 34.111  31.719  232.820 1.00 181.53 ?  95  THR J CG2 1 
ATOM   19837 N N   . ASN K  3 95  C 35.597  27.881  234.837 1.00 201.43 ?  95  ASN J N   1 
ATOM   19838 C CA  . ASN K  3 95  C 36.136  27.068  235.920 1.00 204.67 ?  95  ASN J CA  1 
ATOM   19839 C C   . ASN K  3 95  C 36.880  27.983  236.876 1.00 196.57 ?  95  ASN J C   1 
ATOM   19840 O O   . ASN K  3 95  C 37.918  28.554  236.528 1.00 188.42 ?  95  ASN J O   1 
ATOM   19841 C CB  . ASN K  3 95  C 37.071  25.978  235.401 1.00 206.25 ?  95  ASN J CB  1 
ATOM   19842 C CG  . ASN K  3 95  C 36.378  24.993  234.499 1.00 210.27 ?  95  ASN J CG  1 
ATOM   19843 O OD1 . ASN K  3 95  C 36.970  24.486  233.548 1.00 217.09 ?  95  ASN J OD1 1 
ATOM   19844 N ND2 . ASN K  3 95  C 35.124  24.692  234.806 1.00 206.92 ?  95  ASN J ND2 1 
ATOM   19845 N N   . TRP K  3 96  ? 36.349  28.109  238.085 1.00 220.13 ?  96  TRP J N   1 
ATOM   19846 C CA  . TRP K  3 96  ? 36.920  28.952  239.118 1.00 218.95 ?  96  TRP J CA  1 
ATOM   19847 C C   . TRP K  3 96  ? 37.907  28.176  239.969 1.00 222.22 ?  96  TRP J C   1 
ATOM   19848 O O   . TRP K  3 96  ? 38.361  28.680  241.002 1.00 221.76 ?  96  TRP J O   1 
ATOM   19849 C CB  . TRP K  3 96  ? 35.804  29.552  239.982 1.00 221.34 ?  96  TRP J CB  1 
ATOM   19850 C CG  . TRP K  3 96  ? 34.911  30.503  239.220 1.00 221.09 ?  96  TRP J CG  1 
ATOM   19851 C CD1 . TRP K  3 96  ? 33.768  30.184  238.548 1.00 226.22 ?  96  TRP J CD1 1 
ATOM   19852 C CD2 . TRP K  3 96  ? 35.070  31.927  239.083 1.00 213.83 ?  96  TRP J CD2 1 
ATOM   19853 N NE1 . TRP K  3 96  ? 33.222  31.308  237.977 1.00 224.02 ?  96  TRP J NE1 1 
ATOM   19854 C CE2 . TRP K  3 96  ? 33.996  32.392  238.297 1.00 214.80 ?  96  TRP J CE2 1 
ATOM   19855 C CE3 . TRP K  3 96  ? 36.017  32.849  239.541 1.00 206.27 ?  96  TRP J CE3 1 
ATOM   19856 C CZ2 . TRP K  3 96  ? 33.843  33.737  237.958 1.00 205.62 ?  96  TRP J CZ2 1 
ATOM   19857 C CZ3 . TRP K  3 96  ? 35.863  34.187  239.200 1.00 197.88 ?  96  TRP J CZ3 1 
ATOM   19858 C CH2 . TRP K  3 96  ? 34.784  34.616  238.419 1.00 197.50 ?  96  TRP J CH2 1 
ATOM   19859 N N   . VAL K  3 97  ? 38.230  26.952  239.552 1.00 212.29 ?  97  VAL J N   1 
ATOM   19860 C CA  . VAL K  3 97  ? 39.200  26.091  240.212 1.00 215.33 ?  97  VAL J CA  1 
ATOM   19861 C C   . VAL K  3 97  ? 40.102  25.499  239.130 1.00 211.62 ?  97  VAL J C   1 
ATOM   19862 O O   . VAL K  3 97  ? 39.612  24.963  238.129 1.00 212.94 ?  97  VAL J O   1 
ATOM   19863 C CB  . VAL K  3 97  ? 38.524  24.980  241.044 1.00 223.32 ?  97  VAL J CB  1 
ATOM   19864 C CG1 . VAL K  3 97  ? 37.480  25.574  241.970 1.00 222.00 ?  97  VAL J CG1 1 
ATOM   19865 C CG2 . VAL K  3 97  ? 37.859  23.924  240.152 1.00 227.23 ?  97  VAL J CG2 1 
ATOM   19866 N N   . PHE K  3 98  ? 41.410  25.703  239.273 1.00 220.89 ?  98  PHE J N   1 
ATOM   19867 C CA  . PHE K  3 98  ? 42.370  25.155  238.322 1.00 223.18 ?  98  PHE J CA  1 
ATOM   19868 C C   . PHE K  3 98  ? 42.314  23.630  238.338 1.00 231.15 ?  98  PHE J C   1 
ATOM   19869 O O   . PHE K  3 98  ? 41.906  23.019  239.328 1.00 235.56 ?  98  PHE J O   1 
ATOM   19870 C CB  . PHE K  3 98  ? 43.794  25.618  238.651 1.00 219.51 ?  98  PHE J CB  1 
ATOM   19871 C CG  . PHE K  3 98  ? 44.050  27.083  238.401 1.00 211.91 ?  98  PHE J CG  1 
ATOM   19872 C CD1 . PHE K  3 98  ? 43.145  27.864  237.701 1.00 210.71 ?  98  PHE J CD1 1 
ATOM   19873 C CD2 . PHE K  3 98  ? 45.231  27.666  238.836 1.00 205.91 ?  98  PHE J CD2 1 
ATOM   19874 C CE1 . PHE K  3 98  ? 43.401  29.206  237.468 1.00 203.22 ?  98  PHE J CE1 1 
ATOM   19875 C CE2 . PHE K  3 98  ? 45.494  29.002  238.602 1.00 199.22 ?  98  PHE J CE2 1 
ATOM   19876 C CZ  . PHE K  3 98  ? 44.579  29.772  237.918 1.00 197.40 ?  98  PHE J CZ  1 
ATOM   19877 N N   . GLY K  3 99  ? 42.685  23.002  237.221 1.00 215.79 ?  99  GLY J N   1 
ATOM   19878 C CA  . GLY K  3 99  ? 42.703  21.552  237.188 1.00 227.23 ?  99  GLY J CA  1 
ATOM   19879 C C   . GLY K  3 99  ? 43.784  21.001  238.105 1.00 232.63 ?  99  GLY J C   1 
ATOM   19880 O O   . GLY K  3 99  ? 44.709  21.708  238.507 1.00 227.34 ?  99  GLY J O   1 
ATOM   19881 N N   . GLU K  3 100 ? 43.670  19.722  238.465 1.00 226.39 ?  100 GLU J N   1 
ATOM   19882 C CA  . GLU K  3 100 ? 44.672  19.111  239.339 1.00 233.99 ?  100 GLU J CA  1 
ATOM   19883 C C   . GLU K  3 100 ? 46.074  19.074  238.725 1.00 230.70 ?  100 GLU J C   1 
ATOM   19884 O O   . GLU K  3 100 ? 46.276  18.543  237.628 1.00 229.62 ?  100 GLU J O   1 
ATOM   19885 C CB  . GLU K  3 100 ? 44.235  17.706  239.751 1.00 249.08 ?  100 GLU J CB  1 
ATOM   19886 C CG  . GLU K  3 100 ? 42.937  17.660  240.545 1.00 253.57 ?  100 GLU J CG  1 
ATOM   19887 C CD  . GLU K  3 100 ? 42.582  16.251  240.979 1.00 266.67 ?  100 GLU J CD  1 
ATOM   19888 O OE1 . GLU K  3 100 ? 43.405  15.341  240.751 1.00 275.02 ?  100 GLU J OE1 1 
ATOM   19889 O OE2 . GLU K  3 100 ? 41.498  16.057  241.571 1.00 265.01 -1 100 GLU J OE2 1 
ATOM   19890 N N   . GLY K  3 101 ? 47.028  19.656  239.454 1.00 236.61 ?  101 GLY J N   1 
ATOM   19891 C CA  . GLY K  3 101 ? 48.400  19.777  238.998 1.00 232.06 ?  101 GLY J CA  1 
ATOM   19892 C C   . GLY K  3 101 ? 49.143  18.457  238.886 1.00 242.29 ?  101 GLY J C   1 
ATOM   19893 O O   . GLY K  3 101 ? 48.714  17.417  239.389 1.00 254.98 ?  101 GLY J O   1 
ATOM   19894 N N   . THR K  3 102 ? 50.276  18.517  238.174 1.00 254.12 ?  102 THR J N   1 
ATOM   19895 C CA  . THR K  3 102 ? 51.183  17.388  237.964 1.00 261.62 ?  102 THR J CA  1 
ATOM   19896 C C   . THR K  3 102 ? 52.613  17.810  238.303 1.00 257.58 ?  102 THR J C   1 
ATOM   19897 O O   . THR K  3 102 ? 53.116  18.793  237.749 1.00 250.80 ?  102 THR J O   1 
ATOM   19898 C CB  . THR K  3 102 ? 51.097  16.889  236.522 1.00 257.15 ?  102 THR J CB  1 
ATOM   19899 O OG1 . THR K  3 102 ? 49.730  16.614  236.198 1.00 256.42 ?  102 THR J OG1 1 
ATOM   19900 C CG2 . THR K  3 102 ? 51.908  15.623  236.340 1.00 264.21 ?  102 THR J CG2 1 
ATOM   19901 N N   . THR K  3 103 ? 53.260  17.073  239.213 1.00 255.13 ?  103 THR J N   1 
ATOM   19902 C CA  . THR K  3 103 ? 54.612  17.363  239.693 1.00 250.58 ?  103 THR J CA  1 
ATOM   19903 C C   . THR K  3 103 ? 55.693  16.753  238.799 1.00 252.11 ?  103 THR J C   1 
ATOM   19904 O O   . THR K  3 103 ? 55.657  15.552  238.508 1.00 259.84 ?  103 THR J O   1 
ATOM   19905 C CB  . THR K  3 103 ? 54.784  16.852  241.122 1.00 255.28 ?  103 THR J CB  1 
ATOM   19906 O OG1 . THR K  3 103 ? 53.784  17.442  241.961 1.00 252.03 ?  103 THR J OG1 1 
ATOM   19907 C CG2 . THR K  3 103 ? 56.164  17.219  241.646 1.00 252.84 ?  103 THR J CG2 1 
ATOM   19908 N N   . LEU K  3 104 ? 56.650  17.584  238.370 1.00 247.87 ?  104 LEU J N   1 
ATOM   19909 C CA  . LEU K  3 104 ? 57.779  17.168  237.533 1.00 250.08 ?  104 LEU J CA  1 
ATOM   19910 C C   . LEU K  3 104 ? 59.048  16.845  238.327 1.00 259.20 ?  104 LEU J C   1 
ATOM   19911 O O   . LEU K  3 104 ? 59.592  17.715  239.020 1.00 256.31 ?  104 LEU J O   1 
ATOM   19912 C CB  . LEU K  3 104 ? 58.102  18.255  236.505 1.00 236.09 ?  104 LEU J CB  1 
ATOM   19913 C CG  . LEU K  3 104 ? 59.313  17.956  235.612 1.00 237.15 ?  104 LEU J CG  1 
ATOM   19914 C CD1 . LEU K  3 104 ? 59.140  16.658  234.851 1.00 245.78 ?  104 LEU J CD1 1 
ATOM   19915 C CD2 . LEU K  3 104 ? 59.594  19.100  234.657 1.00 229.32 ?  104 LEU J CD2 1 
ATOM   19916 N N   . ILE K  3 105 ? 59.516  15.601  238.217 1.00 247.21 ?  105 ILE J N   1 
ATOM   19917 C CA  . ILE K  3 105 ? 60.721  15.107  238.887 1.00 252.09 ?  105 ILE J CA  1 
ATOM   19918 C C   . ILE K  3 105 ? 61.844  15.007  237.864 1.00 251.86 ?  105 ILE J C   1 
ATOM   19919 O O   . ILE K  3 105 ? 61.750  14.237  236.901 1.00 254.19 ?  105 ILE J O   1 
ATOM   19920 C CB  . ILE K  3 105 ? 60.515  13.760  239.597 1.00 256.89 ?  105 ILE J CB  1 
ATOM   19921 C CG1 . ILE K  3 105 ? 59.479  13.874  240.709 1.00 251.53 ?  105 ILE J CG1 1 
ATOM   19922 C CG2 . ILE K  3 105 ? 61.840  13.217  240.100 1.00 260.24 ?  105 ILE J CG2 1 
ATOM   19923 C CD1 . ILE K  3 105 ? 58.101  13.809  240.205 1.00 251.84 ?  105 ILE J CD1 1 
ATOM   19924 N N   . VAL K  3 106 ? 62.902  15.783  238.058 1.00 261.03 ?  106 VAL J N   1 
ATOM   19925 C CA  . VAL K  3 106 ? 64.069  15.753  237.181 1.00 261.99 ?  106 VAL J CA  1 
ATOM   19926 C C   . VAL K  3 106 ? 64.991  14.671  237.734 1.00 273.14 ?  106 VAL J C   1 
ATOM   19927 O O   . VAL K  3 106 ? 65.592  14.842  238.795 1.00 274.30 ?  106 VAL J O   1 
ATOM   19928 C CB  . VAL K  3 106 ? 64.775  17.113  237.133 1.00 250.15 ?  106 VAL J CB  1 
ATOM   19929 C CG1 . VAL K  3 106 ? 65.948  17.070  236.194 1.00 253.47 ?  106 VAL J CG1 1 
ATOM   19930 C CG2 . VAL K  3 106 ? 63.814  18.174  236.709 1.00 233.44 ?  106 VAL J CG2 1 
ATOM   19931 N N   . LEU K  3 107 ? 65.091  13.550  237.020 1.00 266.58 ?  107 LEU J N   1 
ATOM   19932 C CA  . LEU K  3 107 ? 65.881  12.419  237.484 1.00 274.09 ?  107 LEU J CA  1 
ATOM   19933 C C   . LEU K  3 107 ? 67.373  12.755  237.500 1.00 275.57 ?  107 LEU J C   1 
ATOM   19934 O O   . LEU K  3 107 ? 67.807  13.820  237.056 1.00 270.72 ?  107 LEU J O   1 
ATOM   19935 C CB  . LEU K  3 107 ? 65.618  11.204  236.595 1.00 275.07 ?  107 LEU J CB  1 
ATOM   19936 C CG  . LEU K  3 107 ? 64.211  10.622  236.736 1.00 273.21 ?  107 LEU J CG  1 
ATOM   19937 C CD1 . LEU K  3 107 ? 63.995  9.464   235.775 1.00 271.01 ?  107 LEU J CD1 1 
ATOM   19938 C CD2 . LEU K  3 107 ? 63.966  10.187  238.172 1.00 276.17 ?  107 LEU J CD2 1 
ATOM   19939 N N   . SER K  3 108 ? 68.162  11.824  238.049 1.00 281.66 ?  108 SER J N   1 
ATOM   19940 C CA  . SER K  3 108 ? 69.617  11.965  238.137 1.00 284.27 ?  108 SER J CA  1 
ATOM   19941 C C   . SER K  3 108 ? 69.976  13.254  238.875 1.00 283.08 ?  108 SER J C   1 
ATOM   19942 O O   . SER K  3 108 ? 70.826  14.034  238.436 1.00 279.67 ?  108 SER J O   1 
ATOM   19943 C CB  . SER K  3 108 ? 70.253  11.928  236.743 1.00 280.90 ?  108 SER J CB  1 
ATOM   19944 O OG  . SER K  3 108 ? 71.662  12.060  236.806 1.00 285.56 ?  108 SER J OG  1 
ATOM   19945 N N   . GLN K  3 109 ? 69.300  13.484  240.003 1.00 282.88 ?  109 GLN J N   1 
ATOM   19946 C CA  . GLN K  3 109 ? 69.614  14.638  240.843 1.00 279.88 ?  109 GLN J CA  1 
ATOM   19947 C C   . GLN K  3 109 ? 71.055  14.630  241.403 1.00 283.80 ?  109 GLN J C   1 
ATOM   19948 O O   . GLN K  3 109 ? 71.732  15.651  241.312 1.00 280.12 ?  109 GLN J O   1 
ATOM   19949 C CB  . GLN K  3 109 ? 68.584  14.731  241.971 1.00 276.73 ?  109 GLN J CB  1 
ATOM   19950 C CG  . GLN K  3 109 ? 68.388  16.130  242.505 1.00 266.03 ?  109 GLN J CG  1 
ATOM   19951 C CD  . GLN K  3 109 ? 67.571  16.991  241.549 1.00 257.53 ?  109 GLN J CD  1 
ATOM   19952 O OE1 . GLN K  3 109 ? 66.789  16.478  240.746 1.00 255.54 ?  109 GLN J OE1 1 
ATOM   19953 N NE2 . GLN K  3 109 ? 67.747  18.304  241.635 1.00 250.39 ?  109 GLN J NE2 1 
ATOM   19954 N N   . PRO K  3 110 ? 71.541  13.501  241.979 1.00 271.51 ?  110 PRO J N   1 
ATOM   19955 C CA  . PRO K  3 110 ? 70.879  12.252  242.383 1.00 277.57 ?  110 PRO J CA  1 
ATOM   19956 C C   . PRO K  3 110 ? 70.837  12.037  243.924 1.00 276.45 ?  110 PRO J C   1 
ATOM   19957 O O   . PRO K  3 110 ? 69.790  11.693  244.468 1.00 274.99 ?  110 PRO J O   1 
ATOM   19958 C CB  . PRO K  3 110 ? 71.743  11.183  241.717 1.00 281.37 ?  110 PRO J CB  1 
ATOM   19959 C CG  . PRO K  3 110 ? 73.120  11.780  241.709 1.00 284.01 ?  110 PRO J CG  1 
ATOM   19960 C CD  . PRO K  3 110 ? 72.985  13.290  241.777 1.00 274.33 ?  110 PRO J CD  1 
ATOM   19961 N N   . LYS K  3 111 ? 71.980  12.240  244.591 1.00 275.33 ?  111 LYS J N   1 
ATOM   19962 C CA  . LYS K  3 111 ? 72.172  12.100  246.034 1.00 274.32 ?  111 LYS J CA  1 
ATOM   19963 C C   . LYS K  3 111 ? 72.761  13.377  246.631 1.00 266.52 ?  111 LYS J C   1 
ATOM   19964 O O   . LYS K  3 111 ? 73.378  14.180  245.928 1.00 267.56 ?  111 LYS J O   1 
ATOM   19965 C CB  . LYS K  3 111 ? 73.043  10.888  246.379 1.00 279.10 ?  111 LYS J CB  1 
ATOM   19966 C CG  . LYS K  3 111 ? 74.102  10.571  245.358 1.00 280.12 ?  111 LYS J CG  1 
ATOM   19967 C CD  . LYS K  3 111 ? 75.045  9.510   245.893 1.00 278.25 ?  111 LYS J CD  1 
ATOM   19968 C CE  . LYS K  3 111 ? 75.923  8.977   244.792 1.00 281.29 ?  111 LYS J CE  1 
ATOM   19969 N NZ  . LYS K  3 111 ? 75.132  8.849   243.539 1.00 276.64 1  111 LYS J NZ  1 
ATOM   19970 N N   . ALA K  3 112 ? 72.559  13.566  247.939 1.00 280.40 ?  112 ALA J N   1 
ATOM   19971 C CA  . ALA K  3 112 ? 73.058  14.752  248.638 1.00 275.18 ?  112 ALA J CA  1 
ATOM   19972 C C   . ALA K  3 112 ? 73.316  14.419  250.103 1.00 275.67 ?  112 ALA J C   1 
ATOM   19973 O O   . ALA K  3 112 ? 72.405  13.979  250.810 1.00 271.50 ?  112 ALA J O   1 
ATOM   19974 C CB  . ALA K  3 112 ? 72.078  15.919  248.521 1.00 263.33 ?  112 ALA J CB  1 
ATOM   19975 N N   . ALA K  3 113 ? 74.561  14.625  250.549 1.00 280.84 ?  113 ALA J N   1 
ATOM   19976 C CA  . ALA K  3 113 ? 74.941  14.347  251.937 1.00 278.31 ?  113 ALA J CA  1 
ATOM   19977 C C   . ALA K  3 113 ? 74.367  15.399  252.886 1.00 272.85 ?  113 ALA J C   1 
ATOM   19978 O O   . ALA K  3 113 ? 74.574  16.600  252.676 1.00 267.43 ?  113 ALA J O   1 
ATOM   19979 C CB  . ALA K  3 113 ? 76.463  14.298  252.065 1.00 287.37 ?  113 ALA J CB  1 
ATOM   19980 N N   . PRO K  3 114 ? 73.660  14.986  253.942 1.00 283.90 ?  114 PRO J N   1 
ATOM   19981 C CA  . PRO K  3 114 ? 73.044  15.946  254.877 1.00 277.42 ?  114 PRO J CA  1 
ATOM   19982 C C   . PRO K  3 114 ? 74.046  16.752  255.700 1.00 276.39 ?  114 PRO J C   1 
ATOM   19983 O O   . PRO K  3 114 ? 75.021  16.208  256.224 1.00 278.43 ?  114 PRO J O   1 
ATOM   19984 C CB  . PRO K  3 114 ? 72.203  15.047  255.791 1.00 275.38 ?  114 PRO J CB  1 
ATOM   19985 C CG  . PRO K  3 114 ? 72.890  13.706  255.726 1.00 281.29 ?  114 PRO J CG  1 
ATOM   19986 C CD  . PRO K  3 114 ? 73.406  13.587  254.326 1.00 286.01 ?  114 PRO J CD  1 
ATOM   19987 N N   . SER K  3 115 ? 73.798  18.066  255.801 1.00 272.13 ?  115 SER J N   1 
ATOM   19988 C CA  . SER K  3 115 ? 74.627  18.978  256.600 1.00 273.64 ?  115 SER J CA  1 
ATOM   19989 C C   . SER K  3 115 ? 73.895  19.252  257.919 1.00 277.76 ?  115 SER J C   1 
ATOM   19990 O O   . SER K  3 115 ? 73.068  20.161  258.013 1.00 277.81 ?  115 SER J O   1 
ATOM   19991 C CB  . SER K  3 115 ? 74.891  20.269  255.828 1.00 270.41 ?  115 SER J CB  1 
ATOM   19992 O OG  . SER K  3 115 ? 75.553  20.010  254.601 1.00 266.62 ?  115 SER J OG  1 
ATOM   19993 N N   . VAL K  3 116 ? 74.204  18.442  258.955 1.00 276.67 ?  116 VAL J N   1 
ATOM   19994 C CA  . VAL K  3 116 ? 73.567  18.533  260.268 1.00 279.33 ?  116 VAL J CA  1 
ATOM   19995 C C   . VAL K  3 116 ? 74.310  19.514  261.175 1.00 277.59 ?  116 VAL J C   1 
ATOM   19996 O O   . VAL K  3 116 ? 75.502  19.772  260.991 1.00 276.18 ?  116 VAL J O   1 
ATOM   19997 C CB  . VAL K  3 116 ? 73.453  17.126  260.896 1.00 284.59 ?  116 VAL J CB  1 
ATOM   19998 C CG1 . VAL K  3 116 ? 72.512  16.265  260.069 1.00 285.20 ?  116 VAL J CG1 1 
ATOM   19999 C CG2 . VAL K  3 116 ? 74.807  16.459  260.945 1.00 283.48 ?  116 VAL J CG2 1 
ATOM   20000 N N   . THR K  3 117 ? 73.573  20.174  262.072 1.00 286.11 ?  117 THR J N   1 
ATOM   20001 C CA  . THR K  3 117 ? 74.163  21.104  263.039 1.00 285.95 ?  117 THR J CA  1 
ATOM   20002 C C   . THR K  3 117 ? 73.349  21.066  264.328 1.00 287.76 ?  117 THR J C   1 
ATOM   20003 O O   . THR K  3 117 ? 72.140  21.315  264.288 1.00 284.13 ?  117 THR J O   1 
ATOM   20004 C CB  . THR K  3 117 ? 74.262  22.530  262.495 1.00 276.05 ?  117 THR J CB  1 
ATOM   20005 O OG1 . THR K  3 117 ? 74.940  22.510  261.232 1.00 274.00 ?  117 THR J OG1 1 
ATOM   20006 C CG2 . THR K  3 117 ? 75.048  23.406  263.473 1.00 275.15 ?  117 THR J CG2 1 
ATOM   20007 N N   . LEU K  3 118 ? 73.995  20.780  265.462 1.00 283.03 ?  118 LEU J N   1 
ATOM   20008 C CA  . LEU K  3 118 ? 73.331  20.647  266.761 1.00 292.12 ?  118 LEU J CA  1 
ATOM   20009 C C   . LEU K  3 118 ? 73.701  21.806  267.676 1.00 296.49 ?  118 LEU J C   1 
ATOM   20010 O O   . LEU K  3 118 ? 74.880  22.004  267.985 1.00 299.57 ?  118 LEU J O   1 
ATOM   20011 C CB  . LEU K  3 118 ? 73.665  19.333  267.475 1.00 297.61 ?  118 LEU J CB  1 
ATOM   20012 C CG  . LEU K  3 118 ? 72.915  19.166  268.820 1.00 297.39 ?  118 LEU J CG  1 
ATOM   20013 C CD1 . LEU K  3 118 ? 71.409  19.217  268.666 1.00 294.39 ?  118 LEU J CD1 1 
ATOM   20014 C CD2 . LEU K  3 118 ? 73.280  17.879  269.533 1.00 302.90 ?  118 LEU J CD2 1 
ATOM   20015 N N   . PHE K  3 119 ? 72.689  22.556  268.123 1.00 294.12 ?  119 PHE J N   1 
ATOM   20016 C CA  . PHE K  3 119 ? 72.905  23.681  269.021 1.00 293.72 ?  119 PHE J CA  1 
ATOM   20017 C C   . PHE K  3 119 ? 72.411  23.325  270.423 1.00 297.54 ?  119 PHE J C   1 
ATOM   20018 O O   . PHE K  3 119 ? 71.311  22.784  270.586 1.00 296.26 ?  119 PHE J O   1 
ATOM   20019 C CB  . PHE K  3 119 ? 72.232  24.979  268.546 1.00 286.11 ?  119 PHE J CB  1 
ATOM   20020 C CG  . PHE K  3 119 ? 73.000  25.702  267.463 1.00 282.17 ?  119 PHE J CG  1 
ATOM   20021 C CD1 . PHE K  3 119 ? 74.096  26.494  267.782 1.00 283.75 ?  119 PHE J CD1 1 
ATOM   20022 C CD2 . PHE K  3 119 ? 72.627  25.595  266.136 1.00 272.33 ?  119 PHE J CD2 1 
ATOM   20023 C CE1 . PHE K  3 119 ? 74.807  27.160  266.791 1.00 277.31 ?  119 PHE J CE1 1 
ATOM   20024 C CE2 . PHE K  3 119 ? 73.333  26.258  265.144 1.00 262.11 ?  119 PHE J CE2 1 
ATOM   20025 C CZ  . PHE K  3 119 ? 74.423  27.041  265.473 1.00 266.02 ?  119 PHE J CZ  1 
ATOM   20026 N N   . PRO K  3 120 ? 73.203  23.652  271.438 1.00 280.10 ?  120 PRO J N   1 
ATOM   20027 C CA  . PRO K  3 120 ? 72.819  23.414  272.837 1.00 288.88 ?  120 PRO J CA  1 
ATOM   20028 C C   . PRO K  3 120 ? 71.764  24.399  273.298 1.00 291.75 ?  120 PRO J C   1 
ATOM   20029 O O   . PRO K  3 120 ? 71.532  25.422  272.634 1.00 287.05 ?  120 PRO J O   1 
ATOM   20030 C CB  . PRO K  3 120 ? 74.137  23.617  273.598 1.00 292.60 ?  120 PRO J CB  1 
ATOM   20031 C CG  . PRO K  3 120 ? 74.882  24.592  272.774 1.00 286.78 ?  120 PRO J CG  1 
ATOM   20032 C CD  . PRO K  3 120 ? 74.536  24.276  271.338 1.00 278.64 ?  120 PRO J CD  1 
ATOM   20033 N N   . PRO K  3 121 ? 71.080  24.118  274.412 1.00 285.66 ?  121 PRO J N   1 
ATOM   20034 C CA  . PRO K  3 121 ? 70.058  25.053  274.873 1.00 288.83 ?  121 PRO J CA  1 
ATOM   20035 C C   . PRO K  3 121 ? 70.742  26.368  275.172 1.00 289.67 ?  121 PRO J C   1 
ATOM   20036 O O   . PRO K  3 121 ? 71.870  26.416  275.667 1.00 292.21 ?  121 PRO J O   1 
ATOM   20037 C CB  . PRO K  3 121 ? 69.506  24.397  276.143 1.00 298.16 ?  121 PRO J CB  1 
ATOM   20038 C CG  . PRO K  3 121 ? 70.587  23.514  276.602 1.00 300.91 ?  121 PRO J CG  1 
ATOM   20039 C CD  . PRO K  3 121 ? 71.247  23.004  275.361 1.00 292.45 ?  121 PRO J CD  1 
ATOM   20040 N N   . SER K  3 122 ? 70.032  27.437  274.863 1.00 282.63 ?  122 SER J N   1 
ATOM   20041 C CA  . SER K  3 122 ? 70.569  28.767  275.008 1.00 282.18 ?  122 SER J CA  1 
ATOM   20042 C C   . SER K  3 122 ? 70.748  29.159  276.455 1.00 286.61 ?  122 SER J C   1 
ATOM   20043 O O   . SER K  3 122 ? 70.142  28.606  277.377 1.00 290.15 ?  122 SER J O   1 
ATOM   20044 C CB  . SER K  3 122 ? 69.627  29.784  274.377 1.00 280.01 ?  122 SER J CB  1 
ATOM   20045 O OG  . SER K  3 122 ? 68.369  29.772  275.024 1.00 282.65 ?  122 SER J OG  1 
ATOM   20046 N N   . SER K  3 123 ? 71.632  30.127  276.637 1.00 277.68 ?  123 SER J N   1 
ATOM   20047 C CA  . SER K  3 123 ? 71.879  30.618  277.970 1.00 288.04 ?  123 SER J CA  1 
ATOM   20048 C C   . SER K  3 123 ? 70.648  31.377  278.436 1.00 292.58 ?  123 SER J C   1 
ATOM   20049 O O   . SER K  3 123 ? 70.411  31.489  279.637 1.00 303.60 ?  123 SER J O   1 
ATOM   20050 C CB  . SER K  3 123 ? 73.136  31.497  277.960 1.00 289.38 ?  123 SER J CB  1 
ATOM   20051 O OG  . SER K  3 123 ? 73.433  32.045  279.229 1.00 299.86 ?  123 SER J OG  1 
ATOM   20052 N N   . GLU K  3 124 ? 69.873  31.915  277.480 1.00 281.96 ?  124 GLU J N   1 
ATOM   20053 C CA  . GLU K  3 124 ? 68.664  32.692  277.744 1.00 284.47 ?  124 GLU J CA  1 
ATOM   20054 C C   . GLU K  3 124 ? 67.418  31.891  278.142 1.00 287.19 ?  124 GLU J C   1 
ATOM   20055 O O   . GLU K  3 124 ? 66.632  32.351  278.981 1.00 295.23 ?  124 GLU J O   1 
ATOM   20056 C CB  . GLU K  3 124 ? 68.315  33.398  276.436 1.00 278.46 ?  124 GLU J CB  1 
ATOM   20057 C CG  . GLU K  3 124 ? 67.191  34.376  276.470 1.00 278.57 ?  124 GLU J CG  1 
ATOM   20058 C CD  . GLU K  3 124 ? 67.666  35.786  276.542 1.00 281.93 ?  124 GLU J CD  1 
ATOM   20059 O OE1 . GLU K  3 124 ? 68.226  36.274  275.533 1.00 275.68 ?  124 GLU J OE1 1 
ATOM   20060 O OE2 . GLU K  3 124 ? 67.503  36.393  277.613 1.00 291.73 -1 124 GLU J OE2 1 
ATOM   20061 N N   . GLU K  3 125 ? 67.210  30.699  277.572 1.00 300.30 ?  125 GLU J N   1 
ATOM   20062 C CA  . GLU K  3 125 ? 66.023  29.900  277.910 1.00 302.54 ?  125 GLU J CA  1 
ATOM   20063 C C   . GLU K  3 125 ? 66.154  29.145  279.218 1.00 311.25 ?  125 GLU J C   1 
ATOM   20064 O O   . GLU K  3 125 ? 65.161  28.943  279.923 1.00 317.54 ?  125 GLU J O   1 
ATOM   20065 C CB  . GLU K  3 125 ? 65.575  28.956  276.806 1.00 292.99 ?  125 GLU J CB  1 
ATOM   20066 C CG  . GLU K  3 125 ? 66.358  27.732  276.540 1.00 288.26 ?  125 GLU J CG  1 
ATOM   20067 C CD  . GLU K  3 125 ? 65.681  26.960  275.436 1.00 279.95 ?  125 GLU J CD  1 
ATOM   20068 O OE1 . GLU K  3 125 ? 64.438  26.856  275.484 1.00 282.62 ?  125 GLU J OE1 1 
ATOM   20069 O OE2 . GLU K  3 125 ? 66.375  26.469  274.524 1.00 276.70 -1 125 GLU J OE2 1 
ATOM   20070 N N   . LEU K  3 126 ? 67.363  28.743  279.569 1.00 295.21 ?  126 LEU J N   1 
ATOM   20071 C CA  . LEU K  3 126 ? 67.555  27.991  280.794 1.00 299.54 ?  126 LEU J CA  1 
ATOM   20072 C C   . LEU K  3 126 ? 67.101  28.835  281.974 1.00 303.63 ?  126 LEU J C   1 
ATOM   20073 O O   . LEU K  3 126 ? 66.705  28.313  283.028 1.00 312.36 ?  126 LEU J O   1 
ATOM   20074 C CB  . LEU K  3 126 ? 69.037  27.655  280.915 1.00 299.43 ?  126 LEU J CB  1 
ATOM   20075 C CG  . LEU K  3 126 ? 69.659  26.636  279.951 1.00 296.51 ?  126 LEU J CG  1 
ATOM   20076 C CD1 . LEU K  3 126 ? 71.160  26.438  280.207 1.00 296.79 ?  126 LEU J CD1 1 
ATOM   20077 C CD2 . LEU K  3 126 ? 68.946  25.312  280.017 1.00 297.72 ?  126 LEU J CD2 1 
ATOM   20078 N N   . GLN K  3 127 ? 67.196  30.145  281.803 1.00 296.46 ?  127 GLN J N   1 
ATOM   20079 C CA  . GLN K  3 127 ? 66.783  31.167  282.742 1.00 306.05 ?  127 GLN J CA  1 
ATOM   20080 C C   . GLN K  3 127 ? 65.267  31.321  282.822 1.00 308.11 ?  127 GLN J C   1 
ATOM   20081 O O   . GLN K  3 127 ? 64.759  31.900  283.786 1.00 317.73 ?  127 GLN J O   1 
ATOM   20082 C CB  . GLN K  3 127 ? 67.466  32.384  282.170 1.00 301.93 ?  127 GLN J CB  1 
ATOM   20083 C CG  . GLN K  3 127 ? 68.933  32.084  282.258 1.00 301.22 ?  127 GLN J CG  1 
ATOM   20084 C CD  . GLN K  3 127 ? 69.848  33.158  281.745 1.00 298.58 ?  127 GLN J CD  1 
ATOM   20085 O OE1 . GLN K  3 127 ? 69.417  34.155  281.190 1.00 296.04 ?  127 GLN J OE1 1 
ATOM   20086 N NE2 . GLN K  3 127 ? 71.141  32.955  281.941 1.00 297.51 ?  127 GLN J NE2 1 
ATOM   20087 N N   . ALA K  3 128 ? 64.544  30.810  281.824 1.00 296.40 ?  128 ALA J N   1 
ATOM   20088 C CA  . ALA K  3 128 ? 63.091  30.814  281.798 1.00 297.01 ?  128 ALA J CA  1 
ATOM   20089 C C   . ALA K  3 128 ? 62.553  29.468  282.246 1.00 299.46 ?  128 ALA J C   1 
ATOM   20090 O O   . ALA K  3 128 ? 61.386  29.148  281.990 1.00 299.37 ?  128 ALA J O   1 
ATOM   20091 C CB  . ALA K  3 128 ? 62.574  31.160  280.400 1.00 292.45 ?  128 ALA J CB  1 
ATOM   20092 N N   . ASN K  3 129 ? 63.390  28.692  282.941 1.00 301.34 ?  129 ASN J N   1 
ATOM   20093 C CA  . ASN K  3 129 ? 63.053  27.357  283.432 1.00 303.83 ?  129 ASN J CA  1 
ATOM   20094 C C   . ASN K  3 129 ? 62.625  26.476  282.257 1.00 300.61 ?  129 ASN J C   1 
ATOM   20095 O O   . ASN K  3 129 ? 61.711  25.655  282.360 1.00 301.87 ?  129 ASN J O   1 
ATOM   20096 C CB  . ASN K  3 129 ? 61.980  27.416  284.524 1.00 307.99 ?  129 ASN J CB  1 
ATOM   20097 C CG  . ASN K  3 129 ? 61.942  26.160  285.371 1.00 311.49 ?  129 ASN J CG  1 
ATOM   20098 O OD1 . ASN K  3 129 ? 62.921  25.417  285.436 1.00 311.59 ?  129 ASN J OD1 1 
ATOM   20099 N ND2 . ASN K  3 129 ? 60.811  25.914  286.025 1.00 314.41 ?  129 ASN J ND2 1 
ATOM   20100 N N   . LYS K  3 130 ? 63.312  26.671  281.124 1.00 322.14 ?  130 LYS J N   1 
ATOM   20101 C CA  . LYS K  3 130 ? 63.087  25.951  279.879 1.00 313.71 ?  130 LYS J CA  1 
ATOM   20102 C C   . LYS K  3 130 ? 64.426  25.602  279.236 1.00 306.71 ?  130 LYS J C   1 
ATOM   20103 O O   . LYS K  3 130 ? 65.416  26.314  279.409 1.00 305.79 ?  130 LYS J O   1 
ATOM   20104 C CB  . LYS K  3 130 ? 62.282  26.807  278.892 1.00 307.63 ?  130 LYS J CB  1 
ATOM   20105 C CG  . LYS K  3 130 ? 60.877  27.178  279.333 1.00 312.68 ?  130 LYS J CG  1 
ATOM   20106 C CD  . LYS K  3 130 ? 60.263  28.121  278.313 1.00 306.17 ?  130 LYS J CD  1 
ATOM   20107 C CE  . LYS K  3 130 ? 58.887  28.593  278.723 1.00 310.52 ?  130 LYS J CE  1 
ATOM   20108 N NZ  . LYS K  3 130 ? 58.713  30.019  278.347 1.00 307.78 1  130 LYS J NZ  1 
ATOM   20109 N N   . ALA K  3 131 ? 64.451  24.503  278.483 1.00 324.83 ?  131 ALA J N   1 
ATOM   20110 C CA  . ALA K  3 131 ? 65.655  24.080  277.775 1.00 313.09 ?  131 ALA J CA  1 
ATOM   20111 C C   . ALA K  3 131 ? 65.262  23.420  276.459 1.00 304.92 ?  131 ALA J C   1 
ATOM   20112 O O   . ALA K  3 131 ? 64.249  22.719  276.404 1.00 306.82 ?  131 ALA J O   1 
ATOM   20113 C CB  . ALA K  3 131 ? 66.507  23.126  278.616 1.00 318.59 ?  131 ALA J CB  1 
ATOM   20114 N N   . THR K  3 132 ? 66.051  23.635  275.403 1.00 308.65 ?  132 THR J N   1 
ATOM   20115 C CA  . THR K  3 132 ? 65.708  23.045  274.109 1.00 301.26 ?  132 THR J CA  1 
ATOM   20116 C C   . THR K  3 132 ? 66.940  22.831  273.236 1.00 294.79 ?  132 THR J C   1 
ATOM   20117 O O   . THR K  3 132 ? 67.673  23.783  272.951 1.00 291.68 ?  132 THR J O   1 
ATOM   20118 C CB  . THR K  3 132 ? 64.692  23.922  273.370 1.00 298.20 ?  132 THR J CB  1 
ATOM   20119 O OG1 . THR K  3 132 ? 63.477  24.011  274.130 1.00 304.43 ?  132 THR J OG1 1 
ATOM   20120 C CG2 . THR K  3 132 ? 64.391  23.339  272.001 1.00 291.74 ?  132 THR J CG2 1 
ATOM   20121 N N   . LEU K  3 133 ? 67.152  21.580  272.812 1.00 303.48 ?  133 LEU J N   1 
ATOM   20122 C CA  . LEU K  3 133 ? 68.220  21.189  271.890 1.00 297.13 ?  133 LEU J CA  1 
ATOM   20123 C C   . LEU K  3 133 ? 67.698  21.270  270.455 1.00 290.01 ?  133 LEU J C   1 
ATOM   20124 O O   . LEU K  3 133 ? 66.581  20.830  270.178 1.00 290.55 ?  133 LEU J O   1 
ATOM   20125 C CB  . LEU K  3 133 ? 68.694  19.768  272.207 1.00 300.61 ?  133 LEU J CB  1 
ATOM   20126 C CG  . LEU K  3 133 ? 69.451  19.584  273.519 1.00 308.12 ?  133 LEU J CG  1 
ATOM   20127 C CD1 . LEU K  3 133 ? 69.746  18.127  273.795 1.00 312.04 ?  133 LEU J CD1 1 
ATOM   20128 C CD2 . LEU K  3 133 ? 70.746  20.332  273.384 1.00 304.69 ?  133 LEU J CD2 1 
ATOM   20129 N N   . VAL K  3 134 ? 68.498  21.841  269.545 1.00 301.65 ?  134 VAL J N   1 
ATOM   20130 C CA  . VAL K  3 134 ? 68.101  22.040  268.146 1.00 295.34 ?  134 VAL J CA  1 
ATOM   20131 C C   . VAL K  3 134 ? 69.029  21.292  267.185 1.00 290.49 ?  134 VAL J C   1 
ATOM   20132 O O   . VAL K  3 134 ? 70.234  21.558  267.174 1.00 289.11 ?  134 VAL J O   1 
ATOM   20133 C CB  . VAL K  3 134 ? 68.130  23.542  267.811 1.00 292.64 ?  134 VAL J CB  1 
ATOM   20134 C CG1 . VAL K  3 134 ? 67.476  23.830  266.487 1.00 287.13 ?  134 VAL J CG1 1 
ATOM   20135 C CG2 . VAL K  3 134 ? 67.549  24.353  268.926 1.00 297.85 ?  134 VAL J CG2 1 
ATOM   20136 N N   . CYS K  3 135 ? 68.465  20.492  266.266 1.00 301.42 ?  135 CYS J N   1 
ATOM   20137 C CA  . CYS K  3 135 ? 69.266  19.732  265.288 1.00 297.05 ?  135 CYS J CA  1 
ATOM   20138 C C   . CYS K  3 135 ? 68.836  20.123  263.873 1.00 291.11 ?  135 CYS J C   1 
ATOM   20139 O O   . CYS K  3 135 ? 67.783  19.678  263.405 1.00 290.64 ?  135 CYS J O   1 
ATOM   20140 C CB  . CYS K  3 135 ? 69.070  18.222  265.388 1.00 299.35 ?  135 CYS J CB  1 
ATOM   20141 S SG  . CYS K  3 135 ? 70.281  17.145  264.511 1.00 295.48 ?  135 CYS J SG  1 
ATOM   20142 N N   . LEU K  3 136 ? 69.613  20.975  263.210 1.00 295.37 ?  136 LEU J N   1 
ATOM   20143 C CA  . LEU K  3 136 ? 69.306  21.447  261.859 1.00 289.83 ?  136 LEU J CA  1 
ATOM   20144 C C   . LEU K  3 136 ? 69.920  20.534  260.797 1.00 286.09 ?  136 LEU J C   1 
ATOM   20145 O O   . LEU K  3 136 ? 71.123  20.261  260.837 1.00 285.68 ?  136 LEU J O   1 
ATOM   20146 C CB  . LEU K  3 136 ? 69.785  22.883  261.654 1.00 287.46 ?  136 LEU J CB  1 
ATOM   20147 C CG  . LEU K  3 136 ? 69.144  23.999  262.480 1.00 290.15 ?  136 LEU J CG  1 
ATOM   20148 C CD1 . LEU K  3 136 ? 67.650  23.760  262.645 1.00 292.07 ?  136 LEU J CD1 1 
ATOM   20149 C CD2 . LEU K  3 136 ? 69.824  24.156  263.833 1.00 295.09 ?  136 LEU J CD2 1 
ATOM   20150 N N   . ILE K  3 137 ? 69.100  20.077  259.848 1.00 289.81 ?  137 ILE J N   1 
ATOM   20151 C CA  . ILE K  3 137 ? 69.520  19.187  258.758 1.00 286.32 ?  137 ILE J CA  1 
ATOM   20152 C C   . ILE K  3 137 ? 69.174  19.836  257.418 1.00 281.24 ?  137 ILE J C   1 
ATOM   20153 O O   . ILE K  3 137 ? 68.006  20.159  257.166 1.00 280.92 ?  137 ILE J O   1 
ATOM   20154 C CB  . ILE K  3 137 ? 68.889  17.789  258.858 1.00 288.53 ?  137 ILE J CB  1 
ATOM   20155 C CG1 . ILE K  3 137 ? 68.907  17.271  260.302 1.00 294.34 ?  137 ILE J CG1 1 
ATOM   20156 C CG2 . ILE K  3 137 ? 69.595  16.824  257.900 1.00 285.65 ?  137 ILE J CG2 1 
ATOM   20157 C CD1 . ILE K  3 137 ? 67.589  17.448  261.054 1.00 298.48 ?  137 ILE J CD1 1 
ATOM   20158 N N   . SER K  3 138 ? 70.186  20.029  256.564 1.00 285.47 ?  138 SER J N   1 
ATOM   20159 C CA  . SER K  3 138 ? 70.000  20.669  255.265 1.00 280.63 ?  138 SER J CA  1 
ATOM   20160 C C   . SER K  3 138 ? 70.893  20.031  254.202 1.00 277.75 ?  138 SER J C   1 
ATOM   20161 O O   . SER K  3 138 ? 71.758  19.198  254.492 1.00 279.23 ?  138 SER J O   1 
ATOM   20162 C CB  . SER K  3 138 ? 70.301  22.172  255.346 1.00 279.26 ?  138 SER J CB  1 
ATOM   20163 O OG  . SER K  3 138 ? 71.643  22.395  255.750 1.00 280.31 ?  138 SER J OG  1 
ATOM   20164 N N   . ASP K  3 139 ? 70.655  20.449  252.952 1.00 278.56 ?  139 ASP J N   1 
ATOM   20165 C CA  . ASP K  3 139 ? 71.405  20.022  251.763 1.00 275.25 ?  139 ASP J CA  1 
ATOM   20166 C C   . ASP K  3 139 ? 71.395  18.502  251.563 1.00 275.72 ?  139 ASP J C   1 
ATOM   20167 O O   . ASP K  3 139 ? 72.425  17.887  251.283 1.00 274.93 ?  139 ASP J O   1 
ATOM   20168 C CB  . ASP K  3 139 ? 72.848  20.536  251.839 1.00 274.96 ?  139 ASP J CB  1 
ATOM   20169 C CG  . ASP K  3 139 ? 72.944  22.049  251.742 1.00 273.65 ?  139 ASP J CG  1 
ATOM   20170 O OD1 . ASP K  3 139 ? 72.202  22.654  250.940 1.00 270.97 ?  139 ASP J OD1 1 
ATOM   20171 O OD2 . ASP K  3 139 ? 73.769  22.636  252.476 1.00 275.34 -1 139 ASP J OD2 1 
ATOM   20172 N N   . PHE K  3 140 ? 70.217  17.888  251.695 1.00 271.23 ?  140 PHE J N   1 
ATOM   20173 C CA  . PHE K  3 140 ? 70.084  16.446  251.498 1.00 271.59 ?  140 PHE J CA  1 
ATOM   20174 C C   . PHE K  3 140 ? 68.974  16.092  250.514 1.00 269.57 ?  140 PHE J C   1 
ATOM   20175 O O   . PHE K  3 140 ? 67.907  16.715  250.518 1.00 269.88 ?  140 PHE J O   1 
ATOM   20176 C CB  . PHE K  3 140 ? 69.836  15.705  252.816 1.00 276.20 ?  140 PHE J CB  1 
ATOM   20177 C CG  . PHE K  3 140 ? 68.565  16.096  253.507 1.00 279.16 ?  140 PHE J CG  1 
ATOM   20178 C CD1 . PHE K  3 140 ? 68.537  17.173  254.374 1.00 281.09 ?  140 PHE J CD1 1 
ATOM   20179 C CD2 . PHE K  3 140 ? 67.397  15.377  253.298 1.00 280.11 ?  140 PHE J CD2 1 
ATOM   20180 C CE1 . PHE K  3 140 ? 67.368  17.531  255.017 1.00 283.88 ?  140 PHE J CE1 1 
ATOM   20181 C CE2 . PHE K  3 140 ? 66.223  15.733  253.934 1.00 283.18 ?  140 PHE J CE2 1 
ATOM   20182 C CZ  . PHE K  3 140 ? 66.209  16.810  254.797 1.00 285.02 ?  140 PHE J CZ  1 
ATOM   20183 N N   . TYR K  3 141 ? 69.240  15.100  249.664 1.00 271.83 ?  141 TYR J N   1 
ATOM   20184 C CA  . TYR K  3 141 ? 68.280  14.605  248.669 1.00 271.86 ?  141 TYR J CA  1 
ATOM   20185 C C   . TYR K  3 141 ? 68.331  13.078  248.614 1.00 273.82 ?  141 TYR J C   1 
ATOM   20186 O O   . TYR K  3 141 ? 69.415  12.492  248.570 1.00 273.87 ?  141 TYR J O   1 
ATOM   20187 C CB  . TYR K  3 141 ? 68.580  15.164  247.269 1.00 267.22 ?  141 TYR J CB  1 
ATOM   20188 C CG  . TYR K  3 141 ? 67.535  14.836  246.205 1.00 262.53 ?  141 TYR J CG  1 
ATOM   20189 C CD1 . TYR K  3 141 ? 66.453  15.678  245.974 1.00 261.14 ?  141 TYR J CD1 1 
ATOM   20190 C CD2 . TYR K  3 141 ? 67.608  13.656  245.468 1.00 259.83 ?  141 TYR J CD2 1 
ATOM   20191 C CE1 . TYR K  3 141 ? 65.495  15.373  245.014 1.00 259.29 ?  141 TYR J CE1 1 
ATOM   20192 C CE2 . TYR K  3 141 ? 66.654  13.342  244.508 1.00 256.81 ?  141 TYR J CE2 1 
ATOM   20193 C CZ  . TYR K  3 141 ? 65.600  14.204  244.287 1.00 257.63 ?  141 TYR J CZ  1 
ATOM   20194 O OH  . TYR K  3 141 ? 64.652  13.897  243.335 1.00 254.06 ?  141 TYR J OH  1 
ATOM   20195 N N   . PRO K  3 142 ? 67.161  12.420  248.610 1.00 267.79 ?  142 PRO J N   1 
ATOM   20196 C CA  . PRO K  3 142 ? 65.798  12.964  248.678 1.00 267.43 ?  142 PRO J CA  1 
ATOM   20197 C C   . PRO K  3 142 ? 65.342  13.295  250.108 1.00 271.97 ?  142 PRO J C   1 
ATOM   20198 O O   . PRO K  3 142 ? 66.041  12.984  251.072 1.00 274.06 ?  142 PRO J O   1 
ATOM   20199 C CB  . PRO K  3 142 ? 64.947  11.837  248.093 1.00 263.06 ?  142 PRO J CB  1 
ATOM   20200 C CG  . PRO K  3 142 ? 65.687  10.606  248.454 1.00 263.34 ?  142 PRO J CG  1 
ATOM   20201 C CD  . PRO K  3 142 ? 67.151  10.961  248.396 1.00 263.63 ?  142 PRO J CD  1 
ATOM   20202 N N   . GLY K  3 143 ? 64.172  13.923  250.221 1.00 272.50 ?  143 GLY J N   1 
ATOM   20203 C CA  . GLY K  3 143 ? 63.589  14.346  251.484 1.00 276.85 ?  143 GLY J CA  1 
ATOM   20204 C C   . GLY K  3 143 ? 62.938  13.191  252.223 1.00 281.37 ?  143 GLY J C   1 
ATOM   20205 O O   . GLY K  3 143 ? 61.723  12.997  252.127 1.00 284.63 ?  143 GLY J O   1 
ATOM   20206 N N   . ALA K  3 144 ? 63.736  12.412  252.958 1.00 268.72 ?  144 ALA J N   1 
ATOM   20207 C CA  . ALA K  3 144 ? 63.215  11.275  253.728 1.00 272.11 ?  144 ALA J CA  1 
ATOM   20208 C C   . ALA K  3 144 ? 64.223  10.973  254.844 1.00 275.15 ?  144 ALA J C   1 
ATOM   20209 O O   . ALA K  3 144 ? 65.178  10.224  254.636 1.00 274.57 ?  144 ALA J O   1 
ATOM   20210 C CB  . ALA K  3 144 ? 62.981  10.067  252.843 1.00 270.47 ?  144 ALA J CB  1 
ATOM   20211 N N   . VAL K  3 145 ? 64.004  11.579  256.018 1.00 283.08 ?  145 VAL J N   1 
ATOM   20212 C CA  . VAL K  3 145 ? 64.910  11.432  257.152 1.00 286.23 ?  145 VAL J CA  1 
ATOM   20213 C C   . VAL K  3 145 ? 64.191  10.937  258.404 1.00 292.62 ?  145 VAL J C   1 
ATOM   20214 O O   . VAL K  3 145 ? 62.978  11.111  258.561 1.00 295.72 ?  145 VAL J O   1 
ATOM   20215 C CB  . VAL K  3 145 ? 65.562  12.800  257.452 1.00 285.41 ?  145 VAL J CB  1 
ATOM   20216 C CG1 . VAL K  3 145 ? 66.464  13.234  256.312 1.00 279.79 ?  145 VAL J CG1 1 
ATOM   20217 C CG2 . VAL K  3 145 ? 64.479  13.851  257.720 1.00 285.67 ?  145 VAL J CG2 1 
ATOM   20218 N N   . THR K  3 146 ? 64.959  10.274  259.284 1.00 290.51 ?  146 THR J N   1 
ATOM   20219 C CA  . THR K  3 146 ? 64.481  9.797   260.583 1.00 297.17 ?  146 THR J CA  1 
ATOM   20220 C C   . THR K  3 146 ? 65.474  10.242  261.657 1.00 300.31 ?  146 THR J C   1 
ATOM   20221 O O   . THR K  3 146 ? 66.670  9.945   261.554 1.00 297.68 ?  146 THR J O   1 
ATOM   20222 C CB  . THR K  3 146 ? 64.332  8.268   260.581 1.00 298.70 ?  146 THR J CB  1 
ATOM   20223 O OG1 . THR K  3 146 ? 65.575  7.663   260.212 1.00 295.74 ?  146 THR J OG1 1 
ATOM   20224 C CG2 . THR K  3 146 ? 63.282  7.834   259.575 1.00 299.57 ?  146 THR J CG2 1 
ATOM   20225 N N   . VAL K  3 147 ? 64.986  10.956  262.678 1.00 292.64 ?  147 VAL J N   1 
ATOM   20226 C CA  . VAL K  3 147 ? 65.814  11.518  263.751 1.00 295.36 ?  147 VAL J CA  1 
ATOM   20227 C C   . VAL K  3 147 ? 65.590  10.753  265.057 1.00 302.62 ?  147 VAL J C   1 
ATOM   20228 O O   . VAL K  3 147 ? 64.439  10.525  265.447 1.00 306.81 ?  147 VAL J O   1 
ATOM   20229 C CB  . VAL K  3 147 ? 65.520  13.019  263.936 1.00 294.61 ?  147 VAL J CB  1 
ATOM   20230 C CG1 . VAL K  3 147 ? 66.437  13.620  264.979 1.00 299.10 ?  147 VAL J CG1 1 
ATOM   20231 C CG2 . VAL K  3 147 ? 65.666  13.761  262.610 1.00 287.69 ?  147 VAL J CG2 1 
ATOM   20232 N N   . ALA K  3 148 ? 66.678  10.355  265.733 1.00 303.23 ?  148 ALA J N   1 
ATOM   20233 C CA  . ALA K  3 148 ? 66.593  9.681   267.033 1.00 312.24 ?  148 ALA J CA  1 
ATOM   20234 C C   . ALA K  3 148 ? 67.514  10.345  268.053 1.00 320.44 ?  148 ALA J C   1 
ATOM   20235 O O   . ALA K  3 148 ? 68.736  10.354  267.862 1.00 319.47 ?  148 ALA J O   1 
ATOM   20236 C CB  . ALA K  3 148 ? 66.946  8.196   266.907 1.00 314.11 ?  148 ALA J CB  1 
ATOM   20237 N N   . TRP K  3 149 ? 66.948  10.899  269.132 1.00 312.20 ?  149 TRP J N   1 
ATOM   20238 C CA  . TRP K  3 149 ? 67.784  11.558  270.130 1.00 318.91 ?  149 TRP J CA  1 
ATOM   20239 C C   . TRP K  3 149 ? 68.323  10.553  271.151 1.00 331.70 ?  149 TRP J C   1 
ATOM   20240 O O   . TRP K  3 149 ? 67.732  9.497   271.388 1.00 338.89 ?  149 TRP J O   1 
ATOM   20241 C CB  . TRP K  3 149 ? 66.983  12.638  270.861 1.00 319.53 ?  149 TRP J CB  1 
ATOM   20242 C CG  . TRP K  3 149 ? 66.530  13.758  269.977 1.00 311.79 ?  149 TRP J CG  1 
ATOM   20243 C CD1 . TRP K  3 149 ? 65.411  13.777  269.203 1.00 308.76 ?  149 TRP J CD1 1 
ATOM   20244 C CD2 . TRP K  3 149 ? 67.159  15.037  269.804 1.00 307.30 ?  149 TRP J CD2 1 
ATOM   20245 N NE1 . TRP K  3 149 ? 65.312  14.975  268.538 1.00 302.83 ?  149 TRP J NE1 1 
ATOM   20246 C CE2 . TRP K  3 149 ? 66.372  15.768  268.892 1.00 301.75 ?  149 TRP J CE2 1 
ATOM   20247 C CE3 . TRP K  3 149 ? 68.315  15.630  270.323 1.00 307.81 ?  149 TRP J CE3 1 
ATOM   20248 C CZ2 . TRP K  3 149 ? 66.701  17.059  268.487 1.00 297.71 ?  149 TRP J CZ2 1 
ATOM   20249 C CZ3 . TRP K  3 149 ? 68.641  16.916  269.919 1.00 302.73 ?  149 TRP J CZ3 1 
ATOM   20250 C CH2 . TRP K  3 149 ? 67.836  17.615  269.009 1.00 297.90 ?  149 TRP J CH2 1 
ATOM   20251 N N   . LYS K  3 150 ? 69.449  10.908  271.775 1.00 315.05 ?  150 LYS J N   1 
ATOM   20252 C CA  . LYS K  3 150 ? 70.112  10.045  272.753 1.00 323.87 ?  150 LYS J CA  1 
ATOM   20253 C C   . LYS K  3 150 ? 70.649  10.808  273.959 1.00 329.64 ?  150 LYS J C   1 
ATOM   20254 O O   . LYS K  3 150 ? 71.340  11.821  273.809 1.00 321.10 ?  150 LYS J O   1 
ATOM   20255 C CB  . LYS K  3 150 ? 71.178  9.134   272.132 1.00 320.04 ?  150 LYS J CB  1 
ATOM   20256 C CG  . LYS K  3 150 ? 70.509  8.014   271.341 1.00 313.93 ?  150 LYS J CG  1 
ATOM   20257 C CD  . LYS K  3 150 ? 71.426  6.868   270.979 1.00 303.69 ?  150 LYS J CD  1 
ATOM   20258 C CE  . LYS K  3 150 ? 70.669  5.897   270.092 1.00 300.97 ?  150 LYS J CE  1 
ATOM   20259 N NZ  . LYS K  3 150 ? 71.527  5.195   269.119 1.00 293.16 1  150 LYS J NZ  1 
ATOM   20260 N N   . ALA K  3 151 ? 70.333  10.298  275.148 1.00 316.58 ?  151 ALA J N   1 
ATOM   20261 C CA  . ALA K  3 151 ? 70.900  10.749  276.417 1.00 322.63 ?  151 ALA J CA  1 
ATOM   20262 C C   . ALA K  3 151 ? 71.978  9.741   276.810 1.00 329.06 ?  151 ALA J C   1 
ATOM   20263 O O   . ALA K  3 151 ? 71.666  8.619   277.224 1.00 335.69 ?  151 ALA J O   1 
ATOM   20264 C CB  . ALA K  3 151 ? 69.827  10.869  277.496 1.00 330.76 ?  151 ALA J CB  1 
ATOM   20265 N N   . ASP K  3 152 ? 73.244  10.150  276.677 1.00 327.80 ?  152 ASP J N   1 
ATOM   20266 C CA  . ASP K  3 152 ? 74.428  9.301   276.798 1.00 325.82 ?  152 ASP J CA  1 
ATOM   20267 C C   . ASP K  3 152 ? 74.369  8.180   275.767 1.00 316.19 ?  152 ASP J C   1 
ATOM   20268 O O   . ASP K  3 152 ? 74.677  8.399   274.591 1.00 304.45 ?  152 ASP J O   1 
ATOM   20269 C CB  . ASP K  3 152 ? 74.528  8.693   278.206 1.00 334.07 ?  152 ASP J CB  1 
ATOM   20270 C CG  . ASP K  3 152 ? 74.813  9.727   279.281 1.00 341.23 ?  152 ASP J CG  1 
ATOM   20271 O OD1 . ASP K  3 152 ? 75.408  10.772  278.960 1.00 340.61 ?  152 ASP J OD1 1 
ATOM   20272 O OD2 . ASP K  3 152 ? 74.433  9.494   280.451 1.00 352.62 -1 152 ASP J OD2 1 
ATOM   20273 N N   . SER K  3 153 ? 73.987  6.978   276.187 1.00 339.60 ?  153 SER J N   1 
ATOM   20274 C CA  . SER K  3 153 ? 73.814  5.862   275.269 1.00 329.35 ?  153 SER J CA  1 
ATOM   20275 C C   . SER K  3 153 ? 72.384  5.347   275.257 1.00 331.54 ?  153 SER J C   1 
ATOM   20276 O O   . SER K  3 153 ? 72.081  4.412   274.507 1.00 320.70 ?  153 SER J O   1 
ATOM   20277 C CB  . SER K  3 153 ? 74.776  4.717   275.616 1.00 328.73 ?  153 SER J CB  1 
ATOM   20278 O OG  . SER K  3 153 ? 74.546  4.233   276.927 1.00 342.30 ?  153 SER J OG  1 
ATOM   20279 N N   . SER K  3 154 ? 71.494  5.951   276.050 1.00 333.87 ?  154 SER J N   1 
ATOM   20280 C CA  . SER K  3 154 ? 70.084  5.615   276.209 1.00 334.19 ?  154 SER J CA  1 
ATOM   20281 C C   . SER K  3 154 ? 69.199  6.523   275.370 1.00 333.17 ?  154 SER J C   1 
ATOM   20282 O O   . SER K  3 154 ? 69.369  7.751   275.392 1.00 336.97 ?  154 SER J O   1 
ATOM   20283 C CB  . SER K  3 154 ? 69.672  5.706   277.676 1.00 339.95 ?  154 SER J CB  1 
ATOM   20284 O OG  . SER K  3 154 ? 68.420  5.073   277.882 1.00 345.03 ?  154 SER J OG  1 
ATOM   20285 N N   . PRO K  3 155 ? 68.260  5.939   274.632 1.00 328.74 ?  155 PRO J N   1 
ATOM   20286 C CA  . PRO K  3 155 ? 67.365  6.728   273.778 1.00 320.57 ?  155 PRO J CA  1 
ATOM   20287 C C   . PRO K  3 155 ? 66.389  7.585   274.576 1.00 330.24 ?  155 PRO J C   1 
ATOM   20288 O O   . PRO K  3 155 ? 66.041  7.287   275.721 1.00 339.24 ?  155 PRO J O   1 
ATOM   20289 C CB  . PRO K  3 155 ? 66.636  5.661   272.954 1.00 308.41 ?  155 PRO J CB  1 
ATOM   20290 C CG  . PRO K  3 155 ? 66.672  4.440   273.813 1.00 314.62 ?  155 PRO J CG  1 
ATOM   20291 C CD  . PRO K  3 155 ? 67.996  4.493   274.525 1.00 321.83 ?  155 PRO J CD  1 
ATOM   20292 N N   . VAL K  3 156 ? 65.947  8.668   273.938 1.00 325.76 ?  156 VAL J N   1 
ATOM   20293 C CA  . VAL K  3 156 ? 64.997  9.620   274.507 1.00 334.28 ?  156 VAL J CA  1 
ATOM   20294 C C   . VAL K  3 156 ? 63.625  9.276   273.951 1.00 333.53 ?  156 VAL J C   1 
ATOM   20295 O O   . VAL K  3 156 ? 63.441  9.189   272.730 1.00 325.12 ?  156 VAL J O   1 
ATOM   20296 C CB  . VAL K  3 156 ? 65.383  11.070  274.170 1.00 329.06 ?  156 VAL J CB  1 
ATOM   20297 C CG1 . VAL K  3 156 ? 64.341  12.027  274.701 1.00 337.29 ?  156 VAL J CG1 1 
ATOM   20298 C CG2 . VAL K  3 156 ? 66.744  11.405  274.742 1.00 329.81 ?  156 VAL J CG2 1 
ATOM   20299 N N   . LYS K  3 157 ? 62.661  9.073   274.852 1.00 311.39 ?  157 LYS J N   1 
ATOM   20300 C CA  . LYS K  3 157 ? 61.330  8.607   274.479 1.00 311.21 ?  157 LYS J CA  1 
ATOM   20301 C C   . LYS K  3 157 ? 60.396  9.745   274.073 1.00 312.55 ?  157 LYS J C   1 
ATOM   20302 O O   . LYS K  3 157 ? 59.853  9.747   272.963 1.00 305.57 ?  157 LYS J O   1 
ATOM   20303 C CB  . LYS K  3 157 ? 60.710  7.923   275.703 1.00 320.16 ?  157 LYS J CB  1 
ATOM   20304 C CG  . LYS K  3 157 ? 61.434  6.710   276.267 1.00 321.23 ?  157 LYS J CG  1 
ATOM   20305 C CD  . LYS K  3 157 ? 61.168  5.388   275.605 1.00 316.07 ?  157 LYS J CD  1 
ATOM   20306 C CE  . LYS K  3 157 ? 62.067  4.356   276.273 1.00 318.34 ?  157 LYS J CE  1 
ATOM   20307 N NZ  . LYS K  3 157 ? 61.643  2.955   276.035 1.00 318.80 1  157 LYS J NZ  1 
ATOM   20308 N N   . ALA K  3 158 ? 60.207  10.718  274.960 1.00 307.83 ?  158 ALA J N   1 
ATOM   20309 C CA  . ALA K  3 158 ? 59.290  11.827  274.743 1.00 310.71 ?  158 ALA J CA  1 
ATOM   20310 C C   . ALA K  3 158 ? 60.037  13.139  274.550 1.00 310.15 ?  158 ALA J C   1 
ATOM   20311 O O   . ALA K  3 158 ? 61.235  13.258  274.822 1.00 309.64 ?  158 ALA J O   1 
ATOM   20312 C CB  . ALA K  3 158 ? 58.306  11.954  275.912 1.00 322.11 ?  158 ALA J CB  1 
ATOM   20313 N N   . GLY K  3 159 ? 59.290  14.132  274.071 1.00 308.39 ?  159 GLY J N   1 
ATOM   20314 C CA  . GLY K  3 159 ? 59.800  15.463  273.840 1.00 306.51 ?  159 GLY J CA  1 
ATOM   20315 C C   . GLY K  3 159 ? 60.380  15.725  272.470 1.00 301.65 ?  159 GLY J C   1 
ATOM   20316 O O   . GLY K  3 159 ? 60.892  16.828  272.240 1.00 299.93 ?  159 GLY J O   1 
ATOM   20317 N N   . VAL K  3 160 ? 60.337  14.757  271.558 1.00 322.92 ?  160 VAL J N   1 
ATOM   20318 C CA  . VAL K  3 160 ? 60.921  14.926  270.231 1.00 306.20 ?  160 VAL J CA  1 
ATOM   20319 C C   . VAL K  3 160 ? 59.859  15.427  269.257 1.00 296.94 ?  160 VAL J C   1 
ATOM   20320 O O   . VAL K  3 160 ? 58.816  14.788  269.076 1.00 297.44 ?  160 VAL J O   1 
ATOM   20321 C CB  . VAL K  3 160 ? 61.536  13.607  269.740 1.00 295.68 ?  160 VAL J CB  1 
ATOM   20322 C CG1 . VAL K  3 160 ? 62.174  13.780  268.367 1.00 283.03 ?  160 VAL J CG1 1 
ATOM   20323 C CG2 . VAL K  3 160 ? 62.537  13.071  270.762 1.00 301.22 ?  160 VAL J CG2 1 
ATOM   20324 N N   . GLU K  3 161 ? 60.124  16.578  268.638 1.00 317.45 ?  161 GLU J N   1 
ATOM   20325 C CA  . GLU K  3 161 ? 59.260  17.186  267.627 1.00 306.65 ?  161 GLU J CA  1 
ATOM   20326 C C   . GLU K  3 161 ? 60.081  17.458  266.371 1.00 294.44 ?  161 GLU J C   1 
ATOM   20327 O O   . GLU K  3 161 ? 61.049  18.224  266.417 1.00 294.69 ?  161 GLU J O   1 
ATOM   20328 C CB  . GLU K  3 161 ? 58.542  18.428  268.156 1.00 305.94 ?  161 GLU J CB  1 
ATOM   20329 C CG  . GLU K  3 161 ? 57.746  18.091  269.416 1.00 321.57 ?  161 GLU J CG  1 
ATOM   20330 C CD  . GLU K  3 161 ? 56.279  18.468  269.313 1.00 320.46 ?  161 GLU J CD  1 
ATOM   20331 O OE1 . GLU K  3 161 ? 55.692  18.259  268.228 1.00 308.84 ?  161 GLU J OE1 1 
ATOM   20332 O OE2 . GLU K  3 161 ? 55.702  18.935  270.316 1.00 335.73 -1 161 GLU J OE2 1 
ATOM   20333 N N   . THR K  3 162 ? 59.698  16.839  265.254 1.00 294.91 ?  162 THR J N   1 
ATOM   20334 C CA  . THR K  3 162 ? 60.449  16.922  264.007 1.00 285.21 ?  162 THR J CA  1 
ATOM   20335 C C   . THR K  3 162 ? 59.587  17.400  262.848 1.00 276.38 ?  162 THR J C   1 
ATOM   20336 O O   . THR K  3 162 ? 58.447  16.956  262.680 1.00 275.79 ?  162 THR J O   1 
ATOM   20337 C CB  . THR K  3 162 ? 61.046  15.556  263.633 1.00 283.64 ?  162 THR J CB  1 
ATOM   20338 O OG1 . THR K  3 162 ? 61.819  15.046  264.726 1.00 290.33 ?  162 THR J OG1 1 
ATOM   20339 C CG2 . THR K  3 162 ? 61.922  15.666  262.390 1.00 276.85 ?  162 THR J CG2 1 
ATOM   20340 N N   . THR K  3 163 ? 60.138  18.321  262.059 1.00 291.13 ?  163 THR J N   1 
ATOM   20341 C CA  . THR K  3 163 ? 59.432  18.848  260.906 1.00 280.98 ?  163 THR J CA  1 
ATOM   20342 C C   . THR K  3 163 ? 59.537  17.867  259.742 1.00 277.36 ?  163 THR J C   1 
ATOM   20343 O O   . THR K  3 163 ? 60.374  16.962  259.727 1.00 284.16 ?  163 THR J O   1 
ATOM   20344 C CB  . THR K  3 163 ? 60.004  20.196  260.475 1.00 273.79 ?  163 THR J CB  1 
ATOM   20345 O OG1 . THR K  3 163 ? 61.271  19.989  259.836 1.00 272.27 ?  163 THR J OG1 1 
ATOM   20346 C CG2 . THR K  3 163 ? 60.190  21.103  261.673 1.00 279.69 ?  163 THR J CG2 1 
ATOM   20347 N N   . THR K  3 164 ? 58.726  18.053  258.813 1.00 284.08 ?  164 THR J N   1 
ATOM   20348 C CA  . THR K  3 164 ? 58.732  17.250  257.596 1.00 274.14 ?  164 THR J CA  1 
ATOM   20349 C C   . THR K  3 164 ? 59.601  17.875  256.508 1.00 266.01 ?  164 THR J C   1 
ATOM   20350 O O   . THR K  3 164 ? 59.640  19.101  256.374 1.00 263.24 ?  164 THR J O   1 
ATOM   20351 C CB  . THR K  3 164 ? 57.317  17.073  257.058 1.00 264.27 ?  164 THR J CB  1 
ATOM   20352 O OG1 . THR K  3 164 ? 56.728  18.357  256.818 1.00 260.46 ?  164 THR J OG1 1 
ATOM   20353 C CG2 . THR K  3 164 ? 56.469  16.303  258.052 1.00 266.49 ?  164 THR J CG2 1 
ATOM   20354 N N   . PRO K  3 165 ? 60.320  17.028  255.765 1.00 272.25 ?  165 PRO J N   1 
ATOM   20355 C CA  . PRO K  3 165 ? 61.185  17.524  254.687 1.00 266.45 ?  165 PRO J CA  1 
ATOM   20356 C C   . PRO K  3 165 ? 60.412  18.475  253.783 1.00 256.92 ?  165 PRO J C   1 
ATOM   20357 O O   . PRO K  3 165 ? 59.217  18.305  253.535 1.00 253.11 ?  165 PRO J O   1 
ATOM   20358 C CB  . PRO K  3 165 ? 61.622  16.247  253.963 1.00 266.40 ?  165 PRO J CB  1 
ATOM   20359 C CG  . PRO K  3 165 ? 61.596  15.208  255.041 1.00 272.97 ?  165 PRO J CG  1 
ATOM   20360 C CD  . PRO K  3 165 ? 60.432  15.567  255.929 1.00 276.30 ?  165 PRO J CD  1 
ATOM   20361 N N   . SER K  3 166 ? 61.120  19.475  253.274 1.00 273.25 ?  166 SER J N   1 
ATOM   20362 C CA  . SER K  3 166 ? 60.506  20.501  252.441 1.00 262.44 ?  166 SER J CA  1 
ATOM   20363 C C   . SER K  3 166 ? 61.600  21.089  251.570 1.00 258.51 ?  166 SER J C   1 
ATOM   20364 O O   . SER K  3 166 ? 62.511  21.751  252.076 1.00 263.67 ?  166 SER J O   1 
ATOM   20365 C CB  . SER K  3 166 ? 59.841  21.578  253.295 1.00 261.50 ?  166 SER J CB  1 
ATOM   20366 O OG  . SER K  3 166 ? 60.757  22.164  254.206 1.00 264.25 ?  166 SER J OG  1 
ATOM   20367 N N   . LYS K  3 167 ? 61.503  20.841  250.269 1.00 272.60 ?  167 LYS J N   1 
ATOM   20368 C CA  . LYS K  3 167 ? 62.502  21.300  249.324 1.00 270.83 ?  167 LYS J CA  1 
ATOM   20369 C C   . LYS K  3 167 ? 62.445  22.816  249.223 1.00 268.12 ?  167 LYS J C   1 
ATOM   20370 O O   . LYS K  3 167 ? 61.384  23.427  249.377 1.00 261.86 ?  167 LYS J O   1 
ATOM   20371 C CB  . LYS K  3 167 ? 62.104  20.669  247.990 1.00 259.81 ?  167 LYS J CB  1 
ATOM   20372 C CG  . LYS K  3 167 ? 62.527  21.225  246.666 1.00 250.50 ?  167 LYS J CG  1 
ATOM   20373 C CD  . LYS K  3 167 ? 61.819  20.295  245.694 1.00 241.71 ?  167 LYS J CD  1 
ATOM   20374 C CE  . LYS K  3 167 ? 61.974  20.655  244.250 1.00 235.41 ?  167 LYS J CE  1 
ATOM   20375 N NZ  . LYS K  3 167 ? 61.180  19.659  243.493 1.00 229.54 1  167 LYS J NZ  1 
ATOM   20376 N N   . GLN K  3 168 ? 63.616  23.435  248.953 1.00 264.35 ?  168 GLN J N   1 
ATOM   20377 C CA  . GLN K  3 168 ? 63.717  24.897  248.876 1.00 263.41 ?  168 GLN J CA  1 
ATOM   20378 C C   . GLN K  3 168 ? 64.517  25.361  247.657 1.00 259.57 ?  168 GLN J C   1 
ATOM   20379 O O   . GLN K  3 168 ? 65.714  25.641  247.771 1.00 261.60 ?  168 GLN J O   1 
ATOM   20380 C CB  . GLN K  3 168 ? 64.365  25.378  250.187 1.00 269.78 ?  168 GLN J CB  1 
ATOM   20381 C CG  . GLN K  3 168 ? 63.837  26.654  250.780 1.00 265.27 ?  168 GLN J CG  1 
ATOM   20382 C CD  . GLN K  3 168 ? 64.488  26.952  252.117 1.00 275.64 ?  168 GLN J CD  1 
ATOM   20383 O OE1 . GLN K  3 168 ? 64.946  26.045  252.817 1.00 283.43 ?  168 GLN J OE1 1 
ATOM   20384 N NE2 . GLN K  3 168 ? 64.533  28.225  252.480 1.00 275.58 ?  168 GLN J NE2 1 
ATOM   20385 N N   . SER K  3 169 ? 63.860  25.448  246.500 1.00 262.85 ?  169 SER J N   1 
ATOM   20386 C CA  . SER K  3 169 ? 64.487  25.960  245.277 1.00 256.45 ?  169 SER J CA  1 
ATOM   20387 C C   . SER K  3 169 ? 65.808  25.253  244.972 1.00 260.08 ?  169 SER J C   1 
ATOM   20388 O O   . SER K  3 169 ? 66.720  25.844  244.389 1.00 257.37 ?  169 SER J O   1 
ATOM   20389 C CB  . SER K  3 169 ? 64.692  27.474  245.381 1.00 253.50 ?  169 SER J CB  1 
ATOM   20390 O OG  . SER K  3 169 ? 65.297  28.003  244.218 1.00 251.45 ?  169 SER J OG  1 
ATOM   20391 N N   . ASN K  3 170 ? 65.931  23.997  245.364 1.00 256.03 ?  170 ASN J N   1 
ATOM   20392 C CA  . ASN K  3 170 ? 67.168  23.245  245.177 1.00 258.83 ?  170 ASN J CA  1 
ATOM   20393 C C   . ASN K  3 170 ? 66.894  21.779  245.457 1.00 263.84 ?  170 ASN J C   1 
ATOM   20394 O O   . ASN K  3 170 ? 65.741  21.340  245.553 1.00 265.19 ?  170 ASN J O   1 
ATOM   20395 C CB  . ASN K  3 170 ? 68.288  23.744  246.096 1.00 261.99 ?  170 ASN J CB  1 
ATOM   20396 C CG  . ASN K  3 170 ? 69.491  24.249  245.332 1.00 258.70 ?  170 ASN J CG  1 
ATOM   20397 O OD1 . ASN K  3 170 ? 69.727  23.845  244.194 1.00 255.23 ?  170 ASN J OD1 1 
ATOM   20398 N ND2 . ASN K  3 170 ? 70.281  25.107  245.967 1.00 259.45 ?  170 ASN J ND2 1 
ATOM   20399 N N   . ASN K  3 171 ? 67.982  21.027  245.569 1.00 266.57 ?  171 ASN J N   1 
ATOM   20400 C CA  . ASN K  3 171 ? 67.954  19.655  246.034 1.00 270.50 ?  171 ASN J CA  1 
ATOM   20401 C C   . ASN K  3 171 ? 67.863  19.623  247.548 1.00 279.38 ?  171 ASN J C   1 
ATOM   20402 O O   . ASN K  3 171 ? 67.572  18.572  248.128 1.00 282.96 ?  171 ASN J O   1 
ATOM   20403 C CB  . ASN K  3 171 ? 69.232  18.943  245.592 1.00 273.36 ?  171 ASN J CB  1 
ATOM   20404 C CG  . ASN K  3 171 ? 70.480  19.546  246.237 1.00 280.23 ?  171 ASN J CG  1 
ATOM   20405 O OD1 . ASN K  3 171 ? 70.536  20.751  246.499 1.00 285.25 ?  171 ASN J OD1 1 
ATOM   20406 N ND2 . ASN K  3 171 ? 71.480  18.711  246.498 1.00 280.50 ?  171 ASN J ND2 1 
ATOM   20407 N N   . LYS K  3 172 ? 68.119  20.771  248.177 1.00 269.47 ?  172 LYS J N   1 
ATOM   20408 C CA  . LYS K  3 172 ? 68.106  20.956  249.622 1.00 275.90 ?  172 LYS J CA  1 
ATOM   20409 C C   . LYS K  3 172 ? 66.693  20.801  250.179 1.00 279.16 ?  172 LYS J C   1 
ATOM   20410 O O   . LYS K  3 172 ? 65.777  21.548  249.816 1.00 273.48 ?  172 LYS J O   1 
ATOM   20411 C CB  . LYS K  3 172 ? 68.723  22.301  250.011 1.00 274.97 ?  172 LYS J CB  1 
ATOM   20412 C CG  . LYS K  3 172 ? 67.780  23.498  250.076 1.00 270.95 ?  172 LYS J CG  1 
ATOM   20413 C CD  . LYS K  3 172 ? 68.514  24.785  250.340 1.00 269.35 ?  172 LYS J CD  1 
ATOM   20414 C CE  . LYS K  3 172 ? 69.149  24.715  251.718 1.00 281.51 ?  172 LYS J CE  1 
ATOM   20415 N NZ  . LYS K  3 172 ? 69.050  26.001  252.456 1.00 290.77 1  172 LYS J NZ  1 
ATOM   20416 N N   . TYR K  3 173 ? 66.475  19.745  250.944 1.00 283.13 ?  173 TYR J N   1 
ATOM   20417 C CA  . TYR K  3 173 ? 65.223  19.624  251.664 1.00 283.15 ?  173 TYR J CA  1 
ATOM   20418 C C   . TYR K  3 173 ? 65.546  20.167  253.054 1.00 287.61 ?  173 TYR J C   1 
ATOM   20419 O O   . TYR K  3 173 ? 66.711  20.192  253.460 1.00 291.48 ?  173 TYR J O   1 
ATOM   20420 C CB  . TYR K  3 173 ? 64.766  18.163  251.704 1.00 283.32 ?  173 TYR J CB  1 
ATOM   20421 C CG  . TYR K  3 173 ? 64.053  17.730  250.431 1.00 274.89 ?  173 TYR J CG  1 
ATOM   20422 C CD1 . TYR K  3 173 ? 64.801  17.398  249.307 1.00 268.68 ?  173 TYR J CD1 1 
ATOM   20423 C CD2 . TYR K  3 173 ? 62.667  17.660  250.334 1.00 266.68 ?  173 TYR J CD2 1 
ATOM   20424 C CE1 . TYR K  3 173 ? 64.205  17.002  248.126 1.00 254.98 ?  173 TYR J CE1 1 
ATOM   20425 C CE2 . TYR K  3 173 ? 62.052  17.259  249.137 1.00 254.98 ?  173 TYR J CE2 1 
ATOM   20426 C CZ  . TYR K  3 173 ? 62.835  16.932  248.039 1.00 246.15 ?  173 TYR J CZ  1 
ATOM   20427 O OH  . TYR K  3 173 ? 62.262  16.534  246.847 1.00 234.06 ?  173 TYR J OH  1 
ATOM   20428 N N   . ALA K  3 174 ? 64.535  20.612  253.792 1.00 272.99 ?  174 ALA J N   1 
ATOM   20429 C CA  . ALA K  3 174 ? 64.799  21.193  255.104 1.00 275.89 ?  174 ALA J CA  1 
ATOM   20430 C C   . ALA K  3 174 ? 64.123  20.413  256.221 1.00 283.03 ?  174 ALA J C   1 
ATOM   20431 O O   . ALA K  3 174 ? 62.985  19.958  256.074 1.00 282.23 ?  174 ALA J O   1 
ATOM   20432 C CB  . ALA K  3 174 ? 64.353  22.655  255.153 1.00 270.26 ?  174 ALA J CB  1 
ATOM   20433 N N   . ALA K  3 175 ? 64.828  20.283  257.348 1.00 265.44 ?  175 ALA J N   1 
ATOM   20434 C CA  . ALA K  3 175 ? 64.287  19.567  258.498 1.00 274.15 ?  175 ALA J CA  1 
ATOM   20435 C C   . ALA K  3 175 ? 64.969  20.001  259.790 1.00 286.01 ?  175 ALA J C   1 
ATOM   20436 O O   . ALA K  3 175 ? 66.201  20.016  259.867 1.00 288.47 ?  175 ALA J O   1 
ATOM   20437 C CB  . ALA K  3 175 ? 64.441  18.056  258.306 1.00 272.40 ?  175 ALA J CB  1 
ATOM   20438 N N   . SER K  3 176 ? 64.164  20.356  260.792 1.00 271.20 ?  176 SER J N   1 
ATOM   20439 C CA  . SER K  3 176 ? 64.632  20.776  262.111 1.00 274.79 ?  176 SER J CA  1 
ATOM   20440 C C   . SER K  3 176 ? 64.006  19.855  263.156 1.00 279.45 ?  176 SER J C   1 
ATOM   20441 O O   . SER K  3 176 ? 62.795  19.611  263.121 1.00 279.57 ?  176 SER J O   1 
ATOM   20442 C CB  . SER K  3 176 ? 64.300  22.247  262.392 1.00 274.89 ?  176 SER J CB  1 
ATOM   20443 O OG  . SER K  3 176 ? 62.967  22.561  262.040 1.00 274.24 ?  176 SER J OG  1 
ATOM   20444 N N   . SER K  3 177 ? 64.823  19.357  264.087 1.00 279.09 ?  177 SER J N   1 
ATOM   20445 C CA  . SER K  3 177 ? 64.386  18.475  265.169 1.00 287.71 ?  177 SER J CA  1 
ATOM   20446 C C   . SER K  3 177 ? 64.646  19.136  266.517 1.00 296.01 ?  177 SER J C   1 
ATOM   20447 O O   . SER K  3 177 ? 65.774  19.555  266.797 1.00 296.26 ?  177 SER J O   1 
ATOM   20448 C CB  . SER K  3 177 ? 65.099  17.119  265.110 1.00 287.52 ?  177 SER J CB  1 
ATOM   20449 O OG  . SER K  3 177 ? 64.594  16.236  266.101 1.00 294.95 ?  177 SER J OG  1 
ATOM   20450 N N   . TYR K  3 178 ? 63.603  19.231  267.344 1.00 290.27 ?  178 TYR J N   1 
ATOM   20451 C CA  . TYR K  3 178 ? 63.681  19.884  268.643 1.00 300.11 ?  178 TYR J CA  1 
ATOM   20452 C C   . TYR K  3 178 ? 63.487  18.890  269.781 1.00 308.48 ?  178 TYR J C   1 
ATOM   20453 O O   . TYR K  3 178 ? 62.759  17.902  269.646 1.00 308.87 ?  178 TYR J O   1 
ATOM   20454 C CB  . TYR K  3 178 ? 62.576  20.937  268.757 1.00 302.76 ?  178 TYR J CB  1 
ATOM   20455 C CG  . TYR K  3 178 ? 62.715  22.058  267.772 1.00 290.20 ?  178 TYR J CG  1 
ATOM   20456 C CD1 . TYR K  3 178 ? 62.183  21.929  266.497 1.00 275.48 ?  178 TYR J CD1 1 
ATOM   20457 C CD2 . TYR K  3 178 ? 63.358  23.239  268.104 1.00 291.49 ?  178 TYR J CD2 1 
ATOM   20458 C CE1 . TYR K  3 178 ? 62.298  22.929  265.576 1.00 268.34 ?  178 TYR J CE1 1 
ATOM   20459 C CE2 . TYR K  3 178 ? 63.476  24.256  267.183 1.00 283.69 ?  178 TYR J CE2 1 
ATOM   20460 C CZ  . TYR K  3 178 ? 62.942  24.091  265.920 1.00 275.16 ?  178 TYR J CZ  1 
ATOM   20461 O OH  . TYR K  3 178 ? 63.048  25.088  264.988 1.00 271.04 ?  178 TYR J OH  1 
ATOM   20462 N N   . LEU K  3 179 ? 64.147  19.163  270.912 1.00 292.03 ?  179 LEU J N   1 
ATOM   20463 C CA  . LEU K  3 179 ? 64.021  18.333  272.112 1.00 296.41 ?  179 LEU J CA  1 
ATOM   20464 C C   . LEU K  3 179 ? 63.878  19.259  273.316 1.00 307.22 ?  179 LEU J C   1 
ATOM   20465 O O   . LEU K  3 179 ? 64.865  19.842  273.776 1.00 312.84 ?  179 LEU J O   1 
ATOM   20466 C CB  . LEU K  3 179 ? 65.220  17.405  272.280 1.00 296.90 ?  179 LEU J CB  1 
ATOM   20467 C CG  . LEU K  3 179 ? 65.216  16.472  273.498 1.00 301.34 ?  179 LEU J CG  1 
ATOM   20468 C CD1 . LEU K  3 179 ? 63.963  15.611  273.524 1.00 302.61 ?  179 LEU J CD1 1 
ATOM   20469 C CD2 . LEU K  3 179 ? 66.473  15.609  273.529 1.00 301.33 ?  179 LEU J CD2 1 
ATOM   20470 N N   . SER K  3 180 ? 62.653  19.391  273.823 1.00 294.32 ?  180 SER J N   1 
ATOM   20471 C CA  . SER K  3 180 ? 62.393  20.254  274.969 1.00 300.82 ?  180 SER J CA  1 
ATOM   20472 C C   . SER K  3 180 ? 62.788  19.492  276.227 1.00 316.96 ?  180 SER J C   1 
ATOM   20473 O O   . SER K  3 180 ? 62.231  18.426  276.511 1.00 321.55 ?  180 SER J O   1 
ATOM   20474 C CB  . SER K  3 180 ? 60.931  20.697  275.012 1.00 298.92 ?  180 SER J CB  1 
ATOM   20475 O OG  . SER K  3 180 ? 60.057  19.603  275.211 1.00 300.05 ?  180 SER J OG  1 
ATOM   20476 N N   . LEU K  3 181 ? 63.735  20.031  276.984 1.00 305.51 ?  181 LEU J N   1 
ATOM   20477 C CA  . LEU K  3 181 ? 64.190  19.404  278.215 1.00 309.94 ?  181 LEU J CA  1 
ATOM   20478 C C   . LEU K  3 181 ? 64.141  20.412  279.349 1.00 327.07 ?  181 LEU J C   1 
ATOM   20479 O O   . LEU K  3 181 ? 63.841  21.592  279.158 1.00 326.77 ?  181 LEU J O   1 
ATOM   20480 C CB  . LEU K  3 181 ? 65.609  18.829  278.085 1.00 308.80 ?  181 LEU J CB  1 
ATOM   20481 C CG  . LEU K  3 181 ? 65.849  17.661  277.127 1.00 306.26 ?  181 LEU J CG  1 
ATOM   20482 C CD1 . LEU K  3 181 ? 67.312  17.246  277.165 1.00 305.88 ?  181 LEU J CD1 1 
ATOM   20483 C CD2 . LEU K  3 181 ? 64.950  16.487  277.478 1.00 308.55 ?  181 LEU J CD2 1 
ATOM   20484 N N   . THR K  3 182 ? 64.416  19.937  280.505 1.00 321.38 ?  182 THR J N   1 
ATOM   20485 C CA  . THR K  3 182 ? 64.445  20.832  281.642 1.00 333.24 ?  182 THR J CA  1 
ATOM   20486 C C   . THR K  3 182 ? 65.885  21.150  282.016 1.00 334.76 ?  182 THR J C   1 
ATOM   20487 O O   . THR K  3 182 ? 66.791  20.357  281.746 1.00 327.35 ?  182 THR J O   1 
ATOM   20488 C CB  . THR K  3 182 ? 63.743  20.206  282.853 1.00 342.56 ?  182 THR J CB  1 
ATOM   20489 O OG1 . THR K  3 182 ? 64.482  19.063  283.303 1.00 344.88 ?  182 THR J OG1 1 
ATOM   20490 C CG2 . THR K  3 182 ? 62.334  19.777  282.488 1.00 343.67 ?  182 THR J CG2 1 
ATOM   20491 N N   . PRO K  3 183 ? 66.124  22.321  282.609 1.00 340.63 ?  183 PRO J N   1 
ATOM   20492 C CA  . PRO K  3 183 ? 67.493  22.658  283.029 1.00 342.99 ?  183 PRO J CA  1 
ATOM   20493 C C   . PRO K  3 183 ? 68.125  21.594  283.906 1.00 351.22 ?  183 PRO J C   1 
ATOM   20494 O O   . PRO K  3 183 ? 69.356  21.469  283.925 1.00 345.75 ?  183 PRO J O   1 
ATOM   20495 C CB  . PRO K  3 183 ? 67.307  23.986  283.772 1.00 352.61 ?  183 PRO J CB  1 
ATOM   20496 C CG  . PRO K  3 183 ? 66.113  24.596  283.121 1.00 345.11 ?  183 PRO J CG  1 
ATOM   20497 C CD  . PRO K  3 183 ? 65.196  23.451  282.788 1.00 344.42 ?  183 PRO J CD  1 
ATOM   20498 N N   . GLU K  3 184 ? 67.320  20.816  284.634 1.00 351.38 ?  184 GLU J N   1 
ATOM   20499 C CA  . GLU K  3 184 ? 67.885  19.737  285.431 1.00 354.03 ?  184 GLU J CA  1 
ATOM   20500 C C   . GLU K  3 184 ? 68.217  18.538  284.551 1.00 341.97 ?  184 GLU J C   1 
ATOM   20501 O O   . GLU K  3 184 ? 69.203  17.836  284.798 1.00 339.76 ?  184 GLU J O   1 
ATOM   20502 C CB  . GLU K  3 184 ? 66.912  19.328  286.539 1.00 367.20 ?  184 GLU J CB  1 
ATOM   20503 C CG  . GLU K  3 184 ? 66.482  20.458  287.458 1.00 387.07 ?  184 GLU J CG  1 
ATOM   20504 C CD  . GLU K  3 184 ? 65.388  20.030  288.417 1.00 406.72 ?  184 GLU J CD  1 
ATOM   20505 O OE1 . GLU K  3 184 ? 64.906  18.884  288.292 1.00 405.82 ?  184 GLU J OE1 1 
ATOM   20506 O OE2 . GLU K  3 184 ? 65.015  20.833  289.299 1.00 423.48 -1 184 GLU J OE2 1 
ATOM   20507 N N   . GLN K  3 185 ? 67.399  18.284  283.528 1.00 353.08 ?  185 GLN J N   1 
ATOM   20508 C CA  . GLN K  3 185 ? 67.658  17.155  282.642 1.00 343.22 ?  185 GLN J CA  1 
ATOM   20509 C C   . GLN K  3 185 ? 68.913  17.391  281.803 1.00 332.99 ?  185 GLN J C   1 
ATOM   20510 O O   . GLN K  3 185 ? 69.664  16.449  281.521 1.00 326.98 ?  185 GLN J O   1 
ATOM   20511 C CB  . GLN K  3 185 ? 66.439  16.884  281.760 1.00 339.87 ?  185 GLN J CB  1 
ATOM   20512 C CG  . GLN K  3 185 ? 66.583  15.664  280.862 1.00 330.50 ?  185 GLN J CG  1 
ATOM   20513 C CD  . GLN K  3 185 ? 66.413  14.345  281.613 1.00 334.53 ?  185 GLN J CD  1 
ATOM   20514 O OE1 . GLN K  3 185 ? 66.861  14.192  282.752 1.00 341.55 ?  185 GLN J OE1 1 
ATOM   20515 N NE2 . GLN K  3 185 ? 65.766  13.382  280.967 1.00 329.89 ?  185 GLN J NE2 1 
ATOM   20516 N N   . TRP K  3 186 ? 69.144  18.640  281.382 1.00 351.35 ?  186 TRP J N   1 
ATOM   20517 C CA  . TRP K  3 186 ? 70.292  18.964  280.536 1.00 338.75 ?  186 TRP J CA  1 
ATOM   20518 C C   . TRP K  3 186 ? 71.628  18.785  281.244 1.00 343.18 ?  186 TRP J C   1 
ATOM   20519 O O   . TRP K  3 186 ? 72.570  18.217  280.678 1.00 332.14 ?  186 TRP J O   1 
ATOM   20520 C CB  . TRP K  3 186 ? 70.169  20.412  280.063 1.00 336.29 ?  186 TRP J CB  1 
ATOM   20521 C CG  . TRP K  3 186 ? 71.434  20.928  279.465 1.00 330.64 ?  186 TRP J CG  1 
ATOM   20522 C CD1 . TRP K  3 186 ? 72.216  21.919  279.984 1.00 333.76 ?  186 TRP J CD1 1 
ATOM   20523 C CD2 . TRP K  3 186 ? 72.111  20.454  278.298 1.00 317.06 ?  186 TRP J CD2 1 
ATOM   20524 N NE1 . TRP K  3 186 ? 73.323  22.111  279.201 1.00 325.53 ?  186 TRP J NE1 1 
ATOM   20525 C CE2 . TRP K  3 186 ? 73.284  21.226  278.158 1.00 312.42 ?  186 TRP J CE2 1 
ATOM   20526 C CE3 . TRP K  3 186 ? 71.836  19.467  277.347 1.00 303.78 ?  186 TRP J CE3 1 
ATOM   20527 C CZ2 . TRP K  3 186 ? 74.178  21.041  277.109 1.00 295.97 ?  186 TRP J CZ2 1 
ATOM   20528 C CZ3 . TRP K  3 186 ? 72.727  19.286  276.306 1.00 291.44 ?  186 TRP J CZ3 1 
ATOM   20529 C CH2 . TRP K  3 186 ? 73.883  20.068  276.196 1.00 288.73 ?  186 TRP J CH2 1 
ATOM   20530 N N   . LYS K  3 187 ? 71.736  19.256  282.478 1.00 325.44 ?  187 LYS J N   1 
ATOM   20531 C CA  . LYS K  3 187 ? 72.988  19.143  283.216 1.00 327.35 ?  187 LYS J CA  1 
ATOM   20532 C C   . LYS K  3 187 ? 73.183  17.769  283.845 1.00 330.04 ?  187 LYS J C   1 
ATOM   20533 O O   . LYS K  3 187 ? 74.236  17.515  284.438 1.00 331.63 ?  187 LYS J O   1 
ATOM   20534 C CB  . LYS K  3 187 ? 73.096  20.265  284.247 1.00 330.09 ?  187 LYS J CB  1 
ATOM   20535 C CG  . LYS K  3 187 ? 73.218  21.629  283.561 1.00 327.09 ?  187 LYS J CG  1 
ATOM   20536 C CD  . LYS K  3 187 ? 73.727  22.721  284.478 1.00 329.34 ?  187 LYS J CD  1 
ATOM   20537 C CE  . LYS K  3 187 ? 75.249  22.701  284.528 1.00 328.87 ?  187 LYS J CE  1 
ATOM   20538 N NZ  . LYS K  3 187 ? 75.844  22.700  283.156 1.00 324.11 1  187 LYS J NZ  1 
ATOM   20539 N N   . SER K  3 188 ? 72.193  16.888  283.718 1.00 336.22 ?  188 SER J N   1 
ATOM   20540 C CA  . SER K  3 188 ? 72.189  15.549  284.290 1.00 338.07 ?  188 SER J CA  1 
ATOM   20541 C C   . SER K  3 188 ? 73.135  14.632  283.529 1.00 327.84 ?  188 SER J C   1 
ATOM   20542 O O   . SER K  3 188 ? 74.223  14.305  284.009 1.00 327.45 ?  188 SER J O   1 
ATOM   20543 C CB  . SER K  3 188 ? 70.773  14.967  284.269 1.00 341.36 ?  188 SER J CB  1 
ATOM   20544 O OG  . SER K  3 188 ? 69.874  15.772  285.010 1.00 351.54 ?  188 SER J OG  1 
ATOM   20545 N N   . HIS K  3 189 ? 72.724  14.216  282.340 1.00 339.39 ?  189 HIS J N   1 
ATOM   20546 C CA  . HIS K  3 189 ? 73.500  13.282  281.544 1.00 329.86 ?  189 HIS J CA  1 
ATOM   20547 C C   . HIS K  3 189 ? 74.822  13.907  281.096 1.00 324.53 ?  189 HIS J C   1 
ATOM   20548 O O   . HIS K  3 189 ? 75.020  15.125  281.143 1.00 326.72 ?  189 HIS J O   1 
ATOM   20549 C CB  . HIS K  3 189 ? 72.685  12.817  280.345 1.00 323.12 ?  189 HIS J CB  1 
ATOM   20550 C CG  . HIS K  3 189 ? 71.396  12.157  280.724 1.00 328.55 ?  189 HIS J CG  1 
ATOM   20551 N ND1 . HIS K  3 189 ? 70.329  12.855  281.247 1.00 336.72 ?  189 HIS J ND1 1 
ATOM   20552 C CD2 . HIS K  3 189 ? 71.016  10.858  280.691 1.00 327.50 ?  189 HIS J CD2 1 
ATOM   20553 C CE1 . HIS K  3 189 ? 69.336  12.019  281.493 1.00 340.35 ?  189 HIS J CE1 1 
ATOM   20554 N NE2 . HIS K  3 189 ? 69.728  10.801  281.167 1.00 334.78 ?  189 HIS J NE2 1 
ATOM   20555 N N   . LYS K  3 190 ? 75.737  13.040  280.652 1.00 322.81 ?  190 LYS J N   1 
ATOM   20556 C CA  . LYS K  3 190 ? 77.065  13.493  280.249 1.00 319.97 ?  190 LYS J CA  1 
ATOM   20557 C C   . LYS K  3 190 ? 77.004  14.317  278.973 1.00 315.45 ?  190 LYS J C   1 
ATOM   20558 O O   . LYS K  3 190 ? 77.575  15.411  278.897 1.00 314.37 ?  190 LYS J O   1 
ATOM   20559 C CB  . LYS K  3 190 ? 77.962  12.288  279.965 1.00 319.34 ?  190 LYS J CB  1 
ATOM   20560 C CG  . LYS K  3 190 ? 78.274  11.327  281.082 1.00 323.31 ?  190 LYS J CG  1 
ATOM   20561 C CD  . LYS K  3 190 ? 79.224  10.279  280.516 1.00 321.67 ?  190 LYS J CD  1 
ATOM   20562 C CE  . LYS K  3 190 ? 79.586  9.207   281.519 1.00 325.32 ?  190 LYS J CE  1 
ATOM   20563 N NZ  . LYS K  3 190 ? 78.376  8.416   281.917 1.00 327.57 1  190 LYS J NZ  1 
ATOM   20564 N N   . SER K  3 191 ? 76.308  13.810  277.962 1.00 328.35 ?  191 SER J N   1 
ATOM   20565 C CA  . SER K  3 191 ? 76.206  14.480  276.676 1.00 318.17 ?  191 SER J CA  1 
ATOM   20566 C C   . SER K  3 191 ? 74.971  13.962  275.961 1.00 312.75 ?  191 SER J C   1 
ATOM   20567 O O   . SER K  3 191 ? 74.486  12.863  276.243 1.00 316.14 ?  191 SER J O   1 
ATOM   20568 C CB  . SER K  3 191 ? 77.456  14.250  275.816 1.00 307.23 ?  191 SER J CB  1 
ATOM   20569 O OG  . SER K  3 191 ? 78.644  14.294  276.586 1.00 309.68 ?  191 SER J OG  1 
ATOM   20570 N N   . TYR K  3 192 ? 74.461  14.778  275.046 1.00 306.00 ?  192 TYR J N   1 
ATOM   20571 C CA  . TYR K  3 192 ? 73.325  14.414  274.219 1.00 302.94 ?  192 TYR J CA  1 
ATOM   20572 C C   . TYR K  3 192 ? 73.841  14.305  272.787 1.00 293.23 ?  192 TYR J C   1 
ATOM   20573 O O   . TYR K  3 192 ? 74.808  14.975  272.411 1.00 289.92 ?  192 TYR J O   1 
ATOM   20574 C CB  . TYR K  3 192 ? 72.196  15.452  274.345 1.00 307.42 ?  192 TYR J CB  1 
ATOM   20575 C CG  . TYR K  3 192 ? 71.378  15.304  275.622 1.00 317.26 ?  192 TYR J CG  1 
ATOM   20576 C CD1 . TYR K  3 192 ? 71.775  15.937  276.797 1.00 324.64 ?  192 TYR J CD1 1 
ATOM   20577 C CD2 . TYR K  3 192 ? 70.221  14.535  275.656 1.00 319.40 ?  192 TYR J CD2 1 
ATOM   20578 C CE1 . TYR K  3 192 ? 71.049  15.804  277.965 1.00 334.17 ?  192 TYR J CE1 1 
ATOM   20579 C CE2 . TYR K  3 192 ? 69.488  14.398  276.822 1.00 328.85 ?  192 TYR J CE2 1 
ATOM   20580 C CZ  . TYR K  3 192 ? 69.908  15.034  277.971 1.00 336.36 ?  192 TYR J CZ  1 
ATOM   20581 O OH  . TYR K  3 192 ? 69.185  14.901  279.132 1.00 346.34 ?  192 TYR J OH  1 
ATOM   20582 N N   . SER K  3 193 ? 73.193  13.450  271.993 1.00 324.44 ?  193 SER J N   1 
ATOM   20583 C CA  . SER K  3 193 ? 73.565  13.167  270.611 1.00 313.08 ?  193 SER J CA  1 
ATOM   20584 C C   . SER K  3 193 ? 72.355  13.329  269.695 1.00 305.90 ?  193 SER J C   1 
ATOM   20585 O O   . SER K  3 193 ? 71.205  13.226  270.121 1.00 309.76 ?  193 SER J O   1 
ATOM   20586 C CB  . SER K  3 193 ? 74.181  11.754  270.474 1.00 304.48 ?  193 SER J CB  1 
ATOM   20587 O OG  . SER K  3 193 ? 73.585  10.825  271.364 1.00 308.75 ?  193 SER J OG  1 
ATOM   20588 N N   . CYS K  3 194 ? 72.632  13.611  268.424 1.00 320.79 ?  194 CYS J N   1 
ATOM   20589 C CA  . CYS K  3 194 ? 71.615  13.785  267.379 1.00 310.78 ?  194 CYS J CA  1 
ATOM   20590 C C   . CYS K  3 194 ? 71.906  12.805  266.235 1.00 300.66 ?  194 CYS J C   1 
ATOM   20591 O O   . CYS K  3 194 ? 72.697  13.092  265.332 1.00 291.89 ?  194 CYS J O   1 
ATOM   20592 C CB  . CYS K  3 194 ? 71.514  15.281  266.881 1.00 309.08 ?  194 CYS J CB  1 
ATOM   20593 S SG  . CYS K  3 194 ? 70.267  15.405  265.576 1.00 315.45 ?  194 CYS J SG  1 
ATOM   20594 N N   . GLN K  3 195 ? 71.284  11.622  266.304 1.00 311.88 ?  195 GLN J N   1 
ATOM   20595 C CA  . GLN K  3 195 ? 71.476  10.565  265.312 1.00 304.45 ?  195 GLN J CA  1 
ATOM   20596 C C   . GLN K  3 195 ? 70.499  10.777  264.159 1.00 293.02 ?  195 GLN J C   1 
ATOM   20597 O O   . GLN K  3 195 ? 69.280  10.659  264.342 1.00 296.05 ?  195 GLN J O   1 
ATOM   20598 C CB  . GLN K  3 195 ? 71.164  9.213   265.953 1.00 310.15 ?  195 GLN J CB  1 
ATOM   20599 C CG  . GLN K  3 195 ? 71.957  8.031   265.468 1.00 302.56 ?  195 GLN J CG  1 
ATOM   20600 C CD  . GLN K  3 195 ? 73.305  7.930   266.113 1.00 309.83 ?  195 GLN J CD  1 
ATOM   20601 O OE1 . GLN K  3 195 ? 73.677  8.763   266.921 1.00 308.94 ?  195 GLN J OE1 1 
ATOM   20602 N NE2 . GLN K  3 195 ? 74.055  6.910   265.756 1.00 315.39 ?  195 GLN J NE2 1 
ATOM   20603 N N   . VAL K  3 196 ? 71.036  11.097  262.978 1.00 298.36 ?  196 VAL J N   1 
ATOM   20604 C CA  . VAL K  3 196 ? 70.252  11.332  261.766 1.00 293.19 ?  196 VAL J CA  1 
ATOM   20605 C C   . VAL K  3 196 ? 70.445  10.180  260.779 1.00 286.86 ?  196 VAL J C   1 
ATOM   20606 O O   . VAL K  3 196 ? 71.566  9.952   260.304 1.00 283.54 ?  196 VAL J O   1 
ATOM   20607 C CB  . VAL K  3 196 ? 70.646  12.668  261.113 1.00 290.86 ?  196 VAL J CB  1 
ATOM   20608 C CG1 . VAL K  3 196 ? 69.879  12.887  259.814 1.00 287.36 ?  196 VAL J CG1 1 
ATOM   20609 C CG2 . VAL K  3 196 ? 70.429  13.835  262.086 1.00 296.12 ?  196 VAL J CG2 1 
ATOM   20610 N N   . THR K  3 197 ? 69.367  9.457   260.468 1.00 290.50 ?  197 THR J N   1 
ATOM   20611 C CA  . THR K  3 197 ? 69.397  8.344   259.516 1.00 284.39 ?  197 THR J CA  1 
ATOM   20612 C C   . THR K  3 197 ? 68.896  8.830   258.157 1.00 278.39 ?  197 THR J C   1 
ATOM   20613 O O   . THR K  3 197 ? 67.700  9.106   258.008 1.00 278.66 ?  197 THR J O   1 
ATOM   20614 C CB  . THR K  3 197 ? 68.564  7.163   260.001 1.00 285.74 ?  197 THR J CB  1 
ATOM   20615 O OG1 . THR K  3 197 ? 69.051  6.717   261.270 1.00 291.15 ?  197 THR J OG1 1 
ATOM   20616 C CG2 . THR K  3 197 ? 68.637  6.022   258.995 1.00 280.65 ?  197 THR J CG2 1 
ATOM   20617 N N   . HIS K  3 198 ? 69.774  8.938   257.161 1.00 291.46 ?  198 HIS J N   1 
ATOM   20618 C CA  . HIS K  3 198 ? 69.330  9.354   255.833 1.00 285.79 ?  198 HIS J CA  1 
ATOM   20619 C C   . HIS K  3 198 ? 69.696  8.264   254.836 1.00 285.30 ?  198 HIS J C   1 
ATOM   20620 O O   . HIS K  3 198 ? 70.869  7.884   254.738 1.00 286.47 ?  198 HIS J O   1 
ATOM   20621 C CB  . HIS K  3 198 ? 69.958  10.688  255.421 1.00 286.05 ?  198 HIS J CB  1 
ATOM   20622 C CG  . HIS K  3 198 ? 69.635  11.105  254.017 1.00 280.02 ?  198 HIS J CG  1 
ATOM   20623 N ND1 . HIS K  3 198 ? 68.520  10.654  253.342 1.00 273.66 ?  198 HIS J ND1 1 
ATOM   20624 C CD2 . HIS K  3 198 ? 70.267  11.952  253.170 1.00 279.98 ?  198 HIS J CD2 1 
ATOM   20625 C CE1 . HIS K  3 198 ? 68.481  11.204  252.141 1.00 266.15 ?  198 HIS J CE1 1 
ATOM   20626 N NE2 . HIS K  3 198 ? 69.534  11.990  252.009 1.00 270.72 ?  198 HIS J NE2 1 
ATOM   20627 N N   . GLU K  3 199 ? 68.693  7.763   254.109 1.00 294.59 ?  199 GLU J N   1 
ATOM   20628 C CA  . GLU K  3 199 ? 68.875  6.705   253.117 1.00 289.82 ?  199 GLU J CA  1 
ATOM   20629 C C   . GLU K  3 199 ? 69.534  5.484   253.742 1.00 293.66 ?  199 GLU J C   1 
ATOM   20630 O O   . GLU K  3 199 ? 68.866  4.612   254.308 1.00 296.67 ?  199 GLU J O   1 
ATOM   20631 C CB  . GLU K  3 199 ? 69.704  7.178   251.920 1.00 279.16 ?  199 GLU J CB  1 
ATOM   20632 C CG  . GLU K  3 199 ? 69.037  8.216   251.040 1.00 272.45 ?  199 GLU J CG  1 
ATOM   20633 C CD  . GLU K  3 199 ? 67.779  7.726   250.363 1.00 266.46 ?  199 GLU J CD  1 
ATOM   20634 O OE1 . GLU K  3 199 ? 67.900  6.974   249.373 1.00 266.30 ?  199 GLU J OE1 1 
ATOM   20635 O OE2 . GLU K  3 199 ? 66.677  8.129   250.790 1.00 267.97 -1 199 GLU J OE2 1 
ATOM   20636 N N   . GLY K  3 200 ? 70.864  5.437   253.643 1.00 276.21 ?  200 GLY J N   1 
ATOM   20637 C CA  . GLY K  3 200 ? 71.668  4.341   254.144 1.00 276.88 ?  200 GLY J CA  1 
ATOM   20638 C C   . GLY K  3 200 ? 72.744  4.751   255.129 1.00 281.15 ?  200 GLY J C   1 
ATOM   20639 O O   . GLY K  3 200 ? 73.309  3.896   255.819 1.00 282.92 ?  200 GLY J O   1 
ATOM   20640 N N   . SER K  3 201 ? 73.056  6.041   255.204 1.00 269.12 ?  201 SER J N   1 
ATOM   20641 C CA  . SER K  3 201 ? 74.099  6.497   256.109 1.00 273.97 ?  201 SER J CA  1 
ATOM   20642 C C   . SER K  3 201 ? 73.470  7.112   257.355 1.00 279.82 ?  201 SER J C   1 
ATOM   20643 O O   . SER K  3 201 ? 72.282  7.450   257.375 1.00 280.28 ?  201 SER J O   1 
ATOM   20644 C CB  . SER K  3 201 ? 74.999  7.518   255.408 1.00 272.31 ?  201 SER J CB  1 
ATOM   20645 O OG  . SER K  3 201 ? 75.954  8.064   256.297 1.00 276.40 ?  201 SER J OG  1 
ATOM   20646 N N   . THR K  3 202 ? 74.283  7.254   258.405 1.00 278.78 ?  202 THR J N   1 
ATOM   20647 C CA  . THR K  3 202 ? 73.814  7.830   259.665 1.00 290.22 ?  202 THR J CA  1 
ATOM   20648 C C   . THR K  3 202 ? 74.876  8.735   260.281 1.00 296.42 ?  202 THR J C   1 
ATOM   20649 O O   . THR K  3 202 ? 75.925  8.250   260.717 1.00 299.61 ?  202 THR J O   1 
ATOM   20650 C CB  . THR K  3 202 ? 73.421  6.721   260.640 1.00 291.94 ?  202 THR J CB  1 
ATOM   20651 O OG1 . THR K  3 202 ? 72.366  5.941   260.064 1.00 288.81 ?  202 THR J OG1 1 
ATOM   20652 C CG2 . THR K  3 202 ? 72.932  7.315   261.951 1.00 294.59 ?  202 THR J CG2 1 
ATOM   20653 N N   . VAL K  3 203 ? 74.606  10.041  260.317 1.00 288.01 ?  203 VAL J N   1 
ATOM   20654 C CA  . VAL K  3 203 ? 75.507  11.046  260.883 1.00 286.65 ?  203 VAL J CA  1 
ATOM   20655 C C   . VAL K  3 203 ? 75.106  11.336  262.326 1.00 293.75 ?  203 VAL J C   1 
ATOM   20656 O O   . VAL K  3 203 ? 73.915  11.491  262.629 1.00 296.02 ?  203 VAL J O   1 
ATOM   20657 C CB  . VAL K  3 203 ? 75.514  12.332  260.037 1.00 281.41 ?  203 VAL J CB  1 
ATOM   20658 C CG1 . VAL K  3 203 ? 76.559  13.303  260.565 1.00 283.96 ?  203 VAL J CG1 1 
ATOM   20659 C CG2 . VAL K  3 203 ? 75.785  12.000  258.575 1.00 274.80 ?  203 VAL J CG2 1 
ATOM   20660 N N   . GLU K  3 204 ? 76.095  11.404  263.223 1.00 285.91 ?  204 GLU J N   1 
ATOM   20661 C CA  . GLU K  3 204 ? 75.874  11.653  264.646 1.00 294.64 ?  204 GLU J CA  1 
ATOM   20662 C C   . GLU K  3 204 ? 76.710  12.833  265.126 1.00 302.35 ?  204 GLU J C   1 
ATOM   20663 O O   . GLU K  3 204 ? 77.932  12.846  264.943 1.00 304.85 ?  204 GLU J O   1 
ATOM   20664 C CB  . GLU K  3 204 ? 76.215  10.431  265.508 1.00 300.13 ?  204 GLU J CB  1 
ATOM   20665 C CG  . GLU K  3 204 ? 76.180  10.758  267.002 1.00 312.20 ?  204 GLU J CG  1 
ATOM   20666 C CD  . GLU K  3 204 ? 76.548  9.590   267.894 1.00 323.52 ?  204 GLU J CD  1 
ATOM   20667 O OE1 . GLU K  3 204 ? 76.638  8.451   267.390 1.00 326.98 ?  204 GLU J OE1 1 
ATOM   20668 O OE2 . GLU K  3 204 ? 76.742  9.816   269.108 1.00 330.29 -1 204 GLU J OE2 1 
ATOM   20669 N N   . LYS K  3 205 ? 76.051  13.821  265.738 1.00 286.90 ?  205 LYS J N   1 
ATOM   20670 C CA  . LYS K  3 205 ? 76.721  14.963  266.347 1.00 290.21 ?  205 LYS J CA  1 
ATOM   20671 C C   . LYS K  3 205 ? 76.314  15.040  267.812 1.00 298.16 ?  205 LYS J C   1 
ATOM   20672 O O   . LYS K  3 205 ? 75.141  14.849  268.146 1.00 301.39 ?  205 LYS J O   1 
ATOM   20673 C CB  . LYS K  3 205 ? 76.335  16.266  265.646 1.00 287.65 ?  205 LYS J CB  1 
ATOM   20674 C CG  . LYS K  3 205 ? 76.989  16.471  264.302 1.00 282.01 ?  205 LYS J CG  1 
ATOM   20675 C CD  . LYS K  3 205 ? 76.695  17.862  263.788 1.00 276.64 ?  205 LYS J CD  1 
ATOM   20676 C CE  . LYS K  3 205 ? 77.485  18.169  262.528 1.00 272.21 ?  205 LYS J CE  1 
ATOM   20677 N NZ  . LYS K  3 205 ? 78.962  18.156  262.713 1.00 273.78 1  205 LYS J NZ  1 
ATOM   20678 N N   . THR K  3 206 ? 77.281  15.329  268.684 1.00 290.87 ?  206 THR J N   1 
ATOM   20679 C CA  . THR K  3 206 ? 77.053  15.342  270.124 1.00 298.69 ?  206 THR J CA  1 
ATOM   20680 C C   . THR K  3 206 ? 77.160  16.760  270.691 1.00 302.70 ?  206 THR J C   1 
ATOM   20681 O O   . THR K  3 206 ? 77.479  17.722  269.983 1.00 299.09 ?  206 THR J O   1 
ATOM   20682 C CB  . THR K  3 206 ? 78.023  14.381  270.822 1.00 300.12 ?  206 THR J CB  1 
ATOM   20683 O OG1 . THR K  3 206 ? 79.370  14.849  270.676 1.00 301.99 ?  206 THR J OG1 1 
ATOM   20684 C CG2 . THR K  3 206 ? 77.911  12.982  270.224 1.00 295.93 ?  206 THR J CG2 1 
ATOM   20685 N N   . VAL K  3 207 ? 76.906  16.871  271.996 1.00 289.72 ?  207 VAL J N   1 
ATOM   20686 C CA  . VAL K  3 207 ? 76.977  18.140  272.718 1.00 291.26 ?  207 VAL J CA  1 
ATOM   20687 C C   . VAL K  3 207 ? 77.173  17.846  274.202 1.00 296.05 ?  207 VAL J C   1 
ATOM   20688 O O   . VAL K  3 207 ? 76.518  16.965  274.764 1.00 298.58 ?  207 VAL J O   1 
ATOM   20689 C CB  . VAL K  3 207 ? 75.718  19.007  272.471 1.00 290.50 ?  207 VAL J CB  1 
ATOM   20690 C CG1 . VAL K  3 207 ? 74.438  18.236  272.814 1.00 292.55 ?  207 VAL J CG1 1 
ATOM   20691 C CG2 . VAL K  3 207 ? 75.804  20.310  273.261 1.00 292.26 ?  207 VAL J CG2 1 
ATOM   20692 N N   . ALA K  3 208 ? 78.067  18.602  274.839 1.00 290.55 ?  208 ALA J N   1 
ATOM   20693 C CA  . ALA K  3 208 ? 78.385  18.425  276.249 1.00 301.93 ?  208 ALA J CA  1 
ATOM   20694 C C   . ALA K  3 208 ? 78.215  19.754  276.970 1.00 312.10 ?  208 ALA J C   1 
ATOM   20695 O O   . ALA K  3 208 ? 78.593  20.802  276.431 1.00 310.06 ?  208 ALA J O   1 
ATOM   20696 C CB  . ALA K  3 208 ? 79.817  17.907  276.449 1.00 295.76 ?  208 ALA J CB  1 
ATOM   20697 N N   . PRO K  3 209 ? 77.649  19.756  278.175 1.00 297.49 ?  209 PRO J N   1 
ATOM   20698 C CA  . PRO K  3 209 ? 77.507  21.015  278.914 1.00 306.48 ?  209 PRO J CA  1 
ATOM   20699 C C   . PRO K  3 209 ? 78.869  21.578  279.288 1.00 313.36 ?  209 PRO J C   1 
ATOM   20700 O O   . PRO K  3 209 ? 79.903  20.912  279.201 1.00 312.82 ?  209 PRO J O   1 
ATOM   20701 C CB  . PRO K  3 209 ? 76.704  20.616  280.158 1.00 313.50 ?  209 PRO J CB  1 
ATOM   20702 C CG  . PRO K  3 209 ? 76.041  19.326  279.790 1.00 308.70 ?  209 PRO J CG  1 
ATOM   20703 C CD  . PRO K  3 209 ? 77.009  18.633  278.879 1.00 299.58 ?  209 PRO J CD  1 
ATOM   20704 N N   . THR K  3 210 ? 78.859  22.833  279.723 1.00 300.29 ?  210 THR J N   1 
ATOM   20705 C CA  . THR K  3 210 ? 80.095  23.505  280.106 1.00 300.75 ?  210 THR J CA  1 
ATOM   20706 C C   . THR K  3 210 ? 80.089  23.937  281.572 1.00 305.31 ?  210 THR J C   1 
ATOM   20707 O O   . THR K  3 210 ? 79.060  23.886  282.248 1.00 307.92 ?  210 THR J O   1 
ATOM   20708 C CB  . THR K  3 210 ? 80.358  24.737  279.216 1.00 297.17 ?  210 THR J CB  1 
ATOM   20709 O OG1 . THR K  3 210 ? 80.417  24.334  277.842 1.00 292.90 ?  210 THR J OG1 1 
ATOM   20710 C CG2 . THR K  3 210 ? 81.677  25.389  279.593 1.00 297.63 ?  210 THR J CG2 1 
ATOM   20711 N N   . GLN L  6 1   ? 53.841  48.486  213.839 1.00 219.18 ?  1   GLN K N   1 
ATOM   20712 C CA  . GLN L  6 1   ? 54.945  47.898  213.091 1.00 218.43 ?  1   GLN K CA  1 
ATOM   20713 C C   . GLN L  6 1   ? 55.697  48.972  212.301 1.00 217.59 ?  1   GLN K C   1 
ATOM   20714 O O   . GLN L  6 1   ? 55.097  49.947  211.852 1.00 218.10 ?  1   GLN K O   1 
ATOM   20715 C CB  . GLN L  6 1   ? 54.380  46.798  212.193 1.00 219.68 ?  1   GLN K CB  1 
ATOM   20716 C CG  . GLN L  6 1   ? 53.336  47.301  211.207 1.00 220.97 ?  1   GLN K CG  1 
ATOM   20717 C CD  . GLN L  6 1   ? 52.180  46.327  211.047 1.00 225.20 ?  1   GLN K CD  1 
ATOM   20718 O OE1 . GLN L  6 1   ? 52.361  45.186  210.628 1.00 228.41 ?  1   GLN K OE1 1 
ATOM   20719 N NE2 . GLN L  6 1   ? 50.978  46.778  211.399 1.00 228.05 ?  1   GLN K NE2 1 
ATOM   20720 N N   . VAL L  6 2   ? 57.011  48.798  212.149 1.00 218.37 ?  2   VAL K N   1 
ATOM   20721 C CA  . VAL L  6 2   ? 57.866  49.745  211.433 1.00 217.55 ?  2   VAL K CA  1 
ATOM   20722 C C   . VAL L  6 2   ? 58.473  49.124  210.177 1.00 217.69 ?  2   VAL K C   1 
ATOM   20723 O O   . VAL L  6 2   ? 59.299  48.205  210.271 1.00 217.18 ?  2   VAL K O   1 
ATOM   20724 C CB  . VAL L  6 2   ? 58.979  50.286  212.343 1.00 216.00 ?  2   VAL K CB  1 
ATOM   20725 C CG1 . VAL L  6 2   ? 59.883  51.245  211.573 1.00 215.25 ?  2   VAL K CG1 1 
ATOM   20726 C CG2 . VAL L  6 2   ? 58.386  50.953  213.589 1.00 215.86 ?  2   VAL K CG2 1 
ATOM   20727 N N   . HIS L  6 3   ? 58.079  49.623  209.003 1.00 234.98 ?  3   HIS K N   1 
ATOM   20728 C CA  . HIS L  6 3   ? 58.600  49.137  207.731 1.00 234.82 ?  3   HIS K CA  1 
ATOM   20729 C C   . HIS L  6 3   ? 59.326  50.274  207.029 1.00 232.77 ?  3   HIS K C   1 
ATOM   20730 O O   . HIS L  6 3   ? 58.763  51.362  206.863 1.00 232.45 ?  3   HIS K O   1 
ATOM   20731 C CB  . HIS L  6 3   ? 57.509  48.591  206.807 1.00 240.71 ?  3   HIS K CB  1 
ATOM   20732 C CG  . HIS L  6 3   ? 58.055  48.014  205.538 1.00 244.37 ?  3   HIS K CG  1 
ATOM   20733 N ND1 . HIS L  6 3   ? 58.909  46.933  205.529 1.00 246.73 ?  3   HIS K ND1 1 
ATOM   20734 C CD2 . HIS L  6 3   ? 57.881  48.367  204.242 1.00 245.36 ?  3   HIS K CD2 1 
ATOM   20735 C CE1 . HIS L  6 3   ? 59.244  46.648  204.283 1.00 244.27 ?  3   HIS K CE1 1 
ATOM   20736 N NE2 . HIS L  6 3   ? 58.629  47.500  203.482 1.00 243.38 ?  3   HIS K NE2 1 
ATOM   20737 N N   . LEU L  6 4   ? 60.566  50.026  206.613 1.00 227.12 ?  4   LEU K N   1 
ATOM   20738 C CA  . LEU L  6 4   ? 61.362  51.021  205.910 1.00 226.64 ?  4   LEU K CA  1 
ATOM   20739 C C   . LEU L  6 4   ? 61.756  50.497  204.538 1.00 227.19 ?  4   LEU K C   1 
ATOM   20740 O O   . LEU L  6 4   ? 62.155  49.336  204.405 1.00 227.22 ?  4   LEU K O   1 
ATOM   20741 C CB  . LEU L  6 4   ? 62.626  51.377  206.698 1.00 225.18 ?  4   LEU K CB  1 
ATOM   20742 C CG  . LEU L  6 4   ? 62.410  51.876  208.125 1.00 224.48 ?  4   LEU K CG  1 
ATOM   20743 C CD1 . LEU L  6 4   ? 63.738  52.219  208.776 1.00 223.07 ?  4   LEU K CD1 1 
ATOM   20744 C CD2 . LEU L  6 4   ? 61.477  53.070  208.142 1.00 224.95 ?  4   LEU K CD2 1 
ATOM   20745 N N   . GLN L  6 5   ? 61.639  51.345  203.518 1.00 230.16 ?  5   GLN K N   1 
ATOM   20746 C CA  . GLN L  6 5   ? 61.995  50.943  202.163 1.00 232.36 ?  5   GLN K CA  1 
ATOM   20747 C C   . GLN L  6 5   ? 62.807  52.079  201.557 1.00 236.29 ?  5   GLN K C   1 
ATOM   20748 O O   . GLN L  6 5   ? 62.342  53.222  201.522 1.00 237.26 ?  5   GLN K O   1 
ATOM   20749 C CB  . GLN L  6 5   ? 60.744  50.644  201.326 1.00 238.28 ?  5   GLN K CB  1 
ATOM   20750 C CG  . GLN L  6 5   ? 60.999  50.243  199.875 1.00 246.65 ?  5   GLN K CG  1 
ATOM   20751 C CD  . GLN L  6 5   ? 61.687  48.891  199.757 1.00 245.49 ?  5   GLN K CD  1 
ATOM   20752 O OE1 . GLN L  6 5   ? 61.641  48.075  200.680 1.00 243.93 ?  5   GLN K OE1 1 
ATOM   20753 N NE2 . GLN L  6 5   ? 62.308  48.638  198.609 1.00 249.22 ?  5   GLN K NE2 1 
ATOM   20754 N N   . GLU L  6 6   ? 64.005  51.767  201.080 1.00 240.03 ?  6   GLU K N   1 
ATOM   20755 C CA  . GLU L  6 6   ? 64.890  52.722  200.428 1.00 242.67 ?  6   GLU K CA  1 
ATOM   20756 C C   . GLU L  6 6   ? 64.769  52.563  198.919 1.00 247.64 ?  6   GLU K C   1 
ATOM   20757 O O   . GLU L  6 6   ? 64.514  51.467  198.414 1.00 249.63 ?  6   GLU K O   1 
ATOM   20758 C CB  . GLU L  6 6   ? 66.340  52.590  200.896 1.00 239.74 ?  6   GLU K CB  1 
ATOM   20759 C CG  . GLU L  6 6   ? 66.810  51.202  201.224 1.00 236.88 ?  6   GLU K CG  1 
ATOM   20760 C CD  . GLU L  6 6   ? 66.401  50.735  202.613 1.00 236.86 ?  6   GLU K CD  1 
ATOM   20761 O OE1 . GLU L  6 6   ? 65.292  51.087  203.060 1.00 239.96 ?  6   GLU K OE1 1 
ATOM   20762 O OE2 . GLU L  6 6   ? 67.198  50.030  203.267 1.00 235.02 -1 6   GLU K OE2 1 
ATOM   20763 N N   . SER L  6 7   ? 64.951  53.665  198.197 1.00 237.43 ?  7   SER K N   1 
ATOM   20764 C CA  . SER L  6 7   ? 64.837  53.614  196.747 1.00 241.24 ?  7   SER K CA  1 
ATOM   20765 C C   . SER L  6 7   ? 65.689  54.684  196.086 1.00 244.99 ?  7   SER K C   1 
ATOM   20766 O O   . SER L  6 7   ? 65.640  55.856  196.476 1.00 245.83 ?  7   SER K O   1 
ATOM   20767 C CB  . SER L  6 7   ? 63.377  53.784  196.321 1.00 238.77 ?  7   SER K CB  1 
ATOM   20768 O OG  . SER L  6 7   ? 62.861  55.010  196.808 1.00 240.08 ?  7   SER K OG  1 
ATOM   20769 N N   . GLY L  6 8   ? 66.475  54.262  195.092 1.00 231.36 ?  8   GLY K N   1 
ATOM   20770 C CA  . GLY L  6 8   ? 67.341  55.157  194.363 1.00 235.11 ?  8   GLY K CA  1 
ATOM   20771 C C   . GLY L  6 8   ? 67.545  54.764  192.910 1.00 240.43 ?  8   GLY K C   1 
ATOM   20772 O O   . GLY L  6 8   ? 66.878  53.870  192.378 1.00 246.90 ?  8   GLY K O   1 
ATOM   20773 N N   . PRO L  6 9   ? 68.486  55.437  192.238 1.00 240.98 ?  9   PRO K N   1 
ATOM   20774 C CA  . PRO L  6 9   ? 68.726  55.134  190.813 1.00 242.11 ?  9   PRO K CA  1 
ATOM   20775 C C   . PRO L  6 9   ? 69.380  53.794  190.528 1.00 242.10 ?  9   PRO K C   1 
ATOM   20776 O O   . PRO L  6 9   ? 68.955  53.094  189.600 1.00 243.08 ?  9   PRO K O   1 
ATOM   20777 C CB  . PRO L  6 9   ? 69.626  56.295  190.365 1.00 242.17 ?  9   PRO K CB  1 
ATOM   20778 C CG  . PRO L  6 9   ? 70.303  56.741  191.607 1.00 240.82 ?  9   PRO K CG  1 
ATOM   20779 C CD  . PRO L  6 9   ? 69.316  56.553  192.717 1.00 240.23 ?  9   PRO K CD  1 
ATOM   20780 N N   . GLY L  6 10  ? 70.400  53.407  191.294 1.00 251.91 ?  10  GLY K N   1 
ATOM   20781 C CA  . GLY L  6 10  ? 71.115  52.173  191.075 1.00 248.51 ?  10  GLY K CA  1 
ATOM   20782 C C   . GLY L  6 10  ? 72.384  52.340  190.256 1.00 252.71 ?  10  GLY K C   1 
ATOM   20783 O O   . GLY L  6 10  ? 73.352  51.602  190.472 1.00 252.58 ?  10  GLY K O   1 
ATOM   20784 N N   . LEU L  6 11  ? 72.390  53.277  189.307 1.00 235.09 ?  11  LEU K N   1 
ATOM   20785 C CA  . LEU L  6 11  ? 73.542  53.568  188.456 1.00 241.54 ?  11  LEU K CA  1 
ATOM   20786 C C   . LEU L  6 11  ? 73.727  55.077  188.427 1.00 246.91 ?  11  LEU K C   1 
ATOM   20787 O O   . LEU L  6 11  ? 72.804  55.805  188.045 1.00 249.43 ?  11  LEU K O   1 
ATOM   20788 C CB  . LEU L  6 11  ? 73.368  53.023  187.035 1.00 245.66 ?  11  LEU K CB  1 
ATOM   20789 C CG  . LEU L  6 11  ? 74.528  53.344  186.086 1.00 251.77 ?  11  LEU K CG  1 
ATOM   20790 C CD1 . LEU L  6 11  ? 75.821  52.758  186.624 1.00 253.30 ?  11  LEU K CD1 1 
ATOM   20791 C CD2 . LEU L  6 11  ? 74.252  52.819  184.688 1.00 255.43 ?  11  LEU K CD2 1 
ATOM   20792 N N   . VAL L  6 12  ? 74.909  55.552  188.817 1.00 244.07 ?  12  VAL K N   1 
ATOM   20793 C CA  . VAL L  6 12  ? 75.192  56.983  188.850 1.00 250.13 ?  12  VAL K CA  1 
ATOM   20794 C C   . VAL L  6 12  ? 76.497  57.249  188.113 1.00 257.83 ?  12  VAL K C   1 
ATOM   20795 O O   . VAL L  6 12  ? 77.520  56.613  188.393 1.00 254.83 ?  12  VAL K O   1 
ATOM   20796 C CB  . VAL L  6 12  ? 75.277  57.518  190.292 1.00 246.10 ?  12  VAL K CB  1 
ATOM   20797 C CG1 . VAL L  6 12  ? 75.591  58.997  190.275 1.00 250.82 ?  12  VAL K CG1 1 
ATOM   20798 C CG2 . VAL L  6 12  ? 73.981  57.251  191.043 1.00 237.40 ?  12  VAL K CG2 1 
ATOM   20799 N N   . LYS L  6 13  ? 76.451  58.190  187.170 1.00 252.56 ?  13  LYS K N   1 
ATOM   20800 C CA  . LYS L  6 13  ? 77.617  58.570  186.389 1.00 256.14 ?  13  LYS K CA  1 
ATOM   20801 C C   . LYS L  6 13  ? 78.659  59.248  187.284 1.00 256.96 ?  13  LYS K C   1 
ATOM   20802 O O   . LYS L  6 13  ? 78.314  59.844  188.307 1.00 256.30 ?  13  LYS K O   1 
ATOM   20803 C CB  . LYS L  6 13  ? 77.198  59.516  185.268 1.00 257.66 ?  13  LYS K CB  1 
ATOM   20804 C CG  . LYS L  6 13  ? 76.020  58.992  184.443 1.00 250.66 ?  13  LYS K CG  1 
ATOM   20805 C CD  . LYS L  6 13  ? 76.243  57.649  183.771 1.00 249.80 ?  13  LYS K CD  1 
ATOM   20806 C CE  . LYS L  6 13  ? 77.038  57.765  182.492 1.00 256.46 ?  13  LYS K CE  1 
ATOM   20807 N NZ  . LYS L  6 13  ? 77.195  56.422  181.869 1.00 263.49 1  13  LYS K NZ  1 
ATOM   20808 N N   . PRO L  6 14  ? 79.941  59.169  186.925 1.00 243.69 ?  14  PRO K N   1 
ATOM   20809 C CA  . PRO L  6 14  ? 80.971  59.855  187.719 1.00 244.82 ?  14  PRO K CA  1 
ATOM   20810 C C   . PRO L  6 14  ? 80.782  61.368  187.770 1.00 252.57 ?  14  PRO K C   1 
ATOM   20811 O O   . PRO L  6 14  ? 80.245  61.984  186.846 1.00 256.50 ?  14  PRO K O   1 
ATOM   20812 C CB  . PRO L  6 14  ? 82.274  59.483  187.000 1.00 242.46 ?  14  PRO K CB  1 
ATOM   20813 C CG  . PRO L  6 14  ? 81.964  58.190  186.309 1.00 238.84 ?  14  PRO K CG  1 
ATOM   20814 C CD  . PRO L  6 14  ? 80.528  58.309  185.882 1.00 242.44 ?  14  PRO K CD  1 
ATOM   20815 N N   . SER L  6 15  ? 81.239  61.963  188.881 1.00 258.44 ?  15  SER K N   1 
ATOM   20816 C CA  . SER L  6 15  ? 81.154  63.411  189.113 1.00 261.52 ?  15  SER K CA  1 
ATOM   20817 C C   . SER L  6 15  ? 79.721  63.936  189.022 1.00 260.51 ?  15  SER K C   1 
ATOM   20818 O O   . SER L  6 15  ? 79.479  65.037  188.524 1.00 263.48 ?  15  SER K O   1 
ATOM   20819 C CB  . SER L  6 15  ? 82.066  64.174  188.148 1.00 266.40 ?  15  SER K CB  1 
ATOM   20820 O OG  . SER L  6 15  ? 83.323  63.535  187.996 1.00 266.83 ?  15  SER K OG  1 
ATOM   20821 N N   . GLU L  6 16  ? 78.761  63.156  189.504 1.00 254.69 ?  16  GLU K N   1 
ATOM   20822 C CA  . GLU L  6 16  ? 77.363  63.568  189.488 1.00 253.36 ?  16  GLU K CA  1 
ATOM   20823 C C   . GLU L  6 16  ? 76.806  63.654  190.913 1.00 252.24 ?  16  GLU K C   1 
ATOM   20824 O O   . GLU L  6 16  ? 77.545  63.562  191.898 1.00 252.12 ?  16  GLU K O   1 
ATOM   20825 C CB  . GLU L  6 16  ? 76.567  62.606  188.609 1.00 252.90 ?  16  GLU K CB  1 
ATOM   20826 C CG  . GLU L  6 16  ? 75.400  63.233  187.891 1.00 255.64 ?  16  GLU K CG  1 
ATOM   20827 C CD  . GLU L  6 16  ? 74.640  62.219  187.076 1.00 255.37 ?  16  GLU K CD  1 
ATOM   20828 O OE1 . GLU L  6 16  ? 75.038  61.035  187.083 1.00 252.45 ?  16  GLU K OE1 1 
ATOM   20829 O OE2 . GLU L  6 16  ? 73.646  62.602  186.427 1.00 259.61 -1 16  GLU K OE2 1 
ATOM   20830 N N   . THR L  6 17  ? 75.485  63.840  191.015 1.00 254.61 ?  17  THR K N   1 
ATOM   20831 C CA  . THR L  6 17  ? 74.792  63.966  192.296 1.00 248.11 ?  17  THR K CA  1 
ATOM   20832 C C   . THR L  6 17  ? 73.807  62.818  192.509 1.00 238.91 ?  17  THR K C   1 
ATOM   20833 O O   . THR L  6 17  ? 72.777  62.740  191.829 1.00 240.16 ?  17  THR K O   1 
ATOM   20834 C CB  . THR L  6 17  ? 74.058  65.306  192.372 1.00 249.15 ?  17  THR K CB  1 
ATOM   20835 O OG1 . THR L  6 17  ? 74.999  66.381  192.259 1.00 257.44 ?  17  THR K OG1 1 
ATOM   20836 C CG2 . THR L  6 17  ? 73.294  65.427  193.682 1.00 252.68 ?  17  THR K CG2 1 
ATOM   20837 N N   . LEU L  6 18  ? 74.133  61.936  193.454 1.00 235.19 ?  18  LEU K N   1 
ATOM   20838 C CA  . LEU L  6 18  ? 73.287  60.809  193.835 1.00 234.99 ?  18  LEU K CA  1 
ATOM   20839 C C   . LEU L  6 18  ? 72.128  61.274  194.712 1.00 234.60 ?  18  LEU K C   1 
ATOM   20840 O O   . LEU L  6 18  ? 72.335  62.030  195.666 1.00 233.71 ?  18  LEU K O   1 
ATOM   20841 C CB  . LEU L  6 18  ? 74.109  59.756  194.578 1.00 234.02 ?  18  LEU K CB  1 
ATOM   20842 C CG  . LEU L  6 18  ? 73.330  58.667  195.321 1.00 233.56 ?  18  LEU K CG  1 
ATOM   20843 C CD1 . LEU L  6 18  ? 72.522  57.817  194.356 1.00 234.66 ?  18  LEU K CD1 1 
ATOM   20844 C CD2 . LEU L  6 18  ? 74.274  57.804  196.143 1.00 232.58 ?  18  LEU K CD2 1 
ATOM   20845 N N   . SER L  6 19  ? 70.910  60.839  194.393 1.00 216.99 ?  19  SER K N   1 
ATOM   20846 C CA  . SER L  6 19  ? 69.738  61.192  195.189 1.00 216.80 ?  19  SER K CA  1 
ATOM   20847 C C   . SER L  6 19  ? 69.009  59.920  195.602 1.00 216.69 ?  19  SER K C   1 
ATOM   20848 O O   . SER L  6 19  ? 68.628  59.117  194.743 1.00 217.57 ?  19  SER K O   1 
ATOM   20849 C CB  . SER L  6 19  ? 68.801  62.124  194.414 1.00 218.04 ?  19  SER K CB  1 
ATOM   20850 O OG  . SER L  6 19  ? 67.716  62.549  195.222 1.00 217.93 ?  19  SER K OG  1 
ATOM   20851 N N   . LEU L  6 20  ? 68.818  59.736  196.910 1.00 231.64 ?  20  LEU K N   1 
ATOM   20852 C CA  . LEU L  6 20  ? 68.147  58.561  197.455 1.00 227.38 ?  20  LEU K CA  1 
ATOM   20853 C C   . LEU L  6 20  ? 66.968  58.991  198.328 1.00 226.22 ?  20  LEU K C   1 
ATOM   20854 O O   . LEU L  6 20  ? 66.895  60.136  198.785 1.00 226.67 ?  20  LEU K O   1 
ATOM   20855 C CB  . LEU L  6 20  ? 69.113  57.695  198.281 1.00 225.55 ?  20  LEU K CB  1 
ATOM   20856 C CG  . LEU L  6 20  ? 70.338  57.094  197.581 1.00 228.45 ?  20  LEU K CG  1 
ATOM   20857 C CD1 . LEU L  6 20  ? 71.216  56.346  198.572 1.00 226.43 ?  20  LEU K CD1 1 
ATOM   20858 C CD2 . LEU L  6 20  ? 69.937  56.177  196.444 1.00 229.07 ?  20  LEU K CD2 1 
ATOM   20859 N N   . THR L  6 21  ? 66.035  58.055  198.554 1.00 232.84 ?  21  THR K N   1 
ATOM   20860 C CA  . THR L  6 21  ? 64.830  58.302  199.344 1.00 230.24 ?  21  THR K CA  1 
ATOM   20861 C C   . THR L  6 21  ? 64.441  57.066  200.152 1.00 226.71 ?  21  THR K C   1 
ATOM   20862 O O   . THR L  6 21  ? 64.426  55.959  199.603 1.00 226.32 ?  21  THR K O   1 
ATOM   20863 C CB  . THR L  6 21  ? 63.668  58.728  198.441 1.00 231.68 ?  21  THR K CB  1 
ATOM   20864 O OG1 . THR L  6 21  ? 64.051  59.882  197.678 1.00 234.48 ?  21  THR K OG1 1 
ATOM   20865 C CG2 . THR L  6 21  ? 62.469  59.093  199.296 1.00 232.94 ?  21  THR K CG2 1 
ATOM   20866 N N   . CYS L  6 22  ? 64.159  57.247  201.462 1.00 248.56 ?  22  CYS K N   1 
ATOM   20867 C CA  . CYS L  6 22  ? 63.745  56.173  202.392 1.00 248.08 ?  22  CYS K CA  1 
ATOM   20868 C C   . CYS L  6 22  ? 62.292  56.330  202.793 1.00 248.85 ?  22  CYS K C   1 
ATOM   20869 O O   . CYS L  6 22  ? 61.923  57.142  203.649 1.00 248.62 ?  22  CYS K O   1 
ATOM   20870 C CB  . CYS L  6 22  ? 64.645  56.190  203.617 1.00 246.56 ?  22  CYS K CB  1 
ATOM   20871 S SG  . CYS L  6 22  ? 64.205  54.972  204.865 1.00 251.45 ?  22  CYS K SG  1 
ATOM   20872 N N   . ASN L  6 23  ? 61.462  55.623  202.120 1.00 244.54 ?  23  ASN K N   1 
ATOM   20873 C CA  . ASN L  6 23  ? 60.045  55.674  202.402 1.00 244.77 ?  23  ASN K CA  1 
ATOM   20874 C C   . ASN L  6 23  ? 59.704  54.950  203.722 1.00 239.14 ?  23  ASN K C   1 
ATOM   20875 O O   . ASN L  6 23  ? 59.955  53.751  203.905 1.00 236.44 ?  23  ASN K O   1 
ATOM   20876 C CB  . ASN L  6 23  ? 59.489  55.176  201.100 1.00 255.23 ?  23  ASN K CB  1 
ATOM   20877 C CG  . ASN L  6 23  ? 58.354  55.983  200.560 1.00 262.66 ?  23  ASN K CG  1 
ATOM   20878 O OD1 . ASN L  6 23  ? 57.596  56.638  201.277 1.00 261.12 ?  23  ASN K OD1 1 
ATOM   20879 N ND2 . ASN L  6 23  ? 58.280  56.034  199.254 1.00 284.26 ?  23  ASN K ND2 1 
ATOM   20880 N N   . VAL L  6 24  ? 59.154  55.708  204.647 1.00 242.83 ?  24  VAL K N   1 
ATOM   20881 C CA  . VAL L  6 24  ? 58.863  55.223  205.983 1.00 239.85 ?  24  VAL K CA  1 
ATOM   20882 C C   . VAL L  6 24  ? 57.369  54.999  206.131 1.00 240.98 ?  24  VAL K C   1 
ATOM   20883 O O   . VAL L  6 24  ? 56.557  55.858  205.763 1.00 243.32 ?  24  VAL K O   1 
ATOM   20884 C CB  . VAL L  6 24  ? 59.367  56.238  207.016 1.00 238.49 ?  24  VAL K CB  1 
ATOM   20885 C CG1 . VAL L  6 24  ? 59.084  55.766  208.392 1.00 234.38 ?  24  VAL K CG1 1 
ATOM   20886 C CG2 . VAL L  6 24  ? 60.852  56.538  206.806 1.00 242.61 ?  24  VAL K CG2 1 
ATOM   20887 N N   . SER L  6 25  ? 57.032  53.833  206.650 1.00 240.96 ?  25  SER K N   1 
ATOM   20888 C CA  . SER L  6 25  ? 55.670  53.449  206.942 1.00 243.81 ?  25  SER K CA  1 
ATOM   20889 C C   . SER L  6 25  ? 55.681  52.807  208.318 1.00 242.32 ?  25  SER K C   1 
ATOM   20890 O O   . SER L  6 25  ? 56.531  51.958  208.603 1.00 246.09 ?  25  SER K O   1 
ATOM   20891 C CB  . SER L  6 25  ? 55.122  52.482  205.891 1.00 251.50 ?  25  SER K CB  1 
ATOM   20892 O OG  . SER L  6 25  ? 55.135  53.070  204.602 1.00 255.14 ?  25  SER K OG  1 
ATOM   20893 N N   . GLY L  6 26  ? 54.751  53.224  209.165 1.00 241.65 ?  26  GLY K N   1 
ATOM   20894 C CA  . GLY L  6 26  ? 54.610  52.702  210.508 1.00 241.33 ?  26  GLY K CA  1 
ATOM   20895 C C   . GLY L  6 26  ? 54.949  53.696  211.592 1.00 240.52 ?  26  GLY K C   1 
ATOM   20896 O O   . GLY L  6 26  ? 54.626  53.453  212.762 1.00 240.66 ?  26  GLY K O   1 
ATOM   20897 N N   . THR L  6 27  ? 55.613  54.790  211.240 1.00 242.95 ?  27  THR K N   1 
ATOM   20898 C CA  . THR L  6 27  ? 55.986  55.829  212.184 1.00 242.25 ?  27  THR K CA  1 
ATOM   20899 C C   . THR L  6 27  ? 56.228  57.093  211.379 1.00 242.73 ?  27  THR K C   1 
ATOM   20900 O O   . THR L  6 27  ? 56.418  57.043  210.160 1.00 243.36 ?  27  THR K O   1 
ATOM   20901 C CB  . THR L  6 27  ? 57.225  55.435  213.000 1.00 240.65 ?  27  THR K CB  1 
ATOM   20902 O OG1 . THR L  6 27  ? 57.575  56.488  213.911 1.00 239.75 ?  27  THR K OG1 1 
ATOM   20903 C CG2 . THR L  6 27  ? 58.390  55.144  212.073 1.00 240.46 ?  27  THR K CG2 1 
ATOM   20904 N N   . LEU L  6 28  ? 56.235  58.222  212.071 1.00 240.04 ?  28  LEU K N   1 
ATOM   20905 C CA  . LEU L  6 28  ? 56.482  59.507  211.434 1.00 239.99 ?  28  LEU K CA  1 
ATOM   20906 C C   . LEU L  6 28  ? 57.964  59.836  211.392 1.00 238.47 ?  28  LEU K C   1 
ATOM   20907 O O   . LEU L  6 28  ? 58.741  59.437  212.267 1.00 237.27 ?  28  LEU K O   1 
ATOM   20908 C CB  . LEU L  6 28  ? 55.725  60.667  212.085 1.00 240.41 ?  28  LEU K CB  1 
ATOM   20909 C CG  . LEU L  6 28  ? 54.196  60.716  212.073 1.00 242.13 ?  28  LEU K CG  1 
ATOM   20910 C CD1 . LEU L  6 28  ? 53.581  60.395  213.423 1.00 242.20 ?  28  LEU K CD1 1 
ATOM   20911 C CD2 . LEU L  6 28  ? 53.735  62.080  211.543 1.00 242.94 ?  28  LEU K CD2 1 
ATOM   20912 N N   . VAL L  6 29  ? 58.351  60.582  210.355 1.00 258.18 ?  29  VAL K N   1 
ATOM   20913 C CA  . VAL L  6 29  ? 59.760  60.916  210.191 1.00 256.12 ?  29  VAL K CA  1 
ATOM   20914 C C   . VAL L  6 29  ? 60.116  62.077  211.094 1.00 257.77 ?  29  VAL K C   1 
ATOM   20915 O O   . VAL L  6 29  ? 61.292  62.438  211.211 1.00 256.03 ?  29  VAL K O   1 
ATOM   20916 C CB  . VAL L  6 29  ? 60.086  61.285  208.733 1.00 255.01 ?  29  VAL K CB  1 
ATOM   20917 C CG1 . VAL L  6 29  ? 59.792  60.116  207.809 1.00 251.44 ?  29  VAL K CG1 1 
ATOM   20918 C CG2 . VAL L  6 29  ? 59.300  62.527  208.310 1.00 255.40 ?  29  VAL K CG2 1 
ATOM   20919 N N   . ARG L  6 30  ? 59.118  62.676  211.730 1.00 260.11 ?  30  ARG K N   1 
ATOM   20920 C CA  . ARG L  6 30  ? 59.344  63.806  212.608 1.00 252.75 ?  30  ARG K CA  1 
ATOM   20921 C C   . ARG L  6 30  ? 59.575  63.318  214.038 1.00 248.98 ?  30  ARG K C   1 
ATOM   20922 O O   . ARG L  6 30  ? 60.203  64.024  214.834 1.00 249.45 ?  30  ARG K O   1 
ATOM   20923 C CB  . ARG L  6 30  ? 58.168  64.799  212.522 1.00 254.64 ?  30  ARG K CB  1 
ATOM   20924 C CG  . ARG L  6 30  ? 58.329  66.084  213.354 1.00 261.04 ?  30  ARG K CG  1 
ATOM   20925 C CD  . ARG L  6 30  ? 57.438  67.300  212.993 1.00 270.18 ?  30  ARG K CD  1 
ATOM   20926 N NE  . ARG L  6 30  ? 55.987  67.085  212.963 1.00 273.98 ?  30  ARG K NE  1 
ATOM   20927 C CZ  . ARG L  6 30  ? 55.142  68.042  212.589 1.00 279.92 ?  30  ARG K CZ  1 
ATOM   20928 N NH1 . ARG L  6 30  ? 55.653  69.212  212.243 1.00 284.48 1  30  ARG K NH1 1 
ATOM   20929 N NH2 . ARG L  6 30  ? 53.823  67.861  212.552 1.00 281.35 ?  30  ARG K NH2 1 
ATOM   20930 N N   . ASP L  6 31  ? 59.045  62.139  214.390 1.00 260.58 ?  31  ASP K N   1 
ATOM   20931 C CA  . ASP L  6 31  ? 59.136  61.602  215.745 1.00 258.57 ?  31  ASP K CA  1 
ATOM   20932 C C   . ASP L  6 31  ? 60.296  60.619  215.949 1.00 254.90 ?  31  ASP K C   1 
ATOM   20933 O O   . ASP L  6 31  ? 60.323  59.916  216.967 1.00 252.23 ?  31  ASP K O   1 
ATOM   20934 C CB  . ASP L  6 31  ? 57.817  60.894  216.088 1.00 258.72 ?  31  ASP K CB  1 
ATOM   20935 C CG  . ASP L  6 31  ? 56.606  61.823  216.000 1.00 259.24 ?  31  ASP K CG  1 
ATOM   20936 O OD1 . ASP L  6 31  ? 56.638  62.759  215.174 1.00 263.41 ?  31  ASP K OD1 1 
ATOM   20937 O OD2 . ASP L  6 31  ? 55.605  61.597  216.716 1.00 261.41 -1 31  ASP K OD2 1 
ATOM   20938 N N   . ASN L  6 32  ? 61.245  60.538  215.015 1.00 234.56 ?  32  ASN K N   1 
ATOM   20939 C CA  . ASN L  6 32  ? 62.361  59.603  215.142 1.00 233.63 ?  32  ASN K CA  1 
ATOM   20940 C C   . ASN L  6 32  ? 63.634  60.175  214.533 1.00 232.79 ?  32  ASN K C   1 
ATOM   20941 O O   . ASN L  6 32  ? 63.606  61.145  213.769 1.00 233.11 ?  32  ASN K O   1 
ATOM   20942 C CB  . ASN L  6 32  ? 62.055  58.226  214.530 1.00 234.43 ?  32  ASN K CB  1 
ATOM   20943 C CG  . ASN L  6 32  ? 60.963  57.470  215.282 1.00 235.17 ?  32  ASN K CG  1 
ATOM   20944 O OD1 . ASN L  6 32  ? 59.773  57.579  214.977 1.00 236.39 ?  32  ASN K OD1 1 
ATOM   20945 N ND2 . ASN L  6 32  ? 61.371  56.709  216.295 1.00 234.50 ?  32  ASN K ND2 1 
ATOM   20946 N N   . TYR L  6 33  ? 64.759  59.552  214.888 1.00 235.11 ?  33  TYR K N   1 
ATOM   20947 C CA  . TYR L  6 33  ? 66.042  59.868  214.281 1.00 235.96 ?  33  TYR K CA  1 
ATOM   20948 C C   . TYR L  6 33  ? 66.218  58.936  213.083 1.00 236.86 ?  33  TYR K C   1 
ATOM   20949 O O   . TYR L  6 33  ? 65.717  57.807  213.081 1.00 236.18 ?  33  TYR K O   1 
ATOM   20950 C CB  . TYR L  6 33  ? 67.179  59.660  215.283 1.00 234.82 ?  33  TYR K CB  1 
ATOM   20951 C CG  . TYR L  6 33  ? 67.244  60.708  216.375 1.00 234.05 ?  33  TYR K CG  1 
ATOM   20952 C CD1 . TYR L  6 33  ? 66.382  60.636  217.463 1.00 233.55 ?  33  TYR K CD1 1 
ATOM   20953 C CD2 . TYR L  6 33  ? 68.145  61.767  216.322 1.00 237.19 ?  33  TYR K CD2 1 
ATOM   20954 C CE1 . TYR L  6 33  ? 66.417  61.574  218.471 1.00 236.63 ?  33  TYR K CE1 1 
ATOM   20955 C CE2 . TYR L  6 33  ? 68.185  62.719  217.333 1.00 240.16 ?  33  TYR K CE2 1 
ATOM   20956 C CZ  . TYR L  6 33  ? 67.316  62.613  218.403 1.00 239.07 ?  33  TYR K CZ  1 
ATOM   20957 O OH  . TYR L  6 33  ? 67.342  63.546  219.414 1.00 239.37 ?  33  TYR K OH  1 
ATOM   20958 N N   . TRP L  6 34  ? 66.940  59.404  212.064 1.00 235.38 ?  34  TRP K N   1 
ATOM   20959 C CA  . TRP L  6 34  ? 67.132  58.627  210.842 1.00 236.57 ?  34  TRP K CA  1 
ATOM   20960 C C   . TRP L  6 34  ? 68.594  58.636  210.413 1.00 237.92 ?  34  TRP K C   1 
ATOM   20961 O O   . TRP L  6 34  ? 69.199  59.708  210.310 1.00 242.59 ?  34  TRP K O   1 
ATOM   20962 C CB  . TRP L  6 34  ? 66.242  59.168  209.721 1.00 238.30 ?  34  TRP K CB  1 
ATOM   20963 C CG  . TRP L  6 34  ? 64.793  59.137  210.098 1.00 237.35 ?  34  TRP K CG  1 
ATOM   20964 C CD1 . TRP L  6 34  ? 64.059  60.182  210.579 1.00 237.45 ?  34  TRP K CD1 1 
ATOM   20965 C CD2 . TRP L  6 34  ? 63.929  57.994  210.133 1.00 236.41 ?  34  TRP K CD2 1 
ATOM   20966 N NE1 . TRP L  6 34  ? 62.779  59.777  210.855 1.00 236.78 ?  34  TRP K NE1 1 
ATOM   20967 C CE2 . TRP L  6 34  ? 62.673  58.437  210.596 1.00 236.17 ?  34  TRP K CE2 1 
ATOM   20968 C CE3 . TRP L  6 34  ? 64.087  56.647  209.796 1.00 236.04 ?  34  TRP K CE3 1 
ATOM   20969 C CZ2 . TRP L  6 34  ? 61.584  57.582  210.731 1.00 235.72 ?  34  TRP K CZ2 1 
ATOM   20970 C CZ3 . TRP L  6 34  ? 63.003  55.800  209.931 1.00 235.49 ?  34  TRP K CZ3 1 
ATOM   20971 C CH2 . TRP L  6 34  ? 61.769  56.270  210.397 1.00 235.40 ?  34  TRP K CH2 1 
ATOM   20972 N N   . SER L  6 35  ? 69.165  57.455  210.165 1.00 226.94 ?  35  SER K N   1 
ATOM   20973 C CA  . SER L  6 35  ? 70.564  57.351  209.768 1.00 228.57 ?  35  SER K CA  1 
ATOM   20974 C C   . SER L  6 35  ? 70.696  56.602  208.447 1.00 233.35 ?  35  SER K C   1 
ATOM   20975 O O   . SER L  6 35  ? 69.862  55.754  208.110 1.00 235.92 ?  35  SER K O   1 
ATOM   20976 C CB  . SER L  6 35  ? 71.382  56.608  210.835 1.00 222.94 ?  35  SER K CB  1 
ATOM   20977 O OG  . SER L  6 35  ? 71.274  57.231  212.101 1.00 220.01 ?  35  SER K OG  1 
ATOM   20978 N N   . TRP L  6 36  ? 71.758  56.921  207.699 1.00 228.82 ?  36  TRP K N   1 
ATOM   20979 C CA  . TRP L  6 36  ? 72.070  56.255  206.437 1.00 231.07 ?  36  TRP K CA  1 
ATOM   20980 C C   . TRP L  6 36  ? 73.422  55.568  206.590 1.00 231.83 ?  36  TRP K C   1 
ATOM   20981 O O   . TRP L  6 36  ? 74.371  56.173  207.100 1.00 232.60 ?  36  TRP K O   1 
ATOM   20982 C CB  . TRP L  6 36  ? 72.126  57.227  205.250 1.00 234.58 ?  36  TRP K CB  1 
ATOM   20983 C CG  . TRP L  6 36  ? 70.787  57.702  204.756 1.00 234.65 ?  36  TRP K CG  1 
ATOM   20984 C CD1 . TRP L  6 36  ? 70.068  58.752  205.246 1.00 234.14 ?  36  TRP K CD1 1 
ATOM   20985 C CD2 . TRP L  6 36  ? 69.963  57.090  203.752 1.00 234.86 ?  36  TRP K CD2 1 
ATOM   20986 N NE1 . TRP L  6 36  ? 68.882  58.875  204.569 1.00 234.46 ?  36  TRP K NE1 1 
ATOM   20987 C CE2 . TRP L  6 36  ? 68.786  57.861  203.654 1.00 234.80 ?  36  TRP K CE2 1 
ATOM   20988 C CE3 . TRP L  6 36  ? 70.113  55.980  202.914 1.00 235.35 ?  36  TRP K CE3 1 
ATOM   20989 C CZ2 . TRP L  6 36  ? 67.768  57.560  202.754 1.00 235.16 ?  36  TRP K CZ2 1 
ATOM   20990 C CZ3 . TRP L  6 36  ? 69.098  55.683  202.019 1.00 235.63 ?  36  TRP K CZ3 1 
ATOM   20991 C CH2 . TRP L  6 36  ? 67.942  56.470  201.947 1.00 235.51 ?  36  TRP K CH2 1 
ATOM   20992 N N   . ILE L  6 37  ? 73.504  54.309  206.167 1.00 233.51 ?  37  ILE K N   1 
ATOM   20993 C CA  . ILE L  6 37  ? 74.721  53.508  206.263 1.00 234.43 ?  37  ILE K CA  1 
ATOM   20994 C C   . ILE L  6 37  ? 75.008  52.873  204.905 1.00 240.71 ?  37  ILE K C   1 
ATOM   20995 O O   . ILE L  6 37  ? 74.135  52.210  204.336 1.00 242.65 ?  37  ILE K O   1 
ATOM   20996 C CB  . ILE L  6 37  ? 74.616  52.428  207.361 1.00 231.52 ?  37  ILE K CB  1 
ATOM   20997 C CG1 . ILE L  6 37  ? 74.220  53.043  208.712 1.00 228.88 ?  37  ILE K CG1 1 
ATOM   20998 C CG2 . ILE L  6 37  ? 75.934  51.685  207.509 1.00 232.76 ?  37  ILE K CG2 1 
ATOM   20999 C CD1 . ILE L  6 37  ? 72.717  53.025  209.002 1.00 226.76 ?  37  ILE K CD1 1 
ATOM   21000 N N   . ARG L  6 38  ? 76.221  53.074  204.384 1.00 230.50 ?  38  ARG K N   1 
ATOM   21001 C CA  . ARG L  6 38  ? 76.624  52.474  203.117 1.00 233.73 ?  38  ARG K CA  1 
ATOM   21002 C C   . ARG L  6 38  ? 77.670  51.395  203.375 1.00 231.55 ?  38  ARG K C   1 
ATOM   21003 O O   . ARG L  6 38  ? 78.374  51.414  204.389 1.00 228.29 ?  38  ARG K O   1 
ATOM   21004 C CB  . ARG L  6 38  ? 77.214  53.494  202.135 1.00 237.73 ?  38  ARG K CB  1 
ATOM   21005 C CG  . ARG L  6 38  ? 78.549  54.086  202.555 1.00 240.15 ?  38  ARG K CG  1 
ATOM   21006 C CD  . ARG L  6 38  ? 79.076  55.001  201.463 1.00 246.18 ?  38  ARG K CD  1 
ATOM   21007 N NE  . ARG L  6 38  ? 80.455  55.416  201.698 1.00 250.56 ?  38  ARG K NE  1 
ATOM   21008 C CZ  . ARG L  6 38  ? 81.160  56.161  200.852 1.00 255.88 ?  38  ARG K CZ  1 
ATOM   21009 N NH1 . ARG L  6 38  ? 80.611  56.572  199.717 1.00 260.52 1  38  ARG K NH1 1 
ATOM   21010 N NH2 . ARG L  6 38  ? 82.416  56.483  201.132 1.00 260.27 ?  38  ARG K NH2 1 
ATOM   21011 N N   . GLN L  6 39  ? 77.762  50.440  202.443 1.00 235.15 ?  39  GLN K N   1 
ATOM   21012 C CA  . GLN L  6 39  ? 78.694  49.331  202.617 1.00 233.20 ?  39  GLN K CA  1 
ATOM   21013 C C   . GLN L  6 39  ? 79.197  48.742  201.303 1.00 240.78 ?  39  GLN K C   1 
ATOM   21014 O O   . GLN L  6 39  ? 78.433  48.102  200.569 1.00 241.34 ?  39  GLN K O   1 
ATOM   21015 C CB  . GLN L  6 39  ? 78.043  48.225  203.444 1.00 228.73 ?  39  GLN K CB  1 
ATOM   21016 C CG  . GLN L  6 39  ? 78.976  47.070  203.711 1.00 229.59 ?  39  GLN K CG  1 
ATOM   21017 C CD  . GLN L  6 39  ? 78.322  45.958  204.492 1.00 227.91 ?  39  GLN K CD  1 
ATOM   21018 O OE1 . GLN L  6 39  ? 77.117  45.981  204.747 1.00 224.10 ?  39  GLN K OE1 1 
ATOM   21019 N NE2 . GLN L  6 39  ? 79.117  44.969  204.879 1.00 232.33 ?  39  GLN K NE2 1 
ATOM   21020 N N   . PRO L  6 40  ? 80.468  48.960  200.964 1.00 233.15 ?  40  PRO K N   1 
ATOM   21021 C CA  . PRO L  6 40  ? 81.038  48.355  199.753 1.00 237.85 ?  40  PRO K CA  1 
ATOM   21022 C C   . PRO L  6 40  ? 81.074  46.834  199.851 1.00 236.41 ?  40  PRO K C   1 
ATOM   21023 O O   . PRO L  6 40  ? 80.922  46.236  200.919 1.00 233.98 ?  40  PRO K O   1 
ATOM   21024 C CB  . PRO L  6 40  ? 82.444  48.960  199.680 1.00 241.09 ?  40  PRO K CB  1 
ATOM   21025 C CG  . PRO L  6 40  ? 82.342  50.227  200.473 1.00 238.69 ?  40  PRO K CG  1 
ATOM   21026 C CD  . PRO L  6 40  ? 81.389  49.925  201.584 1.00 232.43 ?  40  PRO K CD  1 
ATOM   21027 N N   . LEU L  6 41  ? 81.282  46.206  198.694 1.00 222.25 ?  41  LEU K N   1 
ATOM   21028 C CA  . LEU L  6 41  ? 81.297  44.749  198.574 1.00 222.80 ?  41  LEU K CA  1 
ATOM   21029 C C   . LEU L  6 41  ? 82.523  44.124  199.233 1.00 222.55 ?  41  LEU K C   1 
ATOM   21030 O O   . LEU L  6 41  ? 83.649  44.280  198.749 1.00 222.96 ?  41  LEU K O   1 
ATOM   21031 C CB  . LEU L  6 41  ? 81.243  44.368  197.099 1.00 224.04 ?  41  LEU K CB  1 
ATOM   21032 C CG  . LEU L  6 41  ? 80.011  44.867  196.350 1.00 224.45 ?  41  LEU K CG  1 
ATOM   21033 C CD1 . LEU L  6 41  ? 80.042  44.423  194.897 1.00 225.72 ?  41  LEU K CD1 1 
ATOM   21034 C CD2 . LEU L  6 41  ? 78.755  44.374  197.044 1.00 224.11 ?  41  LEU K CD2 1 
ATOM   21035 N N   . GLY L  6 42  ? 82.301  43.415  200.339 1.00 224.94 ?  42  GLY K N   1 
ATOM   21036 C CA  . GLY L  6 42  ? 83.366  42.714  201.027 1.00 225.66 ?  42  GLY K CA  1 
ATOM   21037 C C   . GLY L  6 42  ? 84.127  43.579  201.994 1.00 225.35 ?  42  GLY K C   1 
ATOM   21038 O O   . GLY L  6 42  ? 85.265  43.250  202.344 1.00 227.35 ?  42  GLY K O   1 
ATOM   21039 N N   . LYS L  6 43  ? 83.519  44.665  202.455 1.00 234.32 ?  43  LYS K N   1 
ATOM   21040 C CA  . LYS L  6 43  ? 84.117  45.600  203.390 1.00 234.73 ?  43  LYS K CA  1 
ATOM   21041 C C   . LYS L  6 43  ? 83.155  45.875  204.536 1.00 226.72 ?  43  LYS K C   1 
ATOM   21042 O O   . LYS L  6 43  ? 81.998  45.448  204.529 1.00 222.59 ?  43  LYS K O   1 
ATOM   21043 C CB  . LYS L  6 43  ? 84.543  46.893  202.686 1.00 235.53 ?  43  LYS K CB  1 
ATOM   21044 C CG  . LYS L  6 43  ? 85.646  46.659  201.662 1.00 246.09 ?  43  LYS K CG  1 
ATOM   21045 C CD  . LYS L  6 43  ? 86.919  46.132  202.321 1.00 247.67 ?  43  LYS K CD  1 
ATOM   21046 C CE  . LYS L  6 43  ? 87.506  47.122  203.315 1.00 253.31 ?  43  LYS K CE  1 
ATOM   21047 N NZ  . LYS L  6 43  ? 88.759  46.606  203.941 1.00 246.49 1  43  LYS K NZ  1 
ATOM   21048 N N   . GLN L  6 44  ? 83.661  46.583  205.536 1.00 234.22 ?  44  GLN K N   1 
ATOM   21049 C CA  . GLN L  6 44  ? 82.904  46.938  206.724 1.00 223.16 ?  44  GLN K CA  1 
ATOM   21050 C C   . GLN L  6 44  ? 82.025  48.177  206.520 1.00 222.90 ?  44  GLN K C   1 
ATOM   21051 O O   . GLN L  6 44  ? 82.372  49.090  205.766 1.00 225.41 ?  44  GLN K O   1 
ATOM   21052 C CB  . GLN L  6 44  ? 83.886  47.152  207.874 1.00 222.62 ?  44  GLN K CB  1 
ATOM   21053 C CG  . GLN L  6 44  ? 84.886  48.283  207.618 1.00 229.61 ?  44  GLN K CG  1 
ATOM   21054 C CD  . GLN L  6 44  ? 86.125  48.162  208.492 1.00 234.35 ?  44  GLN K CD  1 
ATOM   21055 O OE1 . GLN L  6 44  ? 86.432  47.079  208.986 1.00 233.29 ?  44  GLN K OE1 1 
ATOM   21056 N NE2 . GLN L  6 44  ? 86.905  49.235  208.583 1.00 241.89 ?  44  GLN K NE2 1 
ATOM   21057 N N   . PRO L  6 45  ? 80.861  48.189  207.176 1.00 235.28 ?  45  PRO K N   1 
ATOM   21058 C CA  . PRO L  6 45  ? 79.899  49.299  207.053 1.00 233.67 ?  45  PRO K CA  1 
ATOM   21059 C C   . PRO L  6 45  ? 80.437  50.673  207.441 1.00 236.20 ?  45  PRO K C   1 
ATOM   21060 O O   . PRO L  6 45  ? 81.133  50.827  208.447 1.00 238.38 ?  45  PRO K O   1 
ATOM   21061 C CB  . PRO L  6 45  ? 78.764  48.874  207.993 1.00 229.06 ?  45  PRO K CB  1 
ATOM   21062 C CG  . PRO L  6 45  ? 78.865  47.387  208.053 1.00 228.07 ?  45  PRO K CG  1 
ATOM   21063 C CD  . PRO L  6 45  ? 80.328  47.083  207.988 1.00 230.91 ?  45  PRO K CD  1 
ATOM   21064 N N   . GLU L  6 46  ? 80.111  51.680  206.623 1.00 233.10 ?  46  GLU K N   1 
ATOM   21065 C CA  . GLU L  6 46  ? 80.530  53.060  206.861 1.00 236.78 ?  46  GLU K CA  1 
ATOM   21066 C C   . GLU L  6 46  ? 79.333  53.959  207.173 1.00 233.32 ?  46  GLU K C   1 
ATOM   21067 O O   . GLU L  6 46  ? 78.405  54.067  206.364 1.00 231.47 ?  46  GLU K O   1 
ATOM   21068 C CB  . GLU L  6 46  ? 81.277  53.644  205.664 1.00 243.46 ?  46  GLU K CB  1 
ATOM   21069 C CG  . GLU L  6 46  ? 81.754  55.064  205.953 1.00 250.26 ?  46  GLU K CG  1 
ATOM   21070 C CD  . GLU L  6 46  ? 82.536  55.687  204.817 1.00 261.09 ?  46  GLU K CD  1 
ATOM   21071 O OE1 . GLU L  6 46  ? 83.037  54.944  203.948 1.00 262.96 ?  46  GLU K OE1 1 
ATOM   21072 O OE2 . GLU L  6 46  ? 82.645  56.932  204.797 1.00 266.70 -1 46  GLU K OE2 1 
ATOM   21073 N N   . TRP L  6 47  ? 79.363  54.594  208.347 1.00 238.20 ?  47  TRP K N   1 
ATOM   21074 C CA  . TRP L  6 47  ? 78.315  55.512  208.793 1.00 237.52 ?  47  TRP K CA  1 
ATOM   21075 C C   . TRP L  6 47  ? 78.352  56.799  207.971 1.00 242.70 ?  47  TRP K C   1 
ATOM   21076 O O   . TRP L  6 47  ? 79.394  57.459  207.895 1.00 247.71 ?  47  TRP K O   1 
ATOM   21077 C CB  . TRP L  6 47  ? 78.483  55.818  210.280 1.00 236.06 ?  47  TRP K CB  1 
ATOM   21078 C CG  . TRP L  6 47  ? 77.274  56.431  210.939 1.00 236.97 ?  47  TRP K CG  1 
ATOM   21079 C CD1 . TRP L  6 47  ? 76.042  56.623  210.382 1.00 235.95 ?  47  TRP K CD1 1 
ATOM   21080 C CD2 . TRP L  6 47  ? 77.181  56.909  212.291 1.00 234.16 ?  47  TRP K CD2 1 
ATOM   21081 N NE1 . TRP L  6 47  ? 75.195  57.205  211.295 1.00 233.81 ?  47  TRP K NE1 1 
ATOM   21082 C CE2 . TRP L  6 47  ? 75.868  57.388  212.475 1.00 232.93 ?  47  TRP K CE2 1 
ATOM   21083 C CE3 . TRP L  6 47  ? 78.082  56.983  213.361 1.00 227.90 ?  47  TRP K CE3 1 
ATOM   21084 C CZ2 . TRP L  6 47  ? 75.434  57.932  213.685 1.00 228.88 ?  47  TRP K CZ2 1 
ATOM   21085 C CZ3 . TRP L  6 47  ? 77.648  57.524  214.561 1.00 222.73 ?  47  TRP K CZ3 1 
ATOM   21086 C CH2 . TRP L  6 47  ? 76.337  57.991  214.713 1.00 224.43 ?  47  TRP K CH2 1 
ATOM   21087 N N   . ILE L  6 48  ? 77.228  57.160  207.353 1.00 222.64 ?  48  ILE K N   1 
ATOM   21088 C CA  . ILE L  6 48  ? 77.186  58.358  206.514 1.00 223.05 ?  48  ILE K CA  1 
ATOM   21089 C C   . ILE L  6 48  ? 76.837  59.612  207.313 1.00 222.36 ?  48  ILE K C   1 
ATOM   21090 O O   . ILE L  6 48  ? 77.464  60.660  207.139 1.00 222.18 ?  48  ILE K O   1 
ATOM   21091 C CB  . ILE L  6 48  ? 76.181  58.142  205.365 1.00 224.21 ?  48  ILE K CB  1 
ATOM   21092 C CG1 . ILE L  6 48  ? 76.477  56.853  204.601 1.00 224.90 ?  48  ILE K CG1 1 
ATOM   21093 C CG2 . ILE L  6 48  ? 76.175  59.326  204.422 1.00 224.78 ?  48  ILE K CG2 1 
ATOM   21094 C CD1 . ILE L  6 48  ? 75.473  56.582  203.504 1.00 226.04 ?  48  ILE K CD1 1 
ATOM   21095 N N   . GLY L  6 49  ? 75.846  59.532  208.185 1.00 232.74 ?  49  GLY K N   1 
ATOM   21096 C CA  . GLY L  6 49  ? 75.428  60.656  208.998 1.00 231.61 ?  49  GLY K CA  1 
ATOM   21097 C C   . GLY L  6 49  ? 74.002  60.469  209.452 1.00 228.37 ?  49  GLY K C   1 
ATOM   21098 O O   . GLY L  6 49  ? 73.254  59.648  208.917 1.00 227.61 ?  49  GLY K O   1 
ATOM   21099 N N   . TYR L  6 50  ? 73.613  61.247  210.462 1.00 238.21 ?  50  TYR K N   1 
ATOM   21100 C CA  . TYR L  6 50  ? 72.263  61.186  211.011 1.00 239.96 ?  50  TYR K CA  1 
ATOM   21101 C C   . TYR L  6 50  ? 71.524  62.505  210.812 1.00 244.89 ?  50  TYR K C   1 
ATOM   21102 O O   . TYR L  6 50  ? 72.125  63.584  210.877 1.00 248.86 ?  50  TYR K O   1 
ATOM   21103 C CB  . TYR L  6 50  ? 72.314  60.808  212.498 1.00 237.14 ?  50  TYR K CB  1 
ATOM   21104 C CG  . TYR L  6 50  ? 73.061  61.786  213.388 1.00 240.70 ?  50  TYR K CG  1 
ATOM   21105 C CD1 . TYR L  6 50  ? 74.437  61.679  213.564 1.00 237.74 ?  50  TYR K CD1 1 
ATOM   21106 C CD2 . TYR L  6 50  ? 72.392  62.794  214.072 1.00 241.18 ?  50  TYR K CD2 1 
ATOM   21107 C CE1 . TYR L  6 50  ? 75.127  62.556  214.382 1.00 239.07 ?  50  TYR K CE1 1 
ATOM   21108 C CE2 . TYR L  6 50  ? 73.075  63.677  214.895 1.00 239.00 ?  50  TYR K CE2 1 
ATOM   21109 C CZ  . TYR L  6 50  ? 74.441  63.553  215.046 1.00 239.53 ?  50  TYR K CZ  1 
ATOM   21110 O OH  . TYR L  6 50  ? 75.125  64.428  215.861 1.00 240.93 ?  50  TYR K OH  1 
ATOM   21111 N N   . VAL L  6 51  ? 70.211  62.401  210.560 1.00 251.71 ?  51  VAL K N   1 
ATOM   21112 C CA  . VAL L  6 51  ? 69.326  63.541  210.331 1.00 251.21 ?  51  VAL K CA  1 
ATOM   21113 C C   . VAL L  6 51  ? 68.100  63.479  211.243 1.00 246.22 ?  51  VAL K C   1 
ATOM   21114 O O   . VAL L  6 51  ? 67.549  62.400  211.492 1.00 239.21 ?  51  VAL K O   1 
ATOM   21115 C CB  . VAL L  6 51  ? 68.904  63.599  208.843 1.00 253.92 ?  51  VAL K CB  1 
ATOM   21116 C CG1 . VAL L  6 51  ? 68.218  62.297  208.413 1.00 250.57 ?  51  VAL K CG1 1 
ATOM   21117 C CG2 . VAL L  6 51  ? 68.023  64.812  208.558 1.00 257.37 ?  51  VAL K CG2 1 
ATOM   21118 N N   . HIS L  6 52  ? 67.690  64.640  211.758 1.00 244.80 ?  52  HIS K N   1 
ATOM   21119 C CA  . HIS L  6 52  ? 66.529  64.756  212.632 1.00 242.96 ?  52  HIS K CA  1 
ATOM   21120 C C   . HIS L  6 52  ? 65.902  66.132  212.434 1.00 245.61 ?  52  HIS K C   1 
ATOM   21121 O O   . HIS L  6 52  ? 66.519  67.035  211.863 1.00 251.57 ?  52  HIS K O   1 
ATOM   21122 C CB  . HIS L  6 52  ? 66.881  64.522  214.104 1.00 240.40 ?  52  HIS K CB  1 
ATOM   21123 C CG  . HIS L  6 52  ? 65.683  64.446  214.998 1.00 238.81 ?  52  HIS K CG  1 
ATOM   21124 N ND1 . HIS L  6 52  ? 64.872  63.333  215.058 1.00 239.71 ?  52  HIS K ND1 1 
ATOM   21125 C CD2 . HIS L  6 52  ? 65.152  65.346  215.859 1.00 236.76 ?  52  HIS K CD2 1 
ATOM   21126 C CE1 . HIS L  6 52  ? 63.895  63.549  215.920 1.00 238.37 ?  52  HIS K CE1 1 
ATOM   21127 N NE2 . HIS L  6 52  ? 64.042  64.763  216.421 1.00 236.64 ?  52  HIS K NE2 1 
ATOM   21128 N N   . ASP L  6 53  ? 64.660  66.283  212.894 1.00 238.93 ?  53  ASP K N   1 
ATOM   21129 C CA  . ASP L  6 53  ? 63.973  67.563  212.787 1.00 243.50 ?  53  ASP K CA  1 
ATOM   21130 C C   . ASP L  6 53  ? 64.631  68.583  213.718 1.00 245.22 ?  53  ASP K C   1 
ATOM   21131 O O   . ASP L  6 53  ? 65.560  68.275  214.472 1.00 243.43 ?  53  ASP K O   1 
ATOM   21132 C CB  . ASP L  6 53  ? 62.490  67.412  213.125 1.00 243.76 ?  53  ASP K CB  1 
ATOM   21133 C CG  . ASP L  6 53  ? 61.626  68.489  212.486 1.00 248.63 ?  53  ASP K CG  1 
ATOM   21134 O OD1 . ASP L  6 53  ? 62.103  69.634  212.329 1.00 248.70 ?  53  ASP K OD1 1 
ATOM   21135 O OD2 . ASP L  6 53  ? 60.453  68.201  212.175 1.00 247.61 -1 53  ASP K OD2 1 
ATOM   21136 N N   . SER L  6 54  ? 64.132  69.820  213.665 1.00 237.52 ?  54  SER K N   1 
ATOM   21137 C CA  . SER L  6 54  ? 64.632  70.929  214.477 1.00 236.64 ?  54  SER K CA  1 
ATOM   21138 C C   . SER L  6 54  ? 66.100  71.246  214.201 1.00 235.64 ?  54  SER K C   1 
ATOM   21139 O O   . SER L  6 54  ? 66.779  71.832  215.049 1.00 234.56 ?  54  SER K O   1 
ATOM   21140 C CB  . SER L  6 54  ? 64.417  70.668  215.974 1.00 235.80 ?  54  SER K CB  1 
ATOM   21141 O OG  . SER L  6 54  ? 65.290  69.659  216.452 1.00 234.68 ?  54  SER K OG  1 
ATOM   21142 N N   . GLY L  6 55  ? 66.613  70.862  213.031 1.00 249.73 ?  55  GLY K N   1 
ATOM   21143 C CA  . GLY L  6 55  ? 67.967  71.205  212.642 1.00 252.49 ?  55  GLY K CA  1 
ATOM   21144 C C   . GLY L  6 55  ? 69.068  70.309  213.171 1.00 252.29 ?  55  GLY K C   1 
ATOM   21145 O O   . GLY L  6 55  ? 70.240  70.549  212.856 1.00 258.11 ?  55  GLY K O   1 
ATOM   21146 N N   . ASP L  6 56  ? 68.739  69.279  213.945 1.00 252.18 ?  56  ASP K N   1 
ATOM   21147 C CA  . ASP L  6 56  ? 69.738  68.371  214.496 1.00 248.84 ?  56  ASP K CA  1 
ATOM   21148 C C   . ASP L  6 56  ? 70.268  67.431  213.419 1.00 246.83 ?  56  ASP K C   1 
ATOM   21149 O O   . ASP L  6 56  ? 69.683  66.369  213.179 1.00 241.60 ?  56  ASP K O   1 
ATOM   21150 C CB  . ASP L  6 56  ? 69.134  67.581  215.657 1.00 240.93 ?  56  ASP K CB  1 
ATOM   21151 C CG  . ASP L  6 56  ? 70.142  66.690  216.352 1.00 239.73 ?  56  ASP K CG  1 
ATOM   21152 O OD1 . ASP L  6 56  ? 71.339  67.040  216.361 1.00 240.47 ?  56  ASP K OD1 1 
ATOM   21153 O OD2 . ASP L  6 56  ? 69.727  65.660  216.929 1.00 236.56 -1 56  ASP K OD2 1 
ATOM   21154 N N   . THR L  6 57  ? 71.371  67.807  212.761 1.00 252.33 ?  57  THR K N   1 
ATOM   21155 C CA  . THR L  6 57  ? 71.948  67.003  211.684 1.00 246.14 ?  57  THR K CA  1 
ATOM   21156 C C   . THR L  6 57  ? 73.466  67.117  211.651 1.00 245.97 ?  57  THR K C   1 
ATOM   21157 O O   . THR L  6 57  ? 74.002  68.228  211.606 1.00 248.33 ?  57  THR K O   1 
ATOM   21158 C CB  . THR L  6 57  ? 71.395  67.445  210.324 1.00 248.17 ?  57  THR K CB  1 
ATOM   21159 O OG1 . THR L  6 57  ? 69.963  67.373  210.329 1.00 251.70 ?  57  THR K OG1 1 
ATOM   21160 C CG2 . THR L  6 57  ? 71.962  66.585  209.203 1.00 244.01 ?  57  THR K CG2 1 
ATOM   21161 N N   . ASN L  6 58  ? 74.150  65.972  211.701 1.00 241.47 ?  58  ASN K N   1 
ATOM   21162 C CA  . ASN L  6 58  ? 75.605  65.915  211.639 1.00 244.32 ?  58  ASN K CA  1 
ATOM   21163 C C   . ASN L  6 58  ? 76.008  64.906  210.568 1.00 244.92 ?  58  ASN K C   1 
ATOM   21164 O O   . ASN L  6 58  ? 75.277  63.950  210.294 1.00 241.01 ?  58  ASN K O   1 
ATOM   21165 C CB  . ASN L  6 58  ? 76.221  65.541  212.996 1.00 237.63 ?  58  ASN K CB  1 
ATOM   21166 C CG  . ASN L  6 58  ? 77.724  65.741  213.034 1.00 243.09 ?  58  ASN K CG  1 
ATOM   21167 O OD1 . ASN L  6 58  ? 78.288  66.451  212.203 1.00 251.95 ?  58  ASN K OD1 1 
ATOM   21168 N ND2 . ASN L  6 58  ? 78.380  65.116  214.006 1.00 247.36 ?  58  ASN K ND2 1 
ATOM   21169 N N   . TYR L  6 59  ? 77.175  65.120  209.967 1.00 240.31 ?  59  TYR K N   1 
ATOM   21170 C CA  . TYR L  6 59  ? 77.678  64.293  208.873 1.00 239.38 ?  59  TYR K CA  1 
ATOM   21171 C C   . TYR L  6 59  ? 78.994  63.614  209.244 1.00 233.67 ?  59  TYR K C   1 
ATOM   21172 O O   . TYR L  6 59  ? 79.573  63.843  210.308 1.00 234.72 ?  59  TYR K O   1 
ATOM   21173 C CB  . TYR L  6 59  ? 77.827  65.098  207.577 1.00 242.78 ?  59  TYR K CB  1 
ATOM   21174 C CG  . TYR L  6 59  ? 76.530  65.674  207.054 1.00 243.92 ?  59  TYR K CG  1 
ATOM   21175 C CD1 . TYR L  6 59  ? 75.337  64.976  207.205 1.00 241.70 ?  59  TYR K CD1 1 
ATOM   21176 C CD2 . TYR L  6 59  ? 76.500  66.877  206.361 1.00 250.87 ?  59  TYR K CD2 1 
ATOM   21177 C CE1 . TYR L  6 59  ? 74.146  65.475  206.712 1.00 243.77 ?  59  TYR K CE1 1 
ATOM   21178 C CE2 . TYR L  6 59  ? 75.309  67.386  205.863 1.00 254.08 ?  59  TYR K CE2 1 
ATOM   21179 C CZ  . TYR L  6 59  ? 74.136  66.680  206.043 1.00 251.53 ?  59  TYR K CZ  1 
ATOM   21180 O OH  . TYR L  6 59  ? 72.952  67.183  205.549 1.00 258.61 ?  59  TYR K OH  1 
ATOM   21181 N N   . ASN L  6 60  ? 79.452  62.773  208.323 1.00 223.48 ?  60  ASN K N   1 
ATOM   21182 C CA  . ASN L  6 60  ? 80.722  62.077  208.462 1.00 224.76 ?  60  ASN K CA  1 
ATOM   21183 C C   . ASN L  6 60  ? 81.868  62.999  208.068 1.00 229.97 ?  60  ASN K C   1 
ATOM   21184 O O   . ASN L  6 60  ? 81.887  63.499  206.937 1.00 235.12 ?  60  ASN K O   1 
ATOM   21185 C CB  . ASN L  6 60  ? 80.730  60.826  207.589 1.00 225.12 ?  60  ASN K CB  1 
ATOM   21186 C CG  . ASN L  6 60  ? 81.870  59.881  207.920 1.00 225.49 ?  60  ASN K CG  1 
ATOM   21187 O OD1 . ASN L  6 60  ? 82.880  60.276  208.500 1.00 226.95 ?  60  ASN K OD1 1 
ATOM   21188 N ND2 . ASN L  6 60  ? 81.701  58.614  207.564 1.00 224.32 ?  60  ASN K ND2 1 
ATOM   21189 N N   . PRO L  6 61  ? 82.815  63.271  208.968 1.00 238.57 ?  61  PRO K N   1 
ATOM   21190 C CA  . PRO L  6 61  ? 83.945  64.158  208.641 1.00 246.44 ?  61  PRO K CA  1 
ATOM   21191 C C   . PRO L  6 61  ? 84.664  63.819  207.344 1.00 253.58 ?  61  PRO K C   1 
ATOM   21192 O O   . PRO L  6 61  ? 85.234  64.714  206.707 1.00 259.44 ?  61  PRO K O   1 
ATOM   21193 C CB  . PRO L  6 61  ? 84.866  63.990  209.856 1.00 241.31 ?  61  PRO K CB  1 
ATOM   21194 C CG  . PRO L  6 61  ? 83.932  63.698  210.979 1.00 228.39 ?  61  PRO K CG  1 
ATOM   21195 C CD  . PRO L  6 61  ? 82.822  62.867  210.385 1.00 228.27 ?  61  PRO K CD  1 
ATOM   21196 N N   . SER L  6 62  ? 84.671  62.550  206.940 1.00 239.83 ?  62  SER K N   1 
ATOM   21197 C CA  . SER L  6 62  ? 85.330  62.153  205.701 1.00 240.87 ?  62  SER K CA  1 
ATOM   21198 C C   . SER L  6 62  ? 84.521  62.534  204.467 1.00 245.04 ?  62  SER K C   1 
ATOM   21199 O O   . SER L  6 62  ? 85.097  62.743  203.393 1.00 249.72 ?  62  SER K O   1 
ATOM   21200 C CB  . SER L  6 62  ? 85.591  60.647  205.714 1.00 231.76 ?  62  SER K CB  1 
ATOM   21201 O OG  . SER L  6 62  ? 84.386  59.927  205.902 1.00 226.83 ?  62  SER K OG  1 
ATOM   21202 N N   . LEU L  6 63  ? 83.200  62.623  204.595 1.00 231.97 ?  63  LEU K N   1 
ATOM   21203 C CA  . LEU L  6 63  ? 82.311  62.970  203.493 1.00 233.82 ?  63  LEU K CA  1 
ATOM   21204 C C   . LEU L  6 63  ? 81.533  64.253  203.780 1.00 233.28 ?  63  LEU K C   1 
ATOM   21205 O O   . LEU L  6 63  ? 80.413  64.434  203.299 1.00 232.74 ?  63  LEU K O   1 
ATOM   21206 C CB  . LEU L  6 63  ? 81.371  61.809  203.174 1.00 232.87 ?  63  LEU K CB  1 
ATOM   21207 C CG  . LEU L  6 63  ? 82.086  60.460  203.042 1.00 233.06 ?  63  LEU K CG  1 
ATOM   21208 C CD1 . LEU L  6 63  ? 81.096  59.327  202.831 1.00 233.43 ?  63  LEU K CD1 1 
ATOM   21209 C CD2 . LEU L  6 63  ? 83.100  60.508  201.910 1.00 236.93 ?  63  LEU K CD2 1 
ATOM   21210 N N   . LYS L  6 64  ? 82.129  65.144  204.578 1.00 243.31 ?  64  LYS K N   1 
ATOM   21211 C CA  . LYS L  6 64  ? 81.459  66.363  205.032 1.00 242.71 ?  64  LYS K CA  1 
ATOM   21212 C C   . LYS L  6 64  ? 81.017  67.248  203.873 1.00 247.40 ?  64  LYS K C   1 
ATOM   21213 O O   . LYS L  6 64  ? 79.872  67.714  203.835 1.00 245.62 ?  64  LYS K O   1 
ATOM   21214 C CB  . LYS L  6 64  ? 82.377  67.179  205.941 1.00 243.97 ?  64  LYS K CB  1 
ATOM   21215 C CG  . LYS L  6 64  ? 81.901  67.377  207.364 1.00 238.44 ?  64  LYS K CG  1 
ATOM   21216 C CD  . LYS L  6 64  ? 82.921  68.217  208.121 1.00 240.49 ?  64  LYS K CD  1 
ATOM   21217 C CE  . LYS L  6 64  ? 82.244  69.232  209.032 1.00 237.75 ?  64  LYS K CE  1 
ATOM   21218 N NZ  . LYS L  6 64  ? 83.229  70.067  209.779 1.00 239.77 1  64  LYS K NZ  1 
ATOM   21219 N N   . SER L  6 65  ? 81.909  67.491  202.916 1.00 244.97 ?  65  SER K N   1 
ATOM   21220 C CA  . SER L  6 65  ? 81.655  68.446  201.848 1.00 253.90 ?  65  SER K CA  1 
ATOM   21221 C C   . SER L  6 65  ? 81.000  67.839  200.614 1.00 259.02 ?  65  SER K C   1 
ATOM   21222 O O   . SER L  6 65  ? 81.116  68.413  199.525 1.00 266.47 ?  65  SER K O   1 
ATOM   21223 C CB  . SER L  6 65  ? 82.962  69.132  201.448 1.00 264.16 ?  65  SER K CB  1 
ATOM   21224 O OG  . SER L  6 65  ? 82.769  69.988  200.337 1.00 274.44 ?  65  SER K OG  1 
ATOM   21225 N N   . ARG L  6 66  ? 80.315  66.702  200.747 1.00 245.68 ?  66  ARG K N   1 
ATOM   21226 C CA  . ARG L  6 66  ? 79.664  66.107  199.582 1.00 247.17 ?  66  ARG K CA  1 
ATOM   21227 C C   . ARG L  6 66  ? 78.243  65.638  199.844 1.00 241.48 ?  66  ARG K C   1 
ATOM   21228 O O   . ARG L  6 66  ? 77.479  65.514  198.880 1.00 242.57 ?  66  ARG K O   1 
ATOM   21229 C CB  . ARG L  6 66  ? 80.451  64.904  199.042 1.00 248.17 ?  66  ARG K CB  1 
ATOM   21230 C CG  . ARG L  6 66  ? 81.885  65.148  198.661 1.00 253.70 ?  66  ARG K CG  1 
ATOM   21231 C CD  . ARG L  6 66  ? 82.370  63.995  197.806 1.00 255.62 ?  66  ARG K CD  1 
ATOM   21232 N NE  . ARG L  6 66  ? 82.132  62.697  198.431 1.00 249.56 ?  66  ARG K NE  1 
ATOM   21233 C CZ  . ARG L  6 66  ? 82.046  61.558  197.753 1.00 250.32 ?  66  ARG K CZ  1 
ATOM   21234 N NH1 . ARG L  6 66  ? 82.185  61.563  196.434 1.00 256.87 1  66  ARG K NH1 1 
ATOM   21235 N NH2 . ARG L  6 66  ? 81.829  60.417  198.392 1.00 245.26 ?  66  ARG K NH2 1 
ATOM   21236 N N   . VAL L  6 67  ? 77.847  65.390  201.095 1.00 269.52 ?  67  VAL K N   1 
ATOM   21237 C CA  . VAL L  6 67  ? 76.531  64.853  201.421 1.00 261.04 ?  67  VAL K CA  1 
ATOM   21238 C C   . VAL L  6 67  ? 75.598  65.951  201.921 1.00 259.24 ?  67  VAL K C   1 
ATOM   21239 O O   . VAL L  6 67  ? 76.028  66.952  202.511 1.00 259.27 ?  67  VAL K O   1 
ATOM   21240 C CB  . VAL L  6 67  ? 76.661  63.712  202.456 1.00 250.82 ?  67  VAL K CB  1 
ATOM   21241 C CG1 . VAL L  6 67  ? 76.961  64.265  203.839 1.00 244.26 ?  67  VAL K CG1 1 
ATOM   21242 C CG2 . VAL L  6 67  ? 75.412  62.849  202.474 1.00 241.82 ?  67  VAL K CG2 1 
ATOM   21243 N N   . HIS L  6 68  ? 74.300  65.766  201.660 1.00 264.60 ?  68  HIS K N   1 
ATOM   21244 C CA  . HIS L  6 68  ? 73.223  66.655  202.094 1.00 261.55 ?  68  HIS K CA  1 
ATOM   21245 C C   . HIS L  6 68  ? 72.009  65.783  202.391 1.00 255.12 ?  68  HIS K C   1 
ATOM   21246 O O   . HIS L  6 68  ? 71.623  64.954  201.561 1.00 250.92 ?  68  HIS K O   1 
ATOM   21247 C CB  . HIS L  6 68  ? 72.840  67.730  201.054 1.00 265.42 ?  68  HIS K CB  1 
ATOM   21248 C CG  . HIS L  6 68  ? 73.921  68.721  200.723 1.00 273.16 ?  68  HIS K CG  1 
ATOM   21249 N ND1 . HIS L  6 68  ? 75.254  68.391  200.614 1.00 276.28 ?  68  HIS K ND1 1 
ATOM   21250 C CD2 . HIS L  6 68  ? 73.850  70.054  200.488 1.00 277.50 ?  68  HIS K CD2 1 
ATOM   21251 C CE1 . HIS L  6 68  ? 75.956  69.472  200.320 1.00 278.26 ?  68  HIS K CE1 1 
ATOM   21252 N NE2 . HIS L  6 68  ? 75.126  70.495  200.238 1.00 279.40 ?  68  HIS K NE2 1 
ATOM   21253 N N   . LEU L  6 69  ? 71.418  65.971  203.569 1.00 258.96 ?  69  LEU K N   1 
ATOM   21254 C CA  . LEU L  6 69  ? 70.249  65.228  204.020 1.00 254.46 ?  69  LEU K CA  1 
ATOM   21255 C C   . LEU L  6 69  ? 69.072  66.159  204.277 1.00 253.94 ?  69  LEU K C   1 
ATOM   21256 O O   . LEU L  6 69  ? 69.233  67.359  204.519 1.00 255.77 ?  69  LEU K O   1 
ATOM   21257 C CB  . LEU L  6 69  ? 70.539  64.417  205.293 1.00 250.28 ?  69  LEU K CB  1 
ATOM   21258 C CG  . LEU L  6 69  ? 71.523  63.252  205.193 1.00 249.70 ?  69  LEU K CG  1 
ATOM   21259 C CD1 . LEU L  6 69  ? 71.669  62.578  206.547 1.00 245.83 ?  69  LEU K CD1 1 
ATOM   21260 C CD2 . LEU L  6 69  ? 71.040  62.253  204.145 1.00 248.92 ?  69  LEU K CD2 1 
ATOM   21261 N N   . SER L  6 70  ? 67.878  65.579  204.217 1.00 258.11 ?  70  SER K N   1 
ATOM   21262 C CA  . SER L  6 70  ? 66.657  66.339  204.429 1.00 254.45 ?  70  SER K CA  1 
ATOM   21263 C C   . SER L  6 70  ? 65.557  65.371  204.833 1.00 248.84 ?  70  SER K C   1 
ATOM   21264 O O   . SER L  6 70  ? 65.646  64.161  204.600 1.00 246.29 ?  70  SER K O   1 
ATOM   21265 C CB  . SER L  6 70  ? 66.254  67.127  203.180 1.00 259.11 ?  70  SER K CB  1 
ATOM   21266 O OG  . SER L  6 70  ? 66.027  66.261  202.083 1.00 256.06 ?  70  SER K OG  1 
ATOM   21267 N N   . LEU L  6 71  ? 64.517  65.933  205.447 1.00 256.10 ?  71  LEU K N   1 
ATOM   21268 C CA  . LEU L  6 71  ? 63.364  65.178  205.909 1.00 253.43 ?  71  LEU K CA  1 
ATOM   21269 C C   . LEU L  6 71  ? 62.101  65.830  205.373 1.00 255.02 ?  71  LEU K C   1 
ATOM   21270 O O   . LEU L  6 71  ? 61.860  67.014  205.629 1.00 256.45 ?  71  LEU K O   1 
ATOM   21271 C CB  . LEU L  6 71  ? 63.317  65.165  207.435 1.00 250.64 ?  71  LEU K CB  1 
ATOM   21272 C CG  . LEU L  6 71  ? 64.413  64.445  208.215 1.00 248.73 ?  71  LEU K CG  1 
ATOM   21273 C CD1 . LEU L  6 71  ? 64.512  65.090  209.577 1.00 248.17 ?  71  LEU K CD1 1 
ATOM   21274 C CD2 . LEU L  6 71  ? 64.117  62.974  208.360 1.00 246.31 ?  71  LEU K CD2 1 
ATOM   21275 N N   . ASP L  6 72  ? 61.296  65.076  204.638 1.00 266.40 ?  72  ASP K N   1 
ATOM   21276 C CA  . ASP L  6 72  ? 60.039  65.602  204.116 1.00 268.07 ?  72  ASP K CA  1 
ATOM   21277 C C   . ASP L  6 72  ? 58.931  65.174  205.074 1.00 265.52 ?  72  ASP K C   1 
ATOM   21278 O O   . ASP L  6 72  ? 58.467  64.032  205.035 1.00 263.92 ?  72  ASP K O   1 
ATOM   21279 C CB  . ASP L  6 72  ? 59.770  65.149  202.687 1.00 270.09 ?  72  ASP K CB  1 
ATOM   21280 C CG  . ASP L  6 72  ? 58.757  66.041  201.986 1.00 272.86 ?  72  ASP K CG  1 
ATOM   21281 O OD1 . ASP L  6 72  ? 57.921  66.663  202.679 1.00 275.91 ?  72  ASP K OD1 1 
ATOM   21282 O OD2 . ASP L  6 72  ? 58.809  66.141  200.743 1.00 276.04 -1 72  ASP K OD2 1 
ATOM   21283 N N   . LYS L  6 73  ? 58.504  66.099  205.933 1.00 260.87 ?  73  LYS K N   1 
ATOM   21284 C CA  . LYS L  6 73  ? 57.472  65.795  206.914 1.00 258.98 ?  73  LYS K CA  1 
ATOM   21285 C C   . LYS L  6 73  ? 56.093  65.759  206.276 1.00 260.34 ?  73  LYS K C   1 
ATOM   21286 O O   . LYS L  6 73  ? 55.156  65.216  206.870 1.00 259.13 ?  73  LYS K O   1 
ATOM   21287 C CB  . LYS L  6 73  ? 57.485  66.821  208.043 1.00 258.76 ?  73  LYS K CB  1 
ATOM   21288 C CG  . LYS L  6 73  ? 58.794  66.896  208.795 1.00 259.04 ?  73  LYS K CG  1 
ATOM   21289 C CD  . LYS L  6 73  ? 58.706  67.945  209.879 1.00 260.67 ?  73  LYS K CD  1 
ATOM   21290 C CE  . LYS L  6 73  ? 58.424  69.325  209.317 1.00 262.58 ?  73  LYS K CE  1 
ATOM   21291 N NZ  . LYS L  6 73  ? 58.331  70.346  210.400 1.00 260.04 1  73  LYS K NZ  1 
ATOM   21292 N N   . SER L  6 74  ? 55.965  66.325  205.076 1.00 273.07 ?  74  SER K N   1 
ATOM   21293 C CA  . SER L  6 74  ? 54.700  66.354  204.355 1.00 275.86 ?  74  SER K CA  1 
ATOM   21294 C C   . SER L  6 74  ? 54.481  65.035  203.629 1.00 275.21 ?  74  SER K C   1 
ATOM   21295 O O   . SER L  6 74  ? 53.351  64.536  203.562 1.00 275.38 ?  74  SER K O   1 
ATOM   21296 C CB  . SER L  6 74  ? 54.686  67.518  203.368 1.00 275.57 ?  74  SER K CB  1 
ATOM   21297 O OG  . SER L  6 74  ? 55.738  67.375  202.435 1.00 275.78 ?  74  SER K OG  1 
ATOM   21298 N N   . LYS L  6 75  ? 55.551  64.463  203.081 1.00 262.41 ?  75  LYS K N   1 
ATOM   21299 C CA  . LYS L  6 75  ? 55.493  63.209  202.349 1.00 261.76 ?  75  LYS K CA  1 
ATOM   21300 C C   . LYS L  6 75  ? 55.931  62.037  203.213 1.00 258.68 ?  75  LYS K C   1 
ATOM   21301 O O   . LYS L  6 75  ? 55.862  60.888  202.763 1.00 257.98 ?  75  LYS K O   1 
ATOM   21302 C CB  . LYS L  6 75  ? 56.381  63.275  201.102 1.00 263.74 ?  75  LYS K CB  1 
ATOM   21303 C CG  . LYS L  6 75  ? 56.016  64.345  200.090 1.00 267.36 ?  75  LYS K CG  1 
ATOM   21304 C CD  . LYS L  6 75  ? 56.961  64.274  198.900 1.00 269.53 ?  75  LYS K CD  1 
ATOM   21305 C CE  . LYS L  6 75  ? 56.648  65.334  197.861 1.00 273.61 ?  75  LYS K CE  1 
ATOM   21306 N NZ  . LYS L  6 75  ? 57.583  65.261  196.703 1.00 276.14 1  75  LYS K NZ  1 
ATOM   21307 N N   . ASN L  6 76  ? 56.376  62.308  204.440 1.00 260.40 ?  76  ASN K N   1 
ATOM   21308 C CA  . ASN L  6 76  ? 56.809  61.294  205.397 1.00 253.75 ?  76  ASN K CA  1 
ATOM   21309 C C   . ASN L  6 76  ? 57.892  60.397  204.796 1.00 251.30 ?  76  ASN K C   1 
ATOM   21310 O O   . ASN L  6 76  ? 57.714  59.192  204.606 1.00 249.31 ?  76  ASN K O   1 
ATOM   21311 C CB  . ASN L  6 76  ? 55.608  60.479  205.889 1.00 253.18 ?  76  ASN K CB  1 
ATOM   21312 C CG  . ASN L  6 76  ? 55.932  59.640  207.105 1.00 249.20 ?  76  ASN K CG  1 
ATOM   21313 O OD1 . ASN L  6 76  ? 55.849  60.109  208.242 1.00 246.03 ?  76  ASN K OD1 1 
ATOM   21314 N ND2 . ASN L  6 76  ? 56.308  58.391  206.873 1.00 247.51 ?  76  ASN K ND2 1 
ATOM   21315 N N   . LEU L  6 77  ? 59.035  61.012  204.495 1.00 251.89 ?  77  LEU K N   1 
ATOM   21316 C CA  . LEU L  6 77  ? 60.156  60.277  203.929 1.00 249.70 ?  77  LEU K CA  1 
ATOM   21317 C C   . LEU L  6 77  ? 61.461  60.986  204.260 1.00 249.13 ?  77  LEU K C   1 
ATOM   21318 O O   . LEU L  6 77  ? 61.480  62.133  204.716 1.00 251.12 ?  77  LEU K O   1 
ATOM   21319 C CB  . LEU L  6 77  ? 60.012  60.103  202.409 1.00 254.26 ?  77  LEU K CB  1 
ATOM   21320 C CG  . LEU L  6 77  ? 59.723  61.314  201.516 1.00 255.65 ?  77  LEU K CG  1 
ATOM   21321 C CD1 . LEU L  6 77  ? 61.001  62.069  201.162 1.00 253.46 ?  77  LEU K CD1 1 
ATOM   21322 C CD2 . LEU L  6 77  ? 59.002  60.869  200.258 1.00 256.17 ?  77  LEU K CD2 1 
ATOM   21323 N N   . VAL L  6 78  ? 62.558  60.270  204.033 1.00 236.67 ?  78  VAL K N   1 
ATOM   21324 C CA  . VAL L  6 78  ? 63.910  60.760  204.263 1.00 235.49 ?  78  VAL K CA  1 
ATOM   21325 C C   . VAL L  6 78  ? 64.600  60.846  202.910 1.00 235.96 ?  78  VAL K C   1 
ATOM   21326 O O   . VAL L  6 78  ? 64.482  59.929  202.089 1.00 236.63 ?  78  VAL K O   1 
ATOM   21327 C CB  . VAL L  6 78  ? 64.694  59.839  205.220 1.00 234.27 ?  78  VAL K CB  1 
ATOM   21328 C CG1 . VAL L  6 78  ? 66.033  60.461  205.589 1.00 233.08 ?  78  VAL K CG1 1 
ATOM   21329 C CG2 . VAL L  6 78  ? 63.875  59.528  206.462 1.00 234.05 ?  78  VAL K CG2 1 
ATOM   21330 N N   . SER L  6 79  ? 65.312  61.941  202.670 1.00 233.50 ?  79  SER K N   1 
ATOM   21331 C CA  . SER L  6 79  ? 65.977  62.140  201.392 1.00 241.22 ?  79  SER K CA  1 
ATOM   21332 C C   . SER L  6 79  ? 67.487  62.129  201.598 1.00 243.51 ?  79  SER K C   1 
ATOM   21333 O O   . SER L  6 79  ? 67.982  62.284  202.717 1.00 238.87 ?  79  SER K O   1 
ATOM   21334 C CB  . SER L  6 79  ? 65.525  63.453  200.743 1.00 243.94 ?  79  SER K CB  1 
ATOM   21335 O OG  . SER L  6 79  ? 66.243  63.714  199.552 1.00 254.17 ?  79  SER K OG  1 
ATOM   21336 N N   . LEU L  6 80  ? 68.223  61.948  200.501 1.00 243.09 ?  80  LEU K N   1 
ATOM   21337 C CA  . LEU L  6 80  ? 69.679  61.928  200.563 1.00 244.23 ?  80  LEU K CA  1 
ATOM   21338 C C   . LEU L  6 80  ? 70.280  62.466  199.270 1.00 253.80 ?  80  LEU K C   1 
ATOM   21339 O O   . LEU L  6 80  ? 69.766  62.189  198.185 1.00 258.91 ?  80  LEU K O   1 
ATOM   21340 C CB  . LEU L  6 80  ? 70.170  60.500  200.833 1.00 240.85 ?  80  LEU K CB  1 
ATOM   21341 C CG  . LEU L  6 80  ? 71.674  60.236  200.883 1.00 240.74 ?  80  LEU K CG  1 
ATOM   21342 C CD1 . LEU L  6 80  ? 71.996  59.264  201.991 1.00 238.57 ?  80  LEU K CD1 1 
ATOM   21343 C CD2 . LEU L  6 80  ? 72.169  59.676  199.569 1.00 250.97 ?  80  LEU K CD2 1 
ATOM   21344 N N   . ARG L  6 81  ? 71.359  63.244  199.392 1.00 239.50 ?  81  ARG K N   1 
ATOM   21345 C CA  . ARG L  6 81  ? 72.054  63.812  198.239 1.00 250.52 ?  81  ARG K CA  1 
ATOM   21346 C C   . ARG L  6 81  ? 73.567  63.698  198.397 1.00 251.26 ?  81  ARG K C   1 
ATOM   21347 O O   . ARG L  6 81  ? 74.106  64.038  199.453 1.00 246.29 ?  81  ARG K O   1 
ATOM   21348 C CB  . ARG L  6 81  ? 71.641  65.261  197.995 1.00 253.12 ?  81  ARG K CB  1 
ATOM   21349 C CG  . ARG L  6 81  ? 70.239  65.383  197.431 1.00 250.89 ?  81  ARG K CG  1 
ATOM   21350 C CD  . ARG L  6 81  ? 69.888  66.828  197.195 1.00 255.38 ?  81  ARG K CD  1 
ATOM   21351 N NE  . ARG L  6 81  ? 70.820  67.431  196.246 1.00 261.51 ?  81  ARG K NE  1 
ATOM   21352 C CZ  . ARG L  6 81  ? 71.817  68.237  196.594 1.00 264.85 ?  81  ARG K CZ  1 
ATOM   21353 N NH1 . ARG L  6 81  ? 72.623  68.743  195.670 1.00 266.84 1  81  ARG K NH1 1 
ATOM   21354 N NH2 . ARG L  6 81  ? 72.005  68.541  197.870 1.00 267.34 ?  81  ARG K NH2 1 
ATOM   21355 N N   . LEU L  6 82  ? 74.242  63.208  197.350 1.00 235.92 ?  82  LEU K N   1 
ATOM   21356 C CA  . LEU L  6 82  ? 75.697  63.036  197.320 1.00 235.52 ?  82  LEU K CA  1 
ATOM   21357 C C   . LEU L  6 82  ? 76.277  63.617  196.035 1.00 236.63 ?  82  LEU K C   1 
ATOM   21358 O O   . LEU L  6 82  ? 76.133  63.022  194.963 1.00 237.64 ?  82  LEU K O   1 
ATOM   21359 C CB  . LEU L  6 82  ? 76.072  61.558  197.437 1.00 235.27 ?  82  LEU K CB  1 
ATOM   21360 C CG  . LEU L  6 82  ? 77.560  61.193  197.457 1.00 234.94 ?  82  LEU K CG  1 
ATOM   21361 C CD1 . LEU L  6 82  ? 78.279  61.867  198.610 1.00 233.76 ?  82  LEU K CD1 1 
ATOM   21362 C CD2 . LEU L  6 82  ? 77.744  59.679  197.505 1.00 234.89 ?  82  LEU K CD2 1 
ATOM   21363 N N   . THR L  6 83  A 76.947  64.764  196.141 1.00 243.45 ?  82  THR K N   1 
ATOM   21364 C CA  . THR L  6 83  A 77.528  65.432  194.983 1.00 252.85 ?  82  THR K CA  1 
ATOM   21365 C C   . THR L  6 83  A 78.952  64.943  194.719 1.00 256.84 ?  82  THR K C   1 
ATOM   21366 O O   . THR L  6 83  A 79.708  64.644  195.647 1.00 253.32 ?  82  THR K O   1 
ATOM   21367 C CB  . THR L  6 83  A 77.542  66.948  195.213 1.00 254.16 ?  82  THR K CB  1 
ATOM   21368 O OG1 . THR L  6 83  A 76.209  67.407  195.473 1.00 250.85 ?  82  THR K OG1 1 
ATOM   21369 C CG2 . THR L  6 83  A 78.101  67.692  194.006 1.00 261.09 ?  82  THR K CG2 1 
ATOM   21370 N N   . GLY L  6 84  B 79.316  64.872  193.435 1.00 250.08 ?  82  GLY K N   1 
ATOM   21371 C CA  . GLY L  6 84  B 80.645  64.432  193.049 1.00 250.78 ?  82  GLY K CA  1 
ATOM   21372 C C   . GLY L  6 84  B 80.984  62.992  193.378 1.00 249.66 ?  82  GLY K C   1 
ATOM   21373 O O   . GLY L  6 84  B 81.917  62.738  194.144 1.00 249.66 ?  82  GLY K O   1 
ATOM   21374 N N   . VAL L  6 85  C 80.258  62.040  192.805 1.00 242.67 ?  82  VAL K N   1 
ATOM   21375 C CA  . VAL L  6 85  C 80.486  60.631  193.105 1.00 242.31 ?  82  VAL K CA  1 
ATOM   21376 C C   . VAL L  6 85  C 81.644  60.075  192.285 1.00 243.12 ?  82  VAL K C   1 
ATOM   21377 O O   . VAL L  6 85  C 81.936  60.530  191.172 1.00 244.28 ?  82  VAL K O   1 
ATOM   21378 C CB  . VAL L  6 85  C 79.198  59.825  192.852 1.00 242.61 ?  82  VAL K CB  1 
ATOM   21379 C CG1 . VAL L  6 85  C 78.113  60.208  193.858 1.00 241.74 ?  82  VAL K CG1 1 
ATOM   21380 C CG2 . VAL L  6 85  C 78.732  60.050  191.431 1.00 244.06 ?  82  VAL K CG2 1 
ATOM   21381 N N   . THR L  6 86  ? 82.316  59.075  192.856 1.00 239.01 ?  83  THR K N   1 
ATOM   21382 C CA  . THR L  6 86  ? 83.420  58.381  192.204 1.00 240.02 ?  83  THR K CA  1 
ATOM   21383 C C   . THR L  6 86  ? 83.211  56.875  192.305 1.00 237.00 ?  83  THR K C   1 
ATOM   21384 O O   . THR L  6 86  ? 82.137  56.424  192.715 1.00 234.75 ?  83  THR K O   1 
ATOM   21385 C CB  . THR L  6 86  ? 84.758  58.770  192.833 1.00 238.74 ?  83  THR K CB  1 
ATOM   21386 O OG1 . THR L  6 86  ? 84.715  58.504  194.241 1.00 237.53 ?  83  THR K OG1 1 
ATOM   21387 C CG2 . THR L  6 86  ? 85.054  60.241  192.594 1.00 240.50 ?  83  THR K CG2 1 
ATOM   21388 N N   . ALA L  6 87  ? 84.243  56.089  191.989 1.00 229.75 ?  84  ALA K N   1 
ATOM   21389 C CA  . ALA L  6 87  ? 84.110  54.639  192.049 1.00 229.80 ?  84  ALA K CA  1 
ATOM   21390 C C   . ALA L  6 87  ? 84.123  54.119  193.477 1.00 228.48 ?  84  ALA K C   1 
ATOM   21391 O O   . ALA L  6 87  ? 83.726  52.973  193.712 1.00 228.37 ?  84  ALA K O   1 
ATOM   21392 C CB  . ALA L  6 87  ? 85.227  53.967  191.251 1.00 230.85 ?  84  ALA K CB  1 
ATOM   21393 N N   . ALA L  6 88  ? 84.579  54.934  194.426 1.00 245.09 ?  85  ALA K N   1 
ATOM   21394 C CA  . ALA L  6 88  ? 84.648  54.534  195.823 1.00 240.02 ?  85  ALA K CA  1 
ATOM   21395 C C   . ALA L  6 88  ? 83.291  54.618  196.502 1.00 234.17 ?  85  ALA K C   1 
ATOM   21396 O O   . ALA L  6 88  ? 83.109  54.036  197.576 1.00 228.15 ?  85  ALA K O   1 
ATOM   21397 C CB  . ALA L  6 88  ? 85.659  55.400  196.577 1.00 240.32 ?  85  ALA K CB  1 
ATOM   21398 N N   . ASP L  6 89  ? 82.344  55.331  195.897 1.00 240.92 ?  86  ASP K N   1 
ATOM   21399 C CA  . ASP L  6 89  ? 81.009  55.523  196.444 1.00 236.40 ?  86  ASP K CA  1 
ATOM   21400 C C   . ASP L  6 89  ? 80.052  54.398  196.073 1.00 234.17 ?  86  ASP K C   1 
ATOM   21401 O O   . ASP L  6 89  ? 78.900  54.412  196.514 1.00 228.36 ?  86  ASP K O   1 
ATOM   21402 C CB  . ASP L  6 89  ? 80.438  56.850  195.934 1.00 238.21 ?  86  ASP K CB  1 
ATOM   21403 C CG  . ASP L  6 89  ? 81.206  58.054  196.444 1.00 242.21 ?  86  ASP K CG  1 
ATOM   21404 O OD1 . ASP L  6 89  ? 81.758  57.989  197.563 1.00 237.52 ?  86  ASP K OD1 1 
ATOM   21405 O OD2 . ASP L  6 89  ? 81.272  59.064  195.710 1.00 244.36 -1 86  ASP K OD2 1 
ATOM   21406 N N   . SER L  6 90  ? 80.507  53.429  195.288 1.00 241.44 ?  87  SER K N   1 
ATOM   21407 C CA  . SER L  6 90  ? 79.718  52.274  194.861 1.00 238.79 ?  87  SER K CA  1 
ATOM   21408 C C   . SER L  6 90  ? 79.489  51.326  196.037 1.00 230.73 ?  87  SER K C   1 
ATOM   21409 O O   . SER L  6 90  ? 80.393  50.582  196.424 1.00 230.52 ?  87  SER K O   1 
ATOM   21410 C CB  . SER L  6 90  ? 80.424  51.566  193.709 1.00 240.72 ?  87  SER K CB  1 
ATOM   21411 O OG  . SER L  6 90  ? 79.729  50.401  193.296 1.00 237.30 ?  87  SER K OG  1 
ATOM   21412 N N   . ALA L  6 91  ? 78.291  51.334  196.623 1.00 234.01 ?  88  ALA K N   1 
ATOM   21413 C CA  . ALA L  6 91  ? 78.034  50.478  197.782 1.00 228.71 ?  88  ALA K CA  1 
ATOM   21414 C C   . ALA L  6 91  ? 76.532  50.220  197.906 1.00 221.94 ?  88  ALA K C   1 
ATOM   21415 O O   . ALA L  6 91  ? 75.751  50.558  197.011 1.00 221.19 ?  88  ALA K O   1 
ATOM   21416 C CB  . ALA L  6 91  ? 78.602  51.115  199.054 1.00 228.64 ?  88  ALA K CB  1 
ATOM   21417 N N   . ILE L  6 92  ? 76.130  49.604  199.018 1.00 225.20 ?  89  ILE K N   1 
ATOM   21418 C CA  . ILE L  6 92  ? 74.732  49.302  199.326 1.00 219.81 ?  89  ILE K CA  1 
ATOM   21419 C C   . ILE L  6 92  ? 74.274  50.228  200.450 1.00 220.38 ?  89  ILE K C   1 
ATOM   21420 O O   . ILE L  6 92  ? 74.720  50.080  201.594 1.00 222.17 ?  89  ILE K O   1 
ATOM   21421 C CB  . ILE L  6 92  ? 74.562  47.829  199.730 1.00 219.49 ?  89  ILE K CB  1 
ATOM   21422 C CG1 . ILE L  6 92  ? 75.137  46.893  198.663 1.00 219.28 ?  89  ILE K CG1 1 
ATOM   21423 C CG2 . ILE L  6 92  ? 73.094  47.501  199.997 1.00 215.51 ?  89  ILE K CG2 1 
ATOM   21424 C CD1 . ILE L  6 92  ? 75.031  45.434  199.044 1.00 221.80 ?  89  ILE K CD1 1 
ATOM   21425 N N   . TYR L  6 93  ? 73.391  51.184  200.142 1.00 227.98 ?  90  TYR K N   1 
ATOM   21426 C CA  . TYR L  6 93  ? 72.928  52.181  201.112 1.00 226.73 ?  90  TYR K CA  1 
ATOM   21427 C C   . TYR L  6 93  ? 71.698  51.738  201.908 1.00 219.00 ?  90  TYR K C   1 
ATOM   21428 O O   . TYR L  6 93  ? 70.669  51.393  201.315 1.00 215.98 ?  90  TYR K O   1 
ATOM   21429 C CB  . TYR L  6 93  ? 72.606  53.495  200.397 1.00 233.39 ?  90  TYR K CB  1 
ATOM   21430 C CG  . TYR L  6 93  ? 73.794  54.195  199.794 1.00 239.34 ?  90  TYR K CG  1 
ATOM   21431 C CD1 . TYR L  6 93  ? 74.323  53.804  198.570 1.00 241.85 ?  90  TYR K CD1 1 
ATOM   21432 C CD2 . TYR L  6 93  ? 74.372  55.271  200.444 1.00 238.90 ?  90  TYR K CD2 1 
ATOM   21433 C CE1 . TYR L  6 93  ? 75.413  54.458  198.030 1.00 247.76 ?  90  TYR K CE1 1 
ATOM   21434 C CE2 . TYR L  6 93  ? 75.452  55.927  199.915 1.00 245.11 ?  90  TYR K CE2 1 
ATOM   21435 C CZ  . TYR L  6 93  ? 75.970  55.522  198.711 1.00 250.08 ?  90  TYR K CZ  1 
ATOM   21436 O OH  . TYR L  6 93  ? 77.053  56.195  198.200 1.00 255.42 ?  90  TYR K OH  1 
ATOM   21437 N N   . TYR L  6 94  ? 71.806  51.736  203.245 1.00 226.38 ?  91  TYR K N   1 
ATOM   21438 C CA  . TYR L  6 94  ? 70.710  51.362  204.135 1.00 224.31 ?  91  TYR K CA  1 
ATOM   21439 C C   . TYR L  6 94  ? 70.181  52.595  204.868 1.00 224.94 ?  91  TYR K C   1 
ATOM   21440 O O   . TYR L  6 94  ? 70.921  53.551  205.119 1.00 225.85 ?  91  TYR K O   1 
ATOM   21441 C CB  . TYR L  6 94  ? 71.117  50.308  205.180 1.00 223.41 ?  91  TYR K CB  1 
ATOM   21442 C CG  . TYR L  6 94  ? 71.612  48.992  204.623 1.00 221.45 ?  91  TYR K CG  1 
ATOM   21443 C CD1 . TYR L  6 94  ? 70.718  47.971  204.332 1.00 218.25 ?  91  TYR K CD1 1 
ATOM   21444 C CD2 . TYR L  6 94  ? 72.967  48.742  204.452 1.00 225.44 ?  91  TYR K CD2 1 
ATOM   21445 C CE1 . TYR L  6 94  ? 71.152  46.762  203.834 1.00 217.97 ?  91  TYR K CE1 1 
ATOM   21446 C CE2 . TYR L  6 94  ? 73.413  47.524  203.959 1.00 227.74 ?  91  TYR K CE2 1 
ATOM   21447 C CZ  . TYR L  6 94  ? 72.498  46.538  203.656 1.00 223.93 ?  91  TYR K CZ  1 
ATOM   21448 O OH  . TYR L  6 94  ? 72.922  45.325  203.161 1.00 225.90 ?  91  TYR K OH  1 
ATOM   21449 N N   . CYS L  6 95  ? 68.885  52.565  205.192 1.00 239.21 ?  92  CYS K N   1 
ATOM   21450 C CA  . CYS L  6 95  ? 68.193  53.578  205.992 1.00 237.42 ?  92  CYS K CA  1 
ATOM   21451 C C   . CYS L  6 95  ? 67.624  52.884  207.229 1.00 234.42 ?  92  CYS K C   1 
ATOM   21452 O O   . CYS L  6 95  ? 66.845  51.933  207.101 1.00 232.26 ?  92  CYS K O   1 
ATOM   21453 C CB  . CYS L  6 95  ? 67.128  54.338  205.190 1.00 232.20 ?  92  CYS K CB  1 
ATOM   21454 S SG  . CYS L  6 95  ? 65.619  53.510  204.742 1.00 251.82 ?  92  CYS K SG  1 
ATOM   21455 N N   . ALA L  6 96  ? 68.027  53.328  208.419 1.00 221.40 ?  93  ALA K N   1 
ATOM   21456 C CA  . ALA L  6 96  ? 67.612  52.666  209.649 1.00 225.09 ?  93  ALA K CA  1 
ATOM   21457 C C   . ALA L  6 96  ? 67.230  53.679  210.717 1.00 224.91 ?  93  ALA K C   1 
ATOM   21458 O O   . ALA L  6 96  ? 67.802  54.769  210.795 1.00 224.01 ?  93  ALA K O   1 
ATOM   21459 C CB  . ALA L  6 96  ? 68.731  51.765  210.187 1.00 231.44 ?  93  ALA K CB  1 
ATOM   21460 N N   . THR L  6 97  ? 66.240  53.306  211.533 1.00 216.66 ?  94  THR K N   1 
ATOM   21461 C CA  . THR L  6 97  ? 65.832  54.153  212.642 1.00 217.64 ?  94  THR K CA  1 
ATOM   21462 C C   . THR L  6 97  ? 66.979  54.219  213.647 1.00 223.58 ?  94  THR K C   1 
ATOM   21463 O O   . THR L  6 97  ? 67.816  53.316  213.722 1.00 228.55 ?  94  THR K O   1 
ATOM   21464 C CB  . THR L  6 97  ? 64.561  53.568  213.285 1.00 217.79 ?  94  THR K CB  1 
ATOM   21465 O OG1 . THR L  6 97  ? 63.434  53.789  212.428 1.00 211.21 ?  94  THR K OG1 1 
ATOM   21466 C CG2 . THR L  6 97  ? 64.259  54.168  214.655 1.00 220.85 ?  94  THR K CG2 1 
ATOM   21467 N N   . THR L  6 98  ? 67.018  55.294  214.434 1.00 212.03 ?  95  THR K N   1 
ATOM   21468 C CA  . THR L  6 98  ? 68.111  55.467  215.382 1.00 217.59 ?  95  THR K CA  1 
ATOM   21469 C C   . THR L  6 98  ? 67.628  55.926  216.749 1.00 221.30 ?  95  THR K C   1 
ATOM   21470 O O   . THR L  6 98  ? 66.951  56.952  216.853 1.00 218.25 ?  95  THR K O   1 
ATOM   21471 C CB  . THR L  6 98  ? 69.110  56.482  214.826 1.00 215.38 ?  95  THR K CB  1 
ATOM   21472 O OG1 . THR L  6 98  ? 69.554  56.049  213.533 1.00 212.58 ?  95  THR K OG1 1 
ATOM   21473 C CG2 . THR L  6 98  ? 70.299  56.618  215.752 1.00 221.35 ?  95  THR K CG2 1 
ATOM   21474 N N   . LYS L  6 99  ? 67.958  55.162  217.788 1.00 204.31 ?  96  LYS K N   1 
ATOM   21475 C CA  . LYS L  6 99  ? 67.676  55.541  219.166 1.00 209.07 ?  96  LYS K CA  1 
ATOM   21476 C C   . LYS L  6 99  ? 68.982  55.922  219.853 1.00 214.43 ?  96  LYS K C   1 
ATOM   21477 O O   . LYS L  6 99  ? 69.989  55.216  219.725 1.00 216.95 ?  96  LYS K O   1 
ATOM   21478 C CB  . LYS L  6 99  ? 66.919  54.456  219.938 1.00 212.69 ?  96  LYS K CB  1 
ATOM   21479 C CG  . LYS L  6 99  ? 65.520  54.174  219.387 1.00 207.24 ?  96  LYS K CG  1 
ATOM   21480 C CD  . LYS L  6 99  ? 64.753  53.206  220.285 1.00 209.94 ?  96  LYS K CD  1 
ATOM   21481 C CE  . LYS L  6 99  ? 63.374  52.873  219.725 1.00 203.80 ?  96  LYS K CE  1 
ATOM   21482 N NZ  . LYS L  6 99  ? 63.402  52.420  218.311 1.00 198.97 1  96  LYS K NZ  1 
ATOM   21483 N N   . HIS L  6 100 ? 68.958  57.034  220.576 1.00 192.65 ?  97  HIS K N   1 
ATOM   21484 C CA  . HIS L  6 100 ? 70.127  57.578  221.249 1.00 196.84 ?  97  HIS K CA  1 
ATOM   21485 C C   . HIS L  6 100 ? 70.197  57.074  222.686 1.00 205.65 ?  97  HIS K C   1 
ATOM   21486 O O   . HIS L  6 100 ? 69.194  56.672  223.283 1.00 207.24 ?  97  HIS K O   1 
ATOM   21487 C CB  . HIS L  6 100 ? 70.122  59.108  221.287 1.00 191.88 ?  97  HIS K CB  1 
ATOM   21488 C CG  . HIS L  6 100 ? 68.974  59.694  222.046 1.00 192.90 ?  97  HIS K CG  1 
ATOM   21489 N ND1 . HIS L  6 100 ? 67.763  60.009  221.469 1.00 187.23 ?  97  HIS K ND1 1 
ATOM   21490 C CD2 . HIS L  6 100 ? 68.861  60.017  223.357 1.00 199.25 ?  97  HIS K CD2 1 
ATOM   21491 C CE1 . HIS L  6 100 ? 66.954  60.502  222.391 1.00 189.93 ?  97  HIS K CE1 1 
ATOM   21492 N NE2 . HIS L  6 100 ? 67.596  60.517  223.545 1.00 197.42 ?  97  HIS K NE2 1 
ATOM   21493 N N   . GLY L  6 101 ? 71.401  57.109  223.244 1.00 193.48 ?  98  GLY K N   1 
ATOM   21494 C CA  . GLY L  6 101 ? 71.589  56.723  224.621 1.00 202.47 ?  98  GLY K CA  1 
ATOM   21495 C C   . GLY L  6 101 ? 72.660  57.631  225.186 1.00 205.02 ?  98  GLY K C   1 
ATOM   21496 O O   . GLY L  6 101 ? 73.476  58.193  224.455 1.00 201.58 ?  98  GLY K O   1 
ATOM   21497 N N   . ARG L  6 102 ? 72.652  57.769  226.505 1.00 208.90 ?  99  ARG K N   1 
ATOM   21498 C CA  . ARG L  6 102 ? 73.594  58.658  227.173 1.00 202.91 ?  99  ARG K CA  1 
ATOM   21499 C C   . ARG L  6 102 ? 74.377  57.890  228.227 1.00 206.33 ?  99  ARG K C   1 
ATOM   21500 O O   . ARG L  6 102 ? 73.806  57.431  229.222 1.00 206.90 ?  99  ARG K O   1 
ATOM   21501 C CB  . ARG L  6 102 ? 72.781  59.842  227.703 1.00 196.05 ?  99  ARG K CB  1 
ATOM   21502 C CG  . ARG L  6 102 ? 73.295  61.223  227.299 1.00 187.76 ?  99  ARG K CG  1 
ATOM   21503 C CD  . ARG L  6 102 ? 72.296  62.222  227.757 1.00 185.73 ?  99  ARG K CD  1 
ATOM   21504 N NE  . ARG L  6 102 ? 71.108  61.726  227.090 1.00 193.41 ?  99  ARG K NE  1 
ATOM   21505 C CZ  . ARG L  6 102 ? 69.943  62.323  227.079 1.00 197.39 ?  99  ARG K CZ  1 
ATOM   21506 N NH1 . ARG L  6 102 ? 68.933  61.771  226.426 1.00 203.61 1  99  ARG K NH1 1 
ATOM   21507 N NH2 . ARG L  6 102 ? 69.784  63.459  227.725 1.00 192.97 ?  99  ARG K NH2 1 
ATOM   21508 N N   . ARG L  6 103 ? 75.686  57.778  228.003 1.00 195.56 ?  100 ARG K N   1 
ATOM   21509 C CA  . ARG L  6 103 ? 76.618  57.073  228.879 1.00 198.94 ?  100 ARG K CA  1 
ATOM   21510 C C   . ARG L  6 103 ? 77.268  58.034  229.872 1.00 196.16 ?  100 ARG K C   1 
ATOM   21511 O O   . ARG L  6 103 ? 78.055  58.898  229.478 1.00 197.46 ?  100 ARG K O   1 
ATOM   21512 C CB  . ARG L  6 103 ? 77.667  56.354  228.033 1.00 204.50 ?  100 ARG K CB  1 
ATOM   21513 C CG  . ARG L  6 103 ? 78.679  55.542  228.803 1.00 207.82 ?  100 ARG K CG  1 
ATOM   21514 C CD  . ARG L  6 103 ? 77.993  54.422  229.532 1.00 213.31 ?  100 ARG K CD  1 
ATOM   21515 N NE  . ARG L  6 103 ? 78.956  53.435  229.993 1.00 217.87 ?  100 ARG K NE  1 
ATOM   21516 C CZ  . ARG L  6 103 ? 79.614  53.513  231.142 1.00 217.11 ?  100 ARG K CZ  1 
ATOM   21517 N NH1 . ARG L  6 103 ? 79.417  54.541  231.956 1.00 211.84 1  100 ARG K NH1 1 
ATOM   21518 N NH2 . ARG L  6 103 ? 80.468  52.558  231.477 1.00 221.62 ?  100 ARG K NH2 1 
ATOM   21519 N N   . ILE L  6 104 A 76.939  57.899  231.155 1.00 214.34 ?  100 ILE K N   1 
ATOM   21520 C CA  . ILE L  6 104 A 77.482  58.758  232.205 1.00 209.01 ?  100 ILE K CA  1 
ATOM   21521 C C   . ILE L  6 104 A 78.595  58.011  232.929 1.00 213.16 ?  100 ILE K C   1 
ATOM   21522 O O   . ILE L  6 104 A 78.387  56.897  233.423 1.00 218.14 ?  100 ILE K O   1 
ATOM   21523 C CB  . ILE L  6 104 A 76.409  59.220  233.207 1.00 204.95 ?  100 ILE K CB  1 
ATOM   21524 C CG1 . ILE L  6 104 A 75.371  60.137  232.543 1.00 199.56 ?  100 ILE K CG1 1 
ATOM   21525 C CG2 . ILE L  6 104 A 77.085  59.870  234.432 1.00 201.74 ?  100 ILE K CG2 1 
ATOM   21526 C CD1 . ILE L  6 104 A 74.197  59.399  231.877 1.00 208.48 ?  100 ILE K CD1 1 
ATOM   21527 N N   . TYR L  6 105 B 79.788  58.620  232.977 1.00 195.15 ?  100 TYR K N   1 
ATOM   21528 C CA  . TYR L  6 105 B 80.948  58.034  233.634 1.00 198.06 ?  100 TYR K CA  1 
ATOM   21529 C C   . TYR L  6 105 B 81.532  58.941  234.705 1.00 199.96 ?  100 TYR K C   1 
ATOM   21530 O O   . TYR L  6 105 B 82.203  58.443  235.616 1.00 202.09 ?  100 TYR K O   1 
ATOM   21531 C CB  . TYR L  6 105 B 82.067  57.726  232.621 1.00 199.79 ?  100 TYR K CB  1 
ATOM   21532 C CG  . TYR L  6 105 B 82.567  58.939  231.853 1.00 200.33 ?  100 TYR K CG  1 
ATOM   21533 C CD1 . TYR L  6 105 B 83.598  59.727  232.360 1.00 202.87 ?  100 TYR K CD1 1 
ATOM   21534 C CD2 . TYR L  6 105 B 82.024  59.291  230.624 1.00 198.44 ?  100 TYR K CD2 1 
ATOM   21535 C CE1 . TYR L  6 105 B 84.063  60.833  231.673 1.00 203.50 ?  100 TYR K CE1 1 
ATOM   21536 C CE2 . TYR L  6 105 B 82.489  60.396  229.927 1.00 199.06 ?  100 TYR K CE2 1 
ATOM   21537 C CZ  . TYR L  6 105 B 83.507  61.163  230.459 1.00 201.60 ?  100 TYR K CZ  1 
ATOM   21538 O OH  . TYR L  6 105 B 83.975  62.265  229.781 1.00 202.34 ?  100 TYR K OH  1 
ATOM   21539 N N   . GLY L  6 106 C 81.293  60.250  234.621 1.00 198.72 ?  100 GLY K N   1 
ATOM   21540 C CA  . GLY L  6 106 C 81.843  61.227  235.538 1.00 200.51 ?  100 GLY K CA  1 
ATOM   21541 C C   . GLY L  6 106 C 80.836  61.726  236.554 1.00 199.00 ?  100 GLY K C   1 
ATOM   21542 O O   . GLY L  6 106 C 80.189  60.930  237.237 1.00 198.17 ?  100 GLY K O   1 
ATOM   21543 N N   . VAL L  6 107 D 80.693  63.044  236.661 1.00 194.66 ?  100 VAL K N   1 
ATOM   21544 C CA  . VAL L  6 107 D 79.817  63.658  237.648 1.00 193.41 ?  100 VAL K CA  1 
ATOM   21545 C C   . VAL L  6 107 D 78.654  64.394  236.981 1.00 190.32 ?  100 VAL K C   1 
ATOM   21546 O O   . VAL L  6 107 D 78.037  65.260  237.600 1.00 189.35 ?  100 VAL K O   1 
ATOM   21547 C CB  . VAL L  6 107 D 80.606  64.592  238.576 1.00 195.82 ?  100 VAL K CB  1 
ATOM   21548 C CG1 . VAL L  6 107 D 81.571  63.788  239.446 1.00 198.72 ?  100 VAL K CG1 1 
ATOM   21549 C CG2 . VAL L  6 107 D 81.341  65.629  237.758 1.00 196.83 ?  100 VAL K CG2 1 
ATOM   21550 N N   . VAL L  6 108 E 78.357  64.071  235.720 1.00 199.10 ?  100 VAL K N   1 
ATOM   21551 C CA  . VAL L  6 108 E 77.234  64.643  234.976 1.00 196.15 ?  100 VAL K CA  1 
ATOM   21552 C C   . VAL L  6 108 E 77.343  66.158  234.838 1.00 196.21 ?  100 VAL K C   1 
ATOM   21553 O O   . VAL L  6 108 E 77.353  66.689  233.721 1.00 195.55 ?  100 VAL K O   1 
ATOM   21554 C CB  . VAL L  6 108 E 75.887  64.278  235.630 1.00 193.73 ?  100 VAL K CB  1 
ATOM   21555 C CG1 . VAL L  6 108 E 74.731  64.784  234.779 1.00 190.70 ?  100 VAL K CG1 1 
ATOM   21556 C CG2 . VAL L  6 108 E 75.776  62.786  235.862 1.00 193.84 ?  100 VAL K CG2 1 
ATOM   21557 N N   . ALA L  6 109 F 77.435  66.860  235.973 1.00 201.06 ?  100 ALA K N   1 
ATOM   21558 C CA  . ALA L  6 109 F 77.444  68.321  235.962 1.00 202.05 ?  100 ALA K CA  1 
ATOM   21559 C C   . ALA L  6 109 F 78.631  68.888  235.196 1.00 206.59 ?  100 ALA K C   1 
ATOM   21560 O O   . ALA L  6 109 F 78.531  69.981  234.628 1.00 212.01 ?  100 ALA K O   1 
ATOM   21561 C CB  . ALA L  6 109 F 77.433  68.857  237.393 1.00 202.75 ?  100 ALA K CB  1 
ATOM   21562 N N   . PHE L  6 110 G 79.753  68.170  235.147 1.00 190.11 ?  100 PHE K N   1 
ATOM   21563 C CA  . PHE L  6 110 G 80.913  68.665  234.422 1.00 192.36 ?  100 PHE K CA  1 
ATOM   21564 C C   . PHE L  6 110 G 80.937  68.183  232.988 1.00 191.57 ?  100 PHE K C   1 
ATOM   21565 O O   . PHE L  6 110 G 82.013  68.113  232.382 1.00 193.72 ?  100 PHE K O   1 
ATOM   21566 C CB  . PHE L  6 110 G 82.223  68.288  235.117 1.00 195.80 ?  100 PHE K CB  1 
ATOM   21567 C CG  . PHE L  6 110 G 82.627  69.240  236.201 1.00 197.51 ?  100 PHE K CG  1 
ATOM   21568 C CD1 . PHE L  6 110 G 83.351  70.381  235.890 1.00 199.15 ?  100 PHE K CD1 1 
ATOM   21569 C CD2 . PHE L  6 110 G 82.327  68.983  237.524 1.00 197.67 ?  100 PHE K CD2 1 
ATOM   21570 C CE1 . PHE L  6 110 G 83.740  71.261  236.873 1.00 200.83 ?  100 PHE K CE1 1 
ATOM   21571 C CE2 . PHE L  6 110 G 82.718  69.860  238.513 1.00 199.36 ?  100 PHE K CE2 1 
ATOM   21572 C CZ  . PHE L  6 110 G 83.424  70.998  238.185 1.00 200.93 ?  100 PHE K CZ  1 
ATOM   21573 N N   . LYS L  6 111 H 79.769  67.842  232.441 1.00 201.46 ?  100 LYS K N   1 
ATOM   21574 C CA  . LYS L  6 111 H 79.644  67.371  231.068 1.00 200.46 ?  100 LYS K CA  1 
ATOM   21575 C C   . LYS L  6 111 H 80.552  66.172  230.817 1.00 202.31 ?  100 LYS K C   1 
ATOM   21576 O O   . LYS L  6 111 H 81.027  65.953  229.700 1.00 203.16 ?  100 LYS K O   1 
ATOM   21577 C CB  . LYS L  6 111 H 79.967  68.522  230.116 1.00 201.39 ?  100 LYS K CB  1 
ATOM   21578 C CG  . LYS L  6 111 H 78.958  69.655  230.230 1.00 199.33 ?  100 LYS K CG  1 
ATOM   21579 C CD  . LYS L  6 111 H 79.279  70.802  229.298 1.00 205.41 ?  100 LYS K CD  1 
ATOM   21580 C CE  . LYS L  6 111 H 78.237  71.900  229.425 1.00 203.99 ?  100 LYS K CE  1 
ATOM   21581 N NZ  . LYS L  6 111 H 78.364  72.917  228.350 1.00 212.66 1  100 LYS K NZ  1 
ATOM   21582 N N   . GLU L  6 112 I 80.789  65.392  231.874 1.00 191.26 ?  100 GLU K N   1 
ATOM   21583 C CA  . GLU L  6 112 I 81.635  64.203  231.825 1.00 193.08 ?  100 GLU K CA  1 
ATOM   21584 C C   . GLU L  6 112 I 80.827  62.990  231.354 1.00 191.02 ?  100 GLU K C   1 
ATOM   21585 O O   . GLU L  6 112 I 80.691  61.981  232.045 1.00 191.12 ?  100 GLU K O   1 
ATOM   21586 C CB  . GLU L  6 112 I 82.254  63.964  233.196 1.00 195.25 ?  100 GLU K CB  1 
ATOM   21587 C CG  . GLU L  6 112 I 83.230  65.050  233.634 1.00 197.77 ?  100 GLU K CG  1 
ATOM   21588 C CD  . GLU L  6 112 I 83.819  64.794  235.010 1.00 199.99 ?  100 GLU K CD  1 
ATOM   21589 O OE1 . GLU L  6 112 I 83.208  64.037  235.790 1.00 199.08 ?  100 GLU K OE1 1 
ATOM   21590 O OE2 . GLU L  6 112 I 84.888  65.361  235.319 1.00 202.72 -1 100 GLU K OE2 1 
ATOM   21591 N N   . TRP L  6 113 J 80.282  63.111  230.142 1.00 203.72 ?  100 TRP K N   1 
ATOM   21592 C CA  . TRP L  6 113 J 79.480  62.051  229.545 1.00 202.19 ?  100 TRP K CA  1 
ATOM   21593 C C   . TRP L  6 113 J 79.549  62.172  228.027 1.00 208.99 ?  100 TRP K C   1 
ATOM   21594 O O   . TRP L  6 113 J 80.125  63.120  227.488 1.00 208.33 ?  100 TRP K O   1 
ATOM   21595 C CB  . TRP L  6 113 J 78.039  62.121  230.074 1.00 201.15 ?  100 TRP K CB  1 
ATOM   21596 C CG  . TRP L  6 113 J 77.284  63.382  229.701 1.00 204.99 ?  100 TRP K CG  1 
ATOM   21597 C CD1 . TRP L  6 113 J 77.802  64.521  229.151 1.00 210.94 ?  100 TRP K CD1 1 
ATOM   21598 C CD2 . TRP L  6 113 J 75.903  63.669  229.976 1.00 202.07 ?  100 TRP K CD2 1 
ATOM   21599 N NE1 . TRP L  6 113 J 76.818  65.465  228.996 1.00 208.85 ?  100 TRP K NE1 1 
ATOM   21600 C CE2 . TRP L  6 113 J 75.645  64.972  229.505 1.00 202.29 ?  100 TRP K CE2 1 
ATOM   21601 C CE3 . TRP L  6 113 J 74.855  62.941  230.549 1.00 199.42 ?  100 TRP K CE3 1 
ATOM   21602 C CZ2 . TRP L  6 113 J 74.384  65.562  229.590 1.00 198.79 ?  100 TRP K CZ2 1 
ATOM   21603 C CZ3 . TRP L  6 113 J 73.604  63.531  230.635 1.00 193.48 ?  100 TRP K CZ3 1 
ATOM   21604 C CH2 . TRP L  6 113 J 73.379  64.826  230.155 1.00 193.21 ?  100 TRP K CH2 1 
ATOM   21605 N N   . PHE L  6 114 K 78.955  61.197  227.335 1.00 207.12 ?  100 PHE K N   1 
ATOM   21606 C CA  . PHE L  6 114 K 78.902  61.234  225.878 1.00 212.50 ?  100 PHE K CA  1 
ATOM   21607 C C   . PHE L  6 114 K 77.702  60.431  225.394 1.00 206.69 ?  100 PHE K C   1 
ATOM   21608 O O   . PHE L  6 114 K 77.298  59.449  226.024 1.00 200.22 ?  100 PHE K O   1 
ATOM   21609 C CB  . PHE L  6 114 K 80.176  60.694  225.212 1.00 217.24 ?  100 PHE K CB  1 
ATOM   21610 C CG  . PHE L  6 114 K 80.405  59.223  225.417 1.00 214.50 ?  100 PHE K CG  1 
ATOM   21611 C CD1 . PHE L  6 114 K 81.040  58.742  226.549 1.00 208.85 ?  100 PHE K CD1 1 
ATOM   21612 C CD2 . PHE L  6 114 K 80.002  58.319  224.444 1.00 210.61 ?  100 PHE K CD2 1 
ATOM   21613 C CE1 . PHE L  6 114 K 81.251  57.380  226.712 1.00 202.67 ?  100 PHE K CE1 1 
ATOM   21614 C CE2 . PHE L  6 114 K 80.208  56.965  224.600 1.00 205.71 ?  100 PHE K CE2 1 
ATOM   21615 C CZ  . PHE L  6 114 K 80.834  56.492  225.734 1.00 202.97 ?  100 PHE K CZ  1 
ATOM   21616 N N   . THR L  6 115 L 77.135  60.868  224.270 1.00 190.26 ?  100 THR K N   1 
ATOM   21617 C CA  . THR L  6 115 L 75.967  60.230  223.675 1.00 187.76 ?  100 THR K CA  1 
ATOM   21618 C C   . THR L  6 115 L 76.375  59.217  222.611 1.00 188.34 ?  100 THR K C   1 
ATOM   21619 O O   . THR L  6 115 L 77.183  59.526  221.729 1.00 189.71 ?  100 THR K O   1 
ATOM   21620 C CB  . THR L  6 115 L 75.063  61.281  223.030 1.00 185.75 ?  100 THR K CB  1 
ATOM   21621 O OG1 . THR L  6 115 L 75.851  62.128  222.183 1.00 187.10 ?  100 THR K OG1 1 
ATOM   21622 C CG2 . THR L  6 115 L 74.397  62.138  224.085 1.00 184.65 ?  100 THR K CG2 1 
ATOM   21623 N N   . TYR L  6 116 M 75.825  58.007  222.703 1.00 191.41 ?  100 TYR K N   1 
ATOM   21624 C CA  . TYR L  6 116 M 76.094  56.949  221.740 1.00 191.77 ?  100 TYR K CA  1 
ATOM   21625 C C   . TYR L  6 116 M 74.808  56.632  220.985 1.00 189.17 ?  100 TYR K C   1 
ATOM   21626 O O   . TYR L  6 116 M 73.721  56.624  221.572 1.00 187.27 ?  100 TYR K O   1 
ATOM   21627 C CB  . TYR L  6 116 M 76.640  55.691  222.432 1.00 193.10 ?  100 TYR K CB  1 
ATOM   21628 C CG  . TYR L  6 116 M 75.710  55.075  223.460 1.00 191.72 ?  100 TYR K CG  1 
ATOM   21629 C CD1 . TYR L  6 116 M 75.698  55.532  224.772 1.00 192.09 ?  100 TYR K CD1 1 
ATOM   21630 C CD2 . TYR L  6 116 M 74.855  54.035  223.121 1.00 190.17 ?  100 TYR K CD2 1 
ATOM   21631 C CE1 . TYR L  6 116 M 74.856  54.976  225.715 1.00 190.95 ?  100 TYR K CE1 1 
ATOM   21632 C CE2 . TYR L  6 116 M 74.009  53.473  224.058 1.00 189.03 ?  100 TYR K CE2 1 
ATOM   21633 C CZ  . TYR L  6 116 M 74.015  53.948  225.353 1.00 189.43 ?  100 TYR K CZ  1 
ATOM   21634 O OH  . TYR L  6 116 M 73.178  53.393  226.292 1.00 188.41 ?  100 TYR K OH  1 
ATOM   21635 N N   . PHE L  6 117 N 74.933  56.358  219.690 1.00 192.48 ?  100 PHE K N   1 
ATOM   21636 C CA  . PHE L  6 117 N 73.799  56.023  218.841 1.00 190.27 ?  100 PHE K CA  1 
ATOM   21637 C C   . PHE L  6 117 N 73.844  54.573  218.389 1.00 190.45 ?  100 PHE K C   1 
ATOM   21638 O O   . PHE L  6 117 N 74.914  54.004  218.171 1.00 192.43 ?  100 PHE K O   1 
ATOM   21639 C CB  . PHE L  6 117 N 73.722  56.925  217.608 1.00 189.90 ?  100 PHE K CB  1 
ATOM   21640 C CG  . PHE L  6 117 N 73.471  58.359  217.926 1.00 189.35 ?  100 PHE K CG  1 
ATOM   21641 C CD1 . PHE L  6 117 N 72.174  58.803  218.106 1.00 186.92 ?  100 PHE K CD1 1 
ATOM   21642 C CD2 . PHE L  6 117 N 74.511  59.261  218.050 1.00 191.28 ?  100 PHE K CD2 1 
ATOM   21643 C CE1 . PHE L  6 117 N 71.912  60.118  218.395 1.00 186.35 ?  100 PHE K CE1 1 
ATOM   21644 C CE2 . PHE L  6 117 N 74.255  60.584  218.344 1.00 190.77 ?  100 PHE K CE2 1 
ATOM   21645 C CZ  . PHE L  6 117 N 72.952  61.012  218.516 1.00 188.27 ?  100 PHE K CZ  1 
ATOM   21646 N N   . TYR L  6 118 O 72.659  54.007  218.184 1.00 217.68 ?  100 TYR K N   1 
ATOM   21647 C CA  . TYR L  6 118 O 72.531  52.637  217.714 1.00 214.65 ?  100 TYR K CA  1 
ATOM   21648 C C   . TYR L  6 118 O 71.240  52.449  216.937 1.00 209.11 ?  100 TYR K C   1 
ATOM   21649 O O   . TYR L  6 118 O 70.175  52.917  217.353 1.00 204.72 ?  100 TYR K O   1 
ATOM   21650 C CB  . TYR L  6 118 O 72.633  51.661  218.901 1.00 212.64 ?  100 TYR K CB  1 
ATOM   21651 C CG  . TYR L  6 118 O 71.592  51.841  219.995 1.00 207.90 ?  100 TYR K CG  1 
ATOM   21652 C CD1 . TYR L  6 118 O 71.804  52.784  220.994 1.00 209.90 ?  100 TYR K CD1 1 
ATOM   21653 C CD2 . TYR L  6 118 O 70.435  51.070  220.061 1.00 200.61 ?  100 TYR K CD2 1 
ATOM   21654 C CE1 . TYR L  6 118 O 70.896  52.977  222.014 1.00 204.07 ?  100 TYR K CE1 1 
ATOM   21655 C CE2 . TYR L  6 118 O 69.510  51.259  221.088 1.00 194.57 ?  100 TYR K CE2 1 
ATOM   21656 C CZ  . TYR L  6 118 O 69.750  52.214  222.059 1.00 196.01 ?  100 TYR K CZ  1 
ATOM   21657 O OH  . TYR L  6 118 O 68.839  52.404  223.076 1.00 188.96 ?  100 TYR K OH  1 
ATOM   21658 N N   . MET L  6 119 P 71.361  51.773  215.794 1.00 209.12 ?  100 MET K N   1 
ATOM   21659 C CA  . MET L  6 119 P 70.231  51.485  214.927 1.00 204.11 ?  100 MET K CA  1 
ATOM   21660 C C   . MET L  6 119 P 69.637  50.145  215.329 1.00 199.18 ?  100 MET K C   1 
ATOM   21661 O O   . MET L  6 119 P 70.363  49.156  215.467 1.00 200.07 ?  100 MET K O   1 
ATOM   21662 C CB  . MET L  6 119 P 70.650  51.447  213.456 1.00 205.64 ?  100 MET K CB  1 
ATOM   21663 C CG  . MET L  6 119 P 71.057  52.787  212.888 1.00 209.93 ?  100 MET K CG  1 
ATOM   21664 S SD  . MET L  6 119 P 72.508  53.478  213.695 1.00 216.52 ?  100 MET K SD  1 
ATOM   21665 C CE  . MET L  6 119 P 73.753  52.261  213.273 1.00 216.26 ?  100 MET K CE  1 
ATOM   21666 N N   . ASP L  6 120 Q 68.320  50.113  215.494 1.00 220.88 ?  100 ASP K N   1 
ATOM   21667 C CA  . ASP L  6 120 Q 67.611  48.909  215.907 1.00 218.02 ?  100 ASP K CA  1 
ATOM   21668 C C   . ASP L  6 120 Q 66.759  48.344  214.790 1.00 217.21 ?  100 ASP K C   1 
ATOM   21669 O O   . ASP L  6 120 Q 66.693  47.124  214.619 1.00 216.15 ?  100 ASP K O   1 
ATOM   21670 C CB  . ASP L  6 120 Q 66.718  49.184  217.128 1.00 211.67 ?  100 ASP K CB  1 
ATOM   21671 C CG  . ASP L  6 120 Q 65.693  50.280  216.875 1.00 207.53 ?  100 ASP K CG  1 
ATOM   21672 O OD1 . ASP L  6 120 Q 66.028  51.252  216.169 1.00 213.71 ?  100 ASP K OD1 1 
ATOM   21673 O OD2 . ASP L  6 120 Q 64.549  50.166  217.372 1.00 198.41 -1 100 ASP K OD2 1 
ATOM   21674 N N   . VAL L  6 121 R 66.118  49.225  214.029 1.00 228.78 ?  100 VAL K N   1 
ATOM   21675 C CA  . VAL L  6 121 R 65.235  48.872  212.927 1.00 228.35 ?  100 VAL K CA  1 
ATOM   21676 C C   . VAL L  6 121 R 65.881  49.381  211.644 1.00 228.78 ?  100 VAL K C   1 
ATOM   21677 O O   . VAL L  6 121 R 65.917  50.592  211.393 1.00 229.29 ?  100 VAL K O   1 
ATOM   21678 C CB  . VAL L  6 121 R 63.835  49.474  213.120 1.00 225.06 ?  100 VAL K CB  1 
ATOM   21679 C CG1 . VAL L  6 121 R 62.915  49.103  211.967 1.00 224.62 ?  100 VAL K CG1 1 
ATOM   21680 C CG2 . VAL L  6 121 R 63.243  49.044  214.460 1.00 215.11 ?  100 VAL K CG2 1 
ATOM   21681 N N   . TRP L  6 122 ? 66.403  48.456  210.845 1.00 223.69 ?  101 TRP K N   1 
ATOM   21682 C CA  . TRP L  6 122 ? 67.071  48.735  209.583 1.00 227.32 ?  101 TRP K CA  1 
ATOM   21683 C C   . TRP L  6 122 ? 66.103  48.624  208.410 1.00 226.56 ?  101 TRP K C   1 
ATOM   21684 O O   . TRP L  6 122 ? 64.938  48.251  208.564 1.00 224.95 ?  101 TRP K O   1 
ATOM   21685 C CB  . TRP L  6 122 ? 68.250  47.791  209.376 1.00 228.57 ?  101 TRP K CB  1 
ATOM   21686 C CG  . TRP L  6 122 ? 69.366  48.023  210.317 1.00 232.14 ?  101 TRP K CG  1 
ATOM   21687 C CD1 . TRP L  6 122 ? 69.359  47.863  211.674 1.00 232.94 ?  101 TRP K CD1 1 
ATOM   21688 C CD2 . TRP L  6 122 ? 70.673  48.473  209.970 1.00 235.91 ?  101 TRP K CD2 1 
ATOM   21689 N NE1 . TRP L  6 122 ? 70.592  48.184  212.191 1.00 237.48 ?  101 TRP K NE1 1 
ATOM   21690 C CE2 . TRP L  6 122 ? 71.416  48.562  211.163 1.00 239.16 ?  101 TRP K CE2 1 
ATOM   21691 C CE3 . TRP L  6 122 ? 71.289  48.807  208.761 1.00 236.46 ?  101 TRP K CE3 1 
ATOM   21692 C CZ2 . TRP L  6 122 ? 72.744  48.973  211.181 1.00 242.80 ?  101 TRP K CZ2 1 
ATOM   21693 C CZ3 . TRP L  6 122 ? 72.602  49.214  208.780 1.00 239.79 ?  101 TRP K CZ3 1 
ATOM   21694 C CH2 . TRP L  6 122 ? 73.319  49.294  209.981 1.00 242.83 ?  101 TRP K CH2 1 
ATOM   21695 N N   . GLY L  6 123 ? 66.600  48.966  207.220 1.00 239.30 ?  102 GLY K N   1 
ATOM   21696 C CA  . GLY L  6 123 ? 65.834  48.853  206.002 1.00 241.34 ?  102 GLY K CA  1 
ATOM   21697 C C   . GLY L  6 123 ? 66.358  47.752  205.088 1.00 239.53 ?  102 GLY K C   1 
ATOM   21698 O O   . GLY L  6 123 ? 67.359  47.092  205.357 1.00 236.16 ?  102 GLY K O   1 
ATOM   21699 N N   . LYS L  6 124 ? 65.639  47.567  203.977 1.00 234.99 ?  103 LYS K N   1 
ATOM   21700 C CA  . LYS L  6 124 ? 66.010  46.544  202.999 1.00 232.36 ?  103 LYS K CA  1 
ATOM   21701 C C   . LYS L  6 124 ? 67.333  46.837  202.287 1.00 236.19 ?  103 LYS K C   1 
ATOM   21702 O O   . LYS L  6 124 ? 68.106  45.914  202.002 1.00 238.50 ?  103 LYS K O   1 
ATOM   21703 C CB  . LYS L  6 124 ? 64.866  46.382  202.003 1.00 230.12 ?  103 LYS K CB  1 
ATOM   21704 C CG  . LYS L  6 124 ? 64.418  44.944  201.861 1.00 231.16 ?  103 LYS K CG  1 
ATOM   21705 C CD  . LYS L  6 124 ? 63.223  44.815  200.943 1.00 232.06 ?  103 LYS K CD  1 
ATOM   21706 C CE  . LYS L  6 124 ? 62.797  43.364  200.834 1.00 234.80 ?  103 LYS K CE  1 
ATOM   21707 N NZ  . LYS L  6 124 ? 61.847  43.142  199.716 1.00 237.99 1  103 LYS K NZ  1 
ATOM   21708 N N   . GLY L  6 125 ? 67.606  48.092  201.984 1.00 221.41 ?  104 GLY K N   1 
ATOM   21709 C CA  . GLY L  6 125 ? 68.821  48.548  201.335 1.00 223.40 ?  104 GLY K CA  1 
ATOM   21710 C C   . GLY L  6 125 ? 68.645  48.703  199.832 1.00 223.76 ?  104 GLY K C   1 
ATOM   21711 O O   . GLY L  6 125 ? 67.800  48.056  199.204 1.00 222.89 ?  104 GLY K O   1 
ATOM   21712 N N   . THR L  6 126 ? 69.444  49.599  199.247 1.00 237.51 ?  105 THR K N   1 
ATOM   21713 C CA  . THR L  6 126 ? 69.466  49.854  197.813 1.00 238.31 ?  105 THR K CA  1 
ATOM   21714 C C   . THR L  6 126 ? 70.867  49.635  197.264 1.00 241.47 ?  105 THR K C   1 
ATOM   21715 O O   . THR L  6 126 ? 71.860  49.817  197.976 1.00 240.09 ?  105 THR K O   1 
ATOM   21716 C CB  . THR L  6 126 ? 69.035  51.287  197.462 1.00 230.82 ?  105 THR K CB  1 
ATOM   21717 O OG1 . THR L  6 126 ? 69.621  52.214  198.385 1.00 231.35 ?  105 THR K OG1 1 
ATOM   21718 C CG2 . THR L  6 126 ? 67.540  51.415  197.493 1.00 226.11 ?  105 THR K CG2 1 
ATOM   21719 N N   . SER L  6 127 ? 70.950  49.247  195.996 1.00 236.31 ?  106 SER K N   1 
ATOM   21720 C CA  . SER L  6 127 ? 72.236  49.016  195.358 1.00 233.56 ?  106 SER K CA  1 
ATOM   21721 C C   . SER L  6 127 ? 72.537  50.235  194.496 1.00 240.54 ?  106 SER K C   1 
ATOM   21722 O O   . SER L  6 127 ? 71.712  50.623  193.663 1.00 243.44 ?  106 SER K O   1 
ATOM   21723 C CB  . SER L  6 127 ? 72.214  47.745  194.508 1.00 235.12 ?  106 SER K CB  1 
ATOM   21724 O OG  . SER L  6 127 ? 71.841  46.615  195.279 1.00 239.15 ?  106 SER K OG  1 
ATOM   21725 N N   . VAL L  6 128 ? 73.704  50.841  194.700 1.00 222.39 ?  107 VAL K N   1 
ATOM   21726 C CA  . VAL L  6 128 ? 74.131  52.008  193.934 1.00 227.58 ?  107 VAL K CA  1 
ATOM   21727 C C   . VAL L  6 128 ? 75.499  51.701  193.340 1.00 234.43 ?  107 VAL K C   1 
ATOM   21728 O O   . VAL L  6 128 ? 76.465  51.491  194.085 1.00 236.07 ?  107 VAL K O   1 
ATOM   21729 C CB  . VAL L  6 128 ? 74.170  53.281  194.795 1.00 227.28 ?  107 VAL K CB  1 
ATOM   21730 C CG1 . VAL L  6 128 ? 74.750  54.430  194.002 1.00 233.50 ?  107 VAL K CG1 1 
ATOM   21731 C CG2 . VAL L  6 128 ? 72.769  53.624  195.296 1.00 223.99 ?  107 VAL K CG2 1 
ATOM   21732 N N   . THR L  6 129 ? 75.587  51.680  192.012 1.00 232.34 ?  108 THR K N   1 
ATOM   21733 C CA  . THR L  6 129 ? 76.829  51.391  191.305 1.00 239.41 ?  108 THR K CA  1 
ATOM   21734 C C   . THR L  6 129 ? 77.280  52.596  190.489 1.00 246.23 ?  108 THR K C   1 
ATOM   21735 O O   . THR L  6 129 ? 76.491  53.155  189.721 1.00 246.23 ?  108 THR K O   1 
ATOM   21736 C CB  . THR L  6 129 ? 76.647  50.180  190.388 1.00 239.40 ?  108 THR K CB  1 
ATOM   21737 O OG1 . THR L  6 129 ? 76.157  49.073  191.155 1.00 233.35 ?  108 THR K OG1 1 
ATOM   21738 C CG2 . THR L  6 129 ? 77.965  49.795  189.742 1.00 246.70 ?  108 THR K CG2 1 
ATOM   21739 N N   . VAL L  6 130 ? 78.535  53.003  190.662 1.00 231.80 ?  109 VAL K N   1 
ATOM   21740 C CA  . VAL L  6 130 ? 79.096  54.136  189.934 1.00 233.63 ?  109 VAL K CA  1 
ATOM   21741 C C   . VAL L  6 130 ? 79.940  53.607  188.778 1.00 235.96 ?  109 VAL K C   1 
ATOM   21742 O O   . VAL L  6 130 ? 80.994  52.999  188.994 1.00 237.52 ?  109 VAL K O   1 
ATOM   21743 C CB  . VAL L  6 130 ? 79.927  55.043  190.848 1.00 234.66 ?  109 VAL K CB  1 
ATOM   21744 C CG1 . VAL L  6 130 ? 80.552  56.165  190.036 1.00 236.78 ?  109 VAL K CG1 1 
ATOM   21745 C CG2 . VAL L  6 130 ? 79.062  55.607  191.957 1.00 232.38 ?  109 VAL K CG2 1 
ATOM   21746 N N   . SER L  6 131 ? 79.481  53.839  187.551 1.00 234.09 ?  110 SER K N   1 
ATOM   21747 C CA  . SER L  6 131 ? 80.192  53.414  186.352 1.00 236.32 ?  110 SER K CA  1 
ATOM   21748 C C   . SER L  6 131 ? 79.774  54.320  185.204 1.00 236.92 ?  110 SER K C   1 
ATOM   21749 O O   . SER L  6 131 ? 78.632  54.786  185.155 1.00 235.07 ?  110 SER K O   1 
ATOM   21750 C CB  . SER L  6 131 ? 79.923  51.946  186.003 1.00 235.74 ?  110 SER K CB  1 
ATOM   21751 O OG  . SER L  6 131 ? 80.649  51.563  184.846 1.00 237.98 ?  110 SER K OG  1 
ATOM   21752 N N   . SER L  6 132 ? 80.707  54.582  184.291 1.00 250.34 ?  111 SER K N   1 
ATOM   21753 C CA  . SER L  6 132 ? 80.408  55.455  183.161 1.00 254.09 ?  111 SER K CA  1 
ATOM   21754 C C   . SER L  6 132 ? 79.749  54.713  181.997 1.00 256.74 ?  111 SER K C   1 
ATOM   21755 O O   . SER L  6 132 ? 79.552  55.318  180.937 1.00 260.18 ?  111 SER K O   1 
ATOM   21756 C CB  . SER L  6 132 ? 81.681  56.159  182.679 1.00 255.22 ?  111 SER K CB  1 
ATOM   21757 O OG  . SER L  6 132 ? 82.694  55.230  182.338 1.00 253.69 ?  111 SER K OG  1 
ATOM   21758 N N   . ALA L  6 133 ? 79.412  53.433  182.170 1.00 263.44 ?  112 ALA K N   1 
ATOM   21759 C CA  . ALA L  6 133 ? 78.770  52.622  181.141 1.00 262.92 ?  112 ALA K CA  1 
ATOM   21760 C C   . ALA L  6 133 ? 77.252  52.779  181.182 1.00 259.68 ?  112 ALA K C   1 
ATOM   21761 O O   . ALA L  6 133 ? 76.669  53.091  182.223 1.00 257.26 ?  112 ALA K O   1 
ATOM   21762 C CB  . ALA L  6 133 ? 79.137  51.147  181.309 1.00 262.88 ?  112 ALA K CB  1 
ATOM   21763 N N   . SER L  6 134 ? 76.616  52.553  180.031 1.00 279.13 ?  113 SER K N   1 
ATOM   21764 C CA  . SER L  6 134 ? 75.170  52.684  179.919 1.00 272.97 ?  113 SER K CA  1 
ATOM   21765 C C   . SER L  6 134 ? 74.438  51.468  180.494 1.00 268.12 ?  113 SER K C   1 
ATOM   21766 O O   . SER L  6 134 ? 75.023  50.421  180.787 1.00 264.79 ?  113 SER K O   1 
ATOM   21767 C CB  . SER L  6 134 ? 74.769  52.893  178.457 1.00 274.56 ?  113 SER K CB  1 
ATOM   21768 O OG  . SER L  6 134 ? 73.469  53.451  178.347 1.00 264.53 ?  113 SER K OG  1 
ATOM   21769 N N   . THR L  6 135 ? 73.126  51.643  180.655 1.00 290.42 ?  114 THR K N   1 
ATOM   21770 C CA  . THR L  6 135 ? 72.213  50.622  181.155 1.00 279.44 ?  114 THR K CA  1 
ATOM   21771 C C   . THR L  6 135 ? 71.652  49.801  179.992 1.00 282.85 ?  114 THR K C   1 
ATOM   21772 O O   . THR L  6 135 ? 71.228  50.368  178.979 1.00 286.87 ?  114 THR K O   1 
ATOM   21773 C CB  . THR L  6 135 ? 71.093  51.294  181.948 1.00 265.31 ?  114 THR K CB  1 
ATOM   21774 O OG1 . THR L  6 135 ? 71.675  52.137  182.946 1.00 258.10 ?  114 THR K OG1 1 
ATOM   21775 C CG2 . THR L  6 135 ? 70.284  50.270  182.669 1.00 252.02 ?  114 THR K CG2 1 
ATOM   21776 N N   . LYS L  6 136 ? 71.645  48.473  180.135 1.00 284.32 ?  115 LYS K N   1 
ATOM   21777 C CA  . LYS L  6 136 ? 71.129  47.567  179.110 1.00 280.87 ?  115 LYS K CA  1 
ATOM   21778 C C   . LYS L  6 136 ? 69.957  46.744  179.626 1.00 272.36 ?  115 LYS K C   1 
ATOM   21779 O O   . LYS L  6 136 ? 70.023  46.186  180.726 1.00 263.13 ?  115 LYS K O   1 
ATOM   21780 C CB  . LYS L  6 136 ? 72.208  46.607  178.604 1.00 281.95 ?  115 LYS K CB  1 
ATOM   21781 C CG  . LYS L  6 136 ? 71.780  45.809  177.375 1.00 274.72 ?  115 LYS K CG  1 
ATOM   21782 C CD  . LYS L  6 136 ? 72.884  44.881  176.893 1.00 275.93 ?  115 LYS K CD  1 
ATOM   21783 C CE  . LYS L  6 136 ? 72.519  44.213  175.573 1.00 284.54 ?  115 LYS K CE  1 
ATOM   21784 N NZ  . LYS L  6 136 ? 71.226  43.481  175.641 1.00 281.11 1  115 LYS K NZ  1 
ATOM   21785 N N   . GLY L  6 137 ? 68.886  46.672  178.835 1.00 285.68 ?  116 GLY K N   1 
ATOM   21786 C CA  . GLY L  6 137 ? 67.737  45.884  179.210 1.00 277.48 ?  116 GLY K CA  1 
ATOM   21787 C C   . GLY L  6 137 ? 68.052  44.410  179.035 1.00 278.07 ?  116 GLY K C   1 
ATOM   21788 O O   . GLY L  6 137 ? 68.634  43.983  178.033 1.00 282.21 ?  116 GLY K O   1 
ATOM   21789 N N   . PRO L  6 138 ? 67.653  43.604  180.013 1.00 276.75 ?  117 PRO K N   1 
ATOM   21790 C CA  . PRO L  6 138 ? 67.921  42.162  179.956 1.00 272.91 ?  117 PRO K CA  1 
ATOM   21791 C C   . PRO L  6 138 ? 67.088  41.428  178.917 1.00 278.81 ?  117 PRO K C   1 
ATOM   21792 O O   . PRO L  6 138 ? 66.036  41.890  178.470 1.00 280.47 ?  117 PRO K O   1 
ATOM   21793 C CB  . PRO L  6 138 ? 67.569  41.688  181.368 1.00 266.03 ?  117 PRO K CB  1 
ATOM   21794 C CG  . PRO L  6 138 ? 66.559  42.671  181.841 1.00 261.88 ?  117 PRO K CG  1 
ATOM   21795 C CD  . PRO L  6 138 ? 66.968  43.992  181.256 1.00 266.76 ?  117 PRO K CD  1 
ATOM   21796 N N   . SER L  6 139 ? 67.593  40.258  178.525 1.00 268.22 ?  118 SER K N   1 
ATOM   21797 C CA  . SER L  6 139 ? 66.901  39.376  177.590 1.00 270.10 ?  118 SER K CA  1 
ATOM   21798 C C   . SER L  6 139 ? 66.634  38.060  178.316 1.00 264.90 ?  118 SER K C   1 
ATOM   21799 O O   . SER L  6 139 ? 67.561  37.282  178.568 1.00 264.36 ?  118 SER K O   1 
ATOM   21800 C CB  . SER L  6 139 ? 67.727  39.156  176.323 1.00 275.04 ?  118 SER K CB  1 
ATOM   21801 O OG  . SER L  6 139 ? 67.968  40.381  175.652 1.00 275.63 ?  118 SER K OG  1 
ATOM   21802 N N   . VAL L  6 140 ? 65.366  37.826  178.646 1.00 270.21 ?  119 VAL K N   1 
ATOM   21803 C CA  . VAL L  6 140 ? 64.910  36.667  179.413 1.00 266.37 ?  119 VAL K CA  1 
ATOM   21804 C C   . VAL L  6 140 ? 64.630  35.491  178.480 1.00 272.16 ?  119 VAL K C   1 
ATOM   21805 O O   . VAL L  6 140 ? 63.928  35.648  177.474 1.00 268.36 ?  119 VAL K O   1 
ATOM   21806 C CB  . VAL L  6 140 ? 63.673  37.024  180.251 1.00 258.34 ?  119 VAL K CB  1 
ATOM   21807 C CG1 . VAL L  6 140 ? 63.276  35.856  181.135 1.00 254.28 ?  119 VAL K CG1 1 
ATOM   21808 C CG2 . VAL L  6 140 ? 63.962  38.254  181.091 1.00 250.99 ?  119 VAL K CG2 1 
ATOM   21809 N N   . PHE L  6 141 ? 65.190  34.314  178.795 1.00 261.84 ?  120 PHE K N   1 
ATOM   21810 C CA  . PHE L  6 141 ? 64.942  33.102  178.004 1.00 263.74 ?  120 PHE K CA  1 
ATOM   21811 C C   . PHE L  6 141 ? 64.449  31.924  178.844 1.00 261.69 ?  120 PHE K C   1 
ATOM   21812 O O   . PHE L  6 141 ? 65.009  31.639  179.918 1.00 257.09 ?  120 PHE K O   1 
ATOM   21813 C CB  . PHE L  6 141 ? 66.207  32.722  177.226 1.00 267.61 ?  120 PHE K CB  1 
ATOM   21814 C CG  . PHE L  6 141 ? 66.665  33.793  176.270 1.00 273.42 ?  120 PHE K CG  1 
ATOM   21815 C CD1 . PHE L  6 141 ? 66.040  33.957  175.042 1.00 276.58 ?  120 PHE K CD1 1 
ATOM   21816 C CD2 . PHE L  6 141 ? 67.707  34.643  176.602 1.00 275.43 ?  120 PHE K CD2 1 
ATOM   21817 C CE1 . PHE L  6 141 ? 66.452  34.946  174.162 1.00 283.69 ?  120 PHE K CE1 1 
ATOM   21818 C CE2 . PHE L  6 141 ? 68.125  35.632  175.725 1.00 281.21 ?  120 PHE K CE2 1 
ATOM   21819 C CZ  . PHE L  6 141 ? 67.496  35.782  174.503 1.00 287.16 ?  120 PHE K CZ  1 
ATOM   21820 N N   . PRO L  6 142 ? 63.404  31.225  178.388 1.00 264.47 ?  121 PRO K N   1 
ATOM   21821 C CA  . PRO L  6 142 ? 62.806  30.118  179.156 1.00 261.10 ?  121 PRO K CA  1 
ATOM   21822 C C   . PRO L  6 142 ? 63.616  28.824  179.138 1.00 262.33 ?  121 PRO K C   1 
ATOM   21823 O O   . PRO L  6 142 ? 64.166  28.425  178.108 1.00 267.79 ?  121 PRO K O   1 
ATOM   21824 C CB  . PRO L  6 142 ? 61.456  29.909  178.459 1.00 261.61 ?  121 PRO K CB  1 
ATOM   21825 C CG  . PRO L  6 142 ? 61.721  30.323  177.054 1.00 266.69 ?  121 PRO K CG  1 
ATOM   21826 C CD  . PRO L  6 142 ? 62.693  31.461  177.121 1.00 264.27 ?  121 PRO K CD  1 
ATOM   21827 N N   . LEU L  6 143 ? 63.691  28.170  180.303 1.00 265.94 ?  122 LEU K N   1 
ATOM   21828 C CA  . LEU L  6 143 ? 64.366  26.879  180.457 1.00 267.78 ?  122 LEU K CA  1 
ATOM   21829 C C   . LEU L  6 143 ? 63.328  25.749  180.476 1.00 265.67 ?  122 LEU K C   1 
ATOM   21830 O O   . LEU L  6 143 ? 62.589  25.597  181.454 1.00 261.24 ?  122 LEU K O   1 
ATOM   21831 C CB  . LEU L  6 143 ? 65.210  26.885  181.728 1.00 263.87 ?  122 LEU K CB  1 
ATOM   21832 C CG  . LEU L  6 143 ? 66.330  27.925  181.655 1.00 264.39 ?  122 LEU K CG  1 
ATOM   21833 C CD1 . LEU L  6 143 ? 67.174  27.922  182.917 1.00 262.39 ?  122 LEU K CD1 1 
ATOM   21834 C CD2 . LEU L  6 143 ? 67.186  27.730  180.413 1.00 264.77 ?  122 LEU K CD2 1 
ATOM   21835 N N   . ALA L  6 144 ? 63.284  24.960  179.397 1.00 272.83 ?  123 ALA K N   1 
ATOM   21836 C CA  . ALA L  6 144 ? 62.296  23.888  179.253 1.00 272.15 ?  123 ALA K CA  1 
ATOM   21837 C C   . ALA L  6 144 ? 62.444  22.792  180.312 1.00 274.45 ?  123 ALA K C   1 
ATOM   21838 O O   . ALA L  6 144 ? 63.563  22.392  180.649 1.00 277.81 ?  123 ALA K O   1 
ATOM   21839 C CB  . ALA L  6 144 ? 62.400  23.262  177.861 1.00 271.42 ?  123 ALA K CB  1 
ATOM   21840 N N   . PRO L  6 145 ? 61.328  22.283  180.844 1.00 279.12 ?  124 PRO K N   1 
ATOM   21841 C CA  . PRO L  6 145 ? 61.374  21.195  181.837 1.00 279.59 ?  124 PRO K CA  1 
ATOM   21842 C C   . PRO L  6 145 ? 61.921  19.878  181.294 1.00 290.94 ?  124 PRO K C   1 
ATOM   21843 O O   . PRO L  6 145 ? 61.616  19.476  180.168 1.00 293.66 ?  124 PRO K O   1 
ATOM   21844 C CB  . PRO L  6 145 ? 59.906  21.040  182.255 1.00 272.66 ?  124 PRO K CB  1 
ATOM   21845 C CG  . PRO L  6 145 ? 59.254  22.330  181.882 1.00 269.12 ?  124 PRO K CG  1 
ATOM   21846 C CD  . PRO L  6 145 ? 59.960  22.787  180.644 1.00 274.99 ?  124 PRO K CD  1 
ATOM   21847 N N   . SER L  6 146 ? 62.732  19.196  182.110 1.00 295.75 ?  125 SER K N   1 
ATOM   21848 C CA  . SER L  6 146 ? 63.292  17.901  181.706 1.00 301.66 ?  125 SER K CA  1 
ATOM   21849 C C   . SER L  6 146 ? 63.626  17.110  182.973 1.00 302.51 ?  125 SER K C   1 
ATOM   21850 O O   . SER L  6 146 ? 64.631  17.393  183.631 1.00 304.48 ?  125 SER K O   1 
ATOM   21851 C CB  . SER L  6 146 ? 64.509  18.069  180.810 1.00 302.94 ?  125 SER K CB  1 
ATOM   21852 O OG  . SER L  6 146 ? 64.161  18.699  179.589 1.00 302.94 ?  125 SER K OG  1 
ATOM   21853 N N   . SER L  6 147 ? 62.785  16.125  183.291 1.00 287.72 ?  126 SER K N   1 
ATOM   21854 C CA  . SER L  6 147 ? 62.968  15.261  184.462 1.00 284.56 ?  126 SER K CA  1 
ATOM   21855 C C   . SER L  6 147 ? 63.131  16.053  185.758 1.00 278.41 ?  126 SER K C   1 
ATOM   21856 O O   . SER L  6 147 ? 63.996  15.745  186.581 1.00 279.65 ?  126 SER K O   1 
ATOM   21857 C CB  . SER L  6 147 ? 64.169  14.330  184.268 1.00 293.56 ?  126 SER K CB  1 
ATOM   21858 O OG  . SER L  6 147 ? 63.971  13.456  183.170 1.00 299.62 ?  126 SER K OG  1 
ATOM   21859 N N   . GLY L  6 152 ? 61.367  9.632   188.594 1.00 275.81 ?  131 GLY K N   1 
ATOM   21860 C CA  . GLY L  6 152 ? 61.568  10.040  189.972 1.00 273.30 ?  131 GLY K CA  1 
ATOM   21861 C C   . GLY L  6 152 ? 60.350  10.704  190.580 1.00 269.86 ?  131 GLY K C   1 
ATOM   21862 O O   . GLY L  6 152 ? 60.259  10.869  191.797 1.00 268.36 ?  131 GLY K O   1 
ATOM   21863 N N   . GLY L  6 153 ? 59.408  11.097  189.726 1.00 280.50 ?  132 GLY K N   1 
ATOM   21864 C CA  . GLY L  6 153 ? 58.199  11.746  190.182 1.00 277.38 ?  132 GLY K CA  1 
ATOM   21865 C C   . GLY L  6 153 ? 58.334  13.235  190.393 1.00 271.38 ?  132 GLY K C   1 
ATOM   21866 O O   . GLY L  6 153 ? 57.343  13.888  190.748 1.00 268.20 ?  132 GLY K O   1 
ATOM   21867 N N   . THR L  6 154 ? 59.526  13.785  190.187 1.00 274.29 ?  133 THR K N   1 
ATOM   21868 C CA  . THR L  6 154 ? 59.839  15.195  190.342 1.00 268.84 ?  133 THR K CA  1 
ATOM   21869 C C   . THR L  6 154 ? 60.345  15.751  189.016 1.00 268.01 ?  133 THR K C   1 
ATOM   21870 O O   . THR L  6 154 ? 60.679  15.006  188.091 1.00 271.75 ?  133 THR K O   1 
ATOM   21871 C CB  . THR L  6 154 ? 60.896  15.395  191.435 1.00 267.55 ?  133 THR K CB  1 
ATOM   21872 O OG1 . THR L  6 154 ? 62.061  14.622  191.113 1.00 271.28 ?  133 THR K OG1 1 
ATOM   21873 C CG2 . THR L  6 154 ? 60.357  14.934  192.774 1.00 268.10 ?  133 THR K CG2 1 
ATOM   21874 N N   . ALA L  6 155 ? 60.394  17.079  188.925 1.00 263.03 ?  134 ALA K N   1 
ATOM   21875 C CA  . ALA L  6 155 ? 60.858  17.734  187.712 1.00 262.23 ?  134 ALA K CA  1 
ATOM   21876 C C   . ALA L  6 155 ? 61.438  19.097  188.061 1.00 257.23 ?  134 ALA K C   1 
ATOM   21877 O O   . ALA L  6 155 ? 61.078  19.699  189.077 1.00 253.44 ?  134 ALA K O   1 
ATOM   21878 C CB  . ALA L  6 155 ? 59.725  17.885  186.688 1.00 262.32 ?  134 ALA K CB  1 
ATOM   21879 N N   . ALA L  6 156 ? 62.339  19.575  187.202 1.00 254.83 ?  135 ALA K N   1 
ATOM   21880 C CA  . ALA L  6 156 ? 62.993  20.866  187.357 1.00 250.45 ?  135 ALA K CA  1 
ATOM   21881 C C   . ALA L  6 156 ? 62.423  21.850  186.343 1.00 248.23 ?  135 ALA K C   1 
ATOM   21882 O O   . ALA L  6 156 ? 62.035  21.468  185.236 1.00 251.16 ?  135 ALA K O   1 
ATOM   21883 C CB  . ALA L  6 156 ? 64.510  20.743  187.177 1.00 252.26 ?  135 ALA K CB  1 
ATOM   21884 N N   . LEU L  6 157 ? 62.390  23.126  186.723 1.00 265.50 ?  136 LEU K N   1 
ATOM   21885 C CA  . LEU L  6 157 ? 61.853  24.170  185.860 1.00 262.91 ?  136 LEU K CA  1 
ATOM   21886 C C   . LEU L  6 157 ? 62.429  25.517  186.286 1.00 257.50 ?  136 LEU K C   1 
ATOM   21887 O O   . LEU L  6 157 ? 62.554  25.777  187.484 1.00 254.27 ?  136 LEU K O   1 
ATOM   21888 C CB  . LEU L  6 157 ? 60.320  24.165  185.916 1.00 261.64 ?  136 LEU K CB  1 
ATOM   21889 C CG  . LEU L  6 157 ? 59.523  24.949  184.877 1.00 261.72 ?  136 LEU K CG  1 
ATOM   21890 C CD1 . LEU L  6 157 ? 58.146  24.337  184.722 1.00 268.66 ?  136 LEU K CD1 1 
ATOM   21891 C CD2 . LEU L  6 157 ? 59.390  26.403  185.281 1.00 253.11 ?  136 LEU K CD2 1 
ATOM   21892 N N   . GLY L  6 158 ? 62.762  26.372  185.320 1.00 262.62 ?  137 GLY K N   1 
ATOM   21893 C CA  . GLY L  6 158 ? 63.323  27.663  185.663 1.00 257.27 ?  137 GLY K CA  1 
ATOM   21894 C C   . GLY L  6 158 ? 63.297  28.652  184.513 1.00 254.93 ?  137 GLY K C   1 
ATOM   21895 O O   . GLY L  6 158 ? 62.766  28.365  183.438 1.00 257.26 ?  137 GLY K O   1 
ATOM   21896 N N   . CYS L  6 159 ? 63.920  29.820  184.747 1.00 260.19 ?  138 CYS K N   1 
ATOM   21897 C CA  . CYS L  6 159 ? 64.040  30.897  183.758 1.00 257.83 ?  138 CYS K CA  1 
ATOM   21898 C C   . CYS L  6 159 ? 65.513  31.287  183.623 1.00 259.77 ?  138 CYS K C   1 
ATOM   21899 O O   . CYS L  6 159 ? 66.374  30.758  184.335 1.00 260.73 ?  138 CYS K O   1 
ATOM   21900 C CB  . CYS L  6 159 ? 63.201  32.129  184.178 1.00 257.51 ?  138 CYS K CB  1 
ATOM   21901 S SG  . CYS L  6 159 ? 61.395  31.824  184.238 1.00 305.33 ?  138 CYS K SG  1 
ATOM   21902 N N   . LEU L  6 160 ? 65.811  32.221  182.711 1.00 258.81 ?  139 LEU K N   1 
ATOM   21903 C CA  . LEU L  6 160 ? 67.184  32.686  182.479 1.00 254.91 ?  139 LEU K CA  1 
ATOM   21904 C C   . LEU L  6 160 ? 67.213  34.153  182.090 1.00 256.48 ?  139 LEU K C   1 
ATOM   21905 O O   . LEU L  6 160 ? 66.533  34.537  181.141 1.00 257.13 ?  139 LEU K O   1 
ATOM   21906 C CB  . LEU L  6 160 ? 67.902  31.843  181.412 1.00 257.32 ?  139 LEU K CB  1 
ATOM   21907 C CG  . LEU L  6 160 ? 69.251  32.443  180.969 1.00 259.56 ?  139 LEU K CG  1 
ATOM   21908 C CD1 . LEU L  6 160 ? 70.236  31.376  180.757 1.00 253.58 ?  139 LEU K CD1 1 
ATOM   21909 C CD2 . LEU L  6 160 ? 69.208  33.209  179.655 1.00 268.02 ?  139 LEU K CD2 1 
ATOM   21910 N N   . VAL L  6 161 ? 67.965  34.966  182.828 1.00 264.40 ?  140 VAL K N   1 
ATOM   21911 C CA  . VAL L  6 161 ? 68.167  36.391  182.541 1.00 265.90 ?  140 VAL K CA  1 
ATOM   21912 C C   . VAL L  6 161 ? 69.587  36.595  181.998 1.00 272.52 ?  140 VAL K C   1 
ATOM   21913 O O   . VAL L  6 161 ? 70.557  36.498  182.760 1.00 273.12 ?  140 VAL K O   1 
ATOM   21914 C CB  . VAL L  6 161 ? 67.922  37.264  183.777 1.00 259.01 ?  140 VAL K CB  1 
ATOM   21915 C CG1 . VAL L  6 161 ? 68.117  38.720  183.423 1.00 259.41 ?  140 VAL K CG1 1 
ATOM   21916 C CG2 . VAL L  6 161 ? 66.525  37.026  184.328 1.00 255.65 ?  140 VAL K CG2 1 
ATOM   21917 N N   . LYS L  6 162 ? 69.738  36.875  180.699 1.00 259.52 ?  141 LYS K N   1 
ATOM   21918 C CA  . LYS L  6 162 ? 71.058  36.960  180.069 1.00 266.28 ?  141 LYS K CA  1 
ATOM   21919 C C   . LYS L  6 162 ? 71.425  38.404  179.723 1.00 271.75 ?  141 LYS K C   1 
ATOM   21920 O O   . LYS L  6 162 ? 70.613  39.133  179.144 1.00 269.29 ?  141 LYS K O   1 
ATOM   21921 C CB  . LYS L  6 162 ? 71.059  36.113  178.791 1.00 271.08 ?  141 LYS K CB  1 
ATOM   21922 C CG  . LYS L  6 162 ? 72.346  36.064  177.990 1.00 277.30 ?  141 LYS K CG  1 
ATOM   21923 C CD  . LYS L  6 162 ? 72.098  35.276  176.708 1.00 285.76 ?  141 LYS K CD  1 
ATOM   21924 C CE  . LYS L  6 162 ? 73.320  35.241  175.812 1.00 290.61 ?  141 LYS K CE  1 
ATOM   21925 N NZ  . LYS L  6 162 ? 74.459  34.507  176.428 1.00 286.05 1  141 LYS K NZ  1 
ATOM   21926 N N   . ASP L  6 163 ? 72.656  38.804  180.055 1.00 271.19 ?  142 ASP K N   1 
ATOM   21927 C CA  . ASP L  6 163 ? 73.186  40.119  179.688 1.00 277.45 ?  142 ASP K CA  1 
ATOM   21928 C C   . ASP L  6 163 ? 72.351  41.334  180.112 1.00 275.36 ?  142 ASP K C   1 
ATOM   21929 O O   . ASP L  6 163 ? 71.501  41.839  179.368 1.00 274.01 ?  142 ASP K O   1 
ATOM   21930 C CB  . ASP L  6 163 ? 73.580  40.154  178.206 1.00 285.67 ?  142 ASP K CB  1 
ATOM   21931 C CG  . ASP L  6 163 ? 74.887  39.389  177.958 1.00 293.59 ?  142 ASP K CG  1 
ATOM   21932 O OD1 . ASP L  6 163 ? 75.190  38.440  178.713 1.00 289.39 ?  142 ASP K OD1 1 
ATOM   21933 O OD2 . ASP L  6 163 ? 75.700  39.851  177.133 1.00 304.18 -1 142 ASP K OD2 1 
ATOM   21934 N N   . TYR L  6 164 ? 72.637  41.843  181.307 1.00 290.52 ?  143 TYR K N   1 
ATOM   21935 C CA  . TYR L  6 164 ? 71.993  43.050  181.799 1.00 289.65 ?  143 TYR K CA  1 
ATOM   21936 C C   . TYR L  6 164 ? 72.998  43.828  182.638 1.00 291.55 ?  143 TYR K C   1 
ATOM   21937 O O   . TYR L  6 164 ? 74.029  43.300  183.068 1.00 290.32 ?  143 TYR K O   1 
ATOM   21938 C CB  . TYR L  6 164 ? 70.718  42.717  182.593 1.00 282.99 ?  143 TYR K CB  1 
ATOM   21939 C CG  . TYR L  6 164 ? 70.987  42.040  183.913 1.00 276.64 ?  143 TYR K CG  1 
ATOM   21940 C CD1 . TYR L  6 164 ? 71.096  40.659  183.991 1.00 268.28 ?  143 TYR K CD1 1 
ATOM   21941 C CD2 . TYR L  6 164 ? 71.105  42.774  185.087 1.00 275.26 ?  143 TYR K CD2 1 
ATOM   21942 C CE1 . TYR L  6 164 ? 71.350  40.025  185.197 1.00 260.25 ?  143 TYR K CE1 1 
ATOM   21943 C CE2 . TYR L  6 164 ? 71.356  42.149  186.302 1.00 266.67 ?  143 TYR K CE2 1 
ATOM   21944 C CZ  . TYR L  6 164 ? 71.476  40.775  186.352 1.00 260.68 ?  143 TYR K CZ  1 
ATOM   21945 O OH  . TYR L  6 164 ? 71.726  40.153  187.558 1.00 257.88 ?  143 TYR K OH  1 
ATOM   21946 N N   . PHE L  6 165 ? 72.677  45.093  182.874 1.00 279.34 ?  144 PHE K N   1 
ATOM   21947 C CA  . PHE L  6 165 ? 73.547  45.972  183.642 1.00 285.85 ?  144 PHE K CA  1 
ATOM   21948 C C   . PHE L  6 165 ? 72.795  47.225  184.068 1.00 287.19 ?  144 PHE K C   1 
ATOM   21949 O O   . PHE L  6 165 ? 72.102  47.831  183.251 1.00 285.23 ?  144 PHE K O   1 
ATOM   21950 C CB  . PHE L  6 165 ? 74.765  46.347  182.782 1.00 293.38 ?  144 PHE K CB  1 
ATOM   21951 C CG  . PHE L  6 165 ? 75.801  47.178  183.492 1.00 299.29 ?  144 PHE K CG  1 
ATOM   21952 C CD1 . PHE L  6 165 ? 76.777  46.581  184.274 1.00 294.23 ?  144 PHE K CD1 1 
ATOM   21953 C CD2 . PHE L  6 165 ? 75.812  48.558  183.354 1.00 304.83 ?  144 PHE K CD2 1 
ATOM   21954 C CE1 . PHE L  6 165 ? 77.738  47.348  184.917 1.00 296.07 ?  144 PHE K CE1 1 
ATOM   21955 C CE2 . PHE L  6 165 ? 76.768  49.330  183.995 1.00 306.25 ?  144 PHE K CE2 1 
ATOM   21956 C CZ  . PHE L  6 165 ? 77.732  48.724  184.777 1.00 302.00 ?  144 PHE K CZ  1 
ATOM   21957 N N   . PRO L  6 166 ? 72.930  47.618  185.349 1.00 303.73 ?  145 PRO K N   1 
ATOM   21958 C CA  . PRO L  6 166 ? 73.698  46.898  186.369 1.00 298.45 ?  145 PRO K CA  1 
ATOM   21959 C C   . PRO L  6 166 ? 72.806  46.087  187.310 1.00 290.78 ?  145 PRO K C   1 
ATOM   21960 O O   . PRO L  6 166 ? 71.625  45.896  187.027 1.00 285.94 ?  145 PRO K O   1 
ATOM   21961 C CB  . PRO L  6 166 ? 74.386  48.027  187.130 1.00 296.35 ?  145 PRO K CB  1 
ATOM   21962 C CG  . PRO L  6 166 ? 73.364  49.122  187.113 1.00 297.05 ?  145 PRO K CG  1 
ATOM   21963 C CD  . PRO L  6 166 ? 72.571  48.971  185.815 1.00 302.42 ?  145 PRO K CD  1 
ATOM   21964 N N   . GLU L  6 167 ? 73.375  45.619  188.415 1.00 278.45 ?  146 GLU K N   1 
ATOM   21965 C CA  . GLU L  6 167 ? 72.632  44.879  189.430 1.00 268.02 ?  146 GLU K CA  1 
ATOM   21966 C C   . GLU L  6 167 ? 71.661  45.802  190.176 1.00 268.67 ?  146 GLU K C   1 
ATOM   21967 O O   . GLU L  6 167 ? 71.883  47.012  190.237 1.00 271.02 ?  146 GLU K O   1 
ATOM   21968 C CB  . GLU L  6 167 ? 73.615  44.231  190.417 1.00 265.01 ?  146 GLU K CB  1 
ATOM   21969 C CG  . GLU L  6 167 ? 74.441  43.075  189.849 1.00 263.10 ?  146 GLU K CG  1 
ATOM   21970 C CD  . GLU L  6 167 ? 73.729  41.736  189.918 1.00 260.48 ?  146 GLU K CD  1 
ATOM   21971 O OE1 . GLU L  6 167 ? 72.535  41.668  189.565 1.00 260.86 ?  146 GLU K OE1 1 
ATOM   21972 O OE2 . GLU L  6 167 ? 74.372  40.746  190.329 1.00 258.04 -1 146 GLU K OE2 1 
ATOM   21973 N N   . PRO L  6 168 ? 70.579  45.240  190.750 1.00 285.14 ?  147 PRO K N   1 
ATOM   21974 C CA  . PRO L  6 168 ? 70.148  43.839  190.705 1.00 279.76 ?  147 PRO K CA  1 
ATOM   21975 C C   . PRO L  6 168 ? 68.894  43.586  189.858 1.00 277.17 ?  147 PRO K C   1 
ATOM   21976 O O   . PRO L  6 168 ? 68.441  44.472  189.131 1.00 273.96 ?  147 PRO K O   1 
ATOM   21977 C CB  . PRO L  6 168 ? 69.859  43.547  192.171 1.00 273.16 ?  147 PRO K CB  1 
ATOM   21978 C CG  . PRO L  6 168 ? 69.274  44.853  192.661 1.00 273.07 ?  147 PRO K CG  1 
ATOM   21979 C CD  . PRO L  6 168 ? 69.895  45.967  191.833 1.00 280.51 ?  147 PRO K CD  1 
ATOM   21980 N N   . VAL L  6 169 ? 68.341  42.375  189.968 1.00 271.71 ?  148 VAL K N   1 
ATOM   21981 C CA  . VAL L  6 169 ? 67.097  41.993  189.302 1.00 270.03 ?  148 VAL K CA  1 
ATOM   21982 C C   . VAL L  6 169 ? 66.251  41.156  190.258 1.00 264.44 ?  148 VAL K C   1 
ATOM   21983 O O   . VAL L  6 169 ? 66.700  40.101  190.720 1.00 261.68 ?  148 VAL K O   1 
ATOM   21984 C CB  . VAL L  6 169 ? 67.350  41.222  187.997 1.00 271.62 ?  148 VAL K CB  1 
ATOM   21985 C CG1 . VAL L  6 169 ? 66.095  40.513  187.566 1.00 268.60 ?  148 VAL K CG1 1 
ATOM   21986 C CG2 . VAL L  6 169 ? 67.794  42.176  186.910 1.00 277.53 ?  148 VAL K CG2 1 
ATOM   21987 N N   . THR L  6 170 ? 65.035  41.615  190.555 1.00 271.79 ?  149 THR K N   1 
ATOM   21988 C CA  . THR L  6 170 ? 64.113  40.896  191.435 1.00 267.10 ?  149 THR K CA  1 
ATOM   21989 C C   . THR L  6 170 ? 63.285  39.911  190.611 1.00 265.36 ?  149 THR K C   1 
ATOM   21990 O O   . THR L  6 170 ? 62.615  40.313  189.653 1.00 267.11 ?  149 THR K O   1 
ATOM   21991 C CB  . THR L  6 170 ? 63.196  41.858  192.188 1.00 266.62 ?  149 THR K CB  1 
ATOM   21992 O OG1 . THR L  6 170 ? 62.439  42.634  191.254 1.00 269.23 ?  149 THR K OG1 1 
ATOM   21993 C CG2 . THR L  6 170 ? 64.008  42.792  193.067 1.00 268.10 ?  149 THR K CG2 1 
ATOM   21994 N N   . VAL L  6 171 ? 63.325  38.630  190.979 1.00 259.79 ?  150 VAL K N   1 
ATOM   21995 C CA  . VAL L  6 171 ? 62.614  37.579  190.252 1.00 258.58 ?  150 VAL K CA  1 
ATOM   21996 C C   . VAL L  6 171 ? 61.645  36.861  191.185 1.00 256.56 ?  150 VAL K C   1 
ATOM   21997 O O   . VAL L  6 171 ? 62.060  36.275  192.193 1.00 254.48 ?  150 VAL K O   1 
ATOM   21998 C CB  . VAL L  6 171 ? 63.580  36.566  189.616 1.00 257.05 ?  150 VAL K CB  1 
ATOM   21999 C CG1 . VAL L  6 171 ? 62.797  35.439  188.939 1.00 255.69 ?  150 VAL K CG1 1 
ATOM   22000 C CG2 . VAL L  6 171 ? 64.494  37.258  188.619 1.00 259.10 ?  150 VAL K CG2 1 
ATOM   22001 N N   . SER L  6 172 ? 60.356  36.911  190.846 1.00 259.27 ?  151 SER K N   1 
ATOM   22002 C CA  . SER L  6 172 ? 59.304  36.239  191.591 1.00 257.55 ?  151 SER K CA  1 
ATOM   22003 C C   . SER L  6 172 ? 58.585  35.281  190.649 1.00 256.75 ?  151 SER K C   1 
ATOM   22004 O O   . SER L  6 172 ? 58.709  35.370  189.427 1.00 257.99 ?  151 SER K O   1 
ATOM   22005 C CB  . SER L  6 172 ? 58.310  37.232  192.215 1.00 259.07 ?  151 SER K CB  1 
ATOM   22006 O OG  . SER L  6 172 ? 57.670  38.029  191.234 1.00 261.57 ?  151 SER K OG  1 
ATOM   22007 N N   . TRP L  6 173 ? 57.823  34.365  191.233 1.00 255.17 ?  152 TRP K N   1 
ATOM   22008 C CA  . TRP L  6 173 ? 57.098  33.342  190.493 1.00 254.14 ?  152 TRP K CA  1 
ATOM   22009 C C   . TRP L  6 173 ? 55.601  33.445  190.750 1.00 253.17 ?  152 TRP K C   1 
ATOM   22010 O O   . TRP L  6 173 ? 55.163  33.473  191.905 1.00 251.74 ?  152 TRP K O   1 
ATOM   22011 C CB  . TRP L  6 173 ? 57.656  31.963  190.844 1.00 252.22 ?  152 TRP K CB  1 
ATOM   22012 C CG  . TRP L  6 173 ? 59.058  31.765  190.322 1.00 253.52 ?  152 TRP K CG  1 
ATOM   22013 C CD1 . TRP L  6 173 ? 60.217  32.228  190.875 1.00 254.32 ?  152 TRP K CD1 1 
ATOM   22014 C CD2 . TRP L  6 173 ? 59.446  30.956  189.201 1.00 254.22 ?  152 TRP K CD2 1 
ATOM   22015 N NE1 . TRP L  6 173 ? 61.297  31.814  190.128 1.00 255.71 ?  152 TRP K NE1 1 
ATOM   22016 C CE2 . TRP L  6 173 ? 60.851  31.025  189.101 1.00 255.66 ?  152 TRP K CE2 1 
ATOM   22017 C CE3 . TRP L  6 173 ? 58.739  30.198  188.261 1.00 253.94 ?  152 TRP K CE3 1 
ATOM   22018 C CZ2 . TRP L  6 173 ? 61.561  30.361  188.101 1.00 256.90 ?  152 TRP K CZ2 1 
ATOM   22019 C CZ3 . TRP L  6 173 ? 59.446  29.542  187.268 1.00 255.05 ?  152 TRP K CZ3 1 
ATOM   22020 C CH2 . TRP L  6 173 ? 60.842  29.627  187.196 1.00 256.54 ?  152 TRP K CH2 1 
ATOM   22021 N N   . ASN L  6 174 ? 54.831  33.497  189.659 1.00 259.60 ?  153 ASN K N   1 
ATOM   22022 C CA  . ASN L  6 174 ? 53.371  33.623  189.682 1.00 261.73 ?  153 ASN K CA  1 
ATOM   22023 C C   . ASN L  6 174 ? 52.926  34.830  190.509 1.00 262.04 ?  153 ASN K C   1 
ATOM   22024 O O   . ASN L  6 174 ? 51.979  34.758  191.296 1.00 263.45 ?  153 ASN K O   1 
ATOM   22025 C CB  . ASN L  6 174 ? 52.725  32.336  190.210 1.00 257.04 ?  153 ASN K CB  1 
ATOM   22026 C CG  . ASN L  6 174 ? 52.155  31.459  189.102 1.00 258.88 ?  153 ASN K CG  1 
ATOM   22027 O OD1 . ASN L  6 174 ? 51.700  31.958  188.074 1.00 264.62 ?  153 ASN K OD1 1 
ATOM   22028 N ND2 . ASN L  6 174 ? 52.170  30.146  189.315 1.00 253.78 ?  153 ASN K ND2 1 
ATOM   22029 N N   . SER L  6 175 ? 53.617  35.956  190.317 1.00 244.41 ?  154 SER K N   1 
ATOM   22030 C CA  . SER L  6 175 ? 53.330  37.203  191.031 1.00 246.15 ?  154 SER K CA  1 
ATOM   22031 C C   . SER L  6 175 ? 53.419  37.009  192.543 1.00 244.44 ?  154 SER K C   1 
ATOM   22032 O O   . SER L  6 175 ? 52.745  37.696  193.312 1.00 245.20 ?  154 SER K O   1 
ATOM   22033 C CB  . SER L  6 175 ? 51.969  37.786  190.629 1.00 247.88 ?  154 SER K CB  1 
ATOM   22034 O OG  . SER L  6 175 ? 50.896  36.991  191.098 1.00 246.22 ?  154 SER K OG  1 
ATOM   22035 N N   . GLY L  6 176 ? 54.263  36.075  192.967 1.00 248.26 ?  155 GLY K N   1 
ATOM   22036 C CA  . GLY L  6 176 ? 54.501  35.792  194.366 1.00 246.47 ?  155 GLY K CA  1 
ATOM   22037 C C   . GLY L  6 176 ? 53.638  34.708  194.975 1.00 244.14 ?  155 GLY K C   1 
ATOM   22038 O O   . GLY L  6 176 ? 53.606  34.587  196.205 1.00 242.88 ?  155 GLY K O   1 
ATOM   22039 N N   . ALA L  6 177 ? 52.933  33.918  194.164 1.00 254.74 ?  156 ALA K N   1 
ATOM   22040 C CA  . ALA L  6 177 ? 52.084  32.849  194.670 1.00 254.16 ?  156 ALA K CA  1 
ATOM   22041 C C   . ALA L  6 177 ? 52.813  31.510  194.730 1.00 250.31 ?  156 ALA K C   1 
ATOM   22042 O O   . ALA L  6 177 ? 52.160  30.461  194.782 1.00 249.46 ?  156 ALA K O   1 
ATOM   22043 C CB  . ALA L  6 177 ? 50.820  32.723  193.816 1.00 255.96 ?  156 ALA K CB  1 
ATOM   22044 N N   . LEU L  6 178 ? 54.150  31.523  194.720 1.00 248.86 ?  157 LEU K N   1 
ATOM   22045 C CA  . LEU L  6 178 ? 54.930  30.286  194.774 1.00 245.42 ?  157 LEU K CA  1 
ATOM   22046 C C   . LEU L  6 178 ? 56.310  30.626  195.340 1.00 244.10 ?  157 LEU K C   1 
ATOM   22047 O O   . LEU L  6 178 ? 57.167  31.144  194.617 1.00 244.18 ?  157 LEU K O   1 
ATOM   22048 C CB  . LEU L  6 178 ? 55.022  29.614  193.412 1.00 244.22 ?  157 LEU K CB  1 
ATOM   22049 C CG  . LEU L  6 178 ? 55.725  28.251  193.405 1.00 241.04 ?  157 LEU K CG  1 
ATOM   22050 C CD1 . LEU L  6 178 ? 55.019  27.292  192.459 1.00 240.37 ?  157 LEU K CD1 1 
ATOM   22051 C CD2 . LEU L  6 178 ? 57.190  28.383  193.023 1.00 241.32 ?  157 LEU K CD2 1 
ATOM   22052 N N   . THR L  6 179 ? 56.498  30.357  196.629 1.00 251.22 ?  158 THR K N   1 
ATOM   22053 C CA  . THR L  6 179 ? 57.740  30.650  197.330 1.00 249.96 ?  158 THR K CA  1 
ATOM   22054 C C   . THR L  6 179 ? 58.420  29.398  197.869 1.00 246.94 ?  158 THR K C   1 
ATOM   22055 O O   . THR L  6 179 ? 59.464  29.507  198.522 1.00 245.76 ?  158 THR K O   1 
ATOM   22056 C CB  . THR L  6 179 ? 57.481  31.625  198.486 1.00 251.80 ?  158 THR K CB  1 
ATOM   22057 O OG1 . THR L  6 179 ? 58.711  31.892  199.170 1.00 250.50 ?  158 THR K OG1 1 
ATOM   22058 C CG2 . THR L  6 179 ? 56.479  31.028  199.472 1.00 252.69 ?  158 THR K CG2 1 
ATOM   22059 N N   . SER L  6 180 ? 57.857  28.221  197.619 1.00 241.41 ?  159 SER K N   1 
ATOM   22060 C CA  . SER L  6 180 ? 58.386  26.952  198.102 1.00 240.40 ?  159 SER K CA  1 
ATOM   22061 C C   . SER L  6 180 ? 59.161  26.242  196.996 1.00 240.69 ?  159 SER K C   1 
ATOM   22062 O O   . SER L  6 180 ? 58.597  25.916  195.946 1.00 240.98 ?  159 SER K O   1 
ATOM   22063 C CB  . SER L  6 180 ? 57.249  26.067  198.607 1.00 239.77 ?  159 SER K CB  1 
ATOM   22064 O OG  . SER L  6 180 ? 56.298  25.843  197.580 1.00 240.06 ?  159 SER K OG  1 
ATOM   22065 N N   . GLY L  6 181 ? 60.454  26.016  197.234 1.00 235.12 ?  160 GLY K N   1 
ATOM   22066 C CA  . GLY L  6 181 ? 61.316  25.333  196.288 1.00 234.48 ?  160 GLY K CA  1 
ATOM   22067 C C   . GLY L  6 181 ? 62.040  26.220  195.300 1.00 236.74 ?  160 GLY K C   1 
ATOM   22068 O O   . GLY L  6 181 ? 62.610  25.703  194.331 1.00 236.51 ?  160 GLY K O   1 
ATOM   22069 N N   . VAL L  6 182 ? 62.038  27.531  195.514 1.00 231.40 ?  161 VAL K N   1 
ATOM   22070 C CA  . VAL L  6 182 ? 62.679  28.488  194.620 1.00 233.76 ?  161 VAL K CA  1 
ATOM   22071 C C   . VAL L  6 182 ? 64.104  28.762  195.094 1.00 233.53 ?  161 VAL K C   1 
ATOM   22072 O O   . VAL L  6 182 ? 64.326  29.078  196.269 1.00 233.05 ?  161 VAL K O   1 
ATOM   22073 C CB  . VAL L  6 182 ? 61.863  29.791  194.554 1.00 236.38 ?  161 VAL K CB  1 
ATOM   22074 C CG1 . VAL L  6 182 ? 60.671  29.634  193.626 1.00 237.17 ?  161 VAL K CG1 1 
ATOM   22075 C CG2 . VAL L  6 182 ? 61.384  30.181  195.944 1.00 236.02 ?  161 VAL K CG2 1 
ATOM   22076 N N   . HIS L  6 183 ? 65.076  28.608  194.190 1.00 259.08 ?  162 HIS K N   1 
ATOM   22077 C CA  . HIS L  6 183 ? 66.489  28.858  194.489 1.00 258.91 ?  162 HIS K CA  1 
ATOM   22078 C C   . HIS L  6 183 ? 67.054  29.740  193.372 1.00 262.12 ?  162 HIS K C   1 
ATOM   22079 O O   . HIS L  6 183 ? 67.359  29.256  192.277 1.00 263.61 ?  162 HIS K O   1 
ATOM   22080 C CB  . HIS L  6 183 ? 67.266  27.550  194.636 1.00 258.02 ?  162 HIS K CB  1 
ATOM   22081 C CG  . HIS L  6 183 ? 66.917  26.778  195.874 1.00 256.78 ?  162 HIS K CG  1 
ATOM   22082 N ND1 . HIS L  6 183 ? 67.412  27.101  197.119 1.00 255.07 ?  162 HIS K ND1 1 
ATOM   22083 C CD2 . HIS L  6 183 ? 66.126  25.694  196.056 1.00 257.81 ?  162 HIS K CD2 1 
ATOM   22084 C CE1 . HIS L  6 183 ? 66.937  26.254  198.015 1.00 252.73 ?  162 HIS K CE1 1 
ATOM   22085 N NE2 . HIS L  6 183 ? 66.154  25.390  197.396 1.00 254.66 ?  162 HIS K NE2 1 
ATOM   22086 N N   . THR L  6 184 ? 67.190  31.034  193.663 1.00 255.33 ?  163 THR K N   1 
ATOM   22087 C CA  . THR L  6 184 ? 67.731  32.026  192.736 1.00 258.92 ?  163 THR K CA  1 
ATOM   22088 C C   . THR L  6 184 ? 69.239  32.167  192.918 1.00 260.81 ?  163 THR K C   1 
ATOM   22089 O O   . THR L  6 184 ? 69.711  32.436  194.028 1.00 260.07 ?  163 THR K O   1 
ATOM   22090 C CB  . THR L  6 184 ? 67.045  33.376  192.931 1.00 259.92 ?  163 THR K CB  1 
ATOM   22091 O OG1 . THR L  6 184 ? 65.639  33.230  192.697 1.00 260.36 ?  163 THR K OG1 1 
ATOM   22092 C CG2 . THR L  6 184 ? 67.610  34.396  191.951 1.00 263.41 ?  163 THR K CG2 1 
ATOM   22093 N N   . PHE L  6 185 ? 70.030  31.962  191.778 1.00 272.29 ?  164 PHE K N   1 
ATOM   22094 C CA  . PHE L  6 185 ? 71.487  32.008  191.777 1.00 272.71 ?  164 PHE K CA  1 
ATOM   22095 C C   . PHE L  6 185 ? 72.046  33.406  191.509 1.00 275.04 ?  164 PHE K C   1 
ATOM   22096 O O   . PHE L  6 185 ? 71.448  34.201  190.780 1.00 278.39 ?  164 PHE K O   1 
ATOM   22097 C CB  . PHE L  6 185 ? 72.041  31.058  190.716 1.00 273.30 ?  164 PHE K CB  1 
ATOM   22098 C CG  . PHE L  6 185 ? 71.763  29.612  190.986 1.00 271.65 ?  164 PHE K CG  1 
ATOM   22099 C CD1 . PHE L  6 185 ? 70.597  29.009  190.549 1.00 270.73 ?  164 PHE K CD1 1 
ATOM   22100 C CD2 . PHE L  6 185 ? 72.701  28.843  191.650 1.00 269.10 ?  164 PHE K CD2 1 
ATOM   22101 C CE1 . PHE L  6 185 ? 70.363  27.667  190.800 1.00 266.77 ?  164 PHE K CE1 1 
ATOM   22102 C CE2 . PHE L  6 185 ? 72.474  27.508  191.902 1.00 266.37 ?  164 PHE K CE2 1 
ATOM   22103 C CZ  . PHE L  6 185 ? 71.305  26.916  191.476 1.00 265.03 ?  164 PHE K CZ  1 
ATOM   22104 N N   . PRO L  6 186 ? 73.198  33.670  192.127 1.00 262.62 ?  165 PRO K N   1 
ATOM   22105 C CA  . PRO L  6 186 ? 73.914  34.934  191.920 1.00 265.09 ?  165 PRO K CA  1 
ATOM   22106 C C   . PRO L  6 186 ? 74.433  35.085  190.501 1.00 266.57 ?  165 PRO K C   1 
ATOM   22107 O O   . PRO L  6 186 ? 74.832  34.112  189.854 1.00 265.23 ?  165 PRO K O   1 
ATOM   22108 C CB  . PRO L  6 186 ? 75.074  34.849  192.917 1.00 263.83 ?  165 PRO K CB  1 
ATOM   22109 C CG  . PRO L  6 186 ? 75.256  33.402  193.141 1.00 260.82 ?  165 PRO K CG  1 
ATOM   22110 C CD  . PRO L  6 186 ? 73.895  32.805  193.085 1.00 259.98 ?  165 PRO K CD  1 
ATOM   22111 N N   . ALA L  6 187 ? 74.425  36.325  190.018 1.00 273.15 ?  166 ALA K N   1 
ATOM   22112 C CA  . ALA L  6 187 ? 74.848  36.583  188.654 1.00 278.51 ?  166 ALA K CA  1 
ATOM   22113 C C   . ALA L  6 187 ? 76.353  36.359  188.503 1.00 281.45 ?  166 ALA K C   1 
ATOM   22114 O O   . ALA L  6 187 ? 77.095  36.223  189.479 1.00 283.19 ?  166 ALA K O   1 
ATOM   22115 C CB  . ALA L  6 187 ? 74.491  38.015  188.251 1.00 281.76 ?  166 ALA K CB  1 
ATOM   22116 N N   . VAL L  6 188 ? 76.797  36.329  187.250 1.00 272.06 ?  167 VAL K N   1 
ATOM   22117 C CA  . VAL L  6 188 ? 78.199  36.169  186.883 1.00 275.18 ?  167 VAL K CA  1 
ATOM   22118 C C   . VAL L  6 188 ? 78.582  37.344  185.995 1.00 281.85 ?  167 VAL K C   1 
ATOM   22119 O O   . VAL L  6 188 ? 77.849  37.678  185.058 1.00 284.90 ?  167 VAL K O   1 
ATOM   22120 C CB  . VAL L  6 188 ? 78.477  34.831  186.176 1.00 274.41 ?  167 VAL K CB  1 
ATOM   22121 C CG1 . VAL L  6 188 ? 77.515  34.625  185.049 1.00 274.64 ?  167 VAL K CG1 1 
ATOM   22122 C CG2 . VAL L  6 188 ? 79.898  34.789  185.659 1.00 279.10 ?  167 VAL K CG2 1 
ATOM   22123 N N   . LEU L  6 189 ? 79.698  37.992  186.300 1.00 275.45 ?  168 LEU K N   1 
ATOM   22124 C CA  . LEU L  6 189 ? 80.149  39.110  185.479 1.00 287.48 ?  168 LEU K CA  1 
ATOM   22125 C C   . LEU L  6 189 ? 80.879  38.554  184.264 1.00 289.33 ?  168 LEU K C   1 
ATOM   22126 O O   . LEU L  6 189 ? 81.987  38.030  184.396 1.00 289.98 ?  168 LEU K O   1 
ATOM   22127 C CB  . LEU L  6 189 ? 81.107  40.010  186.253 1.00 290.23 ?  168 LEU K CB  1 
ATOM   22128 C CG  . LEU L  6 189 ? 81.683  41.238  185.528 1.00 292.21 ?  168 LEU K CG  1 
ATOM   22129 C CD1 . LEU L  6 189 ? 80.600  42.228  185.086 1.00 293.63 ?  168 LEU K CD1 1 
ATOM   22130 C CD2 . LEU L  6 189 ? 82.811  41.907  186.317 1.00 283.39 ?  168 LEU K CD2 1 
ATOM   22131 N N   . GLN L  6 190 ? 80.273  38.636  183.081 1.00 275.21 ?  169 GLN K N   1 
ATOM   22132 C CA  . GLN L  6 190 ? 81.008  38.119  181.938 1.00 279.32 ?  169 GLN K CA  1 
ATOM   22133 C C   . GLN L  6 190 ? 82.128  39.077  181.555 1.00 281.70 ?  169 GLN K C   1 
ATOM   22134 O O   . GLN L  6 190 ? 82.280  40.172  182.105 1.00 282.55 ?  169 GLN K O   1 
ATOM   22135 C CB  . GLN L  6 190 ? 80.143  37.824  180.708 1.00 281.88 ?  169 GLN K CB  1 
ATOM   22136 C CG  . GLN L  6 190 ? 79.053  36.771  180.820 1.00 275.57 ?  169 GLN K CG  1 
ATOM   22137 C CD  . GLN L  6 190 ? 78.271  36.665  179.517 1.00 278.84 ?  169 GLN K CD  1 
ATOM   22138 O OE1 . GLN L  6 190 ? 78.490  37.452  178.597 1.00 285.89 ?  169 GLN K OE1 1 
ATOM   22139 N NE2 . GLN L  6 190 ? 77.417  35.650  179.404 1.00 274.95 ?  169 GLN K NE2 1 
ATOM   22140 N N   . SER L  6 191 ? 82.917  38.646  180.576 1.00 286.35 ?  170 SER K N   1 
ATOM   22141 C CA  . SER L  6 191 ? 84.032  39.452  180.114 1.00 287.15 ?  170 SER K CA  1 
ATOM   22142 C C   . SER L  6 191 ? 83.544  40.682  179.367 1.00 291.36 ?  170 SER K C   1 
ATOM   22143 O O   . SER L  6 191 ? 84.293  41.655  179.236 1.00 292.54 ?  170 SER K O   1 
ATOM   22144 C CB  . SER L  6 191 ? 84.932  38.592  179.232 1.00 285.78 ?  170 SER K CB  1 
ATOM   22145 O OG  . SER L  6 191 ? 84.202  38.121  178.113 1.00 287.75 ?  170 SER K OG  1 
ATOM   22146 N N   . SER L  6 192 ? 82.310  40.658  178.869 1.00 287.51 ?  171 SER K N   1 
ATOM   22147 C CA  . SER L  6 192 ? 81.770  41.809  178.163 1.00 291.55 ?  171 SER K CA  1 
ATOM   22148 C C   . SER L  6 192 ? 81.368  42.920  179.127 1.00 292.36 ?  171 SER K C   1 
ATOM   22149 O O   . SER L  6 192 ? 81.176  44.061  178.692 1.00 295.57 ?  171 SER K O   1 
ATOM   22150 C CB  . SER L  6 192 ? 80.557  41.400  177.327 1.00 293.68 ?  171 SER K CB  1 
ATOM   22151 O OG  . SER L  6 192 ? 79.544  40.851  178.152 1.00 292.37 ?  171 SER K OG  1 
ATOM   22152 N N   . GLY L  6 193 ? 81.244  42.608  180.416 1.00 297.83 ?  172 GLY K N   1 
ATOM   22153 C CA  . GLY L  6 193 ? 80.868  43.576  181.428 1.00 298.27 ?  172 GLY K CA  1 
ATOM   22154 C C   . GLY L  6 193 ? 79.388  43.579  181.733 1.00 299.80 ?  172 GLY K C   1 
ATOM   22155 O O   . GLY L  6 193 ? 78.873  44.587  182.231 1.00 303.73 ?  172 GLY K O   1 
ATOM   22156 N N   . LEU L  6 194 ? 78.698  42.479  181.443 1.00 289.93 ?  173 LEU K N   1 
ATOM   22157 C CA  . LEU L  6 194 ? 77.268  42.299  181.643 1.00 285.62 ?  173 LEU K CA  1 
ATOM   22158 C C   . LEU L  6 194 ? 76.994  41.112  182.560 1.00 277.73 ?  173 LEU K C   1 
ATOM   22159 O O   . LEU L  6 194 ? 77.678  40.085  182.477 1.00 275.94 ?  173 LEU K O   1 
ATOM   22160 C CB  . LEU L  6 194 ? 76.583  42.092  180.290 1.00 288.81 ?  173 LEU K CB  1 
ATOM   22161 C CG  . LEU L  6 194 ? 76.710  43.300  179.355 1.00 296.71 ?  173 LEU K CG  1 
ATOM   22162 C CD1 . LEU L  6 194 ? 76.174  42.993  177.966 1.00 300.07 ?  173 LEU K CD1 1 
ATOM   22163 C CD2 . LEU L  6 194 ? 76.021  44.520  179.934 1.00 296.58 ?  173 LEU K CD2 1 
ATOM   22164 N N   . TYR L  6 195 ? 76.000  41.258  183.439 1.00 285.30 ?  174 TYR K N   1 
ATOM   22165 C CA  . TYR L  6 195 ? 75.604  40.219  184.383 1.00 278.17 ?  174 TYR K CA  1 
ATOM   22166 C C   . TYR L  6 195 ? 74.604  39.252  183.734 1.00 275.81 ?  174 TYR K C   1 
ATOM   22167 O O   . TYR L  6 195 ? 73.996  39.547  182.703 1.00 279.14 ?  174 TYR K O   1 
ATOM   22168 C CB  . TYR L  6 195 ? 75.027  40.822  185.670 1.00 274.35 ?  174 TYR K CB  1 
ATOM   22169 C CG  . TYR L  6 195 ? 75.999  41.689  186.456 1.00 275.70 ?  174 TYR K CG  1 
ATOM   22170 C CD1 . TYR L  6 195 ? 76.911  41.109  187.333 1.00 272.95 ?  174 TYR K CD1 1 
ATOM   22171 C CD2 . TYR L  6 195 ? 75.983  43.076  186.356 1.00 278.75 ?  174 TYR K CD2 1 
ATOM   22172 C CE1 . TYR L  6 195 ? 77.797  41.880  188.063 1.00 273.89 ?  174 TYR K CE1 1 
ATOM   22173 C CE2 . TYR L  6 195 ? 76.867  43.857  187.089 1.00 279.56 ?  174 TYR K CE2 1 
ATOM   22174 C CZ  . TYR L  6 195 ? 77.769  43.252  187.939 1.00 277.11 ?  174 TYR K CZ  1 
ATOM   22175 O OH  . TYR L  6 195 ? 78.643  44.031  188.663 1.00 278.06 ?  174 TYR K OH  1 
ATOM   22176 N N   . SER L  6 196 ? 74.441  38.087  184.367 1.00 280.33 ?  175 SER K N   1 
ATOM   22177 C CA  . SER L  6 196 ? 73.558  37.016  183.888 1.00 275.70 ?  175 SER K CA  1 
ATOM   22178 C C   . SER L  6 196 ? 73.213  36.081  185.043 1.00 269.08 ?  175 SER K C   1 
ATOM   22179 O O   . SER L  6 196 ? 74.122  35.514  185.657 1.00 265.25 ?  175 SER K O   1 
ATOM   22180 C CB  . SER L  6 196 ? 74.218  36.249  182.736 1.00 276.79 ?  175 SER K CB  1 
ATOM   22181 O OG  . SER L  6 196 ? 75.596  36.026  182.977 1.00 273.40 ?  175 SER K OG  1 
ATOM   22182 N N   . LEU L  6 197 ? 71.917  35.908  185.335 1.00 274.01 ?  176 LEU K N   1 
ATOM   22183 C CA  . LEU L  6 197 ? 71.432  35.063  186.431 1.00 268.20 ?  176 LEU K CA  1 
ATOM   22184 C C   . LEU L  6 197 ? 70.580  33.903  185.914 1.00 267.66 ?  176 LEU K C   1 
ATOM   22185 O O   . LEU L  6 197 ? 70.362  33.746  184.711 1.00 272.17 ?  176 LEU K O   1 
ATOM   22186 C CB  . LEU L  6 197 ? 70.480  35.870  187.325 1.00 267.65 ?  176 LEU K CB  1 
ATOM   22187 C CG  . LEU L  6 197 ? 70.621  37.122  188.188 1.00 268.18 ?  176 LEU K CG  1 
ATOM   22188 C CD1 . LEU L  6 197 ? 69.223  37.509  188.619 1.00 265.82 ?  176 LEU K CD1 1 
ATOM   22189 C CD2 . LEU L  6 197 ? 71.421  36.902  189.422 1.00 263.80 ?  176 LEU K CD2 1 
ATOM   22190 N N   . SER L  6 198 ? 70.116  33.076  186.863 1.00 261.43 ?  177 SER K N   1 
ATOM   22191 C CA  . SER L  6 198 ? 69.240  31.935  186.611 1.00 258.42 ?  177 SER K CA  1 
ATOM   22192 C C   . SER L  6 198 ? 68.386  31.691  187.856 1.00 254.84 ?  177 SER K C   1 
ATOM   22193 O O   . SER L  6 198 ? 68.812  31.995  188.974 1.00 254.66 ?  177 SER K O   1 
ATOM   22194 C CB  . SER L  6 198 ? 70.046  30.676  186.261 1.00 256.57 ?  177 SER K CB  1 
ATOM   22195 O OG  . SER L  6 198 ? 70.843  30.872  185.104 1.00 264.37 ?  177 SER K OG  1 
ATOM   22196 N N   . SER L  6 199 ? 67.182  31.137  187.664 1.00 256.66 ?  178 SER K N   1 
ATOM   22197 C CA  . SER L  6 199 ? 66.262  30.842  188.769 1.00 252.82 ?  178 SER K CA  1 
ATOM   22198 C C   . SER L  6 199 ? 65.497  29.547  188.510 1.00 250.17 ?  178 SER K C   1 
ATOM   22199 O O   . SER L  6 199 ? 64.729  29.488  187.547 1.00 250.70 ?  178 SER K O   1 
ATOM   22200 C CB  . SER L  6 199 ? 65.287  32.003  188.981 1.00 253.02 ?  178 SER K CB  1 
ATOM   22201 O OG  . SER L  6 199 ? 64.441  31.762  190.091 1.00 249.72 ?  178 SER K OG  1 
ATOM   22202 N N   . VAL L  6 200 ? 65.668  28.523  189.359 1.00 247.59 ?  179 VAL K N   1 
ATOM   22203 C CA  . VAL L  6 200 ? 64.990  27.239  189.160 1.00 245.58 ?  179 VAL K CA  1 
ATOM   22204 C C   . VAL L  6 200 ? 63.943  26.981  190.245 1.00 244.35 ?  179 VAL K C   1 
ATOM   22205 O O   . VAL L  6 200 ? 64.051  27.477  191.374 1.00 244.20 ?  179 VAL K O   1 
ATOM   22206 C CB  . VAL L  6 200 ? 66.006  26.078  189.118 1.00 244.08 ?  179 VAL K CB  1 
ATOM   22207 C CG1 . VAL L  6 200 ? 66.938  26.240  187.934 1.00 247.23 ?  179 VAL K CG1 1 
ATOM   22208 C CG2 . VAL L  6 200 ? 66.798  26.005  190.420 1.00 243.09 ?  179 VAL K CG2 1 
ATOM   22209 N N   . VAL L  6 201 ? 62.915  26.199  189.886 1.00 249.43 ?  180 VAL K N   1 
ATOM   22210 C CA  . VAL L  6 201 ? 61.831  25.812  190.789 1.00 247.16 ?  180 VAL K CA  1 
ATOM   22211 C C   . VAL L  6 201 ? 61.610  24.305  190.716 1.00 246.58 ?  180 VAL K C   1 
ATOM   22212 O O   . VAL L  6 201 ? 61.390  23.761  189.628 1.00 246.97 ?  180 VAL K O   1 
ATOM   22213 C CB  . VAL L  6 201 ? 60.514  26.537  190.459 1.00 251.54 ?  180 VAL K CB  1 
ATOM   22214 C CG1 . VAL L  6 201 ? 59.421  26.087  191.412 1.00 244.40 ?  180 VAL K CG1 1 
ATOM   22215 C CG2 . VAL L  6 201 ? 60.702  28.025  190.531 1.00 255.99 ?  180 VAL K CG2 1 
ATOM   22216 N N   . THR L  6 202 ? 61.649  23.638  191.869 1.00 239.28 ?  181 THR K N   1 
ATOM   22217 C CA  . THR L  6 202 ? 61.397  22.200  191.963 1.00 236.71 ?  181 THR K CA  1 
ATOM   22218 C C   . THR L  6 202 ? 59.888  21.962  192.013 1.00 236.64 ?  181 THR K C   1 
ATOM   22219 O O   . THR L  6 202 ? 59.243  22.274  193.019 1.00 236.46 ?  181 THR K O   1 
ATOM   22220 C CB  . THR L  6 202 ? 62.095  21.598  193.182 1.00 234.40 ?  181 THR K CB  1 
ATOM   22221 O OG1 . THR L  6 202 ? 61.639  22.247  194.376 1.00 234.61 ?  181 THR K OG1 1 
ATOM   22222 C CG2 . THR L  6 202 ? 63.612  21.743  193.066 1.00 234.37 ?  181 THR K CG2 1 
ATOM   22223 N N   . VAL L  6 203 ? 59.309  21.409  190.951 1.00 255.80 ?  182 VAL K N   1 
ATOM   22224 C CA  . VAL L  6 203 ? 57.862  21.191  190.945 1.00 256.87 ?  182 VAL K CA  1 
ATOM   22225 C C   . VAL L  6 203 ? 57.540  19.728  190.671 1.00 256.28 ?  182 VAL K C   1 
ATOM   22226 O O   . VAL L  6 203 ? 58.319  19.029  190.006 1.00 254.97 ?  182 VAL K O   1 
ATOM   22227 C CB  . VAL L  6 203 ? 57.158  22.089  189.915 1.00 252.90 ?  182 VAL K CB  1 
ATOM   22228 C CG1 . VAL L  6 203 ? 57.222  23.533  190.344 1.00 247.62 ?  182 VAL K CG1 1 
ATOM   22229 C CG2 . VAL L  6 203 ? 57.779  21.906  188.549 1.00 247.00 ?  182 VAL K CG2 1 
ATOM   22230 N N   . PRO L  6 204 ? 56.410  19.227  191.171 1.00 263.59 ?  183 PRO K N   1 
ATOM   22231 C CA  . PRO L  6 204 ? 56.018  17.844  190.883 1.00 262.28 ?  183 PRO K CA  1 
ATOM   22232 C C   . PRO L  6 204 ? 55.786  17.632  189.398 1.00 265.64 ?  183 PRO K C   1 
ATOM   22233 O O   . PRO L  6 204 ? 55.317  18.523  188.686 1.00 265.70 ?  183 PRO K O   1 
ATOM   22234 C CB  . PRO L  6 204 ? 54.717  17.667  191.677 1.00 258.97 ?  183 PRO K CB  1 
ATOM   22235 C CG  . PRO L  6 204 ? 54.219  19.048  191.907 1.00 258.45 ?  183 PRO K CG  1 
ATOM   22236 C CD  . PRO L  6 204 ? 55.443  19.892  192.061 1.00 257.72 ?  183 PRO K CD  1 
ATOM   22237 N N   . SER L  6 205 ? 56.137  16.431  188.928 1.00 282.50 ?  184 SER K N   1 
ATOM   22238 C CA  . SER L  6 205 ? 55.998  16.150  187.506 1.00 285.02 ?  184 SER K CA  1 
ATOM   22239 C C   . SER L  6 205 ? 54.543  16.265  187.091 1.00 288.88 ?  184 SER K C   1 
ATOM   22240 O O   . SER L  6 205 ? 54.246  16.540  185.922 1.00 292.24 ?  184 SER K O   1 
ATOM   22241 C CB  . SER L  6 205 ? 56.531  14.754  187.178 1.00 283.08 ?  184 SER K CB  1 
ATOM   22242 O OG  . SER L  6 205 ? 57.887  14.612  187.561 1.00 277.80 ?  184 SER K OG  1 
ATOM   22243 N N   . SER L  6 206 ? 53.625  16.056  188.035 1.00 272.29 ?  185 SER K N   1 
ATOM   22244 C CA  . SER L  6 206 ? 52.198  16.168  187.770 1.00 271.90 ?  185 SER K CA  1 
ATOM   22245 C C   . SER L  6 206 ? 51.876  17.642  187.554 1.00 270.34 ?  185 SER K C   1 
ATOM   22246 O O   . SER L  6 206 ? 51.394  18.350  188.442 1.00 267.07 ?  185 SER K O   1 
ATOM   22247 C CB  . SER L  6 206 ? 51.390  15.599  188.931 1.00 267.70 ?  185 SER K CB  1 
ATOM   22248 O OG  . SER L  6 206 ? 51.664  16.307  190.132 1.00 263.45 ?  185 SER K OG  1 
ATOM   22249 N N   . SER L  6 207 ? 52.160  18.118  186.348 1.00 262.41 ?  186 SER K N   1 
ATOM   22250 C CA  . SER L  6 207 ? 51.887  19.506  186.018 1.00 265.14 ?  186 SER K CA  1 
ATOM   22251 C C   . SER L  6 207 ? 51.304  19.533  184.617 1.00 266.69 ?  186 SER K C   1 
ATOM   22252 O O   . SER L  6 207 ? 51.679  20.339  183.763 1.00 268.79 ?  186 SER K O   1 
ATOM   22253 C CB  . SER L  6 207 ? 53.150  20.368  186.115 1.00 266.18 ?  186 SER K CB  1 
ATOM   22254 O OG  . SER L  6 207 ? 53.713  20.333  187.416 1.00 264.74 ?  186 SER K OG  1 
ATOM   22255 N N   . LEU L  6 208 ? 50.360  18.619  184.382 1.00 273.10 ?  187 LEU K N   1 
ATOM   22256 C CA  . LEU L  6 208 ? 49.629  18.612  183.125 1.00 278.45 ?  187 LEU K CA  1 
ATOM   22257 C C   . LEU L  6 208 ? 48.805  19.884  183.029 1.00 279.80 ?  187 LEU K C   1 
ATOM   22258 O O   . LEU L  6 208 ? 48.764  20.546  181.985 1.00 281.78 ?  187 LEU K O   1 
ATOM   22259 C CB  . LEU L  6 208 ? 48.767  17.352  183.012 1.00 277.01 ?  187 LEU K CB  1 
ATOM   22260 C CG  . LEU L  6 208 ? 48.289  16.952  181.609 1.00 275.87 ?  187 LEU K CG  1 
ATOM   22261 C CD1 . LEU L  6 208 ? 47.084  17.758  181.140 1.00 279.19 ?  187 LEU K CD1 1 
ATOM   22262 C CD2 . LEU L  6 208 ? 49.441  17.082  180.614 1.00 277.61 ?  187 LEU K CD2 1 
ATOM   22263 N N   . GLY L  6 209 ? 48.131  20.218  184.128 1.00 271.30 ?  188 GLY K N   1 
ATOM   22264 C CA  . GLY L  6 209 ? 47.409  21.455  184.324 1.00 270.32 ?  188 GLY K CA  1 
ATOM   22265 C C   . GLY L  6 209 ? 46.474  21.995  183.264 1.00 280.33 ?  188 GLY K C   1 
ATOM   22266 O O   . GLY L  6 209 ? 45.366  21.491  183.095 1.00 288.30 ?  188 GLY K O   1 
ATOM   22267 N N   . THR L  6 210 ? 46.917  23.030  182.554 1.00 275.74 ?  189 THR K N   1 
ATOM   22268 C CA  . THR L  6 210 ? 48.271  23.557  182.711 1.00 272.37 ?  189 THR K CA  1 
ATOM   22269 C C   . THR L  6 210 ? 48.440  24.427  183.949 1.00 270.89 ?  189 THR K C   1 
ATOM   22270 O O   . THR L  6 210 ? 47.873  25.512  184.049 1.00 274.21 ?  189 THR K O   1 
ATOM   22271 C CB  . THR L  6 210 ? 48.674  24.379  181.479 1.00 271.38 ?  189 THR K CB  1 
ATOM   22272 O OG1 . THR L  6 210 ? 47.751  25.462  181.303 1.00 270.58 ?  189 THR K OG1 1 
ATOM   22273 C CG2 . THR L  6 210 ? 48.651  23.505  180.244 1.00 270.78 ?  189 THR K CG2 1 
ATOM   22274 N N   . GLN L  6 211 ? 49.231  23.930  184.899 1.00 268.14 ?  190 GLN K N   1 
ATOM   22275 C CA  . GLN L  6 211 ? 49.576  24.725  186.067 1.00 262.67 ?  190 GLN K CA  1 
ATOM   22276 C C   . GLN L  6 211 ? 50.566  25.805  185.638 1.00 264.25 ?  190 GLN K C   1 
ATOM   22277 O O   . GLN L  6 211 ? 51.781  25.590  185.693 1.00 264.03 ?  190 GLN K O   1 
ATOM   22278 C CB  . GLN L  6 211 ? 50.161  23.856  187.183 1.00 253.01 ?  190 GLN K CB  1 
ATOM   22279 C CG  . GLN L  6 211 ? 49.481  24.080  188.540 1.00 247.99 ?  190 GLN K CG  1 
ATOM   22280 C CD  . GLN L  6 211 ? 49.790  25.425  189.176 1.00 247.06 ?  190 GLN K CD  1 
ATOM   22281 O OE1 . GLN L  6 211 ? 50.731  26.112  188.788 1.00 249.70 ?  190 GLN K OE1 1 
ATOM   22282 N NE2 . GLN L  6 211 ? 48.971  25.817  190.147 1.00 248.52 ?  190 GLN K NE2 1 
ATOM   22283 N N   . THR L  6 212 ? 50.055  26.959  185.196 1.00 239.54 ?  191 THR K N   1 
ATOM   22284 C CA  . THR L  6 212 ? 50.845  28.038  184.601 1.00 241.82 ?  191 THR K CA  1 
ATOM   22285 C C   . THR L  6 212 ? 51.926  28.574  185.540 1.00 241.61 ?  191 THR K C   1 
ATOM   22286 O O   . THR L  6 212 ? 51.620  29.201  186.561 1.00 241.84 ?  191 THR K O   1 
ATOM   22287 C CB  . THR L  6 212 ? 49.914  29.176  184.161 1.00 244.49 ?  191 THR K CB  1 
ATOM   22288 O OG1 . THR L  6 212 ? 48.786  28.626  183.472 1.00 244.45 ?  191 THR K OG1 1 
ATOM   22289 C CG2 . THR L  6 212 ? 50.628  30.113  183.204 1.00 246.91 ?  191 THR K CG2 1 
ATOM   22290 N N   . TYR L  6 213 ? 53.195  28.325  185.197 1.00 242.54 ?  192 TYR K N   1 
ATOM   22291 C CA  . TYR L  6 213 ? 54.357  28.827  185.936 1.00 242.45 ?  192 TYR K CA  1 
ATOM   22292 C C   . TYR L  6 213 ? 54.907  30.056  185.211 1.00 245.22 ?  192 TYR K C   1 
ATOM   22293 O O   . TYR L  6 213 ? 55.564  29.935  184.173 1.00 245.86 ?  192 TYR K O   1 
ATOM   22294 C CB  . TYR L  6 213 ? 55.405  27.724  186.058 1.00 240.12 ?  192 TYR K CB  1 
ATOM   22295 C CG  . TYR L  6 213 ? 54.933  26.550  186.892 1.00 237.35 ?  192 TYR K CG  1 
ATOM   22296 C CD1 . TYR L  6 213 ? 54.059  26.739  187.951 1.00 236.91 ?  192 TYR K CD1 1 
ATOM   22297 C CD2 . TYR L  6 213 ? 55.329  25.251  186.595 1.00 235.24 ?  192 TYR K CD2 1 
ATOM   22298 C CE1 . TYR L  6 213 ? 53.613  25.674  188.706 1.00 234.44 ?  192 TYR K CE1 1 
ATOM   22299 C CE2 . TYR L  6 213 ? 54.884  24.176  187.347 1.00 232.76 ?  192 TYR K CE2 1 
ATOM   22300 C CZ  . TYR L  6 213 ? 54.023  24.395  188.399 1.00 232.38 ?  192 TYR K CZ  1 
ATOM   22301 O OH  . TYR L  6 213 ? 53.578  23.334  189.154 1.00 229.95 ?  192 TYR K OH  1 
ATOM   22302 N N   . ILE L  6 214 ? 54.640  31.242  185.769 1.00 245.67 ?  193 ILE K N   1 
ATOM   22303 C CA  . ILE L  6 214 ? 55.087  32.521  185.210 1.00 248.43 ?  193 ILE K CA  1 
ATOM   22304 C C   . ILE L  6 214 ? 56.033  33.233  186.178 1.00 248.61 ?  193 ILE K C   1 
ATOM   22305 O O   . ILE L  6 214 ? 55.606  33.687  187.248 1.00 248.54 ?  193 ILE K O   1 
ATOM   22306 C CB  . ILE L  6 214 ? 53.887  33.425  184.885 1.00 250.66 ?  193 ILE K CB  1 
ATOM   22307 C CG1 . ILE L  6 214 ? 52.984  32.770  183.840 1.00 250.67 ?  193 ILE K CG1 1 
ATOM   22308 C CG2 . ILE L  6 214 ? 54.335  34.799  184.426 1.00 253.53 ?  193 ILE K CG2 1 
ATOM   22309 C CD1 . ILE L  6 214 ? 51.767  33.594  183.481 1.00 252.79 ?  193 ILE K CD1 1 
ATOM   22310 N N   . CYS L  6 215 ? 57.312  33.336  185.806 1.00 263.51 ?  194 CYS K N   1 
ATOM   22311 C CA  . CYS L  6 215 ? 58.302  34.047  186.613 1.00 264.30 ?  194 CYS K CA  1 
ATOM   22312 C C   . CYS L  6 215 ? 58.255  35.546  186.311 1.00 267.28 ?  194 CYS K C   1 
ATOM   22313 O O   . CYS L  6 215 ? 58.211  35.936  185.144 1.00 269.78 ?  194 CYS K O   1 
ATOM   22314 C CB  . CYS L  6 215 ? 59.714  33.479  186.350 1.00 265.29 ?  194 CYS K CB  1 
ATOM   22315 S SG  . CYS L  6 215 ? 60.364  33.562  184.610 1.00 268.12 ?  194 CYS K SG  1 
ATOM   22316 N N   . ASN L  6 216 ? 58.298  36.393  187.360 1.00 266.53 ?  195 ASN K N   1 
ATOM   22317 C CA  . ASN L  6 216 ? 58.252  37.853  187.199 1.00 269.55 ?  195 ASN K CA  1 
ATOM   22318 C C   . ASN L  6 216 ? 59.656  38.424  187.401 1.00 271.88 ?  195 ASN K C   1 
ATOM   22319 O O   . ASN L  6 216 ? 60.187  38.398  188.515 1.00 270.47 ?  195 ASN K O   1 
ATOM   22320 C CB  . ASN L  6 216 ? 57.269  38.520  188.170 1.00 268.28 ?  195 ASN K CB  1 
ATOM   22321 C CG  . ASN L  6 216 ? 55.848  37.997  188.040 1.00 266.26 ?  195 ASN K CG  1 
ATOM   22322 O OD1 . ASN L  6 216 ? 55.596  37.019  187.341 1.00 265.31 ?  195 ASN K OD1 1 
ATOM   22323 N ND2 . ASN L  6 216 ? 54.903  38.683  188.682 1.00 265.89 ?  195 ASN K ND2 1 
ATOM   22324 N N   . VAL L  6 217 ? 60.236  38.975  186.332 1.00 266.28 ?  196 VAL K N   1 
ATOM   22325 C CA  . VAL L  6 217 ? 61.580  39.557  186.335 1.00 269.37 ?  196 VAL K CA  1 
ATOM   22326 C C   . VAL L  6 217 ? 61.482  41.078  186.329 1.00 272.85 ?  196 VAL K C   1 
ATOM   22327 O O   . VAL L  6 217 ? 60.799  41.642  185.474 1.00 274.73 ?  196 VAL K O   1 
ATOM   22328 C CB  . VAL L  6 217 ? 62.385  39.064  185.117 1.00 272.03 ?  196 VAL K CB  1 
ATOM   22329 C CG1 . VAL L  6 217 ? 63.770  39.656  185.109 1.00 275.67 ?  196 VAL K CG1 1 
ATOM   22330 C CG2 . VAL L  6 217 ? 62.437  37.536  185.084 1.00 268.85 ?  196 VAL K CG2 1 
ATOM   22331 N N   . ASN L  6 218 ? 62.156  41.748  187.272 1.00 276.99 ?  197 ASN K N   1 
ATOM   22332 C CA  . ASN L  6 218 ? 62.132  43.207  187.353 1.00 280.53 ?  197 ASN K CA  1 
ATOM   22333 C C   . ASN L  6 218 ? 63.559  43.750  187.367 1.00 284.22 ?  197 ASN K C   1 
ATOM   22334 O O   . ASN L  6 218 ? 64.420  43.241  188.088 1.00 282.68 ?  197 ASN K O   1 
ATOM   22335 C CB  . ASN L  6 218 ? 61.349  43.705  188.590 1.00 278.01 ?  197 ASN K CB  1 
ATOM   22336 C CG  . ASN L  6 218 ? 61.392  45.233  188.762 1.00 281.63 ?  197 ASN K CG  1 
ATOM   22337 O OD1 . ASN L  6 218 ? 62.085  45.949  188.036 1.00 286.20 ?  197 ASN K OD1 1 
ATOM   22338 N ND2 . ASN L  6 218 ? 60.627  45.731  189.729 1.00 279.82 ?  197 ASN K ND2 1 
ATOM   22339 N N   . HIS L  6 219 ? 63.800  44.798  186.576 1.00 267.79 ?  198 HIS K N   1 
ATOM   22340 C CA  . HIS L  6 219 ? 65.102  45.466  186.502 1.00 272.22 ?  198 HIS K CA  1 
ATOM   22341 C C   . HIS L  6 219 ? 64.874  46.966  186.633 1.00 275.87 ?  198 HIS K C   1 
ATOM   22342 O O   . HIS L  6 219 ? 64.596  47.648  185.645 1.00 280.34 ?  198 HIS K O   1 
ATOM   22343 C CB  . HIS L  6 219 ? 65.789  45.124  185.179 1.00 276.03 ?  198 HIS K CB  1 
ATOM   22344 C CG  . HIS L  6 219 ? 67.228  45.536  185.092 1.00 280.50 ?  198 HIS K CG  1 
ATOM   22345 N ND1 . HIS L  6 219 ? 67.668  46.796  185.440 1.00 284.35 ?  198 HIS K ND1 1 
ATOM   22346 C CD2 . HIS L  6 219 ? 68.318  44.872  184.642 1.00 282.31 ?  198 HIS K CD2 1 
ATOM   22347 C CE1 . HIS L  6 219 ? 68.970  46.882  185.229 1.00 288.25 ?  198 HIS K CE1 1 
ATOM   22348 N NE2 . HIS L  6 219 ? 69.389  45.727  184.745 1.00 287.11 ?  198 HIS K NE2 1 
ATOM   22349 N N   . LYS L  6 220 ? 65.019  47.464  187.862 1.00 273.49 ?  199 LYS K N   1 
ATOM   22350 C CA  . LYS L  6 220 ? 64.772  48.878  188.141 1.00 276.49 ?  199 LYS K CA  1 
ATOM   22351 C C   . LYS L  6 220 ? 65.669  49.846  187.381 1.00 283.48 ?  199 LYS K C   1 
ATOM   22352 O O   . LYS L  6 220 ? 65.150  50.870  186.901 1.00 287.32 ?  199 LYS K O   1 
ATOM   22353 C CB  . LYS L  6 220 ? 64.840  49.144  189.647 1.00 273.67 ?  199 LYS K CB  1 
ATOM   22354 C CG  . LYS L  6 220 ? 63.864  48.321  190.450 1.00 267.56 ?  199 LYS K CG  1 
ATOM   22355 C CD  . LYS L  6 220 ? 64.048  48.611  191.918 1.00 265.36 ?  199 LYS K CD  1 
ATOM   22356 C CE  . LYS L  6 220 ? 63.127  47.776  192.767 1.00 260.11 ?  199 LYS K CE  1 
ATOM   22357 N NZ  . LYS L  6 220 ? 63.913  46.964  193.718 1.00 258.08 1  199 LYS K NZ  1 
ATOM   22358 N N   . PRO L  6 221 ? 66.980  49.618  187.238 1.00 267.76 ?  200 PRO K N   1 
ATOM   22359 C CA  . PRO L  6 221 ? 67.807  50.597  186.513 1.00 270.32 ?  200 PRO K CA  1 
ATOM   22360 C C   . PRO L  6 221 ? 67.380  50.770  185.069 1.00 272.10 ?  200 PRO K C   1 
ATOM   22361 O O   . PRO L  6 221 ? 67.709  51.795  184.459 1.00 274.74 ?  200 PRO K O   1 
ATOM   22362 C CB  . PRO L  6 221 ? 69.224  50.026  186.651 1.00 268.84 ?  200 PRO K CB  1 
ATOM   22363 C CG  . PRO L  6 221 ? 69.153  49.228  187.925 1.00 266.04 ?  200 PRO K CG  1 
ATOM   22364 C CD  . PRO L  6 221 ? 67.805  48.617  187.936 1.00 264.97 ?  200 PRO K CD  1 
ATOM   22365 N N   . SER L  6 222 ? 66.658  49.804  184.505 1.00 273.26 ?  201 SER K N   1 
ATOM   22366 C CA  . SER L  6 222 ? 66.145  49.926  183.156 1.00 274.88 ?  201 SER K CA  1 
ATOM   22367 C C   . SER L  6 222 ? 64.632  49.924  183.255 1.00 274.98 ?  201 SER K C   1 
ATOM   22368 O O   . SER L  6 222 ? 63.944  50.008  182.230 1.00 276.25 ?  201 SER K O   1 
ATOM   22369 C CB  . SER L  6 222 ? 66.570  48.736  182.280 1.00 273.28 ?  201 SER K CB  1 
ATOM   22370 O OG  . SER L  6 222 ? 67.960  48.647  182.074 1.00 273.12 ?  201 SER K OG  1 
ATOM   22371 N N   . ASN L  6 223 ? 64.119  49.848  184.492 1.00 295.84 ?  202 ASN K N   1 
ATOM   22372 C CA  . ASN L  6 223 ? 62.692  49.806  184.834 1.00 291.85 ?  202 ASN K CA  1 
ATOM   22373 C C   . ASN L  6 223 ? 61.988  48.718  184.028 1.00 289.05 ?  202 ASN K C   1 
ATOM   22374 O O   . ASN L  6 223 ? 60.782  48.790  183.802 1.00 286.91 ?  202 ASN K O   1 
ATOM   22375 C CB  . ASN L  6 223 ? 62.042  51.181  184.663 1.00 295.43 ?  202 ASN K CB  1 
ATOM   22376 C CG  . ASN L  6 223 ? 62.710  52.254  185.529 1.00 297.81 ?  202 ASN K CG  1 
ATOM   22377 O OD1 . ASN L  6 223 ? 62.393  52.421  186.712 1.00 294.39 ?  202 ASN K OD1 1 
ATOM   22378 N ND2 . ASN L  6 223 ? 63.672  52.956  184.943 1.00 303.76 ?  202 ASN K ND2 1 
ATOM   22379 N N   . THR L  6 224 ? 62.673  47.588  183.852 1.00 278.21 ?  203 THR K N   1 
ATOM   22380 C CA  . THR L  6 224 ? 62.228  46.487  182.998 1.00 278.13 ?  203 THR K CA  1 
ATOM   22381 C C   . THR L  6 224 ? 61.659  45.391  183.884 1.00 269.77 ?  203 THR K C   1 
ATOM   22382 O O   . THR L  6 224 ? 62.362  44.857  184.747 1.00 266.64 ?  203 THR K O   1 
ATOM   22383 C CB  . THR L  6 224 ? 63.373  45.964  182.124 1.00 286.11 ?  203 THR K CB  1 
ATOM   22384 O OG1 . THR L  6 224 ? 63.957  47.060  181.406 1.00 288.32 ?  203 THR K OG1 1 
ATOM   22385 C CG2 . THR L  6 224 ? 62.853  44.931  181.119 1.00 289.06 ?  203 THR K CG2 1 
ATOM   22386 N N   . LYS L  6 225 ? 60.385  45.059  183.650 1.00 272.65 ?  204 LYS K N   1 
ATOM   22387 C CA  . LYS L  6 225 ? 59.651  44.018  184.363 1.00 266.02 ?  204 LYS K CA  1 
ATOM   22388 C C   . LYS L  6 225 ? 59.173  42.942  183.392 1.00 267.23 ?  204 LYS K C   1 
ATOM   22389 O O   . LYS L  6 225 ? 58.172  43.153  182.701 1.00 264.98 ?  204 LYS K O   1 
ATOM   22390 C CB  . LYS L  6 225 ? 58.436  44.698  184.983 1.00 264.90 ?  204 LYS K CB  1 
ATOM   22391 C CG  . LYS L  6 225 ? 58.721  45.645  186.122 1.00 265.63 ?  204 LYS K CG  1 
ATOM   22392 C CD  . LYS L  6 225 ? 57.417  46.110  186.742 1.00 266.17 ?  204 LYS K CD  1 
ATOM   22393 C CE  . LYS L  6 225 ? 57.635  47.008  187.941 1.00 266.78 ?  204 LYS K CE  1 
ATOM   22394 N NZ  . LYS L  6 225 ? 56.320  47.381  188.524 1.00 267.20 1  204 LYS K NZ  1 
ATOM   22395 N N   . VAL L  6 226 ? 59.799  41.753  183.434 1.00 263.73 ?  205 VAL K N   1 
ATOM   22396 C CA  . VAL L  6 226 ? 59.496  40.650  182.504 1.00 262.57 ?  205 VAL K CA  1 
ATOM   22397 C C   . VAL L  6 226 ? 58.917  39.409  183.197 1.00 259.63 ?  205 VAL K C   1 
ATOM   22398 O O   . VAL L  6 226 ? 59.564  38.817  184.066 1.00 257.54 ?  205 VAL K O   1 
ATOM   22399 C CB  . VAL L  6 226 ? 60.752  40.243  181.709 1.00 262.36 ?  205 VAL K CB  1 
ATOM   22400 C CG1 . VAL L  6 226 ? 60.460  39.045  180.790 1.00 261.04 ?  205 VAL K CG1 1 
ATOM   22401 C CG2 . VAL L  6 226 ? 61.332  41.431  180.932 1.00 265.31 ?  205 VAL K CG2 1 
ATOM   22402 N N   . ASP L  6 227 ? 57.710  39.004  182.773 1.00 274.84 ?  206 ASP K N   1 
ATOM   22403 C CA  . ASP L  6 227 ? 57.004  37.802  183.219 1.00 270.97 ?  206 ASP K CA  1 
ATOM   22404 C C   . ASP L  6 227 ? 57.190  36.762  182.120 1.00 274.39 ?  206 ASP K C   1 
ATOM   22405 O O   . ASP L  6 227 ? 56.610  36.920  181.052 1.00 277.29 ?  206 ASP K O   1 
ATOM   22406 C CB  . ASP L  6 227 ? 55.530  38.072  183.495 1.00 264.87 ?  206 ASP K CB  1 
ATOM   22407 C CG  . ASP L  6 227 ? 55.318  39.101  184.586 1.00 260.53 ?  206 ASP K CG  1 
ATOM   22408 O OD1 . ASP L  6 227 ? 56.292  39.416  185.291 1.00 261.75 ?  206 ASP K OD1 1 
ATOM   22409 O OD2 . ASP L  6 227 ? 54.174  39.591  184.744 1.00 255.80 -1 206 ASP K OD2 1 
ATOM   22410 N N   . LYS L  6 228 ? 57.902  35.658  182.388 1.00 270.65 ?  207 LYS K N   1 
ATOM   22411 C CA  . LYS L  6 228 ? 58.191  34.637  181.370 1.00 272.20 ?  207 LYS K CA  1 
ATOM   22412 C C   . LYS L  6 228 ? 57.506  33.293  181.687 1.00 267.49 ?  207 LYS K C   1 
ATOM   22413 O O   . LYS L  6 228 ? 57.570  32.819  182.827 1.00 266.78 ?  207 LYS K O   1 
ATOM   22414 C CB  . LYS L  6 228 ? 59.717  34.487  181.336 1.00 273.78 ?  207 LYS K CB  1 
ATOM   22415 C CG  . LYS L  6 228 ? 60.377  33.712  180.229 1.00 274.54 ?  207 LYS K CG  1 
ATOM   22416 C CD  . LYS L  6 228 ? 60.043  34.466  178.966 1.00 280.21 ?  207 LYS K CD  1 
ATOM   22417 C CE  . LYS L  6 228 ? 61.078  34.263  177.890 1.00 281.24 ?  207 LYS K CE  1 
ATOM   22418 N NZ  . LYS L  6 228 ? 60.786  34.993  176.618 1.00 287.56 1  207 LYS K NZ  1 
ATOM   22419 N N   . ARG L  6 229 ? 56.859  32.672  180.679 1.00 267.85 ?  208 ARG K N   1 
ATOM   22420 C CA  . ARG L  6 229 ? 56.164  31.373  180.808 1.00 263.50 ?  208 ARG K CA  1 
ATOM   22421 C C   . ARG L  6 229 ? 56.959  30.194  180.245 1.00 260.52 ?  208 ARG K C   1 
ATOM   22422 O O   . ARG L  6 229 ? 57.405  30.232  179.093 1.00 262.03 ?  208 ARG K O   1 
ATOM   22423 C CB  . ARG L  6 229 ? 54.796  31.386  180.117 1.00 263.58 ?  208 ARG K CB  1 
ATOM   22424 C CG  . ARG L  6 229 ? 53.995  30.085  180.202 1.00 259.58 ?  208 ARG K CG  1 
ATOM   22425 C CD  . ARG L  6 229 ? 52.618  30.256  179.567 1.00 259.38 ?  208 ARG K CD  1 
ATOM   22426 N NE  . ARG L  6 229 ? 51.830  29.028  179.608 1.00 258.36 ?  208 ARG K NE  1 
ATOM   22427 C CZ  . ARG L  6 229 ? 50.581  28.929  179.165 1.00 261.53 ?  208 ARG K CZ  1 
ATOM   22428 N NH1 . ARG L  6 229 ? 49.936  27.772  179.242 1.00 261.29 1  208 ARG K NH1 1 
ATOM   22429 N NH2 . ARG L  6 229 ? 49.978  29.986  178.639 1.00 263.27 ?  208 ARG K NH2 1 
ATOM   22430 N N   . VAL L  6 230 ? 57.120  29.150  181.058 1.00 265.18 ?  209 VAL K N   1 
ATOM   22431 C CA  . VAL L  6 230 ? 57.868  27.937  180.710 1.00 259.85 ?  209 VAL K CA  1 
ATOM   22432 C C   . VAL L  6 230 ? 56.945  26.811  180.246 1.00 256.42 ?  209 VAL K C   1 
ATOM   22433 O O   . VAL L  6 230 ? 56.038  26.399  180.981 1.00 254.96 ?  209 VAL K O   1 
ATOM   22434 C CB  . VAL L  6 230 ? 58.721  27.452  181.891 1.00 255.14 ?  209 VAL K CB  1 
ATOM   22435 C CG1 . VAL L  6 230 ? 59.427  26.156  181.517 1.00 253.04 ?  209 VAL K CG1 1 
ATOM   22436 C CG2 . VAL L  6 230 ? 59.721  28.513  182.286 1.00 258.78 ?  209 VAL K CG2 1 
ATOM   22437 N N   . GLU L  6 231 ? 57.164  26.306  179.026 1.00 268.34 ?  210 GLU K N   1 
ATOM   22438 C CA  . GLU L  6 231 ? 56.366  25.207  178.486 1.00 264.20 ?  210 GLU K CA  1 
ATOM   22439 C C   . GLU L  6 231 ? 57.309  24.145  177.932 1.00 257.93 ?  210 GLU K C   1 
ATOM   22440 O O   . GLU L  6 231 ? 58.289  24.479  177.255 1.00 258.52 ?  210 GLU K O   1 
ATOM   22441 C CB  . GLU L  6 231 ? 55.404  25.670  177.379 1.00 268.22 ?  210 GLU K CB  1 
ATOM   22442 C CG  . GLU L  6 231 ? 54.366  26.689  177.823 1.00 273.58 ?  210 GLU K CG  1 
ATOM   22443 C CD  . GLU L  6 231 ? 53.535  27.215  176.666 1.00 276.97 ?  210 GLU K CD  1 
ATOM   22444 O OE1 . GLU L  6 231 ? 53.866  26.905  175.502 1.00 275.96 ?  210 GLU K OE1 1 
ATOM   22445 O OE2 . GLU L  6 231 ? 52.554  27.944  176.923 1.00 279.82 -1 210 GLU K OE2 1 
ATOM   22446 N N   . PRO L  6 232 ? 57.038  22.848  178.189 1.00 276.13 ?  211 PRO K N   1 
ATOM   22447 C CA  . PRO L  6 232 ? 57.882  21.752  177.686 1.00 270.25 ?  211 PRO K CA  1 
ATOM   22448 C C   . PRO L  6 232 ? 57.985  21.682  176.163 1.00 270.57 ?  211 PRO K C   1 
ATOM   22449 O O   . PRO L  6 232 ? 57.024  22.023  175.477 1.00 270.51 ?  211 PRO K O   1 
ATOM   22450 C CB  . PRO L  6 232 ? 57.197  20.496  178.242 1.00 264.49 ?  211 PRO K CB  1 
ATOM   22451 C CG  . PRO L  6 232 ? 56.442  20.972  179.433 1.00 262.78 ?  211 PRO K CG  1 
ATOM   22452 C CD  . PRO L  6 232 ? 55.972  22.353  179.076 1.00 270.85 ?  211 PRO K CD  1 
HETATM 22453 C C1  . NAG M  7 .   ? 12.967  33.297  153.774 1.00 170.72 ?  901 NAG A C1  1 
HETATM 22454 C C2  . NAG M  7 .   ? 13.369  32.299  152.680 1.00 163.62 ?  901 NAG A C2  1 
HETATM 22455 C C3  . NAG M  7 .   ? 14.130  33.012  151.561 1.00 173.46 ?  901 NAG A C3  1 
HETATM 22456 C C4  . NAG M  7 .   ? 13.358  34.226  151.062 1.00 171.75 ?  901 NAG A C4  1 
HETATM 22457 C C5  . NAG M  7 .   ? 12.975  35.128  152.231 1.00 179.16 ?  901 NAG A C5  1 
HETATM 22458 C C6  . NAG M  7 .   ? 12.093  36.283  151.814 1.00 179.96 ?  901 NAG A C6  1 
HETATM 22459 C C7  . NAG M  7 .   ? 13.633  30.076  153.693 1.00 167.33 ?  901 NAG A C7  1 
HETATM 22460 C C8  . NAG M  7 .   ? 14.607  29.059  154.205 1.00 165.15 ?  901 NAG A C8  1 
HETATM 22461 N N2  . NAG M  7 .   ? 14.164  31.209  153.221 1.00 166.02 ?  901 NAG A N2  1 
HETATM 22462 O O3  . NAG M  7 .   ? 14.345  32.102  150.487 1.00 185.21 ?  901 NAG A O3  1 
HETATM 22463 O O4  . NAG M  7 .   ? 14.186  34.973  150.177 1.00 183.64 ?  901 NAG A O4  1 
HETATM 22464 O O5  . NAG M  7 .   ? 12.225  34.373  153.193 1.00 181.70 ?  901 NAG A O5  1 
HETATM 22465 O O6  . NAG M  7 .   ? 10.720  35.915  151.825 1.00 173.12 ?  901 NAG A O6  1 
HETATM 22466 O O7  . NAG M  7 .   ? 12.421  29.883  153.709 1.00 173.78 ?  901 NAG A O7  1 
HETATM 22467 C C1  . NAG N  7 .   ? 13.742  34.797  148.818 1.00 176.66 ?  902 NAG A C1  1 
HETATM 22468 C C2  . NAG N  7 .   ? 14.344  35.924  147.956 1.00 177.92 ?  902 NAG A C2  1 
HETATM 22469 C C3  . NAG N  7 .   ? 13.955  35.759  146.484 1.00 184.58 ?  902 NAG A C3  1 
HETATM 22470 C C4  . NAG N  7 .   ? 14.277  34.352  146.001 1.00 189.69 ?  902 NAG A C4  1 
HETATM 22471 C C5  . NAG N  7 .   ? 13.662  33.311  146.931 1.00 187.35 ?  902 NAG A C5  1 
HETATM 22472 C C6  . NAG N  7 .   ? 14.040  31.897  146.549 1.00 199.46 ?  902 NAG A C6  1 
HETATM 22473 C C7  . NAG N  7 .   ? 12.883  37.902  148.607 1.00 175.03 ?  902 NAG A C7  1 
HETATM 22474 C C8  . NAG N  7 .   ? 11.633  37.155  148.218 1.00 171.66 ?  902 NAG A C8  1 
HETATM 22475 N N2  . NAG N  7 .   ? 14.069  37.273  148.455 1.00 177.43 ?  902 NAG A N2  1 
HETATM 22476 O O3  . NAG N  7 .   ? 14.653  36.718  145.697 1.00 190.38 ?  902 NAG A O3  1 
HETATM 22477 O O4  . NAG N  7 .   ? 13.652  34.161  144.739 1.00 195.58 ?  902 NAG A O4  1 
HETATM 22478 O O5  . NAG N  7 .   ? 14.124  33.515  148.274 1.00 173.70 ?  902 NAG A O5  1 
HETATM 22479 O O6  . NAG N  7 .   ? 13.228  30.932  147.204 1.00 203.97 ?  902 NAG A O6  1 
HETATM 22480 O O7  . NAG N  7 .   ? 12.827  39.047  149.047 1.00 183.13 ?  902 NAG A O7  1 
HETATM 22481 C C1  . BMA O  8 .   ? 14.591  34.198  143.668 1.00 197.48 ?  903 BMA A C1  1 
HETATM 22482 C C2  . BMA O  8 .   ? 13.964  33.340  142.576 1.00 198.98 ?  903 BMA A C2  1 
HETATM 22483 C C3  . BMA O  8 .   ? 14.806  33.410  141.320 1.00 194.98 ?  903 BMA A C3  1 
HETATM 22484 C C4  . BMA O  8 .   ? 15.084  34.865  140.916 1.00 202.42 ?  903 BMA A C4  1 
HETATM 22485 C C5  . BMA O  8 .   ? 15.710  35.607  142.128 1.00 211.88 ?  903 BMA A C5  1 
HETATM 22486 C C6  . BMA O  8 .   ? 16.044  37.061  141.857 1.00 224.91 ?  903 BMA A C6  1 
HETATM 22487 O O2  . BMA O  8 .   ? 12.682  33.822  142.238 1.00 208.81 ?  903 BMA A O2  1 
HETATM 22488 O O3  . BMA O  8 .   ? 14.166  32.690  140.281 1.00 192.37 ?  903 BMA A O3  1 
HETATM 22489 O O4  . BMA O  8 .   ? 15.964  34.933  139.813 1.00 204.35 ?  903 BMA A O4  1 
HETATM 22490 O O5  . BMA O  8 .   ? 14.795  35.526  143.224 1.00 203.94 ?  903 BMA A O5  1 
HETATM 22491 O O6  . BMA O  8 .   ? 16.203  37.123  140.457 1.00 227.83 ?  903 BMA A O6  1 
HETATM 22492 C C1  . MAN P  9 .   ? 14.964  31.611  139.785 1.00 207.32 ?  904 MAN A C1  1 
HETATM 22493 C C2  . MAN P  9 .   ? 14.834  31.708  138.254 1.00 226.94 ?  904 MAN A C2  1 
HETATM 22494 C C3  . MAN P  9 .   ? 13.462  31.219  137.788 1.00 223.82 ?  904 MAN A C3  1 
HETATM 22495 C C4  . MAN P  9 .   ? 13.110  29.871  138.417 1.00 212.03 ?  904 MAN A C4  1 
HETATM 22496 C C5  . MAN P  9 .   ? 13.150  30.004  139.934 1.00 213.16 ?  904 MAN A C5  1 
HETATM 22497 C C6  . MAN P  9 .   ? 12.809  28.708  140.653 1.00 230.25 ?  904 MAN A C6  1 
HETATM 22498 O O2  . MAN P  9 .   ? 15.782  30.880  137.605 1.00 223.46 ?  904 MAN A O2  1 
HETATM 22499 O O3  . MAN P  9 .   ? 13.384  31.128  136.366 1.00 231.42 ?  904 MAN A O3  1 
HETATM 22500 O O4  . MAN P  9 .   ? 11.816  29.479  138.017 1.00 216.45 ?  904 MAN A O4  1 
HETATM 22501 O O5  . MAN P  9 .   ? 14.495  30.391  140.325 1.00 208.36 ?  904 MAN A O5  1 
HETATM 22502 O O6  . MAN P  9 .   ? 12.618  28.997  142.038 1.00 247.11 ?  904 MAN A O6  1 
HETATM 22503 C C1  . MAN Q  9 .   ? 15.669  38.291  139.819 1.00 227.54 ?  905 MAN A C1  1 
HETATM 22504 C C2  . MAN Q  9 .   ? 16.514  38.427  138.558 1.00 234.37 ?  905 MAN A C2  1 
HETATM 22505 C C3  . MAN Q  9 .   ? 16.232  39.769  137.881 1.00 230.35 ?  905 MAN A C3  1 
HETATM 22506 C C4  . MAN Q  9 .   ? 15.167  40.530  138.675 1.00 227.32 ?  905 MAN A C4  1 
HETATM 22507 C C5  . MAN Q  9 .   ? 15.686  40.706  140.058 1.00 228.99 ?  905 MAN A C5  1 
HETATM 22508 C C6  . MAN Q  9 .   ? 14.787  41.476  140.940 1.00 225.10 ?  905 MAN A C6  1 
HETATM 22509 O O2  . MAN Q  9 .   ? 16.111  37.427  137.615 1.00 235.53 ?  905 MAN A O2  1 
HETATM 22510 O O3  . MAN Q  9 .   ? 15.804  39.597  136.561 1.00 233.69 ?  905 MAN A O3  1 
HETATM 22511 O O4  . MAN Q  9 .   ? 14.943  41.799  138.089 1.00 225.15 ?  905 MAN A O4  1 
HETATM 22512 O O5  . MAN Q  9 .   ? 15.765  39.422  140.666 1.00 232.22 ?  905 MAN A O5  1 
HETATM 22513 O O6  . MAN Q  9 .   ? 13.474  40.980  140.779 1.00 221.36 ?  905 MAN A O6  1 
HETATM 22514 C C1  . MAN R  9 .   ? 12.742  41.937  141.590 1.00 221.75 ?  906 MAN A C1  1 
HETATM 22515 C C2  . MAN R  9 .   ? 11.932  41.177  142.692 1.00 219.37 ?  906 MAN A C2  1 
HETATM 22516 C C3  . MAN R  9 .   ? 10.640  41.993  143.166 1.00 226.58 ?  906 MAN A C3  1 
HETATM 22517 C C4  . MAN R  9 .   ? 10.889  43.585  143.140 1.00 234.01 ?  906 MAN A C4  1 
HETATM 22518 C C5  . MAN R  9 .   ? 11.132  43.839  141.538 1.00 232.42 ?  906 MAN A C5  1 
HETATM 22519 C C6  . MAN R  9 .   ? 11.472  45.258  141.038 1.00 237.19 ?  906 MAN A C6  1 
HETATM 22520 O O2  . MAN R  9 .   ? 12.722  40.781  143.961 1.00 219.01 ?  906 MAN A O2  1 
HETATM 22521 O O3  . MAN R  9 .   ? 9.781   41.544  144.325 1.00 227.58 ?  906 MAN A O3  1 
HETATM 22522 O O4  . MAN R  9 .   ? 9.823   44.302  143.511 1.00 243.04 ?  906 MAN A O4  1 
HETATM 22523 O O5  . MAN R  9 .   ? 11.890  42.682  140.786 1.00 225.98 ?  906 MAN A O5  1 
HETATM 22524 O O6  . MAN R  9 .   ? 11.137  45.311  139.640 1.00 240.03 ?  906 MAN A O6  1 
HETATM 22525 C C1  . MAN S  9 .   ? 16.882  39.615  135.597 1.00 202.76 ?  907 MAN A C1  1 
HETATM 22526 C C2  . MAN S  9 .   ? 17.576  40.998  135.636 1.00 200.96 ?  907 MAN A C2  1 
HETATM 22527 C C3  . MAN S  9 .   ? 16.607  42.079  135.157 1.00 209.98 ?  907 MAN A C3  1 
HETATM 22528 C C4  . MAN S  9 .   ? 15.953  41.672  133.835 1.00 218.64 ?  907 MAN A C4  1 
HETATM 22529 C C5  . MAN S  9 .   ? 15.272  40.292  134.018 1.00 212.16 ?  907 MAN A C5  1 
HETATM 22530 C C6  . MAN S  9 .   ? 14.630  39.768  132.769 1.00 209.81 ?  907 MAN A C6  1 
HETATM 22531 O O2  . MAN S  9 .   ? 18.712  41.078  134.726 1.00 189.77 ?  907 MAN A O2  1 
HETATM 22532 O O3  . MAN S  9 .   ? 17.235  43.335  135.025 1.00 207.56 ?  907 MAN A O3  1 
HETATM 22533 O O4  . MAN S  9 .   ? 14.981  42.639  133.448 1.00 228.41 ?  907 MAN A O4  1 
HETATM 22534 O O5  . MAN S  9 .   ? 16.253  39.329  134.405 1.00 208.28 ?  907 MAN A O5  1 
HETATM 22535 O O6  . MAN S  9 .   ? 13.857  38.624  133.110 1.00 212.61 ?  907 MAN A O6  1 
HETATM 22536 C C1  . NAG T  7 .   ? 16.705  27.461  228.194 1.00 217.91 ?  908 NAG A C1  1 
HETATM 22537 C C2  . NAG T  7 .   ? 16.254  27.710  229.628 1.00 229.86 ?  908 NAG A C2  1 
HETATM 22538 C C3  . NAG T  7 .   ? 15.325  28.920  229.694 1.00 234.14 ?  908 NAG A C3  1 
HETATM 22539 C C4  . NAG T  7 .   ? 15.979  30.130  229.040 1.00 235.25 ?  908 NAG A C4  1 
HETATM 22540 C C5  . NAG T  7 .   ? 16.429  29.779  227.625 1.00 239.53 ?  908 NAG A C5  1 
HETATM 22541 C C6  . NAG T  7 .   ? 17.187  30.899  226.951 1.00 248.23 ?  908 NAG A C6  1 
HETATM 22542 C C7  . NAG T  7 .   ? 16.313  25.500  230.680 1.00 231.88 ?  908 NAG A C7  1 
HETATM 22543 C C8  . NAG T  7 .   ? 15.508  24.361  231.222 1.00 226.96 ?  908 NAG A C8  1 
HETATM 22544 N N2  . NAG T  7 .   ? 15.616  26.531  230.189 1.00 235.05 ?  908 NAG A N2  1 
HETATM 22545 O O3  . NAG T  7 .   ? 15.020  29.211  231.053 1.00 239.53 ?  908 NAG A O3  1 
HETATM 22546 O O4  . NAG T  7 .   ? 15.058  31.214  228.992 1.00 239.02 ?  908 NAG A O4  1 
HETATM 22547 O O5  . NAG T  7 .   ? 17.316  28.653  227.670 1.00 231.26 ?  908 NAG A O5  1 
HETATM 22548 O O6  . NAG T  7 .   ? 16.552  32.153  227.160 1.00 253.16 ?  908 NAG A O6  1 
HETATM 22549 O O7  . NAG T  7 .   ? 17.541  25.488  230.677 1.00 232.35 ?  908 NAG A O7  1 
HETATM 22550 C C1  . NAG U  7 .   ? 21.656  15.716  226.664 1.00 179.16 ?  909 NAG A C1  1 
HETATM 22551 C C2  . NAG U  7 .   ? 23.177  15.843  226.661 1.00 181.60 ?  909 NAG A C2  1 
HETATM 22552 C C3  . NAG U  7 .   ? 23.816  14.477  226.891 1.00 199.26 ?  909 NAG A C3  1 
HETATM 22553 C C4  . NAG U  7 .   ? 23.253  13.817  228.145 1.00 207.03 ?  909 NAG A C4  1 
HETATM 22554 C C5  . NAG U  7 .   ? 21.722  13.810  228.118 1.00 209.37 ?  909 NAG A C5  1 
HETATM 22555 C C6  . NAG U  7 .   ? 21.100  13.317  229.407 1.00 216.42 ?  909 NAG A C6  1 
HETATM 22556 C C7  . NAG U  7 .   ? 23.616  17.736  225.157 1.00 168.32 ?  909 NAG A C7  1 
HETATM 22557 C C8  . NAG U  7 .   ? 24.151  18.158  223.823 1.00 154.56 ?  909 NAG A C8  1 
HETATM 22558 N N2  . NAG U  7 .   ? 23.654  16.425  225.416 1.00 168.75 ?  909 NAG A N2  1 
HETATM 22559 O O3  . NAG U  7 .   ? 25.226  14.639  227.002 1.00 206.31 ?  909 NAG A O3  1 
HETATM 22560 O O4  . NAG U  7 .   ? 23.726  12.476  228.223 1.00 214.69 ?  909 NAG A O4  1 
HETATM 22561 O O5  . NAG U  7 .   ? 21.226  15.140  227.903 1.00 199.39 ?  909 NAG A O5  1 
HETATM 22562 O O6  . NAG U  7 .   ? 19.974  12.483  229.171 1.00 219.72 ?  909 NAG A O6  1 
HETATM 22563 O O7  . NAG U  7 .   ? 23.161  18.544  225.960 1.00 191.72 ?  909 NAG A O7  1 
HETATM 22564 C C1  . NAG V  7 .   ? 24.478  12.309  229.448 1.00 226.05 ?  910 NAG A C1  1 
HETATM 22565 C C2  . NAG V  7 .   ? 24.683  10.815  229.701 1.00 231.37 ?  910 NAG A C2  1 
HETATM 22566 C C3  . NAG V  7 .   ? 25.485  10.607  230.982 1.00 241.02 ?  910 NAG A C3  1 
HETATM 22567 C C4  . NAG V  7 .   ? 26.780  11.411  230.940 1.00 244.29 ?  910 NAG A C4  1 
HETATM 22568 C C5  . NAG V  7 .   ? 26.496  12.875  230.604 1.00 233.77 ?  910 NAG A C5  1 
HETATM 22569 C C6  . NAG V  7 .   ? 27.757  13.686  230.400 1.00 225.57 ?  910 NAG A C6  1 
HETATM 22570 C C7  . NAG V  7 .   ? 22.932  9.380   228.760 1.00 234.66 ?  910 NAG A C7  1 
HETATM 22571 C C8  . NAG V  7 .   ? 21.606  8.723   228.998 1.00 237.87 ?  910 NAG A C8  1 
HETATM 22572 N N2  . NAG V  7 .   ? 23.412  10.113  229.770 1.00 229.32 ?  910 NAG A N2  1 
HETATM 22573 O O3  . NAG V  7 .   ? 25.774  9.222   231.135 1.00 244.60 ?  910 NAG A O3  1 
HETATM 22574 O O4  . NAG V  7 .   ? 27.417  11.349  232.212 1.00 254.40 ?  910 NAG A O4  1 
HETATM 22575 O O5  . NAG V  7 .   ? 25.754  12.962  229.378 1.00 229.79 ?  910 NAG A O5  1 
HETATM 22576 O O6  . NAG V  7 .   ? 27.707  14.931  231.083 1.00 219.58 ?  910 NAG A O6  1 
HETATM 22577 O O7  . NAG V  7 .   ? 23.541  9.253   227.702 1.00 236.35 ?  910 NAG A O7  1 
HETATM 22578 C C1  . BMA W  8 .   ? 28.669  10.647  232.074 1.00 263.35 ?  911 BMA A C1  1 
HETATM 22579 C C2  . BMA W  8 .   ? 29.642  11.192  233.153 1.00 267.89 ?  911 BMA A C2  1 
HETATM 22580 C C3  . BMA W  8 .   ? 30.923  10.358  233.183 1.00 263.88 ?  911 BMA A C3  1 
HETATM 22581 C C4  . BMA W  8 .   ? 30.606  8.846   233.223 1.00 266.11 ?  911 BMA A C4  1 
HETATM 22582 C C5  . BMA W  8 .   ? 29.655  8.468   232.067 1.00 265.98 ?  911 BMA A C5  1 
HETATM 22583 C C6  . BMA W  8 .   ? 29.249  6.997   232.062 1.00 276.51 ?  911 BMA A C6  1 
HETATM 22584 O O2  . BMA W  8 .   ? 29.069  11.105  234.447 1.00 268.72 ?  911 BMA A O2  1 
HETATM 22585 O O3  . BMA W  8 .   ? 31.755  10.722  234.288 1.00 256.64 ?  911 BMA A O3  1 
HETATM 22586 O O4  . BMA W  8 .   ? 31.805  8.101   233.110 1.00 270.35 ?  911 BMA A O4  1 
HETATM 22587 O O5  . BMA W  8 .   ? 28.464  9.244   232.197 1.00 260.89 ?  911 BMA A O5  1 
HETATM 22588 O O6  . BMA W  8 .   ? 29.983  6.292   233.045 1.00 285.95 ?  911 BMA A O6  1 
HETATM 22589 C C1  . MAN X  9 .   ? 32.688  11.725  233.817 1.00 253.11 ?  912 MAN A C1  1 
HETATM 22590 C C2  . MAN X  9 .   ? 34.061  11.503  234.530 1.00 254.65 ?  912 MAN A C2  1 
HETATM 22591 C C3  . MAN X  9 .   ? 34.007  11.982  235.982 1.00 253.92 ?  912 MAN A C3  1 
HETATM 22592 C C4  . MAN X  9 .   ? 33.409  13.396  236.080 1.00 254.91 ?  912 MAN A C4  1 
HETATM 22593 C C5  . MAN X  9 .   ? 32.028  13.425  235.421 1.00 250.78 ?  912 MAN A C5  1 
HETATM 22594 C C6  . MAN X  9 .   ? 31.381  14.798  235.457 1.00 244.47 ?  912 MAN A C6  1 
HETATM 22595 O O2  . MAN X  9 .   ? 35.101  12.257  233.906 1.00 259.32 ?  912 MAN A O2  1 
HETATM 22596 O O3  . MAN X  9 .   ? 35.290  11.953  236.590 1.00 257.15 ?  912 MAN A O3  1 
HETATM 22597 O O4  . MAN X  9 .   ? 33.288  13.780  237.436 1.00 257.01 ?  912 MAN A O4  1 
HETATM 22598 O O5  . MAN X  9 .   ? 32.171  13.041  234.040 1.00 252.90 ?  912 MAN A O5  1 
HETATM 22599 O O6  . MAN X  9 .   ? 31.273  15.207  236.818 1.00 241.16 ?  912 MAN A O6  1 
HETATM 22600 C C1  . MAN Y  9 .   ? 30.538  5.124   232.405 1.00 294.42 ?  913 MAN A C1  1 
HETATM 22601 C C2  . MAN Y  9 .   ? 29.444  4.011   232.422 1.00 294.79 ?  913 MAN A C2  1 
HETATM 22602 C C3  . MAN Y  9 .   ? 29.293  3.410   233.820 1.00 291.56 ?  913 MAN A C3  1 
HETATM 22603 C C4  . MAN Y  9 .   ? 30.656  3.043   234.413 1.00 292.05 ?  913 MAN A C4  1 
HETATM 22604 C C5  . MAN Y  9 .   ? 31.562  4.282   234.420 1.00 292.20 ?  913 MAN A C5  1 
HETATM 22605 C C6  . MAN Y  9 .   ? 32.941  4.004   234.977 1.00 290.56 ?  913 MAN A C6  1 
HETATM 22606 O O2  . MAN Y  9 .   ? 29.796  2.920   231.569 1.00 297.87 ?  913 MAN A O2  1 
HETATM 22607 O O3  . MAN Y  9 .   ? 28.440  2.270   233.814 1.00 290.26 ?  913 MAN A O3  1 
HETATM 22608 O O4  . MAN Y  9 .   ? 30.495  2.569   235.739 1.00 290.67 ?  913 MAN A O4  1 
HETATM 22609 O O5  . MAN Y  9 .   ? 31.730  4.736   233.068 1.00 294.21 ?  913 MAN A O5  1 
HETATM 22610 O O6  . MAN Y  9 .   ? 33.584  5.253   235.211 1.00 288.59 ?  913 MAN A O6  1 
HETATM 22611 C C1  . NAG Z  7 .   ? 9.050   6.867   230.270 1.00 180.35 ?  914 NAG A C1  1 
HETATM 22612 C C2  . NAG Z  7 .   ? 8.805   8.196   230.982 1.00 192.35 ?  914 NAG A C2  1 
HETATM 22613 C C3  . NAG Z  7 .   ? 8.953   8.030   232.491 1.00 203.61 ?  914 NAG A C3  1 
HETATM 22614 C C4  . NAG Z  7 .   ? 8.083   6.886   232.990 1.00 211.50 ?  914 NAG A C4  1 
HETATM 22615 C C5  . NAG Z  7 .   ? 8.390   5.617   232.202 1.00 207.22 ?  914 NAG A C5  1 
HETATM 22616 C C6  . NAG Z  7 .   ? 7.478   4.467   232.560 1.00 211.40 ?  914 NAG A C6  1 
HETATM 22617 C C7  . NAG Z  7 .   ? 9.311   10.200  229.657 1.00 196.98 ?  914 NAG A C7  1 
HETATM 22618 C C8  . NAG Z  7 .   ? 7.865   10.185  229.257 1.00 207.30 ?  914 NAG A C8  1 
HETATM 22619 N N2  . NAG Z  7 .   ? 9.702   9.226   230.486 1.00 193.36 ?  914 NAG A N2  1 
HETATM 22620 O O3  . NAG Z  7 .   ? 8.591   9.242   233.144 1.00 207.60 ?  914 NAG A O3  1 
HETATM 22621 O O4  . NAG Z  7 .   ? 8.336   6.664   234.372 1.00 224.64 ?  914 NAG A O4  1 
HETATM 22622 O O5  . NAG Z  7 .   ? 8.187   5.868   230.806 1.00 196.63 ?  914 NAG A O5  1 
HETATM 22623 O O6  . NAG Z  7 .   ? 8.184   3.236   232.612 1.00 213.14 ?  914 NAG A O6  1 
HETATM 22624 O O7  . NAG Z  7 .   ? 10.088  11.057  229.252 1.00 186.46 ?  914 NAG A O7  1 
HETATM 22625 C C1  . NAG AA 7 .   ? 7.105   6.897   235.083 1.00 248.53 ?  915 NAG A C1  1 
HETATM 22626 C C2  . NAG AA 7 .   ? 7.286   6.448   236.545 1.00 236.19 ?  915 NAG A C2  1 
HETATM 22627 C C3  . NAG AA 7 .   ? 6.036   6.756   237.381 1.00 236.99 ?  915 NAG A C3  1 
HETATM 22628 C C4  . NAG AA 7 .   ? 5.620   8.211   237.202 1.00 239.10 ?  915 NAG A C4  1 
HETATM 22629 C C5  . NAG AA 7 .   ? 5.485   8.546   235.718 1.00 243.65 ?  915 NAG A C5  1 
HETATM 22630 C C6  . NAG AA 7 .   ? 5.150   9.997   235.458 1.00 234.72 ?  915 NAG A C6  1 
HETATM 22631 C C7  . NAG AA 7 .   ? 7.087   3.922   236.303 1.00 227.06 ?  915 NAG A C7  1 
HETATM 22632 C C8  . NAG AA 7 .   ? 5.728   4.051   235.663 1.00 224.27 ?  915 NAG A C8  1 
HETATM 22633 N N2  . NAG AA 7 .   ? 7.719   5.056   236.683 1.00 229.23 ?  915 NAG A N2  1 
HETATM 22634 O O3  . NAG AA 7 .   ? 6.307   6.499   238.754 1.00 238.40 ?  915 NAG A O3  1 
HETATM 22635 O O4  . NAG AA 7 .   ? 4.377   8.445   237.856 1.00 242.19 ?  915 NAG A O4  1 
HETATM 22636 O O5  . NAG AA 7 .   ? 6.724   8.280   235.045 1.00 255.60 ?  915 NAG A O5  1 
HETATM 22637 O O6  . NAG AA 7 .   ? 5.443   10.367  234.117 1.00 229.44 ?  915 NAG A O6  1 
HETATM 22638 O O7  . NAG AA 7 .   ? 7.600   2.821   236.484 1.00 230.57 ?  915 NAG A O7  1 
HETATM 22639 C C1  . NAG BA 7 .   ? -1.031  22.474  215.504 1.00 167.16 ?  916 NAG A C1  1 
HETATM 22640 C C2  . NAG BA 7 .   ? -2.224  23.413  215.355 1.00 182.56 ?  916 NAG A C2  1 
HETATM 22641 C C3  . NAG BA 7 .   ? -1.765  24.772  214.836 1.00 204.88 ?  916 NAG A C3  1 
HETATM 22642 C C4  . NAG BA 7 .   ? -0.659  25.329  215.722 1.00 218.47 ?  916 NAG A C4  1 
HETATM 22643 C C5  . NAG BA 7 .   ? 0.467   24.307  215.872 1.00 211.57 ?  916 NAG A C5  1 
HETATM 22644 C C6  . NAG BA 7 .   ? 1.534   24.745  216.849 1.00 208.60 ?  916 NAG A C6  1 
HETATM 22645 C C7  . NAG BA 7 .   ? -4.419  22.406  214.942 1.00 192.52 ?  916 NAG A C7  1 
HETATM 22646 C C8  . NAG BA 7 .   ? -4.645  22.533  216.420 1.00 196.55 ?  916 NAG A C8  1 
HETATM 22647 N N2  . NAG BA 7 .   ? -3.240  22.844  214.488 1.00 185.82 ?  916 NAG A N2  1 
HETATM 22648 O O3  . NAG BA 7 .   ? -2.870  25.668  214.791 1.00 213.53 ?  916 NAG A O3  1 
HETATM 22649 O O4  . NAG BA 7 .   ? -0.139  26.524  215.150 1.00 233.65 ?  916 NAG A O4  1 
HETATM 22650 O O5  . NAG BA 7 .   ? -0.060  23.068  216.370 1.00 197.01 ?  916 NAG A O5  1 
HETATM 22651 O O6  . NAG BA 7 .   ? 1.052   24.737  218.186 1.00 204.00 ?  916 NAG A O6  1 
HETATM 22652 O O7  . NAG BA 7 .   ? -5.266  21.928  214.194 1.00 198.16 ?  916 NAG A O7  1 
HETATM 22653 C C1  . NAG CA 7 .   ? -0.633  27.645  215.911 1.00 244.51 ?  917 NAG A C1  1 
HETATM 22654 C C2  . NAG CA 7 .   ? 0.478   28.689  216.056 1.00 248.76 ?  917 NAG A C2  1 
HETATM 22655 C C3  . NAG CA 7 .   ? -0.042  29.907  216.817 1.00 256.84 ?  917 NAG A C3  1 
HETATM 22656 C C4  . NAG CA 7 .   ? -1.308  30.446  216.162 1.00 263.32 ?  917 NAG A C4  1 
HETATM 22657 C C5  . NAG CA 7 .   ? -2.344  29.335  216.014 1.00 259.85 ?  917 NAG A C5  1 
HETATM 22658 C C6  . NAG CA 7 .   ? -3.582  29.776  215.266 1.00 263.42 ?  917 NAG A C6  1 
HETATM 22659 C C7  . NAG CA 7 .   ? 2.867   28.102  216.173 1.00 240.68 ?  917 NAG A C7  1 
HETATM 22660 C C8  . NAG CA 7 .   ? 3.950   27.484  217.007 1.00 242.33 ?  917 NAG A C8  1 
HETATM 22661 N N2  . NAG CA 7 .   ? 1.646   28.127  216.721 1.00 244.56 ?  917 NAG A N2  1 
HETATM 22662 O O3  . NAG CA 7 .   ? 0.960   30.918  216.839 1.00 255.78 ?  917 NAG A O3  1 
HETATM 22663 O O4  . NAG CA 7 .   ? -1.859  31.499  216.947 1.00 269.14 ?  917 NAG A O4  1 
HETATM 22664 O O5  . NAG CA 7 .   ? -1.779  28.243  215.272 1.00 250.80 ?  917 NAG A O5  1 
HETATM 22665 O O6  . NAG CA 7 .   ? -4.485  30.477  216.110 1.00 266.63 ?  917 NAG A O6  1 
HETATM 22666 O O7  . NAG CA 7 .   ? 3.088   28.557  215.054 1.00 235.84 ?  917 NAG A O7  1 
HETATM 22667 C C1  . NAG DA 7 .   ? 6.581   41.610  176.086 1.00 193.97 ?  918 NAG A C1  1 
HETATM 22668 C C2  . NAG DA 7 .   ? 5.480   42.491  176.675 1.00 207.56 ?  918 NAG A C2  1 
HETATM 22669 C C3  . NAG DA 7 .   ? 4.462   42.850  175.598 1.00 208.34 ?  918 NAG A C3  1 
HETATM 22670 C C4  . NAG DA 7 .   ? 5.162   43.478  174.400 1.00 215.74 ?  918 NAG A C4  1 
HETATM 22671 C C5  . NAG DA 7 .   ? 6.278   42.559  173.903 1.00 205.39 ?  918 NAG A C5  1 
HETATM 22672 C C6  . NAG DA 7 .   ? 7.095   43.156  172.780 1.00 213.97 ?  918 NAG A C6  1 
HETATM 22673 C C7  . NAG DA 7 .   ? 4.934   42.257  179.056 1.00 212.39 ?  918 NAG A C7  1 
HETATM 22674 C C8  . NAG DA 7 .   ? 4.193   41.456  180.083 1.00 208.88 ?  918 NAG A C8  1 
HETATM 22675 N N2  . NAG DA 7 .   ? 4.827   41.831  177.794 1.00 211.78 ?  918 NAG A N2  1 
HETATM 22676 O O3  . NAG DA 7 .   ? 3.502   43.747  176.146 1.00 213.80 ?  918 NAG A O3  1 
HETATM 22677 O O4  . NAG DA 7 .   ? 4.230   43.726  173.353 1.00 236.39 ?  918 NAG A O4  1 
HETATM 22678 O O5  . NAG DA 7 .   ? 7.191   42.279  174.976 1.00 199.53 ?  918 NAG A O5  1 
HETATM 22679 O O6  . NAG DA 7 .   ? 7.463   42.170  171.824 1.00 222.59 ?  918 NAG A O6  1 
HETATM 22680 O O7  . NAG DA 7 .   ? 5.598   43.244  179.356 1.00 212.67 ?  918 NAG A O7  1 
HETATM 22681 C C1  . NAG EA 7 .   ? 4.095   45.157  173.195 1.00 242.88 ?  919 NAG A C1  1 
HETATM 22682 C C2  . NAG EA 7 .   ? 3.128   45.438  172.043 1.00 245.48 ?  919 NAG A C2  1 
HETATM 22683 C C3  . NAG EA 7 .   ? 2.936   46.943  171.872 1.00 249.25 ?  919 NAG A C3  1 
HETATM 22684 C C4  . NAG EA 7 .   ? 2.524   47.583  173.193 1.00 249.64 ?  919 NAG A C4  1 
HETATM 22685 C C5  . NAG EA 7 .   ? 3.513   47.211  174.296 1.00 246.99 ?  919 NAG A C5  1 
HETATM 22686 C C6  . NAG EA 7 .   ? 3.106   47.720  175.662 1.00 246.89 ?  919 NAG A C6  1 
HETATM 22687 C C7  . NAG EA 7 .   ? 3.089   43.715  170.294 1.00 241.72 ?  919 NAG A C7  1 
HETATM 22688 C C8  . NAG EA 7 .   ? 3.704   43.235  169.015 1.00 241.55 ?  919 NAG A C8  1 
HETATM 22689 N N2  . NAG EA 7 .   ? 3.603   44.838  170.806 1.00 242.02 ?  919 NAG A N2  1 
HETATM 22690 O O3  . NAG EA 7 .   ? 1.941   47.174  170.881 1.00 251.21 ?  919 NAG A O3  1 
HETATM 22691 O O4  . NAG EA 7 .   ? 2.482   48.999  173.052 1.00 252.03 ?  919 NAG A O4  1 
HETATM 22692 O O5  . NAG EA 7 .   ? 3.609   45.782  174.398 1.00 248.39 ?  919 NAG A O5  1 
HETATM 22693 O O6  . NAG EA 7 .   ? 3.832   47.085  176.706 1.00 247.54 ?  919 NAG A O6  1 
HETATM 22694 O O7  . NAG EA 7 .   ? 2.167   43.115  170.839 1.00 241.07 ?  919 NAG A O7  1 
HETATM 22695 C C1  . NAG FA 7 .   ? 24.101  23.984  193.330 1.00 141.08 ?  920 NAG A C1  1 
HETATM 22696 C C2  . NAG FA 7 .   ? 23.857  23.204  194.611 1.00 134.39 ?  920 NAG A C2  1 
HETATM 22697 C C3  . NAG FA 7 .   ? 25.160  22.997  195.368 1.00 144.65 ?  920 NAG A C3  1 
HETATM 22698 C C4  . NAG FA 7 .   ? 26.198  22.361  194.455 1.00 158.05 ?  920 NAG A C4  1 
HETATM 22699 C C5  . NAG FA 7 .   ? 26.366  23.207  193.200 1.00 160.83 ?  920 NAG A C5  1 
HETATM 22700 C C6  . NAG FA 7 .   ? 27.311  22.595  192.196 1.00 170.59 ?  920 NAG A C6  1 
HETATM 22701 C C7  . NAG FA 7 .   ? 21.629  23.443  195.584 1.00 152.90 ?  920 NAG A C7  1 
HETATM 22702 C C8  . NAG FA 7 .   ? 20.744  24.260  196.473 1.00 144.47 ?  920 NAG A C8  1 
HETATM 22703 N N2  . NAG FA 7 .   ? 22.881  23.881  195.445 1.00 145.53 ?  920 NAG A N2  1 
HETATM 22704 O O3  . NAG FA 7 .   ? 24.905  22.182  196.506 1.00 153.70 ?  920 NAG A O3  1 
HETATM 22705 O O4  . NAG FA 7 .   ? 27.443  22.180  195.118 1.00 170.18 ?  920 NAG A O4  1 
HETATM 22706 O O5  . NAG FA 7 .   ? 25.096  23.329  192.546 1.00 157.44 ?  920 NAG A O5  1 
HETATM 22707 O O6  . NAG FA 7 .   ? 26.816  21.348  191.730 1.00 180.60 ?  920 NAG A O6  1 
HETATM 22708 O O7  . NAG FA 7 .   ? 21.229  22.431  195.017 1.00 165.14 ?  920 NAG A O7  1 
HETATM 22709 C C1  . NAG GA 7 .   ? 27.360  20.776  195.453 1.00 182.91 ?  921 NAG A C1  1 
HETATM 22710 C C2  . NAG GA 7 .   ? 28.637  20.023  195.066 1.00 185.97 ?  921 NAG A C2  1 
HETATM 22711 C C3  . NAG GA 7 .   ? 28.509  18.555  195.464 1.00 197.92 ?  921 NAG A C3  1 
HETATM 22712 C C4  . NAG GA 7 .   ? 28.097  18.411  196.925 1.00 203.07 ?  921 NAG A C4  1 
HETATM 22713 C C5  . NAG GA 7 .   ? 26.888  19.288  197.254 1.00 196.74 ?  921 NAG A C5  1 
HETATM 22714 C C6  . NAG GA 7 .   ? 26.560  19.322  198.729 1.00 198.10 ?  921 NAG A C6  1 
HETATM 22715 C C7  . NAG GA 7 .   ? 30.122  20.025  193.105 1.00 198.38 ?  921 NAG A C7  1 
HETATM 22716 C C8  . NAG GA 7 .   ? 30.203  20.175  191.615 1.00 199.56 ?  921 NAG A C8  1 
HETATM 22717 N N2  . NAG GA 7 .   ? 28.902  20.143  193.641 1.00 188.97 ?  921 NAG A N2  1 
HETATM 22718 O O3  . NAG GA 7 .   ? 29.742  17.880  195.242 1.00 208.16 ?  921 NAG A O3  1 
HETATM 22719 O O4  . NAG GA 7 .   ? 27.707  17.060  197.131 1.00 218.19 ?  921 NAG A O4  1 
HETATM 22720 O O5  . NAG GA 7 .   ? 27.136  20.644  196.865 1.00 190.60 ?  921 NAG A O5  1 
HETATM 22721 O O6  . NAG GA 7 .   ? 25.214  19.721  198.950 1.00 197.49 ?  921 NAG A O6  1 
HETATM 22722 O O7  . NAG GA 7 .   ? 31.117  19.806  193.791 1.00 204.63 ?  921 NAG A O7  1 
HETATM 22723 C C1  . BMA HA 8 .   ? 28.496  16.457  198.168 1.00 225.47 ?  922 BMA A C1  1 
HETATM 22724 C C2  . BMA HA 8 .   ? 28.196  14.964  198.064 1.00 229.35 ?  922 BMA A C2  1 
HETATM 22725 C C3  . BMA HA 8 .   ? 29.060  14.178  199.030 1.00 231.89 ?  922 BMA A C3  1 
HETATM 22726 C C4  . BMA HA 8 .   ? 30.540  14.579  198.892 1.00 234.97 ?  922 BMA A C4  1 
HETATM 22727 C C5  . BMA HA 8 .   ? 30.693  16.114  198.985 1.00 236.34 ?  922 BMA A C5  1 
HETATM 22728 C C6  . BMA HA 8 .   ? 32.110  16.578  198.769 1.00 246.34 ?  922 BMA A C6  1 
HETATM 22729 O O2  . BMA HA 8 .   ? 28.507  14.479  196.765 1.00 228.45 ?  922 BMA A O2  1 
HETATM 22730 O O3  . BMA HA 8 .   ? 28.899  12.777  198.829 1.00 234.13 ?  922 BMA A O3  1 
HETATM 22731 O O4  . BMA HA 8 .   ? 31.315  13.970  199.907 1.00 236.17 ?  922 BMA A O4  1 
HETATM 22732 O O5  . BMA HA 8 .   ? 29.872  16.728  197.992 1.00 229.84 ?  922 BMA A O5  1 
HETATM 22733 O O6  . BMA HA 8 .   ? 32.574  16.046  197.544 1.00 253.23 ?  922 BMA A O6  1 
HETATM 22734 C C1  . MAN IA 9 .   ? 34.006  15.914  197.668 1.00 257.43 ?  923 MAN A C1  1 
HETATM 22735 C C2  . MAN IA 9 .   ? 34.648  17.188  197.033 1.00 255.37 ?  923 MAN A C2  1 
HETATM 22736 C C3  . MAN IA 9 .   ? 34.567  17.130  195.506 1.00 249.75 ?  923 MAN A C3  1 
HETATM 22737 C C4  . MAN IA 9 .   ? 35.095  15.785  194.986 1.00 250.82 ?  923 MAN A C4  1 
HETATM 22738 C C5  . MAN IA 9 .   ? 34.300  14.638  195.624 1.00 251.22 ?  923 MAN A C5  1 
HETATM 22739 C C6  . MAN IA 9 .   ? 34.779  13.270  195.178 1.00 240.97 ?  923 MAN A C6  1 
HETATM 22740 O O2  . MAN IA 9 .   ? 36.037  17.286  197.356 1.00 258.29 ?  923 MAN A O2  1 
HETATM 22741 O O3  . MAN IA 9 .   ? 35.279  18.206  194.898 1.00 246.75 ?  923 MAN A O3  1 
HETATM 22742 O O4  . MAN IA 9 .   ? 34.961  15.720  193.575 1.00 251.19 ?  923 MAN A O4  1 
HETATM 22743 O O5  . MAN IA 9 .   ? 34.453  14.707  197.053 1.00 257.27 ?  923 MAN A O5  1 
HETATM 22744 O O6  . MAN IA 9 .   ? 33.726  12.340  195.405 1.00 232.44 ?  923 MAN A O6  1 
HETATM 22745 C C1  . MAN JA 9 .   ? 27.791  12.330  199.650 1.00 245.23 ?  924 MAN A C1  1 
HETATM 22746 C C2  . MAN JA 9 .   ? 27.975  10.833  199.917 1.00 246.83 ?  924 MAN A C2  1 
HETATM 22747 C C3  . MAN JA 9 .   ? 27.814  10.071  198.610 1.00 242.99 ?  924 MAN A C3  1 
HETATM 22748 C C4  . MAN JA 9 .   ? 26.464  10.400  197.944 1.00 240.89 ?  924 MAN A C4  1 
HETATM 22749 C C5  . MAN JA 9 .   ? 26.336  11.906  197.739 1.00 246.95 ?  924 MAN A C5  1 
HETATM 22750 C C6  . MAN JA 9 .   ? 24.974  12.325  197.210 1.00 255.09 ?  924 MAN A C6  1 
HETATM 22751 O O2  . MAN JA 9 .   ? 26.933  10.341  200.767 1.00 251.04 ?  924 MAN A O2  1 
HETATM 22752 O O3  . MAN JA 9 .   ? 27.928  8.683   198.807 1.00 243.84 ?  924 MAN A O3  1 
HETATM 22753 O O4  . MAN JA 9 .   ? 26.371  9.755   196.691 1.00 235.96 ?  924 MAN A O4  1 
HETATM 22754 O O5  . MAN JA 9 .   ? 26.537  12.574  199.009 1.00 244.31 ?  924 MAN A O5  1 
HETATM 22755 O O6  . MAN JA 9 .   ? 24.220  12.854  198.298 1.00 261.11 ?  924 MAN A O6  1 
HETATM 22756 C C1  . MAN KA 9 .   ? 27.490  9.645   201.907 1.00 233.41 ?  925 MAN A C1  1 
HETATM 22757 C C2  . MAN KA 9 .   ? 26.842  10.253  203.186 1.00 232.60 ?  925 MAN A C2  1 
HETATM 22758 C C3  . MAN KA 9 .   ? 27.821  10.207  204.359 1.00 232.56 ?  925 MAN A C3  1 
HETATM 22759 C C4  . MAN KA 9 .   ? 28.713  8.958   204.272 1.00 230.37 ?  925 MAN A C4  1 
HETATM 22760 C C5  . MAN KA 9 .   ? 29.612  9.058   203.017 1.00 231.69 ?  925 MAN A C5  1 
HETATM 22761 C C6  . MAN KA 9 .   ? 30.083  7.708   202.494 1.00 232.02 ?  925 MAN A C6  1 
HETATM 22762 O O2  . MAN KA 9 .   ? 25.702  9.499   203.600 1.00 233.64 ?  925 MAN A O2  1 
HETATM 22763 O O3  . MAN KA 9 .   ? 27.147  10.253  205.618 1.00 234.49 ?  925 MAN A O3  1 
HETATM 22764 O O4  . MAN KA 9 .   ? 29.528  8.861   205.430 1.00 226.41 ?  925 MAN A O4  1 
HETATM 22765 O O5  . MAN KA 9 .   ? 28.915  9.741   201.925 1.00 235.23 ?  925 MAN A O5  1 
HETATM 22766 O O6  . MAN KA 9 .   ? 31.180  7.932   201.613 1.00 233.50 ?  925 MAN A O6  1 
HETATM 22767 C C1  . NAG LA 7 .   ? -3.670  43.596  184.370 1.00 220.17 ?  926 NAG A C1  1 
HETATM 22768 C C2  . NAG LA 7 .   ? -4.865  43.132  183.518 1.00 217.47 ?  926 NAG A C2  1 
HETATM 22769 C C3  . NAG LA 7 .   ? -5.790  44.305  183.173 1.00 217.61 ?  926 NAG A C3  1 
HETATM 22770 C C4  . NAG LA 7 .   ? -6.167  45.074  184.433 1.00 220.12 ?  926 NAG A C4  1 
HETATM 22771 C C5  . NAG LA 7 .   ? -4.910  45.472  185.203 1.00 217.36 ?  926 NAG A C5  1 
HETATM 22772 C C6  . NAG LA 7 .   ? -5.209  46.170  186.509 1.00 212.98 ?  926 NAG A C6  1 
HETATM 22773 C C7  . NAG LA 7 .   ? -3.740  42.747  181.271 1.00 211.13 ?  926 NAG A C7  1 
HETATM 22774 C C8  . NAG LA 7 .   ? -3.209  44.158  181.252 1.00 217.48 ?  926 NAG A C8  1 
HETATM 22775 N N2  . NAG LA 7 .   ? -4.483  42.363  182.332 1.00 210.74 ?  926 NAG A N2  1 
HETATM 22776 O O3  . NAG LA 7 .   ? -6.961  43.811  182.533 1.00 217.47 ?  926 NAG A O3  1 
HETATM 22777 O O4  . NAG LA 7 .   ? -6.887  46.251  184.088 1.00 223.59 ?  926 NAG A O4  1 
HETATM 22778 O O5  . NAG LA 7 .   ? -4.144  44.302  185.522 1.00 221.81 ?  926 NAG A O5  1 
HETATM 22779 O O6  . NAG LA 7 .   ? -4.614  45.496  187.610 1.00 210.18 ?  926 NAG A O6  1 
HETATM 22780 O O7  . NAG LA 7 .   ? -3.507  41.970  180.349 1.00 214.16 ?  926 NAG A O7  1 
HETATM 22781 C C1  . NAG MA 7 .   ? 32.775  31.165  198.314 1.00 177.79 ?  927 NAG A C1  1 
HETATM 22782 C C2  . NAG MA 7 .   ? 33.471  32.534  198.352 1.00 186.69 ?  927 NAG A C2  1 
HETATM 22783 C C3  . NAG MA 7 .   ? 34.456  32.662  197.191 1.00 194.44 ?  927 NAG A C3  1 
HETATM 22784 C C4  . NAG MA 7 .   ? 35.414  31.479  197.170 1.00 206.27 ?  927 NAG A C4  1 
HETATM 22785 C C5  . NAG MA 7 .   ? 34.617  30.176  197.149 1.00 196.47 ?  927 NAG A C5  1 
HETATM 22786 C C6  . NAG MA 7 .   ? 35.475  28.936  197.228 1.00 196.03 ?  927 NAG A C6  1 
HETATM 22787 C C7  . NAG MA 7 .   ? 32.208  34.390  199.352 1.00 203.54 ?  927 NAG A C7  1 
HETATM 22788 C C8  . NAG MA 7 .   ? 31.185  35.459  199.114 1.00 193.51 ?  927 NAG A C8  1 
HETATM 22789 N N2  . NAG MA 7 .   ? 32.498  33.614  198.304 1.00 193.45 ?  927 NAG A N2  1 
HETATM 22790 O O3  . NAG MA 7 .   ? 35.182  33.880  197.312 1.00 194.09 ?  927 NAG A O3  1 
HETATM 22791 O O4  . NAG MA 7 .   ? 36.264  31.566  196.030 1.00 229.31 ?  927 NAG A O4  1 
HETATM 22792 O O5  . NAG MA 7 .   ? 33.747  30.134  198.287 1.00 191.77 ?  927 NAG A O5  1 
HETATM 22793 O O6  . NAG MA 7 .   ? 34.932  27.997  198.146 1.00 199.19 ?  927 NAG A O6  1 
HETATM 22794 O O7  . NAG MA 7 .   ? 32.745  34.233  200.444 1.00 220.94 ?  927 NAG A O7  1 
HETATM 22795 C C1  . NAG NA 7 .   ? 37.626  31.630  196.526 1.00 217.31 ?  928 NAG A C1  1 
HETATM 22796 C C2  . NAG NA 7 .   ? 38.557  30.838  195.598 1.00 221.48 ?  928 NAG A C2  1 
HETATM 22797 C C3  . NAG NA 7 .   ? 39.989  30.897  196.126 1.00 226.02 ?  928 NAG A C3  1 
HETATM 22798 C C4  . NAG NA 7 .   ? 40.432  32.339  196.346 1.00 235.90 ?  928 NAG A C4  1 
HETATM 22799 C C5  . NAG NA 7 .   ? 39.417  33.074  197.217 1.00 228.06 ?  928 NAG A C5  1 
HETATM 22800 C C6  . NAG NA 7 .   ? 39.733  34.542  197.374 1.00 217.44 ?  928 NAG A C6  1 
HETATM 22801 C C7  . NAG NA 7 .   ? 37.685  28.933  194.307 1.00 223.48 ?  928 NAG A C7  1 
HETATM 22802 C C8  . NAG NA 7 .   ? 37.270  27.492  194.356 1.00 222.53 ?  928 NAG A C8  1 
HETATM 22803 N N2  . NAG NA 7 .   ? 38.116  29.459  195.460 1.00 223.71 ?  928 NAG A N2  1 
HETATM 22804 O O3  . NAG NA 7 .   ? 40.846  30.260  195.187 1.00 223.20 ?  928 NAG A O3  1 
HETATM 22805 O O4  . NAG NA 7 .   ? 41.620  32.324  197.130 1.00 244.88 ?  928 NAG A O4  1 
HETATM 22806 O O5  . NAG NA 7 .   ? 38.104  32.994  196.642 1.00 225.26 ?  928 NAG A O5  1 
HETATM 22807 O O6  . NAG NA 7 .   ? 39.155  35.071  198.560 1.00 212.33 ?  928 NAG A O6  1 
HETATM 22808 O O7  . NAG NA 7 .   ? 37.634  29.589  193.270 1.00 221.65 ?  928 NAG A O7  1 
HETATM 22809 C C1  . BMA OA 8 .   ? 42.921  32.679  196.557 1.00 239.07 ?  929 BMA A C1  1 
HETATM 22810 C C2  . BMA OA 8 .   ? 43.648  31.352  196.198 1.00 238.94 ?  929 BMA A C2  1 
HETATM 22811 C C3  . BMA OA 8 .   ? 45.097  31.692  195.966 1.00 239.97 ?  929 BMA A C3  1 
HETATM 22812 C C4  . BMA OA 8 .   ? 45.249  32.762  194.846 1.00 240.55 ?  929 BMA A C4  1 
HETATM 22813 C C5  . BMA OA 8 .   ? 44.293  33.983  195.049 1.00 240.48 ?  929 BMA A C5  1 
HETATM 22814 C C6  . BMA OA 8 .   ? 44.240  34.893  193.835 1.00 240.92 ?  929 BMA A C6  1 
HETATM 22815 O O2  . BMA OA 8 .   ? 43.168  30.852  194.968 1.00 238.48 ?  929 BMA A O2  1 
HETATM 22816 O O3  . BMA OA 8 .   ? 45.869  30.534  195.652 1.00 240.06 ?  929 BMA A O3  1 
HETATM 22817 O O4  . BMA OA 8 .   ? 46.596  33.217  194.800 1.00 241.71 ?  929 BMA A O4  1 
HETATM 22818 O O5  . BMA OA 8 .   ? 42.930  33.526  195.369 1.00 239.46 ?  929 BMA A O5  1 
HETATM 22819 O O6  . BMA OA 8 .   ? 44.066  36.222  194.296 1.00 241.57 ?  929 BMA A O6  1 
HETATM 22820 C C1  . NAG PA 7 .   ? 33.364  15.306  213.342 1.00 179.49 ?  930 NAG A C1  1 
HETATM 22821 C C2  . NAG PA 7 .   ? 34.652  15.500  212.546 1.00 187.53 ?  930 NAG A C2  1 
HETATM 22822 C C3  . NAG PA 7 .   ? 35.181  14.150  212.063 1.00 201.81 ?  930 NAG A C3  1 
HETATM 22823 C C4  . NAG PA 7 .   ? 35.323  13.177  213.229 1.00 206.34 ?  930 NAG A C4  1 
HETATM 22824 C C5  . NAG PA 7 .   ? 34.017  13.098  214.021 1.00 194.99 ?  930 NAG A C5  1 
HETATM 22825 C C6  . NAG PA 7 .   ? 34.133  12.250  215.269 1.00 193.27 ?  930 NAG A C6  1 
HETATM 22826 C C7  . NAG PA 7 .   ? 35.301  17.374  211.106 1.00 201.50 ?  930 NAG A C7  1 
HETATM 22827 C C8  . NAG PA 7 .   ? 34.936  18.211  209.918 1.00 209.25 ?  930 NAG A C8  1 
HETATM 22828 N N2  . NAG PA 7 .   ? 34.444  16.399  211.423 1.00 193.23 ?  930 NAG A N2  1 
HETATM 22829 O O3  . NAG PA 7 .   ? 36.439  14.338  211.426 1.00 209.06 ?  930 NAG A O3  1 
HETATM 22830 O O4  . NAG PA 7 .   ? 35.628  11.875  212.737 1.00 223.20 ?  930 NAG A O4  1 
HETATM 22831 O O5  . NAG PA 7 .   ? 33.611  14.411  214.441 1.00 192.12 ?  930 NAG A O5  1 
HETATM 22832 O O6  . NAG PA 7 .   ? 33.021  12.419  216.138 1.00 193.63 ?  930 NAG A O6  1 
HETATM 22833 O O7  . NAG PA 7 .   ? 36.326  17.572  211.752 1.00 205.43 ?  930 NAG A O7  1 
HETATM 22834 C C1  . NAG QA 7 .   ? 37.008  11.505  212.953 1.00 222.33 ?  931 NAG A C1  1 
HETATM 22835 C C2  . NAG QA 7 .   ? 37.100  9.991   213.174 1.00 232.68 ?  931 NAG A C2  1 
HETATM 22836 C C3  . NAG QA 7 .   ? 38.558  9.567   213.339 1.00 241.20 ?  931 NAG A C3  1 
HETATM 22837 C C4  . NAG QA 7 .   ? 39.395  10.069  212.169 1.00 244.24 ?  931 NAG A C4  1 
HETATM 22838 C C5  . NAG QA 7 .   ? 39.211  11.576  212.001 1.00 233.86 ?  931 NAG A C5  1 
HETATM 22839 C C6  . NAG QA 7 .   ? 39.926  12.130  210.789 1.00 231.02 ?  931 NAG A C6  1 
HETATM 22840 C C7  . NAG QA 7 .   ? 35.408  8.590   214.277 1.00 242.07 ?  931 NAG A C7  1 
HETATM 22841 C C8  . NAG QA 7 .   ? 34.689  8.296   215.559 1.00 240.79 ?  931 NAG A C8  1 
HETATM 22842 N N2  . NAG QA 7 .   ? 36.312  9.575   214.324 1.00 235.92 ?  931 NAG A N2  1 
HETATM 22843 O O3  . NAG QA 7 .   ? 38.629  8.148   213.414 1.00 245.00 ?  931 NAG A O3  1 
HETATM 22844 O O4  . NAG QA 7 .   ? 40.770  9.775   212.392 1.00 253.55 ?  931 NAG A O4  1 
HETATM 22845 O O5  . NAG QA 7 .   ? 37.818  11.878  211.831 1.00 228.97 ?  931 NAG A O5  1 
HETATM 22846 O O6  . NAG QA 7 .   ? 39.120  13.071  210.092 1.00 228.86 ?  931 NAG A O6  1 
HETATM 22847 O O7  . NAG QA 7 .   ? 35.180  7.965   213.245 1.00 246.75 ?  931 NAG A O7  1 
HETATM 22848 C C1  . NAG RA 7 .   ? 31.229  34.191  205.796 1.00 178.87 ?  932 NAG A C1  1 
HETATM 22849 C C2  . NAG RA 7 .   ? 32.268  33.112  206.042 1.00 175.93 ?  932 NAG A C2  1 
HETATM 22850 C C3  . NAG RA 7 .   ? 32.661  33.098  207.514 1.00 177.88 ?  932 NAG A C3  1 
HETATM 22851 C C4  . NAG RA 7 .   ? 33.102  34.491  207.956 1.00 180.35 ?  932 NAG A C4  1 
HETATM 22852 C C5  . NAG RA 7 .   ? 32.055  35.537  207.581 1.00 178.37 ?  932 NAG A C5  1 
HETATM 22853 C C6  . NAG RA 7 .   ? 32.513  36.954  207.846 1.00 171.04 ?  932 NAG A C6  1 
HETATM 22854 C C7  . NAG RA 7 .   ? 32.125  31.239  204.457 1.00 186.35 ?  932 NAG A C7  1 
HETATM 22855 C C8  . NAG RA 7 .   ? 31.533  29.889  204.185 1.00 175.34 ?  932 NAG A C8  1 
HETATM 22856 N N2  . NAG RA 7 .   ? 31.785  31.805  205.621 1.00 177.66 ?  932 NAG A N2  1 
HETATM 22857 O O3  . NAG RA 7 .   ? 33.705  32.148  207.700 1.00 191.13 ?  932 NAG A O3  1 
HETATM 22858 O O4  . NAG RA 7 .   ? 33.261  34.537  209.369 1.00 197.07 ?  932 NAG A O4  1 
HETATM 22859 O O5  . NAG RA 7 .   ? 31.756  35.458  206.181 1.00 192.13 ?  932 NAG A O5  1 
HETATM 22860 O O6  . NAG RA 7 .   ? 33.385  37.424  206.827 1.00 181.11 ?  932 NAG A O6  1 
HETATM 22861 O O7  . NAG RA 7 .   ? 32.878  31.791  203.659 1.00 199.58 ?  932 NAG A O7  1 
HETATM 22862 C C1  . NAG SA 7 .   ? 34.638  34.251  209.657 1.00 192.95 ?  933 NAG A C1  1 
HETATM 22863 C C2  . NAG SA 7 .   ? 35.063  35.020  210.905 1.00 192.21 ?  933 NAG A C2  1 
HETATM 22864 C C3  . NAG SA 7 .   ? 36.503  34.677  211.275 1.00 185.17 ?  933 NAG A C3  1 
HETATM 22865 C C4  . NAG SA 7 .   ? 36.694  33.166  211.363 1.00 190.47 ?  933 NAG A C4  1 
HETATM 22866 C C5  . NAG SA 7 .   ? 36.171  32.482  210.104 1.00 189.46 ?  933 NAG A C5  1 
HETATM 22867 C C6  . NAG SA 7 .   ? 36.204  30.974  210.198 1.00 181.84 ?  933 NAG A C6  1 
HETATM 22868 C C7  . NAG SA 7 .   ? 35.519  37.179  209.789 1.00 213.29 ?  933 NAG A C7  1 
HETATM 22869 C C8  . NAG SA 7 .   ? 35.209  38.645  209.780 1.00 216.65 ?  933 NAG A C8  1 
HETATM 22870 N N2  . NAG SA 7 .   ? 34.898  36.457  210.731 1.00 198.56 ?  933 NAG A N2  1 
HETATM 22871 O O3  . NAG SA 7 .   ? 36.807  35.295  212.521 1.00 176.56 ?  933 NAG A O3  1 
HETATM 22872 O O4  . NAG SA 7 .   ? 38.077  32.848  211.449 1.00 191.29 ?  933 NAG A O4  1 
HETATM 22873 O O5  . NAG SA 7 .   ? 34.805  32.853  209.877 1.00 191.33 ?  933 NAG A O5  1 
HETATM 22874 O O6  . NAG SA 7 .   ? 34.897  30.418  210.150 1.00 173.78 ?  933 NAG A O6  1 
HETATM 22875 O O7  . NAG SA 7 .   ? 36.297  36.676  208.981 1.00 220.07 ?  933 NAG A O7  1 
HETATM 22876 C C1  . BMA TA 8 .   ? 38.503  32.738  212.813 1.00 197.02 ?  934 BMA A C1  1 
HETATM 22877 C C2  . BMA TA 8 .   ? 39.280  31.406  212.930 1.00 192.39 ?  934 BMA A C2  1 
HETATM 22878 C C3  . BMA TA 8 .   ? 40.210  31.384  214.150 1.00 190.74 ?  934 BMA A C3  1 
HETATM 22879 C C4  . BMA TA 8 .   ? 40.931  32.749  214.372 1.00 206.22 ?  934 BMA A C4  1 
HETATM 22880 C C5  . BMA TA 8 .   ? 39.916  33.886  214.378 1.00 207.38 ?  934 BMA A C5  1 
HETATM 22881 C C6  . BMA TA 8 .   ? 40.580  35.237  214.525 1.00 210.37 ?  934 BMA A C6  1 
HETATM 22882 O O2  . BMA TA 8 .   ? 40.104  31.191  211.779 1.00 195.39 ?  934 BMA A O2  1 
HETATM 22883 O O3  . BMA TA 8 .   ? 41.177  30.342  214.003 1.00 178.50 ?  934 BMA A O3  1 
HETATM 22884 O O4  . BMA TA 8 .   ? 41.649  32.780  215.603 1.00 213.42 ?  934 BMA A O4  1 
HETATM 22885 O O5  . BMA TA 8 .   ? 39.270  33.883  213.112 1.00 205.15 ?  934 BMA A O5  1 
HETATM 22886 O O6  . BMA TA 8 .   ? 41.360  35.449  213.360 1.00 217.33 ?  934 BMA A O6  1 
HETATM 22887 C C1  . MAN UA 9 .   ? 41.534  36.866  213.183 1.00 189.69 ?  935 MAN A C1  1 
HETATM 22888 C C2  . MAN UA 9 .   ? 42.061  37.067  211.750 1.00 199.19 ?  935 MAN A C2  1 
HETATM 22889 C C3  . MAN UA 9 .   ? 43.491  36.557  211.643 1.00 211.59 ?  935 MAN A C3  1 
HETATM 22890 C C4  . MAN UA 9 .   ? 44.370  37.131  212.771 1.00 212.42 ?  935 MAN A C4  1 
HETATM 22891 C C5  . MAN UA 9 .   ? 43.743  36.797  214.130 1.00 208.76 ?  935 MAN A C5  1 
HETATM 22892 C C6  . MAN UA 9 .   ? 44.515  37.363  215.313 1.00 214.97 ?  935 MAN A C6  1 
HETATM 22893 O O2  . MAN UA 9 .   ? 42.106  38.446  211.403 1.00 202.53 ?  935 MAN A O2  1 
HETATM 22894 O O3  . MAN UA 9 .   ? 44.054  36.841  210.376 1.00 222.96 ?  935 MAN A O3  1 
HETATM 22895 O O4  . MAN UA 9 .   ? 45.661  36.570  212.708 1.00 208.72 ?  935 MAN A O4  1 
HETATM 22896 O O5  . MAN UA 9 .   ? 42.423  37.361  214.168 1.00 193.30 ?  935 MAN A O5  1 
HETATM 22897 O O6  . MAN UA 9 .   ? 44.081  38.702  215.565 1.00 215.36 ?  935 MAN A O6  1 
HETATM 22898 C C1  . MAN VA 9 .   ? 44.323  38.992  216.962 1.00 220.06 ?  936 MAN A C1  1 
HETATM 22899 C C2  . MAN VA 9 .   ? 43.511  40.268  217.353 1.00 214.73 ?  936 MAN A C2  1 
HETATM 22900 C C3  . MAN VA 9 .   ? 44.137  41.512  216.737 1.00 214.66 ?  936 MAN A C3  1 
HETATM 22901 C C4  . MAN VA 9 .   ? 45.644  41.560  217.013 1.00 220.49 ?  936 MAN A C4  1 
HETATM 22902 C C5  . MAN VA 9 .   ? 46.315  40.271  216.521 1.00 219.57 ?  936 MAN A C5  1 
HETATM 22903 C C6  . MAN VA 9 .   ? 47.797  40.225  216.809 1.00 211.19 ?  936 MAN A C6  1 
HETATM 22904 O O2  . MAN VA 9 .   ? 43.520  40.483  218.765 1.00 216.33 ?  936 MAN A O2  1 
HETATM 22905 O O3  . MAN VA 9 .   ? 43.506  42.703  217.212 1.00 213.01 ?  936 MAN A O3  1 
HETATM 22906 O O4  . MAN VA 9 .   ? 46.215  42.662  216.344 1.00 222.24 ?  936 MAN A O4  1 
HETATM 22907 O O5  . MAN VA 9 .   ? 45.715  39.153  217.186 1.00 222.35 ?  936 MAN A O5  1 
HETATM 22908 O O6  . MAN VA 9 .   ? 48.329  39.063  216.183 1.00 200.88 ?  936 MAN A O6  1 
HETATM 22909 C C1  . MAN WA 9 .   ? 43.870  35.642  209.591 1.00 240.41 ?  937 MAN A C1  1 
HETATM 22910 C C2  . MAN WA 9 .   ? 45.271  34.994  209.338 1.00 245.73 ?  937 MAN A C2  1 
HETATM 22911 C C3  . MAN WA 9 .   ? 46.060  35.834  208.334 1.00 241.56 ?  937 MAN A C3  1 
HETATM 22912 C C4  . MAN WA 9 .   ? 45.227  36.103  207.068 1.00 238.20 ?  937 MAN A C4  1 
HETATM 22913 C C5  . MAN WA 9 .   ? 43.905  36.785  207.445 1.00 237.40 ?  937 MAN A C5  1 
HETATM 22914 C C6  . MAN WA 9 .   ? 43.003  37.030  206.247 1.00 235.91 ?  937 MAN A C6  1 
HETATM 22915 O O2  . MAN WA 9 .   ? 45.129  33.695  208.741 1.00 250.04 ?  937 MAN A O2  1 
HETATM 22916 O O3  . MAN WA 9 .   ? 47.303  35.223  207.991 1.00 238.24 ?  937 MAN A O3  1 
HETATM 22917 O O4  . MAN WA 9 .   ? 45.950  36.942  206.183 1.00 236.41 ?  937 MAN A O4  1 
HETATM 22918 O O5  . MAN WA 9 .   ? 43.190  35.939  208.371 1.00 238.52 ?  937 MAN A O5  1 
HETATM 22919 O O6  . MAN WA 9 .   ? 41.914  37.839  206.671 1.00 235.99 ?  937 MAN A O6  1 
HETATM 22920 C C1  . MAN XA 9 .   ? 41.410  29.741  215.299 1.00 207.09 ?  938 MAN A C1  1 
HETATM 22921 C C2  . MAN XA 9 .   ? 42.649  28.805  215.170 1.00 218.10 ?  938 MAN A C2  1 
HETATM 22922 C C3  . MAN XA 9 .   ? 42.280  27.542  214.406 1.00 196.35 ?  938 MAN A C3  1 
HETATM 22923 C C4  . MAN XA 9 .   ? 41.030  26.891  215.010 1.00 193.33 ?  938 MAN A C4  1 
HETATM 22924 C C5  . MAN XA 9 .   ? 39.863  27.881  215.022 1.00 199.55 ?  938 MAN A C5  1 
HETATM 22925 C C6  . MAN XA 9 .   ? 38.620  27.318  215.685 1.00 203.39 ?  938 MAN A C6  1 
HETATM 22926 O O2  . MAN XA 9 .   ? 43.121  28.385  216.458 1.00 238.03 ?  938 MAN A O2  1 
HETATM 22927 O O3  . MAN XA 9 .   ? 43.355  26.612  214.375 1.00 197.71 ?  938 MAN A O3  1 
HETATM 22928 O O4  . MAN XA 9 .   ? 40.668  25.766  214.247 1.00 197.74 ?  938 MAN A O4  1 
HETATM 22929 O O5  . MAN XA 9 .   ? 40.243  29.050  215.760 1.00 196.21 ?  938 MAN A O5  1 
HETATM 22930 O O6  . MAN XA 9 .   ? 38.881  27.181  217.080 1.00 199.02 ?  938 MAN A O6  1 
HETATM 22931 C C1  . MAN YA 9 .   ? 44.406  29.009  216.689 1.00 230.90 ?  939 MAN A C1  1 
HETATM 22932 C C2  . MAN YA 9 .   ? 45.173  28.163  217.748 1.00 228.06 ?  939 MAN A C2  1 
HETATM 22933 C C3  . MAN YA 9 .   ? 44.523  28.341  219.123 1.00 220.16 ?  939 MAN A C3  1 
HETATM 22934 C C4  . MAN YA 9 .   ? 44.450  29.832  219.486 1.00 224.19 ?  939 MAN A C4  1 
HETATM 22935 C C5  . MAN YA 9 .   ? 43.644  30.586  218.412 1.00 224.02 ?  939 MAN A C5  1 
HETATM 22936 C C6  . MAN YA 9 .   ? 43.584  32.084  218.667 1.00 233.27 ?  939 MAN A C6  1 
HETATM 22937 O O2  . MAN YA 9 .   ? 46.522  28.630  217.849 1.00 246.07 ?  939 MAN A O2  1 
HETATM 22938 O O3  . MAN YA 9 .   ? 45.202  27.601  220.149 1.00 222.00 ?  939 MAN A O3  1 
HETATM 22939 O O4  . MAN YA 9 .   ? 43.818  29.991  220.755 1.00 234.07 ?  939 MAN A O4  1 
HETATM 22940 O O5  . MAN YA 9 .   ? 44.267  30.376  217.112 1.00 225.21 ?  939 MAN A O5  1 
HETATM 22941 O O6  . MAN YA 9 .   ? 44.910  32.599  218.576 1.00 240.54 ?  939 MAN A O6  1 
HETATM 22942 C C1  . MAN ZA 9 .   ? 47.465  27.535  217.963 1.00 233.57 ?  940 MAN A C1  1 
HETATM 22943 C C2  . MAN ZA 9 .   ? 48.889  28.163  217.783 1.00 240.24 ?  940 MAN A C2  1 
HETATM 22944 C C3  . MAN ZA 9 .   ? 49.193  28.404  216.309 1.00 238.52 ?  940 MAN A C3  1 
HETATM 22945 C C4  . MAN ZA 9 .   ? 48.963  27.127  215.500 1.00 240.51 ?  940 MAN A C4  1 
HETATM 22946 C C5  . MAN ZA 9 .   ? 47.504  26.698  215.629 1.00 239.08 ?  940 MAN A C5  1 
HETATM 22947 C C6  . MAN ZA 9 .   ? 47.198  25.413  214.882 1.00 240.99 ?  940 MAN A C6  1 
HETATM 22948 O O2  . MAN ZA 9 .   ? 49.913  27.287  218.262 1.00 241.45 ?  940 MAN A O2  1 
HETATM 22949 O O3  . MAN ZA 9 .   ? 50.523  28.878  216.113 1.00 240.84 ?  940 MAN A O3  1 
HETATM 22950 O O4  . MAN ZA 9 .   ? 49.259  27.367  214.135 1.00 244.94 ?  940 MAN A O4  1 
HETATM 22951 O O5  . MAN ZA 9 .   ? 47.190  26.469  217.029 1.00 235.32 ?  940 MAN A O5  1 
HETATM 22952 O O6  . MAN ZA 9 .   ? 47.830  25.481  213.610 1.00 243.91 ?  940 MAN A O6  1 
HETATM 22953 C C1  . MAN AB 9 .   ? 45.902  32.680  209.429 1.00 248.87 ?  941 MAN A C1  1 
HETATM 22954 C C2  . MAN AB 9 .   ? 45.455  32.620  210.928 1.00 248.24 ?  941 MAN A C2  1 
HETATM 22955 C C3  . MAN AB 9 .   ? 46.607  32.124  211.804 1.00 244.45 ?  941 MAN A C3  1 
HETATM 22956 C C4  . MAN AB 9 .   ? 47.527  31.173  211.022 1.00 240.74 ?  941 MAN A C4  1 
HETATM 22957 C C5  . MAN AB 9 .   ? 48.212  31.959  209.877 1.00 244.36 ?  941 MAN A C5  1 
HETATM 22958 C C6  . MAN AB 9 .   ? 48.709  31.075  208.744 1.00 245.42 ?  941 MAN A C6  1 
HETATM 22959 O O2  . MAN AB 9 .   ? 44.386  31.690  211.118 1.00 248.37 ?  941 MAN A O2  1 
HETATM 22960 O O3  . MAN AB 9 .   ? 46.136  31.491  212.992 1.00 244.57 ?  941 MAN A O3  1 
HETATM 22961 O O4  . MAN AB 9 .   ? 48.517  30.633  211.882 1.00 237.70 ?  941 MAN A O4  1 
HETATM 22962 O O5  . MAN AB 9 .   ? 47.303  32.943  209.300 1.00 246.74 ?  941 MAN A O5  1 
HETATM 22963 O O6  . MAN AB 9 .   ? 49.405  31.900  207.812 1.00 247.31 ?  941 MAN A O6  1 
HETATM 22964 C C1  . NAG BB 7 .   ? 15.156  56.189  180.011 1.00 252.35 ?  942 NAG A C1  1 
HETATM 22965 C C2  . NAG BB 7 .   ? 14.746  55.595  178.668 1.00 260.71 ?  942 NAG A C2  1 
HETATM 22966 C C3  . NAG BB 7 .   ? 15.957  54.981  177.972 1.00 259.61 ?  942 NAG A C3  1 
HETATM 22967 C C4  . NAG BB 7 .   ? 17.090  55.997  177.879 1.00 257.57 ?  942 NAG A C4  1 
HETATM 22968 C C5  . NAG BB 7 .   ? 17.394  56.582  179.257 1.00 258.09 ?  942 NAG A C5  1 
HETATM 22969 C C6  . NAG BB 7 .   ? 18.428  57.683  179.215 1.00 250.42 ?  942 NAG A C6  1 
HETATM 22970 C C7  . NAG BB 7 .   ? 12.406  54.852  178.554 1.00 268.03 ?  942 NAG A C7  1 
HETATM 22971 C C8  . NAG BB 7 .   ? 12.093  56.223  178.029 1.00 272.33 ?  942 NAG A C8  1 
HETATM 22972 N N2  . NAG BB 7 .   ? 13.691  54.609  178.837 1.00 264.23 ?  942 NAG A N2  1 
HETATM 22973 O O3  . NAG BB 7 .   ? 15.584  54.544  176.671 1.00 259.32 ?  942 NAG A O3  1 
HETATM 22974 O O4  . NAG BB 7 .   ? 18.264  55.373  177.373 1.00 252.01 ?  942 NAG A O4  1 
HETATM 22975 O O5  . NAG BB 7 .   ? 16.201  57.154  179.813 1.00 264.50 ?  942 NAG A O5  1 
HETATM 22976 O O6  . NAG BB 7 .   ? 18.800  58.106  180.520 1.00 246.71 ?  942 NAG A O6  1 
HETATM 22977 O O7  . NAG BB 7 .   ? 11.534  54.003  178.711 1.00 265.90 ?  942 NAG A O7  1 
HETATM 22978 C C1  . NAG CB 7 .   ? 11.841  42.900  208.611 1.00 224.53 ?  943 NAG A C1  1 
HETATM 22979 C C2  . NAG CB 7 .   ? 11.340  42.003  209.725 1.00 229.93 ?  943 NAG A C2  1 
HETATM 22980 C C3  . NAG CB 7 .   ? 10.649  42.839  210.800 1.00 247.38 ?  943 NAG A C3  1 
HETATM 22981 C C4  . NAG CB 7 .   ? 11.567  43.961  211.271 1.00 259.13 ?  943 NAG A C4  1 
HETATM 22982 C C5  . NAG CB 7 .   ? 12.087  44.760  210.080 1.00 246.52 ?  943 NAG A C5  1 
HETATM 22983 C C6  . NAG CB 7 .   ? 13.118  45.796  210.461 1.00 240.65 ?  943 NAG A C6  1 
HETATM 22984 C C7  . NAG CB 7 .   ? 10.854  39.968  208.436 1.00 219.01 ?  943 NAG A C7  1 
HETATM 22985 C C8  . NAG CB 7 .   ? 9.789   39.019  207.977 1.00 223.81 ?  943 NAG A C8  1 
HETATM 22986 N N2  . NAG CB 7 .   ? 10.441  40.987  209.201 1.00 224.95 ?  943 NAG A N2  1 
HETATM 22987 O O3  . NAG CB 7 .   ? 10.283  42.000  211.889 1.00 251.80 ?  943 NAG A O3  1 
HETATM 22988 O O4  . NAG CB 7 .   ? 10.876  44.838  212.153 1.00 280.36 ?  943 NAG A O4  1 
HETATM 22989 O O5  . NAG CB 7 .   ? 12.718  43.879  209.142 1.00 234.08 ?  943 NAG A O5  1 
HETATM 22990 O O6  . NAG CB 7 .   ? 13.267  46.778  209.445 1.00 237.39 ?  943 NAG A O6  1 
HETATM 22991 O O7  . NAG CB 7 .   ? 12.035  39.817  208.131 1.00 220.60 ?  943 NAG A O7  1 
HETATM 22992 C C1  . NAG DB 7 .   ? 11.282  44.499  213.493 1.00 260.02 ?  944 NAG A C1  1 
HETATM 22993 C C2  . NAG DB 7 .   ? 11.144  45.720  214.404 1.00 267.53 ?  944 NAG A C2  1 
HETATM 22994 C C3  . NAG DB 7 .   ? 11.502  45.345  215.840 1.00 272.24 ?  944 NAG A C3  1 
HETATM 22995 C C4  . NAG DB 7 .   ? 10.684  44.145  216.298 1.00 272.64 ?  944 NAG A C4  1 
HETATM 22996 C C5  . NAG DB 7 .   ? 10.839  42.992  215.309 1.00 263.16 ?  944 NAG A C5  1 
HETATM 22997 C C6  . NAG DB 7 .   ? 9.960   41.808  215.635 1.00 257.39 ?  944 NAG A C6  1 
HETATM 22998 C C7  . NAG DB 7 .   ? 11.494  47.922  213.370 1.00 268.59 ?  944 NAG A C7  1 
HETATM 22999 C C8  . NAG DB 7 .   ? 12.506  48.946  212.950 1.00 268.17 ?  944 NAG A C8  1 
HETATM 23000 N N2  . NAG DB 7 .   ? 11.982  46.814  213.938 1.00 267.33 ?  944 NAG A N2  1 
HETATM 23001 O O3  . NAG DB 7 .   ? 11.259  46.454  216.698 1.00 276.67 ?  944 NAG A O3  1 
HETATM 23002 O O4  . NAG DB 7 .   ? 11.121  43.722  217.585 1.00 276.56 ?  944 NAG A O4  1 
HETATM 23003 O O5  . NAG DB 7 .   ? 10.469  43.429  213.994 1.00 264.16 ?  944 NAG A O5  1 
HETATM 23004 O O6  . NAG DB 7 .   ? 10.669  40.583  215.503 1.00 252.12 ?  944 NAG A O6  1 
HETATM 23005 O O7  . NAG DB 7 .   ? 10.290  48.091  213.203 1.00 270.24 ?  944 NAG A O7  1 
HETATM 23006 C C1  . NAG EB 7 .   ? 15.724  38.851  210.395 1.00 189.76 ?  945 NAG A C1  1 
HETATM 23007 C C2  . NAG EB 7 .   ? 15.217  38.441  211.779 1.00 211.92 ?  945 NAG A C2  1 
HETATM 23008 C C3  . NAG EB 7 .   ? 14.530  39.619  212.470 1.00 222.73 ?  945 NAG A C3  1 
HETATM 23009 C C4  . NAG EB 7 .   ? 15.468  40.820  212.510 1.00 225.52 ?  945 NAG A C4  1 
HETATM 23010 C C5  . NAG EB 7 .   ? 15.937  41.151  211.095 1.00 201.40 ?  945 NAG A C5  1 
HETATM 23011 C C6  . NAG EB 7 .   ? 16.944  42.277  211.049 1.00 200.52 ?  945 NAG A C6  1 
HETATM 23012 C C7  . NAG EB 7 .   ? 13.197  37.247  210.994 1.00 234.46 ?  945 NAG A C7  1 
HETATM 23013 C C8  . NAG EB 7 .   ? 12.436  35.957  211.054 1.00 234.46 ?  945 NAG A C8  1 
HETATM 23014 N N2  . NAG EB 7 .   ? 14.331  37.288  211.707 1.00 222.05 ?  945 NAG A N2  1 
HETATM 23015 O O3  . NAG EB 7 .   ? 14.153  39.234  213.787 1.00 231.60 ?  945 NAG A O3  1 
HETATM 23016 O O4  . NAG EB 7 .   ? 14.833  41.952  213.099 1.00 252.21 ?  945 NAG A O4  1 
HETATM 23017 O O5  . NAG EB 7 .   ? 16.574  40.002  210.515 1.00 184.23 ?  945 NAG A O5  1 
HETATM 23018 O O6  . NAG EB 7 .   ? 18.278  41.793  211.127 1.00 188.10 ?  945 NAG A O6  1 
HETATM 23019 O O7  . NAG EB 7 .   ? 12.799  38.204  210.335 1.00 240.83 ?  945 NAG A O7  1 
HETATM 23020 C C1  . NAG FB 7 .   ? 15.307  42.129  214.458 1.00 242.73 ?  946 NAG A C1  1 
HETATM 23021 C C2  . NAG FB 7 .   ? 15.617  43.605  214.728 1.00 243.29 ?  946 NAG A C2  1 
HETATM 23022 C C3  . NAG FB 7 .   ? 16.062  43.792  216.177 1.00 244.20 ?  946 NAG A C3  1 
HETATM 23023 C C4  . NAG FB 7 .   ? 15.035  43.198  217.131 1.00 247.42 ?  946 NAG A C4  1 
HETATM 23024 C C5  . NAG FB 7 .   ? 14.744  41.745  216.760 1.00 249.02 ?  946 NAG A C5  1 
HETATM 23025 C C6  . NAG FB 7 .   ? 13.638  41.135  217.591 1.00 248.12 ?  946 NAG A C6  1 
HETATM 23026 C C7  . NAG FB 7 .   ? 16.512  45.254  213.147 1.00 233.40 ?  946 NAG A C7  1 
HETATM 23027 C C8  . NAG FB 7 .   ? 17.659  45.619  212.254 1.00 226.08 ?  946 NAG A C8  1 
HETATM 23028 N N2  . NAG FB 7 .   ? 16.634  44.104  213.817 1.00 238.45 ?  946 NAG A N2  1 
HETATM 23029 O O3  . NAG FB 7 .   ? 16.229  45.178  216.453 1.00 246.12 ?  946 NAG A O3  1 
HETATM 23030 O O4  . NAG FB 7 .   ? 15.522  43.268  218.467 1.00 245.98 ?  946 NAG A O4  1 
HETATM 23031 O O5  . NAG FB 7 .   ? 14.320  41.669  215.390 1.00 249.88 ?  946 NAG A O5  1 
HETATM 23032 O O6  . NAG FB 7 .   ? 13.416  39.774  217.247 1.00 244.47 ?  946 NAG A O6  1 
HETATM 23033 O O7  . NAG FB 7 .   ? 15.519  45.967  213.255 1.00 235.37 ?  946 NAG A O7  1 
HETATM 23034 C C1  . NAG GB 7 .   ? 19.549  48.820  206.500 1.00 238.29 ?  947 NAG A C1  1 
HETATM 23035 C C2  . NAG GB 7 .   ? 19.184  48.368  207.907 1.00 243.63 ?  947 NAG A C2  1 
HETATM 23036 C C3  . NAG GB 7 .   ? 19.323  49.533  208.883 1.00 252.23 ?  947 NAG A C3  1 
HETATM 23037 C C4  . NAG GB 7 .   ? 20.714  50.150  208.783 1.00 259.82 ?  947 NAG A C4  1 
HETATM 23038 C C5  . NAG GB 7 .   ? 21.046  50.483  207.327 1.00 255.31 ?  947 NAG A C5  1 
HETATM 23039 C C6  . NAG GB 7 .   ? 22.468  50.957  207.140 1.00 260.83 ?  947 NAG A C6  1 
HETATM 23040 C C7  . NAG GB 7 .   ? 17.593  46.540  208.286 1.00 236.40 ?  947 NAG A C7  1 
HETATM 23041 C C8  . NAG GB 7 .   ? 16.153  46.126  208.276 1.00 240.29 ?  947 NAG A C8  1 
HETATM 23042 N N2  . NAG GB 7 .   ? 17.842  47.811  207.950 1.00 238.71 ?  947 NAG A N2  1 
HETATM 23043 O O3  . NAG GB 7 .   ? 19.082  49.054  210.202 1.00 253.72 ?  947 NAG A O3  1 
HETATM 23044 O O4  . NAG GB 7 .   ? 20.773  51.375  209.508 1.00 272.13 ?  947 NAG A O4  1 
HETATM 23045 O O5  . NAG GB 7 .   ? 20.882  49.326  206.493 1.00 245.74 ?  947 NAG A O5  1 
HETATM 23046 O O6  . NAG GB 7 .   ? 22.740  51.249  205.776 1.00 265.70 ?  947 NAG A O6  1 
HETATM 23047 O O7  . NAG GB 7 .   ? 18.492  45.761  208.587 1.00 231.94 ?  947 NAG A O7  1 
HETATM 23048 C C1  . NAG HB 7 .   ? 21.101  51.245  210.907 1.00 268.10 ?  948 NAG A C1  1 
HETATM 23049 C C2  . NAG HB 7 .   ? 22.578  51.566  211.146 1.00 265.48 ?  948 NAG A C2  1 
HETATM 23050 C C3  . NAG HB 7 .   ? 22.898  51.526  212.639 1.00 268.28 ?  948 NAG A C3  1 
HETATM 23051 C C4  . NAG HB 7 .   ? 21.941  52.421  213.416 1.00 271.58 ?  948 NAG A C4  1 
HETATM 23052 C C5  . NAG HB 7 .   ? 20.499  52.045  213.094 1.00 271.46 ?  948 NAG A C5  1 
HETATM 23053 C C6  . NAG HB 7 .   ? 19.488  52.954  213.755 1.00 273.37 ?  948 NAG A C6  1 
HETATM 23054 C C7  . NAG HB 7 .   ? 24.653  50.990  209.966 1.00 247.17 ?  948 NAG A C7  1 
HETATM 23055 C C8  . NAG HB 7 .   ? 25.406  49.921  209.234 1.00 243.19 ?  948 NAG A C8  1 
HETATM 23056 N N2  . NAG HB 7 .   ? 23.440  50.650  210.415 1.00 255.22 ?  948 NAG A N2  1 
HETATM 23057 O O3  . NAG HB 7 .   ? 24.238  51.956  212.847 1.00 269.88 ?  948 NAG A O3  1 
HETATM 23058 O O4  . NAG HB 7 .   ? 22.161  52.284  214.815 1.00 271.08 ?  948 NAG A O4  1 
HETATM 23059 O O5  . NAG HB 7 .   ? 20.282  52.136  211.679 1.00 271.86 ?  948 NAG A O5  1 
HETATM 23060 O O6  . NAG HB 7 .   ? 18.327  53.113  212.953 1.00 274.16 ?  948 NAG A O6  1 
HETATM 23061 O O7  . NAG HB 7 .   ? 25.120  52.111  210.143 1.00 245.19 ?  948 NAG A O7  1 
HETATM 23062 C C1  . NAG IB 7 .   ? 28.235  28.910  188.543 1.00 189.67 ?  949 NAG A C1  1 
HETATM 23063 C C2  . NAG IB 7 .   ? 28.225  27.494  187.941 1.00 202.69 ?  949 NAG A C2  1 
HETATM 23064 C C3  . NAG IB 7 .   ? 29.618  27.111  187.457 1.00 204.77 ?  949 NAG A C3  1 
HETATM 23065 C C4  . NAG IB 7 .   ? 30.178  28.169  186.512 1.00 207.62 ?  949 NAG A C4  1 
HETATM 23066 C C5  . NAG IB 7 .   ? 30.156  29.538  187.194 1.00 213.56 ?  949 NAG A C5  1 
HETATM 23067 C C6  . NAG IB 7 .   ? 30.668  30.676  186.333 1.00 219.68 ?  949 NAG A C6  1 
HETATM 23068 C C7  . NAG IB 7 .   ? 26.526  25.950  188.846 1.00 205.02 ?  949 NAG A C7  1 
HETATM 23069 C C8  . NAG IB 7 .   ? 25.676  26.328  187.668 1.00 199.16 ?  949 NAG A C8  1 
HETATM 23070 N N2  . NAG IB 7 .   ? 27.735  26.522  188.910 1.00 207.24 ?  949 NAG A N2  1 
HETATM 23071 O O3  . NAG IB 7 .   ? 29.486  25.862  186.792 1.00 208.05 ?  949 NAG A O3  1 
HETATM 23072 O O4  . NAG IB 7 .   ? 31.511  27.820  186.156 1.00 218.32 ?  949 NAG A O4  1 
HETATM 23073 O O5  . NAG IB 7 .   ? 28.808  29.858  187.575 1.00 208.75 ?  949 NAG A O5  1 
HETATM 23074 O O6  . NAG IB 7 .   ? 30.798  31.875  187.087 1.00 223.23 ?  949 NAG A O6  1 
HETATM 23075 O O7  . NAG IB 7 .   ? 26.142  25.146  189.693 1.00 207.01 ?  949 NAG A O7  1 
HETATM 23076 C C1  . NAG JB 7 .   ? 31.594  27.554  184.739 1.00 213.91 ?  950 NAG A C1  1 
HETATM 23077 C C2  . NAG JB 7 .   ? 33.070  27.602  184.349 1.00 221.24 ?  950 NAG A C2  1 
HETATM 23078 C C3  . NAG JB 7 .   ? 33.228  27.333  182.855 1.00 233.56 ?  950 NAG A C3  1 
HETATM 23079 C C4  . NAG JB 7 .   ? 32.510  26.049  182.448 1.00 246.75 ?  950 NAG A C4  1 
HETATM 23080 C C5  . NAG JB 7 .   ? 31.069  26.033  182.960 1.00 233.52 ?  950 NAG A C5  1 
HETATM 23081 C C6  . NAG JB 7 .   ? 30.360  24.717  182.721 1.00 235.31 ?  950 NAG A C6  1 
HETATM 23082 C C7  . NAG JB 7 .   ? 34.967  29.028  185.005 1.00 204.35 ?  950 NAG A C7  1 
HETATM 23083 C C8  . NAG JB 7 .   ? 35.408  30.417  185.361 1.00 200.79 ?  950 NAG A C8  1 
HETATM 23084 N N2  . NAG JB 7 .   ? 33.669  28.880  184.709 1.00 214.80 ?  950 NAG A N2  1 
HETATM 23085 O O3  . NAG JB 7 .   ? 34.616  27.227  182.556 1.00 235.04 ?  950 NAG A O3  1 
HETATM 23086 O O4  . NAG JB 7 .   ? 32.478  25.964  181.028 1.00 273.84 ?  950 NAG A O4  1 
HETATM 23087 O O5  . NAG JB 7 .   ? 31.041  26.273  184.375 1.00 220.71 ?  950 NAG A O5  1 
HETATM 23088 O O6  . NAG JB 7 .   ? 29.269  24.538  183.615 1.00 233.62 ?  950 NAG A O6  1 
HETATM 23089 O O7  . NAG JB 7 .   ? 35.751  28.084  184.980 1.00 199.49 ?  950 NAG A O7  1 
HETATM 23090 C C1  . BMA KB 8 .   ? 33.497  25.048  180.578 1.00 245.65 ?  951 BMA A C1  1 
HETATM 23091 C C2  . BMA KB 8 .   ? 32.823  23.918  179.772 1.00 274.33 ?  951 BMA A C2  1 
HETATM 23092 C C3  . BMA KB 8 .   ? 33.903  22.981  179.225 1.00 257.94 ?  951 BMA A C3  1 
HETATM 23093 C C4  . BMA KB 8 .   ? 35.051  23.747  178.523 1.00 244.79 ?  951 BMA A C4  1 
HETATM 23094 C C5  . BMA KB 8 .   ? 35.577  24.886  179.413 1.00 231.56 ?  951 BMA A C5  1 
HETATM 23095 C C6  . BMA KB 8 .   ? 36.599  25.755  178.711 1.00 217.36 ?  951 BMA A C6  1 
HETATM 23096 O O2  . BMA KB 8 .   ? 32.135  24.439  178.653 1.00 327.70 ?  951 BMA A O2  1 
HETATM 23097 O O3  . BMA KB 8 .   ? 33.357  22.013  178.337 1.00 254.76 ?  951 BMA A O3  1 
HETATM 23098 O O4  . BMA KB 8 .   ? 36.113  22.852  178.239 1.00 246.47 ?  951 BMA A O4  1 
HETATM 23099 O O5  . BMA KB 8 .   ? 34.472  25.718  179.780 1.00 237.01 ?  951 BMA A O5  1 
HETATM 23100 O O6  . BMA KB 8 .   ? 37.454  24.904  177.970 1.00 209.33 ?  951 BMA A O6  1 
HETATM 23101 C C1  . NAG LB 7 .   ? 28.207  50.140  196.163 1.00 248.59 ?  952 NAG A C1  1 
HETATM 23102 C C2  . NAG LB 7 .   ? 28.164  51.409  195.310 1.00 252.67 ?  952 NAG A C2  1 
HETATM 23103 C C3  . NAG LB 7 .   ? 28.866  52.545  196.056 1.00 258.01 ?  952 NAG A C3  1 
HETATM 23104 C C4  . NAG LB 7 .   ? 28.335  52.666  197.483 1.00 258.23 ?  952 NAG A C4  1 
HETATM 23105 C C5  . NAG LB 7 .   ? 28.290  51.303  198.174 1.00 257.15 ?  952 NAG A C5  1 
HETATM 23106 C C6  . NAG LB 7 .   ? 27.620  51.334  199.526 1.00 262.48 ?  952 NAG A C6  1 
HETATM 23107 C C7  . NAG LB 7 .   ? 28.473  51.918  192.924 1.00 245.61 ?  952 NAG A C7  1 
HETATM 23108 C C8  . NAG LB 7 .   ? 29.214  51.565  191.670 1.00 233.99 ?  952 NAG A C8  1 
HETATM 23109 N N2  . NAG LB 7 .   ? 28.780  51.196  194.009 1.00 245.93 ?  952 NAG A N2  1 
HETATM 23110 O O3  . NAG LB 7 .   ? 28.687  53.770  195.354 1.00 262.20 ?  952 NAG A O3  1 
HETATM 23111 O O4  . NAG LB 7 .   ? 29.175  53.527  198.244 1.00 258.44 ?  952 NAG A O4  1 
HETATM 23112 O O5  . NAG LB 7 .   ? 27.555  50.370  197.373 1.00 254.69 ?  952 NAG A O5  1 
HETATM 23113 O O6  . NAG LB 7 .   ? 27.369  50.017  199.998 1.00 265.74 ?  952 NAG A O6  1 
HETATM 23114 O O7  . NAG LB 7 .   ? 27.634  52.814  192.954 1.00 255.17 ?  952 NAG A O7  1 
HETATM 23115 C C1  . NAG MB 7 .   ? -19.019 25.233  146.709 1.00 239.51 ?  901 NAG B C1  1 
HETATM 23116 C C2  . NAG MB 7 .   ? -19.987 24.047  146.645 1.00 255.86 ?  901 NAG B C2  1 
HETATM 23117 C C3  . NAG MB 7 .   ? -21.430 24.538  146.724 1.00 278.40 ?  901 NAG B C3  1 
HETATM 23118 C C4  . NAG MB 7 .   ? -21.629 25.393  147.967 1.00 285.19 ?  901 NAG B C4  1 
HETATM 23119 C C5  . NAG MB 7 .   ? -20.610 26.529  147.999 1.00 270.86 ?  901 NAG B C5  1 
HETATM 23120 C C6  . NAG MB 7 .   ? -20.668 27.326  149.281 1.00 276.61 ?  901 NAG B C6  1 
HETATM 23121 C C7  . NAG MB 7 .   ? -20.123 21.966  145.349 1.00 252.74 ?  901 NAG B C7  1 
HETATM 23122 C C8  . NAG MB 7 .   ? -19.838 21.303  144.035 1.00 247.06 ?  901 NAG B C8  1 
HETATM 23123 N N2  . NAG MB 7 .   ? -19.779 23.256  145.443 1.00 249.94 ?  901 NAG B N2  1 
HETATM 23124 O O3  . NAG MB 7 .   ? -22.312 23.421  146.758 1.00 288.92 ?  901 NAG B O3  1 
HETATM 23125 O O4  . NAG MB 7 .   ? -22.941 25.945  147.980 1.00 303.97 ?  901 NAG B O4  1 
HETATM 23126 O O5  . NAG MB 7 .   ? -19.277 26.004  147.899 1.00 248.22 ?  901 NAG B O5  1 
HETATM 23127 O O6  . NAG MB 7 .   ? -20.187 28.650  149.094 1.00 274.68 ?  901 NAG B O6  1 
HETATM 23128 O O7  . NAG MB 7 .   ? -20.645 21.363  146.282 1.00 260.56 ?  901 NAG B O7  1 
HETATM 23129 C C1  . NAG NB 7 .   ? -3.187  33.482  137.822 1.00 260.28 ?  902 NAG B C1  1 
HETATM 23130 C C2  . NAG NB 7 .   ? -3.494  34.846  137.234 1.00 276.81 ?  902 NAG B C2  1 
HETATM 23131 C C3  . NAG NB 7 .   ? -3.463  34.767  135.713 1.00 286.37 ?  902 NAG B C3  1 
HETATM 23132 C C4  . NAG NB 7 .   ? -2.127  34.202  135.241 1.00 274.92 ?  902 NAG B C4  1 
HETATM 23133 C C5  . NAG NB 7 .   ? -1.794  32.891  135.959 1.00 271.16 ?  902 NAG B C5  1 
HETATM 23134 C C6  . NAG NB 7 .   ? -0.389  32.405  135.680 1.00 267.14 ?  902 NAG B C6  1 
HETATM 23135 C C7  . NAG NB 7 .   ? -4.888  36.320  138.621 1.00 285.58 ?  902 NAG B C7  1 
HETATM 23136 C C8  . NAG NB 7 .   ? -6.286  36.715  138.995 1.00 299.59 ?  902 NAG B C8  1 
HETATM 23137 N N2  . NAG NB 7 .   ? -4.776  35.350  137.706 1.00 285.67 ?  902 NAG B N2  1 
HETATM 23138 O O3  . NAG NB 7 .   ? -3.678  36.065  135.170 1.00 300.26 ?  902 NAG B O3  1 
HETATM 23139 O O4  . NAG NB 7 .   ? -2.166  33.955  133.840 1.00 272.26 ?  902 NAG B O4  1 
HETATM 23140 O O5  . NAG NB 7 .   ? -1.895  33.053  137.383 1.00 267.74 ?  902 NAG B O5  1 
HETATM 23141 O O6  . NAG NB 7 .   ? -0.380  31.081  135.164 1.00 262.57 ?  902 NAG B O6  1 
HETATM 23142 O O7  . NAG NB 7 .   ? -3.905  36.858  139.124 1.00 274.66 ?  902 NAG B O7  1 
HETATM 23143 C C1  . NAG OB 7 .   ? -13.543 30.474  159.483 1.00 239.49 ?  903 NAG B C1  1 
HETATM 23144 C C2  . NAG OB 7 .   ? -13.194 31.807  158.833 1.00 255.14 ?  903 NAG B C2  1 
HETATM 23145 C C3  . NAG OB 7 .   ? -13.263 32.931  159.862 1.00 270.87 ?  903 NAG B C3  1 
HETATM 23146 C C4  . NAG OB 7 .   ? -14.605 32.915  160.582 1.00 282.86 ?  903 NAG B C4  1 
HETATM 23147 C C5  . NAG OB 7 .   ? -14.890 31.524  161.141 1.00 279.61 ?  903 NAG B C5  1 
HETATM 23148 C C6  . NAG OB 7 .   ? -16.267 31.395  161.749 1.00 295.29 ?  903 NAG B C6  1 
HETATM 23149 C C7  . NAG OB 7 .   ? -11.541 32.458  157.136 1.00 244.45 ?  903 NAG B C7  1 
HETATM 23150 C C8  . NAG OB 7 .   ? -10.139 32.273  156.640 1.00 230.43 ?  903 NAG B C8  1 
HETATM 23151 N N2  . NAG OB 7 .   ? -11.877 31.752  158.220 1.00 246.68 ?  903 NAG B N2  1 
HETATM 23152 O O3  . NAG OB 7 .   ? -13.077 34.179  159.204 1.00 278.20 ?  903 NAG B O3  1 
HETATM 23153 O O4  . NAG OB 7 .   ? -14.595 33.853  161.651 1.00 291.46 ?  903 NAG B O4  1 
HETATM 23154 O O5  . NAG OB 7 .   ? -14.819 30.556  160.086 1.00 262.26 ?  903 NAG B O5  1 
HETATM 23155 O O6  . NAG OB 7 .   ? -16.859 30.145  161.420 1.00 292.82 ?  903 NAG B O6  1 
HETATM 23156 O O7  . NAG OB 7 .   ? -12.332 33.216  156.583 1.00 256.79 ?  903 NAG B O7  1 
HETATM 23157 C C1  . NAG PB 7 .   ? 90.825  78.256  296.946 1.00 185.09 ?  901 NAG C C1  1 
HETATM 23158 C C2  . NAG PB 7 .   ? 91.154  77.092  297.897 1.00 177.66 ?  901 NAG C C2  1 
HETATM 23159 C C3  . NAG PB 7 .   ? 90.056  76.943  298.951 1.00 188.74 ?  901 NAG C C3  1 
HETATM 23160 C C4  . NAG PB 7 .   ? 89.769  78.269  299.644 1.00 186.80 ?  901 NAG C C4  1 
HETATM 23161 C C5  . NAG PB 7 .   ? 89.499  79.358  298.609 1.00 194.43 ?  901 NAG C C5  1 
HETATM 23162 C C6  . NAG PB 7 .   ? 89.345  80.729  299.227 1.00 194.71 ?  901 NAG C C6  1 
HETATM 23163 C C7  . NAG PB 7 .   ? 92.518  75.328  296.864 1.00 180.43 ?  901 NAG C C7  1 
HETATM 23164 C C8  . NAG PB 7 .   ? 92.497  74.014  296.144 1.00 178.80 ?  901 NAG C C8  1 
HETATM 23165 N N2  . NAG PB 7 .   ? 91.324  75.841  297.178 1.00 180.41 ?  901 NAG C N2  1 
HETATM 23166 O O3  . NAG PB 7 .   ? 90.465  75.977  299.914 1.00 200.03 ?  901 NAG C O3  1 
HETATM 23167 O O4  . NAG PB 7 .   ? 88.586  78.109  300.419 1.00 200.21 ?  901 NAG C O4  1 
HETATM 23168 O O5  . NAG PB 7 .   ? 90.609  79.449  297.706 1.00 195.73 ?  901 NAG C O5  1 
HETATM 23169 O O6  . NAG PB 7 .   ? 90.595  81.400  299.323 1.00 185.86 ?  901 NAG C O6  1 
HETATM 23170 O O7  . NAG PB 7 .   ? 93.566  75.904  297.139 1.00 185.34 ?  901 NAG C O7  1 
HETATM 23171 C C1  . NAG QB 7 .   ? 88.879  78.113  301.831 1.00 179.00 ?  902 NAG C C1  1 
HETATM 23172 C C2  . NAG QB 7 .   ? 87.552  78.017  302.617 1.00 181.94 ?  902 NAG C C2  1 
HETATM 23173 C C3  . NAG QB 7 .   ? 87.810  77.977  304.128 1.00 188.00 ?  902 NAG C C3  1 
HETATM 23174 C C4  . NAG QB 7 .   ? 88.827  76.897  304.469 1.00 192.15 ?  902 NAG C C4  1 
HETATM 23175 C C5  . NAG QB 7 .   ? 90.084  77.056  303.622 1.00 188.31 ?  902 NAG C C5  1 
HETATM 23176 C C6  . NAG QB 7 .   ? 91.081  75.944  303.870 1.00 199.88 ?  902 NAG C C6  1 
HETATM 23177 C C7  . NAG QB 7 .   ? 86.618  80.373  302.369 1.00 179.08 ?  902 NAG C C7  1 
HETATM 23178 C C8  . NAG QB 7 .   ? 87.862  80.972  302.974 1.00 173.50 ?  902 NAG C C8  1 
HETATM 23179 N N2  . NAG QB 7 .   ? 86.559  79.029  302.246 1.00 182.33 ?  902 NAG C N2  1 
HETATM 23180 O O3  . NAG QB 7 .   ? 86.594  77.718  304.821 1.00 195.57 ?  902 NAG C O3  1 
HETATM 23181 O O4  . NAG QB 7 .   ? 89.338  77.176  305.762 1.00 196.90 ?  902 NAG C O4  1 
HETATM 23182 O O5  . NAG QB 7 .   ? 89.755  77.027  302.227 1.00 175.48 ?  902 NAG C O5  1 
HETATM 23183 O O6  . NAG QB 7 .   ? 92.379  76.256  303.386 1.00 202.56 ?  902 NAG C O6  1 
HETATM 23184 O O7  . NAG QB 7 .   ? 85.685  81.085  302.002 1.00 188.17 ?  902 NAG C O7  1 
HETATM 23185 C C1  . BMA RB 8 .   ? 88.824  76.543  306.903 1.00 200.58 ?  903 BMA C C1  1 
HETATM 23186 C C2  . BMA RB 8 .   ? 89.998  76.825  307.775 1.00 200.34 ?  903 BMA C C2  1 
HETATM 23187 C C3  . BMA RB 8 .   ? 89.706  76.504  309.222 1.00 196.84 ?  903 BMA C C3  1 
HETATM 23188 C C4  . BMA RB 8 .   ? 88.431  77.187  309.651 1.00 205.74 ?  903 BMA C C4  1 
HETATM 23189 C C5  . BMA RB 8 .   ? 87.300  76.792  308.671 1.00 216.98 ?  903 BMA C C5  1 
HETATM 23190 C C6  . BMA RB 8 .   ? 85.970  77.417  309.002 1.00 231.21 ?  903 BMA C C6  1 
HETATM 23191 O O2  . BMA RB 8 .   ? 90.329  78.237  307.759 1.00 208.60 ?  903 BMA C O2  1 
HETATM 23192 O O3  . BMA RB 8 .   ? 90.783  76.894  310.013 1.00 192.34 ?  903 BMA C O3  1 
HETATM 23193 O O4  . BMA RB 8 .   ? 88.058  76.821  310.973 1.00 208.58 ?  903 BMA C O4  1 
HETATM 23194 O O5  . BMA RB 8 .   ? 87.717  77.193  307.361 1.00 208.14 ?  903 BMA C O5  1 
HETATM 23195 O O6  . BMA RB 8 .   ? 86.466  78.365  309.890 1.00 233.42 ?  903 BMA C O6  1 
HETATM 23196 C C1  . MAN SB 9 .   ? 91.666  75.972  310.621 1.00 197.11 ?  904 MAN C C1  1 
HETATM 23197 C C2  . MAN SB 9 .   ? 91.432  76.274  312.092 1.00 216.38 ?  904 MAN C C2  1 
HETATM 23198 C C3  . MAN SB 9 .   ? 92.001  77.657  312.473 1.00 211.06 ?  904 MAN C C3  1 
HETATM 23199 C C4  . MAN SB 9 .   ? 93.429  77.829  311.967 1.00 197.37 ?  904 MAN C C4  1 
HETATM 23200 C C5  . MAN SB 9 .   ? 93.429  77.627  310.451 1.00 199.13 ?  904 MAN C C5  1 
HETATM 23201 C C6  . MAN SB 9 .   ? 94.808  77.779  309.834 1.00 214.57 ?  904 MAN C C6  1 
HETATM 23202 O O2  . MAN SB 9 .   ? 92.128  75.363  312.925 1.00 212.72 ?  904 MAN C O2  1 
HETATM 23203 O O3  . MAN SB 9 .   ? 91.957  77.885  313.885 1.00 218.09 ?  904 MAN C O3  1 
HETATM 23204 O O4  . MAN SB 9 .   ? 93.901  79.139  312.279 1.00 199.79 ?  904 MAN C O4  1 
HETATM 23205 O O5  . MAN SB 9 .   ? 92.946  76.262  310.163 1.00 196.34 ?  904 MAN C O5  1 
HETATM 23206 O O6  . MAN SB 9 .   ? 94.662  77.833  308.419 1.00 231.95 ?  904 MAN C O6  1 
HETATM 23207 C C1  . MAN TB 9 .   ? 85.636  79.359  310.538 1.00 207.43 ?  905 MAN C C1  1 
HETATM 23208 C C2  . MAN TB 9 .   ? 84.595  78.592  311.514 1.00 215.87 ?  905 MAN C C2  1 
HETATM 23209 C C3  . MAN TB 9 .   ? 83.753  79.602  312.247 1.00 212.46 ?  905 MAN C C3  1 
HETATM 23210 C C4  . MAN TB 9 .   ? 84.185  81.026  311.794 1.00 208.47 ?  905 MAN C C4  1 
HETATM 23211 C C5  . MAN TB 9 .   ? 84.011  81.120  310.236 1.00 210.66 ?  905 MAN C C5  1 
HETATM 23212 C C6  . MAN TB 9 .   ? 84.323  82.468  309.629 1.00 205.66 ?  905 MAN C C6  1 
HETATM 23213 O O2  . MAN TB 9 .   ? 85.292  77.829  312.509 1.00 215.92 ?  905 MAN C O2  1 
HETATM 23214 O O3  . MAN TB 9 .   ? 84.015  79.450  313.631 1.00 215.00 ?  905 MAN C O3  1 
HETATM 23215 O O4  . MAN TB 9 .   ? 83.398  82.021  312.414 1.00 207.27 ?  905 MAN C O4  1 
HETATM 23216 O O5  . MAN TB 9 .   ? 84.982  80.277  309.613 1.00 213.06 ?  905 MAN C O5  1 
HETATM 23217 O O6  . MAN TB 9 .   ? 85.553  83.048  310.141 1.00 199.47 ?  905 MAN C O6  1 
HETATM 23218 C C1  . MAN UB 9 .   ? 85.989  83.947  309.067 1.00 225.12 ?  906 MAN C C1  1 
HETATM 23219 C C2  . MAN UB 9 .   ? 87.354  83.500  308.306 1.00 220.83 ?  906 MAN C C2  1 
HETATM 23220 C C3  . MAN UB 9 .   ? 88.602  83.834  309.158 1.00 225.35 ?  906 MAN C C3  1 
HETATM 23221 C C4  . MAN UB 9 .   ? 88.564  85.315  309.627 1.00 232.75 ?  906 MAN C C4  1 
HETATM 23222 C C5  . MAN UB 9 .   ? 87.269  85.610  310.399 1.00 232.33 ?  906 MAN C C5  1 
HETATM 23223 C C6  . MAN UB 9 .   ? 87.170  87.068  310.834 1.00 237.28 ?  906 MAN C C6  1 
HETATM 23224 O O2  . MAN UB 9 .   ? 87.512  84.192  307.037 1.00 221.28 ?  906 MAN C O2  1 
HETATM 23225 O O3  . MAN UB 9 .   ? 89.819  83.566  308.417 1.00 225.12 ?  906 MAN C O3  1 
HETATM 23226 O O4  . MAN UB 9 .   ? 89.691  85.598  310.481 1.00 239.12 ?  906 MAN C O4  1 
HETATM 23227 O O5  . MAN UB 9 .   ? 86.119  85.308  309.558 1.00 228.61 ?  906 MAN C O5  1 
HETATM 23228 O O6  . MAN UB 9 .   ? 86.224  87.110  311.883 1.00 240.66 ?  906 MAN C O6  1 
HETATM 23229 C C1  . MAN VB 9 .   ? 83.040  78.941  314.605 1.00 206.31 ?  907 MAN C C1  1 
HETATM 23230 C C2  . MAN VB 9 .   ? 83.336  77.363  314.864 1.00 205.37 ?  907 MAN C C2  1 
HETATM 23231 C C3  . MAN VB 9 .   ? 82.093  76.400  314.912 1.00 216.10 ?  907 MAN C C3  1 
HETATM 23232 C C4  . MAN VB 9 .   ? 81.046  77.024  315.807 1.00 225.24 ?  907 MAN C C4  1 
HETATM 23233 C C5  . MAN VB 9 .   ? 80.692  78.449  315.163 1.00 218.62 ?  907 MAN C C5  1 
HETATM 23234 C C6  . MAN VB 9 .   ? 79.709  79.387  315.904 1.00 216.13 ?  907 MAN C C6  1 
HETATM 23235 O O2  . MAN VB 9 .   ? 84.089  77.100  316.086 1.00 193.57 ?  907 MAN C O2  1 
HETATM 23236 O O3  . MAN VB 9 .   ? 82.396  75.063  315.302 1.00 214.22 ?  907 MAN C O3  1 
HETATM 23237 O O4  . MAN VB 9 .   ? 79.879  76.249  315.822 1.00 236.49 ?  907 MAN C O4  1 
HETATM 23238 O O5  . MAN VB 9 .   ? 81.688  79.123  314.258 1.00 213.55 ?  907 MAN C O5  1 
HETATM 23239 O O6  . MAN VB 9 .   ? 79.397  80.459  315.013 1.00 219.10 ?  907 MAN C O6  1 
HETATM 23240 C C1  . NAG WB 7 .   ? 93.303  72.326  222.616 1.00 232.59 ?  908 NAG C C1  1 
HETATM 23241 C C2  . NAG WB 7 .   ? 93.489  72.924  221.220 1.00 244.51 ?  908 NAG C C2  1 
HETATM 23242 C C3  . NAG WB 7 .   ? 93.055  74.387  221.209 1.00 250.35 ?  908 NAG C C3  1 
HETATM 23243 C C4  . NAG WB 7 .   ? 91.643  74.528  221.759 1.00 252.27 ?  908 NAG C C4  1 
HETATM 23244 C C5  . NAG WB 7 .   ? 91.553  73.870  223.133 1.00 256.37 ?  908 NAG C C5  1 
HETATM 23245 C C6  . NAG WB 7 .   ? 90.155  73.869  223.702 1.00 265.87 ?  908 NAG C C6  1 
HETATM 23246 C C7  . NAG WB 7 .   ? 95.382  71.669  220.288 1.00 244.44 ?  908 NAG C C7  1 
HETATM 23247 C C8  . NAG WB 7 .   ? 96.827  71.720  219.897 1.00 239.16 ?  908 NAG C C8  1 
HETATM 23248 N N2  . NAG WB 7 .   ? 94.871  72.799  220.787 1.00 249.03 ?  908 NAG C N2  1 
HETATM 23249 O O3  . NAG WB 7 .   ? 93.107  74.894  219.880 1.00 255.72 ?  908 NAG C O3  1 
HETATM 23250 O O4  . NAG WB 7 .   ? 91.309  75.907  221.861 1.00 257.53 ?  908 NAG C O4  1 
HETATM 23251 O O5  . NAG WB 7 .   ? 91.953  72.496  223.036 1.00 246.66 ?  908 NAG C O5  1 
HETATM 23252 O O6  . NAG WB 7 .   ? 89.633  75.188  223.780 1.00 272.25 ?  908 NAG C O6  1 
HETATM 23253 O O7  . NAG WB 7 .   ? 94.709  70.650  220.162 1.00 243.97 ?  908 NAG C O7  1 
HETATM 23254 C C1  . NAG XB 7 .   ? 83.101  63.818  220.894 1.00 220.08 ?  909 NAG C C1  1 
HETATM 23255 C C2  . NAG XB 7 .   ? 81.809  63.112  221.274 1.00 225.81 ?  909 NAG C C2  1 
HETATM 23256 C C3  . NAG XB 7 .   ? 80.650  63.666  220.444 1.00 238.89 ?  909 NAG C C3  1 
HETATM 23257 C C4  . NAG XB 7 .   ? 80.596  65.189  220.524 1.00 241.65 ?  909 NAG C C4  1 
HETATM 23258 C C5  . NAG XB 7 .   ? 81.965  65.820  220.270 1.00 233.13 ?  909 NAG C C5  1 
HETATM 23259 C C6  . NAG XB 7 .   ? 81.990  67.298  220.582 1.00 243.52 ?  909 NAG C C6  1 
HETATM 23260 C C7  . NAG XB 7 .   ? 82.473  60.863  222.015 1.00 202.25 ?  909 NAG C C7  1 
HETATM 23261 C C8  . NAG XB 7 .   ? 82.497  59.404  221.672 1.00 206.02 ?  909 NAG C C8  1 
HETATM 23262 N N2  . NAG XB 7 .   ? 81.921  61.671  221.103 1.00 210.65 ?  909 NAG C N2  1 
HETATM 23263 O O3  . NAG XB 7 .   ? 79.421  63.118  220.906 1.00 244.42 ?  909 NAG C O3  1 
HETATM 23264 O O4  . NAG XB 7 .   ? 79.675  65.702  219.568 1.00 250.52 ?  909 NAG C O4  1 
HETATM 23265 O O5  . NAG XB 7 .   ? 82.957  65.209  221.107 1.00 223.90 ?  909 NAG C O5  1 
HETATM 23266 O O6  . NAG XB 7 .   ? 82.212  68.075  219.413 1.00 254.60 ?  909 NAG C O6  1 
HETATM 23267 O O7  . NAG XB 7 .   ? 82.936  61.290  223.068 1.00 197.06 ?  909 NAG C O7  1 
HETATM 23268 C C1  . NAG YB 7 .   ? 101.722 62.289  223.932 1.00 176.29 ?  910 NAG C C1  1 
HETATM 23269 C C2  . NAG YB 7 .   ? 100.810 61.064  223.904 1.00 177.66 ?  910 NAG C C2  1 
HETATM 23270 C C3  . NAG YB 7 .   ? 101.633 59.802  223.642 1.00 193.94 ?  910 NAG C C3  1 
HETATM 23271 C C4  . NAG YB 7 .   ? 102.519 59.972  222.411 1.00 201.16 ?  910 NAG C C4  1 
HETATM 23272 C C5  . NAG YB 7 .   ? 103.312 61.279  222.484 1.00 204.75 ?  910 NAG C C5  1 
HETATM 23273 C C6  . NAG YB 7 .   ? 104.072 61.584  221.213 1.00 211.46 ?  910 NAG C C6  1 
HETATM 23274 C C7  . NAG YB 7 .   ? 98.925  61.613  225.377 1.00 165.88 ?  910 NAG C C7  1 
HETATM 23275 C C8  . NAG YB 7 .   ? 98.271  61.355  226.700 1.00 152.66 ?  910 NAG C C8  1 
HETATM 23276 N N2  . NAG YB 7 .   ? 100.053 60.935  225.139 1.00 165.40 ?  910 NAG C N2  1 
HETATM 23277 O O3  . NAG YB 7 .   ? 100.763 58.689  223.467 1.00 199.94 ?  910 NAG C O3  1 
HETATM 23278 O O4  . NAG YB 7 .   ? 103.427 58.878  222.334 1.00 207.70 ?  910 NAG C O4  1 
HETATM 23279 O O5  . NAG YB 7 .   ? 102.423 62.385  222.701 1.00 195.98 ?  910 NAG C O5  1 
HETATM 23280 O O6  . NAG YB 7 .   ? 105.316 62.212  221.490 1.00 215.52 ?  910 NAG C O6  1 
HETATM 23281 O O7  . NAG YB 7 .   ? 98.459  62.405  224.566 1.00 189.69 ?  910 NAG C O7  1 
HETATM 23282 C C1  . NAG ZB 7 .   ? 103.224 58.163  221.093 1.00 215.06 ?  911 NAG C C1  1 
HETATM 23283 C C2  . NAG ZB 7 .   ? 104.392 57.199  220.882 1.00 219.31 ?  911 NAG C C2  1 
HETATM 23284 C C3  . NAG ZB 7 .   ? 104.197 56.416  219.588 1.00 227.45 ?  911 NAG C C3  1 
HETATM 23285 C C4  . NAG ZB 7 .   ? 102.830 55.745  219.570 1.00 230.06 ?  911 NAG C C4  1 
HETATM 23286 C C5  . NAG ZB 7 .   ? 101.727 56.760  219.867 1.00 220.75 ?  911 NAG C C5  1 
HETATM 23287 C C6  . NAG ZB 7 .   ? 100.365 56.120  220.011 1.00 212.08 ?  911 NAG C C6  1 
HETATM 23288 C C7  . NAG ZB 7 .   ? 106.520 57.881  221.888 1.00 223.77 ?  911 NAG C C7  1 
HETATM 23289 C C8  . NAG ZB 7 .   ? 107.783 58.667  221.705 1.00 227.66 ?  911 NAG C C8  1 
HETATM 23290 N N2  . NAG ZB 7 .   ? 105.661 57.907  220.865 1.00 217.93 ?  911 NAG C N2  1 
HETATM 23291 O O3  . NAG ZB 7 .   ? 105.222 55.434  219.472 1.00 230.03 ?  911 NAG C O3  1 
HETATM 23292 O O4  . NAG ZB 7 .   ? 102.593 55.177  218.286 1.00 238.81 ?  911 NAG C O4  1 
HETATM 23293 O O5  . NAG ZB 7 .   ? 101.996 57.428  221.108 1.00 218.17 ?  911 NAG C O5  1 
HETATM 23294 O O6  . NAG ZB 7 .   ? 99.383  56.802  219.243 1.00 206.30 ?  911 NAG C O6  1 
HETATM 23295 O O7  . NAG ZB 7 .   ? 106.287 57.252  222.916 1.00 225.41 ?  911 NAG C O7  1 
HETATM 23296 C C1  . BMA AC 8 .   ? 102.566 53.740  218.419 1.00 251.86 ?  912 BMA C C1  1 
HETATM 23297 C C2  . BMA AC 8 .   ? 101.602 53.165  217.344 1.00 255.82 ?  912 BMA C C2  1 
HETATM 23298 C C3  . BMA AC 8 .   ? 101.689 51.639  217.313 1.00 251.78 ?  912 BMA C C3  1 
HETATM 23299 C C4  . BMA AC 8 .   ? 103.156 51.168  217.266 1.00 254.07 ?  912 BMA C C4  1 
HETATM 23300 C C5  . BMA AC 8 .   ? 103.963 51.810  218.421 1.00 253.08 ?  912 BMA C C5  1 
HETATM 23301 C C6  . BMA AC 8 .   ? 105.437 51.439  218.421 1.00 263.64 ?  912 BMA C C6  1 
HETATM 23302 O O2  . BMA AC 8 .   ? 101.958 53.618  216.053 1.00 257.76 ?  912 BMA C O2  1 
HETATM 23303 O O3  . BMA AC 8 .   ? 100.950 51.096  216.208 1.00 245.34 ?  912 BMA C O3  1 
HETATM 23304 O O4  . BMA AC 8 .   ? 103.211 49.763  217.378 1.00 257.99 ?  912 BMA C O4  1 
HETATM 23305 O O5  . BMA AC 8 .   ? 103.882 53.224  218.291 1.00 248.80 ?  912 BMA C O5  1 
HETATM 23306 O O6  . BMA AC 8 .   ? 105.678 50.455  217.442 1.00 273.72 ?  912 BMA C O6  1 
HETATM 23307 C C1  . MAN BC 9 .   ? 99.613  50.801  216.683 1.00 240.19 ?  913 MAN C C1  1 
HETATM 23308 C C2  . MAN BC 9 .   ? 99.095  49.515  215.965 1.00 242.32 ?  913 MAN C C2  1 
HETATM 23309 C C3  . MAN BC 9 .   ? 98.692  49.819  214.522 1.00 242.66 ?  913 MAN C C3  1 
HETATM 23310 C C4  . MAN BC 9 .   ? 97.778  51.054  214.447 1.00 243.57 ?  913 MAN C C4  1 
HETATM 23311 C C5  . MAN BC 9 .   ? 98.460  52.249  215.105 1.00 238.86 ?  913 MAN C C5  1 
HETATM 23312 C C6  . MAN BC 9 .   ? 97.601  53.503  215.093 1.00 232.26 ?  913 MAN C C6  1 
HETATM 23313 O O2  . MAN BC 9 .   ? 97.928  48.997  216.604 1.00 246.68 ?  913 MAN C O2  1 
HETATM 23314 O O3  . MAN BC 9 .   ? 98.057  48.702  213.921 1.00 246.40 ?  913 MAN C O3  1 
HETATM 23315 O O4  . MAN BC 9 .   ? 97.494  51.368  213.098 1.00 246.55 ?  913 MAN C O4  1 
HETATM 23316 O O5  . MAN BC 9 .   ? 98.734  51.918  216.477 1.00 240.04 ?  913 MAN C O5  1 
HETATM 23317 O O6  . MAN BC 9 .   ? 97.282  53.818  213.741 1.00 229.76 ?  913 MAN C O6  1 
HETATM 23318 C C1  . MAN CC 9 .   ? 106.426 49.409  218.097 1.00 295.36 ?  914 MAN C C1  1 
HETATM 23319 C C2  . MAN CC 9 .   ? 107.934 49.821  218.086 1.00 295.90 ?  914 MAN C C2  1 
HETATM 23320 C C3  . MAN CC 9 .   ? 108.540 49.643  216.693 1.00 294.09 ?  914 MAN C C3  1 
HETATM 23321 C C4  . MAN CC 9 .   ? 108.196 48.264  216.111 1.00 294.58 ?  914 MAN C C4  1 
HETATM 23322 C C5  . MAN CC 9 .   ? 106.673 48.078  216.097 1.00 294.65 ?  914 MAN C C5  1 
HETATM 23323 C C6  . MAN CC 9 .   ? 106.243 46.731  215.551 1.00 293.08 ?  914 MAN C C6  1 
HETATM 23324 O O2  . MAN CC 9 .   ? 108.710 48.998  218.961 1.00 297.73 ?  914 MAN C O2  1 
HETATM 23325 O O3  . MAN CC 9 .   ? 109.953 49.830  216.707 1.00 292.99 ?  914 MAN C O3  1 
HETATM 23326 O O4  . MAN CC 9 .   ? 108.696 48.158  214.790 1.00 294.59 ?  914 MAN C O4  1 
HETATM 23327 O O5  . MAN CC 9 .   ? 106.186 48.172  217.446 1.00 295.35 ?  914 MAN C O5  1 
HETATM 23328 O O6  . MAN CC 9 .   ? 104.840 46.783  215.309 1.00 291.39 ?  914 MAN C O6  1 
HETATM 23329 C C1  . NAG DC 7 .   ? 115.618 68.728  220.407 1.00 174.65 ?  915 NAG C C1  1 
HETATM 23330 C C2  . NAG DC 7 .   ? 114.602 69.628  219.701 1.00 187.35 ?  915 NAG C C2  1 
HETATM 23331 C C3  . NAG DC 7 .   ? 114.693 69.452  218.187 1.00 198.20 ?  915 NAG C C3  1 
HETATM 23332 C C4  . NAG DC 7 .   ? 116.127 69.638  217.708 1.00 206.42 ?  915 NAG C C4  1 
HETATM 23333 C C5  . NAG DC 7 .   ? 117.055 68.712  218.490 1.00 201.41 ?  915 NAG C C5  1 
HETATM 23334 C C6  . NAG DC 7 .   ? 118.515 68.903  218.150 1.00 206.04 ?  915 NAG C C6  1 
HETATM 23335 C C7  . NAG DC 7 .   ? 112.574 70.158  220.982 1.00 192.51 ?  915 NAG C C7  1 
HETATM 23336 C C8  . NAG DC 7 .   ? 113.283 71.408  221.410 1.00 204.26 ?  915 NAG C C8  1 
HETATM 23337 N N2  . NAG DC 7 .   ? 113.254 69.348  220.165 1.00 187.97 ?  915 NAG C N2  1 
HETATM 23338 O O3  . NAG DC 7 .   ? 113.821 70.383  217.555 1.00 203.04 ?  915 NAG C O3  1 
HETATM 23339 O O4  . NAG DC 7 .   ? 116.217 69.314  216.325 1.00 219.17 ?  915 NAG C O4  1 
HETATM 23340 O O5  . NAG DC 7 .   ? 116.925 68.982  219.892 1.00 191.27 ?  915 NAG C O5  1 
HETATM 23341 O O6  . NAG DC 7 .   ? 119.179 67.659  217.977 1.00 206.36 ?  915 NAG C O6  1 
HETATM 23342 O O7  . NAG DC 7 .   ? 111.439 69.894  221.360 1.00 181.69 ?  915 NAG C O7  1 
HETATM 23343 C C1  . NAG EC 7 .   ? 116.601 70.491  215.580 1.00 247.91 ?  916 NAG C C1  1 
HETATM 23344 C C2  . NAG EC 7 .   ? 116.896 70.102  214.116 1.00 234.90 ?  916 NAG C C2  1 
HETATM 23345 C C3  . NAG EC 7 .   ? 117.233 71.336  213.268 1.00 237.06 ?  916 NAG C C3  1 
HETATM 23346 C C4  . NAG EC 7 .   ? 116.168 72.412  213.442 1.00 240.24 ?  916 NAG C C4  1 
HETATM 23347 C C5  . NAG EC 7 .   ? 115.948 72.709  214.925 1.00 245.25 ?  916 NAG C C5  1 
HETATM 23348 C C6  . NAG EC 7 .   ? 114.849 73.716  215.181 1.00 237.31 ?  916 NAG C C6  1 
HETATM 23349 C C7  . NAG EC 7 .   ? 119.201 69.042  214.322 1.00 226.85 ?  916 NAG C C7  1 
HETATM 23350 C C8  . NAG EC 7 .   ? 119.759 70.290  214.955 1.00 224.67 ?  916 NAG C C8  1 
HETATM 23351 N N2  . NAG EC 7 .   ? 117.896 69.040  213.971 1.00 227.92 ?  916 NAG C N2  1 
HETATM 23352 O O3  . NAG EC 7 .   ? 117.316 70.961  211.899 1.00 240.15 ?  916 NAG C O3  1 
HETATM 23353 O O4  . NAG EC 7 .   ? 116.564 73.600  212.764 1.00 244.78 ?  916 NAG C O4  1 
HETATM 23354 O O5  . NAG EC 7 .   ? 115.576 71.505  215.613 1.00 255.80 ?  916 NAG C O5  1 
HETATM 23355 O O6  . NAG EC 7 .   ? 114.303 73.564  216.484 1.00 231.89 ?  916 NAG C O6  1 
HETATM 23356 O O7  . NAG EC 7 .   ? 119.909 68.056  214.131 1.00 230.82 ?  916 NAG C O7  1 
HETATM 23357 C C1  . NAG FC 7 .   ? 107.199 85.231  235.149 1.00 160.52 ?  917 NAG C C1  1 
HETATM 23358 C C2  . NAG FC 7 .   ? 106.972 86.735  235.287 1.00 177.19 ?  917 NAG C C2  1 
HETATM 23359 C C3  . NAG FC 7 .   ? 105.565 87.010  235.807 1.00 199.86 ?  917 NAG C C3  1 
HETATM 23360 C C4  . NAG FC 7 .   ? 104.531 86.316  234.929 1.00 213.19 ?  917 NAG C C4  1 
HETATM 23361 C C5  . NAG FC 7 .   ? 104.864 84.831  234.788 1.00 204.99 ?  917 NAG C C5  1 
HETATM 23362 C C6  . NAG FC 7 .   ? 103.954 84.113  233.818 1.00 201.66 ?  917 NAG C C6  1 
HETATM 23363 C C7  . NAG FC 7 .   ? 108.944 88.139  235.676 1.00 187.91 ?  917 NAG C C7  1 
HETATM 23364 C C8  . NAG FC 7 .   ? 108.952 88.366  234.192 1.00 192.45 ?  917 NAG C C8  1 
HETATM 23365 N N2  . NAG FC 7 .   ? 107.971 87.349  236.144 1.00 180.64 ?  917 NAG C N2  1 
HETATM 23366 O O3  . NAG FC 7 .   ? 105.337 88.415  235.838 1.00 209.73 ?  917 NAG C O3  1 
HETATM 23367 O O4  . NAG FC 7 .   ? 103.236 86.446  235.504 1.00 228.61 ?  917 NAG C O4  1 
HETATM 23368 O O5  . NAG FC 7 .   ? 106.200 84.674  234.288 1.00 190.16 ?  917 NAG C O5  1 
HETATM 23369 O O6  . NAG FC 7 .   ? 104.249 84.458  232.472 1.00 197.20 ?  917 NAG C O6  1 
HETATM 23370 O O7  . NAG FC 7 .   ? 109.780 88.647  236.415 1.00 193.65 ?  917 NAG C O7  1 
HETATM 23371 C C1  . NAG GC 7 .   ? 102.485 87.416  234.749 1.00 235.22 ?  918 NAG C C1  1 
HETATM 23372 C C2  . NAG GC 7 .   ? 101.032 86.947  234.633 1.00 239.36 ?  918 NAG C C2  1 
HETATM 23373 C C3  . NAG GC 7 .   ? 100.202 87.988  233.881 1.00 248.60 ?  918 NAG C C3  1 
HETATM 23374 C C4  . NAG GC 7 .   ? 100.355 89.361  234.525 1.00 256.21 ?  918 NAG C C4  1 
HETATM 23375 C C5  . NAG GC 7 .   ? 101.832 89.730  234.643 1.00 252.74 ?  918 NAG C C5  1 
HETATM 23376 C C6  . NAG GC 7 .   ? 102.058 91.031  235.379 1.00 257.31 ?  918 NAG C C6  1 
HETATM 23377 C C7  . NAG GC 7 .   ? 100.307 84.597  234.491 1.00 229.48 ?  918 NAG C C7  1 
HETATM 23378 C C8  . NAG GC 7 .   ? 100.328 83.344  233.665 1.00 230.06 ?  918 NAG C C8  1 
HETATM 23379 N N2  . NAG GC 7 .   ? 100.949 85.652  233.973 1.00 234.10 ?  918 NAG C N2  1 
HETATM 23380 O O3  . NAG GC 7 .   ? 98.834  87.597  233.891 1.00 247.50 ?  918 NAG C O3  1 
HETATM 23381 O O4  . NAG GC 7 .   ? 99.685  90.351  233.753 1.00 263.14 ?  918 NAG C O4  1 
HETATM 23382 O O5  . NAG GC 7 .   ? 102.527 88.711  235.378 1.00 242.56 ?  918 NAG C O5  1 
HETATM 23383 O O6  . NAG GC 7 .   ? 101.877 92.155  234.528 1.00 261.70 ?  918 NAG C O6  1 
HETATM 23384 O O7  . NAG GC 7 .   ? 99.736  84.649  235.576 1.00 224.85 ?  918 NAG C O7  1 
HETATM 23385 C C1  . NAG HC 7 .   ? 86.793  88.037  274.578 1.00 216.15 ?  919 NAG C C1  1 
HETATM 23386 C C2  . NAG HC 7 .   ? 86.595  89.442  274.005 1.00 230.16 ?  919 NAG C C2  1 
HETATM 23387 C C3  . NAG HC 7 .   ? 86.792  90.487  275.099 1.00 230.60 ?  919 NAG C C3  1 
HETATM 23388 C C4  . NAG HC 7 .   ? 85.885  90.186  276.287 1.00 238.58 ?  919 NAG C C4  1 
HETATM 23389 C C5  . NAG HC 7 .   ? 86.108  88.751  276.765 1.00 227.85 ?  919 NAG C C5  1 
HETATM 23390 C C6  . NAG HC 7 .   ? 85.170  88.337  277.877 1.00 237.17 ?  919 NAG C C6  1 
HETATM 23391 C C7  . NAG HC 7 .   ? 87.088  89.842  271.634 1.00 235.07 ?  919 NAG C C7  1 
HETATM 23392 C C8  . NAG HC 7 .   ? 88.158  90.097  270.619 1.00 230.85 ?  919 NAG C C8  1 
HETATM 23393 N N2  . NAG HC 7 .   ? 87.502  89.691  272.896 1.00 233.79 ?  919 NAG C N2  1 
HETATM 23394 O O3  . NAG HC 7 .   ? 86.515  91.781  274.573 1.00 236.58 ?  919 NAG C O3  1 
HETATM 23395 O O4  . NAG HC 7 .   ? 86.148  91.091  277.354 1.00 258.71 ?  919 NAG C O4  1 
HETATM 23396 O O5  . NAG HC 7 .   ? 85.896  87.835  275.679 1.00 222.38 ?  919 NAG C O5  1 
HETATM 23397 O O6  . NAG HC 7 .   ? 85.844  87.585  278.878 1.00 245.00 ?  919 NAG C O6  1 
HETATM 23398 O O7  . NAG HC 7 .   ? 85.902  89.774  271.327 1.00 236.47 ?  919 NAG C O7  1 
HETATM 23399 C C1  . NAG IC 7 .   ? 85.010  91.963  277.532 1.00 268.00 ?  920 NAG C C1  1 
HETATM 23400 C C2  . NAG IC 7 .   ? 85.274  92.904  278.712 1.00 270.01 ?  920 NAG C C2  1 
HETATM 23401 C C3  . NAG IC 7 .   ? 84.100  93.866  278.889 1.00 274.99 ?  920 NAG C C3  1 
HETATM 23402 C C4  . NAG IC 7 .   ? 83.797  94.587  277.580 1.00 276.10 ?  920 NAG C C4  1 
HETATM 23403 C C5  . NAG IC 7 .   ? 83.599  93.577  276.451 1.00 273.95 ?  920 NAG C C5  1 
HETATM 23404 C C6  . NAG IC 7 .   ? 83.404  94.222  275.097 1.00 274.47 ?  920 NAG C C6  1 
HETATM 23405 C C7  . NAG IC 7 .   ? 86.700  92.110  280.553 1.00 264.33 ?  920 NAG C C7  1 
HETATM 23406 C C8  . NAG IC 7 .   ? 86.761  91.285  281.804 1.00 263.74 ?  920 NAG C C8  1 
HETATM 23407 N N2  . NAG IC 7 .   ? 85.512  92.156  279.937 1.00 265.97 ?  920 NAG C N2  1 
HETATM 23408 O O3  . NAG IC 7 .   ? 84.421  94.809  279.905 1.00 276.27 ?  920 NAG C O3  1 
HETATM 23409 O O4  . NAG IC 7 .   ? 82.621  95.377  277.716 1.00 279.76 ?  920 NAG C O4  1 
HETATM 23410 O O5  . NAG IC 7 .   ? 84.757  92.735  276.346 1.00 274.13 ?  920 NAG C O5  1 
HETATM 23411 O O6  . NAG IC 7 .   ? 83.602  93.294  274.038 1.00 275.04 ?  920 NAG C O6  1 
HETATM 23412 O O7  . NAG IC 7 .   ? 87.682  92.706  280.119 1.00 262.88 ?  920 NAG C O7  1 
HETATM 23413 C C1  . NAG JC 7 .   ? 92.686  64.425  257.570 1.00 157.87 ?  921 NAG C C1  1 
HETATM 23414 C C2  . NAG JC 7 .   ? 93.742  64.371  256.459 1.00 150.14 ?  921 NAG C C2  1 
HETATM 23415 C C3  . NAG JC 7 .   ? 93.575  63.100  255.621 1.00 159.85 ?  921 NAG C C3  1 
HETATM 23416 C C4  . NAG JC 7 .   ? 93.583  61.867  256.518 1.00 173.16 ?  921 NAG C C4  1 
HETATM 23417 C C5  . NAG JC 7 .   ? 92.516  62.011  257.600 1.00 177.05 ?  921 NAG C C5  1 
HETATM 23418 C C6  . NAG JC 7 .   ? 92.548  60.869  258.589 1.00 186.82 ?  921 NAG C C6  1 
HETATM 23419 C C7  . NAG JC 7 .   ? 94.817  66.175  255.209 1.00 168.11 ?  921 NAG C C7  1 
HETATM 23420 C C8  . NAG JC 7 .   ? 94.617  67.382  254.346 1.00 160.01 ?  921 NAG C C8  1 
HETATM 23421 N N2  . NAG JC 7 .   ? 93.706  65.554  255.617 1.00 161.42 ?  921 NAG C N2  1 
HETATM 23422 O O3  . NAG JC 7 .   ? 94.615  63.025  254.653 1.00 167.94 ?  921 NAG C O3  1 
HETATM 23423 O O4  . NAG JC 7 .   ? 93.310  60.692  255.759 1.00 184.83 ?  921 NAG C O4  1 
HETATM 23424 O O5  . NAG JC 7 .   ? 92.755  63.209  258.356 1.00 174.11 ?  921 NAG C O5  1 
HETATM 23425 O O6  . NAG JC 7 .   ? 93.886  60.505  258.905 1.00 195.92 ?  921 NAG C O6  1 
HETATM 23426 O O7  . NAG JC 7 .   ? 95.935  65.778  255.525 1.00 179.54 ?  921 NAG C O7  1 
HETATM 23427 C C1  . NAG KC 7 .   ? 94.538  60.011  255.394 1.00 197.59 ?  922 NAG C C1  1 
HETATM 23428 C C2  . NAG KC 7 .   ? 94.436  58.526  255.738 1.00 200.39 ?  922 NAG C C2  1 
HETATM 23429 C C3  . NAG KC 7 .   ? 95.723  57.807  255.334 1.00 211.18 ?  922 NAG C C3  1 
HETATM 23430 C C4  . NAG KC 7 .   ? 96.088  58.099  253.883 1.00 215.59 ?  922 NAG C C4  1 
HETATM 23431 C C5  . NAG KC 7 .   ? 96.051  59.603  253.600 1.00 209.68 ?  922 NAG C C5  1 
HETATM 23432 C C6  . NAG KC 7 .   ? 96.225  59.933  252.135 1.00 210.47 ?  922 NAG C C6  1 
HETATM 23433 C C7  . NAG KC 7 .   ? 93.639  57.215  257.656 1.00 213.81 ?  922 NAG C C7  1 
HETATM 23434 C C8  . NAG KC 7 .   ? 93.437  57.190  259.142 1.00 215.82 ?  922 NAG C C8  1 
HETATM 23435 N N2  . NAG KC 7 .   ? 94.170  58.336  257.155 1.00 204.12 ?  922 NAG C N2  1 
HETATM 23436 O O3  . NAG KC 7 .   ? 95.570  56.403  255.509 1.00 221.17 ?  922 NAG C O3  1 
HETATM 23437 O O4  . NAG KC 7 .   ? 97.417  57.636  253.662 1.00 229.73 ?  922 NAG C O4  1 
HETATM 23438 O O5  . NAG KC 7 .   ? 94.788  60.157  253.997 1.00 204.62 ?  922 NAG C O5  1 
HETATM 23439 O O6  . NAG KC 7 .   ? 96.527  61.309  251.947 1.00 210.09 ?  922 NAG C O6  1 
HETATM 23440 O O7  . NAG KC 7 .   ? 93.335  56.264  256.942 1.00 219.68 ?  922 NAG C O7  1 
HETATM 23441 C C1  . BMA LC 8 .   ? 97.543  56.651  252.609 1.00 238.66 ?  923 BMA C C1  1 
HETATM 23442 C C2  . BMA LC 8 .   ? 98.992  56.113  252.704 1.00 241.63 ?  923 BMA C C2  1 
HETATM 23443 C C3  . BMA LC 8 .   ? 99.227  55.012  251.666 1.00 243.21 ?  923 BMA C C3  1 
HETATM 23444 C C4  . BMA LC 8 .   ? 98.114  53.952  251.726 1.00 246.54 ?  923 BMA C C4  1 
HETATM 23445 C C5  . BMA LC 8 .   ? 96.721  54.612  251.657 1.00 248.84 ?  923 BMA C C5  1 
HETATM 23446 C C6  . BMA LC 8 .   ? 95.597  53.610  251.801 1.00 259.22 ?  923 BMA C C6  1 
HETATM 23447 O O2  . BMA LC 8 .   ? 99.233  55.526  253.977 1.00 241.02 ?  923 BMA C O2  1 
HETATM 23448 O O3  . BMA LC 8 .   ? 100.508 54.377  251.824 1.00 244.67 ?  923 BMA C O3  1 
HETATM 23449 O O4  . BMA LC 8 .   ? 98.252  53.034  250.654 1.00 246.79 ?  923 BMA C O4  1 
HETATM 23450 O O5  . BMA LC 8 .   ? 96.603  55.590  252.714 1.00 243.26 ?  923 BMA C O5  1 
HETATM 23451 O O6  . BMA LC 8 .   ? 95.817  52.870  252.988 1.00 266.33 ?  923 BMA C O6  1 
HETATM 23452 C C1  . MAN MC 9 .   ? 95.224  51.569  252.806 1.00 272.21 ?  924 MAN C C1  1 
HETATM 23453 C C2  . MAN MC 9 .   ? 93.809  51.638  253.442 1.00 271.39 ?  924 MAN C C2  1 
HETATM 23454 C C3  . MAN MC 9 .   ? 93.905  51.638  254.967 1.00 266.62 ?  924 MAN C C3  1 
HETATM 23455 C C4  . MAN MC 9 .   ? 94.802  50.494  255.454 1.00 267.17 ?  924 MAN C C4  1 
HETATM 23456 C C5  . MAN MC 9 .   ? 96.190  50.624  254.815 1.00 266.39 ?  924 MAN C C5  1 
HETATM 23457 C C6  . MAN MC 9 .   ? 97.137  49.511  255.228 1.00 255.58 ?  924 MAN C C6  1 
HETATM 23458 O O2  . MAN MC 9 .   ? 93.029  50.493  253.097 1.00 274.25 ?  924 MAN C O2  1 
HETATM 23459 O O3  . MAN MC 9 .   ? 92.619  51.549  255.576 1.00 264.78 ?  924 MAN C O3  1 
HETATM 23460 O O4  . MAN MC 9 .   ? 94.927  50.546  256.863 1.00 268.30 ?  924 MAN C O4  1 
HETATM 23461 O O5  . MAN MC 9 .   ? 96.046  50.563  253.385 1.00 271.66 ?  924 MAN C O5  1 
HETATM 23462 O O6  . MAN MC 9 .   ? 98.473  49.954  255.011 1.00 246.26 ?  924 MAN C O6  1 
HETATM 23463 C C1  . MAN NC 9 .   ? 101.487 55.054  250.996 1.00 258.15 ?  925 MAN C C1  1 
HETATM 23464 C C2  . MAN NC 9 .   ? 102.708 54.125  250.740 1.00 258.78 ?  925 MAN C C2  1 
HETATM 23465 C C3  . MAN NC 9 .   ? 103.444 53.904  252.061 1.00 255.10 ?  925 MAN C C3  1 
HETATM 23466 C C4  . MAN NC 9 .   ? 103.829 55.255  252.707 1.00 253.50 ?  925 MAN C C4  1 
HETATM 23467 C C5  . MAN NC 9 .   ? 102.584 56.128  252.889 1.00 260.51 ?  925 MAN C C5  1 
HETATM 23468 C C6  . MAN NC 9 .   ? 102.901 57.526  253.392 1.00 269.14 ?  925 MAN C C6  1 
HETATM 23469 O O2  . MAN NC 9 .   ? 103.664 54.742  249.862 1.00 262.42 ?  925 MAN C O2  1 
HETATM 23470 O O3  . MAN NC 9 .   ? 104.603 53.099  251.891 1.00 255.11 ?  925 MAN C O3  1 
HETATM 23471 O O4  . MAN NC 9 .   ? 104.432 55.038  253.972 1.00 248.72 ?  925 MAN C O4  1 
HETATM 23472 O O5  . MAN NC 9 .   ? 101.905 56.268  251.617 1.00 257.71 ?  925 MAN C O5  1 
HETATM 23473 O O6  . MAN NC 9 .   ? 102.821 58.413  252.274 1.00 274.97 ?  925 MAN C O6  1 
HETATM 23474 C C1  . MAN OC 9 .   ? 103.993 53.903  248.726 1.00 264.42 ?  926 MAN C C1  1 
HETATM 23475 C C2  . MAN OC 9 .   ? 103.791 54.781  247.462 1.00 263.45 ?  926 MAN C C2  1 
HETATM 23476 C C3  . MAN OC 9 .   ? 103.364 53.922  246.274 1.00 262.67 ?  926 MAN C C3  1 
HETATM 23477 C C4  . MAN OC 9 .   ? 104.014 52.534  246.342 1.00 259.68 ?  926 MAN C C4  1 
HETATM 23478 C C5  . MAN OC 9 .   ? 103.476 51.778  247.573 1.00 261.54 ?  926 MAN C C5  1 
HETATM 23479 C C6  . MAN OC 9 .   ? 104.421 50.697  248.080 1.00 261.33 ?  926 MAN C C6  1 
HETATM 23480 O O2  . MAN OC 9 .   ? 105.012 55.412  247.069 1.00 264.10 ?  926 MAN C O2  1 
HETATM 23481 O O3  . MAN OC 9 .   ? 103.666 54.554  245.041 1.00 264.17 ?  926 MAN C O3  1 
HETATM 23482 O O4  . MAN OC 9 .   ? 103.708 51.794  245.171 1.00 254.92 ?  926 MAN C O4  1 
HETATM 23483 O O5  . MAN OC 9 .   ? 103.209 52.704  248.680 1.00 266.12 ?  926 MAN C O5  1 
HETATM 23484 O O6  . MAN OC 9 .   ? 103.694 49.823  248.939 1.00 263.11 ?  926 MAN C O6  1 
HETATM 23485 C C1  . NAG PC 7 .   ? 90.353  97.891  266.668 1.00 229.44 ?  927 NAG C C1  1 
HETATM 23486 C C2  . NAG PC 7 .   ? 91.364  98.678  267.522 1.00 225.83 ?  927 NAG C C2  1 
HETATM 23487 C C3  . NAG PC 7 .   ? 90.840  100.080 267.854 1.00 226.66 ?  927 NAG C C3  1 
HETATM 23488 C C4  . NAG PC 7 .   ? 90.387  100.791 266.585 1.00 230.24 ?  927 NAG C C4  1 
HETATM 23489 C C5  . NAG PC 7 .   ? 89.400  99.919  265.816 1.00 228.30 ?  927 NAG C C5  1 
HETATM 23490 C C6  . NAG PC 7 .   ? 88.975  100.528 264.500 1.00 224.94 ?  927 NAG C C6  1 
HETATM 23491 C C7  . NAG PC 7 .   ? 91.092  97.531  269.774 1.00 218.65 ?  927 NAG C C7  1 
HETATM 23492 C C8  . NAG PC 7 .   ? 89.610  97.810  269.779 1.00 226.37 ?  927 NAG C C8  1 
HETATM 23493 N N2  . NAG PC 7 .   ? 91.814  97.960  268.716 1.00 218.12 ?  927 NAG C N2  1 
HETATM 23494 O O3  . NAG PC 7 .   ? 91.860  100.834 268.498 1.00 225.63 ?  927 NAG C O3  1 
HETATM 23495 O O4  . NAG PC 7 .   ? 89.752  102.020 266.918 1.00 234.49 ?  927 NAG C O4  1 
HETATM 23496 O O5  . NAG PC 7 .   ? 90.004  98.654  265.511 1.00 232.00 ?  927 NAG C O5  1 
HETATM 23497 O O6  . NAG PC 7 .   ? 89.194  99.638  263.414 1.00 221.98 ?  927 NAG C O6  1 
HETATM 23498 O O7  . NAG PC 7 .   ? 91.627  96.935  270.704 1.00 220.78 ?  927 NAG C O7  1 
HETATM 23499 C C1  . NAG QC 7 .   ? 82.694  60.301  252.410 1.00 175.21 ?  928 NAG C C1  1 
HETATM 23500 C C2  . NAG QC 7 .   ? 81.156  60.366  252.356 1.00 185.23 ?  928 NAG C C2  1 
HETATM 23501 C C3  . NAG QC 7 .   ? 80.550  59.534  253.484 1.00 193.81 ?  928 NAG C C3  1 
HETATM 23502 C C4  . NAG QC 7 .   ? 81.114  58.119  253.464 1.00 204.73 ?  928 NAG C C4  1 
HETATM 23503 C C5  . NAG QC 7 .   ? 82.638  58.177  253.505 1.00 193.94 ?  928 NAG C C5  1 
HETATM 23504 C C6  . NAG QC 7 .   ? 83.304  56.826  253.395 1.00 192.52 ?  928 NAG C C6  1 
HETATM 23505 C C7  . NAG QC 7 .   ? 80.140  62.398  251.420 1.00 202.92 ?  928 NAG C C7  1 
HETATM 23506 C C8  . NAG QC 7 .   ? 79.706  63.805  251.700 1.00 193.90 ?  928 NAG C C8  1 
HETATM 23507 N N2  . NAG QC 7 .   ? 80.689  61.741  252.445 1.00 192.90 ?  928 NAG C N2  1 
HETATM 23508 O O3  . NAG QC 7 .   ? 79.133  59.503  253.343 1.00 194.43 ?  928 NAG C O3  1 
HETATM 23509 O O4  . NAG QC 7 .   ? 80.623  57.381  254.578 1.00 228.65 ?  928 NAG C O4  1 
HETATM 23510 O O5  . NAG QC 7 .   ? 83.115  58.951  252.398 1.00 188.41 ?  928 NAG C O5  1 
HETATM 23511 O O6  . NAG QC 7 .   ? 84.491  56.903  252.617 1.00 194.33 ?  928 NAG C O6  1 
HETATM 23512 O O7  . NAG QC 7 .   ? 80.005  61.883  250.315 1.00 219.47 ?  928 NAG C O7  1 
HETATM 23513 C C1  . NAG RC 7 .   ? 79.887  56.243  254.069 1.00 208.02 ?  929 NAG C C1  1 
HETATM 23514 C C2  . NAG RC 7 .   ? 80.107  55.042  254.994 1.00 212.41 ?  929 NAG C C2  1 
HETATM 23515 C C3  . NAG RC 7 .   ? 79.321  53.837  254.485 1.00 216.95 ?  929 NAG C C3  1 
HETATM 23516 C C4  . NAG RC 7 .   ? 77.854  54.201  254.292 1.00 227.92 ?  929 NAG C C4  1 
HETATM 23517 C C5  . NAG RC 7 .   ? 77.723  55.439  253.409 1.00 219.88 ?  929 NAG C C5  1 
HETATM 23518 C C6  . NAG RC 7 .   ? 76.296  55.917  253.270 1.00 210.47 ?  929 NAG C C6  1 
HETATM 23519 C C7  . NAG RC 7 .   ? 82.197  54.822  256.260 1.00 213.66 ?  929 NAG C C7  1 
HETATM 23520 C C8  . NAG RC 7 .   ? 83.649  54.448  256.208 1.00 211.50 ?  929 NAG C C8  1 
HETATM 23521 N N2  . NAG RC 7 .   ? 81.520  54.719  255.111 1.00 213.58 ?  929 NAG C N2  1 
HETATM 23522 O O3  . NAG RC 7 .   ? 79.420  52.774  255.425 1.00 214.44 ?  929 NAG C O3  1 
HETATM 23523 O O4  . NAG RC 7 .   ? 77.153  53.114  253.699 1.00 236.74 ?  929 NAG C O4  1 
HETATM 23524 O O5  . NAG RC 7 .   ? 78.476  56.525  253.972 1.00 216.95 ?  929 NAG C O5  1 
HETATM 23525 O O6  . NAG RC 7 .   ? 76.121  56.691  252.091 1.00 204.87 ?  929 NAG C O6  1 
HETATM 23526 O O7  . NAG RC 7 .   ? 81.661  55.202  257.296 1.00 213.07 ?  929 NAG C O7  1 
HETATM 23527 C C1  . NAG SC 7 .   ? 96.126  51.801  237.200 1.00 182.45 ?  930 NAG C C1  1 
HETATM 23528 C C2  . NAG SC 7 .   ? 95.318  50.799  238.017 1.00 190.74 ?  930 NAG C C2  1 
HETATM 23529 C C3  . NAG SC 7 .   ? 96.218  49.658  238.492 1.00 204.38 ?  930 NAG C C3  1 
HETATM 23530 C C4  . NAG SC 7 .   ? 96.960  49.031  237.318 1.00 207.46 ?  930 NAG C C4  1 
HETATM 23531 C C5  . NAG SC 7 .   ? 97.679  50.108  236.507 1.00 195.93 ?  930 NAG C C5  1 
HETATM 23532 C C6  . NAG SC 7 .   ? 98.328  49.565  235.253 1.00 192.82 ?  930 NAG C C6  1 
HETATM 23533 C C7  . NAG SC 7 .   ? 93.377  51.275  239.427 1.00 206.67 ?  930 NAG C C7  1 
HETATM 23534 C C8  . NAG SC 7 .   ? 92.861  52.012  240.625 1.00 215.87 ?  930 NAG C C8  1 
HETATM 23535 N N2  . NAG SC 7 .   ? 94.671  51.445  239.146 1.00 197.82 ?  930 NAG C N2  1 
HETATM 23536 O O3  . NAG SC 7 .   ? 95.435  48.672  239.155 1.00 211.87 ?  930 NAG C O3  1 
HETATM 23537 O O4  . NAG SC 7 .   ? 97.923  48.096  237.795 1.00 223.79 ?  930 NAG C O4  1 
HETATM 23538 O O5  . NAG SC 7 .   ? 96.750  51.125  236.096 1.00 193.72 ?  930 NAG C O5  1 
HETATM 23539 O O6  . NAG SC 7 .   ? 98.880  50.596  234.445 1.00 193.14 ?  930 NAG C O6  1 
HETATM 23540 O O7  . NAG SC 7 .   ? 92.654  50.557  238.743 1.00 209.96 ?  930 NAG C O7  1 
HETATM 23541 C C1  . NAG TC 7 .   ? 97.531  46.726  237.555 1.00 219.07 ?  931 NAG C C1  1 
HETATM 23542 C C2  . NAG TC 7 .   ? 98.782  45.881  237.292 1.00 228.32 ?  931 NAG C C2  1 
HETATM 23543 C C3  . NAG TC 7 .   ? 98.400  44.413  237.104 1.00 236.00 ?  931 NAG C C3  1 
HETATM 23544 C C4  . NAG TC 7 .   ? 97.565  43.925  238.281 1.00 240.00 ?  931 NAG C C4  1 
HETATM 23545 C C5  . NAG TC 7 .   ? 96.366  44.846  238.491 1.00 230.71 ?  931 NAG C C5  1 
HETATM 23546 C C6  . NAG TC 7 .   ? 95.555  44.486  239.714 1.00 228.98 ?  931 NAG C C6  1 
HETATM 23547 C C7  . NAG TC 7 .   ? 100.812 46.686  236.160 1.00 236.72 ?  931 NAG C C7  1 
HETATM 23548 C C8  . NAG TC 7 .   ? 101.399 47.169  234.867 1.00 234.64 ?  931 NAG C C8  1 
HETATM 23549 N N2  . NAG TC 7 .   ? 99.512  46.370  236.132 1.00 230.73 ?  931 NAG C N2  1 
HETATM 23550 O O3  . NAG TC 7 .   ? 99.578  43.623  236.993 1.00 238.86 ?  931 NAG C O3  1 
HETATM 23551 O O4  . NAG TC 7 .   ? 97.113  42.597  238.042 1.00 248.59 ?  931 NAG C O4  1 
HETATM 23552 O O5  . NAG TC 7 .   ? 96.820  46.195  238.679 1.00 226.54 ?  931 NAG C O5  1 
HETATM 23553 O O6  . NAG TC 7 .   ? 95.235  45.637  240.484 1.00 228.18 ?  931 NAG C O6  1 
HETATM 23554 O O7  . NAG TC 7 .   ? 101.484 46.588  237.182 1.00 241.90 ?  931 NAG C O7  1 
HETATM 23555 C C1  . NAG UC 7 .   ? 81.092  63.283  244.611 1.00 180.28 ?  932 NAG C C1  1 
HETATM 23556 C C2  . NAG UC 7 .   ? 81.443  61.824  244.398 1.00 176.31 ?  932 NAG C C2  1 
HETATM 23557 C C3  . NAG UC 7 .   ? 81.212  61.438  242.942 1.00 177.28 ?  932 NAG C C3  1 
HETATM 23558 C C4  . NAG UC 7 .   ? 79.788  61.793  242.522 1.00 180.54 ?  932 NAG C C4  1 
HETATM 23559 C C5  . NAG UC 7 .   ? 79.471  63.249  242.862 1.00 179.79 ?  932 NAG C C5  1 
HETATM 23560 C C6  . NAG UC 7 .   ? 78.020  63.603  242.625 1.00 173.43 ?  932 NAG C C6  1 
HETATM 23561 C C7  . NAG UC 7 .   ? 83.116  61.061  246.022 1.00 186.34 ?  932 NAG C C7  1 
HETATM 23562 C C8  . NAG UC 7 .   ? 84.570  60.818  246.286 1.00 174.46 ?  932 NAG C C8  1 
HETATM 23563 N N2  . NAG UC 7 .   ? 82.808  61.536  244.808 1.00 177.29 ?  932 NAG C N2  1 
HETATM 23564 O O3  . NAG UC 7 .   ? 81.455  60.043  242.795 1.00 189.56 ?  932 NAG C O3  1 
HETATM 23565 O O4  . NAG UC 7 .   ? 79.624  61.640  241.116 1.00 196.32 ?  932 NAG C O4  1 
HETATM 23566 O O5  . NAG UC 7 .   ? 79.731  63.503  244.250 1.00 194.35 ?  932 NAG C O5  1 
HETATM 23567 O O6  . NAG UC 7 .   ? 77.183  63.095  243.655 1.00 184.34 ?  932 NAG C O6  1 
HETATM 23568 O O7  . NAG UC 7 .   ? 82.256  60.839  246.869 1.00 200.58 ?  932 NAG C O7  1 
HETATM 23569 C C1  . NAG VC 7 .   ? 79.196  60.300  240.806 1.00 205.42 ?  933 NAG C C1  1 
HETATM 23570 C C2  . NAG VC 7 .   ? 78.293  60.327  239.575 1.00 204.36 ?  933 NAG C C2  1 
HETATM 23571 C C3  . NAG VC 7 .   ? 77.876  58.909  239.188 1.00 196.41 ?  933 NAG C C3  1 
HETATM 23572 C C4  . NAG VC 7 .   ? 79.096  58.001  239.060 1.00 200.36 ?  933 NAG C C4  1 
HETATM 23573 C C5  . NAG VC 7 .   ? 79.973  58.101  240.306 1.00 199.82 ?  933 NAG C C5  1 
HETATM 23574 C C6  . NAG VC 7 .   ? 81.268  57.332  240.180 1.00 190.91 ?  933 NAG C C6  1 
HETATM 23575 C C7  . NAG VC 7 .   ? 76.188  60.975  240.702 1.00 227.96 ?  933 NAG C C7  1 
HETATM 23576 C C8  . NAG VC 7 .   ? 75.073  61.977  240.734 1.00 232.63 ?  933 NAG C C8  1 
HETATM 23577 N N2  . NAG VC 7 .   ? 77.130  61.181  239.772 1.00 212.07 ?  933 NAG C N2  1 
HETATM 23578 O O3  . NAG VC 7 .   ? 77.165  58.969  237.957 1.00 187.33 ?  933 NAG C O3  1 
HETATM 23579 O O4  . NAG VC 7 .   ? 78.686  56.642  238.954 1.00 200.51 ?  933 NAG C O4  1 
HETATM 23580 O O5  . NAG VC 7 .   ? 80.328  59.469  240.549 1.00 202.47 ?  933 NAG C O5  1 
HETATM 23581 O O6  . NAG VC 7 .   ? 82.385  58.206  240.087 1.00 182.67 ?  933 NAG C O6  1 
HETATM 23582 O O7  . NAG VC 7 .   ? 76.229  60.027  241.482 1.00 234.77 ?  933 NAG C O7  1 
HETATM 23583 C C1  . BMA WC 8 .   ? 78.502  56.234  237.588 1.00 200.52 ?  934 BMA C C1  1 
HETATM 23584 C C2  . BMA WC 8 .   ? 79.233  54.884  237.415 1.00 194.55 ?  934 BMA C C2  1 
HETATM 23585 C C3  . BMA WC 8 .   ? 78.725  54.105  236.202 1.00 191.67 ?  934 BMA C C3  1 
HETATM 23586 C C4  . BMA WC 8 .   ? 77.190  54.188  236.032 1.00 207.91 ?  934 BMA C C4  1 
HETATM 23587 C C5  . BMA WC 8 .   ? 76.735  55.636  236.072 1.00 210.30 ?  934 BMA C C5  1 
HETATM 23588 C C6  . BMA WC 8 .   ? 75.230  55.755  235.975 1.00 214.14 ?  934 BMA C C6  1 
HETATM 23589 O O2  . BMA WC 8 .   ? 79.027  54.050  238.546 1.00 198.21 ?  934 BMA C O2  1 
HETATM 23590 O O3  . BMA WC 8 .   ? 79.116  52.749  236.310 1.00 178.44 ?  934 BMA C O3  1 
HETATM 23591 O O4  . BMA WC 8 .   ? 76.774  53.609  234.799 1.00 213.91 ?  934 BMA C O4  1 
HETATM 23592 O O5  . BMA WC 8 .   ? 77.113  56.165  237.338 1.00 209.21 ?  934 BMA C O5  1 
HETATM 23593 O O6  . BMA WC 8 .   ? 74.669  55.169  237.146 1.00 222.09 ?  934 BMA C O6  1 
HETATM 23594 C C1  . MAN XC 9 .   ? 73.347  55.711  237.346 1.00 201.61 ?  935 MAN C C1  1 
HETATM 23595 C C2  . MAN XC 9 .   ? 72.888  55.322  238.778 1.00 212.48 ?  935 MAN C C2  1 
HETATM 23596 C C3  . MAN XC 9 .   ? 72.594  53.828  238.852 1.00 224.28 ?  935 MAN C C3  1 
HETATM 23597 C C4  . MAN XC 9 .   ? 71.663  53.393  237.709 1.00 224.40 ?  935 MAN C C4  1 
HETATM 23598 C C5  . MAN XC 9 .   ? 72.278  53.792  236.358 1.00 219.28 ?  935 MAN C C5  1 
HETATM 23599 C C6  . MAN XC 9 .   ? 71.401  53.444  235.165 1.00 224.68 ?  935 MAN C C6  1 
HETATM 23600 O O2  . MAN XC 9 .   ? 71.676  55.978  239.138 1.00 217.33 ?  935 MAN C O2  1 
HETATM 23601 O O3  . MAN XC 9 .   ? 72.047  53.466  240.113 1.00 237.01 ?  935 MAN C O3  1 
HETATM 23602 O O4  . MAN XC 9 .   ? 71.484  51.992  237.742 1.00 220.05 ?  935 MAN C O4  1 
HETATM 23603 O O5  . MAN XC 9 .   ? 72.470  55.219  236.347 1.00 204.54 ?  935 MAN C O5  1 
HETATM 23604 O O6  . MAN XC 9 .   ? 70.469  54.507  234.928 1.00 226.06 ?  935 MAN C O6  1 
HETATM 23605 C C1  . MAN YC 9 .   ? 70.112  54.483  233.525 1.00 227.12 ?  936 MAN C C1  1 
HETATM 23606 C C2  . MAN YC 9 .   ? 69.400  55.822  233.151 1.00 222.81 ?  936 MAN C C2  1 
HETATM 23607 C C3  . MAN YC 9 .   ? 67.997  55.870  233.748 1.00 224.30 ?  936 MAN C C3  1 
HETATM 23608 C C4  . MAN YC 9 .   ? 67.214  54.585  233.435 1.00 229.40 ?  936 MAN C C4  1 
HETATM 23609 C C5  . MAN YC 9 .   ? 68.003  53.357  233.911 1.00 227.67 ?  936 MAN C C5  1 
HETATM 23610 C C6  . MAN YC 9 .   ? 67.315  52.045  233.587 1.00 218.53 ?  936 MAN C C6  1 
HETATM 23611 O O2  . MAN YC 9 .   ? 69.220  55.943  231.736 1.00 223.18 ?  936 MAN C O2  1 
HETATM 23612 O O3  . MAN YC 9 .   ? 67.266  57.012  233.292 1.00 223.48 ?  936 MAN C O3  1 
HETATM 23613 O O4  . MAN YC 9 .   ? 65.960  54.616  234.089 1.00 232.71 ?  936 MAN C O4  1 
HETATM 23614 O O5  . MAN YC 9 .   ? 69.293  53.351  233.262 1.00 228.93 ?  936 MAN C O5  1 
HETATM 23615 O O6  . MAN YC 9 .   ? 68.060  51.000  234.201 1.00 207.43 ?  936 MAN C O6  1 
HETATM 23616 C C1  . MAN ZC 9 .   ? 73.171  53.064  240.929 1.00 237.90 ?  937 MAN C C1  1 
HETATM 23617 C C2  . MAN ZC 9 .   ? 73.082  51.521  241.155 1.00 242.65 ?  937 MAN C C2  1 
HETATM 23618 C C3  . MAN ZC 9 .   ? 71.947  51.195  242.129 1.00 240.07 ?  937 MAN C C3  1 
HETATM 23619 C C4  . MAN ZC 9 .   ? 72.071  52.031  243.412 1.00 238.25 ?  937 MAN C C4  1 
HETATM 23620 C C5  . MAN ZC 9 .   ? 72.095  53.524  243.065 1.00 237.91 ?  937 MAN C C5  1 
HETATM 23621 C C6  . MAN ZC 9 .   ? 72.275  54.408  244.284 1.00 237.88 ?  937 MAN C C6  1 
HETATM 23622 O O2  . MAN ZC 9 .   ? 74.288  51.035  241.759 1.00 246.45 ?  937 MAN C O2  1 
HETATM 23623 O O3  . MAN ZC 9 .   ? 71.899  49.803  242.448 1.00 236.41 ?  937 MAN C O3  1 
HETATM 23624 O O4  . MAN ZC 9 .   ? 70.971  51.765  244.269 1.00 237.98 ?  937 MAN C O4  1 
HETATM 23625 O O5  . MAN ZC 9 .   ? 73.198  53.778  242.169 1.00 237.56 ?  937 MAN C O5  1 
HETATM 23626 O O6  . MAN ZC 9 .   ? 72.078  55.755  243.880 1.00 238.46 ?  937 MAN C O6  1 
HETATM 23627 C C1  . MAN AD 9 .   ? 79.554  52.296  235.011 1.00 209.79 ?  938 MAN C C1  1 
HETATM 23628 C C2  . MAN AD 9 .   ? 79.757  50.751  235.110 1.00 219.85 ?  938 MAN C C2  1 
HETATM 23629 C C3  . MAN AD 9 .   ? 81.036  50.437  235.897 1.00 197.90 ?  938 MAN C C3  1 
HETATM 23630 C C4  . MAN AD 9 .   ? 82.234  51.225  235.339 1.00 194.28 ?  938 MAN C C4  1 
HETATM 23631 C C5  . MAN AD 9 .   ? 81.938  52.731  235.355 1.00 201.64 ?  938 MAN C C5  1 
HETATM 23632 C C6  . MAN AD 9 .   ? 83.057  53.560  234.738 1.00 204.98 ?  938 MAN C C6  1 
HETATM 23633 O O2  . MAN AD 9 .   ? 79.824  50.099  233.820 1.00 238.19 ?  938 MAN C O2  1 
HETATM 23634 O O3  . MAN AD 9 .   ? 81.327  49.040  235.910 1.00 198.21 ?  938 MAN C O3  1 
HETATM 23635 O O4  . MAN AD 9 .   ? 83.386  50.970  236.123 1.00 198.67 ?  938 MAN C O4  1 
HETATM 23636 O O5  . MAN AD 9 .   ? 80.738  52.991  234.589 1.00 198.35 ?  938 MAN C O5  1 
HETATM 23637 O O6  . MAN AD 9 .   ? 83.092  53.302  233.336 1.00 199.24 ?  938 MAN C O6  1 
HETATM 23638 C C1  . MAN BD 9 .   ? 78.585  49.359  233.656 1.00 228.11 ?  939 MAN C C1  1 
HETATM 23639 C C2  . MAN BD 9 .   ? 78.817  48.201  232.640 1.00 223.47 ?  939 MAN C C2  1 
HETATM 23640 C C3  . MAN BD 9 .   ? 78.962  48.790  231.223 1.00 214.53 ?  939 MAN C C3  1 
HETATM 23641 C C4  . MAN BD 9 .   ? 77.743  49.660  230.878 1.00 219.37 ?  939 MAN C C4  1 
HETATM 23642 C C5  . MAN BD 9 .   ? 77.608  50.789  231.904 1.00 220.96 ?  939 MAN C C5  1 
HETATM 23643 C C6  . MAN BD 9 .   ? 76.381  51.656  231.664 1.00 231.19 ?  939 MAN C C6  1 
HETATM 23644 O O2  . MAN BD 9 .   ? 77.708  47.279  232.651 1.00 241.44 ?  939 MAN C O2  1 
HETATM 23645 O O3  . MAN BD 9 .   ? 79.159  47.798  230.211 1.00 214.62 ?  939 MAN C O3  1 
HETATM 23646 O O4  . MAN BD 9 .   ? 77.899  50.220  229.582 1.00 228.34 ?  939 MAN C O4  1 
HETATM 23647 O O5  . MAN BD 9 .   ? 77.500  50.214  233.235 1.00 223.11 ?  939 MAN C O5  1 
HETATM 23648 O O6  . MAN BD 9 .   ? 75.225  50.840  231.842 1.00 238.61 ?  939 MAN C O6  1 
HETATM 23649 C C1  . MAN CD 9 .   ? 78.184  45.926  232.422 1.00 229.93 ?  940 MAN C C1  1 
HETATM 23650 C C2  . MAN CD 9 .   ? 76.976  44.938  232.610 1.00 236.78 ?  940 MAN C C2  1 
HETATM 23651 C C3  . MAN CD 9 .   ? 76.714  44.669  234.086 1.00 236.58 ?  940 MAN C C3  1 
HETATM 23652 C C4  . MAN CD 9 .   ? 78.001  44.225  234.788 1.00 238.26 ?  940 MAN C C4  1 
HETATM 23653 C C5  . MAN CD 9 .   ? 79.054  45.331  234.675 1.00 236.93 ?  940 MAN C C5  1 
HETATM 23654 C C6  . MAN CD 9 .   ? 80.377  44.954  235.319 1.00 238.52 ?  940 MAN C C6  1 
HETATM 23655 O O2  . MAN CD 9 .   ? 77.254  43.674  232.015 1.00 238.19 ?  940 MAN C O2  1 
HETATM 23656 O O3  . MAN CD 9 .   ? 75.688  43.690  234.264 1.00 240.06 ?  940 MAN C O3  1 
HETATM 23657 O O4  . MAN CD 9 .   ? 77.732  43.970  236.159 1.00 244.12 ?  940 MAN C O4  1 
HETATM 23658 O O5  . MAN CD 9 .   ? 79.315  45.606  233.274 1.00 231.79 ?  940 MAN C O5  1 
HETATM 23659 O O6  . MAN CD 9 .   ? 80.096  44.334  236.568 1.00 242.33 ?  940 MAN C O6  1 
HETATM 23660 C C1  . MAN DD 9 .   ? 74.781  49.870  241.055 1.00 243.32 ?  941 MAN C C1  1 
HETATM 23661 C C2  . MAN DD 9 .   ? 75.007  50.244  239.559 1.00 241.31 ?  941 MAN C C2  1 
HETATM 23662 C C3  . MAN DD 9 .   ? 74.832  49.014  238.667 1.00 236.05 ?  941 MAN C C3  1 
HETATM 23663 C C4  . MAN DD 9 .   ? 75.221  47.732  239.420 1.00 232.19 ?  941 MAN C C4  1 
HETATM 23664 C C5  . MAN DD 9 .   ? 74.233  47.519  240.596 1.00 237.51 ?  941 MAN C C5  1 
HETATM 23665 C C6  . MAN DD 9 .   ? 74.779  46.633  241.705 1.00 238.91 ?  941 MAN C C6  1 
HETATM 23666 O O2  . MAN DD 9 .   ? 76.337  50.709  239.327 1.00 240.69 ?  941 MAN C O2  1 
HETATM 23667 O O3  . MAN DD 9 .   ? 75.575  49.123  237.453 1.00 234.58 ?  941 MAN C O3  1 
HETATM 23668 O O4  . MAN DD 9 .   ? 75.172  46.610  238.551 1.00 227.69 ?  941 MAN C O4  1 
HETATM 23669 O O5  . MAN DD 9 .   ? 73.864  48.795  241.197 1.00 241.38 ?  941 MAN C O5  1 
HETATM 23670 O O6  . MAN DD 9 .   ? 73.743  46.432  242.671 1.00 242.40 ?  941 MAN C O6  1 
HETATM 23671 C C1  . NAG ED 7 .   ? 69.859  88.085  271.221 1.00 236.69 ?  942 NAG C C1  1 
HETATM 23672 C C2  . NAG ED 7 .   ? 69.465  88.987  272.390 1.00 247.32 ?  942 NAG C C2  1 
HETATM 23673 C C3  . NAG ED 7 .   ? 69.109  88.148  273.620 1.00 246.23 ?  942 NAG C C3  1 
HETATM 23674 C C4  . NAG ED 7 .   ? 68.048  87.111  273.257 1.00 244.30 ?  942 NAG C C4  1 
HETATM 23675 C C5  . NAG ED 7 .   ? 68.496  86.294  272.044 1.00 242.03 ?  942 NAG C C5  1 
HETATM 23676 C C6  . NAG ED 7 .   ? 67.425  85.320  271.568 1.00 234.27 ?  942 NAG C C6  1 
HETATM 23677 C C7  . NAG ED 7 .   ? 70.242  91.267  272.848 1.00 255.39 ?  942 NAG C C7  1 
HETATM 23678 C C8  . NAG ED 7 .   ? 68.794  91.658  272.813 1.00 260.99 ?  942 NAG C C8  1 
HETATM 23679 N N2  . NAG ED 7 .   ? 70.503  89.965  272.678 1.00 250.71 ?  942 NAG C N2  1 
HETATM 23680 O O3  . NAG ED 7 .   ? 68.691  88.984  274.700 1.00 247.98 ?  942 NAG C O3  1 
HETATM 23681 O O4  . NAG ED 7 .   ? 67.946  86.193  274.338 1.00 238.84 ?  942 NAG C O4  1 
HETATM 23682 O O5  . NAG ED 7 .   ? 68.797  87.172  270.950 1.00 248.32 ?  942 NAG C O5  1 
HETATM 23683 O O6  . NAG ED 7 .   ? 66.881  85.556  270.272 1.00 230.90 ?  942 NAG C O6  1 
HETATM 23684 O O7  . NAG ED 7 .   ? 71.133  92.090  273.040 1.00 253.06 ?  942 NAG C O7  1 
HETATM 23685 C C1  . NAG FD 7 .   ? 82.881  85.022  242.616 1.00 237.24 ?  943 NAG C C1  1 
HETATM 23686 C C2  . NAG FD 7 .   ? 84.047  85.209  241.639 1.00 242.10 ?  943 NAG C C2  1 
HETATM 23687 C C3  . NAG FD 7 .   ? 83.746  86.361  240.680 1.00 260.57 ?  943 NAG C C3  1 
HETATM 23688 C C4  . NAG FD 7 .   ? 82.399  86.158  239.995 1.00 272.90 ?  943 NAG C C4  1 
HETATM 23689 C C5  . NAG FD 7 .   ? 81.302  85.891  241.029 1.00 260.61 ?  943 NAG C C5  1 
HETATM 23690 C C6  . NAG FD 7 .   ? 79.976  85.540  240.391 1.00 254.91 ?  943 NAG C C6  1 
HETATM 23691 C C7  . NAG FD 7 .   ? 85.993  84.439  242.938 1.00 229.50 ?  943 NAG C C7  1 
HETATM 23692 C C8  . NAG FD 7 .   ? 87.304  84.827  243.553 1.00 233.79 ?  943 NAG C C8  1 
HETATM 23693 N N2  . NAG FD 7 .   ? 85.320  85.417  242.317 1.00 236.53 ?  943 NAG C N2  1 
HETATM 23694 O O3  . NAG FD 7 .   ? 84.780  86.453  239.707 1.00 264.52 ?  943 NAG C O3  1 
HETATM 23695 O O4  . NAG FD 7 .   ? 82.047  87.350  239.297 1.00 295.35 ?  943 NAG C O4  1 
HETATM 23696 O O5  . NAG FD 7 .   ? 81.665  84.783  241.870 1.00 247.24 ?  943 NAG C O5  1 
HETATM 23697 O O6  . NAG FD 7 .   ? 78.879  85.871  241.233 1.00 253.14 ?  943 NAG C O6  1 
HETATM 23698 O O7  . NAG FD 7 .   ? 85.553  83.299  243.019 1.00 230.57 ?  943 NAG C O7  1 
HETATM 23699 C C1  . NAG GD 7 .   ? 82.397  87.331  237.895 1.00 286.04 ?  944 NAG C C1  1 
HETATM 23700 C C2  . NAG GD 7 .   ? 81.524  88.358  237.172 1.00 295.12 ?  944 NAG C C2  1 
HETATM 23701 C C3  . NAG GD 7 .   ? 81.880  88.400  235.686 1.00 300.26 ?  944 NAG C C3  1 
HETATM 23702 C C4  . NAG GD 7 .   ? 83.375  88.635  235.505 1.00 300.36 ?  944 NAG C C4  1 
HETATM 23703 C C5  . NAG GD 7 .   ? 84.173  87.602  236.297 1.00 289.25 ?  944 NAG C C5  1 
HETATM 23704 C C6  . NAG GD 7 .   ? 85.660  87.865  236.260 1.00 283.22 ?  944 NAG C C6  1 
HETATM 23705 C C7  . NAG GD 7 .   ? 79.300  88.873  238.077 1.00 297.55 ?  944 NAG C C7  1 
HETATM 23706 C C8  . NAG GD 7 .   ? 77.867  88.441  238.164 1.00 297.63 ?  944 NAG C C8  1 
HETATM 23707 N N2  . NAG GD 7 .   ? 80.108  88.084  237.358 1.00 295.42 ?  944 NAG C N2  1 
HETATM 23708 O O3  . NAG GD 7 .   ? 81.146  89.434  235.039 1.00 306.23 ?  944 NAG C O3  1 
HETATM 23709 O O4  . NAG GD 7 .   ? 83.722  88.535  234.129 1.00 304.66 ?  944 NAG C O4  1 
HETATM 23710 O O5  . NAG GD 7 .   ? 83.783  87.641  237.678 1.00 289.81 ?  944 NAG C O5  1 
HETATM 23711 O O6  . NAG GD 7 .   ? 86.380  86.715  235.838 1.00 276.81 ?  944 NAG C O6  1 
HETATM 23712 O O7  . NAG GD 7 .   ? 79.708  89.890  238.632 1.00 299.58 ?  944 NAG C O7  1 
HETATM 23713 C C1  . NAG HD 7 .   ? 84.481  78.683  240.212 1.00 184.42 ?  945 NAG C C1  1 
HETATM 23714 C C2  . NAG HD 7 .   ? 85.154  79.597  239.172 1.00 207.47 ?  945 NAG C C2  1 
HETATM 23715 C C3  . NAG HD 7 .   ? 84.155  80.642  238.662 1.00 219.49 ?  945 NAG C C3  1 
HETATM 23716 C C4  . NAG HD 7 .   ? 82.900  79.956  238.135 1.00 221.45 ?  945 NAG C C4  1 
HETATM 23717 C C5  . NAG HD 7 .   ? 82.317  79.055  239.221 1.00 196.31 ?  945 NAG C C5  1 
HETATM 23718 C C6  . NAG HD 7 .   ? 81.133  78.247  238.747 1.00 194.20 ?  945 NAG C C6  1 
HETATM 23719 C C7  . NAG HD 7 .   ? 86.375  81.013  240.791 1.00 231.43 ?  945 NAG C C7  1 
HETATM 23720 C C8  . NAG HD 7 .   ? 87.711  81.585  241.158 1.00 232.00 ?  945 NAG C C8  1 
HETATM 23721 N N2  . NAG HD 7 .   ? 86.351  80.239  239.698 1.00 218.29 ?  945 NAG C N2  1 
HETATM 23722 O O3  . NAG HD 7 .   ? 84.757  81.437  237.647 1.00 229.43 ?  945 NAG C O3  1 
HETATM 23723 O O4  . NAG HD 7 .   ? 81.913  80.913  237.761 1.00 249.26 ?  945 NAG C O4  1 
HETATM 23724 O O5  . NAG HD 7 .   ? 83.301  78.103  239.648 1.00 178.19 ?  945 NAG C O5  1 
HETATM 23725 O O6  . NAG HD 7 .   ? 81.544  76.967  238.285 1.00 180.07 ?  945 NAG C O6  1 
HETATM 23726 O O7  . NAG HD 7 .   ? 85.369  81.236  241.457 1.00 237.96 ?  945 NAG C O7  1 
HETATM 23727 C C1  . NAG ID 7 .   ? 81.854  81.077  236.324 1.00 245.09 ?  946 NAG C C1  1 
HETATM 23728 C C2  . NAG ID 7 .   ? 80.409  80.967  235.818 1.00 245.26 ?  946 NAG C C2  1 
HETATM 23729 C C3  . NAG ID 7 .   ? 80.365  81.205  234.309 1.00 246.35 ?  946 NAG C C3  1 
HETATM 23730 C C4  . NAG ID 7 .   ? 81.039  82.524  233.956 1.00 251.63 ?  946 NAG C C4  1 
HETATM 23731 C C5  . NAG ID 7 .   ? 82.447  82.574  234.543 1.00 253.56 ?  946 NAG C C5  1 
HETATM 23732 C C6  . NAG ID 7 .   ? 83.120  83.909  234.333 1.00 254.82 ?  946 NAG C C6  1 
HETATM 23733 C C7  . NAG ID 7 .   ? 78.569  79.529  236.585 1.00 233.34 ?  946 NAG C C7  1 
HETATM 23734 C C8  . NAG ID 7 .   ? 78.127  78.123  236.860 1.00 224.17 ?  946 NAG C C8  1 
HETATM 23735 N N2  . NAG ID 7 .   ? 79.825  79.675  236.146 1.00 238.56 ?  946 NAG C N2  1 
HETATM 23736 O O3  . NAG ID 7 .   ? 79.015  81.216  233.857 1.00 248.03 ?  946 NAG C O3  1 
HETATM 23737 O O4  . NAG ID 7 .   ? 81.120  82.670  232.542 1.00 250.29 ?  946 NAG C O4  1 
HETATM 23738 O O5  . NAG ID 7 .   ? 82.393  82.356  235.961 1.00 254.16 ?  946 NAG C O5  1 
HETATM 23739 O O6  . NAG ID 7 .   ? 84.383  83.955  234.981 1.00 251.53 ?  946 NAG C O6  1 
HETATM 23740 O O7  . NAG ID 7 .   ? 77.825  80.490  236.755 1.00 236.64 ?  946 NAG C O7  1 
HETATM 23741 C C1  . NAG JD 7 .   ? 73.770  80.427  244.664 1.00 236.23 ?  947 NAG C C1  1 
HETATM 23742 C C2  . NAG JD 7 .   ? 73.875  80.978  243.248 1.00 242.78 ?  947 NAG C C2  1 
HETATM 23743 C C3  . NAG JD 7 .   ? 72.491  80.988  242.598 1.00 251.61 ?  947 NAG C C3  1 
HETATM 23744 C C4  . NAG JD 7 .   ? 71.851  79.604  242.678 1.00 257.25 ?  947 NAG C C4  1 
HETATM 23745 C C5  . NAG JD 7 .   ? 71.881  79.090  244.115 1.00 251.79 ?  947 NAG C C5  1 
HETATM 23746 C C6  . NAG JD 7 .   ? 71.412  77.663  244.261 1.00 255.55 ?  947 NAG C C6  1 
HETATM 23747 C C7  . NAG JD 7 .   ? 75.403  82.750  242.463 1.00 238.96 ?  947 NAG C C7  1 
HETATM 23748 C C8  . NAG JD 7 .   ? 75.832  84.176  242.647 1.00 245.06 ?  947 NAG C C8  1 
HETATM 23749 N N2  . NAG JD 7 .   ? 74.428  82.325  243.273 1.00 239.98 ?  947 NAG C N2  1 
HETATM 23750 O O3  . NAG JD 7 .   ? 72.609  81.407  241.243 1.00 254.02 ?  947 NAG C O3  1 
HETATM 23751 O O4  . NAG JD 7 .   ? 70.477  79.664  242.311 1.00 269.84 ?  947 NAG C O4  1 
HETATM 23752 O O5  . NAG JD 7 .   ? 73.216  79.131  244.628 1.00 241.98 ?  947 NAG C O5  1 
HETATM 23753 O O6  . NAG JD 7 .   ? 71.736  77.146  245.544 1.00 258.63 ?  947 NAG C O6  1 
HETATM 23754 O O7  . NAG JD 7 .   ? 75.917  82.020  241.622 1.00 233.90 ?  947 NAG C O7  1 
HETATM 23755 C C1  . NAG KD 7 .   ? 70.197  79.440  240.921 1.00 273.30 ?  948 NAG C C1  1 
HETATM 23756 C C2  . NAG KD 7 .   ? 69.869  77.972  240.635 1.00 268.27 ?  948 NAG C C2  1 
HETATM 23757 C C3  . NAG KD 7 .   ? 69.411  77.803  239.186 1.00 271.29 ?  948 NAG C C3  1 
HETATM 23758 C C4  . NAG KD 7 .   ? 68.269  78.763  238.867 1.00 276.39 ?  948 NAG C C4  1 
HETATM 23759 C C5  . NAG KD 7 .   ? 68.689  80.185  239.221 1.00 278.57 ?  948 NAG C C5  1 
HETATM 23760 C C6  . NAG KD 7 .   ? 67.576  81.190  239.042 1.00 282.35 ?  948 NAG C C6  1 
HETATM 23761 C C7  . NAG KD 7 .   ? 70.916  75.935  241.537 1.00 246.34 ?  948 NAG C C7  1 
HETATM 23762 C C8  . NAG KD 7 .   ? 72.201  75.184  241.723 1.00 241.07 ?  948 NAG C C8  1 
HETATM 23763 N N2  . NAG KD 7 .   ? 71.011  77.111  240.906 1.00 256.45 ?  948 NAG C N2  1 
HETATM 23764 O O3  . NAG KD 7 .   ? 69.006  76.448  239.024 1.00 270.76 ?  948 NAG C O3  1 
HETATM 23765 O O4  . NAG KD 7 .   ? 67.993  78.808  237.470 1.00 276.32 ?  948 NAG C O4  1 
HETATM 23766 O O5  . NAG KD 7 .   ? 69.081  80.251  240.597 1.00 278.56 ?  948 NAG C O5  1 
HETATM 23767 O O6  . NAG KD 7 .   ? 67.850  82.393  239.747 1.00 284.47 ?  948 NAG C O6  1 
HETATM 23768 O O7  . NAG KD 7 .   ? 69.845  75.504  241.954 1.00 243.62 ?  948 NAG C O7  1 
HETATM 23769 C C1  . BMA LD 8 .   ? 67.463  77.622  236.834 1.00 279.84 ?  949 BMA C C1  1 
HETATM 23770 C C2  . BMA LD 8 .   ? 65.942  77.481  237.112 1.00 283.13 ?  949 BMA C C2  1 
HETATM 23771 C C3  . BMA LD 8 .   ? 65.360  76.344  236.254 1.00 281.95 ?  949 BMA C C3  1 
HETATM 23772 C C4  . BMA LD 8 .   ? 65.796  76.462  234.775 1.00 281.11 ?  949 BMA C C4  1 
HETATM 23773 C C5  . BMA LD 8 .   ? 67.323  76.560  234.678 1.00 277.69 ?  949 BMA C C5  1 
HETATM 23774 C C6  . BMA LD 8 .   ? 67.812  76.754  233.256 1.00 277.00 ?  949 BMA C C6  1 
HETATM 23775 O O2  . BMA LD 8 .   ? 65.251  78.659  236.749 1.00 287.71 ?  949 BMA C O2  1 
HETATM 23776 O O3  . BMA LD 8 .   ? 63.941  76.286  236.341 1.00 285.42 ?  949 BMA C O3  1 
HETATM 23777 O O4  . BMA LD 8 .   ? 65.358  75.332  234.043 1.00 279.53 ?  949 BMA C O4  1 
HETATM 23778 O O5  . BMA LD 8 .   ? 67.738  77.696  235.433 1.00 279.40 ?  949 BMA C O5  1 
HETATM 23779 O O6  . BMA LD 8 .   ? 69.229  76.619  233.250 1.00 273.36 ?  949 BMA C O6  1 
HETATM 23780 C C1  . NAG MD 7 .   ? 86.743  63.571  262.443 1.00 196.73 ?  950 NAG C C1  1 
HETATM 23781 C C2  . NAG MD 7 .   ? 87.988  62.894  263.033 1.00 208.86 ?  950 NAG C C2  1 
HETATM 23782 C C3  . NAG MD 7 .   ? 87.624  61.563  263.685 1.00 211.30 ?  950 NAG C C3  1 
HETATM 23783 C C4  . NAG MD 7 .   ? 86.512  61.762  264.704 1.00 215.51 ?  950 NAG C C4  1 
HETATM 23784 C C5  . NAG MD 7 .   ? 85.316  62.409  264.013 1.00 222.25 ?  950 NAG C C5  1 
HETATM 23785 C C6  . NAG MD 7 .   ? 84.166  62.700  264.949 1.00 229.76 ?  950 NAG C C6  1 
HETATM 23786 C C7  . NAG MD 7 .   ? 90.222  63.250  262.070 1.00 209.14 ?  950 NAG C C7  1 
HETATM 23787 C C8  . NAG MD 7 .   ? 90.504  64.108  263.268 1.00 203.61 ?  950 NAG C C8  1 
HETATM 23788 N N2  . NAG MD 7 .   ? 89.005  62.699  262.012 1.00 212.18 ?  950 NAG C N2  1 
HETATM 23789 O O3  . NAG MD 7 .   ? 88.777  61.023  264.319 1.00 213.84 ?  950 NAG C O3  1 
HETATM 23790 O O4  . NAG MD 7 .   ? 86.156  60.521  265.305 1.00 226.65 ?  950 NAG C O4  1 
HETATM 23791 O O5  . NAG MD 7 .   ? 85.717  63.666  263.448 1.00 217.04 ?  950 NAG C O5  1 
HETATM 23792 O O6  . NAG MD 7 .   ? 82.945  62.842  264.237 1.00 234.15 ?  950 NAG C O6  1 
HETATM 23793 O O7  . NAG MD 7 .   ? 91.059  63.063  261.193 1.00 210.15 ?  950 NAG C O7  1 
HETATM 23794 C C1  . NAG ND 7 .   ? 86.353  60.629  266.741 1.00 239.34 ?  951 NAG C C1  1 
HETATM 23795 C C2  . NAG ND 7 .   ? 85.515  59.549  267.430 1.00 247.68 ?  951 NAG C C2  1 
HETATM 23796 C C3  . NAG ND 7 .   ? 85.703  59.620  268.945 1.00 260.53 ?  951 NAG C C3  1 
HETATM 23797 C C4  . NAG ND 7 .   ? 87.183  59.587  269.311 1.00 272.56 ?  951 NAG C C4  1 
HETATM 23798 C C5  . NAG ND 7 .   ? 87.952  60.651  268.527 1.00 258.35 ?  951 NAG C C5  1 
HETATM 23799 C C6  . NAG ND 7 .   ? 89.446  60.591  268.747 1.00 258.95 ?  951 NAG C C6  1 
HETATM 23800 C C7  . NAG ND 7 .   ? 83.359  58.666  266.656 1.00 232.32 ?  951 NAG C C7  1 
HETATM 23801 C C8  . NAG ND 7 .   ? 81.930  58.989  266.343 1.00 229.90 ?  951 NAG C C8  1 
HETATM 23802 N N2  . NAG ND 7 .   ? 84.110  59.686  267.083 1.00 242.32 ?  951 NAG C N2  1 
HETATM 23803 O O3  . NAG ND 7 .   ? 85.022  58.531  269.558 1.00 262.92 ?  951 NAG C O3  1 
HETATM 23804 O O4  . NAG ND 7 .   ? 87.338  59.841  270.704 1.00 300.11 ?  951 NAG C O4  1 
HETATM 23805 O O5  . NAG ND 7 .   ? 87.733  60.480  267.118 1.00 245.13 ?  951 NAG C O5  1 
HETATM 23806 O O6  . NAG ND 7 .   ? 90.110  61.668  268.101 1.00 256.48 ?  951 NAG C O6  1 
HETATM 23807 O O7  . NAG ND 7 .   ? 83.813  57.534  266.529 1.00 226.96 ?  951 NAG C O7  1 
HETATM 23808 C C1  . BMA OD 8 .   ? 87.589  58.620  271.436 1.00 300.66 ?  952 BMA C C1  1 
HETATM 23809 C C2  . BMA OD 8 .   ? 88.806  58.856  272.366 1.00 328.61 ?  952 BMA C C2  1 
HETATM 23810 C C3  . BMA OD 8 .   ? 89.004  57.652  273.290 1.00 312.53 ?  952 BMA C C3  1 
HETATM 23811 C C4  . BMA OD 8 .   ? 87.693  57.252  273.984 1.00 300.94 ?  952 BMA C C4  1 
HETATM 23812 C C5  . BMA OD 8 .   ? 86.597  57.018  272.937 1.00 288.28 ?  952 BMA C C5  1 
HETATM 23813 C C6  . BMA OD 8 .   ? 85.256  56.674  273.558 1.00 275.69 ?  952 BMA C C6  1 
HETATM 23814 O O2  . BMA OD 8 .   ? 88.592  59.986  273.203 1.00 382.42 ?  952 BMA C O2  1 
HETATM 23815 O O3  . BMA OD 8 .   ? 90.013  57.900  274.263 1.00 308.80 ?  952 BMA C O3  1 
HETATM 23816 O O4  . BMA OD 8 .   ? 87.885  56.066  274.737 1.00 302.93 ?  952 BMA C O4  1 
HETATM 23817 O O5  . BMA OD 8 .   ? 86.436  58.228  272.179 1.00 293.44 ?  952 BMA C O5  1 
HETATM 23818 O O6  . BMA OD 8 .   ? 85.493  55.940  274.752 1.00 268.11 ?  952 BMA C O6  1 
HETATM 23819 C C1  . NAG PD 7 .   ? 68.671  74.244  253.680 1.00 227.18 ?  953 NAG C C1  1 
HETATM 23820 C C2  . NAG PD 7 .   ? 67.388  74.039  254.462 1.00 232.07 ?  953 NAG C C2  1 
HETATM 23821 C C3  . NAG PD 7 .   ? 66.198  74.361  253.571 1.00 238.44 ?  953 NAG C C3  1 
HETATM 23822 C C4  . NAG PD 7 .   ? 66.343  75.762  252.985 1.00 239.52 ?  953 NAG C C4  1 
HETATM 23823 C C5  . NAG PD 7 .   ? 67.729  75.981  252.367 1.00 237.73 ?  953 NAG C C5  1 
HETATM 23824 C C6  . NAG PD 7 .   ? 67.981  77.423  251.993 1.00 244.18 ?  953 NAG C C6  1 
HETATM 23825 C C7  . NAG PD 7 .   ? 66.859  72.404  256.217 1.00 224.40 ?  953 NAG C C7  1 
HETATM 23826 C C8  . NAG PD 7 .   ? 66.832  70.953  256.590 1.00 212.33 ?  953 NAG C C8  1 
HETATM 23827 N N2  . NAG PD 7 .   ? 67.294  72.685  254.983 1.00 224.73 ?  953 NAG C N2  1 
HETATM 23828 O O3  . NAG PD 7 .   ? 64.999  74.266  254.331 1.00 243.45 ?  953 NAG C O3  1 
HETATM 23829 O O4  . NAG PD 7 .   ? 65.357  75.963  251.979 1.00 240.55 ?  953 NAG C O4  1 
HETATM 23830 O O5  . NAG PD 7 .   ? 68.771  75.604  253.283 1.00 234.11 ?  953 NAG C O5  1 
HETATM 23831 O O6  . NAG PD 7 .   ? 69.369  77.727  252.001 1.00 246.93 ?  953 NAG C O6  1 
HETATM 23832 O O7  . NAG PD 7 .   ? 66.501  73.283  256.995 1.00 234.33 ?  953 NAG C O7  1 
HETATM 23833 C C1  . NAG QD 7 .   ? 113.742 101.606 304.254 1.00 265.41 ?  901 NAG D C1  1 
HETATM 23834 C C2  . NAG QD 7 .   ? 115.257 101.860 304.289 1.00 277.74 ?  901 NAG D C2  1 
HETATM 23835 C C3  . NAG QD 7 .   ? 115.539 103.359 304.239 1.00 296.88 ?  901 NAG D C3  1 
HETATM 23836 C C4  . NAG QD 7 .   ? 114.873 103.979 303.020 1.00 303.82 ?  901 NAG D C4  1 
HETATM 23837 C C5  . NAG QD 7 .   ? 113.381 103.654 303.006 1.00 293.59 ?  901 NAG D C5  1 
HETATM 23838 C C6  . NAG QD 7 .   ? 112.696 104.120 301.743 1.00 299.54 ?  901 NAG D C6  1 
HETATM 23839 C C7  . NAG QD 7 .   ? 117.172 100.934 305.515 1.00 271.37 ?  901 NAG D C7  1 
HETATM 23840 C C8  . NAG QD 7 .   ? 117.644 100.327 306.802 1.00 265.33 ?  901 NAG D C8  1 
HETATM 23841 N N2  . NAG QD 7 .   ? 115.875 101.260 305.461 1.00 271.43 ?  901 NAG D N2  1 
HETATM 23842 O O3  . NAG QD 7 .   ? 116.943 103.590 304.192 1.00 303.55 ?  901 NAG D O3  1 
HETATM 23843 O O4  . NAG QD 7 .   ? 115.046 105.392 303.038 1.00 319.29 ?  901 NAG D O4  1 
HETATM 23844 O O5  . NAG QD 7 .   ? 113.175 102.234 303.085 1.00 274.09 ?  901 NAG D O5  1 
HETATM 23845 O O6  . NAG QD 7 .   ? 111.354 104.514 301.993 1.00 300.78 ?  901 NAG D O6  1 
HETATM 23846 O O7  . NAG QD 7 .   ? 117.930 101.122 304.568 1.00 276.87 ?  901 NAG D O7  1 
HETATM 23847 C C1  . NAG RD 7 .   ? 106.386 99.590  291.366 1.00 225.07 ?  902 NAG D C1  1 
HETATM 23848 C C2  . NAG RD 7 .   ? 105.011 99.910  291.941 1.00 242.22 ?  902 NAG D C2  1 
HETATM 23849 C C3  . NAG RD 7 .   ? 104.102 100.469 290.850 1.00 256.52 ?  902 NAG D C3  1 
HETATM 23850 C C4  . NAG RD 7 .   ? 104.777 101.630 290.128 1.00 264.58 ?  902 NAG D C4  1 
HETATM 23851 C C5  . NAG RD 7 .   ? 106.177 101.233 289.662 1.00 260.27 ?  902 NAG D C5  1 
HETATM 23852 C C6  . NAG RD 7 .   ? 106.964 102.378 289.068 1.00 272.02 ?  902 NAG D C6  1 
HETATM 23853 C C7  . NAG RD 7 .   ? 103.606 98.772  293.609 1.00 236.87 ?  902 NAG D C7  1 
HETATM 23854 C C8  . NAG RD 7 .   ? 103.095 97.451  294.101 1.00 226.14 ?  902 NAG D C8  1 
HETATM 23855 N N2  . NAG RD 7 .   ? 104.419 98.727  292.547 1.00 237.19 ?  902 NAG D N2  1 
HETATM 23856 O O3  . NAG RD 7 .   ? 102.878 100.901 291.432 1.00 264.90 ?  902 NAG D O3  1 
HETATM 23857 O O4  . NAG RD 7 .   ? 103.996 102.011 289.001 1.00 271.51 ?  902 NAG D O4  1 
HETATM 23858 O O5  . NAG RD 7 .   ? 106.937 100.751 290.777 1.00 244.39 ?  902 NAG D O5  1 
HETATM 23859 O O6  . NAG RD 7 .   ? 108.353 102.251 289.344 1.00 268.20 ?  902 NAG D O6  1 
HETATM 23860 O O7  . NAG RD 7 .   ? 103.295 99.830  294.145 1.00 248.22 ?  902 NAG D O7  1 
HETATM 23861 C C1  . NAG SD 7 .   ? 29.729  32.554  229.696 1.00 236.13 ?  301 NAG I C1  1 
HETATM 23862 C C2  . NAG SD 7 .   ? 30.986  33.340  229.358 1.00 241.89 ?  301 NAG I C2  1 
HETATM 23863 C C3  . NAG SD 7 .   ? 31.066  34.593  230.231 1.00 254.73 ?  301 NAG I C3  1 
HETATM 23864 C C4  . NAG SD 7 .   ? 29.771  35.398  230.162 1.00 255.92 ?  301 NAG I C4  1 
HETATM 23865 C C5  . NAG SD 7 .   ? 28.543  34.505  230.369 1.00 247.32 ?  301 NAG I C5  1 
HETATM 23866 C C6  . NAG SD 7 .   ? 27.235  35.200  230.062 1.00 256.01 ?  301 NAG I C6  1 
HETATM 23867 C C7  . NAG SD 7 .   ? 32.568  31.607  228.631 1.00 220.06 ?  301 NAG I C7  1 
HETATM 23868 C C8  . NAG SD 7 .   ? 33.824  30.859  228.962 1.00 225.49 ?  301 NAG I C8  1 
HETATM 23869 N N2  . NAG SD 7 .   ? 32.179  32.524  229.523 1.00 228.29 ?  301 NAG I N2  1 
HETATM 23870 O O3  . NAG SD 7 .   ? 32.162  35.398  229.812 1.00 260.05 ?  301 NAG I O3  1 
HETATM 23871 O O4  . NAG SD 7 .   ? 29.801  36.389  231.187 1.00 264.85 ?  301 NAG I O4  1 
HETATM 23872 O O5  . NAG SD 7 .   ? 28.598  33.369  229.495 1.00 238.42 ?  301 NAG I O5  1 
HETATM 23873 O O6  . NAG SD 7 .   ? 26.487  35.463  231.242 1.00 267.01 ?  301 NAG I O6  1 
HETATM 23874 O O7  . NAG SD 7 .   ? 31.933  31.388  227.604 1.00 213.76 ?  301 NAG I O7  1 
HETATM 23875 C C1  . NAG TD 7 .   ? 29.439  37.698  230.679 1.00 250.58 ?  302 NAG I C1  1 
HETATM 23876 C C2  . NAG TD 7 .   ? 28.954  38.554  231.850 1.00 254.36 ?  302 NAG I C2  1 
HETATM 23877 C C3  . NAG TD 7 .   ? 28.582  39.952  231.359 1.00 262.38 ?  302 NAG I C3  1 
HETATM 23878 C C4  . NAG TD 7 .   ? 29.713  40.564  230.539 1.00 262.19 ?  302 NAG I C4  1 
HETATM 23879 C C5  . NAG TD 7 .   ? 30.197  39.589  229.464 1.00 256.78 ?  302 NAG I C5  1 
HETATM 23880 C C6  . NAG TD 7 .   ? 31.425  40.068  228.730 1.00 252.81 ?  302 NAG I C6  1 
HETATM 23881 C C7  . NAG TD 7 .   ? 27.875  37.461  233.767 1.00 249.47 ?  302 NAG I C7  1 
HETATM 23882 C C8  . NAG TD 7 .   ? 26.608  36.858  234.295 1.00 251.47 ?  302 NAG I C8  1 
HETATM 23883 N N2  . NAG TD 7 .   ? 27.821  37.932  232.517 1.00 250.61 ?  302 NAG I N2  1 
HETATM 23884 O O3  . NAG TD 7 .   ? 28.291  40.782  232.478 1.00 266.50 ?  302 NAG I O3  1 
HETATM 23885 O O4  . NAG TD 7 .   ? 29.252  41.761  229.921 1.00 265.63 ?  302 NAG I O4  1 
HETATM 23886 O O5  . NAG TD 7 .   ? 30.544  38.330  230.058 1.00 251.99 ?  302 NAG I O5  1 
HETATM 23887 O O6  . NAG TD 7 .   ? 32.098  38.986  228.101 1.00 242.86 ?  302 NAG I O6  1 
HETATM 23888 O O7  . NAG TD 7 .   ? 28.900  37.517  234.439 1.00 248.97 ?  302 NAG I O7  1 
HETATM 23889 C C1  . BMA UD 8 .   ? 29.966  42.906  230.441 1.00 259.98 ?  303 BMA I C1  1 
HETATM 23890 C C2  . BMA UD 8 .   ? 30.804  43.472  229.287 1.00 268.68 ?  303 BMA I C2  1 
HETATM 23891 C C3  . BMA UD 8 .   ? 31.554  44.703  229.756 1.00 274.59 ?  303 BMA I C3  1 
HETATM 23892 C C4  . BMA UD 8 .   ? 30.580  45.733  230.363 1.00 270.26 ?  303 BMA I C4  1 
HETATM 23893 C C5  . BMA UD 8 .   ? 29.752  45.081  231.491 1.00 268.62 ?  303 BMA I C5  1 
HETATM 23894 C C6  . BMA UD 8 .   ? 28.695  46.016  232.057 1.00 270.57 ?  303 BMA I C6  1 
HETATM 23895 O O2  . BMA UD 8 .   ? 29.964  43.888  228.219 1.00 269.51 ?  303 BMA I O2  1 
HETATM 23896 O O3  . BMA UD 8 .   ? 32.323  45.278  228.684 1.00 282.79 ?  303 BMA I O3  1 
HETATM 23897 O O4  . BMA UD 8 .   ? 31.302  46.834  230.882 1.00 261.35 ?  303 BMA I O4  1 
HETATM 23898 O O5  . BMA UD 8 .   ? 29.084  43.909  230.961 1.00 260.83 ?  303 BMA I O5  1 
HETATM 23899 O O6  . BMA UD 8 .   ? 28.262  45.503  233.308 1.00 268.06 ?  303 BMA I O6  1 
HETATM 23900 C C1  . MAN VD 9 .   ? 33.680  44.754  228.711 1.00 269.28 ?  304 MAN I C1  1 
HETATM 23901 C C2  . MAN VD 9 .   ? 34.613  45.749  227.925 1.00 278.91 ?  304 MAN I C2  1 
HETATM 23902 C C3  . MAN VD 9 .   ? 34.512  45.556  226.405 1.00 280.02 ?  304 MAN I C3  1 
HETATM 23903 C C4  . MAN VD 9 .   ? 34.707  44.096  226.049 1.00 275.88 ?  304 MAN I C4  1 
HETATM 23904 C C5  . MAN VD 9 .   ? 33.584  43.320  226.737 1.00 266.32 ?  304 MAN I C5  1 
HETATM 23905 C C6  . MAN VD 9 .   ? 33.532  41.848  226.358 1.00 253.09 ?  304 MAN I C6  1 
HETATM 23906 O O2  . MAN VD 9 .   ? 35.993  45.550  228.270 1.00 281.34 ?  304 MAN I O2  1 
HETATM 23907 O O3  . MAN VD 9 .   ? 35.423  46.406  225.693 1.00 280.39 ?  304 MAN I O3  1 
HETATM 23908 O O4  . MAN VD 9 .   ? 34.605  43.941  224.655 1.00 276.60 ?  304 MAN I O4  1 
HETATM 23909 O O5  . MAN VD 9 .   ? 33.771  43.427  228.178 1.00 266.86 ?  304 MAN I O5  1 
HETATM 23910 O O6  . MAN VD 9 .   ? 33.275  41.752  224.955 1.00 245.66 ?  304 MAN I O6  1 
HETATM 23911 C C1  . NAG WD 7 .   ? 49.124  50.418  252.340 1.00 294.30 ?  305 NAG I C1  1 
HETATM 23912 C C2  . NAG WD 7 .   ? 48.982  50.135  253.787 1.00 290.41 ?  305 NAG I C2  1 
HETATM 23913 C C3  . NAG WD 7 .   ? 48.734  51.413  254.556 1.00 288.90 ?  305 NAG I C3  1 
HETATM 23914 C C4  . NAG WD 7 .   ? 49.799  52.468  254.293 1.00 285.07 ?  305 NAG I C4  1 
HETATM 23915 C C5  . NAG WD 7 .   ? 49.961  52.701  252.781 1.00 288.89 ?  305 NAG I C5  1 
HETATM 23916 C C6  . NAG WD 7 .   ? 51.109  53.612  252.440 1.00 279.86 ?  305 NAG I C6  1 
HETATM 23917 C C7  . NAG WD 7 .   ? 47.827  48.345  254.990 1.00 274.00 ?  305 NAG I C7  1 
HETATM 23918 C C8  . NAG WD 7 .   ? 46.632  47.433  255.033 1.00 262.08 ?  305 NAG I C8  1 
HETATM 23919 N N2  . NAG WD 7 .   ? 47.875  49.231  253.979 1.00 284.77 ?  305 NAG I N2  1 
HETATM 23920 O O3  . NAG WD 7 .   ? 48.513  51.156  255.927 1.00 282.63 ?  305 NAG I O3  1 
HETATM 23921 O O4  . NAG WD 7 .   ? 49.351  53.689  254.861 1.00 278.01 ?  305 NAG I O4  1 
HETATM 23922 O O5  . NAG WD 7 .   ? 50.262  51.450  252.126 1.00 291.96 ?  305 NAG I O5  1 
HETATM 23923 O O6  . NAG WD 7 .   ? 51.456  53.341  251.093 1.00 266.66 ?  305 NAG I O6  1 
HETATM 23924 O O7  . NAG WD 7 .   ? 48.666  48.318  255.880 1.00 274.16 ?  305 NAG I O7  1 
HETATM 23925 C C1  . NAG XD 7 .   ? 57.213  56.753  198.577 1.00 293.52 ?  301 NAG K C1  1 
HETATM 23926 C C2  . NAG XD 7 .   ? 57.552  56.719  197.132 1.00 284.87 ?  301 NAG K C2  1 
HETATM 23927 C C3  . NAG XD 7 .   ? 56.555  57.529  196.334 1.00 275.94 ?  301 NAG K C3  1 
HETATM 23928 C C4  . NAG XD 7 .   ? 55.118  57.094  196.584 1.00 270.17 ?  301 NAG K C4  1 
HETATM 23929 C C5  . NAG XD 7 .   ? 54.814  57.087  198.093 1.00 281.30 ?  301 NAG K C5  1 
HETATM 23930 C C6  . NAG XD 7 .   ? 53.469  56.502  198.423 1.00 276.38 ?  301 NAG K C6  1 
HETATM 23931 C C7  . NAG XD 7 .   ? 59.703  56.869  195.965 1.00 274.45 ?  301 NAG K C7  1 
HETATM 23932 C C8  . NAG XD 7 .   ? 61.068  57.498  195.939 1.00 268.57 ?  301 NAG K C8  1 
HETATM 23933 N N2  . NAG XD 7 .   ? 58.877  57.262  196.951 1.00 289.39 ?  301 NAG K N2  1 
HETATM 23934 O O3  . NAG XD 7 .   ? 56.910  57.583  194.969 1.00 267.34 ?  301 NAG K O3  1 
HETATM 23935 O O4  . NAG XD 7 .   ? 54.265  58.059  195.990 1.00 255.81 ?  301 NAG K O4  1 
HETATM 23936 O O5  . NAG XD 7 .   ? 55.766  56.244  198.776 1.00 293.02 ?  301 NAG K O5  1 
HETATM 23937 O O6  . NAG XD 7 .   ? 53.552  56.028  199.756 1.00 271.32 ?  301 NAG K O6  1 
HETATM 23938 O O7  . NAG XD 7 .   ? 59.353  56.094  195.083 1.00 266.72 ?  301 NAG K O7  1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N   . ALA A 1   ? 3.5879 3.2125 3.0755 -1.1052 -0.6694 0.5740  31  ALA A N   
2     C CA  . ALA A 1   ? 3.5825 3.1781 3.0472 -1.1016 -0.6881 0.5781  31  ALA A CA  
3     C C   . ALA A 1   ? 3.5544 3.1501 3.0858 -1.0646 -0.6934 0.5802  31  ALA A C   
4     O O   . ALA A 1   ? 3.5024 3.0878 3.0597 -1.0352 -0.6668 0.5547  31  ALA A O   
5     C CB  . ALA A 1   ? 3.5837 3.1867 3.0162 -1.1350 -0.7250 0.6111  31  ALA A CB  
6     N N   . GLU A 2   ? 3.6104 3.2165 3.1636 -1.0716 -0.7336 0.6157  32  GLU A N   
7     C CA  . GLU A 2   ? 3.5065 3.1087 3.1088 -1.0503 -0.7567 0.6326  32  GLU A CA  
8     C C   . GLU A 2   ? 3.4276 3.0632 3.0956 -1.0390 -0.7594 0.6473  32  GLU A C   
9     O O   . GLU A 2   ? 3.3393 2.9687 3.0506 -1.0123 -0.7592 0.6446  32  GLU A O   
10    C CB  . GLU A 2   ? 3.6198 3.2188 3.2195 -1.0670 -0.8078 0.6735  32  GLU A CB  
11    C CG  . GLU A 2   ? 3.6110 3.1962 3.2566 -1.0416 -0.8276 0.6838  32  GLU A CG  
12    C CD  . GLU A 2   ? 3.6551 3.2086 3.2720 -1.0467 -0.8543 0.6944  32  GLU A CD  
13    O OE1 . GLU A 2   ? 3.7735 3.3028 3.3280 -1.0577 -0.8381 0.6731  32  GLU A OE1 
14    O OE2 . GLU A 2   ? 3.5349 3.0873 3.1941 -1.0386 -0.8906 0.7233  32  GLU A OE2 
15    N N   . ASN A 3   ? 3.1532 2.8242 2.8300 -1.0584 -0.7602 0.6616  33  ASN A N   
16    C CA  . ASN A 3   ? 3.1324 2.8367 2.8713 -1.0478 -0.7588 0.6736  33  ASN A CA  
17    C C   . ASN A 3   ? 3.0492 2.7405 2.7845 -1.0257 -0.7071 0.6282  33  ASN A C   
18    O O   . ASN A 3   ? 3.0334 2.7183 2.7279 -1.0344 -0.6758 0.6010  33  ASN A O   
19    C CB  . ASN A 3   ? 3.2209 2.9699 2.9723 -1.0774 -0.7785 0.7062  33  ASN A CB  
20    C CG  . ASN A 3   ? 3.2457 2.9930 2.9377 -1.1013 -0.7551 0.6861  33  ASN A CG  
21    O OD1 . ASN A 3   ? 3.2650 2.9785 2.9022 -1.1024 -0.7376 0.6591  33  ASN A OD1 
22    N ND2 . ASN A 3   ? 3.3144 3.0993 3.0193 -1.1205 -0.7544 0.6993  33  ASN A ND2 
23    N N   . LEU A 4   ? 2.8475 2.5347 2.6281 -0.9969 -0.6998 0.6220  34  LEU A N   
24    C CA  . LEU A 4   ? 2.7467 2.4170 2.5289 -0.9717 -0.6550 0.5819  34  LEU A CA  
25    C C   . LEU A 4   ? 2.7144 2.4132 2.5155 -0.9761 -0.6318 0.5774  34  LEU A C   
26    O O   . LEU A 4   ? 2.7508 2.4879 2.5798 -0.9940 -0.6520 0.6082  34  LEU A O   
27    C CB  . LEU A 4   ? 2.6975 2.3550 2.5229 -0.9413 -0.6596 0.5812  34  LEU A CB  
28    C CG  . LEU A 4   ? 2.7167 2.3441 2.5267 -0.9354 -0.6822 0.5848  34  LEU A CG  
29    C CD1 . LEU A 4   ? 2.6637 2.2787 2.5195 -0.9051 -0.6861 0.5833  34  LEU A CD1 
30    C CD2 . LEU A 4   ? 2.6580 2.2504 2.4021 -0.9367 -0.6548 0.5483  34  LEU A CD2 
31    N N   . TRP A 5   ? 2.5965 2.2758 2.3832 -0.9591 -0.5882 0.5383  35  TRP A N   
32    C CA  . TRP A 5   ? 2.5841 2.2808 2.3845 -0.9588 -0.5589 0.5267  35  TRP A CA  
33    C C   . TRP A 5   ? 2.5335 2.2114 2.3551 -0.9270 -0.5299 0.5014  35  TRP A C   
34    O O   . TRP A 5   ? 2.4710 2.1153 2.2733 -0.9084 -0.5175 0.4772  35  TRP A O   
35    C CB  . TRP A 5   ? 2.6430 2.3312 2.3931 -0.9748 -0.5318 0.5021  35  TRP A CB  
36    C CG  . TRP A 5   ? 2.7116 2.4133 2.4323 -1.0066 -0.5580 0.5234  35  TRP A CG  
37    C CD1 . TRP A 5   ? 2.6718 2.3529 2.3514 -1.0158 -0.5725 0.5231  35  TRP A CD1 
38    C CD2 . TRP A 5   ? 2.8325 2.5716 2.5617 -1.0343 -0.5735 0.5493  35  TRP A CD2 
39    N NE1 . TRP A 5   ? 2.7893 2.4915 2.4496 -1.0480 -0.5968 0.5480  35  TRP A NE1 
40    C CE2 . TRP A 5   ? 2.8800 2.6187 2.5706 -1.0599 -0.5980 0.5642  35  TRP A CE2 
41    C CE3 . TRP A 5   ? 2.9137 2.6875 2.6791 -1.0407 -0.5685 0.5615  35  TRP A CE3 
42    C CZ2 . TRP A 5   ? 2.9972 2.7693 2.6843 -1.0915 -0.6183 0.5909  35  TRP A CZ2 
43    C CZ3 . TRP A 5   ? 2.9990 2.8070 2.7625 -1.0716 -0.5875 0.5868  35  TRP A CZ3 
44    C CH2 . TRP A 5   ? 3.0211 2.8281 2.7457 -1.0967 -0.6125 0.6013  35  TRP A CH2 
45    N N   . VAL A 6   ? 2.3228 2.0233 2.1840 -0.9213 -0.5190 0.5077  36  VAL A N   
46    C CA  . VAL A 6   ? 2.3013 1.9857 2.1836 -0.8926 -0.4928 0.4873  36  VAL A CA  
47    C C   . VAL A 6   ? 2.2691 1.9245 2.1111 -0.8843 -0.4495 0.4456  36  VAL A C   
48    O O   . VAL A 6   ? 2.2877 1.9458 2.0993 -0.9016 -0.4353 0.4358  36  VAL A O   
49    C CB  . VAL A 6   ? 2.3622 2.0810 2.2976 -0.8910 -0.4930 0.5081  36  VAL A CB  
50    C CG1 . VAL A 6   ? 2.4014 2.1545 2.3846 -0.8992 -0.5374 0.5521  36  VAL A CG1 
51    C CG2 . VAL A 6   ? 2.4024 2.1394 2.3246 -0.9099 -0.4711 0.5029  36  VAL A CG2 
52    N N   . THR A 7   ? 2.2822 1.9099 2.1261 -0.8572 -0.4293 0.4216  37  THR A N   
53    C CA  . THR A 7   ? 2.2315 1.8333 2.0468 -0.8452 -0.3890 0.3840  37  THR A CA  
54    C C   . THR A 7   ? 2.2151 1.8055 2.0565 -0.8188 -0.3682 0.3717  37  THR A C   
55    O O   . THR A 7   ? 2.1947 1.7757 2.0561 -0.8013 -0.3804 0.3754  37  THR A O   
56    C CB  . THR A 7   ? 2.1511 1.7247 1.9260 -0.8413 -0.3852 0.3617  37  THR A CB  
57    O OG1 . THR A 7   ? 2.1263 1.6921 1.9105 -0.8335 -0.4126 0.3736  37  THR A OG1 
58    C CG2 . THR A 7   ? 2.1810 1.7581 1.9068 -0.8765 -0.3988 0.3703  37  THR A CG2 
59    N N   . VAL A 8   ? 2.0605 1.6507 1.9010 -0.8165 -0.3372 0.3579  38  VAL A N   
60    C CA  . VAL A 8   ? 2.0540 1.6337 1.9157 -0.7942 -0.3147 0.3478  38  VAL A CA  
61    C C   . VAL A 8   ? 1.9560 1.5006 1.7957 -0.7719 -0.2913 0.3140  38  VAL A C   
62    O O   . VAL A 8   ? 1.9500 1.4816 1.7587 -0.7747 -0.2733 0.2918  38  VAL A O   
63    C CB  . VAL A 8   ? 2.1152 1.7088 1.9843 -0.8026 -0.2917 0.3495  38  VAL A CB  
64    C CG1 . VAL A 8   ? 2.1081 1.6903 1.9978 -0.7807 -0.2696 0.3429  38  VAL A CG1 
65    C CG2 . VAL A 8   ? 2.2152 1.8477 2.1076 -0.8257 -0.3141 0.3824  38  VAL A CG2 
66    N N   . TYR A 9   ? 2.1299 1.6607 1.9876 -0.7498 -0.2931 0.3109  39  TYR A N   
67    C CA  . TYR A 9   ? 2.0331 1.5333 1.8755 -0.7269 -0.2717 0.2801  39  TYR A CA  
68    C C   . TYR A 9   ? 2.0296 1.5218 1.8897 -0.7102 -0.2493 0.2750  39  TYR A C   
69    O O   . TYR A 9   ? 2.0718 1.5755 1.9636 -0.7065 -0.2600 0.2963  39  TYR A O   
70    C CB  . TYR A 9   ? 1.9755 1.4621 1.8185 -0.7150 -0.2914 0.2773  39  TYR A CB  
71    C CG  . TYR A 9   ? 1.9564 1.4433 1.7717 -0.7298 -0.3054 0.2758  39  TYR A CG  
72    C CD1 . TYR A 9   ? 2.0213 1.5288 1.8417 -0.7507 -0.3363 0.3044  39  TYR A CD1 
73    C CD2 . TYR A 9   ? 1.8758 1.3437 1.6597 -0.7241 -0.2880 0.2477  39  TYR A CD2 
74    C CE1 . TYR A 9   ? 2.0032 1.5088 1.7942 -0.7655 -0.3491 0.3044  39  TYR A CE1 
75    C CE2 . TYR A 9   ? 1.9157 1.3773 1.6569 -0.7472 -0.3088 0.2535  39  TYR A CE2 
76    C CZ  . TYR A 9   ? 1.9453 1.4264 1.6934 -0.7653 -0.3363 0.2799  39  TYR A CZ  
77    O OH  . TYR A 9   ? 1.9878 1.4611 1.6909 -0.7891 -0.3571 0.2871  39  TYR A OH  
78    N N   . TYR A 10  ? 1.8744 1.3474 1.7159 -0.6998 -0.2194 0.2487  40  TYR A N   
79    C CA  . TYR A 10  ? 1.8572 1.3176 1.7085 -0.6838 -0.1958 0.2421  40  TYR A CA  
80    C C   . TYR A 10  ? 1.8353 1.2673 1.6757 -0.6599 -0.1836 0.2151  40  TYR A C   
81    O O   . TYR A 10  ? 1.8310 1.2523 1.6495 -0.6569 -0.1697 0.1918  40  TYR A O   
82    C CB  . TYR A 10  ? 1.8884 1.3524 1.7300 -0.6937 -0.1712 0.2379  40  TYR A CB  
83    C CG  . TYR A 10  ? 1.8642 1.3143 1.7131 -0.6793 -0.1462 0.2342  40  TYR A CG  
84    C CD1 . TYR A 10  ? 1.9087 1.3668 1.7827 -0.6761 -0.1489 0.2562  40  TYR A CD1 
85    C CD2 . TYR A 10  ? 1.8482 1.2779 1.6794 -0.6691 -0.1206 0.2107  40  TYR A CD2 
86    C CE1 . TYR A 10  ? 1.8816 1.3243 1.7579 -0.6632 -0.1249 0.2545  40  TYR A CE1 
87    C CE2 . TYR A 10  ? 1.8426 1.2571 1.6772 -0.6564 -0.0986 0.2091  40  TYR A CE2 
88    C CZ  . TYR A 10  ? 1.8440 1.2635 1.6988 -0.6536 -0.1000 0.2308  40  TYR A CZ  
89    O OH  . TYR A 10  ? 1.8423 1.2441 1.6961 -0.6409 -0.0770 0.2307  40  TYR A OH  
90    N N   . GLY A 11  ? 1.7841 1.2055 1.6417 -0.6429 -0.1895 0.2188  41  GLY A N   
91    C CA  . GLY A 11  ? 1.7645 1.1597 1.6137 -0.6198 -0.1800 0.1939  41  GLY A CA  
92    C C   . GLY A 11  ? 1.7602 1.1519 1.6169 -0.6127 -0.2044 0.1948  41  GLY A C   
93    O O   . GLY A 11  ? 1.7485 1.1247 1.5917 -0.6000 -0.2006 0.1710  41  GLY A O   
94    N N   . VAL A 12  ? 1.7698 1.1771 1.6512 -0.6200 -0.2298 0.2228  42  VAL A N   
95    C CA  . VAL A 12  ? 1.7686 1.1720 1.6613 -0.6132 -0.2557 0.2269  42  VAL A CA  
96    C C   . VAL A 12  ? 1.7530 1.1383 1.6672 -0.5894 -0.2585 0.2255  42  VAL A C   
97    O O   . VAL A 12  ? 1.7494 1.1361 1.6829 -0.5840 -0.2524 0.2390  42  VAL A O   
98    C CB  . VAL A 12  ? 1.7877 1.2178 1.7007 -0.6322 -0.2867 0.2599  42  VAL A CB  
99    C CG1 . VAL A 12  ? 1.8066 1.2495 1.6929 -0.6546 -0.2868 0.2587  42  VAL A CG1 
100   C CG2 . VAL A 12  ? 1.7894 1.2411 1.7382 -0.6368 -0.2924 0.2900  42  VAL A CG2 
101   N N   . PRO A 13  ? 1.8816 1.2486 1.7925 -0.5741 -0.2665 0.2089  43  PRO A N   
102   C CA  . PRO A 13  ? 1.8649 1.2122 1.7970 -0.5499 -0.2717 0.2060  43  PRO A CA  
103   C C   . PRO A 13  ? 1.9425 1.3047 1.9214 -0.5494 -0.3007 0.2416  43  PRO A C   
104   O O   . PRO A 13  ? 1.9436 1.3023 1.9412 -0.5421 -0.3246 0.2466  43  PRO A O   
105   C CB  . PRO A 13  ? 1.7910 1.1196 1.7065 -0.5371 -0.2736 0.1782  43  PRO A CB  
106   C CG  . PRO A 13  ? 1.7594 1.0949 1.6414 -0.5508 -0.2582 0.1610  43  PRO A CG  
107   C CD  . PRO A 13  ? 1.8188 1.1799 1.7034 -0.5762 -0.2661 0.1875  43  PRO A CD  
108   N N   . VAL A 14  ? 1.8288 1.2096 1.8316 -0.5558 -0.2986 0.2673  44  VAL A N   
109   C CA  . VAL A 14  ? 1.8290 1.2321 1.8879 -0.5537 -0.3246 0.3046  44  VAL A CA  
110   C C   . VAL A 14  ? 1.8176 1.2148 1.9014 -0.5363 -0.3112 0.3143  44  VAL A C   
111   O O   . VAL A 14  ? 1.8242 1.2259 1.8906 -0.5447 -0.2874 0.3152  44  VAL A O   
112   C CB  . VAL A 14  ? 1.8751 1.3183 1.9477 -0.5813 -0.3378 0.3342  44  VAL A CB  
113   C CG1 . VAL A 14  ? 1.9431 1.4164 2.0832 -0.5772 -0.3604 0.3745  44  VAL A CG1 
114   C CG2 . VAL A 14  ? 1.8712 1.3176 1.9219 -0.5964 -0.3554 0.3296  44  VAL A CG2 
115   N N   . TRP A 15  ? 1.8855 1.2756 2.0105 -0.5064 -0.3241 0.3199  45  TRP A N   
116   C CA  . TRP A 15  ? 1.8846 1.3058 2.0299 -0.4549 -0.2973 0.3132  45  TRP A CA  
117   C C   . TRP A 15  ? 1.9253 1.4004 2.1356 -0.4154 -0.3088 0.3310  45  TRP A C   
118   O O   . TRP A 15  ? 1.9372 1.4172 2.1743 -0.4152 -0.3357 0.3391  45  TRP A O   
119   C CB  . TRP A 15  ? 1.8056 1.1971 1.9211 -0.4178 -0.2757 0.2734  45  TRP A CB  
120   C CG  . TRP A 15  ? 1.7687 1.1504 1.8964 -0.3893 -0.2897 0.2535  45  TRP A CG  
121   C CD1 . TRP A 15  ? 1.7803 1.1972 1.9553 -0.3400 -0.2934 0.2532  45  TRP A CD1 
122   C CD2 . TRP A 15  ? 1.7136 1.0455 1.8047 -0.4080 -0.2996 0.2285  45  TRP A CD2 
123   N NE1 . TRP A 15  ? 1.7381 1.1293 1.9082 -0.3275 -0.3053 0.2302  45  TRP A NE1 
124   C CE2 . TRP A 15  ? 1.6962 1.0352 1.8146 -0.3688 -0.3095 0.2147  45  TRP A CE2 
125   C CE3 . TRP A 15  ? 1.6774 0.9592 1.7157 -0.4554 -0.3002 0.2155  45  TRP A CE3 
126   C CZ2 . TRP A 15  ? 1.6457 0.9430 1.7390 -0.3759 -0.3199 0.1889  45  TRP A CZ2 
127   C CZ3 . TRP A 15  ? 1.6179 0.8811 1.6315 -0.4493 -0.3022 0.1843  45  TRP A CZ3 
128   C CH2 . TRP A 15  ? 1.6102 0.8597 1.6512 -0.4230 -0.3205 0.1767  45  TRP A CH2 
129   N N   . LYS A 16  ? 1.7053 1.2201 1.9409 -0.3818 -0.2872 0.3370  46  LYS A N   
130   C CA  . LYS A 16  ? 1.6974 1.2652 1.9957 -0.3400 -0.2931 0.3500  46  LYS A CA  
131   C C   . LYS A 16  ? 1.6714 1.2554 1.9737 -0.2854 -0.2622 0.3295  46  LYS A C   
132   O O   . LYS A 16  ? 1.6742 1.2433 1.9396 -0.2870 -0.2365 0.3197  46  LYS A O   
133   C CB  . LYS A 16  ? 1.7729 1.3853 2.1077 -0.3655 -0.3030 0.3883  46  LYS A CB  
134   C CG  . LYS A 16  ? 1.8091 1.4140 2.1499 -0.4126 -0.3385 0.4104  46  LYS A CG  
135   C CD  . LYS A 16  ? 1.8757 1.5319 2.2609 -0.4331 -0.3522 0.4482  46  LYS A CD  
136   C CE  . LYS A 16  ? 1.8931 1.5417 2.2843 -0.4760 -0.3903 0.4694  46  LYS A CE  
137   N NZ  . LYS A 16  ? 1.8536 1.4931 2.2680 -0.4500 -0.4134 0.4628  46  LYS A NZ  
138   N N   . ASP A 17  ? 1.6617 1.2753 2.0077 -0.2373 -0.2645 0.3230  47  ASP A N   
139   C CA  . ASP A 17  ? 1.6396 1.2713 1.9901 -0.1847 -0.2361 0.3029  47  ASP A CA  
140   C C   . ASP A 17  ? 1.6775 1.3467 2.0401 -0.1809 -0.2145 0.3215  47  ASP A C   
141   O O   . ASP A 17  ? 1.7313 1.4411 2.1365 -0.1918 -0.2242 0.3504  47  ASP A O   
142   C CB  . ASP A 17  ? 1.6384 1.2976 2.0376 -0.1366 -0.2430 0.2934  47  ASP A CB  
143   C CG  . ASP A 17  ? 1.5968 1.2173 1.9829 -0.1373 -0.2615 0.2726  47  ASP A CG  
144   O OD1 . ASP A 17  ? 1.5869 1.1734 1.9491 -0.1823 -0.2821 0.2801  47  ASP A OD1 
145   O OD2 . ASP A 17  ? 1.5740 1.1974 1.9718 -0.0939 -0.2545 0.2477  47  ASP A OD2 
146   N N   . ALA A 18  ? 1.7085 1.3647 2.0342 -0.1645 -0.1851 0.3048  48  ALA A N   
147   C CA  . ALA A 18  ? 1.7117 1.3980 2.0424 -0.1595 -0.1613 0.3202  48  ALA A CA  
148   C C   . ALA A 18  ? 1.7062 1.3842 2.0078 -0.1179 -0.1311 0.2947  48  ALA A C   
149   O O   . ALA A 18  ? 1.6988 1.3509 1.9792 -0.0948 -0.1299 0.2656  48  ALA A O   
150   C CB  . ALA A 18  ? 1.7322 1.3999 2.0330 -0.2151 -0.1604 0.3404  48  ALA A CB  
151   N N   . GLU A 19  ? 2.0607 1.7617 2.3611 -0.1092 -0.1066 0.3060  49  GLU A N   
152   C CA  . GLU A 19  ? 2.0050 1.7022 2.2775 -0.0713 -0.0768 0.2872  49  GLU A CA  
153   C C   . GLU A 19  ? 1.9654 1.6399 2.1938 -0.0976 -0.0554 0.2973  49  GLU A C   
154   O O   . GLU A 19  ? 1.9962 1.6874 2.2370 -0.1290 -0.0545 0.3242  49  GLU A O   
155   C CB  . GLU A 19  ? 2.0832 1.8349 2.4007 -0.0248 -0.0646 0.2893  49  GLU A CB  
156   C CG  . GLU A 19  ? 2.1025 1.8749 2.4638 0.0046  -0.0827 0.2769  49  GLU A CG  
157   C CD  . GLU A 19  ? 2.2290 2.0597 2.6570 0.0174  -0.0881 0.2975  49  GLU A CD  
158   O OE1 . GLU A 19  ? 2.3054 2.1623 2.7465 0.0002  -0.0794 0.3221  49  GLU A OE1 
159   O OE2 . GLU A 19  ? 2.3556 2.2063 2.8239 0.0451  -0.1002 0.2880  49  GLU A OE2 
160   N N   . THR A 20  ? 1.9668 1.6031 2.1444 -0.0850 -0.0380 0.2752  50  THR A N   
161   C CA  . THR A 20  ? 1.9395 1.5472 2.0714 -0.1065 -0.0160 0.2819  50  THR A CA  
162   C C   . THR A 20  ? 1.9078 1.5064 2.0081 -0.0628 0.0101  0.2621  50  THR A C   
163   O O   . THR A 20  ? 1.9226 1.5400 2.0366 -0.0175 0.0113  0.2432  50  THR A O   
164   C CB  . THR A 20  ? 1.9301 1.4834 2.0208 -0.1531 -0.0255 0.2765  50  THR A CB  
165   O OG1 . THR A 20  ? 1.9467 1.4729 1.9961 -0.1737 -0.0022 0.2841  50  THR A OG1 
166   C CG2 . THR A 20  ? 1.8462 1.3656 1.9110 -0.1332 -0.0311 0.2424  50  THR A CG2 
167   N N   . THR A 21  ? 1.8987 1.4677 1.9557 -0.0778 0.0313  0.2671  51  THR A N   
168   C CA  . THR A 21  ? 1.9006 1.4562 1.9215 -0.0410 0.0568  0.2524  51  THR A CA  
169   C C   . THR A 21  ? 1.8859 1.3919 1.8644 -0.0402 0.0538  0.2239  51  THR A C   
170   O O   . THR A 21  ? 1.9079 1.3709 1.8534 -0.0785 0.0544  0.2251  51  THR A O   
171   C CB  . THR A 21  ? 1.9463 1.4945 1.9436 -0.0573 0.0820  0.2742  51  THR A CB  
172   O OG1 . THR A 21  ? 1.9632 1.5571 2.0023 -0.0677 0.0822  0.3010  51  THR A OG1 
173   C CG2 . THR A 21  ? 1.9499 1.4932 1.9169 -0.0145 0.1074  0.2634  51  THR A CG2 
174   N N   . LEU A 22  ? 1.9062 1.4195 1.8861 0.0029  0.0514  0.1973  52  LEU A N   
175   C CA  . LEU A 22  ? 1.8893 1.3624 1.8338 0.0095  0.0483  0.1667  52  LEU A CA  
176   C C   . LEU A 22  ? 1.9066 1.3590 1.8070 0.0343  0.0741  0.1581  52  LEU A C   
177   O O   . LEU A 22  ? 1.9154 1.3951 1.8185 0.0671  0.0920  0.1661  52  LEU A O   
178   C CB  . LEU A 22  ? 1.8465 1.3388 1.8145 0.0430  0.0333  0.1408  52  LEU A CB  
179   C CG  . LEU A 22  ? 1.8310 1.3429 1.8442 0.0236  0.0070  0.1488  52  LEU A CG  
180   C CD1 . LEU A 22  ? 1.7939 1.3234 1.8292 0.0604  -0.0041 0.1224  52  LEU A CD1 
181   C CD2 . LEU A 22  ? 1.8426 1.3155 1.8414 -0.0315 -0.0103 0.1537  52  LEU A CD2 
182   N N   . PHE A 23  ? 1.9124 1.3166 1.7724 0.0185  0.0761  0.1420  53  PHE A N   
183   C CA  . PHE A 23  ? 1.9316 1.3129 1.7495 0.0438  0.0984  0.1319  53  PHE A CA  
184   C C   . PHE A 23  ? 1.9181 1.2911 1.7223 0.0778  0.0930  0.0948  53  PHE A C   
185   O O   . PHE A 23  ? 1.8952 1.2761 1.7202 0.0781  0.0731  0.0766  53  PHE A O   
186   C CB  . PHE A 23  ? 1.9601 1.2929 1.7418 0.0024  0.1092  0.1426  53  PHE A CB  
187   C CG  . PHE A 23  ? 1.9572 1.2514 1.7279 -0.0384 0.0927  0.1277  53  PHE A CG  
188   C CD1 . PHE A 23  ? 1.9525 1.2477 1.7447 -0.0857 0.0754  0.1431  53  PHE A CD1 
189   C CD2 . PHE A 23  ? 1.9614 1.2187 1.6995 -0.0310 0.0948  0.0986  53  PHE A CD2 
190   C CE1 . PHE A 23  ? 1.9527 1.2118 1.7321 -0.1256 0.0606  0.1299  53  PHE A CE1 
191   C CE2 . PHE A 23  ? 1.9606 1.1819 1.6876 -0.0707 0.0810  0.0841  53  PHE A CE2 
192   C CZ  . PHE A 23  ? 1.9569 1.1783 1.7032 -0.1188 0.0642  0.0999  53  PHE A CZ  
193   N N   . CYS A 24  ? 2.3469 1.7035 2.1154 0.1061  0.1110  0.0837  54  CYS A N   
194   C CA  . CYS A 24  ? 2.3196 1.6762 2.0751 0.1451  0.1089  0.0491  54  CYS A CA  
195   C C   . CYS A 24  ? 2.3278 1.6347 2.0499 0.1257  0.1065  0.0268  54  CYS A C   
196   O O   . CYS A 24  ? 2.3575 1.6271 2.0632 0.0830  0.1087  0.0379  54  CYS A O   
197   C CB  . CYS A 24  ? 2.4174 1.7944 2.1565 0.1953  0.1289  0.0491  54  CYS A CB  
198   S SG  . CYS A 24  ? 2.7222 2.0564 2.4109 0.1917  0.1540  0.0630  54  CYS A SG  
199   N N   . ALA A 25  ? 2.4990 1.8078 2.2124 0.1579  0.1025  -0.0068 55  ALA A N   
200   C CA  . ALA A 25  ? 2.5047 1.7727 2.1878 0.1497  0.1015  -0.0341 55  ALA A CA  
201   C C   . ALA A 25  ? 2.4791 1.7664 2.1558 0.2005  0.1021  -0.0666 55  ALA A C   
202   O O   . ALA A 25  ? 2.4436 1.7674 2.1466 0.2235  0.0921  -0.0787 55  ALA A O   
203   C CB  . ALA A 25  ? 2.4917 1.7352 2.1838 0.1032  0.0820  -0.0449 55  ALA A CB  
204   N N   . SER A 26  ? 2.8001 2.0648 2.4431 0.2189  0.1139  -0.0812 56  SER A N   
205   C CA  . SER A 26  ? 2.8205 2.1082 2.4571 0.2686  0.1147  -0.1109 56  SER A CA  
206   C C   . SER A 26  ? 2.9670 2.2192 2.5708 0.2724  0.1194  -0.1360 56  SER A C   
207   O O   . SER A 26  ? 2.9218 2.1741 2.5018 0.3065  0.1329  -0.1377 56  SER A O   
208   C CB  . SER A 26  ? 2.7766 2.1004 2.4116 0.3123  0.1292  -0.0937 56  SER A CB  
209   O OG  . SER A 26  ? 2.8432 2.1430 2.4523 0.3066  0.1474  -0.0662 56  SER A OG  
210   N N   . ASP A 27  ? 3.0497 2.2712 2.6527 0.2366  0.1079  -0.1560 57  ASP A N   
211   C CA  . ASP A 27  ? 3.1218 2.3120 2.6993 0.2382  0.1105  -0.1857 57  ASP A CA  
212   C C   . ASP A 27  ? 3.1771 2.3374 2.7239 0.2426  0.1298  -0.1698 57  ASP A C   
213   O O   . ASP A 27  ? 3.1576 2.3094 2.7004 0.2288  0.1409  -0.1343 57  ASP A O   
214   C CB  . ASP A 27  ? 3.1157 2.3366 2.6949 0.2845  0.1055  -0.2220 57  ASP A CB  
215   C CG  . ASP A 27  ? 3.0325 2.2766 2.6400 0.2785  0.0874  -0.2422 57  ASP A CG  
216   O OD1 . ASP A 27  ? 3.0319 2.2523 2.6485 0.2333  0.0760  -0.2433 57  ASP A OD1 
217   O OD2 . ASP A 27  ? 3.0122 2.2976 2.6322 0.3182  0.0848  -0.2566 57  ASP A OD2 
218   N N   . ALA A 28  ? 3.3354 2.4794 2.8612 0.2620  0.1340  -0.1970 58  ALA A N   
219   C CA  . ALA A 28  ? 3.4174 2.5321 2.9137 0.2731  0.1520  -0.1869 58  ALA A CA  
220   C C   . ALA A 28  ? 3.4814 2.6200 2.9648 0.3313  0.1562  -0.2058 58  ALA A C   
221   O O   . ALA A 28  ? 3.5816 2.7085 3.0421 0.3542  0.1716  -0.1898 58  ALA A O   
222   C CB  . ALA A 28  ? 3.3662 2.4281 2.8480 0.2323  0.1542  -0.2006 58  ALA A CB  
223   N N   . LYS A 29  ? 3.4998 2.6717 2.9964 0.3555  0.1430  -0.2390 59  LYS A N   
224   C CA  . LYS A 29  ? 3.4924 2.7152 2.9936 0.4011  0.1418  -0.2530 59  LYS A CA  
225   C C   . LYS A 29  ? 3.5206 2.7717 3.0162 0.4439  0.1488  -0.2341 59  LYS A C   
226   O O   . LYS A 29  ? 3.5342 2.8214 3.0256 0.4774  0.1529  -0.2287 59  LYS A O   
227   C CB  . LYS A 29  ? 3.3843 2.6679 2.9293 0.3886  0.1224  -0.2859 59  LYS A CB  
228   C CG  . LYS A 29  ? 3.3230 2.6686 2.8816 0.4215  0.1206  -0.2929 59  LYS A CG  
229   C CD  . LYS A 29  ? 3.1535 2.5451 2.7490 0.4036  0.1097  -0.3215 59  LYS A CD  
230   C CE  . LYS A 29  ? 3.1503 2.5521 2.7399 0.4179  0.1140  -0.3234 59  LYS A CE  
231   N NZ  . LYS A 29  ? 3.0152 2.4749 2.6336 0.4209  0.1069  -0.3423 59  LYS A NZ  
232   N N   . ALA A 30  ? 3.4961 2.7585 3.0117 0.4259  0.1453  -0.2152 60  ALA A N   
233   C CA  . ALA A 30  ? 3.4809 2.7856 3.0048 0.4562  0.1507  -0.1939 60  ALA A CA  
234   C C   . ALA A 30  ? 3.5915 2.8807 3.0907 0.4654  0.1695  -0.1577 60  ALA A C   
235   O O   . ALA A 30  ? 3.6166 2.9374 3.1098 0.5018  0.1778  -0.1440 60  ALA A O   
236   C CB  . ALA A 30  ? 3.4127 2.7360 2.9705 0.4296  0.1417  -0.1806 60  ALA A CB  
237   N N   . TYR A 31  ? 3.5248 2.7645 3.0087 0.4313  0.1772  -0.1422 61  TYR A N   
238   C CA  . TYR A 31  ? 3.5855 2.8026 3.0435 0.4364  0.1966  -0.1087 61  TYR A CA  
239   C C   . TYR A 31  ? 3.6272 2.8346 3.0544 0.4771  0.2044  -0.1209 61  TYR A C   
240   O O   . TYR A 31  ? 3.6871 2.8866 3.0905 0.4974  0.2202  -0.0950 61  TYR A O   
241   C CB  . TYR A 31  ? 3.6381 2.8053 3.0926 0.3819  0.2025  -0.0893 61  TYR A CB  
242   C CG  . TYR A 31  ? 3.7278 2.8667 3.1571 0.3789  0.2239  -0.0529 61  TYR A CG  
243   C CD1 . TYR A 31  ? 3.7238 2.8813 3.1597 0.3754  0.2328  -0.0187 61  TYR A CD1 
244   C CD2 . TYR A 31  ? 3.7973 2.8897 3.1974 0.3780  0.2361  -0.0531 61  TYR A CD2 
245   C CE1 . TYR A 31  ? 3.7815 2.9118 3.1932 0.3707  0.2536  0.0143  61  TYR A CE1 
246   C CE2 . TYR A 31  ? 3.8691 2.9323 3.2454 0.3744  0.2570  -0.0194 61  TYR A CE2 
247   C CZ  . TYR A 31  ? 3.8686 2.9505 3.2497 0.3702  0.2658  0.0142  61  TYR A CZ  
248   O OH  . TYR A 31  ? 3.9171 2.9687 3.2732 0.3652  0.2877  0.0471  61  TYR A OH  
249   N N   . GLU A 32  ? 3.6709 2.8800 3.0987 0.4895  0.1933  -0.1600 62  GLU A N   
250   C CA  . GLU A 32  ? 3.6633 2.8757 3.0722 0.5234  0.1951  -0.1750 62  GLU A CA  
251   C C   . GLU A 32  ? 3.6104 2.8946 3.0298 0.5625  0.1876  -0.1767 62  GLU A C   
252   O O   . GLU A 32  ? 3.6078 2.9140 3.0214 0.5813  0.1847  -0.1799 62  GLU A O   
253   C CB  . GLU A 32  ? 3.6052 2.8297 3.0405 0.4926  0.1776  -0.2079 62  GLU A CB  
254   C CG  . GLU A 32  ? 3.6319 2.7900 3.0580 0.4486  0.1833  -0.2093 62  GLU A CG  
255   C CD  . GLU A 32  ? 3.5688 2.7488 3.0265 0.4186  0.1666  -0.2421 62  GLU A CD  
256   O OE1 . GLU A 32  ? 3.5118 2.7520 2.9956 0.4346  0.1544  -0.2609 62  GLU A OE1 
257   O OE2 . GLU A 32  ? 3.6025 2.7406 3.0606 0.3764  0.1669  -0.2479 62  GLU A OE2 
258   N N   . THR A 33  ? 3.5444 2.8638 2.9790 0.5734  0.1844  -0.1745 63  THR A N   
259   C CA  . THR A 33  ? 3.5190 2.9045 2.9625 0.6059  0.1788  -0.1750 63  THR A CA  
260   C C   . THR A 33  ? 3.5352 2.9075 2.9414 0.6401  0.1984  -0.1429 63  THR A C   
261   O O   . THR A 33  ? 3.5140 2.9315 2.9156 0.6683  0.1950  -0.1414 63  THR A O   
262   C CB  . THR A 33  ? 3.4506 2.8746 2.9232 0.6051  0.1718  -0.1814 63  THR A CB  
263   O OG1 . THR A 33  ? 3.4189 2.8382 2.9203 0.5704  0.1573  -0.2060 63  THR A OG1 
264   C CG2 . THR A 33  ? 3.3942 2.8902 2.8827 0.6283  0.1618  -0.1912 63  THR A CG2 
265   N N   . GLU A 34  ? 3.5123 2.8201 2.8913 0.6334  0.2192  -0.1165 64  GLU A N   
266   C CA  . GLU A 34  ? 3.5425 2.8362 2.8946 0.6446  0.2379  -0.0771 64  GLU A CA  
267   C C   . GLU A 34  ? 3.5033 2.8482 2.8526 0.6823  0.2418  -0.0672 64  GLU A C   
268   O O   . GLU A 34  ? 3.4334 2.8108 2.8088 0.6722  0.2392  -0.0623 64  GLU A O   
269   C CB  . GLU A 34  ? 3.6207 2.8831 2.9373 0.6706  0.2453  -0.0776 64  GLU A CB  
270   C CG  . GLU A 34  ? 3.6536 2.8561 2.9609 0.6409  0.2493  -0.0793 64  GLU A CG  
271   C CD  . GLU A 34  ? 3.6753 2.8804 2.9662 0.6638  0.2458  -0.0862 64  GLU A CD  
272   O OE1 . GLU A 34  ? 3.5921 2.8564 2.9057 0.6719  0.2242  -0.1112 64  GLU A OE1 
273   O OE2 . GLU A 34  ? 3.7743 2.9262 3.0340 0.6689  0.2636  -0.0647 64  GLU A OE2 
274   N N   . LYS A 35  ? 3.5698 2.9235 2.8887 0.7239  0.2472  -0.0639 65  LYS A N   
275   C CA  . LYS A 35  ? 3.5469 2.9492 2.8573 0.7572  0.2511  -0.0519 65  LYS A CA  
276   C C   . LYS A 35  ? 3.5994 2.9950 2.9074 0.7448  0.2692  -0.0140 65  LYS A C   
277   O O   . LYS A 35  ? 3.5987 3.0390 2.9239 0.7527  0.2695  -0.0116 65  LYS A O   
278   C CB  . LYS A 35  ? 3.4288 2.9029 2.7779 0.7542  0.2285  -0.0807 65  LYS A CB  
279   C CG  . LYS A 35  ? 3.3870 2.8927 2.7518 0.7475  0.2042  -0.1115 65  LYS A CG  
280   C CD  . LYS A 35  ? 3.4141 2.9210 2.7469 0.7735  0.2040  -0.1043 65  LYS A CD  
281   C CE  . LYS A 35  ? 3.3519 2.8848 2.7075 0.7606  0.1807  -0.1362 65  LYS A CE  
282   N NZ  . LYS A 35  ? 3.4338 2.9280 2.7691 0.7623  0.1824  -0.1335 65  LYS A NZ  
283   N N   . HIS A 36  ? 3.6042 2.9486 2.8949 0.7187  0.2832  0.0160  66  HIS A N   
284   C CA  . HIS A 36  ? 3.6357 2.9758 2.9256 0.6984  0.2997  0.0541  66  HIS A CA  
285   C C   . HIS A 36  ? 3.5166 2.8870 2.8507 0.6681  0.2927  0.0519  66  HIS A C   
286   O O   . HIS A 36  ? 3.3974 2.8088 2.7426 0.6793  0.2976  0.0621  66  HIS A O   
287   C CB  . HIS A 36  ? 3.6528 3.0116 2.9103 0.7364  0.3146  0.0769  66  HIS A CB  
288   C CG  . HIS A 36  ? 3.7604 3.0774 2.9723 0.7579  0.3249  0.0907  66  HIS A CG  
289   N ND1 . HIS A 36  ? 3.8201 3.1530 2.9967 0.8024  0.3325  0.1016  66  HIS A ND1 
290   C CD2 . HIS A 36  ? 3.8139 3.0719 3.0097 0.7396  0.3301  0.0975  66  HIS A CD2 
291   C CE1 . HIS A 36  ? 3.9111 3.1963 3.0523 0.8125  0.3406  0.1148  66  HIS A CE1 
292   N NE2 . HIS A 36  ? 3.9025 3.1414 3.0556 0.7751  0.3400  0.1120  66  HIS A NE2 
293   N N   . ASN A 37  ? 3.5772 2.9274 2.9372 0.6300  0.2808  0.0376  67  ASN A N   
294   C CA  . ASN A 37  ? 3.4518 2.8255 2.8546 0.5985  0.2722  0.0365  67  ASN A CA  
295   C C   . ASN A 37  ? 3.3137 2.7472 2.7427 0.6255  0.2609  0.0137  67  ASN A C   
296   O O   . ASN A 37  ? 3.2165 2.6867 2.6504 0.6425  0.2694  0.0279  67  ASN A O   
297   C CB  . ASN A 37  ? 3.4548 2.8242 2.8601 0.5744  0.2885  0.0758  67  ASN A CB  
298   C CG  . ASN A 37  ? 3.4277 2.7819 2.8644 0.5216  0.2824  0.0834  67  ASN A CG  
299   O OD1 . ASN A 37  ? 3.3792 2.7289 2.8379 0.5024  0.2651  0.0597  67  ASN A OD1 
300   N ND2 . ASN A 37  ? 3.4449 2.7950 2.8849 0.4976  0.2964  0.1165  67  ASN A ND2 
301   N N   . VAL A 38  ? 3.2465 2.6901 2.6929 0.6284  0.2428  -0.0225 68  VAL A N   
302   C CA  . VAL A 38  ? 3.0840 2.5821 2.5573 0.6510  0.2325  -0.0463 68  VAL A CA  
303   C C   . VAL A 38  ? 3.0204 2.5309 2.5373 0.6156  0.2256  -0.0399 68  VAL A C   
304   O O   . VAL A 38  ? 3.0211 2.5002 2.5518 0.5755  0.2172  -0.0400 68  VAL A O   
305   C CB  . VAL A 38  ? 3.0736 2.5776 2.5467 0.6689  0.2170  -0.0889 68  VAL A CB  
306   C CG1 . VAL A 38  ? 3.1001 2.6079 2.5344 0.7128  0.2230  -0.0957 68  VAL A CG1 
307   C CG2 . VAL A 38  ? 3.0896 2.5479 2.5680 0.6307  0.2070  -0.1008 68  VAL A CG2 
308   N N   . TRP A 39  ? 2.7735 2.3301 2.3120 0.6302  0.2294  -0.0336 69  TRP A N   
309   C CA  . TRP A 39  ? 2.7412 2.3160 2.3244 0.6020  0.2230  -0.0263 69  TRP A CA  
310   C C   . TRP A 39  ? 2.7570 2.2976 2.3438 0.5574  0.2289  0.0074  69  TRP A C   
311   O O   . TRP A 39  ? 2.7107 2.2536 2.2874 0.5568  0.2457  0.0378  69  TRP A O   
312   C CB  . TRP A 39  ? 2.7105 2.2933 2.3243 0.5928  0.2022  -0.0599 69  TRP A CB  
313   C CG  . TRP A 39  ? 2.7322 2.3446 2.3940 0.5761  0.1953  -0.0553 69  TRP A CG  
314   C CD1 . TRP A 39  ? 2.6633 2.2616 2.3557 0.5391  0.1800  -0.0583 69  TRP A CD1 
315   C CD2 . TRP A 39  ? 2.7598 2.4190 2.4445 0.5942  0.2041  -0.0438 69  TRP A CD2 
316   N NE1 . TRP A 39  ? 2.6736 2.3081 2.4082 0.5356  0.1773  -0.0502 69  TRP A NE1 
317   C CE2 . TRP A 39  ? 2.7229 2.3953 2.4549 0.5687  0.1926  -0.0419 69  TRP A CE2 
318   C CE3 . TRP A 39  ? 2.7147 2.4065 2.3845 0.6294  0.2206  -0.0357 69  TRP A CE3 
319   C CZ2 . TRP A 39  ? 2.6764 2.3937 2.4439 0.5783  0.1975  -0.0331 69  TRP A CZ2 
320   C CZ3 . TRP A 39  ? 2.6205 2.3567 2.3238 0.6370  0.2262  -0.0277 69  TRP A CZ3 
321   C CH2 . TRP A 39  ? 2.6698 2.4187 2.4230 0.6121  0.2149  -0.0270 69  TRP A CH2 
322   N N   . ALA A 40  ? 2.5843 2.0931 2.1843 0.5187  0.2158  0.0016  70  ALA A N   
323   C CA  . ALA A 40  ? 2.6463 2.1273 2.2550 0.4720  0.2189  0.0307  70  ALA A CA  
324   C C   . ALA A 40  ? 2.7682 2.1908 2.3493 0.4421  0.2200  0.0340  70  ALA A C   
325   O O   . ALA A 40  ? 2.8505 2.2464 2.4177 0.4176  0.2332  0.0632  70  ALA A O   
326   C CB  . ALA A 40  ? 2.5628 2.0621 2.2192 0.4438  0.2018  0.0268  70  ALA A CB  
327   N N   . THR A 41  ? 2.9967 2.3989 2.5701 0.4419  0.2075  0.0039  71  THR A N   
328   C CA  . THR A 41  ? 3.0708 2.4181 2.6239 0.4089  0.2071  0.0027  71  THR A CA  
329   C C   . THR A 41  ? 3.1396 2.4503 2.6526 0.4120  0.2275  0.0245  71  THR A C   
330   O O   . THR A 41  ? 3.1924 2.4904 2.6759 0.4424  0.2325  0.0113  71  THR A O   
331   C CB  . THR A 41  ? 3.0719 2.4086 2.6204 0.4175  0.1928  -0.0370 71  THR A CB  
332   O OG1 . THR A 41  ? 3.0635 2.4335 2.6472 0.4177  0.1751  -0.0582 71  THR A OG1 
333   C CG2 . THR A 41  ? 3.0936 2.3757 2.6296 0.3746  0.1904  -0.0401 71  THR A CG2 
334   N N   . HIS A 42  ? 3.3136 2.6073 2.8257 0.3806  0.2394  0.0579  72  HIS A N   
335   C CA  . HIS A 42  ? 3.4636 2.7161 2.9385 0.3760  0.2602  0.0809  72  HIS A CA  
336   C C   . HIS A 42  ? 3.5102 2.7177 2.9856 0.3196  0.2612  0.0923  72  HIS A C   
337   O O   . HIS A 42  ? 3.5923 2.7545 3.0443 0.3084  0.2645  0.0829  72  HIS A O   
338   C CB  . HIS A 42  ? 3.5242 2.7980 2.9907 0.3940  0.2788  0.1119  72  HIS A CB  
339   C CG  . HIS A 42  ? 3.6248 2.8556 3.0494 0.3953  0.3012  0.1347  72  HIS A CG  
340   N ND1 . HIS A 42  ? 3.7430 2.9321 3.1593 0.3509  0.3128  0.1573  72  HIS A ND1 
341   C CD2 . HIS A 42  ? 3.6700 2.8921 3.0581 0.4355  0.3144  0.1384  72  HIS A CD2 
342   C CE1 . HIS A 42  ? 3.8304 2.9845 3.2072 0.3638  0.3331  0.1736  72  HIS A CE1 
343   N NE2 . HIS A 42  ? 3.7944 2.9674 3.1532 0.4156  0.3339  0.1636  72  HIS A NE2 
344   N N   . ALA A 43  ? 3.1892 2.4093 2.6917 0.2831  0.2585  0.1116  73  ALA A N   
345   C CA  . ALA A 43  ? 3.1310 2.3140 2.6365 0.2263  0.2577  0.1221  73  ALA A CA  
346   C C   . ALA A 43  ? 3.0661 2.2663 2.6084 0.1983  0.2330  0.1064  73  ALA A C   
347   O O   . ALA A 43  ? 3.0808 2.2753 2.6403 0.1526  0.2286  0.1221  73  ALA A O   
348   C CB  . ALA A 43  ? 3.1783 2.3575 2.6821 0.2009  0.2754  0.1598  73  ALA A CB  
349   N N   . CYS A 44  ? 2.9669 2.1888 2.5211 0.2255  0.2166  0.0755  74  CYS A N   
350   C CA  . CYS A 44  ? 2.9036 2.1400 2.4906 0.2028  0.1931  0.0590  74  CYS A CA  
351   C C   . CYS A 44  ? 2.8475 2.0367 2.4207 0.1666  0.1855  0.0408  74  CYS A C   
352   O O   . CYS A 44  ? 2.8711 2.0294 2.4148 0.1793  0.1930  0.0247  74  CYS A O   
353   C CB  . CYS A 44  ? 2.8326 2.1116 2.4382 0.2456  0.1805  0.0331  74  CYS A CB  
354   S SG  . CYS A 44  ? 2.7998 2.1005 2.4496 0.2199  0.1530  0.0188  74  CYS A SG  
355   N N   . VAL A 45  ? 2.7265 1.9112 2.3216 0.1215  0.1704  0.0433  75  VAL A N   
356   C CA  . VAL A 45  ? 2.7360 1.8762 2.3191 0.0790  0.1630  0.0281  75  VAL A CA  
357   C C   . VAL A 45  ? 2.7016 1.8384 2.2816 0.0983  0.1500  -0.0125 75  VAL A C   
358   O O   . VAL A 45  ? 2.6547 1.8270 2.2589 0.1193  0.1349  -0.0278 75  VAL A O   
359   C CB  . VAL A 45  ? 2.7287 1.8705 2.3365 0.0266  0.1486  0.0432  75  VAL A CB  
360   C CG1 . VAL A 45  ? 2.7405 1.8367 2.3339 -0.0195 0.1410  0.0267  75  VAL A CG1 
361   C CG2 . VAL A 45  ? 2.7666 1.9135 2.3777 0.0061  0.1622  0.0820  75  VAL A CG2 
362   N N   . PRO A 46  ? 2.8601 1.9558 2.4117 0.0931  0.1567  -0.0317 76  PRO A N   
363   C CA  . PRO A 46  ? 2.8040 1.8947 2.3529 0.1059  0.1447  -0.0724 76  PRO A CA  
364   C C   . PRO A 46  ? 2.7516 1.8437 2.3229 0.0690  0.1225  -0.0853 76  PRO A C   
365   O O   . PRO A 46  ? 2.7556 1.8268 2.3304 0.0184  0.1183  -0.0696 76  PRO A O   
366   C CB  . PRO A 46  ? 2.8695 1.9102 2.3855 0.0948  0.1583  -0.0835 76  PRO A CB  
367   C CG  . PRO A 46  ? 2.9688 1.9987 2.4672 0.1027  0.1804  -0.0508 76  PRO A CG  
368   C CD  . PRO A 46  ? 2.9790 2.0323 2.4993 0.0803  0.1780  -0.0175 76  PRO A CD  
369   N N   . THR A 47  ? 2.8765 1.9930 2.4615 0.0941  0.1084  -0.1143 77  THR A N   
370   C CA  . THR A 47  ? 2.8761 1.9949 2.4819 0.0646  0.0869  -0.1283 77  THR A CA  
371   C C   . THR A 47  ? 2.9321 2.0031 2.5198 0.0187  0.0829  -0.1468 77  THR A C   
372   O O   . THR A 47  ? 2.9672 2.0114 2.5303 0.0259  0.0931  -0.1678 77  THR A O   
373   C CB  . THR A 47  ? 2.8434 1.9965 2.4648 0.1048  0.0759  -0.1581 77  THR A CB  
374   O OG1 . THR A 47  ? 2.7933 1.9906 2.4288 0.1493  0.0821  -0.1434 77  THR A OG1 
375   C CG2 . THR A 47  ? 2.7805 1.9377 2.4257 0.0761  0.0540  -0.1675 77  THR A CG2 
376   N N   . ASP A 48  ? 3.1127 2.1737 2.7131 -0.0292 0.0681  -0.1383 78  ASP A N   
377   C CA  . ASP A 48  ? 3.1859 2.2036 2.7708 -0.0787 0.0622  -0.1553 78  ASP A CA  
378   C C   . ASP A 48  ? 3.1752 2.1871 2.7528 -0.0606 0.0564  -0.2006 78  ASP A C   
379   O O   . ASP A 48  ? 3.1156 2.1559 2.7122 -0.0390 0.0427  -0.2161 78  ASP A O   
380   C CB  . ASP A 48  ? 3.1572 2.1749 2.7604 -0.1268 0.0435  -0.1381 78  ASP A CB  
381   C CG  . ASP A 48  ? 3.1628 2.1329 2.7457 -0.1876 0.0410  -0.1443 78  ASP A CG  
382   O OD1 . ASP A 48  ? 3.1641 2.1464 2.7478 -0.1845 0.0425  -0.1709 78  ASP A OD1 
383   O OD2 . ASP A 48  ? 3.1351 2.0986 2.7234 -0.2319 0.0350  -0.1171 78  ASP A OD2 
384   N N   . PRO A 49  ? 3.2045 2.1807 2.7560 -0.0686 0.0671  -0.2235 79  PRO A N   
385   C CA  . PRO A 49  ? 3.1471 2.1772 2.7259 -0.0481 0.0571  -0.2573 79  PRO A CA  
386   C C   . PRO A 49  ? 3.0974 2.1698 2.7141 -0.0684 0.0341  -0.2698 79  PRO A C   
387   O O   . PRO A 49  ? 3.0472 2.1597 2.6859 -0.0396 0.0267  -0.2952 79  PRO A O   
388   C CB  . PRO A 49  ? 3.1737 2.2100 2.7541 -0.0646 0.0655  -0.2598 79  PRO A CB  
389   C CG  . PRO A 49  ? 3.2182 2.2000 2.7613 -0.0669 0.0874  -0.2341 79  PRO A CG  
390   C CD  . PRO A 49  ? 3.2545 2.2053 2.7883 -0.0885 0.0847  -0.2072 79  PRO A CD  
391   N N   . ASN A 50  ? 3.1127 2.1839 2.7415 -0.1156 0.0234  -0.2512 80  ASN A N   
392   C CA  . ASN A 50  ? 3.0709 2.1810 2.7355 -0.1341 0.0030  -0.2582 80  ASN A CA  
393   C C   . ASN A 50  ? 3.0478 2.1355 2.7101 -0.1568 -0.0071 -0.2336 80  ASN A C   
394   O O   . ASN A 50  ? 3.0691 2.1590 2.7394 -0.1975 -0.0126 -0.2100 80  ASN A O   
395   C CB  . ASN A 50  ? 3.0975 2.2416 2.7869 -0.1642 -0.0032 -0.2585 80  ASN A CB  
396   C CG  . ASN A 50  ? 3.1551 2.3240 2.8531 -0.1426 0.0018  -0.2821 80  ASN A CG  
397   O OD1 . ASN A 50  ? 3.2229 2.3738 2.8995 -0.1168 0.0160  -0.2887 80  ASN A OD1 
398   N ND2 . ASN A 50  ? 3.1426 2.3537 2.8730 -0.1505 -0.0107 -0.2937 80  ASN A ND2 
399   N N   . PRO A 51  ? 2.9468 2.0167 2.6003 -0.1285 -0.0105 -0.2373 81  PRO A N   
400   C CA  . PRO A 51  ? 2.9041 1.9507 2.5583 -0.1484 -0.0238 -0.2120 81  PRO A CA  
401   C C   . PRO A 51  ? 2.8443 1.9304 2.5352 -0.1810 -0.0423 -0.2104 81  PRO A C   
402   O O   . PRO A 51  ? 2.8305 1.9571 2.5456 -0.1734 -0.0454 -0.2350 81  PRO A O   
403   C CB  . PRO A 51  ? 2.8584 1.9371 2.5297 -0.0928 -0.0245 -0.2164 81  PRO A CB  
404   C CG  . PRO A 51  ? 2.9103 1.9938 2.5638 -0.0489 -0.0060 -0.2395 81  PRO A CG  
405   C CD  . PRO A 51  ? 2.9158 1.9923 2.5618 -0.0733 -0.0037 -0.2632 81  PRO A CD  
406   N N   . GLN A 52  ? 2.8544 1.9324 2.5522 -0.2155 -0.0535 -0.1793 82  GLN A N   
407   C CA  . GLN A 52  ? 2.7669 1.8810 2.4964 -0.2444 -0.0688 -0.1723 82  GLN A CA  
408   C C   . GLN A 52  ? 2.6966 1.7993 2.4368 -0.2439 -0.0881 -0.1598 82  GLN A C   
409   O O   . GLN A 52  ? 2.6808 1.7497 2.4103 -0.2438 -0.0945 -0.1357 82  GLN A O   
410   C CB  . GLN A 52  ? 2.7828 1.9114 2.5177 -0.2842 -0.0667 -0.1460 82  GLN A CB  
411   C CG  . GLN A 52  ? 2.8070 1.9509 2.5373 -0.2859 -0.0520 -0.1580 82  GLN A CG  
412   C CD  . GLN A 52  ? 2.7298 1.9121 2.4833 -0.2769 -0.0553 -0.1841 82  GLN A CD  
413   O OE1 . GLN A 52  ? 2.6683 1.8712 2.4433 -0.2794 -0.0669 -0.1882 82  GLN A OE1 
414   N NE2 . GLN A 52  ? 2.7149 1.9065 2.4650 -0.2660 -0.0450 -0.2006 82  GLN A NE2 
415   N N   . GLU A 53  ? 2.5194 1.6505 2.2834 -0.2425 -0.0977 -0.1745 83  GLU A N   
416   C CA  . GLU A 53  ? 2.5057 1.6302 2.2844 -0.2421 -0.1180 -0.1640 83  GLU A CA  
417   C C   . GLU A 53  ? 2.4886 1.6468 2.2894 -0.2748 -0.1251 -0.1524 83  GLU A C   
418   O O   . GLU A 53  ? 2.4572 1.6455 2.2709 -0.2722 -0.1190 -0.1743 83  GLU A O   
419   C CB  . GLU A 53  ? 2.4847 1.6105 2.2688 -0.2028 -0.1206 -0.1954 83  GLU A CB  
420   C CG  . GLU A 53  ? 2.5403 1.6423 2.3097 -0.1548 -0.1176 -0.2084 83  GLU A CG  
421   C CD  . GLU A 53  ? 2.5950 1.7129 2.3759 -0.1167 -0.1188 -0.2426 83  GLU A CD  
422   O OE1 . GLU A 53  ? 2.5291 1.6655 2.3320 -0.1302 -0.1280 -0.2437 83  GLU A OE1 
423   O OE2 . GLU A 53  ? 2.6622 1.8003 2.4411 -0.0710 -0.1038 -0.2630 83  GLU A OE2 
424   N N   . ILE A 54  ? 2.3866 1.5422 2.1931 -0.3027 -0.1375 -0.1174 84  ILE A N   
425   C CA  . ILE A 54  ? 2.3780 1.5630 2.1992 -0.3303 -0.1441 -0.1045 84  ILE A CA  
426   C C   . ILE A 54  ? 2.3776 1.5557 2.2137 -0.3238 -0.1650 -0.0992 84  ILE A C   
427   O O   . ILE A 54  ? 2.4004 1.5591 2.2455 -0.3229 -0.1834 -0.0751 84  ILE A O   
428   C CB  . ILE A 54  ? 2.4115 1.6041 2.2313 -0.3616 -0.1458 -0.0708 84  ILE A CB  
429   C CG1 . ILE A 54  ? 2.4241 1.6234 2.2303 -0.3670 -0.1251 -0.0770 84  ILE A CG1 
430   C CG2 . ILE A 54  ? 2.4315 1.6488 2.2626 -0.3849 -0.1572 -0.0558 84  ILE A CG2 
431   C CD1 . ILE A 54  ? 2.4326 1.6019 2.2217 -0.3565 -0.1158 -0.0722 84  ILE A CD1 
432   N N   . HIS A 55  ? 2.4062 1.6015 2.2501 -0.3185 -0.1635 -0.1197 85  HIS A N   
433   C CA  . HIS A 55  ? 2.4303 1.6183 2.2877 -0.3120 -0.1824 -0.1160 85  HIS A CA  
434   C C   . HIS A 55  ? 2.4884 1.6857 2.3540 -0.3423 -0.1995 -0.0821 85  HIS A C   
435   O O   . HIS A 55  ? 2.5060 1.7253 2.3675 -0.3608 -0.1928 -0.0821 85  HIS A O   
436   C CB  . HIS A 55  ? 2.4154 1.6197 2.2769 -0.2967 -0.1710 -0.1497 85  HIS A CB  
437   C CG  . HIS A 55  ? 2.4720 1.6679 2.3455 -0.2903 -0.1882 -0.1475 85  HIS A CG  
438   N ND1 . HIS A 55  ? 2.4878 1.6574 2.3729 -0.2685 -0.2080 -0.1407 85  HIS A ND1 
439   C CD2 . HIS A 55  ? 2.4650 1.6741 2.3444 -0.2997 -0.1897 -0.1510 85  HIS A CD2 
440   C CE1 . HIS A 55  ? 2.5028 1.6705 2.4015 -0.2654 -0.2213 -0.1400 85  HIS A CE1 
441   N NE2 . HIS A 55  ? 2.4983 1.6875 2.3893 -0.2859 -0.2097 -0.1457 85  HIS A NE2 
442   N N   . LEU A 56  ? 2.2377 1.4201 2.1189 -0.3446 -0.2230 -0.0527 86  LEU A N   
443   C CA  . LEU A 56  ? 2.3294 1.5245 2.2221 -0.3719 -0.2420 -0.0176 86  LEU A CA  
444   C C   . LEU A 56  ? 2.4064 1.6025 2.3086 -0.3702 -0.2568 -0.0201 86  LEU A C   
445   O O   . LEU A 56  ? 2.3673 1.5485 2.2942 -0.3541 -0.2779 -0.0130 86  LEU A O   
446   C CB  . LEU A 56  ? 2.2819 1.4692 2.1997 -0.3735 -0.2619 0.0172  86  LEU A CB  
447   C CG  . LEU A 56  ? 2.2575 1.4357 2.1665 -0.3698 -0.2472 0.0197  86  LEU A CG  
448   C CD1 . LEU A 56  ? 2.2655 1.4452 2.2075 -0.3754 -0.2659 0.0605  86  LEU A CD1 
449   C CD2 . LEU A 56  ? 2.2659 1.4617 2.1459 -0.3914 -0.2224 0.0128  86  LEU A CD2 
450   N N   . GLU A 57  ? 2.5583 1.7712 2.4443 -0.3845 -0.2454 -0.0307 87  GLU A N   
451   C CA  . GLU A 57  ? 2.5424 1.7543 2.4320 -0.3853 -0.2564 -0.0331 87  GLU A CA  
452   C C   . GLU A 57  ? 2.5557 1.7648 2.4625 -0.4007 -0.2886 0.0062  87  GLU A C   
453   O O   . GLU A 57  ? 2.5216 1.7418 2.4309 -0.4199 -0.2965 0.0340  87  GLU A O   
454   C CB  . GLU A 57  ? 2.4772 1.7089 2.3491 -0.3979 -0.2377 -0.0488 87  GLU A CB  
455   C CG  . GLU A 57  ? 2.4422 1.6720 2.3144 -0.3957 -0.2417 -0.0591 87  GLU A CG  
456   C CD  . GLU A 57  ? 2.3697 1.5923 2.2499 -0.3681 -0.2303 -0.0917 87  GLU A CD  
457   O OE1 . GLU A 57  ? 2.3370 1.5624 2.2182 -0.3510 -0.2137 -0.1128 87  GLU A OE1 
458   O OE2 . GLU A 57  ? 2.3901 1.6045 2.2746 -0.3634 -0.2378 -0.0966 87  GLU A OE2 
459   N N   . ASN A 58  ? 2.4627 1.6593 2.3847 -0.3915 -0.3073 0.0087  88  ASN A N   
460   C CA  . ASN A 58  ? 2.4797 1.6746 2.4256 -0.4030 -0.3409 0.0458  88  ASN A CA  
461   C C   . ASN A 58  ? 2.4731 1.6682 2.4584 -0.3974 -0.3615 0.0757  88  ASN A C   
462   O O   . ASN A 58  ? 2.4368 1.6384 2.4519 -0.4072 -0.3899 0.1107  88  ASN A O   
463   C CB  . ASN A 58  ? 2.5245 1.7370 2.4495 -0.4350 -0.3449 0.0656  88  ASN A CB  
464   C CG  . ASN A 58  ? 2.5269 1.7370 2.4278 -0.4401 -0.3368 0.0479  88  ASN A CG  
465   O OD1 . ASN A 58  ? 2.5987 1.7935 2.5050 -0.4234 -0.3372 0.0306  88  ASN A OD1 
466   N ND2 . ASN A 58  ? 2.3821 1.6074 2.2578 -0.4627 -0.3293 0.0526  88  ASN A ND2 
467   N N   . VAL A 59  ? 2.4958 1.6859 2.4863 -0.3813 -0.3483 0.0646  89  VAL A N   
468   C CA  . VAL A 59  ? 2.4459 1.6391 2.4772 -0.3758 -0.3635 0.0941  89  VAL A CA  
469   C C   . VAL A 59  ? 2.3676 1.5406 2.4455 -0.3370 -0.3773 0.0881  89  VAL A C   
470   O O   . VAL A 59  ? 2.3274 1.4870 2.3924 -0.3076 -0.3603 0.0504  89  VAL A O   
471   C CB  . VAL A 59  ? 2.3704 1.5684 2.3804 -0.3815 -0.3404 0.0892  89  VAL A CB  
472   C CG1 . VAL A 59  ? 2.3274 1.5284 2.3831 -0.3730 -0.3532 0.1200  89  VAL A CG1 
473   C CG2 . VAL A 59  ? 2.4278 1.6480 2.4017 -0.4157 -0.3268 0.0956  89  VAL A CG2 
474   N N   . THR A 60  ? 2.2922 1.5004 2.4242 -0.3198 -0.3927 0.1205  90  THR A N   
475   C CA  . THR A 60  ? 2.2628 1.5069 2.4434 -0.2605 -0.3849 0.1139  90  THR A CA  
476   C C   . THR A 60  ? 2.2567 1.5578 2.4801 -0.2367 -0.3762 0.1411  90  THR A C   
477   O O   . THR A 60  ? 2.2896 1.6140 2.5449 -0.2530 -0.3954 0.1792  90  THR A O   
478   C CB  . THR A 60  ? 2.2993 1.5351 2.5102 -0.2560 -0.4098 0.1242  90  THR A CB  
479   O OG1 . THR A 60  ? 2.3550 1.5361 2.5234 -0.2782 -0.4156 0.0969  90  THR A OG1 
480   C CG2 . THR A 60  ? 2.2890 1.5620 2.5523 -0.1950 -0.3999 0.1162  90  THR A CG2 
481   N N   . GLU A 61  ? 1.9879 1.3119 2.2112 -0.1995 -0.3478 0.1217  91  GLU A N   
482   C CA  . GLU A 61  ? 1.9852 1.3616 2.2438 -0.1760 -0.3353 0.1434  91  GLU A CA  
483   C C   . GLU A 61  ? 1.9713 1.3851 2.2728 -0.1148 -0.3211 0.1297  91  GLU A C   
484   O O   . GLU A 61  ? 1.9534 1.3536 2.2397 -0.0863 -0.3070 0.0932  91  GLU A O   
485   C CB  . GLU A 61  ? 1.9743 1.3476 2.1940 -0.1875 -0.3122 0.1371  91  GLU A CB  
486   C CG  . GLU A 61  ? 1.9780 1.4008 2.2284 -0.1738 -0.3003 0.1638  91  GLU A CG  
487   C CD  . GLU A 61  ? 2.0062 1.4419 2.2724 -0.2162 -0.3201 0.2054  91  GLU A CD  
488   O OE1 . GLU A 61  ? 2.0236 1.4281 2.2729 -0.2591 -0.3434 0.2146  91  GLU A OE1 
489   O OE2 . GLU A 61  ? 2.0128 1.4911 2.3084 -0.2073 -0.3123 0.2286  91  GLU A OE2 
490   N N   . GLU A 62  ? 1.9705 1.4333 2.3263 -0.0956 -0.3242 0.1580  92  GLU A N   
491   C CA  . GLU A 62  ? 1.9945 1.4976 2.3965 -0.0393 -0.3106 0.1481  92  GLU A CA  
492   C C   . GLU A 62  ? 1.9561 1.4874 2.3491 -0.0120 -0.2796 0.1374  92  GLU A C   
493   O O   . GLU A 62  ? 1.9279 1.4772 2.3176 -0.0291 -0.2738 0.1600  92  GLU A O   
494   C CB  . GLU A 62  ? 2.0514 1.5956 2.5198 -0.0292 -0.3276 0.1819  92  GLU A CB  
495   C CG  . GLU A 62  ? 2.1270 1.6479 2.6114 -0.0508 -0.3596 0.1966  92  GLU A CG  
496   C CD  . GLU A 62  ? 2.3251 1.8912 2.8799 -0.0348 -0.3749 0.2292  92  GLU A CD  
497   O OE1 . GLU A 62  ? 2.3626 1.9781 2.9555 -0.0020 -0.3580 0.2341  92  GLU A OE1 
498   O OE2 . GLU A 62  ? 2.4541 2.0068 3.0266 -0.0549 -0.4038 0.2499  92  GLU A OE2 
499   N N   . PHE A 63  ? 2.0105 1.5449 2.3985 0.0296  -0.2599 0.1029  93  PHE A N   
500   C CA  . PHE A 63  ? 2.0006 1.5616 2.3797 0.0617  -0.2304 0.0895  93  PHE A CA  
501   C C   . PHE A 63  ? 2.0328 1.6459 2.4688 0.1094  -0.2205 0.0920  93  PHE A C   
502   O O   . PHE A 63  ? 2.0611 1.6848 2.5409 0.1227  -0.2343 0.0961  93  PHE A O   
503   C CB  . PHE A 63  ? 1.9557 1.4854 2.2852 0.0741  -0.2145 0.0474  93  PHE A CB  
504   C CG  . PHE A 63  ? 1.9085 1.3945 2.1799 0.0320  -0.2154 0.0434  93  PHE A CG  
505   C CD1 . PHE A 63  ? 1.9497 1.3900 2.1969 -0.0064 -0.2355 0.0388  93  PHE A CD1 
506   C CD2 . PHE A 63  ? 1.8744 1.3636 2.1150 0.0306  -0.1954 0.0438  93  PHE A CD2 
507   C CE1 . PHE A 63  ? 1.9582 1.3587 2.1531 -0.0460 -0.2349 0.0333  93  PHE A CE1 
508   C CE2 . PHE A 63  ? 1.8699 1.3181 2.0592 -0.0075 -0.1948 0.0391  93  PHE A CE2 
509   C CZ  . PHE A 63  ? 1.8765 1.2811 2.0436 -0.0461 -0.2143 0.0331  93  PHE A CZ  
510   N N   . ASN A 64  ? 1.9720 1.6172 2.4071 0.1349  -0.1955 0.0897  94  ASN A N   
511   C CA  . ASN A 64  ? 1.9936 1.6900 2.4790 0.1803  -0.1820 0.0893  94  ASN A CA  
512   C C   . ASN A 64  ? 1.9667 1.6788 2.4247 0.2101  -0.1515 0.0691  94  ASN A C   
513   O O   . ASN A 64  ? 2.1459 1.8751 2.5945 0.2034  -0.1390 0.0871  94  ASN A O   
514   C CB  . ASN A 64  ? 2.0256 1.7613 2.5614 0.1710  -0.1911 0.1291  94  ASN A CB  
515   C CG  . ASN A 64  ? 2.0388 1.8234 2.6369 0.2142  -0.1837 0.1286  94  ASN A CG  
516   O OD1 . ASN A 64  ? 2.0121 1.8109 2.6102 0.2537  -0.1629 0.1007  94  ASN A OD1 
517   N ND2 . ASN A 64  ? 2.0895 1.9017 2.7421 0.2067  -0.2004 0.1590  94  ASN A ND2 
518   N N   . MET A 65  ? 2.0690 1.7749 2.5135 0.2422  -0.1397 0.0319  95  MET A N   
519   C CA  . MET A 65  ? 2.0008 1.7200 2.4159 0.2719  -0.1123 0.0102  95  MET A CA  
520   C C   . MET A 65  ? 2.0771 1.8515 2.5300 0.3050  -0.0939 0.0213  95  MET A C   
521   O O   . MET A 65  ? 2.0767 1.8645 2.5035 0.3219  -0.0717 0.0150  95  MET A O   
522   C CB  . MET A 65  ? 1.9620 1.6657 2.3575 0.2983  -0.1056 -0.0333 95  MET A CB  
523   C CG  . MET A 65  ? 2.0498 1.7751 2.4949 0.3279  -0.1088 -0.0461 95  MET A CG  
524   S SD  . MET A 65  ? 2.0011 1.7131 2.4218 0.3599  -0.0969 -0.0996 95  MET A SD  
525   C CE  . MET A 65  ? 1.9145 1.6567 2.3042 0.3914  -0.0664 -0.1129 95  MET A CE  
526   N N   . TRP A 66  ? 2.0511 1.8576 2.5646 0.3149  -0.1021 0.0374  96  TRP A N   
527   C CA  . TRP A 66  ? 2.0655 1.9261 2.6183 0.3468  -0.0836 0.0452  96  TRP A CA  
528   C C   . TRP A 66  ? 2.0667 1.9503 2.6352 0.3246  -0.0837 0.0839  96  TRP A C   
529   O O   . TRP A 66  ? 2.0822 2.0078 2.6709 0.3464  -0.0644 0.0908  96  TRP A O   
530   C CB  . TRP A 66  ? 2.0717 1.9582 2.6864 0.3730  -0.0897 0.0391  96  TRP A CB  
531   C CG  . TRP A 66  ? 2.0534 1.9172 2.6557 0.3930  -0.0894 0.0010  96  TRP A CG  
532   C CD1 . TRP A 66  ? 2.0607 1.8918 2.6707 0.3803  -0.1107 -0.0064 96  TRP A CD1 
533   C CD2 . TRP A 66  ? 2.0093 1.8821 2.5889 0.4285  -0.0665 -0.0355 96  TRP A CD2 
534   N NE1 . TRP A 66  ? 2.0265 1.8449 2.6200 0.4050  -0.1013 -0.0463 96  TRP A NE1 
535   C CE2 . TRP A 66  ? 1.9796 1.8248 2.5549 0.4349  -0.0747 -0.0651 96  TRP A CE2 
536   C CE3 . TRP A 66  ? 2.0030 1.9046 2.5639 0.4547  -0.0400 -0.0459 96  TRP A CE3 
537   C CZ2 . TRP A 66  ? 1.9546 1.8025 2.5092 0.4660  -0.0573 -0.1053 96  TRP A CZ2 
538   C CZ3 . TRP A 66  ? 2.0112 1.9156 2.5509 0.4862  -0.0239 -0.0846 96  TRP A CZ3 
539   C CH2 . TRP A 66  ? 1.9898 1.8688 2.5273 0.4915  -0.0326 -0.1144 96  TRP A CH2 
540   N N   . LYS A 67  ? 1.9715 1.8289 2.5295 0.2806  -0.1041 0.1080  97  LYS A N   
541   C CA  . LYS A 67  ? 1.9659 1.8403 2.5329 0.2527  -0.1056 0.1441  97  LYS A CA  
542   C C   . LYS A 67  ? 2.0037 1.8349 2.5089 0.2143  -0.1067 0.1491  97  LYS A C   
543   O O   . LYS A 67  ? 2.0828 1.9059 2.5874 0.1742  -0.1203 0.1770  97  LYS A O   
544   C CB  . LYS A 67  ? 2.0783 1.9706 2.7020 0.2346  -0.1306 0.1726  97  LYS A CB  
545   C CG  . LYS A 67  ? 2.1554 2.0911 2.8450 0.2732  -0.1287 0.1684  97  LYS A CG  
546   C CD  . LYS A 67  ? 2.2423 2.2262 2.9489 0.3039  -0.0998 0.1677  97  LYS A CD  
547   C CE  . LYS A 67  ? 2.3033 2.3304 3.0755 0.3431  -0.0954 0.1600  97  LYS A CE  
548   N NZ  . LYS A 67  ? 2.4145 2.4890 3.2025 0.3728  -0.0660 0.1572  97  LYS A NZ  
549   N N   . ASN A 68  ? 1.9171 1.7214 2.3704 0.2262  -0.0918 0.1216  98  ASN A N   
550   C CA  . ASN A 68  ? 1.9119 1.6736 2.3060 0.1936  -0.0901 0.1224  98  ASN A CA  
551   C C   . ASN A 68  ? 1.9159 1.6958 2.2891 0.2045  -0.0634 0.1303  98  ASN A C   
552   O O   . ASN A 68  ? 1.9078 1.7113 2.2808 0.2449  -0.0430 0.1136  98  ASN A O   
553   C CB  . ASN A 68  ? 1.8872 1.6065 2.2381 0.1986  -0.0917 0.0870  98  ASN A CB  
554   C CG  . ASN A 68  ? 1.8873 1.5616 2.1786 0.1657  -0.0891 0.0854  98  ASN A CG  
555   O OD1 . ASN A 68  ? 1.8788 1.5427 2.1305 0.1824  -0.0701 0.0670  98  ASN A OD1 
556   N ND2 . ASN A 68  ? 1.8998 1.5471 2.1846 0.1185  -0.1086 0.1042  98  ASN A ND2 
557   N N   . ASN A 69  ? 1.7621 1.5296 2.1160 0.1673  -0.0632 0.1556  99  ASN A N   
558   C CA  . ASN A 69  ? 1.8868 1.6708 2.2241 0.1724  -0.0386 0.1688  99  ASN A CA  
559   C C   . ASN A 69  ? 1.8511 1.6012 2.1260 0.1802  -0.0204 0.1490  99  ASN A C   
560   O O   . ASN A 69  ? 1.9039 1.6660 2.1606 0.1932  0.0027  0.1554  99  ASN A O   
561   C CB  . ASN A 69  ? 2.0161 1.8033 2.3621 0.1284  -0.0452 0.2046  99  ASN A CB  
562   C CG  . ASN A 69  ? 2.1220 1.9347 2.4634 0.1345  -0.0198 0.2216  99  ASN A CG  
563   O OD1 . ASN A 69  ? 2.1561 1.9416 2.4516 0.1159  -0.0064 0.2268  99  ASN A OD1 
564   N ND2 . ASN A 69  ? 2.1153 1.9800 2.5048 0.1605  -0.0122 0.2300  99  ASN A ND2 
565   N N   . MET A 70  ? 2.0816 1.7898 2.3236 0.1726  -0.0301 0.1253  100 MET A N   
566   C CA  . MET A 70  ? 2.0195 1.6965 2.2049 0.1820  -0.0140 0.1048  100 MET A CA  
567   C C   . MET A 70  ? 1.9892 1.6954 2.1739 0.2347  0.0063  0.0848  100 MET A C   
568   O O   . MET A 70  ? 1.9949 1.6913 2.1394 0.2489  0.0257  0.0781  100 MET A O   
569   C CB  . MET A 70  ? 1.8601 1.4921 2.0185 0.1652  -0.0298 0.0805  100 MET A CB  
570   C CG  . MET A 70  ? 1.8639 1.4681 2.0235 0.1120  -0.0514 0.0994  100 MET A CG  
571   S SD  . MET A 70  ? 1.6634 1.2130 1.7897 0.0875  -0.0694 0.0711  100 MET A SD  
572   C CE  . MET A 70  ? 1.5984 1.1134 1.6613 0.0919  -0.0470 0.0517  100 MET A CE  
573   N N   . VAL A 71  ? 1.9098 1.6515 2.1384 0.2636  0.0021  0.0754  101 VAL A N   
574   C CA  . VAL A 71  ? 1.8774 1.6516 2.1099 0.3128  0.0210  0.0559  101 VAL A CA  
575   C C   . VAL A 71  ? 1.9682 1.7765 2.2081 0.3237  0.0420  0.0790  101 VAL A C   
576   O O   . VAL A 71  ? 1.9370 1.7509 2.1458 0.3491  0.0632  0.0708  101 VAL A O   
577   C CB  . VAL A 71  ? 1.8251 1.6262 2.1054 0.3372  0.0110  0.0394  101 VAL A CB  
578   C CG1 . VAL A 71  ? 1.7945 1.6327 2.0804 0.3860  0.0319  0.0196  101 VAL A CG1 
579   C CG2 . VAL A 71  ? 1.6984 1.4628 1.9667 0.3265  -0.0078 0.0148  101 VAL A CG2 
580   N N   . GLU A 72  ? 1.9160 1.7480 2.1970 0.3040  0.0362  0.1085  102 GLU A N   
581   C CA  . GLU A 72  ? 1.9499 1.8165 2.2428 0.3107  0.0558  0.1312  102 GLU A CA  
582   C C   . GLU A 72  ? 1.9598 1.7981 2.2000 0.2919  0.0711  0.1447  102 GLU A C   
583   O O   . GLU A 72  ? 1.9168 1.7764 2.1494 0.3056  0.0933  0.1560  102 GLU A O   
584   C CB  . GLU A 72  ? 2.0244 1.9203 2.3736 0.2884  0.0433  0.1594  102 GLU A CB  
585   C CG  . GLU A 72  ? 2.0053 1.9287 2.4114 0.3066  0.0278  0.1492  102 GLU A CG  
586   C CD  . GLU A 72  ? 1.9362 1.9010 2.3644 0.3551  0.0462  0.1308  102 GLU A CD  
587   O OE1 . GLU A 72  ? 1.9808 1.9677 2.3968 0.3702  0.0701  0.1367  102 GLU A OE1 
588   O OE2 . GLU A 72  ? 1.9184 1.8927 2.3750 0.3771  0.0375  0.1098  102 GLU A OE2 
589   N N   . GLN A 73  ? 2.0508 1.8403 2.2545 0.2600  0.0605  0.1437  103 GLN A N   
590   C CA  . GLN A 73  ? 2.0490 1.8055 2.2010 0.2420  0.0752  0.1540  103 GLN A CA  
591   C C   . GLN A 73  ? 1.9614 1.7017 2.0669 0.2759  0.0910  0.1286  103 GLN A C   
592   O O   . GLN A 73  ? 1.9299 1.6674 2.0038 0.2856  0.1126  0.1371  103 GLN A O   
593   C CB  . GLN A 73  ? 2.1582 1.8691 2.2912 0.1934  0.0579  0.1611  103 GLN A CB  
594   C CG  . GLN A 73  ? 2.2788 2.0022 2.4479 0.1534  0.0439  0.1910  103 GLN A CG  
595   C CD  . GLN A 73  ? 2.3425 2.0193 2.4858 0.1037  0.0293  0.1974  103 GLN A CD  
596   O OE1 . GLN A 73  ? 2.2397 1.8735 2.3345 0.0972  0.0349  0.1830  103 GLN A OE1 
597   N NE2 . GLN A 73  ? 2.3784 2.0645 2.5545 0.0684  0.0102  0.2185  103 GLN A NE2 
598   N N   . MET A 74  ? 2.0760 1.8059 2.1769 0.2939  0.0801  0.0976  104 MET A N   
599   C CA  . MET A 74  ? 1.9828 1.7013 2.0426 0.3272  0.0926  0.0709  104 MET A CA  
600   C C   . MET A 74  ? 1.9346 1.6960 2.0006 0.3712  0.1131  0.0678  104 MET A C   
601   O O   . MET A 74  ? 1.8949 1.6493 1.9202 0.3915  0.1308  0.0636  104 MET A O   
602   C CB  . MET A 74  ? 1.8795 1.5829 1.9390 0.3355  0.0761  0.0372  104 MET A CB  
603   C CG  . MET A 74  ? 1.7678 1.4656 1.7895 0.3716  0.0873  0.0070  104 MET A CG  
604   S SD  . MET A 74  ? 1.6416 1.3228 1.6633 0.3787  0.0690  -0.0345 104 MET A SD  
605   C CE  . MET A 74  ? 1.6531 1.3250 1.6217 0.4144  0.0850  -0.0625 104 MET A CE  
606   N N   . HIS A 75  ? 2.0416 1.8478 2.1582 0.3866  0.1111  0.0696  105 HIS A N   
607   C CA  . HIS A 75  ? 1.9904 1.8397 2.1150 0.4272  0.1310  0.0647  105 HIS A CA  
608   C C   . HIS A 75  ? 1.9828 1.8369 2.0851 0.4235  0.1529  0.0917  105 HIS A C   
609   O O   . HIS A 75  ? 1.9295 1.7912 1.9999 0.4526  0.1721  0.0852  105 HIS A O   
610   C CB  . HIS A 75  ? 2.0059 1.9004 2.1941 0.4386  0.1247  0.0642  105 HIS A CB  
611   C CG  . HIS A 75  ? 1.9639 1.9048 2.1648 0.4801  0.1445  0.0545  105 HIS A CG  
612   N ND1 . HIS A 75  ? 1.9735 1.9199 2.1477 0.5166  0.1538  0.0247  105 HIS A ND1 
613   C CD2 . HIS A 75  ? 2.0096 1.9948 2.2468 0.4897  0.1575  0.0701  105 HIS A CD2 
614   C CE1 . HIS A 75  ? 1.9514 1.9426 2.1434 0.5462  0.1715  0.0225  105 HIS A CE1 
615   N NE2 . HIS A 75  ? 1.9896 2.0046 2.2202 0.5307  0.1746  0.0495  105 HIS A NE2 
616   N N   . THR A 76  ? 1.9524 1.8013 2.0693 0.3867  0.1504  0.1221  106 THR A N   
617   C CA  . THR A 76  ? 1.9442 1.7945 2.0402 0.3780  0.1715  0.1487  106 THR A CA  
618   C C   . THR A 76  ? 1.9146 1.7160 1.9465 0.3703  0.1810  0.1495  106 THR A C   
619   O O   . THR A 76  ? 1.9288 1.7277 1.9323 0.3737  0.2024  0.1661  106 THR A O   
620   C CB  . THR A 76  ? 2.0220 1.8809 2.1529 0.3382  0.1651  0.1792  106 THR A CB  
621   O OG1 . THR A 76  ? 2.2014 2.0239 2.3310 0.3014  0.1424  0.1804  106 THR A OG1 
622   C CG2 . THR A 76  ? 2.0176 1.9312 2.2136 0.3509  0.1606  0.1817  106 THR A CG2 
623   N N   . ASP A 77  ? 1.9558 1.7176 1.9649 0.3600  0.1660  0.1318  107 ASP A N   
624   C CA  . ASP A 77  ? 1.9611 1.6757 1.9122 0.3543  0.1743  0.1298  107 ASP A CA  
625   C C   . ASP A 77  ? 1.9177 1.6389 1.8358 0.4007  0.1878  0.1085  107 ASP A C   
626   O O   . ASP A 77  ? 1.9105 1.6147 1.7864 0.4094  0.2060  0.1180  107 ASP A O   
627   C CB  . ASP A 77  ? 2.0585 1.7301 1.9997 0.3243  0.1538  0.1176  107 ASP A CB  
628   C CG  . ASP A 77  ? 2.1600 1.8123 2.1134 0.2723  0.1454  0.1438  107 ASP A CG  
629   O OD1 . ASP A 77  ? 2.1586 1.8405 2.1425 0.2615  0.1501  0.1682  107 ASP A OD1 
630   O OD2 . ASP A 77  ? 2.1914 1.8011 2.1247 0.2415  0.1343  0.1393  107 ASP A OD2 
631   N N   . ILE A 78  ? 2.0677 1.8127 2.0037 0.4302  0.1788  0.0797  108 ILE A N   
632   C CA  . ILE A 78  ? 2.0099 1.7660 1.9165 0.4744  0.1898  0.0571  108 ILE A CA  
633   C C   . ILE A 78  ? 1.9707 1.7627 1.8750 0.4994  0.2126  0.0723  108 ILE A C   
634   O O   . ILE A 78  ? 1.9615 1.7498 1.8242 0.5256  0.2277  0.0691  108 ILE A O   
635   C CB  . ILE A 78  ? 1.9829 1.7588 1.9131 0.4967  0.1752  0.0220  108 ILE A CB  
636   C CG1 . ILE A 78  ? 1.9921 1.7315 1.9268 0.4661  0.1528  0.0099  108 ILE A CG1 
637   C CG2 . ILE A 78  ? 1.9199 1.7041 1.8157 0.5389  0.1843  -0.0043 108 ILE A CG2 
638   C CD1 . ILE A 78  ? 1.9237 1.6757 1.8786 0.4836  0.1384  -0.0250 108 ILE A CD1 
639   N N   . ILE A 79  ? 2.0065 1.8341 1.9553 0.4916  0.2154  0.0892  109 ILE A N   
640   C CA  . ILE A 79  ? 2.0662 1.9288 2.0148 0.5118  0.2382  0.1040  109 ILE A CA  
641   C C   . ILE A 79  ? 2.0855 1.9182 1.9906 0.4963  0.2557  0.1317  109 ILE A C   
642   O O   . ILE A 79  ? 2.1559 1.9928 2.0247 0.5218  0.2749  0.1345  109 ILE A O   
643   C CB  . ILE A 79  ? 2.0800 1.9876 2.0902 0.5045  0.2371  0.1153  109 ILE A CB  
644   C CG1 . ILE A 79  ? 2.0353 1.9772 2.0864 0.5293  0.2256  0.0866  109 ILE A CG1 
645   C CG2 . ILE A 79  ? 2.1764 2.1141 2.1835 0.5160  0.2624  0.1348  109 ILE A CG2 
646   C CD1 . ILE A 79  ? 2.0245 2.0118 2.1394 0.5253  0.2251  0.0969  109 ILE A CD1 
647   N N   . SER A 80  ? 2.0727 1.8736 1.9788 0.4539  0.2498  0.1526  110 SER A N   
648   C CA  . SER A 80  ? 2.1367 1.9055 2.0006 0.4374  0.2677  0.1781  110 SER A CA  
649   C C   . SER A 80  ? 2.1195 1.8482 1.9255 0.4551  0.2720  0.1655  110 SER A C   
650   O O   . SER A 80  ? 2.1838 1.8939 1.9478 0.4616  0.2917  0.1811  110 SER A O   
651   C CB  . SER A 80  ? 2.1450 1.8878 2.0223 0.3863  0.2597  0.2000  110 SER A CB  
652   O OG  . SER A 80  ? 2.1480 1.8570 2.0217 0.3689  0.2384  0.1839  110 SER A OG  
653   N N   . LEU A 81  ? 2.1563 1.8705 1.9599 0.4627  0.2539  0.1376  111 LEU A N   
654   C CA  . LEU A 81  ? 2.1811 1.8627 1.9344 0.4830  0.2566  0.1222  111 LEU A CA  
655   C C   . LEU A 81  ? 2.1897 1.9007 1.9208 0.5302  0.2720  0.1145  111 LEU A C   
656   O O   . LEU A 81  ? 2.2290 1.9165 1.9117 0.5458  0.2850  0.1201  111 LEU A O   
657   C CB  . LEU A 81  ? 2.1790 1.8472 1.9406 0.4820  0.2339  0.0908  111 LEU A CB  
658   C CG  . LEU A 81  ? 2.3058 1.9232 2.0268 0.4754  0.2290  0.0785  111 LEU A CG  
659   C CD1 . LEU A 81  ? 2.2221 1.8383 1.9646 0.4712  0.2061  0.0473  111 LEU A CD1 
660   C CD2 . LEU A 81  ? 2.4712 2.0826 2.1450 0.5142  0.2429  0.0714  111 LEU A CD2 
661   N N   . TRP A 82  ? 2.2577 2.0200 2.0236 0.5530  0.2708  0.1021  112 TRP A N   
662   C CA  . TRP A 82  ? 2.2343 2.0297 1.9818 0.5968  0.2849  0.0925  112 TRP A CA  
663   C C   . TRP A 82  ? 2.3106 2.1075 2.0321 0.5986  0.3096  0.1232  112 TRP A C   
664   O O   . TRP A 82  ? 2.4225 2.2165 2.0999 0.6272  0.3229  0.1233  112 TRP A O   
665   C CB  . TRP A 82  ? 2.2692 2.1191 2.0658 0.6145  0.2797  0.0739  112 TRP A CB  
666   C CG  . TRP A 82  ? 2.3700 2.2553 2.1525 0.6599  0.2875  0.0512  112 TRP A CG  
667   C CD1 . TRP A 82  ? 2.4207 2.3459 2.2035 0.6825  0.3064  0.0580  112 TRP A CD1 
668   C CD2 . TRP A 82  ? 2.3956 2.2841 2.1659 0.6863  0.2763  0.0160  112 TRP A CD2 
669   N NE1 . TRP A 82  ? 2.4501 2.4019 2.2183 0.7213  0.3077  0.0301  112 TRP A NE1 
670   C CE2 . TRP A 82  ? 2.4656 2.3966 2.2268 0.7246  0.2893  0.0038  112 TRP A CE2 
671   C CE3 . TRP A 82  ? 2.3265 2.1867 2.0916 0.6802  0.2573  -0.0071 112 TRP A CE3 
672   C CZ2 . TRP A 82  ? 2.4485 2.3953 2.1958 0.7567  0.2833  -0.0304 112 TRP A CZ2 
673   C CZ3 . TRP A 82  ? 2.3426 2.2184 2.0950 0.7123  0.2519  -0.0414 112 TRP A CZ3 
674   C CH2 . TRP A 82  ? 2.4090 2.3283 2.1527 0.7502  0.2646  -0.0528 112 TRP A CH2 
675   N N   . ASP A 83  ? 2.0162 1.8168 1.7632 0.5673  0.3160  0.1497  113 ASP A N   
676   C CA  . ASP A 83  ? 2.1167 1.9201 1.8412 0.5664  0.3409  0.1785  113 ASP A CA  
677   C C   . ASP A 83  ? 2.1149 1.8613 1.7846 0.5539  0.3500  0.1962  113 ASP A C   
678   O O   . ASP A 83  ? 2.2027 1.9413 1.8297 0.5717  0.3697  0.2097  113 ASP A O   
679   C CB  . ASP A 83  ? 2.1186 1.9469 1.8899 0.5365  0.3452  0.1997  113 ASP A CB  
680   C CG  . ASP A 83  ? 2.1544 2.0409 1.9819 0.5521  0.3389  0.1833  113 ASP A CG  
681   O OD1 . ASP A 83  ? 2.1696 2.0684 2.0090 0.5738  0.3240  0.1539  113 ASP A OD1 
682   O OD2 . ASP A 83  ? 2.2575 2.1780 2.1175 0.5433  0.3499  0.1988  113 ASP A OD2 
683   N N   . GLN A 84  ? 2.2441 1.9491 1.9140 0.5227  0.3362  0.1966  114 GLN A N   
684   C CA  . GLN A 84  ? 2.3453 1.9932 1.9664 0.5085  0.3450  0.2118  114 GLN A CA  
685   C C   . GLN A 84  ? 2.3718 2.0025 1.9463 0.5468  0.3459  0.1948  114 GLN A C   
686   O O   . GLN A 84  ? 2.4148 2.0091 1.9417 0.5513  0.3607  0.2104  114 GLN A O   
687   C CB  . GLN A 84  ? 2.4403 2.0514 2.0758 0.4654  0.3292  0.2123  114 GLN A CB  
688   C CG  . GLN A 84  ? 2.5880 2.1505 2.1940 0.4311  0.3436  0.2403  114 GLN A CG  
689   C CD  . GLN A 84  ? 2.6265 2.2071 2.2608 0.3984  0.3539  0.2677  114 GLN A CD  
690   O OE1 . GLN A 84  ? 2.6629 2.2944 2.3332 0.4081  0.3551  0.2688  114 GLN A OE1 
691   N NE2 . GLN A 84  ? 2.6819 2.2217 2.3012 0.3586  0.3618  0.2888  114 GLN A NE2 
692   N N   . SER A 85  ? 2.2896 1.9471 1.8777 0.5751  0.3306  0.1629  115 SER A N   
693   C CA  . SER A 85  ? 2.2771 1.9245 1.8256 0.6119  0.3288  0.1434  115 SER A CA  
694   C C   . SER A 85  ? 2.2795 1.9559 1.8000 0.6514  0.3461  0.1486  115 SER A C   
695   O O   . SER A 85  ? 2.2863 1.9507 1.7654 0.6818  0.3480  0.1402  115 SER A O   
696   C CB  . SER A 85  ? 2.2616 1.9276 1.8356 0.6245  0.3061  0.1056  115 SER A CB  
697   O OG  . SER A 85  ? 2.4357 2.0966 1.9733 0.6604  0.3041  0.0854  115 SER A OG  
698   N N   . LEU A 86  ? 2.1839 1.8982 1.7259 0.6509  0.3586  0.1626  116 LEU A N   
699   C CA  . LEU A 86  ? 2.2369 1.9827 1.7555 0.6842  0.3765  0.1685  116 LEU A CA  
700   C C   . LEU A 86  ? 2.3151 2.0407 1.8075 0.6683  0.4004  0.2060  116 LEU A C   
701   O O   . LEU A 86  ? 2.3980 2.1431 1.8645 0.6915  0.4182  0.2162  116 LEU A O   
702   C CB  . LEU A 86  ? 2.1509 1.9600 1.7143 0.6991  0.3746  0.1515  116 LEU A CB  
703   C CG  . LEU A 86  ? 2.0810 1.9151 1.6656 0.7215  0.3546  0.1122  116 LEU A CG  
704   C CD1 . LEU A 86  ? 2.0558 1.9511 1.6824 0.7370  0.3572  0.0977  116 LEU A CD1 
705   C CD2 . LEU A 86  ? 2.0897 1.9120 1.6242 0.7567  0.3527  0.0965  116 LEU A CD2 
706   N N   . LYS A 87  ? 2.5130 2.1994 2.0102 0.6276  0.4016  0.2261  117 LYS A N   
707   C CA  . LYS A 87  ? 2.5398 2.2036 2.0118 0.6087  0.4254  0.2614  117 LYS A CA  
708   C C   . LYS A 87  ? 2.5323 2.1551 1.9378 0.6299  0.4392  0.2741  117 LYS A C   
709   O O   . LYS A 87  ? 2.5459 2.1762 1.9227 0.6427  0.4607  0.2935  117 LYS A O   
710   C CB  . LYS A 87  ? 2.5498 2.1833 2.0455 0.5582  0.4219  0.2768  117 LYS A CB  
711   C CG  . LYS A 87  ? 2.6975 2.3011 2.1683 0.5317  0.4458  0.3119  117 LYS A CG  
712   C CD  . LYS A 87  ? 2.5538 2.1315 2.0515 0.4810  0.4388  0.3219  117 LYS A CD  
713   C CE  . LYS A 87  ? 2.6721 2.2458 2.1696 0.4495  0.4611  0.3534  117 LYS A CE  
714   N NZ  . LYS A 87  ? 2.7843 2.4198 2.3205 0.4561  0.4671  0.3551  117 LYS A NZ  
715   N N   . PRO A 88  ? 2.1537 1.7118 2.3749 0.2029  0.1642  0.0809  118 PRO A N   
716   C CA  . PRO A 88  ? 2.1375 1.6973 2.3686 0.2016  0.1618  0.1039  118 PRO A CA  
717   C C   . PRO A 88  ? 2.2134 1.7920 2.4522 0.1896  0.1462  0.1218  118 PRO A C   
718   O O   . PRO A 88  ? 2.2491 1.8302 2.5010 0.1912  0.1419  0.1436  118 PRO A O   
719   C CB  . PRO A 88  ? 2.1466 1.7014 2.4023 0.2215  0.1721  0.1154  118 PRO A CB  
720   C CG  . PRO A 88  ? 2.1308 1.6924 2.3943 0.2268  0.1734  0.1099  118 PRO A CG  
721   C CD  . PRO A 88  ? 2.1616 1.7185 2.4006 0.2181  0.1708  0.0853  118 PRO A CD  
722   N N   . CYS A 89  ? 2.0622 1.6538 2.2941 0.1783  0.1367  0.1119  119 CYS A N   
723   C CA  . CYS A 89  ? 2.1017 1.7136 2.3412 0.1665  0.1216  0.1254  119 CYS A CA  
724   C C   . CYS A 89  ? 2.0945 1.7137 2.3123 0.1474  0.1124  0.1230  119 CYS A C   
725   O O   . CYS A 89  ? 2.0903 1.7006 2.2855 0.1409  0.1177  0.1067  119 CYS A O   
726   C CB  . CYS A 89  ? 2.1303 1.7527 2.3765 0.1645  0.1156  0.1160  119 CYS A CB  
727   S SG  . CYS A 89  ? 2.3450 1.9676 2.6213 0.1817  0.1225  0.1307  119 CYS A SG  
728   N N   . VAL A 90  ? 1.9738 1.6113 2.1987 0.1376  0.0986  0.1391  120 VAL A N   
729   C CA  . VAL A 90  ? 1.9843 1.6322 2.1885 0.1181  0.0887  0.1404  120 VAL A CA  
730   C C   . VAL A 90  ? 1.9617 1.6221 2.1478 0.1035  0.0846  0.1126  120 VAL A C   
731   O O   . VAL A 90  ? 1.9777 1.6505 2.1743 0.1030  0.0779  0.1038  120 VAL A O   
732   C CB  . VAL A 90  ? 1.9857 1.6511 2.2041 0.1131  0.0741  0.1654  120 VAL A CB  
733   C CG1 . VAL A 90  ? 1.9954 1.6762 2.1904 0.0906  0.0623  0.1647  120 VAL A CG1 
734   C CG2 . VAL A 90  ? 1.9607 1.6138 2.1963 0.1270  0.0762  0.1909  120 VAL A CG2 
735   N N   . LYS A 91  ? 1.9873 1.6444 2.1469 0.0913  0.0883  0.0975  121 LYS A N   
736   C CA  . LYS A 91  ? 1.9930 1.6647 2.1348 0.0763  0.0844  0.0678  121 LYS A CA  
737   C C   . LYS A 91  ? 2.0213 1.7194 2.1533 0.0551  0.0702  0.0731  121 LYS A C   
738   O O   . LYS A 91  ? 2.0300 1.7281 2.1497 0.0453  0.0680  0.0916  121 LYS A O   
739   C CB  . LYS A 91  ? 1.9842 1.6436 2.1032 0.0724  0.0964  0.0458  121 LYS A CB  
740   C CG  . LYS A 91  ? 1.9981 1.6416 2.1057 0.0702  0.1037  0.0639  121 LYS A CG  
741   C CD  . LYS A 91  ? 2.1007 1.7281 2.1922 0.0716  0.1183  0.0412  121 LYS A CD  
742   C CE  . LYS A 91  ? 2.1771 1.7840 2.2605 0.0715  0.1261  0.0599  121 LYS A CE  
743   N NZ  . LYS A 91  ? 2.2371 1.8282 2.3076 0.0740  0.1412  0.0369  121 LYS A NZ  
744   N N   . LEU A 92  ? 1.8375 1.5573 1.9748 0.0479  0.0595  0.0573  122 LEU A N   
745   C CA  . LEU A 92  ? 1.8680 1.6169 1.9982 0.0281  0.0453  0.0599  122 LEU A CA  
746   C C   . LEU A 92  ? 1.8756 1.6419 1.9796 0.0078  0.0448  0.0305  122 LEU A C   
747   O O   . LEU A 92  ? 1.8927 1.6866 1.9964 -0.0052 0.0333  0.0147  122 LEU A O   
748   C CB  . LEU A 92  ? 1.8824 1.6480 2.0368 0.0314  0.0330  0.0599  122 LEU A CB  
749   C CG  . LEU A 92  ? 1.8771 1.6311 2.0588 0.0491  0.0335  0.0878  122 LEU A CG  
750   C CD1 . LEU A 92  ? 1.8938 1.6664 2.0985 0.0489  0.0210  0.0877  122 LEU A CD1 
751   C CD2 . LEU A 92  ? 1.8836 1.6336 2.0643 0.0493  0.0327  0.1198  122 LEU A CD2 
752   N N   . THR A 93  ? 1.9059 1.6585 1.9887 0.0040  0.0570  0.0211  123 THR A N   
753   C CA  . THR A 93  ? 1.9113 1.6835 1.9690 -0.0172 0.0577  -0.0079 123 THR A CA  
754   C C   . THR A 93  ? 1.9421 1.7449 1.9839 -0.0421 0.0464  -0.0010 123 THR A C   
755   O O   . THR A 93  ? 1.9514 1.7834 1.9861 -0.0571 0.0405  -0.0300 123 THR A O   
756   C CB  . THR A 93  ? 1.8931 1.6449 1.9311 -0.0183 0.0738  -0.0156 123 THR A CB  
757   O OG1 . THR A 93  ? 1.9132 1.6609 1.9318 -0.0322 0.0749  0.0102  123 THR A OG1 
758   C CG2 . THR A 93  ? 1.8630 1.5823 1.9173 0.0078  0.0847  -0.0114 123 THR A CG2 
759   N N   . PRO A 94  ? 1.9070 1.7063 1.9423 -0.0478 0.0418  0.0349  124 PRO A N   
760   C CA  . PRO A 94  ? 1.9356 1.7657 1.9523 -0.0728 0.0302  0.0398  124 PRO A CA  
761   C C   . PRO A 94  ? 1.9590 1.8123 1.9961 -0.0718 0.0136  0.0500  124 PRO A C   
762   O O   . PRO A 94  ? 1.9864 1.8511 2.0162 -0.0822 0.0031  0.0750  124 PRO A O   
763   C CB  . PRO A 94  ? 1.9451 1.7554 1.9417 -0.0796 0.0329  0.0732  124 PRO A CB  
764   C CG  . PRO A 94  ? 1.9291 1.7022 1.9470 -0.0527 0.0404  0.0934  124 PRO A CG  
765   C CD  . PRO A 94  ? 1.9059 1.6745 1.9493 -0.0326 0.0460  0.0704  124 PRO A CD  
766   N N   . LEU A 95  ? 1.6994 1.5589 1.7613 -0.0595 0.0105  0.0302  125 LEU A N   
767   C CA  . LEU A 95  ? 1.6897 1.5720 1.7737 -0.0587 -0.0048 0.0337  125 LEU A CA  
768   C C   . LEU A 95  ? 1.6804 1.5961 1.7628 -0.0728 -0.0123 -0.0041 125 LEU A C   
769   O O   . LEU A 95  ? 1.6700 1.6058 1.7728 -0.0722 -0.0252 -0.0083 125 LEU A O   
770   C CB  . LEU A 95  ? 1.6691 1.5316 1.7866 -0.0338 -0.0043 0.0441  125 LEU A CB  
771   C CG  . LEU A 95  ? 1.6711 1.5397 1.8106 -0.0275 -0.0153 0.0755  125 LEU A CG  
772   C CD1 . LEU A 95  ? 1.6969 1.5608 1.8223 -0.0329 -0.0175 0.1086  125 LEU A CD1 
773   C CD2 . LEU A 95  ? 1.6529 1.5009 1.8227 -0.0045 -0.0113 0.0844  125 LEU A CD2 
774   N N   . CYS A 96  ? 1.9277 1.8505 1.9886 -0.0849 -0.0048 -0.0340 126 CYS A N   
775   C CA  . CYS A 96  ? 1.9275 1.8840 1.9887 -0.0976 -0.0121 -0.0744 126 CYS A CA  
776   C C   . CYS A 96  ? 1.9514 1.9474 1.9907 -0.1255 -0.0199 -0.0766 126 CYS A C   
777   O O   . CYS A 96  ? 1.9455 1.9722 1.9743 -0.1420 -0.0214 -0.1125 126 CYS A O   
778   C CB  . CYS A 96  ? 1.8988 1.8464 1.9517 -0.0954 -0.0008 -0.1105 126 CYS A CB  
779   S SG  . CYS A 96  ? 1.8703 1.7758 1.9483 -0.0633 0.0059  -0.1160 126 CYS A SG  
780   N N   . VAL A 97  ? 2.0439 2.0408 2.0762 -0.1309 -0.0254 -0.0390 127 VAL A N   
781   C CA  . VAL A 97  ? 2.0701 2.1036 2.0800 -0.1573 -0.0342 -0.0359 127 VAL A CA  
782   C C   . VAL A 97  ? 2.0811 2.1528 2.1117 -0.1618 -0.0503 -0.0548 127 VAL A C   
783   O O   . VAL A 97  ? 2.0760 2.1402 2.1396 -0.1433 -0.0566 -0.0566 127 VAL A O   
784   C CB  . VAL A 97  ? 2.0968 2.1145 2.0939 -0.1590 -0.0372 0.0116  127 VAL A CB  
785   C CG1 . VAL A 97  ? 2.1204 2.1690 2.0825 -0.1895 -0.0433 0.0173  127 VAL A CG1 
786   C CG2 . VAL A 97  ? 2.0797 2.0513 2.0700 -0.1453 -0.0227 0.0318  127 VAL A CG2 
787   N N   . THR A 98  ? 2.0105 2.1245 2.0211 -0.1878 -0.0568 -0.0705 128 THR A N   
788   C CA  . THR A 98  ? 2.0188 2.1740 2.0475 -0.1947 -0.0729 -0.0897 128 THR A CA  
789   C C   . THR A 98  ? 2.0456 2.1980 2.0960 -0.1839 -0.0857 -0.0556 128 THR A C   
790   O O   . THR A 98  ? 2.0704 2.2151 2.1056 -0.1879 -0.0877 -0.0184 128 THR A O   
791   C CB  . THR A 98  ? 2.0272 2.2294 2.0257 -0.2266 -0.0762 -0.1076 128 THR A CB  
792   O OG1 . THR A 98  ? 2.0502 2.2474 2.0178 -0.2400 -0.0758 -0.0686 128 THR A OG1 
793   C CG2 . THR A 98  ? 2.0031 2.2142 1.9842 -0.2380 -0.0636 -0.1473 128 THR A CG2 
794   N N   . LEU A 99  ? 1.9549 2.1126 2.0416 -0.1702 -0.0951 -0.0687 129 LEU A N   
795   C CA  . LEU A 99  ? 1.9787 2.1349 2.0913 -0.1589 -0.1067 -0.0408 129 LEU A CA  
796   C C   . LEU A 99  ? 1.9873 2.1926 2.1093 -0.1738 -0.1238 -0.0565 129 LEU A C   
797   O O   . LEU A 99  ? 1.9662 2.1915 2.1068 -0.1748 -0.1297 -0.0931 129 LEU A O   
798   C CB  . LEU A 99  ? 1.9650 2.0895 2.1127 -0.1332 -0.1043 -0.0414 129 LEU A CB  
799   C CG  . LEU A 99  ? 1.9414 2.0207 2.0821 -0.1177 -0.0871 -0.0342 129 LEU A CG  
800   C CD1 . LEU A 99  ? 1.9234 1.9747 2.0969 -0.0944 -0.0857 -0.0352 129 LEU A CD1 
801   C CD2 . LEU A 99  ? 1.9558 2.0132 2.0777 -0.1161 -0.0800 0.0056  129 LEU A CD2 
802   N N   . GLN A 100 ? 2.0971 2.3214 2.2073 -0.1846 -0.1328 -0.0298 130 GLN A N   
803   C CA  . GLN A 100 ? 2.0959 2.3671 2.2160 -0.1975 -0.1499 -0.0395 130 GLN A CA  
804   C C   . GLN A 100 ? 2.1050 2.3691 2.2649 -0.1793 -0.1602 -0.0215 130 GLN A C   
805   O O   . GLN A 100 ? 2.1281 2.3880 2.2885 -0.1756 -0.1660 0.0139  130 GLN A O   
806   C CB  . GLN A 100 ? 2.1088 2.4073 2.1913 -0.2213 -0.1547 -0.0235 130 GLN A CB  
807   C CG  . GLN A 100 ? 2.0970 2.4034 2.1412 -0.2412 -0.1427 -0.0445 130 GLN A CG  
808   C CD  . GLN A 100 ? 2.1714 2.5128 2.1758 -0.2702 -0.1480 -0.0364 130 GLN A CD  
809   O OE1 . GLN A 100 ? 2.2540 2.6436 2.2603 -0.2856 -0.1602 -0.0545 130 GLN A OE1 
810   N NE2 . GLN A 100 ? 2.2180 2.5362 2.1854 -0.2791 -0.1389 -0.0108 130 GLN A NE2 
811   N N   . CYS A 101 ? 2.0765 2.3384 2.2703 -0.1679 -0.1632 -0.0464 131 CYS A N   
812   C CA  . CYS A 101 ? 2.0802 2.3304 2.3132 -0.1504 -0.1702 -0.0321 131 CYS A CA  
813   C C   . CYS A 101 ? 2.0636 2.3576 2.3189 -0.1595 -0.1884 -0.0463 131 CYS A C   
814   O O   . CYS A 101 ? 2.0494 2.3830 2.2942 -0.1775 -0.1956 -0.0748 131 CYS A O   
815   C CB  . CYS A 101 ? 2.0722 2.2900 2.3291 -0.1329 -0.1635 -0.0487 131 CYS A CB  
816   S SG  . CYS A 101 ? 2.0743 2.2427 2.3086 -0.1209 -0.1424 -0.0356 131 CYS A SG  
817   N N   . THR A 102 ? 2.1308 2.4191 2.4181 -0.1470 -0.1955 -0.0267 132 THR A N   
818   C CA  . THR A 102 ? 2.1118 2.4371 2.4271 -0.1524 -0.2127 -0.0375 132 THR A CA  
819   C C   . THR A 102 ? 2.1042 2.4060 2.4605 -0.1341 -0.2141 -0.0271 132 THR A C   
820   O O   . THR A 102 ? 2.1150 2.3757 2.4744 -0.1184 -0.2020 -0.0072 132 THR A O   
821   C CB  . THR A 102 ? 2.1165 2.4735 2.4185 -0.1637 -0.2230 -0.0147 132 THR A CB  
822   O OG1 . THR A 102 ? 2.0979 2.4905 2.4305 -0.1673 -0.2394 -0.0259 132 THR A OG1 
823   C CG2 . THR A 102 ? 2.1339 2.4608 2.4336 -0.1502 -0.2179 0.0301  132 THR A CG2 
824   N N   . ASN A 103 ? 2.2430 2.5721 2.6308 -0.1370 -0.2288 -0.0402 133 ASN A N   
825   C CA  . ASN A 103 ? 2.2137 2.5221 2.6402 -0.1223 -0.2301 -0.0300 133 ASN A CA  
826   C C   . ASN A 103 ? 2.2483 2.5424 2.6802 -0.1116 -0.2258 0.0118  133 ASN A C   
827   O O   . ASN A 103 ? 2.2635 2.5750 2.6783 -0.1168 -0.2294 0.0320  133 ASN A O   
828   C CB  . ASN A 103 ? 2.2615 2.6009 2.7243 -0.1276 -0.2472 -0.0495 133 ASN A CB  
829   C CG  . ASN A 103 ? 2.3508 2.6952 2.8251 -0.1323 -0.2536 -0.0920 133 ASN A CG  
830   O OD1 . ASN A 103 ? 2.2599 2.5771 2.7594 -0.1226 -0.2536 -0.0986 133 ASN A OD1 
831   N ND2 . ASN A 103 ? 2.5782 2.9592 3.0375 -0.1474 -0.2610 -0.1213 133 ASN A ND2 
832   N N   . VAL A 104 ? 2.0998 2.3620 2.5563 -0.0966 -0.2188 0.0237  134 VAL A N   
833   C CA  . VAL A 104 ? 2.0970 2.3474 2.5659 -0.0850 -0.2147 0.0594  134 VAL A CA  
834   C C   . VAL A 104 ? 2.0810 2.3692 2.5761 -0.0903 -0.2306 0.0641  134 VAL A C   
835   O O   . VAL A 104 ? 2.0690 2.3833 2.5819 -0.0995 -0.2427 0.0395  134 VAL A O   
836   C CB  . VAL A 104 ? 2.0901 2.3009 2.5790 -0.0697 -0.2023 0.0673  134 VAL A CB  
837   C CG1 . VAL A 104 ? 2.0713 2.2885 2.5964 -0.0713 -0.2109 0.0506  134 VAL A CG1 
838   C CG2 . VAL A 104 ? 2.0840 2.2802 2.5798 -0.0568 -0.1944 0.1027  134 VAL A CG2 
839   N N   . THR A 105 ? 2.2018 2.4939 2.7003 -0.0841 -0.2317 0.0945  135 THR A N   
840   C CA  . THR A 105 ? 2.2132 2.5420 2.7350 -0.0879 -0.2472 0.1012  135 THR A CA  
841   C C   . THR A 105 ? 2.2132 2.5426 2.7797 -0.0832 -0.2494 0.0946  135 THR A C   
842   O O   . THR A 105 ? 2.1693 2.4758 2.7552 -0.0706 -0.2401 0.1127  135 THR A O   
843   C CB  . THR A 105 ? 2.1895 2.5185 2.7046 -0.0802 -0.2485 0.1354  135 THR A CB  
844   O OG1 . THR A 105 ? 2.2282 2.5517 2.6994 -0.0860 -0.2463 0.1426  135 THR A OG1 
845   C CG2 . THR A 105 ? 2.0950 2.4656 2.6316 -0.0849 -0.2665 0.1400  135 THR A CG2 
846   N N   . ASN A 106 ? 2.3022 2.6586 2.8855 -0.0942 -0.2618 0.0680  136 ASN A N   
847   C CA  . ASN A 106 ? 2.2937 2.6532 2.9197 -0.0928 -0.2664 0.0601  136 ASN A CA  
848   C C   . ASN A 106 ? 2.3561 2.7604 2.9966 -0.1066 -0.2851 0.0359  136 ASN A C   
849   O O   . ASN A 106 ? 2.3618 2.7949 2.9786 -0.1165 -0.2933 0.0274  136 ASN A O   
850   C CB  . ASN A 106 ? 2.2260 2.5471 2.8583 -0.0886 -0.2564 0.0465  136 ASN A CB  
851   C CG  . ASN A 106 ? 2.2810 2.6043 2.8970 -0.0979 -0.2614 0.0124  136 ASN A CG  
852   O OD1 . ASN A 106 ? 2.3350 2.6797 2.9236 -0.1061 -0.2654 0.0026  136 ASN A OD1 
853   N ND2 . ASN A 106 ? 2.2577 2.5592 2.8907 -0.0970 -0.2617 -0.0063 136 ASN A ND2 
854   N N   . ASN A 107 ? 2.4706 2.8812 3.1499 -0.1083 -0.2918 0.0241  137 ASN A N   
855   C CA  . ASN A 107 ? 2.5307 2.9845 3.2293 -0.1206 -0.3102 -0.0002 137 ASN A CA  
856   C C   . ASN A 107 ? 2.5995 3.0417 3.3152 -0.1255 -0.3146 -0.0324 137 ASN A C   
857   O O   . ASN A 107 ? 2.6605 3.0940 3.4118 -0.1245 -0.3175 -0.0348 137 ASN A O   
858   C CB  . ASN A 107 ? 2.4663 2.9452 3.2010 -0.1190 -0.3181 0.0150  137 ASN A CB  
859   C CG  . ASN A 107 ? 2.5667 3.0861 3.3301 -0.1306 -0.3364 -0.0115 137 ASN A CG  
860   O OD1 . ASN A 107 ? 2.6350 3.1949 3.3873 -0.1395 -0.3487 -0.0222 137 ASN A OD1 
861   N ND2 . ASN A 107 ? 2.6620 3.1704 3.4619 -0.1315 -0.3385 -0.0228 137 ASN A ND2 
862   N N   . ILE A 108 ? 2.7452 3.1899 3.4365 -0.1318 -0.3166 -0.0581 138 ILE A N   
863   C CA  . ILE A 108 ? 2.7531 3.1938 3.4594 -0.1371 -0.3252 -0.0947 138 ILE A CA  
864   C C   . ILE A 108 ? 2.6948 3.0862 3.4234 -0.1277 -0.3177 -0.0865 138 ILE A C   
865   O O   . ILE A 108 ? 2.6437 3.0068 3.3649 -0.1179 -0.3028 -0.0559 138 ILE A O   
866   C CB  . ILE A 108 ? 2.7233 3.2179 3.4536 -0.1496 -0.3455 -0.1197 138 ILE A CB  
867   C CG1 . ILE A 108 ? 2.6958 3.2329 3.3970 -0.1576 -0.3489 -0.1156 138 ILE A CG1 
868   C CG2 . ILE A 108 ? 2.6839 3.1936 3.4138 -0.1583 -0.3564 -0.1632 138 ILE A CG2 
869   C CD1 . ILE A 108 ? 2.6635 3.2234 3.3714 -0.1560 -0.3516 -0.0859 138 ILE A CD1 
870   N N   . THR A 109 ? 2.7537 3.1295 3.5051 -0.1298 -0.3262 -0.1113 139 THR A N   
871   C CA  . THR A 109 ? 2.7346 3.1325 3.4966 -0.1388 -0.3432 -0.1525 139 THR A CA  
872   C C   . THR A 109 ? 2.7828 3.1714 3.5129 -0.1384 -0.3400 -0.1754 139 THR A C   
873   O O   . THR A 109 ? 2.8005 3.1691 3.4968 -0.1324 -0.3243 -0.1582 139 THR A O   
874   C CB  . THR A 109 ? 2.6472 3.0223 3.4474 -0.1392 -0.3537 -0.1666 139 THR A CB  
875   O OG1 . THR A 109 ? 2.6450 2.9635 3.4359 -0.1297 -0.3418 -0.1539 139 THR A OG1 
876   C CG2 . THR A 109 ? 2.6151 3.0061 3.4501 -0.1424 -0.3581 -0.1491 139 THR A CG2 
877   N N   . ASP A 110 ? 2.9626 3.3671 3.7055 -0.1449 -0.3555 -0.2162 140 ASP A N   
878   C CA  . ASP A 110 ? 2.9986 3.3985 3.7155 -0.1452 -0.3539 -0.2435 140 ASP A CA  
879   C C   . ASP A 110 ? 2.9841 3.3264 3.6993 -0.1341 -0.3483 -0.2452 140 ASP A C   
880   O O   . ASP A 110 ? 2.9760 3.3070 3.6683 -0.1317 -0.3447 -0.2646 140 ASP A O   
881   C CB  . ASP A 110 ? 2.9979 3.4418 3.7299 -0.1561 -0.3731 -0.2901 140 ASP A CB  
882   C CG  . ASP A 110 ? 2.9921 3.4600 3.6891 -0.1620 -0.3689 -0.3129 140 ASP A CG  
883   O OD1 . ASP A 110 ? 3.0269 3.4632 3.6931 -0.1554 -0.3536 -0.3025 140 ASP A OD1 
884   O OD2 . ASP A 110 ? 2.9620 3.4818 3.6625 -0.1741 -0.3806 -0.3426 140 ASP A OD2 
885   N N   . ASP A 111 ? 3.0045 3.3111 3.7422 -0.1281 -0.3474 -0.2251 141 ASP A N   
886   C CA  . ASP A 111 ? 2.9529 3.2029 3.6884 -0.1182 -0.3429 -0.2230 141 ASP A CA  
887   C C   . ASP A 111 ? 2.9338 3.1510 3.6421 -0.1085 -0.3199 -0.1845 141 ASP A C   
888   O O   . ASP A 111 ? 2.8731 3.0428 3.5747 -0.0998 -0.3133 -0.1782 141 ASP A O   
889   C CB  . ASP A 111 ? 2.9291 3.1575 3.7034 -0.1193 -0.3564 -0.2254 141 ASP A CB  
890   C CG  . ASP A 111 ? 2.9368 3.1949 3.7406 -0.1278 -0.3808 -0.2669 141 ASP A CG  
891   O OD1 . ASP A 111 ? 2.9556 3.2352 3.7482 -0.1296 -0.3876 -0.3007 141 ASP A OD1 
892   O OD2 . ASP A 111 ? 2.9421 3.2032 3.7815 -0.1330 -0.3931 -0.2672 141 ASP A OD2 
893   N N   . MET A 112 ? 2.8759 3.1175 3.5688 -0.1097 -0.3086 -0.1592 150 MET A N   
894   C CA  . MET A 112 ? 2.9905 3.2026 3.6597 -0.0999 -0.2876 -0.1246 150 MET A CA  
895   C C   . MET A 112 ? 2.9826 3.1797 3.6154 -0.0954 -0.2782 -0.1359 150 MET A C   
896   O O   . MET A 112 ? 2.9989 3.1635 3.6115 -0.0857 -0.2612 -0.1136 150 MET A O   
897   C CB  . MET A 112 ? 3.0251 3.2668 3.6896 -0.1015 -0.2808 -0.0955 150 MET A CB  
898   C CG  . MET A 112 ? 2.9744 3.2363 3.6742 -0.1055 -0.2884 -0.0819 150 MET A CG  
899   S SD  . MET A 112 ? 3.1438 3.3630 3.8679 -0.0983 -0.2796 -0.0567 150 MET A SD  
900   C CE  . MET A 112 ? 2.7562 3.0147 3.5102 -0.1029 -0.2834 -0.0353 150 MET A CE  
901   N N   . ARG A 113 ? 2.8816 3.1038 3.5081 -0.1027 -0.2892 -0.1723 151 ARG A N   
902   C CA  . ARG A 113 ? 2.8446 3.0611 3.4400 -0.1013 -0.2830 -0.1922 151 ARG A CA  
903   C C   . ARG A 113 ? 2.9103 3.1106 3.4714 -0.0952 -0.2617 -0.1621 151 ARG A C   
904   O O   . ARG A 113 ? 2.8802 3.0514 3.4193 -0.0881 -0.2513 -0.1667 151 ARG A O   
905   C CB  . ARG A 113 ? 2.8229 3.0043 3.4281 -0.0947 -0.2907 -0.2190 151 ARG A CB  
906   C CG  . ARG A 113 ? 2.7862 2.9151 3.4002 -0.0835 -0.2844 -0.1952 151 ARG A CG  
907   C CD  . ARG A 113 ? 2.8277 2.9233 3.4480 -0.0777 -0.2951 -0.2242 151 ARG A CD  
908   N NE  . ARG A 113 ? 2.7631 2.8484 3.3535 -0.0723 -0.2871 -0.2413 151 ARG A NE  
909   C CZ  . ARG A 113 ? 2.7849 2.8319 3.3520 -0.0615 -0.2704 -0.2222 151 ARG A CZ  
910   N NH1 . ARG A 113 ? 2.8649 2.8817 3.4349 -0.0552 -0.2596 -0.1857 151 ARG A NH1 
911   N NH2 . ARG A 113 ? 2.7373 2.7785 3.2789 -0.0575 -0.2640 -0.2411 151 ARG A NH2 
912   N N   . GLY A 114 ? 2.4815 2.7015 3.0396 -0.0978 -0.2565 -0.1321 152 GLY A N   
913   C CA  . GLY A 114 ? 2.4653 2.6762 2.9948 -0.0932 -0.2394 -0.1014 152 GLY A CA  
914   C C   . GLY A 114 ? 2.4997 2.6622 3.0238 -0.0784 -0.2229 -0.0760 152 GLY A C   
915   O O   . GLY A 114 ? 2.5356 2.6911 3.0684 -0.0726 -0.2159 -0.0437 152 GLY A O   
916   N N   . GLU A 115 ? 2.3734 2.5045 2.8832 -0.0721 -0.2167 -0.0914 153 GLU A N   
917   C CA  . GLU A 115 ? 2.3480 2.4336 2.8488 -0.0582 -0.2005 -0.0708 153 GLU A CA  
918   C C   . GLU A 115 ? 2.3332 2.4152 2.8100 -0.0535 -0.1840 -0.0414 153 GLU A C   
919   O O   . GLU A 115 ? 2.2743 2.3324 2.7264 -0.0471 -0.1713 -0.0416 153 GLU A O   
920   C CB  . GLU A 115 ? 2.3599 2.4242 2.8896 -0.0522 -0.2012 -0.0527 153 GLU A CB  
921   C CG  . GLU A 115 ? 2.3770 2.3982 2.8963 -0.0387 -0.1835 -0.0308 153 GLU A CG  
922   C CD  . GLU A 115 ? 2.4885 2.4887 3.0339 -0.0352 -0.1835 -0.0151 153 GLU A CD  
923   O OE1 . GLU A 115 ? 2.4899 2.5032 3.0616 -0.0430 -0.1984 -0.0248 153 GLU A OE1 
924   O OE2 . GLU A 115 ? 2.5170 2.4890 3.0567 -0.0255 -0.1682 0.0071  153 GLU A OE2 
925   N N   . LEU A 116 ? 2.1705 2.2745 2.6552 -0.0560 -0.1848 -0.0164 154 LEU A N   
926   C CA  . LEU A 116 ? 2.1194 2.2202 2.5835 -0.0514 -0.1723 0.0117  154 LEU A CA  
927   C C   . LEU A 116 ? 2.1186 2.2534 2.5592 -0.0644 -0.1782 0.0037  154 LEU A C   
928   O O   . LEU A 116 ? 2.1500 2.3215 2.6020 -0.0755 -0.1927 -0.0053 154 LEU A O   
929   C CB  . LEU A 116 ? 2.0218 2.1269 2.5099 -0.0458 -0.1716 0.0428  154 LEU A CB  
930   C CG  . LEU A 116 ? 1.9926 2.0660 2.5019 -0.0347 -0.1634 0.0538  154 LEU A CG  
931   C CD1 . LEU A 116 ? 1.8491 1.9356 2.3873 -0.0321 -0.1647 0.0787  154 LEU A CD1 
932   C CD2 . LEU A 116 ? 1.9436 1.9798 2.4327 -0.0226 -0.1455 0.0635  154 LEU A CD2 
933   N N   . LYS A 117 ? 2.1471 2.2705 2.5549 -0.0641 -0.1672 0.0068  155 LYS A N   
934   C CA  . LYS A 117 ? 2.1332 2.2861 2.5133 -0.0787 -0.1711 0.0003  155 LYS A CA  
935   C C   . LYS A 117 ? 2.0640 2.2112 2.4236 -0.0765 -0.1635 0.0344  155 LYS A C   
936   O O   . LYS A 117 ? 1.9728 2.0858 2.3252 -0.0639 -0.1495 0.0520  155 LYS A O   
937   C CB  . LYS A 117 ? 2.0817 2.2341 2.4401 -0.0857 -0.1681 -0.0338 155 LYS A CB  
938   C CG  . LYS A 117 ? 2.0449 2.2198 2.4262 -0.0925 -0.1834 -0.0690 155 LYS A CG  
939   C CD  . LYS A 117 ? 1.9791 2.2031 2.3657 -0.1079 -0.1986 -0.0735 155 LYS A CD  
940   C CE  . LYS A 117 ? 1.9747 2.2246 2.3843 -0.1155 -0.2145 -0.1120 155 LYS A CE  
941   N NZ  . LYS A 117 ? 1.9722 2.2732 2.3861 -0.1309 -0.2288 -0.1181 155 LYS A NZ  
942   N N   . ASN A 118 ? 2.2112 2.3917 2.5612 -0.0886 -0.1737 0.0431  156 ASN A N   
943   C CA  . ASN A 118 ? 2.1005 2.2777 2.4291 -0.0886 -0.1709 0.0751  156 ASN A CA  
944   C C   . ASN A 118 ? 2.1145 2.2960 2.4001 -0.1028 -0.1663 0.0681  156 ASN A C   
945   O O   . ASN A 118 ? 2.1704 2.3867 2.4388 -0.1205 -0.1763 0.0606  156 ASN A O   
946   C CB  . ASN A 118 ? 2.0530 2.2618 2.3964 -0.0929 -0.1864 0.0918  156 ASN A CB  
947   C CG  . ASN A 118 ? 1.8975 2.0971 2.2262 -0.0886 -0.1860 0.1280  156 ASN A CG  
948   O OD1 . ASN A 118 ? 1.8344 2.0014 2.1460 -0.0807 -0.1735 0.1421  156 ASN A OD1 
949   N ND2 . ASN A 118 ? 1.8727 2.1005 2.2087 -0.0931 -0.2009 0.1427  156 ASN A ND2 
950   N N   . CYS A 119 ? 2.0582 2.2049 2.3263 -0.0956 -0.1506 0.0699  157 CYS A N   
951   C CA  . CYS A 119 ? 2.0390 2.1832 2.2677 -0.1080 -0.1425 0.0604  157 CYS A CA  
952   C C   . CYS A 119 ? 1.9577 2.0904 2.1578 -0.1113 -0.1394 0.0928  157 CYS A C   
953   O O   . CYS A 119 ? 1.8502 1.9538 2.0592 -0.0953 -0.1343 0.1213  157 CYS A O   
954   C CB  . CYS A 119 ? 1.9908 2.1036 2.2173 -0.0984 -0.1275 0.0413  157 CYS A CB  
955   S SG  . CYS A 119 ? 2.4527 2.5693 2.7118 -0.0922 -0.1326 0.0060  157 CYS A SG  
956   N N   . SER A 120 ? 1.9886 2.1451 2.1549 -0.1330 -0.1433 0.0875  158 SER A N   
957   C CA  . SER A 120 ? 1.9221 2.0672 2.0539 -0.1411 -0.1413 0.1151  158 SER A CA  
958   C C   . SER A 120 ? 1.8860 2.0223 1.9823 -0.1542 -0.1279 0.0978  158 SER A C   
959   O O   . SER A 120 ? 1.9147 2.0764 2.0036 -0.1680 -0.1268 0.0622  158 SER A O   
960   C CB  . SER A 120 ? 1.9826 2.1641 2.0999 -0.1586 -0.1584 0.1275  158 SER A CB  
961   O OG  . SER A 120 ? 2.0012 2.1912 2.1509 -0.1465 -0.1712 0.1452  158 SER A OG  
962   N N   . PHE A 121 ? 1.9993 2.1006 2.0753 -0.1500 -0.1180 0.1212  159 PHE A N   
963   C CA  . PHE A 121 ? 1.9697 2.0586 2.0140 -0.1611 -0.1035 0.1061  159 PHE A CA  
964   C C   . PHE A 121 ? 2.0003 2.0579 2.0175 -0.1627 -0.0989 0.1404  159 PHE A C   
965   O O   . PHE A 121 ? 2.0026 2.0425 2.0303 -0.1502 -0.1061 0.1746  159 PHE A O   
966   C CB  . PHE A 121 ? 1.9513 2.0169 2.0142 -0.1445 -0.0892 0.0818  159 PHE A CB  
967   C CG  . PHE A 121 ? 1.9331 1.9618 2.0250 -0.1167 -0.0845 0.1040  159 PHE A CG  
968   C CD1 . PHE A 121 ? 1.9046 1.9382 2.0343 -0.1017 -0.0916 0.1038  159 PHE A CD1 
969   C CD2 . PHE A 121 ? 1.9476 1.9378 2.0289 -0.1067 -0.0728 0.1243  159 PHE A CD2 
970   C CE1 . PHE A 121 ? 1.8900 1.8930 2.0453 -0.0781 -0.0861 0.1234  159 PHE A CE1 
971   C CE2 . PHE A 121 ? 1.9327 1.8928 2.0411 -0.0818 -0.0679 0.1427  159 PHE A CE2 
972   C CZ  . PHE A 121 ? 1.9036 1.8710 2.0484 -0.0679 -0.0741 0.1422  159 PHE A CZ  
973   N N   . ASN A 122 ? 2.0838 2.1354 2.0666 -0.1788 -0.0876 0.1294  160 ASN A N   
974   C CA  . ASN A 122 ? 2.1174 2.1351 2.0725 -0.1820 -0.0811 0.1571  160 ASN A CA  
975   C C   . ASN A 122 ? 2.1079 2.0812 2.0816 -0.1567 -0.0663 0.1608  160 ASN A C   
976   O O   . ASN A 122 ? 2.0824 2.0527 2.0779 -0.1437 -0.0572 0.1343  160 ASN A O   
977   C CB  . ASN A 122 ? 2.1519 2.1833 2.0628 -0.2118 -0.0738 0.1417  160 ASN A CB  
978   C CG  . ASN A 122 ? 2.2259 2.2882 2.1059 -0.2387 -0.0882 0.1559  160 ASN A CG  
979   O OD1 . ASN A 122 ? 2.2103 2.2540 2.0719 -0.2424 -0.0963 0.1935  160 ASN A OD1 
980   N ND2 . ASN A 122 ? 2.1736 2.2836 2.0474 -0.2578 -0.0923 0.1253  160 ASN A ND2 
981   N N   . MET A 123 ? 2.1437 2.0816 2.1080 -0.1501 -0.0648 0.1937  161 MET A N   
982   C CA  . MET A 123 ? 2.1632 2.0604 2.1455 -0.1260 -0.0512 0.1982  161 MET A CA  
983   C C   . MET A 123 ? 2.2304 2.0919 2.1888 -0.1287 -0.0467 0.2245  161 MET A C   
984   O O   . MET A 123 ? 2.2637 2.1239 2.2015 -0.1411 -0.0591 0.2523  161 MET A O   
985   C CB  . MET A 123 ? 2.1196 2.0083 2.1456 -0.0982 -0.0564 0.2113  161 MET A CB  
986   C CG  . MET A 123 ? 2.1308 1.9833 2.1764 -0.0741 -0.0412 0.2110  161 MET A CG  
987   S SD  . MET A 123 ? 2.4330 2.2837 2.4653 -0.0797 -0.0223 0.1687  161 MET A SD  
988   C CE  . MET A 123 ? 2.0680 1.9577 2.1203 -0.0825 -0.0300 0.1376  161 MET A CE  
989   N N   . THR A 124 ? 2.0812 1.9134 2.0414 -0.1180 -0.0295 0.2143  162 THR A N   
990   C CA  . THR A 124 ? 2.1405 1.9352 2.0823 -0.1183 -0.0235 0.2358  162 THR A CA  
991   C C   . THR A 124 ? 2.1686 1.9336 2.1391 -0.0918 -0.0295 0.2674  162 THR A C   
992   O O   . THR A 124 ? 2.1398 1.8985 2.1460 -0.0669 -0.0243 0.2612  162 THR A O   
993   C CB  . THR A 124 ? 2.1353 1.9126 2.0709 -0.1160 -0.0026 0.2098  162 THR A CB  
994   O OG1 . THR A 124 ? 2.0900 1.8980 2.0031 -0.1392 0.0029  0.1761  162 THR A OG1 
995   C CG2 . THR A 124 ? 2.1905 1.9294 2.1066 -0.1184 0.0034  0.2309  162 THR A CG2 
996   N N   . THR A 125 ? 2.2331 1.9800 2.1876 -0.0976 -0.0411 0.3007  163 THR A N   
997   C CA  . THR A 125 ? 2.2594 1.9779 2.2403 -0.0734 -0.0490 0.3308  163 THR A CA  
998   C C   . THR A 125 ? 2.3052 1.9833 2.2897 -0.0599 -0.0341 0.3320  163 THR A C   
999   O O   . THR A 125 ? 2.2980 1.9724 2.2725 -0.0642 -0.0162 0.3062  163 THR A O   
1000  C CB  . THR A 125 ? 2.2954 2.0095 2.2577 -0.0846 -0.0706 0.3659  163 THR A CB  
1001  O OG1 . THR A 125 ? 2.3516 2.0498 2.2690 -0.1097 -0.0685 0.3731  163 THR A OG1 
1002  C CG2 . THR A 125 ? 2.2445 2.0002 2.2050 -0.0967 -0.0862 0.3651  163 THR A CG2 
1003  N N   . GLU A 126 ? 2.2395 1.8879 2.2399 -0.0427 -0.0422 0.3605  164 GLU A N   
1004  C CA  . GLU A 126 ? 2.2851 1.8948 2.2900 -0.0300 -0.0295 0.3626  164 GLU A CA  
1005  C C   . GLU A 126 ? 2.3209 1.9141 2.2808 -0.0564 -0.0246 0.3636  164 GLU A C   
1006  O O   . GLU A 126 ? 2.3241 1.8999 2.2779 -0.0558 -0.0066 0.3466  164 GLU A O   
1007  C CB  . GLU A 126 ? 2.3161 1.8988 2.3487 -0.0067 -0.0416 0.3922  164 GLU A CB  
1008  C CG  . GLU A 126 ? 2.2632 1.8601 2.3432 0.0205  -0.0455 0.3926  164 GLU A CG  
1009  C CD  . GLU A 126 ? 2.2138 1.8399 2.2983 0.0149  -0.0659 0.4058  164 GLU A CD  
1010  O OE1 . GLU A 126 ? 2.2264 1.8647 2.2756 -0.0107 -0.0762 0.4123  164 GLU A OE1 
1011  O OE2 . GLU A 126 ? 2.1579 1.7956 2.2812 0.0356  -0.0715 0.4097  164 GLU A OE2 
1012  N N   . LEU A 127 ? 2.3012 1.9006 2.2286 -0.0806 -0.0403 0.3832  165 LEU A N   
1013  C CA  . LEU A 127 ? 2.3282 1.9151 2.2087 -0.1105 -0.0372 0.3869  165 LEU A CA  
1014  C C   . LEU A 127 ? 2.2795 1.9018 2.1342 -0.1356 -0.0242 0.3529  165 LEU A C   
1015  O O   . LEU A 127 ? 2.2310 1.8908 2.0976 -0.1350 -0.0248 0.3330  165 LEU A O   
1016  C CB  . LEU A 127 ? 2.3704 1.9497 2.2245 -0.1273 -0.0609 0.4236  165 LEU A CB  
1017  C CG  . LEU A 127 ? 2.4194 1.9569 2.2915 -0.1068 -0.0762 0.4588  165 LEU A CG  
1018  C CD1 . LEU A 127 ? 2.3993 1.9483 2.3178 -0.0770 -0.0892 0.4673  165 LEU A CD1 
1019  C CD2 . LEU A 127 ? 2.4667 1.9846 2.2966 -0.1319 -0.0951 0.4922  165 LEU A CD2 
1020  N N   . ARG A 128 ? 2.5203 2.1301 2.3401 -0.1582 -0.0127 0.3457  166 ARG A N   
1021  C CA  . ARG A 128 ? 2.4843 2.1239 2.2779 -0.1833 0.0018  0.3111  166 ARG A CA  
1022  C C   . ARG A 128 ? 2.5193 2.1848 2.2691 -0.2204 -0.0090 0.3194  166 ARG A C   
1023  O O   . ARG A 128 ? 2.5423 2.2246 2.2594 -0.2488 0.0024  0.2981  166 ARG A O   
1024  C CB  . ARG A 128 ? 2.4775 2.0868 2.2599 -0.1862 0.0209  0.2998  166 ARG A CB  
1025  C CG  . ARG A 128 ? 2.5029 2.1278 2.2781 -0.1949 0.0430  0.2571  166 ARG A CG  
1026  C CD  . ARG A 128 ? 2.5224 2.1835 2.3192 -0.1851 0.0493  0.2204  166 ARG A CD  
1027  N NE  . ARG A 128 ? 2.5455 2.2104 2.3309 -0.1943 0.0696  0.1846  166 ARG A NE  
1028  C CZ  . ARG A 128 ? 2.5390 2.2257 2.2882 -0.2277 0.0757  0.1671  166 ARG A CZ  
1029  N NH1 . ARG A 128 ? 2.5360 2.2426 2.2547 -0.2557 0.0634  0.1833  166 ARG A NH1 
1030  N NH2 . ARG A 128 ? 2.5626 2.2523 2.3055 -0.2335 0.0941  0.1332  166 ARG A NH2 
1031  N N   . ASP A 129 ? 2.3021 1.9736 2.0504 -0.2214 -0.0309 0.3488  167 ASP A N   
1032  C CA  . ASP A 129 ? 2.3116 2.0077 2.0174 -0.2561 -0.0435 0.3605  167 ASP A CA  
1033  C C   . ASP A 129 ? 2.4684 2.2111 2.1842 -0.2576 -0.0569 0.3538  167 ASP A C   
1034  O O   . ASP A 129 ? 2.2991 2.0837 2.0149 -0.2678 -0.0486 0.3186  167 ASP A O   
1035  C CB  . ASP A 129 ? 2.3665 2.0238 2.0480 -0.2642 -0.0602 0.4063  167 ASP A CB  
1036  C CG  . ASP A 129 ? 2.3750 1.9886 2.0397 -0.2701 -0.0472 0.4117  167 ASP A CG  
1037  O OD1 . ASP A 129 ? 2.3898 1.9809 2.0876 -0.2433 -0.0341 0.3994  167 ASP A OD1 
1038  O OD2 . ASP A 129 ? 2.4045 2.0067 2.0231 -0.3019 -0.0502 0.4281  167 ASP A OD2 
1039  N N   . LYS A 130 ? 2.4780 2.2118 2.2037 -0.2466 -0.0788 0.3879  168 LYS A N   
1040  C CA  . LYS A 130 ? 2.5292 2.3018 2.2647 -0.2468 -0.0959 0.3903  168 LYS A CA  
1041  C C   . LYS A 130 ? 2.3928 2.1903 2.1746 -0.2225 -0.0879 0.3592  168 LYS A C   
1042  O O   . LYS A 130 ? 2.3147 2.0884 2.1307 -0.1948 -0.0772 0.3525  168 LYS A O   
1043  C CB  . LYS A 130 ? 2.6491 2.3973 2.3919 -0.2337 -0.1203 0.4342  168 LYS A CB  
1044  C CG  . LYS A 130 ? 2.6890 2.4092 2.3831 -0.2590 -0.1319 0.4684  168 LYS A CG  
1045  C CD  . LYS A 130 ? 2.7307 2.4260 2.4325 -0.2450 -0.1593 0.5113  168 LYS A CD  
1046  C CE  . LYS A 130 ? 2.8347 2.4996 2.4848 -0.2719 -0.1723 0.5459  168 LYS A CE  
1047  N NZ  . LYS A 130 ? 2.8494 2.4882 2.5067 -0.2575 -0.2018 0.5875  168 LYS A NZ  
1048  N N   . LYS A 131 ? 2.5739 2.4198 2.3562 -0.2339 -0.0934 0.3396  169 LYS A N   
1049  C CA  . LYS A 131 ? 2.4100 2.2800 2.2333 -0.2144 -0.0869 0.3087  169 LYS A CA  
1050  C C   . LYS A 131 ? 2.3339 2.2034 2.2011 -0.1858 -0.1002 0.3242  169 LYS A C   
1051  O O   . LYS A 131 ? 2.3794 2.2209 2.2544 -0.1723 -0.1119 0.3583  169 LYS A O   
1052  C CB  . LYS A 131 ? 2.4300 2.3537 2.2370 -0.2397 -0.0889 0.2799  169 LYS A CB  
1053  C CG  . LYS A 131 ? 2.3483 2.2873 2.1137 -0.2716 -0.0756 0.2563  169 LYS A CG  
1054  C CD  . LYS A 131 ? 2.3529 2.3000 2.0707 -0.3031 -0.0887 0.2830  169 LYS A CD  
1055  C CE  . LYS A 131 ? 2.2734 2.2622 1.9930 -0.3108 -0.1085 0.2880  169 LYS A CE  
1056  N NZ  . LYS A 131 ? 2.3770 2.3730 2.0473 -0.3419 -0.1219 0.3152  169 LYS A NZ  
1057  N N   . GLN A 132 ? 2.0350 1.9360 1.9320 -0.1768 -0.0993 0.2984  170 GLN A N   
1058  C CA  . GLN A 132 ? 2.0127 1.9171 1.9531 -0.1513 -0.1102 0.3095  170 GLN A CA  
1059  C C   . GLN A 132 ? 1.9807 1.9300 1.9400 -0.1544 -0.1138 0.2815  170 GLN A C   
1060  O O   . GLN A 132 ? 1.9484 1.9063 1.9183 -0.1522 -0.1003 0.2484  170 GLN A O   
1061  C CB  . GLN A 132 ? 1.9875 1.8566 1.9627 -0.1205 -0.0988 0.3124  170 GLN A CB  
1062  C CG  . GLN A 132 ? 1.9734 1.8438 1.9902 -0.0963 -0.1106 0.3292  170 GLN A CG  
1063  C CD  . GLN A 132 ? 1.9509 1.7893 2.0011 -0.0673 -0.0987 0.3319  170 GLN A CD  
1064  O OE1 . GLN A 132 ? 1.9572 1.7710 1.9993 -0.0643 -0.0820 0.3215  170 GLN A OE1 
1065  N NE2 . GLN A 132 ? 1.9385 1.7788 2.0269 -0.0461 -0.1073 0.3452  170 GLN A NE2 
1066  N N   . LYS A 133 ? 2.0665 2.0435 2.0302 -0.1594 -0.1328 0.2938  171 LYS A N   
1067  C CA  . LYS A 133 ? 2.0649 2.0858 2.0487 -0.1627 -0.1393 0.2696  171 LYS A CA  
1068  C C   . LYS A 133 ? 2.0245 2.0413 2.0595 -0.1340 -0.1423 0.2732  171 LYS A C   
1069  O O   . LYS A 133 ? 2.0318 2.0596 2.0836 -0.1274 -0.1586 0.2930  171 LYS A O   
1070  C CB  . LYS A 133 ? 2.0844 2.1408 2.0432 -0.1858 -0.1578 0.2793  171 LYS A CB  
1071  C CG  . LYS A 133 ? 2.0334 2.1108 1.9438 -0.2195 -0.1535 0.2636  171 LYS A CG  
1072  C CD  . LYS A 133 ? 1.9939 2.1094 1.9103 -0.2303 -0.1451 0.2172  171 LYS A CD  
1073  C CE  . LYS A 133 ? 2.0285 2.1919 1.9616 -0.2358 -0.1613 0.2059  171 LYS A CE  
1074  N NZ  . LYS A 133 ? 1.9733 2.1752 1.9097 -0.2487 -0.1552 0.1594  171 LYS A NZ  
1075  N N   . VAL A 134 ? 1.9491 1.9500 2.0091 -0.1172 -0.1268 0.2539  172 VAL A N   
1076  C CA  . VAL A 134 ? 1.8997 1.8964 2.0065 -0.0922 -0.1277 0.2566  172 VAL A CA  
1077  C C   . VAL A 134 ? 1.8701 1.8938 1.9992 -0.0928 -0.1258 0.2234  172 VAL A C   
1078  O O   . VAL A 134 ? 1.8576 1.8936 1.9708 -0.1063 -0.1189 0.1937  172 VAL A O   
1079  C CB  . VAL A 134 ? 1.9063 1.8606 2.0282 -0.0696 -0.1127 0.2650  172 VAL A CB  
1080  C CG1 . VAL A 134 ? 1.9378 1.8660 2.0538 -0.0618 -0.1193 0.3010  172 VAL A CG1 
1081  C CG2 . VAL A 134 ? 1.8998 1.8383 2.0005 -0.0756 -0.0943 0.2410  172 VAL A CG2 
1082  N N   . TYR A 135 ? 1.9318 1.9649 2.1001 -0.0779 -0.1327 0.2278  173 TYR A N   
1083  C CA  . TYR A 135 ? 1.9186 1.9744 2.1122 -0.0774 -0.1336 0.1998  173 TYR A CA  
1084  C C   . TYR A 135 ? 1.9880 2.0201 2.2165 -0.0546 -0.1229 0.1978  173 TYR A C   
1085  O O   . TYR A 135 ? 2.0094 2.0179 2.2519 -0.0377 -0.1191 0.2215  173 TYR A O   
1086  C CB  . TYR A 135 ? 1.9836 2.0784 2.1930 -0.0845 -0.1526 0.2025  173 TYR A CB  
1087  C CG  . TYR A 135 ? 2.1160 2.2102 2.3602 -0.0675 -0.1614 0.2273  173 TYR A CG  
1088  C CD1 . TYR A 135 ? 2.1840 2.2693 2.4222 -0.0626 -0.1700 0.2600  173 TYR A CD1 
1089  C CD2 . TYR A 135 ? 2.1483 2.2530 2.4320 -0.0576 -0.1624 0.2165  173 TYR A CD2 
1090  C CE1 . TYR A 135 ? 2.2331 2.3217 2.5061 -0.0467 -0.1787 0.2791  173 TYR A CE1 
1091  C CE2 . TYR A 135 ? 2.2121 2.3204 2.5289 -0.0438 -0.1696 0.2362  173 TYR A CE2 
1092  C CZ  . TYR A 135 ? 2.2844 2.3862 2.5969 -0.0379 -0.1776 0.2664  173 TYR A CZ  
1093  O OH  . TYR A 135 ? 2.3507 2.4588 2.6986 -0.0234 -0.1852 0.2833  173 TYR A OH  
1094  N N   . SER A 136 ? 1.9797 2.0186 2.2222 -0.0546 -0.1188 0.1689  174 SER A N   
1095  C CA  . SER A 136 ? 1.9496 1.9684 2.2232 -0.0360 -0.1098 0.1651  174 SER A CA  
1096  C C   . SER A 136 ? 1.9627 2.0058 2.2627 -0.0393 -0.1189 0.1449  174 SER A C   
1097  O O   . SER A 136 ? 1.9523 2.0290 2.2498 -0.0540 -0.1325 0.1348  174 SER A O   
1098  C CB  . SER A 136 ? 1.8917 1.8793 2.1513 -0.0297 -0.0925 0.1508  174 SER A CB  
1099  O OG  . SER A 136 ? 1.8954 1.8642 2.1822 -0.0131 -0.0845 0.1478  174 SER A OG  
1100  N N   . LEU A 137 ? 1.8861 1.9114 2.2113 -0.0258 -0.1117 0.1391  175 LEU A N   
1101  C CA  . LEU A 137 ? 1.9000 1.9402 2.2527 -0.0273 -0.1195 0.1215  175 LEU A CA  
1102  C C   . LEU A 137 ? 1.8672 1.8810 2.2229 -0.0200 -0.1092 0.1010  175 LEU A C   
1103  O O   . LEU A 137 ? 1.8540 1.8409 2.2217 -0.0052 -0.0982 0.1130  175 LEU A O   
1104  C CB  . LEU A 137 ? 1.9047 1.9531 2.2916 -0.0189 -0.1250 0.1425  175 LEU A CB  
1105  C CG  . LEU A 137 ? 1.8622 1.9385 2.2744 -0.0270 -0.1389 0.1272  175 LEU A CG  
1106  C CD1 . LEU A 137 ? 1.8996 2.0138 2.2999 -0.0437 -0.1543 0.1197  175 LEU A CD1 
1107  C CD2 . LEU A 137 ? 1.9296 2.0085 2.3786 -0.0175 -0.1405 0.1449  175 LEU A CD2 
1108  N N   . PHE A 138 ? 1.8587 1.8808 2.2038 -0.0300 -0.1134 0.0695  176 PHE A N   
1109  C CA  . PHE A 138 ? 1.7946 1.7921 2.1402 -0.0235 -0.1067 0.0471  176 PHE A CA  
1110  C C   . PHE A 138 ? 1.7823 1.7885 2.1533 -0.0261 -0.1188 0.0265  176 PHE A C   
1111  O O   . PHE A 138 ? 1.8032 1.8415 2.1863 -0.0371 -0.1333 0.0187  176 PHE A O   
1112  C CB  . PHE A 138 ? 1.8099 1.8053 2.1243 -0.0308 -0.1017 0.0236  176 PHE A CB  
1113  C CG  . PHE A 138 ? 1.8260 1.8093 2.1145 -0.0295 -0.0898 0.0426  176 PHE A CG  
1114  C CD1 . PHE A 138 ? 1.8582 1.8061 2.1446 -0.0138 -0.0746 0.0566  176 PHE A CD1 
1115  C CD2 . PHE A 138 ? 1.8270 1.8338 2.0933 -0.0444 -0.0942 0.0473  176 PHE A CD2 
1116  C CE1 . PHE A 138 ? 1.8726 1.8075 2.1374 -0.0122 -0.0645 0.0737  176 PHE A CE1 
1117  C CE2 . PHE A 138 ? 1.7831 1.7749 2.0251 -0.0439 -0.0844 0.0663  176 PHE A CE2 
1118  C CZ  . PHE A 138 ? 1.8164 1.7717 2.0589 -0.0273 -0.0697 0.0792  176 PHE A CZ  
1119  N N   . TYR A 139 ? 1.6991 1.6753 2.0780 -0.0159 -0.1133 0.0180  177 TYR A N   
1120  C CA  . TYR A 139 ? 1.7319 1.7077 2.1328 -0.0175 -0.1250 -0.0021 177 TYR A CA  
1121  C C   . TYR A 139 ? 1.7647 1.7544 2.1542 -0.0272 -0.1347 -0.0406 177 TYR A C   
1122  O O   . TYR A 139 ? 1.7489 1.7398 2.1120 -0.0301 -0.1281 -0.0524 177 TYR A O   
1123  C CB  . TYR A 139 ? 1.7170 1.6532 2.1255 -0.0037 -0.1159 0.0046  177 TYR A CB  
1124  C CG  . TYR A 139 ? 1.7368 1.6650 2.1596 0.0047  -0.1062 0.0398  177 TYR A CG  
1125  C CD1 . TYR A 139 ? 1.7815 1.6774 2.1993 0.0180  -0.0905 0.0540  177 TYR A CD1 
1126  C CD2 . TYR A 139 ? 1.7392 1.6945 2.1819 -0.0005 -0.1133 0.0568  177 TYR A CD2 
1127  C CE1 . TYR A 139 ? 1.7683 1.6609 2.2013 0.0254  -0.0816 0.0831  177 TYR A CE1 
1128  C CE2 . TYR A 139 ? 1.7365 1.6876 2.1951 0.0075  -0.1050 0.0860  177 TYR A CE2 
1129  C CZ  . TYR A 139 ? 1.7391 1.6596 2.1933 0.0202  -0.0890 0.0985  177 TYR A CZ  
1130  O OH  . TYR A 139 ? 1.7022 1.6223 2.1741 0.0279  -0.0806 0.1248  177 TYR A OH  
1131  N N   . ARG A 140 ? 2.1147 2.1157 2.5260 -0.0325 -0.1507 -0.0617 178 ARG A N   
1132  C CA  . ARG A 140 ? 2.1149 2.1334 2.5204 -0.0413 -0.1618 -0.1018 178 ARG A CA  
1133  C C   . ARG A 140 ? 2.0793 2.0672 2.4695 -0.0328 -0.1556 -0.1234 178 ARG A C   
1134  O O   . ARG A 140 ? 2.0342 2.0370 2.4085 -0.0393 -0.1575 -0.1528 178 ARG A O   
1135  C CB  . ARG A 140 ? 2.0904 2.1264 2.5267 -0.0476 -0.1816 -0.1193 178 ARG A CB  
1136  C CG  . ARG A 140 ? 1.9864 2.0448 2.4242 -0.0564 -0.1963 -0.1638 178 ARG A CG  
1137  C CD  . ARG A 140 ? 2.0539 2.1576 2.4738 -0.0712 -0.1960 -0.1681 178 ARG A CD  
1138  N NE  . ARG A 140 ? 2.1425 2.2868 2.5700 -0.0845 -0.2121 -0.2064 178 ARG A NE  
1139  C CZ  . ARG A 140 ? 2.1983 2.3735 2.6504 -0.0928 -0.2276 -0.2116 178 ARG A CZ  
1140  N NH1 . ARG A 140 ? 2.2357 2.4498 2.6945 -0.1048 -0.2417 -0.2490 178 ARG A NH1 
1141  N NH2 . ARG A 140 ? 2.2837 2.4537 2.7547 -0.0894 -0.2287 -0.1805 178 ARG A NH2 
1142  N N   . LEU A 141 ? 1.8831 1.8303 2.2776 -0.0189 -0.1484 -0.1104 179 LEU A N   
1143  C CA  . LEU A 141 ? 1.8394 1.7545 2.2197 -0.0089 -0.1429 -0.1284 179 LEU A CA  
1144  C C   . LEU A 141 ? 1.8509 1.7597 2.2010 -0.0057 -0.1248 -0.1230 179 LEU A C   
1145  O O   . LEU A 141 ? 1.8580 1.7484 2.1941 0.0004  -0.1208 -0.1441 179 LEU A O   
1146  C CB  . LEU A 141 ? 1.8763 1.7506 2.2684 0.0038  -0.1408 -0.1137 179 LEU A CB  
1147  C CG  . LEU A 141 ? 1.8781 1.7538 2.2997 -0.0003 -0.1591 -0.1190 179 LEU A CG  
1148  C CD1 . LEU A 141 ? 1.9328 1.7903 2.3680 0.0046  -0.1519 -0.0833 179 LEU A CD1 
1149  C CD2 . LEU A 141 ? 1.9091 1.7619 2.3346 0.0041  -0.1731 -0.1513 179 LEU A CD2 
1150  N N   . ASP A 142 ? 1.9694 1.8922 2.3102 -0.0095 -0.1149 -0.0958 180 ASP A N   
1151  C CA  . ASP A 142 ? 1.9637 1.8787 2.2769 -0.0074 -0.0982 -0.0872 180 ASP A CA  
1152  C C   . ASP A 142 ? 1.9269 1.8739 2.2196 -0.0229 -0.1001 -0.1077 180 ASP A C   
1153  O O   . ASP A 142 ? 1.9216 1.8607 2.1896 -0.0229 -0.0876 -0.1111 180 ASP A O   
1154  C CB  . ASP A 142 ? 1.9905 1.9002 2.3044 -0.0026 -0.0873 -0.0456 180 ASP A CB  
1155  C CG  . ASP A 142 ? 2.0358 1.9143 2.3659 0.0126  -0.0807 -0.0247 180 ASP A CG  
1156  O OD1 . ASP A 142 ? 2.0289 1.8789 2.3552 0.0223  -0.0762 -0.0369 180 ASP A OD1 
1157  O OD2 . ASP A 142 ? 2.1155 1.9994 2.4620 0.0143  -0.0803 0.0030  180 ASP A OD2 
1158  N N   . VAL A 143 ? 1.8185 1.8023 2.1203 -0.0369 -0.1149 -0.1216 181 VAL A N   
1159  C CA  . VAL A 143 ? 1.7456 1.7653 2.0273 -0.0544 -0.1168 -0.1398 181 VAL A CA  
1160  C C   . VAL A 143 ? 1.6927 1.7330 1.9828 -0.0614 -0.1305 -0.1863 181 VAL A C   
1161  O O   . VAL A 143 ? 1.6845 1.7126 1.9984 -0.0533 -0.1416 -0.2009 181 VAL A O   
1162  C CB  . VAL A 143 ? 1.7328 1.7848 2.0153 -0.0669 -0.1228 -0.1173 181 VAL A CB  
1163  C CG1 . VAL A 143 ? 1.8102 1.8425 2.0832 -0.0598 -0.1103 -0.0742 181 VAL A CG1 
1164  C CG2 . VAL A 143 ? 1.7651 1.8320 2.0805 -0.0671 -0.1393 -0.1187 181 VAL A CG2 
1165  N N   . VAL A 144 ? 1.7876 1.8598 2.0577 -0.0771 -0.1301 -0.2100 182 VAL A N   
1166  C CA  . VAL A 144 ? 1.8048 1.9049 2.0826 -0.0856 -0.1430 -0.2579 182 VAL A CA  
1167  C C   . VAL A 144 ? 1.8573 2.0046 2.1130 -0.1084 -0.1422 -0.2713 182 VAL A C   
1168  O O   . VAL A 144 ? 1.8794 2.0258 2.1048 -0.1154 -0.1276 -0.2618 182 VAL A O   
1169  C CB  . VAL A 144 ? 1.7913 1.8649 2.0667 -0.0741 -0.1395 -0.2878 182 VAL A CB  
1170  C CG1 . VAL A 144 ? 1.7754 1.8286 2.0203 -0.0716 -0.1186 -0.2746 182 VAL A CG1 
1171  C CG2 . VAL A 144 ? 1.8190 1.9272 2.1001 -0.0843 -0.1521 -0.3406 182 VAL A CG2 
1172  N N   . GLN A 145 ? 1.6892 1.8782 1.9597 -0.1209 -0.1583 -0.2930 183 GLN A N   
1173  C CA  . GLN A 145 ? 1.7696 2.0089 2.0202 -0.1445 -0.1593 -0.3061 183 GLN A CA  
1174  C C   . GLN A 145 ? 1.8059 2.0619 2.0385 -0.1538 -0.1535 -0.3483 183 GLN A C   
1175  O O   . GLN A 145 ? 1.7867 2.0226 2.0302 -0.1415 -0.1545 -0.3765 183 GLN A O   
1176  C CB  . GLN A 145 ? 1.8639 2.1440 2.1390 -0.1538 -0.1788 -0.3202 183 GLN A CB  
1177  C CG  . GLN A 145 ? 1.8753 2.1571 2.1841 -0.1457 -0.1949 -0.3615 183 GLN A CG  
1178  C CD  . GLN A 145 ? 1.8918 2.2137 2.2272 -0.1546 -0.2143 -0.3751 183 GLN A CD  
1179  O OE1 . GLN A 145 ? 1.8789 2.2321 2.2056 -0.1682 -0.2156 -0.3564 183 GLN A OE1 
1180  N NE2 . GLN A 145 ? 1.9817 2.3013 2.3503 -0.1466 -0.2307 -0.4076 183 GLN A NE2 
1181  N N   . ILE A 146 ? 1.7787 2.0727 1.9828 -0.1764 -0.1478 -0.3527 184 ILE A N   
1182  C CA  . ILE A 146 ? 1.7968 2.1141 1.9817 -0.1895 -0.1408 -0.3931 184 ILE A CA  
1183  C C   . ILE A 146 ? 1.9119 2.2901 2.0794 -0.2183 -0.1446 -0.4078 184 ILE A C   
1184  O O   . ILE A 146 ? 1.8907 2.2785 2.0371 -0.2306 -0.1413 -0.3721 184 ILE A O   
1185  C CB  . ILE A 146 ? 1.7961 2.0783 1.9513 -0.1858 -0.1197 -0.3755 184 ILE A CB  
1186  C CG1 . ILE A 146 ? 1.8246 2.1377 1.9571 -0.2039 -0.1112 -0.4160 184 ILE A CG1 
1187  C CG2 . ILE A 146 ? 1.7849 2.0510 1.9165 -0.1902 -0.1100 -0.3206 184 ILE A CG2 
1188  C CD1 . ILE A 146 ? 1.8388 2.1612 1.9955 -0.1957 -0.1200 -0.4715 184 ILE A CD1 
1189  N N   . ASN A 147 ? 2.0328 2.4528 2.2094 -0.2289 -0.1523 -0.4610 185 ASN A N   
1190  C CA  . ASN A 147 ? 2.1217 2.6055 2.2823 -0.2577 -0.1557 -0.4820 185 ASN A CA  
1191  C C   . ASN A 147 ? 2.1837 2.6921 2.3159 -0.2758 -0.1420 -0.5153 185 ASN A C   
1192  O O   . ASN A 147 ? 2.1899 2.6768 2.2887 -0.2815 -0.1242 -0.4909 185 ASN A O   
1193  C CB  . ASN A 147 ? 2.1964 2.7203 2.3937 -0.2586 -0.1773 -0.5204 185 ASN A CB  
1194  C CG  . ASN A 147 ? 2.2817 2.8756 2.4641 -0.2885 -0.1815 -0.5420 185 ASN A CG  
1195  O OD1 . ASN A 147 ? 2.3135 2.9220 2.4590 -0.3080 -0.1716 -0.5136 185 ASN A OD1 
1196  N ND2 . ASN A 147 ? 2.3382 2.9756 2.5491 -0.2926 -0.1971 -0.5931 185 ASN A ND2 
1197  N N   . SER A 157 ? 2.9133 3.6453 2.9399 -0.3917 -0.2179 -0.2613 187 SER A N   
1198  C CA  . SER A 157 ? 2.9779 3.6437 3.0046 -0.3710 -0.2037 -0.2389 187 SER A CA  
1199  C C   . SER A 157 ? 3.0242 3.6512 3.1007 -0.3381 -0.2097 -0.2310 187 SER A C   
1200  O O   . SER A 157 ? 3.0523 3.7021 3.1675 -0.3313 -0.2215 -0.2614 187 SER A O   
1201  C CB  . SER A 157 ? 2.9916 3.6573 3.0062 -0.3781 -0.1885 -0.2767 187 SER A CB  
1202  O OG  . SER A 157 ? 2.9995 3.6072 2.9980 -0.3663 -0.1728 -0.2496 187 SER A OG  
1203  N N   . ASN A 158 ? 3.0065 3.5755 3.0821 -0.3188 -0.2017 -0.1906 188 ASN A N   
1204  C CA  . ASN A 158 ? 2.9155 3.4462 3.0340 -0.2894 -0.2055 -0.1780 188 ASN A CA  
1205  C C   . ASN A 158 ? 2.8398 3.3485 2.9820 -0.2750 -0.1986 -0.2130 188 ASN A C   
1206  O O   . ASN A 158 ? 2.9262 3.4497 3.0534 -0.2864 -0.1911 -0.2477 188 ASN A O   
1207  C CB  . ASN A 158 ? 2.7873 3.2677 2.8962 -0.2746 -0.1992 -0.1242 188 ASN A CB  
1208  C CG  . ASN A 158 ? 2.7909 3.2859 2.8632 -0.2916 -0.2037 -0.0893 188 ASN A CG  
1209  O OD1 . ASN A 158 ? 2.7894 3.3305 2.8580 -0.3072 -0.2172 -0.0945 188 ASN A OD1 
1210  N ND2 . ASN A 158 ? 2.7033 3.1584 2.7481 -0.2887 -0.1934 -0.0539 188 ASN A ND2 
1211  N N   . LYS A 159 ? 2.4900 2.9635 2.6695 -0.2501 -0.2015 -0.2045 189 LYS A N   
1212  C CA  . LYS A 159 ? 2.4305 2.8742 2.6310 -0.2339 -0.1959 -0.2307 189 LYS A CA  
1213  C C   . LYS A 159 ? 2.3419 2.7309 2.5247 -0.2205 -0.1782 -0.2032 189 LYS A C   
1214  O O   . LYS A 159 ? 2.2611 2.6200 2.4429 -0.2096 -0.1750 -0.1599 189 LYS A O   
1215  C CB  . LYS A 159 ? 2.4538 2.8889 2.7024 -0.2164 -0.2090 -0.2380 189 LYS A CB  
1216  C CG  . LYS A 159 ? 2.3587 2.7644 2.6244 -0.2007 -0.2110 -0.1927 189 LYS A CG  
1217  C CD  . LYS A 159 ? 2.3276 2.7162 2.6390 -0.1835 -0.2204 -0.2034 189 LYS A CD  
1218  C CE  . LYS A 159 ? 2.3048 2.7381 2.6444 -0.1920 -0.2398 -0.2238 189 LYS A CE  
1219  N NZ  . LYS A 159 ? 2.3295 2.7443 2.7127 -0.1774 -0.2495 -0.2386 189 LYS A NZ  
1220  N N   . GLU A 160 ? 2.1686 2.5472 2.3388 -0.2213 -0.1672 -0.2303 190 GLU A N   
1221  C CA  . GLU A 160 ? 2.1092 2.4457 2.2546 -0.2148 -0.1490 -0.2107 190 GLU A CA  
1222  C C   . GLU A 160 ? 2.0248 2.3169 2.1940 -0.1902 -0.1437 -0.2196 190 GLU A C   
1223  O O   . GLU A 160 ? 2.0043 2.3052 2.1932 -0.1866 -0.1498 -0.2600 190 GLU A O   
1224  C CB  . GLU A 160 ? 2.1068 2.4671 2.2169 -0.2363 -0.1391 -0.2366 190 GLU A CB  
1225  C CG  . GLU A 160 ? 2.2118 2.6091 2.2857 -0.2639 -0.1396 -0.2236 190 GLU A CG  
1226  C CD  . GLU A 160 ? 2.2874 2.7019 2.3260 -0.2849 -0.1267 -0.2486 190 GLU A CD  
1227  O OE1 . GLU A 160 ? 2.3194 2.7191 2.3653 -0.2764 -0.1183 -0.2783 190 GLU A OE1 
1228  O OE2 . GLU A 160 ? 2.3019 2.7454 2.3054 -0.3104 -0.1252 -0.2392 190 GLU A OE2 
1229  N N   . TYR A 161 ? 1.9393 2.1842 2.1069 -0.1731 -0.1334 -0.1830 191 TYR A N   
1230  C CA  . TYR A 161 ? 1.8326 2.0350 2.0204 -0.1502 -0.1281 -0.1886 191 TYR A CA  
1231  C C   . TYR A 161 ? 1.7967 1.9632 1.9594 -0.1442 -0.1091 -0.1774 191 TYR A C   
1232  O O   . TYR A 161 ? 1.7814 1.9561 1.9117 -0.1589 -0.1003 -0.1685 191 TYR A O   
1233  C CB  . TYR A 161 ? 1.7997 1.9787 2.0175 -0.1324 -0.1342 -0.1585 191 TYR A CB  
1234  C CG  . TYR A 161 ? 1.8607 2.0690 2.1089 -0.1355 -0.1529 -0.1732 191 TYR A CG  
1235  C CD1 . TYR A 161 ? 1.9810 2.2280 2.2277 -0.1501 -0.1632 -0.1629 191 TYR A CD1 
1236  C CD2 . TYR A 161 ? 1.8285 2.0248 2.1071 -0.1237 -0.1612 -0.1970 191 TYR A CD2 
1237  C CE1 . TYR A 161 ? 2.0596 2.3346 2.3360 -0.1527 -0.1803 -0.1777 191 TYR A CE1 
1238  C CE2 . TYR A 161 ? 1.9013 2.1227 2.2095 -0.1267 -0.1789 -0.2109 191 TYR A CE2 
1239  C CZ  . TYR A 161 ? 2.0304 2.2921 2.3383 -0.1411 -0.1880 -0.2020 191 TYR A CZ  
1240  O OH  . TYR A 161 ? 2.1146 2.4023 2.4538 -0.1440 -0.2056 -0.2172 191 TYR A OH  
1241  N N   . ARG A 162 ? 1.8300 1.9559 2.0079 -0.1227 -0.1032 -0.1774 192 ARG A N   
1242  C CA  . ARG A 162 ? 1.7540 1.8418 1.9142 -0.1128 -0.0855 -0.1662 192 ARG A CA  
1243  C C   . ARG A 162 ? 1.6854 1.7314 1.8701 -0.0875 -0.0835 -0.1552 192 ARG A C   
1244  O O   . ARG A 162 ? 1.6739 1.7211 1.8865 -0.0802 -0.0958 -0.1639 192 ARG A O   
1245  C CB  . ARG A 162 ? 1.7967 1.8922 1.9382 -0.1209 -0.0779 -0.2050 192 ARG A CB  
1246  C CG  . ARG A 162 ? 1.7586 1.8436 1.9226 -0.1073 -0.0838 -0.2414 192 ARG A CG  
1247  C CD  . ARG A 162 ? 1.7716 1.8535 1.9186 -0.1093 -0.0735 -0.2750 192 ARG A CD  
1248  N NE  . ARG A 162 ? 1.7168 1.7783 1.8857 -0.0915 -0.0797 -0.3035 192 ARG A NE  
1249  C CZ  . ARG A 162 ? 1.8065 1.8920 1.9925 -0.0944 -0.0945 -0.3459 192 ARG A CZ  
1250  N NH1 . ARG A 162 ? 1.9264 2.0609 2.1109 -0.1149 -0.1034 -0.3663 192 ARG A NH1 
1251  N NH2 . ARG A 162 ? 1.7922 1.8528 1.9969 -0.0767 -0.1015 -0.3682 192 ARG A NH2 
1252  N N   . LEU A 163 ? 1.6420 1.6513 1.8157 -0.0752 -0.0681 -0.1359 193 LEU A N   
1253  C CA  . LEU A 163 ? 1.6939 1.6641 1.8867 -0.0524 -0.0642 -0.1275 193 LEU A CA  
1254  C C   . LEU A 163 ? 1.7129 1.6755 1.9127 -0.0459 -0.0676 -0.1680 193 LEU A C   
1255  O O   . LEU A 163 ? 1.7175 1.6912 1.9003 -0.0540 -0.0637 -0.1981 193 LEU A O   
1256  C CB  . LEU A 163 ? 1.6775 1.6134 1.8569 -0.0410 -0.0467 -0.0992 193 LEU A CB  
1257  C CG  . LEU A 163 ? 1.6374 1.5715 1.8165 -0.0410 -0.0448 -0.0561 193 LEU A CG  
1258  C CD1 . LEU A 163 ? 1.6727 1.5712 1.8426 -0.0275 -0.0283 -0.0327 193 LEU A CD1 
1259  C CD2 . LEU A 163 ? 1.5780 1.5158 1.7876 -0.0337 -0.0562 -0.0400 193 LEU A CD2 
1260  N N   . ILE A 164 ? 1.8155 1.7591 2.0405 -0.0317 -0.0756 -0.1691 194 ILE A N   
1261  C CA  . ILE A 164 ? 1.7932 1.7284 2.0277 -0.0251 -0.0836 -0.2071 194 ILE A CA  
1262  C C   . ILE A 164 ? 1.7623 1.6682 1.9810 -0.0137 -0.0703 -0.2189 194 ILE A C   
1263  O O   . ILE A 164 ? 1.7726 1.6752 1.9944 -0.0097 -0.0768 -0.2554 194 ILE A O   
1264  C CB  . ILE A 164 ? 1.7577 1.6745 2.0213 -0.0134 -0.0960 -0.2002 194 ILE A CB  
1265  C CG1 . ILE A 164 ? 1.7371 1.6566 2.0147 -0.0118 -0.1125 -0.2429 194 ILE A CG1 
1266  C CG2 . ILE A 164 ? 1.7220 1.5954 1.9864 0.0049  -0.0838 -0.1724 194 ILE A CG2 
1267  C CD1 . ILE A 164 ? 1.6720 1.5715 1.9772 -0.0026 -0.1265 -0.2367 194 ILE A CD1 
1268  N N   . ASN A 165 ? 1.7657 1.6513 1.9686 -0.0082 -0.0527 -0.1909 195 ASN A N   
1269  C CA  . ASN A 165 ? 1.8516 1.7086 2.0408 0.0037  -0.0394 -0.2006 195 ASN A CA  
1270  C C   . ASN A 165 ? 1.8466 1.7183 2.0089 -0.0089 -0.0275 -0.2130 195 ASN A C   
1271  O O   . ASN A 165 ? 1.9330 1.7863 2.0836 -0.0013 -0.0169 -0.2277 195 ASN A O   
1272  C CB  . ASN A 165 ? 1.8250 1.6460 2.0170 0.0206  -0.0271 -0.1637 195 ASN A CB  
1273  C CG  . ASN A 165 ? 1.7569 1.5816 1.9370 0.0150  -0.0154 -0.1298 195 ASN A CG  
1274  O OD1 . ASN A 165 ? 1.7673 1.5805 1.9287 0.0162  -0.0010 -0.1267 195 ASN A OD1 
1275  N ND2 . ASN A 165 ? 1.7503 1.5906 1.9418 0.0089  -0.0225 -0.1046 195 ASN A ND2 
1276  N N   . CYS A 166 ? 1.7374 1.6418 1.8890 -0.0287 -0.0291 -0.2070 196 CYS A N   
1277  C CA  . CYS A 166 ? 1.8088 1.7273 1.9324 -0.0440 -0.0174 -0.2149 196 CYS A CA  
1278  C C   . CYS A 166 ? 1.7969 1.7302 1.9139 -0.0494 -0.0182 -0.2643 196 CYS A C   
1279  O O   . CYS A 166 ? 1.8002 1.7350 1.8951 -0.0571 -0.0051 -0.2751 196 CYS A O   
1280  C CB  . CYS A 166 ? 1.9098 1.8622 2.0222 -0.0660 -0.0218 -0.1993 196 CYS A CB  
1281  S SG  . CYS A 166 ? 2.0875 2.0212 2.1971 -0.0620 -0.0163 -0.1405 196 CYS A SG  
1282  N N   . ASN A 167 ? 1.8614 1.8058 1.9983 -0.0457 -0.0338 -0.2957 197 ASN A N   
1283  C CA  . ASN A 167 ? 1.9166 1.8766 2.0519 -0.0489 -0.0371 -0.3462 197 ASN A CA  
1284  C C   . ASN A 167 ? 1.9001 1.8232 2.0467 -0.0252 -0.0382 -0.3615 197 ASN A C   
1285  O O   . ASN A 167 ? 1.9423 1.8745 2.0937 -0.0234 -0.0453 -0.4056 197 ASN A O   
1286  C CB  . ASN A 167 ? 1.9959 1.9975 2.1463 -0.0619 -0.0561 -0.3767 197 ASN A CB  
1287  C CG  . ASN A 167 ? 1.9771 1.9636 2.1584 -0.0463 -0.0744 -0.3791 197 ASN A CG  
1288  O OD1 . ASN A 167 ? 1.8775 1.8492 2.0698 -0.0405 -0.0774 -0.3425 197 ASN A OD1 
1289  N ND2 . ASN A 167 ? 2.0441 2.0351 2.2404 -0.0404 -0.0877 -0.4230 197 ASN A ND2 
1290  N N   . THR A 168 ? 1.8780 1.7608 2.0290 -0.0071 -0.0320 -0.3269 198 THR A N   
1291  C CA  . THR A 168 ? 1.8913 1.7368 2.0502 0.0152  -0.0328 -0.3364 198 THR A CA  
1292  C C   . THR A 168 ? 1.8732 1.6881 2.0157 0.0262  -0.0124 -0.3181 198 THR A C   
1293  O O   . THR A 168 ? 1.8995 1.7020 2.0355 0.0349  -0.0079 -0.3449 198 THR A O   
1294  C CB  . THR A 168 ? 1.9213 1.7450 2.1030 0.0281  -0.0456 -0.3154 198 THR A CB  
1295  O OG1 . THR A 168 ? 1.9524 1.7616 2.1330 0.0310  -0.0350 -0.2673 198 THR A OG1 
1296  C CG2 . THR A 168 ? 2.0232 1.8770 2.2234 0.0169  -0.0659 -0.3312 198 THR A CG2 
1297  N N   . SER A 169 ? 1.9730 1.7763 2.1100 0.0267  -0.0007 -0.2748 199 SER A N   
1298  C CA  . SER A 169 ? 1.9482 1.7220 2.0730 0.0383  0.0180  -0.2562 199 SER A CA  
1299  C C   . SER A 169 ? 1.9260 1.7007 2.0439 0.0314  0.0282  -0.2139 199 SER A C   
1300  O O   . SER A 169 ? 1.9539 1.7519 2.0750 0.0178  0.0206  -0.1996 199 SER A O   
1301  C CB  . SER A 169 ? 1.9801 1.7173 2.1171 0.0616  0.0168  -0.2490 199 SER A CB  
1302  O OG  . SER A 169 ? 1.9677 1.6992 2.1221 0.0655  0.0087  -0.2196 199 SER A OG  
1303  N N   . ALA A 170 ? 1.9650 1.7135 2.0750 0.0422  0.0444  -0.1941 200 ALA A N   
1304  C CA  . ALA A 170 ? 1.9024 1.6469 2.0086 0.0390  0.0528  -0.1538 200 ALA A CA  
1305  C C   . ALA A 170 ? 1.8846 1.6194 2.0127 0.0500  0.0462  -0.1228 200 ALA A C   
1306  O O   . ALA A 170 ? 1.9263 1.6532 2.0697 0.0601  0.0375  -0.1313 200 ALA A O   
1307  C CB  . ALA A 170 ? 1.8307 1.5506 1.9244 0.0477  0.0713  -0.1455 200 ALA A CB  
1308  N N   . ILE A 171 ? 1.8794 1.6137 2.0094 0.0482  0.0501  -0.0868 201 ILE A N   
1309  C CA  . ILE A 171 ? 1.9010 1.6312 2.0530 0.0568  0.0443  -0.0577 201 ILE A CA  
1310  C C   . ILE A 171 ? 1.9058 1.6189 2.0606 0.0664  0.0559  -0.0230 201 ILE A C   
1311  O O   . ILE A 171 ? 1.9418 1.6569 2.0821 0.0583  0.0616  -0.0120 201 ILE A O   
1312  C CB  . ILE A 171 ? 1.8792 1.6403 2.0385 0.0411  0.0285  -0.0534 201 ILE A CB  
1313  C CG1 . ILE A 171 ? 1.8715 1.6304 2.0550 0.0492  0.0231  -0.0234 201 ILE A CG1 
1314  C CG2 . ILE A 171 ? 1.8807 1.6618 2.0201 0.0224  0.0293  -0.0476 201 ILE A CG2 
1315  C CD1 . ILE A 171 ? 1.8402 1.6294 2.0330 0.0352  0.0073  -0.0197 201 ILE A CD1 
1316  N N   . THR A 172 ? 1.9574 1.6533 2.1309 0.0833  0.0591  -0.0065 202 THR A N   
1317  C CA  . THR A 172 ? 1.9293 1.6116 2.1113 0.0944  0.0689  0.0246  202 THR A CA  
1318  C C   . THR A 172 ? 1.9056 1.5941 2.1131 0.0999  0.0625  0.0493  202 THR A C   
1319  O O   . THR A 172 ? 1.8949 1.5840 2.1154 0.1032  0.0563  0.0429  202 THR A O   
1320  C CB  . THR A 172 ? 1.9203 1.5755 2.1003 0.1118  0.0841  0.0194  202 THR A CB  
1321  O OG1 . THR A 172 ? 1.8775 1.5227 2.0727 0.1243  0.0920  0.0482  202 THR A OG1 
1322  C CG2 . THR A 172 ? 1.8750 1.5209 2.0606 0.1203  0.0812  0.0005  202 THR A CG2 
1323  N N   . GLN A 173 ? 1.8203 1.5133 2.0353 0.1002  0.0631  0.0772  203 GLN A N   
1324  C CA  . GLN A 173 ? 1.8414 1.5435 2.0823 0.1052  0.0574  0.1008  203 GLN A CA  
1325  C C   . GLN A 173 ? 1.8485 1.5326 2.1055 0.1241  0.0697  0.1121  203 GLN A C   
1326  O O   . GLN A 173 ? 1.8441 1.5116 2.0956 0.1337  0.0820  0.1161  203 GLN A O   
1327  C CB  . GLN A 173 ? 1.8331 1.5486 2.0770 0.0988  0.0509  0.1251  203 GLN A CB  
1328  C CG  . GLN A 173 ? 1.8095 1.5380 2.0827 0.1040  0.0440  0.1471  203 GLN A CG  
1329  C CD  . GLN A 173 ? 1.8398 1.5787 2.1185 0.1014  0.0368  0.1724  203 GLN A CD  
1330  O OE1 . GLN A 173 ? 1.8339 1.5934 2.1288 0.0969  0.0249  0.1840  203 GLN A OE1 
1331  N NE2 . GLN A 173 ? 1.8730 1.5964 2.1391 0.1048  0.0432  0.1812  203 GLN A NE2 
1332  N N   . ALA A 174 ? 1.8294 1.5175 2.1065 0.1286  0.0668  0.1168  204 ALA A N   
1333  C CA  . ALA A 174 ? 1.7968 1.4728 2.0899 0.1445  0.0787  0.1285  204 ALA A CA  
1334  C C   . ALA A 174 ? 1.8647 1.5475 2.1748 0.1509  0.0814  0.1541  204 ALA A C   
1335  O O   . ALA A 174 ? 1.8622 1.5637 2.1826 0.1435  0.0702  0.1677  204 ALA A O   
1336  C CB  . ALA A 174 ? 1.7486 1.4287 2.0582 0.1446  0.0744  0.1289  204 ALA A CB  
1337  N N   . CYS A 175 ? 1.8609 1.5290 2.1750 0.1654  0.0954  0.1595  205 CYS A N   
1338  C CA  . CYS A 175 ? 1.8745 1.5479 2.2079 0.1738  0.0973  0.1815  205 CYS A CA  
1339  C C   . CYS A 175 ? 1.8774 1.5695 2.2407 0.1763  0.0935  0.1954  205 CYS A C   
1340  O O   . CYS A 175 ? 1.8799 1.5716 2.2498 0.1784  0.0984  0.1896  205 CYS A O   
1341  C CB  . CYS A 175 ? 1.9087 1.5637 2.2430 0.1897  0.1131  0.1813  205 CYS A CB  
1342  S SG  . CYS A 175 ? 2.5261 2.1588 2.8275 0.1872  0.1196  0.1638  205 CYS A SG  
1343  N N   . PRO A 176 ? 2.0264 1.7349 2.4078 0.1757  0.0845  0.2137  206 PRO A N   
1344  C CA  . PRO A 176 ? 2.0707 1.8003 2.4826 0.1772  0.0808  0.2253  206 PRO A CA  
1345  C C   . PRO A 176 ? 2.1473 1.8762 2.5818 0.1929  0.0950  0.2310  206 PRO A C   
1346  O O   . PRO A 176 ? 2.2053 1.9523 2.6651 0.1937  0.0950  0.2380  206 PRO A O   
1347  C CB  . PRO A 176 ? 2.0850 1.8313 2.5072 0.1730  0.0659  0.2414  206 PRO A CB  
1348  C CG  . PRO A 176 ? 2.0823 1.8109 2.4872 0.1769  0.0674  0.2446  206 PRO A CG  
1349  C CD  . PRO A 176 ? 2.0523 1.7605 2.4265 0.1729  0.0763  0.2247  206 PRO A CD  
1350  N N   . LYS A 177 ? 2.3286 2.0390 2.7555 0.2047  0.1073  0.2271  207 LYS A N   
1351  C CA  . LYS A 177 ? 2.3593 2.0708 2.8074 0.2200  0.1216  0.2300  207 LYS A CA  
1352  C C   . LYS A 177 ? 2.3742 2.0831 2.8189 0.2195  0.1325  0.2197  207 LYS A C   
1353  O O   . LYS A 177 ? 2.4527 2.1758 2.9204 0.2247  0.1399  0.2250  207 LYS A O   
1354  C CB  . LYS A 177 ? 2.4312 2.1234 2.8716 0.2323  0.1305  0.2273  207 LYS A CB  
1355  C CG  . LYS A 177 ? 2.3982 2.0797 2.8213 0.2266  0.1197  0.2314  207 LYS A CG  
1356  C CD  . LYS A 177 ? 2.4589 2.1570 2.9025 0.2255  0.1046  0.2503  207 LYS A CD  
1357  C CE  . LYS A 177 ? 2.6844 2.3837 3.1567 0.2433  0.1084  0.2602  207 LYS A CE  
1358  N NZ  . LYS A 177 ? 2.6871 2.3994 3.1778 0.2433  0.0911  0.2780  207 LYS A NZ  
1359  N N   . VAL A 178 ? 2.3325 2.0237 2.7485 0.2129  0.1329  0.2047  208 VAL A N   
1360  C CA  . VAL A 178 ? 2.3277 2.0117 2.7368 0.2124  0.1410  0.1955  208 VAL A CA  
1361  C C   . VAL A 178 ? 2.2718 1.9695 2.6893 0.1991  0.1306  0.1992  208 VAL A C   
1362  O O   . VAL A 178 ? 2.2362 1.9469 2.6589 0.1892  0.1164  0.2040  208 VAL A O   
1363  C CB  . VAL A 178 ? 2.3162 1.9746 2.6928 0.2122  0.1440  0.1762  208 VAL A CB  
1364  C CG1 . VAL A 178 ? 2.3647 2.0097 2.7338 0.2245  0.1545  0.1719  208 VAL A CG1 
1365  C CG2 . VAL A 178 ? 2.2401 1.8969 2.5991 0.1980  0.1286  0.1673  208 VAL A CG2 
1366  N N   . SER A 179 ? 2.1097 1.8043 2.5280 0.1981  0.1375  0.1971  209 SER A N   
1367  C CA  . SER A 179 ? 2.0608 1.7648 2.4866 0.1849  0.1284  0.2003  209 SER A CA  
1368  C C   . SER A 179 ? 2.0691 1.7497 2.4710 0.1805  0.1281  0.1872  209 SER A C   
1369  O O   . SER A 179 ? 2.0968 1.7590 2.4823 0.1893  0.1391  0.1792  209 SER A O   
1370  C CB  . SER A 179 ? 2.0190 1.7457 2.4746 0.1852  0.1356  0.2146  209 SER A CB  
1371  O OG  . SER A 179 ? 2.0863 1.8053 2.5384 0.1924  0.1519  0.2131  209 SER A OG  
1372  N N   . PHE A 180 ? 2.0273 1.7088 2.4282 0.1670  0.1141  0.1847  210 PHE A N   
1373  C CA  . PHE A 180 ? 2.0476 1.7062 2.4284 0.1613  0.1086  0.1724  210 PHE A CA  
1374  C C   . PHE A 180 ? 2.1044 1.7640 2.4950 0.1551  0.1123  0.1828  210 PHE A C   
1375  O O   . PHE A 180 ? 2.1261 1.7743 2.5106 0.1445  0.1013  0.1789  210 PHE A O   
1376  C CB  . PHE A 180 ? 2.0350 1.6926 2.4088 0.1503  0.0893  0.1604  210 PHE A CB  
1377  C CG  . PHE A 180 ? 2.0217 1.6833 2.3858 0.1527  0.0855  0.1513  210 PHE A CG  
1378  C CD1 . PHE A 180 ? 2.0002 1.6553 2.3553 0.1648  0.0982  0.1503  210 PHE A CD1 
1379  C CD2 . PHE A 180 ? 2.0065 1.6795 2.3707 0.1417  0.0693  0.1441  210 PHE A CD2 
1380  C CE1 . PHE A 180 ? 1.9155 1.5730 2.2602 0.1646  0.0948  0.1435  210 PHE A CE1 
1381  C CE2 . PHE A 180 ? 1.9323 1.6103 2.2853 0.1413  0.0663  0.1367  210 PHE A CE2 
1382  C CZ  . PHE A 180 ? 1.8841 1.5534 2.2267 0.1522  0.0792  0.1372  210 PHE A CZ  
1383  N N   . GLU A 181 ? 2.0569 1.7303 2.4630 0.1608  0.1278  0.1957  211 GLU A N   
1384  C CA  . GLU A 181 ? 2.0680 1.7459 2.4831 0.1530  0.1336  0.2062  211 GLU A CA  
1385  C C   . GLU A 181 ? 1.9938 1.6448 2.3831 0.1570  0.1422  0.2005  211 GLU A C   
1386  O O   . GLU A 181 ? 1.9362 1.5846 2.3190 0.1702  0.1568  0.1979  211 GLU A O   
1387  C CB  . GLU A 181 ? 2.0138 1.7227 2.4584 0.1567  0.1468  0.2201  211 GLU A CB  
1388  C CG  . GLU A 181 ? 2.0818 1.8047 2.5417 0.1443  0.1517  0.2319  211 GLU A CG  
1389  C CD  . GLU A 181 ? 2.1829 1.9176 2.6586 0.1281  0.1363  0.2370  211 GLU A CD  
1390  O OE1 . GLU A 181 ? 2.2778 2.0196 2.7602 0.1278  0.1228  0.2336  211 GLU A OE1 
1391  O OE2 . GLU A 181 ? 2.2167 1.9557 2.6991 0.1150  0.1383  0.2450  211 GLU A OE2 
1392  N N   . PRO A 182 ? 2.1124 1.7422 2.4864 0.1465  0.1328  0.1981  212 PRO A N   
1393  C CA  . PRO A 182 ? 2.1142 1.7159 2.4608 0.1502  0.1387  0.1934  212 PRO A CA  
1394  C C   . PRO A 182 ? 2.1453 1.7603 2.4984 0.1513  0.1586  0.2064  212 PRO A C   
1395  O O   . PRO A 182 ? 2.1650 1.7948 2.5330 0.1385  0.1610  0.2201  212 PRO A O   
1396  C CB  . PRO A 182 ? 2.1339 1.7127 2.4689 0.1361  0.1206  0.1914  212 PRO A CB  
1397  C CG  . PRO A 182 ? 2.1340 1.7257 2.4856 0.1288  0.1042  0.1874  212 PRO A CG  
1398  C CD  . PRO A 182 ? 2.1763 1.8049 2.5567 0.1310  0.1141  0.1986  212 PRO A CD  
1399  N N   . ILE A 183 ? 2.1647 1.7762 2.5071 0.1660  0.1733  0.2009  213 ILE A N   
1400  C CA  . ILE A 183 ? 2.1238 1.7508 2.4721 0.1676  0.1930  0.2105  213 ILE A CA  
1401  C C   . ILE A 183 ? 2.0796 1.6792 2.3953 0.1687  0.1979  0.2070  213 ILE A C   
1402  O O   . ILE A 183 ? 2.0628 1.6336 2.3531 0.1770  0.1909  0.1931  213 ILE A O   
1403  C CB  . ILE A 183 ? 2.1426 1.7937 2.5104 0.1836  0.2077  0.2082  213 ILE A CB  
1404  C CG1 . ILE A 183 ? 2.1529 1.7835 2.5027 0.1987  0.2055  0.1921  213 ILE A CG1 
1405  C CG2 . ILE A 183 ? 2.1671 1.8492 2.5700 0.1805  0.2035  0.2163  213 ILE A CG2 
1406  C CD1 . ILE A 183 ? 2.2023 1.8517 2.5708 0.2142  0.2173  0.1898  213 ILE A CD1 
1407  N N   . PRO A 184 ? 1.9831 1.5914 2.2978 0.1597  0.2094  0.2190  214 PRO A N   
1408  C CA  . PRO A 184 ? 2.0099 1.5920 2.2909 0.1589  0.2133  0.2181  214 PRO A CA  
1409  C C   . PRO A 184 ? 2.0066 1.5789 2.2710 0.1790  0.2230  0.2035  214 PRO A C   
1410  O O   . PRO A 184 ? 1.9999 1.5972 2.2820 0.1910  0.2388  0.2006  214 PRO A O   
1411  C CB  . PRO A 184 ? 2.0350 1.6418 2.3255 0.1459  0.2290  0.2342  214 PRO A CB  
1412  C CG  . PRO A 184 ? 2.0328 1.6669 2.3574 0.1335  0.2243  0.2441  214 PRO A CG  
1413  C CD  . PRO A 184 ? 2.0195 1.6630 2.3637 0.1475  0.2181  0.2340  214 PRO A CD  
1414  N N   . ILE A 185 ? 2.0225 1.5577 2.2540 0.1830  0.2125  0.1930  215 ILE A N   
1415  C CA  . ILE A 185 ? 2.0293 1.5521 2.2424 0.2015  0.2200  0.1772  215 ILE A CA  
1416  C C   . ILE A 185 ? 2.0618 1.5590 2.2402 0.1996  0.2207  0.1781  215 ILE A C   
1417  O O   . ILE A 185 ? 2.0786 1.5438 2.2350 0.1916  0.2026  0.1780  215 ILE A O   
1418  C CB  . ILE A 185 ? 2.0183 1.5218 2.2250 0.2114  0.2056  0.1585  215 ILE A CB  
1419  C CG1 . ILE A 185 ? 1.9894 1.5183 2.2273 0.2132  0.2056  0.1588  215 ILE A CG1 
1420  C CG2 . ILE A 185 ? 2.0303 1.5189 2.2161 0.2291  0.2128  0.1412  215 ILE A CG2 
1421  C CD1 . ILE A 185 ? 2.0583 1.5729 2.2900 0.2204  0.1932  0.1409  215 ILE A CD1 
1422  N N   . HIS A 186 ? 2.0004 1.5115 2.1740 0.2067  0.2406  0.1788  216 HIS A N   
1423  C CA  . HIS A 186 ? 2.0180 1.5074 2.1566 0.2058  0.2428  0.1798  216 HIS A CA  
1424  C C   . HIS A 186 ? 1.9682 1.4333 2.0842 0.2251  0.2394  0.1584  216 HIS A C   
1425  O O   . HIS A 186 ? 1.9666 1.4476 2.0955 0.2411  0.2516  0.1458  216 HIS A O   
1426  C CB  . HIS A 186 ? 2.1295 1.6489 2.2721 0.2024  0.2663  0.1901  216 HIS A CB  
1427  C CG  . HIS A 186 ? 2.1598 1.7095 2.3271 0.1838  0.2729  0.2089  216 HIS A CG  
1428  N ND1 . HIS A 186 ? 2.1162 1.6610 2.2672 0.1630  0.2725  0.2262  216 HIS A ND1 
1429  C CD2 . HIS A 186 ? 2.2255 1.8114 2.4328 0.1826  0.2800  0.2126  216 HIS A CD2 
1430  C CE1 . HIS A 186 ? 2.1226 1.7014 2.3037 0.1494  0.2804  0.2386  216 HIS A CE1 
1431  N NE2 . HIS A 186 ? 2.2168 1.8212 2.4329 0.1618  0.2844  0.2302  216 HIS A NE2 
1432  N N   . TYR A 187 ? 1.8027 1.2288 1.8863 0.2236  0.2220  0.1536  217 TYR A N   
1433  C CA  . TYR A 187 ? 1.8182 1.2203 1.8785 0.2413  0.2176  0.1321  217 TYR A CA  
1434  C C   . TYR A 187 ? 1.8776 1.2764 1.9118 0.2454  0.2302  0.1344  217 TYR A C   
1435  O O   . TYR A 187 ? 1.9434 1.3305 1.9573 0.2314  0.2268  0.1506  217 TYR A O   
1436  C CB  . TYR A 187 ? 1.8270 1.1896 1.8681 0.2398  0.1901  0.1219  217 TYR A CB  
1437  C CG  . TYR A 187 ? 1.8664 1.2323 1.9280 0.2440  0.1797  0.1073  217 TYR A CG  
1438  C CD1 . TYR A 187 ? 1.9070 1.2850 1.9922 0.2304  0.1718  0.1178  217 TYR A CD1 
1439  C CD2 . TYR A 187 ? 1.8396 1.1978 1.8961 0.2608  0.1780  0.0823  217 TYR A CD2 
1440  C CE1 . TYR A 187 ? 1.8666 1.2493 1.9684 0.2333  0.1623  0.1042  217 TYR A CE1 
1441  C CE2 . TYR A 187 ? 1.7911 1.1539 1.8639 0.2626  0.1693  0.0686  217 TYR A CE2 
1442  C CZ  . TYR A 187 ? 1.8199 1.1951 1.9144 0.2488  0.1613  0.0799  217 TYR A CZ  
1443  O OH  . TYR A 187 ? 1.8241 1.2057 1.9327 0.2496  0.1527  0.0664  217 TYR A OH  
1444  N N   . CYS A 188 ? 1.8333 1.2426 1.8676 0.2638  0.2445  0.1183  218 CYS A N   
1445  C CA  . CYS A 188 ? 1.8605 1.2726 1.8727 0.2693  0.2586  0.1181  218 CYS A CA  
1446  C C   . CYS A 188 ? 1.8629 1.2483 1.8501 0.2877  0.2514  0.0947  218 CYS A C   
1447  O O   . CYS A 188 ? 1.8625 1.2378 1.8573 0.2983  0.2424  0.0762  218 CYS A O   
1448  C CB  . CYS A 188 ? 1.8369 1.2933 1.8756 0.2748  0.2857  0.1196  218 CYS A CB  
1449  S SG  . CYS A 188 ? 1.7723 1.2635 1.8453 0.2552  0.2931  0.1430  218 CYS A SG  
1450  N N   . ALA A 189 ? 1.7632 1.1381 1.7189 0.2906  0.2556  0.0951  219 ALA A N   
1451  C CA  . ALA A 189 ? 1.7745 1.1253 1.7042 0.3082  0.2494  0.0731  219 ALA A CA  
1452  C C   . ALA A 189 ? 1.7727 1.1507 1.7080 0.3238  0.2736  0.0610  219 ALA A C   
1453  O O   . ALA A 189 ? 1.7854 1.1931 1.7276 0.3179  0.2929  0.0738  219 ALA A O   
1454  C CB  . ALA A 189 ? 1.8335 1.1480 1.7203 0.3014  0.2325  0.0811  219 ALA A CB  
1455  N N   . PRO A 190 ? 1.7262 1.0967 1.6604 0.3434  0.2733  0.0348  220 PRO A N   
1456  C CA  . PRO A 190 ? 1.7541 1.1498 1.6960 0.3591  0.2957  0.0210  220 PRO A CA  
1457  C C   . PRO A 190 ? 1.8285 1.2238 1.7391 0.3606  0.3031  0.0241  220 PRO A C   
1458  O O   . PRO A 190 ? 1.8571 1.2285 1.7361 0.3493  0.2895  0.0378  220 PRO A O   
1459  C CB  . PRO A 190 ? 1.7287 1.1087 1.6716 0.3770  0.2887  -0.0080 220 PRO A CB  
1460  C CG  . PRO A 190 ? 1.7373 1.0783 1.6575 0.3722  0.2610  -0.0111 220 PRO A CG  
1461  C CD  . PRO A 190 ? 1.7688 1.1094 1.6965 0.3513  0.2525  0.0149  220 PRO A CD  
1462  N N   . ALA A 191 ? 1.8604 1.2819 1.7796 0.3743  0.3239  0.0113  221 ALA A N   
1463  C CA  . ALA A 191 ? 1.8600 1.2870 1.7508 0.3762  0.3332  0.0124  221 ALA A CA  
1464  C C   . ALA A 191 ? 1.8590 1.2444 1.7074 0.3834  0.3131  0.0016  221 ALA A C   
1465  O O   . ALA A 191 ? 1.8545 1.2186 1.7030 0.3969  0.3008  -0.0199 221 ALA A O   
1466  C CB  . ALA A 191 ? 1.9439 1.4068 1.8557 0.3923  0.3579  -0.0046 221 ALA A CB  
1467  N N   . GLY A 192 ? 1.9358 1.3102 1.7476 0.3738  0.3091  0.0163  222 GLY A N   
1468  C CA  . GLY A 192 ? 1.9990 1.3322 1.7688 0.3801  0.2877  0.0085  222 GLY A CA  
1469  C C   . GLY A 192 ? 2.0286 1.3203 1.7816 0.3673  0.2588  0.0215  222 GLY A C   
1470  O O   . GLY A 192 ? 2.0817 1.3355 1.7983 0.3708  0.2375  0.0179  222 GLY A O   
1471  N N   . PHE A 193 ? 1.8880 1.1850 1.6691 0.3548  0.2558  0.0333  223 PHE A N   
1472  C CA  . PHE A 193 ? 1.8569 1.1192 1.6293 0.3413  0.2294  0.0457  223 PHE A CA  
1473  C C   . PHE A 193 ? 1.8571 1.1320 1.6325 0.3157  0.2351  0.0785  223 PHE A C   
1474  O O   . PHE A 193 ? 1.8485 1.1631 1.6393 0.3095  0.2602  0.0888  223 PHE A O   
1475  C CB  . PHE A 193 ? 1.8014 1.0595 1.6043 0.3482  0.2194  0.0285  223 PHE A CB  
1476  C CG  . PHE A 193 ? 1.7881 1.0301 1.5853 0.3708  0.2106  -0.0051 223 PHE A CG  
1477  C CD1 . PHE A 193 ? 1.8777 1.1314 1.6655 0.3878  0.2251  -0.0222 223 PHE A CD1 
1478  C CD2 . PHE A 193 ? 1.7997 1.0165 1.6013 0.3745  0.1876  -0.0211 223 PHE A CD2 
1479  C CE1 . PHE A 193 ? 1.9630 1.2037 1.7468 0.4075  0.2176  -0.0537 223 PHE A CE1 
1480  C CE2 . PHE A 193 ? 1.8519 1.0570 1.6492 0.3941  0.1803  -0.0537 223 PHE A CE2 
1481  C CZ  . PHE A 193 ? 1.9306 1.1472 1.7190 0.4104  0.1955  -0.0696 223 PHE A CZ  
1482  N N   . ALA A 194 ? 1.7990 1.0408 1.5615 0.3006  0.2114  0.0937  224 ALA A N   
1483  C CA  . ALA A 194 ? 1.8184 1.0694 1.5837 0.2746  0.2150  0.1245  224 ALA A CA  
1484  C C   . ALA A 194 ? 1.8262 1.0453 1.5960 0.2631  0.1882  0.1321  224 ALA A C   
1485  O O   . ALA A 194 ? 1.8310 1.0138 1.5899 0.2735  0.1635  0.1161  224 ALA A O   
1486  C CB  . ALA A 194 ? 1.8693 1.1123 1.5936 0.2616  0.2180  0.1446  224 ALA A CB  
1487  N N   . ILE A 195 ? 2.0974 1.3330 1.8857 0.2417  0.1933  0.1548  225 ILE A N   
1488  C CA  . ILE A 195 ? 2.0714 1.2819 1.8677 0.2278  0.1700  0.1642  225 ILE A CA  
1489  C C   . ILE A 195 ? 2.1326 1.3235 1.9019 0.2023  0.1621  0.1944  225 ILE A C   
1490  O O   . ILE A 195 ? 2.2443 1.4665 2.0184 0.1859  0.1832  0.2141  225 ILE A O   
1491  C CB  . ILE A 195 ? 1.9397 1.1858 1.7836 0.2234  0.1809  0.1647  225 ILE A CB  
1492  C CG1 . ILE A 195 ? 1.9182 1.1830 1.7872 0.2466  0.1891  0.1370  225 ILE A CG1 
1493  C CG2 . ILE A 195 ? 1.9747 1.1972 1.8273 0.2086  0.1569  0.1738  225 ILE A CG2 
1494  C CD1 . ILE A 195 ? 1.9277 1.2252 1.8412 0.2430  0.1979  0.1377  225 ILE A CD1 
1495  N N   . LEU A 196 ? 2.0175 1.1569 1.7592 0.1986  0.1313  0.1972  226 LEU A N   
1496  C CA  . LEU A 196 ? 2.0729 1.1843 1.7856 0.1737  0.1189  0.2262  226 LEU A CA  
1497  C C   . LEU A 196 ? 2.0688 1.1796 1.8084 0.1541  0.1092  0.2402  226 LEU A C   
1498  O O   . LEU A 196 ? 2.0370 1.1451 1.8048 0.1627  0.0966  0.2239  226 LEU A O   
1499  C CB  . LEU A 196 ? 2.1201 1.1726 1.7894 0.1801  0.0878  0.2226  226 LEU A CB  
1500  C CG  . LEU A 196 ? 2.1225 1.1750 1.7662 0.2019  0.0952  0.2052  226 LEU A CG  
1501  C CD1 . LEU A 196 ? 2.1834 1.1766 1.7832 0.2079  0.0624  0.2029  226 LEU A CD1 
1502  C CD2 . LEU A 196 ? 2.1299 1.2217 1.7630 0.1927  0.1277  0.2206  226 LEU A CD2 
1503  N N   . LYS A 197 ? 2.2048 1.3204 1.9356 0.1266  0.1158  0.2699  227 LYS A N   
1504  C CA  . LYS A 197 ? 2.2080 1.3268 1.9641 0.1050  0.1093  0.2856  227 LYS A CA  
1505  C C   . LYS A 197 ? 2.3117 1.3851 2.0338 0.0803  0.0878  0.3117  227 LYS A C   
1506  O O   . LYS A 197 ? 2.4688 1.5401 2.1578 0.0653  0.0977  0.3320  227 LYS A O   
1507  C CB  . LYS A 197 ? 2.1902 1.3697 1.9801 0.0932  0.1422  0.2957  227 LYS A CB  
1508  C CG  . LYS A 197 ? 2.1444 1.3328 1.9644 0.0718  0.1372  0.3100  227 LYS A CG  
1509  C CD  . LYS A 197 ? 2.1135 1.3645 1.9703 0.0641  0.1688  0.3155  227 LYS A CD  
1510  C CE  . LYS A 197 ? 2.0684 1.3289 1.9569 0.0445  0.1626  0.3273  227 LYS A CE  
1511  N NZ  . LYS A 197 ? 2.0465 1.3687 1.9740 0.0387  0.1914  0.3305  227 LYS A NZ  
1512  N N   . CYS A 198 ? 2.1865 1.2240 1.9169 0.0755  0.0583  0.3109  228 CYS A N   
1513  C CA  . CYS A 198 ? 2.2482 1.2372 1.9509 0.0521  0.0334  0.3346  228 CYS A CA  
1514  C C   . CYS A 198 ? 2.2569 1.2716 1.9774 0.0207  0.0477  0.3612  228 CYS A C   
1515  O O   . CYS A 198 ? 2.2165 1.2613 1.9807 0.0183  0.0535  0.3557  228 CYS A O   
1516  C CB  . CYS A 198 ? 2.2545 1.1955 1.9620 0.0619  -0.0052 0.3192  228 CYS A CB  
1517  S SG  . CYS A 198 ? 2.5827 1.4468 2.2434 0.0445  -0.0438 0.3409  228 CYS A SG  
1518  N N   . LYS A 199 ? 2.6435 1.6468 2.3292 -0.0043 0.0530  0.3898  229 LYS A N   
1519  C CA  . LYS A 199 ? 2.6614 1.6933 2.3603 -0.0364 0.0702  0.4153  229 LYS A CA  
1520  C C   . LYS A 199 ? 2.7889 1.7694 2.4653 -0.0647 0.0437  0.4408  229 LYS A C   
1521  O O   . LYS A 199 ? 2.8410 1.8339 2.5085 -0.0957 0.0570  0.4673  229 LYS A O   
1522  C CB  . LYS A 199 ? 2.6900 1.7608 2.3688 -0.0479 0.1038  0.4292  229 LYS A CB  
1523  C CG  . LYS A 199 ? 2.5518 1.6873 2.2602 -0.0298 0.1379  0.4109  229 LYS A CG  
1524  C CD  . LYS A 199 ? 2.5912 1.7694 2.2887 -0.0532 0.1695  0.4304  229 LYS A CD  
1525  C CE  . LYS A 199 ? 2.4483 1.6904 2.1726 -0.0356 0.2033  0.4123  229 LYS A CE  
1526  N NZ  . LYS A 199 ? 2.4834 1.7679 2.1956 -0.0584 0.2331  0.4287  229 LYS A NZ  
1527  N N   . ASP A 200 ? 2.9941 1.9182 2.6635 -0.0558 0.0062  0.4326  230 ASP A N   
1528  C CA  . ASP A 200 ? 3.1053 1.9813 2.7602 -0.0829 -0.0202 0.4560  230 ASP A CA  
1529  C C   . ASP A 200 ? 2.9876 1.8817 2.6927 -0.0924 -0.0243 0.4526  230 ASP A C   
1530  O O   . ASP A 200 ? 2.8087 1.7305 2.5541 -0.0710 -0.0219 0.4266  230 ASP A O   
1531  C CB  . ASP A 200 ? 3.1163 1.9182 2.7379 -0.0709 -0.0621 0.4505  230 ASP A CB  
1532  C CG  . ASP A 200 ? 3.0098 1.8078 2.6550 -0.0346 -0.0776 0.4126  230 ASP A CG  
1533  O OD1 . ASP A 200 ? 2.9211 1.7707 2.6089 -0.0215 -0.0574 0.3932  230 ASP A OD1 
1534  O OD2 . ASP A 200 ? 2.9802 1.7240 2.6018 -0.0198 -0.1105 0.4018  230 ASP A OD2 
1535  N N   . LYS A 201 ? 3.0535 1.9326 2.7554 -0.1257 -0.0302 0.4793  231 LYS A N   
1536  C CA  . LYS A 201 ? 2.9713 1.8703 2.7213 -0.1366 -0.0330 0.4769  231 LYS A CA  
1537  C C   . LYS A 201 ? 2.9422 1.7934 2.7056 -0.1239 -0.0734 0.4598  231 LYS A C   
1538  O O   . LYS A 201 ? 2.8543 1.7269 2.6627 -0.1226 -0.0771 0.4474  231 LYS A O   
1539  C CB  . LYS A 201 ? 3.0350 1.9412 2.7815 -0.1775 -0.0223 0.5096  231 LYS A CB  
1540  C CG  . LYS A 201 ? 2.9774 1.9591 2.7450 -0.1876 0.0221  0.5150  231 LYS A CG  
1541  C CD  . LYS A 201 ? 3.0717 2.0641 2.7961 -0.2012 0.0454  0.5340  231 LYS A CD  
1542  C CE  . LYS A 201 ? 3.0030 2.0728 2.7558 -0.2139 0.0874  0.5376  231 LYS A CE  
1543  N NZ  . LYS A 201 ? 2.8717 1.9933 2.6559 -0.1810 0.1086  0.5095  231 LYS A NZ  
1544  N N   . LYS A 202 ? 2.8247 1.6130 2.5507 -0.1147 -0.1046 0.4581  232 LYS A N   
1545  C CA  . LYS A 202 ? 2.7890 1.5289 2.5251 -0.1003 -0.1457 0.4386  232 LYS A CA  
1546  C C   . LYS A 202 ? 2.7712 1.4926 2.4896 -0.0650 -0.1578 0.4112  232 LYS A C   
1547  O O   . LYS A 202 ? 2.8496 1.5333 2.5213 -0.0624 -0.1669 0.4205  232 LYS A O   
1548  C CB  . LYS A 202 ? 2.8709 1.5450 2.5800 -0.1259 -0.1777 0.4639  232 LYS A CB  
1549  C CG  . LYS A 202 ? 2.8744 1.5657 2.6056 -0.1612 -0.1682 0.4881  232 LYS A CG  
1550  C CD  . LYS A 202 ? 2.9635 1.5850 2.6677 -0.1867 -0.2021 0.5127  232 LYS A CD  
1551  C CE  . LYS A 202 ? 3.0807 1.6656 2.7218 -0.1989 -0.2016 0.5398  232 LYS A CE  
1552  N NZ  . LYS A 202 ? 3.1612 1.6742 2.7715 -0.2261 -0.2350 0.5676  232 LYS A NZ  
1553  N N   . PHE A 203 ? 2.7886 1.5373 2.5434 -0.0388 -0.1579 0.3774  233 PHE A N   
1554  C CA  . PHE A 203 ? 2.7803 1.5191 2.5241 -0.0051 -0.1666 0.3475  233 PHE A CA  
1555  C C   . PHE A 203 ? 2.6456 1.3974 2.4318 0.0155  -0.1807 0.3119  233 PHE A C   
1556  O O   . PHE A 203 ? 2.5608 1.3660 2.3856 0.0166  -0.1586 0.3033  233 PHE A O   
1557  C CB  . PHE A 203 ? 2.7943 1.5787 2.5278 0.0066  -0.1291 0.3454  233 PHE A CB  
1558  C CG  . PHE A 203 ? 2.7780 1.5503 2.4958 0.0390  -0.1369 0.3171  233 PHE A CG  
1559  C CD1 . PHE A 203 ? 2.8282 1.5413 2.5051 0.0463  -0.1662 0.3168  233 PHE A CD1 
1560  C CD2 . PHE A 203 ? 2.6527 1.4726 2.3968 0.0618  -0.1153 0.2905  233 PHE A CD2 
1561  C CE1 . PHE A 203 ? 2.7157 1.4200 2.3801 0.0764  -0.1734 0.2887  233 PHE A CE1 
1562  C CE2 . PHE A 203 ? 2.6164 1.4269 2.3473 0.0904  -0.1214 0.2635  233 PHE A CE2 
1563  C CZ  . PHE A 203 ? 2.6348 1.3888 2.3266 0.0980  -0.1502 0.2616  233 PHE A CZ  
1564  N N   . ASN A 204 ? 2.8865 1.5908 2.6653 0.0318  -0.2179 0.2904  234 ASN A N   
1565  C CA  . ASN A 204 ? 2.7878 1.5016 2.6046 0.0503  -0.2348 0.2543  234 ASN A CA  
1566  C C   . ASN A 204 ? 2.6902 1.4339 2.5122 0.0806  -0.2213 0.2218  234 ASN A C   
1567  O O   . ASN A 204 ? 2.6275 1.3687 2.4703 0.0990  -0.2407 0.1880  234 ASN A O   
1568  C CB  . ASN A 204 ? 2.8898 1.5405 2.7003 0.0541  -0.2829 0.2424  234 ASN A CB  
1569  C CG  . ASN A 204 ? 2.9372 1.5358 2.7006 0.0667  -0.3025 0.2426  234 ASN A CG  
1570  O OD1 . ASN A 204 ? 2.9164 1.5277 2.6513 0.0734  -0.2797 0.2499  234 ASN A OD1 
1571  N ND2 . ASN A 204 ? 2.9692 1.5098 2.7256 0.0714  -0.3463 0.2323  234 ASN A ND2 
1572  N N   . GLY A 205 ? 2.5710 1.3435 2.3753 0.0858  -0.1890 0.2299  235 GLY A N   
1573  C CA  . GLY A 205 ? 2.5070 1.3101 2.3183 0.1128  -0.1739 0.2002  235 GLY A CA  
1574  C C   . GLY A 205 ? 2.5200 1.2856 2.3008 0.1358  -0.1937 0.1795  235 GLY A C   
1575  O O   . GLY A 205 ? 2.4860 1.2771 2.2667 0.1567  -0.1771 0.1584  235 GLY A O   
1576  N N   . THR A 206 ? 2.6144 1.2724 2.1696 -0.0266 -0.0876 -0.0663 236 THR A N   
1577  C CA  . THR A 206 ? 2.6417 1.2904 2.2151 -0.0088 -0.0925 -0.0571 236 THR A CA  
1578  C C   . THR A 206 ? 2.6887 1.3048 2.2147 -0.0167 -0.1040 -0.0628 236 THR A C   
1579  O O   . THR A 206 ? 2.7399 1.3205 2.2050 -0.0255 -0.1050 -0.0772 236 THR A O   
1580  C CB  . THR A 206 ? 2.6939 1.3201 2.2660 0.0140  -0.0863 -0.0605 236 THR A CB  
1581  O OG1 . THR A 206 ? 2.7504 1.3386 2.2605 0.0091  -0.0834 -0.0793 236 THR A OG1 
1582  C CG2 . THR A 206 ? 2.6478 1.3087 2.2752 0.0251  -0.0757 -0.0503 236 THR A CG2 
1583  N N   . GLY A 207 ? 2.6168 1.2436 2.1684 -0.0138 -0.1120 -0.0510 237 GLY A N   
1584  C CA  . GLY A 207 ? 2.6610 1.2571 2.1698 -0.0208 -0.1243 -0.0546 237 GLY A CA  
1585  C C   . GLY A 207 ? 2.6149 1.2335 2.1307 -0.0399 -0.1312 -0.0491 237 GLY A C   
1586  O O   . GLY A 207 ? 2.5465 1.2073 2.1038 -0.0481 -0.1262 -0.0421 237 GLY A O   
1587  N N   . PRO A 208 ? 2.4829 1.0717 1.9567 -0.0470 -0.1427 -0.0522 238 PRO A N   
1588  C CA  . PRO A 208 ? 2.4770 1.0828 1.9517 -0.0654 -0.1495 -0.0480 238 PRO A CA  
1589  C C   . PRO A 208 ? 2.5553 1.1671 2.0037 -0.0864 -0.1438 -0.0572 238 PRO A C   
1590  O O   . PRO A 208 ? 2.6164 1.1994 2.0168 -0.0903 -0.1395 -0.0694 238 PRO A O   
1591  C CB  . PRO A 208 ? 2.5234 1.0870 1.9521 -0.0651 -0.1634 -0.0497 238 PRO A CB  
1592  C CG  . PRO A 208 ? 2.5888 1.1064 1.9700 -0.0544 -0.1618 -0.0605 238 PRO A CG  
1593  C CD  . PRO A 208 ? 2.5689 1.1059 1.9927 -0.0374 -0.1502 -0.0590 238 PRO A CD  
1594  N N   . CYS A 209 ? 2.6329 1.2828 2.1137 -0.0997 -0.1430 -0.0511 239 CYS A N   
1595  C CA  . CYS A 209 ? 2.7101 1.3717 2.1755 -0.1194 -0.1372 -0.0585 239 CYS A CA  
1596  C C   . CYS A 209 ? 2.7898 1.4415 2.2244 -0.1365 -0.1442 -0.0596 239 CYS A C   
1597  O O   . CYS A 209 ? 2.7448 1.4167 2.2097 -0.1378 -0.1500 -0.0499 239 CYS A O   
1598  C CB  . CYS A 209 ? 2.6461 1.3605 2.1757 -0.1207 -0.1287 -0.0514 239 CYS A CB  
1599  S SG  . CYS A 209 ? 2.7379 1.4732 2.2608 -0.1437 -0.1219 -0.0594 239 CYS A SG  
1600  N N   . PRO A 210 ? 2.6290 1.2489 2.0018 -0.1502 -0.1429 -0.0707 240 PRO A N   
1601  C CA  . PRO A 210 ? 2.7194 1.3266 2.0584 -0.1670 -0.1480 -0.0714 240 PRO A CA  
1602  C C   . PRO A 210 ? 2.7371 1.3872 2.1152 -0.1811 -0.1441 -0.0676 240 PRO A C   
1603  O O   . PRO A 210 ? 2.7263 1.3833 2.1136 -0.1860 -0.1508 -0.0610 240 PRO A O   
1604  C CB  . PRO A 210 ? 2.8154 1.3802 2.0811 -0.1777 -0.1432 -0.0840 240 PRO A CB  
1605  C CG  . PRO A 210 ? 2.7640 1.3074 2.0172 -0.1621 -0.1403 -0.0889 240 PRO A CG  
1606  C CD  . PRO A 210 ? 2.6667 1.2550 1.9921 -0.1497 -0.1363 -0.0826 240 PRO A CD  
1607  N N   . SER A 211 ? 2.7618 1.4399 2.1626 -0.1877 -0.1336 -0.0720 241 SER A N   
1608  C CA  . SER A 211 ? 2.6813 1.4000 2.1205 -0.2005 -0.1288 -0.0696 241 SER A CA  
1609  C C   . SER A 211 ? 2.5092 1.2758 2.0236 -0.1899 -0.1252 -0.0604 241 SER A C   
1610  O O   . SER A 211 ? 2.4353 1.2186 1.9691 -0.1880 -0.1178 -0.0636 241 SER A O   
1611  C CB  . SER A 211 ? 2.6972 1.4120 2.1065 -0.2171 -0.1196 -0.0814 241 SER A CB  
1612  O OG  . SER A 211 ? 2.8402 1.5090 2.1768 -0.2276 -0.1207 -0.0887 241 SER A OG  
1613  N N   . VAL A 212 ? 2.5071 1.2947 2.0615 -0.1840 -0.1300 -0.0485 242 VAL A N   
1614  C CA  . VAL A 212 ? 2.4314 1.2626 2.0550 -0.1739 -0.1256 -0.0370 242 VAL A CA  
1615  C C   . VAL A 212 ? 2.3942 1.2637 2.0569 -0.1849 -0.1217 -0.0322 242 VAL A C   
1616  O O   . VAL A 212 ? 2.4524 1.3154 2.0997 -0.1945 -0.1263 -0.0322 242 VAL A O   
1617  C CB  . VAL A 212 ? 2.4327 1.2601 2.0745 -0.1571 -0.1317 -0.0259 242 VAL A CB  
1618  C CG1 . VAL A 212 ? 2.3770 1.2476 2.0855 -0.1465 -0.1242 -0.0129 242 VAL A CG1 
1619  C CG2 . VAL A 212 ? 2.4900 1.2757 2.0909 -0.1456 -0.1357 -0.0317 242 VAL A CG2 
1620  N N   . SER A 213 ? 2.2794 1.1871 1.9912 -0.1836 -0.1127 -0.0281 243 SER A N   
1621  C CA  . SER A 213 ? 2.2328 1.1794 1.9882 -0.1916 -0.1072 -0.0227 243 SER A CA  
1622  C C   . SER A 213 ? 2.1891 1.1708 2.0010 -0.1791 -0.1008 -0.0085 243 SER A C   
1623  O O   . SER A 213 ? 2.1890 1.1681 2.0076 -0.1669 -0.0983 -0.0053 243 SER A O   
1624  C CB  . SER A 213 ? 2.2174 1.1752 1.9716 -0.2057 -0.1007 -0.0332 243 SER A CB  
1625  O OG  . SER A 213 ? 2.2032 1.1680 1.9675 -0.2012 -0.0955 -0.0359 243 SER A OG  
1626  N N   . THR A 214 ? 2.2562 1.2688 2.1049 -0.1821 -0.0969 0.0004  244 THR A N   
1627  C CA  . THR A 214 ? 2.2200 1.2647 2.1143 -0.1716 -0.0895 0.0151  244 THR A CA  
1628  C C   . THR A 214 ? 2.1796 1.2570 2.1053 -0.1785 -0.0788 0.0160  244 THR A C   
1629  O O   . THR A 214 ? 2.1742 1.2580 2.0995 -0.1920 -0.0770 0.0078  244 THR A O   
1630  C CB  . THR A 214 ? 2.2207 1.2753 2.1294 -0.1679 -0.0932 0.0266  244 THR A CB  
1631  O OG1 . THR A 214 ? 2.1888 1.2744 2.1344 -0.1588 -0.0860 0.0411  244 THR A OG1 
1632  C CG2 . THR A 214 ? 2.2196 1.2815 2.1276 -0.1825 -0.0941 0.0226  244 THR A CG2 
1633  N N   . VAL A 215 ? 2.1380 1.2344 2.0884 -0.1688 -0.0716 0.0262  245 VAL A N   
1634  C CA  . VAL A 215 ? 2.0736 1.1994 2.0499 -0.1737 -0.0625 0.0295  245 VAL A CA  
1635  C C   . VAL A 215 ? 2.0555 1.2042 2.0541 -0.1622 -0.0603 0.0478  245 VAL A C   
1636  O O   . VAL A 215 ? 2.0676 1.2087 2.0641 -0.1494 -0.0637 0.0565  245 VAL A O   
1637  C CB  . VAL A 215 ? 2.0675 1.1891 2.0393 -0.1760 -0.0586 0.0212  245 VAL A CB  
1638  C CG1 . VAL A 215 ? 2.1395 1.2439 2.0878 -0.1896 -0.0629 0.0030  245 VAL A CG1 
1639  C CG2 . VAL A 215 ? 2.0807 1.1852 2.0426 -0.1618 -0.0595 0.0251  245 VAL A CG2 
1640  N N   . GLN A 216 ? 2.0140 1.1911 2.0324 -0.1669 -0.0570 0.0538  246 GLN A N   
1641  C CA  . GLN A 216 ? 1.9967 1.2002 2.0358 -0.1570 -0.0609 0.0718  246 GLN A CA  
1642  C C   . GLN A 216 ? 1.9848 1.1918 2.0264 -0.1501 -0.0579 0.0770  246 GLN A C   
1643  O O   . GLN A 216 ? 1.9823 1.1969 2.0321 -0.1368 -0.0611 0.0904  246 GLN A O   
1644  C CB  . GLN A 216 ? 1.9774 1.2135 2.0397 -0.1644 -0.0645 0.0775  246 GLN A CB  
1645  C CG  . GLN A 216 ? 1.9586 1.2300 2.0522 -0.1537 -0.0741 0.0967  246 GLN A CG  
1646  C CD  . GLN A 216 ? 1.9860 1.2529 2.0804 -0.1445 -0.0796 0.1036  246 GLN A CD  
1647  O OE1 . GLN A 216 ? 2.0282 1.2722 2.1040 -0.1490 -0.0787 0.0953  246 GLN A OE1 
1648  N NE2 . GLN A 216 ? 1.9621 1.2524 2.0805 -0.1320 -0.0859 0.1188  246 GLN A NE2 
1649  N N   . CYS A 217 ? 1.9886 1.1900 2.0238 -0.1594 -0.0519 0.0662  247 CYS A N   
1650  C CA  . CYS A 217 ? 1.9829 1.1853 2.0183 -0.1557 -0.0487 0.0692  247 CYS A CA  
1651  C C   . CYS A 217 ? 1.9905 1.1656 2.0074 -0.1608 -0.0428 0.0521  247 CYS A C   
1652  O O   . CYS A 217 ? 2.0010 1.1693 2.0122 -0.1735 -0.0425 0.0367  247 CYS A O   
1653  C CB  . CYS A 217 ? 1.9635 1.1967 2.0189 -0.1629 -0.0517 0.0752  247 CYS A CB  
1654  S SG  . CYS A 217 ? 2.1187 1.3963 2.2111 -0.1576 -0.0644 0.0946  247 CYS A SG  
1655  N N   . THR A 218 ? 1.8938 1.0549 1.9033 -0.1504 -0.0401 0.0551  248 THR A N   
1656  C CA  . THR A 218 ? 1.9085 1.0470 1.9032 -0.1536 -0.0390 0.0400  248 THR A CA  
1657  C C   . THR A 218 ? 1.8919 1.0419 1.8921 -0.1671 -0.0370 0.0321  248 THR A C   
1658  O O   . THR A 218 ? 1.8699 1.0441 1.8852 -0.1717 -0.0354 0.0408  248 THR A O   
1659  C CB  . THR A 218 ? 1.9222 1.0451 1.9108 -0.1378 -0.0360 0.0471  248 THR A CB  
1660  O OG1 . THR A 218 ? 1.9026 1.0425 1.9025 -0.1332 -0.0309 0.0616  248 THR A OG1 
1661  C CG2 . THR A 218 ? 1.9398 1.0538 1.9263 -0.1232 -0.0373 0.0564  248 THR A CG2 
1662  N N   . HIS A 219 ? 2.0869 1.2188 2.0710 -0.1739 -0.0405 0.0151  249 HIS A N   
1663  C CA  . HIS A 219 ? 2.0754 1.2169 2.0635 -0.1873 -0.0401 0.0055  249 HIS A CA  
1664  C C   . HIS A 219 ? 2.0601 1.2112 2.0587 -0.1817 -0.0348 0.0183  249 HIS A C   
1665  O O   . HIS A 219 ? 2.0637 1.2095 2.0623 -0.1664 -0.0316 0.0327  249 HIS A O   
1666  C CB  . HIS A 219 ? 2.1039 1.2207 2.0608 -0.1959 -0.0486 -0.0162 249 HIS A CB  
1667  C CG  . HIS A 219 ? 2.1316 1.2206 2.0616 -0.1859 -0.0518 -0.0190 249 HIS A CG  
1668  N ND1 . HIS A 219 ? 2.1675 1.2305 2.0734 -0.1755 -0.0556 -0.0199 249 HIS A ND1 
1669  C CD2 . HIS A 219 ? 2.1383 1.2200 2.0597 -0.1850 -0.0516 -0.0220 249 HIS A CD2 
1670  C CE1 . HIS A 219 ? 2.2160 1.2566 2.0998 -0.1677 -0.0566 -0.0235 249 HIS A CE1 
1671  N NE2 . HIS A 219 ? 2.1979 1.2491 2.0900 -0.1734 -0.0542 -0.0250 249 HIS A NE2 
1672  N N   . GLY A 220 ? 2.1151 1.2806 2.1221 -0.1942 -0.0343 0.0137  250 GLY A N   
1673  C CA  . GLY A 220 ? 2.1028 1.2773 2.1166 -0.1916 -0.0314 0.0262  250 GLY A CA  
1674  C C   . GLY A 220 ? 2.1196 1.2721 2.1192 -0.1841 -0.0315 0.0236  250 GLY A C   
1675  O O   . GLY A 220 ? 2.1329 1.2738 2.1183 -0.1941 -0.0372 0.0054  250 GLY A O   
1676  N N   . ILE A 221 ? 2.1312 1.2774 2.1308 -0.1665 -0.0265 0.0411  251 ILE A N   
1677  C CA  . ILE A 221 ? 2.1467 1.2715 2.1348 -0.1566 -0.0253 0.0409  251 ILE A CA  
1678  C C   . ILE A 221 ? 2.1773 1.2959 2.1572 -0.1573 -0.0371 0.0619  251 ILE A C   
1679  O O   . ILE A 221 ? 2.1633 1.2938 2.1537 -0.1449 -0.0358 0.0858  251 ILE A O   
1680  C CB  . ILE A 221 ? 2.1585 1.2662 2.1410 -0.1376 -0.0229 0.0470  251 ILE A CB  
1681  C CG1 . ILE A 221 ? 2.2085 1.3028 2.1765 -0.1427 -0.0310 0.0295  251 ILE A CG1 
1682  C CG2 . ILE A 221 ? 2.1688 1.2438 2.1281 -0.1282 -0.0300 0.0481  251 ILE A CG2 
1683  C CD1 . ILE A 221 ? 2.1987 1.2743 2.1590 -0.1258 -0.0310 0.0335  251 ILE A CD1 
1684  N N   . LYS A 222 ? 2.2787 1.3755 2.2320 -0.1735 -0.0547 0.0540  252 LYS A N   
1685  C CA  . LYS A 222 ? 2.2830 1.3685 2.2235 -0.1790 -0.0738 0.0753  252 LYS A CA  
1686  C C   . LYS A 222 ? 2.3109 1.3582 2.2224 -0.1632 -0.0806 0.0884  252 LYS A C   
1687  O O   . LYS A 222 ? 2.3674 1.3734 2.2345 -0.1623 -0.0813 0.0696  252 LYS A O   
1688  C CB  . LYS A 222 ? 2.2779 1.3497 2.1902 -0.2050 -0.0886 0.0606  252 LYS A CB  
1689  C CG  . LYS A 222 ? 2.2350 1.3477 2.1813 -0.2196 -0.0831 0.0504  252 LYS A CG  
1690  C CD  . LYS A 222 ? 2.2185 1.3186 2.1352 -0.2457 -0.0968 0.0327  252 LYS A CD  
1691  C CE  . LYS A 222 ? 2.3358 1.4038 2.2056 -0.2500 -0.0926 0.0010  252 LYS A CE  
1692  N NZ  . LYS A 222 ? 2.3262 1.4221 2.2306 -0.2408 -0.0742 -0.0160 252 LYS A NZ  
1693  N N   . PRO A 223 ? 2.2316 1.2922 2.1639 -0.1495 -0.0855 0.1196  253 PRO A N   
1694  C CA  . PRO A 223 ? 2.2567 1.2829 2.1642 -0.1321 -0.0899 0.1333  253 PRO A CA  
1695  C C   . PRO A 223 ? 2.3461 1.3253 2.1963 -0.1459 -0.1072 0.1340  253 PRO A C   
1696  O O   . PRO A 223 ? 2.3562 1.3415 2.2122 -0.1455 -0.1204 0.1633  253 PRO A O   
1697  C CB  . PRO A 223 ? 2.2636 1.3320 2.2178 -0.1148 -0.0892 0.1671  253 PRO A CB  
1698  C CG  . PRO A 223 ? 2.2204 1.3343 2.2088 -0.1308 -0.0963 0.1753  253 PRO A CG  
1699  C CD  . PRO A 223 ? 2.1862 1.2978 2.1653 -0.1476 -0.0868 0.1431  253 PRO A CD  
1700  N N   . VAL A 224 ? 2.4517 1.3855 2.2413 -0.1590 -0.1055 0.1021  254 VAL A N   
1701  C CA  . VAL A 224 ? 2.5603 1.4391 2.2722 -0.1758 -0.1143 0.0951  254 VAL A CA  
1702  C C   . VAL A 224 ? 2.6460 1.4950 2.3168 -0.1513 -0.1032 0.0954  254 VAL A C   
1703  O O   . VAL A 224 ? 2.6925 1.4936 2.3296 -0.1412 -0.0938 0.0739  254 VAL A O   
1704  C CB  . VAL A 224 ? 2.5905 1.4483 2.2547 -0.1998 -0.1110 0.0563  254 VAL A CB  
1705  C CG1 . VAL A 224 ? 2.7190 1.5510 2.3082 -0.2130 -0.1094 0.0434  254 VAL A CG1 
1706  C CG2 . VAL A 224 ? 2.5211 1.4315 2.2362 -0.2190 -0.1170 0.0539  254 VAL A CG2 
1707  N N   . VAL A 225 ? 2.4884 1.4004 2.1777 -0.1372 -0.0993 0.1173  255 VAL A N   
1708  C CA  . VAL A 225 ? 2.4802 1.3920 2.1437 -0.1118 -0.0846 0.1181  255 VAL A CA  
1709  C C   . VAL A 225 ? 2.4888 1.3883 2.0792 -0.1239 -0.0750 0.0907  255 VAL A C   
1710  O O   . VAL A 225 ? 2.4720 1.4207 2.0575 -0.1386 -0.0778 0.0950  255 VAL A O   
1711  C CB  . VAL A 225 ? 2.4540 1.4382 2.1701 -0.0933 -0.0837 0.1537  255 VAL A CB  
1712  C CG1 . VAL A 225 ? 2.6104 1.5920 2.3010 -0.0678 -0.0670 0.1521  255 VAL A CG1 
1713  C CG2 . VAL A 225 ? 2.3683 1.3665 2.1561 -0.0847 -0.0931 0.1806  255 VAL A CG2 
1714  N N   . SER A 226 ? 2.2946 1.1276 1.8270 -0.1184 -0.0639 0.0628  256 SER A N   
1715  C CA  . SER A 226 ? 2.3558 1.1708 1.8144 -0.1301 -0.0526 0.0351  256 SER A CA  
1716  C C   . SER A 226 ? 2.4086 1.1644 1.8201 -0.1089 -0.0364 0.0163  256 SER A C   
1717  O O   . SER A 226 ? 2.4433 1.1644 1.8761 -0.0884 -0.0367 0.0210  256 SER A O   
1718  C CB  . SER A 226 ? 2.3731 1.1573 1.7947 -0.1638 -0.0597 0.0085  256 SER A CB  
1719  O OG  . SER A 226 ? 2.3792 1.0923 1.7911 -0.1669 -0.0632 -0.0080 256 SER A OG  
1720  N N   . THR A 227 ? 2.4985 1.2435 1.8457 -0.1141 -0.0223 -0.0051 257 THR A N   
1721  C CA  . THR A 227 ? 2.5430 1.2311 1.8396 -0.0954 -0.0051 -0.0259 257 THR A CA  
1722  C C   . THR A 227 ? 2.6140 1.2428 1.8290 -0.1184 0.0016  -0.0641 257 THR A C   
1723  O O   . THR A 227 ? 2.6089 1.2550 1.8038 -0.1482 -0.0041 -0.0736 257 THR A O   
1724  C CB  . THR A 227 ? 2.5609 1.2900 1.8537 -0.0759 0.0112  -0.0161 257 THR A CB  
1725  O OG1 . THR A 227 ? 2.4986 1.2741 1.7657 -0.0980 0.0137  -0.0178 257 THR A OG1 
1726  C CG2 . THR A 227 ? 2.5568 1.3391 1.9259 -0.0516 0.0071  0.0195  257 THR A CG2 
1727  N N   . GLN A 228 ? 2.6645 1.2232 1.8325 -0.1040 0.0140  -0.0862 258 GLN A N   
1728  C CA  . GLN A 228 ? 2.7783 1.2703 1.8625 -0.1223 0.0233  -0.1240 258 GLN A CA  
1729  C C   . GLN A 228 ? 2.7669 1.2231 1.8361 -0.1530 0.0096  -0.1404 258 GLN A C   
1730  O O   . GLN A 228 ? 2.7740 1.2139 1.8399 -0.1484 0.0099  -0.1550 258 GLN A O   
1731  C CB  . GLN A 228 ? 2.8270 1.3484 1.8616 -0.1353 0.0381  -0.1357 258 GLN A CB  
1732  C CG  . GLN A 228 ? 2.8812 1.4220 1.9152 -0.1069 0.0561  -0.1275 258 GLN A CG  
1733  C CD  . GLN A 228 ? 2.9444 1.5099 1.9251 -0.1221 0.0718  -0.1401 258 GLN A CD  
1734  O OE1 . GLN A 228 ? 2.9587 1.5336 1.9061 -0.1538 0.0677  -0.1526 258 GLN A OE1 
1735  N NE2 . GLN A 228 ? 3.0069 1.5816 1.9779 -0.1004 0.0905  -0.1380 258 GLN A NE2 
1736  N N   . LEU A 229 ? 2.8268 1.3380 1.9240 -0.1780 -0.0026 -0.1309 259 LEU A N   
1737  C CA  . LEU A 229 ? 2.7956 1.2910 1.8884 -0.2078 -0.0146 -0.1460 259 LEU A CA  
1738  C C   . LEU A 229 ? 2.7301 1.2771 1.9156 -0.2027 -0.0324 -0.1185 259 LEU A C   
1739  O O   . LEU A 229 ? 2.6654 1.2508 1.8929 -0.2047 -0.0415 -0.0925 259 LEU A O   
1740  C CB  . LEU A 229 ? 2.7770 1.3046 1.8388 -0.2408 -0.0156 -0.1576 259 LEU A CB  
1741  C CG  . LEU A 229 ? 2.8589 1.3791 1.8476 -0.2456 0.0028  -0.1785 259 LEU A CG  
1742  C CD1 . LEU A 229 ? 2.8898 1.4579 1.8616 -0.2787 -0.0017 -0.1859 259 LEU A CD1 
1743  C CD2 . LEU A 229 ? 2.9538 1.3969 1.8760 -0.2436 0.0165  -0.2106 259 LEU A CD2 
1744  N N   . LEU A 230 ? 2.8820 1.4638 2.1162 -0.1925 -0.0358 -0.1209 260 LEU A N   
1745  C CA  . LEU A 230 ? 2.7722 1.4099 2.0952 -0.1892 -0.0491 -0.1001 260 LEU A CA  
1746  C C   . LEU A 230 ? 2.7485 1.4217 2.0864 -0.2192 -0.0578 -0.1057 260 LEU A C   
1747  O O   . LEU A 230 ? 2.7752 1.4550 2.0882 -0.2340 -0.0541 -0.1291 260 LEU A O   
1748  C CB  . LEU A 230 ? 2.7286 1.3898 2.0927 -0.1712 -0.0476 -0.1038 260 LEU A CB  
1749  C CG  . LEU A 230 ? 2.7266 1.3605 2.0866 -0.1409 -0.0409 -0.0982 260 LEU A CG  
1750  C CD1 . LEU A 230 ? 2.7000 1.3598 2.0996 -0.1294 -0.0418 -0.1027 260 LEU A CD1 
1751  C CD2 . LEU A 230 ? 2.6332 1.2724 2.0335 -0.1233 -0.0448 -0.0686 260 LEU A CD2 
1752  N N   . LEU A 231 ? 2.7430 1.4413 2.1236 -0.2273 -0.0694 -0.0828 261 LEU A N   
1753  C CA  . LEU A 231 ? 2.7402 1.4727 2.1382 -0.2556 -0.0790 -0.0860 261 LEU A CA  
1754  C C   . LEU A 231 ? 2.6704 1.4651 2.1618 -0.2501 -0.0861 -0.0709 261 LEU A C   
1755  O O   . LEU A 231 ? 2.6252 1.4380 2.1710 -0.2298 -0.0881 -0.0464 261 LEU A O   
1756  C CB  . LEU A 231 ? 2.8307 1.5444 2.1998 -0.2754 -0.0879 -0.0721 261 LEU A CB  
1757  C CG  . LEU A 231 ? 2.8972 1.5871 2.1884 -0.2762 -0.0747 -0.0878 261 LEU A CG  
1758  C CD1 . LEU A 231 ? 2.8982 1.6736 2.2098 -0.2791 -0.0780 -0.0685 261 LEU A CD1 
1759  C CD2 . LEU A 231 ? 2.9239 1.5697 2.1430 -0.2967 -0.0656 -0.1285 261 LEU A CD2 
1760  N N   . ASN A 232 ? 2.7294 1.5590 2.2393 -0.2679 -0.0878 -0.0863 262 ASN A N   
1761  C CA  . ASN A 232 ? 2.6424 1.5320 2.2365 -0.2661 -0.0907 -0.0775 262 ASN A CA  
1762  C C   . ASN A 232 ? 2.5896 1.5025 2.2382 -0.2407 -0.0832 -0.0697 262 ASN A C   
1763  O O   . ASN A 232 ? 2.5130 1.4642 2.2294 -0.2316 -0.0833 -0.0494 262 ASN A O   
1764  C CB  . ASN A 232 ? 2.6297 1.5451 2.2665 -0.2753 -0.1026 -0.0519 262 ASN A CB  
1765  C CG  . ASN A 232 ? 2.7327 1.6536 2.3455 -0.3060 -0.1119 -0.0623 262 ASN A CG  
1766  O OD1 . ASN A 232 ? 2.8172 1.7000 2.3566 -0.3224 -0.1125 -0.0778 262 ASN A OD1 
1767  N ND2 . ASN A 232 ? 2.7591 1.7306 2.4343 -0.3146 -0.1171 -0.0562 262 ASN A ND2 
1768  N N   . GLY A 233 ? 2.5646 1.4567 2.1835 -0.2302 -0.0756 -0.0858 263 GLY A N   
1769  C CA  . GLY A 233 ? 2.5259 1.4395 2.1921 -0.2096 -0.0699 -0.0798 263 GLY A CA  
1770  C C   . GLY A 233 ? 2.4945 1.4416 2.1864 -0.2152 -0.0658 -0.0969 263 GLY A C   
1771  O O   . GLY A 233 ? 2.4888 1.4457 2.1679 -0.2328 -0.0672 -0.1121 263 GLY A O   
1772  N N   . SER A 234 ? 2.4251 1.3875 2.1505 -0.2004 -0.0613 -0.0931 264 SER A N   
1773  C CA  . SER A 234 ? 2.4237 1.3787 2.1233 -0.2107 -0.0640 -0.1041 264 SER A CA  
1774  C C   . SER A 234 ? 2.4894 1.4020 2.1167 -0.2131 -0.0624 -0.1231 264 SER A C   
1775  O O   . SER A 234 ? 2.5005 1.3855 2.1047 -0.1988 -0.0600 -0.1228 264 SER A O   
1776  C CB  . SER A 234 ? 2.3870 1.3493 2.1136 -0.2010 -0.0649 -0.0902 264 SER A CB  
1777  O OG  . SER A 234 ? 2.3091 1.3104 2.0988 -0.1992 -0.0634 -0.0723 264 SER A OG  
1778  N N   . LEU A 235 ? 2.5044 1.4120 2.0965 -0.2310 -0.0623 -0.1390 265 LEU A N   
1779  C CA  . LEU A 235 ? 2.5842 1.4518 2.1041 -0.2356 -0.0579 -0.1560 265 LEU A CA  
1780  C C   . LEU A 235 ? 2.6134 1.4541 2.1058 -0.2294 -0.0579 -0.1538 265 LEU A C   
1781  O O   . LEU A 235 ? 2.5532 1.4089 2.0732 -0.2301 -0.0616 -0.1449 265 LEU A O   
1782  C CB  . LEU A 235 ? 2.6301 1.5027 2.1223 -0.2574 -0.0560 -0.1719 265 LEU A CB  
1783  C CG  . LEU A 235 ? 2.5490 1.4470 2.0646 -0.2645 -0.0575 -0.1756 265 LEU A CG  
1784  C CD1 . LEU A 235 ? 2.4622 1.4025 2.0299 -0.2767 -0.0628 -0.1714 265 LEU A CD1 
1785  C CD2 . LEU A 235 ? 2.6387 1.5150 2.0942 -0.2754 -0.0519 -0.1950 265 LEU A CD2 
1786  N N   . ALA A 236 ? 2.5998 1.3996 2.0361 -0.2238 -0.0535 -0.1621 266 ALA A N   
1787  C CA  . ALA A 236 ? 2.6478 1.4172 2.0525 -0.2179 -0.0541 -0.1602 266 ALA A CA  
1788  C C   . ALA A 236 ? 2.7057 1.4625 2.0681 -0.2369 -0.0516 -0.1695 266 ALA A C   
1789  O O   . ALA A 236 ? 2.6978 1.4663 2.0506 -0.2536 -0.0480 -0.1791 266 ALA A O   
1790  C CB  . ALA A 236 ? 2.7109 1.4398 2.0724 -0.2041 -0.0500 -0.1652 266 ALA A CB  
1791  N N   . GLU A 237 ? 2.9015 1.6340 2.2386 -0.2345 -0.0533 -0.1661 267 GLU A N   
1792  C CA  . GLU A 237 ? 3.0213 1.7374 2.3159 -0.2517 -0.0499 -0.1727 267 GLU A CA  
1793  C C   . GLU A 237 ? 3.1595 1.8259 2.3775 -0.2551 -0.0425 -0.1828 267 GLU A C   
1794  O O   . GLU A 237 ? 3.2139 1.8509 2.4100 -0.2401 -0.0430 -0.1815 267 GLU A O   
1795  C CB  . GLU A 237 ? 3.0098 1.7309 2.3226 -0.2505 -0.0562 -0.1625 267 GLU A CB  
1796  C CG  . GLU A 237 ? 2.9202 1.6872 2.3096 -0.2439 -0.0628 -0.1502 267 GLU A CG  
1797  C CD  . GLU A 237 ? 2.9104 1.7128 2.3297 -0.2603 -0.0613 -0.1534 267 GLU A CD  
1798  O OE1 . GLU A 237 ? 2.9915 1.7857 2.3757 -0.2758 -0.0550 -0.1660 267 GLU A OE1 
1799  O OE2 . GLU A 237 ? 2.8839 1.7221 2.3620 -0.2579 -0.0656 -0.1435 267 GLU A OE2 
1800  N N   . GLU A 238 ? 3.2130 1.8709 2.3925 -0.2752 -0.0349 -0.1926 268 GLU A N   
1801  C CA  . GLU A 238 ? 3.2878 1.9008 2.3925 -0.2844 -0.0251 -0.2023 268 GLU A CA  
1802  C C   . GLU A 238 ? 3.3591 1.9546 2.4418 -0.2753 -0.0202 -0.2091 268 GLU A C   
1803  O O   . GLU A 238 ? 3.3904 2.0088 2.4892 -0.2804 -0.0172 -0.2159 268 GLU A O   
1804  C CB  . GLU A 238 ? 3.3373 1.9113 2.4038 -0.2799 -0.0275 -0.1964 268 GLU A CB  
1805  C CG  . GLU A 238 ? 3.2926 1.8842 2.3884 -0.2832 -0.0348 -0.1873 268 GLU A CG  
1806  C CD  . GLU A 238 ? 3.4303 1.9885 2.4693 -0.2988 -0.0294 -0.1894 268 GLU A CD  
1807  O OE1 . GLU A 238 ? 3.6295 2.1405 2.6071 -0.2982 -0.0250 -0.1923 268 GLU A OE1 
1808  O OE2 . GLU A 238 ? 3.4683 2.0463 2.5238 -0.3116 -0.0292 -0.1879 268 GLU A OE2 
1809  N N   . GLU A 239 ? 3.3637 1.9187 2.4098 -0.2620 -0.0196 -0.2080 269 GLU A N   
1810  C CA  . GLU A 239 ? 3.3539 1.8910 2.3804 -0.2515 -0.0142 -0.2149 269 GLU A CA  
1811  C C   . GLU A 239 ? 3.2043 1.7697 2.2916 -0.2317 -0.0216 -0.2082 269 GLU A C   
1812  O O   . GLU A 239 ? 3.1057 1.6897 2.2393 -0.2210 -0.0312 -0.1962 269 GLU A O   
1813  C CB  . GLU A 239 ? 3.4121 1.8933 2.3743 -0.2456 -0.0094 -0.2175 269 GLU A CB  
1814  C CG  . GLU A 239 ? 3.4639 1.9241 2.4276 -0.2301 -0.0187 -0.2073 269 GLU A CG  
1815  C CD  . GLU A 239 ? 3.5708 1.9737 2.4666 -0.2257 -0.0132 -0.2118 269 GLU A CD  
1816  O OE1 . GLU A 239 ? 3.6675 2.0507 2.5242 -0.2307 -0.0018 -0.2222 269 GLU A OE1 
1817  O OE2 . GLU A 239 ? 3.6463 2.0231 2.5265 -0.2181 -0.0203 -0.2051 269 GLU A OE2 
1818  N N   . VAL A 240 ? 3.0901 1.6583 2.1758 -0.2277 -0.0160 -0.2160 270 VAL A N   
1819  C CA  . VAL A 240 ? 3.0058 1.5968 2.1439 -0.2095 -0.0206 -0.2102 270 VAL A CA  
1820  C C   . VAL A 240 ? 3.0383 1.6061 2.1817 -0.1859 -0.0243 -0.2026 270 VAL A C   
1821  O O   . VAL A 240 ? 3.1951 1.7204 2.2885 -0.1809 -0.0206 -0.2068 270 VAL A O   
1822  C CB  . VAL A 240 ? 3.0373 1.6307 2.1621 -0.2120 -0.0125 -0.2222 270 VAL A CB  
1823  C CG1 . VAL A 240 ? 2.9380 1.5649 2.0745 -0.2337 -0.0120 -0.2279 270 VAL A CG1 
1824  C CG2 . VAL A 240 ? 3.2141 1.7608 2.2682 -0.2123 -0.0015 -0.2342 270 VAL A CG2 
1825  N N   . MET A 241 ? 2.9019 1.4982 2.1082 -0.1714 -0.0314 -0.1905 271 MET A N   
1826  C CA  . MET A 241 ? 2.9157 1.5003 2.1428 -0.1489 -0.0362 -0.1806 271 MET A CA  
1827  C C   . MET A 241 ? 2.9604 1.5407 2.2014 -0.1302 -0.0310 -0.1826 271 MET A C   
1828  O O   . MET A 241 ? 2.9296 1.5316 2.1900 -0.1330 -0.0271 -0.1857 271 MET A O   
1829  C CB  . MET A 241 ? 2.8134 1.4337 2.1037 -0.1453 -0.0461 -0.1640 271 MET A CB  
1830  C CG  . MET A 241 ? 2.8349 1.4367 2.1270 -0.1314 -0.0527 -0.1553 271 MET A CG  
1831  S SD  . MET A 241 ? 2.9059 1.4654 2.1251 -0.1451 -0.0538 -0.1628 271 MET A SD  
1832  C CE  . MET A 241 ? 2.8951 1.4889 2.1290 -0.1703 -0.0557 -0.1613 271 MET A CE  
1833  N N   . ILE A 242 ? 2.8078 1.3592 2.0387 -0.1108 -0.0310 -0.1809 272 ILE A N   
1834  C CA  . ILE A 242 ? 2.8652 1.4095 2.1113 -0.0895 -0.0255 -0.1820 272 ILE A CA  
1835  C C   . ILE A 242 ? 2.8163 1.3694 2.1128 -0.0689 -0.0328 -0.1660 272 ILE A C   
1836  O O   . ILE A 242 ? 2.8595 1.3897 2.1389 -0.0637 -0.0383 -0.1633 272 ILE A O   
1837  C CB  . ILE A 242 ? 3.0263 1.5235 2.2080 -0.0845 -0.0161 -0.1976 272 ILE A CB  
1838  C CG1 . ILE A 242 ? 3.0169 1.5055 2.1458 -0.1067 -0.0077 -0.2128 272 ILE A CG1 
1839  C CG2 . ILE A 242 ? 3.0921 1.5820 2.2909 -0.0614 -0.0095 -0.1995 272 ILE A CG2 
1840  C CD1 . ILE A 242 ? 2.9847 1.5016 2.1329 -0.1139 -0.0030 -0.2171 272 ILE A CD1 
1841  N N   . ARG A 243 ? 2.6994 1.2849 2.0572 -0.0574 -0.0328 -0.1546 273 ARG A N   
1842  C CA  . ARG A 243 ? 2.6584 1.2578 2.0696 -0.0389 -0.0385 -0.1372 273 ARG A CA  
1843  C C   . ARG A 243 ? 2.6892 1.2739 2.1106 -0.0152 -0.0325 -0.1334 273 ARG A C   
1844  O O   . ARG A 243 ? 2.7082 1.2740 2.0985 -0.0156 -0.0271 -0.1347 273 ARG A O   
1845  C CB  . ARG A 243 ? 2.5551 1.2008 2.0245 -0.0471 -0.0449 -0.1202 273 ARG A CB  
1846  C CG  . ARG A 243 ? 2.5736 1.2249 2.0233 -0.0693 -0.0516 -0.1223 273 ARG A CG  
1847  C CD  . ARG A 243 ? 2.4804 1.1789 1.9895 -0.0769 -0.0560 -0.1068 273 ARG A CD  
1848  N NE  . ARG A 243 ? 2.4222 1.1268 1.9157 -0.0966 -0.0618 -0.1090 273 ARG A NE  
1849  C CZ  . ARG A 243 ? 2.4132 1.1281 1.8901 -0.1167 -0.0605 -0.1176 273 ARG A CZ  
1850  N NH1 . ARG A 243 ? 2.4629 1.1830 1.9352 -0.1210 -0.0545 -0.1250 273 ARG A NH1 
1851  N NH2 . ARG A 243 ? 2.4140 1.1341 1.8793 -0.1328 -0.0650 -0.1188 273 ARG A NH2 
1852  N N   . SER A 244 ? 2.7363 1.3140 2.1808 0.0055  -0.0340 -0.1278 274 SER A N   
1853  C CA  . SER A 244 ? 2.8291 1.3788 2.2681 0.0314  -0.0293 -0.1227 274 SER A CA  
1854  C C   . SER A 244 ? 2.8484 1.4162 2.3463 0.0505  -0.0344 -0.1087 274 SER A C   
1855  O O   . SER A 244 ? 2.8622 1.4292 2.3618 0.0470  -0.0401 -0.1104 274 SER A O   
1856  C CB  . SER A 244 ? 2.9804 1.4737 2.3448 0.0394  -0.0194 -0.1422 274 SER A CB  
1857  O OG  . SER A 244 ? 3.0694 1.5373 2.4315 0.0670  -0.0130 -0.1383 274 SER A OG  
1858  N N   . GLU A 245 ? 2.6806 1.2527 2.2097 0.0710  -0.0328 -0.0939 275 GLU A N   
1859  C CA  . GLU A 245 ? 2.7103 1.3008 2.2972 0.0905  -0.0362 -0.0794 275 GLU A CA  
1860  C C   . GLU A 245 ? 2.8658 1.4163 2.4243 0.1086  -0.0341 -0.0916 275 GLU A C   
1861  O O   . GLU A 245 ? 2.9243 1.4860 2.5180 0.1154  -0.0385 -0.0861 275 GLU A O   
1862  C CB  . GLU A 245 ? 2.6936 1.3016 2.3214 0.1083  -0.0343 -0.0597 275 GLU A CB  
1863  C CG  . GLU A 245 ? 2.7212 1.3559 2.4154 0.1268  -0.0366 -0.0423 275 GLU A CG  
1864  C CD  . GLU A 245 ? 2.7010 1.3585 2.4380 0.1435  -0.0343 -0.0212 275 GLU A CD  
1865  O OE1 . GLU A 245 ? 2.6958 1.3425 2.4060 0.1427  -0.0313 -0.0208 275 GLU A OE1 
1866  O OE2 . GLU A 245 ? 2.6910 1.3766 2.4863 0.1573  -0.0346 -0.0045 275 GLU A OE2 
1867  N N   . ASN A 246 ? 2.8982 1.4009 2.3918 0.1163  -0.0258 -0.1083 276 ASN A N   
1868  C CA  . ASN A 246 ? 3.0234 1.4855 2.4860 0.1337  -0.0221 -0.1215 276 ASN A CA  
1869  C C   . ASN A 246 ? 3.1234 1.5397 2.5031 0.1265  -0.0114 -0.1437 276 ASN A C   
1870  O O   . ASN A 246 ? 3.1767 1.5694 2.5236 0.1366  0.0000  -0.1485 276 ASN A O   
1871  C CB  . ASN A 246 ? 3.1208 1.5769 2.6146 0.1667  -0.0187 -0.1126 276 ASN A CB  
1872  C CG  . ASN A 246 ? 3.3098 1.7359 2.7943 0.1850  -0.0182 -0.1220 276 ASN A CG  
1873  O OD1 . ASN A 246 ? 3.3613 1.7586 2.7983 0.1751  -0.0174 -0.1383 276 ASN A OD1 
1874  N ND2 . ASN A 246 ? 3.5121 1.9453 3.0428 0.2120  -0.0187 -0.1113 276 ASN A ND2 
1875  N N   . ILE A 247 ? 3.0991 1.5043 2.4448 0.1085  -0.0135 -0.1567 277 ILE A N   
1876  C CA  . ILE A 247 ? 3.1621 1.5281 2.4300 0.0980  -0.0027 -0.1771 277 ILE A CA  
1877  C C   . ILE A 247 ? 3.3387 1.6577 2.5694 0.1231  0.0092  -0.1886 277 ILE A C   
1878  O O   . ILE A 247 ? 3.4299 1.7177 2.6036 0.1226  0.0239  -0.2018 277 ILE A O   
1879  C CB  . ILE A 247 ? 3.0566 1.4255 2.3040 0.0751  -0.0082 -0.1860 277 ILE A CB  
1880  C CG1 . ILE A 247 ? 2.9048 1.3197 2.1921 0.0539  -0.0193 -0.1740 277 ILE A CG1 
1881  C CG2 . ILE A 247 ? 3.1256 1.4619 2.2964 0.0601  0.0034  -0.2051 277 ILE A CG2 
1882  C CD1 . ILE A 247 ? 2.9363 1.3243 2.1630 0.0333  -0.0253 -0.1799 277 ILE A CD1 
1883  N N   . THR A 248 ? 3.3938 1.7080 2.6573 0.1450  0.0043  -0.1843 278 THR A N   
1884  C CA  . THR A 248 ? 3.5401 1.8127 2.7769 0.1715  0.0153  -0.1950 278 THR A CA  
1885  C C   . THR A 248 ? 3.5600 1.8274 2.8011 0.1930  0.0275  -0.1920 278 THR A C   
1886  O O   . THR A 248 ? 3.6687 1.8986 2.8677 0.2090  0.0434  -0.2059 278 THR A O   
1887  C CB  . THR A 248 ? 3.5511 1.8243 2.8302 0.1899  0.0056  -0.1892 278 THR A CB  
1888  O OG1 . THR A 248 ? 3.4530 1.7687 2.8079 0.1984  -0.0045 -0.1680 278 THR A OG1 
1889  C CG2 . THR A 248 ? 3.4997 1.7699 2.7638 0.1702  -0.0036 -0.1941 278 THR A CG2 
1890  N N   . ASN A 249 ? 3.3617 1.6664 2.6526 0.1937  0.0217  -0.1739 279 ASN A N   
1891  C CA  . ASN A 249 ? 3.3432 1.6473 2.6417 0.2137  0.0330  -0.1681 279 ASN A CA  
1892  C C   . ASN A 249 ? 3.3157 1.6057 2.5574 0.1956  0.0456  -0.1761 279 ASN A C   
1893  O O   . ASN A 249 ? 3.1795 1.4936 2.4258 0.1697  0.0375  -0.1696 279 ASN A O   
1894  C CB  . ASN A 249 ? 3.2197 1.5717 2.5993 0.2226  0.0211  -0.1430 279 ASN A CB  
1895  C CG  . ASN A 249 ? 3.2165 1.5686 2.6152 0.2524  0.0322  -0.1354 279 ASN A CG  
1896  O OD1 . ASN A 249 ? 3.2798 1.5979 2.6269 0.2628  0.0511  -0.1488 279 ASN A OD1 
1897  N ND2 . ASN A 249 ? 3.1555 1.5483 2.6290 0.2659  0.0225  -0.1138 279 ASN A ND2 
1898  N N   . ASN A 250 ? 3.5680 1.8199 2.7571 0.2086  0.0667  -0.1908 280 ASN A N   
1899  C CA  . ASN A 250 ? 3.5994 1.8343 2.7293 0.1905  0.0815  -0.1998 280 ASN A CA  
1900  C C   . ASN A 250 ? 3.5163 1.7716 2.6736 0.1970  0.0845  -0.1828 280 ASN A C   
1901  O O   . ASN A 250 ? 3.4805 1.7219 2.5916 0.1822  0.0971  -0.1883 280 ASN A O   
1902  C CB  . ASN A 250 ? 3.7707 1.9586 2.8332 0.2010  0.1068  -0.2222 280 ASN A CB  
1903  C CG  . ASN A 250 ? 3.8498 2.0298 2.9357 0.2394  0.1207  -0.2198 280 ASN A CG  
1904  O OD1 . ASN A 250 ? 3.8892 2.0682 3.0081 0.2628  0.1161  -0.2196 280 ASN A OD1 
1905  N ND2 . ASN A 250 ? 3.8586 2.0350 2.9298 0.2461  0.1382  -0.2175 280 ASN A ND2 
1906  N N   . ALA A 251 ? 3.4991 1.7876 2.7303 0.2175  0.0734  -0.1619 281 ALA A N   
1907  C CA  . ALA A 251 ? 3.4193 1.7326 2.6862 0.2261  0.0745  -0.1415 281 ALA A CA  
1908  C C   . ALA A 251 ? 3.2396 1.5968 2.5523 0.2023  0.0538  -0.1222 281 ALA A C   
1909  O O   . ALA A 251 ? 3.1852 1.5613 2.5183 0.2022  0.0543  -0.1049 281 ALA A O   
1910  C CB  . ALA A 251 ? 3.4243 1.7538 2.7490 0.2639  0.0765  -0.1288 281 ALA A CB  
1911  N N   . LYS A 252 ? 3.1777 1.5521 2.5066 0.1823  0.0375  -0.1244 282 LYS A N   
1912  C CA  . LYS A 252 ? 2.9827 1.4018 2.3566 0.1587  0.0204  -0.1088 282 LYS A CA  
1913  C C   . LYS A 252 ? 2.9250 1.3329 2.2448 0.1259  0.0223  -0.1210 282 LYS A C   
1914  O O   . LYS A 252 ? 2.9421 1.3194 2.2042 0.1147  0.0288  -0.1425 282 LYS A O   
1915  C CB  . LYS A 252 ? 2.9846 1.4318 2.4092 0.1558  0.0051  -0.1046 282 LYS A CB  
1916  C CG  . LYS A 252 ? 2.9186 1.4194 2.4288 0.1603  -0.0069 -0.0785 282 LYS A CG  
1917  C CD  . LYS A 252 ? 3.0286 1.5312 2.5706 0.1938  -0.0012 -0.0658 282 LYS A CD  
1918  C CE  . LYS A 252 ? 2.9617 1.5205 2.5894 0.1975  -0.0116 -0.0388 282 LYS A CE  
1919  N NZ  . LYS A 252 ? 2.9697 1.5359 2.6319 0.2302  -0.0065 -0.0257 282 LYS A NZ  
1920  N N   . ASN A 253 ? 2.8188 1.2538 2.1598 0.1104  0.0166  -0.1066 283 ASN A N   
1921  C CA  . ASN A 253 ? 2.7628 1.1920 2.0592 0.0788  0.0174  -0.1166 283 ASN A CA  
1922  C C   . ASN A 253 ? 2.7029 1.1538 2.0083 0.0556  0.0061  -0.1253 283 ASN A C   
1923  O O   . ASN A 253 ? 2.6851 1.1659 2.0447 0.0602  -0.0047 -0.1171 283 ASN A O   
1924  C CB  . ASN A 253 ? 2.6860 1.1419 2.0123 0.0701  0.0124  -0.0961 283 ASN A CB  
1925  C CG  . ASN A 253 ? 2.7440 1.1749 2.0524 0.0916  0.0264  -0.0872 283 ASN A CG  
1926  O OD1 . ASN A 253 ? 2.7624 1.1667 2.0552 0.1182  0.0389  -0.0935 283 ASN A OD1 
1927  N ND2 . ASN A 253 ? 2.7467 1.1885 2.0611 0.0813  0.0251  -0.0713 283 ASN A ND2 
1928  N N   . ILE A 254 ? 2.5901 1.0264 1.8405 0.0301  0.0102  -0.1421 284 ILE A N   
1929  C CA  . ILE A 254 ? 2.5666 1.0220 1.8172 0.0075  0.0025  -0.1518 284 ILE A CA  
1930  C C   . ILE A 254 ? 2.4795 0.9664 1.7414 -0.0204 -0.0040 -0.1481 284 ILE A C   
1931  O O   . ILE A 254 ? 2.5070 0.9749 1.7161 -0.0376 0.0033  -0.1594 284 ILE A O   
1932  C CB  . ILE A 254 ? 2.6910 1.1062 1.8701 0.0022  0.0134  -0.1757 284 ILE A CB  
1933  C CG1 . ILE A 254 ? 2.8419 1.2250 2.0115 0.0312  0.0203  -0.1796 284 ILE A CG1 
1934  C CG2 . ILE A 254 ? 2.6176 1.0542 1.7997 -0.0189 0.0059  -0.1834 284 ILE A CG2 
1935  C CD1 . ILE A 254 ? 2.9652 1.3078 2.0664 0.0282  0.0323  -0.2019 284 ILE A CD1 
1936  N N   . LEU A 255 ? 2.5024 1.0388 1.8343 -0.0253 -0.0166 -0.1326 285 LEU A N   
1937  C CA  . LEU A 255 ? 2.4558 1.0279 1.8093 -0.0498 -0.0230 -0.1282 285 LEU A CA  
1938  C C   . LEU A 255 ? 2.4553 1.0370 1.7870 -0.0720 -0.0237 -0.1455 285 LEU A C   
1939  O O   . LEU A 255 ? 2.4374 1.0331 1.7904 -0.0697 -0.0272 -0.1482 285 LEU A O   
1940  C CB  . LEU A 255 ? 2.3774 1.0011 1.8168 -0.0448 -0.0328 -0.1051 285 LEU A CB  
1941  C CG  . LEU A 255 ? 2.3770 0.9948 1.8396 -0.0226 -0.0315 -0.0855 285 LEU A CG  
1942  C CD1 . LEU A 255 ? 2.2976 0.9709 1.8456 -0.0202 -0.0393 -0.0609 285 LEU A CD1 
1943  C CD2 . LEU A 255 ? 2.4235 1.0069 1.8330 -0.0266 -0.0249 -0.0870 285 LEU A CD2 
1944  N N   . VAL A 256 ? 2.6366 1.2114 1.9263 -0.0937 -0.0201 -0.1566 286 VAL A N   
1945  C CA  . VAL A 256 ? 2.6183 1.2046 1.8867 -0.1153 -0.0196 -0.1724 286 VAL A CA  
1946  C C   . VAL A 256 ? 2.5236 1.1589 1.8393 -0.1340 -0.0278 -0.1655 286 VAL A C   
1947  O O   . VAL A 256 ? 2.5713 1.2143 1.9003 -0.1386 -0.0306 -0.1553 286 VAL A O   
1948  C CB  . VAL A 256 ? 2.7064 1.2520 1.8924 -0.1271 -0.0076 -0.1919 286 VAL A CB  
1949  C CG1 . VAL A 256 ? 2.7391 1.3000 1.9084 -0.1474 -0.0067 -0.2062 286 VAL A CG1 
1950  C CG2 . VAL A 256 ? 2.7951 1.2927 1.9374 -0.1066 0.0025  -0.1985 286 VAL A CG2 
1951  N N   . GLN A 257 ? 2.6889 1.3568 2.0308 -0.1441 -0.0314 -0.1705 287 GLN A N   
1952  C CA  . GLN A 257 ? 2.6374 1.3536 2.0251 -0.1610 -0.0372 -0.1669 287 GLN A CA  
1953  C C   . GLN A 257 ? 2.6727 1.3838 2.0149 -0.1822 -0.0339 -0.1841 287 GLN A C   
1954  O O   . GLN A 257 ? 2.6962 1.3732 1.9859 -0.1841 -0.0304 -0.1919 287 GLN A O   
1955  C CB  . GLN A 257 ? 2.6034 1.3407 2.0367 -0.1559 -0.0446 -0.1519 287 GLN A CB  
1956  C CG  . GLN A 257 ? 2.5133 1.2899 1.9851 -0.1719 -0.0498 -0.1456 287 GLN A CG  
1957  C CD  . GLN A 257 ? 2.4656 1.2584 1.9748 -0.1676 -0.0560 -0.1306 287 GLN A CD  
1958  O OE1 . GLN A 257 ? 2.5127 1.2848 2.0118 -0.1554 -0.0575 -0.1264 287 GLN A OE1 
1959  N NE2 . GLN A 257 ? 2.3551 1.1852 1.9075 -0.1781 -0.0595 -0.1231 287 GLN A NE2 
1960  N N   . PHE A 258 ? 2.7082 1.4450 2.0607 -0.1994 -0.0349 -0.1884 288 PHE A N   
1961  C CA  . PHE A 258 ? 2.7191 1.4538 2.0299 -0.2211 -0.0312 -0.2040 288 PHE A CA  
1962  C C   . PHE A 258 ? 2.6851 1.4339 2.0049 -0.2348 -0.0355 -0.2003 288 PHE A C   
1963  O O   . PHE A 258 ? 2.6495 1.4229 2.0205 -0.2304 -0.0426 -0.1864 288 PHE A O   
1964  C CB  . PHE A 258 ? 2.7394 1.4768 2.0316 -0.2374 -0.0303 -0.2095 288 PHE A CB  
1965  C CG  . PHE A 258 ? 2.8449 1.5303 2.0661 -0.2359 -0.0220 -0.2154 288 PHE A CG  
1966  C CD1 . PHE A 258 ? 2.9232 1.5714 2.1000 -0.2239 -0.0132 -0.2233 288 PHE A CD1 
1967  C CD2 . PHE A 258 ? 2.8315 1.5053 2.0299 -0.2471 -0.0224 -0.2136 288 PHE A CD2 
1968  C CE1 . PHE A 258 ? 2.9628 1.5643 2.0758 -0.2212 -0.0031 -0.2300 288 PHE A CE1 
1969  C CE2 . PHE A 258 ? 2.8871 1.5134 2.0187 -0.2460 -0.0128 -0.2204 288 PHE A CE2 
1970  C CZ  . PHE A 258 ? 2.9433 1.5340 2.0328 -0.2322 -0.0021 -0.2291 288 PHE A CZ  
1971  N N   . ASN A 259 ? 2.7600 1.4921 2.0281 -0.2518 -0.0297 -0.2130 289 ASN A N   
1972  C CA  . ASN A 259 ? 2.7706 1.5138 2.0393 -0.2678 -0.0312 -0.2128 289 ASN A CA  
1973  C C   . ASN A 259 ? 2.7855 1.5635 2.0741 -0.2864 -0.0322 -0.2200 289 ASN A C   
1974  O O   . ASN A 259 ? 2.7600 1.5694 2.0926 -0.2926 -0.0380 -0.2139 289 ASN A O   
1975  C CB  . ASN A 259 ? 2.8210 1.5223 2.0208 -0.2758 -0.0231 -0.2205 289 ASN A CB  
1976  C CG  . ASN A 259 ? 2.9216 1.6322 2.1166 -0.2944 -0.0222 -0.2219 289 ASN A CG  
1977  O OD1 . ASN A 259 ? 3.0055 1.7231 2.1812 -0.3129 -0.0164 -0.2327 289 ASN A OD1 
1978  N ND2 . ASN A 259 ? 2.9694 1.6801 2.1817 -0.2898 -0.0275 -0.2114 289 ASN A ND2 
1979  N N   . THR A 260 ? 2.7790 1.5524 2.0351 -0.2957 -0.0264 -0.2338 290 THR A N   
1980  C CA  . THR A 260 ? 2.7570 1.5622 2.0268 -0.3132 -0.0279 -0.2431 290 THR A CA  
1981  C C   . THR A 260 ? 2.6712 1.4988 1.9746 -0.3068 -0.0334 -0.2420 290 THR A C   
1982  O O   . THR A 260 ? 2.6818 1.4757 1.9429 -0.2999 -0.0279 -0.2445 290 THR A O   
1983  C CB  . THR A 260 ? 2.8808 1.6651 2.0858 -0.3307 -0.0169 -0.2597 290 THR A CB  
1984  O OG1 . THR A 260 ? 2.9694 1.7224 2.1296 -0.3225 -0.0095 -0.2662 290 THR A OG1 
1985  C CG2 . THR A 260 ? 2.9204 1.6812 2.0913 -0.3394 -0.0104 -0.2598 290 THR A CG2 
1986  N N   . PRO A 261 ? 2.6740 1.5405 2.0311 -0.3131 -0.0424 -0.2362 291 PRO A N   
1987  C CA  . PRO A 261 ? 2.6695 1.5168 2.0061 -0.3198 -0.0460 -0.2283 291 PRO A CA  
1988  C C   . PRO A 261 ? 2.7709 1.5935 2.0346 -0.3401 -0.0401 -0.2437 291 PRO A C   
1989  O O   . PRO A 261 ? 2.8249 1.6645 2.0756 -0.3553 -0.0370 -0.2587 291 PRO A O   
1990  C CB  . PRO A 261 ? 2.6049 1.4970 2.0104 -0.3264 -0.0569 -0.2176 291 PRO A CB  
1991  C CG  . PRO A 261 ? 2.5844 1.5147 2.0210 -0.3324 -0.0562 -0.2298 291 PRO A CG  
1992  C CD  . PRO A 261 ? 2.6481 1.5465 2.0441 -0.3243 -0.0474 -0.2337 291 PRO A CD  
1993  N N   . VAL A 262 ? 2.7197 1.5031 1.9363 -0.3401 -0.0379 -0.2401 292 VAL A N   
1994  C CA  . VAL A 262 ? 2.7896 1.5496 1.9346 -0.3601 -0.0313 -0.2543 292 VAL A CA  
1995  C C   . VAL A 262 ? 2.7746 1.5502 1.9279 -0.3809 -0.0429 -0.2484 292 VAL A C   
1996  O O   . VAL A 262 ? 2.7627 1.5250 1.9292 -0.3753 -0.0505 -0.2312 292 VAL A O   
1997  C CB  . VAL A 262 ? 2.8628 1.5685 1.9448 -0.3479 -0.0199 -0.2566 292 VAL A CB  
1998  C CG1 . VAL A 262 ? 2.9347 1.6212 1.9433 -0.3696 -0.0114 -0.2724 292 VAL A CG1 
1999  C CG2 . VAL A 262 ? 2.8818 1.5728 1.9575 -0.3285 -0.0106 -0.2612 292 VAL A CG2 
2000  N N   . GLN A 263 ? 2.8176 1.6230 1.9659 -0.4051 -0.0453 -0.2611 293 GLN A N   
2001  C CA  . GLN A 263 ? 2.8374 1.6648 1.9959 -0.4286 -0.0589 -0.2564 293 GLN A CA  
2002  C C   . GLN A 263 ? 2.9569 1.7465 2.0481 -0.4397 -0.0578 -0.2567 293 GLN A C   
2003  O O   . GLN A 263 ? 3.0198 1.7884 2.0431 -0.4473 -0.0447 -0.2741 293 GLN A O   
2004  C CB  . GLN A 263 ? 2.8212 1.6890 1.9828 -0.4515 -0.0603 -0.2732 293 GLN A CB  
2005  C CG  . GLN A 263 ? 2.8164 1.7237 2.0129 -0.4748 -0.0782 -0.2673 293 GLN A CG  
2006  C CD  . GLN A 263 ? 2.7801 1.7260 2.0674 -0.4648 -0.0888 -0.2534 293 GLN A CD  
2007  O OE1 . GLN A 263 ? 2.7054 1.6459 2.0310 -0.4396 -0.0849 -0.2432 293 GLN A OE1 
2008  N NE2 . GLN A 263 ? 2.9005 1.8896 2.2248 -0.4847 -0.1021 -0.2532 293 GLN A NE2 
2009  N N   . ILE A 264 ? 2.9305 1.7130 2.0414 -0.4410 -0.0711 -0.2365 294 ILE A N   
2010  C CA  . ILE A 264 ? 2.9549 1.7027 2.0059 -0.4529 -0.0724 -0.2345 294 ILE A CA  
2011  C C   . ILE A 264 ? 2.9189 1.7325 2.0148 -0.4702 -0.0925 -0.2152 294 ILE A C   
2012  O O   . ILE A 264 ? 2.8560 1.6997 2.0266 -0.4674 -0.1074 -0.1950 294 ILE A O   
2013  C CB  . ILE A 264 ? 2.9141 1.6166 1.9646 -0.4242 -0.0676 -0.2166 294 ILE A CB  
2014  C CG1 . ILE A 264 ? 2.9140 1.6678 1.9551 -0.4084 -0.0610 -0.1977 294 ILE A CG1 
2015  C CG2 . ILE A 264 ? 2.8528 1.5797 1.9920 -0.4076 -0.0818 -0.1852 294 ILE A CG2 
2016  C CD1 . ILE A 264 ? 2.8311 1.5741 1.8893 -0.3705 -0.0522 -0.1753 294 ILE A CD1 
2017  N N   . ASN A 265 ? 2.9460 1.8053 2.0118 -0.4797 -0.0910 -0.2157 295 ASN A N   
2018  C CA  . ASN A 265 ? 2.8906 1.8398 2.0092 -0.4872 -0.1088 -0.1919 295 ASN A CA  
2019  C C   . ASN A 265 ? 2.9207 1.9158 2.0396 -0.4654 -0.1052 -0.1636 295 ASN A C   
2020  O O   . ASN A 265 ? 3.0006 1.9784 2.0506 -0.4681 -0.0900 -0.1783 295 ASN A O   
2021  C CB  . ASN A 265 ? 2.9430 1.9057 2.0199 -0.5246 -0.1120 -0.2216 295 ASN A CB  
2022  C CG  . ASN A 265 ? 2.8662 1.7891 1.9465 -0.5490 -0.1158 -0.2502 295 ASN A CG  
2023  O OD1 . ASN A 265 ? 2.8520 1.7314 1.9358 -0.5299 -0.1030 -0.2568 295 ASN A OD1 
2024  N ND2 . ASN A 265 ? 2.9635 1.9301 2.0619 -0.5768 -0.1290 -0.2601 295 ASN A ND2 
2025  N N   . CYS A 266 ? 2.7098 1.7627 1.9041 -0.4459 -0.1183 -0.1241 296 CYS A N   
2026  C CA  . CYS A 266 ? 2.7162 1.8167 1.9186 -0.4256 -0.1163 -0.0942 296 CYS A CA  
2027  C C   . CYS A 266 ? 2.6791 1.8666 1.9356 -0.4325 -0.1375 -0.0661 296 CYS A C   
2028  O O   . CYS A 266 ? 2.6743 1.8900 1.9994 -0.4338 -0.1545 -0.0511 296 CYS A O   
2029  C CB  . CYS A 266 ? 2.7373 1.8189 1.9741 -0.3900 -0.1089 -0.0707 296 CYS A CB  
2030  S SG  . CYS A 266 ? 3.1758 2.1536 2.3540 -0.3775 -0.0860 -0.1007 296 CYS A SG  
2031  N N   . THR A 267 ? 2.5298 1.7581 1.7552 -0.4363 -0.1361 -0.0580 297 THR A N   
2032  C CA  . THR A 267 ? 2.5264 1.8360 1.7938 -0.4430 -0.1567 -0.0310 297 THR A CA  
2033  C C   . THR A 267 ? 2.4766 1.8214 1.7372 -0.4250 -0.1515 -0.0032 297 THR A C   
2034  O O   . THR A 267 ? 2.5273 1.8361 1.7370 -0.4140 -0.1305 -0.0118 297 THR A O   
2035  C CB  . THR A 267 ? 2.6187 1.9518 1.8518 -0.4777 -0.1659 -0.0536 297 THR A CB  
2036  O OG1 . THR A 267 ? 2.6987 1.9863 1.8408 -0.4913 -0.1458 -0.0866 297 THR A OG1 
2037  C CG2 . THR A 267 ? 2.6589 1.9828 1.9281 -0.4947 -0.1781 -0.0702 297 THR A CG2 
2038  N N   . ARG A 268 ? 2.2372 1.6525 1.5497 -0.4230 -0.1712 0.0299  298 ARG A N   
2039  C CA  . ARG A 268 ? 2.2457 1.7041 1.5570 -0.4100 -0.1704 0.0595  298 ARG A CA  
2040  C C   . ARG A 268 ? 2.3103 1.8287 1.6109 -0.4341 -0.1884 0.0654  298 ARG A C   
2041  O O   . ARG A 268 ? 2.4188 1.9944 1.7793 -0.4331 -0.2112 0.0937  298 ARG A O   
2042  C CB  . ARG A 268 ? 2.1963 1.6809 1.5837 -0.3821 -0.1777 0.0982  298 ARG A CB  
2043  C CG  . ARG A 268 ? 2.2035 1.7049 1.5786 -0.3626 -0.1662 0.1215  298 ARG A CG  
2044  C CD  . ARG A 268 ? 2.2126 1.7814 1.5889 -0.3720 -0.1810 0.1465  298 ARG A CD  
2045  N NE  . ARG A 268 ? 2.2421 1.8623 1.6958 -0.3684 -0.2064 0.1774  298 ARG A NE  
2046  C CZ  . ARG A 268 ? 2.2094 1.8538 1.7183 -0.3454 -0.2102 0.2120  298 ARG A CZ  
2047  N NH1 . ARG A 268 ? 2.1248 1.7490 1.6217 -0.3240 -0.1905 0.2199  298 ARG A NH1 
2048  N NH2 . ARG A 268 ? 2.2547 1.9433 1.8315 -0.3438 -0.2331 0.2383  298 ARG A NH2 
2049  N N   . PRO A 269 ? 2.3194 1.8270 1.5440 -0.4557 -0.1790 0.0401  299 PRO A N   
2050  C CA  . PRO A 269 ? 2.3391 1.9021 1.5491 -0.4816 -0.1971 0.0429  299 PRO A CA  
2051  C C   . PRO A 269 ? 2.3523 1.9735 1.5752 -0.4739 -0.2069 0.0801  299 PRO A C   
2052  O O   . PRO A 269 ? 2.4129 2.0464 1.5762 -0.4880 -0.2010 0.0760  299 PRO A O   
2053  C CB  . PRO A 269 ? 2.4077 1.9314 1.5251 -0.5050 -0.1787 0.0037  299 PRO A CB  
2054  C CG  . PRO A 269 ? 2.4317 1.8946 1.5115 -0.4847 -0.1496 -0.0062 299 PRO A CG  
2055  C CD  . PRO A 269 ? 2.3742 1.8161 1.5213 -0.4579 -0.1511 0.0072  299 PRO A CD  
2056  N N   . ASN A 270 ? 2.3021 1.9580 1.5995 -0.4532 -0.2213 0.1163  300 ASN A N   
2057  C CA  . ASN A 270 ? 2.3357 2.0460 1.6472 -0.4462 -0.2319 0.1533  300 ASN A CA  
2058  C C   . ASN A 270 ? 2.3863 2.1443 1.7866 -0.4351 -0.2581 0.1871  300 ASN A C   
2059  O O   . ASN A 270 ? 2.3860 2.1303 1.8388 -0.4114 -0.2544 0.2020  300 ASN A O   
2060  C CB  . ASN A 270 ? 2.2956 1.9817 1.5860 -0.4232 -0.2081 0.1639  300 ASN A CB  
2061  C CG  . ASN A 270 ? 2.3211 1.9814 1.5216 -0.4362 -0.1857 0.1410  300 ASN A CG  
2062  O OD1 . ASN A 270 ? 2.3921 2.0774 1.5484 -0.4614 -0.1929 0.1342  300 ASN A OD1 
2063  N ND2 . ASN A 270 ? 2.3141 1.9237 1.4878 -0.4188 -0.1581 0.1288  300 ASN A ND2 
2064  N N   . ASN A 271 ? 2.3143 2.1275 1.7318 -0.4523 -0.2844 0.1989  301 ASN A N   
2065  C CA  . ASN A 271 ? 2.3449 2.2062 1.8458 -0.4423 -0.3103 0.2320  301 ASN A CA  
2066  C C   . ASN A 271 ? 2.3975 2.2854 1.9175 -0.4214 -0.3112 0.2722  301 ASN A C   
2067  O O   . ASN A 271 ? 2.4512 2.3839 1.9573 -0.4295 -0.3256 0.2931  301 ASN A O   
2068  C CB  . ASN A 271 ? 2.3404 2.2545 1.8532 -0.4661 -0.3392 0.2332  301 ASN A CB  
2069  C CG  . ASN A 271 ? 2.2802 2.2355 1.8851 -0.4567 -0.3651 0.2596  301 ASN A CG  
2070  O OD1 . ASN A 271 ? 2.2669 2.2061 1.9250 -0.4350 -0.3601 0.2727  301 ASN A OD1 
2071  N ND2 . ASN A 271 ? 2.4152 2.4241 2.0393 -0.4731 -0.3930 0.2676  301 ASN A ND2 
2072  N N   . ASN A 272 ? 2.3503 2.2102 1.8993 -0.3957 -0.2958 0.2828  302 ASN A N   
2073  C CA  . ASN A 272 ? 2.3348 2.2158 1.8986 -0.3761 -0.2932 0.3181  302 ASN A CA  
2074  C C   . ASN A 272 ? 2.3271 2.2613 1.9641 -0.3690 -0.3208 0.3559  302 ASN A C   
2075  O O   . ASN A 272 ? 2.3012 2.2477 1.9911 -0.3724 -0.3378 0.3550  302 ASN A O   
2076  C CB  . ASN A 272 ? 2.2847 2.1201 1.8578 -0.3509 -0.2677 0.3165  302 ASN A CB  
2077  C CG  . ASN A 272 ? 2.2771 2.0610 1.7759 -0.3539 -0.2391 0.2839  302 ASN A CG  
2078  O OD1 . ASN A 272 ? 2.3212 2.0952 1.7623 -0.3763 -0.2366 0.2571  302 ASN A OD1 
2079  N ND2 . ASN A 272 ? 2.1770 1.9277 1.6777 -0.3312 -0.2171 0.2856  302 ASN A ND2 
2080  N N   . THR A 273 ? 2.1527 2.1170 1.7916 -0.3593 -0.3242 0.3889  303 THR A N   
2081  C CA  . THR A 273 ? 2.1409 2.1536 1.8429 -0.3504 -0.3485 0.4286  303 THR A CA  
2082  C C   . THR A 273 ? 2.1154 2.1183 1.8467 -0.3238 -0.3341 0.4533  303 THR A C   
2083  O O   . THR A 273 ? 2.1225 2.1054 1.8091 -0.3174 -0.3120 0.4507  303 THR A O   
2084  C CB  . THR A 273 ? 2.2052 2.2665 1.8797 -0.3660 -0.3693 0.4480  303 THR A CB  
2085  O OG1 . THR A 273 ? 2.3433 2.4124 1.9849 -0.3920 -0.3806 0.4220  303 THR A OG1 
2086  C CG2 . THR A 273 ? 2.1692 2.2780 1.9125 -0.3566 -0.3969 0.4880  303 THR A CG2 
2087  N N   . ARG A 274 ? 2.1581 2.1749 1.9646 -0.3088 -0.3455 0.4761  304 ARG A N   
2088  C CA  . ARG A 274 ? 2.1266 2.1361 1.9680 -0.2840 -0.3331 0.5003  304 ARG A CA  
2089  C C   . ARG A 274 ? 2.1256 2.1811 1.9848 -0.2786 -0.3485 0.5420  304 ARG A C   
2090  O O   . ARG A 274 ? 2.1032 2.1933 2.0152 -0.2782 -0.3730 0.5650  304 ARG A O   
2091  C CB  . ARG A 274 ? 2.0811 2.0736 1.9917 -0.2718 -0.3337 0.4997  304 ARG A CB  
2092  C CG  . ARG A 274 ? 2.0405 2.0295 1.9944 -0.2477 -0.3237 0.5261  304 ARG A CG  
2093  C CD  . ARG A 274 ? 1.9936 1.9698 2.0151 -0.2403 -0.3277 0.5255  304 ARG A CD  
2094  N NE  . ARG A 274 ? 1.9480 1.8741 1.9652 -0.2278 -0.3027 0.5074  304 ARG A NE  
2095  C CZ  . ARG A 274 ? 1.8924 1.7954 1.9603 -0.2200 -0.2997 0.5042  304 ARG A CZ  
2096  N NH1 . ARG A 274 ? 1.8838 1.8092 2.0120 -0.2235 -0.3186 0.5171  304 ARG A NH1 
2097  N NH2 . ARG A 274 ? 1.8386 1.6955 1.8966 -0.2090 -0.2780 0.4879  304 ARG A NH2 
2098  N N   . LYS A 275 ? 2.0474 2.1020 1.8606 -0.2753 -0.3339 0.5506  305 LYS A N   
2099  C CA  . LYS A 275 ? 2.0490 2.1389 1.8714 -0.2692 -0.3434 0.5893  305 LYS A CA  
2100  C C   . LYS A 275 ? 2.0090 2.0883 1.8815 -0.2441 -0.3301 0.6087  305 LYS A C   
2101  O O   . LYS A 275 ? 1.9946 2.0391 1.8524 -0.2328 -0.3033 0.5937  305 LYS A O   
2102  C CB  . LYS A 275 ? 2.1023 2.1940 1.8483 -0.2803 -0.3321 0.5865  305 LYS A CB  
2103  C CG  . LYS A 275 ? 2.1455 2.2663 1.8532 -0.3055 -0.3549 0.5845  305 LYS A CG  
2104  C CD  . LYS A 275 ? 2.2071 2.3378 1.8460 -0.3177 -0.3486 0.5916  305 LYS A CD  
2105  C CE  . LYS A 275 ? 2.2476 2.4097 1.8532 -0.3436 -0.3747 0.5917  305 LYS A CE  
2106  N NZ  . LYS A 275 ? 2.3155 2.4791 1.8414 -0.3609 -0.3653 0.5895  305 LYS A NZ  
2107  N N   . SER A 276 ? 2.1054 2.2145 2.0370 -0.2356 -0.3488 0.6419  306 SER A N   
2108  C CA  . SER A 276 ? 2.0644 2.1672 2.0481 -0.2133 -0.3384 0.6631  306 SER A CA  
2109  C C   . SER A 276 ? 2.0765 2.2037 2.0483 -0.2075 -0.3379 0.6967  306 SER A C   
2110  O O   . SER A 276 ? 2.0606 2.2181 2.0714 -0.2036 -0.3569 0.7294  306 SER A O   
2111  C CB  . SER A 276 ? 2.0229 2.1368 2.0832 -0.2078 -0.3565 0.6751  306 SER A CB  
2112  O OG  . SER A 276 ? 2.0204 2.1759 2.0977 -0.2174 -0.3868 0.6967  306 SER A OG  
2113  N N   . ILE A 277 ? 2.1495 2.2620 2.0659 -0.2074 -0.3152 0.6879  307 ILE A N   
2114  C CA  . ILE A 277 ? 2.1644 2.2960 2.0653 -0.2031 -0.3111 0.7169  307 ILE A CA  
2115  C C   . ILE A 277 ? 2.1141 2.2419 2.0714 -0.1810 -0.3005 0.7378  307 ILE A C   
2116  O O   . ILE A 277 ? 2.0648 2.1645 2.0500 -0.1681 -0.2840 0.7218  307 ILE A O   
2117  C CB  . ILE A 277 ? 2.2003 2.3162 2.0276 -0.2101 -0.2873 0.6991  307 ILE A CB  
2118  C CG1 . ILE A 277 ? 2.1590 2.2338 1.9831 -0.1972 -0.2568 0.6697  307 ILE A CG1 
2119  C CG2 . ILE A 277 ? 2.2493 2.3717 2.0171 -0.2344 -0.2983 0.6818  307 ILE A CG2 
2120  C CD1 . ILE A 277 ? 2.1715 2.2295 1.9282 -0.2019 -0.2309 0.6514  307 ILE A CD1 
2121  N N   . ARG A 278 ? 2.0416 2.1970 2.0142 -0.1774 -0.3103 0.7740  308 ARG A N   
2122  C CA  . ARG A 278 ? 1.9930 2.1506 2.0220 -0.1586 -0.3044 0.7987  308 ARG A CA  
2123  C C   . ARG A 278 ? 1.9868 2.1381 1.9894 -0.1503 -0.2783 0.8054  308 ARG A C   
2124  O O   . ARG A 278 ? 2.0312 2.2015 1.9996 -0.1575 -0.2814 0.8247  308 ARG A O   
2125  C CB  . ARG A 278 ? 1.9848 2.1763 2.0502 -0.1601 -0.3333 0.8351  308 ARG A CB  
2126  C CG  . ARG A 278 ? 1.9420 2.1447 2.0362 -0.1688 -0.3603 0.8290  308 ARG A CG  
2127  C CD  . ARG A 278 ? 1.9272 2.1653 2.0513 -0.1706 -0.3902 0.8652  308 ARG A CD  
2128  N NE  . ARG A 278 ? 1.8599 2.1024 2.0407 -0.1539 -0.3881 0.8944  308 ARG A NE  
2129  C CZ  . ARG A 278 ? 1.8323 2.1015 2.0468 -0.1519 -0.4116 0.9281  308 ARG A CZ  
2130  N NH1 . ARG A 278 ? 1.8627 2.1577 2.0609 -0.1648 -0.4402 0.9369  308 ARG A NH1 
2131  N NH2 . ARG A 278 ? 1.7723 2.0414 2.0365 -0.1368 -0.3969 0.9304  308 ARG A NH2 
2132  N N   . ILE A 279 ? 1.8941 2.0185 1.9118 -0.1359 -0.2529 0.7888  309 ILE A N   
2133  C CA  . ILE A 279 ? 1.8877 2.0077 1.8939 -0.1252 -0.2272 0.7951  309 ILE A CA  
2134  C C   . ILE A 279 ? 1.8349 1.9625 1.9062 -0.1094 -0.2276 0.8222  309 ILE A C   
2135  O O   . ILE A 279 ? 1.8008 1.9093 1.9016 -0.0945 -0.2087 0.8136  309 ILE A O   
2136  C CB  . ILE A 279 ? 1.8971 1.9844 1.8772 -0.1187 -0.1984 0.7603  309 ILE A CB  
2137  C CG1 . ILE A 279 ? 1.9384 2.0119 1.8650 -0.1344 -0.2009 0.7295  309 ILE A CG1 
2138  C CG2 . ILE A 279 ? 1.9218 2.0111 1.8757 -0.1127 -0.1732 0.7652  309 ILE A CG2 
2139  C CD1 . ILE A 279 ? 1.9515 1.9898 1.8505 -0.1279 -0.1733 0.6943  309 ILE A CD1 
2140  N N   . GLY A 280 ? 2.2123 2.3669 2.3061 -0.1126 -0.2493 0.8550  312 GLY A N   
2141  C CA  . GLY A 280 ? 2.1704 2.3318 2.3264 -0.0990 -0.2508 0.8814  312 GLY A CA  
2142  C C   . GLY A 280 ? 2.1613 2.3225 2.3169 -0.0881 -0.2265 0.8940  312 GLY A C   
2143  O O   . GLY A 280 ? 2.1864 2.3426 2.2935 -0.0907 -0.2076 0.8814  312 GLY A O   
2144  N N   . PRO A 281 ? 2.1047 2.2720 2.3147 -0.0761 -0.2226 0.9042  313 PRO A N   
2145  C CA  . PRO A 281 ? 2.0520 2.2260 2.3205 -0.0731 -0.2359 0.8923  313 PRO A CA  
2146  C C   . PRO A 281 ? 2.0290 2.1792 2.3364 -0.0657 -0.2285 0.8671  313 PRO A C   
2147  O O   . PRO A 281 ? 2.0171 2.1506 2.3359 -0.0547 -0.2062 0.8548  313 PRO A O   
2148  C CB  . PRO A 281 ? 2.0532 2.2432 2.3521 -0.0650 -0.2251 0.8953  313 PRO A CB  
2149  C CG  . PRO A 281 ? 2.0395 2.2204 2.3170 -0.0576 -0.1992 0.8970  313 PRO A CG  
2150  C CD  . PRO A 281 ? 2.0948 2.2669 2.3091 -0.0666 -0.1995 0.9084  313 PRO A CD  
2151  N N   . GLY A 282 ? 1.9942 2.1427 2.3214 -0.0726 -0.2478 0.8593  314 GLY A N   
2152  C CA  . GLY A 282 ? 1.9590 2.0834 2.3212 -0.0682 -0.2419 0.8346  314 GLY A CA  
2153  C C   . GLY A 282 ? 1.9813 2.0778 2.3093 -0.0751 -0.2473 0.8293  314 GLY A C   
2154  O O   . GLY A 282 ? 1.9610 2.0502 2.3021 -0.0834 -0.2637 0.8208  314 GLY A O   
2155  N N   . GLN A 283 ? 2.0152 2.0969 2.2979 -0.0724 -0.2295 0.8223  315 GLN A N   
2156  C CA  . GLN A 283 ? 2.0443 2.1001 2.2856 -0.0780 -0.2220 0.7848  315 GLN A CA  
2157  C C   . GLN A 283 ? 2.0776 2.1469 2.2770 -0.0960 -0.2409 0.7769  315 GLN A C   
2158  O O   . GLN A 283 ? 2.0916 2.1909 2.2771 -0.1033 -0.2550 0.7999  315 GLN A O   
2159  C CB  . GLN A 283 ? 2.0765 2.1187 2.2781 -0.0701 -0.1949 0.7711  315 GLN A CB  
2160  C CG  . GLN A 283 ? 2.0513 2.0725 2.2885 -0.0527 -0.1747 0.7674  315 GLN A CG  
2161  C CD  . GLN A 283 ? 2.0205 2.0637 2.2983 -0.0433 -0.1717 0.8018  315 GLN A CD  
2162  O OE1 . GLN A 283 ? 2.0212 2.0934 2.2956 -0.0491 -0.1833 0.8283  315 GLN A OE1 
2163  N NE2 . GLN A 283 ? 1.9953 2.0237 2.3099 -0.0292 -0.1563 0.8009  315 GLN A NE2 
2164  N N   . ALA A 284 ? 2.0796 2.1255 2.2578 -0.1038 -0.2414 0.7442  316 ALA A N   
2165  C CA  . ALA A 284 ? 2.1093 2.1652 2.2459 -0.1222 -0.2577 0.7318  316 ALA A CA  
2166  C C   . ALA A 284 ? 2.1444 2.1656 2.2361 -0.1276 -0.2440 0.6911  316 ALA A C   
2167  O O   . ALA A 284 ? 2.1196 2.1102 2.2337 -0.1223 -0.2371 0.6712  316 ALA A O   
2168  C CB  . ALA A 284 ? 2.0657 2.1387 2.2449 -0.1304 -0.2854 0.7410  316 ALA A CB  
2169  N N   . PHE A 285 ? 1.8945 1.9189 1.9217 -0.1389 -0.2397 0.6791  317 PHE A N   
2170  C CA  . PHE A 285 ? 1.9390 1.9307 1.9151 -0.1452 -0.2253 0.6409  317 PHE A CA  
2171  C C   . PHE A 285 ? 1.9563 1.9517 1.9096 -0.1657 -0.2446 0.6241  317 PHE A C   
2172  O O   . PHE A 285 ? 1.9639 1.9932 1.9079 -0.1786 -0.2650 0.6408  317 PHE A O   
2173  C CB  . PHE A 285 ? 1.9910 1.9806 1.9076 -0.1459 -0.2049 0.6349  317 PHE A CB  
2174  C CG  . PHE A 285 ? 2.0445 2.0025 1.9032 -0.1546 -0.1912 0.5967  317 PHE A CG  
2175  C CD1 . PHE A 285 ? 2.0484 1.9648 1.9108 -0.1431 -0.1730 0.5703  317 PHE A CD1 
2176  C CD2 . PHE A 285 ? 2.0929 2.0613 1.8922 -0.1748 -0.1966 0.5875  317 PHE A CD2 
2177  C CE1 . PHE A 285 ? 2.1014 1.9858 1.9094 -0.1507 -0.1600 0.5352  317 PHE A CE1 
2178  C CE2 . PHE A 285 ? 2.1452 2.0829 1.8897 -0.1835 -0.1826 0.5521  317 PHE A CE2 
2179  C CZ  . PHE A 285 ? 2.1502 2.0452 1.8991 -0.1710 -0.1640 0.5258  317 PHE A CZ  
2180  N N   . TYR A 286 ? 2.1568 2.1171 2.1008 -0.1690 -0.2386 0.5910  318 TYR A N   
2181  C CA  . TYR A 286 ? 2.1716 2.1311 2.0925 -0.1893 -0.2540 0.5700  318 TYR A CA  
2182  C C   . TYR A 286 ? 2.2477 2.1876 2.0906 -0.2011 -0.2392 0.5411  318 TYR A C   
2183  O O   . TYR A 286 ? 2.2702 2.1680 2.0900 -0.1971 -0.2201 0.5117  318 TYR A O   
2184  C CB  . TYR A 286 ? 2.1193 2.0517 2.0806 -0.1880 -0.2575 0.5522  318 TYR A CB  
2185  C CG  . TYR A 286 ? 2.0398 1.9923 2.0777 -0.1785 -0.2717 0.5804  318 TYR A CG  
2186  C CD1 . TYR A 286 ? 2.0101 2.0029 2.0772 -0.1878 -0.2981 0.6014  318 TYR A CD1 
2187  C CD2 . TYR A 286 ? 1.9946 1.9261 2.0757 -0.1603 -0.2586 0.5867  318 TYR A CD2 
2188  C CE1 . TYR A 286 ? 1.9369 1.9470 2.0742 -0.1790 -0.3099 0.6272  318 TYR A CE1 
2189  C CE2 . TYR A 286 ? 1.9221 1.8709 2.0717 -0.1529 -0.2700 0.6125  318 TYR A CE2 
2190  C CZ  . TYR A 286 ? 1.8932 1.8805 2.0707 -0.1621 -0.2950 0.6325  318 TYR A CZ  
2191  O OH  . TYR A 286 ? 1.8197 1.8224 2.0656 -0.1544 -0.3050 0.6578  318 TYR A OH  
2192  N N   . ALA A 287 ? 2.0855 2.0545 1.8865 -0.2158 -0.2480 0.5502  319 ALA A N   
2193  C CA  . ALA A 287 ? 2.1577 2.1130 1.8819 -0.2302 -0.2350 0.5258  319 ALA A CA  
2194  C C   . ALA A 287 ? 2.1787 2.1267 1.8771 -0.2514 -0.2473 0.4989  319 ALA A C   
2195  O O   . ALA A 287 ? 2.1329 2.0922 1.8735 -0.2560 -0.2679 0.5012  319 ALA A O   
2196  C CB  . ALA A 287 ? 2.1872 2.1765 1.8758 -0.2390 -0.2388 0.5482  319 ALA A CB  
2197  N N   . THR A 288 ? 2.2448 2.1737 1.8723 -0.2653 -0.2334 0.4724  320 THR A N   
2198  C CA  . THR A 288 ? 2.2765 2.1986 1.8690 -0.2880 -0.2428 0.4453  320 THR A CA  
2199  C C   . THR A 288 ? 2.3140 2.2753 1.8657 -0.3103 -0.2593 0.4564  320 THR A C   
2200  O O   . THR A 288 ? 2.3619 2.3239 1.8596 -0.3161 -0.2457 0.4569  320 THR A O   
2201  C CB  . THR A 288 ? 2.3320 2.2024 1.8694 -0.2910 -0.2165 0.4051  320 THR A CB  
2202  O OG1 . THR A 288 ? 2.3053 2.1385 1.8737 -0.2675 -0.1983 0.3985  320 THR A OG1 
2203  C CG2 . THR A 288 ? 2.3474 2.2055 1.8636 -0.3122 -0.2267 0.3759  320 THR A CG2 
2204  N N   . GLY A 289 ? 2.3948 2.3884 1.9730 -0.3232 -0.2886 0.4651  321 GLY A N   
2205  C CA  . GLY A 289 ? 2.4283 2.4614 1.9735 -0.3450 -0.3091 0.4766  321 GLY A CA  
2206  C C   . GLY A 289 ? 2.4968 2.5110 1.9699 -0.3690 -0.3007 0.4408  321 GLY A C   
2207  O O   . GLY A 289 ? 2.5299 2.4986 1.9684 -0.3670 -0.2745 0.4101  321 GLY A O   
2208  N N   . ASP A 290 A 2.4814 2.5307 1.9309 -0.3922 -0.3237 0.4452  321 ASP A N   
2209  C CA  . ASP A 290 A 2.6121 2.6480 1.9929 -0.4182 -0.3181 0.4120  321 ASP A CA  
2210  C C   . ASP A 290 A 2.5183 2.5299 1.9177 -0.4226 -0.3189 0.3802  321 ASP A C   
2211  O O   . ASP A 290 A 2.4129 2.4327 1.8818 -0.4112 -0.3332 0.3884  321 ASP A O   
2212  C CB  . ASP A 290 A 2.7174 2.8007 2.0703 -0.4422 -0.3444 0.4278  321 ASP A CB  
2213  C CG  . ASP A 290 A 2.6679 2.7969 2.0898 -0.4407 -0.3811 0.4526  321 ASP A CG  
2214  O OD1 . ASP A 290 A 2.5530 2.6887 2.0424 -0.4177 -0.3867 0.4758  321 ASP A OD1 
2215  O OD2 . ASP A 290 A 2.7255 2.8863 2.1324 -0.4632 -0.4049 0.4504  321 ASP A OD2 
2216  N N   . ILE A 291 ? 2.4442 2.4238 1.7789 -0.4404 -0.3023 0.3430  322 ILE A N   
2217  C CA  . ILE A 291 ? 2.4400 2.3887 1.7758 -0.4483 -0.2987 0.3075  322 ILE A CA  
2218  C C   . ILE A 291 ? 2.4503 2.4332 1.7748 -0.4767 -0.3239 0.2981  322 ILE A C   
2219  O O   . ILE A 291 ? 2.5149 2.5150 1.7801 -0.4987 -0.3268 0.2948  322 ILE A O   
2220  C CB  . ILE A 291 ? 2.5048 2.3933 1.7750 -0.4503 -0.2641 0.2708  322 ILE A CB  
2221  C CG1 . ILE A 291 ? 2.4892 2.3461 1.7736 -0.4211 -0.2398 0.2797  322 ILE A CG1 
2222  C CG2 . ILE A 291 ? 2.4962 2.3492 1.7652 -0.4593 -0.2607 0.2341  322 ILE A CG2 
2223  C CD1 . ILE A 291 ? 2.5337 2.3298 1.7590 -0.4194 -0.2059 0.2447  322 ILE A CD1 
2224  N N   . ILE A 292 ? 2.4760 2.4687 1.8571 -0.4772 -0.3415 0.2929  323 ILE A N   
2225  C CA  . ILE A 292 ? 2.4596 2.4872 1.8415 -0.5026 -0.3665 0.2827  323 ILE A CA  
2226  C C   . ILE A 292 ? 2.5178 2.5046 1.8435 -0.5236 -0.3498 0.2354  323 ILE A C   
2227  O O   . ILE A 292 ? 2.4995 2.4471 1.8446 -0.5178 -0.3384 0.2122  323 ILE A O   
2228  C CB  . ILE A 292 ? 2.3206 2.3799 1.7933 -0.4939 -0.3929 0.2988  323 ILE A CB  
2229  C CG1 . ILE A 292 ? 2.2206 2.3143 1.7492 -0.4713 -0.4072 0.3455  323 ILE A CG1 
2230  C CG2 . ILE A 292 ? 2.3162 2.4171 1.7930 -0.5198 -0.4200 0.2890  323 ILE A CG2 
2231  C CD1 . ILE A 292 ? 2.1592 2.2315 1.7573 -0.4447 -0.4002 0.3549  323 ILE A CD1 
2232  N N   . GLY A 293 ? 2.7493 2.7439 2.0023 -0.5493 -0.3480 0.2212  324 GLY A N   
2233  C CA  . GLY A 293 ? 2.8004 2.7606 1.9920 -0.5732 -0.3331 0.1770  324 GLY A CA  
2234  C C   . GLY A 293 ? 2.9029 2.8210 2.0071 -0.5787 -0.3013 0.1596  324 GLY A C   
2235  O O   . GLY A 293 ? 3.0289 2.9641 2.1044 -0.5776 -0.2986 0.1809  324 GLY A O   
2236  N N   . ASP A 294 ? 2.8279 2.6891 1.8899 -0.5850 -0.2770 0.1202  325 ASP A N   
2237  C CA  . ASP A 294 ? 2.9289 2.7423 1.9062 -0.5916 -0.2444 0.0964  325 ASP A CA  
2238  C C   . ASP A 294 ? 2.8864 2.6517 1.8736 -0.5601 -0.2182 0.0996  325 ASP A C   
2239  O O   . ASP A 294 ? 2.7873 2.5365 1.8350 -0.5382 -0.2199 0.1044  325 ASP A O   
2240  C CB  . ASP A 294 ? 2.9728 2.7506 1.8950 -0.6175 -0.2334 0.0509  325 ASP A CB  
2241  C CG  . ASP A 294 ? 3.0253 2.8536 1.9358 -0.6501 -0.2590 0.0464  325 ASP A CG  
2242  O OD1 . ASP A 294 ? 3.0899 2.9666 1.9889 -0.6598 -0.2742 0.0706  325 ASP A OD1 
2243  O OD2 . ASP A 294 ? 3.0140 2.8339 1.9269 -0.6665 -0.2644 0.0187  325 ASP A OD2 
2244  N N   . ILE A 295 ? 2.8480 2.5906 1.7751 -0.5589 -0.1934 0.0963  326 ILE A N   
2245  C CA  . ILE A 295 ? 2.8351 2.5319 1.7647 -0.5301 -0.1663 0.0966  326 ILE A CA  
2246  C C   . ILE A 295 ? 2.8472 2.4743 1.7370 -0.5312 -0.1416 0.0548  326 ILE A C   
2247  O O   . ILE A 295 ? 2.9174 2.5119 1.7299 -0.5468 -0.1195 0.0281  326 ILE A O   
2248  C CB  . ILE A 295 ? 2.8879 2.5894 1.7726 -0.5280 -0.1488 0.1095  326 ILE A CB  
2249  C CG1 . ILE A 295 ? 2.8716 2.6386 1.7897 -0.5279 -0.1729 0.1517  326 ILE A CG1 
2250  C CG2 . ILE A 295 ? 2.8723 2.5259 1.7606 -0.4983 -0.1197 0.1059  326 ILE A CG2 
2251  C CD1 . ILE A 295 ? 2.9110 2.7246 1.7964 -0.5612 -0.1954 0.1555  326 ILE A CD1 
2252  N N   . ARG A 296 ? 2.8704 2.4728 1.8116 -0.5157 -0.1453 0.0490  327 ARG A N   
2253  C CA  . ARG A 296 ? 2.8700 2.4030 1.7809 -0.5142 -0.1245 0.0120  327 ARG A CA  
2254  C C   . ARG A 296 ? 2.8192 2.3174 1.7729 -0.4785 -0.1117 0.0220  327 ARG A C   
2255  O O   . ARG A 296 ? 2.7676 2.2997 1.7867 -0.4579 -0.1239 0.0561  327 ARG A O   
2256  C CB  . ARG A 296 ? 2.8285 2.3571 1.7556 -0.5325 -0.1403 -0.0094 327 ARG A CB  
2257  C CG  . ARG A 296 ? 2.8773 2.4308 1.7540 -0.5696 -0.1493 -0.0275 327 ARG A CG  
2258  C CD  . ARG A 296 ? 2.8230 2.3817 1.7280 -0.5869 -0.1675 -0.0454 327 ARG A CD  
2259  N NE  . ARG A 296 ? 2.7786 2.2703 1.6834 -0.5784 -0.1522 -0.0724 327 ARG A NE  
2260  C CZ  . ARG A 296 ? 2.7200 2.2010 1.6460 -0.5918 -0.1623 -0.0929 327 ARG A CZ  
2261  N NH1 . ARG A 296 ? 2.6801 2.0953 1.6005 -0.5841 -0.1472 -0.1166 327 ARG A NH1 
2262  N NH2 . ARG A 296 ? 2.6986 2.2340 1.6512 -0.6135 -0.1874 -0.0902 327 ARG A NH2 
2263  N N   . GLN A 297 ? 2.8934 2.3231 1.8086 -0.4717 -0.0871 -0.0078 328 GLN A N   
2264  C CA  . GLN A 297 ? 2.8527 2.2427 1.8010 -0.4389 -0.0736 -0.0028 328 GLN A CA  
2265  C C   . GLN A 297 ? 2.7836 2.1362 1.7641 -0.4359 -0.0802 -0.0187 328 GLN A C   
2266  O O   . GLN A 297 ? 2.7885 2.1224 1.7391 -0.4600 -0.0839 -0.0464 328 GLN A O   
2267  C CB  . GLN A 297 ? 2.9221 2.2583 1.8068 -0.4294 -0.0407 -0.0232 328 GLN A CB  
2268  C CG  . GLN A 297 ? 2.9937 2.2903 1.7924 -0.4563 -0.0255 -0.0625 328 GLN A CG  
2269  C CD  . GLN A 297 ? 3.0755 2.3292 1.8121 -0.4476 0.0070  -0.0780 328 GLN A CD  
2270  O OE1 . GLN A 297 ? 3.1410 2.3944 1.8096 -0.4695 0.0193  -0.0931 328 GLN A OE1 
2271  N NE2 . GLN A 297 ? 3.0724 2.2884 1.8322 -0.4159 0.0215  -0.0756 328 GLN A NE2 
2272  N N   . ALA A 298 ? 2.8021 2.1431 1.8420 -0.4074 -0.0810 -0.0016 329 ALA A N   
2273  C CA  . ALA A 298 ? 2.7276 2.0315 1.8016 -0.4033 -0.0870 -0.0137 329 ALA A CA  
2274  C C   . ALA A 298 ? 2.7653 1.9902 1.7733 -0.4082 -0.0651 -0.0544 329 ALA A C   
2275  O O   . ALA A 298 ? 2.8380 2.0307 1.7910 -0.4014 -0.0421 -0.0667 329 ALA A O   
2276  C CB  . ALA A 298 ? 2.6574 1.9642 1.8042 -0.3713 -0.0903 0.0144  329 ALA A CB  
2277  N N   . HIS A 299 ? 2.8879 2.0804 1.9002 -0.4211 -0.0720 -0.0761 330 HIS A N   
2278  C CA  . HIS A 299 ? 2.9205 2.0343 1.8689 -0.4282 -0.0532 -0.1155 330 HIS A CA  
2279  C C   . HIS A 299 ? 2.8281 1.9063 1.8126 -0.4291 -0.0627 -0.1260 330 HIS A C   
2280  O O   . HIS A 299 ? 2.7442 1.8637 1.7934 -0.4335 -0.0842 -0.1089 330 HIS A O   
2281  C CB  . HIS A 299 ? 3.0001 2.1088 1.8702 -0.4614 -0.0464 -0.1455 330 HIS A CB  
2282  C CG  . HIS A 299 ? 2.9597 2.1090 1.8475 -0.4911 -0.0684 -0.1505 330 HIS A CG  
2283  N ND1 . HIS A 299 ? 2.9064 2.1350 1.8296 -0.5000 -0.0885 -0.1246 330 HIS A ND1 
2284  C CD2 . HIS A 299 ? 2.9666 2.0881 1.8415 -0.5142 -0.0735 -0.1791 330 HIS A CD2 
2285  C CE1 . HIS A 299 ? 2.8779 2.1279 1.8129 -0.5261 -0.1056 -0.1368 330 HIS A CE1 
2286  N NE2 . HIS A 299 ? 2.9138 2.1004 1.8200 -0.5358 -0.0962 -0.1705 330 HIS A NE2 
2287  N N   . CYS A 300 ? 3.0007 1.9996 1.9413 -0.4254 -0.0460 -0.1547 331 CYS A N   
2288  C CA  . CYS A 300 ? 2.9189 1.8697 1.8790 -0.4286 -0.0516 -0.1698 331 CYS A CA  
2289  C C   . CYS A 300 ? 2.9562 1.8435 1.8351 -0.4546 -0.0391 -0.2147 331 CYS A C   
2290  O O   . CYS A 300 ? 3.0397 1.8857 1.8485 -0.4528 -0.0182 -0.2337 331 CYS A O   
2291  C CB  . CYS A 300 ? 2.8845 1.7923 1.8739 -0.3949 -0.0443 -0.1581 331 CYS A CB  
2292  S SG  . CYS A 300 ? 2.8071 1.7786 1.9041 -0.3662 -0.0613 -0.1075 331 CYS A SG  
2293  N N   . ASN A 301 ? 2.9419 1.8202 1.8294 -0.4793 -0.0507 -0.2326 332 ASN A N   
2294  C CA  . ASN A 301 ? 2.9692 1.7881 1.7817 -0.5075 -0.0400 -0.2764 332 ASN A CA  
2295  C C   . ASN A 301 ? 2.9573 1.6968 1.7647 -0.5045 -0.0360 -0.2960 332 ASN A C   
2296  O O   . ASN A 301 ? 2.8920 1.6401 1.7659 -0.4994 -0.0506 -0.2819 332 ASN A O   
2297  C CB  . ASN A 301 ? 2.9438 1.8085 1.7610 -0.5433 -0.0550 -0.2883 332 ASN A CB  
2298  C CG  . ASN A 301 ? 3.0258 1.9496 1.8163 -0.5564 -0.0556 -0.2828 332 ASN A CG  
2299  O OD1 . ASN A 301 ? 3.1101 2.0350 1.8678 -0.5421 -0.0421 -0.2743 332 ASN A OD1 
2300  N ND2 . ASN A 301 ? 3.0023 1.9752 1.8055 -0.5849 -0.0713 -0.2887 332 ASN A ND2 
2301  N N   . VAL A 302 ? 3.0747 1.7719 1.8332 -0.4949 -0.0140 -0.3153 333 VAL A N   
2302  C CA  . VAL A 302 ? 3.0462 1.7362 1.8457 -0.4704 -0.0062 -0.3136 333 VAL A CA  
2303  C C   . VAL A 302 ? 3.0803 1.7872 1.8563 -0.4794 0.0074  -0.3318 333 VAL A C   
2304  O O   . VAL A 302 ? 3.1518 1.8406 1.8662 -0.4834 0.0237  -0.3443 333 VAL A O   
2305  C CB  . VAL A 302 ? 3.0663 1.7046 1.8576 -0.4372 0.0053  -0.3065 333 VAL A CB  
2306  C CG1 . VAL A 302 ? 3.0463 1.6852 1.8707 -0.4164 0.0120  -0.3069 333 VAL A CG1 
2307  C CG2 . VAL A 302 ? 3.0221 1.6468 1.8530 -0.4254 -0.0090 -0.2848 333 VAL A CG2 
2308  N N   . SER A 303 ? 3.0708 1.8125 1.8979 -0.4817 0.0013  -0.3325 334 SER A N   
2309  C CA  . SER A 303 ? 3.1199 1.8791 1.9356 -0.4896 0.0121  -0.3475 334 SER A CA  
2310  C C   . SER A 303 ? 3.2342 1.9540 2.0157 -0.4704 0.0312  -0.3528 334 SER A C   
2311  O O   . SER A 303 ? 3.2039 1.9044 2.0129 -0.4459 0.0317  -0.3440 334 SER A O   
2312  C CB  . SER A 303 ? 3.0272 1.8269 1.9111 -0.4901 0.0015  -0.3452 334 SER A CB  
2313  O OG  . SER A 303 ? 2.9649 1.7600 1.9044 -0.4682 -0.0071 -0.3294 334 SER A OG  
2314  N N   . LYS A 304 ? 3.1282 1.8387 1.8515 -0.4819 0.0462  -0.3664 335 LYS A N   
2315  C CA  . LYS A 304 ? 3.1881 1.8605 1.8763 -0.4658 0.0644  -0.3715 335 LYS A CA  
2316  C C   . LYS A 304 ? 3.1587 1.8347 1.8851 -0.4520 0.0642  -0.3695 335 LYS A C   
2317  O O   . LYS A 304 ? 3.2047 1.8477 1.9250 -0.4305 0.0714  -0.3660 335 LYS A O   
2318  C CB  . LYS A 304 ? 3.2656 1.9387 1.8965 -0.4844 0.0796  -0.3866 335 LYS A CB  
2319  C CG  . LYS A 304 ? 3.3003 1.9830 1.8883 -0.5044 0.0806  -0.3916 335 LYS A CG  
2320  C CD  . LYS A 304 ? 3.3783 2.0626 1.9150 -0.5198 0.0978  -0.4059 335 LYS A CD  
2321  C CE  . LYS A 304 ? 3.4367 2.0782 1.9499 -0.5004 0.1159  -0.4092 335 LYS A CE  
2322  N NZ  . LYS A 304 ? 3.5118 2.1549 1.9795 -0.5162 0.1322  -0.4223 335 LYS A NZ  
2323  N N   . ALA A 305 ? 3.3893 2.1064 2.1552 -0.4642 0.0557  -0.3720 336 ALA A N   
2324  C CA  . ALA A 305 ? 3.3607 2.0851 2.1612 -0.4529 0.0556  -0.3709 336 ALA A CA  
2325  C C   . ALA A 305 ? 3.2977 2.0149 2.1460 -0.4285 0.0461  -0.3561 336 ALA A C   
2326  O O   . ALA A 305 ? 3.3334 2.0327 2.1863 -0.4114 0.0504  -0.3533 336 ALA A O   
2327  C CB  . ALA A 305 ? 3.3083 2.0798 2.1413 -0.4710 0.0490  -0.3777 336 ALA A CB  
2328  N N   . THR A 306 ? 3.1281 1.8608 2.0138 -0.4274 0.0326  -0.3459 337 THR A N   
2329  C CA  . THR A 306 ? 3.0589 1.7896 1.9953 -0.4047 0.0234  -0.3308 337 THR A CA  
2330  C C   . THR A 306 ? 3.2050 1.8884 2.1121 -0.3833 0.0304  -0.3247 337 THR A C   
2331  O O   . THR A 306 ? 3.2769 1.9512 2.2085 -0.3628 0.0292  -0.3174 337 THR A O   
2332  C CB  . THR A 306 ? 2.9516 1.7100 1.9361 -0.4096 0.0075  -0.3203 337 THR A CB  
2333  O OG1 . THR A 306 ? 2.8945 1.6969 1.9049 -0.4296 0.0012  -0.3276 337 THR A OG1 
2334  C CG2 . THR A 306 ? 2.8198 1.5849 1.8657 -0.3870 -0.0016 -0.3045 337 THR A CG2 
2335  N N   . TRP A 307 ? 2.9083 1.5629 1.7631 -0.3879 0.0377  -0.3283 338 TRP A N   
2336  C CA  . TRP A 307 ? 3.0453 1.6536 1.8707 -0.3669 0.0453  -0.3237 338 TRP A CA  
2337  C C   . TRP A 307 ? 3.2032 1.7837 1.9966 -0.3555 0.0589  -0.3310 338 TRP A C   
2338  O O   . TRP A 307 ? 3.3176 1.8680 2.1107 -0.3320 0.0613  -0.3247 338 TRP A O   
2339  C CB  . TRP A 307 ? 3.0435 1.6322 1.8199 -0.3772 0.0506  -0.3277 338 TRP A CB  
2340  C CG  . TRP A 307 ? 3.1566 1.6994 1.9076 -0.3545 0.0582  -0.3228 338 TRP A CG  
2341  C CD1 . TRP A 307 ? 3.2719 1.7783 1.9636 -0.3490 0.0759  -0.3329 338 TRP A CD1 
2342  C CD2 . TRP A 307 ? 3.1549 1.6846 1.9432 -0.3325 0.0489  -0.3064 338 TRP A CD2 
2343  N NE1 . TRP A 307 ? 3.3349 1.8052 2.0236 -0.3238 0.0787  -0.3249 338 TRP A NE1 
2344  C CE2 . TRP A 307 ? 3.2707 1.7544 2.0186 -0.3132 0.0620  -0.3081 338 TRP A CE2 
2345  C CE3 . TRP A 307 ? 3.0557 1.6102 1.9111 -0.3265 0.0315  -0.2898 338 TRP A CE3 
2346  C CZ2 . TRP A 307 ? 3.2928 1.7541 2.0655 -0.2876 0.0578  -0.2937 338 TRP A CZ2 
2347  C CZ3 . TRP A 307 ? 3.0819 1.6156 1.9625 -0.3024 0.0271  -0.2742 338 TRP A CZ3 
2348  C CH2 . TRP A 307 ? 3.2040 1.6912 2.0436 -0.2828 0.0399  -0.2761 338 TRP A CH2 
2349  N N   . ASN A 308 ? 3.2532 1.8438 2.0217 -0.3716 0.0673  -0.3437 339 ASN A N   
2350  C CA  . ASN A 308 ? 3.4047 1.9688 2.1417 -0.3637 0.0799  -0.3503 339 ASN A CA  
2351  C C   . ASN A 308 ? 3.4779 2.0468 2.2577 -0.3467 0.0724  -0.3422 339 ASN A C   
2352  O O   . ASN A 308 ? 3.6232 2.1606 2.3883 -0.3290 0.0777  -0.3406 339 ASN A O   
2353  C CB  . ASN A 308 ? 3.4505 2.0325 2.1624 -0.3872 0.0879  -0.3638 339 ASN A CB  
2354  C CG  . ASN A 308 ? 3.7073 2.2557 2.3604 -0.3881 0.1057  -0.3741 339 ASN A CG  
2355  O OD1 . ASN A 308 ? 3.8135 2.3231 2.4365 -0.3726 0.1142  -0.3733 339 ASN A OD1 
2356  N ND2 . ASN A 308 ? 3.8987 2.4633 2.5382 -0.4062 0.1118  -0.3840 339 ASN A ND2 
2357  N N   . GLU A 309 ? 3.5743 2.1839 2.4078 -0.3521 0.0600  -0.3374 340 GLU A N   
2358  C CA  . GLU A 309 ? 3.6203 2.2242 2.4758 -0.3444 0.0556  -0.3279 340 GLU A CA  
2359  C C   . GLU A 309 ? 3.6328 2.2344 2.5307 -0.3189 0.0453  -0.3146 340 GLU A C   
2360  O O   . GLU A 309 ? 3.7627 2.3308 2.6457 -0.3080 0.0469  -0.3070 340 GLU A O   
2361  C CB  . GLU A 309 ? 3.4964 2.1309 2.3747 -0.3647 0.0504  -0.3269 340 GLU A CB  
2362  C CG  . GLU A 309 ? 3.5080 2.1445 2.3441 -0.3901 0.0617  -0.3406 340 GLU A CG  
2363  C CD  . GLU A 309 ? 3.3954 2.0608 2.2510 -0.4111 0.0586  -0.3417 340 GLU A CD  
2364  O OE1 . GLU A 309 ? 3.3101 1.9838 2.2004 -0.4069 0.0507  -0.3315 340 GLU A OE1 
2365  O OE2 . GLU A 309 ? 3.4370 2.1183 2.2742 -0.4317 0.0643  -0.3533 340 GLU A OE2 
2366  N N   . THR A 310 ? 3.2241 1.8404 2.1493 -0.3151 0.0376  -0.3089 341 THR A N   
2367  C CA  . THR A 310 ? 3.2318 1.8411 2.1926 -0.2936 0.0291  -0.2942 341 THR A CA  
2368  C C   . THR A 310 ? 3.4228 1.9839 2.3443 -0.2743 0.0379  -0.2943 341 THR A C   
2369  O O   . THR A 310 ? 3.5103 2.0644 2.4580 -0.2541 0.0331  -0.2858 341 THR A O   
2370  C CB  . THR A 310 ? 3.1139 1.7348 2.0931 -0.2992 0.0215  -0.2866 341 THR A CB  
2371  O OG1 . THR A 310 ? 2.9364 1.6032 1.9551 -0.3166 0.0130  -0.2871 341 THR A OG1 
2372  C CG2 . THR A 310 ? 3.1243 1.7407 2.1455 -0.2769 0.0128  -0.2697 341 THR A CG2 
2373  N N   . LEU A 311 ? 3.2963 1.8257 2.1561 -0.2804 0.0511  -0.3046 342 LEU A N   
2374  C CA  . LEU A 311 ? 3.4475 1.9304 2.2682 -0.2616 0.0616  -0.3068 342 LEU A CA  
2375  C C   . LEU A 311 ? 3.5679 2.0389 2.3803 -0.2540 0.0654  -0.3109 342 LEU A C   
2376  O O   . LEU A 311 ? 3.6423 2.0875 2.4559 -0.2320 0.0656  -0.3065 342 LEU A O   
2377  C CB  . LEU A 311 ? 3.4460 1.9021 2.2025 -0.2718 0.0770  -0.3187 342 LEU A CB  
2378  C CG  . LEU A 311 ? 3.4141 1.8440 2.1586 -0.2579 0.0797  -0.3135 342 LEU A CG  
2379  C CD1 . LEU A 311 ? 3.4114 1.8138 2.0874 -0.2670 0.0981  -0.3275 342 LEU A CD1 
2380  C CD2 . LEU A 311 ? 3.4355 1.8414 2.2021 -0.2264 0.0771  -0.3039 342 LEU A CD2 
2381  N N   . GLY A 312 ? 3.5032 1.9928 2.3083 -0.2719 0.0679  -0.3191 343 GLY A N   
2382  C CA  . GLY A 312 ? 3.6561 2.1118 2.4262 -0.2709 0.0744  -0.3199 343 GLY A CA  
2383  C C   . GLY A 312 ? 3.6987 2.1445 2.4887 -0.2631 0.0645  -0.3054 343 GLY A C   
2384  O O   . GLY A 312 ? 3.8725 2.2758 2.6259 -0.2570 0.0686  -0.3027 343 GLY A O   
2385  N N   . LYS A 313 ? 3.4382 1.9224 2.2848 -0.2634 0.0513  -0.2961 344 LYS A N   
2386  C CA  . LYS A 313 ? 3.4704 1.9486 2.3375 -0.2560 0.0418  -0.2824 344 LYS A CA  
2387  C C   . LYS A 313 ? 3.5746 2.0462 2.4738 -0.2278 0.0349  -0.2742 344 LYS A C   
2388  O O   . LYS A 313 ? 3.5663 2.0180 2.4658 -0.2175 0.0294  -0.2648 344 LYS A O   
2389  C CB  . LYS A 313 ? 3.2771 1.7985 2.1925 -0.2681 0.0314  -0.2753 344 LYS A CB  
2390  C CG  . LYS A 313 ? 3.1772 1.7034 2.0656 -0.2953 0.0371  -0.2808 344 LYS A CG  
2391  C CD  . LYS A 313 ? 2.9704 1.5466 1.9158 -0.3047 0.0269  -0.2764 344 LYS A CD  
2392  C CE  . LYS A 313 ? 2.9535 1.5406 1.9463 -0.2903 0.0146  -0.2611 344 LYS A CE  
2393  N NZ  . LYS A 313 ? 2.7532 1.3885 1.8055 -0.2977 0.0049  -0.2556 344 LYS A NZ  
2394  N N   . VAL A 314 ? 3.5241 2.0128 2.4505 -0.2154 0.0352  -0.2777 345 VAL A N   
2395  C CA  . VAL A 314 ? 3.3549 1.8387 2.3152 -0.1883 0.0304  -0.2701 345 VAL A CA  
2396  C C   . VAL A 314 ? 3.3742 1.8103 2.2873 -0.1741 0.0400  -0.2768 345 VAL A C   
2397  O O   . VAL A 314 ? 3.3165 1.7317 2.2371 -0.1561 0.0353  -0.2689 345 VAL A O   
2398  C CB  . VAL A 314 ? 3.2666 1.7469 2.2263 -0.1862 0.0319  -0.2667 345 VAL A CB  
2399  C CG1 . VAL A 314 ? 3.1132 1.5668 2.0815 -0.1591 0.0315  -0.2580 345 VAL A CG1 
2400  C CG2 . VAL A 314 ? 3.2239 1.7485 2.2334 -0.1987 0.0208  -0.2578 345 VAL A CG2 
2401  N N   . VAL A 315 ? 3.5762 1.9916 2.4364 -0.1828 0.0538  -0.2912 346 VAL A N   
2402  C CA  . VAL A 315 ? 3.6378 2.0087 2.4552 -0.1687 0.0640  -0.2984 346 VAL A CA  
2403  C C   . VAL A 315 ? 3.7894 2.1218 2.5697 -0.1709 0.0629  -0.2933 346 VAL A C   
2404  O O   . VAL A 315 ? 3.7780 2.0741 2.5400 -0.1528 0.0648  -0.2931 346 VAL A O   
2405  C CB  . VAL A 315 ? 3.7442 2.0898 2.4956 -0.1822 0.0820  -0.3132 346 VAL A CB  
2406  C CG1 . VAL A 315 ? 3.9027 2.2627 2.6329 -0.2091 0.0853  -0.3197 346 VAL A CG1 
2407  C CG2 . VAL A 315 ? 3.7420 2.0399 2.4505 -0.1653 0.0942  -0.3206 346 VAL A CG2 
2408  N N   . LYS A 316 ? 3.5610 1.8988 2.3282 -0.1928 0.0598  -0.2891 347 LYS A N   
2409  C CA  . LYS A 316 ? 3.6563 1.9565 2.3858 -0.1964 0.0582  -0.2833 347 LYS A CA  
2410  C C   . LYS A 316 ? 3.5395 1.8424 2.3088 -0.1782 0.0433  -0.2697 347 LYS A C   
2411  O O   . LYS A 316 ? 3.5626 1.8278 2.3013 -0.1725 0.0410  -0.2656 347 LYS A O   
2412  C CB  . LYS A 316 ? 3.8000 2.1050 2.5034 -0.2256 0.0612  -0.2835 347 LYS A CB  
2413  C CG  . LYS A 316 ? 3.9321 2.1851 2.5605 -0.2374 0.0734  -0.2884 347 LYS A CG  
2414  C CD  . LYS A 316 ? 3.9605 2.2079 2.5511 -0.2522 0.0897  -0.3021 347 LYS A CD  
2415  C CE  . LYS A 316 ? 4.0542 2.2474 2.5709 -0.2639 0.1029  -0.3060 347 LYS A CE  
2416  N NZ  . LYS A 316 ? 4.0285 2.2220 2.5096 -0.2864 0.1190  -0.3177 347 LYS A NZ  
2417  N N   . GLN A 317 ? 3.5678 1.9139 2.4039 -0.1693 0.0333  -0.2624 348 GLN A N   
2418  C CA  . GLN A 317 ? 3.4182 1.7728 2.2996 -0.1520 0.0196  -0.2489 348 GLN A CA  
2419  C C   . GLN A 317 ? 3.2821 1.6238 2.1819 -0.1240 0.0202  -0.2494 348 GLN A C   
2420  O O   . GLN A 317 ? 3.1569 1.4893 2.0772 -0.1072 0.0111  -0.2401 348 GLN A O   
2421  C CB  . GLN A 317 ? 3.3106 1.7187 2.2581 -0.1565 0.0099  -0.2397 348 GLN A CB  
2422  C CG  . GLN A 317 ? 3.4048 1.8333 2.3489 -0.1819 0.0077  -0.2380 348 GLN A CG  
2423  C CD  . GLN A 317 ? 3.4075 1.8170 2.3322 -0.1875 0.0014  -0.2302 348 GLN A CD  
2424  O OE1 . GLN A 317 ? 3.4634 1.8289 2.3424 -0.1820 0.0032  -0.2312 348 GLN A OE1 
2425  N NE2 . GLN A 317 ? 3.3302 1.7729 2.2903 -0.1983 -0.0063 -0.2224 348 GLN A NE2 
2426  N N   . LEU A 318 ? 3.4225 1.7648 2.3158 -0.1192 0.0311  -0.2605 349 LEU A N   
2427  C CA  . LEU A 318 ? 3.2699 1.6004 2.1800 -0.0926 0.0345  -0.2629 349 LEU A CA  
2428  C C   . LEU A 318 ? 3.3274 1.6042 2.1839 -0.0830 0.0399  -0.2686 349 LEU A C   
2429  O O   . LEU A 318 ? 3.1961 1.4575 2.0698 -0.0584 0.0382  -0.2666 349 LEU A O   
2430  C CB  . LEU A 318 ? 3.2509 1.5845 2.1488 -0.0933 0.0466  -0.2729 349 LEU A CB  
2431  C CG  . LEU A 318 ? 3.2269 1.5891 2.1502 -0.1027 0.0429  -0.2654 349 LEU A CG  
2432  C CD1 . LEU A 318 ? 3.2405 1.5751 2.1133 -0.1049 0.0581  -0.2740 349 LEU A CD1 
2433  C CD2 . LEU A 318 ? 3.0565 1.4409 2.0453 -0.0857 0.0299  -0.2483 349 LEU A CD2 
2434  N N   . ARG A 319 ? 3.4646 1.7119 2.2571 -0.1023 0.0467  -0.2750 350 ARG A N   
2435  C CA  . ARG A 319 ? 3.5291 1.7212 2.2651 -0.0954 0.0521  -0.2796 350 ARG A CA  
2436  C C   . ARG A 319 ? 3.4979 1.6713 2.2372 -0.0873 0.0381  -0.2677 350 ARG A C   
2437  O O   . ARG A 319 ? 3.5956 1.7239 2.2978 -0.0762 0.0395  -0.2701 350 ARG A O   
2438  C CB  . ARG A 319 ? 3.7495 1.9143 2.4153 -0.1199 0.0645  -0.2884 350 ARG A CB  
2439  C CG  . ARG A 319 ? 3.8286 2.0022 2.4762 -0.1293 0.0802  -0.3022 350 ARG A CG  
2440  C CD  . ARG A 319 ? 4.0599 2.1999 2.6356 -0.1525 0.0933  -0.3095 350 ARG A CD  
2441  N NE  . ARG A 319 ? 4.0897 2.2402 2.6473 -0.1634 0.1084  -0.3229 350 ARG A NE  
2442  C CZ  . ARG A 319 ? 4.1736 2.3532 2.7296 -0.1888 0.1114  -0.3253 350 ARG A CZ  
2443  N NH1 . ARG A 319 ? 4.3013 2.5005 2.8739 -0.2037 0.1014  -0.3157 350 ARG A NH1 
2444  N NH2 . ARG A 319 ? 4.1689 2.3586 2.7067 -0.1998 0.1244  -0.3377 350 ARG A NH2 
2445  N N   . LYS A 320 ? 3.7065 1.9130 2.4884 -0.0928 0.0248  -0.2554 351 LYS A N   
2446  C CA  . LYS A 320 ? 3.6049 1.7969 2.3922 -0.0856 0.0107  -0.2441 351 LYS A CA  
2447  C C   . LYS A 320 ? 3.4106 1.6058 2.2457 -0.0560 0.0036  -0.2391 351 LYS A C   
2448  O O   . LYS A 320 ? 3.3000 1.4795 2.1395 -0.0464 -0.0081 -0.2307 351 LYS A O   
2449  C CB  . LYS A 320 ? 3.5441 1.7734 2.3667 -0.0999 -0.0011 -0.2323 351 LYS A CB  
2450  C CG  . LYS A 320 ? 3.6986 1.9321 2.4890 -0.1294 0.0011  -0.2324 351 LYS A CG  
2451  C CD  . LYS A 320 ? 3.9360 2.1590 2.6794 -0.1481 0.0167  -0.2443 351 LYS A CD  
2452  C CE  . LYS A 320 ? 4.0581 2.2962 2.7887 -0.1760 0.0167  -0.2415 351 LYS A CE  
2453  N NZ  . LYS A 320 ? 4.2829 2.5021 2.9569 -0.1982 0.0318  -0.2515 351 LYS A NZ  
2454  N N   . HIS A 321 ? 3.4956 1.7104 2.3657 -0.0419 0.0108  -0.2440 352 HIS A N   
2455  C CA  . HIS A 321 ? 3.4879 1.7102 2.4100 -0.0136 0.0064  -0.2389 352 HIS A CA  
2456  C C   . HIS A 321 ? 3.5670 1.7632 2.4722 0.0049  0.0196  -0.2516 352 HIS A C   
2457  O O   . HIS A 321 ? 3.5924 1.7800 2.5266 0.0303  0.0168  -0.2489 352 HIS A O   
2458  C CB  . HIS A 321 ? 3.3817 1.6598 2.3768 -0.0114 0.0029  -0.2302 352 HIS A CB  
2459  C CG  . HIS A 321 ? 3.3001 1.6090 2.3198 -0.0284 -0.0090 -0.2178 352 HIS A CG  
2460  N ND1 . HIS A 321 ? 3.2692 1.5916 2.2657 -0.0549 -0.0067 -0.2210 352 HIS A ND1 
2461  C CD2 . HIS A 321 ? 3.2465 1.5760 2.3120 -0.0231 -0.0224 -0.2028 352 HIS A CD2 
2462  C CE1 . HIS A 321 ? 3.2003 1.5501 2.2281 -0.0644 -0.0179 -0.2090 352 HIS A CE1 
2463  N NE2 . HIS A 321 ? 3.1853 1.5398 2.2539 -0.0459 -0.0275 -0.1978 352 HIS A NE2 
2464  N N   . PHE A 322 ? 3.5601 1.7444 2.4201 -0.0073 0.0343  -0.2656 353 PHE A N   
2465  C CA  . PHE A 322 ? 3.6927 1.8545 2.5329 0.0074  0.0493  -0.2797 353 PHE A CA  
2466  C C   . PHE A 322 ? 3.8662 1.9761 2.6265 -0.0017 0.0591  -0.2907 353 PHE A C   
2467  O O   . PHE A 322 ? 3.9908 2.0857 2.7200 -0.0012 0.0751  -0.3047 353 PHE A O   
2468  C CB  . PHE A 322 ? 3.6491 1.8350 2.4971 0.0023  0.0606  -0.2860 353 PHE A CB  
2469  C CG  . PHE A 322 ? 3.5769 1.7844 2.4749 0.0165  0.0546  -0.2732 353 PHE A CG  
2470  C CD1 . PHE A 322 ? 3.6587 1.8436 2.5643 0.0452  0.0605  -0.2722 353 PHE A CD1 
2471  C CD2 . PHE A 322 ? 3.4279 1.6801 2.3705 0.0026  0.0428  -0.2612 353 PHE A CD2 
2472  C CE1 . PHE A 322 ? 3.5641 1.7700 2.5186 0.0593  0.0553  -0.2588 353 PHE A CE1 
2473  C CE2 . PHE A 322 ? 3.3669 1.6391 2.3576 0.0158  0.0372  -0.2477 353 PHE A CE2 
2474  C CZ  . PHE A 322 ? 3.4203 1.6694 2.4167 0.0441  0.0433  -0.2460 353 PHE A CZ  
2475  N N   . GLY A 323 ? 3.7941 1.8756 2.5193 -0.0106 0.0503  -0.2842 354 GLY A N   
2476  C CA  . GLY A 323 ? 3.9569 1.9866 2.6049 -0.0204 0.0592  -0.2922 354 GLY A CA  
2477  C C   . GLY A 323 ? 4.0127 2.0444 2.6158 -0.0531 0.0660  -0.2945 354 GLY A C   
2478  O O   . GLY A 323 ? 3.9240 1.9925 2.5446 -0.0663 0.0721  -0.2981 354 GLY A O   
2479  N N   . ASN A 324 ? 4.1010 2.0924 2.6460 -0.0665 0.0652  -0.2922 355 ASN A N   
2480  C CA  . ASN A 324 ? 4.1291 2.1208 2.6326 -0.0984 0.0719  -0.2928 355 ASN A CA  
2481  C C   . ASN A 324 ? 4.1823 2.1688 2.6516 -0.1100 0.0919  -0.3066 355 ASN A C   
2482  O O   . ASN A 324 ? 4.1069 2.1239 2.5789 -0.1319 0.0975  -0.3088 355 ASN A O   
2483  C CB  . ASN A 324 ? 4.2226 2.1659 2.6669 -0.1086 0.0686  -0.2876 355 ASN A CB  
2484  C CG  . ASN A 324 ? 4.2757 2.2366 2.7119 -0.1364 0.0647  -0.2799 355 ASN A CG  
2485  O OD1 . ASN A 324 ? 4.3183 2.2825 2.7250 -0.1603 0.0772  -0.2848 355 ASN A OD1 
2486  N ND2 . ASN A 324 ? 4.4110 2.3832 2.8733 -0.1340 0.0481  -0.2681 355 ASN A ND2 
2487  N N   . ASN A 325 ? 4.0338 1.9819 2.4707 -0.0958 0.1029  -0.3162 356 ASN A N   
2488  C CA  . ASN A 325 ? 4.0677 2.0056 2.4670 -0.1059 0.1230  -0.3300 356 ASN A CA  
2489  C C   . ASN A 325 ? 4.0089 1.9700 2.4488 -0.0844 0.1289  -0.3393 356 ASN A C   
2490  O O   . ASN A 325 ? 4.1169 2.0472 2.5403 -0.0657 0.1376  -0.3478 356 ASN A O   
2491  C CB  . ASN A 325 ? 4.2383 2.1115 2.5637 -0.1084 0.1334  -0.3345 356 ASN A CB  
2492  C CG  . ASN A 325 ? 4.2759 2.1246 2.5573 -0.1315 0.1293  -0.3253 356 ASN A CG  
2493  O OD1 . ASN A 325 ? 4.3751 2.1750 2.6164 -0.1259 0.1260  -0.3217 356 ASN A OD1 
2494  N ND2 . ASN A 325 ? 4.1893 2.0720 2.4788 -0.1574 0.1294  -0.3218 356 ASN A ND2 
2495  N N   . THR A 326 ? 3.9822 1.9979 2.4761 -0.0869 0.1245  -0.3379 357 THR A N   
2496  C CA  . THR A 326 ? 3.9493 1.9896 2.4825 -0.0681 0.1304  -0.3463 357 THR A CA  
2497  C C   . THR A 326 ? 3.8839 1.9657 2.4250 -0.0878 0.1379  -0.3530 357 THR A C   
2498  O O   . THR A 326 ? 3.8507 1.9526 2.3870 -0.1126 0.1339  -0.3482 357 THR A O   
2499  C CB  . THR A 326 ? 3.8463 1.9134 2.4513 -0.0437 0.1147  -0.3361 357 THR A CB  
2500  O OG1 . THR A 326 ? 3.8685 1.9313 2.4826 -0.0242 0.1250  -0.3420 357 THR A OG1 
2501  C CG2 . THR A 326 ? 3.6820 1.7955 2.3295 -0.0585 0.1011  -0.3244 357 THR A CG2 
2502  N N   . ILE A 327 ? 4.0270 2.0959 2.5501 -0.0784 0.1528  -0.3616 358 ILE A N   
2503  C CA  . ILE A 327 ? 4.0045 2.0884 2.5061 -0.0974 0.1642  -0.3666 358 ILE A CA  
2504  C C   . ILE A 327 ? 3.9168 2.0195 2.4561 -0.0865 0.1574  -0.3574 358 ILE A C   
2505  O O   . ILE A 327 ? 3.9361 2.0197 2.4879 -0.0595 0.1594  -0.3553 358 ILE A O   
2506  C CB  . ILE A 327 ? 4.0510 2.1009 2.4934 -0.0983 0.1888  -0.3818 358 ILE A CB  
2507  C CG1 . ILE A 327 ? 4.0936 2.1245 2.5007 -0.1095 0.1948  -0.3897 358 ILE A CG1 
2508  C CG2 . ILE A 327 ? 3.9606 2.0288 2.3808 -0.1198 0.2002  -0.3872 358 ILE A CG2 
2509  C CD1 . ILE A 327 ? 4.2358 2.2353 2.5854 -0.1130 0.2194  -0.4046 358 ILE A CD1 
2510  N N   . ILE A 328 ? 3.9225 2.0627 2.4816 -0.1069 0.1494  -0.3519 359 ILE A N   
2511  C CA  . ILE A 328 ? 3.7653 1.9256 2.3592 -0.1009 0.1423  -0.3423 359 ILE A CA  
2512  C C   . ILE A 328 ? 3.7075 1.8725 2.2655 -0.1199 0.1562  -0.3502 359 ILE A C   
2513  O O   . ILE A 328 ? 3.6544 1.8404 2.1965 -0.1481 0.1572  -0.3549 359 ILE A O   
2514  C CB  . ILE A 328 ? 3.6489 1.8503 2.3016 -0.1075 0.1198  -0.3281 359 ILE A CB  
2515  C CG1 . ILE A 328 ? 3.6776 1.8728 2.3620 -0.0885 0.1078  -0.3214 359 ILE A CG1 
2516  C CG2 . ILE A 328 ? 3.5285 1.7497 2.2177 -0.1019 0.1125  -0.3173 359 ILE A CG2 
2517  C CD1 . ILE A 328 ? 3.4820 1.7175 2.2247 -0.0938 0.0874  -0.3084 359 ILE A CD1 
2518  N N   . ARG A 329 ? 3.6624 1.8097 2.2090 -0.1049 0.1673  -0.3518 360 ARG A N   
2519  C CA  . ARG A 329 ? 3.6909 1.8408 2.2003 -0.1219 0.1819  -0.3600 360 ARG A CA  
2520  C C   . ARG A 329 ? 3.5957 1.7631 2.1390 -0.1173 0.1727  -0.3484 360 ARG A C   
2521  O O   . ARG A 329 ? 3.5711 1.7311 2.1518 -0.0900 0.1661  -0.3379 360 ARG A O   
2522  C CB  . ARG A 329 ? 3.8207 1.9342 2.2801 -0.1102 0.2071  -0.3736 360 ARG A CB  
2523  C CG  . ARG A 329 ? 3.8697 1.9893 2.2848 -0.1320 0.2240  -0.3839 360 ARG A CG  
2524  C CD  . ARG A 329 ? 3.8565 1.9620 2.2667 -0.1129 0.2363  -0.3840 360 ARG A CD  
2525  N NE  . ARG A 329 ? 3.9756 2.0455 2.3731 -0.0833 0.2531  -0.3906 360 ARG A NE  
2526  C CZ  . ARG A 329 ? 4.0472 2.1011 2.4212 -0.0701 0.2745  -0.3978 360 ARG A CZ  
2527  N NH1 . ARG A 329 ? 3.9545 2.0241 2.3112 -0.0852 0.2815  -0.3992 360 ARG A NH1 
2528  N NH2 . ARG A 329 ? 4.1995 2.2233 2.5677 -0.0419 0.2895  -0.4041 360 ARG A NH2 
2529  N N   . PHE A 330 ? 3.8282 2.0200 2.3604 -0.1443 0.1717  -0.3500 361 PHE A N   
2530  C CA  . PHE A 330 ? 3.7630 1.9703 2.3214 -0.1446 0.1633  -0.3396 361 PHE A CA  
2531  C C   . PHE A 330 ? 3.8148 2.0063 2.3248 -0.1486 0.1833  -0.3496 361 PHE A C   
2532  O O   . PHE A 330 ? 3.8775 2.0717 2.3376 -0.1719 0.1970  -0.3638 361 PHE A O   
2533  C CB  . PHE A 330 ? 3.6791 1.9279 2.2630 -0.1729 0.1461  -0.3340 361 PHE A CB  
2534  C CG  . PHE A 330 ? 3.6199 1.8899 2.2559 -0.1687 0.1273  -0.3236 361 PHE A CG  
2535  C CD1 . PHE A 330 ? 3.5529 1.8349 2.2492 -0.1502 0.1109  -0.3066 361 PHE A CD1 
2536  C CD2 . PHE A 330 ? 3.6337 1.9131 2.2590 -0.1832 0.1273  -0.3308 361 PHE A CD2 
2537  C CE1 . PHE A 330 ? 3.4992 1.8049 2.2429 -0.1478 0.0950  -0.2982 361 PHE A CE1 
2538  C CE2 . PHE A 330 ? 3.5819 1.8815 2.2524 -0.1799 0.1118  -0.3224 361 PHE A CE2 
2539  C CZ  . PHE A 330 ? 3.5142 1.8281 2.2433 -0.1627 0.0957  -0.3067 361 PHE A CZ  
2540  N N   . ALA A 331 ? 3.5805 1.7589 2.1072 -0.1264 0.1852  -0.3416 362 ALA A N   
2541  C CA  . ALA A 331 ? 3.6259 1.7908 2.1089 -0.1282 0.2052  -0.3505 362 ALA A CA  
2542  C C   . ALA A 331 ? 3.5600 1.7330 2.0759 -0.1235 0.1941  -0.3357 362 ALA A C   
2543  O O   . ALA A 331 ? 3.4960 1.6766 2.0737 -0.1068 0.1751  -0.3171 362 ALA A O   
2544  C CB  . ALA A 331 ? 3.7160 1.8458 2.1756 -0.0989 0.2286  -0.3593 362 ALA A CB  
2545  N N   . ASN A 332 ? 3.6288 1.8029 2.1027 -0.1396 0.2061  -0.3435 363 ASN A N   
2546  C CA  . ASN A 332 ? 3.5327 1.7879 2.0841 -0.1343 0.1909  -0.3093 363 ASN A CA  
2547  C C   . ASN A 332 ? 3.5201 1.7931 2.1308 -0.0919 0.1957  -0.2876 363 ASN A C   
2548  O O   . ASN A 332 ? 3.5910 1.8087 2.1795 -0.0664 0.2109  -0.3011 363 ASN A O   
2549  C CB  . ASN A 332 ? 3.5197 1.8422 2.0547 -0.1642 0.1944  -0.3058 363 ASN A CB  
2550  C CG  . ASN A 332 ? 3.6121 1.9269 2.0872 -0.1651 0.2234  -0.3227 363 ASN A CG  
2551  O OD1 . ASN A 332 ? 3.6427 1.9263 2.1114 -0.1363 0.2416  -0.3278 363 ASN A OD1 
2552  N ND2 . ASN A 332 ? 3.6644 1.9995 2.0884 -0.2004 0.2287  -0.3355 363 ASN A ND2 
2553  N N   . SER A 333 ? 3.3572 1.7090 2.0447 -0.0844 0.1825  -0.2537 364 SER A N   
2554  C CA  . SER A 333 ? 3.3327 1.7105 2.0860 -0.0465 0.1840  -0.2302 364 SER A CA  
2555  C C   . SER A 333 ? 3.4205 1.7984 2.1507 -0.0269 0.2122  -0.2383 364 SER A C   
2556  O O   . SER A 333 ? 3.4667 1.8507 2.1414 -0.0454 0.2303  -0.2537 364 SER A O   
2557  C CB  . SER A 333 ? 3.2426 1.7093 2.0738 -0.0482 0.1666  -0.1936 364 SER A CB  
2558  O OG  . SER A 333 ? 3.2567 1.7499 2.1514 -0.0131 0.1684  -0.1713 364 SER A OG  
2559  N N   . SER A 334 ? 3.3283 1.6993 2.1041 0.0110  0.2159  -0.2278 365 SER A N   
2560  C CA  . SER A 334 ? 3.4221 1.7926 2.1892 0.0352  0.2423  -0.2344 365 SER A CA  
2561  C C   . SER A 334 ? 3.4185 1.8767 2.2234 0.0340  0.2498  -0.2118 365 SER A C   
2562  O O   . SER A 334 ? 3.4888 1.9558 2.2562 0.0306  0.2743  -0.2236 365 SER A O   
2563  C CB  . SER A 334 ? 3.4559 1.7887 2.2626 0.0764  0.2413  -0.2315 365 SER A CB  
2564  O OG  . SER A 334 ? 3.4710 1.7162 2.2362 0.0782  0.2356  -0.2535 365 SER A OG  
2565  N N   . GLY A 335 ? 3.2737 1.7953 2.1500 0.0353  0.2296  -0.1798 366 GLY A N   
2566  C CA  . GLY A 335 ? 3.2651 1.8682 2.1770 0.0333  0.2349  -0.1568 366 GLY A CA  
2567  C C   . GLY A 335 ? 3.2089 1.8623 2.2106 0.0559  0.2201  -0.1236 366 GLY A C   
2568  O O   . GLY A 335 ? 3.1817 1.8062 2.2206 0.0760  0.2069  -0.1183 366 GLY A O   
2569  N N   . GLY A 336 ? 3.2514 1.9794 2.2859 0.0517  0.2226  -0.1010 367 GLY A N   
2570  C CA  . GLY A 336 ? 3.1982 1.9805 2.3150 0.0706  0.2111  -0.0687 367 GLY A CA  
2571  C C   . GLY A 336 ? 3.1221 1.9747 2.2679 0.0472  0.1942  -0.0414 367 GLY A C   
2572  O O   . GLY A 336 ? 3.1360 2.0201 2.2465 0.0233  0.2010  -0.0426 367 GLY A O   
2573  N N   . ASP A 337 ? 2.9893 1.8665 2.2001 0.0541  0.1720  -0.0161 368 ASP A N   
2574  C CA  . ASP A 337 ? 2.9133 1.8557 2.1589 0.0349  0.1541  0.0118  368 ASP A CA  
2575  C C   . ASP A 337 ? 2.8767 1.8075 2.0806 0.0007  0.1400  0.0016  368 ASP A C   
2576  O O   . ASP A 337 ? 2.8914 1.7611 2.0501 -0.0068 0.1401  -0.0243 368 ASP A O   
2577  C CB  . ASP A 337 ? 2.8378 1.8051 2.1635 0.0515  0.1353  0.0403  368 ASP A CB  
2578  C CG  . ASP A 337 ? 2.8685 1.8495 2.2392 0.0852  0.1483  0.0503  368 ASP A CG  
2579  O OD1 . ASP A 337 ? 2.9498 1.8962 2.2916 0.1019  0.1691  0.0290  368 ASP A OD1 
2580  O OD2 . ASP A 337 ? 2.8119 1.8390 2.2475 0.0948  0.1380  0.0792  368 ASP A OD2 
2581  N N   . LEU A 338 ? 2.8267 1.8177 2.0471 -0.0202 0.1275  0.0226  369 LEU A N   
2582  C CA  . LEU A 338 ? 2.8057 1.7959 1.9932 -0.0532 0.1129  0.0149  369 LEU A CA  
2583  C C   . LEU A 338 ? 2.7135 1.6770 1.9316 -0.0555 0.0909  0.0167  369 LEU A C   
2584  O O   . LEU A 338 ? 2.6840 1.6182 1.8648 -0.0787 0.0829  -0.0016 369 LEU A O   
2585  C CB  . LEU A 338 ? 2.7267 1.7906 1.9293 -0.0727 0.1033  0.0391  369 LEU A CB  
2586  C CG  . LEU A 338 ? 2.7265 1.7995 1.8914 -0.1083 0.0900  0.0310  369 LEU A CG  
2587  C CD1 . LEU A 338 ? 2.9186 1.9536 1.9983 -0.1246 0.1090  -0.0024 369 LEU A CD1 
2588  C CD2 . LEU A 338 ? 2.6275 1.7763 1.8222 -0.1230 0.0756  0.0609  369 LEU A CD2 
2589  N N   . GLU A 339 ? 2.8768 1.8494 2.1612 -0.0331 0.0819  0.0378  370 GLU A N   
2590  C CA  . GLU A 339 ? 2.8537 1.8018 2.1715 -0.0351 0.0618  0.0415  370 GLU A CA  
2591  C C   . GLU A 339 ? 2.9251 1.7899 2.2057 -0.0280 0.0668  0.0121  370 GLU A C   
2592  O O   . GLU A 339 ? 2.8764 1.7096 2.1672 -0.0364 0.0513  0.0082  370 GLU A O   
2593  C CB  . GLU A 339 ? 2.7550 1.7400 2.1538 -0.0138 0.0523  0.0740  370 GLU A CB  
2594  C CG  . GLU A 339 ? 2.6641 1.7268 2.1047 -0.0244 0.0414  0.1052  370 GLU A CG  
2595  C CD  . GLU A 339 ? 2.6597 1.7687 2.1233 -0.0057 0.0554  0.1237  370 GLU A CD  
2596  O OE1 . GLU A 339 ? 2.6992 1.7827 2.1582 0.0182  0.0723  0.1142  370 GLU A OE1 
2597  O OE2 . GLU A 339 ? 2.6395 1.8097 2.1254 -0.0151 0.0495  0.1473  370 GLU A OE2 
2598  N N   . VAL A 340 ? 2.8839 1.7109 2.1210 -0.0132 0.0882  -0.0086 371 VAL A N   
2599  C CA  . VAL A 340 ? 2.9516 1.6962 2.1505 -0.0038 0.0938  -0.0362 371 VAL A CA  
2600  C C   . VAL A 340 ? 3.0340 1.7352 2.1482 -0.0278 0.1040  -0.0695 371 VAL A C   
2601  O O   . VAL A 340 ? 3.0377 1.6743 2.1164 -0.0359 0.0998  -0.0917 371 VAL A O   
2602  C CB  . VAL A 340 ? 3.0003 1.7262 2.2123 0.0325  0.1104  -0.0374 371 VAL A CB  
2603  C CG1 . VAL A 340 ? 3.0226 1.6613 2.2013 0.0448  0.1126  -0.0627 371 VAL A CG1 
2604  C CG2 . VAL A 340 ? 2.8777 1.6540 2.1730 0.0543  0.1017  -0.0040 371 VAL A CG2 
2605  N N   . THR A 341 ? 3.0317 1.7668 2.1107 -0.0410 0.1176  -0.0736 372 THR A N   
2606  C CA  . THR A 341 ? 3.0842 1.7818 2.0801 -0.0644 0.1299  -0.1051 372 THR A CA  
2607  C C   . THR A 341 ? 2.9826 1.6949 1.9603 -0.1013 0.1134  -0.1089 372 THR A C   
2608  O O   . THR A 341 ? 3.0058 1.6776 1.9144 -0.1230 0.1206  -0.1378 372 THR A O   
2609  C CB  . THR A 341 ? 3.1999 1.9265 2.1631 -0.0644 0.1529  -0.1086 372 THR A CB  
2610  O OG1 . THR A 341 ? 3.1147 1.9230 2.1160 -0.0748 0.1444  -0.0803 372 THR A OG1 
2611  C CG2 . THR A 341 ? 3.2865 1.9950 2.2641 -0.0285 0.1719  -0.1095 372 THR A CG2 
2612  N N   . THR A 342 ? 2.9213 1.6898 1.9588 -0.1089 0.0920  -0.0816 373 THR A N   
2613  C CA  . THR A 342 ? 2.8678 1.6591 1.8980 -0.1425 0.0751  -0.0829 373 THR A CA  
2614  C C   . THR A 342 ? 2.7750 1.5602 1.8585 -0.1439 0.0523  -0.0717 373 THR A C   
2615  O O   . THR A 342 ? 2.7289 1.5099 1.8656 -0.1193 0.0474  -0.0547 373 THR A O   
2616  C CB  . THR A 342 ? 2.8172 1.6908 1.8663 -0.1556 0.0702  -0.0598 373 THR A CB  
2617  O OG1 . THR A 342 ? 2.7155 1.6395 1.8413 -0.1343 0.0616  -0.0245 373 THR A OG1 
2618  C CG2 . THR A 342 ? 2.9106 1.7894 1.9014 -0.1592 0.0932  -0.0723 373 THR A CG2 
2619  N N   . HIS A 343 ? 2.7869 1.5712 1.8545 -0.1743 0.0392  -0.0825 374 HIS A N   
2620  C CA  . HIS A 343 ? 2.6606 1.4423 1.7753 -0.1823 0.0179  -0.0744 374 HIS A CA  
2621  C C   . HIS A 343 ? 2.5519 1.4148 1.7414 -0.1807 0.0018  -0.0369 374 HIS A C   
2622  O O   . HIS A 343 ? 2.5147 1.4259 1.7083 -0.2036 -0.0087 -0.0308 374 HIS A O   
2623  C CB  . HIS A 343 ? 2.6644 1.4163 1.7332 -0.2165 0.0118  -0.1023 374 HIS A CB  
2624  C CG  . HIS A 343 ? 2.5660 1.3257 1.6851 -0.2293 -0.0096 -0.0938 374 HIS A CG  
2625  N ND1 . HIS A 343 ? 2.5155 1.2554 1.6871 -0.2111 -0.0177 -0.0798 374 HIS A ND1 
2626  C CD2 . HIS A 343 ? 2.5078 1.2946 1.6346 -0.2590 -0.0241 -0.0974 374 HIS A CD2 
2627  C CE1 . HIS A 343 ? 2.4317 1.1840 1.6396 -0.2298 -0.0352 -0.0755 374 HIS A CE1 
2628  N NE2 . HIS A 343 ? 2.4246 1.2060 1.6079 -0.2583 -0.0394 -0.0864 374 HIS A NE2 
2629  N N   . SER A 344 ? 2.6419 1.5199 1.8907 -0.1531 -0.0002 -0.0115 375 SER A N   
2630  C CA  . SER A 344 ? 2.5257 1.4768 1.8461 -0.1486 -0.0139 0.0254  375 SER A CA  
2631  C C   . SER A 344 ? 2.4340 1.3882 1.8023 -0.1613 -0.0348 0.0338  375 SER A C   
2632  O O   . SER A 344 ? 2.4357 1.3377 1.8122 -0.1560 -0.0375 0.0246  375 SER A O   
2633  C CB  . SER A 344 ? 2.4983 1.4639 1.8618 -0.1149 -0.0060 0.0481  375 SER A CB  
2634  O OG  . SER A 344 ? 2.5830 1.5370 1.9024 -0.1017 0.0155  0.0366  375 SER A OG  
2635  N N   . PHE A 345 ? 2.3753 1.3895 1.7750 -0.1786 -0.0496 0.0510  376 PHE A N   
2636  C CA  . PHE A 345 ? 2.3128 1.3370 1.7647 -0.1904 -0.0687 0.0610  376 PHE A CA  
2637  C C   . PHE A 345 ? 2.2627 1.3669 1.7614 -0.1988 -0.0831 0.0900  376 PHE A C   
2638  O O   . PHE A 345 ? 2.2785 1.4267 1.7630 -0.1980 -0.0791 0.1006  376 PHE A O   
2639  C CB  . PHE A 345 ? 2.3337 1.3074 1.7444 -0.2172 -0.0726 0.0273  376 PHE A CB  
2640  C CG  . PHE A 345 ? 2.3603 1.3576 1.7268 -0.2452 -0.0746 0.0112  376 PHE A CG  
2641  C CD1 . PHE A 345 ? 2.4432 1.4158 1.7348 -0.2499 -0.0583 -0.0127 376 PHE A CD1 
2642  C CD2 . PHE A 345 ? 2.3168 1.3601 1.7165 -0.2672 -0.0925 0.0193  376 PHE A CD2 
2643  C CE1 . PHE A 345 ? 2.4727 1.4668 1.7218 -0.2770 -0.0600 -0.0277 376 PHE A CE1 
2644  C CE2 . PHE A 345 ? 2.3432 1.4099 1.7031 -0.2931 -0.0954 0.0044  376 PHE A CE2 
2645  C CZ  . PHE A 345 ? 2.4145 1.4567 1.6979 -0.2986 -0.0792 -0.0190 376 PHE A CZ  
2646  N N   . ASN A 346 ? 2.2421 1.3627 1.7967 -0.2070 -0.1000 0.1030  377 ASN A N   
2647  C CA  . ASN A 346 ? 2.1914 1.3835 1.7987 -0.2144 -0.1162 0.1314  377 ASN A CA  
2648  C C   . ASN A 346 ? 2.1772 1.3736 1.7853 -0.2443 -0.1307 0.1165  377 ASN A C   
2649  O O   . ASN A 346 ? 2.1930 1.3431 1.8022 -0.2542 -0.1330 0.0976  377 ASN A O   
2650  C CB  . ASN A 346 ? 2.1324 1.3484 1.8172 -0.1955 -0.1231 0.1648  377 ASN A CB  
2651  C CG  . ASN A 346 ? 2.0908 1.3834 1.8250 -0.1975 -0.1368 0.1982  377 ASN A CG  
2652  O OD1 . ASN A 346 ? 2.0887 1.4131 1.8167 -0.2185 -0.1483 0.1954  377 ASN A OD1 
2653  N ND2 . ASN A 346 ? 2.0629 1.3845 1.8463 -0.1759 -0.1360 0.2297  377 ASN A ND2 
2654  N N   . CYS A 347 ? 2.2807 1.5331 1.8890 -0.2589 -0.1406 0.1250  378 CYS A N   
2655  C CA  . CYS A 347 ? 2.2676 1.5345 1.8820 -0.2871 -0.1557 0.1124  378 CYS A CA  
2656  C C   . CYS A 347 ? 2.2377 1.5833 1.8917 -0.2923 -0.1724 0.1409  378 CYS A C   
2657  O O   . CYS A 347 ? 2.2672 1.6455 1.8871 -0.2962 -0.1714 0.1446  378 CYS A O   
2658  C CB  . CYS A 347 ? 2.3320 1.5589 1.8686 -0.3091 -0.1475 0.0722  378 CYS A CB  
2659  S SG  . CYS A 347 ? 2.6290 1.8786 2.1797 -0.3430 -0.1658 0.0573  378 CYS A SG  
2660  N N   . GLY A 348 ? 2.2483 1.6222 1.9739 -0.2923 -0.1876 0.1615  379 GLY A N   
2661  C CA  . GLY A 348 ? 2.2193 1.6649 1.9903 -0.2960 -0.2056 0.1901  379 GLY A CA  
2662  C C   . GLY A 348 ? 2.1728 1.6578 1.9725 -0.2721 -0.2043 0.2277  379 GLY A C   
2663  O O   . GLY A 348 ? 2.1553 1.6995 1.9802 -0.2742 -0.2182 0.2524  379 GLY A O   
2664  N N   . GLY A 349 ? 2.0782 1.5319 1.8748 -0.2497 -0.1885 0.2326  380 GLY A N   
2665  C CA  . GLY A 349 ? 2.0665 1.5525 1.8881 -0.2267 -0.1843 0.2654  380 GLY A CA  
2666  C C   . GLY A 349 ? 2.1177 1.5962 1.8784 -0.2185 -0.1674 0.2581  380 GLY A C   
2667  O O   . GLY A 349 ? 2.1170 1.6017 1.8891 -0.1966 -0.1568 0.2764  380 GLY A O   
2668  N N   . GLU A 350 ? 2.1015 1.5667 1.7979 -0.2364 -0.1636 0.2308  381 GLU A N   
2669  C CA  . GLU A 350 ? 2.1575 1.6115 1.7904 -0.2321 -0.1459 0.2197  381 GLU A CA  
2670  C C   . GLU A 350 ? 2.1884 1.5730 1.7876 -0.2205 -0.1261 0.1933  381 GLU A C   
2671  O O   . GLU A 350 ? 2.1779 1.5186 1.7834 -0.2247 -0.1276 0.1752  381 GLU A O   
2672  C CB  . GLU A 350 ? 2.1983 1.6677 1.7753 -0.2579 -0.1501 0.2021  381 GLU A CB  
2673  C CG  . GLU A 350 ? 2.1850 1.7234 1.7908 -0.2697 -0.1714 0.2281  381 GLU A CG  
2674  C CD  . GLU A 350 ? 2.2400 1.8190 1.8362 -0.2599 -0.1671 0.2536  381 GLU A CD  
2675  O OE1 . GLU A 350 ? 2.3333 1.8969 1.9299 -0.2382 -0.1502 0.2612  381 GLU A OE1 
2676  O OE2 . GLU A 350 ? 2.2227 1.8487 1.8105 -0.2747 -0.1810 0.2659  381 GLU A OE2 
2677  N N   . PHE A 351 ? 2.1853 1.5591 1.7474 -0.2062 -0.1072 0.1907  382 PHE A N   
2678  C CA  . PHE A 351 ? 2.2230 1.5329 1.7513 -0.1921 -0.0875 0.1669  382 PHE A CA  
2679  C C   . PHE A 351 ? 2.2957 1.5746 1.7409 -0.2055 -0.0730 0.1344  382 PHE A C   
2680  O O   . PHE A 351 ? 2.3339 1.6322 1.7460 -0.2029 -0.0611 0.1373  382 PHE A O   
2681  C CB  . PHE A 351 ? 2.2180 1.5353 1.7741 -0.1623 -0.0752 0.1876  382 PHE A CB  
2682  C CG  . PHE A 351 ? 2.1532 1.4911 1.7872 -0.1483 -0.0866 0.2165  382 PHE A CG  
2683  C CD1 . PHE A 351 ? 2.1356 1.4276 1.7941 -0.1369 -0.0855 0.2096  382 PHE A CD1 
2684  C CD2 . PHE A 351 ? 2.1131 1.5142 1.7938 -0.1476 -0.0986 0.2505  382 PHE A CD2 
2685  C CE1 . PHE A 351 ? 2.0788 1.3889 1.8075 -0.1259 -0.0952 0.2359  382 PHE A CE1 
2686  C CE2 . PHE A 351 ? 2.0575 1.4758 1.8084 -0.1356 -0.1079 0.2767  382 PHE A CE2 
2687  C CZ  . PHE A 351 ? 2.0400 1.4135 1.8151 -0.1252 -0.1057 0.2693  382 PHE A CZ  
2688  N N   . PHE A 352 ? 2.1091 1.3389 1.5195 -0.2214 -0.0731 0.1031  383 PHE A N   
2689  C CA  . PHE A 352 ? 2.1807 1.3763 1.5100 -0.2369 -0.0594 0.0700  383 PHE A CA  
2690  C C   . PHE A 352 ? 2.2322 1.3711 1.5256 -0.2156 -0.0360 0.0533  383 PHE A C   
2691  O O   . PHE A 352 ? 2.2113 1.3234 1.5395 -0.1930 -0.0334 0.0597  383 PHE A O   
2692  C CB  . PHE A 352 ? 2.1865 1.3494 1.4912 -0.2631 -0.0679 0.0418  383 PHE A CB  
2693  C CG  . PHE A 352 ? 2.1470 1.3645 1.4805 -0.2862 -0.0900 0.0528  383 PHE A CG  
2694  C CD1 . PHE A 352 ? 2.0782 1.3195 1.4844 -0.2840 -0.1083 0.0731  383 PHE A CD1 
2695  C CD2 . PHE A 352 ? 2.1821 1.4260 1.4700 -0.3107 -0.0924 0.0420  383 PHE A CD2 
2696  C CE1 . PHE A 352 ? 2.0449 1.3370 1.4809 -0.3038 -0.1288 0.0831  383 PHE A CE1 
2697  C CE2 . PHE A 352 ? 2.1479 1.4436 1.4650 -0.3310 -0.1142 0.0523  383 PHE A CE2 
2698  C CZ  . PHE A 352 ? 2.0795 1.3994 1.4719 -0.3268 -0.1324 0.0727  383 PHE A CZ  
2699  N N   . TYR A 353 ? 2.2709 1.3917 1.4939 -0.2235 -0.0190 0.0314  384 TYR A N   
2700  C CA  . TYR A 353 ? 2.3163 1.3798 1.4958 -0.2059 0.0048  0.0107  384 TYR A CA  
2701  C C   . TYR A 353 ? 2.4235 1.4470 1.5186 -0.2295 0.0162  -0.0259 384 TYR A C   
2702  O O   . TYR A 353 ? 2.4695 1.5161 1.5216 -0.2411 0.0260  -0.0298 384 TYR A O   
2703  C CB  . TYR A 353 ? 2.3227 1.4164 1.5122 -0.1840 0.0193  0.0293  384 TYR A CB  
2704  C CG  . TYR A 353 ? 2.2607 1.3887 1.5302 -0.1598 0.0105  0.0635  384 TYR A CG  
2705  C CD1 . TYR A 353 ? 2.2461 1.3369 1.5429 -0.1321 0.0175  0.0640  384 TYR A CD1 
2706  C CD2 . TYR A 353 ? 2.2184 1.4156 1.5355 -0.1650 -0.0053 0.0956  384 TYR A CD2 
2707  C CE1 . TYR A 353 ? 2.1899 1.3133 1.5590 -0.1115 0.0100  0.0950  384 TYR A CE1 
2708  C CE2 . TYR A 353 ? 2.1635 1.3910 1.5513 -0.1441 -0.0123 0.1265  384 TYR A CE2 
2709  C CZ  . TYR A 353 ? 2.1489 1.3402 1.5623 -0.1180 -0.0041 0.1259  384 TYR A CZ  
2710  O OH  . TYR A 353 ? 2.0948 1.3176 1.5776 -0.0987 -0.0106 0.1564  384 TYR A OH  
2711  N N   . CYS A 354 ? 2.5133 1.4755 1.5822 -0.2378 0.0158  -0.0529 385 CYS A N   
2712  C CA  . CYS A 354 ? 2.5714 1.4962 1.5626 -0.2647 0.0239  -0.0882 385 CYS A CA  
2713  C C   . CYS A 354 ? 2.6339 1.4897 1.5620 -0.2524 0.0495  -0.1155 385 CYS A C   
2714  O O   . CYS A 354 ? 2.6289 1.4430 1.5739 -0.2258 0.0560  -0.1155 385 CYS A O   
2715  C CB  . CYS A 354 ? 2.5542 1.4520 1.5497 -0.2855 0.0083  -0.1040 385 CYS A CB  
2716  S SG  . CYS A 354 ? 2.4842 1.4596 1.5531 -0.3023 -0.0219 -0.0761 385 CYS A SG  
2717  N N   . ASN A 355 ? 2.8528 1.6964 1.7073 -0.2728 0.0636  -0.1392 386 ASN A N   
2718  C CA  . ASN A 355 ? 2.9551 1.7334 1.7403 -0.2656 0.0896  -0.1681 386 ASN A CA  
2719  C C   . ASN A 355 ? 2.9634 1.6637 1.7102 -0.2745 0.0902  -0.1995 386 ASN A C   
2720  O O   . ASN A 355 ? 2.9485 1.6413 1.6610 -0.3057 0.0834  -0.2183 386 ASN A O   
2721  C CB  . ASN A 355 ? 3.0270 1.8223 1.7456 -0.2877 0.1048  -0.1818 386 ASN A CB  
2722  C CG  . ASN A 355 ? 3.1311 1.8720 1.7887 -0.2744 0.1352  -0.2044 386 ASN A CG  
2723  O OD1 . ASN A 355 ? 3.1567 1.8339 1.8068 -0.2538 0.1442  -0.2180 386 ASN A OD1 
2724  N ND2 . ASN A 355 ? 3.3379 2.1025 1.9498 -0.2875 0.1509  -0.2089 386 ASN A ND2 
2725  N N   . THR A 356 ? 3.0243 1.6659 1.7754 -0.2477 0.0981  -0.2056 387 THR A N   
2726  C CA  . THR A 356 ? 3.0346 1.5960 1.7482 -0.2546 0.0982  -0.2342 387 THR A CA  
2727  C C   . THR A 356 ? 3.1399 1.6314 1.7702 -0.2521 0.1241  -0.2666 387 THR A C   
2728  O O   . THR A 356 ? 3.1693 1.5885 1.7811 -0.2355 0.1304  -0.2816 387 THR A O   
2729  C CB  . THR A 356 ? 2.9878 1.5249 1.7612 -0.2293 0.0860  -0.2196 387 THR A CB  
2730  O OG1 . THR A 356 ? 3.0220 1.5649 1.8250 -0.1929 0.0965  -0.2026 387 THR A OG1 
2731  C CG2 . THR A 356 ? 2.8808 1.4768 1.7283 -0.2380 0.0606  -0.1930 387 THR A CG2 
2732  N N   . SER A 357 ? 3.1902 1.7010 1.7678 -0.2689 0.1394  -0.2776 388 SER A N   
2733  C CA  . SER A 357 ? 3.3193 1.7660 1.8128 -0.2705 0.1658  -0.3098 388 SER A CA  
2734  C C   . SER A 357 ? 3.3309 1.7316 1.7530 -0.3062 0.1671  -0.3439 388 SER A C   
2735  O O   . SER A 357 ? 3.4299 1.7640 1.7768 -0.3096 0.1882  -0.3742 388 SER A O   
2736  C CB  . SER A 357 ? 3.4349 1.9226 1.9047 -0.2704 0.1851  -0.3052 388 SER A CB  
2737  O OG  . SER A 357 ? 3.3914 1.9129 1.9203 -0.2366 0.1879  -0.2778 388 SER A OG  
2738  N N   . GLY A 358 ? 3.3914 1.8263 1.8364 -0.3326 0.1456  -0.3399 389 GLY A N   
2739  C CA  . GLY A 358 ? 3.3842 1.7930 1.7767 -0.3681 0.1439  -0.3684 389 GLY A CA  
2740  C C   . GLY A 358 ? 3.3182 1.7268 1.7736 -0.3563 0.1299  -0.3593 389 GLY A C   
2741  O O   . GLY A 358 ? 3.2844 1.7171 1.7499 -0.3708 0.1275  -0.3642 389 GLY A O   
2742  N N   . LEU A 359 ? 3.4043 1.7897 1.9044 -0.3295 0.1210  -0.3448 390 LEU A N   
2743  C CA  . LEU A 359 ? 3.2893 1.6808 1.8528 -0.3153 0.1073  -0.3331 390 LEU A CA  
2744  C C   . LEU A 359 ? 3.3446 1.7032 1.9109 -0.2839 0.1188  -0.3331 390 LEU A C   
2745  O O   . LEU A 359 ? 3.3138 1.6831 1.9103 -0.2794 0.1129  -0.3308 390 LEU A O   
2746  C CB  . LEU A 359 ? 3.2196 1.6181 1.8435 -0.3074 0.0864  -0.3128 390 LEU A CB  
2747  C CG  . LEU A 359 ? 3.1614 1.5943 1.7988 -0.3376 0.0688  -0.3083 390 LEU A CG  
2748  C CD1 . LEU A 359 ? 3.0847 1.5397 1.8043 -0.3203 0.0497  -0.2784 390 LEU A CD1 
2749  C CD2 . LEU A 359 ? 3.0944 1.5725 1.7460 -0.3629 0.0615  -0.3157 390 LEU A CD2 
2750  N N   . PHE A 360 ? 3.3636 1.6845 1.8993 -0.2624 0.1348  -0.3360 391 PHE A N   
2751  C CA  . PHE A 360 ? 3.4458 1.7352 1.9864 -0.2307 0.1446  -0.3356 391 PHE A CA  
2752  C C   . PHE A 360 ? 3.5387 1.8071 2.0164 -0.2323 0.1694  -0.3539 391 PHE A C   
2753  O O   . PHE A 360 ? 3.5796 1.8149 2.0389 -0.2075 0.1852  -0.3570 391 PHE A O   
2754  C CB  . PHE A 360 ? 3.4563 1.7210 2.0249 -0.1995 0.1432  -0.3221 391 PHE A CB  
2755  C CG  . PHE A 360 ? 3.3332 1.6204 1.9688 -0.1980 0.1190  -0.3011 391 PHE A CG  
2756  C CD1 . PHE A 360 ? 3.2402 1.5562 1.9283 -0.1997 0.1016  -0.2922 391 PHE A CD1 
2757  C CD2 . PHE A 360 ? 3.3197 1.6019 1.9656 -0.1972 0.1143  -0.2900 391 PHE A CD2 
2758  C CE1 . PHE A 360 ? 3.1500 1.4932 1.9030 -0.1993 0.0808  -0.2728 391 PHE A CE1 
2759  C CE2 . PHE A 360 ? 3.2250 1.5399 1.9438 -0.1959 0.0914  -0.2655 391 PHE A CE2 
2760  C CZ  . PHE A 360 ? 3.1443 1.4826 1.9114 -0.1979 0.0755  -0.2595 391 PHE A CZ  
2761  N N   . ASN A 361 ? 3.5782 1.8683 2.0256 -0.2613 0.1737  -0.3654 392 ASN A N   
2762  C CA  . ASN A 361 ? 3.7973 2.0740 2.1898 -0.2673 0.1963  -0.3814 392 ASN A CA  
2763  C C   . ASN A 361 ? 3.8199 2.1022 2.2181 -0.2743 0.1946  -0.3852 392 ASN A C   
2764  O O   . ASN A 361 ? 3.8947 2.2027 2.2749 -0.3024 0.1960  -0.3929 392 ASN A O   
2765  C CB  . ASN A 361 ? 3.8776 2.1794 2.2256 -0.2982 0.2042  -0.3910 392 ASN A CB  
2766  C CG  . ASN A 361 ? 4.0358 2.3315 2.3299 -0.3083 0.2274  -0.4062 392 ASN A CG  
2767  O OD1 . ASN A 361 ? 4.1709 2.4323 2.4494 -0.2869 0.2433  -0.4111 392 ASN A OD1 
2768  N ND2 . ASN A 361 ? 4.1807 2.5119 2.4488 -0.3416 0.2288  -0.4133 392 ASN A ND2 
2769  N N   . SER A 362 ? 3.7708 2.0317 2.1946 -0.2498 0.1908  -0.3797 393 SER A N   
2770  C CA  . SER A 362 ? 3.7910 2.0581 2.2191 -0.2577 0.1883  -0.3828 393 SER A CA  
2771  C C   . SER A 362 ? 3.9190 2.1486 2.3423 -0.2309 0.1955  -0.3838 393 SER A C   
2772  O O   . SER A 362 ? 3.9603 2.1630 2.3882 -0.2037 0.1996  -0.3805 393 SER A O   
2773  C CB  . SER A 362 ? 3.6683 1.9693 2.1511 -0.2651 0.1655  -0.3716 393 SER A CB  
2774  O OG  . SER A 362 ? 3.6129 1.9488 2.1044 -0.2889 0.1572  -0.3704 393 SER A OG  
2775  N N   . THR A 363 ? 3.9600 2.1885 2.3751 -0.2386 0.1968  -0.3885 394 THR A N   
2776  C CA  . THR A 363 ? 4.0361 2.2308 2.4475 -0.2158 0.2008  -0.3892 394 THR A CA  
2777  C C   . THR A 363 ? 3.9720 2.1791 2.3980 -0.2260 0.1913  -0.3877 394 THR A C   
2778  O O   . THR A 363 ? 4.0121 2.2239 2.4088 -0.2468 0.2001  -0.3967 394 THR A O   
2779  C CB  . THR A 363 ? 4.1902 2.3512 2.5468 -0.2118 0.2251  -0.4029 394 THR A CB  
2780  O OG1 . THR A 363 ? 4.1909 2.3411 2.5342 -0.2008 0.2359  -0.4048 394 THR A OG1 
2781  C CG2 . THR A 363 ? 4.1947 2.3200 2.5473 -0.1889 0.2283  -0.4041 394 THR A CG2 
2782  N N   . TRP A 364 ? 4.0426 2.2565 2.5147 -0.2115 0.1739  -0.3761 395 TRP A N   
2783  C CA  . TRP A 364 ? 4.0417 2.2703 2.5350 -0.2185 0.1631  -0.3727 395 TRP A CA  
2784  C C   . TRP A 364 ? 4.1199 2.3143 2.6052 -0.1985 0.1645  -0.3731 395 TRP A C   
2785  O O   . TRP A 364 ? 4.1280 2.3036 2.6312 -0.1725 0.1598  -0.3672 395 TRP A O   
2786  C CB  . TRP A 364 ? 3.9311 2.2009 2.4821 -0.2230 0.1428  -0.3605 395 TRP A CB  
2787  C CG  . TRP A 364 ? 3.8850 2.1865 2.4311 -0.2493 0.1443  -0.3643 395 TRP A CG  
2788  C CD1 . TRP A 364 ? 3.8153 2.1230 2.3556 -0.2536 0.1467  -0.3644 395 TRP A CD1 
2789  C CD2 . TRP A 364 ? 3.8609 2.1925 2.4072 -0.2753 0.1432  -0.3691 395 TRP A CD2 
2790  N NE1 . TRP A 364 ? 3.7894 2.1300 2.3254 -0.2818 0.1463  -0.3692 395 TRP A NE1 
2791  C CE2 . TRP A 364 ? 3.7798 2.1365 2.3218 -0.2947 0.1442  -0.3722 395 TRP A CE2 
2792  C CE3 . TRP A 364 ? 3.8511 2.1862 2.3959 -0.2849 0.1424  -0.3705 395 TRP A CE3 
2793  C CZ2 . TRP A 364 ? 3.7545 2.1458 2.2989 -0.3212 0.1430  -0.3776 395 TRP A CZ2 
2794  C CZ3 . TRP A 364 ? 3.8000 2.1540 2.3310 -0.3140 0.1453  -0.3739 395 TRP A CZ3 
2795  C CH2 . TRP A 364 ? 3.7527 2.1518 2.3037 -0.3274 0.1420  -0.3796 395 TRP A CH2 
2796  N N   . ILE A 365 ? 3.9681 2.1547 2.4273 -0.2109 0.1707  -0.3800 396 ILE A N   
2797  C CA  . ILE A 365 ? 4.0580 2.1914 2.4815 -0.1996 0.1756  -0.3786 396 ILE A CA  
2798  C C   . ILE A 365 ? 4.0296 2.1505 2.4592 -0.2026 0.1619  -0.3639 396 ILE A C   
2799  O O   . ILE A 365 ? 3.9429 2.0989 2.4042 -0.2153 0.1508  -0.3564 396 ILE A O   
2800  C CB  . ILE A 365 ? 4.1676 2.2651 2.5219 -0.2188 0.1952  -0.3885 396 ILE A CB  
2801  C CG1 . ILE A 365 ? 4.1643 2.2920 2.5131 -0.2311 0.2070  -0.4018 396 ILE A CG1 
2802  C CG2 . ILE A 365 ? 4.2795 2.3205 2.5961 -0.1999 0.2044  -0.3917 396 ILE A CG2 
2803  C CD1 . ILE A 365 ? 4.2097 2.3178 2.5467 -0.2107 0.2181  -0.4082 396 ILE A CD1 
2804  N N   . SER A 366 ? 4.2528 2.3233 2.6498 -0.1916 0.1631  -0.3603 397 SER A N   
2805  C CA  . SER A 366 ? 4.2867 2.3416 2.6837 -0.1932 0.1503  -0.3468 397 SER A CA  
2806  C C   . SER A 366 ? 4.2717 2.3347 2.6466 -0.2258 0.1519  -0.3433 397 SER A C   
2807  O O   . SER A 366 ? 4.1851 2.2586 2.5786 -0.2312 0.1395  -0.3321 397 SER A O   
2808  C CB  . SER A 366 ? 4.4234 2.4176 2.7763 -0.1792 0.1533  -0.3457 397 SER A CB  
2809  O OG  . SER A 366 ? 4.5839 2.5389 2.8699 -0.1964 0.1711  -0.3536 397 SER A OG  
2810  N N   . ASN A 367 ? 4.1652 2.2237 2.5012 -0.2478 0.1679  -0.3530 398 ASN A N   
2811  C CA  . ASN A 367 ? 4.1563 2.2235 2.4720 -0.2799 0.1720  -0.3515 398 ASN A CA  
2812  C C   . ASN A 367 ? 4.1775 2.2621 2.4754 -0.2997 0.1869  -0.3643 398 ASN A C   
2813  O O   . ASN A 367 ? 4.0963 2.2318 2.4316 -0.3092 0.1823  -0.3669 398 ASN A O   
2814  C CB  . ASN A 367 ? 4.2468 2.2584 2.5037 -0.2901 0.1782  -0.3467 398 ASN A CB  
2815  C CG  . ASN A 367 ? 4.3715 2.3305 2.5731 -0.2834 0.1937  -0.3548 398 ASN A CG  
2816  O OD1 . ASN A 367 ? 4.4202 2.3487 2.6175 -0.2580 0.1898  -0.3532 398 ASN A OD1 
2817  N ND2 . ASN A 367 ? 4.4494 2.3991 2.6107 -0.3060 0.2115  -0.3642 398 ASN A ND2 
2818  N N   . ASN A 379 ? 4.0247 2.8443 2.6179 -0.5873 0.0915  -0.4380 411 ASN A N   
2819  C CA  . ASN A 379 ? 3.8921 2.7374 2.5443 -0.5834 0.0724  -0.4300 411 ASN A CA  
2820  C C   . ASN A 379 ? 3.8126 2.6823 2.4664 -0.5971 0.0576  -0.4254 411 ASN A C   
2821  O O   . ASN A 379 ? 3.7774 2.6913 2.4390 -0.6201 0.0478  -0.4308 411 ASN A O   
2822  C CB  . ASN A 379 ? 3.8429 2.7258 2.5340 -0.5933 0.0670  -0.4365 411 ASN A CB  
2823  C CG  . ASN A 379 ? 3.7091 2.6185 2.4659 -0.5871 0.0486  -0.4286 411 ASN A CG  
2824  O OD1 . ASN A 379 ? 3.6607 2.5527 2.4396 -0.5698 0.0419  -0.4165 411 ASN A OD1 
2825  N ND2 . ASN A 379 ? 3.6417 2.5936 2.4315 -0.6011 0.0406  -0.4353 411 ASN A ND2 
2826  N N   . ASP A 380 ? 3.7814 2.6231 2.4271 -0.5834 0.0549  -0.4151 412 ASP A N   
2827  C CA  . ASP A 380 ? 3.6460 2.5090 2.2913 -0.5968 0.0393  -0.4089 412 ASP A CA  
2828  C C   . ASP A 380 ? 3.5512 2.3847 2.2169 -0.5761 0.0314  -0.3943 412 ASP A C   
2829  O O   . ASP A 380 ? 3.5197 2.3389 2.2287 -0.5553 0.0296  -0.3873 412 ASP A O   
2830  C CB  . ASP A 380 ? 3.6329 2.4983 2.2134 -0.6141 0.0478  -0.4154 412 ASP A CB  
2831  C CG  . ASP A 380 ? 3.5247 2.4368 2.1058 -0.6391 0.0279  -0.4120 412 ASP A CG  
2832  O OD1 . ASP A 380 ? 3.4885 2.4386 2.1209 -0.6484 0.0089  -0.4089 412 ASP A OD1 
2833  O OD2 . ASP A 380 ? 3.5555 2.4690 2.0869 -0.6493 0.0307  -0.4115 412 ASP A OD2 
2834  N N   . SER A 381 ? 3.4513 2.2776 2.0866 -0.5815 0.0263  -0.3887 413 SER A N   
2835  C CA  . SER A 381 ? 3.4021 2.1993 2.0547 -0.5635 0.0180  -0.3743 413 SER A CA  
2836  C C   . SER A 381 ? 3.4377 2.1946 2.0289 -0.5548 0.0313  -0.3744 413 SER A C   
2837  O O   . SER A 381 ? 3.4920 2.2607 2.0298 -0.5715 0.0389  -0.3824 413 SER A O   
2838  C CB  . SER A 381 ? 3.3173 2.1521 2.0102 -0.5799 -0.0088 -0.3635 413 SER A CB  
2839  O OG  . SER A 381 ? 3.2780 2.0841 2.0004 -0.5613 -0.0178 -0.3476 413 SER A OG  
2840  N N   . ILE A 382 ? 3.1824 1.8942 1.7837 -0.5273 0.0347  -0.3651 414 ILE A N   
2841  C CA  . ILE A 382 ? 3.2346 1.9034 1.7845 -0.5130 0.0484  -0.3649 414 ILE A CA  
2842  C C   . ILE A 382 ? 3.2138 1.8857 1.7597 -0.5202 0.0317  -0.3540 414 ILE A C   
2843  O O   . ILE A 382 ? 3.1455 1.8258 1.7609 -0.4983 0.0191  -0.3303 414 ILE A O   
2844  C CB  . ILE A 382 ? 3.2426 1.8612 1.8057 -0.4779 0.0607  -0.3607 414 ILE A CB  
2845  C CG1 . ILE A 382 ? 3.3077 1.9257 1.8742 -0.4729 0.0734  -0.3696 414 ILE A CG1 
2846  C CG2 . ILE A 382 ? 3.3027 1.8777 1.8143 -0.4616 0.0766  -0.3622 414 ILE A CG2 
2847  C CD1 . ILE A 382 ? 3.3474 1.9241 1.9286 -0.4404 0.0818  -0.3644 414 ILE A CD1 
2848  N N   . THR A 383 ? 3.1625 1.8906 1.6927 -0.5291 0.0331  -0.3443 415 THR A N   
2849  C CA  . THR A 383 ? 3.0984 1.9060 1.6978 -0.5108 0.0197  -0.3023 415 THR A CA  
2850  C C   . THR A 383 ? 3.1130 1.9033 1.7167 -0.4742 0.0356  -0.2850 415 THR A C   
2851  O O   . THR A 383 ? 3.1927 1.9349 1.7287 -0.4708 0.0594  -0.3046 415 THR A O   
2852  C CB  . THR A 383 ? 3.1122 1.9876 1.6924 -0.5354 0.0142  -0.2975 415 THR A CB  
2853  O OG1 . THR A 383 ? 3.1110 1.9974 1.6793 -0.5708 0.0019  -0.3190 415 THR A OG1 
2854  C CG2 . THR A 383 ? 3.0401 1.9991 1.6965 -0.5196 -0.0040 -0.2532 415 THR A CG2 
2855  N N   . LEU A 384 ? 3.0027 1.8319 1.6866 -0.4470 0.0231  -0.2489 416 LEU A N   
2856  C CA  . LEU A 384 ? 3.0095 1.8283 1.7069 -0.4116 0.0367  -0.2310 416 LEU A CA  
2857  C C   . LEU A 384 ? 2.9647 1.8658 1.7110 -0.4014 0.0280  -0.1934 416 LEU A C   
2858  O O   . LEU A 384 ? 2.8894 1.8474 1.7025 -0.4034 0.0050  -0.1682 416 LEU A O   
2859  C CB  . LEU A 384 ? 2.9717 1.7478 1.7158 -0.3840 0.0334  -0.2238 416 LEU A CB  
2860  C CG  . LEU A 384 ? 3.0140 1.7040 1.7133 -0.3926 0.0400  -0.2586 416 LEU A CG  
2861  C CD1 . LEU A 384 ? 2.9712 1.6269 1.7224 -0.3656 0.0339  -0.2466 416 LEU A CD1 
2862  C CD2 . LEU A 384 ? 3.1170 1.7471 1.7275 -0.3931 0.0670  -0.2880 416 LEU A CD2 
2863  N N   . PRO A 385 ? 3.0183 1.9261 1.7325 -0.3911 0.0464  -0.1892 417 PRO A N   
2864  C CA  . PRO A 385 ? 2.9843 1.9662 1.7382 -0.3822 0.0402  -0.1543 417 PRO A CA  
2865  C C   . PRO A 385 ? 2.9071 1.9140 1.7466 -0.3507 0.0292  -0.1202 417 PRO A C   
2866  O O   . PRO A 385 ? 2.9148 1.8813 1.7645 -0.3228 0.0418  -0.1203 417 PRO A O   
2867  C CB  . PRO A 385 ? 3.0773 2.0390 1.7691 -0.3766 0.0683  -0.1652 417 PRO A CB  
2868  C CG  . PRO A 385 ? 3.1487 2.0386 1.7592 -0.3934 0.0858  -0.2076 417 PRO A CG  
2869  C CD  . PRO A 385 ? 3.1138 1.9578 1.7488 -0.3890 0.0751  -0.2186 417 PRO A CD  
2870  N N   . CYS A 386 ? 2.7580 1.8317 1.6601 -0.3550 0.0053  -0.0909 418 CYS A N   
2871  C CA  . CYS A 386 ? 2.6918 1.7914 1.6759 -0.3275 -0.0058 -0.0578 418 CYS A CA  
2872  C C   . CYS A 386 ? 2.6259 1.7970 1.6402 -0.3214 -0.0110 -0.0238 418 CYS A C   
2873  O O   . CYS A 386 ? 2.6084 1.8303 1.6176 -0.3436 -0.0241 -0.0153 418 CYS A O   
2874  C CB  . CYS A 386 ? 2.6721 1.7822 1.7128 -0.3352 -0.0299 -0.0514 418 CYS A CB  
2875  S SG  . CYS A 386 ? 2.8640 1.8861 1.8725 -0.3429 -0.0246 -0.0904 418 CYS A SG  
2876  N N   . ARG A 387 ? 2.5715 1.7451 1.6151 -0.2920 -0.0006 -0.0051 419 ARG A N   
2877  C CA  . ARG A 387 ? 2.5466 1.7818 1.6242 -0.2821 -0.0039 0.0287  419 ARG A CA  
2878  C C   . ARG A 387 ? 2.4619 1.7289 1.6273 -0.2650 -0.0232 0.0606  419 ARG A C   
2879  O O   . ARG A 387 ? 2.4321 1.6652 1.6289 -0.2552 -0.0282 0.0555  419 ARG A O   
2880  C CB  . ARG A 387 ? 2.5985 1.8195 1.6478 -0.2633 0.0226  0.0271  419 ARG A CB  
2881  C CG  . ARG A 387 ? 2.7459 2.0292 1.7925 -0.2710 0.0214  0.0506  419 ARG A CG  
2882  C CD  . ARG A 387 ? 3.0389 2.3157 2.0033 -0.2950 0.0368  0.0287  419 ARG A CD  
2883  N NE  . ARG A 387 ? 3.2102 2.4402 2.1296 -0.2810 0.0680  0.0080  419 ARG A NE  
2884  C CZ  . ARG A 387 ? 3.2394 2.4879 2.1578 -0.2680 0.0847  0.0202  419 ARG A CZ  
2885  N NH1 . ARG A 387 ? 3.3275 2.5317 2.2070 -0.2551 0.1137  -0.0010 419 ARG A NH1 
2886  N NH2 . ARG A 387 ? 3.1732 2.4839 2.1293 -0.2682 0.0726  0.0532  419 ARG A NH2 
2887  N N   . ILE A 388 ? 2.2162 1.5466 1.4191 -0.2627 -0.0340 0.0936  420 ILE A N   
2888  C CA  . ILE A 388 ? 2.1480 1.5127 1.4329 -0.2479 -0.0519 0.1259  420 ILE A CA  
2889  C C   . ILE A 388 ? 2.1340 1.5312 1.4488 -0.2255 -0.0439 0.1547  420 ILE A C   
2890  O O   . ILE A 388 ? 2.1660 1.5933 1.4505 -0.2321 -0.0372 0.1621  420 ILE A O   
2891  C CB  . ILE A 388 ? 2.1198 1.5363 1.4337 -0.2692 -0.0791 0.1418  420 ILE A CB  
2892  C CG1 . ILE A 388 ? 2.1277 1.5147 1.4204 -0.2913 -0.0874 0.1133  420 ILE A CG1 
2893  C CG2 . ILE A 388 ? 2.0516 1.4997 1.4490 -0.2536 -0.0957 0.1743  420 ILE A CG2 
2894  C CD1 . ILE A 388 ? 2.0963 1.5340 1.4259 -0.3091 -0.1139 0.1286  420 ILE A CD1 
2895  N N   . LYS A 389 ? 2.1247 1.5109 1.4936 -0.1997 -0.0423 0.1682  421 LYS A N   
2896  C CA  . LYS A 389 ? 2.1097 1.5257 1.5143 -0.1773 -0.0349 0.1954  421 LYS A CA  
2897  C C   . LYS A 389 ? 2.0334 1.4855 1.5171 -0.1690 -0.0553 0.2278  421 LYS A C   
2898  O O   . LYS A 389 ? 1.9950 1.4255 1.5121 -0.1678 -0.0662 0.2242  421 LYS A O   
2899  C CB  . LYS A 389 ? 2.1408 1.5109 1.5377 -0.1515 -0.0111 0.1817  421 LYS A CB  
2900  C CG  . LYS A 389 ? 2.1385 1.5406 1.5628 -0.1304 0.0007  0.2054  421 LYS A CG  
2901  C CD  . LYS A 389 ? 2.1757 1.5361 1.5923 -0.1048 0.0246  0.1905  421 LYS A CD  
2902  C CE  . LYS A 389 ? 2.1451 1.4639 1.5987 -0.0886 0.0192  0.1849  421 LYS A CE  
2903  N NZ  . LYS A 389 ? 2.1998 1.4785 1.6469 -0.0627 0.0408  0.1706  421 LYS A NZ  
2904  N N   . GLN A 390 ? 2.1065 1.6119 1.6178 -0.1646 -0.0598 0.2590  422 GLN A N   
2905  C CA  . GLN A 390 ? 2.0403 1.5838 1.6245 -0.1569 -0.0779 0.2925  422 GLN A CA  
2906  C C   . GLN A 390 ? 2.0196 1.5624 1.6491 -0.1286 -0.0668 0.3100  422 GLN A C   
2907  O O   . GLN A 390 ? 1.9680 1.5129 1.6563 -0.1187 -0.0772 0.3254  422 GLN A O   
2908  C CB  . GLN A 390 ? 2.0310 1.6348 1.6195 -0.1721 -0.0939 0.3181  422 GLN A CB  
2909  C CG  . GLN A 390 ? 2.0357 1.6479 1.5993 -0.2001 -0.1120 0.3057  422 GLN A CG  
2910  C CD  . GLN A 390 ? 2.0346 1.7053 1.5969 -0.2158 -0.1291 0.3300  422 GLN A CD  
2911  O OE1 . GLN A 390 ? 2.0582 1.7538 1.6031 -0.2128 -0.1212 0.3452  422 GLN A OE1 
2912  N NE2 . GLN A 390 ? 2.0102 1.7021 1.5901 -0.2332 -0.1529 0.3328  422 GLN A NE2 
2913  N N   . ILE A 391 ? 2.0207 1.5628 1.6248 -0.1165 -0.0456 0.3080  423 ILE A N   
2914  C CA  . ILE A 391 ? 2.0098 1.5530 1.6524 -0.0897 -0.0325 0.3219  423 ILE A CA  
2915  C C   . ILE A 391 ? 2.0312 1.5156 1.6648 -0.0729 -0.0173 0.2955  423 ILE A C   
2916  O O   . ILE A 391 ? 2.0894 1.5432 1.6697 -0.0721 0.0010  0.2698  423 ILE A O   
2917  C CB  . ILE A 391 ? 2.0467 1.6212 1.6682 -0.0860 -0.0167 0.3326  423 ILE A CB  
2918  C CG1 . ILE A 391 ? 2.0363 1.6638 1.6551 -0.1055 -0.0328 0.3564  423 ILE A CG1 
2919  C CG2 . ILE A 391 ? 2.0311 1.6143 1.6992 -0.0595 -0.0047 0.3492  423 ILE A CG2 
2920  C CD1 . ILE A 391 ? 2.0807 1.7346 1.6665 -0.1075 -0.0172 0.3636  423 ILE A CD1 
2921  N N   . ILE A 392 ? 2.0482 1.5150 1.7326 -0.0598 -0.0249 0.3018  424 ILE A N   
2922  C CA  . ILE A 392 ? 2.0565 1.4643 1.7335 -0.0452 -0.0147 0.2778  424 ILE A CA  
2923  C C   . ILE A 392 ? 2.0245 1.4339 1.7517 -0.0171 -0.0063 0.2930  424 ILE A C   
2924  O O   . ILE A 392 ? 1.9840 1.4371 1.7610 -0.0108 -0.0120 0.3232  424 ILE A O   
2925  C CB  . ILE A 392 ? 2.0373 1.4102 1.7212 -0.0575 -0.0310 0.2653  424 ILE A CB  
2926  C CG1 . ILE A 392 ? 1.9710 1.3702 1.7272 -0.0544 -0.0485 0.2941  424 ILE A CG1 
2927  C CG2 . ILE A 392 ? 2.0676 1.4422 1.7044 -0.0862 -0.0397 0.2496  424 ILE A CG2 
2928  C CD1 . ILE A 392 ? 1.9485 1.3107 1.7185 -0.0645 -0.0623 0.2822  424 ILE A CD1 
2929  N N   . ASN A 393 ? 2.2025 1.5614 1.9156 -0.0005 0.0068  0.2710  425 ASN A N   
2930  C CA  . ASN A 393 ? 2.2577 1.6081 2.0136 0.0274  0.0153  0.2791  425 ASN A CA  
2931  C C   . ASN A 393 ? 2.3333 1.6179 2.0816 0.0352  0.0139  0.2562  425 ASN A C   
2932  O O   . ASN A 393 ? 2.4125 1.6600 2.1399 0.0525  0.0289  0.2372  425 ASN A O   
2933  C CB  . ASN A 393 ? 2.3450 1.7074 2.0863 0.0449  0.0387  0.2757  425 ASN A CB  
2934  C CG  . ASN A 393 ? 2.3934 1.8199 2.1562 0.0426  0.0409  0.3032  425 ASN A CG  
2935  O OD1 . ASN A 393 ? 2.4082 1.8693 2.2213 0.0415  0.0273  0.3312  425 ASN A OD1 
2936  N ND2 . ASN A 393 ? 2.5363 1.9770 2.2603 0.0416  0.0590  0.2953  425 ASN A ND2 
2937  N N   . MET A 394 ? 2.8133 2.0825 2.5792 0.0217  -0.0047 0.2580  426 MET A N   
2938  C CA  . MET A 394 ? 2.8960 2.1002 2.6497 0.0235  -0.0085 0.2361  426 MET A CA  
2939  C C   . MET A 394 ? 2.8935 2.0798 2.6916 0.0500  -0.0057 0.2446  426 MET A C   
2940  O O   . MET A 394 ? 2.8568 2.0854 2.7031 0.0645  -0.0032 0.2699  426 MET A O   
2941  C CB  . MET A 394 ? 2.8109 2.0109 2.5756 -0.0008 -0.0288 0.2378  426 MET A CB  
2942  C CG  . MET A 394 ? 2.8094 1.9451 2.5643 -0.0056 -0.0360 0.2175  426 MET A CG  
2943  S SD  . MET A 394 ? 2.8858 2.0137 2.6049 -0.0420 -0.0493 0.2004  426 MET A SD  
2944  C CE  . MET A 394 ? 2.6176 1.8263 2.3958 -0.0529 -0.0645 0.2375  426 MET A CE  
2945  N N   . TRP A 395 ? 3.0391 2.1604 2.8183 0.0554  -0.0063 0.2226  427 TRP A N   
2946  C CA  . TRP A 395 ? 3.0173 2.1113 2.8315 0.0793  -0.0057 0.2266  427 TRP A CA  
2947  C C   . TRP A 395 ? 3.0627 2.1729 2.8860 0.1073  0.0122  0.2295  427 TRP A C   
2948  O O   . TRP A 395 ? 3.0800 2.1965 2.9514 0.1273  0.0117  0.2442  427 TRP A O   
2949  C CB  . TRP A 395 ? 2.9046 2.0238 2.7851 0.0768  -0.0213 0.2549  427 TRP A CB  
2950  C CG  . TRP A 395 ? 2.8770 1.9678 2.7513 0.0525  -0.0374 0.2477  427 TRP A CG  
2951  C CD1 . TRP A 395 ? 2.8983 1.9207 2.7410 0.0462  -0.0421 0.2231  427 TRP A CD1 
2952  C CD2 . TRP A 395 ? 2.8087 1.9379 2.7078 0.0301  -0.0507 0.2640  427 TRP A CD2 
2953  N NE1 . TRP A 395 ? 2.8791 1.8958 2.7260 0.0199  -0.0566 0.2222  427 TRP A NE1 
2954  C CE2 . TRP A 395 ? 2.8051 1.8878 2.6884 0.0104  -0.0623 0.2472  427 TRP A CE2 
2955  C CE3 . TRP A 395 ? 2.7021 1.8995 2.6353 0.0248  -0.0541 0.2913  427 TRP A CE3 
2956  C CZ2 . TRP A 395 ? 2.7528 1.8576 2.6570 -0.0137 -0.0765 0.2559  427 TRP A CZ2 
2957  C CZ3 . TRP A 395 ? 2.6454 1.8633 2.5984 0.0022  -0.0693 0.3011  427 TRP A CZ3 
2958  C CH2 . TRP A 395 ? 2.6794 1.8525 2.6197 -0.0166 -0.0801 0.2832  427 TRP A CH2 
2959  N N   . GLN A 396 ? 2.8861 2.0037 2.6648 0.1084  0.0287  0.2151  428 GLN A N   
2960  C CA  . GLN A 396 ? 2.9585 2.0914 2.7436 0.1337  0.0481  0.2147  428 GLN A CA  
2961  C C   . GLN A 396 ? 2.9193 2.1148 2.7689 0.1440  0.0474  0.2475  428 GLN A C   
2962  O O   . GLN A 396 ? 2.9317 2.1341 2.8138 0.1688  0.0565  0.2529  428 GLN A O   
2963  C CB  . GLN A 396 ? 3.0340 2.1092 2.8161 0.1579  0.0529  0.1968  428 GLN A CB  
2964  C CG  . GLN A 396 ? 3.1275 2.1381 2.8435 0.1582  0.0618  0.1619  428 GLN A CG  
2965  C CD  . GLN A 396 ? 3.2671 2.2668 2.9780 0.1873  0.0822  0.1494  428 GLN A CD  
2966  O OE1 . GLN A 396 ? 3.2876 2.2905 3.0456 0.2118  0.0818  0.1597  428 GLN A OE1 
2967  N NE2 . GLN A 396 ? 3.3598 2.3457 3.0146 0.1845  0.1001  0.1268  428 GLN A NE2 
2968  N N   . ARG A 397 ? 2.7367 1.9786 2.6052 0.1250  0.0369  0.2695  429 ARG A N   
2969  C CA  . ARG A 397 ? 2.6884 1.9875 2.6162 0.1323  0.0353  0.3016  429 ARG A CA  
2970  C C   . ARG A 397 ? 2.7480 2.0973 2.6610 0.1298  0.0497  0.3088  429 ARG A C   
2971  O O   . ARG A 397 ? 2.7255 2.0855 2.5977 0.1093  0.0487  0.3035  429 ARG A O   
2972  C CB  . ARG A 397 ? 2.5173 1.8342 2.4813 0.1147  0.0142  0.3237  429 ARG A CB  
2973  C CG  . ARG A 397 ? 2.4644 1.7316 2.4472 0.1172  0.0015  0.3179  429 ARG A CG  
2974  C CD  . ARG A 397 ? 2.3166 1.6032 2.3434 0.1020  -0.0169 0.3410  429 ARG A CD  
2975  N NE  . ARG A 397 ? 2.2441 1.5895 2.3234 0.1094  -0.0153 0.3729  429 ARG A NE  
2976  C CZ  . ARG A 397 ? 2.2547 1.6512 2.3440 0.0960  -0.0191 0.3930  429 ARG A CZ  
2977  N NH1 . ARG A 397 ? 2.2316 1.6305 2.2841 0.0746  -0.0258 0.3845  429 ARG A NH1 
2978  N NH2 . ARG A 397 ? 2.2713 1.7162 2.4067 0.1037  -0.0167 0.4215  429 ARG A NH2 
2979  N N   . ILE A 398 ? 2.7142 2.0948 2.6603 0.1493  0.0627  0.3210  430 ILE A N   
2980  C CA  . ILE A 398 ? 2.7435 2.1734 2.6810 0.1475  0.0774  0.3300  430 ILE A CA  
2981  C C   . ILE A 398 ? 2.6890 2.1717 2.6848 0.1486  0.0708  0.3647  430 ILE A C   
2982  O O   . ILE A 398 ? 2.7153 2.1977 2.7607 0.1647  0.0681  0.3758  430 ILE A O   
2983  C CB  . ILE A 398 ? 2.8595 2.2804 2.7795 0.1680  0.1023  0.3105  430 ILE A CB  
2984  C CG1 . ILE A 398 ? 2.8582 2.2194 2.7211 0.1679  0.1082  0.2756  430 ILE A CG1 
2985  C CG2 . ILE A 398 ? 2.8665 2.3357 2.7707 0.1611  0.1181  0.3178  430 ILE A CG2 
2986  C CD1 . ILE A 398 ? 2.8635 2.1714 2.7399 0.1870  0.1039  0.2617  430 ILE A CD1 
2987  N N   . GLY A 399 ? 2.4462 1.9730 2.4343 0.1309  0.0681  0.3820  431 GLY A N   
2988  C CA  . GLY A 399 ? 2.3478 1.9247 2.3844 0.1288  0.0615  0.4159  431 GLY A CA  
2989  C C   . GLY A 399 ? 2.3077 1.8990 2.3496 0.1061  0.0394  0.4334  431 GLY A C   
2990  O O   . GLY A 399 ? 2.2726 1.9094 2.3341 0.0980  0.0349  0.4597  431 GLY A O   
2991  N N   . GLN A 400 ? 2.3244 1.8765 2.3499 0.0958  0.0255  0.4187  432 GLN A N   
2992  C CA  . GLN A 400 ? 2.2142 1.7751 2.2466 0.0744  0.0040  0.4310  432 GLN A CA  
2993  C C   . GLN A 400 ? 2.1854 1.7248 2.1572 0.0555  0.0005  0.4075  432 GLN A C   
2994  O O   . GLN A 400 ? 2.2319 1.7217 2.1783 0.0546  -0.0005 0.3818  432 GLN A O   
2995  C CB  . GLN A 400 ? 2.2353 1.7699 2.3107 0.0775  -0.0096 0.4356  432 GLN A CB  
2996  C CG  . GLN A 400 ? 2.1865 1.7553 2.3045 0.0654  -0.0263 0.4648  432 GLN A CG  
2997  C CD  . GLN A 400 ? 2.2010 1.8191 2.3546 0.0753  -0.0187 0.4935  432 GLN A CD  
2998  O OE1 . GLN A 400 ? 2.1910 1.8501 2.3406 0.0647  -0.0220 0.5113  432 GLN A OE1 
2999  N NE2 . GLN A 400 ? 2.2003 1.8144 2.3877 0.0953  -0.0086 0.4978  432 GLN A NE2 
3000  N N   . ALA A 401 ? 2.0312 1.6066 1.9775 0.0398  -0.0012 0.4162  433 ALA A N   
3001  C CA  . ALA A 401 ? 2.0866 1.6504 1.9758 0.0190  -0.0055 0.3972  433 ALA A CA  
3002  C C   . ALA A 401 ? 2.0470 1.6351 1.9524 -0.0017 -0.0292 0.4143  433 ALA A C   
3003  O O   . ALA A 401 ? 2.0057 1.6390 1.9439 -0.0040 -0.0370 0.4440  433 ALA A O   
3004  C CB  . ALA A 401 ? 2.1558 1.7407 1.9977 0.0147  0.0105  0.3920  433 ALA A CB  
3005  N N   . MET A 402 ? 2.0496 1.6067 1.9339 -0.0162 -0.0404 0.3951  434 MET A N   
3006  C CA  . MET A 402 ? 2.0140 1.5903 1.9154 -0.0359 -0.0631 0.4068  434 MET A CA  
3007  C C   . MET A 402 ? 2.0734 1.6626 1.9223 -0.0586 -0.0689 0.3963  434 MET A C   
3008  O O   . MET A 402 ? 2.1413 1.6965 1.9360 -0.0655 -0.0605 0.3664  434 MET A O   
3009  C CB  . MET A 402 ? 1.9750 1.5098 1.8948 -0.0395 -0.0735 0.3930  434 MET A CB  
3010  C CG  . MET A 402 ? 1.9342 1.4929 1.8844 -0.0576 -0.0961 0.4075  434 MET A CG  
3011  S SD  . MET A 402 ? 1.9370 1.4428 1.8866 -0.0705 -0.1065 0.3812  434 MET A SD  
3012  C CE  . MET A 402 ? 1.9497 1.4795 1.8677 -0.0997 -0.1226 0.3736  434 MET A CE  
3013  N N   . TYR A 403 ? 1.8808 1.5185 1.7457 -0.0703 -0.0835 0.4214  435 TYR A N   
3014  C CA  . TYR A 403 ? 1.9298 1.5867 1.7530 -0.0936 -0.0940 0.4163  435 TYR A CA  
3015  C C   . TYR A 403 ? 1.8964 1.5504 1.7409 -0.1095 -0.1161 0.4136  435 TYR A C   
3016  O O   . TYR A 403 ? 1.8334 1.5170 1.7309 -0.1100 -0.1323 0.4394  435 TYR A O   
3017  C CB  . TYR A 403 ? 1.9352 1.6460 1.7589 -0.0983 -0.0985 0.4448  435 TYR A CB  
3018  C CG  . TYR A 403 ? 1.9840 1.7146 1.7663 -0.1235 -0.1124 0.4403  435 TYR A CG  
3019  C CD1 . TYR A 403 ? 2.0690 1.7903 1.7828 -0.1344 -0.1001 0.4193  435 TYR A CD1 
3020  C CD2 . TYR A 403 ? 1.9584 1.7176 1.7717 -0.1367 -0.1380 0.4567  435 TYR A CD2 
3021  C CE1 . TYR A 403 ? 2.1134 1.8538 1.7890 -0.1588 -0.1136 0.4154  435 TYR A CE1 
3022  C CE2 . TYR A 403 ? 2.0169 1.7963 1.7953 -0.1594 -0.1524 0.4529  435 TYR A CE2 
3023  C CZ  . TYR A 403 ? 2.0722 1.8426 1.7810 -0.1709 -0.1406 0.4325  435 TYR A CZ  
3024  O OH  . TYR A 403 ? 2.1080 1.9000 1.7819 -0.1948 -0.1557 0.4292  435 TYR A OH  
3025  N N   . ALA A 404 ? 1.8713 1.4890 1.6755 -0.1224 -0.1159 0.3820  436 ALA A N   
3026  C CA  . ALA A 404 ? 1.8503 1.4647 1.6719 -0.1396 -0.1355 0.3758  436 ALA A CA  
3027  C C   . ALA A 404 ? 1.8586 1.5235 1.6757 -0.1581 -0.1536 0.3914  436 ALA A C   
3028  O O   . ALA A 404 ? 1.9073 1.5806 1.6689 -0.1700 -0.1497 0.3811  436 ALA A O   
3029  C CB  . ALA A 404 ? 1.8828 1.4440 1.6565 -0.1502 -0.1293 0.3362  436 ALA A CB  
3030  N N   . PRO A 405 ? 1.8794 1.5781 1.7522 -0.1613 -0.1736 0.4160  437 PRO A N   
3031  C CA  . PRO A 405 ? 1.8945 1.6419 1.7654 -0.1777 -0.1930 0.4322  437 PRO A CA  
3032  C C   . PRO A 405 ? 1.9464 1.6841 1.7754 -0.2017 -0.2017 0.4041  437 PRO A C   
3033  O O   . PRO A 405 ? 1.9401 1.6394 1.7672 -0.2077 -0.2005 0.3780  437 PRO A O   
3034  C CB  . PRO A 405 ? 1.8132 1.5886 1.7600 -0.1732 -0.2109 0.4610  437 PRO A CB  
3035  C CG  . PRO A 405 ? 1.7643 1.4963 1.7422 -0.1646 -0.2039 0.4473  437 PRO A CG  
3036  C CD  . PRO A 405 ? 1.7957 1.4880 1.7360 -0.1505 -0.1794 0.4298  437 PRO A CD  
3037  N N   . PRO A 406 ? 1.9791 1.7500 1.7717 -0.2171 -0.2104 0.4081  438 PRO A N   
3038  C CA  . PRO A 406 ? 2.0111 1.7770 1.7617 -0.2418 -0.2189 0.3816  438 PRO A CA  
3039  C C   . PRO A 406 ? 1.9648 1.7382 1.7633 -0.2522 -0.2396 0.3794  438 PRO A C   
3040  O O   . PRO A 406 ? 1.9151 1.7156 1.7784 -0.2441 -0.2533 0.4064  438 PRO A O   
3041  C CB  . PRO A 406 ? 2.0171 1.8283 1.7343 -0.2542 -0.2282 0.3971  438 PRO A CB  
3042  C CG  . PRO A 406 ? 2.0386 1.8599 1.7563 -0.2358 -0.2143 0.4201  438 PRO A CG  
3043  C CD  . PRO A 406 ? 1.9885 1.8013 1.7726 -0.2139 -0.2119 0.4364  438 PRO A CD  
3044  N N   . ILE A 407 ? 2.0844 1.8328 1.8500 -0.2710 -0.2407 0.3461  439 ILE A N   
3045  C CA  . ILE A 407 ? 2.0373 1.7893 1.8423 -0.2841 -0.2581 0.3375  439 ILE A CA  
3046  C C   . ILE A 407 ? 2.0174 1.8033 1.7952 -0.3093 -0.2755 0.3294  439 ILE A C   
3047  O O   . ILE A 407 ? 2.0693 1.8411 1.7787 -0.3233 -0.2669 0.3057  439 ILE A O   
3048  C CB  . ILE A 407 ? 2.0312 1.7215 1.8254 -0.2865 -0.2449 0.3032  439 ILE A CB  
3049  C CG1 . ILE A 407 ? 2.0573 1.7116 1.8671 -0.2613 -0.2264 0.3096  439 ILE A CG1 
3050  C CG2 . ILE A 407 ? 1.9772 1.6716 1.8209 -0.2992 -0.2616 0.2966  439 ILE A CG2 
3051  C CD1 . ILE A 407 ? 1.9860 1.6664 1.8735 -0.2448 -0.2351 0.3445  439 ILE A CD1 
3052  N N   . GLN A 408 ? 2.2781 2.1089 2.1104 -0.3149 -0.3000 0.3489  440 GLN A N   
3053  C CA  . GLN A 408 ? 2.3030 2.1731 2.1205 -0.3378 -0.3205 0.3446  440 GLN A CA  
3054  C C   . GLN A 408 ? 2.2695 2.1109 2.0638 -0.3595 -0.3198 0.3038  440 GLN A C   
3055  O O   . GLN A 408 ? 2.2541 2.0612 2.0775 -0.3578 -0.3144 0.2881  440 GLN A O   
3056  C CB  . GLN A 408 ? 2.2597 2.1849 2.1486 -0.3349 -0.3474 0.3780  440 GLN A CB  
3057  C CG  . GLN A 408 ? 2.2704 2.2169 2.1968 -0.3114 -0.3475 0.4190  440 GLN A CG  
3058  C CD  . GLN A 408 ? 2.2597 2.1818 2.2466 -0.2930 -0.3393 0.4271  440 GLN A CD  
3059  O OE1 . GLN A 408 ? 2.2769 2.1493 2.2538 -0.2915 -0.3223 0.4011  440 GLN A OE1 
3060  N NE2 . GLN A 408 ? 2.2770 2.2322 2.3247 -0.2794 -0.3513 0.4635  440 GLN A NE2 
3061  N N   . GLY A 409 ? 2.3064 2.1613 2.0459 -0.3816 -0.3248 0.2862  441 GLY A N   
3062  C CA  . GLY A 409 ? 2.2650 2.0989 1.9786 -0.4055 -0.3254 0.2475  441 GLY A CA  
3063  C C   . GLY A 409 ? 2.2591 2.0251 1.9100 -0.4083 -0.2981 0.2110  441 GLY A C   
3064  O O   . GLY A 409 ? 2.2525 1.9822 1.8902 -0.3889 -0.2781 0.2142  441 GLY A O   
3065  N N   . VAL A 410 ? 2.2763 2.0254 1.8871 -0.4334 -0.2976 0.1751  442 VAL A N   
3066  C CA  . VAL A 410 ? 2.3440 2.0257 1.8912 -0.4394 -0.2730 0.1371  442 VAL A CA  
3067  C C   . VAL A 410 ? 2.3254 1.9594 1.9115 -0.4279 -0.2647 0.1278  442 VAL A C   
3068  O O   . VAL A 410 ? 2.2874 1.9334 1.9298 -0.4342 -0.2787 0.1276  442 VAL A O   
3069  C CB  . VAL A 410 ? 2.4066 2.0854 1.9000 -0.4717 -0.2755 0.1016  442 VAL A CB  
3070  C CG1 . VAL A 410 ? 2.4596 2.0635 1.8900 -0.4783 -0.2503 0.0614  442 VAL A CG1 
3071  C CG2 . VAL A 410 ? 2.4181 2.1404 1.8662 -0.4839 -0.2822 0.1108  442 VAL A CG2 
3072  N N   . ILE A 411 ? 2.2004 1.7801 1.7577 -0.4113 -0.2419 0.1203  443 ILE A N   
3073  C CA  . ILE A 411 ? 2.1703 1.7002 1.7586 -0.3993 -0.2332 0.1127  443 ILE A CA  
3074  C C   . ILE A 411 ? 2.2101 1.6767 1.7406 -0.4176 -0.2196 0.0674  443 ILE A C   
3075  O O   . ILE A 411 ? 2.2669 1.7034 1.7235 -0.4228 -0.2036 0.0464  443 ILE A O   
3076  C CB  . ILE A 411 ? 2.1619 1.6707 1.7570 -0.3687 -0.2178 0.1329  443 ILE A CB  
3077  C CG1 . ILE A 411 ? 2.1335 1.7045 1.7731 -0.3527 -0.2292 0.1765  443 ILE A CG1 
3078  C CG2 . ILE A 411 ? 2.1279 1.5902 1.7608 -0.3567 -0.2120 0.1287  443 ILE A CG2 
3079  C CD1 . ILE A 411 ? 2.1249 1.6811 1.7752 -0.3235 -0.2142 0.1970  443 ILE A CD1 
3080  N N   . ARG A 412 ? 2.5052 1.9494 2.0678 -0.4283 -0.2250 0.0516  444 ARG A N   
3081  C CA  . ARG A 412 ? 2.5010 1.8803 2.0114 -0.4464 -0.2124 0.0085  444 ARG A CA  
3082  C C   . ARG A 412 ? 2.5017 1.8275 2.0437 -0.4353 -0.2058 0.0043  444 ARG A C   
3083  O O   . ARG A 412 ? 2.4459 1.7949 2.0621 -0.4277 -0.2176 0.0261  444 ARG A O   
3084  C CB  . ARG A 412 ? 2.5553 1.9572 2.0631 -0.4791 -0.2257 -0.0148 444 ARG A CB  
3085  C CG  . ARG A 412 ? 2.6713 2.0087 2.1169 -0.5024 -0.2124 -0.0618 444 ARG A CG  
3086  C CD  . ARG A 412 ? 2.7171 2.0773 2.1861 -0.5322 -0.2270 -0.0818 444 ARG A CD  
3087  N NE  . ARG A 412 ? 2.7347 2.0574 2.2460 -0.5348 -0.2268 -0.0920 444 ARG A NE  
3088  C CZ  . ARG A 412 ? 2.7815 2.1072 2.3136 -0.5607 -0.2350 -0.1149 444 ARG A CZ  
3089  N NH1 . ARG A 412 ? 2.7925 2.1591 2.3085 -0.5855 -0.2448 -0.1302 444 ARG A NH1 
3090  N NH2 . ARG A 412 ? 2.7794 2.0675 2.3484 -0.5627 -0.2330 -0.1231 444 ARG A NH2 
3091  N N   . CYS A 413 ? 2.5951 1.8481 2.0790 -0.4343 -0.1867 -0.0230 445 CYS A N   
3092  C CA  . CYS A 413 ? 2.5971 1.7885 2.0964 -0.4261 -0.1793 -0.0316 445 CYS A CA  
3093  C C   . CYS A 413 ? 2.6523 1.7646 2.0769 -0.4417 -0.1638 -0.0750 445 CYS A C   
3094  O O   . CYS A 413 ? 2.6874 1.7770 2.0402 -0.4441 -0.1505 -0.0926 445 CYS A O   
3095  C CB  . CYS A 413 ? 2.6001 1.7885 2.1298 -0.3918 -0.1732 -0.0006 445 CYS A CB  
3096  S SG  . CYS A 413 ? 2.7530 1.9182 2.2159 -0.3715 -0.1531 -0.0015 445 CYS A SG  
3097  N N   . VAL A 414 ? 2.7099 1.7793 2.1517 -0.4530 -0.1651 -0.0919 446 VAL A N   
3098  C CA  . VAL A 414 ? 2.7425 1.7299 2.1196 -0.4687 -0.1518 -0.1325 446 VAL A CA  
3099  C C   . VAL A 414 ? 2.7475 1.6757 2.1424 -0.4499 -0.1456 -0.1273 446 VAL A C   
3100  O O   . VAL A 414 ? 2.7203 1.6604 2.1830 -0.4472 -0.1555 -0.1109 446 VAL A O   
3101  C CB  . VAL A 414 ? 2.7610 1.7468 2.1349 -0.5052 -0.1591 -0.1623 446 VAL A CB  
3102  C CG1 . VAL A 414 ? 2.7133 1.7395 2.0445 -0.5254 -0.1610 -0.1764 446 VAL A CG1 
3103  C CG2 . VAL A 414 ? 2.7597 1.7930 2.2260 -0.5085 -0.1768 -0.1415 446 VAL A CG2 
3104  N N   . SER A 415 ? 2.8239 1.6903 2.1600 -0.4361 -0.1296 -0.1399 447 SER A N   
3105  C CA  . SER A 415 ? 2.7823 1.6267 2.1502 -0.4040 -0.1209 -0.1298 447 SER A CA  
3106  C C   . SER A 415 ? 2.7401 1.5759 2.0834 -0.3897 -0.1019 -0.1572 447 SER A C   
3107  O O   . SER A 415 ? 2.7655 1.5983 2.0589 -0.4052 -0.0947 -0.1829 447 SER A O   
3108  C CB  . SER A 415 ? 2.7891 1.6140 2.1477 -0.3795 -0.1175 -0.1054 447 SER A CB  
3109  O OG  . SER A 415 ? 2.7612 1.5724 2.1729 -0.3574 -0.1198 -0.0841 447 SER A OG  
3110  N N   . ASN A 416 ? 2.7448 1.5820 2.1277 -0.3603 -0.0952 -0.1490 448 ASN A N   
3111  C CA  . ASN A 416 ? 2.7065 1.5381 2.0757 -0.3452 -0.0811 -0.1677 448 ASN A CA  
3112  C C   . ASN A 416 ? 2.7533 1.5357 2.0821 -0.3234 -0.0720 -0.1643 448 ASN A C   
3113  O O   . ASN A 416 ? 2.7374 1.5156 2.1018 -0.3040 -0.0755 -0.1421 448 ASN A O   
3114  C CB  . ASN A 416 ? 2.6274 1.5075 2.0792 -0.3320 -0.0823 -0.1618 448 ASN A CB  
3115  C CG  . ASN A 416 ? 2.5970 1.5206 2.0762 -0.3504 -0.0853 -0.1753 448 ASN A CG  
3116  O OD1 . ASN A 416 ? 2.6381 1.5568 2.0710 -0.3718 -0.0850 -0.1923 448 ASN A OD1 
3117  N ND2 . ASN A 416 ? 2.5822 1.5513 2.1401 -0.3419 -0.0874 -0.1674 448 ASN A ND2 
3118  N N   . ILE A 417 ? 2.6812 1.4295 1.9394 -0.3252 -0.0597 -0.1854 449 ILE A N   
3119  C CA  . ILE A 417 ? 2.7308 1.4342 1.9515 -0.3025 -0.0489 -0.1862 449 ILE A CA  
3120  C C   . ILE A 417 ? 2.7239 1.4448 1.9836 -0.2821 -0.0456 -0.1870 449 ILE A C   
3121  O O   . ILE A 417 ? 2.7520 1.4808 1.9954 -0.2874 -0.0395 -0.2040 449 ILE A O   
3122  C CB  . ILE A 417 ? 2.7831 1.4453 1.9138 -0.3131 -0.0356 -0.2079 449 ILE A CB  
3123  C CG1 . ILE A 417 ? 2.8092 1.4582 1.8994 -0.3373 -0.0396 -0.2086 449 ILE A CG1 
3124  C CG2 . ILE A 417 ? 2.8038 1.4207 1.9010 -0.2873 -0.0237 -0.2086 449 ILE A CG2 
3125  C CD1 . ILE A 417 ? 2.8969 1.5100 1.8976 -0.3484 -0.0244 -0.2311 449 ILE A CD1 
3126  N N   . THR A 418 ? 2.6713 1.4011 1.9845 -0.2598 -0.0500 -0.1675 450 THR A N   
3127  C CA  . THR A 418 ? 2.6103 1.3644 1.9692 -0.2434 -0.0492 -0.1664 450 THR A CA  
3128  C C   . THR A 418 ? 2.6700 1.3916 2.0131 -0.2185 -0.0434 -0.1633 450 THR A C   
3129  O O   . THR A 418 ? 2.6956 1.4385 2.0811 -0.2052 -0.0446 -0.1595 450 THR A O   
3130  C CB  . THR A 418 ? 2.5240 1.3300 1.9711 -0.2396 -0.0582 -0.1481 450 THR A CB  
3131  O OG1 . THR A 418 ? 2.5067 1.3055 1.9778 -0.2267 -0.0624 -0.1250 450 THR A OG1 
3132  C CG2 . THR A 418 ? 2.4985 1.3398 1.9675 -0.2628 -0.0638 -0.1520 450 THR A CG2 
3133  N N   . GLY A 419 ? 2.6828 1.3549 1.9680 -0.2119 -0.0368 -0.1655 451 GLY A N   
3134  C CA  . GLY A 419 ? 2.7046 1.3477 1.9792 -0.1864 -0.0311 -0.1634 451 GLY A CA  
3135  C C   . GLY A 419 ? 2.7708 1.3606 1.9877 -0.1765 -0.0222 -0.1642 451 GLY A C   
3136  O O   . GLY A 419 ? 2.7841 1.3604 1.9765 -0.1885 -0.0220 -0.1613 451 GLY A O   
3137  N N   . LEU A 420 ? 2.5439 1.1030 1.7390 -0.1548 -0.0142 -0.1685 452 LEU A N   
3138  C CA  . LEU A 420 ? 2.6175 1.1253 1.7585 -0.1411 -0.0022 -0.1716 452 LEU A CA  
3139  C C   . LEU A 420 ? 2.6668 1.1668 1.8436 -0.1081 -0.0025 -0.1562 452 LEU A C   
3140  O O   . LEU A 420 ? 2.6990 1.2276 1.9295 -0.0971 -0.0104 -0.1488 452 LEU A O   
3141  C CB  . LEU A 420 ? 2.6762 1.1496 1.7428 -0.1473 0.0122  -0.1969 452 LEU A CB  
3142  C CG  . LEU A 420 ? 2.6847 1.1747 1.7228 -0.1791 0.0127  -0.2126 452 LEU A CG  
3143  C CD1 . LEU A 420 ? 2.8605 1.3214 1.8314 -0.1838 0.0278  -0.2346 452 LEU A CD1 
3144  C CD2 . LEU A 420 ? 2.7068 1.1986 1.7285 -0.2002 0.0108  -0.2107 452 LEU A CD2 
3145  N N   . ILE A 421 ? 2.5515 1.0135 1.6978 -0.0927 0.0073  -0.1522 453 ILE A N   
3146  C CA  . ILE A 421 ? 2.5934 1.0430 1.7649 -0.0585 0.0106  -0.1399 453 ILE A CA  
3147  C C   . ILE A 421 ? 2.7383 1.1344 1.8389 -0.0456 0.0300  -0.1592 453 ILE A C   
3148  O O   . ILE A 421 ? 2.8343 1.1969 1.8887 -0.0446 0.0433  -0.1624 453 ILE A O   
3149  C CB  . ILE A 421 ? 2.5505 1.0105 1.7631 -0.0461 0.0065  -0.1126 453 ILE A CB  
3150  C CG1 . ILE A 421 ? 2.4333 0.9501 1.7187 -0.0595 -0.0113 -0.0931 453 ILE A CG1 
3151  C CG2 . ILE A 421 ? 2.6049 1.0584 1.8481 -0.0094 0.0107  -0.1000 453 ILE A CG2 
3152  C CD1 . ILE A 421 ? 2.3981 0.9329 1.7318 -0.0469 -0.0165 -0.0617 453 ILE A CD1 
3153  N N   . LEU A 422 ? 2.6435 1.0314 1.7352 -0.0361 0.0327  -0.1718 454 LEU A N   
3154  C CA  . LEU A 422 ? 2.7708 1.1123 1.7977 -0.0254 0.0514  -0.1915 454 LEU A CA  
3155  C C   . LEU A 422 ? 2.8077 1.1342 1.8578 0.0113  0.0561  -0.1849 454 LEU A C   
3156  O O   . LEU A 422 ? 2.7569 1.1127 1.8740 0.0264  0.0424  -0.1685 454 LEU A O   
3157  C CB  . LEU A 422 ? 2.8595 1.1970 1.8500 -0.0421 0.0534  -0.2116 454 LEU A CB  
3158  C CG  . LEU A 422 ? 2.8518 1.2075 1.8190 -0.0778 0.0503  -0.2207 454 LEU A CG  
3159  C CD1 . LEU A 422 ? 2.9972 1.3489 1.9329 -0.0889 0.0539  -0.2375 454 LEU A CD1 
3160  C CD2 . LEU A 422 ? 2.8591 1.1912 1.7700 -0.0918 0.0637  -0.2293 454 LEU A CD2 
3161  N N   . THR A 423 ? 2.9115 1.1950 1.9064 0.0248  0.0768  -0.1990 455 THR A N   
3162  C CA  . THR A 423 ? 3.0159 1.2808 2.0232 0.0604  0.0854  -0.1978 455 THR A CA  
3163  C C   . THR A 423 ? 3.1754 1.4036 2.1193 0.0607  0.1017  -0.2229 455 THR A C   
3164  O O   . THR A 423 ? 3.2335 1.4428 2.1134 0.0384  0.1146  -0.2403 455 THR A O   
3165  C CB  . THR A 423 ? 2.9878 1.2396 1.9998 0.0834  0.0988  -0.1868 455 THR A CB  
3166  O OG1 . THR A 423 ? 3.0870 1.3074 2.0273 0.0679  0.1190  -0.2020 455 THR A OG1 
3167  C CG2 . THR A 423 ? 2.9218 1.2131 2.0041 0.0860  0.0817  -0.1576 455 THR A CG2 
3168  N N   . ARG A 424 ? 3.3032 1.5241 2.2677 0.0852  0.1008  -0.2241 456 ARG A N   
3169  C CA  . ARG A 424 ? 3.4261 1.6140 2.3406 0.0887  0.1140  -0.2449 456 ARG A CA  
3170  C C   . ARG A 424 ? 3.5777 1.7352 2.4762 0.1201  0.1352  -0.2514 456 ARG A C   
3171  O O   . ARG A 424 ? 3.5843 1.7524 2.5321 0.1475  0.1334  -0.2368 456 ARG A O   
3172  C CB  . ARG A 424 ? 3.3572 1.5568 2.3037 0.0912  0.0972  -0.2430 456 ARG A CB  
3173  C CG  . ARG A 424 ? 3.5014 1.6686 2.3957 0.0891  0.1078  -0.2627 456 ARG A CG  
3174  C CD  . ARG A 424 ? 3.5090 1.6909 2.4318 0.0838  0.0894  -0.2593 456 ARG A CD  
3175  N NE  . ARG A 424 ? 3.4135 1.6133 2.4050 0.1084  0.0752  -0.2437 456 ARG A NE  
3176  C CZ  . ARG A 424 ? 3.4876 1.6677 2.4902 0.1354  0.0776  -0.2462 456 ARG A CZ  
3177  N NH1 . ARG A 424 ? 3.6502 1.7900 2.5994 0.1427  0.0941  -0.2640 456 ARG A NH1 
3178  N NH2 . ARG A 424 ? 3.5005 1.7032 2.5704 0.1545  0.0635  -0.2308 456 ARG A NH2 
3179  N N   . ASP A 425 ? 3.5657 1.6893 2.3978 0.1157  0.1566  -0.2732 457 ASP A N   
3180  C CA  . ASP A 425 ? 3.6988 1.7946 2.5117 0.1438  0.1808  -0.2828 457 ASP A CA  
3181  C C   . ASP A 425 ? 3.7905 1.8800 2.6388 0.1731  0.1750  -0.2820 457 ASP A C   
3182  O O   . ASP A 425 ? 3.7188 1.8179 2.5896 0.1672  0.1553  -0.2785 457 ASP A O   
3183  C CB  . ASP A 425 ? 3.7941 1.8605 2.5248 0.1258  0.2066  -0.3068 457 ASP A CB  
3184  C CG  . ASP A 425 ? 3.7222 1.7952 2.4162 0.0969  0.2139  -0.3092 457 ASP A CG  
3185  O OD1 . ASP A 425 ? 3.7680 1.8343 2.4513 0.1069  0.2319  -0.3096 457 ASP A OD1 
3186  O OD2 . ASP A 425 ? 3.6510 1.7377 2.3284 0.0640  0.2019  -0.3108 457 ASP A OD2 
3187  N N   . GLY A 426 ? 3.8553 1.9295 2.7087 0.2049  0.1934  -0.2862 458 GLY A N   
3188  C CA  . GLY A 426 ? 3.9616 2.0299 2.8512 0.2353  0.1892  -0.2863 458 GLY A CA  
3189  C C   . GLY A 426 ? 4.1985 2.2292 3.0349 0.2396  0.2088  -0.3093 458 GLY A C   
3190  O O   . GLY A 426 ? 4.2927 2.3137 3.1515 0.2605  0.2039  -0.3118 458 GLY A O   
3191  N N   . GLY A 427 ? 4.3753 2.3861 3.1418 0.2185  0.2309  -0.3259 459 GLY A N   
3192  C CA  . GLY A 427 ? 4.4978 2.4751 3.2088 0.2175  0.2516  -0.3478 459 GLY A CA  
3193  C C   . GLY A 427 ? 4.5949 2.5620 3.2964 0.2051  0.2352  -0.3513 459 GLY A C   
3194  O O   . GLY A 427 ? 4.5202 2.4953 3.1982 0.1728  0.2244  -0.3506 459 GLY A O   
3195  N N   . SER A 428 ? 4.5347 2.4853 3.2562 0.2307  0.2333  -0.3548 460 SER A N   
3196  C CA  . SER A 428 ? 4.5681 2.5087 3.2863 0.2217  0.2161  -0.3560 460 SER A CA  
3197  C C   . SER A 428 ? 4.7349 2.6431 3.4473 0.2466  0.2248  -0.3679 460 SER A C   
3198  O O   . SER A 428 ? 4.7844 2.6919 3.5355 0.2801  0.2300  -0.3666 460 SER A O   
3199  C CB  . SER A 428 ? 4.4157 2.3878 3.1998 0.2234  0.1843  -0.3354 460 SER A CB  
3200  O OG  . SER A 428 ? 4.2517 2.2568 3.0584 0.2094  0.1758  -0.3217 460 SER A OG  
3201  N N   . THR A 429 ? 4.6077 2.4896 3.2743 0.2320  0.2272  -0.3796 461 THR A N   
3202  C CA  . THR A 429 ? 4.5873 2.4689 3.2048 0.1932  0.2244  -0.3832 461 THR A CA  
3203  C C   . THR A 429 ? 4.4767 2.3941 3.1287 0.1731  0.1973  -0.3660 461 THR A C   
3204  O O   . THR A 429 ? 4.4302 2.3684 3.0668 0.1468  0.1974  -0.3632 461 THR A O   
3205  C CB  . THR A 429 ? 4.5845 2.4610 3.1439 0.1732  0.2513  -0.3958 461 THR A CB  
3206  O OG1 . THR A 429 ? 4.6892 2.5355 3.2208 0.1921  0.2777  -0.4118 461 THR A OG1 
3207  C CG2 . THR A 429 ? 4.5394 2.4128 3.0472 0.1363  0.2519  -0.4021 461 THR A CG2 
3208  N N   . ASN A 430 ? 4.7131 2.6403 3.4156 0.1858  0.1744  -0.3544 462 ASN A N   
3209  C CA  . ASN A 430 ? 4.4561 2.4214 3.1994 0.1694  0.1503  -0.3376 462 ASN A CA  
3210  C C   . ASN A 430 ? 4.4469 2.4133 3.1648 0.1407  0.1398  -0.3391 462 ASN A C   
3211  O O   . ASN A 430 ? 4.3436 2.3387 3.0637 0.1143  0.1314  -0.3327 462 ASN A O   
3212  C CB  . ASN A 430 ? 4.3979 2.3808 3.2150 0.1956  0.1315  -0.3226 462 ASN A CB  
3213  C CG  . ASN A 430 ? 4.2547 2.2817 3.1209 0.1802  0.1089  -0.3043 462 ASN A CG  
3214  O OD1 . ASN A 430 ? 4.1313 2.1811 2.9950 0.1624  0.1099  -0.2996 462 ASN A OD1 
3215  N ND2 . ASN A 430 ? 4.2162 2.2558 3.1293 0.1874  0.0891  -0.2938 462 ASN A ND2 
3216  N N   . SER A 431 ? 4.4653 2.4013 3.1602 0.1460  0.1407  -0.3473 463 SER A N   
3217  C CA  . SER A 431 ? 4.4443 2.3782 3.1157 0.1222  0.1315  -0.3483 463 SER A CA  
3218  C C   . SER A 431 ? 4.4857 2.4109 3.0935 0.0933  0.1474  -0.3600 463 SER A C   
3219  O O   . SER A 431 ? 4.4965 2.4184 3.0813 0.0739  0.1425  -0.3617 463 SER A O   
3220  C CB  . SER A 431 ? 4.4722 2.3735 3.1410 0.1395  0.1269  -0.3523 463 SER A CB  
3221  O OG  . SER A 431 ? 4.3871 2.3009 3.1187 0.1628  0.1099  -0.3403 463 SER A OG  
3222  N N   . THR A 432 ? 4.2335 2.1562 2.8131 0.0893  0.1666  -0.3676 464 THR A N   
3223  C CA  . THR A 432 ? 4.1903 2.1072 2.7114 0.0607  0.1824  -0.3786 464 THR A CA  
3224  C C   . THR A 432 ? 4.0833 2.0404 2.6140 0.0340  0.1766  -0.3715 464 THR A C   
3225  O O   . THR A 432 ? 4.0215 2.0015 2.5610 0.0125  0.1630  -0.3656 464 THR A O   
3226  C CB  . THR A 432 ? 4.2858 2.1737 2.7637 0.0698  0.2100  -0.3936 464 THR A CB  
3227  O OG1 . THR A 432 ? 4.2628 2.1684 2.7579 0.0761  0.2165  -0.3905 464 THR A OG1 
3228  C CG2 . THR A 432 ? 4.3846 2.2359 2.8651 0.1022  0.2157  -0.4000 464 THR A CG2 
3229  N N   . THR A 433 ? 4.1652 2.1310 2.6941 0.0355  0.1876  -0.3725 465 THR A N   
3230  C CA  . THR A 433 ? 4.0153 2.0163 2.5507 0.0108  0.1832  -0.3668 465 THR A CA  
3231  C C   . THR A 433 ? 3.9369 1.9576 2.5230 0.0285  0.1743  -0.3543 465 THR A C   
3232  O O   . THR A 433 ? 4.0171 2.0219 2.6220 0.0587  0.1788  -0.3533 465 THR A O   
3233  C CB  . THR A 433 ? 4.0141 2.0087 2.4928 -0.0104 0.2057  -0.3801 465 THR A CB  
3234  O OG1 . THR A 433 ? 3.8555 1.8850 2.3443 -0.0330 0.1999  -0.3741 465 THR A OG1 
3235  C CG2 . THR A 433 ? 4.0472 2.0146 2.5043 0.0113  0.2281  -0.3896 465 THR A CG2 
3236  N N   . GLU A 434 ? 3.9689 2.0256 2.5797 0.0100  0.1620  -0.3443 466 GLU A N   
3237  C CA  . GLU A 434 ? 3.8328 1.9111 2.4930 0.0232  0.1526  -0.3305 466 GLU A CA  
3238  C C   . GLU A 434 ? 3.7331 1.8292 2.3752 0.0004  0.1588  -0.3311 466 GLU A C   
3239  O O   . GLU A 434 ? 3.7012 1.8136 2.3225 -0.0297 0.1569  -0.3348 466 GLU A O   
3240  C CB  . GLU A 434 ? 3.7170 1.8263 2.4404 0.0252  0.1264  -0.3141 466 GLU A CB  
3241  C CG  . GLU A 434 ? 3.8182 1.9126 2.5641 0.0469  0.1178  -0.3123 466 GLU A CG  
3242  C CD  . GLU A 434 ? 3.9039 1.9826 2.6774 0.0829  0.1215  -0.3088 466 GLU A CD  
3243  O OE1 . GLU A 434 ? 3.8559 1.9411 2.6426 0.0930  0.1279  -0.3042 466 GLU A OE1 
3244  O OE2 . GLU A 434 ? 4.0282 2.0885 2.8116 0.1017  0.1180  -0.3105 466 GLU A OE2 
3245  N N   . THR A 435 ? 3.7314 1.8251 2.3830 0.0152  0.1665  -0.3274 467 THR A N   
3246  C CA  . THR A 435 ? 3.6681 1.7748 2.3011 -0.0042 0.1731  -0.3279 467 THR A CA  
3247  C C   . THR A 435 ? 3.5295 1.6647 2.2217 0.0014  0.1551  -0.3084 467 THR A C   
3248  O O   . THR A 435 ? 3.5198 1.6547 2.2575 0.0306  0.1496  -0.2968 467 THR A O   
3249  C CB  . THR A 435 ? 3.7794 1.8584 2.3669 0.0056  0.2005  -0.3406 467 THR A CB  
3250  O OG1 . THR A 435 ? 3.9568 2.0115 2.4923 -0.0002 0.2175  -0.3580 467 THR A OG1 
3251  C CG2 . THR A 435 ? 3.7353 1.8273 2.2969 -0.0181 0.2077  -0.3427 467 THR A CG2 
3252  N N   . PHE A 436 ? 3.5238 1.6860 2.2185 -0.0267 0.1461  -0.3044 468 PHE A N   
3253  C CA  . PHE A 436 ? 3.3812 1.5730 2.1309 -0.0266 0.1287  -0.2856 468 PHE A CA  
3254  C C   . PHE A 436 ? 3.3966 1.5879 2.1182 -0.0422 0.1380  -0.2874 468 PHE A C   
3255  O O   . PHE A 436 ? 3.4384 1.6284 2.1084 -0.0696 0.1476  -0.3017 468 PHE A O   
3256  C CB  . PHE A 436 ? 3.2966 1.5253 2.0842 -0.0457 0.1071  -0.2778 468 PHE A CB  
3257  C CG  . PHE A 436 ? 3.3106 1.5414 2.1280 -0.0314 0.0971  -0.2749 468 PHE A CG  
3258  C CD1 . PHE A 436 ? 3.2652 1.5125 2.1474 -0.0095 0.0824  -0.2582 468 PHE A CD1 
3259  C CD2 . PHE A 436 ? 3.4347 1.6509 2.2149 -0.0402 0.1028  -0.2884 468 PHE A CD2 
3260  C CE1 . PHE A 436 ? 3.2997 1.5490 2.2074 0.0017  0.0731  -0.2564 468 PHE A CE1 
3261  C CE2 . PHE A 436 ? 3.5000 1.7148 2.3039 -0.0279 0.0935  -0.2859 468 PHE A CE2 
3262  C CZ  . PHE A 436 ? 3.4228 1.6539 2.2895 -0.0074 0.0785  -0.2705 468 PHE A CZ  
3263  N N   . ARG A 437 ? 3.3709 1.5651 2.1278 -0.0252 0.1348  -0.2721 469 ARG A N   
3264  C CA  . ARG A 437 ? 3.3594 1.5495 2.0934 -0.0366 0.1428  -0.2711 469 ARG A CA  
3265  C C   . ARG A 437 ? 3.2326 1.4519 2.0289 -0.0385 0.1218  -0.2467 469 ARG A C   
3266  O O   . ARG A 437 ? 3.1612 1.4011 2.0237 -0.0193 0.1059  -0.2285 469 ARG A O   
3267  C CB  . ARG A 437 ? 3.4147 1.5714 2.1211 -0.0108 0.1674  -0.2767 469 ARG A CB  
3268  C CG  . ARG A 437 ? 3.5394 1.6694 2.1878 -0.0076 0.1904  -0.3002 469 ARG A CG  
3269  C CD  . ARG A 437 ? 3.6419 1.7451 2.2751 0.0224  0.2155  -0.3051 469 ARG A CD  
3270  N NE  . ARG A 437 ? 3.8506 1.9312 2.4384 0.0279  0.2362  -0.3257 469 ARG A NE  
3271  C CZ  . ARG A 437 ? 3.9721 2.0422 2.4911 0.0080  0.2595  -0.3463 469 ARG A CZ  
3272  N NH1 . ARG A 437 ? 3.9046 1.9881 2.3913 -0.0194 0.2639  -0.3499 469 ARG A NH1 
3273  N NH2 . ARG A 437 ? 4.1219 2.1729 2.6067 0.0141  0.2775  -0.3624 469 ARG A NH2 
3274  N N   . PRO A 438 ? 3.2177 1.4423 1.9954 -0.0629 0.1207  -0.2454 470 PRO A N   
3275  C CA  . PRO A 438 ? 3.0626 1.3246 1.9069 -0.0654 0.1002  -0.2180 470 PRO A CA  
3276  C C   . PRO A 438 ? 3.0195 1.3331 1.9359 -0.0307 0.1008  -0.1876 470 PRO A C   
3277  O O   . PRO A 438 ? 3.0368 1.3792 1.9491 -0.0158 0.1185  -0.1853 470 PRO A O   
3278  C CB  . PRO A 438 ? 2.9567 1.2822 1.7951 -0.0987 0.0976  -0.2149 470 PRO A CB  
3279  C CG  . PRO A 438 ? 3.1046 1.4274 1.8803 -0.1024 0.1216  -0.2337 470 PRO A CG  
3280  C CD  . PRO A 438 ? 3.2537 1.4814 1.9659 -0.0915 0.1351  -0.2639 470 PRO A CD  
3281  N N   . GLY A 439 ? 3.0811 1.4055 2.0631 -0.0192 0.0822  -0.1651 471 GLY A N   
3282  C CA  . GLY A 439 ? 3.0337 1.4074 2.0879 0.0121  0.0811  -0.1357 471 GLY A CA  
3283  C C   . GLY A 439 ? 2.9051 1.3414 2.0344 0.0050  0.0610  -0.1040 471 GLY A C   
3284  O O   . GLY A 439 ? 2.8617 1.3220 1.9899 -0.0250 0.0504  -0.1027 471 GLY A O   
3285  N N   . GLY A 440 ? 2.8248 1.2889 2.0208 0.0326  0.0560  -0.0786 472 GLY A N   
3286  C CA  . GLY A 440 ? 2.7303 1.2521 1.9987 0.0275  0.0384  -0.0476 472 GLY A CA  
3287  C C   . GLY A 440 ? 2.7026 1.2757 2.0373 0.0581  0.0411  -0.0195 472 GLY A C   
3288  O O   . GLY A 440 ? 2.7258 1.2673 2.0777 0.0857  0.0425  -0.0185 472 GLY A O   
3289  N N   . GLY A 441 ? 3.0222 1.6746 2.3937 0.0529  0.0416  0.0033  473 GLY A N   
3290  C CA  . GLY A 441 ? 2.9920 1.7008 2.4260 0.0779  0.0451  0.0308  473 GLY A CA  
3291  C C   . GLY A 441 ? 2.9203 1.6438 2.4235 0.0840  0.0266  0.0563  473 GLY A C   
3292  O O   . GLY A 441 ? 2.8750 1.6582 2.4243 0.0735  0.0172  0.0814  473 GLY A O   
3293  N N   . ASP A 442 ? 2.9815 1.6498 2.4918 0.1009  0.0214  0.0506  474 ASP A N   
3294  C CA  . ASP A 442 ? 2.9193 1.5941 2.4915 0.1059  0.0043  0.0733  474 ASP A CA  
3295  C C   . ASP A 442 ? 2.8722 1.5358 2.4427 0.0737  -0.0127 0.0731  474 ASP A C   
3296  O O   . ASP A 442 ? 2.8991 1.5080 2.4266 0.0585  -0.0167 0.0484  474 ASP A O   
3297  C CB  . ASP A 442 ? 2.9584 1.5717 2.5313 0.1308  0.0024  0.0651  474 ASP A CB  
3298  C CG  . ASP A 442 ? 2.8809 1.5548 2.5462 0.1394  -0.0108 0.0909  474 ASP A CG  
3299  O OD1 . ASP A 442 ? 2.8440 1.5498 2.5432 0.1443  -0.0118 0.1197  474 ASP A OD1 
3300  O OD2 . ASP A 442 ? 2.8572 1.5540 2.5635 0.1395  -0.0183 0.0829  474 ASP A OD2 
3301  N N   . MET A 443 ? 2.8397 1.5662 2.4626 0.0624  -0.0219 0.0996  475 MET A N   
3302  C CA  . MET A 443 ? 2.7559 1.4797 2.3849 0.0320  -0.0372 0.1007  475 MET A CA  
3303  C C   . MET A 443 ? 2.6572 1.4034 2.3454 0.0306  -0.0461 0.1001  475 MET A C   
3304  O O   . MET A 443 ? 2.5532 1.3286 2.2641 0.0063  -0.0530 0.0951  475 MET A O   
3305  C CB  . MET A 443 ? 2.6624 1.4678 2.3404 0.0207  -0.0427 0.1285  475 MET A CB  
3306  C CG  . MET A 443 ? 2.6381 1.4964 2.2972 0.0201  -0.0307 0.1306  475 MET A CG  
3307  S SD  . MET A 443 ? 2.9579 1.7795 2.5293 -0.0048 -0.0238 0.0938  475 MET A SD  
3308  C CE  . MET A 443 ? 2.9708 1.8619 2.5307 -0.0028 -0.0100 0.1031  475 MET A CE  
3309  N N   . ARG A 444 ? 2.6149 1.3757 2.3414 0.0554  -0.0421 0.1039  476 ARG A N   
3310  C CA  . ARG A 444 ? 2.4277 1.2361 2.2201 0.0528  -0.0439 0.1029  476 ARG A CA  
3311  C C   . ARG A 444 ? 2.4431 1.2320 2.2031 0.0360  -0.0443 0.0716  476 ARG A C   
3312  O O   . ARG A 444 ? 2.3807 1.2073 2.1820 0.0235  -0.0445 0.0683  476 ARG A O   
3313  C CB  . ARG A 444 ? 2.3947 1.2150 2.2255 0.0819  -0.0392 0.1126  476 ARG A CB  
3314  C CG  . ARG A 444 ? 2.4326 1.2855 2.3077 0.0990  -0.0379 0.1451  476 ARG A CG  
3315  C CD  . ARG A 444 ? 2.5317 1.3891 2.4357 0.1283  -0.0336 0.1498  476 ARG A CD  
3316  N NE  . ARG A 444 ? 2.6603 1.5490 2.6040 0.1466  -0.0321 0.1798  476 ARG A NE  
3317  C CZ  . ARG A 444 ? 2.7693 1.6330 2.6893 0.1739  -0.0287 0.1837  476 ARG A CZ  
3318  N NH1 . ARG A 444 ? 2.8013 1.6070 2.6568 0.1871  -0.0190 0.1594  476 ARG A NH1 
3319  N NH2 . ARG A 444 ? 2.8067 1.7043 2.7628 0.1895  -0.0286 0.2110  476 ARG A NH2 
3320  N N   . ASP A 445 ? 2.5700 1.3004 2.2524 0.0357  -0.0408 0.0486  477 ASP A N   
3321  C CA  . ASP A 445 ? 2.6128 1.3235 2.2570 0.0196  -0.0405 0.0191  477 ASP A CA  
3322  C C   . ASP A 445 ? 2.5249 1.2569 2.1696 -0.0114 -0.0461 0.0137  477 ASP A C   
3323  O O   . ASP A 445 ? 2.4993 1.2470 2.1508 -0.0258 -0.0477 -0.0021 477 ASP A O   
3324  C CB  . ASP A 445 ? 2.7868 1.4308 2.3439 0.0259  -0.0311 -0.0034 477 ASP A CB  
3325  C CG  . ASP A 445 ? 2.8582 1.4796 2.4132 0.0592  -0.0231 0.0001  477 ASP A CG  
3326  O OD1 . ASP A 445 ? 2.7951 1.4465 2.4072 0.0739  -0.0270 0.0086  477 ASP A OD1 
3327  O OD2 . ASP A 445 ? 2.9251 1.4987 2.4205 0.0703  -0.0108 -0.0065 477 ASP A OD2 
3328  N N   . ASN A 446 ? 2.5804 1.3143 2.2190 -0.0214 -0.0492 0.0277  478 ASN A N   
3329  C CA  . ASN A 446 ? 2.5164 1.2702 2.1561 -0.0506 -0.0552 0.0234  478 ASN A CA  
3330  C C   . ASN A 446 ? 2.3738 1.1920 2.0916 -0.0577 -0.0574 0.0315  478 ASN A C   
3331  O O   . ASN A 446 ? 2.3363 1.1721 2.0559 -0.0793 -0.0592 0.0178  478 ASN A O   
3332  C CB  . ASN A 446 ? 2.5402 1.2880 2.1684 -0.0573 -0.0597 0.0437  478 ASN A CB  
3333  C CG  . ASN A 446 ? 2.6930 1.3747 2.2369 -0.0534 -0.0524 0.0356  478 ASN A CG  
3334  O OD1 . ASN A 446 ? 2.7448 1.3882 2.2492 -0.0371 -0.0420 0.0193  478 ASN A OD1 
3335  N ND2 . ASN A 446 ? 2.7497 1.4340 2.2744 -0.0672 -0.0554 0.0480  478 ASN A ND2 
3336  N N   . TRP A 447 ? 2.3450 1.1991 2.1253 -0.0398 -0.0537 0.0523  479 TRP A N   
3337  C CA  . TRP A 447 ? 2.2953 1.2071 2.1421 -0.0457 -0.0476 0.0593  479 TRP A CA  
3338  C C   . TRP A 447 ? 2.2608 1.1762 2.1123 -0.0461 -0.0433 0.0398  479 TRP A C   
3339  O O   . TRP A 447 ? 2.2063 1.1582 2.0904 -0.0582 -0.0376 0.0347  479 TRP A O   
3340  C CB  . TRP A 447 ? 2.2942 1.2407 2.1946 -0.0275 -0.0391 0.0888  479 TRP A CB  
3341  C CG  . TRP A 447 ? 2.3285 1.2619 2.2172 -0.0185 -0.0455 0.1104  479 TRP A CG  
3342  C CD1 . TRP A 447 ? 2.3601 1.2832 2.2533 0.0062  -0.0442 0.1270  479 TRP A CD1 
3343  C CD2 . TRP A 447 ? 2.2918 1.2191 2.1595 -0.0341 -0.0554 0.1177  479 TRP A CD2 
3344  N NE1 . TRP A 447 ? 2.3451 1.2580 2.2219 0.0077  -0.0520 0.1455  479 TRP A NE1 
3345  C CE2 . TRP A 447 ? 2.3213 1.2358 2.1815 -0.0179 -0.0598 0.1410  479 TRP A CE2 
3346  C CE3 . TRP A 447 ? 2.2385 1.1723 2.0950 -0.0604 -0.0614 0.1077  479 TRP A CE3 
3347  C CZ2 . TRP A 447 ? 2.3759 1.2836 2.2165 -0.0288 -0.0713 0.1568  479 TRP A CZ2 
3348  C CZ3 . TRP A 447 ? 2.2677 1.1942 2.1063 -0.0716 -0.0731 0.1220  479 TRP A CZ3 
3349  C CH2 . TRP A 447 ? 2.3583 1.2718 2.1885 -0.0567 -0.0786 0.1474  479 TRP A CH2 
3350  N N   . ARG A 448 ? 2.2416 1.1180 2.0579 -0.0324 -0.0451 0.0289  480 ARG A N   
3351  C CA  . ARG A 448 ? 2.2767 1.1512 2.0927 -0.0307 -0.0430 0.0129  480 ARG A CA  
3352  C C   . ARG A 448 ? 2.2937 1.1612 2.0754 -0.0523 -0.0459 -0.0116 480 ARG A C   
3353  O O   . ARG A 448 ? 2.3239 1.1984 2.1098 -0.0560 -0.0456 -0.0219 480 ARG A O   
3354  C CB  . ARG A 448 ? 2.3657 1.1944 2.1446 -0.0097 -0.0439 0.0077  480 ARG A CB  
3355  C CG  . ARG A 448 ? 2.3657 1.2080 2.1865 0.0136  -0.0406 0.0320  480 ARG A CG  
3356  C CD  . ARG A 448 ? 2.4826 1.2863 2.2780 0.0374  -0.0402 0.0268  480 ARG A CD  
3357  N NE  . ARG A 448 ? 2.4854 1.3083 2.3262 0.0598  -0.0370 0.0514  480 ARG A NE  
3358  C CZ  . ARG A 448 ? 2.5897 1.3826 2.4135 0.0848  -0.0362 0.0528  480 ARG A CZ  
3359  N NH1 . ARG A 448 ? 2.6950 1.4340 2.4532 0.0909  -0.0353 0.0305  480 ARG A NH1 
3360  N NH2 . ARG A 448 ? 2.5812 1.3991 2.4522 0.1045  -0.0334 0.0762  480 ARG A NH2 
3361  N N   . SER A 449 ? 2.4008 1.2487 2.1398 -0.0672 -0.0499 -0.0201 481 SER A N   
3362  C CA  . SER A 449 ? 2.4460 1.2884 2.1498 -0.0881 -0.0515 -0.0430 481 SER A CA  
3363  C C   . SER A 449 ? 2.3837 1.2803 2.1411 -0.1036 -0.0503 -0.0413 481 SER A C   
3364  O O   . SER A 449 ? 2.4320 1.3234 2.1592 -0.1201 -0.0532 -0.0589 481 SER A O   
3365  C CB  . SER A 449 ? 2.4864 1.2893 2.1245 -0.0996 -0.0537 -0.0523 481 SER A CB  
3366  O OG  . SER A 449 ? 2.4135 1.2356 2.0771 -0.1061 -0.0571 -0.0345 481 SER A OG  
3367  N N   . GLU A 450 ? 2.3195 1.2558 2.1380 -0.0987 -0.0463 -0.0201 482 GLU A N   
3368  C CA  . GLU A 450 ? 2.2826 1.2459 2.1215 -0.1131 -0.0484 -0.0167 482 GLU A CA  
3369  C C   . GLU A 450 ? 2.2279 1.2008 2.0889 -0.1049 -0.0482 -0.0046 482 GLU A C   
3370  O O   . GLU A 450 ? 2.2001 1.1850 2.0638 -0.1168 -0.0517 -0.0071 482 GLU A O   
3371  C CB  . GLU A 450 ? 2.2265 1.2248 2.1053 -0.1193 -0.0429 -0.0029 482 GLU A CB  
3372  C CG  . GLU A 450 ? 2.2444 1.2170 2.0783 -0.1328 -0.0510 -0.0138 482 GLU A CG  
3373  C CD  . GLU A 450 ? 2.3165 1.2917 2.1290 -0.1511 -0.0530 -0.0391 482 GLU A CD  
3374  O OE1 . GLU A 450 ? 2.3481 1.3376 2.1699 -0.1591 -0.0549 -0.0421 482 GLU A OE1 
3375  O OE2 . GLU A 450 ? 2.3425 1.2786 2.0912 -0.1607 -0.0587 -0.0545 482 GLU A OE2 
3376  N N   . LEU A 451 ? 2.1178 1.0859 1.9940 -0.0850 -0.0438 0.0082  483 LEU A N   
3377  C CA  . LEU A 451 ? 2.1033 1.0794 1.9984 -0.0762 -0.0429 0.0201  483 LEU A CA  
3378  C C   . LEU A 451 ? 2.1492 1.0901 2.0090 -0.0702 -0.0506 0.0083  483 LEU A C   
3379  O O   . LEU A 451 ? 2.1524 1.0934 2.0253 -0.0587 -0.0504 0.0180  483 LEU A O   
3380  C CB  . LEU A 451 ? 2.0392 1.0343 1.9726 -0.0573 -0.0310 0.0440  483 LEU A CB  
3381  C CG  . LEU A 451 ? 1.9763 1.0046 1.9371 -0.0616 -0.0213 0.0601  483 LEU A CG  
3382  C CD1 . LEU A 451 ? 1.9729 1.0119 1.9536 -0.0405 -0.0079 0.0839  483 LEU A CD1 
3383  C CD2 . LEU A 451 ? 1.9860 1.0347 1.9524 -0.0757 -0.0236 0.0609  483 LEU A CD2 
3384  N N   . TYR A 452 ? 2.1501 1.0594 1.9607 -0.0778 -0.0565 -0.0124 484 TYR A N   
3385  C CA  . TYR A 452 ? 2.2088 1.0801 1.9776 -0.0720 -0.0624 -0.0236 484 TYR A CA  
3386  C C   . TYR A 452 ? 2.2112 1.0803 1.9666 -0.0828 -0.0702 -0.0262 484 TYR A C   
3387  O O   . TYR A 452 ? 2.2525 1.0964 1.9857 -0.0758 -0.0754 -0.0284 484 TYR A O   
3388  C CB  . TYR A 452 ? 2.2568 1.0936 1.9695 -0.0775 -0.0631 -0.0444 484 TYR A CB  
3389  C CG  . TYR A 452 ? 2.2523 1.0882 1.9327 -0.1008 -0.0666 -0.0585 484 TYR A CG  
3390  C CD1 . TYR A 452 ? 2.2115 1.0727 1.9095 -0.1129 -0.0636 -0.0591 484 TYR A CD1 
3391  C CD2 . TYR A 452 ? 2.2921 1.1013 1.9243 -0.1104 -0.0722 -0.0703 484 TYR A CD2 
3392  C CE1 . TYR A 452 ? 2.2091 1.0716 1.8814 -0.1335 -0.0661 -0.0717 484 TYR A CE1 
3393  C CE2 . TYR A 452 ? 2.3119 1.1213 1.9158 -0.1310 -0.0735 -0.0819 484 TYR A CE2 
3394  C CZ  . TYR A 452 ? 2.2487 1.0857 1.8742 -0.1423 -0.0703 -0.0830 484 TYR A CZ  
3395  O OH  . TYR A 452 ? 2.2653 1.1037 1.8653 -0.1622 -0.0710 -0.0946 484 TYR A OH  
3396  N N   . LYS A 453 ? 2.1238 1.0183 1.8926 -0.0995 -0.0711 -0.0257 485 LYS A N   
3397  C CA  . LYS A 453 ? 2.0962 0.9905 1.8526 -0.1115 -0.0778 -0.0286 485 LYS A CA  
3398  C C   . LYS A 453 ? 2.0310 0.9606 1.8370 -0.1099 -0.0758 -0.0114 485 LYS A C   
3399  O O   . LYS A 453 ? 2.1207 1.0590 1.9252 -0.1223 -0.0799 -0.0130 485 LYS A O   
3400  C CB  . LYS A 453 ? 2.1314 1.0220 1.8565 -0.1320 -0.0798 -0.0437 485 LYS A CB  
3401  C CG  . LYS A 453 ? 2.0776 0.9995 1.8318 -0.1415 -0.0745 -0.0428 485 LYS A CG  
3402  C CD  . LYS A 453 ? 2.0987 1.0153 1.8204 -0.1618 -0.0771 -0.0580 485 LYS A CD  
3403  C CE  . LYS A 453 ? 2.0931 1.0375 1.8386 -0.1728 -0.0731 -0.0602 485 LYS A CE  
3404  N NZ  . LYS A 453 ? 2.0768 1.0156 1.7908 -0.1920 -0.0750 -0.0752 485 LYS A NZ  
3405  N N   . TYR A 454 ? 1.9812 0.9305 1.8280 -0.0950 -0.0683 0.0052  486 TYR A N   
3406  C CA  . TYR A 454 ? 1.9479 0.9287 1.8342 -0.0926 -0.0639 0.0222  486 TYR A CA  
3407  C C   . TYR A 454 ? 1.9914 0.9682 1.8922 -0.0727 -0.0611 0.0357  486 TYR A C   
3408  O O   . TYR A 454 ? 2.0050 0.9667 1.9036 -0.0579 -0.0574 0.0370  486 TYR A O   
3409  C CB  . TYR A 454 ? 1.8987 0.9148 1.8193 -0.0956 -0.0535 0.0330  486 TYR A CB  
3410  C CG  . TYR A 454 ? 1.8895 0.9163 1.8057 -0.1145 -0.0549 0.0221  486 TYR A CG  
3411  C CD1 . TYR A 454 ? 1.9628 1.0015 1.8799 -0.1288 -0.0588 0.0179  486 TYR A CD1 
3412  C CD2 . TYR A 454 ? 1.9276 0.9536 1.8400 -0.1180 -0.0521 0.0161  486 TYR A CD2 
3413  C CE1 . TYR A 454 ? 2.0052 1.0547 1.9211 -0.1452 -0.0590 0.0080  486 TYR A CE1 
3414  C CE2 . TYR A 454 ? 1.9406 0.9775 1.8501 -0.1355 -0.0535 0.0059  486 TYR A CE2 
3415  C CZ  . TYR A 454 ? 1.9815 1.0305 1.8939 -0.1485 -0.0565 0.0020  486 TYR A CZ  
3416  O OH  . TYR A 454 ? 2.0728 1.1332 1.9851 -0.1649 -0.0571 -0.0082 486 TYR A OH  
3417  N N   . LYS A 455 ? 1.9613 0.9517 1.8763 -0.0723 -0.0630 0.0455  487 LYS A N   
3418  C CA  . LYS A 455 ? 1.9546 0.9457 1.8845 -0.0543 -0.0602 0.0598  487 LYS A CA  
3419  C C   . LYS A 455 ? 1.9041 0.9229 1.8535 -0.0582 -0.0608 0.0722  487 LYS A C   
3420  O O   . LYS A 455 ? 1.8685 0.8975 1.8155 -0.0744 -0.0664 0.0669  487 LYS A O   
3421  C CB  . LYS A 455 ? 2.0315 0.9873 1.9369 -0.0459 -0.0696 0.0526  487 LYS A CB  
3422  C CG  . LYS A 455 ? 2.0066 0.9547 1.8986 -0.0539 -0.0817 0.0500  487 LYS A CG  
3423  C CD  . LYS A 455 ? 2.1282 1.0420 1.9997 -0.0405 -0.0892 0.0471  487 LYS A CD  
3424  C CE  . LYS A 455 ? 2.1126 1.0193 1.9750 -0.0451 -0.1015 0.0487  487 LYS A CE  
3425  N NZ  . LYS A 455 ? 2.1685 1.0418 2.0134 -0.0301 -0.1086 0.0475  487 LYS A NZ  
3426  N N   . VAL A 456 ? 1.8352 0.8655 1.8010 -0.0426 -0.0558 0.0883  488 VAL A N   
3427  C CA  . VAL A 456 ? 1.8143 0.8729 1.7968 -0.0439 -0.0591 0.1013  488 VAL A CA  
3428  C C   . VAL A 456 ? 1.8408 0.8882 1.8202 -0.0405 -0.0694 0.1022  488 VAL A C   
3429  O O   . VAL A 456 ? 2.0523 1.0764 2.0246 -0.0260 -0.0697 0.1025  488 VAL A O   
3430  C CB  . VAL A 456 ? 1.9621 1.0405 1.9586 -0.0293 -0.0526 0.1181  488 VAL A CB  
3431  C CG1 . VAL A 456 ? 1.9503 1.0635 1.9678 -0.0329 -0.0625 0.1299  488 VAL A CG1 
3432  C CG2 . VAL A 456 ? 1.9076 0.9932 1.9034 -0.0327 -0.0437 0.1176  488 VAL A CG2 
3433  N N   . VAL A 457 ? 1.8189 0.8826 1.8043 -0.0537 -0.0783 0.1025  489 VAL A N   
3434  C CA  . VAL A 457 ? 1.8321 0.8887 1.8160 -0.0531 -0.0897 0.1043  489 VAL A CA  
3435  C C   . VAL A 457 ? 1.7947 0.8879 1.8046 -0.0564 -0.0952 0.1166  489 VAL A C   
3436  O O   . VAL A 457 ? 1.7607 0.8837 1.7862 -0.0645 -0.0928 0.1202  489 VAL A O   
3437  C CB  . VAL A 457 ? 1.8597 0.8938 1.8195 -0.0680 -0.0989 0.0897  489 VAL A CB  
3438  C CG1 . VAL A 457 ? 1.9010 0.8983 1.8332 -0.0639 -0.0992 0.0773  489 VAL A CG1 
3439  C CG2 . VAL A 457 ? 1.8370 0.8907 1.7998 -0.0867 -0.0975 0.0842  489 VAL A CG2 
3440  N N   . LYS A 458 ? 1.8882 0.9807 1.9049 -0.0501 -0.1043 0.1232  490 LYS A N   
3441  C CA  . LYS A 458 ? 1.8834 1.0121 1.9288 -0.0534 -0.1122 0.1345  490 LYS A CA  
3442  C C   . LYS A 458 ? 1.7811 0.9050 1.8197 -0.0678 -0.1225 0.1288  490 LYS A C   
3443  O O   . LYS A 458 ? 1.7412 0.8324 1.7572 -0.0671 -0.1285 0.1221  490 LYS A O   
3444  C CB  . LYS A 458 ? 1.9783 1.1070 2.0361 -0.0362 -0.1166 0.1453  490 LYS A CB  
3445  C CG  . LYS A 458 ? 1.9954 1.1632 2.0894 -0.0277 -0.1194 0.1607  490 LYS A CG  
3446  C CD  . LYS A 458 ? 1.9961 1.1414 2.0857 -0.0104 -0.1226 0.1647  490 LYS A CD  
3447  C CE  . LYS A 458 ? 2.0366 1.2139 2.1604 0.0017  -0.1259 0.1795  490 LYS A CE  
3448  N NZ  . LYS A 458 ? 2.0482 1.2109 2.1639 0.0230  -0.1163 0.1833  490 LYS A NZ  
3449  N N   . ILE A 459 ? 1.7748 0.9317 1.8340 -0.0795 -0.1260 0.1326  491 ILE A N   
3450  C CA  . ILE A 459 ? 1.7825 0.9352 1.8343 -0.0931 -0.1345 0.1280  491 ILE A CA  
3451  C C   . ILE A 459 ? 1.7950 0.9630 1.8680 -0.0888 -0.1457 0.1388  491 ILE A C   
3452  O O   . ILE A 459 ? 1.7724 0.9788 1.8810 -0.0845 -0.1467 0.1505  491 ILE A O   
3453  C CB  . ILE A 459 ? 1.7491 0.9251 1.8091 -0.1082 -0.1306 0.1246  491 ILE A CB  
3454  C CG1 . ILE A 459 ? 1.7397 0.8992 1.7791 -0.1128 -0.1201 0.1132  491 ILE A CG1 
3455  C CG2 . ILE A 459 ? 1.7626 0.9315 1.8124 -0.1212 -0.1379 0.1201  491 ILE A CG2 
3456  C CD1 . ILE A 459 ? 1.7738 0.8895 1.7759 -0.1161 -0.1218 0.0997  491 ILE A CD1 
3457  N N   . GLU A 460 ? 1.7855 0.9256 1.8389 -0.0905 -0.1555 0.1351  492 GLU A N   
3458  C CA  . GLU A 460 ? 1.7750 0.9281 1.8476 -0.0884 -0.1674 0.1446  492 GLU A CA  
3459  C C   . GLU A 460 ? 1.7285 0.8761 1.7882 -0.1047 -0.1752 0.1396  492 GLU A C   
3460  O O   . GLU A 460 ? 1.7871 0.8995 1.8167 -0.1082 -0.1841 0.1331  492 GLU A O   
3461  C CB  . GLU A 460 ? 1.8451 0.9704 1.9082 -0.0738 -0.1737 0.1469  492 GLU A CB  
3462  C CG  . GLU A 460 ? 1.9415 1.0724 2.0170 -0.0563 -0.1638 0.1524  492 GLU A CG  
3463  C CD  . GLU A 460 ? 1.9796 1.0826 2.0471 -0.0392 -0.1680 0.1549  492 GLU A CD  
3464  O OE1 . GLU A 460 ? 2.0873 1.1650 2.1387 -0.0414 -0.1801 0.1516  492 GLU A OE1 
3465  O OE2 . GLU A 460 ? 1.9506 1.0568 2.0276 -0.0229 -0.1595 0.1604  492 GLU A OE2 
3466  N N   . PRO A 461 ? 1.7575 0.9390 1.8386 -0.1147 -0.1723 0.1427  493 PRO A N   
3467  C CA  . PRO A 461 ? 1.8011 0.9761 1.8674 -0.1303 -0.1760 0.1372  493 PRO A CA  
3468  C C   . PRO A 461 ? 1.8444 1.0148 1.9117 -0.1326 -0.1905 0.1426  493 PRO A C   
3469  O O   . PRO A 461 ? 1.8243 0.9844 1.8749 -0.1452 -0.1947 0.1383  493 PRO A O   
3470  C CB  . PRO A 461 ? 1.7425 0.9588 1.8379 -0.1365 -0.1677 0.1408  493 PRO A CB  
3471  C CG  . PRO A 461 ? 1.7262 0.9791 1.8619 -0.1243 -0.1678 0.1536  493 PRO A CG  
3472  C CD  . PRO A 461 ? 1.7597 0.9877 1.8808 -0.1113 -0.1661 0.1522  493 PRO A CD  
3473  N N   . LEU A 462 ? 1.7544 0.9324 1.8413 -0.1210 -0.1979 0.1521  494 LEU A N   
3474  C CA  . LEU A 462 ? 1.8051 0.9800 1.8959 -0.1225 -0.2129 0.1581  494 LEU A CA  
3475  C C   . LEU A 462 ? 1.8768 1.0021 1.9288 -0.1198 -0.2237 0.1515  494 LEU A C   
3476  O O   . LEU A 462 ? 1.9443 1.0532 1.9931 -0.1060 -0.2239 0.1520  494 LEU A O   
3477  C CB  . LEU A 462 ? 1.8501 1.0613 1.9857 -0.1118 -0.2157 0.1719  494 LEU A CB  
3478  C CG  . LEU A 462 ? 1.8406 1.1019 2.0152 -0.1182 -0.2118 0.1797  494 LEU A CG  
3479  C CD1 . LEU A 462 ? 1.8576 1.1582 2.0795 -0.1084 -0.2149 0.1936  494 LEU A CD1 
3480  C CD2 . LEU A 462 ? 1.8116 1.0696 1.9751 -0.1330 -0.2180 0.1777  494 LEU A CD2 
3481  N N   . GLY A 463 ? 2.2695 1.3701 2.2908 -0.1325 -0.2326 0.1454  495 GLY A N   
3482  C CA  . GLY A 463 ? 2.3358 1.3890 2.3173 -0.1317 -0.2462 0.1393  495 GLY A CA  
3483  C C   . GLY A 463 ? 2.4069 1.4528 2.3790 -0.1421 -0.2625 0.1428  495 GLY A C   
3484  O O   . GLY A 463 ? 2.4109 1.4676 2.3799 -0.1560 -0.2604 0.1417  495 GLY A O   
3485  N N   . VAL A 464 ? 2.5072 1.5339 2.4748 -0.1349 -0.2787 0.1472  496 VAL A N   
3486  C CA  . VAL A 464 ? 2.5100 1.5263 2.4674 -0.1437 -0.2971 0.1514  496 VAL A CA  
3487  C C   . VAL A 464 ? 2.5655 1.5278 2.4653 -0.1499 -0.3110 0.1419  496 VAL A C   
3488  O O   . VAL A 464 ? 2.5752 1.5061 2.4502 -0.1412 -0.3116 0.1349  496 VAL A O   
3489  C CB  . VAL A 464 ? 2.5537 1.5848 2.5451 -0.1325 -0.3078 0.1634  496 VAL A CB  
3490  C CG1 . VAL A 464 ? 2.4865 1.5734 2.5322 -0.1298 -0.2963 0.1736  496 VAL A CG1 
3491  C CG2 . VAL A 464 ? 2.6278 1.6336 2.6132 -0.1148 -0.3098 0.1617  496 VAL A CG2 
3492  N N   . ALA A 465 ? 2.6176 1.5677 2.4932 -0.1651 -0.3222 0.1415  497 ALA A N   
3493  C CA  . ALA A 465 ? 2.7019 1.6002 2.5177 -0.1730 -0.3367 0.1331  497 ALA A CA  
3494  C C   . ALA A 465 ? 2.7838 1.6713 2.5836 -0.1850 -0.3553 0.1384  497 ALA A C   
3495  O O   . ALA A 465 ? 2.7449 1.6649 2.5706 -0.1934 -0.3506 0.1446  497 ALA A O   
3496  C CB  . ALA A 465 ? 2.6750 1.5599 2.4568 -0.1837 -0.3239 0.1215  497 ALA A CB  
3497  N N   . PRO A 466 ? 2.7340 1.5755 2.4905 -0.1858 -0.3766 0.1363  498 PRO A N   
3498  C CA  . PRO A 466 ? 2.8075 1.6349 2.5450 -0.1974 -0.3965 0.1418  498 PRO A CA  
3499  C C   . PRO A 466 ? 2.8409 1.6470 2.5299 -0.2170 -0.3957 0.1355  498 PRO A C   
3500  O O   . PRO A 466 ? 2.8394 1.6190 2.4877 -0.2212 -0.3890 0.1250  498 PRO A O   
3501  C CB  . PRO A 466 ? 2.8816 1.6648 2.5904 -0.1885 -0.4195 0.1414  498 PRO A CB  
3502  C CG  . PRO A 466 ? 2.8427 1.5989 2.5236 -0.1803 -0.4111 0.1304  498 PRO A CG  
3503  C CD  . PRO A 466 ? 2.7709 1.5711 2.4963 -0.1743 -0.3842 0.1296  498 PRO A CD  
3504  N N   . THR A 467 ? 2.8191 1.6366 2.5118 -0.2293 -0.4020 0.1421  499 THR A N   
3505  C CA  . THR A 467 ? 2.8885 1.6829 2.5328 -0.2485 -0.4023 0.1374  499 THR A CA  
3506  C C   . THR A 467 ? 2.9927 1.7906 2.6388 -0.2585 -0.4176 0.1469  499 THR A C   
3507  O O   . THR A 467 ? 2.9946 1.8249 2.6894 -0.2516 -0.4219 0.1570  499 THR A O   
3508  C CB  . THR A 467 ? 2.8166 1.6379 2.4737 -0.2556 -0.3753 0.1315  499 THR A CB  
3509  O OG1 . THR A 467 ? 2.9134 1.7115 2.5241 -0.2746 -0.3754 0.1276  499 THR A OG1 
3510  C CG2 . THR A 467 ? 2.7131 1.5911 2.4367 -0.2515 -0.3615 0.1397  499 THR A CG2 
3511  N N   . ARG A 468 ? 2.9969 1.7601 2.5868 -0.2754 -0.4253 0.1437  500 ARG A N   
3512  C CA  . ARG A 468 ? 3.0371 1.7933 2.6136 -0.2879 -0.4410 0.1514  500 ARG A CA  
3513  C C   . ARG A 468 ? 3.0287 1.8290 2.6438 -0.2961 -0.4235 0.1560  500 ARG A C   
3514  O O   . ARG A 468 ? 3.0702 1.8573 2.6536 -0.3128 -0.4228 0.1555  500 ARG A O   
3515  C CB  . ARG A 468 ? 3.1465 1.8422 2.6401 -0.3022 -0.4554 0.1455  500 ARG A CB  
3516  C CG  . ARG A 468 ? 3.1439 1.8252 2.6009 -0.3110 -0.4350 0.1337  500 ARG A CG  
3517  C CD  . ARG A 468 ? 3.1975 1.8174 2.5679 -0.3260 -0.4485 0.1285  500 ARG A CD  
3518  N NE  . ARG A 468 ? 3.1589 1.7680 2.4963 -0.3361 -0.4274 0.1179  500 ARG A NE  
3519  C CZ  . ARG A 468 ? 3.2035 1.7597 2.4637 -0.3481 -0.4331 0.1116  500 ARG A CZ  
3520  N NH1 . ARG A 468 ? 3.2906 1.7987 2.4977 -0.3511 -0.4601 0.1148  500 ARG A NH1 
3521  N NH2 . ARG A 468 ? 3.2155 1.7662 2.4512 -0.3572 -0.4120 0.1021  500 ARG A NH2 
3522  N N   . CYS A 469 ? 2.8142 1.6657 2.4966 -0.2839 -0.4087 0.1606  501 CYS A N   
3523  C CA  . CYS A 469 ? 2.8115 1.7098 2.5392 -0.2877 -0.3906 0.1654  501 CYS A CA  
3524  C C   . CYS A 469 ? 2.8335 1.7690 2.6166 -0.2782 -0.3981 0.1781  501 CYS A C   
3525  O O   . CYS A 469 ? 2.8251 1.7748 2.6401 -0.2626 -0.4006 0.1809  501 CYS A O   
3526  C CB  . CYS A 469 ? 2.7364 1.6664 2.4951 -0.2827 -0.3617 0.1590  501 CYS A CB  
3527  S SG  . CYS A 469 ? 3.3231 2.3089 3.1380 -0.2859 -0.3417 0.1660  501 CYS A SG  
3528  N N   . LYS A 470 ? 2.6606 1.6112 2.4540 -0.2880 -0.4011 0.1857  502 LYS A N   
3529  C CA  . LYS A 470 ? 2.6652 1.6532 2.5104 -0.2813 -0.4076 0.1983  502 LYS A CA  
3530  C C   . LYS A 470 ? 2.6756 1.7060 2.5567 -0.2857 -0.3859 0.2013  502 LYS A C   
3531  O O   . LYS A 470 ? 2.6434 1.6636 2.4987 -0.2989 -0.3741 0.1955  502 LYS A O   
3532  C CB  . LYS A 470 ? 2.8188 1.7816 2.6398 -0.2895 -0.4359 0.2060  502 LYS A CB  
3533  C CG  . LYS A 470 ? 3.0064 2.0040 2.8786 -0.2829 -0.4467 0.2195  502 LYS A CG  
3534  C CD  . LYS A 470 ? 3.1113 2.0781 2.9503 -0.2945 -0.4748 0.2257  502 LYS A CD  
3535  C CE  . LYS A 470 ? 3.1604 2.1594 3.0468 -0.2907 -0.4872 0.2395  502 LYS A CE  
3536  N NZ  . LYS A 470 ? 3.1648 2.1949 3.1051 -0.2716 -0.4840 0.2432  502 LYS A NZ  
3537  N N   . ARG A 471 ? 2.4428 1.5202 2.3830 -0.2749 -0.3802 0.2102  503 ARG A N   
3538  C CA  . ARG A 471 ? 2.4535 1.5679 2.4237 -0.2789 -0.3597 0.2125  503 ARG A CA  
3539  C C   . ARG A 471 ? 2.5700 1.6842 2.5338 -0.2916 -0.3688 0.2200  503 ARG A C   
3540  O O   . ARG A 471 ? 2.6353 1.7148 2.5615 -0.3006 -0.3905 0.2218  503 ARG A O   
3541  C CB  . ARG A 471 ? 2.4109 1.5779 2.4439 -0.2641 -0.3466 0.2188  503 ARG A CB  
3542  C CG  . ARG A 471 ? 2.3096 1.4885 2.3517 -0.2575 -0.3236 0.2099  503 ARG A CG  
3543  C CD  . ARG A 471 ? 2.2090 1.4415 2.3096 -0.2461 -0.3100 0.2169  503 ARG A CD  
3544  N NE  . ARG A 471 ? 2.2718 1.5236 2.4062 -0.2326 -0.3215 0.2255  503 ARG A NE  
3545  C CZ  . ARG A 471 ? 2.2763 1.5760 2.4635 -0.2227 -0.3147 0.2342  503 ARG A CZ  
3546  N NH1 . ARG A 471 ? 2.2180 1.5493 2.4283 -0.2244 -0.2980 0.2356  503 ARG A NH1 
3547  N NH2 . ARG A 471 ? 2.3386 1.6538 2.5555 -0.2113 -0.3247 0.2417  503 ARG A NH2 
3548  N N   . ARG A 472 ? 2.3106 1.4636 2.3113 -0.2920 -0.3529 0.2247  504 ARG A N   
3549  C CA  . ARG A 472 ? 2.5033 1.6591 2.5004 -0.3041 -0.3573 0.2313  504 ARG A CA  
3550  C C   . ARG A 472 ? 2.6303 1.8148 2.6671 -0.2977 -0.3729 0.2456  504 ARG A C   
3551  O O   . ARG A 472 ? 2.6184 1.8115 2.6776 -0.2857 -0.3857 0.2504  504 ARG A O   
3552  C CB  . ARG A 472 ? 2.4903 1.6674 2.5005 -0.3095 -0.3300 0.2274  504 ARG A CB  
3553  C CG  . ARG A 472 ? 2.4338 1.6608 2.5009 -0.2951 -0.3120 0.2306  504 ARG A CG  
3554  C CD  . ARG A 472 ? 2.4240 1.6585 2.4916 -0.2997 -0.2841 0.2216  504 ARG A CD  
3555  N NE  . ARG A 472 ? 2.4016 1.5991 2.4266 -0.3064 -0.2780 0.2083  504 ARG A NE  
3556  C CZ  . ARG A 472 ? 2.2885 1.4901 2.3193 -0.2990 -0.2644 0.2002  504 ARG A CZ  
3557  N NH1 . ARG A 472 ? 2.2568 1.4236 2.2471 -0.3066 -0.2599 0.1884  504 ARG A NH1 
3558  N NH2 . ARG A 472 ? 2.1719 1.4121 2.2477 -0.2844 -0.2563 0.2042  504 ARG A NH2 
3559  N N   . VAL A 473 ? 2.8511 2.0514 2.8981 -0.3061 -0.3697 0.2520  505 VAL A N   
3560  C CA  . VAL A 473 ? 2.9593 2.1827 3.0356 -0.3056 -0.3842 0.2657  505 VAL A CA  
3561  C C   . VAL A 473 ? 3.0047 2.2589 3.1045 -0.3097 -0.3637 0.2684  505 VAL A C   
3562  O O   . VAL A 473 ? 3.0772 2.3499 3.1960 -0.3131 -0.3703 0.2788  505 VAL A O   
3563  C CB  . VAL A 473 ? 3.0853 2.2687 3.1194 -0.3180 -0.4122 0.2693  505 VAL A CB  
3564  C CG1 . VAL A 473 ? 3.0898 2.2496 3.0827 -0.3376 -0.4077 0.2667  505 VAL A CG1 
3565  C CG2 . VAL A 473 ? 2.9546 2.1604 3.0261 -0.3115 -0.4343 0.2836  505 VAL A CG2 
3566  N N   . VAL A 474 ? 2.7574 2.0176 2.8577 -0.3086 -0.3382 0.2588  506 VAL A N   
3567  C CA  . VAL A 474 ? 2.7521 2.0346 2.8685 -0.3124 -0.3144 0.2575  506 VAL A CA  
3568  C C   . VAL A 474 ? 2.8343 2.0924 2.9170 -0.3307 -0.3179 0.2583  506 VAL A C   
3569  O O   . VAL A 474 ? 2.8092 2.0894 2.9127 -0.3336 -0.3125 0.2653  506 VAL A O   
3570  C CB  . VAL A 474 ? 2.6505 1.9870 2.8278 -0.2987 -0.3083 0.2679  506 VAL A CB  
3571  C CG1 . VAL A 474 ? 2.5540 1.9120 2.7477 -0.2995 -0.2812 0.2641  506 VAL A CG1 
3572  C CG2 . VAL A 474 ? 2.5837 1.9408 2.7915 -0.2815 -0.3119 0.2692  506 VAL A CG2 
3573  N N   . GLY A 475 ? 2.6173 1.8288 2.6458 -0.3434 -0.3269 0.2511  507 GLY A N   
3574  C CA  . GLY A 475 ? 2.6403 1.8243 2.6304 -0.3623 -0.3313 0.2512  507 GLY A CA  
3575  C C   . GLY A 475 ? 2.5468 1.7383 2.5392 -0.3707 -0.3028 0.2448  507 GLY A C   
3576  O O   . GLY A 475 ? 2.5389 1.6977 2.4892 -0.3860 -0.2959 0.2360  507 GLY A O   
3577  N N   . ALA B 1   ? 2.4265 2.1458 2.7284 -0.7043 -0.4970 -0.2870 512 ALA B N   
3578  C CA  . ALA B 1   ? 2.4230 2.1376 2.7246 -0.7019 -0.4910 -0.2884 512 ALA B CA  
3579  C C   . ALA B 1   ? 2.4021 2.1241 2.7063 -0.7010 -0.4820 -0.2974 512 ALA B C   
3580  O O   . ALA B 1   ? 2.3815 2.1113 2.6882 -0.7016 -0.4801 -0.3028 512 ALA B O   
3581  C CB  . ALA B 1   ? 2.3835 2.0885 2.6870 -0.6966 -0.4909 -0.2854 512 ALA B CB  
3582  N N   . VAL B 2   ? 2.2267 1.9463 2.5307 -0.6997 -0.4765 -0.2990 513 VAL B N   
3583  C CA  . VAL B 2   ? 2.2130 1.9390 2.5203 -0.6987 -0.4678 -0.3072 513 VAL B CA  
3584  C C   . VAL B 2   ? 2.1403 1.8660 2.4520 -0.6935 -0.4631 -0.3111 513 VAL B C   
3585  O O   . VAL B 2   ? 2.1059 1.8242 2.4178 -0.6899 -0.4653 -0.3073 513 VAL B O   
3586  C CB  . VAL B 2   ? 2.2518 1.9755 2.5579 -0.6991 -0.4637 -0.3071 513 VAL B CB  
3587  C CG1 . VAL B 2   ? 2.3325 2.0578 2.6344 -0.7047 -0.4675 -0.3041 513 VAL B CG1 
3588  C CG2 . VAL B 2   ? 2.2328 1.9465 2.5380 -0.6955 -0.4647 -0.3020 513 VAL B CG2 
3589  N N   . GLY B 3   ? 2.1361 1.8697 2.4515 -0.6932 -0.4565 -0.3190 514 GLY B N   
3590  C CA  . GLY B 3   ? 2.0723 1.8063 2.3917 -0.6887 -0.4514 -0.3233 514 GLY B CA  
3591  C C   . GLY B 3   ? 2.0709 1.8111 2.3939 -0.6883 -0.4422 -0.3312 514 GLY B C   
3592  O O   . GLY B 3   ? 2.1175 1.8640 2.4411 -0.6919 -0.4401 -0.3347 514 GLY B O   
3593  N N   . ILE B 4   ? 1.8922 1.6307 2.2179 -0.6839 -0.4367 -0.3339 515 ILE B N   
3594  C CA  . ILE B 4   ? 1.8834 1.6272 2.2131 -0.6831 -0.4276 -0.3409 515 ILE B CA  
3595  C C   . ILE B 4   ? 1.8768 1.6246 2.2103 -0.6807 -0.4231 -0.3465 515 ILE B C   
3596  O O   . ILE B 4   ? 1.8685 1.6181 2.2051 -0.6785 -0.4156 -0.3512 515 ILE B O   
3597  C CB  . ILE B 4   ? 1.8796 1.6177 2.2088 -0.6806 -0.4243 -0.3388 515 ILE B CB  
3598  C CG1 . ILE B 4   ? 1.8768 1.6209 2.2101 -0.6811 -0.4157 -0.3452 515 ILE B CG1 
3599  C CG2 . ILE B 4   ? 1.8766 1.6076 2.2054 -0.6757 -0.4248 -0.3360 515 ILE B CG2 
3600  C CD1 . ILE B 4   ? 1.9079 1.6481 2.2405 -0.6804 -0.4138 -0.3425 515 ILE B CD1 
3601  N N   . GLY B 5   ? 2.1054 1.8547 2.4385 -0.6814 -0.4278 -0.3459 516 GLY B N   
3602  C CA  . GLY B 5   ? 2.0779 1.8324 2.4145 -0.6803 -0.4240 -0.3517 516 GLY B CA  
3603  C C   . GLY B 5   ? 2.0139 1.7624 2.3503 -0.6758 -0.4254 -0.3488 516 GLY B C   
3604  O O   . GLY B 5   ? 2.0014 1.7413 2.3352 -0.6734 -0.4297 -0.3424 516 GLY B O   
3605  N N   . ALA B 6   ? 2.0766 1.8296 2.4160 -0.6748 -0.4216 -0.3541 517 ALA B N   
3606  C CA  . ALA B 6   ? 2.0323 1.7804 2.3720 -0.6707 -0.4226 -0.3521 517 ALA B CA  
3607  C C   . ALA B 6   ? 1.9927 1.7343 2.3320 -0.6663 -0.4180 -0.3511 517 ALA B C   
3608  O O   . ALA B 6   ? 2.0255 1.7692 2.3656 -0.6665 -0.4117 -0.3544 517 ALA B O   
3609  C CB  . ALA B 6   ? 2.0504 1.8055 2.3933 -0.6711 -0.4190 -0.3584 517 ALA B CB  
3610  N N   . VAL B 7   ? 2.0994 1.8333 2.4378 -0.6624 -0.4213 -0.3466 518 VAL B N   
3611  C CA  . VAL B 7   ? 2.0620 1.7895 2.4000 -0.6581 -0.4174 -0.3457 518 VAL B CA  
3612  C C   . VAL B 7   ? 2.0589 1.7859 2.3987 -0.6549 -0.4147 -0.3480 518 VAL B C   
3613  O O   . VAL B 7   ? 2.0761 1.8081 2.4176 -0.6562 -0.4156 -0.3505 518 VAL B O   
3614  C CB  . VAL B 7   ? 2.0822 1.7997 2.4176 -0.6562 -0.4231 -0.3383 518 VAL B CB  
3615  C CG1 . VAL B 7   ? 2.1251 1.8430 2.4586 -0.6590 -0.4231 -0.3369 518 VAL B CG1 
3616  C CG2 . VAL B 7   ? 2.0849 1.7987 2.4197 -0.6566 -0.4317 -0.3331 518 VAL B CG2 
3617  N N   . PHE B 8   ? 2.1091 1.8300 2.4485 -0.6507 -0.4117 -0.3470 519 PHE B N   
3618  C CA  . PHE B 8   ? 2.1124 1.8319 2.4531 -0.6473 -0.4090 -0.3487 519 PHE B CA  
3619  C C   . PHE B 8   ? 2.1596 1.8683 2.4993 -0.6427 -0.4122 -0.3435 519 PHE B C   
3620  O O   . PHE B 8   ? 2.1633 1.8667 2.5014 -0.6414 -0.4120 -0.3408 519 PHE B O   
3621  C CB  . PHE B 8   ? 2.1243 1.8490 2.4660 -0.6473 -0.3997 -0.3549 519 PHE B CB  
3622  C CG  . PHE B 8   ? 2.1496 1.8734 2.4922 -0.6443 -0.3961 -0.3571 519 PHE B CG  
3623  C CD1 . PHE B 8   ? 2.1918 1.9209 2.5361 -0.6456 -0.3959 -0.3604 519 PHE B CD1 
3624  C CD2 . PHE B 8   ? 2.1410 1.8593 2.4828 -0.6404 -0.3926 -0.3563 519 PHE B CD2 
3625  C CE1 . PHE B 8   ? 2.1883 1.9164 2.5332 -0.6429 -0.3925 -0.3623 519 PHE B CE1 
3626  C CE2 . PHE B 8   ? 2.1536 1.8709 2.4959 -0.6376 -0.3892 -0.3582 519 PHE B CE2 
3627  C CZ  . PHE B 8   ? 2.1459 1.8679 2.4897 -0.6389 -0.3892 -0.3611 519 PHE B CZ  
3628  N N   . LEU B 9   ? 2.2365 1.9421 2.5776 -0.6401 -0.4149 -0.3422 520 LEU B N   
3629  C CA  . LEU B 9   ? 2.0494 1.7445 2.3903 -0.6357 -0.4179 -0.3375 520 LEU B CA  
3630  C C   . LEU B 9   ? 2.0609 1.7536 2.4026 -0.6317 -0.4126 -0.3399 520 LEU B C   
3631  O O   . LEU B 9   ? 2.0445 1.7288 2.3856 -0.6281 -0.4132 -0.3370 520 LEU B O   
3632  C CB  . LEU B 9   ? 2.0399 1.7314 2.3824 -0.6354 -0.4259 -0.3331 520 LEU B CB  
3633  C CG  . LEU B 9   ? 2.1026 1.7956 2.4441 -0.6394 -0.4321 -0.3299 520 LEU B CG  
3634  C CD1 . LEU B 9   ? 2.0957 1.7847 2.4392 -0.6390 -0.4400 -0.3250 520 LEU B CD1 
3635  C CD2 . LEU B 9   ? 2.1450 1.8333 2.4838 -0.6400 -0.4327 -0.3269 520 LEU B CD2 
3636  N N   . GLY B 10  ? 2.3139 2.0136 2.6567 -0.6324 -0.4074 -0.3451 521 GLY B N   
3637  C CA  . GLY B 10  ? 2.2499 1.9478 2.5930 -0.6289 -0.4020 -0.3474 521 GLY B CA  
3638  C C   . GLY B 10  ? 2.1765 1.8723 2.5218 -0.6264 -0.4042 -0.3470 521 GLY B C   
3639  O O   . GLY B 10  ? 2.2059 1.9031 2.5529 -0.6277 -0.4096 -0.3455 521 GLY B O   
3640  N N   . PHE B 11  ? 2.0166 1.7093 2.3618 -0.6228 -0.3998 -0.3483 522 PHE B N   
3641  C CA  . PHE B 11  ? 2.0047 1.6945 2.3521 -0.6198 -0.4012 -0.3479 522 PHE B CA  
3642  C C   . PHE B 11  ? 2.0204 1.7018 2.3695 -0.6173 -0.4088 -0.3423 522 PHE B C   
3643  O O   . PHE B 11  ? 2.0318 1.7057 2.3798 -0.6153 -0.4102 -0.3391 522 PHE B O   
3644  C CB  . PHE B 11  ? 2.0186 1.7055 2.3654 -0.6162 -0.3953 -0.3497 522 PHE B CB  
3645  C CG  . PHE B 11  ? 2.0425 1.7273 2.3916 -0.6132 -0.3959 -0.3500 522 PHE B CG  
3646  C CD1 . PHE B 11  ? 2.0320 1.7242 2.3822 -0.6156 -0.3941 -0.3536 522 PHE B CD1 
3647  C CD2 . PHE B 11  ? 2.0425 1.7180 2.3928 -0.6083 -0.3979 -0.3469 522 PHE B CD2 
3648  C CE1 . PHE B 11  ? 2.0448 1.7351 2.3975 -0.6128 -0.3948 -0.3537 522 PHE B CE1 
3649  C CE2 . PHE B 11  ? 2.0423 1.7157 2.3953 -0.6053 -0.3984 -0.3471 522 PHE B CE2 
3650  C CZ  . PHE B 11  ? 2.0442 1.7251 2.3984 -0.6076 -0.3970 -0.3504 522 PHE B CZ  
3651  N N   . LEU B 12  ? 2.0573 1.7400 2.4093 -0.6177 -0.4135 -0.3412 523 LEU B N   
3652  C CA  . LEU B 12  ? 2.0940 1.7690 2.4484 -0.6158 -0.4210 -0.3357 523 LEU B CA  
3653  C C   . LEU B 12  ? 2.1569 1.8295 2.5095 -0.6181 -0.4252 -0.3321 523 LEU B C   
3654  O O   . LEU B 12  ? 2.1957 1.8596 2.5491 -0.6161 -0.4300 -0.3273 523 LEU B O   
3655  C CB  . LEU B 12  ? 2.0681 1.7332 2.4237 -0.6103 -0.4204 -0.3338 523 LEU B CB  
3656  C CG  . LEU B 12  ? 2.0664 1.7326 2.4242 -0.6076 -0.4173 -0.3365 523 LEU B CG  
3657  C CD1 . LEU B 12  ? 2.0880 1.7440 2.4469 -0.6021 -0.4166 -0.3347 523 LEU B CD1 
3658  C CD2 . LEU B 12  ? 2.0012 1.6715 2.3629 -0.6089 -0.4219 -0.3361 523 LEU B CD2 
3659  N N   . GLY B 13  ? 2.0205 1.7332 2.3875 0.4190  -0.1707 -0.1967 524 GLY B N   
3660  C CA  . GLY B 13  ? 1.9968 1.6907 2.2958 0.4012  -0.1344 -0.2337 524 GLY B CA  
3661  C C   . GLY B 13  ? 2.0451 1.6795 2.2547 0.4101  -0.0968 -0.2367 524 GLY B C   
3662  O O   . GLY B 13  ? 2.0697 1.6704 2.1924 0.3928  -0.0561 -0.2381 524 GLY B O   
3663  N N   . ALA B 14  ? 1.9368 1.5569 2.1652 0.4363  -0.1106 -0.2377 525 ALA B N   
3664  C CA  . ALA B 14  ? 2.0509 1.6218 2.1973 0.4394  -0.0761 -0.2358 525 ALA B CA  
3665  C C   . ALA B 14  ? 2.1635 1.7120 2.2860 0.4498  -0.0672 -0.1916 525 ALA B C   
3666  O O   . ALA B 14  ? 2.2455 1.7895 2.3641 0.4533  -0.0640 -0.1717 525 ALA B O   
3667  C CB  . ALA B 14  ? 2.0853 1.6711 2.2521 0.4365  -0.0850 -0.2442 525 ALA B CB  
3668  N N   . ALA B 15  ? 1.9548 1.4954 2.0625 0.4488  -0.0614 -0.1732 526 ALA B N   
3669  C CA  . ALA B 15  ? 1.9994 1.5152 2.0824 0.4621  -0.0514 -0.1326 526 ALA B CA  
3670  C C   . ALA B 15  ? 2.0566 1.5119 2.0315 0.4626  -0.0041 -0.1355 526 ALA B C   
3671  O O   . ALA B 15  ? 2.2457 1.6947 2.2118 0.4664  0.0037  -0.1075 526 ALA B O   
3672  C CB  . ALA B 15  ? 1.9479 1.4864 2.0468 0.4445  -0.0540 -0.1042 526 ALA B CB  
3673  N N   . GLY B 16  ? 2.1824 1.6141 2.0854 0.4409  0.0289  -0.1650 527 GLY B N   
3674  C CA  . GLY B 16  ? 2.3054 1.6746 2.0980 0.4392  0.0751  -0.1729 527 GLY B CA  
3675  C C   . GLY B 16  ? 2.3150 1.6839 2.0944 0.4305  0.0796  -0.1995 527 GLY B C   
3676  O O   . GLY B 16  ? 2.3647 1.7009 2.0655 0.4175  0.1117  -0.2033 527 GLY B O   
3677  N N   . SER B 17  ? 2.1847 1.5931 2.0410 0.4337  0.0473  -0.2157 528 SER B N   
3678  C CA  . SER B 17  ? 2.1869 1.5966 2.0368 0.4239  0.0510  -0.2383 528 SER B CA  
3679  C C   . SER B 17  ? 2.2709 1.6833 2.1412 0.4354  0.0393  -0.2114 528 SER B C   
3680  O O   . SER B 17  ? 2.3185 1.7452 2.2280 0.4488  0.0229  -0.1770 528 SER B O   
3681  C CB  . SER B 17  ? 2.1253 1.5738 2.0420 0.4202  0.0254  -0.2655 528 SER B CB  
3682  O OG  . SER B 17  ? 2.1046 1.5569 2.0072 0.4081  0.0341  -0.2946 528 SER B OG  
3683  N N   . THR B 18  ? 2.1634 1.5643 2.0071 0.4272  0.0484  -0.2275 529 THR B N   
3684  C CA  . THR B 18  ? 2.2232 1.6256 2.0827 0.4372  0.0366  -0.2066 529 THR B CA  
3685  C C   . THR B 18  ? 2.2029 1.6484 2.1560 0.4474  -0.0003 -0.1901 529 THR B C   
3686  O O   . THR B 18  ? 2.1587 1.6325 2.1601 0.4455  -0.0185 -0.2013 529 THR B O   
3687  C CB  . THR B 18  ? 2.2242 1.6068 2.0395 0.4255  0.0506  -0.2294 529 THR B CB  
3688  O OG1 . THR B 18  ? 2.1673 1.5595 1.9894 0.4094  0.0550  -0.2645 529 THR B OG1 
3689  C CG2 . THR B 18  ? 2.2762 1.6196 1.9983 0.4173  0.0823  -0.2276 529 THR B CG2 
3690  N N   . MET B 19  ? 2.1869 1.6402 2.1628 0.4561  -0.0117 -0.1625 530 MET B N   
3691  C CA  . MET B 19  ? 2.1045 1.6000 2.1596 0.4606  -0.0429 -0.1425 530 MET B CA  
3692  C C   . MET B 19  ? 2.0702 1.5763 2.1421 0.4558  -0.0568 -0.1676 530 MET B C   
3693  O O   . MET B 19  ? 1.9974 1.5404 2.1264 0.4553  -0.0837 -0.1644 530 MET B O   
3694  C CB  . MET B 19  ? 2.1032 1.6039 2.1725 0.4671  -0.0472 -0.1107 530 MET B CB  
3695  C CG  . MET B 19  ? 2.1285 1.6274 2.1937 0.4711  -0.0379 -0.0834 530 MET B CG  
3696  S SD  . MET B 19  ? 2.1717 1.6788 2.2545 0.4767  -0.0413 -0.0498 530 MET B SD  
3697  C CE  . MET B 19  ? 2.1327 1.6892 2.2974 0.4748  -0.0680 -0.0304 530 MET B CE  
3698  N N   . GLY B 20  ? 2.2199 1.6950 2.2402 0.4503  -0.0397 -0.1926 531 GLY B N   
3699  C CA  . GLY B 20  ? 2.1886 1.6706 2.2201 0.4444  -0.0502 -0.2177 531 GLY B CA  
3700  C C   . GLY B 20  ? 2.1485 1.6475 2.1977 0.4365  -0.0538 -0.2436 531 GLY B C   
3701  O O   . GLY B 20  ? 2.0859 1.6131 2.1797 0.4352  -0.0779 -0.2540 531 GLY B O   
3702  N N   . ALA B 21  ? 2.0878 1.5718 2.1022 0.4303  -0.0310 -0.2556 532 ALA B N   
3703  C CA  . ALA B 21  ? 2.0150 1.5175 2.0465 0.4219  -0.0337 -0.2818 532 ALA B CA  
3704  C C   . ALA B 21  ? 1.9595 1.5051 2.0647 0.4309  -0.0674 -0.2637 532 ALA B C   
3705  O O   . ALA B 21  ? 1.9519 1.5324 2.1070 0.4272  -0.0897 -0.2804 532 ALA B O   
3706  C CB  . ALA B 21  ? 1.9390 1.4110 1.9028 0.4082  0.0039  -0.3013 532 ALA B CB  
3707  N N   . ALA B 22  ? 2.0154 1.5621 2.1309 0.4404  -0.0714 -0.2287 533 ALA B N   
3708  C CA  . ALA B 22  ? 1.9969 1.5843 2.1786 0.4442  -0.1003 -0.2059 533 ALA B CA  
3709  C C   . ALA B 22  ? 1.9247 1.5518 2.1692 0.4438  -0.1341 -0.1912 533 ALA B C   
3710  O O   . ALA B 22  ? 1.8820 1.5480 2.1835 0.4408  -0.1602 -0.1777 533 ALA B O   
3711  C CB  . ALA B 22  ? 1.9867 1.5612 2.1537 0.4512  -0.0889 -0.1713 533 ALA B CB  
3712  N N   . SER B 23  ? 1.7672 1.3836 1.9984 0.4445  -0.1338 -0.1945 534 SER B N   
3713  C CA  . SER B 23  ? 1.7443 1.3923 2.0246 0.4426  -0.1637 -0.1842 534 SER B CA  
3714  C C   . SER B 23  ? 1.7304 1.4063 2.0519 0.4351  -0.1864 -0.2126 534 SER B C   
3715  O O   . SER B 23  ? 1.7109 1.4150 2.0772 0.4312  -0.2134 -0.2060 534 SER B O   
3716  C CB  . SER B 23  ? 1.7631 1.3876 2.0136 0.4463  -0.1564 -0.1813 534 SER B CB  
3717  O OG  . SER B 23  ? 1.7731 1.3777 1.9954 0.4528  -0.1378 -0.1538 534 SER B OG  
3718  N N   . MET B 24  ? 1.7834 1.4522 2.0901 0.4318  -0.1745 -0.2446 535 MET B N   
3719  C CA  . MET B 24  ? 1.8344 1.5331 2.1841 0.4247  -0.1935 -0.2735 535 MET B CA  
3720  C C   . MET B 24  ? 1.7606 1.4982 2.1678 0.4211  -0.2155 -0.2663 535 MET B C   
3721  O O   . MET B 24  ? 1.7327 1.5033 2.1909 0.4150  -0.2385 -0.2831 535 MET B O   
3722  C CB  . MET B 24  ? 1.9548 1.6313 2.2609 0.4196  -0.1666 -0.3123 535 MET B CB  
3723  C CG  . MET B 24  ? 1.9668 1.5953 2.1990 0.4195  -0.1356 -0.3167 535 MET B CG  
3724  S SD  . MET B 24  ? 2.0818 1.7070 2.3212 0.4223  -0.1516 -0.3116 535 MET B SD  
3725  C CE  . MET B 24  ? 2.1130 1.6793 2.2595 0.4182  -0.1083 -0.3211 535 MET B CE  
3726  N N   . THR B 25  ? 1.7854 1.5183 2.1847 0.4243  -0.2084 -0.2409 536 THR B N   
3727  C CA  . THR B 25  ? 1.7839 1.5482 2.2298 0.4201  -0.2261 -0.2309 536 THR B CA  
3728  C C   . THR B 25  ? 1.7345 1.5204 2.2127 0.4169  -0.2455 -0.1904 536 THR B C   
3729  O O   . THR B 25  ? 1.7514 1.5539 2.2522 0.4135  -0.2534 -0.1710 536 THR B O   
3730  C CB  . THR B 25  ? 1.8637 1.6047 2.2729 0.4242  -0.2021 -0.2329 536 THR B CB  
3731  O OG1 . THR B 25  ? 1.9756 1.6846 2.3309 0.4244  -0.1734 -0.2675 536 THR B OG1 
3732  C CG2 . THR B 25  ? 1.8135 1.5870 2.2717 0.4190  -0.2203 -0.2362 536 THR B CG2 
3733  N N   . LEU B 26  ? 1.5204 1.3058 1.9987 0.4165  -0.2523 -0.1785 537 LEU B N   
3734  C CA  . LEU B 26  ? 1.5046 1.3082 2.0055 0.4118  -0.2655 -0.1427 537 LEU B CA  
3735  C C   . LEU B 26  ? 1.4834 1.3230 2.0396 0.3996  -0.2937 -0.1429 537 LEU B C   
3736  O O   . LEU B 26  ? 1.4713 1.3268 2.0449 0.3938  -0.3012 -0.1154 537 LEU B O   
3737  C CB  . LEU B 26  ? 1.5115 1.3059 1.9997 0.4138  -0.2660 -0.1345 537 LEU B CB  
3738  C CG  . LEU B 26  ? 1.5328 1.2929 1.9685 0.4249  -0.2395 -0.1255 537 LEU B CG  
3739  C CD1 . LEU B 26  ? 1.5369 1.2948 1.9719 0.4251  -0.2470 -0.1196 537 LEU B CD1 
3740  C CD2 . LEU B 26  ? 1.5317 1.2873 1.9517 0.4295  -0.2231 -0.0925 537 LEU B CD2 
3741  N N   . THR B 27  ? 1.5393 1.3905 2.1217 0.3955  -0.3082 -0.1742 538 THR B N   
3742  C CA  . THR B 27  ? 1.5436 1.4249 2.1769 0.3841  -0.3344 -0.1764 538 THR B CA  
3743  C C   . THR B 27  ? 1.5400 1.4382 2.1955 0.3804  -0.3386 -0.1768 538 THR B C   
3744  O O   . THR B 27  ? 1.5166 1.4383 2.2130 0.3708  -0.3595 -0.1788 538 THR B O   
3745  C CB  . THR B 27  ? 1.6014 1.4890 2.2562 0.3821  -0.3477 -0.2100 538 THR B CB  
3746  O OG1 . THR B 27  ? 1.5761 1.4879 2.2771 0.3714  -0.3723 -0.2094 538 THR B OG1 
3747  C CG2 . THR B 27  ? 1.6274 1.5129 2.2763 0.3876  -0.3368 -0.2451 538 THR B CG2 
3748  N N   . VAL B 28  ? 1.5228 1.4069 2.1506 0.3877  -0.3193 -0.1746 539 VAL B N   
3749  C CA  . VAL B 28  ? 1.5152 1.4134 2.1622 0.3848  -0.3232 -0.1748 539 VAL B CA  
3750  C C   . VAL B 28  ? 1.5098 1.4082 2.1510 0.3819  -0.3216 -0.1345 539 VAL B C   
3751  O O   . VAL B 28  ? 1.4987 1.4188 2.1717 0.3725  -0.3379 -0.1228 539 VAL B O   
3752  C CB  . VAL B 28  ? 1.5289 1.4084 2.1476 0.3945  -0.3017 -0.2031 539 VAL B CB  
3753  C CG1 . VAL B 28  ? 1.5218 1.4152 2.1609 0.3920  -0.3062 -0.2026 539 VAL B CG1 
3754  C CG2 . VAL B 28  ? 1.5543 1.4387 2.1814 0.3954  -0.3021 -0.2456 539 VAL B CG2 
3755  N N   . GLN B 29  ? 1.5756 1.4494 2.1747 0.3899  -0.3010 -0.1130 540 GLN B N   
3756  C CA  . GLN B 29  ? 1.5514 1.4252 2.1420 0.3883  -0.2963 -0.0748 540 GLN B CA  
3757  C C   . GLN B 29  ? 1.5054 1.4009 2.1218 0.3777  -0.3138 -0.0548 540 GLN B C   
3758  O O   . GLN B 29  ? 1.4789 1.3830 2.0997 0.3727  -0.3159 -0.0272 540 GLN B O   
3759  C CB  . GLN B 29  ? 1.5861 1.4266 2.1237 0.4016  -0.2669 -0.0604 540 GLN B CB  
3760  C CG  . GLN B 29  ? 1.6391 1.4493 2.1419 0.4115  -0.2456 -0.0747 540 GLN B CG  
3761  C CD  . GLN B 29  ? 1.6873 1.4789 2.1696 0.4172  -0.2360 -0.1148 540 GLN B CD  
3762  O OE1 . GLN B 29  ? 1.7133 1.4909 2.1819 0.4204  -0.2267 -0.1412 540 GLN B OE1 
3763  N NE2 . GLN B 29  ? 1.6883 1.4782 2.1656 0.4180  -0.2369 -0.1214 540 GLN B NE2 
3764  N N   . ALA B 30  ? 1.3750 1.2763 2.0056 0.3744  -0.3253 -0.0697 541 ALA B N   
3765  C CA  . ALA B 30  ? 1.3689 1.2851 2.0213 0.3646  -0.3414 -0.0560 541 ALA B CA  
3766  C C   . ALA B 30  ? 1.3609 1.2985 2.0546 0.3522  -0.3646 -0.0619 541 ALA B C   
3767  O O   . ALA B 30  ? 1.3579 1.3058 2.0672 0.3432  -0.3760 -0.0444 541 ALA B O   
3768  C CB  . ALA B 30  ? 1.3746 1.2835 2.0238 0.3666  -0.3448 -0.0704 541 ALA B CB  
3769  N N   . ARG B 31  ? 1.4581 1.4014 2.1689 0.3523  -0.3707 -0.0878 542 ARG B N   
3770  C CA  . ARG B 31  ? 1.4722 1.4357 2.2231 0.3421  -0.3922 -0.0970 542 ARG B CA  
3771  C C   . ARG B 31  ? 1.4088 1.3816 2.1667 0.3355  -0.3957 -0.0732 542 ARG B C   
3772  O O   . ARG B 31  ? 1.3852 1.3689 2.1645 0.3251  -0.4112 -0.0608 542 ARG B O   
3773  C CB  . ARG B 31  ? 1.5163 1.4849 2.2805 0.3466  -0.3937 -0.1330 542 ARG B CB  
3774  C CG  . ARG B 31  ? 1.5914 1.5598 2.3676 0.3483  -0.4008 -0.1627 542 ARG B CG  
3775  C CD  . ARG B 31  ? 1.7402 1.7134 2.5225 0.3550  -0.3956 -0.1991 542 ARG B CD  
3776  N NE  . ARG B 31  ? 1.7600 1.7569 2.5769 0.3507  -0.4067 -0.2128 542 ARG B NE  
3777  C CZ  . ARG B 31  ? 1.7380 1.7410 2.5558 0.3571  -0.3972 -0.2398 542 ARG B CZ  
3778  N NH1 . ARG B 31  ? 1.7502 1.7317 2.5308 0.3678  -0.3749 -0.2549 542 ARG B NH1 
3779  N NH2 . ARG B 31  ? 1.6756 1.7047 2.5284 0.3528  -0.4081 -0.2524 542 ARG B NH2 
3780  N N   . ASN B 32  ? 1.6708 1.6358 2.4083 0.3419  -0.3810 -0.0663 543 ASN B N   
3781  C CA  . ASN B 32  ? 1.6527 1.6239 2.3948 0.3360  -0.3842 -0.0440 543 ASN B CA  
3782  C C   . ASN B 32  ? 1.6717 1.6336 2.3891 0.3361  -0.3731 -0.0095 543 ASN B C   
3783  O O   . ASN B 32  ? 1.6981 1.6555 2.4048 0.3360  -0.3670 0.0098  543 ASN B O   
3784  C CB  . ASN B 32  ? 1.6707 1.6367 2.4060 0.3427  -0.3759 -0.0557 543 ASN B CB  
3785  C CG  . ASN B 32  ? 1.6805 1.6607 2.4431 0.3434  -0.3860 -0.0935 543 ASN B CG  
3786  O OD1 . ASN B 32  ? 1.7402 1.7088 2.4868 0.3544  -0.3720 -0.1182 543 ASN B OD1 
3787  N ND2 . ASN B 32  ? 1.7106 1.7145 2.5127 0.3323  -0.4088 -0.0996 543 ASN B ND2 
3788  N N   . LEU B 33  ? 1.5198 1.4788 2.2286 0.3367  -0.3703 -0.0018 544 LEU B N   
3789  C CA  . LEU B 33  ? 1.5666 1.5201 2.2537 0.3381  -0.3589 0.0284  544 LEU B CA  
3790  C C   . LEU B 33  ? 1.5759 1.5431 2.2860 0.3246  -0.3761 0.0442  544 LEU B C   
3791  O O   . LEU B 33  ? 1.5728 1.5387 2.2719 0.3231  -0.3704 0.0690  544 LEU B O   
3792  C CB  . LEU B 33  ? 1.5710 1.5144 2.2354 0.3468  -0.3460 0.0290  544 LEU B CB  
3793  C CG  . LEU B 33  ? 1.6104 1.5467 2.2463 0.3535  -0.3286 0.0564  544 LEU B CG  
3794  C CD1 . LEU B 33  ? 1.6208 1.5412 2.2274 0.3636  -0.3082 0.0677  544 LEU B CD1 
3795  C CD2 . LEU B 33  ? 1.6394 1.5683 2.2583 0.3616  -0.3196 0.0531  544 LEU B CD2 
3796  N N   . LEU B 34  ? 2.1875 1.3242 2.0510 -0.5123 -0.0106 -0.4951 545 LEU B N   
3797  C CA  . LEU B 34  ? 2.1762 1.3239 2.0393 -0.5100 -0.0125 -0.4959 545 LEU B CA  
3798  C C   . LEU B 34  ? 2.1709 1.3250 2.0469 -0.5099 -0.0108 -0.4979 545 LEU B C   
3799  O O   . LEU B 34  ? 2.1599 1.3248 2.0415 -0.5070 -0.0166 -0.4995 545 LEU B O   
3800  C CB  . LEU B 34  ? 2.1796 1.3237 2.0276 -0.5115 -0.0062 -0.4936 545 LEU B CB  
3801  C CG  . LEU B 34  ? 2.1685 1.3232 2.0150 -0.5092 -0.0079 -0.4940 545 LEU B CG  
3802  C CD1 . LEU B 34  ? 2.1579 1.3219 2.0066 -0.5052 -0.0186 -0.4947 545 LEU B CD1 
3803  C CD2 . LEU B 34  ? 2.1741 1.3233 2.0050 -0.5111 -0.0016 -0.4917 545 LEU B CD2 
3804  N N   . SER B 35  ? 2.6019 1.7491 2.4827 -0.5133 -0.0031 -0.4978 546 SER B N   
3805  C CA  . SER B 35  ? 2.6391 1.7908 2.5335 -0.5139 -0.0010 -0.4995 546 SER B CA  
3806  C C   . SER B 35  ? 2.6828 1.8440 2.5768 -0.5126 -0.0000 -0.5000 546 SER B C   
3807  O O   . SER B 35  ? 2.6908 1.8624 2.5917 -0.5096 -0.0073 -0.5018 546 SER B O   
3808  C CB  . SER B 35  ? 2.6299 1.7859 2.5383 -0.5120 -0.0098 -0.5018 546 SER B CB  
3809  O OG  . SER B 35  ? 2.5896 1.7364 2.4998 -0.5135 -0.0104 -0.5014 546 SER B OG  
3810  N N   . GLY B 36  ? 2.4625 1.6197 2.3479 -0.5148 0.0090  -0.4985 547 GLY B N   
3811  C CA  . GLY B 36  ? 2.4295 1.5949 2.3142 -0.5138 0.0106  -0.4988 547 GLY B CA  
3812  C C   . GLY B 36  ? 2.3964 1.5692 2.2721 -0.5107 0.0042  -0.4983 547 GLY B C   
3813  O O   . GLY B 36  ? 2.3978 1.5808 2.2802 -0.5075 -0.0041 -0.4998 547 GLY B O   
3814  N N   . THR B 58  ? 2.3861 1.6925 2.3104 -0.4564 -0.1163 -0.5296 569 THR B N   
3815  C CA  . THR B 58  ? 2.4439 1.7440 2.3721 -0.4563 -0.1212 -0.5332 569 THR B CA  
3816  C C   . THR B 58  ? 2.4478 1.7397 2.3749 -0.4569 -0.1209 -0.5332 569 THR B C   
3817  O O   . THR B 58  ? 2.4245 1.7139 2.3521 -0.4595 -0.1147 -0.5306 569 THR B O   
3818  C CB  . THR B 58  ? 2.4084 1.7072 2.3451 -0.4595 -0.1193 -0.5339 569 THR B CB  
3819  O OG1 . THR B 58  ? 2.3497 1.6463 2.2892 -0.4631 -0.1112 -0.5311 569 THR B OG1 
3820  C CG2 . THR B 58  ? 2.4280 1.7346 2.3660 -0.4589 -0.1202 -0.5340 569 THR B CG2 
3821  N N   . VAL B 59  ? 2.5144 1.8018 2.4397 -0.4546 -0.1275 -0.5363 570 VAL B N   
3822  C CA  . VAL B 59  ? 2.5244 1.8041 2.4487 -0.4549 -0.1277 -0.5364 570 VAL B CA  
3823  C C   . VAL B 59  ? 2.4728 1.7454 2.4043 -0.4586 -0.1255 -0.5368 570 VAL B C   
3824  O O   . VAL B 59  ? 2.3520 1.6261 2.2895 -0.4609 -0.1234 -0.5369 570 VAL B O   
3825  C CB  . VAL B 59  ? 2.6101 1.8866 2.5299 -0.4512 -0.1355 -0.5397 570 VAL B CB  
3826  C CG1 . VAL B 59  ? 2.5907 1.8610 2.5081 -0.4511 -0.1354 -0.5390 570 VAL B CG1 
3827  C CG2 . VAL B 59  ? 2.6741 1.9579 2.5882 -0.4478 -0.1380 -0.5398 570 VAL B CG2 
3828  N N   . TRP B 60  ? 2.4687 1.7335 2.4003 -0.4593 -0.1259 -0.5370 571 TRP B N   
3829  C CA  . TRP B 60  ? 2.4343 1.6914 2.3727 -0.4627 -0.1239 -0.5373 571 TRP B CA  
3830  C C   . TRP B 60  ? 2.3630 1.6211 2.3045 -0.4665 -0.1149 -0.5338 571 TRP B C   
3831  O O   . TRP B 60  ? 2.3117 1.5631 2.2571 -0.4695 -0.1112 -0.5329 571 TRP B O   
3832  C CB  . TRP B 60  ? 2.5205 1.7748 2.4648 -0.4633 -0.1292 -0.5406 571 TRP B CB  
3833  C CG  . TRP B 60  ? 2.5761 1.8208 2.5264 -0.4660 -0.1300 -0.5416 571 TRP B CG  
3834  C CD1 . TRP B 60  ? 2.6374 1.8746 2.5861 -0.4657 -0.1322 -0.5422 571 TRP B CD1 
3835  C CD2 . TRP B 60  ? 2.5819 1.8231 2.5414 -0.4696 -0.1289 -0.5420 571 TRP B CD2 
3836  N NE1 . TRP B 60  ? 2.6410 1.8703 2.5972 -0.4690 -0.1324 -0.5429 571 TRP B NE1 
3837  C CE2 . TRP B 60  ? 2.6015 1.8330 2.5645 -0.4714 -0.1304 -0.5428 571 TRP B CE2 
3838  C CE3 . TRP B 60  ? 2.5715 1.8167 2.5370 -0.4716 -0.1269 -0.5418 571 TRP B CE3 
3839  C CZ2 . TRP B 60  ? 2.5884 1.8142 2.5609 -0.4752 -0.1300 -0.5432 571 TRP B CZ2 
3840  C CZ3 . TRP B 60  ? 2.5715 1.8110 2.5465 -0.4753 -0.1264 -0.5422 571 TRP B CZ3 
3841  C CH2 . TRP B 60  ? 2.5772 1.8071 2.5557 -0.4772 -0.1279 -0.5429 571 TRP B CH2 
3842  N N   . GLY B 61  ? 2.5914 1.8574 2.5309 -0.4663 -0.1111 -0.5319 572 GLY B N   
3843  C CA  . GLY B 61  ? 2.5145 1.7813 2.4548 -0.4695 -0.1023 -0.5286 572 GLY B CA  
3844  C C   . GLY B 61  ? 2.4887 1.7565 2.4205 -0.4685 -0.0996 -0.5259 572 GLY B C   
3845  O O   . GLY B 61  ? 2.4927 1.7581 2.4226 -0.4711 -0.0927 -0.5231 572 GLY B O   
3846  N N   . ILE B 62  ? 2.3287 1.5996 2.2550 -0.4649 -0.1052 -0.5267 573 ILE B N   
3847  C CA  . ILE B 62  ? 2.2846 1.5559 2.2034 -0.4639 -0.1039 -0.5241 573 ILE B CA  
3848  C C   . ILE B 62  ? 2.3040 1.5670 2.2218 -0.4643 -0.1050 -0.5242 573 ILE B C   
3849  O O   . ILE B 62  ? 2.3163 1.5775 2.2285 -0.4644 -0.1031 -0.5217 573 ILE B O   
3850  C CB  . ILE B 62  ? 2.3027 1.5807 2.2169 -0.4598 -0.1095 -0.5248 573 ILE B CB  
3851  C CG1 . ILE B 62  ? 2.2995 1.5797 2.2066 -0.4591 -0.1078 -0.5216 573 ILE B CG1 
3852  C CG2 . ILE B 62  ? 2.3886 1.6630 2.3033 -0.4571 -0.1172 -0.5284 573 ILE B CG2 
3853  C CD1 . ILE B 62  ? 2.3623 1.6490 2.2657 -0.4553 -0.1131 -0.5222 573 ILE B CD1 
3854  N N   . LYS B 63  ? 2.3251 1.5824 2.2481 -0.4645 -0.1085 -0.5270 574 LYS B N   
3855  C CA  . LYS B 63  ? 2.3322 1.5811 2.2551 -0.4650 -0.1099 -0.5272 574 LYS B CA  
3856  C C   . LYS B 63  ? 2.2879 1.5313 2.2112 -0.4690 -0.1023 -0.5243 574 LYS B C   
3857  O O   . LYS B 63  ? 2.2905 1.5287 2.2103 -0.4694 -0.1017 -0.5229 574 LYS B O   
3858  C CB  . LYS B 63  ? 2.3525 1.5965 2.2803 -0.4642 -0.1163 -0.5310 574 LYS B CB  
3859  C CG  . LYS B 63  ? 2.3892 1.6266 2.3142 -0.4631 -0.1194 -0.5313 574 LYS B CG  
3860  C CD  . LYS B 63  ? 2.4519 1.6941 2.3699 -0.4590 -0.1239 -0.5315 574 LYS B CD  
3861  C CE  . LYS B 63  ? 2.5061 1.7424 2.4214 -0.4573 -0.1283 -0.5322 574 LYS B CE  
3862  N NZ  . LYS B 63  ? 2.5770 1.8181 2.4864 -0.4533 -0.1323 -0.5325 574 LYS B NZ  
3863  N N   . GLN B 64  ? 2.3322 1.5764 2.2595 -0.4719 -0.0965 -0.5235 575 GLN B N   
3864  C CA  . GLN B 64  ? 2.3370 1.5753 2.2644 -0.4758 -0.0886 -0.5210 575 GLN B CA  
3865  C C   . GLN B 64  ? 2.3317 1.5727 2.2507 -0.4762 -0.0834 -0.5176 575 GLN B C   
3866  O O   . GLN B 64  ? 2.3365 1.5715 2.2520 -0.4788 -0.0779 -0.5154 575 GLN B O   
3867  C CB  . GLN B 64  ? 2.3397 1.5772 2.2750 -0.4788 -0.0841 -0.5214 575 GLN B CB  
3868  C CG  . GLN B 64  ? 2.3315 1.5779 2.2682 -0.4783 -0.0830 -0.5216 575 GLN B CG  
3869  C CD  . GLN B 64  ? 2.3272 1.5759 2.2583 -0.4800 -0.0750 -0.5184 575 GLN B CD  
3870  O OE1 . GLN B 64  ? 2.3319 1.5745 2.2592 -0.4824 -0.0692 -0.5162 575 GLN B OE1 
3871  N NE2 . GLN B 64  ? 2.3188 1.5758 2.2490 -0.4788 -0.0749 -0.5182 575 GLN B NE2 
3872  N N   . LEU B 65  ? 1.9882 1.0458 1.7632 -0.2961 0.1100  -0.0286 576 LEU B N   
3873  C CA  . LEU B 65  ? 1.9589 1.0420 1.7612 -0.2953 0.1167  -0.0232 576 LEU B CA  
3874  C C   . LEU B 65  ? 1.9423 1.0406 1.7746 -0.2951 0.1196  -0.0232 576 LEU B C   
3875  O O   . LEU B 65  ? 1.9077 1.0379 1.7738 -0.2987 0.1139  -0.0198 576 LEU B O   
3876  C CB  . LEU B 65  ? 1.9920 1.0494 1.7615 -0.2937 0.1385  -0.0221 576 LEU B CB  
3877  C CG  . LEU B 65  ? 1.9639 1.0470 1.7641 -0.2933 0.1461  -0.0182 576 LEU B CG  
3878  C CD1 . LEU B 65  ? 1.9825 1.0512 1.7642 -0.2926 0.1563  -0.0133 576 LEU B CD1 
3879  C CD2 . LEU B 65  ? 1.9989 1.0767 1.8029 -0.2912 0.1650  -0.0210 576 LEU B CD2 
3880  N N   . GLN B 66  ? 2.0207 1.0907 1.8328 -0.2931 0.1325  -0.0283 577 GLN B N   
3881  C CA  . GLN B 66  ? 2.1224 1.2023 1.9596 -0.2927 0.1373  -0.0279 577 GLN B CA  
3882  C C   . GLN B 66  ? 2.0851 1.1914 1.9624 -0.2959 0.1159  -0.0226 577 GLN B C   
3883  O O   . GLN B 66  ? 2.1536 1.2775 2.0577 -0.2984 0.1174  -0.0183 577 GLN B O   
3884  C CB  . GLN B 66  ? 2.2852 1.3270 2.0928 -0.2901 0.1541  -0.0357 577 GLN B CB  
3885  C CG  . GLN B 66  ? 2.4422 1.4900 2.2708 -0.2889 0.1646  -0.0355 577 GLN B CG  
3886  C CD  . GLN B 66  ? 2.6508 1.6651 2.4461 -0.2852 0.1921  -0.0428 577 GLN B CD  
3887  O OE1 . GLN B 66  ? 2.7641 1.7486 2.5178 -0.2843 0.2043  -0.0470 577 GLN B OE1 
3888  N NE2 . GLN B 66  ? 2.7355 1.7531 2.5475 -0.2836 0.2032  -0.0436 577 GLN B NE2 
3889  N N   . ALA B 67  ? 2.1285 1.2357 2.0077 -0.2972 0.0991  -0.0224 578 ALA B N   
3890  C CA  . ALA B 67  ? 2.0838 1.2124 2.0001 -0.3011 0.0813  -0.0161 578 ALA B CA  
3891  C C   . ALA B 67  ? 1.9614 1.1275 1.9031 -0.3063 0.0737  -0.0088 578 ALA B C   
3892  O O   . ALA B 67  ? 1.9225 1.1149 1.9002 -0.3110 0.0659  -0.0001 578 ALA B O   
3893  C CB  . ALA B 67  ? 2.0284 1.1432 1.9386 -0.3003 0.0688  -0.0206 578 ALA B CB  
3894  N N   . ARG B 68  ? 2.0577 1.2265 1.9816 -0.3061 0.0759  -0.0118 579 ARG B N   
3895  C CA  . ARG B 68  ? 1.9487 1.1517 1.8951 -0.3113 0.0692  -0.0082 579 ARG B CA  
3896  C C   . ARG B 68  ? 1.9573 1.1771 1.9165 -0.3145 0.0809  -0.0079 579 ARG B C   
3897  O O   . ARG B 68  ? 1.8635 1.1168 1.8487 -0.3210 0.0751  -0.0059 579 ARG B O   
3898  C CB  . ARG B 68  ? 1.9340 1.1280 1.8549 -0.3096 0.0692  -0.0122 579 ARG B CB  
3899  C CG  . ARG B 68  ? 1.8917 1.1126 1.8287 -0.3136 0.0564  -0.0108 579 ARG B CG  
3900  C CD  . ARG B 68  ? 1.9209 1.1229 1.8257 -0.3107 0.0585  -0.0137 579 ARG B CD  
3901  N NE  . ARG B 68  ? 1.9816 1.1744 1.8752 -0.3093 0.0733  -0.0145 579 ARG B NE  
3902  C CZ  . ARG B 68  ? 2.0177 1.1965 1.8908 -0.3073 0.0768  -0.0136 579 ARG B CZ  
3903  N NH1 . ARG B 68  ? 1.9940 1.1665 1.8508 -0.3069 0.0660  -0.0131 579 ARG B NH1 
3904  N NH2 . ARG B 68  ? 2.0890 1.2599 1.9589 -0.3059 0.0916  -0.0125 579 ARG B NH2 
3905  N N   . VAL B 69  ? 1.7485 0.9469 1.6906 -0.3106 0.0983  -0.0113 580 VAL B N   
3906  C CA  . VAL B 69  ? 1.7373 0.9519 1.6936 -0.3136 0.1118  -0.0125 580 VAL B CA  
3907  C C   . VAL B 69  ? 1.7209 0.9542 1.7058 -0.3182 0.1062  -0.0056 580 VAL B C   
3908  O O   . VAL B 69  ? 1.6931 0.9592 1.7037 -0.3257 0.1057  -0.0033 580 VAL B O   
3909  C CB  . VAL B 69  ? 1.7691 0.9550 1.6984 -0.3070 0.1350  -0.0184 580 VAL B CB  
3910  C CG1 . VAL B 69  ? 1.7619 0.9612 1.7075 -0.3089 0.1508  -0.0204 580 VAL B CG1 
3911  C CG2 . VAL B 69  ? 1.7773 0.9554 1.6898 -0.3050 0.1423  -0.0215 580 VAL B CG2 
3912  N N   . LEU B 70  ? 1.7990 1.0131 1.7819 -0.3150 0.1015  -0.0018 581 LEU B N   
3913  C CA  . LEU B 70  ? 1.8049 1.0345 1.8174 -0.3198 0.0949  0.0084  581 LEU B CA  
3914  C C   . LEU B 70  ? 1.7264 0.9908 1.7734 -0.3280 0.0735  0.0204  581 LEU B C   
3915  O O   . LEU B 70  ? 1.7273 1.0148 1.8003 -0.3366 0.0709  0.0314  581 LEU B O   
3916  C CB  . LEU B 70  ? 1.8570 1.0543 1.8607 -0.3142 0.0958  0.0084  581 LEU B CB  
3917  C CG  . LEU B 70  ? 1.9565 1.1603 1.9876 -0.3184 0.0912  0.0201  581 LEU B CG  
3918  C CD1 . LEU B 70  ? 2.1710 1.3405 2.1844 -0.3118 0.1078  0.0125  581 LEU B CD1 
3919  C CD2 . LEU B 70  ? 1.9035 1.1149 1.9606 -0.3222 0.0674  0.0323  581 LEU B CD2 
3920  N N   . ALA B 71  ? 1.8665 1.1343 1.9119 -0.3271 0.0620  0.0185  582 ALA B N   
3921  C CA  . ALA B 71  ? 1.7646 1.0674 1.8462 -0.3338 0.0439  0.0294  582 ALA B CA  
3922  C C   . ALA B 71  ? 1.6956 1.0388 1.7958 -0.3439 0.0455  0.0311  582 ALA B C   
3923  O O   . ALA B 71  ? 1.6852 1.0601 1.8162 -0.3550 0.0393  0.0432  582 ALA B O   
3924  C CB  . ALA B 71  ? 1.7594 1.0559 1.8326 -0.3296 0.0363  0.0235  582 ALA B CB  
3925  N N   . VAL B 72  ? 1.6231 0.9644 1.7031 -0.3428 0.0577  0.0181  583 VAL B N   
3926  C CA  . VAL B 72  ? 1.6123 0.9906 1.7079 -0.3541 0.0631  0.0140  583 VAL B CA  
3927  C C   . VAL B 72  ? 1.6694 1.0547 1.7698 -0.3606 0.0812  0.0137  583 VAL B C   
3928  O O   . VAL B 72  ? 1.6621 1.0873 1.7855 -0.3740 0.0865  0.0128  583 VAL B O   
3929  C CB  . VAL B 72  ? 1.6185 0.9932 1.6976 -0.3506 0.0702  -0.0000 583 VAL B CB  
3930  C CG1 . VAL B 72  ? 1.5759 0.9434 1.6477 -0.3467 0.0572  -0.0010 583 VAL B CG1 
3931  C CG2 . VAL B 72  ? 1.6912 1.0291 1.7400 -0.3420 0.0914  -0.0084 583 VAL B CG2 
3932  N N   . GLU B 73  ? 1.6474 0.9984 1.7291 -0.3518 0.0928  0.0129  584 GLU B N   
3933  C CA  . GLU B 73  ? 1.7079 1.0665 1.7986 -0.3568 0.1114  0.0130  584 GLU B CA  
3934  C C   . GLU B 73  ? 1.6915 1.0725 1.8100 -0.3675 0.1014  0.0310  584 GLU B C   
3935  O O   . GLU B 73  ? 1.7129 1.1256 1.8536 -0.3789 0.1134  0.0339  584 GLU B O   
3936  C CB  . GLU B 73  ? 1.7861 1.1028 1.8515 -0.3441 0.1265  0.0077  584 GLU B CB  
3937  C CG  . GLU B 73  ? 1.8230 1.1209 1.8641 -0.3355 0.1424  -0.0068 584 GLU B CG  
3938  C CD  . GLU B 73  ? 1.9083 1.1677 1.9254 -0.3246 0.1583  -0.0106 584 GLU B CD  
3939  O OE1 . GLU B 73  ? 1.9325 1.1752 1.9486 -0.3220 0.1529  -0.0038 584 GLU B OE1 
3940  O OE2 . GLU B 73  ? 1.9718 1.2181 1.9731 -0.3189 0.1767  -0.0202 584 GLU B OE2 
3941  N N   . ARG B 74  ? 1.6759 1.0435 1.7973 -0.3645 0.0808  0.0438  585 ARG B N   
3942  C CA  . ARG B 74  ? 1.6624 1.0510 1.8122 -0.3756 0.0693  0.0654  585 ARG B CA  
3943  C C   . ARG B 74  ? 1.5996 1.0424 1.7794 -0.3914 0.0610  0.0730  585 ARG B C   
3944  O O   . ARG B 74  ? 1.6056 1.0852 1.8118 -0.4070 0.0612  0.0903  585 ARG B O   
3945  C CB  . ARG B 74  ? 1.6496 1.0076 1.7977 -0.3674 0.0507  0.0749  585 ARG B CB  
3946  C CG  . ARG B 74  ? 1.6461 1.0241 1.8169 -0.3783 0.0386  0.0990  585 ARG B CG  
3947  C CD  . ARG B 74  ? 1.6943 1.0303 1.8517 -0.3703 0.0340  0.1028  585 ARG B CD  
3948  N NE  . ARG B 74  ? 1.7141 1.0624 1.8713 -0.3820 0.0267  0.1235  585 ARG B NE  
3949  C CZ  . ARG B 74  ? 1.7630 1.0743 1.9035 -0.3796 0.0236  0.1269  585 ARG B CZ  
3950  N NH1 . ARG B 74  ? 1.8627 1.1330 1.9994 -0.3642 0.0232  0.1119  585 ARG B NH1 
3951  N NH2 . ARG B 74  ? 1.8082 1.1192 1.9304 -0.3952 0.0312  0.1400  585 ARG B NH2 
3952  N N   . TYR B 75  ? 1.6154 1.0680 1.7921 -0.3886 0.0552  0.0606  586 TYR B N   
3953  C CA  . TYR B 75  ? 1.5596 1.0672 1.7675 -0.4026 0.0487  0.0637  586 TYR B CA  
3954  C C   . TYR B 75  ? 1.5883 1.1387 1.8074 -0.4170 0.0678  0.0536  586 TYR B C   
3955  O O   . TYR B 75  ? 1.5724 1.1797 1.8278 -0.4338 0.0685  0.0652  586 TYR B O   
3956  C CB  . TYR B 75  ? 1.5098 1.0129 1.7100 -0.3941 0.0389  0.0505  586 TYR B CB  
3957  C CG  . TYR B 75  ? 1.4667 1.0267 1.6970 -0.4069 0.0346  0.0474  586 TYR B CG  
3958  C CD1 . TYR B 75  ? 1.4817 1.0790 1.7482 -0.4082 0.0283  0.0592  586 TYR B CD1 
3959  C CD2 . TYR B 75  ? 1.4740 1.0554 1.6959 -0.4130 0.0428  0.0276  586 TYR B CD2 
3960  C CE1 . TYR B 75  ? 1.4866 1.1405 1.7806 -0.4194 0.0282  0.0517  586 TYR B CE1 
3961  C CE2 . TYR B 75  ? 1.4391 1.0768 1.6881 -0.4250 0.0380  0.0214  586 TYR B CE2 
3962  C CZ  . TYR B 75  ? 1.4833 1.1577 1.7692 -0.4298 0.0284  0.0344  586 TYR B CZ  
3963  O OH  . TYR B 75  ? 1.4702 1.2064 1.7822 -0.4407 0.0252  0.0248  586 TYR B OH  
3964  N N   . LEU B 76  ? 1.5996 1.1302 1.7951 -0.4102 0.0855  0.0319  587 LEU B N   
3965  C CA  . LEU B 76  ? 1.5854 1.1593 1.8000 -0.4218 0.1069  0.0177  587 LEU B CA  
3966  C C   . LEU B 76  ? 1.5893 1.1787 1.8230 -0.4285 0.1209  0.0293  587 LEU B C   
3967  O O   . LEU B 76  ? 1.5676 1.2155 1.8344 -0.4425 0.1346  0.0242  587 LEU B O   
3968  C CB  . LEU B 76  ? 1.5984 1.1470 1.7903 -0.4116 0.1243  -0.0070 587 LEU B CB  
3969  C CG  . LEU B 76  ? 1.5895 1.1376 1.7718 -0.4085 0.1123  -0.0172 587 LEU B CG  
3970  C CD1 . LEU B 76  ? 1.6018 1.1311 1.7695 -0.4001 0.1314  -0.0381 587 LEU B CD1 
3971  C CD2 . LEU B 76  ? 1.5542 1.1687 1.7710 -0.4257 0.1031  -0.0192 587 LEU B CD2 
3972  N N   . ARG B 77  ? 1.6856 1.2286 1.9025 -0.4186 0.1181  0.0436  588 ARG B N   
3973  C CA  . ARG B 77  ? 1.7408 1.2974 1.9775 -0.4245 0.1306  0.0574  588 ARG B CA  
3974  C C   . ARG B 77  ? 1.6997 1.3217 1.9771 -0.4446 0.1205  0.0810  588 ARG B C   
3975  O O   . ARG B 77  ? 1.7615 1.4425 2.0745 -0.4576 0.1351  0.0857  588 ARG B O   
3976  C CB  . ARG B 77  ? 1.7878 1.2831 1.9995 -0.4099 0.1271  0.0673  588 ARG B CB  
3977  C CG  . ARG B 77  ? 1.8540 1.3594 2.0863 -0.4146 0.1403  0.0829  588 ARG B CG  
3978  C CD  . ARG B 77  ? 1.9006 1.3552 2.1156 -0.4045 0.1305  0.0962  588 ARG B CD  
3979  N NE  . ARG B 77  ? 1.8250 1.2644 2.0286 -0.4054 0.1029  0.1072  588 ARG B NE  
3980  C CZ  . ARG B 77  ? 1.8081 1.2610 2.0210 -0.4181 0.0912  0.1305  588 ARG B CZ  
3981  N NH1 . ARG B 77  ? 1.9159 1.4018 2.1530 -0.4296 0.1075  0.1457  588 ARG B NH1 
3982  N NH2 . ARG B 77  ? 1.7656 1.2017 1.9617 -0.4175 0.0676  0.1363  588 ARG B NH2 
3983  N N   . ASP B 78  ? 1.6847 1.3040 1.9611 -0.4470 0.0955  0.0975  589 ASP B N   
3984  C CA  . ASP B 78  ? 1.6662 1.3539 1.9791 -0.4666 0.0851  0.1225  589 ASP B CA  
3985  C C   . ASP B 78  ? 1.5930 1.3612 1.9479 -0.4777 0.0889  0.1104  589 ASP B C   
3986  O O   . ASP B 78  ? 1.6026 1.4565 2.0024 -0.4895 0.0936  0.1236  589 ASP B O   
3987  C CB  . ASP B 78  ? 1.6024 1.2678 1.8948 -0.4570 0.0608  0.1351  589 ASP B CB  
3988  C CG  . ASP B 78  ? 1.7134 1.3115 1.9590 -0.4522 0.0599  0.1437  589 ASP B CG  
3989  O OD1 . ASP B 78  ? 1.8431 1.4350 2.0909 -0.4588 0.0799  0.1497  589 ASP B OD1 
3990  O OD2 . ASP B 78  ? 1.6651 1.2208 1.8861 -0.4384 0.0410  0.1433  589 ASP B OD2 
3991  N N   . GLN B 79  ? 1.6053 1.3543 1.9407 -0.4692 0.0892  0.0811  590 GLN B N   
3992  C CA  . GLN B 79  ? 1.5768 1.3987 1.9409 -0.4794 0.0936  0.0615  590 GLN B CA  
3993  C C   . GLN B 79  ? 1.6306 1.4997 2.0140 -0.4868 0.1179  0.0455  590 GLN B C   
3994  O O   . GLN B 79  ? 1.6635 1.6232 2.0886 -0.4980 0.1207  0.0389  590 GLN B O   
3995  C CB  . GLN B 79  ? 1.5572 1.3421 1.8885 -0.4698 0.0874  0.0355  590 GLN B CB  
3996  C CG  . GLN B 79  ? 1.4954 1.2662 1.8267 -0.4641 0.0642  0.0466  590 GLN B CG  
3997  C CD  . GLN B 79  ? 1.4433 1.3003 1.8284 -0.4755 0.0584  0.0537  590 GLN B CD  
3998  O OE1 . GLN B 79  ? 1.4483 1.3800 1.8583 -0.4871 0.0656  0.0403  590 GLN B OE1 
3999  N NE2 . GLN B 79  ? 1.4305 1.2815 1.8323 -0.4671 0.0533  0.0665  590 GLN B NE2 
4000  N N   . GLN B 80  ? 1.5665 1.3809 1.9243 -0.4776 0.1360  0.0371  591 GLN B N   
4001  C CA  . GLN B 80  ? 1.6237 1.4823 2.0061 -0.4826 0.1607  0.0216  591 GLN B CA  
4002  C C   . GLN B 80  ? 1.6310 1.5631 2.0601 -0.4947 0.1621  0.0501  591 GLN B C   
4003  O O   . GLN B 80  ? 1.6384 1.6612 2.1101 -0.5038 0.1710  0.0431  591 GLN B O   
4004  C CB  . GLN B 80  ? 1.6995 1.4825 2.0480 -0.4671 0.1808  0.0067  591 GLN B CB  
4005  C CG  . GLN B 80  ? 1.7631 1.5884 2.1382 -0.4707 0.2076  -0.0143 591 GLN B CG  
4006  C CD  . GLN B 80  ? 1.8487 1.6020 2.1949 -0.4544 0.2281  -0.0253 591 GLN B CD  
4007  O OE1 . GLN B 80  ? 1.9473 1.6293 2.2580 -0.4409 0.2220  -0.0123 591 GLN B OE1 
4008  N NE2 . GLN B 80  ? 1.9496 1.7258 2.3125 -0.4545 0.2520  -0.0506 591 GLN B NE2 
4009  N N   . LEU B 81  ? 1.6129 1.5107 2.0346 -0.4933 0.1532  0.0827  592 LEU B N   
4010  C CA  . LEU B 81  ? 1.6203 1.5909 2.0849 -0.5057 0.1531  0.1167  592 LEU B CA  
4011  C C   . LEU B 81  ? 1.5607 1.6349 2.0788 -0.5142 0.1374  0.1314  592 LEU B C   
4012  O O   . LEU B 81  ? 1.5783 1.7518 2.1558 -0.5116 0.1458  0.1415  592 LEU B O   
4013  C CB  . LEU B 81  ? 1.6439 1.5466 2.0746 -0.5039 0.1469  0.1423  592 LEU B CB  
4014  C CG  . LEU B 81  ? 1.7228 1.5290 2.1193 -0.4842 0.1606  0.1329  592 LEU B CG  
4015  C CD1 . LEU B 81  ? 1.7482 1.5006 2.1216 -0.4795 0.1542  0.1550  592 LEU B CD1 
4016  C CD2 . LEU B 81  ? 1.8065 1.6447 2.2308 -0.4828 0.1866  0.1258  592 LEU B CD2 
4017  N N   . LEU B 82  ? 1.6935 1.7426 2.2020 -0.5075 0.1206  0.1253  593 LEU B N   
4018  C CA  . LEU B 82  ? 1.5875 1.7157 2.1538 -0.5017 0.1235  0.1159  593 LEU B CA  
4019  C C   . LEU B 82  ? 1.6334 1.8456 2.2147 -0.5119 0.1233  0.0896  593 LEU B C   
4020  O O   . LEU B 82  ? 1.6211 1.9247 2.2348 -0.5126 0.1214  0.0828  593 LEU B O   
4021  C CB  . LEU B 82  ? 1.4627 1.5340 1.9998 -0.4960 0.1107  0.1063  593 LEU B CB  
4022  C CG  . LEU B 82  ? 1.4252 1.5572 1.9701 -0.5066 0.1103  0.1008  593 LEU B CG  
4023  C CD1 . LEU B 82  ? 1.4056 1.5638 1.9457 -0.5119 0.1131  0.1325  593 LEU B CD1 
4024  C CD2 . LEU B 82  ? 1.3838 1.4500 1.8914 -0.5009 0.0947  0.0928  593 LEU B CD2 
4025  N N   . GLY B 83  ? 1.7940 1.9719 2.3367 -0.5145 0.1309  0.0626  594 GLY B N   
4026  C CA  . GLY B 83  ? 1.7976 2.0400 2.3498 -0.5167 0.1381  0.0265  594 GLY B CA  
4027  C C   . GLY B 83  ? 1.8776 2.1907 2.4644 -0.5177 0.1556  0.0257  594 GLY B C   
4028  O O   . GLY B 83  ? 1.9463 2.3570 2.5654 -0.5171 0.1550  0.0127  594 GLY B O   
4029  N N   . ILE B 84  ? 1.6395 1.9028 2.2159 -0.5170 0.1706  0.0381  595 ILE B N   
4030  C CA  . ILE B 84  ? 1.6867 2.0131 2.2955 -0.5166 0.1880  0.0383  595 ILE B CA  
4031  C C   . ILE B 84  ? 1.7060 2.1312 2.3757 -0.5137 0.1826  0.0750  595 ILE B C   
4032  O O   . ILE B 84  ? 1.8304 2.3362 2.5355 -0.5096 0.1930  0.0726  595 ILE B O   
4033  C CB  . ILE B 84  ? 1.7434 1.9862 2.3248 -0.5139 0.2070  0.0413  595 ILE B CB  
4034  C CG1 . ILE B 84  ? 1.7744 1.9597 2.3423 -0.5139 0.1976  0.0827  595 ILE B CG1 
4035  C CG2 . ILE B 84  ? 1.8529 2.0007 2.3858 -0.5072 0.2197  0.0009  595 ILE B CG2 
4036  C CD1 . ILE B 84  ? 1.8733 1.9608 2.4051 -0.5054 0.2148  0.0808  595 ILE B CD1 
4037  N N   . TRP B 85  ? 2.4698 1.8453 2.3376 -0.3176 0.4257  0.7720  596 TRP B N   
4038  C CA  . TRP B 85  ? 2.5589 1.9107 2.3703 -0.3507 0.4116  0.7641  596 TRP B CA  
4039  C C   . TRP B 85  ? 2.6022 1.9679 2.4386 -0.3642 0.4461  0.7598  596 TRP B C   
4040  O O   . TRP B 85  ? 2.5774 1.9692 2.4727 -0.3466 0.4798  0.7622  596 TRP B O   
4041  C CB  . TRP B 85  ? 2.4955 1.8436 2.2598 -0.3637 0.3831  0.7733  596 TRP B CB  
4042  C CG  . TRP B 85  ? 2.5272 1.8586 2.2642 -0.3487 0.3510  0.7741  596 TRP B CG  
4043  C CD1 . TRP B 85  ? 2.6055 1.9200 2.3440 -0.3341 0.3408  0.7661  596 TRP B CD1 
4044  C CD2 . TRP B 85  ? 2.5100 1.8417 2.2179 -0.3447 0.3276  0.7819  596 TRP B CD2 
4045  N NE1 . TRP B 85  ? 2.6167 1.9207 2.3271 -0.3228 0.3121  0.7681  596 TRP B NE1 
4046  C CE2 . TRP B 85  ? 2.5642 1.8786 2.2564 -0.3272 0.3040  0.7774  596 TRP B CE2 
4047  C CE3 . TRP B 85  ? 2.4910 1.8376 2.1879 -0.3527 0.3259  0.7916  596 TRP B CE3 
4048  C CZ2 . TRP B 85  ? 2.5413 1.8541 2.2085 -0.3157 0.2794  0.7816  596 TRP B CZ2 
4049  C CZ3 . TRP B 85  ? 2.5274 1.8732 2.2015 -0.3404 0.3009  0.7967  596 TRP B CZ3 
4050  C CH2 . TRP B 85  ? 2.5237 1.8536 2.1840 -0.3214 0.2780  0.7914  596 TRP B CH2 
4051  N N   . GLY B 86  ? 2.5312 1.8791 2.3226 -0.3957 0.4382  0.7530  597 GLY B N   
4052  C CA  . GLY B 86  ? 2.5889 1.9522 2.4045 -0.4089 0.4716  0.7478  597 GLY B CA  
4053  C C   . GLY B 86  ? 2.5470 1.9419 2.3764 -0.4177 0.4828  0.7605  597 GLY B C   
4054  O O   . GLY B 86  ? 2.6118 2.0078 2.4171 -0.4467 0.4866  0.7582  597 GLY B O   
4055  N N   . CYS B 87  ? 2.2467 1.6694 2.1181 -0.3927 0.4887  0.7744  598 CYS B N   
4056  C CA  . CYS B 87  ? 2.2523 1.7071 2.1411 -0.3989 0.4977  0.7879  598 CYS B CA  
4057  C C   . CYS B 87  ? 2.2332 1.7253 2.2016 -0.3705 0.5316  0.7966  598 CYS B C   
4058  O O   . CYS B 87  ? 2.2418 1.7517 2.2440 -0.3764 0.5652  0.7917  598 CYS B O   
4059  C CB  . CYS B 87  ? 2.2538 1.7034 2.1013 -0.4026 0.4625  0.7992  598 CYS B CB  
4060  S SG  . CYS B 87  ? 2.2846 1.6803 2.0346 -0.4365 0.4289  0.7849  598 CYS B SG  
4061  N N   . SER B 88  ? 2.0343 1.5370 2.0321 -0.3398 0.5231  0.8090  599 SER B N   
4062  C CA  . SER B 88  ? 2.0185 1.5551 2.0895 -0.3119 0.5511  0.8212  599 SER B CA  
4063  C C   . SER B 88  ? 2.0271 1.5977 2.1189 -0.3227 0.5620  0.8341  599 SER B C   
4064  O O   . SER B 88  ? 2.0147 1.6092 2.1318 -0.3066 0.5536  0.8531  599 SER B O   
4065  C CB  . SER B 88  ? 2.0172 1.5513 2.1298 -0.3002 0.5883  0.8077  599 SER B CB  
4066  O OG  . SER B 88  ? 2.0043 1.5665 2.1859 -0.2717 0.6147  0.8195  599 SER B OG  
4067  N N   . GLY B 89  ? 2.0482 1.6230 2.1327 -0.3495 0.5818  0.8238  600 GLY B N   
4068  C CA  . GLY B 89  ? 2.0589 1.6642 2.1543 -0.3653 0.5890  0.8340  600 GLY B CA  
4069  C C   . GLY B 89  ? 2.0634 1.6608 2.1050 -0.3787 0.5499  0.8436  600 GLY B C   
4070  O O   . GLY B 89  ? 2.0792 1.6426 2.0522 -0.4017 0.5253  0.8330  600 GLY B O   
4071  N N   . LYS B 90  ? 2.0505 1.6784 2.1238 -0.3634 0.5442  0.8637  601 LYS B N   
4072  C CA  . LYS B 90  ? 2.0492 1.6728 2.0815 -0.3670 0.5071  0.8742  601 LYS B CA  
4073  C C   . LYS B 90  ? 2.0766 1.6948 2.0565 -0.4042 0.4981  0.8695  601 LYS B C   
4074  O O   . LYS B 90  ? 2.1009 1.7056 2.0550 -0.4330 0.5133  0.8541  601 LYS B O   
4075  C CB  . LYS B 90  ? 2.0265 1.6880 2.1169 -0.3375 0.5066  0.8979  601 LYS B CB  
4076  C CG  . LYS B 90  ? 2.0035 1.6690 2.1467 -0.3002 0.5183  0.9036  601 LYS B CG  
4077  C CD  . LYS B 90  ? 1.9870 1.6923 2.1950 -0.2736 0.5255  0.9279  601 LYS B CD  
4078  C CE  . LYS B 90  ? 1.9705 1.6759 2.2302 -0.2385 0.5424  0.9322  601 LYS B CE  
4079  N NZ  . LYS B 90  ? 1.9576 1.6982 2.2812 -0.2116 0.5503  0.9570  601 LYS B NZ  
4080  N N   . LEU B 91  ? 2.0740 1.7013 2.0366 -0.4034 0.4731  0.8822  602 LEU B N   
4081  C CA  . LEU B 91  ? 2.1001 1.7206 2.0116 -0.4348 0.4628  0.8788  602 LEU B CA  
4082  C C   . LEU B 91  ? 2.1278 1.6924 1.9543 -0.4591 0.4467  0.8580  602 LEU B C   
4083  O O   . LEU B 91  ? 2.1276 1.6638 1.9058 -0.4527 0.4153  0.8563  602 LEU B O   
4084  C CB  . LEU B 91  ? 2.1148 1.7705 2.0623 -0.4556 0.4970  0.8800  602 LEU B CB  
4085  C CG  . LEU B 91  ? 2.0909 1.8017 2.1227 -0.4314 0.5138  0.9015  602 LEU B CG  
4086  C CD1 . LEU B 91  ? 2.1073 1.8536 2.1709 -0.4550 0.5463  0.9004  602 LEU B CD1 
4087  C CD2 . LEU B 91  ? 2.0744 1.7963 2.1018 -0.4142 0.4806  0.9201  602 LEU B CD2 
4088  N N   . ILE B 92  ? 2.1520 1.7001 1.9611 -0.4850 0.4687  0.8419  603 ILE B N   
4089  C CA  . ILE B 92  ? 2.1833 1.6736 1.9122 -0.5074 0.4581  0.8221  603 ILE B CA  
4090  C C   . ILE B 92  ? 2.1842 1.6584 1.9168 -0.5127 0.4697  0.8091  603 ILE B C   
4091  O O   . ILE B 92  ? 2.1700 1.6802 1.9658 -0.5072 0.4966  0.8116  603 ILE B O   
4092  C CB  . ILE B 92  ? 2.2219 1.7007 1.9126 -0.5393 0.4735  0.8138  603 ILE B CB  
4093  C CG1 . ILE B 92  ? 2.2297 1.7487 1.9653 -0.5627 0.5077  0.8123  603 ILE B CG1 
4094  C CG2 . ILE B 92  ? 2.2166 1.7139 1.9048 -0.5310 0.4564  0.8278  603 ILE B CG2 
4095  C CD1 . ILE B 92  ? 2.2584 1.7498 1.9595 -0.5940 0.5217  0.7923  603 ILE B CD1 
4096  N N   . CYS B 93  ? 2.3075 1.7263 1.9770 -0.5177 0.4522  0.7945  604 CYS B N   
4097  C CA  . CYS B 93  ? 2.3090 1.7126 1.9751 -0.5277 0.4548  0.7829  604 CYS B CA  
4098  C C   . CYS B 93  ? 2.3328 1.6747 1.9269 -0.5271 0.4381  0.7581  604 CYS B C   
4099  O O   . CYS B 93  ? 2.3251 1.6413 1.9037 -0.4944 0.4310  0.7617  604 CYS B O   
4100  C CB  . CYS B 93  ? 2.2671 1.6931 1.9956 -0.4906 0.4554  0.7902  604 CYS B CB  
4101  S SG  . CYS B 93  ? 2.2592 1.6546 1.9775 -0.4856 0.4467  0.7770  604 CYS B SG  
4102  N N   . CYS B 94  ? 2.4071 1.7596 1.9964 -0.5543 0.4253  0.7489  605 CYS B N   
4103  C CA  . CYS B 94  ? 2.3433 1.7285 2.0428 -0.4818 0.4439  0.7836  605 CYS B CA  
4104  C C   . CYS B 94  ? 2.3109 1.7073 2.0262 -0.4815 0.4064  0.7875  605 CYS B C   
4105  O O   . CYS B 94  ? 2.3433 1.7090 1.9934 -0.5273 0.3898  0.7633  605 CYS B O   
4106  C CB  . CYS B 94  ? 2.3731 1.7617 2.0519 -0.5228 0.4462  0.7826  605 CYS B CB  
4107  S SG  . CYS B 94  ? 2.4056 1.7988 2.0585 -0.5406 0.4610  0.7865  605 CYS B SG  
4108  N N   . THR B 95  ? 2.5901 1.9186 2.2426 -0.4748 0.4020  0.7713  606 THR B N   
4109  C CA  . THR B 95  ? 2.5744 1.8842 2.2267 -0.4671 0.3841  0.7646  606 THR B CA  
4110  C C   . THR B 95  ? 2.6124 1.8681 2.1920 -0.4881 0.3656  0.7388  606 THR B C   
4111  O O   . THR B 95  ? 2.6441 1.8823 2.1670 -0.5059 0.3488  0.7272  606 THR B O   
4112  C CB  . THR B 95  ? 2.5562 1.8468 2.1989 -0.4320 0.3740  0.7614  606 THR B CB  
4113  O OG1 . THR B 95  ? 2.5867 1.8440 2.1882 -0.4242 0.4016  0.7436  606 THR B OG1 
4114  C CG2 . THR B 95  ? 2.5186 1.8297 2.2040 -0.4245 0.3531  0.7643  606 THR B CG2 
4115  N N   . ASN B 96  ? 2.8968 2.1285 2.4741 -0.4882 0.3619  0.7244  607 ASN B N   
4116  C CA  . ASN B 96  ? 3.0584 2.2348 2.5661 -0.5049 0.3417  0.6930  607 ASN B CA  
4117  C C   . ASN B 96  ? 3.0877 2.2359 2.5600 -0.4907 0.3034  0.6853  607 ASN B C   
4118  O O   . ASN B 96  ? 3.1823 2.2977 2.6406 -0.4885 0.2948  0.6683  607 ASN B O   
4119  C CB  . ASN B 96  ? 3.1742 2.3326 2.6932 -0.5140 0.3652  0.6755  607 ASN B CB  
4120  C CG  . ASN B 96  ? 3.1860 2.3710 2.7335 -0.5304 0.4014  0.6775  607 ASN B CG  
4121  O OD1 . ASN B 96  ? 3.1460 2.3750 2.7266 -0.5312 0.4125  0.6990  607 ASN B OD1 
4122  N ND2 . ASN B 96  ? 3.2957 2.4519 2.8272 -0.5439 0.4201  0.6526  607 ASN B ND2 
4123  N N   . VAL B 97  ? 2.9729 2.1327 2.4291 -0.4812 0.2792  0.6951  608 VAL B N   
4124  C CA  . VAL B 97  ? 3.0111 2.1498 2.4339 -0.4691 0.2391  0.6868  608 VAL B CA  
4125  C C   . VAL B 97  ? 3.0583 2.1810 2.4110 -0.4871 0.1980  0.6753  608 VAL B C   
4126  O O   . VAL B 97  ? 2.9833 2.1323 2.3359 -0.4897 0.1970  0.6877  608 VAL B O   
4127  C CB  . VAL B 97  ? 2.9475 2.1160 2.4177 -0.4371 0.2442  0.7074  608 VAL B CB  
4128  C CG1 . VAL B 97  ? 3.0047 2.1558 2.4372 -0.4274 0.1994  0.6971  608 VAL B CG1 
4129  C CG2 . VAL B 97  ? 2.9363 2.1174 2.4729 -0.4203 0.2797  0.7179  608 VAL B CG2 
4130  N N   . PRO B 98  ? 3.1319 2.2104 2.4230 -0.5008 0.1628  0.6511  609 PRO B N   
4131  C CA  . PRO B 98  ? 3.2084 2.2700 2.4309 -0.5188 0.1198  0.6394  609 PRO B CA  
4132  C C   . PRO B 98  ? 3.2006 2.2865 2.4263 -0.5005 0.0897  0.6499  609 PRO B C   
4133  O O   . PRO B 98  ? 3.2462 2.3354 2.4939 -0.4782 0.0800  0.6519  609 PRO B O   
4134  C CB  . PRO B 98  ? 3.3722 2.3766 2.5347 -0.5332 0.0916  0.6108  609 PRO B CB  
4135  C CG  . PRO B 98  ? 3.4174 2.4157 2.6218 -0.5134 0.1083  0.6100  609 PRO B CG  
4136  C CD  . PRO B 98  ? 3.2549 2.2940 2.5351 -0.5010 0.1605  0.6320  609 PRO B CD  
4137  N N   . TRP B 99  ? 3.2960 2.3990 2.4997 -0.5109 0.0757  0.6552  610 TRP B N   
4138  C CA  . TRP B 99  ? 3.3300 2.4583 2.5357 -0.4956 0.0476  0.6638  610 TRP B CA  
4139  C C   . TRP B 99  ? 3.5168 2.6128 2.6669 -0.5002 -0.0049 0.6424  610 TRP B C   
4140  O O   . TRP B 99  ? 3.6354 2.7014 2.7236 -0.5252 -0.0321 0.6252  610 TRP B O   
4141  C CB  . TRP B 99  ? 3.2362 2.3891 2.4325 -0.5083 0.0486  0.6734  610 TRP B CB  
4142  C CG  . TRP B 99  ? 3.3076 2.4881 2.5093 -0.4926 0.0228  0.6818  610 TRP B CG  
4143  C CD1 . TRP B 99  ? 3.4517 2.6234 2.6065 -0.5005 -0.0237 0.6694  610 TRP B CD1 
4144  C CD2 . TRP B 99  ? 3.1861 2.4072 2.4430 -0.4676 0.0439  0.7037  610 TRP B CD2 
4145  N NE1 . TRP B 99  ? 3.4400 2.6472 2.6214 -0.4807 -0.0324 0.6821  610 TRP B NE1 
4146  C CE2 . TRP B 99  ? 3.2569 2.4930 2.4982 -0.4605 0.0082  0.7030  610 TRP B CE2 
4147  C CE3 . TRP B 99  ? 2.9603 2.2032 2.2762 -0.4508 0.0893  0.7221  610 TRP B CE3 
4148  C CZ2 . TRP B 99  ? 3.0932 2.3645 2.3739 -0.4372 0.0162  0.7197  610 TRP B CZ2 
4149  C CZ3 . TRP B 99  ? 2.8454 2.1188 2.1958 -0.4282 0.0962  0.7380  610 TRP B CZ3 
4150  C CH2 . TRP B 99  ? 2.9077 2.1950 2.2397 -0.4216 0.0596  0.7366  610 TRP B CH2 
4151  N N   . ASN B 100 ? 2.5069 2.3111 3.6989 0.3989  -0.1578 -0.0713 611 ASN B N   
4152  C CA  . ASN B 100 ? 2.6178 2.4262 3.8399 0.4119  -0.1567 -0.0736 611 ASN B CA  
4153  C C   . ASN B 100 ? 2.6336 2.4096 3.8320 0.4223  -0.1833 -0.0635 611 ASN B C   
4154  O O   . ASN B 100 ? 2.6029 2.3284 3.7510 0.4283  -0.1848 -0.0615 611 ASN B O   
4155  C CB  . ASN B 100 ? 2.7029 2.4869 3.9224 0.4231  -0.1195 -0.0880 611 ASN B CB  
4156  C CG  . ASN B 100 ? 2.8274 2.6347 4.0936 0.4321  -0.1117 -0.0931 611 ASN B CG  
4157  O OD1 . ASN B 100 ? 2.8525 2.6972 4.1560 0.4294  -0.1332 -0.0863 611 ASN B OD1 
4158  N ND2 . ASN B 100 ? 2.9106 2.6966 4.1755 0.4427  -0.0800 -0.1053 611 ASN B ND2 
4159  N N   . SER B 101 ? 2.6265 2.4318 3.8617 0.4244  -0.2043 -0.0572 612 SER B N   
4160  C CA  . SER B 101 ? 2.6470 2.4284 3.8655 0.4331  -0.2325 -0.0467 612 SER B CA  
4161  C C   . SER B 101 ? 2.7292 2.4547 3.9172 0.4519  -0.2197 -0.0516 612 SER B C   
4162  O O   . SER B 101 ? 2.7330 2.4244 3.8903 0.4591  -0.2400 -0.0435 612 SER B O   
4163  C CB  . SER B 101 ? 2.7003 2.5279 3.9695 0.4318  -0.2543 -0.0403 612 SER B CB  
4164  O OG  . SER B 101 ? 2.7330 2.5366 3.9876 0.4413  -0.2800 -0.0308 612 SER B OG  
4165  N N   . SER B 102 ? 2.6406 2.3563 3.8364 0.4599  -0.1868 -0.0647 613 SER B N   
4166  C CA  . SER B 102 ? 2.7300 2.3937 3.8985 0.4780  -0.1727 -0.0702 613 SER B CA  
4167  C C   . SER B 102 ? 2.6665 2.2736 3.7724 0.4812  -0.1696 -0.0694 613 SER B C   
4168  O O   . SER B 102 ? 2.7248 2.2844 3.8008 0.4959  -0.1665 -0.0706 613 SER B O   
4169  C CB  . SER B 102 ? 2.8219 2.4908 4.0142 0.4847  -0.1369 -0.0847 613 SER B CB  
4170  O OG  . SER B 102 ? 2.8733 2.5500 4.0601 0.4749  -0.1131 -0.0925 613 SER B OG  
4171  N N   . TRP B 103 ? 2.8116 2.4231 3.8974 0.4677  -0.1704 -0.0674 614 TRP B N   
4172  C CA  . TRP B 103 ? 2.7455 2.3064 3.7722 0.4688  -0.1672 -0.0666 614 TRP B CA  
4173  C C   . TRP B 103 ? 2.6916 2.2339 3.6894 0.4681  -0.2026 -0.0524 614 TRP B C   
4174  O O   . TRP B 103 ? 2.5903 2.1333 3.5652 0.4566  -0.2161 -0.0458 614 TRP B O   
4175  C CB  . TRP B 103 ? 2.6536 2.2303 3.6740 0.4542  -0.1521 -0.0709 614 TRP B CB  
4176  C CG  . TRP B 103 ? 2.7029 2.3012 3.7528 0.4534  -0.1184 -0.0843 614 TRP B CG  
4177  C CD1 . TRP B 103 ? 2.8173 2.4063 3.8836 0.4663  -0.0951 -0.0943 614 TRP B CD1 
4178  C CD2 . TRP B 103 ? 2.6444 2.2796 3.7133 0.4385  -0.1049 -0.0890 614 TRP B CD2 
4179  N NE1 . TRP B 103 ? 2.8339 2.4510 3.9274 0.4604  -0.0676 -0.1049 614 TRP B NE1 
4180  C CE2 . TRP B 103 ? 2.7279 2.3736 3.8235 0.4433  -0.0730 -0.1019 614 TRP B CE2 
4181  C CE3 . TRP B 103 ? 2.5359 2.1959 3.6012 0.4216  -0.1165 -0.0835 614 TRP B CE3 
4182  C CZ2 . TRP B 103 ? 2.7044 2.3842 3.8231 0.4318  -0.0527 -0.1095 614 TRP B CZ2 
4183  C CZ3 . TRP B 103 ? 2.5140 2.2077 3.6021 0.4103  -0.0964 -0.0910 614 TRP B CZ3 
4184  C CH2 . TRP B 103 ? 2.5967 2.3000 3.7112 0.4154  -0.0649 -0.1039 614 TRP B CH2 
4185  N N   . SER B 104 ? 2.8695 2.3946 3.8684 0.4808  -0.2176 -0.0479 615 SER B N   
4186  C CA  . SER B 104 ? 2.8357 2.3429 3.8103 0.4818  -0.2519 -0.0344 615 SER B CA  
4187  C C   . SER B 104 ? 2.7560 2.3117 3.7552 0.4655  -0.2801 -0.0235 615 SER B C   
4188  O O   . SER B 104 ? 2.6556 2.2117 3.6315 0.4538  -0.2881 -0.0187 615 SER B O   
4189  C CB  . SER B 104 ? 2.7828 2.2332 3.6944 0.4849  -0.2503 -0.0330 615 SER B CB  
4190  O OG  . SER B 104 ? 2.7549 2.1876 3.6425 0.4858  -0.2835 -0.0199 615 SER B OG  
4191  N N   . ASN B 105 ? 2.7190 2.3158 3.7651 0.4650  -0.2955 -0.0193 616 ASN B N   
4192  C CA  . ASN B 105 ? 2.6396 2.2869 3.7152 0.4501  -0.3218 -0.0093 616 ASN B CA  
4193  C C   . ASN B 105 ? 2.5593 2.1865 3.6011 0.4474  -0.3553 0.0047  616 ASN B C   
4194  O O   . ASN B 105 ? 2.6227 2.2414 3.6663 0.4552  -0.3779 0.0125  616 ASN B O   
4195  C CB  . ASN B 105 ? 2.7237 2.4150 3.8561 0.4523  -0.3288 -0.0089 616 ASN B CB  
4196  C CG  . ASN B 105 ? 2.8776 2.5401 4.0071 0.4694  -0.3362 -0.0074 616 ASN B CG  
4197  O OD1 . ASN B 105 ? 3.0267 2.6691 4.1586 0.4819  -0.3120 -0.0175 616 ASN B OD1 
4198  N ND2 . ASN B 105 ? 2.8637 2.5248 3.9888 0.4702  -0.3696 0.0053  616 ASN B ND2 
4199  N N   . ARG B 106 ? 2.6029 2.2222 3.6134 0.4364  -0.3582 0.0078  617 ARG B N   
4200  C CA  . ARG B 106 ? 2.5409 2.1445 3.5185 0.4314  -0.3887 0.0209  617 ARG B CA  
4201  C C   . ARG B 106 ? 2.4566 2.1104 3.4562 0.4125  -0.4050 0.0277  617 ARG B C   
4202  O O   . ARG B 106 ? 2.4374 2.1299 3.4682 0.4033  -0.3887 0.0211  617 ARG B O   
4203  C CB  . ARG B 106 ? 2.5029 2.0481 3.4191 0.4357  -0.3791 0.0191  617 ARG B CB  
4204  C CG  . ARG B 106 ? 2.5078 2.0140 3.3862 0.4425  -0.4066 0.0303  617 ARG B CG  
4205  C CD  . ARG B 106 ? 2.6175 2.1058 3.5061 0.4590  -0.4106 0.0301  617 ARG B CD  
4206  N NE  . ARG B 106 ? 2.6737 2.1115 3.5327 0.4739  -0.3841 0.0198  617 ARG B NE  
4207  C CZ  . ARG B 106 ? 2.6893 2.0715 3.4998 0.4840  -0.3892 0.0226  617 ARG B CZ  
4208  N NH1 . ARG B 106 ? 2.6543 2.0244 3.4404 0.4808  -0.4201 0.0353  617 ARG B NH1 
4209  N NH2 . ARG B 106 ? 2.7451 2.0842 3.5316 0.4973  -0.3636 0.0126  617 ARG B NH2 
4210  N N   . ASN B 107 ? 2.7632 2.4164 3.7463 0.4066  -0.4374 0.0412  618 ASN B N   
4211  C CA  . ASN B 107 ? 2.7191 2.4185 3.7208 0.3889  -0.4555 0.0488  618 ASN B CA  
4212  C C   . ASN B 107 ? 2.6056 2.2899 3.5683 0.3782  -0.4511 0.0493  618 ASN B C   
4213  O O   . ASN B 107 ? 2.5876 2.2212 3.5025 0.3845  -0.4401 0.0464  618 ASN B O   
4214  C CB  . ASN B 107 ? 2.7265 2.4357 3.7328 0.3877  -0.4946 0.0638  618 ASN B CB  
4215  C CG  . ASN B 107 ? 2.7434 2.5125 3.7881 0.3718  -0.5145 0.0713  618 ASN B CG  
4216  O OD1 . ASN B 107 ? 2.7068 2.4988 3.7527 0.3581  -0.5089 0.0701  618 ASN B OD1 
4217  N ND2 . ASN B 107 ? 2.9272 2.7214 4.0026 0.3734  -0.5391 0.0796  618 ASN B ND2 
4218  N N   . LEU B 108 ? 2.6102 2.3408 3.5948 0.3616  -0.4604 0.0534  619 LEU B N   
4219  C CA  . LEU B 108 ? 2.5027 2.2267 3.4557 0.3497  -0.4576 0.0543  619 LEU B CA  
4220  C C   . LEU B 108 ? 2.4257 2.1092 3.3289 0.3511  -0.4810 0.0650  619 LEU B C   
4221  O O   . LEU B 108 ? 2.3862 2.0316 3.2438 0.3509  -0.4706 0.0627  619 LEU B O   
4222  C CB  . LEU B 108 ? 2.4136 2.1980 3.4031 0.3320  -0.4670 0.0578  619 LEU B CB  
4223  C CG  . LEU B 108 ? 2.2356 2.0228 3.1976 0.3174  -0.4750 0.0630  619 LEU B CG  
4224  C CD1 . LEU B 108 ? 2.1401 1.8943 3.0666 0.3176  -0.4448 0.0525  619 LEU B CD1 
4225  C CD2 . LEU B 108 ? 2.2686 2.1191 3.2731 0.3011  -0.4852 0.0664  619 LEU B CD2 
4226  N N   . SER B 109 ? 2.2238 1.9149 3.1352 0.3527  -0.5129 0.0770  620 SER B N   
4227  C CA  . SER B 109 ? 2.2370 1.8939 3.1054 0.3537  -0.5387 0.0885  620 SER B CA  
4228  C C   . SER B 109 ? 2.2819 1.8803 3.1158 0.3715  -0.5331 0.0862  620 SER B C   
4229  O O   . SER B 109 ? 2.2999 1.8603 3.0914 0.3744  -0.5500 0.0940  620 SER B O   
4230  C CB  . SER B 109 ? 2.2099 1.9023 3.1038 0.3474  -0.5756 0.1025  620 SER B CB  
4231  O OG  . SER B 109 ? 2.2190 1.8821 3.0721 0.3465  -0.6013 0.1141  620 SER B OG  
4232  N N   . GLU B 110 ? 2.2801 1.8717 3.1323 0.3833  -0.5101 0.0757  621 GLU B N   
4233  C CA  . GLU B 110 ? 2.3437 1.8826 3.1683 0.4010  -0.5019 0.0720  621 GLU B CA  
4234  C C   . GLU B 110 ? 2.3319 1.8290 3.1204 0.4064  -0.4688 0.0602  621 GLU B C   
4235  O O   . GLU B 110 ? 2.3784 1.8262 3.1367 0.4209  -0.4607 0.0569  621 GLU B O   
4236  C CB  . GLU B 110 ? 2.4577 2.0158 3.3265 0.4111  -0.4965 0.0676  621 GLU B CB  
4237  C CG  . GLU B 110 ? 2.5266 2.0831 3.4047 0.4185  -0.5264 0.0781  621 GLU B CG  
4238  C CD  . GLU B 110 ? 2.5923 2.1692 3.5154 0.4281  -0.5181 0.0725  621 GLU B CD  
4239  O OE1 . GLU B 110 ? 2.6420 2.2245 3.5819 0.4314  -0.4873 0.0598  621 GLU B OE1 
4240  O OE2 . GLU B 110 ? 2.6290 2.2173 3.5712 0.4322  -0.5425 0.0808  621 GLU B OE2 
4241  N N   . ILE B 111 ? 2.3623 1.8778 3.1533 0.3952  -0.4498 0.0537  622 ILE B N   
4242  C CA  . ILE B 111 ? 2.3479 1.8274 3.1062 0.3988  -0.4177 0.0422  622 ILE B CA  
4243  C C   . ILE B 111 ? 2.2763 1.7322 2.9875 0.3900  -0.4237 0.0469  622 ILE B C   
4244  O O   . ILE B 111 ? 2.2827 1.6852 2.9458 0.3982  -0.4169 0.0453  622 ILE B O   
4245  C CB  . ILE B 111 ? 2.3464 1.8609 3.1416 0.3939  -0.3876 0.0298  622 ILE B CB  
4246  C CG1 . ILE B 111 ? 2.4299 1.9574 3.2650 0.4053  -0.3765 0.0233  622 ILE B CG1 
4247  C CG2 . ILE B 111 ? 2.3217 1.8034 3.0819 0.3944  -0.3565 0.0192  622 ILE B CG2 
4248  C CD1 . ILE B 111 ? 2.4380 2.0049 3.3140 0.3999  -0.3497 0.0121  622 ILE B CD1 
4249  N N   . TRP B 112 ? 2.7098 1.9810 2.1977 0.9884  -0.1568 0.1512  623 TRP B N   
4250  C CA  . TRP B 112 ? 2.7029 1.9701 2.1991 0.9851  -0.1602 0.1383  623 TRP B CA  
4251  C C   . TRP B 112 ? 2.8696 2.1183 2.3640 0.9900  -0.1435 0.1262  623 TRP B C   
4252  O O   . TRP B 112 ? 2.9010 2.1479 2.4066 0.9872  -0.1451 0.1137  623 TRP B O   
4253  C CB  . TRP B 112 ? 2.6220 1.8830 2.1074 0.9844  -0.1694 0.1385  623 TRP B CB  
4254  C CG  . TRP B 112 ? 2.6053 1.8840 2.0952 0.9791  -0.1861 0.1490  623 TRP B CG  
4255  C CD1 . TRP B 112 ? 2.7008 1.9796 2.1779 0.9822  -0.1889 0.1598  623 TRP B CD1 
4256  C CD2 . TRP B 112 ? 2.5958 1.8929 2.1041 0.9701  -0.2020 0.1486  623 TRP B CD2 
4257  N NE1 . TRP B 112 ? 2.6971 1.9946 2.1866 0.9753  -0.2054 0.1662  623 TRP B NE1 
4258  C CE2 . TRP B 112 ? 2.6625 1.9709 2.1708 0.9677  -0.2132 0.1599  623 TRP B CE2 
4259  C CE3 . TRP B 112 ? 2.5293 1.8344 2.0542 0.9643  -0.2076 0.1397  623 TRP B CE3 
4260  C CZ2 . TRP B 112 ? 2.6504 1.9771 2.1757 0.9593  -0.2286 0.1630  623 TRP B CZ2 
4261  C CZ3 . TRP B 112 ? 2.4873 1.8100 2.0263 0.9564  -0.2229 0.1431  623 TRP B CZ3 
4262  C CH2 . TRP B 112 ? 2.5501 1.8831 2.0898 0.9537  -0.2328 0.1549  623 TRP B CH2 
4263  N N   . ASP B 113 ? 2.7725 2.0076 2.2543 0.9972  -0.1272 0.1292  624 ASP B N   
4264  C CA  . ASP B 113 ? 2.9286 2.1444 2.4097 1.0019  -0.1090 0.1181  624 ASP B CA  
4265  C C   . ASP B 113 ? 2.9631 2.1807 2.4489 1.0049  -0.0963 0.1203  624 ASP B C   
4266  O O   . ASP B 113 ? 3.0387 2.2384 2.5200 1.0102  -0.0779 0.1148  624 ASP B O   
4267  C CB  . ASP B 113 ? 3.0529 2.2433 2.5096 1.0088  -0.0979 0.1187  624 ASP B CB  
4268  C CG  . ASP B 113 ? 3.1638 2.3500 2.6161 1.0062  -0.1088 0.1145  624 ASP B CG  
4269  O OD1 . ASP B 113 ? 3.1470 2.3423 2.6175 0.9999  -0.1182 0.1048  624 ASP B OD1 
4270  O OD2 . ASP B 113 ? 3.1997 2.3737 2.6295 1.0108  -0.1083 0.1208  624 ASP B OD2 
4271  N N   . ASN B 114 ? 2.8910 2.1298 2.3866 1.0014  -0.1054 0.1283  625 ASN B N   
4272  C CA  . ASN B 114 ? 2.9231 2.1651 2.4235 1.0040  -0.0945 0.1307  625 ASN B CA  
4273  C C   . ASN B 114 ? 2.8508 2.1183 2.3683 0.9980  -0.1070 0.1356  625 ASN B C   
4274  O O   . ASN B 114 ? 2.9290 2.2022 2.4472 0.9999  -0.1012 0.1421  625 ASN B O   
4275  C CB  . ASN B 114 ? 2.9397 2.1697 2.4168 1.0113  -0.0834 0.1424  625 ASN B CB  
4276  C CG  . ASN B 114 ? 3.0487 2.2746 2.5275 1.0155  -0.0670 0.1426  625 ASN B CG  
4277  O OD1 . ASN B 114 ? 3.1506 2.3764 2.6465 1.0144  -0.0600 0.1313  625 ASN B OD1 
4278  N ND2 . ASN B 114 ? 3.0728 2.2955 2.5342 1.0207  -0.0608 0.1548  625 ASN B ND2 
4279  N N   . MET B 115 ? 2.8726 2.1549 2.4032 0.9911  -0.1232 0.1330  626 MET B N   
4280  C CA  . MET B 115 ? 2.7757 2.0806 2.3209 0.9855  -0.1341 0.1385  626 MET B CA  
4281  C C   . MET B 115 ? 2.7198 2.0359 2.2807 0.9793  -0.1469 0.1299  626 MET B C   
4282  O O   . MET B 115 ? 2.6866 1.9983 2.2447 0.9771  -0.1542 0.1260  626 MET B O   
4283  C CB  . MET B 115 ? 2.6503 1.9655 2.1890 0.9833  -0.1433 0.1544  626 MET B CB  
4284  C CG  . MET B 115 ? 2.6354 1.9687 2.1846 0.9804  -0.1468 0.1633  626 MET B CG  
4285  S SD  . MET B 115 ? 2.7169 2.0573 2.2569 0.9800  -0.1529 0.1807  626 MET B SD  
4286  C CE  . MET B 115 ? 2.7523 2.1130 2.3081 0.9762  -0.1552 0.1887  626 MET B CE  
4287  N N   . THR B 116 ? 2.6291 1.9589 2.2052 0.9768  -0.1495 0.1269  627 THR B N   
4288  C CA  . THR B 116 ? 2.5462 1.8872 2.1355 0.9716  -0.1615 0.1193  627 THR B CA  
4289  C C   . THR B 116 ? 2.3695 1.7278 1.9629 0.9652  -0.1758 0.1317  627 THR B C   
4290  O O   . THR B 116 ? 2.3986 1.7631 1.9891 0.9647  -0.1757 0.1449  627 THR B O   
4291  C CB  . THR B 116 ? 2.5983 1.9449 2.2012 0.9730  -0.1572 0.1085  627 THR B CB  
4292  O OG1 . THR B 116 ? 2.5749 1.9332 2.1812 0.9729  -0.1558 0.1181  627 THR B OG1 
4293  C CG2 . THR B 116 ? 2.6891 2.0191 2.2920 0.9788  -0.1417 0.0958  627 THR B CG2 
4294  N N   . TRP B 117 ? 2.3725 1.7386 1.9736 0.9602  -0.1878 0.1271  628 TRP B N   
4295  C CA  . TRP B 117 ? 2.3990 1.7807 2.0063 0.9537  -0.2007 0.1381  628 TRP B CA  
4296  C C   . TRP B 117 ? 2.4461 1.8418 2.0628 0.9525  -0.2003 0.1447  628 TRP B C   
4297  O O   . TRP B 117 ? 2.5035 1.9099 2.1238 0.9486  -0.2058 0.1578  628 TRP B O   
4298  C CB  . TRP B 117 ? 2.3475 1.7327 1.9602 0.9492  -0.2122 0.1309  628 TRP B CB  
4299  C CG  . TRP B 117 ? 2.3248 1.7012 1.9292 0.9480  -0.2170 0.1307  628 TRP B CG  
4300  C CD1 . TRP B 117 ? 2.3334 1.6952 1.9310 0.9509  -0.2137 0.1189  628 TRP B CD1 
4301  C CD2 . TRP B 117 ? 2.3666 1.7482 1.9695 0.9437  -0.2260 0.1425  628 TRP B CD2 
4302  N NE1 . TRP B 117 ? 2.3384 1.6956 1.9285 0.9488  -0.2201 0.1228  628 TRP B NE1 
4303  C CE2 . TRP B 117 ? 2.3654 1.7349 1.9589 0.9445  -0.2280 0.1370  628 TRP B CE2 
4304  C CE3 . TRP B 117 ? 2.3838 1.7791 1.9937 0.9394  -0.2325 0.1566  628 TRP B CE3 
4305  C CZ2 . TRP B 117 ? 2.3735 1.7447 1.9637 0.9414  -0.2366 0.1450  628 TRP B CZ2 
4306  C CZ3 . TRP B 117 ? 2.4128 1.8100 2.0212 0.9361  -0.2409 0.1642  628 TRP B CZ3 
4307  C CH2 . TRP B 117 ? 2.4202 1.8057 2.0185 0.9373  -0.2432 0.1583  628 TRP B CH2 
4308  N N   . LEU B 118 ? 2.3867 1.7824 2.0080 0.9559  -0.1938 0.1352  629 LEU B N   
4309  C CA  . LEU B 118 ? 2.4176 1.8253 2.0463 0.9558  -0.1924 0.1403  629 LEU B CA  
4310  C C   . LEU B 118 ? 2.4994 1.9062 2.1231 0.9580  -0.1840 0.1518  629 LEU B C   
4311  O O   . LEU B 118 ? 2.5445 1.9630 2.1731 0.9552  -0.1870 0.1633  629 LEU B O   
4312  C CB  . LEU B 118 ? 2.3967 1.8031 2.0306 0.9600  -0.1869 0.1257  629 LEU B CB  
4313  C CG  . LEU B 118 ? 2.3199 1.7304 1.9596 0.9583  -0.1960 0.1142  629 LEU B CG  
4314  C CD1 . LEU B 118 ? 2.3574 1.7659 2.0024 0.9637  -0.1895 0.0986  629 LEU B CD1 
4315  C CD2 . LEU B 118 ? 2.3130 1.7382 1.9580 0.9531  -0.2067 0.1234  629 LEU B CD2 
4316  N N   . GLN B 119 ? 2.4078 1.8002 2.0215 0.9634  -0.1731 0.1488  630 GLN B N   
4317  C CA  . GLN B 119 ? 2.4902 1.8800 2.0966 0.9666  -0.1642 0.1589  630 GLN B CA  
4318  C C   . GLN B 119 ? 2.5279 1.9216 2.1294 0.9632  -0.1716 0.1728  630 GLN B C   
4319  O O   . GLN B 119 ? 2.6020 2.0018 2.2027 0.9633  -0.1699 0.1841  630 GLN B O   
4320  C CB  . GLN B 119 ? 2.5575 1.9288 2.1536 0.9737  -0.1497 0.1513  630 GLN B CB  
4321  C CG  . GLN B 119 ? 2.7003 2.0665 2.2870 0.9784  -0.1380 0.1598  630 GLN B CG  
4322  C CD  . GLN B 119 ? 2.8944 2.2403 2.4710 0.9855  -0.1226 0.1516  630 GLN B CD  
4323  O OE1 . GLN B 119 ? 2.9023 2.2420 2.4862 0.9872  -0.1174 0.1376  630 GLN B OE1 
4324  N NE2 . GLN B 119 ? 2.9783 2.3134 2.5386 0.9898  -0.1147 0.1598  630 GLN B NE2 
4325  N N   . TRP B 120 ? 2.5129 1.9035 2.1119 0.9605  -0.1799 0.1713  631 TRP B N   
4326  C CA  . TRP B 120 ? 2.5456 1.9401 2.1414 0.9575  -0.1878 0.1829  631 TRP B CA  
4327  C C   . TRP B 120 ? 2.5579 1.9712 2.1689 0.9505  -0.1988 0.1922  631 TRP B C   
4328  O O   . TRP B 120 ? 2.6396 2.0601 2.2523 0.9492  -0.2012 0.2042  631 TRP B O   
4329  C CB  . TRP B 120 ? 2.4948 1.8799 2.0838 0.9570  -0.1932 0.1773  631 TRP B CB  
4330  C CG  . TRP B 120 ? 2.5151 1.9055 2.1035 0.9533  -0.2038 0.1870  631 TRP B CG  
4331  C CD1 . TRP B 120 ? 2.4831 1.8849 2.0833 0.9464  -0.2172 0.1896  631 TRP B CD1 
4332  C CD2 . TRP B 120 ? 2.5853 1.9700 2.1611 0.9570  -0.2019 0.1951  631 TRP B CD2 
4333  N NE1 . TRP B 120 ? 2.5250 1.9290 2.1224 0.9452  -0.2240 0.1984  631 TRP B NE1 
4334  C CE2 . TRP B 120 ? 2.5886 1.9825 2.1707 0.9519  -0.2152 0.2017  631 TRP B CE2 
4335  C CE3 . TRP B 120 ? 2.6530 2.0253 2.2123 0.9647  -0.1899 0.1972  631 TRP B CE3 
4336  C CZ2 . TRP B 120 ? 2.6535 2.0453 2.2264 0.9545  -0.2178 0.2095  631 TRP B CZ2 
4337  C CZ3 . TRP B 120 ? 2.7514 2.1208 2.2995 0.9675  -0.1921 0.2054  631 TRP B CZ3 
4338  C CH2 . TRP B 120 ? 2.7301 2.1097 2.2853 0.9626  -0.2064 0.2111  631 TRP B CH2 
4339  N N   . ASP B 121 ? 2.4863 1.9072 2.1084 0.9465  -0.2052 0.1866  632 ASP B N   
4340  C CA  . ASP B 121 ? 2.4980 1.9350 2.1342 0.9402  -0.2145 0.1955  632 ASP B CA  
4341  C C   . ASP B 121 ? 2.5704 2.0157 2.2115 0.9410  -0.2093 0.2035  632 ASP B C   
4342  O O   . ASP B 121 ? 2.6107 2.0681 2.2623 0.9364  -0.2156 0.2140  632 ASP B O   
4343  C CB  . ASP B 121 ? 2.4322 1.8737 2.0763 0.9371  -0.2210 0.1872  632 ASP B CB  
4344  C CG  . ASP B 121 ? 2.4358 1.8917 2.0934 0.9308  -0.2303 0.1966  632 ASP B CG  
4345  O OD1 . ASP B 121 ? 2.4231 1.8822 2.0852 0.9262  -0.2395 0.2010  632 ASP B OD1 
4346  O OD2 . ASP B 121 ? 2.4860 1.9492 2.1484 0.9316  -0.2280 0.1996  632 ASP B OD2 
4347  N N   . LYS B 122 ? 2.5322 1.9709 2.1665 0.9468  -0.1976 0.1987  633 LYS B N   
4348  C CA  . LYS B 122 ? 2.6679 2.1142 2.3062 0.9478  -0.1923 0.2059  633 LYS B CA  
4349  C C   . LYS B 122 ? 2.8058 2.2537 2.4405 0.9481  -0.1914 0.2185  633 LYS B C   
4350  O O   . LYS B 122 ? 2.9303 2.3882 2.5711 0.9468  -0.1922 0.2280  633 LYS B O   
4351  C CB  . LYS B 122 ? 2.6512 2.0901 2.2841 0.9541  -0.1800 0.1966  633 LYS B CB  
4352  C CG  . LYS B 122 ? 2.6782 2.1239 2.3199 0.9538  -0.1810 0.1891  633 LYS B CG  
4353  C CD  . LYS B 122 ? 2.7661 2.2091 2.4057 0.9595  -0.1692 0.1847  633 LYS B CD  
4354  C CE  . LYS B 122 ? 2.9213 2.3721 2.5623 0.9591  -0.1659 0.1977  633 LYS B CE  
4355  N NZ  . LYS B 122 ? 2.9529 2.4178 2.6035 0.9545  -0.1747 0.2053  633 LYS B NZ  
4356  N N   . GLU B 123 ? 2.7125 2.1496 2.3351 0.9510  -0.1897 0.2183  634 GLU B N   
4357  C CA  . GLU B 123 ? 2.8392 2.2762 2.4555 0.9528  -0.1888 0.2288  634 GLU B CA  
4358  C C   . GLU B 123 ? 2.8027 2.2499 2.4288 0.9470  -0.2022 0.2373  634 GLU B C   
4359  O O   . GLU B 123 ? 2.8913 2.3471 2.5213 0.9468  -0.2051 0.2478  634 GLU B O   
4360  C CB  . GLU B 123 ? 2.9070 2.3264 2.5037 0.9598  -0.1804 0.2244  634 GLU B CB  
4361  C CG  . GLU B 123 ? 2.8429 2.2509 2.4299 0.9665  -0.1654 0.2175  634 GLU B CG  
4362  C CD  . GLU B 123 ? 2.8958 2.2851 2.4625 0.9738  -0.1561 0.2148  634 GLU B CD  
4363  O OE1 . GLU B 123 ? 2.9454 2.3308 2.5046 0.9738  -0.1622 0.2178  634 GLU B OE1 
4364  O OE2 . GLU B 123 ? 2.8957 2.2734 2.4538 0.9798  -0.1424 0.2093  634 GLU B OE2 
4365  N N   . ILE B 124 ? 2.8157 2.2613 2.4441 0.9437  -0.2104 0.2324  635 ILE B N   
4366  C CA  . ILE B 124 ? 2.8427 2.2970 2.4804 0.9387  -0.2230 0.2397  635 ILE B CA  
4367  C C   . ILE B 124 ? 2.8379 2.3055 2.4902 0.9347  -0.2305 0.2441  635 ILE B C   
4368  O O   . ILE B 124 ? 2.8856 2.3608 2.5467 0.9315  -0.2407 0.2506  635 ILE B O   
4369  C CB  . ILE B 124 ? 2.7533 2.1993 2.3850 0.9381  -0.2285 0.2326  635 ILE B CB  
4370  C CG1 . ILE B 124 ? 2.6438 2.0718 2.2550 0.9455  -0.2181 0.2242  635 ILE B CG1 
4371  C CG2 . ILE B 124 ? 2.7886 2.2399 2.4244 0.9356  -0.2392 0.2402  635 ILE B CG2 
4372  C CD1 . ILE B 124 ? 2.7403 2.1618 2.3373 0.9516  -0.2126 0.2304  635 ILE B CD1 
4373  N N   . SER B 125 ? 2.9130 2.3831 2.5683 0.9352  -0.2254 0.2407  636 SER B N   
4374  C CA  . SER B 125 ? 2.9933 2.4743 2.6602 0.9324  -0.2312 0.2447  636 SER B CA  
4375  C C   . SER B 125 ? 3.1643 2.6551 2.8389 0.9320  -0.2354 0.2580  636 SER B C   
4376  O O   . SER B 125 ? 3.2133 2.7125 2.8997 0.9287  -0.2431 0.2634  636 SER B O   
4377  C CB  . SER B 125 ? 2.9776 2.4588 2.6435 0.9347  -0.2237 0.2392  636 SER B CB  
4378  O OG  . SER B 125 ? 3.0776 2.5579 2.7380 0.9390  -0.2142 0.2426  636 SER B OG  
4379  N N   . ASN B 126 ? 3.0575 2.5468 2.7258 0.9357  -0.2301 0.2632  637 ASN B N   
4380  C CA  . ASN B 126 ? 3.1636 2.6621 2.8393 0.9360  -0.2339 0.2751  637 ASN B CA  
4381  C C   . ASN B 126 ? 3.1311 2.6335 2.8144 0.9333  -0.2452 0.2800  637 ASN B C   
4382  O O   . ASN B 126 ? 3.1628 2.6753 2.8595 0.9317  -0.2517 0.2890  637 ASN B O   
4383  C CB  . ASN B 126 ? 3.2836 2.7781 2.9481 0.9414  -0.2250 0.2780  637 ASN B CB  
4384  C CG  . ASN B 126 ? 3.3249 2.8202 2.9869 0.9440  -0.2152 0.2775  637 ASN B CG  
4385  O OD1 . ASN B 126 ? 3.3216 2.8184 2.9875 0.9425  -0.2139 0.2728  637 ASN B OD1 
4386  N ND2 . ASN B 126 ? 3.5459 3.0399 3.2004 0.9485  -0.2081 0.2821  637 ASN B ND2 
4387  N N   . TYR B 127 ? 2.3739 3.3068 2.6260 0.8350  0.8406  1.1932  638 TYR B N   
4388  C CA  . TYR B 127 ? 2.3737 3.3079 2.6514 0.8238  0.8451  1.1950  638 TYR B CA  
4389  C C   . TYR B 127 ? 2.2926 3.2153 2.5825 0.8185  0.8483  1.2033  638 TYR B C   
4390  O O   . TYR B 127 ? 2.2881 3.2101 2.5999 0.8095  0.8509  1.2049  638 TYR B O   
4391  C CB  . TYR B 127 ? 2.3552 3.2932 2.6406 0.8250  0.8339  1.1847  638 TYR B CB  
4392  C CG  . TYR B 127 ? 2.4326 3.3796 2.7023 0.8327  0.8286  1.1756  638 TYR B CG  
4393  C CD1 . TYR B 127 ? 2.5570 3.5172 2.8298 0.8292  0.8366  1.1739  638 TYR B CD1 
4394  C CD2 . TYR B 127 ? 2.4389 3.3816 2.6909 0.8432  0.8163  1.1682  638 TYR B CD2 
4395  C CE1 . TYR B 127 ? 2.7050 3.6734 2.9626 0.8370  0.8319  1.1656  638 TYR B CE1 
4396  C CE2 . TYR B 127 ? 2.5785 3.5281 2.8153 0.8505  0.8119  1.1599  638 TYR B CE2 
4397  C CZ  . TYR B 127 ? 2.7062 3.6685 2.9454 0.8478  0.8194  1.1589  638 TYR B CZ  
4398  O OH  . TYR B 127 ? 2.8541 3.8235 3.0776 0.8556  0.8152  1.1508  638 TYR B OH  
4399  N N   . THR B 128 ? 2.4081 3.3219 2.6837 0.8243  0.8482  1.2086  639 THR B N   
4400  C CA  . THR B 128 ? 2.3348 3.2372 2.6193 0.8206  0.8513  1.2167  639 THR B CA  
4401  C C   . THR B 128 ? 2.3914 3.2917 2.6907 0.8088  0.8673  1.2262  639 THR B C   
4402  O O   . THR B 128 ? 2.3614 3.2563 2.6803 0.8010  0.8695  1.2298  639 THR B O   
4403  C CB  . THR B 128 ? 2.2876 3.1824 2.5506 0.8303  0.8498  1.2207  639 THR B CB  
4404  O OG1 . THR B 128 ? 2.3689 3.2680 2.6118 0.8355  0.8557  1.2219  639 THR B OG1 
4405  C CG2 . THR B 128 ? 2.1993 3.0931 2.4556 0.8392  0.8344  1.2123  639 THR B CG2 
4406  N N   . GLN B 129 ? 2.0741 2.9784 2.3644 0.8070  0.8793  1.2300  640 GLN B N   
4407  C CA  . GLN B 129 ? 2.0988 3.0006 2.4019 0.7949  0.8967  1.2388  640 GLN B CA  
4408  C C   . GLN B 129 ? 2.0841 2.9955 2.4143 0.7834  0.8998  1.2347  640 GLN B C   
4409  O O   . GLN B 129 ? 2.0953 3.0026 2.4440 0.7720  0.9114  1.2410  640 GLN B O   
4410  C CB  . GLN B 129 ? 2.1297 3.0346 2.4153 0.7963  0.9087  1.2425  640 GLN B CB  
4411  C CG  . GLN B 129 ? 2.1618 3.0613 2.4559 0.7845  0.9288  1.2524  640 GLN B CG  
4412  C CD  . GLN B 129 ? 2.1811 3.0613 2.4693 0.7850  0.9335  1.2632  640 GLN B CD  
4413  O OE1 . GLN B 129 ? 2.1758 3.0486 2.4482 0.7962  0.9230  1.2635  640 GLN B OE1 
4414  N NE2 . GLN B 129 ? 2.2046 3.0767 2.5054 0.7729  0.9499  1.2717  640 GLN B NE2 
4415  N N   . ILE B 130 ? 2.1518 3.0758 2.4845 0.7864  0.8902  1.2240  641 ILE B N   
4416  C CA  . ILE B 130 ? 2.1375 3.0721 2.4946 0.7770  0.8924  1.2191  641 ILE B CA  
4417  C C   . ILE B 130 ? 2.1168 3.0438 2.4923 0.7737  0.8855  1.2195  641 ILE B C   
4418  O O   . ILE B 130 ? 2.1178 3.0465 2.5170 0.7624  0.8938  1.2219  641 ILE B O   
4419  C CB  . ILE B 130 ? 2.1311 3.0800 2.4819 0.7831  0.8838  1.2076  641 ILE B CB  
4420  C CG1 . ILE B 130 ? 2.2251 3.1813 2.5562 0.7876  0.8899  1.2072  641 ILE B CG1 
4421  C CG2 . ILE B 130 ? 2.1914 3.1529 2.5665 0.7740  0.8875  1.2022  641 ILE B CG2 
4422  C CD1 . ILE B 130 ? 2.2227 3.1879 2.5384 0.7983  0.8778  1.1967  641 ILE B CD1 
4423  N N   . ILE B 131 ? 2.2945 3.2137 2.6599 0.7832  0.8708  1.2167  642 ILE B N   
4424  C CA  . ILE B 131 ? 2.2094 3.1215 2.5905 0.7812  0.8632  1.2164  642 ILE B CA  
4425  C C   . ILE B 131 ? 2.1864 3.0876 2.5795 0.7732  0.8737  1.2275  642 ILE B C   
4426  O O   . ILE B 131 ? 2.1762 3.0754 2.5916 0.7654  0.8754  1.2291  642 ILE B O   
4427  C CB  . ILE B 131 ? 2.1109 3.0169 2.4765 0.7931  0.8472  1.2111  642 ILE B CB  
4428  C CG1 . ILE B 131 ? 2.1340 3.0487 2.4874 0.8007  0.8372  1.2000  642 ILE B CG1 
4429  C CG2 . ILE B 131 ? 2.0270 2.9250 2.4077 0.7914  0.8401  1.2114  642 ILE B CG2 
4430  C CD1 . ILE B 131 ? 2.0469 2.9555 2.3857 0.8111  0.8229  1.1938  642 ILE B CD1 
4431  N N   . TYR B 132 ? 2.2788 3.1721 2.6562 0.7755  0.8814  1.2354  643 TYR B N   
4432  C CA  . TYR B 132 ? 2.2653 3.1458 2.6502 0.7689  0.8923  1.2465  643 TYR B CA  
4433  C C   . TYR B 132 ? 2.3478 3.2318 2.7568 0.7540  0.9072  1.2500  643 TYR B C   
4434  O O   . TYR B 132 ? 2.3318 3.2074 2.7581 0.7464  0.9121  1.2557  643 TYR B O   
4435  C CB  . TYR B 132 ? 2.2774 3.1492 2.6376 0.7744  0.8998  1.2541  643 TYR B CB  
4436  C CG  . TYR B 132 ? 2.1934 3.0604 2.5319 0.7884  0.8870  1.2519  643 TYR B CG  
4437  C CD1 . TYR B 132 ? 2.1052 2.9734 2.4486 0.7938  0.8712  1.2446  643 TYR B CD1 
4438  C CD2 . TYR B 132 ? 2.2129 3.0751 2.5255 0.7964  0.8912  1.2564  643 TYR B CD2 
4439  C CE1 . TYR B 132 ? 2.0604 2.9258 2.3853 0.8057  0.8606  1.2416  643 TYR B CE1 
4440  C CE2 . TYR B 132 ? 2.1438 3.0034 2.4372 0.8093  0.8800  1.2536  643 TYR B CE2 
4441  C CZ  . TYR B 132 ? 2.0856 2.9474 2.3860 0.8134  0.8650  1.2460  643 TYR B CZ  
4442  O OH  . TYR B 132 ? 2.0796 2.9402 2.3625 0.8253  0.8550  1.2425  643 TYR B OH  
4443  N N   . GLY B 133 ? 2.2245 3.1221 2.6360 0.7494  0.9146  1.2458  644 GLY B N   
4444  C CA  . GLY B 133 ? 2.3150 3.2189 2.7509 0.7345  0.9300  1.2475  644 GLY B CA  
4445  C C   . GLY B 133 ? 2.3029 3.2139 2.7660 0.7286  0.9245  1.2416  644 GLY B C   
4446  O O   . GLY B 133 ? 2.3445 3.2555 2.8316 0.7160  0.9362  1.2450  644 GLY B O   
4447  N N   . LEU B 134 ? 2.1576 3.0743 2.6170 0.7375  0.9073  1.2327  645 LEU B N   
4448  C CA  . LEU B 134 ? 2.1464 3.0692 2.6281 0.7339  0.9009  1.2266  645 LEU B CA  
4449  C C   . LEU B 134 ? 2.0559 2.9645 2.5478 0.7334  0.8955  1.2319  645 LEU B C   
4450  O O   . LEU B 134 ? 2.0474 2.9592 2.5600 0.7292  0.8920  1.2286  645 LEU B O   
4451  C CB  . LEU B 134 ? 2.1403 3.0729 2.6117 0.7439  0.8858  1.2151  645 LEU B CB  
4452  C CG  . LEU B 134 ? 2.2545 3.2065 2.7303 0.7406  0.8920  1.2072  645 LEU B CG  
4453  C CD1 . LEU B 134 ? 2.3219 3.2840 2.8300 0.7269  0.9035  1.2060  645 LEU B CD1 
4454  C CD2 . LEU B 134 ? 2.3259 3.2821 2.7854 0.7411  0.9020  1.2097  645 LEU B CD2 
4455  N N   . LEU B 135 ? 1.8581 2.7519 2.3358 0.7378  0.8952  1.2398  646 LEU B N   
4456  C CA  . LEU B 135 ? 1.8507 2.7310 2.3347 0.7389  0.8900  1.2449  646 LEU B CA  
4457  C C   . LEU B 135 ? 1.8757 2.7462 2.3746 0.7275  0.9059  1.2556  646 LEU B C   
4458  O O   . LEU B 135 ? 1.8664 2.7320 2.3852 0.7223  0.9054  1.2579  646 LEU B O   
4459  C CB  . LEU B 135 ? 1.8502 2.7212 2.3088 0.7515  0.8800  1.2460  646 LEU B CB  
4460  C CG  . LEU B 135 ? 1.8280 2.7056 2.2693 0.7634  0.8645  1.2358  646 LEU B CG  
4461  C CD1 . LEU B 135 ? 1.8316 2.7005 2.2512 0.7740  0.8577  1.2376  646 LEU B CD1 
4462  C CD2 . LEU B 135 ? 1.7959 2.6778 2.2510 0.7642  0.8525  1.2275  646 LEU B CD2 
4463  N N   . GLU B 136 ? 2.3032 3.1699 2.7926 0.7232  0.9208  1.2623  647 GLU B N   
4464  C CA  . GLU B 136 ? 2.3428 3.1969 2.8431 0.7124  0.9374  1.2731  647 GLU B CA  
4465  C C   . GLU B 136 ? 2.4469 3.3106 2.9771 0.6969  0.9508  1.2716  647 GLU B C   
4466  O O   . GLU B 136 ? 2.4817 3.3370 3.0317 0.6874  0.9590  1.2773  647 GLU B O   
4467  C CB  . GLU B 136 ? 2.3899 3.2348 2.8677 0.7130  0.9505  1.2811  647 GLU B CB  
4468  C CG  . GLU B 136 ? 2.3564 3.2008 2.8025 0.7274  0.9413  1.2794  647 GLU B CG  
4469  C CD  . GLU B 136 ? 2.4232 3.2589 2.8493 0.7265  0.9569  1.2876  647 GLU B CD  
4470  O OE1 . GLU B 136 ? 2.5250 3.3647 2.9615 0.7149  0.9733  1.2895  647 GLU B OE1 
4471  O OE2 . GLU B 136 ? 2.3807 3.2062 2.7805 0.7375  0.9533  1.2918  647 GLU B OE2 
4472  N N   . GLU B 137 ? 2.3715 3.2534 2.9060 0.6941  0.9534  1.2633  648 GLU B N   
4473  C CA  . GLU B 137 ? 2.4843 3.3790 3.0475 0.6790  0.9680  1.2601  648 GLU B CA  
4474  C C   . GLU B 137 ? 2.4822 3.3899 3.0702 0.6770  0.9586  1.2510  648 GLU B C   
4475  O O   . GLU B 137 ? 2.5122 3.4193 3.1276 0.6663  0.9659  1.2526  648 GLU B O   
4476  C CB  . GLU B 137 ? 2.5863 3.4955 3.1414 0.6768  0.9776  1.2555  648 GLU B CB  
4477  C CG  . GLU B 137 ? 2.7114 3.6415 3.2958 0.6633  0.9900  1.2474  648 GLU B CG  
4478  C CD  . GLU B 137 ? 2.7901 3.7393 3.3638 0.6669  0.9905  1.2385  648 GLU B CD  
4479  O OE1 . GLU B 137 ? 2.8450 3.8158 3.4370 0.6638  0.9889  1.2268  648 GLU B OE1 
4480  O OE2 . GLU B 137 ? 2.8018 3.7450 3.3485 0.6732  0.9926  1.2428  648 GLU B OE2 
4481  N N   . SER B 138 ? 2.3121 3.2309 2.8903 0.6876  0.9427  1.2413  649 SER B N   
4482  C CA  . SER B 138 ? 2.3251 3.2565 2.9246 0.6861  0.9350  1.2321  649 SER B CA  
4483  C C   . SER B 138 ? 2.2396 3.1582 2.8497 0.6875  0.9262  1.2360  649 SER B C   
4484  O O   . SER B 138 ? 2.2638 3.1903 2.8985 0.6823  0.9252  1.2311  649 SER B O   
4485  C CB  . SER B 138 ? 2.3171 3.2602 2.8996 0.6980  0.9204  1.2214  649 SER B CB  
4486  O OG  . SER B 138 ? 2.2009 3.1311 2.7612 0.7115  0.9034  1.2225  649 SER B OG  
4487  N N   . GLN B 139 ? 2.1113 3.0115 2.7041 0.6948  0.9199  1.2440  650 GLN B N   
4488  C CA  . GLN B 139 ? 2.0326 2.9218 2.6334 0.6979  0.9099  1.2467  650 GLN B CA  
4489  C C   . GLN B 139 ? 2.0468 2.9231 2.6653 0.6877  0.9220  1.2571  650 GLN B C   
4490  O O   . GLN B 139 ? 2.1053 2.9872 2.7523 0.6765  0.9303  1.2562  650 GLN B O   
4491  C CB  . GLN B 139 ? 2.0086 2.8876 2.5823 0.7125  0.8944  1.2470  650 GLN B CB  
4492  C CG  . GLN B 139 ? 1.9862 2.8747 2.5430 0.7237  0.8797  1.2363  650 GLN B CG  
4493  C CD  . GLN B 139 ? 1.9587 2.8557 2.5302 0.7243  0.8706  1.2276  650 GLN B CD  
4494  O OE1 . GLN B 139 ? 1.9653 2.8702 2.5615 0.7147  0.8781  1.2263  650 GLN B OE1 
4495  N NE2 . GLN B 139 ? 1.9369 2.8322 2.4929 0.7357  0.8548  1.2211  650 GLN B NE2 
4496  N N   . ASN B 140 ? 2.3004 2.0331 2.8537 -0.4348 0.3305  0.9783  651 ASN B N   
4497  C CA  . ASN B 140 ? 2.3106 2.0299 2.8463 -0.4419 0.2695  0.9757  651 ASN B CA  
4498  C C   . ASN B 140 ? 2.3728 2.1097 2.8785 -0.4499 0.2165  1.0477  651 ASN B C   
4499  O O   . ASN B 140 ? 2.3940 2.1141 2.8809 -0.4577 0.1662  1.0522  651 ASN B O   
4500  C CB  . ASN B 140 ? 2.2944 2.0413 2.8627 -0.4283 0.2579  0.9155  651 ASN B CB  
4501  C CG  . ASN B 140 ? 2.2969 2.0176 2.8925 -0.4240 0.2976  0.8369  651 ASN B CG  
4502  O OD1 . ASN B 140 ? 2.3033 1.9988 2.9044 -0.4264 0.3494  0.8248  651 ASN B OD1 
4503  N ND2 . ASN B 140 ? 2.2939 2.0190 2.9060 -0.4172 0.2738  0.7827  651 ASN B ND2 
4504  N N   . GLN B 141 ? 2.2962 2.0650 2.7972 -0.4486 0.2266  1.1032  652 GLN B N   
4505  C CA  . GLN B 141 ? 2.3019 2.0831 2.7739 -0.4586 0.1788  1.1726  652 GLN B CA  
4506  C C   . GLN B 141 ? 2.3458 2.0878 2.7833 -0.4742 0.1781  1.2144  652 GLN B C   
4507  O O   . GLN B 141 ? 2.4161 2.1476 2.8257 -0.4874 0.1316  1.2559  652 GLN B O   
4508  C CB  . GLN B 141 ? 2.2819 2.1215 2.7661 -0.4494 0.1828  1.2135  652 GLN B CB  
4509  C CG  . GLN B 141 ? 2.2946 2.1480 2.7512 -0.4602 0.1333  1.2839  652 GLN B CG  
4510  C CD  . GLN B 141 ? 2.3981 2.2419 2.8437 -0.4648 0.0765  1.2767  652 GLN B CD  
4511  O OE1 . GLN B 141 ? 2.4289 2.2825 2.8938 -0.4531 0.0699  1.2282  652 GLN B OE1 
4512  N NE2 . GLN B 141 ? 2.4564 2.2817 2.8672 -0.4770 0.0356  1.3108  652 GLN B NE2 
4513  N N   . GLN B 142 ? 2.4991 2.2178 2.9382 -0.4723 0.2299  1.2009  653 GLN B N   
4514  C CA  . GLN B 142 ? 2.5934 2.2753 2.9921 -0.4780 0.2343  1.2194  653 GLN B CA  
4515  C C   . GLN B 142 ? 2.5595 2.1816 2.9549 -0.4902 0.2393  1.1900  653 GLN B C   
4516  O O   . GLN B 142 ? 2.6341 2.2240 2.9889 -0.4969 0.2163  1.2004  653 GLN B O   
4517  C CB  . GLN B 142 ? 2.6275 2.3200 3.0187 -0.4622 0.2871  1.2131  653 GLN B CB  
4518  C CG  . GLN B 142 ? 2.7447 2.4077 3.0820 -0.4577 0.2895  1.2152  653 GLN B CG  
4519  C CD  . GLN B 142 ? 2.7851 2.4585 3.1154 -0.4417 0.3398  1.2092  653 GLN B CD  
4520  O OE1 . GLN B 142 ? 2.8107 2.5303 3.1486 -0.4302 0.3433  1.2211  653 GLN B OE1 
4521  N NE2 . GLN B 142 ? 2.7902 2.4194 3.1048 -0.4406 0.3785  1.1900  653 GLN B NE2 
4522  N N   . GLU B 143 ? 2.5257 2.1387 2.9491 -0.4824 0.2605  1.1215  654 GLU B N   
4523  C CA  . GLU B 143 ? 2.5057 2.0641 2.9229 -0.4880 0.2663  1.0728  654 GLU B CA  
4524  C C   . GLU B 143 ? 2.5179 2.0616 2.9200 -0.4986 0.2035  1.0693  654 GLU B C   
4525  O O   . GLU B 143 ? 2.5754 2.0737 2.9501 -0.5109 0.1856  1.0729  654 GLU B O   
4526  C CB  . GLU B 143 ? 2.4072 1.9649 2.8636 -0.4758 0.3141  0.9994  654 GLU B CB  
4527  C CG  . GLU B 143 ? 2.4110 1.9160 2.8674 -0.4805 0.3219  0.9410  654 GLU B CG  
4528  C CD  . GLU B 143 ? 2.3975 1.9081 2.8975 -0.4684 0.3696  0.8676  654 GLU B CD  
4529  O OE1 . GLU B 143 ? 2.4078 1.8846 2.9161 -0.4707 0.3719  0.8109  654 GLU B OE1 
4530  O OE2 . GLU B 143 ? 2.3797 1.9233 2.9046 -0.4574 0.4116  0.8667  654 GLU B OE2 
4531  N N   . LYS B 144 ? 2.5135 2.0949 2.9322 -0.4932 0.1699  1.0627  655 LYS B N   
4532  C CA  . LYS B 144 ? 2.5288 2.0967 2.9333 -0.5016 0.1110  1.0600  655 LYS B CA  
4533  C C   . LYS B 144 ? 2.6369 2.1994 3.0054 -0.5169 0.0687  1.1298  655 LYS B C   
4534  O O   . LYS B 144 ? 2.6825 2.2108 3.0286 -0.5297 0.0304  1.1322  655 LYS B O   
4535  C CB  . LYS B 144 ? 2.4656 2.0751 2.8947 -0.4891 0.0876  1.0364  655 LYS B CB  
4536  C CG  . LYS B 144 ? 2.4212 2.0334 2.8860 -0.4750 0.1181  0.9577  655 LYS B CG  
4537  C CD  . LYS B 144 ? 2.4053 2.0587 2.8887 -0.4615 0.0869  0.9380  655 LYS B CD  
4538  C CE  . LYS B 144 ? 2.3941 2.0536 2.9143 -0.4468 0.1134  0.8562  655 LYS B CE  
4539  N NZ  . LYS B 144 ? 2.3811 2.0820 2.9167 -0.4310 0.0807  0.8365  655 LYS B NZ  
4540  N N   . ASN B 145 ? 2.6662 2.2631 3.0301 -0.5161 0.0748  1.1860  656 ASN B N   
4541  C CA  . ASN B 145 ? 2.7776 2.3742 3.1055 -0.5259 0.0381  1.2388  656 ASN B CA  
4542  C C   . ASN B 145 ? 2.8412 2.3927 3.1361 -0.5296 0.0499  1.2267  656 ASN B C   
4543  O O   . ASN B 145 ? 2.9202 2.4578 3.1819 -0.5345 0.0123  1.2339  656 ASN B O   
4544  C CB  . ASN B 145 ? 2.8222 2.4738 3.1422 -0.5082 0.0461  1.2598  656 ASN B CB  
4545  C CG  . ASN B 145 ? 2.9305 2.6015 3.2174 -0.5059 -0.0007 1.2807  656 ASN B CG  
4546  O OD1 . ASN B 145 ? 2.9929 2.6345 3.2537 -0.5147 -0.0277 1.2788  656 ASN B OD1 
4547  N ND2 . ASN B 145 ? 2.9576 2.6798 3.2493 -0.4945 -0.0089 1.2994  656 ASN B ND2 
4548  N N   . GLU B 146 ? 2.9760 2.5045 3.2811 -0.5267 0.1036  1.2078  657 GLU B N   
4549  C CA  . GLU B 146 ? 3.0324 2.5132 3.3053 -0.5298 0.1166  1.1958  657 GLU B CA  
4550  C C   . GLU B 146 ? 3.0180 2.4509 3.2929 -0.5488 0.0870  1.1799  657 GLU B C   
4551  O O   . GLU B 146 ? 3.1171 2.5188 3.3561 -0.5538 0.0673  1.1792  657 GLU B O   
4552  C CB  . GLU B 146 ? 2.9959 2.4576 3.2800 -0.5221 0.1836  1.1766  657 GLU B CB  
4553  C CG  . GLU B 146 ? 3.0219 2.5211 3.2964 -0.5029 0.2170  1.1882  657 GLU B CG  
4554  C CD  . GLU B 146 ? 3.2100 2.7174 3.4330 -0.4938 0.1974  1.2082  657 GLU B CD  
4555  O OE1 . GLU B 146 ? 3.3521 2.8283 3.5444 -0.5010 0.1710  1.2094  657 GLU B OE1 
4556  O OE2 . GLU B 146 ? 3.2282 2.7745 3.4449 -0.4794 0.2093  1.2216  657 GLU B OE2 
4557  N N   . GLN B 147 ? 3.0157 2.4522 3.3196 -0.5450 0.0829  1.1332  658 GLN B N   
4558  C CA  . GLN B 147 ? 3.0036 2.4001 3.3020 -0.5525 0.0558  1.0911  658 GLN B CA  
4559  C C   . GLN B 147 ? 3.0777 2.4742 3.3544 -0.5664 -0.0094 1.1280  658 GLN B C   
4560  O O   . GLN B 147 ? 3.1200 2.4750 3.3778 -0.5781 -0.0354 1.1159  658 GLN B O   
4561  C CB  . GLN B 147 ? 2.8951 2.3034 3.2294 -0.5397 0.0691  1.0251  658 GLN B CB  
4562  C CG  . GLN B 147 ? 2.8910 2.2585 3.2259 -0.5441 0.0520  0.9692  658 GLN B CG  
4563  C CD  . GLN B 147 ? 2.8091 2.1946 3.1825 -0.5291 0.0699  0.9025  658 GLN B CD  
4564  O OE1 . GLN B 147 ? 2.7124 2.1419 3.1124 -0.5156 0.0945  0.8982  658 GLN B OE1 
4565  N NE2 . GLN B 147 ? 2.8444 2.1973 3.2219 -0.5312 0.0579  0.8488  658 GLN B NE2 
4566  N N   . ASP B 148 ? 2.8533 2.2946 3.1328 -0.5656 -0.0356 1.1724  659 ASP B N   
4567  C CA  . ASP B 148 ? 2.8651 2.3063 3.1234 -0.5783 -0.0943 1.2076  659 ASP B CA  
4568  C C   . ASP B 148 ? 2.9540 2.3853 3.1711 -0.5762 -0.1017 1.2136  659 ASP B C   
4569  O O   . ASP B 148 ? 3.0195 2.4361 3.2164 -0.5848 -0.1434 1.2160  659 ASP B O   
4570  C CB  . ASP B 148 ? 2.8525 2.3518 3.1168 -0.5671 -0.1139 1.2338  659 ASP B CB  
4571  C CG  . ASP B 148 ? 2.9431 2.4497 3.1844 -0.5709 -0.1688 1.2483  659 ASP B CG  
4572  O OD1 . ASP B 148 ? 2.9364 2.4273 3.1853 -0.5798 -0.2031 1.2451  659 ASP B OD1 
4573  O OD2 . ASP B 148 ? 3.0311 2.5575 3.2481 -0.5654 -0.1769 1.2618  659 ASP B OD2 
4574  N N   . LEU B 149 ? 2.9239 2.3630 3.1293 -0.5647 -0.0613 1.2160  660 LEU B N   
4575  C CA  . LEU B 149 ? 3.0320 2.4610 3.2001 -0.5620 -0.0660 1.2221  660 LEU B CA  
4576  C C   . LEU B 149 ? 3.0619 2.4300 3.2166 -0.5723 -0.0548 1.1997  660 LEU B C   
4577  O O   . LEU B 149 ? 3.1810 2.5323 3.3064 -0.5757 -0.0749 1.2027  660 LEU B O   
4578  C CB  . LEU B 149 ? 3.0653 2.5265 3.2228 -0.5441 -0.0306 1.2351  660 LEU B CB  
4579  C CG  . LEU B 149 ? 3.1216 2.6407 3.2764 -0.5344 -0.0535 1.2604  660 LEU B CG  
4580  C CD1 . LEU B 149 ? 3.0495 2.6019 3.2342 -0.5346 -0.0700 1.2671  660 LEU B CD1 
4581  C CD2 . LEU B 149 ? 3.1669 2.7106 3.3106 -0.5174 -0.0170 1.2692  660 LEU B CD2 
4582  N N   . LEU B 150 ? 3.3158 2.6517 3.4950 -0.5778 -0.0218 1.1762  661 LEU B N   
4583  C CA  . LEU B 150 ? 3.3473 2.6228 3.5183 -0.5876 -0.0051 1.1512  661 LEU B CA  
4584  C C   . LEU B 150 ? 3.3325 2.5702 3.5107 -0.6069 -0.0460 1.1334  661 LEU B C   
4585  O O   . LEU B 150 ? 3.3532 2.5410 3.5164 -0.6155 -0.0446 1.1128  661 LEU B O   
4586  C CB  . LEU B 150 ? 3.2701 2.5269 3.4692 -0.5841 0.0563  1.1304  661 LEU B CB  
4587  C CG  . LEU B 150 ? 3.2019 2.4889 3.3887 -0.5640 0.1003  1.1448  661 LEU B CG  
4588  C CD1 . LEU B 150 ? 3.1173 2.3942 3.3399 -0.5587 0.1650  1.1239  661 LEU B CD1 
4589  C CD2 . LEU B 150 ? 3.3413 2.6230 3.4785 -0.5547 0.0986  1.1594  661 LEU B CD2 
4590  N N   . ALA B 151 ? 3.1132 2.3755 3.3099 -0.6090 -0.0809 1.1321  662 ALA B N   
4591  C CA  . ALA B 151 ? 3.1046 2.3419 3.3035 -0.6147 -0.1163 1.0930  662 ALA B CA  
4592  C C   . ALA B 151 ? 3.2069 2.4355 3.3819 -0.6321 -0.1751 1.1317  662 ALA B C   
4593  O O   . ALA B 151 ? 3.2293 2.4293 3.4000 -0.6392 -0.2064 1.1038  662 ALA B O   
4594  C CB  . ALA B 151 ? 3.0133 2.2828 3.2443 -0.6014 -0.1185 1.0588  662 ALA B CB  
4595  N N   . LEU B 152 ? 3.2207 2.4909 3.3756 -0.6225 -0.1839 1.1629  663 LEU B N   
4596  C CA  . LEU B 152 ? 3.3140 2.5942 3.4468 -0.6268 -0.2317 1.1768  663 LEU B CA  
4597  C C   . LEU B 152 ? 3.3844 2.6289 3.4885 -0.6331 -0.2357 1.1682  663 LEU B C   
4598  O O   . LEU B 152 ? 3.4208 2.6572 3.5116 -0.6425 -0.2768 1.1701  663 LEU B O   
4599  C CB  . LEU B 152 ? 3.2369 2.5793 3.3663 -0.6138 -0.2381 1.2074  663 LEU B CB  
4600  C CG  . LEU B 152 ? 3.2607 2.6260 3.3760 -0.6001 -0.2031 1.2194  663 LEU B CG  
4601  C CD1 . LEU B 152 ? 3.2998 2.6612 3.3868 -0.6028 -0.2216 1.2274  663 LEU B CD1 
4602  C CD2 . LEU B 152 ? 3.1919 2.6157 3.3201 -0.5859 -0.1937 1.2407  663 LEU B CD2 
4603  N N   . ASP B 153 ? 3.5365 2.7596 3.6310 -0.6279 -0.1934 1.1593  664 ASP B N   
4604  C CA  . ASP B 153 ? 3.5154 2.7034 3.5810 -0.6322 -0.1943 1.1523  664 ASP B CA  
4605  C C   . ASP B 153 ? 3.4863 2.6097 3.5544 -0.6463 -0.1912 1.1186  664 ASP B C   
4606  O O   . ASP B 153 ? 3.4689 2.5545 3.5171 -0.6476 -0.1729 1.1067  664 ASP B O   
4607  C CB  . ASP B 153 ? 3.5128 2.7099 3.5608 -0.6169 -0.1507 1.1627  664 ASP B CB  
4608  C CG  . ASP B 153 ? 3.4932 2.6777 3.5584 -0.6095 -0.0956 1.1494  664 ASP B CG  
4609  O OD1 . ASP B 153 ? 3.4763 2.6297 3.5657 -0.6196 -0.0874 1.1251  664 ASP B OD1 
4610  O OD2 . ASP B 153 ? 3.4999 2.7056 3.5561 -0.5939 -0.0597 1.1621  664 ASP B OD2 
4611  N N   . ALA C 1   ? 2.8511 2.6788 2.8938 0.6939  0.0597  -0.1804 31  ALA C N   
4612  C CA  . ALA C 1   ? 2.8963 2.7775 2.9609 0.7050  0.0580  -0.1956 31  ALA C CA  
4613  C C   . ALA C 1   ? 2.8951 2.8215 2.9861 0.7120  0.0443  -0.2037 31  ALA C C   
4614  O O   . ALA C 1   ? 2.9093 2.8227 2.9796 0.7209  0.0398  -0.2116 31  ALA C O   
4615  C CB  . ALA C 1   ? 2.7550 2.6690 2.8537 0.6964  0.0617  -0.1908 31  ALA C CB  
4616  N N   . GLU C 2   ? 3.0254 3.0023 3.1602 0.7076  0.0368  -0.2023 32  GLU C N   
4617  C CA  . GLU C 2   ? 2.9884 3.0069 3.1470 0.7141  0.0210  -0.2104 32  GLU C CA  
4618  C C   . GLU C 2   ? 2.9467 2.9331 3.0965 0.7089  0.0136  -0.1966 32  GLU C C   
4619  O O   . GLU C 2   ? 2.9367 2.9366 3.0876 0.7176  0.0010  -0.2044 32  GLU C O   
4620  C CB  . GLU C 2   ? 2.9298 3.0064 3.1323 0.7107  0.0141  -0.2134 32  GLU C CB  
4621  C CG  . GLU C 2   ? 2.9210 3.0581 3.1420 0.7199  0.0136  -0.2382 32  GLU C CG  
4622  C CD  . GLU C 2   ? 2.9951 3.1668 3.2162 0.7335  0.0028  -0.2623 32  GLU C CD  
4623  O OE1 . GLU C 2   ? 2.9819 3.1437 3.2014 0.7362  -0.0099 -0.2578 32  GLU C OE1 
4624  O OE2 . GLU C 2   ? 3.0389 3.2441 3.2568 0.7202  0.0084  -0.2799 32  GLU C OE2 
4625  N N   . ASN C 3   ? 2.8435 2.7915 2.9852 0.6946  0.0207  -0.1788 33  ASN C N   
4626  C CA  . ASN C 3   ? 2.8380 2.7579 2.9688 0.6891  0.0152  -0.1689 33  ASN C CA  
4627  C C   . ASN C 3   ? 2.8592 2.7344 2.9514 0.6931  0.0189  -0.1707 33  ASN C C   
4628  O O   . ASN C 3   ? 2.8676 2.7092 2.9371 0.6887  0.0302  -0.1681 33  ASN C O   
4629  C CB  . ASN C 3   ? 2.7872 2.6933 2.9276 0.6717  0.0210  -0.1539 33  ASN C CB  
4630  C CG  . ASN C 3   ? 2.8000 2.6832 2.9307 0.6626  0.0353  -0.1497 33  ASN C CG  
4631  O OD1 . ASN C 3   ? 2.8400 2.7253 2.9634 0.6693  0.0411  -0.1568 33  ASN C OD1 
4632  N ND2 . ASN C 3   ? 2.8245 2.6865 2.9536 0.6480  0.0404  -0.1399 33  ASN C ND2 
4633  N N   . LEU C 4   ? 2.6115 2.4847 2.6949 0.7013  0.0084  -0.1755 34  LEU C N   
4634  C CA  . LEU C 4   ? 2.6078 2.4416 2.6555 0.7060  0.0104  -0.1788 34  LEU C CA  
4635  C C   . LEU C 4   ? 2.5770 2.3680 2.6058 0.6930  0.0153  -0.1665 34  LEU C C   
4636  O O   . LEU C 4   ? 2.5260 2.3215 2.5697 0.6822  0.0147  -0.1573 34  LEU C O   
4637  C CB  . LEU C 4   ? 2.5925 2.4425 2.6400 0.7189  -0.0034 -0.1894 34  LEU C CB  
4638  C CG  . LEU C 4   ? 2.5756 2.4797 2.6463 0.7321  -0.0106 -0.2071 34  LEU C CG  
4639  C CD1 . LEU C 4   ? 2.5656 2.4874 2.6376 0.7439  -0.0260 -0.2194 34  LEU C CD1 
4640  C CD2 . LEU C 4   ? 2.6037 2.5048 2.6583 0.7376  0.0022  -0.2186 34  LEU C CD2 
4641  N N   . TRP C 5   ? 2.6113 2.3617 2.6057 0.6944  0.0201  -0.1687 35  TRP C N   
4642  C CA  . TRP C 5   ? 2.6045 2.3174 2.5787 0.6835  0.0237  -0.1617 35  TRP C CA  
4643  C C   . TRP C 5   ? 2.6265 2.3122 2.5725 0.6903  0.0192  -0.1671 35  TRP C C   
4644  O O   . TRP C 5   ? 2.6376 2.3166 2.5673 0.7012  0.0191  -0.1760 35  TRP C O   
4645  C CB  . TRP C 5   ? 2.6287 2.3140 2.5869 0.6751  0.0352  -0.1590 35  TRP C CB  
4646  C CG  . TRP C 5   ? 2.6006 2.3101 2.5848 0.6683  0.0403  -0.1544 35  TRP C CG  
4647  C CD1 . TRP C 5   ? 2.6252 2.3526 2.6186 0.6741  0.0438  -0.1581 35  TRP C CD1 
4648  C CD2 . TRP C 5   ? 2.5967 2.3153 2.6003 0.6542  0.0429  -0.1466 35  TRP C CD2 
4649  N NE1 . TRP C 5   ? 2.6377 2.3844 2.6568 0.6636  0.0480  -0.1517 35  TRP C NE1 
4650  C CE2 . TRP C 5   ? 2.6178 2.3590 2.6435 0.6511  0.0476  -0.1446 35  TRP C CE2 
4651  C CE3 . TRP C 5   ? 2.6246 2.3353 2.6278 0.6442  0.0421  -0.1426 35  TRP C CE3 
4652  C CZ2 . TRP C 5   ? 2.6044 2.3589 2.6525 0.6374  0.0513  -0.1380 35  TRP C CZ2 
4653  C CZ3 . TRP C 5   ? 2.5951 2.3199 2.6188 0.6317  0.0461  -0.1373 35  TRP C CZ3 
4654  C CH2 . TRP C 5   ? 2.5599 2.3059 2.6063 0.6280  0.0505  -0.1347 35  TRP C CH2 
4655  N N   . VAL C 6   ? 2.4953 2.1655 2.4340 0.6837  0.0159  -0.1630 36  VAL C N   
4656  C CA  . VAL C 6   ? 2.5198 2.1645 2.4331 0.6889  0.0111  -0.1677 36  VAL C CA  
4657  C C   . VAL C 6   ? 2.6115 2.2144 2.4907 0.6869  0.0194  -0.1709 36  VAL C C   
4658  O O   . VAL C 6   ? 2.6057 2.1945 2.4792 0.6784  0.0272  -0.1678 36  VAL C O   
4659  C CB  . VAL C 6   ? 2.5082 2.1467 2.4205 0.6824  0.0057  -0.1637 36  VAL C CB  
4660  C CG1 . VAL C 6   ? 2.4867 2.1583 2.4259 0.6842  -0.0034 -0.1601 36  VAL C CG1 
4661  C CG2 . VAL C 6   ? 2.5212 2.1419 2.4259 0.6690  0.0144  -0.1602 36  VAL C CG2 
4662  N N   . THR C 7   ? 2.5513 2.1327 2.4060 0.6950  0.0167  -0.1779 37  THR C N   
4663  C CA  . THR C 7   ? 2.5694 2.1035 2.3849 0.6932  0.0226  -0.1815 37  THR C CA  
4664  C C   . THR C 7   ? 2.5512 2.0628 2.3461 0.6953  0.0170  -0.1857 37  THR C C   
4665  O O   . THR C 7   ? 2.5304 2.0669 2.3358 0.6902  0.0105  -0.1868 37  THR C O   
4666  C CB  . THR C 7   ? 2.5537 2.0802 2.3531 0.6960  0.0281  -0.1867 37  THR C CB  
4667  O OG1 . THR C 7   ? 2.5424 2.1206 2.3689 0.6867  0.0231  -0.1881 37  THR C OG1 
4668  C CG2 . THR C 7   ? 2.5434 2.0684 2.3472 0.6961  0.0354  -0.1835 37  THR C CG2 
4669  N N   . VAL C 8   ? 2.2776 1.7567 2.0512 0.6862  0.0188  -0.1852 38  VAL C N   
4670  C CA  . VAL C 8   ? 2.3042 1.7604 2.0580 0.6859  0.0140  -0.1893 38  VAL C CA  
4671  C C   . VAL C 8   ? 2.3366 1.7730 2.0639 0.6673  0.0158  -0.1899 38  VAL C C   
4672  O O   . VAL C 8   ? 2.3614 1.7674 2.0637 0.6628  0.0211  -0.1908 38  VAL C O   
4673  C CB  . VAL C 8   ? 2.3110 1.7538 2.0590 0.6744  0.0148  -0.1889 38  VAL C CB  
4674  C CG1 . VAL C 8   ? 2.3363 1.7583 2.0656 0.6739  0.0095  -0.1943 38  VAL C CG1 
4675  C CG2 . VAL C 8   ? 2.2754 1.7528 2.0547 0.6689  0.0146  -0.1834 38  VAL C CG2 
4676  N N   . TYR C 9   ? 2.3416 1.7978 2.0742 0.6511  0.0108  -0.1883 39  TYR C N   
4677  C CA  . TYR C 9   ? 2.3964 1.8407 2.1060 0.6260  0.0126  -0.1876 39  TYR C CA  
4678  C C   . TYR C 9   ? 2.4639 1.8877 2.1592 0.6196  0.0082  -0.1889 39  TYR C C   
4679  O O   . TYR C 9   ? 2.4306 1.8722 2.1429 0.6246  0.0019  -0.1889 39  TYR C O   
4680  C CB  . TYR C 9   ? 2.3494 1.8383 2.0773 0.6108  0.0116  -0.1868 39  TYR C CB  
4681  C CG  . TYR C 9   ? 2.3735 1.8776 2.1082 0.6116  0.0174  -0.1873 39  TYR C CG  
4682  C CD1 . TYR C 9   ? 2.3497 1.8828 2.1154 0.6322  0.0156  -0.1878 39  TYR C CD1 
4683  C CD2 . TYR C 9   ? 2.4309 1.9168 2.1378 0.5911  0.0244  -0.1873 39  TYR C CD2 
4684  C CE1 . TYR C 9   ? 2.3214 1.8701 2.0946 0.6324  0.0211  -0.1888 39  TYR C CE1 
4685  C CE2 . TYR C 9   ? 2.4104 1.9091 2.1210 0.5894  0.0298  -0.1881 39  TYR C CE2 
4686  C CZ  . TYR C 9   ? 2.3260 1.8581 2.0717 0.6103  0.0284  -0.1891 39  TYR C CZ  
4687  O OH  . TYR C 9   ? 2.2891 1.8364 2.0402 0.6078  0.0339  -0.1904 39  TYR C OH  
4688  N N   . TYR C 10  ? 2.0982 1.4831 1.7602 0.6079  0.0107  -0.1904 40  TYR C N   
4689  C CA  . TYR C 10  ? 2.0403 1.4036 1.6862 0.6004  0.0069  -0.1930 40  TYR C CA  
4690  C C   . TYR C 10  ? 2.0353 1.3931 1.6620 0.5737  0.0080  -0.1904 40  TYR C C   
4691  O O   . TYR C 10  ? 2.0825 1.4115 1.6802 0.5633  0.0118  -0.1902 40  TYR C O   
4692  C CB  . TYR C 10  ? 2.0169 1.3368 1.6390 0.6138  0.0068  -0.2001 40  TYR C CB  
4693  C CG  . TYR C 10  ? 2.0376 1.3374 1.6446 0.6082  0.0021  -0.2058 40  TYR C CG  
4694  C CD1 . TYR C 10  ? 2.0772 1.3975 1.7024 0.6103  -0.0021 -0.2076 40  TYR C CD1 
4695  C CD2 . TYR C 10  ? 2.0922 1.3506 1.6644 0.6005  0.0008  -0.2101 40  TYR C CD2 
4696  C CE1 . TYR C 10  ? 2.0896 1.3945 1.7019 0.6035  -0.0061 -0.2140 40  TYR C CE1 
4697  C CE2 . TYR C 10  ? 2.1512 1.3940 1.7113 0.5960  -0.0042 -0.2170 40  TYR C CE2 
4698  C CZ  . TYR C 10  ? 2.1200 1.3884 1.7017 0.5970  -0.0070 -0.2191 40  TYR C CZ  
4699  O OH  . TYR C 10  ? 2.0563 1.3122 1.6269 0.5908  -0.0118 -0.2270 40  TYR C OH  
4700  N N   . GLY C 11  ? 2.0032 1.3869 1.6436 0.5623  0.0045  -0.1888 41  GLY C N   
4701  C CA  . GLY C 11  ? 2.0255 1.4099 1.6510 0.5366  0.0061  -0.1870 41  GLY C CA  
4702  C C   . GLY C 11  ? 2.0112 1.4450 1.6607 0.5266  0.0066  -0.1857 41  GLY C C   
4703  O O   . GLY C 11  ? 2.0306 1.4715 1.6675 0.5050  0.0114  -0.1857 41  GLY C O   
4704  N N   . VAL C 12  ? 1.9906 1.4589 1.6729 0.5419  0.0008  -0.1860 42  VAL C N   
4705  C CA  . VAL C 12  ? 1.9763 1.4949 1.6838 0.5364  -0.0016 -0.1879 42  VAL C CA  
4706  C C   . VAL C 12  ? 1.9752 1.5119 1.6894 0.5252  -0.0076 -0.1887 42  VAL C C   
4707  O O   . VAL C 12  ? 1.9716 1.4918 1.6840 0.5302  -0.0130 -0.1869 42  VAL C O   
4708  C CB  . VAL C 12  ? 1.9462 1.4924 1.6843 0.5600  -0.0073 -0.1890 42  VAL C CB  
4709  C CG1 . VAL C 12  ? 1.9461 1.4809 1.6801 0.5692  -0.0003 -0.1886 42  VAL C CG1 
4710  C CG2 . VAL C 12  ? 1.9310 1.4655 1.6769 0.5775  -0.0155 -0.1872 42  VAL C CG2 
4711  N N   . PRO C 13  ? 1.9621 1.5332 1.6826 0.5085  -0.0064 -0.1926 43  PRO C N   
4712  C CA  . PRO C 13  ? 1.9582 1.5502 1.6867 0.4989  -0.0124 -0.1945 43  PRO C CA  
4713  C C   . PRO C 13  ? 1.9370 1.5542 1.6937 0.5187  -0.0261 -0.1960 43  PRO C C   
4714  O O   . PRO C 13  ? 1.9284 1.5895 1.7068 0.5209  -0.0324 -0.2029 43  PRO C O   
4715  C CB  . PRO C 13  ? 1.9952 1.6223 1.7236 0.4773  -0.0065 -0.2012 43  PRO C CB  
4716  C CG  . PRO C 13  ? 2.0463 1.6523 1.7523 0.4680  0.0046  -0.2002 43  PRO C CG  
4717  C CD  . PRO C 13  ? 1.9859 1.5743 1.7002 0.4934  0.0020  -0.1965 43  PRO C CD  
4718  N N   . VAL C 14  ? 1.9810 1.5714 1.7359 0.5328  -0.0319 -0.1914 44  VAL C N   
4719  C CA  . VAL C 14  ? 1.9644 1.5701 1.7384 0.5499  -0.0462 -0.1921 44  VAL C CA  
4720  C C   . VAL C 14  ? 1.9707 1.5531 1.7331 0.5442  -0.0515 -0.1888 44  VAL C C   
4721  O O   . VAL C 14  ? 1.9761 1.5234 1.7217 0.5434  -0.0467 -0.1857 44  VAL C O   
4722  C CB  . VAL C 14  ? 1.9494 1.5474 1.7319 0.5729  -0.0487 -0.1905 44  VAL C CB  
4723  C CG1 . VAL C 14  ? 1.9397 1.5421 1.7329 0.5880  -0.0645 -0.1901 44  VAL C CG1 
4724  C CG2 . VAL C 14  ? 1.9404 1.5673 1.7385 0.5789  -0.0451 -0.1944 44  VAL C CG2 
4725  N N   . TRP C 15  ? 1.8798 1.4832 1.6513 0.5406  -0.0622 -0.1909 45  TRP C N   
4726  C CA  . TRP C 15  ? 1.8834 1.4681 1.6446 0.5334  -0.0685 -0.1881 45  TRP C CA  
4727  C C   . TRP C 15  ? 1.9151 1.5131 1.6874 0.5457  -0.0869 -0.1895 45  TRP C C   
4728  O O   . TRP C 15  ? 1.9070 1.5364 1.6969 0.5568  -0.0955 -0.1947 45  TRP C O   
4729  C CB  . TRP C 15  ? 1.8784 1.4679 1.6316 0.5106  -0.0625 -0.1888 45  TRP C CB  
4730  C CG  . TRP C 15  ? 1.8777 1.5091 1.6462 0.5061  -0.0672 -0.1952 45  TRP C CG  
4731  C CD1 . TRP C 15  ? 1.9068 1.5587 1.6867 0.5112  -0.0823 -0.1988 45  TRP C CD1 
4732  C CD2 . TRP C 15  ? 1.8813 1.5401 1.6535 0.4950  -0.0574 -0.2008 45  TRP C CD2 
4733  N NE1 . TRP C 15  ? 1.9333 1.6272 1.7265 0.5060  -0.0827 -0.2080 45  TRP C NE1 
4734  C CE2 . TRP C 15  ? 1.9058 1.6065 1.6947 0.4945  -0.0666 -0.2096 45  TRP C CE2 
4735  C CE3 . TRP C 15  ? 1.8904 1.5412 1.6505 0.4845  -0.0424 -0.2003 45  TRP C CE3 
4736  C CZ2 . TRP C 15  ? 1.9217 1.6615 1.7175 0.4827  -0.0599 -0.2194 45  TRP C CZ2 
4737  C CZ3 . TRP C 15  ? 1.9447 1.6297 1.7085 0.4709  -0.0359 -0.2080 45  TRP C CZ3 
4738  C CH2 . TRP C 15  ? 1.9356 1.6673 1.7181 0.4694  -0.0438 -0.2182 45  TRP C CH2 
4739  N N   . LYS C 16  ? 1.9684 1.5414 1.7282 0.5432  -0.0940 -0.1860 46  LYS C N   
4740  C CA  . LYS C 16  ? 2.0000 1.5752 1.7614 0.5515  -0.1133 -0.1865 46  LYS C CA  
4741  C C   . LYS C 16  ? 2.0544 1.6144 1.8018 0.5341  -0.1167 -0.1843 46  LYS C C   
4742  O O   . LYS C 16  ? 2.0430 1.5827 1.7778 0.5199  -0.1055 -0.1819 46  LYS C O   
4743  C CB  . LYS C 16  ? 2.0143 1.5695 1.7706 0.5684  -0.1205 -0.1842 46  LYS C CB  
4744  C CG  . LYS C 16  ? 1.9985 1.5759 1.7732 0.5879  -0.1214 -0.1871 46  LYS C CG  
4745  C CD  . LYS C 16  ? 2.0860 1.6472 1.8571 0.6059  -0.1306 -0.1852 46  LYS C CD  
4746  C CE  . LYS C 16  ? 2.1182 1.7075 1.9114 0.6252  -0.1328 -0.1890 46  LYS C CE  
4747  N NZ  . LYS C 16  ? 2.1536 1.7270 1.9437 0.6432  -0.1393 -0.1867 46  LYS C NZ  
4748  N N   . ASP C 17  ? 2.1159 1.6862 1.8654 0.5358  -0.1335 -0.1863 47  ASP C N   
4749  C CA  . ASP C 17  ? 2.1695 1.7273 1.9066 0.5191  -0.1381 -0.1843 47  ASP C CA  
4750  C C   . ASP C 17  ? 2.1508 1.6708 1.8663 0.5124  -0.1392 -0.1797 47  ASP C C   
4751  O O   . ASP C 17  ? 2.1446 1.6477 1.8514 0.5239  -0.1489 -0.1785 47  ASP C O   
4752  C CB  . ASP C 17  ? 2.1862 1.7588 1.9272 0.5258  -0.1589 -0.1883 47  ASP C CB  
4753  C CG  . ASP C 17  ? 2.1976 1.8146 1.9608 0.5314  -0.1587 -0.1971 47  ASP C CG  
4754  O OD1 . ASP C 17  ? 2.1548 1.7909 1.9313 0.5386  -0.1488 -0.2001 47  ASP C OD1 
4755  O OD2 . ASP C 17  ? 2.1998 1.8339 1.9664 0.5279  -0.1686 -0.2023 47  ASP C OD2 
4756  N N   . ALA C 18  ? 2.2018 1.7099 1.9078 0.4926  -0.1294 -0.1782 48  ALA C N   
4757  C CA  . ALA C 18  ? 2.2378 1.7159 1.9238 0.4825  -0.1297 -0.1770 48  ALA C CA  
4758  C C   . ALA C 18  ? 2.2822 1.7581 1.9625 0.4599  -0.1256 -0.1768 48  ALA C C   
4759  O O   . ALA C 18  ? 2.2828 1.7786 1.9741 0.4535  -0.1221 -0.1767 48  ALA C O   
4760  C CB  . ALA C 18  ? 2.1607 1.6262 1.8432 0.4878  -0.1164 -0.1790 48  ALA C CB  
4761  N N   . GLU C 19  ? 2.3208 1.7745 1.9837 0.4466  -0.1257 -0.1778 49  GLU C N   
4762  C CA  . GLU C 19  ? 2.2939 1.7449 1.9511 0.4241  -0.1223 -0.1785 49  GLU C CA  
4763  C C   . GLU C 19  ? 2.2580 1.6965 1.9070 0.4146  -0.1100 -0.1843 49  GLU C C   
4764  O O   . GLU C 19  ? 2.2520 1.6761 1.8897 0.4187  -0.1105 -0.1885 49  GLU C O   
4765  C CB  . GLU C 19  ? 2.3648 1.8047 2.0078 0.4141  -0.1390 -0.1763 49  GLU C CB  
4766  C CG  . GLU C 19  ? 2.4168 1.8715 2.0693 0.4264  -0.1525 -0.1734 49  GLU C CG  
4767  C CD  . GLU C 19  ? 2.5718 2.0108 2.2069 0.4207  -0.1728 -0.1714 49  GLU C CD  
4768  O OE1 . GLU C 19  ? 2.6795 2.0943 2.2927 0.4048  -0.1763 -0.1712 49  GLU C OE1 
4769  O OE2 . GLU C 19  ? 2.7003 2.1516 2.3422 0.4315  -0.1860 -0.1714 49  GLU C OE2 
4770  N N   . THR C 20  ? 2.1249 1.5696 1.7785 0.4021  -0.0998 -0.1861 50  THR C N   
4771  C CA  . THR C 20  ? 2.0891 1.5238 1.7356 0.3945  -0.0901 -0.1943 50  THR C CA  
4772  C C   . THR C 20  ? 2.0961 1.5347 1.7421 0.3729  -0.0879 -0.1958 50  THR C C   
4773  O O   . THR C 20  ? 2.1167 1.5652 1.7675 0.3636  -0.0930 -0.1899 50  THR C O   
4774  C CB  . THR C 20  ? 2.0871 1.5207 1.7385 0.4080  -0.0785 -0.1966 50  THR C CB  
4775  O OG1 . THR C 20  ? 2.0776 1.4996 1.7201 0.4033  -0.0722 -0.2071 50  THR C OG1 
4776  C CG2 . THR C 20  ? 2.0713 1.5176 1.7322 0.4045  -0.0726 -0.1912 50  THR C CG2 
4777  N N   . THR C 21  ? 2.0905 1.5224 1.7309 0.3659  -0.0810 -0.2053 51  THR C N   
4778  C CA  . THR C 21  ? 2.1588 1.5948 1.7992 0.3461  -0.0787 -0.2089 51  THR C CA  
4779  C C   . THR C 21  ? 2.1286 1.5678 1.7754 0.3474  -0.0696 -0.2062 51  THR C C   
4780  O O   . THR C 21  ? 2.0794 1.5081 1.7215 0.3569  -0.0633 -0.2119 51  THR C O   
4781  C CB  . THR C 21  ? 2.2365 1.6660 1.8669 0.3376  -0.0782 -0.2236 51  THR C CB  
4782  O OG1 . THR C 21  ? 2.3928 1.8139 2.0206 0.3526  -0.0714 -0.2325 51  THR C OG1 
4783  C CG2 . THR C 21  ? 2.2746 1.6993 1.8936 0.3336  -0.0863 -0.2268 51  THR C CG2 
4784  N N   . LEU C 22  ? 2.1085 1.5604 1.7630 0.3374  -0.0695 -0.1981 52  LEU C N   
4785  C CA  . LEU C 22  ? 2.0687 1.5250 1.7263 0.3340  -0.0609 -0.1947 52  LEU C CA  
4786  C C   . LEU C 22  ? 2.0147 1.4671 1.6684 0.3175  -0.0575 -0.2004 52  LEU C C   
4787  O O   . LEU C 22  ? 2.1053 1.5624 1.7603 0.3038  -0.0624 -0.2037 52  LEU C O   
4788  C CB  . LEU C 22  ? 2.1142 1.5907 1.7824 0.3306  -0.0622 -0.1858 52  LEU C CB  
4789  C CG  . LEU C 22  ? 2.1947 1.6799 1.8691 0.3474  -0.0679 -0.1818 52  LEU C CG  
4790  C CD1 . LEU C 22  ? 2.2019 1.7110 1.8873 0.3435  -0.0708 -0.1772 52  LEU C CD1 
4791  C CD2 . LEU C 22  ? 2.2126 1.6916 1.8849 0.3629  -0.0610 -0.1827 52  LEU C CD2 
4792  N N   . PHE C 23  ? 2.0906 1.5328 1.7373 0.3181  -0.0501 -0.2021 53  PHE C N   
4793  C CA  . PHE C 23  ? 2.1519 1.5894 1.7941 0.3036  -0.0481 -0.2076 53  PHE C CA  
4794  C C   . PHE C 23  ? 2.2118 1.6589 1.8564 0.2906  -0.0420 -0.1991 53  PHE C C   
4795  O O   . PHE C 23  ? 2.1417 1.6007 1.7911 0.2929  -0.0388 -0.1908 53  PHE C O   
4796  C CB  . PHE C 23  ? 2.1897 1.6033 1.8169 0.3133  -0.0471 -0.2187 53  PHE C CB  
4797  C CG  . PHE C 23  ? 2.2392 1.6357 1.8542 0.3250  -0.0415 -0.2144 53  PHE C CG  
4798  C CD1 . PHE C 23  ? 2.2012 1.5925 1.8151 0.3429  -0.0414 -0.2135 53  PHE C CD1 
4799  C CD2 . PHE C 23  ? 2.3084 1.6921 1.9103 0.3166  -0.0366 -0.2118 53  PHE C CD2 
4800  C CE1 . PHE C 23  ? 2.2132 1.5886 1.8145 0.3517  -0.0363 -0.2100 53  PHE C CE1 
4801  C CE2 . PHE C 23  ? 2.3256 1.6902 1.9109 0.3241  -0.0319 -0.2082 53  PHE C CE2 
4802  C CZ  . PHE C 23  ? 2.2418 1.6029 1.8274 0.3414  -0.0317 -0.2075 53  PHE C CZ  
4803  N N   . CYS C 24  ? 2.4199 1.8635 2.0609 0.2766  -0.0404 -0.2029 54  CYS C N   
4804  C CA  . CYS C 24  ? 2.4247 1.8789 2.0679 0.2605  -0.0345 -0.1961 54  CYS C CA  
4805  C C   . CYS C 24  ? 2.4190 1.8521 2.0429 0.2596  -0.0278 -0.1959 54  CYS C C   
4806  O O   . CYS C 24  ? 2.4574 1.8647 2.0651 0.2719  -0.0290 -0.2016 54  CYS C O   
4807  C CB  . CYS C 24  ? 2.5120 1.9773 2.1639 0.2430  -0.0373 -0.1995 54  CYS C CB  
4808  S SG  . CYS C 24  ? 2.7955 2.2402 2.4355 0.2407  -0.0403 -0.2140 54  CYS C SG  
4809  N N   . ALA C 25  ? 2.5156 1.9585 2.1387 0.2439  -0.0210 -0.1897 55  ALA C N   
4810  C CA  . ALA C 25  ? 2.5423 1.9646 2.1428 0.2365  -0.0144 -0.1885 55  ALA C CA  
4811  C C   . ALA C 25  ? 2.5737 2.0146 2.1793 0.2153  -0.0079 -0.1833 55  ALA C C   
4812  O O   . ALA C 25  ? 2.5333 2.0057 2.1571 0.2098  -0.0050 -0.1782 55  ALA C O   
4813  C CB  . ALA C 25  ? 2.5618 1.9761 2.1490 0.2445  -0.0090 -0.1843 55  ALA C CB  
4814  N N   . SER C 26  ? 2.7813 2.2033 2.3708 0.2041  -0.0064 -0.1856 56  SER C N   
4815  C CA  . SER C 26  ? 2.8194 2.2608 2.4154 0.1836  0.0001  -0.1810 56  SER C CA  
4816  C C   . SER C 26  ? 3.0241 2.4363 2.5903 0.1718  0.0043  -0.1812 56  SER C C   
4817  O O   . SER C 26  ? 2.9171 2.3224 2.4815 0.1626  0.0016  -0.1845 56  SER C O   
4818  C CB  . SER C 26  ? 2.7495 2.2105 2.3694 0.1782  -0.0059 -0.1843 56  SER C CB  
4819  O OG  . SER C 26  ? 2.7878 2.2269 2.4012 0.1845  -0.0149 -0.1946 56  SER C OG  
4820  N N   . ASP C 27  ? 3.0931 2.4861 2.6331 0.1711  0.0103  -0.1780 57  ASP C N   
4821  C CA  . ASP C 27  ? 3.1591 2.5206 2.6635 0.1567  0.0147  -0.1767 57  ASP C CA  
4822  C C   . ASP C 27  ? 3.1859 2.5079 2.6713 0.1617  0.0036  -0.1843 57  ASP C C   
4823  O O   . ASP C 27  ? 3.1661 2.4806 2.6609 0.1795  -0.0073 -0.1927 57  ASP C O   
4824  C CB  . ASP C 27  ? 3.1839 2.5733 2.6949 0.1332  0.0257  -0.1713 57  ASP C CB  
4825  C CG  . ASP C 27  ? 3.1819 2.6110 2.7077 0.1281  0.0360  -0.1672 57  ASP C CG  
4826  O OD1 . ASP C 27  ? 3.2000 2.6224 2.7128 0.1343  0.0384  -0.1671 57  ASP C OD1 
4827  O OD2 . ASP C 27  ? 3.2227 2.6910 2.7737 0.1184  0.0410  -0.1655 57  ASP C OD2 
4828  N N   . ALA C 28  ? 3.3456 2.6432 2.8026 0.1457  0.0060  -0.1829 58  ALA C N   
4829  C CA  . ALA C 28  ? 3.4047 2.6642 2.8406 0.1489  -0.0058 -0.1911 58  ALA C CA  
4830  C C   . ALA C 28  ? 3.4871 2.7600 2.9290 0.1290  -0.0022 -0.1892 58  ALA C C   
4831  O O   . ALA C 28  ? 3.5391 2.7976 2.9797 0.1322  -0.0132 -0.1980 58  ALA C O   
4832  C CB  . ALA C 28  ? 3.4416 2.6413 2.8240 0.1511  -0.0104 -0.1921 58  ALA C CB  
4833  N N   . LYS C 29  ? 3.6671 2.9700 3.1169 0.1091  0.0126  -0.1796 59  LYS C N   
4834  C CA  . LYS C 29  ? 3.7319 3.0544 3.1922 0.0897  0.0180  -0.1771 59  LYS C CA  
4835  C C   . LYS C 29  ? 3.7363 3.1062 3.2463 0.0929  0.0161  -0.1792 59  LYS C C   
4836  O O   . LYS C 29  ? 3.7550 3.1368 3.2784 0.0831  0.0145  -0.1811 59  LYS C O   
4837  C CB  . LYS C 29  ? 3.7176 3.0551 3.1650 0.0663  0.0350  -0.1682 59  LYS C CB  
4838  C CG  . LYS C 29  ? 3.6801 3.0373 3.1380 0.0465  0.0411  -0.1659 59  LYS C CG  
4839  C CD  . LYS C 29  ? 3.5989 2.9555 3.0290 0.0209  0.0565  -0.1599 59  LYS C CD  
4840  C CE  . LYS C 29  ? 3.5791 2.8875 2.9687 0.0094  0.0516  -0.1606 59  LYS C CE  
4841  N NZ  . LYS C 29  ? 3.5002 2.8228 2.8776 -0.0191 0.0670  -0.1553 59  LYS C NZ  
4842  N N   . ALA C 30  ? 3.7817 3.1766 3.3169 0.1061  0.0153  -0.1790 60  ALA C N   
4843  C CA  . ALA C 30  ? 3.7363 3.1704 3.3124 0.1077  0.0121  -0.1807 60  ALA C CA  
4844  C C   . ALA C 30  ? 3.7358 3.1577 3.3179 0.1161  -0.0016 -0.1922 60  ALA C C   
4845  O O   . ALA C 30  ? 3.7165 3.1662 3.3264 0.1098  -0.0044 -0.1952 60  ALA C O   
4846  C CB  . ALA C 30  ? 3.6109 3.0678 3.2062 0.1202  0.0123  -0.1782 60  ALA C CB  
4847  N N   . TYR C 31  ? 3.8422 3.2242 3.3982 0.1300  -0.0107 -0.2003 61  TYR C N   
4848  C CA  . TYR C 31  ? 3.8825 3.2541 3.4420 0.1393  -0.0248 -0.2154 61  TYR C CA  
4849  C C   . TYR C 31  ? 3.9031 3.2625 3.4516 0.1265  -0.0276 -0.2190 61  TYR C C   
4850  O O   . TYR C 31  ? 3.9206 3.2858 3.4812 0.1289  -0.0383 -0.2325 61  TYR C O   
4851  C CB  . TYR C 31  ? 3.9415 3.2754 3.4766 0.1617  -0.0347 -0.2247 61  TYR C CB  
4852  C CG  . TYR C 31  ? 4.0030 3.3295 3.5417 0.1748  -0.0504 -0.2448 61  TYR C CG  
4853  C CD1 . TYR C 31  ? 3.9306 3.2881 3.4989 0.1808  -0.0546 -0.2538 61  TYR C CD1 
4854  C CD2 . TYR C 31  ? 4.0775 3.3646 3.5869 0.1817  -0.0621 -0.2565 61  TYR C CD2 
4855  C CE1 . TYR C 31  ? 3.9627 3.3190 3.5345 0.1914  -0.0682 -0.2754 61  TYR C CE1 
4856  C CE2 . TYR C 31  ? 4.1043 3.3891 3.6181 0.1956  -0.0778 -0.2787 61  TYR C CE2 
4857  C CZ  . TYR C 31  ? 4.0480 3.3704 3.5944 0.1998  -0.0799 -0.2888 61  TYR C CZ  
4858  O OH  . TYR C 31  ? 4.0141 3.3393 3.5649 0.2119  -0.0948 -0.3140 61  TYR C OH  
4859  N N   . GLU C 32  ? 3.7759 3.1202 3.3010 0.1121  -0.0182 -0.2084 62  GLU C N   
4860  C CA  . GLU C 32  ? 3.7671 3.0972 3.2779 0.0983  -0.0198 -0.2099 62  GLU C CA  
4861  C C   . GLU C 32  ? 3.7208 3.0976 3.2673 0.0799  -0.0118 -0.2053 62  GLU C C   
4862  O O   . GLU C 32  ? 3.7157 3.0876 3.2571 0.0680  -0.0131 -0.2071 62  GLU C O   
4863  C CB  . GLU C 32  ? 3.7540 3.0457 3.2196 0.0876  -0.0125 -0.2006 62  GLU C CB  
4864  C CG  . GLU C 32  ? 3.8020 3.0387 3.2250 0.1040  -0.0225 -0.2056 62  GLU C CG  
4865  C CD  . GLU C 32  ? 3.8439 3.0394 3.2165 0.0896  -0.0156 -0.1964 62  GLU C CD  
4866  O OE1 . GLU C 32  ? 3.7674 2.9749 3.1364 0.0667  -0.0042 -0.1884 62  GLU C OE1 
4867  O OE2 . GLU C 32  ? 3.9583 3.1097 3.2936 0.0997  -0.0210 -0.1976 62  GLU C OE2 
4868  N N   . THR C 33  ? 3.7266 3.1458 3.3066 0.0775  -0.0043 -0.1994 63  THR C N   
4869  C CA  . THR C 33  ? 3.6683 3.1307 3.2819 0.0611  0.0018  -0.1956 63  THR C CA  
4870  C C   . THR C 33  ? 3.6633 3.1377 3.2985 0.0631  -0.0108 -0.2091 63  THR C C   
4871  O O   . THR C 33  ? 3.6217 3.1231 3.2788 0.0479  -0.0085 -0.2089 63  THR C O   
4872  C CB  . THR C 33  ? 3.5980 3.0975 3.2371 0.0598  0.0102  -0.1869 63  THR C CB  
4873  O OG1 . THR C 33  ? 3.6204 3.1098 3.2393 0.0622  0.0193  -0.1789 63  THR C OG1 
4874  C CG2 . THR C 33  ? 3.5649 3.1039 3.2309 0.0409  0.0184  -0.1810 63  THR C CG2 
4875  N N   . GLU C 34  ? 3.5321 2.9878 3.1605 0.0813  -0.0239 -0.2223 64  GLU C N   
4876  C CA  . GLU C 34  ? 3.4979 2.9647 3.1431 0.0862  -0.0375 -0.2404 64  GLU C CA  
4877  C C   . GLU C 34  ? 3.4111 2.9250 3.0942 0.0696  -0.0344 -0.2396 64  GLU C C   
4878  O O   . GLU C 34  ? 3.3337 2.8702 3.0339 0.0681  -0.0302 -0.2331 64  GLU C O   
4879  C CB  . GLU C 34  ? 3.5414 2.9807 3.1671 0.0888  -0.0486 -0.2536 64  GLU C CB  
4880  C CG  . GLU C 34  ? 3.5309 2.9591 3.1420 0.0725  -0.0409 -0.2429 64  GLU C CG  
4881  C CD  . GLU C 34  ? 3.5400 2.9481 3.1384 0.0736  -0.0546 -0.2576 64  GLU C CD  
4882  O OE1 . GLU C 34  ? 3.6099 3.0052 3.2038 0.0906  -0.0712 -0.2775 64  GLU C OE1 
4883  O OE2 . GLU C 34  ? 3.4657 2.8718 3.0584 0.0580  -0.0493 -0.2506 64  GLU C OE2 
4884  N N   . LYS C 35  ? 3.3723 2.8987 3.0664 0.0573  -0.0378 -0.2466 65  LYS C N   
4885  C CA  . LYS C 35  ? 3.3292 2.8990 3.0579 0.0396  -0.0363 -0.2480 65  LYS C CA  
4886  C C   . LYS C 35  ? 3.3359 2.9254 3.0815 0.0433  -0.0450 -0.2608 65  LYS C C   
4887  O O   . LYS C 35  ? 3.3200 2.9365 3.0850 0.0325  -0.0408 -0.2539 65  LYS C O   
4888  C CB  . LYS C 35  ? 3.2570 2.8481 2.9979 0.0253  -0.0213 -0.2277 65  LYS C CB  
4889  C CG  . LYS C 35  ? 3.2629 2.8451 2.9913 0.0151  -0.0107 -0.2168 65  LYS C CG  
4890  C CD  . LYS C 35  ? 3.2798 2.8632 3.0116 0.0053  -0.0156 -0.2256 65  LYS C CD  
4891  C CE  . LYS C 35  ? 3.2935 2.8588 3.0034 -0.0037 -0.0050 -0.2141 65  LYS C CE  
4892  N NZ  . LYS C 35  ? 3.3191 2.8788 3.0269 -0.0117 -0.0109 -0.2222 65  LYS C NZ  
4893  N N   . HIS C 36  ? 3.4107 2.9853 3.1459 0.0583  -0.0577 -0.2806 66  HIS C N   
4894  C CA  . HIS C 36  ? 3.3940 2.9882 3.1421 0.0603  -0.0658 -0.2965 66  HIS C CA  
4895  C C   . HIS C 36  ? 3.3137 2.9097 3.0620 0.0636  -0.0599 -0.2836 66  HIS C C   
4896  O O   . HIS C 36  ? 3.1783 2.8008 2.9439 0.0498  -0.0589 -0.2816 66  HIS C O   
4897  C CB  . HIS C 36  ? 3.3400 2.9739 3.1154 0.0395  -0.0699 -0.3090 66  HIS C CB  
4898  C CG  . HIS C 36  ? 3.3955 3.0296 3.1715 0.0404  -0.0799 -0.3284 66  HIS C CG  
4899  N ND1 . HIS C 36  ? 3.3558 3.0232 3.1557 0.0205  -0.0817 -0.3361 66  HIS C ND1 
4900  C CD2 . HIS C 36  ? 3.4530 3.0571 3.2075 0.0600  -0.0905 -0.3429 66  HIS C CD2 
4901  C CE1 . HIS C 36  ? 3.4139 3.0734 3.2082 0.0283  -0.0931 -0.3551 66  HIS C CE1 
4902  N NE2 . HIS C 36  ? 3.4549 3.0743 3.2204 0.0528  -0.0993 -0.3597 66  HIS C NE2 
4903  N N   . ASN C 37  ? 3.3297 2.8951 3.0563 0.0817  -0.0569 -0.2750 67  ASN C N   
4904  C CA  . ASN C 37  ? 3.2082 2.7717 2.9326 0.0888  -0.0527 -0.2638 67  ASN C CA  
4905  C C   . ASN C 37  ? 3.0653 2.6498 2.8043 0.0742  -0.0437 -0.2452 67  ASN C C   
4906  O O   . ASN C 37  ? 2.9816 2.5898 2.7366 0.0615  -0.0462 -0.2464 67  ASN C O   
4907  C CB  . ASN C 37  ? 3.1439 2.7185 2.8738 0.0922  -0.0614 -0.2799 67  ASN C CB  
4908  C CG  . ASN C 37  ? 3.1165 2.6694 2.8305 0.1130  -0.0624 -0.2790 67  ASN C CG  
4909  O OD1 . ASN C 37  ? 3.1272 2.6588 2.8278 0.1244  -0.0565 -0.2653 67  ASN C OD1 
4910  N ND2 . ASN C 37  ? 3.0569 2.6182 2.7727 0.1160  -0.0693 -0.2940 67  ASN C ND2 
4911  N N   . VAL C 38  ? 2.9697 2.5453 2.7010 0.0756  -0.0339 -0.2292 68  VAL C N   
4912  C CA  . VAL C 38  ? 2.8808 2.4774 2.6252 0.0651  -0.0264 -0.2139 68  VAL C CA  
4913  C C   . VAL C 38  ? 2.8641 2.4556 2.6038 0.0785  -0.0280 -0.2084 68  VAL C C   
4914  O O   . VAL C 38  ? 2.8846 2.4540 2.6076 0.0955  -0.0274 -0.2081 68  VAL C O   
4915  C CB  . VAL C 38  ? 2.8930 2.4879 2.6315 0.0593  -0.0148 -0.2021 68  VAL C CB  
4916  C CG1 . VAL C 38  ? 2.8957 2.5015 2.6433 0.0427  -0.0133 -0.2057 68  VAL C CG1 
4917  C CG2 . VAL C 38  ? 2.9323 2.4945 2.6435 0.0740  -0.0121 -0.2011 68  VAL C CG2 
4918  N N   . TRP C 39  ? 2.6018 2.2119 2.3546 0.0710  -0.0311 -0.2045 69  TRP C N   
4919  C CA  . TRP C 39  ? 2.5805 2.1858 2.3286 0.0830  -0.0348 -0.1996 69  TRP C CA  
4920  C C   . TRP C 39  ? 2.5895 2.1758 2.3253 0.0979  -0.0417 -0.2102 69  TRP C C   
4921  O O   . TRP C 39  ? 2.5747 2.1651 2.3127 0.0918  -0.0493 -0.2213 69  TRP C O   
4922  C CB  . TRP C 39  ? 2.5831 2.1869 2.3264 0.0931  -0.0272 -0.1876 69  TRP C CB  
4923  C CG  . TRP C 39  ? 2.5542 2.1598 2.2974 0.1030  -0.0332 -0.1826 69  TRP C CG  
4924  C CD1 . TRP C 39  ? 2.5531 2.1480 2.2871 0.1216  -0.0332 -0.1797 69  TRP C CD1 
4925  C CD2 . TRP C 39  ? 2.5211 2.1381 2.2721 0.0948  -0.0415 -0.1804 69  TRP C CD2 
4926  N NE1 . TRP C 39  ? 2.5210 2.1204 2.2573 0.1268  -0.0416 -0.1763 69  TRP C NE1 
4927  C CE2 . TRP C 39  ? 2.5033 2.1136 2.2478 0.1105  -0.0474 -0.1764 69  TRP C CE2 
4928  C CE3 . TRP C 39  ? 2.5047 2.1352 2.2656 0.0750  -0.0455 -0.1816 69  TRP C CE3 
4929  C CZ2 . TRP C 39  ? 2.4743 2.0865 2.2185 0.1080  -0.0585 -0.1735 69  TRP C CZ2 
4930  C CZ3 . TRP C 39  ? 2.4760 2.1084 2.2360 0.0709  -0.0555 -0.1783 69  TRP C CZ3 
4931  C CH2 . TRP C 39  ? 2.4634 2.0845 2.2134 0.0877  -0.0626 -0.1742 69  TRP C CH2 
4932  N N   . ALA C 40  ? 2.5666 2.1333 2.2886 0.1162  -0.0385 -0.2079 70  ALA C N   
4933  C CA  . ALA C 40  ? 2.5704 2.1185 2.2803 0.1336  -0.0438 -0.2161 70  ALA C CA  
4934  C C   . ALA C 40  ? 2.6188 2.1437 2.3134 0.1456  -0.0430 -0.2245 70  ALA C C   
4935  O O   . ALA C 40  ? 2.6319 2.1473 2.3205 0.1542  -0.0498 -0.2389 70  ALA C O   
4936  C CB  . ALA C 40  ? 2.5628 2.1060 2.2682 0.1480  -0.0426 -0.2058 70  ALA C CB  
4937  N N   . THR C 41  ? 2.8805 2.3946 2.5657 0.1460  -0.0356 -0.2171 71  THR C N   
4938  C CA  . THR C 41  ? 3.0152 2.4987 2.6784 0.1583  -0.0363 -0.2232 71  THR C CA  
4939  C C   . THR C 41  ? 3.0926 2.5674 2.7521 0.1595  -0.0454 -0.2415 71  THR C C   
4940  O O   . THR C 41  ? 3.1165 2.5896 2.7742 0.1495  -0.0456 -0.2446 71  THR C O   
4941  C CB  . THR C 41  ? 3.1053 2.5787 2.7555 0.1516  -0.0270 -0.2126 71  THR C CB  
4942  O OG1 . THR C 41  ? 3.0987 2.5883 2.7555 0.1492  -0.0188 -0.1991 71  THR C OG1 
4943  C CG2 . THR C 41  ? 3.2033 2.6377 2.8235 0.1651  -0.0286 -0.2166 71  THR C CG2 
4944  N N   . HIS C 42  ? 3.1798 2.6505 2.8378 0.1722  -0.0533 -0.2553 72  HIS C N   
4945  C CA  . HIS C 42  ? 3.2321 2.6967 2.8857 0.1772  -0.0635 -0.2774 72  HIS C CA  
4946  C C   . HIS C 42  ? 3.2823 2.7162 2.9143 0.2013  -0.0683 -0.2861 72  HIS C C   
4947  O O   . HIS C 42  ? 3.3682 2.7735 2.9798 0.2104  -0.0729 -0.2926 72  HIS C O   
4948  C CB  . HIS C 42  ? 3.1687 2.6640 2.8416 0.1667  -0.0692 -0.2915 72  HIS C CB  
4949  C CG  . HIS C 42  ? 3.1801 2.6782 2.8521 0.1694  -0.0799 -0.3179 72  HIS C CG  
4950  N ND1 . HIS C 42  ? 3.2788 2.7481 2.9313 0.1865  -0.0866 -0.3294 72  HIS C ND1 
4951  C CD2 . HIS C 42  ? 3.1743 2.7017 2.8615 0.1568  -0.0862 -0.3369 72  HIS C CD2 
4952  C CE1 . HIS C 42  ? 3.2742 2.7563 2.9317 0.1868  -0.0975 -0.3555 72  HIS C CE1 
4953  N NE2 . HIS C 42  ? 3.2232 2.7430 2.9028 0.1680  -0.0967 -0.3609 72  HIS C NE2 
4954  N N   . ALA C 43  ? 2.9697 2.4065 2.6038 0.2121  -0.0681 -0.2863 73  ALA C N   
4955  C CA  . ALA C 43  ? 2.9367 2.3465 2.5522 0.2355  -0.0714 -0.2932 73  ALA C CA  
4956  C C   . ALA C 43  ? 2.9404 2.3404 2.5505 0.2425  -0.0628 -0.2733 73  ALA C C   
4957  O O   . ALA C 43  ? 2.9397 2.3306 2.5442 0.2590  -0.0637 -0.2758 73  ALA C O   
4958  C CB  . ALA C 43  ? 2.9322 2.3547 2.5537 0.2437  -0.0786 -0.3138 73  ALA C CB  
4959  N N   . CYS C 44  ? 2.9231 2.3281 2.5359 0.2300  -0.0544 -0.2551 74  CYS C N   
4960  C CA  . CYS C 44  ? 2.9189 2.3208 2.5285 0.2352  -0.0466 -0.2388 74  CYS C CA  
4961  C C   . CYS C 44  ? 2.8840 2.2502 2.4656 0.2453  -0.0448 -0.2369 74  CYS C C   
4962  O O   . CYS C 44  ? 2.9279 2.2740 2.4926 0.2400  -0.0465 -0.2400 74  CYS C O   
4963  C CB  . CYS C 44  ? 2.9019 2.3288 2.5264 0.2178  -0.0390 -0.2236 74  CYS C CB  
4964  S SG  . CYS C 44  ? 2.8606 2.2946 2.4870 0.2256  -0.0319 -0.2086 74  CYS C SG  
4965  N N   . VAL C 45  ? 2.6842 2.0408 2.2589 0.2591  -0.0421 -0.2316 75  VAL C N   
4966  C CA  . VAL C 45  ? 2.7505 2.0709 2.2957 0.2686  -0.0408 -0.2298 75  VAL C CA  
4967  C C   . VAL C 45  ? 2.7944 2.1103 2.3267 0.2518  -0.0317 -0.2166 75  VAL C C   
4968  O O   . VAL C 45  ? 2.7697 2.1150 2.3187 0.2414  -0.0235 -0.2057 75  VAL C O   
4969  C CB  . VAL C 45  ? 2.7436 2.0608 2.2888 0.2862  -0.0396 -0.2276 75  VAL C CB  
4970  C CG1 . VAL C 45  ? 2.8121 2.0910 2.3250 0.2939  -0.0382 -0.2254 75  VAL C CG1 
4971  C CG2 . VAL C 45  ? 2.7031 2.0243 2.2581 0.3014  -0.0477 -0.2420 75  VAL C CG2 
4972  N N   . PRO C 46  ? 2.9147 2.1948 2.4158 0.2481  -0.0336 -0.2188 76  PRO C N   
4973  C CA  . PRO C 46  ? 2.9983 2.2708 2.4805 0.2298  -0.0240 -0.2071 76  PRO C CA  
4974  C C   . PRO C 46  ? 3.0423 2.3197 2.5197 0.2314  -0.0150 -0.1976 76  PRO C C   
4975  O O   . PRO C 46  ? 3.0754 2.3349 2.5432 0.2483  -0.0183 -0.2004 76  PRO C O   
4976  C CB  . PRO C 46  ? 3.0647 2.2863 2.5063 0.2302  -0.0316 -0.2136 76  PRO C CB  
4977  C CG  . PRO C 46  ? 3.0150 2.2332 2.4665 0.2437  -0.0452 -0.2300 76  PRO C CG  
4978  C CD  . PRO C 46  ? 2.9257 2.1713 2.4061 0.2590  -0.0461 -0.2340 76  PRO C CD  
4979  N N   . THR C 47  ? 3.0380 2.3427 2.5231 0.2137  -0.0038 -0.1880 77  THR C N   
4980  C CA  . THR C 47  ? 3.0446 2.3634 2.5288 0.2129  0.0048  -0.1815 77  THR C CA  
4981  C C   . THR C 47  ? 3.1266 2.4029 2.5675 0.2100  0.0070  -0.1805 77  THR C C   
4982  O O   . THR C 47  ? 3.2159 2.4571 2.6232 0.1979  0.0062  -0.1808 77  THR C O   
4983  C CB  . THR C 47  ? 3.0079 2.3685 2.5091 0.1938  0.0155  -0.1752 77  THR C CB  
4984  O OG1 . THR C 47  ? 2.9379 2.3318 2.4745 0.1950  0.0120  -0.1759 77  THR C OG1 
4985  C CG2 . THR C 47  ? 2.9139 2.2995 2.4217 0.1957  0.0226  -0.1724 77  THR C CG2 
4986  N N   . ASP C 48  ? 3.1438 2.4213 2.5837 0.2210  0.0089  -0.1793 78  ASP C N   
4987  C CA  . ASP C 48  ? 3.2669 2.5067 2.6660 0.2173  0.0114  -0.1780 78  ASP C CA  
4988  C C   . ASP C 48  ? 3.3200 2.5613 2.6946 0.1879  0.0228  -0.1730 78  ASP C C   
4989  O O   . ASP C 48  ? 3.2700 2.5589 2.6675 0.1761  0.0327  -0.1704 78  ASP C O   
4990  C CB  . ASP C 48  ? 3.2267 2.4822 2.6384 0.2317  0.0134  -0.1773 78  ASP C CB  
4991  C CG  . ASP C 48  ? 3.2320 2.4406 2.6017 0.2339  0.0124  -0.1776 78  ASP C CG  
4992  O OD1 . ASP C 48  ? 3.2992 2.4753 2.6273 0.2141  0.0157  -0.1755 78  ASP C OD1 
4993  O OD2 . ASP C 48  ? 3.1667 2.3693 2.5429 0.2549  0.0080  -0.1800 78  ASP C OD2 
4994  N N   . PRO C 49  ? 3.2790 2.4691 2.6053 0.1754  0.0209  -0.1728 79  PRO C N   
4995  C CA  . PRO C 49  ? 3.3010 2.4891 2.5978 0.1439  0.0323  -0.1685 79  PRO C CA  
4996  C C   . PRO C 49  ? 3.3140 2.5336 2.6101 0.1298  0.0456  -0.1667 79  PRO C C   
4997  O O   . PRO C 49  ? 3.3000 2.5535 2.5997 0.1065  0.0575  -0.1659 79  PRO C O   
4998  C CB  . PRO C 49  ? 3.3710 2.4849 2.6077 0.1388  0.0239  -0.1693 79  PRO C CB  
4999  C CG  . PRO C 49  ? 3.3330 2.4232 2.5803 0.1658  0.0075  -0.1758 79  PRO C CG  
5000  C CD  . PRO C 49  ? 3.3014 2.4323 2.5967 0.1896  0.0066  -0.1780 79  PRO C CD  
5001  N N   . ASN C 50  ? 3.2829 2.4959 2.5755 0.1427  0.0441  -0.1677 80  ASN C N   
5002  C CA  . ASN C 50  ? 3.2494 2.4959 2.5434 0.1302  0.0556  -0.1685 80  ASN C CA  
5003  C C   . ASN C 50  ? 3.1104 2.3990 2.4526 0.1561  0.0526  -0.1706 80  ASN C C   
5004  O O   . ASN C 50  ? 3.0841 2.3535 2.4194 0.1715  0.0483  -0.1712 80  ASN C O   
5005  C CB  . ASN C 50  ? 3.3650 2.5614 2.6021 0.1164  0.0572  -0.1677 80  ASN C CB  
5006  C CG  . ASN C 50  ? 3.5274 2.6763 2.7084 0.0879  0.0595  -0.1653 80  ASN C CG  
5007  O OD1 . ASN C 50  ? 3.5866 2.7125 2.7625 0.0896  0.0528  -0.1641 80  ASN C OD1 
5008  N ND2 . ASN C 50  ? 3.6075 2.7418 2.7445 0.0602  0.0687  -0.1654 80  ASN C ND2 
5009  N N   . PRO C 51  ? 3.0690 2.4125 2.4584 0.1619  0.0539  -0.1720 81  PRO C N   
5010  C CA  . PRO C 51  ? 2.9583 2.3381 2.3900 0.1865  0.0492  -0.1740 81  PRO C CA  
5011  C C   . PRO C 51  ? 2.9140 2.3179 2.3438 0.1821  0.0560  -0.1775 81  PRO C C   
5012  O O   . PRO C 51  ? 2.9729 2.3908 2.3832 0.1565  0.0668  -0.1804 81  PRO C O   
5013  C CB  . PRO C 51  ? 2.9312 2.3606 2.4035 0.1867  0.0492  -0.1751 81  PRO C CB  
5014  C CG  . PRO C 51  ? 2.9997 2.4091 2.4545 0.1689  0.0513  -0.1726 81  PRO C CG  
5015  C CD  . PRO C 51  ? 3.1047 2.4758 2.5087 0.1470  0.0583  -0.1717 81  PRO C CD  
5016  N N   . GLN C 52  ? 2.9330 2.3436 2.3832 0.2062  0.0499  -0.1784 82  GLN C N   
5017  C CA  . GLN C 52  ? 2.8814 2.3172 2.3345 0.2055  0.0548  -0.1827 82  GLN C CA  
5018  C C   . GLN C 52  ? 2.7028 2.1971 2.2056 0.2232  0.0508  -0.1873 82  GLN C C   
5019  O O   . GLN C 52  ? 2.6136 2.1083 2.1427 0.2467  0.0409  -0.1849 82  GLN C O   
5020  C CB  . GLN C 52  ? 2.9232 2.3139 2.3526 0.2181  0.0509  -0.1803 82  GLN C CB  
5021  C CG  . GLN C 52  ? 3.0694 2.3984 2.4419 0.1998  0.0531  -0.1773 82  GLN C CG  
5022  C CD  . GLN C 52  ? 3.0911 2.4302 2.4330 0.1656  0.0655  -0.1801 82  GLN C CD  
5023  O OE1 . GLN C 52  ? 3.0078 2.3998 2.3706 0.1588  0.0725  -0.1863 82  GLN C OE1 
5024  N NE2 . GLN C 52  ? 3.1474 2.4360 2.4378 0.1433  0.0677  -0.1772 82  GLN C NE2 
5025  N N   . GLU C 53  ? 2.5304 2.0732 2.0433 0.2111  0.0577  -0.1953 83  GLU C N   
5026  C CA  . GLU C 53  ? 2.4349 2.0348 1.9914 0.2276  0.0523  -0.2025 83  GLU C CA  
5027  C C   . GLU C 53  ? 2.4094 2.0296 1.9634 0.2261  0.0564  -0.2097 83  GLU C C   
5028  O O   . GLU C 53  ? 2.4431 2.0818 1.9782 0.2003  0.0673  -0.2170 83  GLU C O   
5029  C CB  . GLU C 53  ? 2.4474 2.0965 2.0246 0.2169  0.0543  -0.2096 83  GLU C CB  
5030  C CG  . GLU C 53  ? 2.5509 2.2327 2.1124 0.1862  0.0677  -0.2198 83  GLU C CG  
5031  C CD  . GLU C 53  ? 2.6290 2.3630 2.2171 0.1820  0.0675  -0.2285 83  GLU C CD  
5032  O OE1 . GLU C 53  ? 2.6018 2.3286 2.2070 0.1943  0.0594  -0.2224 83  GLU C OE1 
5033  O OE2 . GLU C 53  ? 2.6541 2.4376 2.2454 0.1660  0.0751  -0.2429 83  GLU C OE2 
5034  N N   . ILE C 54  ? 2.3664 1.9818 1.9371 0.2519  0.0484  -0.2078 84  ILE C N   
5035  C CA  . ILE C 54  ? 2.3613 1.9939 1.9319 0.2531  0.0513  -0.2139 84  ILE C CA  
5036  C C   . ILE C 54  ? 2.3125 2.0131 1.9255 0.2650  0.0456  -0.2260 84  ILE C C   
5037  O O   . ILE C 54  ? 2.2635 1.9740 1.9070 0.2917  0.0332  -0.2244 84  ILE C O   
5038  C CB  . ILE C 54  ? 2.3441 1.9342 1.9099 0.2756  0.0455  -0.2059 84  ILE C CB  
5039  C CG1 . ILE C 54  ? 2.4035 1.9261 1.9233 0.2640  0.0495  -0.1973 84  ILE C CG1 
5040  C CG2 . ILE C 54  ? 2.3252 1.9403 1.8999 0.2811  0.0470  -0.2123 84  ILE C CG2 
5041  C CD1 . ILE C 54  ? 2.3856 1.8641 1.9034 0.2898  0.0415  -0.1904 84  ILE C CD1 
5042  N N   . HIS C 55  ? 2.3997 2.1466 2.0121 0.2447  0.0536  -0.2396 85  HIS C N   
5043  C CA  . HIS C 55  ? 2.3609 2.1770 2.0120 0.2556  0.0471  -0.2554 85  HIS C CA  
5044  C C   . HIS C 55  ? 2.3218 2.1501 1.9905 0.2764  0.0409  -0.2586 85  HIS C C   
5045  O O   . HIS C 55  ? 2.3382 2.1669 1.9896 0.2623  0.0496  -0.2624 85  HIS C O   
5046  C CB  . HIS C 55  ? 2.3946 2.2583 2.0370 0.2245  0.0588  -0.2718 85  HIS C CB  
5047  C CG  . HIS C 55  ? 2.4265 2.3667 2.1069 0.2343  0.0518  -0.2929 85  HIS C CG  
5048  N ND1 . HIS C 55  ? 2.4126 2.3775 2.1277 0.2599  0.0364  -0.2964 85  HIS C ND1 
5049  C CD2 . HIS C 55  ? 2.4360 2.4341 2.1232 0.2212  0.0569  -0.3136 85  HIS C CD2 
5050  C CE1 . HIS C 55  ? 2.3947 2.4276 2.1368 0.2653  0.0308  -0.3185 85  HIS C CE1 
5051  N NE2 . HIS C 55  ? 2.4311 2.4888 2.1591 0.2420  0.0434  -0.3303 85  HIS C NE2 
5052  N N   . LEU C 56  ? 2.1607 1.9970 1.8617 0.3088  0.0256  -0.2568 86  LEU C N   
5053  C CA  . LEU C 56  ? 2.1177 1.9646 1.8390 0.3328  0.0176  -0.2588 86  LEU C CA  
5054  C C   . LEU C 56  ? 2.1005 2.0195 1.8489 0.3343  0.0139  -0.2800 86  LEU C C   
5055  O O   . LEU C 56  ? 2.0783 2.0360 1.8568 0.3524  0.0001  -0.2899 86  LEU C O   
5056  C CB  . LEU C 56  ? 2.0781 1.9013 1.8182 0.3648  0.0024  -0.2487 86  LEU C CB  
5057  C CG  . LEU C 56  ? 2.0908 1.8518 1.8095 0.3650  0.0038  -0.2318 86  LEU C CG  
5058  C CD1 . LEU C 56  ? 2.0491 1.7920 1.7853 0.3948  -0.0106 -0.2245 86  LEU C CD1 
5059  C CD2 . LEU C 56  ? 2.1200 1.8338 1.8043 0.3517  0.0160  -0.2234 86  LEU C CD2 
5060  N N   . GLU C 57  ? 2.3255 2.2625 2.0612 0.3146  0.0254  -0.2885 87  GLU C N   
5061  C CA  . GLU C 57  ? 2.2306 2.2406 1.9907 0.3126  0.0233  -0.3118 87  GLU C CA  
5062  C C   . GLU C 57  ? 2.1382 2.1688 1.9348 0.3490  0.0064  -0.3153 87  GLU C C   
5063  O O   . GLU C 57  ? 2.0901 2.0760 1.8851 0.3682  0.0025  -0.2993 87  GLU C O   
5064  C CB  . GLU C 57  ? 2.2034 2.2202 1.9367 0.2808  0.0400  -0.3184 87  GLU C CB  
5065  C CG  . GLU C 57  ? 2.1969 2.2961 1.9502 0.2687  0.0413  -0.3468 87  GLU C CG  
5066  C CD  . GLU C 57  ? 2.2577 2.4032 2.0144 0.2513  0.0438  -0.3638 87  GLU C CD  
5067  O OE1 . GLU C 57  ? 2.3589 2.4672 2.0916 0.2372  0.0504  -0.3519 87  GLU C OE1 
5068  O OE2 . GLU C 57  ? 2.2438 2.4651 2.0280 0.2522  0.0389  -0.3904 87  GLU C OE2 
5069  N N   . ASN C 58  ? 2.4326 2.5323 2.2616 0.3589  -0.0042 -0.3379 88  ASN C N   
5070  C CA  . ASN C 58  ? 2.3654 2.4942 2.2300 0.3930  -0.0225 -0.3459 88  ASN C CA  
5071  C C   . ASN C 58  ? 2.3601 2.4507 2.2359 0.4260  -0.0403 -0.3310 88  ASN C C   
5072  O O   . ASN C 58  ? 2.3121 2.4154 2.2123 0.4552  -0.0563 -0.3344 88  ASN C O   
5073  C CB  . ASN C 58  ? 2.3645 2.4889 2.2285 0.3939  -0.0163 -0.3434 88  ASN C CB  
5074  C CG  . ASN C 58  ? 2.3415 2.5263 2.2069 0.3681  -0.0057 -0.3663 88  ASN C CG  
5075  O OD1 . ASN C 58  ? 2.4234 2.6707 2.3035 0.3596  -0.0086 -0.3901 88  ASN C OD1 
5076  N ND2 . ASN C 58  ? 2.2957 2.4628 2.1448 0.3550  0.0065  -0.3605 88  ASN C ND2 
5077  N N   . VAL C 59  ? 2.3036 2.3475 2.1607 0.4212  -0.0382 -0.3152 89  VAL C N   
5078  C CA  . VAL C 59  ? 2.2634 2.2661 2.1249 0.4470  -0.0531 -0.3004 89  VAL C CA  
5079  C C   . VAL C 59  ? 2.2228 2.2527 2.0995 0.4572  -0.0697 -0.3110 89  VAL C C   
5080  O O   . VAL C 59  ? 2.2401 2.2865 2.1096 0.4374  -0.0630 -0.3174 89  VAL C O   
5081  C CB  . VAL C 59  ? 2.2508 2.1845 2.0822 0.4361  -0.0419 -0.2776 89  VAL C CB  
5082  C CG1 . VAL C 59  ? 2.1890 2.0863 2.0239 0.4585  -0.0568 -0.2654 89  VAL C CG1 
5083  C CG2 . VAL C 59  ? 2.2280 2.1302 2.0429 0.4307  -0.0289 -0.2680 89  VAL C CG2 
5084  N N   . THR C 60  ? 2.1865 2.2193 2.0821 0.4882  -0.0919 -0.3133 90  THR C N   
5085  C CA  . THR C 60  ? 2.2427 2.2917 2.1492 0.5026  -0.1122 -0.3223 90  THR C CA  
5086  C C   . THR C 60  ? 2.2380 2.2294 2.1349 0.5206  -0.1256 -0.3034 90  THR C C   
5087  O O   . THR C 60  ? 2.1918 2.1691 2.0955 0.5440  -0.1384 -0.2997 90  THR C O   
5088  C CB  . THR C 60  ? 2.2370 2.3478 2.1722 0.5233  -0.1310 -0.3478 90  THR C CB  
5089  O OG1 . THR C 60  ? 2.2424 2.4118 2.1857 0.5032  -0.1175 -0.3681 90  THR C OG1 
5090  C CG2 . THR C 60  ? 2.2439 2.3667 2.1864 0.5396  -0.1541 -0.3580 90  THR C CG2 
5091  N N   . GLU C 61  ? 2.1666 2.1259 2.0466 0.5081  -0.1223 -0.2924 91  GLU C N   
5092  C CA  . GLU C 61  ? 2.1607 2.0657 2.0275 0.5185  -0.1327 -0.2754 91  GLU C CA  
5093  C C   . GLU C 61  ? 2.1872 2.0956 2.0545 0.5250  -0.1516 -0.2807 91  GLU C C   
5094  O O   . GLU C 61  ? 2.2139 2.1497 2.0832 0.5107  -0.1473 -0.2899 91  GLU C O   
5095  C CB  . GLU C 61  ? 2.1581 2.0154 2.0020 0.4978  -0.1131 -0.2568 91  GLU C CB  
5096  C CG  . GLU C 61  ? 2.1451 1.9486 1.9750 0.5068  -0.1216 -0.2410 91  GLU C CG  
5097  C CD  . GLU C 61  ? 2.1117 1.8936 1.9424 0.5253  -0.1250 -0.2348 91  GLU C CD  
5098  O OE1 . GLU C 61  ? 2.0952 1.9016 1.9379 0.5312  -0.1199 -0.2411 91  GLU C OE1 
5099  O OE2 . GLU C 61  ? 2.1013 1.8429 1.9199 0.5326  -0.1323 -0.2242 91  GLU C OE2 
5100  N N   . GLU C 62  ? 2.1743 2.0524 2.0369 0.5456  -0.1725 -0.2749 92  GLU C N   
5101  C CA  . GLU C 62  ? 2.2016 2.0737 2.0594 0.5536  -0.1940 -0.2788 92  GLU C CA  
5102  C C   . GLU C 62  ? 2.2038 2.0304 2.0398 0.5351  -0.1867 -0.2619 92  GLU C C   
5103  O O   . GLU C 62  ? 2.1826 1.9646 2.0037 0.5316  -0.1806 -0.2458 92  GLU C O   
5104  C CB  . GLU C 62  ? 2.2041 2.0610 2.0612 0.5830  -0.2226 -0.2813 92  GLU C CB  
5105  C CG  . GLU C 62  ? 2.2029 2.1066 2.0835 0.6047  -0.2342 -0.3001 92  GLU C CG  
5106  C CD  . GLU C 62  ? 2.2899 2.1737 2.1662 0.6347  -0.2652 -0.3025 92  GLU C CD  
5107  O OE1 . GLU C 62  ? 2.3324 2.1678 2.1852 0.6370  -0.2794 -0.2913 92  GLU C OE1 
5108  O OE2 . GLU C 62  ? 2.3719 2.2875 2.2666 0.6549  -0.2759 -0.3160 92  GLU C OE2 
5109  N N   . PHE C 63  ? 2.0809 1.9219 1.9162 0.5233  -0.1874 -0.2672 93  PHE C N   
5110  C CA  . PHE C 63  ? 2.0807 1.8857 1.8982 0.5053  -0.1822 -0.2538 93  PHE C CA  
5111  C C   . PHE C 63  ? 2.0987 1.8841 1.9062 0.5173  -0.2089 -0.2548 93  PHE C C   
5112  O O   . PHE C 63  ? 2.1213 1.9260 1.9360 0.5391  -0.2316 -0.2683 93  PHE C O   
5113  C CB  . PHE C 63  ? 2.0919 1.9237 1.9133 0.4808  -0.1625 -0.2577 93  PHE C CB  
5114  C CG  . PHE C 63  ? 2.0827 1.9124 1.9012 0.4626  -0.1358 -0.2511 93  PHE C CG  
5115  C CD1 . PHE C 63  ? 2.0879 1.9550 1.9184 0.4629  -0.1263 -0.2621 93  PHE C CD1 
5116  C CD2 . PHE C 63  ? 2.0724 1.8620 1.8742 0.4448  -0.1215 -0.2353 93  PHE C CD2 
5117  C CE1 . PHE C 63  ? 2.0853 1.9442 1.9074 0.4452  -0.1034 -0.2558 93  PHE C CE1 
5118  C CE2 . PHE C 63  ? 2.0727 1.8551 1.8676 0.4298  -0.0998 -0.2302 93  PHE C CE2 
5119  C CZ  . PHE C 63  ? 2.0807 1.8951 1.8840 0.4297  -0.0909 -0.2396 93  PHE C CZ  
5120  N N   . ASN C 64  ? 2.3704 2.1157 2.1590 0.5025  -0.2073 -0.2411 94  ASN C N   
5121  C CA  . ASN C 64  ? 2.4156 2.1361 2.1889 0.5091  -0.2320 -0.2406 94  ASN C CA  
5122  C C   . ASN C 64  ? 2.4077 2.1064 2.1684 0.4837  -0.2217 -0.2300 94  ASN C C   
5123  O O   . ASN C 64  ? 2.5531 2.2121 2.2973 0.4717  -0.2153 -0.2162 94  ASN C O   
5124  C CB  . ASN C 64  ? 2.4185 2.0962 2.1735 0.5249  -0.2507 -0.2334 94  ASN C CB  
5125  C CG  . ASN C 64  ? 2.4729 2.1284 2.2099 0.5373  -0.2823 -0.2372 94  ASN C CG  
5126  O OD1 . ASN C 64  ? 2.4563 2.1127 2.1881 0.5277  -0.2874 -0.2392 94  ASN C OD1 
5127  N ND2 . ASN C 64  ? 2.4742 2.1067 2.1991 0.5587  -0.3045 -0.2381 94  ASN C ND2 
5128  N N   . MET C 65  ? 2.2887 2.0168 2.0581 0.4757  -0.2202 -0.2384 95  MET C N   
5129  C CA  . MET C 65  ? 2.2801 1.9936 2.0409 0.4513  -0.2099 -0.2296 95  MET C CA  
5130  C C   . MET C 65  ? 2.3199 1.9881 2.0568 0.4502  -0.2299 -0.2214 95  MET C C   
5131  O O   . MET C 65  ? 2.3162 1.9623 2.0426 0.4285  -0.2209 -0.2111 95  MET C O   
5132  C CB  . MET C 65  ? 2.2914 2.0495 2.0675 0.4441  -0.2042 -0.2417 95  MET C CB  
5133  C CG  . MET C 65  ? 2.3340 2.1125 2.1140 0.4653  -0.2309 -0.2578 95  MET C CG  
5134  S SD  . MET C 65  ? 2.3314 2.1637 2.1283 0.4556  -0.2237 -0.2739 95  MET C SD  
5135  C CE  . MET C 65  ? 2.3117 2.1088 2.0940 0.4264  -0.2119 -0.2556 95  MET C CE  
5136  N N   . TRP C 66  ? 2.4736 2.1263 2.1995 0.4722  -0.2577 -0.2263 96  TRP C N   
5137  C CA  . TRP C 66  ? 2.4988 2.1044 2.1955 0.4699  -0.2794 -0.2192 96  TRP C CA  
5138  C C   . TRP C 66  ? 2.4459 2.0047 2.1202 0.4668  -0.2806 -0.2068 96  TRP C C   
5139  O O   . TRP C 66  ? 2.3913 1.9075 2.0373 0.4559  -0.2926 -0.1989 96  TRP C O   
5140  C CB  . TRP C 66  ? 2.5641 2.1717 2.2541 0.4950  -0.3123 -0.2323 96  TRP C CB  
5141  C CG  . TRP C 66  ? 2.5841 2.2431 2.2971 0.4998  -0.3117 -0.2484 96  TRP C CG  
5142  C CD1 . TRP C 66  ? 2.5760 2.2849 2.3131 0.5201  -0.3151 -0.2670 96  TRP C CD1 
5143  C CD2 . TRP C 66  ? 2.5686 2.2381 2.2834 0.4824  -0.3059 -0.2489 96  TRP C CD2 
5144  N NE1 . TRP C 66  ? 2.5651 2.3154 2.3175 0.5162  -0.3119 -0.2803 96  TRP C NE1 
5145  C CE2 . TRP C 66  ? 2.5453 2.2715 2.2846 0.4938  -0.3060 -0.2687 96  TRP C CE2 
5146  C CE3 . TRP C 66  ? 2.5342 2.1732 2.2327 0.4578  -0.3005 -0.2358 96  TRP C CE3 
5147  C CZ2 . TRP C 66  ? 2.4997 2.2514 2.2473 0.4820  -0.3002 -0.2749 96  TRP C CZ2 
5148  C CZ3 . TRP C 66  ? 2.5280 2.1915 2.2359 0.4466  -0.2954 -0.2410 96  TRP C CZ3 
5149  C CH2 . TRP C 66  ? 2.5186 2.2371 2.2504 0.4591  -0.2951 -0.2600 96  TRP C CH2 
5150  N N   . LYS C 67  ? 2.5608 2.1276 2.2460 0.4748  -0.2682 -0.2057 97  LYS C N   
5151  C CA  . LYS C 67  ? 2.5565 2.0861 2.2243 0.4721  -0.2653 -0.1958 97  LYS C CA  
5152  C C   . LYS C 67  ? 2.5202 2.0618 2.2023 0.4588  -0.2348 -0.1908 97  LYS C C   
5153  O O   . LYS C 67  ? 2.5558 2.0895 2.2384 0.4661  -0.2278 -0.1883 97  LYS C O   
5154  C CB  . LYS C 67  ? 2.5937 2.1138 2.2560 0.4988  -0.2847 -0.1998 97  LYS C CB  
5155  C CG  . LYS C 67  ? 2.6481 2.1478 2.2897 0.5132  -0.3186 -0.2051 97  LYS C CG  
5156  C CD  . LYS C 67  ? 2.7218 2.1715 2.3275 0.4913  -0.3263 -0.1947 97  LYS C CD  
5157  C CE  . LYS C 67  ? 2.7781 2.1967 2.3545 0.5015  -0.3614 -0.1983 97  LYS C CE  
5158  N NZ  . LYS C 67  ? 2.7812 2.2055 2.3596 0.5349  -0.3856 -0.2088 97  LYS C NZ  
5159  N N   . ASN C 68  ? 2.4650 2.0251 2.1580 0.4398  -0.2173 -0.1901 98  ASN C N   
5160  C CA  . ASN C 68  ? 2.4178 1.9854 2.1204 0.4262  -0.1904 -0.1862 98  ASN C CA  
5161  C C   . ASN C 68  ? 2.3983 1.9346 2.0835 0.4040  -0.1842 -0.1783 98  ASN C C   
5162  O O   . ASN C 68  ? 2.4028 1.9317 2.0796 0.3899  -0.1905 -0.1767 98  ASN C O   
5163  C CB  . ASN C 68  ? 2.4160 2.0237 2.1392 0.4188  -0.1751 -0.1917 98  ASN C CB  
5164  C CG  . ASN C 68  ? 2.3973 2.0063 2.1248 0.4045  -0.1498 -0.1876 98  ASN C CG  
5165  O OD1 . ASN C 68  ? 2.3908 1.9982 2.1165 0.3846  -0.1383 -0.1845 98  ASN C OD1 
5166  N ND2 . ASN C 68  ? 2.3909 2.0013 2.1226 0.4153  -0.1420 -0.1881 98  ASN C ND2 
5167  N N   . ASN C 69  ? 2.4310 1.9508 2.1109 0.4011  -0.1723 -0.1750 99  ASN C N   
5168  C CA  . ASN C 69  ? 2.3559 1.8490 2.0191 0.3815  -0.1677 -0.1711 99  ASN C CA  
5169  C C   . ASN C 69  ? 2.2891 1.7938 1.9612 0.3620  -0.1490 -0.1709 99  ASN C C   
5170  O O   . ASN C 69  ? 2.2967 1.7855 1.9576 0.3436  -0.1464 -0.1699 99  ASN C O   
5171  C CB  . ASN C 69  ? 2.4263 1.8988 2.0795 0.3882  -0.1644 -0.1708 99  ASN C CB  
5172  C CG  . ASN C 69  ? 2.3897 1.8359 2.0222 0.3689  -0.1639 -0.1704 99  ASN C CG  
5173  O OD1 . ASN C 69  ? 2.3259 1.7723 1.9606 0.3581  -0.1487 -0.1728 99  ASN C OD1 
5174  N ND2 . ASN C 69  ? 2.4202 1.8429 2.0300 0.3638  -0.1819 -0.1687 99  ASN C ND2 
5175  N N   . MET C 70  ? 2.3292 1.8609 2.0191 0.3644  -0.1365 -0.1727 100 MET C N   
5176  C CA  . MET C 70  ? 2.2877 1.8272 1.9827 0.3459  -0.1199 -0.1723 100 MET C CA  
5177  C C   . MET C 70  ? 2.3395 1.8816 2.0327 0.3285  -0.1252 -0.1709 100 MET C C   
5178  O O   . MET C 70  ? 2.2931 1.8318 1.9851 0.3100  -0.1156 -0.1700 100 MET C O   
5179  C CB  . MET C 70  ? 2.2554 1.8216 1.9647 0.3502  -0.1072 -0.1747 100 MET C CB  
5180  C CG  . MET C 70  ? 2.2558 1.8211 1.9671 0.3670  -0.1026 -0.1761 100 MET C CG  
5181  S SD  . MET C 70  ? 2.2626 1.8583 1.9855 0.3666  -0.0874 -0.1799 100 MET C SD  
5182  C CE  . MET C 70  ? 2.2161 1.7988 1.9299 0.3435  -0.0701 -0.1771 100 MET C CE  
5183  N N   . VAL C 71  ? 2.3651 1.9126 2.0576 0.3351  -0.1417 -0.1716 101 VAL C N   
5184  C CA  . VAL C 71  ? 2.3712 1.9193 2.0604 0.3201  -0.1490 -0.1704 101 VAL C CA  
5185  C C   . VAL C 71  ? 2.3638 1.8802 2.0327 0.3051  -0.1561 -0.1671 101 VAL C C   
5186  O O   . VAL C 71  ? 2.3205 1.8358 1.9882 0.2839  -0.1504 -0.1659 101 VAL C O   
5187  C CB  . VAL C 71  ? 2.4390 1.9994 2.1304 0.3346  -0.1673 -0.1741 101 VAL C CB  
5188  C CG1 . VAL C 71  ? 2.4703 2.0272 2.1554 0.3199  -0.1766 -0.1728 101 VAL C CG1 
5189  C CG2 . VAL C 71  ? 2.4278 2.0267 2.1401 0.3466  -0.1591 -0.1808 101 VAL C CG2 
5190  N N   . GLU C 72  ? 2.3590 1.8505 2.0109 0.3146  -0.1683 -0.1666 102 GLU C N   
5191  C CA  . GLU C 72  ? 2.3414 1.8026 1.9695 0.2986  -0.1756 -0.1653 102 GLU C CA  
5192  C C   . GLU C 72  ? 2.2539 1.7144 1.8839 0.2828  -0.1582 -0.1679 102 GLU C C   
5193  O O   . GLU C 72  ? 2.2667 1.7131 1.8821 0.2620  -0.1603 -0.1694 102 GLU C O   
5194  C CB  . GLU C 72  ? 2.4270 1.8629 2.0356 0.3135  -0.1904 -0.1650 102 GLU C CB  
5195  C CG  . GLU C 72  ? 2.5635 1.9970 2.1677 0.3331  -0.2115 -0.1646 102 GLU C CG  
5196  C CD  . GLU C 72  ? 2.6967 2.1166 2.2846 0.3219  -0.2292 -0.1630 102 GLU C CD  
5197  O OE1 . GLU C 72  ? 2.7727 2.1728 2.3421 0.2975  -0.2299 -0.1609 102 GLU C OE1 
5198  O OE2 . GLU C 72  ? 2.7390 2.1689 2.3318 0.3379  -0.2434 -0.1654 102 GLU C OE2 
5199  N N   . GLN C 73  ? 2.2721 1.7473 1.9181 0.2920  -0.1422 -0.1699 103 GLN C N   
5200  C CA  . GLN C 73  ? 2.2177 1.6922 1.8656 0.2807  -0.1273 -0.1745 103 GLN C CA  
5201  C C   . GLN C 73  ? 2.2006 1.6908 1.8597 0.2627  -0.1181 -0.1746 103 GLN C C   
5202  O O   . GLN C 73  ? 2.2417 1.7282 1.8967 0.2448  -0.1141 -0.1791 103 GLN C O   
5203  C CB  . GLN C 73  ? 2.1842 1.6625 1.8404 0.2986  -0.1161 -0.1765 103 GLN C CB  
5204  C CG  . GLN C 73  ? 2.2623 1.7250 1.9081 0.3148  -0.1223 -0.1778 103 GLN C CG  
5205  C CD  . GLN C 73  ? 2.2207 1.6865 1.8744 0.3309  -0.1104 -0.1801 103 GLN C CD  
5206  O OE1 . GLN C 73  ? 2.2538 1.7271 1.9151 0.3270  -0.0978 -0.1820 103 GLN C OE1 
5207  N NE2 . GLN C 73  ? 2.2944 1.7526 1.9444 0.3490  -0.1151 -0.1799 103 GLN C NE2 
5208  N N   . MET C 74  ? 1.9922 1.5024 1.6655 0.2668  -0.1147 -0.1710 104 MET C N   
5209  C CA  . MET C 74  ? 1.9837 1.5096 1.6673 0.2499  -0.1055 -0.1705 104 MET C CA  
5210  C C   . MET C 74  ? 1.9895 1.5115 1.6670 0.2305  -0.1148 -0.1695 104 MET C C   
5211  O O   . MET C 74  ? 1.9820 1.5086 1.6630 0.2116  -0.1079 -0.1714 104 MET C O   
5212  C CB  . MET C 74  ? 1.9798 1.5299 1.6776 0.2575  -0.1003 -0.1684 104 MET C CB  
5213  C CG  . MET C 74  ? 1.9722 1.5393 1.6796 0.2397  -0.0907 -0.1676 104 MET C CG  
5214  S SD  . MET C 74  ? 1.9695 1.5686 1.6908 0.2463  -0.0832 -0.1679 104 MET C SD  
5215  C CE  . MET C 74  ? 1.9609 1.5719 1.6885 0.2220  -0.0688 -0.1668 104 MET C CE  
5216  N N   . HIS C 75  ? 2.0789 1.5911 1.7458 0.2349  -0.1315 -0.1669 105 HIS C N   
5217  C CA  . HIS C 75  ? 2.1187 1.6229 1.7753 0.2155  -0.1420 -0.1654 105 HIS C CA  
5218  C C   . HIS C 75  ? 2.1080 1.5971 1.7514 0.1957  -0.1404 -0.1699 105 HIS C C   
5219  O O   . HIS C 75  ? 2.1128 1.6075 1.7579 0.1733  -0.1379 -0.1713 105 HIS C O   
5220  C CB  . HIS C 75  ? 2.2146 1.7025 1.8551 0.2261  -0.1632 -0.1626 105 HIS C CB  
5221  C CG  . HIS C 75  ? 2.3044 1.7801 1.9303 0.2072  -0.1763 -0.1604 105 HIS C CG  
5222  N ND1 . HIS C 75  ? 2.3440 1.8389 1.9833 0.1949  -0.1722 -0.1591 105 HIS C ND1 
5223  C CD2 . HIS C 75  ? 2.4204 1.8647 2.0168 0.1970  -0.1935 -0.1594 105 HIS C CD2 
5224  C CE1 . HIS C 75  ? 2.4440 1.9203 2.0641 0.1788  -0.1866 -0.1572 105 HIS C CE1 
5225  N NE2 . HIS C 75  ? 2.4888 1.9328 2.0809 0.1789  -0.2001 -0.1573 105 HIS C NE2 
5226  N N   . THR C 76  ? 2.1937 1.6666 1.8246 0.2032  -0.1416 -0.1738 106 THR C N   
5227  C CA  . THR C 76  ? 2.1793 1.6426 1.7976 0.1849  -0.1396 -0.1818 106 THR C CA  
5228  C C   . THR C 76  ? 2.1015 1.5824 1.7365 0.1783  -0.1232 -0.1892 106 THR C C   
5229  O O   . THR C 76  ? 2.1230 1.6048 1.7526 0.1594  -0.1213 -0.1986 106 THR C O   
5230  C CB  . THR C 76  ? 2.2315 1.6750 1.8320 0.1962  -0.1444 -0.1854 106 THR C CB  
5231  O OG1 . THR C 76  ? 2.3236 1.7738 1.9379 0.2219  -0.1362 -0.1845 106 THR C OG1 
5232  C CG2 . THR C 76  ? 2.3102 1.7294 1.8866 0.1983  -0.1636 -0.1795 106 THR C CG2 
5233  N N   . ASP C 77  ? 2.1582 1.6526 1.8112 0.1928  -0.1125 -0.1865 107 ASP C N   
5234  C CA  . ASP C 77  ? 2.1179 1.6235 1.7826 0.1882  -0.0991 -0.1929 107 ASP C CA  
5235  C C   . ASP C 77  ? 2.0842 1.6052 1.7594 0.1676  -0.0960 -0.1917 107 ASP C C   
5236  O O   . ASP C 77  ? 2.0866 1.6135 1.7647 0.1528  -0.0917 -0.2005 107 ASP C O   
5237  C CB  . ASP C 77  ? 2.2475 1.7561 1.9209 0.2091  -0.0897 -0.1898 107 ASP C CB  
5238  C CG  . ASP C 77  ? 2.3210 1.8154 1.9859 0.2272  -0.0893 -0.1947 107 ASP C CG  
5239  O OD1 . ASP C 77  ? 2.3526 1.8356 2.0050 0.2264  -0.0976 -0.1981 107 ASP C OD1 
5240  O OD2 . ASP C 77  ? 2.3719 1.8653 2.0406 0.2412  -0.0809 -0.1950 107 ASP C OD2 
5241  N N   . ILE C 78  ? 2.1938 1.7239 1.8760 0.1674  -0.0984 -0.1823 108 ILE C N   
5242  C CA  . ILE C 78  ? 2.1888 1.7350 1.8820 0.1484  -0.0949 -0.1805 108 ILE C CA  
5243  C C   . ILE C 78  ? 2.1823 1.7239 1.8662 0.1252  -0.1036 -0.1845 108 ILE C C   
5244  O O   . ILE C 78  ? 2.1792 1.7334 1.8714 0.1058  -0.0990 -0.1886 108 ILE C O   
5245  C CB  . ILE C 78  ? 2.1823 1.7410 1.8840 0.1547  -0.0964 -0.1716 108 ILE C CB  
5246  C CG1 . ILE C 78  ? 2.1627 1.7275 1.8705 0.1760  -0.0886 -0.1696 108 ILE C CG1 
5247  C CG2 . ILE C 78  ? 2.1057 1.6833 1.8205 0.1362  -0.0903 -0.1699 108 ILE C CG2 
5248  C CD1 . ILE C 78  ? 2.1177 1.6879 1.8319 0.1740  -0.0732 -0.1724 108 ILE C CD1 
5249  N N   . ILE C 79  ? 2.0787 1.6016 1.7433 0.1256  -0.1167 -0.1839 109 ILE C N   
5250  C CA  . ILE C 79  ? 2.1060 1.6210 1.7553 0.1004  -0.1255 -0.1883 109 ILE C CA  
5251  C C   . ILE C 79  ? 2.0874 1.6083 1.7363 0.0869  -0.1190 -0.2028 109 ILE C C   
5252  O O   . ILE C 79  ? 2.1563 1.6901 1.8098 0.0631  -0.1174 -0.2092 109 ILE C O   
5253  C CB  . ILE C 79  ? 2.1686 1.6562 1.7908 0.1042  -0.1419 -0.1847 109 ILE C CB  
5254  C CG1 . ILE C 79  ? 2.3300 1.8123 1.9505 0.1145  -0.1528 -0.1735 109 ILE C CG1 
5255  C CG2 . ILE C 79  ? 2.2645 1.7398 1.8638 0.0755  -0.1499 -0.1915 109 ILE C CG2 
5256  C CD1 . ILE C 79  ? 2.4363 1.8865 2.0261 0.1192  -0.1722 -0.1703 109 ILE C CD1 
5257  N N   . SER C 80  ? 2.1447 1.6592 1.7899 0.1026  -0.1150 -0.2100 110 SER C N   
5258  C CA  . SER C 80  ? 2.1363 1.6593 1.7814 0.0920  -0.1100 -0.2273 110 SER C CA  
5259  C C   . SER C 80  ? 2.1003 1.6439 1.7671 0.0887  -0.0998 -0.2329 110 SER C C   
5260  O O   . SER C 80  ? 2.0916 1.6487 1.7613 0.0718  -0.0986 -0.2480 110 SER C O   
5261  C CB  . SER C 80  ? 2.1495 1.6611 1.7857 0.1119  -0.1084 -0.2346 110 SER C CB  
5262  O OG  . SER C 80  ? 2.1331 1.6435 1.7815 0.1379  -0.1011 -0.2277 110 SER C OG  
5263  N N   . LEU C 81  ? 2.1745 1.7211 1.8549 0.1037  -0.0931 -0.2223 111 LEU C N   
5264  C CA  . LEU C 81  ? 2.1576 1.7192 1.8543 0.0995  -0.0843 -0.2258 111 LEU C CA  
5265  C C   . LEU C 81  ? 2.1447 1.7231 1.8499 0.0729  -0.0860 -0.2258 111 LEU C C   
5266  O O   . LEU C 81  ? 2.1056 1.6987 1.8204 0.0600  -0.0828 -0.2369 111 LEU C O   
5267  C CB  . LEU C 81  ? 2.1879 1.7473 1.8919 0.1177  -0.0768 -0.2136 111 LEU C CB  
5268  C CG  . LEU C 81  ? 2.2734 1.8329 1.9826 0.1255  -0.0678 -0.2184 111 LEU C CG  
5269  C CD1 . LEU C 81  ? 2.3027 1.8590 2.0133 0.1399  -0.0618 -0.2050 111 LEU C CD1 
5270  C CD2 . LEU C 81  ? 2.2512 1.8262 1.9716 0.1065  -0.0649 -0.2242 111 LEU C CD2 
5271  N N   . TRP C 82  ? 2.2651 1.8408 1.9661 0.0652  -0.0923 -0.2143 112 TRP C N   
5272  C CA  . TRP C 82  ? 2.2329 1.8220 1.9400 0.0399  -0.0949 -0.2125 112 TRP C CA  
5273  C C   . TRP C 82  ? 2.2504 1.8446 1.9493 0.0153  -0.1002 -0.2273 112 TRP C C   
5274  O O   . TRP C 82  ? 2.2661 1.8796 1.9766 -0.0060 -0.0981 -0.2332 112 TRP C O   
5275  C CB  . TRP C 82  ? 2.2862 1.8652 1.9848 0.0403  -0.1037 -0.1984 112 TRP C CB  
5276  C CG  . TRP C 82  ? 2.3229 1.9149 2.0302 0.0207  -0.1052 -0.1923 112 TRP C CG  
5277  C CD1 . TRP C 82  ? 2.3508 1.9381 2.0457 -0.0034 -0.1154 -0.1931 112 TRP C CD1 
5278  C CD2 . TRP C 82  ? 2.3127 1.9229 2.0402 0.0229  -0.0968 -0.1846 112 TRP C CD2 
5279  N NE1 . TRP C 82  ? 2.3293 1.9310 2.0372 -0.0151 -0.1140 -0.1863 112 TRP C NE1 
5280  C CE2 . TRP C 82  ? 2.3283 1.9457 2.0573 0.0010  -0.1023 -0.1813 112 TRP C CE2 
5281  C CE3 . TRP C 82  ? 2.2583 1.8791 2.0004 0.0392  -0.0850 -0.1807 112 TRP C CE3 
5282  C CZ2 . TRP C 82  ? 2.2997 1.9366 2.0470 -0.0031 -0.0957 -0.1746 112 TRP C CZ2 
5283  C CZ3 . TRP C 82  ? 2.2434 1.8833 2.0015 0.0332  -0.0782 -0.1744 112 TRP C CZ3 
5284  C CH2 . TRP C 82  ? 2.2669 1.9158 2.0288 0.0132  -0.0833 -0.1716 112 TRP C CH2 
5285  N N   . ASP C 83  ? 2.2063 1.7854 1.8846 0.0161  -0.1067 -0.2347 113 ASP C N   
5286  C CA  . ASP C 83  ? 2.2425 1.8291 1.9099 -0.0115 -0.1115 -0.2507 113 ASP C CA  
5287  C C   . ASP C 83  ? 2.2017 1.8110 1.8829 -0.0145 -0.1049 -0.2719 113 ASP C C   
5288  O O   . ASP C 83  ? 2.2151 1.8459 1.9026 -0.0400 -0.1056 -0.2846 113 ASP C O   
5289  C CB  . ASP C 83  ? 2.3185 1.8818 1.9565 -0.0110 -0.1200 -0.2530 113 ASP C CB  
5290  C CG  . ASP C 83  ? 2.4171 1.9547 2.0370 -0.0090 -0.1306 -0.2345 113 ASP C CG  
5291  O OD1 . ASP C 83  ? 2.4579 1.9959 2.0912 0.0042  -0.1295 -0.2198 113 ASP C OD1 
5292  O OD2 . ASP C 83  ? 2.5443 2.0601 2.1345 -0.0183 -0.1406 -0.2358 113 ASP C OD2 
5293  N N   . GLN C 84  ? 2.1576 1.7627 1.8429 0.0113  -0.0998 -0.2773 114 GLN C N   
5294  C CA  . GLN C 84  ? 2.1122 1.7358 1.8086 0.0121  -0.0962 -0.2992 114 GLN C CA  
5295  C C   . GLN C 84  ? 2.0838 1.7246 1.8025 0.0072  -0.0914 -0.2975 114 GLN C C   
5296  O O   . GLN C 84  ? 2.0680 1.7288 1.7967 -0.0003 -0.0915 -0.3172 114 GLN C O   
5297  C CB  . GLN C 84  ? 2.2398 1.8527 1.9307 0.0391  -0.0942 -0.3095 114 GLN C CB  
5298  C CG  . GLN C 84  ? 2.3374 1.9259 2.0224 0.0677  -0.0914 -0.2940 114 GLN C CG  
5299  C CD  . GLN C 84  ? 2.4955 2.0761 2.1679 0.0830  -0.0926 -0.3096 114 GLN C CD  
5300  O OE1 . GLN C 84  ? 2.5824 2.1639 2.2590 0.0992  -0.0903 -0.3227 114 GLN C OE1 
5301  N NE2 . GLN C 84  ? 2.5624 2.1353 2.2174 0.0762  -0.0972 -0.3105 114 GLN C NE2 
5302  N N   . SER C 85  ? 2.1673 1.8018 1.8937 0.0124  -0.0874 -0.2760 115 SER C N   
5303  C CA  . SER C 85  ? 2.1095 1.7587 1.8552 0.0081  -0.0816 -0.2731 115 SER C CA  
5304  C C   . SER C 85  ? 2.1505 1.8234 1.9064 -0.0231 -0.0842 -0.2777 115 SER C C   
5305  O O   . SER C 85  ? 2.1085 1.7983 1.8819 -0.0305 -0.0801 -0.2794 115 SER C O   
5306  C CB  . SER C 85  ? 2.1165 1.7547 1.8659 0.0223  -0.0754 -0.2505 115 SER C CB  
5307  O OG  . SER C 85  ? 2.0825 1.7341 1.8480 0.0164  -0.0688 -0.2471 115 SER C OG  
5308  N N   . LEU C 86  ? 2.0120 1.6845 1.7552 -0.0422 -0.0911 -0.2794 116 LEU C N   
5309  C CA  . LEU C 86  ? 2.0454 1.7375 1.7933 -0.0751 -0.0946 -0.2838 116 LEU C CA  
5310  C C   . LEU C 86  ? 2.1355 1.8447 1.8769 -0.0948 -0.0994 -0.3103 116 LEU C C   
5311  O O   . LEU C 86  ? 2.1962 1.9257 1.9408 -0.1255 -0.1024 -0.3184 116 LEU C O   
5312  C CB  . LEU C 86  ? 2.0523 1.7275 1.7851 -0.0856 -0.1004 -0.2655 116 LEU C CB  
5313  C CG  . LEU C 86  ? 2.0087 1.6762 1.7512 -0.0702 -0.0961 -0.2431 116 LEU C CG  
5314  C CD1 . LEU C 86  ? 2.0593 1.7107 1.7856 -0.0804 -0.1051 -0.2288 116 LEU C CD1 
5315  C CD2 . LEU C 86  ? 1.9604 1.6534 1.7299 -0.0772 -0.0876 -0.2431 116 LEU C CD2 
5316  N N   . LYS C 87  ? 2.0224 1.7265 1.7548 -0.0786 -0.1001 -0.3256 117 LYS C N   
5317  C CA  . LYS C 87  ? 2.0653 1.7912 1.7922 -0.0974 -0.1043 -0.3548 117 LYS C CA  
5318  C C   . LYS C 87  ? 1.9827 1.7438 1.7340 -0.1069 -0.1034 -0.3753 117 LYS C C   
5319  O O   . LYS C 87  ? 1.9982 1.7869 1.7521 -0.1384 -0.1067 -0.3920 117 LYS C O   
5320  C CB  . LYS C 87  ? 2.1068 1.8202 1.8179 -0.0769 -0.1052 -0.3677 117 LYS C CB  
5321  C CG  . LYS C 87  ? 2.1323 1.8750 1.8393 -0.0964 -0.1089 -0.4024 117 LYS C CG  
5322  C CD  . LYS C 87  ? 2.2201 1.9550 1.9121 -0.0773 -0.1095 -0.4188 117 LYS C CD  
5323  C CE  . LYS C 87  ? 2.2741 1.9787 1.9374 -0.0784 -0.1109 -0.4034 117 LYS C CE  
5324  N NZ  . LYS C 87  ? 2.2985 2.0104 1.9423 -0.1191 -0.1157 -0.4085 117 LYS C NZ  
5325  N N   . PRO C 88  ? 2.1177 1.8793 1.8855 -0.0834 -0.1000 -0.3760 118 PRO C N   
5326  C CA  . PRO C 88  ? 2.0333 1.8270 1.8228 -0.0922 -0.1015 -0.3968 118 PRO C CA  
5327  C C   . PRO C 88  ? 2.0455 1.8520 1.8538 -0.1094 -0.0981 -0.3817 118 PRO C C   
5328  O O   . PRO C 88  ? 2.0112 1.8393 1.8392 -0.1114 -0.0987 -0.3938 118 PRO C O   
5329  C CB  . PRO C 88  ? 1.9662 1.7446 1.7576 -0.0570 -0.1010 -0.4020 118 PRO C CB  
5330  C CG  . PRO C 88  ? 1.9528 1.6944 1.7334 -0.0360 -0.0950 -0.3713 118 PRO C CG  
5331  C CD  . PRO C 88  ? 2.0650 1.7967 1.8292 -0.0481 -0.0957 -0.3603 118 PRO C CD  
5332  N N   . CYS C 89  ? 2.1004 1.8932 1.9023 -0.1205 -0.0956 -0.3567 119 CYS C N   
5333  C CA  . CYS C 89  ? 2.0717 1.8761 1.8905 -0.1365 -0.0920 -0.3416 119 CYS C CA  
5334  C C   . CYS C 89  ? 2.0640 1.8970 1.8860 -0.1753 -0.0966 -0.3545 119 CYS C C   
5335  O O   . CYS C 89  ? 2.0820 1.9195 1.8874 -0.1911 -0.1021 -0.3705 119 CYS C O   
5336  C CB  . CYS C 89  ? 2.0879 1.8648 1.8986 -0.1268 -0.0880 -0.3103 119 CYS C CB  
5337  S SG  . CYS C 89  ? 2.2008 1.9551 2.0152 -0.0889 -0.0799 -0.2946 119 CYS C SG  
5338  N N   . VAL C 90  ? 2.0921 1.9446 1.9344 -0.1923 -0.0937 -0.3478 120 VAL C N   
5339  C CA  . VAL C 90  ? 2.0214 1.9032 1.8688 -0.2312 -0.0976 -0.3596 120 VAL C CA  
5340  C C   . VAL C 90  ? 2.1158 1.9754 1.9376 -0.2501 -0.1015 -0.3434 120 VAL C C   
5341  O O   . VAL C 90  ? 2.1539 1.9896 1.9714 -0.2409 -0.0995 -0.3170 120 VAL C O   
5342  C CB  . VAL C 90  ? 1.8171 1.7263 1.6948 -0.2427 -0.0933 -0.3568 120 VAL C CB  
5343  C CG1 . VAL C 90  ? 1.8006 1.7361 1.6815 -0.2846 -0.0969 -0.3638 120 VAL C CG1 
5344  C CG2 . VAL C 90  ? 1.6589 1.5907 1.5576 -0.2285 -0.0934 -0.3785 120 VAL C CG2 
5345  N N   . LYS C 91  ? 2.0798 1.9468 1.8823 -0.2769 -0.1081 -0.3609 121 LYS C N   
5346  C CA  . LYS C 91  ? 2.0686 1.9110 1.8397 -0.2997 -0.1145 -0.3486 121 LYS C CA  
5347  C C   . LYS C 91  ? 2.0137 1.8771 1.7936 -0.3368 -0.1161 -0.3470 121 LYS C C   
5348  O O   . LYS C 91  ? 1.9381 1.8421 1.7347 -0.3614 -0.1158 -0.3702 121 LYS C O   
5349  C CB  . LYS C 91  ? 2.0728 1.9083 1.8127 -0.3123 -0.1205 -0.3676 121 LYS C CB  
5350  C CG  . LYS C 91  ? 2.0990 1.9769 1.8514 -0.3240 -0.1199 -0.4040 121 LYS C CG  
5351  C CD  . LYS C 91  ? 2.0667 1.9326 1.7880 -0.3246 -0.1235 -0.4203 121 LYS C CD  
5352  C CE  . LYS C 91  ? 2.0957 2.0057 1.8304 -0.3295 -0.1232 -0.4600 121 LYS C CE  
5353  N NZ  . LYS C 91  ? 2.1055 2.0053 1.8106 -0.3273 -0.1253 -0.4765 121 LYS C NZ  
5354  N N   . LEU C 92  ? 1.9314 1.7682 1.7001 -0.3399 -0.1185 -0.3210 122 LEU C N   
5355  C CA  . LEU C 92  ? 1.9263 1.7767 1.7019 -0.3716 -0.1202 -0.3148 122 LEU C CA  
5356  C C   . LEU C 92  ? 1.9593 1.7932 1.6962 -0.4110 -0.1311 -0.3179 122 LEU C C   
5357  O O   . LEU C 92  ? 1.9740 1.7890 1.6980 -0.4261 -0.1365 -0.3006 122 LEU C O   
5358  C CB  . LEU C 92  ? 1.9221 1.7537 1.7081 -0.3501 -0.1170 -0.2861 122 LEU C CB  
5359  C CG  . LEU C 92  ? 1.8942 1.7380 1.7138 -0.3154 -0.1056 -0.2791 122 LEU C CG  
5360  C CD1 . LEU C 92  ? 1.8936 1.7226 1.7192 -0.3025 -0.1029 -0.2530 122 LEU C CD1 
5361  C CD2 . LEU C 92  ? 1.8609 1.7507 1.7156 -0.3257 -0.0990 -0.2979 122 LEU C CD2 
5362  N N   . THR C 93  ? 2.2011 2.0414 1.9166 -0.4300 -0.1349 -0.3410 123 THR C N   
5363  C CA  . THR C 93  ? 2.1963 2.0200 1.8697 -0.4724 -0.1451 -0.3458 123 THR C CA  
5364  C C   . THR C 93  ? 2.1739 2.0193 1.8524 -0.5154 -0.1473 -0.3478 123 THR C C   
5365  O O   . THR C 93  ? 2.1315 1.9406 1.7731 -0.5378 -0.1573 -0.3334 123 THR C O   
5366  C CB  . THR C 93  ? 2.1068 1.9410 1.7580 -0.4875 -0.1467 -0.3742 123 THR C CB  
5367  O OG1 . THR C 93  ? 2.2060 2.0321 1.8175 -0.5371 -0.1552 -0.3826 123 THR C OG1 
5368  C CG2 . THR C 93  ? 2.1058 1.9967 1.7957 -0.4836 -0.1386 -0.4044 123 THR C CG2 
5369  N N   . PRO C 94  ? 2.2327 2.1334 1.9534 -0.5286 -0.1399 -0.3646 124 PRO C N   
5370  C CA  . PRO C 94  ? 2.1300 2.0497 1.8524 -0.5723 -0.1427 -0.3661 124 PRO C CA  
5371  C C   . PRO C 94  ? 2.1166 2.0329 1.8632 -0.5634 -0.1398 -0.3406 124 PRO C C   
5372  O O   . PRO C 94  ? 2.1370 2.0934 1.9143 -0.5848 -0.1356 -0.3472 124 PRO C O   
5373  C CB  . PRO C 94  ? 2.1125 2.0978 1.8677 -0.5928 -0.1372 -0.4012 124 PRO C CB  
5374  C CG  . PRO C 94  ? 2.0941 2.0943 1.8792 -0.5474 -0.1302 -0.4099 124 PRO C CG  
5375  C CD  . PRO C 94  ? 2.2267 2.1724 1.9915 -0.5066 -0.1307 -0.3839 124 PRO C CD  
5376  N N   . LEU C 95  ? 1.9286 1.7989 1.6615 -0.5324 -0.1424 -0.3127 125 LEU C N   
5377  C CA  . LEU C 95  ? 1.9180 1.7814 1.6681 -0.5232 -0.1406 -0.2889 125 LEU C CA  
5378  C C   . LEU C 95  ? 1.9640 1.7769 1.6680 -0.5392 -0.1547 -0.2707 125 LEU C C   
5379  O O   . LEU C 95  ? 1.9630 1.7624 1.6738 -0.5284 -0.1558 -0.2504 125 LEU C O   
5380  C CB  . LEU C 95  ? 1.8958 1.7549 1.6740 -0.4737 -0.1316 -0.2725 125 LEU C CB  
5381  C CG  . LEU C 95  ? 1.8633 1.7495 1.6753 -0.4429 -0.1202 -0.2830 125 LEU C CG  
5382  C CD1 . LEU C 95  ? 1.8670 1.7241 1.6795 -0.4007 -0.1171 -0.2615 125 LEU C CD1 
5383  C CD2 . LEU C 95  ? 1.8214 1.7568 1.6788 -0.4510 -0.1105 -0.2914 125 LEU C CD2 
5384  N N   . CYS C 96  ? 2.1109 1.8936 1.7652 -0.5643 -0.1664 -0.2784 126 CYS C N   
5385  C CA  . CYS C 96  ? 2.1755 1.9016 1.7776 -0.5797 -0.1830 -0.2618 126 CYS C CA  
5386  C C   . CYS C 96  ? 2.1733 1.9100 1.7638 -0.6312 -0.1882 -0.2667 126 CYS C C   
5387  O O   . CYS C 96  ? 2.2693 1.9616 1.8051 -0.6608 -0.2037 -0.2623 126 CYS C O   
5388  C CB  . CYS C 96  ? 2.2974 1.9777 1.8442 -0.5824 -0.1944 -0.2658 126 CYS C CB  
5389  S SG  . CYS C 96  ? 2.2787 1.9327 1.8268 -0.5227 -0.1924 -0.2566 126 CYS C SG  
5390  N N   . VAL C 97  ? 2.2542 2.0488 1.8950 -0.6426 -0.1758 -0.2761 127 VAL C N   
5391  C CA  . VAL C 97  ? 2.3030 2.1183 1.9442 -0.6898 -0.1782 -0.2813 127 VAL C CA  
5392  C C   . VAL C 97  ? 2.3495 2.1298 1.9805 -0.6842 -0.1861 -0.2548 127 VAL C C   
5393  O O   . VAL C 97  ? 2.3266 2.0873 1.9696 -0.6405 -0.1849 -0.2358 127 VAL C O   
5394  C CB  . VAL C 97  ? 2.2136 2.1041 1.9171 -0.6962 -0.1624 -0.3000 127 VAL C CB  
5395  C CG1 . VAL C 97  ? 2.2301 2.1519 1.9332 -0.7522 -0.1644 -0.3141 127 VAL C CG1 
5396  C CG2 . VAL C 97  ? 2.1233 2.0445 1.8440 -0.6807 -0.1547 -0.3238 127 VAL C CG2 
5397  N N   . THR C 98  ? 2.4449 2.2168 2.0507 -0.7298 -0.1950 -0.2549 128 THR C N   
5398  C CA  . THR C 98  ? 2.4473 2.1879 2.0427 -0.7275 -0.2038 -0.2322 128 THR C CA  
5399  C C   . THR C 98  ? 2.3529 2.1381 2.0141 -0.6981 -0.1880 -0.2236 128 THR C C   
5400  O O   . THR C 98  ? 2.2936 2.1402 2.0034 -0.7106 -0.1735 -0.2373 128 THR C O   
5401  C CB  . THR C 98  ? 2.5523 2.2830 2.1128 -0.7862 -0.2146 -0.2368 128 THR C CB  
5402  O OG1 . THR C 98  ? 2.5466 2.3483 2.1511 -0.8184 -0.2007 -0.2576 128 THR C OG1 
5403  C CG2 . THR C 98  ? 2.6519 2.3289 2.1376 -0.8161 -0.2315 -0.2433 128 THR C CG2 
5404  N N   . LEU C 99  ? 2.1829 1.9377 1.8443 -0.6587 -0.1914 -0.2024 129 LEU C N   
5405  C CA  . LEU C 99  ? 2.2036 1.9946 1.9212 -0.6273 -0.1764 -0.1930 129 LEU C CA  
5406  C C   . LEU C 99  ? 2.2077 1.9904 1.9241 -0.6405 -0.1821 -0.1794 129 LEU C C   
5407  O O   . LEU C 99  ? 2.2414 1.9696 1.9157 -0.6320 -0.1992 -0.1657 129 LEU C O   
5408  C CB  . LEU C 99  ? 2.2871 2.0570 2.0085 -0.5727 -0.1743 -0.1819 129 LEU C CB  
5409  C CG  . LEU C 99  ? 2.2919 2.0585 2.0052 -0.5579 -0.1717 -0.1935 129 LEU C CG  
5410  C CD1 . LEU C 99  ? 2.3534 2.0992 2.0699 -0.5056 -0.1700 -0.1820 129 LEU C CD1 
5411  C CD2 . LEU C 99  ? 2.2517 2.0788 2.0097 -0.5690 -0.1549 -0.2126 129 LEU C CD2 
5412  N N   . GLN C 100 ? 2.2456 2.0819 2.0077 -0.6599 -0.1688 -0.1840 130 GLN C N   
5413  C CA  . GLN C 100 ? 2.2363 2.0748 2.0073 -0.6706 -0.1707 -0.1719 130 GLN C CA  
5414  C C   . GLN C 100 ? 2.2802 2.1368 2.0929 -0.6244 -0.1579 -0.1593 130 GLN C C   
5415  O O   . GLN C 100 ? 2.2256 2.1370 2.0927 -0.6199 -0.1389 -0.1628 130 GLN C O   
5416  C CB  . GLN C 100 ? 2.1605 2.0502 1.9605 -0.7164 -0.1625 -0.1841 130 GLN C CB  
5417  C CG  . GLN C 100 ? 2.1641 2.0454 1.9255 -0.7666 -0.1730 -0.2006 130 GLN C CG  
5418  C CD  . GLN C 100 ? 2.2617 2.0765 1.9551 -0.7912 -0.1959 -0.1904 130 GLN C CD  
5419  O OE1 . GLN C 100 ? 2.3275 2.1191 2.0139 -0.7849 -0.2028 -0.1742 130 GLN C OE1 
5420  N NE2 . GLN C 100 ? 2.3147 2.0964 1.9547 -0.8193 -0.2086 -0.2007 130 GLN C NE2 
5421  N N   . CYS C 101 ? 2.1791 1.9900 1.9648 -0.5898 -0.1686 -0.1461 131 CYS C N   
5422  C CA  . CYS C 101 ? 2.1498 1.9781 1.9705 -0.5450 -0.1563 -0.1371 131 CYS C CA  
5423  C C   . CYS C 101 ? 2.1487 1.9775 1.9773 -0.5427 -0.1587 -0.1259 131 CYS C C   
5424  O O   . CYS C 101 ? 2.1829 1.9829 1.9791 -0.5695 -0.1747 -0.1224 131 CYS C O   
5425  C CB  . CYS C 101 ? 2.1806 1.9684 1.9741 -0.5038 -0.1649 -0.1324 131 CYS C CB  
5426  S SG  . CYS C 101 ? 2.1811 1.9687 1.9660 -0.5046 -0.1616 -0.1456 131 CYS C SG  
5427  N N   . THR C 102 ? 2.2475 2.1093 2.1180 -0.5111 -0.1422 -0.1211 132 THR C N   
5428  C CA  . THR C 102 ? 2.2660 2.1346 2.1491 -0.5020 -0.1417 -0.1121 132 THR C CA  
5429  C C   . THR C 102 ? 2.2518 2.1345 2.1580 -0.4549 -0.1301 -0.1085 132 THR C C   
5430  O O   . THR C 102 ? 2.2415 2.1327 2.1579 -0.4339 -0.1206 -0.1121 132 THR C O   
5431  C CB  . THR C 102 ? 2.2363 2.1559 2.1620 -0.5322 -0.1265 -0.1135 132 THR C CB  
5432  O OG1 . THR C 102 ? 2.2781 2.2054 2.2170 -0.5194 -0.1247 -0.1052 132 THR C OG1 
5433  C CG2 . THR C 102 ? 1.9988 1.9743 1.9764 -0.5270 -0.1016 -0.1204 132 THR C CG2 
5434  N N   . ASN C 103 ? 2.6033 2.4893 2.5163 -0.4391 -0.1311 -0.1025 133 ASN C N   
5435  C CA  . ASN C 103 ? 2.5627 2.4673 2.4972 -0.3973 -0.1195 -0.1014 133 ASN C CA  
5436  C C   . ASN C 103 ? 2.4976 2.4600 2.4849 -0.3952 -0.0900 -0.1038 133 ASN C C   
5437  O O   . ASN C 103 ? 2.4655 2.4618 2.4816 -0.4239 -0.0780 -0.1051 133 ASN C O   
5438  C CB  . ASN C 103 ? 2.6172 2.5192 2.5496 -0.3816 -0.1263 -0.0978 133 ASN C CB  
5439  C CG  . ASN C 103 ? 2.6774 2.5174 2.5546 -0.3681 -0.1574 -0.0968 133 ASN C CG  
5440  O OD1 . ASN C 103 ? 2.6337 2.4345 2.4764 -0.3609 -0.1713 -0.0982 133 ASN C OD1 
5441  N ND2 . ASN C 103 ? 2.9121 2.7422 2.7798 -0.3622 -0.1691 -0.0951 133 ASN C ND2 
5442  N N   . VAL C 104 ? 2.4714 2.4436 2.4691 -0.3612 -0.0794 -0.1050 134 VAL C N   
5443  C CA  . VAL C 104 ? 2.4202 2.4400 2.4608 -0.3565 -0.0528 -0.1068 134 VAL C CA  
5444  C C   . VAL C 104 ? 2.4223 2.4817 2.4958 -0.3598 -0.0383 -0.1038 134 VAL C C   
5445  O O   . VAL C 104 ? 2.5245 2.5752 2.5878 -0.3523 -0.0477 -0.1015 134 VAL C O   
5446  C CB  . VAL C 104 ? 2.4329 2.4484 2.4697 -0.3211 -0.0463 -0.1090 134 VAL C CB  
5447  C CG1 . VAL C 104 ? 2.4573 2.4726 2.4889 -0.2915 -0.0487 -0.1084 134 VAL C CG1 
5448  C CG2 . VAL C 104 ? 2.3583 2.4111 2.4289 -0.3210 -0.0221 -0.1113 134 VAL C CG2 
5449  N N   . THR C 105 ? 2.6017 2.7042 2.7138 -0.3709 -0.0162 -0.1047 135 THR C N   
5450  C CA  . THR C 105 ? 2.5017 2.6461 2.6484 -0.3774 0.0003  -0.1021 135 THR C CA  
5451  C C   . THR C 105 ? 2.5506 2.7067 2.7010 -0.3450 0.0098  -0.1022 135 THR C C   
5452  O O   . THR C 105 ? 2.4431 2.6134 2.6029 -0.3280 0.0251  -0.1044 135 THR C O   
5453  C CB  . THR C 105 ? 2.2248 2.4090 2.4087 -0.3959 0.0202  -0.1039 135 THR C CB  
5454  O OG1 . THR C 105 ? 2.2055 2.3848 2.3867 -0.3811 0.0268  -0.1078 135 THR C OG1 
5455  C CG2 . THR C 105 ? 2.1041 2.2920 2.2933 -0.4330 0.0120  -0.1061 135 THR C CG2 
5456  N N   . ASN C 106 ? 2.6728 2.8229 2.8136 -0.3370 -0.0000 -0.1014 136 ASN C N   
5457  C CA  . ASN C 106 ? 2.6291 2.7965 2.7746 -0.3076 0.0077  -0.1051 136 ASN C CA  
5458  C C   . ASN C 106 ? 2.7201 2.8938 2.8679 -0.3120 0.0001  -0.1046 136 ASN C C   
5459  O O   . ASN C 106 ? 2.7510 2.9157 2.8975 -0.3390 -0.0091 -0.0999 136 ASN C O   
5460  C CB  . ASN C 106 ? 2.6811 2.8158 2.7940 -0.2757 -0.0068 -0.1102 136 ASN C CB  
5461  C CG  . ASN C 106 ? 2.8315 2.9155 2.9041 -0.2727 -0.0386 -0.1098 136 ASN C CG  
5462  O OD1 . ASN C 106 ? 2.8825 2.9457 2.9442 -0.2995 -0.0511 -0.1049 136 ASN C OD1 
5463  N ND2 . ASN C 106 ? 2.9264 2.9902 2.9749 -0.2407 -0.0527 -0.1161 136 ASN C ND2 
5464  N N   . ASN C 107 ? 2.7389 2.9287 2.8887 -0.2856 0.0033  -0.1109 137 ASN C N   
5465  C CA  . ASN C 107 ? 2.8176 3.0155 2.9698 -0.2851 -0.0038 -0.1126 137 ASN C CA  
5466  C C   . ASN C 107 ? 2.9602 3.1239 3.0762 -0.2536 -0.0295 -0.1208 137 ASN C C   
5467  O O   . ASN C 107 ? 3.0270 3.2148 3.1489 -0.2253 -0.0230 -0.1314 137 ASN C O   
5468  C CB  . ASN C 107 ? 2.6889 2.9479 2.8824 -0.2838 0.0258  -0.1157 137 ASN C CB  
5469  C CG  . ASN C 107 ? 2.8019 3.0744 2.9983 -0.2747 0.0200  -0.1212 137 ASN C CG  
5470  O OD1 . ASN C 107 ? 2.8562 3.1279 3.0591 -0.2962 0.0147  -0.1155 137 ASN C OD1 
5471  N ND2 . ASN C 107 ? 2.9240 3.2098 3.1148 -0.2422 0.0199  -0.1338 137 ASN C ND2 
5472  N N   . ILE C 108 ? 3.0434 3.1520 3.1210 -0.2601 -0.0592 -0.1172 138 ILE C N   
5473  C CA  . ILE C 108 ? 3.1162 3.1820 3.1529 -0.2335 -0.0902 -0.1242 138 ILE C CA  
5474  C C   . ILE C 108 ? 3.0756 3.1522 3.1099 -0.1950 -0.0865 -0.1356 138 ILE C C   
5475  O O   . ILE C 108 ? 2.9867 3.0868 3.0407 -0.1975 -0.0647 -0.1339 138 ILE C O   
5476  C CB  . ILE C 108 ? 3.0878 3.1630 3.1284 -0.2348 -0.0974 -0.1269 138 ILE C CB  
5477  C CG1 . ILE C 108 ? 2.9769 3.0532 3.0292 -0.2779 -0.0929 -0.1149 138 ILE C CG1 
5478  C CG2 . ILE C 108 ? 3.1324 3.1463 3.1225 -0.2245 -0.1362 -0.1293 138 ILE C CG2 
5479  C CD1 . ILE C 108 ? 2.8209 2.9620 2.9272 -0.2960 -0.0586 -0.1120 138 ILE C CD1 
5480  N N   . THR C 109 ? 3.1291 3.1858 3.1372 -0.1607 -0.1083 -0.1474 139 THR C N   
5481  C CA  . THR C 109 ? 3.2196 3.2323 3.1903 -0.1482 -0.1427 -0.1520 139 THR C CA  
5482  C C   . THR C 109 ? 3.2939 3.2337 3.2151 -0.1576 -0.1733 -0.1440 139 THR C C   
5483  O O   . THR C 109 ? 3.3068 3.2338 3.2261 -0.1782 -0.1661 -0.1343 139 THR C O   
5484  C CB  . THR C 109 ? 3.2899 3.3157 3.2541 -0.1038 -0.1533 -0.1716 139 THR C CB  
5485  O OG1 . THR C 109 ? 3.3288 3.3485 3.2845 -0.0843 -0.1531 -0.1761 139 THR C OG1 
5486  C CG2 . THR C 109 ? 3.2009 3.2988 3.2096 -0.0968 -0.1246 -0.1819 139 THR C CG2 
5487  N N   . ASP C 110 ? 3.3753 3.2661 3.2539 -0.1422 -0.2084 -0.1491 140 ASP C N   
5488  C CA  . ASP C 110 ? 3.4099 3.2256 3.2339 -0.1512 -0.2399 -0.1421 140 ASP C CA  
5489  C C   . ASP C 110 ? 3.5219 3.3139 3.3233 -0.1213 -0.2524 -0.1487 140 ASP C C   
5490  O O   . ASP C 110 ? 3.5934 3.3254 3.3508 -0.1291 -0.2751 -0.1426 140 ASP C O   
5491  C CB  . ASP C 110 ? 3.5159 3.2800 3.2963 -0.1492 -0.2751 -0.1440 140 ASP C CB  
5492  C CG  . ASP C 110 ? 3.5142 3.2095 3.2458 -0.1847 -0.2974 -0.1305 140 ASP C CG  
5493  O OD1 . ASP C 110 ? 3.4826 3.1562 3.2000 -0.1965 -0.2965 -0.1244 140 ASP C OD1 
5494  O OD2 . ASP C 110 ? 3.5896 3.2526 3.2953 -0.2020 -0.3158 -0.1269 140 ASP C OD2 
5495  N N   . ASP C 111 ? 3.4624 3.3006 3.2920 -0.0893 -0.2375 -0.1613 141 ASP C N   
5496  C CA  . ASP C 111 ? 3.4782 3.3005 3.2908 -0.0604 -0.2475 -0.1687 141 ASP C CA  
5497  C C   . ASP C 111 ? 3.3154 3.1627 3.1536 -0.0742 -0.2188 -0.1610 141 ASP C C   
5498  O O   . ASP C 111 ? 3.2703 3.1082 3.0987 -0.0540 -0.2226 -0.1654 141 ASP C O   
5499  C CB  . ASP C 111 ? 3.5602 3.4147 3.3823 -0.0165 -0.2526 -0.1902 141 ASP C CB  
5500  C CG  . ASP C 111 ? 3.6727 3.4960 3.4639 0.0019  -0.2864 -0.2005 141 ASP C CG  
5501  O OD1 . ASP C 111 ? 3.7511 3.5062 3.4960 -0.0108 -0.3160 -0.1914 141 ASP C OD1 
5502  O OD2 . ASP C 111 ? 3.6104 3.4757 3.4206 0.0290  -0.2845 -0.2189 141 ASP C OD2 
5503  N N   . MET C 112 ? 3.3787 3.2571 3.2490 -0.1076 -0.1914 -0.1504 150 MET C N   
5504  C CA  . MET C 112 ? 3.2730 3.1733 3.1666 -0.1219 -0.1654 -0.1437 150 MET C CA  
5505  C C   . MET C 112 ? 3.2478 3.0946 3.1077 -0.1399 -0.1808 -0.1342 150 MET C C   
5506  O O   . MET C 112 ? 3.1631 3.0182 3.0340 -0.1466 -0.1653 -0.1307 150 MET C O   
5507  C CB  . MET C 112 ? 3.1862 3.1348 3.1229 -0.1513 -0.1344 -0.1369 150 MET C CB  
5508  C CG  . MET C 112 ? 3.1370 3.1440 3.1100 -0.1389 -0.1138 -0.1456 150 MET C CG  
5509  S SD  . MET C 112 ? 3.1198 3.1684 3.1118 -0.1078 -0.0937 -0.1580 150 MET C SD  
5510  C CE  . MET C 112 ? 2.9005 2.9562 2.9099 -0.1334 -0.0687 -0.1458 150 MET C CE  
5511  N N   . ARG C 113 ? 3.1556 2.9469 2.9724 -0.1486 -0.2113 -0.1310 151 ARG C N   
5512  C CA  . ARG C 113 ? 3.1829 2.9167 2.9580 -0.1685 -0.2303 -0.1234 151 ARG C CA  
5513  C C   . ARG C 113 ? 3.0180 2.7708 2.8146 -0.1982 -0.2070 -0.1164 151 ARG C C   
5514  O O   . ARG C 113 ? 3.0412 2.7628 2.8140 -0.2021 -0.2144 -0.1145 151 ARG C O   
5515  C CB  . ARG C 113 ? 3.2096 2.9015 2.9476 -0.1367 -0.2537 -0.1290 151 ARG C CB  
5516  C CG  . ARG C 113 ? 3.1178 2.8495 2.8861 -0.1097 -0.2334 -0.1355 151 ARG C CG  
5517  C CD  . ARG C 113 ? 3.2071 2.9031 2.9437 -0.0792 -0.2542 -0.1413 151 ARG C CD  
5518  N NE  . ARG C 113 ? 3.1885 2.8375 2.8927 -0.0986 -0.2644 -0.1329 151 ARG C NE  
5519  C CZ  . ARG C 113 ? 3.2285 2.8541 2.9138 -0.0802 -0.2728 -0.1350 151 ARG C CZ  
5520  N NH1 . ARG C 113 ? 3.2679 2.9137 2.9645 -0.0423 -0.2727 -0.1453 151 ARG C NH1 
5521  N NH2 . ARG C 113 ? 3.1816 2.7661 2.8369 -0.1004 -0.2811 -0.1281 151 ARG C NH2 
5522  N N   . GLY C 114 ? 2.9108 2.7135 2.7508 -0.2191 -0.1804 -0.1136 152 GLY C N   
5523  C CA  . GLY C 114 ? 2.7602 2.5815 2.6205 -0.2470 -0.1609 -0.1094 152 GLY C CA  
5524  C C   . GLY C 114 ? 2.7423 2.5750 2.6131 -0.2270 -0.1480 -0.1125 152 GLY C C   
5525  O O   . GLY C 114 ? 2.6647 2.5436 2.5745 -0.2238 -0.1217 -0.1138 152 GLY C O   
5526  N N   . GLU C 115 ? 2.7832 2.5711 2.6165 -0.2140 -0.1672 -0.1137 153 GLU C N   
5527  C CA  . GLU C 115 ? 2.6725 2.4624 2.5087 -0.1957 -0.1589 -0.1163 153 GLU C CA  
5528  C C   . GLU C 115 ? 2.5045 2.3139 2.3612 -0.2211 -0.1398 -0.1147 153 GLU C C   
5529  O O   . GLU C 115 ? 2.4683 2.2520 2.3047 -0.2259 -0.1461 -0.1153 153 GLU C O   
5530  C CB  . GLU C 115 ? 2.6367 2.4636 2.4994 -0.1624 -0.1439 -0.1221 153 GLU C CB  
5531  C CG  . GLU C 115 ? 2.5340 2.3633 2.3996 -0.1455 -0.1343 -0.1246 153 GLU C CG  
5532  C CD  . GLU C 115 ? 2.6041 2.4673 2.4897 -0.1147 -0.1215 -0.1317 153 GLU C CD  
5533  O OE1 . GLU C 115 ? 2.7034 2.5844 2.5958 -0.1023 -0.1240 -0.1367 153 GLU C OE1 
5534  O OE2 . GLU C 115 ? 2.6241 2.4971 2.5176 -0.1038 -0.1087 -0.1334 153 GLU C OE2 
5535  N N   . LEU C 116 ? 2.3255 2.1812 2.2223 -0.2361 -0.1169 -0.1139 154 LEU C N   
5536  C CA  . LEU C 116 ? 2.1685 2.0459 2.0870 -0.2596 -0.1004 -0.1145 154 LEU C CA  
5537  C C   . LEU C 116 ? 2.2130 2.0868 2.1276 -0.2984 -0.1072 -0.1129 154 LEU C C   
5538  O O   . LEU C 116 ? 2.2765 2.1618 2.1998 -0.3083 -0.1081 -0.1099 154 LEU C O   
5539  C CB  . LEU C 116 ? 2.0501 1.9779 2.0118 -0.2527 -0.0730 -0.1153 154 LEU C CB  
5540  C CG  . LEU C 116 ? 2.0604 1.9921 2.0231 -0.2187 -0.0652 -0.1180 154 LEU C CG  
5541  C CD1 . LEU C 116 ? 2.0044 1.9822 2.0028 -0.2133 -0.0392 -0.1188 154 LEU C CD1 
5542  C CD2 . LEU C 116 ? 2.0691 1.9793 2.0174 -0.2154 -0.0675 -0.1203 154 LEU C CD2 
5543  N N   . LYS C 117 ? 2.0945 1.9540 1.9955 -0.3211 -0.1119 -0.1162 155 LYS C N   
5544  C CA  . LYS C 117 ? 2.1030 1.9595 1.9966 -0.3617 -0.1190 -0.1172 155 LYS C CA  
5545  C C   . LYS C 117 ? 2.0052 1.9024 1.9324 -0.3855 -0.1015 -0.1242 155 LYS C C   
5546  O O   . LYS C 117 ? 1.9815 1.8843 1.9145 -0.3763 -0.0943 -0.1303 155 LYS C O   
5547  C CB  . LYS C 117 ? 2.1865 1.9876 2.0264 -0.3730 -0.1445 -0.1176 155 LYS C CB  
5548  C CG  . LYS C 117 ? 2.2678 2.0339 2.0786 -0.3572 -0.1638 -0.1110 155 LYS C CG  
5549  C CD  . LYS C 117 ? 2.3792 2.1138 2.1564 -0.3898 -0.1832 -0.1082 155 LYS C CD  
5550  C CE  . LYS C 117 ? 2.5225 2.2163 2.2668 -0.3659 -0.2053 -0.1034 155 LYS C CE  
5551  N NZ  . LYS C 117 ? 2.6536 2.3050 2.3554 -0.3949 -0.2285 -0.0999 155 LYS C NZ  
5552  N N   . ASN C 118 ? 2.2365 2.1618 2.1854 -0.4153 -0.0960 -0.1245 156 ASN C N   
5553  C CA  . ASN C 118 ? 2.1504 2.1176 2.1326 -0.4406 -0.0821 -0.1333 156 ASN C CA  
5554  C C   . ASN C 118 ? 2.1936 2.1491 2.1530 -0.4793 -0.0949 -0.1423 156 ASN C C   
5555  O O   . ASN C 118 ? 2.2360 2.1974 2.1937 -0.5116 -0.1002 -0.1421 156 ASN C O   
5556  C CB  . ASN C 118 ? 2.0725 2.0826 2.0950 -0.4507 -0.0675 -0.1294 156 ASN C CB  
5557  C CG  . ASN C 118 ? 1.9783 2.0352 2.0402 -0.4690 -0.0521 -0.1388 156 ASN C CG  
5558  O OD1 . ASN C 118 ? 1.9814 2.0404 2.0423 -0.4697 -0.0515 -0.1493 156 ASN C OD1 
5559  N ND2 . ASN C 118 ? 2.0288 2.1238 2.1254 -0.4833 -0.0406 -0.1364 156 ASN C ND2 
5560  N N   . CYS C 119 ? 2.0358 1.9758 1.9766 -0.4766 -0.0994 -0.1513 157 CYS C N   
5561  C CA  . CYS C 119 ? 2.0832 2.0092 1.9954 -0.5107 -0.1118 -0.1626 157 CYS C CA  
5562  C C   . CYS C 119 ? 1.9843 1.9583 1.9280 -0.5373 -0.1015 -0.1799 157 CYS C C   
5563  O O   . CYS C 119 ? 1.9079 1.9097 1.8815 -0.5189 -0.0886 -0.1869 157 CYS C O   
5564  C CB  . CYS C 119 ? 2.1812 2.0643 2.0535 -0.4933 -0.1230 -0.1649 157 CYS C CB  
5565  S SG  . CYS C 119 ? 2.7384 2.5667 2.5745 -0.4565 -0.1370 -0.1483 157 CYS C SG  
5566  N N   . SER C 120 ? 1.8781 1.8610 1.8128 -0.5812 -0.1087 -0.1879 158 SER C N   
5567  C CA  . SER C 120 ? 1.8500 1.8788 1.8086 -0.6127 -0.1031 -0.2085 158 SER C CA  
5568  C C   . SER C 120 ? 1.8875 1.8949 1.8034 -0.6422 -0.1170 -0.2231 158 SER C C   
5569  O O   . SER C 120 ? 1.9510 1.9133 1.8198 -0.6585 -0.1322 -0.2154 158 SER C O   
5570  C CB  . SER C 120 ? 1.8215 1.8885 1.8098 -0.6442 -0.0980 -0.2086 158 SER C CB  
5571  O OG  . SER C 120 ? 1.7844 1.8759 1.8137 -0.6190 -0.0835 -0.1971 158 SER C OG  
5572  N N   . PHE C 121 ? 1.7925 1.8308 1.7218 -0.6494 -0.1128 -0.2454 159 PHE C N   
5573  C CA  . PHE C 121 ? 1.8275 1.8491 1.7161 -0.6758 -0.1242 -0.2619 159 PHE C CA  
5574  C C   . PHE C 121 ? 1.7963 1.8738 1.7136 -0.6942 -0.1181 -0.2919 159 PHE C C   
5575  O O   . PHE C 121 ? 1.7510 1.8725 1.7169 -0.6785 -0.1064 -0.2988 159 PHE C O   
5576  C CB  . PHE C 121 ? 1.8723 1.8435 1.7239 -0.6436 -0.1309 -0.2551 159 PHE C CB  
5577  C CG  . PHE C 121 ? 1.8347 1.8186 1.7170 -0.5974 -0.1193 -0.2548 159 PHE C CG  
5578  C CD1 . PHE C 121 ? 1.8246 1.7954 1.7222 -0.5592 -0.1129 -0.2340 159 PHE C CD1 
5579  C CD2 . PHE C 121 ? 1.8204 1.8295 1.7142 -0.5930 -0.1153 -0.2770 159 PHE C CD2 
5580  C CE1 . PHE C 121 ? 1.8027 1.7827 1.7239 -0.5202 -0.1024 -0.2339 159 PHE C CE1 
5581  C CE2 . PHE C 121 ? 1.7991 1.8148 1.7165 -0.5515 -0.1061 -0.2766 159 PHE C CE2 
5582  C CZ  . PHE C 121 ? 1.7913 1.7911 1.7211 -0.5164 -0.0994 -0.2544 159 PHE C CZ  
5583  N N   . ASN C 122 ? 1.8713 1.9459 1.7552 -0.7283 -0.1272 -0.3113 160 ASN C N   
5584  C CA  . ASN C 122 ? 1.8876 2.0140 1.7915 -0.7458 -0.1240 -0.3449 160 ASN C CA  
5585  C C   . ASN C 122 ? 1.9273 2.0460 1.8311 -0.7066 -0.1215 -0.3537 160 ASN C C   
5586  O O   . ASN C 122 ? 1.9780 2.0452 1.8507 -0.6787 -0.1253 -0.3369 160 ASN C O   
5587  C CB  . ASN C 122 ? 2.0175 2.1430 1.8856 -0.7822 -0.1308 -0.3559 160 ASN C CB  
5588  C CG  . ASN C 122 ? 2.0084 2.1641 1.8975 -0.7912 -0.1243 -0.3460 160 ASN C CG  
5589  O OD1 . ASN C 122 ? 1.9534 2.1639 1.8863 -0.7818 -0.1146 -0.3572 160 ASN C OD1 
5590  N ND2 . ASN C 122 ? 2.0462 2.1627 1.9007 -0.8084 -0.1310 -0.3255 160 ASN C ND2 
5591  N N   . MET C 123 ? 1.9511 2.1218 1.8891 -0.7043 -0.1163 -0.3815 161 MET C N   
5592  C CA  . MET C 123 ? 1.9959 2.1617 1.9357 -0.6667 -0.1144 -0.3920 161 MET C CA  
5593  C C   . MET C 123 ? 1.9965 2.2178 1.9559 -0.6815 -0.1151 -0.4325 161 MET C C   
5594  O O   . MET C 123 ? 2.0655 2.3397 2.0578 -0.7050 -0.1133 -0.4499 161 MET C O   
5595  C CB  . MET C 123 ? 1.8826 2.0403 1.8531 -0.6169 -0.1053 -0.3727 161 MET C CB  
5596  C CG  . MET C 123 ? 1.8502 1.9924 1.8155 -0.5772 -0.1044 -0.3795 161 MET C CG  
5597  S SD  . MET C 123 ? 2.3905 2.4796 2.2953 -0.5800 -0.1140 -0.3768 161 MET C SD  
5598  C CE  . MET C 123 ? 1.9784 2.0104 1.8583 -0.5703 -0.1162 -0.3357 161 MET C CE  
5599  N N   . THR C 124 ? 2.0926 2.3021 2.0313 -0.6655 -0.1182 -0.4478 162 THR C N   
5600  C CA  . THR C 124 ? 2.1400 2.3997 2.0937 -0.6737 -0.1202 -0.4892 162 THR C CA  
5601  C C   . THR C 124 ? 2.1042 2.3898 2.1027 -0.6329 -0.1155 -0.4969 162 THR C C   
5602  O O   . THR C 124 ? 2.0811 2.3303 2.0790 -0.5889 -0.1119 -0.4766 162 THR C O   
5603  C CB  . THR C 124 ? 2.1647 2.3997 2.0773 -0.6703 -0.1251 -0.5025 162 THR C CB  
5604  O OG1 . THR C 124 ? 2.3059 2.5063 2.1707 -0.7030 -0.1298 -0.4898 162 THR C OG1 
5605  C CG2 . THR C 124 ? 2.2189 2.5033 2.1483 -0.6632 -0.1246 -0.5354 162 THR C CG2 
5606  N N   . THR C 125 ? 1.9240 2.2700 1.9594 -0.6460 -0.1161 -0.5248 163 THR C N   
5607  C CA  . THR C 125 ? 2.0027 2.3740 2.0773 -0.6122 -0.1151 -0.5377 163 THR C CA  
5608  C C   . THR C 125 ? 2.1097 2.4879 2.1766 -0.5891 -0.1209 -0.5682 163 THR C C   
5609  O O   . THR C 125 ? 2.0966 2.4508 2.1267 -0.5934 -0.1233 -0.5724 163 THR C O   
5610  C CB  . THR C 125 ? 2.0855 2.5081 2.2002 -0.6181 -0.1126 -0.5429 163 THR C CB  
5611  O OG1 . THR C 125 ? 2.1685 2.6155 2.2744 -0.6235 -0.1124 -0.5518 163 THR C OG1 
5612  C CG2 . THR C 125 ? 2.0461 2.4624 2.1704 -0.6378 -0.1063 -0.5127 163 THR C CG2 
5613  N N   . GLU C 126 ? 1.9280 2.3374 2.0273 -0.5640 -0.1240 -0.5904 164 GLU C N   
5614  C CA  . GLU C 126 ? 1.9629 2.3816 2.0559 -0.5408 -0.1313 -0.6231 164 GLU C CA  
5615  C C   . GLU C 126 ? 2.0048 2.4494 2.0855 -0.5526 -0.1307 -0.6322 164 GLU C C   
5616  O O   . GLU C 126 ? 2.0022 2.4375 2.0576 -0.5451 -0.1332 -0.6464 164 GLU C O   
5617  C CB  . GLU C 126 ? 2.0293 2.4695 2.1562 -0.5066 -0.1364 -0.6401 164 GLU C CB  
5618  C CG  . GLU C 126 ? 2.0195 2.4119 2.1509 -0.4669 -0.1300 -0.6024 164 GLU C CG  
5619  C CD  . GLU C 126 ? 2.0117 2.4118 2.1673 -0.4823 -0.1225 -0.5770 164 GLU C CD  
5620  O OE1 . GLU C 126 ? 2.0653 2.5030 2.2324 -0.5242 -0.1221 -0.5847 164 GLU C OE1 
5621  O OE2 . GLU C 126 ? 1.9977 2.3667 2.1596 -0.4537 -0.1166 -0.5497 164 GLU C OE2 
5622  N N   . LEU C 127 ? 2.0992 2.5744 2.1967 -0.5684 -0.1257 -0.6223 165 LEU C N   
5623  C CA  . LEU C 127 ? 2.0897 2.5884 2.1757 -0.5802 -0.1223 -0.6277 165 LEU C CA  
5624  C C   . LEU C 127 ? 2.0164 2.4822 2.0627 -0.6107 -0.1183 -0.6064 165 LEU C C   
5625  O O   . LEU C 127 ? 1.9659 2.3983 2.0009 -0.6255 -0.1176 -0.5832 165 LEU C O   
5626  C CB  . LEU C 127 ? 2.1388 2.6801 2.2561 -0.5845 -0.1179 -0.6258 165 LEU C CB  
5627  C CG  . LEU C 127 ? 2.1760 2.7543 2.3304 -0.5558 -0.1226 -0.6482 165 LEU C CG  
5628  C CD1 . LEU C 127 ? 2.1864 2.7549 2.3661 -0.5430 -0.1261 -0.6413 165 LEU C CD1 
5629  C CD2 . LEU C 127 ? 2.2361 2.8576 2.4089 -0.5629 -0.1172 -0.6512 165 LEU C CD2 
5630  N N   . ARG C 128 ? 2.2411 2.7153 2.2645 -0.6200 -0.1159 -0.6148 166 ARG C N   
5631  C CA  . ARG C 128 ? 2.1763 2.6168 2.1566 -0.6480 -0.1135 -0.5973 166 ARG C CA  
5632  C C   . ARG C 128 ? 2.2314 2.6859 2.2108 -0.6739 -0.1069 -0.5815 166 ARG C C   
5633  O O   . ARG C 128 ? 2.2617 2.7022 2.2064 -0.6961 -0.1039 -0.5748 166 ARG C O   
5634  C CB  . ARG C 128 ? 2.2009 2.6405 2.1530 -0.6462 -0.1134 -0.6144 166 ARG C CB  
5635  C CG  . ARG C 128 ? 2.2183 2.6068 2.1211 -0.6658 -0.1149 -0.5986 166 ARG C CG  
5636  C CD  . ARG C 128 ? 2.3450 2.7328 2.2225 -0.6606 -0.1145 -0.6163 166 ARG C CD  
5637  N NE  . ARG C 128 ? 2.4363 2.7924 2.2677 -0.6908 -0.1123 -0.5999 166 ARG C NE  
5638  C CZ  . ARG C 128 ? 2.5393 2.9078 2.3492 -0.7024 -0.1071 -0.6092 166 ARG C CZ  
5639  N NH1 . ARG C 128 ? 2.5183 2.9326 2.3501 -0.6862 -0.1032 -0.6352 166 ARG C NH1 
5640  N NH2 . ARG C 128 ? 2.6690 3.0031 2.4342 -0.7305 -0.1059 -0.5925 166 ARG C NH2 
5641  N N   . ASP C 129 ? 2.1292 2.6087 2.1439 -0.6712 -0.1045 -0.5751 167 ASP C N   
5642  C CA  . ASP C 129 ? 2.0669 2.5625 2.0847 -0.6917 -0.0978 -0.5615 167 ASP C CA  
5643  C C   . ASP C 129 ? 2.1745 2.6472 2.1988 -0.7019 -0.0977 -0.5338 167 ASP C C   
5644  O O   . ASP C 129 ? 2.0439 2.4741 2.0351 -0.7207 -0.0994 -0.5135 167 ASP C O   
5645  C CB  . ASP C 129 ? 2.1086 2.6596 2.1620 -0.6786 -0.0939 -0.5808 167 ASP C CB  
5646  C CG  . ASP C 129 ? 2.1209 2.6961 2.1664 -0.6707 -0.0930 -0.6078 167 ASP C CG  
5647  O OD1 . ASP C 129 ? 2.1365 2.6858 2.1461 -0.6802 -0.0937 -0.6085 167 ASP C OD1 
5648  O OD2 . ASP C 129 ? 2.1492 2.7680 2.2237 -0.6543 -0.0918 -0.6283 167 ASP C OD2 
5649  N N   . LYS C 130 ? 2.2580 2.7572 2.3238 -0.6885 -0.0963 -0.5330 168 LYS C N   
5650  C CA  . LYS C 130 ? 2.2919 2.7752 2.3685 -0.6969 -0.0946 -0.5071 168 LYS C CA  
5651  C C   . LYS C 130 ? 2.1310 2.5690 2.1918 -0.6970 -0.0995 -0.4945 168 LYS C C   
5652  O O   . LYS C 130 ? 2.0523 2.4839 2.1151 -0.6802 -0.1038 -0.5093 168 LYS C O   
5653  C CB  . LYS C 130 ? 2.3460 2.8670 2.4711 -0.6779 -0.0926 -0.5126 168 LYS C CB  
5654  C CG  . LYS C 130 ? 2.2593 2.8250 2.4009 -0.6758 -0.0883 -0.5261 168 LYS C CG  
5655  C CD  . LYS C 130 ? 2.2611 2.8585 2.4475 -0.6565 -0.0877 -0.5301 168 LYS C CD  
5656  C CE  . LYS C 130 ? 2.1970 2.8368 2.3978 -0.6543 -0.0837 -0.5436 168 LYS C CE  
5657  N NZ  . LYS C 130 ? 2.1407 2.8077 2.3822 -0.6351 -0.0842 -0.5471 168 LYS C NZ  
5658  N N   . LYS C 131 ? 2.4112 2.8159 2.4540 -0.7156 -0.0990 -0.4680 169 LYS C N   
5659  C CA  . LYS C 131 ? 2.2187 2.5771 2.2424 -0.7183 -0.1036 -0.4543 169 LYS C CA  
5660  C C   . LYS C 131 ? 2.1514 2.5194 2.2149 -0.7050 -0.1006 -0.4474 169 LYS C C   
5661  O O   . LYS C 131 ? 2.2607 2.6693 2.3646 -0.6886 -0.0971 -0.4592 169 LYS C O   
5662  C CB  . LYS C 131 ? 2.1910 2.5053 2.1712 -0.7437 -0.1064 -0.4306 169 LYS C CB  
5663  C CG  . LYS C 131 ? 2.2029 2.5054 2.1404 -0.7582 -0.1086 -0.4377 169 LYS C CG  
5664  C CD  . LYS C 131 ? 2.1716 2.5030 2.1127 -0.7713 -0.1025 -0.4360 169 LYS C CD  
5665  C CE  . LYS C 131 ? 2.0820 2.3939 2.0186 -0.7860 -0.1020 -0.4096 169 LYS C CE  
5666  N NZ  . LYS C 131 ? 2.1477 2.4856 2.0854 -0.7985 -0.0957 -0.4085 169 LYS C NZ  
5667  N N   . GLN C 132 ? 1.9804 2.3099 2.0311 -0.7123 -0.1020 -0.4280 170 GLN C N   
5668  C CA  . GLN C 132 ? 1.8518 2.1886 1.9380 -0.7020 -0.0971 -0.4206 170 GLN C CA  
5669  C C   . GLN C 132 ? 1.6783 1.9722 1.7455 -0.7119 -0.0968 -0.3900 170 GLN C C   
5670  O O   . GLN C 132 ? 1.7148 1.9543 1.7419 -0.6963 -0.1007 -0.3732 170 GLN C O   
5671  C CB  . GLN C 132 ? 1.9149 2.2424 2.0080 -0.6652 -0.0965 -0.4302 170 GLN C CB  
5672  C CG  . GLN C 132 ? 1.7974 2.1278 1.9260 -0.6301 -0.0874 -0.4134 170 GLN C CG  
5673  C CD  . GLN C 132 ? 1.7776 2.0892 1.9054 -0.5839 -0.0864 -0.4166 170 GLN C CD  
5674  O OE1 . GLN C 132 ? 1.7870 2.0854 1.8903 -0.5767 -0.0924 -0.4318 170 GLN C OE1 
5675  N NE2 . GLN C 132 ? 1.7306 2.0394 1.8829 -0.5534 -0.0787 -0.4023 170 GLN C NE2 
5676  N N   . LYS C 133 ? 1.6997 2.0111 1.7932 -0.7210 -0.0910 -0.3748 171 LYS C N   
5677  C CA  . LYS C 133 ? 1.7173 1.9890 1.7954 -0.7209 -0.0900 -0.3428 171 LYS C CA  
5678  C C   . LYS C 133 ? 1.6610 1.9196 1.7626 -0.6727 -0.0795 -0.3210 171 LYS C C   
5679  O O   . LYS C 133 ? 1.6479 1.9336 1.7867 -0.6695 -0.0704 -0.3131 171 LYS C O   
5680  C CB  . LYS C 133 ? 1.7477 2.0373 1.8367 -0.7423 -0.0878 -0.3313 171 LYS C CB  
5681  C CG  . LYS C 133 ? 1.7720 2.0362 1.8168 -0.7609 -0.0956 -0.3252 171 LYS C CG  
5682  C CD  . LYS C 133 ? 1.7779 2.0319 1.8222 -0.7711 -0.0943 -0.3016 171 LYS C CD  
5683  C CE  . LYS C 133 ? 1.8712 2.0635 1.8594 -0.7893 -0.1068 -0.2861 171 LYS C CE  
5684  N NZ  . LYS C 133 ? 1.9342 2.1128 1.9262 -0.7948 -0.1067 -0.2637 171 LYS C NZ  
5685  N N   . VAL C 134 ? 1.7403 1.9581 1.8192 -0.6358 -0.0801 -0.3121 172 VAL C N   
5686  C CA  . VAL C 134 ? 1.7278 1.9304 1.8226 -0.5917 -0.0702 -0.2926 172 VAL C CA  
5687  C C   . VAL C 134 ? 1.7599 1.9091 1.8218 -0.5753 -0.0728 -0.2651 172 VAL C C   
5688  O O   . VAL C 134 ? 1.7982 1.9122 1.8188 -0.5881 -0.0842 -0.2626 172 VAL C O   
5689  C CB  . VAL C 134 ? 1.7241 1.9261 1.8237 -0.5584 -0.0681 -0.3053 172 VAL C CB  
5690  C CG1 . VAL C 134 ? 1.6875 1.9430 1.8274 -0.5646 -0.0649 -0.3293 172 VAL C CG1 
5691  C CG2 . VAL C 134 ? 1.7583 1.9346 1.8194 -0.5605 -0.0785 -0.3178 172 VAL C CG2 
5692  N N   . TYR C 135 ? 1.9385 2.0822 2.0178 -0.5466 -0.0628 -0.2457 173 TYR C N   
5693  C CA  . TYR C 135 ? 1.9884 2.0896 2.0435 -0.5270 -0.0646 -0.2218 173 TYR C CA  
5694  C C   . TYR C 135 ? 1.9971 2.0756 2.0485 -0.4820 -0.0585 -0.2127 173 TYR C C   
5695  O O   . TYR C 135 ? 1.9552 2.0535 2.0302 -0.4644 -0.0491 -0.2196 173 TYR C O   
5696  C CB  . TYR C 135 ? 2.0033 2.1202 2.0799 -0.5358 -0.0582 -0.2071 173 TYR C CB  
5697  C CG  . TYR C 135 ? 2.0026 2.1497 2.1199 -0.5144 -0.0412 -0.2022 173 TYR C CG  
5698  C CD1 . TYR C 135 ? 1.9516 2.1451 2.1065 -0.5275 -0.0335 -0.2162 173 TYR C CD1 
5699  C CD2 . TYR C 135 ? 2.0239 2.1534 2.1403 -0.4822 -0.0336 -0.1848 173 TYR C CD2 
5700  C CE1 . TYR C 135 ? 1.9472 2.1635 2.1345 -0.5091 -0.0189 -0.2111 173 TYR C CE1 
5701  C CE2 . TYR C 135 ? 2.0020 2.1572 2.1508 -0.4658 -0.0175 -0.1805 173 TYR C CE2 
5702  C CZ  . TYR C 135 ? 1.9852 2.1813 2.1679 -0.4795 -0.0103 -0.1928 173 TYR C CZ  
5703  O OH  . TYR C 135 ? 1.9319 2.1490 2.1421 -0.4643 0.0048  -0.1881 173 TYR C OH  
5704  N N   . SER C 136 ? 1.8528 1.8880 1.8722 -0.4640 -0.0652 -0.1979 174 SER C N   
5705  C CA  . SER C 136 ? 1.8697 1.8820 1.8824 -0.4227 -0.0604 -0.1884 174 SER C CA  
5706  C C   . SER C 136 ? 1.9585 1.9499 1.9610 -0.4080 -0.0617 -0.1695 174 SER C C   
5707  O O   . SER C 136 ? 1.9939 1.9887 1.9967 -0.4279 -0.0657 -0.1636 174 SER C O   
5708  C CB  . SER C 136 ? 1.9191 1.9000 1.8998 -0.4107 -0.0699 -0.1957 174 SER C CB  
5709  O OG  . SER C 136 ? 1.9337 1.8937 1.9083 -0.3722 -0.0654 -0.1866 174 SER C OG  
5710  N N   . LEU C 137 ? 1.8292 1.7997 1.8220 -0.3725 -0.0591 -0.1617 175 LEU C N   
5711  C CA  . LEU C 137 ? 1.9769 1.9310 1.9609 -0.3524 -0.0606 -0.1476 175 LEU C CA  
5712  C C   . LEU C 137 ? 2.0572 1.9704 2.0073 -0.3253 -0.0714 -0.1446 175 LEU C C   
5713  O O   . LEU C 137 ? 2.0033 1.9158 1.9574 -0.2996 -0.0635 -0.1456 175 LEU C O   
5714  C CB  . LEU C 137 ? 1.9472 1.9319 1.9641 -0.3357 -0.0418 -0.1423 175 LEU C CB  
5715  C CG  . LEU C 137 ? 1.9935 1.9798 2.0125 -0.3270 -0.0411 -0.1317 175 LEU C CG  
5716  C CD1 . LEU C 137 ? 2.0234 2.0231 2.0509 -0.3575 -0.0452 -0.1299 175 LEU C CD1 
5717  C CD2 . LEU C 137 ? 1.9400 1.9524 1.9840 -0.3058 -0.0217 -0.1282 175 LEU C CD2 
5718  N N   . PHE C 138 ? 2.0415 1.9189 1.9565 -0.3312 -0.0901 -0.1411 176 PHE C N   
5719  C CA  . PHE C 138 ? 2.0912 1.9275 1.9716 -0.3069 -0.1031 -0.1387 176 PHE C CA  
5720  C C   . PHE C 138 ? 2.2362 2.0548 2.1042 -0.2847 -0.1116 -0.1294 176 PHE C C   
5721  O O   . PHE C 138 ? 2.3186 2.1447 2.1922 -0.2953 -0.1140 -0.1249 176 PHE C O   
5722  C CB  . PHE C 138 ? 2.1013 1.9039 1.9435 -0.3293 -0.1209 -0.1438 176 PHE C CB  
5723  C CG  . PHE C 138 ? 1.9775 1.8008 1.8306 -0.3513 -0.1141 -0.1569 176 PHE C CG  
5724  C CD1 . PHE C 138 ? 1.9270 1.7532 1.7850 -0.3325 -0.1072 -0.1640 176 PHE C CD1 
5725  C CD2 . PHE C 138 ? 1.9177 1.7612 1.7783 -0.3901 -0.1145 -0.1638 176 PHE C CD2 
5726  C CE1 . PHE C 138 ? 1.8117 1.6592 1.6804 -0.3502 -0.1022 -0.1790 176 PHE C CE1 
5727  C CE2 . PHE C 138 ? 1.7900 1.6584 1.6629 -0.4093 -0.1090 -0.1796 176 PHE C CE2 
5728  C CZ  . PHE C 138 ? 1.7436 1.6138 1.6204 -0.3883 -0.1033 -0.1878 176 PHE C CZ  
5729  N N   . TYR C 139 ? 2.0261 1.8228 1.8779 -0.2529 -0.1168 -0.1282 177 TYR C N   
5730  C CA  . TYR C 139 ? 2.1139 1.8928 1.9508 -0.2277 -0.1281 -0.1233 177 TYR C CA  
5731  C C   . TYR C 139 ? 2.1889 1.9192 1.9804 -0.2382 -0.1553 -0.1211 177 TYR C C   
5732  O O   . TYR C 139 ? 2.1797 1.8857 1.9463 -0.2606 -0.1646 -0.1234 177 TYR C O   
5733  C CB  . TYR C 139 ? 2.1290 1.9045 1.9651 -0.1914 -0.1245 -0.1247 177 TYR C CB  
5734  C CG  . TYR C 139 ? 2.0481 1.8657 1.9219 -0.1815 -0.0989 -0.1263 177 TYR C CG  
5735  C CD1 . TYR C 139 ? 1.9781 1.8072 1.8646 -0.1901 -0.0862 -0.1301 177 TYR C CD1 
5736  C CD2 . TYR C 139 ? 2.0459 1.8898 1.9390 -0.1631 -0.0886 -0.1255 177 TYR C CD2 
5737  C CE1 . TYR C 139 ? 1.9479 1.8082 1.8625 -0.1816 -0.0651 -0.1313 177 TYR C CE1 
5738  C CE2 . TYR C 139 ? 1.9701 1.8483 1.8917 -0.1570 -0.0654 -0.1268 177 TYR C CE2 
5739  C CZ  . TYR C 139 ? 1.9372 1.8204 1.8676 -0.1663 -0.0544 -0.1289 177 TYR C CZ  
5740  O OH  . TYR C 139 ? 1.9125 1.8227 1.8650 -0.1607 -0.0336 -0.1299 177 TYR C OH  
5741  N N   . ARG C 140 ? 2.4362 2.1516 2.2145 -0.2219 -0.1688 -0.1179 178 ARG C N   
5742  C CA  . ARG C 140 ? 2.5440 2.2065 2.2737 -0.2299 -0.1976 -0.1156 178 ARG C CA  
5743  C C   . ARG C 140 ? 2.5898 2.2080 2.2809 -0.2163 -0.2139 -0.1170 178 ARG C C   
5744  O O   . ARG C 140 ? 2.6183 2.1907 2.2653 -0.2357 -0.2340 -0.1159 178 ARG C O   
5745  C CB  . ARG C 140 ? 2.5948 2.2524 2.3200 -0.2107 -0.2097 -0.1141 178 ARG C CB  
5746  C CG  . ARG C 140 ? 2.6656 2.2633 2.3366 -0.2157 -0.2426 -0.1119 178 ARG C CG  
5747  C CD  . ARG C 140 ? 2.7561 2.3571 2.4293 -0.1971 -0.2526 -0.1128 178 ARG C CD  
5748  N NE  . ARG C 140 ? 2.7862 2.4305 2.4963 -0.2183 -0.2345 -0.1109 178 ARG C NE  
5749  C CZ  . ARG C 140 ? 2.8330 2.4635 2.5296 -0.2531 -0.2417 -0.1067 178 ARG C CZ  
5750  N NH1 . ARG C 140 ? 2.8600 2.4320 2.5033 -0.2731 -0.2670 -0.1040 178 ARG C NH1 
5751  N NH2 . ARG C 140 ? 2.8709 2.5459 2.6060 -0.2693 -0.2236 -0.1053 178 ARG C NH2 
5752  N N   . LEU C 141 ? 2.4366 2.0671 2.1417 -0.1848 -0.2051 -0.1196 179 LEU C N   
5753  C CA  . LEU C 141 ? 2.3882 1.9813 2.0614 -0.1691 -0.2184 -0.1211 179 LEU C CA  
5754  C C   . LEU C 141 ? 2.3024 1.8888 1.9671 -0.1948 -0.2126 -0.1236 179 LEU C C   
5755  O O   . LEU C 141 ? 2.3056 1.8554 1.9370 -0.1899 -0.2256 -0.1248 179 LEU C O   
5756  C CB  . LEU C 141 ? 2.3826 1.9972 2.0776 -0.1300 -0.2083 -0.1241 179 LEU C CB  
5757  C CG  . LEU C 141 ? 2.4470 2.0764 2.1529 -0.1025 -0.2126 -0.1259 179 LEU C CG  
5758  C CD1 . LEU C 141 ? 2.3704 2.0308 2.1021 -0.0703 -0.1979 -0.1308 179 LEU C CD1 
5759  C CD2 . LEU C 141 ? 2.5304 2.1088 2.1907 -0.0909 -0.2459 -0.1261 179 LEU C CD2 
5760  N N   . ASP C 142 ? 2.4259 2.0489 2.1206 -0.2212 -0.1937 -0.1260 180 ASP C N   
5761  C CA  . ASP C 142 ? 2.3472 1.9736 2.0395 -0.2458 -0.1870 -0.1324 180 ASP C CA  
5762  C C   . ASP C 142 ? 2.3474 1.9514 2.0089 -0.2876 -0.2001 -0.1341 180 ASP C C   
5763  O O   . ASP C 142 ? 2.2767 1.8724 1.9216 -0.3080 -0.2009 -0.1416 180 ASP C O   
5764  C CB  . ASP C 142 ? 2.2436 1.9241 1.9855 -0.2509 -0.1608 -0.1369 180 ASP C CB  
5765  C CG  . ASP C 142 ? 2.2003 1.9004 1.9673 -0.2150 -0.1465 -0.1365 180 ASP C CG  
5766  O OD1 . ASP C 142 ? 2.2218 1.8979 1.9699 -0.1922 -0.1533 -0.1369 180 ASP C OD1 
5767  O OD2 . ASP C 142 ? 2.2360 1.9745 2.0398 -0.2108 -0.1287 -0.1357 180 ASP C OD2 
5768  N N   . VAL C 143 ? 2.2309 1.8263 1.8836 -0.3018 -0.2098 -0.1288 181 VAL C N   
5769  C CA  . VAL C 143 ? 2.2627 1.8390 1.8865 -0.3452 -0.2213 -0.1301 181 VAL C CA  
5770  C C   . VAL C 143 ? 2.3636 1.8767 1.9300 -0.3449 -0.2509 -0.1235 181 VAL C C   
5771  O O   . VAL C 143 ? 2.4035 1.8940 1.9590 -0.3092 -0.2625 -0.1186 181 VAL C O   
5772  C CB  . VAL C 143 ? 2.1989 1.8185 1.8598 -0.3689 -0.2079 -0.1300 181 VAL C CB  
5773  C CG1 . VAL C 143 ? 2.1178 1.7941 1.8284 -0.3742 -0.1822 -0.1385 181 VAL C CG1 
5774  C CG2 . VAL C 143 ? 2.1927 1.8206 1.8717 -0.3428 -0.2080 -0.1217 181 VAL C CG2 
5775  N N   . VAL C 144 ? 2.3467 1.8309 1.8739 -0.3864 -0.2640 -0.1251 182 VAL C N   
5776  C CA  . VAL C 144 ? 2.4525 1.8698 1.9167 -0.3948 -0.2943 -0.1191 182 VAL C CA  
5777  C C   . VAL C 144 ? 2.4719 1.8792 1.9109 -0.4491 -0.3002 -0.1211 182 VAL C C   
5778  O O   . VAL C 144 ? 2.4469 1.8742 1.8881 -0.4838 -0.2898 -0.1304 182 VAL C O   
5779  C CB  . VAL C 144 ? 2.5340 1.8982 1.9491 -0.3796 -0.3119 -0.1195 182 VAL C CB  
5780  C CG1 . VAL C 144 ? 2.5675 1.9207 1.9537 -0.4187 -0.3107 -0.1279 182 VAL C CG1 
5781  C CG2 . VAL C 144 ? 2.6363 1.9317 1.9937 -0.3682 -0.3449 -0.1120 182 VAL C CG2 
5782  N N   . GLN C 145 ? 2.4116 1.7939 1.8306 -0.4569 -0.3158 -0.1140 183 GLN C N   
5783  C CA  . GLN C 145 ? 2.4313 1.8038 1.8265 -0.5085 -0.3221 -0.1148 183 GLN C CA  
5784  C C   . GLN C 145 ? 2.5434 1.8519 1.8632 -0.5422 -0.3440 -0.1172 183 GLN C C   
5785  O O   . GLN C 145 ? 2.6351 1.8938 1.9129 -0.5210 -0.3608 -0.1151 183 GLN C O   
5786  C CB  . GLN C 145 ? 2.4520 1.8094 1.8425 -0.5036 -0.3348 -0.1061 183 GLN C CB  
5787  C CG  . GLN C 145 ? 2.5596 1.8507 1.9010 -0.4690 -0.3647 -0.0993 183 GLN C CG  
5788  C CD  . GLN C 145 ? 2.5799 1.8587 1.9179 -0.4618 -0.3778 -0.0934 183 GLN C CD  
5789  O OE1 . GLN C 145 ? 2.5145 1.8310 1.8834 -0.4870 -0.3647 -0.0928 183 GLN C OE1 
5790  N NE2 . GLN C 145 ? 2.6747 1.8998 1.9736 -0.4273 -0.4053 -0.0901 183 GLN C NE2 
5791  N N   . ILE C 146 ? 2.4266 1.7371 1.7277 -0.5969 -0.3441 -0.1224 184 ILE C N   
5792  C CA  . ILE C 146 ? 2.4956 1.7471 1.7212 -0.6366 -0.3636 -0.1261 184 ILE C CA  
5793  C C   . ILE C 146 ? 2.5252 1.7611 1.7194 -0.6910 -0.3731 -0.1260 184 ILE C C   
5794  O O   . ILE C 146 ? 2.4732 1.7694 1.7155 -0.7152 -0.3539 -0.1315 184 ILE C O   
5795  C CB  . ILE C 146 ? 2.4733 1.7554 1.7080 -0.6530 -0.3471 -0.1407 184 ILE C CB  
5796  C CG1 . ILE C 146 ? 2.5433 1.7715 1.6997 -0.7037 -0.3646 -0.1470 184 ILE C CG1 
5797  C CG2 . ILE C 146 ? 2.3928 1.7637 1.7014 -0.6674 -0.3164 -0.1524 184 ILE C CG2 
5798  C CD1 . ILE C 146 ? 2.6252 1.7630 1.7054 -0.6873 -0.3952 -0.1369 184 ILE C CD1 
5799  N N   . ASN C 147 ? 2.8685 2.0208 1.9797 -0.7100 -0.4041 -0.1197 185 ASN C N   
5800  C CA  . ASN C 147 ? 2.9467 2.0693 2.0104 -0.7680 -0.4172 -0.1199 185 ASN C CA  
5801  C C   . ASN C 147 ? 3.0739 2.1533 2.0653 -0.8194 -0.4280 -0.1290 185 ASN C C   
5802  O O   . ASN C 147 ? 3.0133 2.1433 2.0261 -0.8529 -0.4079 -0.1445 185 ASN C O   
5803  C CB  . ASN C 147 ? 3.0489 2.1022 2.0658 -0.7536 -0.4475 -0.1055 185 ASN C CB  
5804  C CG  . ASN C 147 ? 2.9570 2.0495 2.0165 -0.7628 -0.4390 -0.1017 185 ASN C CG  
5805  O OD1 . ASN C 147 ? 2.8116 1.9849 1.9393 -0.7771 -0.4100 -0.1089 185 ASN C OD1 
5806  N ND2 . ASN C 147 ? 3.0365 2.0714 2.0558 -0.7527 -0.4654 -0.0911 185 ASN C ND2 
5807  N N   . GLU C 160 ? 2.2339 1.7693 1.7405 -0.6612 -0.2761 -0.1259 190 GLU C N   
5808  C CA  . GLU C 160 ? 2.2427 1.7982 1.7541 -0.6704 -0.2656 -0.1391 190 GLU C CA  
5809  C C   . GLU C 160 ? 2.3041 1.8350 1.8064 -0.6229 -0.2685 -0.1364 190 GLU C C   
5810  O O   . GLU C 160 ? 2.3963 1.8638 1.8480 -0.6050 -0.2910 -0.1276 190 GLU C O   
5811  C CB  . GLU C 160 ? 2.3055 1.8233 1.7546 -0.7237 -0.2811 -0.1474 190 GLU C CB  
5812  C CG  . GLU C 160 ? 2.1995 1.7507 1.6570 -0.7804 -0.2756 -0.1563 190 GLU C CG  
5813  C CD  . GLU C 160 ? 2.3374 1.8528 1.7298 -0.8333 -0.2895 -0.1673 190 GLU C CD  
5814  O OE1 . GLU C 160 ? 2.4652 1.9258 1.8046 -0.8239 -0.3041 -0.1662 190 GLU C OE1 
5815  O OE2 . GLU C 160 ? 2.3658 1.9088 1.7590 -0.8853 -0.2858 -0.1780 190 GLU C OE2 
5816  N N   . TYR C 161 ? 2.3348 1.9130 1.8835 -0.6019 -0.2476 -0.1443 191 TYR C N   
5817  C CA  . TYR C 161 ? 2.3082 1.8668 1.8515 -0.5572 -0.2489 -0.1419 191 TYR C CA  
5818  C C   . TYR C 161 ? 2.3098 1.8791 1.8479 -0.5682 -0.2419 -0.1561 191 TYR C C   
5819  O O   . TYR C 161 ? 2.2661 1.8547 1.7993 -0.6114 -0.2383 -0.1692 191 TYR C O   
5820  C CB  . TYR C 161 ? 2.2201 1.8199 1.8218 -0.5115 -0.2312 -0.1364 191 TYR C CB  
5821  C CG  . TYR C 161 ? 2.2612 1.8484 1.8654 -0.4910 -0.2391 -0.1241 191 TYR C CG  
5822  C CD1 . TYR C 161 ? 2.2493 1.8642 1.8776 -0.5126 -0.2333 -0.1216 191 TYR C CD1 
5823  C CD2 . TYR C 161 ? 2.3311 1.8828 1.9162 -0.4481 -0.2520 -0.1169 191 TYR C CD2 
5824  C CE1 . TYR C 161 ? 2.2486 1.8539 1.8795 -0.4920 -0.2404 -0.1121 191 TYR C CE1 
5825  C CE2 . TYR C 161 ? 2.3643 1.9084 1.9525 -0.4271 -0.2599 -0.1092 191 TYR C CE2 
5826  C CZ  . TYR C 161 ? 2.3165 1.8868 1.9269 -0.4487 -0.2539 -0.1068 191 TYR C CZ  
5827  O OH  . TYR C 161 ? 2.3653 1.9288 1.9782 -0.4259 -0.2621 -0.1009 191 TYR C OH  
5828  N N   . ARG C 162 ? 2.2262 1.7849 1.7660 -0.5282 -0.2401 -0.1548 192 ARG C N   
5829  C CA  . ARG C 162 ? 2.2478 1.8179 1.7876 -0.5283 -0.2323 -0.1678 192 ARG C CA  
5830  C C   . ARG C 162 ? 2.1631 1.7366 1.7263 -0.4748 -0.2248 -0.1627 192 ARG C C   
5831  O O   . ARG C 162 ? 2.1524 1.7100 1.7190 -0.4416 -0.2299 -0.1501 192 ARG C O   
5832  C CB  . ARG C 162 ? 2.3959 1.9127 1.8677 -0.5558 -0.2511 -0.1727 192 ARG C CB  
5833  C CG  . ARG C 162 ? 2.4416 1.8941 1.8675 -0.5239 -0.2708 -0.1609 192 ARG C CG  
5834  C CD  . ARG C 162 ? 2.5178 1.9252 1.8824 -0.5477 -0.2845 -0.1682 192 ARG C CD  
5835  N NE  . ARG C 162 ? 2.5661 1.9181 1.8938 -0.5116 -0.3012 -0.1586 192 ARG C NE  
5836  C CZ  . ARG C 162 ? 2.7192 2.0052 1.9917 -0.5097 -0.3276 -0.1471 192 ARG C CZ  
5837  N NH1 . ARG C 162 ? 2.8150 2.0798 2.0609 -0.5427 -0.3400 -0.1430 192 ARG C NH1 
5838  N NH2 . ARG C 162 ? 2.7368 1.9770 1.9798 -0.4743 -0.3429 -0.1404 192 ARG C NH2 
5839  N N   . LEU C 163 ? 2.1782 1.7741 1.7570 -0.4670 -0.2129 -0.1743 193 LEU C N   
5840  C CA  . LEU C 163 ? 2.1824 1.7772 1.7774 -0.4192 -0.2068 -0.1700 193 LEU C CA  
5841  C C   . LEU C 163 ? 2.2596 1.7918 1.8015 -0.4020 -0.2278 -0.1621 193 LEU C C   
5842  O O   . LEU C 163 ? 2.3218 1.8165 1.8140 -0.4285 -0.2423 -0.1662 193 LEU C O   
5843  C CB  . LEU C 163 ? 2.1636 1.7942 1.7850 -0.4155 -0.1906 -0.1852 193 LEU C CB  
5844  C CG  . LEU C 163 ? 2.0830 1.7753 1.7608 -0.4218 -0.1705 -0.1934 193 LEU C CG  
5845  C CD1 . LEU C 163 ? 2.0645 1.7852 1.7631 -0.4127 -0.1582 -0.2096 193 LEU C CD1 
5846  C CD2 . LEU C 163 ? 2.0378 1.7460 1.7509 -0.3920 -0.1616 -0.1796 193 LEU C CD2 
5847  N N   . ILE C 164 ? 2.3558 1.8772 1.9067 -0.3583 -0.2297 -0.1519 194 ILE C N   
5848  C CA  . ILE C 164 ? 2.4201 1.8830 1.9230 -0.3382 -0.2521 -0.1444 194 ILE C CA  
5849  C C   . ILE C 164 ? 2.4583 1.8989 1.9342 -0.3345 -0.2552 -0.1510 194 ILE C C   
5850  O O   . ILE C 164 ? 2.5718 1.9583 1.9987 -0.3271 -0.2760 -0.1464 194 ILE C O   
5851  C CB  . ILE C 164 ? 2.3955 1.8620 1.9204 -0.2913 -0.2523 -0.1354 194 ILE C CB  
5852  C CG1 . ILE C 164 ? 2.4798 1.8853 1.9538 -0.2749 -0.2811 -0.1281 194 ILE C CG1 
5853  C CG2 . ILE C 164 ? 2.3348 1.8290 1.8927 -0.2586 -0.2353 -0.1389 194 ILE C CG2 
5854  C CD1 . ILE C 164 ? 2.4398 1.8522 1.9341 -0.2294 -0.2835 -0.1231 194 ILE C CD1 
5855  N N   . ASN C 165 ? 2.2762 1.7554 1.7805 -0.3400 -0.2363 -0.1627 195 ASN C N   
5856  C CA  . ASN C 165 ? 2.3608 1.8248 1.8447 -0.3339 -0.2369 -0.1704 195 ASN C CA  
5857  C C   . ASN C 165 ? 2.3702 1.8312 1.8249 -0.3795 -0.2388 -0.1845 195 ASN C C   
5858  O O   . ASN C 165 ? 2.4834 1.9269 1.9125 -0.3797 -0.2414 -0.1921 195 ASN C O   
5859  C CB  . ASN C 165 ? 2.3073 1.8139 1.8393 -0.3043 -0.2157 -0.1760 195 ASN C CB  
5860  C CG  . ASN C 165 ? 2.1979 1.7570 1.7674 -0.3273 -0.1975 -0.1898 195 ASN C CG  
5861  O OD1 . ASN C 165 ? 2.1997 1.7705 1.7644 -0.3429 -0.1927 -0.2051 195 ASN C OD1 
5862  N ND2 . ASN C 165 ? 2.1542 1.7466 1.7609 -0.3294 -0.1879 -0.1859 195 ASN C ND2 
5863  N N   . CYS C 166 ? 2.3306 1.8104 1.7888 -0.4189 -0.2372 -0.1893 196 CYS C N   
5864  C CA  . CYS C 166 ? 2.3623 1.8483 1.7961 -0.4663 -0.2374 -0.2061 196 CYS C CA  
5865  C C   . CYS C 166 ? 2.4527 1.8746 1.8137 -0.4855 -0.2588 -0.2041 196 CYS C C   
5866  O O   . CYS C 166 ? 2.4912 1.9133 1.8253 -0.5176 -0.2585 -0.2198 196 CYS C O   
5867  C CB  . CYS C 166 ? 2.3196 1.8377 1.7713 -0.5045 -0.2330 -0.2105 196 CYS C CB  
5868  S SG  . CYS C 166 ? 2.2713 1.8725 1.8029 -0.4976 -0.2064 -0.2226 196 CYS C SG  
5869  N N   . ASN C 167 ? 2.4439 1.8110 1.7708 -0.4668 -0.2782 -0.1866 197 ASN C N   
5870  C CA  . ASN C 167 ? 2.5731 1.8714 1.8259 -0.4821 -0.3015 -0.1832 197 ASN C CA  
5871  C C   . ASN C 167 ? 2.6131 1.8822 1.8533 -0.4396 -0.3072 -0.1781 197 ASN C C   
5872  O O   . ASN C 167 ? 2.7154 1.9214 1.8945 -0.4421 -0.3290 -0.1724 197 ASN C O   
5873  C CB  . ASN C 167 ? 2.6039 1.8528 1.8173 -0.4935 -0.3243 -0.1690 197 ASN C CB  
5874  C CG  . ASN C 167 ? 2.5632 1.7931 1.7898 -0.4420 -0.3341 -0.1533 197 ASN C CG  
5875  O OD1 . ASN C 167 ? 2.4702 1.7470 1.7564 -0.4153 -0.3187 -0.1503 197 ASN C OD1 
5876  N ND2 . ASN C 167 ? 2.7906 1.9512 1.9594 -0.4293 -0.3607 -0.1444 197 ASN C ND2 
5877  N N   . THR C 168 ? 2.5072 1.8192 1.8022 -0.4012 -0.2888 -0.1801 198 THR C N   
5878  C CA  . THR C 168 ? 2.4970 1.7887 1.7870 -0.3600 -0.2919 -0.1761 198 THR C CA  
5879  C C   . THR C 168 ? 2.4642 1.7897 1.7752 -0.3569 -0.2736 -0.1911 198 THR C C   
5880  O O   . THR C 168 ? 2.5273 1.8218 1.8017 -0.3553 -0.2807 -0.1945 198 THR C O   
5881  C CB  . THR C 168 ? 2.4976 1.8036 1.8294 -0.3111 -0.2888 -0.1640 198 THR C CB  
5882  O OG1 . THR C 168 ? 2.4452 1.8158 1.8414 -0.3019 -0.2633 -0.1698 198 THR C OG1 
5883  C CG2 . THR C 168 ? 2.6190 1.8988 1.9352 -0.3124 -0.3060 -0.1521 198 THR C CG2 
5884  N N   . SER C 169 ? 2.5259 1.9126 1.8928 -0.3556 -0.2514 -0.2009 199 SER C N   
5885  C CA  . SER C 169 ? 2.4869 1.9064 1.8756 -0.3486 -0.2352 -0.2168 199 SER C CA  
5886  C C   . SER C 169 ? 2.4219 1.9041 1.8611 -0.3627 -0.2161 -0.2305 199 SER C C   
5887  O O   . SER C 169 ? 2.4094 1.9091 1.8655 -0.3798 -0.2149 -0.2270 199 SER C O   
5888  C CB  . SER C 169 ? 2.4551 1.8706 1.8633 -0.2974 -0.2311 -0.2090 199 SER C CB  
5889  O OG  . SER C 169 ? 2.4010 1.8406 1.8539 -0.2692 -0.2233 -0.1985 199 SER C OG  
5890  N N   . ALA C 170 ? 2.3669 1.8825 1.8298 -0.3540 -0.2021 -0.2469 200 ALA C N   
5891  C CA  . ALA C 170 ? 2.2972 1.8712 1.8083 -0.3609 -0.1856 -0.2622 200 ALA C CA  
5892  C C   . ALA C 170 ? 2.2381 1.8312 1.7962 -0.3234 -0.1757 -0.2489 200 ALA C C   
5893  O O   . ALA C 170 ? 2.2458 1.8116 1.8001 -0.2921 -0.1804 -0.2309 200 ALA C O   
5894  C CB  . ALA C 170 ? 2.2652 1.8644 1.7819 -0.3609 -0.1766 -0.2860 200 ALA C CB  
5895  N N   . ILE C 171 ? 2.1269 1.7680 1.7283 -0.3269 -0.1623 -0.2594 201 ILE C N   
5896  C CA  . ILE C 171 ? 2.0769 1.7369 1.7199 -0.2969 -0.1521 -0.2479 201 ILE C CA  
5897  C C   . ILE C 171 ? 2.0379 1.7402 1.7189 -0.2870 -0.1379 -0.2646 201 ILE C C   
5898  O O   . ILE C 171 ? 2.0257 1.7590 1.7150 -0.3136 -0.1354 -0.2853 201 ILE C O   
5899  C CB  . ILE C 171 ? 2.0804 1.7478 1.7351 -0.3133 -0.1537 -0.2360 201 ILE C CB  
5900  C CG1 . ILE C 171 ? 2.0355 1.7261 1.7327 -0.2850 -0.1412 -0.2261 201 ILE C CG1 
5901  C CG2 . ILE C 171 ? 2.0716 1.7677 1.7292 -0.3583 -0.1534 -0.2518 201 ILE C CG2 
5902  C CD1 . ILE C 171 ? 2.0273 1.7275 1.7382 -0.2978 -0.1414 -0.2146 201 ILE C CD1 
5903  N N   . THR C 172 ? 2.1561 1.8587 1.8579 -0.2488 -0.1298 -0.2571 202 THR C N   
5904  C CA  . THR C 172 ? 2.0659 1.8002 1.7998 -0.2348 -0.1183 -0.2706 202 THR C CA  
5905  C C   . THR C 172 ? 2.0443 1.7882 1.8082 -0.2130 -0.1089 -0.2559 202 THR C C   
5906  O O   . THR C 172 ? 2.0884 1.8104 1.8471 -0.1922 -0.1094 -0.2369 202 THR C O   
5907  C CB  . THR C 172 ? 2.0330 1.7552 1.7568 -0.2100 -0.1173 -0.2797 202 THR C CB  
5908  O OG1 . THR C 172 ? 1.9577 1.7019 1.7102 -0.1898 -0.1076 -0.2884 202 THR C OG1 
5909  C CG2 . THR C 172 ? 2.0038 1.6872 1.7079 -0.1827 -0.1213 -0.2599 202 THR C CG2 
5910  N N   . GLN C 173 ? 2.0446 1.8226 1.8385 -0.2189 -0.1009 -0.2662 203 GLN C N   
5911  C CA  . GLN C 173 ? 2.0403 1.8293 1.8610 -0.2027 -0.0911 -0.2541 203 GLN C CA  
5912  C C   . GLN C 173 ? 2.0189 1.7987 1.8439 -0.1685 -0.0845 -0.2544 203 GLN C C   
5913  O O   . GLN C 173 ? 1.9439 1.7282 1.7677 -0.1625 -0.0852 -0.2721 203 GLN C O   
5914  C CB  . GLN C 173 ? 1.9569 1.7837 1.8060 -0.2239 -0.0862 -0.2646 203 GLN C CB  
5915  C CG  . GLN C 173 ? 1.9236 1.7605 1.7974 -0.2100 -0.0756 -0.2517 203 GLN C CG  
5916  C CD  . GLN C 173 ? 1.8725 1.7461 1.7748 -0.2281 -0.0712 -0.2632 203 GLN C CD  
5917  O OE1 . GLN C 173 ? 1.8873 1.7742 1.8079 -0.2332 -0.0645 -0.2518 203 GLN C OE1 
5918  N NE2 . GLN C 173 ? 1.8070 1.6992 1.7139 -0.2368 -0.0751 -0.2874 203 GLN C NE2 
5919  N N   . ALA C 174 ? 2.1341 1.9017 1.9628 -0.1469 -0.0786 -0.2362 204 ALA C N   
5920  C CA  . ALA C 174 ? 2.0587 1.8168 1.8897 -0.1175 -0.0718 -0.2353 204 ALA C CA  
5921  C C   . ALA C 174 ? 2.0077 1.7872 1.8596 -0.1190 -0.0651 -0.2462 204 ALA C C   
5922  O O   . ALA C 174 ? 2.0221 1.8234 1.8929 -0.1349 -0.0609 -0.2440 204 ALA C O   
5923  C CB  . ALA C 174 ? 2.1010 1.8459 1.9307 -0.0981 -0.0665 -0.2152 204 ALA C CB  
5924  N N   . CYS C 175 ? 2.1034 1.8753 1.9507 -0.1017 -0.0651 -0.2585 205 CYS C N   
5925  C CA  . CYS C 175 ? 2.0278 1.8136 1.8898 -0.0997 -0.0619 -0.2703 205 CYS C CA  
5926  C C   . CYS C 175 ? 2.0491 1.8302 1.9184 -0.0896 -0.0516 -0.2536 205 CYS C C   
5927  O O   . CYS C 175 ? 2.1149 1.8759 1.9729 -0.0724 -0.0468 -0.2385 205 CYS C O   
5928  C CB  . CYS C 175 ? 1.9944 1.7682 1.8457 -0.0808 -0.0664 -0.2881 205 CYS C CB  
5929  S SG  . CYS C 175 ? 2.6161 2.3989 2.4573 -0.0921 -0.0771 -0.3117 205 CYS C SG  
5930  N N   . PRO C 176 ? 2.1437 1.9447 2.0311 -0.1010 -0.0478 -0.2569 206 PRO C N   
5931  C CA  . PRO C 176 ? 2.1808 1.9780 2.0726 -0.0946 -0.0369 -0.2417 206 PRO C CA  
5932  C C   . PRO C 176 ? 2.2147 1.9859 2.0907 -0.0713 -0.0346 -0.2433 206 PRO C C   
5933  O O   . PRO C 176 ? 2.2970 2.0600 2.1694 -0.0659 -0.0250 -0.2305 206 PRO C O   
5934  C CB  . PRO C 176 ? 2.1229 1.9493 2.0377 -0.1153 -0.0354 -0.2481 206 PRO C CB  
5935  C CG  . PRO C 176 ? 2.0374 1.8761 1.9560 -0.1218 -0.0467 -0.2729 206 PRO C CG  
5936  C CD  . PRO C 176 ? 2.0763 1.9056 1.9803 -0.1206 -0.0535 -0.2766 206 PRO C CD  
5937  N N   . LYS C 177 ? 2.6060 2.3638 2.4703 -0.0587 -0.0433 -0.2596 207 LYS C N   
5938  C CA  . LYS C 177 ? 2.5956 2.3239 2.4408 -0.0362 -0.0434 -0.2626 207 LYS C CA  
5939  C C   . LYS C 177 ? 2.6362 2.3390 2.4629 -0.0189 -0.0376 -0.2467 207 LYS C C   
5940  O O   . LYS C 177 ? 2.6643 2.3461 2.4766 -0.0076 -0.0314 -0.2386 207 LYS C O   
5941  C CB  . LYS C 177 ? 2.5480 2.2730 2.3878 -0.0275 -0.0559 -0.2877 207 LYS C CB  
5942  C CG  . LYS C 177 ? 2.4603 2.2211 2.3211 -0.0486 -0.0632 -0.3067 207 LYS C CG  
5943  C CD  . LYS C 177 ? 2.4499 2.2294 2.3283 -0.0622 -0.0612 -0.3081 207 LYS C CD  
5944  C CE  . LYS C 177 ? 2.5733 2.3370 2.4425 -0.0466 -0.0687 -0.3238 207 LYS C CE  
5945  N NZ  . LYS C 177 ? 2.5519 2.3349 2.4385 -0.0604 -0.0682 -0.3268 207 LYS C NZ  
5946  N N   . VAL C 178 ? 2.3765 2.0804 2.2013 -0.0177 -0.0401 -0.2429 208 VAL C N   
5947  C CA  . VAL C 178 ? 2.4177 2.1011 2.2272 -0.0007 -0.0362 -0.2298 208 VAL C CA  
5948  C C   . VAL C 178 ? 2.4431 2.1368 2.2596 -0.0073 -0.0265 -0.2113 208 VAL C C   
5949  O O   . VAL C 178 ? 2.4506 2.1671 2.2839 -0.0255 -0.0239 -0.2079 208 VAL C O   
5950  C CB  . VAL C 178 ? 2.4300 2.1084 2.2327 0.0046  -0.0441 -0.2338 208 VAL C CB  
5951  C CG1 . VAL C 178 ? 2.3786 2.0521 2.1753 0.0101  -0.0530 -0.2553 208 VAL C CG1 
5952  C CG2 . VAL C 178 ? 2.3910 2.0887 2.2046 -0.0148 -0.0469 -0.2286 208 VAL C CG2 
5953  N N   . SER C 179 ? 2.4509 2.1299 2.2548 0.0078  -0.0211 -0.2008 209 SER C N   
5954  C CA  . SER C 179 ? 2.4889 2.1806 2.2984 0.0040  -0.0124 -0.1867 209 SER C CA  
5955  C C   . SER C 179 ? 2.5307 2.2163 2.3331 0.0177  -0.0158 -0.1805 209 SER C C   
5956  O O   . SER C 179 ? 2.5025 2.1686 2.2915 0.0333  -0.0207 -0.1842 209 SER C O   
5957  C CB  . SER C 179 ? 2.4882 2.1731 2.2886 0.0066  -0.0005 -0.1813 209 SER C CB  
5958  O OG  . SER C 179 ? 2.4914 2.1507 2.2705 0.0248  0.0001  -0.1814 209 SER C OG  
5959  N N   . PHE C 180 ? 2.4049 2.1077 2.2163 0.0126  -0.0140 -0.1720 210 PHE C N   
5960  C CA  . PHE C 180 ? 2.4022 2.1013 2.2076 0.0261  -0.0195 -0.1671 210 PHE C CA  
5961  C C   . PHE C 180 ? 2.4995 2.2027 2.3003 0.0376  -0.0098 -0.1616 210 PHE C C   
5962  O O   . PHE C 180 ? 2.5355 2.2503 2.3392 0.0437  -0.0117 -0.1578 210 PHE C O   
5963  C CB  . PHE C 180 ? 2.4139 2.1260 2.2281 0.0157  -0.0277 -0.1638 210 PHE C CB  
5964  C CG  . PHE C 180 ? 2.3746 2.0857 2.1917 -0.0011 -0.0364 -0.1699 210 PHE C CG  
5965  C CD1 . PHE C 180 ? 2.3340 2.0315 2.1437 0.0002  -0.0404 -0.1798 210 PHE C CD1 
5966  C CD2 . PHE C 180 ? 2.3404 2.0649 2.1663 -0.0188 -0.0412 -0.1674 210 PHE C CD2 
5967  C CE1 . PHE C 180 ? 2.3272 2.0287 2.1391 -0.0173 -0.0480 -0.1886 210 PHE C CE1 
5968  C CE2 . PHE C 180 ? 2.3108 2.0360 2.1374 -0.0374 -0.0489 -0.1743 210 PHE C CE2 
5969  C CZ  . PHE C 180 ? 2.3471 2.0627 2.1671 -0.0374 -0.0520 -0.1856 210 PHE C CZ  
5970  N N   . GLU C 181 ? 2.3417 2.0353 2.1333 0.0399  -0.0003 -0.1628 211 GLU C N   
5971  C CA  . GLU C 181 ? 2.4466 2.1440 2.2298 0.0469  0.0101  -0.1593 211 GLU C CA  
5972  C C   . GLU C 181 ? 2.4300 2.1098 2.1995 0.0670  0.0056  -0.1605 211 GLU C C   
5973  O O   . GLU C 181 ? 2.3906 2.0455 2.1474 0.0740  0.0029  -0.1643 211 GLU C O   
5974  C CB  . GLU C 181 ? 2.5001 2.1908 2.2735 0.0374  0.0220  -0.1594 211 GLU C CB  
5975  C CG  . GLU C 181 ? 2.5858 2.2876 2.3503 0.0367  0.0351  -0.1563 211 GLU C CG  
5976  C CD  . GLU C 181 ? 2.6773 2.4152 2.4591 0.0264  0.0416  -0.1540 211 GLU C CD  
5977  O OE1 . GLU C 181 ? 2.6327 2.3839 2.4317 0.0161  0.0383  -0.1530 211 GLU C OE1 
5978  O OE2 . GLU C 181 ? 2.7722 2.5270 2.5500 0.0286  0.0498  -0.1547 211 GLU C OE2 
5979  N N   . PRO C 182 ? 2.2941 1.9868 2.0661 0.0775  0.0036  -0.1588 212 PRO C N   
5980  C CA  . PRO C 182 ? 2.2979 1.9766 2.0589 0.0970  -0.0012 -0.1601 212 PRO C CA  
5981  C C   . PRO C 182 ? 2.3828 2.0486 2.1270 0.0991  0.0098  -0.1609 212 PRO C C   
5982  O O   . PRO C 182 ? 2.4285 2.1095 2.1697 0.0920  0.0213  -0.1601 212 PRO C O   
5983  C CB  . PRO C 182 ? 2.2606 1.9627 2.0302 0.1055  -0.0053 -0.1599 212 PRO C CB  
5984  C CG  . PRO C 182 ? 2.1819 1.9029 1.9660 0.0920  -0.0078 -0.1583 212 PRO C CG  
5985  C CD  . PRO C 182 ? 2.3072 2.0292 2.0931 0.0733  0.0038  -0.1571 212 PRO C CD  
5986  N N   . ILE C 183 ? 2.2921 1.9289 2.0230 0.1078  0.0060  -0.1632 213 ILE C N   
5987  C CA  . ILE C 183 ? 2.3575 1.9747 2.0672 0.1102  0.0142  -0.1639 213 ILE C CA  
5988  C C   . ILE C 183 ? 2.3651 1.9735 2.0667 0.1290  0.0110  -0.1647 213 ILE C C   
5989  O O   . ILE C 183 ? 2.3498 1.9544 2.0581 0.1420  0.0003  -0.1660 213 ILE C O   
5990  C CB  . ILE C 183 ? 2.3289 1.9172 2.0263 0.1064  0.0122  -0.1675 213 ILE C CB  
5991  C CG1 . ILE C 183 ? 2.3109 1.8888 2.0148 0.1161  -0.0008 -0.1730 213 ILE C CG1 
5992  C CG2 . ILE C 183 ? 2.3599 1.9582 2.0631 0.0867  0.0176  -0.1667 213 ILE C CG2 
5993  C CD1 . ILE C 183 ? 2.3711 1.9268 2.0660 0.1139  -0.0049 -0.1810 213 ILE C CD1 
5994  N N   . PRO C 184 ? 2.1410 1.7463 1.8268 0.1291  0.0202  -0.1644 214 PRO C N   
5995  C CA  . PRO C 184 ? 2.1341 1.7350 1.8136 0.1458  0.0181  -0.1656 214 PRO C CA  
5996  C C   . PRO C 184 ? 2.1414 1.7117 1.8135 0.1617  0.0089  -0.1675 214 PRO C C   
5997  O O   . PRO C 184 ? 2.1531 1.6944 1.8097 0.1600  0.0086  -0.1695 214 PRO C O   
5998  C CB  . PRO C 184 ? 2.1717 1.7681 1.8292 0.1362  0.0311  -0.1657 214 PRO C CB  
5999  C CG  . PRO C 184 ? 2.1577 1.7732 1.8180 0.1152  0.0405  -0.1646 214 PRO C CG  
6000  C CD  . PRO C 184 ? 2.1765 1.7847 1.8487 0.1113  0.0336  -0.1632 214 PRO C CD  
6001  N N   . ILE C 185 ? 2.1208 1.6976 1.8030 0.1780  0.0004  -0.1682 215 ILE C N   
6002  C CA  . ILE C 185 ? 2.1221 1.6743 1.7986 0.1939  -0.0079 -0.1708 215 ILE C CA  
6003  C C   . ILE C 185 ? 2.1276 1.6804 1.8007 0.2105  -0.0083 -0.1708 215 ILE C C   
6004  O O   . ILE C 185 ? 2.1187 1.6949 1.8054 0.2175  -0.0126 -0.1702 215 ILE C O   
6005  C CB  . ILE C 185 ? 2.1059 1.6617 1.7962 0.1963  -0.0195 -0.1722 215 ILE C CB  
6006  C CG1 . ILE C 185 ? 2.0997 1.6557 1.7938 0.1791  -0.0193 -0.1738 215 ILE C CG1 
6007  C CG2 . ILE C 185 ? 2.1075 1.6419 1.7912 0.2123  -0.0269 -0.1763 215 ILE C CG2 
6008  C CD1 . ILE C 185 ? 2.0867 1.6462 1.7910 0.1766  -0.0301 -0.1764 215 ILE C CD1 
6009  N N   . HIS C 186 ? 2.2571 1.7840 1.9116 0.2172  -0.0051 -0.1722 216 HIS C N   
6010  C CA  . HIS C 186 ? 2.2496 1.7751 1.9004 0.2327  -0.0052 -0.1726 216 HIS C CA  
6011  C C   . HIS C 186 ? 2.2206 1.7321 1.8756 0.2511  -0.0155 -0.1748 216 HIS C C   
6012  O O   . HIS C 186 ? 2.2339 1.7204 1.8796 0.2537  -0.0184 -0.1786 216 HIS C O   
6013  C CB  . HIS C 186 ? 2.2929 1.7960 1.9183 0.2297  0.0034  -0.1728 216 HIS C CB  
6014  C CG  . HIS C 186 ? 2.3157 1.8280 1.9300 0.2089  0.0146  -0.1712 216 HIS C CG  
6015  N ND1 . HIS C 186 ? 2.3099 1.8446 1.9217 0.2036  0.0226  -0.1719 216 HIS C ND1 
6016  C CD2 . HIS C 186 ? 2.3565 1.8601 1.9605 0.1912  0.0193  -0.1702 216 HIS C CD2 
6017  C CE1 . HIS C 186 ? 2.3294 1.8683 1.9280 0.1822  0.0326  -0.1714 216 HIS C CE1 
6018  N NE2 . HIS C 186 ? 2.3630 1.8820 1.9567 0.1748  0.0307  -0.1695 216 HIS C NE2 
6019  N N   . TYR C 187 ? 2.1908 1.7190 1.8587 0.2640  -0.0215 -0.1741 217 TYR C N   
6020  C CA  . TYR C 187 ? 2.1536 1.6687 1.8231 0.2810  -0.0304 -0.1761 217 TYR C CA  
6021  C C   . TYR C 187 ? 2.1857 1.6881 1.8456 0.2953  -0.0268 -0.1770 217 TYR C C   
6022  O O   . TYR C 187 ? 2.1777 1.6969 1.8402 0.2976  -0.0227 -0.1757 217 TYR C O   
6023  C CB  . TYR C 187 ? 2.1318 1.6658 1.8165 0.2877  -0.0412 -0.1747 217 TYR C CB  
6024  C CG  . TYR C 187 ? 2.1492 1.6829 1.8381 0.2767  -0.0484 -0.1748 217 TYR C CG  
6025  C CD1 . TYR C 187 ? 2.2215 1.7723 1.9175 0.2608  -0.0467 -0.1728 217 TYR C CD1 
6026  C CD2 . TYR C 187 ? 2.0942 1.6118 1.7790 0.2809  -0.0566 -0.1777 217 TYR C CD2 
6027  C CE1 . TYR C 187 ? 2.1698 1.7202 1.8691 0.2492  -0.0534 -0.1729 217 TYR C CE1 
6028  C CE2 . TYR C 187 ? 2.0413 1.5590 1.7274 0.2676  -0.0631 -0.1788 217 TYR C CE2 
6029  C CZ  . TYR C 187 ? 2.0914 1.6249 1.7849 0.2518  -0.0617 -0.1759 217 TYR C CZ  
6030  O OH  . TYR C 187 ? 2.1144 1.6480 1.8086 0.2371  -0.0682 -0.1769 217 TYR C OH  
6031  N N   . CYS C 188 ? 2.1327 1.6079 1.7818 0.3047  -0.0286 -0.1807 218 CYS C N   
6032  C CA  . CYS C 188 ? 2.1478 1.6065 1.7854 0.3184  -0.0254 -0.1819 218 CYS C CA  
6033  C C   . CYS C 188 ? 2.1185 1.5706 1.7613 0.3371  -0.0327 -0.1848 218 CYS C C   
6034  O O   . CYS C 188 ? 2.1440 1.5957 1.7922 0.3372  -0.0396 -0.1878 218 CYS C O   
6035  C CB  . CYS C 188 ? 2.2075 1.6337 1.8215 0.3146  -0.0208 -0.1854 218 CYS C CB  
6036  S SG  . CYS C 188 ? 2.3444 1.7724 1.9468 0.2905  -0.0124 -0.1820 218 CYS C SG  
6037  N N   . ALA C 189 ? 2.0806 1.5280 1.7203 0.3519  -0.0306 -0.1844 219 ALA C N   
6038  C CA  . ALA C 189 ? 2.0503 1.4915 1.6940 0.3706  -0.0361 -0.1870 219 ALA C CA  
6039  C C   . ALA C 189 ? 2.0667 1.4779 1.6937 0.3809  -0.0335 -0.1931 219 ALA C C   
6040  O O   . ALA C 189 ? 2.1011 1.4965 1.7127 0.3785  -0.0274 -0.1927 219 ALA C O   
6041  C CB  . ALA C 189 ? 2.0265 1.4878 1.6825 0.3826  -0.0374 -0.1832 219 ALA C CB  
6042  N N   . PRO C 190 ? 2.0391 1.4407 1.6662 0.3916  -0.0386 -0.1999 220 PRO C N   
6043  C CA  . PRO C 190 ? 2.0703 1.4453 1.6823 0.4039  -0.0375 -0.2087 220 PRO C CA  
6044  C C   . PRO C 190 ? 2.0620 1.4290 1.6699 0.4197  -0.0336 -0.2061 220 PRO C C   
6045  O O   . PRO C 190 ? 2.0312 1.4166 1.6499 0.4213  -0.0317 -0.1981 220 PRO C O   
6046  C CB  . PRO C 190 ? 2.0188 1.3957 1.6354 0.4096  -0.0435 -0.2178 220 PRO C CB  
6047  C CG  . PRO C 190 ? 1.9430 1.3427 1.5751 0.4063  -0.0478 -0.2102 220 PRO C CG  
6048  C CD  . PRO C 190 ? 2.0167 1.4310 1.6549 0.3913  -0.0462 -0.2012 220 PRO C CD  
6049  N N   . ALA C 191 ? 2.1997 1.5403 1.7919 0.4318  -0.0332 -0.2143 221 ALA C N   
6050  C CA  . ALA C 191 ? 2.1377 1.4671 1.7236 0.4466  -0.0296 -0.2124 221 ALA C CA  
6051  C C   . ALA C 191 ? 2.0540 1.4044 1.6596 0.4602  -0.0308 -0.2095 221 ALA C C   
6052  O O   . ALA C 191 ? 2.0344 1.3931 1.6490 0.4644  -0.0355 -0.2141 221 ALA C O   
6053  C CB  . ALA C 191 ? 2.1642 1.4598 1.7290 0.4593  -0.0313 -0.2241 221 ALA C CB  
6054  N N   . GLY C 192 ? 2.2664 1.6251 1.8769 0.4660  -0.0271 -0.2025 222 GLY C N   
6055  C CA  . GLY C 192 ? 2.1552 1.5340 1.7845 0.4798  -0.0291 -0.1996 222 GLY C CA  
6056  C C   . GLY C 192 ? 2.1457 1.5561 1.7938 0.4724  -0.0332 -0.1928 222 GLY C C   
6057  O O   . GLY C 192 ? 2.0954 1.5236 1.7586 0.4840  -0.0365 -0.1901 222 GLY C O   
6058  N N   . PHE C 193 ? 2.1537 1.5710 1.8012 0.4546  -0.0342 -0.1911 223 PHE C N   
6059  C CA  . PHE C 193 ? 2.0850 1.5308 1.7478 0.4466  -0.0391 -0.1864 223 PHE C CA  
6060  C C   . PHE C 193 ? 2.1198 1.5780 1.7804 0.4317  -0.0326 -0.1836 223 PHE C C   
6061  O O   . PHE C 193 ? 2.2129 1.6522 1.8559 0.4244  -0.0250 -0.1843 223 PHE C O   
6062  C CB  . PHE C 193 ? 2.0513 1.4959 1.7145 0.4368  -0.0457 -0.1878 223 PHE C CB  
6063  C CG  . PHE C 193 ? 2.0271 1.4631 1.6902 0.4475  -0.0522 -0.1915 223 PHE C CG  
6064  C CD1 . PHE C 193 ? 2.0378 1.4523 1.6888 0.4513  -0.0495 -0.1996 223 PHE C CD1 
6065  C CD2 . PHE C 193 ? 1.9422 1.3911 1.6149 0.4535  -0.0619 -0.1885 223 PHE C CD2 
6066  C CE1 . PHE C 193 ? 2.0306 1.4401 1.6798 0.4588  -0.0542 -0.2050 223 PHE C CE1 
6067  C CE2 . PHE C 193 ? 1.9608 1.3991 1.6285 0.4605  -0.0675 -0.1920 223 PHE C CE2 
6068  C CZ  . PHE C 193 ? 1.9680 1.3883 1.6242 0.4620  -0.0626 -0.2004 223 PHE C CZ  
6069  N N   . ALA C 194 ? 1.9192 1.4084 1.5951 0.4270  -0.0364 -0.1816 224 ALA C N   
6070  C CA  . ALA C 194 ? 1.9283 1.4363 1.6032 0.4111  -0.0299 -0.1813 224 ALA C CA  
6071  C C   . ALA C 194 ? 1.9198 1.4583 1.6110 0.4056  -0.0372 -0.1816 224 ALA C C   
6072  O O   . ALA C 194 ? 1.9087 1.4551 1.6120 0.4174  -0.0486 -0.1816 224 ALA C O   
6073  C CB  . ALA C 194 ? 1.9314 1.4531 1.6079 0.4157  -0.0242 -0.1828 224 ALA C CB  
6074  N N   . ILE C 195 ? 1.9681 1.5215 1.6566 0.3873  -0.0312 -0.1824 225 ILE C N   
6075  C CA  . ILE C 195 ? 1.9598 1.5441 1.6628 0.3813  -0.0373 -0.1844 225 ILE C CA  
6076  C C   . ILE C 195 ? 1.9616 1.5837 1.6732 0.3773  -0.0330 -0.1905 225 ILE C C   
6077  O O   . ILE C 195 ? 2.0954 1.7180 1.7938 0.3613  -0.0204 -0.1917 225 ILE C O   
6078  C CB  . ILE C 195 ? 1.9865 1.5621 1.6813 0.3618  -0.0336 -0.1821 225 ILE C CB  
6079  C CG1 . ILE C 195 ? 1.9903 1.5328 1.6769 0.3637  -0.0377 -0.1790 225 ILE C CG1 
6080  C CG2 . ILE C 195 ? 1.9599 1.5678 1.6696 0.3565  -0.0401 -0.1847 225 ILE C CG2 
6081  C CD1 . ILE C 195 ? 2.0220 1.5578 1.7026 0.3449  -0.0350 -0.1777 225 ILE C CD1 
6082  N N   . LEU C 196 ? 1.8723 1.5256 1.6035 0.3912  -0.0441 -0.1959 226 LEU C N   
6083  C CA  . LEU C 196 ? 1.8721 1.5694 1.6149 0.3889  -0.0419 -0.2060 226 LEU C CA  
6084  C C   . LEU C 196 ? 1.8738 1.5993 1.6226 0.3754  -0.0427 -0.2115 226 LEU C C   
6085  O O   . LEU C 196 ? 1.8702 1.5887 1.6228 0.3780  -0.0527 -0.2086 226 LEU C O   
6086  C CB  . LEU C 196 ? 1.8604 1.5798 1.6223 0.4130  -0.0555 -0.2119 226 LEU C CB  
6087  C CG  . LEU C 196 ? 1.8564 1.5473 1.6138 0.4279  -0.0552 -0.2059 226 LEU C CG  
6088  C CD1 . LEU C 196 ? 1.8450 1.5589 1.6215 0.4514  -0.0685 -0.2118 226 LEU C CD1 
6089  C CD2 . LEU C 196 ? 1.8665 1.5450 1.6082 0.4153  -0.0383 -0.2043 226 LEU C CD2 
6090  N N   . LYS C 197 ? 1.9258 1.6830 1.6736 0.3596  -0.0319 -0.2201 227 LYS C N   
6091  C CA  . LYS C 197 ? 1.9260 1.7143 1.6790 0.3453  -0.0303 -0.2273 227 LYS C CA  
6092  C C   . LYS C 197 ? 1.9469 1.7930 1.7167 0.3478  -0.0323 -0.2452 227 LYS C C   
6093  O O   . LYS C 197 ? 2.0590 1.9211 1.8236 0.3391  -0.0217 -0.2516 227 LYS C O   
6094  C CB  . LYS C 197 ? 1.9902 1.7604 1.7208 0.3174  -0.0128 -0.2221 227 LYS C CB  
6095  C CG  . LYS C 197 ? 2.1182 1.9188 1.8530 0.3009  -0.0091 -0.2288 227 LYS C CG  
6096  C CD  . LYS C 197 ? 2.1707 1.9473 1.8810 0.2740  0.0071  -0.2220 227 LYS C CD  
6097  C CE  . LYS C 197 ? 2.1373 1.9454 1.8368 0.2515  0.0220  -0.2327 227 LYS C CE  
6098  N NZ  . LYS C 197 ? 2.2764 2.0846 1.9634 0.2269  0.0327  -0.2314 227 LYS C NZ  
6099  N N   . CYS C 198 ? 1.9186 1.7963 1.7069 0.3589  -0.0467 -0.2550 228 CYS C N   
6100  C CA  . CYS C 198 ? 1.9156 1.8540 1.7221 0.3634  -0.0513 -0.2763 228 CYS C CA  
6101  C C   . CYS C 198 ? 1.9237 1.8943 1.7244 0.3361  -0.0356 -0.2860 228 CYS C C   
6102  O O   . CYS C 198 ? 1.9251 1.8894 1.7229 0.3272  -0.0350 -0.2823 228 CYS C O   
6103  C CB  . CYS C 198 ? 1.9088 1.8631 1.7339 0.3884  -0.0758 -0.2840 228 CYS C CB  
6104  S SG  . CYS C 198 ? 1.9033 1.9229 1.7545 0.4103  -0.0923 -0.3112 228 CYS C SG  
6105  N N   . LYS C 199 ? 2.1730 2.1784 1.9706 0.3211  -0.0225 -0.2990 229 LYS C N   
6106  C CA  . LYS C 199 ? 2.1895 2.2243 1.9765 0.2911  -0.0053 -0.3089 229 LYS C CA  
6107  C C   . LYS C 199 ? 2.2040 2.3142 2.0108 0.2919  -0.0084 -0.3376 229 LYS C C   
6108  O O   . LYS C 199 ? 2.2215 2.3644 2.0174 0.2651  0.0086  -0.3503 229 LYS C O   
6109  C CB  . LYS C 199 ? 2.2006 2.2064 1.9557 0.2618  0.0167  -0.2997 229 LYS C CB  
6110  C CG  . LYS C 199 ? 2.2040 2.1942 1.9472 0.2610  0.0223  -0.2969 229 LYS C CG  
6111  C CD  . LYS C 199 ? 2.2190 2.1540 1.9240 0.2358  0.0388  -0.2805 229 LYS C CD  
6112  C CE  . LYS C 199 ? 2.2338 2.1510 1.9173 0.2265  0.0477  -0.2788 229 LYS C CE  
6113  N NZ  . LYS C 199 ? 2.2531 2.2287 1.9377 0.2086  0.0563  -0.3004 229 LYS C NZ  
6114  N N   . ASP C 200 ? 2.4590 2.5980 2.2925 0.3216  -0.0305 -0.3501 230 ASP C N   
6115  C CA  . ASP C 200 ? 2.5017 2.7157 2.3555 0.3249  -0.0362 -0.3810 230 ASP C CA  
6116  C C   . ASP C 200 ? 2.4857 2.7189 2.3438 0.3201  -0.0385 -0.3884 230 ASP C C   
6117  O O   . ASP C 200 ? 2.4775 2.6690 2.3316 0.3267  -0.0456 -0.3712 230 ASP C O   
6118  C CB  . ASP C 200 ? 2.4838 2.7241 2.3636 0.3606  -0.0613 -0.3953 230 ASP C CB  
6119  C CG  . ASP C 200 ? 2.4724 2.6654 2.3564 0.3897  -0.0840 -0.3790 230 ASP C CG  
6120  O OD1 . ASP C 200 ? 2.4664 2.6133 2.3366 0.3823  -0.0810 -0.3592 230 ASP C OD1 
6121  O OD2 . ASP C 200 ? 2.4977 2.7019 2.3982 0.4193  -0.1060 -0.3878 230 ASP C OD2 
6122  N N   . LYS C 201 ? 2.5037 2.8030 2.3698 0.3072  -0.0319 -0.4155 231 LYS C N   
6123  C CA  . LYS C 201 ? 2.5140 2.8349 2.3827 0.2994  -0.0307 -0.4237 231 LYS C CA  
6124  C C   . LYS C 201 ? 2.5214 2.8563 2.4128 0.3338  -0.0597 -0.4343 231 LYS C C   
6125  O O   . LYS C 201 ? 2.5617 2.8955 2.4534 0.3315  -0.0620 -0.4336 231 LYS C O   
6126  C CB  . LYS C 201 ? 2.5368 2.9246 2.4035 0.2716  -0.0120 -0.4507 231 LYS C CB  
6127  C CG  . LYS C 201 ? 2.5386 2.8993 2.3754 0.2376  0.0140  -0.4373 231 LYS C CG  
6128  C CD  . LYS C 201 ? 2.5587 2.9268 2.3708 0.1972  0.0395  -0.4385 231 LYS C CD  
6129  C CE  . LYS C 201 ? 2.5543 2.8762 2.3318 0.1702  0.0587  -0.4205 231 LYS C CE  
6130  N NZ  . LYS C 201 ? 2.5346 2.7737 2.2997 0.1807  0.0544  -0.3862 231 LYS C NZ  
6131  N N   . LYS C 202 ? 2.4619 2.8097 2.3705 0.3653  -0.0828 -0.4451 232 LYS C N   
6132  C CA  . LYS C 202 ? 2.4784 2.8295 2.4024 0.3997  -0.1140 -0.4543 232 LYS C CA  
6133  C C   . LYS C 202 ? 2.4705 2.7633 2.3914 0.4252  -0.1328 -0.4334 232 LYS C C   
6134  O O   . LYS C 202 ? 2.4679 2.7701 2.3966 0.4381  -0.1384 -0.4386 232 LYS C O   
6135  C CB  . LYS C 202 ? 2.5325 2.9627 2.4802 0.4176  -0.1300 -0.4947 232 LYS C CB  
6136  C CG  . LYS C 202 ? 2.5273 3.0048 2.4887 0.4232  -0.1307 -0.5158 232 LYS C CG  
6137  C CD  . LYS C 202 ? 2.5866 3.1455 2.5720 0.4414  -0.1488 -0.5592 232 LYS C CD  
6138  C CE  . LYS C 202 ? 2.5610 3.1971 2.5519 0.4126  -0.1258 -0.5887 232 LYS C CE  
6139  N NZ  . LYS C 202 ? 2.6340 3.2839 2.6268 0.4043  -0.1161 -0.5909 232 LYS C NZ  
6140  N N   . PHE C 203 ? 2.4040 2.6378 2.3128 0.4304  -0.1413 -0.4100 233 PHE C N   
6141  C CA  . PHE C 203 ? 2.3999 2.5744 2.3011 0.4505  -0.1574 -0.3892 233 PHE C CA  
6142  C C   . PHE C 203 ? 2.4145 2.5455 2.3057 0.4601  -0.1753 -0.3766 233 PHE C C   
6143  O O   . PHE C 203 ? 2.4016 2.5080 2.2813 0.4387  -0.1615 -0.3616 233 PHE C O   
6144  C CB  . PHE C 203 ? 2.3683 2.4983 2.2542 0.4315  -0.1351 -0.3640 233 PHE C CB  
6145  C CG  . PHE C 203 ? 2.3634 2.4398 2.2424 0.4508  -0.1490 -0.3458 233 PHE C CG  
6146  C CD1 . PHE C 203 ? 2.3750 2.4652 2.2660 0.4780  -0.1681 -0.3566 233 PHE C CD1 
6147  C CD2 . PHE C 203 ? 2.3477 2.3621 2.2083 0.4413  -0.1429 -0.3192 233 PHE C CD2 
6148  C CE1 . PHE C 203 ? 2.3717 2.4123 2.2545 0.4946  -0.1799 -0.3400 233 PHE C CE1 
6149  C CE2 . PHE C 203 ? 2.3449 2.3127 2.1977 0.4572  -0.1544 -0.3043 233 PHE C CE2 
6150  C CZ  . PHE C 203 ? 2.3572 2.3369 2.2203 0.4835  -0.1725 -0.3140 233 PHE C CZ  
6151  N N   . ASN C 204 ? 2.4476 2.5668 2.3407 0.4913  -0.2068 -0.3827 234 ASN C N   
6152  C CA  . ASN C 204 ? 2.4721 2.5481 2.3514 0.5011  -0.2277 -0.3727 234 ASN C CA  
6153  C C   . ASN C 204 ? 2.4608 2.4637 2.3194 0.4982  -0.2287 -0.3428 234 ASN C C   
6154  O O   . ASN C 204 ? 2.4895 2.4513 2.3330 0.5101  -0.2512 -0.3353 234 ASN C O   
6155  C CB  . ASN C 204 ? 2.5226 2.6140 2.4072 0.5360  -0.2645 -0.3944 234 ASN C CB  
6156  C CG  . ASN C 204 ? 2.5315 2.6222 2.4215 0.5605  -0.2799 -0.3996 234 ASN C CG  
6157  O OD1 . ASN C 204 ? 2.4985 2.5755 2.3885 0.5516  -0.2627 -0.3858 234 ASN C OD1 
6158  N ND2 . ASN C 204 ? 2.5797 2.6819 2.4729 0.5928  -0.3140 -0.4194 234 ASN C ND2 
6159  N N   . GLY C 205 ? 2.2912 2.2764 2.1463 0.4825  -0.2057 -0.3271 235 GLY C N   
6160  C CA  . GLY C 205 ? 2.2802 2.2014 2.1163 0.4782  -0.2046 -0.3017 235 GLY C CA  
6161  C C   . GLY C 205 ? 2.2957 2.1898 2.1268 0.5024  -0.2236 -0.2982 235 GLY C C   
6162  O O   . GLY C 205 ? 2.2833 2.1302 2.0999 0.4973  -0.2186 -0.2790 235 GLY C O   
6163  N N   . THR C 206 ? 2.3407 2.2637 2.1830 0.5288  -0.2460 -0.3173 236 THR C N   
6164  C CA  . THR C 206 ? 2.3589 2.2560 2.1957 0.5532  -0.2662 -0.3148 236 THR C CA  
6165  C C   . THR C 206 ? 2.3524 2.3011 2.2126 0.5693  -0.2675 -0.3343 236 THR C C   
6166  O O   . THR C 206 ? 2.3651 2.3703 2.2432 0.5751  -0.2722 -0.3584 236 THR C O   
6167  C CB  . THR C 206 ? 2.4162 2.2851 2.2370 0.5744  -0.3018 -0.3187 236 THR C CB  
6168  O OG1 . THR C 206 ? 2.4422 2.3566 2.2753 0.5835  -0.3147 -0.3422 236 THR C OG1 
6169  C CG2 . THR C 206 ? 2.4255 2.2348 2.2190 0.5578  -0.3019 -0.2970 236 THR C CG2 
6170  N N   . GLY C 207 ? 2.1251 2.0570 1.9855 0.5760  -0.2635 -0.3254 237 GLY C N   
6171  C CA  . GLY C 207 ? 2.1131 2.0916 1.9956 0.5904  -0.2646 -0.3425 237 GLY C CA  
6172  C C   . GLY C 207 ? 2.0923 2.0838 1.9822 0.5709  -0.2333 -0.3357 237 GLY C C   
6173  O O   . GLY C 207 ? 2.0877 2.0493 1.9647 0.5470  -0.2104 -0.3172 237 GLY C O   
6174  N N   . PRO C 208 ? 2.0506 2.0866 1.9606 0.5815  -0.2335 -0.3518 238 PRO C N   
6175  C CA  . PRO C 208 ? 2.0134 2.0630 1.9285 0.5631  -0.2054 -0.3472 238 PRO C CA  
6176  C C   . PRO C 208 ? 2.0031 2.0876 1.9193 0.5331  -0.1816 -0.3548 238 PRO C C   
6177  O O   . PRO C 208 ? 2.0228 2.1519 1.9489 0.5325  -0.1880 -0.3752 238 PRO C O   
6178  C CB  . PRO C 208 ? 2.0153 2.1080 1.9527 0.5847  -0.2173 -0.3660 238 PRO C CB  
6179  C CG  . PRO C 208 ? 2.0544 2.1824 2.0038 0.6074  -0.2464 -0.3901 238 PRO C CG  
6180  C CD  . PRO C 208 ? 2.0800 2.1542 2.0075 0.6120  -0.2615 -0.3757 238 PRO C CD  
6181  N N   . CYS C 209 ? 2.1452 2.2075 2.0487 0.5082  -0.1545 -0.3391 239 CYS C N   
6182  C CA  . CYS C 209 ? 2.1401 2.2268 2.0380 0.4768  -0.1307 -0.3437 239 CYS C CA  
6183  C C   . CYS C 209 ? 2.1280 2.2484 2.0304 0.4631  -0.1130 -0.3531 239 CYS C C   
6184  O O   . CYS C 209 ? 2.1107 2.2000 2.0055 0.4626  -0.1043 -0.3389 239 CYS C O   
6185  C CB  . CYS C 209 ? 2.1293 2.1595 2.0029 0.4559  -0.1147 -0.3192 239 CYS C CB  
6186  S SG  . CYS C 209 ? 2.1297 2.1767 1.9892 0.4155  -0.0851 -0.3209 239 CYS C SG  
6187  N N   . PRO C 210 ? 2.2279 2.4128 2.1415 0.4509  -0.1074 -0.3780 240 PRO C N   
6188  C CA  . PRO C 210 ? 2.2220 2.4414 2.1370 0.4337  -0.0904 -0.3887 240 PRO C CA  
6189  C C   . PRO C 210 ? 2.2145 2.3954 2.1005 0.4011  -0.0627 -0.3703 240 PRO C C   
6190  O O   . PRO C 210 ? 2.2033 2.3673 2.0826 0.3978  -0.0540 -0.3625 240 PRO C O   
6191  C CB  . PRO C 210 ? 2.2423 2.5405 2.1731 0.4255  -0.0914 -0.4218 240 PRO C CB  
6192  C CG  . PRO C 210 ? 2.2580 2.5661 2.2039 0.4531  -0.1179 -0.4313 240 PRO C CG  
6193  C CD  . PRO C 210 ? 2.2504 2.4837 2.1775 0.4557  -0.1197 -0.4009 240 PRO C CD  
6194  N N   . SER C 211 ? 2.2579 2.4230 2.1254 0.3775  -0.0499 -0.3635 241 SER C N   
6195  C CA  . SER C 211 ? 2.2601 2.3861 2.0958 0.3460  -0.0257 -0.3475 241 SER C CA  
6196  C C   . SER C 211 ? 2.2492 2.3033 2.0683 0.3500  -0.0264 -0.3202 241 SER C C   
6197  O O   . SER C 211 ? 2.2532 2.2967 2.0668 0.3424  -0.0259 -0.3157 241 SER C O   
6198  C CB  . SER C 211 ? 2.2825 2.4455 2.1067 0.3133  -0.0095 -0.3618 241 SER C CB  
6199  O OG  . SER C 211 ? 2.2704 2.5052 2.1096 0.3073  -0.0084 -0.3904 241 SER C OG  
6200  N N   . VAL C 212 ? 2.0351 2.0431 1.8469 0.3614  -0.0272 -0.3037 242 VAL C N   
6201  C CA  . VAL C 212 ? 2.0365 1.9791 1.8335 0.3670  -0.0284 -0.2807 242 VAL C CA  
6202  C C   . VAL C 212 ? 2.0540 1.9521 1.8197 0.3453  -0.0097 -0.2673 242 VAL C C   
6203  O O   . VAL C 212 ? 2.0610 1.9626 1.8185 0.3384  -0.0011 -0.2702 242 VAL C O   
6204  C CB  . VAL C 212 ? 2.0220 1.9435 1.8328 0.3990  -0.0456 -0.2736 242 VAL C CB  
6205  C CG1 . VAL C 212 ? 2.0237 1.8834 1.8193 0.4027  -0.0470 -0.2531 242 VAL C CG1 
6206  C CG2 . VAL C 212 ? 2.0108 1.9725 1.8481 0.4218  -0.0671 -0.2880 242 VAL C CG2 
6207  N N   . SER C 213 ? 1.9748 1.8306 1.7218 0.3344  -0.0047 -0.2537 243 SER C N   
6208  C CA  . SER C 213 ? 1.9947 1.8000 1.7094 0.3177  0.0090  -0.2410 243 SER C CA  
6209  C C   . SER C 213 ? 1.9898 1.7435 1.6996 0.3309  0.0022  -0.2255 243 SER C C   
6210  O O   . SER C 213 ? 1.9761 1.7334 1.7015 0.3426  -0.0093 -0.2239 243 SER C O   
6211  C CB  . SER C 213 ? 2.0174 1.8249 1.7080 0.2845  0.0243  -0.2434 243 SER C CB  
6212  O OG  . SER C 213 ? 2.0122 1.8248 1.7090 0.2802  0.0215  -0.2422 243 SER C OG  
6213  N N   . THR C 214 ? 1.9997 1.7055 1.6861 0.3286  0.0084  -0.2155 244 THR C N   
6214  C CA  . THR C 214 ? 1.9967 1.6555 1.6764 0.3399  0.0031  -0.2040 244 THR C CA  
6215  C C   . THR C 214 ? 2.0184 1.6405 1.6695 0.3191  0.0120  -0.1977 244 THR C C   
6216  O O   . THR C 214 ? 2.0427 1.6567 1.6691 0.2983  0.0234  -0.1989 244 THR C O   
6217  C CB  . THR C 214 ? 1.9936 1.6244 1.6703 0.3587  0.0004  -0.1995 244 THR C CB  
6218  O OG1 . THR C 214 ? 1.9926 1.5808 1.6608 0.3669  -0.0038 -0.1914 244 THR C OG1 
6219  C CG2 . THR C 214 ? 2.0165 1.6307 1.6680 0.3459  0.0121  -0.1998 244 THR C CG2 
6220  N N   . VAL C 215 ? 2.1043 1.7037 1.7571 0.3239  0.0060  -0.1918 245 VAL C N   
6221  C CA  . VAL C 215 ? 2.1365 1.7004 1.7650 0.3078  0.0117  -0.1868 245 VAL C CA  
6222  C C   . VAL C 215 ? 2.1563 1.6841 1.7838 0.3232  0.0038  -0.1820 245 VAL C C   
6223  O O   . VAL C 215 ? 2.1268 1.6615 1.7735 0.3423  -0.0057 -0.1820 245 VAL C O   
6224  C CB  . VAL C 215 ? 2.1346 1.7201 1.7685 0.2903  0.0139  -0.1879 245 VAL C CB  
6225  C CG1 . VAL C 215 ? 2.1233 1.7424 1.7521 0.2706  0.0242  -0.1948 245 VAL C CG1 
6226  C CG2 . VAL C 215 ? 2.0965 1.7062 1.7597 0.3040  0.0018  -0.1887 245 VAL C CG2 
6227  N N   . GLN C 216 ? 2.2851 1.7743 1.8879 0.3138  0.0072  -0.1794 246 GLN C N   
6228  C CA  . GLN C 216 ? 2.3082 1.7663 1.9084 0.3259  0.0002  -0.1785 246 GLN C CA  
6229  C C   . GLN C 216 ? 2.3199 1.7877 1.9314 0.3172  -0.0036 -0.1778 246 GLN C C   
6230  O O   . GLN C 216 ? 2.2908 1.7568 1.9150 0.3278  -0.0119 -0.1786 246 GLN C O   
6231  C CB  . GLN C 216 ? 2.3676 1.7785 1.9347 0.3233  0.0031  -0.1789 246 GLN C CB  
6232  C CG  . GLN C 216 ? 2.3784 1.7599 1.9426 0.3388  -0.0047 -0.1823 246 GLN C CG  
6233  C CD  . GLN C 216 ? 2.3557 1.7422 1.9350 0.3621  -0.0094 -0.1839 246 GLN C CD  
6234  O OE1 . GLN C 216 ? 2.3798 1.7779 1.9628 0.3681  -0.0064 -0.1823 246 GLN C OE1 
6235  N NE2 . GLN C 216 ? 2.3042 1.6825 1.8909 0.3740  -0.0165 -0.1882 246 GLN C NE2 
6236  N N   . CYS C 217 ? 2.4012 1.8805 2.0070 0.2964  0.0029  -0.1769 247 CYS C N   
6237  C CA  . CYS C 217 ? 2.3910 1.8826 2.0070 0.2848  0.0012  -0.1760 247 CYS C CA  
6238  C C   . CYS C 217 ? 2.3529 1.8861 1.9823 0.2727  0.0055  -0.1769 247 CYS C C   
6239  O O   . CYS C 217 ? 2.3607 1.9044 1.9788 0.2609  0.0147  -0.1787 247 CYS C O   
6240  C CB  . CYS C 217 ? 2.4054 1.8660 1.9985 0.2702  0.0048  -0.1755 247 CYS C CB  
6241  S SG  . CYS C 217 ? 2.5791 1.9917 2.1533 0.2849  -0.0015 -0.1790 247 CYS C SG  
6242  N N   . THR C 218 ? 2.0141 1.5705 1.6657 0.2753  -0.0018 -0.1770 248 THR C N   
6243  C CA  . THR C 218 ? 2.0068 1.6038 1.6736 0.2667  -0.0004 -0.1798 248 THR C CA  
6244  C C   . THR C 218 ? 2.0181 1.6157 1.6732 0.2426  0.0099  -0.1789 248 THR C C   
6245  O O   . THR C 218 ? 2.0298 1.5950 1.6673 0.2339  0.0132  -0.1755 248 THR C O   
6246  C CB  . THR C 218 ? 1.9877 1.5994 1.6760 0.2767  -0.0136 -0.1796 248 THR C CB  
6247  O OG1 . THR C 218 ? 1.9850 1.5769 1.6702 0.2680  -0.0155 -0.1758 248 THR C OG1 
6248  C CG2 . THR C 218 ? 1.9797 1.5836 1.6749 0.2995  -0.0246 -0.1797 248 THR C CG2 
6249  N N   . HIS C 219 ? 2.1847 1.8210 1.8498 0.2324  0.0144  -0.1834 249 HIS C N   
6250  C CA  . HIS C 219 ? 2.1850 1.8279 1.8410 0.2088  0.0250  -0.1833 249 HIS C CA  
6251  C C   . HIS C 219 ? 2.1773 1.8119 1.8429 0.2055  0.0193  -0.1787 249 HIS C C   
6252  O O   . HIS C 219 ? 2.1858 1.8162 1.8658 0.2197  0.0071  -0.1770 249 HIS C O   
6253  C CB  . HIS C 219 ? 2.1622 1.8544 1.8285 0.2000  0.0310  -0.1921 249 HIS C CB  
6254  C CG  . HIS C 219 ? 2.1276 1.8545 1.8230 0.2132  0.0193  -0.1968 249 HIS C CG  
6255  N ND1 . HIS C 219 ? 2.0954 1.8406 1.8064 0.2346  0.0080  -0.2024 249 HIS C ND1 
6256  C CD2 . HIS C 219 ? 2.1125 1.8558 1.8218 0.2086  0.0155  -0.1969 249 HIS C CD2 
6257  C CE1 . HIS C 219 ? 2.0640 1.8327 1.7947 0.2430  -0.0034 -0.2061 249 HIS C CE1 
6258  N NE2 . HIS C 219 ? 2.0737 1.8418 1.8038 0.2273  0.0012  -0.2027 249 HIS C NE2 
6259  N N   . GLY C 220 ? 2.2676 1.8995 1.9233 0.1848  0.0283  -0.1770 250 GLY C N   
6260  C CA  . GLY C 220 ? 2.2304 1.8572 1.8950 0.1782  0.0246  -0.1734 250 GLY C CA  
6261  C C   . GLY C 220 ? 2.2522 1.9126 1.9433 0.1821  0.0169  -0.1751 250 GLY C C   
6262  O O   . GLY C 220 ? 2.2489 1.9426 1.9477 0.1722  0.0228  -0.1790 250 GLY C O   
6263  N N   . ILE C 221 ? 2.0519 1.7026 1.7543 0.1958  0.0033  -0.1731 251 ILE C N   
6264  C CA  . ILE C 221 ? 2.0375 1.7101 1.7593 0.2006  -0.0077 -0.1741 251 ILE C CA  
6265  C C   . ILE C 221 ? 2.0293 1.6916 1.7548 0.1881  -0.0103 -0.1700 251 ILE C C   
6266  O O   . ILE C 221 ? 2.0274 1.6636 1.7486 0.1906  -0.0165 -0.1679 251 ILE C O   
6267  C CB  . ILE C 221 ? 2.0340 1.7022 1.7615 0.2227  -0.0225 -0.1752 251 ILE C CB  
6268  C CG1 . ILE C 221 ? 2.0399 1.7250 1.7672 0.2344  -0.0200 -0.1808 251 ILE C CG1 
6269  C CG2 . ILE C 221 ? 2.0263 1.7092 1.7671 0.2268  -0.0363 -0.1761 251 ILE C CG2 
6270  C CD1 . ILE C 221 ? 2.0369 1.7206 1.7706 0.2575  -0.0349 -0.1827 251 ILE C CD1 
6271  N N   . LYS C 222 ? 2.0662 1.7522 1.8003 0.1741  -0.0054 -0.1704 252 LYS C N   
6272  C CA  . LYS C 222 ? 2.0569 1.7392 1.7970 0.1601  -0.0069 -0.1671 252 LYS C CA  
6273  C C   . LYS C 222 ? 2.0587 1.7409 1.8086 0.1676  -0.0234 -0.1664 252 LYS C C   
6274  O O   . LYS C 222 ? 2.0488 1.7512 1.8067 0.1765  -0.0310 -0.1692 252 LYS C O   
6275  C CB  . LYS C 222 ? 2.0537 1.7638 1.8003 0.1434  0.0040  -0.1680 252 LYS C CB  
6276  C CG  . LYS C 222 ? 2.0659 1.7736 1.7978 0.1301  0.0207  -0.1683 252 LYS C CG  
6277  C CD  . LYS C 222 ? 2.0619 1.8022 1.8012 0.1137  0.0314  -0.1704 252 LYS C CD  
6278  C CE  . LYS C 222 ? 2.0782 1.8313 1.8026 0.1054  0.0463  -0.1750 252 LYS C CE  
6279  N NZ  . LYS C 222 ? 2.0809 1.8554 1.8093 0.1209  0.0424  -0.1826 252 LYS C NZ  
6280  N N   . PRO C 223 ? 2.0905 1.7501 1.8375 0.1637  -0.0304 -0.1642 253 PRO C N   
6281  C CA  . PRO C 223 ? 2.0857 1.7412 1.8359 0.1668  -0.0464 -0.1634 253 PRO C CA  
6282  C C   . PRO C 223 ? 2.0880 1.7622 1.8487 0.1529  -0.0484 -0.1621 253 PRO C C   
6283  O O   . PRO C 223 ? 2.0923 1.7597 1.8543 0.1378  -0.0505 -0.1605 253 PRO C O   
6284  C CB  . PRO C 223 ? 2.0815 1.7103 1.8234 0.1624  -0.0501 -0.1639 253 PRO C CB  
6285  C CG  . PRO C 223 ? 2.0412 1.6674 1.7819 0.1510  -0.0365 -0.1650 253 PRO C CG  
6286  C CD  . PRO C 223 ? 2.0476 1.6842 1.7859 0.1562  -0.0252 -0.1643 253 PRO C CD  
6287  N N   . VAL C 224 ? 2.2696 1.9697 2.0380 0.1579  -0.0478 -0.1644 254 VAL C N   
6288  C CA  . VAL C 224 ? 2.2175 1.9377 1.9962 0.1472  -0.0499 -0.1643 254 VAL C CA  
6289  C C   . VAL C 224 ? 2.2287 1.9383 2.0033 0.1554  -0.0710 -0.1642 254 VAL C C   
6290  O O   . VAL C 224 ? 2.1868 1.8998 1.9588 0.1745  -0.0824 -0.1683 254 VAL C O   
6291  C CB  . VAL C 224 ? 2.1527 1.9083 1.9405 0.1486  -0.0396 -0.1697 254 VAL C CB  
6292  C CG1 . VAL C 224 ? 2.1562 1.9334 1.9550 0.1399  -0.0428 -0.1710 254 VAL C CG1 
6293  C CG2 . VAL C 224 ? 2.1387 1.8987 1.9237 0.1367  -0.0191 -0.1691 254 VAL C CG2 
6294  N N   . VAL C 225 ? 2.1473 1.8431 1.9193 0.1403  -0.0774 -0.1604 255 VAL C N   
6295  C CA  . VAL C 225 ? 2.1246 1.8033 1.8859 0.1431  -0.0983 -0.1594 255 VAL C CA  
6296  C C   . VAL C 225 ? 2.1090 1.8096 1.8788 0.1412  -0.1029 -0.1613 255 VAL C C   
6297  O O   . VAL C 225 ? 2.0986 1.8125 1.8784 0.1225  -0.0944 -0.1592 255 VAL C O   
6298  C CB  . VAL C 225 ? 2.1804 1.8347 1.9319 0.1244  -0.1028 -0.1560 255 VAL C CB  
6299  C CG1 . VAL C 225 ? 2.2469 1.8781 1.9803 0.1248  -0.1252 -0.1547 255 VAL C CG1 
6300  C CG2 . VAL C 225 ? 2.1888 1.8264 1.9338 0.1268  -0.0969 -0.1570 255 VAL C CG2 
6301  N N   . SER C 226 ? 1.9358 1.6417 1.7023 0.1615  -0.1170 -0.1665 256 SER C N   
6302  C CA  . SER C 226 ? 1.9392 1.6665 1.7127 0.1633  -0.1237 -0.1712 256 SER C CA  
6303  C C   . SER C 226 ? 1.9651 1.6787 1.7244 0.1862  -0.1498 -0.1767 256 SER C C   
6304  O O   . SER C 226 ? 1.9774 1.6714 1.7249 0.2018  -0.1595 -0.1773 256 SER C O   
6305  C CB  . SER C 226 ? 1.9232 1.6945 1.7165 0.1645  -0.1048 -0.1781 256 SER C CB  
6306  O OG  . SER C 226 ? 1.9264 1.7096 1.7207 0.1834  -0.1024 -0.1851 256 SER C OG  
6307  N N   . THR C 227 ? 1.8594 1.5823 1.6191 0.1887  -0.1621 -0.1813 257 THR C N   
6308  C CA  . THR C 227 ? 1.8884 1.5977 1.6328 0.2119  -0.1900 -0.1887 257 THR C CA  
6309  C C   . THR C 227 ? 1.8848 1.6386 1.6465 0.2267  -0.1898 -0.2033 257 THR C C   
6310  O O   . THR C 227 ? 1.8624 1.6523 1.6443 0.2139  -0.1695 -0.2055 257 THR C O   
6311  C CB  . THR C 227 ? 1.9144 1.5823 1.6335 0.2022  -0.2123 -0.1823 257 THR C CB  
6312  O OG1 . THR C 227 ? 1.9021 1.5854 1.6318 0.1817  -0.2038 -0.1799 257 THR C OG1 
6313  C CG2 . THR C 227 ? 1.9216 1.5477 1.6205 0.1876  -0.2141 -0.1714 257 THR C CG2 
6314  N N   . GLN C 228 ? 2.0118 1.7637 1.7645 0.2542  -0.2134 -0.2148 258 GLN C N   
6315  C CA  . GLN C 228 ? 1.9945 1.7899 1.7616 0.2729  -0.2186 -0.2335 258 GLN C CA  
6316  C C   . GLN C 228 ? 1.9721 1.8223 1.7657 0.2720  -0.1915 -0.2432 258 GLN C C   
6317  O O   . GLN C 228 ? 1.9942 1.8704 1.7941 0.2938  -0.1967 -0.2584 258 GLN C O   
6318  C CB  . GLN C 228 ? 2.0063 1.8069 1.7740 0.2633  -0.2242 -0.2350 258 GLN C CB  
6319  C CG  . GLN C 228 ? 2.0733 1.8199 1.8098 0.2652  -0.2549 -0.2287 258 GLN C CG  
6320  C CD  . GLN C 228 ? 2.0981 1.8505 1.8352 0.2559  -0.2605 -0.2306 258 GLN C CD  
6321  O OE1 . GLN C 228 ? 2.0814 1.8796 1.8443 0.2467  -0.2395 -0.2358 258 GLN C OE1 
6322  N NE2 . GLN C 228 ? 2.1446 1.8485 1.8506 0.2572  -0.2892 -0.2265 258 GLN C NE2 
6323  N N   . LEU C 229 ? 1.9250 1.7203 1.9591 0.5013  -0.2304 -0.2475 259 LEU C N   
6324  C CA  . LEU C 229 ? 1.9079 1.7288 1.9769 0.5137  -0.2291 -0.2508 259 LEU C CA  
6325  C C   . LEU C 229 ? 1.9346 1.7672 2.0461 0.5079  -0.2250 -0.2506 259 LEU C C   
6326  O O   . LEU C 229 ? 1.9312 1.7773 2.0684 0.4927  -0.2131 -0.2555 259 LEU C O   
6327  C CB  . LEU C 229 ? 1.8691 1.7189 1.9557 0.5121  -0.2183 -0.2609 259 LEU C CB  
6328  C CG  . LEU C 229 ? 1.8682 1.7139 1.9167 0.5150  -0.2197 -0.2621 259 LEU C CG  
6329  C CD1 . LEU C 229 ? 1.8375 1.7139 1.9073 0.5111  -0.2090 -0.2731 259 LEU C CD1 
6330  C CD2 . LEU C 229 ? 1.8657 1.6968 1.8793 0.5355  -0.2342 -0.2532 259 LEU C CD2 
6331  N N   . LEU C 230 ? 1.9685 1.7978 2.0868 0.5211  -0.2346 -0.2444 260 LEU C N   
6332  C CA  . LEU C 230 ? 1.9681 1.8113 2.1274 0.5184  -0.2316 -0.2430 260 LEU C CA  
6333  C C   . LEU C 230 ? 1.9383 1.8153 2.1429 0.5211  -0.2209 -0.2499 260 LEU C C   
6334  O O   . LEU C 230 ? 1.9102 1.7983 2.1169 0.5345  -0.2247 -0.2501 260 LEU C O   
6335  C CB  . LEU C 230 ? 1.9663 1.7943 2.1137 0.5324  -0.2462 -0.2340 260 LEU C CB  
6336  C CG  . LEU C 230 ? 1.9902 1.7785 2.0904 0.5289  -0.2578 -0.2276 260 LEU C CG  
6337  C CD1 . LEU C 230 ? 1.9858 1.7573 2.0713 0.5447  -0.2728 -0.2203 260 LEU C CD1 
6338  C CD2 . LEU C 230 ? 2.0178 1.8001 2.1238 0.5055  -0.2518 -0.2271 260 LEU C CD2 
6339  N N   . LEU C 231 ? 1.8914 1.7845 2.1306 0.5083  -0.2078 -0.2551 261 LEU C N   
6340  C CA  . LEU C 231 ? 1.8499 1.7697 2.1304 0.5086  -0.1961 -0.2629 261 LEU C CA  
6341  C C   . LEU C 231 ? 1.8139 1.7478 2.1358 0.5114  -0.1936 -0.2588 261 LEU C C   
6342  O O   . LEU C 231 ? 1.8130 1.7425 2.1388 0.5052  -0.1944 -0.2533 261 LEU C O   
6343  C CB  . LEU C 231 ? 1.8435 1.7706 2.1285 0.4945  -0.1818 -0.2733 261 LEU C CB  
6344  C CG  . LEU C 231 ? 1.8806 1.7959 2.1241 0.4926  -0.1847 -0.2765 261 LEU C CG  
6345  C CD1 . LEU C 231 ? 1.8736 1.7987 2.1203 0.4798  -0.1708 -0.2875 261 LEU C CD1 
6346  C CD2 . LEU C 231 ? 1.8929 1.8116 2.1251 0.5064  -0.1927 -0.2762 261 LEU C CD2 
6347  N N   . ASN C 232 ? 1.9302 1.8824 2.2833 0.5198  -0.1907 -0.2609 262 ASN C N   
6348  C CA  . ASN C 232 ? 1.8979 1.8660 2.2921 0.5224  -0.1869 -0.2558 262 ASN C CA  
6349  C C   . ASN C 232 ? 1.9040 1.8658 2.2883 0.5228  -0.1963 -0.2413 262 ASN C C   
6350  O O   . ASN C 232 ? 1.8861 1.8557 2.2939 0.5191  -0.1927 -0.2372 262 ASN C O   
6351  C CB  . ASN C 232 ? 1.8742 1.8540 2.3007 0.5135  -0.1719 -0.2620 262 ASN C CB  
6352  C CG  . ASN C 232 ? 1.8581 1.8493 2.3073 0.5114  -0.1588 -0.2737 262 ASN C CG  
6353  O OD1 . ASN C 232 ? 1.8370 1.8412 2.3175 0.5097  -0.1505 -0.2698 262 ASN C OD1 
6354  N ND2 . ASN C 232 ? 1.8727 1.8583 2.3008 0.5043  -0.1538 -0.2839 262 ASN C ND2 
6355  N N   . GLY C 233 ? 1.8900 1.8394 2.2394 0.5279  -0.2083 -0.2334 263 GLY C N   
6356  C CA  . GLY C 233 ? 1.9270 1.8680 2.2631 0.5287  -0.2176 -0.2213 263 GLY C CA  
6357  C C   . GLY C 233 ? 1.9527 1.9103 2.2938 0.5260  -0.2164 -0.2066 263 GLY C C   
6358  O O   . GLY C 233 ? 1.9205 1.8967 2.2780 0.5230  -0.2089 -0.2043 263 GLY C O   
6359  N N   . SER C 234 ? 2.0524 2.0020 2.3791 0.5273  -0.2248 -0.1970 264 SER C N   
6360  C CA  . SER C 234 ? 2.0842 2.0488 2.4120 0.5255  -0.2246 -0.1828 264 SER C CA  
6361  C C   . SER C 234 ? 2.1202 2.0773 2.4099 0.5328  -0.2329 -0.1792 264 SER C C   
6362  O O   . SER C 234 ? 2.1489 2.0798 2.4001 0.5403  -0.2441 -0.1826 264 SER C O   
6363  C CB  . SER C 234 ? 2.0579 2.0190 2.3872 0.5243  -0.2297 -0.1754 264 SER C CB  
6364  O OG  . SER C 234 ? 2.0114 1.9849 2.3781 0.5185  -0.2216 -0.1772 264 SER C OG  
6365  N N   . LEU C 235 ? 1.9985 1.9781 2.2981 0.5311  -0.2279 -0.1718 265 LEU C N   
6366  C CA  . LEU C 235 ? 2.0299 2.0094 2.2970 0.5384  -0.2349 -0.1674 265 LEU C CA  
6367  C C   . LEU C 235 ? 2.0511 2.0242 2.2937 0.5421  -0.2425 -0.1572 265 LEU C C   
6368  O O   . LEU C 235 ? 2.0308 2.0118 2.2914 0.5370  -0.2398 -0.1500 265 LEU C O   
6369  C CB  . LEU C 235 ? 2.0154 2.0232 2.3034 0.5357  -0.2283 -0.1626 265 LEU C CB  
6370  C CG  . LEU C 235 ? 2.0000 2.0143 2.3101 0.5331  -0.2217 -0.1740 265 LEU C CG  
6371  C CD1 . LEU C 235 ? 1.9884 2.0297 2.3215 0.5301  -0.2170 -0.1679 265 LEU C CD1 
6372  C CD2 . LEU C 235 ? 2.0324 2.0296 2.3111 0.5415  -0.2283 -0.1857 265 LEU C CD2 
6373  N N   . ALA C 236 ? 2.0179 1.9766 2.2178 0.5519  -0.2518 -0.1570 266 ALA C N   
6374  C CA  . ALA C 236 ? 2.0444 1.9943 2.2164 0.5569  -0.2592 -0.1493 266 ALA C CA  
6375  C C   . ALA C 236 ? 2.0319 2.0138 2.2172 0.5549  -0.2542 -0.1370 266 ALA C C   
6376  O O   . ALA C 236 ? 2.0116 2.0187 2.2214 0.5510  -0.2471 -0.1342 266 ALA C O   
6377  C CB  . ALA C 236 ? 2.1031 2.0236 2.2217 0.5692  -0.2705 -0.1535 266 ALA C CB  
6378  N N   . GLU C 237 ? 2.2861 2.2658 2.4543 0.5580  -0.2587 -0.1298 267 GLU C N   
6379  C CA  . GLU C 237 ? 2.2780 2.2873 2.4572 0.5565  -0.2544 -0.1174 267 GLU C CA  
6380  C C   . GLU C 237 ? 2.3547 2.3634 2.4942 0.5677  -0.2605 -0.1152 267 GLU C C   
6381  O O   . GLU C 237 ? 2.4269 2.4067 2.5233 0.5777  -0.2696 -0.1209 267 GLU C O   
6382  C CB  . GLU C 237 ? 2.2708 2.2831 2.4601 0.5528  -0.2542 -0.1106 267 GLU C CB  
6383  C CG  . GLU C 237 ? 2.2925 2.2996 2.5117 0.5445  -0.2504 -0.1140 267 GLU C CG  
6384  C CD  . GLU C 237 ? 2.2726 2.3097 2.5420 0.5337  -0.2373 -0.1071 267 GLU C CD  
6385  O OE1 . GLU C 237 ? 2.2699 2.3283 2.5513 0.5322  -0.2322 -0.1015 267 GLU C OE1 
6386  O OE2 . GLU C 237 ? 2.2457 2.2845 2.5415 0.5274  -0.2326 -0.1070 267 GLU C OE2 
6387  N N   . GLU C 238 ? 2.4437 2.4841 2.5974 0.5663  -0.2558 -0.1064 268 GLU C N   
6388  C CA  . GLU C 238 ? 2.5427 2.5913 2.6642 0.5766  -0.2599 -0.1025 268 GLU C CA  
6389  C C   . GLU C 238 ? 2.6090 2.6358 2.6936 0.5870  -0.2660 -0.1123 268 GLU C C   
6390  O O   . GLU C 238 ? 2.5940 2.6274 2.6918 0.5850  -0.2637 -0.1170 268 GLU C O   
6391  C CB  . GLU C 238 ? 2.5389 2.5823 2.6353 0.5827  -0.2640 -0.0975 268 GLU C CB  
6392  C CG  . GLU C 238 ? 2.5078 2.5663 2.6377 0.5729  -0.2590 -0.0892 268 GLU C CG  
6393  C CD  . GLU C 238 ? 2.6102 2.6947 2.7391 0.5749  -0.2576 -0.0776 268 GLU C CD  
6394  O OE1 . GLU C 238 ? 2.5930 2.6768 2.7224 0.5742  -0.2582 -0.0738 268 GLU C OE1 
6395  O OE2 . GLU C 238 ? 2.7015 2.8081 2.8290 0.5775  -0.2562 -0.0723 268 GLU C OE2 
6396  N N   . GLU C 239 ? 2.3681 2.3682 2.4054 0.5987  -0.2738 -0.1156 269 GLU C N   
6397  C CA  . GLU C 239 ? 2.3199 2.2956 2.3188 0.6095  -0.2797 -0.1237 269 GLU C CA  
6398  C C   . GLU C 239 ? 2.2407 2.1845 2.2419 0.6057  -0.2825 -0.1340 269 GLU C C   
6399  O O   . GLU C 239 ? 2.1783 2.1090 2.1942 0.5990  -0.2830 -0.1356 269 GLU C O   
6400  C CB  . GLU C 239 ? 2.3461 2.3011 2.2909 0.6246  -0.2870 -0.1234 269 GLU C CB  
6401  C CG  . GLU C 239 ? 2.4174 2.4041 2.3544 0.6307  -0.2842 -0.1142 269 GLU C CG  
6402  C CD  . GLU C 239 ? 2.4990 2.4634 2.3807 0.6473  -0.2906 -0.1154 269 GLU C CD  
6403  O OE1 . GLU C 239 ? 2.4668 2.3900 2.3192 0.6523  -0.2978 -0.1224 269 GLU C OE1 
6404  O OE2 . GLU C 239 ? 2.5874 2.5748 2.4543 0.6557  -0.2885 -0.1095 269 GLU C OE2 
6405  N N   . VAL C 240 ? 2.0705 2.0032 2.0572 0.6106  -0.2843 -0.1409 270 VAL C N   
6406  C CA  . VAL C 240 ? 2.0665 1.9678 2.0520 0.6082  -0.2872 -0.1508 270 VAL C CA  
6407  C C   . VAL C 240 ? 2.1113 1.9695 2.0560 0.6150  -0.2973 -0.1530 270 VAL C C   
6408  O O   . VAL C 240 ? 2.1641 2.0094 2.0668 0.6265  -0.3030 -0.1501 270 VAL C O   
6409  C CB  . VAL C 240 ? 2.0854 1.9840 2.0597 0.6136  -0.2874 -0.1573 270 VAL C CB  
6410  C CG1 . VAL C 240 ? 2.0392 1.9765 2.0575 0.6057  -0.2786 -0.1577 270 VAL C CG1 
6411  C CG2 . VAL C 240 ? 2.1519 2.0430 2.0763 0.6290  -0.2929 -0.1544 270 VAL C CG2 
6412  N N   . MET C 241 ? 2.2204 2.0554 2.1768 0.6084  -0.2998 -0.1587 271 MET C N   
6413  C CA  . MET C 241 ? 2.2294 2.0218 2.1520 0.6128  -0.3108 -0.1609 271 MET C CA  
6414  C C   . MET C 241 ? 2.2888 2.0377 2.1758 0.6190  -0.3189 -0.1680 271 MET C C   
6415  O O   . MET C 241 ? 2.2433 1.9954 2.1463 0.6159  -0.3149 -0.1732 271 MET C O   
6416  C CB  . MET C 241 ? 2.1639 1.9578 2.1208 0.6017  -0.3101 -0.1613 271 MET C CB  
6417  C CG  . MET C 241 ? 2.1744 1.9411 2.1023 0.6062  -0.3206 -0.1600 271 MET C CG  
6418  S SD  . MET C 241 ? 2.2783 2.0685 2.1911 0.6133  -0.3189 -0.1516 271 MET C SD  
6419  C CE  . MET C 241 ? 2.2390 2.0872 2.2197 0.5990  -0.3036 -0.1439 271 MET C CE  
6420  N N   . ILE C 242 ? 2.1866 1.8927 2.0232 0.6283  -0.3306 -0.1683 272 ILE C N   
6421  C CA  . ILE C 242 ? 2.2461 1.9016 2.0413 0.6343  -0.3402 -0.1731 272 ILE C CA  
6422  C C   . ILE C 242 ? 2.2708 1.8824 2.0486 0.6315  -0.3524 -0.1751 272 ILE C C   
6423  O O   . ILE C 242 ? 2.3015 1.9009 2.0549 0.6366  -0.3586 -0.1726 272 ILE C O   
6424  C CB  . ILE C 242 ? 2.3232 1.9618 2.0642 0.6498  -0.3441 -0.1706 272 ILE C CB  
6425  C CG1 . ILE C 242 ? 2.3006 1.9856 2.0587 0.6530  -0.3334 -0.1680 272 ILE C CG1 
6426  C CG2 . ILE C 242 ? 2.3896 1.9721 2.0861 0.6553  -0.3541 -0.1740 272 ILE C CG2 
6427  C CD1 . ILE C 242 ? 2.2767 1.9734 2.0625 0.6472  -0.3277 -0.1731 272 ILE C CD1 
6428  N N   . ARG C 243 ? 2.1911 1.7788 1.9807 0.6239  -0.3563 -0.1800 273 ARG C N   
6429  C CA  . ARG C 243 ? 2.2135 1.7594 1.9898 0.6196  -0.3692 -0.1817 273 ARG C CA  
6430  C C   . ARG C 243 ? 2.2801 1.7647 2.0153 0.6210  -0.3811 -0.1847 273 ARG C C   
6431  O O   . ARG C 243 ? 2.2728 1.7586 2.0184 0.6191  -0.3764 -0.1878 273 ARG C O   
6432  C CB  . ARG C 243 ? 2.1377 1.7135 1.9730 0.6069  -0.3641 -0.1833 273 ARG C CB  
6433  C CG  . ARG C 243 ? 2.0757 1.7077 1.9511 0.6037  -0.3525 -0.1786 273 ARG C CG  
6434  C CD  . ARG C 243 ? 2.0039 1.6674 1.9385 0.5915  -0.3456 -0.1794 273 ARG C CD  
6435  N NE  . ARG C 243 ? 1.9526 1.6645 1.9215 0.5877  -0.3349 -0.1730 273 ARG C NE  
6436  C CZ  . ARG C 243 ? 1.9047 1.6622 1.9099 0.5833  -0.3199 -0.1700 273 ARG C CZ  
6437  N NH1 . ARG C 243 ? 1.8987 1.6620 1.9116 0.5828  -0.3137 -0.1743 273 ARG C NH1 
6438  N NH2 . ARG C 243 ? 1.8663 1.6614 1.8988 0.5792  -0.3116 -0.1626 273 ARG C NH2 
6439  N N   . SER C 244 ? 2.4051 1.8334 2.0918 0.6237  -0.3969 -0.1838 274 SER C N   
6440  C CA  . SER C 244 ? 2.5496 1.9096 2.1909 0.6224  -0.4101 -0.1847 274 SER C CA  
6441  C C   . SER C 244 ? 2.6453 1.9496 2.2529 0.6183  -0.4281 -0.1843 274 SER C C   
6442  O O   . SER C 244 ? 2.6537 1.9628 2.2488 0.6237  -0.4313 -0.1834 274 SER C O   
6443  C CB  . SER C 244 ? 2.6775 2.0130 2.2665 0.6347  -0.4105 -0.1822 274 SER C CB  
6444  O OG  . SER C 244 ? 2.7647 2.0334 2.3075 0.6280  -0.4217 -0.1810 274 SER C OG  
6445  N N   . GLU C 245 ? 2.7348 2.0118 2.3330 0.5854  -0.4288 -0.1820 275 GLU C N   
6446  C CA  . GLU C 245 ? 2.8366 2.0626 2.4011 0.5707  -0.4442 -0.1804 275 GLU C CA  
6447  C C   . GLU C 245 ? 3.0155 2.1684 2.5017 0.5914  -0.4614 -0.1800 275 GLU C C   
6448  O O   . GLU C 245 ? 3.1029 2.2153 2.5566 0.5973  -0.4770 -0.1812 275 GLU C O   
6449  C CB  . GLU C 245 ? 2.8144 2.0359 2.3905 0.5278  -0.4400 -0.1765 275 GLU C CB  
6450  C CG  . GLU C 245 ? 2.8936 2.0691 2.4410 0.5070  -0.4557 -0.1740 275 GLU C CG  
6451  C CD  . GLU C 245 ? 2.8298 2.0096 2.3924 0.4633  -0.4510 -0.1683 275 GLU C CD  
6452  O OE1 . GLU C 245 ? 2.7812 1.9947 2.3715 0.4510  -0.4358 -0.1666 275 GLU C OE1 
6453  O OE2 . GLU C 245 ? 2.8576 2.0090 2.4043 0.4411  -0.4626 -0.1654 275 GLU C OE2 
6454  N N   . ASN C 246 ? 2.9458 2.0805 2.3997 0.6033  -0.4589 -0.1783 276 ASN C N   
6455  C CA  . ASN C 246 ? 3.0715 2.1371 2.4493 0.6267  -0.4738 -0.1771 276 ASN C CA  
6456  C C   . ASN C 246 ? 3.0953 2.1937 2.4696 0.6419  -0.4601 -0.1753 276 ASN C C   
6457  O O   . ASN C 246 ? 3.1471 2.2345 2.5167 0.6356  -0.4563 -0.1728 276 ASN C O   
6458  C CB  . ASN C 246 ? 3.2137 2.2095 2.5415 0.5988  -0.4842 -0.1728 276 ASN C CB  
6459  C CG  . ASN C 246 ? 3.3830 2.2975 2.6293 0.6231  -0.5032 -0.1727 276 ASN C CG  
6460  O OD1 . ASN C 246 ? 3.3975 2.3404 2.6305 0.6434  -0.4958 -0.1738 276 ASN C OD1 
6461  N ND2 . ASN C 246 ? 3.6423 2.4900 2.8441 0.5986  -0.5165 -0.1699 276 ASN C ND2 
6462  N N   . ILE C 247 ? 2.9521 2.0969 2.3303 0.6569  -0.4510 -0.1759 277 ILE C N   
6463  C CA  . ILE C 247 ? 2.9538 2.1372 2.3317 0.6705  -0.4379 -0.1739 277 ILE C CA  
6464  C C   . ILE C 247 ? 3.0631 2.1877 2.3734 0.6794  -0.4449 -0.1703 277 ILE C C   
6465  O O   . ILE C 247 ? 3.0757 2.2124 2.3842 0.6848  -0.4374 -0.1677 277 ILE C O   
6466  C CB  . ILE C 247 ? 2.9167 2.1557 2.3088 0.6825  -0.4289 -0.1745 277 ILE C CB  
6467  C CG1 . ILE C 247 ? 2.8401 2.1291 2.2941 0.6721  -0.4234 -0.1767 277 ILE C CG1 
6468  C CG2 . ILE C 247 ? 2.9270 2.2141 2.3279 0.6938  -0.4149 -0.1720 277 ILE C CG2 
6469  C CD1 . ILE C 247 ? 2.8039 2.1471 2.2745 0.6810  -0.4144 -0.1760 277 ILE C CD1 
6470  N N   . THR C 248 ? 3.1882 2.2480 2.4411 0.6813  -0.4595 -0.1701 278 THR C N   
6471  C CA  . THR C 248 ? 3.3368 2.3340 2.5213 0.6890  -0.4669 -0.1662 278 THR C CA  
6472  C C   . THR C 248 ? 3.3660 2.3158 2.5396 0.6744  -0.4724 -0.1617 278 THR C C   
6473  O O   . THR C 248 ? 3.4364 2.3561 2.5696 0.6813  -0.4726 -0.1568 278 THR C O   
6474  C CB  . THR C 248 ? 3.4445 2.3804 2.5711 0.6924  -0.4821 -0.1681 278 THR C CB  
6475  O OG1 . THR C 248 ? 3.4709 2.3685 2.6043 0.6725  -0.4952 -0.1697 278 THR C OG1 
6476  C CG2 . THR C 248 ? 3.3803 2.3608 2.5105 0.7098  -0.4764 -0.1725 278 THR C CG2 
6477  N N   . ASN C 249 ? 3.3668 2.3103 2.5757 0.6547  -0.4767 -0.1630 279 ASN C N   
6478  C CA  . ASN C 249 ? 3.3462 2.2711 2.5583 0.6222  -0.4743 -0.1583 279 ASN C CA  
6479  C C   . ASN C 249 ? 3.2288 2.2242 2.4940 0.6128  -0.4541 -0.1581 279 ASN C C   
6480  O O   . ASN C 249 ? 3.1299 2.1919 2.4583 0.6097  -0.4426 -0.1629 279 ASN C O   
6481  C CB  . ASN C 249 ? 3.2841 2.2034 2.5200 0.5842  -0.4782 -0.1586 279 ASN C CB  
6482  C CG  . ASN C 249 ? 3.3113 2.2016 2.5327 0.5442  -0.4779 -0.1511 279 ASN C CG  
6483  O OD1 . ASN C 249 ? 3.3436 2.2338 2.5526 0.5417  -0.4707 -0.1463 279 ASN C OD1 
6484  N ND2 . ASN C 249 ? 3.3150 2.1835 2.5383 0.5121  -0.4859 -0.1493 279 ASN C ND2 
6485  N N   . ASN C 250 ? 3.3596 2.3385 2.5970 0.6091  -0.4502 -0.1525 280 ASN C N   
6486  C CA  . ASN C 250 ? 3.3250 2.3662 2.6061 0.6002  -0.4318 -0.1528 280 ASN C CA  
6487  C C   . ASN C 250 ? 3.2553 2.3245 2.5806 0.5565  -0.4217 -0.1519 280 ASN C C   
6488  O O   . ASN C 250 ? 3.1833 2.3030 2.5443 0.5476  -0.4062 -0.1530 280 ASN C O   
6489  C CB  . ASN C 250 ? 3.4468 2.4631 2.6814 0.6124  -0.4309 -0.1466 280 ASN C CB  
6490  C CG  . ASN C 250 ? 3.5792 2.5273 2.7638 0.5882  -0.4401 -0.1381 280 ASN C CG  
6491  O OD1 . ASN C 250 ? 3.6954 2.5722 2.8213 0.5986  -0.4566 -0.1350 280 ASN C OD1 
6492  N ND2 . ASN C 250 ? 3.6307 2.6003 2.8376 0.5555  -0.4297 -0.1343 280 ASN C ND2 
6493  N N   . ALA C 251 ? 3.1620 2.2031 2.4861 0.5291  -0.4298 -0.1499 281 ALA C N   
6494  C CA  . ALA C 251 ? 3.1062 2.1819 2.4741 0.4892  -0.4191 -0.1479 281 ALA C CA  
6495  C C   . ALA C 251 ? 2.9947 2.1324 2.4319 0.4810  -0.4097 -0.1545 281 ALA C C   
6496  O O   . ALA C 251 ? 2.9422 2.1235 2.4239 0.4546  -0.3969 -0.1542 281 ALA C O   
6497  C CB  . ALA C 251 ? 3.1778 2.1947 2.5080 0.4578  -0.4319 -0.1396 281 ALA C CB  
6498  N N   . LYS C 252 ? 2.8152 1.9595 2.2626 0.5040  -0.4152 -0.1600 282 LYS C N   
6499  C CA  . LYS C 252 ? 2.7123 1.9154 2.2248 0.4999  -0.4064 -0.1655 282 LYS C CA  
6500  C C   . LYS C 252 ? 2.6504 1.9107 2.2007 0.5240  -0.3931 -0.1715 282 LYS C C   
6501  O O   . LYS C 252 ? 2.6793 1.9293 2.2022 0.5554  -0.3973 -0.1726 282 LYS C O   
6502  C CB  . LYS C 252 ? 2.7044 1.8869 2.2129 0.5038  -0.4197 -0.1668 282 LYS C CB  
6503  C CG  . LYS C 252 ? 2.7698 1.9097 2.2551 0.4689  -0.4298 -0.1607 282 LYS C CG  
6504  C CD  . LYS C 252 ? 2.7482 1.9391 2.2872 0.4331  -0.4149 -0.1581 282 LYS C CD  
6505  C CE  . LYS C 252 ? 2.7625 1.9231 2.2855 0.3948  -0.4237 -0.1502 282 LYS C CE  
6506  N NZ  . LYS C 252 ? 2.7394 1.9565 2.3156 0.3638  -0.4082 -0.1471 282 LYS C NZ  
6507  N N   . ASN C 253 ? 2.3894 1.7101 2.0020 0.5094  -0.3775 -0.1752 283 ASN C N   
6508  C CA  . ASN C 253 ? 2.3289 1.7057 1.9821 0.5260  -0.3640 -0.1811 283 ASN C CA  
6509  C C   . ASN C 253 ? 2.2973 1.6885 1.9620 0.5555  -0.3693 -0.1843 283 ASN C C   
6510  O O   . ASN C 253 ? 2.2969 1.6694 1.9564 0.5585  -0.3800 -0.1834 283 ASN C O   
6511  C CB  . ASN C 253 ? 2.2510 1.6822 1.9663 0.5021  -0.3473 -0.1845 283 ASN C CB  
6512  C CG  . ASN C 253 ? 2.2701 1.6974 1.9783 0.4750  -0.3401 -0.1814 283 ASN C CG  
6513  O OD1 . ASN C 253 ? 2.3068 1.7254 1.9887 0.4803  -0.3376 -0.1807 283 ASN C OD1 
6514  N ND2 . ASN C 253 ? 2.2473 1.6839 1.9785 0.4461  -0.3366 -0.1787 283 ASN C ND2 
6515  N N   . ILE C 254 ? 2.0923 1.5198 1.7731 0.5766  -0.3620 -0.1876 284 ILE C N   
6516  C CA  . ILE C 254 ? 2.0630 1.5121 1.7563 0.6057  -0.3660 -0.1893 284 ILE C CA  
6517  C C   . ILE C 254 ? 1.9656 1.4794 1.7264 0.6006  -0.3512 -0.1941 284 ILE C C   
6518  O O   . ILE C 254 ? 1.9402 1.4862 1.7175 0.6028  -0.3406 -0.1970 284 ILE C O   
6519  C CB  . ILE C 254 ? 2.1170 1.5546 1.7684 0.6370  -0.3717 -0.1873 284 ILE C CB  
6520  C CG1 . ILE C 254 ? 2.2259 1.5944 1.8062 0.6430  -0.3857 -0.1824 284 ILE C CG1 
6521  C CG2 . ILE C 254 ? 2.0810 1.5621 1.7496 0.6467  -0.3674 -0.1849 284 ILE C CG2 
6522  C CD1 . ILE C 254 ? 2.2841 1.6500 1.8222 0.6662  -0.3866 -0.1785 284 ILE C CD1 
6523  N N   . LEU C 255 ? 2.0460 1.5777 1.8447 0.5936  -0.3508 -0.1949 285 LEU C N   
6524  C CA  . LEU C 255 ? 1.9578 1.5463 1.8205 0.5888  -0.3374 -0.1989 285 LEU C CA  
6525  C C   . LEU C 255 ? 1.9327 1.5557 1.8076 0.6087  -0.3355 -0.1971 285 LEU C C   
6526  O O   . LEU C 255 ? 1.9463 1.5678 1.8057 0.6113  -0.3399 -0.1909 285 LEU C O   
6527  C CB  . LEU C 255 ? 1.9186 1.5146 1.8145 0.5714  -0.3367 -0.1981 285 LEU C CB  
6528  C CG  . LEU C 255 ? 1.9439 1.5164 1.8282 0.5412  -0.3348 -0.1965 285 LEU C CG  
6529  C CD1 . LEU C 255 ? 1.9018 1.4906 1.8233 0.5224  -0.3323 -0.1950 285 LEU C CD1 
6530  C CD2 . LEU C 255 ? 1.9371 1.5259 1.8296 0.5271  -0.3210 -0.1997 285 LEU C CD2 
6531  N N   . VAL C 256 ? 1.9311 1.5934 1.8324 0.6086  -0.3234 -0.2000 286 VAL C N   
6532  C CA  . VAL C 256 ? 1.9060 1.6116 1.8204 0.6105  -0.3153 -0.1946 286 VAL C CA  
6533  C C   . VAL C 256 ? 1.8265 1.5775 1.8027 0.5985  -0.3031 -0.1960 286 VAL C C   
6534  O O   . VAL C 256 ? 1.7918 1.5501 1.8003 0.5917  -0.2971 -0.2040 286 VAL C O   
6535  C CB  . VAL C 256 ? 1.9325 1.6470 1.8264 0.6200  -0.3125 -0.1957 286 VAL C CB  
6536  C CG1 . VAL C 256 ? 1.9141 1.6716 1.8189 0.6222  -0.3063 -0.1891 286 VAL C CG1 
6537  C CG2 . VAL C 256 ? 2.0173 1.6836 1.8492 0.6321  -0.3238 -0.1938 286 VAL C CG2 
6538  N N   . GLN C 257 ? 2.0178 1.7982 2.0095 0.5960  -0.2991 -0.1881 287 GLN C N   
6539  C CA  . GLN C 257 ? 1.9541 1.7759 2.0008 0.5848  -0.2873 -0.1869 287 GLN C CA  
6540  C C   . GLN C 257 ? 1.9677 1.8249 2.0218 0.5866  -0.2811 -0.1813 287 GLN C C   
6541  O O   . GLN C 257 ? 1.9721 1.8305 1.9978 0.5939  -0.2854 -0.1738 287 GLN C O   
6542  C CB  . GLN C 257 ? 1.9251 1.7505 1.9903 0.5781  -0.2881 -0.1812 287 GLN C CB  
6543  C CG  . GLN C 257 ? 1.8650 1.7287 1.9876 0.5663  -0.2752 -0.1797 287 GLN C CG  
6544  C CD  . GLN C 257 ? 1.8356 1.7047 1.9777 0.5603  -0.2754 -0.1737 287 GLN C CD  
6545  O OE1 . GLN C 257 ? 1.8667 1.7143 1.9797 0.5650  -0.2855 -0.1705 287 GLN C OE1 
6546  N NE2 . GLN C 257 ? 1.7842 1.6815 1.9746 0.5504  -0.2642 -0.1723 287 GLN C NE2 
6547  N N   . PHE C 258 ? 2.0117 1.8967 2.1031 0.5803  -0.2714 -0.1855 288 PHE C N   
6548  C CA  . PHE C 258 ? 1.9725 1.8904 2.0741 0.5814  -0.2666 -0.1816 288 PHE C CA  
6549  C C   . PHE C 258 ? 1.9625 1.9104 2.0977 0.5730  -0.2604 -0.1717 288 PHE C C   
6550  O O   . PHE C 258 ? 1.9861 1.9352 2.1481 0.5645  -0.2564 -0.1698 288 PHE C O   
6551  C CB  . PHE C 258 ? 1.9426 1.8729 2.0672 0.5790  -0.2603 -0.1925 288 PHE C CB  
6552  C CG  . PHE C 258 ? 2.0107 1.9192 2.1020 0.5886  -0.2653 -0.2013 288 PHE C CG  
6553  C CD1 . PHE C 258 ? 2.1024 1.9904 2.1436 0.6007  -0.2746 -0.1964 288 PHE C CD1 
6554  C CD2 . PHE C 258 ? 1.9502 1.8589 2.0594 0.5861  -0.2600 -0.2146 288 PHE C CD2 
6555  C CE1 . PHE C 258 ? 2.1064 1.9736 2.1157 0.6102  -0.2789 -0.2030 288 PHE C CE1 
6556  C CE2 . PHE C 258 ? 1.9493 1.8392 2.0279 0.5954  -0.2640 -0.2225 288 PHE C CE2 
6557  C CZ  . PHE C 258 ? 2.0206 1.8894 2.0491 0.6075  -0.2736 -0.2159 288 PHE C CZ  
6558  N N   . ASN C 259 ? 1.9462 1.9195 2.0789 0.5762  -0.2597 -0.1645 289 ASN C N   
6559  C CA  . ASN C 259 ? 1.9687 1.9729 2.1328 0.5689  -0.2539 -0.1540 289 ASN C CA  
6560  C C   . ASN C 259 ? 1.9466 1.9751 2.1494 0.5623  -0.2466 -0.1578 289 ASN C C   
6561  O O   . ASN C 259 ? 1.9160 1.9575 2.1574 0.5524  -0.2391 -0.1548 289 ASN C O   
6562  C CB  . ASN C 259 ? 2.0187 2.0372 2.1571 0.5765  -0.2581 -0.1430 289 ASN C CB  
6563  C CG  . ASN C 259 ? 2.0600 2.1127 2.2312 0.5692  -0.2524 -0.1313 289 ASN C CG  
6564  O OD1 . ASN C 259 ? 2.0854 2.1637 2.2731 0.5681  -0.2503 -0.1292 289 ASN C OD1 
6565  N ND2 . ASN C 259 ? 2.1120 2.1652 2.2926 0.5643  -0.2505 -0.1233 289 ASN C ND2 
6566  N N   . THR C 260 ? 2.1144 2.1484 2.3063 0.5684  -0.2489 -0.1647 290 THR C N   
6567  C CA  . THR C 260 ? 2.1295 2.1824 2.3535 0.5640  -0.2440 -0.1719 290 THR C CA  
6568  C C   . THR C 260 ? 2.0677 2.1013 2.2941 0.5640  -0.2419 -0.1889 290 THR C C   
6569  O O   . THR C 260 ? 2.0629 2.0787 2.2551 0.5728  -0.2474 -0.1948 290 THR C O   
6570  C CB  . THR C 260 ? 2.2091 2.2872 2.4215 0.5713  -0.2488 -0.1685 290 THR C CB  
6571  O OG1 . THR C 260 ? 2.2850 2.3495 2.4546 0.5833  -0.2554 -0.1733 290 THR C OG1 
6572  C CG2 . THR C 260 ? 2.2089 2.3087 2.4200 0.5710  -0.2501 -0.1512 290 THR C CG2 
6573  N N   . PRO C 261 ? 2.1475 2.1832 2.4123 0.5546  -0.2334 -0.1967 291 PRO C N   
6574  C CA  . PRO C 261 ? 2.0938 2.1125 2.3628 0.5539  -0.2297 -0.2136 291 PRO C CA  
6575  C C   . PRO C 261 ? 2.1423 2.1689 2.4018 0.5608  -0.2322 -0.2253 291 PRO C C   
6576  O O   . PRO C 261 ? 2.1928 2.2435 2.4630 0.5618  -0.2337 -0.2234 291 PRO C O   
6577  C CB  . PRO C 261 ? 2.0663 2.0909 2.3806 0.5424  -0.2188 -0.2170 291 PRO C CB  
6578  C CG  . PRO C 261 ? 2.0970 2.1464 2.4319 0.5390  -0.2179 -0.2056 291 PRO C CG  
6579  C CD  . PRO C 261 ? 2.1498 2.2042 2.4553 0.5448  -0.2262 -0.1902 291 PRO C CD  
6580  N N   . VAL C 262 ? 2.0134 2.0211 2.2525 0.5660  -0.2332 -0.2374 292 VAL C N   
6581  C CA  . VAL C 262 ? 2.0295 2.0442 2.2582 0.5732  -0.2346 -0.2504 292 VAL C CA  
6582  C C   . VAL C 262 ? 1.9992 2.0133 2.2567 0.5578  -0.2217 -0.2658 292 VAL C C   
6583  O O   . VAL C 262 ? 1.9916 1.9874 2.2497 0.5489  -0.2143 -0.2713 292 VAL C O   
6584  C CB  . VAL C 262 ? 2.0734 2.0681 2.2547 0.5823  -0.2406 -0.2510 292 VAL C CB  
6585  C CG1 . VAL C 262 ? 2.0918 2.0976 2.2563 0.5738  -0.2358 -0.2584 292 VAL C CG1 
6586  C CG2 . VAL C 262 ? 2.1102 2.1020 2.2575 0.5928  -0.2508 -0.2342 292 VAL C CG2 
6587  N N   . GLN C 263 ? 1.9939 2.0285 2.2725 0.5509  -0.2179 -0.2708 293 GLN C N   
6588  C CA  . GLN C 263 ? 1.9637 1.9970 2.2668 0.5339  -0.2045 -0.2847 293 GLN C CA  
6589  C C   . GLN C 263 ? 1.9890 2.0110 2.2638 0.5240  -0.1978 -0.2951 293 GLN C C   
6590  O O   . GLN C 263 ? 2.0086 2.0381 2.2543 0.5247  -0.2018 -0.2953 293 GLN C O   
6591  C CB  . GLN C 263 ? 1.9591 2.0138 2.2833 0.5285  -0.2045 -0.2873 293 GLN C CB  
6592  C CG  . GLN C 263 ? 1.9356 1.9864 2.2920 0.5138  -0.1919 -0.3006 293 GLN C CG  
6593  C CD  . GLN C 263 ? 1.9128 1.9609 2.3090 0.5170  -0.1888 -0.2964 293 GLN C CD  
6594  O OE1 . GLN C 263 ? 1.9852 2.0311 2.3852 0.5281  -0.1939 -0.2856 293 GLN C OE1 
6595  N NE2 . GLN C 263 ? 1.9042 1.9514 2.3292 0.5074  -0.1805 -0.3052 293 GLN C NE2 
6596  N N   . ILE C 264 ? 2.1027 2.1102 2.3865 0.5151  -0.1874 -0.3027 294 ILE C N   
6597  C CA  . ILE C 264 ? 2.1038 2.1027 2.3640 0.5050  -0.1800 -0.3122 294 ILE C CA  
6598  C C   . ILE C 264 ? 2.1197 2.1210 2.4069 0.4921  -0.1657 -0.3270 294 ILE C C   
6599  O O   . ILE C 264 ? 2.1025 2.1016 2.4224 0.4918  -0.1600 -0.3279 294 ILE C O   
6600  C CB  . ILE C 264 ? 2.0497 2.0289 2.2887 0.5065  -0.1816 -0.3061 294 ILE C CB  
6601  C CG1 . ILE C 264 ? 2.0470 2.0205 2.2613 0.4955  -0.1741 -0.3145 294 ILE C CG1 
6602  C CG2 . ILE C 264 ? 2.0221 1.9949 2.2911 0.5054  -0.1773 -0.3037 294 ILE C CG2 
6603  C CD1 . ILE C 264 ? 1.9991 1.9530 2.1902 0.4942  -0.1763 -0.3077 294 ILE C CD1 
6604  N N   . ASN C 265 ? 2.2247 2.2308 2.4970 0.4827  -0.1601 -0.3386 295 ASN C N   
6605  C CA  . ASN C 265 ? 2.1848 2.1919 2.4767 0.4715  -0.1469 -0.3547 295 ASN C CA  
6606  C C   . ASN C 265 ? 2.1964 2.1991 2.4660 0.4635  -0.1384 -0.3630 295 ASN C C   
6607  O O   . ASN C 265 ? 2.2210 2.2275 2.4584 0.4616  -0.1421 -0.3633 295 ASN C O   
6608  C CB  . ASN C 265 ? 2.1947 2.2141 2.4880 0.4664  -0.1489 -0.3618 295 ASN C CB  
6609  C CG  . ASN C 265 ? 2.1227 2.1495 2.4402 0.4724  -0.1570 -0.3529 295 ASN C CG  
6610  O OD1 . ASN C 265 ? 2.1410 2.1695 2.4581 0.4839  -0.1663 -0.3381 295 ASN C OD1 
6611  N ND2 . ASN C 265 ? 2.0835 2.1150 2.4189 0.4646  -0.1545 -0.3613 295 ASN C ND2 
6612  N N   . CYS C 266 ? 1.8524 1.8498 2.1391 0.4594  -0.1270 -0.3691 296 CYS C N   
6613  C CA  . CYS C 266 ? 1.8445 1.8412 2.1141 0.4515  -0.1179 -0.3763 296 CYS C CA  
6614  C C   . CYS C 266 ? 1.8793 1.8796 2.1684 0.4450  -0.1030 -0.3935 296 CYS C C   
6615  O O   . CYS C 266 ? 1.9035 1.9017 2.2246 0.4480  -0.0972 -0.3961 296 CYS C O   
6616  C CB  . CYS C 266 ? 1.8242 1.8130 2.0888 0.4529  -0.1191 -0.3645 296 CYS C CB  
6617  S SG  . CYS C 266 ? 2.2616 2.2391 2.4976 0.4621  -0.1371 -0.3453 296 CYS C SG  
6618  N N   . THR C 267 ? 1.9601 1.9659 2.2285 0.4373  -0.0966 -0.4051 297 THR C N   
6619  C CA  . THR C 267 ? 1.9357 1.9444 2.2166 0.4323  -0.0825 -0.4231 297 THR C CA  
6620  C C   . THR C 267 ? 1.8791 1.8952 2.1400 0.4263  -0.0738 -0.4281 297 THR C C   
6621  O O   . THR C 267 ? 1.8695 1.8881 2.1027 0.4239  -0.0795 -0.4193 297 THR C O   
6622  C CB  . THR C 267 ? 1.9580 1.9679 2.2363 0.4276  -0.0830 -0.4370 297 THR C CB  
6623  O OG1 . THR C 267 ? 2.0033 2.0207 2.2510 0.4246  -0.0929 -0.4327 297 THR C OG1 
6624  C CG2 . THR C 267 ? 1.9725 1.9751 2.2798 0.4318  -0.0869 -0.4355 297 THR C CG2 
6625  N N   . ARG C 268 ? 1.7115 1.7313 1.9865 0.4248  -0.0599 -0.4421 298 ARG C N   
6626  C CA  . ARG C 268 ? 1.7157 1.7470 1.9758 0.4197  -0.0494 -0.4490 298 ARG C CA  
6627  C C   . ARG C 268 ? 1.7185 1.7524 1.9753 0.4165  -0.0405 -0.4712 298 ARG C C   
6628  O O   . ARG C 268 ? 1.7085 1.7414 1.9844 0.4200  -0.0288 -0.4834 298 ARG C O   
6629  C CB  . ARG C 268 ? 1.7013 1.7384 1.9810 0.4227  -0.0403 -0.4437 298 ARG C CB  
6630  C CG  . ARG C 268 ? 1.7107 1.7628 1.9705 0.4162  -0.0343 -0.4410 298 ARG C CG  
6631  C CD  . ARG C 268 ? 1.7104 1.7759 1.9658 0.4144  -0.0201 -0.4598 298 ARG C CD  
6632  N NE  . ARG C 268 ? 1.6939 1.7618 1.9789 0.4222  -0.0078 -0.4687 298 ARG C NE  
6633  C CZ  . ARG C 268 ? 1.6866 1.7697 1.9848 0.4245  0.0013  -0.4628 298 ARG C CZ  
6634  N NH1 . ARG C 268 ? 1.6945 1.7904 1.9789 0.4172  -0.0013 -0.4481 298 ARG C NH1 
6635  N NH2 . ARG C 268 ? 1.6755 1.7611 2.0000 0.4340  0.0126  -0.4709 298 ARG C NH2 
6636  N N   . PRO C 269 ? 1.8206 1.8581 2.0517 0.4102  -0.0458 -0.4770 299 PRO C N   
6637  C CA  . PRO C 269 ? 1.8278 1.8664 2.0530 0.4055  -0.0392 -0.4988 299 PRO C CA  
6638  C C   . PRO C 269 ? 1.8281 1.8786 2.0443 0.4036  -0.0251 -0.5120 299 PRO C C   
6639  O O   . PRO C 269 ? 1.8417 1.9033 2.0322 0.3969  -0.0240 -0.5206 299 PRO C O   
6640  C CB  . PRO C 269 ? 1.8490 1.8933 2.0470 0.3989  -0.0504 -0.4968 299 PRO C CB  
6641  C CG  . PRO C 269 ? 1.8574 1.9076 2.0380 0.4005  -0.0578 -0.4770 299 PRO C CG  
6642  C CD  . PRO C 269 ? 1.8395 1.8801 2.0440 0.4078  -0.0586 -0.4633 299 PRO C CD  
6643  N N   . ASN C 270 ? 1.8728 1.9243 2.1095 0.4100  -0.0142 -0.5134 300 ASN C N   
6644  C CA  . ASN C 270 ? 1.8543 1.9209 2.0841 0.4103  0.0000  -0.5255 300 ASN C CA  
6645  C C   . ASN C 270 ? 1.8675 1.9291 2.1258 0.4206  0.0120  -0.5332 300 ASN C C   
6646  O O   . ASN C 270 ? 1.8814 1.9466 2.1592 0.4260  0.0134  -0.5190 300 ASN C O   
6647  C CB  . ASN C 270 ? 1.8596 1.9453 2.0748 0.4066  0.0003  -0.5100 300 ASN C CB  
6648  C CG  . ASN C 270 ? 1.8748 1.9700 2.0555 0.3976  -0.0061 -0.5081 300 ASN C CG  
6649  O OD1 . ASN C 270 ? 1.8840 1.9980 2.0479 0.3937  0.0008  -0.5106 300 ASN C OD1 
6650  N ND2 . ASN C 270 ? 1.8847 1.9696 2.0549 0.3950  -0.0195 -0.5016 300 ASN C ND2 
6651  N N   . ASN C 271 ? 1.8894 1.9419 2.1493 0.4236  0.0204  -0.5554 301 ASN C N   
6652  C CA  . ASN C 271 ? 1.8842 1.9306 2.1686 0.4359  0.0328  -0.5634 301 ASN C CA  
6653  C C   . ASN C 271 ? 1.8797 1.9526 2.1624 0.4410  0.0459  -0.5624 301 ASN C C   
6654  O O   . ASN C 271 ? 1.8893 1.9707 2.1584 0.4432  0.0565  -0.5801 301 ASN C O   
6655  C CB  . ASN C 271 ? 1.9009 1.9258 2.1828 0.4382  0.0378  -0.5884 301 ASN C CB  
6656  C CG  . ASN C 271 ? 1.9029 1.9124 2.2116 0.4529  0.0481  -0.5951 301 ASN C CG  
6657  O OD1 . ASN C 271 ? 1.8891 1.9052 2.2212 0.4610  0.0503  -0.5797 301 ASN C OD1 
6658  N ND2 . ASN C 271 ? 1.9242 1.9126 2.2277 0.4565  0.0545  -0.6184 301 ASN C ND2 
6659  N N   . ASN C 272 ? 1.8472 1.9349 2.1424 0.4422  0.0448  -0.5415 302 ASN C N   
6660  C CA  . ASN C 272 ? 1.8457 1.9633 2.1394 0.4446  0.0560  -0.5372 302 ASN C CA  
6661  C C   . ASN C 272 ? 1.8449 1.9666 2.1603 0.4603  0.0713  -0.5472 302 ASN C C   
6662  O O   . ASN C 272 ? 1.8440 1.9443 2.1807 0.4695  0.0721  -0.5513 302 ASN C O   
6663  C CB  . ASN C 272 ? 1.8383 1.9692 2.1367 0.4384  0.0485  -0.5107 302 ASN C CB  
6664  C CG  . ASN C 272 ? 1.8473 1.9760 2.1188 0.4247  0.0349  -0.5003 302 ASN C CG  
6665  O OD1 . ASN C 272 ? 1.8559 1.9726 2.1093 0.4205  0.0293  -0.5107 302 ASN C OD1 
6666  N ND2 . ASN C 272 ? 1.8495 1.9889 2.1171 0.4179  0.0291  -0.4791 302 ASN C ND2 
6667  N N   . THR C 273 ? 1.7607 1.9118 2.0701 0.4641  0.0839  -0.5503 303 THR C N   
6668  C CA  . THR C 273 ? 1.7643 1.9269 2.0913 0.4810  0.0999  -0.5583 303 THR C CA  
6669  C C   . THR C 273 ? 1.7571 1.9578 2.0943 0.4807  0.1048  -0.5377 303 THR C C   
6670  O O   . THR C 273 ? 1.7582 1.9814 2.0781 0.4679  0.1013  -0.5270 303 THR C O   
6671  C CB  . THR C 273 ? 1.7807 1.9441 2.0901 0.4891  0.1121  -0.5849 303 THR C CB  
6672  O OG1 . THR C 273 ? 1.7916 1.9503 2.1197 0.5092  0.1254  -0.5951 303 THR C OG1 
6673  C CG2 . THR C 273 ? 1.7824 1.9837 2.0715 0.4842  0.1186  -0.5839 303 THR C CG2 
6674  N N   . ARG C 274 ? 1.8523 2.0606 2.2174 0.4933  0.1119  -0.5304 304 ARG C N   
6675  C CA  . ARG C 274 ? 1.8498 2.0969 2.2273 0.4924  0.1164  -0.5098 304 ARG C CA  
6676  C C   . ARG C 274 ? 1.7966 2.0776 2.1741 0.5064  0.1350  -0.5194 304 ARG C C   
6677  O O   . ARG C 274 ? 1.7425 2.0202 2.1364 0.5261  0.1464  -0.5297 304 ARG C O   
6678  C CB  . ARG C 274 ? 1.8602 2.1024 2.2685 0.4970  0.1126  -0.4932 304 ARG C CB  
6679  C CG  . ARG C 274 ? 1.8347 2.1202 2.2568 0.4959  0.1181  -0.4726 304 ARG C CG  
6680  C CD  . ARG C 274 ? 1.8195 2.1039 2.2730 0.5021  0.1159  -0.4574 304 ARG C CD  
6681  N NE  . ARG C 274 ? 1.7822 2.0473 2.2348 0.4863  0.0978  -0.4414 304 ARG C NE  
6682  C CZ  . ARG C 274 ? 1.8289 2.0921 2.3049 0.4871  0.0919  -0.4256 304 ARG C CZ  
6683  N NH1 . ARG C 274 ? 1.8697 2.1508 2.3735 0.5026  0.1029  -0.4226 304 ARG C NH1 
6684  N NH2 . ARG C 274 ? 1.8161 2.0604 2.2868 0.4736  0.0751  -0.4128 304 ARG C NH2 
6685  N N   . LYS C 275 ? 1.6360 1.9499 1.9939 0.4971  0.1378  -0.5155 305 LYS C N   
6686  C CA  . LYS C 275 ? 1.6555 2.0112 2.0120 0.5088  0.1547  -0.5203 305 LYS C CA  
6687  C C   . LYS C 275 ? 1.6371 2.0323 2.0156 0.5080  0.1578  -0.4951 305 LYS C C   
6688  O O   . LYS C 275 ? 1.6181 2.0252 1.9939 0.4885  0.1471  -0.4732 305 LYS C O   
6689  C CB  . LYS C 275 ? 1.6709 2.0469 1.9968 0.4978  0.1556  -0.5258 305 LYS C CB  
6690  C CG  . LYS C 275 ? 1.6999 2.0530 2.0045 0.5053  0.1600  -0.5556 305 LYS C CG  
6691  C CD  . LYS C 275 ? 1.7175 2.1034 1.9952 0.4990  0.1652  -0.5606 305 LYS C CD  
6692  C CE  . LYS C 275 ? 1.7490 2.1141 2.0049 0.5068  0.1700  -0.5915 305 LYS C CE  
6693  N NZ  . LYS C 275 ? 1.7443 2.0642 1.9886 0.4944  0.1553  -0.5991 305 LYS C NZ  
6694  N N   . SER C 276 ? 1.6888 2.1039 2.0875 0.5293  0.1725  -0.4983 306 SER C N   
6695  C CA  . SER C 276 ? 1.6808 2.1373 2.1034 0.5315  0.1772  -0.4753 306 SER C CA  
6696  C C   . SER C 276 ? 1.7275 2.2437 2.1457 0.5371  0.1917  -0.4710 306 SER C C   
6697  O O   . SER C 276 ? 1.7623 2.3019 2.1928 0.5605  0.2076  -0.4776 306 SER C O   
6698  C CB  . SER C 276 ? 1.6744 2.1149 2.1256 0.5524  0.1830  -0.4782 306 SER C CB  
6699  O OG  . SER C 276 ? 1.7724 2.2000 2.2199 0.5771  0.1971  -0.5036 306 SER C OG  
6700  N N   . ILE C 277 ? 1.6279 2.1697 2.0274 0.5160  0.1861  -0.4589 307 ILE C N   
6701  C CA  . ILE C 277 ? 1.6063 2.2100 2.0017 0.5177  0.1982  -0.4508 307 ILE C CA  
6702  C C   . ILE C 277 ? 1.5823 2.2288 2.0044 0.5170  0.2011  -0.4251 307 ILE C C   
6703  O O   . ILE C 277 ? 1.6090 2.2414 2.0440 0.5024  0.1884  -0.4069 307 ILE C O   
6704  C CB  . ILE C 277 ? 1.6071 2.2250 1.9751 0.4932  0.1902  -0.4427 307 ILE C CB  
6705  C CG1 . ILE C 277 ? 1.5781 2.1800 1.9462 0.4657  0.1711  -0.4184 307 ILE C CG1 
6706  C CG2 . ILE C 277 ? 1.6267 2.2116 1.9679 0.4955  0.1893  -0.4686 307 ILE C CG2 
6707  C CD1 . ILE C 277 ? 1.6084 2.2217 1.9492 0.4413  0.1625  -0.4073 307 ILE C CD1 
6708  N N   . ARG C 278 ? 1.5003 2.2013 1.9303 0.5335  0.2179  -0.4232 308 ARG C N   
6709  C CA  . ARG C 278 ? 1.4869 2.2346 1.9442 0.5373  0.2233  -0.4005 308 ARG C CA  
6710  C C   . ARG C 278 ? 1.4826 2.2898 1.9343 0.5145  0.2212  -0.3746 308 ARG C C   
6711  O O   . ARG C 278 ? 1.5010 2.3538 1.9414 0.5205  0.2328  -0.3772 308 ARG C O   
6712  C CB  . ARG C 278 ? 1.5054 2.2782 1.9770 0.5730  0.2438  -0.4132 308 ARG C CB  
6713  C CG  . ARG C 278 ? 1.5171 2.2322 1.9929 0.5976  0.2477  -0.4393 308 ARG C CG  
6714  C CD  . ARG C 278 ? 1.5432 2.2857 2.0267 0.6339  0.2690  -0.4520 308 ARG C CD  
6715  N NE  . ARG C 278 ? 1.5297 2.3249 2.0413 0.6423  0.2764  -0.4287 308 ARG C NE  
6716  C CZ  . ARG C 278 ? 1.5485 2.3765 2.0713 0.6748  0.2949  -0.4332 308 ARG C CZ  
6717  N NH1 . ARG C 278 ? 1.5842 2.3934 2.0909 0.7024  0.3078  -0.4614 308 ARG C NH1 
6718  N NH2 . ARG C 278 ? 1.5337 2.4132 2.0826 0.6802  0.3004  -0.4095 308 ARG C NH2 
6719  N N   . ILE C 279 ? 1.5073 2.3134 1.9654 0.4878  0.2059  -0.3497 309 ILE C N   
6720  C CA  . ILE C 279 ? 1.5043 2.3662 1.9598 0.4640  0.2028  -0.3218 309 ILE C CA  
6721  C C   . ILE C 279 ? 1.4929 2.4023 1.9793 0.4716  0.2098  -0.3029 309 ILE C C   
6722  O O   . ILE C 279 ? 1.4753 2.3893 1.9723 0.4501  0.1977  -0.2795 309 ILE C O   
6723  C CB  . ILE C 279 ? 1.4935 2.3251 1.9325 0.4284  0.1812  -0.3053 309 ILE C CB  
6724  C CG1 . ILE C 279 ? 1.4998 2.2702 1.9133 0.4260  0.1729  -0.3263 309 ILE C CG1 
6725  C CG2 . ILE C 279 ? 1.5005 2.3864 1.9281 0.4033  0.1790  -0.2808 309 ILE C CG2 
6726  C CD1 . ILE C 279 ? 1.4924 2.2286 1.8870 0.3948  0.1520  -0.3114 309 ILE C CD1 
6727  N N   . GLY C 280 ? 1.7397 2.6842 2.2393 0.5029  0.2292  -0.3131 312 GLY C N   
6728  C CA  . GLY C 280 ? 1.7346 2.7262 2.2642 0.5156  0.2381  -0.2971 312 GLY C CA  
6729  C C   . GLY C 280 ? 1.7452 2.8116 2.2799 0.4944  0.2378  -0.2659 312 GLY C C   
6730  O O   . GLY C 280 ? 1.7810 2.8613 2.2950 0.4688  0.2304  -0.2561 312 GLY C O   
6731  N N   . PRO C 281 ? 1.6352 2.7518 2.1975 0.5044  0.2456  -0.2490 313 PRO C N   
6732  C CA  . PRO C 281 ? 1.6113 2.7117 2.1983 0.5355  0.2546  -0.2592 313 PRO C CA  
6733  C C   . PRO C 281 ? 1.5784 2.6291 2.1798 0.5224  0.2386  -0.2523 313 PRO C C   
6734  O O   . PRO C 281 ? 1.5384 2.6061 2.1460 0.4935  0.2255  -0.2271 313 PRO C O   
6735  C CB  . PRO C 281 ? 1.5864 2.7736 2.1950 0.5493  0.2696  -0.2397 313 PRO C CB  
6736  C CG  . PRO C 281 ? 1.5653 2.8024 2.1686 0.5112  0.2592  -0.2098 313 PRO C CG  
6737  C CD  . PRO C 281 ? 1.6221 2.8219 2.1929 0.4882  0.2483  -0.2187 313 PRO C CD  
6738  N N   . GLY C 282 ? 1.5946 2.5837 2.2001 0.5434  0.2394  -0.2749 314 GLY C N   
6739  C CA  . GLY C 282 ? 1.5573 2.4997 2.1774 0.5356  0.2258  -0.2705 314 GLY C CA  
6740  C C   . GLY C 282 ? 1.5799 2.4494 2.1785 0.5167  0.2082  -0.2824 314 GLY C C   
6741  O O   . GLY C 282 ? 1.5940 2.4064 2.1944 0.5313  0.2065  -0.3015 314 GLY C O   
6742  N N   . GLN C 283 ? 1.6888 2.5601 2.2661 0.4845  0.1950  -0.2705 315 GLN C N   
6743  C CA  . GLN C 283 ? 1.7128 2.5186 2.2677 0.4665  0.1779  -0.2794 315 GLN C CA  
6744  C C   . GLN C 283 ? 1.7862 2.5557 2.3216 0.4834  0.1846  -0.3092 315 GLN C C   
6745  O O   . GLN C 283 ? 1.7766 2.5773 2.3068 0.5007  0.2005  -0.3203 315 GLN C O   
6746  C CB  . GLN C 283 ? 1.6510 2.4685 2.1850 0.4298  0.1634  -0.2591 315 GLN C CB  
6747  C CG  . GLN C 283 ? 1.6312 2.4599 2.1778 0.4064  0.1498  -0.2320 315 GLN C CG  
6748  C CD  . GLN C 283 ? 1.5059 2.4106 2.0750 0.4075  0.1602  -0.2112 315 GLN C CD  
6749  O OE1 . GLN C 283 ? 1.5619 2.5156 2.1359 0.4255  0.1778  -0.2152 315 GLN C OE1 
6750  N NE2 . GLN C 283 ? 1.4371 2.3540 2.0195 0.3886  0.1491  -0.1885 315 GLN C NE2 
6751  N N   . ALA C 284 ? 1.7624 2.4666 2.2862 0.4782  0.1721  -0.3219 316 ALA C N   
6752  C CA  . ALA C 284 ? 1.7288 2.3930 2.2330 0.4903  0.1754  -0.3498 316 ALA C CA  
6753  C C   . ALA C 284 ? 1.7272 2.3370 2.2107 0.4693  0.1562  -0.3517 316 ALA C C   
6754  O O   . ALA C 284 ? 1.7113 2.2893 2.2046 0.4624  0.1436  -0.3442 316 ALA C O   
6755  C CB  . ALA C 284 ? 1.7009 2.3400 2.2221 0.5218  0.1864  -0.3704 316 ALA C CB  
6756  N N   . PHE C 285 ? 1.7179 2.3193 2.1725 0.4604  0.1544  -0.3615 317 PHE C N   
6757  C CA  . PHE C 285 ? 1.7225 2.2772 2.1536 0.4417  0.1373  -0.3631 317 PHE C CA  
6758  C C   . PHE C 285 ? 1.7334 2.2395 2.1566 0.4564  0.1378  -0.3903 317 PHE C C   
6759  O O   . PHE C 285 ? 1.7332 2.2455 2.1524 0.4742  0.1513  -0.4106 317 PHE C O   
6760  C CB  . PHE C 285 ? 1.7031 2.2781 2.1059 0.4209  0.1333  -0.3547 317 PHE C CB  
6761  C CG  . PHE C 285 ? 1.6775 2.2052 2.0533 0.4060  0.1178  -0.3588 317 PHE C CG  
6762  C CD1 . PHE C 285 ? 1.6222 2.1184 1.9949 0.3893  0.0999  -0.3436 317 PHE C CD1 
6763  C CD2 . PHE C 285 ? 1.6381 2.1550 1.9901 0.4092  0.1211  -0.3775 317 PHE C CD2 
6764  C CE1 . PHE C 285 ? 1.5747 2.0290 1.9214 0.3782  0.0862  -0.3468 317 PHE C CE1 
6765  C CE2 . PHE C 285 ? 1.5872 2.0646 1.9143 0.3964  0.1072  -0.3800 317 PHE C CE2 
6766  C CZ  . PHE C 285 ? 1.5645 2.0107 1.8889 0.3818  0.0899  -0.3644 317 PHE C CZ  
6767  N N   . TYR C 286 ? 1.7270 2.1853 2.1471 0.4487  0.1225  -0.3901 318 TYR C N   
6768  C CA  . TYR C 286 ? 1.7450 2.1559 2.1578 0.4585  0.1199  -0.4126 318 TYR C CA  
6769  C C   . TYR C 286 ? 1.7127 2.1045 2.0923 0.4423  0.1096  -0.4165 318 TYR C C   
6770  O O   . TYR C 286 ? 1.6784 2.0460 2.0478 0.4268  0.0936  -0.4046 318 TYR C O   
6771  C CB  . TYR C 286 ? 1.7616 2.1375 2.1939 0.4616  0.1099  -0.4082 318 TYR C CB  
6772  C CG  . TYR C 286 ? 1.8113 2.2052 2.2772 0.4783  0.1196  -0.4034 318 TYR C CG  
6773  C CD1 . TYR C 286 ? 1.8055 2.2407 2.2817 0.4931  0.1374  -0.4065 318 TYR C CD1 
6774  C CD2 . TYR C 286 ? 1.8196 2.1930 2.3062 0.4795  0.1110  -0.3940 318 TYR C CD2 
6775  C CE1 . TYR C 286 ? 1.7916 2.2455 2.2980 0.5097  0.1466  -0.4007 318 TYR C CE1 
6776  C CE2 . TYR C 286 ? 1.8028 2.1947 2.3202 0.4948  0.1198  -0.3882 318 TYR C CE2 
6777  C CZ  . TYR C 286 ? 1.7765 2.2083 2.3037 0.5101  0.1377  -0.3914 318 TYR C CZ  
6778  O OH  . TYR C 286 ? 1.7388 2.1902 2.2965 0.5269  0.1467  -0.3846 318 TYR C OH  
6779  N N   . ALA C 287 ? 1.7438 2.1467 2.1054 0.4472  0.1190  -0.4332 319 ALA C N   
6780  C CA  . ALA C 287 ? 1.7036 2.0936 2.0333 0.4338  0.1113  -0.4382 319 ALA C CA  
6781  C C   . ALA C 287 ? 1.7028 2.0456 2.0248 0.4388  0.1047  -0.4572 319 ALA C C   
6782  O O   . ALA C 287 ? 1.7384 2.0590 2.0791 0.4529  0.1073  -0.4680 319 ALA C O   
6783  C CB  . ALA C 287 ? 1.6738 2.1006 1.9876 0.4366  0.1244  -0.4476 319 ALA C CB  
6784  N N   . THR C 288 ? 1.7530 2.0816 2.0468 0.4266  0.0959  -0.4601 320 THR C N   
6785  C CA  . THR C 288 ? 1.7434 2.0335 2.0267 0.4292  0.0893  -0.4774 320 THR C CA  
6786  C C   . THR C 288 ? 1.7696 2.0683 2.0350 0.4353  0.0998  -0.5009 320 THR C C   
6787  O O   . THR C 288 ? 1.7195 2.0408 1.9625 0.4263  0.1012  -0.4991 320 THR C O   
6788  C CB  . THR C 288 ? 1.6979 1.9659 1.9608 0.4132  0.0717  -0.4651 320 THR C CB  
6789  O OG1 . THR C 288 ? 1.6999 1.9668 1.9731 0.4052  0.0624  -0.4410 320 THR C OG1 
6790  C CG2 . THR C 288 ? 1.7165 1.9459 1.9771 0.4170  0.0634  -0.4783 320 THR C CG2 
6791  N N   . GLY C 289 ? 1.9640 2.2446 2.2384 0.4502  0.1070  -0.5227 321 GLY C N   
6792  C CA  . GLY C 289 ? 1.9214 2.2047 2.1782 0.4569  0.1165  -0.5477 321 GLY C CA  
6793  C C   . GLY C 289 ? 1.8794 2.1391 2.1110 0.4456  0.1055  -0.5570 321 GLY C C   
6794  O O   . GLY C 289 ? 1.8671 2.1170 2.0904 0.4321  0.0915  -0.5416 321 GLY C O   
6795  N N   . ASP C 290 A 2.0218 2.2725 2.2400 0.4518  0.1118  -0.5828 321 ASP C N   
6796  C CA  . ASP C 290 A 2.0224 2.2534 2.2171 0.4415  0.1022  -0.5938 321 ASP C CA  
6797  C C   . ASP C 290 A 2.0061 2.1972 2.2124 0.4394  0.0897  -0.5929 321 ASP C C   
6798  O O   . ASP C 290 A 1.9940 2.1682 2.2256 0.4491  0.0913  -0.5916 321 ASP C O   
6799  C CB  . ASP C 290 A 2.0195 2.2533 2.1959 0.4478  0.1124  -0.6223 321 ASP C CB  
6800  C CG  . ASP C 290 A 2.0888 2.2986 2.2801 0.4644  0.1213  -0.6424 321 ASP C CG  
6801  O OD1 . ASP C 290 A 2.1373 2.3649 2.3412 0.4794  0.1348  -0.6442 321 ASP C OD1 
6802  O OD2 . ASP C 290 A 2.0812 2.2548 2.2708 0.4626  0.1146  -0.6558 321 ASP C OD2 
6803  N N   . ILE C 291 ? 1.9586 2.1375 2.1457 0.4270  0.0772  -0.5923 322 ILE C N   
6804  C CA  . ILE C 291 ? 1.9904 2.1373 2.1847 0.4232  0.0639  -0.5895 322 ILE C CA  
6805  C C   . ILE C 291 ? 1.9784 2.1021 2.1653 0.4240  0.0644  -0.6148 322 ILE C C   
6806  O O   . ILE C 291 ? 1.9188 2.0504 2.0807 0.4182  0.0660  -0.6297 322 ILE C O   
6807  C CB  . ILE C 291 ? 1.9567 2.1057 2.1340 0.4102  0.0491  -0.5714 322 ILE C CB  
6808  C CG1 . ILE C 291 ? 1.9639 2.1305 2.1458 0.4078  0.0476  -0.5464 322 ILE C CG1 
6809  C CG2 . ILE C 291 ? 1.9879 2.1084 2.1728 0.4078  0.0356  -0.5675 322 ILE C CG2 
6810  C CD1 . ILE C 291 ? 1.9254 2.0893 2.0886 0.3971  0.0331  -0.5279 322 ILE C CD1 
6811  N N   . ILE C 292 ? 2.0269 2.1223 2.2351 0.4304  0.0627  -0.6192 323 ILE C N   
6812  C CA  . ILE C 292 ? 2.0138 2.0810 2.2176 0.4300  0.0619  -0.6416 323 ILE C CA  
6813  C C   . ILE C 292 ? 1.9777 2.0311 2.1731 0.4165  0.0453  -0.6361 323 ILE C C   
6814  O O   . ILE C 292 ? 2.0081 2.0494 2.2214 0.4161  0.0358  -0.6201 323 ILE C O   
6815  C CB  . ILE C 292 ? 2.0655 2.1077 2.2958 0.4437  0.0684  -0.6482 323 ILE C CB  
6816  C CG1 . ILE C 292 ? 2.0794 2.1402 2.3188 0.4594  0.0852  -0.6512 323 ILE C CG1 
6817  C CG2 . ILE C 292 ? 2.0626 2.0716 2.2849 0.4417  0.0671  -0.6721 323 ILE C CG2 
6818  C CD1 . ILE C 292 ? 2.1104 2.1758 2.3811 0.4692  0.0872  -0.6312 323 ILE C CD1 
6819  N N   . GLY C 293 ? 2.0698 2.1281 2.2377 0.4058  0.0418  -0.6488 324 GLY C N   
6820  C CA  . GLY C 293 ? 2.0626 2.1129 2.2199 0.3929  0.0268  -0.6450 324 GLY C CA  
6821  C C   . GLY C 293 ? 2.0527 2.1302 2.1849 0.3837  0.0205  -0.6338 324 GLY C C   
6822  O O   . GLY C 293 ? 2.0656 2.1653 2.1802 0.3834  0.0285  -0.6396 324 GLY C O   
6823  N N   . ASP C 294 ? 2.2029 2.2792 2.3332 0.3774  0.0063  -0.6171 325 ASP C N   
6824  C CA  . ASP C 294 ? 2.1507 2.2491 2.2558 0.3700  -0.0012 -0.6051 325 ASP C CA  
6825  C C   . ASP C 294 ? 2.1504 2.2589 2.2598 0.3751  -0.0025 -0.5809 325 ASP C C   
6826  O O   . ASP C 294 ? 2.1687 2.2650 2.3019 0.3820  -0.0039 -0.5687 325 ASP C O   
6827  C CB  . ASP C 294 ? 2.1490 2.2429 2.2462 0.3617  -0.0160 -0.6003 325 ASP C CB  
6828  C CG  . ASP C 294 ? 2.1533 2.2372 2.2440 0.3531  -0.0163 -0.6236 325 ASP C CG  
6829  O OD1 . ASP C 294 ? 2.1472 2.2375 2.2232 0.3505  -0.0070 -0.6435 325 ASP C OD1 
6830  O OD2 . ASP C 294 ? 2.1703 2.2407 2.2694 0.3482  -0.0263 -0.6218 325 ASP C OD2 
6831  N N   . ILE C 295 ? 2.1672 2.2977 2.2522 0.3709  -0.0026 -0.5737 326 ILE C N   
6832  C CA  . ILE C 295 ? 2.1643 2.3023 2.2472 0.3731  -0.0053 -0.5502 326 ILE C CA  
6833  C C   . ILE C 295 ? 2.1893 2.3186 2.2653 0.3721  -0.0211 -0.5315 326 ILE C C   
6834  O O   . ILE C 295 ? 2.2406 2.3805 2.2906 0.3674  -0.0279 -0.5270 326 ILE C O   
6835  C CB  . ILE C 295 ? 2.1807 2.3444 2.2398 0.3690  0.0012  -0.5492 326 ILE C CB  
6836  C CG1 . ILE C 295 ? 2.1514 2.3267 2.2173 0.3721  0.0172  -0.5680 326 ILE C CG1 
6837  C CG2 . ILE C 295 ? 2.1632 2.3304 2.2185 0.3691  -0.0029 -0.5242 326 ILE C CG2 
6838  C CD1 . ILE C 295 ? 2.1011 2.2704 2.1960 0.3807  0.0247  -0.5634 326 ILE C CD1 
6839  N N   . ARG C 296 ? 2.1686 2.2797 2.2675 0.3779  -0.0266 -0.5206 327 ARG C N   
6840  C CA  . ARG C 296 ? 2.1841 2.2859 2.2794 0.3799  -0.0412 -0.5025 327 ARG C CA  
6841  C C   . ARG C 296 ? 2.1640 2.2581 2.2676 0.3849  -0.0439 -0.4822 327 ARG C C   
6842  O O   . ARG C 296 ? 2.1228 2.2175 2.2434 0.3867  -0.0348 -0.4826 327 ARG C O   
6843  C CB  . ARG C 296 ? 2.1485 2.2362 2.2630 0.3815  -0.0471 -0.5082 327 ARG C CB  
6844  C CG  . ARG C 296 ? 2.1996 2.2951 2.2981 0.3740  -0.0509 -0.5212 327 ARG C CG  
6845  C CD  . ARG C 296 ? 2.1556 2.2368 2.2749 0.3732  -0.0557 -0.5279 327 ARG C CD  
6846  N NE  . ARG C 296 ? 2.1256 2.1959 2.2622 0.3804  -0.0655 -0.5096 327 ARG C NE  
6847  C CZ  . ARG C 296 ? 2.1517 2.2109 2.3085 0.3804  -0.0708 -0.5109 327 ARG C CZ  
6848  N NH1 . ARG C 296 ? 2.1195 2.1718 2.2914 0.3877  -0.0797 -0.4937 327 ARG C NH1 
6849  N NH2 . ARG C 296 ? 2.2237 2.2783 2.3839 0.3724  -0.0678 -0.5296 327 ARG C NH2 
6850  N N   . GLN C 297 ? 2.0912 2.1785 2.1811 0.3873  -0.0567 -0.4642 328 GLN C N   
6851  C CA  . GLN C 297 ? 2.0798 2.1559 2.1719 0.3911  -0.0621 -0.4442 328 GLN C CA  
6852  C C   . GLN C 297 ? 2.0286 2.0882 2.1426 0.3986  -0.0708 -0.4367 328 GLN C C   
6853  O O   . GLN C 297 ? 2.0207 2.0788 2.1384 0.4007  -0.0766 -0.4412 328 GLN C O   
6854  C CB  . GLN C 297 ? 2.1543 2.2309 2.2111 0.3900  -0.0707 -0.4289 328 GLN C CB  
6855  C CG  . GLN C 297 ? 2.2544 2.3367 2.2894 0.3914  -0.0790 -0.4304 328 GLN C CG  
6856  C CD  . GLN C 297 ? 2.3581 2.4436 2.3554 0.3911  -0.0847 -0.4174 328 GLN C CD  
6857  O OE1 . GLN C 297 ? 2.3416 2.4433 2.3175 0.3882  -0.0844 -0.4230 328 GLN C OE1 
6858  N NE2 . GLN C 297 ? 2.4407 2.5099 2.4287 0.3937  -0.0903 -0.3996 328 GLN C NE2 
6859  N N   . ALA C 298 ? 2.1508 2.2004 2.2793 0.4017  -0.0717 -0.4246 329 ALA C N   
6860  C CA  . ALA C 298 ? 2.0479 2.0836 2.1980 0.4093  -0.0795 -0.4163 329 ALA C CA  
6861  C C   . ALA C 298 ? 2.0424 2.0703 2.1713 0.4148  -0.0948 -0.4034 329 ALA C C   
6862  O O   . ALA C 298 ? 2.1091 2.1367 2.2059 0.4138  -0.1000 -0.3951 329 ALA C O   
6863  C CB  . ALA C 298 ? 2.0178 2.0472 2.1847 0.4104  -0.0774 -0.4055 329 ALA C CB  
6864  N N   . HIS C 299 ? 2.0445 2.0670 2.1910 0.4217  -0.1018 -0.4011 330 HIS C N   
6865  C CA  . HIS C 299 ? 2.0696 2.0883 2.1981 0.4293  -0.1161 -0.3888 330 HIS C CA  
6866  C C   . HIS C 299 ? 2.0777 2.0884 2.2325 0.4378  -0.1228 -0.3815 330 HIS C C   
6867  O O   . HIS C 299 ? 2.0453 2.0557 2.2330 0.4368  -0.1162 -0.3887 330 HIS C O   
6868  C CB  . HIS C 299 ? 2.1437 2.1774 2.2557 0.4267  -0.1181 -0.3971 330 HIS C CB  
6869  C CG  . HIS C 299 ? 2.1551 2.1957 2.2931 0.4226  -0.1138 -0.4115 330 HIS C CG  
6870  N ND1 . HIS C 299 ? 2.2766 2.3209 2.4264 0.4140  -0.1011 -0.4296 330 HIS C ND1 
6871  C CD2 . HIS C 299 ? 2.0662 2.1091 2.2198 0.4258  -0.1209 -0.4101 330 HIS C CD2 
6872  C CE1 . HIS C 299 ? 2.1780 2.2226 2.3480 0.4117  -0.1008 -0.4393 330 HIS C CE1 
6873  N NE2 . HIS C 299 ? 2.0699 2.1148 2.2435 0.4178  -0.1128 -0.4271 330 HIS C NE2 
6874  N N   . CYS C 300 ? 2.1386 2.1431 2.2777 0.4476  -0.1360 -0.3667 331 CYS C N   
6875  C CA  . CYS C 300 ? 2.0890 2.0888 2.2487 0.4574  -0.1442 -0.3577 331 CYS C CA  
6876  C C   . CYS C 300 ? 2.1161 2.1261 2.2611 0.4655  -0.1556 -0.3516 331 CYS C C   
6877  O O   . CYS C 300 ? 2.1713 2.1827 2.2815 0.4694  -0.1617 -0.3455 331 CYS C O   
6878  C CB  . CYS C 300 ? 2.0664 2.0482 2.2209 0.4634  -0.1499 -0.3436 331 CYS C CB  
6879  S SG  . CYS C 300 ? 2.0278 2.0026 2.2103 0.4557  -0.1388 -0.3458 331 CYS C SG  
6880  N N   . ASN C 301 ? 2.0954 2.1143 2.2663 0.4683  -0.1587 -0.3523 332 ASN C N   
6881  C CA  . ASN C 301 ? 2.1165 2.1510 2.2776 0.4754  -0.1696 -0.3452 332 ASN C CA  
6882  C C   . ASN C 301 ? 2.0990 2.1301 2.2681 0.4902  -0.1806 -0.3297 332 ASN C C   
6883  O O   . ASN C 301 ? 2.0698 2.0939 2.2697 0.4913  -0.1786 -0.3286 332 ASN C O   
6884  C CB  . ASN C 301 ? 2.1034 2.1546 2.2844 0.4661  -0.1668 -0.3560 332 ASN C CB  
6885  C CG  . ASN C 301 ? 2.1517 2.2123 2.3150 0.4537  -0.1602 -0.3698 332 ASN C CG  
6886  O OD1 . ASN C 301 ? 2.2119 2.2788 2.3419 0.4556  -0.1630 -0.3664 332 ASN C OD1 
6887  N ND2 . ASN C 301 ? 2.1279 2.1897 2.3123 0.4418  -0.1519 -0.3852 332 ASN C ND2 
6888  N N   . VAL C 302 ? 2.0846 2.1220 2.2251 0.5026  -0.1920 -0.3176 333 VAL C N   
6889  C CA  . VAL C 302 ? 2.0904 2.1285 2.2325 0.5192  -0.2037 -0.3027 333 VAL C CA  
6890  C C   . VAL C 302 ? 2.1135 2.1799 2.2464 0.5260  -0.2124 -0.2965 333 VAL C C   
6891  O O   . VAL C 302 ? 2.1499 2.2264 2.2509 0.5278  -0.2148 -0.2954 333 VAL C O   
6892  C CB  . VAL C 302 ? 2.1174 2.1324 2.2287 0.5316  -0.2103 -0.2920 333 VAL C CB  
6893  C CG1 . VAL C 302 ? 2.1302 2.1482 2.2371 0.5512  -0.2233 -0.2774 333 VAL C CG1 
6894  C CG2 . VAL C 302 ? 2.0936 2.0847 2.2185 0.5237  -0.2031 -0.2957 333 VAL C CG2 
6895  N N   . SER C 303 ? 2.1077 2.1893 2.2688 0.5295  -0.2170 -0.2914 334 SER C N   
6896  C CA  . SER C 303 ? 2.1780 2.2916 2.3355 0.5346  -0.2257 -0.2837 334 SER C CA  
6897  C C   . SER C 303 ? 2.2556 2.3764 2.3738 0.5549  -0.2366 -0.2695 334 SER C C   
6898  O O   . SER C 303 ? 2.2876 2.3959 2.3984 0.5719  -0.2435 -0.2589 334 SER C O   
6899  C CB  . SER C 303 ? 2.1426 2.2682 2.3381 0.5362  -0.2293 -0.2779 334 SER C CB  
6900  O OG  . SER C 303 ? 2.1409 2.2463 2.3499 0.5459  -0.2301 -0.2725 334 SER C OG  
6901  N N   . LYS C 304 ? 2.2378 2.3790 2.3297 0.5533  -0.2381 -0.2698 335 LYS C N   
6902  C CA  . LYS C 304 ? 2.2890 2.4390 2.3394 0.5731  -0.2472 -0.2571 335 LYS C CA  
6903  C C   . LYS C 304 ? 2.3003 2.4683 2.3522 0.5941  -0.2591 -0.2408 335 LYS C C   
6904  O O   . LYS C 304 ? 2.3344 2.4923 2.3555 0.6161  -0.2666 -0.2300 335 LYS C O   
6905  C CB  . LYS C 304 ? 2.3209 2.4986 2.3512 0.5650  -0.2458 -0.2606 335 LYS C CB  
6906  C CG  . LYS C 304 ? 2.3725 2.5550 2.3547 0.5828  -0.2516 -0.2506 335 LYS C CG  
6907  C CD  . LYS C 304 ? 2.4006 2.6171 2.3690 0.5723  -0.2497 -0.2543 335 LYS C CD  
6908  C CE  . LYS C 304 ? 2.4573 2.6838 2.3779 0.5915  -0.2552 -0.2430 335 LYS C CE  
6909  N NZ  . LYS C 304 ? 2.4959 2.7438 2.4011 0.6182  -0.2672 -0.2244 335 LYS C NZ  
6910  N N   . ALA C 305 ? 2.4672 2.6613 2.5536 0.5882  -0.2612 -0.2386 336 ALA C N   
6911  C CA  . ALA C 305 ? 2.4658 2.6824 2.5559 0.6078  -0.2724 -0.2223 336 ALA C CA  
6912  C C   . ALA C 305 ? 2.4505 2.6373 2.5467 0.6219  -0.2750 -0.2178 336 ALA C C   
6913  O O   . ALA C 305 ? 2.5214 2.7074 2.5928 0.6451  -0.2839 -0.2055 336 ALA C O   
6914  C CB  . ALA C 305 ? 2.3996 2.6508 2.5269 0.5949  -0.2738 -0.2204 336 ALA C CB  
6915  N N   . THR C 306 ? 2.1572 2.3179 2.2827 0.6076  -0.2668 -0.2280 337 THR C N   
6916  C CA  . THR C 306 ? 2.1376 2.2725 2.2718 0.6182  -0.2691 -0.2241 337 THR C CA  
6917  C C   . THR C 306 ? 2.1701 2.2709 2.2623 0.6294  -0.2712 -0.2224 337 THR C C   
6918  O O   . THR C 306 ? 2.1866 2.2714 2.2593 0.6297  -0.2725 -0.2092 337 THR C O   
6919  C CB  . THR C 306 ? 2.0872 2.2059 2.2626 0.5995  -0.2588 -0.2349 337 THR C CB  
6920  O OG1 . THR C 306 ? 2.0560 2.2019 2.2668 0.5874  -0.2567 -0.2364 337 THR C OG1 
6921  C CG2 . THR C 306 ? 2.0775 2.1750 2.2610 0.5989  -0.2577 -0.2261 337 THR C CG2 
6922  N N   . TRP C 307 ? 2.0605 2.1457 2.1313 0.6197  -0.2650 -0.2315 338 TRP C N   
6923  C CA  . TRP C 307 ? 2.0957 2.1453 2.1268 0.6286  -0.2672 -0.2298 338 TRP C CA  
6924  C C   . TRP C 307 ? 2.1548 2.2100 2.1424 0.6544  -0.2786 -0.2171 338 TRP C C   
6925  O O   . TRP C 307 ? 2.1881 2.2110 2.1432 0.6625  -0.2825 -0.2104 338 TRP C O   
6926  C CB  . TRP C 307 ? 2.1011 2.1369 2.1209 0.6102  -0.2571 -0.2413 338 TRP C CB  
6927  C CG  . TRP C 307 ? 2.1370 2.1338 2.1203 0.6147  -0.2586 -0.2396 338 TRP C CG  
6928  C CD1 . TRP C 307 ? 2.1938 2.1808 2.1317 0.6226  -0.2614 -0.2358 338 TRP C CD1 
6929  C CD2 . TRP C 307 ? 2.1228 2.0847 2.1116 0.6098  -0.2574 -0.2409 338 TRP C CD2 
6930  N NE1 . TRP C 307 ? 2.2189 2.1640 2.1327 0.6228  -0.2626 -0.2345 338 TRP C NE1 
6931  C CE2 . TRP C 307 ? 2.1753 2.1053 2.1197 0.6140  -0.2604 -0.2376 338 TRP C CE2 
6932  C CE3 . TRP C 307 ? 2.0742 2.0298 2.1006 0.6020  -0.2542 -0.2437 338 TRP C CE3 
6933  C CZ2 . TRP C 307 ? 2.1812 2.0734 2.1176 0.6087  -0.2611 -0.2370 338 TRP C CZ2 
6934  C CZ3 . TRP C 307 ? 2.0778 1.9991 2.0969 0.5978  -0.2544 -0.2432 338 TRP C CZ3 
6935  C CH2 . TRP C 307 ? 2.1310 2.0209 2.1054 0.6002  -0.2582 -0.2399 338 TRP C CH2 
6936  N N   . ASN C 308 ? 2.3139 2.4089 2.2970 0.6601  -0.2818 -0.2120 339 ASN C N   
6937  C CA  . ASN C 308 ? 2.3753 2.4793 2.3144 0.6779  -0.2887 -0.1977 339 ASN C CA  
6938  C C   . ASN C 308 ? 2.3874 2.4868 2.3199 0.6742  -0.2886 -0.1827 339 ASN C C   
6939  O O   . ASN C 308 ? 2.4350 2.5128 2.3256 0.6832  -0.2907 -0.1740 339 ASN C O   
6940  C CB  . ASN C 308 ? 2.3878 2.5436 2.3304 0.6834  -0.2919 -0.1954 339 ASN C CB  
6941  C CG  . ASN C 308 ? 2.5494 2.7124 2.4429 0.6999  -0.2958 -0.1882 339 ASN C CG  
6942  O OD1 . ASN C 308 ? 2.5668 2.6925 2.4223 0.7090  -0.2964 -0.1870 339 ASN C OD1 
6943  N ND2 . ASN C 308 ? 2.8089 3.0220 2.7028 0.7033  -0.2989 -0.1820 339 ASN C ND2 
6944  N N   . GLU C 309 ? 2.4202 2.5388 2.3933 0.6614  -0.2857 -0.1802 340 GLU C N   
6945  C CA  . GLU C 309 ? 2.4052 2.5228 2.3762 0.6574  -0.2847 -0.1666 340 GLU C CA  
6946  C C   . GLU C 309 ? 2.3556 2.4282 2.3215 0.6526  -0.2832 -0.1687 340 GLU C C   
6947  O O   . GLU C 309 ? 2.4043 2.4615 2.3450 0.6560  -0.2845 -0.1596 340 GLU C O   
6948  C CB  . GLU C 309 ? 2.4316 2.5875 2.4452 0.6464  -0.2827 -0.1609 340 GLU C CB  
6949  C CG  . GLU C 309 ? 2.4607 2.6296 2.5200 0.6368  -0.2809 -0.1734 340 GLU C CG  
6950  C CD  . GLU C 309 ? 2.5070 2.7132 2.6042 0.6274  -0.2806 -0.1659 340 GLU C CD  
6951  O OE1 . GLU C 309 ? 2.4952 2.6956 2.6154 0.6175  -0.2767 -0.1594 340 GLU C OE1 
6952  O OE2 . GLU C 309 ? 2.5735 2.8172 2.6767 0.6303  -0.2850 -0.1656 340 GLU C OE2 
6953  N N   . THR C 310 ? 2.2190 2.2716 2.2094 0.6446  -0.2804 -0.1812 341 THR C N   
6954  C CA  . THR C 310 ? 2.1781 2.1916 2.1671 0.6387  -0.2794 -0.1831 341 THR C CA  
6955  C C   . THR C 310 ? 2.2141 2.1909 2.1505 0.6510  -0.2851 -0.1820 341 THR C C   
6956  O O   . THR C 310 ? 2.2643 2.2147 2.1812 0.6514  -0.2878 -0.1764 341 THR C O   
6957  C CB  . THR C 310 ? 2.1029 2.1070 2.1292 0.6280  -0.2741 -0.1972 341 THR C CB  
6958  O OG1 . THR C 310 ? 2.1035 2.1386 2.1769 0.6173  -0.2688 -0.1984 341 THR C OG1 
6959  C CG2 . THR C 310 ? 2.0728 2.0411 2.0994 0.6215  -0.2733 -0.1982 341 THR C CG2 
6960  N N   . LEU C 311 ? 2.2150 2.1886 2.1272 0.6617  -0.2875 -0.1874 342 LEU C N   
6961  C CA  . LEU C 311 ? 2.2818 2.2183 2.1412 0.6744  -0.2931 -0.1850 342 LEU C CA  
6962  C C   . LEU C 311 ? 2.4179 2.3586 2.2415 0.6841  -0.2962 -0.1719 342 LEU C C   
6963  O O   . LEU C 311 ? 2.4783 2.3821 2.2653 0.6900  -0.3005 -0.1682 342 LEU C O   
6964  C CB  . LEU C 311 ? 2.3084 2.2455 2.1492 0.6849  -0.2943 -0.1918 342 LEU C CB  
6965  C CG  . LEU C 311 ? 2.3116 2.2073 2.1448 0.6841  -0.2949 -0.2019 342 LEU C CG  
6966  C CD1 . LEU C 311 ? 2.3507 2.2479 2.1565 0.6884  -0.2932 -0.2050 342 LEU C CD1 
6967  C CD2 . LEU C 311 ? 2.3675 2.2149 2.1676 0.6854  -0.3005 -0.1957 342 LEU C CD2 
6968  N N   . GLY C 312 ? 2.5153 2.5003 2.3488 0.6859  -0.2941 -0.1654 343 GLY C N   
6969  C CA  . GLY C 312 ? 2.6165 2.6104 2.4194 0.6949  -0.2950 -0.1537 343 GLY C CA  
6970  C C   . GLY C 312 ? 2.5768 2.5615 2.3912 0.6868  -0.2940 -0.1489 343 GLY C C   
6971  O O   . GLY C 312 ? 2.6148 2.5927 2.3980 0.6951  -0.2952 -0.1417 343 GLY C O   
6972  N N   . LYS C 313 ? 2.5099 2.4953 2.3689 0.6713  -0.2913 -0.1531 344 LYS C N   
6973  C CA  . LYS C 313 ? 2.4501 2.4289 2.3244 0.6626  -0.2901 -0.1487 344 LYS C CA  
6974  C C   . LYS C 313 ? 2.4592 2.3877 2.3082 0.6640  -0.2949 -0.1527 344 LYS C C   
6975  O O   . LYS C 313 ? 2.4500 2.3662 2.2904 0.6632  -0.2965 -0.1484 344 LYS C O   
6976  C CB  . LYS C 313 ? 2.3765 2.3781 2.3092 0.6459  -0.2845 -0.1510 344 LYS C CB  
6977  C CG  . LYS C 313 ? 2.3126 2.3183 2.2697 0.6357  -0.2817 -0.1446 344 LYS C CG  
6978  C CD  . LYS C 313 ? 2.2208 2.2565 2.2340 0.6215  -0.2754 -0.1447 344 LYS C CD  
6979  C CE  . LYS C 313 ? 2.1572 2.1799 2.1932 0.6154  -0.2732 -0.1578 344 LYS C CE  
6980  N NZ  . LYS C 313 ? 2.0888 2.1374 2.1773 0.6028  -0.2668 -0.1596 344 LYS C NZ  
6981  N N   . VAL C 314 ? 2.3236 2.2227 2.1599 0.6663  -0.2978 -0.1610 345 VAL C N   
6982  C CA  . VAL C 314 ? 2.3513 2.2001 2.1614 0.6675  -0.3038 -0.1643 345 VAL C CA  
6983  C C   . VAL C 314 ? 2.4359 2.2563 2.1852 0.6839  -0.3103 -0.1600 345 VAL C C   
6984  O O   . VAL C 314 ? 2.4652 2.2545 2.1897 0.6863  -0.3156 -0.1583 345 VAL C O   
6985  C CB  . VAL C 314 ? 2.3359 2.1636 2.1569 0.6630  -0.3041 -0.1743 345 VAL C CB  
6986  C CG1 . VAL C 314 ? 2.3790 2.1514 2.1663 0.6654  -0.3121 -0.1764 345 VAL C CG1 
6987  C CG2 . VAL C 314 ? 2.2543 2.1062 2.1349 0.6470  -0.2968 -0.1799 345 VAL C CG2 
6988  N N   . VAL C 315 ? 2.5696 2.4008 2.2934 0.6961  -0.3100 -0.1584 346 VAL C N   
6989  C CA  . VAL C 315 ? 2.6581 2.4624 2.3225 0.7132  -0.3149 -0.1545 346 VAL C CA  
6990  C C   . VAL C 315 ? 2.6855 2.5005 2.3345 0.7189  -0.3142 -0.1478 346 VAL C C   
6991  O O   . VAL C 315 ? 2.7532 2.5339 2.3546 0.7308  -0.3191 -0.1465 346 VAL C O   
6992  C CB  . VAL C 315 ? 2.6961 2.5178 2.3414 0.7250  -0.3132 -0.1535 346 VAL C CB  
6993  C CG1 . VAL C 315 ? 2.6698 2.5512 2.3409 0.7245  -0.3068 -0.1486 346 VAL C CG1 
6994  C CG2 . VAL C 315 ? 2.7944 2.5813 2.3763 0.7430  -0.3178 -0.1499 346 VAL C CG2 
6995  N N   . LYS C 316 ? 2.6775 2.5381 2.3654 0.7108  -0.3082 -0.1437 347 LYS C N   
6996  C CA  . LYS C 316 ? 2.7120 2.5842 2.3875 0.7160  -0.3070 -0.1376 347 LYS C CA  
6997  C C   . LYS C 316 ? 2.6522 2.4894 2.3230 0.7113  -0.3118 -0.1400 347 LYS C C   
6998  O O   . LYS C 316 ? 2.6948 2.5239 2.3382 0.7201  -0.3134 -0.1375 347 LYS C O   
6999  C CB  . LYS C 316 ? 2.6701 2.5994 2.3883 0.7079  -0.2996 -0.1312 347 LYS C CB  
7000  C CG  . LYS C 316 ? 2.8230 2.7885 2.5334 0.7168  -0.2961 -0.1270 347 LYS C CG  
7001  C CD  . LYS C 316 ? 2.9595 2.9178 2.6162 0.7365  -0.2965 -0.1231 347 LYS C CD  
7002  C CE  . LYS C 316 ? 3.0365 3.0362 2.6878 0.7450  -0.2922 -0.1178 347 LYS C CE  
7003  N NZ  . LYS C 316 ? 3.0312 3.0276 2.6832 0.7452  -0.2940 -0.1227 347 LYS C NZ  
7004  N N   . GLN C 317 ? 2.5140 2.3315 2.2106 0.6983  -0.3141 -0.1454 348 GLN C N   
7005  C CA  . GLN C 317 ? 2.5092 2.2923 2.2014 0.6934  -0.3198 -0.1480 348 GLN C CA  
7006  C C   . GLN C 317 ? 2.5793 2.3029 2.2209 0.7024  -0.3296 -0.1527 348 GLN C C   
7007  O O   . GLN C 317 ? 2.6098 2.2981 2.2276 0.7044  -0.3369 -0.1543 348 GLN C O   
7008  C CB  . GLN C 317 ? 2.4268 2.2196 2.1730 0.6749  -0.3169 -0.1509 348 GLN C CB  
7009  C CG  . GLN C 317 ? 2.3572 2.2024 2.1550 0.6641  -0.3078 -0.1458 348 GLN C CG  
7010  C CD  . GLN C 317 ? 2.3569 2.2134 2.1539 0.6648  -0.3074 -0.1399 348 GLN C CD  
7011  O OE1 . GLN C 317 ? 2.3905 2.2137 2.1586 0.6697  -0.3142 -0.1420 348 GLN C OE1 
7012  N NE2 . GLN C 317 ? 2.3198 2.2225 2.1489 0.6596  -0.2999 -0.1327 348 GLN C NE2 
7013  N N   . LEU C 318 ? 2.5786 2.2899 2.2025 0.7079  -0.3304 -0.1545 349 LEU C N   
7014  C CA  . LEU C 318 ? 2.6515 2.3042 2.2260 0.7161  -0.3396 -0.1573 349 LEU C CA  
7015  C C   . LEU C 318 ? 2.7442 2.3754 2.2604 0.7345  -0.3433 -0.1544 349 LEU C C   
7016  O O   . LEU C 318 ? 2.8102 2.3858 2.2814 0.7407  -0.3527 -0.1563 349 LEU C O   
7017  C CB  . LEU C 318 ? 2.6539 2.3041 2.2297 0.7166  -0.3382 -0.1595 349 LEU C CB  
7018  C CG  . LEU C 318 ? 2.5724 2.2379 2.2017 0.7002  -0.3344 -0.1648 349 LEU C CG  
7019  C CD1 . LEU C 318 ? 2.5851 2.2454 2.2092 0.7035  -0.3334 -0.1680 349 LEU C CD1 
7020  C CD2 . LEU C 318 ? 2.5528 2.1825 2.1911 0.6891  -0.3405 -0.1683 349 LEU C CD2 
7021  N N   . ARG C 319 ? 2.8628 2.5361 2.3781 0.7436  -0.3362 -0.1499 350 ARG C N   
7022  C CA  . ARG C 319 ? 3.0148 2.6726 2.4765 0.7628  -0.3379 -0.1478 350 ARG C CA  
7023  C C   . ARG C 319 ? 3.0192 2.6603 2.4684 0.7645  -0.3422 -0.1494 350 ARG C C   
7024  O O   . ARG C 319 ? 3.1634 2.7794 2.5629 0.7810  -0.3455 -0.1500 350 ARG C O   
7025  C CB  . ARG C 319 ? 3.0377 2.7483 2.5029 0.7725  -0.3283 -0.1423 350 ARG C CB  
7026  C CG  . ARG C 319 ? 3.0545 2.7827 2.5224 0.7752  -0.3246 -0.1407 350 ARG C CG  
7027  C CD  . ARG C 319 ? 3.1297 2.9059 2.5917 0.7872  -0.3164 -0.1347 350 ARG C CD  
7028  N NE  . ARG C 319 ? 3.1102 2.9075 2.5750 0.7903  -0.3132 -0.1330 350 ARG C NE  
7029  C CZ  . ARG C 319 ? 3.0490 2.8938 2.5606 0.7791  -0.3084 -0.1318 350 ARG C CZ  
7030  N NH1 . ARG C 319 ? 2.9899 2.8636 2.5486 0.7641  -0.3059 -0.1312 350 ARG C NH1 
7031  N NH2 . ARG C 319 ? 3.0286 2.8919 2.5396 0.7832  -0.3065 -0.1311 350 ARG C NH2 
7032  N N   . LYS C 320 ? 2.9976 2.6526 2.4901 0.7487  -0.3420 -0.1504 351 LYS C N   
7033  C CA  . LYS C 320 ? 2.9903 2.6311 2.4738 0.7496  -0.3466 -0.1522 351 LYS C CA  
7034  C C   . LYS C 320 ? 3.0310 2.6039 2.4766 0.7507  -0.3598 -0.1579 351 LYS C C   
7035  O O   . LYS C 320 ? 3.0640 2.6159 2.4912 0.7541  -0.3661 -0.1606 351 LYS C O   
7036  C CB  . LYS C 320 ? 2.8806 2.5619 2.4256 0.7319  -0.3413 -0.1503 351 LYS C CB  
7037  C CG  . LYS C 320 ? 2.8436 2.5886 2.4233 0.7302  -0.3297 -0.1435 351 LYS C CG  
7038  C CD  . LYS C 320 ? 2.7013 2.4801 2.3388 0.7126  -0.3249 -0.1408 351 LYS C CD  
7039  C CE  . LYS C 320 ? 2.6610 2.4982 2.3281 0.7110  -0.3148 -0.1328 351 LYS C CE  
7040  N NZ  . LYS C 320 ? 2.7452 2.6082 2.4235 0.7109  -0.3096 -0.1304 351 LYS C NZ  
7041  N N   . HIS C 321 ? 3.0341 2.5712 2.4662 0.7478  -0.3647 -0.1595 352 HIS C N   
7042  C CA  . HIS C 321 ? 3.0864 2.5552 2.4822 0.7466  -0.3781 -0.1636 352 HIS C CA  
7043  C C   . HIS C 321 ? 3.1877 2.6087 2.5250 0.7598  -0.3835 -0.1632 352 HIS C C   
7044  O O   . HIS C 321 ? 3.2582 2.6158 2.5499 0.7628  -0.3957 -0.1657 352 HIS C O   
7045  C CB  . HIS C 321 ? 3.0187 2.4809 2.4561 0.7269  -0.3803 -0.1653 352 HIS C CB  
7046  C CG  . HIS C 321 ? 2.9233 2.4284 2.4185 0.7133  -0.3751 -0.1655 352 HIS C CG  
7047  N ND1 . HIS C 321 ? 2.8450 2.4141 2.3924 0.7069  -0.3621 -0.1623 352 HIS C ND1 
7048  C CD2 . HIS C 321 ? 2.8977 2.3901 2.4053 0.7050  -0.3812 -0.1679 352 HIS C CD2 
7049  C CE1 . HIS C 321 ? 2.7761 2.3693 2.3660 0.6950  -0.3597 -0.1623 352 HIS C CE1 
7050  N NE2 . HIS C 321 ? 2.8046 2.3542 2.3722 0.6942  -0.3709 -0.1657 352 HIS C NE2 
7051  N N   . PHE C 322 ? 3.2135 2.6616 2.5503 0.7672  -0.3753 -0.1597 353 PHE C N   
7052  C CA  . PHE C 322 ? 3.3069 2.7158 2.5922 0.7800  -0.3786 -0.1580 353 PHE C CA  
7053  C C   . PHE C 322 ? 3.3673 2.8009 2.6231 0.8007  -0.3715 -0.1554 353 PHE C C   
7054  O O   . PHE C 322 ? 3.4297 2.8597 2.6598 0.8117  -0.3686 -0.1524 353 PHE C O   
7055  C CB  . PHE C 322 ? 3.2727 2.6895 2.5825 0.7710  -0.3755 -0.1564 353 PHE C CB  
7056  C CG  . PHE C 322 ? 3.2329 2.6168 2.5632 0.7529  -0.3828 -0.1593 353 PHE C CG  
7057  C CD1 . PHE C 322 ? 3.3059 2.6186 2.5924 0.7518  -0.3944 -0.1593 353 PHE C CD1 
7058  C CD2 . PHE C 322 ? 3.1272 2.5504 2.5201 0.7365  -0.3780 -0.1616 353 PHE C CD2 
7059  C CE1 . PHE C 322 ? 3.2723 2.5550 2.5776 0.7345  -0.4013 -0.1614 353 PHE C CE1 
7060  C CE2 . PHE C 322 ? 3.0928 2.4883 2.5056 0.7209  -0.3839 -0.1646 353 PHE C CE2 
7061  C CZ  . PHE C 322 ? 3.1647 2.4905 2.5339 0.7198  -0.3957 -0.1645 353 PHE C CZ  
7062  N N   . GLY C 323 ? 3.3537 2.8128 2.6127 0.8066  -0.3686 -0.1564 354 GLY C N   
7063  C CA  . GLY C 323 ? 3.4953 2.9818 2.7296 0.8263  -0.3609 -0.1541 354 GLY C CA  
7064  C C   . GLY C 323 ? 3.4863 3.0493 2.7693 0.8226  -0.3479 -0.1492 354 GLY C C   
7065  O O   . GLY C 323 ? 3.3948 2.9842 2.7148 0.8111  -0.3438 -0.1469 354 GLY C O   
7066  N N   . ASN C 324 ? 3.4599 3.0566 2.7388 0.8337  -0.3416 -0.1477 355 ASN C N   
7067  C CA  . ASN C 324 ? 3.3774 3.0461 2.7012 0.8294  -0.3299 -0.1420 355 ASN C CA  
7068  C C   . ASN C 324 ? 3.4104 3.1056 2.7332 0.8353  -0.3232 -0.1374 355 ASN C C   
7069  O O   . ASN C 324 ? 3.3152 3.0562 2.6848 0.8227  -0.3175 -0.1338 355 ASN C O   
7070  C CB  . ASN C 324 ? 3.4142 3.1089 2.7233 0.8438  -0.3245 -0.1405 355 ASN C CB  
7071  C CG  . ASN C 324 ? 3.4525 3.2081 2.8181 0.8303  -0.3169 -0.1356 355 ASN C CG  
7072  O OD1 . ASN C 324 ? 3.5054 3.3116 2.9007 0.8264  -0.3086 -0.1292 355 ASN C OD1 
7073  N ND2 . ASN C 324 ? 3.6180 3.3685 2.9971 0.8234  -0.3203 -0.1380 355 ASN C ND2 
7074  N N   . ASN C 325 ? 3.3793 3.0465 2.6485 0.8551  -0.3239 -0.1376 356 ASN C N   
7075  C CA  . ASN C 325 ? 3.3241 3.0133 2.5831 0.8648  -0.3175 -0.1330 356 ASN C CA  
7076  C C   . ASN C 325 ? 3.2839 2.9233 2.5178 0.8646  -0.3244 -0.1347 356 ASN C C   
7077  O O   . ASN C 325 ? 3.3594 2.9595 2.5398 0.8818  -0.3266 -0.1349 356 ASN C O   
7078  C CB  . ASN C 325 ? 3.4495 3.1495 2.6663 0.8899  -0.3111 -0.1308 356 ASN C CB  
7079  C CG  . ASN C 325 ? 3.4703 3.2232 2.7124 0.8906  -0.3035 -0.1279 356 ASN C CG  
7080  O OD1 . ASN C 325 ? 3.4295 3.1975 2.7107 0.8742  -0.3050 -0.1286 356 ASN C OD1 
7081  N ND2 . ASN C 325 ? 3.5302 3.3130 2.7509 0.9097  -0.2948 -0.1239 356 ASN C ND2 
7082  N N   . THR C 326 ? 3.3670 3.0073 2.6392 0.8454  -0.3274 -0.1357 357 THR C N   
7083  C CA  . THR C 326 ? 3.3888 2.9846 2.6422 0.8432  -0.3337 -0.1367 357 THR C CA  
7084  C C   . THR C 326 ? 3.3064 2.9427 2.6020 0.8326  -0.3292 -0.1350 357 THR C C   
7085  O O   . THR C 326 ? 3.1922 2.8824 2.5373 0.8219  -0.3235 -0.1344 357 THR C O   
7086  C CB  . THR C 326 ? 3.3506 2.8908 2.6023 0.8302  -0.3447 -0.1417 357 THR C CB  
7087  O OG1 . THR C 326 ? 3.4261 2.9171 2.6522 0.8294  -0.3512 -0.1415 357 THR C OG1 
7088  C CG2 . THR C 326 ? 3.2191 2.7925 2.5346 0.8087  -0.3433 -0.1439 357 THR C CG2 
7089  N N   . ILE C 327 ? 3.2105 2.8183 2.4840 0.8361  -0.3322 -0.1342 358 ILE C N   
7090  C CA  . ILE C 327 ? 3.1571 2.7962 2.4625 0.8288  -0.3292 -0.1337 358 ILE C CA  
7091  C C   . ILE C 327 ? 3.1001 2.7076 2.4301 0.8114  -0.3359 -0.1389 358 ILE C C   
7092  O O   . ILE C 327 ? 3.1500 2.6957 2.4471 0.8114  -0.3440 -0.1396 358 ILE C O   
7093  C CB  . ILE C 327 ? 3.2375 2.8710 2.5034 0.8452  -0.3272 -0.1289 358 ILE C CB  
7094  C CG1 . ILE C 327 ? 3.2969 2.9651 2.5407 0.8632  -0.3190 -0.1239 358 ILE C CG1 
7095  C CG2 . ILE C 327 ? 3.1800 2.8469 2.4780 0.8385  -0.3249 -0.1292 358 ILE C CG2 
7096  C CD1 . ILE C 327 ? 3.3773 3.0472 2.5846 0.8803  -0.3154 -0.1184 358 ILE C CD1 
7097  N N   . ILE C 328 ? 3.1119 2.7606 2.4990 0.7964  -0.3323 -0.1424 359 ILE C N   
7098  C CA  . ILE C 328 ? 3.0136 2.6428 2.4330 0.7799  -0.3361 -0.1485 359 ILE C CA  
7099  C C   . ILE C 328 ? 2.9249 2.5788 2.3649 0.7789  -0.3329 -0.1509 359 ILE C C   
7100  O O   . ILE C 328 ? 2.8665 2.5778 2.3372 0.7787  -0.3264 -0.1511 359 ILE C O   
7101  C CB  . ILE C 328 ? 2.9303 2.5849 2.4011 0.7636  -0.3338 -0.1523 359 ILE C CB  
7102  C CG1 . ILE C 328 ? 2.9449 2.5750 2.3925 0.7661  -0.3376 -0.1504 359 ILE C CG1 
7103  C CG2 . ILE C 328 ? 2.8239 2.4620 2.3303 0.7474  -0.3359 -0.1593 359 ILE C CG2 
7104  C CD1 . ILE C 328 ? 2.9729 2.5312 2.3766 0.7681  -0.3478 -0.1514 359 ILE C CD1 
7105  N N   . ARG C 329 ? 2.8962 2.5070 2.3186 0.7785  -0.3379 -0.1526 360 ARG C N   
7106  C CA  . ARG C 329 ? 2.8551 2.4851 2.2934 0.7793  -0.3353 -0.1560 360 ARG C CA  
7107  C C   . ARG C 329 ? 2.7502 2.3649 2.2276 0.7622  -0.3357 -0.1655 360 ARG C C   
7108  O O   . ARG C 329 ? 2.7821 2.3468 2.2476 0.7525  -0.3409 -0.1659 360 ARG C O   
7109  C CB  . ARG C 329 ? 2.9734 2.5691 2.3569 0.7943  -0.3391 -0.1494 360 ARG C CB  
7110  C CG  . ARG C 329 ? 2.9449 2.5734 2.3452 0.7842  -0.3309 -0.1526 360 ARG C CG  
7111  C CD  . ARG C 329 ? 3.0810 2.6806 2.4283 0.7907  -0.3313 -0.1447 360 ARG C CD  
7112  N NE  . ARG C 329 ? 3.1490 2.6827 2.4702 0.7753  -0.3349 -0.1434 360 ARG C NE  
7113  C CZ  . ARG C 329 ? 3.1319 2.6616 2.4714 0.7418  -0.3264 -0.1481 360 ARG C CZ  
7114  N NH1 . ARG C 329 ? 3.0596 2.6447 2.4421 0.7221  -0.3136 -0.1559 360 ARG C NH1 
7115  N NH2 . ARG C 329 ? 3.1647 2.6356 2.4785 0.7277  -0.3310 -0.1450 360 ARG C NH2 
7116  N N   . PHE C 330 ? 2.8192 2.4843 2.3448 0.7409  -0.3235 -0.1731 361 PHE C N   
7117  C CA  . PHE C 330 ? 2.7309 2.3979 2.2993 0.7064  -0.3142 -0.1826 361 PHE C CA  
7118  C C   . PHE C 330 ? 2.6809 2.3491 2.2407 0.6864  -0.3048 -0.1848 361 PHE C C   
7119  O O   . PHE C 330 ? 2.7119 2.4147 2.2674 0.6911  -0.2996 -0.1846 361 PHE C O   
7120  C CB  . PHE C 330 ? 2.6626 2.3821 2.2910 0.6983  -0.3076 -0.1902 361 PHE C CB  
7121  C CG  . PHE C 330 ? 2.6566 2.3754 2.2964 0.7157  -0.3166 -0.1874 361 PHE C CG  
7122  C CD1 . PHE C 330 ? 2.6015 2.2911 2.2560 0.7056  -0.3197 -0.1897 361 PHE C CD1 
7123  C CD2 . PHE C 330 ? 2.6404 2.3936 2.2750 0.7303  -0.3178 -0.1805 361 PHE C CD2 
7124  C CE1 . PHE C 330 ? 2.5576 2.2543 2.2222 0.7056  -0.3221 -0.1852 361 PHE C CE1 
7125  C CE2 . PHE C 330 ? 2.6245 2.3856 2.2693 0.7243  -0.3176 -0.1757 361 PHE C CE2 
7126  C CZ  . PHE C 330 ? 2.5778 2.3108 2.2376 0.7122  -0.3198 -0.1781 361 PHE C CZ  
7127  N N   . ALA C 331 ? 2.5823 2.2159 2.1404 0.6634  -0.3026 -0.1866 362 ALA C N   
7128  C CA  . ALA C 331 ? 2.6666 2.2989 2.2171 0.6424  -0.2938 -0.1879 362 ALA C CA  
7129  C C   . ALA C 331 ? 2.5927 2.2276 2.1837 0.6103  -0.2852 -0.1959 362 ALA C C   
7130  O O   . ALA C 331 ? 2.5322 2.1529 2.1435 0.6046  -0.2887 -0.1975 362 ALA C O   
7131  C CB  . ALA C 331 ? 2.8376 2.4167 2.3266 0.6504  -0.3020 -0.1771 362 ALA C CB  
7132  N N   . ASN C 332 ? 2.6641 2.3203 2.2664 0.5902  -0.2737 -0.2007 363 ASN C N   
7133  C CA  . ASN C 332 ? 2.5576 2.2225 2.1978 0.5612  -0.2640 -0.2081 363 ASN C CA  
7134  C C   . ASN C 332 ? 2.5879 2.2026 2.2041 0.5481  -0.2703 -0.2004 363 ASN C C   
7135  O O   . ASN C 332 ? 2.7042 2.2737 2.2730 0.5608  -0.2823 -0.1902 363 ASN C O   
7136  C CB  . ASN C 332 ? 2.5886 2.2902 2.2428 0.5456  -0.2504 -0.2152 363 ASN C CB  
7137  C CG  . ASN C 332 ? 2.7617 2.4463 2.3676 0.5483  -0.2519 -0.2068 363 ASN C CG  
7138  O OD1 . ASN C 332 ? 2.9051 2.5551 2.4660 0.5670  -0.2631 -0.1960 363 ASN C OD1 
7139  N ND2 . ASN C 332 ? 2.8032 2.5121 2.4172 0.5306  -0.2405 -0.2117 363 ASN C ND2 
7140  N N   . SER C 333 ? 2.5155 2.1386 2.1640 0.5221  -0.2623 -0.2051 364 SER C N   
7141  C CA  . SER C 333 ? 2.5719 2.1553 2.2059 0.5047  -0.2676 -0.1979 364 SER C CA  
7142  C C   . SER C 333 ? 2.7178 2.2670 2.3011 0.4996  -0.2716 -0.1875 364 SER C C   
7143  O O   . SER C 333 ? 2.8198 2.3850 2.3875 0.5041  -0.2664 -0.1873 364 SER C O   
7144  C CB  . SER C 333 ? 2.4779 2.0889 2.1593 0.4783  -0.2560 -0.2046 364 SER C CB  
7145  O OG  . SER C 333 ? 2.5251 2.1026 2.1939 0.4595  -0.2614 -0.1965 364 SER C OG  
7146  N N   . SER C 334 ? 2.5954 2.0947 2.1503 0.4907  -0.2822 -0.1780 365 SER C N   
7147  C CA  . SER C 334 ? 2.6874 2.1481 2.1923 0.4841  -0.2873 -0.1665 365 SER C CA  
7148  C C   . SER C 334 ? 2.6702 2.1538 2.1916 0.4544  -0.2758 -0.1659 365 SER C C   
7149  O O   . SER C 334 ? 2.7551 2.2388 2.2506 0.4523  -0.2726 -0.1608 365 SER C O   
7150  C CB  . SER C 334 ? 2.8045 2.1997 2.2699 0.4838  -0.3038 -0.1564 365 SER C CB  
7151  O OG  . SER C 334 ? 2.8551 2.2278 2.2998 0.5139  -0.3148 -0.1566 365 SER C OG  
7152  N N   . GLY C 335 ? 2.7146 2.2200 2.2782 0.4321  -0.2692 -0.1704 366 GLY C N   
7153  C CA  . GLY C 335 ? 2.7108 2.2431 2.2919 0.4052  -0.2578 -0.1697 366 GLY C CA  
7154  C C   . GLY C 335 ? 2.7115 2.2404 2.3123 0.3777  -0.2578 -0.1653 366 GLY C C   
7155  O O   . GLY C 335 ? 2.7013 2.1999 2.2987 0.3766  -0.2685 -0.1616 366 GLY C O   
7156  N N   . GLY C 336 ? 2.7205 2.2832 2.3414 0.3555  -0.2458 -0.1653 367 GLY C N   
7157  C CA  . GLY C 336 ? 2.7294 2.2998 2.3706 0.3276  -0.2438 -0.1598 367 GLY C CA  
7158  C C   . GLY C 336 ? 2.6762 2.3092 2.3719 0.3181  -0.2258 -0.1709 367 GLY C C   
7159  O O   . GLY C 336 ? 2.6476 2.3155 2.3532 0.3219  -0.2138 -0.1787 367 GLY C O   
7160  N N   . ASP C 337 ? 2.5660 2.2132 2.2960 0.3063  -0.2240 -0.1717 368 ASP C N   
7161  C CA  . ASP C 337 ? 2.5143 2.2184 2.2960 0.2991  -0.2073 -0.1819 368 ASP C CA  
7162  C C   . ASP C 337 ? 2.4605 2.1896 2.2718 0.3225  -0.1997 -0.1989 368 ASP C C   
7163  O O   . ASP C 337 ? 2.4615 2.1670 2.2594 0.3425  -0.2084 -0.2015 368 ASP C O   
7164  C CB  . ASP C 337 ? 2.5088 2.2227 2.3169 0.2800  -0.2075 -0.1760 368 ASP C CB  
7165  C CG  . ASP C 337 ? 2.5099 2.1879 2.3129 0.2860  -0.2217 -0.1723 368 ASP C CG  
7166  O OD1 . ASP C 337 ? 2.5330 2.1736 2.3068 0.3046  -0.2326 -0.1729 368 ASP C OD1 
7167  O OD2 . ASP C 337 ? 2.4999 2.1892 2.3274 0.2723  -0.2219 -0.1684 368 ASP C OD2 
7168  N N   . LEU C 338 ? 2.4368 2.2147 2.2878 0.3196  -0.1834 -0.2103 369 LEU C N   
7169  C CA  . LEU C 338 ? 2.2654 2.0690 2.1459 0.3381  -0.1751 -0.2269 369 LEU C CA  
7170  C C   . LEU C 338 ? 2.2338 2.0342 2.1432 0.3486  -0.1789 -0.2307 369 LEU C C   
7171  O O   . LEU C 338 ? 2.1640 1.9694 2.0846 0.3669  -0.1786 -0.2403 369 LEU C O   
7172  C CB  . LEU C 338 ? 2.1387 1.9909 2.0513 0.3310  -0.1569 -0.2381 369 LEU C CB  
7173  C CG  . LEU C 338 ? 2.0830 1.9618 2.0214 0.3468  -0.1471 -0.2563 369 LEU C CG  
7174  C CD1 . LEU C 338 ? 2.1293 1.9983 2.0364 0.3588  -0.1511 -0.2591 369 LEU C CD1 
7175  C CD2 . LEU C 338 ? 2.0350 1.9574 2.0055 0.3390  -0.1295 -0.2673 369 LEU C CD2 
7176  N N   . GLU C 339 ? 2.1879 1.9817 2.1095 0.3371  -0.1829 -0.2228 370 GLU C N   
7177  C CA  . GLU C 339 ? 2.1248 1.9187 2.0753 0.3474  -0.1861 -0.2261 370 GLU C CA  
7178  C C   . GLU C 339 ? 2.1752 1.9283 2.0977 0.3636  -0.2025 -0.2216 370 GLU C C   
7179  O O   . GLU C 339 ? 2.1102 1.8657 2.0553 0.3763  -0.2052 -0.2255 370 GLU C O   
7180  C CB  . GLU C 339 ? 2.1168 1.9208 2.0895 0.3299  -0.1850 -0.2186 370 GLU C CB  
7181  C CG  . GLU C 339 ? 2.0141 1.8667 2.0252 0.3209  -0.1669 -0.2254 370 GLU C CG  
7182  C CD  . GLU C 339 ? 2.0714 1.9335 2.0690 0.2976  -0.1639 -0.2150 370 GLU C CD  
7183  O OE1 . GLU C 339 ? 2.2145 2.0427 2.1755 0.2857  -0.1769 -0.2013 370 GLU C OE1 
7184  O OE2 . GLU C 339 ? 2.0186 1.9216 2.0407 0.2914  -0.1488 -0.2203 370 GLU C OE2 
7185  N N   . VAL C 340 ? 2.3186 2.0351 2.1922 0.3646  -0.2133 -0.2133 371 VAL C N   
7186  C CA  . VAL C 340 ? 2.3214 1.9966 2.1625 0.3819  -0.2292 -0.2085 371 VAL C CA  
7187  C C   . VAL C 340 ? 2.3289 2.0063 2.1536 0.4035  -0.2291 -0.2146 371 VAL C C   
7188  O O   . VAL C 340 ? 2.3021 1.9679 2.1216 0.4241  -0.2370 -0.2160 371 VAL C O   
7189  C CB  . VAL C 340 ? 2.4064 2.0326 2.1998 0.3702  -0.2433 -0.1940 371 VAL C CB  
7190  C CG1 . VAL C 340 ? 2.3783 1.9600 2.1384 0.3901  -0.2598 -0.1901 371 VAL C CG1 
7191  C CG2 . VAL C 340 ? 2.3984 2.0280 2.2095 0.3458  -0.2434 -0.1872 371 VAL C CG2 
7192  N N   . THR C 341 ? 2.4574 2.1525 2.2738 0.3992  -0.2201 -0.2178 372 THR C N   
7193  C CA  . THR C 341 ? 2.4180 2.1183 2.2161 0.4173  -0.2199 -0.2225 372 THR C CA  
7194  C C   . THR C 341 ? 2.2562 1.9982 2.0948 0.4274  -0.2096 -0.2368 372 THR C C   
7195  O O   . THR C 341 ? 2.2181 1.9660 2.0450 0.4441  -0.2115 -0.2402 372 THR C O   
7196  C CB  . THR C 341 ? 2.4330 2.1366 2.2043 0.4075  -0.2147 -0.2196 372 THR C CB  
7197  O OG1 . THR C 341 ? 2.3485 2.0909 2.1533 0.3899  -0.1995 -0.2268 372 THR C OG1 
7198  C CG2 . THR C 341 ? 2.5485 2.2069 2.2754 0.3973  -0.2259 -0.2040 372 THR C CG2 
7199  N N   . THR C 342 ? 2.1773 1.9480 2.0619 0.4178  -0.1992 -0.2447 373 THR C N   
7200  C CA  . THR C 342 ? 2.1137 1.9201 2.0362 0.4254  -0.1893 -0.2585 373 THR C CA  
7201  C C   . THR C 342 ? 2.0648 1.8766 2.0250 0.4296  -0.1902 -0.2604 373 THR C C   
7202  O O   . THR C 342 ? 2.0690 1.8653 2.0327 0.4225  -0.1950 -0.2528 373 THR C O   
7203  C CB  . THR C 342 ? 2.0807 1.9207 2.0240 0.4117  -0.1731 -0.2687 373 THR C CB  
7204  O OG1 . THR C 342 ? 2.0653 1.9107 2.0278 0.3951  -0.1676 -0.2655 373 THR C OG1 
7205  C CG2 . THR C 342 ? 2.1269 1.9662 2.0343 0.4082  -0.1718 -0.2670 373 THR C CG2 
7206  N N   . HIS C 343 ? 1.9144 1.7491 1.9026 0.4405  -0.1857 -0.2703 374 HIS C N   
7207  C CA  . HIS C 343 ? 1.8664 1.7103 1.8936 0.4453  -0.1851 -0.2725 374 HIS C CA  
7208  C C   . HIS C 343 ? 1.8218 1.6897 1.8864 0.4310  -0.1708 -0.2794 374 HIS C C   
7209  O O   . HIS C 343 ? 1.7867 1.6802 1.8762 0.4305  -0.1592 -0.2915 374 HIS C O   
7210  C CB  . HIS C 343 ? 1.8406 1.6996 1.8827 0.4611  -0.1862 -0.2789 374 HIS C CB  
7211  C CG  . HIS C 343 ? 1.7893 1.6619 1.8751 0.4648  -0.1836 -0.2819 374 HIS C CG  
7212  N ND1 . HIS C 343 ? 1.7835 1.6444 1.8807 0.4643  -0.1888 -0.2740 374 HIS C ND1 
7213  C CD2 . HIS C 343 ? 1.7453 1.6420 1.8661 0.4683  -0.1761 -0.2915 374 HIS C CD2 
7214  C CE1 . HIS C 343 ? 1.7365 1.6155 1.8745 0.4687  -0.1844 -0.2781 374 HIS C CE1 
7215  N NE2 . HIS C 343 ? 1.7142 1.6135 1.8670 0.4711  -0.1767 -0.2885 374 HIS C NE2 
7216  N N   . SER C 344 ? 1.8680 1.7273 1.9349 0.4194  -0.1719 -0.2713 375 SER C N   
7217  C CA  . SER C 344 ? 1.8320 1.7159 1.9319 0.4066  -0.1588 -0.2752 375 SER C CA  
7218  C C   . SER C 344 ? 1.7816 1.6798 1.9248 0.4140  -0.1555 -0.2785 375 SER C C   
7219  O O   . SER C 344 ? 1.7835 1.6669 1.9280 0.4208  -0.1661 -0.2709 375 SER C O   
7220  C CB  . SER C 344 ? 1.8634 1.7357 1.9475 0.3898  -0.1622 -0.2631 375 SER C CB  
7221  O OG  . SER C 344 ? 1.8271 1.7231 1.9476 0.3809  -0.1530 -0.2631 375 SER C OG  
7222  N N   . PHE C 345 ? 1.7508 1.6769 1.9280 0.4134  -0.1410 -0.2898 376 PHE C N   
7223  C CA  . PHE C 345 ? 1.7067 1.6469 1.9261 0.4203  -0.1365 -0.2925 376 PHE C CA  
7224  C C   . PHE C 345 ? 1.6744 1.6425 1.9243 0.4161  -0.1188 -0.3035 376 PHE C C   
7225  O O   . PHE C 345 ? 1.6823 1.6600 1.9205 0.4087  -0.1105 -0.3100 376 PHE C O   
7226  C CB  . PHE C 345 ? 1.6933 1.6288 1.9204 0.4362  -0.1427 -0.2961 376 PHE C CB  
7227  C CG  . PHE C 345 ? 1.6846 1.6313 1.9135 0.4399  -0.1356 -0.3097 376 PHE C CG  
7228  C CD1 . PHE C 345 ? 1.7170 1.6554 1.9105 0.4404  -0.1405 -0.3112 376 PHE C CD1 
7229  C CD2 . PHE C 345 ? 1.6480 1.6127 1.9127 0.4428  -0.1242 -0.3208 376 PHE C CD2 
7230  C CE1 . PHE C 345 ? 1.7105 1.6610 1.9049 0.4423  -0.1346 -0.3236 376 PHE C CE1 
7231  C CE2 . PHE C 345 ? 1.6441 1.6164 1.9082 0.4443  -0.1187 -0.3339 376 PHE C CE2 
7232  C CZ  . PHE C 345 ? 1.6740 1.6406 1.9033 0.4434  -0.1240 -0.3353 376 PHE C CZ  
7233  N N   . ASN C 346 ? 1.7507 1.7318 2.0390 0.4221  -0.1132 -0.3053 377 ASN C N   
7234  C CA  . ASN C 346 ? 1.7226 1.7282 2.0426 0.4220  -0.0966 -0.3153 377 ASN C CA  
7235  C C   . ASN C 346 ? 1.6979 1.7052 2.0425 0.4347  -0.0931 -0.3259 377 ASN C C   
7236  O O   . ASN C 346 ? 1.6893 1.6887 2.0456 0.4433  -0.1016 -0.3205 377 ASN C O   
7237  C CB  . ASN C 346 ? 1.7102 1.7317 2.0555 0.4179  -0.0917 -0.3066 377 ASN C CB  
7238  C CG  . ASN C 346 ? 1.6920 1.7408 2.0620 0.4174  -0.0735 -0.3157 377 ASN C CG  
7239  O OD1 . ASN C 346 ? 1.6786 1.7314 2.0596 0.4251  -0.0644 -0.3301 377 ASN C OD1 
7240  N ND2 . ASN C 346 ? 1.6942 1.7621 2.0726 0.4089  -0.0683 -0.3070 377 ASN C ND2 
7241  N N   . CYS C 347 ? 1.8640 1.8815 2.2155 0.4354  -0.0809 -0.3408 378 CYS C N   
7242  C CA  . CYS C 347 ? 1.8472 1.8644 2.2205 0.4448  -0.0767 -0.3522 378 CYS C CA  
7243  C C   . CYS C 347 ? 1.8369 1.8678 2.2263 0.4451  -0.0596 -0.3671 378 CYS C C   
7244  O O   . CYS C 347 ? 1.8473 1.8816 2.2175 0.4399  -0.0539 -0.3777 378 CYS C O   
7245  C CB  . CYS C 347 ? 1.8603 1.8647 2.2110 0.4468  -0.0865 -0.3559 378 CYS C CB  
7246  S SG  . CYS C 347 ? 1.8476 1.8520 2.2251 0.4546  -0.0819 -0.3685 378 CYS C SG  
7247  N N   . GLY C 348 ? 1.9335 1.9725 2.3575 0.4525  -0.0515 -0.3677 379 GLY C N   
7248  C CA  . GLY C 348 ? 1.8731 1.9229 2.3140 0.4565  -0.0351 -0.3816 379 GLY C CA  
7249  C C   . GLY C 348 ? 1.8826 1.9537 2.3209 0.4513  -0.0248 -0.3794 379 GLY C C   
7250  O O   . GLY C 348 ? 1.8353 1.9174 2.2797 0.4547  -0.0106 -0.3921 379 GLY C O   
7251  N N   . GLY C 349 ? 1.8135 1.8905 2.2414 0.4429  -0.0319 -0.3635 380 GLY C N   
7252  C CA  . GLY C 349 ? 1.7944 1.8942 2.2186 0.4350  -0.0242 -0.3579 380 GLY C CA  
7253  C C   . GLY C 349 ? 1.8019 1.8997 2.1889 0.4220  -0.0290 -0.3562 380 GLY C C   
7254  O O   . GLY C 349 ? 1.7941 1.9064 2.1724 0.4114  -0.0287 -0.3451 380 GLY C O   
7255  N N   . GLU C 350 ? 1.7547 1.8360 2.1195 0.4220  -0.0336 -0.3660 381 GLU C N   
7256  C CA  . GLU C 350 ? 1.7767 1.8546 2.1048 0.4113  -0.0384 -0.3646 381 GLU C CA  
7257  C C   . GLU C 350 ? 1.8469 1.9040 2.1533 0.4061  -0.0559 -0.3489 381 GLU C C   
7258  O O   . GLU C 350 ? 1.8685 1.9110 2.1849 0.4128  -0.0652 -0.3434 381 GLU C O   
7259  C CB  . GLU C 350 ? 1.7284 1.7996 2.0420 0.4143  -0.0359 -0.3818 381 GLU C CB  
7260  C CG  . GLU C 350 ? 1.7083 1.7947 2.0373 0.4199  -0.0192 -0.3999 381 GLU C CG  
7261  C CD  . GLU C 350 ? 1.7227 1.8315 2.0364 0.4127  -0.0091 -0.4033 381 GLU C CD  
7262  O OE1 . GLU C 350 ? 1.8533 1.9716 2.1554 0.4029  -0.0124 -0.3883 381 GLU C OE1 
7263  O OE2 . GLU C 350 ? 1.6304 1.7473 1.9427 0.4164  0.0018  -0.4208 381 GLU C OE2 
7264  N N   . PHE C 351 ? 1.6121 1.6671 1.8870 0.3947  -0.0604 -0.3414 382 PHE C N   
7265  C CA  . PHE C 351 ? 1.6808 1.7119 1.9285 0.3900  -0.0770 -0.3269 382 PHE C CA  
7266  C C   . PHE C 351 ? 1.6837 1.6997 1.8971 0.3908  -0.0836 -0.3312 382 PHE C C   
7267  O O   . PHE C 351 ? 1.6834 1.7057 1.8735 0.3824  -0.0803 -0.3321 382 PHE C O   
7268  C CB  . PHE C 351 ? 1.7296 1.7659 1.9662 0.3754  -0.0791 -0.3118 382 PHE C CB  
7269  C CG  . PHE C 351 ? 1.7681 1.8203 2.0367 0.3742  -0.0749 -0.3047 382 PHE C CG  
7270  C CD1 . PHE C 351 ? 1.8255 1.8617 2.0992 0.3755  -0.0868 -0.2932 382 PHE C CD1 
7271  C CD2 . PHE C 351 ? 1.7307 1.8157 2.0241 0.3734  -0.0591 -0.3098 382 PHE C CD2 
7272  C CE1 . PHE C 351 ? 1.8252 1.8788 2.1287 0.3743  -0.0832 -0.2862 382 PHE C CE1 
7273  C CE2 . PHE C 351 ? 1.7579 1.8610 2.0811 0.3735  -0.0550 -0.3022 382 PHE C CE2 
7274  C CZ  . PHE C 351 ? 1.8056 1.8936 2.1344 0.3733  -0.0671 -0.2902 382 PHE C CZ  
7275  N N   . PHE C 352 ? 1.5906 1.5900 1.8017 0.4012  -0.0927 -0.3330 383 PHE C N   
7276  C CA  . PHE C 352 ? 1.5916 1.5803 1.7721 0.4040  -0.0992 -0.3364 383 PHE C CA  
7277  C C   . PHE C 352 ? 1.6625 1.6284 1.8060 0.4004  -0.1131 -0.3208 383 PHE C C   
7278  O O   . PHE C 352 ? 1.7100 1.6626 1.8539 0.3986  -0.1209 -0.3084 383 PHE C O   
7279  C CB  . PHE C 352 ? 1.5576 1.5414 1.7507 0.4164  -0.1037 -0.3429 383 PHE C CB  
7280  C CG  . PHE C 352 ? 1.5172 1.5171 1.7411 0.4194  -0.0913 -0.3591 383 PHE C CG  
7281  C CD1 . PHE C 352 ? 1.5009 1.5064 1.7614 0.4235  -0.0856 -0.3598 383 PHE C CD1 
7282  C CD2 . PHE C 352 ? 1.5261 1.5342 1.7409 0.4183  -0.0856 -0.3734 383 PHE C CD2 
7283  C CE1 . PHE C 352 ? 1.4959 1.5115 1.7824 0.4273  -0.0744 -0.3746 383 PHE C CE1 
7284  C CE2 . PHE C 352 ? 1.5217 1.5394 1.7618 0.4207  -0.0749 -0.3890 383 PHE C CE2 
7285  C CZ  . PHE C 352 ? 1.5077 1.5274 1.7831 0.4257  -0.0693 -0.3896 383 PHE C CZ  
7286  N N   . TYR C 353 ? 1.6187 1.5792 1.7288 0.3998  -0.1165 -0.3217 384 TYR C N   
7287  C CA  . TYR C 353 ? 1.6802 1.6150 1.7504 0.3991  -0.1300 -0.3076 384 TYR C CA  
7288  C C   . TYR C 353 ? 1.6625 1.5936 1.7087 0.4091  -0.1352 -0.3117 384 TYR C C   
7289  O O   . TYR C 353 ? 1.6462 1.5881 1.6743 0.4047  -0.1300 -0.3169 384 TYR C O   
7290  C CB  . TYR C 353 ? 1.7196 1.6546 1.7688 0.3838  -0.1272 -0.2999 384 TYR C CB  
7291  C CG  . TYR C 353 ? 1.7377 1.6793 1.8086 0.3728  -0.1234 -0.2933 384 TYR C CG  
7292  C CD1 . TYR C 353 ? 1.7986 1.7160 1.8588 0.3685  -0.1352 -0.2783 384 TYR C CD1 
7293  C CD2 . TYR C 353 ? 1.6894 1.6625 1.7906 0.3671  -0.1080 -0.3020 384 TYR C CD2 
7294  C CE1 . TYR C 353 ? 1.8134 1.7410 1.8940 0.3569  -0.1319 -0.2715 384 TYR C CE1 
7295  C CE2 . TYR C 353 ? 1.7013 1.6860 1.8231 0.3578  -0.1041 -0.2949 384 TYR C CE2 
7296  C CZ  . TYR C 353 ? 1.7637 1.7270 1.8758 0.3518  -0.1161 -0.2793 384 TYR C CZ  
7297  O OH  . TYR C 353 ? 1.7725 1.7510 1.9052 0.3411  -0.1125 -0.2714 384 TYR C OH  
7298  N N   . CYS C 354 ? 1.9327 1.8518 1.9782 0.4227  -0.1455 -0.3086 385 CYS C N   
7299  C CA  . CYS C 354 ? 1.9536 1.8768 1.9833 0.4332  -0.1498 -0.3127 385 CYS C CA  
7300  C C   . CYS C 354 ? 2.0323 1.9325 2.0166 0.4408  -0.1628 -0.3001 385 CYS C C   
7301  O O   . CYS C 354 ? 2.0686 1.9423 2.0375 0.4438  -0.1728 -0.2878 385 CYS C O   
7302  C CB  . CYS C 354 ? 1.8852 1.8150 1.9430 0.4445  -0.1527 -0.3168 385 CYS C CB  
7303  S SG  . CYS C 354 ? 1.8800 1.8331 1.9896 0.4387  -0.1379 -0.3324 385 CYS C SG  
7304  N N   . ASN C 355 ? 2.1609 2.0715 2.1231 0.4445  -0.1625 -0.3036 386 ASN C N   
7305  C CA  . ASN C 355 ? 2.2306 2.1240 2.1482 0.4543  -0.1733 -0.2927 386 ASN C CA  
7306  C C   . ASN C 355 ? 2.2427 2.1303 2.1579 0.4730  -0.1847 -0.2876 386 ASN C C   
7307  O O   . ASN C 355 ? 2.2124 2.1236 2.1448 0.4787  -0.1830 -0.2951 386 ASN C O   
7308  C CB  . ASN C 355 ? 2.2595 2.1734 2.1583 0.4513  -0.1674 -0.2988 386 ASN C CB  
7309  C CG  . ASN C 355 ? 2.3425 2.2380 2.1917 0.4589  -0.1762 -0.2862 386 ASN C CG  
7310  O OD1 . ASN C 355 ? 2.3928 2.2603 2.2195 0.4711  -0.1883 -0.2739 386 ASN C OD1 
7311  N ND2 . ASN C 355 ? 2.4817 2.3934 2.3126 0.4529  -0.1701 -0.2894 386 ASN C ND2 
7312  N N   . THR C 356 ? 2.1718 2.0283 2.0646 0.4824  -0.1966 -0.2747 387 THR C N   
7313  C CA  . THR C 356 ? 2.1678 2.0180 2.0559 0.5022  -0.2081 -0.2686 387 THR C CA  
7314  C C   . THR C 356 ? 2.2552 2.0933 2.0956 0.5183  -0.2177 -0.2592 387 THR C C   
7315  O O   . THR C 356 ? 2.2892 2.1015 2.1053 0.5340  -0.2298 -0.2488 387 THR C O   
7316  C CB  . THR C 356 ? 2.1044 1.9292 2.0012 0.5044  -0.2153 -0.2617 387 THR C CB  
7317  O OG1 . THR C 356 ? 2.1397 1.9314 2.0067 0.4963  -0.2192 -0.2533 387 THR C OG1 
7318  C CG2 . THR C 356 ? 2.0016 1.8447 1.9493 0.4932  -0.2061 -0.2703 387 THR C CG2 
7319  N N   . SER C 357 ? 2.2975 2.1544 2.1226 0.5155  -0.2123 -0.2628 388 SER C N   
7320  C CA  . SER C 357 ? 2.3965 2.2480 2.1772 0.5316  -0.2200 -0.2539 388 SER C CA  
7321  C C   . SER C 357 ? 2.3911 2.2739 2.1784 0.5469  -0.2232 -0.2552 388 SER C C   
7322  O O   . SER C 357 ? 2.5155 2.3976 2.2674 0.5646  -0.2307 -0.2463 388 SER C O   
7323  C CB  . SER C 357 ? 2.4461 2.3036 2.2041 0.5207  -0.2129 -0.2552 388 SER C CB  
7324  O OG  . SER C 357 ? 2.4121 2.2403 2.1584 0.5073  -0.2117 -0.2507 388 SER C OG  
7325  N N   . GLY C 358 ? 2.4032 2.3137 2.2341 0.5405  -0.2179 -0.2652 389 GLY C N   
7326  C CA  . GLY C 358 ? 2.3404 2.2837 2.1819 0.5510  -0.2208 -0.2663 389 GLY C CA  
7327  C C   . GLY C 358 ? 2.3158 2.2530 2.1703 0.5662  -0.2302 -0.2594 389 GLY C C   
7328  O O   . GLY C 358 ? 2.3147 2.2783 2.1763 0.5775  -0.2349 -0.2568 389 GLY C O   
7329  N N   . LEU C 359 ? 2.2641 2.1688 2.1221 0.5657  -0.2331 -0.2559 390 LEU C N   
7330  C CA  . LEU C 359 ? 2.2582 2.1539 2.1274 0.5797  -0.2422 -0.2493 390 LEU C CA  
7331  C C   . LEU C 359 ? 2.3427 2.2057 2.1667 0.6006  -0.2550 -0.2362 390 LEU C C   
7332  O O   . LEU C 359 ? 2.3537 2.2199 2.1750 0.6201  -0.2643 -0.2293 390 LEU C O   
7333  C CB  . LEU C 359 ? 2.1498 2.0331 2.0554 0.5659  -0.2375 -0.2543 390 LEU C CB  
7334  C CG  . LEU C 359 ? 2.0429 1.9526 1.9963 0.5480  -0.2251 -0.2672 390 LEU C CG  
7335  C CD1 . LEU C 359 ? 1.9677 1.8624 1.9504 0.5383  -0.2217 -0.2690 390 LEU C CD1 
7336  C CD2 . LEU C 359 ? 2.0567 2.0000 2.0343 0.5548  -0.2264 -0.2692 390 LEU C CD2 
7337  N N   . PHE C 360 ? 2.3233 2.1542 2.1104 0.5974  -0.2560 -0.2324 391 PHE C N   
7338  C CA  . PHE C 360 ? 2.3952 2.1863 2.1352 0.6163  -0.2684 -0.2205 391 PHE C CA  
7339  C C   . PHE C 360 ? 2.4805 2.2709 2.1741 0.6296  -0.2711 -0.2140 391 PHE C C   
7340  O O   . PHE C 360 ? 2.5278 2.2801 2.1803 0.6317  -0.2751 -0.2075 391 PHE C O   
7341  C CB  . PHE C 360 ? 2.4073 2.1552 2.1391 0.6014  -0.2691 -0.2193 391 PHE C CB  
7342  C CG  . PHE C 360 ? 2.3414 2.0925 2.1181 0.5886  -0.2662 -0.2247 391 PHE C CG  
7343  C CD1 . PHE C 360 ? 2.3164 2.0749 2.1115 0.6031  -0.2727 -0.2229 391 PHE C CD1 
7344  C CD2 . PHE C 360 ? 2.3037 2.0554 2.1058 0.5630  -0.2562 -0.2312 391 PHE C CD2 
7345  C CE1 . PHE C 360 ? 2.2568 2.0205 2.0937 0.5922  -0.2697 -0.2270 391 PHE C CE1 
7346  C CE2 . PHE C 360 ? 2.2451 2.0029 2.0888 0.5529  -0.2529 -0.2354 391 PHE C CE2 
7347  C CZ  . PHE C 360 ? 2.2220 1.9851 2.0830 0.5674  -0.2596 -0.2333 391 PHE C CZ  
7348  N N   . ASN C 361 ? 2.5476 2.3813 2.2482 0.6372  -0.2686 -0.2154 392 ASN C N   
7349  C CA  . ASN C 361 ? 2.7534 2.5979 2.4141 0.6520  -0.2707 -0.2087 392 ASN C CA  
7350  C C   . ASN C 361 ? 2.8414 2.7090 2.4914 0.6804  -0.2798 -0.2003 392 ASN C C   
7351  O O   . ASN C 361 ? 2.8837 2.7997 2.5504 0.6811  -0.2766 -0.2022 392 ASN C O   
7352  C CB  . ASN C 361 ? 2.7558 2.6375 2.4323 0.6332  -0.2589 -0.2176 392 ASN C CB  
7353  C CG  . ASN C 361 ? 2.8767 2.7756 2.5146 0.6475  -0.2606 -0.2104 392 ASN C CG  
7354  O OD1 . ASN C 361 ? 2.9284 2.7988 2.5200 0.6668  -0.2682 -0.1989 392 ASN C OD1 
7355  N ND2 . ASN C 361 ? 3.0228 2.9698 2.6796 0.6392  -0.2539 -0.2168 392 ASN C ND2 
7356  N N   . SER C 362 ? 2.7425 2.5780 2.3649 0.7034  -0.2912 -0.1910 393 SER C N   
7357  C CA  . SER C 362 ? 2.7904 2.6520 2.4045 0.7317  -0.2996 -0.1827 393 SER C CA  
7358  C C   . SER C 362 ? 2.8990 2.7195 2.4563 0.7622  -0.3113 -0.1707 393 SER C C   
7359  O O   . SER C 362 ? 2.9187 2.6853 2.4459 0.7594  -0.3141 -0.1693 393 SER C O   
7360  C CB  . SER C 362 ? 2.6300 2.5105 2.2899 0.7297  -0.3012 -0.1861 393 SER C CB  
7361  O OG  . SER C 362 ? 2.4428 2.3556 2.1532 0.7023  -0.2904 -0.1974 393 SER C OG  
7362  N N   . THR C 363 ? 2.8267 2.6747 2.3688 0.7834  -0.3154 -0.1617 394 THR C N   
7363  C CA  . THR C 363 ? 2.9156 2.7330 2.4056 0.7948  -0.3175 -0.1512 394 THR C CA  
7364  C C   . THR C 363 ? 2.9125 2.7675 2.4125 0.7943  -0.3133 -0.1459 394 THR C C   
7365  O O   . THR C 363 ? 2.9193 2.8257 2.4246 0.7996  -0.3092 -0.1418 394 THR C O   
7366  C CB  . THR C 363 ? 2.9692 2.7811 2.4107 0.8125  -0.3183 -0.1442 394 THR C CB  
7367  O OG1 . THR C 363 ? 3.0234 2.7985 2.4543 0.8130  -0.3226 -0.1479 394 THR C OG1 
7368  C CG2 . THR C 363 ? 3.0838 2.8625 2.4725 0.8251  -0.3189 -0.1354 394 THR C CG2 
7369  N N   . TRP C 364 ? 2.9550 2.7864 2.4579 0.7877  -0.3144 -0.1456 395 TRP C N   
7370  C CA  . TRP C 364 ? 2.9419 2.8067 2.4572 0.7862  -0.3102 -0.1409 395 TRP C CA  
7371  C C   . TRP C 364 ? 3.0613 2.9042 2.5247 0.8020  -0.3100 -0.1340 395 TRP C C   
7372  O O   . TRP C 364 ? 3.1226 2.9096 2.5529 0.8056  -0.3151 -0.1351 395 TRP C O   
7373  C CB  . TRP C 364 ? 2.8255 2.6869 2.3826 0.7687  -0.3106 -0.1452 395 TRP C CB  
7374  C CG  . TRP C 364 ? 2.7116 2.6028 2.3232 0.7544  -0.3085 -0.1523 395 TRP C CG  
7375  C CD1 . TRP C 364 ? 2.6423 2.5115 2.2719 0.7468  -0.3103 -0.1615 395 TRP C CD1 
7376  C CD2 . TRP C 364 ? 2.6386 2.5873 2.2927 0.7468  -0.3039 -0.1516 395 TRP C CD2 
7377  N NE1 . TRP C 364 ? 2.5358 2.4447 2.2174 0.7355  -0.3062 -0.1681 395 TRP C NE1 
7378  C CE2 . TRP C 364 ? 2.5233 2.4801 2.2201 0.7350  -0.3031 -0.1618 395 TRP C CE2 
7379  C CE3 . TRP C 364 ? 2.6323 2.6254 2.2926 0.7485  -0.3002 -0.1433 395 TRP C CE3 
7380  C CZ2 . TRP C 364 ? 2.4611 2.4663 2.2049 0.7253  -0.2998 -0.1645 395 TRP C CZ2 
7381  C CZ3 . TRP C 364 ? 2.5352 2.5770 2.2422 0.7378  -0.2975 -0.1442 395 TRP C CZ3 
7382  C CH2 . TRP C 364 ? 2.4690 2.5153 2.2166 0.7265  -0.2978 -0.1549 395 TRP C CH2 
7383  N N   . ILE C 365 ? 3.1204 3.0067 2.5763 0.8116  -0.3040 -0.1275 396 ILE C N   
7384  C CA  . ILE C 365 ? 3.2322 3.1044 2.6423 0.8283  -0.3017 -0.1222 396 ILE C CA  
7385  C C   . ILE C 365 ? 3.2185 3.0974 2.6476 0.8210  -0.3006 -0.1221 396 ILE C C   
7386  O O   . ILE C 365 ? 3.1509 3.0515 2.6282 0.8038  -0.3007 -0.1243 396 ILE C O   
7387  C CB  . ILE C 365 ? 3.2923 3.2107 2.6870 0.8425  -0.2945 -0.1151 396 ILE C CB  
7388  C CG1 . ILE C 365 ? 3.3559 3.2459 2.7066 0.8571  -0.2958 -0.1137 396 ILE C CG1 
7389  C CG2 . ILE C 365 ? 3.3542 3.2952 2.7325 0.8541  -0.2879 -0.1092 396 ILE C CG2 
7390  C CD1 . ILE C 365 ? 3.2452 3.1256 2.6120 0.8481  -0.3008 -0.1181 396 ILE C CD1 
7391  N N   . SER C 366 ? 3.3433 3.2058 2.7354 0.8347  -0.2992 -0.1197 397 SER C N   
7392  C CA  . SER C 366 ? 3.3709 3.2386 2.7770 0.8296  -0.2986 -0.1197 397 SER C CA  
7393  C C   . SER C 366 ? 3.3204 3.2537 2.7746 0.8193  -0.2921 -0.1148 397 SER C C   
7394  O O   . SER C 366 ? 3.2286 3.1710 2.7139 0.8070  -0.2923 -0.1151 397 SER C O   
7395  C CB  . SER C 366 ? 3.5030 3.3479 2.8582 0.8498  -0.2973 -0.1186 397 SER C CB  
7396  O OG  . SER C 366 ? 3.6123 3.4979 2.9530 0.8649  -0.2889 -0.1123 397 SER C OG  
7397  N N   . ASN C 367 ? 3.2471 3.2265 2.7077 0.8237  -0.2867 -0.1095 398 ASN C N   
7398  C CA  . ASN C 367 ? 3.1839 3.2256 2.6881 0.8135  -0.2816 -0.1037 398 ASN C CA  
7399  C C   . ASN C 367 ? 3.1308 3.2141 2.6458 0.8140  -0.2791 -0.1005 398 ASN C C   
7400  O O   . ASN C 367 ? 3.0493 3.1520 2.6040 0.7991  -0.2815 -0.1031 398 ASN C O   
7401  C CB  . ASN C 367 ? 3.2447 3.3100 2.7349 0.8240  -0.2755 -0.0970 398 ASN C CB  
7402  C CG  . ASN C 367 ? 3.3757 3.4352 2.8140 0.8479  -0.2712 -0.0944 398 ASN C CG  
7403  O OD1 . ASN C 367 ? 3.4777 3.4894 2.8733 0.8615  -0.2733 -0.0985 398 ASN C OD1 
7404  N ND2 . ASN C 367 ? 3.4508 3.5586 2.8922 0.8533  -0.2652 -0.0876 398 ASN C ND2 
7405  N N   . ASN C 379 ? 2.7645 3.1241 2.8216 0.5197  -0.2615 -0.2533 411 ASN C N   
7406  C CA  . ASN C 379 ? 2.6777 3.0097 2.7736 0.5122  -0.2579 -0.2594 411 ASN C CA  
7407  C C   . ASN C 379 ? 2.5765 2.8715 2.6839 0.4931  -0.2451 -0.2810 411 ASN C C   
7408  O O   . ASN C 379 ? 2.5153 2.8141 2.6403 0.4703  -0.2410 -0.2934 411 ASN C O   
7409  C CB  . ASN C 379 ? 2.6373 2.9998 2.7634 0.4998  -0.2642 -0.2537 411 ASN C CB  
7410  C CG  . ASN C 379 ? 2.5293 2.8658 2.6961 0.4942  -0.2612 -0.2575 411 ASN C CG  
7411  O OD1 . ASN C 379 ? 2.4992 2.8030 2.6714 0.5062  -0.2573 -0.2586 411 ASN C OD1 
7412  N ND2 . ASN C 379 ? 2.4594 2.8102 2.6542 0.4750  -0.2631 -0.2591 411 ASN C ND2 
7413  N N   . ASP C 380 ? 2.5922 2.8515 2.6886 0.5022  -0.2389 -0.2855 412 ASP C N   
7414  C CA  . ASP C 380 ? 2.4404 2.6687 2.5479 0.4857  -0.2264 -0.3048 412 ASP C CA  
7415  C C   . ASP C 380 ? 2.4193 2.6093 2.5303 0.4957  -0.2213 -0.3055 412 ASP C C   
7416  O O   . ASP C 380 ? 2.4724 2.6551 2.5951 0.5097  -0.2268 -0.2944 412 ASP C O   
7417  C CB  . ASP C 380 ? 2.4364 2.6730 2.5152 0.4756  -0.2213 -0.3148 412 ASP C CB  
7418  C CG  . ASP C 380 ? 2.4017 2.6216 2.4962 0.4534  -0.2096 -0.3365 412 ASP C CG  
7419  O OD1 . ASP C 380 ? 2.3752 2.5851 2.5030 0.4430  -0.2069 -0.3435 412 ASP C OD1 
7420  O OD2 . ASP C 380 ? 2.4460 2.6621 2.5187 0.4475  -0.2029 -0.3462 412 ASP C OD2 
7421  N N   . SER C 381 ? 2.2916 2.4588 2.3924 0.4880  -0.2113 -0.3180 413 SER C N   
7422  C CA  . SER C 381 ? 2.2795 2.4126 2.3832 0.4938  -0.2061 -0.3189 413 SER C CA  
7423  C C   . SER C 381 ? 2.2456 2.3659 2.3131 0.4966  -0.2028 -0.3199 413 SER C C   
7424  O O   . SER C 381 ? 2.1906 2.3238 2.2401 0.4874  -0.1989 -0.3276 413 SER C O   
7425  C CB  . SER C 381 ? 2.1899 2.3057 2.3288 0.4789  -0.1951 -0.3339 413 SER C CB  
7426  O OG  . SER C 381 ? 2.1866 2.3109 2.3588 0.4762  -0.1981 -0.3321 413 SER C OG  
7427  N N   . ILE C 382 ? 2.2977 2.3927 2.3539 0.5086  -0.2049 -0.3116 414 ILE C N   
7428  C CA  . ILE C 382 ? 2.2815 2.3587 2.3036 0.5108  -0.2024 -0.3106 414 ILE C CA  
7429  C C   . ILE C 382 ? 2.1594 2.2164 2.1967 0.4961  -0.1902 -0.3230 414 ILE C C   
7430  O O   . ILE C 382 ? 2.1333 2.1700 2.1887 0.4973  -0.1888 -0.3213 414 ILE C O   
7431  C CB  . ILE C 382 ? 2.3425 2.4003 2.3383 0.5309  -0.2123 -0.2945 414 ILE C CB  
7432  C CG1 . ILE C 382 ? 2.4067 2.4869 2.3859 0.5489  -0.2242 -0.2813 414 ILE C CG1 
7433  C CG2 . ILE C 382 ? 2.3227 2.3590 2.2827 0.5305  -0.2098 -0.2932 414 ILE C CG2 
7434  C CD1 . ILE C 382 ? 2.4610 2.5440 2.4655 0.5591  -0.2312 -0.2738 414 ILE C CD1 
7435  N N   . THR C 383 ? 2.2900 2.3557 2.3205 0.4823  -0.1813 -0.3354 415 THR C N   
7436  C CA  . THR C 383 ? 2.2018 2.2542 2.2448 0.4691  -0.1690 -0.3476 415 THR C CA  
7437  C C   . THR C 383 ? 2.2047 2.2366 2.2200 0.4720  -0.1687 -0.3401 415 THR C C   
7438  O O   . THR C 383 ? 2.2446 2.2774 2.2238 0.4789  -0.1742 -0.3317 415 THR C O   
7439  C CB  . THR C 383 ? 2.1331 2.2039 2.1773 0.4541  -0.1599 -0.3643 415 THR C CB  
7440  O OG1 . THR C 383 ? 2.1344 2.2225 2.1990 0.4503  -0.1624 -0.3697 415 THR C OG1 
7441  C CG2 . THR C 383 ? 2.0776 2.1376 2.1396 0.4424  -0.1465 -0.3778 415 THR C CG2 
7442  N N   . LEU C 384 ? 2.1812 2.1949 2.2128 0.4666  -0.1625 -0.3420 416 LEU C N   
7443  C CA  . LEU C 384 ? 2.1655 2.1584 2.1736 0.4663  -0.1627 -0.3339 416 LEU C CA  
7444  C C   . LEU C 384 ? 2.1286 2.1236 2.1452 0.4509  -0.1493 -0.3448 416 LEU C C   
7445  O O   . LEU C 384 ? 2.0748 2.0738 2.1252 0.4442  -0.1407 -0.3547 416 LEU C O   
7446  C CB  . LEU C 384 ? 2.1577 2.1267 2.1716 0.4746  -0.1702 -0.3218 416 LEU C CB  
7447  C CG  . LEU C 384 ? 2.2480 2.2147 2.2531 0.4921  -0.1837 -0.3104 416 LEU C CG  
7448  C CD1 . LEU C 384 ? 2.2666 2.2094 2.2784 0.4990  -0.1903 -0.3005 416 LEU C CD1 
7449  C CD2 . LEU C 384 ? 2.3042 2.2697 2.2642 0.5019  -0.1912 -0.3019 416 LEU C CD2 
7450  N N   . PRO C 385 ? 2.1348 2.1281 2.1208 0.4463  -0.1473 -0.3424 417 PRO C N   
7451  C CA  . PRO C 385 ? 2.0838 2.0830 2.0744 0.4323  -0.1347 -0.3510 417 PRO C CA  
7452  C C   . PRO C 385 ? 2.0516 2.0364 2.0612 0.4272  -0.1312 -0.3469 417 PRO C C   
7453  O O   . PRO C 385 ? 2.1534 2.1166 2.1471 0.4299  -0.1390 -0.3326 417 PRO C O   
7454  C CB  . PRO C 385 ? 2.1529 2.1503 2.1014 0.4313  -0.1372 -0.3433 417 PRO C CB  
7455  C CG  . PRO C 385 ? 2.2181 2.2170 2.1431 0.4445  -0.1483 -0.3360 417 PRO C CG  
7456  C CD  . PRO C 385 ? 2.2257 2.2132 2.1696 0.4552  -0.1567 -0.3304 417 PRO C CD  
7457  N N   . CYS C 386 ? 2.0474 2.0442 2.0898 0.4200  -0.1195 -0.3595 418 CYS C N   
7458  C CA  . CYS C 386 ? 2.0607 2.0506 2.1254 0.4155  -0.1149 -0.3560 418 CYS C CA  
7459  C C   . CYS C 386 ? 2.0183 2.0234 2.0855 0.4037  -0.1015 -0.3635 418 CYS C C   
7460  O O   . CYS C 386 ? 1.9822 2.0057 2.0573 0.4006  -0.0916 -0.3792 418 CYS C O   
7461  C CB  . CYS C 386 ? 2.0594 2.0513 2.1642 0.4205  -0.1126 -0.3621 418 CYS C CB  
7462  S SG  . CYS C 386 ? 2.2823 2.2601 2.3869 0.4348  -0.1286 -0.3511 418 CYS C SG  
7463  N N   . ARG C 387 ? 1.9974 1.9950 2.0564 0.3969  -0.1020 -0.3518 419 ARG C N   
7464  C CA  . ARG C 387 ? 1.9660 1.9791 2.0276 0.3853  -0.0908 -0.3535 419 ARG C CA  
7465  C C   . ARG C 387 ? 1.8877 1.9065 1.9857 0.3839  -0.0841 -0.3541 419 ARG C C   
7466  O O   . ARG C 387 ? 1.9357 1.9414 2.0505 0.3902  -0.0906 -0.3487 419 ARG C O   
7467  C CB  . ARG C 387 ? 2.0370 2.0371 2.0642 0.3776  -0.0978 -0.3367 419 ARG C CB  
7468  C CG  . ARG C 387 ? 2.1686 2.1600 2.1552 0.3805  -0.1055 -0.3323 419 ARG C CG  
7469  C CD  . ARG C 387 ? 2.2704 2.2881 2.2486 0.3761  -0.0951 -0.3447 419 ARG C CD  
7470  N NE  . ARG C 387 ? 2.3390 2.3718 2.3201 0.3634  -0.0856 -0.3426 419 ARG C NE  
7471  C CZ  . ARG C 387 ? 2.3740 2.4268 2.3384 0.3560  -0.0782 -0.3457 419 ARG C CZ  
7472  N NH1 . ARG C 387 ? 2.3837 2.4432 2.3263 0.3598  -0.0792 -0.3516 419 ARG C NH1 
7473  N NH2 . ARG C 387 ? 2.3688 2.4381 2.3388 0.3448  -0.0699 -0.3421 419 ARG C NH2 
7474  N N   . ILE C 388 ? 1.5527 1.5941 1.6632 0.3767  -0.0707 -0.3605 420 ILE C N   
7475  C CA  . ILE C 388 ? 1.5400 1.5920 1.6848 0.3765  -0.0628 -0.3607 420 ILE C CA  
7476  C C   . ILE C 388 ? 1.5526 1.6200 1.6926 0.3641  -0.0576 -0.3506 420 ILE C C   
7477  O O   . ILE C 388 ? 1.5680 1.6532 1.6933 0.3578  -0.0501 -0.3548 420 ILE C O   
7478  C CB  . ILE C 388 ? 1.5316 1.6006 1.7043 0.3833  -0.0493 -0.3807 420 ILE C CB  
7479  C CG1 . ILE C 388 ? 1.5193 1.5739 1.7001 0.3933  -0.0550 -0.3892 420 ILE C CG1 
7480  C CG2 . ILE C 388 ? 1.5214 1.6042 1.7276 0.3846  -0.0399 -0.3798 420 ILE C CG2 
7481  C CD1 . ILE C 388 ? 1.5151 1.5798 1.7223 0.3991  -0.0431 -0.4078 420 ILE C CD1 
7482  N N   . LYS C 389 ? 1.5585 1.6211 1.7103 0.3599  -0.0618 -0.3368 421 LYS C N   
7483  C CA  . LYS C 389 ? 1.5665 1.6462 1.7165 0.3463  -0.0578 -0.3250 421 LYS C CA  
7484  C C   . LYS C 389 ? 1.5772 1.6782 1.7658 0.3486  -0.0484 -0.3257 421 LYS C C   
7485  O O   . LYS C 389 ? 1.5939 1.6838 1.8042 0.3570  -0.0521 -0.3256 421 LYS C O   
7486  C CB  . LYS C 389 ? 1.6098 1.6642 1.7320 0.3356  -0.0731 -0.3048 421 LYS C CB  
7487  C CG  . LYS C 389 ? 1.6354 1.7068 1.7493 0.3178  -0.0705 -0.2911 421 LYS C CG  
7488  C CD  . LYS C 389 ? 1.6885 1.7280 1.7695 0.3060  -0.0869 -0.2717 421 LYS C CD  
7489  C CE  . LYS C 389 ? 1.6978 1.7109 1.7875 0.3101  -0.0988 -0.2644 421 LYS C CE  
7490  N NZ  . LYS C 389 ? 1.7784 1.7552 1.8319 0.2991  -0.1155 -0.2468 421 LYS C NZ  
7491  N N   . GLN C 390 ? 1.5010 1.6350 1.6982 0.3422  -0.0358 -0.3260 422 GLN C N   
7492  C CA  . GLN C 390 ? 1.4883 1.6486 1.7210 0.3455  -0.0252 -0.3259 422 GLN C CA  
7493  C C   . GLN C 390 ? 1.4921 1.6630 1.7263 0.3305  -0.0298 -0.3048 422 GLN C C   
7494  O O   . GLN C 390 ? 1.5156 1.6941 1.7768 0.3334  -0.0290 -0.2994 422 GLN C O   
7495  C CB  . GLN C 390 ? 1.4930 1.6871 1.7378 0.3516  -0.0068 -0.3413 422 GLN C CB  
7496  C CG  . GLN C 390 ? 1.4884 1.6716 1.7397 0.3672  -0.0013 -0.3640 422 GLN C CG  
7497  C CD  . GLN C 390 ? 1.4991 1.7108 1.7565 0.3738  0.0160  -0.3812 422 GLN C CD  
7498  O OE1 . GLN C 390 ? 1.5138 1.7513 1.7578 0.3658  0.0223  -0.3781 422 GLN C OE1 
7499  N NE2 . GLN C 390 ? 1.4939 1.7001 1.7705 0.3887  0.0236  -0.3993 422 GLN C NE2 
7500  N N   . ILE C 391 ? 1.5276 1.7011 1.7336 0.3139  -0.0345 -0.2924 423 ILE C N   
7501  C CA  . ILE C 391 ? 1.5368 1.7186 1.7391 0.2956  -0.0406 -0.2710 423 ILE C CA  
7502  C C   . ILE C 391 ? 1.5436 1.6805 1.7232 0.2890  -0.0604 -0.2584 423 ILE C C   
7503  O O   . ILE C 391 ? 1.5623 1.6719 1.7066 0.2842  -0.0700 -0.2552 423 ILE C O   
7504  C CB  . ILE C 391 ? 1.5594 1.7666 1.7416 0.2797  -0.0359 -0.2629 423 ILE C CB  
7505  C CG1 . ILE C 391 ? 1.5556 1.8050 1.7551 0.2895  -0.0164 -0.2781 423 ILE C CG1 
7506  C CG2 . ILE C 391 ? 1.5695 1.7911 1.7515 0.2588  -0.0413 -0.2402 423 ILE C CG2 
7507  C CD1 . ILE C 391 ? 1.5774 1.8537 1.7558 0.2762  -0.0113 -0.2720 423 ILE C CD1 
7508  N N   . ILE C 392 ? 1.4921 1.6210 1.6904 0.2899  -0.0667 -0.2513 424 ILE C N   
7509  C CA  . ILE C 392 ? 1.4985 1.5836 1.6764 0.2870  -0.0853 -0.2416 424 ILE C CA  
7510  C C   . ILE C 392 ? 1.5101 1.5957 1.6851 0.2673  -0.0942 -0.2216 424 ILE C C   
7511  O O   . ILE C 392 ? 1.5047 1.6287 1.7031 0.2588  -0.0855 -0.2154 424 ILE C O   
7512  C CB  . ILE C 392 ? 1.4731 1.5422 1.6726 0.3068  -0.0877 -0.2518 424 ILE C CB  
7513  C CG1 . ILE C 392 ? 1.4513 1.5492 1.6923 0.3097  -0.0800 -0.2500 424 ILE C CG1 
7514  C CG2 . ILE C 392 ? 1.4630 1.5322 1.6662 0.3240  -0.0797 -0.2712 424 ILE C CG2 
7515  C CD1 . ILE C 392 ? 1.4277 1.5107 1.6906 0.3266  -0.0837 -0.2560 424 ILE C CD1 
7516  N N   . ASN C 393 ? 1.8771 1.9185 2.0214 0.2607  -0.1123 -0.2115 425 ASN C N   
7517  C CA  . ASN C 393 ? 1.9775 2.0071 2.1116 0.2411  -0.1248 -0.1929 425 ASN C CA  
7518  C C   . ASN C 393 ? 2.0758 2.0574 2.1943 0.2485  -0.1421 -0.1909 425 ASN C C   
7519  O O   . ASN C 393 ? 2.1795 2.1201 2.2587 0.2387  -0.1575 -0.1810 425 ASN C O   
7520  C CB  . ASN C 393 ? 2.0497 2.0724 2.1483 0.2172  -0.1308 -0.1783 425 ASN C CB  
7521  C CG  . ASN C 393 ? 2.1141 2.1906 2.2309 0.2047  -0.1160 -0.1741 425 ASN C CG  
7522  O OD1 . ASN C 393 ? 2.1567 2.2728 2.3099 0.2052  -0.1065 -0.1736 425 ASN C OD1 
7523  N ND2 . ASN C 393 ? 2.1438 2.2243 2.2350 0.1939  -0.1141 -0.1700 425 ASN C ND2 
7524  N N   . MET C 394 ? 2.3710 2.3569 2.5194 0.2669  -0.1396 -0.2001 426 MET C N   
7525  C CA  . MET C 394 ? 2.4041 2.3496 2.5404 0.2774  -0.1547 -0.1995 426 MET C CA  
7526  C C   . MET C 394 ? 2.4069 2.3370 2.5342 0.2605  -0.1683 -0.1838 426 MET C C   
7527  O O   . MET C 394 ? 2.4417 2.3985 2.5796 0.2409  -0.1650 -0.1733 426 MET C O   
7528  C CB  . MET C 394 ? 2.3393 2.2977 2.5124 0.3006  -0.1479 -0.2124 426 MET C CB  
7529  C CG  . MET C 394 ? 2.2740 2.2798 2.4948 0.3017  -0.1327 -0.2148 426 MET C CG  
7530  S SD  . MET C 394 ? 2.1018 2.1149 2.3621 0.3285  -0.1269 -0.2282 426 MET C SD  
7531  C CE  . MET C 394 ? 2.0749 2.0693 2.3161 0.3438  -0.1249 -0.2437 426 MET C CE  
7532  N N   . TRP C 395 ? 2.5919 2.4792 2.6980 0.2685  -0.1842 -0.1823 427 TRP C N   
7533  C CA  . TRP C 395 ? 2.6846 2.5477 2.7761 0.2549  -0.1999 -0.1694 427 TRP C CA  
7534  C C   . TRP C 395 ? 2.8155 2.6586 2.8692 0.2272  -0.2092 -0.1548 427 TRP C C   
7535  O O   . TRP C 395 ? 2.8416 2.6820 2.8926 0.2079  -0.2179 -0.1427 427 TRP C O   
7536  C CB  . TRP C 395 ? 2.5857 2.4885 2.7221 0.2514  -0.1935 -0.1664 427 TRP C CB  
7537  C CG  . TRP C 395 ? 2.4909 2.4058 2.6614 0.2766  -0.1880 -0.1776 427 TRP C CG  
7538  C CD1 . TRP C 395 ? 2.4379 2.3217 2.5998 0.2942  -0.1990 -0.1816 427 TRP C CD1 
7539  C CD2 . TRP C 395 ? 2.4528 2.4153 2.6718 0.2876  -0.1698 -0.1856 427 TRP C CD2 
7540  N NE1 . TRP C 395 ? 2.4611 2.3718 2.6646 0.3140  -0.1889 -0.1910 427 TRP C NE1 
7541  C CE2 . TRP C 395 ? 2.4591 2.4155 2.6973 0.3103  -0.1711 -0.1938 427 TRP C CE2 
7542  C CE3 . TRP C 395 ? 2.4117 2.4212 2.6584 0.2812  -0.1526 -0.1864 427 TRP C CE3 
7543  C CZ2 . TRP C 395 ? 2.4136 2.4056 2.6972 0.3255  -0.1561 -0.2025 427 TRP C CZ2 
7544  C CZ3 . TRP C 395 ? 2.3909 2.4347 2.6813 0.2983  -0.1375 -0.1960 427 TRP C CZ3 
7545  C CH2 . TRP C 395 ? 2.3954 2.4285 2.7036 0.3196  -0.1395 -0.2039 427 TRP C CH2 
7546  N N   . GLN C 396 ? 2.6600 2.4893 2.6836 0.2237  -0.2081 -0.1550 428 GLN C N   
7547  C CA  . GLN C 396 ? 2.7561 2.5642 2.7418 0.1969  -0.2173 -0.1400 428 GLN C CA  
7548  C C   . GLN C 396 ? 2.7292 2.5821 2.7397 0.1713  -0.2108 -0.1285 428 GLN C C   
7549  O O   . GLN C 396 ? 2.8025 2.6387 2.7916 0.1459  -0.2229 -0.1132 428 GLN C O   
7550  C CB  . GLN C 396 ? 2.8731 2.6177 2.8142 0.1922  -0.2396 -0.1319 428 GLN C CB  
7551  C CG  . GLN C 396 ? 2.9301 2.6230 2.8294 0.2115  -0.2490 -0.1375 428 GLN C CG  
7552  C CD  . GLN C 396 ? 3.0644 2.7075 2.9075 0.1930  -0.2633 -0.1244 428 GLN C CD  
7553  O OE1 . GLN C 396 ? 3.1728 2.7889 2.9959 0.1722  -0.2770 -0.1124 428 GLN C OE1 
7554  N NE2 . GLN C 396 ? 3.0514 2.6808 2.8677 0.2000  -0.2608 -0.1262 428 GLN C NE2 
7555  N N   . ARG C 397 ? 2.4782 2.3888 2.5332 0.1779  -0.1917 -0.1355 429 ARG C N   
7556  C CA  . ARG C 397 ? 2.4334 2.3950 2.5163 0.1578  -0.1835 -0.1250 429 ARG C CA  
7557  C C   . ARG C 397 ? 2.4896 2.4779 2.5636 0.1437  -0.1740 -0.1200 429 ARG C C   
7558  O O   . ARG C 397 ? 2.4785 2.4782 2.5561 0.1594  -0.1622 -0.1324 429 ARG C O   
7559  C CB  . ARG C 397 ? 2.3100 2.3204 2.4470 0.1759  -0.1676 -0.1351 429 ARG C CB  
7560  C CG  . ARG C 397 ? 2.2953 2.2909 2.4489 0.1892  -0.1750 -0.1385 429 ARG C CG  
7561  C CD  . ARG C 397 ? 2.2408 2.2544 2.4056 0.1679  -0.1814 -0.1232 429 ARG C CD  
7562  N NE  . ARG C 397 ? 2.2224 2.2984 2.4165 0.1556  -0.1662 -0.1164 429 ARG C NE  
7563  C CZ  . ARG C 397 ? 2.1280 2.2534 2.3670 0.1727  -0.1478 -0.1247 429 ARG C CZ  
7564  N NH1 . ARG C 397 ? 2.0063 2.1245 2.2666 0.2006  -0.1428 -0.1397 429 ARG C NH1 
7565  N NH2 . ARG C 397 ? 2.1662 2.3483 2.4279 0.1622  -0.1345 -0.1174 429 ARG C NH2 
7566  N N   . ILE C 398 ? 2.4583 2.4584 2.5207 0.1134  -0.1793 -0.1017 430 ILE C N   
7567  C CA  . ILE C 398 ? 2.5258 2.5585 2.5818 0.0970  -0.1705 -0.0937 430 ILE C CA  
7568  C C   . ILE C 398 ? 2.5133 2.6134 2.6079 0.0836  -0.1592 -0.0844 430 ILE C C   
7569  O O   . ILE C 398 ? 2.5760 2.6803 2.6776 0.0675  -0.1679 -0.0724 430 ILE C O   
7570  C CB  . ILE C 398 ? 2.6024 2.5905 2.6066 0.0711  -0.1873 -0.0776 430 ILE C CB  
7571  C CG1 . ILE C 398 ? 2.6169 2.5363 2.5820 0.0879  -0.1992 -0.0863 430 ILE C CG1 
7572  C CG2 . ILE C 398 ? 2.6210 2.6456 2.6193 0.0555  -0.1775 -0.0691 430 ILE C CG2 
7573  C CD1 . ILE C 398 ? 2.5396 2.4674 2.5100 0.1144  -0.1860 -0.1039 430 ILE C CD1 
7574  N N   . GLY C 399 ? 2.3108 2.4649 2.4292 0.0907  -0.1400 -0.0898 431 GLY C N   
7575  C CA  . GLY C 399 ? 2.2727 2.4968 2.4280 0.0825  -0.1267 -0.0818 431 GLY C CA  
7576  C C   . GLY C 399 ? 2.1399 2.4049 2.3398 0.1126  -0.1069 -0.0996 431 GLY C C   
7577  O O   . GLY C 399 ? 2.1378 2.4638 2.3638 0.1134  -0.0907 -0.0978 431 GLY C O   
7578  N N   . GLN C 400 ? 2.0993 2.3315 2.3072 0.1376  -0.1082 -0.1162 432 GLN C N   
7579  C CA  . GLN C 400 ? 1.9598 2.2210 2.2079 0.1664  -0.0914 -0.1334 432 GLN C CA  
7580  C C   . GLN C 400 ? 1.8630 2.0931 2.1004 0.1898  -0.0875 -0.1541 432 GLN C C   
7581  O O   . GLN C 400 ? 1.8794 2.0610 2.1034 0.2000  -0.0986 -0.1609 432 GLN C O   
7582  C CB  . GLN C 400 ? 1.9909 2.2468 2.2632 0.1736  -0.0968 -0.1323 432 GLN C CB  
7583  C CG  . GLN C 400 ? 2.0050 2.3177 2.3246 0.1876  -0.0794 -0.1355 432 GLN C CG  
7584  C CD  . GLN C 400 ? 2.0000 2.3705 2.3290 0.1667  -0.0726 -0.1182 432 GLN C CD  
7585  O OE1 . GLN C 400 ? 1.9313 2.3477 2.2766 0.1748  -0.0553 -0.1225 432 GLN C OE1 
7586  N NE2 . GLN C 400 ? 2.0742 2.4437 2.3920 0.1395  -0.0867 -0.0983 432 GLN C NE2 
7587  N N   . ALA C 401 ? 1.6930 1.9527 1.9353 0.1979  -0.0720 -0.1637 433 ALA C N   
7588  C CA  . ALA C 401 ? 1.6873 1.9251 1.9212 0.2186  -0.0668 -0.1838 433 ALA C CA  
7589  C C   . ALA C 401 ? 1.6834 1.9528 1.9565 0.2433  -0.0489 -0.2009 433 ALA C C   
7590  O O   . ALA C 401 ? 1.6860 2.0061 1.9819 0.2440  -0.0342 -0.1995 433 ALA C O   
7591  C CB  . ALA C 401 ? 1.7104 1.9537 1.9159 0.2091  -0.0636 -0.1831 433 ALA C CB  
7592  N N   . MET C 402 ? 1.5749 1.8141 1.8548 0.2638  -0.0503 -0.2163 434 MET C N   
7593  C CA  . MET C 402 ? 1.5898 1.8489 1.9046 0.2875  -0.0353 -0.2328 434 MET C CA  
7594  C C   . MET C 402 ? 1.5904 1.8422 1.8963 0.3019  -0.0266 -0.2530 434 MET C C   
7595  O O   . MET C 402 ? 1.5693 1.7828 1.8496 0.3035  -0.0363 -0.2585 434 MET C O   
7596  C CB  . MET C 402 ? 1.5890 1.8241 1.9228 0.3002  -0.0422 -0.2355 434 MET C CB  
7597  C CG  . MET C 402 ? 1.6063 1.8646 1.9785 0.3227  -0.0265 -0.2493 434 MET C CG  
7598  S SD  . MET C 402 ? 1.6121 1.8372 2.0034 0.3415  -0.0336 -0.2568 434 MET C SD  
7599  C CE  . MET C 402 ? 1.5981 1.7794 1.9583 0.3481  -0.0408 -0.2717 434 MET C CE  
7600  N N   . TYR C 403 ? 1.6262 1.9155 1.9523 0.3129  -0.0086 -0.2637 435 TYR C N   
7601  C CA  . TYR C 403 ? 1.5972 1.8828 1.9184 0.3276  0.0013  -0.2850 435 TYR C CA  
7602  C C   . TYR C 403 ? 1.6035 1.8765 1.9515 0.3498  0.0064  -0.3007 435 TYR C C   
7603  O O   . TYR C 403 ? 1.6411 1.9411 2.0196 0.3612  0.0186  -0.3037 435 TYR C O   
7604  C CB  . TYR C 403 ? 1.5901 1.9209 1.9140 0.3280  0.0178  -0.2894 435 TYR C CB  
7605  C CG  . TYR C 403 ? 1.5384 1.8640 1.8573 0.3440  0.0280  -0.3134 435 TYR C CG  
7606  C CD1 . TYR C 403 ? 1.4918 1.8016 1.7786 0.3380  0.0237  -0.3193 435 TYR C CD1 
7607  C CD2 . TYR C 403 ? 1.5368 1.8727 1.8824 0.3652  0.0417  -0.3303 435 TYR C CD2 
7608  C CE1 . TYR C 403 ? 1.4464 1.7527 1.7284 0.3515  0.0325  -0.3417 435 TYR C CE1 
7609  C CE2 . TYR C 403 ? 1.4885 1.8165 1.8280 0.3785  0.0501  -0.3530 435 TYR C CE2 
7610  C CZ  . TYR C 403 ? 1.4443 1.7587 1.7523 0.3709  0.0454  -0.3589 435 TYR C CZ  
7611  O OH  . TYR C 403 ? 1.4482 1.7562 1.7496 0.3828  0.0533  -0.3818 435 TYR C OH  
7612  N N   . ALA C 404 ? 1.5058 1.7388 1.8421 0.3560  -0.0030 -0.3095 436 ALA C N   
7613  C CA  . ALA C 404 ? 1.4894 1.7080 1.8490 0.3751  0.0003  -0.3235 436 ALA C CA  
7614  C C   . ALA C 404 ? 1.4971 1.7314 1.8632 0.3878  0.0168  -0.3437 436 ALA C C   
7615  O O   . ALA C 404 ? 1.5117 1.7409 1.8534 0.3849  0.0177  -0.3533 436 ALA C O   
7616  C CB  . ALA C 404 ? 1.4846 1.6606 1.8281 0.3774  -0.0144 -0.3266 436 ALA C CB  
7617  N N   . PRO C 405 ? 1.4865 1.7393 1.8834 0.4025  0.0299  -0.3508 437 PRO C N   
7618  C CA  . PRO C 405 ? 1.4990 1.7628 1.8992 0.4158  0.0454  -0.3712 437 PRO C CA  
7619  C C   . PRO C 405 ? 1.5019 1.7306 1.8915 0.4228  0.0415  -0.3893 437 PRO C C   
7620  O O   . PRO C 405 ? 1.4882 1.6877 1.8826 0.4249  0.0304  -0.3876 437 PRO C O   
7621  C CB  . PRO C 405 ? 1.4908 1.7752 1.9268 0.4316  0.0578  -0.3720 437 PRO C CB  
7622  C CG  . PRO C 405 ? 1.4692 1.7391 1.9219 0.4296  0.0462  -0.3573 437 PRO C CG  
7623  C CD  . PRO C 405 ? 1.4714 1.7345 1.9000 0.4085  0.0308  -0.3404 437 PRO C CD  
7624  N N   . PRO C 406 ? 1.5588 1.7908 1.9324 0.4257  0.0497  -0.4067 438 PRO C N   
7625  C CA  . PRO C 406 ? 1.5218 1.7232 1.8838 0.4303  0.0458  -0.4243 438 PRO C CA  
7626  C C   . PRO C 406 ? 1.5360 1.7182 1.9244 0.4453  0.0484  -0.4338 438 PRO C C   
7627  O O   . PRO C 406 ? 1.5682 1.7647 1.9823 0.4567  0.0589  -0.4337 438 PRO C O   
7628  C CB  . PRO C 406 ? 1.5380 1.7554 1.8826 0.4319  0.0576  -0.4412 438 PRO C CB  
7629  C CG  . PRO C 406 ? 1.5431 1.7971 1.8813 0.4229  0.0625  -0.4275 438 PRO C CG  
7630  C CD  . PRO C 406 ? 1.5426 1.8099 1.9073 0.4242  0.0626  -0.4102 438 PRO C CD  
7631  N N   . ILE C 407 ? 1.6171 1.7682 1.9990 0.4455  0.0386  -0.4410 439 ILE C N   
7632  C CA  . ILE C 407 ? 1.6276 1.7573 2.0324 0.4574  0.0390  -0.4490 439 ILE C CA  
7633  C C   . ILE C 407 ? 1.6259 1.7390 2.0191 0.4614  0.0434  -0.4725 439 ILE C C   
7634  O O   . ILE C 407 ? 1.6330 1.7378 2.0002 0.4521  0.0363  -0.4779 439 ILE C O   
7635  C CB  . ILE C 407 ? 1.6348 1.7435 2.0445 0.4539  0.0225  -0.4356 439 ILE C CB  
7636  C CG1 . ILE C 407 ? 1.6657 1.7879 2.0787 0.4469  0.0159  -0.4130 439 ILE C CG1 
7637  C CG2 . ILE C 407 ? 1.6465 1.7380 2.0842 0.4662  0.0235  -0.4404 439 ILE C CG2 
7638  C CD1 . ILE C 407 ? 1.7094 1.8541 2.1514 0.4544  0.0262  -0.4058 439 ILE C CD1 
7639  N N   . GLN C 408 ? 1.8386 1.9465 2.2501 0.4751  0.0550  -0.4860 440 GLN C N   
7640  C CA  . GLN C 408 ? 1.8417 1.9304 2.2426 0.4790  0.0598  -0.5098 440 GLN C CA  
7641  C C   . GLN C 408 ? 1.8491 1.9067 2.2497 0.4746  0.0466  -0.5121 440 GLN C C   
7642  O O   . GLN C 408 ? 1.8940 1.9415 2.3149 0.4770  0.0390  -0.4995 440 GLN C O   
7643  C CB  . GLN C 408 ? 1.8620 1.9499 2.2814 0.4965  0.0757  -0.5228 440 GLN C CB  
7644  C CG  . GLN C 408 ? 1.8844 2.0081 2.3133 0.5046  0.0890  -0.5157 440 GLN C CG  
7645  C CD  . GLN C 408 ? 1.9892 2.1240 2.4484 0.5102  0.0881  -0.4952 440 GLN C CD  
7646  O OE1 . GLN C 408 ? 1.9533 2.0800 2.4185 0.5015  0.0745  -0.4796 440 GLN C OE1 
7647  N NE2 . GLN C 408 ? 2.0812 2.2361 2.5586 0.5255  0.1026  -0.4952 440 GLN C NE2 
7648  N N   . GLY C 409 ? 1.7895 1.8348 2.1667 0.4677  0.0437  -0.5279 441 GLY C N   
7649  C CA  . GLY C 409 ? 1.7813 1.8009 2.1562 0.4624  0.0320  -0.5316 441 GLY C CA  
7650  C C   . GLY C 409 ? 1.7600 1.7819 2.1233 0.4517  0.0157  -0.5149 441 GLY C C   
7651  O O   . GLY C 409 ? 1.7412 1.7786 2.1013 0.4488  0.0120  -0.4980 441 GLY C O   
7652  N N   . VAL C 410 ? 1.8593 1.8646 2.2144 0.4456  0.0055  -0.5197 442 VAL C N   
7653  C CA  . VAL C 410 ? 1.8725 1.8792 2.2154 0.4380  -0.0102 -0.5047 442 VAL C CA  
7654  C C   . VAL C 410 ? 1.8686 1.8713 2.2365 0.4440  -0.0173 -0.4857 442 VAL C C   
7655  O O   . VAL C 410 ? 1.8733 1.8632 2.2664 0.4507  -0.0160 -0.4872 442 VAL C O   
7656  C CB  . VAL C 410 ? 1.9054 1.9005 2.2335 0.4300  -0.0185 -0.5149 442 VAL C CB  
7657  C CG1 . VAL C 410 ? 1.9223 1.9206 2.2401 0.4255  -0.0346 -0.4979 442 VAL C CG1 
7658  C CG2 . VAL C 410 ? 1.9096 1.9115 2.2104 0.4231  -0.0121 -0.5331 442 VAL C CG2 
7659  N N   . ILE C 411 ? 1.7918 1.8043 2.1516 0.4419  -0.0252 -0.4678 443 ILE C N   
7660  C CA  . ILE C 411 ? 1.7875 1.7978 2.1674 0.4473  -0.0327 -0.4493 443 ILE C CA  
7661  C C   . ILE C 411 ? 1.8147 1.8171 2.1858 0.4452  -0.0488 -0.4403 443 ILE C C   
7662  O O   . ILE C 411 ? 1.8301 1.8355 2.1722 0.4390  -0.0563 -0.4383 443 ILE C O   
7663  C CB  . ILE C 411 ? 1.7664 1.7902 2.1419 0.4460  -0.0321 -0.4348 443 ILE C CB  
7664  C CG1 . ILE C 411 ? 1.7398 1.7783 2.1213 0.4475  -0.0160 -0.4430 443 ILE C CG1 
7665  C CG2 . ILE C 411 ? 1.7598 1.7815 2.1569 0.4515  -0.0394 -0.4173 443 ILE C CG2 
7666  C CD1 . ILE C 411 ? 1.7203 1.7749 2.0985 0.4438  -0.0155 -0.4279 443 ILE C CD1 
7667  N N   . ARG C 412 ? 2.0378 2.0321 2.4335 0.4512  -0.0539 -0.4343 444 ARG C N   
7668  C CA  . ARG C 412 ? 2.0837 2.0745 2.4745 0.4512  -0.0691 -0.4237 444 ARG C CA  
7669  C C   . ARG C 412 ? 2.0973 2.0885 2.5096 0.4593  -0.0753 -0.4061 444 ARG C C   
7670  O O   . ARG C 412 ? 2.0566 2.0472 2.4978 0.4653  -0.0680 -0.4052 444 ARG C O   
7671  C CB  . ARG C 412 ? 2.0982 2.0808 2.4960 0.4487  -0.0714 -0.4338 444 ARG C CB  
7672  C CG  . ARG C 412 ? 2.1633 2.1485 2.5541 0.4482  -0.0872 -0.4224 444 ARG C CG  
7673  C CD  . ARG C 412 ? 2.2001 2.1779 2.6085 0.4459  -0.0896 -0.4280 444 ARG C CD  
7674  N NE  . ARG C 412 ? 2.2222 2.1924 2.6660 0.4538  -0.0857 -0.4233 444 ARG C NE  
7675  C CZ  . ARG C 412 ? 2.2612 2.2232 2.7253 0.4532  -0.0884 -0.4239 444 ARG C CZ  
7676  N NH1 . ARG C 412 ? 2.3448 2.3062 2.7971 0.4436  -0.0955 -0.4291 444 ARG C NH1 
7677  N NH2 . ARG C 412 ? 2.2787 2.2345 2.7747 0.4615  -0.0843 -0.4184 444 ARG C NH2 
7678  N N   . CYS C 413 ? 2.0862 2.0790 2.4825 0.4604  -0.0888 -0.3921 445 CYS C N   
7679  C CA  . CYS C 413 ? 2.0670 2.0599 2.4772 0.4681  -0.0973 -0.3751 445 CYS C CA  
7680  C C   . CYS C 413 ? 2.0461 2.0389 2.4406 0.4715  -0.1132 -0.3645 445 CYS C C   
7681  O O   . CYS C 413 ? 2.0396 2.0331 2.4024 0.4682  -0.1190 -0.3649 445 CYS C O   
7682  C CB  . CYS C 413 ? 2.0678 2.0633 2.4737 0.4675  -0.0947 -0.3669 445 CYS C CB  
7683  S SG  . CYS C 413 ? 2.1286 2.1221 2.4901 0.4601  -0.1001 -0.3631 445 CYS C SG  
7684  N N   . VAL C 414 ? 2.0269 2.0211 2.4442 0.4794  -0.1196 -0.3542 446 VAL C N   
7685  C CA  . VAL C 414 ? 2.0500 2.0477 2.4575 0.4858  -0.1346 -0.3422 446 VAL C CA  
7686  C C   . VAL C 414 ? 2.0444 2.0408 2.4570 0.4941  -0.1411 -0.3271 446 VAL C C   
7687  O O   . VAL C 414 ? 2.0257 2.0241 2.4692 0.4978  -0.1369 -0.3235 446 VAL C O   
7688  C CB  . VAL C 414 ? 2.0630 2.0663 2.4934 0.4873  -0.1374 -0.3427 446 VAL C CB  
7689  C CG1 . VAL C 414 ? 2.0602 2.0727 2.4801 0.4950  -0.1528 -0.3290 446 VAL C CG1 
7690  C CG2 . VAL C 414 ? 2.0680 2.0696 2.4934 0.4769  -0.1307 -0.3592 446 VAL C CG2 
7691  N N   . SER C 415 ? 1.9760 1.9680 2.3568 0.4974  -0.1515 -0.3186 447 SER C N   
7692  C CA  . SER C 415 ? 1.9216 1.9081 2.3002 0.5041  -0.1588 -0.3055 447 SER C CA  
7693  C C   . SER C 415 ? 1.9371 1.9251 2.2998 0.5158  -0.1742 -0.2942 447 SER C C   
7694  O O   . SER C 415 ? 1.9517 1.9473 2.3037 0.5181  -0.1789 -0.2955 447 SER C O   
7695  C CB  . SER C 415 ? 1.9180 1.8929 2.2698 0.4972  -0.1571 -0.3051 447 SER C CB  
7696  O OG  . SER C 415 ? 1.9014 1.8799 2.2689 0.4876  -0.1426 -0.3143 447 SER C OG  
7697  N N   . ASN C 416 ? 1.9462 1.9283 2.3067 0.5235  -0.1823 -0.2827 448 ASN C N   
7698  C CA  . ASN C 416 ? 1.9418 1.9243 2.2844 0.5360  -0.1966 -0.2707 448 ASN C CA  
7699  C C   . ASN C 416 ? 1.9615 1.9235 2.2612 0.5394  -0.2051 -0.2667 448 ASN C C   
7700  O O   . ASN C 416 ? 1.9953 1.9437 2.2916 0.5344  -0.2041 -0.2644 448 ASN C O   
7701  C CB  . ASN C 416 ? 1.9230 1.9136 2.2866 0.5295  -0.1946 -0.2544 448 ASN C CB  
7702  C CG  . ASN C 416 ? 1.8919 1.9017 2.2855 0.5241  -0.1886 -0.2513 448 ASN C CG  
7703  O OD1 . ASN C 416 ? 1.8922 1.9064 2.3002 0.5229  -0.1831 -0.2647 448 ASN C OD1 
7704  N ND2 . ASN C 416 ? 1.9670 1.9868 2.3704 0.5209  -0.1894 -0.2345 448 ASN C ND2 
7705  N N   . ILE C 417 ? 1.8784 1.8380 2.1437 0.5465  -0.2132 -0.2646 449 ILE C N   
7706  C CA  . ILE C 417 ? 1.9155 1.8521 2.1361 0.5519  -0.2227 -0.2585 449 ILE C CA  
7707  C C   . ILE C 417 ? 1.9261 1.8591 2.1399 0.5628  -0.2336 -0.2447 449 ILE C C   
7708  O O   . ILE C 417 ? 1.9299 1.8774 2.1344 0.5662  -0.2374 -0.2353 449 ILE C O   
7709  C CB  . ILE C 417 ? 1.9469 1.8831 2.1308 0.5548  -0.2256 -0.2604 449 ILE C CB  
7710  C CG1 . ILE C 417 ? 1.9322 1.8754 2.1217 0.5382  -0.2125 -0.2728 449 ILE C CG1 
7711  C CG2 . ILE C 417 ? 1.9919 1.9000 2.1282 0.5617  -0.2353 -0.2534 449 ILE C CG2 
7712  C CD1 . ILE C 417 ? 1.9626 1.9073 2.1158 0.5397  -0.2148 -0.2746 449 ILE C CD1 
7713  N N   . THR C 418 ? 1.8633 1.7800 2.0781 0.5595  -0.2355 -0.2401 450 THR C N   
7714  C CA  . THR C 418 ? 1.8668 1.7824 2.0744 0.5585  -0.2410 -0.2249 450 THR C CA  
7715  C C   . THR C 418 ? 1.9136 1.7962 2.0759 0.5667  -0.2537 -0.2202 450 THR C C   
7716  O O   . THR C 418 ? 1.9139 1.7916 2.0687 0.5659  -0.2586 -0.2099 450 THR C O   
7717  C CB  . THR C 418 ? 1.8291 1.7558 2.0773 0.5479  -0.2334 -0.2219 450 THR C CB  
7718  O OG1 . THR C 418 ? 1.8294 1.7387 2.0822 0.5467  -0.2335 -0.2302 450 THR C OG1 
7719  C CG2 . THR C 418 ? 1.7879 1.7424 2.0782 0.5403  -0.2207 -0.2254 450 THR C CG2 
7720  N N   . GLY C 419 ? 1.9069 1.7647 2.0371 0.5747  -0.2593 -0.2277 451 GLY C N   
7721  C CA  . GLY C 419 ? 1.9432 1.7636 2.0267 0.5827  -0.2722 -0.2226 451 GLY C CA  
7722  C C   . GLY C 419 ? 1.9547 1.7496 2.0023 0.5758  -0.2717 -0.2264 451 GLY C C   
7723  O O   . GLY C 419 ? 1.9259 1.7338 1.9889 0.5601  -0.2595 -0.2333 451 GLY C O   
7724  N N   . LEU C 420 ? 1.9025 1.6612 1.9000 0.5845  -0.2837 -0.2208 452 LEU C N   
7725  C CA  . LEU C 420 ? 1.9260 1.6576 1.8830 0.5755  -0.2836 -0.2209 452 LEU C CA  
7726  C C   . LEU C 420 ? 1.9861 1.6735 1.9107 0.5681  -0.2930 -0.2154 452 LEU C C   
7727  O O   . LEU C 420 ? 2.0811 1.7539 2.0025 0.5761  -0.3029 -0.2112 452 LEU C O   
7728  C CB  . LEU C 420 ? 1.9750 1.7029 1.8937 0.5951  -0.2894 -0.2186 452 LEU C CB  
7729  C CG  . LEU C 420 ? 1.9590 1.7309 1.9051 0.6048  -0.2837 -0.2220 452 LEU C CG  
7730  C CD1 . LEU C 420 ? 2.0934 1.8641 1.9989 0.6250  -0.2905 -0.2177 452 LEU C CD1 
7731  C CD2 . LEU C 420 ? 1.9271 1.7264 1.9090 0.5840  -0.2680 -0.2313 452 LEU C CD2 
7732  N N   . ILE C 421 ? 1.8172 1.4834 1.7168 0.5517  -0.2902 -0.2152 453 ILE C N   
7733  C CA  . ILE C 421 ? 1.8607 1.4801 1.7213 0.5419  -0.2999 -0.2090 453 ILE C CA  
7734  C C   . ILE C 421 ? 1.9331 1.5211 1.7382 0.5498  -0.3057 -0.2055 453 ILE C C   
7735  O O   . ILE C 421 ? 1.9340 1.5262 1.7332 0.5361  -0.2975 -0.2070 453 ILE C O   
7736  C CB  . ILE C 421 ? 1.8584 1.4824 1.7411 0.5119  -0.2914 -0.2097 453 ILE C CB  
7737  C CG1 . ILE C 421 ? 1.8165 1.4746 1.7549 0.5062  -0.2846 -0.2126 453 ILE C CG1 
7738  C CG2 . ILE C 421 ? 1.9060 1.4814 1.7472 0.4993  -0.3029 -0.2020 453 ILE C CG2 
7739  C CD1 . ILE C 421 ? 1.8131 1.4809 1.7752 0.4787  -0.2762 -0.2120 453 ILE C CD1 
7740  N N   . LEU C 422 ? 1.9864 1.5434 1.7499 0.5730  -0.3196 -0.2006 454 LEU C N   
7741  C CA  . LEU C 422 ? 2.1310 1.6589 1.8403 0.5864  -0.3256 -0.1965 454 LEU C CA  
7742  C C   . LEU C 422 ? 2.2332 1.6983 1.8890 0.5815  -0.3384 -0.1896 454 LEU C C   
7743  O O   . LEU C 422 ? 2.2559 1.6958 1.9087 0.5762  -0.3471 -0.1877 454 LEU C O   
7744  C CB  . LEU C 422 ? 2.2008 1.7406 1.8963 0.6199  -0.3315 -0.1952 454 LEU C CB  
7745  C CG  . LEU C 422 ? 2.1054 1.7054 1.8495 0.6250  -0.3208 -0.2008 454 LEU C CG  
7746  C CD1 . LEU C 422 ? 2.2476 1.8598 1.9737 0.6576  -0.3282 -0.1971 454 LEU C CD1 
7747  C CD2 . LEU C 422 ? 2.0546 1.6795 1.8122 0.6080  -0.3071 -0.2056 454 LEU C CD2 
7748  N N   . THR C 423 ? 2.3323 1.7721 1.9450 0.5824  -0.3396 -0.1856 455 THR C N   
7749  C CA  . THR C 423 ? 2.4090 1.7845 1.9633 0.5795  -0.3521 -0.1781 455 THR C CA  
7750  C C   . THR C 423 ? 2.5336 1.8853 2.0352 0.6085  -0.3589 -0.1737 455 THR C C   
7751  O O   . THR C 423 ? 2.5471 1.9345 2.0564 0.6194  -0.3505 -0.1753 455 THR C O   
7752  C CB  . THR C 423 ? 2.3875 1.7516 1.9390 0.5462  -0.3463 -0.1751 455 THR C CB  
7753  O OG1 . THR C 423 ? 2.4637 1.8626 2.0260 0.5433  -0.3333 -0.1774 455 THR C OG1 
7754  C CG2 . THR C 423 ? 2.2211 1.6071 1.8200 0.5185  -0.3404 -0.1779 455 THR C CG2 
7755  N N   . ARG C 424 ? 2.6961 1.9867 2.1426 0.6213  -0.3744 -0.1680 456 ARG C N   
7756  C CA  . ARG C 424 ? 2.7825 2.0429 2.1726 0.6526  -0.3826 -0.1628 456 ARG C CA  
7757  C C   . ARG C 424 ? 2.9127 2.1190 2.2503 0.6411  -0.3871 -0.1552 456 ARG C C   
7758  O O   . ARG C 424 ? 2.9215 2.0903 2.2493 0.6145  -0.3918 -0.1526 456 ARG C O   
7759  C CB  . ARG C 424 ? 2.8367 2.0636 2.1968 0.6810  -0.3977 -0.1620 456 ARG C CB  
7760  C CG  . ARG C 424 ? 2.9525 2.1648 2.2618 0.7146  -0.4028 -0.1571 456 ARG C CG  
7761  C CD  . ARG C 424 ? 2.9904 2.2124 2.2933 0.7188  -0.4044 -0.1579 456 ARG C CD  
7762  N NE  . ARG C 424 ? 2.9994 2.1609 2.2790 0.7081  -0.4178 -0.1583 456 ARG C NE  
7763  C CZ  . ARG C 424 ? 3.1382 2.2318 2.3539 0.7122  -0.4295 -0.1544 456 ARG C CZ  
7764  N NH1 . ARG C 424 ? 3.2525 2.3305 2.4211 0.7282  -0.4285 -0.1496 456 ARG C NH1 
7765  N NH2 . ARG C 424 ? 3.1977 2.2380 2.3957 0.6999  -0.4424 -0.1553 456 ARG C NH2 
7766  N N   . ASP C 425 ? 2.8660 2.0700 2.1698 0.6607  -0.3857 -0.1508 457 ASP C N   
7767  C CA  . ASP C 425 ? 2.9445 2.0989 2.1979 0.6515  -0.3894 -0.1424 457 ASP C CA  
7768  C C   . ASP C 425 ? 3.0554 2.1293 2.2422 0.6683  -0.4078 -0.1365 457 ASP C C   
7769  O O   . ASP C 425 ? 3.0763 2.1373 2.2508 0.6944  -0.4172 -0.1390 457 ASP C O   
7770  C CB  . ASP C 425 ? 2.9564 2.1385 2.1967 0.6672  -0.3811 -0.1391 457 ASP C CB  
7771  C CG  . ASP C 425 ? 2.8554 2.1104 2.1553 0.6478  -0.3633 -0.1455 457 ASP C CG  
7772  O OD1 . ASP C 425 ? 2.8378 2.0955 2.1460 0.6189  -0.3560 -0.1440 457 ASP C OD1 
7773  O OD2 . ASP C 425 ? 2.7947 2.1040 2.1327 0.6611  -0.3570 -0.1521 457 ASP C OD2 
7774  N N   . GLY C 426 ? 3.2926 2.3115 2.4346 0.6532  -0.4132 -0.1283 458 GLY C N   
7775  C CA  . GLY C 426 ? 3.4611 2.3951 2.5348 0.6655  -0.4311 -0.1224 458 GLY C CA  
7776  C C   . GLY C 426 ? 3.6482 2.5494 2.6610 0.6984  -0.4354 -0.1148 458 GLY C C   
7777  O O   . GLY C 426 ? 3.7953 2.6258 2.7463 0.7187  -0.4505 -0.1107 458 GLY C O   
7778  N N   . GLY C 427 ? 3.8403 2.7922 2.8686 0.7049  -0.4224 -0.1129 459 GLY C N   
7779  C CA  . GLY C 427 ? 3.9459 2.8751 2.9192 0.7375  -0.4251 -0.1047 459 GLY C CA  
7780  C C   . GLY C 427 ? 4.0634 2.9985 3.0180 0.7740  -0.4291 -0.1080 459 GLY C C   
7781  O O   . GLY C 427 ? 3.9558 2.9652 2.9549 0.7821  -0.4182 -0.1146 459 GLY C O   
7782  N N   . SER C 428 ? 3.9817 2.8582 2.8795 0.7788  -0.4371 -0.1057 460 SER C N   
7783  C CA  . SER C 428 ? 4.0250 2.9234 2.9132 0.7947  -0.4336 -0.1122 460 SER C CA  
7784  C C   . SER C 428 ? 4.2195 3.0555 3.0346 0.8081  -0.4398 -0.1087 460 SER C C   
7785  O O   . SER C 428 ? 4.2762 3.0341 3.0503 0.7956  -0.4525 -0.1041 460 SER C O   
7786  C CB  . SER C 428 ? 3.9076 2.8130 2.8290 0.7814  -0.4383 -0.1210 460 SER C CB  
7787  O OG  . SER C 428 ? 3.9192 2.7482 2.8142 0.7625  -0.4532 -0.1194 460 SER C OG  
7788  N N   . THR C 429 ? 4.1436 3.0086 2.9393 0.8325  -0.4317 -0.1107 461 THR C N   
7789  C CA  . THR C 429 ? 4.1220 3.0757 2.9560 0.8483  -0.4166 -0.1143 461 THR C CA  
7790  C C   . THR C 429 ? 4.0293 3.0398 2.9269 0.8370  -0.4133 -0.1223 461 THR C C   
7791  O O   . THR C 429 ? 3.9479 3.0245 2.8988 0.8334  -0.4041 -0.1232 461 THR C O   
7792  C CB  . THR C 429 ? 4.0610 3.0544 2.9054 0.8561  -0.4065 -0.1067 461 THR C CB  
7793  O OG1 . THR C 429 ? 4.0442 3.1084 2.9043 0.8751  -0.3933 -0.1089 461 THR C OG1 
7794  C CG2 . THR C 429 ? 3.8701 2.8894 2.7640 0.8381  -0.4058 -0.1051 461 THR C CG2 
7795  N N   . ASN C 430 ? 4.1841 3.1682 3.0734 0.8325  -0.4211 -0.1283 462 ASN C N   
7796  C CA  . ASN C 430 ? 3.9549 2.9817 2.9005 0.8196  -0.4199 -0.1350 462 ASN C CA  
7797  C C   . ASN C 430 ? 3.9282 3.0207 2.8938 0.8343  -0.4094 -0.1393 462 ASN C C   
7798  O O   . ASN C 430 ? 3.7930 2.9503 2.8173 0.8269  -0.4015 -0.1416 462 ASN C O   
7799  C CB  . ASN C 430 ? 3.9588 2.9247 2.8879 0.8051  -0.4344 -0.1386 462 ASN C CB  
7800  C CG  . ASN C 430 ? 3.8790 2.8864 2.8684 0.7900  -0.4334 -0.1445 462 ASN C CG  
7801  O OD1 . ASN C 430 ? 3.7584 2.7740 2.7885 0.7719  -0.4338 -0.1440 462 ASN C OD1 
7802  N ND2 . ASN C 430 ? 3.9148 2.9479 2.9096 0.7978  -0.4318 -0.1499 462 ASN C ND2 
7803  N N   . SER C 431 ? 4.1042 3.1801 3.0216 0.8547  -0.4091 -0.1402 463 SER C N   
7804  C CA  . SER C 431 ? 4.0671 3.2005 2.9984 0.8691  -0.3997 -0.1438 463 SER C CA  
7805  C C   . SER C 431 ? 3.9823 3.1856 2.9385 0.8795  -0.3848 -0.1397 463 SER C C   
7806  O O   . SER C 431 ? 3.9747 3.2273 2.9402 0.8918  -0.3759 -0.1412 463 SER C O   
7807  C CB  . SER C 431 ? 4.1685 3.2584 3.0370 0.8893  -0.4046 -0.1471 463 SER C CB  
7808  O OG  . SER C 431 ? 4.1583 3.1871 3.0046 0.8794  -0.4192 -0.1518 463 SER C OG  
7809  N N   . THR C 432 ? 3.7268 2.9359 2.6934 0.8746  -0.3821 -0.1343 464 THR C N   
7810  C CA  . THR C 432 ? 3.5758 2.8502 2.5647 0.8838  -0.3691 -0.1303 464 THR C CA  
7811  C C   . THR C 432 ? 3.4536 2.7856 2.5121 0.8654  -0.3645 -0.1314 464 THR C C   
7812  O O   . THR C 432 ? 3.3800 2.7658 2.4774 0.8623  -0.3584 -0.1341 464 THR C O   
7813  C CB  . THR C 432 ? 3.6507 2.8972 2.6021 0.8934  -0.3687 -0.1234 464 THR C CB  
7814  O OG1 . THR C 432 ? 3.6223 2.8445 2.5903 0.8753  -0.3748 -0.1212 464 THR C OG1 
7815  C CG2 . THR C 432 ? 3.7429 2.9197 2.6236 0.9089  -0.3751 -0.1226 464 THR C CG2 
7816  N N   . THR C 433 ? 3.4930 2.8137 2.5675 0.8533  -0.3673 -0.1294 465 THR C N   
7817  C CA  . THR C 433 ? 3.3411 2.7133 2.4796 0.8375  -0.3629 -0.1318 465 THR C CA  
7818  C C   . THR C 433 ? 3.3572 2.6879 2.5131 0.8175  -0.3720 -0.1350 465 THR C C   
7819  O O   . THR C 433 ? 3.4737 2.7355 2.5890 0.8155  -0.3818 -0.1330 465 THR C O   
7820  C CB  . THR C 433 ? 3.2529 2.6647 2.4024 0.8432  -0.3558 -0.1277 465 THR C CB  
7821  O OG1 . THR C 433 ? 3.1222 2.5777 2.3327 0.8276  -0.3527 -0.1319 465 THR C OG1 
7822  C CG2 . THR C 433 ? 3.3003 2.6564 2.4058 0.8475  -0.3616 -0.1223 465 THR C CG2 
7823  N N   . GLU C 434 ? 3.2848 2.6575 2.5015 0.8023  -0.3685 -0.1397 466 GLU C N   
7824  C CA  . GLU C 434 ? 3.1994 2.5437 2.4421 0.7831  -0.3748 -0.1437 466 GLU C CA  
7825  C C   . GLU C 434 ? 3.0193 2.4082 2.3140 0.7747  -0.3681 -0.1469 466 GLU C C   
7826  O O   . GLU C 434 ? 2.9550 2.4087 2.2864 0.7766  -0.3589 -0.1487 466 GLU C O   
7827  C CB  . GLU C 434 ? 3.1395 2.4846 2.4053 0.7725  -0.3777 -0.1483 466 GLU C CB  
7828  C CG  . GLU C 434 ? 3.2272 2.5229 2.4390 0.7813  -0.3858 -0.1471 466 GLU C CG  
7829  C CD  . GLU C 434 ? 3.3981 2.6105 2.5629 0.7767  -0.3987 -0.1450 466 GLU C CD  
7830  O OE1 . GLU C 434 ? 3.3798 2.5720 2.5595 0.7636  -0.4020 -0.1447 466 GLU C OE1 
7831  O OE2 . GLU C 434 ? 3.5286 2.6939 2.6397 0.7863  -0.4058 -0.1438 466 GLU C OE2 
7832  N N   . THR C 435 ? 3.0089 2.3614 2.3055 0.7651  -0.3731 -0.1482 467 THR C N   
7833  C CA  . THR C 435 ? 2.8986 2.2881 2.2417 0.7535  -0.3653 -0.1535 467 THR C CA  
7834  C C   . THR C 435 ? 2.7910 2.1854 2.1831 0.7219  -0.3615 -0.1610 467 THR C C   
7835  O O   . THR C 435 ? 2.8118 2.1553 2.1862 0.7084  -0.3689 -0.1598 467 THR C O   
7836  C CB  . THR C 435 ? 2.9615 2.3323 2.2769 0.7390  -0.3603 -0.1491 467 THR C CB  
7837  O OG1 . THR C 435 ? 3.0973 2.4646 2.3660 0.7700  -0.3636 -0.1411 467 THR C OG1 
7838  C CG2 . THR C 435 ? 2.8612 2.2869 2.2284 0.7101  -0.3443 -0.1559 467 THR C CG2 
7839  N N   . PHE C 436 ? 2.7326 2.1881 2.1849 0.7100  -0.3503 -0.1683 468 PHE C N   
7840  C CA  . PHE C 436 ? 2.6164 2.0859 2.1203 0.6827  -0.3448 -0.1754 468 PHE C CA  
7841  C C   . PHE C 436 ? 2.5725 2.0790 2.1149 0.6536  -0.3292 -0.1813 468 PHE C C   
7842  O O   . PHE C 436 ? 2.5665 2.1155 2.1220 0.6579  -0.3208 -0.1837 468 PHE C O   
7843  C CB  . PHE C 436 ? 2.5098 2.0171 2.0527 0.6964  -0.3457 -0.1790 468 PHE C CB  
7844  C CG  . PHE C 436 ? 2.6032 2.0857 2.1143 0.7130  -0.3562 -0.1733 468 PHE C CG  
7845  C CD1 . PHE C 436 ? 2.6941 2.1115 2.1601 0.7128  -0.3677 -0.1698 468 PHE C CD1 
7846  C CD2 . PHE C 436 ? 2.6300 2.1603 2.1555 0.7172  -0.3503 -0.1708 468 PHE C CD2 
7847  C CE1 . PHE C 436 ? 2.7967 2.1987 2.2341 0.7177  -0.3727 -0.1658 468 PHE C CE1 
7848  C CE2 . PHE C 436 ? 2.7081 2.2244 2.2056 0.7223  -0.3547 -0.1661 468 PHE C CE2 
7849  C CZ  . PHE C 436 ? 2.8128 2.2655 2.2663 0.7233  -0.3657 -0.1645 468 PHE C CZ  
7850  N N   . ARG C 437 ? 2.6013 2.0928 2.1605 0.6243  -0.3257 -0.1835 469 ARG C N   
7851  C CA  . ARG C 437 ? 2.5162 2.0386 2.1098 0.5961  -0.3112 -0.1891 469 ARG C CA  
7852  C C   . ARG C 437 ? 2.4312 1.9720 2.0768 0.5745  -0.3053 -0.1953 469 ARG C C   
7853  O O   . ARG C 437 ? 2.4507 1.9657 2.0954 0.5740  -0.3139 -0.1929 469 ARG C O   
7854  C CB  . ARG C 437 ? 2.5413 2.0286 2.0972 0.5800  -0.3114 -0.1831 469 ARG C CB  
7855  C CG  . ARG C 437 ? 2.6247 2.0906 2.1261 0.6014  -0.3170 -0.1757 469 ARG C CG  
7856  C CD  . ARG C 437 ? 2.7017 2.1255 2.1630 0.5855  -0.3191 -0.1679 469 ARG C CD  
7857  N NE  . ARG C 437 ? 2.8654 2.2619 2.2702 0.6092  -0.3259 -0.1595 469 ARG C NE  
7858  C CZ  . ARG C 437 ? 2.9282 2.3512 2.3243 0.6133  -0.3181 -0.1583 469 ARG C CZ  
7859  N NH1 . ARG C 437 ? 2.8097 2.2852 2.2489 0.5945  -0.3036 -0.1661 469 ARG C NH1 
7860  N NH2 . ARG C 437 ? 3.0581 2.4553 2.4013 0.6369  -0.3248 -0.1494 469 ARG C NH2 
7861  N N   . PRO C 438 ? 2.3318 1.9173 2.0225 0.5574  -0.2906 -0.2032 470 PRO C N   
7862  C CA  . PRO C 438 ? 2.2629 1.8674 2.0030 0.5380  -0.2838 -0.2086 470 PRO C CA  
7863  C C   . PRO C 438 ? 2.2739 1.8489 2.0039 0.5133  -0.2850 -0.2040 470 PRO C C   
7864  O O   . PRO C 438 ? 2.3057 1.8654 2.0088 0.5014  -0.2833 -0.2002 470 PRO C O   
7865  C CB  . PRO C 438 ? 2.1962 1.8521 1.9777 0.5290  -0.2678 -0.2185 470 PRO C CB  
7866  C CG  . PRO C 438 ? 2.2344 1.8893 1.9822 0.5315  -0.2655 -0.2171 470 PRO C CG  
7867  C CD  . PRO C 438 ? 2.3114 1.9335 2.0098 0.5566  -0.2797 -0.2082 470 PRO C CD  
7868  N N   . GLY C 439 ? 2.3033 1.8727 2.0555 0.5050  -0.2882 -0.2034 471 GLY C N   
7869  C CA  . GLY C 439 ? 2.3289 1.8750 2.0746 0.4797  -0.2900 -0.1981 471 GLY C CA  
7870  C C   . GLY C 439 ? 2.2618 1.8416 2.0619 0.4624  -0.2808 -0.2024 471 GLY C C   
7871  O O   . GLY C 439 ? 2.1720 1.7951 2.0158 0.4669  -0.2697 -0.2108 471 GLY C O   
7872  N N   . GLY C 440 ? 2.2749 1.8356 2.0723 0.4424  -0.2853 -0.1963 472 GLY C N   
7873  C CA  . GLY C 440 ? 2.1289 1.7237 1.9768 0.4269  -0.2764 -0.1990 472 GLY C CA  
7874  C C   . GLY C 440 ? 2.1889 1.7707 2.0298 0.3982  -0.2780 -0.1908 472 GLY C C   
7875  O O   . GLY C 440 ? 2.2537 1.7934 2.0618 0.3923  -0.2924 -0.1827 472 GLY C O   
7876  N N   . GLY C 441 ? 2.3030 1.9215 2.1739 0.3799  -0.2635 -0.1928 473 GLY C N   
7877  C CA  . GLY C 441 ? 2.2957 1.9116 2.1642 0.3512  -0.2636 -0.1840 473 GLY C CA  
7878  C C   . GLY C 441 ? 2.2381 1.8679 2.1385 0.3416  -0.2651 -0.1813 473 GLY C C   
7879  O O   . GLY C 441 ? 2.2124 1.8871 2.1571 0.3316  -0.2518 -0.1837 473 GLY C O   
7880  N N   . ASP C 442 ? 2.3540 1.9458 2.2307 0.3457  -0.2813 -0.1762 474 ASP C N   
7881  C CA  . ASP C 442 ? 2.2501 1.8525 2.1529 0.3371  -0.2848 -0.1730 474 ASP C CA  
7882  C C   . ASP C 442 ? 2.1229 1.7671 2.0770 0.3557  -0.2751 -0.1820 474 ASP C C   
7883  O O   . ASP C 442 ? 2.0944 1.7292 2.0445 0.3805  -0.2798 -0.1873 474 ASP C O   
7884  C CB  . ASP C 442 ? 2.2914 1.8390 2.1513 0.3391  -0.3055 -0.1668 474 ASP C CB  
7885  C CG  . ASP C 442 ? 2.2479 1.8017 2.1248 0.3204  -0.3109 -0.1604 474 ASP C CG  
7886  O OD1 . ASP C 442 ? 2.1880 1.7791 2.0955 0.2982  -0.3007 -0.1564 474 ASP C OD1 
7887  O OD2 . ASP C 442 ? 2.3427 1.8671 2.2028 0.3287  -0.3251 -0.1593 474 ASP C OD2 
7888  N N   . MET C 443 ? 2.2470 1.9384 2.2489 0.3441  -0.2614 -0.1830 475 MET C N   
7889  C CA  . MET C 443 ? 2.1156 1.8466 2.1678 0.3601  -0.2510 -0.1908 475 MET C CA  
7890  C C   . MET C 443 ? 2.0917 1.8154 2.1530 0.3669  -0.2617 -0.1873 475 MET C C   
7891  O O   . MET C 443 ? 2.0335 1.7846 2.1329 0.3825  -0.2559 -0.1923 475 MET C O   
7892  C CB  . MET C 443 ? 2.0374 1.8188 2.1349 0.3473  -0.2328 -0.1925 475 MET C CB  
7893  C CG  . MET C 443 ? 2.1662 1.9573 2.2538 0.3378  -0.2224 -0.1952 475 MET C CG  
7894  S SD  . MET C 443 ? 2.3141 2.0986 2.3894 0.3607  -0.2183 -0.2074 475 MET C SD  
7895  C CE  . MET C 443 ? 2.1901 1.9886 2.2532 0.3439  -0.2066 -0.2084 475 MET C CE  
7896  N N   . ARG C 444 ? 2.1340 1.8203 2.1597 0.3550  -0.2774 -0.1787 476 ARG C N   
7897  C CA  . ARG C 444 ? 2.0948 1.7706 2.1233 0.3605  -0.2892 -0.1755 476 ARG C CA  
7898  C C   . ARG C 444 ? 2.1231 1.7814 2.1399 0.3910  -0.2966 -0.1814 476 ARG C C   
7899  O O   . ARG C 444 ? 2.1225 1.7909 2.1594 0.4032  -0.3007 -0.1818 476 ARG C O   
7900  C CB  . ARG C 444 ? 2.1929 1.8272 2.1789 0.3384  -0.3050 -0.1658 476 ARG C CB  
7901  C CG  . ARG C 444 ? 2.1920 1.8579 2.2056 0.3107  -0.2998 -0.1580 476 ARG C CG  
7902  C CD  . ARG C 444 ? 2.3625 1.9902 2.3341 0.2834  -0.3145 -0.1474 476 ARG C CD  
7903  N NE  . ARG C 444 ? 2.4071 2.0586 2.3858 0.2599  -0.3035 -0.1422 476 ARG C NE  
7904  C CZ  . ARG C 444 ? 2.4982 2.1275 2.4451 0.2312  -0.3114 -0.1316 476 ARG C CZ  
7905  N NH1 . ARG C 444 ? 2.5757 2.1520 2.4777 0.2204  -0.3314 -0.1254 476 ARG C NH1 
7906  N NH2 . ARG C 444 ? 2.5518 2.2119 2.5109 0.2131  -0.2992 -0.1271 476 ARG C NH2 
7907  N N   . ASP C 445 ? 2.1279 1.7640 2.1135 0.4037  -0.2979 -0.1853 477 ASP C N   
7908  C CA  . ASP C 445 ? 2.1533 1.7789 2.1278 0.4335  -0.3040 -0.1900 477 ASP C CA  
7909  C C   . ASP C 445 ? 2.0374 1.7127 2.0661 0.4478  -0.2907 -0.1965 477 ASP C C   
7910  O O   . ASP C 445 ? 2.0089 1.6889 2.0460 0.4692  -0.2957 -0.1980 477 ASP C O   
7911  C CB  . ASP C 445 ? 2.2842 1.8790 2.2128 0.4427  -0.3075 -0.1914 477 ASP C CB  
7912  C CG  . ASP C 445 ? 2.4162 1.9570 2.2885 0.4286  -0.3209 -0.1842 477 ASP C CG  
7913  O OD1 . ASP C 445 ? 2.4240 1.9363 2.2780 0.4233  -0.3342 -0.1794 477 ASP C OD1 
7914  O OD2 . ASP C 445 ? 2.4876 2.0141 2.3334 0.4219  -0.3183 -0.1832 477 ASP C OD2 
7915  N N   . ASN C 446 ? 2.0409 1.7527 2.1052 0.4362  -0.2739 -0.2002 478 ASN C N   
7916  C CA  . ASN C 446 ? 1.9796 1.7348 2.0938 0.4477  -0.2605 -0.2069 478 ASN C CA  
7917  C C   . ASN C 446 ? 1.9060 1.6835 2.0584 0.4520  -0.2609 -0.2042 478 ASN C C   
7918  O O   . ASN C 446 ? 1.8907 1.6921 2.0741 0.4687  -0.2565 -0.2078 478 ASN C O   
7919  C CB  . ASN C 446 ? 1.9672 1.7526 2.1080 0.4324  -0.2430 -0.2113 478 ASN C CB  
7920  C CG  . ASN C 446 ? 2.0172 1.7877 2.1252 0.4279  -0.2406 -0.2144 478 ASN C CG  
7921  O OD1 . ASN C 446 ? 2.0856 1.8185 2.1466 0.4308  -0.2527 -0.2109 478 ASN C OD1 
7922  N ND2 . ASN C 446 ? 1.9820 1.7814 2.1134 0.4208  -0.2248 -0.2208 478 ASN C ND2 
7923  N N   . TRP C 447 ? 1.9354 1.7066 2.0860 0.4365  -0.2666 -0.1971 479 TRP C N   
7924  C CA  . TRP C 447 ? 1.8853 1.6794 2.0712 0.4398  -0.2674 -0.1935 479 TRP C CA  
7925  C C   . TRP C 447 ? 1.9263 1.6957 2.0896 0.4577  -0.2839 -0.1912 479 TRP C C   
7926  O O   . TRP C 447 ? 1.9196 1.7111 2.1136 0.4698  -0.2843 -0.1900 479 TRP C O   
7927  C CB  . TRP C 447 ? 1.8765 1.6789 2.0703 0.4146  -0.2666 -0.1863 479 TRP C CB  
7928  C CG  . TRP C 447 ? 1.8796 1.6943 2.0757 0.3952  -0.2545 -0.1868 479 TRP C CG  
7929  C CD1 . TRP C 447 ? 1.9363 1.7302 2.1004 0.3722  -0.2596 -0.1809 479 TRP C CD1 
7930  C CD2 . TRP C 447 ? 1.8254 1.6752 2.0554 0.3972  -0.2359 -0.1936 479 TRP C CD2 
7931  N NE1 . TRP C 447 ? 1.8881 1.7060 2.0657 0.3604  -0.2449 -0.1829 479 TRP C NE1 
7932  C CE2 . TRP C 447 ? 1.8284 1.6799 2.0456 0.3761  -0.2301 -0.1914 479 TRP C CE2 
7933  C CE3 . TRP C 447 ? 1.7820 1.6608 2.0508 0.4144  -0.2239 -0.2012 479 TRP C CE3 
7934  C CZ2 . TRP C 447 ? 1.7874 1.6695 2.0287 0.3735  -0.2125 -0.1975 479 TRP C CZ2 
7935  C CZ3 . TRP C 447 ? 1.7369 1.6416 2.0280 0.4109  -0.2070 -0.2077 479 TRP C CZ3 
7936  C CH2 . TRP C 447 ? 1.7460 1.6528 2.0232 0.3914  -0.2012 -0.2063 479 TRP C CH2 
7937  N N   . ARG C 448 ? 1.8652 1.5887 1.9739 0.4604  -0.2976 -0.1903 480 ARG C N   
7938  C CA  . ARG C 448 ? 1.9788 1.6725 2.0563 0.4787  -0.3144 -0.1886 480 ARG C CA  
7939  C C   . ARG C 448 ? 1.9812 1.6930 2.0730 0.5072  -0.3129 -0.1925 480 ARG C C   
7940  O O   . ARG C 448 ? 2.0267 1.7309 2.1093 0.5255  -0.3240 -0.1907 480 ARG C O   
7941  C CB  . ARG C 448 ? 2.0711 1.7099 2.0846 0.4746  -0.3271 -0.1872 480 ARG C CB  
7942  C CG  . ARG C 448 ? 2.0559 1.6747 2.0528 0.4446  -0.3311 -0.1815 480 ARG C CG  
7943  C CD  . ARG C 448 ? 2.2472 1.8053 2.1782 0.4394  -0.3458 -0.1787 480 ARG C CD  
7944  N NE  . ARG C 448 ? 2.2529 1.7976 2.1735 0.4070  -0.3490 -0.1721 480 ARG C NE  
7945  C CZ  . ARG C 448 ? 2.3733 1.8739 2.2458 0.3913  -0.3567 -0.1681 480 ARG C CZ  
7946  N NH1 . ARG C 448 ? 2.4021 1.8665 2.2316 0.4069  -0.3616 -0.1703 480 ARG C NH1 
7947  N NH2 . ARG C 448 ? 2.3945 1.8889 2.2619 0.3597  -0.3595 -0.1607 480 ARG C NH2 
7948  N N   . SER C 449 ? 1.8651 1.6015 1.9781 0.5107  -0.2996 -0.1977 481 SER C N   
7949  C CA  . SER C 449 ? 1.8914 1.6482 2.0192 0.5344  -0.2976 -0.2007 481 SER C CA  
7950  C C   . SER C 449 ? 1.8171 1.6152 1.9997 0.5408  -0.2911 -0.1996 481 SER C C   
7951  O O   . SER C 449 ? 1.8129 1.6333 2.0058 0.5490  -0.2860 -0.1968 481 SER C O   
7952  C CB  . SER C 449 ? 1.9332 1.7011 2.0634 0.5326  -0.2861 -0.2068 481 SER C CB  
7953  O OG  . SER C 449 ? 1.8838 1.6803 2.0544 0.5153  -0.2702 -0.2102 481 SER C OG  
7954  N N   . GLU C 450 ? 1.8744 1.6887 2.0873 0.5252  -0.2856 -0.1970 482 GLU C N   
7955  C CA  . GLU C 450 ? 1.8241 1.6773 2.0897 0.5303  -0.2787 -0.1949 482 GLU C CA  
7956  C C   . GLU C 450 ? 1.7921 1.6443 2.0617 0.5268  -0.2876 -0.1881 482 GLU C C   
7957  O O   . GLU C 450 ? 1.6891 1.5704 1.9909 0.5320  -0.2838 -0.1830 482 GLU C O   
7958  C CB  . GLU C 450 ? 1.7519 1.6363 2.0601 0.5169  -0.2599 -0.1985 482 GLU C CB  
7959  C CG  . GLU C 450 ? 1.7970 1.6847 2.1036 0.5204  -0.2509 -0.2063 482 GLU C CG  
7960  C CD  . GLU C 450 ? 1.8811 1.7843 2.1940 0.5312  -0.2481 -0.2033 482 GLU C CD  
7961  O OE1 . GLU C 450 ? 1.8884 1.8133 2.2211 0.5267  -0.2429 -0.1930 482 GLU C OE1 
7962  O OE2 . GLU C 450 ? 1.9300 1.8260 2.2213 0.5348  -0.2474 -0.2069 482 GLU C OE2 
7963  N N   . LEU C 451 ? 1.8498 1.6708 2.0837 0.5116  -0.2966 -0.1857 483 LEU C N   
7964  C CA  . LEU C 451 ? 1.7668 1.5833 1.9987 0.5044  -0.3064 -0.1796 483 LEU C CA  
7965  C C   . LEU C 451 ? 1.8089 1.5860 1.9925 0.5187  -0.3259 -0.1787 483 LEU C C   
7966  O O   . LEU C 451 ? 1.8107 1.5684 1.9747 0.5099  -0.3375 -0.1750 483 LEU C O   
7967  C CB  . LEU C 451 ? 1.7602 1.5687 1.9839 0.4750  -0.3042 -0.1768 483 LEU C CB  
7968  C CG  . LEU C 451 ? 1.7032 1.5550 1.9761 0.4613  -0.2851 -0.1765 483 LEU C CG  
7969  C CD1 . LEU C 451 ? 1.7183 1.5626 1.9772 0.4325  -0.2841 -0.1725 483 LEU C CD1 
7970  C CD2 . LEU C 451 ? 1.6286 1.5227 1.9529 0.4686  -0.2792 -0.1725 483 LEU C CD2 
7971  N N   . TYR C 452 ? 1.7909 1.5565 1.9539 0.5410  -0.3299 -0.1820 484 TYR C N   
7972  C CA  . TYR C 452 ? 1.8401 1.5696 1.9535 0.5567  -0.3465 -0.1810 484 TYR C CA  
7973  C C   . TYR C 452 ? 1.8103 1.5664 1.9367 0.5555  -0.3442 -0.1734 484 TYR C C   
7974  O O   . TYR C 452 ? 1.8775 1.6056 1.9639 0.5614  -0.3572 -0.1720 484 TYR C O   
7975  C CB  . TYR C 452 ? 1.9218 1.6469 2.0059 0.5620  -0.3397 -0.1811 484 TYR C CB  
7976  C CG  . TYR C 452 ? 1.8994 1.6756 2.0153 0.5587  -0.3205 -0.1754 484 TYR C CG  
7977  C CD1 . TYR C 452 ? 1.8623 1.6704 2.0197 0.5525  -0.3051 -0.1776 484 TYR C CD1 
7978  C CD2 . TYR C 452 ? 1.9229 1.7127 2.0259 0.5617  -0.3186 -0.1679 484 TYR C CD2 
7979  C CE1 . TYR C 452 ? 1.8112 1.6590 1.9947 0.5485  -0.2897 -0.1717 484 TYR C CE1 
7980  C CE2 . TYR C 452 ? 1.8683 1.7010 1.9997 0.5578  -0.3028 -0.1613 484 TYR C CE2 
7981  C CZ  . TYR C 452 ? 1.8270 1.6864 1.9977 0.5509  -0.2891 -0.1629 484 TYR C CZ  
7982  O OH  . TYR C 452 ? 1.7793 1.6754 1.9754 0.5465  -0.2755 -0.1559 484 TYR C OH  
7983  N N   . LYS C 453 ? 1.7603 1.5676 1.9395 0.5483  -0.3277 -0.1684 485 LYS C N   
7984  C CA  . LYS C 453 ? 1.6988 1.5349 1.8936 0.5464  -0.3232 -0.1597 485 LYS C CA  
7985  C C   . LYS C 453 ? 1.6369 1.4882 1.8660 0.5418  -0.3275 -0.1583 485 LYS C C   
7986  O O   . LYS C 453 ? 1.6379 1.5227 1.8925 0.5384  -0.3196 -0.1502 485 LYS C O   
7987  C CB  . LYS C 453 ? 1.6873 1.5686 1.9142 0.5411  -0.3018 -0.1518 485 LYS C CB  
7988  C CG  . LYS C 453 ? 1.6429 1.5520 1.9167 0.5334  -0.2865 -0.1531 485 LYS C CG  
7989  C CD  . LYS C 453 ? 1.5575 1.5060 1.8619 0.5275  -0.2674 -0.1435 485 LYS C CD  
7990  C CE  . LYS C 453 ? 1.5723 1.5179 1.8507 0.5311  -0.2652 -0.1415 485 LYS C CE  
7991  N NZ  . LYS C 453 ? 1.5454 1.5274 1.8559 0.5247  -0.2488 -0.1314 485 LYS C NZ  
7992  N N   . TYR C 454 ? 1.7238 1.5525 1.9548 0.5417  -0.3405 -0.1650 486 TYR C N   
7993  C CA  . TYR C 454 ? 1.6742 1.5239 1.9380 0.5316  -0.3426 -0.1616 486 TYR C CA  
7994  C C   . TYR C 454 ? 1.7249 1.5351 1.9449 0.5103  -0.3556 -0.1606 486 TYR C C   
7995  O O   . TYR C 454 ? 1.7790 1.5475 1.9551 0.5007  -0.3603 -0.1638 486 TYR C O   
7996  C CB  . TYR C 454 ? 1.6507 1.5387 1.9632 0.5158  -0.3226 -0.1604 486 TYR C CB  
7997  C CG  . TYR C 454 ? 1.6350 1.5626 1.9900 0.5260  -0.3047 -0.1593 486 TYR C CG  
7998  C CD1 . TYR C 454 ? 1.6206 1.5863 2.0038 0.5216  -0.2921 -0.1485 486 TYR C CD1 
7999  C CD2 . TYR C 454 ? 1.6730 1.5999 2.0296 0.5252  -0.2930 -0.1645 486 TYR C CD2 
8000  C CE1 . TYR C 454 ? 1.6141 1.6111 2.0237 0.5164  -0.2696 -0.1419 486 TYR C CE1 
8001  C CE2 . TYR C 454 ? 1.6503 1.6101 2.0341 0.5201  -0.2712 -0.1593 486 TYR C CE2 
8002  C CZ  . TYR C 454 ? 1.5976 1.5901 2.0068 0.5156  -0.2601 -0.1476 486 TYR C CZ  
8003  O OH  . TYR C 454 ? 1.6728 1.6915 2.1059 0.5106  -0.2404 -0.1412 486 TYR C OH  
8004  N N   . LYS C 455 ? 1.8071 1.6309 2.0392 0.5021  -0.3616 -0.1556 487 LYS C N   
8005  C CA  . LYS C 455 ? 1.8968 1.6895 2.0938 0.4773  -0.3736 -0.1534 487 LYS C CA  
8006  C C   . LYS C 455 ? 1.8303 1.6650 2.0672 0.4644  -0.3713 -0.1462 487 LYS C C   
8007  O O   . LYS C 455 ? 1.7030 1.5775 1.9798 0.4814  -0.3669 -0.1435 487 LYS C O   
8008  C CB  . LYS C 455 ? 1.9723 1.7070 2.1053 0.4878  -0.3950 -0.1574 487 LYS C CB  
8009  C CG  . LYS C 455 ? 1.9078 1.6470 2.0387 0.5014  -0.4078 -0.1562 487 LYS C CG  
8010  C CD  . LYS C 455 ? 2.0211 1.6935 2.0801 0.5058  -0.4292 -0.1610 487 LYS C CD  
8011  C CE  . LYS C 455 ? 1.9990 1.6700 2.0486 0.5134  -0.4438 -0.1605 487 LYS C CE  
8012  N NZ  . LYS C 455 ? 2.1369 1.7363 2.1117 0.5160  -0.4650 -0.1662 487 LYS C NZ  
8013  N N   . VAL C 456 ? 1.8856 1.7127 2.1110 0.4336  -0.3742 -0.1420 488 VAL C N   
8014  C CA  . VAL C 456 ? 1.7617 1.6315 2.0233 0.4159  -0.3710 -0.1338 488 VAL C CA  
8015  C C   . VAL C 456 ? 1.7616 1.6068 1.9902 0.4101  -0.3914 -0.1325 488 VAL C C   
8016  O O   . VAL C 456 ? 1.8675 1.6551 2.0375 0.3999  -0.4075 -0.1359 488 VAL C O   
8017  C CB  . VAL C 456 ? 1.8048 1.6892 2.0767 0.3842  -0.3612 -0.1285 488 VAL C CB  
8018  C CG1 . VAL C 456 ? 1.7429 1.6778 2.0540 0.3674  -0.3571 -0.1188 488 VAL C CG1 
8019  C CG2 . VAL C 456 ? 1.7933 1.6992 2.0941 0.3912  -0.3413 -0.1313 488 VAL C CG2 
8020  N N   . VAL C 457 ? 1.6443 1.5312 1.9086 0.4174  -0.3911 -0.1278 489 VAL C N   
8021  C CA  . VAL C 457 ? 1.6767 1.5482 1.9151 0.4107  -0.4096 -0.1264 489 VAL C CA  
8022  C C   . VAL C 457 ? 1.6467 1.5757 1.9310 0.3919  -0.4031 -0.1162 489 VAL C C   
8023  O O   . VAL C 457 ? 1.5907 1.5760 1.9327 0.3969  -0.3843 -0.1108 489 VAL C O   
8024  C CB  . VAL C 457 ? 1.6678 1.5314 1.8969 0.4446  -0.4193 -0.1313 489 VAL C CB  
8025  C CG1 . VAL C 457 ? 1.7096 1.5149 1.8864 0.4627  -0.4279 -0.1405 489 VAL C CG1 
8026  C CG2 . VAL C 457 ? 1.5932 1.5195 1.8869 0.4678  -0.4033 -0.1271 489 VAL C CG2 
8027  N N   . LYS C 458 ? 1.7000 1.6141 1.9571 0.3701  -0.4189 -0.1135 490 LYS C N   
8028  C CA  . LYS C 458 ? 1.6972 1.6660 1.9928 0.3510  -0.4152 -0.1030 490 LYS C CA  
8029  C C   . LYS C 458 ? 1.7137 1.6942 2.0118 0.3668  -0.4269 -0.1033 490 LYS C C   
8030  O O   . LYS C 458 ? 1.7491 1.6785 1.9968 0.3756  -0.4455 -0.1111 490 LYS C O   
8031  C CB  . LYS C 458 ? 1.8070 1.7603 2.0746 0.3091  -0.4241 -0.0976 490 LYS C CB  
8032  C CG  . LYS C 458 ? 1.9046 1.7867 2.1005 0.2956  -0.4496 -0.1036 490 LYS C CG  
8033  C CD  . LYS C 458 ? 2.0017 1.8782 2.1782 0.2506  -0.4568 -0.0956 490 LYS C CD  
8034  C CE  . LYS C 458 ? 2.1464 1.9461 2.2484 0.2344  -0.4830 -0.1015 490 LYS C CE  
8035  N NZ  . LYS C 458 ? 2.1314 1.8898 2.1952 0.2022  -0.4873 -0.0988 490 LYS C NZ  
8036  N N   . ILE C 459 ? 1.5156 1.5634 1.8702 0.3698  -0.4163 -0.0943 491 ILE C N   
8037  C CA  . ILE C 459 ? 1.5023 1.5738 1.8691 0.3856  -0.4247 -0.0926 491 ILE C CA  
8038  C C   . ILE C 459 ? 1.5354 1.6095 1.8835 0.3555  -0.4393 -0.0878 491 ILE C C   
8039  O O   . ILE C 459 ? 1.5302 1.6395 1.9009 0.3274  -0.4322 -0.0782 491 ILE C O   
8040  C CB  . ILE C 459 ? 1.4352 1.5788 1.8741 0.4067  -0.4053 -0.0845 491 ILE C CB  
8041  C CG1 . ILE C 459 ? 1.4063 1.5443 1.8609 0.4350  -0.3925 -0.0896 491 ILE C CG1 
8042  C CG2 . ILE C 459 ? 1.4216 1.5931 1.8737 0.4219  -0.4141 -0.0815 491 ILE C CG2 
8043  C CD1 . ILE C 459 ? 1.4261 1.5173 1.8397 0.4607  -0.4062 -0.0996 491 ILE C CD1 
8044  N N   . GLU C 460 ? 1.6634 1.7013 1.9688 0.3614  -0.4601 -0.0944 492 GLU C N   
8045  C CA  . GLU C 460 ? 1.6845 1.7221 1.9685 0.3345  -0.4764 -0.0912 492 GLU C CA  
8046  C C   . GLU C 460 ? 1.6140 1.6938 1.9265 0.3587  -0.4787 -0.0893 492 GLU C C   
8047  O O   . GLU C 460 ? 1.6470 1.6909 1.9223 0.3777  -0.4947 -0.0983 492 GLU C O   
8048  C CB  . GLU C 460 ? 1.7734 1.7261 1.9767 0.3198  -0.5006 -0.1016 492 GLU C CB  
8049  C CG  . GLU C 460 ? 1.9138 1.8178 2.0822 0.2961  -0.5006 -0.1033 492 GLU C CG  
8050  C CD  . GLU C 460 ? 1.9936 1.8098 2.0800 0.2832  -0.5256 -0.1131 492 GLU C CD  
8051  O OE1 . GLU C 460 ? 2.0815 1.8736 2.1376 0.2956  -0.5424 -0.1201 492 GLU C OE1 
8052  O OE2 . GLU C 460 ? 1.9754 1.7465 2.0269 0.2611  -0.5285 -0.1138 492 GLU C OE2 
8053  N N   . PRO C 461 ? 1.5158 1.6738 1.8944 0.3598  -0.4625 -0.0771 493 PRO C N   
8054  C CA  . PRO C 461 ? 1.4777 1.6839 1.8923 0.3857  -0.4614 -0.0732 493 PRO C CA  
8055  C C   . PRO C 461 ? 1.5099 1.7145 1.8981 0.3733  -0.4814 -0.0738 493 PRO C C   
8056  O O   . PRO C 461 ? 1.4828 1.7256 1.8959 0.3945  -0.4825 -0.0710 493 PRO C O   
8057  C CB  . PRO C 461 ? 1.4176 1.7036 1.9068 0.3847  -0.4378 -0.0587 493 PRO C CB  
8058  C CG  . PRO C 461 ? 1.4390 1.7255 1.9220 0.3463  -0.4346 -0.0534 493 PRO C CG  
8059  C CD  . PRO C 461 ? 1.4890 1.6959 1.9113 0.3371  -0.4446 -0.0653 493 PRO C CD  
8060  N N   . LEU C 462 ? 1.6994 1.8635 2.0395 0.3384  -0.4970 -0.0766 494 LEU C N   
8061  C CA  . LEU C 462 ? 1.7843 1.9411 2.0933 0.3214  -0.5177 -0.0781 494 LEU C CA  
8062  C C   . LEU C 462 ? 1.8538 1.9338 2.0940 0.3379  -0.5398 -0.0942 494 LEU C C   
8063  O O   . LEU C 462 ? 1.9465 1.9524 2.1290 0.3271  -0.5506 -0.1035 494 LEU C O   
8064  C CB  . LEU C 462 ? 1.8714 2.0237 2.1627 0.2728  -0.5239 -0.0719 494 LEU C CB  
8065  C CG  . LEU C 462 ? 1.8388 2.0824 2.1977 0.2575  -0.5069 -0.0543 494 LEU C CG  
8066  C CD1 . LEU C 462 ? 1.9032 2.1477 2.2446 0.2083  -0.5134 -0.0466 494 LEU C CD1 
8067  C CD2 . LEU C 462 ? 1.7434 2.0454 2.1370 0.2743  -0.5080 -0.0491 494 LEU C CD2 
8068  N N   . GLY C 463 ? 2.0605 2.1595 2.3069 0.3658  -0.5460 -0.0971 495 GLY C N   
8069  C CA  . GLY C 463 ? 2.1299 2.1650 2.3139 0.3861  -0.5666 -0.1120 495 GLY C CA  
8070  C C   . GLY C 463 ? 2.2125 2.2742 2.3936 0.3856  -0.5807 -0.1119 495 GLY C C   
8071  O O   . GLY C 463 ? 2.0992 2.2368 2.3388 0.3985  -0.5698 -0.1018 495 GLY C O   
8072  N N   . VAL C 464 ? 2.3763 2.3744 2.4879 0.3703  -0.6051 -0.1232 496 VAL C N   
8073  C CA  . VAL C 464 ? 2.3329 2.3445 2.4292 0.3669  -0.6219 -0.1258 496 VAL C CA  
8074  C C   . VAL C 464 ? 2.3653 2.3416 2.4241 0.4093  -0.6342 -0.1393 496 VAL C C   
8075  O O   . VAL C 464 ? 2.3864 2.2949 2.3980 0.4276  -0.6396 -0.1504 496 VAL C O   
8076  C CB  . VAL C 464 ? 2.4154 2.3777 2.4558 0.3203  -0.6425 -0.1300 496 VAL C CB  
8077  C CG1 . VAL C 464 ? 2.4980 2.4930 2.5366 0.3094  -0.6568 -0.1294 496 VAL C CG1 
8078  C CG2 . VAL C 464 ? 2.4462 2.4283 2.5125 0.2798  -0.6306 -0.1176 496 VAL C CG2 
8079  N N   . ALA C 465 ? 2.3877 2.4127 2.4672 0.4262  -0.6384 -0.1375 497 ALA C N   
8080  C CA  . ALA C 465 ? 2.4074 2.4058 2.4531 0.4683  -0.6495 -0.1493 497 ALA C CA  
8081  C C   . ALA C 465 ? 2.4008 2.4270 2.4394 0.4703  -0.6644 -0.1517 497 ALA C C   
8082  O O   . ALA C 465 ? 2.3610 2.4626 2.4538 0.4550  -0.6566 -0.1387 497 ALA C O   
8083  C CB  . ALA C 465 ? 2.3142 2.3595 2.4131 0.5104  -0.6297 -0.1426 497 ALA C CB  
8084  N N   . PRO C 466 ? 2.3485 2.3160 2.3201 0.4899  -0.6856 -0.1679 498 PRO C N   
8085  C CA  . PRO C 466 ? 2.4113 2.3993 2.3686 0.4925  -0.7016 -0.1723 498 PRO C CA  
8086  C C   . PRO C 466 ? 2.3650 2.4267 2.3715 0.5357  -0.6926 -0.1660 498 PRO C C   
8087  O O   . PRO C 466 ? 2.3345 2.3988 2.3524 0.5743  -0.6833 -0.1660 498 PRO C O   
8088  C CB  . PRO C 466 ? 2.5489 2.4331 2.4074 0.4976  -0.7279 -0.1937 498 PRO C CB  
8089  C CG  . PRO C 466 ? 2.5272 2.3625 2.3653 0.5259  -0.7210 -0.1988 498 PRO C CG  
8090  C CD  . PRO C 466 ? 2.4329 2.3053 2.3313 0.5070  -0.6973 -0.1838 498 PRO C CD  
8091  N N   . THR C 467 ? 2.3365 2.4601 2.3718 0.5278  -0.6958 -0.1597 499 THR C N   
8092  C CA  . THR C 467 ? 2.3490 2.5429 2.4261 0.5663  -0.6904 -0.1535 499 THR C CA  
8093  C C   . THR C 467 ? 2.4023 2.6319 2.4769 0.5496  -0.7039 -0.1535 499 THR C C   
8094  O O   . THR C 467 ? 2.4372 2.6600 2.5011 0.5056  -0.7110 -0.1525 499 THR C O   
8095  C CB  . THR C 467 ? 2.1898 2.4657 2.3565 0.5751  -0.6564 -0.1323 499 THR C CB  
8096  O OG1 . THR C 467 ? 2.1974 2.5265 2.3931 0.5842  -0.6260 -0.1209 499 THR C OG1 
8097  C CG2 . THR C 467 ? 2.1150 2.4443 2.3350 0.5399  -0.6497 -0.1182 499 THR C CG2 
8098  N N   . ARG C 468 ? 2.3462 2.6166 2.4315 0.5835  -0.7053 -0.1534 500 ARG C N   
8099  C CA  . ARG C 468 ? 2.3624 2.6719 2.4450 0.5772  -0.7194 -0.1544 500 ARG C CA  
8100  C C   . ARG C 468 ? 2.3907 2.8013 2.5568 0.5563  -0.6990 -0.1318 500 ARG C C   
8101  O O   . ARG C 468 ? 2.3825 2.8517 2.5810 0.5606  -0.6776 -0.1199 500 ARG C O   
8102  C CB  . ARG C 468 ? 2.3888 2.6855 2.4426 0.6058  -0.7042 -0.1603 500 ARG C CB  
8103  C CG  . ARG C 468 ? 2.3379 2.6674 2.4403 0.6182  -0.6542 -0.1434 500 ARG C CG  
8104  C CD  . ARG C 468 ? 2.3642 2.6879 2.4422 0.6415  -0.6381 -0.1472 500 ARG C CD  
8105  N NE  . ARG C 468 ? 2.3340 2.6944 2.4619 0.6420  -0.5925 -0.1271 500 ARG C NE  
8106  C CZ  . ARG C 468 ? 2.3532 2.7106 2.4682 0.6573  -0.5724 -0.1262 500 ARG C CZ  
8107  N NH1 . ARG C 468 ? 2.4277 2.7488 2.4824 0.6779  -0.5911 -0.1453 500 ARG C NH1 
8108  N NH2 . ARG C 468 ? 2.3566 2.7450 2.5167 0.6505  -0.5350 -0.1060 500 ARG C NH2 
8109  N N   . CYS C 469 ? 2.2459 2.6667 2.4406 0.5220  -0.6922 -0.1226 501 CYS C N   
8110  C CA  . CYS C 469 ? 2.1932 2.7055 2.4650 0.5008  -0.6746 -0.1010 501 CYS C CA  
8111  C C   . CYS C 469 ? 2.1434 2.6460 2.3958 0.4471  -0.6841 -0.1004 501 CYS C C   
8112  O O   . CYS C 469 ? 2.1185 2.5532 2.3299 0.4197  -0.6895 -0.1078 501 CYS C O   
8113  C CB  . CYS C 469 ? 2.1924 2.7367 2.5273 0.5055  -0.6472 -0.0856 501 CYS C CB  
8114  S SG  . CYS C 469 ? 2.6222 3.2741 3.0453 0.4780  -0.6263 -0.0595 501 CYS C SG  
8115  N N   . LYS C 470 ? 2.1305 2.7029 2.4125 0.4316  -0.6864 -0.0906 502 LYS C N   
8116  C CA  . LYS C 470 ? 2.1148 2.6922 2.3852 0.3791  -0.6949 -0.0871 502 LYS C CA  
8117  C C   . LYS C 470 ? 2.0039 2.6914 2.3615 0.3691  -0.6731 -0.0618 502 LYS C C   
8118  O O   . LYS C 470 ? 1.9665 2.7266 2.3800 0.4012  -0.6603 -0.0503 502 LYS C O   
8119  C CB  . LYS C 470 ? 2.2779 2.8229 2.4840 0.3618  -0.7239 -0.1021 502 LYS C CB  
8120  C CG  . LYS C 470 ? 2.3880 2.9273 2.5748 0.3028  -0.7342 -0.0989 502 LYS C CG  
8121  C CD  . LYS C 470 ? 2.3775 2.8930 2.5058 0.2824  -0.7625 -0.1122 502 LYS C CD  
8122  C CE  . LYS C 470 ? 2.4708 2.9891 2.5865 0.2211  -0.7713 -0.1058 502 LYS C CE  
8123  N NZ  . LYS C 470 ? 2.4939 2.9914 2.5532 0.1966  -0.7997 -0.1183 502 LYS C NZ  
8124  N N   . ARG C 471 ? 2.0105 2.7117 2.3792 0.3247  -0.6691 -0.0521 503 ARG C N   
8125  C CA  . ARG C 471 ? 2.0631 2.8678 2.5119 0.3147  -0.6480 -0.0275 503 ARG C CA  
8126  C C   . ARG C 471 ? 2.1763 3.0468 2.6360 0.3011  -0.6585 -0.0211 503 ARG C C   
8127  O O   . ARG C 471 ? 2.2835 3.1272 2.6981 0.3107  -0.6791 -0.0355 503 ARG C O   
8128  C CB  . ARG C 471 ? 2.0494 2.8474 2.5047 0.2735  -0.6397 -0.0190 503 ARG C CB  
8129  C CG  . ARG C 471 ? 1.9435 2.7407 2.4391 0.2907  -0.6146 -0.0115 503 ARG C CG  
8130  C CD  . ARG C 471 ? 1.8711 2.6882 2.3855 0.2499  -0.6044 0.0013  503 ARG C CD  
8131  N NE  . ARG C 471 ? 1.9101 2.6437 2.3508 0.2111  -0.6254 -0.0124 503 ARG C NE  
8132  C CZ  . ARG C 471 ? 1.9676 2.7059 2.4050 0.1669  -0.6248 -0.0039 503 ARG C CZ  
8133  N NH1 . ARG C 471 ? 1.9824 2.8071 2.4859 0.1570  -0.6038 0.0177  503 ARG C NH1 
8134  N NH2 . ARG C 471 ? 2.0201 2.6768 2.3869 0.1328  -0.6455 -0.0166 503 ARG C NH2 
8135  N N   . ARG C 472 ? 2.1712 3.1290 2.6894 0.2802  -0.6444 0.0004  504 ARG C N   
8136  C CA  . ARG C 472 ? 2.2524 3.2837 2.7882 0.2674  -0.6521 0.0093  504 ARG C CA  
8137  C C   . ARG C 472 ? 2.3298 3.3393 2.8179 0.2110  -0.6724 0.0054  504 ARG C C   
8138  O O   . ARG C 472 ? 2.3178 3.2420 2.7474 0.1851  -0.6852 -0.0080 504 ARG C O   
8139  C CB  . ARG C 472 ? 2.1836 3.3294 2.8117 0.2810  -0.6252 0.0364  504 ARG C CB  
8140  C CG  . ARG C 472 ? 2.0859 3.2603 2.7629 0.3353  -0.6068 0.0421  504 ARG C CG  
8141  C CD  . ARG C 472 ? 2.0589 3.2892 2.8109 0.3348  -0.5676 0.0697  504 ARG C CD  
8142  N NE  . ARG C 472 ? 2.0641 3.2892 2.8295 0.3286  -0.5632 0.0698  504 ARG C NE  
8143  C CZ  . ARG C 472 ? 2.0947 3.2671 2.8638 0.3511  -0.5463 0.0665  504 ARG C CZ  
8144  N NH1 . ARG C 472 ? 2.1065 3.2298 2.8661 0.3775  -0.5309 0.0654  504 ARG C NH1 
8145  N NH2 . ARG C 472 ? 2.1546 3.3115 2.9304 0.3395  -0.5389 0.0670  504 ARG C NH2 
8146  N N   . VAL C 473 ? 2.3396 3.4296 2.8545 0.1906  -0.6751 0.0186  505 VAL C N   
8147  C CA  . VAL C 473 ? 2.3861 3.4695 2.8611 0.1357  -0.6948 0.0174  505 VAL C CA  
8148  C C   . VAL C 473 ? 2.3464 3.5267 2.8864 0.1092  -0.6758 0.0448  505 VAL C C   
8149  O O   . VAL C 473 ? 2.2879 3.5430 2.9018 0.1378  -0.6494 0.0632  505 VAL C O   
8150  C CB  . VAL C 473 ? 2.3880 3.4778 2.8264 0.1318  -0.7192 0.0066  505 VAL C CB  
8151  C CG1 . VAL C 473 ? 2.4443 3.5817 2.8786 0.0789  -0.7306 0.0167  505 VAL C CG1 
8152  C CG2 . VAL C 473 ? 2.4303 3.4029 2.7793 0.1354  -0.7453 -0.0228 505 VAL C CG2 
8153  N N   . ALA D 1   ? 3.4605 3.4149 3.8879 1.0455  0.0267  -0.0434 6   ALA L N   
8154  C CA  . ALA D 1   ? 3.4539 3.4485 3.8715 1.0267  0.0509  -0.0566 6   ALA L CA  
8155  C C   . ALA D 1   ? 3.5301 3.5131 3.9055 0.9730  0.0585  -0.0916 6   ALA L C   
8156  O O   . ALA D 1   ? 3.4189 3.3660 3.7608 0.9338  0.0648  -0.0925 6   ALA L O   
8157  C CB  . ALA D 1   ? 3.2570 3.3640 3.7234 1.0750  0.0729  -0.0624 6   ALA L CB  
8158  N N   . PRO D 2   ? 3.5860 3.5979 3.9621 0.9702  0.0580  -0.1201 7   PRO L N   
8159  C CA  . PRO D 2   ? 3.4701 3.4713 3.8064 0.9194  0.0652  -0.1535 7   PRO L CA  
8160  C C   . PRO D 2   ? 3.4055 3.2964 3.6934 0.8717  0.0434  -0.1491 7   PRO L C   
8161  O O   . PRO D 2   ? 3.5201 3.3533 3.8088 0.8812  0.0206  -0.1292 7   PRO L O   
8162  C CB  . PRO D 2   ? 3.4032 3.4763 3.7623 0.9395  0.0711  -0.1828 7   PRO L CB  
8163  C CG  . PRO D 2   ? 3.4298 3.4999 3.8225 0.9844  0.0537  -0.1619 7   PRO L CG  
8164  C CD  . PRO D 2   ? 3.4651 3.5270 3.8795 1.0138  0.0525  -0.1250 7   PRO L CD  
8165  N N   . THR D 3   ? 3.2918 3.1535 3.5371 0.8196  0.0508  -0.1678 8   THR L N   
8166  C CA  . THR D 3   ? 3.3507 3.1096 3.5467 0.7698  0.0321  -0.1668 8   THR L CA  
8167  C C   . THR D 3   ? 3.3812 3.1477 3.5472 0.7293  0.0387  -0.2058 8   THR L C   
8168  O O   . THR D 3   ? 3.3611 3.2042 3.5360 0.7296  0.0609  -0.2319 8   THR L O   
8169  C CB  . THR D 3   ? 3.3727 3.0687 3.5393 0.7397  0.0318  -0.1460 8   THR L CB  
8170  O OG1 . THR D 3   ? 3.3597 3.1104 3.5224 0.7265  0.0574  -0.1623 8   THR L OG1 
8171  C CG2 . THR D 3   ? 3.3471 3.0253 3.5403 0.7771  0.0227  -0.1059 8   THR L CG2 
8172  N N   . PHE D 4   ? 3.4332 3.1185 3.5630 0.6940  0.0191  -0.2096 9   PHE L N   
8173  C CA  . PHE D 4   ? 3.4672 3.1491 3.5660 0.6538  0.0222  -0.2454 9   PHE L CA  
8174  C C   . PHE D 4   ? 3.5281 3.1062 3.5711 0.5958  0.0087  -0.2438 9   PHE L C   
8175  O O   . PHE D 4   ? 3.5499 3.0475 3.5802 0.5914  -0.0120 -0.2163 9   PHE L O   
8176  C CB  . PHE D 4   ? 3.4629 3.1662 3.5799 0.6754  0.0117  -0.2593 9   PHE L CB  
8177  C CG  . PHE D 4   ? 3.4072 3.2200 3.5746 0.7255  0.0276  -0.2701 9   PHE L CG  
8178  C CD1 . PHE D 4   ? 3.3647 3.2079 3.5767 0.7801  0.0232  -0.2444 9   PHE L CD1 
8179  C CD2 . PHE D 4   ? 3.3979 3.2830 3.5678 0.7180  0.0467  -0.3063 9   PHE L CD2 
8180  C CE1 . PHE D 4   ? 3.3139 3.2581 3.5721 0.8262  0.0379  -0.2546 9   PHE L CE1 
8181  C CE2 . PHE D 4   ? 3.3473 3.3335 3.5632 0.7638  0.0613  -0.3167 9   PHE L CE2 
8182  C CZ  . PHE D 4   ? 3.3053 3.3211 3.5654 0.8180  0.0569  -0.2908 9   PHE L CZ  
8183  N N   . VAL D 5   ? 3.4110 2.9922 3.4210 0.5516  0.0207  -0.2734 11  VAL L N   
8184  C CA  . VAL D 5   ? 3.6231 3.1126 3.5779 0.4926  0.0102  -0.2780 11  VAL L CA  
8185  C C   . VAL D 5   ? 3.7271 3.2319 3.6600 0.4617  0.0148  -0.3172 11  VAL L C   
8186  O O   . VAL D 5   ? 3.6782 3.2524 3.6146 0.4552  0.0369  -0.3438 11  VAL L O   
8187  C CB  . VAL D 5   ? 3.4983 2.9642 3.4280 0.4624  0.0216  -0.2699 11  VAL L CB  
8188  C CG1 . VAL D 5   ? 3.3312 2.7419 3.2665 0.4779  0.0084  -0.2286 11  VAL L CG1 
8189  C CG2 . VAL D 5   ? 3.3458 2.9101 3.2985 0.4774  0.0503  -0.2862 11  VAL L CG2 
8190  N N   . SER D 6   ? 3.6819 3.1235 3.5930 0.4433  -0.0058 -0.3209 12  SER L N   
8191  C CA  . SER D 6   ? 3.7375 3.1856 3.6263 0.4131  -0.0040 -0.3569 12  SER L CA  
8192  C C   . SER D 6   ? 3.8859 3.2473 3.7168 0.3500  -0.0103 -0.3633 12  SER L C   
8193  O O   . SER D 6   ? 3.9332 3.2033 3.7403 0.3332  -0.0310 -0.3409 12  SER L O   
8194  C CB  . SER D 6   ? 3.7427 3.1830 3.6465 0.4353  -0.0218 -0.3592 12  SER L CB  
8195  O OG  . SER D 6   ? 3.8515 3.1970 3.7388 0.4290  -0.0478 -0.3320 12  SER L OG  
8196  N N   . VAL D 7   ? 3.9975 3.3881 3.8062 0.3154  0.0073  -0.3941 13  VAL L N   
8197  C CA  . VAL D 7   ? 4.1467 3.4650 3.9006 0.2540  0.0048  -0.4040 13  VAL L CA  
8198  C C   . VAL D 7   ? 4.3063 3.6446 4.0394 0.2234  0.0111  -0.4439 13  VAL L C   
8199  O O   . VAL D 7   ? 4.2425 3.6704 3.9978 0.2384  0.0305  -0.4687 13  VAL L O   
8200  C CB  . VAL D 7   ? 3.9495 3.2762 3.6916 0.2362  0.0221  -0.3983 13  VAL L CB  
8201  C CG1 . VAL D 7   ? 4.0075 3.2644 3.6931 0.1722  0.0206  -0.4112 13  VAL L CG1 
8202  C CG2 . VAL D 7   ? 3.8285 3.1274 3.5877 0.2631  0.0146  -0.3580 13  VAL L CG2 
8203  N N   . ALA D 8   ? 4.1857 3.4404 3.8762 0.1807  -0.0054 -0.4498 14  ALA L N   
8204  C CA  . ALA D 8   ? 4.2584 3.5193 3.9235 0.1463  -0.0015 -0.4866 14  ALA L CA  
8205  C C   . ALA D 8   ? 4.2370 3.5394 3.8839 0.1143  0.0229  -0.5118 14  ALA L C   
8206  O O   . ALA D 8   ? 4.1471 3.4303 3.7797 0.0979  0.0302  -0.4990 14  ALA L O   
8207  C CB  . ALA D 8   ? 4.2641 3.4179 3.8841 0.1045  -0.0246 -0.4841 14  ALA L CB  
8208  N N   . PRO D 9   ? 4.1549 3.5161 3.8027 0.1060  0.0359  -0.5477 15  PRO L N   
8209  C CA  . PRO D 9   ? 4.1161 3.5214 3.7475 0.0761  0.0596  -0.5739 15  PRO L CA  
8210  C C   . PRO D 9   ? 4.1383 3.4602 3.7150 0.0165  0.0559  -0.5744 15  PRO L C   
8211  O O   . PRO D 9   ? 4.2499 3.4911 3.7918 -0.0162 0.0376  -0.5755 15  PRO L O   
8212  C CB  . PRO D 9   ? 4.1564 3.6187 3.7933 0.0743  0.0672  -0.6113 15  PRO L CB  
8213  C CG  . PRO D 9   ? 4.0657 3.5530 3.7418 0.1233  0.0553  -0.6018 15  PRO L CG  
8214  C CD  . PRO D 9   ? 4.1258 3.5227 3.7937 0.1275  0.0304  -0.5659 15  PRO L CD  
8215  N N   . GLY D 10  ? 4.0195 3.3616 3.5887 0.0026  0.0734  -0.5735 16  GLY L N   
8216  C CA  . GLY D 10  ? 4.0028 3.2733 3.5218 -0.0529 0.0723  -0.5745 16  GLY L CA  
8217  C C   . GLY D 10  ? 4.0189 3.2090 3.5249 -0.0569 0.0576  -0.5369 16  GLY L C   
8218  O O   . GLY D 10  ? 4.0321 3.1668 3.4993 -0.0997 0.0585  -0.5343 16  GLY L O   
8219  N N   . GLN D 11  ? 4.0862 3.2690 3.6238 -0.0132 0.0441  -0.5079 17  GLN L N   
8220  C CA  . GLN D 11  ? 4.0200 3.1276 3.5493 -0.0120 0.0285  -0.4703 17  GLN L CA  
8221  C C   . GLN D 11  ? 3.8068 2.9575 3.3588 0.0107  0.0445  -0.4523 17  GLN L C   
8222  O O   . GLN D 11  ? 3.7202 2.9354 3.2758 0.0047  0.0677  -0.4713 17  GLN L O   
8223  C CB  . GLN D 11  ? 4.0312 3.1095 3.5834 0.0238  0.0058  -0.4482 17  GLN L CB  
8224  C CG  . GLN D 11  ? 4.1780 3.2124 3.7091 0.0038  -0.0110 -0.4647 17  GLN L CG  
8225  C CD  . GLN D 11  ? 4.2993 3.2286 3.7741 -0.0534 -0.0253 -0.4639 17  GLN L CD  
8226  O OE1 . GLN D 11  ? 4.4436 3.3633 3.8848 -0.0971 -0.0139 -0.4824 17  GLN L OE1 
8227  N NE2 . GLN D 11  ? 4.2357 3.0856 3.7001 -0.0532 -0.0506 -0.4427 17  GLN L NE2 
8228  N N   . THR D 12  ? 3.7601 2.8751 3.3270 0.0364  0.0322  -0.4158 18  THR L N   
8229  C CA  . THR D 12  ? 3.7211 2.8662 3.3086 0.0585  0.0445  -0.3944 18  THR L CA  
8230  C C   . THR D 12  ? 3.6671 2.8544 3.3065 0.1207  0.0400  -0.3707 18  THR L C   
8231  O O   . THR D 12  ? 3.6751 2.8139 3.3206 0.1368  0.0182  -0.3512 18  THR L O   
8232  C CB  . THR D 12  ? 3.7572 2.8107 3.3082 0.0246  0.0347  -0.3702 18  THR L CB  
8233  O OG1 . THR D 12  ? 3.8074 2.8230 3.3100 -0.0337 0.0393  -0.3929 18  THR L OG1 
8234  C CG2 . THR D 12  ? 3.7170 2.8041 3.2887 0.0462  0.0486  -0.3495 18  THR L CG2 
8235  N N   . ALA D 13  ? 3.8300 3.1078 3.5064 0.1553  0.0607  -0.3727 19  ALA L N   
8236  C CA  . ALA D 13  ? 3.7591 3.0881 3.4872 0.2159  0.0601  -0.3518 19  ALA L CA  
8237  C C   . ALA D 13  ? 3.7196 3.0333 3.4554 0.2283  0.0629  -0.3197 19  ALA L C   
8238  O O   . ALA D 13  ? 3.6619 2.9754 3.3776 0.2015  0.0770  -0.3232 19  ALA L O   
8239  C CB  . ALA D 13  ? 3.5883 3.0331 3.3551 0.2490  0.0816  -0.3761 19  ALA L CB  
8240  N N   . ARG D 14  ? 3.7222 3.0237 3.4876 0.2693  0.0495  -0.2886 20  ARG L N   
8241  C CA  . ARG D 14  ? 3.5805 2.8662 3.3567 0.2859  0.0502  -0.2555 20  ARG L CA  
8242  C C   . ARG D 14  ? 3.4888 2.8490 3.3219 0.3496  0.0555  -0.2407 20  ARG L C   
8243  O O   . ARG D 14  ? 3.4959 2.8659 3.3534 0.3806  0.0432  -0.2373 20  ARG L O   
8244  C CB  . ARG D 14  ? 3.5781 2.7536 3.3282 0.2684  0.0243  -0.2263 20  ARG L CB  
8245  C CG  . ARG D 14  ? 3.7154 2.8060 3.4085 0.2063  0.0153  -0.2373 20  ARG L CG  
8246  C CD  . ARG D 14  ? 3.8398 2.9040 3.5043 0.1724  0.0262  -0.2318 20  ARG L CD  
8247  N NE  . ARG D 14  ? 4.0253 3.0019 3.6353 0.1142  0.0152  -0.2398 20  ARG L NE  
8248  C CZ  . ARG D 14  ? 4.0163 2.9311 3.5926 0.0792  0.0140  -0.2268 20  ARG L CZ  
8249  N NH1 . ARG D 14  ? 3.9261 2.8570 3.5176 0.0965  0.0231  -0.2050 20  ARG L NH1 
8250  N NH2 . ARG D 14  ? 4.1568 2.9935 3.6841 0.0269  0.0036  -0.2354 20  ARG L NH2 
8251  N N   . ILE D 15  ? 3.6975 3.1100 3.5515 0.3691  0.0738  -0.2317 21  ILE L N   
8252  C CA  . ILE D 15  ? 3.5041 2.9965 3.4125 0.4289  0.0824  -0.2201 21  ILE L CA  
8253  C C   . ILE D 15  ? 3.3352 2.8054 3.2556 0.4480  0.0807  -0.1835 21  ILE L C   
8254  O O   . ILE D 15  ? 3.2813 2.7349 3.1803 0.4223  0.0908  -0.1794 21  ILE L O   
8255  C CB  . ILE D 15  ? 3.3580 2.9574 3.2878 0.4413  0.1102  -0.2489 21  ILE L CB  
8256  C CG1 . ILE D 15  ? 3.3582 2.9848 3.2812 0.4283  0.1112  -0.2843 21  ILE L CG1 
8257  C CG2 . ILE D 15  ? 3.1433 2.8238 3.1280 0.5019  0.1208  -0.2342 21  ILE L CG2 
8258  C CD1 . ILE D 15  ? 3.2725 2.9970 3.2100 0.4330  0.1378  -0.3154 21  ILE L CD1 
8259  N N   . THR D 16  ? 3.1138 2.5850 3.0686 0.4932  0.0683  -0.1573 22  THR L N   
8260  C CA  . THR D 16  ? 3.0891 2.5434 3.0603 0.5170  0.0658  -0.1214 22  THR L CA  
8261  C C   . THR D 16  ? 3.0218 2.5778 3.0469 0.5731  0.0824  -0.1188 22  THR L C   
8262  O O   . THR D 16  ? 3.0124 2.6168 3.0693 0.6079  0.0801  -0.1264 22  THR L O   
8263  C CB  . THR D 16  ? 3.1077 2.4789 3.0758 0.5250  0.0378  -0.0903 22  THR L CB  
8264  O OG1 . THR D 16  ? 3.0900 2.4873 3.0876 0.5602  0.0272  -0.0931 22  THR L OG1 
8265  C CG2 . THR D 16  ? 3.1747 2.4427 3.0883 0.4687  0.0217  -0.0912 22  THR L CG2 
8266  N N   . CYS D 17  ? 3.0955 2.6836 3.1309 0.5822  0.0989  -0.1080 23  CYS L N   
8267  C CA  . CYS D 17  ? 3.0151 2.6994 3.1011 0.6350  0.1155  -0.1047 23  CYS L CA  
8268  C C   . CYS D 17  ? 2.9840 2.6597 3.0814 0.6514  0.1197  -0.0732 23  CYS L C   
8269  O O   . CYS D 17  ? 2.9494 2.5686 3.0131 0.6153  0.1195  -0.0644 23  CYS L O   
8270  C CB  . CYS D 17  ? 2.9275 2.6996 3.0186 0.6296  0.1421  -0.1394 23  CYS L CB  
8271  S SG  . CYS D 17  ? 3.2736 3.1692 3.4243 0.6910  0.1662  -0.1377 23  CYS L SG  
8272  N N   . GLY D 18  ? 3.0987 2.8313 3.2439 0.7062  0.1236  -0.0563 24  GLY L N   
8273  C CA  . GLY D 18  ? 2.9571 2.6893 3.1172 0.7259  0.1287  -0.0267 24  GLY L CA  
8274  C C   . GLY D 18  ? 3.0049 2.6402 3.1500 0.7194  0.1047  0.0078  24  GLY L C   
8275  O O   . GLY D 18  ? 3.1482 2.7101 3.2650 0.6924  0.0845  0.0074  24  GLY L O   
8276  N N   . GLU D 19  ? 3.1140 2.7484 3.2778 0.7442  0.1066  0.0378  25  GLU L N   
8277  C CA  . GLU D 19  ? 3.1217 2.6676 3.2735 0.7402  0.0850  0.0724  25  GLU L CA  
8278  C C   . GLU D 19  ? 3.1735 2.6375 3.2716 0.6816  0.0811  0.0725  25  GLU L C   
8279  O O   . GLU D 19  ? 3.1786 2.6542 3.2494 0.6446  0.0945  0.0455  25  GLU L O   
8280  C CB  . GLU D 19  ? 2.9640 2.5414 3.1538 0.7856  0.0903  0.1027  25  GLU L CB  
8281  C CG  . GLU D 19  ? 2.8659 2.4804 3.0527 0.7772  0.1137  0.1007  25  GLU L CG  
8282  C CD  . GLU D 19  ? 2.7421 2.3779 2.9624 0.8182  0.1178  0.1325  25  GLU L CD  
8283  O OE1 . GLU D 19  ? 2.7506 2.3935 3.0044 0.8602  0.1060  0.1521  25  GLU L OE1 
8284  O OE2 . GLU D 19  ? 2.7450 2.3910 2.9584 0.8084  0.1329  0.1377  25  GLU L OE2 
8285  N N   . GLU D 20  ? 3.1831 2.5629 3.2657 0.6727  0.0625  0.1032  26  GLU L N   
8286  C CA  . GLU D 20  ? 3.2668 2.5662 3.2999 0.6193  0.0580  0.1067  26  GLU L CA  
8287  C C   . GLU D 20  ? 3.1378 2.4658 3.1698 0.6144  0.0788  0.1114  26  GLU L C   
8288  O O   . GLU D 20  ? 3.0156 2.3963 3.0846 0.6555  0.0891  0.1276  26  GLU L O   
8289  C CB  . GLU D 20  ? 3.3295 2.5269 3.3442 0.6093  0.0311  0.1378  26  GLU L CB  
8290  C CG  . GLU D 20  ? 3.4059 2.5584 3.4133 0.6060  0.0083  0.1344  26  GLU L CG  
8291  C CD  . GLU D 20  ? 3.5285 2.6363 3.5551 0.6370  -0.0135 0.1696  26  GLU L CD  
8292  O OE1 . GLU D 20  ? 3.5688 2.6825 3.6156 0.6621  -0.0106 0.1966  26  GLU L OE1 
8293  O OE2 . GLU D 20  ? 3.6200 2.6834 3.6397 0.6345  -0.0339 0.1704  26  GLU L OE2 
8294  N N   . SER D 21  ? 2.9596 2.9745 3.0777 -0.2253 0.1355  -0.7254 27  SER L N   
8295  C CA  . SER D 21  ? 2.8802 2.8945 2.9679 -0.2103 0.1314  -0.6739 27  SER L CA  
8296  C C   . SER D 21  ? 2.8534 2.8638 2.9889 -0.1772 0.1212  -0.6945 27  SER L C   
8297  O O   . SER D 21  ? 2.8760 2.8529 3.0510 -0.1456 0.0992  -0.7365 27  SER L O   
8298  C CB  . SER D 21  ? 3.0219 2.9854 3.0548 -0.1866 0.1046  -0.6341 27  SER L CB  
8299  O OG  . SER D 21  ? 2.8765 2.8290 2.8900 -0.1605 0.0938  -0.5940 27  SER L OG  
8300  N N   . LEU D 22  ? 2.8357 2.8811 2.9672 -0.1850 0.1373  -0.6642 28  LEU L N   
8301  C CA  . LEU D 22  ? 2.7885 2.8355 2.9602 -0.1569 0.1303  -0.6755 28  LEU L CA  
8302  C C   . LEU D 22  ? 2.6830 2.7032 2.8157 -0.1272 0.1119  -0.6253 28  LEU L C   
8303  O O   . LEU D 22  ? 2.6427 2.6396 2.8026 -0.0898 0.0922  -0.6369 28  LEU L O   
8304  C CB  . LEU D 22  ? 2.7222 2.8324 2.9246 -0.1881 0.1638  -0.6817 28  LEU L CB  
8305  C CG  . LEU D 22  ? 2.5945 2.7140 2.8513 -0.1645 0.1605  -0.7049 28  LEU L CG  
8306  C CD1 . LEU D 22  ? 2.7342 2.8197 3.0457 -0.1334 0.1380  -0.7640 28  LEU L CD1 
8307  C CD2 . LEU D 22  ? 2.5392 2.7239 2.8233 -0.2001 0.1960  -0.7096 28  LEU L CD2 
8308  N N   . GLY D 23  ? 2.6769 2.6998 2.7465 -0.1431 0.1177  -0.5701 29  GLY L N   
8309  C CA  . GLY D 23  ? 2.6318 2.6291 2.6578 -0.1171 0.1012  -0.5183 29  GLY L CA  
8310  C C   . GLY D 23  ? 2.7660 2.7413 2.7263 -0.1261 0.0953  -0.4760 29  GLY L C   
8311  O O   . GLY D 23  ? 2.8897 2.8576 2.8442 -0.1430 0.0964  -0.4943 29  GLY L O   
8312  N N   . SER D 24  ? 2.7943 2.7589 2.7052 -0.1147 0.0889  -0.4194 30  SER L N   
8313  C CA  . SER D 24  ? 2.8210 2.7676 2.6674 -0.1242 0.0846  -0.3738 30  SER L CA  
8314  C C   . SER D 24  ? 2.7346 2.7313 2.5600 -0.1778 0.1181  -0.3580 30  SER L C   
8315  O O   . SER D 24  ? 2.5394 2.5838 2.3670 -0.2021 0.1438  -0.3412 30  SER L O   
8316  C CB  . SER D 24  ? 2.7571 2.6838 2.5577 -0.0994 0.0715  -0.3163 30  SER L CB  
8317  O OG  . SER D 24  ? 2.7671 2.7376 2.5691 -0.1137 0.0932  -0.2921 30  SER L OG  
8318  N N   . ARG D 25  ? 2.8433 2.8292 2.6487 -0.1963 0.1179  -0.3639 31  ARG L N   
8319  C CA  . ARG D 25  ? 2.7482 2.7792 2.5367 -0.2472 0.1485  -0.3551 31  ARG L CA  
8320  C C   . ARG D 25  ? 2.7380 2.7623 2.4560 -0.2616 0.1494  -0.2948 31  ARG L C   
8321  O O   . ARG D 25  ? 2.7923 2.7727 2.4757 -0.2323 0.1246  -0.2651 31  ARG L O   
8322  C CB  . ARG D 25  ? 2.8313 2.8616 2.6508 -0.2639 0.1516  -0.4088 31  ARG L CB  
8323  C CG  . ARG D 25  ? 2.7679 2.8236 2.6565 -0.2668 0.1627  -0.4679 31  ARG L CG  
8324  C CD  . ARG D 25  ? 2.8635 2.9218 2.7743 -0.2884 0.1688  -0.5145 31  ARG L CD  
8325  N NE  . ARG D 25  ? 2.7935 2.8857 2.7669 -0.2994 0.1857  -0.5669 31  ARG L NE  
8326  C CZ  . ARG D 25  ? 2.9743 3.0790 2.9751 -0.3213 0.1963  -0.6114 31  ARG L CZ  
8327  N NH1 . ARG D 25  ? 3.0831 3.1686 3.0540 -0.3347 0.1913  -0.6104 31  ARG L NH1 
8328  N NH2 . ARG D 25  ? 2.9959 3.1325 3.0539 -0.3298 0.2119  -0.6566 31  ARG L NH2 
8329  N N   . SER D 26  ? 2.6996 2.7698 2.3975 -0.3081 0.1791  -0.2771 32  SER L N   
8330  C CA  . SER D 26  ? 2.7253 2.7970 2.3596 -0.3306 0.1848  -0.2243 32  SER L CA  
8331  C C   . SER D 26  ? 2.7571 2.8607 2.3953 -0.3761 0.2079  -0.2464 32  SER L C   
8332  O O   . SER D 26  ? 2.7187 2.8714 2.3443 -0.4153 0.2374  -0.2277 32  SER L O   
8333  C CB  . SER D 26  ? 2.6526 2.7536 2.2513 -0.3401 0.1999  -0.1665 32  SER L CB  
8334  O OG  . SER D 26  ? 2.6797 2.7799 2.2161 -0.3602 0.2040  -0.1139 32  SER L OG  
8335  N N   . VAL D 27  ? 2.7869 2.8615 2.4439 -0.3701 0.1937  -0.2883 33  VAL L N   
8336  C CA  . VAL D 27  ? 2.8658 2.9671 2.5333 -0.4096 0.2134  -0.3176 33  VAL L CA  
8337  C C   . VAL D 27  ? 2.9391 3.0487 2.5457 -0.4413 0.2231  -0.2701 33  VAL L C   
8338  O O   . VAL D 27  ? 3.0129 3.0822 2.5788 -0.4257 0.2020  -0.2402 33  VAL L O   
8339  C CB  . VAL D 27  ? 2.9680 3.0329 2.6713 -0.3920 0.1938  -0.3748 33  VAL L CB  
8340  C CG1 . VAL D 27  ? 3.0149 3.1091 2.7321 -0.4326 0.2150  -0.4082 33  VAL L CG1 
8341  C CG2 . VAL D 27  ? 2.9692 3.0216 2.7313 -0.3565 0.1812  -0.4185 33  VAL L CG2 
8342  N N   . ILE D 28  ? 2.8123 2.9743 2.4124 -0.4860 0.2551  -0.2623 34  ILE L N   
8343  C CA  . ILE D 28  ? 2.8417 3.0176 2.3879 -0.5214 0.2677  -0.2215 34  ILE L CA  
8344  C C   . ILE D 28  ? 2.9013 3.0893 2.4638 -0.5520 0.2790  -0.2630 34  ILE L C   
8345  O O   . ILE D 28  ? 2.8714 3.0973 2.4748 -0.5720 0.3002  -0.3013 34  ILE L O   
8346  C CB  . ILE D 28  ? 2.7617 2.9867 2.2815 -0.5488 0.2949  -0.1745 34  ILE L CB  
8347  C CG1 . ILE D 28  ? 2.7079 2.9220 2.2289 -0.5136 0.2836  -0.1491 34  ILE L CG1 
8348  C CG2 . ILE D 28  ? 2.7955 3.0241 2.2517 -0.5763 0.3011  -0.1220 34  ILE L CG2 
8349  C CD1 . ILE D 28  ? 2.6198 2.8808 2.1245 -0.5343 0.3086  -0.1095 34  ILE L CD1 
8350  N N   . TRP D 29  ? 2.8354 2.9919 2.3660 -0.5556 0.2650  -0.2551 35  TRP L N   
8351  C CA  . TRP D 29  ? 2.9212 3.0831 2.4627 -0.5825 0.2723  -0.2926 35  TRP L CA  
8352  C C   . TRP D 29  ? 2.8946 3.0909 2.3911 -0.6294 0.2958  -0.2563 35  TRP L C   
8353  O O   . TRP D 29  ? 2.8690 3.0653 2.3154 -0.6345 0.2960  -0.1983 35  TRP L O   
8354  C CB  . TRP D 29  ? 2.9883 3.0913 2.5259 -0.5563 0.2406  -0.3110 35  TRP L CB  
8355  C CG  . TRP D 29  ? 2.9657 3.0353 2.5521 -0.5132 0.2182  -0.3555 35  TRP L CG  
8356  C CD1 . TRP D 29  ? 2.9337 2.9655 2.5187 -0.4692 0.1930  -0.3405 35  TRP L CD1 
8357  C CD2 . TRP D 29  ? 2.9747 3.0447 2.6182 -0.5095 0.2186  -0.4224 35  TRP L CD2 
8358  N NE1 . TRP D 29  ? 2.9527 2.9619 2.5909 -0.4387 0.1777  -0.3940 35  TRP L NE1 
8359  C CE2 . TRP D 29  ? 2.9935 3.0256 2.6686 -0.4627 0.1930  -0.4447 35  TRP L CE2 
8360  C CE3 . TRP D 29  ? 2.9754 3.0743 2.6462 -0.5410 0.2381  -0.4654 35  TRP L CE3 
8361  C CZ2 . TRP D 29  ? 3.0502 3.0729 2.7834 -0.4470 0.1864  -0.5080 35  TRP L CZ2 
8362  C CZ3 . TRP D 29  ? 3.0043 3.0940 2.7326 -0.5250 0.2319  -0.5280 35  TRP L CZ3 
8363  C CH2 . TRP D 29  ? 3.0548 3.1068 2.8140 -0.4787 0.2063  -0.5486 35  TRP L CH2 
8364  N N   . TYR D 30  ? 3.0095 3.2349 2.5244 -0.6633 0.3156  -0.2911 36  TYR L N   
8365  C CA  . TYR D 30  ? 3.0402 3.2993 2.5171 -0.7097 0.3386  -0.2642 36  TYR L CA  
8366  C C   . TYR D 30  ? 3.1931 3.4427 2.6809 -0.7275 0.3375  -0.3067 36  TYR L C   
8367  O O   . TYR D 30  ? 3.2838 3.5239 2.8203 -0.7145 0.3321  -0.3636 36  TYR L O   
8368  C CB  . TYR D 30  ? 2.8777 3.1998 2.3659 -0.7405 0.3734  -0.2575 36  TYR L CB  
8369  C CG  . TYR D 30  ? 2.7899 3.1242 2.2604 -0.7277 0.3764  -0.2095 36  TYR L CG  
8370  C CD1 . TYR D 30  ? 2.7866 3.1272 2.1990 -0.7424 0.3808  -0.1459 36  TYR L CD1 
8371  C CD2 . TYR D 30  ? 2.7124 3.0519 2.2246 -0.7010 0.3748  -0.2279 36  TYR L CD2 
8372  C CE1 . TYR D 30  ? 2.7083 3.0598 2.1042 -0.7304 0.3836  -0.1022 36  TYR L CE1 
8373  C CE2 . TYR D 30  ? 2.6344 2.9845 2.1306 -0.6890 0.3772  -0.1848 36  TYR L CE2 
8374  C CZ  . TYR D 30  ? 2.6325 2.9886 2.0702 -0.7037 0.3817  -0.1221 36  TYR L CZ  
8375  O OH  . TYR D 30  ? 2.5562 2.9225 1.9779 -0.6911 0.3841  -0.0795 36  TYR L OH  
8376  N N   . GLN D 31  ? 2.9821 3.2339 2.4242 -0.7569 0.3424  -0.2784 37  GLN L N   
8377  C CA  . GLN D 31  ? 3.0740 3.3187 2.5184 -0.7784 0.3428  -0.3120 37  GLN L CA  
8378  C C   . GLN D 31  ? 3.0729 3.3692 2.4996 -0.8295 0.3752  -0.3023 37  GLN L C   
8379  O O   . GLN D 31  ? 3.0491 3.3666 2.4316 -0.8503 0.3872  -0.2486 37  GLN L O   
8380  C CB  . GLN D 31  ? 3.1635 3.3582 2.5673 -0.7670 0.3161  -0.2884 37  GLN L CB  
8381  C CG  . GLN D 31  ? 3.2652 3.4473 2.6668 -0.7869 0.3133  -0.3187 37  GLN L CG  
8382  C CD  . GLN D 31  ? 3.3489 3.4853 2.7048 -0.7773 0.2885  -0.2850 37  GLN L CD  
8383  O OE1 . GLN D 31  ? 3.3688 3.4621 2.7353 -0.7578 0.2652  -0.3138 37  GLN L OE1 
8384  N NE2 . GLN D 31  ? 3.4003 3.5462 2.7045 -0.7914 0.2935  -0.2226 37  GLN L NE2 
8385  N N   . GLN D 32  ? 2.8721 3.1883 2.3322 -0.8497 0.3892  -0.3533 38  GLN L N   
8386  C CA  . GLN D 32  ? 2.8802 3.2453 2.3253 -0.8983 0.4200  -0.3478 38  GLN L CA  
8387  C C   . GLN D 32  ? 2.9892 3.3380 2.4284 -0.9167 0.4154  -0.3772 38  GLN L C   
8388  O O   . GLN D 32  ? 3.0168 3.3636 2.4986 -0.9143 0.4160  -0.4347 38  GLN L O   
8389  C CB  . GLN D 32  ? 2.8090 3.2242 2.2994 -0.9110 0.4475  -0.3792 38  GLN L CB  
8390  C CG  . GLN D 32  ? 2.7994 3.2695 2.2726 -0.9602 0.4814  -0.3672 38  GLN L CG  
8391  C CD  . GLN D 32  ? 2.7751 3.2941 2.2955 -0.9716 0.5083  -0.4003 38  GLN L CD  
8392  O OE1 . GLN D 32  ? 2.7740 3.2846 2.3464 -0.9477 0.5020  -0.4476 38  GLN L OE1 
8393  N NE2 . GLN D 32  ? 2.7556 3.3266 2.2587 -1.0087 0.5386  -0.3756 38  GLN L NE2 
8394  N N   . ARG D 33  ? 3.1729 3.5093 2.5596 -0.9342 0.4103  -0.3375 39  ARG L N   
8395  C CA  . ARG D 33  ? 3.3566 3.6815 2.7320 -0.9565 0.4080  -0.3594 39  ARG L CA  
8396  C C   . ARG D 33  ? 3.3583 3.7381 2.7451 -0.9995 0.4420  -0.3805 39  ARG L C   
8397  O O   . ARG D 33  ? 3.2380 3.6627 2.6130 -1.0213 0.4665  -0.3511 39  ARG L O   
8398  C CB  . ARG D 33  ? 3.4557 3.7516 2.7721 -0.9621 0.3923  -0.3090 39  ARG L CB  
8399  C CG  . ARG D 33  ? 3.4180 3.6717 2.7320 -0.9586 0.3713  -0.3377 39  ARG L CG  
8400  C CD  . ARG D 33  ? 3.5085 3.7098 2.8491 -0.9104 0.3398  -0.3623 39  ARG L CD  
8401  N NE  . ARG D 33  ? 3.4489 3.6150 2.7652 -0.8772 0.3166  -0.3189 39  ARG L NE  
8402  C CZ  . ARG D 33  ? 3.5053 3.6233 2.8422 -0.8350 0.2878  -0.3393 39  ARG L CZ  
8403  N NH1 . ARG D 33  ? 3.5792 3.6819 2.9602 -0.8238 0.2805  -0.4004 39  ARG L NH1 
8404  N NH2 . ARG D 33  ? 3.5119 3.5971 2.8259 -0.8042 0.2664  -0.2999 39  ARG L NH2 
8405  N N   . PRO D 34  ? 3.2531 3.6311 2.6628 -1.0122 0.4446  -0.4310 40  PRO L N   
8406  C CA  . PRO D 34  ? 3.2405 3.6710 2.6630 -1.0520 0.4773  -0.4536 40  PRO L CA  
8407  C C   . PRO D 34  ? 3.1330 3.6001 2.5062 -1.0939 0.4993  -0.4050 40  PRO L C   
8408  O O   . PRO D 34  ? 3.2505 3.6993 2.5787 -1.1085 0.4904  -0.3762 40  PRO L O   
8409  C CB  . PRO D 34  ? 3.3745 3.7835 2.8168 -1.0561 0.4692  -0.5079 40  PRO L CB  
8410  C CG  . PRO D 34  ? 3.3754 3.7230 2.7978 -1.0283 0.4339  -0.4985 40  PRO L CG  
8411  C CD  . PRO D 34  ? 3.2583 3.5866 2.6830 -0.9910 0.4182  -0.4702 40  PRO L CD  
8412  N N   . GLY D 35  ? 2.9979 3.5181 2.3812 -1.1132 0.5284  -0.3962 41  GLY L N   
8413  C CA  . GLY D 35  ? 2.9345 3.4970 2.2770 -1.1533 0.5533  -0.3522 41  GLY L CA  
8414  C C   . GLY D 35  ? 2.8802 3.4440 2.1815 -1.1484 0.5506  -0.2849 41  GLY L C   
8415  O O   . GLY D 35  ? 2.8726 3.4662 2.1338 -1.1818 0.5683  -0.2439 41  GLY L O   
8416  N N   . GLN D 36  ? 3.2252 3.7585 2.5352 -1.1081 0.5297  -0.2721 42  GLN L N   
8417  C CA  . GLN D 36  ? 3.1662 3.6975 2.4371 -1.1001 0.5254  -0.2082 42  GLN L CA  
8418  C C   . GLN D 36  ? 2.9349 3.4814 2.2357 -1.0754 0.5300  -0.2052 42  GLN L C   
8419  O O   . GLN D 36  ? 2.7496 3.3159 2.1010 -1.0700 0.5408  -0.2506 42  GLN L O   
8420  C CB  . GLN D 36  ? 3.3118 3.7847 2.5518 -1.0731 0.4915  -0.1825 42  GLN L CB  
8421  C CG  . GLN D 36  ? 3.4032 3.8553 2.6105 -1.0940 0.4830  -0.1800 42  GLN L CG  
8422  C CD  . GLN D 36  ? 3.5077 3.9026 2.6862 -1.0653 0.4494  -0.1530 42  GLN L CD  
8423  O OE1 . GLN D 36  ? 3.6009 3.9756 2.7758 -1.0332 0.4348  -0.1267 42  GLN L OE1 
8424  N NE2 . GLN D 36  ? 3.6123 3.9804 2.7699 -1.0764 0.4369  -0.1592 42  GLN L NE2 
8425  N N   . ALA D 37  ? 3.1846 3.7225 2.4535 -1.0604 0.5220  -0.1495 43  ALA L N   
8426  C CA  . ALA D 37  ? 2.9704 3.5210 2.2616 -1.0367 0.5251  -0.1398 43  ALA L CA  
8427  C C   . ALA D 37  ? 3.0137 3.5104 2.3202 -0.9862 0.4918  -0.1477 43  ALA L C   
8428  O O   . ALA D 37  ? 3.1164 3.5673 2.3959 -0.9708 0.4666  -0.1333 43  ALA L O   
8429  C CB  . ALA D 37  ? 2.8140 3.3917 2.0610 -1.0520 0.5389  -0.0735 43  ALA L CB  
8430  N N   . PRO D 38  ? 2.9646 3.4661 2.3151 -0.9598 0.4913  -0.1713 44  PRO L N   
8431  C CA  . PRO D 38  ? 2.9211 3.3725 2.2881 -0.9103 0.4599  -0.1795 44  PRO L CA  
8432  C C   . PRO D 38  ? 2.9257 3.3476 2.2428 -0.8922 0.4415  -0.1181 44  PRO L C   
8433  O O   . PRO D 38  ? 2.9312 3.3801 2.2174 -0.9055 0.4556  -0.0686 44  PRO L O   
8434  C CB  . PRO D 38  ? 2.8120 3.2881 2.2285 -0.8943 0.4702  -0.2040 44  PRO L CB  
8435  C CG  . PRO D 38  ? 2.7938 3.3226 2.2357 -0.9323 0.5023  -0.2353 44  PRO L CG  
8436  C CD  . PRO D 38  ? 2.8564 3.4088 2.2475 -0.9743 0.5191  -0.1972 44  PRO L CD  
8437  N N   . SER D 39  ? 2.8689 3.2347 2.1779 -0.8616 0.4098  -0.1213 45  SER L N   
8438  C CA  . SER D 39  ? 2.8715 3.2032 2.1350 -0.8403 0.3891  -0.0665 45  SER L CA  
8439  C C   . SER D 39  ? 2.8705 3.1600 2.1578 -0.7885 0.3616  -0.0776 45  SER L C   
8440  O O   . SER D 39  ? 2.9123 3.1837 2.2465 -0.7675 0.3508  -0.1317 45  SER L O   
8441  C CB  . SER D 39  ? 2.9720 3.2719 2.1961 -0.8505 0.3742  -0.0517 45  SER L CB  
8442  O OG  . SER D 39  ? 3.0611 3.3237 2.3157 -0.8324 0.3544  -0.1038 45  SER L OG  
8443  N N   . LEU D 40  ? 2.9441 3.2216 2.2009 -0.7683 0.3523  -0.0265 46  LEU L N   
8444  C CA  . LEU D 40  ? 2.8835 3.1207 2.1573 -0.7184 0.3260  -0.0303 46  LEU L CA  
8445  C C   . LEU D 40  ? 3.0901 3.2666 2.3511 -0.6908 0.2927  -0.0354 46  LEU L C   
8446  O O   . LEU D 40  ? 3.2254 3.3856 2.4389 -0.7012 0.2856  0.0027  46  LEU L O   
8447  C CB  . LEU D 40  ? 2.7945 3.0396 2.0381 -0.7061 0.3275  0.0274  46  LEU L CB  
8448  C CG  . LEU D 40  ? 2.7644 2.9669 2.0202 -0.6536 0.2998  0.0291  46  LEU L CG  
8449  C CD1 . LEU D 40  ? 2.7061 2.9130 2.0259 -0.6331 0.2993  -0.0280 46  LEU L CD1 
8450  C CD2 . LEU D 40  ? 2.6932 2.9026 1.9117 -0.6439 0.3014  0.0912  46  LEU L CD2 
8451  N N   . ILE D 41  ? 2.9808 3.1243 2.2845 -0.6558 0.2724  -0.0822 47  ILE L N   
8452  C CA  . ILE D 41  ? 3.0113 3.0951 2.3093 -0.6245 0.2393  -0.0920 47  ILE L CA  
8453  C C   . ILE D 41  ? 3.0047 3.0523 2.3081 -0.5752 0.2149  -0.0797 47  ILE L C   
8454  O O   . ILE D 41  ? 3.0183 3.0292 2.2838 -0.5544 0.1940  -0.0406 47  ILE L O   
8455  C CB  . ILE D 41  ? 3.0353 3.1044 2.3757 -0.6246 0.2329  -0.1588 47  ILE L CB  
8456  C CG1 . ILE D 41  ? 3.0554 3.1530 2.3843 -0.6718 0.2533  -0.1685 47  ILE L CG1 
8457  C CG2 . ILE D 41  ? 3.0879 3.0939 2.4259 -0.5874 0.1973  -0.1693 47  ILE L CG2 
8458  C CD1 . ILE D 41  ? 3.0233 3.1798 2.3690 -0.7057 0.2869  -0.1773 47  ILE L CD1 
8459  N N   . ILE D 42  ? 3.1674 3.2233 2.5188 -0.5549 0.2163  -0.1143 48  ILE L N   
8460  C CA  . ILE D 42  ? 3.0734 3.0954 2.4347 -0.5071 0.1931  -0.1081 48  ILE L CA  
8461  C C   . ILE D 42  ? 2.8587 2.9185 2.2462 -0.5052 0.2107  -0.1082 48  ILE L C   
8462  O O   . ILE D 42  ? 2.8406 2.9295 2.2754 -0.5165 0.2263  -0.1539 48  ILE L O   
8463  C CB  . ILE D 42  ? 3.0597 3.0366 2.4619 -0.4722 0.1668  -0.1622 48  ILE L CB  
8464  C CG1 . ILE D 42  ? 3.1892 3.1219 2.5641 -0.4675 0.1451  -0.1590 48  ILE L CG1 
8465  C CG2 . ILE D 42  ? 2.8807 2.8330 2.3029 -0.4257 0.1480  -0.1627 48  ILE L CG2 
8466  C CD1 . ILE D 42  ? 3.3458 3.2360 2.7611 -0.4341 0.1202  -0.2119 48  ILE L CD1 
8467  N N   . TYR D 43  ? 2.9800 3.0402 2.3367 -0.4915 0.2087  -0.0567 49  TYR L N   
8468  C CA  . TYR D 43  ? 2.8828 2.9722 2.2608 -0.4835 0.2210  -0.0515 49  TYR L CA  
8469  C C   . TYR D 43  ? 2.8751 2.9194 2.2650 -0.4303 0.1915  -0.0528 49  TYR L C   
8470  O O   . TYR D 43  ? 2.9380 2.9336 2.3046 -0.4039 0.1648  -0.0396 49  TYR L O   
8471  C CB  . TYR D 43  ? 2.8268 2.9547 2.1598 -0.5109 0.2434  0.0092  49  TYR L CB  
8472  C CG  . TYR D 43  ? 2.8508 2.9478 2.1262 -0.4936 0.2264  0.0710  49  TYR L CG  
8473  C CD1 . TYR D 43  ? 2.9253 3.0063 2.1565 -0.5102 0.2213  0.0977  49  TYR L CD1 
8474  C CD2 . TYR D 43  ? 2.8014 2.8850 2.0663 -0.4608 0.2153  0.1028  49  TYR L CD2 
8475  C CE1 . TYR D 43  ? 2.9500 3.0028 2.1289 -0.4946 0.2059  0.1545  49  TYR L CE1 
8476  C CE2 . TYR D 43  ? 2.8257 2.8809 2.0373 -0.4447 0.2000  0.1597  49  TYR L CE2 
8477  C CZ  . TYR D 43  ? 2.8998 2.9400 2.0689 -0.4617 0.1955  0.1854  49  TYR L CZ  
8478  O OH  . TYR D 43  ? 2.9264 2.9390 2.0434 -0.4456 0.1805  0.2422  49  TYR L OH  
8479  N N   . ASN D 44  ? 2.8696 2.9295 2.2978 -0.4141 0.1960  -0.0709 50  ASN L N   
8480  C CA  . ASN D 44  ? 2.8593 2.8787 2.3041 -0.3632 0.1687  -0.0768 50  ASN L CA  
8481  C C   . ASN D 44  ? 2.9410 2.9088 2.4082 -0.3344 0.1401  -0.1195 50  ASN L C   
8482  O O   . ASN D 44  ? 2.9916 2.9114 2.4321 -0.3041 0.1132  -0.0991 50  ASN L O   
8483  C CB  . ASN D 44  ? 2.8431 2.8441 2.2357 -0.3436 0.1575  -0.0120 50  ASN L CB  
8484  C CG  . ASN D 44  ? 2.8200 2.7870 2.2312 -0.2930 0.1334  -0.0163 50  ASN L CG  
8485  O OD1 . ASN D 44  ? 2.7922 2.7613 2.2567 -0.2772 0.1309  -0.0630 50  ASN L OD1 
8486  N ND2 . ASN D 44  ? 2.8345 2.7695 2.2018 -0.2671 0.1150  0.0321  50  ASN L ND2 
8487  N N   . ASN D 45  ? 2.8742 2.8532 2.3904 -0.3455 0.1468  -0.1790 51  ASN L N   
8488  C CA  . ASN D 45  ? 2.9825 2.9173 2.5285 -0.3198 0.1220  -0.2272 51  ASN L CA  
8489  C C   . ASN D 45  ? 3.1714 3.0702 2.6802 -0.3225 0.1062  -0.2149 51  ASN L C   
8490  O O   . ASN D 45  ? 3.2349 3.1305 2.7621 -0.3378 0.1074  -0.2543 51  ASN L O   
8491  C CB  . ASN D 45  ? 2.9836 2.8797 2.5507 -0.2677 0.0951  -0.2355 51  ASN L CB  
8492  C CG  . ASN D 45  ? 2.8640 2.7914 2.4752 -0.2620 0.1077  -0.2557 51  ASN L CG  
8493  O OD1 . ASN D 45  ? 2.8156 2.7809 2.4664 -0.2869 0.1291  -0.2937 51  ASN L OD1 
8494  N ND2 . ASN D 45  ? 2.6941 2.6076 2.2969 -0.2304 0.0957  -0.2279 51  ASN L ND2 
8495  N N   . ASN D 46  ? 3.0218 2.8924 2.4791 -0.3070 0.0909  -0.1615 52  ASN L N   
8496  C CA  . ASN D 46  ? 3.1344 2.9679 2.5574 -0.3066 0.0739  -0.1493 52  ASN L CA  
8497  C C   . ASN D 46  ? 3.1150 2.9493 2.4727 -0.3171 0.0761  -0.0784 52  ASN L C   
8498  O O   . ASN D 46  ? 3.2658 3.0573 2.5897 -0.2968 0.0532  -0.0524 52  ASN L O   
8499  C CB  . ASN D 46  ? 3.1988 2.9722 2.6384 -0.2587 0.0383  -0.1741 52  ASN L CB  
8500  C CG  . ASN D 46  ? 3.3688 3.1083 2.7939 -0.2624 0.0232  -0.1861 52  ASN L CG  
8501  O OD1 . ASN D 46  ? 3.4716 3.2339 2.8895 -0.3011 0.0398  -0.1937 52  ASN L OD1 
8502  N ND2 . ASN D 46  ? 3.3590 3.0432 2.7793 -0.2217 -0.0088 -0.1875 52  ASN L ND2 
8503  N N   . ASP D 47  ? 3.2269 3.1097 2.5661 -0.3485 0.1037  -0.0457 53  ASP L N   
8504  C CA  . ASP D 47  ? 3.1919 3.0820 2.4693 -0.3638 0.1097  0.0221  53  ASP L CA  
8505  C C   . ASP D 47  ? 3.1588 3.0890 2.4162 -0.4169 0.1364  0.0314  53  ASP L C   
8506  O O   . ASP D 47  ? 3.0918 3.0712 2.3707 -0.4473 0.1640  0.0159  53  ASP L O   
8507  C CB  . ASP D 47  ? 3.0763 2.9876 2.3418 -0.3537 0.1184  0.0614  53  ASP L CB  
8508  C CG  . ASP D 47  ? 3.0031 2.8714 2.2777 -0.3003 0.0904  0.0625  53  ASP L CG  
8509  O OD1 . ASP D 47  ? 3.1503 2.9681 2.4207 -0.2711 0.0624  0.0536  53  ASP L OD1 
8510  O OD2 . ASP D 47  ? 2.9555 2.8410 2.2424 -0.2877 0.0965  0.0714  53  ASP L OD2 
8511  N N   . ARG D 48  ? 3.0529 2.9632 2.2745 -0.4269 0.1283  0.0521  54  ARG L N   
8512  C CA  . ARG D 48  ? 3.0999 3.0371 2.2952 -0.4736 0.1474  0.0650  54  ARG L CA  
8513  C C   . ARG D 48  ? 3.0732 3.0274 2.2091 -0.4918 0.1579  0.1369  54  ARG L C   
8514  O O   . ARG D 48  ? 3.0904 3.0117 2.1918 -0.4650 0.1386  0.1788  54  ARG L O   
8515  C CB  . ARG D 48  ? 3.2040 3.1023 2.3978 -0.4712 0.1282  0.0401  54  ARG L CB  
8516  C CG  . ARG D 48  ? 3.2310 3.0870 2.4649 -0.4290 0.1024  -0.0055 54  ARG L CG  
8517  C CD  . ARG D 48  ? 3.3870 3.1945 2.6045 -0.4183 0.0775  -0.0112 54  ARG L CD  
8518  N NE  . ARG D 48  ? 3.4713 3.2658 2.6351 -0.4144 0.0706  0.0509  54  ARG L NE  
8519  C CZ  . ARG D 48  ? 3.5538 3.3145 2.6855 -0.4089 0.0533  0.0726  54  ARG L CZ  
8520  N NH1 . ARG D 48  ? 3.6585 3.3937 2.8050 -0.4069 0.0406  0.0374  54  ARG L NH1 
8521  N NH2 . ARG D 48  ? 3.6061 3.3588 2.6893 -0.4060 0.0490  0.1315  54  ARG L NH2 
8522  N N   . PRO D 49  ? 3.2055 3.2102 2.3300 -0.5372 0.1881  0.1496  55  PRO L N   
8523  C CA  . PRO D 49  ? 3.1878 3.2137 2.2566 -0.5603 0.2012  0.2161  55  PRO L CA  
8524  C C   . PRO D 49  ? 3.2835 3.2847 2.3083 -0.5728 0.1903  0.2442  55  PRO L C   
8525  O O   . PRO D 49  ? 3.3621 3.3256 2.3974 -0.5602 0.1702  0.2144  55  PRO L O   
8526  C CB  . PRO D 49  ? 3.1295 3.2182 2.2097 -0.6054 0.2374  0.2088  55  PRO L CB  
8527  C CG  . PRO D 49  ? 3.1652 3.2582 2.2935 -0.6163 0.2410  0.1408  55  PRO L CG  
8528  C CD  . PRO D 49  ? 3.1833 3.2300 2.3479 -0.5691 0.2127  0.1018  55  PRO L CD  
8529  N N   . SER D 50  ? 3.5330 3.5557 2.5085 -0.5980 0.2036  0.3019  56  SER L N   
8530  C CA  . SER D 50  ? 3.7234 3.7255 2.6545 -0.6121 0.1944  0.3337  56  SER L CA  
8531  C C   . SER D 50  ? 3.8750 3.8956 2.8192 -0.6512 0.2077  0.2970  56  SER L C   
8532  O O   . SER D 50  ? 3.7953 3.8645 2.7538 -0.6858 0.2358  0.2828  56  SER L O   
8533  C CB  . SER D 50  ? 3.6112 3.6344 2.4877 -0.6296 0.2066  0.4055  56  SER L CB  
8534  O OG  . SER D 50  ? 3.4664 3.5482 2.3456 -0.6684 0.2399  0.4105  56  SER L OG  
8535  N N   . GLY D 51  ? 3.4492 3.4309 2.3888 -0.6454 0.1875  0.2811  57  GLY L N   
8536  C CA  . GLY D 51  ? 3.5311 3.5261 2.4818 -0.6804 0.1977  0.2459  57  GLY L CA  
8537  C C   . GLY D 51  ? 3.6179 3.5906 2.6208 -0.6634 0.1855  0.1753  57  GLY L C   
8538  O O   . GLY D 51  ? 3.7132 3.6870 2.7243 -0.6871 0.1886  0.1441  57  GLY L O   
8539  N N   . ILE D 52  ? 3.4730 3.4259 2.5114 -0.6236 0.1718  0.1487  58  ILE L N   
8540  C CA  . ILE D 52  ? 3.4287 3.3615 2.5197 -0.6056 0.1604  0.0806  58  ILE L CA  
8541  C C   . ILE D 52  ? 3.4776 3.3474 2.5648 -0.5661 0.1247  0.0752  58  ILE L C   
8542  O O   . ILE D 52  ? 3.4575 3.2995 2.5297 -0.5306 0.1068  0.1058  58  ILE L O   
8543  C CB  . ILE D 52  ? 3.3078 3.2603 2.4456 -0.5877 0.1687  0.0494  58  ILE L CB  
8544  C CG1 . ILE D 52  ? 3.2316 3.2469 2.3703 -0.6261 0.2043  0.0600  58  ILE L CG1 
8545  C CG2 . ILE D 52  ? 3.3335 3.2686 2.5271 -0.5723 0.1589  -0.0222 58  ILE L CG2 
8546  C CD1 . ILE D 52  ? 3.2732 3.3208 2.4209 -0.6711 0.2257  0.0307  58  ILE L CD1 
8547  N N   . PRO D 53  ? 3.4328 3.2792 2.5332 -0.5709 0.1137  0.0372  59  PRO L N   
8548  C CA  . PRO D 53  ? 3.5799 3.3665 2.6791 -0.5353 0.0800  0.0278  59  PRO L CA  
8549  C C   . PRO D 53  ? 3.5560 3.3140 2.6972 -0.4885 0.0611  -0.0078 59  PRO L C   
8550  O O   . PRO D 53  ? 3.3940 3.1777 2.5732 -0.4844 0.0738  -0.0359 59  PRO L O   
8551  C CB  . PRO D 53  ? 3.6001 3.3808 2.7105 -0.5596 0.0798  -0.0122 59  PRO L CB  
8552  C CG  . PRO D 53  ? 3.5162 3.3494 2.6557 -0.5947 0.1105  -0.0456 59  PRO L CG  
8553  C CD  . PRO D 53  ? 3.3953 3.2720 2.5110 -0.6123 0.1337  0.0016  59  PRO L CD  
8554  N N   . ASP D 54  ? 3.6753 3.3782 2.8098 -0.4516 0.0296  -0.0061 60  ASP L N   
8555  C CA  . ASP D 54  ? 3.7128 3.3846 2.8849 -0.4048 0.0093  -0.0379 60  ASP L CA  
8556  C C   . ASP D 54  ? 3.7556 3.4204 2.9820 -0.4019 0.0060  -0.1110 60  ASP L C   
8557  O O   . ASP D 54  ? 3.7883 3.4251 3.0498 -0.3640 -0.0120 -0.1441 60  ASP L O   
8558  C CB  . ASP D 54  ? 3.8664 3.4799 3.0137 -0.3647 -0.0242 -0.0127 60  ASP L CB  
8559  C CG  . ASP D 54  ? 3.7935 3.4052 2.8799 -0.3729 -0.0247 0.0590  60  ASP L CG  
8560  O OD1 . ASP D 54  ? 3.7067 3.3561 2.7732 -0.3903 -0.0041 0.0963  60  ASP L OD1 
8561  O OD2 . ASP D 54  ? 3.8153 3.3861 2.8743 -0.3597 -0.0466 0.0786  60  ASP L OD2 
8562  N N   . ARG D 55  ? 3.6933 3.3826 2.9263 -0.4414 0.0229  -0.1362 61  ARG L N   
8563  C CA  . ARG D 55  ? 3.7270 3.4152 3.0108 -0.4439 0.0233  -0.2059 61  ARG L CA  
8564  C C   . ARG D 55  ? 3.6764 3.4005 3.0080 -0.4434 0.0415  -0.2414 61  ARG L C   
8565  O O   . ARG D 55  ? 3.7209 3.4344 3.1016 -0.4277 0.0350  -0.2987 61  ARG L O   
8566  C CB  . ARG D 55  ? 3.6843 3.3897 2.9548 -0.4879 0.0371  -0.2155 61  ARG L CB  
8567  C CG  . ARG D 55  ? 3.7301 3.3980 2.9543 -0.4871 0.0177  -0.1799 61  ARG L CG  
8568  C CD  . ARG D 55  ? 3.8797 3.5567 3.0913 -0.5267 0.0265  -0.1921 61  ARG L CD  
8569  N NE  . ARG D 55  ? 3.8735 3.6054 3.0669 -0.5732 0.0588  -0.1709 61  ARG L NE  
8570  C CZ  . ARG D 55  ? 3.8484 3.6215 3.0709 -0.6029 0.0836  -0.2089 61  ARG L CZ  
8571  N NH1 . ARG D 55  ? 3.7619 3.5291 3.0358 -0.5918 0.0807  -0.2726 61  ARG L NH1 
8572  N NH2 . ARG D 55  ? 3.9177 3.7384 3.1174 -0.6443 0.1115  -0.1824 61  ARG L NH2 
8573  N N   . PHE D 56  ? 3.7405 3.5065 3.0585 -0.4600 0.0638  -0.2077 62  PHE L N   
8574  C CA  . PHE D 56  ? 3.6500 3.4543 3.0101 -0.4624 0.0831  -0.2354 62  PHE L CA  
8575  C C   . PHE D 56  ? 3.5724 3.3583 2.9449 -0.4188 0.0682  -0.2250 62  PHE L C   
8576  O O   . PHE D 56  ? 3.4582 3.2431 2.7933 -0.4103 0.0662  -0.1702 62  PHE L O   
8577  C CB  . PHE D 56  ? 3.4367 3.2994 2.7769 -0.5073 0.1172  -0.2071 62  PHE L CB  
8578  C CG  . PHE D 56  ? 3.5819 3.4644 2.9127 -0.5502 0.1326  -0.2207 62  PHE L CG  
8579  C CD1 . PHE D 56  ? 3.6442 3.5168 2.9231 -0.5693 0.1294  -0.1784 62  PHE L CD1 
8580  C CD2 . PHE D 56  ? 3.6099 3.5157 2.9847 -0.5686 0.1473  -0.2782 62  PHE L CD2 
8581  C CE1 . PHE D 56  ? 3.7514 3.6398 3.0209 -0.6081 0.1421  -0.1912 62  PHE L CE1 
8582  C CE2 . PHE D 56  ? 3.7165 3.6381 3.0817 -0.6069 0.1602  -0.2915 62  PHE L CE2 
8583  C CZ  . PHE D 56  ? 3.8114 3.7240 3.1237 -0.6267 0.1574  -0.2481 62  PHE L CZ  
8584  N N   . SER D 57  ? 3.6052 3.3773 3.0304 -0.3917 0.0582  -0.2775 63  SER L N   
8585  C CA  . SER D 57  ? 3.3820 3.1362 2.8256 -0.3495 0.0435  -0.2756 63  SER L CA  
8586  C C   . SER D 57  ? 3.3346 3.1221 2.8355 -0.3521 0.0598  -0.3232 63  SER L C   
8587  O O   . SER D 57  ? 3.4103 3.2130 2.9460 -0.3710 0.0703  -0.3724 63  SER L O   
8588  C CB  . SER D 57  ? 3.4151 3.1067 2.8657 -0.3039 0.0072  -0.2912 63  SER L CB  
8589  O OG  . SER D 57  ? 3.5796 3.2403 2.9818 -0.3049 -0.0075 -0.2549 63  SER L OG  
8590  N N   . GLY D 58  ? 3.3124 3.1099 2.8235 -0.3317 0.0612  -0.3086 64  GLY L N   
8591  C CA  . GLY D 58  ? 3.2771 3.1065 2.8419 -0.3323 0.0762  -0.3494 64  GLY L CA  
8592  C C   . GLY D 58  ? 3.2916 3.0888 2.8909 -0.2835 0.0531  -0.3712 64  GLY L C   
8593  O O   . GLY D 58  ? 3.2998 3.0586 2.8732 -0.2502 0.0298  -0.3398 64  GLY L O   
8594  N N   . SER D 59  ? 3.2929 3.1050 2.9504 -0.2785 0.0591  -0.4245 65  SER L N   
8595  C CA  . SER D 59  ? 3.2103 2.9931 2.9033 -0.2326 0.0374  -0.4471 65  SER L CA  
8596  C C   . SER D 59  ? 3.0659 2.8600 2.7422 -0.2174 0.0395  -0.4032 65  SER L C   
8597  O O   . SER D 59  ? 2.8811 2.7233 2.5494 -0.2462 0.0665  -0.3804 65  SER L O   
8598  C CB  . SER D 59  ? 3.1828 2.9841 2.9430 -0.2334 0.0458  -0.5126 65  SER L CB  
8599  O OG  . SER D 59  ? 3.0757 2.8650 2.8702 -0.1962 0.0331  -0.5265 65  SER L OG  
8600  N N   . PRO D 60  ? 3.2107 2.9610 2.8809 -0.1725 0.0115  -0.3900 66  PRO L N   
8601  C CA  . PRO D 60  ? 3.1305 2.8877 2.7842 -0.1548 0.0114  -0.3485 66  PRO L CA  
8602  C C   . PRO D 60  ? 3.0282 2.8233 2.7315 -0.1572 0.0282  -0.3766 66  PRO L C   
8603  O O   . PRO D 60  ? 3.0838 2.8777 2.8418 -0.1489 0.0256  -0.4332 66  PRO L O   
8604  C CB  . PRO D 60  ? 3.1992 2.8956 2.8451 -0.1031 -0.0252 -0.3425 66  PRO L CB  
8605  C CG  . PRO D 60  ? 3.2168 2.8822 2.9003 -0.0898 -0.0419 -0.3999 66  PRO L CG  
8606  C CD  . PRO D 60  ? 3.2553 2.9465 2.9330 -0.1349 -0.0219 -0.4130 66  PRO L CD  
8607  N N   . GLY D 61  ? 2.8753 2.7047 2.5596 -0.1690 0.0458  -0.3365 67  GLY L N   
8608  C CA  . GLY D 61  ? 2.8478 2.7146 2.5770 -0.1720 0.0623  -0.3589 67  GLY L CA  
8609  C C   . GLY D 61  ? 2.8413 2.6776 2.5909 -0.1238 0.0389  -0.3627 67  GLY L C   
8610  O O   . GLY D 61  ? 2.8149 2.6760 2.5735 -0.1201 0.0487  -0.3478 67  GLY L O   
8611  N N   . SER D 62  A 2.9547 2.7365 2.7116 -0.0862 0.0074  -0.3828 67  SER L N   
8612  C CA  . SER D 62  A 2.9956 2.7426 2.7728 -0.0376 -0.0180 -0.3904 67  SER L CA  
8613  C C   . SER D 62  A 3.0657 2.7914 2.9039 -0.0155 -0.0329 -0.4571 67  SER L C   
8614  O O   . SER D 62  A 2.9879 2.6868 2.8513 0.0245  -0.0534 -0.4710 67  SER L O   
8615  C CB  . SER D 62  A 3.0038 2.6991 2.7310 -0.0051 -0.0461 -0.3486 67  SER L CB  
8616  O OG  . SER D 62  A 2.9495 2.6617 2.6173 -0.0270 -0.0332 -0.2868 67  SER L OG  
8617  N N   . THR D 63  B 3.0468 2.7826 2.9087 -0.0397 -0.0236 -0.4980 67  THR L N   
8618  C CA  . THR D 63  B 3.1347 2.8538 3.0558 -0.0225 -0.0353 -0.5631 67  THR L CA  
8619  C C   . THR D 63  B 3.0238 2.7928 2.9976 -0.0422 -0.0104 -0.5971 67  THR L C   
8620  O O   . THR D 63  B 2.9398 2.7562 2.9112 -0.0855 0.0196  -0.5950 67  THR L O   
8621  C CB  . THR D 63  B 3.1831 2.8852 3.1013 -0.0374 -0.0390 -0.5896 67  THR L CB  
8622  O OG1 . THR D 63  B 3.2765 2.9373 3.1407 -0.0238 -0.0591 -0.5511 67  THR L OG1 
8623  C CG2 . THR D 63  B 3.1888 2.8648 3.1643 -0.0129 -0.0561 -0.6540 67  THR L CG2 
8624  N N   . PHE D 64  C 3.0539 2.8126 3.0751 -0.0108 -0.0227 -0.6280 67  PHE L N   
8625  C CA  . PHE D 64  C 2.8817 2.6852 2.9558 -0.0247 -0.0015 -0.6597 67  PHE L CA  
8626  C C   . PHE D 64  C 2.9066 2.7072 3.0369 -0.0262 -0.0028 -0.7267 67  PHE L C   
8627  O O   . PHE D 64  C 2.9778 2.7345 3.1334 0.0099  -0.0300 -0.7585 67  PHE L O   
8628  C CB  . PHE D 64  C 2.8480 2.6461 2.9413 0.0083  -0.0123 -0.6515 67  PHE L CB  
8629  C CG  . PHE D 64  C 2.7695 2.5653 2.8072 0.0144  -0.0139 -0.5861 67  PHE L CG  
8630  C CD1 . PHE D 64  C 2.7126 2.5428 2.7037 -0.0240 0.0104  -0.5415 67  PHE L CD1 
8631  C CD2 . PHE D 64  C 2.7068 2.4672 2.7390 0.0581  -0.0391 -0.5691 67  PHE L CD2 
8632  C CE1 . PHE D 64  C 2.6244 2.4535 2.5643 -0.0189 0.0095  -0.4808 67  PHE L CE1 
8633  C CE2 . PHE D 64  C 2.6504 2.4093 2.6310 0.0638  -0.0400 -0.5086 67  PHE L CE2 
8634  C CZ  . PHE D 64  C 2.5797 2.3732 2.5143 0.0252  -0.0155 -0.4643 67  PHE L CZ  
8635  N N   . GLY D 65  ? 2.8190 2.6661 2.9684 -0.0673 0.0265  -0.7477 68  GLY L N   
8636  C CA  . GLY D 65  ? 2.9016 2.7528 3.1040 -0.0734 0.0296  -0.8102 68  GLY L CA  
8637  C C   . GLY D 65  ? 3.0351 2.8813 3.2179 -0.0992 0.0344  -0.8219 68  GLY L C   
8638  O O   . GLY D 65  ? 3.1410 2.9758 3.3632 -0.0958 0.0290  -0.8740 68  GLY L O   
8639  N N   . THR D 66  ? 3.0729 2.9273 3.1971 -0.1248 0.0443  -0.7754 69  THR L N   
8640  C CA  . THR D 66  ? 3.0943 2.9442 3.1946 -0.1509 0.0489  -0.7810 69  THR L CA  
8641  C C   . THR D 66  ? 3.0055 2.9095 3.0788 -0.2012 0.0837  -0.7539 69  THR L C   
8642  O O   . THR D 66  ? 2.8955 2.8318 2.9529 -0.2125 0.0998  -0.7171 69  THR L O   
8643  C CB  . THR D 66  ? 3.1416 2.9387 3.1908 -0.1300 0.0218  -0.7489 69  THR L CB  
8644  O OG1 . THR D 66  ? 3.1405 2.9387 3.1416 -0.1251 0.0211  -0.6869 69  THR L OG1 
8645  C CG2 . THR D 66  ? 3.0913 2.8333 3.1687 -0.0822 -0.0126 -0.7817 69  THR L CG2 
8646  N N   . THR D 67  ? 3.0652 2.9786 3.1331 -0.2313 0.0949  -0.7726 70  THR L N   
8647  C CA  . THR D 67  ? 2.9959 2.9587 3.0380 -0.2801 0.1272  -0.7504 70  THR L CA  
8648  C C   . THR D 67  ? 3.0284 2.9760 3.0001 -0.2907 0.1227  -0.6932 70  THR L C   
8649  O O   . THR D 67  ? 3.1183 3.0159 3.0648 -0.2646 0.0951  -0.6810 70  THR L O   
8650  C CB  . THR D 67  ? 2.9676 2.9498 3.0384 -0.3088 0.1428  -0.7992 70  THR L CB  
8651  O OG1 . THR D 67  ? 3.0606 2.9962 3.1205 -0.2964 0.1200  -0.8167 70  THR L OG1 
8652  C CG2 . THR D 67  ? 2.9410 2.9429 3.0822 -0.3011 0.1500  -0.8547 70  THR L CG2 
8653  N N   . ALA D 68  ? 2.9846 2.9765 2.9248 -0.3294 0.1501  -0.6573 71  ALA L N   
8654  C CA  . ALA D 68  ? 3.0073 2.9900 2.8809 -0.3437 0.1488  -0.6019 71  ALA L CA  
8655  C C   . ALA D 68  ? 3.1423 3.1022 3.0013 -0.3570 0.1416  -0.6200 71  ALA L C   
8656  O O   . ALA D 68  ? 3.1859 3.1708 3.0684 -0.3850 0.1589  -0.6568 71  ALA L O   
8657  C CB  . ALA D 68  ? 2.8711 2.9096 2.7184 -0.3842 0.1815  -0.5633 71  ALA L CB  
8658  N N   . THR D 69  ? 2.9868 2.8988 2.8070 -0.3364 0.1159  -0.5940 72  THR L N   
8659  C CA  . THR D 69  ? 3.0559 2.9393 2.8610 -0.3439 0.1047  -0.6092 72  THR L CA  
8660  C C   . THR D 69  ? 3.1356 3.0119 2.8731 -0.3610 0.1041  -0.5506 72  THR L C   
8661  O O   . THR D 69  ? 3.2080 3.0634 2.9108 -0.3398 0.0903  -0.5042 72  THR L O   
8662  C CB  . THR D 69  ? 3.1136 2.9392 2.9422 -0.2994 0.0704  -0.6419 72  THR L CB  
8663  O OG1 . THR D 69  ? 3.0860 2.9193 2.9787 -0.2836 0.0711  -0.6959 72  THR L OG1 
8664  C CG2 . THR D 69  ? 3.2148 3.0121 3.0312 -0.3081 0.0595  -0.6612 72  THR L CG2 
8665  N N   . LEU D 70  ? 3.2041 3.0979 2.9233 -0.3991 0.1191  -0.5532 73  LEU L N   
8666  C CA  . LEU D 70  ? 3.2915 3.1805 2.9488 -0.4204 0.1201  -0.5025 73  LEU L CA  
8667  C C   . LEU D 70  ? 3.4775 3.3214 3.1250 -0.4131 0.0980  -0.5210 73  LEU L C   
8668  O O   . LEU D 70  ? 3.5793 3.4299 3.2511 -0.4314 0.1049  -0.5653 73  LEU L O   
8669  C CB  . LEU D 70  ? 3.1992 3.1446 2.8397 -0.4719 0.1549  -0.4872 73  LEU L CB  
8670  C CG  . LEU D 70  ? 3.2042 3.1491 2.7808 -0.4974 0.1581  -0.4338 73  LEU L CG  
8671  C CD1 . LEU D 70  ? 3.1573 3.0864 2.6922 -0.4767 0.1466  -0.3726 73  LEU L CD1 
8672  C CD2 . LEU D 70  ? 3.1898 3.1908 2.7549 -0.5485 0.1928  -0.4255 73  LEU L CD2 
8673  N N   . THR D 71  ? 3.3062 3.1043 2.9186 -0.3862 0.0717  -0.4875 74  THR L N   
8674  C CA  . THR D 71  ? 3.4092 3.1605 3.0102 -0.3753 0.0480  -0.5008 74  THR L CA  
8675  C C   . THR D 71  ? 3.4572 3.2136 3.0007 -0.4074 0.0549  -0.4555 74  THR L C   
8676  O O   . THR D 71  ? 3.4276 3.1908 2.9276 -0.4108 0.0579  -0.3977 74  THR L O   
8677  C CB  . THR D 71  ? 3.4311 3.1266 3.0299 -0.3241 0.0136  -0.4929 74  THR L CB  
8678  O OG1 . THR D 71  ? 3.3805 3.0711 3.0336 -0.2942 0.0068  -0.5354 74  THR L OG1 
8679  C CG2 . THR D 71  ? 3.5374 3.1846 3.1244 -0.3130 -0.0108 -0.5059 74  THR L CG2 
8680  N N   . ILE D 72  ? 3.5657 3.3185 3.1090 -0.4307 0.0570  -0.4814 75  ILE L N   
8681  C CA  . ILE D 72  ? 3.5747 3.3316 3.0663 -0.4627 0.0629  -0.4431 75  ILE L CA  
8682  C C   . ILE D 72  ? 3.7244 3.4281 3.2054 -0.4464 0.0350  -0.4552 75  ILE L C   
8683  O O   . ILE D 72  ? 3.8227 3.5194 3.3301 -0.4549 0.0336  -0.5037 75  ILE L O   
8684  C CB  . ILE D 72  ? 3.4305 3.2383 2.9262 -0.5126 0.0949  -0.4584 75  ILE L CB  
8685  C CG1 . ILE D 72  ? 3.1164 2.9774 2.6282 -0.5274 0.1228  -0.4516 75  ILE L CG1 
8686  C CG2 . ILE D 72  ? 3.4564 3.2677 2.8971 -0.5454 0.1002  -0.4165 75  ILE L CG2 
8687  C CD1 . ILE D 72  ? 3.0852 2.9975 2.6042 -0.5749 0.1549  -0.4689 75  ILE L CD1 
8688  N N   . THR D 73  ? 3.5958 3.2620 3.0386 -0.4228 0.0127  -0.4110 76  THR L N   
8689  C CA  . THR D 73  ? 3.7461 3.3608 3.1740 -0.4066 -0.0146 -0.4151 76  THR L CA  
8690  C C   . THR D 73  ? 3.9172 3.5416 3.3027 -0.4464 -0.0053 -0.3894 76  THR L C   
8691  O O   . THR D 73  ? 3.8457 3.5080 3.1999 -0.4782 0.0167  -0.3496 76  THR L O   
8692  C CB  . THR D 73  ? 3.6522 3.2228 3.0562 -0.3641 -0.0422 -0.3772 76  THR L CB  
8693  O OG1 . THR D 73  ? 3.6093 3.1972 2.9628 -0.3774 -0.0329 -0.3103 76  THR L OG1 
8694  C CG2 . THR D 73  ? 3.4610 3.0221 2.9062 -0.3244 -0.0517 -0.4015 76  THR L CG2 
8695  N N   . SER D 74  ? 3.8275 3.4173 3.2123 -0.4447 -0.0224 -0.4124 77  SER L N   
8696  C CA  . SER D 74  ? 3.9285 3.5225 3.2757 -0.4809 -0.0165 -0.3929 77  SER L CA  
8697  C C   . SER D 74  ? 3.8001 3.4513 3.1517 -0.5293 0.0180  -0.4035 77  SER L C   
8698  O O   . SER D 74  ? 3.7769 3.4594 3.0907 -0.5599 0.0361  -0.3585 77  SER L O   
8699  C CB  . SER D 74  ? 3.9402 3.5185 3.2288 -0.4786 -0.0262 -0.3225 77  SER L CB  
8700  O OG  . SER D 74  ? 3.9822 3.5565 3.2359 -0.5089 -0.0255 -0.3054 77  SER L OG  
8701  N N   . VAL D 75  ? 3.7216 3.3861 3.1215 -0.5349 0.0268  -0.4649 78  VAL L N   
8702  C CA  . VAL D 75  ? 3.6911 3.4094 3.1034 -0.5774 0.0593  -0.4841 78  VAL L CA  
8703  C C   . VAL D 75  ? 3.7693 3.4942 3.1444 -0.6167 0.0668  -0.4685 78  VAL L C   
8704  O O   . VAL D 75  ? 3.8678 3.5569 3.2388 -0.6130 0.0485  -0.4862 78  VAL L O   
8705  C CB  . VAL D 75  ? 3.6868 3.4119 3.1602 -0.5708 0.0639  -0.5555 78  VAL L CB  
8706  C CG1 . VAL D 75  ? 3.6584 3.4408 3.1447 -0.6135 0.0985  -0.5733 78  VAL L CG1 
8707  C CG2 . VAL D 75  ? 3.6102 3.3249 3.1205 -0.5298 0.0539  -0.5705 78  VAL L CG2 
8708  N N   . GLU D 76  ? 3.7067 3.4776 3.0547 -0.6548 0.0934  -0.4353 79  GLU L N   
8709  C CA  . GLU D 76  ? 3.8852 3.6677 3.1966 -0.6952 0.1032  -0.4178 79  GLU L CA  
8710  C C   . GLU D 76  ? 3.9142 3.7496 3.2437 -0.7359 0.1355  -0.4464 79  GLU L C   
8711  O O   . GLU D 76  ? 3.8466 3.7148 3.2111 -0.7354 0.1531  -0.4694 79  GLU L O   
8712  C CB  . GLU D 76  ? 3.8103 3.6025 3.0646 -0.7091 0.1073  -0.3443 79  GLU L CB  
8713  C CG  . GLU D 76  ? 3.8869 3.6430 3.1185 -0.6715 0.0838  -0.3007 79  GLU L CG  
8714  C CD  . GLU D 76  ? 3.9423 3.7060 3.1141 -0.6912 0.0876  -0.2306 79  GLU L CD  
8715  O OE1 . GLU D 76  ? 3.9370 3.7374 3.0877 -0.7342 0.1102  -0.2169 79  GLU L OE1 
8716  O OE2 . GLU D 76  ? 3.9642 3.6980 3.1103 -0.6637 0.0686  -0.1890 79  GLU L OE2 
8717  N N   . ALA D 77  ? 3.9621 3.8048 3.2674 -0.7714 0.1429  -0.4451 80  ALA L N   
8718  C CA  . ALA D 77  ? 3.8790 3.7700 3.1973 -0.8120 0.1731  -0.4716 80  ALA L CA  
8719  C C   . ALA D 77  ? 3.7808 3.7241 3.0841 -0.8343 0.2011  -0.4338 80  ALA L C   
8720  O O   . ALA D 77  ? 3.6906 3.6790 3.0175 -0.8582 0.2279  -0.4589 80  ALA L O   
8721  C CB  . ALA D 77  ? 3.9023 3.7881 3.1918 -0.8449 0.1735  -0.4716 80  ALA L CB  
8722  N N   . GLY D 78  ? 4.0770 4.0145 3.3410 -0.8264 0.1951  -0.3729 81  GLY L N   
8723  C CA  . GLY D 78  ? 3.8363 3.8190 3.0813 -0.8446 0.2190  -0.3304 81  GLY L CA  
8724  C C   . GLY D 78  ? 3.6244 3.6267 2.9102 -0.8228 0.2275  -0.3485 81  GLY L C   
8725  O O   . GLY D 78  ? 3.3687 3.4164 2.6503 -0.8416 0.2523  -0.3270 81  GLY L O   
8726  N N   . ASP D 79  ? 3.8323 3.8002 3.1568 -0.7830 0.2068  -0.3863 82  ASP L N   
8727  C CA  . ASP D 79  ? 3.7123 3.6895 3.0804 -0.7556 0.2091  -0.4090 82  ASP L CA  
8728  C C   . ASP D 79  ? 3.6887 3.7024 3.1065 -0.7717 0.2313  -0.4662 82  ASP L C   
8729  O O   . ASP D 79  ? 3.6172 3.6428 3.0749 -0.7518 0.2354  -0.4883 82  ASP L O   
8730  C CB  . ASP D 79  ? 3.7324 3.6541 3.1201 -0.7054 0.1756  -0.4256 82  ASP L CB  
8731  C CG  . ASP D 79  ? 3.7406 3.6265 3.0822 -0.6846 0.1535  -0.3683 82  ASP L CG  
8732  O OD1 . ASP D 79  ? 3.6910 3.6002 2.9930 -0.7015 0.1658  -0.3135 82  ASP L OD1 
8733  O OD2 . ASP D 79  ? 3.8030 3.6376 3.1479 -0.6511 0.1239  -0.3779 82  ASP L OD2 
8734  N N   . GLU D 80  ? 3.7384 3.7706 3.1549 -0.8069 0.2457  -0.4899 83  GLU L N   
8735  C CA  . GLU D 80  ? 3.7285 3.7954 3.1900 -0.8247 0.2674  -0.5448 83  GLU L CA  
8736  C C   . GLU D 80  ? 3.5255 3.6511 2.9909 -0.8475 0.2993  -0.5271 83  GLU L C   
8737  O O   . GLU D 80  ? 3.4826 3.6440 2.9178 -0.8867 0.3216  -0.5015 83  GLU L O   
8738  C CB  . GLU D 80  ? 3.8589 3.9282 3.3063 -0.8583 0.2735  -0.5640 83  GLU L CB  
8739  C CG  . GLU D 80  ? 3.8422 3.9444 3.3298 -0.8803 0.2953  -0.6204 83  GLU L CG  
8740  C CD  . GLU D 80  ? 3.9016 3.9666 3.4263 -0.8591 0.2761  -0.6796 83  GLU L CD  
8741  O OE1 . GLU D 80  ? 3.9442 3.9601 3.4509 -0.8413 0.2487  -0.6743 83  GLU L OE1 
8742  O OE2 . GLU D 80  ? 3.7901 3.8753 3.3621 -0.8605 0.2888  -0.7313 83  GLU L OE2 
8743  N N   . ALA D 81  ? 3.5068 3.6430 3.0102 -0.8234 0.3020  -0.5413 84  ALA L N   
8744  C CA  . ALA D 81  ? 3.4047 3.5959 2.9149 -0.8428 0.3316  -0.5256 84  ALA L CA  
8745  C C   . ALA D 81  ? 3.3302 3.5292 2.8968 -0.8153 0.3328  -0.5619 84  ALA L C   
8746  O O   . ALA D 81  ? 3.3592 3.5229 2.9613 -0.7830 0.3120  -0.6022 84  ALA L O   
8747  C CB  . ALA D 81  ? 3.3558 3.5543 2.8183 -0.8450 0.3332  -0.4557 84  ALA L CB  
8748  N N   . ASP D 82  ? 3.1858 3.4324 2.7601 -0.8293 0.3578  -0.5463 85  ASP L N   
8749  C CA  . ASP D 82  ? 3.1408 3.4039 2.7641 -0.8080 0.3634  -0.5706 85  ASP L CA  
8750  C C   . ASP D 82  ? 3.1011 3.3478 2.7070 -0.7781 0.3493  -0.5250 85  ASP L C   
8751  O O   . ASP D 82  ? 3.0837 3.3326 2.6390 -0.7886 0.3504  -0.4682 85  ASP L O   
8752  C CB  . ASP D 82  ? 2.9861 3.3132 2.6271 -0.8428 0.4003  -0.5791 85  ASP L CB  
8753  C CG  . ASP D 82  ? 3.0883 3.4330 2.7585 -0.8663 0.4146  -0.6332 85  ASP L CG  
8754  O OD1 . ASP D 82  ? 3.2225 3.5321 2.9202 -0.8462 0.3959  -0.6778 85  ASP L OD1 
8755  O OD2 . ASP D 82  ? 3.0384 3.4314 2.7027 -0.9050 0.4443  -0.6303 85  ASP L OD2 
8756  N N   . TYR D 83  ? 3.1665 3.3963 2.8142 -0.7405 0.3358  -0.5499 86  TYR L N   
8757  C CA  . TYR D 83  ? 3.0951 3.3063 2.7315 -0.7079 0.3205  -0.5124 86  TYR L CA  
8758  C C   . TYR D 83  ? 3.0427 3.2826 2.7251 -0.6951 0.3324  -0.5305 86  TYR L C   
8759  O O   . TYR D 83  ? 3.0548 3.2903 2.7906 -0.6792 0.3289  -0.5844 86  TYR L O   
8760  C CB  . TYR D 83  ? 3.0819 3.2285 2.7141 -0.6658 0.2829  -0.5158 86  TYR L CB  
8761  C CG  . TYR D 83  ? 3.1737 3.2902 2.7539 -0.6753 0.2692  -0.4858 86  TYR L CG  
8762  C CD1 . TYR D 83  ? 3.2821 3.3846 2.8645 -0.6902 0.2655  -0.5185 86  TYR L CD1 
8763  C CD2 . TYR D 83  ? 3.2035 3.3051 2.7321 -0.6688 0.2596  -0.4236 86  TYR L CD2 
8764  C CE1 . TYR D 83  ? 3.3984 3.4730 2.9331 -0.6990 0.2525  -0.4898 86  TYR L CE1 
8765  C CE2 . TYR D 83  ? 3.3554 3.4296 2.8369 -0.6771 0.2469  -0.3944 86  TYR L CE2 
8766  C CZ  . TYR D 83  ? 3.4440 3.5048 2.9289 -0.6924 0.2432  -0.4275 86  TYR L CZ  
8767  O OH  . TYR D 83  ? 3.6080 3.6415 3.0461 -0.7009 0.2302  -0.3974 86  TYR L OH  
8768  N N   . TYR D 84  ? 3.2185 3.4870 2.8802 -0.7016 0.3460  -0.4849 87  TYR L N   
8769  C CA  . TYR D 84  ? 3.0883 3.3852 2.7876 -0.6902 0.3575  -0.4928 87  TYR L CA  
8770  C C   . TYR D 84  ? 3.0585 3.3231 2.7451 -0.6503 0.3345  -0.4590 87  TYR L C   
8771  O O   . TYR D 84  ? 3.0949 3.3276 2.7346 -0.6401 0.3171  -0.4170 87  TYR L O   
8772  C CB  . TYR D 84  ? 2.9037 3.2631 2.5915 -0.7308 0.3935  -0.4683 87  TYR L CB  
8773  C CG  . TYR D 84  ? 2.8866 3.2815 2.5895 -0.7702 0.4181  -0.5029 87  TYR L CG  
8774  C CD1 . TYR D 84  ? 2.9243 3.3177 2.6813 -0.7638 0.4179  -0.5666 87  TYR L CD1 
8775  C CD2 . TYR D 84  ? 2.8613 3.2893 2.5234 -0.8130 0.4405  -0.4720 87  TYR L CD2 
8776  C CE1 . TYR D 84  ? 2.9380 3.3628 2.7087 -0.7986 0.4400  -0.5990 87  TYR L CE1 
8777  C CE2 . TYR D 84  ? 2.8778 3.3370 2.5529 -0.8482 0.4624  -0.5044 87  TYR L CE2 
8778  C CZ  . TYR D 84  ? 2.9161 3.3734 2.6455 -0.8405 0.4620  -0.5680 87  TYR L CZ  
8779  O OH  . TYR D 84  ? 2.8964 3.3843 2.6391 -0.8744 0.4838  -0.6009 87  TYR L OH  
8780  N N   . CYS D 85  ? 2.9447 3.2178 2.6740 -0.6272 0.3345  -0.4777 88  CYS L N   
8781  C CA  . CYS D 85  ? 2.8580 3.1033 2.5806 -0.5882 0.3139  -0.4496 88  CYS L CA  
8782  C C   . CYS D 85  ? 2.7797 3.0677 2.5200 -0.5919 0.3338  -0.4355 88  CYS L C   
8783  O O   . CYS D 85  ? 2.7424 3.0708 2.5240 -0.6096 0.3561  -0.4690 88  CYS L O   
8784  C CB  . CYS D 85  ? 2.9177 3.1144 2.6793 -0.5436 0.2837  -0.4919 88  CYS L CB  
8785  S SG  . CYS D 85  ? 3.0678 3.2874 2.9107 -0.5364 0.2936  -0.5620 88  CYS L SG  
8786  N N   . HIS D 86  ? 2.8099 3.0886 2.5186 -0.5745 0.3256  -0.3853 89  HIS L N   
8787  C CA  . HIS D 86  ? 2.7376 3.0522 2.4588 -0.5743 0.3415  -0.3664 89  HIS L CA  
8788  C C   . HIS D 86  ? 2.7289 3.0073 2.4727 -0.5247 0.3154  -0.3715 89  HIS L C   
8789  O O   . HIS D 86  ? 2.7451 2.9905 2.4520 -0.5003 0.2955  -0.3307 89  HIS L O   
8790  C CB  . HIS D 86  ? 2.7126 3.0537 2.3777 -0.5989 0.3577  -0.3012 89  HIS L CB  
8791  C CG  . HIS D 86  ? 2.6378 3.0294 2.3191 -0.6124 0.3830  -0.2887 89  HIS L CG  
8792  N ND1 . HIS D 86  ? 2.6068 3.0261 2.2447 -0.6313 0.3988  -0.2313 89  HIS L ND1 
8793  C CD2 . HIS D 86  ? 2.5894 3.0083 2.3264 -0.6090 0.3948  -0.3263 89  HIS L CD2 
8794  C CE1 . HIS D 86  ? 2.5425 3.0040 2.2086 -0.6391 0.4193  -0.2344 89  HIS L CE1 
8795  N NE2 . HIS D 86  ? 2.5299 2.9923 2.2565 -0.6260 0.4173  -0.2915 89  HIS L NE2 
8796  N N   . ILE D 87  ? 2.6791 2.7186 2.8171 0.2182  0.1842  -0.2290 90  ILE L N   
8797  C CA  . ILE D 87  ? 2.6689 2.6335 2.7830 0.2070  0.1748  -0.2255 90  ILE L CA  
8798  C C   . ILE D 87  ? 2.6198 2.5548 2.6694 0.2046  0.2262  -0.1835 90  ILE L C   
8799  O O   . ILE D 87  ? 2.4800 2.4599 2.5235 0.2097  0.2673  -0.1818 90  ILE L O   
8800  C CB  . ILE D 87  ? 2.7227 2.7023 2.8858 0.2046  0.1544  -0.2737 90  ILE L CB  
8801  C CG1 . ILE D 87  ? 2.6635 2.6735 2.8926 0.2073  0.1027  -0.3165 90  ILE L CG1 
8802  C CG2 . ILE D 87  ? 2.8143 2.7168 2.9509 0.1933  0.1470  -0.2691 90  ILE L CG2 
8803  C CD1 . ILE D 87  ? 2.6047 2.5540 2.8298 0.2014  0.0562  -0.3104 90  ILE L CD1 
8804  N N   . TRP D 88  ? 2.7603 2.6189 2.7606 0.1964  0.2244  -0.1495 91  TRP L N   
8805  C CA  . TRP D 88  ? 2.7349 2.5555 2.6724 0.1926  0.2699  -0.1096 91  TRP L CA  
8806  C C   . TRP D 88  ? 2.8211 2.5672 2.7416 0.1807  0.2543  -0.1133 91  TRP L C   
8807  O O   . TRP D 88  ? 2.9046 2.5792 2.7934 0.1723  0.2360  -0.0922 91  TRP L O   
8808  C CB  . TRP D 88  ? 2.6818 2.4759 2.5683 0.1932  0.2897  -0.0611 91  TRP L CB  
8809  C CG  . TRP D 88  ? 2.6932 2.5559 2.5813 0.2050  0.3200  -0.0480 91  TRP L CG  
8810  C CD1 . TRP D 88  ? 2.7234 2.6322 2.6432 0.2126  0.3017  -0.0566 91  TRP L CD1 
8811  C CD2 . TRP D 88  ? 2.6043 2.4995 2.4620 0.2110  0.3742  -0.0258 91  TRP L CD2 
8812  N NE1 . TRP D 88  ? 2.6261 2.5927 2.5356 0.2230  0.3414  -0.0396 91  TRP L NE1 
8813  C CE2 . TRP D 88  ? 2.5488 2.5079 2.4200 0.2222  0.3861  -0.0207 91  TRP L CE2 
8814  C CE3 . TRP D 88  ? 2.5491 2.4241 2.3682 0.2078  0.4136  -0.0092 91  TRP L CE3 
8815  C CZ2 . TRP D 88  ? 2.4675 2.4694 2.3145 0.2305  0.4351  0.0003  91  TRP L CZ2 
8816  C CZ3 . TRP D 88  ? 2.4665 2.3841 2.2615 0.2158  0.4626  0.0116  91  TRP L CZ3 
8817  C CH2 . TRP D 88  ? 2.4489 2.4288 2.2576 0.2271  0.4727  0.0162  91  TRP L CH2 
8818  N N   . ASP D 89  ? 2.6848 2.4468 2.6246 0.1796  0.2630  -0.1394 92  ASP L N   
8819  C CA  . ASP D 89  ? 2.7536 2.4510 2.6835 0.1689  0.2475  -0.1479 92  ASP L CA  
8820  C C   . ASP D 89  ? 2.8037 2.4720 2.6752 0.1654  0.2975  -0.1136 92  ASP L C   
8821  O O   . ASP D 89  ? 2.7029 2.4214 2.5644 0.1722  0.3418  -0.1043 92  ASP L O   
8822  C CB  . ASP D 89  ? 2.6361 2.3678 2.6285 0.1695  0.2220  -0.2016 92  ASP L CB  
8823  C CG  . ASP D 89  ? 2.7709 2.4339 2.7691 0.1589  0.1837  -0.2187 92  ASP L CG  
8824  O OD1 . ASP D 89  ? 2.8718 2.4619 2.8170 0.1505  0.1915  -0.1873 92  ASP L OD1 
8825  O OD2 . ASP D 89  ? 2.6883 2.3694 2.7442 0.1591  0.1449  -0.2638 92  ASP L OD2 
8826  N N   . SER D 90  ? 2.8592 2.4452 2.6915 0.1546  0.2899  -0.0950 93  SER L N   
8827  C CA  . SER D 90  ? 2.7917 2.3409 2.5658 0.1501  0.3345  -0.0612 93  SER L CA  
8828  C C   . SER D 90  ? 2.8347 2.3965 2.6220 0.1483  0.3508  -0.0849 93  SER L C   
8829  O O   . SER D 90  ? 2.8046 2.3460 2.5462 0.1457  0.3921  -0.0586 93  SER L O   
8830  C CB  . SER D 90  ? 2.7120 2.1655 2.4376 0.1386  0.3198  -0.0321 93  SER L CB  
8831  O OG  . SER D 90  ? 2.6849 2.0954 2.4373 0.1306  0.2730  -0.0630 93  SER L OG  
8832  N N   . ARG D 91  ? 2.5346 2.1303 2.3829 0.1495  0.3209  -0.1336 94  ARG L N   
8833  C CA  . ARG D 91  ? 2.5318 2.1423 2.3972 0.1475  0.3354  -0.1595 94  ARG L CA  
8834  C C   . ARG D 91  ? 2.4959 2.1979 2.4024 0.1570  0.3572  -0.1865 94  ARG L C   
8835  O O   . ARG D 91  ? 2.4919 2.2136 2.4056 0.1560  0.3807  -0.2028 94  ARG L O   
8836  C CB  . ARG D 91  ? 2.5473 2.1176 2.4487 0.1398  0.2864  -0.1960 94  ARG L CB  
8837  C CG  . ARG D 91  ? 2.5864 2.0619 2.4436 0.1294  0.2660  -0.1698 94  ARG L CG  
8838  C CD  . ARG D 91  ? 2.6031 2.0384 2.4942 0.1222  0.2188  -0.2057 94  ARG L CD  
8839  N NE  . ARG D 91  ? 2.5933 2.0585 2.5132 0.1221  0.2327  -0.2369 94  ARG L NE  
8840  C CZ  . ARG D 91  ? 2.6085 2.0400 2.5545 0.1156  0.2013  -0.2676 94  ARG L CZ  
8841  N NH1 . ARG D 91  ? 2.6350 2.0006 2.5802 0.1088  0.1535  -0.2706 94  ARG L NH1 
8842  N NH2 . ARG D 91  ? 2.5984 2.0607 2.5706 0.1157  0.2176  -0.2953 94  ARG L NH2 
8843  N N   . ARG D 92  ? 2.5906 2.3463 2.5225 0.1656  0.3505  -0.1916 95  ARG L N   
8844  C CA  . ARG D 92  ? 2.5120 2.3547 2.4832 0.1746  0.3684  -0.2176 95  ARG L CA  
8845  C C   . ARG D 92  ? 2.5590 2.4361 2.4914 0.1825  0.4138  -0.1801 95  ARG L C   
8846  O O   . ARG D 92  ? 2.5345 2.3827 2.4303 0.1832  0.4159  -0.1433 95  ARG L O   
8847  C CB  . ARG D 92  ? 2.4870 2.3732 2.5265 0.1791  0.3225  -0.2595 95  ARG L CB  
8848  C CG  . ARG D 92  ? 2.5107 2.3673 2.5940 0.1722  0.2753  -0.3002 95  ARG L CG  
8849  C CD  . ARG D 92  ? 2.6708 2.5513 2.7762 0.1699  0.2941  -0.3304 95  ARG L CD  
8850  N NE  . ARG D 92  ? 2.8490 2.7144 3.0071 0.1648  0.2483  -0.3758 95  ARG L NE  
8851  C CZ  . ARG D 92  ? 2.9889 2.8709 3.1754 0.1618  0.2551  -0.4086 95  ARG L CZ  
8852  N NH1 . ARG D 92  ? 3.1103 2.9772 3.3465 0.1576  0.2108  -0.4499 95  ARG L NH1 
8853  N NH2 . ARG D 92  ? 2.9206 2.8336 3.0858 0.1630  0.3063  -0.4004 95  ARG L NH2 
8854  N N   . PRO D 93  A 2.8555 2.7938 2.7948 0.1883  0.4511  -0.1891 95  PRO L N   
8855  C CA  . PRO D 93  A 2.7930 2.7687 2.6980 0.1967  0.4941  -0.1560 95  PRO L CA  
8856  C C   . PRO D 93  A 2.7989 2.8078 2.7245 0.2045  0.4728  -0.1535 95  PRO L C   
8857  O O   . PRO D 93  A 2.7968 2.8127 2.7695 0.2044  0.4269  -0.1826 95  PRO L O   
8858  C CB  . PRO D 93  A 2.6142 2.6532 2.5369 0.2005  0.5276  -0.1793 95  PRO L CB  
8859  C CG  . PRO D 93  A 2.5916 2.6021 2.5321 0.1915  0.5165  -0.2081 95  PRO L CG  
8860  C CD  . PRO D 93  A 2.7144 2.6845 2.6875 0.1863  0.4593  -0.2279 95  PRO L CD  
8861  N N   . THR D 94  B 2.8271 2.8561 2.7158 0.2114  0.5075  -0.1176 95  THR L N   
8862  C CA  . THR D 94  B 2.7931 2.8535 2.6950 0.2193  0.4932  -0.1100 95  THR L CA  
8863  C C   . THR D 94  B 2.8078 2.9431 2.7733 0.2261  0.4744  -0.1541 95  THR L C   
8864  O O   . THR D 94  B 2.7804 2.9710 2.7566 0.2308  0.5029  -0.1686 95  THR L O   
8865  C CB  . THR D 94  B 2.6855 2.7590 2.5365 0.2261  0.5393  -0.0653 95  THR L CB  
8866  O OG1 . THR D 94  B 2.4845 2.4888 2.2755 0.2195  0.5602  -0.0248 95  THR L OG1 
8867  C CG2 . THR D 94  B 2.6844 2.7864 2.5461 0.2340  0.5257  -0.0548 95  THR L CG2 
8868  N N   . ASN D 95  C 2.6937 2.8293 2.7010 0.2260  0.4260  -0.1760 95  ASN L N   
8869  C CA  . ASN D 95  C 2.6639 2.8675 2.7342 0.2321  0.4032  -0.2185 95  ASN L CA  
8870  C C   . ASN D 95  C 2.6226 2.8806 2.6881 0.2430  0.4214  -0.2013 95  ASN L C   
8871  O O   . ASN D 95  C 2.5541 2.7959 2.6070 0.2454  0.4075  -0.1779 95  ASN L O   
8872  C CB  . ASN D 95  C 2.6445 2.8273 2.7613 0.2281  0.3438  -0.2485 95  ASN L CB  
8873  C CG  . ASN D 95  C 2.6274 2.7595 2.7549 0.2179  0.3218  -0.2700 95  ASN L CG  
8874  O OD1 . ASN D 95  C 2.6066 2.7006 2.6955 0.2122  0.3485  -0.2528 95  ASN L OD1 
8875  N ND2 . ASN D 95  C 2.5169 2.6492 2.6984 0.2157  0.2719  -0.3091 95  ASN L ND2 
8876  N N   . TRP D 96  ? 2.8545 3.1765 2.9305 0.2494  0.4520  -0.2139 96  TRP L N   
8877  C CA  . TRP D 96  ? 2.7889 3.1687 2.8618 0.2603  0.4723  -0.2010 96  TRP L CA  
8878  C C   . TRP D 96  ? 2.7286 3.1665 2.8647 0.2657  0.4384  -0.2403 96  TRP L C   
8879  O O   . TRP D 96  ? 2.6674 3.1627 2.8102 0.2749  0.4529  -0.2384 96  TRP L O   
8880  C CB  . TRP D 96  ? 2.6991 3.1137 2.7435 0.2640  0.5257  -0.1912 96  TRP L CB  
8881  C CG  . TRP D 96  ? 2.7361 3.0987 2.7140 0.2605  0.5630  -0.1471 96  TRP L CG  
8882  C CD1 . TRP D 96  ? 2.7370 3.0550 2.6926 0.2517  0.5763  -0.1454 96  TRP L CD1 
8883  C CD2 . TRP D 96  ? 2.7673 3.1199 2.6931 0.2660  0.5933  -0.0989 96  TRP L CD2 
8884  N NE1 . TRP D 96  ? 2.7561 3.0352 2.6482 0.2511  0.6123  -0.0987 96  TRP L NE1 
8885  C CE2 . TRP D 96  ? 2.7765 3.0763 2.6497 0.2599  0.6236  -0.0697 96  TRP L CE2 
8886  C CE3 . TRP D 96  ? 2.7719 3.1548 2.6914 0.2755  0.5973  -0.0781 96  TRP L CE3 
8887  C CZ2 . TRP D 96  ? 2.8078 3.0846 2.6233 0.2630  0.6575  -0.0210 96  TRP L CZ2 
8888  C CZ3 . TRP D 96  ? 2.7273 3.0874 2.5903 0.2787  0.6307  -0.0300 96  TRP L CZ3 
8889  C CH2 . TRP D 96  ? 2.7714 3.0791 2.5834 0.2725  0.6604  -0.0021 96  TRP L CH2 
8890  N N   . VAL D 97  ? 2.4127 2.8364 2.5951 0.2601  0.3936  -0.2765 97  VAL L N   
8891  C CA  . VAL D 97  ? 2.4160 2.8887 2.6616 0.2643  0.3562  -0.3162 97  VAL L CA  
8892  C C   . VAL D 97  ? 2.4570 2.8817 2.7233 0.2592  0.3033  -0.3238 97  VAL L C   
8893  O O   . VAL D 97  ? 2.4757 2.8462 2.7411 0.2502  0.2851  -0.3316 97  VAL L O   
8894  C CB  . VAL D 97  ? 2.3945 2.9111 2.6871 0.2627  0.3558  -0.3647 97  VAL L CB  
8895  C CG1 . VAL D 97  ? 2.3969 2.9572 2.7563 0.2660  0.3132  -0.4069 97  VAL L CG1 
8896  C CG2 . VAL D 97  ? 2.3514 2.9168 2.6220 0.2672  0.4095  -0.3585 97  VAL L CG2 
8897  N N   . PHE D 98  ? 2.3408 2.7839 2.6241 0.2647  0.2789  -0.3208 98  PHE L N   
8898  C CA  . PHE D 98  ? 2.4470 2.8474 2.7504 0.2602  0.2279  -0.3286 98  PHE L CA  
8899  C C   . PHE D 98  ? 2.4603 2.8689 2.8241 0.2560  0.1886  -0.3812 98  PHE L C   
8900  O O   . PHE D 98  ? 2.3342 2.8005 2.7367 0.2592  0.1958  -0.4156 98  PHE L O   
8901  C CB  . PHE D 98  ? 2.4983 2.9267 2.8132 0.2676  0.2109  -0.3193 98  PHE L CB  
8902  C CG  . PHE D 98  ? 2.5601 2.9687 2.8174 0.2706  0.2408  -0.2669 98  PHE L CG  
8903  C CD1 . PHE D 98  ? 2.5647 2.9218 2.7634 0.2656  0.2737  -0.2301 98  PHE L CD1 
8904  C CD2 . PHE D 98  ? 2.5960 3.0362 2.8592 0.2784  0.2344  -0.2549 98  PHE L CD2 
8905  C CE1 . PHE D 98  ? 2.5829 2.9221 2.7310 0.2685  0.3004  -0.1831 98  PHE L CE1 
8906  C CE2 . PHE D 98  ? 2.6173 3.0398 2.8307 0.2812  0.2606  -0.2082 98  PHE L CE2 
8907  C CZ  . PHE D 98  ? 2.6101 2.9821 2.7662 0.2763  0.2938  -0.1724 98  PHE L CZ  
8908  N N   . GLY D 99  ? 2.4615 2.8108 2.8332 0.2486  0.1463  -0.3877 99  GLY L N   
8909  C CA  . GLY D 99  ? 2.5554 2.9063 2.9849 0.2448  0.1042  -0.4368 99  GLY L CA  
8910  C C   . GLY D 99  ? 2.5778 2.9916 3.0678 0.2518  0.0746  -0.4717 99  GLY L C   
8911  O O   . GLY D 99  ? 2.5238 2.9670 3.0097 0.2587  0.0772  -0.4556 99  GLY L O   
8912  N N   . GLU D 100 ? 2.5016 2.9372 3.0500 0.2502  0.0460  -0.5212 100 GLU L N   
8913  C CA  . GLU D 100 ? 2.5760 3.0716 3.1851 0.2565  0.0165  -0.5574 100 GLU L CA  
8914  C C   . GLU D 100 ? 2.5314 3.0015 3.1476 0.2573  -0.0265 -0.5497 100 GLU L C   
8915  O O   . GLU D 100 ? 2.5926 2.9990 3.2059 0.2503  -0.0623 -0.5500 100 GLU L O   
8916  C CB  . GLU D 100 ? 2.7226 3.2425 3.3957 0.2541  -0.0096 -0.6134 100 GLU L CB  
8917  C CG  . GLU D 100 ? 2.8468 3.4093 3.5294 0.2541  0.0285  -0.6329 100 GLU L CG  
8918  C CD  . GLU D 100 ? 2.9555 3.5415 3.7069 0.2515  -0.0024 -0.6905 100 GLU L CD  
8919  O OE1 . GLU D 100 ? 2.9593 3.5324 3.7508 0.2509  -0.0533 -0.7141 100 GLU L OE1 
8920  O OE2 . GLU D 100 ? 2.9911 3.6091 3.7574 0.2500  0.0237  -0.7130 100 GLU L OE2 
8921  N N   . GLY D 101 ? 2.5574 3.0778 3.1818 0.2657  -0.0221 -0.5430 101 GLY L N   
8922  C CA  . GLY D 101 ? 2.5908 3.0947 3.2191 0.2673  -0.0571 -0.5326 101 GLY L CA  
8923  C C   . GLY D 101 ? 2.6261 3.1275 3.3141 0.2654  -0.1155 -0.5758 101 GLY L C   
8924  O O   . GLY D 101 ? 2.6220 3.1495 3.3589 0.2647  -0.1301 -0.6193 101 GLY L O   
8925  N N   . THR D 102 ? 2.6876 3.1544 3.3700 0.2644  -0.1494 -0.5625 102 THR L N   
8926  C CA  . THR D 102 ? 2.7277 3.1862 3.4611 0.2628  -0.2078 -0.5980 102 THR L CA  
8927  C C   . THR D 102 ? 2.7364 3.2271 3.4825 0.2695  -0.2240 -0.5916 102 THR L C   
8928  O O   . THR D 102 ? 2.7471 3.2103 3.4476 0.2694  -0.2126 -0.5504 102 THR L O   
8929  C CB  . THR D 102 ? 2.7785 3.1458 3.4889 0.2525  -0.2399 -0.5890 102 THR L CB  
8930  O OG1 . THR D 102 ? 2.7664 3.1023 3.4588 0.2464  -0.2202 -0.5898 102 THR L OG1 
8931  C CG2 . THR D 102 ? 2.8220 3.1794 3.5874 0.2507  -0.3011 -0.6297 102 THR L CG2 
8932  N N   . THR D 103 ? 2.8676 3.4171 3.6757 0.2752  -0.2494 -0.6325 103 THR L N   
8933  C CA  . THR D 103 ? 2.8712 3.4597 3.6988 0.2821  -0.2658 -0.6321 103 THR L CA  
8934  C C   . THR D 103 ? 2.9297 3.4685 3.7711 0.2776  -0.3216 -0.6392 103 THR L C   
8935  O O   . THR D 103 ? 2.9593 3.4789 3.8396 0.2734  -0.3613 -0.6751 103 THR L O   
8936  C CB  . THR D 103 ? 2.8387 3.5140 3.7262 0.2901  -0.2665 -0.6732 103 THR L CB  
8937  O OG1 . THR D 103 ? 2.7891 3.5082 3.6612 0.2937  -0.2142 -0.6668 103 THR L OG1 
8938  C CG2 . THR D 103 ? 2.8431 3.5597 3.7479 0.2976  -0.2809 -0.6705 103 THR L CG2 
8939  N N   . LEU D 104 ? 2.9441 3.4623 3.7543 0.2783  -0.3249 -0.6058 104 LEU L N   
8940  C CA  . LEU D 104 ? 3.0501 3.5209 3.8679 0.2737  -0.3755 -0.6086 104 LEU L CA  
8941  C C   . LEU D 104 ? 3.1583 3.6872 4.0276 0.2813  -0.4041 -0.6345 104 LEU L C   
8942  O O   . LEU D 104 ? 3.1196 3.6959 3.9821 0.2887  -0.3812 -0.6173 104 LEU L O   
8943  C CB  . LEU D 104 ? 2.9867 3.3953 3.7392 0.2686  -0.3638 -0.5574 104 LEU L CB  
8944  C CG  . LEU D 104 ? 3.0309 3.3871 3.7845 0.2631  -0.4134 -0.5564 104 LEU L CG  
8945  C CD1 . LEU D 104 ? 3.1310 3.4359 3.9080 0.2553  -0.4584 -0.5875 104 LEU L CD1 
8946  C CD2 . LEU D 104 ? 3.0797 3.3763 3.7670 0.2575  -0.3970 -0.5053 104 LEU L CD2 
8947  N N   . ILE D 105 ? 3.1329 3.6578 4.0537 0.2796  -0.4542 -0.6758 105 ILE L N   
8948  C CA  . ILE D 105 ? 3.1760 3.7519 4.1508 0.2860  -0.4874 -0.7055 105 ILE L CA  
8949  C C   . ILE D 105 ? 3.3373 3.8566 4.3031 0.2810  -0.5322 -0.6961 105 ILE L C   
8950  O O   . ILE D 105 ? 3.3972 3.8544 4.3653 0.2731  -0.5688 -0.7080 105 ILE L O   
8951  C CB  . ILE D 105 ? 3.0786 3.6954 4.1219 0.2881  -0.5122 -0.7616 105 ILE L CB  
8952  C CG1 . ILE D 105 ? 2.9040 3.5773 3.9545 0.2923  -0.4657 -0.7709 105 ILE L CG1 
8953  C CG2 . ILE D 105 ? 3.0633 3.7294 4.1616 0.2944  -0.5482 -0.7917 105 ILE L CG2 
8954  C CD1 . ILE D 105 ? 2.8381 3.5536 3.9559 0.2938  -0.4859 -0.8264 105 ILE L CD1 
8955  N N   . VAL D 106 ? 3.2422 3.7810 4.1973 0.2853  -0.5300 -0.6751 106 VAL L N   
8956  C CA  . VAL D 106 ? 3.3154 3.8055 4.2626 0.2807  -0.5711 -0.6663 106 VAL L CA  
8957  C C   . VAL D 106 ? 3.4323 3.9620 4.4470 0.2851  -0.6185 -0.7117 106 VAL L C   
8958  O O   . VAL D 106 ? 3.4176 4.0181 4.4626 0.2941  -0.6120 -0.7220 106 VAL L O   
8959  C CB  . VAL D 106 ? 3.1848 3.6740 4.0872 0.2826  -0.5458 -0.6212 106 VAL L CB  
8960  C CG1 . VAL D 106 ? 3.2644 3.7000 4.1573 0.2766  -0.5878 -0.6129 106 VAL L CG1 
8961  C CG2 . VAL D 106 ? 3.0979 3.5508 3.9359 0.2786  -0.4981 -0.5778 106 VAL L CG2 
8962  N N   . LEU D 107 ? 3.2487 3.7320 4.2871 0.2789  -0.6668 -0.7392 107 LEU L N   
8963  C CA  . LEU D 107 ? 3.3243 3.8395 4.4285 0.2825  -0.7150 -0.7849 107 LEU L CA  
8964  C C   . LEU D 107 ? 3.4137 3.9334 4.5187 0.2846  -0.7381 -0.7742 107 LEU L C   
8965  O O   . LEU D 107 ? 3.4330 3.9235 4.4872 0.2821  -0.7203 -0.7320 107 LEU L O   
8966  C CB  . LEU D 107 ? 3.2869 3.7417 4.4097 0.2748  -0.7617 -0.8129 107 LEU L CB  
8967  C CG  . LEU D 107 ? 3.2630 3.7202 4.4013 0.2734  -0.7485 -0.8353 107 LEU L CG  
8968  C CD1 . LEU D 107 ? 3.2813 3.6718 4.4347 0.2656  -0.7982 -0.8601 107 LEU L CD1 
8969  C CD2 . LEU D 107 ? 3.2155 3.7654 4.4135 0.2827  -0.7360 -0.8732 107 LEU L CD2 
8970  N N   . SER D 108 ? 3.5153 4.0725 4.6804 0.2891  -0.7787 -0.8140 108 SER L N   
8971  C CA  . SER D 108 ? 3.5195 4.0847 4.6940 0.2913  -0.8063 -0.8107 108 SER L CA  
8972  C C   . SER D 108 ? 3.4285 4.0431 4.5786 0.2981  -0.7631 -0.7779 108 SER L C   
8973  O O   . SER D 108 ? 3.4117 3.9993 4.5273 0.2959  -0.7639 -0.7464 108 SER L O   
8974  C CB  . SER D 108 ? 3.5750 4.0484 4.7141 0.2808  -0.8422 -0.7927 108 SER L CB  
8975  O OG  . SER D 108 ? 3.6336 4.1139 4.7815 0.2825  -0.8686 -0.7899 108 SER L OG  
8976  N N   . GLN D 109 ? 3.5466 4.2338 4.7149 0.3063  -0.7252 -0.7862 109 GLN L N   
8977  C CA  . GLN D 109 ? 3.4948 4.2370 4.6462 0.3141  -0.6852 -0.7598 109 GLN L CA  
8978  C C   . GLN D 109 ? 3.5343 4.3144 4.7147 0.3198  -0.7108 -0.7677 109 GLN L C   
8979  O O   . GLN D 109 ? 3.5458 4.3234 4.6923 0.3211  -0.6945 -0.7327 109 GLN L O   
8980  C CB  . GLN D 109 ? 3.3593 4.1725 4.5301 0.3215  -0.6448 -0.7738 109 GLN L CB  
8981  C CG  . GLN D 109 ? 3.2365 4.0877 4.3700 0.3277  -0.5912 -0.7367 109 GLN L CG  
8982  C CD  . GLN D 109 ? 3.2449 4.0404 4.3116 0.3218  -0.5540 -0.6933 109 GLN L CD  
8983  O OE1 . GLN D 109 ? 3.2478 3.9920 4.3012 0.3142  -0.5582 -0.6967 109 GLN L OE1 
8984  N NE2 . GLN D 109 ? 3.1854 3.9915 4.2105 0.3253  -0.5173 -0.6528 109 GLN L NE2 
8985  N N   . PRO D 110 ? 3.4218 4.2375 4.6651 0.3232  -0.7505 -0.8133 110 PRO L N   
8986  C CA  . PRO D 110 ? 3.4248 4.2627 4.7219 0.3239  -0.7711 -0.8615 110 PRO L CA  
8987  C C   . PRO D 110 ? 3.3200 4.2543 4.6682 0.3342  -0.7565 -0.8919 110 PRO L C   
8988  O O   . PRO D 110 ? 3.2427 4.2077 4.6111 0.3357  -0.7373 -0.9136 110 PRO L O   
8989  C CB  . PRO D 110 ? 3.4411 4.2369 4.7671 0.3192  -0.8337 -0.8865 110 PRO L CB  
8990  C CG  . PRO D 110 ? 3.4897 4.2893 4.8033 0.3213  -0.8444 -0.8652 110 PRO L CG  
8991  C CD  . PRO D 110 ? 3.4221 4.2286 4.6796 0.3231  -0.7912 -0.8162 110 PRO L CD  
8992  N N   . LYS D 111 ? 3.2239 4.2036 4.5917 0.3408  -0.7656 -0.8934 111 LYS L N   
8993  C CA  . LYS D 111 ? 3.1078 4.1622 4.5060 0.3484  -0.7458 -0.9137 111 LYS L CA  
8994  C C   . LYS D 111 ? 2.9473 4.0583 4.3333 0.3573  -0.7184 -0.8863 111 LYS L C   
8995  O O   . LYS D 111 ? 3.0083 4.0815 4.3509 0.3551  -0.7148 -0.8480 111 LYS L O   
8996  C CB  . LYS D 111 ? 3.1623 4.1855 4.5653 0.3445  -0.7649 -0.9318 111 LYS L CB  
8997  C CG  . LYS D 111 ? 3.1533 4.0967 4.5538 0.3364  -0.7976 -0.9450 111 LYS L CG  
8998  C CD  . LYS D 111 ? 3.1155 4.0193 4.5104 0.3346  -0.8200 -0.9469 111 LYS L CD  
8999  C CE  . LYS D 111 ? 3.1919 4.0161 4.5837 0.3289  -0.8505 -0.9577 111 LYS L CE  
9000  N NZ  . LYS D 111 ? 3.1964 3.9847 4.5840 0.3287  -0.8705 -0.9584 111 LYS L NZ  
9001  N N   . ALA D 112 ? 2.9512 4.1346 4.3567 0.3647  -0.6885 -0.8990 112 ALA L N   
9002  C CA  . ALA D 112 ? 2.8614 4.0964 4.2499 0.3731  -0.6561 -0.8726 112 ALA L CA  
9003  C C   . ALA D 112 ? 2.8676 4.1601 4.2790 0.3766  -0.6401 -0.8966 112 ALA L C   
9004  O O   . ALA D 112 ? 2.8580 4.1789 4.2870 0.3768  -0.6221 -0.9206 112 ALA L O   
9005  C CB  . ALA D 112 ? 2.7132 3.9349 4.0430 0.3726  -0.6013 -0.8323 112 ALA L CB  
9006  N N   . ALA D 113 ? 2.8344 4.1349 4.2373 0.3776  -0.6435 -0.8875 113 ALA L N   
9007  C CA  . ALA D 113 ? 2.8028 4.1462 4.2158 0.3792  -0.6266 -0.9048 113 ALA L CA  
9008  C C   . ALA D 113 ? 2.7651 4.1820 4.1759 0.3888  -0.5843 -0.8938 113 ALA L C   
9009  O O   . ALA D 113 ? 2.6431 4.0813 4.0372 0.3963  -0.5706 -0.8624 113 ALA L O   
9010  C CB  . ALA D 113 ? 2.9018 4.2291 4.3054 0.3773  -0.6436 -0.8964 113 ALA L CB  
9011  N N   . PRO D 114 ? 2.7483 4.2042 4.1738 0.3893  -0.5616 -0.9183 114 PRO L N   
9012  C CA  . PRO D 114 ? 2.5944 4.1175 4.0139 0.3983  -0.5188 -0.9070 114 PRO L CA  
9013  C C   . PRO D 114 ? 2.6217 4.1767 4.0263 0.4033  -0.5078 -0.8884 114 PRO L C   
9014  O O   . PRO D 114 ? 2.6503 4.1960 4.0590 0.3987  -0.5234 -0.9012 114 PRO L O   
9015  C CB  . PRO D 114 ? 2.5444 4.0911 3.9836 0.3947  -0.5038 -0.9427 114 PRO L CB  
9016  C CG  . PRO D 114 ? 2.6731 4.1755 4.1270 0.3857  -0.5374 -0.9708 114 PRO L CG  
9017  C CD  . PRO D 114 ? 2.7120 4.1512 4.1591 0.3820  -0.5727 -0.9571 114 PRO L CD  
9018  N N   . SER D 115 ? 2.5642 4.1562 3.9510 0.4135  -0.4798 -0.8575 115 SER L N   
9019  C CA  . SER D 115 ? 2.4877 4.1132 3.8583 0.4194  -0.4655 -0.8367 115 SER L CA  
9020  C C   . SER D 115 ? 2.4646 4.1495 3.8320 0.4244  -0.4255 -0.8430 115 SER L C   
9021  O O   . SER D 115 ? 2.3520 4.0700 3.7053 0.4335  -0.3915 -0.8234 115 SER L O   
9022  C CB  . SER D 115 ? 2.4118 4.0352 3.7623 0.4279  -0.4610 -0.7971 115 SER L CB  
9023  O OG  . SER D 115 ? 2.5521 4.1179 3.9036 0.4221  -0.4988 -0.7919 115 SER L OG  
9024  N N   . VAL D 116 ? 2.5324 4.2287 3.9110 0.4186  -0.4287 -0.8704 116 VAL L N   
9025  C CA  . VAL D 116 ? 2.5265 4.2745 3.9022 0.4212  -0.3943 -0.8807 116 VAL L CA  
9026  C C   . VAL D 116 ? 2.5143 4.2965 3.8700 0.4275  -0.3784 -0.8584 116 VAL L C   
9027  O O   . VAL D 116 ? 2.5261 4.2914 3.8785 0.4267  -0.4000 -0.8479 116 VAL L O   
9028  C CB  . VAL D 116 ? 2.5348 4.2779 3.9334 0.4119  -0.4051 -0.9234 116 VAL L CB  
9029  C CG1 . VAL D 116 ? 2.5495 4.2637 3.9666 0.4065  -0.4148 -0.9447 116 VAL L CG1 
9030  C CG2 . VAL D 116 ? 2.5912 4.3052 3.9973 0.4064  -0.4378 -0.9342 116 VAL L CG2 
9031  N N   . THR D 117 ? 2.5827 4.4119 3.9235 0.4338  -0.3395 -0.8503 117 THR L N   
9032  C CA  . THR D 117 ? 2.5836 4.4482 3.9034 0.4402  -0.3204 -0.8298 117 THR L CA  
9033  C C   . THR D 117 ? 2.5764 4.4841 3.8898 0.4405  -0.2870 -0.8440 117 THR L C   
9034  O O   . THR D 117 ? 2.5559 4.4777 3.8618 0.4431  -0.2588 -0.8422 117 THR L O   
9035  C CB  . THR D 117 ? 2.4963 4.3675 3.7914 0.4512  -0.3040 -0.7870 117 THR L CB  
9036  O OG1 . THR D 117 ? 2.5462 4.3748 3.8479 0.4498  -0.3354 -0.7757 117 THR L OG1 
9037  C CG2 . THR D 117 ? 2.3739 4.2755 3.6491 0.4571  -0.2901 -0.7667 117 THR L CG2 
9038  N N   . LEU D 118 ? 2.3487 4.2756 3.6635 0.4377  -0.2892 -0.8576 118 LEU L N   
9039  C CA  . LEU D 118 ? 2.3921 4.3577 3.7012 0.4365  -0.2613 -0.8742 118 LEU L CA  
9040  C C   . LEU D 118 ? 2.5054 4.5061 3.7861 0.4446  -0.2372 -0.8475 118 LEU L C   
9041  O O   . LEU D 118 ? 2.6154 4.6157 3.8945 0.4457  -0.2532 -0.8398 118 LEU L O   
9042  C CB  . LEU D 118 ? 2.4228 4.3837 3.7563 0.4268  -0.2819 -0.9147 118 LEU L CB  
9043  C CG  . LEU D 118 ? 2.4565 4.4553 3.7873 0.4238  -0.2561 -0.9371 118 LEU L CG  
9044  C CD1 . LEU D 118 ? 2.4393 4.4481 3.7668 0.4228  -0.2281 -0.9428 118 LEU L CD1 
9045  C CD2 . LEU D 118 ? 2.5386 4.5305 3.8942 0.4149  -0.2787 -0.9764 118 LEU L CD2 
9046  N N   . PHE D 119 ? 2.4429 4.4715 3.6995 0.4502  -0.1980 -0.8329 119 PHE L N   
9047  C CA  . PHE D 119 ? 2.4578 4.5178 3.6839 0.4581  -0.1728 -0.8069 119 PHE L CA  
9048  C C   . PHE D 119 ? 2.4636 4.5566 3.6827 0.4543  -0.1511 -0.8274 119 PHE L C   
9049  O O   . PHE D 119 ? 2.4110 4.5092 3.6324 0.4494  -0.1337 -0.8462 119 PHE L O   
9050  C CB  . PHE D 119 ? 2.3798 4.4434 3.5749 0.4685  -0.1425 -0.7677 119 PHE L CB  
9051  C CG  . PHE D 119 ? 2.3658 4.4068 3.5593 0.4747  -0.1603 -0.7389 119 PHE L CG  
9052  C CD1 . PHE D 119 ? 2.4094 4.4588 3.5911 0.4801  -0.1663 -0.7171 119 PHE L CD1 
9053  C CD2 . PHE D 119 ? 2.2570 4.2680 3.4607 0.4750  -0.1711 -0.7339 119 PHE L CD2 
9054  C CE1 . PHE D 119 ? 2.3166 4.3451 3.4966 0.4851  -0.1819 -0.6909 119 PHE L CE1 
9055  C CE2 . PHE D 119 ? 2.1232 4.1131 3.3245 0.4803  -0.1875 -0.7077 119 PHE L CE2 
9056  C CZ  . PHE D 119 ? 2.1203 4.1191 3.3096 0.4851  -0.1925 -0.6861 119 PHE L CZ  
9057  N N   . PRO D 120 ? 2.2740 4.3887 3.4839 0.4563  -0.1516 -0.8240 120 PRO L N   
9058  C CA  . PRO D 120 ? 2.4063 4.5538 3.6064 0.4533  -0.1307 -0.8411 120 PRO L CA  
9059  C C   . PRO D 120 ? 2.4219 4.5903 3.5835 0.4597  -0.0877 -0.8157 120 PRO L C   
9060  O O   . PRO D 120 ? 2.3053 4.4661 3.4446 0.4684  -0.0740 -0.7803 120 PRO L O   
9061  C CB  . PRO D 120 ? 2.4531 4.6122 3.6545 0.4548  -0.1483 -0.8404 120 PRO L CB  
9062  C CG  . PRO D 120 ? 2.3320 4.4743 3.5254 0.4627  -0.1597 -0.8057 120 PRO L CG  
9063  C CD  . PRO D 120 ? 2.2164 4.3249 3.4248 0.4610  -0.1726 -0.8044 120 PRO L CD  
9064  N N   . PRO D 121 ? 2.2902 4.4824 3.4407 0.4553  -0.0646 -0.8324 121 PRO L N   
9065  C CA  . PRO D 121 ? 2.2942 4.5009 3.4026 0.4604  -0.0225 -0.8071 121 PRO L CA  
9066  C C   . PRO D 121 ? 2.2789 4.4987 3.3596 0.4711  -0.0156 -0.7722 121 PRO L C   
9067  O O   . PRO D 121 ? 2.2922 4.5237 3.3836 0.4721  -0.0364 -0.7775 121 PRO L O   
9068  C CB  . PRO D 121 ? 2.3561 4.5844 3.4629 0.4515  -0.0070 -0.8370 121 PRO L CB  
9069  C CG  . PRO D 121 ? 2.3845 4.6194 3.5265 0.4453  -0.0406 -0.8702 121 PRO L CG  
9070  C CD  . PRO D 121 ? 2.3466 4.5515 3.5199 0.4449  -0.0751 -0.8742 121 PRO L CD  
9071  N N   . SER D 122 ? 2.2201 4.4359 3.2639 0.4791  0.0141  -0.7363 122 SER L N   
9072  C CA  . SER D 122 ? 2.2199 4.4455 3.2365 0.4898  0.0214  -0.7014 122 SER L CA  
9073  C C   . SER D 122 ? 2.2326 4.4879 3.2294 0.4898  0.0355  -0.7058 122 SER L C   
9074  O O   . SER D 122 ? 2.2444 4.5112 3.2362 0.4823  0.0509  -0.7278 122 SER L O   
9075  C CB  . SER D 122 ? 2.2215 4.4323 3.2004 0.4982  0.0516  -0.6615 122 SER L CB  
9076  O OG  . SER D 122 ? 2.2137 4.3981 3.2064 0.4963  0.0474  -0.6627 122 SER L OG  
9077  N N   . SER D 123 ? 2.3598 4.6269 3.3455 0.4980  0.0293  -0.6846 123 SER L N   
9078  C CA  . SER D 123 ? 2.4434 4.7388 3.4092 0.4994  0.0410  -0.6861 123 SER L CA  
9079  C C   . SER D 123 ? 2.4611 4.7584 3.3794 0.5026  0.0829  -0.6634 123 SER L C   
9080  O O   . SER D 123 ? 2.5641 4.8812 3.4636 0.5003  0.0987  -0.6715 123 SER L O   
9081  C CB  . SER D 123 ? 2.4319 4.7372 3.3987 0.5076  0.0226  -0.6689 123 SER L CB  
9082  O OG  . SER D 123 ? 2.2841 4.5812 3.2205 0.5186  0.0387  -0.6267 123 SER L OG  
9083  N N   . GLU D 124 ? 2.5453 4.8190 3.4416 0.5075  0.1011  -0.6340 124 GLU L N   
9084  C CA  . GLU D 124 ? 2.5271 4.7926 3.3734 0.5103  0.1413  -0.6075 124 GLU L CA  
9085  C C   . GLU D 124 ? 2.6182 4.8757 3.4556 0.4992  0.1631  -0.6280 124 GLU L C   
9086  O O   . GLU D 124 ? 2.5961 4.8524 3.3924 0.4982  0.1941  -0.6158 124 GLU L O   
9087  C CB  . GLU D 124 ? 2.3716 4.6097 3.2004 0.5179  0.1513  -0.5715 124 GLU L CB  
9088  C CG  . GLU D 124 ? 2.3780 4.6000 3.1512 0.5218  0.1911  -0.5371 124 GLU L CG  
9089  C CD  . GLU D 124 ? 2.3183 4.5135 3.0770 0.5295  0.1981  -0.5022 124 GLU L CD  
9090  O OE1 . GLU D 124 ? 2.3156 4.4989 3.1064 0.5282  0.1790  -0.5112 124 GLU L OE1 
9091  O OE2 . GLU D 124 ? 2.3002 4.4848 3.0152 0.5366  0.2224  -0.4662 124 GLU L OE2 
9092  N N   . GLU D 125 ? 2.5314 4.7793 3.4042 0.4908  0.1484  -0.6569 125 GLU L N   
9093  C CA  . GLU D 125 ? 2.6263 4.8655 3.4944 0.4795  0.1676  -0.6784 125 GLU L CA  
9094  C C   . GLU D 125 ? 2.7482 5.0125 3.6281 0.4704  0.1645  -0.7134 125 GLU L C   
9095  O O   . GLU D 125 ? 2.8623 5.1230 3.7206 0.4622  0.1901  -0.7216 125 GLU L O   
9096  C CB  . GLU D 125 ? 2.5188 4.7362 3.4180 0.4739  0.1555  -0.6956 125 GLU L CB  
9097  C CG  . GLU D 125 ? 2.4827 4.7094 3.4348 0.4650  0.1232  -0.7406 125 GLU L CG  
9098  C CD  . GLU D 125 ? 2.4241 4.6256 3.4009 0.4605  0.1147  -0.7529 125 GLU L CD  
9099  O OE1 . GLU D 125 ? 2.4370 4.6183 3.3855 0.4595  0.1436  -0.7373 125 GLU L OE1 
9100  O OE2 . GLU D 125 ? 2.3911 4.5903 3.4133 0.4574  0.0797  -0.7782 125 GLU L OE2 
9101  N N   . LEU D 126 ? 2.4512 4.7388 3.3637 0.4710  0.1340  -0.7335 126 LEU L N   
9102  C CA  . LEU D 126 ? 2.5750 4.8872 3.5023 0.4622  0.1283  -0.7689 126 LEU L CA  
9103  C C   . LEU D 126 ? 2.7761 5.1025 3.6596 0.4625  0.1586  -0.7569 126 LEU L C   
9104  O O   . LEU D 126 ? 2.8964 5.2349 3.7812 0.4525  0.1670  -0.7838 126 LEU L O   
9105  C CB  . LEU D 126 ? 2.4310 4.7610 3.3941 0.4647  0.0908  -0.7845 126 LEU L CB  
9106  C CG  . LEU D 126 ? 2.2121 4.5279 3.2235 0.4612  0.0545  -0.8062 126 LEU L CG  
9107  C CD1 . LEU D 126 ? 2.1956 4.5249 3.2318 0.4634  0.0214  -0.8170 126 LEU L CD1 
9108  C CD2 . LEU D 126 ? 2.2974 4.6059 3.3356 0.4483  0.0514  -0.8447 126 LEU L CD2 
9109  N N   . GLN D 127 ? 2.7759 5.0996 3.6202 0.4733  0.1750  -0.7174 127 GLN L N   
9110  C CA  . GLN D 127 ? 2.8444 5.1761 3.6430 0.4739  0.2041  -0.7029 127 GLN L CA  
9111  C C   . GLN D 127 ? 2.7992 5.1050 3.5634 0.4661  0.2389  -0.6961 127 GLN L C   
9112  O O   . GLN D 127 ? 2.8140 5.1223 3.5429 0.4626  0.2629  -0.6919 127 GLN L O   
9113  C CB  . GLN D 127 ? 2.8282 5.1589 3.5933 0.4876  0.2120  -0.6611 127 GLN L CB  
9114  C CG  . GLN D 127 ? 2.5051 4.8077 3.2672 0.4933  0.2134  -0.6352 127 GLN L CG  
9115  C CD  . GLN D 127 ? 2.4466 4.7451 3.1776 0.5063  0.2210  -0.5937 127 GLN L CD  
9116  O OE1 . GLN D 127 ? 2.5829 4.8984 3.2903 0.5112  0.2282  -0.5833 127 GLN L OE1 
9117  N NE2 . GLN D 127 ? 2.3546 4.6329 3.0897 0.5127  0.2157  -0.5714 127 GLN L NE2 
9118  N N   . ALA D 128 ? 2.6394 4.9184 3.4121 0.4628  0.2418  -0.6949 128 ALA L N   
9119  C CA  . ALA D 128 ? 2.6397 4.8903 3.3809 0.4544  0.2738  -0.6893 128 ALA L CA  
9120  C C   . ALA D 128 ? 2.8694 5.1249 3.6422 0.4401  0.2684  -0.7327 128 ALA L C   
9121  O O   . ALA D 128 ? 2.9353 5.1655 3.6976 0.4315  0.2871  -0.7362 128 ALA L O   
9122  C CB  . ALA D 128 ? 2.5015 4.7180 3.2292 0.4591  0.2831  -0.6608 128 ALA L CB  
9123  N N   . ASN D 129 ? 2.7072 4.9942 3.5185 0.4372  0.2423  -0.7660 129 ASN L N   
9124  C CA  . ASN D 129 ? 2.7873 5.0842 3.6340 0.4237  0.2324  -0.8112 129 ASN L CA  
9125  C C   . ASN D 129 ? 2.7525 5.0281 3.6311 0.4190  0.2210  -0.8260 129 ASN L C   
9126  O O   . ASN D 129 ? 2.8171 5.0839 3.7057 0.4069  0.2293  -0.8510 129 ASN L O   
9127  C CB  . ASN D 129 ? 2.8704 5.1656 3.6848 0.4131  0.2632  -0.8181 129 ASN L CB  
9128  C CG  . ASN D 129 ? 2.8845 5.2008 3.7349 0.4003  0.2507  -0.8656 129 ASN L CG  
9129  O OD1 . ASN D 129 ? 2.8672 5.2055 3.7617 0.4009  0.2184  -0.8916 129 ASN L OD1 
9130  N ND2 . ASN D 129 ? 2.9804 5.2887 3.8106 0.3883  0.2762  -0.8766 129 ASN L ND2 
9131  N N   . LYS D 130 ? 2.9259 5.1928 3.8211 0.4285  0.2013  -0.8106 130 LYS L N   
9132  C CA  . LYS D 130 ? 2.8140 5.0598 3.7396 0.4257  0.1880  -0.8222 130 LYS L CA  
9133  C C   . LYS D 130 ? 2.6851 4.9386 3.6545 0.4320  0.1470  -0.8307 130 LYS L C   
9134  O O   . LYS D 130 ? 2.6109 4.8768 3.5749 0.4417  0.1359  -0.8117 130 LYS L O   
9135  C CB  . LYS D 130 ? 2.6168 4.8307 3.5048 0.4311  0.2135  -0.7836 130 LYS L CB  
9136  C CG  . LYS D 130 ? 2.6903 4.8865 3.5300 0.4243  0.2546  -0.7707 130 LYS L CG  
9137  C CD  . LYS D 130 ? 2.4463 4.6084 3.2451 0.4304  0.2790  -0.7293 130 LYS L CD  
9138  C CE  . LYS D 130 ? 2.5040 4.6432 3.2507 0.4230  0.3193  -0.7141 130 LYS L CE  
9139  N NZ  . LYS D 130 ? 2.4407 4.5430 3.1441 0.4284  0.3435  -0.6723 130 LYS L NZ  
9140  N N   . ALA D 131 ? 2.7097 4.9525 3.7217 0.4259  0.1241  -0.8594 131 ALA L N   
9141  C CA  . ALA D 131 ? 2.5358 4.7764 3.5906 0.4295  0.0833  -0.8702 131 ALA L CA  
9142  C C   . ALA D 131 ? 2.3914 4.6044 3.4712 0.4262  0.0726  -0.8802 131 ALA L C   
9143  O O   . ALA D 131 ? 2.4499 4.6543 3.5326 0.4169  0.0866  -0.8996 131 ALA L O   
9144  C CB  . ALA D 131 ? 2.5617 4.8235 3.6517 0.4231  0.0555  -0.9081 131 ALA L CB  
9145  N N   . THR D 132 ? 2.4964 4.6942 3.5938 0.4334  0.0476  -0.8672 132 THR L N   
9146  C CA  . THR D 132 ? 2.3359 4.5061 3.4572 0.4311  0.0353  -0.8753 132 THR L CA  
9147  C C   . THR D 132 ? 2.2948 4.4526 3.4495 0.4353  -0.0068 -0.8766 132 THR L C   
9148  O O   . THR D 132 ? 2.2561 4.4139 3.3972 0.4450  -0.0118 -0.8460 132 THR L O   
9149  C CB  . THR D 132 ? 2.3079 4.4589 3.3923 0.4367  0.0676  -0.8406 132 THR L CB  
9150  O OG1 . THR D 132 ? 2.3522 4.5069 3.4023 0.4308  0.1064  -0.8396 132 THR L OG1 
9151  C CG2 . THR D 132 ? 2.2826 4.4055 3.3931 0.4349  0.0532  -0.8497 132 THR L CG2 
9152  N N   . LEU D 133 ? 2.4815 4.6258 3.6784 0.4273  -0.0369 -0.9118 133 LEU L N   
9153  C CA  . LEU D 133 ? 2.4133 4.5361 3.6413 0.4288  -0.0786 -0.9159 133 LEU L CA  
9154  C C   . LEU D 133 ? 2.2879 4.3808 3.5200 0.4318  -0.0812 -0.9019 133 LEU L C   
9155  O O   . LEU D 133 ? 2.2798 4.3642 3.5142 0.4271  -0.0657 -0.9136 133 LEU L O   
9156  C CB  . LEU D 133 ? 2.5910 4.7095 3.8584 0.4183  -0.1091 -0.9610 133 LEU L CB  
9157  C CG  . LEU D 133 ? 2.7028 4.8478 3.9711 0.4153  -0.1132 -0.9776 133 LEU L CG  
9158  C CD1 . LEU D 133 ? 2.8582 4.9954 4.1639 0.4047  -0.1394 -1.0237 133 LEU L CD1 
9159  C CD2 . LEU D 133 ? 2.4484 4.5965 3.7069 0.4235  -0.1280 -0.9523 133 LEU L CD2 
9160  N N   . VAL D 134 ? 2.5836 4.6599 3.8163 0.4393  -0.1005 -0.8768 134 VAL L N   
9161  C CA  . VAL D 134 ? 2.5310 4.5791 3.7654 0.4434  -0.1040 -0.8597 134 VAL L CA  
9162  C C   . VAL D 134 ? 2.4818 4.4982 3.7515 0.4401  -0.1513 -0.8731 134 VAL L C   
9163  O O   . VAL D 134 ? 2.4630 4.4764 3.7374 0.4416  -0.1755 -0.8671 134 VAL L O   
9164  C CB  . VAL D 134 ? 2.4458 4.4984 3.6425 0.4558  -0.0804 -0.8125 134 VAL L CB  
9165  C CG1 . VAL D 134 ? 2.4099 4.4366 3.6026 0.4603  -0.0747 -0.7946 134 VAL L CG1 
9166  C CG2 . VAL D 134 ? 2.4710 4.5515 3.6279 0.4586  -0.0374 -0.7974 134 VAL L CG2 
9167  N N   . CYS D 135 ? 2.6815 4.6707 3.9734 0.4355  -0.1644 -0.8897 135 CYS L N   
9168  C CA  . CYS D 135 ? 2.7192 4.6706 4.0415 0.4313  -0.2098 -0.9025 135 CYS L CA  
9169  C C   . CYS D 135 ? 2.5221 4.4462 3.8418 0.4365  -0.2120 -0.8809 135 CYS L C   
9170  O O   . CYS D 135 ? 2.4770 4.3912 3.8047 0.4339  -0.2023 -0.8928 135 CYS L O   
9171  C CB  . CYS D 135 ? 2.9776 4.9146 4.3330 0.4197  -0.2306 -0.9477 135 CYS L CB  
9172  S SG  . CYS D 135 ? 2.9696 4.8564 4.3571 0.4129  -0.2878 -0.9675 135 CYS L SG  
9173  N N   . LEU D 136 ? 2.6767 4.5888 3.9849 0.4437  -0.2234 -0.8496 136 LEU L N   
9174  C CA  . LEU D 136 ? 2.5776 4.4642 3.8814 0.4495  -0.2259 -0.8268 136 LEU L CA  
9175  C C   . LEU D 136 ? 2.5461 4.3862 3.8794 0.4422  -0.2740 -0.8437 136 LEU L C   
9176  O O   . LEU D 136 ? 2.5389 4.3628 3.8810 0.4380  -0.3056 -0.8485 136 LEU L O   
9177  C CB  . LEU D 136 ? 2.5723 4.4549 3.8361 0.4580  -0.2107 -0.7795 136 LEU L CB  
9178  C CG  . LEU D 136 ? 2.5594 4.4703 3.7790 0.4644  -0.1609 -0.7522 136 LEU L CG  
9179  C CD1 . LEU D 136 ? 2.5385 4.4415 3.7390 0.4589  -0.1273 -0.7592 136 LEU L CD1 
9180  C CD2 . LEU D 136 ? 2.6225 4.5858 3.8509 0.4686  -0.1577 -0.7619 136 LEU L CD2 
9181  N N   . ILE D 137 ? 2.6077 4.4064 3.9393 0.4366  -0.2765 -0.8467 137 ILE L N   
9182  C CA  . ILE D 137 ? 2.5812 4.3330 3.9401 0.4298  -0.3216 -0.8637 137 ILE L CA  
9183  C C   . ILE D 137 ? 2.5329 4.2104 3.8410 0.4250  -0.3163 -0.8221 137 ILE L C   
9184  O O   . ILE D 137 ? 2.5653 4.2163 3.8352 0.4214  -0.2830 -0.8040 137 ILE L O   
9185  C CB  . ILE D 137 ? 2.6402 4.3933 4.0376 0.4227  -0.3326 -0.9084 137 ILE L CB  
9186  C CG1 . ILE D 137 ? 2.7175 4.5056 4.1187 0.4182  -0.3162 -0.9332 137 ILE L CG1 
9187  C CG2 . ILE D 137 ? 2.6080 4.3057 4.0274 0.4135  -0.3825 -0.9269 137 ILE L CG2 
9188  C CD1 . ILE D 137 ? 2.6714 4.4538 4.0967 0.4094  -0.3171 -0.9718 137 ILE L CD1 
9189  N N   . SER D 138 ? 2.6127 4.2552 3.9201 0.4243  -0.3489 -0.8077 138 SER L N   
9190  C CA  . SER D 138 ? 2.6616 4.2320 3.9205 0.4192  -0.3455 -0.7680 138 SER L CA  
9191  C C   . SER D 138 ? 2.7719 4.2949 4.0520 0.4135  -0.3966 -0.7775 138 SER L C   
9192  O O   . SER D 138 ? 2.7738 4.3222 4.1048 0.4147  -0.4348 -0.8115 138 SER L O   
9193  C CB  . SER D 138 ? 2.5870 4.1602 3.7989 0.4255  -0.3170 -0.7207 138 SER L CB  
9194  O OG  . SER D 138 ? 2.5971 4.2028 3.8338 0.4316  -0.3412 -0.7241 138 SER L OG  
9195  N N   . ASP D 139 ? 2.8072 4.2590 4.0454 0.4070  -0.3963 -0.7462 139 ASP L N   
9196  C CA  . ASP D 139 ? 2.7452 4.1391 3.9900 0.4003  -0.4408 -0.7469 139 ASP L CA  
9197  C C   . ASP D 139 ? 2.7810 4.1693 4.0787 0.3953  -0.4823 -0.7952 139 ASP L C   
9198  O O   . ASP D 139 ? 2.8174 4.1997 4.1491 0.3944  -0.5271 -0.8148 139 ASP L O   
9199  C CB  . ASP D 139 ? 2.6593 4.0655 3.9086 0.4050  -0.4607 -0.7334 139 ASP L CB  
9200  C CG  . ASP D 139 ? 2.5932 3.9880 3.7868 0.4083  -0.4251 -0.6823 139 ASP L CG  
9201  O OD1 . ASP D 139 ? 2.6107 3.9527 3.7564 0.4029  -0.4023 -0.6515 139 ASP L OD1 
9202  O OD2 . ASP D 139 ? 2.4220 3.8612 3.6206 0.4163  -0.4197 -0.6733 139 ASP L OD2 
9203  N N   . PHE D 140 ? 2.7667 4.1550 4.0713 0.3919  -0.4678 -0.8148 140 PHE L N   
9204  C CA  . PHE D 140 ? 2.7922 4.1744 4.1474 0.3871  -0.5050 -0.8612 140 PHE L CA  
9205  C C   . PHE D 140 ? 2.8031 4.1212 4.1351 0.3780  -0.5021 -0.8570 140 PHE L C   
9206  O O   . PHE D 140 ? 2.8150 4.1221 4.1059 0.3767  -0.4599 -0.8334 140 PHE L O   
9207  C CB  . PHE D 140 ? 2.8237 4.2810 4.2278 0.3919  -0.4969 -0.9032 140 PHE L CB  
9208  C CG  . PHE D 140 ? 2.7778 4.2590 4.1568 0.3928  -0.4448 -0.8953 140 PHE L CG  
9209  C CD1 . PHE D 140 ? 2.6600 4.1818 4.0087 0.3999  -0.4033 -0.8685 140 PHE L CD1 
9210  C CD2 . PHE D 140 ? 2.8425 4.3052 4.2284 0.3866  -0.4379 -0.9153 140 PHE L CD2 
9211  C CE1 . PHE D 140 ? 2.6507 4.1928 3.9746 0.4004  -0.3559 -0.8615 140 PHE L CE1 
9212  C CE2 . PHE D 140 ? 2.8162 4.2999 4.1782 0.3869  -0.3898 -0.9084 140 PHE L CE2 
9213  C CZ  . PHE D 140 ? 2.7218 4.2448 4.0521 0.3937  -0.3488 -0.8814 140 PHE L CZ  
9214  N N   . TYR D 141 ? 2.8580 4.1328 4.2161 0.3717  -0.5480 -0.8800 141 TYR L N   
9215  C CA  . TYR D 141 ? 2.9634 4.1744 4.3046 0.3628  -0.5525 -0.8800 141 TYR L CA  
9216  C C   . TYR D 141 ? 3.0353 4.2482 4.4379 0.3598  -0.5966 -0.9324 141 TYR L C   
9217  O O   . TYR D 141 ? 3.0342 4.2551 4.4755 0.3613  -0.6396 -0.9545 141 TYR L O   
9218  C CB  . TYR D 141 ? 2.9623 4.0935 4.2546 0.3565  -0.5646 -0.8412 141 TYR L CB  
9219  C CG  . TYR D 141 ? 3.0173 4.0782 4.2809 0.3472  -0.5631 -0.8331 141 TYR L CG  
9220  C CD1 . TYR D 141 ? 2.9800 4.0197 4.1891 0.3452  -0.5159 -0.7978 141 TYR L CD1 
9221  C CD2 . TYR D 141 ? 3.0480 4.0651 4.3399 0.3406  -0.6086 -0.8620 141 TYR L CD2 
9222  C CE1 . TYR D 141 ? 3.0415 4.0174 4.2237 0.3367  -0.5136 -0.7901 141 TYR L CE1 
9223  C CE2 . TYR D 141 ? 3.0520 4.0045 4.3172 0.3321  -0.6073 -0.8548 141 TYR L CE2 
9224  C CZ  . TYR D 141 ? 3.0685 4.0011 4.2788 0.3301  -0.5594 -0.8186 141 TYR L CZ  
9225  O OH  . TYR D 141 ? 3.1037 3.9719 4.2866 0.3216  -0.5576 -0.8109 141 TYR L OH  
9226  N N   . PRO D 142 ? 2.9645 4.1703 4.3775 0.3556  -0.5865 -0.9532 142 PRO L N   
9227  C CA  . PRO D 142 ? 2.9304 4.1273 4.2994 0.3536  -0.5360 -0.9295 142 PRO L CA  
9228  C C   . PRO D 142 ? 2.8262 4.1007 4.2029 0.3606  -0.4930 -0.9358 142 PRO L C   
9229  O O   . PRO D 142 ? 2.8099 4.1455 4.2307 0.3665  -0.5043 -0.9630 142 PRO L O   
9230  C CB  . PRO D 142 ? 2.9975 4.1587 4.3872 0.3462  -0.5527 -0.9586 142 PRO L CB  
9231  C CG  . PRO D 142 ? 3.0507 4.2445 4.5125 0.3479  -0.5980 -1.0106 142 PRO L CG  
9232  C CD  . PRO D 142 ? 3.0138 4.2134 4.4831 0.3520  -0.6280 -1.0023 142 PRO L CD  
9233  N N   . GLY D 143 ? 2.8446 4.1148 4.1776 0.3596  -0.4444 -0.9108 143 GLY L N   
9234  C CA  . GLY D 143 ? 2.8416 4.1783 4.1725 0.3654  -0.4000 -0.9121 143 GLY L CA  
9235  C C   . GLY D 143 ? 2.9391 4.3186 4.3199 0.3642  -0.3989 -0.9610 143 GLY L C   
9236  O O   . GLY D 143 ? 3.0237 4.3932 4.3899 0.3599  -0.3709 -0.9631 143 GLY L O   
9237  N N   . ALA D 144 ? 2.7277 4.1556 4.1684 0.3678  -0.4290 -1.0012 144 ALA L N   
9238  C CA  . ALA D 144 ? 2.7661 4.2402 4.2605 0.3667  -0.4300 -1.0516 144 ALA L CA  
9239  C C   . ALA D 144 ? 2.7262 4.2676 4.2705 0.3735  -0.4487 -1.0806 144 ALA L C   
9240  O O   . ALA D 144 ? 2.7377 4.2382 4.2896 0.3679  -0.4856 -1.0947 144 ALA L O   
9241  C CB  . ALA D 144 ? 2.7831 4.2144 4.3106 0.3593  -0.4660 -1.0831 144 ALA L CB  
9242  N N   . VAL D 145 ? 2.7216 4.3214 4.2552 0.3791  -0.4107 -1.0737 145 VAL L N   
9243  C CA  . VAL D 145 ? 2.8397 4.4600 4.3700 0.3781  -0.4122 -1.0821 145 VAL L CA  
9244  C C   . VAL D 145 ? 2.9807 4.6454 4.5194 0.3752  -0.3800 -1.1086 145 VAL L C   
9245  O O   . VAL D 145 ? 3.0038 4.6948 4.5403 0.3767  -0.3456 -1.1085 145 VAL L O   
9246  C CB  . VAL D 145 ? 2.7558 4.4004 4.2584 0.3869  -0.4004 -1.0443 145 VAL L CB  
9247  C CG1 . VAL D 145 ? 2.6265 4.2243 4.1210 0.3881  -0.4355 -1.0211 145 VAL L CG1 
9248  C CG2 . VAL D 145 ? 2.6747 4.3571 4.1499 0.3949  -0.3508 -1.0167 145 VAL L CG2 
9249  N N   . THR D 146 ? 2.7125 4.3830 4.2592 0.3709  -0.3902 -1.1313 146 THR L N   
9250  C CA  . THR D 146 ? 2.7823 4.4933 4.3359 0.3672  -0.3636 -1.1580 146 THR L CA  
9251  C C   . THR D 146 ? 2.8046 4.5452 4.3430 0.3699  -0.3573 -1.1497 146 THR L C   
9252  O O   . THR D 146 ? 2.8078 4.5236 4.3489 0.3697  -0.3873 -1.1509 146 THR L O   
9253  C CB  . THR D 146 ? 2.7985 4.4832 4.3831 0.3585  -0.3845 -1.2026 146 THR L CB  
9254  O OG1 . THR D 146 ? 2.7865 4.4293 4.3782 0.3578  -0.4237 -1.2091 146 THR L OG1 
9255  C CG2 . THR D 146 ? 2.8249 4.4816 4.4252 0.3553  -0.3895 -1.2122 146 THR L CG2 
9256  N N   . VAL D 147 ? 2.6932 4.4838 4.2134 0.3726  -0.3177 -1.1404 147 VAL L N   
9257  C CA  . VAL D 147 ? 2.6891 4.5107 4.1918 0.3757  -0.3086 -1.1295 147 VAL L CA  
9258  C C   . VAL D 147 ? 2.7568 4.6047 4.2713 0.3687  -0.2969 -1.1655 147 VAL L C   
9259  O O   . VAL D 147 ? 2.8507 4.7180 4.3682 0.3643  -0.2705 -1.1814 147 VAL L O   
9260  C CB  . VAL D 147 ? 2.6380 4.4942 4.1064 0.3847  -0.2719 -1.0897 147 VAL L CB  
9261  C CG1 . VAL D 147 ? 2.6680 4.5523 4.1186 0.3881  -0.2663 -1.0775 147 VAL L CG1 
9262  C CG2 . VAL D 147 ? 2.5782 4.4096 4.0362 0.3920  -0.2792 -1.0560 147 VAL L CG2 
9263  N N   . ALA D 148 ? 2.7143 4.5614 4.2344 0.3674  -0.3156 -1.1783 148 ALA L N   
9264  C CA  . ALA D 148 ? 2.8599 4.7327 4.3902 0.3613  -0.3058 -1.2119 148 ALA L CA  
9265  C C   . ALA D 148 ? 2.9134 4.8156 4.4246 0.3652  -0.2990 -1.1977 148 ALA L C   
9266  O O   . ALA D 148 ? 2.8971 4.7793 4.4077 0.3685  -0.3247 -1.1881 148 ALA L O   
9267  C CB  . ALA D 148 ? 2.9240 4.7612 4.4863 0.3556  -0.3374 -1.2509 148 ALA L CB  
9268  N N   . TRP D 149 ? 2.9722 4.9194 4.4663 0.3645  -0.2644 -1.1957 149 TRP L N   
9269  C CA  . TRP D 149 ? 2.9876 4.9639 4.4625 0.3682  -0.2567 -1.1823 149 TRP L CA  
9270  C C   . TRP D 149 ? 3.1204 5.1019 4.6147 0.3621  -0.2695 -1.2203 149 TRP L C   
9271  O O   . TRP D 149 ? 3.2314 5.2068 4.7491 0.3545  -0.2720 -1.2571 149 TRP L O   
9272  C CB  . TRP D 149 ? 2.8812 4.8994 4.3251 0.3708  -0.2137 -1.1609 149 TRP L CB  
9273  C CG  . TRP D 149 ? 2.7147 4.7281 4.1351 0.3790  -0.1979 -1.1199 149 TRP L CG  
9274  C CD1 . TRP D 149 ? 2.5427 4.5437 3.9626 0.3786  -0.1840 -1.1149 149 TRP L CD1 
9275  C CD2 . TRP D 149 ? 2.5620 4.5845 3.9539 0.3891  -0.1910 -1.0783 149 TRP L CD2 
9276  N NE1 . TRP D 149 ? 2.3363 4.3362 3.7290 0.3884  -0.1694 -1.0726 149 TRP L NE1 
9277  C CE2 . TRP D 149 ? 2.3965 4.4100 3.7719 0.3949  -0.1734 -1.0496 149 TRP L CE2 
9278  C CE3 . TRP D 149 ? 2.5373 4.5736 3.9166 0.3941  -0.1981 -1.0628 149 TRP L CE3 
9279  C CZ2 . TRP D 149 ? 2.3260 4.3439 3.6728 0.4056  -0.1624 -1.0066 149 TRP L CZ2 
9280  C CZ3 . TRP D 149 ? 2.3732 4.4140 3.7252 0.4042  -0.1883 -1.0204 149 TRP L CZ3 
9281  C CH2 . TRP D 149 ? 2.3244 4.3562 3.6604 0.4100  -0.1705 -0.9928 149 TRP L CH2 
9282  N N   . LYS D 150 ? 2.8287 4.8216 4.3132 0.3657  -0.2769 -1.2113 150 LYS L N   
9283  C CA  . LYS D 150 ? 2.9681 4.9648 4.4691 0.3614  -0.2894 -1.2445 150 LYS L CA  
9284  C C   . LYS D 150 ? 2.9726 5.0106 4.4514 0.3639  -0.2713 -1.2328 150 LYS L C   
9285  O O   . LYS D 150 ? 2.8642 4.9079 4.3212 0.3713  -0.2704 -1.1975 150 LYS L O   
9286  C CB  . LYS D 150 ? 2.8745 4.8258 4.3935 0.3630  -0.3281 -1.2513 150 LYS L CB  
9287  C CG  . LYS D 150 ? 2.9346 4.8449 4.4794 0.3593  -0.3461 -1.2733 150 LYS L CG  
9288  C CD  . LYS D 150 ? 2.9465 4.8678 4.5140 0.3516  -0.3377 -1.3186 150 LYS L CD  
9289  C CE  . LYS D 150 ? 2.8742 4.7531 4.4697 0.3486  -0.3570 -1.3439 150 LYS L CE  
9290  N NZ  . LYS D 150 ? 2.9651 4.7956 4.5747 0.3524  -0.3924 -1.3479 150 LYS L NZ  
9291  N N   . ALA D 151 ? 2.8855 4.9515 4.3703 0.3576  -0.2575 -1.2630 151 ALA L N   
9292  C CA  . ALA D 151 ? 2.8321 4.9352 4.3002 0.3587  -0.2442 -1.2599 151 ALA L CA  
9293  C C   . ALA D 151 ? 2.9223 5.0143 4.4095 0.3574  -0.2690 -1.2861 151 ALA L C   
9294  O O   . ALA D 151 ? 3.0277 5.1180 4.5379 0.3505  -0.2728 -1.3260 151 ALA L O   
9295  C CB  . ALA D 151 ? 2.7821 4.9238 4.2409 0.3520  -0.2103 -1.2744 151 ALA L CB  
9296  N N   . ASP D 152 ? 2.9506 5.0344 4.4280 0.3643  -0.2849 -1.2633 152 ASP L N   
9297  C CA  . ASP D 152 ? 2.9832 5.0481 4.4766 0.3647  -0.3106 -1.2808 152 ASP L CA  
9298  C C   . ASP D 152 ? 3.0095 5.0274 4.5307 0.3625  -0.3359 -1.3022 152 ASP L C   
9299  O O   . ASP D 152 ? 2.8966 4.8781 4.4178 0.3663  -0.3546 -1.2812 152 ASP L O   
9300  C CB  . ASP D 152 ? 3.0218 5.1191 4.5208 0.3600  -0.3000 -1.3127 152 ASP L CB  
9301  C CG  . ASP D 152 ? 2.9358 5.0763 4.4068 0.3629  -0.2790 -1.2919 152 ASP L CG  
9302  O OD1 . ASP D 152 ? 2.9021 5.0416 4.3526 0.3703  -0.2806 -1.2538 152 ASP L OD1 
9303  O OD2 . ASP D 152 ? 3.0122 5.1873 4.4815 0.3577  -0.2606 -1.3135 152 ASP L OD2 
9304  N N   . SER D 153 ? 2.8739 4.8912 4.4187 0.3565  -0.3367 -1.3441 153 SER L N   
9305  C CA  . SER D 153 ? 2.8552 4.8291 4.4276 0.3549  -0.3580 -1.3677 153 SER L CA  
9306  C C   . SER D 153 ? 2.8919 4.8733 4.4781 0.3480  -0.3425 -1.3936 153 SER L C   
9307  O O   . SER D 153 ? 2.8029 4.7498 4.4132 0.3466  -0.3578 -1.4153 153 SER L O   
9308  C CB  . SER D 153 ? 2.8880 4.8463 4.4809 0.3555  -0.3764 -1.3966 153 SER L CB  
9309  O OG  . SER D 153 ? 2.8124 4.7657 4.3924 0.3612  -0.3892 -1.3737 153 SER L OG  
9310  N N   . SER D 154 ? 3.0180 5.0430 4.5886 0.3436  -0.3117 -1.3907 154 SER L N   
9311  C CA  . SER D 154 ? 3.0187 5.0590 4.5968 0.3356  -0.2906 -1.4114 154 SER L CA  
9312  C C   . SER D 154 ? 2.9537 4.9909 4.5163 0.3371  -0.2782 -1.3807 154 SER L C   
9313  O O   . SER D 154 ? 2.9055 4.9583 4.4404 0.3428  -0.2670 -1.3422 154 SER L O   
9314  C CB  . SER D 154 ? 3.0412 5.1309 4.6085 0.3294  -0.2629 -1.4254 154 SER L CB  
9315  O OG  . SER D 154 ? 2.9795 5.0730 4.5617 0.3280  -0.2738 -1.4551 154 SER L OG  
9316  N N   . PRO D 155 ? 2.9367 4.9529 4.5170 0.3329  -0.2797 -1.3964 155 PRO L N   
9317  C CA  . PRO D 155 ? 2.8981 4.9096 4.4652 0.3344  -0.2672 -1.3687 155 PRO L CA  
9318  C C   . PRO D 155 ? 2.9274 4.9827 4.4699 0.3309  -0.2274 -1.3562 155 PRO L C   
9319  O O   . PRO D 155 ? 2.9024 4.9876 4.4453 0.3237  -0.2097 -1.3794 155 PRO L O   
9320  C CB  . PRO D 155 ? 2.8890 4.8673 4.4855 0.3297  -0.2798 -1.3971 155 PRO L CB  
9321  C CG  . PRO D 155 ? 2.9261 4.9111 4.5464 0.3230  -0.2824 -1.4435 155 PRO L CG  
9322  C CD  . PRO D 155 ? 2.9253 4.9191 4.5394 0.3274  -0.2931 -1.4410 155 PRO L CD  
9323  N N   . VAL D 156 ? 2.9523 5.0090 4.4714 0.3363  -0.2125 -1.3180 156 VAL L N   
9324  C CA  . VAL D 156 ? 2.9235 5.0140 4.4137 0.3348  -0.1720 -1.2995 156 VAL L CA  
9325  C C   . VAL D 156 ? 2.9565 5.0344 4.4556 0.3289  -0.1585 -1.3094 156 VAL L C   
9326  O O   . VAL D 156 ? 2.8913 4.9385 4.3985 0.3327  -0.1724 -1.2983 156 VAL L O   
9327  C CB  . VAL D 156 ? 2.7545 4.8533 4.2097 0.3459  -0.1601 -1.2492 156 VAL L CB  
9328  C CG1 . VAL D 156 ? 2.6821 4.8077 4.1037 0.3452  -0.1164 -1.2289 156 VAL L CG1 
9329  C CG2 . VAL D 156 ? 2.6612 4.7719 4.1084 0.3514  -0.1738 -1.2397 156 VAL L CG2 
9330  N N   . LYS D 157 ? 2.8209 4.9209 4.3177 0.3191  -0.1315 -1.3300 157 LYS L N   
9331  C CA  . LYS D 157 ? 2.8367 4.9249 4.3435 0.3116  -0.1176 -1.3441 157 LYS L CA  
9332  C C   . LYS D 157 ? 2.7762 4.8686 4.2455 0.3154  -0.0818 -1.3046 157 LYS L C   
9333  O O   . LYS D 157 ? 2.6278 4.6955 4.1000 0.3183  -0.0831 -1.2927 157 LYS L O   
9334  C CB  . LYS D 157 ? 2.8155 4.9216 4.3378 0.2978  -0.1058 -1.3861 157 LYS L CB  
9335  C CG  . LYS D 157 ? 2.8437 4.9408 4.4040 0.2939  -0.1388 -1.4294 157 LYS L CG  
9336  C CD  . LYS D 157 ? 2.9536 5.0719 4.5269 0.2799  -0.1232 -1.4692 157 LYS L CD  
9337  C CE  . LYS D 157 ? 3.0437 5.1494 4.6546 0.2769  -0.1535 -1.5140 157 LYS L CE  
9338  N NZ  . LYS D 157 ? 3.0149 5.0896 4.6356 0.2889  -0.1891 -1.5040 157 LYS L NZ  
9339  N N   . ALA D 158 ? 2.9164 5.0369 4.3485 0.3159  -0.0492 -1.2833 158 ALA L N   
9340  C CA  . ALA D 158 ? 2.8212 4.9407 4.2113 0.3193  -0.0112 -1.2456 158 ALA L CA  
9341  C C   . ALA D 158 ? 2.6540 4.7794 4.0108 0.3330  -0.0064 -1.2003 158 ALA L C   
9342  O O   . ALA D 158 ? 2.6496 4.7859 4.0126 0.3385  -0.0280 -1.1983 158 ALA L O   
9343  C CB  . ALA D 158 ? 2.8269 4.9658 4.1917 0.3088  0.0275  -1.2518 158 ALA L CB  
9344  N N   . GLY D 159 ? 3.0020 5.1175 4.3218 0.3384  0.0232  -1.1636 159 GLY L N   
9345  C CA  . GLY D 159 ? 2.8633 4.9814 4.1474 0.3514  0.0333  -1.1181 159 GLY L CA  
9346  C C   . GLY D 159 ? 2.7588 4.8535 4.0569 0.3615  0.0075  -1.1005 159 GLY L C   
9347  O O   . GLY D 159 ? 2.6230 4.7189 3.8949 0.3727  0.0126  -1.0627 159 GLY L O   
9348  N N   . VAL D 160 ? 2.9397 5.0118 4.2782 0.3577  -0.0206 -1.1264 160 VAL L N   
9349  C CA  . VAL D 160 ? 2.7646 4.8106 4.1186 0.3662  -0.0488 -1.1117 160 VAL L CA  
9350  C C   . VAL D 160 ? 2.6829 4.7080 4.0185 0.3690  -0.0250 -1.0905 160 VAL L C   
9351  O O   . VAL D 160 ? 2.7503 4.7654 4.0945 0.3607  -0.0129 -1.1108 160 VAL L O   
9352  C CB  . VAL D 160 ? 2.6876 4.7143 4.0922 0.3608  -0.0948 -1.1497 160 VAL L CB  
9353  C CG1 . VAL D 160 ? 2.5637 4.6055 3.9792 0.3602  -0.1176 -1.1633 160 VAL L CG1 
9354  C CG2 . VAL D 160 ? 2.8139 4.8351 4.2432 0.3486  -0.0911 -1.1896 160 VAL L CG2 
9355  N N   . GLU D 161 ? 2.8017 4.8198 4.1100 0.3806  -0.0167 -1.0490 161 GLU L N   
9356  C CA  . GLU D 161 ? 2.6425 4.6381 3.9286 0.3855  0.0056  -1.0235 161 GLU L CA  
9357  C C   . GLU D 161 ? 2.4544 4.4289 3.7574 0.3950  -0.0263 -1.0070 161 GLU L C   
9358  O O   . GLU D 161 ? 2.3595 4.3421 3.6510 0.4034  -0.0357 -0.9825 161 GLU L O   
9359  C CB  . GLU D 161 ? 2.5895 4.5947 3.8157 0.3893  0.0551  -0.9867 161 GLU L CB  
9360  C CG  . GLU D 161 ? 2.7227 4.7464 3.9375 0.3776  0.0789  -1.0079 161 GLU L CG  
9361  C CD  . GLU D 161 ? 2.8713 4.8804 4.0458 0.3722  0.1233  -0.9953 161 GLU L CD  
9362  O OE1 . GLU D 161 ? 2.8770 4.8777 4.0018 0.3790  0.1536  -0.9545 161 GLU L OE1 
9363  O OE2 . GLU D 161 ? 3.0801 5.0836 4.2717 0.3605  0.1274  -1.0261 161 GLU L OE2 
9364  N N   . THR D 162 ? 2.6505 4.5966 3.9801 0.3933  -0.0435 -1.0200 162 THR L N   
9365  C CA  . THR D 162 ? 2.5973 4.5179 3.9475 0.4002  -0.0795 -1.0092 162 THR L CA  
9366  C C   . THR D 162 ? 2.5810 4.4543 3.8967 0.4005  -0.0625 -0.9791 162 THR L C   
9367  O O   . THR D 162 ? 2.6179 4.4742 3.9267 0.3933  -0.0428 -0.9895 162 THR L O   
9368  C CB  . THR D 162 ? 2.6202 4.5207 4.0221 0.3918  -0.1285 -1.0492 162 THR L CB  
9369  O OG1 . THR D 162 ? 2.6743 4.5946 4.0879 0.3859  -0.1422 -1.0721 162 THR L OG1 
9370  C CG2 . THR D 162 ? 2.5736 4.4420 3.9918 0.3972  -0.1691 -1.0363 162 THR L CG2 
9371  N N   . THR D 163 ? 2.8165 4.6528 4.0968 0.4048  -0.0701 -0.9362 163 THR L N   
9372  C CA  . THR D 163 ? 2.7005 4.4717 3.9305 0.4012  -0.0559 -0.8981 163 THR L CA  
9373  C C   . THR D 163 ? 2.6963 4.4170 3.9543 0.3938  -0.0951 -0.9154 163 THR L C   
9374  O O   . THR D 163 ? 2.6917 4.4239 4.0046 0.3931  -0.1377 -0.9500 163 THR L O   
9375  C CB  . THR D 163 ? 2.5260 4.2766 3.7104 0.4081  -0.0510 -0.8472 163 THR L CB  
9376  O OG1 . THR D 163 ? 2.6392 4.4461 3.8182 0.4167  -0.0333 -0.8411 163 THR L OG1 
9377  C CG2 . THR D 163 ? 2.2843 3.9834 3.4036 0.4059  -0.0163 -0.8026 163 THR L CG2 
9378  N N   . THR D 164 ? 2.6807 4.3462 3.9011 0.3886  -0.0811 -0.8920 164 THR L N   
9379  C CA  . THR D 164 ? 2.7140 4.3217 3.9491 0.3813  -0.1145 -0.9008 164 THR L CA  
9380  C C   . THR D 164 ? 2.6555 4.2119 3.8644 0.3830  -0.1379 -0.8637 164 THR L C   
9381  O O   . THR D 164 ? 2.6536 4.1993 3.8116 0.3873  -0.1126 -0.8193 164 THR L O   
9382  C CB  . THR D 164 ? 2.8291 4.4009 4.0366 0.3738  -0.0861 -0.8962 164 THR L CB  
9383  O OG1 . THR D 164 ? 2.7716 4.2786 3.9825 0.3672  -0.1172 -0.8955 164 THR L OG1 
9384  C CG2 . THR D 164 ? 2.8203 4.3799 3.9577 0.3763  -0.0359 -0.8477 164 THR L CG2 
9385  N N   . PRO D 165 ? 2.6167 4.1425 3.8610 0.3794  -0.1866 -0.8829 165 PRO L N   
9386  C CA  . PRO D 165 ? 2.5800 4.0536 3.8016 0.3796  -0.2123 -0.8510 165 PRO L CA  
9387  C C   . PRO D 165 ? 2.5761 3.9923 3.7295 0.3766  -0.1815 -0.8019 165 PRO L C   
9388  O O   . PRO D 165 ? 2.6129 4.0072 3.7460 0.3713  -0.1567 -0.8004 165 PRO L O   
9389  C CB  . PRO D 165 ? 2.5977 4.0405 3.8665 0.3736  -0.2644 -0.8857 165 PRO L CB  
9390  C CG  . PRO D 165 ? 2.6251 4.1301 3.9563 0.3746  -0.2740 -0.9392 165 PRO L CG  
9391  C CD  . PRO D 165 ? 2.6491 4.1906 3.9590 0.3753  -0.2217 -0.9373 165 PRO L CD  
9392  N N   . SER D 166 ? 2.8041 4.1956 3.9222 0.3799  -0.1830 -0.7618 166 SER L N   
9393  C CA  . SER D 166 ? 2.8275 4.1661 3.8798 0.3776  -0.1528 -0.7130 166 SER L CA  
9394  C C   . SER D 166 ? 2.8032 4.0995 3.8324 0.3781  -0.1740 -0.6798 166 SER L C   
9395  O O   . SER D 166 ? 2.7969 4.1249 3.8244 0.3855  -0.1731 -0.6657 166 SER L O   
9396  C CB  . SER D 166 ? 2.7994 4.1753 3.8140 0.3835  -0.0993 -0.6891 166 SER L CB  
9397  O OG  . SER D 166 ? 2.6672 4.0969 3.6934 0.3927  -0.0991 -0.6864 166 SER L OG  
9398  N N   . LYS D 167 ? 2.8946 4.1193 3.9062 0.3700  -0.1931 -0.6682 167 LYS L N   
9399  C CA  . LYS D 167 ? 2.8526 4.0309 3.8412 0.3688  -0.2143 -0.6380 167 LYS L CA  
9400  C C   . LYS D 167 ? 2.9215 4.0877 3.8498 0.3724  -0.1746 -0.5860 167 LYS L C   
9401  O O   . LYS D 167 ? 2.9502 4.1146 3.8414 0.3725  -0.1317 -0.5663 167 LYS L O   
9402  C CB  . LYS D 167 ? 2.8803 3.9793 3.8555 0.3581  -0.2373 -0.6352 167 LYS L CB  
9403  C CG  . LYS D 167 ? 2.7802 3.8617 3.8048 0.3532  -0.2904 -0.6744 167 LYS L CG  
9404  C CD  . LYS D 167 ? 2.7926 3.7924 3.7957 0.3424  -0.3066 -0.6681 167 LYS L CD  
9405  C CE  . LYS D 167 ? 2.7952 3.7610 3.7407 0.3389  -0.2606 -0.6339 167 LYS L CE  
9406  N NZ  . LYS D 167 ? 2.7980 3.6817 3.7198 0.3284  -0.2772 -0.6252 167 LYS L NZ  
9407  N N   . GLN D 168 ? 2.8558 4.0139 3.7752 0.3753  -0.1897 -0.5636 168 GLN L N   
9408  C CA  . GLN D 168 ? 2.8611 4.0072 3.7271 0.3790  -0.1565 -0.5142 168 GLN L CA  
9409  C C   . GLN D 168 ? 2.9040 3.9882 3.7498 0.3736  -0.1825 -0.4896 168 GLN L C   
9410  O O   . GLN D 168 ? 2.7864 3.8863 3.6461 0.3775  -0.2027 -0.4861 168 GLN L O   
9411  C CB  . GLN D 168 ? 2.7655 3.9824 3.6387 0.3906  -0.1368 -0.5093 168 GLN L CB  
9412  C CG  . GLN D 168 ? 2.7769 4.0498 3.6569 0.3955  -0.1030 -0.5255 168 GLN L CG  
9413  C CD  . GLN D 168 ? 2.7707 4.1125 3.6594 0.4068  -0.0875 -0.5228 168 GLN L CD  
9414  O OE1 . GLN D 168 ? 2.7582 4.1190 3.6690 0.4111  -0.1131 -0.5253 168 GLN L OE1 
9415  N NE2 . GLN D 168 ? 2.8505 4.2285 3.7201 0.4115  -0.0455 -0.5172 168 GLN L NE2 
9416  N N   . SER D 169 ? 2.9378 3.9507 3.7498 0.3641  -0.1816 -0.4725 169 SER L N   
9417  C CA  . SER D 169 ? 2.9438 3.8907 3.7287 0.3574  -0.2017 -0.4460 169 SER L CA  
9418  C C   . SER D 169 ? 2.8970 3.8414 3.7241 0.3558  -0.2552 -0.4709 169 SER L C   
9419  O O   . SER D 169 ? 2.8476 3.7620 3.6584 0.3538  -0.2694 -0.4488 169 SER L O   
9420  C CB  . SER D 169 ? 2.8522 3.7970 3.5906 0.3619  -0.1682 -0.3988 169 SER L CB  
9421  O OG  . SER D 169 ? 2.9320 3.8128 3.6437 0.3546  -0.1861 -0.3737 169 SER L OG  
9422  N N   . ASN D 170 ? 2.9103 3.8840 3.7916 0.3562  -0.2857 -0.5168 170 ASN L N   
9423  C CA  . ASN D 170 ? 2.8212 3.7947 3.7434 0.3553  -0.3368 -0.5409 170 ASN L CA  
9424  C C   . ASN D 170 ? 2.7502 3.7430 3.7275 0.3538  -0.3675 -0.5921 170 ASN L C   
9425  O O   . ASN D 170 ? 2.6813 3.6750 3.6601 0.3517  -0.3508 -0.6057 170 ASN L O   
9426  C CB  . ASN D 170 ? 2.7593 3.7938 3.6993 0.3653  -0.3355 -0.5377 170 ASN L CB  
9427  C CG  . ASN D 170 ? 2.7489 3.7480 3.6718 0.3629  -0.3559 -0.5131 170 ASN L CG  
9428  O OD1 . ASN D 170 ? 2.8014 3.7362 3.7159 0.3536  -0.3861 -0.5114 170 ASN L OD1 
9429  N ND2 . ASN D 170 ? 2.6730 3.7129 3.5890 0.3711  -0.3385 -0.4932 170 ASN L ND2 
9430  N N   . ASN D 171 ? 2.8353 3.8428 3.8587 0.3547  -0.4128 -0.6209 171 ASN L N   
9431  C CA  . ASN D 171 ? 2.8679 3.9068 3.9507 0.3551  -0.4418 -0.6722 171 ASN L CA  
9432  C C   . ASN D 171 ? 2.8162 3.9434 3.9317 0.3652  -0.4209 -0.6926 171 ASN L C   
9433  O O   . ASN D 171 ? 2.8577 4.0202 4.0196 0.3661  -0.4329 -0.7344 171 ASN L O   
9434  C CB  . ASN D 171 ? 3.0092 4.0269 4.1293 0.3519  -0.5001 -0.6966 171 ASN L CB  
9435  C CG  . ASN D 171 ? 2.9935 4.0490 4.1282 0.3586  -0.5132 -0.6915 171 ASN L CG  
9436  O OD1 . ASN D 171 ? 3.0697 4.1951 4.2215 0.3678  -0.4931 -0.6964 171 ASN L OD1 
9437  N ND2 . ASN D 171 ? 2.8804 3.8882 4.0087 0.3536  -0.5483 -0.6825 171 ASN L ND2 
9438  N N   . LYS D 172 ? 2.9081 4.0693 3.9991 0.3725  -0.3903 -0.6634 172 LYS L N   
9439  C CA  . LYS D 172 ? 2.8992 4.1421 4.0126 0.3825  -0.3676 -0.6758 172 LYS L CA  
9440  C C   . LYS D 172 ? 2.8753 4.1411 3.9815 0.3829  -0.3292 -0.6840 172 LYS L C   
9441  O O   . LYS D 172 ? 2.8075 4.0494 3.8633 0.3817  -0.2900 -0.6504 172 LYS L O   
9442  C CB  . LYS D 172 ? 2.8359 4.0979 3.9154 0.3895  -0.3415 -0.6364 172 LYS L CB  
9443  C CG  . LYS D 172 ? 2.8159 4.1568 3.9076 0.3995  -0.3104 -0.6439 172 LYS L CG  
9444  C CD  . LYS D 172 ? 2.6993 4.0572 3.7538 0.4068  -0.2807 -0.6032 172 LYS L CD  
9445  C CE  . LYS D 172 ? 2.6420 3.9684 3.6374 0.4050  -0.2340 -0.5650 172 LYS L CE  
9446  N NZ  . LYS D 172 ? 2.6810 4.0598 3.6559 0.4147  -0.1913 -0.5461 172 LYS L NZ  
9447  N N   . TYR D 173 ? 2.8375 4.1481 3.9938 0.3841  -0.3404 -0.7289 173 TYR L N   
9448  C CA  . TYR D 173 ? 2.7841 4.1269 3.9380 0.3850  -0.3028 -0.7400 173 TYR L CA  
9449  C C   . TYR D 173 ? 2.7377 4.1566 3.9012 0.3950  -0.2793 -0.7415 173 TYR L C   
9450  O O   . TYR D 173 ? 2.6986 4.1486 3.8882 0.4004  -0.3024 -0.7488 173 TYR L O   
9451  C CB  . TYR D 173 ? 2.7911 4.1396 3.9959 0.3800  -0.3282 -0.7898 173 TYR L CB  
9452  C CG  . TYR D 173 ? 2.8022 4.0792 3.9920 0.3701  -0.3397 -0.7886 173 TYR L CG  
9453  C CD1 . TYR D 173 ? 2.8570 4.0766 4.0498 0.3648  -0.3827 -0.7862 173 TYR L CD1 
9454  C CD2 . TYR D 173 ? 2.8222 4.0883 3.9961 0.3658  -0.3100 -0.7915 173 TYR L CD2 
9455  C CE1 . TYR D 173 ? 2.8414 3.9939 4.0205 0.3558  -0.3960 -0.7856 173 TYR L CE1 
9456  C CE2 . TYR D 173 ? 2.9067 4.1066 4.0687 0.3568  -0.3233 -0.7915 173 TYR L CE2 
9457  C CZ  . TYR D 173 ? 2.8458 3.9890 4.0105 0.3519  -0.3667 -0.7886 173 TYR L CZ  
9458  O OH  . TYR D 173 ? 2.6678 3.7430 3.8186 0.3429  -0.3808 -0.7879 173 TYR L OH  
9459  N N   . ALA D 174 ? 2.7278 4.1756 3.8688 0.3975  -0.2336 -0.7342 174 ALA L N   
9460  C CA  . ALA D 174 ? 2.7046 4.2214 3.8489 0.4068  -0.2088 -0.7334 174 ALA L CA  
9461  C C   . ALA D 174 ? 2.7432 4.3131 3.9212 0.4071  -0.1953 -0.7734 174 ALA L C   
9462  O O   . ALA D 174 ? 2.8701 4.4220 4.0417 0.4011  -0.1793 -0.7834 174 ALA L O   
9463  C CB  . ALA D 174 ? 2.6691 4.1774 3.7508 0.4110  -0.1633 -0.6836 174 ALA L CB  
9464  N N   . ALA D 175 ? 3.0555 4.4341 3.2010 -0.5780 -0.4515 -0.8250 175 ALA L N   
9465  C CA  . ALA D 175 ? 3.0664 4.4993 3.2834 -0.5386 -0.4377 -0.7991 175 ALA L CA  
9466  C C   . ALA D 175 ? 3.1326 4.6181 3.3569 -0.4983 -0.3928 -0.8483 175 ALA L C   
9467  O O   . ALA D 175 ? 3.1397 4.6161 3.3587 -0.4932 -0.3712 -0.8860 175 ALA L O   
9468  C CB  . ALA D 175 ? 3.0990 4.5161 3.3894 -0.5364 -0.4503 -0.7532 175 ALA L CB  
9469  N N   . SER D 176 ? 3.0786 4.6188 3.3157 -0.4697 -0.3789 -0.8474 176 SER L N   
9470  C CA  . SER D 176 ? 3.0123 4.6073 3.2590 -0.4291 -0.3367 -0.8908 176 SER L CA  
9471  C C   . SER D 176 ? 3.0933 4.7384 3.4200 -0.3914 -0.3274 -0.8551 176 SER L C   
9472  O O   . SER D 176 ? 3.2183 4.8758 3.5647 -0.3925 -0.3482 -0.8116 176 SER L O   
9473  C CB  . SER D 176 ? 2.8005 4.4175 2.9799 -0.4284 -0.3247 -0.9314 176 SER L CB  
9474  O OG  . SER D 176 ? 2.8002 4.4177 2.9629 -0.4432 -0.3518 -0.8974 176 SER L OG  
9475  N N   . SER D 177 ? 2.8813 4.5555 3.2530 -0.3580 -0.2959 -0.8743 177 SER L N   
9476  C CA  . SER D 177 ? 2.9639 4.6879 3.4134 -0.3185 -0.2817 -0.8469 177 SER L CA  
9477  C C   . SER D 177 ? 2.9545 4.7365 3.4021 -0.2785 -0.2397 -0.8937 177 SER L C   
9478  O O   . SER D 177 ? 2.9384 4.7183 3.3615 -0.2719 -0.2139 -0.9440 177 SER L O   
9479  C CB  . SER D 177 ? 3.0287 4.7351 3.5422 -0.3132 -0.2831 -0.8220 177 SER L CB  
9480  O OG  . SER D 177 ? 3.0698 4.7951 3.5956 -0.2871 -0.2468 -0.8659 177 SER L OG  
9481  N N   . TYR D 178 ? 2.9149 4.7478 3.3873 -0.2521 -0.2329 -0.8776 178 TYR L N   
9482  C CA  . TYR D 178 ? 2.8586 4.7496 3.3295 -0.2135 -0.1946 -0.9186 178 TYR L CA  
9483  C C   . TYR D 178 ? 2.9083 4.8475 3.4622 -0.1710 -0.1757 -0.8960 178 TYR L C   
9484  O O   . TYR D 178 ? 3.0172 4.9571 3.6261 -0.1697 -0.1960 -0.8409 178 TYR L O   
9485  C CB  . TYR D 178 ? 2.8297 4.7449 3.2564 -0.2156 -0.1996 -0.9233 178 TYR L CB  
9486  C CG  . TYR D 178 ? 2.8425 4.7167 3.1832 -0.2538 -0.2140 -0.9516 178 TYR L CG  
9487  C CD1 . TYR D 178 ? 2.7432 4.5681 3.0602 -0.2946 -0.2542 -0.9160 178 TYR L CD1 
9488  C CD2 . TYR D 178 ? 2.8257 4.7106 3.1087 -0.2489 -0.1877 -1.0133 178 TYR L CD2 
9489  C CE1 . TYR D 178 ? 2.6702 4.4568 2.9088 -0.3297 -0.2680 -0.9409 178 TYR L CE1 
9490  C CE2 . TYR D 178 ? 2.7950 4.6420 2.9992 -0.2841 -0.2013 -1.0386 178 TYR L CE2 
9491  C CZ  . TYR D 178 ? 2.7698 4.5678 2.9522 -0.3243 -0.2414 -1.0020 178 TYR L CZ  
9492  O OH  . TYR D 178 ? 2.7262 4.4718 2.8318 -0.3546 -0.2495 -1.0165 178 TYR L OH  
9493  N N   . LEU D 179 ? 2.6494 4.6294 3.2115 -0.1359 -0.1362 -0.9395 179 LEU L N   
9494  C CA  . LEU D 179 ? 2.7115 4.7420 3.3483 -0.0918 -0.1128 -0.9262 179 LEU L CA  
9495  C C   . LEU D 179 ? 2.8003 4.8881 3.4192 -0.0585 -0.0791 -0.9676 179 LEU L C   
9496  O O   . LEU D 179 ? 2.8026 4.8984 3.3911 -0.0477 -0.0503 -1.0224 179 LEU L O   
9497  C CB  . LEU D 179 ? 2.7437 4.7605 3.4192 -0.0813 -0.0972 -0.9368 179 LEU L CB  
9498  C CG  . LEU D 179 ? 2.7994 4.8654 3.5535 -0.0358 -0.0722 -0.9243 179 LEU L CG  
9499  C CD1 . LEU D 179 ? 2.8859 4.9674 3.6991 -0.0296 -0.0946 -0.8592 179 LEU L CD1 
9500  C CD2 . LEU D 179 ? 2.7873 4.8344 3.5735 -0.0290 -0.0582 -0.9369 179 LEU L CD2 
9501  N N   . SER D 180 ? 2.5940 4.7214 3.2324 -0.0427 -0.0833 -0.9406 180 SER L N   
9502  C CA  . SER D 180 ? 2.6054 4.7894 3.2298 -0.0111 -0.0542 -0.9734 180 SER L CA  
9503  C C   . SER D 180 ? 2.7840 5.0163 3.4726 0.0357  -0.0201 -0.9814 180 SER L C   
9504  O O   . SER D 180 ? 2.8833 5.1323 3.6415 0.0525  -0.0260 -0.9360 180 SER L O   
9505  C CB  . SER D 180 ? 2.5166 4.7225 3.1375 -0.0135 -0.0735 -0.9393 180 SER L CB  
9506  O OG  . SER D 180 ? 2.4107 4.5714 2.9703 -0.0568 -0.1048 -0.9333 180 SER L OG  
9507  N N   . LEU D 181 ? 2.6043 4.8589 3.2700 0.0567  0.0155  -1.0385 181 LEU L N   
9508  C CA  . LEU D 181 ? 2.6522 4.9532 3.3731 0.1019  0.0504  -1.0521 181 LEU L CA  
9509  C C   . LEU D 181 ? 2.7338 5.0879 3.4288 0.1314  0.0823  -1.0958 181 LEU L C   
9510  O O   . LEU D 181 ? 2.7402 5.0928 3.3724 0.1161  0.0784  -1.1185 181 LEU L O   
9511  C CB  . LEU D 181 ? 2.6506 4.9258 3.3793 0.1025  0.0662  -1.0805 181 LEU L CB  
9512  C CG  . LEU D 181 ? 2.6971 4.9238 3.4610 0.0801  0.0415  -1.0423 181 LEU L CG  
9513  C CD1 . LEU D 181 ? 2.7103 4.9189 3.4763 0.0853  0.0631  -1.0798 181 LEU L CD1 
9514  C CD2 . LEU D 181 ? 2.7453 4.9960 3.5908 0.1005  0.0324  -0.9843 181 LEU L CD2 
9515  N N   . THR D 182 ? 2.7189 5.1201 3.4635 0.1744  0.1140  -1.1067 182 THR L N   
9516  C CA  . THR D 182 ? 2.7455 5.1996 3.4722 0.2065  0.1476  -1.1492 182 THR L CA  
9517  C C   . THR D 182 ? 2.8009 5.1961 3.4829 0.2056  0.1614  -1.1833 182 THR L C   
9518  O O   . THR D 182 ? 2.8163 5.2098 3.5309 0.2080  0.1721  -1.1959 182 THR L O   
9519  C CB  . THR D 182 ? 2.6949 5.1764 3.4767 0.2437  0.1552  -1.1111 182 THR L CB  
9520  O OG1 . THR D 182 ? 2.7629 5.2434 3.6027 0.2652  0.1696  -1.1030 182 THR L OG1 
9521  C CG2 . THR D 182 ? 2.6196 5.1335 3.4446 0.2386  0.1305  -1.0602 182 THR L CG2 
9522  N N   . PRO D 183 ? 2.9253 5.2669 3.5404 0.1984  0.1556  -1.1892 183 PRO L N   
9523  C CA  . PRO D 183 ? 2.9618 5.2434 3.5478 0.1943  0.1619  -1.2056 183 PRO L CA  
9524  C C   . PRO D 183 ? 3.0472 5.3242 3.6783 0.2238  0.1810  -1.1976 183 PRO L C   
9525  O O   . PRO D 183 ? 3.0337 5.2738 3.6551 0.2188  0.1882  -1.2150 183 PRO L O   
9526  C CB  . PRO D 183 ? 2.9657 5.2100 3.5038 0.1891  0.1517  -1.1946 183 PRO L CB  
9527  C CG  . PRO D 183 ? 2.8698 5.1424 3.3889 0.1735  0.1353  -1.1888 183 PRO L CG  
9528  C CD  . PRO D 183 ? 2.8620 5.1993 3.4340 0.1892  0.1404  -1.1782 183 PRO L CD  
9529  N N   . GLU D 184 ? 2.9713 5.2815 3.6523 0.2537  0.1889  -1.1683 184 GLU L N   
9530  C CA  . GLU D 184 ? 3.0101 5.3140 3.7363 0.2812  0.2068  -1.1571 184 GLU L CA  
9531  C C   . GLU D 184 ? 2.9744 5.3127 3.7641 0.2834  0.2137  -1.1629 184 GLU L C   
9532  O O   . GLU D 184 ? 3.0278 5.3452 3.8354 0.2927  0.2269  -1.1714 184 GLU L O   
9533  C CB  . GLU D 184 ? 3.0439 5.3657 3.8017 0.3110  0.2116  -1.1188 184 GLU L CB  
9534  C CG  . GLU D 184 ? 3.1034 5.3949 3.8058 0.3098  0.2049  -1.1111 184 GLU L CG  
9535  C CD  . GLU D 184 ? 3.2841 5.5957 4.0160 0.3365  0.2086  -1.0736 184 GLU L CD  
9536  O OE1 . GLU D 184 ? 3.3138 5.6647 4.1117 0.3545  0.2143  -1.0503 184 GLU L OE1 
9537  O OE2 . GLU D 184 ? 3.4382 5.7261 4.1311 0.3383  0.2046  -1.0648 184 GLU L OE2 
9538  N N   . GLN D 185 ? 2.9551 5.3487 3.7852 0.2738  0.2037  -1.1557 185 GLN L N   
9539  C CA  . GLN D 185 ? 2.9028 5.3366 3.8087 0.2730  0.2059  -1.1553 185 GLN L CA  
9540  C C   . GLN D 185 ? 2.8729 5.2673 3.7368 0.2462  0.2075  -1.1967 185 GLN L C   
9541  O O   . GLN D 185 ? 2.8649 5.2339 3.7599 0.2445  0.2081  -1.1914 185 GLN L O   
9542  C CB  . GLN D 185 ? 2.8390 5.2636 3.7693 0.2498  0.1686  -1.0976 185 GLN L CB  
9543  C CG  . GLN D 185 ? 2.8392 5.2200 3.8111 0.2326  0.1482  -1.0614 185 GLN L CG  
9544  C CD  . GLN D 185 ? 2.8382 5.2245 3.8717 0.2340  0.1231  -0.9934 185 GLN L CD  
9545  O OE1 . GLN D 185 ? 2.8595 5.2742 3.8977 0.2400  0.1142  -0.9689 185 GLN L OE1 
9546  N NE2 . GLN D 185 ? 2.8781 5.2362 3.9597 0.2278  0.1108  -0.9615 185 GLN L NE2 
9547  N N   . TRP D 186 ? 3.0292 5.3944 3.8114 0.2198  0.2011  -1.2277 186 TRP L N   
9548  C CA  . TRP D 186 ? 2.9489 5.2737 3.6846 0.1917  0.2011  -1.2670 186 TRP L CA  
9549  C C   . TRP D 186 ? 2.9947 5.2669 3.7182 0.2015  0.2132  -1.2773 186 TRP L C   
9550  O O   . TRP D 186 ? 2.9445 5.2039 3.6785 0.1930  0.2200  -1.2996 186 TRP L O   
9551  C CB  . TRP D 186 ? 2.8462 5.1320 3.4925 0.1590  0.1838  -1.2829 186 TRP L CB  
9552  C CG  . TRP D 186 ? 2.8924 5.1165 3.4833 0.1295  0.1791  -1.3117 186 TRP L CG  
9553  C CD1 . TRP D 186 ? 2.8795 5.0445 3.4238 0.1189  0.1741  -1.3104 186 TRP L CD1 
9554  C CD2 . TRP D 186 ? 2.8920 5.0998 3.4776 0.1059  0.1763  -1.3343 186 TRP L CD2 
9555  N NE1 . TRP D 186 ? 2.8744 4.9955 3.3895 0.0921  0.1708  -1.3310 186 TRP L NE1 
9556  C CE2 . TRP D 186 ? 2.8390 4.9830 3.3705 0.0831  0.1720  -1.3516 186 TRP L CE2 
9557  C CE3 . TRP D 186 ? 2.7838 4.9528 3.4044 0.0833  0.1447  -1.2826 186 TRP L CE3 
9558  C CZ2 . TRP D 186 ? 2.7304 4.8381 3.2373 0.0552  0.1669  -1.3760 186 TRP L CZ2 
9559  C CZ3 . TRP D 186 ? 2.7571 4.8681 3.3529 0.0500  0.1298  -1.2893 186 TRP L CZ3 
9560  C CH2 . TRP D 186 ? 2.7436 4.8346 3.2805 0.0388  0.1457  -1.3465 186 TRP L CH2 
9561  N N   . LYS D 187 ? 2.9344 5.1762 3.6363 0.2179  0.2160  -1.2611 187 LYS L N   
9562  C CA  . LYS D 187 ? 2.9662 5.1626 3.6605 0.2268  0.2277  -1.2673 187 LYS L CA  
9563  C C   . LYS D 187 ? 2.9881 5.2085 3.7531 0.2586  0.2451  -1.2529 187 LYS L C   
9564  O O   . LYS D 187 ? 3.0127 5.1998 3.7778 0.2678  0.2566  -1.2581 187 LYS L O   
9565  C CB  . LYS D 187 ? 2.9679 5.1242 3.6176 0.2311  0.2246  -1.2531 187 LYS L CB  
9566  C CG  . LYS D 187 ? 2.9555 5.0798 3.5435 0.1998  0.2076  -1.2619 187 LYS L CG  
9567  C CD  . LYS D 187 ? 2.9605 5.0461 3.5238 0.1744  0.2062  -1.2857 187 LYS L CD  
9568  C CE  . LYS D 187 ? 2.9462 4.9977 3.4575 0.1454  0.1905  -1.2841 187 LYS L CE  
9569  N NZ  . LYS D 187 ? 2.9708 4.9808 3.4598 0.1209  0.1896  -1.3005 187 LYS L NZ  
9570  N N   . SER D 188 ? 2.9044 5.1826 3.7348 0.2749  0.2459  -1.2303 188 SER L N   
9571  C CA  . SER D 188 ? 2.9073 5.2116 3.8164 0.3052  0.2590  -1.2065 188 SER L CA  
9572  C C   . SER D 188 ? 2.8718 5.1857 3.8262 0.3000  0.2656  -1.2252 188 SER L C   
9573  O O   . SER D 188 ? 2.8974 5.1754 3.8464 0.3076  0.2781  -1.2368 188 SER L O   
9574  C CB  . SER D 188 ? 2.8585 5.2228 3.8317 0.3204  0.2518  -1.1676 188 SER L CB  
9575  O OG  . SER D 188 ? 2.8992 5.2536 3.8327 0.3275  0.2472  -1.1494 188 SER L OG  
9576  N N   . HIS D 189 ? 2.8875 5.2349 3.8824 0.2821  0.2512  -1.2186 189 HIS L N   
9577  C CA  . HIS D 189 ? 2.9274 5.2259 3.9415 0.2621  0.2376  -1.2048 189 HIS L CA  
9578  C C   . HIS D 189 ? 2.8682 5.1289 3.8220 0.2408  0.2462  -1.2580 189 HIS L C   
9579  O O   . HIS D 189 ? 2.7555 5.0184 3.6446 0.2322  0.2549  -1.3002 189 HIS L O   
9580  C CB  . HIS D 189 ? 2.9654 5.2245 3.9933 0.2280  0.1947  -1.1456 189 HIS L CB  
9581  C CG  . HIS D 189 ? 2.9108 5.2036 4.0031 0.2480  0.1850  -1.0903 189 HIS L CG  
9582  N ND1 . HIS D 189 ? 2.9853 5.2710 4.1474 0.2554  0.1755  -1.0458 189 HIS L ND1 
9583  C CD2 . HIS D 189 ? 2.7856 5.1194 3.8840 0.2625  0.1836  -1.0721 189 HIS L CD2 
9584  C CE1 . HIS D 189 ? 2.9387 5.2594 4.1471 0.2734  0.1684  -1.0023 189 HIS L CE1 
9585  N NE2 . HIS D 189 ? 2.8459 5.1963 4.0171 0.2780  0.1730  -1.0171 189 HIS L NE2 
9586  N N   . LYS D 190 ? 2.6801 4.9052 3.6567 0.2319  0.2431  -1.2544 190 LYS L N   
9587  C CA  . LYS D 190 ? 2.6884 4.8764 3.6159 0.2133  0.2518  -1.3024 190 LYS L CA  
9588  C C   . LYS D 190 ? 2.7079 4.8455 3.5668 0.1647  0.2223  -1.3047 190 LYS L C   
9589  O O   . LYS D 190 ? 2.7079 4.8363 3.5013 0.1529  0.2326  -1.3534 190 LYS L O   
9590  C CB  . LYS D 190 ? 2.7150 4.8743 3.6886 0.2129  0.2507  -1.2892 190 LYS L CB  
9591  C CG  . LYS D 190 ? 2.7019 4.9026 3.7442 0.2582  0.2791  -1.2879 190 LYS L CG  
9592  C CD  . LYS D 190 ? 2.7327 4.8954 3.8097 0.2500  0.2740  -1.2767 190 LYS L CD  
9593  C CE  . LYS D 190 ? 2.7221 4.9227 3.8744 0.2931  0.2975  -1.2659 190 LYS L CE  
9594  N NZ  . LYS D 190 ? 2.7068 4.9352 3.9162 0.3070  0.2831  -1.2078 190 LYS L NZ  
9595  N N   . SER D 191 ? 2.9660 5.0707 3.8387 0.1364  0.1855  -1.2523 191 SER L N   
9596  C CA  . SER D 191 ? 2.9315 4.9855 3.7425 0.0891  0.1550  -1.2497 191 SER L CA  
9597  C C   . SER D 191 ? 2.9374 4.9774 3.7733 0.0697  0.1177  -1.1855 191 SER L C   
9598  O O   . SER D 191 ? 2.9820 5.0373 3.8866 0.0869  0.1124  -1.1412 191 SER L O   
9599  C CB  . SER D 191 ? 2.9171 4.9150 3.7057 0.0615  0.1489  -1.2687 191 SER L CB  
9600  O OG  . SER D 191 ? 2.8965 4.9089 3.6856 0.0855  0.1840  -1.3181 191 SER L OG  
9601  N N   . TYR D 192 ? 2.9994 5.0108 3.7779 0.0341  0.0922  -1.1814 192 TYR L N   
9602  C CA  . TYR D 192 ? 2.9963 4.9868 3.7864 0.0092  0.0538  -1.1239 192 TYR L CA  
9603  C C   . TYR D 192 ? 2.9918 4.9132 3.7474 -0.0374 0.0245  -1.1164 192 TYR L C   
9604  O O   . TYR D 192 ? 2.9742 4.8681 3.6754 -0.0547 0.0319  -1.1611 192 TYR L O   
9605  C CB  . TYR D 192 ? 2.9530 4.9696 3.7068 0.0073  0.0472  -1.1217 192 TYR L CB  
9606  C CG  . TYR D 192 ? 2.9653 5.0467 3.7694 0.0504  0.0662  -1.1075 192 TYR L CG  
9607  C CD1 . TYR D 192 ? 2.9572 5.0872 3.7561 0.0864  0.1047  -1.1534 192 TYR L CD1 
9608  C CD2 . TYR D 192 ? 2.9778 5.0717 3.8350 0.0549  0.0453  -1.0477 192 TYR L CD2 
9609  C CE1 . TYR D 192 ? 2.9271 5.1163 3.7731 0.1259  0.1220  -1.1395 192 TYR L CE1 
9610  C CE2 . TYR D 192 ? 2.9906 5.1432 3.8946 0.0939  0.0621  -1.0335 192 TYR L CE2 
9611  C CZ  . TYR D 192 ? 2.9446 5.1446 3.8429 0.1293  0.1004  -1.0794 192 TYR L CZ  
9612  O OH  . TYR D 192 ? 2.9138 5.1722 3.8594 0.1682  0.1168  -1.0644 192 TYR L OH  
9613  N N   . SER D 193 ? 3.2734 5.1669 4.0612 -0.0577 -0.0089 -1.0597 193 SER L N   
9614  C CA  . SER D 193 ? 3.1969 5.0245 3.9591 -0.1014 -0.0387 -1.0464 193 SER L CA  
9615  C C   . SER D 193 ? 3.0121 4.8155 3.7563 -0.1335 -0.0781 -1.0018 193 SER L C   
9616  O O   . SER D 193 ? 3.0869 4.9228 3.8619 -0.1195 -0.0855 -0.9664 193 SER L O   
9617  C CB  . SER D 193 ? 3.1404 4.9477 3.9647 -0.0974 -0.0421 -1.0198 193 SER L CB  
9618  O OG  . SER D 193 ? 3.1723 5.0021 4.0165 -0.0668 -0.0060 -1.0593 193 SER L OG  
9619  N N   . CYS D 194 ? 3.1485 4.8947 3.8418 -0.1768 -0.1032 -1.0040 194 CYS L N   
9620  C CA  . CYS D 194 ? 3.1158 4.8319 3.7882 -0.2113 -0.1427 -0.9623 194 CYS L CA  
9621  C C   . CYS D 194 ? 3.1362 4.7928 3.8238 -0.2438 -0.1718 -0.9297 194 CYS L C   
9622  O O   . CYS D 194 ? 3.0519 4.6610 3.6887 -0.2756 -0.1812 -0.9526 194 CYS L O   
9623  C CB  . CYS D 194 ? 3.0126 4.7161 3.5980 -0.2365 -0.1492 -0.9948 194 CYS L CB  
9624  S SG  . CYS D 194 ? 3.1048 4.7694 3.6697 -0.2787 -0.1994 -0.9393 194 CYS L SG  
9625  N N   . GLN D 195 ? 3.0199 4.6792 3.7779 -0.2354 -0.1855 -0.8767 195 GLN L N   
9626  C CA  . GLN D 195 ? 3.0544 4.6598 3.8329 -0.2640 -0.2132 -0.8422 195 GLN L CA  
9627  C C   . GLN D 195 ? 3.0220 4.5938 3.7761 -0.3011 -0.2547 -0.8003 195 GLN L C   
9628  O O   . GLN D 195 ? 3.0301 4.6264 3.8158 -0.2925 -0.2680 -0.7584 195 GLN L O   
9629  C CB  . GLN D 195 ? 3.2412 4.8616 4.1069 -0.2396 -0.2101 -0.8035 195 GLN L CB  
9630  C CG  . GLN D 195 ? 3.3291 4.9797 4.2315 -0.2025 -0.1721 -0.8357 195 GLN L CG  
9631  C CD  . GLN D 195 ? 3.3521 5.0138 4.3404 -0.1821 -0.1742 -0.7903 195 GLN L CD  
9632  O OE1 . GLN D 195 ? 3.4050 5.0522 4.4248 -0.1959 -0.2042 -0.7351 195 GLN L OE1 
9633  N NE2 . GLN D 195 ? 3.3256 5.0124 4.3521 -0.1495 -0.1428 -0.8132 195 GLN L NE2 
9634  N N   . VAL D 196 ? 3.2627 4.7788 3.9605 -0.3420 -0.2750 -0.8115 196 VAL L N   
9635  C CA  . VAL D 196 ? 3.2519 4.7303 3.9195 -0.3806 -0.3151 -0.7755 196 VAL L CA  
9636  C C   . VAL D 196 ? 3.2444 4.6708 3.9417 -0.4068 -0.3433 -0.7355 196 VAL L C   
9637  O O   . VAL D 196 ? 3.2294 4.6172 3.9085 -0.4234 -0.3413 -0.7584 196 VAL L O   
9638  C CB  . VAL D 196 ? 3.1460 4.5990 3.7235 -0.4094 -0.3194 -0.8162 196 VAL L CB  
9639  C CG1 . VAL D 196 ? 2.9421 4.3534 3.4890 -0.4502 -0.3617 -0.7780 196 VAL L CG1 
9640  C CG2 . VAL D 196 ? 2.9925 4.4978 3.5404 -0.3831 -0.2914 -0.8557 196 VAL L CG2 
9641  N N   . THR D 197 ? 3.0869 4.5124 3.8295 -0.4107 -0.3697 -0.6758 197 THR L N   
9642  C CA  . THR D 197 ? 3.1724 4.5517 3.9489 -0.4347 -0.3993 -0.6300 197 THR L CA  
9643  C C   . THR D 197 ? 3.1207 4.4503 3.8454 -0.4809 -0.4383 -0.6089 197 THR L C   
9644  O O   . THR D 197 ? 3.1371 4.4784 3.8586 -0.4861 -0.4574 -0.5778 197 THR L O   
9645  C CB  . THR D 197 ? 3.2349 4.6435 4.0955 -0.4102 -0.4044 -0.5763 197 THR L CB  
9646  O OG1 . THR D 197 ? 3.2985 4.7536 4.2056 -0.3668 -0.3672 -0.5977 197 THR L OG1 
9647  C CG2 . THR D 197 ? 3.1870 4.5470 4.0822 -0.4352 -0.4345 -0.5304 197 THR L CG2 
9648  N N   . HIS D 198 ? 3.2428 4.5171 3.9271 -0.5142 -0.4502 -0.6253 198 HIS L N   
9649  C CA  . HIS D 198 ? 3.2206 4.4425 3.8541 -0.5599 -0.4873 -0.6073 198 HIS L CA  
9650  C C   . HIS D 198 ? 3.4530 4.6225 4.1151 -0.5852 -0.5130 -0.5717 198 HIS L C   
9651  O O   . HIS D 198 ? 3.5678 4.7173 4.2367 -0.5854 -0.5001 -0.5945 198 HIS L O   
9652  C CB  . HIS D 198 ? 3.0804 4.2813 3.6285 -0.5802 -0.4791 -0.6632 198 HIS L CB  
9653  C CG  . HIS D 198 ? 3.1160 4.2588 3.6092 -0.6282 -0.5156 -0.6492 198 HIS L CG  
9654  N ND1 . HIS D 198 ? 3.1546 4.2431 3.6123 -0.6587 -0.5241 -0.6681 198 HIS L ND1 
9655  C CD2 . HIS D 198 ? 3.1143 4.2444 3.5825 -0.6509 -0.5460 -0.6176 198 HIS L CD2 
9656  C CE1 . HIS D 198 ? 3.1448 4.1899 3.5574 -0.6979 -0.5579 -0.6491 198 HIS L CE1 
9657  N NE2 . HIS D 198 ? 3.1141 4.1832 3.5321 -0.6941 -0.5719 -0.6183 198 HIS L NE2 
9658  N N   . GLU D 199 ? 3.1350 4.2823 3.8138 -0.6066 -0.5494 -0.5161 199 GLU L N   
9659  C CA  . GLU D 199 ? 3.2468 4.3443 3.9546 -0.6318 -0.5771 -0.4767 199 GLU L CA  
9660  C C   . GLU D 199 ? 3.3692 4.4836 4.1514 -0.6032 -0.5586 -0.4671 199 GLU L C   
9661  O O   . GLU D 199 ? 3.4772 4.6214 4.3253 -0.5808 -0.5606 -0.4262 199 GLU L O   
9662  C CB  . GLU D 199 ? 3.1601 4.1960 3.8049 -0.6724 -0.5911 -0.5014 199 GLU L CB  
9663  C CG  . GLU D 199 ? 3.1308 4.1379 3.7059 -0.7079 -0.6180 -0.4995 199 GLU L CG  
9664  C CD  . GLU D 199 ? 3.1579 4.1466 3.7568 -0.7274 -0.6575 -0.4351 199 GLU L CD  
9665  O OE1 . GLU D 199 ? 3.1996 4.1398 3.8117 -0.7543 -0.6837 -0.4043 199 GLU L OE1 
9666  O OE2 . GLU D 199 ? 3.1397 4.1618 3.7437 -0.7164 -0.6625 -0.4153 199 GLU L OE2 
9667  N N   . GLY D 200 ? 3.3036 4.3991 4.0749 -0.6039 -0.5402 -0.5054 200 GLY L N   
9668  C CA  . GLY D 200 ? 3.3228 4.4292 4.1589 -0.5793 -0.5223 -0.5010 200 GLY L CA  
9669  C C   . GLY D 200 ? 3.2186 4.3591 4.0507 -0.5476 -0.4789 -0.5582 200 GLY L C   
9670  O O   . GLY D 200 ? 3.2777 4.4408 4.1684 -0.5186 -0.4588 -0.5560 200 GLY L O   
9671  N N   . SER D 201 ? 3.3538 4.4984 4.1180 -0.5523 -0.4639 -0.6095 201 SER L N   
9672  C CA  . SER D 201 ? 3.2338 4.4092 3.9899 -0.5235 -0.4229 -0.6661 201 SER L CA  
9673  C C   . SER D 201 ? 3.2082 4.4477 3.9676 -0.4883 -0.3986 -0.6817 201 SER L C   
9674  O O   . SER D 201 ? 3.1783 4.4333 3.9291 -0.4916 -0.4142 -0.6570 201 SER L O   
9675  C CB  . SER D 201 ? 3.1967 4.3352 3.8756 -0.5501 -0.4186 -0.7177 201 SER L CB  
9676  O OG  . SER D 201 ? 3.0415 4.1727 3.6557 -0.5722 -0.4333 -0.7257 201 SER L OG  
9677  N N   . THR D 202 ? 3.0682 4.3449 3.8403 -0.4541 -0.3600 -0.7235 202 THR L N   
9678  C CA  . THR D 202 ? 3.0513 4.3907 3.8276 -0.4176 -0.3326 -0.7440 202 THR L CA  
9679  C C   . THR D 202 ? 3.0104 4.3635 3.7454 -0.4038 -0.2971 -0.8122 202 THR L C   
9680  O O   . THR D 202 ? 3.0520 4.4084 3.8150 -0.3863 -0.2748 -0.8331 202 THR L O   
9681  C CB  . THR D 202 ? 3.1121 4.4968 3.9732 -0.3787 -0.3206 -0.7107 202 THR L CB  
9682  O OG1 . THR D 202 ? 3.2221 4.5932 4.1202 -0.3927 -0.3547 -0.6466 202 THR L OG1 
9683  C CG2 . THR D 202 ? 3.0646 4.5144 3.9294 -0.3407 -0.2918 -0.7328 202 THR L CG2 
9684  N N   . VAL D 203 ? 3.2338 4.5944 3.9025 -0.4120 -0.2922 -0.8466 203 VAL L N   
9685  C CA  . VAL D 203 ? 3.1258 4.5000 3.7479 -0.4009 -0.2597 -0.9126 203 VAL L CA  
9686  C C   . VAL D 203 ? 3.1977 4.6406 3.8415 -0.3564 -0.2276 -0.9307 203 VAL L C   
9687  O O   . VAL D 203 ? 3.2266 4.6992 3.8778 -0.3480 -0.2356 -0.9058 203 VAL L O   
9688  C CB  . VAL D 203 ? 2.9594 4.2998 3.4938 -0.4371 -0.2732 -0.9407 203 VAL L CB  
9689  C CG1 . VAL D 203 ? 2.9004 4.2500 3.3870 -0.4278 -0.2404 -1.0093 203 VAL L CG1 
9690  C CG2 . VAL D 203 ? 2.9002 4.1730 3.4161 -0.4823 -0.3093 -0.9146 203 VAL L CG2 
9691  N N   . GLU D 204 ? 2.9369 4.4055 3.5915 -0.3273 -0.1913 -0.9737 204 GLU L N   
9692  C CA  . GLU D 204 ? 3.0061 4.5402 3.6829 -0.2832 -0.1585 -0.9937 204 GLU L CA  
9693  C C   . GLU D 204 ? 2.9407 4.4881 3.5614 -0.2746 -0.1273 -1.0622 204 GLU L C   
9694  O O   . GLU D 204 ? 2.9000 4.4250 3.5086 -0.2784 -0.1136 -1.0959 204 GLU L O   
9695  C CB  . GLU D 204 ? 3.1675 4.7303 3.9278 -0.2478 -0.1420 -0.9729 204 GLU L CB  
9696  C CG  . GLU D 204 ? 3.2595 4.8883 4.0460 -0.2000 -0.1044 -0.9980 204 GLU L CG  
9697  C CD  . GLU D 204 ? 3.4209 5.0741 4.2896 -0.1668 -0.0896 -0.9763 204 GLU L CD  
9698  O OE1 . GLU D 204 ? 3.5530 5.1746 4.4618 -0.1809 -0.1116 -0.9347 204 GLU L OE1 
9699  O OE2 . GLU D 204 ? 3.3848 5.0889 4.2784 -0.1266 -0.0563 -1.0001 204 GLU L OE2 
9700  N N   . LYS D 205 ? 2.9491 4.5329 3.5357 -0.2632 -0.1164 -1.0825 205 LYS L N   
9701  C CA  . LYS D 205 ? 2.9176 4.5232 3.4538 -0.2503 -0.0850 -1.1462 205 LYS L CA  
9702  C C   . LYS D 205 ? 2.9156 4.5902 3.4847 -0.2044 -0.0561 -1.1543 205 LYS L C   
9703  O O   . LYS D 205 ? 2.9112 4.6126 3.5066 -0.1951 -0.0675 -1.1165 205 LYS L O   
9704  C CB  . LYS D 205 ? 2.8668 4.4459 3.3190 -0.2846 -0.1005 -1.1676 205 LYS L CB  
9705  C CG  . LYS D 205 ? 2.8667 4.3792 3.2752 -0.3271 -0.1202 -1.1774 205 LYS L CG  
9706  C CD  . LYS D 205 ? 2.8178 4.3079 3.1404 -0.3574 -0.1302 -1.2065 205 LYS L CD  
9707  C CE  . LYS D 205 ? 2.8037 4.2631 3.0753 -0.3723 -0.1160 -1.2605 205 LYS L CE  
9708  N NZ  . LYS D 205 ? 2.8081 4.2002 3.0521 -0.4173 -0.1475 -1.2450 205 LYS L NZ  
9709  N N   . THR D 206 ? 2.8778 4.5812 3.4452 -0.1759 -0.0188 -1.2035 206 THR L N   
9710  C CA  . THR D 206 ? 2.8861 4.6550 3.4879 -0.1294 0.0128  -1.2161 206 THR L CA  
9711  C C   . THR D 206 ? 2.8481 4.6451 3.3889 -0.1205 0.0360  -1.2700 206 THR L C   
9712  O O   . THR D 206 ? 2.8163 4.5820 3.2875 -0.1500 0.0284  -1.2990 206 THR L O   
9713  C CB  . THR D 206 ? 2.9354 4.7199 3.5939 -0.0986 0.0391  -1.2265 206 THR L CB  
9714  O OG1 . THR D 206 ? 2.9341 4.6968 3.5515 -0.1055 0.0575  -1.2805 206 THR L OG1 
9715  C CG2 . THR D 206 ? 2.9774 4.7326 3.6951 -0.1085 0.0157  -1.1734 206 THR L CG2 
9716  N N   . VAL D 207 ? 2.9590 4.8160 3.5275 -0.0788 0.0647  -1.2826 207 VAL L N   
9717  C CA  . VAL D 207 ? 2.9367 4.8288 3.4564 -0.0635 0.0904  -1.3328 207 VAL L CA  
9718  C C   . VAL D 207 ? 3.0960 5.0482 3.6639 -0.0128 0.1278  -1.3500 207 VAL L C   
9719  O O   . VAL D 207 ? 3.1526 5.1345 3.7859 0.0114  0.1276  -1.3107 207 VAL L O   
9720  C CB  . VAL D 207 ? 2.7435 4.6451 3.2264 -0.0777 0.0711  -1.3161 207 VAL L CB  
9721  C CG1 . VAL D 207 ? 2.7595 4.6900 3.3047 -0.0615 0.0571  -1.2576 207 VAL L CG1 
9722  C CG2 . VAL D 207 ? 2.6940 4.6336 3.1278 -0.0606 0.0986  -1.3683 207 VAL L CG2 
9723  N N   . ALA D 208 ? 2.9729 4.9428 3.5071 0.0031  0.1601  -1.4093 208 ALA L N   
9724  C CA  . ALA D 208 ? 2.9636 4.9881 3.5336 0.0502  0.1989  -1.4358 208 ALA L CA  
9725  C C   . ALA D 208 ? 2.9319 4.9437 3.4639 0.0519  0.1972  -1.4224 208 ALA L C   
9726  O O   . ALA D 208 ? 2.8753 4.8381 3.3551 0.0222  0.1832  -1.4175 208 ALA L O   
9727  C CB  . ALA D 208 ? 2.9665 4.9715 3.5518 0.0580  0.2177  -1.4619 208 ALA L CB  
9728  N N   . PRO D 209 ? 2.9704 5.0133 3.5324 0.0840  0.2067  -1.4014 209 PRO L N   
9729  C CA  . PRO D 209 ? 3.0087 5.0263 3.5370 0.0836  0.2002  -1.3784 209 PRO L CA  
9730  C C   . PRO D 209 ? 3.0924 5.0560 3.5995 0.0773  0.2047  -1.3780 209 PRO L C   
9731  O O   . PRO D 209 ? 3.1220 5.0704 3.6435 0.0787  0.2144  -1.3938 209 PRO L O   
9732  C CB  . PRO D 209 ? 3.0106 5.0678 3.5777 0.1208  0.2100  -1.3582 209 PRO L CB  
9733  C CG  . PRO D 209 ? 2.9744 5.0891 3.5973 0.1366  0.2178  -1.3634 209 PRO L CG  
9734  C CD  . PRO D 209 ? 2.9909 5.0926 3.6224 0.1216  0.2224  -1.3914 209 PRO L CD  
9735  N N   . THR D 210 ? 3.1590 5.0946 3.6339 0.0713  0.1982  -1.3580 210 THR L N   
9736  C CA  . THR D 210 ? 3.1426 5.0289 3.5973 0.0662  0.2027  -1.3529 210 THR L CA  
9737  C C   . THR D 210 ? 3.1573 5.0385 3.6157 0.0905  0.2093  -1.3332 210 THR L C   
9738  O O   . THR D 210 ? 3.1316 5.0396 3.5978 0.1059  0.2069  -1.3190 210 THR L O   
9739  C CB  . THR D 210 ? 2.9702 4.8150 3.3809 0.0348  0.1910  -1.3439 210 THR L CB  
9740  O OG1 . THR D 210 ? 2.9075 4.7463 3.3073 0.0098  0.1840  -1.3597 210 THR L OG1 
9741  C CG2 . THR D 210 ? 2.9168 4.7136 3.3107 0.0319  0.1974  -1.3373 210 THR L CG2 
9742  N N   . GLN E 1   ? 2.4691 2.2342 2.2507 -0.8908 0.0439  0.1030  1   GLN E N   
9743  C CA  . GLN E 1   ? 2.4204 2.1937 2.1988 -0.8889 0.0248  0.1063  1   GLN E CA  
9744  C C   . GLN E 1   ? 2.4184 2.2096 2.1606 -0.8911 -0.0039 0.0973  1   GLN E C   
9745  O O   . GLN E 1   ? 2.4000 2.1955 2.1087 -0.8917 -0.0168 0.0887  1   GLN E O   
9746  C CB  . GLN E 1   ? 2.4509 2.2273 2.3083 -0.8815 0.0226  0.1370  1   GLN E CB  
9747  C CG  . GLN E 1   ? 2.5108 2.2716 2.4251 -0.8768 0.0546  0.1555  1   GLN E CG  
9748  C CD  . GLN E 1   ? 2.6205 2.3747 2.5487 -0.8772 0.0737  0.1568  1   GLN E CD  
9749  O OE1 . GLN E 1   ? 2.7204 2.4855 2.6482 -0.8789 0.0605  0.1558  1   GLN E OE1 
9750  N NE2 . GLN E 1   ? 2.5469 2.2830 2.4872 -0.8755 0.1034  0.1606  1   GLN E NE2 
9751  N N   . GLU E 2   ? 2.0424 1.8434 1.7927 -0.8919 -0.0134 0.1012  2   GLU E N   
9752  C CA  . GLU E 2   ? 2.0387 1.8554 1.7635 -0.8930 -0.0398 0.0983  2   GLU E CA  
9753  C C   . GLU E 2   ? 2.0196 1.8368 1.6699 -0.8993 -0.0340 0.0708  2   GLU E C   
9754  O O   . GLU E 2   ? 2.0448 1.8591 1.6784 -0.9034 -0.0222 0.0618  2   GLU E O   
9755  C CB  . GLU E 2   ? 2.0875 1.9126 1.8539 -0.8917 -0.0518 0.1162  2   GLU E CB  
9756  C CG  . GLU E 2   ? 2.1282 1.9525 1.9739 -0.8858 -0.0512 0.1444  2   GLU E CG  
9757  C CD  . GLU E 2   ? 2.1840 2.0181 2.0660 -0.8852 -0.0682 0.1624  2   GLU E CD  
9758  O OE1 . GLU E 2   ? 2.2218 2.0527 2.1625 -0.8826 -0.0566 0.1809  2   GLU E OE1 
9759  O OE2 . GLU E 2   ? 2.1966 2.0403 2.0483 -0.8875 -0.0918 0.1589  2   GLU E OE2 
9760  N N   . VAL E 3   ? 1.9771 1.7980 1.5852 -0.9001 -0.0411 0.0583  3   VAL E N   
9761  C CA  . VAL E 3   ? 1.9797 1.8009 1.5203 -0.9058 -0.0309 0.0329  3   VAL E CA  
9762  C C   . VAL E 3   ? 1.9713 1.8054 1.4853 -0.9049 -0.0485 0.0293  3   VAL E C   
9763  O O   . VAL E 3   ? 1.9620 1.7998 1.5019 -0.9001 -0.0665 0.0430  3   VAL E O   
9764  C CB  . VAL E 3   ? 1.9931 1.7990 1.5058 -0.9087 -0.0089 0.0176  3   VAL E CB  
9765  C CG1 . VAL E 3   ? 2.0047 1.7952 1.5427 -0.9096 0.0118  0.0205  3   VAL E CG1 
9766  C CG2 . VAL E 3   ? 1.9893 1.7917 1.5137 -0.9051 -0.0160 0.0244  3   VAL E CG2 
9767  N N   . LEU E 4   ? 2.0803 1.9206 1.5447 -0.9097 -0.0416 0.0114  4   LEU E N   
9768  C CA  . LEU E 4   ? 2.0717 1.9235 1.5085 -0.9095 -0.0512 0.0051  4   LEU E CA  
9769  C C   . LEU E 4   ? 2.0552 1.9043 1.4444 -0.9142 -0.0316 -0.0163 4   LEU E C   
9770  O O   . LEU E 4   ? 2.0502 1.8959 1.4125 -0.9199 -0.0123 -0.0304 4   LEU E O   
9771  C CB  . LEU E 4   ? 2.0782 1.9424 1.5072 -0.9112 -0.0597 0.0059  4   LEU E CB  
9772  C CG  . LEU E 4   ? 2.0971 1.9640 1.5697 -0.9074 -0.0816 0.0278  4   LEU E CG  
9773  C CD1 . LEU E 4   ? 2.1047 1.9797 1.5631 -0.9115 -0.0845 0.0262  4   LEU E CD1 
9774  C CD2 . LEU E 4   ? 2.0987 1.9688 1.5930 -0.9016 -0.1034 0.0404  4   LEU E CD2 
9775  N N   . VAL E 5   ? 2.1232 1.9734 1.5039 -0.9121 -0.0367 -0.0182 5   VAL E N   
9776  C CA  . VAL E 5   ? 2.1118 1.9601 1.4515 -0.9167 -0.0201 -0.0364 5   VAL E CA  
9777  C C   . VAL E 5   ? 2.1170 1.9814 1.4419 -0.9166 -0.0260 -0.0421 5   VAL E C   
9778  O O   . VAL E 5   ? 2.1269 1.9964 1.4726 -0.9112 -0.0452 -0.0317 5   VAL E O   
9779  C CB  . VAL E 5   ? 2.1066 1.9407 1.4499 -0.9152 -0.0189 -0.0342 5   VAL E CB  
9780  C CG1 . VAL E 5   ? 2.0988 1.9294 1.3987 -0.9210 -0.0015 -0.0525 5   VAL E CG1 
9781  C CG2 . VAL E 5   ? 2.1000 1.9184 1.4697 -0.9145 -0.0128 -0.0262 5   VAL E CG2 
9782  N N   . GLN E 6   ? 2.1614 2.0338 1.4544 -0.9228 -0.0088 -0.0587 6   GLN E N   
9783  C CA  . GLN E 6   ? 2.1721 2.0618 1.4566 -0.9238 -0.0102 -0.0660 6   GLN E CA  
9784  C C   . GLN E 6   ? 2.1743 2.0657 1.4396 -0.9265 -0.0001 -0.0785 6   GLN E C   
9785  O O   . GLN E 6   ? 2.1620 2.0412 1.4083 -0.9303 0.0136  -0.0853 6   GLN E O   
9786  C CB  . GLN E 6   ? 2.1737 2.0744 1.4431 -0.9295 0.0019  -0.0749 6   GLN E CB  
9787  C CG  . GLN E 6   ? 2.1750 2.0751 1.4635 -0.9275 -0.0101 -0.0622 6   GLN E CG  
9788  C CD  . GLN E 6   ? 2.1799 2.0906 1.4516 -0.9338 0.0011  -0.0709 6   GLN E CD  
9789  O OE1 . GLN E 6   ? 2.1795 2.0842 1.4498 -0.9365 0.0054  -0.0688 6   GLN E OE1 
9790  N NE2 . GLN E 6   ? 2.1895 2.1162 1.4514 -0.9364 0.0058  -0.0809 6   GLN E NE2 
9791  N N   . SER E 7   ? 2.1335 2.0392 1.4062 -0.9247 -0.0077 -0.0817 7   SER E N   
9792  C CA  . SER E 7   ? 2.1429 2.0532 1.4048 -0.9273 -0.0006 -0.0936 7   SER E CA  
9793  C C   . SER E 7   ? 2.1370 2.0541 1.3725 -0.9364 0.0237  -0.1108 7   SER E C   
9794  O O   . SER E 7   ? 2.1316 2.0530 1.3576 -0.9405 0.0343  -0.1145 7   SER E O   
9795  C CB  . SER E 7   ? 2.1657 2.0910 1.4492 -0.9225 -0.0157 -0.0943 7   SER E CB  
9796  O OG  . SER E 7   ? 2.1694 2.1101 1.4590 -0.9235 -0.0153 -0.0974 7   SER E OG  
9797  N N   . GLY E 8   ? 2.2622 2.1795 1.4870 -0.9401 0.0317  -0.1211 8   GLY E N   
9798  C CA  . GLY E 8   ? 2.2577 2.1793 1.4590 -0.9495 0.0542  -0.1367 8   GLY E CA  
9799  C C   . GLY E 8   ? 2.2774 2.2236 1.4861 -0.9528 0.0596  -0.1480 8   GLY E C   
9800  O O   . GLY E 8   ? 2.2946 2.2549 1.5261 -0.9476 0.0461  -0.1456 8   GLY E O   
9801  N N   . ALA E 9   ? 2.4202 2.3712 1.6097 -0.9620 0.0802  -0.1614 9   ALA E N   
9802  C CA  . ALA E 9   ? 2.4432 2.4181 1.6386 -0.9669 0.0886  -0.1740 9   ALA E CA  
9803  C C   . ALA E 9   ? 2.4738 2.4668 1.6957 -0.9633 0.0765  -0.1806 9   ALA E C   
9804  O O   . ALA E 9   ? 2.4799 2.4668 1.7085 -0.9604 0.0675  -0.1804 9   ALA E O   
9805  C CB  . ALA E 9   ? 2.4418 2.4169 1.6140 -0.9781 0.1116  -0.1877 9   ALA E CB  
9806  N N   . GLU E 10  ? 2.3994 2.4141 1.6366 -0.9635 0.0758  -0.1874 10  GLU E N   
9807  C CA  . GLU E 10  ? 2.4313 2.4648 1.6970 -0.9593 0.0638  -0.1963 10  GLU E CA  
9808  C C   . GLU E 10  ? 2.4625 2.5210 1.7337 -0.9664 0.0767  -0.2139 10  GLU E C   
9809  O O   . GLU E 10  ? 2.4637 2.5270 1.7212 -0.9724 0.0904  -0.2154 10  GLU E O   
9810  C CB  . GLU E 10  ? 2.4343 2.4681 1.7214 -0.9494 0.0430  -0.1851 10  GLU E CB  
9811  C CG  . GLU E 10  ? 2.4130 2.4239 1.7000 -0.9421 0.0277  -0.1675 10  GLU E CG  
9812  C CD  . GLU E 10  ? 2.4301 2.4432 1.7459 -0.9320 0.0036  -0.1625 10  GLU E CD  
9813  O OE1 . GLU E 10  ? 2.4529 2.4832 1.7889 -0.9300 -0.0018 -0.1756 10  GLU E OE1 
9814  O OE2 . GLU E 10  ? 2.4153 2.4129 1.7353 -0.9259 -0.0106 -0.1461 10  GLU E OE2 
9815  N N   . VAL E 11  ? 2.5170 2.5917 1.8098 -0.9654 0.0710  -0.2279 11  VAL E N   
9816  C CA  . VAL E 11  ? 2.5454 2.6473 1.8527 -0.9701 0.0783  -0.2460 11  VAL E CA  
9817  C C   . VAL E 11  ? 2.5696 2.6862 1.9102 -0.9608 0.0588  -0.2507 11  VAL E C   
9818  O O   . VAL E 11  ? 2.5781 2.6881 1.9342 -0.9527 0.0409  -0.2486 11  VAL E O   
9819  C CB  . VAL E 11  ? 2.5736 2.6829 1.8791 -0.9780 0.0883  -0.2618 11  VAL E CB  
9820  C CG1 . VAL E 11  ? 2.6392 2.7788 1.9670 -0.9813 0.0915  -0.2816 11  VAL E CG1 
9821  C CG2 . VAL E 11  ? 2.5650 2.6599 1.8368 -0.9882 0.1090  -0.2589 11  VAL E CG2 
9822  N N   . LYS E 12  ? 2.6536 2.7892 2.0045 -0.9621 0.0622  -0.2579 12  LYS E N   
9823  C CA  . LYS E 12  ? 2.6805 2.8326 2.0635 -0.9543 0.0459  -0.2668 12  LYS E CA  
9824  C C   . LYS E 12  ? 2.7226 2.9031 2.1160 -0.9609 0.0580  -0.2864 12  LYS E C   
9825  O O   . LYS E 12  ? 2.7321 2.9177 2.1060 -0.9712 0.0782  -0.2887 12  LYS E O   
9826  C CB  . LYS E 12  ? 2.6708 2.8126 2.0581 -0.9467 0.0318  -0.2517 12  LYS E CB  
9827  C CG  . LYS E 12  ? 2.6336 2.7507 2.0204 -0.9382 0.0146  -0.2345 12  LYS E CG  
9828  C CD  . LYS E 12  ? 2.6533 2.7722 2.0654 -0.9296 -0.0043 -0.2420 12  LYS E CD  
9829  C CE  . LYS E 12  ? 2.6523 2.7466 2.0639 -0.9215 -0.0219 -0.2236 12  LYS E CE  
9830  N NZ  . LYS E 12  ? 2.6646 2.7579 2.0986 -0.9131 -0.0413 -0.2302 12  LYS E NZ  
9831  N N   . LYS E 13  ? 2.6311 2.8298 2.0559 -0.9549 0.0449  -0.3013 13  LYS E N   
9832  C CA  . LYS E 13  ? 2.6751 2.9025 2.1142 -0.9601 0.0541  -0.3210 13  LYS E CA  
9833  C C   . LYS E 13  ? 2.6825 2.9154 2.1231 -0.9593 0.0539  -0.3175 13  LYS E C   
9834  O O   . LYS E 13  ? 2.6560 2.8728 2.0969 -0.9518 0.0396  -0.3027 13  LYS E O   
9835  C CB  . LYS E 13  ? 2.7033 2.9480 2.1764 -0.9534 0.0387  -0.3400 13  LYS E CB  
9836  C CG  . LYS E 13  ? 2.6984 2.9403 2.1965 -0.9397 0.0136  -0.3387 13  LYS E CG  
9837  C CD  . LYS E 13  ? 2.7187 2.9712 2.2471 -0.9318 -0.0046 -0.3556 13  LYS E CD  
9838  C CE  . LYS E 13  ? 2.7194 2.9698 2.2735 -0.9181 -0.0297 -0.3566 13  LYS E CE  
9839  N NZ  . LYS E 13  ? 2.7320 2.9849 2.3118 -0.9086 -0.0514 -0.3692 13  LYS E NZ  
9840  N N   . PRO E 14  ? 2.5451 2.8000 1.9863 -0.9677 0.0693  -0.3310 14  PRO E N   
9841  C CA  . PRO E 14  ? 2.5593 2.8195 2.0010 -0.9681 0.0691  -0.3291 14  PRO E CA  
9842  C C   . PRO E 14  ? 2.5597 2.8219 2.0305 -0.9557 0.0450  -0.3322 14  PRO E C   
9843  O O   . PRO E 14  ? 2.5742 2.8483 2.0723 -0.9489 0.0329  -0.3468 14  PRO E O   
9844  C CB  . PRO E 14  ? 2.6100 2.8974 2.0526 -0.9793 0.0891  -0.3480 14  PRO E CB  
9845  C CG  . PRO E 14  ? 2.6102 2.8981 2.0391 -0.9874 0.1043  -0.3519 14  PRO E CG  
9846  C CD  . PRO E 14  ? 2.5785 2.8523 2.0164 -0.9787 0.0886  -0.3473 14  PRO E CD  
9847  N N   . GLY E 15  ? 2.5803 2.8295 2.0448 -0.9529 0.0370  -0.3187 15  GLY E N   
9848  C CA  . GLY E 15  ? 2.5790 2.8265 2.0679 -0.9418 0.0139  -0.3202 15  GLY E CA  
9849  C C   . GLY E 15  ? 2.5374 2.7602 2.0318 -0.9304 -0.0083 -0.3044 15  GLY E C   
9850  O O   . GLY E 15  ? 2.5299 2.7443 2.0384 -0.9219 -0.0281 -0.3001 15  GLY E O   
9851  N N   . ALA E 16  ? 2.6532 2.8635 2.1361 -0.9306 -0.0055 -0.2960 16  ALA E N   
9852  C CA  . ALA E 16  ? 2.6177 2.8047 2.1040 -0.9210 -0.0245 -0.2811 16  ALA E CA  
9853  C C   . ALA E 16  ? 2.5857 2.7488 2.0499 -0.9221 -0.0258 -0.2567 16  ALA E C   
9854  O O   . ALA E 16  ? 2.5913 2.7554 2.0394 -0.9293 -0.0147 -0.2518 16  ALA E O   
9855  C CB  . ALA E 16  ? 2.6112 2.7950 2.0935 -0.9218 -0.0205 -0.2836 16  ALA E CB  
9856  N N   . SER E 17  ? 2.6235 2.7647 2.0879 -0.9150 -0.0407 -0.2412 17  SER E N   
9857  C CA  . SER E 17  ? 2.5932 2.7111 2.0402 -0.9149 -0.0449 -0.2176 17  SER E CA  
9858  C C   . SER E 17  ? 2.5662 2.6674 1.9953 -0.9161 -0.0396 -0.2060 17  SER E C   
9859  O O   . SER E 17  ? 2.5672 2.6692 2.0032 -0.9134 -0.0421 -0.2128 17  SER E O   
9860  C CB  . SER E 17  ? 2.5843 2.6897 2.0510 -0.9046 -0.0714 -0.2082 17  SER E CB  
9861  O OG  . SER E 17  ? 2.6079 2.7267 2.0897 -0.9037 -0.0767 -0.2194 17  SER E OG  
9862  N N   . VAL E 18  ? 2.5887 2.6745 1.9945 -0.9203 -0.0329 -0.1891 18  VAL E N   
9863  C CA  . VAL E 18  ? 2.5619 2.6294 1.9493 -0.9213 -0.0286 -0.1767 18  VAL E CA  
9864  C C   . VAL E 18  ? 2.5366 2.5827 1.9235 -0.9162 -0.0446 -0.1545 18  VAL E C   
9865  O O   . VAL E 18  ? 2.5343 2.5789 1.9212 -0.9169 -0.0494 -0.1471 18  VAL E O   
9866  C CB  . VAL E 18  ? 2.5564 2.6265 1.9151 -0.9321 -0.0029 -0.1804 18  VAL E CB  
9867  C CG1 . VAL E 18  ? 2.5507 2.6189 1.8944 -0.9373 0.0037  -0.1727 18  VAL E CG1 
9868  C CG2 . VAL E 18  ? 2.5307 2.5826 1.8718 -0.9329 0.0018  -0.1718 18  VAL E CG2 
9869  N N   . LYS E 19  ? 2.3876 2.4171 1.7751 -0.9114 -0.0539 -0.1439 19  LYS E N   
9870  C CA  . LYS E 19  ? 2.3681 2.3775 1.7572 -0.9068 -0.0690 -0.1225 19  LYS E CA  
9871  C C   . LYS E 19  ? 2.3469 2.3422 1.7126 -0.9108 -0.0568 -0.1143 19  LYS E C   
9872  O O   . LYS E 19  ? 2.3479 2.3394 1.7070 -0.9114 -0.0512 -0.1190 19  LYS E O   
9873  C CB  . LYS E 19  ? 2.3732 2.3745 1.7865 -0.8971 -0.0927 -0.1169 19  LYS E CB  
9874  C CG  . LYS E 19  ? 2.3590 2.3412 1.7787 -0.8926 -0.1101 -0.0945 19  LYS E CG  
9875  C CD  . LYS E 19  ? 2.3779 2.3519 1.8209 -0.8837 -0.1328 -0.0893 19  LYS E CD  
9876  C CE  . LYS E 19  ? 2.4059 2.3795 1.8712 -0.8785 -0.1533 -0.0840 19  LYS E CE  
9877  N NZ  . LYS E 19  ? 2.4478 2.4037 1.9285 -0.8723 -0.1751 -0.0649 19  LYS E NZ  
9878  N N   . VAL E 20  ? 2.3147 2.3016 1.6686 -0.9136 -0.0538 -0.1029 20  VAL E N   
9879  C CA  . VAL E 20  ? 2.2938 2.2668 1.6278 -0.9168 -0.0431 -0.0964 20  VAL E CA  
9880  C C   . VAL E 20  ? 2.2825 2.2382 1.6293 -0.9109 -0.0620 -0.0756 20  VAL E C   
9881  O O   . VAL E 20  ? 2.2850 2.2406 1.6489 -0.9074 -0.0784 -0.0658 20  VAL E O   
9882  C CB  . VAL E 20  ? 2.2828 2.2622 1.5942 -0.9255 -0.0224 -0.1037 20  VAL E CB  
9883  C CG1 . VAL E 20  ? 2.2809 2.2617 1.5978 -0.9257 -0.0306 -0.0952 20  VAL E CG1 
9884  C CG2 . VAL E 20  ? 2.3000 2.2664 1.5889 -0.9297 -0.0078 -0.1029 20  VAL E CG2 
9885  N N   . SER E 21  ? 2.1809 2.1220 1.5214 -0.9102 -0.0600 -0.0691 21  SER E N   
9886  C CA  . SER E 21  ? 2.1753 2.1016 1.5334 -0.9048 -0.0777 -0.0498 21  SER E CA  
9887  C C   . SER E 21  ? 2.1557 2.0710 1.5047 -0.9078 -0.0688 -0.0436 21  SER E C   
9888  O O   . SER E 21  ? 2.1451 2.0593 1.4698 -0.9137 -0.0481 -0.0547 21  SER E O   
9889  C CB  . SER E 21  ? 2.1852 2.1025 1.5541 -0.8998 -0.0886 -0.0452 21  SER E CB  
9890  O OG  . SER E 21  ? 2.1786 2.0891 1.5261 -0.9039 -0.0722 -0.0533 21  SER E OG  
9891  N N   . CYS E 22  ? 2.1861 2.0931 1.5589 -0.9035 -0.0858 -0.0258 22  CYS E N   
9892  C CA  . CYS E 22  ? 2.1741 2.0712 1.5515 -0.9049 -0.0821 -0.0177 22  CYS E CA  
9893  C C   . CYS E 22  ? 2.1784 2.0650 1.5901 -0.8988 -0.1011 0.0014  22  CYS E C   
9894  O O   . CYS E 22  ? 2.1854 2.0740 1.6224 -0.8946 -0.1219 0.0148  22  CYS E O   
9895  C CB  . CYS E 22  ? 2.1705 2.0735 1.5470 -0.9081 -0.0818 -0.0158 22  CYS E CB  
9896  S SG  . CYS E 22  ? 2.1695 2.0624 1.5679 -0.9083 -0.0858 -0.0010 22  CYS E SG  
9897  N N   . ARG E 23  ? 2.0792 1.9543 1.4935 -0.8989 -0.0937 0.0028  23  ARG E N   
9898  C CA  . ARG E 23  ? 2.0859 1.9522 1.5369 -0.8938 -0.1090 0.0206  23  ARG E CA  
9899  C C   . ARG E 23  ? 2.0821 1.9416 1.5578 -0.8944 -0.1047 0.0303  23  ARG E C   
9900  O O   . ARG E 23  ? 2.0703 1.9243 1.5286 -0.8988 -0.0846 0.0199  23  ARG E O   
9901  C CB  . ARG E 23  ? 2.0884 1.9458 1.5319 -0.8932 -0.1051 0.0171  23  ARG E CB  
9902  C CG  . ARG E 23  ? 2.0990 1.9479 1.5831 -0.8886 -0.1193 0.0360  23  ARG E CG  
9903  C CD  . ARG E 23  ? 2.1105 1.9511 1.5868 -0.8880 -0.1197 0.0339  23  ARG E CD  
9904  N NE  . ARG E 23  ? 2.1195 1.9535 1.6381 -0.8840 -0.1333 0.0531  23  ARG E NE  
9905  C CZ  . ARG E 23  ? 2.1362 1.9660 1.6619 -0.8815 -0.1453 0.0588  23  ARG E CZ  
9906  N NH1 . ARG E 23  ? 2.1431 1.9681 1.7109 -0.8785 -0.1563 0.0775  23  ARG E NH1 
9907  N NH2 . ARG E 23  ? 2.1484 1.9794 1.6427 -0.8822 -0.1458 0.0465  23  ARG E NH2 
9908  N N   . ALA E 24  ? 1.9900 1.8499 1.5095 -0.8901 -0.1235 0.0505  24  ALA E N   
9909  C CA  . ALA E 24  ? 1.9898 1.8455 1.5463 -0.8899 -0.1219 0.0636  24  ALA E CA  
9910  C C   . ALA E 24  ? 1.9905 1.8359 1.5791 -0.8876 -0.1168 0.0729  24  ALA E C   
9911  O O   . ALA E 24  ? 1.9869 1.8310 1.5918 -0.8841 -0.1291 0.0817  24  ALA E O   
9912  C CB  . ALA E 24  ? 1.9840 1.8463 1.5743 -0.8870 -0.1445 0.0821  24  ALA E CB  
9913  N N   . PHE E 25  ? 1.9077 1.7448 1.5069 -0.8898 -0.0974 0.0713  25  PHE E N   
9914  C CA  . PHE E 25  ? 1.9105 1.7367 1.5482 -0.8879 -0.0881 0.0822  25  PHE E CA  
9915  C C   . PHE E 25  ? 1.9098 1.7349 1.6018 -0.8862 -0.0826 0.0991  25  PHE E C   
9916  O O   . PHE E 25  ? 1.9118 1.7396 1.5965 -0.8886 -0.0776 0.0948  25  PHE E O   
9917  C CB  . PHE E 25  ? 1.9237 1.7362 1.5245 -0.8920 -0.0640 0.0643  25  PHE E CB  
9918  C CG  . PHE E 25  ? 1.9263 1.7390 1.4779 -0.8939 -0.0672 0.0492  25  PHE E CG  
9919  C CD1 . PHE E 25  ? 1.9283 1.7337 1.4874 -0.8923 -0.0707 0.0543  25  PHE E CD1 
9920  C CD2 . PHE E 25  ? 1.9282 1.7483 1.4289 -0.8975 -0.0646 0.0308  25  PHE E CD2 
9921  C CE1 . PHE E 25  ? 1.9316 1.7368 1.4485 -0.8940 -0.0740 0.0417  25  PHE E CE1 
9922  C CE2 . PHE E 25  ? 1.9310 1.7523 1.3939 -0.8988 -0.0657 0.0189  25  PHE E CE2 
9923  C CZ  . PHE E 25  ? 1.9327 1.7463 1.4033 -0.8970 -0.0711 0.0243  25  PHE E CZ  
9924  N N   . GLY E 26  ? 2.0186 1.8399 1.7677 -0.8821 -0.0820 0.1194  26  GLY E N   
9925  C CA  . GLY E 26  ? 2.0286 1.8470 1.8362 -0.8800 -0.0697 0.1370  26  GLY E CA  
9926  C C   . GLY E 26  ? 2.0831 1.9136 1.9292 -0.8778 -0.0891 0.1549  26  GLY E C   
9927  O O   . GLY E 26  ? 2.1100 1.9393 2.0042 -0.8764 -0.0786 0.1696  26  GLY E O   
9928  N N   . TYR E 27  ? 2.0791 1.9200 1.9063 -0.8776 -0.1162 0.1554  27  TYR E N   
9929  C CA  . TYR E 27  ? 2.1066 1.9570 1.9675 -0.8760 -0.1380 0.1740  27  TYR E CA  
9930  C C   . TYR E 27  ? 2.1027 1.9593 1.9482 -0.8744 -0.1658 0.1770  27  TYR E C   
9931  O O   . TYR E 27  ? 2.0925 1.9467 1.9021 -0.8744 -0.1666 0.1641  27  TYR E O   
9932  C CB  . TYR E 27  ? 2.1376 1.9916 1.9777 -0.8798 -0.1385 0.1674  27  TYR E CB  
9933  C CG  . TYR E 27  ? 2.1056 1.9640 1.8799 -0.8832 -0.1483 0.1480  27  TYR E CG  
9934  C CD1 . TYR E 27  ? 2.0853 1.9397 1.8052 -0.8866 -0.1307 0.1234  27  TYR E CD1 
9935  C CD2 . TYR E 27  ? 2.1109 1.9766 1.8785 -0.8833 -0.1733 0.1551  27  TYR E CD2 
9936  C CE1 . TYR E 27  ? 2.0629 1.9227 1.7281 -0.8896 -0.1358 0.1071  27  TYR E CE1 
9937  C CE2 . TYR E 27  ? 2.0943 1.9633 1.8070 -0.8862 -0.1781 0.1388  27  TYR E CE2 
9938  C CZ  . TYR E 27  ? 2.0658 1.9329 1.7297 -0.8891 -0.1583 0.1151  27  TYR E CZ  
9939  O OH  . TYR E 27  ? 2.0501 1.9223 1.6653 -0.8920 -0.1599 0.1001  27  TYR E OH  
9940  N N   . THR E 28  ? 2.0772 1.9404 1.9506 -0.8731 -0.1887 0.1952  28  THR E N   
9941  C CA  . THR E 28  ? 2.0717 1.9386 1.9350 -0.8713 -0.2163 0.2008  28  THR E CA  
9942  C C   . THR E 28  ? 2.0651 1.9343 1.8705 -0.8741 -0.2235 0.1834  28  THR E C   
9943  O O   . THR E 28  ? 2.0844 1.9565 1.8835 -0.8768 -0.2285 0.1850  28  THR E O   
9944  C CB  . THR E 28  ? 2.0974 1.9687 2.0118 -0.8693 -0.2385 0.2283  28  THR E CB  
9945  O OG1 . THR E 28  ? 2.1017 1.9717 2.0728 -0.8668 -0.2279 0.2452  28  THR E OG1 
9946  C CG2 . THR E 28  ? 2.0902 1.9627 1.9914 -0.8675 -0.2678 0.2341  28  THR E CG2 
9947  N N   . PHE E 29  ? 2.1553 2.0231 1.9204 -0.8736 -0.2227 0.1676  29  PHE E N   
9948  C CA  . PHE E 29  ? 2.1440 2.0143 1.8557 -0.8762 -0.2230 0.1495  29  PHE E CA  
9949  C C   . PHE E 29  ? 2.1587 2.0321 1.8718 -0.8767 -0.2456 0.1595  29  PHE E C   
9950  O O   . PHE E 29  ? 2.1553 2.0312 1.8374 -0.8806 -0.2416 0.1492  29  PHE E O   
9951  C CB  . PHE E 29  ? 2.1271 1.9958 1.8092 -0.8745 -0.2219 0.1364  29  PHE E CB  
9952  C CG  . PHE E 29  ? 2.1183 1.9909 1.7539 -0.8766 -0.2206 0.1191  29  PHE E CG  
9953  C CD1 . PHE E 29  ? 2.1066 1.9821 1.7065 -0.8814 -0.2006 0.1015  29  PHE E CD1 
9954  C CD2 . PHE E 29  ? 2.1226 1.9958 1.7535 -0.8738 -0.2383 0.1205  29  PHE E CD2 
9955  C CE1 . PHE E 29  ? 2.0986 1.9797 1.6613 -0.8836 -0.1970 0.0862  29  PHE E CE1 
9956  C CE2 . PHE E 29  ? 2.1166 1.9943 1.7123 -0.8756 -0.2346 0.1045  29  PHE E CE2 
9957  C CZ  . PHE E 29  ? 2.1042 1.9868 1.6669 -0.8806 -0.2133 0.0876  29  PHE E CZ  
9958  N N   . THR E 30  ? 2.2493 2.1216 1.9976 -0.8734 -0.2691 0.1800  30  THR E N   
9959  C CA  . THR E 30  ? 2.2597 2.1319 2.0085 -0.8740 -0.2932 0.1908  30  THR E CA  
9960  C C   . THR E 30  ? 2.2981 2.1716 2.0709 -0.8769 -0.2995 0.2058  30  THR E C   
9961  O O   . THR E 30  ? 2.3256 2.1973 2.1005 -0.8781 -0.3212 0.2173  30  THR E O   
9962  C CB  . THR E 30  ? 2.2745 2.1433 2.0491 -0.8696 -0.3174 0.2071  30  THR E CB  
9963  O OG1 . THR E 30  ? 2.2945 2.1639 2.1171 -0.8671 -0.3172 0.2241  30  THR E OG1 
9964  C CG2 . THR E 30  ? 2.2579 2.1245 2.0039 -0.8672 -0.3145 0.1916  30  THR E CG2 
9965  N N   . GLY E 31  ? 2.1512 2.0266 1.9428 -0.8783 -0.2813 0.2062  31  GLY E N   
9966  C CA  . GLY E 31  ? 2.1940 2.0708 2.0151 -0.8807 -0.2866 0.2219  31  GLY E CA  
9967  C C   . GLY E 31  ? 2.2007 2.0780 1.9885 -0.8864 -0.2776 0.2102  31  GLY E C   
9968  O O   . GLY E 31  ? 2.2410 2.1187 2.0511 -0.8890 -0.2839 0.2237  31  GLY E O   
9969  N N   . ASN E 32  ? 2.1721 2.0497 1.9080 -0.8889 -0.2627 0.1862  32  ASN E N   
9970  C CA  . ASN E 32  ? 2.1677 2.0463 1.8706 -0.8950 -0.2511 0.1740  32  ASN E CA  
9971  C C   . ASN E 32  ? 2.1305 2.0106 1.7804 -0.8976 -0.2484 0.1553  32  ASN E C   
9972  O O   . ASN E 32  ? 2.1023 1.9835 1.7339 -0.8948 -0.2411 0.1425  32  ASN E O   
9973  C CB  . ASN E 32  ? 2.1655 2.0438 1.8657 -0.8965 -0.2230 0.1616  32  ASN E CB  
9974  C CG  . ASN E 32  ? 2.2055 2.0822 1.9635 -0.8939 -0.2199 0.1790  32  ASN E CG  
9975  O OD1 . ASN E 32  ? 2.2038 2.0795 1.9938 -0.8890 -0.2193 0.1867  32  ASN E OD1 
9976  N ND2 . ASN E 32  ? 2.2429 2.1190 2.0165 -0.8973 -0.2162 0.1857  32  ASN E ND2 
9977  N N   . ALA E 33  ? 2.1903 2.0705 1.8177 -0.9032 -0.2533 0.1542  33  ALA E N   
9978  C CA  . ALA E 33  ? 2.1613 2.0445 1.7411 -0.9068 -0.2445 0.1349  33  ALA E CA  
9979  C C   . ALA E 33  ? 2.1379 2.0254 1.6877 -0.9087 -0.2149 0.1124  33  ALA E C   
9980  O O   . ALA E 33  ? 2.1441 2.0304 1.7033 -0.9095 -0.2014 0.1114  33  ALA E O   
9981  C CB  . ALA E 33  ? 2.1744 2.0562 1.7373 -0.9138 -0.2524 0.1384  33  ALA E CB  
9982  N N   . LEU E 34  ? 2.2319 2.1242 1.7475 -0.9096 -0.2043 0.0943  34  LEU E N   
9983  C CA  . LEU E 34  ? 2.2150 2.1117 1.7008 -0.9117 -0.1772 0.0731  34  LEU E CA  
9984  C C   . LEU E 34  ? 2.2356 2.1399 1.6816 -0.9184 -0.1636 0.0560  34  LEU E C   
9985  O O   . LEU E 34  ? 2.2359 2.1440 1.6748 -0.9184 -0.1713 0.0532  34  LEU E O   
9986  C CB  . LEU E 34  ? 2.1881 2.0852 1.6760 -0.9060 -0.1737 0.0666  34  LEU E CB  
9987  C CG  . LEU E 34  ? 2.1698 2.0694 1.6296 -0.9082 -0.1470 0.0467  34  LEU E CG  
9988  C CD1 . LEU E 34  ? 2.1419 2.0340 1.6196 -0.9072 -0.1390 0.0514  34  LEU E CD1 
9989  C CD2 . LEU E 34  ? 2.1437 2.0463 1.5943 -0.9046 -0.1447 0.0370  34  LEU E CD2 
9990  N N   . HIS E 35  ? 2.2883 2.1948 1.7112 -0.9241 -0.1426 0.0441  35  HIS E N   
9991  C CA  . HIS E 35  ? 2.3079 2.2227 1.6943 -0.9317 -0.1262 0.0276  35  HIS E CA  
9992  C C   . HIS E 35  ? 2.2846 2.2070 1.6471 -0.9321 -0.1035 0.0068  35  HIS E C   
9993  O O   . HIS E 35  ? 2.2635 2.1819 1.6301 -0.9287 -0.0961 0.0039  35  HIS E O   
9994  C CB  . HIS E 35  ? 2.3271 2.2394 1.7018 -0.9388 -0.1169 0.0272  35  HIS E CB  
9995  C CG  . HIS E 35  ? 2.3403 2.2454 1.7388 -0.9396 -0.1382 0.0479  35  HIS E CG  
9996  N ND1 . HIS E 35  ? 2.3771 2.2831 1.7651 -0.9451 -0.1481 0.0525  35  HIS E ND1 
9997  C CD2 . HIS E 35  ? 2.3139 2.2109 1.7481 -0.9362 -0.1507 0.0654  35  HIS E CD2 
9998  C CE1 . HIS E 35  ? 2.3798 2.2778 1.7933 -0.9452 -0.1674 0.0725  35  HIS E CE1 
9999  N NE2 . HIS E 35  ? 2.3361 2.2296 1.7806 -0.9395 -0.1691 0.0808  35  HIS E NE2 
10000 N N   . TRP E 36  ? 2.4837 2.4173 1.8228 -0.9370 -0.0925 -0.0076 36  TRP E N   
10001 C CA  . TRP E 36  ? 2.4659 2.4096 1.7805 -0.9402 -0.0678 -0.0287 36  TRP E CA  
10002 C C   . TRP E 36  ? 2.4979 2.4484 1.7850 -0.9501 -0.0495 -0.0401 36  TRP E C   
10003 O O   . TRP E 36  ? 2.5178 2.4725 1.8009 -0.9546 -0.0547 -0.0380 36  TRP E O   
10004 C CB  . TRP E 36  ? 2.4199 2.3740 1.7386 -0.9371 -0.0693 -0.0375 36  TRP E CB  
10005 C CG  . TRP E 36  ? 2.3826 2.3300 1.7252 -0.9279 -0.0851 -0.0288 36  TRP E CG  
10006 C CD1 . TRP E 36  ? 2.3734 2.3137 1.7423 -0.9219 -0.1105 -0.0126 36  TRP E CD1 
10007 C CD2 . TRP E 36  ? 2.3520 2.2985 1.6933 -0.9245 -0.0767 -0.0357 36  TRP E CD2 
10008 N NE1 . TRP E 36  ? 2.3369 2.2724 1.7216 -0.9148 -0.1179 -0.0091 36  TRP E NE1 
10009 C CE2 . TRP E 36  ? 2.3240 2.2629 1.6914 -0.9164 -0.0975 -0.0230 36  TRP E CE2 
10010 C CE3 . TRP E 36  ? 2.3477 2.2981 1.6677 -0.9281 -0.0538 -0.0513 36  TRP E CE3 
10011 C CZ2 . TRP E 36  ? 2.2926 2.2275 1.6641 -0.9120 -0.0960 -0.0253 36  TRP E CZ2 
10012 C CZ3 . TRP E 36  ? 2.3184 2.2643 1.6422 -0.9238 -0.0527 -0.0534 36  TRP E CZ3 
10013 C CH2 . TRP E 36  ? 2.2913 2.2295 1.6401 -0.9159 -0.0736 -0.0404 36  TRP E CH2 
10014 N N   . VAL E 37  ? 2.4896 2.4403 1.7576 -0.9540 -0.0282 -0.0522 37  VAL E N   
10015 C CA  . VAL E 37  ? 2.5230 2.4783 1.7648 -0.9636 -0.0095 -0.0632 37  VAL E CA  
10016 C C   . VAL E 37  ? 2.5122 2.4775 1.7339 -0.9673 0.0152  -0.0837 37  VAL E C   
10017 O O   . VAL E 37  ? 2.4913 2.4514 1.7153 -0.9632 0.0196  -0.0867 37  VAL E O   
10018 C CB  . VAL E 37  ? 2.5429 2.4840 1.7859 -0.9653 -0.0108 -0.0549 37  VAL E CB  
10019 C CG1 . VAL E 37  ? 2.5749 2.5195 1.7895 -0.9756 0.0091  -0.0677 37  VAL E CG1 
10020 C CG2 . VAL E 37  ? 2.5481 2.4805 1.8164 -0.9621 -0.0367 -0.0333 37  VAL E CG2 
10021 N N   . ARG E 38  ? 2.6092 2.5887 1.8122 -0.9757 0.0314  -0.0977 38  ARG E N   
10022 C CA  . ARG E 38  ? 2.5994 2.5899 1.7867 -0.9802 0.0546  -0.1169 38  ARG E CA  
10023 C C   . ARG E 38  ? 2.6476 2.6390 1.8093 -0.9904 0.0745  -0.1274 38  ARG E C   
10024 O O   . ARG E 38  ? 2.6848 2.6728 1.8394 -0.9951 0.0714  -0.1221 38  ARG E O   
10025 C CB  . ARG E 38  ? 2.5864 2.5976 1.7810 -0.9811 0.0586  -0.1281 38  ARG E CB  
10026 C CG  . ARG E 38  ? 2.6361 2.6612 1.8238 -0.9891 0.0640  -0.1341 38  ARG E CG  
10027 C CD  . ARG E 38  ? 2.6379 2.6844 1.8390 -0.9891 0.0685  -0.1477 38  ARG E CD  
10028 N NE  . ARG E 38  ? 2.6908 2.7528 1.8860 -0.9976 0.0768  -0.1566 38  ARG E NE  
10029 C CZ  . ARG E 38  ? 2.7038 2.7864 1.9128 -0.9988 0.0811  -0.1702 38  ARG E CZ  
10030 N NH1 . ARG E 38  ? 2.6681 2.7576 1.8981 -0.9915 0.0763  -0.1759 38  ARG E NH1 
10031 N NH2 . ARG E 38  ? 2.7567 2.8528 1.9596 -1.0073 0.0895  -0.1785 38  ARG E NH2 
10032 N N   . GLN E 39  ? 2.6937 2.6890 1.8417 -0.9942 0.0944  -0.1424 39  GLN E N   
10033 C CA  . GLN E 39  ? 2.7558 2.7511 1.8795 -1.0040 0.1149  -0.1546 39  GLN E CA  
10034 C C   . GLN E 39  ? 2.7806 2.7943 1.8966 -1.0103 0.1353  -0.1737 39  GLN E C   
10035 O O   . GLN E 39  ? 2.7582 2.7710 1.8769 -1.0077 0.1404  -0.1791 39  GLN E O   
10036 C CB  . GLN E 39  ? 2.7557 2.7293 1.8724 -1.0024 0.1171  -0.1517 39  GLN E CB  
10037 C CG  . GLN E 39  ? 2.8223 2.7909 1.9155 -1.0120 0.1357  -0.1630 39  GLN E CG  
10038 C CD  . GLN E 39  ? 2.8222 2.7668 1.9159 -1.0092 0.1327  -0.1572 39  GLN E CD  
10039 O OE1 . GLN E 39  ? 2.7746 2.7081 1.8805 -1.0017 0.1260  -0.1516 39  GLN E OE1 
10040 N NE2 . GLN E 39  ? 2.8792 2.8155 1.9619 -1.0156 0.1380  -0.1590 39  GLN E NE2 
10041 N N   . ALA E 40  ? 2.8188 2.8492 1.9271 -1.0190 0.1465  -0.1837 40  ALA E N   
10042 C CA  . ALA E 40  ? 2.8527 2.9022 1.9581 -1.0259 0.1658  -0.2024 40  ALA E CA  
10043 C C   . ALA E 40  ? 2.8956 2.9348 1.9791 -1.0326 0.1835  -0.2115 40  ALA E C   
10044 O O   . ALA E 40  ? 2.9173 2.9385 1.9860 -1.0341 0.1829  -0.2059 40  ALA E O   
10045 C CB  . ALA E 40  ? 2.9002 2.9710 2.0059 -1.0339 0.1731  -0.2112 40  ALA E CB  
10046 N N   . PRO E 41  ? 2.9725 3.0216 2.0556 -1.0368 0.1980  -0.2257 41  PRO E N   
10047 C CA  . PRO E 41  ? 3.0136 3.0497 2.0759 -1.0431 0.2137  -0.2340 41  PRO E CA  
10048 C C   . PRO E 41  ? 3.0882 3.1221 2.1303 -1.0530 0.2253  -0.2397 41  PRO E C   
10049 O O   . PRO E 41  ? 3.1343 3.1875 2.1762 -1.0606 0.2334  -0.2483 41  PRO E O   
10050 C CB  . PRO E 41  ? 3.0277 3.0803 2.0978 -1.0475 0.2257  -0.2486 41  PRO E CB  
10051 C CG  . PRO E 41  ? 3.0082 3.0855 2.1034 -1.0446 0.2180  -0.2507 41  PRO E CG  
10052 C CD  . PRO E 41  ? 2.9568 3.0275 2.0610 -1.0355 0.1985  -0.2343 41  PRO E CD  
10053 N N   . GLY E 42  ? 2.9672 2.9768 1.9935 -1.0531 0.2258  -0.2354 42  GLY E N   
10054 C CA  . GLY E 42  ? 3.0412 3.0442 2.0487 -1.0619 0.2346  -0.2398 42  GLY E CA  
10055 C C   . GLY E 42  ? 3.0500 3.0525 2.0587 -1.0613 0.2217  -0.2287 42  GLY E C   
10056 O O   . GLY E 42  ? 3.1153 3.1121 2.1085 -1.0693 0.2278  -0.2319 42  GLY E O   
10057 N N   . GLN E 43  ? 2.9246 2.9314 1.9513 -1.0527 0.2034  -0.2154 43  GLN E N   
10058 C CA  . GLN E 43  ? 2.9309 2.9390 1.9603 -1.0529 0.1902  -0.2043 43  GLN E CA  
10059 C C   . GLN E 43  ? 2.8869 2.8738 1.9278 -1.0436 0.1683  -0.1852 43  GLN E C   
10060 O O   . GLN E 43  ? 2.8594 2.8306 1.9057 -1.0373 0.1651  -0.1818 43  GLN E O   
10061 C CB  . GLN E 43  ? 2.9046 2.9358 1.9488 -1.0518 0.1861  -0.2049 43  GLN E CB  
10062 C CG  . GLN E 43  ? 2.9426 2.9979 1.9852 -1.0600 0.2061  -0.2241 43  GLN E CG  
10063 C CD  . GLN E 43  ? 3.0319 3.0890 2.0518 -1.0731 0.2243  -0.2362 43  GLN E CD  
10064 O OE1 . GLN E 43  ? 3.0746 3.1276 2.0827 -1.0784 0.2216  -0.2318 43  GLN E OE1 
10065 N NE2 . GLN E 43  ? 3.0650 3.1273 2.0789 -1.0788 0.2420  -0.2513 43  GLN E NE2 
10066 N N   . GLY E 44  ? 2.8044 2.7908 1.8507 -1.0433 0.1530  -0.1726 44  GLY E N   
10067 C CA  . GLY E 44  ? 2.7677 2.7365 1.8302 -1.0354 0.1301  -0.1531 44  GLY E CA  
10068 C C   . GLY E 44  ? 2.6903 2.6629 1.7768 -1.0249 0.1120  -0.1413 44  GLY E C   
10069 O O   . GLY E 44  ? 2.6598 2.6451 1.7515 -1.0219 0.1173  -0.1486 44  GLY E O   
10070 N N   . LEU E 45  ? 2.8975 2.8586 2.0013 -1.0194 0.0892  -0.1224 45  LEU E N   
10071 C CA  . LEU E 45  ? 2.8269 2.7871 1.9566 -1.0089 0.0689  -0.1086 45  LEU E CA  
10072 C C   . LEU E 45  ? 2.8240 2.7939 1.9590 -1.0101 0.0562  -0.1013 45  LEU E C   
10073 O O   . LEU E 45  ? 2.8694 2.8372 1.9960 -1.0168 0.0517  -0.0960 45  LEU E O   
10074 C CB  . LEU E 45  ? 2.7988 2.7397 1.9510 -1.0018 0.0508  -0.0916 45  LEU E CB  
10075 C CG  . LEU E 45  ? 2.7968 2.7253 1.9493 -0.9997 0.0619  -0.0978 45  LEU E CG  
10076 C CD1 . LEU E 45  ? 2.7919 2.7029 1.9706 -0.9955 0.0465  -0.0814 45  LEU E CD1 
10077 C CD2 . LEU E 45  ? 2.7423 2.6735 1.8998 -0.9929 0.0660  -0.1034 45  LEU E CD2 
10078 N N   . GLU E 46  ? 2.7310 2.7105 1.8803 -1.0040 0.0502  -0.1014 46  GLU E N   
10079 C CA  . GLU E 46  ? 2.7307 2.7189 1.8879 -1.0045 0.0385  -0.0965 46  GLU E CA  
10080 C C   . GLU E 46  ? 2.6946 2.6759 1.8804 -0.9933 0.0143  -0.0813 46  GLU E C   
10081 O O   . GLU E 46  ? 2.6562 2.6393 1.8536 -0.9861 0.0148  -0.0845 46  GLU E O   
10082 C CB  . GLU E 46  ? 2.7492 2.7593 1.8987 -1.0096 0.0568  -0.1154 46  GLU E CB  
10083 C CG  . GLU E 46  ? 2.7549 2.7745 1.9135 -1.0109 0.0470  -0.1136 46  GLU E CG  
10084 C CD  . GLU E 46  ? 2.7863 2.8295 1.9411 -1.0169 0.0666  -0.1342 46  GLU E CD  
10085 O OE1 . GLU E 46  ? 2.8224 2.8745 1.9744 -1.0233 0.0669  -0.1373 46  GLU E OE1 
10086 O OE2 . GLU E 46  ? 2.7822 2.8352 1.9375 -1.0161 0.0819  -0.1476 46  GLU E OE2 
10087 N N   . TRP E 47  ? 2.5162 2.4889 1.7129 -0.9926 -0.0073 -0.0645 47  TRP E N   
10088 C CA  . TRP E 47  ? 2.4913 2.4561 1.7165 -0.9829 -0.0328 -0.0482 47  TRP E CA  
10089 C C   . TRP E 47  ? 2.4608 2.4371 1.6948 -0.9806 -0.0368 -0.0542 47  TRP E C   
10090 O O   . TRP E 47  ? 2.4787 2.4630 1.7030 -0.9875 -0.0337 -0.0598 47  TRP E O   
10091 C CB  . TRP E 47  ? 2.5253 2.4765 1.7594 -0.9843 -0.0545 -0.0282 47  TRP E CB  
10092 C CG  . TRP E 47  ? 2.5099 2.4514 1.7756 -0.9753 -0.0824 -0.0091 47  TRP E CG  
10093 C CD1 . TRP E 47  ? 2.4867 2.4190 1.7775 -0.9668 -0.0937 0.0024  47  TRP E CD1 
10094 C CD2 . TRP E 47  ? 2.5153 2.4550 1.7923 -0.9745 -0.1024 0.0002  47  TRP E CD2 
10095 N NE1 . TRP E 47  ? 2.4829 2.4087 1.8002 -0.9608 -0.1195 0.0190  47  TRP E NE1 
10096 C CE2 . TRP E 47  ? 2.5006 2.4298 1.8090 -0.9652 -0.1258 0.0179  47  TRP E CE2 
10097 C CE3 . TRP E 47  ? 2.5297 2.4752 1.7941 -0.9811 -0.1025 -0.0052 47  TRP E CE3 
10098 C CZ2 . TRP E 47  ? 2.5030 2.4265 1.8291 -0.9624 -0.1500 0.0304  47  TRP E CZ2 
10099 C CZ3 . TRP E 47  ? 2.5265 2.4654 1.8083 -0.9781 -0.1263 0.0064  47  TRP E CZ3 
10100 C CH2 . TRP E 47  ? 2.5146 2.4421 1.8262 -0.9688 -0.1501 0.0241  47  TRP E CH2 
10101 N N   . LEU E 48  ? 2.5593 2.5360 1.8129 -0.9712 -0.0439 -0.0537 48  LEU E N   
10102 C CA  . LEU E 48  ? 2.5142 2.4999 1.7823 -0.9674 -0.0512 -0.0590 48  LEU E CA  
10103 C C   . LEU E 48  ? 2.5111 2.4852 1.8017 -0.9619 -0.0804 -0.0411 48  LEU E C   
10104 O O   . LEU E 48  ? 2.4986 2.4774 1.7943 -0.9633 -0.0878 -0.0442 48  LEU E O   
10105 C CB  . LEU E 48  ? 2.4577 2.4500 1.7358 -0.9605 -0.0445 -0.0688 48  LEU E CB  
10106 C CG  . LEU E 48  ? 2.4618 2.4649 1.7219 -0.9647 -0.0175 -0.0866 48  LEU E CG  
10107 C CD1 . LEU E 48  ? 2.4193 2.4247 1.6928 -0.9571 -0.0175 -0.0918 48  LEU E CD1 
10108 C CD2 . LEU E 48  ? 2.5117 2.5338 1.7590 -0.9736 0.0002  -0.1042 48  LEU E CD2 
10109 N N   . GLY E 49  ? 2.4401 2.3993 1.7460 -0.9560 -0.0971 -0.0232 49  GLY E N   
10110 C CA  . GLY E 49  ? 2.4409 2.3886 1.7712 -0.9506 -0.1257 -0.0051 49  GLY E CA  
10111 C C   . GLY E 49  ? 2.4379 2.3740 1.7897 -0.9429 -0.1383 0.0105  49  GLY E C   
10112 O O   . GLY E 49  ? 2.4344 2.3705 1.7812 -0.9420 -0.1246 0.0064  49  GLY E O   
10113 N N   . TRP E 50  ? 2.2582 2.1841 1.6354 -0.9378 -0.1648 0.0282  50  TRP E N   
10114 C CA  . TRP E 50  ? 2.2526 2.1695 1.6564 -0.9302 -0.1777 0.0433  50  TRP E CA  
10115 C C   . TRP E 50  ? 2.2235 2.1348 1.6536 -0.9230 -0.2018 0.0539  50  TRP E C   
10116 O O   . TRP E 50  ? 2.2158 2.1268 1.6453 -0.9243 -0.2125 0.0528  50  TRP E O   
10117 C CB  . TRP E 50  ? 2.2994 2.2077 1.7130 -0.9328 -0.1854 0.0597  50  TRP E CB  
10118 C CG  . TRP E 50  ? 2.3388 2.2392 1.7621 -0.9361 -0.2081 0.0767  50  TRP E CG  
10119 C CD1 . TRP E 50  ? 2.3519 2.2519 1.7646 -0.9400 -0.2167 0.0751  50  TRP E CD1 
10120 C CD2 . TRP E 50  ? 2.3640 2.2556 1.8096 -0.9367 -0.2241 0.0974  50  TRP E CD2 
10121 N NE1 . TRP E 50  ? 2.3974 2.2869 1.8210 -0.9432 -0.2385 0.0943  50  TRP E NE1 
10122 C CE2 . TRP E 50  ? 2.4035 2.2886 1.8485 -0.9411 -0.2437 0.1087  50  TRP E CE2 
10123 C CE3 . TRP E 50  ? 2.3406 2.2292 1.8102 -0.9339 -0.2238 0.1074  50  TRP E CE3 
10124 C CZ2 . TRP E 50  ? 2.4275 2.3035 1.8933 -0.9431 -0.2640 0.1307  50  TRP E CZ2 
10125 C CZ3 . TRP E 50  ? 2.3449 2.2264 1.8402 -0.9353 -0.2428 0.1286  50  TRP E CZ3 
10126 C CH2 . TRP E 50  ? 2.3912 2.2666 1.8837 -0.9399 -0.2633 0.1406  50  TRP E CH2 
10127 N N   . ILE E 51  ? 2.2410 2.1472 1.6949 -0.9158 -0.2099 0.0636  51  ILE E N   
10128 C CA  . ILE E 51  ? 2.2056 2.1059 1.6859 -0.9086 -0.2319 0.0741  51  ILE E CA  
10129 C C   . ILE E 51  ? 2.2373 2.1284 1.7499 -0.9049 -0.2495 0.0971  51  ILE E C   
10130 O O   . ILE E 51  ? 2.2583 2.1495 1.7763 -0.9051 -0.2394 0.0998  51  ILE E O   
10131 C CB  . ILE E 51  ? 2.1380 2.0436 1.6167 -0.9032 -0.2223 0.0602  51  ILE E CB  
10132 C CG1 . ILE E 51  ? 2.0855 1.9843 1.5909 -0.8959 -0.2457 0.0705  51  ILE E CG1 
10133 C CG2 . ILE E 51  ? 2.1475 2.0542 1.6229 -0.9020 -0.2053 0.0566  51  ILE E CG2 
10134 C CD1 . ILE E 51  ? 2.0143 1.9184 1.5173 -0.8913 -0.2389 0.0554  51  ILE E CD1 
10135 N N   . ASN E 52  ? 2.1715 2.0547 1.7078 -0.9017 -0.2758 0.1135  52  ASN E N   
10136 C CA  . ASN E 52  ? 2.1924 2.0687 1.7660 -0.8974 -0.2943 0.1361  52  ASN E CA  
10137 C C   . ASN E 52  ? 2.1290 2.0051 1.7178 -0.8901 -0.2960 0.1350  52  ASN E C   
10138 O O   . ASN E 52  ? 2.0676 1.9410 1.6577 -0.8869 -0.3077 0.1328  52  ASN E O   
10139 C CB  . ASN E 52  ? 2.2197 2.0870 1.8103 -0.8985 -0.3228 0.1556  52  ASN E CB  
10140 C CG  . ASN E 52  ? 2.2518 2.1139 1.8852 -0.8945 -0.3426 0.1811  52  ASN E CG  
10141 O OD1 . ASN E 52  ? 2.2278 2.0913 1.8826 -0.8889 -0.3410 0.1845  52  ASN E OD1 
10142 N ND2 . ASN E 52  ? 2.3076 2.1638 1.9545 -0.8981 -0.3612 0.1996  52  ASN E ND2 
10143 N N   . PRO E 53  A 2.1742 2.0521 1.7753 -0.8875 -0.2847 0.1359  52  PRO E N   
10144 C CA  . PRO E 53  A 2.1161 1.9933 1.7266 -0.8816 -0.2845 0.1332  52  PRO E CA  
10145 C C   . PRO E 53  A 2.0799 1.9500 1.7252 -0.8768 -0.3114 0.1537  52  PRO E C   
10146 O O   . PRO E 53  A 2.0058 1.8740 1.6556 -0.8723 -0.3159 0.1512  52  PRO E O   
10147 C CB  . PRO E 53  A 2.1508 2.0297 1.7668 -0.8816 -0.2654 0.1306  52  PRO E CB  
10148 C CG  . PRO E 53  A 2.1809 2.0636 1.7750 -0.8877 -0.2488 0.1218  52  PRO E CG  
10149 C CD  . PRO E 53  A 2.2136 2.0941 1.8148 -0.8905 -0.2675 0.1347  52  PRO E CD  
10150 N N   . HIS E 54  ? 2.3105 2.1767 1.9810 -0.8779 -0.3300 0.1744  53  HIS E N   
10151 C CA  . HIS E 54  ? 2.2598 2.1192 1.9637 -0.8739 -0.3573 0.1957  53  HIS E CA  
10152 C C   . HIS E 54  ? 2.1959 2.0490 1.8864 -0.8730 -0.3735 0.1920  53  HIS E C   
10153 O O   . HIS E 54  ? 2.1121 1.9614 1.8110 -0.8683 -0.3828 0.1925  53  HIS E O   
10154 C CB  . HIS E 54  ? 2.3134 2.1709 2.0479 -0.8761 -0.3727 0.2193  53  HIS E CB  
10155 C CG  . HIS E 54  ? 2.2477 2.0978 2.0148 -0.8731 -0.4033 0.2433  53  HIS E CG  
10156 N ND1 . HIS E 54  ? 2.1647 2.0138 1.9595 -0.8678 -0.4109 0.2532  53  HIS E ND1 
10157 C CD2 . HIS E 54  ? 2.2742 2.1165 2.0493 -0.8752 -0.4288 0.2601  53  HIS E CD2 
10158 C CE1 . HIS E 54  ? 2.1274 1.9692 1.9469 -0.8665 -0.4401 0.2754  53  HIS E CE1 
10159 N NE2 . HIS E 54  ? 2.2042 2.0411 2.0119 -0.8708 -0.4519 0.2801  53  HIS E NE2 
10160 N N   . SER E 55  ? 2.2803 2.1315 1.9506 -0.8778 -0.3767 0.1875  54  SER E N   
10161 C CA  . SER E 55  ? 2.2310 2.0750 1.8918 -0.8776 -0.3921 0.1836  54  SER E CA  
10162 C C   . SER E 55  ? 2.1774 2.0276 1.8104 -0.8770 -0.3741 0.1561  54  SER E C   
10163 O O   . SER E 55  ? 2.1431 1.9885 1.7773 -0.8741 -0.3855 0.1505  54  SER E O   
10164 C CB  . SER E 55  ? 2.2967 2.1346 1.9495 -0.8839 -0.4043 0.1914  54  SER E CB  
10165 O OG  . SER E 55  ? 2.3589 2.2047 1.9826 -0.8899 -0.3820 0.1759  54  SER E OG  
10166 N N   . GLY E 56  ? 2.3500 2.2109 1.9604 -0.8795 -0.3468 0.1388  55  GLY E N   
10167 C CA  . GLY E 56  ? 2.3127 2.1819 1.8977 -0.8801 -0.3290 0.1132  55  GLY E CA  
10168 C C   . GLY E 56  ? 2.3493 2.2215 1.9122 -0.8866 -0.3239 0.1025  55  GLY E C   
10169 O O   . GLY E 56  ? 2.3289 2.2108 1.8729 -0.8879 -0.3071 0.0804  55  GLY E O   
10170 N N   . ASP E 57  ? 2.3546 2.2192 1.9206 -0.8912 -0.3379 0.1177  56  ASP E N   
10171 C CA  . ASP E 57  ? 2.3982 2.2642 1.9418 -0.8986 -0.3335 0.1089  56  ASP E CA  
10172 C C   . ASP E 57  ? 2.4386 2.3172 1.9553 -0.9040 -0.3039 0.0934  56  ASP E C   
10173 O O   . ASP E 57  ? 2.4599 2.3416 1.9770 -0.9038 -0.2924 0.0973  56  ASP E O   
10174 C CB  . ASP E 57  ? 2.4852 2.3389 2.0370 -0.9030 -0.3554 0.1309  56  ASP E CB  
10175 C CG  . ASP E 57  ? 2.4855 2.3251 2.0596 -0.8992 -0.3858 0.1453  56  ASP E CG  
10176 O OD1 . ASP E 57  ? 2.4188 2.2584 1.9990 -0.8938 -0.3892 0.1349  56  ASP E OD1 
10177 O OD2 . ASP E 57  ? 2.5672 2.3955 2.1533 -0.9018 -0.4072 0.1672  56  ASP E OD2 
10178 N N   . THR E 58  ? 2.2964 2.1823 1.7908 -0.9092 -0.2915 0.0752  57  THR E N   
10179 C CA  . THR E 58  ? 2.3126 2.2112 1.7801 -0.9151 -0.2630 0.0593  57  THR E CA  
10180 C C   . THR E 58  ? 2.3530 2.2519 1.8001 -0.9247 -0.2604 0.0558  57  THR E C   
10181 O O   . THR E 58  ? 2.3763 2.2686 1.8270 -0.9262 -0.2764 0.0571  57  THR E O   
10182 C CB  . THR E 58  ? 2.3224 2.2350 1.7824 -0.9123 -0.2436 0.0357  57  THR E CB  
10183 O OG1 . THR E 58  ? 2.3518 2.2667 1.8163 -0.9114 -0.2515 0.0241  57  THR E OG1 
10184 C CG2 . THR E 58  ? 2.2865 2.1978 1.7633 -0.9038 -0.2454 0.0388  57  THR E CG2 
10185 N N   . THR E 59  ? 2.3736 2.2788 1.7983 -0.9316 -0.2404 0.0511  58  THR E N   
10186 C CA  . THR E 59  ? 2.4196 2.3290 1.8189 -0.9419 -0.2299 0.0423  58  THR E CA  
10187 C C   . THR E 59  ? 2.4369 2.3627 1.8134 -0.9457 -0.1980 0.0221  58  THR E C   
10188 O O   . THR E 59  ? 2.4180 2.3452 1.7899 -0.9451 -0.1862 0.0239  58  THR E O   
10189 C CB  . THR E 59  ? 2.4255 2.3232 1.8200 -0.9483 -0.2415 0.0613  58  THR E CB  
10190 O OG1 . THR E 59  ? 2.4128 2.2953 1.8298 -0.9451 -0.2724 0.0808  58  THR E OG1 
10191 C CG2 . THR E 59  ? 2.4777 2.3791 1.8430 -0.9600 -0.2299 0.0520  58  THR E CG2 
10192 N N   . THR E 60  ? 2.5491 2.4873 1.9131 -0.9499 -0.1845 0.0024  59  THR E N   
10193 C CA  . THR E 60  ? 2.5724 2.5281 1.9172 -0.9540 -0.1545 -0.0180 59  THR E CA  
10194 C C   . THR E 60  ? 2.6207 2.5811 1.9385 -0.9664 -0.1407 -0.0235 59  THR E C   
10195 O O   . THR E 60  ? 2.6485 2.6040 1.9632 -0.9716 -0.1515 -0.0208 59  THR E O   
10196 C CB  . THR E 60  ? 2.5878 2.5580 1.9431 -0.9496 -0.1479 -0.0380 59  THR E CB  
10197 O OG1 . THR E 60  ? 2.5471 2.5111 1.9272 -0.9384 -0.1632 -0.0320 59  THR E OG1 
10198 C CG2 . THR E 60  ? 2.6097 2.5987 1.9490 -0.9535 -0.1179 -0.0578 59  THR E CG2 
10199 N N   . SER E 61  ? 2.6537 2.6219 1.9510 -0.9716 -0.1173 -0.0310 60  SER E N   
10200 C CA  . SER E 61  ? 2.7076 2.6829 1.9779 -0.9840 -0.1004 -0.0396 60  SER E CA  
10201 C C   . SER E 61  ? 2.7503 2.7403 2.0211 -0.9874 -0.0933 -0.0577 60  SER E C   
10202 O O   . SER E 61  ? 2.7461 2.7491 2.0311 -0.9815 -0.0870 -0.0720 60  SER E O   
10203 C CB  . SER E 61  ? 2.7190 2.7028 1.9697 -0.9880 -0.0744 -0.0494 60  SER E CB  
10204 O OG  . SER E 61  ? 2.7762 2.7660 2.0004 -1.0005 -0.0584 -0.0570 60  SER E OG  
10205 N N   . GLN E 62  ? 2.7454 2.7335 2.0022 -0.9972 -0.0950 -0.0576 61  GLN E N   
10206 C CA  . GLN E 62  ? 2.7855 2.7855 2.0478 -0.9997 -0.0930 -0.0738 61  GLN E CA  
10207 C C   . GLN E 62  ? 2.8234 2.8490 2.0800 -1.0033 -0.0641 -0.0986 61  GLN E C   
10208 O O   . GLN E 62  ? 2.8487 2.8879 2.1203 -1.0012 -0.0629 -0.1149 61  GLN E O   
10209 C CB  . GLN E 62  ? 2.8259 2.8162 2.0724 -1.0104 -0.1014 -0.0677 61  GLN E CB  
10210 C CG  . GLN E 62  ? 2.7939 2.7613 2.0550 -1.0053 -0.1344 -0.0472 61  GLN E CG  
10211 C CD  . GLN E 62  ? 2.8030 2.7712 2.0854 -0.9997 -0.1492 -0.0563 61  GLN E CD  
10212 O OE1 . GLN E 62  ? 2.8621 2.8375 2.1376 -1.0066 -0.1442 -0.0704 61  GLN E OE1 
10213 N NE2 . GLN E 62  ? 2.7565 2.7175 2.0656 -0.9870 -0.1675 -0.0495 61  GLN E NE2 
10214 N N   . LYS E 63  ? 2.7547 2.7873 1.9917 -1.0088 -0.0419 -0.1027 62  LYS E N   
10215 C CA  . LYS E 63  ? 2.7866 2.8435 2.0214 -1.0115 -0.0155 -0.1254 62  LYS E CA  
10216 C C   . LYS E 63  ? 2.7551 2.8211 2.0173 -0.9995 -0.0187 -0.1344 62  LYS E C   
10217 O O   . LYS E 63  ? 2.7883 2.8758 2.0604 -1.0001 -0.0058 -0.1549 62  LYS E O   
10218 C CB  . LYS E 63  ? 2.7977 2.8559 2.0084 -1.0176 0.0052  -0.1261 62  LYS E CB  
10219 C CG  . LYS E 63  ? 2.8707 2.9529 2.0788 -1.0211 0.0324  -0.1487 62  LYS E CG  
10220 C CD  . LYS E 63  ? 2.8567 2.9369 2.0400 -1.0272 0.0510  -0.1493 62  LYS E CD  
10221 C CE  . LYS E 63  ? 2.9460 3.0482 2.1310 -1.0292 0.0749  -0.1706 62  LYS E CE  
10222 N NZ  . LYS E 63  ? 2.9045 3.0023 2.0666 -1.0342 0.0916  -0.1719 62  LYS E NZ  
10223 N N   . PHE E 64  ? 2.8065 2.8568 2.0825 -0.9889 -0.0367 -0.1196 63  PHE E N   
10224 C CA  . PHE E 64  ? 2.7744 2.8300 2.0743 -0.9777 -0.0413 -0.1257 63  PHE E CA  
10225 C C   . PHE E 64  ? 2.7560 2.8035 2.0827 -0.9683 -0.0677 -0.1211 63  PHE E C   
10226 O O   . PHE E 64  ? 2.7301 2.7799 2.0776 -0.9585 -0.0745 -0.1251 63  PHE E O   
10227 C CB  . PHE E 64  ? 2.7231 2.7674 2.0186 -0.9728 -0.0402 -0.1143 63  PHE E CB  
10228 C CG  . PHE E 64  ? 2.7419 2.7923 2.0118 -0.9812 -0.0153 -0.1204 63  PHE E CG  
10229 C CD1 . PHE E 64  ? 2.7680 2.8382 2.0351 -0.9842 0.0071  -0.1404 63  PHE E CD1 
10230 C CD2 . PHE E 64  ? 2.7394 2.7756 1.9893 -0.9864 -0.0153 -0.1069 63  PHE E CD2 
10231 C CE1 . PHE E 64  ? 2.7901 2.8646 2.0333 -0.9923 0.0294  -0.1466 63  PHE E CE1 
10232 C CE2 . PHE E 64  ? 2.7634 2.8036 1.9896 -0.9939 0.0066  -0.1137 63  PHE E CE2 
10233 C CZ  . PHE E 64  ? 2.7889 2.8478 2.0109 -0.9971 0.0294  -0.1336 63  PHE E CZ  
10234 N N   . GLN E 65  ? 2.7755 2.8123 2.1016 -0.9712 -0.0837 -0.1127 64  GLN E N   
10235 C CA  . GLN E 65  ? 2.7608 2.7866 2.1113 -0.9626 -0.1109 -0.1072 64  GLN E CA  
10236 C C   . GLN E 65  ? 2.7861 2.8289 2.1592 -0.9560 -0.1100 -0.1290 64  GLN E C   
10237 O O   . GLN E 65  ? 2.8383 2.9007 2.2081 -0.9618 -0.0940 -0.1489 64  GLN E O   
10238 C CB  . GLN E 65  ? 2.7855 2.7991 2.1284 -0.9691 -0.1251 -0.0991 64  GLN E CB  
10239 C CG  . GLN E 65  ? 2.7996 2.8010 2.1668 -0.9607 -0.1536 -0.0954 64  GLN E CG  
10240 C CD  . GLN E 65  ? 2.8121 2.7951 2.1944 -0.9512 -0.1742 -0.0745 64  GLN E CD  
10241 O OE1 . GLN E 65  ? 2.8161 2.7876 2.1876 -0.9536 -0.1756 -0.0559 64  GLN E OE1 
10242 N NE2 . GLN E 65  ? 2.8094 2.7901 2.2182 -0.9403 -0.1906 -0.0781 64  GLN E NE2 
10243 N N   . GLY E 66  ? 2.7140 2.7496 2.1111 -0.9440 -0.1277 -0.1254 65  GLY E N   
10244 C CA  . GLY E 66  ? 2.7375 2.7864 2.1592 -0.9360 -0.1318 -0.1447 65  GLY E CA  
10245 C C   . GLY E 66  ? 2.7387 2.8058 2.1626 -0.9342 -0.1122 -0.1588 65  GLY E C   
10246 O O   . GLY E 66  ? 2.7592 2.8381 2.2051 -0.9270 -0.1163 -0.1752 65  GLY E O   
10247 N N   . ARG E 67  ? 2.7573 2.8265 2.1594 -0.9407 -0.0924 -0.1536 66  ARG E N   
10248 C CA  . ARG E 67  ? 2.7563 2.8407 2.1567 -0.9406 -0.0730 -0.1658 66  ARG E CA  
10249 C C   . ARG E 67  ? 2.6954 2.7648 2.0906 -0.9362 -0.0750 -0.1501 66  ARG E C   
10250 O O   . ARG E 67  ? 2.6782 2.7519 2.0846 -0.9302 -0.0740 -0.1563 66  ARG E O   
10251 C CB  . ARG E 67  ? 2.7999 2.9023 2.1785 -0.9531 -0.0449 -0.1784 66  ARG E CB  
10252 C CG  . ARG E 67  ? 2.8142 2.9388 2.1994 -0.9533 -0.0268 -0.1986 66  ARG E CG  
10253 C CD  . ARG E 67  ? 2.8684 3.0143 2.2376 -0.9658 -0.0001 -0.2143 66  ARG E CD  
10254 N NE  . ARG E 67  ? 2.8660 3.0054 2.2038 -0.9755 0.0172  -0.2053 66  ARG E NE  
10255 C CZ  . ARG E 67  ? 2.8508 2.9925 2.1770 -0.9777 0.0329  -0.2074 66  ARG E CZ  
10256 N NH1 . ARG E 67  ? 2.8358 2.9849 2.1787 -0.9713 0.0327  -0.2164 66  ARG E NH1 
10257 N NH2 . ARG E 67  ? 2.8552 2.9898 2.1530 -0.9862 0.0473  -0.2005 66  ARG E NH2 
10258 N N   . VAL E 68  ? 2.7886 2.8404 2.1674 -0.9393 -0.0785 -0.1301 67  VAL E N   
10259 C CA  . VAL E 68  ? 2.7337 2.7696 2.1088 -0.9350 -0.0827 -0.1138 67  VAL E CA  
10260 C C   . VAL E 68  ? 2.6939 2.7107 2.0879 -0.9267 -0.1114 -0.0956 67  VAL E C   
10261 O O   . VAL E 68  ? 2.6987 2.7071 2.0949 -0.9283 -0.1256 -0.0868 67  VAL E O   
10262 C CB  . VAL E 68  ? 2.7298 2.7597 2.0774 -0.9434 -0.0686 -0.1049 67  VAL E CB  
10263 C CG1 . VAL E 68  ? 2.6994 2.7116 2.0464 -0.9384 -0.0761 -0.0877 67  VAL E CG1 
10264 C CG2 . VAL E 68  ? 2.7654 2.8132 2.0947 -0.9515 -0.0401 -0.1229 67  VAL E CG2 
10265 N N   . TYR E 69  ? 2.5824 2.5916 1.9895 -0.9184 -0.1202 -0.0899 68  TYR E N   
10266 C CA  . TYR E 69  ? 2.5480 2.5403 1.9761 -0.9100 -0.1471 -0.0735 68  TYR E CA  
10267 C C   . TYR E 69  ? 2.4986 2.4769 1.9247 -0.9071 -0.1498 -0.0566 68  TYR E C   
10268 O O   . TYR E 69  ? 2.4852 2.4673 1.9045 -0.9065 -0.1361 -0.0627 68  TYR E O   
10269 C CB  . TYR E 69  ? 2.5586 2.5553 2.0112 -0.9014 -0.1598 -0.0845 68  TYR E CB  
10270 C CG  . TYR E 69  ? 2.6082 2.6166 2.0695 -0.9023 -0.1628 -0.1008 68  TYR E CG  
10271 C CD1 . TYR E 69  ? 2.6161 2.6139 2.0903 -0.8998 -0.1850 -0.0938 68  TYR E CD1 
10272 C CD2 . TYR E 69  ? 2.6502 2.6801 2.1078 -0.9058 -0.1441 -0.1236 68  TYR E CD2 
10273 C CE1 . TYR E 69  ? 2.6655 2.6730 2.1471 -0.9006 -0.1883 -0.1100 68  TYR E CE1 
10274 C CE2 . TYR E 69  ? 2.7006 2.7421 2.1679 -0.9064 -0.1472 -0.1396 68  TYR E CE2 
10275 C CZ  . TYR E 69  ? 2.7085 2.7383 2.1870 -0.9037 -0.1691 -0.1332 68  TYR E CZ  
10276 O OH  . TYR E 69  ? 2.7623 2.8028 2.2497 -0.9044 -0.1724 -0.1505 68  TYR E OH  
10277 N N   . MET E 70  ? 2.4377 2.4001 1.8716 -0.9056 -0.1682 -0.0359 69  MET E N   
10278 C CA  . MET E 70  ? 2.3942 2.3437 1.8317 -0.9028 -0.1735 -0.0185 69  MET E CA  
10279 C C   . MET E 70  ? 2.3701 2.3080 1.8348 -0.8942 -0.1987 -0.0056 69  MET E C   
10280 O O   . MET E 70  ? 2.3766 2.3089 1.8558 -0.8924 -0.2184 0.0010  69  MET E O   
10281 C CB  . MET E 70  ? 2.3883 2.3300 1.8174 -0.9082 -0.1752 -0.0039 69  MET E CB  
10282 C CG  . MET E 70  ? 2.4113 2.3620 1.8124 -0.9167 -0.1501 -0.0148 69  MET E CG  
10283 S SD  . MET E 70  ? 2.4231 2.3655 1.8159 -0.9237 -0.1559 0.0001  69  MET E SD  
10284 C CE  . MET E 70  ? 2.4648 2.4107 1.8585 -0.9271 -0.1668 -0.0042 69  MET E CE  
10285 N N   . THR E 71  ? 2.5379 2.4715 2.0086 -0.8897 -0.1980 -0.0020 70  THR E N   
10286 C CA  . THR E 71  ? 2.5156 2.4380 2.0114 -0.8822 -0.2203 0.0112  70  THR E CA  
10287 C C   . THR E 71  ? 2.4796 2.3934 1.9786 -0.8811 -0.2188 0.0252  70  THR E C   
10288 O O   . THR E 71  ? 2.4739 2.3904 1.9551 -0.8855 -0.1998 0.0213  70  THR E O   
10289 C CB  . THR E 71  ? 2.5291 2.4564 2.0334 -0.8767 -0.2227 -0.0027 70  THR E CB  
10290 O OG1 . THR E 71  ? 2.5304 2.4663 2.0178 -0.8786 -0.2007 -0.0171 70  THR E OG1 
10291 C CG2 . THR E 71  ? 2.5691 2.5045 2.0787 -0.8763 -0.2282 -0.0166 70  THR E CG2 
10292 N N   . ARG E 72  ? 2.2137 2.1170 1.7369 -0.8755 -0.2388 0.0410  71  ARG E N   
10293 C CA  . ARG E 72  ? 2.1829 2.0791 1.7144 -0.8742 -0.2377 0.0533  71  ARG E CA  
10294 C C   . ARG E 72  ? 2.1712 2.0602 1.7227 -0.8679 -0.2529 0.0604  71  ARG E C   
10295 O O   . ARG E 72  ? 2.1817 2.0678 1.7478 -0.8641 -0.2714 0.0630  71  ARG E O   
10296 C CB  . ARG E 72  ? 2.1678 2.0582 1.7140 -0.8760 -0.2470 0.0725  71  ARG E CB  
10297 C CG  . ARG E 72  ? 2.1737 2.0588 1.7396 -0.8746 -0.2723 0.0865  71  ARG E CG  
10298 C CD  . ARG E 72  ? 2.1569 2.0325 1.7550 -0.8691 -0.2952 0.1059  71  ARG E CD  
10299 N NE  . ARG E 72  ? 2.1676 2.0369 1.7815 -0.8686 -0.3196 0.1192  71  ARG E NE  
10300 C CZ  . ARG E 72  ? 2.1696 2.0310 1.8044 -0.8639 -0.3418 0.1295  71  ARG E CZ  
10301 N NH1 . ARG E 72  ? 2.1827 2.0368 1.8288 -0.8644 -0.3637 0.1412  71  ARG E NH1 
10302 N NH2 . ARG E 72  ? 2.1616 2.0212 1.8048 -0.8593 -0.3428 0.1283  71  ARG E NH2 
10303 N N   . ASP E 73  ? 2.4147 2.2998 1.9662 -0.8674 -0.2447 0.0630  72  ASP E N   
10304 C CA  . ASP E 73  ? 2.4035 2.2802 1.9753 -0.8626 -0.2585 0.0738  72  ASP E CA  
10305 C C   . ASP E 73  ? 2.3770 2.2478 1.9690 -0.8632 -0.2606 0.0920  72  ASP E C   
10306 O O   . ASP E 73  ? 2.3619 2.2324 1.9433 -0.8661 -0.2422 0.0874  72  ASP E O   
10307 C CB  . ASP E 73  ? 2.4109 2.2886 1.9651 -0.8622 -0.2457 0.0584  72  ASP E CB  
10308 C CG  . ASP E 73  ? 2.4072 2.2757 1.9796 -0.8578 -0.2604 0.0684  72  ASP E CG  
10309 O OD1 . ASP E 73  ? 2.3940 2.2557 1.9934 -0.8557 -0.2771 0.0883  72  ASP E OD1 
10310 O OD2 . ASP E 73  ? 2.4200 2.2881 1.9807 -0.8569 -0.2555 0.0566  72  ASP E OD2 
10311 N N   . LYS E 74  ? 2.4263 2.2922 2.0498 -0.8607 -0.2827 0.1124  73  LYS E N   
10312 C CA  . LYS E 74  ? 2.4047 2.2677 2.0570 -0.8611 -0.2855 0.1309  73  LYS E CA  
10313 C C   . LYS E 74  ? 2.3709 2.2292 2.0341 -0.8599 -0.2788 0.1341  73  LYS E C   
10314 O O   . LYS E 74  ? 2.3068 2.1645 1.9850 -0.8617 -0.2676 0.1400  73  LYS E O   
10315 C CB  . LYS E 74  ? 2.4052 2.2648 2.0907 -0.8588 -0.3124 0.1530  73  LYS E CB  
10316 C CG  . LYS E 74  ? 2.4156 2.2777 2.0922 -0.8614 -0.3185 0.1527  73  LYS E CG  
10317 C CD  . LYS E 74  ? 2.4103 2.2677 2.1207 -0.8605 -0.3441 0.1773  73  LYS E CD  
10318 C CE  . LYS E 74  ? 2.4200 2.2701 2.1403 -0.8566 -0.3683 0.1847  73  LYS E CE  
10319 N NZ  . LYS E 74  ? 2.4188 2.2634 2.1644 -0.8569 -0.3937 0.2072  73  LYS E NZ  
10320 N N   . SER E 75  ? 2.3884 2.2428 2.0467 -0.8572 -0.2852 0.1304  74  SER E N   
10321 C CA  . SER E 75  ? 2.3345 2.1827 2.0040 -0.8567 -0.2814 0.1356  74  SER E CA  
10322 C C   . SER E 75  ? 2.2922 2.1397 1.9385 -0.8608 -0.2541 0.1217  74  SER E C   
10323 O O   . SER E 75  ? 2.2256 2.0679 1.8896 -0.8620 -0.2462 0.1292  74  SER E O   
10324 C CB  . SER E 75  ? 2.3762 2.2195 2.0393 -0.8535 -0.2933 0.1321  74  SER E CB  
10325 O OG  . SER E 75  ? 2.4166 2.2630 2.0432 -0.8545 -0.2810 0.1096  74  SER E OG  
10326 N N   . ILE E 76  ? 2.2722 2.1243 1.8805 -0.8635 -0.2386 0.1015  75  ILE E N   
10327 C CA  . ILE E 76  ? 2.2408 2.0911 1.8218 -0.8681 -0.2129 0.0871  75  ILE E CA  
10328 C C   . ILE E 76  ? 2.2351 2.0901 1.8106 -0.8715 -0.1992 0.0835  75  ILE E C   
10329 O O   . ILE E 76  ? 2.2342 2.0882 1.7812 -0.8758 -0.1773 0.0688  75  ILE E O   
10330 C CB  . ILE E 76  ? 2.2826 2.1344 1.8250 -0.8696 -0.2032 0.0668  75  ILE E CB  
10331 C CG1 . ILE E 76  ? 2.3437 2.2060 1.8763 -0.8684 -0.2087 0.0580  75  ILE E CG1 
10332 C CG2 . ILE E 76  ? 2.2749 2.1191 1.8219 -0.8672 -0.2133 0.0699  75  ILE E CG2 
10333 C CD1 . ILE E 76  ? 2.3734 2.2413 1.8741 -0.8705 -0.1951 0.0365  75  ILE E CD1 
10334 N N   . ASN E 77  ? 2.1309 1.9899 1.7320 -0.8701 -0.2120 0.0968  76  ASN E N   
10335 C CA  . ASN E 77  ? 2.1424 2.0048 1.7437 -0.8734 -0.2014 0.0962  76  ASN E CA  
10336 C C   . ASN E 77  ? 2.1553 2.0234 1.7117 -0.8776 -0.1845 0.0749  76  ASN E C   
10337 O O   . ASN E 77  ? 2.1645 2.0323 1.7069 -0.8817 -0.1661 0.0669  76  ASN E O   
10338 C CB  . ASN E 77  ? 2.1395 1.9957 1.7615 -0.8748 -0.1868 0.1015  76  ASN E CB  
10339 C CG  . ASN E 77  ? 2.1313 1.9838 1.8048 -0.8712 -0.1998 0.1238  76  ASN E CG  
10340 O OD1 . ASN E 77  ? 2.1329 1.9887 1.8320 -0.8681 -0.2222 0.1391  76  ASN E OD1 
10341 N ND2 . ASN E 77  ? 2.1272 1.9724 1.8174 -0.8720 -0.1846 0.1262  76  ASN E ND2 
10342 N N   . THR E 78  ? 2.2115 2.0849 1.7485 -0.8768 -0.1897 0.0654  77  THR E N   
10343 C CA  . THR E 78  ? 2.2254 2.1060 1.7238 -0.8809 -0.1716 0.0444  77  THR E CA  
10344 C C   . THR E 78  ? 2.2436 2.1330 1.7389 -0.8811 -0.1800 0.0419  77  THR E C   
10345 O O   . THR E 78  ? 2.2428 2.1319 1.7562 -0.8770 -0.2000 0.0497  77  THR E O   
10346 C CB  . THR E 78  ? 2.2183 2.0981 1.6970 -0.8807 -0.1637 0.0312  77  THR E CB  
10347 O OG1 . THR E 78  ? 2.2071 2.0771 1.6829 -0.8821 -0.1531 0.0319  77  THR E OG1 
10348 C CG2 . THR E 78  ? 2.2367 2.1266 1.6822 -0.8853 -0.1450 0.0102  77  THR E CG2 
10349 N N   . ALA E 79  ? 2.3307 2.2270 1.8029 -0.8864 -0.1642 0.0307  78  ALA E N   
10350 C CA  . ALA E 79  ? 2.3541 2.2596 1.8173 -0.8885 -0.1660 0.0240  78  ALA E CA  
10351 C C   . ALA E 79  ? 2.3672 2.2833 1.8036 -0.8917 -0.1474 0.0019  78  ALA E C   
10352 O O   . ALA E 79  ? 2.3669 2.2833 1.7836 -0.8948 -0.1283 -0.0088 78  ALA E O   
10353 C CB  . ALA E 79  ? 2.3755 2.2819 1.8349 -0.8932 -0.1623 0.0287  78  ALA E CB  
10354 N N   . PHE E 80  ? 2.4091 2.3341 1.8474 -0.8911 -0.1530 -0.0055 79  PHE E N   
10355 C CA  . PHE E 80  ? 2.4260 2.3644 1.8479 -0.8939 -0.1372 -0.0267 79  PHE E CA  
10356 C C   . PHE E 80  ? 2.4597 2.4094 1.8723 -0.8991 -0.1303 -0.0349 79  PHE E C   
10357 O O   . PHE E 80  ? 2.4710 2.4179 1.8949 -0.8984 -0.1453 -0.0254 79  PHE E O   
10358 C CB  . PHE E 80  ? 2.4194 2.3605 1.8577 -0.8878 -0.1495 -0.0325 79  PHE E CB  
10359 C CG  . PHE E 80  ? 2.3910 2.3207 1.8390 -0.8830 -0.1582 -0.0242 79  PHE E CG  
10360 C CD1 . PHE E 80  ? 2.3845 2.3144 1.8172 -0.8848 -0.1433 -0.0341 79  PHE E CD1 
10361 C CD2 . PHE E 80  ? 2.3752 2.2937 1.8476 -0.8772 -0.1816 -0.0067 79  PHE E CD2 
10362 C CE1 . PHE E 80  ? 2.3624 2.2807 1.8016 -0.8813 -0.1509 -0.0267 79  PHE E CE1 
10363 C CE2 . PHE E 80  ? 2.3531 2.2615 1.8344 -0.8735 -0.1890 0.0010  79  PHE E CE2 
10364 C CZ  . PHE E 80  ? 2.3465 2.2544 1.8102 -0.8756 -0.1735 -0.0091 79  PHE E CZ  
10365 N N   . LEU E 81  ? 2.3160 2.2780 1.7076 -0.9049 -0.1076 -0.0526 80  LEU E N   
10366 C CA  . LEU E 81  ? 2.3536 2.3291 1.7347 -0.9111 -0.0970 -0.0641 80  LEU E CA  
10367 C C   . LEU E 81  ? 2.3687 2.3608 1.7534 -0.9109 -0.0891 -0.0843 80  LEU E C   
10368 O O   . LEU E 81  ? 2.3661 2.3630 1.7417 -0.9124 -0.0748 -0.0949 80  LEU E O   
10369 C CB  . LEU E 81  ? 2.3740 2.3507 1.7289 -0.9192 -0.0759 -0.0673 80  LEU E CB  
10370 C CG  . LEU E 81  ? 2.4186 2.4082 1.7594 -0.9272 -0.0630 -0.0777 80  LEU E CG  
10371 C CD1 . LEU E 81  ? 2.4292 2.4120 1.7774 -0.9275 -0.0798 -0.0638 80  LEU E CD1 
10372 C CD2 . LEU E 81  ? 2.4429 2.4345 1.7568 -0.9351 -0.0392 -0.0853 80  LEU E CD2 
10373 N N   . ASP E 82  ? 2.3514 2.3519 1.7510 -0.9092 -0.0991 -0.0901 81  ASP E N   
10374 C CA  . ASP E 82  ? 2.3746 2.3935 1.7824 -0.9090 -0.0927 -0.1112 81  ASP E CA  
10375 C C   . ASP E 82  ? 2.4186 2.4533 1.8135 -0.9177 -0.0762 -0.1234 81  ASP E C   
10376 O O   . ASP E 82  ? 2.4375 2.4707 1.8339 -0.9196 -0.0838 -0.1186 81  ASP E O   
10377 C CB  . ASP E 82  ? 2.3726 2.3905 1.8088 -0.9004 -0.1162 -0.1122 81  ASP E CB  
10378 C CG  . ASP E 82  ? 2.3366 2.3413 1.7865 -0.8922 -0.1314 -0.1033 81  ASP E CG  
10379 O OD1 . ASP E 82  ? 2.3426 2.3522 1.7917 -0.8910 -0.1239 -0.1130 81  ASP E OD1 
10380 O OD2 . ASP E 82  ? 2.3906 2.3800 1.8521 -0.8874 -0.1512 -0.0862 81  ASP E OD2 
10381 N N   . VAL E 83  ? 2.5039 2.5532 1.8862 -0.9237 -0.0539 -0.1391 82  VAL E N   
10382 C CA  . VAL E 83  ? 2.5518 2.6190 1.9236 -0.9325 -0.0363 -0.1533 82  VAL E CA  
10383 C C   . VAL E 83  ? 2.5776 2.6662 1.9689 -0.9307 -0.0342 -0.1750 82  VAL E C   
10384 O O   . VAL E 83  ? 2.5720 2.6671 1.9675 -0.9293 -0.0280 -0.1847 82  VAL E O   
10385 C CB  . VAL E 83  ? 2.5683 2.6367 1.9117 -0.9417 -0.0122 -0.1553 82  VAL E CB  
10386 C CG1 . VAL E 83  ? 2.6224 2.7073 1.9540 -0.9516 0.0046  -0.1672 82  VAL E CG1 
10387 C CG2 . VAL E 83  ? 2.5425 2.5888 1.8711 -0.9413 -0.0171 -0.1350 82  VAL E CG2 
10388 N N   . THR E 84  A 2.6517 2.7509 2.0557 -0.9308 -0.0403 -0.1832 82  THR E N   
10389 C CA  . THR E 84  A 2.6788 2.7975 2.1071 -0.9269 -0.0437 -0.2040 82  THR E CA  
10390 C C   . THR E 84  A 2.7324 2.8747 2.1545 -0.9366 -0.0235 -0.2221 82  THR E C   
10391 O O   . THR E 84  A 2.7553 2.8974 2.1539 -0.9464 -0.0086 -0.2176 82  THR E O   
10392 C CB  . THR E 84  A 2.6698 2.7817 2.1222 -0.9177 -0.0698 -0.2017 82  THR E CB  
10393 O OG1 . THR E 84  A 2.7185 2.8305 2.1643 -0.9230 -0.0707 -0.1995 82  THR E OG1 
10394 C CG2 . THR E 84  A 2.6330 2.7201 2.0896 -0.9096 -0.0897 -0.1810 82  THR E CG2 
10395 N N   . ARG E 85  B 2.5473 2.7103 1.9920 -0.9337 -0.0243 -0.2432 82  ARG E N   
10396 C CA  . ARG E 85  B 2.6065 2.7955 2.0520 -0.9420 -0.0067 -0.2635 82  ARG E CA  
10397 C C   . ARG E 85  B 2.6253 2.8202 2.0436 -0.9542 0.0202  -0.2641 82  ARG E C   
10398 O O   . ARG E 85  B 2.6649 2.8672 2.0668 -0.9643 0.0352  -0.2666 82  ARG E O   
10399 C CB  . ARG E 85  B 2.6395 2.8314 2.0876 -0.9443 -0.0124 -0.2655 82  ARG E CB  
10400 C CG  . ARG E 85  B 2.6243 2.8066 2.0975 -0.9322 -0.0407 -0.2642 82  ARG E CG  
10401 C CD  . ARG E 85  B 2.6721 2.8629 2.1512 -0.9349 -0.0446 -0.2738 82  ARG E CD  
10402 N NE  . ARG E 85  B 2.6852 2.8660 2.1372 -0.9453 -0.0364 -0.2604 82  ARG E NE  
10403 C CZ  . ARG E 85  B 2.6613 2.8179 2.1062 -0.9433 -0.0531 -0.2406 82  ARG E CZ  
10404 N NH1 . ARG E 85  B 2.6228 2.7629 2.0856 -0.9314 -0.0777 -0.2317 82  ARG E NH1 
10405 N NH2 . ARG E 85  B 2.6800 2.8284 2.1000 -0.9533 -0.0460 -0.2295 82  ARG E NH2 
10406 N N   . LEU E 86  C 2.7035 2.8936 2.1164 -0.9534 0.0257  -0.2621 82  LEU E N   
10407 C CA  . LEU E 86  C 2.7158 2.9050 2.1010 -0.9637 0.0483  -0.2600 82  LEU E CA  
10408 C C   . LEU E 86  C 2.7794 2.9953 2.1639 -0.9739 0.0694  -0.2807 82  LEU E C   
10409 O O   . LEU E 86  C 2.8087 3.0461 2.2181 -0.9718 0.0673  -0.2995 82  LEU E O   
10410 C CB  . LEU E 86  C 2.6798 2.8578 2.0616 -0.9603 0.0479  -0.2556 82  LEU E CB  
10411 C CG  . LEU E 86  C 2.6195 2.7694 1.9944 -0.9529 0.0325  -0.2333 82  LEU E CG  
10412 C CD1 . LEU E 86  C 2.5914 2.7335 1.9688 -0.9488 0.0298  -0.2330 82  LEU E CD1 
10413 C CD2 . LEU E 86  C 2.6147 2.7487 1.9595 -0.9592 0.0417  -0.2177 82  LEU E CD2 
10414 N N   . THR E 87  ? 2.7669 2.9810 2.1231 -0.9850 0.0890  -0.2775 83  THR E N   
10415 C CA  . THR E 87  ? 2.8281 3.0641 2.1783 -0.9963 0.1117  -0.2951 83  THR E CA  
10416 C C   . THR E 87  ? 2.8259 3.0491 2.1477 -1.0032 0.1272  -0.2885 83  THR E C   
10417 O O   . THR E 87  ? 2.7791 2.9778 2.0860 -0.9991 0.1205  -0.2709 83  THR E O   
10418 C CB  . THR E 87  ? 2.8819 3.1304 2.2249 -1.0050 0.1214  -0.3008 83  THR E CB  
10419 O OG1 . THR E 87  ? 2.8814 3.1114 2.1914 -1.0117 0.1288  -0.2850 83  THR E OG1 
10420 C CG2 . THR E 87  ? 2.8772 3.1290 2.2419 -0.9978 0.1031  -0.3016 83  THR E CG2 
10421 N N   . SER E 88  ? 2.9568 3.1965 2.2715 -1.0137 0.1476  -0.3036 84  SER E N   
10422 C CA  . SER E 88  ? 2.9660 3.1937 2.2541 -1.0208 0.1627  -0.3001 84  SER E CA  
10423 C C   . SER E 88  ? 2.9631 3.1694 2.2192 -1.0246 0.1668  -0.2834 84  SER E C   
10424 O O   . SER E 88  ? 2.9571 3.1456 2.1911 -1.0267 0.1731  -0.2759 84  SER E O   
10425 C CB  . SER E 88  ? 3.0359 3.2860 2.3244 -1.0321 0.1827  -0.3205 84  SER E CB  
10426 O OG  . SER E 88  ? 3.0933 3.3604 2.3800 -1.0399 0.1925  -0.3290 84  SER E OG  
10427 N N   . ASP E 89  ? 2.8917 3.0986 2.1450 -1.0256 0.1623  -0.2780 85  ASP E N   
10428 C CA  . ASP E 89  ? 2.8922 3.0784 2.1175 -1.0287 0.1624  -0.2619 85  ASP E CA  
10429 C C   . ASP E 89  ? 2.8247 2.9838 2.0466 -1.0186 0.1446  -0.2413 85  ASP E C   
10430 O O   . ASP E 89  ? 2.8218 2.9615 2.0212 -1.0204 0.1437  -0.2279 85  ASP E O   
10431 C CB  . ASP E 89  ? 2.9197 3.1130 2.1456 -1.0323 0.1590  -0.2612 85  ASP E CB  
10432 C CG  . ASP E 89  ? 2.9810 3.1570 2.1760 -1.0390 0.1623  -0.2486 85  ASP E CG  
10433 O OD1 . ASP E 89  ? 3.0771 3.2506 2.2495 -1.0475 0.1791  -0.2528 85  ASP E OD1 
10434 O OD2 . ASP E 89  ? 2.9903 3.1540 2.1845 -1.0358 0.1467  -0.2346 85  ASP E OD2 
10435 N N   . ASP E 90  ? 2.7981 2.9555 2.0427 -1.0081 0.1296  -0.2390 86  ASP E N   
10436 C CA  . ASP E 90  ? 2.7352 2.8683 1.9798 -0.9984 0.1120  -0.2202 86  ASP E CA  
10437 C C   . ASP E 90  ? 2.7143 2.8343 1.9467 -0.9977 0.1186  -0.2181 86  ASP E C   
10438 O O   . ASP E 90  ? 2.6648 2.7646 1.8965 -0.9902 0.1055  -0.2033 86  ASP E O   
10439 C CB  . ASP E 90  ? 2.6962 2.8324 1.9713 -0.9876 0.0911  -0.2186 86  ASP E CB  
10440 C CG  . ASP E 90  ? 2.7146 2.8584 2.0008 -0.9873 0.0815  -0.2184 86  ASP E CG  
10441 O OD1 . ASP E 90  ? 2.7235 2.8555 1.9940 -0.9906 0.0786  -0.2063 86  ASP E OD1 
10442 O OD2 . ASP E 90  ? 2.7238 2.8848 2.0347 -0.9841 0.0761  -0.2312 86  ASP E OD2 
10443 N N   . THR E 91  ? 2.7049 2.8355 1.9284 -1.0058 0.1380  -0.2328 87  THR E N   
10444 C CA  . THR E 91  ? 2.6955 2.8123 1.9041 -1.0070 0.1460  -0.2321 87  THR E CA  
10445 C C   . THR E 91  ? 2.6930 2.7862 1.8749 -1.0084 0.1480  -0.2189 87  THR E C   
10446 O O   . THR E 91  ? 2.7347 2.8284 1.9014 -1.0150 0.1553  -0.2188 87  THR E O   
10447 C CB  . THR E 91  ? 2.7508 2.8843 1.9559 -1.0169 0.1660  -0.2514 87  THR E CB  
10448 O OG1 . THR E 91  ? 2.7477 2.9013 1.9816 -1.0139 0.1607  -0.2638 87  THR E OG1 
10449 C CG2 . THR E 91  ? 2.7524 2.8688 1.9374 -1.0200 0.1759  -0.2508 87  THR E CG2 
10450 N N   . GLY E 92  ? 2.6078 2.6802 1.7848 -1.0025 0.1410  -0.2085 88  GLY E N   
10451 C CA  . GLY E 92  ? 2.6150 2.6645 1.7711 -1.0027 0.1412  -0.1975 88  GLY E CA  
10452 C C   . GLY E 92  ? 2.5591 2.5881 1.7203 -0.9933 0.1268  -0.1841 88  GLY E C   
10453 O O   . GLY E 92  ? 2.5205 2.5518 1.6977 -0.9875 0.1183  -0.1836 88  GLY E O   
10454 N N   . ILE E 93  ? 2.4895 2.4982 1.6384 -0.9921 0.1239  -0.1738 89  ILE E N   
10455 C CA  . ILE E 93  ? 2.4443 2.4326 1.5997 -0.9836 0.1099  -0.1603 89  ILE E CA  
10456 C C   . ILE E 93  ? 2.4050 2.3893 1.5790 -0.9764 0.0871  -0.1433 89  ILE E C   
10457 O O   . ILE E 93  ? 2.4368 2.4208 1.6073 -0.9793 0.0845  -0.1387 89  ILE E O   
10458 C CB  . ILE E 93  ? 2.4663 2.4345 1.6026 -0.9865 0.1199  -0.1611 89  ILE E CB  
10459 C CG1 . ILE E 93  ? 2.5321 2.5018 1.6501 -0.9939 0.1413  -0.1774 89  ILE E CG1 
10460 C CG2 . ILE E 93  ? 2.4355 2.3836 1.5836 -0.9778 0.1047  -0.1470 89  ILE E CG2 
10461 C CD1 . ILE E 93  ? 2.6234 2.5714 1.7222 -0.9970 0.1522  -0.1801 89  ILE E CD1 
10462 N N   . TYR E 94  ? 2.4914 2.4717 1.6855 -0.9676 0.0699  -0.1336 90  TYR E N   
10463 C CA  . TYR E 94  ? 2.4543 2.4302 1.6699 -0.9605 0.0461  -0.1167 90  TYR E CA  
10464 C C   . TYR E 94  ? 2.4305 2.3858 1.6555 -0.9543 0.0339  -0.1021 90  TYR E C   
10465 O O   . TYR E 94  ? 2.4169 2.3641 1.6437 -0.9508 0.0345  -0.1024 90  TYR E O   
10466 C CB  . TYR E 94  ? 2.4389 2.4258 1.6751 -0.9550 0.0339  -0.1167 90  TYR E CB  
10467 C CG  . TYR E 94  ? 2.4672 2.4756 1.7041 -0.9599 0.0415  -0.1296 90  TYR E CG  
10468 C CD1 . TYR E 94  ? 2.5087 2.5314 1.7341 -0.9669 0.0623  -0.1479 90  TYR E CD1 
10469 C CD2 . TYR E 94  ? 2.4689 2.4832 1.7195 -0.9583 0.0277  -0.1238 90  TYR E CD2 
10470 C CE1 . TYR E 94  ? 2.5351 2.5791 1.7656 -0.9716 0.0693  -0.1606 90  TYR E CE1 
10471 C CE2 . TYR E 94  ? 2.4993 2.5334 1.7520 -0.9631 0.0353  -0.1370 90  TYR E CE2 
10472 C CZ  . TYR E 94  ? 2.5329 2.5827 1.7767 -0.9696 0.0562  -0.1555 90  TYR E CZ  
10473 O OH  . TYR E 94  ? 2.5845 2.6557 1.8343 -0.9745 0.0636  -0.1694 90  TYR E OH  
10474 N N   . TYR E 95  ? 2.3229 2.2701 1.5564 -0.9534 0.0223  -0.0893 91  TYR E N   
10475 C CA  . TYR E 95  ? 2.2940 2.2239 1.5456 -0.9477 0.0092  -0.0743 91  TYR E CA  
10476 C C   . TYR E 95  ? 2.2695 2.1981 1.5513 -0.9407 -0.0175 -0.0558 91  TYR E C   
10477 O O   . TYR E 95  ? 2.2796 2.2163 1.5643 -0.9421 -0.0261 -0.0523 91  TYR E O   
10478 C CB  . TYR E 95  ? 2.3437 2.2643 1.5904 -0.9520 0.0148  -0.0724 91  TYR E CB  
10479 C CG  . TYR E 95  ? 2.3807 2.2984 1.5992 -0.9591 0.0400  -0.0896 91  TYR E CG  
10480 C CD1 . TYR E 95  ? 2.3724 2.2765 1.5884 -0.9578 0.0488  -0.0936 91  TYR E CD1 
10481 C CD2 . TYR E 95  ? 2.4465 2.3739 1.6415 -0.9678 0.0549  -0.1015 91  TYR E CD2 
10482 C CE1 . TYR E 95  ? 2.4270 2.3261 1.6167 -0.9648 0.0714  -0.1094 91  TYR E CE1 
10483 C CE2 . TYR E 95  ? 2.4894 2.4134 1.6597 -0.9747 0.0773  -0.1170 91  TYR E CE2 
10484 C CZ  . TYR E 95  ? 2.4916 2.4009 1.6590 -0.9731 0.0852  -0.1209 91  TYR E CZ  
10485 O OH  . TYR E 95  ? 2.5684 2.4724 1.7105 -0.9805 0.1073  -0.1366 91  TYR E OH  
10486 N N   . CYS E 96  ? 2.1636 2.0815 1.4683 -0.9338 -0.0302 -0.0442 92  CYS E N   
10487 C CA  . CYS E 96  ? 2.1415 2.0545 1.4794 -0.9280 -0.0554 -0.0237 92  CYS E CA  
10488 C C   . CYS E 96  ? 2.1540 2.0559 1.5089 -0.9283 -0.0575 -0.0133 92  CYS E C   
10489 O O   . CYS E 96  ? 2.1660 2.0597 1.5158 -0.9295 -0.0430 -0.0197 92  CYS E O   
10490 C CB  . CYS E 96  ? 2.1053 2.0145 1.4648 -0.9203 -0.0694 -0.0156 92  CYS E CB  
10491 S SG  . CYS E 96  ? 2.0954 1.9924 1.4565 -0.9181 -0.0589 -0.0186 92  CYS E SG  
10492 N N   . ALA E 97  ? 2.1336 2.0345 1.5114 -0.9274 -0.0756 0.0028  93  ALA E N   
10493 C CA  . ALA E 97  ? 2.1492 2.0412 1.5510 -0.9278 -0.0786 0.0142  93  ALA E CA  
10494 C C   . ALA E 97  ? 2.1343 2.0243 1.5779 -0.9230 -0.1053 0.0378  93  ALA E C   
10495 O O   . ALA E 97  ? 2.1429 2.0378 1.5839 -0.9240 -0.1198 0.0438  93  ALA E O   
10496 C CB  . ALA E 97  ? 2.2000 2.0936 1.5786 -0.9359 -0.0667 0.0064  93  ALA E CB  
10497 N N   . ARG E 98  ? 2.2653 2.1477 1.7489 -0.9183 -0.1109 0.0512  94  ARG E N   
10498 C CA  . ARG E 98  ? 2.2542 2.1354 1.7837 -0.9140 -0.1352 0.0751  94  ARG E CA  
10499 C C   . ARG E 98  ? 2.2934 2.1737 1.8349 -0.9183 -0.1417 0.0856  94  ARG E C   
10500 O O   . ARG E 98  ? 2.3227 2.1996 1.8600 -0.9222 -0.1262 0.0798  94  ARG E O   
10501 C CB  . ARG E 98  ? 2.2280 2.1029 1.8017 -0.9083 -0.1352 0.0864  94  ARG E CB  
10502 C CG  . ARG E 98  ? 2.2179 2.0929 1.8435 -0.9038 -0.1589 0.1119  94  ARG E CG  
10503 C CD  . ARG E 98  ? 2.2004 2.0702 1.8745 -0.8990 -0.1531 0.1231  94  ARG E CD  
10504 N NE  . ARG E 98  ? 2.2299 2.0953 1.9309 -0.9009 -0.1394 0.1281  94  ARG E NE  
10505 C CZ  . ARG E 98  ? 2.2268 2.0866 1.9752 -0.8975 -0.1278 0.1383  94  ARG E CZ  
10506 N NH1 . ARG E 98  ? 2.1965 2.0545 1.9678 -0.8926 -0.1282 0.1441  94  ARG E NH1 
10507 N NH2 . ARG E 98  ? 2.2600 2.1151 2.0343 -0.8990 -0.1137 0.1432  94  ARG E NH2 
10508 N N   . ASP E 99  ? 2.1722 2.0544 1.7293 -0.9179 -0.1653 0.1017  95  ASP E N   
10509 C CA  . ASP E 99  ? 2.2096 2.0897 1.7854 -0.9217 -0.1756 0.1162  95  ASP E CA  
10510 C C   . ASP E 99  ? 2.1999 2.0768 1.8377 -0.9166 -0.1880 0.1395  95  ASP E C   
10511 O O   . ASP E 99  ? 2.1671 2.0446 1.8314 -0.9107 -0.2004 0.1499  95  ASP E O   
10512 C CB  . ASP E 99  ? 2.2295 2.1118 1.7856 -0.9255 -0.1940 0.1212  95  ASP E CB  
10513 C CG  . ASP E 99  ? 2.2817 2.1619 1.8311 -0.9330 -0.1963 0.1263  95  ASP E CG  
10514 O OD1 . ASP E 99  ? 2.2958 2.1725 1.8855 -0.9324 -0.2083 0.1457  95  ASP E OD1 
10515 O OD2 . ASP E 99  ? 2.3120 2.1946 1.8176 -0.9399 -0.1855 0.1116  95  ASP E OD2 
10516 N N   . LYS E 100 ? 2.1392 2.0132 1.8027 -0.9191 -0.1834 0.1482  96  LYS E N   
10517 C CA  . LYS E 100 ? 2.1408 2.0135 1.8687 -0.9151 -0.1947 0.1731  96  LYS E CA  
10518 C C   . LYS E 100 ? 2.1372 2.0120 1.8810 -0.9138 -0.2258 0.1927  96  LYS E C   
10519 O O   . LYS E 100 ? 2.1203 1.9959 1.9109 -0.9085 -0.2373 0.2107  96  LYS E O   
10520 C CB  . LYS E 100 ? 2.1875 2.0569 1.9371 -0.9191 -0.1858 0.1797  96  LYS E CB  
10521 C CG  . LYS E 100 ? 2.1964 2.0610 1.9361 -0.9198 -0.1548 0.1621  96  LYS E CG  
10522 C CD  . LYS E 100 ? 2.2505 2.1106 2.0052 -0.9244 -0.1455 0.1668  96  LYS E CD  
10523 C CE  . LYS E 100 ? 2.2627 2.1217 2.0914 -0.9203 -0.1503 0.1936  96  LYS E CE  
10524 N NZ  . LYS E 100 ? 2.2394 2.0939 2.1094 -0.9135 -0.1285 0.1952  96  LYS E NZ  
10525 N N   . TYR E 101 ? 2.2632 2.1380 1.9686 -0.9192 -0.2389 0.1899  97  TYR E N   
10526 C CA  . TYR E 101 ? 2.2630 2.1369 1.9712 -0.9188 -0.2679 0.2049  97  TYR E CA  
10527 C C   . TYR E 101 ? 2.2831 2.1557 2.0449 -0.9178 -0.2899 0.2341  97  TYR E C   
10528 O O   . TYR E 101 ? 2.2734 2.1450 2.0542 -0.9148 -0.3137 0.2503  97  TYR E O   
10529 C CB  . TYR E 101 ? 2.2178 2.0931 1.9203 -0.9128 -0.2720 0.1996  97  TYR E CB  
10530 C CG  . TYR E 101 ? 2.2239 2.0966 1.9022 -0.9142 -0.2933 0.2023  97  TYR E CG  
10531 C CD1 . TYR E 101 ? 2.2509 2.1227 1.8811 -0.9209 -0.2891 0.1888  97  TYR E CD1 
10532 C CD2 . TYR E 101 ? 2.2071 2.0774 1.9118 -0.9092 -0.3163 0.2184  97  TYR E CD2 
10533 C CE1 . TYR E 101 ? 2.2608 2.1287 1.8718 -0.9224 -0.3062 0.1906  97  TYR E CE1 
10534 C CE2 . TYR E 101 ? 2.2180 2.0834 1.9019 -0.9105 -0.3352 0.2205  97  TYR E CE2 
10535 C CZ  . TYR E 101 ? 2.2446 2.1084 1.8825 -0.9171 -0.3294 0.2062  97  TYR E CZ  
10536 O OH  . TYR E 101 ? 2.2600 2.1177 1.8806 -0.9187 -0.3463 0.2076  97  TYR E OH  
10537 N N   . TYR E 102 ? 2.2929 2.1652 2.0818 -0.9202 -0.2823 0.2421  98  TYR E N   
10538 C CA  . TYR E 102 ? 2.3357 2.2075 2.1738 -0.9203 -0.3036 0.2708  98  TYR E CA  
10539 C C   . TYR E 102 ? 2.3528 2.2201 2.1673 -0.9252 -0.3340 0.2821  98  TYR E C   
10540 O O   . TYR E 102 ? 2.3797 2.2434 2.1432 -0.9318 -0.3325 0.2687  98  TYR E O   
10541 C CB  . TYR E 102 ? 2.3629 2.2341 2.2260 -0.9236 -0.2898 0.2759  98  TYR E CB  
10542 C CG  . TYR E 102 ? 2.3624 2.2348 2.2584 -0.9188 -0.2593 0.2690  98  TYR E CG  
10543 C CD1 . TYR E 102 ? 2.3327 2.2074 2.2498 -0.9115 -0.2508 0.2669  98  TYR E CD1 
10544 C CD2 . TYR E 102 ? 2.4126 2.2821 2.3198 -0.9217 -0.2387 0.2657  98  TYR E CD2 
10545 C CE1 . TYR E 102 ? 2.3404 2.2135 2.2868 -0.9076 -0.2212 0.2612  98  TYR E CE1 
10546 C CE2 . TYR E 102 ? 2.4044 2.2719 2.3426 -0.9173 -0.2090 0.2602  98  TYR E CE2 
10547 C CZ  . TYR E 102 ? 2.3795 2.2484 2.3367 -0.9103 -0.1999 0.2580  98  TYR E CZ  
10548 O OH  . TYR E 102 ? 2.4037 2.2680 2.3904 -0.9062 -0.1690 0.2532  98  TYR E OH  
10549 N N   . GLY E 103 ? 2.3003 2.1669 2.1528 -0.9225 -0.3610 0.3076  99  GLY E N   
10550 C CA  . GLY E 103 ? 2.3311 2.1904 2.1634 -0.9271 -0.3917 0.3204  99  GLY E CA  
10551 C C   . GLY E 103 ? 2.3102 2.1648 2.0931 -0.9274 -0.3950 0.3042  99  GLY E C   
10552 O O   . GLY E 103 ? 2.3564 2.2025 2.1100 -0.9330 -0.4134 0.3083  99  GLY E O   
10553 N N   . ASN E 104 ? 2.1712 2.0305 1.9454 -0.9218 -0.3768 0.2863  100 ASN E N   
10554 C CA  . ASN E 104 ? 2.1504 2.0068 1.8812 -0.9213 -0.3756 0.2691  100 ASN E CA  
10555 C C   . ASN E 104 ? 2.1791 2.0328 1.8549 -0.9296 -0.3648 0.2510  100 ASN E C   
10556 O O   . ASN E 104 ? 2.1880 2.0360 1.8324 -0.9324 -0.3736 0.2457  100 ASN E O   
10557 C CB  . ASN E 104 ? 2.1538 2.0029 1.8965 -0.9189 -0.4066 0.2864  100 ASN E CB  
10558 C CG  . ASN E 104 ? 2.1297 1.9823 1.9265 -0.9110 -0.4173 0.3049  100 ASN E CG  
10559 O OD1 . ASN E 104 ? 2.0884 1.9471 1.8956 -0.9053 -0.4004 0.2947  100 ASN E OD1 
10560 N ND2 . ASN E 104 ? 2.1594 2.0079 1.9909 -0.9112 -0.4459 0.3331  100 ASN E ND2 
10561 N N   . GLU E 105 A 2.2710 2.1286 1.9366 -0.9337 -0.3438 0.2409  100 GLU E N   
10562 C CA  . GLU E 105 A 2.3044 2.1613 1.9181 -0.9418 -0.3289 0.2222  100 GLU E CA  
10563 C C   . GLU E 105 A 2.2891 2.1530 1.8911 -0.9416 -0.2969 0.2020  100 GLU E C   
10564 O O   . GLU E 105 A 2.2667 2.1336 1.9038 -0.9365 -0.2880 0.2055  100 GLU E O   
10565 C CB  . GLU E 105 A 2.3939 2.2438 2.0017 -0.9507 -0.3440 0.2362  100 GLU E CB  
10566 C CG  . GLU E 105 A 2.4402 2.2914 2.0876 -0.9510 -0.3443 0.2511  100 GLU E CG  
10567 C CD  . GLU E 105 A 2.5276 2.3712 2.1674 -0.9603 -0.3606 0.2655  100 GLU E CD  
10568 O OE1 . GLU E 105 A 2.5930 2.4376 2.2637 -0.9616 -0.3599 0.2771  100 GLU E OE1 
10569 O OE2 . GLU E 105 A 2.5391 2.3750 2.1431 -0.9667 -0.3732 0.2652  100 GLU E OE2 
10570 N N   . ALA E 106 B 2.3285 2.1942 1.8814 -0.9477 -0.2790 0.1811  100 ALA E N   
10571 C CA  . ALA E 106 B 2.3263 2.1973 1.8615 -0.9487 -0.2491 0.1611  100 ALA E CA  
10572 C C   . ALA E 106 B 2.3609 2.2295 1.9183 -0.9519 -0.2447 0.1695  100 ALA E C   
10573 O O   . ALA E 106 B 2.4070 2.2709 1.9628 -0.9586 -0.2571 0.1811  100 ALA E O   
10574 C CB  . ALA E 106 B 2.3477 2.2222 1.8272 -0.9557 -0.2320 0.1390  100 ALA E CB  
10575 N N   . VAL E 107 C 2.3512 2.2216 1.9309 -0.9472 -0.2270 0.1640  100 VAL E N   
10576 C CA  . VAL E 107 C 2.3829 2.2504 1.9915 -0.9491 -0.2193 0.1712  100 VAL E CA  
10577 C C   . VAL E 107 C 2.3887 2.2568 1.9717 -0.9507 -0.1883 0.1479  100 VAL E C   
10578 O O   . VAL E 107 C 2.4369 2.3021 2.0050 -0.9575 -0.1775 0.1425  100 VAL E O   
10579 C CB  . VAL E 107 C 2.3621 2.2292 2.0379 -0.9415 -0.2288 0.1928  100 VAL E CB  
10580 C CG1 . VAL E 107 C 2.3982 2.2622 2.1077 -0.9429 -0.2156 0.1989  100 VAL E CG1 
10581 C CG2 . VAL E 107 C 2.3682 2.2342 2.0674 -0.9411 -0.2613 0.2173  100 VAL E CG2 
10582 N N   . GLY E 108 D 2.4113 2.2820 1.9884 -0.9450 -0.1746 0.1344  100 GLY E N   
10583 C CA  . GLY E 108 D 2.4171 2.2872 1.9657 -0.9468 -0.1462 0.1116  100 GLY E CA  
10584 C C   . GLY E 108 D 2.3648 2.2368 1.9115 -0.9400 -0.1366 0.1011  100 GLY E C   
10585 O O   . GLY E 108 D 2.3243 2.1968 1.9056 -0.9330 -0.1495 0.1140  100 GLY E O   
10586 N N   . MET E 109 E 2.2547 2.1274 1.7596 -0.9428 -0.1137 0.0776  100 MET E N   
10587 C CA  . MET E 109 E 2.2089 2.0833 1.7008 -0.9381 -0.1032 0.0646  100 MET E CA  
10588 C C   . MET E 109 E 2.2143 2.0802 1.7288 -0.9355 -0.0857 0.0616  100 MET E C   
10589 O O   . MET E 109 E 2.2445 2.1061 1.7338 -0.9402 -0.0648 0.0459  100 MET E O   
10590 C CB  . MET E 109 E 2.2264 2.1075 1.6606 -0.9432 -0.0887 0.0418  100 MET E CB  
10591 C CG  . MET E 109 E 2.2421 2.1307 1.6565 -0.9467 -0.1023 0.0445  100 MET E CG  
10592 S SD  . MET E 109 E 2.2670 2.1663 1.6242 -0.9527 -0.0818 0.0188  100 MET E SD  
10593 C CE  . MET E 109 E 2.2867 2.1908 1.6344 -0.9579 -0.0987 0.0275  100 MET E CE  
10594 N N   . ASP E 110 ? 2.3143 2.1771 1.8773 -0.9283 -0.0932 0.0770  101 ASP E N   
10595 C CA  . ASP E 110 ? 2.3218 2.1751 1.9189 -0.9255 -0.0767 0.0794  101 ASP E CA  
10596 C C   . ASP E 110 ? 2.3130 2.1614 1.8934 -0.9229 -0.0602 0.0647  101 ASP E C   
10597 O O   . ASP E 110 ? 2.3426 2.1805 1.9349 -0.9228 -0.0406 0.0605  101 ASP E O   
10598 C CB  . ASP E 110 ? 2.3170 2.1693 1.9847 -0.9196 -0.0900 0.1069  101 ASP E CB  
10599 C CG  . ASP E 110 ? 2.2840 2.1412 1.9697 -0.9135 -0.1065 0.1166  101 ASP E CG  
10600 O OD1 . ASP E 110 ? 2.2555 2.1176 1.8992 -0.9140 -0.1128 0.1047  101 ASP E OD1 
10601 O OD2 . ASP E 110 ? 2.2912 2.1470 2.0351 -0.9082 -0.1117 0.1367  101 ASP E OD2 
10602 N N   . VAL E 111 ? 2.2332 2.0875 1.7867 -0.9211 -0.0669 0.0572  102 VAL E N   
10603 C CA  . VAL E 111 ? 2.2093 2.0589 1.7418 -0.9196 -0.0524 0.0428  102 VAL E CA  
10604 C C   . VAL E 111 ? 2.2046 2.0623 1.6790 -0.9233 -0.0492 0.0234  102 VAL E C   
10605 O O   . VAL E 111 ? 2.1894 2.0567 1.6578 -0.9220 -0.0657 0.0281  102 VAL E O   
10606 C CB  . VAL E 111 ? 2.1653 2.0131 1.7388 -0.9123 -0.0627 0.0576  102 VAL E CB  
10607 C CG1 . VAL E 111 ? 2.1441 1.9870 1.6875 -0.9119 -0.0498 0.0419  102 VAL E CG1 
10608 C CG2 . VAL E 111 ? 2.1745 2.0148 1.8116 -0.9087 -0.0590 0.0770  102 VAL E CG2 
10609 N N   . TRP E 112 ? 2.2833 2.1368 1.7177 -0.9278 -0.0269 0.0025  103 TRP E N   
10610 C CA  . TRP E 112 ? 2.2853 2.1479 1.6695 -0.9318 -0.0192 -0.0158 103 TRP E CA  
10611 C C   . TRP E 112 ? 2.2601 2.1186 1.6265 -0.9304 -0.0088 -0.0269 103 TRP E C   
10612 O O   . TRP E 112 ? 2.2626 2.1079 1.6350 -0.9302 0.0035  -0.0301 103 TRP E O   
10613 C CB  . TRP E 112 ? 2.3382 2.2015 1.6870 -0.9400 -0.0010 -0.0317 103 TRP E CB  
10614 C CG  . TRP E 112 ? 2.3681 2.2365 1.7244 -0.9430 -0.0108 -0.0230 103 TRP E CG  
10615 C CD1 . TRP E 112 ? 2.3806 2.2431 1.7760 -0.9415 -0.0214 -0.0058 103 TRP E CD1 
10616 C CD2 . TRP E 112 ? 2.3951 2.2753 1.7203 -0.9488 -0.0095 -0.0307 103 TRP E CD2 
10617 N NE1 . TRP E 112 ? 2.4135 2.2822 1.8000 -0.9463 -0.0287 -0.0023 103 TRP E NE1 
10618 C CE2 . TRP E 112 ? 2.4234 2.3026 1.7660 -0.9510 -0.0211 -0.0178 103 TRP E CE2 
10619 C CE3 . TRP E 112 ? 2.4011 2.2931 1.6892 -0.9528 0.0011  -0.0464 103 TRP E CE3 
10620 C CZ2 . TRP E 112 ? 2.4579 2.3459 1.7771 -0.9574 -0.0224 -0.0209 103 TRP E CZ2 
10621 C CZ3 . TRP E 112 ? 2.4348 2.3371 1.7048 -0.9587 0.0012  -0.0494 103 TRP E CZ3 
10622 C CH2 . TRP E 112 ? 2.4631 2.3625 1.7461 -0.9612 -0.0105 -0.0370 103 TRP E CH2 
10623 N N   . GLY E 113 ? 2.1916 2.0608 1.5381 -0.9297 -0.0133 -0.0323 104 GLY E N   
10624 C CA  . GLY E 113 ? 2.1771 2.0445 1.4989 -0.9304 -0.0014 -0.0454 104 GLY E CA  
10625 C C   . GLY E 113 ? 2.2179 2.0833 1.5001 -0.9382 0.0240  -0.0660 104 GLY E C   
10626 O O   . GLY E 113 ? 2.2577 2.1247 1.5287 -0.9433 0.0325  -0.0713 104 GLY E O   
10627 N N   . GLN E 114 ? 2.2651 2.1263 1.5254 -0.9398 0.0362  -0.0775 105 GLN E N   
10628 C CA  . GLN E 114 ? 2.3069 2.1648 1.5304 -0.9478 0.0606  -0.0967 105 GLN E CA  
10629 C C   . GLN E 114 ? 2.3303 2.2073 1.5298 -0.9533 0.0685  -0.1082 105 GLN E C   
10630 O O   . GLN E 114 ? 2.3750 2.2523 1.5471 -0.9609 0.0885  -0.1234 105 GLN E O   
10631 C CB  . GLN E 114 ? 2.2958 2.1413 1.5043 -0.9486 0.0709  -0.1043 105 GLN E CB  
10632 C CG  . GLN E 114 ? 2.2768 2.1352 1.4716 -0.9491 0.0697  -0.1096 105 GLN E CG  
10633 C CD  . GLN E 114 ? 2.2273 2.0900 1.4504 -0.9409 0.0466  -0.0945 105 GLN E CD  
10634 O OE1 . GLN E 114 ? 2.2072 2.0683 1.4608 -0.9352 0.0299  -0.0792 105 GLN E OE1 
10635 N NE2 . GLN E 114 ? 2.2119 2.0806 1.4279 -0.9406 0.0450  -0.0984 105 GLN E NE2 
10636 N N   . GLY E 115 ? 2.1787 2.0712 1.3909 -0.9499 0.0540  -0.1014 106 GLY E N   
10637 C CA  . GLY E 115 ? 2.1786 2.0905 1.3764 -0.9548 0.0615  -0.1118 106 GLY E CA  
10638 C C   . GLY E 115 ? 2.1773 2.0976 1.3688 -0.9553 0.0663  -0.1205 106 GLY E C   
10639 O O   . GLY E 115 ? 2.1834 2.0930 1.3663 -0.9556 0.0726  -0.1243 106 GLY E O   
10640 N N   . THR E 116 ? 2.3005 2.2400 1.4988 -0.9556 0.0627  -0.1237 107 THR E N   
10641 C CA  . THR E 116 ? 2.2943 2.2452 1.4933 -0.9564 0.0664  -0.1333 107 THR E CA  
10642 C C   . THR E 116 ? 2.3393 2.3103 1.5294 -0.9643 0.0819  -0.1486 107 THR E C   
10643 O O   . THR E 116 ? 2.3520 2.3355 1.5502 -0.9646 0.0776  -0.1476 107 THR E O   
10644 C CB  . THR E 116 ? 2.2549 2.2106 1.4804 -0.9480 0.0447  -0.1240 107 THR E CB  
10645 O OG1 . THR E 116 ? 2.2163 2.1538 1.4518 -0.9413 0.0307  -0.1097 107 THR E OG1 
10646 C CG2 . THR E 116 ? 2.2556 2.2234 1.4851 -0.9490 0.0481  -0.1357 107 THR E CG2 
10647 N N   . SER E 117 ? 2.4823 2.4562 1.6572 -0.9711 0.0996  -0.1626 108 SER E N   
10648 C CA  . SER E 117 ? 2.5287 2.5236 1.7000 -0.9791 0.1142  -0.1781 108 SER E CA  
10649 C C   . SER E 117 ? 2.5195 2.5347 1.7158 -0.9760 0.1048  -0.1833 108 SER E C   
10650 O O   . SER E 117 ? 2.4912 2.5043 1.6983 -0.9720 0.0969  -0.1835 108 SER E O   
10651 C CB  . SER E 117 ? 2.5654 2.5557 1.7155 -0.9878 0.1344  -0.1908 108 SER E CB  
10652 O OG  . SER E 117 ? 2.6157 2.6273 1.7658 -0.9962 0.1479  -0.2060 108 SER E OG  
10653 N N   . VAL E 118 ? 2.5751 2.6090 1.7812 -0.9778 0.1049  -0.1881 109 VAL E N   
10654 C CA  . VAL E 118 ? 2.5779 2.6332 1.8096 -0.9754 0.0974  -0.1968 109 VAL E CA  
10655 C C   . VAL E 118 ? 2.6372 2.7145 1.8662 -0.9851 0.1155  -0.2150 109 VAL E C   
10656 O O   . VAL E 118 ? 2.6728 2.7541 1.8890 -0.9911 0.1255  -0.2163 109 VAL E O   
10657 C CB  . VAL E 118 ? 2.5546 2.6122 1.8047 -0.9680 0.0787  -0.1865 109 VAL E CB  
10658 C CG1 . VAL E 118 ? 2.5784 2.6584 1.8552 -0.9657 0.0720  -0.1986 109 VAL E CG1 
10659 C CG2 . VAL E 118 ? 2.4996 2.5363 1.7561 -0.9586 0.0595  -0.1687 109 VAL E CG2 
10660 N N   . THR E 119 ? 2.7056 2.7969 1.9478 -0.9870 0.1185  -0.2292 110 THR E N   
10661 C CA  . THR E 119 ? 2.7699 2.8848 2.0161 -0.9960 0.1334  -0.2479 110 THR E CA  
10662 C C   . THR E 119 ? 2.7733 2.9117 2.0524 -0.9914 0.1221  -0.2585 110 THR E C   
10663 O O   . THR E 119 ? 2.7514 2.8906 2.0506 -0.9845 0.1079  -0.2606 110 THR E O   
10664 C CB  . THR E 119 ? 2.7956 2.9085 2.0319 -1.0032 0.1460  -0.2581 110 THR E CB  
10665 O OG1 . THR E 119 ? 2.8113 2.9012 2.0163 -1.0073 0.1569  -0.2497 110 THR E OG1 
10666 C CG2 . THR E 119 ? 2.8733 3.0111 2.1163 -1.0129 0.1601  -0.2776 110 THR E CG2 
10667 N N   . VAL E 120 ? 2.6241 2.7807 1.9083 -0.9954 0.1280  -0.2659 111 VAL E N   
10668 C CA  . VAL E 120 ? 2.6450 2.8256 1.9598 -0.9921 0.1195  -0.2789 111 VAL E CA  
10669 C C   . VAL E 120 ? 2.7154 2.9204 2.0353 -1.0020 0.1359  -0.3000 111 VAL E C   
10670 O O   . VAL E 120 ? 2.7709 2.9817 2.0735 -1.0118 0.1533  -0.3037 111 VAL E O   
10671 C CB  . VAL E 120 ? 2.6384 2.8213 1.9573 -0.9892 0.1122  -0.2721 111 VAL E CB  
10672 C CG1 . VAL E 120 ? 2.6708 2.8777 2.0217 -0.9854 0.1034  -0.2875 111 VAL E CG1 
10673 C CG2 . VAL E 120 ? 2.5774 2.7356 1.8929 -0.9798 0.0944  -0.2509 111 VAL E CG2 
10674 N N   . SER E 121 ? 2.6298 3.0687 2.5416 -0.6605 -0.0715 -0.9022 112 SER E N   
10675 C CA  . SER E 121 ? 2.7245 3.1413 2.5810 -0.6823 -0.0790 -0.8790 112 SER E CA  
10676 C C   . SER E 121 ? 2.6965 3.1551 2.5805 -0.6880 -0.0495 -0.8782 112 SER E C   
10677 O O   . SER E 121 ? 2.6216 3.1021 2.5567 -0.6748 -0.0250 -0.8924 112 SER E O   
10678 C CB  . SER E 121 ? 2.7902 3.1137 2.5842 -0.6878 -0.0947 -0.8617 112 SER E CB  
10679 O OG  . SER E 121 ? 2.8797 3.1872 2.6246 -0.7088 -0.0991 -0.8399 112 SER E OG  
10680 N N   . SER E 122 ? 2.6628 3.1334 2.5135 -0.7076 -0.0514 -0.8615 113 SER E N   
10681 C CA  . SER E 122 ? 2.6304 3.1281 2.4983 -0.7138 -0.0242 -0.8583 113 SER E CA  
10682 C C   . SER E 122 ? 2.6560 3.0825 2.4801 -0.7225 -0.0217 -0.8404 113 SER E C   
10683 O O   . SER E 122 ? 2.6338 3.0714 2.4659 -0.7280 0.0003  -0.8357 113 SER E O   
10684 C CB  . SER E 122 ? 2.6236 3.1776 2.4838 -0.7300 -0.0223 -0.8507 113 SER E CB  
10685 O OG  . SER E 122 ? 2.5914 3.2201 2.5009 -0.7201 -0.0181 -0.8696 113 SER E OG  
10686 N N   . ALA E 123 ? 3.0562 3.4104 2.8335 -0.7232 -0.0439 -0.8307 114 ALA E N   
10687 C CA  . ALA E 123 ? 3.0911 3.3742 2.8286 -0.7283 -0.0415 -0.8157 114 ALA E CA  
10688 C C   . ALA E 123 ? 2.9875 3.2668 2.7699 -0.7121 -0.0170 -0.8286 114 ALA E C   
10689 O O   . ALA E 123 ? 2.9388 3.2469 2.7723 -0.6943 -0.0104 -0.8488 114 ALA E O   
10690 C CB  . ALA E 123 ? 3.1448 3.3538 2.8290 -0.7282 -0.0697 -0.8065 114 ALA E CB  
10691 N N   . SER E 124 ? 3.0292 3.2728 2.7923 -0.7182 -0.0032 -0.8166 115 SER E N   
10692 C CA  . SER E 124 ? 2.9577 3.1873 2.7540 -0.7048 0.0199  -0.8248 115 SER E CA  
10693 C C   . SER E 124 ? 3.0008 3.1430 2.7456 -0.7071 0.0123  -0.8095 115 SER E C   
10694 O O   . SER E 124 ? 3.0893 3.1951 2.7772 -0.7231 -0.0012 -0.7904 115 SER E O   
10695 C CB  . SER E 124 ? 2.9208 3.2072 2.7570 -0.7073 0.0498  -0.8286 115 SER E CB  
10696 O OG  . SER E 124 ? 2.9945 3.2965 2.7978 -0.7279 0.0499  -0.8122 115 SER E OG  
10697 N N   . THR E 125 ? 3.2268 3.3377 2.9934 -0.6904 0.0225  -0.8184 116 THR E N   
10698 C CA  . THR E 125 ? 3.2496 3.2758 2.9735 -0.6866 0.0131  -0.8088 116 THR E CA  
10699 C C   . THR E 125 ? 3.3306 3.3121 2.9993 -0.7035 0.0138  -0.7859 116 THR E C   
10700 O O   . THR E 125 ? 3.3445 3.3477 3.0220 -0.7116 0.0346  -0.7798 116 THR E O   
10701 C CB  . THR E 125 ? 3.1921 3.2078 2.9594 -0.6670 0.0333  -0.8221 116 THR E CB  
10702 O OG1 . THR E 125 ? 3.1517 3.1974 2.9642 -0.6505 0.0304  -0.8427 116 THR E OG1 
10703 C CG2 . THR E 125 ? 3.2220 3.1523 2.9474 -0.6624 0.0280  -0.8119 116 THR E CG2 
10704 N N   . LYS E 126 ? 3.2064 3.1263 2.8181 -0.7085 -0.0094 -0.7736 117 LYS E N   
10705 C CA  . LYS E 126 ? 3.3020 3.1729 2.8535 -0.7250 -0.0135 -0.7511 117 LYS E CA  
10706 C C   . LYS E 126 ? 3.3362 3.1287 2.8469 -0.7172 -0.0307 -0.7468 117 LYS E C   
10707 O O   . LYS E 126 ? 3.3379 3.1188 2.8437 -0.7088 -0.0520 -0.7549 117 LYS E O   
10708 C CB  . LYS E 126 ? 3.3980 3.2950 2.9165 -0.7465 -0.0270 -0.7380 117 LYS E CB  
10709 C CG  . LYS E 126 ? 3.5293 3.3797 2.9846 -0.7660 -0.0301 -0.7134 117 LYS E CG  
10710 C CD  . LYS E 126 ? 3.5526 3.4008 3.0085 -0.7732 -0.0045 -0.7036 117 LYS E CD  
10711 C CE  . LYS E 126 ? 3.6550 3.4600 3.0462 -0.7945 -0.0076 -0.6780 117 LYS E CE  
10712 N NZ  . LYS E 126 ? 3.7021 3.4294 3.0516 -0.7891 -0.0198 -0.6713 117 LYS E NZ  
10713 N N   . GLY E 127 ? 3.2810 3.0206 2.7627 -0.7195 -0.0209 -0.7343 118 GLY E N   
10714 C CA  . GLY E 127 ? 3.3260 2.9908 2.7633 -0.7147 -0.0350 -0.7275 118 GLY E CA  
10715 C C   . GLY E 127 ? 3.4250 3.0668 2.8030 -0.7336 -0.0543 -0.7100 118 GLY E C   
10716 O O   . GLY E 127 ? 3.4788 3.1501 2.8389 -0.7545 -0.0515 -0.6964 118 GLY E O   
10717 N N   . PRO E 128 ? 3.1534 2.7420 2.4996 -0.7267 -0.0732 -0.7097 119 PRO E N   
10718 C CA  . PRO E 128 ? 3.2559 2.8218 2.5453 -0.7444 -0.0914 -0.6933 119 PRO E CA  
10719 C C   . PRO E 128 ? 3.3302 2.8592 2.5691 -0.7644 -0.0805 -0.6683 119 PRO E C   
10720 O O   . PRO E 128 ? 3.3207 2.8175 2.5580 -0.7600 -0.0633 -0.6640 119 PRO E O   
10721 C CB  . PRO E 128 ? 3.2911 2.8078 2.5664 -0.7278 -0.1108 -0.7024 119 PRO E CB  
10722 C CG  . PRO E 128 ? 3.2297 2.7178 2.5342 -0.7062 -0.0969 -0.7141 119 PRO E CG  
10723 C CD  . PRO E 128 ? 3.1226 2.6696 2.4832 -0.7022 -0.0781 -0.7244 119 PRO E CD  
10724 N N   . SER E 129 ? 3.2581 2.7922 2.4540 -0.7871 -0.0907 -0.6507 120 SER E N   
10725 C CA  . SER E 129 ? 3.3494 2.8356 2.4833 -0.8075 -0.0869 -0.6243 120 SER E CA  
10726 C C   . SER E 129 ? 3.4195 2.8433 2.5108 -0.8034 -0.1046 -0.6202 120 SER E C   
10727 O O   . SER E 129 ? 3.4699 2.9036 2.5573 -0.8013 -0.1253 -0.6267 120 SER E O   
10728 C CB  . SER E 129 ? 3.4396 2.9610 2.5464 -0.8353 -0.0882 -0.6055 120 SER E CB  
10729 O OG  . SER E 129 ? 3.4357 3.0163 2.5828 -0.8385 -0.0709 -0.6101 120 SER E OG  
10730 N N   . VAL E 130 ? 3.4360 2.7963 2.4948 -0.8022 -0.0962 -0.6092 121 VAL E N   
10731 C CA  . VAL E 130 ? 3.5001 2.7968 2.5194 -0.7967 -0.1098 -0.6055 121 VAL E CA  
10732 C C   . VAL E 130 ? 3.6232 2.8742 2.5687 -0.8229 -0.1106 -0.5739 121 VAL E C   
10733 O O   . VAL E 130 ? 3.6410 2.8688 2.5644 -0.8330 -0.0937 -0.5575 121 VAL E O   
10734 C CB  . VAL E 130 ? 3.4430 2.6970 2.4822 -0.7721 -0.1002 -0.6182 121 VAL E CB  
10735 C CG1 . VAL E 130 ? 3.5147 2.7049 2.5136 -0.7661 -0.1141 -0.6150 121 VAL E CG1 
10736 C CG2 . VAL E 130 ? 3.3532 2.6514 2.4646 -0.7474 -0.0982 -0.6472 121 VAL E CG2 
10737 N N   . PHE E 131 ? 3.6284 2.8656 2.5344 -0.8339 -0.1307 -0.5648 122 PHE E N   
10738 C CA  . PHE E 131 ? 3.7571 2.9526 2.5906 -0.8605 -0.1347 -0.5333 122 PHE E CA  
10739 C C   . PHE E 131 ? 3.8341 2.9618 2.6232 -0.8555 -0.1487 -0.5278 122 PHE E C   
10740 O O   . PHE E 131 ? 3.8071 2.9393 2.6186 -0.8376 -0.1628 -0.5477 122 PHE E O   
10741 C CB  . PHE E 131 ? 3.8138 3.0567 2.6344 -0.8831 -0.1457 -0.5224 122 PHE E CB  
10742 C CG  . PHE E 131 ? 3.7431 3.0566 2.6084 -0.8878 -0.1328 -0.5287 122 PHE E CG  
10743 C CD1 . PHE E 131 ? 3.7350 3.0470 2.5942 -0.8988 -0.1119 -0.5154 122 PHE E CD1 
10744 C CD2 . PHE E 131 ? 3.6889 3.0701 2.6016 -0.8808 -0.1412 -0.5477 122 PHE E CD2 
10745 C CE1 . PHE E 131 ? 3.6741 3.0509 2.5743 -0.9027 -0.0992 -0.5214 122 PHE E CE1 
10746 C CE2 . PHE E 131 ? 3.6283 3.0737 2.5814 -0.8850 -0.1284 -0.5530 122 PHE E CE2 
10747 C CZ  . PHE E 131 ? 3.6217 3.0649 2.5686 -0.8960 -0.1072 -0.5399 122 PHE E CZ  
10748 N N   . PRO E 132 ? 3.9064 2.9703 2.6318 -0.8708 -0.1453 -0.5008 123 PRO E N   
10749 C CA  . PRO E 132 ? 3.9896 2.9853 2.6684 -0.8669 -0.1580 -0.4933 123 PRO E CA  
10750 C C   . PRO E 132 ? 4.0821 3.0828 2.7290 -0.8804 -0.1812 -0.4853 123 PRO E C   
10751 O O   . PRO E 132 ? 4.1395 3.1699 2.7670 -0.9039 -0.1857 -0.4692 123 PRO E O   
10752 C CB  . PRO E 132 ? 4.0706 3.0020 2.6894 -0.8821 -0.1465 -0.4640 123 PRO E CB  
10753 C CG  . PRO E 132 ? 4.0815 3.0520 2.6955 -0.9054 -0.1372 -0.4483 123 PRO E CG  
10754 C CD  . PRO E 132 ? 3.9480 2.9966 2.6397 -0.8915 -0.1294 -0.4757 123 PRO E CD  
10755 N N   . LEU E 133 ? 4.0443 3.0158 2.6864 -0.8649 -0.1956 -0.4966 124 LEU E N   
10756 C CA  . LEU E 133 ? 4.1749 3.1174 2.7551 -0.8856 -0.2159 -0.4819 124 LEU E CA  
10757 C C   . LEU E 133 ? 4.2908 3.1366 2.7946 -0.8952 -0.2159 -0.4576 124 LEU E C   
10758 O O   . LEU E 133 ? 4.2909 3.0866 2.7853 -0.8802 -0.2158 -0.4677 124 LEU E O   
10759 C CB  . LEU E 133 ? 4.1463 3.1102 2.7513 -0.8730 -0.2302 -0.5086 124 LEU E CB  
10760 C CG  . LEU E 133 ? 4.0309 3.0887 2.7125 -0.8606 -0.2316 -0.5344 124 LEU E CG  
10761 C CD1 . LEU E 133 ? 3.9897 3.0595 2.6998 -0.8425 -0.2429 -0.5640 124 LEU E CD1 
10762 C CD2 . LEU E 133 ? 4.0970 3.2012 2.7644 -0.8837 -0.2411 -0.5178 124 LEU E CD2 
10763 N N   . ALA E 134 ? 4.1927 3.0116 2.6422 -0.9196 -0.2159 -0.4252 125 ALA E N   
10764 C CA  . ALA E 134 ? 4.2892 3.0201 2.6741 -0.9257 -0.2120 -0.4017 125 ALA E CA  
10765 C C   . ALA E 134 ? 4.4667 3.1276 2.7785 -0.9376 -0.2318 -0.3884 125 ALA E C   
10766 O O   . ALA E 134 ? 4.5563 3.2336 2.8458 -0.9548 -0.2492 -0.3819 125 ALA E O   
10767 C CB  . ALA E 134 ? 4.3205 3.0453 2.6727 -0.9471 -0.2049 -0.3714 125 ALA E CB  
10768 N N   . PRO E 135 ? 4.6178 3.1998 2.8908 -0.9283 -0.2300 -0.3835 126 PRO E N   
10769 C CA  . PRO E 135 ? 4.7871 3.2958 2.9867 -0.9384 -0.2495 -0.3694 126 PRO E CA  
10770 C C   . PRO E 135 ? 4.9591 3.4329 3.0834 -0.9715 -0.2615 -0.3316 126 PRO E C   
10771 O O   . PRO E 135 ? 4.9808 3.4449 3.0869 -0.9831 -0.2514 -0.3105 126 PRO E O   
10772 C CB  . PRO E 135 ? 4.7971 3.2314 2.9766 -0.9190 -0.2405 -0.3706 126 PRO E CB  
10773 C CG  . PRO E 135 ? 4.6875 3.1407 2.9000 -0.9116 -0.2179 -0.3685 126 PRO E CG  
10774 C CD  . PRO E 135 ? 4.5295 3.0839 2.8219 -0.9077 -0.2103 -0.3890 126 PRO E CD  
10775 N N   . SER E 136 ? 4.8905 3.3468 2.9721 -0.9867 -0.2836 -0.3231 127 SER E N   
10776 C CA  . SER E 136 ? 5.0923 3.5116 3.1003 -1.0189 -0.2973 -0.2866 127 SER E CA  
10777 C C   . SER E 136 ? 5.2073 3.5302 3.1436 -1.0245 -0.2952 -0.2591 127 SER E C   
10778 O O   . SER E 136 ? 5.2314 3.4925 3.1470 -1.0069 -0.2952 -0.2648 127 SER E O   
10779 C CB  . SER E 136 ? 5.2243 3.6324 3.1964 -1.0312 -0.3227 -0.2833 127 SER E CB  
10780 O OG  . SER E 136 ? 5.4186 3.7790 3.3139 -1.0622 -0.3372 -0.2461 127 SER E OG  
10781 N N   . SER E 137 ? 5.1020 3.4128 3.0006 -1.0485 -0.2932 -0.2291 128 SER E N   
10782 C CA  . SER E 137 ? 5.2278 3.4458 3.0504 -1.0569 -0.2943 -0.1998 128 SER E CA  
10783 C C   . SER E 137 ? 5.4188 3.5586 3.1609 -1.0707 -0.3190 -0.1802 128 SER E C   
10784 O O   . SER E 137 ? 5.5506 3.6036 3.2249 -1.0741 -0.3229 -0.1580 128 SER E O   
10785 C CB  . SER E 137 ? 5.2862 3.5142 3.0906 -1.0795 -0.2860 -0.1733 128 SER E CB  
10786 O OG  . SER E 137 ? 5.3171 3.5781 3.1082 -1.1073 -0.2988 -0.1582 128 SER E OG  
10787 N N   . LYS E 138 ? 5.4331 3.6024 3.1805 -1.0786 -0.3363 -0.1874 129 LYS E N   
10788 C CA  . LYS E 138 ? 5.5524 3.6540 3.2275 -1.0917 -0.3617 -0.1702 129 LYS E CA  
10789 C C   . LYS E 138 ? 5.5858 3.6543 3.2644 -1.0657 -0.3687 -0.1933 129 LYS E C   
10790 O O   . LYS E 138 ? 5.6771 3.6983 3.3048 -1.0727 -0.3911 -0.1846 129 LYS E O   
10791 C CB  . LYS E 138 ? 5.5584 3.7104 3.2331 -1.1168 -0.3777 -0.1621 129 LYS E CB  
10792 C CG  . LYS E 138 ? 5.5303 3.7112 3.1967 -1.1451 -0.3727 -0.1368 129 LYS E CG  
10793 C CD  . LYS E 138 ? 5.5381 3.6813 3.1808 -1.1498 -0.3563 -0.1167 129 LYS E CD  
10794 C CE  . LYS E 138 ? 5.7648 3.7934 3.3131 -1.1599 -0.3684 -0.0863 129 LYS E CE  
10795 N NZ  . LYS E 138 ? 5.7662 3.7654 3.3013 -1.1571 -0.3505 -0.0736 129 LYS E NZ  
10796 N N   . SER E 139 ? 5.6173 3.7125 3.3576 -1.0359 -0.3500 -0.2227 130 SER E N   
10797 C CA  . SER E 139 ? 5.6055 3.6753 3.3593 -1.0086 -0.3532 -0.2477 130 SER E CA  
10798 C C   . SER E 139 ? 5.7614 3.7189 3.4267 -1.0098 -0.3690 -0.2260 130 SER E C   
10799 O O   . SER E 139 ? 5.8000 3.6937 3.4085 -1.0193 -0.3671 -0.1985 130 SER E O   
10800 C CB  . SER E 139 ? 5.4042 3.5026 3.2273 -0.9784 -0.3275 -0.2748 130 SER E CB  
10801 O OG  . SER E 139 ? 5.2261 3.4282 3.1342 -0.9738 -0.3153 -0.2987 130 SER E OG  
10802 N N   . THR E 140 ? 5.4876 3.4227 3.1418 -0.9994 -0.3855 -0.2391 131 THR E N   
10803 C CA  . THR E 140 ? 5.6108 3.4430 3.1782 -1.0024 -0.4059 -0.2184 131 THR E CA  
10804 C C   . THR E 140 ? 5.6324 3.3893 3.1733 -0.9825 -0.3939 -0.2135 131 THR E C   
10805 O O   . THR E 140 ? 5.5639 3.3398 3.1610 -0.9537 -0.3757 -0.2404 131 THR E O   
10806 C CB  . THR E 140 ? 5.6395 3.4731 3.2135 -0.9899 -0.4234 -0.2393 131 THR E CB  
10807 O OG1 . THR E 140 ? 5.6046 3.5207 3.2129 -1.0055 -0.4326 -0.2471 131 THR E OG1 
10808 C CG2 . THR E 140 ? 5.7700 3.4996 3.2505 -0.9962 -0.4478 -0.2153 131 THR E CG2 
10809 N N   . SER E 141 ? 5.7159 3.3891 3.1719 -0.9981 -0.4039 -0.1786 132 SER E N   
10810 C CA  . SER E 141 ? 5.7293 3.3286 3.1517 -0.9806 -0.3943 -0.1704 132 SER E CA  
10811 C C   . SER E 141 ? 5.7753 3.3287 3.1967 -0.9505 -0.3991 -0.1901 132 SER E C   
10812 O O   . SER E 141 ? 5.8419 3.3516 3.2179 -0.9538 -0.4225 -0.1852 132 SER E O   
10813 C CB  . SER E 141 ? 5.8584 3.3763 3.1840 -1.0047 -0.4087 -0.1287 132 SER E CB  
10814 O OG  . SER E 141 ? 5.9818 3.4219 3.2662 -0.9862 -0.4037 -0.1206 132 SER E OG  
10815 N N   . GLY E 142 ? 5.8708 3.4346 3.3435 -0.9206 -0.3765 -0.2122 133 GLY E N   
10816 C CA  . GLY E 142 ? 5.8674 3.4042 3.3586 -0.8891 -0.3762 -0.2362 133 GLY E CA  
10817 C C   . GLY E 142 ? 5.7956 3.3952 3.3451 -0.8815 -0.3816 -0.2671 133 GLY E C   
10818 O O   . GLY E 142 ? 5.8425 3.4206 3.4062 -0.8563 -0.3837 -0.2878 133 GLY E O   
10819 N N   . GLY E 143 ? 5.7431 3.4221 3.3282 -0.9016 -0.3834 -0.2713 134 GLY E N   
10820 C CA  . GLY E 143 ? 5.6781 3.4271 3.3159 -0.8991 -0.3907 -0.2982 134 GLY E CA  
10821 C C   . GLY E 143 ? 5.4631 3.3054 3.2050 -0.8812 -0.3662 -0.3325 134 GLY E C   
10822 O O   . GLY E 143 ? 5.3552 3.1958 3.1331 -0.8609 -0.3436 -0.3425 134 GLY E O   
10823 N N   . THR E 144 ? 5.2607 3.1868 3.0523 -0.8883 -0.3711 -0.3507 135 THR E N   
10824 C CA  . THR E 144 ? 5.0633 3.0832 2.9557 -0.8713 -0.3515 -0.3856 135 THR E CA  
10825 C C   . THR E 144 ? 4.9890 3.0875 2.9136 -0.8928 -0.3446 -0.3788 135 THR E C   
10826 O O   . THR E 144 ? 5.0780 3.1909 2.9688 -0.9190 -0.3615 -0.3609 135 THR E O   
10827 C CB  . THR E 144 ? 5.0375 3.0969 2.9691 -0.8574 -0.3625 -0.4169 135 THR E CB  
10828 O OG1 . THR E 144 ? 5.0788 3.0699 2.9918 -0.8328 -0.3651 -0.4271 135 THR E OG1 
10829 C CG2 . THR E 144 ? 4.8415 3.0054 2.8769 -0.8435 -0.3448 -0.4517 135 THR E CG2 
10830 N N   . ALA E 145 ? 5.0765 3.2250 3.0669 -0.8808 -0.3198 -0.3927 136 ALA E N   
10831 C CA  . ALA E 145 ? 4.9815 3.2090 3.0134 -0.8957 -0.3102 -0.3904 136 ALA E CA  
10832 C C   . ALA E 145 ? 4.8037 3.1261 2.9342 -0.8767 -0.2997 -0.4293 136 ALA E C   
10833 O O   . ALA E 145 ? 4.7167 3.0388 2.8909 -0.8493 -0.2905 -0.4562 136 ALA E O   
10834 C CB  . ALA E 145 ? 4.9363 3.1447 2.9619 -0.8978 -0.2907 -0.3725 136 ALA E CB  
10835 N N   . ALA E 146 ? 4.8107 3.2139 2.9767 -0.8908 -0.3011 -0.4318 137 ALA E N   
10836 C CA  . ALA E 146 ? 4.6343 3.1328 2.8943 -0.8744 -0.2913 -0.4662 137 ALA E CA  
10837 C C   . ALA E 146 ? 4.5024 3.0555 2.8071 -0.8774 -0.2721 -0.4629 137 ALA E C   
10838 O O   . ALA E 146 ? 4.5625 3.1093 2.8284 -0.9011 -0.2732 -0.4343 137 ALA E O   
10839 C CB  . ALA E 146 ? 4.6640 3.2200 2.9356 -0.8839 -0.3107 -0.4765 137 ALA E CB  
10840 N N   . LEU E 147 ? 4.4047 3.0094 2.7907 -0.8530 -0.2549 -0.4918 138 LEU E N   
10841 C CA  . LEU E 147 ? 4.2797 2.9429 2.7178 -0.8517 -0.2371 -0.4931 138 LEU E CA  
10842 C C   . LEU E 147 ? 4.2027 2.9449 2.7347 -0.8277 -0.2301 -0.5309 138 LEU E C   
10843 O O   . LEU E 147 ? 4.2076 2.9527 2.7619 -0.8118 -0.2372 -0.5551 138 LEU E O   
10844 C CB  . LEU E 147 ? 4.2848 2.8970 2.7077 -0.8454 -0.2187 -0.4789 138 LEU E CB  
10845 C CG  . LEU E 147 ? 4.2938 2.8621 2.7340 -0.8175 -0.2089 -0.4965 138 LEU E CG  
10846 C CD1 . LEU E 147 ? 4.2118 2.8352 2.7384 -0.7937 -0.1881 -0.5201 138 LEU E CD1 
10847 C CD2 . LEU E 147 ? 4.3630 2.8355 2.7290 -0.8220 -0.2069 -0.4696 138 LEU E CD2 
10848 N N   . GLY E 148 ? 4.2831 3.0879 2.8699 -0.8244 -0.2167 -0.5356 139 GLY E N   
10849 C CA  . GLY E 148 ? 4.1196 2.9992 2.7936 -0.8023 -0.2121 -0.5692 139 GLY E CA  
10850 C C   . GLY E 148 ? 3.9840 2.9240 2.7096 -0.8000 -0.1976 -0.5691 139 GLY E C   
10851 O O   . GLY E 148 ? 3.9988 2.9202 2.6969 -0.8126 -0.1881 -0.5451 139 GLY E O   
10852 N N   . CYS E 149 ? 4.0337 3.0452 2.8338 -0.7829 -0.1969 -0.5963 140 CYS E N   
10853 C CA  . CYS E 149 ? 3.9007 2.9787 2.7566 -0.7784 -0.1864 -0.5996 140 CYS E CA  
10854 C C   . CYS E 149 ? 3.8607 3.0142 2.7559 -0.7786 -0.1990 -0.6148 140 CYS E C   
10855 O O   . CYS E 149 ? 3.8500 3.0181 2.7685 -0.7661 -0.2098 -0.6378 140 CYS E O   
10856 C CB  . CYS E 149 ? 3.7571 2.8390 2.6677 -0.7545 -0.1677 -0.6170 140 CYS E CB  
10857 S SG  . CYS E 149 ? 3.7690 2.7767 2.6393 -0.7572 -0.1470 -0.5965 140 CYS E SG  
10858 N N   . LEU E 150 ? 3.9019 3.0976 2.7938 -0.7984 -0.1955 -0.6006 141 LEU E N   
10859 C CA  . LEU E 150 ? 3.8533 3.1252 2.7852 -0.7998 -0.2032 -0.6129 141 LEU E CA  
10860 C C   . LEU E 150 ? 3.6947 3.0101 2.6897 -0.7866 -0.1855 -0.6297 141 LEU E C   
10861 O O   . LEU E 150 ? 3.6374 2.9494 2.6281 -0.7967 -0.1661 -0.6171 141 LEU E O   
10862 C CB  . LEU E 150 ? 3.9358 3.2284 2.8269 -0.8311 -0.2067 -0.5873 141 LEU E CB  
10863 C CG  . LEU E 150 ? 3.8859 3.2591 2.8154 -0.8355 -0.2114 -0.5963 141 LEU E CG  
10864 C CD1 . LEU E 150 ? 3.9201 3.3206 2.8747 -0.8188 -0.2333 -0.6181 141 LEU E CD1 
10865 C CD2 . LEU E 150 ? 3.9842 3.3708 2.8700 -0.8675 -0.2117 -0.5682 141 LEU E CD2 
10866 N N   . VAL E 151 ? 3.4642 2.8190 2.5156 -0.7643 -0.1924 -0.6570 142 VAL E N   
10867 C CA  . VAL E 151 ? 3.4103 2.8032 2.5226 -0.7499 -0.1766 -0.6735 142 VAL E CA  
10868 C C   . VAL E 151 ? 3.3748 2.8436 2.5187 -0.7566 -0.1814 -0.6795 142 VAL E C   
10869 O O   . VAL E 151 ? 3.3659 2.8644 2.5354 -0.7444 -0.1980 -0.6966 142 VAL E O   
10870 C CB  . VAL E 151 ? 3.3997 2.7739 2.5517 -0.7187 -0.1789 -0.6985 142 VAL E CB  
10871 C CG1 . VAL E 151 ? 3.3470 2.7570 2.5577 -0.7057 -0.1612 -0.7123 142 VAL E CG1 
10872 C CG2 . VAL E 151 ? 3.4398 2.7381 2.5571 -0.7124 -0.1750 -0.6918 142 VAL E CG2 
10873 N N   . LYS E 152 ? 3.3704 2.8706 2.5115 -0.7762 -0.1666 -0.6650 143 LYS E N   
10874 C CA  . LYS E 152 ? 3.3728 2.9389 2.5258 -0.7902 -0.1712 -0.6627 143 LYS E CA  
10875 C C   . LYS E 152 ? 3.2928 2.9143 2.4988 -0.7873 -0.1512 -0.6716 143 LYS E C   
10876 O O   . LYS E 152 ? 3.2578 2.8644 2.4711 -0.7867 -0.1304 -0.6676 143 LYS E O   
10877 C CB  . LYS E 152 ? 3.5063 3.0632 2.6007 -0.8206 -0.1730 -0.6340 143 LYS E CB  
10878 C CG  . LYS E 152 ? 3.5632 3.1854 2.6643 -0.8362 -0.1794 -0.6299 143 LYS E CG  
10879 C CD  . LYS E 152 ? 3.6897 3.2934 2.7271 -0.8650 -0.1860 -0.6013 143 LYS E CD  
10880 C CE  . LYS E 152 ? 3.7318 3.4020 2.7781 -0.8835 -0.1835 -0.5935 143 LYS E CE  
10881 N NZ  . LYS E 152 ? 3.7285 3.4539 2.8128 -0.8717 -0.1986 -0.6129 143 LYS E NZ  
10882 N N   . ASP E 153 ? 3.4226 3.1084 2.6643 -0.7856 -0.1572 -0.6832 144 ASP E N   
10883 C CA  . ASP E 153 ? 3.3544 3.1043 2.6437 -0.7871 -0.1389 -0.6897 144 ASP E CA  
10884 C C   . ASP E 153 ? 3.2498 2.9988 2.5881 -0.7663 -0.1210 -0.7065 144 ASP E C   
10885 O O   . ASP E 153 ? 3.2245 2.9782 2.5737 -0.7705 -0.0983 -0.7012 144 ASP E O   
10886 C CB  . ASP E 153 ? 3.4100 3.1732 2.6724 -0.8128 -0.1240 -0.6674 144 ASP E CB  
10887 C CG  . ASP E 153 ? 3.5228 3.3074 2.7486 -0.8348 -0.1383 -0.6518 144 ASP E CG  
10888 O OD1 . ASP E 153 ? 3.5359 3.3446 2.7699 -0.8295 -0.1574 -0.6612 144 ASP E OD1 
10889 O OD2 . ASP E 153 ? 3.6254 3.4031 2.8139 -0.8577 -0.1302 -0.6295 144 ASP E OD2 
10890 N N   . TYR E 154 ? 3.2371 2.9801 2.6045 -0.7439 -0.1309 -0.7263 145 TYR E N   
10891 C CA  . TYR E 154 ? 3.1316 2.8808 2.5493 -0.7246 -0.1135 -0.7426 145 TYR E CA  
10892 C C   . TYR E 154 ? 3.0558 2.8643 2.5258 -0.7130 -0.1166 -0.7626 145 TYR E C   
10893 O O   . TYR E 154 ? 3.1028 2.9299 2.5662 -0.7139 -0.1375 -0.7664 145 TYR E O   
10894 C CB  . TYR E 154 ? 3.1276 2.8061 2.5333 -0.7070 -0.1163 -0.7472 145 TYR E CB  
10895 C CG  . TYR E 154 ? 3.1529 2.8025 2.5455 -0.6938 -0.1425 -0.7570 145 TYR E CG  
10896 C CD1 . TYR E 154 ? 3.2594 2.8686 2.5976 -0.7027 -0.1616 -0.7451 145 TYR E CD1 
10897 C CD2 . TYR E 154 ? 3.0840 2.7460 2.5179 -0.6726 -0.1464 -0.7777 145 TYR E CD2 
10898 C CE1 . TYR E 154 ? 3.2883 2.8721 2.6152 -0.6897 -0.1851 -0.7550 145 TYR E CE1 
10899 C CE2 . TYR E 154 ? 3.1193 2.7535 2.5400 -0.6599 -0.1706 -0.7869 145 TYR E CE2 
10900 C CZ  . TYR E 154 ? 3.2238 2.8194 2.5919 -0.6677 -0.1904 -0.7763 145 TYR E CZ  
10901 O OH  . TYR E 154 ? 3.3286 2.8979 2.6842 -0.6542 -0.2142 -0.7864 145 TYR E OH  
10902 N N   . PHE E 155 ? 3.1289 2.9686 2.6514 -0.7023 -0.0943 -0.7750 146 PHE E N   
10903 C CA  . PHE E 155 ? 3.0607 2.9567 2.6381 -0.6900 -0.0922 -0.7951 146 PHE E CA  
10904 C C   . PHE E 155 ? 2.9666 2.8673 2.5941 -0.6729 -0.0679 -0.8090 146 PHE E C   
10905 O O   . PHE E 155 ? 2.9392 2.8318 2.5714 -0.6758 -0.0466 -0.8027 146 PHE E O   
10906 C CB  . PHE E 155 ? 3.0600 3.0344 2.6591 -0.7039 -0.0862 -0.7945 146 PHE E CB  
10907 C CG  . PHE E 155 ? 2.9880 3.0272 2.6461 -0.6919 -0.0817 -0.8153 146 PHE E CG  
10908 C CD1 . PHE E 155 ? 2.8990 2.9834 2.6168 -0.6827 -0.0537 -0.8287 146 PHE E CD1 
10909 C CD2 . PHE E 155 ? 3.0154 3.0720 2.6705 -0.6894 -0.1046 -0.8219 146 PHE E CD2 
10910 C CE1 . PHE E 155 ? 2.8382 2.9857 2.6132 -0.6712 -0.0476 -0.8488 146 PHE E CE1 
10911 C CE2 . PHE E 155 ? 2.9561 3.0743 2.6662 -0.6785 -0.0993 -0.8412 146 PHE E CE2 
10912 C CZ  . PHE E 155 ? 2.8678 3.0325 2.6389 -0.6693 -0.0703 -0.8549 146 PHE E CZ  
10913 N N   . PRO E 156 ? 2.8576 2.7719 2.5226 -0.6551 -0.0702 -0.8278 147 PRO E N   
10914 C CA  . PRO E 156 ? 2.8802 2.7909 2.5366 -0.6483 -0.0962 -0.8360 147 PRO E CA  
10915 C C   . PRO E 156 ? 2.9411 2.7674 2.5537 -0.6384 -0.1146 -0.8327 147 PRO E C   
10916 O O   . PRO E 156 ? 2.9651 2.7393 2.5520 -0.6389 -0.1074 -0.8224 147 PRO E O   
10917 C CB  . PRO E 156 ? 2.7981 2.7644 2.5228 -0.6330 -0.0813 -0.8582 147 PRO E CB  
10918 C CG  . PRO E 156 ? 2.7399 2.6932 2.4942 -0.6235 -0.0534 -0.8618 147 PRO E CG  
10919 C CD  . PRO E 156 ? 2.7643 2.7044 2.4894 -0.6399 -0.0434 -0.8432 147 PRO E CD  
10920 N N   . GLU E 157 ? 2.7481 2.5615 2.3522 -0.6289 -0.1374 -0.8414 148 GLU E N   
10921 C CA  . GLU E 157 ? 2.7905 2.5277 2.3642 -0.6144 -0.1512 -0.8429 148 GLU E CA  
10922 C C   . GLU E 157 ? 2.7667 2.4927 2.3808 -0.5965 -0.1281 -0.8550 148 GLU E C   
10923 O O   . GLU E 157 ? 2.7166 2.5022 2.3875 -0.5936 -0.1055 -0.8659 148 GLU E O   
10924 C CB  . GLU E 157 ? 2.8206 2.5487 2.3775 -0.6073 -0.1806 -0.8507 148 GLU E CB  
10925 C CG  . GLU E 157 ? 2.8930 2.6234 2.4058 -0.6223 -0.2060 -0.8391 148 GLU E CG  
10926 C CD  . GLU E 157 ? 2.9551 2.6517 2.4373 -0.6166 -0.2317 -0.8482 148 GLU E CD  
10927 O OE1 . GLU E 157 ? 2.9536 2.6932 2.4511 -0.6177 -0.2417 -0.8597 148 GLU E OE1 
10928 O OE2 . GLU E 157 ? 3.0116 2.6440 2.4544 -0.6151 -0.2375 -0.8466 148 GLU E OE2 
10929 N N   . PRO E 158 ? 2.9772 2.6299 2.5649 -0.5836 -0.1324 -0.8537 149 PRO E N   
10930 C CA  . PRO E 158 ? 3.0710 2.6537 2.5976 -0.5851 -0.1539 -0.8418 149 PRO E CA  
10931 C C   . PRO E 158 ? 3.0982 2.6429 2.6009 -0.5922 -0.1396 -0.8266 149 PRO E C   
10932 O O   . PRO E 158 ? 3.0468 2.6114 2.5776 -0.5944 -0.1132 -0.8247 149 PRO E O   
10933 C CB  . PRO E 158 ? 3.0858 2.6191 2.6088 -0.5633 -0.1634 -0.8544 149 PRO E CB  
10934 C CG  . PRO E 158 ? 2.9992 2.5523 2.5751 -0.5507 -0.1345 -0.8646 149 PRO E CG  
10935 C CD  . PRO E 158 ? 2.9326 2.5715 2.5560 -0.5633 -0.1158 -0.8675 149 PRO E CD  
10936 N N   . VAL E 159 ? 3.2466 2.7388 2.6979 -0.5962 -0.1563 -0.8160 150 VAL E N   
10937 C CA  . VAL E 159 ? 3.2637 2.7034 2.6876 -0.5981 -0.1447 -0.8035 150 VAL E CA  
10938 C C   . VAL E 159 ? 3.2954 2.6703 2.7037 -0.5772 -0.1555 -0.8110 150 VAL E C   
10939 O O   . VAL E 159 ? 3.3544 2.7222 2.7559 -0.5705 -0.1741 -0.8234 150 VAL E O   
10940 C CB  . VAL E 159 ? 3.3468 2.7803 2.7236 -0.6223 -0.1492 -0.7834 150 VAL E CB  
10941 C CG1 . VAL E 159 ? 3.3275 2.8207 2.7202 -0.6418 -0.1342 -0.7748 150 VAL E CG1 
10942 C CG2 . VAL E 159 ? 3.4332 2.8601 2.7763 -0.6269 -0.1776 -0.7831 150 VAL E CG2 
10943 N N   . THR E 160 ? 3.4183 2.7469 2.8184 -0.5710 -0.1396 -0.8052 151 THR E N   
10944 C CA  . THR E 160 ? 3.4604 2.7234 2.8372 -0.5549 -0.1484 -0.8083 151 THR E CA  
10945 C C   . THR E 160 ? 3.5420 2.7665 2.8691 -0.5711 -0.1468 -0.7896 151 THR E C   
10946 O O   . THR E 160 ? 3.5456 2.7766 2.8627 -0.5876 -0.1293 -0.7740 151 THR E O   
10947 C CB  . THR E 160 ? 3.4286 2.6643 2.8335 -0.5334 -0.1298 -0.8158 151 THR E CB  
10948 O OG1 . THR E 160 ? 3.4336 2.6738 2.8449 -0.5427 -0.1036 -0.8037 151 THR E OG1 
10949 C CG2 . THR E 160 ? 3.3664 2.6388 2.8162 -0.5200 -0.1273 -0.8324 151 THR E CG2 
10950 N N   . VAL E 161 ? 3.4429 2.6247 2.7293 -0.5748 -0.1584 -0.7914 152 VAL E N   
10951 C CA  . VAL E 161 ? 3.5306 2.6684 2.7607 -0.5925 -0.1559 -0.7712 152 VAL E CA  
10952 C C   . VAL E 161 ? 3.5831 2.6523 2.7913 -0.5805 -0.1511 -0.7755 152 VAL E C   
10953 O O   . VAL E 161 ? 3.6151 2.6687 2.8238 -0.5706 -0.1606 -0.7935 152 VAL E O   
10954 C CB  . VAL E 161 ? 3.6250 2.7749 2.8093 -0.6183 -0.1724 -0.7625 152 VAL E CB  
10955 C CG1 . VAL E 161 ? 3.7487 2.8466 2.8662 -0.6392 -0.1683 -0.7363 152 VAL E CG1 
10956 C CG2 . VAL E 161 ? 3.6018 2.8232 2.8119 -0.6281 -0.1775 -0.7594 152 VAL E CG2 
10957 N N   . SER E 162 ? 3.5104 2.5387 2.6990 -0.5810 -0.1361 -0.7586 153 SER E N   
10958 C CA  . SER E 162 ? 3.5759 2.5336 2.7312 -0.5744 -0.1304 -0.7558 153 SER E CA  
10959 C C   . SER E 162 ? 3.6748 2.5906 2.7633 -0.5983 -0.1264 -0.7263 153 SER E C   
10960 O O   . SER E 162 ? 3.6766 2.6196 2.7542 -0.6160 -0.1250 -0.7092 153 SER E O   
10961 C CB  . SER E 162 ? 3.4980 2.4395 2.6959 -0.5469 -0.1145 -0.7633 153 SER E CB  
10962 O OG  . SER E 162 ? 3.4525 2.4072 2.6594 -0.5520 -0.0984 -0.7476 153 SER E OG  
10963 N N   . TRP E 163 ? 3.5961 2.4424 2.6369 -0.5985 -0.1248 -0.7189 154 TRP E N   
10964 C CA  . TRP E 163 ? 3.6984 2.4911 2.6691 -0.6187 -0.1206 -0.6882 154 TRP E CA  
10965 C C   . TRP E 163 ? 3.6894 2.4322 2.6614 -0.6012 -0.1035 -0.6828 154 TRP E C   
10966 O O   . TRP E 163 ? 3.6806 2.3963 2.6703 -0.5799 -0.1010 -0.6988 154 TRP E O   
10967 C CB  . TRP E 163 ? 3.8358 2.5826 2.7332 -0.6380 -0.1368 -0.6775 154 TRP E CB  
10968 C CG  . TRP E 163 ? 3.8627 2.6559 2.7461 -0.6608 -0.1530 -0.6738 154 TRP E CG  
10969 C CD1 . TRP E 163 ? 3.8315 2.6735 2.7457 -0.6581 -0.1672 -0.6957 154 TRP E CD1 
10970 C CD2 . TRP E 163 ? 3.9265 2.7245 2.7640 -0.6889 -0.1566 -0.6460 154 TRP E CD2 
10971 N NE1 . TRP E 163 ? 3.8722 2.7499 2.7624 -0.6827 -0.1793 -0.6829 154 TRP E NE1 
10972 C CE2 . TRP E 163 ? 3.9315 2.7827 2.7751 -0.7019 -0.1729 -0.6523 154 TRP E CE2 
10973 C CE3 . TRP E 163 ? 3.9833 2.7457 2.7748 -0.7039 -0.1480 -0.6160 154 TRP E CE3 
10974 C CZ2 . TRP E 163 ? 3.9914 2.8615 2.7983 -0.7291 -0.1800 -0.6294 154 TRP E CZ2 
10975 C CZ3 . TRP E 163 ? 4.0436 2.8232 2.7976 -0.7312 -0.1553 -0.5937 154 TRP E CZ3 
10976 C CH2 . TRP E 163 ? 4.0474 2.8805 2.8101 -0.7435 -0.1709 -0.6003 154 TRP E CH2 
10977 N N   . ASN E 164 ? 3.7723 2.5034 2.7246 -0.6101 -0.0921 -0.6599 155 ASN E N   
10978 C CA  . ASN E 164 ? 3.7688 2.4543 2.7166 -0.5970 -0.0744 -0.6513 155 ASN E CA  
10979 C C   . ASN E 164 ? 3.6592 2.3649 2.6773 -0.5674 -0.0637 -0.6763 155 ASN E C   
10980 O O   . ASN E 164 ? 3.6685 2.3320 2.6898 -0.5482 -0.0566 -0.6802 155 ASN E O   
10981 C CB  . ASN E 164 ? 3.8928 2.4974 2.7726 -0.6002 -0.0778 -0.6357 155 ASN E CB  
10982 C CG  . ASN E 164 ? 4.0150 2.5872 2.8137 -0.6313 -0.0861 -0.6050 155 ASN E CG  
10983 O OD1 . ASN E 164 ? 4.0005 2.6122 2.7990 -0.6485 -0.0867 -0.5941 155 ASN E OD1 
10984 N ND2 . ASN E 164 ? 4.1410 2.6394 2.8691 -0.6382 -0.0931 -0.5898 155 ASN E ND2 
10985 N N   . SER E 165 ? 3.7509 2.5208 2.8237 -0.5639 -0.0628 -0.6920 156 SER E N   
10986 C CA  . SER E 165 ? 3.6366 2.4305 2.7747 -0.5381 -0.0530 -0.7131 156 SER E CA  
10987 C C   . SER E 165 ? 3.6383 2.4171 2.8043 -0.5111 -0.0638 -0.7349 156 SER E C   
10988 O O   . SER E 165 ? 3.6182 2.3891 2.8212 -0.4876 -0.0536 -0.7463 156 SER E O   
10989 C CB  . SER E 165 ? 3.6357 2.4040 2.7720 -0.5344 -0.0282 -0.7013 156 SER E CB  
10990 O OG  . SER E 165 ? 3.6531 2.4452 2.7747 -0.5567 -0.0175 -0.6851 156 SER E OG  
10991 N N   . GLY E 166 ? 3.4707 2.2390 2.6086 -0.5191 -0.0808 -0.7400 157 GLY E N   
10992 C CA  . GLY E 166 ? 3.4987 2.2456 2.6465 -0.5022 -0.0874 -0.7612 157 GLY E CA  
10993 C C   . GLY E 166 ? 3.5683 2.2388 2.6615 -0.5023 -0.0848 -0.7513 157 GLY E C   
10994 O O   . GLY E 166 ? 3.5987 2.2462 2.6933 -0.4895 -0.0905 -0.7678 157 GLY E O   
10995 N N   . ALA E 167 ? 3.7770 2.4052 2.8197 -0.5157 -0.0765 -0.7241 158 ALA E N   
10996 C CA  . ALA E 167 ? 3.8896 2.4392 2.8743 -0.5150 -0.0742 -0.7108 158 ALA E CA  
10997 C C   . ALA E 167 ? 4.0170 2.5315 2.9302 -0.5375 -0.0914 -0.7014 158 ALA E C   
10998 O O   . ALA E 167 ? 4.1190 2.5669 2.9841 -0.5343 -0.0940 -0.6944 158 ALA E O   
10999 C CB  . ALA E 167 ? 3.9175 2.4317 2.8696 -0.5204 -0.0606 -0.6834 158 ALA E CB  
11000 N N   . LEU E 168 ? 3.8328 2.3901 2.7370 -0.5595 -0.1042 -0.6998 159 LEU E N   
11001 C CA  . LEU E 168 ? 3.9483 2.4813 2.7874 -0.5821 -0.1233 -0.6906 159 LEU E CA  
11002 C C   . LEU E 168 ? 3.8968 2.4883 2.7781 -0.5794 -0.1368 -0.7182 159 LEU E C   
11003 O O   . LEU E 168 ? 3.8082 2.4704 2.7347 -0.5835 -0.1382 -0.7266 159 LEU E O   
11004 C CB  . LEU E 168 ? 4.0102 2.5425 2.7946 -0.6132 -0.1284 -0.6606 159 LEU E CB  
11005 C CG  . LEU E 168 ? 4.1329 2.6443 2.8476 -0.6394 -0.1501 -0.6470 159 LEU E CG  
11006 C CD1 . LEU E 168 ? 4.2706 2.6923 2.9148 -0.6382 -0.1575 -0.6345 159 LEU E CD1 
11007 C CD2 . LEU E 168 ? 4.1744 2.6982 2.8495 -0.6682 -0.1533 -0.6190 159 LEU E CD2 
11008 N N   . THR E 169 ? 3.9688 2.5305 2.8346 -0.5714 -0.1469 -0.7317 160 THR E N   
11009 C CA  . THR E 169 ? 3.9308 2.5425 2.8328 -0.5670 -0.1608 -0.7592 160 THR E CA  
11010 C C   . THR E 169 ? 4.0606 2.6373 2.8948 -0.5839 -0.1816 -0.7531 160 THR E C   
11011 O O   . THR E 169 ? 4.0536 2.6793 2.8928 -0.5966 -0.1973 -0.7615 160 THR E O   
11012 C CB  . THR E 169 ? 3.8471 2.4691 2.8176 -0.5327 -0.1524 -0.7902 160 THR E CB  
11013 O OG1 . THR E 169 ? 3.9263 2.4716 2.8629 -0.5199 -0.1460 -0.7850 160 THR E OG1 
11014 C CG2 . THR E 169 ? 3.7124 2.3785 2.7534 -0.5159 -0.1363 -0.7965 160 THR E CG2 
11015 N N   . SER E 170 ? 3.9704 2.4628 2.7406 -0.5833 -0.1832 -0.7378 161 SER E N   
11016 C CA  . SER E 170 ? 4.1086 2.5568 2.8060 -0.5984 -0.2050 -0.7281 161 SER E CA  
11017 C C   . SER E 170 ? 4.1778 2.6393 2.8215 -0.6325 -0.2203 -0.7027 161 SER E C   
11018 O O   . SER E 170 ? 4.1963 2.6474 2.8144 -0.6474 -0.2133 -0.6770 161 SER E O   
11019 C CB  . SER E 170 ? 4.2281 2.5764 2.8614 -0.5908 -0.2035 -0.7102 161 SER E CB  
11020 O OG  . SER E 170 ? 4.1691 2.5067 2.8536 -0.5583 -0.1891 -0.7335 161 SER E OG  
11021 N N   . GLY E 171 ? 4.1133 2.5989 2.7403 -0.6444 -0.2416 -0.7097 162 GLY E N   
11022 C CA  . GLY E 171 ? 4.2120 2.7123 2.7885 -0.6762 -0.2583 -0.6859 162 GLY E CA  
11023 C C   . GLY E 171 ? 4.1225 2.7133 2.7525 -0.6863 -0.2537 -0.6903 162 GLY E C   
11024 O O   . GLY E 171 ? 4.1979 2.8045 2.7897 -0.7127 -0.2652 -0.6688 162 GLY E O   
11025 N N   . VAL E 172 ? 4.0151 2.6646 2.7317 -0.6654 -0.2382 -0.7166 163 VAL E N   
11026 C CA  . VAL E 172 ? 3.9402 2.6752 2.7121 -0.6708 -0.2341 -0.7219 163 VAL E CA  
11027 C C   . VAL E 172 ? 3.9166 2.7195 2.7210 -0.6713 -0.2515 -0.7445 163 VAL E C   
11028 O O   . VAL E 172 ? 3.9156 2.7253 2.7516 -0.6518 -0.2559 -0.7723 163 VAL E O   
11029 C CB  . VAL E 172 ? 3.8732 2.6357 2.7201 -0.6469 -0.2119 -0.7372 163 VAL E CB  
11030 C CG1 . VAL E 172 ? 3.7976 2.6471 2.7022 -0.6497 -0.2103 -0.7438 163 VAL E CG1 
11031 C CG2 . VAL E 172 ? 3.8937 2.5954 2.7080 -0.6477 -0.1952 -0.7129 163 VAL E CG2 
11032 N N   . HIS E 173 ? 3.9521 2.8059 2.7492 -0.6927 -0.2612 -0.7324 164 HIS E N   
11033 C CA  . HIS E 173 ? 3.9611 2.8948 2.8009 -0.6920 -0.2753 -0.7527 164 HIS E CA  
11034 C C   . HIS E 173 ? 3.7820 2.7879 2.6784 -0.6919 -0.2657 -0.7530 164 HIS E C   
11035 O O   . HIS E 173 ? 3.7717 2.7848 2.6397 -0.7131 -0.2639 -0.7271 164 HIS E O   
11036 C CB  . HIS E 173 ? 4.1498 3.0811 2.9269 -0.7171 -0.2984 -0.7365 164 HIS E CB  
11037 C CG  . HIS E 173 ? 4.3365 3.2017 3.0585 -0.7161 -0.3118 -0.7373 164 HIS E CG  
11038 N ND1 . HIS E 173 ? 4.3820 3.2550 3.1374 -0.6942 -0.3173 -0.7691 164 HIS E ND1 
11039 C CD2 . HIS E 173 ? 4.4834 3.2703 3.1170 -0.7335 -0.3219 -0.7092 164 HIS E CD2 
11040 C CE1 . HIS E 173 ? 4.5534 3.3562 3.2435 -0.6979 -0.3296 -0.7608 164 HIS E CE1 
11041 N NE2 . HIS E 173 ? 4.6124 3.3604 3.2268 -0.7213 -0.3334 -0.7239 164 HIS E NE2 
11042 N N   . THR E 174 ? 3.9976 3.0533 2.9711 -0.6680 -0.2601 -0.7805 165 THR E N   
11043 C CA  . THR E 174 ? 3.8293 2.9546 2.8574 -0.6658 -0.2539 -0.7817 165 THR E CA  
11044 C C   . THR E 174 ? 3.8606 3.0526 2.9132 -0.6672 -0.2727 -0.7964 165 THR E C   
11045 O O   . THR E 174 ? 3.8799 3.0879 2.9679 -0.6485 -0.2798 -0.8225 165 THR E O   
11046 C CB  . THR E 174 ? 3.6541 2.7856 2.7455 -0.6391 -0.2365 -0.7969 165 THR E CB  
11047 O OG1 . THR E 174 ? 3.6530 2.7258 2.7209 -0.6384 -0.2191 -0.7811 165 THR E OG1 
11048 C CG2 . THR E 174 ? 3.5374 2.7389 2.6809 -0.6372 -0.2321 -0.7967 165 THR E CG2 
11049 N N   . PHE E 175 ? 3.7946 3.0243 2.8273 -0.6891 -0.2805 -0.7786 166 PHE E N   
11050 C CA  . PHE E 175 ? 3.8442 3.1330 2.8893 -0.6932 -0.2997 -0.7883 166 PHE E CA  
11051 C C   . PHE E 175 ? 3.6604 3.0156 2.7813 -0.6747 -0.2967 -0.8072 166 PHE E C   
11052 O O   . PHE E 175 ? 3.5118 2.8786 2.6681 -0.6672 -0.2799 -0.8035 166 PHE E O   
11053 C CB  . PHE E 175 ? 3.8942 3.2020 2.8947 -0.7218 -0.3079 -0.7613 166 PHE E CB  
11054 C CG  . PHE E 175 ? 4.1073 3.3532 3.0259 -0.7422 -0.3180 -0.7417 166 PHE E CG  
11055 C CD1 . PHE E 175 ? 4.2786 3.5253 3.1692 -0.7467 -0.3392 -0.7483 166 PHE E CD1 
11056 C CD2 . PHE E 175 ? 4.1516 3.3345 3.0181 -0.7565 -0.3069 -0.7149 166 PHE E CD2 
11057 C CE1 . PHE E 175 ? 4.4902 3.6738 3.3005 -0.7658 -0.3497 -0.7271 166 PHE E CE1 
11058 C CE2 . PHE E 175 ? 4.3489 3.4668 3.1345 -0.7756 -0.3174 -0.6931 166 PHE E CE2 
11059 C CZ  . PHE E 175 ? 4.5327 3.6494 3.2892 -0.7804 -0.3391 -0.6986 166 PHE E CZ  
11060 N N   . PRO E 176 ? 3.6850 3.0814 2.8283 -0.6678 -0.3128 -0.8255 167 PRO E N   
11061 C CA  . PRO E 176 ? 3.5172 2.9765 2.7238 -0.6550 -0.3105 -0.8377 167 PRO E CA  
11062 C C   . PRO E 176 ? 3.4262 2.9321 2.6434 -0.6687 -0.3037 -0.8181 167 PRO E C   
11063 O O   . PRO E 176 ? 3.5110 3.0224 2.6878 -0.6897 -0.3104 -0.7991 167 PRO E O   
11064 C CB  . PRO E 176 ? 3.6262 3.1188 2.8357 -0.6531 -0.3321 -0.8538 167 PRO E CB  
11065 C CG  . PRO E 176 ? 3.8375 3.2721 2.9989 -0.6541 -0.3424 -0.8595 167 PRO E CG  
11066 C CD  . PRO E 176 ? 3.8874 3.2703 2.9963 -0.6711 -0.3332 -0.8351 167 PRO E CD  
11067 N N   . ALA E 177 ? 3.3454 2.8827 2.6148 -0.6574 -0.2888 -0.8212 168 ALA E N   
11068 C CA  . ALA E 177 ? 3.3063 2.8888 2.5883 -0.6689 -0.2814 -0.8037 168 ALA E CA  
11069 C C   . ALA E 177 ? 3.3382 2.9781 2.6197 -0.6795 -0.2983 -0.8030 168 ALA E C   
11070 O O   . ALA E 177 ? 3.3255 2.9878 2.6229 -0.6720 -0.3106 -0.8200 168 ALA E O   
11071 C CB  . ALA E 177 ? 3.2441 2.8535 2.5832 -0.6548 -0.2621 -0.8081 168 ALA E CB  
11072 N N   . VAL E 178 ? 3.1927 2.8570 2.4558 -0.6971 -0.2981 -0.7825 169 VAL E N   
11073 C CA  . VAL E 178 ? 3.2064 2.9307 2.4743 -0.7065 -0.3111 -0.7793 169 VAL E CA  
11074 C C   . VAL E 178 ? 3.1309 2.9076 2.4407 -0.7074 -0.2952 -0.7724 169 VAL E C   
11075 O O   . VAL E 178 ? 3.1198 2.8833 2.4253 -0.7171 -0.2740 -0.7616 169 VAL E O   
11076 C CB  . VAL E 178 ? 3.3373 3.0441 2.5420 -0.7294 -0.3234 -0.7599 169 VAL E CB  
11077 C CG1 . VAL E 178 ? 3.3677 3.0582 2.5475 -0.7450 -0.3093 -0.7347 169 VAL E CG1 
11078 C CG2 . VAL E 178 ? 3.3642 3.1212 2.5635 -0.7375 -0.3424 -0.7599 169 VAL E CG2 
11079 N N   . LEU E 179 ? 3.1227 2.9633 2.4670 -0.7069 -0.2982 -0.7809 170 LEU E N   
11080 C CA  . LEU E 179 ? 3.0726 2.9751 2.4486 -0.7200 -0.2766 -0.7769 170 LEU E CA  
11081 C C   . LEU E 179 ? 3.1754 3.1037 2.5163 -0.7451 -0.2803 -0.7568 170 LEU E C   
11082 O O   . LEU E 179 ? 3.2430 3.1958 2.5703 -0.7493 -0.2997 -0.7555 170 LEU E O   
11083 C CB  . LEU E 179 ? 3.0052 2.9688 2.4376 -0.7087 -0.2735 -0.7953 170 LEU E CB  
11084 C CG  . LEU E 179 ? 2.9400 2.9754 2.4152 -0.7185 -0.2485 -0.7956 170 LEU E CG  
11085 C CD1 . LEU E 179 ? 2.8807 2.8984 2.3708 -0.7187 -0.2209 -0.7932 170 LEU E CD1 
11086 C CD2 . LEU E 179 ? 2.8975 2.9950 2.4288 -0.7066 -0.2452 -0.8151 170 LEU E CD2 
11087 N N   . GLN E 180 ? 3.3270 3.2500 2.6529 -0.7620 -0.2611 -0.7407 171 GLN E N   
11088 C CA  . GLN E 180 ? 3.4072 3.3505 2.6974 -0.7881 -0.2610 -0.7192 171 GLN E CA  
11089 C C   . GLN E 180 ? 3.4112 3.4362 2.7371 -0.7956 -0.2537 -0.7223 171 GLN E C   
11090 O O   . GLN E 180 ? 3.3038 3.3699 2.6838 -0.7828 -0.2423 -0.7395 171 GLN E O   
11091 C CB  . GLN E 180 ? 3.4449 3.3532 2.7068 -0.8037 -0.2419 -0.7005 171 GLN E CB  
11092 C CG  . GLN E 180 ? 3.4954 3.3233 2.7165 -0.7989 -0.2482 -0.6948 171 GLN E CG  
11093 C CD  . GLN E 180 ? 3.5057 3.2975 2.7052 -0.8111 -0.2269 -0.6786 171 GLN E CD  
11094 O OE1 . GLN E 180 ? 3.6276 3.3837 2.7731 -0.8302 -0.2285 -0.6563 171 GLN E OE1 
11095 N NE2 . GLN E 180 ? 3.3952 3.1958 2.6355 -0.8006 -0.2064 -0.6887 171 GLN E NE2 
11096 N N   . SER E 181 ? 3.4662 3.5154 2.7608 -0.8171 -0.2593 -0.7049 172 SER E N   
11097 C CA  . SER E 181 ? 3.4602 3.5873 2.7845 -0.8259 -0.2518 -0.7062 172 SER E CA  
11098 C C   . SER E 181 ? 3.3962 3.5571 2.7582 -0.8288 -0.2220 -0.7086 172 SER E C   
11099 O O   . SER E 181 ? 3.3659 3.5950 2.7687 -0.8286 -0.2120 -0.7173 172 SER E O   
11100 C CB  . SER E 181 ? 3.5879 3.7281 2.8666 -0.8508 -0.2606 -0.6839 172 SER E CB  
11101 O OG  . SER E 181 ? 3.6873 3.7924 2.9265 -0.8706 -0.2481 -0.6619 172 SER E OG  
11102 N N   . SER E 182 ? 3.3434 3.4593 2.6924 -0.8313 -0.2071 -0.7012 173 SER E N   
11103 C CA  . SER E 182 ? 3.2843 3.4273 2.6667 -0.8329 -0.1786 -0.7034 173 SER E CA  
11104 C C   . SER E 182 ? 3.1560 3.3197 2.5996 -0.8091 -0.1674 -0.7281 173 SER E C   
11105 O O   . SER E 182 ? 3.1024 3.3080 2.5849 -0.8086 -0.1437 -0.7338 173 SER E O   
11106 C CB  . SER E 182 ? 3.3219 3.4075 2.6673 -0.8435 -0.1670 -0.6862 173 SER E CB  
11107 O OG  . SER E 182 ? 3.2719 3.2930 2.6090 -0.8272 -0.1733 -0.6929 173 SER E OG  
11108 N N   . GLY E 183 ? 3.3979 3.5344 2.8510 -0.7896 -0.1829 -0.7426 174 GLY E N   
11109 C CA  . GLY E 183 ? 3.2691 3.4181 2.7769 -0.7679 -0.1715 -0.7645 174 GLY E CA  
11110 C C   . GLY E 183 ? 3.2308 3.3159 2.7344 -0.7565 -0.1632 -0.7663 174 GLY E C   
11111 O O   . GLY E 183 ? 3.1482 3.2404 2.6966 -0.7387 -0.1518 -0.7836 174 GLY E O   
11112 N N   . LEU E 184 ? 3.1042 3.1289 2.5561 -0.7666 -0.1672 -0.7489 175 LEU E N   
11113 C CA  . LEU E 184 ? 3.0832 3.0409 2.5237 -0.7559 -0.1618 -0.7491 175 LEU E CA  
11114 C C   . LEU E 184 ? 3.1391 3.0371 2.5413 -0.7479 -0.1878 -0.7490 175 LEU E C   
11115 O O   . LEU E 184 ? 3.2210 3.1182 2.5878 -0.7582 -0.2076 -0.7402 175 LEU E O   
11116 C CB  . LEU E 184 ? 3.1186 3.0505 2.5292 -0.7723 -0.1447 -0.7297 175 LEU E CB  
11117 C CG  . LEU E 184 ? 3.0793 3.0690 2.5209 -0.7823 -0.1194 -0.7276 175 LEU E CG  
11118 C CD1 . LEU E 184 ? 3.1213 3.0780 2.5284 -0.7980 -0.1042 -0.7078 175 LEU E CD1 
11119 C CD2 . LEU E 184 ? 2.9643 2.9880 2.4708 -0.7632 -0.1015 -0.7490 175 LEU E CD2 
11120 N N   . TYR E 185 ? 3.1462 2.9948 2.5557 -0.7293 -0.1866 -0.7589 176 TYR E N   
11121 C CA  . TYR E 185 ? 3.1964 2.9859 2.5728 -0.7188 -0.2092 -0.7612 176 TYR E CA  
11122 C C   . TYR E 185 ? 3.2807 3.0101 2.5997 -0.7314 -0.2099 -0.7415 176 TYR E C   
11123 O O   . TYR E 185 ? 3.2828 3.0031 2.5917 -0.7435 -0.1904 -0.7282 176 TYR E O   
11124 C CB  . TYR E 185 ? 3.1193 2.8813 2.5280 -0.6931 -0.2063 -0.7801 176 TYR E CB  
11125 C CG  . TYR E 185 ? 3.0428 2.8612 2.5055 -0.6814 -0.2048 -0.7988 176 TYR E CG  
11126 C CD1 . TYR E 185 ? 3.0617 2.8884 2.5248 -0.6724 -0.2283 -0.8093 176 TYR E CD1 
11127 C CD2 . TYR E 185 ? 2.9538 2.8202 2.4678 -0.6798 -0.1783 -0.8060 176 TYR E CD2 
11128 C CE1 . TYR E 185 ? 2.9939 2.8748 2.5064 -0.6632 -0.2247 -0.8258 176 TYR E CE1 
11129 C CE2 . TYR E 185 ? 2.8849 2.8081 2.4510 -0.6701 -0.1734 -0.8234 176 TYR E CE2 
11130 C CZ  . TYR E 185 ? 2.9048 2.8353 2.4700 -0.6623 -0.1962 -0.8330 176 TYR E CZ  
11131 O OH  . TYR E 185 ? 2.8367 2.8271 2.4555 -0.6533 -0.1893 -0.8504 176 TYR E OH  
11132 N N   . SER E 186 ? 3.2654 2.9544 2.5461 -0.7289 -0.2320 -0.7396 177 SER E N   
11133 C CA  . SER E 186 ? 3.3505 2.9775 2.5752 -0.7394 -0.2332 -0.7220 177 SER E CA  
11134 C C   . SER E 186 ? 3.3876 2.9661 2.5935 -0.7229 -0.2533 -0.7317 177 SER E C   
11135 O O   . SER E 186 ? 3.3919 2.9911 2.6088 -0.7145 -0.2713 -0.7462 177 SER E O   
11136 C CB  . SER E 186 ? 3.4501 3.0904 2.6287 -0.7685 -0.2367 -0.6979 177 SER E CB  
11137 O OG  . SER E 186 ? 3.5349 3.1133 2.6573 -0.7814 -0.2343 -0.6778 177 SER E OG  
11138 N N   . LEU E 187 ? 3.4612 2.9750 2.6353 -0.7218 -0.2475 -0.7239 178 LEU E N   
11139 C CA  . LEU E 187 ? 3.5442 3.0041 2.6775 -0.7223 -0.2583 -0.7292 178 LEU E CA  
11140 C C   . LEU E 187 ? 3.6248 3.0210 2.7001 -0.7380 -0.2496 -0.7057 178 LEU E C   
11141 O O   . LEU E 187 ? 3.6034 2.9962 2.6798 -0.7427 -0.2344 -0.6900 178 LEU E O   
11142 C CB  . LEU E 187 ? 3.4630 2.9050 2.6329 -0.6966 -0.2565 -0.7556 178 LEU E CB  
11143 C CG  . LEU E 187 ? 3.3908 2.8032 2.5901 -0.6786 -0.2365 -0.7599 178 LEU E CG  
11144 C CD1 . LEU E 187 ? 3.4679 2.8058 2.6199 -0.6836 -0.2278 -0.7473 178 LEU E CD1 
11145 C CD2 . LEU E 187 ? 3.3126 2.7330 2.5605 -0.6537 -0.2369 -0.7865 178 LEU E CD2 
11146 N N   . SER E 188 ? 3.8143 3.1576 2.8358 -0.7466 -0.2595 -0.7021 179 SER E N   
11147 C CA  . SER E 188 ? 3.8913 3.1603 2.8553 -0.7581 -0.2511 -0.6813 179 SER E CA  
11148 C C   . SER E 188 ? 3.8828 3.0961 2.8449 -0.7403 -0.2487 -0.6976 179 SER E C   
11149 O O   . SER E 188 ? 3.8707 3.0927 2.8498 -0.7280 -0.2604 -0.7202 179 SER E O   
11150 C CB  . SER E 188 ? 4.0632 3.3048 2.9512 -0.7874 -0.2642 -0.6550 179 SER E CB  
11151 O OG  . SER E 188 ? 4.0837 3.3634 2.9667 -0.8052 -0.2617 -0.6345 179 SER E OG  
11152 N N   . SER E 189 ? 3.7864 2.9419 2.7272 -0.7386 -0.2335 -0.6858 180 SER E N   
11153 C CA  . SER E 189 ? 3.8089 2.8984 2.7330 -0.7252 -0.2302 -0.6945 180 SER E CA  
11154 C C   . SER E 189 ? 3.9438 2.9567 2.7833 -0.7463 -0.2308 -0.6643 180 SER E C   
11155 O O   . SER E 189 ? 3.9645 2.9616 2.7813 -0.7584 -0.2201 -0.6406 180 SER E O   
11156 C CB  . SER E 189 ? 3.6968 2.7826 2.6752 -0.6999 -0.2108 -0.7078 180 SER E CB  
11157 O OG  . SER E 189 ? 3.7219 2.7442 2.6855 -0.6859 -0.2068 -0.7159 180 SER E OG  
11158 N N   . VAL E 190 ? 3.8845 2.8477 2.6755 -0.7502 -0.2441 -0.6641 181 VAL E N   
11159 C CA  . VAL E 190 ? 4.0275 2.9098 2.7310 -0.7697 -0.2483 -0.6337 181 VAL E CA  
11160 C C   . VAL E 190 ? 4.0580 2.8673 2.7434 -0.7525 -0.2444 -0.6417 181 VAL E C   
11161 O O   . VAL E 190 ? 3.9875 2.8112 2.7213 -0.7289 -0.2430 -0.6716 181 VAL E O   
11162 C CB  . VAL E 190 ? 4.1518 3.0324 2.7971 -0.7948 -0.2713 -0.6175 181 VAL E CB  
11163 C CG1 . VAL E 190 ? 4.1274 3.0808 2.7919 -0.8111 -0.2738 -0.6084 181 VAL E CG1 
11164 C CG2 . VAL E 190 ? 4.2696 3.1595 2.9243 -0.7840 -0.2878 -0.6419 181 VAL E CG2 
11165 N N   . VAL E 191 ? 4.2713 3.0003 2.8857 -0.7640 -0.2425 -0.6138 182 VAL E N   
11166 C CA  . VAL E 191 ? 4.3243 2.9735 2.9081 -0.7497 -0.2399 -0.6153 182 VAL E CA  
11167 C C   . VAL E 191 ? 4.4970 3.0657 2.9802 -0.7727 -0.2530 -0.5802 182 VAL E C   
11168 O O   . VAL E 191 ? 4.5541 3.1184 2.9989 -0.7957 -0.2539 -0.5520 182 VAL E O   
11169 C CB  . VAL E 191 ? 4.2397 2.8734 2.8621 -0.7286 -0.2155 -0.6204 182 VAL E CB  
11170 C CG1 . VAL E 191 ? 4.2600 2.8841 2.8564 -0.7449 -0.2049 -0.5912 182 VAL E CG1 
11171 C CG2 . VAL E 191 ? 4.2949 2.8474 2.8876 -0.7120 -0.2123 -0.6218 182 VAL E CG2 
11172 N N   . THR E 192 ? 4.4089 2.9129 2.8486 -0.7664 -0.2642 -0.5812 183 THR E N   
11173 C CA  . THR E 192 ? 4.5788 2.9949 2.9205 -0.7847 -0.2773 -0.5472 183 THR E CA  
11174 C C   . THR E 192 ? 4.6085 2.9455 2.9265 -0.7684 -0.2637 -0.5393 183 THR E C   
11175 O O   . THR E 192 ? 4.5446 2.8747 2.9044 -0.7410 -0.2536 -0.5637 183 THR E O   
11176 C CB  . THR E 192 ? 4.6816 3.0734 2.9795 -0.7905 -0.3028 -0.5490 183 THR E CB  
11177 O OG1 . THR E 192 ? 4.6317 3.0261 2.9729 -0.7625 -0.3008 -0.5820 183 THR E OG1 
11178 C CG2 . THR E 192 ? 4.6978 3.1642 3.0076 -0.8103 -0.3178 -0.5499 183 THR E CG2 
11179 N N   . VAL E 193 ? 4.7550 3.0336 3.0064 -0.7849 -0.2635 -0.5048 184 VAL E N   
11180 C CA  . VAL E 193 ? 4.7841 2.9930 3.0123 -0.7710 -0.2493 -0.4936 184 VAL E CA  
11181 C C   . VAL E 193 ? 4.9681 3.0876 3.0923 -0.7907 -0.2644 -0.4558 184 VAL E C   
11182 O O   . VAL E 193 ? 5.0577 3.1784 3.1348 -0.8182 -0.2815 -0.4352 184 VAL E O   
11183 C CB  . VAL E 193 ? 4.6702 2.9180 2.9472 -0.7661 -0.2250 -0.4933 184 VAL E CB  
11184 C CG1 . VAL E 193 ? 4.4892 2.8217 2.8697 -0.7448 -0.2107 -0.5301 184 VAL E CG1 
11185 C CG2 . VAL E 193 ? 4.7092 2.9798 2.9568 -0.7959 -0.2285 -0.4669 184 VAL E CG2 
11186 N N   . PRO E 194 ? 5.0530 3.0938 3.1400 -0.7766 -0.2588 -0.4456 185 PRO E N   
11187 C CA  . PRO E 194 ? 5.2372 3.1904 3.2246 -0.7942 -0.2725 -0.4083 185 PRO E CA  
11188 C C   . PRO E 194 ? 5.2524 3.2170 3.2152 -0.8189 -0.2677 -0.3809 185 PRO E C   
11189 O O   . PRO E 194 ? 5.1476 3.1548 3.1599 -0.8129 -0.2467 -0.3863 185 PRO E O   
11190 C CB  . PRO E 194 ? 5.2696 3.1518 3.2420 -0.7680 -0.2622 -0.4085 185 PRO E CB  
11191 C CG  . PRO E 194 ? 5.1500 3.0736 3.2038 -0.7382 -0.2505 -0.4470 185 PRO E CG  
11192 C CD  . PRO E 194 ? 4.9838 3.0106 3.1169 -0.7428 -0.2416 -0.4680 185 PRO E CD  
11193 N N   . SER E 195 ? 5.2339 3.1598 3.1193 -0.8470 -0.2880 -0.3509 186 SER E N   
11194 C CA  . SER E 195 ? 5.2804 3.2087 3.1336 -0.8721 -0.2852 -0.3221 186 SER E CA  
11195 C C   . SER E 195 ? 5.2966 3.1748 3.1278 -0.8624 -0.2692 -0.3073 186 SER E C   
11196 O O   . SER E 195 ? 5.2785 3.1834 3.1190 -0.8727 -0.2567 -0.2956 186 SER E O   
11197 C CB  . SER E 195 ? 5.5035 3.3892 3.2731 -0.9028 -0.3110 -0.2915 186 SER E CB  
11198 O OG  . SER E 195 ? 5.5249 3.4659 3.3181 -0.9129 -0.3253 -0.3043 186 SER E OG  
11199 N N   . SER E 196 ? 5.3273 3.1331 3.1277 -0.8423 -0.2699 -0.3072 187 SER E N   
11200 C CA  . SER E 196 ? 5.3400 3.1019 3.1240 -0.8298 -0.2542 -0.2957 187 SER E CA  
11201 C C   . SER E 196 ? 5.1610 2.9896 3.0315 -0.8119 -0.2266 -0.3169 187 SER E C   
11202 O O   . SER E 196 ? 5.1585 2.9700 3.0201 -0.8083 -0.2127 -0.3044 187 SER E O   
11203 C CB  . SER E 196 ? 5.4176 3.1000 3.1660 -0.8070 -0.2590 -0.2971 187 SER E CB  
11204 O OG  . SER E 196 ? 5.3066 3.0195 3.1225 -0.7801 -0.2516 -0.3315 187 SER E OG  
11205 N N   . SER E 197 ? 5.2560 3.1596 3.2091 -0.8002 -0.2191 -0.3486 188 SER E N   
11206 C CA  . SER E 197 ? 5.0771 3.0446 3.1159 -0.7817 -0.1942 -0.3701 188 SER E CA  
11207 C C   . SER E 197 ? 5.0119 3.0475 3.0800 -0.8000 -0.1864 -0.3644 188 SER E C   
11208 O O   . SER E 197 ? 4.8869 2.9696 3.0184 -0.7861 -0.1661 -0.3776 188 SER E O   
11209 C CB  . SER E 197 ? 4.9557 2.9717 3.0726 -0.7585 -0.1895 -0.4080 188 SER E CB  
11210 O OG  . SER E 197 ? 4.9181 3.0006 3.0651 -0.7727 -0.1995 -0.4200 188 SER E OG  
11211 N N   . LEU E 198 ? 4.9624 3.0056 2.9884 -0.8299 -0.2018 -0.3450 189 LEU E N   
11212 C CA  . LEU E 198 ? 4.8975 3.0074 2.9533 -0.8464 -0.1941 -0.3398 189 LEU E CA  
11213 C C   . LEU E 198 ? 4.9116 2.9977 2.9470 -0.8476 -0.1794 -0.3198 189 LEU E C   
11214 O O   . LEU E 198 ? 5.0516 3.0641 3.0100 -0.8573 -0.1864 -0.2926 189 LEU E O   
11215 C CB  . LEU E 198 ? 4.9945 3.1136 3.0060 -0.8785 -0.2140 -0.3210 189 LEU E CB  
11216 C CG  . LEU E 198 ? 4.9864 3.1389 3.0164 -0.8813 -0.2305 -0.3387 189 LEU E CG  
11217 C CD1 . LEU E 198 ? 5.0971 3.2541 3.0772 -0.9147 -0.2496 -0.3151 189 LEU E CD1 
11218 C CD2 . LEU E 198 ? 4.8068 3.0526 2.9372 -0.8641 -0.2182 -0.3743 189 LEU E CD2 
11219 N N   . GLY E 199 ? 4.7611 2.9102 2.8654 -0.8373 -0.1597 -0.3333 190 GLY E N   
11220 C CA  . GLY E 199 ? 4.7824 2.9202 2.8783 -0.8362 -0.1443 -0.3181 190 GLY E CA  
11221 C C   . GLY E 199 ? 4.7768 2.8785 2.8872 -0.8078 -0.1298 -0.3269 190 GLY E C   
11222 O O   . GLY E 199 ? 4.8398 2.9535 2.9703 -0.8014 -0.1117 -0.3258 190 GLY E O   
11223 N N   . THR E 200 ? 4.8120 2.8624 2.9025 -0.7936 -0.1372 -0.3340 191 THR E N   
11224 C CA  . THR E 200 ? 4.7767 2.7927 2.8831 -0.7651 -0.1240 -0.3434 191 THR E CA  
11225 C C   . THR E 200 ? 4.6117 2.6890 2.8159 -0.7388 -0.1098 -0.3790 191 THR E C   
11226 O O   . THR E 200 ? 4.5692 2.6572 2.8165 -0.7180 -0.0915 -0.3880 191 THR E O   
11227 C CB  . THR E 200 ? 4.9209 2.8522 2.9606 -0.7608 -0.1385 -0.3340 191 THR E CB  
11228 O OG1 . THR E 200 ? 5.0900 2.9606 3.0379 -0.7835 -0.1511 -0.2996 191 THR E OG1 
11229 C CG2 . THR E 200 ? 4.8838 2.7840 2.9459 -0.7294 -0.1244 -0.3455 191 THR E CG2 
11230 N N   . GLN E 201 ? 4.7610 2.8804 3.0013 -0.7398 -0.1187 -0.3993 192 GLN E N   
11231 C CA  . GLN E 201 ? 4.6041 2.7879 2.9382 -0.7172 -0.1078 -0.4339 192 GLN E CA  
11232 C C   . GLN E 201 ? 4.4941 2.7627 2.8785 -0.7293 -0.1057 -0.4420 192 GLN E C   
11233 O O   . GLN E 201 ? 4.5485 2.8331 2.9054 -0.7527 -0.1205 -0.4335 192 GLN E O   
11234 C CB  . GLN E 201 ? 4.6127 2.7830 2.9527 -0.7068 -0.1199 -0.4533 192 GLN E CB  
11235 C CG  . GLN E 201 ? 4.4583 2.6976 2.8928 -0.6857 -0.1124 -0.4903 192 GLN E CG  
11236 C CD  . GLN E 201 ? 4.3685 2.6140 2.8614 -0.6559 -0.0916 -0.5054 192 GLN E CD  
11237 O OE1 . GLN E 201 ? 4.4366 2.6224 2.9049 -0.6410 -0.0876 -0.5010 192 GLN E OE1 
11238 N NE2 . GLN E 201 ? 4.2213 2.5397 2.7927 -0.6464 -0.0792 -0.5232 192 GLN E NE2 
11239 N N   . THR E 202 ? 4.4296 2.7485 2.8823 -0.7146 -0.0873 -0.4570 193 THR E N   
11240 C CA  . THR E 202 ? 4.3426 2.7357 2.8390 -0.7258 -0.0828 -0.4658 193 THR E CA  
11241 C C   . THR E 202 ? 4.2461 2.7000 2.8109 -0.7127 -0.0917 -0.4970 193 THR E C   
11242 O O   . THR E 202 ? 4.2012 2.6511 2.8048 -0.6882 -0.0897 -0.5192 193 THR E O   
11243 C CB  . THR E 202 ? 4.2548 2.6647 2.7827 -0.7188 -0.0588 -0.4687 193 THR E CB  
11244 O OG1 . THR E 202 ? 4.3672 2.7277 2.8291 -0.7343 -0.0517 -0.4387 193 THR E OG1 
11245 C CG2 . THR E 202 ? 4.1703 2.6599 2.7525 -0.7262 -0.0533 -0.4815 193 THR E CG2 
11246 N N   . TYR E 203 ? 4.1987 2.7072 2.7744 -0.7301 -0.1013 -0.4982 194 TYR E N   
11247 C CA  . TYR E 203 ? 4.1254 2.6938 2.7578 -0.7222 -0.1103 -0.5261 194 TYR E CA  
11248 C C   . TYR E 203 ? 4.0189 2.6640 2.7076 -0.7254 -0.1010 -0.5363 194 TYR E C   
11249 O O   . TYR E 203 ? 4.0573 2.7195 2.7183 -0.7499 -0.1008 -0.5176 194 TYR E O   
11250 C CB  . TYR E 203 ? 4.2284 2.7835 2.8076 -0.7444 -0.1321 -0.5179 194 TYR E CB  
11251 C CG  . TYR E 203 ? 4.3541 2.8269 2.8694 -0.7439 -0.1423 -0.5098 194 TYR E CG  
11252 C CD1 . TYR E 203 ? 4.3186 2.7788 2.8632 -0.7205 -0.1426 -0.5344 194 TYR E CD1 
11253 C CD2 . TYR E 203 ? 4.5074 2.9142 2.9328 -0.7662 -0.1525 -0.4772 194 TYR E CD2 
11254 C CE1 . TYR E 203 ? 4.4325 2.8165 2.9189 -0.7184 -0.1522 -0.5271 194 TYR E CE1 
11255 C CE2 . TYR E 203 ? 4.6243 2.9529 2.9893 -0.7644 -0.1633 -0.4689 194 TYR E CE2 
11256 C CZ  . TYR E 203 ? 4.5806 2.8983 2.9767 -0.7401 -0.1629 -0.4941 194 TYR E CZ  
11257 O OH  . TYR E 203 ? 4.7036 2.9424 3.0397 -0.7367 -0.1737 -0.4858 194 TYR E OH  
11258 N N   . ILE E 204 ? 3.9308 2.6172 2.6929 -0.7022 -0.0929 -0.5647 195 ILE E N   
11259 C CA  . ILE E 204 ? 3.8235 2.5783 2.6409 -0.7026 -0.0828 -0.5769 195 ILE E CA  
11260 C C   . ILE E 204 ? 3.7752 2.5845 2.6576 -0.6847 -0.0940 -0.6083 195 ILE E C   
11261 O O   . ILE E 204 ? 3.7741 2.5693 2.6873 -0.6599 -0.0952 -0.6277 195 ILE E O   
11262 C CB  . ILE E 204 ? 3.7926 2.5389 2.6346 -0.6906 -0.0588 -0.5783 195 ILE E CB  
11263 C CG1 . ILE E 204 ? 3.8402 2.5336 2.6155 -0.7083 -0.0485 -0.5470 195 ILE E CG1 
11264 C CG2 . ILE E 204 ? 3.7278 2.5454 2.6306 -0.6887 -0.0489 -0.5927 195 ILE E CG2 
11265 C CD1 . ILE E 204 ? 3.8222 2.4949 2.6121 -0.6949 -0.0258 -0.5466 195 ILE E CD1 
11266 N N   . CYS E 205 ? 4.0356 2.9065 2.9382 -0.6966 -0.1023 -0.6130 196 CYS E N   
11267 C CA  . CYS E 205 ? 3.9506 2.8790 2.9181 -0.6793 -0.1116 -0.6425 196 CYS E CA  
11268 C C   . CYS E 205 ? 3.8293 2.8039 2.8558 -0.6696 -0.0946 -0.6550 196 CYS E C   
11269 O O   . CYS E 205 ? 3.8284 2.8222 2.8474 -0.6862 -0.0819 -0.6409 196 CYS E O   
11270 C CB  . CYS E 205 ? 4.0068 2.9776 2.9644 -0.6957 -0.1313 -0.6415 196 CYS E CB  
11271 S SG  . CYS E 205 ? 4.0196 3.0453 2.9713 -0.7243 -0.1248 -0.6247 196 CYS E SG  
11272 N N   . ASN E 206 ? 3.7744 2.7652 2.8578 -0.6428 -0.0945 -0.6806 197 ASN E N   
11273 C CA  . ASN E 206 ? 3.6646 2.6944 2.8050 -0.6306 -0.0788 -0.6931 197 ASN E CA  
11274 C C   . ASN E 206 ? 3.6012 2.6955 2.7888 -0.6248 -0.0916 -0.7129 197 ASN E C   
11275 O O   . ASN E 206 ? 3.5890 2.6840 2.7964 -0.6074 -0.1073 -0.7311 197 ASN E O   
11276 C CB  . ASN E 206 ? 3.6188 2.6130 2.7847 -0.6045 -0.0670 -0.7040 197 ASN E CB  
11277 C CG  . ASN E 206 ? 3.7018 2.6236 2.8161 -0.6059 -0.0622 -0.6878 197 ASN E CG  
11278 O OD1 . ASN E 206 ? 3.7392 2.6245 2.8445 -0.5924 -0.0721 -0.6950 197 ASN E OD1 
11279 N ND2 . ASN E 206 ? 3.7322 2.6321 2.8106 -0.6223 -0.0466 -0.6653 197 ASN E ND2 
11280 N N   . VAL E 207 ? 3.7571 2.9045 2.9610 -0.6392 -0.0848 -0.7087 198 VAL E N   
11281 C CA  . VAL E 207 ? 3.7075 2.9187 2.9482 -0.6388 -0.0962 -0.7229 198 VAL E CA  
11282 C C   . VAL E 207 ? 3.6099 2.8627 2.9042 -0.6307 -0.0769 -0.7320 198 VAL E C   
11283 O O   . VAL E 207 ? 3.6168 2.8857 2.9092 -0.6446 -0.0588 -0.7196 198 VAL E O   
11284 C CB  . VAL E 207 ? 3.7779 3.0199 2.9869 -0.6660 -0.1057 -0.7082 198 VAL E CB  
11285 C CG1 . VAL E 207 ? 3.7435 3.0525 2.9917 -0.6644 -0.1173 -0.7230 198 VAL E CG1 
11286 C CG2 . VAL E 207 ? 3.9228 3.1192 3.0719 -0.6771 -0.1218 -0.6950 198 VAL E CG2 
11287 N N   . ASN E 208 ? 3.6995 2.9689 3.0397 -0.6089 -0.0796 -0.7527 199 ASN E N   
11288 C CA  . ASN E 208 ? 3.6079 2.9184 3.0009 -0.6008 -0.0600 -0.7622 199 ASN E CA  
11289 C C   . ASN E 208 ? 3.5600 2.9361 2.9877 -0.6027 -0.0685 -0.7746 199 ASN E C   
11290 O O   . ASN E 208 ? 3.5910 2.9688 3.0157 -0.5965 -0.0906 -0.7842 199 ASN E O   
11291 C CB  . ASN E 208 ? 3.5923 2.8688 3.0101 -0.5750 -0.0509 -0.7739 199 ASN E CB  
11292 C CG  . ASN E 208 ? 3.6782 2.8927 3.0650 -0.5723 -0.0399 -0.7614 199 ASN E CG  
11293 O OD1 . ASN E 208 ? 3.7373 2.9369 3.0860 -0.5910 -0.0353 -0.7432 199 ASN E OD1 
11294 N ND2 . ASN E 208 ? 3.6948 2.8730 3.0961 -0.5496 -0.0346 -0.7702 199 ASN E ND2 
11295 N N   . HIS E 209 ? 3.3116 2.7431 2.7729 -0.6113 -0.0499 -0.7745 200 HIS E N   
11296 C CA  . HIS E 209 ? 3.2743 2.7755 2.7750 -0.6138 -0.0520 -0.7861 200 HIS E CA  
11297 C C   . HIS E 209 ? 3.2238 2.7646 2.7824 -0.6049 -0.0239 -0.7963 200 HIS E C   
11298 O O   . HIS E 209 ? 3.1976 2.7619 2.7667 -0.6151 -0.0032 -0.7885 200 HIS E O   
11299 C CB  . HIS E 209 ? 3.2691 2.8102 2.7507 -0.6380 -0.0572 -0.7742 200 HIS E CB  
11300 C CG  . HIS E 209 ? 3.2350 2.8477 2.7536 -0.6411 -0.0610 -0.7854 200 HIS E CG  
11301 N ND1 . HIS E 209 ? 3.1903 2.8664 2.7412 -0.6518 -0.0424 -0.7849 200 HIS E ND1 
11302 C CD2 . HIS E 209 ? 3.2389 2.8713 2.7679 -0.6344 -0.0804 -0.7976 200 HIS E CD2 
11303 C CE1 . HIS E 209 ? 3.1675 2.9008 2.7485 -0.6517 -0.0493 -0.7965 200 HIS E CE1 
11304 N NE2 . HIS E 209 ? 3.1964 2.9045 2.7643 -0.6416 -0.0725 -0.8040 200 HIS E NE2 
11305 N N   . LYS E 210 ? 3.3488 2.8984 2.9452 -0.5863 -0.0219 -0.8136 201 LYS E N   
11306 C CA  . LYS E 210 ? 3.2568 2.8424 2.9119 -0.5761 0.0072  -0.8243 201 LYS E CA  
11307 C C   . LYS E 210 ? 3.2002 2.8706 2.9022 -0.5864 0.0233  -0.8299 201 LYS E C   
11308 O O   . LYS E 210 ? 3.1453 2.8415 2.8822 -0.5856 0.0503  -0.8307 201 LYS E O   
11309 C CB  . LYS E 210 ? 3.2155 2.7930 2.9015 -0.5541 0.0073  -0.8417 201 LYS E CB  
11310 C CG  . LYS E 210 ? 3.1267 2.7335 2.8728 -0.5420 0.0401  -0.8517 201 LYS E CG  
11311 C CD  . LYS E 210 ? 3.1068 2.7092 2.8872 -0.5204 0.0436  -0.8687 201 LYS E CD  
11312 C CE  . LYS E 210 ? 3.0964 2.7186 2.9322 -0.5084 0.0772  -0.8756 201 LYS E CE  
11313 N NZ  . LYS E 210 ? 3.0140 2.7280 2.9232 -0.5099 0.0979  -0.8898 201 LYS E NZ  
11314 N N   . PRO E 211 ? 3.1212 2.8393 2.8292 -0.5950 0.0090  -0.8346 202 PRO E N   
11315 C CA  . PRO E 211 ? 3.0663 2.8677 2.8234 -0.6028 0.0270  -0.8410 202 PRO E CA  
11316 C C   . PRO E 211 ? 3.0790 2.8875 2.8232 -0.6181 0.0427  -0.8262 202 PRO E C   
11317 O O   . PRO E 211 ? 3.0181 2.8784 2.8100 -0.6176 0.0681  -0.8323 202 PRO E O   
11318 C CB  . PRO E 211 ? 3.1025 2.9396 2.8508 -0.6115 0.0041  -0.8439 202 PRO E CB  
11319 C CG  . PRO E 211 ? 3.1358 2.9242 2.8602 -0.5995 -0.0193 -0.8491 202 PRO E CG  
11320 C CD  . PRO E 211 ? 3.1762 2.8817 2.8559 -0.5952 -0.0218 -0.8372 202 PRO E CD  
11321 N N   . SER E 212 ? 3.2800 3.0396 2.9623 -0.6315 0.0292  -0.8072 203 SER E N   
11322 C CA  . SER E 212 ? 3.2943 3.0567 2.9610 -0.6463 0.0449  -0.7921 203 SER E CA  
11323 C C   . SER E 212 ? 3.3149 3.0175 2.9660 -0.6386 0.0575  -0.7848 203 SER E C   
11324 O O   . SER E 212 ? 3.3410 3.0375 2.9777 -0.6489 0.0723  -0.7720 203 SER E O   
11325 C CB  . SER E 212 ? 3.3919 3.1449 3.0034 -0.6678 0.0270  -0.7746 203 SER E CB  
11326 O OG  . SER E 212 ? 3.4475 3.1323 3.0057 -0.6673 0.0051  -0.7658 203 SER E OG  
11327 N N   . ASN E 213 ? 3.4822 3.1426 3.1374 -0.6200 0.0529  -0.7932 204 ASN E N   
11328 C CA  . ASN E 213 ? 3.4902 3.0893 3.1287 -0.6104 0.0630  -0.7868 204 ASN E CA  
11329 C C   . ASN E 213 ? 3.6042 3.1509 3.1788 -0.6248 0.0554  -0.7653 204 ASN E C   
11330 O O   . ASN E 213 ? 3.6198 3.1571 3.1875 -0.6306 0.0738  -0.7547 204 ASN E O   
11331 C CB  . ASN E 213 ? 3.4355 3.0611 3.1240 -0.6020 0.0948  -0.7928 204 ASN E CB  
11332 C CG  . ASN E 213 ? 3.5038 3.0692 3.1868 -0.5851 0.1028  -0.7922 204 ASN E CG  
11333 O OD1 . ASN E 213 ? 3.5121 3.0476 3.1787 -0.5872 0.1172  -0.7806 204 ASN E OD1 
11334 N ND2 . ASN E 213 ? 3.5662 3.1107 3.2579 -0.5685 0.0918  -0.8040 204 ASN E ND2 
11335 N N   . THR E 214 ? 3.4222 2.9464 2.9521 -0.6339 0.0300  -0.7583 205 THR E N   
11336 C CA  . THR E 214 ? 3.5227 3.0005 2.9925 -0.6490 0.0244  -0.7377 205 THR E CA  
11337 C C   . THR E 214 ? 3.5530 2.9612 2.9867 -0.6381 0.0074  -0.7364 205 THR E C   
11338 O O   . THR E 214 ? 3.5395 2.9427 2.9835 -0.6248 -0.0093 -0.7498 205 THR E O   
11339 C CB  . THR E 214 ? 3.5702 3.0780 3.0119 -0.6723 0.0120  -0.7267 205 THR E CB  
11340 O OG1 . THR E 214 ? 3.5816 3.1080 3.0281 -0.6690 -0.0111 -0.7373 205 THR E OG1 
11341 C CG2 . THR E 214 ? 3.5456 3.1175 3.0170 -0.6845 0.0312  -0.7251 205 THR E CG2 
11342 N N   . LYS E 215 ? 3.7432 3.0980 3.1346 -0.6436 0.0132  -0.7203 206 LYS E N   
11343 C CA  . LYS E 215 ? 3.8133 3.0998 3.1641 -0.6364 0.0003  -0.7157 206 LYS E CA  
11344 C C   . LYS E 215 ? 3.9166 3.1734 3.2060 -0.6594 -0.0023 -0.6921 206 LYS E C   
11345 O O   . LYS E 215 ? 3.9433 3.2082 3.2228 -0.6730 0.0146  -0.6786 206 LYS E O   
11346 C CB  . LYS E 215 ? 3.8008 3.0444 3.1631 -0.6171 0.0161  -0.7186 206 LYS E CB  
11347 C CG  . LYS E 215 ? 3.7459 3.0092 3.1647 -0.5937 0.0224  -0.7393 206 LYS E CG  
11348 C CD  . LYS E 215 ? 3.7485 2.9647 3.1707 -0.5767 0.0385  -0.7384 206 LYS E CD  
11349 C CE  . LYS E 215 ? 3.7138 2.9431 3.1877 -0.5530 0.0454  -0.7576 206 LYS E CE  
11350 N NZ  . LYS E 215 ? 3.6970 2.9965 3.2243 -0.5558 0.0621  -0.7666 206 LYS E NZ  
11351 N N   . VAL E 216 ? 3.6167 2.8491 2.8661 -0.6666 -0.0235 -0.6868 207 VAL E N   
11352 C CA  . VAL E 216 ? 3.7177 2.9193 2.9036 -0.6903 -0.0263 -0.6623 207 VAL E CA  
11353 C C   . VAL E 216 ? 3.7924 2.9234 2.9343 -0.6848 -0.0357 -0.6559 207 VAL E C   
11354 O O   . VAL E 216 ? 3.7935 2.9136 2.9455 -0.6697 -0.0516 -0.6704 207 VAL E O   
11355 C CB  . VAL E 216 ? 3.7634 3.0068 2.9337 -0.7114 -0.0408 -0.6561 207 VAL E CB  
11356 C CG1 . VAL E 216 ? 3.8781 3.0828 2.9776 -0.7361 -0.0445 -0.6288 207 VAL E CG1 
11357 C CG2 . VAL E 216 ? 3.6998 3.0098 2.9090 -0.7185 -0.0280 -0.6595 207 VAL E CG2 
11358 N N   . ASP E 217 ? 3.9091 2.9920 3.0020 -0.6965 -0.0254 -0.6341 208 ASP E N   
11359 C CA  . ASP E 217 ? 3.9957 3.0082 3.0354 -0.6964 -0.0324 -0.6221 208 ASP E CA  
11360 C C   . ASP E 217 ? 4.1022 3.0976 3.0756 -0.7262 -0.0382 -0.5947 208 ASP E C   
11361 O O   . ASP E 217 ? 4.1068 3.1179 3.0678 -0.7431 -0.0257 -0.5799 208 ASP E O   
11362 C CB  . ASP E 217 ? 3.9922 2.9548 3.0269 -0.6828 -0.0146 -0.6182 208 ASP E CB  
11363 C CG  . ASP E 217 ? 3.8919 2.8667 2.9892 -0.6533 -0.0084 -0.6432 208 ASP E CG  
11364 O OD1 . ASP E 217 ? 3.8685 2.8467 2.9893 -0.6372 -0.0233 -0.6614 208 ASP E OD1 
11365 O OD2 . ASP E 217 ? 3.8422 2.8211 2.9633 -0.6461 0.0118  -0.6437 208 ASP E OD2 
11366 N N   . LYS E 218 ? 3.8046 2.7870 2.7454 -0.7344 -0.0587 -0.5904 209 LYS E N   
11367 C CA  . LYS E 218 ? 3.9136 2.8799 2.7900 -0.7636 -0.0654 -0.5629 209 LYS E CA  
11368 C C   . LYS E 218 ? 4.0247 2.9143 2.8369 -0.7668 -0.0740 -0.5461 209 LYS E C   
11369 O O   . LYS E 218 ? 4.0450 2.9184 2.8565 -0.7559 -0.0896 -0.5566 209 LYS E O   
11370 C CB  . LYS E 218 ? 3.9192 2.9408 2.8047 -0.7766 -0.0817 -0.5666 209 LYS E CB  
11371 C CG  . LYS E 218 ? 4.0226 3.0386 2.8491 -0.8085 -0.0853 -0.5373 209 LYS E CG  
11372 C CD  . LYS E 218 ? 3.9931 3.0379 2.8295 -0.8202 -0.0652 -0.5280 209 LYS E CD  
11373 C CE  . LYS E 218 ? 4.1144 3.1682 2.9033 -0.8515 -0.0691 -0.5020 209 LYS E CE  
11374 N NZ  . LYS E 218 ? 4.0961 3.1916 2.9063 -0.8608 -0.0503 -0.4981 209 LYS E NZ  
11375 N N   . LYS E 219 ? 3.8783 2.7200 2.6358 -0.7812 -0.0641 -0.5199 210 LYS E N   
11376 C CA  . LYS E 219 ? 3.9959 2.7630 2.6858 -0.7867 -0.0728 -0.5004 210 LYS E CA  
11377 C C   . LYS E 219 ? 4.1017 2.8675 2.7427 -0.8111 -0.0923 -0.4827 210 LYS E C   
11378 O O   . LYS E 219 ? 4.1261 2.9250 2.7552 -0.8334 -0.0917 -0.4694 210 LYS E O   
11379 C CB  . LYS E 219 ? 4.0410 2.7565 2.6869 -0.7933 -0.0564 -0.4777 210 LYS E CB  
11380 C CG  . LYS E 219 ? 4.1625 2.7962 2.7379 -0.7965 -0.0642 -0.4572 210 LYS E CG  
11381 C CD  . LYS E 219 ? 4.1960 2.7798 2.7328 -0.7989 -0.0474 -0.4376 210 LYS E CD  
11382 C CE  . LYS E 219 ? 4.3339 2.8365 2.7921 -0.8058 -0.0572 -0.4133 210 LYS E CE  
11383 N NZ  . LYS E 219 ? 4.3707 2.8231 2.7885 -0.8070 -0.0418 -0.3943 210 LYS E NZ  
11384 N N   . VAL E 220 ? 4.0084 2.7365 2.6217 -0.8067 -0.1094 -0.4825 211 VAL E N   
11385 C CA  . VAL E 220 ? 4.1120 2.8365 2.6807 -0.8271 -0.1301 -0.4675 211 VAL E CA  
11386 C C   . VAL E 220 ? 4.2472 2.8870 2.7363 -0.8369 -0.1358 -0.4399 211 VAL E C   
11387 O O   . VAL E 220 ? 4.2622 2.8538 2.7429 -0.8189 -0.1384 -0.4460 211 VAL E O   
11388 C CB  . VAL E 220 ? 4.0799 2.8390 2.6864 -0.8134 -0.1476 -0.4924 211 VAL E CB  
11389 C CG1 . VAL E 220 ? 4.1976 2.9528 2.7518 -0.8388 -0.1676 -0.4749 211 VAL E CG1 
11390 C CG2 . VAL E 220 ? 3.9433 2.7830 2.6297 -0.8010 -0.1416 -0.5204 211 VAL E CG2 
11391 N N   . GLU E 221 ? 4.2360 2.8570 2.6671 -0.8647 -0.1379 -0.4096 212 GLU E N   
11392 C CA  . GLU E 221 ? 4.4040 2.9437 2.7559 -0.8758 -0.1422 -0.3803 212 GLU E CA  
11393 C C   . GLU E 221 ? 4.5225 3.0555 2.8191 -0.9051 -0.1597 -0.3550 212 GLU E C   
11394 O O   . GLU E 221 ? 4.4687 3.0621 2.7871 -0.9194 -0.1633 -0.3569 212 GLU E O   
11395 C CB  . GLU E 221 ? 4.4117 2.9223 2.7435 -0.8788 -0.1221 -0.3653 212 GLU E CB  
11396 C CG  . GLU E 221 ? 4.3419 2.9034 2.6879 -0.8969 -0.1104 -0.3582 212 GLU E CG  
11397 C CD  . GLU E 221 ? 4.3474 2.8917 2.6937 -0.8916 -0.0881 -0.3532 212 GLU E CD  
11398 O OE1 . GLU E 221 ? 4.3281 2.9244 2.7110 -0.8959 -0.0742 -0.3587 212 GLU E OE1 
11399 O OE2 . GLU E 221 ? 4.4434 2.9231 2.7545 -0.8820 -0.0845 -0.3446 212 GLU E OE2 
11400 N N   . PRO E 222 ? 4.4954 2.9527 2.7162 -0.9161 -0.1707 -0.3302 213 PRO E N   
11401 C CA  . PRO E 222 ? 4.6297 3.0700 2.7868 -0.9485 -0.1863 -0.3013 213 PRO E CA  
11402 C C   . PRO E 222 ? 4.6070 3.0841 2.7639 -0.9692 -0.1765 -0.2846 213 PRO E C   
11403 O O   . PRO E 222 ? 4.5923 3.0551 2.7433 -0.9692 -0.1591 -0.2773 213 PRO E O   
11404 C CB  . PRO E 222 ? 4.7765 3.1149 2.8462 -0.9556 -0.1943 -0.2758 213 PRO E CB  
11405 C CG  . PRO E 222 ? 4.7305 3.0373 2.8192 -0.9269 -0.1899 -0.2973 213 PRO E CG  
11406 C CD  . PRO E 222 ? 4.5513 2.9274 2.7323 -0.9025 -0.1701 -0.3266 213 PRO E CD  
11407 N N   . LYS E 223 ? 4.7442 3.2636 2.8991 -0.9903 -0.1874 -0.2772 214 LYS E N   
11408 C CA  . LYS E 223 ? 4.7289 3.2844 2.8793 -1.0148 -0.1784 -0.2612 214 LYS E CA  
11409 C C   . LYS E 223 ? 4.9220 3.4146 2.9904 -1.0410 -0.1821 -0.2227 214 LYS E C   
11410 O O   . LYS E 223 ? 5.0799 3.5153 3.0940 -1.0473 -0.1984 -0.2062 214 LYS E O   
11411 C CB  . LYS E 223 ? 4.6883 3.3174 2.8720 -1.0264 -0.1880 -0.2692 214 LYS E CB  
11412 C CG  . LYS E 223 ? 4.7334 3.4086 2.9213 -1.0501 -0.1777 -0.2560 214 LYS E CG  
11413 C CD  . LYS E 223 ? 4.7255 3.4704 2.9420 -1.0615 -0.1883 -0.2624 214 LYS E CD  
11414 C CE  . LYS E 223 ? 4.7303 3.5199 2.9504 -1.0852 -0.1770 -0.2485 214 LYS E CE  
11415 N NZ  . LYS E 223 ? 4.7598 3.6134 3.0004 -1.0989 -0.1877 -0.2509 214 LYS E NZ  
11416 N N   . ASP F 1   ? 3.9619 2.2669 1.7165 -0.9269 0.3318  -0.0916 1   ASP F N   
11417 C CA  . ASP F 1   ? 3.9252 2.1910 1.6516 -0.9062 0.3154  -0.0809 1   ASP F CA  
11418 C C   . ASP F 1   ? 3.9929 2.2457 1.6968 -0.8974 0.3102  -0.0600 1   ASP F C   
11419 O O   . ASP F 1   ? 4.0738 2.3402 1.7763 -0.9100 0.3196  -0.0523 1   ASP F O   
11420 C CB  . ASP F 1   ? 3.9784 2.2066 1.7232 -0.9035 0.3003  -0.0849 1   ASP F CB  
11421 C CG  . ASP F 1   ? 3.9203 2.1684 1.7113 -0.9101 0.3016  -0.1069 1   ASP F CG  
11422 O OD1 . ASP F 1   ? 3.8202 2.1103 1.6282 -0.9139 0.3132  -0.1196 1   ASP F OD1 
11423 O OD2 . ASP F 1   ? 3.9674 2.1889 1.7784 -0.9114 0.2905  -0.1117 1   ASP F OD2 
11424 N N   . ILE F 2   ? 4.1695 2.3991 1.8621 -0.8739 0.2945  -0.0517 2   ILE F N   
11425 C CA  . ILE F 2   ? 4.2354 2.4486 1.9111 -0.8621 0.2860  -0.0331 2   ILE F CA  
11426 C C   . ILE F 2   ? 4.3517 2.5070 2.0035 -0.8644 0.2751  -0.0240 2   ILE F C   
11427 O O   . ILE F 2   ? 4.3041 2.4303 1.9501 -0.8581 0.2659  -0.0299 2   ILE F O   
11428 C CB  . ILE F 2   ? 4.0986 2.3269 1.7798 -0.8342 0.2768  -0.0300 2   ILE F CB  
11429 C CG1 . ILE F 2   ? 3.9906 2.2761 1.6951 -0.8324 0.2872  -0.0368 2   ILE F CG1 
11430 C CG2 . ILE F 2   ? 4.1691 2.3734 1.8306 -0.8213 0.2663  -0.0115 2   ILE F CG2 
11431 C CD1 . ILE F 2   ? 3.8722 2.1751 1.5868 -0.8065 0.2796  -0.0361 2   ILE F CD1 
11432 N N   . GLN F 3   ? 4.1302 2.2687 1.7692 -0.8730 0.2756  -0.0095 3   GLN F N   
11433 C CA  . GLN F 3   ? 4.2347 2.3191 1.8545 -0.8753 0.2649  0.0009  3   GLN F CA  
11434 C C   . GLN F 3   ? 4.2190 2.2847 1.8237 -0.8520 0.2504  0.0142  3   GLN F C   
11435 O O   . GLN F 3   ? 4.2342 2.3237 1.8399 -0.8451 0.2527  0.0231  3   GLN F O   
11436 C CB  . GLN F 3   ? 4.3982 2.4737 2.0188 -0.9001 0.2747  0.0090  3   GLN F CB  
11437 C CG  . GLN F 3   ? 4.4319 2.5229 2.0883 -0.9204 0.2836  -0.0068 3   GLN F CG  
11438 C CD  . GLN F 3   ? 4.3873 2.5310 2.0573 -0.9316 0.3023  -0.0170 3   GLN F CD  
11439 O OE1 . GLN F 3   ? 4.4192 2.5860 2.0767 -0.9363 0.3132  -0.0080 3   GLN F OE1 
11440 N NE2 . GLN F 3   ? 4.3030 2.4698 2.0068 -0.9336 0.3041  -0.0377 3   GLN F NE2 
11441 N N   . LEU F 4   ? 4.3092 2.3319 1.9000 -0.8400 0.2356  0.0155  4   LEU F N   
11442 C CA  . LEU F 4   ? 4.2984 2.2957 1.8738 -0.8192 0.2212  0.0276  4   LEU F CA  
11443 C C   . LEU F 4   ? 4.4363 2.3875 1.9971 -0.8286 0.2142  0.0386  4   LEU F C   
11444 O O   . LEU F 4   ? 4.4698 2.3882 2.0285 -0.8383 0.2101  0.0342  4   LEU F O   
11445 C CB  . LEU F 4   ? 4.1476 2.1304 1.7196 -0.7968 0.2093  0.0207  4   LEU F CB  
11446 C CG  . LEU F 4   ? 3.9829 2.0079 1.5746 -0.7846 0.2143  0.0097  4   LEU F CG  
11447 C CD1 . LEU F 4   ? 3.8448 1.8489 1.4334 -0.7629 0.2023  0.0048  4   LEU F CD1 
11448 C CD2 . LEU F 4   ? 3.9651 2.0280 1.5658 -0.7757 0.2188  0.0174  4   LEU F CD2 
11449 N N   . THR F 5   ? 4.3549 2.3036 1.9089 -0.8255 0.2123  0.0532  5   THR F N   
11450 C CA  . THR F 5   ? 4.4805 2.3893 2.0251 -0.8330 0.2057  0.0649  5   THR F CA  
11451 C C   . THR F 5   ? 4.4538 2.3335 1.9818 -0.8102 0.1893  0.0739  5   THR F C   
11452 O O   . THR F 5   ? 4.4249 2.3240 1.9502 -0.7962 0.1886  0.0811  5   THR F O   
11453 C CB  . THR F 5   ? 4.6048 2.5333 2.1560 -0.8498 0.2178  0.0753  5   THR F CB  
11454 O OG1 . THR F 5   ? 4.6266 2.5840 2.1944 -0.8711 0.2342  0.0660  5   THR F OG1 
11455 C CG2 . THR F 5   ? 4.7311 2.6193 2.2785 -0.8576 0.2110  0.0870  5   THR F CG2 
11456 N N   . GLN F 6   ? 4.5711 2.4047 2.0899 -0.8063 0.1759  0.0732  6   GLN F N   
11457 C CA  . GLN F 6   ? 4.5500 2.3527 2.0527 -0.7852 0.1601  0.0804  6   GLN F CA  
11458 C C   . GLN F 6   ? 4.6749 2.4500 2.1743 -0.7925 0.1551  0.0940  6   GLN F C   
11459 O O   . GLN F 6   ? 4.7632 2.5252 2.2737 -0.8116 0.1579  0.0940  6   GLN F O   
11460 C CB  . GLN F 6   ? 4.4665 2.2362 1.9605 -0.7726 0.1471  0.0704  6   GLN F CB  
11461 C CG  . GLN F 6   ? 4.3163 2.1118 1.8137 -0.7600 0.1503  0.0585  6   GLN F CG  
11462 C CD  . GLN F 6   ? 4.2230 1.9852 1.7098 -0.7455 0.1374  0.0499  6   GLN F CD  
11463 O OE1 . GLN F 6   ? 4.1548 1.9176 1.6463 -0.7508 0.1397  0.0384  6   GLN F OE1 
11464 N NE2 . GLN F 6   ? 4.2173 1.9501 1.6892 -0.7268 0.1239  0.0555  6   GLN F NE2 
11465 N N   . SER F 7   ? 4.6152 2.3827 2.1035 -0.7769 0.1476  0.1051  7   SER F N   
11466 C CA  . SER F 7   ? 4.7161 2.4562 2.2013 -0.7810 0.1414  0.1185  7   SER F CA  
11467 C C   . SER F 7   ? 4.6770 2.3883 2.1463 -0.7584 0.1256  0.1243  7   SER F C   
11468 O O   . SER F 7   ? 4.6020 2.3279 2.0646 -0.7403 0.1238  0.1237  7   SER F O   
11469 C CB  . SER F 7   ? 4.8037 2.5735 2.2956 -0.7928 0.1543  0.1308  7   SER F CB  
11470 O OG  . SER F 7   ? 4.7435 2.5456 2.2315 -0.7789 0.1577  0.1340  7   SER F OG  
11471 N N   . PRO F 8   ? 4.8826 2.5540 2.3491 -0.7591 0.1141  0.1293  8   PRO F N   
11472 C CA  . PRO F 8   ? 4.9603 2.6124 2.4419 -0.7783 0.1138  0.1281  8   PRO F CA  
11473 C C   . PRO F 8   ? 4.9124 2.5501 2.4002 -0.7802 0.1086  0.1118  8   PRO F C   
11474 O O   . PRO F 8   ? 4.8212 2.4564 2.2962 -0.7646 0.1033  0.1031  8   PRO F O   
11475 C CB  . PRO F 8   ? 5.0006 2.6169 2.4784 -0.7710 0.1001  0.1383  8   PRO F CB  
11476 C CG  . PRO F 8   ? 4.9108 2.5135 2.3677 -0.7456 0.0884  0.1368  8   PRO F CG  
11477 C CD  . PRO F 8   ? 4.8597 2.5024 2.3115 -0.7390 0.0993  0.1356  8   PRO F CD  
11478 N N   . SER F 9   ? 4.9649 2.5948 2.4757 -0.7985 0.1099  0.1071  9   SER F N   
11479 C CA  . SER F 9   ? 4.9273 2.5431 2.4496 -0.7987 0.1021  0.0908  9   SER F CA  
11480 C C   . SER F 9   ? 4.8777 2.4539 2.3928 -0.7800 0.0808  0.0873  9   SER F C   
11481 O O   . SER F 9   ? 4.8038 2.3696 2.3157 -0.7693 0.0722  0.0747  9   SER F O   
11482 C CB  . SER F 9   ? 5.0114 2.6355 2.5694 -0.8219 0.1084  0.0844  9   SER F CB  
11483 O OG  . SER F 9   ? 5.0403 2.7018 2.6049 -0.8385 0.1282  0.0829  9   SER F OG  
11484 N N   . PHE F 10  ? 4.9791 2.5341 2.4924 -0.7754 0.0721  0.0980  10  PHE F N   
11485 C CA  . PHE F 10  ? 4.9191 2.4379 2.4259 -0.7573 0.0517  0.0950  10  PHE F CA  
11486 C C   . PHE F 10  ? 4.9218 2.4285 2.4072 -0.7449 0.0478  0.1098  10  PHE F C   
11487 O O   . PHE F 10  ? 4.9995 2.5091 2.4936 -0.7548 0.0524  0.1223  10  PHE F O   
11488 C CB  . PHE F 10  ? 4.9516 2.4550 2.4918 -0.7654 0.0411  0.0889  10  PHE F CB  
11489 C CG  . PHE F 10  ? 4.9474 2.4663 2.5158 -0.7757 0.0432  0.0727  10  PHE F CG  
11490 C CD1 . PHE F 10  ? 5.0424 2.5873 2.6381 -0.7989 0.0581  0.0720  10  PHE F CD1 
11491 C CD2 . PHE F 10  ? 4.8464 2.3563 2.4156 -0.7611 0.0303  0.0581  10  PHE F CD2 
11492 C CE1 . PHE F 10  ? 5.0456 2.6077 2.6713 -0.8075 0.0596  0.0559  10  PHE F CE1 
11493 C CE2 . PHE F 10  ? 4.8405 2.3688 2.4398 -0.7688 0.0313  0.0429  10  PHE F CE2 
11494 C CZ  . PHE F 10  ? 4.9471 2.5018 2.5758 -0.7920 0.0457  0.0414  10  PHE F CZ  
11495 N N   . LEU F 11  ? 4.9637 2.4580 2.4235 -0.7230 0.0396  0.1079  11  LEU F N   
11496 C CA  . LEU F 11  ? 4.9609 2.4469 2.4022 -0.7090 0.0357  0.1200  11  LEU F CA  
11497 C C   . LEU F 11  ? 4.9032 2.3503 2.3367 -0.6920 0.0161  0.1164  11  LEU F C   
11498 O O   . LEU F 11  ? 4.8178 2.2520 2.2419 -0.6792 0.0075  0.1043  11  LEU F O   
11499 C CB  . LEU F 11  ? 4.9095 2.4194 2.3325 -0.6965 0.0437  0.1204  11  LEU F CB  
11500 C CG  . LEU F 11  ? 4.9301 2.4483 2.3437 -0.6866 0.0454  0.1341  11  LEU F CG  
11501 C CD1 . LEU F 11  ? 4.9025 2.4614 2.3145 -0.6829 0.0584  0.1340  11  LEU F CD1 
11502 C CD2 . LEU F 11  ? 4.9013 2.3872 2.2984 -0.6645 0.0298  0.1342  11  LEU F CD2 
11503 N N   . SER F 12  ? 5.0093 2.4389 2.4471 -0.6916 0.0092  0.1270  12  SER F N   
11504 C CA  . SER F 12  ? 5.0489 2.4433 2.4797 -0.6750 -0.0092 0.1250  12  SER F CA  
11505 C C   . SER F 12  ? 5.0875 2.4768 2.4945 -0.6576 -0.0110 0.1338  12  SER F C   
11506 O O   . SER F 12  ? 5.1430 2.5481 2.5504 -0.6626 -0.0021 0.1472  12  SER F O   
11507 C CB  . SER F 12  ? 5.1378 2.5158 2.5938 -0.6853 -0.0169 0.1297  12  SER F CB  
11508 O OG  . SER F 12  ? 5.1020 2.4867 2.5860 -0.6997 -0.0164 0.1197  12  SER F OG  
11509 N N   . ALA F 13  ? 5.1134 2.4823 2.5013 -0.6368 -0.0224 0.1259  13  ALA F N   
11510 C CA  . ALA F 13  ? 5.1490 2.5131 2.5174 -0.6190 -0.0244 0.1324  13  ALA F CA  
11511 C C   . ALA F 13  ? 5.1603 2.4896 2.5142 -0.5993 -0.0415 0.1246  13  ALA F C   
11512 O O   . ALA F 13  ? 5.1141 2.4285 2.4702 -0.5972 -0.0505 0.1129  13  ALA F O   
11513 C CB  . ALA F 13  ? 5.0728 2.4663 2.4306 -0.6125 -0.0122 0.1303  13  ALA F CB  
11514 N N   . SER F 14  ? 5.1516 2.4701 2.4919 -0.5844 -0.0458 0.1312  14  SER F N   
11515 C CA  . SER F 14  ? 5.1767 2.4634 2.5008 -0.5642 -0.0607 0.1251  14  SER F CA  
11516 C C   . SER F 14  ? 5.1076 2.3999 2.4109 -0.5461 -0.0573 0.1175  14  SER F C   
11517 O O   . SER F 14  ? 5.0652 2.3861 2.3693 -0.5468 -0.0444 0.1209  14  SER F O   
11518 C CB  . SER F 14  ? 5.2977 2.5668 2.6221 -0.5591 -0.0680 0.1370  14  SER F CB  
11519 O OG  . SER F 14  ? 5.3650 2.6283 2.7119 -0.5754 -0.0711 0.1438  14  SER F OG  
11520 N N   . VAL F 15  ? 4.9571 2.2240 2.2446 -0.5297 -0.0689 0.1066  15  VAL F N   
11521 C CA  . VAL F 15  ? 4.9109 2.1782 2.1789 -0.5102 -0.0665 0.1000  15  VAL F CA  
11522 C C   . VAL F 15  ? 4.9738 2.2500 2.2405 -0.5029 -0.0615 0.1111  15  VAL F C   
11523 O O   . VAL F 15  ? 5.0749 2.3350 2.3427 -0.5018 -0.0687 0.1202  15  VAL F O   
11524 C CB  . VAL F 15  ? 4.9189 2.1528 2.1682 -0.4926 -0.0812 0.0893  15  VAL F CB  
11525 C CG1 . VAL F 15  ? 4.8864 2.1177 2.1159 -0.4712 -0.0783 0.0835  15  VAL F CG1 
11526 C CG2 . VAL F 15  ? 4.8504 2.0812 2.1034 -0.4984 -0.0859 0.0785  15  VAL F CG2 
11527 N N   . GLY F 16  ? 4.9546 2.2581 2.2223 -0.4974 -0.0495 0.1104  16  GLY F N   
11528 C CA  . GLY F 16  ? 5.0023 2.3206 2.2730 -0.4898 -0.0440 0.1205  16  GLY F CA  
11529 C C   . GLY F 16  ? 5.0072 2.3618 2.2967 -0.5054 -0.0320 0.1324  16  GLY F C   
11530 O O   . GLY F 16  ? 5.0273 2.4017 2.3212 -0.4984 -0.0260 0.1398  16  GLY F O   
11531 N N   . ASP F 17  ? 4.9344 2.2987 2.2355 -0.5259 -0.0283 0.1347  17  ASP F N   
11532 C CA  . ASP F 17  ? 4.9478 2.3466 2.2653 -0.5411 -0.0163 0.1462  17  ASP F CA  
11533 C C   . ASP F 17  ? 4.8518 2.2899 2.1773 -0.5393 -0.0032 0.1416  17  ASP F C   
11534 O O   . ASP F 17  ? 4.7567 2.1976 2.0800 -0.5346 -0.0014 0.1286  17  ASP F O   
11535 C CB  . ASP F 17  ? 4.9596 2.3588 2.2885 -0.5639 -0.0145 0.1486  17  ASP F CB  
11536 C CG  . ASP F 17  ? 5.0724 2.4433 2.4034 -0.5693 -0.0246 0.1577  17  ASP F CG  
11537 O OD1 . ASP F 17  ? 5.1462 2.4987 2.4691 -0.5560 -0.0326 0.1632  17  ASP F OD1 
11538 O OD2 . ASP F 17  ? 5.0872 2.4553 2.4306 -0.5870 -0.0241 0.1593  17  ASP F OD2 
11539 N N   . LYS F 18  ? 5.0328 2.5022 2.3691 -0.5427 0.0057  0.1528  18  LYS F N   
11540 C CA  . LYS F 18  ? 4.9497 2.4625 2.2995 -0.5461 0.0190  0.1504  18  LYS F CA  
11541 C C   . LYS F 18  ? 4.9410 2.4714 2.3018 -0.5698 0.0270  0.1529  18  LYS F C   
11542 O O   . LYS F 18  ? 5.0276 2.5556 2.3915 -0.5820 0.0272  0.1650  18  LYS F O   
11543 C CB  . LYS F 18  ? 4.9859 2.5247 2.3418 -0.5372 0.0238  0.1608  18  LYS F CB  
11544 C CG  . LYS F 18  ? 4.9070 2.4932 2.2789 -0.5405 0.0370  0.1590  18  LYS F CG  
11545 C CD  . LYS F 18  ? 4.9488 2.5595 2.3264 -0.5310 0.0402  0.1697  18  LYS F CD  
11546 C CE  . LYS F 18  ? 4.8700 2.5286 2.2643 -0.5340 0.0524  0.1674  18  LYS F CE  
11547 N NZ  . LYS F 18  ? 4.9466 2.6281 2.3458 -0.5222 0.0543  0.1762  18  LYS F NZ  
11548 N N   . VAL F 19  ? 4.8919 2.4401 2.2596 -0.5766 0.0342  0.1418  19  VAL F N   
11549 C CA  . VAL F 19  ? 4.8927 2.4593 2.2714 -0.5994 0.0431  0.1428  19  VAL F CA  
11550 C C   . VAL F 19  ? 4.8002 2.4109 2.1928 -0.6026 0.0563  0.1370  19  VAL F C   
11551 O O   . VAL F 19  ? 4.7042 2.3249 2.0986 -0.5886 0.0573  0.1278  19  VAL F O   
11552 C CB  . VAL F 19  ? 4.8875 2.4239 2.2615 -0.6096 0.0368  0.1344  19  VAL F CB  
11553 C CG1 . VAL F 19  ? 4.9975 2.4934 2.3627 -0.6084 0.0237  0.1408  19  VAL F CG1 
11554 C CG2 . VAL F 19  ? 4.7562 2.2835 2.1238 -0.5980 0.0334  0.1187  19  VAL F CG2 
11555 N N   . THR F 20  ? 4.7605 2.3984 2.1644 -0.6212 0.0668  0.1426  20  THR F N   
11556 C CA  . THR F 20  ? 4.6850 2.3674 2.1038 -0.6274 0.0800  0.1377  20  THR F CA  
11557 C C   . THR F 20  ? 4.6812 2.3693 2.1067 -0.6508 0.0874  0.1338  20  THR F C   
11558 O O   . THR F 20  ? 4.7811 2.4594 2.2062 -0.6657 0.0882  0.1429  20  THR F O   
11559 C CB  . THR F 20  ? 4.7418 2.4592 2.1685 -0.6257 0.0871  0.1495  20  THR F CB  
11560 O OG1 . THR F 20  ? 4.7398 2.4520 2.1614 -0.6040 0.0803  0.1528  20  THR F OG1 
11561 C CG2 . THR F 20  ? 4.6624 2.4267 2.1054 -0.6323 0.1002  0.1437  20  THR F CG2 
11562 N N   . ILE F 21  ? 4.6198 2.3236 2.0529 -0.6541 0.0932  0.1206  21  ILE F N   
11563 C CA  . ILE F 21  ? 4.6066 2.3193 2.0477 -0.6764 0.1016  0.1155  21  ILE F CA  
11564 C C   . ILE F 21  ? 4.5544 2.3181 2.0118 -0.6819 0.1161  0.1125  21  ILE F C   
11565 O O   . ILE F 21  ? 4.4847 2.2724 1.9485 -0.6667 0.1178  0.1097  21  ILE F O   
11566 C CB  . ILE F 21  ? 4.5202 2.2058 1.9564 -0.6778 0.0957  0.1021  21  ILE F CB  
11567 C CG1 . ILE F 21  ? 4.3876 2.0877 1.8273 -0.6621 0.0966  0.0901  21  ILE F CG1 
11568 C CG2 . ILE F 21  ? 4.5684 2.2042 1.9891 -0.6711 0.0802  0.1044  21  ILE F CG2 
11569 C CD1 . ILE F 21  ? 4.3043 1.9801 1.7388 -0.6631 0.0914  0.0771  21  ILE F CD1 
11570 N N   . THR F 22  ? 4.6284 2.4094 2.0945 -0.7039 0.1268  0.1129  22  THR F N   
11571 C CA  . THR F 22  ? 4.6138 2.4442 2.0948 -0.7114 0.1410  0.1123  22  THR F CA  
11572 C C   . THR F 22  ? 4.5285 2.3746 2.0205 -0.7258 0.1500  0.0985  22  THR F C   
11573 O O   . THR F 22  ? 4.5315 2.3523 2.0203 -0.7398 0.1488  0.0946  22  THR F O   
11574 C CB  . THR F 22  ? 4.7565 2.5985 2.2384 -0.7252 0.1477  0.1266  22  THR F CB  
11575 O OG1 . THR F 22  ? 4.8512 2.6835 2.3243 -0.7107 0.1399  0.1396  22  THR F OG1 
11576 C CG2 . THR F 22  ? 4.7601 2.6526 2.2564 -0.7347 0.1628  0.1250  22  THR F CG2 
11577 N N   . CYS F 23  ? 4.6378 2.5257 2.1441 -0.7222 0.1588  0.0913  23  CYS F N   
11578 C CA  . CYS F 23  ? 4.5558 2.4672 2.0756 -0.7359 0.1694  0.0783  23  CYS F CA  
11579 C C   . CYS F 23  ? 4.5660 2.5278 2.1004 -0.7433 0.1829  0.0804  23  CYS F C   
11580 O O   . CYS F 23  ? 4.5337 2.5218 2.0742 -0.7283 0.1830  0.0831  23  CYS F O   
11581 C CB  . CYS F 23  ? 4.4098 2.3214 1.9350 -0.7212 0.1653  0.0650  23  CYS F CB  
11582 S SG  . CYS F 23  ? 4.2953 2.2367 1.8391 -0.7353 0.1774  0.0478  23  CYS F SG  
11583 N N   . ARG F 24  ? 4.3705 2.3458 1.9107 -0.7662 0.1945  0.0791  24  ARG F N   
11584 C CA  . ARG F 24  ? 4.3790 2.4022 1.9323 -0.7749 0.2081  0.0798  24  ARG F CA  
11585 C C   . ARG F 24  ? 4.2782 2.3287 1.8478 -0.7877 0.2195  0.0639  24  ARG F C   
11586 O O   . ARG F 24  ? 4.2700 2.3006 1.8388 -0.8026 0.2215  0.0568  24  ARG F O   
11587 C CB  . ARG F 24  ? 4.5272 2.5491 2.0750 -0.7911 0.2144  0.0929  24  ARG F CB  
11588 C CG  . ARG F 24  ? 4.6387 2.6377 2.1722 -0.7794 0.2043  0.1095  24  ARG F CG  
11589 C CD  . ARG F 24  ? 4.7632 2.7721 2.2951 -0.7941 0.2129  0.1228  24  ARG F CD  
11590 N NE  . ARG F 24  ? 4.7898 2.8438 2.3281 -0.7894 0.2204  0.1262  24  ARG F NE  
11591 C CZ  . ARG F 24  ? 4.8147 2.8739 2.3457 -0.7769 0.2157  0.1398  24  ARG F CZ  
11592 N NH1 . ARG F 24  ? 4.8981 2.9208 2.4159 -0.7685 0.2043  0.1514  24  ARG F NH1 
11593 N NH2 . ARG F 24  ? 4.8385 2.9393 2.3755 -0.7732 0.2223  0.1420  24  ARG F NH2 
11594 N N   . ALA F 25  ? 4.1158 2.2118 1.7008 -0.7822 0.2267  0.0585  25  ALA F N   
11595 C CA  . ALA F 25  ? 4.0892 2.2170 1.6924 -0.7933 0.2381  0.0430  25  ALA F CA  
11596 C C   . ALA F 25  ? 4.0932 2.2561 1.7041 -0.8117 0.2531  0.0445  25  ALA F C   
11597 O O   . ALA F 25  ? 4.1036 2.2837 1.7112 -0.8080 0.2547  0.0559  25  ALA F O   
11598 C CB  . ALA F 25  ? 4.0544 2.2111 1.6730 -0.7745 0.2364  0.0344  25  ALA F CB  
11599 N N   . SER F 26  ? 4.1754 2.3484 1.7963 -0.8318 0.2643  0.0329  26  SER F N   
11600 C CA  . SER F 26  ? 4.2332 2.4396 1.8627 -0.8509 0.2802  0.0324  26  SER F CA  
11601 C C   . SER F 26  ? 4.1827 2.4416 1.8283 -0.8429 0.2867  0.0266  26  SER F C   
11602 O O   . SER F 26  ? 4.2361 2.5249 1.8854 -0.8530 0.2977  0.0297  26  SER F O   
11603 C CB  . SER F 26  ? 4.2087 2.4107 1.8460 -0.8749 0.2909  0.0205  26  SER F CB  
11604 O OG  . SER F 26  ? 4.0663 2.2802 1.7173 -0.8717 0.2913  0.0035  26  SER F OG  
11605 N N   . GLN F 27  ? 4.1677 2.4382 1.8236 -0.8250 0.2804  0.0183  27  GLN F N   
11606 C CA  . GLN F 27  ? 4.0987 2.4163 1.7703 -0.8143 0.2842  0.0140  27  GLN F CA  
11607 C C   . GLN F 27  ? 4.0502 2.3601 1.7201 -0.7877 0.2708  0.0185  27  GLN F C   
11608 O O   . GLN F 27  ? 4.0410 2.3124 1.7011 -0.7784 0.2599  0.0207  27  GLN F O   
11609 C CB  . GLN F 27  ? 3.9900 2.3401 1.6850 -0.8233 0.2947  -0.0053 27  GLN F CB  
11610 C CG  . GLN F 27  ? 4.0538 2.4235 1.7547 -0.8491 0.3107  -0.0112 27  GLN F CG  
11611 C CD  . GLN F 27  ? 4.1243 2.5336 1.8279 -0.8513 0.3190  -0.0058 27  GLN F CD  
11612 O OE1 . GLN F 27  ? 4.1142 2.5407 1.8173 -0.8334 0.3131  0.0007  27  GLN F OE1 
11613 N NE2 . GLN F 27  ? 4.2213 2.6448 1.9272 -0.8733 0.3332  -0.0082 27  GLN F NE2 
11614 N N   . GLY F 28  ? 3.8867 2.2330 1.5658 -0.7753 0.2717  0.0197  28  GLY F N   
11615 C CA  . GLY F 28  ? 3.8751 2.2173 1.5542 -0.7506 0.2604  0.0237  28  GLY F CA  
11616 C C   . GLY F 28  ? 3.8464 2.1842 1.5399 -0.7417 0.2573  0.0103  28  GLY F C   
11617 O O   . GLY F 28  ? 3.8206 2.1882 1.5342 -0.7475 0.2655  -0.0038 28  GLY F O   
11618 N N   . VAL F 29  ? 4.0505 2.3513 1.7339 -0.7272 0.2456  0.0146  29  VAL F N   
11619 C CA  . VAL F 29  ? 3.9246 2.2183 1.6197 -0.7156 0.2416  0.0040  29  VAL F CA  
11620 C C   . VAL F 29  ? 3.8782 2.1772 1.5768 -0.6906 0.2340  0.0082  29  VAL F C   
11621 O O   . VAL F 29  ? 3.7938 2.0789 1.4981 -0.6781 0.2291  0.0026  29  VAL F O   
11622 C CB  . VAL F 29  ? 3.9353 2.1806 1.6168 -0.7199 0.2351  0.0027  29  VAL F CB  
11623 C CG1 . VAL F 29  ? 3.9713 2.2133 1.6514 -0.7456 0.2437  -0.0033 29  VAL F CG1 
11624 C CG2 . VAL F 29  ? 4.0388 2.2444 1.6966 -0.7110 0.2239  0.0174  29  VAL F CG2 
11625 N N   . ARG F 30  ? 4.1159 2.4338 1.8108 -0.6832 0.2332  0.0181  30  ARG F N   
11626 C CA  . ARG F 30  ? 4.0802 2.4032 1.7767 -0.6603 0.2263  0.0231  30  ARG F CA  
11627 C C   . ARG F 30  ? 4.0965 2.3722 1.7776 -0.6473 0.2148  0.0294  30  ARG F C   
11628 O O   . ARG F 30  ? 4.1993 2.4423 1.8611 -0.6537 0.2101  0.0382  30  ARG F O   
11629 C CB  . ARG F 30  ? 3.9738 2.3327 1.6952 -0.6534 0.2317  0.0102  30  ARG F CB  
11630 C CG  . ARG F 30  ? 3.9859 2.3919 1.7216 -0.6656 0.2426  0.0037  30  ARG F CG  
11631 C CD  . ARG F 30  ? 3.8882 2.3263 1.6492 -0.6590 0.2474  -0.0102 30  ARG F CD  
11632 N NE  . ARG F 30  ? 3.8234 2.2513 1.5956 -0.6675 0.2509  -0.0226 30  ARG F NE  
11633 C CZ  . ARG F 30  ? 3.8341 2.2790 1.6162 -0.6869 0.2603  -0.0325 30  ARG F CZ  
11634 N NH1 . ARG F 30  ? 3.9393 2.4118 1.7210 -0.6995 0.2675  -0.0312 30  ARG F NH1 
11635 N NH2 . ARG F 30  ? 3.7730 2.2066 1.5645 -0.6938 0.2627  -0.0435 30  ARG F NH2 
11636 N N   . ASN F 31  ? 4.1287 2.3989 1.8173 -0.6291 0.2102  0.0254  31  ASN F N   
11637 C CA  . ASN F 31  ? 4.1363 2.3620 1.8112 -0.6163 0.2000  0.0295  31  ASN F CA  
11638 C C   . ASN F 31  ? 4.0549 2.2594 1.7343 -0.6186 0.1996  0.0186  31  ASN F C   
11639 O O   . ASN F 31  ? 4.0349 2.2073 1.7065 -0.6050 0.1919  0.0194  31  ASN F O   
11640 C CB  . ASN F 31  ? 4.1026 2.3319 1.7798 -0.5933 0.1950  0.0337  31  ASN F CB  
11641 C CG  . ASN F 31  ? 3.9765 2.2337 1.6767 -0.5844 0.2003  0.0222  31  ASN F CG  
11642 O OD1 . ASN F 31  ? 3.9339 2.2187 1.6508 -0.5957 0.2086  0.0119  31  ASN F OD1 
11643 N ND2 . ASN F 31  ? 3.9700 2.2191 1.6715 -0.5644 0.1958  0.0238  31  ASN F ND2 
11644 N N   . GLU F 32  ? 4.0179 2.2395 1.7092 -0.6352 0.2078  0.0082  32  GLU F N   
11645 C CA  . GLU F 32  ? 3.9321 2.1417 1.6320 -0.6359 0.2084  -0.0035 32  GLU F CA  
11646 C C   . GLU F 32  ? 3.9886 2.1551 1.6690 -0.6482 0.2034  -0.0024 32  GLU F C   
11647 O O   . GLU F 32  ? 3.9907 2.1598 1.6725 -0.6678 0.2091  -0.0085 32  GLU F O   
11648 C CB  . GLU F 32  ? 3.8768 2.1289 1.6017 -0.6461 0.2197  -0.0162 32  GLU F CB  
11649 C CG  . GLU F 32  ? 3.8341 2.1272 1.5779 -0.6331 0.2237  -0.0180 32  GLU F CG  
11650 C CD  . GLU F 32  ? 3.8043 2.1434 1.5715 -0.6451 0.2353  -0.0297 32  GLU F CD  
11651 O OE1 . GLU F 32  ? 3.7885 2.1613 1.5726 -0.6352 0.2387  -0.0333 32  GLU F OE1 
11652 O OE2 . GLU F 32  ? 3.8294 2.1704 1.5981 -0.6647 0.2410  -0.0359 32  GLU F OE2 
11653 N N   . LEU F 33  ? 3.7922 1.9176 1.4533 -0.6362 0.1925  0.0053  33  LEU F N   
11654 C CA  . LEU F 33  ? 3.8785 1.9598 1.5164 -0.6462 0.1859  0.0092  33  LEU F CA  
11655 C C   . LEU F 33  ? 3.8672 1.9064 1.4914 -0.6283 0.1743  0.0110  33  LEU F C   
11656 O O   . LEU F 33  ? 3.8587 1.8983 1.4834 -0.6088 0.1702  0.0159  33  LEU F O   
11657 C CB  . LEU F 33  ? 4.0159 2.0919 1.6385 -0.6542 0.1847  0.0218  33  LEU F CB  
11658 C CG  . LEU F 33  ? 4.1151 2.1479 1.7152 -0.6678 0.1791  0.0256  33  LEU F CG  
11659 C CD1 . LEU F 33  ? 4.1882 2.2354 1.7905 -0.6934 0.1888  0.0234  33  LEU F CD1 
11660 C CD2 . LEU F 33  ? 4.2051 2.2121 1.7864 -0.6593 0.1702  0.0390  33  LEU F CD2 
11661 N N   . ALA F 34  ? 3.8187 1.8215 1.4300 -0.6351 0.1690  0.0066  34  ALA F N   
11662 C CA  . ALA F 34  ? 3.8112 1.7709 1.4071 -0.6196 0.1576  0.0072  34  ALA F CA  
11663 C C   . ALA F 34  ? 3.9200 1.8334 1.4884 -0.6290 0.1485  0.0124  34  ALA F C   
11664 O O   . ALA F 34  ? 3.9775 1.8898 1.5408 -0.6501 0.1520  0.0125  34  ALA F O   
11665 C CB  . ALA F 34  ? 3.6942 1.6512 1.3006 -0.6155 0.1583  -0.0044 34  ALA F CB  
11666 N N   . TRP F 35  ? 3.7608 1.6360 1.3117 -0.6133 0.1371  0.0167  35  TRP F N   
11667 C CA  . TRP F 35  ? 3.8110 1.6374 1.3349 -0.6189 0.1264  0.0205  35  TRP F CA  
11668 C C   . TRP F 35  ? 3.8039 1.5931 1.3166 -0.6087 0.1172  0.0133  35  TRP F C   
11669 O O   . TRP F 35  ? 3.7869 1.5800 1.3077 -0.5896 0.1164  0.0102  35  TRP F O   
11670 C CB  . TRP F 35  ? 3.9156 1.7261 1.4253 -0.6096 0.1196  0.0326  35  TRP F CB  
11671 C CG  . TRP F 35  ? 3.9983 1.8372 1.5136 -0.6206 0.1266  0.0418  35  TRP F CG  
11672 C CD1 . TRP F 35  ? 3.9849 1.8646 1.5166 -0.6142 0.1338  0.0458  35  TRP F CD1 
11673 C CD2 . TRP F 35  ? 4.1130 1.9398 1.6168 -0.6393 0.1264  0.0490  35  TRP F CD2 
11674 N NE1 . TRP F 35  ? 4.0842 1.9783 1.6143 -0.6276 0.1381  0.0549  35  TRP F NE1 
11675 C CE2 . TRP F 35  ? 4.1650 2.0275 1.6789 -0.6432 0.1342  0.0573  35  TRP F CE2 
11676 C CE3 . TRP F 35  ? 4.1774 1.9665 1.6639 -0.6531 0.1204  0.0497  35  TRP F CE3 
11677 C CZ2 . TRP F 35  ? 4.2813 2.1434 1.7891 -0.6602 0.1370  0.0664  35  TRP F CZ2 
11678 C CZ3 . TRP F 35  ? 4.2896 2.0788 1.7721 -0.6704 0.1234  0.0588  35  TRP F CZ3 
11679 C CH2 . TRP F 35  ? 4.3426 2.1681 1.8357 -0.6737 0.1321  0.0672  35  TRP F CH2 
11680 N N   . TYR F 36  ? 4.0363 1.7887 1.5297 -0.6215 0.1102  0.0112  36  TYR F N   
11681 C CA  . TYR F 36  ? 4.0003 1.7125 1.4785 -0.6141 0.0998  0.0047  36  TYR F CA  
11682 C C   . TYR F 36  ? 4.1032 1.7642 1.5512 -0.6160 0.0860  0.0097  36  TYR F C   
11683 O O   . TYR F 36  ? 4.1996 1.8565 1.6407 -0.6301 0.0860  0.0169  36  TYR F O   
11684 C CB  . TYR F 36  ? 3.9292 1.6468 1.4148 -0.6287 0.1040  -0.0056 36  TYR F CB  
11685 C CG  . TYR F 36  ? 3.8186 1.5874 1.3361 -0.6276 0.1173  -0.0118 36  TYR F CG  
11686 C CD1 . TYR F 36  ? 3.8249 1.6366 1.3603 -0.6430 0.1300  -0.0116 36  TYR F CD1 
11687 C CD2 . TYR F 36  ? 3.7081 1.4826 1.2386 -0.6110 0.1172  -0.0176 36  TYR F CD2 
11688 C CE1 . TYR F 36  ? 3.7217 1.5801 1.2863 -0.6417 0.1415  -0.0181 36  TYR F CE1 
11689 C CE2 . TYR F 36  ? 3.6048 1.4260 1.1655 -0.6098 0.1290  -0.0233 36  TYR F CE2 
11690 C CZ  . TYR F 36  ? 3.6108 1.4736 1.1882 -0.6251 0.1408  -0.0240 36  TYR F CZ  
11691 O OH  . TYR F 36  ? 3.5081 1.4171 1.1153 -0.6237 0.1520  -0.0304 36  TYR F OH  
11692 N N   . GLN F 37  ? 4.1219 1.7451 1.5536 -0.6008 0.0744  0.0060  37  GLN F N   
11693 C CA  . GLN F 37  ? 4.2011 1.7724 1.6032 -0.6013 0.0592  0.0074  37  GLN F CA  
11694 C C   . GLN F 37  ? 4.1558 1.7008 1.5469 -0.6088 0.0528  -0.0020 37  GLN F C   
11695 O O   . GLN F 37  ? 4.0574 1.6091 1.4586 -0.6003 0.0554  -0.0084 37  GLN F O   
11696 C CB  . GLN F 37  ? 4.2189 1.7654 1.6077 -0.5764 0.0496  0.0095  37  GLN F CB  
11697 C CG  . GLN F 37  ? 4.2972 1.7941 1.6562 -0.5736 0.0330  0.0107  37  GLN F CG  
11698 C CD  . GLN F 37  ? 4.2913 1.7634 1.6367 -0.5481 0.0245  0.0096  37  GLN F CD  
11699 O OE1 . GLN F 37  ? 4.2162 1.6743 1.5581 -0.5355 0.0215  0.0022  37  GLN F OE1 
11700 N NE2 . GLN F 37  ? 4.3723 1.8391 1.7116 -0.5403 0.0213  0.0177  37  GLN F NE2 
11701 N N   . GLN F 38  ? 4.1858 1.7077 1.5667 -0.6228 0.0444  -0.0005 38  GLN F N   
11702 C CA  . GLN F 38  ? 4.1555 1.6728 1.5514 -0.6224 0.0348  -0.0076 38  GLN F CA  
11703 C C   . GLN F 38  ? 4.2161 1.7112 1.6163 -0.6145 0.0169  -0.0047 38  GLN F C   
11704 O O   . GLN F 38  ? 4.3138 1.8017 1.7162 -0.6245 0.0151  0.0017  38  GLN F O   
11705 C CB  . GLN F 38  ? 4.1235 1.6739 1.5591 -0.6446 0.0428  -0.0147 38  GLN F CB  
11706 C CG  . GLN F 38  ? 4.0458 1.6130 1.5200 -0.6385 0.0325  -0.0249 38  GLN F CG  
11707 C CD  . GLN F 38  ? 4.0119 1.6153 1.5292 -0.6592 0.0403  -0.0342 38  GLN F CD  
11708 O OE1 . GLN F 38  ? 4.0798 1.6894 1.6052 -0.6798 0.0476  -0.0321 38  GLN F OE1 
11709 N NE2 . GLN F 38  ? 3.9161 1.5447 1.4629 -0.6534 0.0393  -0.0438 38  GLN F NE2 
11710 N N   . LYS F 39  ? 2.8771 2.8451 1.7911 -0.9287 0.1695  0.2130  39  LYS F N   
11711 C CA  . LYS F 39  ? 2.9190 2.8853 1.8185 -0.9258 0.1750  0.2047  39  LYS F CA  
11712 C C   . LYS F 39  ? 2.8235 2.8491 1.7817 -0.8933 0.1937  0.1937  39  LYS F C   
11713 O O   . LYS F 39  ? 2.7041 2.7833 1.7295 -0.8638 0.2098  0.1947  39  LYS F O   
11714 C CB  . LYS F 39  ? 2.9031 2.8918 1.8274 -0.9163 0.1939  0.2105  39  LYS F CB  
11715 C CG  . LYS F 39  ? 3.0373 2.9546 1.8956 -0.9518 0.1726  0.2232  39  LYS F CG  
11716 C CD  . LYS F 39  ? 3.0708 3.0116 1.9601 -0.9430 0.1958  0.2290  39  LYS F CD  
11717 C CE  . LYS F 39  ? 3.2842 3.1410 2.1053 -0.9811 0.1709  0.2449  39  LYS F CE  
11718 N NZ  . LYS F 39  ? 3.3381 3.2146 2.1944 -0.9755 0.1969  0.2508  39  LYS F NZ  
11719 N N   . PRO F 40  ? 3.0332 3.0461 1.9667 -0.8988 0.1906  0.1843  40  PRO F N   
11720 C CA  . PRO F 40  ? 2.9627 3.0240 1.9470 -0.8715 0.2044  0.1759  40  PRO F CA  
11721 C C   . PRO F 40  ? 2.8234 2.9584 1.8930 -0.8262 0.2333  0.1796  40  PRO F C   
11722 O O   . PRO F 40  ? 2.8312 2.9835 1.9150 -0.8160 0.2473  0.1831  40  PRO F O   
11723 C CB  . PRO F 40  ? 3.0721 3.1058 2.0132 -0.8897 0.1976  0.1672  40  PRO F CB  
11724 C CG  . PRO F 40  ? 3.2272 3.1794 2.0816 -0.9321 0.1723  0.1696  40  PRO F CG  
11725 C CD  . PRO F 40  ? 3.2101 3.1549 2.0629 -0.9337 0.1712  0.1814  40  PRO F CD  
11726 N N   . GLY F 41  ? 2.9159 3.0905 2.0365 -0.8030 0.2422  0.1784  41  GLY F N   
11727 C CA  . GLY F 41  ? 2.8235 3.0635 2.0099 -0.7743 0.2657  0.1796  41  GLY F CA  
11728 C C   . GLY F 41  ? 2.7270 2.9881 1.9686 -0.7432 0.2833  0.1930  41  GLY F C   
11729 O O   . GLY F 41  ? 2.6734 2.9858 1.9719 -0.7169 0.3054  0.1954  41  GLY F O   
11730 N N   . LYS F 42  ? 2.6988 2.9256 1.9124 -0.7641 0.2714  0.1989  42  LYS F N   
11731 C CA  . LYS F 42  ? 2.6306 2.8798 1.8878 -0.7541 0.2857  0.2091  42  LYS F CA  
11732 C C   . LYS F 42  ? 2.6133 2.8498 1.8663 -0.7682 0.2725  0.2112  42  LYS F C   
11733 O O   . LYS F 42  ? 2.6810 2.8756 1.8755 -0.7960 0.2478  0.2056  42  LYS F O   
11734 C CB  . LYS F 42  ? 2.7088 2.9316 1.9307 -0.7810 0.2829  0.2147  42  LYS F CB  
11735 C CG  . LYS F 42  ? 2.7806 3.0122 1.9993 -0.7709 0.2962  0.2120  42  LYS F CG  
11736 C CD  . LYS F 42  ? 2.6971 2.9916 2.0019 -0.7186 0.3307  0.2154  42  LYS F CD  
11737 C CE  . LYS F 42  ? 2.7974 3.1002 2.0983 -0.7099 0.3466  0.2146  42  LYS F CE  
11738 N NZ  . LYS F 42  ? 2.7456 3.1009 2.1261 -0.6581 0.3812  0.2208  42  LYS F NZ  
11739 N N   . ALA F 43  ? 2.5334 2.8063 1.8517 -0.7481 0.2909  0.2193  43  ALA F N   
11740 C CA  . ALA F 43  ? 2.5279 2.7902 1.8432 -0.7654 0.2790  0.2222  43  ALA F CA  
11741 C C   . ALA F 43  ? 2.6476 2.8523 1.8880 -0.8173 0.2524  0.2276  43  ALA F C   
11742 O O   . ALA F 43  ? 2.6979 2.8854 1.9175 -0.8315 0.2526  0.2322  43  ALA F O   
11743 C CB  . ALA F 43  ? 2.4002 2.7165 1.8124 -0.7311 0.3075  0.2297  43  ALA F CB  
11744 N N   . PRO F 44  ? 2.5240 2.6905 1.7182 -0.8468 0.2278  0.2285  44  PRO F N   
11745 C CA  . PRO F 44  ? 2.6435 2.7426 1.7632 -0.8957 0.1981  0.2385  44  PRO F CA  
11746 C C   . PRO F 44  ? 2.5978 2.7209 1.7762 -0.8993 0.2119  0.2520  44  PRO F C   
11747 O O   . PRO F 44  ? 2.4653 2.6602 1.7482 -0.8654 0.2443  0.2524  44  PRO F O   
11748 C CB  . PRO F 44  ? 2.6876 2.7510 1.7620 -0.9170 0.1736  0.2372  44  PRO F CB  
11749 C CG  . PRO F 44  ? 2.6314 2.7284 1.7324 -0.8866 0.1864  0.2230  44  PRO F CG  
11750 C CD  . PRO F 44  ? 2.4941 2.6675 1.6937 -0.8380 0.2234  0.2215  44  PRO F CD  
11751 N N   . ASN F 45  ? 2.5596 2.6140 1.6734 -0.9412 0.1856  0.2642  45  ASN F N   
11752 C CA  . ASN F 45  ? 2.5967 2.6540 1.7659 -0.9590 0.1894  0.2797  45  ASN F CA  
11753 C C   . ASN F 45  ? 2.7511 2.7191 1.8684 -0.9879 0.1323  0.2838  45  ASN F C   
11754 O O   . ASN F 45  ? 2.9150 2.7900 1.9106 -1.0122 0.0909  0.2855  45  ASN F O   
11755 C CB  . ASN F 45  ? 2.6856 2.7279 1.8523 -0.9640 0.1980  0.2843  45  ASN F CB  
11756 C CG  . ASN F 45  ? 2.5131 2.6527 1.7877 -0.9135 0.2504  0.2751  45  ASN F CG  
11757 O OD1 . ASN F 45  ? 2.3325 2.5412 1.6778 -0.8716 0.2766  0.2668  45  ASN F OD1 
11758 N ND2 . ASN F 45  ? 2.5759 2.7116 1.8592 -0.9156 0.2641  0.2779  45  ASN F ND2 
11759 N N   . LEU F 46  ? 2.3508 2.3445 1.5819 -0.9574 0.1188  0.2720  46  LEU F N   
11760 C CA  . LEU F 46  ? 2.4214 2.3330 1.6387 -0.9496 0.0489  0.2585  46  LEU F CA  
11761 C C   . LEU F 46  ? 2.5615 2.3907 1.7796 -0.9263 -0.0082 0.2434  46  LEU F C   
11762 O O   . LEU F 46  ? 2.5184 2.3795 1.8422 -0.8924 0.0021  0.2333  46  LEU F O   
11763 C CB  . LEU F 46  ? 2.3552 2.3248 1.7055 -0.9228 0.0524  0.2481  46  LEU F CB  
11764 C CG  . LEU F 46  ? 2.4187 2.3155 1.7750 -0.9101 -0.0197 0.2311  46  LEU F CG  
11765 C CD1 . LEU F 46  ? 2.4930 2.3250 1.7034 -0.9490 -0.0453 0.2400  46  LEU F CD1 
11766 C CD2 . LEU F 46  ? 2.3397 2.3072 1.8554 -0.8782 -0.0093 0.2180  46  LEU F CD2 
11767 N N   . LEU F 47  ? 2.5332 2.2538 1.6324 -0.9439 -0.0675 0.2422  47  LEU F N   
11768 C CA  . LEU F 47  ? 2.7166 2.3457 1.8017 -0.9244 -0.1299 0.2288  47  LEU F CA  
11769 C C   . LEU F 47  ? 2.7885 2.3629 1.9161 -0.9001 -0.1981 0.2113  47  LEU F C   
11770 O O   . LEU F 47  ? 2.7810 2.3454 2.0104 -0.8623 -0.2289 0.1935  47  LEU F O   
11771 C CB  . LEU F 47  ? 2.9013 2.4381 1.8205 -0.9588 -0.1521 0.2400  47  LEU F CB  
11772 C CG  . LEU F 47  ? 2.8643 2.4352 1.7256 -0.9847 -0.0968 0.2546  47  LEU F CG  
11773 C CD1 . LEU F 47  ? 3.0560 2.5261 1.7535 -1.0202 -0.1249 0.2646  47  LEU F CD1 
11774 C CD2 . LEU F 47  ? 2.8171 2.4271 1.7734 -0.9540 -0.0772 0.2451  47  LEU F CD2 
11775 N N   . ILE F 48  ? 2.7203 2.2566 1.7697 -0.9212 -0.2229 0.2152  48  ILE F N   
11776 C CA  . ILE F 48  ? 2.8365 2.2973 1.8836 -0.9046 -0.2979 0.1996  48  ILE F CA  
11777 C C   . ILE F 48  ? 2.7275 2.2328 1.8012 -0.9111 -0.2865 0.1987  48  ILE F C   
11778 O O   . ILE F 48  ? 2.6376 2.1809 1.6478 -0.9445 -0.2384 0.2157  48  ILE F O   
11779 C CB  . ILE F 48  ? 3.0797 2.4097 1.9578 -0.9267 -0.3555 0.2056  48  ILE F CB  
11780 C CG1 . ILE F 48  ? 3.1875 2.4691 2.0423 -0.9194 -0.3699 0.2053  48  ILE F CG1 
11781 C CG2 . ILE F 48  ? 3.2026 2.4530 2.0666 -0.9099 -0.4343 0.1903  48  ILE F CG2 
11782 C CD1 . ILE F 48  ? 3.1925 2.4447 2.1535 -0.8745 -0.4239 0.1831  48  ILE F CD1 
11783 N N   . TYR F 49  ? 2.7636 2.2684 1.9391 -0.8788 -0.3288 0.1777  49  TYR F N   
11784 C CA  . TYR F 49  ? 2.6995 2.2255 1.8883 -0.8839 -0.3334 0.1731  49  TYR F CA  
11785 C C   . TYR F 49  ? 2.8565 2.2913 2.0377 -0.8621 -0.4233 0.1520  49  TYR F C   
11786 O O   . TYR F 49  ? 2.9736 2.3475 2.1720 -0.8378 -0.4755 0.1401  49  TYR F O   
11787 C CB  . TYR F 49  ? 2.5324 2.1847 1.8881 -0.8653 -0.2766 0.1679  49  TYR F CB  
11788 C CG  . TYR F 49  ? 2.4818 2.1702 2.0117 -0.8180 -0.2890 0.1471  49  TYR F CG  
11789 C CD1 . TYR F 49  ? 2.4919 2.1660 2.1177 -0.7879 -0.3418 0.1225  49  TYR F CD1 
11790 C CD2 . TYR F 49  ? 2.4252 2.1621 2.0266 -0.8030 -0.2468 0.1509  49  TYR F CD2 
11791 C CE1 . TYR F 49  ? 2.4456 2.1528 2.2390 -0.7448 -0.3518 0.1026  49  TYR F CE1 
11792 C CE2 . TYR F 49  ? 2.3810 2.1492 2.1449 -0.7594 -0.2545 0.1319  49  TYR F CE2 
11793 C CZ  . TYR F 49  ? 2.3901 2.1439 2.2525 -0.7308 -0.3063 0.1079  49  TYR F CZ  
11794 O OH  . TYR F 49  ? 2.3466 2.1311 2.3777 -0.6877 -0.3129 0.0882  49  TYR F OH  
11795 N N   . TYR F 50  ? 2.7259 2.1505 1.8796 -0.8704 -0.4421 0.1470  50  TYR F N   
11796 C CA  . TYR F 50  ? 2.8434 2.1727 1.9603 -0.8546 -0.5300 0.1282  50  TYR F CA  
11797 C C   . TYR F 50  ? 3.0825 2.2845 2.0387 -0.8670 -0.5836 0.1363  50  TYR F C   
11798 O O   . TYR F 50  ? 3.2401 2.3581 2.1886 -0.8427 -0.6620 0.1200  50  TYR F O   
11799 C CB  . TYR F 50  ? 2.8032 2.1563 2.0970 -0.8057 -0.5709 0.0991  50  TYR F CB  
11800 C CG  . TYR F 50  ? 2.6782 2.1417 2.1316 -0.7903 -0.5313 0.0873  50  TYR F CG  
11801 C CD1 . TYR F 50  ? 2.6541 2.1524 2.0689 -0.8147 -0.5013 0.0937  50  TYR F CD1 
11802 C CD2 . TYR F 50  ? 2.5970 2.1266 2.2423 -0.7506 -0.5241 0.0691  50  TYR F CD2 
11803 C CE1 . TYR F 50  ? 2.5493 2.1476 2.1131 -0.8004 -0.4647 0.0830  50  TYR F CE1 
11804 C CE2 . TYR F 50  ? 2.4938 2.1220 2.2887 -0.7359 -0.4864 0.0587  50  TYR F CE2 
11805 C CZ  . TYR F 50  ? 2.4699 2.1324 2.2233 -0.7608 -0.4575 0.0657  50  TYR F CZ  
11806 O OH  . TYR F 50  ? 2.3679 2.1277 2.2724 -0.7461 -0.4194 0.0555  50  TYR F OH  
11807 N N   . ALA F 51  ? 3.0536 2.2424 1.8847 -0.9046 -0.5402 0.1617  51  ALA F N   
11808 C CA  . ALA F 51  ? 3.1755 2.2499 1.8428 -0.9238 -0.5748 0.1745  51  ALA F CA  
11809 C C   . ALA F 51  ? 3.2059 2.2386 1.9101 -0.8981 -0.6100 0.1672  51  ALA F C   
11810 O O   . ALA F 51  ? 3.2668 2.2406 1.8613 -0.9179 -0.6081 0.1823  51  ALA F O   
11811 C CB  . ALA F 51  ? 3.3041 2.2678 1.8445 -0.9298 -0.6427 0.1707  51  ALA F CB  
11812 N N   . SER F 52  ? 3.1809 2.2403 2.0384 -0.8548 -0.6419 0.1438  52  SER F N   
11813 C CA  . SER F 52  ? 3.2418 2.2633 2.1398 -0.8303 -0.6725 0.1364  52  SER F CA  
11814 C C   . SER F 52  ? 3.0321 2.1517 2.1193 -0.7984 -0.6359 0.1239  52  SER F C   
11815 O O   . SER F 52  ? 3.0525 2.1426 2.1768 -0.7781 -0.6572 0.1174  52  SER F O   
11816 C CB  . SER F 52  ? 3.4248 2.3358 2.2965 -0.8044 -0.7721 0.1190  52  SER F CB  
11817 O OG  . SER F 52  ? 3.3510 2.2922 2.3318 -0.7776 -0.8036 0.0964  52  SER F OG  
11818 N N   . THR F 53  ? 2.9049 2.1365 2.1126 -0.7924 -0.5814 0.1204  53  THR F N   
11819 C CA  . THR F 53  ? 2.8018 2.1212 2.1966 -0.7577 -0.5497 0.1070  53  THR F CA  
11820 C C   . THR F 53  ? 2.7244 2.1172 2.1260 -0.7728 -0.4667 0.1251  53  THR F C   
11821 O O   . THR F 53  ? 2.6811 2.1248 2.0246 -0.8044 -0.4086 0.1437  53  THR F O   
11822 C CB  . THR F 53  ? 2.7192 2.1187 2.2547 -0.7381 -0.5369 0.0920  53  THR F CB  
11823 O OG1 . THR F 53  ? 2.7959 2.1243 2.3306 -0.7209 -0.6200 0.0717  53  THR F OG1 
11824 C CG2 . THR F 53  ? 2.6165 2.1034 2.3469 -0.7015 -0.5002 0.0792  53  THR F CG2 
11825 N N   . LEU F 54  ? 2.9151 2.3122 2.3879 -0.7494 -0.4624 0.1187  54  LEU F N   
11826 C CA  . LEU F 54  ? 2.8068 2.2701 2.2913 -0.7588 -0.3879 0.1328  54  LEU F CA  
11827 C C   . LEU F 54  ? 2.5753 2.1658 2.2009 -0.7455 -0.3160 0.1328  54  LEU F C   
11828 O O   . LEU F 54  ? 2.4589 2.0887 2.2389 -0.7093 -0.3231 0.1145  54  LEU F O   
11829 C CB  . LEU F 54  ? 2.8257 2.2526 2.3477 -0.7353 -0.4056 0.1240  54  LEU F CB  
11830 C CG  . LEU F 54  ? 3.0142 2.3435 2.3833 -0.7579 -0.4358 0.1340  54  LEU F CG  
11831 C CD1 . LEU F 54  ? 3.0080 2.3735 2.2741 -0.7974 -0.3698 0.1575  54  LEU F CD1 
11832 C CD2 . LEU F 54  ? 3.2229 2.4409 2.4747 -0.7693 -0.5140 0.1328  54  LEU F CD2 
11833 N N   . GLN F 55  ? 2.7433 2.3974 2.3176 -0.7745 -0.2465 0.1535  55  GLN F N   
11834 C CA  . GLN F 55  ? 2.5283 2.3030 2.2249 -0.7627 -0.1709 0.1574  55  GLN F CA  
11835 C C   . GLN F 55  ? 2.4240 2.2336 2.2329 -0.7293 -0.1442 0.1494  55  GLN F C   
11836 O O   . GLN F 55  ? 2.5089 2.2661 2.2629 -0.7298 -0.1590 0.1496  55  GLN F O   
11837 C CB  . GLN F 55  ? 2.4973 2.3228 2.0994 -0.8022 -0.1071 0.1822  55  GLN F CB  
11838 C CG  . GLN F 55  ? 2.2840 2.2319 1.9916 -0.7925 -0.0235 0.1906  55  GLN F CG  
11839 C CD  . GLN F 55  ? 2.1399 2.1554 1.9809 -0.7719 -0.0096 0.1821  55  GLN F CD  
11840 O OE1 . GLN F 55  ? 2.1969 2.1717 2.0433 -0.7690 -0.0615 0.1699  55  GLN F OE1 
11841 N NE2 . GLN F 55  ? 1.9560 2.0742 1.9045 -0.7568 0.0609  0.1883  55  GLN F NE2 
11842 N N   . SER F 56  ? 2.4339 2.3306 2.4032 -0.6993 -0.1037 0.1420  56  SER F N   
11843 C CA  . SER F 56  ? 2.3214 2.2589 2.4098 -0.6651 -0.0694 0.1347  56  SER F CA  
11844 C C   . SER F 56  ? 2.3252 2.2772 2.3327 -0.6818 -0.0205 0.1510  56  SER F C   
11845 O O   . SER F 56  ? 2.2972 2.2995 2.2380 -0.7095 0.0310  0.1705  56  SER F O   
11846 C CB  . SER F 56  ? 2.1215 2.1621 2.3758 -0.6383 -0.0154 0.1311  56  SER F CB  
11847 O OG  . SER F 56  ? 2.0793 2.1537 2.4546 -0.6022 0.0171  0.1229  56  SER F OG  
11848 N N   . GLY F 57  ? 2.4331 2.3410 2.4505 -0.6640 -0.0374 0.1419  57  GLY F N   
11849 C CA  . GLY F 57  ? 2.4586 2.3762 2.4104 -0.6751 0.0048  0.1530  57  GLY F CA  
11850 C C   . GLY F 57  ? 2.6106 2.4483 2.3857 -0.7132 -0.0275 0.1626  57  GLY F C   
11851 O O   . GLY F 57  ? 2.6462 2.4786 2.3669 -0.7207 -0.0028 0.1679  57  GLY F O   
11852 N N   . VAL F 58  ? 2.5453 2.3191 2.2284 -0.7370 -0.0805 0.1647  58  VAL F N   
11853 C CA  . VAL F 58  ? 2.7300 2.4209 2.2439 -0.7735 -0.1114 0.1746  58  VAL F CA  
11854 C C   . VAL F 58  ? 2.8406 2.4403 2.3450 -0.7561 -0.1685 0.1605  58  VAL F C   
11855 O O   . VAL F 58  ? 2.8461 2.4134 2.4364 -0.7255 -0.2172 0.1430  58  VAL F O   
11856 C CB  . VAL F 58  ? 2.8420 2.4920 2.2600 -0.8031 -0.1459 0.1822  58  VAL F CB  
11857 C CG1 . VAL F 58  ? 3.0439 2.5993 2.2907 -0.8386 -0.1791 0.1922  58  VAL F CG1 
11858 C CG2 . VAL F 58  ? 2.7293 2.4714 2.1567 -0.8218 -0.0853 0.1966  58  VAL F CG2 
11859 N N   . PRO F 59  ? 2.8132 2.3699 2.2198 -0.7741 -0.1655 0.1666  59  PRO F N   
11860 C CA  . PRO F 59  ? 2.9182 2.3897 2.3200 -0.7568 -0.2166 0.1533  59  PRO F CA  
11861 C C   . PRO F 59  ? 3.0863 2.4544 2.4319 -0.7584 -0.3006 0.1474  59  PRO F C   
11862 O O   . PRO F 59  ? 3.1846 2.5196 2.4275 -0.7875 -0.3202 0.1584  59  PRO F O   
11863 C CB  . PRO F 59  ? 2.9964 2.4455 2.2819 -0.7852 -0.1920 0.1643  59  PRO F CB  
11864 C CG  . PRO F 59  ? 2.8662 2.4157 2.1516 -0.8021 -0.1150 0.1782  59  PRO F CG  
11865 C CD  . PRO F 59  ? 2.8052 2.4010 2.1225 -0.8068 -0.1085 0.1840  59  PRO F CD  
11866 N N   . SER F 60  ? 3.0526 2.3678 2.4674 -0.7255 -0.3502 0.1294  60  SER F N   
11867 C CA  . SER F 60  ? 3.2046 2.4207 2.5843 -0.7187 -0.4355 0.1208  60  SER F CA  
11868 C C   . SER F 60  ? 3.4081 2.5225 2.6068 -0.7538 -0.4725 0.1343  60  SER F C   
11869 O O   . SER F 60  ? 3.5649 2.5948 2.7040 -0.7549 -0.5399 0.1321  60  SER F O   
11870 C CB  . SER F 60  ? 3.2485 2.4340 2.7483 -0.6750 -0.4759 0.0985  60  SER F CB  
11871 O OG  . SER F 60  ? 3.3511 2.5190 2.8373 -0.6725 -0.4575 0.0978  60  SER F OG  
11872 N N   . ARG F 61  ? 3.3094 2.4273 2.4193 -0.7817 -0.4308 0.1476  61  ARG F N   
11873 C CA  . ARG F 61  ? 3.5187 2.5407 2.4597 -0.8164 -0.4608 0.1610  61  ARG F CA  
11874 C C   . ARG F 61  ? 3.5903 2.6007 2.4235 -0.8509 -0.4616 0.1771  61  ARG F C   
11875 O O   . ARG F 61  ? 3.7679 2.6871 2.4603 -0.8776 -0.4946 0.1882  61  ARG F O   
11876 C CB  . ARG F 61  ? 3.5039 2.5377 2.3895 -0.8366 -0.4141 0.1687  61  ARG F CB  
11877 C CG  . ARG F 61  ? 3.3697 2.5069 2.2548 -0.8588 -0.3348 0.1806  61  ARG F CG  
11878 C CD  . ARG F 61  ? 3.3881 2.5340 2.2229 -0.8757 -0.2943 0.1849  61  ARG F CD  
11879 N NE  . ARG F 61  ? 3.2560 2.5041 2.0981 -0.8933 -0.2202 0.1949  61  ARG F NE  
11880 C CZ  . ARG F 61  ? 3.0725 2.4179 2.0332 -0.8681 -0.1702 0.1886  61  ARG F CZ  
11881 N NH1 . ARG F 61  ? 3.0518 2.4053 2.1363 -0.8254 -0.1839 0.1717  61  ARG F NH1 
11882 N NH2 . ARG F 61  ? 2.9998 2.4325 1.9558 -0.8850 -0.1058 0.1994  61  ARG F NH2 
11883 N N   . PHE F 62  ? 3.4295 2.5280 2.3262 -0.8506 -0.4244 0.1789  62  PHE F N   
11884 C CA  . PHE F 62  ? 3.4935 2.5863 2.3070 -0.8788 -0.4258 0.1914  62  PHE F CA  
11885 C C   . PHE F 62  ? 3.5526 2.5961 2.3980 -0.8559 -0.4936 0.1788  62  PHE F C   
11886 O O   . PHE F 62  ? 3.4605 2.5414 2.4492 -0.8174 -0.5077 0.1606  62  PHE F O   
11887 C CB  . PHE F 62  ? 3.3084 2.5222 2.1782 -0.8894 -0.3516 0.1991  62  PHE F CB  
11888 C CG  . PHE F 62  ? 3.2750 2.5355 2.0917 -0.9178 -0.2868 0.2134  62  PHE F CG  
11889 C CD1 . PHE F 62  ? 3.3841 2.6190 2.0612 -0.9628 -0.2703 0.2319  62  PHE F CD1 
11890 C CD2 . PHE F 62  ? 3.1572 2.4864 2.0641 -0.8991 -0.2419 0.2077  62  PHE F CD2 
11891 C CE1 . PHE F 62  ? 3.3597 2.6377 1.9924 -0.9888 -0.2137 0.2433  62  PHE F CE1 
11892 C CE2 . PHE F 62  ? 3.1262 2.4972 1.9819 -0.9242 -0.1858 0.2193  62  PHE F CE2 
11893 C CZ  . PHE F 62  ? 3.2356 2.5821 1.9565 -0.9692 -0.1731 0.2366  62  PHE F CZ  
11894 N N   . SER F 63  ? 3.3721 2.3296 2.0841 -0.8789 -0.5356 0.1879  63  SER F N   
11895 C CA  . SER F 63  ? 3.4411 2.3529 2.1642 -0.8616 -0.5981 0.1771  63  SER F CA  
11896 C C   . SER F 63  ? 3.5712 2.4420 2.1486 -0.8992 -0.5996 0.1937  63  SER F C   
11897 O O   . SER F 63  ? 3.6458 2.4995 2.1038 -0.9373 -0.5650 0.2131  63  SER F O   
11898 C CB  . SER F 63  ? 3.5899 2.3951 2.3047 -0.8348 -0.6805 0.1643  63  SER F CB  
11899 O OG  . SER F 63  ? 3.8013 2.5010 2.3509 -0.8617 -0.7055 0.1796  63  SER F OG  
11900 N N   . ALA F 64  ? 3.5641 2.4176 2.1536 -0.8879 -0.6399 0.1849  64  ALA F N   
11901 C CA  . ALA F 64  ? 3.6733 2.4892 2.1308 -0.9210 -0.6404 0.1989  64  ALA F CA  
11902 C C   . ALA F 64  ? 3.7927 2.5339 2.2345 -0.9001 -0.7195 0.1850  64  ALA F C   
11903 O O   . ALA F 64  ? 3.7261 2.4853 2.2975 -0.8603 -0.7579 0.1627  64  ALA F O   
11904 C CB  . ALA F 64  ? 3.4768 2.4069 1.9778 -0.9407 -0.5655 0.2066  64  ALA F CB  
11905 N N   . THR F 65  ? 3.7462 2.4019 2.0274 -0.9269 -0.7429 0.1979  65  THR F N   
11906 C CA  . THR F 65  ? 3.8941 2.4601 2.1239 -0.9109 -0.8216 0.1872  65  THR F CA  
11907 C C   . THR F 65  ? 3.8806 2.4326 1.9969 -0.9428 -0.8043 0.1993  65  THR F C   
11908 O O   . THR F 65  ? 3.7707 2.3686 1.8338 -0.9798 -0.7351 0.2180  65  THR F O   
11909 C CB  . THR F 65  ? 4.1995 2.6280 2.3176 -0.9044 -0.8910 0.1906  65  THR F CB  
11910 O OG1 . THR F 65  ? 4.3768 2.7397 2.3181 -0.9470 -0.8659 0.2168  65  THR F OG1 
11911 C CG2 . THR F 65  ? 4.2037 2.6420 2.4231 -0.8771 -0.9026 0.1806  65  THR F CG2 
11912 N N   . GLY F 66  ? 3.9545 2.4415 2.0357 -0.9272 -0.8694 0.1872  66  GLY F N   
11913 C CA  . GLY F 66  ? 3.9679 2.4123 1.9162 -0.9553 -0.8664 0.1979  66  GLY F CA  
11914 C C   . GLY F 66  ? 3.8380 2.3406 1.8610 -0.9444 -0.8687 0.1814  66  GLY F C   
11915 O O   . GLY F 66  ? 3.6890 2.2946 1.8857 -0.9202 -0.8519 0.1639  66  GLY F O   
11916 N N   . SER F 67  ? 3.9931 2.4259 1.8804 -0.9627 -0.8882 0.1872  67  SER F N   
11917 C CA  . SER F 67  ? 3.9621 2.4364 1.8889 -0.9588 -0.8893 0.1734  67  SER F CA  
11918 C C   . SER F 67  ? 4.0535 2.4596 1.7932 -0.9982 -0.8723 0.1929  67  SER F C   
11919 O O   . SER F 67  ? 4.1417 2.4657 1.7623 -1.0100 -0.8624 0.2145  67  SER F O   
11920 C CB  . SER F 67  ? 4.0117 2.4442 2.0060 -0.9139 -0.9794 0.1433  67  SER F CB  
11921 O OG  . SER F 67  ? 3.9097 2.4465 2.1160 -0.8806 -0.9738 0.1213  67  SER F OG  
11922 N N   . GLY F 68  ? 4.0589 2.5132 1.8165 -1.0064 -0.8504 0.1863  68  GLY F N   
11923 C CA  . GLY F 68  ? 4.1260 2.5314 1.7658 -1.0247 -0.8144 0.2044  68  GLY F CA  
11924 C C   . GLY F 68  ? 4.0733 2.5204 1.6838 -1.0602 -0.7168 0.2319  68  GLY F C   
11925 O O   . GLY F 68  ? 3.9539 2.5097 1.6298 -1.0829 -0.6548 0.2356  68  GLY F O   
11926 N N   . THR F 69  ? 4.2257 2.5898 1.7499 -1.0642 -0.7029 0.2478  69  THR F N   
11927 C CA  . THR F 69  ? 4.1837 2.5821 1.7000 -1.0940 -0.6175 0.2642  69  THR F CA  
11928 C C   . THR F 69  ? 4.1965 2.5870 1.7141 -1.1001 -0.6055 0.2736  69  THR F C   
11929 O O   . THR F 69  ? 4.1526 2.5833 1.6849 -1.1221 -0.5380 0.2803  69  THR F O   
11930 C CB  . THR F 69  ? 4.3564 2.6767 1.7872 -1.0988 -0.6028 0.2683  69  THR F CB  
11931 O OG1 . THR F 69  ? 4.5645 2.7593 1.9090 -1.0783 -0.6663 0.2703  69  THR F OG1 
11932 C CG2 . THR F 69  ? 4.3485 2.6811 1.7761 -1.0958 -0.6051 0.2594  69  THR F CG2 
11933 N N   . HIS F 70  ? 4.3400 2.6834 1.8523 -1.0795 -0.6709 0.2700  70  HIS F N   
11934 C CA  . HIS F 70  ? 4.4336 2.7534 1.9333 -1.0844 -0.6645 0.2791  70  HIS F CA  
11935 C C   . HIS F 70  ? 4.3841 2.7589 1.9564 -1.0760 -0.6917 0.2718  70  HIS F C   
11936 O O   . HIS F 70  ? 4.4506 2.8019 2.0496 -1.0502 -0.7679 0.2539  70  HIS F O   
11937 C CB  . HIS F 70  ? 4.7023 2.8846 2.1057 -1.0679 -0.7198 0.2825  70  HIS F CB  
11938 C CG  . HIS F 70  ? 4.8341 2.9815 2.2177 -1.0727 -0.7186 0.2910  70  HIS F CG  
11939 N ND1 . HIS F 70  ? 4.9947 3.1048 2.3884 -1.0512 -0.7836 0.2859  70  HIS F ND1 
11940 C CD2 . HIS F 70  ? 4.8547 2.9995 2.2154 -1.0955 -0.6634 0.3003  70  HIS F CD2 
11941 C CE1 . HIS F 70  ? 5.0518 3.1344 2.4194 -1.0623 -0.7654 0.2957  70  HIS F CE1 
11942 N NE2 . HIS F 70  ? 4.9757 3.0794 2.3239 -1.0893 -0.6930 0.3039  70  HIS F NE2 
11943 N N   . PHE F 71  ? 4.3143 2.7659 1.9309 -1.0961 -0.6310 0.2805  71  PHE F N   
11944 C CA  . PHE F 71  ? 4.2429 2.7635 1.9386 -1.0913 -0.6403 0.2735  71  PHE F CA  
11945 C C   . PHE F 71  ? 4.3030 2.8131 1.9774 -1.1033 -0.6134 0.2856  71  PHE F C   
11946 O O   . PHE F 71  ? 4.2855 2.7986 1.9393 -1.1212 -0.5531 0.2958  71  PHE F O   
11947 C CB  . PHE F 71  ? 3.9689 2.6355 1.7937 -1.0952 -0.5727 0.2696  71  PHE F CB  
11948 C CG  . PHE F 71  ? 3.8952 2.5842 1.7573 -1.0837 -0.5900 0.2564  71  PHE F CG  
11949 C CD1 . PHE F 71  ? 3.8720 2.5409 1.6356 -1.1128 -0.5652 0.2675  71  PHE F CD1 
11950 C CD2 . PHE F 71  ? 3.8412 2.5721 1.8495 -1.0408 -0.6283 0.2313  71  PHE F CD2 
11951 C CE1 . PHE F 71  ? 3.8055 2.4899 1.5895 -1.1056 -0.5844 0.2548  71  PHE F CE1 
11952 C CE2 . PHE F 71  ? 3.7873 2.5381 1.8323 -1.0305 -0.6456 0.2173  71  PHE F CE2 
11953 C CZ  . PHE F 71  ? 3.7616 2.4889 1.6924 -1.0628 -0.6242 0.2288  71  PHE F CZ  
11954 N N   . THR F 72  ? 4.0194 2.5449 1.7920 -1.0725 -0.6394 0.2726  72  THR F N   
11955 C CA  . THR F 72  ? 4.0079 2.5360 1.7770 -1.0815 -0.6131 0.2808  72  THR F CA  
11956 C C   . THR F 72  ? 3.8761 2.5176 1.8236 -1.0540 -0.5847 0.2663  72  THR F C   
11957 O O   . THR F 72  ? 3.8228 2.5097 1.8979 -1.0183 -0.6086 0.2470  72  THR F O   
11958 C CB  . THR F 72  ? 4.2784 2.6758 1.9602 -1.0706 -0.6793 0.2818  72  THR F CB  
11959 O OG1 . THR F 72  ? 4.3516 2.7298 2.1278 -1.0239 -0.7471 0.2596  72  THR F OG1 
11960 C CG2 . THR F 72  ? 4.4188 2.7092 1.9553 -1.0881 -0.6926 0.2956  72  THR F CG2 
11961 N N   . LEU F 73  ? 4.0580 2.7429 2.0121 -1.0710 -0.5325 0.2754  73  LEU F N   
11962 C CA  . LEU F 73  ? 3.9523 2.7282 2.0532 -1.0463 -0.5043 0.2637  73  LEU F CA  
11963 C C   . LEU F 73  ? 4.1245 2.8367 2.1812 -1.0465 -0.5202 0.2660  73  LEU F C   
11964 O O   . LEU F 73  ? 4.2048 2.8657 2.1364 -1.0816 -0.5031 0.2827  73  LEU F O   
11965 C CB  . LEU F 73  ? 3.7145 2.6167 1.8730 -1.0656 -0.4195 0.2714  73  LEU F CB  
11966 C CG  . LEU F 73  ? 3.5916 2.5886 1.8828 -1.0446 -0.3791 0.2630  73  LEU F CG  
11967 C CD1 . LEU F 73  ? 3.5052 2.5673 1.9606 -1.0006 -0.3918 0.2433  73  LEU F CD1 
11968 C CD2 . LEU F 73  ? 3.4686 2.5593 1.7589 -1.0742 -0.2980 0.2767  73  LEU F CD2 
11969 N N   . THR F 74  ? 3.8992 2.6149 2.0612 -1.0080 -0.5505 0.2489  74  THR F N   
11970 C CA  . THR F 74  ? 3.9819 2.6345 2.1119 -1.0042 -0.5703 0.2485  74  THR F CA  
11971 C C   . THR F 74  ? 3.8082 2.5532 2.0724 -0.9838 -0.5291 0.2375  74  THR F C   
11972 O O   . THR F 74  ? 3.7239 2.5442 2.1306 -0.9516 -0.5233 0.2225  74  THR F O   
11973 C CB  . THR F 74  ? 4.1321 2.6752 2.2458 -0.9750 -0.6576 0.2379  74  THR F CB  
11974 O OG1 . THR F 74  ? 4.3559 2.8024 2.3260 -0.9948 -0.6955 0.2499  74  THR F OG1 
11975 C CG2 . THR F 74  ? 4.2245 2.7068 2.3192 -0.9683 -0.6772 0.2364  74  THR F CG2 
11976 N N   . VAL F 75  ? 4.0291 2.7657 2.2471 -1.0019 -0.5000 0.2445  75  VAL F N   
11977 C CA  . VAL F 75  ? 3.8963 2.6924 2.2208 -0.9803 -0.4724 0.2329  75  VAL F CA  
11978 C C   . VAL F 75  ? 4.0300 2.7279 2.3264 -0.9656 -0.5244 0.2261  75  VAL F C   
11979 O O   . VAL F 75  ? 4.2056 2.8199 2.3737 -0.9928 -0.5371 0.2380  75  VAL F O   
11980 C CB  . VAL F 75  ? 3.7993 2.6713 2.1043 -1.0099 -0.3963 0.2432  75  VAL F CB  
11981 C CG1 . VAL F 75  ? 3.6550 2.5967 2.0775 -0.9834 -0.3648 0.2298  75  VAL F CG1 
11982 C CG2 . VAL F 75  ? 3.7285 2.6856 2.0407 -1.0294 -0.3476 0.2532  75  VAL F CG2 
11983 N N   . SER F 76  ? 3.8401 2.5470 2.2595 -0.9226 -0.5536 0.2069  76  SER F N   
11984 C CA  . SER F 76  ? 4.0069 2.6157 2.4079 -0.9049 -0.6110 0.1993  76  SER F CA  
11985 C C   . SER F 76  ? 4.0622 2.6627 2.4243 -0.9208 -0.5787 0.2026  76  SER F C   
11986 O O   . SER F 76  ? 4.2427 2.7428 2.5083 -0.9319 -0.6139 0.2079  76  SER F O   
11987 C CB  . SER F 76  ? 3.9578 2.5845 2.5119 -0.8547 -0.6468 0.1768  76  SER F CB  
11988 O OG  . SER F 76  ? 3.7911 2.5277 2.4777 -0.8370 -0.5892 0.1666  76  SER F OG  
11989 N N   . SER F 77  ? 4.1512 2.8547 2.5868 -0.9210 -0.5124 0.1990  77  SER F N   
11990 C CA  . SER F 77  ? 4.1931 2.8989 2.5860 -0.9399 -0.4753 0.2016  77  SER F CA  
11991 C C   . SER F 77  ? 4.0325 2.8514 2.4449 -0.9595 -0.3967 0.2077  77  SER F C   
11992 O O   . SER F 77  ? 3.8761 2.7899 2.4106 -0.9347 -0.3618 0.1983  77  SER F O   
11993 C CB  . SER F 77  ? 4.2264 2.9215 2.7112 -0.9045 -0.4906 0.1830  77  SER F CB  
11994 O OG  . SER F 77  ? 4.3077 2.9827 2.7363 -0.9228 -0.4670 0.1841  77  SER F OG  
11995 N N   . LEU F 78  ? 4.1536 2.9615 2.4486 -1.0031 -0.3687 0.2237  78  LEU F N   
11996 C CA  . LEU F 78  ? 4.0087 2.9199 2.3129 -1.0244 -0.2976 0.2306  78  LEU F CA  
11997 C C   . LEU F 78  ? 3.9439 2.9204 2.3211 -1.0096 -0.2551 0.2188  78  LEU F C   
11998 O O   . LEU F 78  ? 4.0597 2.9836 2.4117 -1.0080 -0.2689 0.2117  78  LEU F O   
11999 C CB  . LEU F 78  ? 4.0834 2.9599 2.2464 -1.0749 -0.2801 0.2488  78  LEU F CB  
12000 C CG  . LEU F 78  ? 4.1056 2.9473 2.1866 -1.0993 -0.2950 0.2644  78  LEU F CG  
12001 C CD1 . LEU F 78  ? 4.2393 3.0140 2.1744 -1.1459 -0.2879 0.2801  78  LEU F CD1 
12002 C CD2 . LEU F 78  ? 3.9128 2.8657 2.0573 -1.1008 -0.2480 0.2684  78  LEU F CD2 
12003 N N   . GLN F 79  ? 3.8787 2.9682 2.3439 -0.9985 -0.2024 0.2170  79  GLN F N   
12004 C CA  . GLN F 79  ? 3.8032 2.9676 2.3278 -0.9874 -0.1514 0.2085  79  GLN F CA  
12005 C C   . GLN F 79  ? 3.7237 2.9575 2.1957 -1.0222 -0.0936 0.2211  79  GLN F C   
12006 O O   . GLN F 79  ? 3.6886 2.9333 2.1114 -1.0479 -0.0867 0.2354  79  GLN F O   
12007 C CB  . GLN F 79  ? 3.6665 2.9069 2.3429 -0.9417 -0.1339 0.1962  79  GLN F CB  
12008 C CG  . GLN F 79  ? 3.7344 2.9137 2.4791 -0.9054 -0.1908 0.1824  79  GLN F CG  
12009 C CD  . GLN F 79  ? 3.6107 2.8641 2.5110 -0.8603 -0.1671 0.1685  79  GLN F CD  
12010 O OE1 . GLN F 79  ? 3.4749 2.8249 2.4283 -0.8554 -0.1068 0.1706  79  GLN F OE1 
12011 N NE2 . GLN F 79  ? 3.6642 2.8710 2.6396 -0.8264 -0.2138 0.1544  79  GLN F NE2 
12012 N N   . PRO F 80  ? 3.8512 3.1292 2.3283 -1.0245 -0.0528 0.2154  80  PRO F N   
12013 C CA  . PRO F 80  ? 3.7903 3.1301 2.2134 -1.0588 -0.0020 0.2264  80  PRO F CA  
12014 C C   . PRO F 80  ? 3.6224 3.0522 2.0892 -1.0607 0.0341  0.2378  80  PRO F C   
12015 O O   . PRO F 80  ? 3.6043 3.0530 2.0049 -1.0956 0.0551  0.2505  80  PRO F O   
12016 C CB  . PRO F 80  ? 3.7748 3.1603 2.2333 -1.0448 0.0335  0.2135  80  PRO F CB  
12017 C CG  . PRO F 80  ? 3.9096 3.2129 2.3766 -1.0240 -0.0094 0.1988  80  PRO F CG  
12018 C CD  . PRO F 80  ? 3.9074 3.1723 2.4285 -0.9988 -0.0542 0.1981  80  PRO F CD  
12019 N N   . GLU F 81  ? 3.7517 3.2386 2.3351 -1.0228 0.0430  0.2324  81  GLU F N   
12020 C CA  . GLU F 81  ? 3.5931 3.1670 2.2231 -1.0239 0.0793  0.2432  81  GLU F CA  
12021 C C   . GLU F 81  ? 3.6127 3.1451 2.1972 -1.0431 0.0475  0.2541  81  GLU F C   
12022 O O   . GLU F 81  ? 3.4956 3.0936 2.1040 -1.0505 0.0767  0.2642  81  GLU F O   
12023 C CB  . GLU F 81  ? 3.4580 3.1072 2.2308 -0.9776 0.1027  0.2346  81  GLU F CB  
12024 C CG  . GLU F 81  ? 3.4887 3.0898 2.3389 -0.9416 0.0552  0.2219  81  GLU F CG  
12025 C CD  . GLU F 81  ? 3.5851 3.1506 2.4722 -0.9140 0.0418  0.2051  81  GLU F CD  
12026 O OE1 . GLU F 81  ? 3.6636 3.1974 2.4759 -0.9319 0.0455  0.2031  81  GLU F OE1 
12027 O OE2 . GLU F 81  ? 3.6050 3.1756 2.6008 -0.8743 0.0291  0.1929  81  GLU F OE2 
12028 N N   . ASP F 82  ? 3.4758 2.9003 1.9938 -1.0506 -0.0106 0.2524  82  ASP F N   
12029 C CA  . ASP F 82  ? 3.5106 2.8874 1.9793 -1.0659 -0.0441 0.2616  82  ASP F CA  
12030 C C   . ASP F 82  ? 3.5795 2.9248 1.9178 -1.1161 -0.0337 0.2781  82  ASP F C   
12031 O O   . ASP F 82  ? 3.5970 2.9159 1.9089 -1.1216 -0.0556 0.2798  82  ASP F O   
12032 C CB  . ASP F 82  ? 3.6449 2.9170 2.1041 -1.0467 -0.1147 0.2525  82  ASP F CB  
12033 C CG  . ASP F 82  ? 3.5817 2.8804 2.1776 -0.9967 -0.1285 0.2353  82  ASP F CG  
12034 O OD1 . ASP F 82  ? 3.4212 2.8171 2.1221 -0.9764 -0.0885 0.2328  82  ASP F OD1 
12035 O OD2 . ASP F 82  ? 3.6968 2.9180 2.2973 -0.9775 -0.1788 0.2245  82  ASP F OD2 
12036 N N   . PHE F 83  ? 3.6941 3.0669 2.0365 -1.1123 -0.0121 0.2608  83  PHE F N   
12037 C CA  . PHE F 83  ? 3.7172 3.0905 2.0458 -1.1147 -0.0129 0.2442  83  PHE F CA  
12038 C C   . PHE F 83  ? 3.5346 3.0241 1.9632 -1.0894 0.0249  0.2317  83  PHE F C   
12039 O O   . PHE F 83  ? 3.4226 2.9988 1.9247 -1.0671 0.0609  0.2227  83  PHE F O   
12040 C CB  . PHE F 83  ? 3.8123 3.1589 2.1061 -1.1237 -0.0098 0.2332  83  PHE F CB  
12041 C CG  . PHE F 83  ? 4.0113 3.2307 2.1987 -1.1472 -0.0523 0.2447  83  PHE F CG  
12042 C CD1 . PHE F 83  ? 4.0677 3.2485 2.2287 -1.1500 -0.0620 0.2573  83  PHE F CD1 
12043 C CD2 . PHE F 83  ? 4.1489 3.2820 2.2629 -1.1645 -0.0831 0.2440  83  PHE F CD2 
12044 C CE1 . PHE F 83  ? 4.2531 3.3134 2.3289 -1.1612 -0.1088 0.2643  83  PHE F CE1 
12045 C CE2 . PHE F 83  ? 4.3385 3.3495 2.3547 -1.1810 -0.1257 0.2546  83  PHE F CE2 
12046 C CZ  . PHE F 83  ? 4.3947 3.3651 2.3826 -1.1809 -0.1412 0.2668  83  PHE F CZ  
12047 N N   . ALA F 84  ? 3.4848 2.9699 1.9124 -1.0907 0.0144  0.2313  84  ALA F N   
12048 C CA  . ALA F 84  ? 3.3185 2.8995 1.8348 -1.0661 0.0424  0.2244  84  ALA F CA  
12049 C C   . ALA F 84  ? 3.3627 2.9025 1.8428 -1.0775 0.0218  0.2237  84  ALA F C   
12050 O O   . ALA F 84  ? 3.5169 2.9591 1.9085 -1.1017 -0.0110 0.2280  84  ALA F O   
12051 C CB  . ALA F 84  ? 3.2030 2.8393 1.7814 -1.0508 0.0586  0.2353  84  ALA F CB  
12052 N N   . THR F 85  ? 3.1582 2.7690 1.7058 -1.0582 0.0412  0.2184  85  THR F N   
12053 C CA  . THR F 85  ? 3.1941 2.7706 1.7117 -1.0681 0.0247  0.2182  85  THR F CA  
12054 C C   . THR F 85  ? 3.1700 2.7389 1.6870 -1.0717 0.0109  0.2322  85  THR F C   
12055 O O   . THR F 85  ? 3.0986 2.7361 1.6855 -1.0545 0.0322  0.2367  85  THR F O   
12056 C CB  . THR F 85  ? 3.0865 2.7370 1.6724 -1.0462 0.0519  0.2039  85  THR F CB  
12057 O OG1 . THR F 85  ? 3.1256 2.7748 1.7060 -1.0471 0.0603  0.1929  85  THR F OG1 
12058 C CG2 . THR F 85  ? 3.1273 2.7442 1.6837 -1.0564 0.0381  0.2037  85  THR F CG2 
12059 N N   . TYR F 86  ? 3.1926 2.6742 1.6301 -1.0937 -0.0250 0.2398  86  TYR F N   
12060 C CA  . TYR F 86  ? 3.1935 2.6470 1.6112 -1.1022 -0.0487 0.2548  86  TYR F CA  
12061 C C   . TYR F 86  ? 3.1878 2.6392 1.5999 -1.1040 -0.0523 0.2492  86  TYR F C   
12062 O O   . TYR F 86  ? 3.2865 2.6885 1.6497 -1.1127 -0.0614 0.2415  86  TYR F O   
12063 C CB  . TYR F 86  ? 3.3686 2.6971 1.6786 -1.1246 -0.1020 0.2726  86  TYR F CB  
12064 C CG  . TYR F 86  ? 3.4251 2.7465 1.7364 -1.1247 -0.1023 0.2821  86  TYR F CG  
12065 C CD1 . TYR F 86  ? 3.4885 2.7879 1.7745 -1.1267 -0.0972 0.2737  86  TYR F CD1 
12066 C CD2 . TYR F 86  ? 3.3400 2.6732 1.6827 -1.1241 -0.1067 0.3005  86  TYR F CD2 
12067 C CE1 . TYR F 86  ? 3.5088 2.7990 1.7930 -1.1273 -0.0962 0.2817  86  TYR F CE1 
12068 C CE2 . TYR F 86  ? 3.3285 2.6709 1.7350 -1.0978 -0.1096 0.2892  86  TYR F CE2 
12069 C CZ  . TYR F 86  ? 3.4202 2.7281 1.7556 -1.1166 -0.1009 0.2929  86  TYR F CZ  
12070 O OH  . TYR F 86  ? 3.4231 2.7384 1.8197 -1.0905 -0.1029 0.2807  86  TYR F OH  
12071 N N   . PHE F 87  ? 3.2456 2.7509 1.7106 -1.0964 -0.0426 0.2536  87  PHE F N   
12072 C CA  . PHE F 87  ? 3.2342 2.7419 1.6975 -1.0981 -0.0449 0.2489  87  PHE F CA  
12073 C C   . PHE F 87  ? 3.2884 2.7371 1.7007 -1.1160 -0.0832 0.2668  87  PHE F C   
12074 O O   . PHE F 87  ? 3.2459 2.7049 1.6798 -1.1185 -0.0894 0.2826  87  PHE F O   
12075 C CB  . PHE F 87  ? 3.0461 2.6760 1.6251 -1.0688 0.0015  0.2362  87  PHE F CB  
12076 C CG  . PHE F 87  ? 2.9974 2.6771 1.6219 -1.0474 0.0307  0.2200  87  PHE F CG  
12077 C CD1 . PHE F 87  ? 3.0479 2.7081 1.6509 -1.0495 0.0318  0.2092  87  PHE F CD1 
12078 C CD2 . PHE F 87  ? 2.9085 2.6512 1.5966 -1.0252 0.0562  0.2170  87  PHE F CD2 
12079 C CE1 . PHE F 87  ? 3.0098 2.7108 1.6531 -1.0319 0.0548  0.1970  87  PHE F CE1 
12080 C CE2 . PHE F 87  ? 2.8726 2.6536 1.5967 -1.0062 0.0773  0.2041  87  PHE F CE2 
12081 C CZ  . PHE F 87  ? 2.9229 2.6827 1.6247 -1.0105 0.0754  0.1946  87  PHE F CZ  
12082 N N   . CYS F 88  ? 3.2670 2.6512 1.6137 -1.1281 -0.1096 0.2658  88  CYS F N   
12083 C CA  . CYS F 88  ? 3.3020 2.6411 1.6075 -1.1400 -0.1461 0.2796  88  CYS F CA  
12084 C C   . CYS F 88  ? 3.1824 2.6015 1.5564 -1.1331 -0.1137 0.2697  88  CYS F C   
12085 O O   . CYS F 88  ? 3.1323 2.6041 1.5509 -1.1200 -0.0784 0.2519  88  CYS F O   
12086 C CB  . CYS F 88  ? 3.5174 2.7136 1.6908 -1.1525 -0.2083 0.2845  88  CYS F CB  
12087 S SG  . CYS F 88  ? 3.6194 2.7764 1.7532 -1.1555 -0.1940 0.2681  88  CYS F SG  
12088 N N   . GLN F 89  ? 3.2648 2.6886 1.6461 -1.1412 -0.1296 0.2827  89  GLN F N   
12089 C CA  . GLN F 89  ? 3.1479 2.6490 1.5991 -1.1355 -0.0994 0.2748  89  GLN F CA  
12090 C C   . GLN F 89  ? 3.2248 2.6583 1.6105 -1.1551 -0.1476 0.2898  89  GLN F C   
12091 O O   . GLN F 89  ? 3.2191 2.6362 1.6833 -1.1170 -0.1950 0.2721  89  GLN F O   
12092 C CB  . GLN F 89  ? 2.9339 2.5720 1.5333 -1.1117 -0.0436 0.2712  89  GLN F CB  
12093 C CG  . GLN F 89  ? 2.8013 2.5245 1.4866 -1.0984 -0.0125 0.2625  89  GLN F CG  
12094 C CD  . GLN F 89  ? 2.6564 2.4578 1.4579 -1.0933 0.0104  0.2736  89  GLN F CD  
12095 O OE1 . GLN F 89  ? 2.5920 2.4304 1.4571 -1.0828 0.0270  0.2793  89  GLN F OE1 
12096 N NE2 . GLN F 89  ? 2.6032 2.4328 1.4475 -1.1005 0.0140  0.2747  89  GLN F NE2 
12097 N N   . HIS F 90  ? 3.2669 2.6931 1.6300 -1.1591 -0.1476 0.2798  90  HIS F N   
12098 C CA  . HIS F 90  ? 3.3066 2.6941 1.6651 -1.1515 -0.1961 0.2725  90  HIS F CA  
12099 C C   . HIS F 90  ? 3.1262 2.6299 1.6119 -1.1453 -0.1497 0.2673  90  HIS F C   
12100 O O   . HIS F 90  ? 3.0183 2.6066 1.5423 -1.1543 -0.0850 0.2711  90  HIS F O   
12101 C CB  . HIS F 90  ? 3.5055 2.7764 1.6980 -1.1746 -0.2345 0.2759  90  HIS F CB  
12102 C CG  . HIS F 90  ? 3.4466 2.7735 1.6859 -1.1755 -0.1868 0.2626  90  HIS F CG  
12103 N ND1 . HIS F 90  ? 3.4290 2.7670 1.6662 -1.1832 -0.1957 0.2616  90  HIS F ND1 
12104 C CD2 . HIS F 90  ? 3.4040 2.7794 1.6925 -1.1656 -0.1373 0.2468  90  HIS F CD2 
12105 C CE1 . HIS F 90  ? 3.3800 2.7693 1.6645 -1.1795 -0.1492 0.2471  90  HIS F CE1 
12106 N NE2 . HIS F 90  ? 3.3643 2.7765 1.6798 -1.1662 -0.1170 0.2373  90  HIS F NE2 
12107 N N   . MET F 91  ? 3.1110 2.6272 1.7008 -1.1101 -0.1896 0.2442  91  MET F N   
12108 C CA  . MET F 91  ? 2.9568 2.5719 1.6695 -1.1011 -0.1547 0.2360  91  MET F CA  
12109 C C   . MET F 91  ? 3.0325 2.5974 1.7233 -1.0941 -0.2041 0.2176  91  MET F C   
12110 O O   . MET F 91  ? 2.9133 2.5488 1.7327 -1.0739 -0.1963 0.2022  91  MET F O   
12111 C CB  . MET F 91  ? 2.7878 2.4938 1.6879 -1.0614 -0.1416 0.2240  91  MET F CB  
12112 C CG  . MET F 91  ? 2.8533 2.4956 1.7988 -1.0222 -0.2181 0.2016  91  MET F CG  
12113 S SD  . MET F 91  ? 2.7605 2.4504 1.8132 -0.9951 -0.1995 0.2028  91  MET F SD  
12114 C CE  . MET F 91  ? 2.9179 2.5208 1.7844 -1.0305 -0.2008 0.2254  91  MET F CE  
12115 N N   . SER F 92  ? 3.0138 2.4568 1.5444 -1.1095 -0.2548 0.2183  92  SER F N   
12116 C CA  . SER F 92  ? 3.1091 2.4903 1.6140 -1.0965 -0.3148 0.1974  92  SER F CA  
12117 C C   . SER F 92  ? 3.0759 2.4975 1.5671 -1.1195 -0.2754 0.1989  92  SER F C   
12118 O O   . SER F 92  ? 3.1069 2.5082 1.6217 -1.1034 -0.3164 0.1774  92  SER F O   
12119 C CB  . SER F 92  ? 3.3498 2.5808 1.6795 -1.1033 -0.3828 0.1986  92  SER F CB  
12120 O OG  . SER F 92  ? 3.4569 2.6423 1.6254 -1.1483 -0.3455 0.2241  92  SER F OG  
12121 N N   . SER F 93  ? 3.0776 2.5560 1.5354 -1.1558 -0.1987 0.2224  93  SER F N   
12122 C CA  . SER F 93  ? 3.0581 2.5709 1.4932 -1.1813 -0.1572 0.2261  93  SER F CA  
12123 C C   . SER F 93  ? 2.9436 2.5467 1.4224 -1.1913 -0.0764 0.2362  93  SER F C   
12124 O O   . SER F 93  ? 2.9158 2.5324 1.4183 -1.1746 -0.0644 0.2349  93  SER F O   
12125 C CB  . SER F 93  ? 3.2765 2.6657 1.5353 -1.2012 -0.1989 0.2246  93  SER F CB  
12126 O OG  . SER F 93  ? 3.4046 2.7208 1.5759 -1.2058 -0.1991 0.2320  93  SER F OG  
12127 N N   . TYR F 94  ? 3.0067 2.6833 1.5588 -1.1792 -0.0369 0.2205  94  TYR F N   
12128 C CA  . TYR F 94  ? 2.8681 2.6435 1.5323 -1.1363 0.0161  0.2026  94  TYR F CA  
12129 C C   . TYR F 94  ? 2.9765 2.7006 1.5817 -1.1302 0.0170  0.1902  94  TYR F C   
12130 O O   . TYR F 94  ? 3.1237 2.7675 1.6361 -1.1526 -0.0048 0.1884  94  TYR F O   
12131 C CB  . TYR F 94  ? 2.7235 2.5985 1.5006 -1.1138 0.0544  0.1924  94  TYR F CB  
12132 C CG  . TYR F 94  ? 2.5752 2.5294 1.4664 -1.1076 0.0702  0.2009  94  TYR F CG  
12133 C CD1 . TYR F 94  ? 2.4448 2.4643 1.4344 -1.0761 0.0922  0.2049  94  TYR F CD1 
12134 C CD2 . TYR F 94  ? 2.5633 2.5289 1.4811 -1.1319 0.0654  0.2033  94  TYR F CD2 
12135 C CE1 . TYR F 94  ? 2.3054 2.3998 1.4256 -1.0652 0.1103  0.2098  94  TYR F CE1 
12136 C CE2 . TYR F 94  ? 2.4152 2.4608 1.4800 -1.1242 0.0816  0.2059  94  TYR F CE2 
12137 C CZ  . TYR F 94  ? 2.2860 2.3965 1.4547 -1.0881 0.1048  0.2084  94  TYR F CZ  
12138 O OH  . TYR F 94  ? 2.1374 2.3288 1.4709 -1.0722 0.1214  0.2057  94  TYR F OH  
12139 N N   . PRO F 95  ? 2.9486 2.7172 1.6118 -1.0982 0.0432  0.1829  95  PRO F N   
12140 C CA  . PRO F 95  ? 2.7964 2.6451 1.5573 -1.0664 0.0665  0.1851  95  PRO F CA  
12141 C C   . PRO F 95  ? 2.8605 2.6572 1.5673 -1.0842 0.0402  0.1979  95  PRO F C   
12142 O O   . PRO F 95  ? 3.0265 2.7229 1.6237 -1.1099 0.0078  0.2018  95  PRO F O   
12143 C CB  . PRO F 95  ? 2.7454 2.6342 1.5597 -1.0291 0.0956  0.1727  95  PRO F CB  
12144 C CG  . PRO F 95  ? 2.9194 2.7193 1.6330 -1.0540 0.0771  0.1689  95  PRO F CG  
12145 C CD  . PRO F 95  ? 3.0296 2.7664 1.6633 -1.0902 0.0517  0.1724  95  PRO F CD  
12146 N N   . LEU F 96  ? 2.8712 2.7308 1.6560 -1.0673 0.0546  0.2049  96  LEU F N   
12147 C CA  . LEU F 96  ? 2.9166 2.7375 1.6646 -1.0775 0.0362  0.2158  96  LEU F CA  
12148 C C   . LEU F 96  ? 2.9680 2.7668 1.6919 -1.0640 0.0417  0.2063  96  LEU F C   
12149 O O   . LEU F 96  ? 2.8846 2.7436 1.6770 -1.0308 0.0730  0.1940  96  LEU F O   
12150 C CB  . LEU F 96  ? 2.7576 2.6645 1.6169 -1.0547 0.0616  0.2228  96  LEU F CB  
12151 C CG  . LEU F 96  ? 2.7359 2.6421 1.6174 -1.0809 0.0469  0.2409  96  LEU F CG  
12152 C CD1 . LEU F 96  ? 2.7342 2.6445 1.6223 -1.0980 0.0424  0.2402  96  LEU F CD1 
12153 C CD2 . LEU F 96  ? 2.5634 2.5681 1.5872 -1.0480 0.0841  0.2428  96  LEU F CD2 
12154 N N   . THR F 97  ? 2.9963 2.7025 1.6222 -1.0887 0.0087  0.2137  97  THR F N   
12155 C CA  . THR F 97  ? 3.0510 2.7350 1.6578 -1.0799 0.0144  0.2063  97  THR F CA  
12156 C C   . THR F 97  ? 3.1067 2.7491 1.6755 -1.0892 -0.0047 0.2166  97  THR F C   
12157 O O   . THR F 97  ? 3.1599 2.7529 1.6799 -1.1094 -0.0360 0.2320  97  THR F O   
12158 C CB  . THR F 97  ? 3.2155 2.8125 1.7322 -1.0982 -0.0024 0.2015  97  THR F CB  
12159 O OG1 . THR F 97  ? 3.3742 2.8608 1.7788 -1.1286 -0.0485 0.2145  97  THR F OG1 
12160 C CG2 . THR F 97  ? 3.1745 2.8084 1.7249 -1.0895 0.0176  0.1910  97  THR F CG2 
12161 N N   . PHE F 98  ? 3.1737 2.8336 1.7644 -1.0735 0.0123  0.2089  98  PHE F N   
12162 C CA  . PHE F 98  ? 3.2230 2.8515 1.7859 -1.0783 0.0013  0.2148  98  PHE F CA  
12163 C C   . PHE F 98  ? 3.3903 2.9304 1.8673 -1.0941 -0.0160 0.2118  98  PHE F C   
12164 O O   . PHE F 98  ? 3.4233 2.9596 1.8966 -1.0914 -0.0043 0.2019  98  PHE F O   
12165 C CB  . PHE F 98  ? 3.0733 2.7974 1.7363 -1.0453 0.0373  0.2084  98  PHE F CB  
12166 C CG  . PHE F 98  ? 2.9179 2.7237 1.6688 -1.0259 0.0568  0.2138  98  PHE F CG  
12167 C CD1 . PHE F 98  ? 2.7933 2.6720 1.6232 -1.0017 0.0819  0.2079  98  PHE F CD1 
12168 C CD2 . PHE F 98  ? 2.9005 2.7083 1.6591 -1.0302 0.0522  0.2257  98  PHE F CD2 
12169 C CE1 . PHE F 98  ? 2.6530 2.6056 1.5718 -0.9806 0.1033  0.2133  98  PHE F CE1 
12170 C CE2 . PHE F 98  ? 2.7598 2.6444 1.6102 -1.0115 0.0755  0.2317  98  PHE F CE2 
12171 C CZ  . PHE F 98  ? 2.6346 2.5922 1.5675 -0.9856 0.1019  0.2251  98  PHE F CZ  
12172 N N   . GLY F 99  ? 3.1604 2.6280 1.5703 -1.1095 -0.0432 0.2213  99  GLY F N   
12173 C CA  . GLY F 99  ? 3.2343 2.6285 1.5776 -1.1199 -0.0534 0.2185  99  GLY F CA  
12174 C C   . GLY F 99  ? 3.1586 2.6178 1.5653 -1.1022 -0.0194 0.2062  99  GLY F C   
12175 O O   . GLY F 99  ? 3.0525 2.6084 1.5519 -1.0781 0.0090  0.2007  99  GLY F O   
12176 N N   . GLY F 100 ? 3.3537 2.7532 1.7061 -1.1131 -0.0242 0.2027  100 GLY F N   
12177 C CA  . GLY F 100 ? 3.3091 2.7579 1.7097 -1.1000 0.0031  0.1916  100 GLY F CA  
12178 C C   . GLY F 100 ? 3.2824 2.7489 1.7004 -1.0958 0.0054  0.1931  100 GLY F C   
12179 O O   . GLY F 100 ? 3.2361 2.7477 1.6974 -1.0836 0.0268  0.1842  100 GLY F O   
12180 N N   . GLY F 101 ? 3.3669 2.7941 1.7479 -1.1060 -0.0181 0.2050  101 GLY F N   
12181 C CA  . GLY F 101 ? 3.3498 2.7885 1.7419 -1.1034 -0.0178 0.2084  101 GLY F CA  
12182 C C   . GLY F 101 ? 3.5225 2.8650 1.8275 -1.1244 -0.0413 0.2124  101 GLY F C   
12183 O O   . GLY F 101 ? 3.6354 2.9267 1.8942 -1.1357 -0.0443 0.2080  101 GLY F O   
12184 N N   . THR F 102 ? 3.4565 2.7725 1.7387 -1.1291 -0.0575 0.2218  102 THR F N   
12185 C CA  . THR F 102 ? 3.6092 2.8404 1.8172 -1.1452 -0.0791 0.2262  102 THR F CA  
12186 C C   . THR F 102 ? 3.5325 2.8223 1.7910 -1.1354 -0.0586 0.2225  102 THR F C   
12187 O O   . THR F 102 ? 3.4508 2.7778 1.7433 -1.1264 -0.0566 0.2294  102 THR F O   
12188 C CB  . THR F 102 ? 3.7467 2.8685 1.8630 -1.1590 -0.1282 0.2434  102 THR F CB  
12189 O OG1 . THR F 102 ? 3.8412 2.8962 1.8997 -1.1671 -0.1493 0.2460  102 THR F OG1 
12190 C CG2 . THR F 102 ? 3.8957 2.9346 1.9434 -1.1705 -0.1510 0.2486  102 THR F CG2 
12191 N N   . LYS F 103 ? 3.5906 2.8876 1.8529 -1.1376 -0.0427 0.2121  103 LYS F N   
12192 C CA  . LYS F 103 ? 3.5349 2.8798 1.8367 -1.1295 -0.0246 0.2075  103 LYS F CA  
12193 C C   . LYS F 103 ? 3.6947 2.9452 1.9136 -1.1492 -0.0522 0.2159  103 LYS F C   
12194 O O   . LYS F 103 ? 3.8469 3.0154 1.9951 -1.1674 -0.0694 0.2160  103 LYS F O   
12195 C CB  . LYS F 103 ? 3.4765 2.8840 1.8310 -1.1199 0.0056  0.1917  103 LYS F CB  
12196 C CG  . LYS F 103 ? 3.4095 2.8743 1.8106 -1.1082 0.0258  0.1858  103 LYS F CG  
12197 C CD  . LYS F 103 ? 3.3425 2.8710 1.7989 -1.0958 0.0515  0.1715  103 LYS F CD  
12198 C CE  . LYS F 103 ? 3.2532 2.8490 1.7651 -1.0783 0.0721  0.1662  103 LYS F CE  
12199 N NZ  . LYS F 103 ? 3.1589 2.8268 1.7365 -1.0589 0.0951  0.1546  103 LYS F NZ  
12200 N N   . VAL F 104 ? 3.8319 3.0914 2.0589 -1.1448 -0.0558 0.2235  104 VAL F N   
12201 C CA  . VAL F 104 ? 3.9787 3.1501 2.1307 -1.1600 -0.0834 0.2325  104 VAL F CA  
12202 C C   . VAL F 104 ? 3.9508 3.1690 2.1363 -1.1566 -0.0568 0.2222  104 VAL F C   
12203 O O   . VAL F 104 ? 3.8158 3.1210 2.0737 -1.1386 -0.0293 0.2188  104 VAL F O   
12204 C CB  . VAL F 104 ? 3.9897 3.1248 2.1172 -1.1586 -0.1112 0.2503  104 VAL F CB  
12205 C CG1 . VAL F 104 ? 4.1620 3.1903 2.2028 -1.1720 -0.1481 0.2609  104 VAL F CG1 
12206 C CG2 . VAL F 104 ? 4.0013 3.1010 2.1038 -1.1598 -0.1376 0.2595  104 VAL F CG2 
12207 N N   . GLU F 105 ? 4.1855 3.3447 2.3176 -1.1736 -0.0643 0.2172  105 GLU F N   
12208 C CA  . GLU F 105 ? 4.1782 3.3732 2.3330 -1.1740 -0.0418 0.2064  105 GLU F CA  
12209 C C   . GLU F 105 ? 4.3391 3.4413 2.4148 -1.1910 -0.0673 0.2143  105 GLU F C   
12210 O O   . GLU F 105 ? 4.4844 3.4818 2.4790 -1.2038 -0.1054 0.2267  105 GLU F O   
12211 C CB  . GLU F 105 ? 4.1859 3.4040 2.3567 -1.1795 -0.0235 0.1918  105 GLU F CB  
12212 C CG  . GLU F 105 ? 4.4212 3.5359 2.5066 -1.2040 -0.0465 0.1941  105 GLU F CG  
12213 C CD  . GLU F 105 ? 4.5096 3.6261 2.5903 -1.2171 -0.0309 0.1814  105 GLU F CD  
12214 O OE1 . GLU F 105 ? 4.4543 3.6542 2.6024 -1.2064 -0.0034 0.1691  105 GLU F OE1 
12215 O OE2 . GLU F 105 ? 4.6745 3.7035 2.6804 -1.2383 -0.0484 0.1844  105 GLU F OE2 
12216 N N   . ILE F 106 ? 4.3677 3.5061 2.4658 -1.1891 -0.0477 0.2069  106 ILE F N   
12217 C CA  . ILE F 106 ? 4.5113 3.5704 2.5411 -1.2031 -0.0677 0.2131  106 ILE F CA  
12218 C C   . ILE F 106 ? 4.6632 3.6546 2.6336 -1.2260 -0.0760 0.2064  106 ILE F C   
12219 O O   . ILE F 106 ? 4.6217 3.6653 2.6288 -1.2287 -0.0503 0.1918  106 ILE F O   
12220 C CB  . ILE F 106 ? 4.4302 3.5587 2.5089 -1.1907 -0.0401 0.2077  106 ILE F CB  
12221 C CG1 . ILE F 106 ? 4.3015 3.4962 2.4408 -1.1684 -0.0277 0.2156  106 ILE F CG1 
12222 C CG2 . ILE F 106 ? 4.6229 3.6663 2.6279 -1.2056 -0.0598 0.2130  106 ILE F CG2 
12223 C CD1 . ILE F 106 ? 4.2635 3.5194 2.4467 -1.1549 0.0016  0.2119  106 ILE F CD1 
12224 N N   . LYS F 107 ? 4.5951 3.4664 2.4726 -1.2418 -0.1140 0.2180  107 LYS F N   
12225 C CA  . LYS F 107 ? 4.7576 3.5564 2.5730 -1.2643 -0.1216 0.2132  107 LYS F CA  
12226 C C   . LYS F 107 ? 4.7822 3.5957 2.5995 -1.2700 -0.1065 0.2054  107 LYS F C   
12227 O O   . LYS F 107 ? 4.7609 3.5814 2.5825 -1.2602 -0.1095 0.2109  107 LYS F O   
12228 C CB  . LYS F 107 ? 4.9534 3.6137 2.6675 -1.2754 -0.1696 0.2289  107 LYS F CB  
12229 C CG  . LYS F 107 ? 4.9858 3.6158 2.6829 -1.2726 -0.1863 0.2354  107 LYS F CG  
12230 C CD  . LYS F 107 ? 5.2793 3.7678 2.8739 -1.2788 -0.2385 0.2514  107 LYS F CD  
12231 C CE  . LYS F 107 ? 5.4996 3.9113 3.0301 -1.3003 -0.2411 0.2475  107 LYS F CE  
12232 N NZ  . LYS F 107 ? 5.7101 4.0308 3.1735 -1.3042 -0.2685 0.2557  107 LYS F NZ  
12233 N N   . ARG F 108 ? 4.8783 3.6944 2.6896 -1.2865 -0.0901 0.1924  108 ARG F N   
12234 C CA  . ARG F 108 ? 4.9432 3.7516 2.7374 -1.2976 -0.0806 0.1845  108 ARG F CA  
12235 C C   . ARG F 108 ? 5.1035 3.8416 2.8388 -1.3252 -0.0860 0.1790  108 ARG F C   
12236 O O   . ARG F 108 ? 5.1577 3.8582 2.8688 -1.3334 -0.0946 0.1812  108 ARG F O   
12237 C CB  . ARG F 108 ? 4.7777 3.7112 2.6605 -1.2835 -0.0404 0.1691  108 ARG F CB  
12238 C CG  . ARG F 108 ? 4.6658 3.6802 2.6134 -1.2794 -0.0157 0.1566  108 ARG F CG  
12239 C CD  . ARG F 108 ? 4.5914 3.6889 2.5925 -1.2766 0.0151  0.1397  108 ARG F CD  
12240 N NE  . ARG F 108 ? 4.7478 3.7847 2.6898 -1.3049 0.0116  0.1324  108 ARG F NE  
12241 C CZ  . ARG F 108 ? 4.7440 3.8183 2.7008 -1.3082 0.0295  0.1201  108 ARG F CZ  
12242 N NH1 . ARG F 108 ? 4.5930 3.7646 2.6211 -1.2823 0.0522  0.1141  108 ARG F NH1 
12243 N NH2 . ARG F 108 ? 4.8982 3.9098 2.7955 -1.3369 0.0248  0.1137  108 ARG F NH2 
12244 N N   . THR F 109 ? 5.0809 3.7992 2.7902 -1.3399 -0.0797 0.1714  109 THR F N   
12245 C CA  . THR F 109 ? 5.2363 3.8899 2.8903 -1.3681 -0.0821 0.1653  109 THR F CA  
12246 C C   . THR F 109 ? 5.1528 3.8820 2.8616 -1.3730 -0.0533 0.1502  109 THR F C   
12247 O O   . THR F 109 ? 4.9798 3.8194 2.7724 -1.3560 -0.0275 0.1406  109 THR F O   
12248 C CB  . THR F 109 ? 5.3343 3.9576 2.9529 -1.3830 -0.0793 0.1590  109 THR F CB  
12249 O OG1 . THR F 109 ? 5.1877 3.9234 2.8812 -1.3728 -0.0456 0.1436  109 THR F OG1 
12250 C CG2 . THR F 109 ? 5.4278 3.9704 2.9889 -1.3763 -0.1103 0.1744  109 THR F CG2 
12251 N N   . VAL F 110 ? 5.2211 3.8861 2.8793 -1.3951 -0.0589 0.1487  110 VAL F N   
12252 C CA  . VAL F 110 ? 5.1577 3.8807 2.8571 -1.4020 -0.0343 0.1348  110 VAL F CA  
12253 C C   . VAL F 110 ? 5.1034 3.8968 2.8452 -1.4093 -0.0090 0.1177  110 VAL F C   
12254 O O   . VAL F 110 ? 5.1816 3.9321 2.8807 -1.4264 -0.0121 0.1145  110 VAL F O   
12255 C CB  . VAL F 110 ? 5.2754 3.9044 2.9007 -1.4254 -0.0448 0.1371  110 VAL F CB  
12256 C CG1 . VAL F 110 ? 5.2256 3.9077 2.8857 -1.4361 -0.0186 0.1216  110 VAL F CG1 
12257 C CG2 . VAL F 110 ? 5.3139 3.8870 2.9064 -1.4143 -0.0674 0.1527  110 VAL F CG2 
12258 N N   . ALA F 111 ? 5.2307 4.1294 3.0542 -1.3958 0.0148  0.1068  111 ALA F N   
12259 C CA  . ALA F 111 ? 5.1719 4.1436 3.0403 -1.4004 0.0376  0.0902  111 ALA F CA  
12260 C C   . ALA F 111 ? 5.1233 4.1434 3.0292 -1.4055 0.0538  0.0789  111 ALA F C   
12261 O O   . ALA F 111 ? 4.9988 4.0729 2.9574 -1.3840 0.0592  0.0812  111 ALA F O   
12262 C CB  . ALA F 111 ? 5.0046 4.0691 2.9446 -1.3703 0.0497  0.0891  111 ALA F CB  
12263 N N   . ALA F 112 ? 5.0961 4.0944 2.9726 -1.4344 0.0613  0.0667  112 ALA F N   
12264 C CA  . ALA F 112 ? 5.0513 4.0924 2.9590 -1.4413 0.0767  0.0553  112 ALA F CA  
12265 C C   . ALA F 112 ? 4.9110 4.0711 2.9099 -1.4200 0.0947  0.0452  112 ALA F C   
12266 O O   . ALA F 112 ? 4.8719 4.0716 2.8941 -1.4124 0.0994  0.0417  112 ALA F O   
12267 C CB  . ALA F 112 ? 5.1593 4.1407 3.0060 -1.4799 0.0799  0.0447  112 ALA F CB  
12268 N N   . PRO F 113 ? 4.8761 4.0918 2.9250 -1.4086 0.1049  0.0411  113 PRO F N   
12269 C CA  . PRO F 113 ? 4.7129 4.0366 2.8453 -1.3873 0.1200  0.0325  113 PRO F CA  
12270 C C   . PRO F 113 ? 4.7600 4.1041 2.8894 -1.4120 0.1303  0.0160  113 PRO F C   
12271 O O   . PRO F 113 ? 4.8571 4.1443 2.9319 -1.4460 0.1304  0.0087  113 PRO F O   
12272 C CB  . PRO F 113 ? 4.6382 3.9954 2.8102 -1.3717 0.1253  0.0339  113 PRO F CB  
12273 C CG  . PRO F 113 ? 4.7993 4.0667 2.9001 -1.3984 0.1192  0.0359  113 PRO F CG  
12274 C CD  . PRO F 113 ? 4.9059 4.0852 2.9348 -1.4125 0.1031  0.0451  113 PRO F CD  
12275 N N   . SER F 114 ? 4.5102 3.9358 2.6971 -1.3943 0.1398  0.0103  114 SER F N   
12276 C CA  . SER F 114 ? 4.5259 3.9918 2.7263 -1.4127 0.1506  -0.0060 114 SER F CA  
12277 C C   . SER F 114 ? 4.4194 3.9517 2.6797 -1.3968 0.1586  -0.0096 114 SER F C   
12278 O O   . SER F 114 ? 4.2682 3.8588 2.5894 -1.3589 0.1606  -0.0015 114 SER F O   
12279 C CB  . SER F 114 ? 4.4617 3.9803 2.6897 -1.4004 0.1569  -0.0102 114 SER F CB  
12280 O OG  . SER F 114 ? 4.5659 4.0213 2.7365 -1.4140 0.1504  -0.0072 114 SER F OG  
12281 N N   . VAL F 115 ? 4.3459 3.8679 2.5878 -1.4252 0.1638  -0.0215 115 VAL F N   
12282 C CA  . VAL F 115 ? 4.2792 3.8480 2.5659 -1.4133 0.1708  -0.0240 115 VAL F CA  
12283 C C   . VAL F 115 ? 4.2343 3.8701 2.5559 -1.4214 0.1799  -0.0386 115 VAL F C   
12284 O O   . VAL F 115 ? 4.3038 3.9188 2.5867 -1.4565 0.1820  -0.0515 115 VAL F O   
12285 C CB  . VAL F 115 ? 4.3650 3.8650 2.6010 -1.4361 0.1711  -0.0242 115 VAL F CB  
12286 C CG1 . VAL F 115 ? 4.2969 3.8443 2.5809 -1.4195 0.1796  -0.0250 115 VAL F CG1 
12287 C CG2 . VAL F 115 ? 4.4251 3.8504 2.6157 -1.4321 0.1601  -0.0097 115 VAL F CG2 
12288 N N   . PHE F 116 ? 4.1199 3.8338 2.5123 -1.3894 0.1847  -0.0365 116 PHE F N   
12289 C CA  . PHE F 116 ? 4.0687 3.8529 2.5009 -1.3912 0.1919  -0.0481 116 PHE F CA  
12290 C C   . PHE F 116 ? 3.9950 3.8172 2.4711 -1.3733 0.1967  -0.0465 116 PHE F C   
12291 O O   . PHE F 116 ? 3.9058 3.7350 2.4120 -1.3409 0.1953  -0.0338 116 PHE F O   
12292 C CB  . PHE F 116 ? 3.9530 3.8008 2.4301 -1.3632 0.1933  -0.0452 116 PHE F CB  
12293 C CG  . PHE F 116 ? 4.0222 3.8314 2.4573 -1.3753 0.1903  -0.0449 116 PHE F CG  
12294 C CD1 . PHE F 116 ? 4.0023 3.7768 2.4263 -1.3556 0.1847  -0.0310 116 PHE F CD1 
12295 C CD2 . PHE F 116 ? 4.1152 3.9202 2.5186 -1.4079 0.1932  -0.0589 116 PHE F CD2 
12296 C CE1 . PHE F 116 ? 4.0730 3.8090 2.4556 -1.3658 0.1822  -0.0303 116 PHE F CE1 
12297 C CE2 . PHE F 116 ? 4.1866 3.9530 2.5490 -1.4178 0.1915  -0.0585 116 PHE F CE2 
12298 C CZ  . PHE F 116 ? 4.1660 3.8970 2.5177 -1.3959 0.1860  -0.0439 116 PHE F CZ  
12299 N N   . ILE F 117 ? 4.0314 3.8775 2.5101 -1.3948 0.2029  -0.0597 117 ILE F N   
12300 C CA  . ILE F 117 ? 3.9603 3.8486 2.4836 -1.3773 0.2087  -0.0588 117 ILE F CA  
12301 C C   . ILE F 117 ? 3.8677 3.8381 2.4414 -1.3672 0.2113  -0.0655 117 ILE F C   
12302 O O   . ILE F 117 ? 3.9182 3.9011 2.4737 -1.3937 0.2114  -0.0779 117 ILE F O   
12303 C CB  . ILE F 117 ? 4.0551 3.8966 2.5370 -1.4090 0.2157  -0.0666 117 ILE F CB  
12304 C CG1 . ILE F 117 ? 4.0148 3.8922 2.5294 -1.4006 0.2217  -0.0669 117 ILE F CG1 
12305 C CG2 . ILE F 117 ? 4.1269 3.9615 2.5706 -1.4538 0.2197  -0.0851 117 ILE F CG2 
12306 C CD1 . ILE F 117 ? 4.1026 3.9259 2.5749 -1.4260 0.2313  -0.0705 117 ILE F CD1 
12307 N N   . PHE F 118 ? 3.9398 3.9643 2.5620 -1.3437 0.2119  -0.0611 118 PHE F N   
12308 C CA  . PHE F 118 ? 3.8530 3.9562 2.5221 -1.3332 0.2136  -0.0659 118 PHE F CA  
12309 C C   . PHE F 118 ? 3.8537 3.9843 2.5357 -1.3460 0.2174  -0.0728 118 PHE F C   
12310 O O   . PHE F 118 ? 3.8175 3.9462 2.5070 -1.3393 0.2170  -0.0677 118 PHE F O   
12311 C CB  . PHE F 118 ? 3.7177 3.8652 2.4281 -1.2975 0.2108  -0.0549 118 PHE F CB  
12312 C CG  . PHE F 118 ? 3.7187 3.8397 2.4166 -1.2818 0.2093  -0.0473 118 PHE F CG  
12313 C CD1 . PHE F 118 ? 3.7326 3.8755 2.4316 -1.2807 0.2118  -0.0517 118 PHE F CD1 
12314 C CD2 . PHE F 118 ? 3.7163 3.7888 2.3951 -1.2725 0.2054  -0.0370 118 PHE F CD2 
12315 C CE1 . PHE F 118 ? 3.7599 3.8773 2.4331 -1.2805 0.2106  -0.0488 118 PHE F CE1 
12316 C CE2 . PHE F 118 ? 3.7223 3.7693 2.3882 -1.2572 0.2045  -0.0296 118 PHE F CE2 
12317 C CZ  . PHE F 118 ? 3.7537 3.8226 2.4109 -1.2680 0.2069  -0.0374 118 PHE F CZ  
12318 N N   . PRO F 119 ? 3.8090 3.9649 2.4936 -1.3638 0.2219  -0.0843 119 PRO F N   
12319 C CA  . PRO F 119 ? 3.8042 3.9928 2.5055 -1.3727 0.2266  -0.0901 119 PRO F CA  
12320 C C   . PRO F 119 ? 3.6661 3.9261 2.4204 -1.3461 0.2232  -0.0844 119 PRO F C   
12321 O O   . PRO F 119 ? 3.5803 3.8721 2.3602 -1.3221 0.2189  -0.0778 119 PRO F O   
12322 C CB  . PRO F 119 ? 3.8779 4.0803 2.5717 -1.3951 0.2318  -0.1031 119 PRO F CB  
12323 C CG  . PRO F 119 ? 3.8716 4.0832 2.5661 -1.3887 0.2273  -0.1034 119 PRO F CG  
12324 C CD  . PRO F 119 ? 3.8608 4.0204 2.5342 -1.3763 0.2231  -0.0926 119 PRO F CD  
12325 N N   . PRO F 120 ? 3.8319 4.1169 2.6029 -1.3481 0.2265  -0.0859 120 PRO F N   
12326 C CA  . PRO F 120 ? 3.7147 4.0702 2.5362 -1.3237 0.2238  -0.0807 120 PRO F CA  
12327 C C   . PRO F 120 ? 3.7269 4.1417 2.5744 -1.3206 0.2229  -0.0858 120 PRO F C   
12328 O O   . PRO F 120 ? 3.8144 4.2261 2.6457 -1.3432 0.2261  -0.0966 120 PRO F O   
12329 C CB  . PRO F 120 ? 3.7536 4.1121 2.5783 -1.3323 0.2295  -0.0828 120 PRO F CB  
12330 C CG  . PRO F 120 ? 3.9070 4.2135 2.6882 -1.3644 0.2377  -0.0925 120 PRO F CG  
12331 C CD  . PRO F 120 ? 3.9515 4.1987 2.6948 -1.3710 0.2348  -0.0912 120 PRO F CD  
12332 N N   . SER F 121 ? 3.6663 4.1351 2.5540 -1.2915 0.2195  -0.0774 121 SER F N   
12333 C CA  . SER F 121 ? 3.6504 4.1803 2.5646 -1.2850 0.2191  -0.0804 121 SER F CA  
12334 C C   . SER F 121 ? 3.6869 4.2562 2.6175 -1.2965 0.2212  -0.0868 121 SER F C   
12335 O O   . SER F 121 ? 3.6900 4.2535 2.6245 -1.2984 0.2233  -0.0851 121 SER F O   
12336 C CB  . SER F 121 ? 3.5327 4.1074 2.4835 -1.2480 0.2177  -0.0680 121 SER F CB  
12337 O OG  . SER F 121 ? 3.4580 4.0583 2.4379 -1.2301 0.2173  -0.0597 121 SER F OG  
12338 N N   . ASP F 122 ? 3.7070 4.3162 2.6464 -1.3041 0.2214  -0.0942 122 ASP F N   
12339 C CA  . ASP F 122 ? 3.7510 4.4050 2.7100 -1.3121 0.2233  -0.0992 122 ASP F CA  
12340 C C   . ASP F 122 ? 3.6543 4.3604 2.6555 -1.2833 0.2211  -0.0876 122 ASP F C   
12341 O O   . ASP F 122 ? 3.6652 4.3914 2.6799 -1.2871 0.2236  -0.0883 122 ASP F O   
12342 C CB  . ASP F 122 ? 3.8099 4.5008 2.7718 -1.3233 0.2230  -0.1086 122 ASP F CB  
12343 C CG  . ASP F 122 ? 3.9661 4.6079 2.8873 -1.3556 0.2271  -0.1219 122 ASP F CG  
12344 O OD1 . ASP F 122 ? 3.9924 4.5761 2.8841 -1.3723 0.2320  -0.1243 122 ASP F OD1 
12345 O OD2 . ASP F 122 ? 4.0367 4.7013 2.9492 -1.3717 0.2257  -0.1320 122 ASP F OD2 
12346 N N   . GLU F 123 ? 3.7489 4.4759 2.7709 -1.2532 0.2182  -0.0763 123 GLU F N   
12347 C CA  . GLU F 123 ? 3.6575 4.4312 2.7192 -1.2234 0.2176  -0.0640 123 GLU F CA  
12348 C C   . GLU F 123 ? 3.6382 4.3839 2.6992 -1.2229 0.2189  -0.0600 123 GLU F C   
12349 O O   . GLU F 123 ? 3.6156 4.3951 2.7020 -1.2143 0.2199  -0.0558 123 GLU F O   
12350 C CB  . GLU F 123 ? 3.5670 4.3569 2.6454 -1.1905 0.2178  -0.0523 123 GLU F CB  
12351 C CG  . GLU F 123 ? 3.4792 4.3219 2.5993 -1.1575 0.2189  -0.0390 123 GLU F CG  
12352 C CD  . GLU F 123 ? 3.3961 4.2453 2.5284 -1.1236 0.2227  -0.0269 123 GLU F CD  
12353 O OE1 . GLU F 123 ? 3.4116 4.2291 2.5202 -1.1261 0.2242  -0.0295 123 GLU F OE1 
12354 O OE2 . GLU F 123 ? 3.3290 4.2122 2.4930 -1.0937 0.2255  -0.0145 123 GLU F OE2 
12355 N N   . GLN F 124 ? 3.7204 4.4040 2.7516 -1.2315 0.2193  -0.0607 124 GLN F N   
12356 C CA  . GLN F 124 ? 3.7057 4.3598 2.7325 -1.2315 0.2213  -0.0572 124 GLN F CA  
12357 C C   . GLN F 124 ? 3.8256 4.4704 2.8393 -1.2570 0.2266  -0.0663 124 GLN F C   
12358 O O   . GLN F 124 ? 3.8262 4.4800 2.8539 -1.2516 0.2300  -0.0627 124 GLN F O   
12359 C CB  . GLN F 124 ? 3.6914 4.2792 2.6854 -1.2362 0.2206  -0.0559 124 GLN F CB  
12360 C CG  . GLN F 124 ? 3.6764 4.2336 2.6651 -1.2337 0.2225  -0.0514 124 GLN F CG  
12361 C CD  . GLN F 124 ? 3.6976 4.1842 2.6468 -1.2436 0.2217  -0.0512 124 GLN F CD  
12362 O OE1 . GLN F 124 ? 3.7630 4.2156 2.6823 -1.2588 0.2209  -0.0564 124 GLN F OE1 
12363 N NE2 . GLN F 124 ? 3.6721 4.1356 2.6199 -1.2351 0.2221  -0.0450 124 GLN F NE2 
12364 N N   . LEU F 125 ? 3.7237 4.3487 2.7102 -1.2843 0.2294  -0.0778 125 LEU F N   
12365 C CA  . LEU F 125 ? 3.8354 4.4474 2.8077 -1.3086 0.2381  -0.0863 125 LEU F CA  
12366 C C   . LEU F 125 ? 3.8414 4.5162 2.8515 -1.2996 0.2399  -0.0843 125 LEU F C   
12367 O O   . LEU F 125 ? 3.9186 4.5868 2.9287 -1.3083 0.2485  -0.0858 125 LEU F O   
12368 C CB  . LEU F 125 ? 3.9188 4.5052 2.8599 -1.3365 0.2416  -0.0985 125 LEU F CB  
12369 C CG  . LEU F 125 ? 3.9839 4.4951 2.8797 -1.3511 0.2432  -0.1008 125 LEU F CG  
12370 C CD1 . LEU F 125 ? 4.1404 4.6319 3.0093 -1.3749 0.2458  -0.1117 125 LEU F CD1 
12371 C CD2 . LEU F 125 ? 4.0649 4.5260 2.9372 -1.3628 0.2528  -0.1004 125 LEU F CD2 
12372 N N   . LYS F 126 ? 3.6622 4.3969 2.7038 -1.2819 0.2332  -0.0804 126 LYS F N   
12373 C CA  . LYS F 126 ? 3.6409 4.4374 2.7193 -1.2705 0.2338  -0.0765 126 LYS F CA  
12374 C C   . LYS F 126 ? 3.5840 4.3862 2.6834 -1.2517 0.2360  -0.0663 126 LYS F C   
12375 O O   . LYS F 126 ? 3.6386 4.4715 2.7585 -1.2505 0.2407  -0.0648 126 LYS F O   
12376 C CB  . LYS F 126 ? 3.5900 4.4453 2.6954 -1.2516 0.2265  -0.0721 126 LYS F CB  
12377 C CG  . LYS F 126 ? 3.6828 4.5431 2.7713 -1.2729 0.2257  -0.0840 126 LYS F CG  
12378 C CD  . LYS F 126 ? 3.6929 4.6145 2.8071 -1.2549 0.2201  -0.0799 126 LYS F CD  
12379 C CE  . LYS F 126 ? 3.5362 4.4649 2.6656 -1.2227 0.2171  -0.0668 126 LYS F CE  
12380 N NZ  . LYS F 126 ? 3.5710 4.5521 2.7179 -1.2061 0.2150  -0.0634 126 LYS F NZ  
12381 N N   . SER F 127 ? 3.8586 4.6321 2.9542 -1.2368 0.2334  -0.0591 127 SER F N   
12382 C CA  . SER F 127 ? 3.7996 4.5814 2.9175 -1.2162 0.2350  -0.0489 127 SER F CA  
12383 C C   . SER F 127 ? 3.8765 4.6088 2.9707 -1.2332 0.2434  -0.0529 127 SER F C   
12384 O O   . SER F 127 ? 3.8836 4.6213 2.9945 -1.2195 0.2464  -0.0460 127 SER F O   
12385 C CB  . SER F 127 ? 3.7029 4.4812 2.8316 -1.1896 0.2296  -0.0385 127 SER F CB  
12386 O OG  . SER F 127 ? 3.7308 4.4460 2.8248 -1.2007 0.2294  -0.0416 127 SER F OG  
12387 N N   . GLY F 128 ? 3.8146 4.4980 2.8698 -1.2622 0.2487  -0.0635 128 GLY F N   
12388 C CA  . GLY F 128 ? 3.9006 4.5357 2.9305 -1.2801 0.2600  -0.0676 128 GLY F CA  
12389 C C   . GLY F 128 ? 3.8926 4.4600 2.8846 -1.2876 0.2601  -0.0679 128 GLY F C   
12390 O O   . GLY F 128 ? 3.9802 4.5040 2.9485 -1.3016 0.2704  -0.0704 128 GLY F O   
12391 N N   . THR F 129 ? 5.3368 2.0434 3.3764 -1.3003 -0.5059 -0.0503 129 THR F N   
12392 C CA  . THR F 129 ? 5.2833 2.1003 3.3144 -1.3698 -0.5045 -0.0358 129 THR F CA  
12393 C C   . THR F 129 ? 5.1873 2.0740 3.2571 -1.3499 -0.5602 0.0037  129 THR F C   
12394 O O   . THR F 129 ? 5.1730 2.0224 3.2513 -1.2942 -0.5965 0.0219  129 THR F O   
12395 C CB  . THR F 129 ? 5.3419 2.1686 3.2749 -1.4385 -0.4689 -0.0363 129 THR F CB  
12396 O OG1 . THR F 129 ? 5.3533 2.1483 3.2379 -1.4185 -0.4914 -0.0114 129 THR F OG1 
12397 C CG2 . THR F 129 ? 5.4435 2.1955 3.3354 -1.4573 -0.4105 -0.0756 129 THR F CG2 
12398 N N   . ALA F 130 ? 5.2806 2.2700 3.3729 -1.3960 -0.5654 0.0173  130 ALA F N   
12399 C CA  . ALA F 130 ? 5.2012 2.2670 3.3282 -1.3872 -0.6124 0.0568  130 ALA F CA  
12400 C C   . ALA F 130 ? 5.1426 2.3012 3.2147 -1.4649 -0.6018 0.0771  130 ALA F C   
12401 O O   . ALA F 130 ? 5.1639 2.3747 3.2319 -1.5182 -0.5710 0.0628  130 ALA F O   
12402 C CB  . ALA F 130 ? 5.2114 2.3132 3.4393 -1.3549 -0.6329 0.0552  130 ALA F CB  
12403 N N   . SER F 131 ? 5.1204 2.3027 3.1503 -1.4712 -0.6273 0.1100  131 SER F N   
12404 C CA  . SER F 131 ? 5.0837 2.3643 3.0669 -1.5393 -0.6259 0.1351  131 SER F CA  
12405 C C   . SER F 131 ? 5.0341 2.3885 3.0668 -1.5217 -0.6732 0.1786  131 SER F C   
12406 O O   . SER F 131 ? 5.0009 2.3244 3.0563 -1.4667 -0.7112 0.1994  131 SER F O   
12407 C CB  . SER F 131 ? 5.0697 2.3281 2.9598 -1.5694 -0.6136 0.1388  131 SER F CB  
12408 O OG  . SER F 131 ? 5.1615 2.3522 3.0032 -1.5898 -0.5646 0.0988  131 SER F OG  
12409 N N   . VAL F 132 ? 4.9175 2.3694 2.9655 -1.5680 -0.6693 0.1929  132 VAL F N   
12410 C CA  . VAL F 132 ? 4.8335 2.3636 2.9233 -1.5609 -0.7073 0.2374  132 VAL F CA  
12411 C C   . VAL F 132 ? 4.8317 2.4516 2.8508 -1.6301 -0.7038 0.2652  132 VAL F C   
12412 O O   . VAL F 132 ? 4.8664 2.5341 2.8413 -1.6947 -0.6686 0.2490  132 VAL F O   
12413 C CB  . VAL F 132 ? 4.7856 2.3569 2.9549 -1.5552 -0.7049 0.2352  132 VAL F CB  
12414 C CG1 . VAL F 132 ? 4.7018 2.3287 2.9268 -1.5287 -0.7454 0.2805  132 VAL F CG1 
12415 C CG2 . VAL F 132 ? 4.8083 2.2938 3.0348 -1.5035 -0.6937 0.1939  132 VAL F CG2 
12416 N N   . VAL F 133 ? 4.8314 2.4782 2.8402 -1.6171 -0.7399 0.3059  133 VAL F N   
12417 C CA  . VAL F 133 ? 4.8308 2.5606 2.7708 -1.6777 -0.7406 0.3339  133 VAL F CA  
12418 C C   . VAL F 133 ? 4.7484 2.5833 2.7292 -1.6799 -0.7678 0.3842  133 VAL F C   
12419 O O   . VAL F 133 ? 4.6889 2.5168 2.7344 -1.6153 -0.8000 0.4089  133 VAL F O   
12420 C CB  . VAL F 133 ? 4.8611 2.5394 2.7449 -1.6625 -0.7542 0.3404  133 VAL F CB  
12421 C CG1 . VAL F 133 ? 4.8521 2.6241 2.6726 -1.7219 -0.7593 0.3722  133 VAL F CG1 
12422 C CG2 . VAL F 133 ? 4.9491 2.5305 2.7875 -1.6616 -0.7186 0.2928  133 VAL F CG2 
12423 N N   . CYS F 134 ? 4.8222 2.7775 2.7736 -1.7366 -0.7479 0.3974  134 CYS F N   
12424 C CA  . CYS F 134 ? 4.7439 2.8344 2.7251 -1.7284 -0.7626 0.4478  134 CYS F CA  
12425 C C   . CYS F 134 ? 4.7542 2.9192 2.6579 -1.7753 -0.7662 0.4714  134 CYS F C   
12426 O O   . CYS F 134 ? 4.8120 2.9994 2.6453 -1.8438 -0.7383 0.4469  134 CYS F O   
12427 C CB  . CYS F 134 ? 4.7222 2.9014 2.7368 -1.7497 -0.7357 0.4461  134 CYS F CB  
12428 S SG  . CYS F 134 ? 4.6286 2.9605 2.6916 -1.7251 -0.7491 0.5096  134 CYS F SG  
12429 N N   . LEU F 135 ? 4.7824 2.9851 2.6994 -1.7397 -0.7992 0.5166  135 LEU F N   
12430 C CA  . LEU F 135 ? 4.7849 3.0591 2.6356 -1.7755 -0.8074 0.5430  135 LEU F CA  
12431 C C   . LEU F 135 ? 4.7168 3.1491 2.5872 -1.7764 -0.8126 0.5936  135 LEU F C   
12432 O O   . LEU F 135 ? 4.6509 3.1070 2.5923 -1.7196 -0.8302 0.6266  135 LEU F O   
12433 C CB  . LEU F 135 ? 4.7831 2.9744 2.6247 -1.7348 -0.8406 0.5567  135 LEU F CB  
12434 C CG  . LEU F 135 ? 4.7662 3.0392 2.5571 -1.7562 -0.8562 0.5944  135 LEU F CG  
12435 C CD1 . LEU F 135 ? 4.8365 3.1346 2.5350 -1.8384 -0.8283 0.5673  135 LEU F CD1 
12436 C CD2 . LEU F 135 ? 4.7534 2.9441 2.5505 -1.7040 -0.8917 0.6122  135 LEU F CD2 
12437 N N   . LEU F 136 ? 4.8358 3.3766 2.6426 -1.8405 -0.7954 0.5985  136 LEU F N   
12438 C CA  . LEU F 136 ? 4.8262 3.5263 2.6338 -1.8459 -0.8003 0.6492  136 LEU F CA  
12439 C C   . LEU F 136 ? 4.7901 3.5268 2.5359 -1.8683 -0.8173 0.6694  136 LEU F C   
12440 O O   . LEU F 136 ? 4.7898 3.5290 2.4622 -1.9318 -0.8005 0.6391  136 LEU F O   
12441 C CB  . LEU F 136 ? 4.8609 3.6730 2.6449 -1.9019 -0.7664 0.6379  136 LEU F CB  
12442 C CG  . LEU F 136 ? 4.9061 3.7261 2.7486 -1.8856 -0.7458 0.6284  136 LEU F CG  
12443 C CD1 . LEU F 136 ? 4.9280 3.5935 2.7997 -1.8703 -0.7370 0.5775  136 LEU F CD1 
12444 C CD2 . LEU F 136 ? 4.9383 3.8858 2.7387 -1.9493 -0.7140 0.6206  136 LEU F CD2 
12445 N N   . ASN F 137 ? 4.7820 3.5469 2.5570 -1.8185 -0.8481 0.7187  137 ASN F N   
12446 C CA  . ASN F 137 ? 4.7468 3.5290 2.4703 -1.8306 -0.8676 0.7384  137 ASN F CA  
12447 C C   . ASN F 137 ? 4.7366 3.6897 2.4438 -1.8441 -0.8715 0.7888  137 ASN F C   
12448 O O   . ASN F 137 ? 4.7450 3.7687 2.5074 -1.7996 -0.8789 0.8324  137 ASN F O   
12449 C CB  . ASN F 137 ? 4.7249 3.3995 2.4860 -1.7637 -0.9017 0.7547  137 ASN F CB  
12450 C CG  . ASN F 137 ? 4.7368 3.3537 2.4331 -1.7845 -0.9139 0.7456  137 ASN F CG  
12451 O OD1 . ASN F 137 ? 4.8085 3.3775 2.4429 -1.8385 -0.8931 0.7026  137 ASN F OD1 
12452 N ND2 . ASN F 137 ? 4.6949 3.3157 2.4032 -1.7433 -0.9450 0.7857  137 ASN F ND2 
12453 N N   . ASN F 138 ? 4.7523 3.7726 2.3935 -1.9016 -0.8630 0.7773  138 ASN F N   
12454 C CA  . ASN F 138 ? 4.7017 3.8947 2.4024 -1.8879 -0.8551 0.7917  138 ASN F CA  
12455 C C   . ASN F 138 ? 4.7163 4.0643 2.4704 -1.8751 -0.8366 0.8154  138 ASN F C   
12456 O O   . ASN F 138 ? 4.7009 4.1244 2.5398 -1.8094 -0.8421 0.8514  138 ASN F O   
12457 C CB  . ASN F 138 ? 4.6580 3.8363 2.4303 -1.8152 -0.8796 0.8158  138 ASN F CB  
12458 C CG  . ASN F 138 ? 4.6403 3.6929 2.3623 -1.8283 -0.8944 0.7925  138 ASN F CG  
12459 O OD1 . ASN F 138 ? 4.6607 3.6422 2.2910 -1.8942 -0.8834 0.7586  138 ASN F OD1 
12460 N ND2 . ASN F 138 ? 4.6084 3.6314 2.3879 -1.7651 -0.9164 0.8090  138 ASN F ND2 
12461 N N   . PHE F 139 ? 4.6838 4.0772 2.3852 -1.9375 -0.8117 0.7937  139 PHE F N   
12462 C CA  . PHE F 139 ? 4.7079 4.2451 2.4515 -1.9283 -0.7920 0.8139  139 PHE F CA  
12463 C C   . PHE F 139 ? 4.6970 4.3887 2.4238 -1.9838 -0.7638 0.7933  139 PHE F C   
12464 O O   . PHE F 139 ? 4.6840 4.3536 2.3490 -2.0478 -0.7537 0.7547  139 PHE F O   
12465 C CB  . PHE F 139 ? 4.7755 4.2434 2.4876 -1.9427 -0.7845 0.8123  139 PHE F CB  
12466 C CG  . PHE F 139 ? 4.8046 4.1916 2.4323 -2.0194 -0.7662 0.7591  139 PHE F CG  
12467 C CD1 . PHE F 139 ? 4.7947 4.0075 2.4313 -2.0092 -0.7701 0.7180  139 PHE F CD1 
12468 C CD2 . PHE F 139 ? 4.8338 4.3270 2.4157 -2.0854 -0.7366 0.7351  139 PHE F CD2 
12469 C CE1 . PHE F 139 ? 4.8155 3.9559 2.4142 -2.0636 -0.7431 0.6557  139 PHE F CE1 
12470 C CE2 . PHE F 139 ? 4.8534 4.2761 2.3984 -2.1434 -0.7099 0.6702  139 PHE F CE2 
12471 C CZ  . PHE F 139 ? 4.8454 4.0886 2.3988 -2.1321 -0.7121 0.6312  139 PHE F CZ  
12472 N N   . TYR F 140 ? 4.5528 4.4009 2.3371 -1.9563 -0.7490 0.8197  140 TYR F N   
12473 C CA  . TYR F 140 ? 4.5541 4.5680 2.3341 -1.9999 -0.7211 0.8051  140 TYR F CA  
12474 C C   . TYR F 140 ? 4.6028 4.7318 2.4232 -1.9707 -0.7055 0.8326  140 TYR F C   
12475 O O   . TYR F 140 ? 4.6152 4.7504 2.4970 -1.8971 -0.7146 0.8749  140 TYR F O   
12476 C CB  . TYR F 140 ? 4.4974 4.6153 2.3185 -1.9845 -0.7208 0.8132  140 TYR F CB  
12477 C CG  . TYR F 140 ? 4.4992 4.7868 2.3159 -2.0315 -0.6930 0.7958  140 TYR F CG  
12478 C CD1 . TYR F 140 ? 4.5215 4.9701 2.3954 -1.9919 -0.6808 0.8260  140 TYR F CD1 
12479 C CD2 . TYR F 140 ? 4.4871 4.7719 2.2415 -2.1145 -0.6766 0.7486  140 TYR F CD2 
12480 C CE1 . TYR F 140 ? 4.5285 5.1347 2.4007 -2.0314 -0.6574 0.8103  140 TYR F CE1 
12481 C CE2 . TYR F 140 ? 4.4918 4.9359 2.2472 -2.1579 -0.6505 0.7311  140 TYR F CE2 
12482 C CZ  . TYR F 140 ? 4.5114 5.1178 2.3270 -2.1152 -0.6430 0.7624  140 TYR F CZ  
12483 O OH  . TYR F 140 ? 4.5204 5.2891 2.3388 -2.1551 -0.6191 0.7454  140 TYR F OH  
12484 N N   . PRO F 141 ? 4.5743 4.7957 2.3611 -2.0272 -0.6793 0.8079  141 PRO F N   
12485 C CA  . PRO F 141 ? 4.5730 4.8030 2.2896 -2.1187 -0.6600 0.7542  141 PRO F CA  
12486 C C   . PRO F 141 ? 4.6061 4.6640 2.2392 -2.1724 -0.6600 0.7162  141 PRO F C   
12487 O O   . PRO F 141 ? 4.6303 4.5594 2.2600 -2.1377 -0.6781 0.7334  141 PRO F O   
12488 C CB  . PRO F 141 ? 4.6129 5.0130 2.3426 -2.1381 -0.6324 0.7519  141 PRO F CB  
12489 C CG  . PRO F 141 ? 4.6591 5.0716 2.4328 -2.0727 -0.6362 0.7956  141 PRO F CG  
12490 C CD  . PRO F 141 ? 4.6245 4.9685 2.4518 -1.9945 -0.6631 0.8366  141 PRO F CD  
12491 N N   . ARG F 142 ? 4.7011 4.7566 2.2674 -2.2562 -0.6370 0.6638  142 ARG F N   
12492 C CA  . ARG F 142 ? 4.7355 4.6186 2.2134 -2.3100 -0.6334 0.6209  142 ARG F CA  
12493 C C   . ARG F 142 ? 4.8064 4.6337 2.2586 -2.3118 -0.6278 0.6204  142 ARG F C   
12494 O O   . ARG F 142 ? 4.8200 4.4789 2.2700 -2.3041 -0.6287 0.5938  142 ARG F O   
12495 C CB  . ARG F 142 ? 4.7384 4.6445 2.1555 -2.3999 -0.6004 0.5621  142 ARG F CB  
12496 C CG  . ARG F 142 ? 4.8130 4.5260 2.1397 -2.4502 -0.5958 0.5117  142 ARG F CG  
12497 C CD  . ARG F 142 ? 4.8865 4.6295 2.1626 -2.5365 -0.5514 0.4528  142 ARG F CD  
12498 N NE  . ARG F 142 ? 4.9697 4.5239 2.1821 -2.5692 -0.5410 0.4020  142 ARG F NE  
12499 C CZ  . ARG F 142 ? 5.0230 4.4662 2.2211 -2.5907 -0.5223 0.3548  142 ARG F CZ  
12500 N NH1 . ARG F 142 ? 5.0065 4.5071 2.2298 -2.5921 -0.5157 0.3543  142 ARG F NH1 
12501 N NH2 . ARG F 142 ? 5.0870 4.3624 2.2663 -2.5903 -0.4992 0.3129  142 ARG F NH2 
12502 N N   . GLU F 143 ? 4.7524 4.7173 2.2431 -2.3010 -0.6115 0.6380  143 GLU F N   
12503 C CA  . GLU F 143 ? 4.8251 4.7423 2.2973 -2.3092 -0.5967 0.6305  143 GLU F CA  
12504 C C   . GLU F 143 ? 4.8192 4.6043 2.3733 -2.2246 -0.6140 0.6561  143 GLU F C   
12505 O O   . GLU F 143 ? 4.8074 4.6346 2.4020 -2.1622 -0.6358 0.7160  143 GLU F O   
12506 C CB  . GLU F 143 ? 4.8623 4.9612 2.3665 -2.3056 -0.5761 0.6494  143 GLU F CB  
12507 C CG  . GLU F 143 ? 4.9335 4.9946 2.4516 -2.2899 -0.5600 0.6545  143 GLU F CG  
12508 C CD  . GLU F 143 ? 4.9617 4.9081 2.4674 -2.3396 -0.5318 0.5808  143 GLU F CD  
12509 O OE1 . GLU F 143 ? 4.9552 4.9076 2.3969 -2.4133 -0.5179 0.5318  143 GLU F OE1 
12510 O OE2 . GLU F 143 ? 4.9952 4.8443 2.5555 -2.3053 -0.5216 0.5708  143 GLU F OE2 
12511 N N   . ALA F 144 ? 4.9152 4.5422 2.4934 -2.2231 -0.6026 0.6093  144 ALA F N   
12512 C CA  . ALA F 144 ? 4.9146 4.4131 2.5719 -2.1483 -0.6162 0.6227  144 ALA F CA  
12513 C C   . ALA F 144 ? 4.9634 4.3553 2.6409 -2.1631 -0.5890 0.5682  144 ALA F C   
12514 O O   . ALA F 144 ? 4.9799 4.3381 2.6060 -2.2272 -0.5663 0.5136  144 ALA F O   
12515 C CB  . ALA F 144 ? 4.8549 4.2345 2.5228 -2.1119 -0.6479 0.6290  144 ALA F CB  
12516 N N   . LYS F 145 ? 4.9630 4.3017 2.7159 -2.1044 -0.5893 0.5822  145 LYS F N   
12517 C CA  . LYS F 145 ? 4.9992 4.2315 2.7826 -2.1080 -0.5658 0.5341  145 LYS F CA  
12518 C C   . LYS F 145 ? 4.9711 4.0468 2.8222 -2.0415 -0.5864 0.5307  145 LYS F C   
12519 O O   . LYS F 145 ? 4.9227 4.0051 2.8308 -1.9772 -0.6084 0.5761  145 LYS F O   
12520 C CB  . LYS F 145 ? 5.0081 4.3308 2.8198 -2.1056 -0.5406 0.5464  145 LYS F CB  
12521 C CG  . LYS F 145 ? 5.0774 4.2980 2.9242 -2.1084 -0.5150 0.4983  145 LYS F CG  
12522 C CD  . LYS F 145 ? 5.1579 4.4887 2.9984 -2.1373 -0.4823 0.4979  145 LYS F CD  
12523 C CE  . LYS F 145 ? 5.1365 4.5526 3.0308 -2.0791 -0.4867 0.5589  145 LYS F CE  
12524 N NZ  . LYS F 145 ? 5.2078 4.7004 3.1061 -2.0981 -0.4519 0.5539  145 LYS F NZ  
12525 N N   . VAL F 146 ? 5.1219 4.0591 2.9659 -2.0564 -0.5777 0.4763  146 VAL F N   
12526 C CA  . VAL F 146 ? 5.1145 3.9011 3.0207 -1.9960 -0.5943 0.4641  146 VAL F CA  
12527 C C   . VAL F 146 ? 5.1545 3.8676 3.0930 -2.0014 -0.5654 0.4181  146 VAL F C   
12528 O O   . VAL F 146 ? 5.2484 3.9370 3.1366 -2.0603 -0.5372 0.3713  146 VAL F O   
12529 C CB  . VAL F 146 ? 5.0927 3.7686 2.9614 -1.9984 -0.6125 0.4438  146 VAL F CB  
12530 C CG1 . VAL F 146 ? 5.0824 3.6143 3.0168 -1.9305 -0.6319 0.4338  146 VAL F CG1 
12531 C CG2 . VAL F 146 ? 5.0192 3.7722 2.8511 -1.9992 -0.6388 0.4870  146 VAL F CG2 
12532 N N   . GLN F 147 ? 4.9845 3.6625 3.0070 -1.9415 -0.5706 0.4298  147 GLN F N   
12533 C CA  . GLN F 147 ? 5.0167 3.6218 3.0814 -1.9373 -0.5457 0.3885  147 GLN F CA  
12534 C C   . GLN F 147 ? 4.9969 3.4644 3.1287 -1.8721 -0.5670 0.3752  147 GLN F C   
12535 O O   . GLN F 147 ? 4.9437 3.4130 3.1264 -1.8141 -0.5956 0.4121  147 GLN F O   
12536 C CB  . GLN F 147 ? 5.0090 3.7130 3.1155 -1.9297 -0.5256 0.4110  147 GLN F CB  
12537 C CG  . GLN F 147 ? 5.1060 3.9559 3.1472 -1.9911 -0.5041 0.4241  147 GLN F CG  
12538 C CD  . GLN F 147 ? 5.1587 4.0880 3.2339 -1.9888 -0.4767 0.4356  147 GLN F CD  
12539 O OE1 . GLN F 147 ? 5.2501 4.1088 3.3733 -1.9755 -0.4584 0.4051  147 GLN F OE1 
12540 N NE2 . GLN F 147 ? 5.2074 4.2856 3.2565 -2.0007 -0.4726 0.4800  147 GLN F NE2 
12541 N N   . TRP F 148 ? 4.9678 3.3192 3.0989 -1.8810 -0.5520 0.3220  148 TRP F N   
12542 C CA  . TRP F 148 ? 4.9583 3.1803 3.1517 -1.8204 -0.5692 0.3025  148 TRP F CA  
12543 C C   . TRP F 148 ? 4.9606 3.1698 3.2339 -1.7919 -0.5520 0.2873  148 TRP F C   
12544 O O   . TRP F 148 ? 5.0041 3.2406 3.2651 -1.8330 -0.5174 0.2630  148 TRP F O   
12545 C CB  . TRP F 148 ? 5.0139 3.1112 3.1582 -1.8412 -0.5620 0.2546  148 TRP F CB  
12546 C CG  . TRP F 148 ? 5.0078 3.0828 3.0887 -1.8508 -0.5838 0.2675  148 TRP F CG  
12547 C CD1 . TRP F 148 ? 4.9946 3.1111 2.9858 -1.9169 -0.5701 0.2630  148 TRP F CD1 
12548 C CD2 . TRP F 148 ? 4.9606 2.9616 3.0627 -1.7932 -0.6213 0.2830  148 TRP F CD2 
12549 N NE1 . TRP F 148 ? 4.9422 3.0149 2.8979 -1.9038 -0.5963 0.2769  148 TRP F NE1 
12550 C CE2 . TRP F 148 ? 4.9213 2.9218 2.9427 -1.8273 -0.6284 0.2901  148 TRP F CE2 
12551 C CE3 . TRP F 148 ? 4.9352 2.8748 3.1171 -1.7170 -0.6491 0.2902  148 TRP F CE3 
12552 C CZ2 . TRP F 148 ? 4.8752 2.8122 2.8917 -1.7862 -0.6622 0.3064  148 TRP F CZ2 
12553 C CZ3 . TRP F 148 ? 4.9043 2.7855 3.0814 -1.6766 -0.6837 0.3054  148 TRP F CZ3 
12554 C CH2 . TRP F 148 ? 4.8678 2.7461 2.9619 -1.7104 -0.6901 0.3145  148 TRP F CH2 
12555 N N   . LYS F 149 ? 4.8916 3.0602 3.2471 -1.7227 -0.5752 0.2998  149 LYS F N   
12556 C CA  . LYS F 149 ? 4.9027 3.0457 3.3423 -1.6895 -0.5610 0.2813  149 LYS F CA  
12557 C C   . LYS F 149 ? 4.8955 2.9122 3.3889 -1.6343 -0.5809 0.2510  149 LYS F C   
12558 O O   . LYS F 149 ? 4.8612 2.8473 3.3699 -1.5913 -0.6159 0.2700  149 LYS F O   
12559 C CB  . LYS F 149 ? 4.8621 3.1007 3.3599 -1.6581 -0.5642 0.3280  149 LYS F CB  
12560 C CG  . LYS F 149 ? 4.8955 3.2641 3.3453 -1.7073 -0.5403 0.3571  149 LYS F CG  
12561 C CD  . LYS F 149 ? 4.8741 3.3364 3.3660 -1.6724 -0.5469 0.4137  149 LYS F CD  
12562 C CE  . LYS F 149 ? 4.9415 3.5388 3.3756 -1.7190 -0.5257 0.4458  149 LYS F CE  
12563 N NZ  . LYS F 149 ? 4.8985 3.5864 3.3702 -1.6822 -0.5274 0.5040  149 LYS F NZ  
12564 N N   . VAL F 150 ? 4.8580 2.8046 3.3789 -1.6347 -0.5587 0.2038  150 VAL F N   
12565 C CA  . VAL F 150 ? 4.8631 2.6969 3.4403 -1.5802 -0.5743 0.1713  150 VAL F CA  
12566 C C   . VAL F 150 ? 4.8603 2.6994 3.5311 -1.5508 -0.5585 0.1547  150 VAL F C   
12567 O O   . VAL F 150 ? 4.9072 2.7485 3.5762 -1.5841 -0.5233 0.1267  150 VAL F O   
12568 C CB  . VAL F 150 ? 4.9321 2.6616 3.4518 -1.6039 -0.5616 0.1262  150 VAL F CB  
12569 C CG1 . VAL F 150 ? 4.9370 2.5618 3.5161 -1.5389 -0.5779 0.0958  150 VAL F CG1 
12570 C CG2 . VAL F 150 ? 4.9394 2.6651 3.3645 -1.6374 -0.5727 0.1419  150 VAL F CG2 
12571 N N   . ASP F 151 ? 4.7803 2.6203 3.5331 -1.4900 -0.5829 0.1698  151 ASP F N   
12572 C CA  . ASP F 151 ? 4.7592 2.6198 3.6067 -1.4608 -0.5682 0.1609  151 ASP F CA  
12573 C C   . ASP F 151 ? 4.7380 2.6983 3.5767 -1.5020 -0.5336 0.1824  151 ASP F C   
12574 O O   . ASP F 151 ? 4.7267 2.6871 3.5982 -1.5142 -0.5020 0.1561  151 ASP F O   
12575 C CB  . ASP F 151 ? 4.8620 2.6316 3.7558 -1.4411 -0.5569 0.1043  151 ASP F CB  
12576 C CG  . ASP F 151 ? 4.8549 2.5430 3.7914 -1.3794 -0.5929 0.0874  151 ASP F CG  
12577 O OD1 . ASP F 151 ? 4.7830 2.4949 3.7464 -1.3426 -0.6241 0.1184  151 ASP F OD1 
12578 O OD2 . ASP F 151 ? 4.9690 2.5715 3.9137 -1.3659 -0.5892 0.0432  151 ASP F OD2 
12579 N N   . ASN F 152 ? 4.7382 2.7858 3.5304 -1.5221 -0.5396 0.2317  152 ASN F N   
12580 C CA  . ASN F 152 ? 4.6964 2.8521 3.4695 -1.5578 -0.5104 0.2617  152 ASN F CA  
12581 C C   . ASN F 152 ? 4.7812 2.9482 3.4959 -1.6209 -0.4747 0.2325  152 ASN F C   
12582 O O   . ASN F 152 ? 4.8067 3.0505 3.5212 -1.6458 -0.4444 0.2447  152 ASN F O   
12583 C CB  . ASN F 152 ? 4.6732 2.8604 3.5391 -1.5194 -0.4959 0.2735  152 ASN F CB  
12584 C CG  . ASN F 152 ? 4.5745 2.7877 3.4844 -1.4694 -0.5230 0.3161  152 ASN F CG  
12585 O OD1 . ASN F 152 ? 4.5335 2.8263 3.4041 -1.4783 -0.5286 0.3660  152 ASN F OD1 
12586 N ND2 . ASN F 152 ? 4.6027 2.7503 3.5945 -1.4163 -0.5395 0.2952  152 ASN F ND2 
12587 N N   . ALA F 153 ? 4.6742 2.7652 3.3378 -1.6473 -0.4751 0.1937  153 ALA F N   
12588 C CA  . ALA F 153 ? 4.7377 2.8364 3.3363 -1.7127 -0.4407 0.1643  153 ALA F CA  
12589 C C   . ALA F 153 ? 4.7677 2.9064 3.2660 -1.7615 -0.4479 0.1811  153 ALA F C   
12590 O O   . ALA F 153 ? 4.7824 2.8607 3.2516 -1.7498 -0.4741 0.1793  153 ALA F O   
12591 C CB  . ALA F 153 ? 4.7929 2.7733 3.4052 -1.7106 -0.4280 0.1049  153 ALA F CB  
12592 N N   . LEU F 154 ? 4.7972 3.0392 3.2425 -1.8158 -0.4240 0.1963  154 LEU F N   
12593 C CA  . LEU F 154 ? 4.7863 3.0809 3.1367 -1.8677 -0.4278 0.2093  154 LEU F CA  
12594 C C   . LEU F 154 ? 4.9140 3.1156 3.2037 -1.9096 -0.4147 0.1582  154 LEU F C   
12595 O O   . LEU F 154 ? 4.9765 3.1318 3.2677 -1.9340 -0.3833 0.1147  154 LEU F O   
12596 C CB  . LEU F 154 ? 4.7323 3.1671 3.0432 -1.9155 -0.4033 0.2335  154 LEU F CB  
12597 C CG  . LEU F 154 ? 4.7736 3.2886 2.9895 -1.9712 -0.4066 0.2490  154 LEU F CG  
12598 C CD1 . LEU F 154 ? 4.7138 3.2395 2.9270 -1.9355 -0.4475 0.2916  154 LEU F CD1 
12599 C CD2 . LEU F 154 ? 4.7088 3.3709 2.8929 -2.0120 -0.3823 0.2723  154 LEU F CD2 
12600 N N   . GLN F 155 ? 4.7889 2.9599 3.0241 -1.9176 -0.4362 0.1639  155 GLN F N   
12601 C CA  . GLN F 155 ? 4.8698 2.9435 3.0423 -1.9536 -0.4233 0.1194  155 GLN F CA  
12602 C C   . GLN F 155 ? 4.9178 3.0686 2.9957 -2.0368 -0.3987 0.1125  155 GLN F C   
12603 O O   . GLN F 155 ? 4.8840 3.1538 2.9327 -2.0560 -0.4091 0.1516  155 GLN F O   
12604 C CB  . GLN F 155 ? 4.8709 2.8565 3.0367 -1.9131 -0.4584 0.1268  155 GLN F CB  
12605 C CG  . GLN F 155 ? 4.8227 2.7394 3.0796 -1.8300 -0.4870 0.1335  155 GLN F CG  
12606 C CD  . GLN F 155 ? 4.8542 2.6797 3.1601 -1.8012 -0.4650 0.0851  155 GLN F CD  
12607 O OE1 . GLN F 155 ? 4.9092 2.6579 3.1918 -1.7876 -0.4496 0.0493  155 GLN F OE1 
12608 N NE2 . GLN F 155 ? 4.8167 2.6595 3.1962 -1.7832 -0.4598 0.0849  155 GLN F NE2 
12609 N N   . SER F 156 ? 4.7762 2.8762 2.8147 -2.0681 -0.3618 0.0621  156 SER F N   
12610 C CA  . SER F 156 ? 4.8305 2.9935 2.7800 -2.1388 -0.3337 0.0453  156 SER F CA  
12611 C C   . SER F 156 ? 4.9043 2.9662 2.8188 -2.1289 -0.3079 -0.0008 156 SER F C   
12612 O O   . SER F 156 ? 4.9263 2.8893 2.8849 -2.0857 -0.2940 -0.0316 156 SER F O   
12613 C CB  . SER F 156 ? 4.8450 3.0985 2.7808 -2.1984 -0.2988 0.0317  156 SER F CB  
12614 O OG  . SER F 156 ? 4.7752 3.1197 2.7578 -2.1873 -0.3158 0.0752  156 SER F OG  
12615 N N   . GLY F 157 ? 4.9443 3.0334 2.7801 -2.1697 -0.2998 -0.0044 157 GLY F N   
12616 C CA  . GLY F 157 ? 5.0245 3.0289 2.8150 -2.1732 -0.2669 -0.0471 157 GLY F CA  
12617 C C   . GLY F 157 ? 5.0349 2.9205 2.8362 -2.1107 -0.2870 -0.0453 157 GLY F C   
12618 O O   . GLY F 157 ? 5.1046 2.9283 2.8552 -2.1197 -0.2606 -0.0732 157 GLY F O   
12619 N N   . ASN F 158 ? 5.0196 2.8704 2.8840 -2.0478 -0.3309 -0.0143 158 ASN F N   
12620 C CA  . ASN F 158 ? 5.0283 2.7693 2.9051 -1.9847 -0.3523 -0.0122 158 ASN F CA  
12621 C C   . ASN F 158 ? 4.9940 2.7640 2.8416 -1.9796 -0.3919 0.0292  158 ASN F C   
12622 O O   . ASN F 158 ? 4.9886 2.6763 2.8533 -1.9222 -0.4173 0.0383  158 ASN F O   
12623 C CB  . ASN F 158 ? 4.9912 2.6583 2.9608 -1.9100 -0.3720 -0.0138 158 ASN F CB  
12624 C CG  . ASN F 158 ? 4.9078 2.6479 2.9409 -1.8999 -0.4015 0.0196  158 ASN F CG  
12625 O OD1 . ASN F 158 ? 4.8721 2.7153 2.8809 -1.9424 -0.4138 0.0521  158 ASN F OD1 
12626 N ND2 . ASN F 158 ? 4.8783 2.5658 2.9945 -1.8432 -0.4117 0.0121  158 ASN F ND2 
12627 N N   . SER F 159 ? 4.9393 2.8259 2.7429 -2.0372 -0.3981 0.0547  159 SER F N   
12628 C CA  . SER F 159 ? 4.9090 2.8284 2.6824 -2.0361 -0.4340 0.0939  159 SER F CA  
12629 C C   . SER F 159 ? 4.9584 2.9414 2.6399 -2.1067 -0.4098 0.0847  159 SER F C   
12630 O O   . SER F 159 ? 4.9961 3.0403 2.6415 -2.1666 -0.3719 0.0586  159 SER F O   
12631 C CB  . SER F 159 ? 4.8209 2.8316 2.6381 -2.0306 -0.4746 0.1454  159 SER F CB  
12632 O OG  . SER F 159 ? 4.8105 2.9424 2.6115 -2.0941 -0.4573 0.1508  159 SER F OG  
12633 N N   . GLN F 160 ? 4.9435 2.9130 2.5882 -2.0985 -0.4319 0.1053  160 GLN F N   
12634 C CA  . GLN F 160 ? 4.9806 3.0173 2.5419 -2.1613 -0.4162 0.1029  160 GLN F CA  
12635 C C   . GLN F 160 ? 4.9188 3.0276 2.4737 -2.1599 -0.4626 0.1553  160 GLN F C   
12636 O O   . GLN F 160 ? 4.8733 2.9269 2.4719 -2.0985 -0.5025 0.1849  160 GLN F O   
12637 C CB  . GLN F 160 ? 5.0651 2.9935 2.5756 -2.1560 -0.3854 0.0669  160 GLN F CB  
12638 C CG  . GLN F 160 ? 5.1395 3.0111 2.6399 -2.1727 -0.3313 0.0137  160 GLN F CG  
12639 C CD  . GLN F 160 ? 5.2289 3.0001 2.6727 -2.1738 -0.2968 -0.0186 160 GLN F CD  
12640 O OE1 . GLN F 160 ? 5.2441 2.8973 2.7057 -2.1129 -0.3077 -0.0182 160 GLN F OE1 
12641 N NE2 . GLN F 160 ? 5.2913 3.1110 2.6658 -2.2433 -0.2535 -0.0469 160 GLN F NE2 
12642 N N   . GLU F 161 ? 5.2280 3.4642 2.7296 -2.2272 -0.4570 0.1662  161 GLU F N   
12643 C CA  . GLU F 161 ? 5.1194 3.4383 2.6078 -2.2345 -0.4971 0.2154  161 GLU F CA  
12644 C C   . GLU F 161 ? 5.1281 3.4491 2.5394 -2.2670 -0.4845 0.2046  161 GLU F C   
12645 O O   . GLU F 161 ? 5.2012 3.5190 2.5580 -2.3124 -0.4385 0.1613  161 GLU F O   
12646 C CB  . GLU F 161 ? 5.0471 3.5307 2.5395 -2.2847 -0.5054 0.2441  161 GLU F CB  
12647 C CG  . GLU F 161 ? 5.0793 3.5717 2.6520 -2.2478 -0.5237 0.2685  161 GLU F CG  
12648 C CD  . GLU F 161 ? 4.9913 3.6674 2.5762 -2.2602 -0.5268 0.3066  161 GLU F CD  
12649 O OE1 . GLU F 161 ? 4.9249 3.7163 2.4482 -2.3210 -0.5169 0.3077  161 GLU F OE1 
12650 O OE2 . GLU F 161 ? 5.0019 3.7082 2.6575 -2.2084 -0.5377 0.3351  161 GLU F OE2 
12651 N N   . SER F 162 ? 5.1837 3.5083 2.5920 -2.2434 -0.5240 0.2442  162 SER F N   
12652 C CA  . SER F 162 ? 5.1426 3.4966 2.4806 -2.2784 -0.5187 0.2443  162 SER F CA  
12653 C C   . SER F 162 ? 5.0689 3.5451 2.4117 -2.2895 -0.5629 0.3005  162 SER F C   
12654 O O   . SER F 162 ? 5.0019 3.4614 2.4022 -2.2382 -0.6061 0.3425  162 SER F O   
12655 C CB  . SER F 162 ? 5.1854 3.3878 2.5089 -2.2293 -0.5189 0.2315  162 SER F CB  
12656 O OG  . SER F 162 ? 5.2240 3.4494 2.4774 -2.2661 -0.5082 0.2283  162 SER F OG  
12657 N N   . VAL F 163 ? 5.2457 3.8472 2.5307 -2.3546 -0.5509 0.3018  163 VAL F N   
12658 C CA  . VAL F 163 ? 5.1330 3.8664 2.4177 -2.3693 -0.5903 0.3542  163 VAL F CA  
12659 C C   . VAL F 163 ? 5.0756 3.8156 2.2991 -2.3891 -0.5877 0.3543  163 VAL F C   
12660 O O   . VAL F 163 ? 5.1340 3.8596 2.3001 -2.4300 -0.5427 0.3111  163 VAL F O   
12661 C CB  . VAL F 163 ? 5.0796 3.9961 2.3585 -2.4252 -0.5819 0.3624  163 VAL F CB  
12662 C CG1 . VAL F 163 ? 4.9605 4.0245 2.2605 -2.3933 -0.6171 0.4270  163 VAL F CG1 
12663 C CG2 . VAL F 163 ? 5.1424 4.0465 2.4759 -2.4031 -0.5682 0.3530  163 VAL F CG2 
12664 N N   . THR F 164 ? 5.2114 3.9718 2.4483 -2.3606 -0.6337 0.4028  164 THR F N   
12665 C CA  . THR F 164 ? 5.1376 3.9166 2.3205 -2.3791 -0.6333 0.4085  164 THR F CA  
12666 C C   . THR F 164 ? 5.0662 4.0381 2.2165 -2.4430 -0.6152 0.4158  164 THR F C   
12667 O O   . THR F 164 ? 5.0461 4.1533 2.2233 -2.4555 -0.6196 0.4335  164 THR F O   
12668 C CB  . THR F 164 ? 5.0673 3.8096 2.2782 -2.3244 -0.6879 0.4589  164 THR F CB  
12669 O OG1 . THR F 164 ? 5.0116 3.8885 2.2782 -2.2856 -0.7166 0.5134  164 THR F OG1 
12670 C CG2 . THR F 164 ? 5.1301 3.6868 2.3805 -2.2527 -0.6993 0.4524  164 THR F CG2 
12671 N N   . GLU F 165 ? 5.2240 4.2115 2.3257 -2.4762 -0.5894 0.4034  165 GLU F N   
12672 C CA  . GLU F 165 ? 5.1289 4.3050 2.2405 -2.5195 -0.5721 0.4200  165 GLU F CA  
12673 C C   . GLU F 165 ? 5.0168 4.2951 2.2141 -2.4627 -0.6178 0.4808  165 GLU F C   
12674 O O   . GLU F 165 ? 5.0137 4.1965 2.2302 -2.4023 -0.6590 0.5104  165 GLU F O   
12675 C CB  . GLU F 165 ? 5.1129 4.2719 2.1679 -2.5640 -0.5341 0.3919  165 GLU F CB  
12676 C CG  . GLU F 165 ? 5.2195 4.3093 2.2045 -2.6122 -0.4769 0.3255  165 GLU F CG  
12677 C CD  . GLU F 165 ? 5.2319 4.4585 2.2256 -2.6642 -0.4430 0.3037  165 GLU F CD  
12678 O OE1 . GLU F 165 ? 5.1747 4.5845 2.2073 -2.6944 -0.4384 0.3243  165 GLU F OE1 
12679 O OE2 . GLU F 165 ? 5.4393 4.5940 2.4162 -2.6699 -0.4196 0.2633  165 GLU F OE2 
12680 N N   . GLN F 166 ? 4.9057 4.3834 2.1660 -2.4703 -0.6083 0.4960  166 GLN F N   
12681 C CA  . GLN F 166 ? 4.7930 4.3839 2.1506 -2.4001 -0.6416 0.5475  166 GLN F CA  
12682 C C   . GLN F 166 ? 4.7475 4.2709 2.1111 -2.3711 -0.6613 0.5618  166 GLN F C   
12683 O O   . GLN F 166 ? 4.7995 4.3101 2.1191 -2.4207 -0.6373 0.5358  166 GLN F O   
12684 C CB  . GLN F 166 ? 4.7596 4.5727 2.1718 -2.4189 -0.6197 0.5511  166 GLN F CB  
12685 C CG  . GLN F 166 ? 4.7181 4.6643 2.2322 -2.3412 -0.6457 0.6026  166 GLN F CG  
12686 C CD  . GLN F 166 ? 4.7168 4.8766 2.2771 -2.3564 -0.6238 0.6050  166 GLN F CD  
12687 O OE1 . GLN F 166 ? 4.7217 4.9541 2.2508 -2.4260 -0.5915 0.5696  166 GLN F OE1 
12688 N NE2 . GLN F 166 ? 4.7163 4.9763 2.3501 -2.2897 -0.6391 0.6467  166 GLN F NE2 
12689 N N   . ASP F 167 ? 4.7910 4.2698 2.2093 -2.2902 -0.7021 0.6025  167 ASP F N   
12690 C CA  . ASP F 167 ? 4.7598 4.1632 2.1861 -2.2563 -0.7234 0.6157  167 ASP F CA  
12691 C C   . ASP F 167 ? 4.7165 4.2707 2.1879 -2.2644 -0.7104 0.6225  167 ASP F C   
12692 O O   . ASP F 167 ? 4.6954 4.4186 2.2388 -2.2408 -0.7076 0.6445  167 ASP F O   
12693 C CB  . ASP F 167 ? 4.7451 4.0889 2.2336 -2.1639 -0.7660 0.6568  167 ASP F CB  
12694 C CG  . ASP F 167 ? 4.7200 3.9609 2.2095 -2.1282 -0.7889 0.6652  167 ASP F CG  
12695 O OD1 . ASP F 167 ? 4.7495 3.8250 2.1579 -2.1535 -0.7913 0.6407  167 ASP F OD1 
12696 O OD2 . ASP F 167 ? 4.6775 3.9988 2.2459 -2.0728 -0.8030 0.6954  167 ASP F OD2 
12697 N N   . SER F 168 ? 4.6499 4.1385 2.0749 -2.2968 -0.7015 0.6035  168 SER F N   
12698 C CA  . SER F 168 ? 4.6251 4.2452 2.0813 -2.3141 -0.6866 0.6045  168 SER F CA  
12699 C C   . SER F 168 ? 4.5719 4.2872 2.1295 -2.2311 -0.7150 0.6501  168 SER F C   
12700 O O   . SER F 168 ? 4.5494 4.4242 2.1545 -2.2330 -0.7033 0.6586  168 SER F O   
12701 C CB  . SER F 168 ? 4.7051 4.2104 2.0847 -2.3619 -0.6717 0.5766  168 SER F CB  
12702 O OG  . SER F 168 ? 4.6894 4.0602 2.0732 -2.3046 -0.7063 0.5963  168 SER F OG  
12703 N N   . LYS F 169 ? 4.5611 4.1831 2.1533 -2.1567 -0.7495 0.6785  169 LYS F N   
12704 C CA  . LYS F 169 ? 4.5279 4.2243 2.2142 -2.0749 -0.7712 0.7192  169 LYS F CA  
12705 C C   . LYS F 169 ? 4.5303 4.3404 2.2922 -2.0207 -0.7759 0.7512  169 LYS F C   
12706 O O   . LYS F 169 ? 4.5160 4.4843 2.3377 -1.9988 -0.7667 0.7705  169 LYS F O   
12707 C CB  . LYS F 169 ? 4.5409 4.0779 2.2290 -2.0209 -0.8024 0.7304  169 LYS F CB  
12708 C CG  . LYS F 169 ? 4.5413 3.9797 2.1675 -2.0581 -0.7995 0.7071  169 LYS F CG  
12709 C CD  . LYS F 169 ? 4.5579 3.9034 2.2199 -1.9869 -0.8304 0.7269  169 LYS F CD  
12710 C CE  . LYS F 169 ? 4.6018 3.8727 2.3032 -1.9182 -0.8580 0.7471  169 LYS F CE  
12711 N NZ  . LYS F 169 ? 4.5644 3.7107 2.2805 -1.8602 -0.8863 0.7544  169 LYS F NZ  
12712 N N   . ASP F 170 ? 4.4844 4.2136 2.2413 -1.9982 -0.7886 0.7571  170 ASP F N   
12713 C CA  . ASP F 170 ? 4.4944 4.3051 2.3222 -1.9382 -0.7943 0.7908  170 ASP F CA  
12714 C C   . ASP F 170 ? 4.5262 4.4252 2.3353 -1.9803 -0.7725 0.7805  170 ASP F C   
12715 O O   . ASP F 170 ? 4.5434 4.5129 2.4042 -1.9351 -0.7734 0.8080  170 ASP F O   
12716 C CB  . ASP F 170 ? 4.5038 4.1780 2.3524 -1.8757 -0.8231 0.8087  170 ASP F CB  
12717 C CG  . ASP F 170 ? 4.5371 4.0588 2.3081 -1.9152 -0.8292 0.7825  170 ASP F CG  
12718 O OD1 . ASP F 170 ? 4.5647 4.1058 2.2792 -1.9802 -0.8084 0.7575  170 ASP F OD1 
12719 O OD2 . ASP F 170 ? 4.5388 3.9173 2.3048 -1.8788 -0.8543 0.7856  170 ASP F OD2 
12720 N N   . SER F 171 ? 4.4526 4.3464 2.1879 -2.0654 -0.7502 0.7406  171 SER F N   
12721 C CA  . SER F 171 ? 4.4831 4.4718 2.1972 -2.1151 -0.7246 0.7233  171 SER F CA  
12722 C C   . SER F 171 ? 4.5249 4.4436 2.2271 -2.1010 -0.7319 0.7283  171 SER F C   
12723 O O   . SER F 171 ? 4.5567 4.5749 2.2676 -2.1149 -0.7154 0.7286  171 SER F O   
12724 C CB  . SER F 171 ? 4.4741 4.6709 2.2556 -2.0940 -0.7111 0.7451  171 SER F CB  
12725 O OG  . SER F 171 ? 4.4424 4.7140 2.2283 -2.1179 -0.7008 0.7356  171 SER F OG  
12726 N N   . THR F 172 ? 4.6481 4.3990 2.3307 -2.0726 -0.7564 0.7326  172 THR F N   
12727 C CA  . THR F 172 ? 4.6930 4.3646 2.3566 -2.0647 -0.7630 0.7343  172 THR F CA  
12728 C C   . THR F 172 ? 4.7450 4.2844 2.3041 -2.1392 -0.7512 0.6877  172 THR F C   
12729 O O   . THR F 172 ? 4.7554 4.2486 2.2564 -2.1923 -0.7382 0.6552  172 THR F O   
12730 C CB  . THR F 172 ? 4.6905 4.2632 2.4024 -1.9825 -0.7961 0.7686  172 THR F CB  
12731 O OG1 . THR F 172 ? 4.6741 4.1015 2.3523 -1.9790 -0.8154 0.7563  172 THR F OG1 
12732 C CG2 . THR F 172 ? 4.6649 4.3640 2.4775 -1.9083 -0.8011 0.8118  172 THR F CG2 
12733 N N   . TYR F 173 ? 4.7145 4.1882 2.2479 -2.1413 -0.7530 0.6846  173 TYR F N   
12734 C CA  . TYR F 173 ? 4.8390 4.1692 2.2736 -2.1995 -0.7438 0.6423  173 TYR F CA  
12735 C C   . TYR F 173 ? 4.9194 4.0802 2.3541 -2.1466 -0.7729 0.6571  173 TYR F C   
12736 O O   . TYR F 173 ? 4.8927 4.0681 2.3932 -2.0775 -0.7958 0.7033  173 TYR F O   
12737 C CB  . TYR F 173 ? 4.8829 4.2870 2.2883 -2.2537 -0.7134 0.6171  173 TYR F CB  
12738 C CG  . TYR F 173 ? 4.7958 4.3692 2.2088 -2.3075 -0.6781 0.5968  173 TYR F CG  
12739 C CD1 . TYR F 173 ? 4.7240 4.4843 2.2176 -2.2753 -0.6742 0.6295  173 TYR F CD1 
12740 C CD2 . TYR F 173 ? 4.8228 4.3677 2.1634 -2.3881 -0.6456 0.5439  173 TYR F CD2 
12741 C CE1 . TYR F 173 ? 4.7147 4.6332 2.2160 -2.3219 -0.6441 0.6110  173 TYR F CE1 
12742 C CE2 . TYR F 173 ? 4.7616 4.4643 2.1120 -2.4378 -0.6112 0.5258  173 TYR F CE2 
12743 C CZ  . TYR F 173 ? 4.7253 4.6169 2.1565 -2.4048 -0.6134 0.5593  173 TYR F CZ  
12744 O OH  . TYR F 173 ? 4.7203 4.7726 2.1625 -2.4519 -0.5823 0.5403  173 TYR F OH  
12745 N N   . SER F 174 ? 5.0033 4.0093 2.4204 -2.1615 -0.7582 0.6056  174 SER F N   
12746 C CA  . SER F 174 ? 5.0764 3.9365 2.5544 -2.0996 -0.7665 0.5972  174 SER F CA  
12747 C C   . SER F 174 ? 5.1848 3.9703 2.6503 -2.1380 -0.7301 0.5383  174 SER F C   
12748 O O   . SER F 174 ? 5.2084 4.0040 2.6070 -2.2120 -0.6999 0.4966  174 SER F O   
12749 C CB  . SER F 174 ? 5.0660 3.7839 2.5417 -2.0588 -0.7911 0.5987  174 SER F CB  
12750 O OG  . SER F 174 ? 4.9697 3.7455 2.4665 -2.0148 -0.8261 0.6543  174 SER F OG  
12751 N N   . LEU F 175 ? 4.9555 3.6659 2.4873 -2.0878 -0.7315 0.5338  175 LEU F N   
12752 C CA  . LEU F 175 ? 5.0009 3.6493 2.5324 -2.1163 -0.6974 0.4827  175 LEU F CA  
12753 C C   . LEU F 175 ? 5.0123 3.5013 2.6004 -2.0523 -0.7074 0.4682  175 LEU F C   
12754 O O   . LEU F 175 ? 4.9964 3.4746 2.6531 -1.9814 -0.7368 0.5039  175 LEU F O   
12755 C CB  . LEU F 175 ? 5.0283 3.8094 2.5849 -2.1341 -0.6796 0.4918  175 LEU F CB  
12756 C CG  . LEU F 175 ? 5.0830 3.8297 2.6443 -2.1657 -0.6427 0.4439  175 LEU F CG  
12757 C CD1 . LEU F 175 ? 5.1062 4.0224 2.6543 -2.2103 -0.6226 0.4532  175 LEU F CD1 
12758 C CD2 . LEU F 175 ? 5.1039 3.7490 2.7468 -2.0981 -0.6497 0.4420  175 LEU F CD2 
12759 N N   . SER F 176 ? 5.0419 3.4102 2.6008 -2.0780 -0.6811 0.4148  176 SER F N   
12760 C CA  . SER F 176 ? 5.0671 3.2905 2.6758 -2.0244 -0.6836 0.3926  176 SER F CA  
12761 C C   . SER F 176 ? 5.1220 3.3423 2.7436 -2.0540 -0.6473 0.3537  176 SER F C   
12762 O O   . SER F 176 ? 5.1444 3.4106 2.7109 -2.1160 -0.6094 0.3213  176 SER F O   
12763 C CB  . SER F 176 ? 5.0636 3.1511 2.6362 -1.9984 -0.6778 0.3638  176 SER F CB  
12764 O OG  . SER F 176 ? 5.0905 3.1633 2.5984 -2.0476 -0.6298 0.3159  176 SER F OG  
12765 N N   . SER F 177 ? 4.7987 2.9774 2.4984 -1.9977 -0.6547 0.3552  177 SER F N   
12766 C CA  . SER F 177 ? 4.8320 2.9779 2.5515 -2.0132 -0.6215 0.3147  177 SER F CA  
12767 C C   . SER F 177 ? 4.8489 2.8496 2.6141 -1.9396 -0.6240 0.2891  177 SER F C   
12768 O O   . SER F 177 ? 4.7984 2.7576 2.6220 -1.8770 -0.6603 0.3150  177 SER F O   
12769 C CB  . SER F 177 ? 4.7660 3.0249 2.5465 -2.0012 -0.6204 0.3390  177 SER F CB  
12770 O OG  . SER F 177 ? 4.8013 3.0263 2.5983 -2.0201 -0.5873 0.2984  177 SER F OG  
12771 N N   . THR F 178 ? 4.7736 2.7018 2.5138 -1.9466 -0.5846 0.2386  178 THR F N   
12772 C CA  . THR F 178 ? 4.8012 2.5937 2.5754 -1.8802 -0.5829 0.2121  178 THR F CA  
12773 C C   . THR F 178 ? 4.8220 2.5832 2.6376 -1.8755 -0.5518 0.1748  178 THR F C   
12774 O O   . THR F 178 ? 4.8767 2.6559 2.6516 -1.9271 -0.5084 0.1412  178 THR F O   
12775 C CB  . THR F 178 ? 4.8774 2.5916 2.5828 -1.8840 -0.5623 0.1874  178 THR F CB  
12776 O OG1 . THR F 178 ? 4.8594 2.6082 2.5233 -1.8931 -0.5893 0.2213  178 THR F OG1 
12777 C CG2 . THR F 178 ? 4.9047 2.4825 2.6447 -1.8106 -0.5647 0.1667  178 THR F CG2 
12778 N N   . LEU F 179 ? 4.9700 2.6853 2.8675 -1.8132 -0.5732 0.1791  179 LEU F N   
12779 C CA  . LEU F 179 ? 4.9822 2.6622 2.9313 -1.7985 -0.5486 0.1456  179 LEU F CA  
12780 C C   . LEU F 179 ? 5.0358 2.5861 2.9925 -1.7458 -0.5378 0.1117  179 LEU F C   
12781 O O   . LEU F 179 ? 5.0168 2.5065 2.9994 -1.6847 -0.5705 0.1256  179 LEU F O   
12782 C CB  . LEU F 179 ? 4.9039 2.6151 2.9418 -1.7617 -0.5772 0.1698  179 LEU F CB  
12783 C CG  . LEU F 179 ? 4.9055 2.5743 3.0125 -1.7333 -0.5589 0.1377  179 LEU F CG  
12784 C CD1 . LEU F 179 ? 4.9330 2.6626 3.0177 -1.7980 -0.5167 0.1160  179 LEU F CD1 
12785 C CD2 . LEU F 179 ? 4.8285 2.5076 3.0264 -1.6816 -0.5936 0.1630  179 LEU F CD2 
12786 N N   . THR F 180 ? 5.0010 2.5101 2.9347 -1.7682 -0.4917 0.0682  180 THR F N   
12787 C CA  . THR F 180 ? 5.0617 2.4477 2.9962 -1.7218 -0.4764 0.0369  180 THR F CA  
12788 C C   . THR F 180 ? 5.0671 2.4159 3.0669 -1.6961 -0.4575 0.0057  180 THR F C   
12789 O O   . THR F 180 ? 5.0863 2.4766 3.0801 -1.7432 -0.4223 -0.0161 180 THR F O   
12790 C CB  . THR F 180 ? 5.1519 2.5053 2.9968 -1.7673 -0.4338 0.0114  180 THR F CB  
12791 O OG1 . THR F 180 ? 5.1444 2.5485 2.9281 -1.8004 -0.4490 0.0392  180 THR F OG1 
12792 C CG2 . THR F 180 ? 5.2181 2.4392 3.0580 -1.7155 -0.4200 -0.0136 180 THR F CG2 
12793 N N   . LEU F 181 ? 5.2541 2.5280 3.3161 -1.6215 -0.4809 0.0027  181 LEU F N   
12794 C CA  . LEU F 181 ? 5.3140 2.5452 3.4445 -1.5876 -0.4670 -0.0274 181 LEU F CA  
12795 C C   . LEU F 181 ? 5.3581 2.4685 3.4922 -1.5281 -0.4630 -0.0501 181 LEU F C   
12796 O O   . LEU F 181 ? 5.3286 2.3929 3.4357 -1.4953 -0.4860 -0.0339 181 LEU F O   
12797 C CB  . LEU F 181 ? 5.3419 2.6187 3.5635 -1.5519 -0.5033 -0.0079 181 LEU F CB  
12798 C CG  . LEU F 181 ? 5.4131 2.8073 3.6380 -1.6014 -0.5123 0.0224  181 LEU F CG  
12799 C CD1 . LEU F 181 ? 5.4339 2.8565 3.7424 -1.5547 -0.5545 0.0496  181 LEU F CD1 
12800 C CD2 . LEU F 181 ? 5.5144 2.9552 3.7345 -1.6568 -0.4696 -0.0019 181 LEU F CD2 
12801 N N   . SER F 182 ? 5.4944 2.5539 3.6600 -1.5140 -0.4329 -0.0870 182 SER F N   
12802 C CA  . SER F 182 ? 5.5547 2.5045 3.7411 -1.4470 -0.4347 -0.1060 182 SER F CA  
12803 C C   . SER F 182 ? 5.5339 2.4809 3.8010 -1.3762 -0.4868 -0.0886 182 SER F C   
12804 O O   . SER F 182 ? 5.4924 2.5159 3.8149 -1.3792 -0.5114 -0.0712 182 SER F O   
12805 C CB  . SER F 182 ? 5.6514 2.5531 3.8565 -1.4489 -0.3905 -0.1486 182 SER F CB  
12806 O OG  . SER F 182 ? 5.6693 2.6214 3.9544 -1.4452 -0.3950 -0.1572 182 SER F OG  
12807 N N   . LYS F 183 ? 5.4689 2.3271 3.7408 -1.3115 -0.5024 -0.0934 183 LYS F N   
12808 C CA  . LYS F 183 ? 5.4599 2.3120 3.8094 -1.2403 -0.5505 -0.0827 183 LYS F CA  
12809 C C   . LYS F 183 ? 5.5031 2.3824 3.9457 -1.2243 -0.5496 -0.1043 183 LYS F C   
12810 O O   . LYS F 183 ? 5.4367 2.3698 3.9483 -1.2009 -0.5850 -0.0890 183 LYS F O   
12811 C CB  . LYS F 183 ? 5.5073 2.2552 3.8415 -1.1737 -0.5614 -0.0900 183 LYS F CB  
12812 C CG  . LYS F 183 ? 5.5019 2.2425 3.9133 -1.0963 -0.6121 -0.0826 183 LYS F CG  
12813 C CD  . LYS F 183 ? 5.5658 2.2011 3.9570 -1.0296 -0.6184 -0.0930 183 LYS F CD  
12814 C CE  . LYS F 183 ? 5.5410 2.1789 3.9853 -0.9576 -0.6756 -0.0765 183 LYS F CE  
12815 N NZ  . LYS F 183 ? 5.5310 2.2164 4.0821 -0.9289 -0.6976 -0.0909 183 LYS F NZ  
12816 N N   . ALA F 184 ? 5.5284 2.3696 3.9755 -1.2357 -0.5077 -0.1408 184 ALA F N   
12817 C CA  . ALA F 184 ? 5.5313 2.3963 4.0648 -1.2240 -0.5019 -0.1645 184 ALA F CA  
12818 C C   . ALA F 184 ? 5.4452 2.4183 4.0106 -1.2700 -0.5073 -0.1466 184 ALA F C   
12819 O O   . ALA F 184 ? 5.3924 2.4037 4.0397 -1.2413 -0.5332 -0.1429 184 ALA F O   
12820 C CB  . ALA F 184 ? 5.6330 2.4447 4.1523 -1.2407 -0.4504 -0.2042 184 ALA F CB  
12821 N N   . ASP F 185 ? 5.5585 2.5825 4.0590 -1.3419 -0.4813 -0.1361 185 ASP F N   
12822 C CA  . ASP F 185 ? 5.5168 2.6437 4.0375 -1.3880 -0.4837 -0.1165 185 ASP F CA  
12823 C C   . ASP F 185 ? 5.4685 2.6450 4.0139 -1.3665 -0.5329 -0.0751 185 ASP F C   
12824 O O   . ASP F 185 ? 5.4772 2.7168 4.0834 -1.3673 -0.5468 -0.0619 185 ASP F O   
12825 C CB  . ASP F 185 ? 5.5399 2.7130 3.9774 -1.4684 -0.4477 -0.1138 185 ASP F CB  
12826 C CG  . ASP F 185 ? 5.6141 2.7730 4.0489 -1.5003 -0.3973 -0.1531 185 ASP F CG  
12827 O OD1 . ASP F 185 ? 5.6417 2.7714 4.1477 -1.4655 -0.3915 -0.1785 185 ASP F OD1 
12828 O OD2 . ASP F 185 ? 5.6450 2.8253 4.0071 -1.5612 -0.3630 -0.1597 185 ASP F OD2 
12829 N N   . TYR F 186 ? 5.4037 2.5515 3.9014 -1.3482 -0.5574 -0.0535 186 TYR F N   
12830 C CA  . TYR F 186 ? 5.3547 2.5466 3.8724 -1.3266 -0.6041 -0.0132 186 TYR F CA  
12831 C C   . TYR F 186 ? 5.3356 2.5225 3.9564 -1.2621 -0.6350 -0.0180 186 TYR F C   
12832 O O   . TYR F 186 ? 5.3246 2.5778 3.9946 -1.2617 -0.6569 0.0060  186 TYR F O   
12833 C CB  . TYR F 186 ? 5.3033 2.4507 3.7546 -1.3103 -0.6230 0.0048  186 TYR F CB  
12834 C CG  . TYR F 186 ? 5.2528 2.4411 3.7214 -1.2858 -0.6711 0.0461  186 TYR F CG  
12835 C CD1 . TYR F 186 ? 5.2584 2.5368 3.7092 -1.3333 -0.6790 0.0816  186 TYR F CD1 
12836 C CD2 . TYR F 186 ? 5.2019 2.3406 3.7031 -1.2151 -0.7080 0.0503  186 TYR F CD2 
12837 C CE1 . TYR F 186 ? 5.2168 2.5315 3.6839 -1.3111 -0.7208 0.1206  186 TYR F CE1 
12838 C CE2 . TYR F 186 ? 5.1572 2.3346 3.6753 -1.1929 -0.7505 0.0872  186 TYR F CE2 
12839 C CZ  . TYR F 186 ? 5.1659 2.4295 3.6676 -1.2411 -0.7559 0.1226  186 TYR F CZ  
12840 O OH  . TYR F 186 ? 5.1252 2.4263 3.6441 -1.2191 -0.7961 0.1607  186 TYR F OH  
12841 N N   . GLU F 187 ? 5.2088 2.3185 3.8636 -1.2071 -0.6358 -0.0497 187 GLU F N   
12842 C CA  . GLU F 187 ? 5.1874 2.2935 3.9404 -1.1438 -0.6661 -0.0591 187 GLU F CA  
12843 C C   . GLU F 187 ? 5.2325 2.3773 4.0608 -1.1561 -0.6460 -0.0814 187 GLU F C   
12844 O O   . GLU F 187 ? 5.2198 2.3746 4.1366 -1.1106 -0.6680 -0.0908 187 GLU F O   
12845 C CB  . GLU F 187 ? 5.2263 2.2399 3.9864 -1.0785 -0.6767 -0.0842 187 GLU F CB  
12846 C CG  . GLU F 187 ? 5.2355 2.2041 3.9182 -1.0644 -0.6938 -0.0623 187 GLU F CG  
12847 C CD  . GLU F 187 ? 5.2893 2.1743 3.9858 -0.9898 -0.7136 -0.0797 187 GLU F CD  
12848 O OE1 . GLU F 187 ? 5.3752 2.1965 4.0729 -0.9737 -0.6873 -0.1138 187 GLU F OE1 
12849 O OE2 . GLU F 187 ? 5.2488 2.1325 3.9535 -0.9462 -0.7554 -0.0587 187 GLU F OE2 
12850 N N   . LYS F 188 ? 5.1120 2.2803 3.9078 -1.2166 -0.6039 -0.0917 188 LYS F N   
12851 C CA  . LYS F 188 ? 5.0884 2.2946 3.9474 -1.2344 -0.5802 -0.1117 188 LYS F CA  
12852 C C   . LYS F 188 ? 5.0191 2.3176 3.8990 -1.2684 -0.5888 -0.0773 188 LYS F C   
12853 O O   . LYS F 188 ? 4.9966 2.3334 3.9252 -1.2877 -0.5683 -0.0879 188 LYS F O   
12854 C CB  . LYS F 188 ? 5.1557 2.3428 3.9678 -1.2826 -0.5290 -0.1399 188 LYS F CB  
12855 C CG  . LYS F 188 ? 5.1470 2.3525 4.0256 -1.2923 -0.5002 -0.1703 188 LYS F CG  
12856 C CD  . LYS F 188 ? 5.2117 2.4081 4.0369 -1.3460 -0.4494 -0.1942 188 LYS F CD  
12857 C CE  . LYS F 188 ? 5.2931 2.4007 4.0653 -1.3296 -0.4345 -0.2167 188 LYS F CE  
12858 N NZ  . LYS F 188 ? 5.3568 2.4539 4.0871 -1.3787 -0.3824 -0.2440 188 LYS F NZ  
12859 N N   . HIS F 189 ? 4.9649 2.2974 3.8094 -1.2743 -0.6179 -0.0352 189 HIS F N   
12860 C CA  . HIS F 189 ? 4.9675 2.3839 3.8264 -1.3033 -0.6279 0.0036  189 HIS F CA  
12861 C C   . HIS F 189 ? 4.9112 2.3366 3.7882 -1.2621 -0.6748 0.0372  189 HIS F C   
12862 O O   . HIS F 189 ? 4.8696 2.2432 3.7231 -1.2249 -0.6974 0.0355  189 HIS F O   
12863 C CB  . HIS F 189 ? 5.0154 2.4852 3.7858 -1.3800 -0.6038 0.0261  189 HIS F CB  
12864 C CG  . HIS F 189 ? 5.0805 2.5476 3.8267 -1.4246 -0.5564 -0.0067 189 HIS F CG  
12865 N ND1 . HIS F 189 ? 5.0983 2.5329 3.7644 -1.4563 -0.5310 -0.0243 189 HIS F ND1 
12866 C CD2 . HIS F 189 ? 5.1324 2.6249 3.9239 -1.4431 -0.5279 -0.0256 189 HIS F CD2 
12867 C CE1 . HIS F 189 ? 5.1605 2.6025 3.8248 -1.4918 -0.4897 -0.0531 189 HIS F CE1 
12868 N NE2 . HIS F 189 ? 5.1823 2.6593 3.9212 -1.4845 -0.4877 -0.0541 189 HIS F NE2 
12869 N N   . LYS F 190 ? 4.8445 2.3403 3.7653 -1.2657 -0.6860 0.0688  190 LYS F N   
12870 C CA  . LYS F 190 ? 4.7897 2.3114 3.7416 -1.2221 -0.7250 0.1012  190 LYS F CA  
12871 C C   . LYS F 190 ? 4.7977 2.3923 3.6897 -1.2560 -0.7316 0.1538  190 LYS F C   
12872 O O   . LYS F 190 ? 4.7619 2.3336 3.6036 -1.2477 -0.7587 0.1734  190 LYS F O   
12873 C CB  . LYS F 190 ? 4.7751 2.3368 3.8413 -1.1793 -0.7286 0.0963  190 LYS F CB  
12874 C CG  . LYS F 190 ? 4.7262 2.3317 3.8241 -1.1442 -0.7614 0.1345  190 LYS F CG  
12875 C CD  . LYS F 190 ? 4.7065 2.3408 3.9190 -1.1000 -0.7637 0.1236  190 LYS F CD  
12876 C CE  . LYS F 190 ? 4.7629 2.4700 4.0076 -1.1318 -0.7249 0.1348  190 LYS F CE  
12877 N NZ  . LYS F 190 ? 4.7389 2.4808 4.0899 -1.0920 -0.7249 0.1327  190 LYS F NZ  
12878 N N   . VAL F 191 ? 4.7827 2.4664 3.6772 -1.2931 -0.7068 0.1776  191 VAL F N   
12879 C CA  . VAL F 191 ? 4.7895 2.5578 3.6425 -1.3161 -0.7137 0.2311  191 VAL F CA  
12880 C C   . VAL F 191 ? 4.8212 2.6029 3.5650 -1.3797 -0.6997 0.2396  191 VAL F C   
12881 O O   . VAL F 191 ? 4.8669 2.6624 3.5802 -1.4274 -0.6653 0.2208  191 VAL F O   
12882 C CB  . VAL F 191 ? 4.8169 2.6787 3.7240 -1.3205 -0.6921 0.2559  191 VAL F CB  
12883 C CG1 . VAL F 191 ? 4.8135 2.7611 3.6892 -1.3292 -0.7034 0.3146  191 VAL F CG1 
12884 C CG2 . VAL F 191 ? 4.7941 2.6363 3.8126 -1.2652 -0.6964 0.2359  191 VAL F CG2 
12885 N N   . TYR F 192 ? 4.9714 2.7504 3.6565 -1.3820 -0.7253 0.2662  192 TYR F N   
12886 C CA  . TYR F 192 ? 4.9965 2.7966 3.5780 -1.4428 -0.7142 0.2765  192 TYR F CA  
12887 C C   . TYR F 192 ? 5.0008 2.9053 3.5588 -1.4553 -0.7259 0.3323  192 TYR F C   
12888 O O   . TYR F 192 ? 4.9603 2.8662 3.5399 -1.4142 -0.7583 0.3604  192 TYR F O   
12889 C CB  . TYR F 192 ? 4.9566 2.6543 3.4800 -1.4383 -0.7298 0.2556  192 TYR F CB  
12890 C CG  . TYR F 192 ? 4.9625 2.5619 3.4907 -1.4359 -0.7102 0.2020  192 TYR F CG  
12891 C CD1 . TYR F 192 ? 4.9226 2.4583 3.5279 -1.3705 -0.7240 0.1762  192 TYR F CD1 
12892 C CD2 . TYR F 192 ? 5.0022 2.5938 3.4662 -1.4894 -0.6720 0.1755  192 TYR F CD2 
12893 C CE1 . TYR F 192 ? 4.9218 2.3923 3.5405 -1.3543 -0.7002 0.1283  192 TYR F CE1 
12894 C CE2 . TYR F 192 ? 5.0023 2.5252 3.4796 -1.4733 -0.6461 0.1276  192 TYR F CE2 
12895 C CZ  . TYR F 192 ? 4.9637 2.4256 3.5180 -1.4054 -0.6607 0.1055  192 TYR F CZ  
12896 O OH  . TYR F 192 ? 4.9674 2.3622 3.5350 -1.3888 -0.6346 0.0596  192 TYR F OH  
12897 N N   . ALA F 193 ? 4.9755 2.9690 3.4880 -1.5113 -0.6993 0.3480  193 ALA F N   
12898 C CA  . ALA F 193 ? 4.9898 3.0980 3.4823 -1.5242 -0.7046 0.4020  193 ALA F CA  
12899 C C   . ALA F 193 ? 5.0342 3.2038 3.4305 -1.5961 -0.6854 0.4067  193 ALA F C   
12900 O O   . ALA F 193 ? 5.0758 3.2368 3.4427 -1.6408 -0.6545 0.3724  193 ALA F O   
12901 C CB  . ALA F 193 ? 5.0013 3.1879 3.5636 -1.5058 -0.6881 0.4249  193 ALA F CB  
12902 N N   . CYS F 194 ? 5.1677 3.4005 3.5154 -1.6083 -0.7029 0.4466  194 CYS F N   
12903 C CA  . CYS F 194 ? 5.1846 3.5105 3.4504 -1.6748 -0.6851 0.4591  194 CYS F CA  
12904 C C   . CYS F 194 ? 5.1269 3.5873 3.4076 -1.6674 -0.6862 0.5157  194 CYS F C   
12905 O O   . CYS F 194 ? 5.0704 3.5449 3.3854 -1.6207 -0.7125 0.5543  194 CYS F O   
12906 C CB  . CYS F 194 ? 5.0865 3.3769 3.2721 -1.7028 -0.7003 0.4545  194 CYS F CB  
12907 S SG  . CYS F 194 ? 5.0034 3.3005 3.1927 -1.6557 -0.7462 0.5040  194 CYS F SG  
12908 N N   . GLU F 195 ? 5.0018 3.5601 3.2558 -1.7119 -0.6561 0.5206  195 GLU F N   
12909 C CA  . GLU F 195 ? 4.8899 3.5834 3.1502 -1.7077 -0.6504 0.5742  195 GLU F CA  
12910 C C   . GLU F 195 ? 4.8397 3.6359 3.0094 -1.7661 -0.6470 0.5908  195 GLU F C   
12911 O O   . GLU F 195 ? 4.8958 3.6993 3.0082 -1.8264 -0.6254 0.5545  195 GLU F O   
12912 C CB  . GLU F 195 ? 4.9276 3.6604 3.2336 -1.7058 -0.6176 0.5700  195 GLU F CB  
12913 C CG  . GLU F 195 ? 4.8904 3.7384 3.2234 -1.6793 -0.6116 0.6290  195 GLU F CG  
12914 C CD  . GLU F 195 ? 5.0149 3.9060 3.3805 -1.6841 -0.5747 0.6247  195 GLU F CD  
12915 O OE1 . GLU F 195 ? 5.1144 3.9560 3.4762 -1.7147 -0.5538 0.5751  195 GLU F OE1 
12916 O OE2 . GLU F 195 ? 4.9862 3.9569 3.3814 -1.6555 -0.5648 0.6717  195 GLU F OE2 
12917 N N   . VAL F 196 ? 5.1731 4.0496 3.3308 -1.7487 -0.6672 0.6436  196 VAL F N   
12918 C CA  . VAL F 196 ? 5.0329 4.0092 3.1084 -1.7976 -0.6702 0.6622  196 VAL F CA  
12919 C C   . VAL F 196 ? 4.9326 4.0672 3.0032 -1.7990 -0.6571 0.7133  196 VAL F C   
12920 O O   . VAL F 196 ? 4.9092 4.0738 3.0330 -1.7440 -0.6646 0.7595  196 VAL F O   
12921 C CB  . VAL F 196 ? 4.9591 3.8986 3.0161 -1.7773 -0.7061 0.6815  196 VAL F CB  
12922 C CG1 . VAL F 196 ? 4.8037 3.8629 2.7835 -1.8228 -0.7094 0.7071  196 VAL F CG1 
12923 C CG2 . VAL F 196 ? 5.0336 3.8216 3.0815 -1.7799 -0.7162 0.6312  196 VAL F CG2 
12924 N N   . THR F 197 ? 4.8483 4.0843 2.8539 -1.8612 -0.6356 0.7043  197 THR F N   
12925 C CA  . THR F 197 ? 4.8185 4.2182 2.8052 -1.8682 -0.6225 0.7513  197 THR F CA  
12926 C C   . THR F 197 ? 4.8291 4.3314 2.7394 -1.9085 -0.6355 0.7697  197 THR F C   
12927 O O   . THR F 197 ? 4.8810 4.3743 2.7297 -1.9704 -0.6301 0.7268  197 THR F O   
12928 C CB  . THR F 197 ? 4.8517 4.3051 2.8262 -1.9077 -0.5851 0.7258  197 THR F CB  
12929 O OG1 . THR F 197 ? 4.9110 4.2628 2.9565 -1.8736 -0.5719 0.7033  197 THR F OG1 
12930 C CG2 . THR F 197 ? 4.8371 4.4618 2.7936 -1.9067 -0.5714 0.7785  197 THR F CG2 
12931 N N   . HIS F 198 ? 4.8942 4.4936 2.8086 -1.8740 -0.6501 0.8320  198 HIS F N   
12932 C CA  . HIS F 198 ? 4.8954 4.6098 2.7416 -1.9078 -0.6624 0.8549  198 HIS F CA  
12933 C C   . HIS F 198 ? 4.8774 4.7313 2.7361 -1.8676 -0.6625 0.9272  198 HIS F C   
12934 O O   . HIS F 198 ? 4.8522 4.6729 2.7758 -1.8021 -0.6651 0.9638  198 HIS F O   
12935 C CB  . HIS F 198 ? 4.8762 4.5012 2.7081 -1.9030 -0.6941 0.8469  198 HIS F CB  
12936 C CG  . HIS F 198 ? 4.8805 4.6140 2.6425 -1.9422 -0.7058 0.8631  198 HIS F CG  
12937 N ND1 . HIS F 198 ? 4.8260 4.6681 2.6629 -1.8809 -0.7135 0.8962  198 HIS F ND1 
12938 C CD2 . HIS F 198 ? 4.8780 4.6352 2.5788 -2.0097 -0.6993 0.8190  198 HIS F CD2 
12939 C CE1 . HIS F 198 ? 4.8159 4.7446 2.6410 -1.9101 -0.7115 0.8754  198 HIS F CE1 
12940 N NE2 . HIS F 198 ? 4.8204 4.7013 2.5652 -1.9891 -0.7030 0.8282  198 HIS F NE2 
12941 N N   . GLN F 199 ? 4.7254 4.7421 2.5744 -1.8860 -0.6518 0.9251  199 GLN F N   
12942 C CA  . GLN F 199 ? 4.6970 4.8583 2.6145 -1.8236 -0.6391 0.9673  199 GLN F CA  
12943 C C   . GLN F 199 ? 4.6455 4.8022 2.6322 -1.7475 -0.6587 1.0025  199 GLN F C   
12944 O O   . GLN F 199 ? 4.6270 4.8653 2.6725 -1.6838 -0.6465 1.0433  199 GLN F O   
12945 C CB  . GLN F 199 ? 4.7065 5.0441 2.6138 -1.8545 -0.6209 0.9515  199 GLN F CB  
12946 C CG  . GLN F 199 ? 4.6839 5.0683 2.5914 -1.8706 -0.6349 0.9322  199 GLN F CG  
12947 C CD  . GLN F 199 ? 4.6868 5.2620 2.6091 -1.8798 -0.6159 0.9300  199 GLN F CD  
12948 O OE1 . GLN F 199 ? 4.6606 5.3378 2.6418 -1.8166 -0.6125 0.9676  199 GLN F OE1 
12949 N NE2 . GLN F 199 ? 4.7239 5.3460 2.5924 -1.9580 -0.6017 0.8848  199 GLN F NE2 
12950 N N   . GLY F 200 ? 4.9997 5.0615 2.9791 -1.7512 -0.6859 0.9871  200 GLY F N   
12951 C CA  . GLY F 200 ? 4.9517 5.0007 2.9968 -1.6798 -0.7032 1.0169  200 GLY F CA  
12952 C C   . GLY F 200 ? 4.9384 4.8749 3.0269 -1.6238 -0.7112 1.0459  200 GLY F C   
12953 O O   . GLY F 200 ? 4.9008 4.8411 3.0521 -1.5576 -0.7187 1.0738  200 GLY F O   
12954 N N   . LEU F 201 ? 4.9308 4.7650 2.9889 -1.6508 -0.7072 1.0378  201 LEU F N   
12955 C CA  . LEU F 201 ? 4.9236 4.6410 3.0250 -1.6056 -0.7119 1.0614  201 LEU F CA  
12956 C C   . LEU F 201 ? 4.9485 4.7442 3.0946 -1.5650 -0.6809 1.0995  201 LEU F C   
12957 O O   . LEU F 201 ? 4.9964 4.8734 3.1123 -1.5974 -0.6550 1.0967  201 LEU F O   
12958 C CB  . LEU F 201 ? 4.9447 4.5123 3.0346 -1.6387 -0.7137 1.0132  201 LEU F CB  
12959 C CG  . LEU F 201 ? 4.9400 4.4009 3.0026 -1.6640 -0.7402 0.9681  201 LEU F CG  
12960 C CD1 . LEU F 201 ? 4.9604 4.3074 3.0357 -1.6888 -0.7280 0.9008  201 LEU F CD1 
12961 C CD2 . LEU F 201 ? 4.9036 4.2824 3.0100 -1.6071 -0.7707 0.9901  201 LEU F CD2 
12962 N N   . SER F 202 ? 4.8706 4.6430 3.0881 -1.4934 -0.6811 1.1338  202 SER F N   
12963 C CA  . SER F 202 ? 4.8991 4.7228 3.1579 -1.4524 -0.6479 1.1713  202 SER F CA  
12964 C C   . SER F 202 ? 4.9526 4.6926 3.1913 -1.4891 -0.6308 1.1630  202 SER F C   
12965 O O   . SER F 202 ? 4.9754 4.7840 3.2179 -1.4852 -0.5969 1.1815  202 SER F O   
12966 C CB  . SER F 202 ? 4.8962 4.6864 3.2330 -1.3734 -0.6489 1.2042  202 SER F CB  
12967 O OG  . SER F 202 ? 4.9592 4.5899 3.3155 -1.3703 -0.6720 1.1919  202 SER F OG  
12968 N N   . SER F 203 ? 5.0259 4.6304 3.2934 -1.4992 -0.6451 1.1038  203 SER F N   
12969 C CA  . SER F 203 ? 5.0201 4.5493 3.3256 -1.5097 -0.6228 1.0539  203 SER F CA  
12970 C C   . SER F 203 ? 5.0097 4.4373 3.2958 -1.5503 -0.6427 0.9865  203 SER F C   
12971 O O   . SER F 203 ? 4.9890 4.3628 3.2630 -1.5469 -0.6751 0.9803  203 SER F O   
12972 C CB  . SER F 203 ? 5.0295 4.4745 3.4284 -1.4488 -0.6114 1.0607  203 SER F CB  
12973 O OG  . SER F 203 ? 5.0590 4.4491 3.4945 -1.4588 -0.5855 1.0169  203 SER F OG  
12974 N N   . PRO F 204 ? 4.8786 4.2779 3.1578 -1.5886 -0.6221 0.9367  204 PRO F N   
12975 C CA  . PRO F 204 ? 4.9167 4.2025 3.1841 -1.6205 -0.6359 0.8714  204 PRO F CA  
12976 C C   . PRO F 204 ? 4.8941 4.0449 3.2255 -1.5715 -0.6611 0.8560  204 PRO F C   
12977 O O   . PRO F 204 ? 4.8791 3.9991 3.2841 -1.5186 -0.6560 0.8736  204 PRO F O   
12978 C CB  . PRO F 204 ? 4.9700 4.2426 3.2463 -1.6497 -0.6023 0.8297  204 PRO F CB  
12979 C CG  . PRO F 204 ? 4.9916 4.4133 3.2359 -1.6643 -0.5756 0.8707  204 PRO F CG  
12980 C CD  . PRO F 204 ? 4.9747 4.4555 3.2446 -1.6092 -0.5839 0.9396  204 PRO F CD  
12981 N N   . VAL F 205 ? 4.8668 3.9369 3.1691 -1.5895 -0.6867 0.8215  205 VAL F N   
12982 C CA  . VAL F 205 ? 4.8412 3.7913 3.1924 -1.5441 -0.7156 0.8083  205 VAL F CA  
12983 C C   . VAL F 205 ? 4.8677 3.6936 3.2347 -1.5556 -0.7137 0.7418  205 VAL F C   
12984 O O   . VAL F 205 ? 4.9044 3.7166 3.2115 -1.6086 -0.7064 0.7054  205 VAL F O   
12985 C CB  . VAL F 205 ? 4.8358 3.7896 3.1400 -1.5454 -0.7492 0.8295  205 VAL F CB  
12986 C CG1 . VAL F 205 ? 4.8287 3.6463 3.1667 -1.5108 -0.7786 0.8015  205 VAL F CG1 
12987 C CG2 . VAL F 205 ? 4.8188 3.8755 3.1273 -1.5159 -0.7545 0.8978  205 VAL F CG2 
12988 N N   . THR F 206 ? 4.4859 3.2238 2.9340 -1.5060 -0.7183 0.7251  206 THR F N   
12989 C CA  . THR F 206 ? 4.5173 3.1321 2.9917 -1.5029 -0.7204 0.6651  206 THR F CA  
12990 C C   . THR F 206 ? 4.5027 3.0219 3.0027 -1.4593 -0.7579 0.6582  206 THR F C   
12991 O O   . THR F 206 ? 4.4528 2.9740 3.0088 -1.4086 -0.7726 0.6874  206 THR F O   
12992 C CB  . THR F 206 ? 4.5066 3.0992 3.0574 -1.4812 -0.6942 0.6446  206 THR F CB  
12993 O OG1 . THR F 206 ? 4.5267 3.2033 3.0482 -1.5237 -0.6585 0.6480  206 THR F OG1 
12994 C CG2 . THR F 206 ? 4.5385 3.0069 3.1187 -1.4738 -0.6979 0.5833  206 THR F CG2 
12995 N N   . LYS F 207 ? 4.6860 3.1213 3.1433 -1.4784 -0.7712 0.6197  207 LYS F N   
12996 C CA  . LYS F 207 ? 4.6692 2.9978 3.1502 -1.4363 -0.8037 0.6025  207 LYS F CA  
12997 C C   . LYS F 207 ? 4.7109 2.9338 3.2181 -1.4317 -0.7951 0.5430  207 LYS F C   
12998 O O   . LYS F 207 ? 4.7455 2.9539 3.2044 -1.4795 -0.7726 0.5113  207 LYS F O   
12999 C CB  . LYS F 207 ? 4.6758 2.9911 3.0785 -1.4566 -0.8272 0.6127  207 LYS F CB  
13000 C CG  . LYS F 207 ? 4.6600 3.0759 3.0357 -1.4576 -0.8399 0.6715  207 LYS F CG  
13001 C CD  . LYS F 207 ? 4.6342 3.0443 3.0812 -1.3921 -0.8631 0.7036  207 LYS F CD  
13002 C CE  . LYS F 207 ? 4.6303 3.1334 3.0477 -1.3907 -0.8755 0.7626  207 LYS F CE  
13003 N NZ  . LYS F 207 ? 4.6669 3.1547 3.1490 -1.3285 -0.8977 0.7916  207 LYS F NZ  
13004 N N   . SER F 208 ? 4.6803 2.8323 3.2637 -1.3747 -0.8117 0.5269  208 SER F N   
13005 C CA  . SER F 208 ? 4.7012 2.7612 3.3203 -1.3629 -0.8031 0.4721  208 SER F CA  
13006 C C   . SER F 208 ? 4.6759 2.6432 3.3383 -1.3043 -0.8370 0.4548  208 SER F C   
13007 O O   . SER F 208 ? 4.6570 2.6361 3.3374 -1.2692 -0.8649 0.4854  208 SER F O   
13008 C CB  . SER F 208 ? 4.7076 2.8010 3.3974 -1.3567 -0.7737 0.4616  208 SER F CB  
13009 O OG  . SER F 208 ? 4.6934 2.8156 3.4617 -1.3072 -0.7837 0.4876  208 SER F OG  
13010 N N   . PHE F 209 ? 4.7378 2.6139 3.4152 -1.2935 -0.8335 0.4048  209 PHE F N   
13011 C CA  . PHE F 209 ? 4.7256 2.5187 3.4593 -1.2326 -0.8611 0.3804  209 PHE F CA  
13012 C C   . PHE F 209 ? 4.7624 2.5057 3.5521 -1.2204 -0.8416 0.3306  209 PHE F C   
13013 O O   . PHE F 209 ? 4.8017 2.5511 3.5662 -1.2636 -0.8088 0.3108  209 PHE F O   
13014 C CB  . PHE F 209 ? 4.7398 2.4527 3.4080 -1.2255 -0.8866 0.3730  209 PHE F CB  
13015 C CG  . PHE F 209 ? 4.8056 2.4554 3.4025 -1.2670 -0.8645 0.3385  209 PHE F CG  
13016 C CD1 . PHE F 209 ? 4.8308 2.3879 3.4508 -1.2425 -0.8601 0.2910  209 PHE F CD1 
13017 C CD2 . PHE F 209 ? 4.8249 2.5100 3.3320 -1.3309 -0.8462 0.3522  209 PHE F CD2 
13018 C CE1 . PHE F 209 ? 4.9125 2.4152 3.4690 -1.2753 -0.8334 0.2593  209 PHE F CE1 
13019 C CE2 . PHE F 209 ? 4.8703 2.4946 3.3117 -1.3718 -0.8219 0.3179  209 PHE F CE2 
13020 C CZ  . PHE F 209 ? 4.9234 2.4576 3.3906 -1.3409 -0.8132 0.2720  209 PHE F CZ  
13021 N N   . ASN F 210 ? 4.5872 2.2835 3.4533 -1.1613 -0.8623 0.3090  210 ASN F N   
13022 C CA  . ASN F 210 ? 4.6170 2.2563 3.5386 -1.1401 -0.8504 0.2580  210 ASN F CA  
13023 C C   . ASN F 210 ? 4.6525 2.1876 3.5410 -1.1150 -0.8698 0.2266  210 ASN F C   
13024 O O   . ASN F 210 ? 4.6294 2.1343 3.5176 -1.0745 -0.9050 0.2367  210 ASN F O   
13025 C CB  . ASN F 210 ? 4.5769 2.2409 3.6115 -1.0909 -0.8572 0.2504  210 ASN F CB  
13026 C CG  . ASN F 210 ? 4.5533 2.3105 3.6229 -1.1133 -0.8302 0.2786  210 ASN F CG  
13027 O OD1 . ASN F 210 ? 4.5912 2.3791 3.6370 -1.1582 -0.7957 0.2759  210 ASN F OD1 
13028 N ND2 . ASN F 210 ? 4.5192 2.3211 3.6436 -1.0815 -0.8438 0.3063  210 ASN F ND2 
13029 N N   . ARG F 211 ? 4.5294 2.0092 3.3875 -1.1384 -0.8451 0.1899  211 ARG F N   
13030 C CA  . ARG F 211 ? 4.5871 1.9816 3.4142 -1.1064 -0.8511 0.1596  211 ARG F CA  
13031 C C   . ARG F 211 ? 4.6422 2.0027 3.5484 -1.0294 -0.8825 0.1403  211 ARG F C   
13032 O O   . ARG F 211 ? 4.6257 1.9979 3.6196 -1.0056 -0.8800 0.1172  211 ARG F O   
13033 C CB  . ARG F 211 ? 4.6680 2.0252 3.4731 -1.1329 -0.8105 0.1197  211 ARG F CB  
13034 C CG  . ARG F 211 ? 4.7308 1.9977 3.5148 -1.0917 -0.8108 0.0864  211 ARG F CG  
13035 C CD  . ARG F 211 ? 4.8282 2.0566 3.5974 -1.1156 -0.7677 0.0465  211 ARG F CD  
13036 N NE  . ARG F 211 ? 4.8542 2.0998 3.7111 -1.1049 -0.7550 0.0190  211 ARG F NE  
13037 C CZ  . ARG F 211 ? 4.8908 2.0971 3.8204 -1.0456 -0.7670 -0.0128 211 ARG F CZ  
13038 N NH1 . ARG F 211 ? 4.9213 2.1490 3.9298 -1.0418 -0.7525 -0.0382 211 ARG F NH1 
13039 N NH2 . ARG F 211 ? 4.9228 2.0697 3.8450 -0.9901 -0.7930 -0.0197 211 ARG F NH2 
13040 N N   . GLY F 212 ? 4.3904 1.7111 3.2648 -0.9914 -0.9114 0.1487  212 GLY F N   
13041 C CA  . GLY F 212 ? 4.3686 1.6621 3.3092 -0.9181 -0.9451 0.1328  212 GLY F CA  
13042 C C   . GLY F 212 ? 4.3042 1.6423 3.2713 -0.8955 -0.9812 0.1687  212 GLY F C   
13043 O O   . GLY F 212 ? 4.2501 1.6532 3.2504 -0.9202 -0.9786 0.1935  212 GLY F O   
13044 N N   . GLN G 1   ? 1.8219 3.5239 2.0731 0.2563  0.0835  -0.2862 1   GLN G N   
13045 C CA  . GLN G 1   ? 1.7929 3.4588 2.0717 0.2592  0.1142  -0.2899 1   GLN G CA  
13046 C C   . GLN G 1   ? 1.7659 3.4624 2.1148 0.2325  0.0948  -0.2726 1   GLN G C   
13047 O O   . GLN G 1   ? 1.7947 3.4962 2.1737 0.2329  0.1029  -0.2786 1   GLN G O   
13048 C CB  . GLN G 1   ? 1.7854 3.3748 2.0590 0.2656  0.1522  -0.2863 1   GLN G CB  
13049 C CG  . GLN G 1   ? 1.8185 3.3692 2.0357 0.2790  0.1601  -0.2890 1   GLN G CG  
13050 C CD  . GLN G 1   ? 1.8127 3.3923 2.0452 0.2625  0.1328  -0.2717 1   GLN G CD  
13051 O OE1 . GLN G 1   ? 1.8311 3.4078 2.1092 0.2442  0.1300  -0.2554 1   GLN G OE1 
13052 N NE2 . GLN G 1   ? 1.7311 3.3334 1.9213 0.2697  0.1129  -0.2763 1   GLN G NE2 
13053 N N   . GLU G 2   ? 1.4057 3.1130 1.7718 0.2098  0.0701  -0.2516 2   GLU G N   
13054 C CA  . GLU G 2   ? 1.3787 3.0885 1.7969 0.1839  0.0553  -0.2316 2   GLU G CA  
13055 C C   . GLU G 2   ? 1.4246 3.1742 1.8467 0.1701  0.0214  -0.2281 2   GLU G C   
13056 O O   . GLU G 2   ? 1.4241 3.1859 1.8198 0.1609  -0.0007 -0.2211 2   GLU G O   
13057 C CB  . GLU G 2   ? 1.3147 3.0007 1.7355 0.1692  0.0506  -0.2128 2   GLU G CB  
13058 C CG  . GLU G 2   ? 1.2928 2.9368 1.7069 0.1826  0.0797  -0.2164 2   GLU G CG  
13059 C CD  . GLU G 2   ? 1.2364 2.8573 1.6649 0.1681  0.0754  -0.1987 2   GLU G CD  
13060 O OE1 . GLU G 2   ? 1.2083 2.8085 1.6101 0.1755  0.0836  -0.2000 2   GLU G OE1 
13061 O OE2 . GLU G 2   ? 1.2295 2.8513 1.6952 0.1501  0.0634  -0.1838 2   GLU G OE2 
13062 N N   . VAL G 3   ? 1.0703 2.8329 1.5266 0.1680  0.0192  -0.2324 3   VAL G N   
13063 C CA  . VAL G 3   ? 1.1079 2.9016 1.5680 0.1571  -0.0131 -0.2319 3   VAL G CA  
13064 C C   . VAL G 3   ? 1.1274 2.9157 1.6423 0.1401  -0.0187 -0.2211 3   VAL G C   
13065 O O   . VAL G 3   ? 1.1110 2.8819 1.6616 0.1440  0.0058  -0.2223 3   VAL G O   
13066 C CB  . VAL G 3   ? 1.1047 2.9318 1.5366 0.1814  -0.0171 -0.2586 3   VAL G CB  
13067 C CG1 . VAL G 3   ? 1.0864 2.9202 1.4636 0.1991  -0.0160 -0.2690 3   VAL G CG1 
13068 C CG2 . VAL G 3   ? 1.1459 2.9088 1.5632 0.1974  0.0173  -0.2729 3   VAL G CG2 
13069 N N   . LEU G 4   ? 1.0124 2.8095 1.5341 0.1209  -0.0501 -0.2101 4   LEU G N   
13070 C CA  . LEU G 4   ? 1.0315 2.8256 1.6008 0.1043  -0.0616 -0.2005 4   LEU G CA  
13071 C C   . LEU G 4   ? 1.0424 2.8624 1.6045 0.1068  -0.0858 -0.2144 4   LEU G C   
13072 O O   . LEU G 4   ? 1.0389 2.8643 1.5660 0.1042  -0.1084 -0.2150 4   LEU G O   
13073 C CB  . LEU G 4   ? 1.0299 2.7995 1.6151 0.0778  -0.0769 -0.1721 4   LEU G CB  
13074 C CG  . LEU G 4   ? 0.9848 2.7273 1.5814 0.0736  -0.0604 -0.1577 4   LEU G CG  
13075 C CD1 . LEU G 4   ? 0.9800 2.7051 1.5757 0.0523  -0.0770 -0.1344 4   LEU G CD1 
13076 C CD2 . LEU G 4   ? 0.9777 2.7084 1.6272 0.0749  -0.0438 -0.1571 4   LEU G CD2 
13077 N N   . VAL G 5   ? 1.0008 2.8332 1.5972 0.1123  -0.0810 -0.2268 5   VAL G N   
13078 C CA  . VAL G 5   ? 1.0470 2.8523 1.6129 0.1132  -0.1023 -0.2388 5   VAL G CA  
13079 C C   . VAL G 5   ? 1.0782 2.9016 1.7049 0.0901  -0.1228 -0.2254 5   VAL G C   
13080 O O   . VAL G 5   ? 1.0922 2.9001 1.7628 0.0856  -0.1039 -0.2198 5   VAL G O   
13081 C CB  . VAL G 5   ? 1.1004 2.8073 1.5997 0.1355  -0.0719 -0.2597 5   VAL G CB  
13082 C CG1 . VAL G 5   ? 1.1658 2.8220 1.6162 0.1359  -0.0959 -0.2713 5   VAL G CG1 
13083 C CG2 . VAL G 5   ? 1.0768 2.7643 1.5180 0.1586  -0.0480 -0.2714 5   VAL G CG2 
13084 N N   . GLN G 6   ? 1.0080 2.8460 1.6318 0.0750  -0.1593 -0.2188 6   GLN G N   
13085 C CA  . GLN G 6   ? 1.0087 2.8320 1.6721 0.0508  -0.1773 -0.2010 6   GLN G CA  
13086 C C   . GLN G 6   ? 1.0411 2.8592 1.7001 0.0529  -0.1979 -0.2184 6   GLN G C   
13087 O O   . GLN G 6   ? 1.0943 2.8637 1.6840 0.0687  -0.2008 -0.2366 6   GLN G O   
13088 C CB  . GLN G 6   ? 1.0104 2.8100 1.6630 0.0302  -0.1948 -0.1759 6   GLN G CB  
13089 C CG  . GLN G 6   ? 0.9908 2.7735 1.6393 0.0255  -0.1760 -0.1574 6   GLN G CG  
13090 C CD  . GLN G 6   ? 0.9929 2.7565 1.6383 0.0064  -0.1908 -0.1357 6   GLN G CD  
13091 O OE1 . GLN G 6   ? 0.9898 2.7485 1.6056 0.0080  -0.1852 -0.1313 6   GLN G OE1 
13092 N NE2 . GLN G 6   ? 0.9985 2.7525 1.6770 -0.0111 -0.2083 -0.1230 6   GLN G NE2 
13093 N N   . SER G 7   ? 1.0018 2.8207 1.7118 0.0357  -0.2075 -0.2083 7   SER G N   
13094 C CA  . SER G 7   ? 1.0768 2.8414 1.7661 0.0336  -0.2222 -0.2183 7   SER G CA  
13095 C C   . SER G 7   ? 1.0885 2.8788 1.7603 0.0258  -0.2635 -0.2201 7   SER G C   
13096 O O   . SER G 7   ? 1.0638 2.8725 1.7349 0.0166  -0.2729 -0.2043 7   SER G O   
13097 C CB  . SER G 7   ? 1.1182 2.8852 1.8746 0.0154  -0.2240 -0.2051 7   SER G CB  
13098 O OG  . SER G 7   ? 1.1230 2.9271 1.9251 -0.0071 -0.2400 -0.1776 7   SER G OG  
13099 N N   . GLY G 8   ? 1.2283 2.9600 1.8627 0.0292  -0.2777 -0.2343 8   GLY G N   
13100 C CA  . GLY G 8   ? 1.2458 2.9893 1.8592 0.0248  -0.3173 -0.2398 8   GLY G CA  
13101 C C   . GLY G 8   ? 1.2651 3.0551 1.9434 -0.0026 -0.3457 -0.2187 8   GLY G C   
13102 O O   . GLY G 8   ? 1.2881 3.0757 2.0155 -0.0184 -0.3336 -0.1978 8   GLY G O   
13103 N N   . ALA G 9   ? 1.3523 3.1248 2.0074 -0.0072 -0.3726 -0.2178 9   ALA G N   
13104 C CA  . ALA G 9   ? 1.4006 3.1557 2.0913 -0.0309 -0.3875 -0.1927 9   ALA G CA  
13105 C C   . ALA G 9   ? 1.4683 3.2223 2.2034 -0.0449 -0.3991 -0.1901 9   ALA G C   
13106 O O   . ALA G 9   ? 1.4799 3.2426 2.2090 -0.0359 -0.4084 -0.2147 9   ALA G O   
13107 C CB  . ALA G 9   ? 1.4083 3.1473 2.0723 -0.0304 -0.4162 -0.1983 9   ALA G CB  
13108 N N   . GLU G 10  ? 1.2364 2.9792 2.0156 -0.0661 -0.3991 -0.1620 10  GLU G N   
13109 C CA  . GLU G 10  ? 1.3085 3.0479 2.1349 -0.0813 -0.4092 -0.1549 10  GLU G CA  
13110 C C   . GLU G 10  ? 1.3772 3.0991 2.2309 -0.1004 -0.4300 -0.1354 10  GLU G C   
13111 O O   . GLU G 10  ? 1.3672 3.0816 2.2180 -0.1051 -0.4257 -0.1199 10  GLU G O   
13112 C CB  . GLU G 10  ? 1.3121 3.0557 2.1756 -0.0863 -0.3828 -0.1398 10  GLU G CB  
13113 C CG  . GLU G 10  ? 1.2463 3.0102 2.0975 -0.0677 -0.3590 -0.1593 10  GLU G CG  
13114 C CD  . GLU G 10  ? 1.2609 3.0302 2.1642 -0.0733 -0.3450 -0.1553 10  GLU G CD  
13115 O OE1 . GLU G 10  ? 1.3229 3.0839 2.2647 -0.0892 -0.3608 -0.1467 10  GLU G OE1 
13116 O OE2 . GLU G 10  ? 1.2050 2.9861 2.1144 -0.0617 -0.3175 -0.1610 10  GLU G OE2 
13117 N N   . VAL G 11  ? 1.3378 3.0552 2.2200 -0.1109 -0.4520 -0.1384 11  VAL G N   
13118 C CA  . VAL G 11  ? 1.4020 3.1051 2.3219 -0.1298 -0.4706 -0.1201 11  VAL G CA  
13119 C C   . VAL G 11  ? 1.4621 3.1632 2.4322 -0.1433 -0.4668 -0.1073 11  VAL G C   
13120 O O   . VAL G 11  ? 1.4664 3.1761 2.4452 -0.1403 -0.4675 -0.1213 11  VAL G O   
13121 C CB  . VAL G 11  ? 1.4449 3.1402 2.3552 -0.1307 -0.5054 -0.1354 11  VAL G CB  
13122 C CG1 . VAL G 11  ? 1.5536 3.2372 2.5128 -0.1504 -0.5237 -0.1181 11  VAL G CG1 
13123 C CG2 . VAL G 11  ? 1.4072 3.0996 2.2738 -0.1186 -0.5114 -0.1449 11  VAL G CG2 
13124 N N   . LYS G 12  ? 1.5646 3.2550 2.5680 -0.1571 -0.4630 -0.0834 12  LYS G N   
13125 C CA  . LYS G 12  ? 1.6285 3.3126 2.6813 -0.1705 -0.4634 -0.0704 12  LYS G CA  
13126 C C   . LYS G 12  ? 1.7110 3.3835 2.7948 -0.1855 -0.4786 -0.0564 12  LYS G C   
13127 O O   . LYS G 12  ? 1.7418 3.4130 2.8123 -0.1858 -0.4802 -0.0524 12  LYS G O   
13128 C CB  . LYS G 12  ? 1.6143 3.2976 2.6761 -0.1685 -0.4361 -0.0581 12  LYS G CB  
13129 C CG  . LYS G 12  ? 1.5229 3.2203 2.5715 -0.1549 -0.4188 -0.0724 12  LYS G CG  
13130 C CD  . LYS G 12  ? 1.5294 3.2342 2.6098 -0.1583 -0.4279 -0.0842 12  LYS G CD  
13131 C CE  . LYS G 12  ? 1.4773 3.2002 2.5551 -0.1442 -0.4050 -0.1004 12  LYS G CE  
13132 N NZ  . LYS G 12  ? 1.4734 3.2078 2.5856 -0.1466 -0.4107 -0.1173 12  LYS G NZ  
13133 N N   . LYS G 13  ? 1.5969 3.2633 2.7250 -0.1977 -0.4890 -0.0508 13  LYS G N   
13134 C CA  . LYS G 13  ? 1.6623 3.3209 2.8248 -0.2114 -0.5008 -0.0402 13  LYS G CA  
13135 C C   . LYS G 13  ? 1.6551 3.3100 2.8295 -0.2163 -0.4814 -0.0234 13  LYS G C   
13136 O O   . LYS G 13  ? 1.5998 3.2536 2.7697 -0.2115 -0.4636 -0.0189 13  LYS G O   
13137 C CB  . LYS G 13  ? 1.6955 3.3499 2.8984 -0.2215 -0.5216 -0.0449 13  LYS G CB  
13138 C CG  . LYS G 13  ? 1.6960 3.3484 2.9292 -0.2252 -0.5117 -0.0402 13  LYS G CG  
13139 C CD  . LYS G 13  ? 1.7568 3.4078 3.0244 -0.2336 -0.5327 -0.0488 13  LYS G CD  
13140 C CE  . LYS G 13  ? 1.7526 3.4017 3.0593 -0.2386 -0.5227 -0.0438 13  LYS G CE  
13141 N NZ  . LYS G 13  ? 1.7706 3.4220 3.1065 -0.2456 -0.5403 -0.0547 13  LYS G NZ  
13142 N N   . PRO G 14  ? 1.4839 3.1388 2.6731 -0.2259 -0.4848 -0.0149 14  PRO G N   
13143 C CA  . PRO G 14  ? 1.4511 3.1051 2.6458 -0.2318 -0.4684 0.0003  14  PRO G CA  
13144 C C   . PRO G 14  ? 1.4614 3.1082 2.6865 -0.2368 -0.4666 0.0046  14  PRO G C   
13145 O O   . PRO G 14  ? 1.5089 3.1532 2.7657 -0.2422 -0.4811 -0.0017 14  PRO G O   
13146 C CB  . PRO G 14  ? 1.4841 3.1450 2.6949 -0.2433 -0.4763 0.0056  14  PRO G CB  
13147 C CG  . PRO G 14  ? 1.5020 3.1669 2.7037 -0.2387 -0.4905 -0.0063 14  PRO G CG  
13148 C CD  . PRO G 14  ? 1.5263 3.1849 2.7238 -0.2309 -0.5025 -0.0196 14  PRO G CD  
13149 N N   . GLY G 15  ? 1.4123 3.0558 2.6285 -0.2349 -0.4493 0.0148  15  GLY G N   
13150 C CA  . GLY G 15  ? 1.4141 3.0504 2.6595 -0.2389 -0.4469 0.0193  15  GLY G CA  
13151 C C   . GLY G 15  ? 1.3744 3.0067 2.6251 -0.2287 -0.4396 0.0121  15  GLY G C   
13152 O O   . GLY G 15  ? 1.3543 2.9804 2.6269 -0.2295 -0.4331 0.0164  15  GLY G O   
13153 N N   . ALA G 16  ? 1.5278 3.1659 2.7598 -0.2194 -0.4402 0.0009  16  ALA G N   
13154 C CA  . ALA G 16  ? 1.4813 3.1226 2.7175 -0.2100 -0.4307 -0.0066 16  ALA G CA  
13155 C C   . ALA G 16  ? 1.4071 3.0489 2.6125 -0.1988 -0.4086 -0.0031 16  ALA G C   
13156 O O   . ALA G 16  ? 1.3837 3.0217 2.5667 -0.1995 -0.4020 0.0062  16  ALA G O   
13157 C CB  . ALA G 16  ? 1.4926 3.1454 2.7162 -0.2054 -0.4410 -0.0220 16  ALA G CB  
13158 N N   . SER G 17  ? 1.5206 3.1697 2.7258 -0.1883 -0.3958 -0.0114 17  SER G N   
13159 C CA  . SER G 17  ? 1.4461 3.0973 2.6247 -0.1762 -0.3739 -0.0111 17  SER G CA  
13160 C C   . SER G 17  ? 1.4199 3.0898 2.5643 -0.1624 -0.3653 -0.0286 17  SER G C   
13161 O O   . SER G 17  ? 1.4313 3.1138 2.5848 -0.1614 -0.3732 -0.0424 17  SER G O   
13162 C CB  . SER G 17  ? 1.3958 3.0393 2.6141 -0.1751 -0.3624 -0.0062 17  SER G CB  
13163 O OG  . SER G 17  ? 1.4206 3.0487 2.6662 -0.1867 -0.3720 0.0059  17  SER G OG  
13164 N N   . VAL G 18  ? 1.4333 3.1067 2.5360 -0.1512 -0.3493 -0.0304 18  VAL G N   
13165 C CA  . VAL G 18  ? 1.4023 3.0947 2.4670 -0.1353 -0.3384 -0.0498 18  VAL G CA  
13166 C C   . VAL G 18  ? 1.3148 3.0096 2.3740 -0.1229 -0.3119 -0.0511 18  VAL G C   
13167 O O   . VAL G 18  ? 1.2780 2.9576 2.3381 -0.1257 -0.3045 -0.0360 18  VAL G O   
13168 C CB  . VAL G 18  ? 1.4446 3.1400 2.4604 -0.1322 -0.3466 -0.0540 18  VAL G CB  
13169 C CG1 . VAL G 18  ? 1.3986 3.0829 2.3932 -0.1334 -0.3362 -0.0393 18  VAL G CG1 
13170 C CG2 . VAL G 18  ? 1.3843 3.1000 2.3606 -0.1149 -0.3409 -0.0786 18  VAL G CG2 
13171 N N   . LYS G 19  ? 1.2941 3.0088 2.3490 -0.1086 -0.2974 -0.0716 19  LYS G N   
13172 C CA  . LYS G 19  ? 1.2093 2.9287 2.2614 -0.0944 -0.2698 -0.0769 19  LYS G CA  
13173 C C   . LYS G 19  ? 1.1728 2.9112 2.1698 -0.0765 -0.2593 -0.0974 19  LYS G C   
13174 O O   . LYS G 19  ? 1.1602 2.9201 2.1441 -0.0674 -0.2633 -0.1213 19  LYS G O   
13175 C CB  . LYS G 19  ? 1.1683 2.8963 2.2740 -0.0905 -0.2552 -0.0862 19  LYS G CB  
13176 C CG  . LYS G 19  ? 1.0850 2.8134 2.1973 -0.0761 -0.2248 -0.0905 19  LYS G CG  
13177 C CD  . LYS G 19  ? 1.0553 2.7920 2.2278 -0.0706 -0.2053 -0.1031 19  LYS G CD  
13178 C CE  . LYS G 19  ? 1.0349 2.7453 2.2591 -0.0797 -0.2032 -0.0798 19  LYS G CE  
13179 N NZ  . LYS G 19  ? 0.9698 2.6815 2.2309 -0.0651 -0.1701 -0.0914 19  LYS G NZ  
13180 N N   . VAL G 20  ? 1.1461 2.8769 2.1110 -0.0706 -0.2468 -0.0904 20  VAL G N   
13181 C CA  . VAL G 20  ? 1.0979 2.8433 2.0090 -0.0541 -0.2374 -0.1068 20  VAL G CA  
13182 C C   . VAL G 20  ? 1.0192 2.7687 1.9318 -0.0386 -0.2068 -0.1137 20  VAL G C   
13183 O O   . VAL G 20  ? 0.9939 2.7250 1.9340 -0.0441 -0.1973 -0.0974 20  VAL G O   
13184 C CB  . VAL G 20  ? 1.1003 2.8329 1.9729 -0.0610 -0.2485 -0.0935 20  VAL G CB  
13185 C CG1 . VAL G 20  ? 1.0849 2.8252 1.9102 -0.0449 -0.2317 -0.1033 20  VAL G CG1 
13186 C CG2 . VAL G 20  ? 1.1548 2.8888 2.0175 -0.0697 -0.2764 -0.0959 20  VAL G CG2 
13187 N N   . SER G 21  ? 1.1122 2.8845 1.9965 -0.0182 -0.1922 -0.1390 21  SER G N   
13188 C CA  . SER G 21  ? 1.0401 2.8165 1.9296 -0.0012 -0.1595 -0.1486 21  SER G CA  
13189 C C   . SER G 21  ? 1.0056 2.7871 1.8370 0.0130  -0.1503 -0.1558 21  SER G C   
13190 O O   . SER G 21  ? 1.0205 2.8103 1.8084 0.0144  -0.1678 -0.1615 21  SER G O   
13191 C CB  . SER G 21  ? 1.0151 2.8057 1.9296 0.0148  -0.1392 -0.1760 21  SER G CB  
13192 O OG  . SER G 21  ? 1.0541 2.7991 1.8921 0.0281  -0.1416 -0.1953 21  SER G OG  
13193 N N   . CYS G 22  ? 1.1699 2.9424 2.0037 0.0229  -0.1235 -0.1545 22  CYS G N   
13194 C CA  . CYS G 22  ? 1.1324 2.9064 1.9159 0.0363  -0.1112 -0.1599 22  CYS G CA  
13195 C C   . CYS G 22  ? 1.0657 2.8379 1.8645 0.0552  -0.0744 -0.1726 22  CYS G C   
13196 O O   . CYS G 22  ? 1.0304 2.7795 1.8675 0.0490  -0.0629 -0.1589 22  CYS G O   
13197 C CB  . CYS G 22  ? 1.1434 2.8932 1.9092 0.0210  -0.1221 -0.1349 22  CYS G CB  
13198 S SG  . CYS G 22  ? 1.0750 2.8179 1.7920 0.0334  -0.1038 -0.1361 22  CYS G SG  
13199 N N   . ARG G 23  ? 1.0264 2.8191 1.7968 0.0794  -0.0552 -0.1992 23  ARG G N   
13200 C CA  . ARG G 23  ? 0.9818 2.7568 1.7593 0.1003  -0.0121 -0.2134 23  ARG G CA  
13201 C C   . ARG G 23  ? 0.9421 2.7165 1.6729 0.1133  0.0007  -0.2155 23  ARG G C   
13202 O O   . ARG G 23  ? 0.9523 2.7463 1.6322 0.1203  -0.0135 -0.2235 23  ARG G O   
13203 C CB  . ARG G 23  ? 1.0464 2.7281 1.7694 0.1161  0.0119  -0.2337 23  ARG G CB  
13204 C CG  . ARG G 23  ? 1.0276 2.6562 1.7416 0.1365  0.0620  -0.2457 23  ARG G CG  
13205 C CD  . ARG G 23  ? 1.0995 2.6322 1.7737 0.1490  0.0910  -0.2634 23  ARG G CD  
13206 N NE  . ARG G 23  ? 1.0852 2.5703 1.7586 0.1674  0.1421  -0.2736 23  ARG G NE  
13207 C CZ  . ARG G 23  ? 1.1307 2.5430 1.8095 0.1750  0.1781  -0.2843 23  ARG G CZ  
13208 N NH1 . ARG G 23  ? 1.1185 2.4918 1.8008 0.1915  0.2260  -0.2931 23  ARG G NH1 
13209 N NH2 . ARG G 23  ? 1.1923 2.5697 1.8743 0.1662  0.1675  -0.2866 23  ARG G NH2 
13210 N N   . ALA G 24  ? 1.0314 2.7746 1.7784 0.1158  0.0254  -0.2077 24  ALA G N   
13211 C CA  . ALA G 24  ? 1.0207 2.7484 1.7252 0.1253  0.0377  -0.2068 24  ALA G CA  
13212 C C   . ALA G 24  ? 1.0418 2.7573 1.7220 0.1550  0.0801  -0.2327 24  ALA G C   
13213 O O   . ALA G 24  ? 1.0541 2.7477 1.7668 0.1655  0.1130  -0.2440 24  ALA G O   
13214 C CB  . ALA G 24  ? 1.0046 2.6994 1.7386 0.1120  0.0392  -0.1847 24  ALA G CB  
13215 N N   . PHE G 25  ? 1.1474 2.8686 1.7666 0.1693  0.0821  -0.2424 25  PHE G N   
13216 C CA  . PHE G 25  ? 1.1520 2.8426 1.7300 0.1984  0.1248  -0.2647 25  PHE G CA  
13217 C C   . PHE G 25  ? 1.1174 2.7832 1.6605 0.2005  0.1287  -0.2560 25  PHE G C   
13218 O O   . PHE G 25  ? 1.1018 2.7903 1.6291 0.1868  0.0966  -0.2422 25  PHE G O   
13219 C CB  . PHE G 25  ? 1.2364 2.8697 1.7236 0.2098  0.1176  -0.2802 25  PHE G CB  
13220 C CG  . PHE G 25  ? 1.3018 2.8870 1.7845 0.2023  0.1089  -0.2837 25  PHE G CG  
13221 C CD1 . PHE G 25  ? 1.3536 2.8510 1.8101 0.2152  0.1467  -0.2973 25  PHE G CD1 
13222 C CD2 . PHE G 25  ? 1.3136 2.9401 1.8197 0.1821  0.0649  -0.2736 25  PHE G CD2 
13223 C CE1 . PHE G 25  ? 1.4155 2.8667 1.8670 0.2084  0.1397  -0.3013 25  PHE G CE1 
13224 C CE2 . PHE G 25  ? 1.3733 2.9550 1.8764 0.1752  0.0566  -0.2772 25  PHE G CE2 
13225 C CZ  . PHE G 25  ? 1.4324 2.9264 1.9073 0.1885  0.0936  -0.2914 25  PHE G CZ  
13226 N N   . GLY G 26  ? 1.3068 2.9177 1.8359 0.2172  0.1701  -0.2645 26  GLY G N   
13227 C CA  . GLY G 26  ? 1.2716 2.8523 1.7630 0.2229  0.1777  -0.2601 26  GLY G CA  
13228 C C   . GLY G 26  ? 1.2245 2.7940 1.7563 0.2044  0.1672  -0.2373 26  GLY G C   
13229 O O   . GLY G 26  ? 1.1928 2.7428 1.6961 0.2070  0.1688  -0.2330 26  GLY G O   
13230 N N   . TYR G 27  ? 1.1533 2.7305 1.7481 0.1866  0.1564  -0.2232 27  TYR G N   
13231 C CA  . TYR G 27  ? 1.0918 2.6507 1.7231 0.1719  0.1491  -0.2036 27  TYR G CA  
13232 C C   . TYR G 27  ? 1.0877 2.6386 1.7933 0.1623  0.1541  -0.1956 27  TYR G C   
13233 O O   . TYR G 27  ? 1.1390 2.7013 1.8661 0.1651  0.1610  -0.2047 27  TYR G O   
13234 C CB  . TYR G 27  ? 1.0734 2.6593 1.6831 0.1541  0.1101  -0.1880 27  TYR G CB  
13235 C CG  . TYR G 27  ? 1.0739 2.6883 1.7096 0.1344  0.0797  -0.1758 27  TYR G CG  
13236 C CD1 . TYR G 27  ? 1.1338 2.7830 1.7484 0.1335  0.0631  -0.1829 27  TYR G CD1 
13237 C CD2 . TYR G 27  ? 1.0337 2.6364 1.7144 0.1169  0.0668  -0.1568 27  TYR G CD2 
13238 C CE1 . TYR G 27  ? 1.1494 2.8157 1.7877 0.1142  0.0358  -0.1700 27  TYR G CE1 
13239 C CE2 . TYR G 27  ? 1.0575 2.6768 1.7588 0.0989  0.0403  -0.1443 27  TYR G CE2 
13240 C CZ  . TYR G 27  ? 1.1096 2.7582 1.7895 0.0969  0.0256  -0.1502 27  TYR G CZ  
13241 O OH  . TYR G 27  ? 1.1384 2.7963 1.8390 0.0782  0.0001  -0.1365 27  TYR G OH  
13242 N N   . THR G 28  ? 1.2879 2.8195 2.0341 0.1514  0.1497  -0.1792 28  THR G N   
13243 C CA  . THR G 28  ? 1.2843 2.8061 2.1067 0.1426  0.1525  -0.1697 28  THR G CA  
13244 C C   . THR G 28  ? 1.2858 2.8391 2.1247 0.1217  0.1134  -0.1553 28  THR G C   
13245 O O   . THR G 28  ? 1.2642 2.8225 2.0883 0.1079  0.0864  -0.1404 28  THR G O   
13246 C CB  . THR G 28  ? 1.2712 2.7597 2.1317 0.1410  0.1618  -0.1582 28  THR G CB  
13247 O OG1 . THR G 28  ? 1.2847 2.7365 2.1295 0.1599  0.2003  -0.1702 28  THR G OG1 
13248 C CG2 . THR G 28  ? 1.2769 2.7573 2.2213 0.1328  0.1624  -0.1475 28  THR G CG2 
13249 N N   . PHE G 29  ? 1.0234 2.5926 1.8912 0.1197  0.1127  -0.1603 29  PHE G N   
13250 C CA  . PHE G 29  ? 1.0445 2.6387 1.9257 0.1000  0.0767  -0.1470 29  PHE G CA  
13251 C C   . PHE G 29  ? 1.0111 2.5907 1.9317 0.0826  0.0554  -0.1241 29  PHE G C   
13252 O O   . PHE G 29  ? 1.0152 2.6046 1.9175 0.0667  0.0248  -0.1102 29  PHE G O   
13253 C CB  . PHE G 29  ? 1.0928 2.6997 2.0128 0.1016  0.0840  -0.1567 29  PHE G CB  
13254 C CG  . PHE G 29  ? 1.1242 2.7497 2.0660 0.0806  0.0484  -0.1419 29  PHE G CG  
13255 C CD1 . PHE G 29  ? 1.1480 2.7949 2.0409 0.0705  0.0190  -0.1364 29  PHE G CD1 
13256 C CD2 . PHE G 29  ? 1.1371 2.7545 2.1497 0.0713  0.0453  -0.1330 29  PHE G CD2 
13257 C CE1 . PHE G 29  ? 1.1868 2.8420 2.0984 0.0512  -0.0112 -0.1221 29  PHE G CE1 
13258 C CE2 . PHE G 29  ? 1.1729 2.8016 2.2039 0.0520  0.0127  -0.1187 29  PHE G CE2 
13259 C CZ  . PHE G 29  ? 1.1994 2.8450 2.1783 0.0420  -0.0147 -0.1131 29  PHE G CZ  
13260 N N   . THR G 30  ? 1.2631 2.8167 2.2373 0.0864  0.0727  -0.1203 30  THR G N   
13261 C CA  . THR G 30  ? 1.2387 2.7789 2.2585 0.0720  0.0525  -0.1004 30  THR G CA  
13262 C C   . THR G 30  ? 1.1909 2.7205 2.1753 0.0693  0.0427  -0.0929 30  THR G C   
13263 O O   . THR G 30  ? 1.1859 2.7034 2.2046 0.0595  0.0271  -0.0787 30  THR G O   
13264 C CB  . THR G 30  ? 1.2373 2.7561 2.3369 0.0777  0.0738  -0.0988 30  THR G CB  
13265 O OG1 . THR G 30  ? 1.2178 2.7163 2.3085 0.0968  0.1111  -0.1118 30  THR G OG1 
13266 C CG2 . THR G 30  ? 1.2872 2.8170 2.4298 0.0767  0.0789  -0.1034 30  THR G CG2 
13267 N N   . GLY G 31  ? 1.2554 2.7894 2.1735 0.0782  0.0509  -0.1027 31  GLY G N   
13268 C CA  . GLY G 31  ? 1.2332 2.7566 2.1182 0.0773  0.0456  -0.0977 31  GLY G CA  
13269 C C   . GLY G 31  ? 1.2381 2.7760 2.0733 0.0641  0.0179  -0.0883 31  GLY G C   
13270 O O   . GLY G 31  ? 1.2379 2.7677 2.0465 0.0627  0.0137  -0.0841 31  GLY G O   
13271 N N   . ASN G 32  ? 1.1394 2.6973 1.9616 0.0546  0.0006  -0.0850 32  ASN G N   
13272 C CA  . ASN G 32  ? 1.1438 2.7127 1.9186 0.0428  -0.0207 -0.0762 32  ASN G CA  
13273 C C   . ASN G 32  ? 1.1829 2.7599 1.9812 0.0271  -0.0427 -0.0647 32  ASN G C   
13274 O O   . ASN G 32  ? 1.2247 2.8114 2.0465 0.0276  -0.0422 -0.0693 32  ASN G O   
13275 C CB  . ASN G 32  ? 1.1567 2.7431 1.8673 0.0506  -0.0162 -0.0877 32  ASN G CB  
13276 C CG  . ASN G 32  ? 1.1236 2.7010 1.8060 0.0665  0.0044  -0.0997 32  ASN G CG  
13277 O OD1 . ASN G 32  ? 1.1277 2.6987 1.8270 0.0804  0.0255  -0.1117 32  ASN G OD1 
13278 N ND2 . ASN G 32  ? 1.1161 2.6912 1.7556 0.0649  0.0001  -0.0966 32  ASN G ND2 
13279 N N   . ALA G 33  ? 1.0978 2.6711 1.8877 0.0135  -0.0612 -0.0505 33  ALA G N   
13280 C CA  . ALA G 33  ? 1.1482 2.7281 1.9501 -0.0018 -0.0822 -0.0394 33  ALA G CA  
13281 C C   . ALA G 33  ? 1.1774 2.7769 1.9404 -0.0019 -0.0845 -0.0455 33  ALA G C   
13282 O O   . ALA G 33  ? 1.1704 2.7790 1.8856 0.0068  -0.0751 -0.0550 33  ALA G O   
13283 C CB  . ALA G 33  ? 1.1479 2.7222 1.9379 -0.0144 -0.0978 -0.0250 33  ALA G CB  
13284 N N   . LEU G 34  ? 1.1780 2.7838 1.9642 -0.0117 -0.0987 -0.0405 34  LEU G N   
13285 C CA  . LEU G 34  ? 1.1725 2.7968 1.9315 -0.0119 -0.1030 -0.0471 34  LEU G CA  
13286 C C   . LEU G 34  ? 1.2039 2.8298 1.9617 -0.0291 -0.1240 -0.0334 34  LEU G C   
13287 O O   . LEU G 34  ? 1.2272 2.8445 2.0260 -0.0400 -0.1367 -0.0227 34  LEU G O   
13288 C CB  . LEU G 34  ? 1.1579 2.7917 1.9477 -0.0046 -0.0970 -0.0588 34  LEU G CB  
13289 C CG  . LEU G 34  ? 1.1520 2.8078 1.9117 -0.0016 -0.1014 -0.0697 34  LEU G CG  
13290 C CD1 . LEU G 34  ? 1.1293 2.7965 1.8435 0.0159  -0.0846 -0.0867 34  LEU G CD1 
13291 C CD2 . LEU G 34  ? 1.1549 2.8202 1.9549 -0.0015 -0.1041 -0.0762 34  LEU G CD2 
13292 N N   . HIS G 35  ? 1.1632 2.8003 1.8771 -0.0312 -0.1271 -0.0344 35  HIS G N   
13293 C CA  . HIS G 35  ? 1.1972 2.8375 1.9074 -0.0464 -0.1436 -0.0228 35  HIS G CA  
13294 C C   . HIS G 35  ? 1.1988 2.8510 1.9162 -0.0484 -0.1534 -0.0286 35  HIS G C   
13295 O O   . HIS G 35  ? 1.1730 2.8364 1.8792 -0.0365 -0.1465 -0.0437 35  HIS G O   
13296 C CB  . HIS G 35  ? 1.2102 2.8566 1.8743 -0.0480 -0.1400 -0.0203 35  HIS G CB  
13297 C CG  . HIS G 35  ? 1.2147 2.8522 1.8655 -0.0461 -0.1312 -0.0155 35  HIS G CG  
13298 N ND1 . HIS G 35  ? 1.2514 2.8838 1.9103 -0.0582 -0.1392 -0.0009 35  HIS G ND1 
13299 C CD2 . HIS G 35  ? 1.1924 2.8262 1.8217 -0.0336 -0.1160 -0.0239 35  HIS G CD2 
13300 C CE1 . HIS G 35  ? 1.2507 2.8773 1.8938 -0.0533 -0.1299 -0.0006 35  HIS G CE1 
13301 N NE2 . HIS G 35  ? 1.2146 2.8406 1.8408 -0.0385 -0.1158 -0.0143 35  HIS G NE2 
13302 N N   . TRP G 36  ? 1.1488 2.7997 1.8852 -0.0633 -0.1702 -0.0174 36  TRP G N   
13303 C CA  . TRP G 36  ? 1.1605 2.8221 1.8986 -0.0677 -0.1826 -0.0211 36  TRP G CA  
13304 C C   . TRP G 36  ? 1.1958 2.8618 1.9137 -0.0783 -0.1901 -0.0124 36  TRP G C   
13305 O O   . TRP G 36  ? 1.2290 2.8892 1.9558 -0.0898 -0.1947 0.0018  36  TRP G O   
13306 C CB  . TRP G 36  ? 1.1765 2.8334 1.9624 -0.0760 -0.1961 -0.0170 36  TRP G CB  
13307 C CG  . TRP G 36  ? 1.1472 2.8052 1.9581 -0.0653 -0.1875 -0.0278 36  TRP G CG  
13308 C CD1 . TRP G 36  ? 1.1383 2.7851 1.9792 -0.0620 -0.1788 -0.0253 36  TRP G CD1 
13309 C CD2 . TRP G 36  ? 1.1293 2.8030 1.9397 -0.0558 -0.1857 -0.0443 36  TRP G CD2 
13310 N NE1 . TRP G 36  ? 1.1161 2.7709 1.9784 -0.0512 -0.1689 -0.0387 36  TRP G NE1 
13311 C CE2 . TRP G 36  ? 1.1104 2.7834 1.9518 -0.0469 -0.1727 -0.0511 36  TRP G CE2 
13312 C CE3 . TRP G 36  ? 1.1324 2.8215 1.9207 -0.0535 -0.1945 -0.0549 36  TRP G CE3 
13313 C CZ2 . TRP G 36  ? 1.0952 2.7859 1.9439 -0.0354 -0.1654 -0.0693 36  TRP G CZ2 
13314 C CZ3 . TRP G 36  ? 1.1173 2.8229 1.9096 -0.0421 -0.1913 -0.0731 36  TRP G CZ3 
13315 C CH2 . TRP G 36  ? 1.0989 2.8071 1.9201 -0.0329 -0.1755 -0.0808 36  TRP G CH2 
13316 N N   . VAL G 37  ? 1.1847 2.8630 1.8776 -0.0741 -0.1913 -0.0215 37  VAL G N   
13317 C CA  . VAL G 37  ? 1.2185 2.9040 1.8946 -0.0821 -0.1957 -0.0158 37  VAL G CA  
13318 C C   . VAL G 37  ? 1.2340 2.9279 1.9191 -0.0844 -0.2108 -0.0225 37  VAL G C   
13319 O O   . VAL G 37  ? 1.2090 2.9085 1.8866 -0.0734 -0.2120 -0.0372 37  VAL G O   
13320 C CB  . VAL G 37  ? 1.2050 2.8965 1.8395 -0.0727 -0.1803 -0.0215 37  VAL G CB  
13321 C CG1 . VAL G 37  ? 1.2452 2.9472 1.8681 -0.0806 -0.1841 -0.0169 37  VAL G CG1 
13322 C CG2 . VAL G 37  ? 1.1937 2.8760 1.8198 -0.0704 -0.1671 -0.0155 37  VAL G CG2 
13323 N N   . ARG G 38  ? 1.2127 2.9089 1.9137 -0.0984 -0.2230 -0.0126 38  ARG G N   
13324 C CA  . ARG G 38  ? 1.2332 2.9356 1.9481 -0.1019 -0.2399 -0.0182 38  ARG G CA  
13325 C C   . ARG G 38  ? 1.2671 2.9801 1.9702 -0.1059 -0.2414 -0.0170 38  ARG G C   
13326 O O   . ARG G 38  ? 1.2864 3.0035 1.9769 -0.1102 -0.2307 -0.0084 38  ARG G O   
13327 C CB  . ARG G 38  ? 1.2651 2.9614 2.0208 -0.1155 -0.2562 -0.0091 38  ARG G CB  
13328 C CG  . ARG G 38  ? 1.3170 3.0147 2.0874 -0.1312 -0.2593 0.0072  38  ARG G CG  
13329 C CD  . ARG G 38  ? 1.3535 3.0460 2.1642 -0.1434 -0.2766 0.0137  38  ARG G CD  
13330 N NE  . ARG G 38  ? 1.4120 3.1100 2.2364 -0.1586 -0.2801 0.0284  38  ARG G NE  
13331 C CZ  . ARG G 38  ? 1.4567 3.1523 2.3154 -0.1711 -0.2940 0.0362  38  ARG G CZ  
13332 N NH1 . ARG G 38  ? 1.4491 3.1352 2.3332 -0.1701 -0.3063 0.0305  38  ARG G NH1 
13333 N NH2 . ARG G 38  ? 1.5144 3.2192 2.3817 -0.1848 -0.2951 0.0495  38  ARG G NH2 
13334 N N   . GLN G 39  ? 1.4047 3.1233 2.1139 -0.1043 -0.2559 -0.0265 39  GLN G N   
13335 C CA  . GLN G 39  ? 1.4414 3.1707 2.1468 -0.1067 -0.2599 -0.0281 39  GLN G CA  
13336 C C   . GLN G 39  ? 1.4805 3.2110 2.2193 -0.1152 -0.2835 -0.0294 39  GLN G C   
13337 O O   . GLN G 39  ? 1.4700 3.1978 2.2099 -0.1082 -0.2974 -0.0418 39  GLN G O   
13338 C CB  . GLN G 39  ? 1.4156 3.1502 2.0870 -0.0906 -0.2531 -0.0431 39  GLN G CB  
13339 C CG  . GLN G 39  ? 1.4522 3.1978 2.1206 -0.0914 -0.2556 -0.0455 39  GLN G CG  
13340 C CD  . GLN G 39  ? 1.4268 3.1766 2.0581 -0.0753 -0.2442 -0.0582 39  GLN G CD  
13341 O OE1 . GLN G 39  ? 1.3875 3.1340 1.9987 -0.0619 -0.2429 -0.0704 39  GLN G OE1 
13342 N NE2 . GLN G 39  ? 1.4546 3.2137 2.0773 -0.0763 -0.2356 -0.0560 39  GLN G NE2 
13343 N N   . ALA G 40  ? 1.5032 3.2391 2.2683 -0.1300 -0.2884 -0.0174 40  ALA G N   
13344 C CA  . ALA G 40  ? 1.5485 3.2865 2.3486 -0.1385 -0.3107 -0.0188 40  ALA G CA  
13345 C C   . ALA G 40  ? 1.5652 3.3112 2.3610 -0.1320 -0.3194 -0.0304 40  ALA G C   
13346 O O   . ALA G 40  ? 1.5575 3.3112 2.3293 -0.1255 -0.3055 -0.0327 40  ALA G O   
13347 C CB  . ALA G 40  ? 1.6046 3.3495 2.4348 -0.1559 -0.3115 -0.0032 40  ALA G CB  
13348 N N   . PRO G 41  ? 1.5144 3.2581 2.3341 -0.1332 -0.3438 -0.0383 41  PRO G N   
13349 C CA  . PRO G 41  ? 1.5332 3.2817 2.3497 -0.1256 -0.3562 -0.0507 41  PRO G CA  
13350 C C   . PRO G 41  ? 1.5767 3.3407 2.4063 -0.1318 -0.3480 -0.0445 41  PRO G C   
13351 O O   . PRO G 41  ? 1.6251 3.3977 2.4893 -0.1462 -0.3500 -0.0340 41  PRO G O   
13352 C CB  . PRO G 41  ? 1.5690 3.3107 2.4173 -0.1299 -0.3870 -0.0570 41  PRO G CB  
13353 C CG  . PRO G 41  ? 1.5790 3.3161 2.4537 -0.1426 -0.3882 -0.0458 41  PRO G CG  
13354 C CD  . PRO G 41  ? 1.5319 3.2669 2.3819 -0.1410 -0.3628 -0.0372 41  PRO G CD  
13355 N N   . GLY G 42  ? 1.6218 3.3912 2.4240 -0.1208 -0.3382 -0.0518 42  GLY G N   
13356 C CA  . GLY G 42  ? 1.6847 3.4707 2.4971 -0.1253 -0.3287 -0.0475 42  GLY G CA  
13357 C C   . GLY G 42  ? 1.6919 3.4872 2.4913 -0.1325 -0.3022 -0.0336 42  GLY G C   
13358 O O   . GLY G 42  ? 1.7285 3.5407 2.5360 -0.1374 -0.2926 -0.0294 42  GLY G O   
13359 N N   . GLN G 43  ? 1.8234 3.6088 2.6040 -0.1333 -0.2911 -0.0266 43  GLN G N   
13360 C CA  . GLN G 43  ? 1.8125 3.6041 2.5816 -0.1413 -0.2707 -0.0123 43  GLN G CA  
13361 C C   . GLN G 43  ? 1.7570 3.5422 2.4800 -0.1290 -0.2511 -0.0152 43  GLN G C   
13362 O O   . GLN G 43  ? 1.7101 3.4889 2.4106 -0.1144 -0.2513 -0.0284 43  GLN G O   
13363 C CB  . GLN G 43  ? 1.8456 3.6303 2.6357 -0.1533 -0.2762 -0.0007 43  GLN G CB  
13364 C CG  . GLN G 43  ? 1.9085 3.6979 2.7455 -0.1651 -0.2964 0.0014  43  GLN G CG  
13365 C CD  . GLN G 43  ? 2.0278 3.8394 2.8887 -0.1738 -0.2955 0.0043  43  GLN G CD  
13366 O OE1 . GLN G 43  ? 2.0928 3.9199 2.9449 -0.1807 -0.2782 0.0145  43  GLN G OE1 
13367 N NE2 . GLN G 43  ? 2.0724 3.8867 2.9659 -0.1739 -0.3149 -0.0046 43  GLN G NE2 
13368 N N   . GLY G 44  ? 1.6409 3.4287 2.3498 -0.1350 -0.2348 -0.0030 44  GLY G N   
13369 C CA  . GLY G 44  ? 1.5968 3.3785 2.2660 -0.1249 -0.2166 -0.0044 44  GLY G CA  
13370 C C   . GLY G 44  ? 1.5457 3.3091 2.2085 -0.1208 -0.2163 -0.0035 44  GLY G C   
13371 O O   . GLY G 44  ? 1.5346 3.2890 2.2194 -0.1222 -0.2308 -0.0056 44  GLY G O   
13372 N N   . LEU G 45  ? 1.5895 3.3481 2.2243 -0.1156 -0.2001 -0.0008 45  LEU G N   
13373 C CA  . LEU G 45  ? 1.5359 3.2779 2.1652 -0.1095 -0.1973 -0.0015 45  LEU G CA  
13374 C C   . LEU G 45  ? 1.5634 3.3015 2.2063 -0.1218 -0.1972 0.0146  45  LEU G C   
13375 O O   . LEU G 45  ? 1.6120 3.3605 2.2458 -0.1298 -0.1897 0.0249  45  LEU G O   
13376 C CB  . LEU G 45  ? 1.4904 3.2285 2.0833 -0.0945 -0.1809 -0.0103 45  LEU G CB  
13377 C CG  . LEU G 45  ? 1.4714 3.2139 2.0467 -0.0807 -0.1806 -0.0271 45  LEU G CG  
13378 C CD1 . LEU G 45  ? 1.4713 3.2139 2.0094 -0.0686 -0.1624 -0.0333 45  LEU G CD1 
13379 C CD2 . LEU G 45  ? 1.4505 3.1860 2.0354 -0.0728 -0.1914 -0.0379 45  LEU G CD2 
13380 N N   . GLU G 46  ? 1.3833 3.1081 2.0483 -0.1233 -0.2062 0.0164  46  GLU G N   
13381 C CA  . GLU G 46  ? 1.4066 3.1261 2.0901 -0.1347 -0.2100 0.0310  46  GLU G CA  
13382 C C   . GLU G 46  ? 1.3618 3.0638 2.0485 -0.1266 -0.2072 0.0284  46  GLU G C   
13383 O O   . GLU G 46  ? 1.3275 3.0216 2.0263 -0.1191 -0.2122 0.0187  46  GLU G O   
13384 C CB  . GLU G 46  ? 1.4481 3.1697 2.1680 -0.1478 -0.2272 0.0374  46  GLU G CB  
13385 C CG  . GLU G 46  ? 1.4836 3.2017 2.2234 -0.1606 -0.2328 0.0528  46  GLU G CG  
13386 C CD  . GLU G 46  ? 1.5337 3.2564 2.3080 -0.1741 -0.2488 0.0591  46  GLU G CD  
13387 O OE1 . GLU G 46  ? 1.5870 3.3160 2.3727 -0.1877 -0.2523 0.0737  46  GLU G OE1 
13388 O OE2 . GLU G 46  ? 1.5264 3.2473 2.3162 -0.1713 -0.2587 0.0493  46  GLU G OE2 
13389 N N   . TRP G 47  ? 1.2602 2.9582 1.9383 -0.1283 -0.1998 0.0370  47  TRP G N   
13390 C CA  . TRP G 47  ? 1.2237 2.9054 1.9102 -0.1210 -0.1970 0.0352  47  TRP G CA  
13391 C C   . TRP G 47  ? 1.2440 2.9161 1.9716 -0.1303 -0.2120 0.0434  47  TRP G C   
13392 O O   . TRP G 47  ? 1.2960 2.9727 2.0346 -0.1440 -0.2199 0.0568  47  TRP G O   
13393 C CB  . TRP G 47  ? 1.2292 2.9106 1.8925 -0.1194 -0.1857 0.0407  47  TRP G CB  
13394 C CG  . TRP G 47  ? 1.1950 2.8600 1.8677 -0.1105 -0.1816 0.0376  47  TRP G CG  
13395 C CD1 . TRP G 47  ? 1.1597 2.8180 1.8209 -0.0951 -0.1702 0.0245  47  TRP G CD1 
13396 C CD2 . TRP G 47  ? 1.2151 2.8696 1.9132 -0.1164 -0.1891 0.0476  47  TRP G CD2 
13397 N NE1 . TRP G 47  ? 1.1524 2.7965 1.8340 -0.0912 -0.1693 0.0256  47  TRP G NE1 
13398 C CE2 . TRP G 47  ? 1.1724 2.8131 1.8780 -0.1039 -0.1818 0.0395  47  TRP G CE2 
13399 C CE3 . TRP G 47  ? 1.2699 2.9265 1.9866 -0.1310 -0.2021 0.0625  47  TRP G CE3 
13400 C CZ2 . TRP G 47  ? 1.1821 2.8096 1.9176 -0.1054 -0.1881 0.0452  47  TRP G CZ2 
13401 C CZ3 . TRP G 47  ? 1.2803 2.9240 2.0223 -0.1323 -0.2093 0.0682  47  TRP G CZ3 
13402 C CH2 . TRP G 47  ? 1.2363 2.8649 1.9896 -0.1195 -0.2028 0.0592  47  TRP G CH2 
13403 N N   . LEU G 48  ? 1.2690 2.9301 2.0194 -0.1232 -0.2155 0.0350  48  LEU G N   
13404 C CA  . LEU G 48  ? 1.2889 2.9399 2.0822 -0.1305 -0.2292 0.0407  48  LEU G CA  
13405 C C   . LEU G 48  ? 1.2838 2.9213 2.0944 -0.1280 -0.2271 0.0448  48  LEU G C   
13406 O O   . LEU G 48  ? 1.3247 2.9563 2.1628 -0.1380 -0.2389 0.0554  48  LEU G O   
13407 C CB  . LEU G 48  ? 1.2626 2.9120 2.0763 -0.1249 -0.2346 0.0292  48  LEU G CB  
13408 C CG  . LEU G 48  ? 1.2675 2.9287 2.0705 -0.1258 -0.2405 0.0223  48  LEU G CG  
13409 C CD1 . LEU G 48  ? 1.2414 2.9025 2.0623 -0.1190 -0.2459 0.0099  48  LEU G CD1 
13410 C CD2 . LEU G 48  ? 1.3278 2.9940 2.1453 -0.1418 -0.2538 0.0338  48  LEU G CD2 
13411 N N   . GLY G 49  ? 1.2350 2.8679 2.0322 -0.1145 -0.2133 0.0360  49  GLY G N   
13412 C CA  . GLY G 49  ? 1.2275 2.8470 2.0468 -0.1106 -0.2113 0.0379  49  GLY G CA  
13413 C C   . GLY G 49  ? 1.1720 2.7887 1.9821 -0.0941 -0.1947 0.0242  49  GLY G C   
13414 O O   . GLY G 49  ? 1.1406 2.7667 1.9248 -0.0858 -0.1858 0.0134  49  GLY G O   
13415 N N   . TRP G 50  ? 1.2027 2.8071 2.0368 -0.0891 -0.1912 0.0244  50  TRP G N   
13416 C CA  . TRP G 50  ? 1.1548 2.7566 1.9874 -0.0734 -0.1741 0.0115  50  TRP G CA  
13417 C C   . TRP G 50  ? 1.1531 2.7414 2.0422 -0.0705 -0.1753 0.0111  50  TRP G C   
13418 O O   . TRP G 50  ? 1.1906 2.7695 2.1142 -0.0801 -0.1902 0.0210  50  TRP G O   
13419 C CB  . TRP G 50  ? 1.1410 2.7440 1.9297 -0.0661 -0.1607 0.0090  50  TRP G CB  
13420 C CG  . TRP G 50  ? 1.1677 2.7610 1.9626 -0.0702 -0.1645 0.0185  50  TRP G CG  
13421 C CD1 . TRP G 50  ? 1.2129 2.8004 2.0363 -0.0822 -0.1814 0.0309  50  TRP G CD1 
13422 C CD2 . TRP G 50  ? 1.1567 2.7466 1.9271 -0.0622 -0.1526 0.0154  50  TRP G CD2 
13423 N NE1 . TRP G 50  ? 1.2305 2.8126 2.0487 -0.0820 -0.1815 0.0356  50  TRP G NE1 
13424 C CE2 . TRP G 50  ? 1.1959 2.7788 1.9825 -0.0700 -0.1638 0.0264  50  TRP G CE2 
13425 C CE3 . TRP G 50  ? 1.1222 2.7146 1.8585 -0.0490 -0.1345 0.0040  50  TRP G CE3 
13426 C CZ2 . TRP G 50  ? 1.2002 2.7790 1.9711 -0.0653 -0.1576 0.0264  50  TRP G CZ2 
13427 C CZ3 . TRP G 50  ? 1.1266 2.7132 1.8476 -0.0445 -0.1275 0.0042  50  TRP G CZ3 
13428 C CH2 . TRP G 50  ? 1.1646 2.7447 1.9035 -0.0527 -0.1391 0.0153  50  TRP G CH2 
13429 N N   . ILE G 51  ? 1.1554 2.7440 2.0553 -0.0569 -0.1589 -0.0014 51  ILE G N   
13430 C CA  . ILE G 51  ? 1.1533 2.7317 2.1133 -0.0522 -0.1550 -0.0042 51  ILE G CA  
13431 C C   . ILE G 51  ? 1.1232 2.6961 2.0796 -0.0375 -0.1340 -0.0130 51  ILE G C   
13432 O O   . ILE G 51  ? 1.0938 2.6756 2.0035 -0.0275 -0.1190 -0.0227 51  ILE G O   
13433 C CB  . ILE G 51  ? 1.1458 2.7338 2.1350 -0.0505 -0.1532 -0.0117 51  ILE G CB  
13434 C CG1 . ILE G 51  ? 1.1476 2.7265 2.2054 -0.0455 -0.1456 -0.0147 51  ILE G CG1 
13435 C CG2 . ILE G 51  ? 1.1092 2.7153 2.0537 -0.0390 -0.1378 -0.0263 51  ILE G CG2 
13436 C CD1 . ILE G 51  ? 1.1550 2.7440 2.2495 -0.0470 -0.1464 -0.0198 51  ILE G CD1 
13437 N N   . ASN G 52  ? 1.1091 2.6666 2.1170 -0.0359 -0.1336 -0.0102 52  ASN G N   
13438 C CA  . ASN G 52  ? 1.0863 2.6362 2.1057 -0.0216 -0.1121 -0.0189 52  ASN G CA  
13439 C C   . ASN G 52  ? 1.0734 2.6267 2.1371 -0.0122 -0.0945 -0.0291 52  ASN G C   
13440 O O   . ASN G 52  ? 1.0971 2.6436 2.2256 -0.0170 -0.1011 -0.0247 52  ASN G O   
13441 C CB  . ASN G 52  ? 1.1116 2.6434 2.1691 -0.0244 -0.1207 -0.0112 52  ASN G CB  
13442 C CG  . ASN G 52  ? 1.0923 2.6141 2.1624 -0.0100 -0.0985 -0.0192 52  ASN G CG  
13443 O OD1 . ASN G 52  ? 1.0702 2.5938 2.1533 0.0022  -0.0750 -0.0299 52  ASN G OD1 
13444 N ND2 . ASN G 52  ? 1.1070 2.6183 2.1724 -0.0111 -0.1049 -0.0144 52  ASN G ND2 
13445 N N   . PRO G 53  A 1.0912 2.6553 2.1237 0.0016  -0.0713 -0.0438 52  PRO G N   
13446 C CA  . PRO G 53  A 1.0845 2.6551 2.1552 0.0114  -0.0514 -0.0556 52  PRO G CA  
13447 C C   . PRO G 53  A 1.0957 2.6483 2.2341 0.0189  -0.0337 -0.0558 52  PRO G C   
13448 O O   . PRO G 53  A 1.1067 2.6613 2.2960 0.0233  -0.0199 -0.0610 52  PRO G O   
13449 C CB  . PRO G 53  A 1.0550 2.6403 2.0657 0.0262  -0.0308 -0.0732 52  PRO G CB  
13450 C CG  . PRO G 53  A 1.0482 2.6403 1.9926 0.0188  -0.0489 -0.0672 52  PRO G CG  
13451 C CD  . PRO G 53  A 1.0674 2.6409 2.0262 0.0087  -0.0633 -0.0514 52  PRO G CD  
13452 N N   . HIS G 54  ? 1.1771 2.7124 2.3203 0.0207  -0.0330 -0.0502 53  HIS G N   
13453 C CA  . HIS G 54  ? 1.1933 2.7098 2.4064 0.0274  -0.0177 -0.0479 53  HIS G CA  
13454 C C   . HIS G 54  ? 1.2408 2.7509 2.5285 0.0147  -0.0395 -0.0337 53  HIS G C   
13455 O O   . HIS G 54  ? 1.2746 2.7833 2.6252 0.0184  -0.0258 -0.0323 53  HIS G O   
13456 C CB  . HIS G 54  ? 1.1907 2.6919 2.3868 0.0317  -0.0150 -0.0456 53  HIS G CB  
13457 C CG  . HIS G 54  ? 1.2441 2.7253 2.5156 0.0366  -0.0050 -0.0387 53  HIS G CG  
13458 N ND1 . HIS G 54  ? 1.2746 2.7490 2.5912 0.0504  0.0284  -0.0425 53  HIS G ND1 
13459 C CD2 . HIS G 54  ? 1.2903 2.7578 2.6001 0.0301  -0.0234 -0.0266 53  HIS G CD2 
13460 C CE1 . HIS G 54  ? 1.3065 2.7662 2.6860 0.0519  0.0302  -0.0273 53  HIS G CE1 
13461 N NE2 . HIS G 54  ? 1.3250 2.7801 2.7048 0.0393  -0.0029 -0.0189 53  HIS G NE2 
13462 N N   . SER G 55  ? 1.1743 2.6804 2.4543 0.0002  -0.0724 -0.0229 54  SER G N   
13463 C CA  . SER G 55  ? 1.2324 2.7291 2.5805 -0.0117 -0.0972 -0.0122 54  SER G CA  
13464 C C   . SER G 55  ? 1.2476 2.7555 2.6007 -0.0227 -0.1134 -0.0106 54  SER G C   
13465 O O   . SER G 55  ? 1.2988 2.8003 2.7215 -0.0290 -0.1252 -0.0060 54  SER G O   
13466 C CB  . SER G 55  ? 1.2584 2.7446 2.5931 -0.0204 -0.1246 -0.0062 54  SER G CB  
13467 O OG  . SER G 55  ? 1.2392 2.7366 2.4954 -0.0280 -0.1376 -0.0041 54  SER G OG  
13468 N N   . GLY G 56  ? 1.2078 2.7319 2.4925 -0.0251 -0.1148 -0.0141 55  GLY G N   
13469 C CA  . GLY G 56  ? 1.2279 2.7613 2.5117 -0.0372 -0.1338 -0.0106 55  GLY G CA  
13470 C C   . GLY G 56  ? 1.2597 2.7883 2.5186 -0.0520 -0.1650 -0.0006 55  GLY G C   
13471 O O   . GLY G 56  ? 1.2815 2.8167 2.5352 -0.0624 -0.1808 0.0030  55  GLY G O   
13472 N N   . ASP G 57  ? 1.1906 2.7091 2.4333 -0.0528 -0.1729 0.0037  56  ASP G N   
13473 C CA  . ASP G 57  ? 1.2285 2.7457 2.4418 -0.0657 -0.1986 0.0130  56  ASP G CA  
13474 C C   . ASP G 57  ? 1.2136 2.7457 2.3542 -0.0705 -0.1983 0.0166  56  ASP G C   
13475 O O   . ASP G 57  ? 1.1702 2.7119 2.2673 -0.0620 -0.1795 0.0103  56  ASP G O   
13476 C CB  . ASP G 57  ? 1.2433 2.7510 2.4464 -0.0641 -0.2037 0.0159  56  ASP G CB  
13477 C CG  . ASP G 57  ? 1.2812 2.7738 2.5611 -0.0619 -0.2128 0.0117  56  ASP G CG  
13478 O OD1 . ASP G 57  ? 1.3133 2.8030 2.6539 -0.0639 -0.2182 0.0066  56  ASP G OD1 
13479 O OD2 . ASP G 57  ? 1.3239 2.8084 2.6056 -0.0583 -0.2153 0.0115  56  ASP G OD2 
13480 N N   . THR G 58  ? 1.1732 2.7077 2.3031 -0.0840 -0.2193 0.0256  57  THR G N   
13481 C CA  . THR G 58  ? 1.1696 2.7176 2.2414 -0.0905 -0.2210 0.0301  57  THR G CA  
13482 C C   . THR G 58  ? 1.2162 2.7651 2.2587 -0.1018 -0.2365 0.0423  57  THR G C   
13483 O O   . THR G 58  ? 1.2633 2.8040 2.3367 -0.1078 -0.2529 0.0479  57  THR G O   
13484 C CB  . THR G 58  ? 1.1813 2.7358 2.2718 -0.0970 -0.2284 0.0293  57  THR G CB  
13485 O OG1 . THR G 58  ? 1.2386 2.7847 2.3758 -0.1072 -0.2491 0.0350  57  THR G OG1 
13486 C CG2 . THR G 58  ? 1.1420 2.7007 2.2584 -0.0861 -0.2115 0.0174  57  THR G CG2 
13487 N N   . THR G 59  ? 1.2185 2.7799 2.2018 -0.1043 -0.2307 0.0458  58  THR G N   
13488 C CA  . THR G 59  ? 1.2693 2.8385 2.2225 -0.1170 -0.2427 0.0587  58  THR G CA  
13489 C C   . THR G 59  ? 1.2671 2.8502 2.1898 -0.1227 -0.2408 0.0598  58  THR G C   
13490 O O   . THR G 59  ? 1.2253 2.8161 2.1139 -0.1151 -0.2259 0.0520  58  THR G O   
13491 C CB  . THR G 59  ? 1.2723 2.8450 2.1855 -0.1145 -0.2355 0.0621  58  THR G CB  
13492 O OG1 . THR G 59  ? 1.2767 2.8357 2.2232 -0.1089 -0.2392 0.0600  58  THR G OG1 
13493 C CG2 . THR G 59  ? 1.3325 2.9183 2.2156 -0.1288 -0.2458 0.0766  58  THR G CG2 
13494 N N   . THR G 60  ? 1.3481 2.9346 2.2846 -0.1358 -0.2567 0.0688  59  THR G N   
13495 C CA  . THR G 60  ? 1.3550 2.9536 2.2735 -0.1424 -0.2579 0.0700  59  THR G CA  
13496 C C   . THR G 60  ? 1.4032 3.0164 2.2858 -0.1541 -0.2606 0.0830  59  THR G C   
13497 O O   . THR G 60  ? 1.4648 3.0784 2.3514 -0.1626 -0.2704 0.0947  59  THR G O   
13498 C CB  . THR G 60  ? 1.3900 2.9838 2.3529 -0.1494 -0.2727 0.0704  59  THR G CB  
13499 O OG1 . THR G 60  ? 1.3629 2.9458 2.3650 -0.1394 -0.2692 0.0592  59  THR G OG1 
13500 C CG2 . THR G 60  ? 1.3895 2.9950 2.3377 -0.1544 -0.2739 0.0690  59  THR G CG2 
13501 N N   . SER G 61  ? 1.3523 2.9795 2.2007 -0.1544 -0.2518 0.0807  60  SER G N   
13502 C CA  . SER G 61  ? 1.4043 3.0495 2.2256 -0.1669 -0.2531 0.0930  60  SER G CA  
13503 C C   . SER G 61  ? 1.4712 3.1183 2.3207 -0.1823 -0.2710 0.1056  60  SER G C   
13504 O O   . SER G 61  ? 1.4721 3.1115 2.3542 -0.1838 -0.2804 0.1017  60  SER G O   
13505 C CB  . SER G 61  ? 1.3865 3.0456 2.1810 -0.1651 -0.2437 0.0866  60  SER G CB  
13506 O OG  . SER G 61  ? 1.4415 3.1210 2.2141 -0.1774 -0.2430 0.0983  60  SER G OG  
13507 N N   . GLN G 62  ? 1.4597 3.1185 2.2955 -0.1941 -0.2758 0.1212  61  GLN G N   
13508 C CA  . GLN G 62  ? 1.5299 3.1896 2.3917 -0.2087 -0.2937 0.1349  61  GLN G CA  
13509 C C   . GLN G 62  ? 1.5597 3.2293 2.4322 -0.2187 -0.2989 0.1377  61  GLN G C   
13510 O O   . GLN G 62  ? 1.6087 3.2743 2.5116 -0.2282 -0.3140 0.1446  61  GLN G O   
13511 C CB  . GLN G 62  ? 1.5955 3.2697 2.4345 -0.2201 -0.2974 0.1528  61  GLN G CB  
13512 C CG  . GLN G 62  ? 1.5798 3.2403 2.4219 -0.2120 -0.3000 0.1511  61  GLN G CG  
13513 C CD  . GLN G 62  ? 1.6166 3.2597 2.5024 -0.2148 -0.3200 0.1542  61  GLN G CD  
13514 O OE1 . GLN G 62  ? 1.7060 3.3564 2.5982 -0.2297 -0.3353 0.1705  61  GLN G OE1 
13515 N NE2 . GLN G 62  ? 1.5642 3.1857 2.4822 -0.2008 -0.3200 0.1389  61  GLN G NE2 
13516 N N   . LYS G 63  ? 1.4083 3.0910 2.2585 -0.2169 -0.2875 0.1320  62  LYS G N   
13517 C CA  . LYS G 63  ? 1.4286 3.1184 2.2951 -0.2240 -0.2932 0.1309  62  LYS G CA  
13518 C C   . LYS G 63  ? 1.3969 3.0672 2.3009 -0.2174 -0.3025 0.1188  62  LYS G C   
13519 O O   . LYS G 63  ? 1.4362 3.1077 2.3665 -0.2264 -0.3142 0.1214  62  LYS G O   
13520 C CB  . LYS G 63  ? 1.4046 3.1094 2.2443 -0.2201 -0.2801 0.1235  62  LYS G CB  
13521 C CG  . LYS G 63  ? 1.4248 3.1372 2.2836 -0.2263 -0.2868 0.1204  62  LYS G CG  
13522 C CD  . LYS G 63  ? 1.4056 3.1325 2.2413 -0.2214 -0.2754 0.1121  62  LYS G CD  
13523 C CE  . LYS G 63  ? 1.4187 3.1493 2.2791 -0.2249 -0.2847 0.1055  62  LYS G CE  
13524 N NZ  . LYS G 63  ? 1.4006 3.1433 2.2441 -0.2188 -0.2764 0.0955  62  LYS G NZ  
13525 N N   . PHE G 64  ? 1.4819 3.1361 2.3900 -0.2023 -0.2970 0.1058  63  PHE G N   
13526 C CA  . PHE G 64  ? 1.4491 3.0893 2.3904 -0.1953 -0.3028 0.0934  63  PHE G CA  
13527 C C   . PHE G 64  ? 1.4563 3.0800 2.4341 -0.1936 -0.3111 0.0936  63  PHE G C   
13528 O O   . PHE G 64  ? 1.4314 3.0453 2.4404 -0.1877 -0.3143 0.0832  63  PHE G O   
13529 C CB  . PHE G 64  ? 1.3733 3.0121 2.2955 -0.1798 -0.2895 0.0779  63  PHE G CB  
13530 C CG  . PHE G 64  ? 1.3687 3.0230 2.2595 -0.1801 -0.2829 0.0752  63  PHE G CG  
13531 C CD1 . PHE G 64  ? 1.3884 3.0489 2.2924 -0.1855 -0.2922 0.0720  63  PHE G CD1 
13532 C CD2 . PHE G 64  ? 1.3522 3.0154 2.2034 -0.1754 -0.2686 0.0756  63  PHE G CD2 
13533 C CE1 . PHE G 64  ? 1.3904 3.0651 2.2717 -0.1856 -0.2879 0.0686  63  PHE G CE1 
13534 C CE2 . PHE G 64  ? 1.3548 3.0330 2.1821 -0.1757 -0.2630 0.0723  63  PHE G CE2 
13535 C CZ  . PHE G 64  ? 1.3740 3.0578 2.2179 -0.1807 -0.2730 0.0688  63  PHE G CZ  
13536 N N   . GLN G 65  ? 1.4678 3.0898 2.4440 -0.1985 -0.3149 0.1046  64  GLN G N   
13537 C CA  . GLN G 65  ? 1.4794 3.0857 2.4932 -0.1959 -0.3239 0.1035  64  GLN G CA  
13538 C C   . GLN G 65  ? 1.5196 3.1203 2.5778 -0.2027 -0.3387 0.1025  64  GLN G C   
13539 O O   . GLN G 65  ? 1.5790 3.1886 2.6374 -0.2161 -0.3483 0.1124  64  GLN G O   
13540 C CB  . GLN G 65  ? 1.5310 3.1393 2.5335 -0.2028 -0.3302 0.1177  64  GLN G CB  
13541 C CG  . GLN G 65  ? 1.5528 3.1453 2.5970 -0.2001 -0.3420 0.1158  64  GLN G CG  
13542 C CD  . GLN G 65  ? 1.4806 3.0600 2.5411 -0.1832 -0.3309 0.0999  64  GLN G CD  
13543 O OE1 . GLN G 65  ? 1.4478 3.0298 2.4761 -0.1747 -0.3160 0.0963  64  GLN G OE1 
13544 N NE2 . GLN G 65  ? 1.4785 3.0456 2.5906 -0.1785 -0.3370 0.0902  64  GLN G NE2 
13545 N N   . GLY G 66  ? 1.4267 3.0144 2.5243 -0.1939 -0.3395 0.0903  65  GLY G N   
13546 C CA  . GLY G 66  ? 1.4652 3.0483 2.6082 -0.1992 -0.3521 0.0868  65  GLY G CA  
13547 C C   . GLY G 66  ? 1.4475 3.0359 2.5943 -0.1994 -0.3511 0.0789  65  GLY G C   
13548 O O   . GLY G 66  ? 1.4772 3.0625 2.6628 -0.2031 -0.3604 0.0740  65  GLY G O   
13549 N N   . ARG G 67  ? 1.4303 3.0275 2.5387 -0.1954 -0.3407 0.0765  66  ARG G N   
13550 C CA  . ARG G 67  ? 1.4137 3.0174 2.5212 -0.1947 -0.3413 0.0682  66  ARG G CA  
13551 C C   . ARG G 67  ? 1.3349 2.9400 2.4268 -0.1799 -0.3270 0.0553  66  ARG G C   
13552 O O   . ARG G 67  ? 1.3167 2.9238 2.4260 -0.1762 -0.3287 0.0452  66  ARG G O   
13553 C CB  . ARG G 67  ? 1.4473 3.0640 2.5249 -0.2045 -0.3441 0.0762  66  ARG G CB  
13554 C CG  . ARG G 67  ? 1.4613 3.0835 2.5526 -0.2088 -0.3533 0.0699  66  ARG G CG  
13555 C CD  . ARG G 67  ? 1.5110 3.1464 2.5863 -0.2210 -0.3578 0.0795  66  ARG G CD  
13556 N NE  . ARG G 67  ? 1.4782 3.1244 2.5116 -0.2164 -0.3454 0.0793  66  ARG G NE  
13557 C CZ  . ARG G 67  ? 1.4426 3.0948 2.4621 -0.2102 -0.3432 0.0685  66  ARG G CZ  
13558 N NH1 . ARG G 67  ? 1.4329 3.0817 2.4750 -0.2079 -0.3533 0.0577  66  ARG G NH1 
13559 N NH2 . ARG G 67  ? 1.4214 3.0839 2.4048 -0.2062 -0.3318 0.0681  66  ARG G NH2 
13560 N N   . VAL G 68  ? 1.3804 2.9867 2.4377 -0.1716 -0.3128 0.0555  67  VAL G N   
13561 C CA  . VAL G 68  ? 1.3102 2.9195 2.3487 -0.1569 -0.2971 0.0436  67  VAL G CA  
13562 C C   . VAL G 68  ? 1.2848 2.8838 2.3489 -0.1483 -0.2890 0.0407  67  VAL G C   
13563 O O   . VAL G 68  ? 1.3020 2.8931 2.3694 -0.1507 -0.2904 0.0484  67  VAL G O   
13564 C CB  . VAL G 68  ? 1.2835 2.9020 2.2677 -0.1528 -0.2857 0.0441  67  VAL G CB  
13565 C CG1 . VAL G 68  ? 1.2171 2.8387 2.1797 -0.1368 -0.2685 0.0316  67  VAL G CG1 
13566 C CG2 . VAL G 68  ? 1.3075 2.9372 2.2747 -0.1600 -0.2931 0.0446  67  VAL G CG2 
13567 N N   . TYR G 69  ? 1.1872 2.7885 2.2711 -0.1386 -0.2805 0.0292  68  TYR G N   
13568 C CA  . TYR G 69  ? 1.1671 2.7605 2.2864 -0.1301 -0.2708 0.0250  68  TYR G CA  
13569 C C   . TYR G 69  ? 1.1038 2.7067 2.2006 -0.1145 -0.2492 0.0130  68  TYR G C   
13570 O O   . TYR G 69  ? 1.0819 2.6995 2.1628 -0.1100 -0.2450 0.0033  68  TYR G O   
13571 C CB  . TYR G 69  ? 1.1998 2.7892 2.3820 -0.1344 -0.2795 0.0223  68  TYR G CB  
13572 C CG  . TYR G 69  ? 1.2698 2.8498 2.4778 -0.1483 -0.3001 0.0314  68  TYR G CG  
13573 C CD1 . TYR G 69  ? 1.3010 2.8691 2.5370 -0.1499 -0.3054 0.0351  68  TYR G CD1 
13574 C CD2 . TYR G 69  ? 1.3106 2.8954 2.5143 -0.1595 -0.3147 0.0349  68  TYR G CD2 
13575 C CE1 . TYR G 69  ? 1.3726 2.9364 2.6261 -0.1621 -0.3239 0.0420  68  TYR G CE1 
13576 C CE2 . TYR G 69  ? 1.3811 2.9603 2.6052 -0.1719 -0.3316 0.0427  68  TYR G CE2 
13577 C CZ  . TYR G 69  ? 1.4127 2.9826 2.6590 -0.1731 -0.3359 0.0464  68  TYR G CZ  
13578 O OH  . TYR G 69  ? 1.4898 3.0580 2.7507 -0.1855 -0.3526 0.0544  68  TYR G OH  
13579 N N   . MET G 70  ? 1.2451 2.8411 2.3404 -0.1059 -0.2361 0.0125  69  MET G N   
13580 C CA  . MET G 70  ? 1.1905 2.7950 2.2648 -0.0901 -0.2131 0.0005  69  MET G CA  
13581 C C   . MET G 70  ? 1.1832 2.7823 2.3141 -0.0822 -0.2007 -0.0048 69  MET G C   
13582 O O   . MET G 70  ? 1.2080 2.7909 2.3784 -0.0858 -0.2068 0.0024  69  MET G O   
13583 C CB  . MET G 70  ? 1.1704 2.7714 2.1962 -0.0855 -0.2051 0.0032  69  MET G CB  
13584 C CG  . MET G 70  ? 1.1739 2.7838 2.1438 -0.0906 -0.2108 0.0060  69  MET G CG  
13585 S SD  . MET G 70  ? 1.1731 2.7779 2.0978 -0.0903 -0.2051 0.0135  69  MET G SD  
13586 C CE  . MET G 70  ? 1.2347 2.8264 2.1928 -0.1056 -0.2249 0.0300  69  MET G CE  
13587 N N   . THR G 71  ? 1.2652 2.8795 2.4014 -0.0707 -0.1826 -0.0190 70  THR G N   
13588 C CA  . THR G 71  ? 1.2600 2.8730 2.4502 -0.0609 -0.1632 -0.0264 70  THR G CA  
13589 C C   . THR G 71  ? 1.2144 2.8416 2.3711 -0.0422 -0.1344 -0.0438 70  THR G C   
13590 O O   . THR G 71  ? 1.1899 2.8297 2.2848 -0.0377 -0.1332 -0.0508 70  THR G O   
13591 C CB  . THR G 71  ? 1.2903 2.9106 2.5366 -0.0659 -0.1669 -0.0293 70  THR G CB  
13592 O OG1 . THR G 71  ? 1.2805 2.9233 2.4928 -0.0649 -0.1683 -0.0407 70  THR G OG1 
13593 C CG2 . THR G 71  ? 1.3443 2.9475 2.6306 -0.0831 -0.1947 -0.0140 70  THR G CG2 
13594 N N   . ARG G 72  ? 1.0641 2.6881 2.2641 -0.0304 -0.1098 -0.0520 71  ARG G N   
13595 C CA  . ARG G 72  ? 1.0304 2.6655 2.2032 -0.0104 -0.0780 -0.0721 71  ARG G CA  
13596 C C   . ARG G 72  ? 1.0431 2.6802 2.2760 0.0010  -0.0492 -0.0865 71  ARG G C   
13597 O O   . ARG G 72  ? 1.0736 2.6974 2.3750 -0.0057 -0.0519 -0.0761 71  ARG G O   
13598 C CB  . ARG G 72  ? 1.0074 2.6273 2.1511 -0.0035 -0.0690 -0.0682 71  ARG G CB  
13599 C CG  . ARG G 72  ? 1.0283 2.6229 2.2228 -0.0103 -0.0766 -0.0519 71  ARG G CG  
13600 C CD  . ARG G 72  ? 1.0317 2.6158 2.2833 0.0029  -0.0471 -0.0587 71  ARG G CD  
13601 N NE  . ARG G 72  ? 1.0553 2.6167 2.3589 -0.0037 -0.0584 -0.0425 71  ARG G NE  
13602 C CZ  . ARG G 72  ? 1.0818 2.6325 2.4628 -0.0007 -0.0468 -0.0374 71  ARG G CZ  
13603 N NH1 . ARG G 72  ? 1.1063 2.6381 2.5328 -0.0070 -0.0621 -0.0217 71  ARG G NH1 
13604 N NH2 . ARG G 72  ? 1.0929 2.6525 2.5052 0.0092  -0.0193 -0.0482 71  ARG G NH2 
13605 N N   . ASP G 73  ? 1.1728 2.8252 2.3794 0.0193  -0.0201 -0.1123 72  ASP G N   
13606 C CA  . ASP G 73  ? 1.1897 2.8373 2.4418 0.0358  0.0197  -0.1342 72  ASP G CA  
13607 C C   . ASP G 73  ? 1.1676 2.8029 2.3847 0.0563  0.0534  -0.1475 72  ASP G C   
13608 O O   . ASP G 73  ? 1.1476 2.7976 2.3022 0.0689  0.0635  -0.1650 72  ASP G O   
13609 C CB  . ASP G 73  ? 1.2060 2.8772 2.4575 0.0411  0.0283  -0.1603 72  ASP G CB  
13610 C CG  . ASP G 73  ? 1.2629 2.8819 2.5469 0.0561  0.0728  -0.1812 72  ASP G CG  
13611 O OD1 . ASP G 73  ? 1.2667 2.8745 2.5889 0.0672  0.1031  -0.1854 72  ASP G OD1 
13612 O OD2 . ASP G 73  ? 1.3301 2.8982 2.5914 0.0562  0.0779  -0.1909 72  ASP G OD2 
13613 N N   . LYS G 74  ? 1.2549 2.8621 2.5128 0.0599  0.0692  -0.1380 73  LYS G N   
13614 C CA  . LYS G 74  ? 1.2394 2.8283 2.4649 0.0769  0.0977  -0.1458 73  LYS G CA  
13615 C C   . LYS G 74  ? 1.2558 2.8345 2.4665 0.1010  0.1466  -0.1787 73  LYS G C   
13616 O O   . LYS G 74  ? 1.2427 2.8147 2.3936 0.1162  0.1656  -0.1906 73  LYS G O   
13617 C CB  . LYS G 74  ? 1.2528 2.8134 2.5321 0.0746  0.1013  -0.1268 73  LYS G CB  
13618 C CG  . LYS G 74  ? 1.2417 2.8028 2.5214 0.0548  0.0581  -0.0988 73  LYS G CG  
13619 C CD  . LYS G 74  ? 1.2520 2.7876 2.5688 0.0570  0.0636  -0.0842 73  LYS G CD  
13620 C CE  . LYS G 74  ? 1.2945 2.8209 2.6987 0.0545  0.0682  -0.0700 73  LYS G CE  
13621 N NZ  . LYS G 74  ? 1.3048 2.8150 2.7415 0.0531  0.0615  -0.0480 73  LYS G NZ  
13622 N N   . SER G 75  ? 1.1350 2.7047 2.3969 0.1054  0.1696  -0.1956 74  SER G N   
13623 C CA  . SER G 75  ? 1.1786 2.7050 2.4182 0.1287  0.2233  -0.2270 74  SER G CA  
13624 C C   . SER G 75  ? 1.1889 2.6911 2.3149 0.1382  0.2227  -0.2388 74  SER G C   
13625 O O   . SER G 75  ? 1.2214 2.6737 2.2882 0.1586  0.2611  -0.2557 74  SER G O   
13626 C CB  . SER G 75  ? 1.2550 2.7225 2.5385 0.1263  0.2421  -0.2332 74  SER G CB  
13627 O OG  . SER G 75  ? 1.2737 2.7392 2.5322 0.1127  0.2103  -0.2291 74  SER G OG  
13628 N N   . ILE G 76  ? 1.1732 2.7077 2.2683 0.1238  0.1793  -0.2303 75  ILE G N   
13629 C CA  . ILE G 76  ? 1.1861 2.7000 2.1796 0.1312  0.1712  -0.2409 75  ILE G CA  
13630 C C   . ILE G 76  ? 1.1135 2.6984 2.0767 0.1273  0.1401  -0.2315 75  ILE G C   
13631 O O   . ILE G 76  ? 1.1176 2.7012 2.0088 0.1289  0.1211  -0.2366 75  ILE G O   
13632 C CB  . ILE G 76  ? 1.2301 2.7191 2.2058 0.1197  0.1474  -0.2417 75  ILE G CB  
13633 C CG1 . ILE G 76  ? 1.1912 2.7469 2.2419 0.0940  0.1032  -0.2193 75  ILE G CG1 
13634 C CG2 . ILE G 76  ? 1.3198 2.7208 2.2964 0.1291  0.1863  -0.2573 75  ILE G CG2 
13635 C CD1 . ILE G 76  ? 1.2258 2.7701 2.2596 0.0806  0.0731  -0.2178 75  ILE G CD1 
13636 N N   . ASN G 77  ? 1.0822 2.7275 2.0995 0.1223  0.1338  -0.2184 76  ASN G N   
13637 C CA  . ASN G 77  ? 1.0476 2.7041 2.0094 0.1159  0.1064  -0.2029 76  ASN G CA  
13638 C C   . ASN G 77  ? 1.0318 2.7229 1.9706 0.0977  0.0599  -0.1915 76  ASN G C   
13639 O O   . ASN G 77  ? 1.0146 2.7228 1.8934 0.0998  0.0445  -0.1932 76  ASN G O   
13640 C CB  . ASN G 77  ? 1.0464 2.6948 1.9408 0.1397  0.1340  -0.2224 76  ASN G CB  
13641 C CG  . ASN G 77  ? 1.0734 2.6722 1.9814 0.1571  0.1824  -0.2318 76  ASN G CG  
13642 O OD1 . ASN G 77  ? 1.0785 2.6534 2.0435 0.1488  0.1869  -0.2168 76  ASN G OD1 
13643 N ND2 . ASN G 77  ? 1.0992 2.6753 1.9514 0.1818  0.2188  -0.2559 76  ASN G ND2 
13644 N N   . THR G 78  ? 1.1036 2.8004 2.0908 0.0797  0.0379  -0.1797 77  THR G N   
13645 C CA  . THR G 78  ? 1.0950 2.8155 2.0635 0.0633  -0.0016 -0.1712 77  THR G CA  
13646 C C   . THR G 78  ? 1.1148 2.8180 2.1142 0.0381  -0.0322 -0.1404 77  THR G C   
13647 O O   . THR G 78  ? 1.1336 2.8190 2.1934 0.0323  -0.0268 -0.1309 77  THR G O   
13648 C CB  . THR G 78  ? 1.1351 2.8636 2.1155 0.0675  0.0015  -0.1910 77  THR G CB  
13649 O OG1 . THR G 78  ? 1.1887 2.8550 2.0898 0.0902  0.0299  -0.2132 77  THR G OG1 
13650 C CG2 . THR G 78  ? 1.1371 2.8966 2.1075 0.0494  -0.0421 -0.1822 77  THR G CG2 
13651 N N   . ALA G 79  ? 1.0425 2.7482 2.0009 0.0247  -0.0623 -0.1261 78  ALA G N   
13652 C CA  . ALA G 79  ? 1.0620 2.7506 2.0398 0.0024  -0.0904 -0.1002 78  ALA G CA  
13653 C C   . ALA G 79  ? 1.0849 2.7866 2.0627 -0.0102 -0.1159 -0.0985 78  ALA G C   
13654 O O   . ALA G 79  ? 1.0819 2.8055 2.0234 -0.0038 -0.1199 -0.1137 78  ALA G O   
13655 C CB  . ALA G 79  ? 1.0518 2.7265 1.9855 -0.0031 -0.1000 -0.0862 78  ALA G CB  
13656 N N   . PHE G 80  ? 0.9753 2.6624 1.9948 -0.0278 -0.1349 -0.0803 79  PHE G N   
13657 C CA  . PHE G 80  ? 1.0891 2.7824 2.1156 -0.0416 -0.1598 -0.0760 79  PHE G CA  
13658 C C   . PHE G 80  ? 1.1391 2.8131 2.1547 -0.0591 -0.1836 -0.0535 79  PHE G C   
13659 O O   . PHE G 80  ? 1.1307 2.7850 2.1612 -0.0641 -0.1840 -0.0395 79  PHE G O   
13660 C CB  . PHE G 80  ? 1.1757 2.8707 2.2688 -0.0464 -0.1598 -0.0779 79  PHE G CB  
13661 C CG  . PHE G 80  ? 1.1393 2.8536 2.2522 -0.0283 -0.1309 -0.1037 79  PHE G CG  
13662 C CD1 . PHE G 80  ? 1.1637 2.9058 2.2572 -0.0200 -0.1297 -0.1280 79  PHE G CD1 
13663 C CD2 . PHE G 80  ? 1.0852 2.7884 2.2397 -0.0187 -0.1039 -0.1065 79  PHE G CD2 
13664 C CE1 . PHE G 80  ? 1.1428 2.8862 2.2467 -0.0006 -0.0974 -0.1561 79  PHE G CE1 
13665 C CE2 . PHE G 80  ? 1.0566 2.7727 2.2323 -0.0002 -0.0702 -0.1340 79  PHE G CE2 
13666 C CZ  . PHE G 80  ? 1.0904 2.8125 2.2321 0.0095  -0.0645 -0.1587 79  PHE G CZ  
13667 N N   . LEU G 81  ? 0.9982 2.6786 1.9891 -0.0675 -0.2027 -0.0523 80  LEU G N   
13668 C CA  . LEU G 81  ? 1.0601 2.7254 2.0449 -0.0837 -0.2229 -0.0341 80  LEU G CA  
13669 C C   . LEU G 81  ? 1.1797 2.8457 2.1967 -0.0965 -0.2436 -0.0308 80  LEU G C   
13670 O O   . LEU G 81  ? 1.2047 2.8862 2.2091 -0.0946 -0.2505 -0.0427 80  LEU G O   
13671 C CB  . LEU G 81  ? 1.0086 2.6790 1.9351 -0.0817 -0.2245 -0.0354 80  LEU G CB  
13672 C CG  . LEU G 81  ? 1.0557 2.7147 1.9731 -0.0965 -0.2393 -0.0190 80  LEU G CG  
13673 C CD1 . LEU G 81  ? 1.0228 2.6670 1.9426 -0.0992 -0.2328 -0.0064 80  LEU G CD1 
13674 C CD2 . LEU G 81  ? 1.0247 2.6936 1.8955 -0.0946 -0.2418 -0.0237 80  LEU G CD2 
13675 N N   . ASP G 82  ? 0.9594 2.6087 2.0173 -0.1091 -0.2549 -0.0162 81  ASP G N   
13676 C CA  . ASP G 82  ? 1.0665 2.7132 2.1562 -0.1228 -0.2757 -0.0112 81  ASP G CA  
13677 C C   . ASP G 82  ? 1.1057 2.7425 2.1780 -0.1353 -0.2908 0.0023  81  ASP G C   
13678 O O   . ASP G 82  ? 1.1067 2.7312 2.1823 -0.1399 -0.2907 0.0136  81  ASP G O   
13679 C CB  . ASP G 82  ? 1.1243 2.7614 2.2780 -0.1275 -0.2777 -0.0069 81  ASP G CB  
13680 C CG  . ASP G 82  ? 1.1066 2.7583 2.2877 -0.1167 -0.2615 -0.0214 81  ASP G CG  
13681 O OD1 . ASP G 82  ? 1.1370 2.8059 2.3176 -0.1161 -0.2654 -0.0333 81  ASP G OD1 
13682 O OD2 . ASP G 82  ? 1.0619 2.7092 2.2667 -0.1085 -0.2442 -0.0225 81  ASP G OD2 
13683 N N   . VAL G 83  ? 1.0508 2.6951 2.1058 -0.1406 -0.3035 -0.0002 82  VAL G N   
13684 C CA  . VAL G 83  ? 1.0962 2.7353 2.1428 -0.1531 -0.3166 0.0110  82  VAL G CA  
13685 C C   . VAL G 83  ? 1.1880 2.8242 2.2748 -0.1652 -0.3360 0.0132  82  VAL G C   
13686 O O   . VAL G 83  ? 1.2073 2.8517 2.2996 -0.1645 -0.3445 0.0033  82  VAL G O   
13687 C CB  . VAL G 83  ? 1.0547 2.7040 2.0550 -0.1498 -0.3155 0.0065  82  VAL G CB  
13688 C CG1 . VAL G 83  ? 1.0961 2.7434 2.0913 -0.1624 -0.3238 0.0190  82  VAL G CG1 
13689 C CG2 . VAL G 83  ? 1.0027 2.6566 1.9637 -0.1359 -0.2955 0.0008  82  VAL G CG2 
13690 N N   . THR G 84  A 1.2674 2.8933 2.3806 -0.1761 -0.3437 0.0249  82  THR G N   
13691 C CA  . THR G 84  A 1.3446 2.9665 2.5005 -0.1874 -0.3606 0.0266  82  THR G CA  
13692 C C   . THR G 84  A 1.3943 3.0180 2.5437 -0.2001 -0.3724 0.0356  82  THR G C   
13693 O O   . THR G 84  A 1.3770 3.0050 2.4931 -0.2012 -0.3665 0.0424  82  THR G O   
13694 C CB  . THR G 84  A 1.3775 2.9885 2.5753 -0.1894 -0.3603 0.0304  82  THR G CB  
13695 O OG1 . THR G 84  A 1.3994 3.0045 2.5863 -0.1948 -0.3599 0.0427  82  THR G OG1 
13696 C CG2 . THR G 84  A 1.3242 2.9353 2.5313 -0.1764 -0.3446 0.0227  82  THR G CG2 
13697 N N   . ARG G 85  B 1.3654 2.9877 2.5494 -0.2102 -0.3880 0.0354  82  ARG G N   
13698 C CA  . ARG G 85  B 1.4252 3.0515 2.6122 -0.2236 -0.3993 0.0434  82  ARG G CA  
13699 C C   . ARG G 85  B 1.3963 3.0330 2.5489 -0.2226 -0.3978 0.0424  82  ARG G C   
13700 O O   . ARG G 85  B 1.4204 3.0638 2.5559 -0.2292 -0.3944 0.0527  82  ARG G O   
13701 C CB  . ARG G 85  B 1.4733 3.0969 2.6631 -0.2322 -0.3975 0.0584  82  ARG G CB  
13702 C CG  . ARG G 85  B 1.4886 3.1015 2.7121 -0.2315 -0.3988 0.0582  82  ARG G CG  
13703 C CD  . ARG G 85  B 1.5655 3.1775 2.7956 -0.2433 -0.4041 0.0737  82  ARG G CD  
13704 N NE  . ARG G 85  B 1.5677 3.1837 2.7603 -0.2436 -0.3954 0.0858  82  ARG G NE  
13705 C CZ  . ARG G 85  B 1.5343 3.1437 2.7180 -0.2363 -0.3874 0.0877  82  ARG G CZ  
13706 N NH1 . ARG G 85  B 1.5322 3.1308 2.7451 -0.2277 -0.3861 0.0780  82  ARG G NH1 
13707 N NH2 . ARG G 85  B 1.5419 3.1571 2.6899 -0.2379 -0.3805 0.0989  82  ARG G NH2 
13708 N N   . LEU G 86  C 1.4965 3.1368 2.6402 -0.2147 -0.4009 0.0295  82  LEU G N   
13709 C CA  . LEU G 86  C 1.4727 3.1221 2.5828 -0.2103 -0.3991 0.0252  82  LEU G CA  
13710 C C   . LEU G 86  C 1.5289 3.1854 2.6504 -0.2221 -0.4112 0.0291  82  LEU G C   
13711 O O   . LEU G 86  C 1.5869 3.2417 2.7425 -0.2319 -0.4256 0.0293  82  LEU G O   
13712 C CB  . LEU G 86  C 1.4323 3.0850 2.5308 -0.1994 -0.4031 0.0094  82  LEU G CB  
13713 C CG  . LEU G 86  C 1.3663 3.0195 2.4447 -0.1855 -0.3867 0.0032  82  LEU G CG  
13714 C CD1 . LEU G 86  C 1.3547 3.0157 2.4280 -0.1773 -0.3934 -0.0134 82  LEU G CD1 
13715 C CD2 . LEU G 86  C 1.3119 2.9691 2.3477 -0.1777 -0.3697 0.0055  82  LEU G CD2 
13716 N N   . THR G 87  ? 1.4687 3.1348 2.5634 -0.2213 -0.4043 0.0316  83  THR G N   
13717 C CA  . THR G 87  ? 1.5047 3.1815 2.6096 -0.2298 -0.4140 0.0321  83  THR G CA  
13718 C C   . THR G 87  ? 1.4552 3.1386 2.5324 -0.2199 -0.4123 0.0222  83  THR G C   
13719 O O   . THR G 87  ? 1.3924 3.0732 2.4386 -0.2071 -0.4020 0.0160  83  THR G O   
13720 C CB  . THR G 87  ? 1.5444 3.2317 2.6513 -0.2425 -0.4061 0.0484  83  THR G CB  
13721 O OG1 . THR G 87  ? 1.4934 3.1882 2.5635 -0.2372 -0.3885 0.0529  83  THR G OG1 
13722 C CG2 . THR G 87  ? 1.5862 3.2665 2.7095 -0.2502 -0.4053 0.0597  83  THR G CG2 
13723 N N   . SER G 88  ? 1.6725 3.3656 2.7634 -0.2259 -0.4226 0.0201  84  SER G N   
13724 C CA  . SER G 88  ? 1.6340 3.3335 2.7047 -0.2173 -0.4244 0.0102  84  SER G CA  
13725 C C   . SER G 88  ? 1.5682 3.2758 2.6029 -0.2119 -0.4022 0.0156  84  SER G C   
13726 O O   . SER G 88  ? 1.5254 3.2360 2.5354 -0.2012 -0.4000 0.0062  84  SER G O   
13727 C CB  . SER G 88  ? 1.7248 3.4337 2.8273 -0.2262 -0.4409 0.0074  84  SER G CB  
13728 O OG  . SER G 88  ? 1.7932 3.5151 2.9135 -0.2399 -0.4324 0.0213  84  SER G OG  
13729 N N   . ASP G 89  ? 1.6109 3.3227 2.6411 -0.2191 -0.3871 0.0303  85  ASP G N   
13730 C CA  . ASP G 89  ? 1.5505 3.2699 2.5451 -0.2144 -0.3664 0.0355  85  ASP G CA  
13731 C C   . ASP G 89  ? 1.4587 3.1674 2.4199 -0.1989 -0.3557 0.0281  85  ASP G C   
13732 O O   . ASP G 89  ? 1.4009 3.1151 2.3299 -0.1920 -0.3398 0.0281  85  ASP G O   
13733 C CB  . ASP G 89  ? 1.6036 3.3302 2.5998 -0.2267 -0.3557 0.0534  85  ASP G CB  
13734 C CG  . ASP G 89  ? 1.5853 3.3249 2.5483 -0.2251 -0.3364 0.0598  85  ASP G CG  
13735 O OD1 . ASP G 89  ? 1.6148 3.3677 2.5728 -0.2235 -0.3340 0.0548  85  ASP G OD1 
13736 O OD2 . ASP G 89  ? 1.5969 3.3339 2.5406 -0.2255 -0.3247 0.0693  85  ASP G OD2 
13737 N N   . ASP G 90  ? 1.4150 3.1108 2.3849 -0.1937 -0.3633 0.0215  86  ASP G N   
13738 C CA  . ASP G 90  ? 1.3465 3.0351 2.2907 -0.1797 -0.3523 0.0143  86  ASP G CA  
13739 C C   . ASP G 90  ? 1.3022 2.9938 2.2253 -0.1668 -0.3568 -0.0025 86  ASP G C   
13740 O O   . ASP G 90  ? 1.2481 2.9379 2.1475 -0.1543 -0.3468 -0.0106 86  ASP G O   
13741 C CB  . ASP G 90  ? 1.3853 3.0622 2.3537 -0.1813 -0.3567 0.0158  86  ASP G CB  
13742 C CG  . ASP G 90  ? 1.4275 3.1003 2.4133 -0.1925 -0.3529 0.0317  86  ASP G CG  
13743 O OD1 . ASP G 90  ? 1.3900 3.0659 2.3536 -0.1924 -0.3386 0.0401  86  ASP G OD1 
13744 O OD2 . ASP G 90  ? 1.4981 3.1655 2.5187 -0.2016 -0.3653 0.0355  86  ASP G OD2 
13745 N N   . THR G 91  ? 1.4361 3.1333 2.3683 -0.1694 -0.3725 -0.0086 87  THR G N   
13746 C CA  . THR G 91  ? 1.3986 3.0988 2.3085 -0.1572 -0.3800 -0.0249 87  THR G CA  
13747 C C   . THR G 91  ? 1.3137 3.0205 2.1844 -0.1466 -0.3610 -0.0275 87  THR G C   
13748 O O   . THR G 91  ? 1.3069 3.0203 2.1755 -0.1520 -0.3505 -0.0182 87  THR G O   
13749 C CB  . THR G 91  ? 1.4833 3.1863 2.4171 -0.1635 -0.4035 -0.0296 87  THR G CB  
13750 O OG1 . THR G 91  ? 1.5554 3.2513 2.5222 -0.1713 -0.4226 -0.0304 87  THR G OG1 
13751 C CG2 . THR G 91  ? 1.4422 3.1477 2.3498 -0.1506 -0.4132 -0.0461 87  THR G CG2 
13752 N N   . GLY G 92  ? 1.4183 3.1254 2.2577 -0.1315 -0.3563 -0.0410 88  GLY G N   
13753 C CA  . GLY G 92  ? 1.3860 3.0992 2.1876 -0.1200 -0.3389 -0.0456 88  GLY G CA  
13754 C C   . GLY G 92  ? 1.3327 3.0467 2.1039 -0.1038 -0.3300 -0.0594 88  GLY G C   
13755 O O   . GLY G 92  ? 1.3225 3.0347 2.1016 -0.1011 -0.3384 -0.0668 88  GLY G O   
13756 N N   . ILE G 93  ? 1.3450 3.0641 2.0819 -0.0927 -0.3122 -0.0636 89  ILE G N   
13757 C CA  . ILE G 93  ? 1.2963 3.0193 2.0020 -0.0759 -0.2991 -0.0769 89  ILE G CA  
13758 C C   . ILE G 93  ? 1.2636 2.9824 1.9692 -0.0765 -0.2765 -0.0664 89  ILE G C   
13759 O O   . ILE G 93  ? 1.2687 2.9850 1.9705 -0.0822 -0.2650 -0.0542 89  ILE G O   
13760 C CB  . ILE G 93  ? 1.2875 3.0180 1.9558 -0.0621 -0.2950 -0.0897 89  ILE G CB  
13761 C CG1 . ILE G 93  ? 1.3239 3.0553 1.9934 -0.0602 -0.3216 -0.1017 89  ILE G CG1 
13762 C CG2 . ILE G 93  ? 1.2404 2.9773 1.8762 -0.0440 -0.2784 -0.1034 89  ILE G CG2 
13763 C CD1 . ILE G 93  ? 1.3242 3.0608 1.9588 -0.0456 -0.3212 -0.1154 89  ILE G CD1 
13764 N N   . TYR G 94  ? 1.2856 3.0046 1.9971 -0.0704 -0.2710 -0.0719 90  TYR G N   
13765 C CA  . TYR G 94  ? 1.2591 2.9718 1.9775 -0.0702 -0.2523 -0.0632 90  TYR G CA  
13766 C C   . TYR G 94  ? 1.2154 2.9360 1.9022 -0.0518 -0.2331 -0.0768 90  TYR G C   
13767 O O   . TYR G 94  ? 1.1995 2.9317 1.8771 -0.0392 -0.2342 -0.0945 90  TYR G O   
13768 C CB  . TYR G 94  ? 1.2658 2.9728 2.0245 -0.0774 -0.2589 -0.0585 90  TYR G CB  
13769 C CG  . TYR G 94  ? 1.3123 3.0095 2.1043 -0.0960 -0.2743 -0.0423 90  TYR G CG  
13770 C CD1 . TYR G 94  ? 1.3497 3.0493 2.1521 -0.1034 -0.2951 -0.0442 90  TYR G CD1 
13771 C CD2 . TYR G 94  ? 1.3248 3.0105 2.1381 -0.1057 -0.2692 -0.0260 90  TYR G CD2 
13772 C CE1 . TYR G 94  ? 1.3971 3.0895 2.2315 -0.1199 -0.3079 -0.0303 90  TYR G CE1 
13773 C CE2 . TYR G 94  ? 1.3737 3.0531 2.2155 -0.1216 -0.2828 -0.0126 90  TYR G CE2 
13774 C CZ  . TYR G 94  ? 1.4093 3.0928 2.2619 -0.1287 -0.3009 -0.0148 90  TYR G CZ  
13775 O OH  . TYR G 94  ? 1.4625 3.1416 2.3448 -0.1442 -0.3132 -0.0024 90  TYR G OH  
13776 N N   . TYR G 95  ? 1.1380 2.8535 1.8080 -0.0497 -0.2157 -0.0698 91  TYR G N   
13777 C CA  . TYR G 95  ? 1.1007 2.8216 1.7426 -0.0330 -0.1959 -0.0810 91  TYR G CA  
13778 C C   . TYR G 95  ? 1.0826 2.7926 1.7449 -0.0334 -0.1819 -0.0732 91  TYR G C   
13779 O O   . TYR G 95  ? 1.0984 2.7950 1.7814 -0.0466 -0.1847 -0.0562 91  TYR G O   
13780 C CB  . TYR G 95  ? 1.1036 2.8258 1.7093 -0.0291 -0.1869 -0.0806 91  TYR G CB  
13781 C CG  . TYR G 95  ? 1.1277 2.8588 1.7167 -0.0281 -0.2001 -0.0879 91  TYR G CG  
13782 C CD1 . TYR G 95  ? 1.1194 2.8628 1.6831 -0.0120 -0.2024 -0.1078 91  TYR G CD1 
13783 C CD2 . TYR G 95  ? 1.1663 2.8941 1.7668 -0.0424 -0.2107 -0.0759 91  TYR G CD2 
13784 C CE1 . TYR G 95  ? 1.1475 2.8959 1.6992 -0.0107 -0.2176 -0.1147 91  TYR G CE1 
13785 C CE2 . TYR G 95  ? 1.1940 2.9288 1.7868 -0.0416 -0.2236 -0.0826 91  TYR G CE2 
13786 C CZ  . TYR G 95  ? 1.1847 2.9280 1.7537 -0.0259 -0.2281 -0.1016 91  TYR G CZ  
13787 O OH  . TYR G 95  ? 1.2197 2.9669 1.7840 -0.0248 -0.2440 -0.1085 91  TYR G OH  
13788 N N   . CYS G 96  ? 1.0356 2.7523 1.6939 -0.0182 -0.1673 -0.0866 92  CYS G N   
13789 C CA  . CYS G 96  ? 1.0172 2.7226 1.6869 -0.0144 -0.1499 -0.0820 92  CYS G CA  
13790 C C   . CYS G 96  ? 1.0019 2.7085 1.6291 -0.0030 -0.1345 -0.0877 92  CYS G C   
13791 O O   . CYS G 96  ? 0.9959 2.7174 1.5903 0.0092  -0.1322 -0.1027 92  CYS G O   
13792 C CB  . CYS G 96  ? 0.9993 2.7107 1.6981 -0.0042 -0.1399 -0.0935 92  CYS G CB  
13793 S SG  . CYS G 96  ? 0.9797 2.7187 1.6486 0.0191  -0.1300 -0.1227 92  CYS G SG  
13794 N N   . ALA G 97  ? 1.1337 2.8246 1.7614 -0.0065 -0.1257 -0.0765 93  ALA G N   
13795 C CA  . ALA G 97  ? 1.1248 2.8147 1.7131 0.0023  -0.1123 -0.0803 93  ALA G CA  
13796 C C   . ALA G 97  ? 1.1138 2.7872 1.7155 0.0054  -0.0990 -0.0757 93  ALA G C   
13797 O O   . ALA G 97  ? 1.1430 2.8024 1.7712 -0.0065 -0.1049 -0.0608 93  ALA G O   
13798 C CB  . ALA G 97  ? 1.1518 2.8414 1.7173 -0.0084 -0.1199 -0.0702 93  ALA G CB  
13799 N N   . ARG G 98  ? 1.1964 2.8713 1.7808 0.0218  -0.0819 -0.0890 94  ARG G N   
13800 C CA  . ARG G 98  ? 1.2333 2.8905 1.8314 0.0266  -0.0683 -0.0865 94  ARG G CA  
13801 C C   . ARG G 98  ? 1.2889 2.9363 1.8595 0.0214  -0.0680 -0.0773 94  ARG G C   
13802 O O   . ARG G 98  ? 1.2929 2.9494 1.8219 0.0235  -0.0679 -0.0809 94  ARG G O   
13803 C CB  . ARG G 98  ? 1.2122 2.8730 1.8007 0.0466  -0.0485 -0.1047 94  ARG G CB  
13804 C CG  . ARG G 98  ? 1.2492 2.8883 1.8585 0.0523  -0.0332 -0.1031 94  ARG G CG  
13805 C CD  . ARG G 98  ? 1.2381 2.8776 1.8299 0.0727  -0.0112 -0.1212 94  ARG G CD  
13806 N NE  . ARG G 98  ? 1.2527 2.8952 1.7899 0.0788  -0.0096 -0.1258 94  ARG G NE  
13807 C CZ  . ARG G 98  ? 1.2505 2.8923 1.7605 0.0964  0.0066  -0.1407 94  ARG G CZ  
13808 N NH1 . ARG G 98  ? 1.2360 2.8721 1.7667 0.1106  0.0260  -0.1530 94  ARG G NH1 
13809 N NH2 . ARG G 98  ? 1.2690 2.9134 1.7316 0.1003  0.0050  -0.1436 94  ARG G NH2 
13810 N N   . ASP G 99  ? 1.2212 2.8513 1.8173 0.0152  -0.0683 -0.0661 95  ASP G N   
13811 C CA  . ASP G 99  ? 1.2785 2.9003 1.8509 0.0121  -0.0664 -0.0592 95  ASP G CA  
13812 C C   . ASP G 99  ? 1.2980 2.9082 1.8633 0.0261  -0.0498 -0.0683 95  ASP G C   
13813 O O   . ASP G 99  ? 1.2896 2.8900 1.8899 0.0334  -0.0413 -0.0731 95  ASP G O   
13814 C CB  . ASP G 99  ? 1.3258 2.9377 1.9280 -0.0027 -0.0787 -0.0423 95  ASP G CB  
13815 C CG  . ASP G 99  ? 1.3837 2.9978 1.9532 -0.0099 -0.0811 -0.0339 95  ASP G CG  
13816 O OD1 . ASP G 99  ? 1.4202 3.0275 1.9712 -0.0030 -0.0715 -0.0373 95  ASP G OD1 
13817 O OD2 . ASP G 99  ? 1.3954 3.0185 1.9593 -0.0224 -0.0918 -0.0242 95  ASP G OD2 
13818 N N   . LYS G 100 ? 1.3473 2.9581 1.8697 0.0298  -0.0444 -0.0708 96  LYS G N   
13819 C CA  . LYS G 100 ? 1.3747 2.9714 1.8895 0.0413  -0.0306 -0.0775 96  LYS G CA  
13820 C C   . LYS G 100 ? 1.4175 2.9955 1.9769 0.0372  -0.0315 -0.0688 96  LYS G C   
13821 O O   . LYS G 100 ? 1.4248 2.9880 2.0069 0.0472  -0.0192 -0.0751 96  LYS G O   
13822 C CB  . LYS G 100 ? 1.4105 3.0109 1.8749 0.0424  -0.0285 -0.0787 96  LYS G CB  
13823 C CG  . LYS G 100 ? 1.3750 2.9935 1.7991 0.0481  -0.0278 -0.0886 96  LYS G CG  
13824 C CD  . LYS G 100 ? 1.4185 3.0415 1.7994 0.0468  -0.0270 -0.0879 96  LYS G CD  
13825 C CE  . LYS G 100 ? 1.4514 3.0595 1.8157 0.0576  -0.0162 -0.0945 96  LYS G CE  
13826 N NZ  . LYS G 100 ? 1.4144 3.0232 1.7622 0.0741  -0.0074 -0.1103 96  LYS G NZ  
13827 N N   . TYR G 101 ? 1.2977 2.8761 1.8723 0.0227  -0.0458 -0.0546 97  TYR G N   
13828 C CA  . TYR G 101 ? 1.3387 2.9028 1.9627 0.0172  -0.0521 -0.0455 97  TYR G CA  
13829 C C   . TYR G 101 ? 1.3881 2.9373 2.0136 0.0242  -0.0436 -0.0479 97  TYR G C   
13830 O O   . TYR G 101 ? 1.4092 2.9434 2.0840 0.0262  -0.0426 -0.0465 97  TYR G O   
13831 C CB  . TYR G 101 ? 1.3016 2.8602 1.9806 0.0192  -0.0514 -0.0475 97  TYR G CB  
13832 C CG  . TYR G 101 ? 1.3379 2.8885 2.0699 0.0078  -0.0671 -0.0348 97  TYR G CG  
13833 C CD1 . TYR G 101 ? 1.3609 2.9194 2.0862 -0.0071 -0.0855 -0.0222 97  TYR G CD1 
13834 C CD2 . TYR G 101 ? 1.3527 2.8879 2.1446 0.0121  -0.0633 -0.0356 97  TYR G CD2 
13835 C CE1 . TYR G 101 ? 1.3984 2.9497 2.1707 -0.0172 -0.1019 -0.0112 97  TYR G CE1 
13836 C CE2 . TYR G 101 ? 1.3909 2.9190 2.2345 0.0019  -0.0804 -0.0246 97  TYR G CE2 
13837 C CZ  . TYR G 101 ? 1.4138 2.9499 2.2452 -0.0126 -0.1007 -0.0127 97  TYR G CZ  
13838 O OH  . TYR G 101 ? 1.4555 2.9845 2.3362 -0.0224 -0.1197 -0.0027 97  TYR G OH  
13839 N N   . TYR G 102 ? 1.4680 3.0208 2.0433 0.0280  -0.0376 -0.0519 98  TYR G N   
13840 C CA  . TYR G 102 ? 1.5188 3.0587 2.0930 0.0327  -0.0323 -0.0529 98  TYR G CA  
13841 C C   . TYR G 102 ? 1.5774 3.1138 2.1847 0.0218  -0.0465 -0.0402 98  TYR G C   
13842 O O   . TYR G 102 ? 1.5982 3.1481 2.1973 0.0093  -0.0597 -0.0298 98  TYR G O   
13843 C CB  . TYR G 102 ? 1.5384 3.0870 2.0516 0.0353  -0.0273 -0.0571 98  TYR G CB  
13844 C CG  . TYR G 102 ? 1.4948 3.0447 1.9733 0.0474  -0.0153 -0.0705 98  TYR G CG  
13845 C CD1 . TYR G 102 ? 1.4456 2.9879 1.9458 0.0579  -0.0055 -0.0799 98  TYR G CD1 
13846 C CD2 . TYR G 102 ? 1.5092 3.0701 1.9340 0.0488  -0.0136 -0.0743 98  TYR G CD2 
13847 C CE1 . TYR G 102 ? 1.4115 2.9576 1.8778 0.0696  0.0042  -0.0926 98  TYR G CE1 
13848 C CE2 . TYR G 102 ? 1.4755 3.0385 1.8696 0.0601  -0.0055 -0.0867 98  TYR G CE2 
13849 C CZ  . TYR G 102 ? 1.4269 2.9833 1.8403 0.0706  0.0026  -0.0959 98  TYR G CZ  
13850 O OH  . TYR G 102 ? 1.3980 2.9591 1.7788 0.0825  0.0094  -0.1086 98  TYR G OH  
13851 N N   . GLY G 103 ? 1.5238 3.0461 2.1690 0.0268  -0.0439 -0.0415 99  GLY G N   
13852 C CA  . GLY G 103 ? 1.5855 3.1090 2.2654 0.0177  -0.0597 -0.0308 99  GLY G CA  
13853 C C   . GLY G 103 ? 1.5763 3.0945 2.3041 0.0081  -0.0750 -0.0218 99  GLY G C   
13854 O O   . GLY G 103 ? 1.6266 3.1492 2.3734 -0.0021 -0.0929 -0.0114 99  GLY G O   
13855 N N   . ASN G 104 ? 1.3194 2.8369 2.0640 0.0113  -0.0691 -0.0263 100 ASN G N   
13856 C CA  . ASN G 104 ? 1.3039 2.8231 2.0910 0.0025  -0.0829 -0.0191 100 ASN G CA  
13857 C C   . ASN G 104 ? 1.3214 2.8557 2.0803 -0.0122 -0.1001 -0.0076 100 ASN G C   
13858 O O   . ASN G 104 ? 1.3408 2.8741 2.1348 -0.0224 -0.1181 0.0020  100 ASN G O   
13859 C CB  . ASN G 104 ? 1.3445 2.8477 2.2053 0.0019  -0.0916 -0.0154 100 ASN G CB  
13860 C CG  . ASN G 104 ? 1.3317 2.8195 2.2281 0.0160  -0.0716 -0.0256 100 ASN G CG  
13861 O OD1 . ASN G 104 ? 1.2765 2.7644 2.1773 0.0239  -0.0552 -0.0336 100 ASN G OD1 
13862 N ND2 . ASN G 104 ? 1.3844 2.8595 2.3074 0.0196  -0.0719 -0.0253 100 ASN G ND2 
13863 N N   . GLU G 105 A 1.3679 2.9164 2.0653 -0.0131 -0.0941 -0.0089 100 GLU G N   
13864 C CA  . GLU G 105 A 1.3810 2.9459 2.0504 -0.0264 -0.1055 0.0015  100 GLU G CA  
13865 C C   . GLU G 105 A 1.3284 2.9066 1.9530 -0.0239 -0.0956 -0.0046 100 GLU G C   
13866 O O   . GLU G 105 A 1.2963 2.8724 1.8998 -0.0118 -0.0808 -0.0168 100 GLU G O   
13867 C CB  . GLU G 105 A 1.4552 3.0277 2.0986 -0.0329 -0.1108 0.0094  100 GLU G CB  
13868 C CG  . GLU G 105 A 1.4678 3.0487 2.0631 -0.0241 -0.0949 0.0013  100 GLU G CG  
13869 C CD  . GLU G 105 A 1.5451 3.1418 2.1149 -0.0312 -0.0997 0.0094  100 GLU G CD  
13870 O OE1 . GLU G 105 A 1.5633 3.1700 2.0919 -0.0255 -0.0877 0.0035  100 GLU G OE1 
13871 O OE2 . GLU G 105 A 1.5880 3.1870 2.1788 -0.0426 -0.1160 0.0214  100 GLU G OE2 
13872 N N   . ALA G 106 B 1.4182 3.0103 2.0298 -0.0357 -0.1048 0.0038  100 ALA G N   
13873 C CA  . ALA G 106 B 1.3715 2.9772 1.9483 -0.0346 -0.0985 -0.0015 100 ALA G CA  
13874 C C   . ALA G 106 B 1.3947 3.0082 1.9208 -0.0286 -0.0860 -0.0075 100 ALA G C   
13875 O O   . ALA G 106 B 1.4586 3.0779 1.9667 -0.0337 -0.0865 -0.0010 100 ALA G O   
13876 C CB  . ALA G 106 B 1.3716 2.9902 1.9504 -0.0496 -0.1113 0.0100  100 ALA G CB  
13877 N N   . VAL G 107 C 1.4493 3.0646 1.9529 -0.0176 -0.0752 -0.0203 100 VAL G N   
13878 C CA  . VAL G 107 C 1.4666 3.0879 1.9237 -0.0105 -0.0640 -0.0278 100 VAL G CA  
13879 C C   . VAL G 107 C 1.4249 3.0611 1.8575 -0.0097 -0.0627 -0.0336 100 VAL G C   
13880 O O   . VAL G 107 C 1.4553 3.1047 1.8578 -0.0135 -0.0607 -0.0320 100 VAL G O   
13881 C CB  . VAL G 107 C 1.4609 3.0673 1.9146 0.0046  -0.0522 -0.0396 100 VAL G CB  
13882 C CG1 . VAL G 107 C 1.4751 3.0871 1.8806 0.0120  -0.0424 -0.0479 100 VAL G CG1 
13883 C CG2 . VAL G 107 C 1.5106 3.1026 1.9932 0.0034  -0.0545 -0.0339 100 VAL G CG2 
13884 N N   . GLY G 108 D 1.5213 3.1570 1.9693 -0.0045 -0.0640 -0.0407 100 GLY G N   
13885 C CA  . GLY G 108 D 1.4792 3.1298 1.9101 -0.0036 -0.0656 -0.0468 100 GLY G CA  
13886 C C   . GLY G 108 D 1.4087 3.0591 1.8595 0.0037  -0.0670 -0.0559 100 GLY G C   
13887 O O   . GLY G 108 D 1.3917 3.0312 1.8607 0.0122  -0.0613 -0.0612 100 GLY G O   
13888 N N   . MET G 109 E 1.3040 2.9682 1.7533 0.0005  -0.0745 -0.0581 100 MET G N   
13889 C CA  . MET G 109 E 1.2767 2.9459 1.7438 0.0061  -0.0785 -0.0668 100 MET G CA  
13890 C C   . MET G 109 E 1.2640 2.9443 1.6982 0.0217  -0.0708 -0.0840 100 MET G C   
13891 O O   . MET G 109 E 1.2809 2.9744 1.6959 0.0212  -0.0755 -0.0877 100 MET G O   
13892 C CB  . MET G 109 E 1.2925 2.9696 1.7807 -0.0070 -0.0942 -0.0591 100 MET G CB  
13893 C CG  . MET G 109 E 1.3156 2.9839 1.8337 -0.0229 -0.1033 -0.0418 100 MET G CG  
13894 S SD  . MET G 109 E 1.3412 3.0175 1.8855 -0.0379 -0.1222 -0.0335 100 MET G SD  
13895 C CE  . MET G 109 E 1.3799 3.0482 1.9461 -0.0546 -0.1294 -0.0135 100 MET G CE  
13896 N N   . ASP G 110 ? 1.4612 3.1364 1.8921 0.0361  -0.0592 -0.0950 101 ASP G N   
13897 C CA  . ASP G 110 ? 1.4564 3.1409 1.8519 0.0527  -0.0505 -0.1115 101 ASP G CA  
13898 C C   . ASP G 110 ? 1.4403 3.1415 1.8383 0.0639  -0.0525 -0.1265 101 ASP G C   
13899 O O   . ASP G 110 ? 1.4459 3.1611 1.8126 0.0766  -0.0506 -0.1403 101 ASP G O   
13900 C CB  . ASP G 110 ? 1.4484 3.1171 1.8350 0.0633  -0.0357 -0.1158 101 ASP G CB  
13901 C CG  . ASP G 110 ? 1.4242 3.0817 1.8482 0.0683  -0.0285 -0.1179 101 ASP G CG  
13902 O OD1 . ASP G 110 ? 1.4160 3.0756 1.8757 0.0600  -0.0361 -0.1120 101 ASP G OD1 
13903 O OD2 . ASP G 110 ? 1.4178 3.0630 1.8388 0.0805  -0.0145 -0.1253 101 ASP G OD2 
13904 N N   . VAL G 111 ? 1.2825 2.9843 1.7169 0.0604  -0.0571 -0.1250 102 VAL G N   
13905 C CA  . VAL G 111 ? 1.2726 2.9932 1.7111 0.0712  -0.0597 -0.1403 102 VAL G CA  
13906 C C   . VAL G 111 ? 1.2783 3.0033 1.7477 0.0566  -0.0775 -0.1320 102 VAL G C   
13907 O O   . VAL G 111 ? 1.2759 2.9875 1.7814 0.0444  -0.0803 -0.1187 102 VAL G O   
13908 C CB  . VAL G 111 ? 1.2519 2.9690 1.7072 0.0860  -0.0424 -0.1514 102 VAL G CB  
13909 C CG1 . VAL G 111 ? 1.2475 2.9876 1.7101 0.0973  -0.0447 -0.1681 102 VAL G CG1 
13910 C CG2 . VAL G 111 ? 1.2524 2.9618 1.6761 0.1014  -0.0254 -0.1603 102 VAL G CG2 
13911 N N   . TRP G 112 ? 1.1809 2.9231 1.6377 0.0580  -0.0912 -0.1400 103 TRP G N   
13912 C CA  . TRP G 112 ? 1.1935 2.9380 1.6772 0.0441  -0.1107 -0.1330 103 TRP G CA  
13913 C C   . TRP G 112 ? 1.1893 2.9525 1.6781 0.0554  -0.1180 -0.1508 103 TRP G C   
13914 O O   . TRP G 112 ? 1.1893 2.9691 1.6481 0.0736  -0.1155 -0.1699 103 TRP G O   
13915 C CB  . TRP G 112 ? 1.2239 2.9688 1.6950 0.0335  -0.1245 -0.1258 103 TRP G CB  
13916 C CG  . TRP G 112 ? 1.2372 2.9677 1.7081 0.0207  -0.1194 -0.1083 103 TRP G CG  
13917 C CD1 . TRP G 112 ? 1.2341 2.9583 1.6812 0.0258  -0.1040 -0.1072 103 TRP G CD1 
13918 C CD2 . TRP G 112 ? 1.2621 2.9843 1.7568 0.0014  -0.1302 -0.0905 103 TRP G CD2 
13919 N NE1 . TRP G 112 ? 1.2557 2.9698 1.7089 0.0112  -0.1049 -0.0905 103 TRP G NE1 
13920 C CE2 . TRP G 112 ? 1.2737 2.9876 1.7558 -0.0035 -0.1202 -0.0801 103 TRP G CE2 
13921 C CE3 . TRP G 112 ? 1.2805 3.0023 1.8055 -0.0117 -0.1478 -0.0830 103 TRP G CE3 
13922 C CZ2 . TRP G 112 ? 1.3041 3.0127 1.8014 -0.0202 -0.1263 -0.0634 103 TRP G CZ2 
13923 C CZ3 . TRP G 112 ? 1.3102 3.0249 1.8520 -0.0286 -0.1535 -0.0656 103 TRP G CZ3 
13924 C CH2 . TRP G 112 ? 1.3222 3.0318 1.8493 -0.0323 -0.1424 -0.0563 103 TRP G CH2 
13925 N N   . GLY G 113 ? 1.0676 2.8289 1.5937 0.0452  -0.1282 -0.1456 104 GLY G N   
13926 C CA  . GLY G 113 ? 1.0824 2.8615 1.6140 0.0524  -0.1411 -0.1617 104 GLY G CA  
13927 C C   . GLY G 113 ? 1.1014 2.8848 1.6119 0.0495  -0.1643 -0.1654 104 GLY G C   
13928 O O   . GLY G 113 ? 1.1012 2.8747 1.6015 0.0398  -0.1685 -0.1537 104 GLY G O   
13929 N N   . GLN G 114 ? 1.0432 2.8407 1.5489 0.0586  -0.1802 -0.1834 105 GLN G N   
13930 C CA  . GLN G 114 ? 1.0792 2.8752 1.5653 0.0576  -0.2059 -0.1893 105 GLN G CA  
13931 C C   . GLN G 114 ? 1.1058 2.8870 1.6246 0.0342  -0.2259 -0.1717 105 GLN G C   
13932 O O   . GLN G 114 ? 1.1404 2.9157 1.6515 0.0298  -0.2460 -0.1721 105 GLN G O   
13933 C CB  . GLN G 114 ? 1.0950 2.9054 1.5565 0.0776  -0.2212 -0.2171 105 GLN G CB  
13934 C CG  . GLN G 114 ? 1.1098 2.9214 1.5987 0.0708  -0.2393 -0.2220 105 GLN G CG  
13935 C CD  . GLN G 114 ? 1.0786 2.9041 1.6003 0.0743  -0.2174 -0.2244 105 GLN G CD  
13936 O OE1 . GLN G 114 ? 1.0458 2.8720 1.5781 0.0762  -0.1890 -0.2157 105 GLN G OE1 
13937 N NE2 . GLN G 114 ? 1.0951 2.9288 1.6359 0.0751  -0.2307 -0.2369 105 GLN G NE2 
13938 N N   . GLY G 115 ? 0.9847 2.7588 1.5418 0.0197  -0.2213 -0.1565 106 GLY G N   
13939 C CA  . GLY G 115 ? 0.9900 2.7512 1.5802 -0.0015 -0.2393 -0.1397 106 GLY G CA  
13940 C C   . GLY G 115 ? 1.0073 2.7722 1.6169 -0.0037 -0.2600 -0.1492 106 GLY G C   
13941 O O   . GLY G 115 ? 1.0261 2.8017 1.6128 0.0111  -0.2708 -0.1715 106 GLY G O   
13942 N N   . THR G 116 ? 1.1248 2.8795 1.7753 -0.0218 -0.2675 -0.1328 107 THR G N   
13943 C CA  . THR G 116 ? 1.1508 2.9066 1.8258 -0.0277 -0.2884 -0.1387 107 THR G CA  
13944 C C   . THR G 116 ? 1.1936 2.9354 1.8912 -0.0466 -0.3096 -0.1232 107 THR G C   
13945 O O   . THR G 116 ? 1.1998 2.9311 1.9224 -0.0611 -0.3039 -0.1022 107 THR G O   
13946 C CB  . THR G 116 ? 1.1359 2.8938 1.8477 -0.0313 -0.2767 -0.1344 107 THR G CB  
13947 O OG1 . THR G 116 ? 1.0996 2.8734 1.7969 -0.0123 -0.2547 -0.1507 107 THR G OG1 
13948 C CG2 . THR G 116 ? 1.1692 2.9289 1.9085 -0.0386 -0.2984 -0.1406 107 THR G CG2 
13949 N N   . SER G 117 ? 1.2149 2.9559 1.9037 -0.0455 -0.3352 -0.1350 108 SER G N   
13950 C CA  . SER G 117 ? 1.2615 2.9910 1.9771 -0.0624 -0.3565 -0.1226 108 SER G CA  
13951 C C   . SER G 117 ? 1.2831 3.0078 2.0415 -0.0765 -0.3666 -0.1143 108 SER G C   
13952 O O   . SER G 117 ? 1.2865 3.0165 2.0470 -0.0716 -0.3749 -0.1286 108 SER G O   
13953 C CB  . SER G 117 ? 1.2993 3.0260 1.9940 -0.0560 -0.3830 -0.1386 108 SER G CB  
13954 O OG  . SER G 117 ? 1.3475 3.0647 2.0744 -0.0721 -0.4030 -0.1269 108 SER G OG  
13955 N N   . VAL G 118 ? 1.3826 3.0981 2.1745 -0.0933 -0.3658 -0.0928 109 VAL G N   
13956 C CA  . VAL G 118 ? 1.4130 3.1218 2.2487 -0.1080 -0.3765 -0.0827 109 VAL G CA  
13957 C C   . VAL G 118 ? 1.4691 3.1708 2.3290 -0.1218 -0.3975 -0.0743 109 VAL G C   
13958 O O   . VAL G 118 ? 1.4815 3.1822 2.3426 -0.1272 -0.3911 -0.0631 109 VAL G O   
13959 C CB  . VAL G 118 ? 1.3958 3.0994 2.2529 -0.1145 -0.3566 -0.0657 109 VAL G CB  
13960 C CG1 . VAL G 118 ? 1.4386 3.1336 2.3428 -0.1300 -0.3697 -0.0548 109 VAL G CG1 
13961 C CG2 . VAL G 118 ? 1.3455 3.0567 2.1876 -0.1007 -0.3362 -0.0749 109 VAL G CG2 
13962 N N   . THR G 119 ? 1.4947 3.1933 2.3751 -0.1274 -0.4222 -0.0809 110 THR G N   
13963 C CA  . THR G 119 ? 1.5544 3.2466 2.4659 -0.1408 -0.4441 -0.0742 110 THR G CA  
13964 C C   . THR G 119 ? 1.5890 3.2752 2.5455 -0.1552 -0.4506 -0.0634 110 THR G C   
13965 O O   . THR G 119 ? 1.5950 3.2807 2.5600 -0.1546 -0.4594 -0.0717 110 THR G O   
13966 C CB  . THR G 119 ? 1.5863 3.2766 2.4853 -0.1356 -0.4722 -0.0918 110 THR G CB  
13967 O OG1 . THR G 119 ? 1.5612 3.2556 2.4183 -0.1213 -0.4672 -0.1025 110 THR G OG1 
13968 C CG2 . THR G 119 ? 1.6511 3.3354 2.5889 -0.1495 -0.4949 -0.0848 110 THR G CG2 
13969 N N   . VAL G 120 ? 1.4410 3.1243 2.4256 -0.1677 -0.4463 -0.0467 111 VAL G N   
13970 C CA  . VAL G 120 ? 1.4845 3.1618 2.5127 -0.1816 -0.4531 -0.0365 111 VAL G CA  
13971 C C   . VAL G 120 ? 1.5511 3.2278 2.6098 -0.1924 -0.4750 -0.0359 111 VAL G C   
13972 O O   . VAL G 120 ? 1.5721 3.2545 2.6337 -0.1964 -0.4709 -0.0297 111 VAL G O   
13973 C CB  . VAL G 120 ? 1.4801 3.1555 2.5159 -0.1872 -0.4319 -0.0199 111 VAL G CB  
13974 C CG1 . VAL G 120 ? 1.5333 3.2025 2.6133 -0.2008 -0.4408 -0.0113 111 VAL G CG1 
13975 C CG2 . VAL G 120 ? 1.4177 3.0929 2.4276 -0.1760 -0.4111 -0.0212 111 VAL G CG2 
13976 N N   . SER G 121 ? 2.5437 2.8240 2.3241 -0.4451 -0.5967 0.6358  112 SER G N   
13977 C CA  . SER G 121 ? 2.6021 2.8911 2.3782 -0.4587 -0.5991 0.6079  112 SER G CA  
13978 C C   . SER G 121 ? 2.6475 2.9125 2.4207 -0.4489 -0.6071 0.6205  112 SER G C   
13979 O O   . SER G 121 ? 2.6217 2.8681 2.3992 -0.4202 -0.6092 0.6430  112 SER G O   
13980 C CB  . SER G 121 ? 2.5746 2.8881 2.3566 -0.4344 -0.5935 0.5724  112 SER G CB  
13981 O OG  . SER G 121 ? 2.6341 2.9564 2.4129 -0.4473 -0.5958 0.5449  112 SER G OG  
13982 N N   . SER G 122 ? 2.6733 2.9393 2.4398 -0.4734 -0.6112 0.6046  113 SER G N   
13983 C CA  . SER G 122 ? 2.7211 2.9682 2.4853 -0.4622 -0.6183 0.6087  113 SER G CA  
13984 C C   . SER G 122 ? 2.7122 2.9716 2.4804 -0.4296 -0.6158 0.5801  113 SER G C   
13985 O O   . SER G 122 ? 2.7457 2.9908 2.5129 -0.4143 -0.6207 0.5812  113 SER G O   
13986 C CB  . SER G 122 ? 2.8106 3.0500 2.5640 -0.5051 -0.6247 0.6072  113 SER G CB  
13987 O OG  . SER G 122 ? 2.8291 3.0501 2.5779 -0.5317 -0.6296 0.6386  113 SER G OG  
13988 N N   . ALA G 123 ? 3.0361 3.3213 2.8092 -0.4190 -0.6088 0.5546  114 ALA G N   
13989 C CA  . ALA G 123 ? 3.0318 3.3283 2.8095 -0.3838 -0.6069 0.5291  114 ALA G CA  
13990 C C   . ALA G 123 ? 2.9824 3.2609 2.7637 -0.3407 -0.6075 0.5495  114 ALA G C   
13991 O O   . ALA G 123 ? 2.9644 3.2295 2.7475 -0.3349 -0.6066 0.5784  114 ALA G O   
13992 C CB  . ALA G 123 ? 2.9771 3.3038 2.7608 -0.3812 -0.6000 0.5004  114 ALA G CB  
13993 N N   . SER G 124 ? 3.0687 3.3460 2.8506 -0.3112 -0.6089 0.5343  115 SER G N   
13994 C CA  . SER G 124 ? 3.0390 3.2980 2.8228 -0.2711 -0.6091 0.5517  115 SER G CA  
13995 C C   . SER G 124 ? 3.0036 3.2755 2.7894 -0.2345 -0.6064 0.5267  115 SER G C   
13996 O O   . SER G 124 ? 3.0254 3.3174 2.8117 -0.2390 -0.6064 0.4946  115 SER G O   
13997 C CB  . SER G 124 ? 3.0976 3.3317 2.8784 -0.2721 -0.6155 0.5682  115 SER G CB  
13998 O OG  . SER G 124 ? 3.1171 3.3373 2.8960 -0.3051 -0.6193 0.5929  115 SER G OG  
13999 N N   . THR G 125 ? 3.2556 3.5149 3.0424 -0.1986 -0.6043 0.5421  116 THR G N   
14000 C CA  . THR G 125 ? 3.2126 3.4819 3.0001 -0.1629 -0.6013 0.5247  116 THR G CA  
14001 C C   . THR G 125 ? 3.2644 3.5437 3.0502 -0.1505 -0.6044 0.4926  116 THR G C   
14002 O O   . THR G 125 ? 3.3270 3.5924 3.1094 -0.1431 -0.6081 0.4937  116 THR G O   
14003 C CB  . THR G 125 ? 3.2015 3.4488 2.9876 -0.1282 -0.5993 0.5499  116 THR G CB  
14004 O OG1 . THR G 125 ? 3.1811 3.4209 2.9700 -0.1390 -0.5962 0.5785  116 THR G OG1 
14005 C CG2 . THR G 125 ? 3.1737 3.4285 2.9581 -0.0916 -0.5967 0.5337  116 THR G CG2 
14006 N N   . LYS G 126 ? 3.0429 3.3464 2.8319 -0.1467 -0.6030 0.4635  117 LYS G N   
14007 C CA  . LYS G 126 ? 3.0964 3.4117 2.8851 -0.1355 -0.6063 0.4310  117 LYS G CA  
14008 C C   . LYS G 126 ? 3.0544 3.3869 2.8466 -0.1103 -0.6049 0.4092  117 LYS G C   
14009 O O   . LYS G 126 ? 3.0113 3.3598 2.8091 -0.1209 -0.6015 0.4049  117 LYS G O   
14010 C CB  . LYS G 126 ? 3.1677 3.4992 2.9586 -0.1733 -0.6081 0.4099  117 LYS G CB  
14011 C CG  . LYS G 126 ? 3.2530 3.5992 3.0452 -0.1637 -0.6114 0.3740  117 LYS G CG  
14012 C CD  . LYS G 126 ? 3.3262 3.6523 3.1119 -0.1387 -0.6155 0.3786  117 LYS G CD  
14013 C CE  . LYS G 126 ? 3.3832 3.7244 3.1701 -0.1323 -0.6191 0.3427  117 LYS G CE  
14014 N NZ  . LYS G 126 ? 3.3612 3.7199 3.1530 -0.1058 -0.6192 0.3190  117 LYS G NZ  
14015 N N   . GLY G 127 ? 3.0012 3.3299 2.7900 -0.0773 -0.6080 0.3955  118 GLY G N   
14016 C CA  . GLY G 127 ? 2.9741 3.3190 2.7658 -0.0538 -0.6088 0.3713  118 GLY G CA  
14017 C C   . GLY G 127 ? 3.0048 3.3783 2.8053 -0.0745 -0.6107 0.3351  118 GLY G C   
14018 O O   . GLY G 127 ? 3.0686 3.4460 2.8696 -0.0965 -0.6127 0.3242  118 GLY G O   
14019 N N   . PRO G 128 ? 2.8489 3.2430 2.6571 -0.0680 -0.6101 0.3152  119 PRO G N   
14020 C CA  . PRO G 128 ? 2.8822 3.3057 2.7015 -0.0896 -0.6111 0.2798  119 PRO G CA  
14021 C C   . PRO G 128 ? 2.9414 3.3715 2.7615 -0.0745 -0.6172 0.2506  119 PRO G C   
14022 O O   . PRO G 128 ? 2.9565 3.3727 2.7694 -0.0398 -0.6213 0.2520  119 PRO G O   
14023 C CB  . PRO G 128 ? 2.8544 3.2948 2.6823 -0.0808 -0.6091 0.2696  119 PRO G CB  
14024 C CG  . PRO G 128 ? 2.8227 3.2426 2.6418 -0.0410 -0.6103 0.2887  119 PRO G CG  
14025 C CD  . PRO G 128 ? 2.7991 3.1906 2.6068 -0.0421 -0.6083 0.3241  119 PRO G CD  
14026 N N   . SER G 129 ? 2.7913 3.2428 2.6197 -0.1021 -0.6176 0.2235  120 SER G N   
14027 C CA  . SER G 129 ? 2.8472 3.3135 2.6809 -0.0907 -0.6231 0.1882  120 SER G CA  
14028 C C   . SER G 129 ? 2.8375 3.3295 2.6851 -0.0815 -0.6241 0.1606  120 SER G C   
14029 O O   . SER G 129 ? 2.8248 3.3352 2.6825 -0.1069 -0.6194 0.1538  120 SER G O   
14030 C CB  . SER G 129 ? 2.9150 3.3919 2.7512 -0.1255 -0.6227 0.1717  120 SER G CB  
14031 O OG  . SER G 129 ? 2.9302 3.3826 2.7541 -0.1348 -0.6225 0.1978  120 SER G OG  
14032 N N   . VAL G 130 ? 2.9049 3.3972 2.7530 -0.0455 -0.6307 0.1448  121 VAL G N   
14033 C CA  . VAL G 130 ? 2.8999 3.4130 2.7608 -0.0306 -0.6335 0.1201  121 VAL G CA  
14034 C C   . VAL G 130 ? 2.9704 3.5050 2.8426 -0.0289 -0.6397 0.0792  121 VAL G C   
14035 O O   . VAL G 130 ? 3.0044 3.5288 2.8693 -0.0075 -0.6459 0.0730  121 VAL G O   
14036 C CB  . VAL G 130 ? 2.8559 3.3509 2.7078 0.0110  -0.6372 0.1353  121 VAL G CB  
14037 C CG1 . VAL G 130 ? 2.8550 3.3708 2.7206 0.0252  -0.6410 0.1101  121 VAL G CG1 
14038 C CG2 . VAL G 130 ? 2.7912 3.2642 2.6321 0.0090  -0.6306 0.1761  121 VAL G CG2 
14039 N N   . PHE G 131 ? 2.9302 3.4950 2.8208 -0.0516 -0.6378 0.0509  122 PHE G N   
14040 C CA  . PHE G 131 ? 3.0030 3.5923 2.9080 -0.0550 -0.6426 0.0097  122 PHE G CA  
14041 C C   . PHE G 131 ? 3.0089 3.6215 2.9325 -0.0408 -0.6464 -0.0177 122 PHE G C   
14042 O O   . PHE G 131 ? 2.9659 3.5847 2.8956 -0.0470 -0.6419 -0.0101 122 PHE G O   
14043 C CB  . PHE G 131 ? 3.0508 3.6573 2.9630 -0.1006 -0.6362 -0.0039 122 PHE G CB  
14044 C CG  . PHE G 131 ? 3.0533 3.6372 2.9481 -0.1184 -0.6329 0.0230  122 PHE G CG  
14045 C CD1 . PHE G 131 ? 3.0833 3.6500 2.9665 -0.1008 -0.6383 0.0261  122 PHE G CD1 
14046 C CD2 . PHE G 131 ? 3.0301 3.6093 2.9202 -0.1527 -0.6248 0.0452  122 PHE G CD2 
14047 C CE1 . PHE G 131 ? 3.0908 3.6362 2.9593 -0.1166 -0.6357 0.0506  122 PHE G CE1 
14048 C CE2 . PHE G 131 ? 3.0382 3.5955 2.9130 -0.1687 -0.6230 0.0701  122 PHE G CE2 
14049 C CZ  . PHE G 131 ? 3.0689 3.6095 2.9335 -0.1505 -0.6284 0.0726  122 PHE G CZ  
14050 N N   . PRO G 132 ? 2.9952 3.6206 2.9284 -0.0213 -0.6552 -0.0498 123 PRO G N   
14051 C CA  . PRO G 132 ? 3.0094 3.6568 2.9621 -0.0066 -0.6604 -0.0774 123 PRO G CA  
14052 C C   . PRO G 132 ? 3.0439 3.7251 3.0200 -0.0424 -0.6542 -0.1052 123 PRO G C   
14053 O O   . PRO G 132 ? 3.0958 3.7903 3.0771 -0.0727 -0.6500 -0.1207 123 PRO G O   
14054 C CB  . PRO G 132 ? 3.0696 3.7185 3.0244 0.0229  -0.6724 -0.1025 123 PRO G CB  
14055 C CG  . PRO G 132 ? 3.1114 3.7561 3.0584 0.0049  -0.6703 -0.1038 123 PRO G CG  
14056 C CD  . PRO G 132 ? 3.0514 3.6707 2.9784 -0.0099 -0.6617 -0.0621 123 PRO G CD  
14057 N N   . LEU G 133 ? 3.0572 3.7519 3.0471 -0.0390 -0.6534 -0.1119 124 LEU G N   
14058 C CA  . LEU G 133 ? 3.1078 3.8380 3.1248 -0.0637 -0.6499 -0.1467 124 LEU G CA  
14059 C C   . LEU G 133 ? 3.1504 3.8955 3.1851 -0.0323 -0.6620 -0.1800 124 LEU G C   
14060 O O   . LEU G 133 ? 3.1161 3.8583 3.1545 -0.0066 -0.6672 -0.1772 124 LEU G O   
14061 C CB  . LEU G 133 ? 3.0556 3.7915 3.0775 -0.0827 -0.6406 -0.1327 124 LEU G CB  
14062 C CG  . LEU G 133 ? 3.0082 3.7298 3.0136 -0.1153 -0.6292 -0.0992 124 LEU G CG  
14063 C CD1 . LEU G 133 ? 2.9575 3.6810 2.9659 -0.1250 -0.6220 -0.0825 124 LEU G CD1 
14064 C CD2 . LEU G 133 ? 3.0879 3.8264 3.0990 -0.1578 -0.6224 -0.1171 124 LEU G CD2 
14065 N N   . ALA G 134 ? 2.9819 3.7422 3.0272 -0.0344 -0.6670 -0.2114 125 ALA G N   
14066 C CA  . ALA G 134 ? 3.0146 3.7823 3.0720 0.0007  -0.6810 -0.2384 125 ALA G CA  
14067 C C   . ALA G 134 ? 3.0708 3.8702 3.1595 -0.0034 -0.6823 -0.2712 125 ALA G C   
14068 O O   . ALA G 134 ? 3.1768 4.0019 3.2834 -0.0395 -0.6728 -0.2898 125 ALA G O   
14069 C CB  . ALA G 134 ? 3.1187 3.8927 3.1781 0.0008  -0.6865 -0.2622 125 ALA G CB  
14070 N N   . PRO G 135 ? 3.0815 3.8793 3.1773 0.0326  -0.6940 -0.2794 126 PRO G N   
14071 C CA  . PRO G 135 ? 3.1173 3.9452 3.2450 0.0307  -0.6963 -0.3119 126 PRO G CA  
14072 C C   . PRO G 135 ? 3.3088 4.1694 3.4638 0.0147  -0.6984 -0.3579 126 PRO G C   
14073 O O   . PRO G 135 ? 3.3962 4.2540 3.5476 0.0269  -0.7064 -0.3705 126 PRO G O   
14074 C CB  . PRO G 135 ? 3.1133 3.9263 3.2378 0.0772  -0.7114 -0.3092 126 PRO G CB  
14075 C CG  . PRO G 135 ? 3.1179 3.9023 3.2157 0.1025  -0.7193 -0.2925 126 PRO G CG  
14076 C CD  . PRO G 135 ? 3.0594 3.8276 3.1345 0.0765  -0.7061 -0.2611 126 PRO G CD  
14077 N N   . SER G 136 ? 3.1667 4.0588 3.3491 -0.0139 -0.6905 -0.3832 127 SER G N   
14078 C CA  . SER G 136 ? 3.3894 4.3154 3.6007 -0.0318 -0.6910 -0.4290 127 SER G CA  
14079 C C   . SER G 136 ? 3.4269 4.3600 3.6547 0.0058  -0.7092 -0.4584 127 SER G C   
14080 O O   . SER G 136 ? 3.3444 4.2725 3.5780 0.0364  -0.7193 -0.4576 127 SER G O   
14081 C CB  . SER G 136 ? 3.4630 4.4210 3.7023 -0.0656 -0.6796 -0.4514 127 SER G CB  
14082 O OG  . SER G 136 ? 3.6721 4.6648 3.9430 -0.0799 -0.6807 -0.4992 127 SER G OG  
14083 N N   . SER G 137 ? 3.2336 4.1780 3.4687 0.0032  -0.7137 -0.4844 128 SER G N   
14084 C CA  . SER G 137 ? 3.2693 4.2246 3.5239 0.0348  -0.7311 -0.5172 128 SER G CA  
14085 C C   . SER G 137 ? 3.3460 4.3384 3.6429 0.0282  -0.7329 -0.5583 128 SER G C   
14086 O O   . SER G 137 ? 3.3757 4.3775 3.6923 0.0570  -0.7488 -0.5853 128 SER G O   
14087 C CB  . SER G 137 ? 3.3666 4.3257 3.6188 0.0312  -0.7346 -0.5350 128 SER G CB  
14088 O OG  . SER G 137 ? 3.4644 4.4505 3.7325 -0.0125 -0.7211 -0.5574 128 SER G OG  
14089 N N   . LYS G 138 ? 3.4279 4.4404 3.7389 -0.0089 -0.7173 -0.5636 129 LYS G N   
14090 C CA  . LYS G 138 ? 3.4812 4.5294 3.8330 -0.0193 -0.7164 -0.6015 129 LYS G CA  
14091 C C   . LYS G 138 ? 3.3226 4.3631 3.6768 -0.0020 -0.7187 -0.5853 129 LYS G C   
14092 O O   . LYS G 138 ? 3.3576 4.4254 3.7434 -0.0143 -0.7151 -0.6105 129 LYS G O   
14093 C CB  . LYS G 138 ? 3.6128 4.6883 3.9788 -0.0717 -0.6971 -0.6184 129 LYS G CB  
14094 C CG  . LYS G 138 ? 3.7117 4.7955 4.0732 -0.0984 -0.6909 -0.6327 129 LYS G CG  
14095 C CD  . LYS G 138 ? 3.6969 4.7721 4.0536 -0.0682 -0.7065 -0.6435 129 LYS G CD  
14096 C CE  . LYS G 138 ? 3.7845 4.8915 4.1819 -0.0542 -0.7184 -0.6943 129 LYS G CE  
14097 N NZ  . LYS G 138 ? 3.7592 4.8567 4.1499 -0.0264 -0.7335 -0.7034 129 LYS G NZ  
14098 N N   . SER G 139 ? 3.5637 4.5674 3.8852 0.0253  -0.7240 -0.5439 130 SER G N   
14099 C CA  . SER G 139 ? 3.4492 4.4414 3.7682 0.0424  -0.7259 -0.5241 130 SER G CA  
14100 C C   . SER G 139 ? 3.5323 4.5463 3.8873 0.0642  -0.7392 -0.5601 130 SER G C   
14101 O O   . SER G 139 ? 3.5913 4.6127 3.9607 0.0872  -0.7546 -0.5876 130 SER G O   
14102 C CB  . SER G 139 ? 3.3492 4.2981 3.6286 0.0755  -0.7334 -0.4803 130 SER G CB  
14103 O OG  . SER G 139 ? 3.2557 4.1839 3.5037 0.0544  -0.7200 -0.4438 130 SER G OG  
14104 N N   . THR G 140 ? 3.4249 4.4490 3.7948 0.0565  -0.7334 -0.5599 131 THR G N   
14105 C CA  . THR G 140 ? 3.4970 4.5468 3.9065 0.0698  -0.7434 -0.5971 131 THR G CA  
14106 C C   . THR G 140 ? 3.5181 4.5483 3.9231 0.1203  -0.7665 -0.5964 131 THR G C   
14107 O O   . THR G 140 ? 3.4375 4.4330 3.8105 0.1449  -0.7713 -0.5589 131 THR G O   
14108 C CB  . THR G 140 ? 3.4727 4.5318 3.8935 0.0529  -0.7321 -0.5904 131 THR G CB  
14109 O OG1 . THR G 140 ? 3.4898 4.5614 3.9077 0.0055  -0.7104 -0.5849 131 THR G OG1 
14110 C CG2 . THR G 140 ? 3.5710 4.6619 4.0381 0.0600  -0.7401 -0.6340 131 THR G CG2 
14111 N N   . SER G 141 ? 3.3331 4.3853 3.7703 0.1351  -0.7809 -0.6386 132 SER G N   
14112 C CA  . SER G 141 ? 3.3517 4.3877 3.7882 0.1821  -0.8047 -0.6428 132 SER G CA  
14113 C C   . SER G 141 ? 3.3486 4.3730 3.7858 0.2016  -0.8097 -0.6282 132 SER G C   
14114 O O   . SER G 141 ? 3.3688 4.4190 3.8382 0.1871  -0.8045 -0.6490 132 SER G O   
14115 C CB  . SER G 141 ? 3.4894 4.5567 3.9673 0.1895  -0.8183 -0.6948 132 SER G CB  
14116 O OG  . SER G 141 ? 3.5711 4.6268 4.0553 0.2325  -0.8416 -0.7025 132 SER G OG  
14117 N N   . GLY G 142 ? 3.5106 4.4957 3.9120 0.2343  -0.8196 -0.5928 133 GLY G N   
14118 C CA  . GLY G 142 ? 3.4802 4.4485 3.8750 0.2531  -0.8236 -0.5729 133 GLY G CA  
14119 C C   . GLY G 142 ? 3.3733 4.3430 3.7605 0.2218  -0.8017 -0.5479 133 GLY G C   
14120 O O   . GLY G 142 ? 3.4099 4.3712 3.7960 0.2304  -0.8015 -0.5336 133 GLY G O   
14121 N N   . GLY G 143 ? 3.5857 4.5663 3.9679 0.1846  -0.7834 -0.5433 134 GLY G N   
14122 C CA  . GLY G 143 ? 3.5153 4.5005 3.8920 0.1492  -0.7620 -0.5230 134 GLY G CA  
14123 C C   . GLY G 143 ? 3.4400 4.3886 3.7701 0.1489  -0.7535 -0.4719 134 GLY G C   
14124 O O   . GLY G 143 ? 3.3714 4.2869 3.6729 0.1825  -0.7648 -0.4470 134 GLY G O   
14125 N N   . THR G 144 ? 3.2218 4.1757 3.5440 0.1101  -0.7336 -0.4564 135 THR G N   
14126 C CA  . THR G 144 ? 3.1097 4.0317 3.3914 0.1049  -0.7238 -0.4080 135 THR G CA  
14127 C C   . THR G 144 ? 3.0952 4.0162 3.3628 0.0815  -0.7157 -0.4036 135 THR G C   
14128 O O   . THR G 144 ? 3.1445 4.0941 3.4327 0.0474  -0.7062 -0.4292 135 THR G O   
14129 C CB  . THR G 144 ? 3.0501 3.9745 3.3306 0.0795  -0.7078 -0.3877 135 THR G CB  
14130 O OG1 . THR G 144 ? 3.0926 4.0130 3.3818 0.1040  -0.7156 -0.3871 135 THR G OG1 
14131 C CG2 . THR G 144 ? 2.9622 3.8554 3.2031 0.0710  -0.6972 -0.3390 135 THR G CG2 
14132 N N   . ALA G 145 ? 3.1987 4.0863 3.4311 0.0995  -0.7193 -0.3717 136 ALA G N   
14133 C CA  . ALA G 145 ? 3.1968 4.0772 3.4108 0.0799  -0.7118 -0.3605 136 ALA G CA  
14134 C C   . ALA G 145 ? 3.0918 3.9451 3.2735 0.0674  -0.6993 -0.3127 136 ALA G C   
14135 O O   . ALA G 145 ? 3.0467 3.8758 3.2105 0.0893  -0.7016 -0.2835 136 ALA G O   
14136 C CB  . ALA G 145 ? 3.2283 4.0930 3.4295 0.1104  -0.7266 -0.3650 136 ALA G CB  
14137 N N   . ALA G 146 ? 3.1797 4.0369 3.3540 0.0319  -0.6863 -0.3051 137 ALA G N   
14138 C CA  . ALA G 146 ? 3.0955 3.9279 3.2406 0.0170  -0.6748 -0.2611 137 ALA G CA  
14139 C C   . ALA G 146 ? 3.0796 3.8917 3.2005 0.0183  -0.6756 -0.2452 137 ALA G C   
14140 O O   . ALA G 146 ? 3.1379 3.9650 3.2684 0.0075  -0.6775 -0.2710 137 ALA G O   
14141 C CB  . ALA G 146 ? 3.0904 3.9421 3.2457 -0.0293 -0.6580 -0.2615 137 ALA G CB  
14142 N N   . LEU G 147 ? 3.0032 3.7815 3.0935 0.0316  -0.6742 -0.2033 138 LEU G N   
14143 C CA  . LEU G 147 ? 2.9861 3.7417 3.0516 0.0326  -0.6738 -0.1826 138 LEU G CA  
14144 C C   . LEU G 147 ? 2.9009 3.6297 2.9411 0.0249  -0.6642 -0.1362 138 LEU G C   
14145 O O   . LEU G 147 ? 2.8555 3.5817 2.8960 0.0243  -0.6596 -0.1207 138 LEU G O   
14146 C CB  . LEU G 147 ? 3.0106 3.7491 3.0657 0.0746  -0.6889 -0.1866 138 LEU G CB  
14147 C CG  . LEU G 147 ? 2.9758 3.6933 3.0200 0.1132  -0.6973 -0.1697 138 LEU G CG  
14148 C CD1 . LEU G 147 ? 2.9232 3.6021 2.9329 0.1304  -0.6962 -0.1277 138 LEU G CD1 
14149 C CD2 . LEU G 147 ? 3.0785 3.8039 3.1361 0.1455  -0.7140 -0.2014 138 LEU G CD2 
14150 N N   . GLY G 148 ? 2.9140 3.6224 2.9327 0.0195  -0.6614 -0.1140 139 GLY G N   
14151 C CA  . GLY G 148 ? 2.8435 3.5275 2.8405 0.0102  -0.6524 -0.0709 139 GLY G CA  
14152 C C   . GLY G 148 ? 2.8302 3.4921 2.8059 0.0068  -0.6511 -0.0501 139 GLY G C   
14153 O O   . GLY G 148 ? 2.8803 3.5426 2.8552 0.0165  -0.6578 -0.0670 139 GLY G O   
14154 N N   . CYS G 149 ? 2.7142 3.3568 2.6734 -0.0076 -0.6424 -0.0131 140 CYS G N   
14155 C CA  . CYS G 149 ? 2.7218 3.3421 2.6614 -0.0153 -0.6396 0.0116  140 CYS G CA  
14156 C C   . CYS G 149 ? 2.7153 3.3380 2.6532 -0.0578 -0.6282 0.0287  140 CYS G C   
14157 O O   . CYS G 149 ? 2.7062 3.3299 2.6457 -0.0686 -0.6218 0.0442  140 CYS G O   
14158 C CB  . CYS G 149 ? 2.7287 3.3145 2.6455 0.0178  -0.6425 0.0462  140 CYS G CB  
14159 S SG  . CYS G 149 ? 2.7426 3.3166 2.6524 0.0655  -0.6562 0.0320  140 CYS G SG  
14160 N N   . LEU G 150 ? 2.8527 3.4753 2.7865 -0.0819 -0.6259 0.0262  141 LEU G N   
14161 C CA  . LEU G 150 ? 2.8481 3.4673 2.7758 -0.1218 -0.6166 0.0456  141 LEU G CA  
14162 C C   . LEU G 150 ? 2.8131 3.3978 2.7183 -0.1123 -0.6161 0.0869  141 LEU G C   
14163 O O   . LEU G 150 ? 2.8273 3.3968 2.7224 -0.0959 -0.6212 0.0898  141 LEU G O   
14164 C CB  . LEU G 150 ? 2.9185 3.5563 2.8539 -0.1550 -0.6146 0.0193  141 LEU G CB  
14165 C CG  . LEU G 150 ? 2.9390 3.5725 2.8663 -0.1990 -0.6064 0.0358  141 LEU G CG  
14166 C CD1 . LEU G 150 ? 2.9280 3.5715 2.8612 -0.2241 -0.5980 0.0443  141 LEU G CD1 
14167 C CD2 . LEU G 150 ? 3.0361 3.6879 2.9705 -0.2266 -0.6057 0.0051  141 LEU G CD2 
14168 N N   . VAL G 151 ? 2.6843 3.2568 2.5825 -0.1227 -0.6099 0.1181  142 VAL G N   
14169 C CA  . VAL G 151 ? 2.6889 3.2293 2.5684 -0.1133 -0.6089 0.1587  142 VAL G CA  
14170 C C   . VAL G 151 ? 2.6902 3.2267 2.5647 -0.1554 -0.6027 0.1752  142 VAL G C   
14171 O O   . VAL G 151 ? 2.6826 3.2241 2.5596 -0.1791 -0.5964 0.1871  142 VAL G O   
14172 C CB  . VAL G 151 ? 2.6823 3.2097 2.5572 -0.0899 -0.6074 0.1829  142 VAL G CB  
14173 C CG1 . VAL G 151 ? 2.6874 3.1823 2.5446 -0.0797 -0.6061 0.2232  142 VAL G CG1 
14174 C CG2 . VAL G 151 ? 2.6829 3.2147 2.5621 -0.0504 -0.6144 0.1641  142 VAL G CG2 
14175 N N   . LYS G 152 ? 2.7487 3.2756 2.6156 -0.1654 -0.6048 0.1764  143 LYS G N   
14176 C CA  . LYS G 152 ? 2.7771 3.3052 2.6411 -0.2089 -0.6006 0.1817  143 LYS G CA  
14177 C C   . LYS G 152 ? 2.7820 3.2789 2.6297 -0.2100 -0.6016 0.2170  143 LYS G C   
14178 O O   . LYS G 152 ? 2.7830 3.2619 2.6231 -0.1801 -0.6064 0.2253  143 LYS G O   
14179 C CB  . LYS G 152 ? 2.8748 3.4241 2.7467 -0.2275 -0.6021 0.1446  143 LYS G CB  
14180 C CG  . LYS G 152 ? 2.9527 3.5055 2.8212 -0.2756 -0.5975 0.1455  143 LYS G CG  
14181 C CD  . LYS G 152 ? 3.0294 3.6082 2.9085 -0.2950 -0.5974 0.1042  143 LYS G CD  
14182 C CE  . LYS G 152 ? 3.1090 3.6836 2.9791 -0.3378 -0.5947 0.1074  143 LYS G CE  
14183 N NZ  . LYS G 152 ? 3.1253 3.6991 2.9917 -0.3737 -0.5879 0.1259  143 LYS G NZ  
14184 N N   . ASP G 153 ? 2.9402 3.4309 2.7830 -0.2453 -0.5973 0.2373  144 ASP G N   
14185 C CA  . ASP G 153 ? 2.9530 3.4165 2.7825 -0.2555 -0.5987 0.2683  144 ASP G CA  
14186 C C   . ASP G 153 ? 2.9005 3.3371 2.7223 -0.2211 -0.6003 0.3010  144 ASP G C   
14187 O O   . ASP G 153 ? 2.9224 3.3400 2.7370 -0.2011 -0.6045 0.3102  144 ASP G O   
14188 C CB  . ASP G 153 ? 3.0291 3.4900 2.8545 -0.2625 -0.6030 0.2529  144 ASP G CB  
14189 C CG  . ASP G 153 ? 3.1100 3.5912 2.9392 -0.3055 -0.6004 0.2288  144 ASP G CG  
14190 O OD1 . ASP G 153 ? 3.1044 3.5958 2.9362 -0.3354 -0.5952 0.2314  144 ASP G OD1 
14191 O OD2 . ASP G 153 ? 3.2081 3.6944 3.0370 -0.3101 -0.6034 0.2072  144 ASP G OD2 
14192 N N   . TYR G 154 ? 2.9660 3.4011 2.7895 -0.2153 -0.5965 0.3185  145 TYR G N   
14193 C CA  . TYR G 154 ? 2.9131 3.3227 2.7295 -0.1878 -0.5967 0.3518  145 TYR G CA  
14194 C C   . TYR G 154 ? 2.8749 3.2740 2.6886 -0.2119 -0.5927 0.3836  145 TYR G C   
14195 O O   . TYR G 154 ? 2.8935 3.3080 2.7114 -0.2441 -0.5890 0.3783  145 TYR G O   
14196 C CB  . TYR G 154 ? 2.8699 3.2831 2.6892 -0.1488 -0.5967 0.3456  145 TYR G CB  
14197 C CG  . TYR G 154 ? 2.8304 3.2635 2.6586 -0.1564 -0.5922 0.3372  145 TYR G CG  
14198 C CD1 . TYR G 154 ? 2.8631 3.3248 2.7028 -0.1632 -0.5925 0.3007  145 TYR G CD1 
14199 C CD2 . TYR G 154 ? 2.7755 3.1988 2.6016 -0.1559 -0.5878 0.3654  145 TYR G CD2 
14200 C CE1 . TYR G 154 ? 2.8348 3.3146 2.6839 -0.1697 -0.5883 0.2925  145 TYR G CE1 
14201 C CE2 . TYR G 154 ? 2.7517 3.1927 2.5858 -0.1626 -0.5836 0.3579  145 TYR G CE2 
14202 C CZ  . TYR G 154 ? 2.7848 3.2539 2.6304 -0.1694 -0.5839 0.3214  145 TYR G CZ  
14203 O OH  . TYR G 154 ? 2.7779 3.2646 2.6327 -0.1759 -0.5796 0.3133  145 TYR G OH  
14204 N N   . PHE G 155 ? 3.0549 3.4274 2.8617 -0.1961 -0.5934 0.4165  146 PHE G N   
14205 C CA  . PHE G 155 ? 3.0015 3.3611 2.8061 -0.2136 -0.5905 0.4496  146 PHE G CA  
14206 C C   . PHE G 155 ? 2.9565 3.2913 2.7569 -0.1810 -0.5902 0.4795  146 PHE G C   
14207 O O   . PHE G 155 ? 3.0082 3.3284 2.8046 -0.1558 -0.5934 0.4814  146 PHE G O   
14208 C CB  . PHE G 155 ? 3.0098 3.3610 2.8103 -0.2518 -0.5928 0.4607  146 PHE G CB  
14209 C CG  . PHE G 155 ? 2.9025 3.2395 2.7007 -0.2715 -0.5913 0.4948  146 PHE G CG  
14210 C CD1 . PHE G 155 ? 2.8447 3.1543 2.6395 -0.2579 -0.5936 0.5273  146 PHE G CD1 
14211 C CD2 . PHE G 155 ? 2.8505 3.2018 2.6509 -0.3036 -0.5874 0.4940  146 PHE G CD2 
14212 C CE1 . PHE G 155 ? 2.7227 3.0195 2.5168 -0.2756 -0.5929 0.5585  146 PHE G CE1 
14213 C CE2 . PHE G 155 ? 2.7330 3.0710 2.5310 -0.3218 -0.5865 0.5255  146 PHE G CE2 
14214 C CZ  . PHE G 155 ? 2.6629 2.9737 2.4581 -0.3076 -0.5896 0.5579  146 PHE G CZ  
14215 N N   . PRO G 156 ? 2.8551 3.1854 2.6566 -0.1815 -0.5860 0.5022  147 PRO G N   
14216 C CA  . PRO G 156 ? 2.7475 3.0959 2.5539 -0.2055 -0.5815 0.4988  147 PRO G CA  
14217 C C   . PRO G 156 ? 2.7058 3.0723 2.5172 -0.1822 -0.5789 0.4768  147 PRO G C   
14218 O O   . PRO G 156 ? 2.7634 3.1296 2.5738 -0.1510 -0.5816 0.4614  147 PRO G O   
14219 C CB  . PRO G 156 ? 2.5813 2.9111 2.3857 -0.2097 -0.5791 0.5369  147 PRO G CB  
14220 C CG  . PRO G 156 ? 2.5680 2.8764 2.3688 -0.1699 -0.5800 0.5526  147 PRO G CG  
14221 C CD  . PRO G 156 ? 2.7551 3.0599 2.5530 -0.1589 -0.5851 0.5354  147 PRO G CD  
14222 N N   . GLU G 157 ? 2.6020 2.9836 2.4185 -0.1972 -0.5742 0.4750  148 GLU G N   
14223 C CA  . GLU G 157 ? 2.5078 2.9017 2.3289 -0.1716 -0.5719 0.4611  148 GLU G CA  
14224 C C   . GLU G 157 ? 2.4860 2.8575 2.3008 -0.1364 -0.5709 0.4875  148 GLU G C   
14225 O O   . GLU G 157 ? 2.4894 2.8396 2.2992 -0.1390 -0.5704 0.5182  148 GLU G O   
14226 C CB  . GLU G 157 ? 2.4997 2.9142 2.3281 -0.1968 -0.5666 0.4543  148 GLU G CB  
14227 C CG  . GLU G 157 ? 2.5614 3.0018 2.3974 -0.2278 -0.5663 0.4220  148 GLU G CG  
14228 C CD  . GLU G 157 ? 2.6563 3.1207 2.5023 -0.2366 -0.5614 0.4047  148 GLU G CD  
14229 O OE1 . GLU G 157 ? 2.6694 3.1388 2.5164 -0.2679 -0.5564 0.4153  148 GLU G OE1 
14230 O OE2 . GLU G 157 ? 2.6227 3.0999 2.4756 -0.2112 -0.5627 0.3812  148 GLU G OE2 
14231 N N   . PRO G 158 ? 2.6966 3.0723 2.5117 -0.1038 -0.5709 0.4754  149 PRO G N   
14232 C CA  . PRO G 158 ? 2.7157 3.1144 2.5376 -0.0953 -0.5731 0.4387  149 PRO G CA  
14233 C C   . PRO G 158 ? 2.7513 3.1457 2.5694 -0.0653 -0.5794 0.4202  149 PRO G C   
14234 O O   . PRO G 158 ? 2.7631 3.1353 2.5722 -0.0478 -0.5813 0.4365  149 PRO G O   
14235 C CB  . PRO G 158 ? 2.6865 3.0884 2.5100 -0.0777 -0.5697 0.4430  149 PRO G CB  
14236 C CG  . PRO G 158 ? 2.6647 3.0379 2.4773 -0.0544 -0.5681 0.4771  149 PRO G CG  
14237 C CD  . PRO G 158 ? 2.6743 3.0323 2.4836 -0.0756 -0.5680 0.4998  149 PRO G CD  
14238 N N   . VAL G 159 ? 2.8174 3.2335 2.6434 -0.0602 -0.5826 0.3855  150 VAL G N   
14239 C CA  . VAL G 159 ? 2.8286 3.2425 2.6515 -0.0261 -0.5890 0.3660  150 VAL G CA  
14240 C C   . VAL G 159 ? 2.8120 3.2329 2.6375 -0.0011 -0.5897 0.3559  150 VAL G C   
14241 O O   . VAL G 159 ? 2.8225 3.2588 2.6568 -0.0158 -0.5858 0.3524  150 VAL G O   
14242 C CB  . VAL G 159 ? 2.8844 3.3171 2.7149 -0.0383 -0.5937 0.3319  150 VAL G CB  
14243 C CG1 . VAL G 159 ? 2.9800 3.4012 2.8050 -0.0573 -0.5941 0.3427  150 VAL G CG1 
14244 C CG2 . VAL G 159 ? 2.9030 3.3662 2.7487 -0.0670 -0.5913 0.3069  150 VAL G CG2 
14245 N N   . THR G 160 ? 2.9349 3.3436 2.7522 0.0365  -0.5949 0.3514  151 THR G N   
14246 C CA  . THR G 160 ? 2.9294 3.3449 2.7486 0.0625  -0.5984 0.3357  151 THR G CA  
14247 C C   . THR G 160 ? 2.9786 3.4088 2.8040 0.0744  -0.6070 0.2989  151 THR G C   
14248 O O   . THR G 160 ? 3.0142 3.4359 2.8335 0.0818  -0.6111 0.2942  151 THR G O   
14249 C CB  . THR G 160 ? 2.9340 3.3221 2.7370 0.0977  -0.5983 0.3595  151 THR G CB  
14250 O OG1 . THR G 160 ? 2.9936 3.3623 2.7844 0.1171  -0.6020 0.3638  151 THR G OG1 
14251 C CG2 . THR G 160 ? 2.9017 3.2762 2.7002 0.0863  -0.5896 0.3953  151 THR G CG2 
14252 N N   . VAL G 161 ? 2.7834 3.2358 2.6218 0.0759  -0.6099 0.2724  152 VAL G N   
14253 C CA  . VAL G 161 ? 2.8302 3.2993 2.6776 0.0868  -0.6187 0.2351  152 VAL G CA  
14254 C C   . VAL G 161 ? 2.8410 3.3095 2.6882 0.1193  -0.6250 0.2243  152 VAL G C   
14255 O O   . VAL G 161 ? 2.8272 3.3031 2.6807 0.1160  -0.6217 0.2276  152 VAL G O   
14256 C CB  . VAL G 161 ? 2.8623 3.3638 2.7304 0.0519  -0.6170 0.2066  152 VAL G CB  
14257 C CG1 . VAL G 161 ? 2.9409 3.4593 2.8194 0.0638  -0.6264 0.1677  152 VAL G CG1 
14258 C CG2 . VAL G 161 ? 2.8831 3.3832 2.7493 0.0164  -0.6105 0.2202  152 VAL G CG2 
14259 N N   . SER G 162 ? 2.7517 3.2107 2.5911 0.1503  -0.6344 0.2118  153 SER G N   
14260 C CA  . SER G 162 ? 2.7575 3.2171 2.5972 0.1811  -0.6431 0.1956  153 SER G CA  
14261 C C   . SER G 162 ? 2.7644 3.2403 2.6146 0.1893  -0.6538 0.1580  153 SER G C   
14262 O O   . SER G 162 ? 2.7670 3.2479 2.6192 0.1765  -0.6542 0.1486  153 SER G O   
14263 C CB  . SER G 162 ? 2.7706 3.1968 2.5859 0.2161  -0.6451 0.2206  153 SER G CB  
14264 O OG  . SER G 162 ? 2.7837 3.1919 2.5846 0.2286  -0.6480 0.2258  153 SER G OG  
14265 N N   . TRP G 163 ? 2.7363 3.2203 2.5935 0.2108  -0.6629 0.1361  154 TRP G N   
14266 C CA  . TRP G 163 ? 2.7445 3.2420 2.6115 0.2239  -0.6749 0.1004  154 TRP G CA  
14267 C C   . TRP G 163 ? 2.7626 3.2360 2.6111 0.2661  -0.6859 0.1028  154 TRP G C   
14268 O O   . TRP G 163 ? 2.7650 3.2276 2.6068 0.2843  -0.6877 0.1129  154 TRP G O   
14269 C CB  . TRP G 163 ? 2.7513 3.2829 2.6469 0.2103  -0.6778 0.0664  154 TRP G CB  
14270 C CG  . TRP G 163 ? 2.7516 3.3090 2.6656 0.1686  -0.6689 0.0552  154 TRP G CG  
14271 C CD1 . TRP G 163 ? 2.7115 3.2788 2.6327 0.1379  -0.6571 0.0681  154 TRP G CD1 
14272 C CD2 . TRP G 163 ? 2.7973 3.3722 2.7224 0.1520  -0.6708 0.0300  154 TRP G CD2 
14273 N NE1 . TRP G 163 ? 2.7337 3.3234 2.6694 0.1028  -0.6518 0.0518  154 TRP G NE1 
14274 C CE2 . TRP G 163 ? 2.7862 3.3810 2.7246 0.1107  -0.6598 0.0283  154 TRP G CE2 
14275 C CE3 . TRP G 163 ? 2.8515 3.4270 2.7761 0.1677  -0.6808 0.0084  154 TRP G CE3 
14276 C CZ2 . TRP G 163 ? 2.8287 3.4433 2.7792 0.0845  -0.6581 0.0057  154 TRP G CZ2 
14277 C CZ3 . TRP G 163 ? 2.8912 3.4873 2.8291 0.1422  -0.6791 -0.0142 154 TRP G CZ3 
14278 C CH2 . TRP G 163 ? 2.8806 3.4957 2.8310 0.1009  -0.6677 -0.0153 154 TRP G CH2 
14279 N N   . ASN G 164 ? 2.9010 3.3660 2.7408 0.2806  -0.6933 0.0928  155 ASN G N   
14280 C CA  . ASN G 164 ? 2.9335 3.3738 2.7530 0.3196  -0.7042 0.0944  155 ASN G CA  
14281 C C   . ASN G 164 ? 2.8879 3.2960 2.6822 0.3364  -0.6986 0.1318  155 ASN G C   
14282 O O   . ASN G 164 ? 2.9059 3.2986 2.6880 0.3645  -0.7058 0.1341  155 ASN G O   
14283 C CB  . ASN G 164 ? 2.9898 3.4443 2.8226 0.3384  -0.7183 0.0621  155 ASN G CB  
14284 C CG  . ASN G 164 ? 3.0464 3.5305 2.9029 0.3263  -0.7251 0.0235  155 ASN G CG  
14285 O OD1 . ASN G 164 ? 3.0492 3.5392 2.9077 0.3082  -0.7205 0.0208  155 ASN G OD1 
14286 N ND2 . ASN G 164 ? 3.0961 3.5988 2.9713 0.3362  -0.7362 -0.0070 155 ASN G ND2 
14287 N N   . SER G 165 ? 2.9420 3.3396 2.7285 0.3184  -0.6857 0.1611  156 SER G N   
14288 C CA  . SER G 165 ? 2.8992 3.2664 2.6628 0.3311  -0.6786 0.1981  156 SER G CA  
14289 C C   . SER G 165 ? 2.8724 3.2387 2.6368 0.3372  -0.6770 0.2070  156 SER G C   
14290 O O   . SER G 165 ? 2.8744 3.2144 2.6181 0.3585  -0.6756 0.2296  156 SER G O   
14291 C CB  . SER G 165 ? 2.9337 3.2709 2.6714 0.3637  -0.6848 0.2054  156 SER G CB  
14292 O OG  . SER G 165 ? 2.9689 3.3036 2.7040 0.3567  -0.6839 0.2033  156 SER G OG  
14293 N N   . GLY G 166 ? 2.8200 3.2147 2.6083 0.3177  -0.6765 0.1894  157 GLY G N   
14294 C CA  . GLY G 166 ? 2.7983 3.1945 2.5897 0.3199  -0.6740 0.1972  157 GLY G CA  
14295 C C   . GLY G 166 ? 2.8483 3.2529 2.6472 0.3413  -0.6870 0.1706  157 GLY G C   
14296 O O   . GLY G 166 ? 2.8353 3.2443 2.6399 0.3416  -0.6857 0.1733  157 GLY G O   
14297 N N   . ALA G 167 ? 2.8158 3.2224 2.6152 0.3591  -0.7000 0.1450  158 ALA G N   
14298 C CA  . ALA G 167 ? 2.8729 3.2869 2.6805 0.3803  -0.7142 0.1187  158 ALA G CA  
14299 C C   . ALA G 167 ? 2.8932 3.3457 2.7355 0.3582  -0.7157 0.0869  158 ALA G C   
14300 O O   . ALA G 167 ? 2.9371 3.3989 2.7912 0.3715  -0.7256 0.0669  158 ALA G O   
14301 C CB  . ALA G 167 ? 2.9355 3.3366 2.7306 0.4081  -0.7286 0.1027  158 ALA G CB  
14302 N N   . LEU G 168 ? 2.8496 3.3241 2.7085 0.3247  -0.7064 0.0813  159 LEU G N   
14303 C CA  . LEU G 168 ? 2.8680 3.3798 2.7597 0.2989  -0.7052 0.0520  159 LEU G CA  
14304 C C   . LEU G 168 ? 2.8073 3.3282 2.7055 0.2656  -0.6891 0.0715  159 LEU G C   
14305 O O   . LEU G 168 ? 2.7697 3.2856 2.6603 0.2450  -0.6790 0.0903  159 LEU G O   
14306 C CB  . LEU G 168 ? 2.9106 3.4423 2.8167 0.2861  -0.7090 0.0238  159 LEU G CB  
14307 C CG  . LEU G 168 ? 2.9362 3.5073 2.8763 0.2556  -0.7059 -0.0073 159 LEU G CG  
14308 C CD1 . LEU G 168 ? 2.9877 3.5748 2.9478 0.2705  -0.7164 -0.0348 159 LEU G CD1 
14309 C CD2 . LEU G 168 ? 2.9742 3.5617 2.9247 0.2408  -0.7075 -0.0307 159 LEU G CD2 
14310 N N   . THR G 169 ? 2.9087 3.4421 2.8205 0.2605  -0.6871 0.0673  160 THR G N   
14311 C CA  . THR G 169 ? 2.8560 3.3988 2.7746 0.2296  -0.6726 0.0844  160 THR G CA  
14312 C C   . THR G 169 ? 2.8846 3.4625 2.8348 0.2080  -0.6712 0.0549  160 THR G C   
14313 O O   . THR G 169 ? 2.8625 3.4585 2.8247 0.1721  -0.6598 0.0554  160 THR G O   
14314 C CB  . THR G 169 ? 2.8102 3.3266 2.7083 0.2446  -0.6680 0.1192  160 THR G CB  
14315 O OG1 . THR G 169 ? 2.8493 3.3609 2.7478 0.2742  -0.6791 0.1075  160 THR G OG1 
14316 C CG2 . THR G 169 ? 2.7771 3.2599 2.6451 0.2594  -0.6657 0.1512  160 THR G CG2 
14317 N N   . SER G 170 ? 2.7632 3.3506 2.7270 0.2285  -0.6827 0.0293  161 SER G N   
14318 C CA  . SER G 170 ? 2.8010 3.4221 2.7969 0.2100  -0.6817 -0.0006 161 SER G CA  
14319 C C   . SER G 170 ? 2.8349 3.4857 2.8529 0.1810  -0.6789 -0.0296 161 SER G C   
14320 O O   . SER G 170 ? 2.8681 3.5184 2.8843 0.1896  -0.6865 -0.0440 161 SER G O   
14321 C CB  . SER G 170 ? 2.8626 3.4862 2.8692 0.2411  -0.6970 -0.0243 161 SER G CB  
14322 O OG  . SER G 170 ? 2.8377 3.4334 2.8231 0.2665  -0.6993 0.0021  161 SER G OG  
14323 N N   . GLY G 171 ? 2.7326 3.4088 2.7705 0.1457  -0.6677 -0.0383 162 GLY G N   
14324 C CA  . GLY G 171 ? 2.7702 3.4759 2.8295 0.1142  -0.6633 -0.0663 162 GLY G CA  
14325 C C   . GLY G 171 ? 2.7336 3.4312 2.7772 0.0906  -0.6544 -0.0475 162 GLY G C   
14326 O O   . GLY G 171 ? 2.7660 3.4856 2.8242 0.0639  -0.6509 -0.0699 162 GLY G O   
14327 N N   . VAL G 172 ? 2.8372 3.5038 2.8522 0.0988  -0.6505 -0.0077 163 VAL G N   
14328 C CA  . VAL G 172 ? 2.8036 3.4599 2.8033 0.0775  -0.6427 0.0124  163 VAL G CA  
14329 C C   . VAL G 172 ? 2.7678 3.4337 2.7714 0.0375  -0.6280 0.0272  163 VAL G C   
14330 O O   . VAL G 172 ? 2.7290 3.3886 2.7290 0.0371  -0.6226 0.0469  163 VAL G O   
14331 C CB  . VAL G 172 ? 2.7572 3.3759 2.7261 0.1045  -0.6454 0.0477  163 VAL G CB  
14332 C CG1 . VAL G 172 ? 2.7222 3.3299 2.6771 0.0812  -0.6368 0.0708  163 VAL G CG1 
14333 C CG2 . VAL G 172 ? 2.7977 3.4067 2.7612 0.1414  -0.6599 0.0321  163 VAL G CG2 
14334 N N   . HIS G 173 ? 2.7088 3.3894 2.7186 0.0032  -0.6216 0.0178  164 HIS G N   
14335 C CA  . HIS G 173 ? 2.6760 3.3604 2.6837 -0.0367 -0.6082 0.0358  164 HIS G CA  
14336 C C   . HIS G 173 ? 2.6536 3.3197 2.6420 -0.0486 -0.6055 0.0580  164 HIS G C   
14337 O O   . HIS G 173 ? 2.6954 3.3711 2.6884 -0.0594 -0.6078 0.0382  164 HIS G O   
14338 C CB  . HIS G 173 ? 2.7274 3.4475 2.7611 -0.0721 -0.6022 0.0026  164 HIS G CB  
14339 C CG  . HIS G 173 ? 2.7509 3.4900 2.8056 -0.0647 -0.6032 -0.0177 164 HIS G CG  
14340 N ND1 . HIS G 173 ? 2.7096 3.4415 2.7604 -0.0638 -0.5978 0.0041  164 HIS G ND1 
14341 C CD2 . HIS G 173 ? 2.8163 3.5812 2.8970 -0.0575 -0.6094 -0.0583 164 HIS G CD2 
14342 C CE1 . HIS G 173 ? 2.7489 3.5010 2.8220 -0.0565 -0.6005 -0.0220 164 HIS G CE1 
14343 N NE2 . HIS G 173 ? 2.8145 3.5870 2.9067 -0.0524 -0.6078 -0.0603 164 HIS G NE2 
14344 N N   . THR G 174 ? 2.8639 3.5036 2.8315 -0.0465 -0.6008 0.0984  165 THR G N   
14345 C CA  . THR G 174 ? 2.8442 3.4655 2.7945 -0.0608 -0.5975 0.1230  165 THR G CA  
14346 C C   . THR G 174 ? 2.8287 3.4575 2.7807 -0.1044 -0.5861 0.1362  165 THR G C   
14347 O O   . THR G 174 ? 2.7852 3.4061 2.7324 -0.1084 -0.5804 0.1604  165 THR G O   
14348 C CB  . THR G 174 ? 2.7946 3.3813 2.7219 -0.0301 -0.6001 0.1587  165 THR G CB  
14349 O OG1 . THR G 174 ? 2.8171 3.3963 2.7412 0.0086  -0.6109 0.1450  165 THR G OG1 
14350 C CG2 . THR G 174 ? 2.7787 3.3470 2.6907 -0.0465 -0.5964 0.1841  165 THR G CG2 
14351 N N   . PHE G 175 ? 2.6751 3.3186 2.6331 -0.1374 -0.5831 0.1202  166 PHE G N   
14352 C CA  . PHE G 175 ? 2.6772 3.3316 2.6383 -0.1819 -0.5729 0.1258  166 PHE G CA  
14353 C C   . PHE G 175 ? 2.6288 3.2562 2.5693 -0.1933 -0.5686 0.1693  166 PHE G C   
14354 O O   . PHE G 175 ? 2.6112 3.2146 2.5365 -0.1749 -0.5730 0.1891  166 PHE G O   
14355 C CB  . PHE G 175 ? 2.7440 3.4207 2.7158 -0.2142 -0.5711 0.0952  166 PHE G CB  
14356 C CG  . PHE G 175 ? 2.7982 3.5071 2.7950 -0.2145 -0.5723 0.0515  166 PHE G CG  
14357 C CD1 . PHE G 175 ? 2.8147 3.5461 2.8266 -0.2409 -0.5643 0.0383  166 PHE G CD1 
14358 C CD2 . PHE G 175 ? 2.8383 3.5551 2.8443 -0.1883 -0.5817 0.0232  166 PHE G CD2 
14359 C CE1 . PHE G 175 ? 2.8707 3.6324 2.9079 -0.2411 -0.5653 -0.0029 166 PHE G CE1 
14360 C CE2 . PHE G 175 ? 2.8939 3.6408 2.9251 -0.1880 -0.5835 -0.0178 166 PHE G CE2 
14361 C CZ  . PHE G 175 ? 2.9108 3.6805 2.9584 -0.2144 -0.5752 -0.0312 166 PHE G CZ  
14362 N N   . PRO G 176 ? 2.6170 3.2474 2.5571 -0.2233 -0.5601 0.1846  167 PRO G N   
14363 C CA  . PRO G 176 ? 2.5811 3.1873 2.5034 -0.2384 -0.5565 0.2246  167 PRO G CA  
14364 C C   . PRO G 176 ? 2.6139 3.2118 2.5273 -0.2563 -0.5586 0.2265  167 PRO G C   
14365 O O   . PRO G 176 ? 2.6714 3.2883 2.5933 -0.2775 -0.5584 0.1973  167 PRO G O   
14366 C CB  . PRO G 176 ? 2.5819 3.2008 2.5093 -0.2749 -0.5473 0.2292  167 PRO G CB  
14367 C CG  . PRO G 176 ? 2.5935 3.2365 2.5394 -0.2645 -0.5462 0.2009  167 PRO G CG  
14368 C CD  . PRO G 176 ? 2.6340 3.2898 2.5905 -0.2437 -0.5536 0.1660  167 PRO G CD  
14369 N N   . ALA G 177 ? 2.6178 3.1869 2.5147 -0.2471 -0.5606 0.2607  168 ALA G N   
14370 C CA  . ALA G 177 ? 2.6524 3.2104 2.5399 -0.2633 -0.5631 0.2660  168 ALA G CA  
14371 C C   . ALA G 177 ? 2.6872 3.2564 2.5755 -0.3137 -0.5572 0.2630  168 ALA G C   
14372 O O   . ALA G 177 ? 2.6634 3.2350 2.5516 -0.3352 -0.5512 0.2768  168 ALA G O   
14373 C CB  . ALA G 177 ? 2.6148 3.1397 2.4861 -0.2469 -0.5655 0.3057  168 ALA G CB  
14374 N N   . VAL G 178 ? 2.5127 3.0873 2.4001 -0.3332 -0.5591 0.2456  169 VAL G N   
14375 C CA  . VAL G 178 ? 2.5525 3.1362 2.4381 -0.3823 -0.5542 0.2407  169 VAL G CA  
14376 C C   . VAL G 178 ? 2.5646 3.1224 2.4334 -0.3948 -0.5578 0.2666  169 VAL G C   
14377 O O   . VAL G 178 ? 2.5744 3.1211 2.4391 -0.3736 -0.5640 0.2649  169 VAL G O   
14378 C CB  . VAL G 178 ? 2.6250 3.2388 2.5245 -0.3983 -0.5527 0.1952  169 VAL G CB  
14379 C CG1 . VAL G 178 ? 2.6717 3.2866 2.5636 -0.4436 -0.5502 0.1913  169 VAL G CG1 
14380 C CG2 . VAL G 178 ? 2.6195 3.2619 2.5374 -0.4017 -0.5469 0.1701  169 VAL G CG2 
14381 N N   . LEU G 179 ? 2.6698 3.2178 2.5291 -0.4298 -0.5545 0.2898  170 LEU G N   
14382 C CA  . LEU G 179 ? 2.6958 3.2194 2.5401 -0.4455 -0.5587 0.3136  170 LEU G CA  
14383 C C   . LEU G 179 ? 2.7790 3.3154 2.6221 -0.4805 -0.5582 0.2873  170 LEU G C   
14384 O O   . LEU G 179 ? 2.8157 3.3665 2.6595 -0.5198 -0.5524 0.2766  170 LEU G O   
14385 C CB  . LEU G 179 ? 2.6704 3.1760 2.5046 -0.4671 -0.5568 0.3512  170 LEU G CB  
14386 C CG  . LEU G 179 ? 2.6972 3.1751 2.5168 -0.4808 -0.5626 0.3781  170 LEU G CG  
14387 C CD1 . LEU G 179 ? 2.6723 3.1310 2.4901 -0.4385 -0.5691 0.3895  170 LEU G CD1 
14388 C CD2 . LEU G 179 ? 2.6756 3.1368 2.4868 -0.5026 -0.5616 0.4140  170 LEU G CD2 
14389 N N   . GLN G 180 ? 2.7917 3.3223 2.6325 -0.4668 -0.5638 0.2768  171 GLN G N   
14390 C CA  . GLN G 180 ? 2.8755 3.4173 2.7148 -0.4968 -0.5637 0.2507  171 GLN G CA  
14391 C C   . GLN G 180 ? 2.9180 3.4401 2.7406 -0.5362 -0.5648 0.2742  171 GLN G C   
14392 O O   . GLN G 180 ? 2.8814 3.3788 2.6942 -0.5345 -0.5675 0.3114  171 GLN G O   
14393 C CB  . GLN G 180 ? 2.8975 3.4382 2.7393 -0.4678 -0.5698 0.2331  171 GLN G CB  
14394 C CG  . GLN G 180 ? 2.8688 3.4283 2.7263 -0.4298 -0.5703 0.2078  171 GLN G CG  
14395 C CD  . GLN G 180 ? 2.8833 3.4357 2.7404 -0.3963 -0.5774 0.1980  171 GLN G CD  
14396 O OE1 . GLN G 180 ? 2.9327 3.5047 2.7992 -0.3941 -0.5784 0.1628  171 GLN G OE1 
14397 N NE2 . GLN G 180 ? 2.8457 3.3701 2.6924 -0.3703 -0.5822 0.2286  171 GLN G NE2 
14398 N N   . SER G 181 ? 2.9450 3.4784 2.7645 -0.5728 -0.5629 0.2513  172 SER G N   
14399 C CA  . SER G 181 ? 3.0006 3.5151 2.8026 -0.6126 -0.5648 0.2704  172 SER G CA  
14400 C C   . SER G 181 ? 3.0014 3.4849 2.7923 -0.5952 -0.5739 0.2971  172 SER G C   
14401 O O   . SER G 181 ? 3.0316 3.4925 2.8081 -0.6204 -0.5774 0.3239  172 SER G O   
14402 C CB  . SER G 181 ? 3.0975 3.6305 2.8980 -0.6520 -0.5609 0.2369  172 SER G CB  
14403 O OG  . SER G 181 ? 3.1698 3.7119 2.9770 -0.6323 -0.5638 0.2094  172 SER G OG  
14404 N N   . SER G 182 ? 3.0236 3.5048 2.8209 -0.5532 -0.5780 0.2902  173 SER G N   
14405 C CA  . SER G 182 ? 3.0256 3.4783 2.8140 -0.5343 -0.5860 0.3137  173 SER G CA  
14406 C C   . SER G 182 ? 2.9543 3.3827 2.7396 -0.5129 -0.5887 0.3546  173 SER G C   
14407 O O   . SER G 182 ? 2.9646 3.3664 2.7417 -0.5059 -0.5950 0.3795  173 SER G O   
14408 C CB  . SER G 182 ? 3.0293 3.4883 2.8250 -0.4971 -0.5891 0.2911  173 SER G CB  
14409 O OG  . SER G 182 ? 2.9573 3.4258 2.7646 -0.4577 -0.5874 0.2870  173 SER G OG  
14410 N N   . GLY G 183 ? 3.0730 3.5099 2.8655 -0.5022 -0.5839 0.3614  174 GLY G N   
14411 C CA  . GLY G 183 ? 3.0042 3.4204 2.7955 -0.4784 -0.5856 0.3974  174 GLY G CA  
14412 C C   . GLY G 183 ? 2.9444 3.3607 2.7438 -0.4272 -0.5861 0.3951  174 GLY G C   
14413 O O   . GLY G 183 ? 2.8874 3.2867 2.6861 -0.4047 -0.5868 0.4238  174 GLY G O   
14414 N N   . LEU G 184 ? 2.8041 3.2384 2.6108 -0.4087 -0.5860 0.3618  175 LEU G N   
14415 C CA  . LEU G 184 ? 2.7542 3.1905 2.5677 -0.3614 -0.5869 0.3555  175 LEU G CA  
14416 C C   . LEU G 184 ? 2.7274 3.1915 2.5529 -0.3567 -0.5817 0.3307  175 LEU G C   
14417 O O   . LEU G 184 ? 2.7664 3.2533 2.5975 -0.3863 -0.5780 0.3056  175 LEU G O   
14418 C CB  . LEU G 184 ? 2.7952 3.2298 2.6081 -0.3408 -0.5920 0.3365  175 LEU G CB  
14419 C CG  . LEU G 184 ? 2.8367 3.2457 2.6387 -0.3484 -0.5973 0.3564  175 LEU G CG  
14420 C CD1 . LEU G 184 ? 2.8776 3.2861 2.6793 -0.3264 -0.6018 0.3359  175 LEU G CD1 
14421 C CD2 . LEU G 184 ? 2.7889 3.1698 2.5856 -0.3318 -0.5988 0.3973  175 LEU G CD2 
14422 N N   . TYR G 185 ? 2.8334 3.2951 2.6631 -0.3196 -0.5814 0.3374  176 TYR G N   
14423 C CA  . TYR G 185 ? 2.8079 3.2936 2.6494 -0.3112 -0.5774 0.3159  176 TYR G CA  
14424 C C   . TYR G 185 ? 2.8379 3.3422 2.6886 -0.2903 -0.5805 0.2779  176 TYR G C   
14425 O O   . TYR G 185 ? 2.8617 3.3565 2.7083 -0.2712 -0.5859 0.2730  176 TYR G O   
14426 C CB  . TYR G 185 ? 2.7348 3.2091 2.5758 -0.2813 -0.5760 0.3398  176 TYR G CB  
14427 C CG  . TYR G 185 ? 2.7042 3.1630 2.5386 -0.3011 -0.5727 0.3757  176 TYR G CG  
14428 C CD1 . TYR G 185 ? 2.6931 3.1663 2.5322 -0.3273 -0.5667 0.3754  176 TYR G CD1 
14429 C CD2 . TYR G 185 ? 2.6898 3.1196 2.5141 -0.2935 -0.5757 0.4095  176 TYR G CD2 
14430 C CE1 . TYR G 185 ? 2.6685 3.1274 2.5013 -0.3455 -0.5642 0.4082  176 TYR G CE1 
14431 C CE2 . TYR G 185 ? 2.6658 3.0816 2.4854 -0.3113 -0.5735 0.4421  176 TYR G CE2 
14432 C CZ  . TYR G 185 ? 2.6547 3.0850 2.4781 -0.3373 -0.5680 0.4415  176 TYR G CZ  
14433 O OH  . TYR G 185 ? 2.6345 3.0506 2.4529 -0.3552 -0.5663 0.4740  176 TYR G OH  
14434 N N   . SER G 186 ? 2.6351 3.1664 2.4991 -0.2945 -0.5772 0.2505  177 SER G N   
14435 C CA  . SER G 186 ? 2.6622 3.2130 2.5379 -0.2728 -0.5807 0.2136  177 SER G CA  
14436 C C   . SER G 186 ? 2.6358 3.2068 2.5253 -0.2628 -0.5778 0.1984  177 SER G C   
14437 O O   . SER G 186 ? 2.6237 3.2036 2.5168 -0.2878 -0.5713 0.2038  177 SER G O   
14438 C CB  . SER G 186 ? 2.7403 3.3097 2.6214 -0.3014 -0.5806 0.1818  177 SER G CB  
14439 O OG  . SER G 186 ? 2.7701 3.3570 2.6630 -0.2781 -0.5850 0.1469  177 SER G OG  
14440 N N   . LEU G 187 ? 2.6742 3.2514 2.5708 -0.2261 -0.5831 0.1794  178 LEU G N   
14441 C CA  . LEU G 187 ? 2.6638 3.2622 2.5759 -0.2147 -0.5821 0.1584  178 LEU G CA  
14442 C C   . LEU G 187 ? 2.6667 3.2785 2.5892 -0.1877 -0.5896 0.1239  178 LEU G C   
14443 O O   . LEU G 187 ? 2.6762 3.2767 2.5913 -0.1721 -0.5955 0.1218  178 LEU G O   
14444 C CB  . LEU G 187 ? 2.6570 3.2397 2.5634 -0.1900 -0.5811 0.1866  178 LEU G CB  
14445 C CG  . LEU G 187 ? 2.6616 3.2183 2.5556 -0.1456 -0.5871 0.2068  178 LEU G CG  
14446 C CD1 . LEU G 187 ? 2.6627 3.2285 2.5647 -0.1093 -0.5946 0.1796  178 LEU G CD1 
14447 C CD2 . LEU G 187 ? 2.6558 3.1947 2.5413 -0.1377 -0.5828 0.2424  178 LEU G CD2 
14448 N N   . SER G 188 ? 2.8051 3.4410 2.7454 -0.1826 -0.5897 0.0964  179 SER G N   
14449 C CA  . SER G 188 ? 2.8370 3.4846 2.7886 -0.1518 -0.5981 0.0654  179 SER G CA  
14450 C C   . SER G 188 ? 2.7963 3.4394 2.7503 -0.1176 -0.6015 0.0714  179 SER G C   
14451 O O   . SER G 188 ? 2.7585 3.4037 2.7148 -0.1266 -0.5955 0.0845  179 SER G O   
14452 C CB  . SER G 188 ? 2.9074 3.5898 2.8814 -0.1748 -0.5968 0.0217  179 SER G CB  
14453 O OG  . SER G 188 ? 2.9579 3.6434 2.9286 -0.2003 -0.5956 0.0121  179 SER G OG  
14454 N N   . SER G 189 ? 2.7740 3.4096 2.7261 -0.0786 -0.6112 0.0622  180 SER G N   
14455 C CA  . SER G 189 ? 2.7550 3.3886 2.7106 -0.0445 -0.6165 0.0602  180 SER G CA  
14456 C C   . SER G 189 ? 2.8179 3.4741 2.7925 -0.0297 -0.6254 0.0175  180 SER G C   
14457 O O   . SER G 189 ? 2.8546 3.5083 2.8266 -0.0171 -0.6324 0.0038  180 SER G O   
14458 C CB  . SER G 189 ? 2.7107 3.3104 2.6439 -0.0084 -0.6211 0.0911  180 SER G CB  
14459 O OG  . SER G 189 ? 2.7005 3.2971 2.6355 0.0237  -0.6266 0.0885  180 SER G OG  
14460 N N   . VAL G 190 ? 2.7640 3.4421 2.7583 -0.0311 -0.6252 -0.0035 181 VAL G N   
14461 C CA  . VAL G 190 ? 2.8293 3.5314 2.8457 -0.0186 -0.6338 -0.0457 181 VAL G CA  
14462 C C   . VAL G 190 ? 2.8217 3.5186 2.8411 0.0174  -0.6417 -0.0468 181 VAL G C   
14463 O O   . VAL G 190 ? 2.7678 3.4497 2.7769 0.0244  -0.6380 -0.0195 181 VAL G O   
14464 C CB  . VAL G 190 ? 2.8813 3.6193 2.9236 -0.0563 -0.6270 -0.0781 181 VAL G CB  
14465 C CG1 . VAL G 190 ? 2.9019 3.6435 2.9391 -0.0932 -0.6195 -0.0773 181 VAL G CG1 
14466 C CG2 . VAL G 190 ? 2.8532 3.6000 2.9037 -0.0723 -0.6184 -0.0698 181 VAL G CG2 
14467 N N   . VAL G 191 ? 2.8764 3.5854 2.9099 0.0403  -0.6534 -0.0791 182 VAL G N   
14468 C CA  . VAL G 191 ? 2.8853 3.5923 2.9249 0.0735  -0.6629 -0.0867 182 VAL G CA  
14469 C C   . VAL G 191 ? 2.9679 3.7064 3.0380 0.0749  -0.6709 -0.1341 182 VAL G C   
14470 O O   . VAL G 191 ? 3.0178 3.7682 3.0956 0.0687  -0.6745 -0.1575 182 VAL G O   
14471 C CB  . VAL G 191 ? 2.8647 3.5381 2.8787 0.1152  -0.6730 -0.0654 182 VAL G CB  
14472 C CG1 . VAL G 191 ? 2.9090 3.5796 2.9188 0.1259  -0.6813 -0.0807 182 VAL G CG1 
14473 C CG2 . VAL G 191 ? 2.8784 3.5483 2.8972 0.1485  -0.6836 -0.0732 182 VAL G CG2 
14474 N N   . THR G 192 ? 2.9261 3.6785 3.0148 0.0824  -0.6737 -0.1490 183 THR G N   
14475 C CA  . THR G 192 ? 3.0085 3.7893 3.1281 0.0890  -0.6831 -0.1939 183 THR G CA  
14476 C C   . THR G 192 ? 3.0280 3.7921 3.1420 0.1357  -0.7003 -0.1970 183 THR G C   
14477 O O   . THR G 192 ? 2.9865 3.7287 3.0849 0.1566  -0.7022 -0.1717 183 THR G O   
14478 C CB  . THR G 192 ? 3.0317 3.8417 3.1794 0.0648  -0.6754 -0.2130 183 THR G CB  
14479 O OG1 . THR G 192 ? 2.9760 3.7702 3.1127 0.0728  -0.6715 -0.1846 183 THR G OG1 
14480 C CG2 . THR G 192 ? 3.0306 3.8611 3.1866 0.0167  -0.6600 -0.2192 183 THR G CG2 
14481 N N   . VAL G 193 ? 3.1088 3.8832 3.2352 0.1513  -0.7130 -0.2281 184 VAL G N   
14482 C CA  . VAL G 193 ? 3.1394 3.8962 3.2579 0.1954  -0.7311 -0.2325 184 VAL G CA  
14483 C C   . VAL G 193 ? 3.2364 4.0227 3.3891 0.2019  -0.7433 -0.2806 184 VAL G C   
14484 O O   . VAL G 193 ? 3.2771 4.0946 3.4551 0.1729  -0.7372 -0.3091 184 VAL G O   
14485 C CB  . VAL G 193 ? 3.1196 3.8473 3.2072 0.2133  -0.7358 -0.2126 184 VAL G CB  
14486 C CG1 . VAL G 193 ? 3.0280 3.7259 3.0833 0.2087  -0.7243 -0.1652 184 VAL G CG1 
14487 C CG2 . VAL G 193 ? 3.1633 3.9090 3.2610 0.1932  -0.7342 -0.2353 184 VAL G CG2 
14488 N N   . PRO G 194 ? 3.2017 3.9788 3.3562 0.2392  -0.7608 -0.2911 185 PRO G N   
14489 C CA  . PRO G 194 ? 3.3087 4.1130 3.4968 0.2477  -0.7743 -0.3375 185 PRO G CA  
14490 C C   . PRO G 194 ? 3.3416 4.1556 3.5329 0.2405  -0.7769 -0.3572 185 PRO G C   
14491 O O   . PRO G 194 ? 3.3223 4.1112 3.4845 0.2525  -0.7791 -0.3368 185 PRO G O   
14492 C CB  . PRO G 194 ? 3.3474 4.1296 3.5263 0.2925  -0.7938 -0.3355 185 PRO G CB  
14493 C CG  . PRO G 194 ? 3.2762 4.0289 3.4264 0.3001  -0.7870 -0.2932 185 PRO G CG  
14494 C CD  . PRO G 194 ? 3.1797 3.9222 3.3074 0.2740  -0.7691 -0.2624 185 PRO G CD  
14495 N N   . SER G 195 ? 3.3226 4.1741 3.5501 0.2195  -0.7758 -0.3977 186 SER G N   
14496 C CA  . SER G 195 ? 3.3773 4.2413 3.6113 0.2114  -0.7784 -0.4207 186 SER G CA  
14497 C C   . SER G 195 ? 3.4247 4.2720 3.6495 0.2515  -0.7992 -0.4291 186 SER G C   
14498 O O   . SER G 195 ? 3.4555 4.2984 3.6701 0.2522  -0.8017 -0.4330 186 SER G O   
14499 C CB  . SER G 195 ? 3.4963 4.4047 3.7734 0.1833  -0.7741 -0.4655 186 SER G CB  
14500 O OG  . SER G 195 ? 3.4786 4.4016 3.7611 0.1427  -0.7538 -0.4575 186 SER G OG  
14501 N N   . SER G 196 ? 3.3115 4.1496 3.5401 0.2844  -0.8147 -0.4334 187 SER G N   
14502 C CA  . SER G 196 ? 3.3599 4.1784 3.5763 0.3236  -0.8356 -0.4388 187 SER G CA  
14503 C C   . SER G 196 ? 3.2930 4.0711 3.4630 0.3386  -0.8343 -0.3986 187 SER G C   
14504 O O   . SER G 196 ? 3.3254 4.0913 3.4825 0.3567  -0.8451 -0.4035 187 SER G O   
14505 C CB  . SER G 196 ? 3.3917 4.2038 3.6171 0.3546  -0.8519 -0.4460 187 SER G CB  
14506 O OG  . SER G 196 ? 3.3072 4.0940 3.5080 0.3602  -0.8450 -0.4079 187 SER G OG  
14507 N N   . SER G 197 ? 3.4207 4.1785 3.5660 0.3295  -0.8204 -0.3591 188 SER G N   
14508 C CA  . SER G 197 ? 3.3501 4.0676 3.4522 0.3470  -0.8195 -0.3196 188 SER G CA  
14509 C C   . SER G 197 ? 3.3353 4.0496 3.4232 0.3286  -0.8100 -0.3110 188 SER G C   
14510 O O   . SER G 197 ? 3.2970 3.9791 3.3507 0.3427  -0.8094 -0.2811 188 SER G O   
14511 C CB  . SER G 197 ? 3.2649 3.9622 3.3473 0.3446  -0.8083 -0.2810 188 SER G CB  
14512 O OG  . SER G 197 ? 3.2214 3.9307 3.3068 0.3062  -0.7880 -0.2676 188 SER G OG  
14513 N N   . LEU G 198 ? 3.2057 3.9519 3.3189 0.2972  -0.8023 -0.3365 189 LEU G N   
14514 C CA  . LEU G 198 ? 3.1933 3.9372 3.2942 0.2791  -0.7941 -0.3307 189 LEU G CA  
14515 C C   . LEU G 198 ? 3.2498 3.9792 3.3382 0.3082  -0.8098 -0.3405 189 LEU G C   
14516 O O   . LEU G 198 ? 3.3341 4.0795 3.4438 0.3233  -0.8247 -0.3751 189 LEU G O   
14517 C CB  . LEU G 198 ? 3.2267 4.0091 3.3588 0.2402  -0.7841 -0.3608 189 LEU G CB  
14518 C CG  . LEU G 198 ? 3.1830 3.9828 3.3287 0.2058  -0.7673 -0.3545 189 LEU G CG  
14519 C CD1 . LEU G 198 ? 3.2364 4.0742 3.4125 0.1689  -0.7591 -0.3888 189 LEU G CD1 
14520 C CD2 . LEU G 198 ? 3.0865 3.8604 3.2011 0.1925  -0.7529 -0.3085 189 LEU G CD2 
14521 N N   . GLY G 199 ? 3.2786 3.9776 3.3329 0.3159  -0.8065 -0.3102 190 GLY G N   
14522 C CA  . GLY G 199 ? 3.3276 4.0089 3.3652 0.3429  -0.8199 -0.3147 190 GLY G CA  
14523 C C   . GLY G 199 ? 3.3422 3.9917 3.3563 0.3839  -0.8340 -0.2991 190 GLY G C   
14524 O O   . GLY G 199 ? 3.4760 4.0988 3.4628 0.4045  -0.8400 -0.2860 190 GLY G O   
14525 N N   . THR G 200 ? 3.4050 4.0560 3.4283 0.3956  -0.8394 -0.3004 191 THR G N   
14526 C CA  . THR G 200 ? 3.4084 4.0277 3.4078 0.4332  -0.8525 -0.2842 191 THR G CA  
14527 C C   . THR G 200 ? 3.3196 3.9072 3.2862 0.4348  -0.8402 -0.2380 191 THR G C   
14528 O O   . THR G 200 ? 3.3568 3.9097 3.2908 0.4614  -0.8461 -0.2159 191 THR G O   
14529 C CB  . THR G 200 ? 3.4680 4.1025 3.4926 0.4464  -0.8653 -0.3080 191 THR G CB  
14530 O OG1 . THR G 200 ? 3.5757 4.2357 3.6288 0.4508  -0.8796 -0.3510 191 THR G OG1 
14531 C CG2 . THR G 200 ? 3.4738 4.0733 3.4714 0.4831  -0.8780 -0.2883 191 THR G CG2 
14532 N N   . GLN G 201 ? 3.3182 3.9169 3.2929 0.4062  -0.8230 -0.2233 192 GLN G N   
14533 C CA  . GLN G 201 ? 3.2295 3.8018 3.1771 0.4033  -0.8098 -0.1802 192 GLN G CA  
14534 C C   . GLN G 201 ? 3.1791 3.7513 3.1187 0.3752  -0.7935 -0.1631 192 GLN G C   
14535 O O   . GLN G 201 ? 3.1777 3.7787 3.1406 0.3433  -0.7850 -0.1793 192 GLN G O   
14536 C CB  . GLN G 201 ? 3.1897 3.7729 3.1515 0.3921  -0.8029 -0.1741 192 GLN G CB  
14537 C CG  . GLN G 201 ? 3.0987 3.6592 3.0369 0.3840  -0.7876 -0.1309 192 GLN G CG  
14538 C CD  . GLN G 201 ? 3.0880 3.6081 2.9906 0.4176  -0.7936 -0.1029 192 GLN G CD  
14539 O OE1 . GLN G 201 ? 3.1308 3.6414 3.0303 0.4450  -0.8074 -0.1103 192 GLN G OE1 
14540 N NE2 . GLN G 201 ? 3.0355 3.5309 2.9110 0.4154  -0.7835 -0.0707 192 GLN G NE2 
14541 N N   . THR G 202 ? 3.1552 3.6944 3.0617 0.3865  -0.7894 -0.1308 193 THR G N   
14542 C CA  . THR G 202 ? 3.1103 3.6454 3.0074 0.3618  -0.7747 -0.1112 193 THR G CA  
14543 C C   . THR G 202 ? 3.0310 3.5688 2.9304 0.3364  -0.7584 -0.0863 193 THR G C   
14544 O O   . THR G 202 ? 2.9906 3.5133 2.8797 0.3483  -0.7570 -0.0658 193 THR G O   
14545 C CB  . THR G 202 ? 3.1023 3.6010 2.9648 0.3834  -0.7758 -0.0857 193 THR G CB  
14546 O OG1 . THR G 202 ? 3.1797 3.6774 3.0403 0.4036  -0.7903 -0.1099 193 THR G OG1 
14547 C CG2 . THR G 202 ? 3.0541 3.5464 2.9072 0.3586  -0.7606 -0.0625 193 THR G CG2 
14548 N N   . TYR G 203 ? 3.1012 3.6573 3.0131 0.3008  -0.7465 -0.0879 194 TYR G N   
14549 C CA  . TYR G 203 ? 3.0308 3.5908 2.9454 0.2726  -0.7311 -0.0653 194 TYR G CA  
14550 C C   . TYR G 203 ? 2.9921 3.5355 2.8887 0.2562  -0.7199 -0.0375 194 TYR G C   
14551 O O   . TYR G 203 ? 3.0219 3.5753 2.9236 0.2397  -0.7186 -0.0504 194 TYR G O   
14552 C CB  . TYR G 203 ? 3.0473 3.6454 2.9946 0.2412  -0.7265 -0.0930 194 TYR G CB  
14553 C CG  . TYR G 203 ? 3.0814 3.6960 3.0487 0.2549  -0.7357 -0.1170 194 TYR G CG  
14554 C CD1 . TYR G 203 ? 3.0393 3.6433 3.0013 0.2648  -0.7338 -0.0980 194 TYR G CD1 
14555 C CD2 . TYR G 203 ? 3.1600 3.8007 3.1525 0.2579  -0.7464 -0.1589 194 TYR G CD2 
14556 C CE1 . TYR G 203 ? 3.0746 3.6927 3.0551 0.2775  -0.7425 -0.1194 194 TYR G CE1 
14557 C CE2 . TYR G 203 ? 3.1967 3.8523 3.2094 0.2708  -0.7554 -0.1811 194 TYR G CE2 
14558 C CZ  . TYR G 203 ? 3.1534 3.7971 3.1597 0.2807  -0.7536 -0.1611 194 TYR G CZ  
14559 O OH  . TYR G 203 ? 3.1918 3.8496 3.2186 0.2937  -0.7631 -0.1833 194 TYR G OH  
14560 N N   . ILE G 204 ? 2.9758 3.4936 2.8519 0.2607  -0.7122 0.0003  195 ILE G N   
14561 C CA  . ILE G 204 ? 2.9359 3.4344 2.7945 0.2480  -0.7020 0.0307  195 ILE G CA  
14562 C C   . ILE G 204 ? 2.8654 3.3618 2.7239 0.2270  -0.6893 0.0584  195 ILE G C   
14563 O O   . ILE G 204 ? 2.8332 3.3195 2.6859 0.2417  -0.6890 0.0727  195 ILE G O   
14564 C CB  . ILE G 204 ? 2.9366 3.4000 2.7666 0.2806  -0.7064 0.0515  195 ILE G CB  
14565 C CG1 . ILE G 204 ? 3.0102 3.4752 2.8393 0.3014  -0.7196 0.0237  195 ILE G CG1 
14566 C CG2 . ILE G 204 ? 2.8967 3.3404 2.7111 0.2674  -0.6955 0.0831  195 ILE G CG2 
14567 C CD1 . ILE G 204 ? 3.0218 3.4531 2.8228 0.3368  -0.7257 0.0396  195 ILE G CD1 
14568 N N   . CYS G 205 ? 3.0640 3.5693 2.9284 0.1922  -0.6791 0.0658  196 CYS G N   
14569 C CA  . CYS G 205 ? 2.9984 3.4988 2.8603 0.1705  -0.6671 0.0951  196 CYS G CA  
14570 C C   . CYS G 205 ? 2.9633 3.4324 2.8022 0.1757  -0.6616 0.1317  196 CYS G C   
14571 O O   . CYS G 205 ? 2.9883 3.4499 2.8205 0.1734  -0.6626 0.1315  196 CYS G O   
14572 C CB  . CYS G 205 ? 2.9988 3.5266 2.8801 0.1277  -0.6595 0.0825  196 CYS G CB  
14573 S SG  . CYS G 205 ? 3.0273 3.5552 2.9057 0.0999  -0.6555 0.0827  196 CYS G SG  
14574 N N   . ASN G 206 ? 2.9936 3.4445 2.8213 0.1828  -0.6559 0.1625  197 ASN G N   
14575 C CA  . ASN G 206 ? 2.9602 3.3811 2.7678 0.1888  -0.6501 0.1985  197 ASN G CA  
14576 C C   . ASN G 206 ? 2.9125 3.3357 2.7246 0.1557  -0.6388 0.2219  197 ASN G C   
14577 O O   . ASN G 206 ? 2.8756 3.3053 2.6935 0.1483  -0.6344 0.2297  197 ASN G O   
14578 C CB  . ASN G 206 ? 2.9422 3.3379 2.7319 0.2243  -0.6523 0.2166  197 ASN G CB  
14579 C CG  . ASN G 206 ? 2.9885 3.3870 2.7772 0.2542  -0.6645 0.1903  197 ASN G CG  
14580 O OD1 . ASN G 206 ? 2.9849 3.3917 2.7798 0.2634  -0.6680 0.1811  197 ASN G OD1 
14581 N ND2 . ASN G 206 ? 3.0352 3.4260 2.8158 0.2699  -0.6716 0.1782  197 ASN G ND2 
14582 N N   . VAL G 207 ? 3.1091 3.5265 2.9184 0.1358  -0.6348 0.2331  198 VAL G N   
14583 C CA  . VAL G 207 ? 3.0743 3.4945 2.8883 0.1008  -0.6256 0.2529  198 VAL G CA  
14584 C C   . VAL G 207 ? 3.0559 3.4456 2.8537 0.1075  -0.6211 0.2895  198 VAL G C   
14585 O O   . VAL G 207 ? 3.1053 3.4826 2.8956 0.1123  -0.6233 0.2917  198 VAL G O   
14586 C CB  . VAL G 207 ? 3.1210 3.5626 2.9476 0.0662  -0.6251 0.2324  198 VAL G CB  
14587 C CG1 . VAL G 207 ? 3.1065 3.5493 2.9360 0.0291  -0.6164 0.2536  198 VAL G CG1 
14588 C CG2 . VAL G 207 ? 3.1872 3.6596 3.0315 0.0615  -0.6296 0.1932  198 VAL G CG2 
14589 N N   . ASN G 208 ? 3.0926 3.4705 2.8859 0.1078  -0.6149 0.3177  199 ASN G N   
14590 C CA  . ASN G 208 ? 3.0757 3.4256 2.8562 0.1137  -0.6099 0.3532  199 ASN G CA  
14591 C C   . ASN G 208 ? 3.0446 3.3967 2.8313 0.0779  -0.6029 0.3741  199 ASN G C   
14592 O O   . ASN G 208 ? 3.0303 3.3992 2.8267 0.0576  -0.5996 0.3715  199 ASN G O   
14593 C CB  . ASN G 208 ? 3.0758 3.4072 2.8446 0.1446  -0.6083 0.3713  199 ASN G CB  
14594 C CG  . ASN G 208 ? 3.1536 3.4789 2.9130 0.1808  -0.6160 0.3529  199 ASN G CG  
14595 O OD1 . ASN G 208 ? 3.2037 3.5357 2.9645 0.1851  -0.6226 0.3296  199 ASN G OD1 
14596 N ND2 . ASN G 208 ? 3.1733 3.4854 2.9225 0.2065  -0.6156 0.3634  199 ASN G ND2 
14597 N N   . HIS G 209 ? 2.9732 3.3076 2.7542 0.0702  -0.6010 0.3947  200 HIS G N   
14598 C CA  . HIS G 209 ? 2.9583 3.2904 2.7436 0.0371  -0.5959 0.4172  200 HIS G CA  
14599 C C   . HIS G 209 ? 2.9395 3.2420 2.7151 0.0504  -0.5926 0.4520  200 HIS G C   
14600 O O   . HIS G 209 ? 2.9865 3.2741 2.7566 0.0581  -0.5947 0.4563  200 HIS G O   
14601 C CB  . HIS G 209 ? 2.9934 3.3373 2.7848 0.0067  -0.5983 0.4023  200 HIS G CB  
14602 C CG  . HIS G 209 ? 2.9847 3.3268 2.7796 -0.0298 -0.5943 0.4231  200 HIS G CG  
14603 N ND1 . HIS G 209 ? 3.0131 3.3392 2.8043 -0.0427 -0.5951 0.4395  200 HIS G ND1 
14604 C CD2 . HIS G 209 ? 2.9615 3.3151 2.7628 -0.0565 -0.5899 0.4301  200 HIS G CD2 
14605 C CE1 . HIS G 209 ? 2.9933 3.3204 2.7880 -0.0757 -0.5922 0.4561  200 HIS G CE1 
14606 N NE2 . HIS G 209 ? 2.9618 3.3056 2.7622 -0.0849 -0.5888 0.4508  200 HIS G NE2 
14607 N N   . LYS G 210 ? 2.9377 3.2320 2.7121 0.0527  -0.5871 0.4762  201 LYS G N   
14608 C CA  . LYS G 210 ? 2.9368 3.2036 2.7032 0.0685  -0.5834 0.5083  201 LYS G CA  
14609 C C   . LYS G 210 ? 2.9569 3.2115 2.7262 0.0458  -0.5826 0.5294  201 LYS G C   
14610 O O   . LYS G 210 ? 2.9517 3.1845 2.7151 0.0621  -0.5823 0.5446  201 LYS G O   
14611 C CB  . LYS G 210 ? 2.8580 3.1204 2.6234 0.0750  -0.5776 0.5281  201 LYS G CB  
14612 C CG  . LYS G 210 ? 2.8613 3.0955 2.6179 0.0973  -0.5734 0.5575  201 LYS G CG  
14613 C CD  . LYS G 210 ? 2.8062 3.0356 2.5612 0.1041  -0.5672 0.5770  201 LYS G CD  
14614 C CE  . LYS G 210 ? 2.7952 2.9969 2.5406 0.1306  -0.5628 0.6018  201 LYS G CE  
14615 N NZ  . LYS G 210 ? 2.7441 2.9320 2.4955 0.1138  -0.5596 0.6302  201 LYS G NZ  
14616 N N   . PRO G 211 ? 2.9579 3.2245 2.7356 0.0085  -0.5823 0.5316  202 PRO G N   
14617 C CA  . PRO G 211 ? 2.8763 3.1285 2.6557 -0.0124 -0.5828 0.5537  202 PRO G CA  
14618 C C   . PRO G 211 ? 2.9885 3.2306 2.7645 -0.0049 -0.5874 0.5458  202 PRO G C   
14619 O O   . PRO G 211 ? 2.9313 3.1518 2.7058 -0.0008 -0.5872 0.5680  202 PRO G O   
14620 C CB  . PRO G 211 ? 2.7700 3.0407 2.5570 -0.0542 -0.5831 0.5484  202 PRO G CB  
14621 C CG  . PRO G 211 ? 2.7626 3.0505 2.5524 -0.0525 -0.5795 0.5394  202 PRO G CG  
14622 C CD  . PRO G 211 ? 2.8931 3.1842 2.6785 -0.0168 -0.5811 0.5183  202 PRO G CD  
14623 N N   . SER G 212 ? 3.0744 3.3315 2.8498 -0.0025 -0.5915 0.5143  203 SER G N   
14624 C CA  . SER G 212 ? 3.1510 3.3995 2.9223 0.0077  -0.5959 0.5040  203 SER G CA  
14625 C C   . SER G 212 ? 3.1924 3.4314 2.9550 0.0490  -0.5963 0.4963  203 SER G C   
14626 O O   . SER G 212 ? 3.2568 3.4861 3.0145 0.0624  -0.5994 0.4891  203 SER G O   
14627 C CB  . SER G 212 ? 3.1527 3.4229 2.9282 -0.0147 -0.6003 0.4732  203 SER G CB  
14628 O OG  . SER G 212 ? 3.1201 3.4126 2.8983 -0.0073 -0.6010 0.4456  203 SER G OG  
14629 N N   . ASN G 213 ? 3.2736 3.5138 3.0332 0.0688  -0.5934 0.4987  204 ASN G N   
14630 C CA  . ASN G 213 ? 3.2615 3.4929 3.0109 0.1074  -0.5941 0.4907  204 ASN G CA  
14631 C C   . ASN G 213 ? 3.3476 3.5894 3.0947 0.1166  -0.6008 0.4582  204 ASN G C   
14632 O O   . ASN G 213 ? 3.4057 3.6331 3.1451 0.1354  -0.6029 0.4562  204 ASN G O   
14633 C CB  . ASN G 213 ? 3.2569 3.4593 2.9978 0.1302  -0.5903 0.5170  204 ASN G CB  
14634 C CG  . ASN G 213 ? 3.2753 3.4681 3.0045 0.1659  -0.5886 0.5166  204 ASN G CG  
14635 O OD1 . ASN G 213 ? 3.2688 3.4462 2.9872 0.1921  -0.5896 0.5137  204 ASN G OD1 
14636 N ND2 . ASN G 213 ? 3.3087 3.5101 3.0391 0.1664  -0.5861 0.5191  204 ASN G ND2 
14637 N N   . THR G 214 ? 3.1581 3.4261 2.9135 0.1001  -0.6039 0.4324  205 THR G N   
14638 C CA  . THR G 214 ? 3.2108 3.4926 2.9664 0.1086  -0.6106 0.3986  205 THR G CA  
14639 C C   . THR G 214 ? 3.1482 3.4443 2.9048 0.1258  -0.6129 0.3797  205 THR G C   
14640 O O   . THR G 214 ? 3.0904 3.3952 2.8523 0.1172  -0.6094 0.3861  205 THR G O   
14641 C CB  . THR G 214 ? 3.2298 3.5315 2.9959 0.0744  -0.6129 0.3798  205 THR G CB  
14642 O OG1 . THR G 214 ? 3.1874 3.5058 2.9635 0.0450  -0.6093 0.3825  205 THR G OG1 
14643 C CG2 . THR G 214 ? 3.2979 3.5841 3.0615 0.0611  -0.6127 0.3944  205 THR G CG2 
14644 N N   . LYS G 215 ? 3.3691 3.6666 3.1204 0.1504  -0.6193 0.3566  206 LYS G N   
14645 C CA  . LYS G 215 ? 3.3497 3.6617 3.1031 0.1671  -0.6240 0.3337  206 LYS G CA  
14646 C C   . LYS G 215 ? 3.4060 3.7365 3.1660 0.1646  -0.6316 0.2981  206 LYS G C   
14647 O O   . LYS G 215 ? 3.4774 3.7978 3.2306 0.1726  -0.6346 0.2941  206 LYS G O   
14648 C CB  . LYS G 215 ? 3.3493 3.6399 3.0866 0.2061  -0.6253 0.3430  206 LYS G CB  
14649 C CG  . LYS G 215 ? 3.3255 3.5970 3.0556 0.2114  -0.6174 0.3772  206 LYS G CG  
14650 C CD  . LYS G 215 ? 3.3248 3.5755 3.0376 0.2494  -0.6189 0.3830  206 LYS G CD  
14651 C CE  . LYS G 215 ? 3.2977 3.5312 3.0039 0.2549  -0.6106 0.4150  206 LYS G CE  
14652 N NZ  . LYS G 215 ? 3.3552 3.5731 3.0616 0.2416  -0.6033 0.4433  206 LYS G NZ  
14653 N N   . VAL G 216 ? 3.1812 3.5393 2.9555 0.1509  -0.6343 0.2722  207 VAL G N   
14654 C CA  . VAL G 216 ? 3.2292 3.6064 3.0116 0.1487  -0.6416 0.2366  207 VAL G CA  
14655 C C   . VAL G 216 ? 3.1991 3.5911 2.9874 0.1684  -0.6484 0.2113  207 VAL G C   
14656 O O   . VAL G 216 ? 3.1737 3.5766 2.9699 0.1628  -0.6460 0.2121  207 VAL G O   
14657 C CB  . VAL G 216 ? 3.2491 3.6482 3.0461 0.1079  -0.6388 0.2243  207 VAL G CB  
14658 C CG1 . VAL G 216 ? 3.3165 3.7377 3.1236 0.1058  -0.6459 0.1851  207 VAL G CG1 
14659 C CG2 . VAL G 216 ? 3.3104 3.6924 3.1004 0.0904  -0.6341 0.2483  207 VAL G CG2 
14660 N N   . ASP G 217 ? 3.2568 3.6484 3.0412 0.1915  -0.6573 0.1892  208 ASP G N   
14661 C CA  . ASP G 217 ? 3.2471 3.6546 3.0393 0.2091  -0.6663 0.1596  208 ASP G CA  
14662 C C   . ASP G 217 ? 3.2915 3.7237 3.0987 0.1941  -0.6715 0.1246  208 ASP G C   
14663 O O   . ASP G 217 ? 3.3769 3.8028 3.1788 0.1895  -0.6719 0.1233  208 ASP G O   
14664 C CB  . ASP G 217 ? 3.2562 3.6407 3.0299 0.2505  -0.6735 0.1631  208 ASP G CB  
14665 C CG  . ASP G 217 ? 3.2400 3.5994 2.9980 0.2653  -0.6676 0.1973  208 ASP G CG  
14666 O OD1 . ASP G 217 ? 3.1941 3.5617 2.9597 0.2558  -0.6633 0.2049  208 ASP G OD1 
14667 O OD2 . ASP G 217 ? 3.2838 3.6156 3.0221 0.2861  -0.6670 0.2159  208 ASP G OD2 
14668 N N   . LYS G 218 ? 3.0847 3.5461 2.9122 0.1806  -0.6736 0.0980  209 LYS G N   
14669 C CA  . LYS G 218 ? 3.1136 3.6009 2.9577 0.1646  -0.6779 0.0626  209 LYS G CA  
14670 C C   . LYS G 218 ? 3.1065 3.6137 2.9652 0.1813  -0.6876 0.0298  209 LYS G C   
14671 O O   . LYS G 218 ? 3.0672 3.5878 2.9378 0.1759  -0.6859 0.0263  209 LYS G O   
14672 C CB  . LYS G 218 ? 3.0979 3.6047 2.9558 0.1206  -0.6686 0.0610  209 LYS G CB  
14673 C CG  . LYS G 218 ? 3.1340 3.6628 3.0049 0.0999  -0.6708 0.0296  209 LYS G CG  
14674 C CD  . LYS G 218 ? 3.1882 3.6971 3.0435 0.1026  -0.6712 0.0409  209 LYS G CD  
14675 C CE  . LYS G 218 ? 3.2204 3.7492 3.0868 0.0761  -0.6713 0.0144  209 LYS G CE  
14676 N NZ  . LYS G 218 ? 3.2698 3.7787 3.1212 0.0729  -0.6701 0.0291  209 LYS G NZ  
14677 N N   . LYS G 219 ? 2.9580 3.4667 2.8163 0.2020  -0.6983 0.0060  210 LYS G N   
14678 C CA  . LYS G 219 ? 2.9575 3.4871 2.8327 0.2162  -0.7091 -0.0286 210 LYS G CA  
14679 C C   . LYS G 219 ? 2.9765 3.5423 2.8789 0.1840  -0.7070 -0.0609 210 LYS G C   
14680 O O   . LYS G 219 ? 3.0073 3.5798 2.9118 0.1627  -0.7035 -0.0682 210 LYS G O   
14681 C CB  . LYS G 219 ? 2.9994 3.5170 2.8640 0.2495  -0.7220 -0.0426 210 LYS G CB  
14682 C CG  . LYS G 219 ? 3.0492 3.5845 2.9297 0.2690  -0.7357 -0.0773 210 LYS G CG  
14683 C CD  . LYS G 219 ? 3.1021 3.6185 2.9659 0.3032  -0.7483 -0.0837 210 LYS G CD  
14684 C CE  . LYS G 219 ? 3.1706 3.7057 3.0518 0.3207  -0.7636 -0.1216 210 LYS G CE  
14685 N NZ  . LYS G 219 ? 3.2257 3.7404 3.0885 0.3541  -0.7766 -0.1266 210 LYS G NZ  
14686 N N   . VAL G 220 ? 3.0487 3.6372 2.9717 0.1803  -0.7088 -0.0804 211 VAL G N   
14687 C CA  . VAL G 220 ? 3.0860 3.7105 3.0369 0.1495  -0.7058 -0.1123 211 VAL G CA  
14688 C C   . VAL G 220 ? 3.1557 3.7995 3.1255 0.1697  -0.7194 -0.1515 211 VAL G C   
14689 O O   . VAL G 220 ? 3.1505 3.7929 3.1242 0.1929  -0.7265 -0.1547 211 VAL G O   
14690 C CB  . VAL G 220 ? 3.0381 3.6752 3.0001 0.1239  -0.6952 -0.1032 211 VAL G CB  
14691 C CG1 . VAL G 220 ? 3.0859 3.7597 3.0756 0.0898  -0.6909 -0.1368 211 VAL G CG1 
14692 C CG2 . VAL G 220 ? 2.9687 3.5838 2.9109 0.1074  -0.6835 -0.0621 211 VAL G CG2 
14693 N N   . GLU G 221 ? 3.0237 3.6847 3.0053 0.1611  -0.7233 -0.1812 212 GLU G N   
14694 C CA  . GLU G 221 ? 3.0998 3.7781 3.0992 0.1809  -0.7374 -0.2193 212 GLU G CA  
14695 C C   . GLU G 221 ? 3.1612 3.8760 3.1891 0.1496  -0.7341 -0.2565 212 GLU G C   
14696 O O   . GLU G 221 ? 3.1510 3.8722 3.1783 0.1152  -0.7221 -0.2509 212 GLU G O   
14697 C CB  . GLU G 221 ? 3.1342 3.7901 3.1140 0.2120  -0.7485 -0.2174 212 GLU G CB  
14698 C CG  . GLU G 221 ? 3.1435 3.7895 3.1089 0.1962  -0.7421 -0.2070 212 GLU G CG  
14699 C CD  . GLU G 221 ? 3.1600 3.7764 3.1000 0.2286  -0.7508 -0.1945 212 GLU G CD  
14700 O OE1 . GLU G 221 ? 3.1844 3.7832 3.1063 0.2206  -0.7443 -0.1742 212 GLU G OE1 
14701 O OE2 . GLU G 221 ? 3.1900 3.8002 3.1281 0.2616  -0.7642 -0.2054 212 GLU G OE2 
14702 N N   . PRO G 222 ? 2.9643 3.7035 3.0178 0.1599  -0.7447 -0.2951 213 PRO G N   
14703 C CA  . PRO G 222 ? 3.0364 3.8113 3.1182 0.1312  -0.7418 -0.3337 213 PRO G CA  
14704 C C   . PRO G 222 ? 3.0749 3.8466 3.1466 0.1178  -0.7392 -0.3367 213 PRO G C   
14705 O O   . PRO G 222 ? 3.0887 3.8387 3.1413 0.1428  -0.7475 -0.3283 213 PRO G O   
14706 C CB  . PRO G 222 ? 3.1081 3.9018 3.2147 0.1562  -0.7575 -0.3711 213 PRO G CB  
14707 C CG  . PRO G 222 ? 3.0617 3.8364 3.1589 0.1863  -0.7642 -0.3514 213 PRO G CG  
14708 C CD  . PRO G 222 ? 2.9831 3.7192 3.0423 0.1964  -0.7593 -0.3052 213 PRO G CD  
14709 N N   . LYS G 223 ? 3.3443 4.1371 3.4281 0.0773  -0.7275 -0.3488 214 LYS G N   
14710 C CA  . LYS G 223 ? 3.3847 4.1753 3.4592 0.0595  -0.7236 -0.3515 214 LYS G CA  
14711 C C   . LYS G 223 ? 3.5075 4.3197 3.6014 0.0676  -0.7340 -0.3942 214 LYS G C   
14712 O O   . LYS G 223 ? 3.5681 4.4080 3.6911 0.0698  -0.7395 -0.4285 214 LYS G O   
14713 C CB  . LYS G 223 ? 3.3858 4.1890 3.4636 0.0114  -0.7072 -0.3477 214 LYS G CB  
14714 C CG  . LYS G 223 ? 3.4663 4.2640 3.5317 -0.0092 -0.7026 -0.3467 214 LYS G CG  
14715 C CD  . LYS G 223 ? 3.4693 4.2802 3.5383 -0.0583 -0.6875 -0.3458 214 LYS G CD  
14716 C CE  . LYS G 223 ? 3.5107 4.3153 3.5670 -0.0780 -0.6841 -0.3461 214 LYS G CE  
14717 N NZ  . LYS G 223 ? 3.5488 4.3671 3.6085 -0.1275 -0.6703 -0.3493 214 LYS G NZ  
14718 N N   . ALA H 1   ? 2.0059 2.5266 2.6724 0.7119  -0.5945 0.4067  512 ALA D N   
14719 C CA  . ALA H 1   ? 1.9330 2.4630 2.5985 0.7136  -0.6075 0.4183  512 ALA D CA  
14720 C C   . ALA H 1   ? 1.8776 2.3908 2.5162 0.7197  -0.6212 0.3911  512 ALA D C   
14721 O O   . ALA H 1   ? 1.8629 2.3582 2.4827 0.7229  -0.6191 0.3627  512 ALA D O   
14722 C CB  . ALA H 1   ? 1.9082 2.4336 2.5675 0.7131  -0.6071 0.4123  512 ALA D CB  
14723 N N   . VAL H 2   ? 1.7587 2.2760 2.3951 0.7214  -0.6363 0.3982  513 VAL D N   
14724 C CA  . VAL H 2   ? 1.7804 2.2756 2.3951 0.7245  -0.6541 0.3707  513 VAL D CA  
14725 C C   . VAL H 2   ? 1.7831 2.2496 2.3709 0.7262  -0.6588 0.3313  513 VAL D C   
14726 O O   . VAL H 2   ? 1.7753 2.2418 2.3611 0.7256  -0.6530 0.3295  513 VAL D O   
14727 C CB  . VAL H 2   ? 1.8041 2.3083 2.4243 0.7253  -0.6706 0.3875  513 VAL D CB  
14728 C CG1 . VAL H 2   ? 1.8043 2.3360 2.4430 0.7272  -0.6652 0.4211  513 VAL D CG1 
14729 C CG2 . VAL H 2   ? 1.8073 2.3195 2.4310 0.7247  -0.6722 0.3984  513 VAL D CG2 
14730 N N   . GLY H 3   ? 2.0108 2.4529 2.5770 0.7287  -0.6692 0.2991  514 GLY D N   
14731 C CA  . GLY H 3   ? 1.9426 2.3568 2.4802 0.7315  -0.6740 0.2594  514 GLY D CA  
14732 C C   . GLY H 3   ? 1.9657 2.3557 2.4880 0.7318  -0.6954 0.2345  514 GLY D C   
14733 O O   . GLY H 3   ? 1.9747 2.3661 2.5035 0.7312  -0.7029 0.2410  514 GLY D O   
14734 N N   . ILE H 4   ? 1.8039 2.1705 2.3058 0.7326  -0.7058 0.2054  515 ILE D N   
14735 C CA  . ILE H 4   ? 1.8268 2.1670 2.3147 0.7319  -0.7279 0.1799  515 ILE D CA  
14736 C C   . ILE H 4   ? 1.8244 2.1378 2.2802 0.7369  -0.7261 0.1360  515 ILE D C   
14737 O O   . ILE H 4   ? 1.8416 2.1292 2.2813 0.7365  -0.7432 0.1088  515 ILE D O   
14738 C CB  . ILE H 4   ? 1.8462 2.1815 2.3415 0.7273  -0.7466 0.1871  515 ILE D CB  
14739 C CG1 . ILE H 4   ? 1.8719 2.1831 2.3608 0.7248  -0.7712 0.1694  515 ILE D CG1 
14740 C CG2 . ILE H 4   ? 1.8416 2.1683 2.3242 0.7282  -0.7436 0.1721  515 ILE D CG2 
14741 C CD1 . ILE H 4   ? 1.8923 2.2045 2.3961 0.7194  -0.7897 0.1862  515 ILE D CD1 
14742 N N   . GLY H 5   ? 1.9867 2.3057 2.4322 0.7417  -0.7052 0.1279  516 GLY D N   
14743 C CA  . GLY H 5   ? 1.9837 2.2804 2.3970 0.7478  -0.7011 0.0866  516 GLY D CA  
14744 C C   . GLY H 5   ? 1.9747 2.2631 2.3676 0.7514  -0.6918 0.0654  516 GLY D C   
14745 O O   . GLY H 5   ? 1.9694 2.2694 2.3733 0.7492  -0.6873 0.0828  516 GLY D O   
14746 N N   . ALA H 6   ? 2.0322 2.3004 2.3935 0.7575  -0.6884 0.0265  517 ALA D N   
14747 C CA  . ALA H 6   ? 2.0538 2.3122 2.3900 0.7624  -0.6784 0.0010  517 ALA D CA  
14748 C C   . ALA H 6   ? 2.0359 2.2787 2.3685 0.7594  -0.6956 -0.0084 517 ALA D C   
14749 O O   . ALA H 6   ? 2.0562 2.2862 2.3950 0.7551  -0.7174 -0.0097 517 ALA D O   
14750 C CB  . ALA H 6   ? 2.0294 2.2701 2.3312 0.7698  -0.6715 -0.0393 517 ALA D CB  
14751 N N   . VAL H 7   ? 1.9614 2.2046 2.2831 0.7618  -0.6856 -0.0157 518 VAL D N   
14752 C CA  . VAL H 7   ? 1.9742 2.2022 2.2892 0.7599  -0.6994 -0.0275 518 VAL D CA  
14753 C C   . VAL H 7   ? 1.9701 2.1780 2.2479 0.7669  -0.6927 -0.0695 518 VAL D C   
14754 O O   . VAL H 7   ? 1.9594 2.1649 2.2168 0.7730  -0.6791 -0.0893 518 VAL D O   
14755 C CB  . VAL H 7   ? 1.9691 2.2169 2.3076 0.7556  -0.6958 0.0053  518 VAL D CB  
14756 C CG1 . VAL H 7   ? 1.9812 2.2422 2.3527 0.7480  -0.7102 0.0407  518 VAL D CG1 
14757 C CG2 . VAL H 7   ? 2.0383 2.3083 2.3807 0.7588  -0.6696 0.0205  518 VAL D CG2 
14758 N N   . PHE H 8   ? 2.1275 2.3213 2.3952 0.7663  -0.7017 -0.0837 519 PHE D N   
14759 C CA  . PHE H 8   ? 2.0705 2.2450 2.3026 0.7728  -0.6965 -0.1237 519 PHE D CA  
14760 C C   . PHE H 8   ? 2.0754 2.2539 2.3044 0.7734  -0.6896 -0.1211 519 PHE D C   
14761 O O   . PHE H 8   ? 2.0629 2.2463 2.3130 0.7676  -0.7005 -0.0992 519 PHE D O   
14762 C CB  . PHE H 8   ? 2.0820 2.2269 2.2992 0.7720  -0.7190 -0.1536 519 PHE D CB  
14763 C CG  . PHE H 8   ? 2.0816 2.2047 2.2615 0.7784  -0.7161 -0.1965 519 PHE D CG  
14764 C CD1 . PHE H 8   ? 2.0709 2.1906 2.2249 0.7853  -0.7022 -0.2214 519 PHE D CD1 
14765 C CD2 . PHE H 8   ? 2.0931 2.1983 2.2633 0.7773  -0.7285 -0.2130 519 PHE D CD2 
14766 C CE1 . PHE H 8   ? 2.0709 2.1712 2.1893 0.7911  -0.6999 -0.2615 519 PHE D CE1 
14767 C CE2 . PHE H 8   ? 2.0932 2.1781 2.2287 0.7831  -0.7265 -0.2530 519 PHE D CE2 
14768 C CZ  . PHE H 8   ? 2.0820 2.1648 2.1912 0.7900  -0.7120 -0.2773 519 PHE D CZ  
14769 N N   . LEU H 9   ? 1.9891 2.1655 2.1907 0.7805  -0.6715 -0.1439 520 LEU D N   
14770 C CA  . LEU H 9   ? 1.9821 2.1630 2.1797 0.7816  -0.6632 -0.1417 520 LEU D CA  
14771 C C   . LEU H 9   ? 1.9914 2.1469 2.1593 0.7847  -0.6715 -0.1789 520 LEU D C   
14772 O O   . LEU H 9   ? 1.9926 2.1478 2.1620 0.7836  -0.6728 -0.1752 520 LEU D O   
14773 C CB  . LEU H 9   ? 1.9586 2.1571 2.1465 0.7873  -0.6350 -0.1386 520 LEU D CB  
14774 C CG  . LEU H 9   ? 1.9454 2.1699 2.1591 0.7853  -0.6218 -0.1039 520 LEU D CG  
14775 C CD1 . LEU H 9   ? 1.9234 2.1612 2.1224 0.7913  -0.5940 -0.1068 520 LEU D CD1 
14776 C CD2 . LEU H 9   ? 1.9501 2.1909 2.2027 0.7773  -0.6311 -0.0625 520 LEU D CD2 
14777 N N   . GLY H 10  ? 2.1472 2.2818 2.2886 0.7885  -0.6769 -0.2142 521 GLY D N   
14778 C CA  . GLY H 10  ? 2.1570 2.2659 2.2697 0.7913  -0.6861 -0.2515 521 GLY D CA  
14779 C C   . GLY H 10  ? 2.1422 2.2491 2.2191 0.7995  -0.6662 -0.2804 521 GLY D C   
14780 O O   . GLY H 10  ? 2.1247 2.2482 2.1958 0.8035  -0.6450 -0.2752 521 GLY D O   
14781 N N   . PHE H 11  ? 2.1116 2.1969 2.1630 0.8018  -0.6738 -0.3123 522 PHE D N   
14782 C CA  . PHE H 11  ? 2.1058 2.1874 2.1202 0.8091  -0.6573 -0.3423 522 PHE D CA  
14783 C C   . PHE H 11  ? 2.1380 2.2414 2.1567 0.8109  -0.6363 -0.3224 522 PHE D C   
14784 O O   . PHE H 11  ? 2.1536 2.2620 2.1914 0.8073  -0.6409 -0.3021 522 PHE D O   
14785 C CB  . PHE H 11  ? 2.1118 2.1664 2.1011 0.8103  -0.6715 -0.3777 522 PHE D CB  
14786 C CG  . PHE H 11  ? 2.1013 2.1509 2.0492 0.8172  -0.6568 -0.4118 522 PHE D CG  
14787 C CD1 . PHE H 11  ? 2.0964 2.1426 2.0189 0.8212  -0.6504 -0.4361 522 PHE D CD1 
14788 C CD2 . PHE H 11  ? 2.1117 2.1610 2.0451 0.8193  -0.6499 -0.4195 522 PHE D CD2 
14789 C CE1 . PHE H 11  ? 2.0900 2.1336 1.9727 0.8265  -0.6380 -0.4669 522 PHE D CE1 
14790 C CE2 . PHE H 11  ? 2.1205 2.1666 2.0143 0.8248  -0.6372 -0.4504 522 PHE D CE2 
14791 C CZ  . PHE H 11  ? 2.1103 2.1541 1.9784 0.8281  -0.6316 -0.4738 522 PHE D CZ  
14792 N N   . LEU H 12  ? 2.0989 2.2151 2.0990 0.8163  -0.6133 -0.3285 523 LEU D N   
14793 C CA  . LEU H 12  ? 2.0815 2.2184 2.0833 0.8186  -0.5910 -0.3109 523 LEU D CA  
14794 C C   . LEU H 12  ? 2.1218 2.2797 2.1661 0.8132  -0.5899 -0.2652 523 LEU D C   
14795 O O   . LEU H 12  ? 2.1939 2.3657 2.2471 0.8131  -0.5785 -0.2467 523 LEU D O   
14796 C CB  . LEU H 12  ? 2.0819 2.2101 2.0631 0.8209  -0.5893 -0.3282 523 LEU D CB  
14797 C CG  . LEU H 12  ? 2.0824 2.1935 2.0181 0.8262  -0.5872 -0.3728 523 LEU D CG  
14798 C CD1 . LEU H 12  ? 2.0837 2.1873 2.0029 0.8277  -0.5870 -0.3860 523 LEU D CD1 
14799 C CD2 . LEU H 12  ? 2.0694 2.1931 1.9809 0.8312  -0.5647 -0.3828 523 LEU D CD2 
14800 N N   . GLY H 13  ? 1.6240 1.9028 2.3297 0.6161  0.1361  -0.1275 524 GLY D N   
14801 C CA  . GLY H 13  ? 1.6310 1.9268 2.3191 0.6187  0.1413  -0.1445 524 GLY D CA  
14802 C C   . GLY H 13  ? 1.6930 1.9955 2.3636 0.6297  0.1296  -0.1577 524 GLY D C   
14803 O O   . GLY H 13  ? 1.7417 2.0561 2.3991 0.6354  0.1254  -0.1714 524 GLY D O   
14804 N N   . ALA H 14  ? 1.6471 1.9423 2.3178 0.6331  0.1227  -0.1547 525 ALA D N   
14805 C CA  . ALA H 14  ? 1.7205 2.0217 2.3750 0.6442  0.1095  -0.1690 525 ALA D CA  
14806 C C   . ALA H 14  ? 1.7653 2.0528 2.4185 0.6524  0.0921  -0.1664 525 ALA D C   
14807 O O   . ALA H 14  ? 1.8019 2.0803 2.4517 0.6591  0.0792  -0.1663 525 ALA D O   
14808 C CB  . ALA H 14  ? 1.7164 2.0166 2.3709 0.6442  0.1099  -0.1679 525 ALA D CB  
14809 N N   . ALA H 15  ? 1.5295 1.8149 2.1855 0.6521  0.0908  -0.1639 526 ALA D N   
14810 C CA  . ALA H 15  ? 1.5769 1.8496 2.2322 0.6597  0.0736  -0.1612 526 ALA D CA  
14811 C C   . ALA H 15  ? 1.6658 1.9473 2.3005 0.6721  0.0578  -0.1847 526 ALA D C   
14812 O O   . ALA H 15  ? 1.7252 1.9946 2.3553 0.6810  0.0391  -0.1870 526 ALA D O   
14813 C CB  . ALA H 15  ? 1.5497 1.8189 2.2158 0.6553  0.0772  -0.1508 526 ALA D CB  
14814 N N   . GLY H 16  ? 1.5672 1.8703 2.1899 0.6731  0.0642  -0.2028 527 GLY D N   
14815 C CA  . GLY H 16  ? 1.6515 1.9698 2.2546 0.6845  0.0508  -0.2281 527 GLY D CA  
14816 C C   . GLY H 16  ? 1.6831 2.0156 2.2757 0.6889  0.0493  -0.2414 527 GLY D C   
14817 O O   . GLY H 16  ? 1.7592 2.1082 2.3352 0.6995  0.0372  -0.2644 527 GLY D O   
14818 N N   . SER H 17  ? 1.6754 2.0034 2.2776 0.6814  0.0609  -0.2282 528 SER D N   
14819 C CA  . SER H 17  ? 1.7177 2.0595 2.3115 0.6850  0.0603  -0.2390 528 SER D CA  
14820 C C   . SER H 17  ? 1.7649 2.0899 2.3551 0.6944  0.0409  -0.2398 528 SER D C   
14821 O O   . SER H 17  ? 1.7507 2.0516 2.3483 0.6956  0.0307  -0.2273 528 SER D O   
14822 C CB  . SER H 17  ? 1.6291 1.9730 2.2347 0.6729  0.0804  -0.2251 528 SER D CB  
14823 O OG  . SER H 17  ? 1.6303 1.9886 2.2382 0.6646  0.0966  -0.2254 528 SER D OG  
14824 N N   . THR H 18  ? 1.8248 2.1640 2.4037 0.7013  0.0351  -0.2547 529 THR D N   
14825 C CA  . THR H 18  ? 1.8770 2.2006 2.4514 0.7106  0.0160  -0.2570 529 THR D CA  
14826 C C   . THR H 18  ? 1.8157 2.1129 2.4072 0.7023  0.0211  -0.2304 529 THR D C   
14827 O O   . THR H 18  ? 1.7362 2.0321 2.3419 0.6901  0.0404  -0.2135 529 THR D O   
14828 C CB  . THR H 18  ? 1.9344 2.2817 2.4945 0.7187  0.0114  -0.2775 529 THR D CB  
14829 O OG1 . THR H 18  ? 1.8825 2.2519 2.4469 0.7089  0.0335  -0.2748 529 THR D OG1 
14830 C CG2 . THR H 18  ? 2.0300 2.3983 2.5705 0.7326  -0.0051 -0.3065 529 THR D CG2 
14831 N N   . MET H 19  ? 1.9940 2.2702 2.5842 0.7096  0.0021  -0.2275 530 MET D N   
14832 C CA  . MET H 19  ? 1.9230 2.1756 2.5288 0.7026  0.0050  -0.2022 530 MET D CA  
14833 C C   . MET H 19  ? 1.9576 2.2185 2.5674 0.6968  0.0187  -0.1980 530 MET D C   
14834 O O   . MET H 19  ? 1.8939 2.1442 2.5202 0.6862  0.0316  -0.1763 530 MET D O   
14835 C CB  . MET H 19  ? 1.9256 2.1553 2.5272 0.7120  -0.0198 -0.2011 530 MET D CB  
14836 C CG  . MET H 19  ? 1.9390 2.1556 2.5396 0.7166  -0.0350 -0.2010 530 MET D CG  
14837 S SD  . MET H 19  ? 1.9633 2.1520 2.5568 0.7281  -0.0675 -0.2022 530 MET D SD  
14838 C CE  . MET H 19  ? 2.0333 2.2044 2.6446 0.7181  -0.0587 -0.1709 530 MET D CE  
14839 N N   . GLY H 20  ? 1.9793 2.2607 2.5745 0.7041  0.0153  -0.2191 531 GLY D N   
14840 C CA  . GLY H 20  ? 2.0251 2.3173 2.6237 0.6988  0.0283  -0.2162 531 GLY D CA  
14841 C C   . GLY H 20  ? 2.0204 2.3257 2.6292 0.6860  0.0523  -0.2084 531 GLY D C   
14842 O O   . GLY H 20  ? 2.0093 2.3100 2.6304 0.6768  0.0652  -0.1939 531 GLY D O   
14843 N N   . ALA H 21  ? 1.8602 2.1814 2.4639 0.6856  0.0574  -0.2184 532 ALA D N   
14844 C CA  . ALA H 21  ? 1.8568 2.1898 2.4691 0.6738  0.0786  -0.2121 532 ALA D CA  
14845 C C   . ALA H 21  ? 1.7561 2.0651 2.3869 0.6636  0.0863  -0.1887 532 ALA D C   
14846 O O   . ALA H 21  ? 1.7397 2.0475 2.3830 0.6527  0.1019  -0.1769 532 ALA D O   
14847 C CB  . ALA H 21  ? 1.8927 2.2519 2.4926 0.6769  0.0806  -0.2310 532 ALA D CB  
14848 N N   . ALA H 22  ? 1.9706 2.2618 2.6036 0.6674  0.0746  -0.1824 533 ALA D N   
14849 C CA  . ALA H 22  ? 1.8607 2.1334 2.5116 0.6587  0.0806  -0.1608 533 ALA D CA  
14850 C C   . ALA H 22  ? 1.8002 2.0545 2.4660 0.6535  0.0814  -0.1412 533 ALA D C   
14851 O O   . ALA H 22  ? 1.7103 1.9534 2.3934 0.6450  0.0880  -0.1234 533 ALA D O   
14852 C CB  . ALA H 22  ? 1.8049 2.0674 2.4540 0.6646  0.0671  -0.1599 533 ALA D CB  
14853 N N   . SER H 23  ? 1.8348 2.0871 2.4944 0.6587  0.0738  -0.1448 534 SER D N   
14854 C CA  . SER H 23  ? 1.7725 2.0083 2.4454 0.6540  0.0741  -0.1269 534 SER D CA  
14855 C C   . SER H 23  ? 1.7745 2.0155 2.4592 0.6429  0.0914  -0.1208 534 SER D C   
14856 O O   . SER H 23  ? 1.6892 1.9167 2.3885 0.6370  0.0930  -0.1052 534 SER D O   
14857 C CB  . SER H 23  ? 1.8336 2.0657 2.4951 0.6635  0.0598  -0.1341 534 SER D CB  
14858 O OG  . SER H 23  ? 1.8324 2.0561 2.4838 0.6739  0.0406  -0.1402 534 SER D OG  
14859 N N   . MET H 24  ? 1.8473 2.1076 2.5265 0.6400  0.1031  -0.1330 535 MET D N   
14860 C CA  . MET H 24  ? 1.8757 2.1412 2.5652 0.6297  0.1181  -0.1292 535 MET D CA  
14861 C C   . MET H 24  ? 1.7666 2.0240 2.4724 0.6199  0.1261  -0.1182 535 MET D C   
14862 O O   . MET H 24  ? 1.7450 2.0004 2.4632 0.6110  0.1347  -0.1132 535 MET D O   
14863 C CB  . MET H 24  ? 2.0646 2.3568 2.7406 0.6311  0.1262  -0.1473 535 MET D CB  
14864 C CG  . MET H 24  ? 2.1711 2.4791 2.8285 0.6425  0.1163  -0.1644 535 MET D CG  
14865 S SD  . MET H 24  ? 2.3136 2.6138 2.9712 0.6463  0.1087  -0.1608 535 MET D SD  
14866 C CE  . MET H 24  ? 2.3660 2.6939 2.9996 0.6604  0.0976  -0.1878 535 MET D CE  
14867 N N   . THR H 25  ? 1.8743 2.1277 2.5807 0.6218  0.1219  -0.1158 536 THR D N   
14868 C CA  . THR H 25  ? 1.8166 2.0657 2.5373 0.6137  0.1281  -0.1081 536 THR D CA  
14869 C C   . THR H 25  ? 1.6613 1.8926 2.3935 0.6089  0.1183  -0.0916 536 THR D C   
14870 O O   . THR H 25  ? 1.5736 1.8028 2.3115 0.6032  0.1178  -0.0868 536 THR D O   
14871 C CB  . THR H 25  ? 1.8950 2.1559 2.6049 0.6165  0.1306  -0.1182 536 THR D CB  
14872 O OG1 . THR H 25  ? 1.7794 2.0374 2.5030 0.6085  0.1370  -0.1119 536 THR D OG1 
14873 C CG2 . THR H 25  ? 1.7994 2.0567 2.5000 0.6263  0.1173  -0.1201 536 THR D CG2 
14874 N N   . LEU H 26  ? 1.6298 1.8499 2.3643 0.6102  0.1098  -0.0830 537 LEU D N   
14875 C CA  . LEU H 26  ? 1.4783 1.6840 2.2222 0.6051  0.0990  -0.0671 537 LEU D CA  
14876 C C   . LEU H 26  ? 1.3875 1.5899 2.1436 0.5903  0.0997  -0.0623 537 LEU D C   
14877 O O   . LEU H 26  ? 1.3833 1.5820 2.1494 0.5854  0.0923  -0.0544 537 LEU D O   
14878 C CB  . LEU H 26  ? 1.4597 1.6548 2.2027 0.6096  0.0898  -0.0594 537 LEU D CB  
14879 C CG  . LEU H 26  ? 1.5550 1.7501 2.2879 0.6265  0.0821  -0.0647 537 LEU D CG  
14880 C CD1 . LEU H 26  ? 1.5419 1.7252 2.2744 0.6291  0.0730  -0.0561 537 LEU D CD1 
14881 C CD2 . LEU H 26  ? 1.5530 1.7453 2.2863 0.6325  0.0737  -0.0606 537 LEU D CD2 
14882 N N   . THR H 27  ? 1.6899 1.8952 2.4461 0.5839  0.1061  -0.0689 538 THR D N   
14883 C CA  . THR H 27  ? 1.5853 1.7878 2.3514 0.5729  0.1021  -0.0691 538 THR D CA  
14884 C C   . THR H 27  ? 1.5601 1.7708 2.3268 0.5700  0.1071  -0.0754 538 THR D C   
14885 O O   . THR H 27  ? 1.5166 1.7271 2.2878 0.5641  0.1026  -0.0786 538 THR D O   
14886 C CB  . THR H 27  ? 1.6145 1.8157 2.3791 0.5686  0.1045  -0.0744 538 THR D CB  
14887 O OG1 . THR H 27  ? 1.5470 1.7448 2.3173 0.5618  0.0957  -0.0767 538 THR D OG1 
14888 C CG2 . THR H 27  ? 1.7607 1.9733 2.5165 0.5703  0.1189  -0.0845 538 THR D CG2 
14889 N N   . VAL H 28  ? 1.3723 1.5906 2.1326 0.5760  0.1147  -0.0783 539 VAL D N   
14890 C CA  . VAL H 28  ? 1.3559 1.5821 2.1160 0.5738  0.1202  -0.0837 539 VAL D CA  
14891 C C   . VAL H 28  ? 1.2845 1.5093 2.0519 0.5745  0.1121  -0.0767 539 VAL D C   
14892 O O   . VAL H 28  ? 1.2505 1.4783 2.0240 0.5697  0.1092  -0.0780 539 VAL D O   
14893 C CB  . VAL H 28  ? 1.5109 1.7486 2.2591 0.5799  0.1328  -0.0934 539 VAL D CB  
14894 C CG1 . VAL H 28  ? 1.4853 1.7304 2.2331 0.5778  0.1383  -0.0981 539 VAL D CG1 
14895 C CG2 . VAL H 28  ? 1.6122 1.8543 2.3551 0.5785  0.1405  -0.1004 539 VAL D CG2 
14896 N N   . GLN H 29  ? 1.3507 1.5718 2.1166 0.5818  0.1072  -0.0697 540 GLN D N   
14897 C CA  . GLN H 29  ? 1.3512 1.5708 2.1251 0.5825  0.0983  -0.0609 540 GLN D CA  
14898 C C   . GLN H 29  ? 1.3448 1.5586 2.1331 0.5754  0.0846  -0.0526 540 GLN D C   
14899 O O   . GLN H 29  ? 1.3416 1.5578 2.1397 0.5734  0.0758  -0.0475 540 GLN D O   
14900 C CB  . GLN H 29  ? 1.3647 1.5814 2.1306 0.5945  0.0948  -0.0567 540 GLN D CB  
14901 C CG  . GLN H 29  ? 1.3714 1.5977 2.1249 0.6037  0.1027  -0.0691 540 GLN D CG  
14902 C CD  . GLN H 29  ? 1.3755 1.6079 2.1177 0.6086  0.1108  -0.0821 540 GLN D CD  
14903 O OE1 . GLN H 29  ? 1.3754 1.6194 2.1106 0.6109  0.1201  -0.0945 540 GLN D OE1 
14904 N NE2 . GLN H 29  ? 1.3789 1.6049 2.1201 0.6102  0.1072  -0.0793 540 GLN D NE2 
14905 N N   . ALA H 30  ? 1.4050 1.6128 2.1944 0.5721  0.0810  -0.0526 541 ALA D N   
14906 C CA  . ALA H 30  ? 1.3804 1.5845 2.1804 0.5671  0.0649  -0.0487 541 ALA D CA  
14907 C C   . ALA H 30  ? 1.3299 1.5423 2.1288 0.5641  0.0617  -0.0589 541 ALA D C   
14908 O O   . ALA H 30  ? 1.3226 1.5387 2.1246 0.5646  0.0476  -0.0577 541 ALA D O   
14909 C CB  . ALA H 30  ? 1.3825 1.5770 2.1808 0.5666  0.0615  -0.0456 541 ALA D CB  
14910 N N   . ARG H 31  ? 1.4655 1.6820 2.2566 0.5634  0.0748  -0.0679 542 ARG D N   
14911 C CA  . ARG H 31  ? 1.4560 1.6788 2.2422 0.5627  0.0752  -0.0756 542 ARG D CA  
14912 C C   . ARG H 31  ? 1.4553 1.6882 2.2442 0.5642  0.0741  -0.0758 542 ARG D C   
14913 O O   . ARG H 31  ? 1.4309 1.6699 2.2187 0.5668  0.0665  -0.0751 542 ARG D O   
14914 C CB  . ARG H 31  ? 1.4264 1.6493 2.2051 0.5610  0.0899  -0.0832 542 ARG D CB  
14915 C CG  . ARG H 31  ? 1.4319 1.6486 2.2056 0.5596  0.0892  -0.0862 542 ARG D CG  
14916 C CD  . ARG H 31  ? 1.5561 1.7752 2.3241 0.5581  0.1042  -0.0926 542 ARG D CD  
14917 N NE  . ARG H 31  ? 1.5842 1.8098 2.3485 0.5573  0.1124  -0.0989 542 ARG D NE  
14918 C CZ  . ARG H 31  ? 1.5954 1.8266 2.3552 0.5569  0.1257  -0.1036 542 ARG D CZ  
14919 N NH1 . ARG H 31  ? 1.6929 1.9253 2.4498 0.5589  0.1319  -0.1029 542 ARG D NH1 
14920 N NH2 . ARG H 31  ? 1.5841 1.8207 2.3407 0.5558  0.1327  -0.1089 542 ARG D NH2 
14921 N N   . ASN H 32  ? 1.6956 1.9316 2.4865 0.5642  0.0825  -0.0755 543 ASN D N   
14922 C CA  . ASN H 32  ? 1.6914 1.9373 2.4853 0.5654  0.0820  -0.0759 543 ASN D CA  
14923 C C   . ASN H 32  ? 1.7533 2.0009 2.5573 0.5669  0.0692  -0.0670 543 ASN D C   
14924 O O   . ASN H 32  ? 1.7881 2.0426 2.5962 0.5679  0.0701  -0.0657 543 ASN D O   
14925 C CB  . ASN H 32  ? 1.7042 1.9535 2.4933 0.5654  0.0968  -0.0808 543 ASN D CB  
14926 C CG  . ASN H 32  ? 1.7173 1.9659 2.4971 0.5636  0.1082  -0.0892 543 ASN D CG  
14927 O OD1 . ASN H 32  ? 1.7064 1.9532 2.4800 0.5642  0.1182  -0.0918 543 ASN D OD1 
14928 N ND2 . ASN H 32  ? 1.7366 1.9874 2.5140 0.5629  0.1064  -0.0930 543 ASN D ND2 
14929 N N   . LEU H 33  ? 1.4162 1.6577 2.2247 0.5671  0.0565  -0.0607 544 LEU D N   
14930 C CA  . LEU H 33  ? 1.4234 1.6656 2.2422 0.5681  0.0423  -0.0513 544 LEU D CA  
14931 C C   . LEU H 33  ? 1.4144 1.6692 2.2322 0.5717  0.0294  -0.0508 544 LEU D C   
14932 O O   . LEU H 33  ? 1.4900 1.7523 2.3148 0.5734  0.0193  -0.0452 544 LEU D O   
14933 C CB  . LEU H 33  ? 1.4888 1.7175 2.3121 0.5671  0.0349  -0.0425 544 LEU D CB  
14934 C CG  . LEU H 33  ? 1.6154 1.8402 2.4508 0.5673  0.0217  -0.0291 544 LEU D CG  
14935 C CD1 . LEU H 33  ? 1.6840 1.9095 2.5209 0.5699  0.0323  -0.0225 544 LEU D CD1 
14936 C CD2 . LEU H 33  ? 1.6649 1.8752 2.5027 0.5668  0.0171  -0.0181 544 LEU D CD2 
14937 N N   . LEU H 34  ? 1.2253 2.8005 1.8062 0.6245  0.1304  0.0487  545 LEU D N   
14938 C CA  . LEU H 34  ? 1.2170 2.7790 1.7721 0.6224  0.1185  0.0602  545 LEU D CA  
14939 C C   . LEU H 34  ? 1.2088 2.7463 1.7667 0.6209  0.1116  0.0801  545 LEU D C   
14940 O O   . LEU H 34  ? 1.1995 2.7113 1.7540 0.6187  0.0993  0.0865  545 LEU D O   
14941 C CB  . LEU H 34  ? 1.2231 2.8134 1.7411 0.6221  0.1228  0.0625  545 LEU D CB  
14942 C CG  . LEU H 34  ? 1.2158 2.7965 1.7061 0.6199  0.1116  0.0725  545 LEU D CG  
14943 C CD1 . LEU H 34  ? 1.2092 2.7726 1.7071 0.6186  0.1020  0.0608  545 LEU D CD1 
14944 C CD2 . LEU H 34  ? 1.2233 2.8352 1.6805 0.6203  0.1165  0.0730  545 LEU D CD2 
14945 N N   . SER H 35  ? 1.5620 3.1073 2.1262 0.6218  0.1196  0.0896  546 SER D N   
14946 C CA  . SER H 35  ? 1.6110 3.1355 2.1799 0.6207  0.1148  0.1082  546 SER D CA  
14947 C C   . SER H 35  ? 1.6300 3.1428 2.1691 0.6185  0.1053  0.1241  546 SER D C   
14948 O O   . SER H 35  ? 1.6241 3.1073 2.1667 0.6160  0.0936  0.1283  546 SER D O   
14949 C CB  . SER H 35  ? 1.6316 3.1251 2.2362 0.6200  0.1076  0.1053  546 SER D CB  
14950 O OG  . SER H 35  ? 1.6551 3.1590 2.2902 0.6223  0.1168  0.0913  546 SER D OG  
14951 N N   . GLY H 36  ? 1.7326 3.2682 2.2428 0.6193  0.1103  0.1329  547 GLY D N   
14952 C CA  . GLY H 36  ? 1.6700 3.1967 2.1521 0.6177  0.1022  0.1476  547 GLY D CA  
14953 C C   . GLY H 36  ? 1.6163 3.1399 2.0809 0.6160  0.0944  0.1404  547 GLY D C   
14954 O O   . GLY H 36  ? 1.5653 3.0623 2.0269 0.6131  0.0838  0.1461  547 GLY D O   
14955 N N   . THR H 58  ? 1.7513 2.8123 2.2395 0.5451  -0.0982 0.1727  569 THR D N   
14956 C CA  . THR H 58  ? 1.7686 2.8002 2.2822 0.5450  -0.1068 0.1775  569 THR D CA  
14957 C C   . THR H 58  ? 1.7728 2.8177 2.3092 0.5510  -0.1044 0.1671  569 THR D C   
14958 O O   . THR H 58  ? 1.7428 2.8151 2.2771 0.5552  -0.0920 0.1628  569 THR D O   
14959 C CB  . THR H 58  ? 1.7317 2.7461 2.2463 0.5427  -0.1036 0.1916  569 THR D CB  
14960 O OG1 . THR H 58  ? 1.5933 2.6343 2.1025 0.5465  -0.0894 0.1918  569 THR D OG1 
14961 C CG2 . THR H 58  ? 1.7910 2.7890 2.2851 0.5366  -0.1069 0.2015  569 THR D CG2 
14962 N N   . VAL H 59  ? 1.9503 2.9751 2.5085 0.5517  -0.1167 0.1631  570 VAL D N   
14963 C CA  . VAL H 59  ? 2.0013 3.0366 2.5839 0.5577  -0.1158 0.1520  570 VAL D CA  
14964 C C   . VAL H 59  ? 1.8840 2.9150 2.4859 0.5598  -0.1097 0.1578  570 VAL D C   
14965 O O   . VAL H 59  ? 1.7338 2.7555 2.3278 0.5567  -0.1060 0.1700  570 VAL D O   
14966 C CB  . VAL H 59  ? 2.1222 3.1349 2.7222 0.5578  -0.1326 0.1465  570 VAL D CB  
14967 C CG1 . VAL H 59  ? 2.1717 3.2018 2.7917 0.5645  -0.1311 0.1316  570 VAL D CG1 
14968 C CG2 . VAL H 59  ? 2.2031 3.2128 2.7816 0.5539  -0.1408 0.1451  570 VAL D CG2 
14969 N N   . TRP H 60  ? 1.9845 3.0230 2.6124 0.5653  -0.1085 0.1485  571 TRP D N   
14970 C CA  . TRP H 60  ? 1.8947 2.9329 2.5450 0.5681  -0.1025 0.1512  571 TRP D CA  
14971 C C   . TRP H 60  ? 1.7666 2.8342 2.4011 0.5698  -0.0853 0.1538  571 TRP D C   
14972 O O   . TRP H 60  ? 1.6503 2.7302 2.3012 0.5737  -0.0770 0.1519  571 TRP D O   
14973 C CB  . TRP H 60  ? 1.8933 2.8948 2.5558 0.5637  -0.1124 0.1642  571 TRP D CB  
14974 C CG  . TRP H 60  ? 1.9380 2.9346 2.6321 0.5670  -0.1112 0.1636  571 TRP D CG  
14975 C CD1 . TRP H 60  ? 1.9962 2.9978 2.7198 0.5724  -0.1131 0.1520  571 TRP D CD1 
14976 C CD2 . TRP H 60  ? 1.9131 2.9004 2.6130 0.5653  -0.1074 0.1744  571 TRP D CD2 
14977 N NE1 . TRP H 60  ? 1.9805 2.9769 2.7293 0.5741  -0.1106 0.1548  571 TRP D NE1 
14978 C CE2 . TRP H 60  ? 1.9231 2.9109 2.6572 0.5697  -0.1072 0.1685  571 TRP D CE2 
14979 C CE3 . TRP H 60  ? 1.8873 2.8661 2.5670 0.5606  -0.1043 0.1881  571 TRP D CE3 
14980 C CZ2 . TRP H 60  ? 1.8863 2.8673 2.6345 0.5694  -0.1041 0.1758  571 TRP D CZ2 
14981 C CZ3 . TRP H 60  ? 1.8625 2.8339 2.5552 0.5603  -0.1015 0.1956  571 TRP D CZ3 
14982 C CH2 . TRP H 60  ? 1.8595 2.8324 2.5859 0.5646  -0.1015 0.1894  571 TRP D CH2 
14983 N N   . GLY H 61  ? 1.8627 2.9418 2.4659 0.5670  -0.0803 0.1582  572 GLY D N   
14984 C CA  . GLY H 61  ? 1.7435 2.8516 2.3288 0.5689  -0.0653 0.1602  572 GLY D CA  
14985 C C   . GLY H 61  ? 1.7831 2.9241 2.3573 0.5725  -0.0585 0.1464  572 GLY D C   
14986 O O   . GLY H 61  ? 1.7972 2.9669 2.3618 0.5756  -0.0461 0.1437  572 GLY D O   
14987 N N   . ILE H 62  ? 1.4718 2.6082 2.0458 0.5718  -0.0675 0.1375  573 ILE D N   
14988 C CA  . ILE H 62  ? 1.5218 2.6874 2.0874 0.5749  -0.0631 0.1224  573 ILE D CA  
14989 C C   . ILE H 62  ? 1.5956 2.7700 2.1881 0.5807  -0.0615 0.1096  573 ILE D C   
14990 O O   . ILE H 62  ? 1.6641 2.8658 2.2521 0.5841  -0.0554 0.0962  573 ILE D O   
14991 C CB  . ILE H 62  ? 1.6591 2.8162 2.2127 0.5716  -0.0739 0.1182  573 ILE D CB  
14992 C CG1 . ILE H 62  ? 1.7211 2.9113 2.2577 0.5735  -0.0682 0.1043  573 ILE D CG1 
14993 C CG2 . ILE H 62  ? 1.7258 2.8558 2.3049 0.5720  -0.0887 0.1144  573 ILE D CG2 
14994 C CD1 . ILE H 62  ? 1.7531 2.9385 2.2777 0.5701  -0.0785 0.0992  573 ILE D CD1 
14995 N N   . LYS H 63  ? 1.5189 2.6713 2.1400 0.5817  -0.0667 0.1131  574 LYS D N   
14996 C CA  . LYS H 63  ? 1.5819 2.7414 2.2321 0.5874  -0.0652 0.1010  574 LYS D CA  
14997 C C   . LYS H 63  ? 1.5392 2.7317 2.1869 0.5915  -0.0483 0.0964  574 LYS D C   
14998 O O   . LYS H 63  ? 1.6110 2.8238 2.2693 0.5962  -0.0431 0.0817  574 LYS D O   
14999 C CB  . LYS H 63  ? 1.5951 2.7233 2.2769 0.5873  -0.0746 0.1069  574 LYS D CB  
15000 C CG  . LYS H 63  ? 1.6060 2.7322 2.3209 0.5928  -0.0795 0.0930  574 LYS D CG  
15001 C CD  . LYS H 63  ? 1.7160 2.8300 2.4304 0.5926  -0.0941 0.0846  574 LYS D CD  
15002 C CE  . LYS H 63  ? 1.6235 2.7298 2.3730 0.5981  -0.1015 0.0722  574 LYS D CE  
15003 N NZ  . LYS H 63  ? 1.7021 2.7942 2.4507 0.5982  -0.1177 0.0645  574 LYS D NZ  
15004 N N   . GLN H 64  ? 1.6196 2.8175 2.2532 0.5897  -0.0399 0.1088  575 GLN D N   
15005 C CA  . GLN H 64  ? 1.5477 2.7755 2.1767 0.5930  -0.0245 0.1072  575 GLN D CA  
15006 C C   . GLN H 64  ? 1.5946 2.8529 2.1918 0.5933  -0.0161 0.1026  575 GLN D C   
15007 O O   . GLN H 64  ? 1.6360 2.9229 2.2308 0.5969  -0.0042 0.0960  575 GLN D O   
15008 C CB  . GLN H 64  ? 1.4280 2.6471 2.0555 0.5912  -0.0204 0.1234  575 GLN D CB  
15009 C CG  . GLN H 64  ? 1.3982 2.6017 1.9998 0.5857  -0.0253 0.1379  575 GLN D CG  
15010 C CD  . GLN H 64  ? 1.3693 2.5997 1.9375 0.5856  -0.0157 0.1407  575 GLN D CD  
15011 O OE1 . GLN H 64  ? 1.3925 2.6524 1.9567 0.5894  -0.0046 0.1349  575 GLN D OE1 
15012 N NE2 . GLN H 64  ? 1.3823 2.6027 1.9268 0.5811  -0.0203 0.1491  575 GLN D NE2 
15013 N N   . LEU H 65  ? 1.4838 2.1657 1.7628 0.0256  0.5175  -0.0234 576 LEU D N   
15014 C CA  . LEU H 65  ? 1.4941 2.1677 1.7754 0.0126  0.5205  -0.0062 576 LEU D CA  
15015 C C   . LEU H 65  ? 1.5883 2.2404 1.8676 0.0016  0.5181  0.0131  576 LEU D C   
15016 O O   . LEU H 65  ? 1.5426 2.1641 1.8130 0.0016  0.5158  0.0216  576 LEU D O   
15017 C CB  . LEU H 65  ? 1.5184 2.2150 1.8154 0.0001  0.5287  0.0009  576 LEU D CB  
15018 C CG  . LEU H 65  ? 1.4926 2.1809 1.7926 -0.0101 0.5306  0.0222  576 LEU D CG  
15019 C CD1 . LEU H 65  ? 1.5021 2.2069 1.8110 -0.0075 0.5380  0.0201  576 LEU D CD1 
15020 C CD2 . LEU H 65  ? 1.5556 2.2393 1.8643 -0.0243 0.5308  0.0530  576 LEU D CD2 
15021 N N   . GLN H 66  ? 1.5649 2.2281 1.8527 -0.0083 0.5194  0.0211  577 GLN D N   
15022 C CA  . GLN H 66  ? 1.6724 2.3166 1.9581 -0.0205 0.5164  0.0415  577 GLN D CA  
15023 C C   . GLN H 66  ? 1.6791 2.2902 1.9490 -0.0075 0.5118  0.0331  577 GLN D C   
15024 O O   . GLN H 66  ? 1.7682 2.3540 2.0327 -0.0166 0.5095  0.0486  577 GLN D O   
15025 C CB  . GLN H 66  ? 1.8523 2.5119 2.1514 -0.0320 0.5189  0.0555  577 GLN D CB  
15026 C CG  . GLN H 66  ? 1.9526 2.6189 2.2510 -0.0242 0.5182  0.0401  577 GLN D CG  
15027 C CD  . GLN H 66  ? 2.1298 2.8051 2.4425 -0.0363 0.5203  0.0627  577 GLN D CD  
15028 O OE1 . GLN H 66  ? 2.1578 2.8349 2.4803 -0.0478 0.5198  0.0941  577 GLN D OE1 
15029 N NE2 . GLN H 66  ? 2.2565 2.9388 2.5710 -0.0311 0.5206  0.0511  577 GLN D NE2 
15030 N N   . ALA H 67  ? 1.8623 2.4653 2.1245 0.0139  0.5114  0.0106  578 ALA D N   
15031 C CA  . ALA H 67  ? 1.7764 2.3313 2.0237 0.0290  0.5108  0.0008  578 ALA D CA  
15032 C C   . ALA H 67  ? 1.6447 2.1551 1.8819 0.0325  0.5128  -0.0002 578 ALA D C   
15033 O O   . ALA H 67  ? 1.6703 2.1344 1.8968 0.0328  0.5137  0.0009  578 ALA D O   
15034 C CB  . ALA H 67  ? 1.7031 2.2569 1.9464 0.0479  0.5109  -0.0212 578 ALA D CB  
15035 N N   . ARG H 68  ? 1.7711 2.2937 2.0114 0.0344  0.5140  -0.0036 579 ARG D N   
15036 C CA  . ARG H 68  ? 1.6630 2.1445 1.8950 0.0366  0.5163  -0.0057 579 ARG D CA  
15037 C C   . ARG H 68  ? 1.7138 2.1966 1.9488 0.0196  0.5152  0.0169  579 ARG D C   
15038 O O   . ARG H 68  ? 1.6778 2.1219 1.9051 0.0191  0.5169  0.0178  579 ARG D O   
15039 C CB  . ARG H 68  ? 1.5411 2.0356 1.7751 0.0452  0.5178  -0.0179 579 ARG D CB  
15040 C CG  . ARG H 68  ? 1.5691 2.1201 1.8156 0.0373  0.5170  -0.0091 579 ARG D CG  
15041 C CD  . ARG H 68  ? 1.5363 2.0896 1.7811 0.0485  0.5188  -0.0232 579 ARG D CD  
15042 N NE  . ARG H 68  ? 1.5160 2.1186 1.7713 0.0414  0.5193  -0.0187 579 ARG D NE  
15043 C CZ  . ARG H 68  ? 1.3681 1.9699 1.6229 0.0425  0.5210  -0.0196 579 ARG D CZ  
15044 N NH1 . ARG H 68  ? 1.2518 1.8043 1.4965 0.0495  0.5222  -0.0243 579 ARG D NH1 
15045 N NH2 . ARG H 68  ? 1.3518 1.9965 1.6166 0.0346  0.5230  -0.0181 579 ARG D NH2 
15046 N N   . VAL H 69  ? 1.4192 1.9431 1.6655 0.0032  0.5127  0.0352  580 VAL D N   
15047 C CA  . VAL H 69  ? 1.4194 1.9403 1.6681 -0.0173 0.5106  0.0606  580 VAL D CA  
15048 C C   . VAL H 69  ? 1.4209 1.9035 1.6592 -0.0201 0.5088  0.0669  580 VAL D C   
15049 O O   . VAL H 69  ? 1.4247 1.8750 1.6556 -0.0285 0.5078  0.0791  580 VAL D O   
15050 C CB  . VAL H 69  ? 1.4201 1.9853 1.6843 -0.0367 0.5100  0.0785  580 VAL D CB  
15051 C CG1 . VAL H 69  ? 1.4256 1.9780 1.6907 -0.0603 0.5060  0.1090  580 VAL D CG1 
15052 C CG2 . VAL H 69  ? 1.4231 2.0142 1.6959 -0.0361 0.5136  0.0757  580 VAL D CG2 
15053 N N   . LEU H 70  ? 1.5767 2.0613 1.8136 -0.0132 0.5087  0.0580  581 LEU D N   
15054 C CA  . LEU H 70  ? 1.6525 2.0987 1.8777 -0.0133 0.5082  0.0604  581 LEU D CA  
15055 C C   . LEU H 70  ? 1.6006 1.9856 1.8089 0.0044  0.5128  0.0394  581 LEU D C   
15056 O O   . LEU H 70  ? 1.6572 1.9824 1.8571 0.0049  0.5255  0.0449  581 LEU D O   
15057 C CB  . LEU H 70  ? 1.7453 2.2053 1.9750 -0.0070 0.5108  0.0548  581 LEU D CB  
15058 C CG  . LEU H 70  ? 1.8590 2.2591 2.0863 0.0002  0.5299  0.0638  581 LEU D CG  
15059 C CD1 . LEU H 70  ? 2.0406 2.4236 2.2830 -0.0181 0.5440  0.1108  581 LEU D CD1 
15060 C CD2 . LEU H 70  ? 1.9040 2.3223 2.1307 0.0128  0.5271  0.0445  581 LEU D CD2 
15061 N N   . ALA H 71  ? 1.7248 2.1015 1.9319 0.0190  0.5159  0.0187  582 ALA D N   
15062 C CA  . ALA H 71  ? 1.6627 1.9775 1.8541 0.0307  0.5202  -0.0022 582 ALA D CA  
15063 C C   . ALA H 71  ? 1.6249 1.9092 1.8102 0.0216  0.5214  0.0086  582 ALA D C   
15064 O O   . ALA H 71  ? 1.6451 1.8742 1.8146 0.0244  0.5242  0.0003  582 ALA D O   
15065 C CB  . ALA H 71  ? 1.5583 1.8744 1.7516 0.0420  0.5220  -0.0221 582 ALA D CB  
15066 N N   . VAL H 72  ? 1.4929 1.8129 1.6898 0.0104  0.5190  0.0270  583 VAL D N   
15067 C CA  . VAL H 72  ? 1.4396 1.7349 1.6318 0.0007  0.5192  0.0392  583 VAL D CA  
15068 C C   . VAL H 72  ? 1.5275 1.8147 1.7191 -0.0166 0.5193  0.0664  583 VAL D C   
15069 O O   . VAL H 72  ? 1.5288 1.7630 1.7139 -0.0213 0.5297  0.0762  583 VAL D O   
15070 C CB  . VAL H 72  ? 1.3406 1.6729 1.5451 -0.0048 0.5178  0.0486  583 VAL D CB  
15071 C CG1 . VAL H 72  ? 1.2601 1.5888 1.4645 0.0109  0.5216  0.0245  583 VAL D CG1 
15072 C CG2 . VAL H 72  ? 1.3789 1.7750 1.5992 -0.0198 0.5126  0.0706  583 VAL D CG2 
15073 N N   . GLU H 73  ? 1.4057 1.7175 1.6099 -0.0240 0.5239  0.0846  584 GLU D N   
15074 C CA  . GLU H 73  ? 1.5219 1.7948 1.7325 -0.0377 0.5400  0.1209  584 GLU D CA  
15075 C C   . GLU H 73  ? 1.6033 1.7967 1.7969 -0.0259 0.5588  0.1083  584 GLU D C   
15076 O O   . GLU H 73  ? 1.6545 1.7887 1.8413 -0.0355 0.5727  0.1310  584 GLU D O   
15077 C CB  . GLU H 73  ? 1.6156 1.9337 1.8444 -0.0486 0.5378  0.1460  584 GLU D CB  
15078 C CG  . GLU H 73  ? 1.6245 2.0093 1.8680 -0.0659 0.5232  0.1632  584 GLU D CG  
15079 C CD  . GLU H 73  ? 1.7951 2.2129 2.0552 -0.0750 0.5222  0.1863  584 GLU D CD  
15080 O OE1 . GLU H 73  ? 1.8318 2.2341 2.0917 -0.0645 0.5307  0.1813  584 GLU D OE1 
15081 O OE2 . GLU H 73  ? 1.8865 2.3415 2.1594 -0.0913 0.5135  0.2088  584 GLU D OE2 
15082 N N   . ARG H 74  ? 1.7221 1.9114 1.9053 -0.0069 0.5572  0.0724  585 ARG D N   
15083 C CA  . ARG H 74  ? 1.7912 1.9049 1.9532 0.0053  0.5732  0.0528  585 ARG D CA  
15084 C C   . ARG H 74  ? 1.7198 1.7792 1.8625 0.0095  0.5751  0.0352  585 ARG D C   
15085 O O   . ARG H 74  ? 1.7888 1.7722 1.9107 0.0123  0.5934  0.0306  585 ARG D O   
15086 C CB  . ARG H 74  ? 1.7967 1.9288 1.9543 0.0219  0.5645  0.0227  585 ARG D CB  
15087 C CG  . ARG H 74  ? 1.8609 1.9204 1.9945 0.0349  0.5766  -0.0006 585 ARG D CG  
15088 C CD  . ARG H 74  ? 1.9218 1.9971 2.0584 0.0432  0.5780  -0.0069 585 ARG D CD  
15089 N NE  . ARG H 74  ? 1.9847 1.9939 2.0962 0.0565  0.5873  -0.0296 585 ARG D NE  
15090 C CZ  . ARG H 74  ? 2.0241 2.0363 2.1328 0.0668  0.5873  -0.0412 585 ARG D CZ  
15091 N NH1 . ARG H 74  ? 2.0063 2.0831 2.1368 0.0647  0.5804  -0.0315 585 ARG D NH1 
15092 N NH2 . ARG H 74  ? 2.0745 2.0261 2.1570 0.0796  0.5922  -0.0624 585 ARG D NH2 
15093 N N   . TYR H 75  ? 1.9148 2.0106 2.0613 0.0101  0.5565  0.0254  586 TYR D N   
15094 C CA  . TYR H 75  ? 1.8368 1.8851 1.9673 0.0130  0.5564  0.0109  586 TYR D CA  
15095 C C   . TYR H 75  ? 1.8682 1.8769 1.9973 -0.0013 0.5722  0.0380  586 TYR D C   
15096 O O   . TYR H 75  ? 1.9112 1.8449 2.0192 0.0000  0.5879  0.0324  586 TYR D O   
15097 C CB  . TYR H 75  ? 1.6764 1.7765 1.8113 0.0171  0.5313  -0.0031 586 TYR D CB  
15098 C CG  . TYR H 75  ? 1.5951 1.6444 1.7185 0.0180  0.5352  -0.0138 586 TYR D CG  
15099 C CD1 . TYR H 75  ? 1.5854 1.5800 1.6926 0.0265  0.5388  -0.0378 586 TYR D CD1 
15100 C CD2 . TYR H 75  ? 1.5254 1.5838 1.6549 0.0086  0.5343  0.0015  586 TYR D CD2 
15101 C CE1 . TYR H 75  ? 1.5149 1.4647 1.6123 0.0248  0.5420  -0.0459 586 TYR D CE1 
15102 C CE2 . TYR H 75  ? 1.4513 1.4632 1.5704 0.0092  0.5380  -0.0084 586 TYR D CE2 
15103 C CZ  . TYR H 75  ? 1.4494 1.4067 1.5526 0.0168  0.5420  -0.0320 586 TYR D CZ  
15104 O OH  . TYR H 75  ? 1.3793 1.2924 1.4730 0.0149  0.5453  -0.0399 586 TYR D OH  
15105 N N   . LEU H 76  ? 1.4872 1.5462 1.6362 -0.0165 0.5660  0.0694  587 LEU D N   
15106 C CA  . LEU H 76  ? 1.5031 1.5311 1.6523 -0.0341 0.5735  0.1019  587 LEU D CA  
15107 C C   . LEU H 76  ? 1.6455 1.6136 1.7852 -0.0452 0.5909  0.1295  587 LEU D C   
15108 O O   . LEU H 76  ? 1.6621 1.5725 1.7879 -0.0589 0.5960  0.1512  587 LEU D O   
15109 C CB  . LEU H 76  ? 1.4791 1.5801 1.6511 -0.0503 0.5558  0.1309  587 LEU D CB  
15110 C CG  . LEU H 76  ? 1.4396 1.5838 1.6123 -0.0417 0.5398  0.1059  587 LEU D CG  
15111 C CD1 . LEU H 76  ? 1.4209 1.6312 1.6099 -0.0581 0.5246  0.1301  587 LEU D CD1 
15112 C CD2 . LEU H 76  ? 1.4491 1.5332 1.6039 -0.0345 0.5453  0.0873  587 LEU D CD2 
15113 N N   . ARG H 77  ? 1.7400 1.7170 1.8836 -0.0418 0.5965  0.1320  588 ARG D N   
15114 C CA  . ARG H 77  ? 1.8908 1.8013 2.0191 -0.0542 0.6100  0.1611  588 ARG D CA  
15115 C C   . ARG H 77  ? 1.9300 1.7440 2.0171 -0.0428 0.6316  0.1331  588 ARG D C   
15116 O O   . ARG H 77  ? 1.9868 1.7240 2.0443 -0.0560 0.6075  0.1537  588 ARG D O   
15117 C CB  . ARG H 77  ? 1.9885 1.9276 2.1282 -0.0510 0.6125  0.1676  588 ARG D CB  
15118 C CG  . ARG H 77  ? 2.0306 1.9370 2.1490 -0.0250 0.6306  0.1219  588 ARG D CG  
15119 C CD  . ARG H 77  ? 2.1915 2.1236 2.3217 -0.0246 0.6331  0.1347  588 ARG D CD  
15120 N NE  . ARG H 77  ? 2.2643 2.1743 2.3755 0.0025  0.6433  0.0867  588 ARG D NE  
15121 C CZ  . ARG H 77  ? 2.3343 2.1682 2.4084 0.0108  0.6254  0.0758  588 ARG D CZ  
15122 N NH1 . ARG H 77  ? 2.4591 2.2270 2.5070 -0.0057 0.5770  0.1063  588 ARG D NH1 
15123 N NH2 . ARG H 77  ? 2.2835 2.1062 2.3449 0.0364  0.6454  0.0332  588 ARG D NH2 
15124 N N   . ASP H 78  ? 2.0110 1.8258 2.0886 -0.0153 0.6366  0.0800  589 ASP D N   
15125 C CA  . ASP H 78  ? 2.0383 1.7692 2.0765 -0.0008 0.6520  0.0483  589 ASP D CA  
15126 C C   . ASP H 78  ? 1.9533 1.6542 1.9819 -0.0075 0.6507  0.0497  589 ASP D C   
15127 O O   . ASP H 78  ? 2.0055 1.6212 1.9953 -0.0077 0.6677  0.0470  589 ASP D O   
15128 C CB  . ASP H 78  ? 1.9831 1.7334 2.0201 0.0226  0.6369  0.0019  589 ASP D CB  
15129 C CG  . ASP H 78  ? 2.0707 1.8320 2.1079 0.0321  0.6399  -0.0045 589 ASP D CG  
15130 O OD1 . ASP H 78  ? 2.2004 1.9168 2.2202 0.0286  0.6632  0.0148  589 ASP D OD1 
15131 O OD2 . ASP H 78  ? 2.0039 1.8192 2.0560 0.0412  0.6178  -0.0252 589 ASP D OD2 
15132 N N   . GLN H 79  ? 2.0237 1.7910 2.0818 -0.0125 0.6306  0.0538  590 GLN D N   
15133 C CA  . GLN H 79  ? 1.9276 1.6721 1.9793 -0.0183 0.6280  0.0554  590 GLN D CA  
15134 C C   . GLN H 79  ? 1.9822 1.6869 2.0253 -0.0442 0.6314  0.1023  590 GLN D C   
15135 O O   . GLN H 79  ? 1.9611 1.6055 1.9804 -0.0496 0.6354  0.1039  590 GLN D O   
15136 C CB  . GLN H 79  ? 1.7671 1.5926 1.8476 -0.0179 0.6037  0.0511  590 GLN D CB  
15137 C CG  . GLN H 79  ? 1.6318 1.4818 1.7120 -0.0015 0.5868  0.0136  590 GLN D CG  
15138 C CD  . GLN H 79  ? 1.6773 1.4630 1.7329 0.0052  0.5893  -0.0101 590 GLN D CD  
15139 O OE1 . GLN H 79  ? 1.7444 1.5273 1.7919 0.0152  0.5779  -0.0344 590 GLN D OE1 
15140 N NE2 . GLN H 79  ? 1.6336 1.3719 1.6774 -0.0023 0.6013  0.0005  590 GLN D NE2 
15141 N N   . GLN H 80  ? 1.7836 1.5180 1.8446 -0.0641 0.6190  0.1453  591 GLN D N   
15142 C CA  . GLN H 80  ? 1.8443 1.5320 1.8959 -0.0953 0.5961  0.1994  591 GLN D CA  
15143 C C   . GLN H 80  ? 1.9812 1.5599 1.9808 -0.0908 0.5619  0.1907  591 GLN D C   
15144 O O   . GLN H 80  ? 1.9955 1.5078 1.9691 -0.1029 0.5337  0.2065  591 GLN D O   
15145 C CB  . GLN H 80  ? 1.8829 1.6354 1.9683 -0.1147 0.5704  0.2450  591 GLN D CB  
15146 C CG  . GLN H 80  ? 1.8672 1.5867 1.9500 -0.1466 0.5276  0.3017  591 GLN D CG  
15147 C CD  . GLN H 80  ? 1.9085 1.6928 2.0241 -0.1648 0.5010  0.3466  591 GLN D CD  
15148 O OE1 . GLN H 80  ? 1.9741 1.8048 2.1067 -0.1551 0.5153  0.3392  591 GLN D OE1 
15149 N NE2 . GLN H 80  ? 1.8717 1.6658 1.9967 -0.1908 0.4606  0.3908  591 GLN D NE2 
15150 N N   . LEU H 81  ? 2.0406 1.6004 2.0237 -0.0724 0.5599  0.1651  592 LEU D N   
15151 C CA  . LEU H 81  ? 2.1700 1.6276 2.1006 -0.0622 0.5281  0.1497  592 LEU D CA  
15152 C C   . LEU H 81  ? 2.1383 1.5375 2.0366 -0.0457 0.5490  0.1132  592 LEU D C   
15153 O O   . LEU H 81  ? 2.2210 1.5313 2.0769 -0.0471 0.5173  0.1157  592 LEU D O   
15154 C CB  . LEU H 81  ? 2.2599 1.7190 2.1825 -0.0422 0.5301  0.1248  592 LEU D CB  
15155 C CG  . LEU H 81  ? 2.3237 1.8311 2.2719 -0.0548 0.5071  0.1563  592 LEU D CG  
15156 C CD1 . LEU H 81  ? 2.4076 1.9057 2.3417 -0.0314 0.5118  0.1244  592 LEU D CD1 
15157 C CD2 . LEU H 81  ? 2.4429 1.9012 2.3767 -0.0810 0.4477  0.2045  592 LEU D CD2 
15158 N N   . LEU H 82  ? 2.2070 1.6549 2.1243 -0.0295 0.6017  0.0792  593 LEU D N   
15159 C CA  . LEU H 82  ? 2.1498 1.5519 2.0411 -0.0134 0.6264  0.0439  593 LEU D CA  
15160 C C   . LEU H 82  ? 2.0832 1.4604 1.9705 -0.0324 0.6156  0.0676  593 LEU D C   
15161 O O   . LEU H 82  ? 2.0762 1.3908 1.9305 -0.0227 0.6202  0.0464  593 LEU D O   
15162 C CB  . LEU H 82  ? 2.0267 1.4959 1.9458 0.0056  0.6817  0.0059  593 LEU D CB  
15163 C CG  . LEU H 82  ? 1.9866 1.4200 1.8847 0.0232  0.6672  -0.0329 593 LEU D CG  
15164 C CD1 . LEU H 82  ? 2.1208 1.4910 1.9762 0.0417  0.6629  -0.0538 593 LEU D CD1 
15165 C CD2 . LEU H 82  ? 1.8438 1.3652 1.7833 0.0236  0.6356  -0.0468 593 LEU D CD2 
15166 N N   . GLY H 83  ? 2.2608 1.6850 2.1801 -0.0590 0.6005  0.1122  594 GLY D N   
15167 C CA  . GLY H 83  ? 2.1866 1.5952 2.1070 -0.0790 0.5896  0.1389  594 GLY D CA  
15168 C C   . GLY H 83  ? 2.3216 1.6520 2.2108 -0.0977 0.5308  0.1737  594 GLY D C   
15169 O O   . GLY H 83  ? 2.3954 1.6632 2.2574 -0.1025 0.5175  0.1760  594 GLY D O   
15170 N N   . ILE H 84  ? 2.1290 1.4613 2.0217 -0.1086 0.4939  0.2018  595 ILE D N   
15171 C CA  . ILE H 84  ? 2.2396 1.4973 2.1037 -0.1277 0.4343  0.2372  595 ILE D CA  
15172 C C   . ILE H 84  ? 2.4101 1.5596 2.2140 -0.1084 0.4146  0.2065  595 ILE D C   
15173 O O   . ILE H 84  ? 2.5787 1.6492 2.3494 -0.1204 0.3691  0.2274  595 ILE D O   
15174 C CB  . ILE H 84  ? 2.3265 1.6158 2.2109 -0.1442 0.3999  0.2752  595 ILE D CB  
15175 C CG1 . ILE H 84  ? 2.4514 1.7457 2.3275 -0.1208 0.4101  0.2434  595 ILE D CG1 
15176 C CG2 . ILE H 84  ? 2.2139 1.6076 2.1559 -0.1650 0.4145  0.3119  595 ILE D CG2 
15177 C CD1 . ILE H 84  ? 2.5556 1.8911 2.4555 -0.1351 0.3826  0.2777  595 ILE D CD1 
15178 N N   . TRP H 85  ? 2.4094 1.5532 2.1979 -0.0780 0.4468  0.1579  596 TRP D N   
15179 C CA  . TRP H 85  ? 2.5664 1.6123 2.2975 -0.0559 0.4343  0.1255  596 TRP D CA  
15180 C C   . TRP H 85  ? 2.4789 1.4947 2.1942 -0.0501 0.4576  0.1066  596 TRP D C   
15181 O O   . TRP H 85  ? 2.3108 1.3823 2.0603 -0.0629 0.4833  0.1176  596 TRP D O   
15182 C CB  . TRP H 85  ? 2.5580 1.6139 2.2808 -0.0255 0.4605  0.0825  596 TRP D CB  
15183 C CG  . TRP H 85  ? 2.6815 1.7618 2.4165 -0.0294 0.4374  0.0985  596 TRP D CG  
15184 C CD1 . TRP H 85  ? 2.8114 1.8841 2.5521 -0.0545 0.3890  0.1444  596 TRP D CD1 
15185 C CD2 . TRP H 85  ? 2.6701 1.7893 2.4150 -0.0082 0.4617  0.0697  596 TRP D CD2 
15186 N NE1 . TRP H 85  ? 2.8594 1.9625 2.6119 -0.0500 0.3815  0.1458  596 TRP D NE1 
15187 C CE2 . TRP H 85  ? 2.7726 1.9045 2.5276 -0.0215 0.4257  0.1000  596 TRP D CE2 
15188 C CE3 . TRP H 85  ? 2.6268 1.7713 2.3736 0.0203  0.5097  0.0221  596 TRP D CE3 
15189 C CZ2 . TRP H 85  ? 2.7688 1.9369 2.5347 -0.0068 0.4366  0.0834  596 TRP D CZ2 
15190 C CZ3 . TRP H 85  ? 2.6513 1.8319 2.4095 0.0346  0.5200  0.0061  596 TRP D CZ3 
15191 C CH2 . TRP H 85  ? 2.7156 1.9074 2.4828 0.0213  0.4838  0.0361  596 TRP D CH2 
15192 N N   . GLY H 86  ? 2.7314 1.6600 2.3943 -0.0292 0.4501  0.0769  597 GLY D N   
15193 C CA  . GLY H 86  ? 2.6894 1.6213 2.3427 -0.0203 0.4648  0.0542  597 GLY D CA  
15194 C C   . GLY H 86  ? 2.5609 1.5423 2.2302 0.0018  0.5269  0.0125  597 GLY D C   
15195 O O   . GLY H 86  ? 2.6262 1.6097 2.2716 0.0219  0.5293  -0.0192 597 GLY D O   
15196 N N   . CYS H 87  ? 2.3323 1.3824 2.0492 -0.0046 0.5685  0.0169  598 CYS D N   
15197 C CA  . CYS H 87  ? 2.1863 1.2909 1.9236 0.0166  0.6257  -0.0235 598 CYS D CA  
15198 C C   . CYS H 87  ? 1.9947 1.1824 1.7815 0.0011  0.6586  -0.0108 598 CYS D C   
15199 O O   . CYS H 87  ? 1.9433 1.1238 1.7279 0.0020  0.6807  -0.0217 598 CYS D O   
15200 C CB  . CYS H 87  ? 2.2294 1.3752 1.9805 0.0318  0.6372  -0.0406 598 CYS D CB  
15201 S SG  . CYS H 87  ? 2.4307 1.5100 2.1333 0.0496  0.5953  -0.0527 598 CYS D SG  
15202 N N   . SER H 88  ? 2.2210 1.4884 2.0520 -0.0128 0.6609  0.0129  599 SER D N   
15203 C CA  . SER H 88  ? 2.0328 1.3919 1.9156 -0.0213 0.6792  0.0201  599 SER D CA  
15204 C C   . SER H 88  ? 1.9084 1.3061 1.8122 -0.0049 0.6622  -0.0170 599 SER D C   
15205 O O   . SER H 88  ? 1.8263 1.3016 1.7658 -0.0021 0.6428  -0.0229 599 SER D O   
15206 C CB  . SER H 88  ? 2.0077 1.3598 1.8938 -0.0411 0.6606  0.0484  599 SER D CB  
15207 O OG  . SER H 88  ? 1.8150 1.2631 1.7514 -0.0409 0.6471  0.0488  599 SER D OG  
15208 N N   . GLY H 89  ? 1.8174 1.1711 1.6980 -0.0038 0.6586  -0.0293 600 GLY D N   
15209 C CA  . GLY H 89  ? 1.7085 1.1083 1.6046 -0.0012 0.6308  -0.0465 600 GLY D CA  
15210 C C   . GLY H 89  ? 1.7969 1.2178 1.6897 0.0095  0.6195  -0.0592 600 GLY D C   
15211 O O   . GLY H 89  ? 1.9567 1.3264 1.8124 0.0172  0.6258  -0.0627 600 GLY D O   
15212 N N   . LYS H 90  ? 1.7594 1.2557 1.6862 0.0124  0.5984  -0.0676 601 LYS D N   
15213 C CA  . LYS H 90  ? 1.9015 1.4243 1.8300 0.0226  0.5885  -0.0784 601 LYS D CA  
15214 C C   . LYS H 90  ? 1.9081 1.4220 1.8167 0.0322  0.5729  -0.0932 601 LYS D C   
15215 O O   . LYS H 90  ? 1.8873 1.3606 1.7712 0.0322  0.5736  -0.0936 601 LYS D O   
15216 C CB  . LYS H 90  ? 1.7788 1.3856 1.7445 0.0235  0.5686  -0.0822 601 LYS D CB  
15217 C CG  . LYS H 90  ? 1.6467 1.2860 1.6358 0.0166  0.5748  -0.0674 601 LYS D CG  
15218 C CD  . LYS H 90  ? 1.5243 1.2386 1.5417 0.0181  0.5548  -0.0722 601 LYS D CD  
15219 C CE  . LYS H 90  ? 1.4383 1.1981 1.4766 0.0127  0.5532  -0.0564 601 LYS D CE  
15220 N NZ  . LYS H 90  ? 1.3773 1.1087 1.4108 0.0050  0.5605  -0.0451 601 LYS D NZ  
15221 N N   . LEU H 91  ? 2.0080 1.5657 1.9279 0.0416  0.5568  -0.1047 602 LEU D N   
15222 C CA  . LEU H 91  ? 1.9911 1.5417 1.8970 0.0513  0.5486  -0.1179 602 LEU D CA  
15223 C C   . LEU H 91  ? 2.1257 1.6247 1.9920 0.0635  0.5458  -0.1223 602 LEU D C   
15224 O O   . LEU H 91  ? 2.2346 1.7224 2.0897 0.0735  0.5463  -0.1278 602 LEU D O   
15225 C CB  . LEU H 91  ? 1.8389 1.3822 1.7508 0.0430  0.5559  -0.1199 602 LEU D CB  
15226 C CG  . LEU H 91  ? 1.7864 1.3662 1.7329 0.0325  0.5612  -0.1196 602 LEU D CG  
15227 C CD1 . LEU H 91  ? 1.7786 1.3503 1.7311 0.0253  0.5676  -0.1237 602 LEU D CD1 
15228 C CD2 . LEU H 91  ? 1.8279 1.4431 1.7896 0.0385  0.5585  -0.1266 602 LEU D CD2 
15229 N N   . ILE H 92  ? 2.0875 1.5432 1.9284 0.0627  0.5471  -0.1200 603 ILE D N   
15230 C CA  . ILE H 92  ? 2.2161 1.6094 2.0118 0.0755  0.5440  -0.1250 603 ILE D CA  
15231 C C   . ILE H 92  ? 2.3564 1.6825 2.1206 0.0690  0.5576  -0.1130 603 ILE D C   
15232 O O   . ILE H 92  ? 2.3368 1.6702 2.1146 0.0551  0.5679  -0.1029 603 ILE D O   
15233 C CB  . ILE H 92  ? 2.1095 1.5172 1.8973 0.0878  0.5227  -0.1387 603 ILE D CB  
15234 C CG1 . ILE H 92  ? 1.9899 1.3976 1.7851 0.0753  0.5355  -0.1322 603 ILE D CG1 
15235 C CG2 . ILE H 92  ? 2.0640 1.5051 1.8698 0.0924  0.5270  -0.1474 603 ILE D CG2 
15236 C CD1 . ILE H 92  ? 2.0889 1.4506 1.8491 0.0800  0.5281  -0.1312 603 ILE D CD1 
15237 N N   . CYS H 93  ? 1.9684 1.2251 1.6880 0.0799  0.5519  -0.1146 604 CYS D N   
15238 C CA  . CYS H 93  ? 2.1134 1.2978 1.7952 0.0766  0.5508  -0.1049 604 CYS D CA  
15239 C C   . CYS H 93  ? 2.3349 1.4493 1.9679 0.0934  0.5190  -0.1124 604 CYS D C   
15240 O O   . CYS H 93  ? 2.4007 1.5112 2.0298 0.1039  0.5110  -0.1197 604 CYS D O   
15241 C CB  . CYS H 93  ? 2.2162 1.3774 1.9072 0.0617  0.5760  -0.0869 604 CYS D CB  
15242 S SG  . CYS H 93  ? 2.5724 1.6692 2.2406 0.0689  0.5648  -0.0819 604 CYS D SG  
15243 N N   . CYS H 94  ? 2.4184 1.4795 2.0163 0.0957  0.4959  -0.1103 605 CYS D N   
15244 C CA  . CYS H 94  ? 2.5821 1.5744 2.1359 0.1093  0.4550  -0.1149 605 CYS D CA  
15245 C C   . CYS H 94  ? 2.7169 1.6312 2.2473 0.0967  0.4315  -0.0929 605 CYS D C   
15246 O O   . CYS H 94  ? 2.6505 1.5651 2.1981 0.0779  0.4473  -0.0742 605 CYS D O   
15247 C CB  . CYS H 94  ? 2.5355 1.5274 2.0731 0.1194  0.4361  -0.1258 605 CYS D CB  
15248 S SG  . CYS H 94  ? 2.3746 1.4570 1.9474 0.1315  0.4481  -0.1456 605 CYS D SG  
15249 N N   . THR H 95  ? 2.6430 1.4954 2.1405 0.1044  0.3889  -0.0911 606 THR D N   
15250 C CA  . THR H 95  ? 2.7614 1.5443 2.2425 0.0875  0.3500  -0.0623 606 THR D CA  
15251 C C   . THR H 95  ? 2.8938 1.6184 2.3378 0.0965  0.2970  -0.0641 606 THR D C   
15252 O O   . THR H 95  ? 2.9053 1.6380 2.3351 0.1186  0.2936  -0.0888 606 THR D O   
15253 C CB  . THR H 95  ? 2.8361 1.6067 2.3265 0.0808  0.3503  -0.0479 606 THR D CB  
15254 O OG1 . THR H 95  ? 2.7266 1.5647 2.2532 0.0837  0.4058  -0.0601 606 THR D OG1 
15255 C CG2 . THR H 95  ? 2.8403 1.5736 2.3376 0.0501  0.3206  -0.0039 606 THR D CG2 
15256 N N   . ASN H 96  ? 3.1244 1.7982 2.5593 0.0774  0.2547  -0.0353 607 ASN D N   
15257 C CA  . ASN H 96  ? 3.3431 1.9635 2.7488 0.0830  0.2031  -0.0337 607 ASN D CA  
15258 C C   . ASN H 96  ? 3.4980 2.0754 2.8895 0.0824  0.1666  -0.0215 607 ASN D C   
15259 O O   . ASN H 96  ? 3.6106 2.1461 2.9965 0.0661  0.1201  0.0060  607 ASN D O   
15260 C CB  . ASN H 96  ? 3.3598 1.9600 2.7705 0.0619  0.1754  -0.0087 607 ASN D CB  
15261 C CG  . ASN H 96  ? 3.2065 1.8468 2.6289 0.0624  0.2098  -0.0203 607 ASN D CG  
15262 O OD1 . ASN H 96  ? 3.1237 1.8150 2.5597 0.0712  0.2587  -0.0389 607 ASN D OD1 
15263 N ND2 . ASN H 96  ? 3.2158 1.8375 2.6367 0.0516  0.1840  -0.0072 607 ASN D ND2 
15264 N N   . VAL H 97  ? 3.1854 1.7785 2.5743 0.0995  0.1870  -0.0406 608 VAL D N   
15265 C CA  . VAL H 97  ? 3.2961 1.8508 2.6699 0.1014  0.1552  -0.0318 608 VAL D CA  
15266 C C   . VAL H 97  ? 3.2901 1.8441 2.6412 0.1322  0.1546  -0.0653 608 VAL D C   
15267 O O   . VAL H 97  ? 3.1636 1.7691 2.5269 0.1496  0.1947  -0.0921 608 VAL D O   
15268 C CB  . VAL H 97  ? 3.2855 1.8588 2.6807 0.0900  0.1775  -0.0171 608 VAL D CB  
15269 C CG1 . VAL H 97  ? 3.3606 1.8967 2.7377 0.0953  0.1454  -0.0115 608 VAL D CG1 
15270 C CG2 . VAL H 97  ? 3.2775 1.8535 2.6981 0.0556  0.1708  0.0243  608 VAL D CG2 
15271 N N   . PRO H 98  ? 3.4292 1.9334 2.7512 0.1383  0.1099  -0.0630 609 PRO D N   
15272 C CA  . PRO H 98  ? 3.4638 1.9674 2.7644 0.1666  0.1080  -0.0917 609 PRO D CA  
15273 C C   . PRO H 98  ? 3.4515 1.9667 2.7555 0.1768  0.1186  -0.1002 609 PRO D C   
15274 O O   . PRO H 98  ? 3.5397 2.0254 2.8422 0.1628  0.0981  -0.0774 609 PRO D O   
15275 C CB  . PRO H 98  ? 3.7130 2.1540 2.9795 0.1655  0.0558  -0.0800 609 PRO D CB  
15276 C CG  . PRO H 98  ? 3.8070 2.2174 3.0814 0.1352  0.0248  -0.0413 609 PRO D CG  
15277 C CD  . PRO H 98  ? 3.5664 2.0184 2.8764 0.1182  0.0592  -0.0318 609 PRO D CD  
15278 N N   . TRP H 99  ? 3.5473 2.1107 2.8596 0.1995  0.1491  -0.1306 610 TRP D N   
15279 C CA  . TRP H 99  ? 3.5847 2.1684 2.9043 0.2108  0.1620  -0.1414 610 TRP D CA  
15280 C C   . TRP H 99  ? 3.8224 2.3492 3.1073 0.2205  0.1191  -0.1393 610 TRP D C   
15281 O O   . TRP H 99  ? 3.8813 2.4006 3.1469 0.2380  0.1072  -0.1553 610 TRP D O   
15282 C CB  . TRP H 99  ? 3.3662 2.0283 2.7121 0.2293  0.2019  -0.1716 610 TRP D CB  
15283 C CG  . TRP H 99  ? 3.3704 2.0629 2.7293 0.2404  0.2159  -0.1834 610 TRP D CG  
15284 C CD1 . TRP H 99  ? 3.4361 2.1213 2.7815 0.2590  0.2006  -0.1979 610 TRP D CD1 
15285 C CD2 . TRP H 99  ? 3.2298 1.9684 2.6193 0.2336  0.2496  -0.1818 610 TRP D CD2 
15286 N NE1 . TRP H 99  ? 3.4013 2.1249 2.7677 0.2639  0.2204  -0.2055 610 TRP D NE1 
15287 C CE2 . TRP H 99  ? 3.2776 2.0354 2.6714 0.2488  0.2510  -0.1960 610 TRP D CE2 
15288 C CE3 . TRP H 99  ? 3.0522 1.8196 2.4671 0.2161  0.2806  -0.1694 610 TRP D CE3 
15289 C CZ2 . TRP H 99  ? 3.1492 1.9556 2.5722 0.2470  0.2809  -0.1985 610 TRP D CZ2 
15290 C CZ3 . TRP H 99  ? 2.9582 1.7738 2.4024 0.2146  0.3128  -0.1717 610 TRP D CZ3 
15291 C CH2 . TRP H 99  ? 2.9878 1.8233 2.4360 0.2300  0.3120  -0.1863 610 TRP D CH2 
15292 N N   . ASN H 100 ? 3.6016 2.0897 2.8786 0.2084  0.0955  -0.1175 611 ASN D N   
15293 C CA  . ASN H 100 ? 3.7734 2.2090 3.0174 0.2156  0.0522  -0.1128 611 ASN D CA  
15294 C C   . ASN H 100 ? 3.7557 2.2243 3.0005 0.2425  0.0723  -0.1427 611 ASN D C   
15295 O O   . ASN H 100 ? 3.6473 2.1658 2.9204 0.2464  0.1084  -0.1534 611 ASN D O   
15296 C CB  . ASN H 100 ? 3.8401 2.2371 3.0838 0.1916  0.0215  -0.0774 611 ASN D CB  
15297 C CG  . ASN H 100 ? 4.0596 2.3943 3.2677 0.1887  -0.0378 -0.0609 611 ASN D CG  
15298 O OD1 . ASN H 100 ? 4.1450 2.4577 3.3229 0.2056  -0.0557 -0.0762 611 ASN D OD1 
15299 N ND2 . ASN H 100 ? 4.3507 2.6603 3.5639 0.1648  -0.0696 -0.0262 611 ASN D ND2 
15300 N N   . SER H 101 ? 3.7114 2.1557 2.9261 0.2604  0.0494  -0.1554 612 SER D N   
15301 C CA  . SER H 101 ? 3.6566 2.1355 2.8741 0.2851  0.0663  -0.1822 612 SER D CA  
15302 C C   . SER H 101 ? 3.6763 2.1501 2.8951 0.2877  0.0619  -0.1798 612 SER D C   
15303 O O   . SER H 101 ? 3.5874 2.1102 2.8245 0.3041  0.0877  -0.2017 612 SER D O   
15304 C CB  . SER H 101 ? 3.7386 2.1843 2.9185 0.3024  0.0400  -0.1918 612 SER D CB  
15305 O OG  . SER H 101 ? 3.9022 2.3588 3.0830 0.3024  0.0485  -0.1964 612 SER D OG  
15306 N N   . SER H 102 ? 3.8764 2.2961 3.0795 0.2701  0.0281  -0.1519 613 SER D N   
15307 C CA  . SER H 102 ? 3.9194 2.3290 3.1218 0.2711  0.0195  -0.1462 613 SER D CA  
15308 C C   . SER H 102 ? 3.7311 2.2033 2.9749 0.2702  0.0691  -0.1549 613 SER D C   
15309 O O   . SER H 102 ? 3.7281 2.2097 2.9764 0.2778  0.0744  -0.1595 613 SER D O   
15310 C CB  . SER H 102 ? 4.1062 2.4504 3.2895 0.2467  -0.0321 -0.1081 613 SER D CB  
15311 O OG  . SER H 102 ? 4.0905 2.4373 3.2952 0.2197  -0.0274 -0.0826 613 SER D OG  
15312 N N   . TRP H 103 ? 3.8608 2.3774 3.1339 0.2614  0.1056  -0.1572 614 TRP D N   
15313 C CA  . TRP H 103 ? 3.6845 2.2685 2.9983 0.2595  0.1563  -0.1653 614 TRP D CA  
15314 C C   . TRP H 103 ? 3.5572 2.2235 2.8992 0.2805  0.1916  -0.1999 614 TRP D C   
15315 O O   . TRP H 103 ? 3.4069 2.1398 2.7819 0.2789  0.2258  -0.2112 614 TRP D O   
15316 C CB  . TRP H 103 ? 3.5657 2.1637 2.8989 0.2389  0.1777  -0.1503 614 TRP D CB  
15317 C CG  . TRP H 103 ? 3.6915 2.2201 3.0070 0.2123  0.1402  -0.1108 614 TRP D CG  
15318 C CD1 . TRP H 103 ? 3.8572 2.3265 3.1517 0.2006  0.0949  -0.0831 614 TRP D CD1 
15319 C CD2 . TRP H 103 ? 3.6625 2.1838 2.9861 0.1904  0.1404  -0.0903 614 TRP D CD2 
15320 N NE1 . TRP H 103 ? 3.9539 2.3879 3.2482 0.1701  0.0650  -0.0439 614 TRP D NE1 
15321 C CE2 . TRP H 103 ? 3.8155 2.2789 3.1269 0.1641  0.0934  -0.0485 614 TRP D CE2 
15322 C CE3 . TRP H 103 ? 3.5017 2.0660 2.8449 0.1888  0.1734  -0.1012 614 TRP D CE3 
15323 C CZ2 . TRP H 103 ? 3.7849 2.2367 3.1062 0.1362  0.0797  -0.0174 614 TRP D CZ2 
15324 C CZ3 . TRP H 103 ? 3.5063 2.0489 2.8532 0.1638  0.1618  -0.0734 614 TRP D CZ3 
15325 C CH2 . TRP H 103 ? 3.6222 2.1108 2.9595 0.1376  0.1156  -0.0318 614 TRP D CH2 
15326 N N   . SER H 104 ? 3.7422 2.4055 3.0731 0.2981  0.1782  -0.2136 615 SER D N   
15327 C CA  . SER H 104 ? 3.6040 2.3432 2.9640 0.3153  0.2023  -0.2420 615 SER D CA  
15328 C C   . SER H 104 ? 3.5472 2.3094 2.9126 0.3193  0.2053  -0.2530 615 SER D C   
15329 O O   . SER H 104 ? 3.3708 2.1945 2.7711 0.3121  0.2337  -0.2580 615 SER D O   
15330 C CB  . SER H 104 ? 3.4058 2.2342 2.8170 0.3115  0.2457  -0.2509 615 SER D CB  
15331 O OG  . SER H 104 ? 3.3221 2.2279 2.7672 0.3235  0.2610  -0.2747 615 SER D OG  
15332 N N   . ASN H 105 ? 2.6008 2.5456 3.4770 0.2030  -0.0322 -1.4716 616 ASN D N   
15333 C CA  . ASN H 105 ? 2.5893 2.5256 3.4717 0.1943  -0.0239 -1.4684 616 ASN D CA  
15334 C C   . ASN H 105 ? 2.6055 2.5491 3.5190 0.1937  -0.0290 -1.4749 616 ASN D C   
15335 O O   . ASN H 105 ? 2.7009 2.6456 3.6297 0.1970  -0.0240 -1.4779 616 ASN D O   
15336 C CB  . ASN H 105 ? 2.6851 2.6091 3.5560 0.1928  -0.0072 -1.4626 616 ASN D CB  
15337 C CG  . ASN H 105 ? 2.7945 2.7221 3.6742 0.2014  -0.0036 -1.4661 616 ASN D CG  
15338 O OD1 . ASN H 105 ? 2.8119 2.7496 3.6956 0.2095  -0.0127 -1.4712 616 ASN D OD1 
15339 N ND2 . ASN H 105 ? 2.8797 2.7992 3.7627 0.1997  0.0095  -1.4635 616 ASN D ND2 
15340 N N   . ARG H 106 ? 2.5408 2.4895 3.4640 0.1896  -0.0388 -1.4772 617 ARG D N   
15341 C CA  . ARG H 106 ? 2.5474 2.5023 3.4994 0.1878  -0.0438 -1.4830 617 ARG D CA  
15342 C C   . ARG H 106 ? 2.4907 2.4371 3.4428 0.1777  -0.0390 -1.4786 617 ARG D C   
15343 O O   . ARG H 106 ? 2.4445 2.3827 3.3750 0.1726  -0.0350 -1.4720 617 ARG D O   
15344 C CB  . ARG H 106 ? 2.4946 2.4641 3.4609 0.1922  -0.0606 -1.4905 617 ARG D CB  
15345 C CG  . ARG H 106 ? 2.5438 2.5230 3.5095 0.2025  -0.0672 -1.4952 617 ARG D CG  
15346 C CD  . ARG H 106 ? 2.6506 2.6363 3.6400 0.2082  -0.0664 -1.5016 617 ARG D CD  
15347 N NE  . ARG H 106 ? 2.6960 2.6931 3.6882 0.2183  -0.0750 -1.5074 617 ARG D NE  
15348 C CZ  . ARG H 106 ? 2.7884 2.7938 3.8010 0.2250  -0.0769 -1.5140 617 ARG D CZ  
15349 N NH1 . ARG H 106 ? 2.8446 2.8479 3.8765 0.2223  -0.0707 -1.5155 617 ARG D NH1 
15350 N NH2 . ARG H 106 ? 2.8265 2.8424 3.8401 0.2343  -0.0849 -1.5190 617 ARG D NH2 
15351 N N   . ASN H 107 ? 2.4571 2.4056 3.4337 0.1749  -0.0391 -1.4822 618 ASN D N   
15352 C CA  . ASN H 107 ? 2.4101 2.3513 3.3896 0.1656  -0.0348 -1.4786 618 ASN D CA  
15353 C C   . ASN H 107 ? 2.3778 2.3262 3.3670 0.1629  -0.0476 -1.4818 618 ASN D C   
15354 O O   . ASN H 107 ? 2.3760 2.3361 3.3746 0.1681  -0.0602 -1.4879 618 ASN D O   
15355 C CB  . ASN H 107 ? 2.4948 2.4323 3.4941 0.1632  -0.0260 -1.4797 618 ASN D CB  
15356 C CG  . ASN H 107 ? 2.4691 2.3949 3.4633 0.1536  -0.0162 -1.4735 618 ASN D CG  
15357 O OD1 . ASN H 107 ? 2.4037 2.3281 3.3931 0.1482  -0.0205 -1.4715 618 ASN D OD1 
15358 N ND2 . ASN H 107 ? 2.5590 2.4763 3.5542 0.1517  -0.0029 -1.4703 618 ASN D ND2 
15359 N N   . LEU H 108 ? 2.4705 2.4115 3.4571 0.1545  -0.0441 -1.4776 619 LEU D N   
15360 C CA  . LEU H 108 ? 2.3992 2.3454 3.3935 0.1511  -0.0547 -1.4796 619 LEU D CA  
15361 C C   . LEU H 108 ? 2.3968 2.3540 3.4221 0.1535  -0.0637 -1.4880 619 LEU D C   
15362 O O   . LEU H 108 ? 2.3939 2.3610 3.4269 0.1555  -0.0766 -1.4926 619 LEU D O   
15363 C CB  . LEU H 108 ? 2.3982 2.3337 3.3858 0.1418  -0.0476 -1.4735 619 LEU D CB  
15364 C CG  . LEU H 108 ? 2.3946 2.3324 3.3781 0.1380  -0.0568 -1.4727 619 LEU D CG  
15365 C CD1 . LEU H 108 ? 2.3947 2.3348 3.3551 0.1413  -0.0627 -1.4705 619 LEU D CD1 
15366 C CD2 . LEU H 108 ? 2.3941 2.3211 3.3718 0.1292  -0.0486 -1.4668 619 LEU D CD2 
15367 N N   . SER H 109 ? 2.1576 2.1136 3.2011 0.1533  -0.0571 -1.4902 620 SER D N   
15368 C CA  . SER H 109 ? 2.1554 2.1216 3.2291 0.1552  -0.0649 -1.4982 620 SER D CA  
15369 C C   . SER H 109 ? 2.1564 2.1341 3.2385 0.1648  -0.0722 -1.5049 620 SER D C   
15370 O O   . SER H 109 ? 2.1545 2.1428 3.2609 0.1675  -0.0807 -1.5124 620 SER D O   
15371 C CB  . SER H 109 ? 2.1562 2.1164 3.2468 0.1511  -0.0548 -1.4978 620 SER D CB  
15372 O OG  . SER H 109 ? 2.1539 2.1235 3.2740 0.1520  -0.0624 -1.5053 620 SER D OG  
15373 N N   . GLU H 110 ? 2.1874 2.1633 3.2498 0.1698  -0.0689 -1.5024 621 GLU D N   
15374 C CA  . GLU H 110 ? 2.1889 2.1750 3.2559 0.1794  -0.0749 -1.5081 621 GLU D CA  
15375 C C   . GLU H 110 ? 2.1874 2.1818 3.2434 0.1834  -0.0874 -1.5099 621 GLU D C   
15376 O O   . GLU H 110 ? 2.1882 2.1927 3.2491 0.1916  -0.0945 -1.5154 621 GLU D O   
15377 C CB  . GLU H 110 ? 2.1938 2.1725 3.2454 0.1830  -0.0630 -1.5040 621 GLU D CB  
15378 C CG  . GLU H 110 ? 2.1958 2.1657 3.2560 0.1795  -0.0495 -1.5016 621 GLU D CG  
15379 C CD  . GLU H 110 ? 2.2009 2.1636 3.2449 0.1833  -0.0378 -1.4974 621 GLU D CD  
15380 O OE1 . GLU H 110 ? 2.2030 2.1691 3.2328 0.1898  -0.0410 -1.4977 621 GLU D OE1 
15381 O OE2 . GLU H 110 ? 2.2029 2.1562 3.2481 0.1797  -0.0251 -1.4936 621 GLU D OE2 
15382 N N   . ILE H 111 ? 2.1573 2.1478 3.1989 0.1781  -0.0902 -1.5055 622 ILE D N   
15383 C CA  . ILE H 111 ? 2.1557 2.1532 3.1856 0.1811  -0.1016 -1.5065 622 ILE D CA  
15384 C C   . ILE H 111 ? 2.1512 2.1574 3.1982 0.1788  -0.1140 -1.5112 622 ILE D C   
15385 O O   . ILE H 111 ? 2.1497 2.1684 3.2070 0.1844  -0.1261 -1.5177 622 ILE D O   
15386 C CB  . ILE H 111 ? 2.1568 2.1438 3.1556 0.1775  -0.0959 -1.4978 622 ILE D CB  
15387 C CG1 . ILE H 111 ? 2.1616 2.1415 3.1419 0.1811  -0.0852 -1.4937 622 ILE D CG1 
15388 C CG2 . ILE H 111 ? 2.1544 2.1480 3.1425 0.1791  -0.1079 -1.4982 622 ILE D CG2 
15389 C CD1 . ILE H 111 ? 2.1630 2.1317 3.1133 0.1768  -0.0781 -1.4849 622 ILE D CD1 
15390 N N   . TRP H 112 ? 1.7185 2.9256 2.2694 0.4876  -0.5693 -0.8274 623 TRP D N   
15391 C CA  . TRP H 112 ? 1.6694 2.9192 2.2688 0.4606  -0.6173 -0.7951 623 TRP D CA  
15392 C C   . TRP H 112 ? 1.6484 2.9599 2.3207 0.4709  -0.6378 -0.6945 623 TRP D C   
15393 O O   . TRP H 112 ? 1.6100 2.9468 2.3261 0.4430  -0.6829 -0.6612 623 TRP D O   
15394 C CB  . TRP H 112 ? 1.6534 2.9478 2.2403 0.4733  -0.6161 -0.8313 623 TRP D CB  
15395 C CG  . TRP H 112 ? 1.6719 2.9078 2.1919 0.4608  -0.6000 -0.9311 623 TRP D CG  
15396 C CD1 . TRP H 112 ? 1.7087 2.9324 2.1781 0.4937  -0.5571 -0.9813 623 TRP D CD1 
15397 C CD2 . TRP H 112 ? 1.6542 2.8407 2.1539 0.4132  -0.6281 -0.9909 623 TRP D CD2 
15398 N NE1 . TRP H 112 ? 1.7151 2.8833 2.1365 0.4679  -0.5570 -1.0678 623 TRP D NE1 
15399 C CE2 . TRP H 112 ? 1.6813 2.8277 2.1209 0.4189  -0.5990 -1.0751 623 TRP D CE2 
15400 C CE3 . TRP H 112 ? 1.6206 2.7914 2.1464 0.3672  -0.6750 -0.9813 623 TRP D CE3 
15401 C CZ2 . TRP H 112 ? 1.6739 2.7688 2.0829 0.3798  -0.6139 -1.1480 623 TRP D CZ2 
15402 C CZ3 . TRP H 112 ? 1.6148 2.7330 2.1062 0.3300  -0.6889 -1.0547 623 TRP D CZ3 
15403 C CH2 . TRP H 112 ? 1.6418 2.7203 2.0769 0.3362  -0.6539 -1.1316 623 TRP D CH2 
15404 N N   . ASP H 113 ? 1.7885 3.1238 2.4759 0.5095  -0.6070 -0.6451 624 ASP D N   
15405 C CA  . ASP H 113 ? 1.7704 3.1701 2.5311 0.5230  -0.6229 -0.5471 624 ASP D CA  
15406 C C   . ASP H 113 ? 1.7981 3.1661 2.5692 0.5305  -0.6093 -0.5082 624 ASP D C   
15407 O O   . ASP H 113 ? 1.7961 3.2194 2.6212 0.5562  -0.6059 -0.4295 624 ASP D O   
15408 C CB  . ASP H 113 ? 1.7682 3.2567 2.5521 0.5720  -0.5990 -0.5091 624 ASP D CB  
15409 C CG  . ASP H 113 ? 1.7364 3.2653 2.5221 0.5635  -0.6198 -0.5324 624 ASP D CG  
15410 O OD1 . ASP H 113 ? 1.7019 3.2199 2.5078 0.5199  -0.6664 -0.5357 624 ASP D OD1 
15411 O OD2 . ASP H 113 ? 1.7478 3.3180 2.5134 0.6013  -0.5905 -0.5474 624 ASP D OD2 
15412 N N   . ASN H 114 ? 1.9093 3.1894 2.6302 0.5086  -0.6013 -0.5618 625 ASN D N   
15413 C CA  . ASN H 114 ? 1.9810 3.2229 2.7060 0.5142  -0.5890 -0.5300 625 ASN D CA  
15414 C C   . ASN H 114 ? 2.0060 3.1470 2.6829 0.4733  -0.5981 -0.5872 625 ASN D C   
15415 O O   . ASN H 114 ? 2.1460 3.2388 2.8015 0.4813  -0.5762 -0.5870 625 ASN D O   
15416 C CB  . ASN H 114 ? 2.1948 3.4546 2.8984 0.5692  -0.5341 -0.5250 625 ASN D CB  
15417 C CG  . ASN H 114 ? 2.3418 3.5889 3.0705 0.5829  -0.5246 -0.4679 625 ASN D CG  
15418 O OD1 . ASN H 114 ? 2.2370 3.4885 3.0177 0.5593  -0.5610 -0.4112 625 ASN D OD1 
15419 N ND2 . ASN H 114 ? 2.5562 3.7861 3.2476 0.6216  -0.4772 -0.4831 625 ASN D ND2 
15420 N N   . MET H 115 ? 1.9984 3.1057 2.6574 0.4306  -0.6291 -0.6347 626 MET D N   
15421 C CA  . MET H 115 ? 1.9628 2.9748 2.5729 0.3921  -0.6354 -0.6928 626 MET D CA  
15422 C C   . MET H 115 ? 1.8745 2.8703 2.4957 0.3437  -0.6856 -0.7068 626 MET D C   
15423 O O   . MET H 115 ? 1.8421 2.8850 2.4779 0.3403  -0.7024 -0.7157 626 MET D O   
15424 C CB  . MET H 115 ? 2.0123 2.9842 2.5511 0.4025  -0.5943 -0.7810 626 MET D CB  
15425 C CG  . MET H 115 ? 2.0787 2.9544 2.5581 0.3848  -0.5743 -0.8379 626 MET D CG  
15426 S SD  . MET H 115 ? 2.2518 3.0887 2.7172 0.4123  -0.5390 -0.8091 626 MET D SD  
15427 C CE  . MET H 115 ? 2.2871 3.0074 2.6772 0.3754  -0.5271 -0.8967 626 MET D CE  
15428 N N   . THR H 116 ? 1.8396 2.7691 2.4541 0.3079  -0.7105 -0.7053 627 THR D N   
15429 C CA  . THR H 116 ? 1.8133 2.7151 2.4304 0.2615  -0.7576 -0.7224 627 THR D CA  
15430 C C   . THR H 116 ? 1.8303 2.6598 2.3787 0.2367  -0.7432 -0.8166 627 THR D C   
15431 O O   . THR H 116 ? 1.8671 2.6536 2.3676 0.2495  -0.7015 -0.8612 627 THR D O   
15432 C CB  . THR H 116 ? 1.8147 2.6821 2.4608 0.2357  -0.7962 -0.6687 627 THR D CB  
15433 O OG1 . THR H 116 ? 1.8582 2.6454 2.4600 0.2302  -0.7735 -0.6933 627 THR D OG1 
15434 C CG2 . THR H 116 ? 1.7993 2.7389 2.5183 0.2601  -0.8102 -0.5730 627 THR D CG2 
15435 N N   . TRP H 117 ? 1.8126 2.6291 2.3573 0.2010  -0.7784 -0.8464 628 TRP D N   
15436 C CA  . TRP H 117 ? 1.8135 2.5644 2.2977 0.1756  -0.7663 -0.9345 628 TRP D CA  
15437 C C   . TRP H 117 ? 1.8730 2.5318 2.3184 0.1538  -0.7590 -0.9533 628 TRP D C   
15438 O O   . TRP H 117 ? 1.9267 2.5300 2.3175 0.1483  -0.7271 -1.0206 628 TRP D O   
15439 C CB  . TRP H 117 ? 1.7870 2.5269 2.2693 0.1434  -0.7846 -0.9347 628 TRP D CB  
15440 C CG  . TRP H 117 ? 1.7645 2.5614 2.2523 0.1614  -0.7688 -0.9459 628 TRP D CG  
15441 C CD1 . TRP H 117 ? 1.7299 2.6063 2.2681 0.1743  -0.7951 -0.8989 628 TRP D CD1 
15442 C CD2 . TRP H 117 ? 1.7774 2.5512 2.2191 0.1678  -0.7209 -1.0005 628 TRP D CD2 
15443 N NE1 . TRP H 117 ? 1.7217 2.6257 2.2442 0.1888  -0.7695 -0.9282 628 TRP D NE1 
15444 C CE2 . TRP H 117 ? 1.7496 2.5924 2.2149 0.1855  -0.7251 -0.9906 628 TRP D CE2 
15445 C CE3 . TRP H 117 ? 1.8100 2.5117 2.1966 0.1603  -0.6729 -1.0472 628 TRP D CE3 
15446 C CZ2 . TRP H 117 ? 1.7536 2.5943 2.1891 0.1966  -0.6868 -1.0315 628 TRP D CZ2 
15447 C CZ3 . TRP H 117 ? 1.8111 2.5145 2.1745 0.1704  -0.6339 -1.0784 628 TRP D CZ3 
15448 C CH2 . TRP H 117 ? 1.7834 2.5549 2.1708 0.1889  -0.6424 -1.0733 628 TRP D CH2 
15449 N N   . LEU H 118 ? 1.7888 2.4298 2.2621 0.1413  -0.7888 -0.8936 629 LEU D N   
15450 C CA  . LEU H 118 ? 1.8277 2.3814 2.2658 0.1222  -0.7842 -0.9035 629 LEU D CA  
15451 C C   . LEU H 118 ? 1.8685 2.4027 2.2818 0.1530  -0.7345 -0.9078 629 LEU D C   
15452 O O   . LEU H 118 ? 1.9057 2.3649 2.2651 0.1414  -0.7099 -0.9580 629 LEU D O   
15453 C CB  . LEU H 118 ? 1.8205 2.3677 2.2996 0.1060  -0.8307 -0.8317 629 LEU D CB  
15454 C CG  . LEU H 118 ? 1.7933 2.3304 2.2836 0.0687  -0.8810 -0.8282 629 LEU D CG  
15455 C CD1 . LEU H 118 ? 1.7889 2.3264 2.3255 0.0588  -0.9295 -0.7527 629 LEU D CD1 
15456 C CD2 . LEU H 118 ? 1.8264 2.2582 2.2372 0.0362  -0.8360 -0.8619 629 LEU D CD2 
15457 N N   . GLN H 119 ? 1.9691 2.5697 2.4205 0.1929  -0.7191 -0.8552 630 GLN D N   
15458 C CA  . GLN H 119 ? 2.0334 2.6199 2.4631 0.2261  -0.6726 -0.8553 630 GLN D CA  
15459 C C   . GLN H 119 ? 2.0776 2.6529 2.4558 0.2401  -0.6292 -0.9322 630 GLN D C   
15460 O O   . GLN H 119 ? 2.1786 2.7018 2.5124 0.2502  -0.5925 -0.9649 630 GLN D O   
15461 C CB  . GLN H 119 ? 2.0534 2.7184 2.5409 0.2661  -0.6691 -0.7755 630 GLN D CB  
15462 C CG  . GLN H 119 ? 2.1803 2.8335 2.6520 0.3030  -0.6253 -0.7628 630 GLN D CG  
15463 C CD  . GLN H 119 ? 2.1987 2.9355 2.7320 0.3429  -0.6225 -0.6814 630 GLN D CD  
15464 O OE1 . GLN H 119 ? 2.1161 2.9160 2.7073 0.3396  -0.6564 -0.6294 630 GLN D OE1 
15465 N NE2 . GLN H 119 ? 2.3116 3.0489 2.8335 0.3809  -0.5822 -0.6692 630 GLN D NE2 
15466 N N   . TRP H 120 ? 2.1012 2.7227 2.4845 0.2398  -0.6348 -0.9621 631 TRP D N   
15467 C CA  . TRP H 120 ? 2.1348 2.7502 2.4729 0.2531  -0.5978 -1.0349 631 TRP D CA  
15468 C C   . TRP H 120 ? 2.1483 2.6774 2.4309 0.2161  -0.5925 -1.1108 631 TRP D C   
15469 O O   . TRP H 120 ? 2.2378 2.7232 2.4728 0.2251  -0.5541 -1.1625 631 TRP D O   
15470 C CB  . TRP H 120 ? 2.0450 2.7334 2.4073 0.2605  -0.6114 -1.0421 631 TRP D CB  
15471 C CG  . TRP H 120 ? 2.0613 2.7428 2.3799 0.2672  -0.5834 -1.1206 631 TRP D CG  
15472 C CD1 . TRP H 120 ? 2.0092 2.6569 2.3008 0.2344  -0.5908 -1.1829 631 TRP D CD1 
15473 C CD2 . TRP H 120 ? 2.1233 2.8392 2.4260 0.3108  -0.5445 -1.1365 631 TRP D CD2 
15474 N NE1 . TRP H 120 ? 2.0415 2.6896 2.3059 0.2524  -0.5456 -1.2117 631 TRP D NE1 
15475 C CE2 . TRP H 120 ? 2.1105 2.8068 2.3737 0.3006  -0.5332 -1.2171 631 TRP D CE2 
15476 C CE3 . TRP H 120 ? 2.1955 2.9544 2.5118 0.3584  -0.5176 -1.0909 631 TRP D CE3 
15477 C CZ2 . TRP H 120 ? 2.1674 2.8830 2.4030 0.3359  -0.4981 -1.2538 631 TRP D CZ2 
15478 C CZ3 . TRP H 120 ? 2.2547 3.0324 2.5409 0.3946  -0.4812 -1.1275 631 TRP D CZ3 
15479 C CH2 . TRP H 120 ? 2.2399 2.9947 2.4855 0.3830  -0.4727 -1.2084 631 TRP D CH2 
15480 N N   . ASP H 121 ? 2.2308 2.7331 2.5187 0.1744  -0.6309 -1.1173 632 ASP D N   
15481 C CA  . ASP H 121 ? 2.2434 2.6554 2.4824 0.1390  -0.5956 -1.1325 632 ASP D CA  
15482 C C   . ASP H 121 ? 2.3527 2.6917 2.5564 0.1346  -0.5794 -1.1449 632 ASP D C   
15483 O O   . ASP H 121 ? 2.4023 2.6710 2.5603 0.1135  -0.5343 -1.1486 632 ASP D O   
15484 C CB  . ASP H 121 ? 2.1452 2.5336 2.3931 0.1001  -0.6139 -1.0889 632 ASP D CB  
15485 C CG  . ASP H 121 ? 2.1570 2.4631 2.3535 0.0662  -0.5688 -1.0843 632 ASP D CG  
15486 O OD1 . ASP H 121 ? 2.1209 2.4330 2.3058 0.0620  -0.5399 -1.0883 632 ASP D OD1 
15487 O OD2 . ASP H 121 ? 2.2065 2.4447 2.3747 0.0442  -0.5650 -1.0738 632 ASP D OD2 
15488 N N   . LYS H 122 ? 2.2056 2.5594 2.4325 0.1535  -0.6058 -1.1232 633 LYS D N   
15489 C CA  . LYS H 122 ? 2.3164 2.5971 2.5106 0.1518  -0.5858 -1.1218 633 LYS D CA  
15490 C C   . LYS H 122 ? 2.4268 2.6927 2.5822 0.1811  -0.5341 -1.1626 633 LYS D C   
15491 O O   . LYS H 122 ? 2.5219 2.7119 2.6307 0.1712  -0.5110 -1.1973 633 LYS D O   
15492 C CB  . LYS H 122 ? 2.3329 2.6318 2.5694 0.1655  -0.6048 -1.0361 633 LYS D CB  
15493 C CG  . LYS H 122 ? 2.4376 2.6553 2.6433 0.1567  -0.5952 -1.0289 633 LYS D CG  
15494 C CD  . LYS H 122 ? 2.4264 2.5637 2.5974 0.1101  -0.6162 -1.0633 633 LYS D CD  
15495 C CE  . LYS H 122 ? 2.5606 2.6212 2.7036 0.1053  -0.6076 -1.0474 633 LYS D CE  
15496 N NZ  . LYS H 122 ? 2.5702 2.6582 2.7621 0.1199  -0.6330 -0.9618 633 LYS D NZ  
15497 N N   . GLU H 123 ? 2.2800 2.6155 2.4523 0.2178  -0.5161 -1.1584 634 GLU D N   
15498 C CA  . GLU H 123 ? 2.3173 2.6430 2.4530 0.2501  -0.4689 -1.1948 634 GLU D CA  
15499 C C   . GLU H 123 ? 2.3205 2.6197 2.4194 0.2317  -0.4430 -1.2518 634 GLU D C   
15500 O O   . GLU H 123 ? 2.3897 2.6296 2.4475 0.2256  -0.3992 -1.2573 634 GLU D O   
15501 C CB  . GLU H 123 ? 2.3090 2.7197 2.4794 0.2997  -0.4562 -1.1488 634 GLU D CB  
15502 C CG  . GLU H 123 ? 2.3410 2.7758 2.5517 0.3205  -0.4638 -1.0645 634 GLU D CG  
15503 C CD  . GLU H 123 ? 2.3713 2.8875 2.6125 0.3723  -0.4450 -1.0212 634 GLU D CD  
15504 O OE1 . GLU H 123 ? 2.3621 2.9153 2.5911 0.3919  -0.4280 -1.0566 634 GLU D OE1 
15505 O OE2 . GLU H 123 ? 2.4141 2.9572 2.6915 0.3940  -0.4474 -0.9513 634 GLU D OE2 
15506 N N   . ILE H 124 ? 2.4108 2.7514 2.5341 0.2161  -0.4543 -1.2384 635 ILE D N   
15507 C CA  . ILE H 124 ? 2.3974 2.7183 2.5003 0.1966  -0.4154 -1.2343 635 ILE D CA  
15508 C C   . ILE H 124 ? 2.3857 2.6305 2.4633 0.1462  -0.4019 -1.2085 635 ILE D C   
15509 O O   . ILE H 124 ? 2.3835 2.6038 2.4403 0.1269  -0.3728 -1.2021 635 ILE D O   
15510 C CB  . ILE H 124 ? 2.2892 2.6825 2.4250 0.2047  -0.4300 -1.2318 635 ILE D CB  
15511 C CG1 . ILE H 124 ? 2.2814 2.7604 2.4471 0.2523  -0.4606 -1.2500 635 ILE D CG1 
15512 C CG2 . ILE H 124 ? 2.3091 2.6948 2.4237 0.2040  -0.3897 -1.2389 635 ILE D CG2 
15513 C CD1 . ILE H 124 ? 2.3955 2.8868 2.5348 0.2995  -0.4290 -1.2803 635 ILE D CD1 
15514 N N   . SER H 125 ? 2.5797 2.7857 2.6560 0.1260  -0.4239 -1.1924 636 SER D N   
15515 C CA  . SER H 125 ? 2.5782 2.7107 2.6221 0.0816  -0.4096 -1.1673 636 SER D CA  
15516 C C   . SER H 125 ? 2.6845 2.7561 2.6783 0.0724  -0.3618 -1.1748 636 SER D C   
15517 O O   . SER H 125 ? 2.6786 2.7034 2.6426 0.0408  -0.3421 -1.1575 636 SER D O   
15518 C CB  . SER H 125 ? 2.5948 2.6891 2.6385 0.0661  -0.4386 -1.1512 636 SER D CB  
15519 O OG  . SER H 125 ? 2.7102 2.7807 2.7412 0.0868  -0.4347 -1.1701 636 SER D OG  
15520 N N   . ASN H 126 ? 2.6578 2.7286 2.6398 0.1014  -0.3444 -1.1988 637 ASN D N   
15521 C CA  . ASN H 126 ? 2.7737 2.7866 2.7079 0.0948  -0.3018 -1.2042 637 ASN D CA  
15522 C C   . ASN H 126 ? 2.7513 2.7799 2.6797 0.0926  -0.2791 -1.2057 637 ASN D C   
15523 O O   . ASN H 126 ? 2.8086 2.7805 2.6972 0.0716  -0.2512 -1.1987 637 ASN D O   
15524 C CB  . ASN H 126 ? 2.8887 2.9025 2.8140 0.1318  -0.2909 -1.2280 637 ASN D CB  
15525 C CG  . ASN H 126 ? 2.9595 2.9251 2.8713 0.1283  -0.3004 -1.2257 637 ASN D CG  
15526 O OD1 . ASN H 126 ? 2.9108 2.8524 2.8272 0.1010  -0.3228 -1.2070 637 ASN D OD1 
15527 N ND2 . ASN H 126 ? 3.1311 3.0801 3.0247 0.1575  -0.2838 -1.2434 637 ASN D ND2 
15528 N N   . TYR H 127 ? 3.0140 1.9676 2.9422 0.0340  0.9925  -0.0087 638 TYR D N   
15529 C CA  . TYR H 127 ? 2.9868 1.9553 2.9452 0.0305  0.9902  -0.0177 638 TYR D CA  
15530 C C   . TYR H 127 ? 2.8265 1.8082 2.8032 0.0317  0.9834  -0.0262 638 TYR D C   
15531 O O   . TYR H 127 ? 2.7956 1.7915 2.7979 0.0295  0.9792  -0.0342 638 TYR D O   
15532 C CB  . TYR H 127 ? 3.0663 2.0467 3.0298 0.0326  0.9771  -0.0176 638 TYR D CB  
15533 C CG  . TYR H 127 ? 3.2401 2.2090 3.1820 0.0331  0.9805  -0.0086 638 TYR D CG  
15534 C CD1 . TYR H 127 ? 3.3457 2.3047 3.2894 0.0273  0.9948  -0.0069 638 TYR D CD1 
15535 C CD2 . TYR H 127 ? 3.2916 2.2608 3.2126 0.0393  0.9688  -0.0020 638 TYR D CD2 
15536 C CE1 . TYR H 127 ? 3.4993 2.4483 3.4234 0.0277  0.9982  0.0012  638 TYR D CE1 
15537 C CE2 . TYR H 127 ? 3.4407 2.3999 3.3420 0.0397  0.9718  0.0061  638 TYR D CE2 
15538 C CZ  . TYR H 127 ? 3.5476 2.4970 3.4505 0.0340  0.9865  0.0077  638 TYR D CZ  
15539 O OH  . TYR H 127 ? 3.7061 2.6462 3.5891 0.0347  0.9894  0.0157  638 TYR D OH  
15540 N N   . THR H 128 ? 3.0253 2.0027 2.9895 0.0351  0.9824  -0.0247 639 THR D N   
15541 C CA  . THR H 128 ? 2.9490 1.9388 2.9293 0.0366  0.9761  -0.0326 639 THR D CA  
15542 C C   . THR H 128 ? 2.9795 1.9703 2.9829 0.0300  0.9885  -0.0400 639 THR D C   
15543 O O   . THR H 128 ? 2.9536 1.9602 2.9814 0.0291  0.9823  -0.0486 639 THR D O   
15544 C CB  . THR H 128 ? 2.8822 1.8650 2.8433 0.0411  0.9750  -0.0293 639 THR D CB  
15545 O OG1 . THR H 128 ? 2.9877 1.9494 2.9275 0.0393  0.9898  -0.0220 639 THR D OG1 
15546 C CG2 . THR H 128 ? 2.7702 1.7602 2.7177 0.0485  0.9576  -0.0255 639 THR D CG2 
15547 N N   . GLN H 129 ? 2.7771 1.7510 2.7732 0.0253  1.0062  -0.0367 640 GLN D N   
15548 C CA  . GLN H 129 ? 2.7951 1.7681 2.8120 0.0188  1.0193  -0.0431 640 GLN D CA  
15549 C C   . GLN H 129 ? 2.8168 1.8002 2.8577 0.0143  1.0190  -0.0484 640 GLN D C   
15550 O O   . GLN H 129 ? 2.7972 1.7889 2.8629 0.0102  1.0229  -0.0566 640 GLN D O   
15551 C CB  . GLN H 129 ? 2.8801 1.8309 2.8810 0.0153  1.0380  -0.0372 640 GLN D CB  
15552 C CG  . GLN H 129 ? 2.9632 1.9101 2.9818 0.0090  1.0531  -0.0428 640 GLN D CG  
15553 C CD  . GLN H 129 ? 2.8970 1.8507 2.9231 0.0110  1.0505  -0.0488 640 GLN D CD  
15554 O OE1 . GLN H 129 ? 2.8062 1.7623 2.8185 0.0170  1.0404  -0.0469 640 GLN D OE1 
15555 N NE2 . GLN H 129 ? 2.9654 1.9223 3.0137 0.0058  1.0596  -0.0560 640 GLN D NE2 
15556 N N   . ILE H 130 ? 2.8805 1.8638 2.9146 0.0151  1.0143  -0.0439 641 ILE D N   
15557 C CA  . ILE H 130 ? 2.9104 1.9035 2.9662 0.0114  1.0131  -0.0487 641 ILE D CA  
15558 C C   . ILE H 130 ? 2.8305 1.8454 2.9075 0.0141  0.9965  -0.0569 641 ILE D C   
15559 O O   . ILE H 130 ? 2.8107 1.8358 2.9140 0.0102  0.9977  -0.0649 641 ILE D O   
15560 C CB  . ILE H 130 ? 2.9753 1.9620 3.0162 0.0120  1.0123  -0.0414 641 ILE D CB  
15561 C CG1 . ILE H 130 ? 3.0673 2.0318 3.0855 0.0097  1.0285  -0.0328 641 ILE D CG1 
15562 C CG2 . ILE H 130 ? 2.9678 1.9637 3.0311 0.0081  1.0121  -0.0465 641 ILE D CG2 
15563 C CD1 . ILE H 130 ? 3.1503 2.1079 3.1527 0.0103  1.0285  -0.0253 641 ILE D CD1 
15564 N N   . ILE H 131 ? 2.8930 1.9152 2.9591 0.0209  0.9806  -0.0548 642 ILE D N   
15565 C CA  . ILE H 131 ? 2.8019 1.8442 2.8859 0.0243  0.9637  -0.0617 642 ILE D CA  
15566 C C   . ILE H 131 ? 2.7409 1.7916 2.8452 0.0223  0.9656  -0.0704 642 ILE D C   
15567 O O   . ILE H 131 ? 2.7205 1.7865 2.8492 0.0213  0.9588  -0.0785 642 ILE D O   
15568 C CB  . ILE H 131 ? 2.7108 1.7571 2.7765 0.0321  0.9476  -0.0568 642 ILE D CB  
15569 C CG1 . ILE H 131 ? 2.8155 1.8549 2.8623 0.0340  0.9448  -0.0486 642 ILE D CG1 
15570 C CG2 . ILE H 131 ? 2.6155 1.6820 2.6991 0.0358  0.9302  -0.0638 642 ILE D CG2 
15571 C CD1 . ILE H 131 ? 2.7170 1.7603 2.7462 0.0416  0.9290  -0.0436 642 ILE D CD1 
15572 N N   . TYR H 132 ? 2.9364 1.9772 3.0306 0.0220  0.9748  -0.0690 643 TYR D N   
15573 C CA  . TYR H 132 ? 2.8414 1.8897 2.9533 0.0204  0.9769  -0.0769 643 TYR D CA  
15574 C C   . TYR H 132 ? 2.8973 1.9501 3.0363 0.0134  0.9864  -0.0844 643 TYR D C   
15575 O O   . TYR H 132 ? 2.8641 1.9310 3.0257 0.0126  0.9816  -0.0930 643 TYR D O   
15576 C CB  . TYR H 132 ? 2.7902 1.8240 2.8847 0.0207  0.9878  -0.0732 643 TYR D CB  
15577 C CG  . TYR H 132 ? 2.7580 1.7896 2.8289 0.0279  0.9776  -0.0676 643 TYR D CG  
15578 C CD1 . TYR H 132 ? 2.7118 1.7560 2.7811 0.0336  0.9592  -0.0672 643 TYR D CD1 
15579 C CD2 . TYR H 132 ? 2.8165 1.8328 2.8661 0.0291  0.9864  -0.0622 643 TYR D CD2 
15580 C CE1 . TYR H 132 ? 2.6739 1.7160 2.7219 0.0402  0.9501  -0.0620 643 TYR D CE1 
15581 C CE2 . TYR H 132 ? 2.7791 1.7931 2.8071 0.0358  0.9771  -0.0571 643 TYR D CE2 
15582 C CZ  . TYR H 132 ? 2.6528 1.6799 2.6804 0.0412  0.9591  -0.0570 643 TYR D CZ  
15583 O OH  . TYR H 132 ? 2.5202 1.5454 2.5272 0.0477  0.9498  -0.0520 643 TYR D OH  
15584 N N   . GLY H 133 ? 2.8379 1.8793 2.9756 0.0083  0.9995  -0.0813 644 GLY D N   
15585 C CA  . GLY H 133 ? 2.8642 1.9093 3.0279 0.0015  1.0090  -0.0883 644 GLY D CA  
15586 C C   . GLY H 133 ? 2.8844 1.9471 3.0702 0.0016  0.9968  -0.0946 644 GLY D C   
15587 O O   . GLY H 133 ? 2.9240 1.9961 3.1359 -0.0025 0.9993  -0.1030 644 GLY D O   
15588 N N   . LEU H 134 ? 2.8512 1.9183 3.0270 0.0063  0.9835  -0.0907 645 LEU D N   
15589 C CA  . LEU H 134 ? 2.8544 1.9376 3.0495 0.0071  0.9709  -0.0963 645 LEU D CA  
15590 C C   . LEU H 134 ? 2.7344 1.8352 2.9428 0.0112  0.9556  -0.1030 645 LEU D C   
15591 O O   . LEU H 134 ? 2.6747 1.7898 2.9021 0.0116  0.9453  -0.1088 645 LEU D O   
15592 C CB  . LEU H 134 ? 2.8552 1.9364 3.0349 0.0106  0.9626  -0.0896 645 LEU D CB  
15593 C CG  . LEU H 134 ? 2.9266 1.9984 3.1069 0.0056  0.9742  -0.0870 645 LEU D CG  
15594 C CD1 . LEU H 134 ? 3.0109 2.0928 3.2223 0.0003  0.9771  -0.0962 645 LEU D CD1 
15595 C CD2 . LEU H 134 ? 2.9779 2.0297 3.1413 0.0018  0.9929  -0.0806 645 LEU D CD2 
15596 N N   . LEU H 135 ? 2.5244 1.6243 2.7233 0.0143  0.9537  -0.1023 646 LEU D N   
15597 C CA  . LEU H 135 ? 2.5074 1.6235 2.7172 0.0185  0.9392  -0.1081 646 LEU D CA  
15598 C C   . LEU H 135 ? 2.5108 1.6332 2.7429 0.0144  0.9459  -0.1168 646 LEU D C   
15599 O O   . LEU H 135 ? 2.4959 1.6343 2.7495 0.0149  0.9363  -0.1245 646 LEU D O   
15600 C CB  . LEU H 135 ? 2.5060 1.6186 2.6923 0.0250  0.9316  -0.1023 646 LEU D CB  
15601 C CG  . LEU H 135 ? 2.5023 1.6088 2.6642 0.0299  0.9239  -0.0931 646 LEU D CG  
15602 C CD1 . LEU H 135 ? 2.5016 1.6054 2.6431 0.0358  0.9173  -0.0886 646 LEU D CD1 
15603 C CD2 . LEU H 135 ? 2.4823 1.6020 2.6539 0.0326  0.9086  -0.0950 646 LEU D CD2 
15604 N N   . GLU H 136 ? 2.7747 1.8845 3.0020 0.0105  0.9622  -0.1157 647 GLU D N   
15605 C CA  . GLU H 136 ? 2.7949 1.9097 3.0420 0.0066  0.9694  -0.1235 647 GLU D CA  
15606 C C   . GLU H 136 ? 2.9435 2.0610 3.2156 -0.0006 0.9789  -0.1297 647 GLU D C   
15607 O O   . GLU H 136 ? 2.9414 2.0712 3.2377 -0.0028 0.9773  -0.1384 647 GLU D O   
15608 C CB  . GLU H 136 ? 2.7265 1.8265 2.9577 0.0057  0.9826  -0.1198 647 GLU D CB  
15609 C CG  . GLU H 136 ? 2.7770 1.8569 2.9902 0.0026  0.9978  -0.1119 647 GLU D CG  
15610 C CD  . GLU H 136 ? 2.8110 1.8765 3.0095 0.0019  1.0106  -0.1087 647 GLU D CD  
15611 O OE1 . GLU H 136 ? 2.8411 1.8893 3.0178 0.0015  1.0199  -0.1006 647 GLU D OE1 
15612 O OE2 . GLU H 136 ? 2.8222 1.8937 3.0311 0.0017  1.0112  -0.1145 647 GLU D OE2 
15613 N N   . GLU H 137 ? 3.0132 2.1197 3.2801 -0.0042 0.9886  -0.1252 648 GLU D N   
15614 C CA  . GLU H 137 ? 3.0897 2.1966 3.3789 -0.0113 0.9994  -0.1303 648 GLU D CA  
15615 C C   . GLU H 137 ? 3.0523 2.1728 3.3580 -0.0108 0.9878  -0.1344 648 GLU D C   
15616 O O   . GLU H 137 ? 2.9911 2.1242 3.3234 -0.0135 0.9856  -0.1432 648 GLU D O   
15617 C CB  . GLU H 137 ? 3.2739 2.3610 3.5493 -0.0157 1.0172  -0.1235 648 GLU D CB  
15618 C CG  . GLU H 137 ? 3.4209 2.5070 3.7158 -0.0225 1.0277  -0.1269 648 GLU D CG  
15619 C CD  . GLU H 137 ? 3.5110 2.5938 3.7971 -0.0217 1.0244  -0.1217 648 GLU D CD  
15620 O OE1 . GLU H 137 ? 3.5030 2.5883 3.7724 -0.0155 1.0108  -0.1170 648 GLU D OE1 
15621 O OE2 . GLU H 137 ? 3.5856 2.6631 3.8815 -0.0272 1.0355  -0.1223 648 GLU D OE2 
15622 N N   . SER H 138 ? 3.0658 2.1837 3.3559 -0.0071 0.9800  -0.1282 649 SER D N   
15623 C CA  . SER H 138 ? 3.0448 2.1735 3.3485 -0.0066 0.9698  -0.1314 649 SER D CA  
15624 C C   . SER H 138 ? 2.8758 2.0238 3.1945 -0.0023 0.9517  -0.1382 649 SER D C   
15625 O O   . SER H 138 ? 2.9334 2.0927 3.2711 -0.0030 0.9446  -0.1437 649 SER D O   
15626 C CB  . SER H 138 ? 3.0613 2.1821 3.3427 -0.0033 0.9655  -0.1226 649 SER D CB  
15627 O OG  . SER H 138 ? 2.9181 2.0429 3.1822 0.0042  0.9503  -0.1185 649 SER D OG  
15628 N N   . GLN H 139 ? 2.7662 1.9182 3.0762 0.0024  0.9438  -0.1377 650 GLN D N   
15629 C CA  . GLN H 139 ? 2.7458 1.9153 3.0665 0.0074  0.9257  -0.1429 650 GLN D CA  
15630 C C   . GLN H 139 ? 2.7212 1.9020 3.0661 0.0048  0.9266  -0.1525 650 GLN D C   
15631 O O   . GLN H 139 ? 2.7877 1.9779 3.1571 0.0014  0.9264  -0.1599 650 GLN D O   
15632 C CB  . GLN H 139 ? 2.6777 1.8463 2.9751 0.0147  0.9144  -0.1367 650 GLN D CB  
15633 C CG  . GLN H 139 ? 2.6501 1.8112 2.9259 0.0182  0.9094  -0.1281 650 GLN D CG  
15634 C CD  . GLN H 139 ? 2.6770 1.8484 2.9651 0.0194  0.8982  -0.1308 650 GLN D CD  
15635 O OE1 . GLN H 139 ? 2.7218 1.9088 3.0271 0.0216  0.8858  -0.1374 650 GLN D OE1 
15636 N NE2 . GLN H 139 ? 2.7299 1.8928 3.0094 0.0180  0.9025  -0.1258 650 GLN D NE2 
15637 N N   . ASN H 140 ? 3.6890 1.3386 2.4393 0.0984  1.2544  0.2156  651 ASN D N   
15638 C CA  . ASN H 140 ? 3.6355 1.2786 2.3862 0.0910  1.2434  0.2049  651 ASN D CA  
15639 C C   . ASN H 140 ? 3.6868 1.3142 2.4037 0.0860  1.2533  0.1787  651 ASN D C   
15640 O O   . ASN H 140 ? 3.6957 1.3172 2.4101 0.0803  1.2463  0.1677  651 ASN D O   
15641 C CB  . ASN H 140 ? 3.6237 1.2692 2.4002 0.0844  1.2189  0.2094  651 ASN D CB  
15642 C CG  . ASN H 140 ? 3.6172 1.2788 2.4305 0.0875  1.2054  0.2352  651 ASN D CG  
15643 O OD1 . ASN H 140 ? 3.6112 1.2749 2.4479 0.0825  1.1848  0.2401  651 ASN D OD1 
15644 N ND2 . ASN H 140 ? 3.6188 1.2918 2.4375 0.0957  1.2166  0.2516  651 ASN D ND2 
15645 N N   . GLN H 141 ? 3.6907 1.3115 2.3823 0.0879  1.2690  0.1689  652 GLN D N   
15646 C CA  . GLN H 141 ? 3.7575 1.3650 2.4158 0.0834  1.2804  0.1455  652 GLN D CA  
15647 C C   . GLN H 141 ? 3.8761 1.4822 2.5174 0.0897  1.2998  0.1437  652 GLN D C   
15648 O O   . GLN H 141 ? 3.9523 1.5498 2.5717 0.0859  1.3069  0.1270  652 GLN D O   
15649 C CB  . GLN H 141 ? 3.7922 1.3929 2.4313 0.0811  1.2866  0.1356  652 GLN D CB  
15650 C CG  . GLN H 141 ? 3.9197 1.5082 2.5252 0.0750  1.2969  0.1121  652 GLN D CG  
15651 C CD  . GLN H 141 ? 3.8701 1.4549 2.4778 0.0654  1.2824  0.0992  652 GLN D CD  
15652 O OE1 . GLN H 141 ? 3.7745 1.3620 2.4041 0.0613  1.2634  0.1035  652 GLN D OE1 
15653 N NE2 . GLN H 141 ? 3.9045 1.4835 2.4904 0.0619  1.2907  0.0832  652 GLN D NE2 
15654 N N   . GLN H 142 ? 3.8538 1.4691 2.5063 0.0991  1.3077  0.1612  653 GLN D N   
15655 C CA  . GLN H 142 ? 3.8724 1.4877 2.5125 0.1066  1.3259  0.1629  653 GLN D CA  
15656 C C   . GLN H 142 ? 3.8121 1.4367 2.4735 0.1082  1.3185  0.1767  653 GLN D C   
15657 O O   . GLN H 142 ? 3.9108 1.5321 2.5593 0.1104  1.3295  0.1723  653 GLN D O   
15658 C CB  . GLN H 142 ? 3.8628 1.4846 2.5057 0.1166  1.3382  0.1758  653 GLN D CB  
15659 C CG  . GLN H 142 ? 3.9789 1.5915 2.5965 0.1193  1.3538  0.1644  653 GLN D CG  
15660 C CD  . GLN H 142 ? 4.0715 1.6768 2.6640 0.1253  1.3758  0.1557  653 GLN D CD  
15661 O OE1 . GLN H 142 ? 4.1712 1.7656 2.7393 0.1206  1.3826  0.1379  653 GLN D OE1 
15662 N NE2 . GLN H 142 ? 4.1244 1.7362 2.7232 0.1360  1.3871  0.1687  653 GLN D NE2 
15663 N N   . GLU H 143 ? 3.7466 1.3819 2.4401 0.1061  1.2991  0.1928  654 GLU D N   
15664 C CA  . GLU H 143 ? 3.6706 1.3160 2.3875 0.1067  1.2897  0.2083  654 GLU D CA  
15665 C C   . GLU H 143 ? 3.7371 1.3743 2.4521 0.0984  1.2786  0.1955  654 GLU D C   
15666 O O   . GLU H 143 ? 3.8146 1.4520 2.5278 0.0992  1.2821  0.1968  654 GLU D O   
15667 C CB  . GLU H 143 ? 3.6537 1.3144 2.4063 0.1075  1.2729  0.2311  654 GLU D CB  
15668 C CG  . GLU H 143 ? 3.6485 1.3214 2.4299 0.1067  1.2593  0.2497  654 GLU D CG  
15669 C CD  . GLU H 143 ? 3.6411 1.3288 2.4567 0.1070  1.2427  0.2712  654 GLU D CD  
15670 O OE1 . GLU H 143 ? 3.6345 1.3255 2.4741 0.1012  1.2218  0.2778  654 GLU D OE1 
15671 O OE2 . GLU H 143 ? 3.6422 1.3360 2.4591 0.1123  1.2495  0.2787  654 GLU D OE2 
15672 N N   . LYS H 144 ? 3.7718 1.4018 2.4874 0.0905  1.2648  0.1830  655 LYS D N   
15673 C CA  . LYS H 144 ? 3.7989 1.4212 2.5142 0.0825  1.2527  0.1694  655 LYS D CA  
15674 C C   . LYS H 144 ? 3.9272 1.5377 2.6084 0.0812  1.2690  0.1479  655 LYS D C   
15675 O O   . LYS H 144 ? 3.9491 1.5561 2.6290 0.0780  1.2654  0.1412  655 LYS D O   
15676 C CB  . LYS H 144 ? 3.7365 1.3551 2.4619 0.0748  1.2339  0.1613  655 LYS D CB  
15677 C CG  . LYS H 144 ? 3.6254 1.2552 2.3881 0.0749  1.2141  0.1824  655 LYS D CG  
15678 C CD  . LYS H 144 ? 3.6208 1.2455 2.3934 0.0672  1.1949  0.1731  655 LYS D CD  
15679 C CE  . LYS H 144 ? 3.6139 1.2492 2.4245 0.0672  1.1742  0.1939  655 LYS D CE  
15680 N NZ  . LYS H 144 ? 3.6097 1.2477 2.4446 0.0644  1.1573  0.2006  655 LYS D NZ  
15681 N N   . ASN H 145 ? 4.0102 1.6148 2.6642 0.0832  1.2862  0.1369  656 ASN D N   
15682 C CA  . ASN H 145 ? 4.1419 1.7365 2.7631 0.0820  1.3027  0.1178  656 ASN D CA  
15683 C C   . ASN H 145 ? 4.2172 1.8141 2.8349 0.0891  1.3161  0.1260  656 ASN D C   
15684 O O   . ASN H 145 ? 4.2447 1.8351 2.8449 0.0869  1.3229  0.1133  656 ASN D O   
15685 C CB  . ASN H 145 ? 4.1806 1.7692 2.7753 0.0826  1.3177  0.1067  656 ASN D CB  
15686 C CG  . ASN H 145 ? 4.2840 1.8632 2.8466 0.0770  1.3284  0.0841  656 ASN D CG  
15687 O OD1 . ASN H 145 ? 4.3046 1.8819 2.8600 0.0764  1.3323  0.0785  656 ASN D OD1 
15688 N ND2 . ASN H 145 ? 4.2935 1.8681 2.8374 0.0722  1.3324  0.0718  656 ASN D ND2 
15689 N N   . GLU H 146 ? 4.1777 1.7849 2.8119 0.0973  1.3197  0.1473  657 GLU D N   
15690 C CA  . GLU H 146 ? 4.1436 1.7545 2.7765 0.1036  1.3311  0.1565  657 GLU D CA  
15691 C C   . GLU H 146 ? 4.1270 1.7402 2.7772 0.0986  1.3158  0.1606  657 GLU D C   
15692 O O   . GLU H 146 ? 4.2043 1.8132 2.8421 0.0993  1.3241  0.1557  657 GLU D O   
15693 C CB  . GLU H 146 ? 4.0923 1.7167 2.7415 0.1130  1.3370  0.1795  657 GLU D CB  
15694 C CG  . GLU H 146 ? 4.1540 1.7758 2.7859 0.1200  1.3546  0.1763  657 GLU D CG  
15695 C CD  . GLU H 146 ? 4.3506 1.9605 2.9486 0.1238  1.3774  0.1603  657 GLU D CD  
15696 O OE1 . GLU H 146 ? 4.3814 1.9881 2.9710 0.1234  1.3822  0.1563  657 GLU D OE1 
15697 O OE2 . GLU H 146 ? 4.4088 2.0123 2.9886 0.1272  1.3901  0.1519  657 GLU D OE2 
15698 N N   . GLN H 147 ? 4.1835 1.8015 2.8607 0.0930  1.2929  0.1673  658 GLN D N   
15699 C CA  . GLN H 147 ? 4.1360 1.7559 2.8327 0.0883  1.2763  0.1722  658 GLN D CA  
15700 C C   . GLN H 147 ? 4.1799 1.7866 2.8573 0.0816  1.2754  0.1479  658 GLN D C   
15701 O O   . GLN H 147 ? 4.1771 1.7828 2.8598 0.0797  1.2704  0.1486  658 GLN D O   
15702 C CB  . GLN H 147 ? 4.0033 1.6303 2.7339 0.0837  1.2511  0.1836  658 GLN D CB  
15703 C CG  . GLN H 147 ? 3.9176 1.5606 2.6813 0.0867  1.2407  0.2121  658 GLN D CG  
15704 C CD  . GLN H 147 ? 3.7827 1.4313 2.5786 0.0820  1.2157  0.2217  658 GLN D CD  
15705 O OE1 . GLN H 147 ? 3.7855 1.4256 2.5787 0.0767  1.2063  0.2065  658 GLN D OE1 
15706 N NE2 . GLN H 147 ? 3.6638 1.3274 2.4908 0.0836  1.2045  0.2471  658 GLN D NE2 
15707 N N   . ASP H 148 ? 4.1650 1.7627 2.8207 0.0775  1.2792  0.1266  659 ASP D N   
15708 C CA  . ASP H 148 ? 4.2013 1.7898 2.8387 0.0710  1.2787  0.1036  659 ASP D CA  
15709 C C   . ASP H 148 ? 4.2794 1.8638 2.8928 0.0752  1.2992  0.0993  659 ASP D C   
15710 O O   . ASP H 148 ? 4.2922 1.8721 2.8979 0.0712  1.2973  0.0873  659 ASP D O   
15711 C CB  . ASP H 148 ? 4.1799 1.7629 2.7984 0.0651  1.2794  0.0833  659 ASP D CB  
15712 C CG  . ASP H 148 ? 4.2069 1.7848 2.8088 0.0575  1.2769  0.0596  659 ASP D CG  
15713 O OD1 . ASP H 148 ? 4.1403 1.7185 2.7588 0.0511  1.2566  0.0524  659 ASP D OD1 
15714 O OD2 . ASP H 148 ? 4.3032 1.8779 2.8765 0.0577  1.2944  0.0482  659 ASP D OD2 
15715 N N   . LEU H 149 ? 4.1419 1.7283 2.7441 0.0835  1.3185  0.1087  660 LEU D N   
15716 C CA  . LEU H 149 ? 4.1808 1.7634 2.7611 0.0889  1.3392  0.1068  660 LEU D CA  
15717 C C   . LEU H 149 ? 4.2068 1.7966 2.8067 0.0931  1.3362  0.1267  660 LEU D C   
15718 O O   . LEU H 149 ? 4.2261 1.8121 2.8118 0.0954  1.3479  0.1239  660 LEU D O   
15719 C CB  . LEU H 149 ? 4.2171 1.7981 2.7767 0.0963  1.3611  0.1067  660 LEU D CB  
15720 C CG  . LEU H 149 ? 4.2178 1.7900 2.7453 0.0920  1.3725  0.0844  660 LEU D CG  
15721 C CD1 . LEU H 149 ? 4.1633 1.7356 2.6959 0.0826  1.3559  0.0740  660 LEU D CD1 
15722 C CD2 . LEU H 149 ? 4.2613 1.8315 2.7711 0.1001  1.3936  0.0864  660 LEU D CD2 
15723 N N   . LEU H 150 ? 4.1796 1.7812 2.8120 0.0940  1.3210  0.1480  661 LEU D N   
15724 C CA  . LEU H 150 ? 4.1731 1.7856 2.8262 0.0971  1.3171  0.1702  661 LEU D CA  
15725 C C   . LEU H 150 ? 4.1197 1.7303 2.7897 0.0895  1.2972  0.1692  661 LEU D C   
15726 O O   . LEU H 150 ? 4.1099 1.7269 2.7917 0.0904  1.2949  0.1839  661 LEU D O   
15727 C CB  . LEU H 150 ? 4.1176 1.7467 2.7992 0.1011  1.3095  0.1951  661 LEU D CB  
15728 C CG  . LEU H 150 ? 4.1621 1.7934 2.8292 0.1092  1.3282  0.1961  661 LEU D CG  
15729 C CD1 . LEU H 150 ? 4.0659 1.7134 2.7604 0.1127  1.3201  0.2180  661 LEU D CD1 
15730 C CD2 . LEU H 150 ? 4.2739 1.9003 2.9122 0.1165  1.3540  0.1895  661 LEU D CD2 
15731 N N   . ALA H 151 ? 4.1198 1.7225 2.7917 0.0819  1.2824  0.1523  662 ALA D N   
15732 C CA  . ALA H 151 ? 4.0712 1.6711 2.7611 0.0745  1.2606  0.1481  662 ALA D CA  
15733 C C   . ALA H 151 ? 4.1149 1.7030 2.7814 0.0705  1.2654  0.1243  662 ALA D C   
15734 O O   . ALA H 151 ? 4.0916 1.6773 2.7723 0.0652  1.2486  0.1204  662 ALA D O   
15735 C CB  . ALA H 151 ? 4.0078 1.6080 2.7168 0.0688  1.2395  0.1433  662 ALA D CB  
15736 N N   . LEU H 152 ? 4.1587 1.7402 2.7911 0.0729  1.2870  0.1083  663 LEU D N   
15737 C CA  . LEU H 152 ? 4.1765 1.7496 2.7861 0.0688  1.2920  0.0855  663 LEU D CA  
15738 C C   . LEU H 152 ? 4.2808 1.8518 2.8846 0.0721  1.3014  0.0924  663 LEU D C   
15739 O O   . LEU H 152 ? 4.2669 1.8326 2.8616 0.0677  1.2985  0.0770  663 LEU D O   
15740 C CB  . LEU H 152 ? 4.2163 1.7854 2.7920 0.0690  1.3108  0.0672  663 LEU D CB  
15741 C CG  . LEU H 152 ? 4.2349 1.8031 2.7907 0.0781  1.3369  0.0761  663 LEU D CG  
15742 C CD1 . LEU H 152 ? 4.2196 1.7825 2.7522 0.0811  1.3548  0.0710  663 LEU D CD1 
15743 C CD2 . LEU H 152 ? 4.1523 1.7193 2.6878 0.0781  1.3483  0.0661  663 LEU D CD2 
15744 N N   . ASP H 153 ? 4.3092 1.8861 2.9182 0.0793  1.3122  0.1149  664 ASP D N   
15745 C CA  . ASP H 153 ? 4.3067 1.8831 2.9104 0.0823  1.3214  0.1235  664 ASP D CA  
15746 C C   . ASP H 153 ? 4.2521 1.8365 2.8892 0.0792  1.3010  0.1440  664 ASP D C   
15747 O O   . ASP H 153 ? 4.2478 1.8361 2.8864 0.0813  1.3061  0.1575  664 ASP D O   
15748 C CB  . ASP H 153 ? 4.3228 1.9039 2.9116 0.0918  1.3456  0.1355  664 ASP D CB  
15749 C CG  . ASP H 153 ? 4.3104 1.9063 2.9223 0.0963  1.3415  0.1584  664 ASP D CG  
15750 O OD1 . ASP H 153 ? 4.2910 1.8950 2.9338 0.0921  1.3197  0.1712  664 ASP D OD1 
15751 O OD2 . ASP H 153 ? 4.3857 1.9854 2.9855 0.1039  1.3593  0.1627  664 ASP D OD2 
15752 N N   . ASP I 1   ? 2.1848 2.7644 3.0138 0.2097  0.0723  0.8938  1   ASP H N   
15753 C CA  . ASP I 1   ? 2.0827 2.6887 2.9125 0.2736  0.0732  0.8634  1   ASP H CA  
15754 C C   . ASP I 1   ? 2.0528 2.7440 2.8630 0.2797  0.0680  0.8291  1   ASP H C   
15755 O O   . ASP I 1   ? 2.1047 2.8396 2.9009 0.2324  0.0657  0.8226  1   ASP H O   
15756 C CB  . ASP I 1   ? 2.1382 2.7525 2.9756 0.2915  0.0849  0.8217  1   ASP H CB  
15757 C CG  . ASP I 1   ? 2.2861 2.8240 3.1419 0.2755  0.0910  0.8500  1   ASP H CG  
15758 O OD1 . ASP I 1   ? 2.1956 2.6680 3.0602 0.2594  0.0856  0.9040  1   ASP H OD1 
15759 O OD2 . ASP I 1   ? 2.4573 3.0009 3.3188 0.2790  0.1011  0.8177  1   ASP H OD2 
15760 N N   . ILE I 2   ? 2.0167 2.7303 2.8261 0.3380  0.0660  0.8080  2   ILE H N   
15761 C CA  . ILE I 2   ? 1.9858 2.7821 2.7781 0.3523  0.0615  0.7693  2   ILE H CA  
15762 C C   . ILE I 2   ? 1.9793 2.8322 2.7686 0.3704  0.0702  0.7064  2   ILE H C   
15763 O O   . ILE I 2   ? 1.9773 2.8006 2.7783 0.4079  0.0761  0.6967  2   ILE H O   
15764 C CB  . ILE I 2   ? 1.9492 2.7329 2.7413 0.4048  0.0517  0.7900  2   ILE H CB  
15765 C CG1 . ILE I 2   ? 1.9550 2.6917 2.7479 0.3824  0.0425  0.8498  2   ILE H CG1 
15766 C CG2 . ILE I 2   ? 1.9159 2.7856 2.6918 0.4269  0.0475  0.7444  2   ILE H CG2 
15767 C CD1 . ILE I 2   ? 1.9226 2.6321 2.7181 0.4342  0.0333  0.8779  2   ILE H CD1 
15768 N N   . GLN I 3   ? 1.9768 2.9108 2.7507 0.3430  0.0711  0.6636  3   GLN H N   
15769 C CA  . GLN I 3   ? 1.9704 2.9666 2.7400 0.3561  0.0786  0.6010  3   GLN H CA  
15770 C C   . GLN I 3   ? 1.9293 2.9867 2.6888 0.4020  0.0723  0.5672  3   GLN H C   
15771 O O   . GLN I 3   ? 1.9128 3.0063 2.6608 0.3936  0.0637  0.5722  3   GLN H O   
15772 C CB  . GLN I 3   ? 2.0511 3.1001 2.8110 0.2952  0.0845  0.5712  3   GLN H CB  
15773 C CG  . GLN I 3   ? 2.1915 3.1902 2.9610 0.2524  0.0929  0.5897  3   GLN H CG  
15774 C CD  . GLN I 3   ? 2.1721 3.1149 2.9436 0.2108  0.0876  0.6487  3   GLN H CD  
15775 O OE1 . GLN I 3   ? 2.1164 3.0896 2.8754 0.1798  0.0810  0.6588  3   GLN H OE1 
15776 N NE2 . GLN I 3   ? 2.2303 3.0910 3.0177 0.2092  0.0904  0.6878  3   GLN H NE2 
15777 N N   . LEU I 4   ? 1.9135 2.9818 2.6774 0.4502  0.0764  0.5328  4   LEU H N   
15778 C CA  . LEU I 4   ? 1.8770 3.0074 2.6315 0.4947  0.0714  0.4922  4   LEU H CA  
15779 C C   . LEU I 4   ? 1.8802 3.0861 2.6275 0.4825  0.0785  0.4278  4   LEU H C   
15780 O O   . LEU I 4   ? 1.8981 3.0910 2.6532 0.4815  0.0884  0.4084  4   LEU H O   
15781 C CB  . LEU I 4   ? 1.8552 2.9432 2.6188 0.5617  0.0697  0.5000  4   LEU H CB  
15782 C CG  . LEU I 4   ? 1.8481 2.8605 2.6199 0.5838  0.0627  0.5609  4   LEU H CG  
15783 C CD1 . LEU I 4   ? 1.8275 2.8051 2.6074 0.6502  0.0625  0.5603  4   LEU H CD1 
15784 C CD2 . LEU I 4   ? 1.8279 2.8675 2.5881 0.5774  0.0509  0.5791  4   LEU H CD2 
15785 N N   . THR I 5   ? 1.8627 3.1476 2.5958 0.4733  0.0735  0.3947  5   THR H N   
15786 C CA  . THR I 5   ? 1.8632 3.2278 2.5885 0.4606  0.0790  0.3318  5   THR H CA  
15787 C C   . THR I 5   ? 1.8256 3.2434 2.5447 0.5156  0.0730  0.2913  5   THR H C   
15788 O O   . THR I 5   ? 1.8001 3.2425 2.5113 0.5311  0.0626  0.2981  5   THR H O   
15789 C CB  . THR I 5   ? 1.8768 3.2949 2.5905 0.3991  0.0786  0.3225  5   THR H CB  
15790 O OG1 . THR I 5   ? 1.9123 3.2763 2.6310 0.3484  0.0830  0.3641  5   THR H OG1 
15791 C CG2 . THR I 5   ? 1.8801 3.3773 2.5873 0.3838  0.0855  0.2577  5   THR H CG2 
15792 N N   . GLN I 6   ? 1.8227 3.2577 2.5454 0.5446  0.0792  0.2495  6   GLN H N   
15793 C CA  . GLN I 6   ? 1.7895 3.2734 2.5067 0.5978  0.0738  0.2080  6   GLN H CA  
15794 C C   . GLN I 6   ? 1.7864 3.3643 2.4938 0.5785  0.0760  0.1454  6   GLN H C   
15795 O O   . GLN I 6   ? 1.8121 3.4080 2.5207 0.5387  0.0857  0.1235  6   GLN H O   
15796 C CB  . GLN I 6   ? 1.7857 3.2262 2.5130 0.6486  0.0782  0.2024  6   GLN H CB  
15797 C CG  . GLN I 6   ? 1.7814 3.1357 2.5179 0.6787  0.0744  0.2597  6   GLN H CG  
15798 C CD  . GLN I 6   ? 1.7746 3.0905 2.5197 0.7326  0.0780  0.2521  6   GLN H CD  
15799 O OE1 . GLN I 6   ? 1.7946 3.0413 2.5522 0.7321  0.0850  0.2810  6   GLN H OE1 
15800 N NE2 . GLN I 6   ? 1.7468 3.1072 2.4851 0.7793  0.0731  0.2130  6   GLN H NE2 
15801 N N   . SER I 7   ? 2.0109 3.6484 2.7089 0.6075  0.0668  0.1165  7   SER H N   
15802 C CA  . SER I 7   ? 2.0204 3.7509 2.7096 0.5960  0.0675  0.0546  7   SER H CA  
15803 C C   . SER I 7   ? 1.9161 3.6894 2.6006 0.6559  0.0592  0.0169  7   SER H C   
15804 O O   . SER I 7   ? 1.8187 3.5707 2.5016 0.6942  0.0492  0.0412  7   SER H O   
15805 C CB  . SER I 7   ? 2.0226 3.8014 2.7020 0.5451  0.0638  0.0565  7   SER H CB  
15806 O OG  . SER I 7   ? 1.9313 3.7005 2.6060 0.5623  0.0520  0.0889  7   SER H OG  
15807 N N   . PRO I 8   ? 1.8866 3.7206 2.5690 0.6638  0.0631  -0.0429 8   PRO H N   
15808 C CA  . PRO I 8   ? 1.9988 3.8547 2.6837 0.6225  0.0755  -0.0726 8   PRO H CA  
15809 C C   . PRO I 8   ? 2.0729 3.8594 2.7695 0.6331  0.0854  -0.0568 8   PRO H C   
15810 O O   . PRO I 8   ? 2.0226 3.7533 2.7248 0.6794  0.0825  -0.0320 8   PRO H O   
15811 C CB  . PRO I 8   ? 1.9659 3.9093 2.6446 0.6407  0.0737  -0.1413 8   PRO H CB  
15812 C CG  . PRO I 8   ? 1.8499 3.7862 2.5276 0.7079  0.0636  -0.1447 8   PRO H CG  
15813 C CD  . PRO I 8   ? 1.8201 3.7070 2.4970 0.7153  0.0549  -0.0867 8   PRO H CD  
15814 N N   . SER I 9   ? 2.1654 3.9550 2.8656 0.5904  0.0971  -0.0708 9   SER H N   
15815 C CA  . SER I 9   ? 2.2511 3.9802 2.9627 0.6006  0.1070  -0.0613 9   SER H CA  
15816 C C   . SER I 9   ? 2.2149 3.9688 2.9275 0.6506  0.1082  -0.1086 9   SER H C   
15817 O O   . SER I 9   ? 2.2209 3.9174 2.9421 0.6849  0.1117  -0.0948 9   SER H O   
15818 C CB  . SER I 9   ? 2.3905 4.1161 3.1050 0.5394  0.1187  -0.0627 9   SER H CB  
15819 O OG  . SER I 9   ? 2.4310 4.1092 3.1471 0.4984  0.1183  -0.0086 9   SER H OG  
15820 N N   . PHE I 10  ? 2.0882 3.9268 2.7925 0.6554  0.1053  -0.1645 10  PHE H N   
15821 C CA  . PHE I 10  ? 2.0387 3.9082 2.7428 0.7030  0.1050  -0.2127 10  PHE H CA  
15822 C C   . PHE I 10  ? 1.9229 3.8654 2.6166 0.7285  0.0929  -0.2470 10  PHE H C   
15823 O O   . PHE I 10  ? 1.9304 3.9423 2.6173 0.6945  0.0918  -0.2761 10  PHE H O   
15824 C CB  . PHE I 10  ? 2.1386 4.0385 2.8455 0.6774  0.1171  -0.2563 10  PHE H CB  
15825 C CG  . PHE I 10  ? 2.2606 4.0889 2.9782 0.6553  0.1289  -0.2254 10  PHE H CG  
15826 C CD1 . PHE I 10  ? 2.3677 4.1815 3.0869 0.5938  0.1356  -0.2019 10  PHE H CD1 
15827 C CD2 . PHE I 10  ? 2.2613 4.0355 2.9873 0.6963  0.1329  -0.2195 10  PHE H CD2 
15828 C CE1 . PHE I 10  ? 2.4867 4.2334 3.2162 0.5741  0.1458  -0.1734 10  PHE H CE1 
15829 C CE2 . PHE I 10  ? 2.3771 4.0852 3.1138 0.6769  0.1436  -0.1915 10  PHE H CE2 
15830 C CZ  . PHE I 10  ? 2.4987 4.1928 3.2374 0.6160  0.1498  -0.1684 10  PHE H CZ  
15831 N N   . LEU I 11  ? 2.2057 4.1320 2.8983 0.7879  0.0840  -0.2437 11  LEU H N   
15832 C CA  . LEU I 11  ? 2.0943 4.0798 2.7777 0.8195  0.0709  -0.2702 11  LEU H CA  
15833 C C   . LEU I 11  ? 2.0682 4.0871 2.7504 0.8670  0.0694  -0.3220 11  LEU H C   
15834 O O   . LEU I 11  ? 2.0207 3.9877 2.7079 0.9055  0.0717  -0.3125 11  LEU H O   
15835 C CB  . LEU I 11  ? 2.0284 3.9670 2.7102 0.8503  0.0601  -0.2212 11  LEU H CB  
15836 C CG  . LEU I 11  ? 2.0369 4.0289 2.7088 0.8694  0.0456  -0.2327 11  LEU H CG  
15837 C CD1 . LEU I 11  ? 2.0033 3.9422 2.6747 0.8718  0.0385  -0.1719 11  LEU H CD1 
15838 C CD2 . LEU I 11  ? 2.0117 4.0327 2.6796 0.9309  0.0374  -0.2714 11  LEU H CD2 
15839 N N   . SER I 12  ? 2.1230 4.2283 2.7986 0.8637  0.0655  -0.3768 12  SER H N   
15840 C CA  . SER I 12  ? 2.1171 4.2631 2.7904 0.9080  0.0622  -0.4298 12  SER H CA  
15841 C C   . SER I 12  ? 2.1025 4.2781 2.7681 0.9539  0.0461  -0.4382 12  SER H C   
15842 O O   . SER I 12  ? 2.1361 4.3569 2.7958 0.9363  0.0385  -0.4404 12  SER H O   
15843 C CB  . SER I 12  ? 2.1807 4.4044 2.8529 0.8756  0.0683  -0.4885 12  SER H CB  
15844 O OG  . SER I 12  ? 2.1959 4.3922 2.8748 0.8337  0.0832  -0.4819 12  SER H OG  
15845 N N   . ALA I 13  ? 2.3573 4.5070 3.0223 1.0124  0.0409  -0.4432 13  ALA H N   
15846 C CA  . ALA I 13  ? 2.3445 4.5169 3.0019 1.0603  0.0252  -0.4507 13  ALA H CA  
15847 C C   . ALA I 13  ? 2.3469 4.4756 2.9800 1.0929  0.0189  -0.4756 13  ALA H C   
15848 O O   . ALA I 13  ? 2.3215 4.4196 2.9633 1.1018  0.0290  -0.4798 13  ALA H O   
15849 C CB  . ALA I 13  ? 2.2969 4.4057 2.9538 1.0744  0.0187  -0.3884 13  ALA H CB  
15850 N N   . SER I 14  ? 2.4281 4.5351 3.0206 1.0987  0.0006  -0.4872 14  SER H N   
15851 C CA  . SER I 14  ? 2.4508 4.4982 3.0053 1.1149  -0.0100 -0.5048 14  SER H CA  
15852 C C   . SER I 14  ? 2.4137 4.3577 2.9438 1.1348  -0.0187 -0.4577 14  SER H C   
15853 O O   . SER I 14  ? 2.3842 4.3087 2.9170 1.1350  -0.0218 -0.4189 14  SER H O   
15854 C CB  . SER I 14  ? 2.5285 4.6236 3.0529 1.1060  -0.0251 -0.5517 14  SER H CB  
15855 O OG  . SER I 14  ? 2.5652 4.7536 3.1100 1.0842  -0.0168 -0.5978 14  SER H OG  
15856 N N   . VAL I 15  ? 2.3553 4.2333 2.8627 1.1492  -0.0219 -0.4610 15  VAL H N   
15857 C CA  . VAL I 15  ? 2.3330 4.1165 2.8115 1.1630  -0.0311 -0.4245 15  VAL H CA  
15858 C C   . VAL I 15  ? 2.3733 4.1654 2.8223 1.1589  -0.0474 -0.4249 15  VAL H C   
15859 O O   . VAL I 15  ? 2.4375 4.2800 2.8673 1.1528  -0.0579 -0.4661 15  VAL H O   
15860 C CB  . VAL I 15  ? 2.3438 4.0734 2.7991 1.1740  -0.0338 -0.4392 15  VAL H CB  
15861 C CG1 . VAL I 15  ? 2.3304 3.9706 2.7536 1.1832  -0.0434 -0.4066 15  VAL H CG1 
15862 C CG2 . VAL I 15  ? 2.3014 4.0150 2.7862 1.1786  -0.0167 -0.4344 15  VAL H CG2 
15863 N N   . GLY I 16  ? 2.4187 4.1598 2.8639 1.1616  -0.0498 -0.3790 16  GLY H N   
15864 C CA  . GLY I 16  ? 2.4507 4.1936 2.8693 1.1575  -0.0637 -0.3741 16  GLY H CA  
15865 C C   . GLY I 16  ? 2.4471 4.2484 2.8875 1.1453  -0.0622 -0.3622 16  GLY H C   
15866 O O   . GLY I 16  ? 2.4608 4.2507 2.8817 1.1424  -0.0721 -0.3474 16  GLY H O   
15867 N N   . ASP I 17  ? 2.3326 4.1973 2.8131 1.1365  -0.0499 -0.3679 17  ASP H N   
15868 C CA  . ASP I 17  ? 2.3332 4.2628 2.8377 1.1216  -0.0480 -0.3572 17  ASP H CA  
15869 C C   . ASP I 17  ? 2.2735 4.1458 2.7878 1.1252  -0.0467 -0.2960 17  ASP H C   
15870 O O   . ASP I 17  ? 2.2178 4.0148 2.7376 1.1366  -0.0408 -0.2612 17  ASP H O   
15871 C CB  . ASP I 17  ? 2.3328 4.3480 2.8802 1.1075  -0.0333 -0.3789 17  ASP H CB  
15872 C CG  . ASP I 17  ? 2.4026 4.4990 2.9435 1.0942  -0.0356 -0.4414 17  ASP H CG  
15873 O OD1 . ASP I 17  ? 2.4552 4.5441 2.9585 1.0975  -0.0503 -0.4666 17  ASP H OD1 
15874 O OD2 . ASP I 17  ? 2.4067 4.5757 2.9804 1.0784  -0.0224 -0.4653 17  ASP H OD2 
15875 N N   . LYS I 18  ? 2.1516 4.0595 2.6674 1.1139  -0.0527 -0.2833 18  LYS H N   
15876 C CA  . LYS I 18  ? 2.0980 3.9786 2.6331 1.1115  -0.0503 -0.2277 18  LYS H CA  
15877 C C   . LYS I 18  ? 2.0815 4.0440 2.6657 1.0973  -0.0381 -0.2245 18  LYS H C   
15878 O O   . LYS I 18  ? 2.1270 4.1866 2.7236 1.0792  -0.0374 -0.2602 18  LYS H O   
15879 C CB  . LYS I 18  ? 2.1243 4.0039 2.6365 1.1046  -0.0628 -0.2151 18  LYS H CB  
15880 C CG  . LYS I 18  ? 2.0735 3.9315 2.6054 1.0991  -0.0615 -0.1582 18  LYS H CG  
15881 C CD  . LYS I 18  ? 2.1036 3.9612 2.6113 1.0913  -0.0736 -0.1489 18  LYS H CD  
15882 C CE  . LYS I 18  ? 2.0527 3.8861 2.5791 1.0845  -0.0729 -0.0909 18  LYS H CE  
15883 N NZ  . LYS I 18  ? 2.0753 3.8928 2.5746 1.0780  -0.0841 -0.0793 18  LYS H NZ  
15884 N N   . VAL I 19  ? 3.0126 3.5064 2.5164 0.4607  -0.0428 -0.5811 19  VAL H N   
15885 C CA  . VAL I 19  ? 3.0013 3.5152 2.4998 0.4551  -0.0242 -0.5699 19  VAL H CA  
15886 C C   . VAL I 19  ? 2.9419 3.4756 2.4369 0.4542  -0.0056 -0.5502 19  VAL H C   
15887 O O   . VAL I 19  ? 2.8999 3.4083 2.3788 0.4563  -0.0015 -0.5385 19  VAL H O   
15888 C CB  . VAL I 19  ? 3.0322 3.4920 2.4880 0.4496  -0.0138 -0.5592 19  VAL H CB  
15889 C CG1 . VAL I 19  ? 3.1116 3.5585 2.5717 0.4498  -0.0332 -0.5790 19  VAL H CG1 
15890 C CG2 . VAL I 19  ? 2.9822 3.3804 2.3944 0.4473  -0.0025 -0.5411 19  VAL H CG2 
15891 N N   . THR I 20  ? 2.7836 3.3657 2.2946 0.4509  0.0050  -0.5466 20  THR H N   
15892 C CA  . THR I 20  ? 2.7365 3.3476 2.2468 0.4500  0.0221  -0.5277 20  THR H CA  
15893 C C   . THR I 20  ? 2.7378 3.3523 2.2324 0.4467  0.0413  -0.5121 20  THR H C   
15894 O O   . THR I 20  ? 2.7841 3.4244 2.2932 0.4437  0.0382  -0.5226 20  THR H O   
15895 C CB  . THR I 20  ? 2.7484 3.4322 2.3019 0.4484  0.0139  -0.5410 20  THR H CB  
15896 O OG1 . THR I 20  ? 2.7502 3.4299 2.3200 0.4518  -0.0024 -0.5562 20  THR H OG1 
15897 C CG2 . THR I 20  ? 2.7051 3.4232 2.2564 0.4466  0.0304  -0.5207 20  THR H CG2 
15898 N N   . ILE I 21  ? 2.6698 3.2592 2.1368 0.4477  0.0618  -0.4876 21  ILE H N   
15899 C CA  . ILE I 21  ? 2.6712 3.2659 2.1255 0.4461  0.0830  -0.4706 21  ILE H CA  
15900 C C   . ILE I 21  ? 2.6352 3.2819 2.1023 0.4479  0.0951  -0.4532 21  ILE H C   
15901 O O   . ILE I 21  ? 2.5933 3.2484 2.0648 0.4505  0.0924  -0.4487 21  ILE H O   
15902 C CB  . ILE I 21  ? 2.6575 3.1785 2.0697 0.4451  0.1006  -0.4567 21  ILE H CB  
15903 C CG1 . ILE I 21  ? 2.5998 3.0878 1.9929 0.4482  0.1107  -0.4408 21  ILE H CG1 
15904 C CG2 . ILE I 21  ? 2.6985 3.1722 2.0961 0.4412  0.0871  -0.4740 21  ILE H CG2 
15905 C CD1 . ILE I 21  ? 2.5887 3.0075 1.9426 0.4451  0.1316  -0.4281 21  ILE H CD1 
15906 N N   . THR I 22  ? 2.5540 3.2380 2.0272 0.4464  0.1080  -0.4429 22  THR H N   
15907 C CA  . THR I 22  ? 2.5353 3.2866 2.0273 0.4464  0.1156  -0.4287 22  THR H CA  
15908 C C   . THR I 22  ? 2.5118 3.2527 1.9845 0.4507  0.1427  -0.3987 22  THR H C   
15909 O O   . THR I 22  ? 2.5321 3.2369 1.9872 0.4510  0.1560  -0.3935 22  THR H O   
15910 C CB  . THR I 22  ? 2.5889 3.4112 2.1132 0.4396  0.1054  -0.4435 22  THR H CB  
15911 O OG1 . THR I 22  ? 2.6110 3.4474 2.1587 0.4360  0.0826  -0.4716 22  THR H OG1 
15912 C CG2 . THR I 22  ? 2.5777 3.4745 2.1192 0.4369  0.1138  -0.4272 22  THR H CG2 
15913 N N   . CYS I 23  ? 2.5268 3.3005 2.0046 0.4539  0.1518  -0.3788 23  CYS H N   
15914 C CA  . CYS I 23  ? 2.5068 3.2856 1.9752 0.4594  0.1783  -0.3472 23  CYS H CA  
15915 C C   . CYS I 23  ? 2.5066 3.3759 2.0017 0.4571  0.1783  -0.3338 23  CYS H C   
15916 O O   . CYS I 23  ? 2.4805 3.3840 1.9884 0.4550  0.1668  -0.3369 23  CYS H O   
15917 C CB  . CYS I 23  ? 2.4514 3.1724 1.8962 0.4662  0.1920  -0.3313 23  CYS H CB  
15918 S SG  . CYS I 23  ? 2.4243 3.1459 1.8619 0.4750  0.2284  -0.2900 23  CYS H SG  
15919 N N   . ARG I 24  ? 2.3659 3.2762 1.8700 0.4561  0.1910  -0.3187 24  ARG H N   
15920 C CA  . ARG I 24  ? 2.3721 3.3742 1.9013 0.4514  0.1917  -0.3029 24  ARG H CA  
15921 C C   . ARG I 24  ? 2.3515 3.3654 1.8777 0.4594  0.2192  -0.2617 24  ARG H C   
15922 O O   . ARG I 24  ? 2.3647 3.3369 1.8784 0.4655  0.2394  -0.2490 24  ARG H O   
15923 C CB  . ARG I 24  ? 2.4379 3.4951 1.9874 0.4414  0.1815  -0.3181 24  ARG H CB  
15924 C CG  . ARG I 24  ? 2.4680 3.5245 2.0291 0.4332  0.1559  -0.3574 24  ARG H CG  
15925 C CD  . ARG I 24  ? 2.5316 3.6618 2.1191 0.4213  0.1470  -0.3696 24  ARG H CD  
15926 N NE  . ARG I 24  ? 2.5283 3.7435 2.1394 0.4108  0.1409  -0.3654 24  ARG H NE  
15927 C CZ  . ARG I 24  ? 2.5474 3.8002 2.1807 0.3995  0.1224  -0.3932 24  ARG H CZ  
15928 N NH1 . ARG I 24  ? 2.5721 3.7863 2.2098 0.3992  0.1080  -0.4252 24  ARG H NH1 
15929 N NH2 . ARG I 24  ? 2.5440 3.8752 2.1970 0.3875  0.1191  -0.3883 24  ARG H NH2 
15930 N N   . ALA I 25  ? 2.2814 3.3540 1.8216 0.4586  0.2207  -0.2401 25  ALA H N   
15931 C CA  . ALA I 25  ? 2.2624 3.3595 1.8079 0.4659  0.2458  -0.1960 25  ALA H CA  
15932 C C   . ALA I 25  ? 2.3050 3.4995 1.8775 0.4566  0.2457  -0.1776 25  ALA H C   
15933 O O   . ALA I 25  ? 2.3250 3.5847 1.9138 0.4430  0.2247  -0.1947 25  ALA H O   
15934 C CB  . ALA I 25  ? 2.1983 3.2960 1.7419 0.4712  0.2488  -0.1778 25  ALA H CB  
15935 N N   . SER I 26  ? 2.2448 3.4500 1.8244 0.4627  0.2703  -0.1420 26  SER H N   
15936 C CA  . SER I 26  ? 2.2902 3.5897 1.8971 0.4532  0.2715  -0.1179 26  SER H CA  
15937 C C   . SER I 26  ? 2.2801 3.6574 1.9062 0.4471  0.2680  -0.0883 26  SER H C   
15938 O O   . SER I 26  ? 2.3234 3.7914 1.9719 0.4325  0.2594  -0.0765 26  SER H O   
15939 C CB  . SER I 26  ? 2.3235 3.6104 1.9373 0.4617  0.3003  -0.0846 26  SER H CB  
15940 O OG  . SER I 26  ? 2.2770 3.5324 1.8926 0.4751  0.3264  -0.0465 26  SER H OG  
15941 N N   . GLN I 27  ? 2.1806 3.5255 1.7982 0.4563  0.2742  -0.0754 27  GLN H N   
15942 C CA  . GLN I 27  ? 2.1448 3.5574 1.7784 0.4500  0.2687  -0.0503 27  GLN H CA  
15943 C C   . GLN I 27  ? 2.0846 3.4507 1.7000 0.4536  0.2565  -0.0757 27  GLN H C   
15944 O O   . GLN I 27  ? 2.0656 3.3426 1.6571 0.4634  0.2578  -0.1011 27  GLN H O   
15945 C CB  . GLN I 27  ? 2.1296 3.5609 1.7811 0.4595  0.2955  0.0101  27  GLN H CB  
15946 C CG  . GLN I 27  ? 2.1894 3.6905 1.8690 0.4522  0.3047  0.0447  27  GLN H CG  
15947 C CD  . GLN I 27  ? 2.2135 3.8290 1.9156 0.4299  0.2838  0.0545  27  GLN H CD  
15948 O OE1 . GLN I 27  ? 2.1778 3.8235 1.8774 0.4203  0.2657  0.0402  27  GLN H OE1 
15949 N NE2 . GLN I 27  ? 2.3008 3.9814 2.0260 0.4197  0.2866  0.0793  27  GLN H NE2 
15950 N N   . GLY I 28  ? 1.9362 3.3649 1.5639 0.4437  0.2442  -0.0681 28  GLY H N   
15951 C CA  . GLY I 28  ? 1.9343 3.3263 1.5483 0.4459  0.2323  -0.0909 28  GLY H CA  
15952 C C   . GLY I 28  ? 1.9520 3.2697 1.5499 0.4653  0.2523  -0.0682 28  GLY H C   
15953 O O   . GLY I 28  ? 1.9569 3.2956 1.5671 0.4724  0.2721  -0.0213 28  GLY H O   
15954 N N   . VAL I 29  ? 2.1754 3.4058 1.7484 0.4731  0.2477  -0.0999 29  VAL H N   
15955 C CA  . VAL I 29  ? 2.1251 3.2790 1.6802 0.4891  0.2649  -0.0852 29  VAL H CA  
15956 C C   . VAL I 29  ? 2.0721 3.2054 1.6171 0.4888  0.2497  -0.1029 29  VAL H C   
15957 O O   . VAL I 29  ? 2.0354 3.0948 1.5613 0.5000  0.2591  -0.1017 29  VAL H O   
15958 C CB  . VAL I 29  ? 2.1452 3.2055 1.6777 0.4978  0.2773  -0.1009 29  VAL H CB  
15959 C CG1 . VAL I 29  ? 2.1937 3.2720 1.7381 0.4995  0.2967  -0.0790 29  VAL H CG1 
15960 C CG2 . VAL I 29  ? 2.1664 3.1902 1.6849 0.4902  0.2530  -0.1505 29  VAL H CG2 
15961 N N   . ARG I 30  ? 2.1988 3.3959 1.7574 0.4749  0.2274  -0.1200 30  ARG H N   
15962 C CA  . ARG I 30  ? 2.1474 3.3355 1.7016 0.4725  0.2121  -0.1376 30  ARG H CA  
15963 C C   . ARG I 30  ? 2.1402 3.2351 1.6717 0.4778  0.2035  -0.1739 30  ARG H C   
15964 O O   . ARG I 30  ? 2.1901 3.2652 1.7195 0.4734  0.1950  -0.2011 30  ARG H O   
15965 C CB  . ARG I 30  ? 2.1013 3.3009 1.6575 0.4810  0.2265  -0.0975 30  ARG H CB  
15966 C CG  . ARG I 30  ? 2.1417 3.4400 1.7245 0.4731  0.2324  -0.0579 30  ARG H CG  
15967 C CD  . ARG I 30  ? 2.1056 3.4047 1.6920 0.4836  0.2483  -0.0149 30  ARG H CD  
15968 N NE  . ARG I 30  ? 2.1314 3.3664 1.7104 0.5019  0.2761  0.0128  30  ARG H NE  
15969 C CZ  . ARG I 30  ? 2.1669 3.4322 1.7651 0.5050  0.2956  0.0517  30  ARG H CZ  
15970 N NH1 . ARG I 30  ? 2.2384 3.5978 1.8615 0.4904  0.2876  0.0671  30  ARG H NH1 
15971 N NH2 . ARG I 30  ? 2.1653 3.3676 1.7604 0.5210  0.3235  0.0749  30  ARG H NH2 
15972 N N   . ASN I 31  ? 2.2351 3.2740 1.7508 0.4862  0.2047  -0.1741 31  ASN H N   
15973 C CA  . ASN I 31  ? 2.2278 3.1783 1.7221 0.4901  0.1972  -0.2026 31  ASN H CA  
15974 C C   . ASN I 31  ? 2.2122 3.0833 1.6829 0.5026  0.2195  -0.1858 31  ASN H C   
15975 O O   . ASN I 31  ? 2.2011 2.9976 1.6515 0.5054  0.2160  -0.2021 31  ASN H O   
15976 C CB  . ASN I 31  ? 2.2034 3.1441 1.6968 0.4884  0.1818  -0.2174 31  ASN H CB  
15977 C CG  . ASN I 31  ? 2.1253 3.0544 1.6108 0.4984  0.1962  -0.1865 31  ASN H CG  
15978 O OD1 . ASN I 31  ? 2.1452 3.1007 1.6354 0.5045  0.2159  -0.1505 31  ASN H OD1 
15979 N ND2 . ASN I 31  ? 2.1609 3.0511 1.6369 0.5003  0.1867  -0.1990 31  ASN H ND2 
15980 N N   . GLU I 32  ? 2.2929 3.1803 1.7682 0.5089  0.2433  -0.1528 32  GLU H N   
15981 C CA  . GLU I 32  ? 2.2758 3.0957 1.7347 0.5206  0.2700  -0.1315 32  GLU H CA  
15982 C C   . GLU I 32  ? 2.3291 3.0976 1.7748 0.5189  0.2770  -0.1474 32  GLU H C   
15983 O O   . GLU I 32  ? 2.3612 3.1428 1.8151 0.5217  0.2965  -0.1281 32  GLU H O   
15984 C CB  . GLU I 32  ? 2.2759 3.1423 1.7535 0.5288  0.2944  -0.0836 32  GLU H CB  
15985 C CG  . GLU I 32  ? 2.2165 3.1326 1.7063 0.5295  0.2875  -0.0658 32  GLU H CG  
15986 C CD  . GLU I 32  ? 2.2400 3.2276 1.7574 0.5332  0.3053  -0.0164 32  GLU H CD  
15987 O OE1 . GLU I 32  ? 2.2230 3.2533 1.7519 0.5334  0.3020  0.0040  32  GLU H OE1 
15988 O OE2 . GLU I 32  ? 2.2861 3.2898 1.8163 0.5348  0.3220  0.0037  32  GLU H OE2 
15989 N N   . LEU I 33  ? 2.0726 2.7828 1.4994 0.5136  0.2608  -0.1818 33  LEU H N   
15990 C CA  . LEU I 33  ? 2.1230 2.7914 1.5380 0.5085  0.2606  -0.2023 33  LEU H CA  
15991 C C   . LEU I 33  ? 2.1176 2.7027 1.5065 0.5054  0.2528  -0.2255 33  LEU H C   
15992 O O   . LEU I 33  ? 2.0913 2.6694 1.4782 0.5037  0.2340  -0.2391 33  LEU H O   
15993 C CB  . LEU I 33  ? 2.1652 2.8874 1.5968 0.4994  0.2388  -0.2245 33  LEU H CB  
15994 C CG  . LEU I 33  ? 2.2186 2.9058 1.6408 0.4944  0.2384  -0.2433 33  LEU H CG  
15995 C CD1 . LEU I 33  ? 2.2598 3.0093 1.7013 0.4927  0.2452  -0.2327 33  LEU H CD1 
15996 C CD2 . LEU I 33  ? 2.2400 2.9074 1.6596 0.4864  0.2098  -0.2798 33  LEU H CD2 
15997 N N   . ALA I 34  ? 2.1885 2.7132 1.5587 0.5035  0.2678  -0.2292 34  ALA H N   
15998 C CA  . ALA I 34  ? 2.1905 2.6377 1.5345 0.4976  0.2620  -0.2493 34  ALA H CA  
15999 C C   . ALA I 34  ? 2.2444 2.6668 1.5793 0.4883  0.2541  -0.2724 34  ALA H C   
16000 O O   . ALA I 34  ? 2.2783 2.7258 1.6220 0.4880  0.2636  -0.2682 34  ALA H O   
16001 C CB  . ALA I 34  ? 2.1693 2.5580 1.4954 0.5012  0.2905  -0.2316 34  ALA H CB  
16002 N N   . TRP I 35  ? 2.2186 2.5930 1.5365 0.4807  0.2367  -0.2954 35  TRP H N   
16003 C CA  . TRP I 35  ? 2.2376 2.5796 1.5429 0.4712  0.2291  -0.3163 35  TRP H CA  
16004 C C   . TRP I 35  ? 2.2678 2.5309 1.5411 0.4635  0.2413  -0.3201 35  TRP H C   
16005 O O   . TRP I 35  ? 2.2744 2.5070 1.5363 0.4636  0.2396  -0.3182 35  TRP H O   
16006 C CB  . TRP I 35  ? 2.2611 2.6237 1.5782 0.4676  0.1951  -0.3413 35  TRP H CB  
16007 C CG  . TRP I 35  ? 2.2732 2.7137 1.6227 0.4707  0.1822  -0.3445 35  TRP H CG  
16008 C CD1 . TRP I 35  ? 2.2442 2.7401 1.6163 0.4751  0.1726  -0.3404 35  TRP H CD1 
16009 C CD2 . TRP I 35  ? 2.3222 2.7948 1.6848 0.4674  0.1774  -0.3544 35  TRP H CD2 
16010 N NE1 . TRP I 35  ? 2.2737 2.8356 1.6723 0.4733  0.1629  -0.3476 35  TRP H NE1 
16011 C CE2 . TRP I 35  ? 2.3217 2.8705 1.7154 0.4692  0.1653  -0.3561 35  TRP H CE2 
16012 C CE3 . TRP I 35  ? 2.3675 2.8130 1.7183 0.4620  0.1824  -0.3625 35  TRP H CE3 
16013 C CZ2 . TRP I 35  ? 2.3667 2.9650 1.7807 0.4658  0.1583  -0.3656 35  TRP H CZ2 
16014 C CZ3 . TRP I 35  ? 2.4090 2.9025 1.7799 0.4603  0.1749  -0.3710 35  TRP H CZ3 
16015 C CH2 . TRP I 35  ? 2.4092 2.9784 1.8118 0.4622  0.1629  -0.3726 35  TRP H CH2 
16016 N N   . TYR I 36  ? 2.4556 2.6876 1.7145 0.4554  0.2533  -0.3266 36  TYR H N   
16017 C CA  . TYR I 36  ? 2.4691 2.6303 1.6972 0.4442  0.2669  -0.3324 36  TYR H CA  
16018 C C   . TYR I 36  ? 2.5202 2.6559 1.7328 0.4316  0.2518  -0.3554 36  TYR H C   
16019 O O   . TYR I 36  ? 2.5505 2.7199 1.7768 0.4327  0.2402  -0.3633 36  TYR H O   
16020 C CB  . TYR I 36  ? 2.4687 2.6107 1.6926 0.4446  0.3052  -0.3154 36  TYR H CB  
16021 C CG  . TYR I 36  ? 2.4228 2.5871 1.6626 0.4582  0.3243  -0.2887 36  TYR H CG  
16022 C CD1 . TYR I 36  ? 2.4124 2.6410 1.6805 0.4708  0.3286  -0.2702 36  TYR H CD1 
16023 C CD2 . TYR I 36  ? 2.3935 2.5166 1.6206 0.4580  0.3384  -0.2807 36  TYR H CD2 
16024 C CE1 . TYR I 36  ? 2.3727 2.6246 1.6560 0.4834  0.3461  -0.2426 36  TYR H CE1 
16025 C CE2 . TYR I 36  ? 2.3534 2.4963 1.5961 0.4716  0.3564  -0.2542 36  TYR H CE2 
16026 C CZ  . TYR I 36  ? 2.3427 2.5502 1.6137 0.4845  0.3603  -0.2342 36  TYR H CZ  
16027 O OH  . TYR I 36  ? 2.3045 2.5350 1.5922 0.4981  0.3781  -0.2045 36  TYR H OH  
16028 N N   . GLN I 37  ? 2.6072 2.6848 1.7909 0.4192  0.2519  -0.3657 37  GLN H N   
16029 C CA  . GLN I 37  ? 2.6593 2.7043 1.8217 0.4047  0.2426  -0.3849 37  GLN H CA  
16030 C C   . GLN I 37  ? 2.6779 2.6767 1.8164 0.3913  0.2735  -0.3843 37  GLN H C   
16031 O O   . GLN I 37  ? 2.6543 2.6237 1.7821 0.3885  0.2921  -0.3767 37  GLN H O   
16032 C CB  . GLN I 37  ? 2.6691 2.6895 1.8170 0.3991  0.2146  -0.3988 37  GLN H CB  
16033 C CG  . GLN I 37  ? 2.7256 2.7170 1.8514 0.3850  0.2002  -0.4177 37  GLN H CG  
16034 C CD  . GLN I 37  ? 2.7353 2.6978 1.8437 0.3794  0.1767  -0.4277 37  GLN H CD  
16035 O OE1 . GLN I 37  ? 2.7303 2.6515 1.8140 0.3694  0.1874  -0.4257 37  GLN H OE1 
16036 N NE2 . GLN I 37  ? 2.7581 2.7451 1.8818 0.3862  0.1447  -0.4389 37  GLN H NE2 
16037 N N   . GLN I 38  ? 2.5629 2.5565 1.6947 0.3826  0.2790  -0.3937 38  GLN H N   
16038 C CA  . GLN I 38  ? 2.5870 2.5390 1.6971 0.3670  0.3068  -0.3980 38  GLN H CA  
16039 C C   . GLN I 38  ? 2.6408 2.5690 1.7272 0.3499  0.2926  -0.4189 38  GLN H C   
16040 O O   . GLN I 38  ? 2.6673 2.6216 1.7634 0.3539  0.2747  -0.4249 38  GLN H O   
16041 C CB  . GLN I 38  ? 2.5877 2.5606 1.7170 0.3742  0.3384  -0.3842 38  GLN H CB  
16042 C CG  . GLN I 38  ? 2.6097 2.5427 1.7226 0.3598  0.3695  -0.3891 38  GLN H CG  
16043 C CD  . GLN I 38  ? 2.6158 2.5694 1.7514 0.3686  0.4016  -0.3744 38  GLN H CD  
16044 O OE1 . GLN I 38  ? 2.6291 2.6210 1.7831 0.3771  0.3981  -0.3693 38  GLN H OE1 
16045 N NE2 . GLN I 38  ? 2.6104 2.5395 1.7460 0.3679  0.4329  -0.3665 38  GLN H NE2 
16046 N N   . LYS I 39  ? 1.8500 3.1509 2.1539 0.6399  -0.1644 -0.4215 39  LYS H N   
16047 C CA  . LYS I 39  ? 1.8872 3.1882 2.1685 0.6494  -0.1705 -0.4321 39  LYS H CA  
16048 C C   . LYS I 39  ? 1.8980 3.1962 2.1533 0.6637  -0.1822 -0.4515 39  LYS H C   
16049 O O   . LYS I 39  ? 1.8752 3.1788 2.1283 0.6709  -0.1818 -0.4516 39  LYS H O   
16050 C CB  . LYS I 39  ? 1.8887 3.2100 2.1657 0.6604  -0.1594 -0.4161 39  LYS H CB  
16051 C CG  . LYS I 39  ? 1.8873 3.2108 2.1879 0.6467  -0.1484 -0.3979 39  LYS H CG  
16052 C CD  . LYS I 39  ? 1.8926 3.2361 2.1888 0.6579  -0.1372 -0.3820 39  LYS H CD  
16053 C CE  . LYS I 39  ? 1.8961 3.2407 2.2162 0.6436  -0.1267 -0.3644 39  LYS H CE  
16054 N NZ  . LYS I 39  ? 1.9070 3.2705 2.2230 0.6542  -0.1155 -0.3487 39  LYS H NZ  
16055 N N   . PRO I 40  ? 1.9100 3.1994 2.1457 0.6678  -0.1927 -0.4683 40  PRO H N   
16056 C CA  . PRO I 40  ? 1.9233 3.2081 2.1347 0.6803  -0.2048 -0.4880 40  PRO H CA  
16057 C C   . PRO I 40  ? 1.9080 3.2126 2.1048 0.7001  -0.2002 -0.4823 40  PRO H C   
16058 O O   . PRO I 40  ? 1.9099 3.2310 2.1005 0.7103  -0.1921 -0.4706 40  PRO H O   
16059 C CB  . PRO I 40  ? 1.9630 3.2391 2.1568 0.6823  -0.2138 -0.5023 40  PRO H CB  
16060 C CG  . PRO I 40  ? 1.9729 3.2387 2.1869 0.6636  -0.2105 -0.4960 40  PRO H CG  
16061 C CD  . PRO I 40  ? 1.9422 3.2227 2.1782 0.6593  -0.1951 -0.4714 40  PRO H CD  
16062 N N   . GLY I 41  ? 1.8840 3.1865 2.0751 0.7055  -0.2054 -0.4906 41  GLY H N   
16063 C CA  . GLY I 41  ? 1.8744 3.1938 2.0503 0.7243  -0.2026 -0.4875 41  GLY H CA  
16064 C C   . GLY I 41  ? 1.8373 3.1729 2.0297 0.7256  -0.1884 -0.4661 41  GLY H C   
16065 O O   . GLY I 41  ? 1.8310 3.1814 2.0114 0.7414  -0.1852 -0.4623 41  GLY H O   
16066 N N   . LYS I 42  ? 1.8081 3.1415 2.0276 0.7097  -0.1800 -0.4521 42  LYS H N   
16067 C CA  . LYS I 42  ? 1.7719 3.1201 2.0088 0.7097  -0.1660 -0.4310 42  LYS H CA  
16068 C C   . LYS I 42  ? 1.7442 3.0827 2.0041 0.6951  -0.1653 -0.4287 42  LYS H C   
16069 O O   . LYS I 42  ? 1.7542 3.0740 2.0213 0.6813  -0.1735 -0.4398 42  LYS H O   
16070 C CB  . LYS I 42  ? 1.7689 3.1266 2.0187 0.7050  -0.1541 -0.4125 42  LYS H CB  
16071 C CG  . LYS I 42  ? 1.7989 3.1673 2.0276 0.7190  -0.1535 -0.4127 42  LYS H CG  
16072 C CD  . LYS I 42  ? 1.7977 3.1830 2.0070 0.7398  -0.1513 -0.4111 42  LYS H CD  
16073 C CE  . LYS I 42  ? 1.8253 3.2235 2.0166 0.7532  -0.1480 -0.4070 42  LYS H CE  
16074 N NZ  . LYS I 42  ? 1.8355 3.2512 2.0097 0.7731  -0.1444 -0.4029 42  LYS H NZ  
16075 N N   . ALA I 43  ? 1.8046 3.1558 2.0756 0.6984  -0.1554 -0.4141 43  ALA H N   
16076 C CA  . ALA I 43  ? 1.7755 3.1199 2.0707 0.6844  -0.1525 -0.4083 43  ALA H CA  
16077 C C   . ALA I 43  ? 1.7647 3.1045 2.0855 0.6663  -0.1451 -0.3950 43  ALA H C   
16078 O O   . ALA I 43  ? 1.7702 3.1186 2.0922 0.6675  -0.1379 -0.3842 43  ALA H O   
16079 C CB  . ALA I 43  ? 1.7438 3.1038 2.0436 0.6935  -0.1436 -0.3958 43  ALA H CB  
16080 N N   . PRO I 44  ? 1.7096 3.0356 2.0506 0.6493  -0.1470 -0.3957 44  PRO H N   
16081 C CA  . PRO I 44  ? 1.6981 3.0197 2.0648 0.6316  -0.1396 -0.3821 44  PRO H CA  
16082 C C   . PRO I 44  ? 1.6645 3.0039 2.0473 0.6332  -0.1239 -0.3586 44  PRO H C   
16083 O O   . PRO I 44  ? 1.6409 2.9935 2.0210 0.6445  -0.1184 -0.3520 44  PRO H O   
16084 C CB  . PRO I 44  ? 1.6904 2.9944 2.0729 0.6156  -0.1454 -0.3887 44  PRO H CB  
16085 C CG  . PRO I 44  ? 1.7146 3.0091 2.0756 0.6235  -0.1591 -0.4107 44  PRO H CG  
16086 C CD  . PRO I 44  ? 1.7115 3.0235 2.0517 0.6451  -0.1570 -0.4104 44  PRO H CD  
16087 N N   . ASN I 45  ? 1.7793 3.1182 2.1793 0.6214  -0.1166 -0.3460 45  ASN H N   
16088 C CA  . ASN I 45  ? 1.7494 3.1020 2.1686 0.6192  -0.1017 -0.3234 45  ASN H CA  
16089 C C   . ASN I 45  ? 1.7315 3.0731 2.1804 0.5978  -0.0981 -0.3147 45  ASN H C   
16090 O O   . ASN I 45  ? 1.7550 3.0813 2.2095 0.5843  -0.1040 -0.3213 45  ASN H O   
16091 C CB  . ASN I 45  ? 1.7698 3.1340 2.1824 0.6258  -0.0947 -0.3140 45  ASN H CB  
16092 C CG  . ASN I 45  ? 1.7724 3.1546 2.1633 0.6476  -0.0914 -0.3123 45  ASN H CG  
16093 O OD1 . ASN I 45  ? 1.7614 3.1470 2.1405 0.6583  -0.0953 -0.3195 45  ASN H OD1 
16094 N ND2 . ASN I 45  ? 1.8055 3.1993 2.1911 0.6541  -0.0843 -0.3026 45  ASN H ND2 
16095 N N   . LEU I 46  ? 1.6351 2.9844 2.1028 0.5949  -0.0884 -0.2997 46  LEU H N   
16096 C CA  . LEU I 46  ? 1.6167 2.9564 2.1134 0.5752  -0.0843 -0.2903 46  LEU H CA  
16097 C C   . LEU I 46  ? 1.6267 2.9681 2.1385 0.5653  -0.0758 -0.2761 46  LEU H C   
16098 O O   . LEU I 46  ? 1.6222 2.9791 2.1336 0.5736  -0.0656 -0.2627 46  LEU H O   
16099 C CB  . LEU I 46  ? 1.5703 2.9183 2.0820 0.5759  -0.0765 -0.2788 46  LEU H CB  
16100 C CG  . LEU I 46  ? 1.5428 2.8818 2.0850 0.5563  -0.0719 -0.2683 46  LEU H CG  
16101 C CD1 . LEU I 46  ? 1.5595 2.8778 2.1039 0.5435  -0.0840 -0.2836 46  LEU H CD1 
16102 C CD2 . LEU I 46  ? 1.4954 2.8455 2.0507 0.5597  -0.0628 -0.2557 46  LEU H CD2 
16103 N N   . LEU I 47  ? 1.4232 2.7482 1.9480 0.5475  -0.0800 -0.2790 47  LEU H N   
16104 C CA  . LEU I 47  ? 1.4085 2.7322 1.9501 0.5355  -0.0727 -0.2661 47  LEU H CA  
16105 C C   . LEU I 47  ? 1.3883 2.7067 1.9606 0.5183  -0.0657 -0.2522 47  LEU H C   
16106 O O   . LEU I 47  ? 1.3838 2.7112 1.9720 0.5151  -0.0538 -0.2343 47  LEU H O   
16107 C CB  . LEU I 47  ? 1.4372 2.7458 1.9706 0.5276  -0.0824 -0.2789 47  LEU H CB  
16108 C CG  . LEU I 47  ? 1.4693 2.7815 1.9730 0.5430  -0.0897 -0.2929 47  LEU H CG  
16109 C CD1 . LEU I 47  ? 1.5144 2.8094 2.0131 0.5328  -0.0997 -0.3060 47  LEU H CD1 
16110 C CD2 . LEU I 47  ? 1.4736 2.8047 1.9706 0.5557  -0.0796 -0.2803 47  LEU H CD2 
16111 N N   . ILE I 48  ? 1.3941 2.6974 1.9748 0.5068  -0.0729 -0.2602 48  ILE H N   
16112 C CA  . ILE I 48  ? 1.3729 2.6673 1.9821 0.4883  -0.0684 -0.2494 48  ILE H CA  
16113 C C   . ILE I 48  ? 1.3728 2.6637 1.9865 0.4877  -0.0717 -0.2538 48  ILE H C   
16114 O O   . ILE I 48  ? 1.3814 2.6667 1.9776 0.4942  -0.0822 -0.2707 48  ILE H O   
16115 C CB  . ILE I 48  ? 1.3538 2.6288 1.9703 0.4703  -0.0750 -0.2552 48  ILE H CB  
16116 C CG1 . ILE I 48  ? 1.3844 2.6628 1.9987 0.4697  -0.0710 -0.2495 48  ILE H CG1 
16117 C CG2 . ILE I 48  ? 1.3326 2.5968 1.9770 0.4512  -0.0717 -0.2456 48  ILE H CG2 
16118 C CD1 . ILE I 48  ? 1.3691 2.6555 2.0064 0.4627  -0.0572 -0.2278 48  ILE H CD1 
16119 N N   . TYR I 49  ? 1.4072 2.7015 2.0443 0.4802  -0.0626 -0.2386 49  TYR H N   
16120 C CA  . TYR I 49  ? 1.3784 2.6665 2.0249 0.4753  -0.0654 -0.2412 49  TYR H CA  
16121 C C   . TYR I 49  ? 1.3632 2.6426 2.0396 0.4556  -0.0595 -0.2278 49  TYR H C   
16122 O O   . TYR I 49  ? 1.3698 2.6505 2.0595 0.4480  -0.0519 -0.2152 49  TYR H O   
16123 C CB  . TYR I 49  ? 1.3391 2.6437 1.9800 0.4912  -0.0602 -0.2372 49  TYR H CB  
16124 C CG  . TYR I 49  ? 1.3346 2.6559 1.9884 0.4953  -0.0455 -0.2171 49  TYR H CG  
16125 C CD1 . TYR I 49  ? 1.3233 2.6453 2.0028 0.4856  -0.0370 -0.2028 49  TYR H CD1 
16126 C CD2 . TYR I 49  ? 1.3500 2.6860 1.9898 0.5093  -0.0402 -0.2129 49  TYR H CD2 
16127 C CE1 . TYR I 49  ? 1.3270 2.6635 2.0184 0.4892  -0.0236 -0.1850 49  TYR H CE1 
16128 C CE2 . TYR I 49  ? 1.3538 2.7046 2.0049 0.5131  -0.0267 -0.1948 49  TYR H CE2 
16129 C CZ  . TYR I 49  ? 1.3424 2.6932 2.0193 0.5030  -0.0185 -0.1812 49  TYR H CZ  
16130 O OH  . TYR I 49  ? 1.3466 2.7115 2.0347 0.5066  -0.0052 -0.1639 49  TYR H OH  
16131 N N   . TYR I 50  ? 1.4066 2.6764 2.0933 0.4473  -0.0632 -0.2307 50  TYR H N   
16132 C CA  . TYR I 50  ? 1.3971 2.6549 2.1104 0.4273  -0.0601 -0.2207 50  TYR H CA  
16133 C C   . TYR I 50  ? 1.4445 2.6873 2.1607 0.4130  -0.0645 -0.2236 50  TYR H C   
16134 O O   . TYR I 50  ? 1.4433 2.6803 2.1809 0.3983  -0.0585 -0.2108 50  TYR H O   
16135 C CB  . TYR I 50  ? 1.3527 2.6225 2.0882 0.4254  -0.0456 -0.1995 50  TYR H CB  
16136 C CG  . TYR I 50  ? 1.3033 2.5854 2.0410 0.4359  -0.0408 -0.1952 50  TYR H CG  
16137 C CD1 . TYR I 50  ? 1.2956 2.5720 2.0268 0.4378  -0.0489 -0.2067 50  TYR H CD1 
16138 C CD2 . TYR I 50  ? 1.2677 2.5665 2.0141 0.4433  -0.0282 -0.1796 50  TYR H CD2 
16139 C CE1 . TYR I 50  ? 1.2537 2.5413 1.9869 0.4473  -0.0445 -0.2027 50  TYR H CE1 
16140 C CE2 . TYR I 50  ? 1.2247 2.5346 1.9731 0.4526  -0.0237 -0.1756 50  TYR H CE2 
16141 C CZ  . TYR I 50  ? 1.2178 2.5221 1.9596 0.4546  -0.0319 -0.1870 50  TYR H CZ  
16142 O OH  . TYR I 50  ? 1.1781 2.4933 1.9218 0.4639  -0.0274 -0.1830 50  TYR H OH  
16143 N N   . ALA I 51  ? 1.3384 2.5745 2.0325 0.4176  -0.0751 -0.2406 51  ALA H N   
16144 C CA  . ALA I 51  ? 1.3899 2.6107 2.0820 0.4058  -0.0813 -0.2470 51  ALA H CA  
16145 C C   . ALA I 51  ? 1.4064 2.6339 2.1040 0.4042  -0.0731 -0.2349 51  ALA H C   
16146 O O   . ALA I 51  ? 1.4529 2.6730 2.1400 0.4018  -0.0786 -0.2428 51  ALA H O   
16147 C CB  . ALA I 51  ? 1.4024 2.6035 2.1119 0.3852  -0.0851 -0.2466 51  ALA H CB  
16148 N N   . SER I 52  ? 1.4480 2.6887 2.1619 0.4054  -0.0602 -0.2162 52  SER H N   
16149 C CA  . SER I 52  ? 1.4669 2.7130 2.1872 0.4030  -0.0521 -0.2045 52  SER H CA  
16150 C C   . SER I 52  ? 1.4401 2.7081 2.1581 0.4182  -0.0410 -0.1928 52  SER H C   
16151 O O   . SER I 52  ? 1.4608 2.7338 2.1822 0.4174  -0.0344 -0.1837 52  SER H O   
16152 C CB  . SER I 52  ? 1.4702 2.7054 2.2185 0.3826  -0.0466 -0.1906 52  SER H CB  
16153 O OG  . SER I 52  ? 1.4185 2.6575 2.1856 0.3796  -0.0396 -0.1796 52  SER H OG  
16154 N N   . THR I 53  ? 1.3758 2.6562 2.0875 0.4318  -0.0385 -0.1927 53  THR H N   
16155 C CA  . THR I 53  ? 1.3494 2.6498 2.0611 0.4448  -0.0269 -0.1799 53  THR H CA  
16156 C C   . THR I 53  ? 1.3704 2.6827 2.0537 0.4640  -0.0298 -0.1887 53  THR H C   
16157 O O   . THR I 53  ? 1.3741 2.6849 2.0372 0.4736  -0.0393 -0.2042 53  THR H O   
16158 C CB  . THR I 53  ? 1.3460 2.6543 2.0677 0.4489  -0.0216 -0.1733 53  THR H CB  
16159 O OG1 . THR I 53  ? 1.3265 2.6239 2.0755 0.4309  -0.0184 -0.1642 53  THR H OG1 
16160 C CG2 . THR I 53  ? 1.3608 2.6893 2.0818 0.4623  -0.0096 -0.1602 53  THR H CG2 
16161 N N   . LEU I 54  ? 1.5463 2.8696 2.2277 0.4695  -0.0216 -0.1788 54  LEU H N   
16162 C CA  . LEU I 54  ? 1.5689 2.9041 2.2237 0.4878  -0.0233 -0.1853 54  LEU H CA  
16163 C C   . LEU I 54  ? 1.5334 2.8850 2.1772 0.5057  -0.0195 -0.1837 54  LEU H C   
16164 O O   . LEU I 54  ? 1.4991 2.8603 2.1575 0.5064  -0.0089 -0.1692 54  LEU H O   
16165 C CB  . LEU I 54  ? 1.6005 2.9428 2.2576 0.4879  -0.0151 -0.1741 54  LEU H CB  
16166 C CG  . LEU I 54  ? 1.6558 2.9868 2.3075 0.4799  -0.0213 -0.1812 54  LEU H CG  
16167 C CD1 . LEU I 54  ? 1.6784 3.0084 2.3006 0.4924  -0.0329 -0.2002 54  LEU H CD1 
16168 C CD2 . LEU I 54  ? 1.6662 2.9776 2.3376 0.4584  -0.0257 -0.1824 54  LEU H CD2 
16169 N N   . GLN I 55  ? 1.6255 2.9797 2.2431 0.5200  -0.0282 -0.1989 55  GLN H N   
16170 C CA  . GLN I 55  ? 1.6023 2.9727 2.2054 0.5389  -0.0250 -0.1980 55  GLN H CA  
16171 C C   . GLN I 55  ? 1.6133 3.0006 2.2116 0.5496  -0.0141 -0.1848 55  GLN H C   
16172 O O   . GLN I 55  ? 1.6520 3.0388 2.2460 0.5480  -0.0134 -0.1836 55  GLN H O   
16173 C CB  . GLN I 55  ? 1.6205 2.9885 2.1955 0.5515  -0.0375 -0.2180 55  GLN H CB  
16174 C CG  . GLN I 55  ? 1.6088 2.9936 2.1639 0.5729  -0.0352 -0.2187 55  GLN H CG  
16175 C CD  . GLN I 55  ? 1.5613 2.9525 2.1277 0.5750  -0.0298 -0.2115 55  GLN H CD  
16176 O OE1 . GLN I 55  ? 1.5346 2.9166 2.1226 0.5608  -0.0292 -0.2079 55  GLN H OE1 
16177 N NE2 . GLN I 55  ? 1.5523 2.9593 2.1040 0.5929  -0.0260 -0.2092 55  GLN H NE2 
16178 N N   . SER I 56  ? 1.7212 3.1234 2.3209 0.5600  -0.0055 -0.1747 56  SER H N   
16179 C CA  . SER I 56  ? 1.7337 3.1529 2.3281 0.5713  0.0052  -0.1619 56  SER H CA  
16180 C C   . SER I 56  ? 1.7769 3.2012 2.3429 0.5852  -0.0001 -0.1714 56  SER H C   
16181 O O   . SER I 56  ? 1.7857 3.2094 2.3297 0.5963  -0.0096 -0.1865 56  SER H O   
16182 C CB  . SER I 56  ? 1.6986 3.1322 2.2933 0.5828  0.0126  -0.1536 56  SER H CB  
16183 O OG  . SER I 56  ? 1.7182 3.1677 2.3095 0.5926  0.0236  -0.1400 56  SER H OG  
16184 N N   . GLY I 57  ? 1.6220 3.0510 2.1885 0.5846  0.0060  -0.1627 57  GLY H N   
16185 C CA  . GLY I 57  ? 1.6676 3.1021 2.2086 0.5974  0.0022  -0.1699 57  GLY H CA  
16186 C C   . GLY I 57  ? 1.7051 3.1246 2.2394 0.5892  -0.0087 -0.1838 57  GLY H C   
16187 O O   . GLY I 57  ? 1.7467 3.1699 2.2621 0.5979  -0.0113 -0.1887 57  GLY H O   
16188 N N   . VAL I 58  ? 1.6842 3.0870 2.2330 0.5731  -0.0151 -0.1903 58  VAL H N   
16189 C CA  . VAL I 58  ? 1.7211 3.1083 2.2648 0.5639  -0.0255 -0.2034 58  VAL H CA  
16190 C C   . VAL I 58  ? 1.7518 3.1368 2.3101 0.5523  -0.0188 -0.1919 58  VAL H C   
16191 O O   . VAL I 58  ? 1.7318 3.1177 2.3146 0.5416  -0.0091 -0.1764 58  VAL H O   
16192 C CB  . VAL I 58  ? 1.7021 3.0720 2.2563 0.5505  -0.0345 -0.2138 58  VAL H CB  
16193 C CG1 . VAL I 58  ? 1.7437 3.0967 2.2939 0.5399  -0.0449 -0.2268 58  VAL H CG1 
16194 C CG2 . VAL I 58  ? 1.6781 3.0500 2.2166 0.5626  -0.0415 -0.2259 58  VAL H CG2 
16195 N N   . PRO I 59  ? 1.9508 3.3329 2.4950 0.5541  -0.0236 -0.1989 59  PRO H N   
16196 C CA  . PRO I 59  ? 2.0025 3.3837 2.5591 0.5444  -0.0168 -0.1876 59  PRO H CA  
16197 C C   . PRO I 59  ? 1.9953 3.3608 2.5791 0.5218  -0.0164 -0.1830 59  PRO H C   
16198 O O   . PRO I 59  ? 1.9749 3.3260 2.5631 0.5124  -0.0252 -0.1936 59  PRO H O   
16199 C CB  . PRO I 59  ? 2.0567 3.4351 2.5902 0.5509  -0.0251 -0.2005 59  PRO H CB  
16200 C CG  . PRO I 59  ? 2.0590 3.4444 2.5658 0.5696  -0.0320 -0.2134 59  PRO H CG  
16201 C CD  . PRO I 59  ? 1.9754 3.3572 2.4899 0.5676  -0.0344 -0.2167 59  PRO H CD  
16202 N N   . SER I 60  ? 2.0174 3.3857 2.6195 0.5132  -0.0059 -0.1668 60  SER H N   
16203 C CA  . SER I 60  ? 2.0140 3.3684 2.6436 0.4918  -0.0037 -0.1597 60  SER H CA  
16204 C C   . SER I 60  ? 2.0443 3.3808 2.6725 0.4793  -0.0142 -0.1717 60  SER H C   
16205 O O   . SER I 60  ? 2.0532 3.3754 2.7018 0.4612  -0.0152 -0.1693 60  SER H O   
16206 C CB  . SER I 60  ? 2.0534 3.4152 2.7004 0.4867  0.0097  -0.1403 60  SER H CB  
16207 O OG  . SER I 60  ? 2.1458 3.5130 2.7792 0.4928  0.0108  -0.1399 60  SER H OG  
16208 N N   . ARG I 61  ? 1.9903 3.3267 2.5948 0.4882  -0.0220 -0.1845 61  ARG H N   
16209 C CA  . ARG I 61  ? 2.0325 3.3514 2.6344 0.4767  -0.0324 -0.1969 61  ARG H CA  
16210 C C   . ARG I 61  ? 2.0090 3.3132 2.6100 0.4704  -0.0437 -0.2117 61  ARG H C   
16211 O O   . ARG I 61  ? 2.0392 3.3264 2.6425 0.4576  -0.0519 -0.2208 61  ARG H O   
16212 C CB  . ARG I 61  ? 2.0785 3.4014 2.6547 0.4886  -0.0377 -0.2071 61  ARG H CB  
16213 C CG  . ARG I 61  ? 2.0592 3.3898 2.6087 0.5078  -0.0445 -0.2207 61  ARG H CG  
16214 C CD  . ARG I 61  ? 2.1069 3.4416 2.6315 0.5196  -0.0492 -0.2297 61  ARG H CD  
16215 N NE  . ARG I 61  ? 2.0895 3.4317 2.5882 0.5384  -0.0555 -0.2423 61  ARG H NE  
16216 C CZ  . ARG I 61  ? 2.0697 3.4300 2.5583 0.5551  -0.0487 -0.2352 61  ARG H CZ  
16217 N NH1 . ARG I 61  ? 2.0630 3.4356 2.5652 0.5553  -0.0353 -0.2158 61  ARG H NH1 
16218 N NH2 . ARG I 61  ? 2.0581 3.4237 2.5227 0.5716  -0.0553 -0.2475 61  ARG H NH2 
16219 N N   . PHE I 62  ? 2.7449 3.4112 1.9473 1.3452  -0.2333 -0.4563 62  PHE H N   
16220 C CA  . PHE I 62  ? 2.6854 3.3802 1.9438 1.3220  -0.1968 -0.4406 62  PHE H CA  
16221 C C   . PHE I 62  ? 2.6531 3.3597 1.8978 1.3169  -0.1844 -0.4133 62  PHE H C   
16222 O O   . PHE I 62  ? 2.6359 3.3248 1.8284 1.3283  -0.1898 -0.3946 62  PHE H O   
16223 C CB  . PHE I 62  ? 2.6249 3.3135 1.8998 1.3141  -0.1706 -0.4273 62  PHE H CB  
16224 C CG  . PHE I 62  ? 2.6486 3.3314 1.9497 1.3147  -0.1757 -0.4532 62  PHE H CG  
16225 C CD1 . PHE I 62  ? 2.6461 3.3525 2.0135 1.2979  -0.1585 -0.4652 62  PHE H CD1 
16226 C CD2 . PHE I 62  ? 2.6732 3.3264 1.9324 1.3324  -0.1973 -0.4648 62  PHE H CD2 
16227 C CE1 . PHE I 62  ? 2.6668 3.3687 2.0584 1.2988  -0.1629 -0.4892 62  PHE H CE1 
16228 C CE2 . PHE I 62  ? 2.6946 3.3436 1.9774 1.3333  -0.2023 -0.4889 62  PHE H CE2 
16229 C CZ  . PHE I 62  ? 2.6903 3.3642 2.0393 1.3166  -0.1850 -0.5014 62  PHE H CZ  
16230 N N   . SER I 63  ? 2.6192 3.3559 1.9111 1.3002  -0.1682 -0.4109 63  SER H N   
16231 C CA  . SER I 63  ? 2.5812 3.3344 1.8705 1.2919  -0.1511 -0.3834 63  SER H CA  
16232 C C   . SER I 63  ? 2.5519 3.3364 1.9100 1.2679  -0.1203 -0.3765 63  SER H C   
16233 O O   . SER I 63  ? 2.5756 3.3691 1.9809 1.2596  -0.1171 -0.3968 63  SER H O   
16234 C CB  . SER I 63  ? 2.6360 3.3888 1.8908 1.3031  -0.1759 -0.3897 63  SER H CB  
16235 O OG  . SER I 63  ? 2.6946 3.4643 1.9863 1.2977  -0.1851 -0.4142 63  SER H OG  
16236 N N   . ALA I 64  ? 2.4432 3.2442 1.8068 1.2572  -0.0978 -0.3473 64  ALA H N   
16237 C CA  . ALA I 64  ? 2.4172 3.2462 1.8440 1.2343  -0.0671 -0.3366 64  ALA H CA  
16238 C C   . ALA I 64  ? 2.3998 3.2490 1.8217 1.2275  -0.0567 -0.3126 64  ALA H C   
16239 O O   . ALA I 64  ? 2.3820 3.2231 1.7529 1.2385  -0.0644 -0.2958 64  ALA H O   
16240 C CB  . ALA I 64  ? 2.3568 3.1835 1.8098 1.2236  -0.0389 -0.3205 64  ALA H CB  
16241 N N   . THR I 65  ? 2.4477 3.3229 1.9230 1.2096  -0.0394 -0.3113 65  THR H N   
16242 C CA  . THR I 65  ? 2.4579 3.3552 1.9349 1.2019  -0.0304 -0.2921 65  THR H CA  
16243 C C   . THR I 65  ? 2.4280 3.3493 1.9662 1.1783  0.0036  -0.2750 65  THR H C   
16244 O O   . THR I 65  ? 2.4148 3.3355 1.9970 1.1681  0.0185  -0.2817 65  THR H O   
16245 C CB  . THR I 65  ? 2.5824 3.4862 2.0549 1.2076  -0.0530 -0.3141 65  THR H CB  
16246 O OG1 . THR I 65  ? 2.6764 3.5920 2.2066 1.1959  -0.0480 -0.3354 65  THR H OG1 
16247 C CG2 . THR I 65  ? 2.6691 3.5472 2.0844 1.2311  -0.0884 -0.3342 65  THR H CG2 
16248 N N   . GLY I 66  ? 2.4691 3.4113 2.0095 1.1699  0.0155  -0.2525 66  GLY H N   
16249 C CA  . GLY I 66  ? 2.4501 3.4162 2.0484 1.1476  0.0443  -0.2382 66  GLY H CA  
16250 C C   . GLY I 66  ? 2.3871 3.3656 1.9863 1.1371  0.0699  -0.2001 66  GLY H C   
16251 O O   . GLY I 66  ? 2.3424 3.3096 1.9024 1.1458  0.0701  -0.1823 66  GLY H O   
16252 N N   . SER I 67  ? 2.4706 3.4724 2.1147 1.1184  0.0913  -0.1869 67  SER H N   
16253 C CA  . SER I 67  ? 2.4201 3.4367 2.0750 1.1054  0.1174  -0.1507 67  SER H CA  
16254 C C   . SER I 67  ? 2.4634 3.4977 2.1846 1.0835  0.1406  -0.1487 67  SER H C   
16255 O O   . SER I 67  ? 2.5181 3.5560 2.2707 1.0796  0.1351  -0.1729 67  SER H O   
16256 C CB  . SER I 67  ? 2.4558 3.4857 2.0669 1.1113  0.1115  -0.1277 67  SER H CB  
16257 O OG  . SER I 67  ? 2.4910 3.5061 2.0475 1.1266  0.1028  -0.1146 67  SER H OG  
16258 N N   . GLY I 68  ? 2.2203 3.2651 1.9626 1.0694  0.1665  -0.1191 68  GLY H N   
16259 C CA  . GLY I 68  ? 2.1955 3.2561 1.9977 1.0485  0.1891  -0.1142 68  GLY H CA  
16260 C C   . GLY I 68  ? 2.1951 3.2443 2.0478 1.0408  0.1984  -0.1368 68  GLY H C   
16261 O O   . GLY I 68  ? 2.1989 3.2352 2.0612 1.0388  0.2107  -0.1319 68  GLY H O   
16262 N N   . THR I 69  ? 2.2009 3.2552 2.0870 1.0365  0.1934  -0.1613 69  THR H N   
16263 C CA  . THR I 69  ? 2.2119 3.2580 2.1498 1.0286  0.2026  -0.1836 69  THR H CA  
16264 C C   . THR I 69  ? 2.2495 3.2815 2.1765 1.0430  0.1779  -0.2189 69  THR H C   
16265 O O   . THR I 69  ? 2.2791 3.3041 2.2465 1.0381  0.1840  -0.2385 69  THR H O   
16266 C CB  . THR I 69  ? 2.2616 3.3247 2.2559 1.0101  0.2200  -0.1836 69  THR H CB  
16267 O OG1 . THR I 69  ? 2.3255 3.4003 2.3078 1.0148  0.2029  -0.1947 69  THR H OG1 
16268 C CG2 . THR I 69  ? 2.2336 3.3096 2.2426 0.9948  0.2450  -0.1497 69  THR H CG2 
16269 N N   . HIS I 70  ? 2.3279 3.3553 2.2018 1.0607  0.1502  -0.2277 70  HIS H N   
16270 C CA  . HIS I 70  ? 2.3869 3.4031 2.2502 1.0742  0.1242  -0.2619 70  HIS H CA  
16271 C C   . HIS I 70  ? 2.3608 3.3569 2.1628 1.0949  0.1012  -0.2667 70  HIS H C   
16272 O O   . HIS I 70  ? 2.3374 3.3339 2.0899 1.1045  0.0907  -0.2518 70  HIS H O   
16273 C CB  . HIS I 70  ? 2.4588 3.4891 2.3216 1.0757  0.1098  -0.2740 70  HIS H CB  
16274 C CG  . HIS I 70  ? 2.5429 3.5636 2.3966 1.0890  0.0827  -0.3087 70  HIS H CG  
16275 N ND1 . HIS I 70  ? 2.5993 3.6101 2.3959 1.1085  0.0526  -0.3196 70  HIS H ND1 
16276 C CD2 . HIS I 70  ? 2.6062 3.6255 2.5004 1.0859  0.0808  -0.3349 70  HIS H CD2 
16277 C CE1 . HIS I 70  ? 2.6331 3.6372 2.4356 1.1167  0.0326  -0.3511 70  HIS H CE1 
16278 N NE2 . HIS I 70  ? 2.6444 3.6545 2.5056 1.1033  0.0492  -0.3607 70  HIS H NE2 
16279 N N   . PHE I 71  ? 2.4480 3.4262 2.2530 1.1020  0.0933  -0.2877 71  PHE H N   
16280 C CA  . PHE I 71  ? 2.4271 3.3831 2.1774 1.1213  0.0725  -0.2939 71  PHE H CA  
16281 C C   . PHE I 71  ? 2.4795 3.4229 2.2295 1.1326  0.0484  -0.3304 71  PHE H C   
16282 O O   . PHE I 71  ? 2.5145 3.4628 2.3146 1.1236  0.0561  -0.3477 71  PHE H O   
16283 C CB  . PHE I 71  ? 2.3635 3.3075 2.1127 1.1184  0.0915  -0.2757 71  PHE H CB  
16284 C CG  . PHE I 71  ? 2.3143 3.2711 2.0663 1.1068  0.1160  -0.2388 71  PHE H CG  
16285 C CD1 . PHE I 71  ? 2.3158 3.2881 2.1248 1.0859  0.1450  -0.2262 71  PHE H CD1 
16286 C CD2 . PHE I 71  ? 2.2587 3.2119 1.9560 1.1169  0.1100  -0.2165 71  PHE H CD2 
16287 C CE1 . PHE I 71  ? 2.2649 3.2495 2.0759 1.0752  0.1662  -0.1921 71  PHE H CE1 
16288 C CE2 . PHE I 71  ? 2.2234 3.1903 1.9232 1.1064  0.1319  -0.1817 71  PHE H CE2 
16289 C CZ  . PHE I 71  ? 2.2181 3.2010 1.9744 1.0855  0.1595  -0.1695 71  PHE H CZ  
16290 N N   . THR I 72  ? 2.3919 3.3189 2.0848 1.1529  0.0189  -0.3417 72  THR H N   
16291 C CA  . THR I 72  ? 2.4405 3.3536 2.1248 1.1661  -0.0072 -0.3753 72  THR H CA  
16292 C C   . THR I 72  ? 2.4187 3.3054 2.0476 1.1843  -0.0247 -0.3771 72  THR H C   
16293 O O   . THR I 72  ? 2.3799 3.2589 1.9641 1.1911  -0.0250 -0.3552 72  THR H O   
16294 C CB  . THR I 72  ? 2.5134 3.4330 2.1845 1.1743  -0.0332 -0.3953 72  THR H CB  
16295 O OG1 . THR I 72  ? 2.5107 3.4253 2.1243 1.1863  -0.0480 -0.3823 72  THR H OG1 
16296 C CG2 . THR I 72  ? 2.5447 3.4893 2.2711 1.1570  -0.0171 -0.3959 72  THR H CG2 
16297 N N   . LEU I 73  ? 2.4497 3.3226 2.0818 1.1924  -0.0392 -0.4034 73  LEU H N   
16298 C CA  . LEU I 73  ? 2.4491 3.2952 2.0283 1.2117  -0.0614 -0.4117 73  LEU H CA  
16299 C C   . LEU I 73  ? 2.5288 3.3683 2.0919 1.2264  -0.0964 -0.4452 73  LEU H C   
16300 O O   . LEU I 73  ? 2.5645 3.4157 2.1713 1.2202  -0.0977 -0.4672 73  LEU H O   
16301 C CB  . LEU I 73  ? 2.4211 3.2550 2.0173 1.2083  -0.0455 -0.4109 73  LEU H CB  
16302 C CG  . LEU I 73  ? 2.4239 3.2290 1.9694 1.2280  -0.0683 -0.4223 73  LEU H CG  
16303 C CD1 . LEU I 73  ? 2.4107 3.2006 1.8992 1.2374  -0.0686 -0.3956 73  LEU H CD1 
16304 C CD2 . LEU I 73  ? 2.4766 3.2731 2.0517 1.2239  -0.0561 -0.4328 73  LEU H CD2 
16305 N N   . THR I 74  ? 2.5772 3.3976 2.0776 1.2459  -0.1244 -0.4486 74  THR H N   
16306 C CA  . THR I 74  ? 2.6545 3.4671 2.1327 1.2616  -0.1599 -0.4782 74  THR H CA  
16307 C C   . THR I 74  ? 2.6670 3.4500 2.0971 1.2810  -0.1836 -0.4893 74  THR H C   
16308 O O   . THR I 74  ? 2.6333 3.3977 2.0191 1.2890  -0.1825 -0.4702 74  THR H O   
16309 C CB  . THR I 74  ? 2.6907 3.5075 2.1369 1.2683  -0.1754 -0.4739 74  THR H CB  
16310 O OG1 . THR I 74  ? 2.7017 3.5465 2.1938 1.2503  -0.1542 -0.4650 74  THR H OG1 
16311 C CG2 . THR I 74  ? 2.7873 3.5950 2.2103 1.2849  -0.2124 -0.5042 74  THR H CG2 
16312 N N   . VAL I 75  ? 2.6693 3.4483 2.1084 1.2888  -0.2051 -0.5200 75  VAL H N   
16313 C CA  . VAL I 75  ? 2.7109 3.4624 2.1014 1.3099  -0.2352 -0.5354 75  VAL H CA  
16314 C C   . VAL I 75  ? 2.7961 3.5452 2.1601 1.3244  -0.2700 -0.5560 75  VAL H C   
16315 O O   . VAL I 75  ? 2.8539 3.6212 2.2547 1.3202  -0.2770 -0.5777 75  VAL H O   
16316 C CB  . VAL I 75  ? 2.7060 3.4540 2.1247 1.3090  -0.2341 -0.5548 75  VAL H CB  
16317 C CG1 . VAL I 75  ? 2.7511 3.4690 2.1156 1.3311  -0.2642 -0.5673 75  VAL H CG1 
16318 C CG2 . VAL I 75  ? 2.6562 3.4095 2.1104 1.2921  -0.1962 -0.5349 75  VAL H CG2 
16319 N N   . SER I 76  ? 2.7794 3.5056 2.0798 1.3418  -0.2913 -0.5488 76  SER H N   
16320 C CA  . SER I 76  ? 2.8603 3.5825 2.1322 1.3559  -0.3230 -0.5648 76  SER H CA  
16321 C C   . SER I 76  ? 2.9319 3.6475 2.2043 1.3687  -0.3528 -0.5979 76  SER H C   
16322 O O   . SER I 76  ? 3.0024 3.7296 2.2868 1.3720  -0.3706 -0.6182 76  SER H O   
16323 C CB  . SER I 76  ? 2.8620 3.5586 2.0653 1.3718  -0.3375 -0.5473 76  SER H CB  
16324 O OG  . SER I 76  ? 2.8505 3.5176 2.0132 1.3858  -0.3483 -0.5445 76  SER H OG  
16325 N N   . SER I 77  ? 2.9282 3.6256 2.1870 1.3767  -0.3588 -0.6035 77  SER H N   
16326 C CA  . SER I 77  ? 2.9888 3.6826 2.2524 1.3881  -0.3852 -0.6348 77  SER H CA  
16327 C C   . SER I 77  ? 2.9415 3.6317 2.2273 1.3826  -0.3700 -0.6368 77  SER H C   
16328 O O   . SER I 77  ? 2.9093 3.5751 2.1588 1.3898  -0.3679 -0.6226 77  SER H O   
16329 C CB  . SER I 77  ? 3.0579 3.7230 2.2570 1.4136  -0.4240 -0.6430 77  SER H CB  
16330 O OG  . SER I 77  ? 3.1320 3.7985 2.3383 1.4249  -0.4519 -0.6744 77  SER H OG  
16331 N N   . LEU I 78  ? 2.9134 3.6269 2.2585 1.3702  -0.3590 -0.6543 78  LEU H N   
16332 C CA  . LEU I 78  ? 2.8697 3.5815 2.2415 1.3637  -0.3423 -0.6574 78  LEU H CA  
16333 C C   . LEU I 78  ? 2.9093 3.5971 2.2430 1.3841  -0.3720 -0.6753 78  LEU H C   
16334 O O   . LEU I 78  ? 2.9845 3.6714 2.3040 1.3988  -0.4052 -0.6991 78  LEU H O   
16335 C CB  . LEU I 78  ? 2.8699 3.6118 2.3137 1.3470  -0.3260 -0.6739 78  LEU H CB  
16336 C CG  . LEU I 78  ? 2.8180 3.5835 2.3129 1.3232  -0.2882 -0.6550 78  LEU H CG  
16337 C CD1 . LEU I 78  ? 2.8482 3.6416 2.4070 1.3116  -0.2825 -0.6768 78  LEU H CD1 
16338 C CD2 . LEU I 78  ? 2.7359 3.4938 2.2405 1.3117  -0.2547 -0.6309 78  LEU H CD2 
16339 N N   . GLN I 79  ? 2.9140 3.5823 2.2315 1.3852  -0.3600 -0.6636 79  GLN H N   
16340 C CA  . GLN I 79  ? 2.9452 3.5912 2.2336 1.4019  -0.3822 -0.6790 79  GLN H CA  
16341 C C   . GLN I 79  ? 2.9143 3.5697 2.2501 1.3907  -0.3622 -0.6900 79  GLN H C   
16342 O O   . GLN I 79  ? 2.8598 3.5324 2.2426 1.3702  -0.3271 -0.6781 79  GLN H O   
16343 C CB  . GLN I 79  ? 2.9275 3.5386 2.1522 1.4146  -0.3860 -0.6563 79  GLN H CB  
16344 C CG  . GLN I 79  ? 2.9570 3.5564 2.1333 1.4258  -0.4039 -0.6432 79  GLN H CG  
16345 C CD  . GLN I 79  ? 2.9540 3.5161 2.0648 1.4419  -0.4135 -0.6246 79  GLN H CD  
16346 O OE1 . GLN I 79  ? 3.0156 3.5600 2.1160 1.4446  -0.4067 -0.6212 79  GLN H OE1 
16347 N NE2 . GLN I 79  ? 2.9810 3.5299 2.0475 1.4529  -0.4290 -0.6122 79  GLN H NE2 
16348 N N   . PRO I 80  ? 2.8734 3.5180 2.1992 1.4039  -0.3839 -0.7131 80  PRO H N   
16349 C CA  . PRO I 80  ? 2.8501 3.5049 2.2230 1.3936  -0.3662 -0.7269 80  PRO H CA  
16350 C C   . PRO I 80  ? 2.7690 3.4175 2.1581 1.3777  -0.3253 -0.7021 80  PRO H C   
16351 O O   . PRO I 80  ? 2.7388 3.4059 2.1844 1.3607  -0.2986 -0.7061 80  PRO H O   
16352 C CB  . PRO I 80  ? 2.9028 3.5381 2.2419 1.4146  -0.3991 -0.7493 80  PRO H CB  
16353 C CG  . PRO I 80  ? 2.9741 3.6052 2.2746 1.4329  -0.4377 -0.7588 80  PRO H CG  
16354 C CD  . PRO I 80  ? 2.9473 3.5727 2.2228 1.4288  -0.4269 -0.7298 80  PRO H CD  
16355 N N   . GLU I 81  ? 2.9859 3.6087 2.3278 1.3829  -0.3190 -0.6762 81  GLU H N   
16356 C CA  . GLU I 81  ? 2.9122 3.5291 2.2685 1.3685  -0.2802 -0.6522 81  GLU H CA  
16357 C C   . GLU I 81  ? 2.8586 3.4985 2.2546 1.3476  -0.2471 -0.6299 81  GLU H C   
16358 O O   . GLU I 81  ? 2.7997 3.4394 2.2171 1.3337  -0.2125 -0.6101 81  GLU H O   
16359 C CB  . GLU I 81  ? 2.8969 3.4793 2.1902 1.3810  -0.2835 -0.6311 81  GLU H CB  
16360 C CG  . GLU I 81  ? 2.9012 3.4746 2.1474 1.3896  -0.2963 -0.6116 81  GLU H CG  
16361 C CD  . GLU I 81  ? 2.9778 3.5327 2.1726 1.4135  -0.3406 -0.6280 81  GLU H CD  
16362 O OE1 . GLU I 81  ? 3.0333 3.5955 2.2425 1.4207  -0.3638 -0.6579 81  GLU H OE1 
16363 O OE2 . GLU I 81  ? 2.9843 3.5173 2.1249 1.4255  -0.3523 -0.6104 81  GLU H OE2 
16364 N N   . ASP I 82  ? 2.7884 3.4478 2.1948 1.3451  -0.2566 -0.6322 82  ASP H N   
16365 C CA  . ASP I 82  ? 2.7417 3.4229 2.1841 1.3259  -0.2267 -0.6107 82  ASP H CA  
16366 C C   . ASP I 82  ? 2.7355 3.4447 2.2516 1.3072  -0.2049 -0.6225 82  ASP H C   
16367 O O   . ASP I 82  ? 2.6992 3.4262 2.2513 1.2896  -0.1766 -0.6041 82  ASP H O   
16368 C CB  . ASP I 82  ? 2.7688 3.4569 2.1872 1.3311  -0.2446 -0.6059 82  ASP H CB  
16369 C CG  . ASP I 82  ? 2.7743 3.4348 2.1207 1.3483  -0.2628 -0.5905 82  ASP H CG  
16370 O OD1 . ASP I 82  ? 2.7352 3.3750 2.0558 1.3507  -0.2507 -0.5730 82  ASP H OD1 
16371 O OD2 . ASP I 82  ? 2.8206 3.4794 2.1366 1.3594  -0.2885 -0.5952 82  ASP H OD2 
16372 N N   . PHE I 83  ? 2.6428 3.3561 2.1820 1.3108  -0.2171 -0.6521 83  PHE H N   
16373 C CA  . PHE I 83  ? 2.6411 3.3796 2.2501 1.2939  -0.1965 -0.6643 83  PHE H CA  
16374 C C   . PHE I 83  ? 2.5851 3.3172 2.2216 1.2808  -0.1602 -0.6508 83  PHE H C   
16375 O O   . PHE I 83  ? 2.5865 3.3007 2.2081 1.2886  -0.1641 -0.6605 83  PHE H O   
16376 C CB  . PHE I 83  ? 2.7062 3.4535 2.3285 1.3037  -0.2252 -0.7020 83  PHE H CB  
16377 C CG  . PHE I 83  ? 2.7656 3.5238 2.3721 1.3138  -0.2570 -0.7157 83  PHE H CG  
16378 C CD1 . PHE I 83  ? 2.8056 3.5444 2.3499 1.3351  -0.2925 -0.7206 83  PHE H CD1 
16379 C CD2 . PHE I 83  ? 2.7854 3.5718 2.4386 1.3019  -0.2505 -0.7223 83  PHE H CD2 
16380 C CE1 . PHE I 83  ? 2.8657 3.6132 2.3950 1.3447  -0.3211 -0.7328 83  PHE H CE1 
16381 C CE2 . PHE I 83  ? 2.8444 3.6401 2.4827 1.3112  -0.2789 -0.7348 83  PHE H CE2 
16382 C CZ  . PHE I 83  ? 2.8851 3.6612 2.4614 1.3327  -0.3141 -0.7402 83  PHE H CZ  
16383 N N   . ALA I 84  ? 2.6388 3.3851 2.3153 1.2612  -0.1249 -0.6285 84  ALA H N   
16384 C CA  . ALA I 84  ? 2.5811 3.3201 2.2783 1.2480  -0.0871 -0.6070 84  ALA H CA  
16385 C C   . ALA I 84  ? 2.5521 3.3140 2.3019 1.2263  -0.0545 -0.5879 84  ALA H C   
16386 O O   . ALA I 84  ? 2.5802 3.3626 2.3516 1.2221  -0.0619 -0.5949 84  ALA H O   
16387 C CB  . ALA I 84  ? 2.5470 3.2603 2.1871 1.2571  -0.0866 -0.5832 84  ALA H CB  
16388 N N   . THR I 85  ? 2.4784 3.2365 2.2493 1.2128  -0.0184 -0.5640 85  THR H N   
16389 C CA  . THR I 85  ? 2.4525 3.2294 2.2694 1.1924  0.0142  -0.5415 85  THR H CA  
16390 C C   . THR I 85  ? 2.4104 3.1834 2.1917 1.1920  0.0208  -0.5083 85  THR H C   
16391 O O   . THR I 85  ? 2.3823 3.1348 2.1195 1.2011  0.0192  -0.4952 85  THR H O   
16392 C CB  . THR I 85  ? 2.4291 3.2055 2.2972 1.1766  0.0513  -0.5365 85  THR H CB  
16393 O OG1 . THR I 85  ? 2.4671 3.2472 2.3665 1.1777  0.0448  -0.5682 85  THR H OG1 
16394 C CG2 . THR I 85  ? 2.4062 3.2018 2.3242 1.1555  0.0839  -0.5144 85  THR H CG2 
16395 N N   . TYR I 86  ? 2.3026 3.0957 2.1027 1.1818  0.0282  -0.4947 86  TYR H N   
16396 C CA  . TYR I 86  ? 2.2633 3.0574 2.0330 1.1807  0.0338  -0.4639 86  TYR H CA  
16397 C C   . TYR I 86  ? 2.2279 3.0392 2.0471 1.1587  0.0713  -0.4387 86  TYR H C   
16398 O O   . TYR I 86  ? 2.2518 3.0812 2.1238 1.1456  0.0829  -0.4467 86  TYR H O   
16399 C CB  . TYR I 86  ? 2.2946 3.0961 2.0311 1.1910  0.0038  -0.4699 86  TYR H CB  
16400 C CG  . TYR I 86  ? 2.3299 3.1124 2.0088 1.2141  -0.0350 -0.4900 86  TYR H CG  
16401 C CD1 . TYR I 86  ? 2.3873 3.1708 2.0743 1.2225  -0.0593 -0.5241 86  TYR H CD1 
16402 C CD2 . TYR I 86  ? 2.3092 3.0728 1.9251 1.2278  -0.0476 -0.4744 86  TYR H CD2 
16403 C CE1 . TYR I 86  ? 2.4251 3.1909 2.0595 1.2438  -0.0957 -0.5421 86  TYR H CE1 
16404 C CE2 . TYR I 86  ? 2.3478 3.0919 1.9104 1.2491  -0.0831 -0.4920 86  TYR H CE2 
16405 C CZ  . TYR I 86  ? 2.4067 3.1518 1.9788 1.2570  -0.1074 -0.5258 86  TYR H CZ  
16406 O OH  . TYR I 86  ? 2.4497 3.1752 1.9692 1.2784  -0.1436 -0.5429 86  TYR H OH  
16407 N N   . PHE I 87  ? 2.0489 2.8543 1.8501 1.1550  0.0898  -0.4079 87  PHE H N   
16408 C CA  . PHE I 87  ? 2.0164 2.8368 1.8581 1.1351  0.1242  -0.3806 87  PHE H CA  
16409 C C   . PHE I 87  ? 2.0032 2.8315 1.8111 1.1358  0.1227  -0.3524 87  PHE H C   
16410 O O   . PHE I 87  ? 2.0211 2.8361 1.7700 1.1511  0.1048  -0.3451 87  PHE H O   
16411 C CB  . PHE I 87  ? 2.0162 2.8247 1.8758 1.1272  0.1535  -0.3670 87  PHE H CB  
16412 C CG  . PHE I 87  ? 2.0257 2.8283 1.9265 1.1232  0.1621  -0.3914 87  PHE H CG  
16413 C CD1 . PHE I 87  ? 2.0039 2.8212 1.9709 1.1050  0.1868  -0.3941 87  PHE H CD1 
16414 C CD2 . PHE I 87  ? 2.0577 2.8395 1.9304 1.1379  0.1458  -0.4116 87  PHE H CD2 
16415 C CE1 . PHE I 87  ? 2.0138 2.8256 2.0184 1.1015  0.1957  -0.4165 87  PHE H CE1 
16416 C CE2 . PHE I 87  ? 2.0676 2.8449 1.9774 1.1344  0.1538  -0.4345 87  PHE H CE2 
16417 C CZ  . PHE I 87  ? 2.0456 2.8381 2.0215 1.1163  0.1792  -0.4369 87  PHE H CZ  
16418 N N   . CYS I 88  ? 2.1027 2.9524 1.9481 1.1193  0.1420  -0.3365 88  CYS H N   
16419 C CA  . CYS I 88  ? 2.0860 2.9457 1.9097 1.1157  0.1493  -0.3048 88  CYS H CA  
16420 C C   . CYS I 88  ? 2.0664 2.9299 1.9221 1.0992  0.1852  -0.2773 88  CYS H C   
16421 O O   . CYS I 88  ? 2.0582 2.9227 1.9660 1.0864  0.2065  -0.2840 88  CYS H O   
16422 C CB  . CYS I 88  ? 2.0673 2.9491 1.9046 1.1099  0.1425  -0.3057 88  CYS H CB  
16423 S SG  . CYS I 88  ? 2.0402 2.9420 1.9601 1.0877  0.1659  -0.3145 88  CYS H SG  
16424 N N   . GLN I 89  ? 2.2380 3.1038 2.0620 1.0998  0.1918  -0.2463 89  GLN H N   
16425 C CA  . GLN I 89  ? 2.1983 3.0668 2.0445 1.0860  0.2235  -0.2177 89  GLN H CA  
16426 C C   . GLN I 89  ? 2.1674 3.0522 1.9936 1.0819  0.2287  -0.1850 89  GLN H C   
16427 O O   . GLN I 89  ? 2.1553 3.0381 1.9277 1.0959  0.2085  -0.1785 89  GLN H O   
16428 C CB  . GLN I 89  ? 2.1699 3.0149 1.9892 1.0949  0.2278  -0.2131 89  GLN H CB  
16429 C CG  . GLN I 89  ? 2.1290 2.9756 1.9647 1.0825  0.2590  -0.1817 89  GLN H CG  
16430 C CD  . GLN I 89  ? 2.0871 2.9196 1.8653 1.0951  0.2557  -0.1591 89  GLN H CD  
16431 O OE1 . GLN I 89  ? 2.0925 2.9055 1.8257 1.1130  0.2347  -0.1725 89  GLN H OE1 
16432 N NE2 . GLN I 89  ? 2.0486 2.8903 1.8277 1.0861  0.2763  -0.1243 89  GLN H NE2 
16433 N N   . HIS I 90  ? 2.2938 3.1943 2.1623 1.0630  0.2555  -0.1646 90  HIS H N   
16434 C CA  . HIS I 90  ? 2.2602 3.1773 2.1132 1.0575  0.2635  -0.1309 90  HIS H CA  
16435 C C   . HIS I 90  ? 2.2150 3.1264 2.0646 1.0523  0.2862  -0.1013 90  HIS H C   
16436 O O   . HIS I 90  ? 2.2184 3.1192 2.0993 1.0455  0.3039  -0.1060 90  HIS H O   
16437 C CB  . HIS I 90  ? 2.2845 3.2251 2.1846 1.0397  0.2758  -0.1265 90  HIS H CB  
16438 C CG  . HIS I 90  ? 2.2788 3.2249 2.2286 1.0204  0.3075  -0.1100 90  HIS H CG  
16439 N ND1 . HIS I 90  ? 2.2435 3.2011 2.1884 1.0118  0.3237  -0.0745 90  HIS H ND1 
16440 C CD2 . HIS I 90  ? 2.3043 3.2454 2.3083 1.0085  0.3257  -0.1242 90  HIS H CD2 
16441 C CE1 . HIS I 90  ? 2.2521 3.2110 2.2454 0.9954  0.3495  -0.0679 90  HIS H CE1 
16442 N NE2 . HIS I 90  ? 2.2887 3.2375 2.3189 0.9930  0.3518  -0.0981 90  HIS H NE2 
16443 N N   . MET I 91  ? 2.3257 3.2448 2.1369 1.0558  0.2859  -0.0704 91  MET H N   
16444 C CA  . MET I 91  ? 2.2832 3.2005 2.0894 1.0506  0.3071  -0.0377 91  MET H CA  
16445 C C   . MET I 91  ? 2.2627 3.2041 2.0733 1.0391  0.3189  -0.0040 91  MET H C   
16446 O O   . MET I 91  ? 2.2224 3.1648 2.0109 1.0394  0.3291  0.0278  91  MET H O   
16447 C CB  . MET I 91  ? 2.2508 3.1484 1.9977 1.0693  0.2955  -0.0303 91  MET H CB  
16448 C CG  . MET I 91  ? 2.2407 3.1412 1.9313 1.0853  0.2694  -0.0283 91  MET H CG  
16449 S SD  . MET I 91  ? 2.2527 3.1222 1.8893 1.1101  0.2422  -0.0543 91  MET H SD  
16450 C CE  . MET I 91  ? 2.3145 3.1818 1.9877 1.1089  0.2274  -0.1003 91  MET H CE  
16451 N N   . SER I 92  ? 2.0827 3.0436 1.9212 1.0292  0.3175  -0.0098 92  SER H N   
16452 C CA  . SER I 92  ? 2.0684 3.0527 1.9049 1.0202  0.3244  0.0206  92  SER H CA  
16453 C C   . SER I 92  ? 2.0609 3.0528 1.9372 1.0018  0.3530  0.0451  92  SER H C   
16454 O O   . SER I 92  ? 2.0412 3.0501 1.9090 0.9957  0.3600  0.0765  92  SER H O   
16455 C CB  . SER I 92  ? 2.1100 3.1115 1.9609 1.0165  0.3127  0.0053  92  SER H CB  
16456 O OG  . SER I 92  ? 2.1574 3.1601 2.0670 1.0028  0.3237  -0.0160 92  SER H OG  
16457 N N   . SER I 93  ? 2.0094 2.9894 1.9280 0.9931  0.3691  0.0316  93  SER H N   
16458 C CA  . SER I 93  ? 2.0133 2.9986 1.9712 0.9757  0.3958  0.0518  93  SER H CA  
16459 C C   . SER I 93  ? 2.0362 3.0028 2.0303 0.9715  0.4091  0.0304  93  SER H C   
16460 O O   . SER I 93  ? 2.0549 3.0081 2.0509 0.9798  0.3977  -0.0015 93  SER H O   
16461 C CB  . SER I 93  ? 2.0488 3.0560 2.0436 0.9598  0.4028  0.0559  93  SER H CB  
16462 O OG  . SER I 93  ? 2.0975 3.1048 2.1237 0.9576  0.3954  0.0209  93  SER H OG  
16463 N N   . TYR I 94  ? 2.0106 2.9764 2.0327 0.9588  0.4330  0.0482  94  TYR H N   
16464 C CA  . TYR I 94  ? 2.0354 2.9862 2.0890 0.9569  0.4486  0.0324  94  TYR H CA  
16465 C C   . TYR I 94  ? 2.1014 3.0640 2.2076 0.9501  0.4582  0.0114  94  TYR H C   
16466 O O   . TYR I 94  ? 2.1309 3.1153 2.2555 0.9428  0.4643  0.0237  94  TYR H O   
16467 C CB  . TYR I 94  ? 2.0208 2.9689 2.0731 0.9534  0.4705  0.0642  94  TYR H CB  
16468 C CG  . TYR I 94  ? 1.9620 2.8958 1.9657 0.9616  0.4650  0.0846  94  TYR H CG  
16469 C CD1 . TYR I 94  ? 1.9478 2.8606 1.9237 0.9768  0.4548  0.0671  94  TYR H CD1 
16470 C CD2 . TYR I 94  ? 1.9307 2.8753 1.9113 0.9596  0.4707  0.1250  94  TYR H CD2 
16471 C CE1 . TYR I 94  ? 1.9050 2.8074 1.8307 0.9899  0.4507  0.0887  94  TYR H CE1 
16472 C CE2 . TYR I 94  ? 1.8847 2.8202 1.8172 0.9724  0.4669  0.1474  94  TYR H CE2 
16473 C CZ  . TYR I 94  ? 1.8868 2.8008 1.7918 0.9874  0.4572  0.1289  94  TYR H CZ  
16474 O OH  . TYR I 94  ? 1.9022 2.8062 1.7592 1.0003  0.4539  0.1511  94  TYR H OH  
16475 N N   . PRO I 95  ? 2.0194 2.9674 2.1503 0.9524  0.4600  -0.0202 95  PRO H N   
16476 C CA  . PRO I 95  ? 1.9923 2.9139 2.1012 0.9616  0.4509  -0.0380 95  PRO H CA  
16477 C C   . PRO I 95  ? 1.9817 2.8962 2.0633 0.9724  0.4223  -0.0622 95  PRO H C   
16478 O O   . PRO I 95  ? 2.0077 2.9347 2.1048 0.9696  0.4122  -0.0762 95  PRO H O   
16479 C CB  . PRO I 95  ? 2.0383 2.9521 2.1926 0.9582  0.4676  -0.0606 95  PRO H CB  
16480 C CG  . PRO I 95  ? 2.0913 3.0259 2.2886 0.9506  0.4724  -0.0718 95  PRO H CG  
16481 C CD  . PRO I 95  ? 2.0836 3.0403 2.2693 0.9453  0.4741  -0.0395 95  PRO H CD  
16482 N N   . LEU I 96  ? 2.0125 2.9099 2.0476 0.9894  0.4092  -0.0645 96  LEU H N   
16483 C CA  . LEU I 96  ? 2.0182 2.9085 2.0216 1.0059  0.3813  -0.0894 96  LEU H CA  
16484 C C   . LEU I 96  ? 2.0658 2.9511 2.1124 1.0028  0.3797  -0.1270 96  LEU H C   
16485 O O   . LEU I 96  ? 2.0826 2.9583 2.1668 0.9949  0.3980  -0.1374 96  LEU H O   
16486 C CB  . LEU I 96  ? 1.9876 2.8568 1.9364 1.0241  0.3701  -0.0865 96  LEU H CB  
16487 C CG  . LEU I 96  ? 1.9820 2.8534 1.8691 1.0364  0.3571  -0.0596 96  LEU H CG  
16488 C CD1 . LEU I 96  ? 1.9624 2.8501 1.8553 1.0243  0.3762  -0.0206 96  LEU H CD1 
16489 C CD2 . LEU I 96  ? 2.0104 2.8571 1.8511 1.0533  0.3494  -0.0606 96  LEU H CD2 
16490 N N   . THR I 97  ? 2.0451 2.9373 2.0866 1.0088  0.3581  -0.1473 97  THR H N   
16491 C CA  . THR I 97  ? 2.0902 2.9787 2.1697 1.0072  0.3542  -0.1823 97  THR H CA  
16492 C C   . THR I 97  ? 2.1041 2.9854 2.1435 1.0262  0.3215  -0.2061 97  THR H C   
16493 O O   . THR I 97  ? 2.0875 2.9720 2.0773 1.0379  0.3013  -0.1966 97  THR H O   
16494 C CB  . THR I 97  ? 2.1286 3.0365 2.2621 0.9902  0.3653  -0.1862 97  THR H CB  
16495 O OG1 . THR I 97  ? 2.1283 3.0527 2.2375 0.9931  0.3491  -0.1768 97  THR H OG1 
16496 C CG2 . THR I 97  ? 2.1304 3.0476 2.3016 0.9745  0.3963  -0.1646 97  THR H CG2 
16497 N N   . PHE I 98  ? 2.0813 2.9529 2.1431 1.0293  0.3164  -0.2375 98  PHE H N   
16498 C CA  . PHE I 98  ? 2.1044 2.9689 2.1356 1.0464  0.2852  -0.2649 98  PHE H CA  
16499 C C   . PHE I 98  ? 2.1558 3.0339 2.2287 1.0400  0.2803  -0.2876 98  PHE H C   
16500 O O   . PHE I 98  ? 2.1765 3.0627 2.3074 1.0232  0.3037  -0.2888 98  PHE H O   
16501 C CB  . PHE I 98  ? 2.1069 2.9481 2.1248 1.0575  0.2804  -0.2840 98  PHE H CB  
16502 C CG  . PHE I 98  ? 2.0640 2.8887 2.0327 1.0676  0.2802  -0.2652 98  PHE H CG  
16503 C CD1 . PHE I 98  ? 2.0355 2.8563 2.0203 1.0571  0.3089  -0.2423 98  PHE H CD1 
16504 C CD2 . PHE I 98  ? 2.0594 2.8715 1.9654 1.0880  0.2511  -0.2710 98  PHE H CD2 
16505 C CE1 . PHE I 98  ? 2.0433 2.8487 1.9825 1.0667  0.3093  -0.2242 98  PHE H CE1 
16506 C CE2 . PHE I 98  ? 2.0750 2.8705 1.9351 1.0977  0.2516  -0.2533 98  PHE H CE2 
16507 C CZ  . PHE I 98  ? 2.0668 2.8592 1.9436 1.0871  0.2811  -0.2295 98  PHE H CZ  
16508 N N   . GLY I 99  ? 1.9848 2.8649 2.0277 1.0535  0.2497  -0.3057 99  GLY H N   
16509 C CA  . GLY I 99  ? 1.9813 2.8719 2.0589 1.0505  0.2417  -0.3309 99  GLY H CA  
16510 C C   . GLY I 99  ? 1.9975 2.8770 2.1045 1.0517  0.2446  -0.3583 99  GLY H C   
16511 O O   . GLY I 99  ? 2.0147 2.8766 2.1097 1.0571  0.2491  -0.3610 99  GLY H O   
16512 N N   . GLY I 100 ? 2.1296 3.0200 2.2756 1.0468  0.2422  -0.3791 100 GLY H N   
16513 C CA  . GLY I 100 ? 2.1579 3.0408 2.3355 1.0473  0.2457  -0.4054 100 GLY H CA  
16514 C C   . GLY I 100 ? 2.1744 3.0460 2.3113 1.0676  0.2126  -0.4326 100 GLY H C   
16515 O O   . GLY I 100 ? 2.1927 3.0564 2.3486 1.0700  0.2140  -0.4543 100 GLY H O   
16516 N N   . GLY I 101 ? 2.2973 3.1675 2.3782 1.0825  0.1830  -0.4320 101 GLY H N   
16517 C CA  . GLY I 101 ? 2.3161 3.1738 2.3520 1.1028  0.1492  -0.4562 101 GLY H CA  
16518 C C   . GLY I 101 ? 2.3721 3.2420 2.4105 1.1100  0.1217  -0.4831 101 GLY H C   
16519 O O   . GLY I 101 ? 2.4068 3.2925 2.4945 1.0989  0.1318  -0.4919 101 GLY H O   
16520 N N   . THR I 102 ? 2.2762 3.1382 2.2597 1.1291  0.0860  -0.4962 102 THR H N   
16521 C CA  . THR I 102 ? 2.2894 3.1597 2.2660 1.1397  0.0543  -0.5249 102 THR H CA  
16522 C C   . THR I 102 ? 2.3249 3.1779 2.2665 1.1580  0.0273  -0.5496 102 THR H C   
16523 O O   . THR I 102 ? 2.3427 3.1779 2.2293 1.1714  0.0123  -0.5426 102 THR H O   
16524 C CB  . THR I 102 ? 2.2840 3.1618 2.2245 1.1460  0.0341  -0.5167 102 THR H CB  
16525 O OG1 . THR I 102 ? 2.2517 3.1476 2.2281 1.1288  0.0578  -0.4967 102 THR H OG1 
16526 C CG2 . THR I 102 ? 2.3026 3.1857 2.2287 1.1595  -0.0019 -0.5474 102 THR H CG2 
16527 N N   . LYS I 103 ? 2.6451 3.9539 2.6219 0.4733  -1.3252 -0.1785 103 LYS H N   
16528 C CA  . LYS I 103 ? 2.6291 3.9322 2.6184 0.4732  -1.3259 -0.2009 103 LYS H CA  
16529 C C   . LYS I 103 ? 2.6411 3.9194 2.5992 0.4708  -1.3508 -0.2322 103 LYS H C   
16530 O O   . LYS I 103 ? 2.6504 3.9146 2.5970 0.4769  -1.3455 -0.2530 103 LYS H O   
16531 C CB  . LYS I 103 ? 2.6085 3.9176 2.6361 0.4842  -1.2880 -0.2145 103 LYS H CB  
16532 C CG  . LYS I 103 ? 2.5899 3.8959 2.6346 0.4844  -1.2860 -0.2352 103 LYS H CG  
16533 C CD  . LYS I 103 ? 2.5689 3.8838 2.6538 0.4949  -1.2472 -0.2438 103 LYS H CD  
16534 C CE  . LYS I 103 ? 2.5492 3.8653 2.6538 0.4939  -1.2451 -0.2575 103 LYS H CE  
16535 N NZ  . LYS I 103 ? 2.5276 3.8573 2.6743 0.5028  -1.2075 -0.2576 103 LYS H NZ  
16536 N N   . VAL I 104 ? 2.6406 3.9138 2.5854 0.4620  -1.3775 -0.2355 104 VAL H N   
16537 C CA  . VAL I 104 ? 2.6518 3.9021 2.5661 0.4586  -1.4039 -0.2635 104 VAL H CA  
16538 C C   . VAL I 104 ? 2.6336 3.8774 2.5664 0.4624  -1.3948 -0.2921 104 VAL H C   
16539 O O   . VAL I 104 ? 2.6181 3.8722 2.5693 0.4590  -1.3944 -0.2847 104 VAL H O   
16540 C CB  . VAL I 104 ? 2.6657 3.9133 2.5493 0.4458  -1.4422 -0.2482 104 VAL H CB  
16541 C CG1 . VAL I 104 ? 2.6787 3.9019 2.5293 0.4426  -1.4693 -0.2772 104 VAL H CG1 
16542 C CG2 . VAL I 104 ? 2.6825 3.9389 2.5503 0.4419  -1.4500 -0.2172 104 VAL H CG2 
16543 N N   . GLU I 105 ? 2.8141 4.0409 2.7422 0.4696  -1.3874 -0.3247 105 GLU H N   
16544 C CA  . GLU I 105 ? 2.7981 4.0169 2.7427 0.4744  -1.3772 -0.3551 105 GLU H CA  
16545 C C   . GLU I 105 ? 2.8100 4.0051 2.7225 0.4709  -1.4050 -0.3839 105 GLU H C   
16546 O O   . GLU I 105 ? 2.8310 4.0140 2.7104 0.4676  -1.4256 -0.3850 105 GLU H O   
16547 C CB  . GLU I 105 ? 2.8996 4.1201 2.8714 0.4870  -1.3401 -0.3702 105 GLU H CB  
16548 C CG  . GLU I 105 ? 3.0606 4.2695 3.0139 0.4923  -1.3365 -0.3798 105 GLU H CG  
16549 C CD  . GLU I 105 ? 3.1902 4.3908 3.1609 0.5038  -1.3095 -0.4098 105 GLU H CD  
16550 O OE1 . GLU I 105 ? 3.2970 4.5106 3.3037 0.5103  -1.2792 -0.4077 105 GLU H OE1 
16551 O OE2 . GLU I 105 ? 3.1910 4.3723 3.1396 0.5062  -1.3185 -0.4354 105 GLU H OE2 
16552 N N   . ILE I 106 ? 2.8891 4.0777 2.8116 0.4718  -1.4052 -0.4073 106 ILE H N   
16553 C CA  . ILE I 106 ? 2.8616 4.0284 2.7565 0.4685  -1.4310 -0.4355 106 ILE H CA  
16554 C C   . ILE I 106 ? 2.9956 4.1465 2.8885 0.4781  -1.4167 -0.4681 106 ILE H C   
16555 O O   . ILE I 106 ? 3.0882 4.2442 3.0110 0.4874  -1.3856 -0.4791 106 ILE H O   
16556 C CB  . ILE I 106 ? 2.8270 3.9889 2.7339 0.4613  -1.4314 -0.4418 106 ILE H CB  
16557 C CG1 . ILE I 106 ? 2.8246 3.9985 2.7358 0.4489  -1.4376 -0.4061 106 ILE H CG1 
16558 C CG2 . ILE I 106 ? 2.8416 3.9629 2.7212 0.4469  -1.4335 -0.4595 106 ILE H CG2 
16559 C CD1 . ILE I 106 ? 2.8133 3.9784 2.7336 0.4388  -1.4358 -0.4088 106 ILE H CD1 
16560 N N   . LYS I 107 ? 2.9153 4.0417 2.7733 0.4729  -1.4326 -0.4805 107 LYS H N   
16561 C CA  . LYS I 107 ? 3.0360 4.1467 2.8878 0.4823  -1.4264 -0.5154 107 LYS H CA  
16562 C C   . LYS I 107 ? 3.0170 4.1078 2.8736 0.4784  -1.4203 -0.5411 107 LYS H C   
16563 O O   . LYS I 107 ? 2.9445 4.0175 2.7908 0.4615  -1.4244 -0.5311 107 LYS H O   
16564 C CB  . LYS I 107 ? 3.0981 4.1813 2.9119 0.4728  -1.4339 -0.5131 107 LYS H CB  
16565 C CG  . LYS I 107 ? 3.1382 4.2386 2.9450 0.4787  -1.4391 -0.4927 107 LYS H CG  
16566 C CD  . LYS I 107 ? 3.2254 4.2964 2.9936 0.4672  -1.4467 -0.4902 107 LYS H CD  
16567 C CE  . LYS I 107 ? 3.3575 4.4141 3.1188 0.4784  -1.4405 -0.5245 107 LYS H CE  
16568 N NZ  . LYS I 107 ? 3.4425 4.4988 3.1846 0.4829  -1.4447 -0.5189 107 LYS H NZ  
16569 N N   . ARG I 108 ? 2.9691 4.0635 2.8417 0.4940  -1.4100 -0.5742 108 ARG H N   
16570 C CA  . ARG I 108 ? 2.9628 4.0356 2.8374 0.4917  -1.4033 -0.6025 108 ARG H CA  
16571 C C   . ARG I 108 ? 3.0704 4.1347 2.9427 0.5049  -1.3958 -0.6365 108 ARG H C   
16572 O O   . ARG I 108 ? 3.1596 4.2282 3.0298 0.5117  -1.3870 -0.6331 108 ARG H O   
16573 C CB  . ARG I 108 ? 2.9420 4.0361 2.8519 0.4977  -1.3959 -0.6072 108 ARG H CB  
16574 C CG  . ARG I 108 ? 3.0386 4.1510 2.9866 0.5075  -1.3590 -0.5996 108 ARG H CG  
16575 C CD  . ARG I 108 ? 3.0379 4.1549 3.0190 0.5127  -1.3384 -0.6170 108 ARG H CD  
16576 N NE  . ARG I 108 ? 3.0904 4.1892 3.0672 0.5190  -1.3349 -0.6557 108 ARG H NE  
16577 C CZ  . ARG I 108 ? 3.0921 4.1878 3.0854 0.5215  -1.3288 -0.6782 108 ARG H CZ  
16578 N NH1 . ARG I 108 ? 3.0398 4.1493 3.0550 0.5181  -1.3256 -0.6660 108 ARG H NH1 
16579 N NH2 . ARG I 108 ? 3.1488 4.2277 3.1367 0.5273  -1.3259 -0.7130 108 ARG H NH2 
16580 N N   . THR I 109 ? 3.0364 4.0805 2.9099 0.5041  -1.3888 -0.6642 109 THR H N   
16581 C CA  . THR I 109 ? 3.1331 4.1679 3.0061 0.5161  -1.3805 -0.6986 109 THR H CA  
16582 C C   . THR I 109 ? 3.2320 4.2853 3.1425 0.5292  -1.3474 -0.7017 109 THR H C   
16583 O O   . THR I 109 ? 3.2150 4.2860 3.1561 0.5296  -1.3303 -0.6865 109 THR H O   
16584 C CB  . THR I 109 ? 3.0951 4.1011 2.9635 0.5100  -1.3744 -0.7231 109 THR H CB  
16585 O OG1 . THR I 109 ? 3.0688 4.0914 2.9678 0.5137  -1.3678 -0.7283 109 THR H OG1 
16586 C CG2 . THR I 109 ? 3.0165 3.9879 2.8510 0.4884  -1.3830 -0.7075 109 THR H CG2 
16587 N N   . VAL I 110 ? 3.1732 4.2175 3.0813 0.5375  -1.3321 -0.7182 110 VAL H N   
16588 C CA  . VAL I 110 ? 3.1594 4.2143 3.1018 0.5478  -1.2935 -0.7199 110 VAL H CA  
16589 C C   . VAL I 110 ? 3.1368 4.1936 3.1086 0.5525  -1.2760 -0.7413 110 VAL H C   
16590 O O   . VAL I 110 ? 3.1359 4.1776 3.0976 0.5528  -1.2876 -0.7703 110 VAL H O   
16591 C CB  . VAL I 110 ? 3.1726 4.2150 3.1027 0.5552  -1.2839 -0.7358 110 VAL H CB  
16592 C CG1 . VAL I 110 ? 3.1576 4.2088 3.1231 0.5663  -1.2441 -0.7426 110 VAL H CG1 
16593 C CG2 . VAL I 110 ? 3.1936 4.2369 3.0985 0.5510  -1.2975 -0.7114 110 VAL H CG2 
16594 N N   . ALA I 111 ? 3.1856 4.2614 3.1944 0.5565  -1.2478 -0.7272 111 ALA H N   
16595 C CA  . ALA I 111 ? 3.1820 4.2620 3.2222 0.5613  -1.2283 -0.7448 111 ALA H CA  
16596 C C   . ALA I 111 ? 3.2707 4.3630 3.3461 0.5714  -1.1883 -0.7425 111 ALA H C   
16597 O O   . ALA I 111 ? 3.2673 4.3765 3.3573 0.5713  -1.1746 -0.7133 111 ALA H O   
16598 C CB  . ALA I 111 ? 3.0763 4.1685 3.1274 0.5537  -1.2388 -0.7282 111 ALA H CB  
16599 N N   . ALA I 112 ? 3.2945 4.3784 3.3836 0.5800  -1.1694 -0.7733 112 ALA H N   
16600 C CA  . ALA I 112 ? 3.2769 4.3712 3.3998 0.5900  -1.1308 -0.7743 112 ALA H CA  
16601 C C   . ALA I 112 ? 3.2108 4.3239 3.3711 0.5905  -1.1112 -0.7623 112 ALA H C   
16602 O O   . ALA I 112 ? 3.2313 4.3445 3.3948 0.5859  -1.1235 -0.7681 112 ALA H O   
16603 C CB  . ALA I 112 ? 3.3075 4.3864 3.4325 0.5988  -1.1177 -0.8118 112 ALA H CB  
16604 N N   . PRO I 113 ? 3.3508 4.4799 3.5398 0.5962  -1.0806 -0.7455 113 PRO H N   
16605 C CA  . PRO I 113 ? 3.2893 4.4367 3.5152 0.5972  -1.0600 -0.7338 113 PRO H CA  
16606 C C   . PRO I 113 ? 3.2500 4.3935 3.5008 0.6043  -1.0399 -0.7646 113 PRO H C   
16607 O O   . PRO I 113 ? 3.2391 4.3710 3.4899 0.6119  -1.0276 -0.7910 113 PRO H O   
16608 C CB  . PRO I 113 ? 3.2440 4.4076 3.4897 0.6018  -1.0333 -0.7080 113 PRO H CB  
16609 C CG  . PRO I 113 ? 3.2678 4.4190 3.4979 0.6078  -1.0279 -0.7213 113 PRO H CG  
16610 C CD  . PRO I 113 ? 3.3431 4.4746 3.5319 0.6018  -1.0635 -0.7354 113 PRO H CD  
16611 N N   . SER I 114 ? 2.8175 5.5827 2.5833 -0.0838 0.3422  0.4199  114 SER H N   
16612 C CA  . SER I 114 ? 2.7912 5.6489 2.6046 -0.1178 0.3517  0.4202  114 SER H CA  
16613 C C   . SER I 114 ? 2.7862 5.6087 2.5996 -0.1613 0.3417  0.4089  114 SER H C   
16614 O O   . SER I 114 ? 2.7482 5.4983 2.5579 -0.1711 0.3180  0.3939  114 SER H O   
16615 C CB  . SER I 114 ? 2.7144 5.6233 2.5778 -0.1154 0.3423  0.4141  114 SER H CB  
16616 O OG  . SER I 114 ? 2.7559 5.7060 2.6228 -0.0766 0.3531  0.4254  114 SER H OG  
16617 N N   . VAL I 115 ? 2.6864 5.5606 2.5046 -0.1875 0.3598  0.4161  115 VAL H N   
16618 C CA  . VAL I 115 ? 2.6947 5.5337 2.5057 -0.2269 0.3539  0.4079  115 VAL H CA  
16619 C C   . VAL I 115 ? 2.6529 5.5728 2.5164 -0.2659 0.3569  0.4033  115 VAL H C   
16620 O O   . VAL I 115 ? 2.6579 5.6733 2.5487 -0.2671 0.3763  0.4140  115 VAL H O   
16621 C CB  . VAL I 115 ? 2.7791 5.6001 2.5469 -0.2268 0.3717  0.4196  115 VAL H CB  
16622 C CG1 . VAL I 115 ? 2.7650 5.5415 2.5237 -0.2665 0.3637  0.4105  115 VAL H CG1 
16623 C CG2 . VAL I 115 ? 2.8245 5.5713 2.5406 -0.1856 0.3702  0.4251  115 VAL H CG2 
16624 N N   . PHE I 116 ? 2.5678 5.4490 2.4453 -0.2978 0.3375  0.3873  116 PHE H N   
16625 C CA  . PHE I 116 ? 2.5104 5.4561 2.4361 -0.3377 0.3370  0.3804  116 PHE H CA  
16626 C C   . PHE I 116 ? 2.5038 5.3962 2.4168 -0.3752 0.3283  0.3707  116 PHE H C   
16627 O O   . PHE I 116 ? 2.5303 5.3258 2.4116 -0.3718 0.3110  0.3620  116 PHE H O   
16628 C CB  . PHE I 116 ? 2.4395 5.3981 2.4059 -0.3380 0.3187  0.3680  116 PHE H CB  
16629 C CG  . PHE I 116 ? 2.4443 5.4417 2.4212 -0.2988 0.3234  0.3759  116 PHE H CG  
16630 C CD1 . PHE I 116 ? 2.4460 5.3728 2.3927 -0.2613 0.3121  0.3751  116 PHE H CD1 
16631 C CD2 . PHE I 116 ? 2.4233 5.5276 2.4404 -0.2995 0.3391  0.3841  116 PHE H CD2 
16632 C CE1 . PHE I 116 ? 2.4314 5.3932 2.3882 -0.2252 0.3164  0.3823  116 PHE H CE1 
16633 C CE2 . PHE I 116 ? 2.4014 5.5415 2.4287 -0.2634 0.3435  0.3915  116 PHE H CE2 
16634 C CZ  . PHE I 116 ? 2.4089 5.4776 2.4061 -0.2262 0.3323  0.3906  116 PHE H CZ  
16635 N N   . ILE I 117 ? 2.6871 5.6424 2.6250 -0.4109 0.3403  0.3724  117 ILE H N   
16636 C CA  . ILE I 117 ? 2.6087 5.5244 2.5416 -0.4503 0.3327  0.3629  117 ILE H CA  
16637 C C   . ILE I 117 ? 2.4980 5.4600 2.4837 -0.4856 0.3229  0.3502  117 ILE H C   
16638 O O   . ILE I 117 ? 2.4840 5.5391 2.5099 -0.4897 0.3336  0.3545  117 ILE H O   
16639 C CB  . ILE I 117 ? 2.6492 5.5909 2.5618 -0.4642 0.3552  0.3756  117 ILE H CB  
16640 C CG1 . ILE I 117 ? 2.5831 5.4692 2.4839 -0.5017 0.3458  0.3657  117 ILE H CG1 
16641 C CG2 . ILE I 117 ? 2.6491 5.7099 2.6000 -0.4760 0.3775  0.3861  117 ILE H CG2 
16642 C CD1 . ILE I 117 ? 2.6386 5.5228 2.5070 -0.5094 0.3647  0.3777  117 ILE H CD1 
16643 N N   . PHE I 118 ? 2.5595 5.4555 2.5452 -0.5102 0.3020  0.3344  118 PHE H N   
16644 C CA  . PHE I 118 ? 2.4548 5.3832 2.4878 -0.5449 0.2904  0.3206  118 PHE H CA  
16645 C C   . PHE I 118 ? 2.3923 5.2961 2.4225 -0.5873 0.2882  0.3136  118 PHE H C   
16646 O O   . PHE I 118 ? 2.3861 5.1973 2.3827 -0.5907 0.2749  0.3069  118 PHE H O   
16647 C CB  . PHE I 118 ? 2.4147 5.2890 2.4576 -0.5338 0.2646  0.3061  118 PHE H CB  
16648 C CG  . PHE I 118 ? 2.4783 5.3727 2.5242 -0.4918 0.2656  0.3124  118 PHE H CG  
16649 C CD1 . PHE I 118 ? 2.4764 5.4633 2.5671 -0.4902 0.2727  0.3150  118 PHE H CD1 
16650 C CD2 . PHE I 118 ? 2.5385 5.3600 2.5425 -0.4541 0.2596  0.3158  118 PHE H CD2 
16651 C CE1 . PHE I 118 ? 2.5414 5.5480 2.6357 -0.4518 0.2739  0.3210  118 PHE H CE1 
16652 C CE2 . PHE I 118 ? 2.5966 5.4372 2.6040 -0.4155 0.2607  0.3216  118 PHE H CE2 
16653 C CZ  . PHE I 118 ? 2.6015 5.5349 2.6543 -0.4143 0.2679  0.3243  118 PHE H CZ  
16654 N N   . PRO I 119 ? 2.4338 5.4163 2.4978 -0.6201 0.3005  0.3150  119 PRO H N   
16655 C CA  . PRO I 119 ? 2.4467 5.4088 2.5120 -0.6623 0.2977  0.3076  119 PRO H CA  
16656 C C   . PRO I 119 ? 2.4272 5.3354 2.5101 -0.6840 0.2714  0.2876  119 PRO H C   
16657 O O   . PRO I 119 ? 2.3943 5.3044 2.4996 -0.6714 0.2578  0.2798  119 PRO H O   
16658 C CB  . PRO I 119 ? 2.4212 5.4938 2.5255 -0.6878 0.3173  0.3142  119 PRO H CB  
16659 C CG  . PRO I 119 ? 2.3781 5.5206 2.5168 -0.6678 0.3195  0.3165  119 PRO H CG  
16660 C CD  . PRO I 119 ? 2.3953 5.4904 2.5007 -0.6203 0.3164  0.3227  119 PRO H CD  
16661 N N   . PRO I 120 ? 2.7403 5.5989 2.8137 -0.7162 0.2637  0.2791  120 PRO H N   
16662 C CA  . PRO I 120 ? 2.6568 5.4716 2.7514 -0.7407 0.2397  0.2600  120 PRO H CA  
16663 C C   . PRO I 120 ? 2.6114 5.5128 2.7634 -0.7669 0.2407  0.2533  120 PRO H C   
16664 O O   . PRO I 120 ? 2.6081 5.5936 2.7817 -0.7837 0.2596  0.2612  120 PRO H O   
16665 C CB  . PRO I 120 ? 2.6487 5.4029 2.7192 -0.7702 0.2364  0.2556  120 PRO H CB  
16666 C CG  . PRO I 120 ? 2.7209 5.5253 2.7772 -0.7738 0.2623  0.2718  120 PRO H CG  
16667 C CD  . PRO I 120 ? 2.7965 5.6327 2.8379 -0.7306 0.2759  0.2867  120 PRO H CD  
16668 N N   . SER I 121 ? 2.5466 5.4269 2.7231 -0.7698 0.2200  0.2388  121 SER H N   
16669 C CA  . SER I 121 ? 2.4789 5.4325 2.7095 -0.7965 0.2181  0.2303  121 SER H CA  
16670 C C   . SER I 121 ? 2.4188 5.3735 2.6640 -0.8445 0.2168  0.2215  121 SER H C   
16671 O O   . SER I 121 ? 2.4210 5.3009 2.6368 -0.8573 0.2098  0.2174  121 SER H O   
16672 C CB  . SER I 121 ? 2.4446 5.3698 2.6956 -0.7861 0.1957  0.2168  121 SER H CB  
16673 O OG  . SER I 121 ? 2.4186 5.2442 2.6510 -0.7964 0.1739  0.2032  121 SER H OG  
16674 N N   . ASP I 122 ? 2.5138 5.5560 2.8050 -0.8713 0.2240  0.2190  122 ASP H N   
16675 C CA  . ASP I 122 ? 2.4659 5.5156 2.7766 -0.9183 0.2222  0.2095  122 ASP H CA  
16676 C C   . ASP I 122 ? 2.4094 5.3800 2.7240 -0.9356 0.1960  0.1903  122 ASP H C   
16677 O O   . ASP I 122 ? 2.3869 5.3209 2.6970 -0.9678 0.1911  0.1829  122 ASP H O   
16678 C CB  . ASP I 122 ? 2.4315 5.5924 2.7927 -0.9414 0.2340  0.2100  122 ASP H CB  
16679 C CG  . ASP I 122 ? 2.5162 5.7551 2.8740 -0.9334 0.2611  0.2286  122 ASP H CG  
16680 O OD1 . ASP I 122 ? 2.5425 5.7498 2.8604 -0.9215 0.2719  0.2399  122 ASP H OD1 
16681 O OD2 . ASP I 122 ? 2.5670 5.8391 2.9405 -0.9218 0.2592  0.2266  122 ASP H OD2 
16682 N N   . GLU I 123 ? 2.2636 5.2079 2.5873 -0.9150 0.1791  0.1823  123 GLU H N   
16683 C CA  . GLU I 123 ? 2.2181 5.0859 2.5455 -0.9294 0.1538  0.1643  123 GLU H CA  
16684 C C   . GLU I 123 ? 2.2455 5.0076 2.5251 -0.9269 0.1450  0.1629  123 GLU H C   
16685 O O   . GLU I 123 ? 2.2403 4.9513 2.5209 -0.9565 0.1320  0.1506  123 GLU H O   
16686 C CB  . GLU I 123 ? 2.2131 5.0697 2.5544 -0.9023 0.1385  0.1580  123 GLU H CB  
16687 C CG  . GLU I 123 ? 2.1616 4.9500 2.5137 -0.9183 0.1125  0.1389  123 GLU H CG  
16688 C CD  . GLU I 123 ? 2.1667 4.9328 2.5258 -0.8873 0.0971  0.1340  123 GLU H CD  
16689 O OE1 . GLU I 123 ? 2.2094 5.0212 2.5694 -0.8554 0.1072  0.1450  123 GLU H OE1 
16690 O OE2 . GLU I 123 ? 2.1312 4.8344 2.4954 -0.8950 0.0751  0.1192  123 GLU H OE2 
16691 N N   . GLN I 124 ? 2.4378 5.1655 2.6751 -0.8917 0.1517  0.1755  124 GLN H N   
16692 C CA  . GLN I 124 ? 2.4649 5.0933 2.6546 -0.8875 0.1442  0.1753  124 GLN H CA  
16693 C C   . GLN I 124 ? 2.5377 5.1717 2.7173 -0.9200 0.1565  0.1789  124 GLN H C   
16694 O O   . GLN I 124 ? 2.5930 5.1519 2.7528 -0.9381 0.1451  0.1713  124 GLN H O   
16695 C CB  . GLN I 124 ? 2.5206 5.1172 2.6681 -0.8414 0.1500  0.1885  124 GLN H CB  
16696 C CG  . GLN I 124 ? 2.5529 5.0426 2.6493 -0.8330 0.1408  0.1882  124 GLN H CG  
16697 C CD  . GLN I 124 ? 2.6245 5.0916 2.6780 -0.7899 0.1503  0.2029  124 GLN H CD  
16698 O OE1 . GLN I 124 ? 2.6766 5.2142 2.7361 -0.7698 0.1682  0.2157  124 GLN H OE1 
16699 N NE2 . GLN I 124 ? 2.6528 5.0209 2.6629 -0.7754 0.1383  0.2012  124 GLN H NE2 
16700 N N   . LEU I 125 ? 2.4489 5.1712 2.6421 -0.9275 0.1797  0.1908  125 LEU H N   
16701 C CA  . LEU I 125 ? 2.5195 5.2536 2.7045 -0.9577 0.1930  0.1954  125 LEU H CA  
16702 C C   . LEU I 125 ? 2.5326 5.2565 2.7455 -1.0035 0.1812  0.1796  125 LEU H C   
16703 O O   . LEU I 125 ? 2.6157 5.3027 2.8114 -1.0276 0.1824  0.1786  125 LEU H O   
16704 C CB  . LEU I 125 ? 2.4994 5.3383 2.7000 -0.9575 0.2195  0.2105  125 LEU H CB  
16705 C CG  . LEU I 125 ? 2.5547 5.3994 2.7193 -0.9175 0.2357  0.2287  125 LEU H CG  
16706 C CD1 . LEU I 125 ? 2.6151 5.5717 2.8034 -0.9166 0.2603  0.2424  125 LEU H CD1 
16707 C CD2 . LEU I 125 ? 2.6678 5.4403 2.7825 -0.9161 0.2391  0.2349  125 LEU H CD2 
16708 N N   . LYS I 126 ? 2.6031 5.3608 2.8595 -1.0161 0.1702  0.1674  126 LYS H N   
16709 C CA  . LYS I 126 ? 2.5913 5.3379 2.8756 -1.0588 0.1579  0.1514  126 LYS H CA  
16710 C C   . LYS I 126 ? 2.6303 5.2633 2.8863 -1.0643 0.1371  0.1404  126 LYS H C   
16711 O O   . LYS I 126 ? 2.6926 5.3021 2.9565 -1.1007 0.1311  0.1310  126 LYS H O   
16712 C CB  . LYS I 126 ? 2.5148 5.3147 2.8486 -1.0664 0.1490  0.1404  126 LYS H CB  
16713 C CG  . LYS I 126 ? 2.4975 5.4156 2.8670 -1.0725 0.1688  0.1486  126 LYS H CG  
16714 C CD  . LYS I 126 ? 2.4763 5.4404 2.8942 -1.0830 0.1584  0.1362  126 LYS H CD  
16715 C CE  . LYS I 126 ? 2.3857 5.2998 2.7995 -1.0530 0.1396  0.1296  126 LYS H CE  
16716 N NZ  . LYS I 126 ? 2.3862 5.3317 2.8367 -1.0510 0.1293  0.1185  126 LYS H NZ  
16717 N N   . SER I 127 ? 2.7057 5.2674 2.9294 -1.0292 0.1256  0.1414  127 SER H N   
16718 C CA  . SER I 127 ? 2.7427 5.1956 2.9411 -1.0323 0.1041  0.1305  127 SER H CA  
16719 C C   . SER I 127 ? 2.8486 5.2386 2.9981 -1.0305 0.1096  0.1387  127 SER H C   
16720 O O   . SER I 127 ? 2.9298 5.2294 3.0572 -1.0371 0.0929  0.1302  127 SER H O   
16721 C CB  . SER I 127 ? 2.7094 5.1115 2.8984 -0.9967 0.0867  0.1260  127 SER H CB  
16722 O OG  . SER I 127 ? 2.7484 5.1320 2.8983 -0.9561 0.0952  0.1401  127 SER H OG  
16723 N N   . GLY I 128 ? 2.6418 5.0765 2.7739 -1.0218 0.1325  0.1551  128 GLY H N   
16724 C CA  . GLY I 128 ? 2.7391 5.1241 2.8281 -1.0242 0.1400  0.1634  128 GLY H CA  
16725 C C   . GLY I 128 ? 2.7583 5.1036 2.7988 -0.9818 0.1460  0.1768  128 GLY H C   
16726 O O   . GLY I 128 ? 2.8572 5.1560 2.8593 -0.9824 0.1514  0.1836  128 GLY H O   
16727 N N   . THR I 129 ? 2.6244 4.9859 2.6650 -0.9450 0.1453  0.1810  129 THR H N   
16728 C CA  . THR I 129 ? 2.6563 4.9862 2.6524 -0.9036 0.1522  0.1942  129 THR H CA  
16729 C C   . THR I 129 ? 2.6169 5.0368 2.6279 -0.8786 0.1707  0.2069  129 THR H C   
16730 O O   . THR I 129 ? 2.5727 5.0649 2.6280 -0.8864 0.1721  0.2030  129 THR H O   
16731 C CB  . THR I 129 ? 2.6581 4.8935 2.6290 -0.8766 0.1296  0.1865  129 THR H CB  
16732 O OG1 . THR I 129 ? 2.6612 4.9240 2.6669 -0.8660 0.1185  0.1784  129 THR H OG1 
16733 C CG2 . THR I 129 ? 2.6911 4.8357 2.6475 -0.9011 0.1107  0.1740  129 THR H CG2 
16734 N N   . ALA I 130 ? 2.6345 5.0489 2.6077 -0.8481 0.1850  0.2222  130 ALA H N   
16735 C CA  . ALA I 130 ? 2.6001 5.0924 2.5808 -0.8202 0.2034  0.2359  130 ALA H CA  
16736 C C   . ALA I 130 ? 2.6241 5.0615 2.5638 -0.7735 0.2001  0.2429  130 ALA H C   
16737 O O   . ALA I 130 ? 2.7097 5.0839 2.6033 -0.7624 0.2021  0.2489  130 ALA H O   
16738 C CB  . ALA I 130 ? 2.6695 5.2305 2.6485 -0.8328 0.2300  0.2504  130 ALA H CB  
16739 N N   . SER I 131 ? 2.6453 5.1065 2.6019 -0.7465 0.1952  0.2421  131 SER H N   
16740 C CA  . SER I 131 ? 2.6445 5.0656 2.5673 -0.7003 0.1935  0.2493  131 SER H CA  
16741 C C   . SER I 131 ? 2.6305 5.1397 2.5627 -0.6754 0.2157  0.2647  131 SER H C   
16742 O O   . SER I 131 ? 2.5828 5.1722 2.5588 -0.6813 0.2201  0.2637  131 SER H O   
16743 C CB  . SER I 131 ? 2.5859 4.9545 2.5175 -0.6854 0.1686  0.2361  131 SER H CB  
16744 O OG  . SER I 131 ? 2.6147 4.8995 2.5370 -0.7074 0.1478  0.2220  131 SER H OG  
16745 N N   . VAL I 132 ? 2.5052 4.9987 2.3959 -0.6474 0.2294  0.2790  132 VAL H N   
16746 C CA  . VAL I 132 ? 2.5157 5.0826 2.4082 -0.6191 0.2506  0.2948  132 VAL H CA  
16747 C C   . VAL I 132 ? 2.5186 5.0342 2.3819 -0.5729 0.2429  0.2977  132 VAL H C   
16748 O O   . VAL I 132 ? 2.5705 4.9977 2.3889 -0.5583 0.2347  0.2974  132 VAL H O   
16749 C CB  . VAL I 132 ? 2.5928 5.1905 2.4621 -0.6243 0.2751  0.3101  132 VAL H CB  
16750 C CG1 . VAL I 132 ? 2.5931 5.2880 2.4784 -0.6048 0.2982  0.3253  132 VAL H CG1 
16751 C CG2 . VAL I 132 ? 2.6313 5.2455 2.5175 -0.6718 0.2777  0.3049  132 VAL H CG2 
16752 N N   . VAL I 133 ? 2.4368 5.0076 2.3254 -0.5497 0.2457  0.3008  133 VAL H N   
16753 C CA  . VAL I 133 ? 2.4347 4.9621 2.3035 -0.5070 0.2363  0.3017  133 VAL H CA  
16754 C C   . VAL I 133 ? 2.4672 5.0509 2.3243 -0.4735 0.2590  0.3198  133 VAL H C   
16755 O O   . VAL I 133 ? 2.4496 5.1304 2.3399 -0.4786 0.2757  0.3273  133 VAL H O   
16756 C CB  . VAL I 133 ? 2.3409 4.8769 2.2489 -0.5057 0.2177  0.2890  133 VAL H CB  
16757 C CG1 . VAL I 133 ? 2.3408 4.8418 2.2311 -0.4601 0.2102  0.2914  133 VAL H CG1 
16758 C CG2 . VAL I 133 ? 2.3158 4.7876 2.2319 -0.5365 0.1943  0.2710  133 VAL H CG2 
16759 N N   . CYS I 134 ? 2.3780 4.9003 2.1881 -0.4392 0.2594  0.3266  134 CYS H N   
16760 C CA  . CYS I 134 ? 2.3882 4.9481 2.1822 -0.4011 0.2778  0.3427  134 CYS H CA  
16761 C C   . CYS I 134 ? 2.3799 4.8959 2.1659 -0.3633 0.2627  0.3389  134 CYS H C   
16762 O O   . CYS I 134 ? 2.4038 4.8241 2.1591 -0.3535 0.2443  0.3309  134 CYS H O   
16763 C CB  . CYS I 134 ? 2.4429 4.9688 2.1866 -0.3922 0.2926  0.3546  134 CYS H CB  
16764 S SG  . CYS I 134 ? 2.4601 5.0388 2.1824 -0.3497 0.3194  0.3761  134 CYS H SG  
16765 N N   . LEU I 135 ? 2.4618 5.0476 2.2762 -0.3426 0.2702  0.3445  135 LEU H N   
16766 C CA  . LEU I 135 ? 2.4477 5.0045 2.2614 -0.3072 0.2569  0.3413  135 LEU H CA  
16767 C C   . LEU I 135 ? 2.4689 5.0408 2.2551 -0.2646 0.2737  0.3574  135 LEU H C   
16768 O O   . LEU I 135 ? 2.4610 5.1174 2.2604 -0.2613 0.2967  0.3705  135 LEU H O   
16769 C CB  . LEU I 135 ? 2.3896 5.0120 2.2591 -0.3150 0.2505  0.3344  135 LEU H CB  
16770 C CG  . LEU I 135 ? 2.3689 4.9885 2.2450 -0.2760 0.2426  0.3348  135 LEU H CG  
16771 C CD1 . LEU I 135 ? 2.3848 4.8952 2.2349 -0.2623 0.2168  0.3228  135 LEU H CD1 
16772 C CD2 . LEU I 135 ? 2.3115 5.0138 2.2447 -0.2857 0.2415  0.3309  135 LEU H CD2 
16773 N N   . LEU I 136 ? 2.4670 4.9572 2.2154 -0.2325 0.2623  0.3562  136 LEU H N   
16774 C CA  . LEU I 136 ? 2.6181 5.1120 2.3406 -0.1880 0.2742  0.3693  136 LEU H CA  
16775 C C   . LEU I 136 ? 2.5570 5.0358 2.2954 -0.1607 0.2581  0.3629  136 LEU H C   
16776 O O   . LEU I 136 ? 2.5730 4.9681 2.2979 -0.1567 0.2349  0.3508  136 LEU H O   
16777 C CB  . LEU I 136 ? 2.8931 5.3017 2.5549 -0.1713 0.2750  0.3737  136 LEU H CB  
16778 C CG  . LEU I 136 ? 2.9545 5.3709 2.5883 -0.1864 0.2943  0.3839  136 LEU H CG  
16779 C CD1 . LEU I 136 ? 2.8842 5.3072 2.5363 -0.2350 0.2908  0.3757  136 LEU H CD1 
16780 C CD2 . LEU I 136 ? 3.1522 5.4758 2.7252 -0.1624 0.2916  0.3872  136 LEU H CD2 
16781 N N   . ASN I 137 ? 2.6417 5.2009 2.4089 -0.1420 0.2701  0.3713  137 ASN H N   
16782 C CA  . ASN I 137 ? 2.5097 5.0702 2.3014 -0.1204 0.2559  0.3653  137 ASN H CA  
16783 C C   . ASN I 137 ? 2.6564 5.2053 2.4222 -0.0716 0.2626  0.3760  137 ASN H C   
16784 O O   . ASN I 137 ? 2.7133 5.3232 2.4753 -0.0558 0.2858  0.3912  137 ASN H O   
16785 C CB  . ASN I 137 ? 2.2696 4.9322 2.1202 -0.1378 0.2617  0.3648  137 ASN H CB  
16786 C CG  . ASN I 137 ? 2.1994 4.8477 2.0816 -0.1355 0.2392  0.3515  137 ASN H CG  
16787 O OD1 . ASN I 137 ? 2.1842 4.7551 2.0583 -0.1467 0.2168  0.3375  137 ASN H OD1 
16788 N ND2 . ASN I 137 ? 2.2058 4.9280 2.1241 -0.1205 0.2451  0.3561  137 ASN H ND2 
16789 N N   . ASN I 138 ? 2.5573 5.0285 2.3065 -0.0483 0.2421  0.3678  138 ASN H N   
16790 C CA  . ASN I 138 ? 2.6429 5.1037 2.3783 -0.0019 0.2432  0.3746  138 ASN H CA  
16791 C C   . ASN I 138 ? 2.9417 5.3955 2.6321 0.0247  0.2634  0.3901  138 ASN H C   
16792 O O   . ASN I 138 ? 3.0006 5.5248 2.6993 0.0446  0.2836  0.4037  138 ASN H O   
16793 C CB  . ASN I 138 ? 2.4794 5.0322 2.2644 0.0071  0.2493  0.3782  138 ASN H CB  
16794 C CG  . ASN I 138 ? 2.2164 4.7685 2.0431 -0.0127 0.2277  0.3628  138 ASN H CG  
16795 O OD1 . ASN I 138 ? 2.1585 4.6359 1.9760 -0.0295 0.2069  0.3491  138 ASN H OD1 
16796 N ND2 . ASN I 138 ? 2.1580 4.7937 2.0311 -0.0107 0.2327  0.3650  138 ASN H ND2 
16797 N N   . PHE I 139 ? 2.7842 5.1509 2.4265 0.0249  0.2574  0.3877  139 PHE H N   
16798 C CA  . PHE I 139 ? 3.0035 5.3526 2.5988 0.0489  0.2748  0.4012  139 PHE H CA  
16799 C C   . PHE I 139 ? 3.0199 5.2657 2.5688 0.0812  0.2600  0.3978  139 PHE H C   
16800 O O   . PHE I 139 ? 2.8923 5.0674 2.4394 0.0781  0.2351  0.3839  139 PHE H O   
16801 C CB  . PHE I 139 ? 3.0800 5.4305 2.6562 0.0187  0.2873  0.4051  139 PHE H CB  
16802 C CG  . PHE I 139 ? 3.0101 5.2770 2.5696 -0.0092 0.2671  0.3911  139 PHE H CG  
16803 C CD1 . PHE I 139 ? 2.9031 5.1887 2.5003 -0.0489 0.2563  0.3795  139 PHE H CD1 
16804 C CD2 . PHE I 139 ? 3.0651 5.2356 2.5709 0.0038  0.2595  0.3898  139 PHE H CD2 
16805 C CE1 . PHE I 139 ? 2.8330 5.0418 2.4154 -0.0747 0.2379  0.3669  139 PHE H CE1 
16806 C CE2 . PHE I 139 ? 3.0122 5.1058 2.5028 -0.0219 0.2410  0.3774  139 PHE H CE2 
16807 C CZ  . PHE I 139 ? 2.8881 5.0010 2.4173 -0.0611 0.2303  0.3659  139 PHE H CZ  
16808 N N   . TYR I 140 ? 2.9138 5.1529 2.4253 0.1128  0.2759  0.4108  140 TYR H N   
16809 C CA  . TYR I 140 ? 2.9510 5.0943 2.4109 0.1446  0.2664  0.4101  140 TYR H CA  
16810 C C   . TYR I 140 ? 3.1000 5.2438 2.5161 0.1604  0.2891  0.4249  140 TYR H C   
16811 O O   . TYR I 140 ? 3.1552 5.3816 2.5841 0.1673  0.3129  0.4384  140 TYR H O   
16812 C CB  . TYR I 140 ? 2.9117 5.0461 2.3798 0.1828  0.2570  0.4091  140 TYR H CB  
16813 C CG  . TYR I 140 ? 2.9369 4.9712 2.3542 0.2157  0.2452  0.4072  140 TYR H CG  
16814 C CD1 . TYR I 140 ? 3.0848 5.1150 2.4648 0.2499  0.2620  0.4204  140 TYR H CD1 
16815 C CD2 . TYR I 140 ? 2.8303 4.7739 2.2367 0.2121  0.2174  0.3923  140 TYR H CD2 
16816 C CE1 . TYR I 140 ? 3.0980 5.0372 2.4312 0.2796  0.2514  0.4185  140 TYR H CE1 
16817 C CE2 . TYR I 140 ? 2.8639 4.7161 2.2239 0.2418  0.2065  0.3905  140 TYR H CE2 
16818 C CZ  . TYR I 140 ? 2.9958 4.8463 2.3192 0.2754  0.2235  0.4036  140 TYR H CZ  
16819 O OH  . TYR I 140 ? 2.9991 4.7589 2.2759 0.3049  0.2126  0.4017  140 TYR H OH  
16820 N N   . PRO I 141 ? 3.0037 5.0554 2.3676 0.1672  0.2820  0.4228  141 PRO H N   
16821 C CA  . PRO I 141 ? 2.9354 4.8812 2.2762 0.1616  0.2548  0.4081  141 PRO H CA  
16822 C C   . PRO I 141 ? 2.8672 4.7947 2.2210 0.1153  0.2436  0.3971  141 PRO H C   
16823 O O   . PRO I 141 ? 2.8734 4.8718 2.2550 0.0856  0.2569  0.4005  141 PRO H O   
16824 C CB  . PRO I 141 ? 3.0282 4.9021 2.3066 0.1869  0.2595  0.4145  141 PRO H CB  
16825 C CG  . PRO I 141 ? 3.1294 5.0694 2.3990 0.1856  0.2891  0.4303  141 PRO H CG  
16826 C CD  . PRO I 141 ? 3.1183 5.1681 2.4386 0.1863  0.3035  0.4372  141 PRO H CD  
16827 N N   . ARG I 142 ? 3.0610 4.8923 2.3939 0.1098  0.2190  0.3841  142 ARG H N   
16828 C CA  . ARG I 142 ? 2.9814 4.7884 2.3290 0.0672  0.2049  0.3718  142 ARG H CA  
16829 C C   . ARG I 142 ? 3.0745 4.8908 2.4026 0.0401  0.2202  0.3778  142 ARG H C   
16830 O O   . ARG I 142 ? 3.0246 4.8656 2.3790 0.0007  0.2182  0.3719  142 ARG H O   
16831 C CB  . ARG I 142 ? 2.9067 4.6035 2.2311 0.0706  0.1760  0.3578  142 ARG H CB  
16832 C CG  . ARG I 142 ? 2.8108 4.4836 2.1588 0.0290  0.1577  0.3432  142 ARG H CG  
16833 C CD  . ARG I 142 ? 2.7213 4.2810 2.0415 0.0335  0.1303  0.3305  142 ARG H CD  
16834 N NE  . ARG I 142 ? 2.6130 4.1533 1.9621 -0.0034 0.1112  0.3157  142 ARG H NE  
16835 C CZ  . ARG I 142 ? 2.6584 4.1740 1.9991 -0.0385 0.1091  0.3114  142 ARG H CZ  
16836 N NH1 . ARG I 142 ? 2.8130 4.3208 2.1172 -0.0418 0.1250  0.3208  142 ARG H NH1 
16837 N NH2 . ARG I 142 ? 2.4938 3.9929 1.8629 -0.0704 0.0912  0.2976  142 ARG H NH2 
16838 N N   . GLU I 143 ? 2.8741 4.6709 2.1565 0.0601  0.2356  0.3894  143 GLU H N   
16839 C CA  . GLU I 143 ? 2.9564 4.7511 2.2153 0.0359  0.2488  0.3949  143 GLU H CA  
16840 C C   . GLU I 143 ? 2.9450 4.8480 2.2438 0.0101  0.2700  0.4025  143 GLU H C   
16841 O O   . GLU I 143 ? 3.0031 4.9826 2.3173 0.0282  0.2893  0.4142  143 GLU H O   
16842 C CB  . GLU I 143 ? 3.1001 4.8573 2.3030 0.0664  0.2621  0.4067  143 GLU H CB  
16843 C CG  . GLU I 143 ? 3.2345 5.0070 2.4147 0.0460  0.2813  0.4159  143 GLU H CG  
16844 C CD  . GLU I 143 ? 3.2371 4.9504 2.4078 0.0091  0.2666  0.4053  143 GLU H CD  
16845 O OE1 . GLU I 143 ? 3.2221 4.8538 2.3822 0.0093  0.2414  0.3923  143 GLU H OE1 
16846 O OE2 . GLU I 143 ? 3.3059 5.0548 2.4805 -0.0202 0.2803  0.4099  143 GLU H OE2 
16847 N N   . ALA I 144 ? 3.0414 4.9505 2.3573 -0.0322 0.2662  0.3959  144 ALA H N   
16848 C CA  . ALA I 144 ? 3.0260 5.0328 2.3793 -0.0609 0.2850  0.4019  144 ALA H CA  
16849 C C   . ALA I 144 ? 3.0224 5.0041 2.3659 -0.1007 0.2840  0.3980  144 ALA H C   
16850 O O   . ALA I 144 ? 2.9902 4.8914 2.3193 -0.1148 0.2629  0.3857  144 ALA H O   
16851 C CB  . ALA I 144 ? 2.9254 4.9977 2.3388 -0.0733 0.2780  0.3948  144 ALA H CB  
16852 N N   . LYS I 145 ? 3.0899 5.1411 2.4414 -0.1186 0.3072  0.4087  145 LYS H N   
16853 C CA  . LYS I 145 ? 3.0841 5.1239 2.4291 -0.1571 0.3098  0.4068  145 LYS H CA  
16854 C C   . LYS I 145 ? 2.9706 5.1045 2.3691 -0.1925 0.3190  0.4063  145 LYS H C   
16855 O O   . LYS I 145 ? 2.9483 5.1721 2.3708 -0.1852 0.3389  0.4172  145 LYS H O   
16856 C CB  . LYS I 145 ? 3.2049 5.2327 2.5033 -0.1477 0.3298  0.4207  145 LYS H CB  
16857 C CG  . LYS I 145 ? 3.2527 5.2702 2.5439 -0.1871 0.3335  0.4197  145 LYS H CG  
16858 C CD  . LYS I 145 ? 3.4124 5.3764 2.6457 -0.1749 0.3437  0.4290  145 LYS H CD  
16859 C CE  . LYS I 145 ? 3.4697 5.5019 2.6932 -0.1533 0.3731  0.4476  145 LYS H CE  
16860 N NZ  . LYS I 145 ? 3.6013 5.5912 2.7727 -0.1491 0.3852  0.4570  145 LYS H NZ  
16861 N N   . VAL I 146 ? 3.1725 5.2850 2.5894 -0.2307 0.3046  0.3938  146 VAL H N   
16862 C CA  . VAL I 146 ? 3.0804 5.2723 2.5455 -0.2691 0.3115  0.3917  146 VAL H CA  
16863 C C   . VAL I 146 ? 3.1022 5.2702 2.5503 -0.3035 0.3155  0.3914  146 VAL H C   
16864 O O   . VAL I 146 ? 3.1844 5.2654 2.6082 -0.3143 0.2977  0.3816  146 VAL H O   
16865 C CB  . VAL I 146 ? 3.0168 5.2120 2.5266 -0.2855 0.2899  0.3757  146 VAL H CB  
16866 C CG1 . VAL I 146 ? 2.8772 5.1578 2.4367 -0.3249 0.2980  0.3739  146 VAL H CG1 
16867 C CG2 . VAL I 146 ? 2.9982 5.2101 2.5224 -0.2499 0.2847  0.3758  146 VAL H CG2 
16868 N N   . GLN I 147 ? 3.0134 5.2583 2.4744 -0.3205 0.3388  0.4024  147 GLN H N   
16869 C CA  . GLN I 147 ? 3.0191 5.2551 2.4689 -0.3547 0.3455  0.4035  147 GLN H CA  
16870 C C   . GLN I 147 ? 2.8715 5.1928 2.3745 -0.3934 0.3519  0.4008  147 GLN H C   
16871 O O   . GLN I 147 ? 2.7785 5.1910 2.3143 -0.3885 0.3669  0.4083  147 GLN H O   
16872 C CB  . GLN I 147 ? 3.1109 5.3561 2.5210 -0.3394 0.3694  0.4207  147 GLN H CB  
16873 C CG  . GLN I 147 ? 3.3121 5.4747 2.6667 -0.3013 0.3651  0.4244  147 GLN H CG  
16874 C CD  . GLN I 147 ? 3.4436 5.6046 2.7565 -0.2934 0.3869  0.4396  147 GLN H CD  
16875 O OE1 . GLN I 147 ? 3.5063 5.6790 2.8175 -0.3237 0.3957  0.4423  147 GLN H OE1 
16876 N NE2 . GLN I 147 ? 3.5862 5.7330 2.8656 -0.2524 0.3958  0.4497  147 GLN H NE2 
16877 N N   . TRP I 148 ? 2.9591 5.2505 2.4706 -0.4318 0.3405  0.3901  148 TRP H N   
16878 C CA  . TRP I 148 ? 2.8277 5.1920 2.3871 -0.4722 0.3456  0.3864  148 TRP H CA  
16879 C C   . TRP I 148 ? 2.8552 5.2527 2.4028 -0.4933 0.3672  0.3977  148 TRP H C   
16880 O O   . TRP I 148 ? 2.9867 5.3195 2.4921 -0.4953 0.3673  0.4001  148 TRP H O   
16881 C CB  . TRP I 148 ? 2.7576 5.0736 2.3368 -0.5036 0.3205  0.3676  148 TRP H CB  
16882 C CG  . TRP I 148 ? 2.6870 4.9997 2.2953 -0.4923 0.3017  0.3561  148 TRP H CG  
16883 C CD1 . TRP I 148 ? 2.7577 4.9883 2.3456 -0.4696 0.2803  0.3473  148 TRP H CD1 
16884 C CD2 . TRP I 148 ? 2.5731 4.9697 2.2364 -0.5025 0.3028  0.3524  148 TRP H CD2 
16885 N NE1 . TRP I 148 ? 2.6461 4.9039 2.2732 -0.4652 0.2680  0.3385  148 TRP H NE1 
16886 C CE2 . TRP I 148 ? 2.5495 4.9089 2.2231 -0.4851 0.2815  0.3414  148 TRP H CE2 
16887 C CE3 . TRP I 148 ? 2.5422 5.0417 2.2472 -0.5249 0.3197  0.3575  148 TRP H CE3 
16888 C CZ2 . TRP I 148 ? 2.4965 4.9181 2.2200 -0.4892 0.2768  0.3353  148 TRP H CZ2 
16889 C CZ3 . TRP I 148 ? 2.4898 5.0508 2.2441 -0.5290 0.3147  0.3513  148 TRP H CZ3 
16890 C CH2 . TRP I 148 ? 2.4675 4.9894 2.2305 -0.5112 0.2935  0.3404  148 TRP H CH2 
16891 N N   . LYS I 149 ? 2.8311 5.3300 2.4166 -0.5091 0.3853  0.4047  149 LYS H N   
16892 C CA  . LYS I 149 ? 2.9079 5.4506 2.4910 -0.5330 0.4061  0.4149  149 LYS H CA  
16893 C C   . LYS I 149 ? 2.8363 5.4461 2.4724 -0.5755 0.4062  0.4077  149 LYS H C   
16894 O O   . LYS I 149 ? 2.7617 5.4410 2.4409 -0.5756 0.4070  0.4057  149 LYS H O   
16895 C CB  . LYS I 149 ? 2.9715 5.5775 2.5431 -0.5059 0.4331  0.4342  149 LYS H CB  
16896 C CG  . LYS I 149 ? 3.0770 5.6153 2.5925 -0.4660 0.4350  0.4421  149 LYS H CG  
16897 C CD  . LYS I 149 ? 3.1434 5.7458 2.6524 -0.4341 0.4591  0.4597  149 LYS H CD  
16898 C CE  . LYS I 149 ? 3.2746 5.8051 2.7283 -0.3935 0.4590  0.4660  149 LYS H CE  
16899 N NZ  . LYS I 149 ? 3.3176 5.9072 2.7628 -0.3613 0.4829  0.4834  149 LYS H NZ  
16900 N N   . VAL I 150 ? 3.0132 5.6018 2.6459 -0.6114 0.4052  0.4039  150 VAL H N   
16901 C CA  . VAL I 150 ? 2.9628 5.6086 2.6423 -0.6549 0.4054  0.3969  150 VAL H CA  
16902 C C   . VAL I 150 ? 3.0571 5.7476 2.7300 -0.6747 0.4288  0.4096  150 VAL H C   
16903 O O   . VAL I 150 ? 3.1457 5.7776 2.7834 -0.6844 0.4291  0.4112  150 VAL H O   
16904 C CB  . VAL I 150 ? 2.9538 5.5296 2.6397 -0.6832 0.3799  0.3782  150 VAL H CB  
16905 C CG1 . VAL I 150 ? 2.9020 5.5389 2.6364 -0.7280 0.3809  0.3711  150 VAL H CG1 
16906 C CG2 . VAL I 150 ? 2.8679 5.3962 2.5581 -0.6617 0.3569  0.3662  150 VAL H CG2 
16907 N N   . ASP I 151 ? 2.8527 5.1927 3.0668 0.5164  -0.0349 0.9636  151 ASP H N   
16908 C CA  . ASP I 151 ? 2.9277 5.3083 3.1396 0.5121  -0.0251 0.9797  151 ASP H CA  
16909 C C   . ASP I 151 ? 3.0275 5.4436 3.2265 0.5281  -0.0233 0.9768  151 ASP H C   
16910 O O   . ASP I 151 ? 3.0592 5.4959 3.2466 0.5274  -0.0232 0.9853  151 ASP H O   
16911 C CB  . ASP I 151 ? 2.9694 5.3403 3.1769 0.4966  -0.0287 0.9918  151 ASP H CB  
16912 C CG  . ASP I 151 ? 2.8851 5.2370 3.1077 0.4798  -0.0260 0.9992  151 ASP H CG  
16913 O OD1 . ASP I 151 ? 2.8457 5.2054 3.0822 0.4795  -0.0175 0.9999  151 ASP H OD1 
16914 O OD2 . ASP I 151 ? 2.9347 5.2640 3.1549 0.4674  -0.0325 1.0042  151 ASP H OD2 
16915 N N   . ASN I 152 ? 2.8859 5.3085 3.0871 0.5430  -0.0222 0.9644  152 ASN H N   
16916 C CA  . ASN I 152 ? 2.9654 5.4216 3.1559 0.5604  -0.0205 0.9588  152 ASN H CA  
16917 C C   . ASN I 152 ? 3.0265 5.4760 3.1983 0.5679  -0.0316 0.9520  152 ASN H C   
16918 O O   . ASN I 152 ? 3.1549 5.6367 3.3146 0.5797  -0.0297 0.9515  152 ASN H O   
16919 C CB  . ASN I 152 ? 3.0718 5.5767 3.2631 0.5595  -0.0071 0.9737  152 ASN H CB  
16920 C CG  . ASN I 152 ? 3.0563 5.5747 3.2636 0.5585  0.0040  0.9766  152 ASN H CG  
16921 O OD1 . ASN I 152 ? 3.0923 5.6165 3.3020 0.5718  0.0054  0.9656  152 ASN H OD1 
16922 N ND2 . ASN I 152 ? 3.0803 5.6025 3.2985 0.5429  0.0112  0.9910  152 ASN H ND2 
16923 N N   . ALA I 153 ? 2.8398 5.2481 3.0082 0.5617  -0.0433 0.9464  153 ALA H N   
16924 C CA  . ALA I 153 ? 2.9107 5.3069 3.0614 0.5695  -0.0553 0.9377  153 ALA H CA  
16925 C C   . ALA I 153 ? 2.8453 5.2133 2.9989 0.5808  -0.0656 0.9173  153 ALA H C   
16926 O O   . ALA I 153 ? 2.7795 5.1126 2.9451 0.5733  -0.0696 0.9126  153 ALA H O   
16927 C CB  . ALA I 153 ? 2.9075 5.2782 3.0510 0.5545  -0.0619 0.9464  153 ALA H CB  
16928 N N   . LEU I 154 ? 3.0070 5.3907 3.1503 0.5988  -0.0700 0.9050  154 LEU H N   
16929 C CA  . LEU I 154 ? 2.9476 5.3083 3.0949 0.6110  -0.0804 0.8847  154 LEU H CA  
16930 C C   . LEU I 154 ? 2.9367 5.2553 3.0781 0.6057  -0.0945 0.8780  154 LEU H C   
16931 O O   . LEU I 154 ? 2.9902 5.3074 3.1148 0.6032  -0.0996 0.8827  154 LEU H O   
16932 C CB  . LEU I 154 ? 3.0144 5.4048 3.1518 0.6320  -0.0822 0.8729  154 LEU H CB  
16933 C CG  . LEU I 154 ? 3.0349 5.4072 3.1789 0.6467  -0.0928 0.8506  154 LEU H CG  
16934 C CD1 . LEU I 154 ? 2.9490 5.3077 3.1159 0.6441  -0.0885 0.8468  154 LEU H CD1 
16935 C CD2 . LEU I 154 ? 3.1103 5.5158 3.2437 0.6674  -0.0943 0.8393  154 LEU H CD2 
16936 N N   . GLN I 155 ? 2.8880 5.1724 3.0433 0.6041  -0.1008 0.8671  155 GLN H N   
16937 C CA  . GLN I 155 ? 2.8561 5.0986 3.0086 0.5985  -0.1140 0.8601  155 GLN H CA  
16938 C C   . GLN I 155 ? 2.8610 5.0943 3.0092 0.6154  -0.1270 0.8396  155 GLN H C   
16939 O O   . GLN I 155 ? 2.8502 5.0963 3.0075 0.6291  -0.1263 0.8279  155 GLN H O   
16940 C CB  . GLN I 155 ? 2.7710 4.9807 2.9421 0.5857  -0.1133 0.8610  155 GLN H CB  
16941 C CG  . GLN I 155 ? 2.7616 4.9807 2.9394 0.5696  -0.1007 0.8797  155 GLN H CG  
16942 C CD  . GLN I 155 ? 2.8013 5.0173 2.9659 0.5567  -0.1019 0.8932  155 GLN H CD  
16943 O OE1 . GLN I 155 ? 2.7795 4.9612 2.9414 0.5477  -0.1110 0.8917  155 GLN H OE1 
16944 N NE2 . GLN I 155 ? 2.8700 5.1222 3.0268 0.5557  -0.0928 0.9065  155 GLN H NE2 
16945 N N   . SER I 156 ? 2.6218 4.8325 2.7565 0.6145  -0.1391 0.8350  156 SER H N   
16946 C CA  . SER I 156 ? 2.6313 4.8278 2.7628 0.6288  -0.1532 0.8150  156 SER H CA  
16947 C C   . SER I 156 ? 2.6014 4.7547 2.7303 0.6196  -0.1656 0.8113  156 SER H C   
16948 O O   . SER I 156 ? 2.6292 4.7716 2.7475 0.6061  -0.1654 0.8240  156 SER H O   
16949 C CB  . SER I 156 ? 2.7451 4.9710 2.8559 0.6440  -0.1562 0.8108  156 SER H CB  
16950 O OG  . SER I 156 ? 2.8432 5.1114 2.9542 0.6513  -0.1439 0.8164  156 SER H OG  
16951 N N   . GLY I 157 ? 2.6192 4.7484 2.7587 0.6270  -0.1766 0.7934  157 GLY H N   
16952 C CA  . GLY I 157 ? 2.5947 4.6844 2.7315 0.6213  -0.1900 0.7867  157 GLY H CA  
16953 C C   . GLY I 157 ? 2.5243 4.5808 2.6759 0.6046  -0.1888 0.7920  157 GLY H C   
16954 O O   . GLY I 157 ? 2.5029 4.5252 2.6563 0.6015  -0.2005 0.7834  157 GLY H O   
16955 N N   . ASN I 158 ? 2.5618 4.6274 2.7239 0.5940  -0.1754 0.8056  158 ASN H N   
16956 C CA  . ASN I 158 ? 2.4981 4.5338 2.6736 0.5783  -0.1735 0.8111  158 ASN H CA  
16957 C C   . ASN I 158 ? 2.4277 4.4581 2.6275 0.5811  -0.1690 0.8043  158 ASN H C   
16958 O O   . ASN I 158 ? 2.3764 4.3876 2.5882 0.5686  -0.1646 0.8103  158 ASN H O   
16959 C CB  . ASN I 158 ? 2.5171 4.5626 2.6878 0.5623  -0.1624 0.8316  158 ASN H CB  
16960 C CG  . ASN I 158 ? 2.5497 4.6379 2.7206 0.5663  -0.1483 0.8416  158 ASN H CG  
16961 O OD1 . ASN I 158 ? 2.5515 4.6606 2.7280 0.5804  -0.1458 0.8333  158 ASN H OD1 
16962 N ND2 . ASN I 158 ? 2.5781 4.6798 2.7440 0.5539  -0.1393 0.8593  158 ASN H ND2 
16963 N N   . SER I 159 ? 2.3609 4.4074 2.5683 0.5975  -0.1701 0.7917  159 SER H N   
16964 C CA  . SER I 159 ? 2.2998 4.3414 2.5308 0.6014  -0.1662 0.7848  159 SER H CA  
16965 C C   . SER I 159 ? 2.2728 4.2985 2.5143 0.6147  -0.1792 0.7637  159 SER H C   
16966 O O   . SER I 159 ? 2.3111 4.3432 2.5413 0.6258  -0.1890 0.7534  159 SER H O   
16967 C CB  . SER I 159 ? 2.3207 4.3996 2.5561 0.6084  -0.1532 0.7901  159 SER H CB  
16968 O OG  . SER I 159 ? 2.3749 4.4812 2.6005 0.6249  -0.1566 0.7813  159 SER H OG  
16969 N N   . GLN I 160 ? 2.1853 4.1908 2.4496 0.6138  -0.1792 0.7573  160 GLN H N   
16970 C CA  . GLN I 160 ? 2.1539 4.1453 2.4345 0.6261  -0.1902 0.7375  160 GLN H CA  
16971 C C   . GLN I 160 ? 2.1188 4.1167 2.4236 0.6318  -0.1824 0.7339  160 GLN H C   
16972 O O   . GLN I 160 ? 2.0921 4.0877 2.4040 0.6218  -0.1711 0.7461  160 GLN H O   
16973 C CB  . GLN I 160 ? 2.1100 4.0613 2.3959 0.6183  -0.2011 0.7315  160 GLN H CB  
16974 C CG  . GLN I 160 ? 2.1488 4.0906 2.4125 0.6158  -0.2118 0.7307  160 GLN H CG  
16975 C CD  . GLN I 160 ? 2.1084 4.0113 2.3786 0.6100  -0.2237 0.7224  160 GLN H CD  
16976 O OE1 . GLN I 160 ? 2.0779 3.9581 2.3512 0.5955  -0.2206 0.7312  160 GLN H OE1 
16977 N NE2 . GLN I 160 ? 2.1104 4.0057 2.3829 0.6217  -0.2376 0.7049  160 GLN H NE2 
16978 N N   . GLU I 161 ? 2.2099 4.2157 2.5277 0.6482  -0.1888 0.7167  161 GLU H N   
16979 C CA  . GLU I 161 ? 2.1821 4.1929 2.5248 0.6555  -0.1831 0.7108  161 GLU H CA  
16980 C C   . GLU I 161 ? 2.1251 4.1056 2.4928 0.6588  -0.1929 0.6953  161 GLU H C   
16981 O O   . GLU I 161 ? 2.1182 4.0841 2.4850 0.6627  -0.2063 0.6830  161 GLU H O   
16982 C CB  . GLU I 161 ? 2.2312 4.2768 2.5734 0.6725  -0.1819 0.7023  161 GLU H CB  
16983 C CG  . GLU I 161 ? 2.2883 4.3678 2.6107 0.6705  -0.1698 0.7178  161 GLU H CG  
16984 C CD  . GLU I 161 ? 2.3353 4.4488 2.6599 0.6879  -0.1682 0.7084  161 GLU H CD  
16985 O OE1 . GLU I 161 ? 2.3260 4.4363 2.6663 0.7016  -0.1776 0.6889  161 GLU H OE1 
16986 O OE2 . GLU I 161 ? 2.3829 4.5266 2.6944 0.6879  -0.1575 0.7199  161 GLU H OE2 
16987 N N   . SER I 162 ? 2.1242 4.0960 2.5150 0.6574  -0.1858 0.6962  162 SER H N   
16988 C CA  . SER I 162 ? 2.1153 4.0637 2.5351 0.6627  -0.1930 0.6812  162 SER H CA  
16989 C C   . SER I 162 ? 2.1097 4.0721 2.5521 0.6724  -0.1854 0.6768  162 SER H C   
16990 O O   . SER I 162 ? 2.1028 4.0763 2.5428 0.6671  -0.1721 0.6906  162 SER H O   
16991 C CB  . SER I 162 ? 2.1002 4.0142 2.5266 0.6480  -0.1923 0.6881  162 SER H CB  
16992 O OG  . SER I 162 ? 2.0926 3.9846 2.5475 0.6534  -0.1996 0.6733  162 SER H OG  
16993 N N   . VAL I 163 ? 2.1998 4.1619 2.6651 0.6866  -0.1939 0.6571  163 VAL H N   
16994 C CA  . VAL I 163 ? 2.2054 4.1802 2.6950 0.6975  -0.1885 0.6498  163 VAL H CA  
16995 C C   . VAL I 163 ? 2.1539 4.1014 2.6787 0.6999  -0.1932 0.6374  163 VAL H C   
16996 O O   . VAL I 163 ? 2.1254 4.0546 2.6589 0.7017  -0.2055 0.6249  163 VAL H O   
16997 C CB  . VAL I 163 ? 2.2558 4.2611 2.7432 0.7146  -0.1934 0.6360  163 VAL H CB  
16998 C CG1 . VAL I 163 ? 2.2709 4.2909 2.7819 0.7249  -0.1864 0.6302  163 VAL H CG1 
16999 C CG2 . VAL I 163 ? 2.3106 4.3424 2.7617 0.7125  -0.1900 0.6476  163 VAL H CG2 
17000 N N   . THR I 164 ? 2.2775 4.2225 2.8228 0.7000  -0.1833 0.6412  164 THR H N   
17001 C CA  . THR I 164 ? 2.2348 4.1567 2.8164 0.7033  -0.1860 0.6298  164 THR H CA  
17002 C C   . THR I 164 ? 2.2479 4.1812 2.8554 0.7210  -0.1942 0.6071  164 THR H C   
17003 O O   . THR I 164 ? 2.2962 4.2579 2.8959 0.7312  -0.1939 0.6023  164 THR H O   
17004 C CB  . THR I 164 ? 2.2257 4.1412 2.8196 0.6976  -0.1719 0.6423  164 THR H CB  
17005 O OG1 . THR I 164 ? 2.2740 4.2177 2.8661 0.7054  -0.1635 0.6448  164 THR H OG1 
17006 C CG2 . THR I 164 ? 2.2085 4.1118 2.7792 0.6802  -0.1642 0.6633  164 THR H CG2 
17007 N N   . GLU I 165 ? 2.2573 4.1685 2.8971 0.7246  -0.2013 0.5926  165 GLU H N   
17008 C CA  . GLU I 165 ? 2.2637 4.1825 2.9372 0.7404  -0.2069 0.5710  165 GLU H CA  
17009 C C   . GLU I 165 ? 2.2898 4.2196 2.9803 0.7450  -0.1947 0.5746  165 GLU H C   
17010 O O   . GLU I 165 ? 2.2854 4.2080 2.9702 0.7352  -0.1828 0.5921  165 GLU H O   
17011 C CB  . GLU I 165 ? 2.2105 4.1019 2.9180 0.7418  -0.2159 0.5559  165 GLU H CB  
17012 C CG  . GLU I 165 ? 2.1873 4.0691 2.8837 0.7405  -0.2302 0.5473  165 GLU H CG  
17013 C CD  . GLU I 165 ? 2.2244 4.1304 2.9136 0.7541  -0.2406 0.5311  165 GLU H CD  
17014 O OE1 . GLU I 165 ? 2.2412 4.1599 2.9578 0.7679  -0.2426 0.5142  165 GLU H OE1 
17015 O OE2 . GLU I 165 ? 2.2926 4.2043 2.9491 0.7513  -0.2468 0.5349  165 GLU H OE2 
17016 N N   . GLN I 166 ? 2.2294 4.1774 2.9400 0.7602  -0.1978 0.5574  166 GLN H N   
17017 C CA  . GLN I 166 ? 2.2604 4.2186 2.9906 0.7662  -0.1874 0.5579  166 GLN H CA  
17018 C C   . GLN I 166 ? 2.2231 4.1535 2.9818 0.7600  -0.1806 0.5625  166 GLN H C   
17019 O O   . GLN I 166 ? 2.1854 4.0940 2.9731 0.7612  -0.1874 0.5502  166 GLN H O   
17020 C CB  . GLN I 166 ? 2.2927 4.2685 3.0489 0.7839  -0.1943 0.5340  166 GLN H CB  
17021 C CG  . GLN I 166 ? 2.3376 4.3282 3.1113 0.7918  -0.1844 0.5330  166 GLN H CG  
17022 C CD  . GLN I 166 ? 2.3822 4.3948 3.1746 0.8092  -0.1914 0.5098  166 GLN H CD  
17023 O OE1 . GLN I 166 ? 2.3627 4.3695 3.1767 0.8167  -0.2032 0.4896  166 GLN H OE1 
17024 N NE2 . GLN I 166 ? 2.4401 4.4787 3.2249 0.8160  -0.1842 0.5121  166 GLN H NE2 
17025 N N   . ASP I 167 ? 2.2039 4.1358 2.9541 0.7536  -0.1669 0.5803  167 ASP H N   
17026 C CA  . ASP I 167 ? 2.1905 4.0967 2.9625 0.7470  -0.1591 0.5874  167 ASP H CA  
17027 C C   . ASP I 167 ? 2.1936 4.0931 3.0133 0.7590  -0.1605 0.5686  167 ASP H C   
17028 O O   . ASP I 167 ? 2.2312 4.1507 3.0638 0.7710  -0.1599 0.5580  167 ASP H O   
17029 C CB  . ASP I 167 ? 2.2173 4.1299 2.9693 0.7392  -0.1442 0.6094  167 ASP H CB  
17030 C CG  . ASP I 167 ? 2.2096 4.0949 2.9754 0.7303  -0.1359 0.6201  167 ASP H CG  
17031 O OD1 . ASP I 167 ? 2.1837 4.0492 2.9376 0.7189  -0.1378 0.6280  167 ASP H OD1 
17032 O OD2 . ASP I 167 ? 2.2256 4.1090 3.0135 0.7350  -0.1275 0.6205  167 ASP H OD2 
17033 N N   . SER I 168 ? 2.1910 4.0624 3.0379 0.7558  -0.1623 0.5640  168 SER H N   
17034 C CA  . SER I 168 ? 2.1892 4.0523 3.0853 0.7666  -0.1644 0.5446  168 SER H CA  
17035 C C   . SER I 168 ? 2.2337 4.1023 3.1477 0.7717  -0.1521 0.5483  168 SER H C   
17036 O O   . SER I 168 ? 2.2699 4.1432 3.2202 0.7838  -0.1538 0.5306  168 SER H O   
17037 C CB  . SER I 168 ? 2.1417 3.9734 3.0613 0.7608  -0.1675 0.5412  168 SER H CB  
17038 O OG  . SER I 168 ? 2.1490 3.9635 3.0621 0.7502  -0.1556 0.5606  168 SER H OG  
17039 N N   . LYS I 169 ? 2.0158 3.8842 2.9061 0.7629  -0.1399 0.5705  169 LYS H N   
17040 C CA  . LYS I 169 ? 2.0711 3.9425 2.9778 0.7673  -0.1280 0.5751  169 LYS H CA  
17041 C C   . LYS I 169 ? 2.1284 4.0314 3.0181 0.7744  -0.1247 0.5762  169 LYS H C   
17042 O O   . LYS I 169 ? 2.1781 4.0920 3.0947 0.7867  -0.1245 0.5621  169 LYS H O   
17043 C CB  . LYS I 169 ? 2.0889 3.9432 2.9814 0.7549  -0.1160 0.5978  169 LYS H CB  
17044 C CG  . LYS I 169 ? 2.0415 3.8641 2.9560 0.7493  -0.1162 0.5974  169 LYS H CG  
17045 C CD  . LYS I 169 ? 2.0864 3.8957 2.9975 0.7422  -0.1020 0.6164  169 LYS H CD  
17046 C CE  . LYS I 169 ? 2.1481 3.9736 3.0164 0.7343  -0.0942 0.6372  169 LYS H CE  
17047 N NZ  . LYS I 169 ? 2.1171 3.9275 2.9761 0.7248  -0.0818 0.6570  169 LYS H NZ  
17048 N N   . ASP I 170 ? 2.3066 4.2249 3.1528 0.7667  -0.1219 0.5926  170 ASP H N   
17049 C CA  . ASP I 170 ? 2.3682 4.3168 3.1947 0.7717  -0.1166 0.5974  170 ASP H CA  
17050 C C   . ASP I 170 ? 2.3882 4.3623 3.1988 0.7790  -0.1266 0.5859  170 ASP H C   
17051 O O   . ASP I 170 ? 2.4427 4.4443 3.2360 0.7840  -0.1229 0.5886  170 ASP H O   
17052 C CB  . ASP I 170 ? 2.3736 4.3258 3.1638 0.7591  -0.1054 0.6233  170 ASP H CB  
17053 C CG  . ASP I 170 ? 2.3547 4.3037 3.1100 0.7465  -0.1095 0.6345  170 ASP H CG  
17054 O OD1 . ASP I 170 ? 2.3246 4.2811 3.0711 0.7491  -0.1204 0.6245  170 ASP H OD1 
17055 O OD2 . ASP I 170 ? 2.3615 4.3001 3.0983 0.7339  -0.1015 0.6535  170 ASP H OD2 
17056 N N   . SER I 171 ? 2.3144 4.2803 3.1293 0.7799  -0.1389 0.5733  171 SER H N   
17057 C CA  . SER I 171 ? 2.3321 4.3202 3.1354 0.7884  -0.1497 0.5596  171 SER H CA  
17058 C C   . SER I 171 ? 2.3557 4.3663 3.1107 0.7824  -0.1474 0.5753  171 SER H C   
17059 O O   . SER I 171 ? 2.3976 4.4348 3.1392 0.7912  -0.1522 0.5670  171 SER H O   
17060 C CB  . SER I 171 ? 2.3840 4.3907 3.2148 0.8051  -0.1518 0.5397  171 SER H CB  
17061 O OG  . SER I 171 ? 2.3647 4.3513 3.2431 0.8111  -0.1550 0.5228  171 SER H OG  
17062 N N   . THR I 172 ? 2.2731 4.2747 3.0022 0.7677  -0.1397 0.5975  172 THR H N   
17063 C CA  . THR I 172 ? 2.2922 4.3134 2.9779 0.7606  -0.1371 0.6128  172 THR H CA  
17064 C C   . THR I 172 ? 2.2473 4.2554 2.9137 0.7516  -0.1458 0.6153  172 THR H C   
17065 O O   . THR I 172 ? 2.1965 4.1781 2.8808 0.7488  -0.1525 0.6082  172 THR H O   
17066 C CB  . THR I 172 ? 2.3063 4.3293 2.9748 0.7500  -0.1225 0.6359  172 THR H CB  
17067 O OG1 . THR I 172 ? 2.2541 4.2458 2.9300 0.7383  -0.1191 0.6455  172 THR H OG1 
17068 C CG2 . THR I 172 ? 2.3585 4.3954 3.0443 0.7594  -0.1141 0.6335  172 THR H CG2 
17069 N N   . TYR I 173 ? 2.2843 4.3116 2.9137 0.7470  -0.1451 0.6259  173 TYR H N   
17070 C CA  . TYR I 173 ? 2.2538 4.2714 2.8590 0.7371  -0.1515 0.6318  173 TYR H CA  
17071 C C   . TYR I 173 ? 2.2524 4.2703 2.8295 0.7215  -0.1404 0.6564  173 TYR H C   
17072 O O   . TYR I 173 ? 2.2853 4.3199 2.8556 0.7206  -0.1289 0.6677  173 TYR H O   
17073 C CB  . TYR I 173 ? 2.2873 4.3281 2.8722 0.7451  -0.1608 0.6227  173 TYR H CB  
17074 C CG  . TYR I 173 ? 2.2956 4.3411 2.9037 0.7613  -0.1730 0.5971  173 TYR H CG  
17075 C CD1 . TYR I 173 ? 2.3465 4.4165 2.9671 0.7758  -0.1717 0.5854  173 TYR H CD1 
17076 C CD2 . TYR I 173 ? 2.2558 4.2829 2.8724 0.7622  -0.1862 0.5841  173 TYR H CD2 
17077 C CE1 . TYR I 173 ? 2.3558 4.4312 2.9984 0.7908  -0.1829 0.5609  173 TYR H CE1 
17078 C CE2 . TYR I 173 ? 2.2634 4.2959 2.9019 0.7772  -0.1975 0.5599  173 TYR H CE2 
17079 C CZ  . TYR I 173 ? 2.3129 4.3697 2.9646 0.7913  -0.1958 0.5482  173 TYR H CZ  
17080 O OH  . TYR I 173 ? 2.3222 4.3851 2.9972 0.8063  -0.2070 0.5231  173 TYR H OH  
17081 N N   . SER I 174 ? 2.2788 4.2782 2.8405 0.7093  -0.1440 0.6641  174 SER H N   
17082 C CA  . SER I 174 ? 2.2813 4.2834 2.8141 0.6944  -0.1353 0.6856  174 SER H CA  
17083 C C   . SER I 174 ? 2.2813 4.2853 2.7884 0.6895  -0.1436 0.6868  174 SER H C   
17084 O O   . SER I 174 ? 2.2618 4.2530 2.7753 0.6938  -0.1563 0.6728  174 SER H O   
17085 C CB  . SER I 174 ? 2.2360 4.2096 2.7771 0.6816  -0.1287 0.6970  174 SER H CB  
17086 O OG  . SER I 174 ? 2.2465 4.2206 2.8075 0.6856  -0.1194 0.6987  174 SER H OG  
17087 N N   . LEU I 175 ? 2.3118 4.2874 2.8609 -1.2821 -0.1749 0.1312  175 LEU H N   
17088 C CA  . LEU I 175 ? 2.3165 4.3172 2.8772 -1.2869 -0.1699 0.1566  175 LEU H CA  
17089 C C   . LEU I 175 ? 2.2799 4.2781 2.8838 -1.2618 -0.1474 0.1526  175 LEU H C   
17090 O O   . LEU I 175 ? 2.2618 4.2450 2.8689 -1.2497 -0.1332 0.1217  175 LEU H O   
17091 C CB  . LEU I 175 ? 2.3496 4.3655 2.8676 -1.3113 -0.1729 0.1487  175 LEU H CB  
17092 C CG  . LEU I 175 ? 2.3606 4.4041 2.8822 -1.3206 -0.1691 0.1730  175 LEU H CG  
17093 C CD1 . LEU I 175 ? 2.4030 4.4612 2.8743 -1.3507 -0.1823 0.1726  175 LEU H CD1 
17094 C CD2 . LEU I 175 ? 2.3360 4.3813 2.8817 -1.3046 -0.1459 0.1597  175 LEU H CD2 
17095 N N   . SER I 176 ? 2.1577 4.1701 2.7942 -1.2542 -0.1446 0.1843  176 SER H N   
17096 C CA  . SER I 176 ? 2.1291 4.1420 2.8055 -1.2329 -0.1244 0.1856  176 SER H CA  
17097 C C   . SER I 176 ? 2.1712 4.2090 2.8437 -1.2448 -0.1218 0.2058  176 SER H C   
17098 O O   . SER I 176 ? 2.1891 4.2453 2.8495 -1.2610 -0.1359 0.2344  176 SER H O   
17099 C CB  . SER I 176 ? 2.0581 4.0646 2.7799 -1.2107 -0.1214 0.2048  176 SER H CB  
17100 O OG  . SER I 176 ? 2.0529 4.0790 2.7801 -1.2192 -0.1332 0.2431  176 SER H OG  
17101 N N   . SER I 177 ? 1.9485 3.9867 2.6308 -1.2367 -0.1041 0.1912  177 SER H N   
17102 C CA  . SER I 177 ? 1.9583 4.0184 2.6449 -1.2432 -0.0984 0.2100  177 SER H CA  
17103 C C   . SER I 177 ? 1.9254 3.9793 2.6604 -1.2172 -0.0798 0.2150  177 SER H C   
17104 O O   . SER I 177 ? 1.9009 3.9364 2.6511 -1.2001 -0.0653 0.1890  177 SER H O   
17105 C CB  . SER I 177 ? 1.9788 4.0474 2.6286 -1.2602 -0.0948 0.1887  177 SER H CB  
17106 O OG  . SER I 177 ? 1.9910 4.0823 2.6428 -1.2684 -0.0910 0.2089  177 SER H OG  
17107 N N   . THR I 178 ? 1.9150 3.9839 2.6736 -1.2145 -0.0804 0.2483  178 THR H N   
17108 C CA  . THR I 178 ? 1.8857 3.9487 2.6917 -1.1899 -0.0647 0.2575  178 THR H CA  
17109 C C   . THR I 178 ? 1.8938 3.9744 2.7058 -1.1940 -0.0562 0.2715  178 THR H C   
17110 O O   . THR I 178 ? 1.9167 4.0188 2.7180 -1.2090 -0.0663 0.2992  178 THR H O   
17111 C CB  . THR I 178 ? 1.8761 3.9396 2.7095 -1.1795 -0.0720 0.2853  178 THR H CB  
17112 O OG1 . THR I 178 ? 1.8718 3.9206 2.6966 -1.1781 -0.0817 0.2737  178 THR H OG1 
17113 C CG2 . THR I 178 ? 1.8447 3.8992 2.7263 -1.1529 -0.0551 0.2905  178 THR H CG2 
17114 N N   . LEU I 179 ? 2.1699 4.2410 2.9989 -1.1804 -0.0379 0.2529  179 LEU H N   
17115 C CA  . LEU I 179 ? 2.2130 4.2977 3.0514 -1.1813 -0.0275 0.2635  179 LEU H CA  
17116 C C   . LEU I 179 ? 2.1728 4.2517 3.0600 -1.1582 -0.0166 0.2816  179 LEU H C   
17117 O O   . LEU I 179 ? 2.1240 4.1817 3.0390 -1.1366 -0.0057 0.2665  179 LEU H O   
17118 C CB  . LEU I 179 ? 2.2456 4.3236 3.0716 -1.1812 -0.0142 0.2320  179 LEU H CB  
17119 C CG  . LEU I 179 ? 2.2889 4.3768 3.1277 -1.1790 -0.0005 0.2372  179 LEU H CG  
17120 C CD1 . LEU I 179 ? 2.3762 4.4920 3.1856 -1.2037 -0.0103 0.2564  179 LEU H CD1 
17121 C CD2 . LEU I 179 ? 2.2983 4.3728 3.1335 -1.1718 0.0145  0.2032  179 LEU H CD2 
17122 N N   . THR I 180 ? 2.1718 4.2694 3.0689 -1.1628 -0.0197 0.3136  180 THR H N   
17123 C CA  . THR I 180 ? 2.1467 4.2413 3.0876 -1.1426 -0.0110 0.3339  180 THR H CA  
17124 C C   . THR I 180 ? 2.1866 4.2900 3.1405 -1.1410 0.0013  0.3415  180 THR H C   
17125 O O   . THR I 180 ? 2.2707 4.3953 3.2039 -1.1592 -0.0050 0.3572  180 THR H O   
17126 C CB  . THR I 180 ? 2.1443 4.2524 3.0894 -1.1467 -0.0255 0.3678  180 THR H CB  
17127 O OG1 . THR I 180 ? 2.1529 4.2542 3.0814 -1.1514 -0.0386 0.3610  180 THR H OG1 
17128 C CG2 . THR I 180 ? 2.1180 4.2206 3.1083 -1.1238 -0.0159 0.3851  180 THR H CG2 
17129 N N   . LEU I 181 ? 2.2907 4.3775 3.2786 -1.1193 0.0186  0.3306  181 LEU H N   
17130 C CA  . LEU I 181 ? 2.3302 4.4214 3.3361 -1.1143 0.0319  0.3367  181 LEU H CA  
17131 C C   . LEU I 181 ? 2.2896 4.3698 3.3417 -1.0904 0.0423  0.3491  181 LEU H C   
17132 O O   . LEU I 181 ? 2.2260 4.2901 3.2968 -1.0748 0.0436  0.3425  181 LEU H O   
17133 C CB  . LEU I 181 ? 2.3476 4.4283 3.3453 -1.1130 0.0445  0.3052  181 LEU H CB  
17134 C CG  . LEU I 181 ? 2.4140 4.5024 3.3656 -1.1343 0.0372  0.2855  181 LEU H CG  
17135 C CD1 . LEU I 181 ? 2.4502 4.5215 3.4001 -1.1262 0.0507  0.2505  181 LEU H CD1 
17136 C CD2 . LEU I 181 ? 2.5198 4.6350 3.4472 -1.1559 0.0312  0.3032  181 LEU H CD2 
17137 N N   . SER I 182 ? 2.5660 4.6556 3.6358 -1.0879 0.0496  0.3674  182 SER H N   
17138 C CA  . SER I 182 ? 2.5574 4.6347 3.6704 -1.0649 0.0624  0.3741  182 SER H CA  
17139 C C   . SER I 182 ? 2.5105 4.5639 3.6400 -1.0492 0.0788  0.3429  182 SER H C   
17140 O O   . SER I 182 ? 2.5344 4.5843 3.6427 -1.0571 0.0818  0.3197  182 SER H O   
17141 C CB  . SER I 182 ? 2.6313 4.7246 3.7573 -1.0672 0.0656  0.4015  182 SER H CB  
17142 O OG  . SER I 182 ? 2.6951 4.7933 3.8098 -1.0761 0.0728  0.3922  182 SER H OG  
17143 N N   . LYS I 183 ? 2.4799 4.5171 3.6473 -1.0267 0.0891  0.3428  183 LYS H N   
17144 C CA  . LYS I 183 ? 2.4526 4.4660 3.6393 -1.0102 0.1047  0.3152  183 LYS H CA  
17145 C C   . LYS I 183 ? 2.5270 4.5429 3.7123 -1.0147 0.1152  0.3087  183 LYS H C   
17146 O O   . LYS I 183 ? 2.5162 4.5197 3.6938 -1.0131 0.1225  0.2817  183 LYS H O   
17147 C CB  . LYS I 183 ? 2.4312 4.4296 3.6597 -0.9862 0.1138  0.3202  183 LYS H CB  
17148 C CG  . LYS I 183 ? 2.3838 4.3566 3.6341 -0.9683 0.1293  0.2926  183 LYS H CG  
17149 C CD  . LYS I 183 ? 2.3851 4.3452 3.6769 -0.9455 0.1387  0.2996  183 LYS H CD  
17150 C CE  . LYS I 183 ? 2.3927 4.3253 3.7037 -0.9271 0.1507  0.2708  183 LYS H CE  
17151 N NZ  . LYS I 183 ? 2.4688 4.3940 3.7791 -0.9282 0.1617  0.2541  183 LYS H NZ  
17152 N N   . ALA I 184 ? 2.6070 4.6390 3.7999 -1.0198 0.1161  0.3336  184 ALA H N   
17153 C CA  . ALA I 184 ? 2.6814 4.7173 3.8738 -1.0246 0.1256  0.3302  184 ALA H CA  
17154 C C   . ALA I 184 ? 2.7341 4.7792 3.8864 -1.0438 0.1208  0.3137  184 ALA H C   
17155 O O   . ALA I 184 ? 2.7585 4.7943 3.9081 -1.0418 0.1307  0.2913  184 ALA H O   
17156 C CB  . ALA I 184 ? 2.7312 4.7857 3.9336 -1.0295 0.1243  0.3625  184 ALA H CB  
17157 N N   . ASP I 185 ? 2.7692 4.8334 3.8893 -1.0630 0.1054  0.3249  185 ASP H N   
17158 C CA  . ASP I 185 ? 2.8300 4.9049 3.9091 -1.0827 0.0999  0.3095  185 ASP H CA  
17159 C C   . ASP I 185 ? 2.7831 4.8389 3.8510 -1.0773 0.1026  0.2752  185 ASP H C   
17160 O O   . ASP I 185 ? 2.8144 4.8709 3.8598 -1.0854 0.1065  0.2540  185 ASP H O   
17161 C CB  . ASP I 185 ? 2.8502 4.9482 3.8980 -1.1039 0.0818  0.3291  185 ASP H CB  
17162 C CG  . ASP I 185 ? 2.9769 5.0983 4.0221 -1.1159 0.0790  0.3576  185 ASP H CG  
17163 O OD1 . ASP I 185 ? 3.0574 5.1784 4.1189 -1.1108 0.0911  0.3587  185 ASP H OD1 
17164 O OD2 . ASP I 185 ? 2.9984 5.1385 4.0250 -1.1307 0.0644  0.3794  185 ASP H OD2 
17165 N N   . TYR I 186 ? 2.6947 4.7342 3.7768 -1.0641 0.1003  0.2697  186 TYR H N   
17166 C CA  . TYR I 186 ? 2.6594 4.6796 3.7320 -1.0578 0.1024  0.2378  186 TYR H CA  
17167 C C   . TYR I 186 ? 2.6975 4.7006 3.7864 -1.0443 0.1193  0.2153  186 TYR H C   
17168 O O   . TYR I 186 ? 2.6900 4.6878 3.7558 -1.0490 0.1218  0.1889  186 TYR H O   
17169 C CB  . TYR I 186 ? 2.5584 4.5640 3.6494 -1.0436 0.0982  0.2389  186 TYR H CB  
17170 C CG  . TYR I 186 ? 2.4935 4.4781 3.5763 -1.0360 0.1000  0.2069  186 TYR H CG  
17171 C CD1 . TYR I 186 ? 2.5287 4.5179 3.5705 -1.0524 0.0899  0.1904  186 TYR H CD1 
17172 C CD2 . TYR I 186 ? 2.4529 4.4131 3.5681 -1.0125 0.1117  0.1931  186 TYR H CD2 
17173 C CE1 . TYR I 186 ? 2.4733 4.4432 3.5064 -1.0455 0.0915  0.1611  186 TYR H CE1 
17174 C CE2 . TYR I 186 ? 2.4181 4.3589 3.5252 -1.0053 0.1131  0.1645  186 TYR H CE2 
17175 C CZ  . TYR I 186 ? 2.4223 4.3681 3.4882 -1.0218 0.1030  0.1485  186 TYR H CZ  
17176 O OH  . TYR I 186 ? 2.4249 4.3514 3.4813 -1.0147 0.1042  0.1197  186 TYR H OH  
17177 N N   . GLU I 187 ? 2.5107 4.5049 3.6386 -1.0276 0.1308  0.2253  187 GLU H N   
17178 C CA  . GLU I 187 ? 2.5179 4.4947 3.6650 -1.0137 0.1465  0.2063  187 GLU H CA  
17179 C C   . GLU I 187 ? 2.6079 4.5980 3.7416 -1.0256 0.1523  0.2058  187 GLU H C   
17180 O O   . GLU I 187 ? 2.6184 4.5959 3.7636 -1.0164 0.1648  0.1893  187 GLU H O   
17181 C CB  . GLU I 187 ? 2.4820 4.4439 3.6759 -0.9917 0.1563  0.2170  187 GLU H CB  
17182 C CG  . GLU I 187 ? 2.3920 4.3419 3.6008 -0.9791 0.1514  0.2181  187 GLU H CG  
17183 C CD  . GLU I 187 ? 2.4200 4.3522 3.6737 -0.9558 0.1629  0.2218  187 GLU H CD  
17184 O OE1 . GLU I 187 ? 2.4712 4.4113 3.7462 -0.9532 0.1673  0.2433  187 GLU H OE1 
17185 O OE2 . GLU I 187 ? 2.3429 4.2536 3.6099 -0.9402 0.1674  0.2029  187 GLU H OE2 
17186 N N   . LYS I 188 ? 2.5059 4.5215 3.6158 -1.0456 0.1434  0.2239  188 LYS H N   
17187 C CA  . LYS I 188 ? 2.6197 4.6510 3.7138 -1.0587 0.1478  0.2244  188 LYS H CA  
17188 C C   . LYS I 188 ? 2.6406 4.6777 3.6928 -1.0733 0.1448  0.1992  188 LYS H C   
17189 O O   . LYS I 188 ? 2.7254 4.7768 3.7600 -1.0852 0.1482  0.1966  188 LYS H O   
17190 C CB  . LYS I 188 ? 2.6689 4.7258 3.7571 -1.0734 0.1395  0.2568  188 LYS H CB  
17191 C CG  . LYS I 188 ? 2.8075 4.8803 3.8900 -1.0835 0.1455  0.2644  188 LYS H CG  
17192 C CD  . LYS I 188 ? 2.8692 4.9679 3.9414 -1.0993 0.1351  0.2962  188 LYS H CD  
17193 C CE  . LYS I 188 ? 2.8306 4.9255 3.9345 -1.0876 0.1327  0.3216  188 LYS H CE  
17194 N NZ  . LYS I 188 ? 2.9180 5.0379 4.0130 -1.1020 0.1231  0.3536  188 LYS H NZ  
17195 N N   . HIS I 189 ? 2.7155 4.7418 3.7515 -1.0722 0.1388  0.1799  189 HIS H N   
17196 C CA  . HIS I 189 ? 2.7107 4.7409 3.7056 -1.0854 0.1357  0.1537  189 HIS H CA  
17197 C C   . HIS I 189 ? 2.6126 4.6168 3.6117 -1.0703 0.1394  0.1256  189 HIS H C   
17198 O O   . HIS I 189 ? 2.5720 4.5580 3.6015 -1.0526 0.1408  0.1292  189 HIS H O   
17199 C CB  . HIS I 189 ? 2.7426 4.7942 3.6989 -1.1084 0.1188  0.1624  189 HIS H CB  
17200 C CG  . HIS I 189 ? 2.8238 4.9020 3.7726 -1.1244 0.1134  0.1907  189 HIS H CG  
17201 N ND1 . HIS I 189 ? 2.8546 4.9435 3.8098 -1.1291 0.1022  0.2201  189 HIS H ND1 
17202 C CD2 . HIS I 189 ? 2.9193 5.0160 3.8539 -1.1368 0.1175  0.1943  189 HIS H CD2 
17203 C CE1 . HIS I 189 ? 2.9238 5.0361 3.8692 -1.1437 0.0995  0.2407  189 HIS H CE1 
17204 N NE2 . HIS I 189 ? 2.9760 5.0935 3.9090 -1.1486 0.1086  0.2256  189 HIS H NE2 
17205 N N   . LYS I 190 ? 2.6259 4.6290 3.5934 -1.0775 0.1411  0.0972  190 LYS H N   
17206 C CA  . LYS I 190 ? 2.5887 4.5677 3.5553 -1.0643 0.1451  0.0679  190 LYS H CA  
17207 C C   . LYS I 190 ? 2.5870 4.5681 3.5157 -1.0769 0.1324  0.0525  190 LYS H C   
17208 O O   . LYS I 190 ? 2.5380 4.5036 3.4756 -1.0675 0.1270  0.0496  190 LYS H O   
17209 C CB  . LYS I 190 ? 2.6519 4.6242 3.6146 -1.0593 0.1590  0.0439  190 LYS H CB  
17210 C CG  . LYS I 190 ? 2.6146 4.5653 3.5661 -1.0495 0.1622  0.0106  190 LYS H CG  
17211 C CD  . LYS I 190 ? 2.6740 4.6180 3.6243 -1.0432 0.1764  -0.0111 190 LYS H CD  
17212 C CE  . LYS I 190 ? 2.7644 4.7329 3.6744 -1.0649 0.1761  -0.0197 190 LYS H CE  
17213 N NZ  . LYS I 190 ? 2.7828 4.7444 3.6851 -1.0593 0.1891  -0.0461 190 LYS H NZ  
17214 N N   . VAL I 191 ? 2.6354 4.6355 3.5214 -1.0983 0.1275  0.0426  191 VAL H N   
17215 C CA  . VAL I 191 ? 2.6325 4.6327 3.4787 -1.1105 0.1175  0.0215  191 VAL H CA  
17216 C C   . VAL I 191 ? 2.6212 4.6353 3.4541 -1.1253 0.1000  0.0436  191 VAL H C   
17217 O O   . VAL I 191 ? 2.6535 4.6911 3.4766 -1.1411 0.0940  0.0659  191 VAL H O   
17218 C CB  . VAL I 191 ? 2.6930 4.7078 3.4981 -1.1269 0.1208  -0.0010 191 VAL H CB  
17219 C CG1 . VAL I 191 ? 2.7254 4.7361 3.4912 -1.1367 0.1124  -0.0272 191 VAL H CG1 
17220 C CG2 . VAL I 191 ? 2.7558 4.7605 3.5760 -1.1131 0.1384  -0.0180 191 VAL H CG2 
17221 N N   . TYR I 192 ? 2.6314 4.6308 3.4637 -1.1201 0.0915  0.0378  192 TYR H N   
17222 C CA  . TYR I 192 ? 2.6363 4.6463 3.4539 -1.1338 0.0739  0.0561  192 TYR H CA  
17223 C C   . TYR I 192 ? 2.6044 4.6105 3.3811 -1.1458 0.0645  0.0308  192 TYR H C   
17224 O O   . TYR I 192 ? 2.5623 4.5458 3.3425 -1.1325 0.0683  0.0072  192 TYR H O   
17225 C CB  . TYR I 192 ? 2.5248 4.5219 3.3820 -1.1166 0.0712  0.0764  192 TYR H CB  
17226 C CG  . TYR I 192 ? 2.5376 4.5416 3.4315 -1.1080 0.0782  0.1045  192 TYR H CG  
17227 C CD1 . TYR I 192 ? 2.5219 4.5111 3.4502 -1.0877 0.0946  0.0991  192 TYR H CD1 
17228 C CD2 . TYR I 192 ? 2.5546 4.5799 3.4473 -1.1206 0.0683  0.1363  192 TYR H CD2 
17229 C CE1 . TYR I 192 ? 2.5312 4.5261 3.4922 -1.0802 0.1010  0.1239  192 TYR H CE1 
17230 C CE2 . TYR I 192 ? 2.5836 4.6150 3.5084 -1.1128 0.0749  0.1613  192 TYR H CE2 
17231 C CZ  . TYR I 192 ? 2.5572 4.5733 3.5161 -1.0928 0.0913  0.1547  192 TYR H CZ  
17232 O OH  . TYR I 192 ? 2.6063 4.6279 3.5967 -1.0854 0.0977  0.1791  192 TYR H OH  
17233 N N   . ALA I 193 ? 2.4882 4.5156 3.2259 -1.1709 0.0519  0.0358  193 ALA H N   
17234 C CA  . ALA I 193 ? 2.5273 4.5534 3.2211 -1.1855 0.0427  0.0114  193 ALA H CA  
17235 C C   . ALA I 193 ? 2.5204 4.5631 3.1889 -1.2072 0.0230  0.0317  193 ALA H C   
17236 O O   . ALA I 193 ? 2.5714 4.6359 3.2395 -1.2193 0.0181  0.0586  193 ALA H O   
17237 C CB  . ALA I 193 ? 2.5970 4.6332 3.2575 -1.1969 0.0510  -0.0147 193 ALA H CB  
17238 N N   . CYS I 194 ? 2.6188 4.6505 3.2662 -1.2121 0.0113  0.0191  194 CYS H N   
17239 C CA  . CYS I 194 ? 2.6514 4.6970 3.2657 -1.2354 -0.0084 0.0317  194 CYS H CA  
17240 C C   . CYS I 194 ? 2.7109 4.7570 3.2754 -1.2522 -0.0126 0.0003  194 CYS H C   
17241 O O   . CYS I 194 ? 2.6973 4.7229 3.2566 -1.2419 -0.0068 -0.0300 194 CYS H O   
17242 C CB  . CYS I 194 ? 2.6090 4.6419 3.2411 -1.2281 -0.0208 0.0481  194 CYS H CB  
17243 S SG  . CYS I 194 ? 2.5958 4.5958 3.2296 -1.2121 -0.0210 0.0178  194 CYS H SG  
17244 N N   . GLU I 195 ? 2.5878 4.6574 3.1154 -1.2779 -0.0222 0.0072  195 GLU H N   
17245 C CA  . GLU I 195 ? 2.6642 4.7378 3.1413 -1.2967 -0.0270 -0.0206 195 GLU H CA  
17246 C C   . GLU I 195 ? 2.6523 4.7277 3.1005 -1.3154 -0.0493 -0.0101 195 GLU H C   
17247 O O   . GLU I 195 ? 2.6729 4.7651 3.1214 -1.3278 -0.0611 0.0219  195 GLU H O   
17248 C CB  . GLU I 195 ? 2.7840 4.8839 3.2380 -1.3125 -0.0204 -0.0230 195 GLU H CB  
17249 C CG  . GLU I 195 ? 2.8956 4.9978 3.3028 -1.3262 -0.0188 -0.0589 195 GLU H CG  
17250 C CD  . GLU I 195 ? 3.0629 5.1946 3.4455 -1.3440 -0.0139 -0.0585 195 GLU H CD  
17251 O OE1 . GLU I 195 ? 3.0959 5.2465 3.4954 -1.3478 -0.0139 -0.0284 195 GLU H OE1 
17252 O OE2 . GLU I 195 ? 3.1466 5.2829 3.4930 -1.3540 -0.0098 -0.0886 195 GLU H OE2 
17253 N N   . VAL I 196 ? 2.7193 4.7764 3.1424 -1.3172 -0.0552 -0.0367 196 VAL H N   
17254 C CA  . VAL I 196 ? 2.7230 4.7748 3.1220 -1.3314 -0.0765 -0.0293 196 VAL H CA  
17255 C C   . VAL I 196 ? 2.8191 4.8774 3.1618 -1.3550 -0.0843 -0.0522 196 VAL H C   
17256 O O   . VAL I 196 ? 2.8583 4.9074 3.1829 -1.3515 -0.0741 -0.0873 196 VAL H O   
17257 C CB  . VAL I 196 ? 2.6518 4.6735 3.0705 -1.3125 -0.0788 -0.0390 196 VAL H CB  
17258 C CG1 . VAL I 196 ? 2.6637 4.6776 3.0518 -1.3281 -0.1007 -0.0368 196 VAL H CG1 
17259 C CG2 . VAL I 196 ? 2.5791 4.5962 3.0520 -1.2910 -0.0735 -0.0129 196 VAL H CG2 
17260 N N   . THR I 197 ? 2.5046 4.5786 2.8194 -1.3788 -0.1022 -0.0323 197 THR H N   
17261 C CA  . THR I 197 ? 2.5428 4.6223 2.8025 -1.4030 -0.1128 -0.0504 197 THR H CA  
17262 C C   . THR I 197 ? 2.5613 4.6243 2.8018 -1.4120 -0.1347 -0.0450 197 THR H C   
17263 O O   . THR I 197 ? 2.5654 4.6332 2.8201 -1.4161 -0.1479 -0.0117 197 THR H O   
17264 C CB  . THR I 197 ? 2.5715 4.6839 2.8099 -1.4256 -0.1163 -0.0322 197 THR H CB  
17265 O OG1 . THR I 197 ? 2.5535 4.6807 2.8130 -1.4161 -0.0960 -0.0348 197 THR H OG1 
17266 C CG2 . THR I 197 ? 2.6115 4.7291 2.7918 -1.4500 -0.1261 -0.0535 197 THR H CG2 
17267 N N   . HIS I 198 ? 2.8051 4.8482 3.0134 -1.4146 -0.1384 -0.0774 198 HIS H N   
17268 C CA  . HIS I 198 ? 2.8073 4.8317 2.9933 -1.4235 -0.1595 -0.0759 198 HIS H CA  
17269 C C   . HIS I 198 ? 2.8922 4.9040 3.0282 -1.4342 -0.1625 -0.1130 198 HIS H C   
17270 O O   . HIS I 198 ? 2.9201 4.9272 3.0516 -1.4245 -0.1458 -0.1448 198 HIS H O   
17271 C CB  . HIS I 198 ? 2.7164 4.7154 2.9397 -1.4007 -0.1598 -0.0725 198 HIS H CB  
17272 C CG  . HIS I 198 ? 2.7129 4.6936 2.9186 -1.4088 -0.1820 -0.0657 198 HIS H CG  
17273 N ND1 . HIS I 198 ? 2.7502 4.7047 2.9260 -1.4092 -0.1883 -0.0959 198 HIS H ND1 
17274 C CD2 . HIS I 198 ? 2.6776 4.6618 2.8919 -1.4162 -0.1995 -0.0316 198 HIS H CD2 
17275 C CE1 . HIS I 198 ? 2.7394 4.6814 2.9063 -1.4167 -0.2090 -0.0806 198 HIS H CE1 
17276 N NE2 . HIS I 198 ? 2.6938 4.6542 2.8836 -1.4214 -0.2162 -0.0416 198 HIS H NE2 
17277 N N   . GLN I 199 ? 2.8274 4.8329 2.9256 -1.4538 -0.1841 -0.1086 199 GLN H N   
17278 C CA  . GLN I 199 ? 2.9223 4.9161 2.9693 -1.4655 -0.1887 -0.1419 199 GLN H CA  
17279 C C   . GLN I 199 ? 2.9123 4.8716 2.9589 -1.4468 -0.1836 -0.1758 199 GLN H C   
17280 O O   . GLN I 199 ? 2.9878 4.9365 2.9983 -1.4499 -0.1806 -0.2095 199 GLN H O   
17281 C CB  . GLN I 199 ? 2.9796 4.9716 2.9864 -1.4901 -0.2143 -0.1279 199 GLN H CB  
17282 C CG  . GLN I 199 ? 2.9336 4.8976 2.9456 -1.4860 -0.2325 -0.1177 199 GLN H CG  
17283 C CD  . GLN I 199 ? 3.0073 4.9612 2.9709 -1.5087 -0.2568 -0.1153 199 GLN H CD  
17284 O OE1 . GLN I 199 ? 3.0716 5.0008 3.0000 -1.5097 -0.2619 -0.1455 199 GLN H OE1 
17285 N NE2 . GLN I 199 ? 3.0011 4.9727 2.9625 -1.5262 -0.2722 -0.0791 199 GLN H NE2 
17286 N N   . GLY I 200 ? 3.0943 5.0360 3.1804 -1.4268 -0.1824 -0.1677 200 GLY H N   
17287 C CA  . GLY I 200 ? 3.0873 4.9970 3.1766 -1.4075 -0.1764 -0.1987 200 GLY H CA  
17288 C C   . GLY I 200 ? 3.0797 4.9908 3.1851 -1.3896 -0.1508 -0.2257 200 GLY H C   
17289 O O   . GLY I 200 ? 3.0920 4.9788 3.1881 -1.3768 -0.1442 -0.2584 200 GLY H O   
17290 N N   . LEU I 201 ? 3.0863 5.0250 3.2146 -1.3886 -0.1366 -0.2125 201 LEU H N   
17291 C CA  . LEU I 201 ? 3.0835 5.0271 3.2252 -1.3740 -0.1123 -0.2361 201 LEU H CA  
17292 C C   . LEU I 201 ? 3.1885 5.1488 3.2855 -1.3916 -0.1082 -0.2575 201 LEU H C   
17293 O O   . LEU I 201 ? 3.2274 5.2131 3.3061 -1.4127 -0.1160 -0.2388 201 LEU H O   
17294 C CB  . LEU I 201 ? 3.0113 4.9745 3.2008 -1.3631 -0.0994 -0.2103 201 LEU H CB  
17295 C CG  . LEU I 201 ? 2.9052 4.8550 3.1452 -1.3425 -0.0995 -0.1885 201 LEU H CG  
17296 C CD1 . LEU I 201 ? 2.8614 4.8343 3.1398 -1.3379 -0.0910 -0.1577 201 LEU H CD1 
17297 C CD2 . LEU I 201 ? 2.8649 4.7871 3.1253 -1.3166 -0.0862 -0.2159 201 LEU H CD2 
17298 N N   . SER I 202 ? 3.1386 5.0852 3.2177 -1.3828 -0.0960 -0.2963 202 SER H N   
17299 C CA  . SER I 202 ? 3.2407 5.2053 3.2805 -1.3971 -0.0892 -0.3181 202 SER H CA  
17300 C C   . SER I 202 ? 3.2315 5.2302 3.2918 -1.3989 -0.0731 -0.3057 202 SER H C   
17301 O O   . SER I 202 ? 3.3128 5.3360 3.3431 -1.4166 -0.0715 -0.3103 202 SER H O   
17302 C CB  . SER I 202 ? 3.2917 5.2340 3.3103 -1.3850 -0.0783 -0.3624 202 SER H CB  
17303 O OG  . SER I 202 ? 3.2364 5.1714 3.2930 -1.3606 -0.0580 -0.3740 202 SER H OG  
17304 N N   . SER I 203 ? 3.2980 5.2976 3.4088 -1.3802 -0.0615 -0.2898 203 SER H N   
17305 C CA  . SER I 203 ? 3.2851 5.3129 3.4203 -1.3791 -0.0468 -0.2749 203 SER H CA  
17306 C C   . SER I 203 ? 3.1860 5.2142 3.3721 -1.3670 -0.0480 -0.2381 203 SER H C   
17307 O O   . SER I 203 ? 3.1159 5.1192 3.3285 -1.3498 -0.0507 -0.2351 203 SER H O   
17308 C CB  . SER I 203 ? 3.2960 5.3220 3.4396 -1.3627 -0.0230 -0.3061 203 SER H CB  
17309 O OG  . SER I 203 ? 3.3017 5.3554 3.4636 -1.3637 -0.0099 -0.2925 203 SER H OG  
17310 N N   . PRO I 204 ? 3.1843 5.2402 3.3845 -1.3751 -0.0462 -0.2097 204 PRO H N   
17311 C CA  . PRO I 204 ? 3.1269 5.1836 3.3769 -1.3618 -0.0455 -0.1749 204 PRO H CA  
17312 C C   . PRO I 204 ? 3.0614 5.0979 3.3549 -1.3320 -0.0283 -0.1851 204 PRO H C   
17313 O O   . PRO I 204 ? 3.0847 5.1173 3.3761 -1.3222 -0.0116 -0.2134 204 PRO H O   
17314 C CB  . PRO I 204 ? 3.1854 5.2757 3.4372 -1.3747 -0.0415 -0.1523 204 PRO H CB  
17315 C CG  . PRO I 204 ? 3.2850 5.3925 3.4824 -1.4022 -0.0518 -0.1628 204 PRO H CG  
17316 C CD  . PRO I 204 ? 3.3297 5.4173 3.4971 -1.3991 -0.0481 -0.2054 204 PRO H CD  
17317 N N   . VAL I 205 ? 3.0588 5.0824 3.3918 -1.3174 -0.0327 -0.1612 205 VAL H N   
17318 C CA  . VAL I 205 ? 2.9831 4.9842 3.3585 -1.2886 -0.0195 -0.1680 205 VAL H CA  
17319 C C   . VAL I 205 ? 2.9289 4.9402 3.3509 -1.2766 -0.0114 -0.1372 205 VAL H C   
17320 O O   . VAL I 205 ? 2.9096 4.9337 3.3422 -1.2847 -0.0226 -0.1033 205 VAL H O   
17321 C CB  . VAL I 205 ? 2.9282 4.9023 3.3123 -1.2787 -0.0308 -0.1690 205 VAL H CB  
17322 C CG1 . VAL I 205 ? 2.8426 4.7986 3.2772 -1.2501 -0.0190 -0.1647 205 VAL H CG1 
17323 C CG2 . VAL I 205 ? 2.9771 4.9339 3.3222 -1.2828 -0.0338 -0.2057 205 VAL H CG2 
17324 N N   . THR I 206 ? 2.7101 4.7145 3.1593 -1.2570 0.0078  -0.1488 206 THR H N   
17325 C CA  . THR I 206 ? 2.6565 4.6637 3.1536 -1.2410 0.0172  -0.1234 206 THR H CA  
17326 C C   . THR I 206 ? 2.5731 4.5513 3.1095 -1.2127 0.0253  -0.1300 206 THR H C   
17327 O O   . THR I 206 ? 2.5707 4.5313 3.1024 -1.2009 0.0355  -0.1614 206 THR H O   
17328 C CB  . THR I 206 ? 2.7014 4.7259 3.1994 -1.2421 0.0330  -0.1281 206 THR H CB  
17329 O OG1 . THR I 206 ? 2.7817 4.8349 3.2437 -1.2686 0.0253  -0.1204 206 THR H OG1 
17330 C CG2 . THR I 206 ? 2.6490 4.6741 3.1968 -1.2251 0.0423  -0.1016 206 THR H CG2 
17331 N N   . LYS I 207 ? 2.6851 4.6589 3.2595 -1.2018 0.0207  -0.1005 207 LYS H N   
17332 C CA  . LYS I 207 ? 2.6066 4.5569 3.2254 -1.1740 0.0299  -0.1002 207 LYS H CA  
17333 C C   . LYS I 207 ? 2.5777 4.5365 3.2376 -1.1630 0.0398  -0.0741 207 LYS H C   
17334 O O   . LYS I 207 ? 2.5848 4.5626 3.2502 -1.1736 0.0321  -0.0435 207 LYS H O   
17335 C CB  . LYS I 207 ? 2.5513 4.4866 3.1819 -1.1682 0.0165  -0.0895 207 LYS H CB  
17336 C CG  . LYS I 207 ? 2.5639 4.4818 3.1637 -1.1713 0.0093  -0.1180 207 LYS H CG  
17337 C CD  . LYS I 207 ? 2.5506 4.4453 3.1614 -1.1500 0.0254  -0.1493 207 LYS H CD  
17338 C CE  . LYS I 207 ? 2.5275 4.3977 3.1276 -1.1432 0.0188  -0.1699 207 LYS H CE  
17339 N NZ  . LYS I 207 ? 2.5699 4.4277 3.1423 -1.1407 0.0284  -0.2103 207 LYS H NZ  
17340 N N   . SER I 208 ? 2.7682 4.7121 3.4564 -1.1416 0.0564  -0.0860 208 SER H N   
17341 C CA  . SER I 208 ? 2.7501 4.7006 3.4751 -1.1312 0.0672  -0.0647 208 SER H CA  
17342 C C   . SER I 208 ? 2.6826 4.6075 3.4500 -1.1026 0.0794  -0.0702 208 SER H C   
17343 O O   . SER I 208 ? 2.6559 4.5589 3.4209 -1.0911 0.0815  -0.0940 208 SER H O   
17344 C CB  . SER I 208 ? 2.8170 4.7850 3.5241 -1.1416 0.0772  -0.0732 208 SER H CB  
17345 O OG  . SER I 208 ? 2.8323 4.7867 3.5267 -1.1337 0.0889  -0.1085 208 SER H OG  
17346 N N   . PHE I 209 ? 2.7657 4.6933 3.5719 -1.0912 0.0871  -0.0469 209 PHE H N   
17347 C CA  . PHE I 209 ? 2.7137 4.6198 3.5609 -1.0650 0.1010  -0.0508 209 PHE H CA  
17348 C C   . PHE I 209 ? 2.7324 4.6493 3.6024 -1.0620 0.1121  -0.0347 209 PHE H C   
17349 O O   . PHE I 209 ? 2.7759 4.7164 3.6371 -1.0780 0.1075  -0.0143 209 PHE H O   
17350 C CB  . PHE I 209 ? 2.6427 4.5341 3.5243 -1.0490 0.0961  -0.0344 209 PHE H CB  
17351 C CG  . PHE I 209 ? 2.6344 4.5424 3.5364 -1.0537 0.0890  0.0029  209 PHE H CG  
17352 C CD1 . PHE I 209 ? 2.6155 4.5236 3.5575 -1.0403 0.0989  0.0228  209 PHE H CD1 
17353 C CD2 . PHE I 209 ? 2.6490 4.5722 3.5292 -1.0716 0.0724  0.0182  209 PHE H CD2 
17354 C CE1 . PHE I 209 ? 2.6134 4.5369 3.5729 -1.0444 0.0929  0.0564  209 PHE H CE1 
17355 C CE2 . PHE I 209 ? 2.6441 4.5828 3.5415 -1.0757 0.0660  0.0526  209 PHE H CE2 
17356 C CZ  . PHE I 209 ? 2.6272 4.5663 3.5641 -1.0619 0.0765  0.0714  209 PHE H CZ  
17357 N N   . ASN I 210 ? 2.6156 4.5148 3.5147 -1.0415 0.1265  -0.0437 210 ASN H N   
17358 C CA  . ASN I 210 ? 2.6240 4.5286 3.5522 -1.0347 0.1376  -0.0274 210 ASN H CA  
17359 C C   . ASN I 210 ? 2.5622 4.4547 3.5386 -1.0156 0.1397  -0.0047 210 ASN H C   
17360 O O   . ASN I 210 ? 2.5067 4.3763 3.5024 -0.9974 0.1424  -0.0147 210 ASN H O   
17361 C CB  . ASN I 210 ? 2.6394 4.5336 3.5667 -1.0260 0.1525  -0.0520 210 ASN H CB  
17362 C CG  . ASN I 210 ? 2.7102 4.6198 3.5908 -1.0453 0.1523  -0.0733 210 ASN H CG  
17363 O OD1 . ASN I 210 ? 2.7656 4.7005 3.6252 -1.0653 0.1465  -0.0606 210 ASN H OD1 
17364 N ND2 . ASN I 210 ? 2.7117 4.6068 3.5751 -1.0394 0.1589  -0.1061 210 ASN H ND2 
17365 N N   . ARG I 211 ? 2.5811 4.4895 3.5758 -1.0199 0.1384  0.0254  211 ARG H N   
17366 C CA  . ARG I 211 ? 2.5307 4.4307 3.5700 -1.0032 0.1406  0.0482  211 ARG H CA  
17367 C C   . ARG I 211 ? 2.5108 4.3870 3.5839 -0.9794 0.1554  0.0367  211 ARG H C   
17368 O O   . ARG I 211 ? 2.5260 4.4016 3.6026 -0.9775 0.1662  0.0297  211 ARG H O   
17369 C CB  . ARG I 211 ? 2.5658 4.4873 3.6169 -1.0119 0.1394  0.0797  211 ARG H CB  
17370 C CG  . ARG I 211 ? 2.5235 4.4373 3.6209 -0.9943 0.1438  0.1024  211 ARG H CG  
17371 C CD  . ARG I 211 ? 2.5675 4.5022 3.6746 -1.0030 0.1436  0.1318  211 ARG H CD  
17372 N NE  . ARG I 211 ? 2.6180 4.5576 3.7239 -1.0062 0.1543  0.1268  211 ARG H NE  
17373 C CZ  . ARG I 211 ? 2.6187 4.5449 3.7577 -0.9898 0.1680  0.1258  211 ARG H CZ  
17374 N NH1 . ARG I 211 ? 2.6938 4.6259 3.8292 -0.9944 0.1766  0.1218  211 ARG H NH1 
17375 N NH2 . ARG I 211 ? 2.5687 4.4758 3.7443 -0.9692 0.1730  0.1287  211 ARG H NH2 
17376 N N   . GLY I 212 ? 2.5743 4.4310 3.6720 -0.9616 0.1553  0.0354  212 GLY H N   
17377 C CA  . GLY I 212 ? 2.5376 4.3704 3.6672 -0.9385 0.1680  0.0247  212 GLY H CA  
17378 C C   . GLY I 212 ? 2.5106 4.3231 3.6233 -0.9309 0.1690  -0.0067 212 GLY H C   
17379 O O   . GLY I 212 ? 2.5573 4.3736 3.6334 -0.9427 0.1682  -0.0281 212 GLY H O   
17380 N N   . GLN J 1   ? 3.7961 2.1416 3.5859 -0.6773 -0.4943 0.5699  1   GLN I N   
17381 C CA  . GLN J 1   ? 3.6939 2.1016 3.5064 -0.7051 -0.4835 0.5644  1   GLN I CA  
17382 C C   . GLN J 1   ? 3.6659 2.1162 3.4032 -0.6851 -0.4923 0.5077  1   GLN I C   
17383 O O   . GLN J 1   ? 3.7360 2.1522 3.4110 -0.6634 -0.5231 0.4794  1   GLN I O   
17384 C CB  . GLN J 1   ? 3.6903 2.0675 3.5545 -0.7505 -0.5117 0.5999  1   GLN I CB  
17385 C CG  . GLN J 1   ? 3.8002 2.1203 3.6237 -0.7520 -0.5636 0.5884  1   GLN I CG  
17386 C CD  . GLN J 1   ? 3.9957 2.2354 3.8220 -0.7407 -0.5841 0.6115  1   GLN I CD  
17387 O OE1 . GLN J 1   ? 4.0560 2.2802 3.9159 -0.7321 -0.5596 0.6382  1   GLN I OE1 
17388 N NE2 . GLN J 1   ? 4.0965 2.2847 3.8879 -0.7408 -0.6293 0.6013  1   GLN I NE2 
17389 N N   . VAL J 2   ? 3.7262 2.2509 3.4697 -0.6921 -0.4649 0.4909  2   VAL I N   
17390 C CA  . VAL J 2   ? 3.6963 2.2693 3.3737 -0.6750 -0.4687 0.4378  2   VAL I CA  
17391 C C   . VAL J 2   ? 3.6358 2.2388 3.3336 -0.7122 -0.4823 0.4394  2   VAL I C   
17392 O O   . VAL J 2   ? 3.5576 2.2048 3.3117 -0.7382 -0.4560 0.4602  2   VAL I O   
17393 C CB  . VAL J 2   ? 3.6444 2.2836 3.3032 -0.6467 -0.4241 0.4102  2   VAL I CB  
17394 C CG1 . VAL J 2   ? 3.6210 2.3103 3.2129 -0.6306 -0.4289 0.3556  2   VAL I CG1 
17395 C CG2 . VAL J 2   ? 3.7091 2.3182 3.3456 -0.6087 -0.4110 0.4083  2   VAL I CG2 
17396 N N   . HIS J 3   ? 3.8049 2.3843 3.4577 -0.7149 -0.5232 0.4177  3   HIS I N   
17397 C CA  . HIS J 3   ? 3.7108 2.3155 3.3763 -0.7484 -0.5400 0.4168  3   HIS I CA  
17398 C C   . HIS J 3   ? 3.6745 2.3231 3.2664 -0.7287 -0.5473 0.3612  3   HIS I C   
17399 O O   . HIS J 3   ? 3.7602 2.3817 3.2847 -0.6994 -0.5703 0.3285  3   HIS I O   
17400 C CB  . HIS J 3   ? 3.7959 2.3359 3.4798 -0.7757 -0.5848 0.4434  3   HIS I CB  
17401 C CG  . HIS J 3   ? 3.7674 2.3344 3.4696 -0.8117 -0.6001 0.4459  3   HIS I CG  
17402 N ND1 . HIS J 3   ? 3.7175 2.3282 3.4849 -0.8440 -0.5747 0.4729  3   HIS I ND1 
17403 C CD2 . HIS J 3   ? 3.7921 2.3507 3.4543 -0.8195 -0.6377 0.4236  3   HIS I CD2 
17404 C CE1 . HIS J 3   ? 3.6808 2.3074 3.4485 -0.8705 -0.5963 0.4683  3   HIS I CE1 
17405 N NE2 . HIS J 3   ? 3.7149 2.3108 3.4191 -0.8563 -0.6345 0.4386  3   HIS I NE2 
17406 N N   . LEU J 4   ? 3.6157 2.3316 3.2218 -0.7453 -0.5277 0.3511  4   LEU I N   
17407 C CA  . LEU J 4   ? 3.5401 2.3056 3.0840 -0.7309 -0.5310 0.3006  4   LEU I CA  
17408 C C   . LEU J 4   ? 3.5064 2.2860 3.0670 -0.7680 -0.5533 0.3064  4   LEU I C   
17409 O O   . LEU J 4   ? 3.4533 2.2463 3.0826 -0.8037 -0.5421 0.3434  4   LEU I O   
17410 C CB  . LEU J 4   ? 3.4665 2.3069 3.0063 -0.7128 -0.4839 0.2777  4   LEU I CB  
17411 C CG  . LEU J 4   ? 3.4880 2.3215 3.0137 -0.6758 -0.4576 0.2719  4   LEU I CG  
17412 C CD1 . LEU J 4   ? 3.4223 2.3336 2.9434 -0.6590 -0.4120 0.2469  4   LEU I CD1 
17413 C CD2 . LEU J 4   ? 3.6348 2.4222 3.0857 -0.6400 -0.4861 0.2407  4   LEU I CD2 
17414 N N   . GLN J 5   ? 3.5572 2.3349 3.0546 -0.7592 -0.5846 0.2695  5   GLN I N   
17415 C CA  . GLN J 5   ? 3.5454 2.3347 3.0490 -0.7911 -0.6095 0.2705  5   GLN I CA  
17416 C C   . GLN J 5   ? 3.5416 2.3856 2.9796 -0.7737 -0.6092 0.2174  5   GLN I C   
17417 O O   . GLN J 5   ? 3.6019 2.4335 2.9691 -0.7398 -0.6233 0.1785  5   GLN I O   
17418 C CB  . GLN J 5   ? 3.6235 2.3377 3.1195 -0.8033 -0.6593 0.2856  5   GLN I CB  
17419 C CG  . GLN J 5   ? 3.6245 2.3441 3.1229 -0.8351 -0.6896 0.2863  5   GLN I CG  
17420 C CD  . GLN J 5   ? 3.5561 2.2985 3.1357 -0.8785 -0.6748 0.3289  5   GLN I CD  
17421 O OE1 . GLN J 5   ? 3.5240 2.2582 3.1654 -0.8895 -0.6508 0.3671  5   GLN I OE1 
17422 N NE2 . GLN J 5   ? 3.5404 2.3099 3.1202 -0.9037 -0.6901 0.3234  5   GLN I NE2 
17423 N N   . GLU J 6   ? 3.4887 2.3928 2.9507 -0.7970 -0.5931 0.2162  6   GLU I N   
17424 C CA  . GLU J 6   ? 3.4972 2.4581 2.9046 -0.7855 -0.5914 0.1691  6   GLU I CA  
17425 C C   . GLU J 6   ? 3.5651 2.5118 2.9554 -0.8088 -0.6324 0.1647  6   GLU I C   
17426 O O   . GLU J 6   ? 3.5572 2.4769 2.9989 -0.8444 -0.6492 0.2033  6   GLU I O   
17427 C CB  . GLU J 6   ? 3.3813 2.4212 2.8246 -0.7957 -0.5466 0.1685  6   GLU I CB  
17428 C CG  . GLU J 6   ? 3.3450 2.4084 2.8018 -0.7713 -0.5037 0.1680  6   GLU I CG  
17429 C CD  . GLU J 6   ? 3.3124 2.3473 2.8471 -0.7908 -0.4875 0.2214  6   GLU I CD  
17430 O OE1 . GLU J 6   ? 3.3285 2.3156 2.9018 -0.8200 -0.5134 0.2582  6   GLU I OE1 
17431 O OE2 . GLU J 6   ? 3.2755 2.3348 2.8322 -0.7761 -0.4493 0.2262  6   GLU I OE2 
17432 N N   . SER J 7   ? 3.5599 2.5257 2.8771 -0.7882 -0.6484 0.1169  7   SER I N   
17433 C CA  . SER J 7   ? 3.6196 2.5752 2.9132 -0.8070 -0.6875 0.1078  7   SER I CA  
17434 C C   . SER J 7   ? 3.6296 2.6416 2.8582 -0.7883 -0.6845 0.0551  7   SER I C   
17435 O O   . SER J 7   ? 3.6605 2.6800 2.8302 -0.7502 -0.6783 0.0165  7   SER I O   
17436 C CB  . SER J 7   ? 3.7407 2.6166 3.0045 -0.7999 -0.7335 0.1106  7   SER I CB  
17437 O OG  . SER J 7   ? 3.7743 2.6338 2.9728 -0.7568 -0.7362 0.0745  7   SER I OG  
17438 N N   . GLY J 8   ? 3.5687 2.6204 2.8086 -0.8150 -0.6884 0.0539  8   GLY I N   
17439 C CA  . GLY J 8   ? 3.5440 2.6503 2.7258 -0.8006 -0.6862 0.0061  8   GLY I CA  
17440 C C   . GLY J 8   ? 3.5856 2.7007 2.7642 -0.8296 -0.7148 0.0060  8   GLY I C   
17441 O O   . GLY J 8   ? 3.6165 2.6890 2.8314 -0.8590 -0.7417 0.0405  8   GLY I O   
17442 N N   . PRO J 9   ? 3.6222 2.7940 2.7571 -0.8214 -0.7093 -0.0334 9   PRO I N   
17443 C CA  . PRO J 9   ? 3.6611 2.8455 2.7896 -0.8479 -0.7357 -0.0358 9   PRO I CA  
17444 C C   . PRO J 9   ? 3.5975 2.8105 2.8036 -0.8902 -0.7192 0.0050  9   PRO I C   
17445 O O   . PRO J 9   ? 3.6238 2.8113 2.8540 -0.9209 -0.7479 0.0296  9   PRO I O   
17446 C CB  . PRO J 9   ? 3.6918 2.9340 2.7532 -0.8237 -0.7272 -0.0903 9   PRO I CB  
17447 C CG  . PRO J 9   ? 3.6300 2.9116 2.6936 -0.7981 -0.6823 -0.1041 9   PRO I CG  
17448 C CD  . PRO J 9   ? 3.6133 2.8379 2.6994 -0.7867 -0.6808 -0.0788 9   PRO I CD  
17449 N N   . GLY J 10  ? 3.7069 2.9725 2.9532 -0.8920 -0.6734 0.0127  10  GLY I N   
17450 C CA  . GLY J 10  ? 3.6461 2.9469 2.9658 -0.9291 -0.6518 0.0483  10  GLY I CA  
17451 C C   . GLY J 10  ? 3.6447 3.0188 2.9515 -0.9375 -0.6373 0.0238  10  GLY I C   
17452 O O   . GLY J 10  ? 3.5837 3.0086 2.9422 -0.9546 -0.6020 0.0399  10  GLY I O   
17453 N N   . LEU J 11  ? 3.5997 2.9804 2.8393 -0.9258 -0.6637 -0.0144 11  LEU I N   
17454 C CA  . LEU J 11  ? 3.6123 3.0611 2.8323 -0.9315 -0.6527 -0.0412 11  LEU I CA  
17455 C C   . LEU J 11  ? 3.6722 3.1373 2.8043 -0.8916 -0.6583 -0.0988 11  LEU I C   
17456 O O   . LEU J 11  ? 3.7466 3.1647 2.8250 -0.8763 -0.6957 -0.1168 11  LEU I O   
17457 C CB  . LEU J 11  ? 3.6562 3.0990 2.8905 -0.9671 -0.6834 -0.0239 11  LEU I CB  
17458 C CG  . LEU J 11  ? 3.6546 3.1687 2.8920 -0.9842 -0.6690 -0.0368 11  LEU I CG  
17459 C CD1 . LEU J 11  ? 3.7020 3.1972 2.9598 -1.0207 -0.7028 -0.0122 11  LEU I CD1 
17460 C CD2 . LEU J 11  ? 3.7009 3.2619 2.8629 -0.9538 -0.6636 -0.0939 11  LEU I CD2 
17461 N N   . VAL J 12  ? 3.5529 3.0840 2.6709 -0.8743 -0.6214 -0.1278 12  VAL I N   
17462 C CA  . VAL J 12  ? 3.6092 3.1631 2.6465 -0.8358 -0.6217 -0.1836 12  VAL I CA  
17463 C C   . VAL J 12  ? 3.6193 3.2497 2.6445 -0.8417 -0.6032 -0.2094 12  VAL I C   
17464 O O   . VAL J 12  ? 3.5513 3.2333 2.6274 -0.8564 -0.5659 -0.1952 12  VAL I O   
17465 C CB  . VAL J 12  ? 3.5727 3.1284 2.5967 -0.8000 -0.5931 -0.1993 12  VAL I CB  
17466 C CG1 . VAL J 12  ? 3.6391 3.2203 2.5790 -0.7608 -0.5940 -0.2580 12  VAL I CG1 
17467 C CG2 . VAL J 12  ? 3.5690 3.0488 2.6042 -0.7937 -0.6115 -0.1737 12  VAL I CG2 
17468 N N   . LYS J 13  ? 3.5315 3.1689 2.4895 -0.8300 -0.6289 -0.2474 13  LYS I N   
17469 C CA  . LYS J 13  ? 3.5576 3.2655 2.4969 -0.8335 -0.6143 -0.2751 13  LYS I CA  
17470 C C   . LYS J 13  ? 3.5205 3.2868 2.4455 -0.8054 -0.5706 -0.3066 13  LYS I C   
17471 O O   . LYS J 13  ? 3.5074 3.2554 2.4081 -0.7739 -0.5616 -0.3219 13  LYS I O   
17472 C CB  . LYS J 13  ? 3.6722 3.3708 2.5368 -0.8229 -0.6525 -0.3116 13  LYS I CB  
17473 C CG  . LYS J 13  ? 3.7239 3.3615 2.5902 -0.8452 -0.6999 -0.2878 13  LYS I CG  
17474 C CD  . LYS J 13  ? 3.6838 3.3341 2.6207 -0.8905 -0.6978 -0.2439 13  LYS I CD  
17475 C CE  . LYS J 13  ? 3.7363 3.3250 2.6764 -0.9126 -0.7452 -0.2196 13  LYS I CE  
17476 N NZ  . LYS J 13  ? 3.7008 3.3011 2.7107 -0.9569 -0.7433 -0.1760 13  LYS I NZ  
17477 N N   . PRO J 14  ? 3.6329 3.4700 2.5740 -0.8164 -0.5428 -0.3160 14  PRO I N   
17478 C CA  . PRO J 14  ? 3.6057 3.5024 2.5319 -0.7898 -0.5016 -0.3486 14  PRO I CA  
17479 C C   . PRO J 14  ? 3.6875 3.5836 2.5249 -0.7484 -0.5141 -0.4032 14  PRO I C   
17480 O O   . PRO J 14  ? 3.7769 3.6495 2.5605 -0.7443 -0.5511 -0.4232 14  PRO I O   
17481 C CB  . PRO J 14  ? 3.5994 3.5668 2.5545 -0.8140 -0.4795 -0.3485 14  PRO I CB  
17482 C CG  . PRO J 14  ? 3.5772 3.5197 2.5926 -0.8573 -0.4962 -0.2991 14  PRO I CG  
17483 C CD  . PRO J 14  ? 3.6319 3.4978 2.6158 -0.8560 -0.5445 -0.2920 14  PRO I CD  
17484 N N   . SER J 15  ? 3.6451 3.5677 2.4679 -0.7173 -0.4822 -0.4273 15  SER I N   
17485 C CA  . SER J 15  ? 3.7163 3.6428 2.4581 -0.6749 -0.4876 -0.4800 15  SER I CA  
17486 C C   . SER J 15  ? 3.7771 3.6275 2.4714 -0.6586 -0.5305 -0.4848 15  SER I C   
17487 O O   . SER J 15  ? 3.8862 3.7303 2.5080 -0.6358 -0.5539 -0.5249 15  SER I O   
17488 C CB  . SER J 15  ? 3.7957 3.7786 2.4914 -0.6708 -0.4880 -0.5206 15  SER I CB  
17489 O OG  . SER J 15  ? 3.8619 3.8206 2.5389 -0.6913 -0.5280 -0.5158 15  SER I OG  
17490 N N   . GLU J 16  ? 3.6560 3.4481 2.3918 -0.6704 -0.5410 -0.4438 16  GLU I N   
17491 C CA  . GLU J 16  ? 3.7119 3.4284 2.4111 -0.6564 -0.5799 -0.4434 16  GLU I CA  
17492 C C   . GLU J 16  ? 3.6590 3.3464 2.3703 -0.6328 -0.5618 -0.4346 16  GLU I C   
17493 O O   . GLU J 16  ? 3.5919 3.3212 2.3303 -0.6240 -0.5203 -0.4353 16  GLU I O   
17494 C CB  . GLU J 16  ? 3.7144 3.3820 2.4504 -0.6932 -0.6141 -0.4016 16  GLU I CB  
17495 C CG  . GLU J 16  ? 3.8137 3.4195 2.4954 -0.6846 -0.6642 -0.4137 16  GLU I CG  
17496 C CD  . GLU J 16  ? 3.8096 3.3693 2.5343 -0.7223 -0.6952 -0.3699 16  GLU I CD  
17497 O OE1 . GLU J 16  ? 3.7304 3.3073 2.5266 -0.7547 -0.6769 -0.3305 16  GLU I OE1 
17498 O OE2 . GLU J 16  ? 3.8892 3.3961 2.5767 -0.7195 -0.7379 -0.3752 16  GLU I OE2 
17499 N N   . THR J 17  ? 3.8344 3.4498 2.5257 -0.6224 -0.5932 -0.4262 17  THR I N   
17500 C CA  . THR J 17  ? 3.8405 3.4204 2.5395 -0.5994 -0.5809 -0.4168 17  THR I CA  
17501 C C   . THR J 17  ? 3.7750 3.2941 2.5348 -0.6261 -0.5952 -0.3619 17  THR I C   
17502 O O   . THR J 17  ? 3.7916 3.2527 2.5369 -0.6346 -0.6364 -0.3513 17  THR I O   
17503 C CB  . THR J 17  ? 3.9521 3.5013 2.5701 -0.5577 -0.6016 -0.4588 17  THR I CB  
17504 O OG1 . THR J 17  ? 3.9338 3.4388 2.5624 -0.5385 -0.5947 -0.4439 17  THR I OG1 
17505 C CG2 . THR J 17  ? 3.9987 3.5023 2.5715 -0.5626 -0.6525 -0.4686 17  THR I CG2 
17506 N N   . LEU J 18  ? 3.7257 3.2588 2.5540 -0.6394 -0.5613 -0.3274 18  LEU I N   
17507 C CA  . LEU J 18  ? 3.5958 3.0751 2.4870 -0.6639 -0.5695 -0.2740 18  LEU I CA  
17508 C C   . LEU J 18  ? 3.6661 3.0831 2.5359 -0.6364 -0.5809 -0.2722 18  LEU I C   
17509 O O   . LEU J 18  ? 3.7441 3.1761 2.5889 -0.6031 -0.5571 -0.2953 18  LEU I O   
17510 C CB  . LEU J 18  ? 3.4109 2.9292 2.3820 -0.6863 -0.5276 -0.2392 18  LEU I CB  
17511 C CG  . LEU J 18  ? 3.3113 2.7778 2.3485 -0.7047 -0.5271 -0.1859 18  LEU I CG  
17512 C CD1 . LEU J 18  ? 3.3020 2.7177 2.3639 -0.7385 -0.5665 -0.1523 18  LEU I CD1 
17513 C CD2 . LEU J 18  ? 3.2135 2.7257 2.3233 -0.7215 -0.4817 -0.1583 18  LEU I CD2 
17514 N N   . SER J 19  ? 3.3236 2.6707 2.2037 -0.6501 -0.6172 -0.2446 19  SER I N   
17515 C CA  . SER J 19  ? 3.4462 2.7279 2.3107 -0.6275 -0.6313 -0.2380 19  SER I CA  
17516 C C   . SER J 19  ? 3.4006 2.6349 2.3393 -0.6561 -0.6343 -0.1803 19  SER I C   
17517 O O   . SER J 19  ? 3.3961 2.6073 2.3655 -0.6897 -0.6592 -0.1526 19  SER I O   
17518 C CB  . SER J 19  ? 3.6129 2.8476 2.4067 -0.6105 -0.6776 -0.2662 19  SER I CB  
17519 O OG  . SER J 19  ? 3.7894 2.9636 2.5656 -0.5859 -0.6893 -0.2627 19  SER I OG  
17520 N N   . LEU J 20  ? 3.5023 2.7229 2.4694 -0.6426 -0.6090 -0.1624 20  LEU I N   
17521 C CA  . LEU J 20  ? 3.4863 2.6634 2.5243 -0.6661 -0.6071 -0.1082 20  LEU I CA  
17522 C C   . LEU J 20  ? 3.6338 2.7459 2.6510 -0.6392 -0.6199 -0.1046 20  LEU I C   
17523 O O   . LEU J 20  ? 3.7399 2.8527 2.6961 -0.6007 -0.6184 -0.1427 20  LEU I O   
17524 C CB  . LEU J 20  ? 3.2938 2.5199 2.3990 -0.6796 -0.5593 -0.0832 20  LEU I CB  
17525 C CG  . LEU J 20  ? 3.2175 2.5090 2.3537 -0.7084 -0.5424 -0.0814 20  LEU I CG  
17526 C CD1 . LEU J 20  ? 3.1510 2.4882 2.3498 -0.7165 -0.4941 -0.0595 20  LEU I CD1 
17527 C CD2 . LEU J 20  ? 3.2298 2.4926 2.4009 -0.7493 -0.5740 -0.0489 20  LEU I CD2 
17528 N N   . THR J 21  ? 3.6024 2.6577 2.6712 -0.6600 -0.6328 -0.0579 21  THR I N   
17529 C CA  . THR J 21  ? 3.7284 2.7163 2.7859 -0.6391 -0.6468 -0.0476 21  THR I CA  
17530 C C   . THR J 21  ? 3.6855 2.6462 2.8229 -0.6601 -0.6301 0.0071  21  THR I C   
17531 O O   . THR J 21  ? 3.6280 2.5841 2.8235 -0.6989 -0.6357 0.0441  21  THR I O   
17532 C CB  . THR J 21  ? 3.9033 2.8289 2.9208 -0.6398 -0.6993 -0.0542 21  THR I CB  
17533 O OG1 . THR J 21  ? 3.9690 2.9218 2.9122 -0.6208 -0.7149 -0.1055 21  THR I OG1 
17534 C CG2 . THR J 21  ? 4.0794 2.9375 3.0816 -0.6153 -0.7126 -0.0468 21  THR I CG2 
17535 N N   . CYS J 22  ? 3.9004 2.8454 3.0412 -0.6346 -0.6083 0.0121  22  CYS I N   
17536 C CA  . CYS J 22  ? 3.8203 2.7379 3.0327 -0.6490 -0.5899 0.0620  22  CYS I CA  
17537 C C   . CYS J 22  ? 3.9087 2.7450 3.1110 -0.6363 -0.6172 0.0778  22  CYS I C   
17538 O O   . CYS J 22  ? 3.9832 2.8016 3.1464 -0.6000 -0.6118 0.0590  22  CYS I O   
17539 C CB  . CYS J 22  ? 3.6981 2.6663 2.9262 -0.6302 -0.5400 0.0567  22  CYS I CB  
17540 S SG  . CYS J 22  ? 3.5948 2.5341 2.9058 -0.6430 -0.5136 0.1139  22  CYS I SG  
17541 N N   . ASN J 23  ? 3.7614 2.5484 2.9945 -0.6650 -0.6485 0.1096  23  ASN I N   
17542 C CA  . ASN J 23  ? 3.8299 2.5377 3.0576 -0.6556 -0.6760 0.1269  23  ASN I CA  
17543 C C   . ASN J 23  ? 3.7196 2.4069 3.0035 -0.6541 -0.6475 0.1661  23  ASN I C   
17544 O O   . ASN J 23  ? 3.6456 2.3420 3.0025 -0.6847 -0.6293 0.2074  23  ASN I O   
17545 C CB  . ASN J 23  ? 3.8807 2.5534 3.1195 -0.6876 -0.7183 0.1424  23  ASN I CB  
17546 C CG  . ASN J 23  ? 4.1954 2.8077 3.3765 -0.6702 -0.7634 0.1225  23  ASN I CG  
17547 O OD1 . ASN J 23  ? 4.2627 2.8366 3.4129 -0.6394 -0.7673 0.1133  23  ASN I OD1 
17548 N ND2 . ASN J 23  ? 4.5161 3.1230 3.6774 -0.6877 -0.7977 0.1118  23  ASN I ND2 
17549 N N   . VAL J 24  ? 3.8171 2.4788 3.0650 -0.6172 -0.6426 0.1515  24  VAL I N   
17550 C CA  . VAL J 24  ? 3.7317 2.3772 3.0209 -0.6083 -0.6138 0.1815  24  VAL I CA  
17551 C C   . VAL J 24  ? 3.7797 2.3400 3.0792 -0.6083 -0.6435 0.2099  24  VAL I C   
17552 O O   . VAL J 24  ? 3.9211 2.4389 3.1646 -0.5888 -0.6772 0.1868  24  VAL I O   
17553 C CB  . VAL J 24  ? 3.7629 2.4448 3.0052 -0.5650 -0.5832 0.1446  24  VAL I CB  
17554 C CG1 . VAL J 24  ? 3.6781 2.3455 2.9605 -0.5543 -0.5529 0.1740  24  VAL I CG1 
17555 C CG2 . VAL J 24  ? 3.7103 2.4765 2.9388 -0.5646 -0.5562 0.1132  24  VAL I CG2 
17556 N N   . SER J 25  ? 3.6858 2.2225 3.0579 -0.6308 -0.6310 0.2599  25  SER I N   
17557 C CA  . SER J 25  ? 3.8232 2.2816 3.2179 -0.6334 -0.6529 0.2937  25  SER I CA  
17558 C C   . SER J 25  ? 3.7803 2.2397 3.2259 -0.6282 -0.6143 0.3260  25  SER I C   
17559 O O   . SER J 25  ? 3.6799 2.1841 3.1801 -0.6490 -0.5822 0.3472  25  SER I O   
17560 C CB  . SER J 25  ? 3.8785 2.2996 3.3196 -0.6759 -0.6849 0.3289  25  SER I CB  
17561 O OG  . SER J 25  ? 3.9697 2.3916 3.3645 -0.6814 -0.7206 0.2994  25  SER I OG  
17562 N N   . GLY J 26  ? 3.7466 2.1572 3.1747 -0.6007 -0.6171 0.3298  26  GLY I N   
17563 C CA  . GLY J 26  ? 3.7067 2.1131 3.1797 -0.5934 -0.5823 0.3604  26  GLY I CA  
17564 C C   . GLY J 26  ? 3.7125 2.1453 3.1406 -0.5490 -0.5531 0.3296  26  GLY I C   
17565 O O   . GLY J 26  ? 3.7293 2.1478 3.1864 -0.5376 -0.5287 0.3535  26  GLY I O   
17566 N N   . THR J 27  ? 3.7140 2.1859 3.0734 -0.5238 -0.5540 0.2778  27  THR I N   
17567 C CA  . THR J 27  ? 3.7314 2.2307 3.0452 -0.4806 -0.5268 0.2458  27  THR I CA  
17568 C C   . THR J 27  ? 3.7766 2.2898 3.0049 -0.4539 -0.5479 0.1895  27  THR I C   
17569 O O   . THR J 27  ? 3.8015 2.3194 3.0110 -0.4712 -0.5757 0.1744  27  THR I O   
17570 C CB  . THR J 27  ? 3.6264 2.1989 2.9748 -0.4827 -0.4770 0.2478  27  THR I CB  
17571 O OG1 . THR J 27  ? 3.6493 2.2484 2.9512 -0.4394 -0.4514 0.2151  27  THR I OG1 
17572 C CG2 . THR J 27  ? 3.5726 2.2068 2.9233 -0.5058 -0.4739 0.2297  27  THR I CG2 
17573 N N   . LEU J 28  ? 3.7360 2.2558 2.9125 -0.4113 -0.5342 0.1588  28  LEU I N   
17574 C CA  . LEU J 28  ? 3.8692 2.4035 2.9617 -0.3810 -0.5504 0.1035  28  LEU I CA  
17575 C C   . LEU J 28  ? 3.8144 2.4345 2.8900 -0.3756 -0.5203 0.0694  28  LEU I C   
17576 O O   . LEU J 28  ? 3.6886 2.3547 2.8036 -0.3781 -0.4794 0.0816  28  LEU I O   
17577 C CB  . LEU J 28  ? 3.9831 2.4819 3.0258 -0.3367 -0.5517 0.0856  28  LEU I CB  
17578 C CG  . LEU J 28  ? 4.0730 2.4844 3.1215 -0.3363 -0.5841 0.1130  28  LEU I CG  
17579 C CD1 . LEU J 28  ? 4.2026 2.5861 3.1974 -0.2900 -0.5827 0.0910  28  LEU I CD1 
17580 C CD2 . LEU J 28  ? 4.1604 2.5357 3.1900 -0.3563 -0.6323 0.1071  28  LEU I CD2 
17581 N N   . VAL J 29  ? 3.9541 2.5957 2.9699 -0.3675 -0.5409 0.0255  29  VAL I N   
17582 C CA  . VAL J 29  ? 3.8993 2.6221 2.8975 -0.3642 -0.5153 -0.0084 29  VAL I CA  
17583 C C   . VAL J 29  ? 3.9248 2.6815 2.8750 -0.3195 -0.4872 -0.0455 29  VAL I C   
17584 O O   . VAL J 29  ? 3.8434 2.6704 2.7846 -0.3133 -0.4584 -0.0715 29  VAL I O   
17585 C CB  . VAL J 29  ? 4.0064 2.7380 2.9606 -0.3743 -0.5494 -0.0396 29  VAL I CB  
17586 C CG1 . VAL J 29  ? 3.9235 2.7380 2.8753 -0.3827 -0.5254 -0.0651 29  VAL I CG1 
17587 C CG2 . VAL J 29  ? 4.0315 2.7096 3.0215 -0.4121 -0.5872 -0.0044 29  VAL I CG2 
17588 N N   . ARG J 30  ? 3.8301 2.5389 2.7521 -0.2887 -0.4935 -0.0472 30  ARG I N   
17589 C CA  . ARG J 30  ? 3.8629 2.5977 2.7366 -0.2443 -0.4693 -0.0819 30  ARG I CA  
17590 C C   . ARG J 30  ? 3.7257 2.4791 2.6488 -0.2385 -0.4257 -0.0546 30  ARG I C   
17591 O O   . ARG J 30  ? 3.6867 2.4885 2.5855 -0.2100 -0.3940 -0.0822 30  ARG I O   
17592 C CB  . ARG J 30  ? 4.0323 2.7082 2.8425 -0.2112 -0.5000 -0.1030 30  ARG I CB  
17593 C CG  . ARG J 30  ? 4.0906 2.7919 2.8443 -0.1636 -0.4784 -0.1425 30  ARG I CG  
17594 C CD  . ARG J 30  ? 4.3006 2.9545 2.9820 -0.1348 -0.5145 -0.1734 30  ARG I CD  
17595 N NE  . ARG J 30  ? 4.4013 2.9740 3.1040 -0.1429 -0.5421 -0.1369 30  ARG I NE  
17596 C CZ  . ARG J 30  ? 4.5828 3.0993 3.2358 -0.1244 -0.5784 -0.1523 30  ARG I CZ  
17597 N NH1 . ARG J 30  ? 4.6802 3.2131 3.2581 -0.0965 -0.5917 -0.2041 30  ARG I NH1 
17598 N NH2 . ARG J 30  ? 4.6662 3.1101 3.3452 -0.1339 -0.6014 -0.1161 30  ARG I NH2 
17599 N N   . ASP J 31  ? 3.8282 2.5463 2.8209 -0.2655 -0.4229 -0.0014 31  ASP I N   
17600 C CA  . ASP J 31  ? 3.7648 2.4928 2.8074 -0.2612 -0.3841 0.0289  31  ASP I CA  
17601 C C   . ASP J 31  ? 3.6421 2.4328 2.7472 -0.2903 -0.3496 0.0472  31  ASP I C   
17602 O O   . ASP J 31  ? 3.6114 2.4059 2.7718 -0.2963 -0.3202 0.0813  31  ASP I O   
17603 C CB  . ASP J 31  ? 3.8130 2.4656 2.9000 -0.2746 -0.3994 0.0791  31  ASP I CB  
17604 C CG  . ASP J 31  ? 3.9402 2.5331 2.9774 -0.2388 -0.4186 0.0686  31  ASP I CG  
17605 O OD1 . ASP J 31  ? 4.0110 2.6027 2.9759 -0.2129 -0.4387 0.0243  31  ASP I OD1 
17606 O OD2 . ASP J 31  ? 3.9729 2.5213 3.0440 -0.2362 -0.4127 0.1048  31  ASP I OD2 
17607 N N   . ASN J 32  ? 3.6307 2.4695 2.7300 -0.3090 -0.3526 0.0266  32  ASN I N   
17608 C CA  . ASN J 32  ? 3.5463 2.4440 2.7063 -0.3367 -0.3198 0.0446  32  ASN I CA  
17609 C C   . ASN J 32  ? 3.5155 2.4851 2.6392 -0.3319 -0.3096 -0.0008 32  ASN I C   
17610 O O   . ASN J 32  ? 3.5496 2.5175 2.6079 -0.3163 -0.3348 -0.0406 32  ASN I O   
17611 C CB  . ASN J 32  ? 3.5367 2.4077 2.7646 -0.3852 -0.3358 0.0921  32  ASN I CB  
17612 C CG  . ASN J 32  ? 3.5576 2.3641 2.8324 -0.3931 -0.3399 0.1412  32  ASN I CG  
17613 O OD1 . ASN J 32  ? 3.6142 2.3535 2.8710 -0.3913 -0.3754 0.1502  32  ASN I OD1 
17614 N ND2 . ASN J 32  ? 3.5120 2.3388 2.8480 -0.4019 -0.3034 0.1732  32  ASN I ND2 
17615 N N   . TYR J 33  ? 3.5537 2.5867 2.7219 -0.3459 -0.2723 0.0058  33  TYR I N   
17616 C CA  . TYR J 33  ? 3.5333 2.6376 2.6811 -0.3488 -0.2604 -0.0304 33  TYR I CA  
17617 C C   . TYR J 33  ? 3.5495 2.6546 2.7382 -0.3950 -0.2794 -0.0074 33  TYR I C   
17618 O O   . TYR J 33  ? 3.5496 2.6214 2.8010 -0.4257 -0.2839 0.0407  33  TYR I O   
17619 C CB  . TYR J 33  ? 3.4699 2.6436 2.6429 -0.3382 -0.2099 -0.0374 33  TYR I CB  
17620 C CG  . TYR J 33  ? 3.4485 2.6338 2.5690 -0.2895 -0.1913 -0.0714 33  TYR I CG  
17621 C CD1 . TYR J 33  ? 3.4309 2.5723 2.5588 -0.2694 -0.1843 -0.0504 33  TYR I CD1 
17622 C CD2 . TYR J 33  ? 3.4403 2.6822 2.5056 -0.2638 -0.1794 -0.1240 33  TYR I CD2 
17623 C CE1 . TYR J 33  ? 3.4048 2.5574 2.4851 -0.2247 -0.1671 -0.0811 33  TYR I CE1 
17624 C CE2 . TYR J 33  ? 3.4169 2.6704 2.4349 -0.2193 -0.1622 -0.1552 33  TYR I CE2 
17625 C CZ  . TYR J 33  ? 3.3971 2.6059 2.4225 -0.1998 -0.1562 -0.1336 33  TYR I CZ  
17626 O OH  . TYR J 33  ? 3.3701 2.5906 2.3481 -0.1552 -0.1393 -0.1644 33  TYR I OH  
17627 N N   . TRP J 34  ? 3.4710 2.6143 2.6247 -0.4000 -0.2906 -0.0415 34  TRP I N   
17628 C CA  . TRP J 34  ? 3.4684 2.6130 2.6539 -0.4422 -0.3112 -0.0233 34  TRP I CA  
17629 C C   . TRP J 34  ? 3.3859 2.6114 2.5761 -0.4532 -0.2882 -0.0468 34  TRP I C   
17630 O O   . TRP J 34  ? 3.3944 2.6597 2.5261 -0.4267 -0.2828 -0.0948 34  TRP I O   
17631 C CB  . TRP J 34  ? 3.5872 2.6795 2.7208 -0.4413 -0.3614 -0.0382 34  TRP I CB  
17632 C CG  . TRP J 34  ? 3.6512 2.6627 2.7820 -0.4314 -0.3849 -0.0145 34  TRP I CG  
17633 C CD1 . TRP J 34  ? 3.7000 2.6784 2.7727 -0.3918 -0.3948 -0.0389 34  TRP I CD1 
17634 C CD2 . TRP J 34  ? 3.6559 2.6101 2.8451 -0.4611 -0.4010 0.0379  34  TRP I CD2 
17635 N NE1 . TRP J 34  ? 3.7583 2.6623 2.8495 -0.3949 -0.4156 -0.0048 34  TRP I NE1 
17636 C CE2 . TRP J 34  ? 3.7283 2.6160 2.8908 -0.4372 -0.4200 0.0425  34  TRP I CE2 
17637 C CE3 . TRP J 34  ? 3.6062 2.5586 2.8677 -0.5055 -0.4013 0.0813  34  TRP I CE3 
17638 C CZ2 . TRP J 34  ? 3.7669 2.5873 2.9731 -0.4563 -0.4388 0.0887  34  TRP I CZ2 
17639 C CZ3 . TRP J 34  ? 3.6669 2.5525 2.9711 -0.5243 -0.4203 0.1268  34  TRP I CZ3 
17640 C CH2 . TRP J 34  ? 3.7509 2.5714 3.0276 -0.4998 -0.4386 0.1302  34  TRP I CH2 
17641 N N   . SER J 35  ? 3.3600 2.6099 2.6201 -0.4920 -0.2745 -0.0129 35  SER I N   
17642 C CA  . SER J 35  ? 3.2908 2.6172 2.5642 -0.5060 -0.2512 -0.0300 35  SER I CA  
17643 C C   . SER J 35  ? 3.3057 2.6308 2.6081 -0.5485 -0.2748 -0.0114 35  SER I C   
17644 O O   . SER J 35  ? 3.3461 2.6184 2.6868 -0.5752 -0.2976 0.0289  35  SER I O   
17645 C CB  . SER J 35  ? 3.1622 2.5352 2.4973 -0.5113 -0.2029 -0.0094 35  SER I CB  
17646 O OG  . SER J 35  ? 3.1949 2.5711 2.5056 -0.4722 -0.1797 -0.0255 35  SER I OG  
17647 N N   . TRP J 36  ? 3.2561 2.6411 2.5401 -0.5543 -0.2684 -0.0413 36  TRP I N   
17648 C CA  . TRP J 36  ? 3.1525 2.5510 2.4608 -0.5929 -0.2856 -0.0297 36  TRP I CA  
17649 C C   . TRP J 36  ? 3.0531 2.5242 2.4154 -0.6129 -0.2457 -0.0216 36  TRP I C   
17650 O O   . TRP J 36  ? 3.0245 2.5531 2.3688 -0.5905 -0.2138 -0.0527 36  TRP I O   
17651 C CB  . TRP J 36  ? 3.2103 2.6134 2.4469 -0.5840 -0.3174 -0.0723 36  TRP I CB  
17652 C CG  . TRP J 36  ? 3.3550 2.6826 2.5504 -0.5779 -0.3648 -0.0721 36  TRP I CG  
17653 C CD1 . TRP J 36  ? 3.4455 2.7323 2.5833 -0.5413 -0.3796 -0.0945 36  TRP I CD1 
17654 C CD2 . TRP J 36  ? 3.4230 2.7083 2.6324 -0.6098 -0.4038 -0.0487 36  TRP I CD2 
17655 N NE1 . TRP J 36  ? 3.5413 2.7627 2.6576 -0.5488 -0.4253 -0.0862 36  TRP I NE1 
17656 C CE2 . TRP J 36  ? 3.5389 2.7584 2.6981 -0.5905 -0.4409 -0.0585 36  TRP I CE2 
17657 C CE3 . TRP J 36  ? 3.3475 2.6446 2.6072 -0.6527 -0.4109 -0.0206 36  TRP I CE3 
17658 C CZ2 . TRP J 36  ? 3.6034 2.7692 2.7620 -0.6127 -0.4846 -0.0414 36  TRP I CZ2 
17659 C CZ3 . TRP J 36  ? 3.3794 2.6232 2.6376 -0.6745 -0.4543 -0.0035 36  TRP I CZ3 
17660 C CH2 . TRP J 36  ? 3.4999 2.6791 2.7081 -0.6545 -0.4906 -0.0142 36  TRP I CH2 
17661 N N   . ILE J 37  ? 2.9796 2.4472 2.4088 -0.6549 -0.2479 0.0202  37  ILE I N   
17662 C CA  . ILE J 37  ? 2.9103 2.4404 2.4007 -0.6798 -0.2126 0.0355  37  ILE I CA  
17663 C C   . ILE J 37  ? 2.9022 2.4443 2.4114 -0.7178 -0.2331 0.0455  37  ILE I C   
17664 O O   . ILE J 37  ? 2.9337 2.4224 2.4602 -0.7419 -0.2660 0.0749  37  ILE I O   
17665 C CB  . ILE J 37  ? 2.8791 2.3954 2.4458 -0.6938 -0.1871 0.0835  37  ILE I CB  
17666 C CG1 . ILE J 37  ? 2.8927 2.3931 2.4359 -0.6541 -0.1694 0.0728  37  ILE I CG1 
17667 C CG2 . ILE J 37  ? 2.8062 2.3896 2.4358 -0.7186 -0.1497 0.0975  37  ILE I CG2 
17668 C CD1 . ILE J 37  ? 2.9542 2.3700 2.4820 -0.6441 -0.2000 0.0920  37  ILE I CD1 
17669 N N   . ARG J 38  ? 3.1390 2.7511 2.6440 -0.7225 -0.2139 0.0206  38  ARG I N   
17670 C CA  . ARG J 38  ? 3.0572 2.6924 2.5795 -0.7570 -0.2277 0.0266  38  ARG I CA  
17671 C C   . ARG J 38  ? 2.9254 2.6106 2.5270 -0.7879 -0.1929 0.0561  38  ARG I C   
17672 O O   . ARG J 38  ? 2.8735 2.5965 2.5019 -0.7763 -0.1530 0.0559  38  ARG I O   
17673 C CB  . ARG J 38  ? 3.0565 2.7389 2.5110 -0.7379 -0.2308 -0.0276 38  ARG I CB  
17674 C CG  . ARG J 38  ? 2.9351 2.6344 2.3822 -0.7646 -0.2538 -0.0330 38  ARG I CG  
17675 C CD  . ARG J 38  ? 3.0016 2.7452 2.3751 -0.7376 -0.2539 -0.0904 38  ARG I CD  
17676 N NE  . ARG J 38  ? 2.9150 2.7393 2.3111 -0.7391 -0.2123 -0.1053 38  ARG I NE  
17677 C CZ  . ARG J 38  ? 2.9729 2.8504 2.3194 -0.7204 -0.2033 -0.1521 38  ARG I CZ  
17678 N NH1 . ARG J 38  ? 3.1026 2.9622 2.3721 -0.6982 -0.2329 -0.1897 38  ARG I NH1 
17679 N NH2 . ARG J 38  ? 2.8645 2.8136 2.2391 -0.7237 -0.1643 -0.1616 38  ARG I NH2 
17680 N N   . GLN J 39  ? 3.0558 2.7403 2.6957 -0.8276 -0.2086 0.0823  39  GLN I N   
17681 C CA  . GLN J 39  ? 2.9430 2.6724 2.6606 -0.8597 -0.1780 0.1126  39  GLN I CA  
17682 C C   . GLN J 39  ? 2.8729 2.6261 2.6080 -0.8952 -0.1928 0.1196  39  GLN I C   
17683 O O   . GLN J 39  ? 2.8638 2.5696 2.6151 -0.9212 -0.2259 0.1480  39  GLN I O   
17684 C CB  . GLN J 39  ? 2.9493 2.6367 2.7382 -0.8796 -0.1720 0.1666  39  GLN I CB  
17685 C CG  . GLN J 39  ? 2.8454 2.5803 2.7162 -0.9119 -0.1387 0.1979  39  GLN I CG  
17686 C CD  . GLN J 39  ? 2.8629 2.5574 2.8064 -0.9334 -0.1328 0.2521  39  GLN I CD  
17687 O OE1 . GLN J 39  ? 2.9978 2.6252 2.9334 -0.9275 -0.1564 0.2696  39  GLN I OE1 
17688 N NE2 . GLN J 39  ? 2.7316 2.4669 2.7474 -0.9589 -0.1012 0.2793  39  GLN I NE2 
17689 N N   . PRO J 40  ? 2.9994 2.8238 2.7311 -0.8973 -0.1701 0.0947  40  PRO I N   
17690 C CA  . PRO J 40  ? 2.9248 2.7744 2.6794 -0.9328 -0.1812 0.1047  40  PRO I CA  
17691 C C   . PRO J 40  ? 2.8566 2.7001 2.7022 -0.9733 -0.1705 0.1600  40  PRO I C   
17692 O O   . PRO J 40  ? 2.8552 2.6910 2.7491 -0.9733 -0.1463 0.1865  40  PRO I O   
17693 C CB  . PRO J 40  ? 2.8754 2.8061 2.6093 -0.9210 -0.1519 0.0649  40  PRO I CB  
17694 C CG  . PRO J 40  ? 2.9484 2.8820 2.6191 -0.8741 -0.1426 0.0228  40  PRO I CG  
17695 C CD  . PRO J 40  ? 2.9978 2.8802 2.6922 -0.8639 -0.1387 0.0500  40  PRO I CD  
17696 N N   . LEU J 41  ? 2.9447 2.7927 2.8136 -1.0082 -0.1887 0.1774  41  LEU I N   
17697 C CA  . LEU J 41  ? 2.8991 2.7402 2.8531 -1.0492 -0.1825 0.2300  41  LEU I CA  
17698 C C   . LEU J 41  ? 2.7876 2.6974 2.7985 -1.0582 -0.1337 0.2369  41  LEU I C   
17699 O O   . LEU J 41  ? 2.7582 2.7294 2.7646 -1.0637 -0.1187 0.2156  41  LEU I O   
17700 C CB  . LEU J 41  ? 2.8618 2.6904 2.8214 -1.0827 -0.2161 0.2443  41  LEU I CB  
17701 C CG  . LEU J 41  ? 2.8941 2.6525 2.8034 -1.0774 -0.2663 0.2410  41  LEU I CG  
17702 C CD1 . LEU J 41  ? 2.8707 2.6469 2.6984 -1.0576 -0.2869 0.1915  41  LEU I CD1 
17703 C CD2 . LEU J 41  ? 2.8605 2.5779 2.8200 -1.1186 -0.2936 0.2874  41  LEU I CD2 
17704 N N   . GLY J 42  ? 2.7004 2.6000 2.7653 -1.0596 -0.1088 0.2667  42  GLY I N   
17705 C CA  . GLY J 42  ? 2.6232 2.5832 2.7479 -1.0693 -0.0627 0.2773  42  GLY I CA  
17706 C C   . GLY J 42  ? 2.6332 2.6418 2.7272 -1.0322 -0.0277 0.2378  42  GLY I C   
17707 O O   . GLY J 42  ? 2.5760 2.6494 2.7049 -1.0380 0.0089  0.2332  42  GLY I O   
17708 N N   . LYS J 43  ? 2.6216 2.6012 2.6521 -0.9943 -0.0380 0.2090  43  LYS I N   
17709 C CA  . LYS J 43  ? 2.6341 2.6538 2.6287 -0.9555 -0.0079 0.1696  43  LYS I CA  
17710 C C   . LYS J 43  ? 2.7147 2.6859 2.7011 -0.9295 -0.0059 0.1778  43  LYS I C   
17711 O O   . LYS J 43  ? 2.7718 2.6769 2.7724 -0.9399 -0.0310 0.2100  43  LYS I O   
17712 C CB  . LYS J 43  ? 2.6587 2.7011 2.5697 -0.9301 -0.0223 0.1153  43  LYS I CB  
17713 C CG  . LYS J 43  ? 2.5834 2.6815 2.5008 -0.9525 -0.0193 0.1036  43  LYS I CG  
17714 C CD  . LYS J 43  ? 2.4975 2.6688 2.4679 -0.9595 0.0287  0.1046  43  LYS I CD  
17715 C CE  . LYS J 43  ? 2.5185 2.7281 2.4509 -0.9180 0.0585  0.0630  43  LYS I CE  
17716 N NZ  . LYS J 43  ? 2.4350 2.7171 2.4188 -0.9243 0.1053  0.0624  43  LYS I NZ  
17717 N N   . GLN J 44  ? 2.8444 2.8496 2.8087 -0.8956 0.0247  0.1485  44  GLN I N   
17718 C CA  . GLN J 44  ? 2.9043 2.8686 2.8589 -0.8683 0.0297  0.1538  44  GLN I CA  
17719 C C   . GLN J 44  ? 3.0236 2.9405 2.8939 -0.8365 -0.0042 0.1228  44  GLN I C   
17720 O O   . GLN J 44  ? 3.0358 2.9738 2.8450 -0.8222 -0.0173 0.0816  44  GLN I O   
17721 C CB  . GLN J 44  ? 2.8073 2.8260 2.7751 -0.8445 0.0768  0.1369  44  GLN I CB  
17722 C CG  . GLN J 44  ? 2.7574 2.8349 2.6667 -0.8147 0.0918  0.0805  44  GLN I CG  
17723 C CD  . GLN J 44  ? 2.7098 2.8569 2.6463 -0.8376 0.1099  0.0720  44  GLN I CD  
17724 O OE1 . GLN J 44  ? 2.6963 2.8411 2.6790 -0.8763 0.0999  0.1030  44  GLN I OE1 
17725 N NE2 . GLN J 44  ? 2.6499 2.8599 2.5590 -0.8138 0.1374  0.0302  44  GLN I NE2 
17726 N N   . PRO J 45  ? 2.8738 2.7256 2.7411 -0.8256 -0.0189 0.1430  45  PRO I N   
17727 C CA  . PRO J 45  ? 2.9488 2.7496 2.7398 -0.7961 -0.0523 0.1171  45  PRO I CA  
17728 C C   . PRO J 45  ? 2.9844 2.8227 2.7063 -0.7531 -0.0381 0.0619  45  PRO I C   
17729 O O   . PRO J 45  ? 2.9646 2.8441 2.6982 -0.7340 -0.0001 0.0507  45  PRO I O   
17730 C CB  . PRO J 45  ? 3.0490 2.7857 2.8649 -0.7914 -0.0569 0.1524  45  PRO I CB  
17731 C CG  . PRO J 45  ? 3.0048 2.7426 2.9098 -0.8311 -0.0433 0.2039  45  PRO I CG  
17732 C CD  . PRO J 45  ? 2.8689 2.6885 2.8058 -0.8421 -0.0069 0.1930  45  PRO I CD  
17733 N N   . GLU J 46  ? 2.8878 2.7113 2.5372 -0.7376 -0.0696 0.0268  46  GLU I N   
17734 C CA  . GLU J 46  ? 2.9621 2.8167 2.5391 -0.6968 -0.0617 -0.0280 46  GLU I CA  
17735 C C   . GLU J 46  ? 3.0511 2.8426 2.5676 -0.6649 -0.0891 -0.0418 46  GLU I C   
17736 O O   . GLU J 46  ? 3.0885 2.8266 2.5781 -0.6726 -0.1303 -0.0366 46  GLU I O   
17737 C CB  . GLU J 46  ? 2.9802 2.8767 2.5197 -0.7033 -0.0734 -0.0618 46  GLU I CB  
17738 C CG  . GLU J 46  ? 3.0503 2.9858 2.5159 -0.6638 -0.0652 -0.1204 46  GLU I CG  
17739 C CD  . GLU J 46  ? 3.0698 3.0479 2.5051 -0.6739 -0.0757 -0.1498 46  GLU I CD  
17740 O OE1 . GLU J 46  ? 3.0073 3.0001 2.4898 -0.7119 -0.0783 -0.1241 46  GLU I OE1 
17741 O OE2 . GLU J 46  ? 3.1500 3.1477 2.5156 -0.6442 -0.0807 -0.1981 46  GLU I OE2 
17742 N N   . TRP J 47  ? 2.8373 2.6360 2.3334 -0.6291 -0.0656 -0.0595 47  TRP I N   
17743 C CA  . TRP J 47  ? 2.9275 2.6721 2.3665 -0.5945 -0.0856 -0.0748 47  TRP I CA  
17744 C C   . TRP J 47  ? 3.0189 2.7683 2.3721 -0.5704 -0.1102 -0.1260 47  TRP I C   
17745 O O   . TRP J 47  ? 3.0349 2.8455 2.3588 -0.5547 -0.0907 -0.1656 47  TRP I O   
17746 C CB  . TRP J 47  ? 2.9398 2.6989 2.3826 -0.5630 -0.0501 -0.0809 47  TRP I CB  
17747 C CG  . TRP J 47  ? 3.0167 2.7100 2.4214 -0.5340 -0.0687 -0.0805 47  TRP I CG  
17748 C CD1 . TRP J 47  ? 3.0659 2.6884 2.4429 -0.5365 -0.1117 -0.0706 47  TRP I CD1 
17749 C CD2 . TRP J 47  ? 3.0577 2.7512 2.4468 -0.4974 -0.0447 -0.0916 47  TRP I CD2 
17750 N NE1 . TRP J 47  ? 3.1365 2.7144 2.4833 -0.5044 -0.1155 -0.0738 47  TRP I NE1 
17751 C CE2 . TRP J 47  ? 3.1319 2.7522 2.4848 -0.4798 -0.0748 -0.0866 47  TRP I CE2 
17752 C CE3 . TRP J 47  ? 3.0396 2.7881 2.4424 -0.4778 -0.0006 -0.1052 47  TRP I CE3 
17753 C CZ2 . TRP J 47  ? 3.1874 2.7881 2.5173 -0.4434 -0.0621 -0.0941 47  TRP I CZ2 
17754 C CZ3 . TRP J 47  ? 3.0913 2.8206 2.4707 -0.4415 0.0117  -0.1131 47  TRP I CZ3 
17755 C CH2 . TRP J 47  ? 3.1633 2.8194 2.5065 -0.4247 -0.0188 -0.1072 47  TRP I CH2 
17756 N N   . ILE J 48  ? 2.9874 2.6731 2.3007 -0.5674 -0.1528 -0.1258 48  ILE I N   
17757 C CA  . ILE J 48  ? 3.0282 2.7149 2.2599 -0.5457 -0.1789 -0.1733 48  ILE I CA  
17758 C C   . ILE J 48  ? 3.0602 2.7347 2.2283 -0.4973 -0.1756 -0.2092 48  ILE I C   
17759 O O   . ILE J 48  ? 3.0603 2.7752 2.1723 -0.4714 -0.1695 -0.2570 48  ILE I O   
17760 C CB  . ILE J 48  ? 3.0798 2.7079 2.2972 -0.5669 -0.2280 -0.1589 48  ILE I CB  
17761 C CG1 . ILE J 48  ? 3.0479 2.6872 2.3305 -0.6151 -0.2310 -0.1216 48  ILE I CG1 
17762 C CG2 . ILE J 48  ? 3.1187 2.7523 2.2546 -0.5472 -0.2544 -0.2078 48  ILE I CG2 
17763 C CD1 . ILE J 48  ? 3.0972 2.6786 2.3705 -0.6377 -0.2789 -0.1048 48  ILE I CD1 
17764 N N   . GLY J 49  ? 3.0793 2.7000 2.2548 -0.4840 -0.1788 -0.1874 49  GLY I N   
17765 C CA  . GLY J 49  ? 3.1108 2.7167 2.2286 -0.4385 -0.1760 -0.2182 49  GLY I CA  
17766 C C   . GLY J 49  ? 3.1592 2.6851 2.2804 -0.4326 -0.1978 -0.1888 49  GLY I C   
17767 O O   . GLY J 49  ? 3.1786 2.6560 2.3335 -0.4621 -0.2232 -0.1512 49  GLY I O   
17768 N N   . TYR J 50  ? 3.3697 2.8818 2.4558 -0.3936 -0.1875 -0.2061 50  TYR I N   
17769 C CA  . TYR J 50  ? 3.4178 2.8552 2.5032 -0.3833 -0.2058 -0.1810 50  TYR I CA  
17770 C C   . TYR J 50  ? 3.5060 2.9086 2.5067 -0.3473 -0.2347 -0.2200 50  TYR I C   
17771 O O   . TYR J 50  ? 3.5061 2.9491 2.4514 -0.3173 -0.2245 -0.2674 50  TYR I O   
17772 C CB  . TYR J 50  ? 3.3850 2.8287 2.5096 -0.3693 -0.1681 -0.1602 50  TYR I CB  
17773 C CG  . TYR J 50  ? 3.3857 2.8782 2.4697 -0.3280 -0.1367 -0.2020 50  TYR I CG  
17774 C CD1 . TYR J 50  ? 3.3229 2.8943 2.4249 -0.3298 -0.1000 -0.2197 50  TYR I CD1 
17775 C CD2 . TYR J 50  ? 3.4294 2.8884 2.4597 -0.2875 -0.1430 -0.2224 50  TYR I CD2 
17776 C CE1 . TYR J 50  ? 3.3053 2.9210 2.3717 -0.2921 -0.0714 -0.2577 50  TYR I CE1 
17777 C CE2 . TYR J 50  ? 3.4070 2.9098 2.4010 -0.2496 -0.1145 -0.2599 50  TYR I CE2 
17778 C CZ  . TYR J 50  ? 3.3436 2.9246 2.3557 -0.2521 -0.0789 -0.2776 50  TYR I CZ  
17779 O OH  . TYR J 50  ? 3.3200 2.9452 2.2966 -0.2144 -0.0507 -0.3155 50  TYR I OH  
17780 N N   . VAL J 51  ? 3.5375 2.8645 2.5293 -0.3504 -0.2708 -0.1996 51  VAL I N   
17781 C CA  . VAL J 51  ? 3.6316 2.9155 2.5473 -0.3190 -0.3025 -0.2313 51  VAL I CA  
17782 C C   . VAL J 51  ? 3.6611 2.8781 2.5820 -0.3027 -0.3094 -0.2060 51  VAL I C   
17783 O O   . VAL J 51  ? 3.6573 2.8367 2.6384 -0.3278 -0.3114 -0.1572 51  VAL I O   
17784 C CB  . VAL J 51  ? 3.6932 2.9494 2.5821 -0.3390 -0.3474 -0.2382 51  VAL I CB  
17785 C CG1 . VAL J 51  ? 3.6682 2.8758 2.6193 -0.3800 -0.3677 -0.1847 51  VAL I CG1 
17786 C CG2 . VAL J 51  ? 3.8120 3.0253 2.6208 -0.3058 -0.3805 -0.2731 51  VAL I CG2 
17787 N N   . HIS J 52  ? 3.6242 2.8270 2.4822 -0.2603 -0.3125 -0.2392 52  HIS I N   
17788 C CA  . HIS J 52  ? 3.6734 2.8143 2.5267 -0.2393 -0.3192 -0.2211 52  HIS I CA  
17789 C C   . HIS J 52  ? 3.7398 2.8524 2.5079 -0.2014 -0.3454 -0.2638 52  HIS I C   
17790 O O   . HIS J 52  ? 3.7365 2.8871 2.4502 -0.1865 -0.3497 -0.3098 52  HIS I O   
17791 C CB  . HIS J 52  ? 3.6222 2.7878 2.5084 -0.2228 -0.2750 -0.2080 52  HIS I CB  
17792 C CG  . HIS J 52  ? 3.6689 2.7697 2.5607 -0.2062 -0.2804 -0.1820 52  HIS I CG  
17793 N ND1 . HIS J 52  ? 3.7015 2.7877 2.5374 -0.1618 -0.2781 -0.2097 52  HIS I ND1 
17794 C CD2 . HIS J 52  ? 3.6939 2.7400 2.6400 -0.2278 -0.2887 -0.1309 52  HIS I CD2 
17795 C CE1 . HIS J 52  ? 3.7446 2.7702 2.6003 -0.1568 -0.2841 -0.1765 52  HIS I CE1 
17796 N NE2 . HIS J 52  ? 3.7413 2.7415 2.6639 -0.1963 -0.2906 -0.1284 52  HIS I NE2 
17797 N N   . ASP J 53  ? 3.9729 3.0174 2.7307 -0.1862 -0.3634 -0.2476 53  ASP I N   
17798 C CA  . ASP J 53  ? 4.1089 3.1205 2.7888 -0.1492 -0.3882 -0.2846 53  ASP I CA  
17799 C C   . ASP J 53  ? 4.1280 3.1864 2.7664 -0.1071 -0.3560 -0.3236 53  ASP I C   
17800 O O   . ASP J 53  ? 4.0407 3.1534 2.7125 -0.1069 -0.3154 -0.3200 53  ASP I O   
17801 C CB  . ASP J 53  ? 4.2033 3.1306 2.8892 -0.1448 -0.4131 -0.2538 53  ASP I CB  
17802 C CG  . ASP J 53  ? 4.3465 3.2274 2.9592 -0.1215 -0.4539 -0.2852 53  ASP I CG  
17803 O OD1 . ASP J 53  ? 4.4043 3.3175 2.9522 -0.0919 -0.4528 -0.3350 53  ASP I OD1 
17804 O OD2 . ASP J 53  ? 4.3886 3.2003 3.0090 -0.1323 -0.4869 -0.2601 53  ASP I OD2 
17805 N N   . SER J 54  ? 4.2746 3.3113 2.8394 -0.0707 -0.3748 -0.3615 54  SER I N   
17806 C CA  . SER J 54  ? 4.2655 3.3396 2.7808 -0.0271 -0.3501 -0.4028 54  SER I CA  
17807 C C   . SER J 54  ? 4.1978 3.3566 2.7009 -0.0262 -0.3248 -0.4389 54  SER I C   
17808 O O   . SER J 54  ? 4.1444 3.3482 2.6289 0.0028  -0.2928 -0.4643 54  SER I O   
17809 C CB  . SER J 54  ? 4.2618 3.3280 2.8096 -0.0102 -0.3180 -0.3776 54  SER I CB  
17810 O OG  . SER J 54  ? 4.3011 3.4081 2.8038 0.0310  -0.2922 -0.4173 54  SER I OG  
17811 N N   . GLY J 55  ? 4.3528 3.5348 2.8666 -0.0575 -0.3382 -0.4414 55  GLY I N   
17812 C CA  . GLY J 55  ? 4.2888 3.5483 2.7880 -0.0582 -0.3186 -0.4767 55  GLY I CA  
17813 C C   . GLY J 55  ? 4.1652 3.4855 2.7292 -0.0780 -0.2757 -0.4574 55  GLY I C   
17814 O O   . GLY J 55  ? 4.1274 3.5142 2.6826 -0.0798 -0.2581 -0.4860 55  GLY I O   
17815 N N   . ASP J 56  ? 4.0782 3.3788 2.7073 -0.0929 -0.2582 -0.4101 56  ASP I N   
17816 C CA  . ASP J 56  ? 3.9104 3.2665 2.6054 -0.1126 -0.2171 -0.3888 56  ASP I CA  
17817 C C   . ASP J 56  ? 3.8293 3.2016 2.5690 -0.1591 -0.2270 -0.3679 56  ASP I C   
17818 O O   . ASP J 56  ? 3.8378 3.1697 2.6304 -0.1911 -0.2397 -0.3218 56  ASP I O   
17819 C CB  . ASP J 56  ? 3.8302 3.1561 2.5780 -0.1125 -0.1972 -0.3451 56  ASP I CB  
17820 C CG  . ASP J 56  ? 3.6854 3.0693 2.4992 -0.1292 -0.1530 -0.3251 56  ASP I CG  
17821 O OD1 . ASP J 56  ? 3.6501 3.1039 2.4528 -0.1234 -0.1296 -0.3571 56  ASP I OD1 
17822 O OD2 . ASP J 56  ? 3.6603 3.0203 2.5371 -0.1477 -0.1416 -0.2779 56  ASP I OD2 
17823 N N   . THR J 57  ? 2.8873 3.6821 2.8178 -0.2549 -0.3265 -0.4931 57  THR I N   
17824 C CA  . THR J 57  ? 2.8185 3.6016 2.7543 -0.2673 -0.3580 -0.4827 57  THR I CA  
17825 C C   . THR J 57  ? 2.7495 3.5519 2.7104 -0.2871 -0.3898 -0.4440 57  THR I C   
17826 O O   . THR J 57  ? 2.8454 3.6836 2.7965 -0.2886 -0.3778 -0.4082 57  THR I O   
17827 C CB  . THR J 57  ? 2.9175 3.7113 2.8131 -0.2585 -0.3377 -0.4703 57  THR I CB  
17828 O OG1 . THR J 57  ? 2.8766 3.6534 2.7478 -0.2396 -0.3065 -0.5059 57  THR I OG1 
17829 C CG2 . THR J 57  ? 2.8616 3.6408 2.7627 -0.2709 -0.3706 -0.4623 57  THR I CG2 
17830 N N   . ASN J 58  ? 2.7297 3.5087 2.7229 -0.3022 -0.4299 -0.4514 58  ASN I N   
17831 C CA  . ASN J 58  ? 2.7062 3.4994 2.7256 -0.3221 -0.4638 -0.4173 58  ASN I CA  
17832 C C   . ASN J 58  ? 2.6356 3.4104 2.6614 -0.3339 -0.4970 -0.4133 58  ASN I C   
17833 O O   . ASN J 58  ? 2.5906 3.3332 2.6146 -0.3294 -0.5023 -0.4459 58  ASN I O   
17834 C CB  . ASN J 58  ? 2.6065 3.3913 2.6654 -0.3308 -0.4826 -0.4279 58  ASN I CB  
17835 C CG  . ASN J 58  ? 2.5806 3.3868 2.6636 -0.3499 -0.5114 -0.3886 58  ASN I CG  
17836 O OD1 . ASN J 58  ? 2.6834 3.5176 2.7507 -0.3546 -0.5100 -0.3503 58  ASN I OD1 
17837 N ND2 . ASN J 58  ? 2.5069 3.3008 2.6280 -0.3608 -0.5368 -0.3977 58  ASN I ND2 
17838 N N   . TYR J 59  ? 2.6472 3.4423 2.6808 -0.3493 -0.5198 -0.3733 59  TYR I N   
17839 C CA  . TYR J 59  ? 2.5874 3.3704 2.6255 -0.3616 -0.5513 -0.3624 59  TYR I CA  
17840 C C   . TYR J 59  ? 2.5034 3.2793 2.5829 -0.3823 -0.5949 -0.3509 59  TYR I C   
17841 O O   . TYR J 59  ? 2.4607 3.2433 2.5651 -0.3877 -0.6010 -0.3484 59  TYR I O   
17842 C CB  . TYR J 59  ? 2.6750 3.4881 2.6828 -0.3623 -0.5412 -0.3228 59  TYR I CB  
17843 C CG  . TYR J 59  ? 2.8106 3.6320 2.7755 -0.3432 -0.5006 -0.3297 59  TYR I CG  
17844 C CD1 . TYR J 59  ? 2.8343 3.6266 2.7872 -0.3293 -0.4856 -0.3717 59  TYR I CD1 
17845 C CD2 . TYR J 59  ? 2.9829 3.8411 2.9190 -0.3395 -0.4780 -0.2937 59  TYR I CD2 
17846 C CE1 . TYR J 59  ? 2.9830 3.7826 2.8963 -0.3120 -0.4486 -0.3779 59  TYR I CE1 
17847 C CE2 . TYR J 59  ? 3.1220 3.9878 3.0187 -0.3223 -0.4411 -0.2996 59  TYR I CE2 
17848 C CZ  . TYR J 59  ? 3.1206 3.9571 3.0059 -0.3086 -0.4264 -0.3416 59  TYR I CZ  
17849 O OH  . TYR J 59  ? 3.2216 4.0660 3.0674 -0.2914 -0.3895 -0.3471 59  TYR I OH  
17850 N N   . ASN J 60  ? 2.5762 3.3381 2.6620 -0.3937 -0.6254 -0.3437 60  ASN I N   
17851 C CA  . ASN J 60  ? 2.5079 3.2626 2.6305 -0.4142 -0.6689 -0.3303 60  ASN I CA  
17852 C C   . ASN J 60  ? 2.5502 3.3422 2.6733 -0.4263 -0.6765 -0.2798 60  ASN I C   
17853 O O   . ASN J 60  ? 2.6203 3.4314 2.7169 -0.4258 -0.6685 -0.2528 60  ASN I O   
17854 C CB  . ASN J 60  ? 2.4722 3.1972 2.6000 -0.4213 -0.6980 -0.3423 60  ASN I CB  
17855 C CG  . ASN J 60  ? 2.3925 3.1012 2.5620 -0.4410 -0.7441 -0.3393 60  ASN I CG  
17856 O OD1 . ASN J 60  ? 2.3771 3.1033 2.5687 -0.4522 -0.7572 -0.3164 60  ASN I OD1 
17857 N ND2 . ASN J 60  ? 2.3449 3.0198 2.5250 -0.4452 -0.7689 -0.3622 60  ASN I ND2 
17858 N N   . PRO J 61  ? 2.5552 3.3591 2.7070 -0.4368 -0.6904 -0.2661 61  PRO I N   
17859 C CA  . PRO J 61  ? 2.5828 3.4223 2.7369 -0.4491 -0.6987 -0.2179 61  PRO I CA  
17860 C C   . PRO J 61  ? 2.6173 3.4580 2.7691 -0.4624 -0.7261 -0.1913 61  PRO I C   
17861 O O   . PRO J 61  ? 2.6911 3.5637 2.8294 -0.4678 -0.7228 -0.1508 61  PRO I O   
17862 C CB  . PRO J 61  ? 2.4584 3.2962 2.6527 -0.4606 -0.7203 -0.2184 61  PRO I CB  
17863 C CG  . PRO J 61  ? 2.4210 3.2379 2.6203 -0.4472 -0.7017 -0.2615 61  PRO I CG  
17864 C CD  . PRO J 61  ? 2.4544 3.2413 2.6358 -0.4364 -0.6951 -0.2948 61  PRO I CD  
17865 N N   . SER J 62  ? 2.5463 3.3528 2.7114 -0.4681 -0.7534 -0.2131 62  SER I N   
17866 C CA  . SER J 62  ? 2.5414 3.3455 2.7052 -0.4808 -0.7810 -0.1908 62  SER I CA  
17867 C C   . SER J 62  ? 2.6430 3.4556 2.7650 -0.4699 -0.7575 -0.1835 62  SER I C   
17868 O O   . SER J 62  ? 2.6855 3.5116 2.7976 -0.4789 -0.7702 -0.1520 62  SER I O   
17869 C CB  . SER J 62  ? 2.3946 3.1579 2.5864 -0.4897 -0.8175 -0.2189 62  SER I CB  
17870 O OG  . SER J 62  ? 2.2902 3.0406 2.5193 -0.4965 -0.8349 -0.2350 62  SER I OG  
17871 N N   . LEU J 63  ? 2.4385 3.2432 2.5360 -0.4509 -0.7238 -0.2121 63  LEU I N   
17872 C CA  . LEU J 63  ? 2.5172 3.3286 2.5743 -0.4389 -0.6988 -0.2089 63  LEU I CA  
17873 C C   . LEU J 63  ? 2.5946 3.4348 2.6213 -0.4225 -0.6531 -0.2019 63  LEU I C   
17874 O O   . LEU J 63  ? 2.6476 3.4854 2.6423 -0.4071 -0.6246 -0.2160 63  LEU I O   
17875 C CB  . LEU J 63  ? 2.4855 3.2580 2.5378 -0.4307 -0.7012 -0.2509 63  LEU I CB  
17876 C CG  . LEU J 63  ? 2.4061 3.1471 2.4914 -0.4461 -0.7464 -0.2627 63  LEU I CG  
17877 C CD1 . LEU J 63  ? 2.4020 3.1043 2.4838 -0.4372 -0.7474 -0.3066 63  LEU I CD1 
17878 C CD2 . LEU J 63  ? 2.4373 3.1905 2.5230 -0.4619 -0.7735 -0.2243 63  LEU I CD2 
17879 N N   . LYS J 64  ? 2.5361 3.4035 2.5729 -0.4257 -0.6458 -0.1807 64  LYS I N   
17880 C CA  . LYS J 64  ? 2.5239 3.4179 2.5352 -0.4102 -0.6029 -0.1760 64  LYS I CA  
17881 C C   . LYS J 64  ? 2.5398 3.4589 2.5102 -0.4025 -0.5780 -0.1509 64  LYS I C   
17882 O O   . LYS J 64  ? 2.5353 3.4564 2.4758 -0.3847 -0.5424 -0.1666 64  LYS I O   
17883 C CB  . LYS J 64  ? 2.5111 3.4327 2.5411 -0.4174 -0.6034 -0.1514 64  LYS I CB  
17884 C CG  . LYS J 64  ? 2.4854 3.4039 2.5244 -0.4067 -0.5824 -0.1773 64  LYS I CG  
17885 C CD  . LYS J 64  ? 2.4759 3.4245 2.5327 -0.4157 -0.5857 -0.1473 64  LYS I CD  
17886 C CE  . LYS J 64  ? 2.4574 3.4260 2.4978 -0.3999 -0.5451 -0.1523 64  LYS I CE  
17887 N NZ  . LYS J 64  ? 2.4477 3.4464 2.5048 -0.4080 -0.5470 -0.1233 64  LYS I NZ  
17888 N N   . SER J 65  ? 2.6133 3.5512 2.5815 -0.4156 -0.5961 -0.1121 65  SER I N   
17889 C CA  . SER J 65  ? 2.7007 3.6668 2.6314 -0.4096 -0.5727 -0.0837 65  SER I CA  
17890 C C   . SER J 65  ? 2.7281 3.6755 2.6371 -0.4063 -0.5760 -0.0933 65  SER I C   
17891 O O   . SER J 65  ? 2.7914 3.7596 2.6753 -0.4071 -0.5692 -0.0643 65  SER I O   
17892 C CB  . SER J 65  ? 2.7212 3.7210 2.6581 -0.4248 -0.5873 -0.0343 65  SER I CB  
17893 O OG  . SER J 65  ? 2.6777 3.6631 2.6403 -0.4437 -0.6307 -0.0240 65  SER I OG  
17894 N N   . ARG J 66  ? 2.7493 3.6583 2.6675 -0.4025 -0.5860 -0.1334 66  ARG I N   
17895 C CA  . ARG J 66  ? 2.7808 3.6697 2.6797 -0.3990 -0.5896 -0.1457 66  ARG I CA  
17896 C C   . ARG J 66  ? 2.7952 3.6556 2.6817 -0.3818 -0.5684 -0.1924 66  ARG I C   
17897 O O   . ARG J 66  ? 2.8406 3.6915 2.7011 -0.3740 -0.5586 -0.2014 66  ARG I O   
17898 C CB  . ARG J 66  ? 2.7135 3.5803 2.6389 -0.4172 -0.6360 -0.1426 66  ARG I CB  
17899 C CG  . ARG J 66  ? 2.7185 3.6108 2.6564 -0.4355 -0.6602 -0.0965 66  ARG I CG  
17900 C CD  . ARG J 66  ? 2.6872 3.5592 2.6414 -0.4514 -0.7017 -0.0908 66  ARG I CD  
17901 N NE  . ARG J 66  ? 2.6034 3.4368 2.5893 -0.4560 -0.7283 -0.1265 66  ARG I NE  
17902 C CZ  . ARG J 66  ? 2.5811 3.3811 2.5632 -0.4511 -0.7351 -0.1585 66  ARG I CZ  
17903 N NH1 . ARG J 66  ? 2.6387 3.4394 2.5865 -0.4415 -0.7172 -0.1591 66  ARG I NH1 
17904 N NH2 . ARG J 66  ? 2.4994 3.2656 2.5119 -0.4558 -0.7599 -0.1898 66  ARG I NH2 
17905 N N   . VAL J 67  ? 2.9126 3.7593 2.8164 -0.3754 -0.5606 -0.2226 67  VAL I N   
17906 C CA  . VAL J 67  ? 2.9062 3.7236 2.8014 -0.3599 -0.5429 -0.2689 67  VAL I CA  
17907 C C   . VAL J 67  ? 2.9722 3.8081 2.8386 -0.3408 -0.4960 -0.2754 67  VAL I C   
17908 O O   . VAL J 67  ? 2.9953 3.8612 2.8605 -0.3400 -0.4804 -0.2528 67  VAL I O   
17909 C CB  . VAL J 67  ? 2.8013 3.5873 2.7354 -0.3656 -0.5670 -0.3016 67  VAL I CB  
17910 C CG1 . VAL J 67  ? 2.7762 3.5776 2.7265 -0.3639 -0.5549 -0.3007 67  VAL I CG1 
17911 C CG2 . VAL J 67  ? 2.7754 3.5248 2.7034 -0.3534 -0.5592 -0.3492 67  VAL I CG2 
17912 N N   . HIS J 68  ? 3.0613 3.8790 2.9037 -0.3251 -0.4733 -0.3063 68  HIS I N   
17913 C CA  . HIS J 68  ? 3.0836 3.9121 2.8972 -0.3052 -0.4282 -0.3198 68  HIS I CA  
17914 C C   . HIS J 68  ? 3.0384 3.8296 2.8495 -0.2930 -0.4201 -0.3698 68  HIS I C   
17915 O O   . HIS J 68  ? 3.0081 3.7758 2.8144 -0.2942 -0.4339 -0.3840 68  HIS I O   
17916 C CB  . HIS J 68  ? 3.1560 4.0141 2.9295 -0.2980 -0.4021 -0.2906 68  HIS I CB  
17917 C CG  . HIS J 68  ? 3.1987 4.0949 2.9738 -0.3091 -0.4075 -0.2419 68  HIS I CG  
17918 N ND1 . HIS J 68  ? 3.1413 4.0537 2.9407 -0.3162 -0.4134 -0.2280 68  HIS I ND1 
17919 C CD2 . HIS J 68  ? 3.2260 4.1474 2.9816 -0.3144 -0.4081 -0.2039 68  HIS I CD2 
17920 C CE1 . HIS J 68  ? 3.1691 4.1150 2.9639 -0.3253 -0.4171 -0.1838 68  HIS I CE1 
17921 N NE2 . HIS J 68  ? 3.2508 4.2028 3.0192 -0.3245 -0.4141 -0.1683 68  HIS I NE2 
17922 N N   . LEU J 69  ? 3.0779 3.8635 2.8921 -0.2816 -0.3979 -0.3962 69  LEU I N   
17923 C CA  . LEU J 69  ? 3.0280 3.7795 2.8408 -0.2693 -0.3874 -0.4448 69  LEU I CA  
17924 C C   . LEU J 69  ? 3.0796 3.8415 2.8577 -0.2481 -0.3399 -0.4580 69  LEU I C   
17925 O O   . LEU J 69  ? 3.1455 3.9402 2.9083 -0.2432 -0.3154 -0.4333 69  LEU I O   
17926 C CB  . LEU J 69  ? 2.9504 3.6800 2.8022 -0.2751 -0.4067 -0.4704 69  LEU I CB  
17927 C CG  . LEU J 69  ? 2.8726 3.5839 2.7609 -0.2948 -0.4549 -0.4668 69  LEU I CG  
17928 C CD1 . LEU J 69  ? 2.7852 3.4755 2.7102 -0.2989 -0.4701 -0.4939 69  LEU I CD1 
17929 C CD2 . LEU J 69  ? 2.8447 3.5288 2.7260 -0.2962 -0.4713 -0.4826 69  LEU I CD2 
17930 N N   . SER J 70  ? 3.2060 3.9395 2.9715 -0.2356 -0.3268 -0.4974 70  SER I N   
17931 C CA  . SER J 70  ? 3.2519 3.9918 2.9840 -0.2151 -0.2819 -0.5133 70  SER I CA  
17932 C C   . SER J 70  ? 3.1938 3.8956 2.9276 -0.2043 -0.2756 -0.5645 70  SER I C   
17933 O O   . SER J 70  ? 3.1271 3.7980 2.8802 -0.2118 -0.3043 -0.5855 70  SER I O   
17934 C CB  . SER J 70  ? 3.2921 4.0515 2.9843 -0.2083 -0.2616 -0.4910 70  SER I CB  
17935 O OG  . SER J 70  ? 3.3570 4.1483 3.0487 -0.2202 -0.2730 -0.4437 70  SER I OG  
17936 N N   . LEU J 71  ? 3.2565 3.9611 2.9693 -0.1866 -0.2370 -0.5841 71  LEU I N   
17937 C CA  . LEU J 71  ? 3.2329 3.9046 2.9428 -0.1738 -0.2238 -0.6327 71  LEU I CA  
17938 C C   . LEU J 71  ? 3.3183 3.9971 2.9844 -0.1549 -0.1828 -0.6402 71  LEU I C   
17939 O O   . LEU J 71  ? 3.3975 4.1049 3.0425 -0.1457 -0.1516 -0.6230 71  LEU I O   
17940 C CB  . LEU J 71  ? 3.1945 3.8595 2.9270 -0.1708 -0.2179 -0.6544 71  LEU I CB  
17941 C CG  . LEU J 71  ? 3.0914 3.7441 2.8692 -0.1882 -0.2577 -0.6548 71  LEU I CG  
17942 C CD1 . LEU J 71  ? 3.0801 3.7295 2.8764 -0.1836 -0.2470 -0.6748 71  LEU I CD1 
17943 C CD2 . LEU J 71  ? 2.9927 3.6089 2.7892 -0.1965 -0.2910 -0.6788 71  LEU I CD2 
17944 N N   . ASP J 72  ? 3.2389 3.8918 2.8914 -0.1492 -0.1828 -0.6658 72  ASP I N   
17945 C CA  . ASP J 72  ? 3.2984 3.9536 2.9097 -0.1312 -0.1454 -0.6770 72  ASP I CA  
17946 C C   . ASP J 72  ? 3.3046 3.9349 2.9129 -0.1160 -0.1227 -0.7237 72  ASP I C   
17947 O O   . ASP J 72  ? 3.2113 3.8068 2.8299 -0.1157 -0.1363 -0.7585 72  ASP I O   
17948 C CB  . ASP J 72  ? 3.2477 3.8913 2.8439 -0.1340 -0.1582 -0.6750 72  ASP I CB  
17949 C CG  . ASP J 72  ? 3.3528 4.0104 2.9039 -0.1185 -0.1214 -0.6704 72  ASP I CG  
17950 O OD1 . ASP J 72  ? 3.4590 4.1224 2.9905 -0.1025 -0.0848 -0.6848 72  ASP I OD1 
17951 O OD2 . ASP J 72  ? 3.3648 4.0277 2.8999 -0.1224 -0.1291 -0.6518 72  ASP I OD2 
17952 N N   . LYS J 73  ? 3.1626 3.8101 2.7570 -0.1035 -0.0883 -0.7249 73  LYS I N   
17953 C CA  . LYS J 73  ? 3.1404 3.7648 2.7319 -0.0891 -0.0661 -0.7688 73  LYS I CA  
17954 C C   . LYS J 73  ? 3.1528 3.7647 2.7082 -0.0731 -0.0386 -0.7914 73  LYS I C   
17955 O O   . LYS J 73  ? 3.1413 3.7261 2.6958 -0.0628 -0.0269 -0.8326 73  LYS I O   
17956 C CB  . LYS J 73  ? 3.1524 3.7980 2.7410 -0.0806 -0.0379 -0.7643 73  LYS I CB  
17957 C CG  . LYS J 73  ? 3.1520 3.8102 2.7755 -0.0943 -0.0601 -0.7455 73  LYS I CG  
17958 C CD  . LYS J 73  ? 3.1329 3.8121 2.7494 -0.0839 -0.0283 -0.7428 73  LYS I CD  
17959 C CE  . LYS J 73  ? 3.1811 3.8958 2.7601 -0.0743 0.0044  -0.7119 73  LYS I CE  
17960 N NZ  . LYS J 73  ? 3.1950 3.9301 2.7670 -0.0639 0.0355  -0.7095 73  LYS I NZ  
17961 N N   . SER J 74  ? 3.1600 3.7910 2.6860 -0.0711 -0.0286 -0.7654 74  SER I N   
17962 C CA  . SER J 74  ? 3.1842 3.8058 2.6745 -0.0563 -0.0025 -0.7836 74  SER I CA  
17963 C C   . SER J 74  ? 3.1591 3.7480 2.6569 -0.0620 -0.0290 -0.8051 74  SER I C   
17964 O O   . SER J 74  ? 3.1580 3.7222 2.6415 -0.0505 -0.0148 -0.8405 74  SER I O   
17965 C CB  . SER J 74  ? 3.2669 3.9234 2.7221 -0.0515 0.0202  -0.7464 74  SER I CB  
17966 O OG  . SER J 74  ? 3.2959 3.9662 2.7594 -0.0674 -0.0090 -0.7104 74  SER I OG  
17967 N N   . LYS J 75  ? 3.1273 3.7157 2.6478 -0.0798 -0.0677 -0.7840 75  LYS I N   
17968 C CA  . LYS J 75  ? 3.1097 3.6691 2.6396 -0.0872 -0.0966 -0.8000 75  LYS I CA  
17969 C C   . LYS J 75  ? 3.0560 3.5853 2.6273 -0.0972 -0.1288 -0.8266 75  LYS I C   
17970 O O   . LYS J 75  ? 3.0363 3.5375 2.6192 -0.1031 -0.1540 -0.8454 75  LYS I O   
17971 C CB  . LYS J 75  ? 3.1335 3.7111 2.6612 -0.1008 -0.1196 -0.7592 75  LYS I CB  
17972 C CG  . LYS J 75  ? 3.1961 3.8031 2.6829 -0.0920 -0.0901 -0.7317 75  LYS I CG  
17973 C CD  . LYS J 75  ? 3.2136 3.8372 2.6996 -0.1062 -0.1147 -0.6921 75  LYS I CD  
17974 C CE  . LYS J 75  ? 3.2817 3.9352 2.7270 -0.0975 -0.0851 -0.6642 75  LYS I CE  
17975 N NZ  . LYS J 75  ? 3.3138 3.9558 2.7389 -0.0970 -0.0908 -0.6663 75  LYS I NZ  
17976 N N   . ASN J 76  ? 3.2327 3.7677 2.8260 -0.0991 -0.1281 -0.8285 76  ASN I N   
17977 C CA  . ASN J 76  ? 3.1411 3.6499 2.7743 -0.1079 -0.1558 -0.8533 76  ASN I CA  
17978 C C   . ASN J 76  ? 3.1048 3.6040 2.7664 -0.1276 -0.2026 -0.8389 76  ASN I C   
17979 O O   . ASN J 76  ? 3.0709 3.5379 2.7473 -0.1317 -0.2254 -0.8656 76  ASN I O   
17980 C CB  . ASN J 76  ? 3.1374 3.6110 2.7679 -0.0956 -0.1435 -0.9047 76  ASN I CB  
17981 C CG  . ASN J 76  ? 3.1315 3.5814 2.8000 -0.1014 -0.1633 -0.9323 76  ASN I CG  
17982 O OD1 . ASN J 76  ? 3.1450 3.6014 2.8196 -0.0957 -0.1461 -0.9400 76  ASN I OD1 
17983 N ND2 . ASN J 76  ? 3.0876 3.5098 2.7821 -0.1128 -0.1996 -0.9474 76  ASN I ND2 
17984 N N   . LEU J 77  ? 3.1451 3.6731 2.8143 -0.1398 -0.2167 -0.7956 77  LEU I N   
17985 C CA  . LEU J 77  ? 3.1416 3.6638 2.8374 -0.1591 -0.2607 -0.7777 77  LEU I CA  
17986 C C   . LEU J 77  ? 3.1256 3.6775 2.8399 -0.1721 -0.2743 -0.7377 77  LEU I C   
17987 O O   . LEU J 77  ? 3.1403 3.7209 2.8421 -0.1659 -0.2484 -0.7191 77  LEU I O   
17988 C CB  . LEU J 77  ? 3.1684 3.6909 2.8420 -0.1612 -0.2676 -0.7633 77  LEU I CB  
17989 C CG  . LEU J 77  ? 3.1857 3.7408 2.8196 -0.1534 -0.2388 -0.7317 77  LEU I CG  
17990 C CD1 . LEU J 77  ? 3.1552 3.7439 2.7962 -0.1672 -0.2537 -0.6818 77  LEU I CD1 
17991 C CD2 . LEU J 77  ? 3.1793 3.7212 2.7878 -0.1486 -0.2367 -0.7400 77  LEU I CD2 
17992 N N   . VAL J 78  ? 3.1312 3.6756 2.8758 -0.1903 -0.3158 -0.7250 78  VAL I N   
17993 C CA  . VAL J 78  ? 3.0971 3.6663 2.8636 -0.2053 -0.3357 -0.6873 78  VAL I CA  
17994 C C   . VAL J 78  ? 3.1227 3.7064 2.8812 -0.2167 -0.3554 -0.6506 78  VAL I C   
17995 O O   . VAL J 78  ? 3.1274 3.6892 2.8866 -0.2211 -0.3756 -0.6608 78  VAL I O   
17996 C CB  . VAL J 78  ? 3.0139 3.5620 2.8255 -0.2180 -0.3695 -0.7028 78  VAL I CB  
17997 C CG1 . VAL J 78  ? 2.9716 3.5473 2.8044 -0.2319 -0.3856 -0.6646 78  VAL I CG1 
17998 C CG2 . VAL J 78  ? 3.0274 3.5546 2.8465 -0.2064 -0.3521 -0.7452 78  VAL I CG2 
17999 N N   . SER J 79  ? 3.0928 3.7133 2.8434 -0.2214 -0.3494 -0.6080 79  SER I N   
18000 C CA  . SER J 79  ? 3.1478 3.7861 2.8889 -0.2319 -0.3652 -0.5699 79  SER I CA  
18001 C C   . SER J 79  ? 3.1593 3.8108 2.9327 -0.2515 -0.3991 -0.5387 79  SER I C   
18002 O O   . SER J 79  ? 3.1217 3.7767 2.9197 -0.2553 -0.4034 -0.5407 79  SER I O   
18003 C CB  . SER J 79  ? 3.1733 3.8453 2.8739 -0.2210 -0.3289 -0.5434 79  SER I CB  
18004 O OG  . SER J 79  ? 3.2547 3.9461 2.9464 -0.2317 -0.3438 -0.5044 79  SER I OG  
18005 N N   . LEU J 80  ? 3.0316 3.6905 2.8048 -0.2642 -0.4234 -0.5096 80  LEU I N   
18006 C CA  . LEU J 80  ? 3.0348 3.7070 2.8366 -0.2835 -0.4567 -0.4771 80  LEU I CA  
18007 C C   . LEU J 80  ? 3.1217 3.8196 2.9043 -0.2909 -0.4618 -0.4343 80  LEU I C   
18008 O O   . LEU J 80  ? 3.1172 3.8071 2.8774 -0.2873 -0.4597 -0.4368 80  LEU I O   
18009 C CB  . LEU J 80  ? 2.9440 3.5818 2.7830 -0.2966 -0.4985 -0.4984 80  LEU I CB  
18010 C CG  . LEU J 80  ? 2.9339 3.5793 2.8057 -0.3177 -0.5379 -0.4690 80  LEU I CG  
18011 C CD1 . LEU J 80  ? 2.8746 3.4929 2.7869 -0.3252 -0.5637 -0.4962 80  LEU I CD1 
18012 C CD2 . LEU J 80  ? 2.9243 3.5651 2.7923 -0.3289 -0.5647 -0.4503 80  LEU I CD2 
18013 N N   . ARG J 81  ? 2.8730 3.6020 2.6643 -0.3012 -0.4684 -0.3951 81  ARG I N   
18014 C CA  . ARG J 81  ? 2.9470 3.7032 2.7227 -0.3096 -0.4744 -0.3511 81  ARG I CA  
18015 C C   . ARG J 81  ? 2.9485 3.7157 2.7569 -0.3301 -0.5103 -0.3208 81  ARG I C   
18016 O O   . ARG J 81  ? 2.9350 3.7126 2.7643 -0.3334 -0.5109 -0.3164 81  ARG I O   
18017 C CB  . ARG J 81  ? 3.0224 3.8143 2.7630 -0.2970 -0.4330 -0.3293 81  ARG I CB  
18018 C CG  . ARG J 81  ? 3.0841 3.8673 2.7878 -0.2783 -0.4001 -0.3527 81  ARG I CG  
18019 C CD  . ARG J 81  ? 3.1521 3.9696 2.8203 -0.2653 -0.3586 -0.3323 81  ARG I CD  
18020 N NE  . ARG J 81  ? 3.1800 4.0300 2.8360 -0.2744 -0.3633 -0.2851 81  ARG I NE  
18021 C CZ  . ARG J 81  ? 3.1844 4.0660 2.8485 -0.2814 -0.3629 -0.2514 81  ARG I CZ  
18022 N NH1 . ARG J 81  ? 3.2470 4.1569 2.8990 -0.2896 -0.3674 -0.2094 81  ARG I NH1 
18023 N NH2 . ARG J 81  ? 3.1651 4.0500 2.8492 -0.2802 -0.3577 -0.2599 81  ARG I NH2 
18024 N N   . LEU J 82  ? 2.6784 3.4433 2.4909 -0.3437 -0.5399 -0.3000 82  LEU I N   
18025 C CA  . LEU J 82  ? 2.6847 3.4593 2.5266 -0.3640 -0.5759 -0.2694 82  LEU I CA  
18026 C C   . LEU J 82  ? 2.7076 3.5083 2.5299 -0.3717 -0.5806 -0.2262 82  LEU I C   
18027 O O   . LEU J 82  ? 2.7263 3.5131 2.5398 -0.3754 -0.5956 -0.2263 82  LEU I O   
18028 C CB  . LEU J 82  ? 2.6868 3.4248 2.5629 -0.3760 -0.6168 -0.2920 82  LEU I CB  
18029 C CG  . LEU J 82  ? 2.6930 3.4369 2.6023 -0.3975 -0.6568 -0.2639 82  LEU I CG  
18030 C CD1 . LEU J 82  ? 2.6750 3.4406 2.6032 -0.4010 -0.6519 -0.2499 82  LEU I CD1 
18031 C CD2 . LEU J 82  ? 2.6959 3.4012 2.6362 -0.4078 -0.6954 -0.2894 82  LEU I CD2 
18032 N N   . THR J 83  A 2.5948 3.4329 2.4112 -0.3748 -0.5691 -0.1893 82  THR I N   
18033 C CA  . THR J 83  A 2.6767 3.5424 2.4741 -0.3820 -0.5716 -0.1465 82  THR I CA  
18034 C C   . THR J 83  A 2.6948 3.5617 2.5224 -0.4042 -0.6149 -0.1198 82  THR I C   
18035 O O   . THR J 83  A 2.6434 3.5068 2.5045 -0.4137 -0.6342 -0.1212 82  THR I O   
18036 C CB  . THR J 83  A 2.7063 3.6129 2.4809 -0.3743 -0.5371 -0.1186 82  THR I CB  
18037 O OG1 . THR J 83  A 2.6869 3.6069 2.4882 -0.3808 -0.5427 -0.1090 82  THR I OG1 
18038 C CG2 . THR J 83  A 2.7412 3.6472 2.4842 -0.3520 -0.4934 -0.1439 82  THR I CG2 
18039 N N   . GLY J 84  B 2.6041 3.4766 2.4197 -0.4126 -0.6300 -0.0951 82  GLY I N   
18040 C CA  . GLY J 84  B 2.6174 3.4915 2.4582 -0.4337 -0.6707 -0.0679 82  GLY I CA  
18041 C C   . GLY J 84  B 2.6158 3.4525 2.4925 -0.4442 -0.7090 -0.0937 82  GLY I C   
18042 O O   . GLY J 84  B 2.6074 3.4431 2.5176 -0.4564 -0.7325 -0.0880 82  GLY I O   
18043 N N   . VAL J 85  C 2.6363 3.4420 2.5061 -0.4396 -0.7157 -0.1219 82  VAL I N   
18044 C CA  . VAL J 85  C 2.6353 3.4030 2.5370 -0.4481 -0.7505 -0.1500 82  VAL I CA  
18045 C C   . VAL J 85  C 2.6564 3.4216 2.5740 -0.4678 -0.7915 -0.1232 82  VAL I C   
18046 O O   . VAL J 85  C 2.6757 3.4605 2.5723 -0.4719 -0.7911 -0.0913 82  VAL I O   
18047 C CB  . VAL J 85  C 2.6350 3.3704 2.5222 -0.4342 -0.7394 -0.1927 82  VAL I CB  
18048 C CG1 . VAL J 85  C 2.6118 3.3451 2.4903 -0.4162 -0.7034 -0.2233 82  VAL I CG1 
18049 C CG2 . VAL J 85  C 2.6565 3.3987 2.5073 -0.4292 -0.7278 -0.1798 82  VAL I CG2 
18050 N N   . THR J 86  ? 2.7543 3.4955 2.7098 -0.4803 -0.8272 -0.1361 83  THR I N   
18051 C CA  . THR J 86  ? 2.7978 3.5320 2.7724 -0.4994 -0.8691 -0.1151 83  THR I CA  
18052 C C   . THR J 86  ? 2.7346 3.4254 2.7310 -0.5026 -0.8972 -0.1515 83  THR I C   
18053 O O   . THR J 86  ? 2.6675 3.3353 2.6588 -0.4891 -0.8817 -0.1913 83  THR I O   
18054 C CB  . THR J 86  ? 2.8154 3.5685 2.8191 -0.5154 -0.8899 -0.0857 83  THR I CB  
18055 O OG1 . THR J 86  ? 2.7247 3.4641 2.7569 -0.5138 -0.8920 -0.1124 83  THR I OG1 
18056 C CG2 . THR J 86  ? 2.8916 3.6889 2.8739 -0.5139 -0.8652 -0.0458 83  THR I CG2 
18057 N N   . ALA J 87  ? 2.8930 3.5720 2.9146 -0.5205 -0.9388 -0.1389 84  ALA I N   
18058 C CA  . ALA J 87  ? 2.7972 3.4352 2.8405 -0.5244 -0.9675 -0.1721 84  ALA I CA  
18059 C C   . ALA J 87  ? 2.6523 3.2706 2.7292 -0.5244 -0.9755 -0.2029 84  ALA I C   
18060 O O   . ALA J 87  ? 2.6165 3.1993 2.7087 -0.5231 -0.9909 -0.2389 84  ALA I O   
18061 C CB  . ALA J 87  ? 2.8605 3.4920 2.9201 -0.5437 -1.0098 -0.1484 84  ALA I CB  
18062 N N   . ALA J 88  ? 2.7961 3.4367 2.8846 -0.5259 -0.9655 -0.1896 85  ALA I N   
18063 C CA  . ALA J 88  ? 2.7096 3.3340 2.8301 -0.5262 -0.9723 -0.2166 85  ALA I CA  
18064 C C   . ALA J 88  ? 2.6865 3.2994 2.7929 -0.5062 -0.9377 -0.2559 85  ALA I C   
18065 O O   . ALA J 88  ? 2.6092 3.2000 2.7401 -0.5044 -0.9436 -0.2880 85  ALA I O   
18066 C CB  . ALA J 88  ? 2.7234 3.3766 2.8615 -0.5353 -0.9744 -0.1871 85  ALA I CB  
18067 N N   . ASP J 89  ? 2.7575 3.3848 2.8248 -0.4913 -0.9019 -0.2541 86  ASP I N   
18068 C CA  . ASP J 89  ? 2.7343 3.3530 2.7841 -0.4715 -0.8661 -0.2892 86  ASP I CA  
18069 C C   . ASP J 89  ? 2.7173 3.2995 2.7610 -0.4639 -0.8701 -0.3279 86  ASP I C   
18070 O O   . ASP J 89  ? 2.6478 3.2182 2.6782 -0.4477 -0.8427 -0.3610 86  ASP I O   
18071 C CB  . ASP J 89  ? 2.7697 3.4217 2.7793 -0.4585 -0.8245 -0.2690 86  ASP I CB  
18072 C CG  . ASP J 89  ? 2.7949 3.4835 2.8083 -0.4627 -0.8140 -0.2355 86  ASP I CG  
18073 O OD1 . ASP J 89  ? 2.7374 3.4233 2.7815 -0.4689 -0.8259 -0.2410 86  ASP I OD1 
18074 O OD2 . ASP J 89  ? 2.8432 3.5635 2.8287 -0.4598 -0.7935 -0.2038 86  ASP I OD2 
18075 N N   . SER J 90  ? 2.8475 3.4114 2.9009 -0.4754 -0.9036 -0.3245 87  SER I N   
18076 C CA  . SER J 90  ? 2.7933 3.3216 2.8431 -0.4700 -0.9117 -0.3597 87  SER I CA  
18077 C C   . SER J 90  ? 2.6864 3.1825 2.7683 -0.4695 -0.9249 -0.4008 87  SER I C   
18078 O O   . SER J 90  ? 2.6677 3.1497 2.7845 -0.4843 -0.9612 -0.4003 87  SER I O   
18079 C CB  . SER J 90  ? 2.8326 3.3524 2.8854 -0.4838 -0.9456 -0.3411 87  SER I CB  
18080 O OG  . SER J 90  ? 2.8523 3.3765 2.9374 -0.5030 -0.9813 -0.3169 87  SER I OG  
18081 N N   . ALA J 91  ? 1.8081 3.2372 3.2519 -0.4181 -0.5025 0.2375  88  ALA I N   
18082 C CA  . ALA J 91  ? 1.7741 3.1692 3.2005 -0.4123 -0.5160 0.2470  88  ALA I CA  
18083 C C   . ALA J 91  ? 1.7118 3.1018 3.1234 -0.3624 -0.5053 0.2273  88  ALA I C   
18084 O O   . ALA J 91  ? 1.6806 3.0883 3.0928 -0.3340 -0.4884 0.2097  88  ALA I O   
18085 C CB  . ALA J 91  ? 1.8031 3.1913 3.2275 -0.4408 -0.5318 0.2392  88  ALA I CB  
18086 N N   . ILE J 92  ? 1.7719 3.1347 3.1680 -0.3532 -0.5153 0.2298  89  ILE I N   
18087 C CA  . ILE J 92  ? 1.7099 3.0629 3.0876 -0.3098 -0.5064 0.2117  89  ILE I CA  
18088 C C   . ILE J 92  ? 1.7172 3.0743 3.0857 -0.3059 -0.5105 0.1834  89  ILE I C   
18089 O O   . ILE J 92  ? 1.7236 3.0629 3.0878 -0.3266 -0.5273 0.1914  89  ILE I O   
18090 C CB  . ILE J 92  ? 1.6898 3.0086 3.0583 -0.3005 -0.5137 0.2365  89  ILE I CB  
18091 C CG1 . ILE J 92  ? 1.7152 3.0294 3.0955 -0.3067 -0.5121 0.2661  89  ILE I CG1 
18092 C CG2 . ILE J 92  ? 1.6598 2.9693 3.0081 -0.2558 -0.5019 0.2171  89  ILE I CG2 
18093 C CD1 . ILE J 92  ? 1.7109 2.9910 3.0881 -0.2977 -0.5208 0.2912  89  ILE I CD1 
18094 N N   . TYR J 93  ? 1.6811 3.0595 3.0459 -0.2803 -0.4966 0.1500  90  TYR I N   
18095 C CA  . TYR J 93  ? 1.7187 3.1059 3.0803 -0.2772 -0.5021 0.1276  90  TYR I CA  
18096 C C   . TYR J 93  ? 1.6870 3.0554 3.0284 -0.2496 -0.5036 0.1265  90  TYR I C   
18097 O O   . TYR J 93  ? 1.6711 3.0376 3.0071 -0.2211 -0.4934 0.1304  90  TYR I O   
18098 C CB  . TYR J 93  ? 1.7839 3.2068 3.1687 -0.2749 -0.4979 0.1211  90  TYR I CB  
18099 C CG  . TYR J 93  ? 1.8600 3.3055 3.2678 -0.3048 -0.4974 0.1193  90  TYR I CG  
18100 C CD1 . TYR J 93  ? 1.8364 3.2861 3.2509 -0.3092 -0.4865 0.1283  90  TYR I CD1 
18101 C CD2 . TYR J 93  ? 1.9060 3.3686 3.3291 -0.3291 -0.5079 0.1085  90  TYR I CD2 
18102 C CE1 . TYR J 93  ? 1.8880 3.3579 3.3236 -0.3384 -0.4850 0.1264  90  TYR I CE1 
18103 C CE2 . TYR J 93  ? 1.9694 3.4528 3.4148 -0.3574 -0.5066 0.1060  90  TYR I CE2 
18104 C CZ  . TYR J 93  ? 1.9758 3.4626 3.4272 -0.3626 -0.4947 0.1150  90  TYR I CZ  
18105 O OH  . TYR J 93  ? 2.0349 3.5419 3.5086 -0.3926 -0.4925 0.1124  90  TYR I OH  
18106 N N   . TYR J 94  ? 1.8127 3.1659 3.1422 -0.2590 -0.5160 0.1210  91  TYR I N   
18107 C CA  . TYR J 94  ? 1.7751 3.1101 3.0851 -0.2367 -0.5182 0.1191  91  TYR I CA  
18108 C C   . TYR J 94  ? 1.8110 3.1610 3.1255 -0.2373 -0.5271 0.1079  91  TYR I C   
18109 O O   . TYR J 94  ? 1.7924 3.1588 3.1208 -0.2610 -0.5365 0.1009  91  TYR I O   
18110 C CB  . TYR J 94  ? 1.7210 3.0232 3.0128 -0.2458 -0.5272 0.1255  91  TYR I CB  
18111 C CG  . TYR J 94  ? 1.6629 2.9471 2.9627 -0.2510 -0.5287 0.1577  91  TYR I CG  
18112 C CD1 . TYR J 94  ? 1.6912 2.9761 2.9868 -0.2208 -0.5116 0.1580  91  TYR I CD1 
18113 C CD2 . TYR J 94  ? 1.6798 2.9435 2.9896 -0.2861 -0.5482 0.1867  91  TYR I CD2 
18114 C CE1 . TYR J 94  ? 1.7114 2.9800 3.0158 -0.2234 -0.5134 0.1872  91  TYR I CE1 
18115 C CE2 . TYR J 94  ? 1.6536 2.8998 2.9718 -0.2902 -0.5508 0.2158  91  TYR I CE2 
18116 C CZ  . TYR J 94  ? 1.6869 2.9372 3.0042 -0.2578 -0.5332 0.2164  91  TYR I CZ  
18117 O OH  . TYR J 94  ? 1.7889 3.0219 3.1165 -0.2600 -0.5363 0.2452  91  TYR I OH  
18118 N N   . CYS J 95  ? 1.9420 3.2859 3.2448 -0.2112 -0.5241 0.1061  92  CYS I N   
18119 C CA  . CYS J 95  ? 1.9703 3.3231 3.2725 -0.2077 -0.5326 0.0961  92  CYS I CA  
18120 C C   . CYS J 95  ? 1.9799 3.3035 3.2567 -0.1988 -0.5382 0.0961  92  CYS I C   
18121 O O   . CYS J 95  ? 1.9808 3.2872 3.2434 -0.1762 -0.5286 0.1015  92  CYS I O   
18122 C CB  . CYS J 95  ? 2.0186 3.3925 3.3308 -0.1862 -0.5237 0.0927  92  CYS I CB  
18123 S SG  . CYS J 95  ? 2.3295 3.6857 3.6239 -0.1500 -0.5086 0.0988  92  CYS I SG  
18124 N N   . ALA J 96  ? 1.8745 3.1919 3.1455 -0.2169 -0.5536 0.0898  93  ALA I N   
18125 C CA  . ALA J 96  ? 1.8939 3.1823 3.1401 -0.2120 -0.5600 0.0896  93  ALA I CA  
18126 C C   . ALA J 96  ? 1.9593 3.2513 3.2016 -0.2181 -0.5741 0.0803  93  ALA I C   
18127 O O   . ALA J 96  ? 1.9885 3.2998 3.2462 -0.2366 -0.5838 0.0739  93  ALA I O   
18128 C CB  . ALA J 96  ? 1.8637 3.1270 3.0983 -0.2316 -0.5664 0.0936  93  ALA I CB  
18129 N N   . THR J 97  ? 1.8300 3.1035 3.0522 -0.2023 -0.5750 0.0795  94  THR I N   
18130 C CA  . THR J 97  ? 1.9130 3.1854 3.1279 -0.2081 -0.5892 0.0717  94  THR I CA  
18131 C C   . THR J 97  ? 1.9457 3.2025 3.1533 -0.2379 -0.6062 0.0693  94  THR I C   
18132 O O   . THR J 97  ? 1.8905 3.1288 3.0907 -0.2498 -0.6061 0.0740  94  THR I O   
18133 C CB  . THR J 97  ? 1.9337 3.1859 3.1262 -0.1870 -0.5866 0.0720  94  THR I CB  
18134 O OG1 . THR J 97  ? 1.9352 3.1572 3.1085 -0.1884 -0.5861 0.0771  94  THR I OG1 
18135 C CG2 . THR J 97  ? 1.9389 3.2018 3.1354 -0.1582 -0.5697 0.0741  94  THR I CG2 
18136 N N   . THR J 98  ? 1.8696 3.1323 3.0781 -0.2505 -0.6214 0.0616  95  THR I N   
18137 C CA  . THR J 98  ? 1.8842 3.1314 3.0853 -0.2805 -0.6390 0.0583  95  THR I CA  
18138 C C   . THR J 98  ? 1.9747 3.2044 3.1564 -0.2838 -0.6547 0.0530  95  THR I C   
18139 O O   . THR J 98  ? 2.0356 3.2828 3.2245 -0.2754 -0.6588 0.0477  95  THR I O   
18140 C CB  . THR J 98  ? 1.8394 3.1146 3.0671 -0.3015 -0.6444 0.0537  95  THR I CB  
18141 O OG1 . THR J 98  ? 1.7767 3.0667 3.0214 -0.2996 -0.6297 0.0590  95  THR I OG1 
18142 C CG2 . THR J 98  ? 1.8056 3.0621 3.0247 -0.3337 -0.6618 0.0504  95  THR I CG2 
18143 N N   . LYS J 99  ? 1.7862 2.9802 2.9423 -0.2962 -0.6637 0.0541  96  LYS I N   
18144 C CA  . LYS J 99  ? 1.8814 3.0529 3.0156 -0.3040 -0.6807 0.0493  96  LYS I CA  
18145 C C   . LYS J 99  ? 1.8320 2.9918 2.9634 -0.3378 -0.6988 0.0449  96  LYS I C   
18146 O O   . LYS J 99  ? 1.7103 2.8570 2.8392 -0.3552 -0.6983 0.0472  96  LYS I O   
18147 C CB  . LYS J 99  ? 1.8973 3.0324 3.0007 -0.2956 -0.6794 0.0522  96  LYS I CB  
18148 C CG  . LYS J 99  ? 1.9581 3.0941 3.0543 -0.2649 -0.6678 0.0543  96  LYS I CG  
18149 C CD  . LYS J 99  ? 1.9028 3.0576 3.0141 -0.2400 -0.6457 0.0601  96  LYS I CD  
18150 C CE  . LYS J 99  ? 1.7960 2.9361 2.8898 -0.2153 -0.6367 0.0621  96  LYS I CE  
18151 N NZ  . LYS J 99  ? 1.9020 3.0529 2.9950 -0.2022 -0.6390 0.0580  96  LYS I NZ  
18152 N N   . HIS J 100 ? 1.6661 2.8299 2.7979 -0.3474 -0.7150 0.0384  97  HIS I N   
18153 C CA  . HIS J 100 ? 1.6431 2.7964 2.7729 -0.3791 -0.7334 0.0335  97  HIS I CA  
18154 C C   . HIS J 100 ? 1.6899 2.7954 2.7818 -0.3928 -0.7488 0.0322  97  HIS I C   
18155 O O   . HIS J 100 ? 1.7655 2.8524 2.8362 -0.3772 -0.7483 0.0333  97  HIS I O   
18156 C CB  . HIS J 100 ? 1.6765 2.8604 2.8289 -0.3838 -0.7442 0.0265  97  HIS I CB  
18157 C CG  . HIS J 100 ? 1.7837 2.9649 2.9256 -0.3693 -0.7522 0.0236  97  HIS I CG  
18158 N ND1 . HIS J 100 ? 1.8126 3.0189 2.9665 -0.3414 -0.7400 0.0242  97  HIS I ND1 
18159 C CD2 . HIS J 100 ? 1.8724 3.0272 2.9921 -0.3798 -0.7717 0.0200  97  HIS I CD2 
18160 C CE1 . HIS J 100 ? 1.9153 3.1112 3.0552 -0.3355 -0.7512 0.0213  97  HIS I CE1 
18161 N NE2 . HIS J 100 ? 1.9549 3.1197 3.0741 -0.3582 -0.7708 0.0190  97  HIS I NE2 
18162 N N   . GLY J 101 ? 1.7541 2.8353 2.8389 -0.4252 -0.7656 0.0340  98  GLY I N   
18163 C CA  . GLY J 101 ? 1.7994 2.8233 2.8524 -0.4486 -0.7925 0.0445  98  GLY I CA  
18164 C C   . GLY J 101 ? 1.8408 2.8551 2.8938 -0.4807 -0.8133 0.0404  98  GLY I C   
18165 O O   . GLY J 101 ? 1.8331 2.8764 2.9123 -0.4916 -0.8092 0.0367  98  GLY I O   
18166 N N   . ARG J 102 ? 2.0345 3.0053 3.0566 -0.4963 -0.8362 0.0410  99  ARG I N   
18167 C CA  . ARG J 102 ? 2.1296 3.0843 3.1458 -0.5263 -0.8583 0.0365  99  ARG I CA  
18168 C C   . ARG J 102 ? 2.1711 3.0498 3.1481 -0.5610 -0.8867 0.0541  99  ARG I C   
18169 O O   . ARG J 102 ? 2.2039 3.0385 3.1463 -0.5599 -0.8982 0.0582  99  ARG I O   
18170 C CB  . ARG J 102 ? 2.2119 3.1921 3.2279 -0.5119 -0.8591 0.0150  99  ARG I CB  
18171 C CG  . ARG J 102 ? 2.2118 3.2584 3.2703 -0.4887 -0.8431 0.0071  99  ARG I CG  
18172 C CD  . ARG J 102 ? 2.3436 3.4008 3.4066 -0.4823 -0.8586 0.0026  99  ARG I CD  
18173 N NE  . ARG J 102 ? 2.3529 3.4663 3.4578 -0.4661 -0.8509 -0.0000 99  ARG I NE  
18174 C CZ  . ARG J 102 ? 2.4183 3.5582 3.5361 -0.4371 -0.8352 0.0023  99  ARG I CZ  
18175 N NH1 . ARG J 102 ? 2.5038 3.6224 3.5985 -0.4189 -0.8243 0.0079  99  ARG I NH1 
18176 N NH2 . ARG J 102 ? 2.4008 3.5892 3.5551 -0.4267 -0.8302 -0.0016 99  ARG I NH2 
18177 N N   . ARG J 103 ? 1.9288 2.7907 2.9089 -0.5925 -0.8974 0.0636  100 ARG I N   
18178 C CA  . ARG J 103 ? 2.0347 2.8222 2.9743 -0.6299 -0.9238 0.0791  100 ARG I CA  
18179 C C   . ARG J 103 ? 2.1541 2.9175 3.0755 -0.6543 -0.9469 0.0704  100 ARG I C   
18180 O O   . ARG J 103 ? 2.1716 2.9649 3.1181 -0.6669 -0.9473 0.0630  100 ARG I O   
18181 C CB  . ARG J 103 ? 2.0083 2.7849 2.9556 -0.6522 -0.9223 0.0956  100 ARG I CB  
18182 C CG  . ARG J 103 ? 2.1829 2.8774 3.0811 -0.6911 -0.9490 0.1095  100 ARG I CG  
18183 C CD  . ARG J 103 ? 2.1805 2.8187 3.0368 -0.6866 -0.9578 0.1174  100 ARG I CD  
18184 N NE  . ARG J 103 ? 2.3929 2.9491 3.1996 -0.7245 -0.9796 0.1312  100 ARG I NE  
18185 C CZ  . ARG J 103 ? 2.5363 3.0322 3.2967 -0.7518 -1.0039 0.1286  100 ARG I CZ  
18186 N NH1 . ARG J 103 ? 2.6174 3.0345 3.3272 -0.7858 -1.0213 0.1396  100 ARG I NH1 
18187 N NH2 . ARG J 103 ? 2.4811 2.9925 3.2429 -0.7449 -1.0106 0.1141  100 ARG I NH2 
18188 N N   . ILE J 104 A 2.0615 2.7702 2.9392 -0.6611 -0.9661 0.0708  100 ILE I N   
18189 C CA  . ILE J 104 A 2.1738 2.8517 3.0279 -0.6829 -0.9898 0.0632  100 ILE I CA  
18190 C C   . ILE J 104 A 2.2670 2.8639 3.0734 -0.7234 -1.0140 0.0778  100 ILE I C   
18191 O O   . ILE J 104 A 2.3029 2.8412 3.0681 -0.7301 -1.0213 0.0895  100 ILE I O   
18192 C CB  . ILE J 104 A 2.2328 2.8985 3.0646 -0.6653 -0.9965 0.0530  100 ILE I CB  
18193 C CG1 . ILE J 104 A 2.1764 2.9198 3.0507 -0.6321 -0.9773 0.0336  100 ILE I CG1 
18194 C CG2 . ILE J 104 A 2.3235 2.9231 3.1088 -0.6949 -1.0274 0.0528  100 ILE I CG2 
18195 C CD1 . ILE J 104 A 2.1289 2.9236 3.0328 -0.5974 -0.9473 0.0327  100 ILE I CD1 
18196 N N   . TYR J 105 B 2.0044 2.5965 2.8142 -0.7508 -1.0260 0.0759  100 TYR I N   
18197 C CA  . TYR J 105 B 2.0852 2.6010 2.8479 -0.7913 -1.0482 0.0877  100 TYR I CA  
18198 C C   . TYR J 105 B 2.1459 2.6304 2.8843 -0.8118 -1.0719 0.0790  100 TYR I C   
18199 O O   . TYR J 105 B 2.2208 2.6263 2.9035 -0.8418 -1.0931 0.0868  100 TYR I O   
18200 C CB  . TYR J 105 B 2.0882 2.6186 2.8733 -0.8111 -1.0404 0.0972  100 TYR I CB  
18201 C CG  . TYR J 105 B 2.0596 2.6631 2.9009 -0.8085 -1.0303 0.0854  100 TYR I CG  
18202 C CD1 . TYR J 105 B 2.1118 2.7028 2.9487 -0.8356 -1.0472 0.0795  100 TYR I CD1 
18203 C CD2 . TYR J 105 B 1.9836 2.6662 2.8805 -0.7798 -1.0037 0.0793  100 TYR I CD2 
18204 C CE1 . TYR J 105 B 2.0876 2.7453 2.9769 -0.8344 -1.0381 0.0673  100 TYR I CE1 
18205 C CE2 . TYR J 105 B 1.9613 2.7078 2.9068 -0.7787 -0.9941 0.0666  100 TYR I CE2 
18206 C CZ  . TYR J 105 B 2.0130 2.7477 2.9558 -0.8063 -1.0115 0.0605  100 TYR I CZ  
18207 O OH  . TYR J 105 B 1.9925 2.7910 2.9847 -0.8061 -1.0022 0.0465  100 TYR I OH  
18208 N N   . GLY J 106 C 2.0482 2.5904 2.8246 -0.7966 -1.0688 0.0624  100 GLY I N   
18209 C CA  . GLY J 106 C 2.1000 2.6231 2.8627 -0.8138 -1.0904 0.0529  100 GLY I CA  
18210 C C   . GLY J 106 C 2.1054 2.6129 2.8455 -0.7976 -1.1008 0.0435  100 GLY I C   
18211 O O   . GLY J 106 C 2.1240 2.5766 2.8179 -0.7950 -1.1073 0.0507  100 GLY I O   
18212 N N   . VAL J 107 D 2.0739 2.6290 2.8457 -0.7875 -1.1023 0.0268  100 VAL I N   
18213 C CA  . VAL J 107 D 2.0833 2.6264 2.8360 -0.7743 -1.1137 0.0170  100 VAL I CA  
18214 C C   . VAL J 107 D 2.0035 2.6263 2.8026 -0.7353 -1.0907 0.0023  100 VAL I C   
18215 O O   . VAL J 107 D 2.0020 2.6372 2.8013 -0.7228 -1.0969 -0.0100 100 VAL I O   
18216 C CB  . VAL J 107 D 2.1452 2.6665 2.8872 -0.7975 -1.1387 0.0095  100 VAL I CB  
18217 C CG1 . VAL J 107 D 2.1746 2.6581 2.8797 -0.7910 -1.1560 0.0043  100 VAL I CG1 
18218 C CG2 . VAL J 107 D 2.2179 2.6738 2.9234 -0.8364 -1.1565 0.0223  100 VAL I CG2 
18219 N N   . VAL J 108 E 1.9165 2.5919 2.7528 -0.7164 -1.0640 0.0034  100 VAL I N   
18220 C CA  . VAL J 108 E 1.8392 2.5877 2.7148 -0.6786 -1.0385 -0.0097 100 VAL I CA  
18221 C C   . VAL J 108 E 1.8288 2.6357 2.7447 -0.6731 -1.0394 -0.0274 100 VAL I C   
18222 O O   . VAL J 108 E 1.7918 2.6602 2.7574 -0.6633 -1.0265 -0.0289 100 VAL I O   
18223 C CB  . VAL J 108 E 1.8256 2.5495 2.6700 -0.6569 -1.0376 -0.0087 100 VAL I CB  
18224 C CG1 . VAL J 108 E 1.7510 2.5448 2.6332 -0.6198 -1.0123 -0.0183 100 VAL I CG1 
18225 C CG2 . VAL J 108 E 1.8475 2.5067 2.6503 -0.6663 -1.0421 0.0105  100 VAL I CG2 
18226 N N   . ALA J 109 F 1.8191 2.5951 2.7148 -0.6854 -1.0658 -0.0302 100 ALA I N   
18227 C CA  . ALA J 109 F 1.8330 2.6480 2.7662 -0.6861 -1.0817 -0.0356 100 ALA I CA  
18228 C C   . ALA J 109 F 1.8394 2.6939 2.8139 -0.7044 -1.0807 -0.0406 100 ALA I C   
18229 O O   . ALA J 109 F 1.8285 2.7376 2.8499 -0.6989 -1.0835 -0.0459 100 ALA I O   
18230 C CB  . ALA J 109 F 1.8944 2.6589 2.7920 -0.6987 -1.1119 -0.0371 100 ALA I CB  
18231 N N   . PHE J 110 G 1.8738 2.7010 2.8317 -0.7269 -1.0769 -0.0398 100 PHE I N   
18232 C CA  . PHE J 110 G 1.8828 2.7444 2.8783 -0.7463 -1.0757 -0.0446 100 PHE I CA  
18233 C C   . PHE J 110 G 1.8266 2.7371 2.8579 -0.7355 -1.0468 -0.0431 100 PHE I C   
18234 O O   . PHE J 110 G 1.8341 2.7579 2.8840 -0.7546 -1.0410 -0.0452 100 PHE I O   
18235 C CB  . PHE J 110 G 1.9463 2.7472 2.9057 -0.7811 -1.0919 -0.0410 100 PHE I CB  
18236 C CG  . PHE J 110 G 2.0036 2.7773 2.9461 -0.7969 -1.1192 -0.0488 100 PHE I CG  
18237 C CD1 . PHE J 110 G 2.0274 2.8365 3.0092 -0.8121 -1.1324 -0.0560 100 PHE I CD1 
18238 C CD2 . PHE J 110 G 2.0505 2.7515 2.9363 -0.8021 -1.1403 -0.0408 100 PHE I CD2 
18239 C CE1 . PHE J 110 G 2.0878 2.8663 3.0538 -0.8285 -1.1621 -0.0595 100 PHE I CE1 
18240 C CE2 . PHE J 110 G 2.1069 2.7781 2.9739 -0.8169 -1.1663 -0.0470 100 PHE I CE2 
18241 C CZ  . PHE J 110 G 2.1266 2.8359 3.0344 -0.8302 -1.1785 -0.0553 100 PHE I CZ  
18242 N N   . LYS J 111 H 1.9702 2.9062 3.0110 -0.7055 -1.0289 -0.0393 100 LYS I N   
18243 C CA  . LYS J 111 H 1.9155 2.8957 2.9878 -0.6918 -1.0012 -0.0370 100 LYS I CA  
18244 C C   . LYS J 111 H 1.9256 2.8698 2.9763 -0.7105 -0.9929 -0.0287 100 LYS I C   
18245 O O   . LYS J 111 H 1.9029 2.8780 2.9828 -0.7136 -0.9773 -0.0257 100 LYS I O   
18246 C CB  . LYS J 111 H 1.9016 2.9504 3.0330 -0.6923 -0.9976 -0.0440 100 LYS I CB  
18247 C CG  . LYS J 111 H 1.8897 2.9771 3.0470 -0.6721 -1.0051 -0.0485 100 LYS I CG  
18248 C CD  . LYS J 111 H 1.8985 3.0536 3.1138 -0.6739 -1.0008 -0.0571 100 LYS I CD  
18249 C CE  . LYS J 111 H 1.9350 3.1278 3.1750 -0.6536 -1.0079 -0.0621 100 LYS I CE  
18250 N NZ  . LYS J 111 H 1.9742 3.2376 3.2714 -0.6506 -0.9984 -0.0709 100 LYS I NZ  
18251 N N   . GLU J 112 I 1.8445 2.7111 2.8440 -0.7296 -1.0146 -0.0130 100 GLU I N   
18252 C CA  . GLU J 112 I 1.8832 2.6932 2.8543 -0.7565 -1.0220 0.0089  100 GLU I CA  
18253 C C   . GLU J 112 I 1.8434 2.6443 2.8034 -0.7370 -1.0056 0.0221  100 GLU I C   
18254 O O   . GLU J 112 I 1.8738 2.6101 2.7876 -0.7452 -1.0168 0.0367  100 GLU I O   
18255 C CB  . GLU J 112 I 1.9643 2.6927 2.8812 -0.7865 -1.0531 0.0172  100 GLU I CB  
18256 C CG  . GLU J 112 I 2.0082 2.7435 2.9374 -0.8092 -1.0700 0.0060  100 GLU I CG  
18257 C CD  . GLU J 112 I 2.0918 2.7433 2.9639 -0.8382 -1.1010 0.0135  100 GLU I CD  
18258 O OE1 . GLU J 112 I 2.1116 2.7056 2.9351 -0.8347 -1.1099 0.0222  100 GLU I OE1 
18259 O OE2 . GLU J 112 I 2.1393 2.7817 3.0141 -0.8644 -1.1163 0.0098  100 GLU I OE2 
18260 N N   . TRP J 113 J 2.1770 3.0444 3.1802 -0.7107 -0.9784 0.0156  100 TRP I N   
18261 C CA  . TRP J 113 J 2.0996 2.9719 3.1022 -0.6880 -0.9593 0.0258  100 TRP I CA  
18262 C C   . TRP J 113 J 1.9943 2.9321 3.0454 -0.6746 -0.9331 0.0217  100 TRP I C   
18263 O O   . TRP J 113 J 2.0327 3.0138 3.1179 -0.6814 -0.9293 0.0092  100 TRP I O   
18264 C CB  . TRP J 113 J 2.0814 2.9608 3.0726 -0.6547 -0.9526 0.0176  100 TRP I CB  
18265 C CG  . TRP J 113 J 2.1288 3.0777 3.1549 -0.6274 -0.9380 -0.0064 100 TRP I CG  
18266 C CD1 . TRP J 113 J 2.1695 3.1653 3.2323 -0.6338 -0.9380 -0.0198 100 TRP I CD1 
18267 C CD2 . TRP J 113 J 2.1646 3.1386 3.1936 -0.5935 -0.9268 -0.0126 100 TRP I CD2 
18268 N NE1 . TRP J 113 J 2.2096 3.2469 3.2997 -0.6124 -0.9390 -0.0224 100 TRP I NE1 
18269 C CE2 . TRP J 113 J 2.2005 3.2243 3.2699 -0.5875 -0.9320 -0.0177 100 TRP I CE2 
18270 C CE3 . TRP J 113 J 2.1946 3.1478 3.1978 -0.5718 -0.9189 -0.0081 100 TRP I CE3 
18271 C CZ2 . TRP J 113 J 2.2605 3.3111 3.3430 -0.5611 -0.9296 -0.0179 100 TRP I CZ2 
18272 C CZ3 . TRP J 113 J 2.2229 3.2032 3.2397 -0.5457 -0.9164 -0.0079 100 TRP I CZ3 
18273 C CH2 . TRP J 113 J 2.2593 3.2865 3.3144 -0.5406 -0.9217 -0.0126 100 TRP I CH2 
18274 N N   . PHE J 114 K 2.0649 3.0088 3.1186 -0.6556 -0.9151 0.0320  100 PHE I N   
18275 C CA  . PHE J 114 K 1.9731 2.9753 3.0686 -0.6396 -0.8892 0.0287  100 PHE I CA  
18276 C C   . PHE J 114 K 1.8523 2.8659 2.9464 -0.6053 -0.8692 0.0327  100 PHE I C   
18277 O O   . PHE J 114 K 1.8250 2.7909 2.8862 -0.6046 -0.8769 0.0465  100 PHE I O   
18278 C CB  . PHE J 114 K 1.9723 2.9612 3.0752 -0.6696 -0.8908 0.0450  100 PHE I CB  
18279 C CG  . PHE J 114 K 1.9134 2.8432 2.9826 -0.6832 -0.8978 0.0701  100 PHE I CG  
18280 C CD1 . PHE J 114 K 1.9765 2.8341 3.0005 -0.7137 -0.9238 0.0821  100 PHE I CD1 
18281 C CD2 . PHE J 114 K 1.7880 2.7338 2.8702 -0.6658 -0.8782 0.0810  100 PHE I CD2 
18282 C CE1 . PHE J 114 K 1.9465 2.7487 2.9380 -0.7267 -0.9299 0.1031  100 PHE I CE1 
18283 C CE2 . PHE J 114 K 1.7979 2.6917 2.8516 -0.6780 -0.8847 0.1032  100 PHE I CE2 
18284 C CZ  . PHE J 114 K 1.8673 2.6892 2.8756 -0.7088 -0.9105 0.1137  100 PHE I CZ  
18285 N N   . THR J 115 L 1.7208 2.7967 2.8497 -0.5770 -0.8435 0.0194  100 THR I N   
18286 C CA  . THR J 115 L 1.6654 2.7582 2.7954 -0.5418 -0.8218 0.0203  100 THR I CA  
18287 C C   . THR J 115 L 1.6499 2.7436 2.7923 -0.5439 -0.8090 0.0378  100 THR I C   
18288 O O   . THR J 115 L 1.6486 2.7705 2.8186 -0.5550 -0.8020 0.0368  100 THR I O   
18289 C CB  . THR J 115 L 1.6272 2.7770 2.7871 -0.5142 -0.8095 0.0066  100 THR I CB  
18290 O OG1 . THR J 115 L 1.6323 2.8225 2.8303 -0.5265 -0.8077 0.0019  100 THR I OG1 
18291 C CG2 . THR J 115 L 1.6501 2.7910 2.7986 -0.5124 -0.8287 0.0017  100 THR I CG2 
18292 N N   . TYR J 116 M 1.7727 2.8356 2.8954 -0.5338 -0.8066 0.0539  100 TYR I N   
18293 C CA  . TYR J 116 M 1.7420 2.8033 2.8744 -0.5329 -0.7949 0.0718  100 TYR I CA  
18294 C C   . TYR J 116 M 1.6786 2.7709 2.8199 -0.4905 -0.7693 0.0660  100 TYR I C   
18295 O O   . TYR J 116 M 1.6611 2.7479 2.7853 -0.4686 -0.7674 0.0582  100 TYR I O   
18296 C CB  . TYR J 116 M 1.7890 2.7840 2.8909 -0.5602 -0.8149 0.0968  100 TYR I CB  
18297 C CG  . TYR J 116 M 1.7953 2.7493 2.8640 -0.5503 -0.8246 0.1002  100 TYR I CG  
18298 C CD1 . TYR J 116 M 1.8371 2.7563 2.8772 -0.5650 -0.8463 0.0941  100 TYR I CD1 
18299 C CD2 . TYR J 116 M 1.7621 2.7104 2.8278 -0.5270 -0.8128 0.1098  100 TYR I CD2 
18300 C CE1 . TYR J 116 M 1.8479 2.7272 2.8561 -0.5576 -0.8555 0.0971  100 TYR I CE1 
18301 C CE2 . TYR J 116 M 1.7689 2.6802 2.8059 -0.5190 -0.8216 0.1124  100 TYR I CE2 
18302 C CZ  . TYR J 116 M 1.8115 2.6878 2.8189 -0.5350 -0.8430 0.1060  100 TYR I CZ  
18303 O OH  . TYR J 116 M 1.8348 2.6719 2.8116 -0.5285 -0.8522 0.1083  100 TYR I OH  
18304 N N   . PHE J 117 N 1.6782 2.8005 2.8438 -0.4797 -0.7500 0.0698  100 PHE I N   
18305 C CA  . PHE J 117 N 1.6209 2.7707 2.7939 -0.4407 -0.7248 0.0644  100 PHE I CA  
18306 C C   . PHE J 117 N 1.6170 2.7411 2.7865 -0.4404 -0.7217 0.0892  100 PHE I C   
18307 O O   . PHE J 117 N 1.6493 2.7518 2.8222 -0.4691 -0.7322 0.1083  100 PHE I O   
18308 C CB  . PHE J 117 N 1.5840 2.7908 2.7865 -0.4234 -0.7030 0.0453  100 PHE I CB  
18309 C CG  . PHE J 117 N 1.5958 2.8285 2.8124 -0.4239 -0.7130 0.0338  100 PHE I CG  
18310 C CD1 . PHE J 117 N 1.5786 2.8226 2.7944 -0.3988 -0.7124 0.0320  100 PHE I CD1 
18311 C CD2 . PHE J 117 N 1.6281 2.8727 2.8605 -0.4510 -0.7251 0.0273  100 PHE I CD2 
18312 C CE1 . PHE J 117 N 1.5929 2.8598 2.8234 -0.4003 -0.7239 0.0241  100 PHE I CE1 
18313 C CE2 . PHE J 117 N 1.6713 2.9406 2.9201 -0.4519 -0.7367 0.0189  100 PHE I CE2 
18314 C CZ  . PHE J 117 N 1.6752 2.9555 2.9228 -0.4264 -0.7364 0.0174  100 PHE I CZ  
18315 N N   . TYR J 118 O 1.7871 2.9148 2.9501 -0.4073 -0.7065 0.0880  100 TYR I N   
18316 C CA  . TYR J 118 O 1.7410 2.8485 2.9041 -0.4021 -0.7019 0.1097  100 TYR I CA  
18317 C C   . TYR J 118 O 1.7526 2.8880 2.9198 -0.3588 -0.6751 0.1000  100 TYR I C   
18318 O O   . TYR J 118 O 1.7451 2.8908 2.8994 -0.3347 -0.6672 0.0823  100 TYR I O   
18319 C CB  . TYR J 118 O 1.7820 2.8332 2.9198 -0.4196 -0.7242 0.1269  100 TYR I CB  
18320 C CG  . TYR J 118 O 1.8707 2.9080 2.9854 -0.4022 -0.7273 0.1161  100 TYR I CG  
18321 C CD1 . TYR J 118 O 1.9344 2.9723 3.0363 -0.4097 -0.7381 0.0998  100 TYR I CD1 
18322 C CD2 . TYR J 118 O 1.8391 2.8622 2.9452 -0.3790 -0.7200 0.1226  100 TYR I CD2 
18323 C CE1 . TYR J 118 O 1.9519 2.9757 3.0313 -0.3953 -0.7414 0.0912  100 TYR I CE1 
18324 C CE2 . TYR J 118 O 1.8612 2.8709 2.9457 -0.3650 -0.7227 0.1135  100 TYR I CE2 
18325 C CZ  . TYR J 118 O 1.8845 2.8941 2.9547 -0.3737 -0.7335 0.0982  100 TYR I CZ  
18326 O OH  . TYR J 118 O 1.8287 2.8229 2.8759 -0.3615 -0.7371 0.0905  100 TYR I OH  
18327 N N   . MET J 119 P 1.8494 2.9952 3.0324 -0.3500 -0.6613 0.1112  100 MET I N   
18328 C CA  . MET J 119 P 1.7600 2.9283 2.9447 -0.3100 -0.6355 0.1027  100 MET I CA  
18329 C C   . MET J 119 P 1.7573 2.8939 2.9300 -0.2974 -0.6366 0.1187  100 MET I C   
18330 O O   . MET J 119 P 1.7979 2.9039 2.9746 -0.3176 -0.6506 0.1430  100 MET I O   
18331 C CB  . MET J 119 P 1.6907 2.8852 2.8978 -0.3055 -0.6200 0.1060  100 MET I CB  
18332 C CG  . MET J 119 P 1.6770 2.9087 2.8992 -0.3110 -0.6141 0.0860  100 MET I CG  
18333 S SD  . MET J 119 P 1.7019 2.9220 2.9305 -0.3587 -0.6408 0.0920  100 MET I SD  
18334 C CE  . MET J 119 P 1.7357 2.9267 2.9732 -0.3897 -0.6519 0.1276  100 MET I CE  
18335 N N   . ASP J 120 Q 1.8659 3.0095 3.0239 -0.2646 -0.6220 0.1044  100 ASP I N   
18336 C CA  . ASP J 120 Q 1.8684 2.9854 3.0160 -0.2494 -0.6210 0.1162  100 ASP I CA  
18337 C C   . ASP J 120 Q 1.8354 2.9697 2.9865 -0.2138 -0.5948 0.1130  100 ASP I C   
18338 O O   . ASP J 120 Q 1.8349 2.9495 2.9914 -0.2075 -0.5940 0.1311  100 ASP I O   
18339 C CB  . ASP J 120 Q 1.8976 3.0021 3.0213 -0.2416 -0.6264 0.1042  100 ASP I CB  
18340 C CG  . ASP J 120 Q 1.8904 3.0289 3.0050 -0.2159 -0.6086 0.0777  100 ASP I CG  
18341 O OD1 . ASP J 120 Q 1.9024 3.0669 3.0373 -0.2219 -0.6089 0.0764  100 ASP I OD1 
18342 O OD2 . ASP J 120 Q 1.8985 3.0298 3.0007 -0.1978 -0.6058 0.0765  100 ASP I OD2 
18343 N N   . VAL J 121 R 1.9518 3.1194 3.1013 -0.1917 -0.5755 0.0920  100 VAL I N   
18344 C CA  . VAL J 121 R 1.9595 3.1373 3.1165 -0.1627 -0.5571 0.0972  100 VAL I CA  
18345 C C   . VAL J 121 R 1.9107 3.1126 3.0902 -0.1673 -0.5506 0.1003  100 VAL I C   
18346 O O   . VAL J 121 R 1.9177 3.1428 3.1111 -0.1734 -0.5538 0.0958  100 VAL I O   
18347 C CB  . VAL J 121 R 1.9916 3.1762 3.1440 -0.1423 -0.5532 0.0931  100 VAL I CB  
18348 C CG1 . VAL J 121 R 1.9581 3.1499 3.1158 -0.1140 -0.5344 0.0977  100 VAL I CG1 
18349 C CG2 . VAL J 121 R 2.0124 3.1737 3.1423 -0.1404 -0.5606 0.0898  100 VAL I CG2 
18350 N N   . TRP J 122 ? 1.8497 3.0466 3.0335 -0.1650 -0.5421 0.1076  101 TRP I N   
18351 C CA  . TRP J 122 ? 1.8319 3.0494 3.0358 -0.1700 -0.5355 0.1116  101 TRP I CA  
18352 C C   . TRP J 122 ? 1.8271 3.0537 3.0361 -0.1409 -0.5186 0.1159  101 TRP I C   
18353 O O   . TRP J 122 ? 1.8678 3.0833 3.0648 -0.1176 -0.5116 0.1160  101 TRP I O   
18354 C CB  . TRP J 122 ? 1.8215 3.0246 3.0384 -0.1919 -0.5437 0.1327  101 TRP I CB  
18355 C CG  . TRP J 122 ? 1.8904 3.0807 3.1150 -0.2310 -0.5683 0.1448  101 TRP I CG  
18356 C CD1 . TRP J 122 ? 1.9143 3.0784 3.1276 -0.2448 -0.5864 0.1497  101 TRP I CD1 
18357 C CD2 . TRP J 122 ? 1.9292 3.1311 3.1708 -0.2627 -0.5779 0.1505  101 TRP I CD2 
18358 N NE1 . TRP J 122 ? 2.0023 3.1572 3.2223 -0.2840 -0.6077 0.1587  101 TRP I NE1 
18359 C CE2 . TRP J 122 ? 2.0089 3.1879 3.2465 -0.2956 -0.6022 0.1591  101 TRP I CE2 
18360 C CE3 . TRP J 122 ? 1.8713 3.0990 3.1301 -0.2678 -0.5685 0.1493  101 TRP I CE3 
18361 C CZ2 . TRP J 122 ? 2.0462 3.2273 3.2950 -0.3329 -0.6165 0.1656  101 TRP I CZ2 
18362 C CZ3 . TRP J 122 ? 1.8873 3.1199 3.1603 -0.3048 -0.5822 0.1567  101 TRP I CZ3 
18363 C CH2 . TRP J 122 ? 1.9885 3.1979 3.2558 -0.3369 -0.6056 0.1644  101 TRP I CH2 
18364 N N   . GLY J 123 ? 1.9280 3.1743 3.1546 -0.1436 -0.5120 0.1191  102 GLY I N   
18365 C CA  . GLY J 123 ? 1.9172 3.1698 3.1479 -0.1191 -0.4967 0.1236  102 GLY I CA  
18366 C C   . GLY J 123 ? 1.8992 3.1441 3.1331 -0.1169 -0.4886 0.1335  102 GLY I C   
18367 O O   . GLY J 123 ? 1.8821 3.1183 3.1162 -0.1352 -0.4950 0.1365  102 GLY I O   
18368 N N   . LYS J 124 ? 1.9294 3.1761 3.1648 -0.0944 -0.4750 0.1385  103 LYS I N   
18369 C CA  . LYS J 124 ? 1.9460 3.1852 3.1844 -0.0898 -0.4673 0.1484  103 LYS I CA  
18370 C C   . LYS J 124 ? 1.9274 3.1853 3.1834 -0.1143 -0.4704 0.1510  103 LYS I C   
18371 O O   . LYS J 124 ? 1.9379 3.1872 3.1963 -0.1243 -0.4714 0.1588  103 LYS I O   
18372 C CB  . LYS J 124 ? 1.9942 3.2282 3.2279 -0.0602 -0.4527 0.1526  103 LYS I CB  
18373 C CG  . LYS J 124 ? 1.9944 3.2062 3.2100 -0.0383 -0.4492 0.1504  103 LYS I CG  
18374 C CD  . LYS J 124 ? 2.0184 3.2227 3.2276 -0.0102 -0.4351 0.1530  103 LYS I CD  
18375 C CE  . LYS J 124 ? 2.0330 3.2304 3.2462 -0.0026 -0.4273 0.1632  103 LYS I CE  
18376 N NZ  . LYS J 124 ? 2.0941 3.2713 3.3021 -0.0026 -0.4303 0.1681  103 LYS I NZ  
18377 N N   . GLY J 125 ? 1.8895 3.1733 3.1596 -0.1249 -0.4722 0.1455  104 GLY I N   
18378 C CA  . GLY J 125 ? 1.9021 3.2056 3.1904 -0.1497 -0.4746 0.1468  104 GLY I CA  
18379 C C   . GLY J 125 ? 1.8993 3.2174 3.1988 -0.1406 -0.4627 0.1528  104 GLY I C   
18380 O O   . GLY J 125 ? 1.8855 3.1917 3.1766 -0.1160 -0.4525 0.1589  104 GLY I O   
18381 N N   . THR J 126 ? 1.8708 3.2150 3.1899 -0.1614 -0.4642 0.1505  105 THR I N   
18382 C CA  . THR J 126 ? 1.9151 3.2767 3.2474 -0.1588 -0.4543 0.1555  105 THR I CA  
18383 C C   . THR J 126 ? 1.8834 3.2517 3.2276 -0.1867 -0.4561 0.1605  105 THR I C   
18384 O O   . THR J 126 ? 1.8482 3.2173 3.1963 -0.2130 -0.4660 0.1562  105 THR I O   
18385 C CB  . THR J 126 ? 1.9435 3.3341 3.2909 -0.1578 -0.4531 0.1466  105 THR I CB  
18386 O OG1 . THR J 126 ? 1.9850 3.3930 3.3456 -0.1570 -0.4435 0.1514  105 THR I OG1 
18387 C CG2 . THR J 126 ? 1.9114 3.3206 3.2731 -0.1849 -0.4650 0.1365  105 THR I CG2 
18388 N N   . SER J 127 ? 1.8287 3.2004 3.1776 -0.1822 -0.4465 0.1694  106 SER I N   
18389 C CA  . SER J 127 ? 1.8212 3.1997 3.1845 -0.2104 -0.4485 0.1823  106 SER I CA  
18390 C C   . SER J 127 ? 1.8977 3.3086 3.2800 -0.2240 -0.4422 0.1718  106 SER I C   
18391 O O   . SER J 127 ? 1.9221 3.3460 3.3091 -0.2062 -0.4337 0.1727  106 SER I O   
18392 C CB  . SER J 127 ? 1.8203 3.1819 3.1831 -0.2010 -0.4462 0.2114  106 SER I CB  
18393 O OG  . SER J 127 ? 1.8682 3.2380 3.2532 -0.2355 -0.4542 0.2427  106 SER I OG  
18394 N N   . VAL J 128 ? 1.7443 3.1709 3.1455 -0.2614 -0.4510 0.1774  107 VAL I N   
18395 C CA  . VAL J 128 ? 1.7817 3.2400 3.2038 -0.2778 -0.4447 0.1656  107 VAL I CA  
18396 C C   . VAL J 128 ? 1.8405 3.3067 3.2814 -0.3184 -0.4511 0.1995  107 VAL I C   
18397 O O   . VAL J 128 ? 1.8703 3.3283 3.3155 -0.3508 -0.4658 0.2167  107 VAL I O   
18398 C CB  . VAL J 128 ? 1.8013 3.2801 3.2368 -0.2901 -0.4525 0.1487  107 VAL I CB  
18399 C CG1 . VAL J 128 ? 1.8547 3.3682 3.3184 -0.3120 -0.4483 0.1435  107 VAL I CG1 
18400 C CG2 . VAL J 128 ? 1.7734 3.2539 3.2026 -0.2604 -0.4537 0.1424  107 VAL I CG2 
18401 N N   . THR J 129 ? 1.7798 3.2598 3.2298 -0.3183 -0.4407 0.2089  108 THR I N   
18402 C CA  . THR J 129 ? 1.8430 3.3320 3.3087 -0.3569 -0.4445 0.2406  108 THR I CA  
18403 C C   . THR J 129 ? 1.8905 3.4149 3.3770 -0.3719 -0.4343 0.2245  108 THR I C   
18404 O O   . THR J 129 ? 1.8772 3.4143 3.3649 -0.3449 -0.4207 0.2032  108 THR I O   
18405 C CB  . THR J 129 ? 1.8430 3.3172 3.3027 -0.3465 -0.4419 0.2705  108 THR I CB  
18406 O OG1 . THR J 129 ? 1.8061 3.2473 3.2498 -0.3280 -0.4505 0.2820  108 THR I OG1 
18407 C CG2 . THR J 129 ? 1.8836 3.3634 3.3568 -0.3906 -0.4482 0.3049  108 THR I CG2 
18408 N N   . VAL J 130 ? 1.7676 3.3054 3.2699 -0.4155 -0.4409 0.2336  109 VAL I N   
18409 C CA  . VAL J 130 ? 1.8257 3.3978 3.3512 -0.4340 -0.4314 0.2192  109 VAL I CA  
18410 C C   . VAL J 130 ? 1.8911 3.4715 3.4232 -0.4621 -0.4268 0.2507  109 VAL I C   
18411 O O   . VAL J 130 ? 1.9404 3.5094 3.4701 -0.5008 -0.4369 0.2789  109 VAL I O   
18412 C CB  . VAL J 130 ? 1.8782 3.4614 3.4177 -0.4642 -0.4400 0.2048  109 VAL I CB  
18413 C CG1 . VAL J 130 ? 1.9891 3.6080 3.5565 -0.4841 -0.4295 0.1910  109 VAL I CG1 
18414 C CG2 . VAL J 130 ? 1.8561 3.4325 3.3889 -0.4364 -0.4448 0.1734  109 VAL I CG2 
18415 N N   . SER J 131 ? 1.8949 3.4927 3.4333 -0.4444 -0.4120 0.2454  110 SER I N   
18416 C CA  . SER J 131 ? 1.9817 3.5901 3.5257 -0.4693 -0.4061 0.2739  110 SER I CA  
18417 C C   . SER J 131 ? 2.0725 3.7103 3.6317 -0.4555 -0.3889 0.2543  110 SER I C   
18418 O O   . SER J 131 ? 2.0355 3.6737 3.5923 -0.4155 -0.3821 0.2257  110 SER I O   
18419 C CB  . SER J 131 ? 1.9559 3.5376 3.4818 -0.4575 -0.4106 0.3071  110 SER I CB  
18420 O OG  . SER J 131 ? 2.0143 3.6060 3.5450 -0.4842 -0.4058 0.3353  110 SER I OG  
18421 N N   . SER J 132 ? 1.9887 3.6486 3.5619 -0.4907 -0.3820 0.2689  111 SER I N   
18422 C CA  . SER J 132 ? 2.1031 3.7921 3.6932 -0.4832 -0.3657 0.2530  111 SER I CA  
18423 C C   . SER J 132 ? 2.1087 3.7923 3.6863 -0.4616 -0.3581 0.2716  111 SER I C   
18424 O O   . SER J 132 ? 2.1010 3.8069 3.6902 -0.4580 -0.3447 0.2639  111 SER I O   
18425 C CB  . SER J 132 ? 2.2808 3.9974 3.8922 -0.5318 -0.3598 0.2586  111 SER I CB  
18426 O OG  . SER J 132 ? 2.4102 4.1156 4.0087 -0.5709 -0.3644 0.2984  111 SER I OG  
18427 N N   . ALA J 133 ? 2.2399 3.8939 3.7956 -0.4470 -0.3669 0.2956  112 ALA I N   
18428 C CA  . ALA J 133 ? 2.2384 3.8836 3.7822 -0.4246 -0.3620 0.3149  112 ALA I CA  
18429 C C   . ALA J 133 ? 2.1794 3.8127 3.7117 -0.3707 -0.3561 0.2853  112 ALA I C   
18430 O O   . ALA J 133 ? 2.1068 3.7281 3.6335 -0.3494 -0.3598 0.2575  112 ALA I O   
18431 C CB  . ALA J 133 ? 2.1588 3.7749 3.6879 -0.4332 -0.3753 0.3539  112 ALA I CB  
18432 N N   . SER J 134 ? 2.4768 4.1112 4.0033 -0.3505 -0.3470 0.2911  113 SER I N   
18433 C CA  . SER J 134 ? 2.3748 3.9933 3.8863 -0.3021 -0.3409 0.2623  113 SER I CA  
18434 C C   . SER J 134 ? 2.2976 3.8779 3.7837 -0.2715 -0.3488 0.2699  113 SER I C   
18435 O O   . SER J 134 ? 2.3084 3.8747 3.7911 -0.2848 -0.3591 0.3022  113 SER I O   
18436 C CB  . SER J 134 ? 2.3560 3.9867 3.8689 -0.2919 -0.3287 0.2648  113 SER I CB  
18437 O OG  . SER J 134 ? 2.1873 3.8100 3.6915 -0.2544 -0.3229 0.2335  113 SER I OG  
18438 N N   . THR J 135 ? 2.4939 4.0554 3.9622 -0.2307 -0.3438 0.2377  114 THR I N   
18439 C CA  . THR J 135 ? 2.3950 3.9216 3.8377 -0.1973 -0.3484 0.2402  114 THR I CA  
18440 C C   . THR J 135 ? 2.3996 3.9094 3.8270 -0.1741 -0.3428 0.2533  114 THR I C   
18441 O O   . THR J 135 ? 2.4559 3.9826 3.8891 -0.1698 -0.3350 0.2549  114 THR I O   
18442 C CB  . THR J 135 ? 2.3013 3.8310 3.7421 -0.1774 -0.3512 0.2287  114 THR I CB  
18443 O OG1 . THR J 135 ? 2.2920 3.8392 3.7490 -0.1995 -0.3573 0.2162  114 THR I OG1 
18444 C CG2 . THR J 135 ? 2.1799 3.6739 3.5959 -0.1489 -0.3558 0.2319  114 THR I CG2 
18445 N N   . LYS J 136 ? 2.4563 3.9385 3.8702 -0.1625 -0.3495 0.2754  115 LYS I N   
18446 C CA  . LYS J 136 ? 2.4128 3.8764 3.8131 -0.1395 -0.3463 0.2916  115 LYS I CA  
18447 C C   . LYS J 136 ? 2.3335 3.7580 3.7044 -0.0990 -0.3457 0.2757  115 LYS I C   
18448 O O   . LYS J 136 ? 2.2710 3.6761 3.6338 -0.0938 -0.3524 0.2731  115 LYS I O   
18449 C CB  . LYS J 136 ? 2.4089 3.8718 3.8230 -0.1605 -0.3564 0.3412  115 LYS I CB  
18450 C CG  . LYS J 136 ? 2.4253 3.8729 3.8292 -0.1377 -0.3531 0.3580  115 LYS I CG  
18451 C CD  . LYS J 136 ? 2.3907 3.8332 3.8089 -0.1545 -0.3648 0.4068  115 LYS I CD  
18452 C CE  . LYS J 136 ? 2.4041 3.8339 3.8119 -0.1294 -0.3602 0.4176  115 LYS I CE  
18453 N NZ  . LYS J 136 ? 2.4245 3.8228 3.8323 -0.1169 -0.3722 0.4495  115 LYS I NZ  
18454 N N   . GLY J 137 ? 2.3471 3.7662 3.7086 -0.0755 -0.3394 0.2792  116 GLY I N   
18455 C CA  . GLY J 137 ? 2.3046 3.6925 3.6450 -0.0431 -0.3393 0.2798  116 GLY I CA  
18456 C C   . GLY J 137 ? 2.3120 3.6686 3.6392 -0.0314 -0.3429 0.2915  116 GLY I C   
18457 O O   . GLY J 137 ? 2.3637 3.7231 3.6954 -0.0381 -0.3428 0.3059  116 GLY I O   
18458 N N   . PRO J 138 ? 2.3376 3.6655 3.6510 -0.0144 -0.3471 0.2897  117 PRO I N   
18459 C CA  . PRO J 138 ? 2.3059 3.6024 3.6081 -0.0006 -0.3517 0.3016  117 PRO I CA  
18460 C C   . PRO J 138 ? 2.3681 3.6434 3.6546 0.0267  -0.3462 0.3075  117 PRO I C   
18461 O O   . PRO J 138 ? 2.3967 3.6756 3.6782 0.0387  -0.3390 0.3036  117 PRO I O   
18462 C CB  . PRO J 138 ? 2.2048 3.4792 3.4965 0.0105  -0.3560 0.2929  117 PRO I CB  
18463 C CG  . PRO J 138 ? 2.1879 3.4742 3.4794 0.0143  -0.3514 0.2810  117 PRO I CG  
18464 C CD  . PRO J 138 ? 2.2593 3.5832 3.5687 -0.0086 -0.3487 0.2779  117 PRO I CD  
18465 N N   . SER J 139 ? 2.4103 3.6676 3.7000 0.0321  -0.3524 0.3333  118 SER I N   
18466 C CA  . SER J 139 ? 2.4838 3.7130 3.7524 0.0610  -0.3482 0.3325  118 SER I CA  
18467 C C   . SER J 139 ? 2.5023 3.6939 3.7603 0.0821  -0.3536 0.3382  118 SER I C   
18468 O O   . SER J 139 ? 2.5660 3.7525 3.8484 0.0715  -0.3657 0.3747  118 SER I O   
18469 C CB  . SER J 139 ? 2.5583 3.8022 3.8479 0.0477  -0.3523 0.3692  118 SER I CB  
18470 O OG  . SER J 139 ? 2.6509 3.9031 3.9733 0.0233  -0.3668 0.4131  118 SER I OG  
18471 N N   . VAL J 140 ? 2.5684 3.7385 3.8047 0.1065  -0.3467 0.3191  119 VAL I N   
18472 C CA  . VAL J 140 ? 2.5527 3.6878 3.7754 0.1280  -0.3489 0.3167  119 VAL I CA  
18473 C C   . VAL J 140 ? 2.6533 3.7557 3.8614 0.1531  -0.3487 0.3247  119 VAL I C   
18474 O O   . VAL J 140 ? 2.6565 3.7577 3.8587 0.1627  -0.3423 0.3260  119 VAL I O   
18475 C CB  . VAL J 140 ? 2.4493 3.5829 3.6664 0.1359  -0.3426 0.3036  119 VAL I CB  
18476 C CG1 . VAL J 140 ? 2.4470 3.5478 3.6523 0.1553  -0.3443 0.3002  119 VAL I CG1 
18477 C CG2 . VAL J 140 ? 2.3919 3.5567 3.6225 0.1119  -0.3440 0.2956  119 VAL I CG2 
18478 N N   . PHE J 141 ? 2.5354 3.6113 3.7424 0.1628  -0.3570 0.3358  120 PHE I N   
18479 C CA  . PHE J 141 ? 2.6194 3.6596 3.8117 0.1887  -0.3580 0.3430  120 PHE I CA  
18480 C C   . PHE J 141 ? 2.6144 3.6188 3.7908 0.2122  -0.3583 0.3337  120 PHE I C   
18481 O O   . PHE J 141 ? 2.5599 3.5629 3.7584 0.2026  -0.3661 0.3497  120 PHE I O   
18482 C CB  . PHE J 141 ? 2.7040 3.7476 3.9305 0.1741  -0.3710 0.3904  120 PHE I CB  
18483 C CG  . PHE J 141 ? 2.7270 3.8088 3.9682 0.1506  -0.3695 0.4003  120 PHE I CG  
18484 C CD1 . PHE J 141 ? 2.7266 3.8065 3.9465 0.1634  -0.3613 0.3865  120 PHE I CD1 
18485 C CD2 . PHE J 141 ? 2.6970 3.8173 3.9726 0.1144  -0.3764 0.4220  120 PHE I CD2 
18486 C CE1 . PHE J 141 ? 2.6951 3.8112 3.9299 0.1417  -0.3591 0.3958  120 PHE I CE1 
18487 C CE2 . PHE J 141 ? 2.7121 3.8699 4.0008 0.0915  -0.3737 0.4297  120 PHE I CE2 
18488 C CZ  . PHE J 141 ? 2.7364 3.8924 4.0056 0.1060  -0.3646 0.4172  120 PHE I CZ  
18489 N N   . PRO J 142 ? 2.6581 3.6377 3.8183 0.2364  -0.3517 0.3273  121 PRO I N   
18490 C CA  . PRO J 142 ? 2.6390 3.5874 3.7883 0.2578  -0.3502 0.3202  121 PRO I CA  
18491 C C   . PRO J 142 ? 2.6810 3.5922 3.8198 0.2754  -0.3593 0.3278  121 PRO I C   
18492 O O   . PRO J 142 ? 2.7544 3.6506 3.8971 0.2808  -0.3654 0.3471  121 PRO I O   
18493 C CB  . PRO J 142 ? 2.7081 3.6480 3.8484 0.2731  -0.3405 0.3139  121 PRO I CB  
18494 C CG  . PRO J 142 ? 2.7547 3.7037 3.8954 0.2690  -0.3410 0.3229  121 PRO I CG  
18495 C CD  . PRO J 142 ? 2.6883 3.6711 3.8439 0.2423  -0.3451 0.3285  121 PRO I CD  
18496 N N   . LEU J 143 ? 2.6014 3.4967 3.7437 0.2817  -0.3615 0.3274  122 LEU I N   
18497 C CA  . LEU J 143 ? 2.6788 3.5358 3.8362 0.2949  -0.3717 0.3528  122 LEU I CA  
18498 C C   . LEU J 143 ? 2.7164 3.5388 3.8341 0.3293  -0.3626 0.3262  122 LEU I C   
18499 O O   . LEU J 143 ? 2.6937 3.5152 3.8049 0.3357  -0.3555 0.3099  122 LEU I O   
18500 C CB  . LEU J 143 ? 2.6705 3.5297 3.8627 0.2786  -0.3817 0.3729  122 LEU I CB  
18501 C CG  . LEU J 143 ? 2.6482 3.5411 3.8811 0.2417  -0.3942 0.4025  122 LEU I CG  
18502 C CD1 . LEU J 143 ? 2.6448 3.5352 3.9085 0.2266  -0.4063 0.4197  122 LEU I CD1 
18503 C CD2 . LEU J 143 ? 2.7156 3.6004 3.9674 0.2346  -0.4070 0.4368  122 LEU I CD2 
18504 N N   . ALA J 144 ? 2.6224 3.4170 3.7250 0.3478  -0.3645 0.3308  123 ALA I N   
18505 C CA  . ALA J 144 ? 2.7124 3.4781 3.7976 0.3744  -0.3579 0.3197  123 ALA I CA  
18506 C C   . ALA J 144 ? 2.8049 3.5385 3.8821 0.3926  -0.3586 0.3153  123 ALA I C   
18507 O O   . ALA J 144 ? 2.8528 3.5655 3.9523 0.3896  -0.3703 0.3399  123 ALA I O   
18508 C CB  . ALA J 144 ? 2.7341 3.4748 3.8058 0.3890  -0.3625 0.3282  123 ALA I CB  
18509 N N   . PRO J 145 ? 2.7986 3.5272 3.8751 0.4048  -0.3490 0.3027  124 PRO I N   
18510 C CA  . PRO J 145 ? 2.8562 3.5547 3.9256 0.4233  -0.3478 0.2976  124 PRO I CA  
18511 C C   . PRO J 145 ? 3.0680 3.7179 4.1192 0.4485  -0.3540 0.3045  124 PRO I C   
18512 O O   . PRO J 145 ? 3.1371 3.7736 4.1799 0.4592  -0.3548 0.3073  124 PRO I O   
18513 C CB  . PRO J 145 ? 2.8381 3.5467 3.9112 0.4289  -0.3356 0.2831  124 PRO I CB  
18514 C CG  . PRO J 145 ? 2.7586 3.5064 3.8415 0.4081  -0.3313 0.2804  124 PRO I CG  
18515 C CD  . PRO J 145 ? 2.7608 3.5131 3.8429 0.4002  -0.3385 0.2925  124 PRO I CD  
18516 N N   . SER J 146 ? 2.8892 3.5096 3.9480 0.4554  -0.3598 0.3147  125 SER I N   
18517 C CA  . SER J 146 ? 3.0493 3.6152 4.1059 0.4771  -0.3673 0.3291  125 SER I CA  
18518 C C   . SER J 146 ? 3.0974 3.6350 4.1702 0.4853  -0.3680 0.3329  125 SER I C   
18519 O O   . SER J 146 ? 3.1171 3.6481 4.2283 0.4681  -0.3801 0.3563  125 SER I O   
18520 C CB  . SER J 146 ? 3.0516 3.5980 4.1322 0.4656  -0.3851 0.3631  125 SER I CB  
18521 O OG  . SER J 146 ? 2.9577 3.5275 4.0225 0.4605  -0.3834 0.3590  125 SER I OG  
18522 N N   . SER J 147 ? 2.9576 3.4785 4.0008 0.5108  -0.3558 0.3105  126 SER I N   
18523 C CA  . SER J 147 ? 3.0123 3.5041 4.0675 0.5220  -0.3539 0.3108  126 SER I CA  
18524 C C   . SER J 147 ? 2.9244 3.4449 4.0101 0.4999  -0.3542 0.3135  126 SER I C   
18525 O O   . SER J 147 ? 2.9635 3.4563 4.0807 0.4960  -0.3636 0.3307  126 SER I O   
18526 C CB  . SER J 147 ? 3.1353 3.5644 4.2072 0.5321  -0.3685 0.3354  126 SER I CB  
18527 O OG  . SER J 147 ? 3.2334 3.6313 4.2733 0.5555  -0.3673 0.3312  126 SER I OG  
18528 N N   . GLY J 152 ? 3.1101 3.4609 4.1283 0.6299  -0.3046 0.2551  131 GLY I N   
18529 C CA  . GLY J 152 ? 3.0201 3.3789 4.0698 0.6165  -0.3041 0.2563  131 GLY I CA  
18530 C C   . GLY J 152 ? 2.8815 3.2961 3.9169 0.6080  -0.2906 0.2371  131 GLY I C   
18531 O O   . GLY J 152 ? 2.8738 3.2957 3.9284 0.6012  -0.2864 0.2338  131 GLY I O   
18532 N N   . GLY J 153 ? 3.1637 3.6123 4.1922 0.6030  -0.2879 0.2307  132 GLY I N   
18533 C CA  . GLY J 153 ? 3.0930 3.5867 4.1376 0.5887  -0.2802 0.2206  132 GLY I CA  
18534 C C   . GLY J 153 ? 2.9932 3.5276 4.0458 0.5608  -0.2855 0.2235  132 GLY I C   
18535 O O   . GLY J 153 ? 2.8818 3.4514 3.9446 0.5475  -0.2798 0.2158  132 GLY I O   
18536 N N   . THR J 154 ? 2.9782 3.5070 4.0255 0.5515  -0.2965 0.2346  133 THR I N   
18537 C CA  . THR J 154 ? 2.8700 3.4360 3.9256 0.5244  -0.3031 0.2387  133 THR I CA  
18538 C C   . THR J 154 ? 2.8902 3.4607 3.9426 0.5161  -0.3130 0.2496  133 THR I C   
18539 O O   . THR J 154 ? 2.9633 3.5024 4.0042 0.5323  -0.3164 0.2555  133 THR I O   
18540 C CB  . THR J 154 ? 2.8334 3.3877 3.9273 0.5112  -0.3121 0.2547  133 THR I CB  
18541 O OG1 . THR J 154 ? 2.9897 3.4932 4.1081 0.5195  -0.3242 0.2762  133 THR I OG1 
18542 C CG2 . THR J 154 ? 2.7031 3.2557 3.7986 0.5185  -0.3015 0.2423  133 THR I CG2 
18543 N N   . ALA J 155 ? 2.7256 3.3350 3.7878 0.4906  -0.3173 0.2522  134 ALA I N   
18544 C CA  . ALA J 155 ? 2.7340 3.3524 3.7951 0.4802  -0.3258 0.2623  134 ALA I CA  
18545 C C   . ALA J 155 ? 2.6864 3.3391 3.7702 0.4498  -0.3335 0.2719  134 ALA I C   
18546 O O   . ALA J 155 ? 2.6245 3.3028 3.7123 0.4375  -0.3293 0.2625  134 ALA I O   
18547 C CB  . ALA J 155 ? 2.7092 3.3432 3.7728 0.4806  -0.3204 0.2579  134 ALA I CB  
18548 N N   . ALA J 156 ? 2.7714 3.4242 3.8756 0.4361  -0.3458 0.2938  135 ALA I N   
18549 C CA  . ALA J 156 ? 2.7374 3.4241 3.8713 0.4043  -0.3549 0.3089  135 ALA I CA  
18550 C C   . ALA J 156 ? 2.6889 3.4109 3.7996 0.3945  -0.3497 0.2953  135 ALA I C   
18551 O O   . ALA J 156 ? 2.7104 3.4216 3.7948 0.4095  -0.3462 0.2875  135 ALA I O   
18552 C CB  . ALA J 156 ? 2.8140 3.4766 3.9910 0.3919  -0.3749 0.3470  135 ALA I CB  
18553 N N   . LEU J 157 ? 2.8193 3.5811 3.9392 0.3696  -0.3496 0.2916  136 LEU I N   
18554 C CA  . LEU J 157 ? 2.7661 3.5603 3.8756 0.3567  -0.3453 0.2820  136 LEU I CA  
18555 C C   . LEU J 157 ? 2.6557 3.4862 3.7828 0.3267  -0.3506 0.2864  136 LEU I C   
18556 O O   . LEU J 157 ? 2.5666 3.4056 3.7088 0.3162  -0.3525 0.2874  136 LEU I O   
18557 C CB  . LEU J 157 ? 2.7600 3.5625 3.8686 0.3623  -0.3332 0.2700  136 LEU I CB  
18558 C CG  . LEU J 157 ? 2.7322 3.5569 3.8431 0.3529  -0.3289 0.2697  136 LEU I CG  
18559 C CD1 . LEU J 157 ? 2.8096 3.6248 3.9135 0.3685  -0.3195 0.2605  136 LEU I CD1 
18560 C CD2 . LEU J 157 ? 2.6311 3.4931 3.7522 0.3276  -0.3282 0.2666  136 LEU I CD2 
18561 N N   . GLY J 158 ? 2.7717 3.6238 3.9052 0.3107  -0.3538 0.2937  137 GLY I N   
18562 C CA  . GLY J 158 ? 2.7209 3.6096 3.8789 0.2794  -0.3591 0.3022  137 GLY I CA  
18563 C C   . GLY J 158 ? 2.6500 3.5638 3.8021 0.2672  -0.3570 0.2988  137 GLY I C   
18564 O O   . GLY J 158 ? 2.6586 3.5623 3.8007 0.2801  -0.3525 0.2987  137 GLY I O   
18565 N N   . CYS J 159 ? 2.7292 3.6769 3.9049 0.2376  -0.3621 0.3081  138 CYS I N   
18566 C CA  . CYS J 159 ? 2.6537 3.6292 3.8302 0.2220  -0.3605 0.3069  138 CYS I CA  
18567 C C   . CYS J 159 ? 2.5584 3.5531 3.7815 0.1910  -0.3755 0.3469  138 CYS I C   
18568 O O   . CYS J 159 ? 2.5442 3.5289 3.7967 0.1816  -0.3885 0.3727  138 CYS I O   
18569 C CB  . CYS J 159 ? 2.6220 3.6259 3.7981 0.2101  -0.3521 0.2913  138 CYS I CB  
18570 S SG  . CYS J 159 ? 3.3051 4.2937 4.4680 0.2321  -0.3398 0.2809  138 CYS I SG  
18571 N N   . LEU J 160 ? 2.7740 3.7967 4.0042 0.1734  -0.3750 0.3517  139 LEU I N   
18572 C CA  . LEU J 160 ? 2.6159 3.6626 3.8876 0.1401  -0.3892 0.3887  139 LEU I CA  
18573 C C   . LEU J 160 ? 2.4677 3.5562 3.7388 0.1178  -0.3827 0.3752  139 LEU I C   
18574 O O   . LEU J 160 ? 2.4233 3.5163 3.6728 0.1289  -0.3720 0.3569  139 LEU I O   
18575 C CB  . LEU J 160 ? 2.6254 3.6542 3.9138 0.1431  -0.3998 0.4235  139 LEU I CB  
18576 C CG  . LEU J 160 ? 2.5278 3.5856 3.8568 0.1040  -0.4160 0.4621  139 LEU I CG  
18577 C CD1 . LEU J 160 ? 2.5995 3.6262 3.9518 0.1043  -0.4361 0.5020  139 LEU I CD1 
18578 C CD2 . LEU J 160 ? 2.4221 3.5125 3.7517 0.0894  -0.4102 0.4645  139 LEU I CD2 
18579 N N   . VAL J 161 ? 2.5034 3.6202 3.7977 0.0867  -0.3897 0.3831  140 VAL I N   
18580 C CA  . VAL J 161 ? 2.3761 3.5328 3.6740 0.0625  -0.3848 0.3713  140 VAL I CA  
18581 C C   . VAL J 161 ? 2.3555 3.5364 3.6907 0.0277  -0.3978 0.4112  140 VAL I C   
18582 O O   . VAL J 161 ? 2.3531 3.5393 3.7153 0.0015  -0.4129 0.4357  140 VAL I O   
18583 C CB  . VAL J 161 ? 2.3293 3.5006 3.6221 0.0514  -0.3829 0.3469  140 VAL I CB  
18584 C CG1 . VAL J 161 ? 2.2851 3.4941 3.5814 0.0293  -0.3777 0.3320  140 VAL I CG1 
18585 C CG2 . VAL J 161 ? 2.4309 3.5784 3.6861 0.0837  -0.3716 0.3096  140 VAL I CG2 
18586 N N   . LYS J 162 ? 2.3735 3.5688 3.7096 0.0248  -0.3933 0.4179  141 LYS I N   
18587 C CA  . LYS J 162 ? 2.3954 3.6133 3.7639 -0.0081 -0.4054 0.4574  141 LYS I CA  
18588 C C   . LYS J 162 ? 2.4160 3.6795 3.7925 -0.0385 -0.3989 0.4481  141 LYS I C   
18589 O O   . LYS J 162 ? 2.3897 3.6631 3.7455 -0.0247 -0.3837 0.4167  141 LYS I O   
18590 C CB  . LYS J 162 ? 2.5194 3.7213 3.8856 0.0087  -0.4063 0.4773  141 LYS I CB  
18591 C CG  . LYS J 162 ? 2.5647 3.7897 3.9626 -0.0262 -0.4202 0.5203  141 LYS I CG  
18592 C CD  . LYS J 162 ? 2.5672 3.7578 3.9743 -0.0141 -0.4365 0.5565  141 LYS I CD  
18593 C CE  . LYS J 162 ? 2.6414 3.8593 4.0768 -0.0541 -0.4514 0.5977  141 LYS I CE  
18594 N NZ  . LYS J 162 ? 2.7237 3.9047 4.1660 -0.0428 -0.4717 0.6355  141 LYS I NZ  
18595 N N   . ASP J 163 ? 3.1325 3.9565 3.1561 -1.2142 -0.0905 -0.6966 142 ASP I N   
18596 C CA  . ASP J 163 ? 3.1958 4.0021 3.1754 -1.2733 -0.0316 -0.7568 142 ASP I CA  
18597 C C   . ASP J 163 ? 3.0298 3.9241 3.1019 -1.2332 0.0661  -0.7909 142 ASP I C   
18598 O O   . ASP J 163 ? 3.0024 3.8912 3.0707 -1.2950 0.1182  -0.8014 142 ASP I O   
18599 C CB  . ASP J 163 ? 3.3486 4.0471 3.2018 -1.4194 -0.0400 -0.7684 142 ASP I CB  
18600 C CG  . ASP J 163 ? 3.5524 4.1563 3.2978 -1.4685 -0.1289 -0.7522 142 ASP I CG  
18601 O OD1 . ASP J 163 ? 3.5470 4.1647 3.3200 -1.3932 -0.1952 -0.7140 142 ASP I OD1 
18602 O OD2 . ASP J 163 ? 3.7646 4.2804 3.3982 -1.5818 -0.1334 -0.7768 142 ASP I OD2 
18603 N N   . TYR J 164 ? 3.2936 4.2682 3.4484 -1.1312 0.0920  -0.8086 143 TYR I N   
18604 C CA  . TYR J 164 ? 3.1339 4.1886 3.3718 -1.0957 0.1850  -0.8448 143 TYR I CA  
18605 C C   . TYR J 164 ? 3.0854 4.1784 3.3469 -1.0406 0.2073  -0.8859 143 TYR I C   
18606 O O   . TYR J 164 ? 3.1211 4.1968 3.3585 -1.0046 0.1495  -0.8782 143 TYR I O   
18607 C CB  . TYR J 164 ? 2.9703 4.1197 3.3338 -0.9990 0.2105  -0.8123 143 TYR I CB  
18608 C CG  . TYR J 164 ? 2.8213 4.0429 3.2735 -0.8644 0.1745  -0.7838 143 TYR I CG  
18609 C CD1 . TYR J 164 ? 2.8434 4.0491 3.2943 -0.8287 0.0942  -0.7296 143 TYR I CD1 
18610 C CD2 . TYR J 164 ? 2.6907 3.9977 3.2295 -0.7725 0.2223  -0.8116 143 TYR I CD2 
18611 C CE1 . TYR J 164 ? 2.7424 4.0156 3.2757 -0.7050 0.0626  -0.7043 143 TYR I CE1 
18612 C CE2 . TYR J 164 ? 2.5760 3.9493 3.1957 -0.6500 0.1910  -0.7864 143 TYR I CE2 
18613 C CZ  . TYR J 164 ? 2.6018 3.9584 3.2187 -0.6165 0.1116  -0.7330 143 TYR I CZ  
18614 O OH  . TYR J 164 ? 2.5147 3.9385 3.2129 -0.4939 0.0817  -0.7087 143 TYR I OH  
18615 N N   . PHE J 165 ? 2.9931 4.1391 3.3034 -1.0340 0.2928  -0.9297 144 PHE I N   
18616 C CA  . PHE J 165 ? 3.0254 4.2144 3.3651 -0.9858 0.3288  -0.9746 144 PHE I CA  
18617 C C   . PHE J 165 ? 2.9667 4.2343 3.3909 -0.9571 0.4255  -1.0103 144 PHE I C   
18618 O O   . PHE J 165 ? 2.9902 4.2381 3.3917 -1.0348 0.4752  -1.0280 144 PHE I O   
18619 C CB  . PHE J 165 ? 3.1705 4.2695 3.3876 -1.0873 0.3140  -1.0124 144 PHE I CB  
18620 C CG  . PHE J 165 ? 3.1917 4.3223 3.4232 -1.0492 0.3432  -1.0593 144 PHE I CG  
18621 C CD1 . PHE J 165 ? 3.1491 4.2902 3.3886 -0.9767 0.2901  -1.0498 144 PHE I CD1 
18622 C CD2 . PHE J 165 ? 3.2037 4.3479 3.4340 -1.0934 0.4233  -1.1147 144 PHE I CD2 
18623 C CE1 . PHE J 165 ? 3.0906 4.2592 3.3414 -0.9449 0.3182  -1.0941 144 PHE I CE1 
18624 C CE2 . PHE J 165 ? 3.1501 4.3219 3.3919 -1.0625 0.4514  -1.1593 144 PHE I CE2 
18625 C CZ  . PHE J 165 ? 3.0755 4.2595 3.3274 -0.9883 0.3989  -1.1488 144 PHE I CZ  
18626 N N   . PRO J 166 ? 3.0268 4.3840 3.5492 -0.8446 0.4524  -1.0212 145 PRO I N   
18627 C CA  . PRO J 166 ? 2.9314 4.3192 3.4896 -0.7449 0.3964  -0.9992 145 PRO I CA  
18628 C C   . PRO J 166 ? 2.7681 4.2320 3.4336 -0.6367 0.3815  -0.9498 145 PRO I C   
18629 O O   . PRO J 166 ? 2.7382 4.2164 3.4349 -0.6505 0.4023  -0.9271 145 PRO I O   
18630 C CB  . PRO J 166 ? 2.7885 4.2273 3.3853 -0.6994 0.4483  -1.0504 145 PRO I CB  
18631 C CG  . PRO J 166 ? 2.7184 4.2088 3.3738 -0.7096 0.5398  -1.0789 145 PRO I CG  
18632 C CD  . PRO J 166 ? 2.8784 4.3039 3.4684 -0.8202 0.5439  -1.0675 145 PRO I CD  
18633 N N   . GLU J 167 ? 2.5385 4.0505 3.2592 -0.5306 0.3463  -0.9340 146 GLU I N   
18634 C CA  . GLU J 167 ? 2.4165 4.0070 3.2440 -0.4181 0.3325  -0.8898 146 GLU I CA  
18635 C C   . GLU J 167 ? 2.2916 3.9781 3.2292 -0.3574 0.4188  -0.9093 146 GLU I C   
18636 O O   . GLU J 167 ? 2.2824 3.9862 3.2245 -0.3744 0.4816  -0.9598 146 GLU I O   
18637 C CB  . GLU J 167 ? 2.3747 3.9896 3.2283 -0.3223 0.2732  -0.8719 146 GLU I CB  
18638 C CG  . GLU J 167 ? 2.4875 4.0182 3.2501 -0.3617 0.1788  -0.8399 146 GLU I CG  
18639 C CD  . GLU J 167 ? 2.4349 3.9995 3.2554 -0.2752 0.1188  -0.7809 146 GLU I CD  
18640 O OE1 . GLU J 167 ? 2.3055 3.9634 3.2371 -0.1656 0.1428  -0.7700 146 GLU I OE1 
18641 O OE2 . GLU J 167 ? 2.5281 4.0259 3.2830 -0.3172 0.0473  -0.7454 146 GLU I OE2 
18642 N N   . PRO J 168 ? 2.4619 4.2109 3.4887 -0.2866 0.4220  -0.8695 147 PRO I N   
18643 C CA  . PRO J 168 ? 2.4632 4.1963 3.4906 -0.2667 0.3520  -0.8095 147 PRO I CA  
18644 C C   . PRO J 168 ? 2.4600 4.1689 3.4752 -0.3325 0.3642  -0.7851 147 PRO I C   
18645 O O   . PRO J 168 ? 2.4904 4.1796 3.4787 -0.4104 0.4221  -0.8156 147 PRO I O   
18646 C CB  . PRO J 168 ? 2.3550 4.1898 3.5052 -0.1251 0.3535  -0.7859 147 PRO I CB  
18647 C CG  . PRO J 168 ? 2.2698 4.1777 3.4971 -0.0959 0.4478  -0.8241 147 PRO I CG  
18648 C CD  . PRO J 168 ? 2.3613 4.2157 3.5094 -0.1932 0.4895  -0.8811 147 PRO I CD  
18649 N N   . VAL J 169 ? 2.3329 4.0446 3.3695 -0.2990 0.3089  -0.7299 148 VAL I N   
18650 C CA  . VAL J 169 ? 2.3610 4.0585 3.3983 -0.3456 0.3139  -0.6991 148 VAL I CA  
18651 C C   . VAL J 169 ? 2.3010 4.0757 3.4431 -0.2370 0.2954  -0.6502 148 VAL I C   
18652 O O   . VAL J 169 ? 2.3271 4.1025 3.4759 -0.1801 0.2263  -0.6157 148 VAL I O   
18653 C CB  . VAL J 169 ? 2.5279 4.1163 3.4464 -0.4539 0.2507  -0.6791 148 VAL I CB  
18654 C CG1 . VAL J 169 ? 2.6003 4.1847 3.5348 -0.4743 0.2383  -0.6345 148 VAL I CG1 
18655 C CG2 . VAL J 169 ? 2.6106 4.1259 3.4307 -0.5738 0.2841  -0.7273 148 VAL I CG2 
18656 N N   . THR J 170 ? 2.3544 4.1937 3.5777 -0.2083 0.3565  -0.6474 149 THR I N   
18657 C CA  . THR J 170 ? 2.3071 4.2231 3.6335 -0.1091 0.3473  -0.6025 149 THR I CA  
18658 C C   . THR J 170 ? 2.4372 4.3087 3.7312 -0.1626 0.3064  -0.5562 149 THR I C   
18659 O O   . THR J 170 ? 2.4841 4.3170 3.7377 -0.2524 0.3392  -0.5650 149 THR I O   
18660 C CB  . THR J 170 ? 2.1010 4.1104 3.5332 -0.0481 0.4323  -0.6214 149 THR I CB  
18661 O OG1 . THR J 170 ? 2.0828 4.0659 3.4862 -0.1387 0.4904  -0.6436 149 THR I OG1 
18662 C CG2 . THR J 170 ? 1.9585 4.0144 3.4265 0.0109  0.4694  -0.6654 149 THR I CG2 
18663 N N   . VAL J 171 ? 2.0841 3.9608 3.3959 -0.1078 0.2351  -0.5075 150 VAL I N   
18664 C CA  . VAL J 171 ? 2.1989 4.0334 3.4807 -0.1518 0.1875  -0.4603 150 VAL I CA  
18665 C C   . VAL J 171 ? 2.1183 4.0370 3.5107 -0.0485 0.1813  -0.4154 150 VAL I C   
18666 O O   . VAL J 171 ? 2.1285 4.0955 3.5760 0.0509  0.1462  -0.3966 150 VAL I O   
18667 C CB  . VAL J 171 ? 2.3885 4.1357 3.5730 -0.1979 0.0970  -0.4398 150 VAL I CB  
18668 C CG1 . VAL J 171 ? 2.5093 4.2195 3.6718 -0.2351 0.0476  -0.3888 150 VAL I CG1 
18669 C CG2 . VAL J 171 ? 2.4922 4.1519 3.5624 -0.3070 0.1029  -0.4834 150 VAL I CG2 
18670 N N   . SER J 172 ? 1.9775 3.9137 3.4018 -0.0724 0.2158  -0.3986 151 SER I N   
18671 C CA  . SER J 172 ? 1.8997 3.9112 3.4243 0.0141  0.2124  -0.3547 151 SER I CA  
18672 C C   . SER J 172 ? 1.9636 3.9222 3.4455 -0.0493 0.1675  -0.3112 151 SER I C   
18673 O O   . SER J 172 ? 2.0586 3.9309 3.4429 -0.1624 0.1576  -0.3204 151 SER I O   
18674 C CB  . SER J 172 ? 1.8101 3.9056 3.4291 0.0576  0.3014  -0.3735 151 SER I CB  
18675 O OG  . SER J 172 ? 1.8551 3.9121 3.4312 -0.0421 0.3532  -0.3956 151 SER I OG  
18676 N N   . TRP J 173 ? 1.8866 3.8983 3.4430 0.0249  0.1407  -0.2638 152 TRP I N   
18677 C CA  . TRP J 173 ? 1.9951 3.9673 3.5245 -0.0194 0.0940  -0.2174 152 TRP I CA  
18678 C C   . TRP J 173 ? 1.9294 3.9671 3.5448 0.0109  0.1409  -0.1956 152 TRP I C   
18679 O O   . TRP J 173 ? 1.8220 3.9526 3.5435 0.1166  0.1661  -0.1861 152 TRP I O   
18680 C CB  . TRP J 173 ? 2.0887 4.0490 3.6125 0.0302  0.0025  -0.1750 152 TRP I CB  
18681 C CG  . TRP J 173 ? 2.1869 4.0628 3.6064 -0.0237 -0.0517 -0.1913 152 TRP I CG  
18682 C CD1 . TRP J 173 ? 2.1561 4.0360 3.5644 0.0102  -0.0536 -0.2236 152 TRP I CD1 
18683 C CD2 . TRP J 173 ? 2.3367 4.1103 3.6476 -0.1216 -0.1141 -0.1748 152 TRP I CD2 
18684 N NE1 . TRP J 173 ? 2.2823 4.0678 3.5803 -0.0620 -0.1128 -0.2285 152 TRP I NE1 
18685 C CE2 . TRP J 173 ? 2.3936 4.1124 3.6301 -0.1433 -0.1511 -0.1988 152 TRP I CE2 
18686 C CE3 . TRP J 173 ? 2.4479 4.1704 3.7168 -0.1933 -0.1425 -0.1418 152 TRP I CE3 
18687 C CZ2 . TRP J 173 ? 2.5406 4.1552 3.6623 -0.2341 -0.2153 -0.1908 152 TRP I CZ2 
18688 C CZ3 . TRP J 173 ? 2.5923 4.2117 3.7478 -0.2830 -0.2062 -0.1340 152 TRP I CZ3 
18689 C CH2 . TRP J 173 ? 2.6257 4.1920 3.7086 -0.3026 -0.2421 -0.1583 152 TRP I CH2 
18690 N N   . ASN J 174 ? 2.0541 4.0413 3.6213 -0.0838 0.1525  -0.1883 153 ASN I N   
18691 C CA  . ASN J 174 ? 2.0528 4.0883 3.6867 -0.0748 0.1968  -0.1683 153 ASN I CA  
18692 C C   . ASN J 174 ? 1.8659 3.9848 3.5857 -0.0186 0.2855  -0.2020 153 ASN I C   
18693 O O   . ASN J 174 ? 1.7915 3.9925 3.6115 0.0601  0.3129  -0.1811 153 ASN I O   
18694 C CB  . ASN J 174 ? 2.1042 4.1812 3.8009 -0.0014 0.1437  -0.1095 153 ASN I CB  
18695 C CG  . ASN J 174 ? 2.2115 4.2187 3.8449 -0.0831 0.0941  -0.0721 153 ASN I CG  
18696 O OD1 . ASN J 174 ? 2.2398 4.1939 3.8154 -0.1828 0.1225  -0.0851 153 ASN I OD1 
18697 N ND2 . ASN J 174 ? 2.2032 4.2097 3.8468 -0.0410 0.0190  -0.0257 153 ASN I ND2 
18698 N N   . SER J 175 ? 1.7022 3.7984 3.3809 -0.0608 0.3304  -0.2552 154 SER I N   
18699 C CA  . SER J 175 ? 1.6241 3.7898 3.3720 -0.0179 0.4157  -0.2947 154 SER I CA  
18700 C C   . SER J 175 ? 1.5166 3.7792 3.3714 0.1198  0.4189  -0.2861 154 SER I C   
18701 O O   . SER J 175 ? 1.4697 3.7425 3.3670 0.1768  0.4728  -0.2801 154 SER I O   
18702 C CB  . SER J 175 ? 1.6065 3.7934 3.3877 -0.0536 0.4787  -0.2939 154 SER I CB  
18703 O OG  . SER J 175 ? 1.5191 3.7846 3.3828 0.0053  0.5568  -0.3249 154 SER I OG  
18704 N N   . GLY J 176 ? 1.5214 3.7782 3.3682 0.1701  0.3496  -0.2653 155 GLY I N   
18705 C CA  . GLY J 176 ? 1.4394 3.7591 3.3648 0.2961  0.3416  -0.2518 155 GLY I CA  
18706 C C   . GLY J 176 ? 1.4267 3.7204 3.3861 0.3643  0.3048  -0.1826 155 GLY I C   
18707 O O   . GLY J 176 ? 1.4300 3.6237 3.3834 0.4384  0.3016  -0.1472 155 GLY I O   
18708 N N   . ALA J 177 ? 1.5762 3.9360 3.5651 0.3260  0.2772  -0.1640 156 ALA I N   
18709 C CA  . ALA J 177 ? 1.6016 3.9463 3.6273 0.3819  0.2405  -0.1035 156 ALA I CA  
18710 C C   . ALA J 177 ? 1.6957 4.0719 3.7221 0.4154  0.1499  -0.0748 156 ALA I C   
18711 O O   . ALA J 177 ? 1.7439 4.1240 3.7937 0.4378  0.1068  -0.0267 156 ALA I O   
18712 C CB  . ALA J 177 ? 1.6437 4.0300 3.6912 0.3221  0.2602  -0.0877 156 ALA I CB  
18713 N N   . LEU J 178 ? 1.6279 3.9640 3.5975 0.4097  0.1172  -0.0979 157 LEU I N   
18714 C CA  . LEU J 178 ? 1.7594 4.0605 3.6932 0.4299  0.0271  -0.0676 157 LEU I CA  
18715 C C   . LEU J 178 ? 1.7262 4.0290 3.6462 0.4726  0.0149  -0.0988 157 LEU I C   
18716 O O   . LEU J 178 ? 1.7656 3.9993 3.5975 0.3976  0.0149  -0.1340 157 LEU I O   
18717 C CB  . LEU J 178 ? 1.9233 4.1181 3.7451 0.3140  -0.0242 -0.0542 157 LEU I CB  
18718 C CG  . LEU J 178 ? 2.0506 4.1989 3.8270 0.3214  -0.1217 -0.0192 157 LEU I CG  
18719 C CD1 . LEU J 178 ? 2.0451 4.2624 3.9121 0.4181  -0.1558 0.0317  157 LEU I CD1 
18720 C CD2 . LEU J 178 ? 2.1763 4.2169 3.8388 0.1970  -0.1628 -0.0105 157 LEU I CD2 
18721 N N   . THR J 179 ? 1.7116 3.9644 3.6517 0.5603  0.0079  -0.0750 158 THR I N   
18722 C CA  . THR J 179 ? 1.7056 3.9019 3.6075 0.5935  -0.0008 -0.0916 158 THR I CA  
18723 C C   . THR J 179 ? 1.8185 3.9654 3.7017 0.6378  -0.0789 -0.0550 158 THR I C   
18724 O O   . THR J 179 ? 1.8340 3.9292 3.6833 0.6644  -0.0914 -0.0625 158 THR I O   
18725 C CB  . THR J 179 ? 1.6107 3.6944 3.5027 0.6177  0.0687  -0.0921 158 THR I CB  
18726 O OG1 . THR J 179 ? 1.6487 3.6814 3.5022 0.6436  0.0596  -0.1032 158 THR I OG1 
18727 C CG2 . THR J 179 ? 1.5426 3.5322 3.4599 0.6464  0.0682  -0.0529 158 THR I CG2 
18728 N N   . SER J 180 ? 1.6972 3.8524 3.5973 0.6419  -0.1302 -0.0151 159 SER I N   
18729 C CA  . SER J 180 ? 1.8072 3.9006 3.6861 0.6761  -0.2032 0.0210  159 SER I CA  
18730 C C   . SER J 180 ? 1.8915 4.0681 3.7490 0.6494  -0.2872 0.0237  159 SER I C   
18731 O O   . SER J 180 ? 1.9241 4.1475 3.7810 0.5954  -0.3091 0.0362  159 SER I O   
18732 C CB  . SER J 180 ? 1.8653 3.8929 3.7704 0.6935  -0.2097 0.0574  159 SER I CB  
18733 O OG  . SER J 180 ? 1.9329 4.0414 3.8661 0.6617  -0.2143 0.0696  159 SER I OG  
18734 N N   . GLY J 181 ? 1.8396 3.9875 3.6544 0.6653  -0.3332 0.0145  160 GLY I N   
18735 C CA  . GLY J 181 ? 1.9378 4.0819 3.6905 0.6176  -0.4178 0.0162  160 GLY I CA  
18736 C C   . GLY J 181 ? 1.9615 4.0222 3.6090 0.5079  -0.3966 -0.0283 160 GLY I C   
18737 O O   . GLY J 181 ? 2.0854 4.0532 3.6325 0.4246  -0.4517 -0.0219 160 GLY I O   
18738 N N   . VAL J 182 ? 2.0227 4.1132 3.6897 0.5046  -0.3191 -0.0730 161 VAL I N   
18739 C CA  . VAL J 182 ? 2.0383 4.0569 3.6118 0.4028  -0.2904 -0.1191 161 VAL I CA  
18740 C C   . VAL J 182 ? 2.0434 4.0494 3.5872 0.4325  -0.3103 -0.1490 161 VAL I C   
18741 O O   . VAL J 182 ? 1.9445 4.0273 3.5670 0.5313  -0.2859 -0.1602 161 VAL I O   
18742 C CB  . VAL J 182 ? 1.9134 3.9704 3.5237 0.3790  -0.1934 -0.1524 161 VAL I CB  
18743 C CG1 . VAL J 182 ? 1.9841 3.9627 3.4938 0.2669  -0.1657 -0.1986 161 VAL I CG1 
18744 C CG2 . VAL J 182 ? 1.8735 3.9529 3.5249 0.3627  -0.1733 -0.1202 161 VAL I CG2 
18745 N N   . HIS J 183 ? 2.2378 4.1466 3.6679 0.3475  -0.3552 -0.1616 162 HIS I N   
18746 C CA  . HIS J 183 ? 2.2788 4.1632 3.6665 0.3619  -0.3780 -0.1909 162 HIS I CA  
18747 C C   . HIS J 183 ? 2.2658 4.0672 3.5476 0.2422  -0.3520 -0.2349 162 HIS I C   
18748 O O   . HIS J 183 ? 2.3588 4.0673 3.5406 0.1476  -0.3981 -0.2266 162 HIS I O   
18749 C CB  . HIS J 183 ? 2.4168 4.2635 3.7698 0.3894  -0.4755 -0.1571 162 HIS I CB  
18750 C CG  . HIS J 183 ? 2.4201 4.3511 3.8768 0.5162  -0.5022 -0.1198 162 HIS I CG  
18751 N ND1 . HIS J 183 ? 2.3130 4.3483 3.8825 0.6138  -0.4441 -0.1270 162 HIS I ND1 
18752 C CD2 . HIS J 183 ? 2.5031 4.4289 3.9667 0.5621  -0.5815 -0.0762 162 HIS I CD2 
18753 C CE1 . HIS J 183 ? 2.3297 4.3904 3.9542 0.7020  -0.4790 -0.0842 162 HIS I CE1 
18754 N NE2 . HIS J 183 ? 2.4148 4.4420 3.9948 0.6847  -0.5688 -0.0578 162 HIS I NE2 
18755 N N   . THR J 184 ? 2.2987 4.1345 3.6033 0.2472  -0.2779 -0.2819 163 THR I N   
18756 C CA  . THR J 184 ? 2.3095 4.0775 3.5235 0.1419  -0.2441 -0.3290 163 THR I CA  
18757 C C   . THR J 184 ? 2.3807 4.1125 3.5389 0.1470  -0.2779 -0.3554 163 THR I C   
18758 O O   . THR J 184 ? 2.3183 4.1142 3.5403 0.2407  -0.2654 -0.3682 163 THR I O   
18759 C CB  . THR J 184 ? 2.1319 3.9570 3.4013 0.1434  -0.1446 -0.3669 163 THR I CB  
18760 O OG1 . THR J 184 ? 2.1011 3.9568 3.4193 0.1357  -0.1145 -0.3416 163 THR I OG1 
18761 C CG2 . THR J 184 ? 2.0827 3.8390 3.2590 0.0344  -0.1084 -0.4170 163 THR I CG2 
18762 N N   . PHE J 185 ? 2.4264 4.0534 3.4634 0.0451  -0.3227 -0.3629 164 PHE I N   
18763 C CA  . PHE J 185 ? 2.5126 4.0888 3.4790 0.0328  -0.3628 -0.3857 164 PHE I CA  
18764 C C   . PHE J 185 ? 2.4331 3.9901 3.3566 -0.0247 -0.3002 -0.4457 164 PHE I C   
18765 O O   . PHE J 185 ? 2.3618 3.9011 3.2624 -0.1018 -0.2439 -0.4677 164 PHE I O   
18766 C CB  . PHE J 185 ? 2.6819 4.1540 3.5394 -0.0464 -0.4468 -0.3608 164 PHE I CB  
18767 C CG  . PHE J 185 ? 2.7381 4.2238 3.6308 0.0138  -0.5185 -0.3036 164 PHE I CG  
18768 C CD1 . PHE J 185 ? 2.7481 4.2379 3.6634 -0.0050 -0.5232 -0.2662 164 PHE I CD1 
18769 C CD2 . PHE J 185 ? 2.7953 4.2917 3.7006 0.0912  -0.5806 -0.2877 164 PHE I CD2 
18770 C CE1 . PHE J 185 ? 2.7841 4.2882 3.7337 0.0513  -0.5891 -0.2140 164 PHE I CE1 
18771 C CE2 . PHE J 185 ? 2.8656 4.3761 3.8050 0.1481  -0.6465 -0.2359 164 PHE I CE2 
18772 C CZ  . PHE J 185 ? 2.8506 4.3653 3.8125 0.1281  -0.6507 -0.1991 164 PHE I CZ  
18773 N N   . PRO J 186 ? 2.3157 3.8773 3.2297 0.0143  -0.3105 -0.4719 165 PRO I N   
18774 C CA  . PRO J 186 ? 2.3657 3.9056 3.2339 -0.0388 -0.2578 -0.5297 165 PRO I CA  
18775 C C   . PRO J 186 ? 2.5321 3.9588 3.2671 -0.1780 -0.2769 -0.5462 165 PRO I C   
18776 O O   . PRO J 186 ? 2.6184 3.9713 3.2786 -0.2224 -0.3517 -0.5181 165 PRO I O   
18777 C CB  . PRO J 186 ? 2.3312 3.8968 3.2171 0.0417  -0.2840 -0.5430 165 PRO I CB  
18778 C CG  . PRO J 186 ? 2.3327 3.8866 3.2204 0.0921  -0.3723 -0.4927 165 PRO I CG  
18779 C CD  . PRO J 186 ? 2.2650 3.8561 3.2144 0.1138  -0.3701 -0.4498 165 PRO I CD  
18780 N N   . ALA J 187 ? 2.5614 3.9754 3.2676 -0.2469 -0.2076 -0.5930 166 ALA I N   
18781 C CA  . ALA J 187 ? 2.6986 4.0108 3.2826 -0.3834 -0.2117 -0.6146 166 ALA I CA  
18782 C C   . ALA J 187 ? 2.7884 4.0285 3.2782 -0.4169 -0.2670 -0.6309 166 ALA I C   
18783 O O   . ALA J 187 ? 2.7490 4.0213 3.2695 -0.3360 -0.2919 -0.6333 166 ALA I O   
18784 C CB  . ALA J 187 ? 2.7026 4.0285 3.2885 -0.4387 -0.1190 -0.6638 166 ALA I CB  
18785 N N   . VAL J 188 ? 2.9360 4.0757 3.3082 -0.5402 -0.2861 -0.6421 167 VAL I N   
18786 C CA  . VAL J 188 ? 3.0313 4.0885 3.2976 -0.5947 -0.3363 -0.6596 167 VAL I CA  
18787 C C   . VAL J 188 ? 3.1047 4.1133 3.2958 -0.6999 -0.2809 -0.7138 167 VAL I C   
18788 O O   . VAL J 188 ? 3.1402 4.1192 3.3000 -0.7843 -0.2444 -0.7205 167 VAL I O   
18789 C CB  . VAL J 188 ? 3.1033 4.0733 3.2860 -0.6460 -0.4285 -0.6169 167 VAL I CB  
18790 C CG1 . VAL J 188 ? 3.1461 4.0751 3.2952 -0.7322 -0.4191 -0.5984 167 VAL I CG1 
18791 C CG2 . VAL J 188 ? 3.2029 4.0797 3.2662 -0.7172 -0.4748 -0.6391 167 VAL I CG2 
18792 N N   . LEU J 189 ? 3.2086 4.2095 3.3711 -0.6939 -0.2755 -0.7521 168 LEU I N   
18793 C CA  . LEU J 189 ? 3.3224 4.2777 3.4113 -0.7868 -0.2278 -0.8069 168 LEU I CA  
18794 C C   . LEU J 189 ? 3.4086 4.2427 3.3586 -0.9022 -0.2887 -0.8020 168 LEU I C   
18795 O O   . LEU J 189 ? 3.4014 4.1918 3.3000 -0.8928 -0.3569 -0.7921 168 LEU I O   
18796 C CB  . LEU J 189 ? 3.2956 4.2907 3.4093 -0.7309 -0.2029 -0.8478 168 LEU I CB  
18797 C CG  . LEU J 189 ? 3.3060 4.2521 3.3409 -0.8326 -0.1528 -0.9053 168 LEU I CG  
18798 C CD1 . LEU J 189 ? 3.2662 4.2597 3.3513 -0.8567 -0.0580 -0.9339 168 LEU I CD1 
18799 C CD2 . LEU J 189 ? 3.2391 4.1871 3.2548 -0.8056 -0.1546 -0.9436 168 LEU I CD2 
18800 N N   . GLN J 190 ? 3.4812 4.2593 3.3688 -1.0116 -0.2651 -0.8088 169 GLN I N   
18801 C CA  . GLN J 190 ? 3.6097 4.2713 3.3640 -1.1222 -0.3238 -0.8033 169 GLN I CA  
18802 C C   . GLN J 190 ? 3.6864 4.2997 3.3603 -1.1774 -0.3146 -0.8531 169 GLN I C   
18803 O O   . GLN J 190 ? 3.6362 4.3056 3.3567 -1.1376 -0.2571 -0.8940 169 GLN I O   
18804 C CB  . GLN J 190 ? 3.6518 4.2645 3.3560 -1.2312 -0.2946 -0.8031 169 GLN I CB  
18805 C CG  . GLN J 190 ? 3.4657 4.1124 3.2326 -1.2049 -0.2962 -0.7579 169 GLN I CG  
18806 C CD  . GLN J 190 ? 3.5147 4.1108 3.2261 -1.3199 -0.2595 -0.7660 169 GLN I CD  
18807 O OE1 . GLN J 190 ? 3.6118 4.1546 3.2449 -1.4148 -0.2264 -0.8080 169 GLN I OE1 
18808 N NE2 . GLN J 190 ? 3.4525 4.0677 3.2066 -1.3105 -0.2628 -0.7266 169 GLN I NE2 
18809 N N   . SER J 191 ? 3.6453 4.1517 3.1951 -1.2718 -0.3728 -0.8499 170 SER I N   
18810 C CA  . SER J 191 ? 3.7137 4.1686 3.1802 -1.3309 -0.3667 -0.8965 170 SER I CA  
18811 C C   . SER J 191 ? 3.7515 4.1952 3.1994 -1.4006 -0.2780 -0.9347 170 SER I C   
18812 O O   . SER J 191 ? 3.7869 4.2139 3.2124 -1.4005 -0.2384 -0.9621 170 SER I O   
18813 C CB  . SER J 191 ? 3.8049 4.1389 3.1587 -1.3794 -0.4450 -0.8617 170 SER I CB  
18814 O OG  . SER J 191 ? 3.8696 4.1283 3.1744 -1.4413 -0.4457 -0.8228 170 SER I OG  
18815 N N   . SER J 192 ? 3.8020 4.2498 3.2662 -1.4405 -0.2439 -0.9217 171 SER I N   
18816 C CA  . SER J 192 ? 3.7804 4.2174 3.2391 -1.4857 -0.1561 -0.9387 171 SER I CA  
18817 C C   . SER J 192 ? 3.7371 4.2922 3.2976 -1.4473 -0.0789 -0.9972 171 SER I C   
18818 O O   . SER J 192 ? 3.7141 4.2669 3.2720 -1.4745 -0.0011 -1.0195 171 SER I O   
18819 C CB  . SER J 192 ? 3.6866 4.0885 3.1292 -1.5357 -0.1536 -0.9012 171 SER I CB  
18820 O OG  . SER J 192 ? 3.5815 4.0717 3.1119 -1.5064 -0.1699 -0.8997 171 SER I OG  
18821 N N   . GLY J 193 ? 3.8289 4.4730 3.4941 -1.3280 -0.0889 -0.9827 172 GLY I N   
18822 C CA  . GLY J 193 ? 3.7056 4.4555 3.4850 -1.2434 -0.0125 -1.0087 172 GLY I CA  
18823 C C   . GLY J 193 ? 3.6033 4.4220 3.4793 -1.1993 0.0283  -0.9840 172 GLY I C   
18824 O O   . GLY J 193 ? 3.5008 4.3912 3.4522 -1.1670 0.1074  -1.0134 172 GLY I O   
18825 N N   . LEU J 194 ? 3.5173 4.3143 3.3909 -1.2000 -0.0230 -0.9315 173 LEU I N   
18826 C CA  . LEU J 194 ? 3.4184 4.2728 3.3764 -1.1635 0.0070  -0.9023 173 LEU I CA  
18827 C C   . LEU J 194 ? 3.3244 4.2299 3.3607 -1.0518 -0.0477 -0.8483 173 LEU I C   
18828 O O   . LEU J 194 ? 3.3666 4.2259 3.3566 -1.0438 -0.1289 -0.8188 173 LEU I O   
18829 C CB  . LEU J 194 ? 3.4755 4.2514 3.3531 -1.2806 -0.0015 -0.8881 173 LEU I CB  
18830 C CG  . LEU J 194 ? 3.5437 4.2686 3.3451 -1.3981 0.0564  -0.9388 173 LEU I CG  
18831 C CD1 . LEU J 194 ? 3.5148 4.1521 3.2262 -1.5145 0.0337  -0.9197 173 LEU I CD1 
18832 C CD2 . LEU J 194 ? 3.4326 4.2411 3.3217 -1.3663 0.1547  -0.9749 173 LEU I CD2 
18833 N N   . TYR J 195 ? 3.2156 4.2179 3.3716 -0.9634 -0.0029 -0.8364 174 TYR I N   
18834 C CA  . TYR J 195 ? 3.0982 4.1584 3.3389 -0.8534 -0.0466 -0.7861 174 TYR I CA  
18835 C C   . TYR J 195 ? 3.0747 4.1062 3.3054 -0.8875 -0.0803 -0.7371 174 TYR I C   
18836 O O   . TYR J 195 ? 3.1536 4.1396 3.3346 -0.9835 -0.0537 -0.7438 174 TYR I O   
18837 C CB  . TYR J 195 ? 2.9244 4.1039 3.3002 -0.7360 0.0133  -0.7947 174 TYR I CB  
18838 C CG  . TYR J 195 ? 2.9040 4.1235 3.3053 -0.6825 0.0416  -0.8375 174 TYR I CG  
18839 C CD1 . TYR J 195 ? 2.9100 4.1465 3.3294 -0.5997 -0.0140 -0.8229 174 TYR I CD1 
18840 C CD2 . TYR J 195 ? 2.9318 4.1768 3.3450 -0.7087 0.1239  -0.8911 174 TYR I CD2 
18841 C CE1 . TYR J 195 ? 2.9283 4.2026 3.3729 -0.5478 0.0103  -0.8604 174 TYR I CE1 
18842 C CE2 . TYR J 195 ? 2.9719 4.2559 3.4117 -0.6564 0.1489  -0.9293 174 TYR I CE2 
18843 C CZ  . TYR J 195 ? 2.9646 4.2627 3.4196 -0.5762 0.0917  -0.9135 174 TYR I CZ  
18844 O OH  . TYR J 195 ? 2.9764 4.3127 3.4573 -0.5245 0.1158  -0.9510 174 TYR I OH  
18845 N N   . SER J 196 ? 2.9625 4.0215 3.2417 -0.8064 -0.1401 -0.6874 175 SER I N   
18846 C CA  . SER J 196 ? 2.9543 3.9917 3.2319 -0.8235 -0.1817 -0.6357 175 SER I CA  
18847 C C   . SER J 196 ? 2.8690 3.9817 3.2475 -0.6955 -0.2184 -0.5911 175 SER I C   
18848 O O   . SER J 196 ? 2.8850 3.9974 3.2613 -0.6381 -0.2733 -0.5811 175 SER I O   
18849 C CB  . SER J 196 ? 3.0730 3.9934 3.2216 -0.9250 -0.2551 -0.6200 175 SER I CB  
18850 O OG  . SER J 196 ? 3.0813 3.9891 3.2265 -0.8689 -0.3413 -0.5805 175 SER I OG  
18851 N N   . LEU J 197 ? 2.9058 4.0820 3.3713 -0.6509 -0.1895 -0.5643 176 LEU I N   
18852 C CA  . LEU J 197 ? 2.7788 4.0326 3.3467 -0.5285 -0.2184 -0.5218 176 LEU I CA  
18853 C C   . LEU J 197 ? 2.8669 4.0979 3.4323 -0.5433 -0.2686 -0.4668 176 LEU I C   
18854 O O   . LEU J 197 ? 3.0555 4.2104 3.5403 -0.6481 -0.2814 -0.4604 176 LEU I O   
18855 C CB  . LEU J 197 ? 2.6062 3.9688 3.2963 -0.4494 -0.1369 -0.5343 176 LEU I CB  
18856 C CG  . LEU J 197 ? 2.4350 3.8755 3.1974 -0.3889 -0.0603 -0.5786 176 LEU I CG  
18857 C CD1 . LEU J 197 ? 2.3910 3.9113 3.2532 -0.3479 0.0048  -0.5703 176 LEU I CD1 
18858 C CD2 . LEU J 197 ? 2.2470 3.7445 3.0699 -0.2729 -0.0883 -0.5731 176 LEU I CD2 
18859 N N   . SER J 198 ? 2.7132 4.0126 3.3694 -0.4347 -0.2977 -0.4268 177 SER I N   
18860 C CA  . SER J 198 ? 2.7210 4.0170 3.3960 -0.4262 -0.3441 -0.3718 177 SER I CA  
18861 C C   . SER J 198 ? 2.6002 4.0083 3.4111 -0.2976 -0.3262 -0.3453 177 SER I C   
18862 O O   . SER J 198 ? 2.5244 3.9983 3.4006 -0.2048 -0.3107 -0.3596 177 SER I O   
18863 C CB  . SER J 198 ? 2.7998 4.0216 3.3996 -0.4449 -0.4449 -0.3398 177 SER I CB  
18864 O OG  . SER J 198 ? 2.9343 4.0497 3.4055 -0.5648 -0.4649 -0.3624 177 SER I OG  
18865 N N   . SER J 199 ? 2.6330 4.0620 3.4856 -0.2931 -0.3287 -0.3065 178 SER I N   
18866 C CA  . SER J 199 ? 2.4876 4.0199 3.4671 -0.1773 -0.3137 -0.2770 178 SER I CA  
18867 C C   . SER J 199 ? 2.5694 4.0884 3.5562 -0.1749 -0.3729 -0.2195 178 SER I C   
18868 O O   . SER J 199 ? 2.6640 4.1422 3.6139 -0.2558 -0.3638 -0.2085 178 SER I O   
18869 C CB  . SER J 199 ? 2.3685 3.9704 3.4222 -0.1641 -0.2169 -0.3016 178 SER I CB  
18870 O OG  . SER J 199 ? 2.2015 3.9045 3.3780 -0.0498 -0.2012 -0.2748 178 SER I OG  
18871 N N   . VAL J 200 ? 2.4166 3.9700 3.4511 -0.0837 -0.4326 -0.1831 179 VAL I N   
18872 C CA  . VAL J 200 ? 2.5113 4.0540 3.5550 -0.0763 -0.4930 -0.1278 179 VAL I CA  
18873 C C   . VAL J 200 ? 2.3886 4.0403 3.5644 0.0373  -0.4709 -0.0985 179 VAL I C   
18874 O O   . VAL J 200 ? 2.2649 3.9971 3.5222 0.1310  -0.4351 -0.1140 179 VAL I O   
18875 C CB  . VAL J 200 ? 2.6525 4.1354 3.6344 -0.0730 -0.5909 -0.1036 179 VAL I CB  
18876 C CG1 . VAL J 200 ? 2.7359 4.1055 3.5826 -0.1937 -0.6152 -0.1285 179 VAL I CG1 
18877 C CG2 . VAL J 200 ? 2.5682 4.1100 3.6080 0.0396  -0.6073 -0.1092 179 VAL I CG2 
18878 N N   . VAL J 201 ? 2.2780 3.9314 3.4742 0.0274  -0.4925 -0.0556 180 VAL I N   
18879 C CA  . VAL J 201 ? 2.1941 3.9443 3.5099 0.1263  -0.4777 -0.0220 180 VAL I CA  
18880 C C   . VAL J 201 ? 2.2812 4.0148 3.5974 0.1480  -0.5619 0.0335  180 VAL I C   
18881 O O   . VAL J 201 ? 2.3957 4.0547 3.6392 0.0608  -0.5991 0.0532  180 VAL I O   
18882 C CB  . VAL J 201 ? 2.1460 3.9312 3.5046 0.0959  -0.4012 -0.0271 180 VAL I CB  
18883 C CG1 . VAL J 201 ? 2.0644 3.9493 3.5462 0.1991  -0.3884 0.0090  180 VAL I CG1 
18884 C CG2 . VAL J 201 ? 2.0684 3.8702 3.4275 0.0732  -0.3164 -0.0833 180 VAL I CG2 
18885 N N   . THR J 202 ? 2.0387 3.8427 3.4375 0.2642  -0.5912 0.0584  181 THR I N   
18886 C CA  . THR J 202 ? 2.1548 3.9579 3.5704 0.3019  -0.6686 0.1116  181 THR I CA  
18887 C C   . THR J 202 ? 2.1893 4.0492 3.6823 0.3230  -0.6402 0.1441  181 THR I C   
18888 O O   . THR J 202 ? 2.0456 4.0027 3.6453 0.4129  -0.5933 0.1460  181 THR I O   
18889 C CB  . THR J 202 ? 2.0455 3.9010 3.5171 0.4175  -0.7099 0.1226  181 THR I CB  
18890 O OG1 . THR J 202 ? 1.8721 3.8348 3.4559 0.5166  -0.6460 0.1105  181 THR I OG1 
18891 C CG2 . THR J 202 ? 2.0265 3.8193 3.4152 0.3917  -0.7437 0.0925  181 THR I CG2 
18892 N N   . VAL J 203 ? 2.2584 4.0586 3.6988 0.2414  -0.6685 0.1698  182 VAL I N   
18893 C CA  . VAL J 203 ? 2.2493 4.0974 3.7566 0.2529  -0.6423 0.2009  182 VAL I CA  
18894 C C   . VAL J 203 ? 2.4194 4.2445 3.9210 0.2557  -0.7218 0.2549  182 VAL I C   
18895 O O   . VAL J 203 ? 2.5293 4.2718 3.9437 0.2041  -0.7930 0.2650  182 VAL I O   
18896 C CB  . VAL J 203 ? 2.1431 3.9537 3.6069 0.1484  -0.5804 0.1785  182 VAL I CB  
18897 C CG1 . VAL J 203 ? 1.9404 3.7972 3.4384 0.1640  -0.4924 0.1299  182 VAL I CG1 
18898 C CG2 . VAL J 203 ? 2.2105 3.9001 3.5398 0.0233  -0.6213 0.1695  182 VAL I CG2 
18899 N N   . PRO J 204 ? 2.2189 4.1154 3.8120 0.3155  -0.7125 0.2904  183 PRO I N   
18900 C CA  . PRO J 204 ? 2.3407 4.2181 3.9320 0.3159  -0.7847 0.3424  183 PRO I CA  
18901 C C   . PRO J 204 ? 2.4912 4.2689 3.9810 0.1867  -0.8072 0.3497  183 PRO I C   
18902 O O   . PRO J 204 ? 2.4776 4.2299 3.9344 0.1088  -0.7491 0.3251  183 PRO I O   
18903 C CB  . PRO J 204 ? 2.2141 4.1940 3.9271 0.3973  -0.7477 0.3700  183 PRO I CB  
18904 C CG  . PRO J 204 ? 2.0171 4.0439 3.7694 0.3968  -0.6503 0.3317  183 PRO I CG  
18905 C CD  . PRO J 204 ? 2.0308 4.0317 3.7362 0.3897  -0.6360 0.2849  183 PRO I CD  
18906 N N   . SER J 205 ? 2.6477 4.3681 4.0874 0.1646  -0.8935 0.3839  184 SER I N   
18907 C CA  . SER J 205 ? 2.7795 4.3986 4.1164 0.0424  -0.9254 0.3932  184 SER I CA  
18908 C C   . SER J 205 ? 2.7757 4.4142 4.1444 0.0045  -0.8823 0.4108  184 SER I C   
18909 O O   . SER J 205 ? 2.8457 4.4092 4.1340 -0.1063 -0.8751 0.4040  184 SER I O   
18910 C CB  . SER J 205 ? 2.9255 4.4913 4.2182 0.0409  -1.0282 0.4317  184 SER I CB  
18911 O OG  . SER J 205 ? 2.9411 4.4852 4.2011 0.0745  -1.0719 0.4169  184 SER I OG  
18912 N N   . SER J 206 ? 2.6573 4.3948 4.1413 0.0940  -0.8540 0.4335  185 SER I N   
18913 C CA  . SER J 206 ? 2.6471 4.4144 4.1739 0.0705  -0.8106 0.4517  185 SER I CA  
18914 C C   . SER J 206 ? 2.5563 4.3287 4.0755 0.0200  -0.7178 0.4079  185 SER I C   
18915 O O   . SER J 206 ? 2.4308 4.2891 4.0378 0.0865  -0.6506 0.3931  185 SER I O   
18916 C CB  . SER J 206 ? 2.5886 4.4647 4.2435 0.1879  -0.8049 0.4854  185 SER I CB  
18917 O OG  . SER J 206 ? 2.4483 4.4072 4.1804 0.2803  -0.7545 0.4596  185 SER I OG  
18918 N N   . SER J 207 ? 2.5697 4.2479 3.9814 -0.0998 -0.7138 0.3856  186 SER I N   
18919 C CA  . SER J 207 ? 2.5644 4.2407 3.9616 -0.1553 -0.6276 0.3426  186 SER I CA  
18920 C C   . SER J 207 ? 2.6530 4.2494 3.9695 -0.2808 -0.6226 0.3460  186 SER I C   
18921 O O   . SER J 207 ? 2.7149 4.2466 3.9492 -0.3721 -0.5936 0.3093  186 SER I O   
18922 C CB  . SER J 207 ? 2.5814 4.2294 3.9275 -0.1683 -0.6102 0.2933  186 SER I CB  
18923 O OG  . SER J 207 ? 2.4997 4.2210 3.9197 -0.0527 -0.6138 0.2893  186 SER I OG  
18924 N N   . LEU J 208 ? 2.8553 4.4558 4.1947 -0.2864 -0.6519 0.3910  187 LEU I N   
18925 C CA  . LEU J 208 ? 2.9853 4.5195 4.2598 -0.3989 -0.6429 0.3974  187 LEU I CA  
18926 C C   . LEU J 208 ? 2.9350 4.5037 4.2397 -0.4253 -0.5451 0.3664  187 LEU I C   
18927 O O   . LEU J 208 ? 3.0041 4.5051 4.2289 -0.5304 -0.5159 0.3401  187 LEU I O   
18928 C CB  . LEU J 208 ? 3.0450 4.5855 4.3481 -0.3888 -0.6940 0.4533  187 LEU I CB  
18929 C CG  . LEU J 208 ? 3.0894 4.5395 4.3043 -0.5100 -0.7167 0.4686  187 LEU I CG  
18930 C CD1 . LEU J 208 ? 3.2160 4.6839 4.4510 -0.5589 -0.6377 0.4576  187 LEU I CD1 
18931 C CD2 . LEU J 208 ? 3.1555 4.4942 4.2393 -0.6081 -0.7504 0.4422  187 LEU I CD2 
18932 N N   . GLY J 209 ? 2.9362 4.6104 4.3567 -0.3295 -0.4945 0.3695  188 GLY I N   
18933 C CA  . GLY J 209 ? 2.7800 4.5043 4.2480 -0.3302 -0.3994 0.3393  188 GLY I CA  
18934 C C   . GLY J 209 ? 2.9044 4.5876 4.3313 -0.4324 -0.3536 0.3321  188 GLY I C   
18935 O O   . GLY J 209 ? 3.0636 4.7658 4.5262 -0.4355 -0.3556 0.3671  188 GLY I O   
18936 N N   . THR J 210 ? 2.7948 4.4234 4.1483 -0.5153 -0.3114 0.2865  189 THR I N   
18937 C CA  . THR J 210 ? 2.7593 4.3609 4.0655 -0.5158 -0.3140 0.2464  189 THR I CA  
18938 C C   . THR J 210 ? 2.6096 4.3036 4.0050 -0.4186 -0.2546 0.2173  189 THR I C   
18939 O O   . THR J 210 ? 2.5391 4.2708 3.9700 -0.4238 -0.1746 0.1889  189 THR I O   
18940 C CB  . THR J 210 ? 2.8186 4.3291 4.0134 -0.6425 -0.2865 0.2057  189 THR I CB  
18941 O OG1 . THR J 210 ? 2.7641 4.3063 3.9910 -0.6690 -0.1993 0.1820  189 THR I OG1 
18942 C CG2 . THR J 210 ? 2.9745 4.3851 4.0703 -0.7436 -0.3487 0.2313  189 THR I CG2 
18943 N N   . GLN J 211 ? 2.7547 4.4845 4.1864 -0.3287 -0.2955 0.2250  190 GLN I N   
18944 C CA  . GLN J 211 ? 2.5884 4.3976 4.0944 -0.2385 -0.2461 0.1951  190 GLN I CA  
18945 C C   . GLN J 211 ? 2.6104 4.3629 4.0355 -0.3060 -0.2165 0.1409  190 GLN I C   
18946 O O   . GLN J 211 ? 2.6876 4.3993 4.0591 -0.3066 -0.2616 0.1289  190 GLN I O   
18947 C CB  . GLN J 211 ? 2.5430 4.4021 4.1060 -0.1269 -0.3020 0.2199  190 GLN I CB  
18948 C CG  . GLN J 211 ? 2.4073 4.3468 4.0453 -0.0286 -0.2588 0.1909  190 GLN I CG  
18949 C CD  . GLN J 211 ? 2.3064 4.3191 4.0219 -0.0023 -0.1653 0.1698  190 GLN I CD  
18950 O OE1 . GLN J 211 ? 2.2730 4.2674 3.9565 -0.0538 -0.1056 0.1251  190 GLN I OE1 
18951 N NE2 . GLN J 211 ? 2.2633 4.3597 4.0816 0.0786  -0.1521 0.2018  190 GLN I NE2 
18952 N N   . THR J 212 ? 2.6124 4.3605 4.0267 -0.3652 -0.1413 0.1081  191 THR I N   
18953 C CA  . THR J 212 ? 2.6250 4.3127 3.9558 -0.4461 -0.1082 0.0563  191 THR I CA  
18954 C C   . THR J 212 ? 2.5314 4.2550 3.8852 -0.3782 -0.0952 0.0217  191 THR I C   
18955 O O   . THR J 212 ? 2.4125 4.2235 3.8581 -0.2966 -0.0390 0.0063  191 THR I O   
18956 C CB  . THR J 212 ? 2.6111 4.3040 3.9460 -0.5070 -0.0244 0.0304  191 THR I CB  
18957 O OG1 . THR J 212 ? 2.6164 4.2610 3.8803 -0.5767 0.0145  -0.0234 191 THR I OG1 
18958 C CG2 . THR J 212 ? 2.4894 4.2945 3.9516 -0.4117 0.0401  0.0323  191 THR I CG2 
18959 N N   . TYR J 213 ? 2.4798 4.1360 3.7506 -0.4103 -0.1487 0.0102  192 TYR I N   
18960 C CA  . TYR J 213 ? 2.4092 4.0849 3.6847 -0.3599 -0.1418 -0.0248 192 TYR I CA  
18961 C C   . TYR J 213 ? 2.4295 4.0480 3.6245 -0.4515 -0.0950 -0.0797 192 TYR I C   
18962 O O   . TYR J 213 ? 2.5372 4.0599 3.6220 -0.5464 -0.1326 -0.0879 192 TYR I O   
18963 C CB  . TYR J 213 ? 2.4613 4.1029 3.7006 -0.3302 -0.2321 -0.0020 192 TYR I CB  
18964 C CG  . TYR J 213 ? 2.4325 4.1384 3.7578 -0.2272 -0.2774 0.0479  192 TYR I CG  
18965 C CD1 . TYR J 213 ? 2.3165 4.1289 3.7629 -0.1284 -0.2297 0.0561  192 TYR I CD1 
18966 C CD2 . TYR J 213 ? 2.5277 4.1881 3.8133 -0.2284 -0.3678 0.0865  192 TYR I CD2 
18967 C CE1 . TYR J 213 ? 2.2954 4.1681 3.8209 -0.0342 -0.2698 0.1008  192 TYR I CE1 
18968 C CE2 . TYR J 213 ? 2.5083 4.2287 3.8735 -0.1338 -0.4088 0.1313  192 TYR I CE2 
18969 C CZ  . TYR J 213 ? 2.3919 4.2187 3.8769 -0.0373 -0.3592 0.1382  192 TYR I CZ  
18970 O OH  . TYR J 213 ? 2.3777 4.2650 3.9419 0.0566  -0.3997 0.1825  192 TYR I OH  
18971 N N   . ILE J 214 ? 2.4122 4.0899 3.6626 -0.4232 -0.0128 -0.1173 193 ILE I N   
18972 C CA  . ILE J 214 ? 2.4538 4.0908 3.6420 -0.5001 0.0412  -0.1727 193 ILE I CA  
18973 C C   . ILE J 214 ? 2.3766 4.0630 3.6033 -0.4259 0.0663  -0.2091 193 ILE I C   
18974 O O   . ILE J 214 ? 2.2788 4.0584 3.6084 -0.3353 0.1157  -0.2152 193 ILE I O   
18975 C CB  . ILE J 214 ? 2.4495 4.1055 3.6611 -0.5463 0.1217  -0.1896 193 ILE I CB  
18976 C CG1 . ILE J 214 ? 2.5366 4.1369 3.7021 -0.6271 0.0951  -0.1547 193 ILE I CG1 
18977 C CG2 . ILE J 214 ? 2.4406 4.0623 3.5959 -0.6178 0.1810  -0.2491 193 ILE I CG2 
18978 C CD1 . ILE J 214 ? 2.5256 4.1406 3.7111 -0.6762 0.1705  -0.1681 193 ILE I CD1 
18979 N N   . CYS J 215 ? 2.5876 4.2116 3.7316 -0.4639 0.0323  -0.2329 194 CYS I N   
18980 C CA  . CYS J 215 ? 2.5201 4.1813 3.6887 -0.4040 0.0539  -0.2702 194 CYS I CA  
18981 C C   . CYS J 215 ? 2.4767 4.1374 3.6298 -0.4567 0.1386  -0.3266 194 CYS I C   
18982 O O   . CYS J 215 ? 2.5526 4.1390 3.6189 -0.5698 0.1522  -0.3457 194 CYS I O   
18983 C CB  . CYS J 215 ? 2.5568 4.1499 3.6422 -0.4229 -0.0211 -0.2706 194 CYS I CB  
18984 S SG  . CYS J 215 ? 2.7035 4.1582 3.6275 -0.5866 -0.0467 -0.2913 194 CYS I SG  
18985 N N   . ASN J 216 ? 2.4630 4.2068 3.7002 -0.3748 0.1957  -0.3538 195 ASN I N   
18986 C CA  . ASN J 216 ? 2.3732 4.1272 3.6080 -0.4128 0.2795  -0.4083 195 ASN I CA  
18987 C C   . ASN J 216 ? 2.3278 4.0632 3.5218 -0.4103 0.2784  -0.4511 195 ASN I C   
18988 O O   . ASN J 216 ? 2.2078 4.0031 3.4641 -0.3107 0.2718  -0.4530 195 ASN I O   
18989 C CB  . ASN J 216 ? 2.2124 4.0706 3.5682 -0.3306 0.3512  -0.4122 195 ASN I CB  
18990 C CG  . ASN J 216 ? 2.2566 4.1365 3.6560 -0.3314 0.3555  -0.3706 195 ASN I CG  
18991 O OD1 . ASN J 216 ? 2.3911 4.2139 3.7377 -0.3825 0.2995  -0.3346 195 ASN I OD1 
18992 N ND2 . ASN J 216 ? 2.1390 4.0996 3.6328 -0.2781 0.4231  -0.3764 195 ASN I ND2 
18993 N N   . VAL J 217 ? 2.4688 4.1223 3.5592 -0.5201 0.2867  -0.4859 196 VAL I N   
18994 C CA  . VAL J 217 ? 2.4483 4.0712 3.4843 -0.5372 0.2862  -0.5293 196 VAL I CA  
18995 C C   . VAL J 217 ? 2.3317 3.9827 3.3856 -0.5598 0.3778  -0.5849 196 VAL I C   
18996 O O   . VAL J 217 ? 2.3677 3.9903 3.3910 -0.6422 0.4220  -0.5996 196 VAL I O   
18997 C CB  . VAL J 217 ? 2.6265 4.1334 3.5280 -0.6473 0.2271  -0.5295 196 VAL I CB  
18998 C CG1 . VAL J 217 ? 2.6167 4.0909 3.4604 -0.6668 0.2260  -0.5740 196 VAL I CG1 
18999 C CG2 . VAL J 217 ? 2.7414 4.2197 3.6260 -0.6263 0.1361  -0.4736 196 VAL I CG2 
19000 N N   . ASN J 218 ? 2.5657 4.2721 3.6688 -0.4872 0.4063  -0.6163 197 ASN I N   
19001 C CA  . ASN J 218 ? 2.4456 4.1850 3.5723 -0.4977 0.4922  -0.6710 197 ASN I CA  
19002 C C   . ASN J 218 ? 2.4174 4.1251 3.4874 -0.5140 0.4867  -0.7141 197 ASN I C   
19003 O O   . ASN J 218 ? 2.3795 4.1000 3.4603 -0.4472 0.4387  -0.7039 197 ASN I O   
19004 C CB  . ASN J 218 ? 2.2521 4.1055 3.5125 -0.3842 0.5472  -0.6699 197 ASN I CB  
19005 C CG  . ASN J 218 ? 2.1163 4.0072 3.4052 -0.3870 0.6342  -0.7276 197 ASN I CG  
19006 O OD1 . ASN J 218 ? 2.1827 4.0159 3.3943 -0.4820 0.6615  -0.7680 197 ASN I OD1 
19007 N ND2 . ASN J 218 ? 1.9236 3.9121 3.3244 -0.2819 0.6776  -0.7317 197 ASN I ND2 
19008 N N   . HIS J 219 ? 2.4579 4.1261 3.4696 -0.6016 0.5374  -0.7631 198 HIS I N   
19009 C CA  . HIS J 219 ? 2.4498 4.0860 3.4039 -0.6288 0.5417  -0.8098 198 HIS I CA  
19010 C C   . HIS J 219 ? 2.3264 4.0070 3.3183 -0.6326 0.6343  -0.8650 198 HIS I C   
19011 O O   . HIS J 219 ? 2.4418 4.0823 3.3842 -0.7277 0.6785  -0.8925 198 HIS I O   
19012 C CB  . HIS J 219 ? 2.6604 4.1815 3.4776 -0.7528 0.4979  -0.8163 198 HIS I CB  
19013 C CG  . HIS J 219 ? 2.6684 4.1527 3.4230 -0.7737 0.4855  -0.8556 198 HIS I CG  
19014 N ND1 . HIS J 219 ? 2.8161 4.2091 3.4542 -0.8927 0.4816  -0.8856 198 HIS I ND1 
19015 C CD2 . HIS J 219 ? 2.5455 4.0724 3.3378 -0.6909 0.4769  -0.8702 198 HIS I CD2 
19016 C CE1 . HIS J 219 ? 2.7917 4.1729 3.3987 -0.8825 0.4711  -0.9169 198 HIS I CE1 
19017 N NE2 . HIS J 219 ? 2.6264 4.0878 3.3256 -0.7608 0.4681  -0.9083 198 HIS I NE2 
19018 N N   . LYS J 220 ? 2.4165 4.1799 3.4968 -0.5287 0.6635  -0.8807 199 LYS I N   
19019 C CA  . LYS J 220 ? 2.2855 4.0990 3.4121 -0.5214 0.7518  -0.9317 199 LYS I CA  
19020 C C   . LYS J 220 ? 2.3587 4.1070 3.3912 -0.6212 0.7766  -0.9862 199 LYS I C   
19021 O O   . LYS J 220 ? 2.3567 4.0978 3.3818 -0.6722 0.8411  -1.0185 199 LYS I O   
19022 C CB  . LYS J 220 ? 2.0786 3.9630 3.2922 -0.3880 0.7579  -0.9305 199 LYS I CB  
19023 C CG  . LYS J 220 ? 2.0118 3.9356 3.3028 -0.2745 0.7251  -0.8681 199 LYS I CG  
19024 C CD  . LYS J 220 ? 1.9583 3.8268 3.2541 -0.2144 0.7412  -0.8192 199 LYS I CD  
19025 C CE  . LYS J 220 ? 1.8618 3.7645 3.2238 -0.1075 0.7051  -0.7539 199 LYS I CE  
19026 N NZ  . LYS J 220 ? 1.7091 3.6028 3.0799 -0.0074 0.6715  -0.7298 199 LYS I NZ  
19027 N N   . PRO J 221 ? 2.3679 4.0591 3.3225 -0.6485 0.7260  -0.9965 200 PRO I N   
19028 C CA  . PRO J 221 ? 2.4466 4.0772 3.3122 -0.7455 0.7529  -1.0501 200 PRO I CA  
19029 C C   . PRO J 221 ? 2.6275 4.1774 3.4025 -0.8785 0.7641  -1.0568 200 PRO I C   
19030 O O   . PRO J 221 ? 2.6603 4.1778 3.3828 -0.9555 0.8097  -1.1061 200 PRO I O   
19031 C CB  . PRO J 221 ? 2.5020 4.0874 3.3053 -0.7388 0.6829  -1.0477 200 PRO I CB  
19032 C CG  . PRO J 221 ? 2.3530 4.0109 3.2483 -0.6076 0.6500  -1.0125 200 PRO I CG  
19033 C CD  . PRO J 221 ? 2.3399 4.0347 3.2991 -0.5760 0.6521  -0.9676 200 PRO I CD  
19034 N N   . SER J 222 ? 2.4576 3.9751 3.2134 -0.9083 0.7254  -1.0100 201 SER I N   
19035 C CA  . SER J 222 ? 2.5474 3.9897 3.2200 -1.0328 0.7356  -1.0139 201 SER I CA  
19036 C C   . SER J 222 ? 2.4990 3.9879 3.2419 -1.0193 0.7801  -0.9941 201 SER I C   
19037 O O   . SER J 222 ? 2.5621 3.9989 3.2509 -1.1138 0.7933  -0.9925 201 SER I O   
19038 C CB  . SER J 222 ? 2.6450 3.9962 3.2204 -1.0949 0.6481  -0.9751 201 SER I CB  
19039 O OG  . SER J 222 ? 2.7025 3.9993 3.2004 -1.1200 0.6030  -0.9922 201 SER I OG  
19040 N N   . ASN J 223 ? 2.7214 4.3075 3.5837 -0.9030 0.8036  -0.9797 202 ASN I N   
19041 C CA  . ASN J 223 ? 2.6127 4.2578 3.5590 -0.8684 0.8459  -0.9589 202 ASN I CA  
19042 C C   . ASN J 223 ? 2.7541 4.3488 3.6610 -0.9183 0.7972  -0.9082 202 ASN I C   
19043 O O   . ASN J 223 ? 2.7627 4.3686 3.6941 -0.9452 0.8337  -0.8982 202 ASN I O   
19044 C CB  . ASN J 223 ? 2.6176 4.2034 3.5223 -0.8897 0.8976  -0.9881 202 ASN I CB  
19045 C CG  . ASN J 223 ? 2.5092 4.0842 3.4165 -0.8200 0.9091  -1.0174 202 ASN I CG  
19046 O OD1 . ASN J 223 ? 2.4315 4.0591 3.4032 -0.7185 0.8908  -1.0030 202 ASN I OD1 
19047 N ND2 . ASN J 223 ? 2.5140 4.0162 3.3422 -0.8845 0.9314  -1.0593 202 ASN I ND2 
19048 N N   . THR J 224 ? 2.5251 4.0751 3.3849 -0.9138 0.7126  -0.8720 203 THR I N   
19049 C CA  . THR J 224 ? 2.6726 4.1632 3.4807 -0.9652 0.6529  -0.8235 203 THR I CA  
19050 C C   . THR J 224 ? 2.6295 4.1803 3.5243 -0.8597 0.6122  -0.7677 203 THR I C   
19051 O O   . THR J 224 ? 2.5837 4.1643 3.5102 -0.7762 0.5701  -0.7541 203 THR I O   
19052 C CB  . THR J 224 ? 2.8387 4.2277 3.5233 -1.0455 0.5845  -0.8228 203 THR I CB  
19053 O OG1 . THR J 224 ? 2.8844 4.2221 3.4919 -1.1399 0.6258  -0.8773 203 THR I OG1 
19054 C CG2 . THR J 224 ? 2.9930 4.3153 3.6182 -1.1120 0.5302  -0.7772 203 THR I CG2 
19055 N N   . LYS J 225 ? 2.5340 4.1024 3.4662 -0.8641 0.6244  -0.7358 204 LYS I N   
19056 C CA  . LYS J 225 ? 2.5012 4.1225 3.5118 -0.7747 0.5865  -0.6802 204 LYS I CA  
19057 C C   . LYS J 225 ? 2.6671 4.2187 3.6140 -0.8466 0.5317  -0.6364 204 LYS I C   
19058 O O   . LYS J 225 ? 2.7093 4.2459 3.6474 -0.9082 0.5664  -0.6339 204 LYS I O   
19059 C CB  . LYS J 225 ? 2.3491 4.0679 3.4773 -0.7015 0.6576  -0.6827 204 LYS I CB  
19060 C CG  . LYS J 225 ? 2.2904 4.0816 3.5172 -0.5947 0.6324  -0.6316 204 LYS I CG  
19061 C CD  . LYS J 225 ? 2.0967 3.9934 3.4409 -0.4958 0.7011  -0.6511 204 LYS I CD  
19062 C CE  . LYS J 225 ? 2.0591 3.9635 3.4091 -0.5530 0.7880  -0.6910 204 LYS I CE  
19063 N NZ  . LYS J 225 ? 1.9397 3.8269 3.3145 -0.4347 0.8062  -0.6748 204 LYS I NZ  
19064 N N   . VAL J 226 ? 2.5125 4.0249 3.4198 -0.8345 0.4460  -0.6010 205 VAL I N   
19065 C CA  . VAL J 226 ? 2.5950 4.0340 3.4335 -0.9030 0.3835  -0.5589 205 VAL I CA  
19066 C C   . VAL J 226 ? 2.5451 4.0288 3.4528 -0.8150 0.3301  -0.4996 205 VAL I C   
19067 O O   . VAL J 226 ? 2.5254 4.0382 3.4650 -0.7317 0.2846  -0.4838 205 VAL I O   
19068 C CB  . VAL J 226 ? 2.7043 4.0415 3.4182 -0.9839 0.3221  -0.5674 205 VAL I CB  
19069 C CG1 . VAL J 226 ? 2.8077 4.0696 3.4525 -1.0500 0.2526  -0.5210 205 VAL I CG1 
19070 C CG2 . VAL J 226 ? 2.7613 4.0487 3.3987 -1.0776 0.3722  -0.6272 205 VAL I CG2 
19071 N N   . ASP J 227 ? 2.5824 4.0692 3.5105 -0.8367 0.3349  -0.4668 206 ASP I N   
19072 C CA  . ASP J 227 ? 2.5974 4.1198 3.5849 -0.7691 0.2862  -0.4084 206 ASP I CA  
19073 C C   . ASP J 227 ? 2.7502 4.1776 3.6409 -0.8517 0.2100  -0.3741 206 ASP I C   
19074 O O   . ASP J 227 ? 2.8142 4.1885 3.6504 -0.9471 0.2242  -0.3734 206 ASP I O   
19075 C CB  . ASP J 227 ? 2.5260 4.1181 3.6040 -0.7366 0.3448  -0.3953 206 ASP I CB  
19076 C CG  . ASP J 227 ? 2.3581 4.0427 3.5311 -0.6565 0.4208  -0.4296 206 ASP I CG  
19077 O OD1 . ASP J 227 ? 2.2728 3.9887 3.4703 -0.5883 0.4109  -0.4451 206 ASP I OD1 
19078 O OD2 . ASP J 227 ? 2.3033 4.0336 3.5327 -0.6536 0.4873  -0.4374 206 ASP I OD2 
19079 N N   . LYS J 228 ? 2.7246 4.1324 3.5972 -0.8136 0.1291  -0.3439 207 LYS I N   
19080 C CA  . LYS J 228 ? 2.8500 4.1667 3.6302 -0.8867 0.0505  -0.3107 207 LYS I CA  
19081 C C   . LYS J 228 ? 2.8371 4.1850 3.6733 -0.8212 -0.0065 -0.2497 207 LYS I C   
19082 O O   . LYS J 228 ? 2.7594 4.1770 3.6761 -0.7096 -0.0255 -0.2320 207 LYS I O   
19083 C CB  . LYS J 228 ? 2.9038 4.1574 3.6005 -0.9089 -0.0045 -0.3267 207 LYS I CB  
19084 C CG  . LYS J 228 ? 3.0152 4.1657 3.6041 -0.9888 -0.0888 -0.2985 207 LYS I CG  
19085 C CD  . LYS J 228 ? 3.1173 4.1837 3.6130 -1.1219 -0.0756 -0.3076 207 LYS I CD  
19086 C CE  . LYS J 228 ? 3.1442 4.1751 3.5782 -1.1917 -0.0232 -0.3668 207 LYS I CE  
19087 N NZ  . LYS J 228 ? 3.2598 4.1803 3.5624 -1.2891 -0.0778 -0.3758 207 LYS I NZ  
19088 N N   . ARG J 229 ? 2.7108 4.0069 3.5037 -0.8912 -0.0342 -0.2179 208 ARG I N   
19089 C CA  . ARG J 229 ? 2.6934 4.0095 3.5293 -0.8428 -0.0912 -0.1591 208 ARG I CA  
19090 C C   . ARG J 229 ? 2.7872 4.0164 3.5320 -0.8874 -0.1867 -0.1318 208 ARG I C   
19091 O O   . ARG J 229 ? 2.8909 4.0247 3.5263 -1.0003 -0.2042 -0.1429 208 ARG I O   
19092 C CB  . ARG J 229 ? 2.6823 4.0153 3.5521 -0.8717 -0.0578 -0.1361 208 ARG I CB  
19093 C CG  . ARG J 229 ? 2.6620 4.0187 3.5791 -0.8173 -0.1188 -0.0751 208 ARG I CG  
19094 C CD  . ARG J 229 ? 2.6472 4.0319 3.6107 -0.8318 -0.0856 -0.0497 208 ARG I CD  
19095 N NE  . ARG J 229 ? 2.7805 4.0846 3.6570 -0.9585 -0.0732 -0.0564 208 ARG I NE  
19096 C CZ  . ARG J 229 ? 2.8785 4.1687 3.7568 -0.9924 -0.0878 -0.0190 208 ARG I CZ  
19097 N NH1 . ARG J 229 ? 2.8681 4.2204 3.8311 -0.9086 -0.1145 0.0266  208 ARG I NH1 
19098 N NH2 . ARG J 229 ? 2.9832 4.1984 3.7796 -1.1094 -0.0749 -0.0274 208 ARG I NH2 
19099 N N   . VAL J 230 ? 2.9424 4.2047 3.7326 -0.7984 -0.2477 -0.0963 209 VAL I N   
19100 C CA  . VAL J 230 ? 2.9853 4.1773 3.7041 -0.8195 -0.3431 -0.0671 209 VAL I CA  
19101 C C   . VAL J 230 ? 3.0109 4.1905 3.7389 -0.8287 -0.3913 -0.0120 209 VAL I C   
19102 O O   . VAL J 230 ? 2.9166 4.1768 3.7461 -0.7430 -0.3846 0.0188  209 VAL I O   
19103 C CB  . VAL J 230 ? 2.7999 4.0333 3.5600 -0.7158 -0.3843 -0.0629 209 VAL I CB  
19104 C CG1 . VAL J 230 ? 2.8271 3.9882 3.5160 -0.7375 -0.4838 -0.0303 209 VAL I CG1 
19105 C CG2 . VAL J 230 ? 2.7486 3.9834 3.4876 -0.7159 -0.3433 -0.1173 209 VAL I CG2 
19106 N N   . GLU J 231 ? 2.9901 4.0689 3.6120 -0.9333 -0.4397 0.0004  210 GLU I N   
19107 C CA  . GLU J 231 ? 2.9717 4.0288 3.5913 -0.9522 -0.4894 0.0518  210 GLU I CA  
19108 C C   . GLU J 231 ? 3.0174 3.9875 3.5464 -0.9905 -0.5861 0.0742  210 GLU I C   
19109 O O   . GLU J 231 ? 3.1166 4.0049 3.5428 -1.0693 -0.6013 0.0460  210 GLU I O   
19110 C CB  . GLU J 231 ? 3.0118 4.0257 3.5875 -1.0578 -0.4470 0.0464  210 GLU I CB  
19111 C CG  . GLU J 231 ? 2.9919 4.0825 3.6485 -1.0337 -0.3509 0.0245  210 GLU I CG  
19112 C CD  . GLU J 231 ? 3.1702 4.2077 3.7701 -1.1473 -0.3105 0.0145  210 GLU I CD  
19113 O OE1 . GLU J 231 ? 3.2630 4.2009 3.7546 -1.2490 -0.3537 0.0190  210 GLU I OE1 
19114 O OE2 . GLU J 231 ? 3.2228 4.3170 3.8849 -1.1359 -0.2352 0.0010  210 GLU I OE2 
19115 N N   . PRO J 232 ? 3.0873 4.0721 3.6512 -0.9369 -0.6536 0.1250  211 PRO I N   
19116 C CA  . PRO J 232 ? 3.1035 4.0086 3.5872 -0.9670 -0.7502 0.1507  211 PRO I CA  
19117 C C   . PRO J 232 ? 3.2102 4.0001 3.5696 -1.1059 -0.7757 0.1506  211 PRO I C   
19118 O O   . PRO J 232 ? 3.2189 3.9943 3.5780 -1.1451 -0.7827 0.1806  211 PRO I O   
19119 C CB  . PRO J 232 ? 2.9663 3.9261 3.5318 -0.8816 -0.7992 0.2060  211 PRO I CB  
19120 C CG  . PRO J 232 ? 2.8129 3.8928 3.5084 -0.7764 -0.7334 0.2014  211 PRO I CG  
19121 C CD  . PRO J 232 ? 2.9415 4.0261 3.6295 -0.8348 -0.6417 0.1598  211 PRO I CD  
19122 N N   . ALA K 1   ? 2.9108 4.6277 3.9403 -0.0829 -0.5831 -0.2704 6   ALA J N   
19123 C CA  . ALA K 1   ? 2.8863 4.6011 3.9027 -0.0791 -0.5853 -0.2731 6   ALA J CA  
19124 C C   . ALA K 1   ? 2.8902 4.5909 3.8984 -0.0711 -0.5696 -0.2670 6   ALA J C   
19125 O O   . ALA K 1   ? 2.8352 4.5144 3.8176 -0.0653 -0.5682 -0.2712 6   ALA J O   
19126 C CB  . ALA K 1   ? 2.7850 4.5324 3.8234 -0.0846 -0.5949 -0.2719 6   ALA J CB  
19127 N N   . PRO K 2   ? 3.0051 4.7177 4.0344 -0.0705 -0.5578 -0.2569 7   PRO J N   
19128 C CA  . PRO K 2   ? 2.8569 4.5567 3.8793 -0.0629 -0.5429 -0.2507 7   PRO J CA  
19129 C C   . PRO K 2   ? 2.7245 4.3924 3.7258 -0.0571 -0.5321 -0.2508 7   PRO J C   
19130 O O   . PRO K 2   ? 2.7895 4.4505 3.7914 -0.0594 -0.5325 -0.2521 7   PRO J O   
19131 C CB  . PRO K 2   ? 2.8187 4.5449 3.8737 -0.0653 -0.5355 -0.2402 7   PRO J CB  
19132 C CG  . PRO K 2   ? 2.8588 4.5992 3.9317 -0.0723 -0.5411 -0.2401 7   PRO J CG  
19133 C CD  . PRO K 2   ? 2.9365 4.6764 3.9981 -0.0766 -0.5577 -0.2505 7   PRO J CD  
19134 N N   . THR K 3   ? 2.5658 4.2139 3.5479 -0.0492 -0.5226 -0.2495 8   THR J N   
19135 C CA  . THR K 3   ? 2.5961 4.2136 3.5568 -0.0425 -0.5114 -0.2493 8   THR J CA  
19136 C C   . THR K 3   ? 2.5674 4.1820 3.5331 -0.0364 -0.4947 -0.2393 8   THR J C   
19137 O O   . THR K 3   ? 2.5262 4.1562 3.5032 -0.0358 -0.4928 -0.2346 8   THR J O   
19138 C CB  . THR K 3   ? 2.6221 4.2128 3.5480 -0.0378 -0.5168 -0.2589 8   THR J CB  
19139 O OG1 . THR K 3   ? 2.6193 4.2136 3.5387 -0.0350 -0.5185 -0.2592 8   THR J OG1 
19140 C CG2 . THR K 3   ? 2.6546 4.2460 3.5749 -0.0437 -0.5329 -0.2689 8   THR J CG2 
19141 N N   . PHE K 4   ? 2.4813 4.0759 3.4386 -0.0318 -0.4825 -0.2362 9   PHE J N   
19142 C CA  . PHE K 4   ? 2.4595 4.0498 3.4213 -0.0258 -0.4658 -0.2264 9   PHE J CA  
19143 C C   . PHE K 4   ? 2.4972 4.0535 3.4298 -0.0171 -0.4555 -0.2278 9   PHE J C   
19144 O O   . PHE K 4   ? 2.5461 4.0841 3.4630 -0.0166 -0.4582 -0.2340 9   PHE J O   
19145 C CB  . PHE K 4   ? 2.4449 4.0524 3.4357 -0.0297 -0.4586 -0.2179 9   PHE J CB  
19146 C CG  . PHE K 4   ? 2.4044 4.0470 3.4263 -0.0369 -0.4653 -0.2141 9   PHE J CG  
19147 C CD1 . PHE K 4   ? 2.4167 4.0768 3.4516 -0.0450 -0.4789 -0.2188 9   PHE J CD1 
19148 C CD2 . PHE K 4   ? 2.3597 4.0181 3.3984 -0.0353 -0.4579 -0.2058 9   PHE J CD2 
19149 C CE1 . PHE K 4   ? 2.3860 4.0790 3.4495 -0.0511 -0.4848 -0.2152 9   PHE J CE1 
19150 C CE2 . PHE K 4   ? 2.3288 4.0195 3.3960 -0.0414 -0.4640 -0.2026 9   PHE J CE2 
19151 C CZ  . PHE K 4   ? 2.3426 4.0508 3.4220 -0.0492 -0.4774 -0.2073 9   PHE J CZ  
19152 N N   . VAL K 5   ? 2.3535 3.9020 3.2794 -0.0100 -0.4438 -0.2219 11  VAL J N   
19153 C CA  . VAL K 5   ? 2.4496 3.9677 3.3494 -0.0008 -0.4321 -0.2214 11  VAL J CA  
19154 C C   . VAL K 5   ? 2.4733 3.9943 3.3856 0.0037  -0.4153 -0.2096 11  VAL J C   
19155 O O   . VAL K 5   ? 2.3781 3.9110 3.2990 0.0050  -0.4125 -0.2043 11  VAL J O   
19156 C CB  . VAL K 5   ? 2.4013 3.9012 3.2712 0.0048  -0.4362 -0.2281 11  VAL J CB  
19157 C CG1 . VAL K 5   ? 2.4823 3.9537 3.3283 0.0149  -0.4223 -0.2258 11  VAL J CG1 
19158 C CG2 . VAL K 5   ? 2.2820 3.7744 3.1364 0.0013  -0.4516 -0.2401 11  VAL J CG2 
19159 N N   . SER K 6   ? 2.4037 3.9140 3.3175 0.0061  -0.4042 -0.2054 12  SER J N   
19160 C CA  . SER K 6   ? 2.3950 3.9070 3.3205 0.0105  -0.3878 -0.1941 12  SER J CA  
19161 C C   . SER K 6   ? 2.4604 3.9417 3.3566 0.0209  -0.3764 -0.1939 12  SER J C   
19162 O O   . SER K 6   ? 2.5655 4.0247 3.4421 0.0237  -0.3759 -0.1994 12  SER J O   
19163 C CB  . SER K 6   ? 2.4768 3.9990 3.4254 0.0063  -0.3823 -0.1885 12  SER J CB  
19164 O OG  . SER K 6   ? 2.5965 4.0988 3.5306 0.0073  -0.3825 -0.1939 12  SER J OG  
19165 N N   . VAL K 7   ? 2.5933 4.0736 3.4872 0.0266  -0.3674 -0.1874 13  VAL J N   
19166 C CA  . VAL K 7   ? 2.6379 4.0914 3.5050 0.0369  -0.3562 -0.1861 13  VAL J CA  
19167 C C   . VAL K 7   ? 2.6478 4.1054 3.5283 0.0413  -0.3397 -0.1736 13  VAL J C   
19168 O O   . VAL K 7   ? 2.5456 4.0250 3.4480 0.0385  -0.3392 -0.1672 13  VAL J O   
19169 C CB  . VAL K 7   ? 2.5031 3.9474 3.3472 0.0405  -0.3631 -0.1919 13  VAL J CB  
19170 C CG1 . VAL K 7   ? 2.5311 3.9493 3.3490 0.0516  -0.3506 -0.1894 13  VAL J CG1 
19171 C CG2 . VAL K 7   ? 2.4827 3.9210 3.3119 0.0366  -0.3790 -0.2045 13  VAL J CG2 
19172 N N   . ALA K 8   ? 2.6720 4.1089 3.5396 0.0484  -0.3265 -0.1702 14  ALA J N   
19173 C CA  . ALA K 8   ? 2.6603 4.0983 3.5381 0.0534  -0.3100 -0.1584 14  ALA J CA  
19174 C C   . ALA K 8   ? 2.5588 3.9964 3.4296 0.0587  -0.3062 -0.1542 14  ALA J C   
19175 O O   . ALA K 8   ? 2.5198 3.9441 3.3665 0.0623  -0.3120 -0.1607 14  ALA J O   
19176 C CB  . ALA K 8   ? 2.7630 4.1761 3.6239 0.0606  -0.2973 -0.1569 14  ALA J CB  
19177 N N   . PRO K 9   ? 2.6441 4.0965 3.5363 0.0592  -0.2969 -0.1434 15  PRO J N   
19178 C CA  . PRO K 9   ? 2.5491 4.0024 3.4375 0.0641  -0.2929 -0.1385 15  PRO J CA  
19179 C C   . PRO K 9   ? 2.5781 4.0025 3.4342 0.0748  -0.2840 -0.1388 15  PRO J C   
19180 O O   . PRO K 9   ? 2.6643 4.0717 3.5104 0.0803  -0.2724 -0.1359 15  PRO J O   
19181 C CB  . PRO K 9   ? 2.4675 3.9390 3.3852 0.0633  -0.2819 -0.1261 15  PRO J CB  
19182 C CG  . PRO K 9   ? 2.4601 3.9495 3.4021 0.0548  -0.2866 -0.1266 15  PRO J CG  
19183 C CD  . PRO K 9   ? 2.5991 4.0703 3.5222 0.0546  -0.2905 -0.1352 15  PRO J CD  
19184 N N   . GLY K 10  ? 2.5723 3.9913 3.4120 0.0778  -0.2895 -0.1422 16  GLY J N   
19185 C CA  . GLY K 10  ? 2.5533 3.9464 3.3623 0.0880  -0.2817 -0.1424 16  GLY J CA  
19186 C C   . GLY K 10  ? 2.6473 4.0188 3.4261 0.0901  -0.2894 -0.1542 16  GLY J C   
19187 O O   . GLY K 10  ? 2.6891 4.0394 3.4401 0.0986  -0.2854 -0.1560 16  GLY J O   
19188 N N   . GLN K 11  ? 2.5831 3.9596 3.3670 0.0829  -0.3005 -0.1623 17  GLN J N   
19189 C CA  . GLN K 11  ? 2.6552 4.0119 3.4123 0.0842  -0.3086 -0.1740 17  GLN J CA  
19190 C C   . GLN K 11  ? 2.5666 3.9275 3.3141 0.0811  -0.3241 -0.1825 17  GLN J C   
19191 O O   . GLN K 11  ? 2.4671 3.8374 3.2189 0.0819  -0.3248 -0.1787 17  GLN J O   
19192 C CB  . GLN K 11  ? 2.7344 4.0946 3.5027 0.0778  -0.3129 -0.1780 17  GLN J CB  
19193 C CG  . GLN K 11  ? 2.8710 4.2044 3.6144 0.0834  -0.3093 -0.1838 17  GLN J CG  
19194 C CD  . GLN K 11  ? 2.9431 4.2612 3.6787 0.0928  -0.2910 -0.1753 17  GLN J CD  
19195 O OE1 . GLN K 11  ? 2.9822 4.3129 3.7391 0.0925  -0.2805 -0.1645 17  GLN J OE1 
19196 N NE2 . GLN K 11  ? 2.9614 4.2524 3.6662 0.1012  -0.2870 -0.1802 17  GLN J NE2 
19197 N N   . THR K 12  ? 2.6729 4.0266 3.4075 0.0777  -0.3366 -0.1940 18  THR J N   
19198 C CA  . THR K 12  ? 2.5912 3.9476 3.3152 0.0748  -0.3517 -0.2028 18  THR J CA  
19199 C C   . THR K 12  ? 2.5570 3.9305 3.2973 0.0641  -0.3669 -0.2097 18  THR J C   
19200 O O   . THR K 12  ? 2.6449 4.0123 3.3844 0.0616  -0.3691 -0.2142 18  THR J O   
19201 C CB  . THR K 12  ? 2.6580 3.9857 3.3443 0.0825  -0.3532 -0.2112 18  THR J CB  
19202 O OG1 . THR K 12  ? 2.7034 4.0157 3.3744 0.0929  -0.3388 -0.2043 18  THR J OG1 
19203 C CG2 . THR K 12  ? 2.5603 3.8902 3.2349 0.0799  -0.3685 -0.2201 18  THR J CG2 
19204 N N   . ALA K 13  ? 2.6872 4.0822 3.4426 0.0578  -0.3775 -0.2105 19  ALA J N   
19205 C CA  . ALA K 13  ? 2.6812 4.0943 3.4525 0.0476  -0.3924 -0.2169 19  ALA J CA  
19206 C C   . ALA K 13  ? 2.5947 4.0009 3.3452 0.0465  -0.4074 -0.2283 19  ALA J C   
19207 O O   . ALA K 13  ? 2.5236 3.9241 3.2596 0.0510  -0.4081 -0.2289 19  ALA J O   
19208 C CB  . ALA K 13  ? 2.5773 4.0220 3.3827 0.0407  -0.3945 -0.2100 19  ALA J CB  
19209 N N   . ARG K 14  ? 2.4958 3.9029 3.2457 0.0405  -0.4193 -0.2371 20  ARG J N   
19210 C CA  . ARG K 14  ? 2.4377 3.8396 3.1699 0.0383  -0.4347 -0.2486 20  ARG J CA  
19211 C C   . ARG K 14  ? 2.3816 3.8074 3.1367 0.0273  -0.4488 -0.2525 20  ARG J C   
19212 O O   . ARG K 14  ? 2.4452 3.8784 3.2170 0.0226  -0.4479 -0.2509 20  ARG J O   
19213 C CB  . ARG K 14  ? 2.5317 3.9024 3.2308 0.0449  -0.4337 -0.2563 20  ARG J CB  
19214 C CG  . ARG K 14  ? 2.6678 4.0263 3.3661 0.0458  -0.4275 -0.2565 20  ARG J CG  
19215 C CD  . ARG K 14  ? 2.7592 4.0864 3.4216 0.0537  -0.4270 -0.2646 20  ARG J CD  
19216 N NE  . ARG K 14  ? 2.8179 4.1292 3.4661 0.0641  -0.4110 -0.2577 20  ARG J NE  
19217 C CZ  . ARG K 14  ? 2.8071 4.1030 3.4300 0.0719  -0.4089 -0.2594 20  ARG J CZ  
19218 N NH1 . ARG K 14  ? 2.7418 4.0355 3.3499 0.0707  -0.4218 -0.2681 20  ARG J NH1 
19219 N NH2 . ARG K 14  ? 2.8621 4.1452 3.4749 0.0811  -0.3937 -0.2521 20  ARG J NH2 
19220 N N   . ILE K 15  ? 2.4912 3.9292 3.2471 0.0233  -0.4616 -0.2574 21  ILE J N   
19221 C CA  . ILE K 15  ? 2.4168 3.8807 3.1955 0.0131  -0.4753 -0.2604 21  ILE J CA  
19222 C C   . ILE K 15  ? 2.3719 3.8305 3.1337 0.0100  -0.4918 -0.2726 21  ILE J C   
19223 O O   . ILE K 15  ? 2.3214 3.7690 3.0621 0.0141  -0.4955 -0.2771 21  ILE J O   
19224 C CB  . ILE K 15  ? 2.3015 3.7913 3.1036 0.0103  -0.4756 -0.2535 21  ILE J CB  
19225 C CG1 . ILE K 15  ? 2.3374 3.8365 3.1611 0.0119  -0.4606 -0.2413 21  ILE J CG1 
19226 C CG2 . ILE K 15  ? 2.2144 3.7296 3.0353 0.0007  -0.4915 -0.2582 21  ILE J CG2 
19227 C CD1 . ILE K 15  ? 2.2315 3.7538 3.0769 0.0104  -0.4596 -0.2343 21  ILE J CD1 
19228 N N   . THR K 16  ? 2.1189 3.5862 2.8909 0.0026  -0.5018 -0.2777 22  THR J N   
19229 C CA  . THR K 16  ? 2.0722 3.5364 2.8313 -0.0014 -0.5181 -0.2892 22  THR J CA  
19230 C C   . THR K 16  ? 1.9617 3.4572 2.7464 -0.0105 -0.5303 -0.2894 22  THR J C   
19231 O O   . THR K 16  ? 1.9670 3.4836 2.7795 -0.0163 -0.5293 -0.2840 22  THR J O   
19232 C CB  . THR K 16  ? 2.1707 3.6205 2.9217 -0.0029 -0.5210 -0.2952 22  THR J CB  
19233 O OG1 . THR K 16  ? 2.2203 3.6874 2.9996 -0.0088 -0.5183 -0.2894 22  THR J OG1 
19234 C CG2 . THR K 16  ? 2.2779 3.6958 3.0017 0.0066  -0.5100 -0.2961 22  THR J CG2 
19235 N N   . CYS K 17  ? 2.3577 3.8561 3.1322 -0.0117 -0.5419 -0.2960 23  CYS J N   
19236 C CA  . CYS K 17  ? 2.2506 3.7768 3.0449 -0.0195 -0.5548 -0.2976 23  CYS J CA  
19237 C C   . CYS K 17  ? 2.1933 3.7123 2.9679 -0.0213 -0.5700 -0.3091 23  CYS J C   
19238 O O   . CYS K 17  ? 2.2110 3.7050 2.9561 -0.0151 -0.5693 -0.3145 23  CYS J O   
19239 C CB  . CYS K 17  ? 2.1738 3.7164 2.9810 -0.0182 -0.5511 -0.2908 23  CYS J CB  
19240 S SG  . CYS K 17  ? 2.0284 3.6044 2.8573 -0.0270 -0.5680 -0.2939 23  CYS J SG  
19241 N N   . GLY K 18  ? 2.0485 3.5894 2.8392 -0.0296 -0.5839 -0.3130 24  GLY J N   
19242 C CA  . GLY K 18  ? 1.9910 3.5277 2.7653 -0.0319 -0.5991 -0.3238 24  GLY J CA  
19243 C C   . GLY K 18  ? 2.0585 3.5750 2.8142 -0.0323 -0.6047 -0.3323 24  GLY J C   
19244 O O   . GLY K 18  ? 2.1598 3.6614 2.9112 -0.0298 -0.5963 -0.3306 24  GLY J O   
19245 N N   . GLU K 19  ? 2.0608 3.5773 2.8056 -0.0357 -0.6197 -0.3419 25  GLU J N   
19246 C CA  . GLU K 19  ? 2.1111 3.6101 2.8382 -0.0368 -0.6280 -0.3514 25  GLU J CA  
19247 C C   . GLU K 19  ? 2.1749 3.6397 2.8679 -0.0274 -0.6211 -0.3553 25  GLU J C   
19248 O O   . GLU K 19  ? 2.1664 3.6220 2.8505 -0.0202 -0.6096 -0.3501 25  GLU J O   
19249 C CB  . GLU K 19  ? 2.0202 3.5324 2.7475 -0.0430 -0.6459 -0.3596 25  GLU J CB  
19250 C CG  . GLU K 19  ? 2.0529 3.5438 2.7508 -0.0414 -0.6565 -0.3714 25  GLU J CG  
19251 C CD  . GLU K 19  ? 2.0290 3.5373 2.7325 -0.0484 -0.6736 -0.3779 25  GLU J CD  
19252 O OE1 . GLU K 19  ? 2.0579 3.5946 2.7895 -0.0557 -0.6787 -0.3743 25  GLU J OE1 
19253 O OE2 . GLU K 19  ? 2.0452 3.5393 2.7247 -0.0462 -0.6817 -0.3865 25  GLU J OE2 
19254 N N   . GLU K 20  ? 2.2423 3.6886 2.9166 -0.0272 -0.6280 -0.3643 26  GLU J N   
19255 C CA  . GLU K 20  ? 2.2978 3.7118 2.9387 -0.0184 -0.6232 -0.3693 26  GLU J CA  
19256 C C   . GLU K 20  ? 2.2162 3.6238 2.8360 -0.0152 -0.6299 -0.3751 26  GLU J C   
19257 O O   . GLU K 20  ? 2.1502 3.5727 2.7753 -0.0211 -0.6435 -0.3799 26  GLU J O   
19258 C CB  . GLU K 20  ? 2.3763 3.7723 3.0043 -0.0193 -0.6290 -0.3776 26  GLU J CB  
19259 C CG  . GLU K 20  ? 2.4794 3.8770 3.1246 -0.0215 -0.6220 -0.3728 26  GLU J CG  
19260 C CD  . GLU K 20  ? 2.5915 3.9590 3.2133 -0.0162 -0.6195 -0.3789 26  GLU J CD  
19261 O OE1 . GLU K 20  ? 2.5791 3.9253 3.1716 -0.0109 -0.6234 -0.3870 26  GLU J OE1 
19262 O OE2 . GLU K 20  ? 2.6941 4.0592 3.3267 -0.0172 -0.6136 -0.3756 26  GLU J OE2 
19263 N N   . SER K 21  ? 2.1331 3.5184 2.7286 -0.0058 -0.6205 -0.3746 27  SER J N   
19264 C CA  . SER K 21  ? 2.1049 3.4831 2.6795 -0.0021 -0.6260 -0.3796 27  SER J CA  
19265 C C   . SER K 21  ? 2.1391 3.5051 2.6935 -0.0039 -0.6408 -0.3923 27  SER J C   
19266 O O   . SER K 21  ? 2.2033 3.5501 2.7436 -0.0020 -0.6412 -0.3978 27  SER J O   
19267 C CB  . SER K 21  ? 2.1394 3.4955 2.6916 0.0089  -0.6122 -0.3760 27  SER J CB  
19268 O OG  . SER K 21  ? 2.1497 3.4929 2.6760 0.0132  -0.6183 -0.3827 27  SER J OG  
19269 N N   . LEU K 22  ? 2.2294 3.6066 2.7827 -0.0075 -0.6531 -0.3971 28  LEU J N   
19270 C CA  . LEU K 22  ? 2.2568 3.6237 2.7908 -0.0092 -0.6677 -0.4091 28  LEU J CA  
19271 C C   . LEU K 22  ? 2.2661 3.6167 2.7714 -0.0023 -0.6692 -0.4138 28  LEU J C   
19272 O O   . LEU K 22  ? 2.3161 3.6471 2.7963 0.0002  -0.6762 -0.4235 28  LEU J O   
19273 C CB  . LEU K 22  ? 2.2123 3.6054 2.7673 -0.0197 -0.6830 -0.4122 28  LEU J CB  
19274 C CG  . LEU K 22  ? 2.2450 3.6302 2.7849 -0.0232 -0.6991 -0.4245 28  LEU J CG  
19275 C CD1 . LEU K 22  ? 2.3217 3.6855 2.8495 -0.0215 -0.6982 -0.4295 28  LEU J CD1 
19276 C CD2 . LEU K 22  ? 2.2033 3.6167 2.7663 -0.0335 -0.7133 -0.4263 28  LEU J CD2 
19277 N N   . GLY K 23  ? 2.1537 3.5123 2.6629 0.0008  -0.6625 -0.4069 29  GLY J N   
19278 C CA  . GLY K 23  ? 2.1594 3.5051 2.6445 0.0075  -0.6623 -0.4094 29  GLY J CA  
19279 C C   . GLY K 23  ? 2.1451 3.4904 2.6324 0.0142  -0.6470 -0.3989 29  GLY J C   
19280 O O   . GLY K 23  ? 2.1446 3.4927 2.6461 0.0155  -0.6346 -0.3903 29  GLY J O   
19281 N N   . SER K 24  ? 2.1137 3.4554 2.5871 0.0185  -0.6479 -0.3993 30  SER J N   
19282 C CA  . SER K 24  ? 2.1018 3.4442 2.5776 0.0247  -0.6345 -0.3892 30  SER J CA  
19283 C C   . SER K 24  ? 2.0354 3.4080 2.5469 0.0182  -0.6332 -0.3805 30  SER J C   
19284 O O   . SER K 24  ? 1.9887 3.3820 2.5153 0.0108  -0.6453 -0.3833 30  SER J O   
19285 C CB  . SER K 24  ? 2.1074 3.4408 2.5614 0.0299  -0.6377 -0.3923 30  SER J CB  
19286 O OG  . SER K 24  ? 2.0623 3.4131 2.5246 0.0227  -0.6532 -0.3978 30  SER J OG  
19287 N N   . ARG K 25  ? 2.0709 3.4462 2.5962 0.0209  -0.6186 -0.3702 31  ARG J N   
19288 C CA  . ARG K 25  ? 1.9992 3.4022 2.5590 0.0150  -0.6161 -0.3617 31  ARG J CA  
19289 C C   . ARG K 25  ? 1.9787 3.3878 2.5446 0.0196  -0.6069 -0.3525 31  ARG J C   
19290 O O   . ARG K 25  ? 2.0145 3.4049 2.5584 0.0280  -0.5996 -0.3512 31  ARG J O   
19291 C CB  . ARG K 25  ? 2.0153 3.4182 2.5891 0.0144  -0.6057 -0.3559 31  ARG J CB  
19292 C CG  . ARG K 25  ? 2.0254 3.4309 2.6058 0.0078  -0.6138 -0.3619 31  ARG J CG  
19293 C CD  . ARG K 25  ? 1.9724 3.4081 2.5882 -0.0013 -0.6176 -0.3574 31  ARG J CD  
19294 N NE  . ARG K 25  ? 1.9843 3.4239 2.6059 -0.0082 -0.6277 -0.3639 31  ARG J NE  
19295 C CZ  . ARG K 25  ? 1.9911 3.4367 2.6302 -0.0114 -0.6229 -0.3599 31  ARG J CZ  
19296 N NH1 . ARG K 25  ? 1.9844 3.4325 2.6362 -0.0084 -0.6082 -0.3497 31  ARG J NH1 
19297 N NH2 . ARG K 25  ? 2.0403 3.4897 2.6847 -0.0178 -0.6329 -0.3659 31  ARG J NH2 
19298 N N   . SER K 26  ? 2.0541 3.4907 2.6510 0.0139  -0.6078 -0.3461 32  SER J N   
19299 C CA  . SER K 26  ? 2.0128 3.4589 2.6220 0.0172  -0.5986 -0.3362 32  SER J CA  
19300 C C   . SER K 26  ? 1.9712 3.4402 2.6146 0.0120  -0.5933 -0.3279 32  SER J C   
19301 O O   . SER K 26  ? 1.8760 3.3709 2.5443 0.0060  -0.5994 -0.3256 32  SER J O   
19302 C CB  . SER K 26  ? 1.9725 3.4299 2.5821 0.0156  -0.6088 -0.3389 32  SER J CB  
19303 O OG  . SER K 26  ? 1.9251 3.3904 2.5461 0.0192  -0.5998 -0.3292 32  SER J OG  
19304 N N   . VAL K 27  ? 1.9767 3.4362 2.6215 0.0144  -0.5817 -0.3234 33  VAL J N   
19305 C CA  . VAL K 27  ? 1.9557 3.4354 2.6315 0.0094  -0.5767 -0.3161 33  VAL J CA  
19306 C C   . VAL K 27  ? 1.9486 3.4418 2.6430 0.0117  -0.5671 -0.3052 33  VAL J C   
19307 O O   . VAL K 27  ? 1.9821 3.4602 2.6643 0.0197  -0.5550 -0.2995 33  VAL J O   
19308 C CB  . VAL K 27  ? 2.0069 3.4713 2.6778 0.0116  -0.5670 -0.3146 33  VAL J CB  
19309 C CG1 . VAL K 27  ? 1.9827 3.4690 2.6864 0.0059  -0.5628 -0.3073 33  VAL J CG1 
19310 C CG2 . VAL K 27  ? 2.0231 3.4729 2.6746 0.0097  -0.5771 -0.3258 33  VAL J CG2 
19311 N N   . ILE K 28  ? 1.8492 3.3712 2.5737 0.0048  -0.5724 -0.3021 34  ILE J N   
19312 C CA  . ILE K 28  ? 1.8303 3.3679 2.5765 0.0061  -0.5641 -0.2917 34  ILE J CA  
19313 C C   . ILE K 28  ? 1.8184 3.3695 2.5903 0.0029  -0.5561 -0.2845 34  ILE J C   
19314 O O   . ILE K 28  ? 1.7916 3.3597 2.5806 -0.0047 -0.5644 -0.2874 34  ILE J O   
19315 C CB  . ILE K 28  ? 1.7913 3.3518 2.5525 0.0016  -0.5757 -0.2933 34  ILE J CB  
19316 C CG1 . ILE K 28  ? 1.8038 3.3514 2.5387 0.0031  -0.5867 -0.3028 34  ILE J CG1 
19317 C CG2 . ILE K 28  ? 1.7860 3.3567 2.5634 0.0050  -0.5663 -0.2830 34  ILE J CG2 
19318 C CD1 . ILE K 28  ? 1.7693 3.3384 2.5169 -0.0020 -0.6002 -0.3063 34  ILE J CD1 
19319 N N   . TRP K 29  ? 1.8445 3.3884 2.6194 0.0086  -0.5401 -0.2749 35  TRP J N   
19320 C CA  . TRP K 29  ? 1.8386 3.3930 2.6365 0.0066  -0.5307 -0.2672 35  TRP J CA  
19321 C C   . TRP K 29  ? 1.8067 3.3862 2.6345 0.0047  -0.5275 -0.2585 35  TRP J C   
19322 O O   . TRP K 29  ? 1.8066 3.3877 2.6333 0.0080  -0.5264 -0.2556 35  TRP J O   
19323 C CB  . TRP K 29  ? 1.9352 3.4649 2.7172 0.0142  -0.5147 -0.2623 35  TRP J CB  
19324 C CG  . TRP K 29  ? 1.9996 3.5061 2.7558 0.0157  -0.5173 -0.2706 35  TRP J CG  
19325 C CD1 . TRP K 29  ? 2.0147 3.4966 2.7384 0.0214  -0.5190 -0.2771 35  TRP J CD1 
19326 C CD2 . TRP K 29  ? 2.0642 3.5695 2.8251 0.0118  -0.5179 -0.2731 35  TRP J CD2 
19327 N NE1 . TRP K 29  ? 2.0828 3.5486 2.7909 0.0212  -0.5213 -0.2839 35  TRP J NE1 
19328 C CE2 . TRP K 29  ? 2.1164 3.5958 2.8470 0.0153  -0.5206 -0.2815 35  TRP J CE2 
19329 C CE3 . TRP K 29  ? 2.0859 3.6097 2.8740 0.0057  -0.5167 -0.2690 35  TRP J CE3 
19330 C CZ2 . TRP K 29  ? 2.1911 3.6625 2.9183 0.0128  -0.5223 -0.2859 35  TRP J CZ2 
19331 C CZ3 . TRP K 29  ? 2.1611 3.6770 2.9457 0.0032  -0.5182 -0.2731 35  TRP J CZ3 
19332 C CH2 . TRP K 29  ? 2.2138 3.7036 2.9683 0.0067  -0.5210 -0.2815 35  TRP J CH2 
19333 N N   . TYR K 30  ? 1.8720 3.4714 2.7270 -0.0007 -0.5262 -0.2543 36  TYR J N   
19334 C CA  . TYR K 30  ? 1.8598 3.4845 2.7456 -0.0030 -0.5232 -0.2461 36  TYR J CA  
19335 C C   . TYR K 30  ? 1.9137 3.5432 2.8174 -0.0035 -0.5112 -0.2380 36  TYR J C   
19336 O O   . TYR K 30  ? 1.9980 3.6208 2.8979 -0.0056 -0.5109 -0.2408 36  TYR J O   
19337 C CB  . TYR K 30  ? 1.8066 3.4590 2.7118 -0.0111 -0.5392 -0.2511 36  TYR J CB  
19338 C CG  . TYR K 30  ? 1.7542 3.4050 2.6452 -0.0107 -0.5509 -0.2582 36  TYR J CG  
19339 C CD1 . TYR K 30  ? 1.7469 3.4042 2.6436 -0.0078 -0.5497 -0.2541 36  TYR J CD1 
19340 C CD2 . TYR K 30  ? 1.7336 3.3759 2.6055 -0.0134 -0.5633 -0.2690 36  TYR J CD2 
19341 C CE1 . TYR K 30  ? 1.7396 3.3951 2.6232 -0.0075 -0.5606 -0.2606 36  TYR J CE1 
19342 C CE2 . TYR K 30  ? 1.7272 3.3677 2.5858 -0.0131 -0.5741 -0.2756 36  TYR J CE2 
19343 C CZ  . TYR K 30  ? 1.7456 3.3927 2.6100 -0.0102 -0.5727 -0.2714 36  TYR J CZ  
19344 O OH  . TYR K 30  ? 1.7728 3.4181 2.6241 -0.0099 -0.5835 -0.2779 36  TYR J OH  
19345 N N   . GLN K 31  ? 1.8847 3.5254 2.8082 -0.0015 -0.5013 -0.2281 37  GLN J N   
19346 C CA  . GLN K 31  ? 1.9003 3.5480 2.8434 -0.0020 -0.4898 -0.2197 37  GLN J CA  
19347 C C   . GLN K 31  ? 1.8231 3.5039 2.8013 -0.0078 -0.4940 -0.2154 37  GLN J C   
19348 O O   . GLN K 31  ? 1.7687 3.4615 2.7566 -0.0071 -0.4964 -0.2131 37  GLN J O   
19349 C CB  . GLN K 31  ? 1.9469 3.5770 2.8821 0.0064  -0.4724 -0.2107 37  GLN J CB  
19350 C CG  . GLN K 31  ? 2.0215 3.6569 2.9754 0.0065  -0.4595 -0.2017 37  GLN J CG  
19351 C CD  . GLN K 31  ? 2.0688 3.6890 3.0166 0.0148  -0.4427 -0.1924 37  GLN J CD  
19352 O OE1 . GLN K 31  ? 2.0186 3.6282 2.9653 0.0176  -0.4305 -0.1872 37  GLN J OE1 
19353 N NE2 . GLN K 31  ? 2.1705 3.7906 3.1155 0.0186  -0.4420 -0.1897 37  GLN J NE2 
19354 N N   . GLN K 32  ? 1.8181 3.5139 2.8156 -0.0134 -0.4949 -0.2144 38  GLN J N   
19355 C CA  . GLN K 32  ? 1.7641 3.4923 2.7954 -0.0190 -0.4990 -0.2105 38  GLN J CA  
19356 C C   . GLN K 32  ? 1.8150 3.5505 2.8670 -0.0188 -0.4860 -0.2009 38  GLN J C   
19357 O O   . GLN K 32  ? 1.8672 3.6038 2.9237 -0.0222 -0.4854 -0.2016 38  GLN J O   
19358 C CB  . GLN K 32  ? 1.7197 3.4658 2.7589 -0.0269 -0.5154 -0.2188 38  GLN J CB  
19359 C CG  . GLN K 32  ? 1.6577 3.4382 2.7302 -0.0322 -0.5213 -0.2158 38  GLN J CG  
19360 C CD  . GLN K 32  ? 1.6697 3.4681 2.7587 -0.0395 -0.5281 -0.2180 38  GLN J CD  
19361 O OE1 . GLN K 32  ? 1.7297 3.5158 2.8110 -0.0401 -0.5240 -0.2185 38  GLN J OE1 
19362 N NE2 . GLN K 32  ? 1.6354 3.4297 2.7320 -0.0450 -0.5316 -0.2132 38  GLN J NE2 
19363 N N   . ARG K 33  ? 1.9384 3.6788 3.0031 -0.0150 -0.4758 -0.1920 39  ARG J N   
19364 C CA  . ARG K 33  ? 1.9777 3.7279 3.0649 -0.0148 -0.4637 -0.1823 39  ARG J CA  
19365 C C   . ARG K 33  ? 1.9611 3.7442 3.0794 -0.0225 -0.4722 -0.1822 39  ARG J C   
19366 O O   . ARG K 33  ? 1.9136 3.7157 3.0421 -0.0260 -0.4844 -0.1862 39  ARG J O   
19367 C CB  . ARG K 33  ? 1.9847 3.7304 3.0759 -0.0084 -0.4510 -0.1730 39  ARG J CB  
19368 C CG  . ARG K 33  ? 2.0879 3.8252 3.1848 -0.0049 -0.4339 -0.1637 39  ARG J CG  
19369 C CD  . ARG K 33  ? 2.1157 3.8201 3.1816 0.0004  -0.4260 -0.1655 39  ARG J CD  
19370 N NE  . ARG K 33  ? 2.1016 3.7826 3.1410 0.0076  -0.4223 -0.1663 39  ARG J NE  
19371 C CZ  . ARG K 33  ? 2.1345 3.7870 3.1468 0.0131  -0.4146 -0.1674 39  ARG J CZ  
19372 N NH1 . ARG K 33  ? 2.1800 3.8238 3.1887 0.0122  -0.4100 -0.1679 39  ARG J NH1 
19373 N NH2 . ARG K 33  ? 2.1464 3.7789 3.1350 0.0198  -0.4114 -0.1680 39  ARG J NH2 
19374 N N   . PRO K 34  ? 1.8083 3.5992 2.9423 -0.0251 -0.4662 -0.1777 40  PRO J N   
19375 C CA  . PRO K 34  ? 1.7721 3.5947 2.9357 -0.0323 -0.4741 -0.1775 40  PRO J CA  
19376 C C   . PRO K 34  ? 1.7034 3.5533 2.8933 -0.0335 -0.4773 -0.1736 40  PRO J C   
19377 O O   . PRO K 34  ? 1.7261 3.5780 2.9275 -0.0297 -0.4663 -0.1651 40  PRO J O   
19378 C CB  . PRO K 34  ? 1.8257 3.6473 3.0002 -0.0327 -0.4624 -0.1708 40  PRO J CB  
19379 C CG  . PRO K 34  ? 1.8796 3.6736 3.0362 -0.0251 -0.4470 -0.1654 40  PRO J CG  
19380 C CD  . PRO K 34  ? 1.8465 3.6175 2.9720 -0.0214 -0.4517 -0.1725 40  PRO J CD  
19381 N N   . GLY K 35  ? 1.6941 3.5278 2.8764 -0.0390 -0.4858 -0.1741 41  GLY J N   
19382 C CA  . GLY K 35  ? 1.6863 3.5072 2.8748 -0.0409 -0.4841 -0.1660 41  GLY J CA  
19383 C C   . GLY K 35  ? 1.6900 3.5078 2.8702 -0.0374 -0.4880 -0.1682 41  GLY J C   
19384 O O   . GLY K 35  ? 1.6998 3.5091 2.8871 -0.0380 -0.4858 -0.1613 41  GLY J O   
19385 N N   . GLN K 36  ? 1.9325 3.7564 3.0976 -0.0338 -0.4942 -0.1778 42  GLN J N   
19386 C CA  . GLN K 36  ? 1.9216 3.7438 3.0782 -0.0300 -0.4982 -0.1804 42  GLN J CA  
19387 C C   . GLN K 36  ? 1.8960 3.7057 3.0284 -0.0318 -0.5110 -0.1904 42  GLN J C   
19388 O O   . GLN K 36  ? 1.8463 3.6462 2.9690 -0.0368 -0.5168 -0.1944 42  GLN J O   
19389 C CB  . GLN K 36  ? 1.9438 3.7785 3.1025 -0.0220 -0.4900 -0.1798 42  GLN J CB  
19390 C CG  . GLN K 36  ? 1.9630 3.8058 3.1438 -0.0200 -0.4761 -0.1688 42  GLN J CG  
19391 C CD  . GLN K 36  ? 1.9756 3.7933 3.1414 -0.0122 -0.4604 -0.1617 42  GLN J CD  
19392 O OE1 . GLN K 36  ? 2.0096 3.8057 3.1500 -0.0078 -0.4601 -0.1645 42  GLN J OE1 
19393 N NE2 . GLN K 36  ? 1.9918 3.8122 3.1731 -0.0103 -0.4469 -0.1522 42  GLN J NE2 
19394 N N   . ALA K 37  ? 1.8299 3.6393 2.9520 -0.0277 -0.5156 -0.1944 43  ALA J N   
19395 C CA  . ALA K 37  ? 1.7895 3.5862 2.8881 -0.0292 -0.5275 -0.2038 43  ALA J CA  
19396 C C   . ALA K 37  ? 1.7984 3.5962 2.8789 -0.0235 -0.5288 -0.2123 43  ALA J C   
19397 O O   . ALA K 37  ? 1.8546 3.6349 2.9267 -0.0173 -0.5150 -0.2055 43  ALA J O   
19398 C CB  . ALA K 37  ? 1.7835 3.5684 2.8769 -0.0290 -0.5313 -0.2018 43  ALA J CB  
19399 N N   . PRO K 38  ? 1.7420 3.5302 2.8024 -0.0260 -0.5391 -0.2219 44  PRO J N   
19400 C CA  . PRO K 38  ? 1.7362 3.4916 2.7625 -0.0211 -0.5347 -0.2254 44  PRO J CA  
19401 C C   . PRO K 38  ? 1.7737 3.5121 2.7830 -0.0141 -0.5299 -0.2234 44  PRO J C   
19402 O O   . PRO K 38  ? 1.8119 3.5605 2.8253 -0.0145 -0.5380 -0.2255 44  PRO J O   
19403 C CB  . PRO K 38  ? 1.7373 3.4926 2.7506 -0.0261 -0.5503 -0.2368 44  PRO J CB  
19404 C CG  . PRO K 38  ? 1.7254 3.5025 2.7632 -0.0338 -0.5564 -0.2358 44  PRO J CG  
19405 C CD  . PRO K 38  ? 1.7329 3.5113 2.7891 -0.0338 -0.5481 -0.2242 44  PRO J CD  
19406 N N   . SER K 39  ? 1.7884 3.5007 2.7784 -0.0075 -0.5164 -0.2193 45  SER J N   
19407 C CA  . SER K 39  ? 1.8101 3.5037 2.7819 -0.0001 -0.5099 -0.2165 45  SER J CA  
19408 C C   . SER K 39  ? 1.8274 3.4913 2.7631 0.0038  -0.5102 -0.2232 45  SER J C   
19409 O O   . SER K 39  ? 1.8497 3.5020 2.7748 0.0030  -0.5082 -0.2261 45  SER J O   
19410 C CB  . SER K 39  ? 1.8315 3.5203 2.8124 0.0055  -0.4923 -0.2046 45  SER J CB  
19411 O OG  . SER K 39  ? 1.8497 3.5239 2.8231 0.0072  -0.4817 -0.2020 45  SER J OG  
19412 N N   . LEU K 40  ? 1.8506 3.5024 2.7677 0.0080  -0.5129 -0.2256 46  LEU J N   
19413 C CA  . LEU K 40  ? 1.8059 3.4297 2.6878 0.0123  -0.5137 -0.2322 46  LEU J CA  
19414 C C   . LEU K 40  ? 1.8727 3.4722 2.7388 0.0202  -0.4966 -0.2255 46  LEU J C   
19415 O O   . LEU K 40  ? 1.9178 3.5163 2.7910 0.0251  -0.4851 -0.2161 46  LEU J O   
19416 C CB  . LEU K 40  ? 1.7853 3.4051 2.6533 0.0146  -0.5218 -0.2364 46  LEU J CB  
19417 C CG  . LEU K 40  ? 1.8551 3.4461 2.6859 0.0196  -0.5229 -0.2431 46  LEU J CG  
19418 C CD1 . LEU K 40  ? 1.8321 3.4190 2.6514 0.0147  -0.5335 -0.2536 46  LEU J CD1 
19419 C CD2 . LEU K 40  ? 1.8819 3.4703 2.7016 0.0222  -0.5296 -0.2457 46  LEU J CD2 
19420 N N   . ILE K 41  ? 1.8317 3.4113 2.6765 0.0215  -0.4949 -0.2305 47  ILE J N   
19421 C CA  . ILE K 41  ? 1.9111 3.4660 2.7382 0.0292  -0.4794 -0.2254 47  ILE J CA  
19422 C C   . ILE K 41  ? 1.9714 3.4991 2.7621 0.0353  -0.4807 -0.2317 47  ILE J C   
19423 O O   . ILE K 41  ? 2.0242 3.5368 2.8009 0.0431  -0.4711 -0.2267 47  ILE J O   
19424 C CB  . ILE K 41  ? 1.8993 3.4526 2.7325 0.0267  -0.4743 -0.2248 47  ILE J CB  
19425 C CG1 . ILE K 41  ? 1.8815 3.4608 2.7505 0.0218  -0.4709 -0.2172 47  ILE J CG1 
19426 C CG2 . ILE K 41  ? 1.9964 3.5223 2.8080 0.0350  -0.4594 -0.2211 47  ILE J CG2 
19427 C CD1 . ILE K 41  ? 1.8883 3.4704 2.7695 0.0269  -0.4574 -0.2055 47  ILE J CD1 
19428 N N   . ILE K 42  ? 2.1236 3.6447 2.8986 0.0320  -0.4925 -0.2427 48  ILE J N   
19429 C CA  . ILE K 42  ? 2.1207 3.6162 2.8607 0.0375  -0.4949 -0.2498 48  ILE J CA  
19430 C C   . ILE K 42  ? 2.0394 3.5420 2.7739 0.0317  -0.5133 -0.2609 48  ILE J C   
19431 O O   . ILE K 42  ? 2.0057 3.5178 2.7482 0.0247  -0.5226 -0.2670 48  ILE J O   
19432 C CB  . ILE K 42  ? 2.1558 3.6279 2.8757 0.0412  -0.4877 -0.2522 48  ILE J CB  
19433 C CG1 . ILE K 42  ? 2.1911 3.6531 2.9123 0.0483  -0.4689 -0.2413 48  ILE J CG1 
19434 C CG2 . ILE K 42  ? 2.1739 3.6218 2.8585 0.0457  -0.4931 -0.2614 48  ILE J CG2 
19435 C CD1 . ILE K 42  ? 2.3150 3.7542 3.0172 0.0524  -0.4612 -0.2433 48  ILE J CD1 
19436 N N   . TYR K 43  ? 2.0846 3.5830 2.8060 0.0345  -0.5184 -0.2634 49  TYR J N   
19437 C CA  . TYR K 43  ? 2.0069 3.5087 2.7189 0.0301  -0.5353 -0.2742 49  TYR J CA  
19438 C C   . TYR K 43  ? 2.1289 3.6019 2.8036 0.0365  -0.5358 -0.2809 49  TYR J C   
19439 O O   . TYR K 43  ? 2.2316 3.6850 2.8894 0.0450  -0.5233 -0.2760 49  TYR J O   
19440 C CB  . TYR K 43  ? 1.9028 3.4240 2.6298 0.0278  -0.5427 -0.2726 49  TYR J CB  
19441 C CG  . TYR K 43  ? 1.9773 3.4861 2.6912 0.0359  -0.5347 -0.2672 49  TYR J CG  
19442 C CD1 . TYR K 43  ? 1.9924 3.5036 2.7196 0.0403  -0.5204 -0.2553 49  TYR J CD1 
19443 C CD2 . TYR K 43  ? 2.0207 3.5153 2.7089 0.0393  -0.5415 -0.2736 49  TYR J CD2 
19444 C CE1 . TYR K 43  ? 2.0656 3.5657 2.7815 0.0478  -0.5129 -0.2498 49  TYR J CE1 
19445 C CE2 . TYR K 43  ? 2.0699 3.5535 2.7464 0.0469  -0.5341 -0.2682 49  TYR J CE2 
19446 C CZ  . TYR K 43  ? 2.0807 3.5671 2.7713 0.0511  -0.5198 -0.2561 49  TYR J CZ  
19447 O OH  . TYR K 43  ? 2.0616 3.5375 2.7413 0.0586  -0.5123 -0.2502 49  TYR J OH  
19448 N N   . ASN K 44  ? 2.0500 3.5209 2.7121 0.0326  -0.5502 -0.2921 50  ASN J N   
19449 C CA  . ASN K 44  ? 2.0972 3.5417 2.7239 0.0378  -0.5528 -0.3000 50  ASN J CA  
19450 C C   . ASN K 44  ? 2.3220 3.7434 2.9321 0.0438  -0.5405 -0.2985 50  ASN J C   
19451 O O   . ASN K 44  ? 2.4314 3.8322 3.0205 0.0527  -0.5302 -0.2954 50  ASN J O   
19452 C CB  . ASN K 44  ? 1.9837 3.4201 2.5950 0.0440  -0.5519 -0.2986 50  ASN J CB  
19453 C CG  . ASN K 44  ? 2.0668 3.4793 2.6427 0.0484  -0.5576 -0.3081 50  ASN J CG  
19454 O OD1 . ASN K 44  ? 2.0904 3.4968 2.6559 0.0451  -0.5663 -0.3175 50  ASN J OD1 
19455 N ND2 . ASN K 44  ? 2.1520 3.5512 2.7096 0.0560  -0.5527 -0.3057 50  ASN J ND2 
19456 N N   . ASN K 45  ? 1.9611 3.3873 2.5822 0.0387  -0.5416 -0.3004 51  ASN J N   
19457 C CA  . ASN K 45  ? 2.1446 3.5505 2.7521 0.0431  -0.5320 -0.3003 51  ASN J CA  
19458 C C   . ASN K 45  ? 2.2509 3.6491 2.8612 0.0502  -0.5133 -0.2889 51  ASN J C   
19459 O O   . ASN K 45  ? 2.3278 3.7299 2.9530 0.0486  -0.5057 -0.2841 51  ASN J O   
19460 C CB  . ASN K 45  ? 2.1963 3.5756 2.7676 0.0483  -0.5363 -0.3099 51  ASN J CB  
19461 C CG  . ASN K 45  ? 2.0899 3.4741 2.6566 0.0414  -0.5545 -0.3217 51  ASN J CG  
19462 O OD1 . ASN K 45  ? 2.0563 3.4569 2.6425 0.0331  -0.5622 -0.3242 51  ASN J OD1 
19463 N ND2 . ASN K 45  ? 2.0254 3.3958 2.5664 0.0450  -0.5614 -0.3289 51  ASN J ND2 
19464 N N   . ASN K 46  ? 2.2228 3.6103 2.8194 0.0580  -0.5056 -0.2841 52  ASN J N   
19465 C CA  . ASN K 46  ? 2.3099 3.6885 2.9070 0.0655  -0.4875 -0.2733 52  ASN J CA  
19466 C C   . ASN K 46  ? 2.2301 3.6135 2.8308 0.0699  -0.4819 -0.2653 52  ASN J C   
19467 O O   . ASN K 46  ? 2.3034 3.6705 2.8894 0.0789  -0.4691 -0.2592 52  ASN J O   
19468 C CB  . ASN K 46  ? 2.4680 3.8167 3.0342 0.0739  -0.4795 -0.2762 52  ASN J CB  
19469 C CG  . ASN K 46  ? 2.5877 3.9296 3.1592 0.0794  -0.4616 -0.2660 52  ASN J CG  
19470 O OD1 . ASN K 46  ? 2.5650 3.9247 3.1647 0.0754  -0.4563 -0.2582 52  ASN J OD1 
19471 N ND2 . ASN K 46  ? 2.7184 4.0348 3.2626 0.0889  -0.4522 -0.2660 52  ASN J ND2 
19472 N N   . ASP K 47  ? 2.3365 3.7422 2.9569 0.0640  -0.4910 -0.2649 53  ASP J N   
19473 C CA  . ASP K 47  ? 2.2556 3.6682 2.8832 0.0674  -0.4866 -0.2570 53  ASP J CA  
19474 C C   . ASP K 47  ? 2.1862 3.6241 2.8502 0.0626  -0.4824 -0.2478 53  ASP J C   
19475 O O   . ASP K 47  ? 2.0598 3.5199 2.7459 0.0540  -0.4931 -0.2508 53  ASP J O   
19476 C CB  . ASP K 47  ? 2.0429 3.4594 2.6617 0.0656  -0.5005 -0.2640 53  ASP J CB  
19477 C CG  . ASP K 47  ? 2.0453 3.4358 2.6270 0.0717  -0.5030 -0.2717 53  ASP J CG  
19478 O OD1 . ASP K 47  ? 2.2087 3.5777 2.7710 0.0797  -0.4910 -0.2690 53  ASP J OD1 
19479 O OD2 . ASP K 47  ? 1.9562 3.3479 2.5281 0.0688  -0.5168 -0.2806 53  ASP J OD2 
19480 N N   . ARG K 48  ? 2.1935 3.6279 2.8637 0.0685  -0.4666 -0.2364 54  ARG J N   
19481 C CA  . ARG K 48  ? 2.1410 3.5980 2.8454 0.0649  -0.4612 -0.2269 54  ARG J CA  
19482 C C   . ARG K 48  ? 2.0429 3.5122 2.7592 0.0658  -0.4623 -0.2213 54  ARG J C   
19483 O O   . ARG K 48  ? 2.0858 3.5403 2.7841 0.0733  -0.4566 -0.2182 54  ARG J O   
19484 C CB  . ARG K 48  ? 2.2354 3.6830 2.9425 0.0701  -0.4434 -0.2175 54  ARG J CB  
19485 C CG  . ARG K 48  ? 2.3741 3.7938 3.0512 0.0810  -0.4317 -0.2147 54  ARG J CG  
19486 C CD  . ARG K 48  ? 2.4926 3.9071 3.1767 0.0871  -0.4131 -0.2024 54  ARG J CD  
19487 N NE  . ARG K 48  ? 2.4961 3.9304 3.2081 0.0856  -0.4090 -0.1925 54  ARG J NE  
19488 C CZ  . ARG K 48  ? 2.4478 3.8791 3.1571 0.0914  -0.4031 -0.1854 54  ARG J CZ  
19489 N NH1 . ARG K 48  ? 2.3704 3.7798 3.0494 0.0993  -0.4004 -0.1872 54  ARG J NH1 
19490 N NH2 . ARG K 48  ? 2.5290 3.9792 3.2659 0.0896  -0.3996 -0.1765 54  ARG J NH2 
19491 N N   . PRO K 49  ? 2.0676 3.5639 2.8142 0.0587  -0.4692 -0.2197 55  PRO J N   
19492 C CA  . PRO K 49  ? 2.0384 3.5479 2.7993 0.0593  -0.4704 -0.2141 55  PRO J CA  
19493 C C   . PRO K 49  ? 2.0795 3.5885 2.8527 0.0649  -0.4539 -0.2007 55  PRO J C   
19494 O O   . PRO K 49  ? 2.1236 3.6201 2.8913 0.0690  -0.4410 -0.1958 55  PRO J O   
19495 C CB  . PRO K 49  ? 1.9703 3.5090 2.7600 0.0495  -0.4835 -0.2176 55  PRO J CB  
19496 C CG  . PRO K 49  ? 1.9451 3.4889 2.7451 0.0450  -0.4818 -0.2187 55  PRO J CG  
19497 C CD  . PRO K 49  ? 1.9999 3.5162 2.7686 0.0495  -0.4776 -0.2236 55  PRO J CD  
19498 N N   . SER K 50  ? 2.2496 3.7723 3.0399 0.0651  -0.4542 -0.1947 56  SER J N   
19499 C CA  . SER K 50  ? 2.3088 3.8319 3.1121 0.0704  -0.4389 -0.1816 56  SER J CA  
19500 C C   . SER K 50  ? 2.3122 3.8526 3.1443 0.0656  -0.4341 -0.1766 56  SER J C   
19501 O O   . SER K 50  ? 2.2419 3.8052 3.0968 0.0577  -0.4446 -0.1801 56  SER J O   
19502 C CB  . SER K 50  ? 2.3123 3.8466 3.1279 0.0714  -0.4419 -0.1770 56  SER J CB  
19503 O OG  . SER K 50  ? 2.2467 3.8071 3.0871 0.0630  -0.4556 -0.1812 56  SER J OG  
19504 N N   . GLY K 51  ? 2.2815 3.8115 3.1130 0.0705  -0.4182 -0.1683 57  GLY J N   
19505 C CA  . GLY K 51  ? 2.2203 3.7653 3.0783 0.0666  -0.4123 -0.1629 57  GLY J CA  
19506 C C   . GLY K 51  ? 2.1899 3.7246 3.0383 0.0656  -0.4087 -0.1665 57  GLY J C   
19507 O O   . GLY K 51  ? 2.1283 3.6716 2.9959 0.0638  -0.4008 -0.1606 57  GLY J O   
19508 N N   . ILE K 52  ? 2.1650 3.6816 2.9849 0.0667  -0.4141 -0.1759 58  ILE J N   
19509 C CA  . ILE K 52  ? 2.2719 3.7780 3.0819 0.0655  -0.4121 -0.1804 58  ILE J CA  
19510 C C   . ILE K 52  ? 2.4564 3.9349 3.2410 0.0749  -0.3975 -0.1765 58  ILE J C   
19511 O O   . ILE K 52  ? 2.5267 3.9874 3.2857 0.0811  -0.3970 -0.1785 58  ILE J O   
19512 C CB  . ILE K 52  ? 2.2567 3.7608 3.0522 0.0604  -0.4282 -0.1939 58  ILE J CB  
19513 C CG1 . ILE K 52  ? 2.0780 3.6097 2.8975 0.0516  -0.4429 -0.1977 58  ILE J CG1 
19514 C CG2 . ILE K 52  ? 2.3711 3.8651 3.1581 0.0589  -0.4266 -0.1984 58  ILE J CG2 
19515 C CD1 . ILE K 52  ? 1.9974 3.5525 2.8502 0.0455  -0.4413 -0.1929 58  ILE J CD1 
19516 N N   . PRO K 53  ? 2.3726 3.8472 3.1637 0.0764  -0.3854 -0.1706 59  PRO J N   
19517 C CA  . PRO K 53  ? 2.5525 4.0011 3.3199 0.0856  -0.3711 -0.1669 59  PRO J CA  
19518 C C   . PRO K 53  ? 2.6922 4.1191 3.4275 0.0876  -0.3767 -0.1779 59  PRO J C   
19519 O O   . PRO K 53  ? 2.6431 4.0752 3.3763 0.0812  -0.3909 -0.1881 59  PRO J O   
19520 C CB  . PRO K 53  ? 2.5527 4.0072 3.3396 0.0846  -0.3596 -0.1594 59  PRO J CB  
19521 C CG  . PRO K 53  ? 2.4111 3.8897 3.2236 0.0741  -0.3710 -0.1636 59  PRO J CG  
19522 C CD  . PRO K 53  ? 2.2747 3.7699 3.0966 0.0699  -0.3840 -0.1668 59  PRO J CD  
19523 N N   . ASP K 54  ? 2.7044 4.1063 3.4138 0.0969  -0.3655 -0.1758 60  ASP J N   
19524 C CA  . ASP K 54  ? 2.8472 4.2271 3.5250 0.0997  -0.3702 -0.1862 60  ASP J CA  
19525 C C   . ASP K 54  ? 2.9092 4.2852 3.5888 0.0967  -0.3688 -0.1897 60  ASP J C   
19526 O O   . ASP K 54  ? 3.0024 4.3596 3.6573 0.0991  -0.3717 -0.1982 60  ASP J O   
19527 C CB  . ASP K 54  ? 3.0216 4.3758 3.6697 0.1113  -0.3588 -0.1831 60  ASP J CB  
19528 C CG  . ASP K 54  ? 2.9928 4.3401 3.6457 0.1174  -0.3404 -0.1721 60  ASP J CG  
19529 O OD1 . ASP K 54  ? 2.8421 4.2074 3.5245 0.1133  -0.3354 -0.1642 60  ASP J OD1 
19530 O OD2 . ASP K 54  ? 3.1270 4.4511 3.7545 0.1262  -0.3309 -0.1716 60  ASP J OD2 
19531 N N   . ARG K 55  ? 2.8057 4.1991 3.5145 0.0917  -0.3644 -0.1835 61  ARG J N   
19532 C CA  . ARG K 55  ? 2.8525 4.2447 3.5665 0.0881  -0.3634 -0.1863 61  ARG J CA  
19533 C C   . ARG K 55  ? 2.8007 4.2009 3.5160 0.0795  -0.3807 -0.1980 61  ARG J C   
19534 O O   . ARG K 55  ? 2.8927 4.2843 3.6009 0.0778  -0.3826 -0.2038 61  ARG J O   
19535 C CB  . ARG K 55  ? 2.7488 4.1592 3.4950 0.0848  -0.3544 -0.1760 61  ARG J CB  
19536 C CG  . ARG K 55  ? 2.7655 4.1697 3.5132 0.0928  -0.3372 -0.1637 61  ARG J CG  
19537 C CD  . ARG K 55  ? 2.6755 4.0959 3.4537 0.0898  -0.3279 -0.1541 61  ARG J CD  
19538 N NE  . ARG K 55  ? 2.4840 3.9334 3.2932 0.0811  -0.3370 -0.1529 61  ARG J NE  
19539 C CZ  . ARG K 55  ? 2.4029 3.8690 3.2307 0.0723  -0.3458 -0.1572 61  ARG J CZ  
19540 N NH1 . ARG K 55  ? 2.4966 3.9531 3.3158 0.0707  -0.3469 -0.1628 61  ARG J NH1 
19541 N NH2 . ARG K 55  ? 2.2297 3.7224 3.0850 0.0652  -0.3536 -0.1558 61  ARG J NH2 
19542 N N   . PHE K 56  ? 2.9538 4.3706 3.6784 0.0741  -0.3934 -0.2015 62  PHE J N   
19543 C CA  . PHE K 56  ? 2.8738 4.3001 3.6008 0.0658  -0.4103 -0.2123 62  PHE J CA  
19544 C C   . PHE K 56  ? 2.9449 4.3519 3.6393 0.0693  -0.4188 -0.2223 62  PHE J C   
19545 O O   . PHE K 56  ? 2.8724 4.2777 3.5577 0.0725  -0.4211 -0.2221 62  PHE J O   
19546 C CB  . PHE K 56  ? 2.6300 4.0859 3.3858 0.0580  -0.4198 -0.2108 62  PHE J CB  
19547 C CG  . PHE K 56  ? 2.5499 4.0261 3.3385 0.0543  -0.4124 -0.2014 62  PHE J CG  
19548 C CD1 . PHE K 56  ? 2.4930 3.9743 3.2940 0.0586  -0.4007 -0.1902 62  PHE J CD1 
19549 C CD2 . PHE K 56  ? 2.5089 3.9990 3.3161 0.0468  -0.4170 -0.2034 62  PHE J CD2 
19550 C CE1 . PHE K 56  ? 2.3826 3.8824 3.2138 0.0554  -0.3938 -0.1815 62  PHE J CE1 
19551 C CE2 . PHE K 56  ? 2.4151 3.9241 3.2524 0.0437  -0.4100 -0.1946 62  PHE J CE2 
19552 C CZ  . PHE K 56  ? 2.3562 3.8699 3.2053 0.0480  -0.3985 -0.1838 62  PHE J CZ  
19553 N N   . SER K 57  ? 2.5687 3.9613 3.2459 0.0688  -0.4235 -0.2311 63  SER J N   
19554 C CA  . SER K 57  ? 2.6271 4.0009 3.2732 0.0718  -0.4321 -0.2416 63  SER J CA  
19555 C C   . SER K 57  ? 2.5881 3.9673 3.2356 0.0637  -0.4473 -0.2525 63  SER J C   
19556 O O   . SER K 57  ? 2.5917 3.9789 3.2553 0.0585  -0.4473 -0.2523 63  SER J O   
19557 C CB  . SER K 57  ? 2.8305 4.1746 3.4470 0.0821  -0.4207 -0.2415 63  SER J CB  
19558 O OG  . SER K 57  ? 2.8908 4.2286 3.5103 0.0815  -0.4150 -0.2416 63  SER J OG  
19559 N N   . GLY K 58  ? 2.5561 3.9305 3.1862 0.0628  -0.4601 -0.2620 64  GLY J N   
19560 C CA  . GLY K 58  ? 2.5173 3.8959 3.1466 0.0554  -0.4755 -0.2728 64  GLY J CA  
19561 C C   . GLY K 58  ? 2.6039 3.9567 3.1987 0.0600  -0.4806 -0.2833 64  GLY J C   
19562 O O   . GLY K 58  ? 2.6505 3.9853 3.2211 0.0683  -0.4758 -0.2834 64  GLY J O   
19563 N N   . SER K 59  ? 2.3251 3.6764 2.9183 0.0546  -0.4904 -0.2919 65  SER J N   
19564 C CA  . SER K 59  ? 2.3844 3.7124 2.9464 0.0581  -0.4969 -0.3028 65  SER J CA  
19565 C C   . SER K 59  ? 2.2517 3.5795 2.7992 0.0579  -0.5089 -0.3096 65  SER J C   
19566 O O   . SER K 59  ? 2.1154 3.4651 2.6808 0.0507  -0.5190 -0.3104 65  SER J O   
19567 C CB  . SER K 59  ? 2.4301 3.7590 2.9971 0.0515  -0.5057 -0.3103 65  SER J CB  
19568 O OG  . SER K 59  ? 2.2895 3.6423 2.8773 0.0413  -0.5196 -0.3135 65  SER J OG  
19569 N N   . PRO K 60  ? 2.2986 3.6024 2.8137 0.0659  -0.5079 -0.3147 66  PRO J N   
19570 C CA  . PRO K 60  ? 2.1692 3.4714 2.6688 0.0663  -0.5190 -0.3213 66  PRO J CA  
19571 C C   . PRO K 60  ? 2.0633 3.3743 2.5658 0.0575  -0.5371 -0.3321 66  PRO J C   
19572 O O   . PRO K 60  ? 2.1295 3.4351 2.6307 0.0544  -0.5412 -0.3379 66  PRO J O   
19573 C CB  . PRO K 60  ? 2.2440 3.5164 2.7075 0.0772  -0.5129 -0.3246 66  PRO J CB  
19574 C CG  . PRO K 60  ? 2.4171 3.6748 2.8753 0.0800  -0.5047 -0.3248 66  PRO J CG  
19575 C CD  . PRO K 60  ? 2.4518 3.7286 2.9426 0.0753  -0.4967 -0.3148 66  PRO J CD  
19576 N N   . GLY K 61  ? 2.0228 3.3477 2.5300 0.0534  -0.5479 -0.3347 67  GLY J N   
19577 C CA  . GLY K 61  ? 2.0121 3.3467 2.5226 0.0451  -0.5654 -0.3446 67  GLY J CA  
19578 C C   . GLY K 61  ? 2.0392 3.3526 2.5172 0.0485  -0.5744 -0.3561 67  GLY J C   
19579 O O   . GLY K 61  ? 2.0332 3.3532 2.5077 0.0442  -0.5882 -0.3633 67  GLY J O   
19580 N N   . SER K 62  A 2.0623 3.3495 2.5160 0.0565  -0.5663 -0.3580 67  SER J N   
19581 C CA  . SER K 62  A 2.0514 3.3156 2.4724 0.0609  -0.5732 -0.3690 67  SER J CA  
19582 C C   . SER K 62  A 2.1606 3.4105 2.5733 0.0603  -0.5752 -0.3759 67  SER J C   
19583 O O   . SER K 62  A 2.1543 3.3854 2.5410 0.0633  -0.5822 -0.3860 67  SER J O   
19584 C CB  . SER K 62  A 2.1022 3.3456 2.4967 0.0727  -0.5624 -0.3661 67  SER J CB  
19585 O OG  . SER K 62  A 2.2732 3.5062 2.6673 0.0791  -0.5459 -0.3582 67  SER J OG  
19586 N N   . THR K 63  B 2.2132 3.4712 2.6472 0.0567  -0.5691 -0.3707 67  THR J N   
19587 C CA  . THR K 63  B 2.3198 3.5664 2.7502 0.0555  -0.5706 -0.3762 67  THR J CA  
19588 C C   . THR K 63  B 2.2406 3.5040 2.6886 0.0442  -0.5861 -0.3825 67  THR J C   
19589 O O   . THR K 63  B 2.1809 3.4700 2.6586 0.0365  -0.5882 -0.3770 67  THR J O   
19590 C CB  . THR K 63  B 2.4833 3.7295 2.9276 0.0578  -0.5552 -0.3667 67  THR J CB  
19591 O OG1 . THR K 63  B 2.5604 3.7933 2.9903 0.0681  -0.5406 -0.3599 67  THR J OG1 
19592 C CG2 . THR K 63  B 2.5976 3.8282 3.0344 0.0581  -0.5557 -0.3726 67  THR J CG2 
19593 N N   . PHE K 64  C 2.3768 3.6260 2.8067 0.0435  -0.5969 -0.3939 67  PHE J N   
19594 C CA  . PHE K 64  C 2.3005 3.5632 2.7436 0.0334  -0.6126 -0.4009 67  PHE J CA  
19595 C C   . PHE K 64  C 2.4243 3.6848 2.8787 0.0300  -0.6112 -0.4015 67  PHE J C   
19596 O O   . PHE K 64  C 2.5308 3.7676 2.9655 0.0357  -0.6078 -0.4061 67  PHE J O   
19597 C CB  . PHE K 64  C 2.1986 3.4487 2.6167 0.0339  -0.6265 -0.4133 67  PHE J CB  
19598 C CG  . PHE K 64  C 2.0728 3.3230 2.4775 0.0377  -0.6283 -0.4135 67  PHE J CG  
19599 C CD1 . PHE K 64  C 1.9914 3.2644 2.4169 0.0345  -0.6262 -0.4053 67  PHE J CD1 
19600 C CD2 . PHE K 64  C 2.0328 3.2609 2.4048 0.0442  -0.6324 -0.4219 67  PHE J CD2 
19601 C CE1 . PHE K 64  C 1.8735 3.1470 2.2877 0.0378  -0.6282 -0.4054 67  PHE J CE1 
19602 C CE2 . PHE K 64  C 1.9331 3.1617 2.2932 0.0475  -0.6342 -0.4219 67  PHE J CE2 
19603 C CZ  . PHE K 64  C 1.8581 3.1094 2.2396 0.0442  -0.6321 -0.4135 67  PHE J CZ  
19604 N N   . GLY K 65  ? 2.1858 3.4710 2.6719 0.0210  -0.6140 -0.3968 68  GLY J N   
19605 C CA  . GLY K 65  ? 2.2906 3.5777 2.7917 0.0165  -0.6137 -0.3965 68  GLY J CA  
19606 C C   . GLY K 65  ? 2.4141 3.7095 2.9365 0.0171  -0.5989 -0.3850 68  GLY J C   
19607 O O   . GLY K 65  ? 2.5310 3.8215 3.0603 0.0157  -0.5961 -0.3848 68  GLY J O   
19608 N N   . THR K 66  ? 2.3065 3.6142 2.8400 0.0190  -0.5897 -0.3754 69  THR J N   
19609 C CA  . THR K 66  ? 2.3788 3.6953 2.9330 0.0197  -0.5754 -0.3640 69  THR J CA  
19610 C C   . THR K 66  ? 2.2470 3.5951 2.8318 0.0128  -0.5769 -0.3564 69  THR J C   
19611 O O   . THR K 66  ? 2.0960 3.4561 2.6819 0.0099  -0.5862 -0.3589 69  THR J O   
19612 C CB  . THR K 66  ? 2.4538 3.7509 2.9896 0.0308  -0.5594 -0.3586 69  THR J CB  
19613 O OG1 . THR K 66  ? 2.3428 3.6390 2.8652 0.0348  -0.5607 -0.3588 69  THR J OG1 
19614 C CG2 . THR K 66  ? 2.5708 3.8376 3.0791 0.0379  -0.5565 -0.3653 69  THR J CG2 
19615 N N   . THR K 67  ? 2.3528 3.7145 2.9628 0.0104  -0.5678 -0.3471 70  THR J N   
19616 C CA  . THR K 67  ? 2.1815 3.5736 2.8221 0.0042  -0.5682 -0.3394 70  THR J CA  
19617 C C   . THR K 67  ? 2.1600 3.5525 2.8002 0.0107  -0.5555 -0.3305 70  THR J C   
19618 O O   . THR K 67  ? 2.2892 3.6602 2.9105 0.0195  -0.5437 -0.3281 70  THR J O   
19619 C CB  . THR K 67  ? 2.1965 3.6047 2.8659 -0.0020 -0.5651 -0.3337 70  THR J CB  
19620 O OG1 . THR K 67  ? 2.3630 3.7558 3.0287 0.0041  -0.5497 -0.3279 70  THR J OG1 
19621 C CG2 . THR K 67  ? 2.1976 3.6075 2.8697 -0.0090 -0.5785 -0.3421 70  THR J CG2 
19622 N N   . ALA K 68  ? 2.2519 3.6694 2.9134 0.0064  -0.5582 -0.3255 71  ALA J N   
19623 C CA  . ALA K 68  ? 2.2216 3.6423 2.8863 0.0117  -0.5470 -0.3166 71  ALA J CA  
19624 C C   . ALA K 68  ? 2.3231 3.7439 3.0017 0.0145  -0.5307 -0.3062 71  ALA J C   
19625 O O   . ALA K 68  ? 2.2982 3.7358 3.0021 0.0085  -0.5302 -0.3022 71  ALA J O   
19626 C CB  . ALA K 68  ? 2.0285 3.4774 2.7151 0.0058  -0.5548 -0.3142 71  ALA J CB  
19627 N N   . THR K 69  ? 2.0749 3.4767 2.7366 0.0239  -0.5173 -0.3016 72  THR J N   
19628 C CA  . THR K 69  ? 2.1702 3.5680 2.8406 0.0280  -0.5008 -0.2919 72  THR J CA  
19629 C C   . THR K 69  ? 2.1370 3.5393 2.8122 0.0333  -0.4897 -0.2822 72  THR J C   
19630 O O   . THR K 69  ? 2.1519 3.5415 2.8062 0.0395  -0.4887 -0.2836 72  THR J O   
19631 C CB  . THR K 69  ? 2.3717 3.7395 3.0160 0.0352  -0.4938 -0.2956 72  THR J CB  
19632 O OG1 . THR K 69  ? 2.4022 3.7658 3.0428 0.0301  -0.5048 -0.3048 72  THR J OG1 
19633 C CG2 . THR K 69  ? 2.4829 3.8471 3.1370 0.0391  -0.4771 -0.2858 72  THR J CG2 
19634 N N   . LEU K 70  ? 2.4320 3.8525 3.1352 0.0308  -0.4814 -0.2722 73  LEU J N   
19635 C CA  . LEU K 70  ? 2.3854 3.8123 3.0979 0.0352  -0.4699 -0.2617 73  LEU J CA  
19636 C C   . LEU K 70  ? 2.5069 3.9210 3.2185 0.0415  -0.4522 -0.2534 73  LEU J C   
19637 O O   . LEU K 70  ? 2.4821 3.9056 3.2136 0.0377  -0.4479 -0.2492 73  LEU J O   
19638 C CB  . LEU K 70  ? 2.1904 3.6496 2.9367 0.0276  -0.4744 -0.2565 73  LEU J CB  
19639 C CG  . LEU K 70  ? 2.1208 3.5892 2.8801 0.0313  -0.4637 -0.2456 73  LEU J CG  
19640 C CD1 . LEU K 70  ? 2.1248 3.5812 2.8626 0.0375  -0.4643 -0.2471 73  LEU J CD1 
19641 C CD2 . LEU K 70  ? 1.9327 3.4336 2.7268 0.0235  -0.4687 -0.2412 73  LEU J CD2 
19642 N N   . THR K 71  ? 2.4729 3.8664 3.1623 0.0511  -0.4420 -0.2507 74  THR J N   
19643 C CA  . THR K 71  ? 2.6009 3.9800 3.2861 0.0582  -0.4249 -0.2430 74  THR J CA  
19644 C C   . THR K 71  ? 2.5087 3.9004 3.2120 0.0606  -0.4135 -0.2307 74  THR J C   
19645 O O   . THR K 71  ? 2.4460 3.8401 3.1450 0.0633  -0.4144 -0.2288 74  THR J O   
19646 C CB  . THR K 71  ? 2.7917 4.1396 3.4404 0.0679  -0.4201 -0.2476 74  THR J CB  
19647 O OG1 . THR K 71  ? 2.8606 4.1967 3.4932 0.0656  -0.4310 -0.2593 74  THR J OG1 
19648 C CG2 . THR K 71  ? 2.9378 4.2715 3.5824 0.0754  -0.4024 -0.2396 74  THR J CG2 
19649 N N   . ILE K 72  ? 2.8425 4.2421 3.5665 0.0597  -0.4027 -0.2222 75  ILE J N   
19650 C CA  . ILE K 72  ? 2.7491 4.1612 3.4928 0.0617  -0.3911 -0.2099 75  ILE J CA  
19651 C C   . ILE K 72  ? 2.8671 4.2614 3.6025 0.0698  -0.3735 -0.2027 75  ILE J C   
19652 O O   . ILE K 72  ? 2.8676 4.2638 3.6150 0.0677  -0.3680 -0.2000 75  ILE J O   
19653 C CB  . ILE K 72  ? 2.5605 4.0029 3.3411 0.0526  -0.3948 -0.2055 75  ILE J CB  
19654 C CG1 . ILE K 72  ? 2.4380 3.8982 3.2265 0.0446  -0.4128 -0.2132 75  ILE J CG1 
19655 C CG2 . ILE K 72  ? 2.4630 3.9180 3.2636 0.0549  -0.3833 -0.1931 75  ILE J CG2 
19656 C CD1 . ILE K 72  ? 2.2596 3.7504 3.0837 0.0357  -0.4175 -0.2097 75  ILE J CD1 
19657 N N   . THR K 73  ? 2.7445 4.1220 3.4598 0.0790  -0.3646 -0.1992 76  THR J N   
19658 C CA  . THR K 73  ? 2.8518 4.2125 3.5582 0.0874  -0.3474 -0.1919 76  THR J CA  
19659 C C   . THR K 73  ? 2.7244 4.1019 3.4584 0.0871  -0.3360 -0.1787 76  THR J C   
19660 O O   . THR K 73  ? 2.5803 3.9777 3.3331 0.0833  -0.3401 -0.1750 76  THR J O   
19661 C CB  . THR K 73  ? 2.9973 4.3337 3.6709 0.0978  -0.3424 -0.1931 76  THR J CB  
19662 O OG1 . THR K 73  ? 2.9067 4.2524 3.5844 0.0991  -0.3432 -0.1885 76  THR J OG1 
19663 C CG2 . THR K 73  ? 3.1304 4.4501 3.7764 0.0982  -0.3540 -0.2064 76  THR J CG2 
19664 N N   . SER K 74  ? 2.8239 4.1932 3.5603 0.0913  -0.3217 -0.1719 77  SER J N   
19665 C CA  . SER K 74  ? 2.7145 4.0979 3.4766 0.0916  -0.3095 -0.1592 77  SER J CA  
19666 C C   . SER K 74  ? 2.5292 3.9429 3.3260 0.0810  -0.3176 -0.1577 77  SER J C   
19667 O O   . SER K 74  ? 2.4005 3.8324 3.2158 0.0787  -0.3189 -0.1524 77  SER J O   
19668 C CB  . SER K 74  ? 2.7067 4.0865 3.4630 0.0988  -0.3011 -0.1513 77  SER J CB  
19669 O OG  . SER K 74  ? 2.8734 4.2259 3.5979 0.1090  -0.2929 -0.1522 77  SER J OG  
19670 N N   . VAL K 75  ? 2.6771 4.0958 3.4825 0.0747  -0.3231 -0.1626 78  VAL J N   
19671 C CA  . VAL K 75  ? 2.5074 3.9543 3.3443 0.0646  -0.3317 -0.1622 78  VAL J CA  
19672 C C   . VAL K 75  ? 2.3815 3.8449 3.2467 0.0642  -0.3201 -0.1497 78  VAL J C   
19673 O O   . VAL K 75  ? 2.4225 3.8768 3.2885 0.0685  -0.3064 -0.1432 78  VAL J O   
19674 C CB  . VAL K 75  ? 2.5274 3.9745 3.3664 0.0586  -0.3390 -0.1694 78  VAL J CB  
19675 C CG1 . VAL K 75  ? 2.3478 3.8251 3.2188 0.0483  -0.3486 -0.1691 78  VAL J CG1 
19676 C CG2 . VAL K 75  ? 2.6554 4.0849 3.4657 0.0594  -0.3502 -0.1817 78  VAL J CG2 
19677 N N   . GLU K 76  ? 2.6054 4.0931 3.4938 0.0594  -0.3257 -0.1466 79  GLU J N   
19678 C CA  . GLU K 76  ? 2.4742 3.9804 3.3919 0.0582  -0.3165 -0.1353 79  GLU J CA  
19679 C C   . GLU K 76  ? 2.3163 3.8512 3.2639 0.0481  -0.3268 -0.1368 79  GLU J C   
19680 O O   . GLU K 76  ? 2.2973 3.8389 3.2431 0.0422  -0.3415 -0.1460 79  GLU J O   
19681 C CB  . GLU K 76  ? 2.4284 3.9383 3.3485 0.0626  -0.3125 -0.1289 79  GLU J CB  
19682 C CG  . GLU K 76  ? 2.3464 3.8691 3.2680 0.0584  -0.3278 -0.1351 79  GLU J CG  
19683 C CD  . GLU K 76  ? 2.3369 3.8575 3.2544 0.0640  -0.3240 -0.1299 79  GLU J CD  
19684 O OE1 . GLU K 76  ? 2.3609 3.8750 3.2803 0.0702  -0.3093 -0.1200 79  GLU J OE1 
19685 O OE2 . GLU K 76  ? 2.3035 3.8293 3.2163 0.0621  -0.3357 -0.1355 79  GLU J OE2 
19686 N N   . ALA K 77  ? 2.4182 3.9704 3.3938 0.0462  -0.3189 -0.1273 80  ALA J N   
19687 C CA  . ALA K 77  ? 2.2799 3.8606 3.2857 0.0371  -0.3272 -0.1275 80  ALA J CA  
19688 C C   . ALA K 77  ? 2.2203 3.8199 3.2352 0.0326  -0.3413 -0.1318 80  ALA J C   
19689 O O   . ALA K 77  ? 2.1659 3.7861 3.1978 0.0247  -0.3529 -0.1361 80  ALA J O   
19690 C CB  . ALA K 77  ? 2.2838 3.8790 3.3173 0.0370  -0.3151 -0.1160 80  ALA J CB  
19691 N N   . GLY K 78  ? 2.2838 3.8769 3.2876 0.0375  -0.3406 -0.1306 81  GLY J N   
19692 C CA  . GLY K 78  ? 2.2370 3.8464 3.2481 0.0340  -0.3535 -0.1345 81  GLY J CA  
19693 C C   . GLY K 78  ? 2.2096 3.8149 3.2035 0.0303  -0.3692 -0.1469 81  GLY J C   
19694 O O   . GLY K 78  ? 2.1629 3.7856 3.1663 0.0256  -0.3819 -0.1511 81  GLY J O   
19695 N N   . ASP K 79  ? 2.2993 3.8813 3.2671 0.0327  -0.3687 -0.1529 82  ASP J N   
19696 C CA  . ASP K 79  ? 2.3285 3.9037 3.2775 0.0298  -0.3830 -0.1649 82  ASP J CA  
19697 C C   . ASP K 79  ? 2.2619 3.8536 3.2264 0.0209  -0.3936 -0.1702 82  ASP J C   
19698 O O   . ASP K 79  ? 2.2947 3.8831 3.2464 0.0175  -0.4064 -0.1802 82  ASP J O   
19699 C CB  . ASP K 79  ? 2.5239 4.0666 3.4382 0.0366  -0.3780 -0.1692 82  ASP J CB  
19700 C CG  . ASP K 79  ? 2.5944 4.1198 3.4902 0.0456  -0.3689 -0.1649 82  ASP J CG  
19701 O OD1 . ASP K 79  ? 2.4885 4.0254 3.3927 0.0458  -0.3715 -0.1621 82  ASP J OD1 
19702 O OD2 . ASP K 79  ? 2.7568 4.2572 3.6294 0.0526  -0.3593 -0.1644 82  ASP J OD2 
19703 N N   . GLU K 80  ? 2.3687 3.9782 3.3606 0.0171  -0.3885 -0.1637 83  GLU J N   
19704 C CA  . GLU K 80  ? 2.2977 3.9245 3.3071 0.0088  -0.3971 -0.1671 83  GLU J CA  
19705 C C   . GLU K 80  ? 2.2392 3.8913 3.2640 0.0020  -0.4129 -0.1719 83  GLU J C   
19706 O O   . GLU K 80  ? 2.2091 3.8850 3.2599 -0.0005 -0.4129 -0.1663 83  GLU J O   
19707 C CB  . GLU K 80  ? 2.2997 3.9389 3.3346 0.0076  -0.3860 -0.1575 83  GLU J CB  
19708 C CG  . GLU K 80  ? 2.2956 3.9534 3.3504 -0.0006 -0.3933 -0.1597 83  GLU J CG  
19709 C CD  . GLU K 80  ? 2.2897 3.9571 3.3674 -0.0013 -0.3812 -0.1501 83  GLU J CD  
19710 O OE1 . GLU K 80  ? 2.3126 3.9627 3.3821 0.0051  -0.3666 -0.1440 83  GLU J OE1 
19711 O OE2 . GLU K 80  ? 2.2649 3.9574 3.3688 -0.0080 -0.3864 -0.1488 83  GLU J OE2 
19712 N N   . ALA K 81  ? 2.1308 3.7783 3.1399 -0.0009 -0.4265 -0.1824 84  ALA J N   
19713 C CA  . ALA K 81  ? 2.0747 3.7446 3.0956 -0.0073 -0.4425 -0.1881 84  ALA J CA  
19714 C C   . ALA K 81  ? 2.0718 3.7341 3.0759 -0.0111 -0.4557 -0.1993 84  ALA J C   
19715 O O   . ALA K 81  ? 2.1985 3.8397 3.1843 -0.0092 -0.4525 -0.2025 84  ALA J O   
19716 C CB  . ALA K 81  ? 2.0674 3.7384 3.0828 -0.0039 -0.4450 -0.1879 84  ALA J CB  
19717 N N   . ASP K 82  ? 2.0278 3.7078 3.0387 -0.0165 -0.4708 -0.2054 85  ASP J N   
19718 C CA  . ASP K 82  ? 2.0839 3.7598 3.0806 -0.0206 -0.4850 -0.2163 85  ASP J CA  
19719 C C   . ASP K 82  ? 2.0672 3.7248 3.0358 -0.0162 -0.4900 -0.2227 85  ASP J C   
19720 O O   . ASP K 82  ? 1.9640 3.6247 2.9334 -0.0129 -0.4883 -0.2198 85  ASP J O   
19721 C CB  . ASP K 82  ? 2.0073 3.7142 3.0284 -0.0292 -0.4988 -0.2191 85  ASP J CB  
19722 C CG  . ASP K 82  ? 2.1664 3.8897 3.2119 -0.0342 -0.4959 -0.2145 85  ASP J CG  
19723 O OD1 . ASP K 82  ? 2.2949 4.0017 3.3326 -0.0324 -0.4875 -0.2129 85  ASP J OD1 
19724 O OD2 . ASP K 82  ? 2.1589 3.9114 3.2312 -0.0397 -0.5020 -0.2126 85  ASP J OD2 
19725 N N   . TYR K 83  ? 2.2329 3.8716 3.1772 -0.0161 -0.4964 -0.2316 86  TYR J N   
19726 C CA  . TYR K 83  ? 2.1822 3.8015 3.0974 -0.0118 -0.5014 -0.2384 86  TYR J CA  
19727 C C   . TYR K 83  ? 2.1775 3.7995 3.0842 -0.0173 -0.5185 -0.2497 86  TYR J C   
19728 O O   . TYR K 83  ? 2.2431 3.8595 3.1460 -0.0204 -0.5219 -0.2540 86  TYR J O   
19729 C CB  . TYR K 83  ? 2.2255 3.8124 3.1134 -0.0035 -0.4894 -0.2376 86  TYR J CB  
19730 C CG  . TYR K 83  ? 2.2359 3.8188 3.1295 0.0029  -0.4727 -0.2266 86  TYR J CG  
19731 C CD1 . TYR K 83  ? 2.2940 3.8815 3.2049 0.0027  -0.4612 -0.2186 86  TYR J CD1 
19732 C CD2 . TYR K 83  ? 2.1630 3.7376 3.0449 0.0091  -0.4684 -0.2241 86  TYR J CD2 
19733 C CE1 . TYR K 83  ? 2.2578 3.8417 3.1740 0.0085  -0.4459 -0.2084 86  TYR J CE1 
19734 C CE2 . TYR K 83  ? 2.1485 3.7195 3.0359 0.0149  -0.4532 -0.2138 86  TYR J CE2 
19735 C CZ  . TYR K 83  ? 2.2094 3.7851 3.1139 0.0146  -0.4420 -0.2060 86  TYR J CZ  
19736 O OH  . TYR K 83  ? 2.2082 3.7803 3.1183 0.0204  -0.4269 -0.1956 86  TYR J OH  
19737 N N   . TYR K 84  ? 2.0780 3.7083 2.9819 -0.0186 -0.5292 -0.2542 87  TYR J N   
19738 C CA  . TYR K 84  ? 2.0901 3.7236 2.9852 -0.0236 -0.5461 -0.2649 87  TYR J CA  
19739 C C   . TYR K 84  ? 2.0660 3.6749 2.9281 -0.0181 -0.5490 -0.2716 87  TYR J C   
19740 O O   . TYR K 84  ? 1.9856 3.5808 2.8356 -0.0110 -0.5396 -0.2675 87  TYR J O   
19741 C CB  . TYR K 84  ? 1.9888 3.6540 2.9085 -0.0299 -0.5573 -0.2653 87  TYR J CB  
19742 C CG  . TYR K 84  ? 2.0067 3.6979 2.9589 -0.0357 -0.5562 -0.2596 87  TYR J CG  
19743 C CD1 . TYR K 84  ? 2.1331 3.8231 3.0894 -0.0393 -0.5561 -0.2606 87  TYR J CD1 
19744 C CD2 . TYR K 84  ? 1.9449 3.6614 2.9239 -0.0373 -0.5548 -0.2530 87  TYR J CD2 
19745 C CE1 . TYR K 84  ? 2.1586 3.8724 3.1445 -0.0445 -0.5548 -0.2551 87  TYR J CE1 
19746 C CE2 . TYR K 84  ? 1.9667 3.7072 2.9752 -0.0423 -0.5536 -0.2477 87  TYR J CE2 
19747 C CZ  . TYR K 84  ? 2.0578 3.7969 3.0695 -0.0459 -0.5535 -0.2487 87  TYR J CZ  
19748 O OH  . TYR K 84  ? 2.0282 3.7912 3.0691 -0.0508 -0.5522 -0.2433 87  TYR J OH  
19749 N N   . CYS K 85  ? 1.9700 3.5733 2.8174 -0.0213 -0.5621 -0.2819 88  CYS J N   
19750 C CA  . CYS K 85  ? 1.9456 3.5265 2.7616 -0.0166 -0.5665 -0.2893 88  CYS J CA  
19751 C C   . CYS K 85  ? 1.8898 3.4835 2.7052 -0.0223 -0.5844 -0.2982 88  CYS J C   
19752 O O   . CYS K 85  ? 1.9096 3.5217 2.7413 -0.0298 -0.5944 -0.3013 88  CYS J O   
19753 C CB  . CYS K 85  ? 2.0676 3.6197 2.8579 -0.0128 -0.5626 -0.2939 88  CYS J CB  
19754 S SG  . CYS K 85  ? 2.1493 3.7044 2.9425 -0.0206 -0.5744 -0.3021 88  CYS J SG  
19755 N N   . HIS K 86  ? 1.8356 3.4195 2.6322 -0.0184 -0.5882 -0.3019 89  HIS J N   
19756 C CA  . HIS K 86  ? 1.8068 3.3998 2.5992 -0.0226 -0.6047 -0.3106 89  HIS J CA  
19757 C C   . HIS K 86  ? 1.8766 3.4422 2.6344 -0.0190 -0.6095 -0.3199 89  HIS J C   
19758 O O   . HIS K 86  ? 1.8173 3.3646 2.5536 -0.0121 -0.6050 -0.3201 89  HIS J O   
19759 C CB  . HIS K 86  ? 1.6874 3.2942 2.4888 -0.0214 -0.6062 -0.3072 89  HIS J CB  
19760 C CG  . HIS K 86  ? 1.6670 3.2923 2.4748 -0.0275 -0.6233 -0.3144 89  HIS J CG  
19761 N ND1 . HIS K 86  ? 1.5685 3.2060 2.3823 -0.0271 -0.6278 -0.3136 89  HIS J ND1 
19762 C CD2 . HIS K 86  ? 1.7381 3.3715 2.5469 -0.0342 -0.6371 -0.3226 89  HIS J CD2 
19763 C CE1 . HIS K 86  ? 1.5793 3.2319 2.3976 -0.0332 -0.6437 -0.3212 89  HIS J CE1 
19764 N NE2 . HIS K 86  ? 1.6814 3.3320 2.4968 -0.0375 -0.6495 -0.3266 89  HIS J NE2 
19765 N N   . ILE K 87  ? 1.8428 3.4059 2.5958 -0.0237 -0.6188 -0.3275 90  ILE J N   
19766 C CA  . ILE K 87  ? 1.8777 3.4148 2.5990 -0.0208 -0.6237 -0.3368 90  ILE J CA  
19767 C C   . ILE K 87  ? 1.7895 3.3279 2.4979 -0.0215 -0.6368 -0.3445 90  ILE J C   
19768 O O   . ILE K 87  ? 1.7696 3.3298 2.4930 -0.0286 -0.6496 -0.3480 90  ILE J O   
19769 C CB  . ILE K 87  ? 2.0180 3.5534 2.7409 -0.0260 -0.6298 -0.3422 90  ILE J CB  
19770 C CG1 . ILE K 87  ? 2.0463 3.5799 2.7820 -0.0251 -0.6166 -0.3344 90  ILE J CG1 
19771 C CG2 . ILE K 87  ? 2.0397 3.5501 2.7311 -0.0235 -0.6369 -0.3527 90  ILE J CG2 
19772 C CD1 . ILE K 87  ? 1.9616 3.4683 2.6769 -0.0156 -0.6014 -0.3306 90  ILE J CD1 
19773 N N   . TRP K 88  ? 1.9775 3.4930 2.6582 -0.0142 -0.6335 -0.3469 91  TRP J N   
19774 C CA  . TRP K 88  ? 1.9369 3.4488 2.6006 -0.0138 -0.6452 -0.3547 91  TRP J CA  
19775 C C   . TRP K 88  ? 2.0017 3.4859 2.6327 -0.0104 -0.6491 -0.3641 91  TRP J C   
19776 O O   . TRP K 88  ? 1.9706 3.4316 2.5772 -0.0023 -0.6415 -0.3640 91  TRP J O   
19777 C CB  . TRP K 88  ? 1.8005 3.3114 2.4603 -0.0081 -0.6391 -0.3494 91  TRP J CB  
19778 C CG  . TRP K 88  ? 1.7338 3.2736 2.4233 -0.0122 -0.6407 -0.3432 91  TRP J CG  
19779 C CD1 . TRP K 88  ? 1.7120 3.2652 2.4253 -0.0119 -0.6298 -0.3327 91  TRP J CD1 
19780 C CD2 . TRP K 88  ? 1.7088 3.2676 2.4070 -0.0171 -0.6545 -0.3476 91  TRP J CD2 
19781 N NE1 . TRP K 88  ? 1.6746 3.2544 2.4114 -0.0163 -0.6362 -0.3304 91  TRP J NE1 
19782 C CE2 . TRP K 88  ? 1.6636 3.2472 2.3915 -0.0195 -0.6514 -0.3394 91  TRP J CE2 
19783 C CE3 . TRP K 88  ? 1.7184 3.2755 2.4022 -0.0196 -0.6695 -0.3577 91  TRP J CE3 
19784 C CZ2 . TRP K 88  ? 1.5994 3.2064 2.3431 -0.0241 -0.6627 -0.3413 91  TRP J CZ2 
19785 C CZ3 . TRP K 88  ? 1.6299 3.2101 2.3292 -0.0243 -0.6805 -0.3593 91  TRP J CZ3 
19786 C CH2 . TRP K 88  ? 1.5708 3.1757 2.2997 -0.0265 -0.6771 -0.3512 91  TRP J CH2 
19787 N N   . ASP K 89  ? 1.7720 3.2591 2.4026 -0.0165 -0.6615 -0.3723 92  ASP J N   
19788 C CA  . ASP K 89  ? 1.8009 3.2629 2.4023 -0.0140 -0.6663 -0.3819 92  ASP J CA  
19789 C C   . ASP K 89  ? 1.8032 3.2656 2.3906 -0.0157 -0.6810 -0.3909 92  ASP J C   
19790 O O   . ASP K 89  ? 1.7781 3.2644 2.3836 -0.0223 -0.6915 -0.3920 92  ASP J O   
19791 C CB  . ASP K 89  ? 1.8406 3.3031 2.4495 -0.0192 -0.6700 -0.3851 92  ASP J CB  
19792 C CG  . ASP K 89  ? 1.9192 3.3512 2.4990 -0.0142 -0.6685 -0.3919 92  ASP J CG  
19793 O OD1 . ASP K 89  ? 1.8932 3.3064 2.4456 -0.0086 -0.6707 -0.3975 92  ASP J OD1 
19794 O OD2 . ASP K 89  ? 2.0064 3.4332 2.5910 -0.0154 -0.6647 -0.3913 92  ASP J OD2 
19795 N N   . SER K 90  ? 1.7446 3.1810 2.2999 -0.0095 -0.6818 -0.3974 93  SER J N   
19796 C CA  . SER K 90  ? 1.7497 3.1839 2.2889 -0.0103 -0.6952 -0.4062 93  SER J CA  
19797 C C   . SER K 90  ? 1.7473 3.1851 2.2853 -0.0174 -0.7109 -0.4163 93  SER J C   
19798 O O   . SER K 90  ? 1.7476 3.1871 2.2757 -0.0194 -0.7234 -0.4237 93  SER J O   
19799 C CB  . SER K 90  ? 1.7836 3.1884 2.2882 -0.0008 -0.6902 -0.4095 93  SER J CB  
19800 O OG  . SER K 90  ? 1.8087 3.1907 2.2952 0.0023  -0.6873 -0.4141 93  SER J OG  
19801 N N   . ARG K 91  ? 1.6793 3.1183 2.2273 -0.0213 -0.7106 -0.4167 94  ARG J N   
19802 C CA  . ARG K 91  ? 1.6765 3.1193 2.2254 -0.0282 -0.7250 -0.4255 94  ARG J CA  
19803 C C   . ARG K 91  ? 1.6426 3.1162 2.2256 -0.0375 -0.7305 -0.4218 94  ARG J C   
19804 O O   . ARG K 91  ? 1.6343 3.1172 2.2225 -0.0444 -0.7440 -0.4284 94  ARG J O   
19805 C CB  . ARG K 91  ? 1.7027 3.1211 2.2345 -0.0254 -0.7220 -0.4299 94  ARG J CB  
19806 C CG  . ARG K 91  ? 1.7371 3.1251 2.2342 -0.0158 -0.7170 -0.4341 94  ARG J CG  
19807 C CD  . ARG K 91  ? 1.7635 3.1274 2.2428 -0.0130 -0.7158 -0.4398 94  ARG J CD  
19808 N NE  . ARG K 91  ? 1.8144 3.1810 2.2930 -0.0198 -0.7316 -0.4494 94  ARG J NE  
19809 C CZ  . ARG K 91  ? 1.9116 3.2582 2.3741 -0.0186 -0.7347 -0.4567 94  ARG J CZ  
19810 N NH1 . ARG K 91  ? 1.9480 3.2707 2.3935 -0.0107 -0.7231 -0.4557 94  ARG J NH1 
19811 N NH2 . ARG K 91  ? 1.9727 3.3235 2.4365 -0.0252 -0.7495 -0.4651 94  ARG J NH2 
19812 N N   . ARG K 92  ? 1.7635 3.2533 2.3697 -0.0378 -0.7205 -0.4115 95  ARG J N   
19813 C CA  . ARG K 92  ? 1.7673 3.2865 2.4064 -0.0459 -0.7243 -0.4072 95  ARG J CA  
19814 C C   . ARG K 92  ? 1.6556 3.1892 2.3079 -0.0480 -0.7236 -0.4001 95  ARG J C   
19815 O O   . ARG K 92  ? 1.5666 3.1033 2.2144 -0.0418 -0.7197 -0.3994 95  ARG J O   
19816 C CB  . ARG K 92  ? 1.7959 3.3157 2.4502 -0.0445 -0.7097 -0.3979 95  ARG J CB  
19817 C CG  . ARG K 92  ? 1.8739 3.3696 2.5130 -0.0419 -0.7051 -0.4008 95  ARG J CG  
19818 C CD  . ARG K 92  ? 1.9836 3.4820 2.6265 -0.0486 -0.7167 -0.4076 95  ARG J CD  
19819 N NE  . ARG K 92  ? 2.0478 3.5503 2.7085 -0.0507 -0.7088 -0.4017 95  ARG J NE  
19820 C CZ  . ARG K 92  ? 2.1848 3.6904 2.8535 -0.0565 -0.7158 -0.4051 95  ARG J CZ  
19821 N NH1 . ARG K 92  ? 2.2641 3.7734 2.9496 -0.0579 -0.7076 -0.3989 95  ARG J NH1 
19822 N NH2 . ARG K 92  ? 2.2279 3.7328 2.8881 -0.0607 -0.7308 -0.4146 95  ARG J NH2 
19823 N N   . PRO K 93  A 1.7653 3.2906 2.4272 -0.0568 -0.7213 -0.3894 95  PRO J N   
19824 C CA  . PRO K 93  A 1.6828 3.2088 2.3540 -0.0591 -0.7158 -0.3783 95  PRO J CA  
19825 C C   . PRO K 93  A 1.5836 3.1315 2.2775 -0.0556 -0.7064 -0.3717 95  PRO J C   
19826 O O   . PRO K 93  A 1.6039 3.1670 2.3098 -0.0529 -0.7031 -0.3736 95  PRO J O   
19827 C CB  . PRO K 93  A 1.7563 3.2699 2.4344 -0.0689 -0.7155 -0.3687 95  PRO J CB  
19828 C CG  . PRO K 93  A 1.8869 3.3872 2.5494 -0.0712 -0.7237 -0.3772 95  PRO J CG  
19829 C CD  . PRO K 93  A 1.8912 3.4033 2.5523 -0.0646 -0.7251 -0.3878 95  PRO J CD  
19830 N N   . THR K 94  B 1.7575 3.3066 2.4576 -0.0558 -0.7021 -0.3637 95  THR J N   
19831 C CA  . THR K 94  B 1.6680 3.2364 2.3895 -0.0526 -0.6930 -0.3565 95  THR J CA  
19832 C C   . THR K 94  B 1.7347 3.3116 2.4802 -0.0578 -0.6862 -0.3473 95  THR J C   
19833 O O   . THR K 94  B 1.8066 3.3732 2.5582 -0.0652 -0.6853 -0.3390 95  THR J O   
19834 C CB  . THR K 94  B 1.5710 3.1356 2.2944 -0.0531 -0.6904 -0.3490 95  THR J CB  
19835 O OG1 . THR K 94  B 1.6044 3.1499 2.3225 -0.0607 -0.6933 -0.3436 95  THR J OG1 
19836 C CG2 . THR K 94  B 1.5429 3.1067 2.2478 -0.0457 -0.6949 -0.3573 95  THR J CG2 
19837 N N   . ASN K 95  C 1.7663 3.3620 2.5252 -0.0536 -0.6815 -0.3489 95  ASN J N   
19838 C CA  . ASN K 95  C 1.7963 3.4017 2.5785 -0.0578 -0.6745 -0.3405 95  ASN J CA  
19839 C C   . ASN K 95  C 1.6847 3.2974 2.4865 -0.0589 -0.6655 -0.3278 95  ASN J C   
19840 O O   . ASN K 95  C 1.5743 3.2014 2.3836 -0.0530 -0.6606 -0.3269 95  ASN J O   
19841 C CB  . ASN K 95  C 1.8079 3.4310 2.5978 -0.0527 -0.6723 -0.3466 95  ASN J CB  
19842 C CG  . ASN K 95  C 1.8701 3.4799 2.6392 -0.0515 -0.6795 -0.3579 95  ASN J CG  
19843 O OD1 . ASN K 95  C 1.9714 3.5556 2.7214 -0.0451 -0.6691 -0.3569 95  ASN J OD1 
19844 N ND2 . ASN K 95  C 1.8347 3.4315 2.5957 -0.0580 -0.6874 -0.3600 95  ASN J ND2 
19845 N N   . TRP K 96  ? 1.9837 3.5865 2.7939 -0.0663 -0.6635 -0.3179 96  TRP J N   
19846 C CA  . TRP K 96  ? 1.9616 3.5679 2.7896 -0.0680 -0.6558 -0.3056 96  TRP J CA  
19847 C C   . TRP K 96  ? 1.9899 3.6111 2.8423 -0.0690 -0.6471 -0.2982 96  TRP J C   
19848 O O   . TRP K 96  ? 1.9781 3.6011 2.8468 -0.0712 -0.6403 -0.2872 96  TRP J O   
19849 C CB  . TRP K 96  ? 2.0001 3.5868 2.8231 -0.0747 -0.6585 -0.2989 96  TRP J CB  
19850 C CG  . TRP K 96  ? 2.0091 3.5815 2.8099 -0.0736 -0.6659 -0.3046 96  TRP J CG  
19851 C CD1 . TRP K 96  ? 2.0858 3.6442 2.8652 -0.0750 -0.6747 -0.3129 96  TRP J CD1 
19852 C CD2 . TRP K 96  ? 1.9188 3.4886 2.7170 -0.0711 -0.6650 -0.3019 96  TRP J CD2 
19853 N NE1 . TRP K 96  ? 2.0669 3.6146 2.8302 -0.0735 -0.6791 -0.3158 96  TRP J NE1 
19854 C CE2 . TRP K 96  ? 1.9441 3.4987 2.7187 -0.0711 -0.6734 -0.3091 96  TRP J CE2 
19855 C CE3 . TRP K 96  ? 1.8150 3.3937 2.6286 -0.0689 -0.6579 -0.2942 96  TRP J CE3 
19856 C CZ2 . TRP K 96  ? 1.8326 3.3810 2.5989 -0.0690 -0.6749 -0.3087 96  TRP J CZ2 
19857 C CZ3 . TRP K 96  ? 1.7134 3.2860 2.5191 -0.0668 -0.6597 -0.2939 96  TRP J CZ3 
19858 C CH2 . TRP K 96  ? 1.7213 3.2791 2.5037 -0.0669 -0.6681 -0.3011 96  TRP J CH2 
19859 N N   . VAL K 97  ? 1.8600 3.4911 2.7148 -0.0674 -0.6474 -0.3041 97  VAL J N   
19860 C CA  . VAL K 97  ? 1.8859 3.5323 2.7632 -0.0679 -0.6393 -0.2983 97  VAL J CA  
19861 C C   . VAL K 97  ? 1.8329 3.4971 2.7106 -0.0606 -0.6383 -0.3072 97  VAL J C   
19862 O O   . VAL K 97  ? 1.8563 3.5173 2.7171 -0.0582 -0.6459 -0.3189 97  VAL J O   
19863 C CB  . VAL K 97  ? 1.9880 3.6270 2.8701 -0.0749 -0.6407 -0.2951 97  VAL J CB  
19864 C CG1 . VAL K 97  ? 1.9789 3.5992 2.8569 -0.0813 -0.6432 -0.2877 97  VAL J CG1 
19865 C CG2 . VAL K 97  ? 2.0438 3.6790 2.9108 -0.0745 -0.6490 -0.3071 97  VAL J CG2 
19866 N N   . PHE K 98  ? 1.9383 3.6205 2.8340 -0.0565 -0.6293 -0.3020 98  PHE J N   
19867 C CA  . PHE K 98  ? 1.9686 3.6516 2.8594 -0.0493 -0.6222 -0.3047 98  PHE J CA  
19868 C C   . PHE K 98  ? 2.0736 3.7467 2.9624 -0.0512 -0.6193 -0.3055 98  PHE J C   
19869 O O   . PHE K 98  ? 2.1166 3.8086 3.0250 -0.0579 -0.6254 -0.3056 98  PHE J O   
19870 C CB  . PHE K 98  ? 1.9142 3.6046 2.8217 -0.0455 -0.6081 -0.2936 98  PHE J CB  
19871 C CG  . PHE K 98  ? 1.8170 3.5112 2.7232 -0.0420 -0.6081 -0.2920 98  PHE J CG  
19872 C CD1 . PHE K 98  ? 1.8113 3.4973 2.6977 -0.0409 -0.6182 -0.2998 98  PHE J CD1 
19873 C CD2 . PHE K 98  ? 1.7312 3.4364 2.6559 -0.0394 -0.5976 -0.2822 98  PHE J CD2 
19874 C CE1 . PHE K 98  ? 1.7154 3.4049 2.6013 -0.0376 -0.6181 -0.2980 98  PHE J CE1 
19875 C CE2 . PHE K 98  ? 1.6454 3.3540 2.5699 -0.0360 -0.5975 -0.2804 98  PHE J CE2 
19876 C CZ  . PHE K 98  ? 1.6316 3.3322 2.5367 -0.0352 -0.6078 -0.2882 98  PHE J CZ  
19877 N N   . GLY K 99  ? 1.8970 3.5403 2.7617 -0.0452 -0.6105 -0.3063 99  GLY J N   
19878 C CA  . GLY K 99  ? 2.0462 3.6787 2.9088 -0.0465 -0.6071 -0.3068 99  GLY J CA  
19879 C C   . GLY K 99  ? 2.1010 3.7478 2.9901 -0.0478 -0.5961 -0.2967 99  GLY J C   
19880 O O   . GLY K 99  ? 2.0250 3.6837 2.9291 -0.0458 -0.5881 -0.2888 99  GLY J O   
19881 N N   . GLU K 100 ? 2.0199 3.6661 2.9158 -0.0513 -0.5957 -0.2968 100 GLU J N   
19882 C CA  . GLU K 100 ? 2.1033 3.7628 3.0243 -0.0528 -0.5853 -0.2872 100 GLU J CA  
19883 C C   . GLU K 100 ? 2.0696 3.7121 2.9839 -0.0449 -0.5675 -0.2795 100 GLU J C   
19884 O O   . GLU K 100 ? 2.0736 3.6877 2.9634 -0.0393 -0.5611 -0.2817 100 GLU J O   
19885 C CB  . GLU K 100 ? 2.2921 3.9521 3.2197 -0.0578 -0.5886 -0.2891 100 GLU J CB  
19886 C CG  . GLU K 100 ? 2.3383 4.0189 3.2775 -0.0661 -0.6054 -0.2952 100 GLU J CG  
19887 C CD  . GLU K 100 ? 2.5009 4.1826 3.4487 -0.0710 -0.6078 -0.2960 100 GLU J CD  
19888 O OE1 . GLU K 100 ? 2.6115 4.2797 3.5584 -0.0681 -0.5961 -0.2914 100 GLU J OE1 
19889 O OE2 . GLU K 100 ? 2.4722 4.1688 3.4284 -0.0777 -0.6213 -0.3009 100 GLU J OE2 
19890 N N   . GLY K 101 ? 2.1309 3.7917 3.0676 -0.0446 -0.5598 -0.2704 101 GLY J N   
19891 C CA  . GLY K 101 ? 2.0782 3.7269 3.0123 -0.0375 -0.5430 -0.2620 101 GLY J CA  
19892 C C   . GLY K 101 ? 2.2120 3.8476 3.1464 -0.0357 -0.5314 -0.2577 101 GLY J C   
19893 O O   . GLY K 101 ? 2.3683 4.0087 3.3112 -0.0408 -0.5356 -0.2595 101 GLY J O   
19894 N N   . THR K 102 ? 2.3709 3.9891 3.2953 -0.0281 -0.5165 -0.2517 102 THR J N   
19895 C CA  . THR K 102 ? 2.4709 4.0749 3.3944 -0.0250 -0.5032 -0.2465 102 THR J CA  
19896 C C   . THR K 102 ? 2.4118 4.0234 3.3516 -0.0213 -0.4885 -0.2350 102 THR J C   
19897 O O   . THR K 102 ? 2.3308 3.9363 3.2620 -0.0158 -0.4831 -0.2322 102 THR J O   
19898 C CB  . THR K 102 ? 2.4374 4.0067 3.3266 -0.0181 -0.4992 -0.2519 102 THR J CB  
19899 O OG1 . THR K 102 ? 2.4354 3.9981 3.3094 -0.0215 -0.5137 -0.2630 102 THR J OG1 
19900 C CG2 . THR K 102 ? 2.5318 4.0867 3.4201 -0.0154 -0.4870 -0.2477 102 THR J CG2 
19901 N N   . THR K 103 ? 2.3684 3.9935 3.3319 -0.0244 -0.4821 -0.2281 103 THR J N   
19902 C CA  . THR K 103 ? 2.3011 3.9361 3.2838 -0.0219 -0.4685 -0.2168 103 THR J CA  
19903 C C   . THR K 103 ? 2.3340 3.9433 3.3016 -0.0141 -0.4522 -0.2119 103 THR J C   
19904 O O   . THR K 103 ? 2.4396 4.0343 3.3988 -0.0138 -0.4494 -0.2139 103 THR J O   
19905 C CB  . THR K 103 ? 2.3403 4.0029 3.3562 -0.0289 -0.4695 -0.2117 103 THR J CB  
19906 O OG1 . THR K 103 ? 2.2862 3.9735 3.3162 -0.0358 -0.4847 -0.2162 103 THR J OG1 
19907 C CG2 . THR K 103 ? 2.2989 3.9727 3.3351 -0.0264 -0.4560 -0.2003 103 THR J CG2 
19908 N N   . LEU K 104 ? 2.2832 3.8873 3.2476 -0.0078 -0.4416 -0.2055 104 LEU J N   
19909 C CA  . LEU K 104 ? 2.3232 3.9046 3.2742 0.0002  -0.4253 -0.1997 104 LEU J CA  
19910 C C   . LEU K 104 ? 2.4260 4.0199 3.4025 0.0002  -0.4123 -0.1885 104 LEU J C   
19911 O O   . LEU K 104 ? 2.3758 3.9897 3.3731 -0.0008 -0.4100 -0.1819 104 LEU J O   
19912 C CB  . LEU K 104 ? 2.1574 3.7242 3.0886 0.0078  -0.4207 -0.1989 104 LEU J CB  
19913 C CG  . LEU K 104 ? 2.1830 3.7272 3.1003 0.0168  -0.4033 -0.1923 104 LEU J CG  
19914 C CD1 . LEU K 104 ? 2.3077 3.8271 3.2038 0.0196  -0.4005 -0.1972 104 LEU J CD1 
19915 C CD2 . LEU K 104 ? 2.0939 3.6259 2.9933 0.0240  -0.3995 -0.1910 104 LEU J CD2 
19916 N N   . ILE K 105 ? 2.2787 3.8607 3.2533 0.0013  -0.4040 -0.1864 105 ILE J N   
19917 C CA  . ILE K 105 ? 2.3303 3.9212 3.3269 0.0016  -0.3910 -0.1761 105 ILE J CA  
19918 C C   . ILE K 105 ? 2.3412 3.9077 3.3205 0.0110  -0.3748 -0.1706 105 ILE J C   
19919 O O   . ILE K 105 ? 2.3873 3.9282 3.3424 0.0154  -0.3715 -0.1748 105 ILE J O   
19920 C CB  . ILE K 105 ? 2.3845 3.9815 3.3945 -0.0041 -0.3927 -0.1767 105 ILE J CB  
19921 C CG1 . ILE K 105 ? 2.3012 3.9249 3.3310 -0.0135 -0.4081 -0.1809 105 ILE J CG1 
19922 C CG2 . ILE K 105 ? 2.4193 4.0209 3.4478 -0.0026 -0.3777 -0.1660 105 ILE J CG2 
19923 C CD1 . ILE K 105 ? 2.3146 3.9294 3.3249 -0.0157 -0.4224 -0.1924 105 ILE J CD1 
19924 N N   . VAL K 106 ? 2.4507 4.0251 3.4422 0.0143  -0.3647 -0.1613 106 VAL J N   
19925 C CA  . VAL K 106 ? 2.4740 4.0281 3.4523 0.0232  -0.3484 -0.1546 106 VAL J CA  
19926 C C   . VAL K 106 ? 2.6089 4.1655 3.6035 0.0226  -0.3372 -0.1475 106 VAL J C   
19927 O O   . VAL K 106 ? 2.6066 4.1857 3.6299 0.0190  -0.3338 -0.1400 106 VAL J O   
19928 C CB  . VAL K 106 ? 2.3193 3.8810 3.3041 0.0270  -0.3430 -0.1477 106 VAL J CB  
19929 C CG1 . VAL K 106 ? 2.3733 3.9137 3.3437 0.0364  -0.3263 -0.1407 106 VAL J CG1 
19930 C CG2 . VAL K 106 ? 2.1121 3.6739 3.0836 0.0267  -0.3551 -0.1548 106 VAL J CG2 
19931 N N   . LEU K 107 ? 2.5395 4.0731 3.5161 0.0262  -0.3316 -0.1499 107 LEU J N   
19932 C CA  . LEU K 107 ? 2.6300 4.1640 3.6201 0.0255  -0.3217 -0.1441 107 LEU J CA  
19933 C C   . LEU K 107 ? 2.6452 4.1798 3.6452 0.0310  -0.3050 -0.1322 107 LEU J C   
19934 O O   . LEU K 107 ? 2.5864 4.1188 3.5808 0.0358  -0.3006 -0.1286 107 LEU J O   
19935 C CB  . LEU K 107 ? 2.6594 4.1666 3.6254 0.0288  -0.3200 -0.1502 107 LEU J CB  
19936 C CG  . LEU K 107 ? 2.6374 4.1453 3.5980 0.0225  -0.3358 -0.1611 107 LEU J CG  
19937 C CD1 . LEU K 107 ? 2.6272 4.1069 3.5629 0.0266  -0.3339 -0.1673 107 LEU J CD1 
19938 C CD2 . LEU K 107 ? 2.6551 4.1905 3.6476 0.0130  -0.3420 -0.1590 107 LEU J CD2 
19939 N N   . SER K 108 ? 2.7158 4.2541 3.7317 0.0300  -0.2956 -0.1259 108 SER J N   
19940 C CA  . SER K 108 ? 2.7450 4.2840 3.7719 0.0348  -0.2792 -0.1143 108 SER J CA  
19941 C C   . SER K 108 ? 2.7146 4.2775 3.7636 0.0328  -0.2799 -0.1081 108 SER J C   
19942 O O   . SER K 108 ? 2.6740 4.2322 3.7200 0.0388  -0.2703 -0.1015 108 SER J O   
19943 C CB  . SER K 108 ? 2.7218 4.2310 3.7200 0.0451  -0.2675 -0.1131 108 SER J CB  
19944 O OG  . SER K 108 ? 2.7772 4.2869 3.7859 0.0499  -0.2514 -0.1017 108 SER J OG  
19945 N N   . GLN K 109 ? 2.6959 4.2850 3.7673 0.0243  -0.2918 -0.1103 109 GLN J N   
19946 C CA  . GLN K 109 ? 2.6415 4.2558 3.7368 0.0218  -0.2934 -0.1047 109 GLN J CA  
19947 C C   . GLN K 109 ? 2.6806 4.3043 3.7980 0.0238  -0.2786 -0.0924 109 GLN J C   
19948 O O   . GLN K 109 ? 2.6310 4.2589 3.7535 0.0275  -0.2730 -0.0864 109 GLN J O   
19949 C CB  . GLN K 109 ? 2.5863 4.2269 3.7012 0.0124  -0.3090 -0.1098 109 GLN J CB  
19950 C CG  . GLN K 109 ? 2.4389 4.1009 3.5681 0.0102  -0.3164 -0.1090 109 GLN J CG  
19951 C CD  . GLN K 109 ? 2.3439 3.9929 3.4481 0.0130  -0.3247 -0.1165 109 GLN J CD  
19952 O OE1 . GLN K 109 ? 2.3335 3.9631 3.4128 0.0140  -0.3298 -0.1247 109 GLN J OE1 
19953 N NE2 . GLN K 109 ? 2.2479 3.9073 3.3587 0.0143  -0.3263 -0.1139 109 GLN J NE2 
19954 N N   . PRO K 110 ? 2.5193 4.1465 3.6504 0.0216  -0.2722 -0.0885 110 PRO J N   
19955 C CA  . PRO K 110 ? 2.5949 4.2232 3.7285 0.0161  -0.2782 -0.0936 110 PRO J CA  
19956 C C   . PRO K 110 ? 2.5586 4.2185 3.7269 0.0078  -0.2830 -0.0902 110 PRO J C   
19957 O O   . PRO K 110 ? 2.5344 4.2057 3.7082 0.0011  -0.2959 -0.0967 110 PRO J O   
19958 C CB  . PRO K 110 ? 2.6547 4.2599 3.7762 0.0218  -0.2639 -0.0898 110 PRO J CB  
19959 C CG  . PRO K 110 ? 2.6843 4.2913 3.8153 0.0271  -0.2492 -0.0787 110 PRO J CG  
19960 C CD  . PRO K 110 ? 2.5563 4.1755 3.6915 0.0275  -0.2544 -0.0781 110 PRO J CD  
19961 N N   . LYS K 111 ? 2.5322 4.2058 3.7233 0.0085  -0.2724 -0.0799 111 LYS J N   
19962 C CA  . LYS K 111 ? 2.4981 4.2018 3.7231 0.0019  -0.2744 -0.0751 111 LYS J CA  
19963 C C   . LYS K 111 ? 2.3858 4.1100 3.6308 0.0022  -0.2729 -0.0687 111 LYS J C   
19964 O O   . LYS K 111 ? 2.4060 4.1192 3.6409 0.0085  -0.2657 -0.0653 111 LYS J O   
19965 C CB  . LYS K 111 ? 2.5558 4.2570 3.7918 0.0020  -0.2626 -0.0684 111 LYS J CB  
19966 C CG  . LYS K 111 ? 2.5832 4.2581 3.8019 0.0104  -0.2466 -0.0633 111 LYS J CG  
19967 C CD  . LYS K 111 ? 2.5533 4.2307 3.7882 0.0100  -0.2350 -0.0557 111 LYS J CD  
19968 C CE  . LYS K 111 ? 2.6085 4.2569 3.8225 0.0182  -0.2203 -0.0524 111 LYS J CE  
19969 N NZ  . LYS K 111 ? 2.5696 4.1916 3.7497 0.0219  -0.2253 -0.0617 111 LYS J NZ  
19970 N N   . ALA K 112 ? 2.5418 4.2964 3.8155 -0.0044 -0.2799 -0.0672 112 ALA J N   
19971 C CA  . ALA K 112 ? 2.4610 4.2379 3.7565 -0.0047 -0.2798 -0.0617 112 ALA J CA  
19972 C C   . ALA K 112 ? 2.4461 4.2528 3.7755 -0.0107 -0.2808 -0.0568 112 ALA J C   
19973 O O   . ALA K 112 ? 2.3852 4.2069 3.7235 -0.0173 -0.2921 -0.0618 112 ALA J O   
19974 C CB  . ALA K 112 ? 2.3106 4.0947 3.5999 -0.0062 -0.2938 -0.0689 112 ALA J CB  
19975 N N   . ALA K 113 ? 2.5024 4.3177 3.8506 -0.0083 -0.2689 -0.0468 113 ALA J N   
19976 C CA  . ALA K 113 ? 2.4498 4.2936 3.8309 -0.0133 -0.2685 -0.0413 113 ALA J CA  
19977 C C   . ALA K 113 ? 2.3642 4.2376 3.7653 -0.0178 -0.2813 -0.0437 113 ALA J C   
19978 O O   . ALA K 113 ? 2.2948 4.1707 3.6958 -0.0149 -0.2821 -0.0428 113 ALA J O   
19979 C CB  . ALA K 113 ? 2.5607 4.4035 3.9547 -0.0089 -0.2518 -0.0300 113 ALA J CB  
19980 N N   . PRO K 114 ? 2.4906 4.3871 3.9093 -0.0248 -0.2914 -0.0465 114 PRO J N   
19981 C CA  . PRO K 114 ? 2.3925 4.3181 3.8300 -0.0291 -0.3045 -0.0494 114 PRO J CA  
19982 C C   . PRO K 114 ? 2.3633 4.3105 3.8279 -0.0280 -0.2989 -0.0412 114 PRO J C   
19983 O O   . PRO K 114 ? 2.3814 4.3348 3.8628 -0.0275 -0.2881 -0.0331 114 PRO J O   
19984 C CB  . PRO K 114 ? 2.3566 4.3000 3.8066 -0.0364 -0.3139 -0.0529 114 PRO J CB  
19985 C CG  . PRO K 114 ? 2.4353 4.3669 3.8857 -0.0357 -0.3018 -0.0474 114 PRO J CG  
19986 C CD  . PRO K 114 ? 2.5159 4.4128 3.9384 -0.0289 -0.2911 -0.0469 114 PRO J CD  
19987 N N   . SER K 115 ? 3.2164 3.3844 3.7389 -0.2340 -0.9828 -0.1232 115 SER J N   
19988 C CA  . SER K 115 ? 3.2715 3.3669 3.7588 -0.2188 -0.9771 -0.1689 115 SER J CA  
19989 C C   . SER K 115 ? 3.3775 3.4478 3.7281 -0.2379 -0.9551 -0.1337 115 SER J C   
19990 O O   . SER K 115 ? 3.3750 3.4943 3.6862 -0.2204 -0.8680 -0.1120 115 SER J O   
19991 C CB  . SER K 115 ? 3.1926 3.3283 3.7534 -0.1706 -0.8961 -0.2057 115 SER J CB  
19992 O OG  . SER K 115 ? 3.0945 3.2544 3.7815 -0.1525 -0.9157 -0.2371 115 SER J OG  
19993 N N   . VAL K 116 ? 3.4144 3.4069 3.6910 -0.2745 -1.0357 -0.1277 116 VAL J N   
19994 C CA  . VAL K 116 ? 3.5032 3.4636 3.6465 -0.2971 -1.0283 -0.0935 116 VAL J CA  
19995 C C   . VAL K 116 ? 3.5224 3.4084 3.6166 -0.2819 -1.0178 -0.1364 116 VAL J C   
19996 O O   . VAL K 116 ? 3.5012 3.3369 3.6555 -0.2656 -1.0488 -0.1935 116 VAL J O   
19997 C CB  . VAL K 116 ? 3.6019 3.5208 3.6902 -0.3449 -1.1193 -0.0616 116 VAL J CB  
19998 C CG1 . VAL K 116 ? 3.5708 3.5712 3.6944 -0.3595 -1.1166 -0.0114 116 VAL J CG1 
19999 C CG2 . VAL K 116 ? 3.5994 3.4371 3.7344 -0.3556 -1.2166 -0.1095 116 VAL J CG2 
20000 N N   . THR K 117 ? 3.6647 3.5508 3.6552 -0.2828 -0.9642 -0.1098 117 THR J N   
20001 C CA  . THR K 117 ? 3.7066 3.5217 3.6364 -0.2704 -0.9520 -0.1450 117 THR J CA  
20002 C C   . THR K 117 ? 3.7841 3.5752 3.5741 -0.2957 -0.9440 -0.1011 117 THR J C   
20003 O O   . THR K 117 ? 3.7294 3.5892 3.4771 -0.2947 -0.8773 -0.0523 117 THR J O   
20004 C CB  . THR K 117 ? 3.5526 3.4056 3.5304 -0.2237 -0.8614 -0.1760 117 THR J CB  
20005 O OG1 . THR K 117 ? 3.4727 3.3551 3.5830 -0.2007 -0.8671 -0.2125 117 THR J OG1 
20006 C CG2 . THR K 117 ? 3.5870 3.3569 3.5107 -0.2119 -0.8615 -0.2190 117 THR J CG2 
20007 N N   . LEU K 118 ? 3.7799 3.4753 3.4985 -0.3173 -1.0098 -0.1179 118 LEU J N   
20008 C CA  . LEU K 118 ? 3.9515 3.6132 3.5345 -0.3439 -1.0138 -0.0787 118 LEU J CA  
20009 C C   . LEU K 118 ? 4.0477 3.6534 3.5640 -0.3250 -0.9784 -0.1089 118 LEU J C   
20010 O O   . LEU K 118 ? 4.1064 3.6353 3.6404 -0.3187 -1.0232 -0.1623 118 LEU J O   
20011 C CB  . LEU K 118 ? 4.0589 3.6526 3.5962 -0.3879 -1.1191 -0.0672 118 LEU J CB  
20012 C CG  . LEU K 118 ? 4.1143 3.6763 3.5090 -0.4160 -1.1219 -0.0230 118 LEU J CG  
20013 C CD1 . LEU K 118 ? 4.0608 3.7117 3.4130 -0.4198 -1.0516 0.0422  118 LEU J CD1 
20014 C CD2 . LEU K 118 ? 4.2220 3.7148 3.5723 -0.4590 -1.2269 -0.0132 118 LEU J CD2 
20015 N N   . PHE K 119 ? 4.0313 3.6747 3.4693 -0.3166 -0.8991 -0.0741 119 PHE J N   
20016 C CA  . PHE K 119 ? 4.0663 3.6615 3.4322 -0.2988 -0.8591 -0.0973 119 PHE J CA  
20017 C C   . PHE K 119 ? 4.1780 3.7223 3.4049 -0.3308 -0.8851 -0.0610 119 PHE J C   
20018 O O   . PHE K 119 ? 4.1647 3.7542 3.3377 -0.3526 -0.8723 -0.0019 119 PHE J O   
20019 C CB  . PHE K 119 ? 3.9415 3.6097 3.3198 -0.2604 -0.7448 -0.0922 119 PHE J CB  
20020 C CG  . PHE K 119 ? 3.8435 3.5348 3.3428 -0.2217 -0.7149 -0.1445 119 PHE J CG  
20021 C CD1 . PHE K 119 ? 3.8819 3.5054 3.3941 -0.2003 -0.7219 -0.2041 119 PHE J CD1 
20022 C CD2 . PHE K 119 ? 3.6559 3.4360 3.2556 -0.2067 -0.6798 -0.1340 119 PHE J CD2 
20023 C CE1 . PHE K 119 ? 3.7560 3.4007 3.3800 -0.1647 -0.6944 -0.2519 119 PHE J CE1 
20024 C CE2 . PHE K 119 ? 3.4824 3.2836 3.1930 -0.1708 -0.6521 -0.1818 119 PHE J CE2 
20025 C CZ  . PHE K 119 ? 3.5502 3.2839 3.2733 -0.1498 -0.6593 -0.2405 119 PHE J CZ  
20026 N N   . PRO K 120 ? 4.0080 3.4590 3.1757 -0.3329 -0.9196 -0.0958 120 PRO J N   
20027 C CA  . PRO K 120 ? 4.1830 3.5781 3.2150 -0.3606 -0.9432 -0.0664 120 PRO J CA  
20028 C C   . PRO K 120 ? 4.2336 3.6693 3.1823 -0.3452 -0.8482 -0.0333 120 PRO J C   
20029 O O   . PRO K 120 ? 4.1398 3.6322 3.1346 -0.3095 -0.7657 -0.0444 120 PRO J O   
20030 C CB  . PRO K 120 ? 4.2723 3.5580 3.2872 -0.3600 -1.0035 -0.1240 120 PRO J CB  
20031 C CG  . PRO K 120 ? 4.1617 3.4601 3.2744 -0.3193 -0.9634 -0.1783 120 PRO J CG  
20032 C CD  . PRO K 120 ? 3.9902 3.3811 3.2158 -0.3089 -0.9391 -0.1659 120 PRO J CD  
20033 N N   . PRO K 121 ? 4.2056 3.6161 3.0319 -0.3708 -0.8556 0.0088  121 PRO J N   
20034 C CA  . PRO K 121 ? 4.2605 3.7093 3.0045 -0.3561 -0.7646 0.0415  121 PRO J CA  
20035 C C   . PRO K 121 ? 4.2871 3.6937 3.0255 -0.3218 -0.7237 -0.0101 121 PRO J C   
20036 O O   . PRO K 121 ? 4.3487 3.6681 3.0859 -0.3225 -0.7801 -0.0587 121 PRO J O   
20037 C CB  . PRO K 121 ? 4.4366 3.8416 3.0506 -0.3929 -0.8022 0.0856  121 PRO J CB  
20038 C CG  . PRO K 121 ? 4.5004 3.8151 3.1177 -0.4184 -0.9100 0.0547  121 PRO J CG  
20039 C CD  . PRO K 121 ? 4.3390 3.6804 3.0923 -0.4129 -0.9458 0.0262  121 PRO J CD  
20040 N N   . SER K 122 ? 4.1779 3.6481 2.9127 -0.2917 -0.6242 0.0016  122 SER J N   
20041 C CA  . SER K 122 ? 4.1802 3.6241 2.9174 -0.2556 -0.5733 -0.0446 122 SER J CA  
20042 C C   . SER K 122 ? 4.3057 3.6644 2.9197 -0.2633 -0.5861 -0.0510 122 SER J C   
20043 O O   . SER K 122 ? 4.3921 3.7290 2.9031 -0.2924 -0.6087 -0.0087 122 SER J O   
20044 C CB  . SER K 122 ? 4.1162 3.6532 2.8697 -0.2235 -0.4605 -0.0235 122 SER J CB  
20045 O OG  . SER K 122 ? 4.1737 3.7436 2.8222 -0.2372 -0.4176 0.0372  122 SER J OG  
20046 N N   . SER K 123 ? 4.2048 3.5130 2.8327 -0.2361 -0.5731 -0.1063 123 SER J N   
20047 C CA  . SER K 123 ? 4.4008 3.6262 2.9171 -0.2391 -0.5815 -0.1183 123 SER J CA  
20048 C C   . SER K 123 ? 4.4738 3.7455 2.8975 -0.2289 -0.4915 -0.0735 123 SER J C   
20049 O O   . SER K 123 ? 4.6702 3.8892 2.9760 -0.2417 -0.4975 -0.0579 123 SER J O   
20050 C CB  . SER K 123 ? 4.4227 3.5871 2.9854 -0.2107 -0.5871 -0.1898 123 SER J CB  
20051 O OG  . SER K 123 ? 4.6178 3.6997 3.0757 -0.2111 -0.5939 -0.2056 123 SER J OG  
20052 N N   . GLU K 124 ? 4.2885 3.6587 2.7659 -0.2050 -0.4073 -0.0534 124 GLU J N   
20053 C CA  . GLU K 124 ? 4.3260 3.7528 2.7299 -0.1916 -0.3132 -0.0108 124 GLU J CA  
20054 C C   . GLU K 124 ? 4.3735 3.8406 2.6979 -0.2228 -0.3110 0.0621  124 GLU J C   
20055 O O   . GLU K 124 ? 4.5112 3.9782 2.7281 -0.2232 -0.2648 0.0948  124 GLU J O   
20056 C CB  . GLU K 124 ? 4.1842 3.7070 2.6891 -0.1572 -0.2317 -0.0148 124 GLU J CB  
20057 C CG  . GLU K 124 ? 4.1802 3.7693 2.6347 -0.1351 -0.1253 0.0192  124 GLU J CG  
20058 C CD  . GLU K 124 ? 4.2278 3.7969 2.6876 -0.0960 -0.0666 -0.0264 124 GLU J CD  
20059 O OE1 . GLU K 124 ? 4.1021 3.7001 2.6722 -0.0681 -0.0441 -0.0659 124 GLU J OE1 
20060 O OE2 . GLU K 124 ? 4.4025 3.9252 2.7566 -0.0933 -0.0449 -0.0235 124 GLU J OE2 
20061 N N   . GLU K 125 ? 4.5119 4.0130 2.8853 -0.2489 -0.3600 0.0890  125 GLU J N   
20062 C CA  . GLU K 125 ? 4.5503 4.0918 2.8529 -0.2792 -0.3595 0.1592  125 GLU J CA  
20063 C C   . GLU K 125 ? 4.7248 4.1824 2.9188 -0.3155 -0.4335 0.1745  125 GLU J C   
20064 O O   . GLU K 125 ? 4.8326 4.3047 2.9278 -0.3331 -0.4137 0.2281  125 GLU J O   
20065 C CB  . GLU K 125 ? 4.3747 3.9937 2.7640 -0.2930 -0.3741 0.1894  125 GLU J CB  
20066 C CG  . GLU K 125 ? 4.3079 3.8891 2.7556 -0.3200 -0.4754 0.1733  125 GLU J CG  
20067 C CD  . GLU K 125 ? 4.1470 3.8185 2.6714 -0.3296 -0.4703 0.2107  125 GLU J CD  
20068 O OE1 . GLU K 125 ? 4.1757 3.9116 2.6510 -0.3380 -0.4223 0.2698  125 GLU J OE1 
20069 O OE2 . GLU K 125 ? 4.0673 3.7460 2.6999 -0.3283 -0.5129 0.1819  125 GLU J OE2 
20070 N N   . LEU K 126 ? 4.5459 3.9153 2.7554 -0.3264 -0.5177 0.1283  126 LEU J N   
20071 C CA  . LEU K 126 ? 4.6614 3.9479 2.7717 -0.3612 -0.5927 0.1402  126 LEU J CA  
20072 C C   . LEU K 126 ? 4.7672 4.0197 2.7498 -0.3537 -0.5454 0.1534  126 LEU J C   
20073 O O   . LEU K 126 ? 4.9268 4.1394 2.8022 -0.3818 -0.5773 0.1873  126 LEU J O   
20074 C CB  . LEU K 126 ? 4.6746 3.8712 2.8313 -0.3665 -0.6811 0.0791  126 LEU J CB  
20075 C CG  . LEU K 126 ? 4.5955 3.8035 2.8669 -0.3802 -0.7499 0.0628  126 LEU J CG  
20076 C CD1 . LEU K 126 ? 4.6199 3.7309 2.9258 -0.3832 -0.8334 -0.0004 126 LEU J CD1 
20077 C CD2 . LEU K 126 ? 4.6112 3.8446 2.8563 -0.4197 -0.7960 0.1189  126 LEU J CD2 
20078 N N   . GLN K 127 ? 4.6679 3.9335 2.6626 -0.3155 -0.4708 0.1248  127 GLN J N   
20079 C CA  . GLN K 127 ? 4.8325 4.0754 2.7208 -0.2999 -0.4108 0.1314  127 GLN J CA  
20080 C C   . GLN K 127 ? 4.8534 4.1763 2.6769 -0.3014 -0.3344 0.1990  127 GLN J C   
20081 O O   . GLN K 127 ? 5.0193 4.3203 2.7326 -0.2980 -0.2958 0.2181  127 GLN J O   
20082 C CB  . GLN K 127 ? 4.7559 4.0010 2.7153 -0.2576 -0.3610 0.0751  127 GLN J CB  
20083 C CG  . GLN K 127 ? 4.7593 3.9174 2.7682 -0.2621 -0.4466 0.0139  127 GLN J CG  
20084 C CD  . GLN K 127 ? 4.7053 3.8488 2.7905 -0.2238 -0.4168 -0.0496 127 GLN J CD  
20085 O OE1 . GLN K 127 ? 4.6431 3.8476 2.7574 -0.1913 -0.3293 -0.0508 127 GLN J OE1 
20086 N NE2 . GLN K 127 ? 4.7081 3.7691 2.8267 -0.2275 -0.4911 -0.1035 127 GLN J NE2 
20087 N N   . ALA K 128 ? 4.6524 4.0669 2.5426 -0.3064 -0.3126 0.2354  128 ALA J N   
20088 C CA  . ALA K 128 ? 4.6499 4.1461 2.4892 -0.3108 -0.2461 0.3026  128 ALA J CA  
20089 C C   . ALA K 128 ? 4.6995 4.1917 2.4868 -0.3549 -0.3080 0.3545  128 ALA J C   
20090 O O   . ALA K 128 ? 4.6785 4.2472 2.4489 -0.3648 -0.2692 0.4131  128 ALA J O   
20091 C CB  . ALA K 128 ? 4.5211 4.1248 2.4659 -0.2868 -0.1771 0.3115  128 ALA J CB  
20092 N N   . ASN K 129 ? 4.7625 4.1651 2.5219 -0.3815 -0.4035 0.3338  129 ASN J N   
20093 C CA  . ASN K 129 ? 4.8159 4.2013 2.5270 -0.4251 -0.4747 0.3765  129 ASN J CA  
20094 C C   . ASN K 129 ? 4.7159 4.1829 2.5232 -0.4375 -0.4855 0.4046  129 ASN J C   
20095 O O   . ASN K 129 ? 4.7310 4.2372 2.5015 -0.4646 -0.4941 0.4628  129 ASN J O   
20096 C CB  . ASN K 129 ? 4.9145 4.3000 2.4877 -0.4393 -0.4422 0.4329  129 ASN J CB  
20097 C CG  . ASN K 129 ? 4.9997 4.3326 2.5030 -0.4837 -0.5286 0.4630  129 ASN J CG  
20098 O OD1 . ASN K 129 ? 5.0105 4.2806 2.5477 -0.5018 -0.6173 0.4307  129 ASN J OD1 
20099 N ND2 . ASN K 129 ? 5.0608 4.4192 2.4663 -0.5013 -0.5031 0.5252  129 ASN J ND2 
20100 N N   . LYS K 130 ? 4.9384 4.4305 2.8710 -0.4165 -0.4847 0.3617  130 LYS J N   
20101 C CA  . LYS K 130 ? 4.7708 4.3375 2.8113 -0.4224 -0.4944 0.3767  130 LYS J CA  
20102 C C   . LYS K 130 ? 4.6602 4.1853 2.8081 -0.4192 -0.5630 0.3166  130 LYS J C   
20103 O O   . LYS K 130 ? 4.6624 4.1292 2.8270 -0.3980 -0.5687 0.2594  130 LYS J O   
20104 C CB  . LYS K 130 ? 4.6410 4.3117 2.7359 -0.3899 -0.3906 0.3926  130 LYS J CB  
20105 C CG  . LYS K 130 ? 4.7167 4.4438 2.7200 -0.3902 -0.3140 0.4545  130 LYS J CG  
20106 C CD  . LYS K 130 ? 4.5810 4.4041 2.6481 -0.3543 -0.2131 0.4596  130 LYS J CD  
20107 C CE  . LYS K 130 ? 4.6462 4.5268 2.6252 -0.3512 -0.1311 0.5184  130 LYS J CE  
20108 N NZ  . LYS K 130 ? 4.5918 4.5128 2.5895 -0.3079 -0.0330 0.4986  130 LYS J NZ  
20109 N N   . ALA K 131 ? 4.8548 4.4106 3.0765 -0.4400 -0.6149 0.3299  131 ALA J N   
20110 C CA  . ALA K 131 ? 4.6804 4.2049 3.0105 -0.4380 -0.6804 0.2772  131 ALA J CA  
20111 C C   . ALA K 131 ? 4.5131 4.1240 2.9486 -0.4409 -0.6781 0.2983  131 ALA J C   
20112 O O   . ALA K 131 ? 4.5289 4.1924 2.9365 -0.4636 -0.6737 0.3569  131 ALA J O   
20113 C CB  . ALA K 131 ? 4.7962 4.2214 3.0872 -0.4712 -0.7892 0.2601  131 ALA J CB  
20114 N N   . THR K 132 ? 4.5152 4.1411 3.0711 -0.4182 -0.6811 0.2514  132 THR J N   
20115 C CA  . THR K 132 ? 4.3595 4.0677 3.0193 -0.4187 -0.6774 0.2690  132 THR J CA  
20116 C C   . THR K 132 ? 4.2445 3.9302 3.0261 -0.4076 -0.7281 0.2109  132 THR J C   
20117 O O   . THR K 132 ? 4.1947 3.8639 3.0240 -0.3747 -0.6990 0.1593  132 THR J O   
20118 C CB  . THR K 132 ? 4.2786 4.0887 2.9627 -0.3895 -0.5680 0.2955  132 THR J CB  
20119 O OG1 . THR K 132 ? 4.3854 4.2224 2.9592 -0.4022 -0.5231 0.3548  132 THR J OG1 
20120 C CG2 . THR K 132 ? 4.1320 4.0255 2.9275 -0.3884 -0.5648 0.3104  132 THR J CG2 
20121 N N   . LEU K 133 ? 4.3381 4.0234 3.1693 -0.4348 -0.8036 0.2200  133 LEU J N   
20122 C CA  . LEU K 133 ? 4.2219 3.8944 3.1734 -0.4279 -0.8564 0.1724  133 LEU J CA  
20123 C C   . LEU K 133 ? 4.0620 3.8386 3.1186 -0.4081 -0.8030 0.1853  133 LEU J C   
20124 O O   . LEU K 133 ? 4.0503 3.8974 3.0920 -0.4214 -0.7758 0.2417  133 LEU J O   
20125 C CB  . LEU K 133 ? 4.2860 3.9034 3.2325 -0.4684 -0.9666 0.1773  133 LEU J CB  
20126 C CG  . LEU K 133 ? 4.4468 3.9527 3.3075 -0.4880 -1.0341 0.1546  133 LEU J CG  
20127 C CD1 . LEU K 133 ? 4.5136 3.9759 3.3665 -0.5298 -1.1379 0.1680  133 LEU J CD1 
20128 C CD2 . LEU K 133 ? 4.4032 3.8532 3.3204 -0.4602 -1.0439 0.0824  133 LEU J CD2 
20129 N N   . VAL K 134 ? 4.1709 3.9573 3.3332 -0.3762 -0.7871 0.1337  134 VAL J N   
20130 C CA  . VAL K 134 ? 4.0238 3.9063 3.2913 -0.3527 -0.7328 0.1393  134 VAL J CA  
20131 C C   . VAL K 134 ? 3.9253 3.8007 3.3114 -0.3543 -0.7994 0.1042  134 VAL J C   
20132 O O   . VAL K 134 ? 3.9134 3.7276 3.3439 -0.3412 -0.8351 0.0459  134 VAL J O   
20133 C CB  . VAL K 134 ? 3.9711 3.8839 3.2639 -0.3075 -0.6388 0.1104  134 VAL J CB  
20134 C CG1 . VAL K 134 ? 3.8360 3.8557 3.2178 -0.2837 -0.5694 0.1266  134 VAL J CG1 
20135 C CG2 . VAL K 134 ? 4.0836 3.9769 3.2563 -0.3043 -0.5862 0.1298  134 VAL J CG2 
20136 N N   . CYS K 135 ? 4.0204 3.9656 3.4667 -0.3651 -0.8062 0.1371  135 CYS J N   
20137 C CA  . CYS K 135 ? 3.9270 3.8719 3.4875 -0.3667 -0.8678 0.1078  135 CYS J CA  
20138 C C   . CYS K 135 ? 3.7842 3.8286 3.4481 -0.3372 -0.8007 0.1114  135 CYS J C   
20139 O O   . CYS K 135 ? 3.7522 3.8721 3.4187 -0.3475 -0.7743 0.1628  135 CYS J O   
20140 C CB  . CYS K 135 ? 3.9635 3.8981 3.5123 -0.4096 -0.9515 0.1425  135 CYS J CB  
20141 S SG  . CYS K 135 ? 3.8848 3.7883 3.5540 -0.4186 -1.0512 0.1009  135 CYS J SG  
20142 N N   . LEU K 136 ? 3.8100 3.8560 3.5565 -0.3003 -0.7705 0.0584  136 LEU J N   
20143 C CA  . LEU K 136 ? 3.6758 3.8122 3.5241 -0.2686 -0.7046 0.0556  136 LEU J CA  
20144 C C   . LEU K 136 ? 3.5867 3.7348 3.5485 -0.2729 -0.7656 0.0369  136 LEU J C   
20145 O O   . LEU K 136 ? 3.5906 3.6701 3.5937 -0.2742 -0.8332 -0.0113 136 LEU J O   
20146 C CB  . LEU K 136 ? 3.6350 3.7716 3.5154 -0.2247 -0.6353 0.0094  136 LEU J CB  
20147 C CG  . LEU K 136 ? 3.7000 3.8398 3.4846 -0.2111 -0.5569 0.0243  136 LEU J CG  
20148 C CD1 . LEU K 136 ? 3.7241 3.9326 3.4404 -0.2277 -0.5108 0.0956  136 LEU J CD1 
20149 C CD2 . LEU K 136 ? 3.8275 3.8628 3.5220 -0.2241 -0.6015 -0.0001 136 LEU J CD2 
20150 N N   . ILE K 137 ? 3.5882 3.8229 3.6004 -0.2745 -0.7414 0.0747  137 ILE J N   
20151 C CA  . ILE K 137 ? 3.5006 3.7581 3.6203 -0.2783 -0.7926 0.0638  137 ILE J CA  
20152 C C   . ILE K 137 ? 3.3726 3.7231 3.5902 -0.2415 -0.7149 0.0599  137 ILE J C   
20153 O O   . ILE K 137 ? 3.3497 3.7784 3.5455 -0.2355 -0.6423 0.1044  137 ILE J O   
20154 C CB  . ILE K 137 ? 3.5340 3.8040 3.6248 -0.3205 -0.8525 0.1154  137 ILE J CB  
20155 C CG1 . ILE K 137 ? 3.6736 3.8642 3.6458 -0.3572 -0.9103 0.1325  137 ILE J CG1 
20156 C CG2 . ILE K 137 ? 3.4624 3.7316 3.6592 -0.3264 -0.9228 0.0938  137 ILE J CG2 
20157 C CD1 . ILE K 137 ? 3.7513 3.9762 3.6133 -0.3717 -0.8581 0.1932  137 ILE J CD1 
20158 N N   . SER K 138 ? 3.3930 3.7353 3.7181 -0.2165 -0.7296 0.0069  138 SER J N   
20159 C CA  . SER K 138 ? 3.2710 3.6957 3.6961 -0.1793 -0.6595 -0.0036 138 SER J CA  
20160 C C   . SER K 138 ? 3.1947 3.6180 3.7406 -0.1729 -0.7153 -0.0389 138 SER J C   
20161 O O   . SER K 138 ? 3.2338 3.5875 3.7881 -0.1944 -0.8064 -0.0612 138 SER J O   
20162 C CB  . SER K 138 ? 3.2534 3.6757 3.6816 -0.1394 -0.5829 -0.0406 138 SER J CB  
20163 O OG  . SER K 138 ? 3.2907 3.6247 3.7351 -0.1325 -0.6326 -0.1002 138 SER J OG  
20164 N N   . ASP K 139 ? 3.1471 3.6503 3.7866 -0.1422 -0.6573 -0.0430 139 ASP J N   
20165 C CA  . ASP K 139 ? 3.0586 3.5764 3.8231 -0.1283 -0.6918 -0.0761 139 ASP J CA  
20166 C C   . ASP K 139 ? 3.0621 3.5714 3.8426 -0.1645 -0.7799 -0.0525 139 ASP J C   
20167 O O   . ASP K 139 ? 3.0477 3.5094 3.8888 -0.1692 -0.8539 -0.0890 139 ASP J O   
20168 C CB  . ASP K 139 ? 3.0635 3.5086 3.8753 -0.1074 -0.7211 -0.1460 139 ASP J CB  
20169 C CG  . ASP K 139 ? 3.0368 3.5002 3.8604 -0.0657 -0.6319 -0.1749 139 ASP J CG  
20170 O OD1 . ASP K 139 ? 2.9615 3.5110 3.8230 -0.0405 -0.5500 -0.1575 139 ASP J OD1 
20171 O OD2 . ASP K 139 ? 3.0921 3.4829 3.8868 -0.0582 -0.6443 -0.2153 139 ASP J OD2 
20172 N N   . PHE K 140 ? 3.0073 3.5639 3.7342 -0.1903 -0.7717 0.0092  140 PHE J N   
20173 C CA  . PHE K 140 ? 3.0085 3.5635 3.7470 -0.2254 -0.8505 0.0369  140 PHE J CA  
20174 C C   . PHE K 140 ? 2.9359 3.5924 3.7142 -0.2246 -0.8096 0.0845  140 PHE J C   
20175 O O   . PHE K 140 ? 2.9313 3.6516 3.6712 -0.2152 -0.7286 0.1211  140 PHE J O   
20176 C CB  . PHE K 140 ? 3.1258 3.6199 3.7488 -0.2691 -0.9093 0.0682  140 PHE J CB  
20177 C CG  . PHE K 140 ? 3.1846 3.7165 3.7057 -0.2787 -0.8462 0.1221  140 PHE J CG  
20178 C CD1 . PHE K 140 ? 3.2426 3.7466 3.6910 -0.2651 -0.7949 0.1116  140 PHE J CD1 
20179 C CD2 . PHE K 140 ? 3.1836 3.7783 3.6811 -0.3013 -0.8388 0.1838  140 PHE J CD2 
20180 C CE1 . PHE K 140 ? 3.2979 3.8363 3.6517 -0.2735 -0.7367 0.1615  140 PHE J CE1 
20181 C CE2 . PHE K 140 ? 3.2418 3.8719 3.6460 -0.3100 -0.7804 0.2342  140 PHE J CE2 
20182 C CZ  . PHE K 140 ? 3.2987 3.9004 3.6305 -0.2959 -0.7292 0.2231  140 PHE J CZ  
20183 N N   . TYR K 141 ? 2.9336 3.6045 3.7901 -0.2338 -0.8659 0.0832  141 TYR J N   
20184 C CA  . TYR K 141 ? 2.8883 3.6507 3.7905 -0.2355 -0.8401 0.1263  141 TYR J CA  
20185 C C   . TYR K 141 ? 2.9178 3.6597 3.8264 -0.2741 -0.9351 0.1481  141 TYR J C   
20186 O O   . TYR K 141 ? 2.9253 3.6049 3.8756 -0.2812 -1.0136 0.1099  141 TYR J O   
20187 C CB  . TYR K 141 ? 2.7690 3.5905 3.7938 -0.1938 -0.7930 0.0949  141 TYR J CB  
20188 C CG  . TYR K 141 ? 2.6600 3.5825 3.7326 -0.1902 -0.7528 0.1384  141 TYR J CG  
20189 C CD1 . TYR K 141 ? 2.6225 3.6241 3.6756 -0.1715 -0.6539 0.1707  141 TYR J CD1 
20190 C CD2 . TYR K 141 ? 2.6005 3.5379 3.7338 -0.2071 -0.8157 0.1490  141 TYR J CD2 
20191 C CE1 . TYR K 141 ? 2.5543 3.6474 3.6502 -0.1687 -0.6180 0.2108  141 TYR J CE1 
20192 C CE2 . TYR K 141 ? 2.5179 3.5460 3.6937 -0.2044 -0.7807 0.1889  141 TYR J CE2 
20193 C CZ  . TYR K 141 ? 2.5087 3.6144 3.6656 -0.1853 -0.6819 0.2197  141 TYR J CZ  
20194 O OH  . TYR K 141 ? 2.4195 3.6151 3.6187 -0.1825 -0.6473 0.2594  141 TYR J OH  
20195 N N   . PRO K 142 ? 2.8373 3.6318 3.7057 -0.2991 -0.9289 0.2098  142 PRO J N   
20196 C CA  . PRO K 142 ? 2.8252 3.6952 3.6408 -0.2953 -0.8422 0.2615  142 PRO J CA  
20197 C C   . PRO K 142 ? 2.9394 3.7696 3.6248 -0.3147 -0.8281 0.2863  142 PRO J C   
20198 O O   . PRO K 142 ? 3.0125 3.7556 3.6448 -0.3350 -0.8919 0.2672  142 PRO J O   
20199 C CB  . PRO K 142 ? 2.7448 3.6720 3.5785 -0.3204 -0.8680 0.3130  142 PRO J CB  
20200 C CG  . PRO K 142 ? 2.7735 3.6278 3.6044 -0.3540 -0.9797 0.3027  142 PRO J CG  
20201 C CD  . PRO K 142 ? 2.7820 3.5672 3.6674 -0.3336 -1.0149 0.2321  142 PRO J CD  
20202 N N   . GLY K 143 ? 2.9411 3.8359 3.5769 -0.3078 -0.7443 0.3288  143 GLY J N   
20203 C CA  . GLY K 143 ? 3.0449 3.9154 3.5586 -0.3221 -0.7164 0.3569  143 GLY J CA  
20204 C C   . GLY K 143 ? 3.1341 3.9887 3.5678 -0.3694 -0.7738 0.4101  143 GLY J C   
20205 O O   . GLY K 143 ? 3.1642 4.0854 3.5650 -0.3808 -0.7352 0.4671  143 GLY J O   
20206 N N   . ALA K 144 ? 3.0136 3.7806 3.4160 -0.3973 -0.8664 0.3924  144 ALA J N   
20207 C CA  . ALA K 144 ? 3.0905 3.8334 3.4150 -0.4438 -0.9284 0.4400  144 ALA J CA  
20208 C C   . ALA K 144 ? 3.1846 3.8165 3.4532 -0.4639 -1.0065 0.4078  144 ALA J C   
20209 O O   . ALA K 144 ? 3.1774 3.7590 3.4962 -0.4742 -1.0876 0.3758  144 ALA J O   
20210 C CB  . ALA K 144 ? 3.0350 3.8169 3.4249 -0.4625 -0.9788 0.4639  144 ALA J CB  
20211 N N   . VAL K 145 ? 3.3321 3.9267 3.4969 -0.4686 -0.9801 0.4162  145 VAL J N   
20212 C CA  . VAL K 145 ? 3.4275 3.9170 3.5309 -0.4854 -1.0453 0.3860  145 VAL J CA  
20213 C C   . VAL K 145 ? 3.5599 4.0208 3.5376 -0.5232 -1.0673 0.4356  145 VAL J C   
20214 O O   . VAL K 145 ? 3.5974 4.1177 3.5211 -0.5285 -1.0096 0.4888  145 VAL J O   
20215 C CB  . VAL K 145 ? 3.4295 3.8866 3.5280 -0.4498 -0.9934 0.3362  145 VAL J CB  
20216 C CG1 . VAL K 145 ? 3.3129 3.7830 3.5349 -0.4141 -0.9842 0.2808  145 VAL J CG1 
20217 C CG2 . VAL K 145 ? 3.4342 3.9486 3.4715 -0.4327 -0.8894 0.3694  145 VAL J CG2 
20218 N N   . THR K 146 ? 3.5787 3.9477 3.5116 -0.5503 -1.1542 0.4183  146 THR J N   
20219 C CA  . THR K 146 ? 3.7181 4.0435 3.5295 -0.5866 -1.1856 0.4573  146 THR J CA  
20220 C C   . THR K 146 ? 3.8100 4.0350 3.5652 -0.5856 -1.2174 0.4126  146 THR J C   
20221 O O   . THR K 146 ? 3.7809 3.9435 3.5859 -0.5849 -1.2831 0.3628  146 THR J O   
20222 C CB  . THR K 146 ? 3.7413 4.0563 3.5516 -0.6284 -1.2729 0.4896  146 THR J CB  
20223 O OG1 . THR K 146 ? 3.6980 3.9571 3.5816 -0.6311 -1.3547 0.4406  146 THR J OG1 
20224 C CG2 . THR K 146 ? 3.7029 4.1175 3.5619 -0.6305 -1.2399 0.5371  146 THR J CG2 
20225 N N   . VAL K 147 ? 3.7524 3.9617 3.4048 -0.5852 -1.1711 0.4300  147 VAL J N   
20226 C CA  . VAL K 147 ? 3.8381 3.9563 3.4278 -0.5819 -1.1896 0.3907  147 VAL J CA  
20227 C C   . VAL K 147 ? 3.9886 4.0454 3.4641 -0.6235 -1.2489 0.4230  147 VAL J C   
20228 O O   . VAL K 147 ? 4.0520 4.1488 3.4567 -0.6420 -1.2212 0.4822  147 VAL J O   
20229 C CB  . VAL K 147 ? 3.8307 3.9724 3.3908 -0.5461 -1.0896 0.3801  147 VAL J CB  
20230 C CG1 . VAL K 147 ? 3.9382 3.9852 3.4409 -0.5407 -1.1096 0.3357  147 VAL J CG1 
20231 C CG2 . VAL K 147 ? 3.6830 3.8913 3.3567 -0.5051 -1.0279 0.3517  147 VAL J CG2 
20232 N N   . ALA K 148 ? 4.0347 3.9949 3.4920 -0.6383 -1.3299 0.3851  148 ALA J N   
20233 C CA  . ALA K 148 ? 4.2078 4.1003 3.5555 -0.6764 -1.3893 0.4096  148 ALA J CA  
20234 C C   . ALA K 148 ? 4.3616 4.1607 3.6530 -0.6686 -1.4054 0.3636  148 ALA J C   
20235 O O   . ALA K 148 ? 4.3485 4.0917 3.6981 -0.6589 -1.4529 0.3067  148 ALA J O   
20236 C CB  . ALA K 148 ? 4.2323 4.0955 3.6071 -0.7124 -1.4917 0.4178  148 ALA J CB  
20237 N N   . TRP K 149 ? 4.3005 4.0819 3.4797 -0.6726 -1.3667 0.3875  149 TRP J N   
20238 C CA  . TRP K 149 ? 4.4344 4.1271 3.5556 -0.6648 -1.3797 0.3451  149 TRP J CA  
20239 C C   . TRP K 149 ? 4.6483 4.2498 3.7051 -0.7038 -1.4805 0.3448  149 TRP J C   
20240 O O   . TRP K 149 ? 4.7487 4.3591 3.7687 -0.7388 -1.5228 0.3915  149 TRP J O   
20241 C CB  . TRP K 149 ? 4.4678 4.1777 3.4953 -0.6503 -1.2936 0.3683  149 TRP J CB  
20242 C CG  . TRP K 149 ? 4.3242 4.1150 3.4072 -0.6098 -1.1919 0.3637  149 TRP J CG  
20243 C CD1 . TRP K 149 ? 4.2435 4.1343 3.3536 -0.6039 -1.1298 0.4091  149 TRP J CD1 
20244 C CD2 . TRP K 149 ? 4.2607 4.0394 3.3758 -0.5696 -1.1392 0.3120  149 TRP J CD2 
20245 N NE1 . TRP K 149 ? 4.1351 4.0773 3.2938 -0.5626 -1.0422 0.3885  149 TRP J NE1 
20246 C CE2 . TRP K 149 ? 4.1423 4.0175 3.3051 -0.5408 -1.0459 0.3291  149 TRP J CE2 
20247 C CE3 . TRP K 149 ? 4.2967 3.9924 3.4062 -0.5553 -1.1623 0.2529  149 TRP J CE3 
20248 C CZ2 . TRP K 149 ? 4.0719 3.9631 3.2764 -0.4985 -0.9756 0.2894  149 TRP J CZ2 
20249 C CZ3 . TRP K 149 ? 4.2131 3.9248 3.3645 -0.5132 -1.0924 0.2135  149 TRP J CZ3 
20250 C CH2 . TRP K 149 ? 4.1039 3.9127 3.3021 -0.4854 -1.0001 0.2320  149 TRP J CH2 
20251 N N   . LYS K 150 ? 4.4720 3.9848 3.5136 -0.6974 -1.5180 0.2918  150 LYS J N   
20252 C CA  . LYS K 150 ? 4.6343 4.0527 3.6187 -0.7312 -1.6149 0.2831  150 LYS J CA  
20253 C C   . LYS K 150 ? 4.7640 4.0994 3.6616 -0.7250 -1.6135 0.2537  150 LYS J C   
20254 O O   . LYS K 150 ? 4.6510 3.9669 3.5823 -0.6922 -1.5803 0.2041  150 LYS J O   
20255 C CB  . LYS K 150 ? 4.5663 3.9497 3.6440 -0.7413 -1.7038 0.2461  150 LYS J CB  
20256 C CG  . LYS K 150 ? 4.4518 3.8995 3.5768 -0.7634 -1.7286 0.2901  150 LYS J CG  
20257 C CD  . LYS K 150 ? 4.3144 3.7190 3.5053 -0.7840 -1.8297 0.2655  150 LYS J CD  
20258 C CE  . LYS K 150 ? 4.2357 3.7156 3.4841 -0.7947 -1.8247 0.3089  150 LYS J CE  
20259 N NZ  . LYS K 150 ? 4.0940 3.5717 3.4729 -0.7709 -1.8257 0.2720  150 LYS J NZ  
20260 N N   . ALA K 151 ? 4.6520 3.9382 3.4383 -0.7569 -1.6512 0.2850  151 ALA J N   
20261 C CA  . ALA K 151 ? 4.7895 3.9841 3.4848 -0.7595 -1.6712 0.2599  151 ALA J CA  
20262 C C   . ALA K 151 ? 4.8977 4.0041 3.6011 -0.7869 -1.7843 0.2308  151 ALA J C   
20263 O O   . ALA K 151 ? 5.0009 4.0920 3.6619 -0.8244 -1.8447 0.2672  151 ALA J O   
20264 C CB  . ALA K 151 ? 4.9352 4.1331 3.4990 -0.7759 -1.6366 0.3141  151 ALA J CB  
20265 N N   . ASP K 152 ? 4.8825 3.9315 3.6409 -0.7680 -1.8123 0.1654  152 ASP J N   
20266 C CA  . ASP K 152 ? 4.8718 3.8427 3.6651 -0.7869 -1.9157 0.1272  152 ASP J CA  
20267 C C   . ASP K 152 ? 4.6985 3.7205 3.5948 -0.7935 -1.9370 0.1429  152 ASP J C   
20268 O O   . ASP K 152 ? 4.4986 3.5660 3.5033 -0.7705 -1.9190 0.1178  152 ASP J O   
20269 C CB  . ASP K 152 ? 5.0391 3.9293 3.7245 -0.8174 -1.9687 0.1427  152 ASP J CB  
20270 C CG  . ASP K 152 ? 5.1831 4.0081 3.7740 -0.8077 -1.9520 0.1185  152 ASP J CG  
20271 O OD1 . ASP K 152 ? 5.1619 3.9813 3.7986 -0.7725 -1.9105 0.0716  152 ASP J OD1 
20272 O OD2 . ASP K 152 ? 5.3797 4.1619 3.8562 -0.8315 -1.9702 0.1474  152 ASP J OD2 
20273 N N   . SER K 153 ? 5.0030 4.0217 3.8784 -0.8158 -1.9535 0.1836  153 SER J N   
20274 C CA  . SER K 153 ? 4.8242 3.8947 3.7948 -0.8156 -1.9499 0.2039  153 SER J CA  
20275 C C   . SER K 153 ? 4.8479 3.9839 3.7651 -0.8437 -1.9381 0.2738  153 SER J C   
20276 O O   . SER K 153 ? 4.6716 3.8545 3.6590 -0.8461 -1.9329 0.2959  153 SER J O   
20277 C CB  . SER K 153 ? 4.8229 3.8305 3.8371 -0.8128 -1.9782 0.1860  153 SER J CB  
20278 O OG  . SER K 153 ? 5.0466 3.9997 3.9596 -0.8388 -2.0033 0.2121  153 SER J OG  
20279 N N   . SER K 154 ? 4.9169 4.0587 3.7098 -0.8632 -1.9297 0.3103  154 SER J N   
20280 C CA  . SER K 154 ? 4.9244 4.1270 3.6462 -0.8890 -1.9115 0.3818  154 SER J CA  
20281 C C   . SER K 154 ? 4.8725 4.1712 3.6153 -0.8677 -1.8316 0.4035  154 SER J C   
20282 O O   . SER K 154 ? 4.9202 4.2209 3.6620 -0.8339 -1.7659 0.3746  154 SER J O   
20283 C CB  . SER K 154 ? 5.0626 4.2130 3.6409 -0.9117 -1.9213 0.4100  154 SER J CB  
20284 O OG  . SER K 154 ? 5.1278 4.3296 3.6521 -0.9365 -1.9053 0.4791  154 SER J OG  
20285 N N   . PRO K 155 ? 4.7778 4.1588 3.5539 -0.8780 -1.8140 0.4515  155 PRO J N   
20286 C CA  . PRO K 155 ? 4.6280 4.1088 3.4432 -0.8493 -1.7141 0.4730  155 PRO J CA  
20287 C C   . PRO K 155 ? 4.7782 4.2804 3.4889 -0.8421 -1.6346 0.5090  155 PRO J C   
20288 O O   . PRO K 155 ? 4.9423 4.4024 3.5449 -0.8676 -1.6568 0.5386  155 PRO J O   
20289 C CB  . PRO K 155 ? 4.4342 3.9848 3.2991 -0.8705 -1.7336 0.5191  155 PRO J CB  
20290 C CG  . PRO K 155 ? 4.5540 4.0468 3.3533 -0.9150 -1.8217 0.5445  155 PRO J CG  
20291 C CD  . PRO K 155 ? 4.6807 4.0680 3.4792 -0.9066 -1.8613 0.4836  155 PRO J CD  
20292 N N   . VAL K 156 ? 4.6875 4.2570 3.4331 -0.8062 -1.5401 0.5060  156 VAL J N   
20293 C CA  . VAL K 156 ? 4.8128 4.4146 3.4736 -0.7928 -1.4519 0.5376  156 VAL J CA  
20294 C C   . VAL K 156 ? 4.7691 4.4705 3.4331 -0.8015 -1.4046 0.6033  156 VAL J C   
20295 O O   . VAL K 156 ? 4.6062 4.3784 3.3686 -0.7881 -1.3817 0.6044  156 VAL J O   
20296 C CB  . VAL K 156 ? 4.7314 4.3437 3.4275 -0.7468 -1.3759 0.4921  156 VAL J CB  
20297 C CG1 . VAL K 156 ? 4.8511 4.5024 3.4619 -0.7330 -1.2828 0.5276  156 VAL J CG1 
20298 C CG2 . VAL K 156 ? 4.7756 4.2879 3.4677 -0.7388 -1.4240 0.4275  156 VAL J CG2 
20299 N N   . LYS K 157 ? 4.5230 4.2295 3.0790 -0.8239 -1.3904 0.6585  157 LYS J N   
20300 C CA  . LYS K 157 ? 4.4947 4.2884 3.0414 -0.8384 -1.3555 0.7263  157 LYS J CA  
20301 C C   . LYS K 157 ? 4.4846 4.3614 3.0296 -0.8064 -1.2403 0.7472  157 LYS J C   
20302 O O   . LYS K 157 ? 4.3418 4.3043 2.9640 -0.7943 -1.1990 0.7642  157 LYS J O   
20303 C CB  . LYS K 157 ? 4.6600 4.4191 3.0854 -0.8765 -1.3901 0.7768  157 LYS J CB  
20304 C CG  . LYS K 157 ? 4.7064 4.3853 3.1134 -0.9136 -1.5034 0.7684  157 LYS J CG  
20305 C CD  . LYS K 157 ? 4.6113 4.3247 3.0733 -0.9426 -1.5612 0.7991  157 LYS J CD  
20306 C CE  . LYS K 157 ? 4.6787 4.2988 3.1181 -0.9752 -1.6726 0.7799  157 LYS J CE  
20307 N NZ  . LYS K 157 ? 4.6680 4.3087 3.1363 -1.0062 -1.7195 0.8166  157 LYS J NZ  
20308 N N   . ALA K 158 ? 4.4623 4.3141 2.9199 -0.7923 -1.1880 0.7457  158 ALA J N   
20309 C CA  . ALA K 158 ? 4.4804 4.4045 2.9207 -0.7634 -1.0783 0.7678  158 ALA J CA  
20310 C C   . ALA K 158 ? 4.4681 4.3736 2.9424 -0.7212 -1.0284 0.7081  158 ALA J C   
20311 O O   . ALA K 158 ? 4.4827 4.3096 2.9726 -0.7158 -1.0774 0.6518  158 ALA J O   
20312 C CB  . ALA K 158 ? 4.6705 4.5907 2.9775 -0.7797 -1.0472 0.8210  158 ALA J CB  
20313 N N   . GLY K 159 ? 4.4172 4.3976 2.9028 -0.6912 -0.9286 0.7222  159 GLY J N   
20314 C CA  . GLY K 159 ? 4.3846 4.3615 2.9000 -0.6491 -0.8668 0.6731  159 GLY J CA  
20315 C C   . GLY K 159 ? 4.2640 4.2817 2.9155 -0.6211 -0.8533 0.6314  159 GLY J C   
20316 O O   . GLY K 159 ? 4.2337 4.2457 2.9167 -0.5854 -0.8052 0.5866  159 GLY J O   
20317 N N   . VAL K 160 ? 4.4930 4.5501 3.2262 -0.6356 -0.8944 0.6436  160 VAL J N   
20318 C CA  . VAL K 160 ? 4.2249 4.3191 3.0902 -0.6100 -0.8870 0.6037  160 VAL J CA  
20319 C C   . VAL K 160 ? 4.0550 4.2617 2.9657 -0.5882 -0.7952 0.6373  160 VAL J C   
20320 O O   . VAL K 160 ? 4.0469 4.3133 2.9413 -0.6085 -0.7864 0.6956  160 VAL J O   
20321 C CB  . VAL K 160 ? 4.0762 4.1484 3.0099 -0.6360 -0.9845 0.5944  160 VAL J CB  
20322 C CG1 . VAL K 160 ? 3.8582 3.9667 2.9291 -0.6087 -0.9781 0.5518  160 VAL J CG1 
20323 C CG2 . VAL K 160 ? 4.2006 4.1611 3.0831 -0.6597 -1.0765 0.5647  160 VAL J CG2 
20324 N N   . GLU K 161 ? 4.2864 4.5216 3.2534 -0.5469 -0.7267 0.6006  161 GLU J N   
20325 C CA  . GLU K 161 ? 4.0967 4.4365 3.1182 -0.5206 -0.6363 0.6228  161 GLU J CA  
20326 C C   . GLU K 161 ? 3.8905 4.2518 3.0450 -0.4913 -0.6336 0.5709  161 GLU J C   
20327 O O   . GLU K 161 ? 3.9008 4.2150 3.0812 -0.4661 -0.6293 0.5135  161 GLU J O   
20328 C CB  . GLU K 161 ? 4.1044 4.4690 3.0510 -0.4976 -0.5396 0.6385  161 GLU J CB  
20329 C CG  . GLU K 161 ? 4.3544 4.6953 3.1684 -0.5280 -0.5469 0.6908  161 GLU J CG  
20330 C CD  . GLU K 161 ? 4.3244 4.7548 3.0968 -0.5235 -0.4596 0.7523  161 GLU J CD  
20331 O OE1 . GLU K 161 ? 4.1240 4.6396 2.9709 -0.5175 -0.4292 0.7753  161 GLU J OE1 
20332 O OE2 . GLU K 161 ? 4.5585 4.9742 3.2234 -0.5268 -0.4231 0.7787  161 GLU J OE2 
20333 N N   . THR K 162 ? 3.8448 4.2767 3.0836 -0.4941 -0.6361 0.5911  162 THR J N   
20334 C CA  . THR K 162 ? 3.6712 4.1257 3.0400 -0.4698 -0.6418 0.5460  162 THR J CA  
20335 C C   . THR K 162 ? 3.5005 4.0649 2.9359 -0.4445 -0.5571 0.5691  162 THR J C   
20336 O O   . THR K 162 ? 3.4787 4.1084 2.8918 -0.4603 -0.5334 0.6279  162 THR J O   
20337 C CB  . THR K 162 ? 3.6420 4.0680 3.0672 -0.4980 -0.7435 0.5391  162 THR J CB  
20338 O OG1 . THR K 162 ? 3.7820 4.1060 3.1433 -0.5237 -0.8252 0.5202  162 THR J OG1 
20339 C CG2 . THR K 162 ? 3.5062 3.9481 3.0646 -0.4716 -0.7524 0.4882  162 THR J CG2 
20340 N N   . THR K 163 ? 3.6536 4.2376 3.1705 -0.4048 -0.5110 0.5224  163 THR J N   
20341 C CA  . THR K 163 ? 3.4675 4.1531 3.0554 -0.3772 -0.4299 0.5376  163 THR J CA  
20342 C C   . THR K 163 ? 3.3733 4.1000 3.0651 -0.3856 -0.4744 0.5409  163 THR J C   
20343 O O   . THR K 163 ? 3.4669 4.1390 3.1910 -0.4050 -0.5641 0.5178  163 THR J O   
20344 C CB  . THR K 163 ? 3.3576 4.0486 2.9965 -0.3312 -0.3646 0.4855  163 THR J CB  
20345 O OG1 . THR K 163 ? 3.3187 3.9712 3.0551 -0.3201 -0.4193 0.4269  163 THR J OG1 
20346 C CG2 . THR K 163 ? 3.4849 4.1155 3.0265 -0.3236 -0.3379 0.4702  163 THR J CG2 
20347 N N   . THR K 164 ? 3.4113 4.2299 3.1525 -0.3710 -0.4137 0.5681  164 THR J N   
20348 C CA  . THR K 164 ? 3.2342 4.1031 3.0789 -0.3738 -0.4427 0.5724  164 THR J CA  
20349 C C   . THR K 164 ? 3.0875 3.9704 3.0494 -0.3349 -0.4222 0.5144  164 THR J C   
20350 O O   . THR K 164 ? 3.0430 3.9448 3.0139 -0.2996 -0.3464 0.4912  164 THR J O   
20351 C CB  . THR K 164 ? 3.0762 4.0457 2.9190 -0.3786 -0.3863 0.6362  164 THR J CB  
20352 O OG1 . THR K 164 ? 3.0096 4.0378 2.8487 -0.3436 -0.2792 0.6398  164 THR J OG1 
20353 C CG2 . THR K 164 ? 3.1441 4.1018 2.8795 -0.4197 -0.4149 0.6956  164 THR J CG2 
20354 N N   . PRO K 165 ? 3.1414 4.0120 3.1908 -0.3415 -0.4911 0.4904  165 PRO J N   
20355 C CA  . PRO K 165 ? 3.0249 3.9079 3.1909 -0.3057 -0.4779 0.4353  165 PRO J CA  
20356 C C   . PRO K 165 ? 2.8567 3.8368 3.0685 -0.2704 -0.3727 0.4480  165 PRO J C   
20357 O O   . PRO K 165 ? 2.7904 3.8444 2.9824 -0.2782 -0.3300 0.5030  165 PRO J O   
20358 C CB  . PRO K 165 ? 3.0000 3.8793 3.2426 -0.3254 -0.5618 0.4316  165 PRO J CB  
20359 C CG  . PRO K 165 ? 3.1334 3.9488 3.2893 -0.3708 -0.6428 0.4577  165 PRO J CG  
20360 C CD  . PRO K 165 ? 3.2053 4.0443 3.2486 -0.3826 -0.5880 0.5108  165 PRO J CD  
20361 N N   . SER K 166 ? 3.0425 4.0217 3.3180 -0.2311 -0.3317 0.3960  166 SER J N   
20362 C CA  . SER K 166 ? 2.8619 3.9272 3.1825 -0.1938 -0.2294 0.4009  166 SER J CA  
20363 C C   . SER K 166 ? 2.7789 3.8357 3.2074 -0.1571 -0.2231 0.3361  166 SER J C   
20364 O O   . SER K 166 ? 2.8696 3.8613 3.2874 -0.1424 -0.2287 0.2882  166 SER J O   
20365 C CB  . SER K 166 ? 2.8795 3.9513 3.1050 -0.1830 -0.1508 0.4190  166 SER J CB  
20366 O OG  . SER K 166 ? 2.9582 3.9431 3.1390 -0.1765 -0.1685 0.3745  166 SER J OG  
20367 N N   . LYS K 167 ? 2.9011 4.0236 3.4327 -0.1426 -0.2118 0.3355  167 LYS J N   
20368 C CA  . LYS K 167 ? 2.8421 3.9635 3.4847 -0.1083 -0.2079 0.2770  167 LYS J CA  
20369 C C   . LYS K 167 ? 2.7973 3.9456 3.4444 -0.0668 -0.1108 0.2543  167 LYS J C   
20370 O O   . LYS K 167 ? 2.7162 3.9207 3.3127 -0.0598 -0.0329 0.2925  167 LYS J O   
20371 C CB  . LYS K 167 ? 2.6449 3.8442 3.3824 -0.1047 -0.2073 0.2957  167 LYS J CB  
20372 C CG  . LYS K 167 ? 2.4704 3.7186 3.3289 -0.0643 -0.1671 0.2590  167 LYS J CG  
20373 C CD  . LYS K 167 ? 2.3170 3.6372 3.2296 -0.0764 -0.1790 0.2984  167 LYS J CD  
20374 C CE  . LYS K 167 ? 2.1751 3.5611 3.2085 -0.0404 -0.1380 0.2758  167 LYS J CE  
20375 N NZ  . LYS K 167 ? 2.0681 3.5186 3.1348 -0.0585 -0.1550 0.3214  167 LYS J NZ  
20376 N N   . GLN K 168 ? 2.7424 3.8497 3.4521 -0.0386 -0.1159 0.1908  168 GLN J N   
20377 C CA  . GLN K 168 ? 2.7221 3.8459 3.4405 0.0019  -0.0294 0.1622  168 GLN J CA  
20378 C C   . GLN K 168 ? 2.6229 3.7705 3.4691 0.0400  -0.0118 0.1116  168 GLN J C   
20379 O O   . GLN K 168 ? 2.6590 3.7415 3.5391 0.0528  -0.0455 0.0556  168 GLN J O   
20380 C CB  . GLN K 168 ? 2.8619 3.8925 3.4958 -0.0036 -0.0501 0.1345  168 GLN J CB  
20381 C CG  . GLN K 168 ? 2.8235 3.8676 3.3881 0.0170  0.0384  0.1409  168 GLN J CG  
20382 C CD  . GLN K 168 ? 3.0165 3.9628 3.4940 0.0065  0.0054  0.1159  168 GLN J CD  
20383 O OE1 . GLN K 168 ? 3.1517 4.0282 3.5891 -0.0264 -0.0812 0.1150  168 GLN J OE1 
20384 N NE2 . GLN K 168 ? 3.0277 3.9680 3.4751 0.0344  0.0739  0.0956  168 GLN J NE2 
20385 N N   . SER K 169 ? 2.6101 3.8502 3.5266 0.0582  0.0411  0.1315  169 SER J N   
20386 C CA  . SER K 169 ? 2.4775 3.7510 3.5154 0.0971  0.0690  0.0879  169 SER J CA  
20387 C C   . SER K 169 ? 2.5203 3.7307 3.6309 0.0924  -0.0221 0.0399  169 SER J C   
20388 O O   . SER K 169 ? 2.4629 3.6618 3.6540 0.1241  -0.0122 -0.0126 169 SER J O   
20389 C CB  . SER K 169 ? 2.4394 3.7163 3.4761 0.1362  0.1513  0.0556  169 SER J CB  
20390 O OG  . SER K 169 ? 2.3639 3.6731 3.5170 0.1744  0.1803  0.0135  169 SER J OG  
20391 N N   . ASN K 170 ? 2.4920 3.6607 3.5754 0.0534  -0.1110 0.0570  170 ASN J N   
20392 C CA  . ASN K 170 ? 2.5293 3.6327 3.6725 0.0451  -0.2035 0.0142  170 ASN J CA  
20393 C C   . ASN K 170 ? 2.6097 3.6947 3.7202 0.0000  -0.2872 0.0511  170 ASN J C   
20394 O O   . ASN K 170 ? 2.6266 3.7614 3.6880 -0.0207 -0.2695 0.1088  170 ASN J O   
20395 C CB  . ASN K 170 ? 2.6126 3.6192 3.7229 0.0489  -0.2349 -0.0362 170 ASN J CB  
20396 C CG  . ASN K 170 ? 2.5417 3.5297 3.7582 0.0834  -0.2386 -0.1006 170 ASN J CG  
20397 O OD1 . ASN K 170 ? 2.4515 3.4778 3.7681 0.0952  -0.2516 -0.1114 170 ASN J OD1 
20398 N ND2 . ASN K 170 ? 2.5787 3.5054 3.7739 0.0993  -0.2302 -0.1441 170 ASN J ND2 
20399 N N   . ASN K 171 ? 2.6583 3.6712 3.7990 -0.0144 -0.3790 0.0167  171 ASN J N   
20400 C CA  . ASN K 171 ? 2.7340 3.7078 3.8361 -0.0587 -0.4703 0.0426  171 ASN J CA  
20401 C C   . ASN K 171 ? 2.9112 3.8158 3.8883 -0.0872 -0.4958 0.0570  171 ASN J C   
20402 O O   . ASN K 171 ? 2.9843 3.8623 3.9045 -0.1268 -0.5588 0.0902  171 ASN J O   
20403 C CB  . ASN K 171 ? 2.7614 3.6805 3.9446 -0.0608 -0.5571 -0.0041 171 ASN J CB  
20404 C CG  . ASN K 171 ? 2.8797 3.7108 4.0571 -0.0485 -0.5819 -0.0632 171 ASN J CG  
20405 O OD1 . ASN K 171 ? 2.9492 3.7805 4.1084 -0.0216 -0.5154 -0.0830 171 ASN J OD1 
20406 N ND2 . ASN K 171 ? 2.9032 3.6587 4.0957 -0.0683 -0.6777 -0.0913 171 ASN J ND2 
20407 N N   . LYS K 172 ? 2.8093 3.6847 3.7449 -0.0667 -0.4473 0.0316  172 LYS J N   
20408 C CA  . LYS K 172 ? 2.9524 3.7599 3.7704 -0.0872 -0.4617 0.0385  172 LYS J CA  
20409 C C   . LYS K 172 ? 3.0109 3.8632 3.7328 -0.1098 -0.4238 0.1062  172 LYS J C   
20410 O O   . LYS K 172 ? 2.9151 3.8427 3.6332 -0.0896 -0.3345 0.1320  172 LYS J O   
20411 C CB  . LYS K 172 ? 2.9554 3.7282 3.7639 -0.0549 -0.4121 -0.0074 172 LYS J CB  
20412 C CG  . LYS K 172 ? 2.8976 3.7313 3.6659 -0.0305 -0.3022 0.0147  172 LYS J CG  
20413 C CD  . LYS K 172 ? 2.8877 3.6855 3.6609 0.0031  -0.2590 -0.0362 172 LYS J CD  
20414 C CE  . LYS K 172 ? 3.1060 3.8007 3.7894 -0.0185 -0.3149 -0.0540 172 LYS J CE  
20415 N NZ  . LYS K 172 ? 3.2506 3.9285 3.8687 0.0022  -0.2469 -0.0659 172 LYS J NZ  
20416 N N   . TYR K 173 ? 3.0974 3.9104 3.7499 -0.1520 -0.4930 0.1379  173 TYR J N   
20417 C CA  . TYR K 173 ? 3.1222 3.9644 3.6718 -0.1752 -0.4622 0.1998  173 TYR J CA  
20418 C C   . TYR K 173 ? 3.2392 4.0026 3.6860 -0.1822 -0.4669 0.1860  173 TYR J C   
20419 O O   . TYR K 173 ? 3.3126 3.9947 3.7675 -0.1813 -0.5203 0.1369  173 TYR J O   
20420 C CB  . TYR K 173 ? 3.1290 3.9752 3.6608 -0.2173 -0.5336 0.2440  173 TYR J CB  
20421 C CG  . TYR K 173 ? 2.9645 3.9049 3.5753 -0.2116 -0.5090 0.2738  173 TYR J CG  
20422 C CD1 . TYR K 173 ? 2.8432 3.7942 3.5711 -0.1963 -0.5400 0.2384  173 TYR J CD1 
20423 C CD2 . TYR K 173 ? 2.8482 3.8657 3.4190 -0.2207 -0.4555 0.3359  173 TYR J CD2 
20424 C CE1 . TYR K 173 ? 2.6171 3.6513 3.4195 -0.1901 -0.5199 0.2630  173 TYR J CE1 
20425 C CE2 . TYR K 173 ? 2.6462 3.7487 3.2930 -0.2149 -0.4350 0.3613  173 TYR J CE2 
20426 C CZ  . TYR K 173 ? 2.4935 3.6032 3.2558 -0.1994 -0.4678 0.3241  173 TYR J CZ  
20427 O OH  . TYR K 173 ? 2.2878 3.4793 3.1262 -0.1929 -0.4491 0.3474  173 TYR J OH  
20428 N N   . ALA K 174 ? 3.0789 3.8648 3.4287 -0.1888 -0.4114 0.2284  174 ALA J N   
20429 C CA  . ALA K 174 ? 3.1730 3.8866 3.4231 -0.1932 -0.4101 0.2160  174 ALA J CA  
20430 C C   . ALA K 174 ? 3.3113 3.9962 3.4466 -0.2360 -0.4493 0.2664  174 ALA J C   
20431 O O   . ALA K 174 ? 3.2891 4.0366 3.3976 -0.2524 -0.4273 0.3239  174 ALA J O   
20432 C CB  . ALA K 174 ? 3.0963 3.8482 3.3241 -0.1578 -0.3039 0.2121  174 ALA J CB  
20433 N N   . ALA K 175 ? 3.1429 3.7326 3.2098 -0.2534 -0.5062 0.2447  175 ALA J N   
20434 C CA  . ALA K 175 ? 3.3032 3.8562 3.2571 -0.2937 -0.5473 0.2885  175 ALA J CA  
20435 C C   . ALA K 175 ? 3.5138 3.9704 3.3829 -0.2985 -0.5723 0.2595  175 ALA J C   
20436 O O   . ALA K 175 ? 3.5556 3.9428 3.4620 -0.2925 -0.6243 0.2046  175 ALA J O   
20437 C CB  . ALA K 175 ? 3.2781 3.8151 3.2567 -0.3302 -0.6420 0.3054  175 ALA J CB  
20438 N N   . SER K 176 ? 3.3651 3.8182 3.1210 -0.3089 -0.5348 0.2965  176 SER J N   
20439 C CA  . SER K 176 ? 3.4714 3.8373 3.1319 -0.3152 -0.5524 0.2773  176 SER J CA  
20440 C C   . SER K 176 ? 3.5760 3.9128 3.1290 -0.3590 -0.5998 0.3281  176 SER J C   
20441 O O   . SER K 176 ? 3.5690 3.9701 3.0834 -0.3715 -0.5629 0.3869  176 SER J O   
20442 C CB  . SER K 176 ? 3.4796 3.8646 3.1004 -0.2818 -0.4550 0.2694  176 SER J CB  
20443 O OG  . SER K 176 ? 3.4465 3.9243 3.0491 -0.2750 -0.3735 0.3219  176 SER J OG  
20444 N N   . SER K 177 ? 3.6198 3.8601 3.1243 -0.3819 -0.6807 0.3058  177 SER J N   
20445 C CA  . SER K 177 ? 3.7772 3.9769 3.1776 -0.4240 -0.7341 0.3479  177 SER J CA  
20446 C C   . SER K 177 ? 3.9435 4.0672 3.2363 -0.4245 -0.7291 0.3341  177 SER J C   
20447 O O   . SER K 177 ? 3.9654 4.0183 3.2728 -0.4116 -0.7570 0.2777  177 SER J O   
20448 C CB  . SER K 177 ? 3.7799 3.9299 3.2145 -0.4559 -0.8448 0.3381  177 SER J CB  
20449 O OG  . SER K 177 ? 3.9176 4.0354 3.2538 -0.4969 -0.8938 0.3828  177 SER J OG  
20450 N N   . TYR K 178 ? 3.9016 4.0404 3.0872 -0.4391 -0.6934 0.3856  178 TYR J N   
20451 C CA  . TYR K 178 ? 4.0846 4.1590 3.1593 -0.4394 -0.6804 0.3798  178 TYR J CA  
20452 C C   . TYR K 178 ? 4.2433 4.2599 3.2175 -0.4832 -0.7513 0.4136  178 TYR J C   
20453 O O   . TYR K 178 ? 4.2391 4.2926 3.2039 -0.5117 -0.7769 0.4631  178 TYR J O   
20454 C CB  . TYR K 178 ? 4.1142 4.2529 3.1363 -0.4178 -0.5720 0.4131  178 TYR J CB  
20455 C CG  . TYR K 178 ? 3.9088 4.1016 3.0159 -0.3729 -0.4937 0.3808  178 TYR J CG  
20456 C CD1 . TYR K 178 ? 3.6609 3.9468 2.8591 -0.3610 -0.4563 0.3986  178 TYR J CD1 
20457 C CD2 . TYR K 178 ? 3.9422 4.0943 3.0389 -0.3425 -0.4567 0.3334  178 TYR J CD2 
20458 C CE1 . TYR K 178 ? 3.5271 3.8641 2.8044 -0.3203 -0.3852 0.3700  178 TYR J CE1 
20459 C CE2 . TYR K 178 ? 3.7998 4.0030 2.9761 -0.3015 -0.3848 0.3045  178 TYR J CE2 
20460 C CZ  . TYR K 178 ? 3.6309 3.9267 2.8972 -0.2906 -0.3493 0.3232  178 TYR J CZ  
20461 O OH  . TYR K 178 ? 3.5346 3.8826 2.8810 -0.2498 -0.2777 0.2952  178 TYR J OH  
20462 N N   . LEU K 179 ? 4.0906 4.0157 2.9894 -0.4882 -0.7831 0.3863  179 LEU J N   
20463 C CA  . LEU K 179 ? 4.2019 4.0640 2.9964 -0.5278 -0.8481 0.4147  179 LEU J CA  
20464 C C   . LEU K 179 ? 4.3920 4.2079 3.0730 -0.5194 -0.8078 0.4135  179 LEU J C   
20465 O O   . LEU K 179 ? 4.4900 4.2334 3.1631 -0.5052 -0.8241 0.3610  179 LEU J O   
20466 C CB  . LEU K 179 ? 4.2252 4.0046 3.0510 -0.5496 -0.9581 0.3767  179 LEU J CB  
20467 C CG  . LEU K 179 ? 4.3391 4.0469 3.0636 -0.5915 -1.0346 0.4014  179 LEU J CG  
20468 C CD1 . LEU K 179 ? 4.3495 4.1161 3.0323 -0.6213 -1.0324 0.4744  179 LEU J CD1 
20469 C CD2 . LEU K 179 ? 4.3499 3.9797 3.1193 -0.6095 -1.1408 0.3588  179 LEU J CD2 
20470 N N   . SER K 180 ? 4.2438 4.1013 2.8376 -0.5281 -0.7555 0.4713  180 SER J N   
20471 C CA  . SER K 180 ? 4.3765 4.1962 2.8571 -0.5205 -0.7128 0.4762  180 SER J CA  
20472 C C   . SER K 180 ? 4.6431 4.3685 3.0314 -0.5559 -0.7971 0.4799  180 SER J C   
20473 O O   . SER K 180 ? 4.7119 4.4438 3.0617 -0.5912 -0.8409 0.5266  180 SER J O   
20474 C CB  . SER K 180 ? 4.3441 4.2456 2.7681 -0.5153 -0.6233 0.5368  180 SER J CB  
20475 O OG  . SER K 180 ? 4.3628 4.2924 2.7454 -0.5518 -0.6537 0.5983  180 SER J OG  
20476 N N   . LEU K 181 ? 4.5391 4.1775 2.8912 -0.5467 -0.8199 0.4317  181 LEU J N   
20477 C CA  . LEU K 181 ? 4.6567 4.1999 2.9198 -0.5775 -0.8985 0.4300  181 LEU J CA  
20478 C C   . LEU K 181 ? 4.9258 4.4198 3.0816 -0.5642 -0.8568 0.4222  181 LEU J C   
20479 O O   . LEU K 181 ? 4.9100 4.4402 3.0657 -0.5306 -0.7707 0.4140  181 LEU J O   
20480 C CB  . LEU K 181 ? 4.6460 4.1135 2.9733 -0.5856 -0.9925 0.3734  181 LEU J CB  
20481 C CG  . LEU K 181 ? 4.5720 4.0669 2.9975 -0.6042 -1.0551 0.3763  181 LEU J CG  
20482 C CD1 . LEU K 181 ? 4.5789 3.9884 3.0548 -0.6097 -1.1443 0.3164  181 LEU J CD1 
20483 C CD2 . LEU K 181 ? 4.6130 4.1283 2.9822 -0.6448 -1.0914 0.4409  181 LEU J CD2 
20484 N N   . THR K 182 ? 4.9105 4.3241 2.9763 -0.5903 -0.9173 0.4256  182 THR J N   
20485 C CA  . THR K 182 ? 5.1143 4.4726 3.0749 -0.5793 -0.8861 0.4160  182 THR J CA  
20486 C C   . THR K 182 ? 5.1604 4.4219 3.1370 -0.5695 -0.9382 0.3459  182 THR J C   
20487 O O   . THR K 182 ? 5.0600 4.2802 3.0976 -0.5845 -1.0202 0.3161  182 THR J O   
20488 C CB  . THR K 182 ? 5.2856 4.6129 3.1172 -0.6136 -0.9127 0.4682  182 THR J CB  
20489 O OG1 . THR K 182 ? 5.3419 4.5957 3.1662 -0.6476 -1.0206 0.4571  182 THR J OG1 
20490 C CG2 . THR K 182 ? 5.2728 4.6943 3.0907 -0.6265 -0.8687 0.5395  182 THR J CG2 
20491 N N   . PRO K 183 ? 5.2638 4.4889 3.1895 -0.5435 -0.8912 0.3179  183 PRO J N   
20492 C CA  . PRO K 183 ? 5.3223 4.4520 3.2580 -0.5342 -0.9405 0.2512  183 PRO J CA  
20493 C C   . PRO K 183 ? 5.4731 4.5128 3.3588 -0.5716 -1.0467 0.2465  183 PRO J C   
20494 O O   . PRO K 183 ? 5.4123 4.3827 3.3420 -0.5707 -1.1095 0.1920  183 PRO J O   
20495 C CB  . PRO K 183 ? 5.4780 4.5870 3.3327 -0.5073 -0.8686 0.2410  183 PRO J CB  
20496 C CG  . PRO K 183 ? 5.3439 4.5584 3.2104 -0.4871 -0.7676 0.2813  183 PRO J CG  
20497 C CD  . PRO K 183 ? 5.3139 4.5887 3.1837 -0.5180 -0.7870 0.3421  183 PRO J CD  
20498 N N   . GLU K 184 ? 5.5054 4.5442 3.3011 -0.6044 -1.0690 0.3023  184 GLU J N   
20499 C CA  . GLU K 184 ? 5.5815 4.5381 3.3321 -0.6414 -1.1714 0.3005  184 GLU J CA  
20500 C C   . GLU K 184 ? 5.3893 4.3665 3.2375 -0.6627 -1.2402 0.3007  184 GLU J C   
20501 O O   . GLU K 184 ? 5.3798 4.2843 3.2452 -0.6812 -1.3297 0.2691  184 GLU J O   
20502 C CB  . GLU K 184 ? 5.7953 4.7426 3.4139 -0.6689 -1.1713 0.3603  184 GLU J CB  
20503 C CG  . GLU K 184 ? 6.0883 5.0172 3.6014 -0.6497 -1.1027 0.3662  184 GLU J CG  
20504 C CD  . GLU K 184 ? 6.3764 5.3107 3.7665 -0.6759 -1.0950 0.4317  184 GLU J CD  
20505 O OE1 . GLU K 184 ? 6.3557 5.3158 3.7479 -0.7079 -1.1376 0.4742  184 GLU J OE1 
20506 O OE2 . GLU K 184 ? 6.6289 5.5411 3.9204 -0.6644 -1.0471 0.4406  184 GLU J OE2 
20507 N N   . GLN K 185 ? 5.4762 4.5514 3.3879 -0.6606 -1.2002 0.3364  185 GLN J N   
20508 C CA  . GLN K 185 ? 5.3117 4.4114 3.3177 -0.6798 -1.2621 0.3385  185 GLN J CA  
20509 C C   . GLN K 185 ? 5.1501 4.2277 3.2741 -0.6581 -1.2890 0.2708  185 GLN J C   
20510 O O   . GLN K 185 ? 5.0664 4.1105 3.2469 -0.6772 -1.3722 0.2509  185 GLN J O   
20511 C CB  . GLN K 185 ? 5.2200 4.4312 3.2625 -0.6814 -1.2084 0.3940  185 GLN J CB  
20512 C CG  . GLN K 185 ? 5.0611 4.3020 3.1946 -0.7031 -1.2707 0.4028  185 GLN J CG  
20513 C CD  . GLN K 185 ? 5.1475 4.3471 3.2159 -0.7493 -1.3540 0.4391  185 GLN J CD  
20514 O OE1 . GLN K 185 ? 5.2930 4.4067 3.2774 -0.7657 -1.4026 0.4288  185 GLN J OE1 
20515 N NE2 . GLN K 185 ? 5.0552 4.3161 3.1632 -0.7704 -1.3712 0.4818  185 GLN J NE2 
20516 N N   . TRP K 186 ? 5.3629 4.4604 3.5263 -0.6178 -1.2185 0.2355  186 TRP J N   
20517 C CA  . TRP K 186 ? 5.1699 4.2528 3.4484 -0.5937 -1.2351 0.1717  186 TRP J CA  
20518 C C   . TRP K 186 ? 5.2677 4.2385 3.5331 -0.6022 -1.3177 0.1183  186 TRP J C   
20519 O O   . TRP K 186 ? 5.1071 4.0527 3.4599 -0.6066 -1.3821 0.0819  186 TRP J O   
20520 C CB  . TRP K 186 ? 5.1139 4.2404 3.4231 -0.5489 -1.1365 0.1490  186 TRP J CB  
20521 C CG  . TRP K 186 ? 5.0207 4.1148 3.4272 -0.5222 -1.1515 0.0788  186 TRP J CG  
20522 C CD1 . TRP K 186 ? 5.0881 4.1197 3.4735 -0.4989 -1.1382 0.0292  186 TRP J CD1 
20523 C CD2 . TRP K 186 ? 4.7979 3.9142 3.3346 -0.5171 -1.1874 0.0491  186 TRP J CD2 
20524 N NE1 . TRP K 186 ? 4.9524 3.9680 3.4480 -0.4792 -1.1614 -0.0288 186 TRP J NE1 
20525 C CE2 . TRP K 186 ? 4.7379 3.8047 3.3278 -0.4896 -1.1915 -0.0180 186 TRP J CE2 
20526 C CE3 . TRP K 186 ? 4.5849 3.7585 3.1989 -0.5324 -1.2153 0.0728  186 TRP J CE3 
20527 C CZ2 . TRP K 186 ? 4.4852 3.5586 3.2018 -0.4769 -1.2220 -0.0612 186 TRP J CZ2 
20528 C CZ3 . TRP K 186 ? 4.3849 3.5643 3.1240 -0.5195 -1.2457 0.0293  186 TRP J CZ3 
20529 C CH2 . TRP K 186 ? 4.3505 3.4804 3.1396 -0.4919 -1.2485 -0.0368 186 TRP J CH2 
20530 N N   . LYS K 187 ? 5.1018 4.0041 3.2594 -0.6045 -1.3178 0.1128  187 LYS J N   
20531 C CA  . LYS K 187 ? 5.1685 3.9619 3.3072 -0.6120 -1.3939 0.0623  187 LYS J CA  
20532 C C   . LYS K 187 ? 5.2351 3.9734 3.3313 -0.6564 -1.4938 0.0814  187 LYS J C   
20533 O O   . LYS K 187 ? 5.2900 3.9371 3.3734 -0.6666 -1.5665 0.0415  187 LYS J O   
20534 C CB  . LYS K 187 ? 5.2523 3.9923 3.2975 -0.5938 -1.3529 0.0440  187 LYS J CB  
20535 C CG  . LYS K 187 ? 5.1808 3.9615 3.2857 -0.5479 -1.2668 0.0103  187 LYS J CG  
20536 C CD  . LYS K 187 ? 5.2553 3.9661 3.2919 -0.5276 -1.2440 -0.0265 187 LYS J CD  
20537 C CE  . LYS K 187 ? 5.2600 3.8853 3.3501 -0.5234 -1.3146 -0.0948 187 LYS J CE  
20538 N NZ  . LYS K 187 ? 5.1367 3.8052 3.3730 -0.5043 -1.3152 -0.1295 187 LYS J NZ  
20539 N N   . SER K 188 ? 5.3025 4.0947 3.3777 -0.6825 -1.4986 0.1413  188 SER J N   
20540 C CA  . SER K 188 ? 5.3544 4.1055 3.3851 -0.7261 -1.5868 0.1687  188 SER J CA  
20541 C C   . SER K 188 ? 5.1954 3.9286 3.3325 -0.7378 -1.6683 0.1366  188 SER J C   
20542 O O   . SER K 188 ? 5.2199 3.8658 3.3558 -0.7483 -1.7443 0.0957  188 SER J O   
20543 C CB  . SER K 188 ? 5.3870 4.2119 3.3713 -0.7473 -1.5574 0.2439  188 SER J CB  
20544 O OG  . SER K 188 ? 5.5448 4.3854 3.4266 -0.7377 -1.4837 0.2760  188 SER J OG  
20545 N N   . HIS K 189 ? 5.2836 4.0992 3.5127 -0.7357 -1.6527 0.1551  189 HIS J N   
20546 C CA  . HIS K 189 ? 5.1312 3.9393 3.4627 -0.7476 -1.7270 0.1310  189 HIS J CA  
20547 C C   . HIS K 189 ? 5.0494 3.8151 3.4661 -0.7192 -1.7404 0.0573  189 HIS J C   
20548 O O   . HIS K 189 ? 5.0788 3.8415 3.4938 -0.6861 -1.6790 0.0274  189 HIS J O   
20549 C CB  . HIS K 189 ? 4.9854 3.8970 3.3946 -0.7480 -1.6969 0.1685  189 HIS J CB  
20550 C CG  . HIS K 189 ? 5.0650 4.0208 3.3977 -0.7765 -1.6860 0.2414  189 HIS J CG  
20551 N ND1 . HIS K 189 ? 5.1852 4.1775 3.4309 -0.7688 -1.6074 0.2816  189 HIS J ND1 
20552 C CD2 . HIS K 189 ? 5.0496 4.0164 3.3775 -0.8130 -1.7452 0.2813  189 HIS J CD2 
20553 C CE1 . HIS K 189 ? 5.2374 4.2637 3.4305 -0.7990 -1.6174 0.3437  189 HIS J CE1 
20554 N NE2 . HIS K 189 ? 5.1557 4.1672 3.3971 -0.8264 -1.7007 0.3448  189 HIS J NE2 
20555 N N   . LYS K 190 ? 5.0133 3.7459 3.5060 -0.7328 -1.8230 0.0282  190 LYS J N   
20556 C CA  . LYS K 190 ? 4.9652 3.6517 3.5407 -0.7095 -1.8473 -0.0419 190 LYS J CA  
20557 C C   . LYS K 190 ? 4.8463 3.6110 3.5285 -0.6704 -1.7728 -0.0611 190 LYS J C   
20558 O O   . LYS K 190 ? 4.8301 3.5779 3.5368 -0.6376 -1.7326 -0.1058 190 LYS J O   
20559 C CB  . LYS K 190 ? 4.9508 3.5938 3.5887 -0.7341 -1.9516 -0.0630 190 LYS J CB  
20560 C CG  . LYS K 190 ? 5.0458 3.6174 3.6213 -0.7618 -2.0115 -0.0495 190 LYS J CG  
20561 C CD  . LYS K 190 ? 4.9799 3.5537 3.6884 -0.7476 -2.0246 -0.0652 190 LYS J CD  
20562 C CE  . LYS K 190 ? 5.0555 3.5735 3.7318 -0.7634 -2.0578 -0.0476 190 LYS J CE  
20563 N NZ  . LYS K 190 ? 5.0997 3.6465 3.6999 -0.7983 -2.0664 0.0163  190 LYS J NZ  
20564 N N   . SER K 191 ? 4.9595 3.8106 3.7057 -0.6733 -1.7532 -0.0273 191 SER J N   
20565 C CA  . SER K 191 ? 4.7688 3.6993 3.6209 -0.6381 -1.6857 -0.0421 191 SER J CA  
20566 C C   . SER K 191 ? 4.6613 3.6907 3.5313 -0.6476 -1.6493 0.0176  191 SER J C   
20567 O O   . SER K 191 ? 4.7166 3.7471 3.5481 -0.6833 -1.6981 0.0600  191 SER J O   
20568 C CB  . SER K 191 ? 4.5975 3.5044 3.5716 -0.6264 -1.7374 -0.0991 191 SER J CB  
20569 O OG  . SER K 191 ? 4.6704 3.4738 3.6222 -0.6307 -1.8008 -0.1479 191 SER J OG  
20570 N N   . TYR K 192 ? 4.5288 3.6412 3.4568 -0.6154 -1.5624 0.0209  192 TYR J N   
20571 C CA  . TYR K 192 ? 4.4461 3.6591 3.4051 -0.6188 -1.5196 0.0728  192 TYR J CA  
20572 C C   . TYR K 192 ? 4.2603 3.5192 3.3618 -0.5989 -1.5221 0.0425  192 TYR J C   
20573 O O   . TYR K 192 ? 4.2050 3.4383 3.3724 -0.5709 -1.5171 -0.0143 192 TYR J O   
20574 C CB  . TYR K 192 ? 4.5000 3.7768 3.4036 -0.5980 -1.4119 0.1067  192 TYR J CB  
20575 C CG  . TYR K 192 ? 4.6793 3.9319 3.4431 -0.6234 -1.4083 0.1544  192 TYR J CG  
20576 C CD1 . TYR K 192 ? 4.8286 4.0040 3.5023 -0.6205 -1.4096 0.1330  192 TYR J CD1 
20577 C CD2 . TYR K 192 ? 4.7024 4.0087 3.4247 -0.6500 -1.4042 0.2204  192 TYR J CD2 
20578 C CE1 . TYR K 192 ? 4.9997 4.1516 3.5457 -0.6430 -1.4069 0.1758  192 TYR J CE1 
20579 C CE2 . TYR K 192 ? 4.8718 4.1556 3.4673 -0.6728 -1.4013 0.2639  192 TYR J CE2 
20580 C CZ  . TYR K 192 ? 5.0220 4.2286 3.5296 -0.6689 -1.4025 0.2413  192 TYR J CZ  
20581 O OH  . TYR K 192 ? 5.1983 4.3819 3.5792 -0.6909 -1.3994 0.2844  192 TYR J OH  
20582 N N   . SER K 193 ? 4.6175 3.9438 3.7659 -0.6135 -1.5304 0.0810  193 SER J N   
20583 C CA  . SER K 193 ? 4.4134 3.7882 3.6941 -0.5990 -1.5380 0.0604  193 SER J CA  
20584 C C   . SER K 193 ? 4.2735 3.7615 3.5879 -0.5874 -1.4603 0.1058  193 SER J C   
20585 O O   . SER K 193 ? 4.3352 3.8619 3.5724 -0.6023 -1.4252 0.1619  193 SER J O   
20586 C CB  . SER K 193 ? 4.3054 3.6399 3.6236 -0.6315 -1.6456 0.0558  193 SER J CB  
20587 O OG  . SER K 193 ? 4.3988 3.7100 3.6223 -0.6725 -1.6916 0.1039  193 SER J OG  
20588 N N   . CYS K 194 ? 4.4052 3.9465 3.8368 -0.5595 -1.4323 0.0805  194 CYS J N   
20589 C CA  . CYS K 194 ? 4.2249 3.8755 3.7078 -0.5445 -1.3601 0.1162  194 CYS J CA  
20590 C C   . CYS K 194 ? 4.0497 3.7324 3.6417 -0.5517 -1.4104 0.1122  194 CYS J C   
20591 O O   . CYS K 194 ? 3.9017 3.5912 3.5975 -0.5258 -1.4102 0.0664  194 CYS J O   
20592 C CB  . CYS K 194 ? 4.1763 3.8734 3.6941 -0.4977 -1.2575 0.0924  194 CYS J CB  
20593 S SG  . CYS K 194 ? 4.1905 4.0219 3.7733 -0.4812 -1.1739 0.1375  194 CYS J SG  
20594 N N   . GLN K 195 ? 4.1946 3.8940 3.7613 -0.5876 -1.4564 0.1602  195 GLN J N   
20595 C CA  . GLN K 195 ? 4.0604 3.7878 3.7193 -0.5994 -1.5103 0.1627  195 GLN J CA  
20596 C C   . GLN K 195 ? 3.8580 3.6973 3.5780 -0.5813 -1.4365 0.1951  195 GLN J C   
20597 O O   . GLN K 195 ? 3.8974 3.7912 3.5598 -0.5942 -1.3961 0.2529  195 GLN J O   
20598 C CB  . GLN K 195 ? 4.1634 3.8600 3.7607 -0.6470 -1.5900 0.2036  195 GLN J CB  
20599 C CG  . GLN K 195 ? 4.0542 3.7194 3.7223 -0.6664 -1.6857 0.1846  195 GLN J CG  
20600 C CD  . GLN K 195 ? 4.1832 3.7435 3.8453 -0.6715 -1.7593 0.1305  195 GLN J CD  
20601 O OE1 . GLN K 195 ? 4.2075 3.7170 3.8138 -0.6598 -1.7391 0.1054  195 GLN J OE1 
20602 N NE2 . GLN K 195 ? 4.2405 3.7721 3.9707 -0.6595 -1.7669 0.1126  195 GLN J NE2 
20603 N N   . VAL K 196 ? 3.8755 3.7489 3.7121 -0.5512 -1.4187 0.1579  196 VAL J N   
20604 C CA  . VAL K 196 ? 3.7510 3.7290 3.6600 -0.5303 -1.3506 0.1808  196 VAL J CA  
20605 C C   . VAL K 196 ? 3.6324 3.6353 3.6315 -0.5438 -1.4110 0.1845  196 VAL J C   
20606 O O   . VAL K 196 ? 3.5769 3.5413 3.6549 -0.5354 -1.4625 0.1354  196 VAL J O   
20607 C CB  . VAL K 196 ? 3.6905 3.6956 3.6652 -0.4821 -1.2746 0.1368  196 VAL J CB  
20608 C CG1 . VAL K 196 ? 3.5838 3.6965 3.6382 -0.4599 -1.2067 0.1586  196 VAL J CG1 
20609 C CG2 . VAL K 196 ? 3.7952 3.7767 3.6794 -0.4679 -1.2126 0.1335  196 VAL J CG2 
20610 N N   . THR K 197 ? 3.6609 3.7276 3.6492 -0.5644 -1.4051 0.2424  197 THR J N   
20611 C CA  . THR K 197 ? 3.5461 3.6442 3.6153 -0.5782 -1.4576 0.2528  197 THR J CA  
20612 C C   . THR K 197 ? 3.4062 3.6031 3.5683 -0.5461 -1.3840 0.2577  197 THR J C   
20613 O O   . THR K 197 ? 3.3947 3.6655 3.5274 -0.5438 -1.3159 0.3054  197 THR J O   
20614 C CB  . THR K 197 ? 3.5833 3.6874 3.5863 -0.6226 -1.5039 0.3129  197 THR J CB  
20615 O OG1 . THR K 197 ? 3.7117 3.7225 3.6282 -0.6520 -1.5727 0.3075  197 THR J OG1 
20616 C CG2 . THR K 197 ? 3.4799 3.6145 3.5691 -0.6359 -1.5595 0.3213  197 THR J CG2 
20617 N N   . HIS K 198 ? 3.5335 3.7337 3.8069 -0.5212 -1.3960 0.2100  198 HIS J N   
20618 C CA  . HIS K 198 ? 3.4002 3.6934 3.7653 -0.4907 -1.3294 0.2137  198 HIS J CA  
20619 C C   . HIS K 198 ? 3.3575 3.6655 3.8169 -0.5000 -1.3937 0.2084  198 HIS J C   
20620 O O   . HIS K 198 ? 3.3767 3.6229 3.8850 -0.5007 -1.4625 0.1622  198 HIS J O   
20621 C CB  . HIS K 198 ? 3.3841 3.6812 3.8033 -0.4446 -1.2663 0.1614  198 HIS J CB  
20622 C CG  . HIS K 198 ? 3.2435 3.6311 3.7648 -0.4117 -1.2031 0.1594  198 HIS J CG  
20623 N ND1 . HIS K 198 ? 3.1292 3.6021 3.6664 -0.4192 -1.1740 0.2112  198 HIS J ND1 
20624 C CD2 . HIS K 198 ? 3.2068 3.6131 3.8182 -0.3708 -1.1620 0.1122  198 HIS J CD2 
20625 C CE1 . HIS K 198 ? 2.9801 3.5201 3.6122 -0.3843 -1.1178 0.1957  198 HIS J CE1 
20626 N NE2 . HIS K 198 ? 3.0352 3.5366 3.7143 -0.3544 -1.1096 0.1359  198 HIS J NE2 
20627 N N   . GLU K 199 ? 3.4401 3.8292 3.9239 -0.5073 -1.3716 0.2558  199 GLU J N   
20628 C CA  . GLU K 199 ? 3.3450 3.7549 3.9120 -0.5139 -1.4191 0.2566  199 GLU J CA  
20629 C C   . GLU K 199 ? 3.4456 3.7528 3.9592 -0.5260 -1.4565 0.2419  199 GLU J C   
20630 O O   . GLU K 199 ? 3.5102 3.8075 3.9545 -0.5554 -1.4739 0.2852  199 GLU J O   
20631 C CB  . GLU K 199 ? 3.1664 3.5911 3.8492 -0.4702 -1.3880 0.2023  199 GLU J CB  
20632 C CG  . GLU K 199 ? 3.0292 3.5526 3.7700 -0.4396 -1.3048 0.2118  199 GLU J CG  
20633 C CD  . GLU K 199 ? 2.9193 3.5339 3.6711 -0.4491 -1.2735 0.2703  199 GLU J CD  
20634 O OE1 . GLU K 199 ? 2.8859 3.5223 3.7099 -0.4445 -1.2913 0.2665  199 GLU J OE1 
20635 O OE2 . GLU K 199 ? 2.9478 3.6057 3.6280 -0.4536 -1.2119 0.3155  199 GLU J OE2 
20636 N N   . GLY K 200 ? 3.2377 3.4712 3.7857 -0.5025 -1.4660 0.1828  200 GLY J N   
20637 C CA  . GLY K 200 ? 3.2892 3.4296 3.8012 -0.5084 -1.4963 0.1662  200 GLY J CA  
20638 C C   . GLY K 200 ? 3.3855 3.4368 3.8602 -0.5065 -1.5256 0.1256  200 GLY J C   
20639 O O   . GLY K 200 ? 3.4487 3.4232 3.8779 -0.5170 -1.5548 0.1206  200 GLY J O   
20640 N N   . SER K 201 ? 3.2234 3.2829 3.7190 -0.4919 -1.5174 0.0957  201 SER J N   
20641 C CA  . SER K 201 ? 3.3247 3.2982 3.7867 -0.4877 -1.5424 0.0539  201 SER J CA  
20642 C C   . SER K 201 ? 3.4344 3.3975 3.7998 -0.5175 -1.5669 0.0777  201 SER J C   
20643 O O   . SER K 201 ? 3.4260 3.4602 3.7631 -0.5362 -1.5578 0.1236  201 SER J O   
20644 C CB  . SER K 201 ? 3.2749 3.2507 3.8210 -0.4495 -1.5175 -0.0018 201 SER J CB  
20645 O OG  . SER K 201 ? 3.3647 3.2602 3.8772 -0.4448 -1.5390 -0.0419 201 SER J OG  
20646 N N   . THR K 202 ? 3.4696 3.3437 3.7792 -0.5218 -1.5961 0.0492  202 THR J N   
20647 C CA  . THR K 202 ? 3.6578 3.5067 3.8628 -0.5493 -1.6207 0.0672  202 THR J CA  
20648 C C   . THR K 202 ? 3.7642 3.5404 3.9580 -0.5337 -1.6324 0.0112  202 THR J C   
20649 O O   . THR K 202 ? 3.8332 3.5293 4.0214 -0.5262 -1.6500 -0.0187 202 THR J O   
20650 C CB  . THR K 202 ? 3.7245 3.5313 3.8365 -0.5832 -1.6513 0.1080  202 THR J CB  
20651 O OG1 . THR K 202 ? 3.6584 3.5349 3.7799 -0.5974 -1.6376 0.1604  202 THR J OG1 
20652 C CG2 . THR K 202 ? 3.8070 3.5854 3.8008 -0.6114 -1.6739 0.1288  202 THR J CG2 
20653 N N   . VAL K 203 ? 3.6509 3.4557 3.8364 -0.5149 -1.5823 0.0002  203 VAL J N   
20654 C CA  . VAL K 203 ? 3.6598 3.4013 3.8305 -0.4925 -1.5691 -0.0519 203 VAL J CA  
20655 C C   . VAL K 203 ? 3.8104 3.5042 3.8468 -0.5109 -1.5614 -0.0300 203 VAL J C   
20656 O O   . VAL K 203 ? 3.8454 3.5886 3.8134 -0.5186 -1.5082 0.0217  203 VAL J O   
20657 C CB  . VAL K 203 ? 3.5514 3.3499 3.7911 -0.4448 -1.4766 -0.0785 203 VAL J CB  
20658 C CG1 . VAL K 203 ? 3.6088 3.3376 3.8428 -0.4220 -1.4712 -0.1365 203 VAL J CG1 
20659 C CG2 . VAL K 203 ? 3.4060 3.2591 3.7761 -0.4274 -1.4809 -0.0940 203 VAL J CG2 
20660 N N   . GLU K 204 ? 3.7559 3.3535 3.7540 -0.5179 -1.6148 -0.0688 204 GLU J N   
20661 C CA  . GLU K 204 ? 3.9278 3.4682 3.7990 -0.5355 -1.6168 -0.0543 204 GLU J CA  
20662 C C   . GLU K 204 ? 4.0475 3.5326 3.9077 -0.5074 -1.5901 -0.1074 204 GLU J C   
20663 O O   . GLU K 204 ? 4.0772 3.5076 3.9982 -0.4974 -1.6371 -0.1620 204 GLU J O   
20664 C CB  . GLU K 204 ? 4.0417 3.5068 3.8549 -0.5794 -1.7198 -0.0436 204 GLU J CB  
20665 C CG  . GLU K 204 ? 4.2603 3.6553 3.9467 -0.5945 -1.7261 -0.0381 204 GLU J CG  
20666 C CD  . GLU K 204 ? 4.4458 3.7686 4.0779 -0.6264 -1.7979 -0.0266 204 GLU J CD  
20667 O OE1 . GLU K 204 ? 4.4654 3.8054 4.1530 -0.6256 -1.7988 -0.0098 204 GLU J OE1 
20668 O OE2 . GLU K 204 ? 4.5866 3.8396 4.1234 -0.6400 -1.8202 -0.0317 204 GLU J OE2 
20669 N N   . LYS K 205 ? 3.8727 3.3722 3.6558 -0.4946 -1.5150 -0.0911 205 LYS J N   
20670 C CA  . LYS K 205 ? 3.9421 3.3873 3.6972 -0.4704 -1.4867 -0.1356 205 LYS J CA  
20671 C C   . LYS K 205 ? 4.1069 3.4991 3.7227 -0.4932 -1.4923 -0.1102 205 LYS J C   
20672 O O   . LYS K 205 ? 4.1574 3.5925 3.7016 -0.5094 -1.4600 -0.0533 205 LYS J O   
20673 C CB  . LYS K 205 ? 3.8720 3.3874 3.6699 -0.4272 -1.3799 -0.1445 205 LYS J CB  
20674 C CG  . LYS K 205 ? 3.7424 3.2946 3.6780 -0.3972 -1.3700 -0.1844 205 LYS J CG  
20675 C CD  . LYS K 205 ? 3.6453 3.2543 3.6116 -0.3541 -1.2654 -0.1975 205 LYS J CD  
20676 C CE  . LYS K 205 ? 3.5350 3.1706 3.6370 -0.3216 -1.2565 -0.2442 205 LYS J CE  
20677 N NZ  . LYS K 205 ? 3.5702 3.1189 3.7132 -0.3169 -1.3229 -0.3066 205 LYS J NZ  
20678 N N   . THR K 206 ? 4.0584 3.3575 3.6358 -0.4939 -1.5325 -0.1522 206 THR J N   
20679 C CA  . THR K 206 ? 4.2220 3.4586 3.6681 -0.5164 -1.5491 -0.1338 206 THR J CA  
20680 C C   . THR K 206 ? 4.2956 3.5110 3.6945 -0.4868 -1.4808 -0.1589 206 THR J C   
20681 O O   . THR K 206 ? 4.2165 3.4614 3.6861 -0.4493 -1.4246 -0.1931 206 THR J O   
20682 C CB  . THR K 206 ? 4.2797 3.4190 3.7044 -0.5475 -1.6603 -0.1562 206 THR J CB  
20683 O OG1 . THR K 206 ? 4.3021 3.3826 3.7895 -0.5262 -1.6876 -0.2239 206 THR J OG1 
20684 C CG2 . THR K 206 ? 4.2025 3.3646 3.6767 -0.5760 -1.7269 -0.1315 206 THR J CG2 
20685 N N   . VAL K 207 ? 4.1898 3.3514 3.4666 -0.5043 -1.4881 -0.1418 207 VAL J N   
20686 C CA  . VAL K 207 ? 4.2402 3.3720 3.4544 -0.4808 -1.4303 -0.1621 207 VAL J CA  
20687 C C   . VAL K 207 ? 4.3714 3.4117 3.4652 -0.5090 -1.4842 -0.1571 207 VAL J C   
20688 O O   . VAL K 207 ? 4.4282 3.4656 3.4509 -0.5434 -1.5180 -0.1099 207 VAL J O   
20689 C CB  . VAL K 207 ? 4.2107 3.4307 3.3965 -0.4600 -1.3204 -0.1225 207 VAL J CB  
20690 C CG1 . VAL K 207 ? 4.2476 3.5105 3.3576 -0.4915 -1.3168 -0.0506 207 VAL J CG1 
20691 C CG2 . VAL K 207 ? 4.2673 3.4527 3.3844 -0.4362 -1.2628 -0.1438 207 VAL J CG2 
20692 N N   . ALA K 208 ? 4.3344 3.3001 3.4050 -0.4939 -1.4911 -0.2057 208 ALA J N   
20693 C CA  . ALA K 208 ? 4.5466 3.4186 3.5069 -0.5171 -1.5423 -0.2087 208 ALA J CA  
20694 C C   . ALA K 208 ? 4.7058 3.5598 3.5927 -0.4924 -1.4715 -0.2196 208 ALA J C   
20695 O O   . ALA K 208 ? 4.6544 3.5261 3.6003 -0.4554 -1.4169 -0.2572 208 ALA J O   
20696 C CB  . ALA K 208 ? 4.4858 3.2665 3.4850 -0.5274 -1.6388 -0.2618 208 ALA J CB  
20697 N N   . PRO K 209 ? 4.5749 3.3943 3.3340 -0.5113 -1.4697 -0.1877 209 PRO J N   
20698 C CA  . PRO K 209 ? 4.7210 3.5184 3.4054 -0.4882 -1.4048 -0.1987 209 PRO J CA  
20699 C C   . PRO K 209 ? 4.8317 3.5405 3.5342 -0.4726 -1.4398 -0.2667 209 PRO J C   
20700 O O   . PRO K 209 ? 4.8267 3.4797 3.5792 -0.4851 -1.5223 -0.3014 209 PRO J O   
20701 C CB  . PRO K 209 ? 4.8656 3.6355 3.4104 -0.5186 -1.4162 -0.1490 209 PRO J CB  
20702 C CG  . PRO K 209 ? 4.7857 3.6008 3.3425 -0.5511 -1.4545 -0.0993 209 PRO J CG  
20703 C CD  . PRO K 209 ? 4.6333 3.4397 3.3096 -0.5535 -1.5201 -0.1359 209 PRO J CD  
20704 N N   . THR K 210 ? 4.6848 3.3804 3.3443 -0.4450 -1.3755 -0.2853 210 THR J N   
20705 C CA  . THR K 210 ? 4.7138 3.3275 3.3858 -0.4274 -1.3995 -0.3493 210 THR J CA  
20706 C C   . THR K 210 ? 4.8415 3.3781 3.3809 -0.4352 -1.4036 -0.3486 210 THR J C   
20707 O O   . THR K 210 ? 4.9024 3.4565 3.3408 -0.4491 -1.3737 -0.2986 210 THR J O   
20708 C CB  . THR K 210 ? 4.6250 3.2831 3.3832 -0.3816 -1.3229 -0.3867 210 THR J CB  
20709 O OG1 . THR K 210 ? 4.5060 3.2331 3.3897 -0.3735 -1.3213 -0.3896 210 THR J OG1 
20710 C CG2 . THR K 210 ? 4.6537 3.2257 3.4292 -0.3643 -1.3519 -0.4536 210 THR J CG2 
20711 N N   . GLN L 1   ? 2.1266 3.7618 2.4394 -1.3046 0.1919  -0.9302 1   GLN K N   
20712 C CA  . GLN L 1   ? 2.1247 3.7461 2.4284 -1.3072 0.1920  -0.9171 1   GLN K CA  
20713 C C   . GLN L 1   ? 2.1163 3.7290 2.4222 -1.3007 0.1675  -0.8949 1   GLN K C   
20714 O O   . GLN L 1   ? 2.1130 3.7437 2.4303 -1.2944 0.1542  -0.8974 1   GLN K O   
20715 C CB  . GLN L 1   ? 2.1294 3.7816 2.4357 -1.3114 0.2127  -0.9408 1   GLN K CB  
20716 C CG  . GLN L 1   ? 2.1272 3.8194 2.4492 -1.3061 0.2102  -0.9581 1   GLN K CG  
20717 C CD  . GLN L 1   ? 2.1678 3.8939 2.4950 -1.3104 0.2348  -0.9904 1   GLN K CD  
20718 O OE1 . GLN L 1   ? 2.2093 3.9397 2.5297 -1.3164 0.2516  -0.9992 1   GLN K OE1 
20719 N NE2 . GLN L 1   ? 2.1916 3.9422 2.5311 -1.3074 0.2371  -1.0088 1   GLN K NE2 
20720 N N   . VAL L 2   ? 2.1389 3.7239 2.4342 -1.3026 0.1612  -0.8736 2   VAL K N   
20721 C CA  . VAL L 2   ? 2.1327 3.7062 2.4271 -1.2981 0.1392  -0.8514 2   VAL K CA  
20722 C C   . VAL L 2   ? 2.1325 3.7149 2.4237 -1.3009 0.1441  -0.8510 2   VAL K C   
20723 O O   . VAL L 2   ? 2.1344 3.7008 2.4168 -1.3058 0.1537  -0.8463 2   VAL K O   
20724 C CB  . VAL L 2   ? 2.1300 3.6622 2.4148 -1.2973 0.1244  -0.8245 2   VAL K CB  
20725 C CG1 . VAL L 2   ? 2.1250 3.6458 2.4077 -1.2937 0.1027  -0.8023 2   VAL K CG1 
20726 C CG2 . VAL L 2   ? 2.1304 3.6533 2.4181 -1.2945 0.1188  -0.8244 2   VAL K CG2 
20727 N N   . HIS L 3   ? 2.3407 3.9481 2.6395 -1.2978 0.1370  -0.8558 3   HIS K N   
20728 C CA  . HIS L 3   ? 2.3361 3.9540 2.6319 -1.3005 0.1406  -0.8558 3   HIS K CA  
20729 C C   . HIS L 3   ? 2.3142 3.9221 2.6079 -1.2974 0.1174  -0.8343 3   HIS K C   
20730 O O   . HIS L 3   ? 2.3049 3.9213 2.6059 -1.2922 0.1017  -0.8326 3   HIS K O   
20731 C CB  . HIS L 3   ? 2.3942 4.0523 2.6993 -1.3011 0.1547  -0.8821 3   HIS K CB  
20732 C CG  . HIS L 3   ? 2.4384 4.1067 2.7397 -1.3045 0.1598  -0.8827 3   HIS K CG  
20733 N ND1 . HIS L 3   ? 2.4759 4.1308 2.7678 -1.3100 0.1725  -0.8804 3   HIS K ND1 
20734 C CD2 . HIS L 3   ? 2.4423 4.1324 2.7479 -1.3032 0.1535  -0.8855 3   HIS K CD2 
20735 C CE1 . HIS L 3   ? 2.4406 4.1092 2.7312 -1.3121 0.1744  -0.8820 3   HIS K CE1 
20736 N NE2 . HIS L 3   ? 2.4198 4.1098 2.7179 -1.3083 0.1633  -0.8849 3   HIS K NE2 
20737 N N   . LEU L 4   ? 2.2519 3.8420 2.5357 -1.3007 0.1151  -0.8186 4   LEU K N   
20738 C CA  . LEU L 4   ? 2.2508 3.8305 2.5300 -1.2995 0.0948  -0.7981 4   LEU K CA  
20739 C C   . LEU L 4   ? 2.2534 3.8494 2.5296 -1.3036 0.1010  -0.8019 4   LEU K C   
20740 O O   . LEU L 4   ? 2.2547 3.8515 2.5273 -1.3081 0.1178  -0.8089 4   LEU K O   
20741 C CB  . LEU L 4   ? 2.2486 3.7896 2.5177 -1.2999 0.0839  -0.7732 4   LEU K CB  
20742 C CG  . LEU L 4   ? 2.2463 3.7665 2.5163 -1.2963 0.0773  -0.7668 4   LEU K CG  
20743 C CD1 . LEU L 4   ? 2.2445 3.7270 2.5043 -1.2968 0.0660  -0.7417 4   LEU K CD1 
20744 C CD2 . LEU L 4   ? 2.2458 3.7770 2.5242 -1.2904 0.0619  -0.7686 4   LEU K CD2 
20745 N N   . GLN L 5   ? 2.2864 3.8948 2.5640 -1.3024 0.0872  -0.7976 5   GLN K N   
20746 C CA  . GLN L 5   ? 2.3100 3.9345 2.5841 -1.3068 0.0919  -0.8008 5   GLN K CA  
20747 C C   . GLN L 5   ? 2.3669 3.9777 2.6332 -1.3074 0.0703  -0.7787 5   GLN K C   
20748 O O   . GLN L 5   ? 2.3779 3.9891 2.6478 -1.3034 0.0523  -0.7731 5   GLN K O   
20749 C CB  . GLN L 5   ? 2.3687 4.0312 2.6535 -1.3059 0.1008  -0.8247 5   GLN K CB  
20750 C CG  . GLN L 5   ? 2.4695 4.1509 2.7510 -1.3105 0.1059  -0.8295 5   GLN K CG  
20751 C CD  . GLN L 5   ? 2.4578 4.1368 2.7331 -1.3161 0.1258  -0.8349 5   GLN K CD  
20752 O OE1 . GLN L 5   ? 2.4406 4.1112 2.7166 -1.3163 0.1392  -0.8418 5   GLN K OE1 
20753 N NE2 . GLN L 5   ? 2.5046 4.1909 2.7738 -1.3209 0.1276  -0.8326 5   GLN K NE2 
20754 N N   . GLU L 6   ? 2.4220 4.0206 2.6776 -1.3127 0.0719  -0.7671 6   GLU K N   
20755 C CA  . GLU L 6   ? 2.4629 4.0489 2.7086 -1.3153 0.0541  -0.7469 6   GLU K CA  
20756 C C   . GLU L 6   ? 2.5179 4.1292 2.7620 -1.3199 0.0572  -0.7548 6   GLU K C   
20757 O O   . GLU L 6   ? 2.5353 4.1668 2.7826 -1.3224 0.0757  -0.7720 6   GLU K O   
20758 C CB  . GLU L 6   ? 2.4393 3.9955 2.6742 -1.3185 0.0526  -0.7282 6   GLU K CB  
20759 C CG  . GLU L 6   ? 2.4038 3.9573 2.6392 -1.3211 0.0727  -0.7367 6   GLU K CG  
20760 C CD  . GLU L 6   ? 2.4055 3.9471 2.6468 -1.3171 0.0801  -0.7421 6   GLU K CD  
20761 O OE1 . GLU L 6   ? 2.4392 3.9902 2.6880 -1.3127 0.0782  -0.7510 6   GLU K OE1 
20762 O OE2 . GLU L 6   ? 2.3896 3.9121 2.6281 -1.3187 0.0872  -0.7376 6   GLU K OE2 
20763 N N   . SER L 7   ? 2.3911 4.0006 2.6294 -1.3212 0.0386  -0.7424 7   SER K N   
20764 C CA  . SER L 7   ? 2.4327 4.0650 2.6683 -1.3262 0.0397  -0.7488 7   SER K CA  
20765 C C   . SER L 7   ? 2.4896 4.1075 2.7115 -1.3310 0.0207  -0.7280 7   SER K C   
20766 O O   . SER L 7   ? 2.5062 4.1080 2.7261 -1.3279 0.0005  -0.7144 7   SER K O   
20767 C CB  . SER L 7   ? 2.3875 4.0484 2.6364 -1.3218 0.0384  -0.7671 7   SER K CB  
20768 O OG  . SER L 7   ? 2.4057 4.0573 2.6591 -1.3159 0.0173  -0.7593 7   SER K OG  
20769 N N   . GLY L 8   ? 2.3184 3.9420 2.5303 -1.3390 0.0276  -0.7261 8   GLY K N   
20770 C CA  . GLY L 8   ? 2.3748 3.9868 2.5715 -1.3456 0.0125  -0.7079 8   GLY K CA  
20771 C C   . GLY L 8   ? 2.4374 4.0704 2.6273 -1.3540 0.0199  -0.7145 8   GLY K C   
20772 O O   . GLY L 8   ? 2.5079 4.1668 2.7062 -1.3539 0.0351  -0.7341 8   GLY K O   
20773 N N   . PRO L 9   ? 2.4536 4.0755 2.6272 -1.3620 0.0093  -0.6983 9   PRO K N   
20774 C CA  . PRO L 9   ? 2.4642 4.1054 2.6294 -1.3712 0.0155  -0.7036 9   PRO K CA  
20775 C C   . PRO L 9   ? 2.4611 4.1120 2.6257 -1.3756 0.0383  -0.7136 9   PRO K C   
20776 O O   . PRO L 9   ? 2.4639 4.1404 2.6315 -1.3786 0.0505  -0.7295 9   PRO K O   
20777 C CB  . PRO L 9   ? 2.4777 4.1001 2.6237 -1.3791 -0.0027 -0.6818 9   PRO K CB  
20778 C CG  . PRO L 9   ? 2.4715 4.0637 2.6149 -1.3752 -0.0105 -0.6657 9   PRO K CG  
20779 C CD  . PRO L 9   ? 2.4581 4.0502 2.6193 -1.3635 -0.0092 -0.6748 9   PRO K CD  
20780 N N   . GLY L 10  ? 2.5928 4.2240 2.7545 -1.3757 0.0439  -0.7054 10  GLY K N   
20781 C CA  . GLY L 10  ? 2.5476 4.1851 2.7095 -1.3794 0.0632  -0.7143 10  GLY K CA  
20782 C C   . GLY L 10  ? 2.6076 4.2405 2.7537 -1.3900 0.0621  -0.7035 10  GLY K C   
20783 O O   . GLY L 10  ? 2.6085 4.2343 2.7540 -1.3922 0.0725  -0.7034 10  GLY K O   
20784 N N   . LEU L 11  ? 2.3873 4.0245 2.5207 -1.3970 0.0497  -0.6953 11  LEU K N   
20785 C CA  . LEU L 11  ? 2.4760 4.1097 2.5917 -1.4087 0.0478  -0.6848 11  LEU K CA  
20786 C C   . LEU L 11  ? 2.5548 4.1705 2.6563 -1.4123 0.0251  -0.6644 11  LEU K C   
20787 O O   . LEU L 11  ? 2.5845 4.2067 2.6858 -1.4112 0.0130  -0.6647 11  LEU K O   
20788 C CB  . LEU L 11  ? 2.5203 4.1819 2.6318 -1.4168 0.0588  -0.6983 11  LEU K CB  
20789 C CG  . LEU L 11  ? 2.6048 4.2648 2.6966 -1.4303 0.0574  -0.6885 11  LEU K CG  
20790 C CD1 . LEU L 11  ? 2.6289 4.2753 2.7200 -1.4317 0.0662  -0.6844 11  LEU K CD1 
20791 C CD2 . LEU L 11  ? 2.6432 4.3312 2.7309 -1.4383 0.0680  -0.7026 11  LEU K CD2 
20792 N N   . VAL L 12  ? 2.5303 4.1233 2.6200 -1.4165 0.0187  -0.6474 12  VAL K N   
20793 C CA  . VAL L 12  ? 2.6189 4.1918 2.6930 -1.4205 -0.0027 -0.6271 12  VAL K CA  
20794 C C   . VAL L 12  ? 2.7251 4.2929 2.7785 -1.4341 -0.0026 -0.6163 12  VAL K C   
20795 O O   . VAL L 12  ? 2.6887 4.2514 2.7423 -1.4361 0.0082  -0.6159 12  VAL K O   
20796 C CB  . VAL L 12  ? 2.5752 4.1210 2.6546 -1.4112 -0.0138 -0.6148 12  VAL K CB  
20797 C CG1 . VAL L 12  ? 2.6479 4.1725 2.7097 -1.4158 -0.0360 -0.5941 12  VAL K CG1 
20798 C CG2 . VAL L 12  ? 2.4564 4.0081 2.5558 -1.3985 -0.0131 -0.6264 12  VAL K CG2 
20799 N N   . LYS L 13  ? 2.6638 4.2328 2.6995 -1.4438 -0.0149 -0.6081 13  LYS K N   
20800 C CA  . LYS L 13  ? 2.7182 4.2829 2.7310 -1.4586 -0.0158 -0.5975 13  LYS K CA  
20801 C C   . LYS L 13  ? 2.7414 4.2769 2.7448 -1.4592 -0.0253 -0.5784 13  LYS K C   
20802 O O   . LYS L 13  ? 2.7376 4.2539 2.7467 -1.4499 -0.0378 -0.5695 13  LYS K O   
20803 C CB  . LYS L 13  ? 2.7417 4.3114 2.7369 -1.4686 -0.0291 -0.5922 13  LYS K CB  
20804 C CG  . LYS L 13  ? 2.6402 4.2375 2.6462 -1.4666 -0.0231 -0.6104 13  LYS K CG  
20805 C CD  . LYS L 13  ? 2.6186 4.2415 2.6310 -1.4701 0.0005  -0.6283 13  LYS K CD  
20806 C CE  . LYS L 13  ? 2.7076 4.3391 2.6976 -1.4873 0.0043  -0.6256 13  LYS K CE  
20807 N NZ  . LYS L 13  ? 2.7855 4.4424 2.7834 -1.4896 0.0272  -0.6446 13  LYS K NZ  
20808 N N   . PRO L 14  ? 2.5793 4.1115 2.5683 -1.4701 -0.0194 -0.5724 14  PRO K N   
20809 C CA  . PRO L 14  ? 2.6060 4.1111 2.5850 -1.4716 -0.0288 -0.5542 14  PRO K CA  
20810 C C   . PRO L 14  ? 2.7172 4.2017 2.6778 -1.4751 -0.0516 -0.5355 14  PRO K C   
20811 O O   . PRO L 14  ? 2.7690 4.2602 2.7166 -1.4824 -0.0601 -0.5342 14  PRO K O   
20812 C CB  . PRO L 14  ? 2.5782 4.0902 2.5440 -1.4850 -0.0174 -0.5546 14  PRO K CB  
20813 C CG  . PRO L 14  ? 2.5183 4.0591 2.4974 -1.4847 0.0021  -0.5762 14  PRO K CG  
20814 C CD  . PRO L 14  ? 2.5577 4.1117 2.5423 -1.4803 -0.0021 -0.5842 14  PRO K CD  
20815 N N   . SER L 15  ? 2.8007 4.2588 2.7602 -1.4698 -0.0620 -0.5210 15  SER K N   
20816 C CA  . SER L 15  ? 2.8533 4.2876 2.7955 -1.4720 -0.0844 -0.5021 15  SER K CA  
20817 C C   . SER L 15  ? 2.8374 4.2747 2.7863 -1.4648 -0.0976 -0.5056 15  SER K C   
20818 O O   . SER L 15  ? 2.8841 4.3119 2.8152 -1.4712 -0.1148 -0.4953 15  SER K O   
20819 C CB  . SER L 15  ? 2.9271 4.3566 2.8382 -1.4904 -0.0896 -0.4899 15  SER K CB  
20820 O OG  . SER L 15  ? 2.9324 4.3668 2.8393 -1.4982 -0.0747 -0.4915 15  SER K OG  
20821 N N   . GLU L 16  ? 2.7507 4.2008 2.7254 -1.4516 -0.0902 -0.5208 16  GLU K N   
20822 C CA  . GLU L 16  ? 2.7289 4.1840 2.7138 -1.4434 -0.1019 -0.5267 16  GLU K CA  
20823 C C   . GLU L 16  ? 2.7132 4.1540 2.7167 -1.4276 -0.1079 -0.5258 16  GLU K C   
20824 O O   . GLU L 16  ? 2.7170 4.1402 2.7222 -1.4240 -0.1057 -0.5176 16  GLU K O   
20825 C CB  . GLU L 16  ? 2.7080 4.1954 2.7056 -1.4433 -0.0877 -0.5476 16  GLU K CB  
20826 C CG  . GLU L 16  ? 2.7396 4.2363 2.7372 -1.4429 -0.1016 -0.5521 16  GLU K CG  
20827 C CD  . GLU L 16  ? 2.7209 4.2500 2.7319 -1.4423 -0.0863 -0.5733 16  GLU K CD  
20828 O OE1 . GLU L 16  ? 2.6765 4.2197 2.6958 -1.4423 -0.0648 -0.5842 16  GLU K OE1 
20829 O OE2 . GLU L 16  ? 2.7701 4.3101 2.7837 -1.4416 -0.0964 -0.5796 16  GLU K OE2 
20830 N N   . THR L 17  ? 2.7358 4.1845 2.7537 -1.4184 -0.1160 -0.5349 17  THR K N   
20831 C CA  . THR L 17  ? 2.6512 4.0889 2.6870 -1.4038 -0.1222 -0.5360 17  THR K CA  
20832 C C   . THR L 17  ? 2.5182 3.9800 2.5792 -1.3943 -0.1062 -0.5579 17  THR K C   
20833 O O   . THR L 17  ? 2.5246 4.0069 2.5936 -1.3928 -0.1074 -0.5709 17  THR K O   
20834 C CB  . THR L 17  ? 2.6705 4.0943 2.7018 -1.4002 -0.1481 -0.5278 17  THR K CB  
20835 O OG1 . THR L 17  ? 2.7923 4.1910 2.7982 -1.4091 -0.1628 -0.5068 17  THR K OG1 
20836 C CG2 . THR L 17  ? 2.7119 4.1262 2.7625 -1.3851 -0.1542 -0.5306 17  THR K CG2 
20837 N N   . LEU L 18  ? 2.4682 3.9267 2.5411 -1.3884 -0.0917 -0.5619 18  LEU K N   
20838 C CA  . LEU L 18  ? 2.4519 3.9295 2.5470 -1.3797 -0.0755 -0.5818 18  LEU K CA  
20839 C C   . LEU L 18  ? 2.4435 3.9169 2.5532 -1.3678 -0.0865 -0.5855 18  LEU K C   
20840 O O   . LEU L 18  ? 2.4412 3.8899 2.5486 -1.3631 -0.0997 -0.5721 18  LEU K O   
20841 C CB  . LEU L 18  ? 2.4397 3.9114 2.5405 -1.3781 -0.0581 -0.5837 18  LEU K CB  
20842 C CG  . LEU L 18  ? 2.4231 3.9060 2.5450 -1.3686 -0.0430 -0.6012 18  LEU K CG  
20843 C CD1 . LEU L 18  ? 2.4234 3.9388 2.5536 -1.3700 -0.0289 -0.6221 18  LEU K CD1 
20844 C CD2 . LEU L 18  ? 2.4139 3.8840 2.5392 -1.3674 -0.0303 -0.5995 18  LEU K CD2 
20845 N N   . SER L 19  ? 2.2073 3.7052 2.3322 -1.3629 -0.0812 -0.6041 19  SER K N   
20846 C CA  . SER L 19  ? 2.1996 3.6976 2.3404 -1.3515 -0.0900 -0.6108 19  SER K CA  
20847 C C   . SER L 19  ? 2.1850 3.7035 2.3448 -1.3455 -0.0689 -0.6318 19  SER K C   
20848 O O   . SER L 19  ? 2.1859 3.7305 2.3503 -1.3485 -0.0551 -0.6475 19  SER K O   
20849 C CB  . SER L 19  ? 2.2119 3.7193 2.3533 -1.3507 -0.1088 -0.6137 19  SER K CB  
20850 O OG  . SER L 19  ? 2.2055 3.7120 2.3627 -1.3394 -0.1192 -0.6201 19  SER K OG  
20851 N N   . LEU L 20  ? 2.3752 3.8814 2.5448 -1.3375 -0.0663 -0.6323 20  LEU K N   
20852 C CA  . LEU L 20  ? 2.3106 3.8326 2.4963 -1.3322 -0.0466 -0.6513 20  LEU K CA  
20853 C C   . LEU L 20  ? 2.2908 3.8138 2.4909 -1.3222 -0.0545 -0.6585 20  LEU K C   
20854 O O   . LEU L 20  ? 2.3033 3.8082 2.5009 -1.3185 -0.0750 -0.6461 20  LEU K O   
20855 C CB  . LEU L 20  ? 2.2934 3.7996 2.4770 -1.3330 -0.0321 -0.6470 20  LEU K CB  
20856 C CG  . LEU L 20  ? 2.3341 3.8395 2.5063 -1.3420 -0.0219 -0.6422 20  LEU K CG  
20857 C CD1 . LEU L 20  ? 2.3144 3.8013 2.4876 -1.3408 -0.0115 -0.6379 20  LEU K CD1 
20858 C CD2 . LEU L 20  ? 2.3305 3.8668 2.5064 -1.3462 -0.0060 -0.6606 20  LEU K CD2 
20859 N N   . THR L 21  ? 2.3623 3.9070 2.5774 -1.3181 -0.0380 -0.6797 21  THR K N   
20860 C CA  . THR L 21  ? 2.3224 3.8733 2.5525 -1.3093 -0.0420 -0.6907 21  THR K CA  
20861 C C   . THR L 21  ? 2.2714 3.8308 2.5116 -1.3067 -0.0192 -0.7067 21  THR K C   
20862 O O   . THR L 21  ? 2.2599 3.8378 2.5016 -1.3106 0.0002  -0.7202 21  THR K O   
20863 C CB  . THR L 21  ? 2.3286 3.9059 2.5682 -1.3068 -0.0503 -0.7043 21  THR K CB  
20864 O OG1 . THR L 21  ? 2.3712 3.9382 2.5998 -1.3099 -0.0728 -0.6890 21  THR K OG1 
20865 C CG2 . THR L 21  ? 2.3373 3.9204 2.5931 -1.2973 -0.0565 -0.7153 21  THR K CG2 
20866 N N   . CYS L 22  ? 2.5512 4.0958 2.7971 -1.3008 -0.0215 -0.7051 22  CYS K N   
20867 C CA  . CYS L 22  ? 2.5410 4.0899 2.7949 -1.2988 -0.0014 -0.7195 22  CYS K CA  
20868 C C   . CYS L 22  ? 2.5392 4.1075 2.8085 -1.2923 -0.0013 -0.7376 22  CYS K C   
20869 O O   . CYS L 22  ? 2.5390 4.0951 2.8126 -1.2867 -0.0145 -0.7325 22  CYS K O   
20870 C CB  . CYS L 22  ? 2.5352 4.0509 2.7822 -1.2983 -0.0029 -0.7034 22  CYS K CB  
20871 S SG  . CYS L 22  ? 2.5948 4.1101 2.8491 -1.2967 0.0190  -0.7186 22  CYS K SG  
20872 N N   . ASN L 23  ? 2.4714 4.0708 2.7494 -1.2929 0.0125  -0.7589 23  ASN K N   
20873 C CA  . ASN L 23  ? 2.4613 4.0838 2.7551 -1.2871 0.0148  -0.7791 23  ASN K CA  
20874 C C   . ASN L 23  ? 2.3903 4.0077 2.6883 -1.2856 0.0308  -0.7887 23  ASN K C   
20875 O O   . ASN L 23  ? 2.3565 3.9757 2.6513 -1.2899 0.0519  -0.7967 23  ASN K O   
20876 C CB  . ASN L 23  ? 2.5811 4.2364 2.8801 -1.2895 0.0235  -0.7960 23  ASN K CB  
20877 C CG  . ASN L 23  ? 2.6634 4.3410 2.9754 -1.2839 0.0093  -0.8068 23  ASN K CG  
20878 O OD1 . ASN L 23  ? 2.6404 4.3181 2.9627 -1.2772 -0.0009 -0.8108 23  ASN K OD1 
20879 N ND2 . ASN L 23  ? 2.9314 4.6265 3.2428 -1.2866 0.0060  -0.8102 23  ASN K ND2 
20880 N N   . VAL L 24  ? 2.4373 4.0470 2.7420 -1.2798 0.0197  -0.7874 24  VAL K N   
20881 C CA  . VAL L 24  ? 2.4016 4.0029 2.7088 -1.2787 0.0316  -0.7938 24  VAL K CA  
20882 C C   . VAL L 24  ? 2.4001 4.0330 2.7232 -1.2750 0.0411  -0.8206 24  VAL K C   
20883 O O   . VAL L 24  ? 2.4206 4.0696 2.7549 -1.2694 0.0266  -0.8268 24  VAL K O   
20884 C CB  . VAL L 24  ? 2.3970 3.9653 2.6993 -1.2752 0.0129  -0.7730 24  VAL K CB  
20885 C CG1 . VAL L 24  ? 2.3476 3.9062 2.6515 -1.2747 0.0247  -0.7790 24  VAL K CG1 
20886 C CG2 . VAL L 24  ? 2.4642 4.0027 2.7511 -1.2787 0.0027  -0.7469 24  VAL K CG2 
20887 N N   . SER L 25  ? 2.3966 4.0383 2.7205 -1.2784 0.0650  -0.8369 25  SER K N   
20888 C CA  . SER L 25  ? 2.4185 4.0894 2.7558 -1.2763 0.0784  -0.8638 25  SER K CA  
20889 C C   . SER L 25  ? 2.4063 4.0617 2.7391 -1.2791 0.0932  -0.8670 25  SER K C   
20890 O O   . SER L 25  ? 2.4644 4.1009 2.7851 -1.2848 0.1048  -0.8598 25  SER K O   
20891 C CB  . SER L 25  ? 2.5031 4.2075 2.8452 -1.2794 0.0966  -0.8856 25  SER K CB  
20892 O OG  . SER L 25  ? 2.5436 4.2615 2.8891 -1.2775 0.0826  -0.8822 25  SER K OG  
20893 N N   . GLY L 26  ? 2.3921 4.0548 2.7345 -1.2752 0.0919  -0.8778 26  GLY K N   
20894 C CA  . GLY L 26  ? 2.3937 4.0435 2.7321 -1.2781 0.1054  -0.8826 26  GLY K CA  
20895 C C   . GLY L 26  ? 2.3942 4.0147 2.7298 -1.2745 0.0878  -0.8642 26  GLY K C   
20896 O O   . GLY L 26  ? 2.3989 4.0116 2.7334 -1.2762 0.0969  -0.8700 26  GLY K O   
20897 N N   . THR L 27  ? 2.4315 4.0345 2.7650 -1.2701 0.0632  -0.8422 27  THR K N   
20898 C CA  . THR L 27  ? 2.4333 4.0074 2.7639 -1.2661 0.0441  -0.8234 27  THR K CA  
20899 C C   . THR L 27  ? 2.4395 4.0102 2.7729 -1.2603 0.0170  -0.8088 27  THR K C   
20900 O O   . THR L 27  ? 2.4432 4.0266 2.7766 -1.2612 0.0142  -0.8084 27  THR K O   
20901 C CB  . THR L 27  ? 2.4312 3.9670 2.7455 -1.2709 0.0470  -0.8030 27  THR K CB  
20902 O OG1 . THR L 27  ? 2.4300 3.9377 2.7415 -1.2667 0.0279  -0.7847 27  THR K OG1 
20903 C CG2 . THR L 27  ? 2.4359 3.9606 2.7400 -1.2742 0.0448  -0.7877 27  THR K CG2 
20904 N N   . LEU L 28  ? 2.4110 3.9634 2.7459 -1.2549 -0.0033 -0.7967 28  LEU K N   
20905 C CA  . LEU L 28  ? 2.4127 3.9572 2.7488 -1.2494 -0.0313 -0.7816 28  LEU K CA  
20906 C C   . LEU L 28  ? 2.4111 3.9195 2.7301 -1.2522 -0.0428 -0.7524 28  LEU K C   
20907 O O   . LEU L 28  ? 2.4080 3.8907 2.7164 -1.2557 -0.0357 -0.7407 28  LEU K O   
20908 C CB  . LEU L 28  ? 2.4148 3.9580 2.7616 -1.2412 -0.0507 -0.7837 28  LEU K CB  
20909 C CG  . LEU L 28  ? 2.4179 3.9976 2.7845 -1.2361 -0.0467 -0.8121 28  LEU K CG  
20910 C CD1 . LEU L 28  ? 2.4168 3.9977 2.7878 -1.2363 -0.0331 -0.8246 28  LEU K CD1 
20911 C CD2 . LEU L 28  ? 2.4234 4.0074 2.8000 -1.2272 -0.0767 -0.8098 28  LEU K CD2 
20912 N N   . VAL L 29  ? 2.6623 4.1690 2.9785 -1.2510 -0.0610 -0.7410 29  VAL K N   
20913 C CA  . VAL L 29  ? 2.6521 4.1276 2.9518 -1.2543 -0.0714 -0.7145 29  VAL K CA  
20914 C C   . VAL L 29  ? 2.6847 4.1294 2.9801 -1.2495 -0.0931 -0.6960 29  VAL K C   
20915 O O   . VAL L 29  ? 2.6771 4.0924 2.9586 -1.2518 -0.1022 -0.6733 29  VAL K O   
20916 C CB  . VAL L 29  ? 2.6364 4.1206 2.9322 -1.2561 -0.0822 -0.7089 29  VAL K CB  
20917 C CG1 . VAL L 29  ? 2.5800 4.0941 2.8793 -1.2610 -0.0605 -0.7267 29  VAL K CG1 
20918 C CG2 . VAL L 29  ? 2.6355 4.1280 2.9405 -1.2490 -0.1069 -0.7115 29  VAL K CG2 
20919 N N   . ARG L 30  ? 2.7081 4.1595 3.0154 -1.2429 -0.1016 -0.7062 30  ARG K N   
20920 C CA  . ARG L 30  ? 2.6252 4.0486 2.9296 -1.2377 -0.1228 -0.6906 30  ARG K CA  
20921 C C   . ARG L 30  ? 2.5850 3.9898 2.8854 -1.2393 -0.1100 -0.6879 30  ARG K C   
20922 O O   . ARG L 30  ? 2.6039 3.9776 2.8964 -1.2372 -0.1237 -0.6694 30  ARG K O   
20923 C CB  . ARG L 30  ? 2.6389 4.0780 2.9584 -1.2289 -0.1418 -0.7028 30  ARG K CB  
20924 C CG  . ARG L 30  ? 2.7303 4.1407 3.0473 -1.2224 -0.1670 -0.6878 30  ARG K CG  
20925 C CD  . ARG L 30  ? 2.8392 4.2584 3.1679 -1.2131 -0.1940 -0.6946 30  ARG K CD  
20926 N NE  . ARG L 30  ? 2.8686 4.3237 3.2176 -1.2082 -0.1881 -0.7230 30  ARG K NE  
20927 C CZ  . ARG L 30  ? 2.9362 4.4022 3.2972 -1.1995 -0.2113 -0.7320 30  ARG K CZ  
20928 N NH1 . ARG L 30  ? 3.0050 4.4462 3.3575 -1.1955 -0.2407 -0.7140 30  ARG K NH1 
20929 N NH2 . ARG L 30  ? 2.9365 4.4366 3.3168 -1.1946 -0.2063 -0.7589 30  ARG K NH2 
20930 N N   . ASP L 31  ? 2.7241 4.1472 3.0296 -1.2430 -0.0844 -0.7065 31  ASP K N   
20931 C CA  . ASP L 31  ? 2.7051 4.1125 3.0068 -1.2453 -0.0712 -0.7067 31  ASP K CA  
20932 C C   . ASP L 31  ? 2.6702 4.0572 2.9575 -1.2526 -0.0563 -0.6950 31  ASP K C   
20933 O O   . ASP L 31  ? 2.6409 4.0180 2.9248 -1.2558 -0.0417 -0.6984 31  ASP K O   
20934 C CB  . ASP L 31  ? 2.6924 4.1310 3.0070 -1.2457 -0.0518 -0.7356 31  ASP K CB  
20935 C CG  . ASP L 31  ? 2.6861 4.1465 3.0172 -1.2378 -0.0659 -0.7498 31  ASP K CG  
20936 O OD1 . ASP L 31  ? 2.7374 4.1992 3.0716 -1.2328 -0.0876 -0.7427 31  ASP K OD1 
20937 O OD2 . ASP L 31  ? 2.7048 4.1817 3.0457 -1.2369 -0.0553 -0.7692 31  ASP K OD2 
20938 N N   . ASN L 32  ? 2.4175 3.7983 2.6964 -1.2554 -0.0599 -0.6821 32  ASN K N   
20939 C CA  . ASN L 32  ? 2.4156 3.7787 2.6826 -1.2617 -0.0469 -0.6722 32  ASN K CA  
20940 C C   . ASN L 32  ? 2.4157 3.7578 2.6715 -1.2626 -0.0621 -0.6487 32  ASN K C   
20941 O O   . ASN L 32  ? 2.4184 3.7642 2.6746 -1.2597 -0.0799 -0.6422 32  ASN K O   
20942 C CB  . ASN L 32  ? 2.4162 3.8049 2.6860 -1.2672 -0.0224 -0.6914 32  ASN K CB  
20943 C CG  . ASN L 32  ? 2.4174 3.8229 2.6950 -1.2683 -0.0036 -0.7142 32  ASN K CG  
20944 O OD1 . ASN L 32  ? 2.4190 3.8541 2.7086 -1.2657 -0.0004 -0.7338 32  ASN K OD1 
20945 N ND2 . ASN L 32  ? 2.4178 3.8038 2.6882 -1.2723 0.0088  -0.7118 32  ASN K ND2 
20946 N N   . TYR L 33  ? 2.4559 3.7757 2.7014 -1.2668 -0.0550 -0.6364 33  TYR K N   
20947 C CA  . TYR L 33  ? 2.4761 3.7786 2.7106 -1.2691 -0.0649 -0.6164 33  TYR K CA  
20948 C C   . TYR L 33  ? 2.4800 3.8048 2.7147 -1.2743 -0.0506 -0.6263 33  TYR K C   
20949 O O   . TYR L 33  ? 2.4638 3.8062 2.7039 -1.2770 -0.0305 -0.6442 33  TYR K O   
20950 C CB  . TYR L 33  ? 2.4764 3.7443 2.7014 -1.2705 -0.0651 -0.5993 33  TYR K CB  
20951 C CG  . TYR L 33  ? 2.4762 3.7180 2.6984 -1.2656 -0.0819 -0.5854 33  TYR K CG  
20952 C CD1 . TYR L 33  ? 2.4682 3.7093 2.6964 -1.2630 -0.0775 -0.5952 33  TYR K CD1 
20953 C CD2 . TYR L 33  ? 2.5269 3.7453 2.7398 -1.2639 -0.1017 -0.5633 33  TYR K CD2 
20954 C CE1 . TYR L 33  ? 2.5157 3.7335 2.7416 -1.2585 -0.0924 -0.5833 33  TYR K CE1 
20955 C CE2 . TYR L 33  ? 2.5735 3.7679 2.7836 -1.2592 -0.1170 -0.5512 33  TYR K CE2 
20956 C CZ  . TYR L 33  ? 2.5574 3.7516 2.7745 -1.2563 -0.1124 -0.5613 33  TYR K CZ  
20957 O OH  . TYR L 33  ? 2.5700 3.7406 2.7843 -1.2516 -0.1273 -0.5499 33  TYR K OH  
20958 N N   . TRP L 34  ? 2.4638 3.7877 2.6918 -1.2763 -0.0605 -0.6148 34  TRP K N   
20959 C CA  . TRP L 34  ? 2.4719 3.8173 2.6994 -1.2815 -0.0485 -0.6234 34  TRP K CA  
20960 C C   . TRP L 34  ? 2.4990 3.8264 2.7144 -1.2860 -0.0525 -0.6053 34  TRP K C   
20961 O O   . TRP L 34  ? 2.5666 3.8769 2.7737 -1.2853 -0.0708 -0.5873 34  TRP K O   
20962 C CB  . TRP L 34  ? 2.4826 3.8559 2.7160 -1.2802 -0.0552 -0.6336 34  TRP K CB  
20963 C CG  . TRP L 34  ? 2.4591 3.8531 2.7061 -1.2756 -0.0510 -0.6533 34  TRP K CG  
20964 C CD1 . TRP L 34  ? 2.4592 3.8507 2.7122 -1.2694 -0.0670 -0.6528 34  TRP K CD1 
20965 C CD2 . TRP L 34  ? 2.4358 3.8547 2.6920 -1.2769 -0.0289 -0.6769 34  TRP K CD2 
20966 N NE1 . TRP L 34  ? 2.4381 3.8538 2.7045 -1.2667 -0.0564 -0.6752 34  TRP K NE1 
20967 C CE2 . TRP L 34  ? 2.4242 3.8570 2.6921 -1.2715 -0.0325 -0.6903 34  TRP K CE2 
20968 C CE3 . TRP L 34  ? 2.4271 3.8585 2.6828 -1.2821 -0.0068 -0.6888 34  TRP K CE3 
20969 C CZ2 . TRP L 34  ? 2.4062 3.8656 2.6846 -1.2717 -0.0137 -0.7150 34  TRP K CZ2 
20970 C CZ3 . TRP L 34  ? 2.4087 3.8648 2.6739 -1.2823 0.0113  -0.7128 34  TRP K CZ3 
20971 C CH2 . TRP L 34  ? 2.3992 3.8695 2.6754 -1.2774 0.0083  -0.7258 34  TRP K CH2 
20972 N N   . SER L 35  ? 2.3591 3.6902 2.5735 -1.2907 -0.0357 -0.6107 35  SER K N   
20973 C CA  . SER L 35  ? 2.3879 3.7041 2.5927 -1.2951 -0.0378 -0.5959 35  SER K CA  
20974 C C   . SER L 35  ? 2.4401 3.7811 2.6450 -1.3005 -0.0258 -0.6067 35  SER K C   
20975 O O   . SER L 35  ? 2.4619 3.8272 2.6747 -1.3011 -0.0105 -0.6265 35  SER K O   
20976 C CB  . SER L 35  ? 2.3250 3.6169 2.5288 -1.2954 -0.0305 -0.5900 35  SER K CB  
20977 O OG  . SER L 35  ? 2.2959 3.5643 2.4991 -1.2907 -0.0406 -0.5804 35  SER K OG  
20978 N N   . TRP L 36  ? 2.3880 3.7228 2.5834 -1.3049 -0.0323 -0.5938 36  TRP K N   
20979 C CA  . TRP L 36  ? 2.4100 3.7657 2.6039 -1.3109 -0.0217 -0.6019 36  TRP K CA  
20980 C C   . TRP L 36  ? 2.4262 3.7661 2.6163 -1.3145 -0.0155 -0.5942 36  TRP K C   
20981 O O   . TRP L 36  ? 2.4466 3.7611 2.6298 -1.3144 -0.0271 -0.5760 36  TRP K O   
20982 C CB  . TRP L 36  ? 2.4539 3.8196 2.6394 -1.3143 -0.0344 -0.5952 36  TRP K CB  
20983 C CG  . TRP L 36  ? 2.4453 3.8334 2.6368 -1.3115 -0.0387 -0.6068 36  TRP K CG  
20984 C CD1 . TRP L 36  ? 2.4403 3.8220 2.6341 -1.3060 -0.0545 -0.6025 36  TRP K CD1 
20985 C CD2 . TRP L 36  ? 2.4351 3.8556 2.6330 -1.3134 -0.0271 -0.6262 36  TRP K CD2 
20986 N NE1 . TRP L 36  ? 2.4328 3.8411 2.6346 -1.3043 -0.0546 -0.6177 36  TRP K NE1 
20987 C CE2 . TRP L 36  ? 2.4281 3.8607 2.6324 -1.3089 -0.0376 -0.6323 36  TRP K CE2 
20988 C CE3 . TRP L 36  ? 2.4341 3.8747 2.6333 -1.3184 -0.0094 -0.6392 36  TRP K CE3 
20989 C CZ2 . TRP L 36  ? 2.4196 3.8837 2.6317 -1.3091 -0.0310 -0.6508 36  TRP K CZ2 
20990 C CZ3 . TRP L 36  ? 2.4252 3.8967 2.6311 -1.3188 -0.0023 -0.6572 36  TRP K CZ3 
20991 C CH2 . TRP L 36  ? 2.4176 3.9008 2.6300 -1.3142 -0.0131 -0.6628 36  TRP K CH2 
20992 N N   . ILE L 37  ? 2.4407 3.7956 2.6361 -1.3175 0.0023  -0.6086 37  ILE K N   
20993 C CA  . ILE L 37  ? 2.4564 3.7994 2.6514 -1.3206 0.0093  -0.6047 37  ILE K CA  
20994 C C   . ILE L 37  ? 2.5284 3.8951 2.7225 -1.3267 0.0198  -0.6147 37  ILE K C   
20995 O O   . ILE L 37  ? 2.5429 3.9344 2.7423 -1.3274 0.0323  -0.6329 37  ILE K O   
20996 C CB  . ILE L 37  ? 2.4201 3.7525 2.6241 -1.3179 0.0211  -0.6129 37  ILE K CB  
20997 C CG1 . ILE L 37  ? 2.3939 3.7044 2.5983 -1.3123 0.0117  -0.6045 37  ILE K CG1 
20998 C CG2 . ILE L 37  ? 2.4402 3.7579 2.6456 -1.3204 0.0253  -0.6077 37  ILE K CG2 
20999 C CD1 . ILE L 37  ? 2.3598 3.6861 2.5698 -1.3091 0.0169  -0.6193 37  ILE K CD1 
21000 N N   . ARG L 38  ? 2.4038 3.7633 2.5909 -1.3314 0.0152  -0.6035 38  ARG K N   
21001 C CA  . ARG L 38  ? 2.4382 3.8188 2.6238 -1.3379 0.0252  -0.6123 38  ARG K CA  
21002 C C   . ARG L 38  ? 2.4114 3.7833 2.6033 -1.3394 0.0350  -0.6146 38  ARG K C   
21003 O O   . ARG L 38  ? 2.3776 3.7242 2.5720 -1.3366 0.0296  -0.6039 38  ARG K O   
21004 C CB  . ARG L 38  ? 2.4923 3.8757 2.6646 -1.3438 0.0136  -0.5999 38  ARG K CB  
21005 C CG  . ARG L 38  ? 2.5339 3.8917 2.6989 -1.3457 0.0023  -0.5804 38  ARG K CG  
21006 C CD  . ARG L 38  ? 2.6134 3.9770 2.7634 -1.3533 -0.0067 -0.5706 38  ARG K CD  
21007 N NE  . ARG L 38  ? 2.6781 4.0213 2.8208 -1.3567 -0.0145 -0.5545 38  ARG K NE  
21008 C CZ  . ARG L 38  ? 2.7499 4.0946 2.8779 -1.3648 -0.0216 -0.5446 38  ARG K CZ  
21009 N NH1 . ARG L 38  ? 2.8051 4.1695 2.9239 -1.3702 -0.0226 -0.5485 38  ARG K NH1 
21010 N NH2 . ARG L 38  ? 2.8133 4.1401 2.9357 -1.3678 -0.0276 -0.5312 38  ARG K NH2 
21011 N N   . GLN L 39  ? 2.4486 3.8419 2.6440 -1.3436 0.0492  -0.6292 39  GLN K N   
21012 C CA  . GLN L 39  ? 2.4232 3.8105 2.6268 -1.3449 0.0589  -0.6338 39  GLN K CA  
21013 C C   . GLN L 39  ? 2.5120 3.9214 2.7149 -1.3515 0.0687  -0.6435 39  GLN K C   
21014 O O   . GLN L 39  ? 2.5103 3.9440 2.7155 -1.3530 0.0809  -0.6604 39  GLN K O   
21015 C CB  . GLN L 39  ? 2.3634 3.7489 2.5785 -1.3405 0.0709  -0.6475 39  GLN K CB  
21016 C CG  . GLN L 39  ? 2.3739 3.7508 2.5989 -1.3413 0.0794  -0.6521 39  GLN K CG  
21017 C CD  . GLN L 39  ? 2.3503 3.7245 2.5848 -1.3382 0.0914  -0.6657 39  GLN K CD  
21018 O OE1 . GLN L 39  ? 2.2996 3.6820 2.5332 -1.3359 0.0955  -0.6739 39  GLN K OE1 
21019 N NE2 . GLN L 39  ? 2.4069 3.7697 2.6510 -1.3385 0.0970  -0.6686 39  GLN K NE2 
21020 N N   . PRO L 40  ? 2.4190 3.8213 2.6184 -1.3560 0.0639  -0.6338 40  PRO K N   
21021 C CA  . PRO L 40  ? 2.4717 3.8945 2.6710 -1.3628 0.0739  -0.6436 40  PRO K CA  
21022 C C   . PRO L 40  ? 2.4464 3.8760 2.6602 -1.3613 0.0899  -0.6610 40  PRO K C   
21023 O O   . PRO L 40  ? 2.4173 3.8318 2.6412 -1.3559 0.0924  -0.6632 40  PRO K O   
21024 C CB  . PRO L 40  ? 2.5192 3.9281 2.7130 -1.3671 0.0640  -0.6282 40  PRO K CB  
21025 C CG  . PRO L 40  ? 2.4990 3.8861 2.6842 -1.3639 0.0471  -0.6094 40  PRO K CG  
21026 C CD  . PRO L 40  ? 2.4202 3.7973 2.6138 -1.3556 0.0483  -0.6131 40  PRO K CD  
21027 N N   . LEU L 41  ? 2.2592 3.7118 2.4735 -1.3669 0.1009  -0.6737 41  LEU K N   
21028 C CA  . LEU L 41  ? 2.2585 3.7210 2.4858 -1.3665 0.1168  -0.6918 41  LEU K CA  
21029 C C   . LEU L 41  ? 2.2576 3.7012 2.4972 -1.3653 0.1162  -0.6884 41  LEU K C   
21030 O O   . LEU L 41  ? 2.2627 3.7066 2.5020 -1.3698 0.1133  -0.6834 41  LEU K O   
21031 C CB  . LEU L 41  ? 2.2657 3.7578 2.4890 -1.3731 0.1274  -0.7052 41  LEU K CB  
21032 C CG  . LEU L 41  ? 2.2673 3.7805 2.4804 -1.3745 0.1287  -0.7108 41  LEU K CG  
21033 C CD1 . LEU L 41  ? 2.2752 3.8167 2.4845 -1.3815 0.1395  -0.7241 41  LEU K CD1 
21034 C CD2 . LEU L 41  ? 2.2604 3.7746 2.4800 -1.3682 0.1351  -0.7212 41  LEU K CD2 
21035 N N   . GLY L 42  ? 2.2894 3.7170 2.5402 -1.3596 0.1189  -0.6915 42  GLY K N   
21036 C CA  . GLY L 42  ? 2.3001 3.7092 2.5649 -1.3579 0.1183  -0.6895 42  GLY K CA  
21037 C C   . GLY L 42  ? 2.3057 3.6867 2.5698 -1.3552 0.1022  -0.6692 42  GLY K C   
21038 O O   . GLY L 42  ? 2.3319 3.6995 2.6068 -1.3551 0.0989  -0.6650 42  GLY K O   
21039 N N   . LYS L 43  ? 2.4263 3.7980 2.6789 -1.3529 0.0920  -0.6570 43  LYS K N   
21040 C CA  . LYS L 43  ? 2.4413 3.7861 2.6912 -1.3501 0.0762  -0.6372 43  LYS K CA  
21041 C C   . LYS L 43  ? 2.3459 3.6747 2.5939 -1.3441 0.0719  -0.6328 43  LYS K C   
21042 O O   . LYS L 43  ? 2.2898 3.6303 2.5375 -1.3427 0.0809  -0.6449 43  LYS K O   
21043 C CB  . LYS L 43  ? 2.4550 3.8040 2.6901 -1.3547 0.0655  -0.6240 43  LYS K CB  
21044 C CG  . LYS L 43  ? 2.5837 3.9462 2.8203 -1.3614 0.0693  -0.6273 43  LYS K CG  
21045 C CD  . LYS L 43  ? 2.6047 3.9491 2.8564 -1.3599 0.0666  -0.6237 43  LYS K CD  
21046 C CE  . LYS L 43  ? 2.6866 4.0030 2.9349 -1.3570 0.0502  -0.6033 43  LYS K CE  
21047 N NZ  . LYS L 43  ? 2.6004 3.9000 2.8651 -1.3554 0.0471  -0.6003 43  LYS K NZ  
21048 N N   . GLN L 44  ? 2.4501 3.7522 2.6971 -1.3408 0.0583  -0.6158 44  GLN K N   
21049 C CA  . GLN L 44  ? 2.3168 3.6004 2.5617 -1.3353 0.0525  -0.6096 44  GLN K CA  
21050 C C   . GLN L 44  ? 2.3164 3.6060 2.5470 -1.3348 0.0446  -0.6026 44  GLN K C   
21051 O O   . GLN L 44  ? 2.3493 3.6455 2.5698 -1.3383 0.0371  -0.5941 44  GLN K O   
21052 C CB  . GLN L 44  ? 2.3187 3.5705 2.5692 -1.3320 0.0409  -0.5945 44  GLN K CB  
21053 C CG  . GLN L 44  ? 2.4125 3.6563 2.6554 -1.3341 0.0271  -0.5774 44  GLN K CG  
21054 C CD  . GLN L 44  ? 2.4778 3.6955 2.7307 -1.3320 0.0188  -0.5667 44  GLN K CD  
21055 O OE1 . GLN L 44  ? 2.4622 3.6722 2.7297 -1.3302 0.0247  -0.5741 44  GLN K OE1 
21056 N NE2 . GLN L 44  ? 2.5800 3.7853 2.8254 -1.3328 0.0054  -0.5501 44  GLN K NE2 
21057 N N   . PRO L 45  ? 2.4740 3.7619 2.7037 -1.3309 0.0466  -0.6071 45  PRO K N   
21058 C CA  . PRO L 45  ? 2.4550 3.7494 2.6740 -1.3296 0.0392  -0.6025 45  PRO K CA  
21059 C C   . PRO L 45  ? 2.4968 3.7713 2.7065 -1.3284 0.0207  -0.5812 45  PRO K C   
21060 O O   . PRO L 45  ? 2.5324 3.7805 2.7446 -1.3256 0.0127  -0.5692 45  PRO K O   
21061 C CB  . PRO L 45  ? 2.3963 3.6871 2.6196 -1.3253 0.0452  -0.6114 45  PRO K CB  
21062 C CG  . PRO L 45  ? 2.3788 3.6740 2.6127 -1.3266 0.0607  -0.6266 45  PRO K CG  
21063 C CD  . PRO L 45  ? 2.4173 3.6998 2.6565 -1.3283 0.0573  -0.6188 45  PRO K CD  
21064 N N   . GLU L 46  ? 2.4569 3.7440 2.6557 -1.3308 0.0136  -0.5765 46  GLU K N   
21065 C CA  . GLU L 46  ? 2.5129 3.7831 2.7007 -1.3304 -0.0042 -0.5568 46  GLU K CA  
21066 C C   . GLU L 46  ? 2.4705 3.7414 2.6532 -1.3265 -0.0122 -0.5547 46  GLU K C   
21067 O O   . GLU L 46  ? 2.4400 3.7342 2.6208 -1.3279 -0.0084 -0.5648 46  GLU K O   
21068 C CB  . GLU L 46  ? 2.5975 3.8780 2.7748 -1.3375 -0.0087 -0.5505 46  GLU K CB  
21069 C CG  . GLU L 46  ? 2.6944 3.9555 2.8590 -1.3377 -0.0271 -0.5297 46  GLU K CG  
21070 C CD  . GLU L 46  ? 2.8331 4.1025 2.9848 -1.3460 -0.0318 -0.5226 46  GLU K CD  
21071 O OE1 . GLU L 46  ? 2.8503 4.1364 3.0047 -1.3515 -0.0209 -0.5320 46  GLU K OE1 
21072 O OE2 . GLU L 46  ? 2.9122 4.1710 3.0503 -1.3475 -0.0463 -0.5077 46  GLU K OE2 
21073 N N   . TRP L 47  ? 2.5411 3.7867 2.7225 -1.3216 -0.0234 -0.5421 47  TRP K N   
21074 C CA  . TRP L 47  ? 2.5347 3.7777 2.7124 -1.3173 -0.0328 -0.5390 47  TRP K CA  
21075 C C   . TRP L 47  ? 2.6030 3.8505 2.7680 -1.3202 -0.0466 -0.5283 47  TRP K C   
21076 O O   . TRP L 47  ? 2.6746 3.9070 2.8304 -1.3230 -0.0569 -0.5126 47  TRP K O   
21077 C CB  . TRP L 47  ? 2.5257 3.7387 2.7048 -1.3117 -0.0411 -0.5278 47  TRP K CB  
21078 C CG  . TRP L 47  ? 2.5376 3.7492 2.7172 -1.3065 -0.0467 -0.5295 47  TRP K CG  
21079 C CD1 . TRP L 47  ? 2.5162 3.7513 2.6975 -1.3059 -0.0442 -0.5415 47  TRP K CD1 
21080 C CD2 . TRP L 47  ? 2.5105 3.6965 2.6899 -1.3012 -0.0557 -0.5197 47  TRP K CD2 
21081 N NE1 . TRP L 47  ? 2.4915 3.7178 2.6744 -1.3004 -0.0512 -0.5403 47  TRP K NE1 
21082 C CE2 . TRP L 47  ? 2.4910 3.6871 2.6721 -1.2977 -0.0580 -0.5269 47  TRP K CE2 
21083 C CE3 . TRP L 47  ? 2.4417 3.5974 2.6202 -1.2991 -0.0621 -0.5060 47  TRP K CE3 
21084 C CZ2 . TRP L 47  ? 2.4458 3.6233 2.6273 -1.2925 -0.0661 -0.5211 47  TRP K CZ2 
21085 C CZ3 . TRP L 47  ? 2.3829 3.5192 2.5607 -1.2939 -0.0702 -0.4996 47  TRP K CZ3 
21086 C CH2 . TRP L 47  ? 2.4003 3.5477 2.5794 -1.2908 -0.0719 -0.5072 47  TRP K CH2 
21087 N N   . ILE L 48  ? 2.3423 3.6101 2.5067 -1.3199 -0.0472 -0.5369 48  ILE K N   
21088 C CA  . ILE L 48  ? 2.3501 3.6224 2.5024 -1.3231 -0.0609 -0.5277 48  ILE K CA  
21089 C C   . ILE L 48  ? 2.3496 3.6021 2.4970 -1.3180 -0.0790 -0.5143 48  ILE K C   
21090 O O   . ILE L 48  ? 2.3563 3.5948 2.4909 -1.3205 -0.0937 -0.4979 48  ILE K O   
21091 C CB  . ILE L 48  ? 2.3532 3.6576 2.5081 -1.3254 -0.0540 -0.5438 48  ILE K CB  
21092 C CG1 . ILE L 48  ? 2.3537 3.6779 2.5136 -1.3301 -0.0353 -0.5582 48  ILE K CG1 
21093 C CG2 . ILE L 48  ? 2.3634 3.6719 2.5053 -1.3298 -0.0685 -0.5345 48  ILE K CG2 
21094 C CD1 . ILE L 48  ? 2.3566 3.7124 2.5194 -1.3322 -0.0276 -0.5748 48  ILE K CD1 
21095 N N   . GLY L 49  ? 2.4784 3.7295 2.6352 -1.3113 -0.0782 -0.5214 49  GLY K N   
21096 C CA  . GLY L 49  ? 2.4709 3.7042 2.6249 -1.3058 -0.0947 -0.5109 49  GLY K CA  
21097 C C   . GLY L 49  ? 2.4216 3.6680 2.5876 -1.3000 -0.0906 -0.5262 49  GLY K C   
21098 O O   . GLY L 49  ? 2.4005 3.6725 2.5750 -1.3009 -0.0767 -0.5446 49  GLY K O   
21099 N N   . TYR L 50  ? 2.5517 3.7806 2.7184 -1.2941 -0.1026 -0.5191 50  TYR K N   
21100 C CA  . TYR L 50  ? 2.5665 3.8064 2.7446 -1.2885 -0.1000 -0.5332 50  TYR K CA  
21101 C C   . TYR L 50  ? 2.6287 3.8704 2.8056 -1.2848 -0.1190 -0.5297 50  TYR K C   
21102 O O   . TYR L 50  ? 2.6893 3.9107 2.8554 -1.2846 -0.1365 -0.5118 50  TYR K O   
21103 C CB  . TYR L 50  ? 2.5363 3.7555 2.7185 -1.2846 -0.0959 -0.5313 50  TYR K CB  
21104 C CG  . TYR L 50  ? 2.5954 3.7813 2.7688 -1.2819 -0.1127 -0.5101 50  TYR K CG  
21105 C CD1 . TYR L 50  ? 2.5678 3.7324 2.7328 -1.2848 -0.1142 -0.4950 50  TYR K CD1 
21106 C CD2 . TYR L 50  ? 2.6045 3.7807 2.7787 -1.2761 -0.1270 -0.5061 50  TYR K CD2 
21107 C CE1 . TYR L 50  ? 2.5974 3.7321 2.7541 -1.2823 -0.1290 -0.4760 50  TYR K CE1 
21108 C CE2 . TYR L 50  ? 2.5899 3.7355 2.7555 -1.2735 -0.1420 -0.4870 50  TYR K CE2 
21109 C CZ  . TYR L 50  ? 2.6066 3.7315 2.7630 -1.2767 -0.1427 -0.4718 50  TYR K CZ  
21110 O OH  . TYR L 50  ? 2.6374 3.7322 2.7848 -1.2742 -0.1573 -0.4531 50  TYR K OH  
21111 N N   . VAL L 51  ? 2.7031 3.9693 2.8915 -1.2818 -0.1155 -0.5476 51  VAL K N   
21112 C CA  . VAL L 51  ? 2.6938 3.9658 2.8851 -1.2772 -0.1333 -0.5487 51  VAL K CA  
21113 C C   . VAL L 51  ? 2.6235 3.9029 2.8289 -1.2705 -0.1309 -0.5629 51  VAL K C   
21114 O O   . VAL L 51  ? 2.5262 3.8217 2.7408 -1.2709 -0.1118 -0.5797 51  VAL K O   
21115 C CB  . VAL L 51  ? 2.7189 4.0180 2.9110 -1.2807 -0.1341 -0.5578 51  VAL K CB  
21116 C CG1 . VAL L 51  ? 2.6625 3.9922 2.8660 -1.2824 -0.1115 -0.5805 51  VAL K CG1 
21117 C CG2 . VAL L 51  ? 2.7599 4.0636 2.9555 -1.2757 -0.1551 -0.5589 51  VAL K CG2 
21118 N N   . HIS L 52  ? 2.6093 3.8763 2.8156 -1.2646 -0.1503 -0.5564 52  HIS K N   
21119 C CA  . HIS L 52  ? 2.5795 3.8529 2.7990 -1.2580 -0.1508 -0.5694 52  HIS K CA  
21120 C C   . HIS L 52  ? 2.6125 3.8847 2.8347 -1.2520 -0.1755 -0.5670 52  HIS K C   
21121 O O   . HIS L 52  ? 2.6963 3.9550 2.9073 -1.2531 -0.1930 -0.5516 52  HIS K O   
21122 C CB  . HIS L 52  ? 2.5559 3.8048 2.7735 -1.2564 -0.1460 -0.5626 52  HIS K CB  
21123 C CG  . HIS L 52  ? 2.5281 3.7866 2.7588 -1.2513 -0.1420 -0.5783 52  HIS K CG  
21124 N ND1 . HIS L 52  ? 2.5279 3.8112 2.7688 -1.2530 -0.1206 -0.6000 52  HIS K ND1 
21125 C CD2 . HIS L 52  ? 2.5046 3.7519 2.7393 -1.2449 -0.1564 -0.5763 52  HIS K CD2 
21126 C CE1 . HIS L 52  ? 2.5063 3.7940 2.7567 -1.2484 -0.1212 -0.6109 52  HIS K CE1 
21127 N NE2 . HIS L 52  ? 2.4925 3.7588 2.7400 -1.2432 -0.1430 -0.5970 52  HIS K NE2 
21128 N N   . ASP L 53  ? 2.5182 3.8049 2.7551 -1.2458 -0.1772 -0.5831 53  ASP K N   
21129 C CA  . ASP L 53  ? 2.5747 3.8605 2.8166 -1.2387 -0.2019 -0.5832 53  ASP K CA  
21130 C C   . ASP L 53  ? 2.6120 3.8614 2.8438 -1.2353 -0.2202 -0.5627 53  ASP K C   
21131 O O   . ASP L 53  ? 2.6002 3.8269 2.8222 -1.2382 -0.2130 -0.5492 53  ASP K O   
21132 C CB  . ASP L 53  ? 2.5630 3.8744 2.8244 -1.2328 -0.1981 -0.6072 53  ASP K CB  
21133 C CG  . ASP L 53  ? 2.6181 3.9406 2.8880 -1.2259 -0.2219 -0.6140 53  ASP K CG  
21134 O OD1 . ASP L 53  ? 2.6298 3.9297 2.8900 -1.2234 -0.2461 -0.5976 53  ASP K OD1 
21135 O OD2 . ASP L 53  ? 2.5897 3.9429 2.8756 -1.2227 -0.2169 -0.6364 53  ASP K OD2 
21136 N N   . SER L 54  ? 2.5157 3.7592 2.7499 -1.2285 -0.2451 -0.5609 54  SER K N   
21137 C CA  . SER L 54  ? 2.5188 3.7289 2.7437 -1.2242 -0.2653 -0.5428 54  SER K CA  
21138 C C   . SER L 54  ? 2.5221 3.7055 2.7255 -1.2303 -0.2703 -0.5184 54  SER K C   
21139 O O   . SER L 54  ? 2.5217 3.6754 2.7150 -1.2287 -0.2793 -0.5018 54  SER K O   
21140 C CB  . SER L 54  ? 2.5100 3.7089 2.7405 -1.2208 -0.2572 -0.5449 54  SER K CB  
21141 O OG  . SER L 54  ? 2.5015 3.6909 2.7245 -1.2274 -0.2363 -0.5378 54  SER K OG  
21142 N N   . GLY L 55  ? 2.6995 3.8937 2.8954 -1.2375 -0.2640 -0.5162 55  GLY K N   
21143 C CA  . GLY L 55  ? 2.7487 3.9210 2.9238 -1.2441 -0.2689 -0.4946 55  GLY K CA  
21144 C C   . GLY L 55  ? 2.7529 3.9127 2.9202 -1.2499 -0.2501 -0.4848 55  GLY K C   
21145 O O   . GLY L 55  ? 2.8380 3.9808 2.9883 -1.2557 -0.2531 -0.4675 55  GLY K O   
21146 N N   . ASP L 56  ? 2.7452 3.9128 2.9238 -1.2488 -0.2311 -0.4960 56  ASP K N   
21147 C CA  . ASP L 56  ? 2.7091 3.8639 2.8817 -1.2535 -0.2145 -0.4884 56  ASP K CA  
21148 C C   . ASP L 56  ? 2.6790 3.8510 2.8484 -1.2614 -0.1988 -0.4923 56  ASP K C   
21149 O O   . ASP L 56  ? 2.6010 3.7972 2.7815 -1.2627 -0.1807 -0.5101 56  ASP K O   
21150 C CB  . ASP L 56  ? 2.6042 3.7612 2.7889 -1.2501 -0.2002 -0.5003 56  ASP K CB  
21151 C CG  . ASP L 56  ? 2.5966 3.7365 2.7754 -1.2540 -0.1857 -0.4924 56  ASP K CG  
21152 O OD1 . ASP L 56  ? 2.6180 3.7354 2.7833 -1.2566 -0.1924 -0.4735 56  ASP K OD1 
21153 O OD2 . ASP L 56  ? 2.5509 3.6991 2.7384 -1.2543 -0.1681 -0.5053 56  ASP K OD2 
21154 N N   . THR L 57  ? 2.7577 3.9181 2.9115 -1.2670 -0.2050 -0.4764 57  THR K N   
21155 C CA  . THR L 57  ? 2.6755 3.8516 2.8252 -1.2749 -0.1915 -0.4794 57  THR K CA  
21156 C C   . THR L 57  ? 2.6862 3.8402 2.8194 -1.2807 -0.1930 -0.4601 57  THR K C   
21157 O O   . THR L 57  ? 2.7271 3.8619 2.8465 -1.2815 -0.2104 -0.4435 57  THR K O   
21158 C CB  . THR L 57  ? 2.6943 3.8921 2.8430 -1.2774 -0.1990 -0.4861 57  THR K CB  
21159 O OG1 . THR L 57  ? 2.7262 3.9458 2.8916 -1.2715 -0.1987 -0.5051 57  THR K OG1 
21160 C CG2 . THR L 57  ? 2.6372 3.8526 2.7817 -1.2860 -0.1841 -0.4902 57  THR K CG2 
21161 N N   . ASN L 58  ? 2.6277 3.7843 2.7627 -1.2847 -0.1752 -0.4627 58  ASN K N   
21162 C CA  . ASN L 58  ? 2.6738 3.8130 2.7961 -1.2902 -0.1746 -0.4472 58  ASN K CA  
21163 C C   . ASN L 58  ? 2.6739 3.8347 2.7972 -1.2974 -0.1585 -0.4563 58  ASN K C   
21164 O O   . ASN L 58  ? 2.6126 3.7965 2.7482 -1.2969 -0.1438 -0.4745 58  ASN K O   
21165 C CB  . ASN L 58  ? 2.5966 3.7113 2.7210 -1.2868 -0.1710 -0.4398 58  ASN K CB  
21166 C CG  . ASN L 58  ? 2.6772 3.7709 2.7884 -1.2913 -0.1748 -0.4220 58  ASN K CG  
21167 O OD1 . ASN L 58  ? 2.7942 3.8870 2.8918 -1.2967 -0.1836 -0.4121 58  ASN K OD1 
21168 N ND2 . ASN L 58  ? 2.7355 3.8122 2.8507 -1.2895 -0.1684 -0.4183 58  ASN K ND2 
21169 N N   . TYR L 59  ? 2.6224 3.7761 2.7321 -1.3043 -0.1611 -0.4441 59  TYR K N   
21170 C CA  . TYR L 59  ? 2.6044 3.7776 2.7131 -1.3119 -0.1476 -0.4514 59  TYR K CA  
21171 C C   . TYR L 59  ? 2.5370 3.6969 2.6445 -1.3148 -0.1394 -0.4447 59  TYR K C   
21172 O O   . TYR L 59  ? 2.5592 3.6938 2.6652 -1.3113 -0.1450 -0.4332 59  TYR K O   
21173 C CB  . TYR L 59  ? 2.6494 3.8318 2.7434 -1.3193 -0.1568 -0.4460 59  TYR K CB  
21174 C CG  . TYR L 59  ? 2.6574 3.8557 2.7548 -1.3167 -0.1651 -0.4546 59  TYR K CG  
21175 C CD1 . TYR L 59  ? 2.6168 3.8349 2.7318 -1.3111 -0.1554 -0.4736 59  TYR K CD1 
21176 C CD2 . TYR L 59  ? 2.7516 3.9458 2.8344 -1.3203 -0.1824 -0.4448 59  TYR K CD2 
21177 C CE1 . TYR L 59  ? 2.6359 3.8700 2.7561 -1.3083 -0.1633 -0.4830 59  TYR K CE1 
21178 C CE2 . TYR L 59  ? 2.7860 3.9944 2.8736 -1.3174 -0.1915 -0.4537 59  TYR K CE2 
21179 C CZ  . TYR L 59  ? 2.7402 3.9692 2.8476 -1.3110 -0.1820 -0.4731 59  TYR K CZ  
21180 O OH  . TYR L 59  ? 2.8226 4.0668 2.9365 -1.3075 -0.1918 -0.4831 59  TYR K OH  
21181 N N   . ASN L 60  ? 2.4016 3.5795 2.5102 -1.3212 -0.1263 -0.4529 60  ASN K N   
21182 C CA  . ASN L 60  ? 2.4204 3.5900 2.5296 -1.3246 -0.1185 -0.4491 60  ASN K CA  
21183 C C   . ASN L 60  ? 2.4967 3.6528 2.5882 -1.3312 -0.1298 -0.4314 60  ASN K C   
21184 O O   . ASN L 60  ? 2.5617 3.7306 2.6412 -1.3383 -0.1331 -0.4301 60  ASN K O   
21185 C CB  . ASN L 60  ? 2.4134 3.6089 2.5312 -1.3288 -0.1002 -0.4661 60  ASN K CB  
21186 C CG  . ASN L 60  ? 2.4185 3.6060 2.5430 -1.3302 -0.0908 -0.4662 60  ASN K CG  
21187 O OD1 . ASN L 60  ? 2.4460 3.6111 2.5658 -1.3303 -0.0987 -0.4520 60  ASN K OD1 
21188 N ND2 . ASN L 60  ? 2.3935 3.5994 2.5301 -1.3310 -0.0741 -0.4831 60  ASN K ND2 
21189 N N   . PRO L 61  ? 2.6154 3.7456 2.7037 -1.3295 -0.1363 -0.4175 61  PRO K N   
21190 C CA  . PRO L 61  ? 2.7255 3.8424 2.7959 -1.3363 -0.1467 -0.4006 61  PRO K CA  
21191 C C   . PRO L 61  ? 2.8117 3.9475 2.8755 -1.3468 -0.1386 -0.4046 61  PRO K C   
21192 O O   . PRO L 61  ? 2.8935 4.0258 2.9384 -1.3547 -0.1473 -0.3931 61  PRO K O   
21193 C CB  . PRO L 61  ? 2.6673 3.7585 2.7427 -1.3320 -0.1488 -0.3911 61  PRO K CB  
21194 C CG  . PRO L 61  ? 2.5021 3.5852 2.5906 -1.3220 -0.1482 -0.3964 61  PRO K CG  
21195 C CD  . PRO L 61  ? 2.4876 3.5982 2.5875 -1.3213 -0.1355 -0.4162 61  PRO K CD  
21196 N N   . SER L 62  ? 2.6264 3.7817 2.7043 -1.3477 -0.1220 -0.4206 62  SER K N   
21197 C CA  . SER L 62  ? 2.6348 3.8096 2.7076 -1.3577 -0.1132 -0.4262 62  SER K CA  
21198 C C   . SER L 62  ? 2.6835 3.8805 2.7463 -1.3634 -0.1134 -0.4321 62  SER K C   
21199 O O   . SER L 62  ? 2.7435 3.9514 2.7933 -1.3737 -0.1121 -0.4305 62  SER K O   
21200 C CB  . SER L 62  ? 2.5088 3.6962 2.6009 -1.3561 -0.0958 -0.4420 62  SER K CB  
21201 O OG  . SER L 62  ? 2.4377 3.6375 2.5433 -1.3498 -0.0873 -0.4569 62  SER K OG  
21202 N N   . LEU L 63  ? 2.5136 3.7178 2.5824 -1.3573 -0.1151 -0.4395 63  LEU K N   
21203 C CA  . LEU L 63  ? 2.5323 3.7574 2.5945 -1.3615 -0.1165 -0.4462 63  LEU K CA  
21204 C C   . LEU L 63  ? 2.5325 3.7453 2.5859 -1.3579 -0.1347 -0.4363 63  LEU K C   
21205 O O   . LEU L 63  ? 2.5196 3.7475 2.5760 -1.3562 -0.1370 -0.4450 63  LEU K O   
21206 C CB  . LEU L 63  ? 2.5060 3.7566 2.5854 -1.3580 -0.1007 -0.4677 63  LEU K CB  
21207 C CG  . LEU L 63  ? 2.5014 3.7619 2.5918 -1.3600 -0.0829 -0.4785 63  LEU K CG  
21208 C CD1 . LEU L 63  ? 2.4931 3.7767 2.5995 -1.3562 -0.0676 -0.4996 63  LEU K CD1 
21209 C CD2 . LEU L 63  ? 2.5516 3.8216 2.6292 -1.3716 -0.0799 -0.4758 63  LEU K CD2 
21210 N N   . LYS L 64  ? 2.6720 3.8572 2.7155 -1.3564 -0.1483 -0.4187 64  LYS K N   
21211 C CA  . LYS L 64  ? 2.6720 3.8417 2.7083 -1.3518 -0.1666 -0.4088 64  LYS K CA  
21212 C C   . LYS L 64  ? 2.7333 3.9127 2.7542 -1.3587 -0.1769 -0.4066 64  LYS K C   
21213 O O   . LYS L 64  ? 2.7076 3.8919 2.7330 -1.3536 -0.1857 -0.4115 64  LYS K O   
21214 C CB  . LYS L 64  ? 2.7023 3.8406 2.7269 -1.3510 -0.1788 -0.3891 64  LYS K CB  
21215 C CG  . LYS L 64  ? 2.6353 3.7542 2.6703 -1.3394 -0.1853 -0.3858 64  LYS K CG  
21216 C CD  . LYS L 64  ? 2.6761 3.7646 2.6970 -1.3400 -0.1973 -0.3655 64  LYS K CD  
21217 C CE  . LYS L 64  ? 2.6489 3.7173 2.6673 -1.3319 -0.2138 -0.3571 64  LYS K CE  
21218 N NZ  . LYS L 64  ? 2.6894 3.7277 2.6929 -1.3325 -0.2254 -0.3371 64  LYS K NZ  
21219 N N   . SER L 65  ? 2.7075 3.8898 2.7104 -1.3707 -0.1766 -0.3998 65  SER K N   
21220 C CA  . SER L 65  ? 2.8256 4.0120 2.8095 -1.3791 -0.1883 -0.3946 65  SER K CA  
21221 C C   . SER L 65  ? 2.8786 4.0958 2.8674 -1.3837 -0.1785 -0.4110 65  SER K C   
21222 O O   . SER L 65  ? 2.9771 4.1999 2.9478 -1.3942 -0.1843 -0.4070 65  SER K O   
21223 C CB  . SER L 65  ? 2.9688 4.1409 2.9270 -1.3913 -0.1938 -0.3776 65  SER K CB  
21224 O OG  . SER L 65  ? 3.1046 4.2806 3.0422 -1.4013 -0.2041 -0.3728 65  SER K OG  
21225 N N   . ARG L 66  ? 2.6955 3.9324 2.7070 -1.3769 -0.1638 -0.4291 66  ARG K N   
21226 C CA  . ARG L 66  ? 2.7028 3.9695 2.7190 -1.3810 -0.1541 -0.4452 66  ARG K CA  
21227 C C   . ARG L 66  ? 2.6183 3.9007 2.6561 -1.3705 -0.1507 -0.4619 66  ARG K C   
21228 O O   . ARG L 66  ? 2.6241 3.9285 2.6640 -1.3729 -0.1489 -0.4733 66  ARG K O   
21229 C CB  . ARG L 66  ? 2.7088 3.9922 2.7285 -1.3873 -0.1336 -0.4544 66  ARG K CB  
21230 C CG  . ARG L 66  ? 2.7881 4.0622 2.7891 -1.3987 -0.1331 -0.4420 66  ARG K CG  
21231 C CD  . ARG L 66  ? 2.8029 4.1008 2.8085 -1.4055 -0.1137 -0.4554 66  ARG K CD  
21232 N NE  . ARG L 66  ? 2.7152 4.0219 2.7449 -1.3964 -0.0982 -0.4703 66  ARG K NE  
21233 C CZ  . ARG L 66  ? 2.7135 4.0446 2.7530 -1.3986 -0.0809 -0.4872 66  ARG K CZ  
21234 N NH1 . ARG L 66  ? 2.7941 4.1438 2.8218 -1.4095 -0.0768 -0.4914 66  ARG K NH1 
21235 N NH2 . ARG L 66  ? 2.6408 3.9770 2.7009 -1.3905 -0.0679 -0.4998 66  ARG K NH2 
21236 N N   . VAL L 67  ? 2.9717 4.2439 3.0249 -1.3594 -0.1499 -0.4642 67  VAL K N   
21237 C CA  . VAL L 67  ? 2.8521 4.1401 2.9260 -1.3500 -0.1445 -0.4813 67  VAL K CA  
21238 C C   . VAL L 67  ? 2.8324 4.1095 2.9081 -1.3425 -0.1641 -0.4773 67  VAL K C   
21239 O O   . VAL L 67  ? 2.8451 4.0963 2.9098 -1.3414 -0.1798 -0.4606 67  VAL K O   
21240 C CB  . VAL L 67  ? 2.7180 4.0040 2.8081 -1.3435 -0.1286 -0.4891 67  VAL K CB  
21241 C CG1 . VAL L 67  ? 2.6448 3.9012 2.7348 -1.3368 -0.1389 -0.4756 67  VAL K CG1 
21242 C CG2 . VAL L 67  ? 2.5897 3.8994 2.6990 -1.3374 -0.1166 -0.5104 67  VAL K CG2 
21243 N N   . HIS L 68  ? 2.8886 4.1864 2.9787 -1.3372 -0.1633 -0.4935 68  HIS K N   
21244 C CA  . HIS L 68  ? 2.8493 4.1423 2.9462 -1.3287 -0.1807 -0.4949 68  HIS K CA  
21245 C C   . HIS L 68  ? 2.7524 4.0684 2.8725 -1.3208 -0.1685 -0.5167 68  HIS K C   
21246 O O   . HIS L 68  ? 2.6882 4.0308 2.8149 -1.3239 -0.1546 -0.5318 68  HIS K O   
21247 C CB  . HIS L 68  ? 2.9011 4.1968 2.9869 -1.3326 -0.1998 -0.4914 68  HIS K CB  
21248 C CG  . HIS L 68  ? 3.0153 4.2879 3.0756 -1.3412 -0.2136 -0.4701 68  HIS K CG  
21249 N ND1 . HIS L 68  ? 3.0624 4.3265 3.1086 -1.3501 -0.2036 -0.4592 68  HIS K ND1 
21250 C CD2 . HIS L 68  ? 3.0808 4.3365 3.1265 -1.3424 -0.2372 -0.4583 68  HIS K CD2 
21251 C CE1 . HIS L 68  ? 3.1018 4.3458 3.1250 -1.3571 -0.2192 -0.4415 68  HIS K CE1 
21252 N NE2 . HIS L 68  ? 3.1189 4.3566 3.1406 -1.3528 -0.2398 -0.4402 68  HIS K NE2 
21253 N N   . LEU L 69  ? 2.8007 4.1066 2.9322 -1.3112 -0.1731 -0.5185 69  LEU K N   
21254 C CA  . LEU L 69  ? 2.7301 4.0557 2.8825 -1.3039 -0.1619 -0.5386 69  LEU K CA  
21255 C C   . LEU L 69  ? 2.7199 4.0469 2.8816 -1.2956 -0.1802 -0.5438 69  LEU K C   
21256 O O   . LEU L 69  ? 2.7532 4.0588 2.9062 -1.2934 -0.2018 -0.5299 69  LEU K O   
21257 C CB  . LEU L 69  ? 2.6785 3.9930 2.8380 -1.3002 -0.1477 -0.5394 69  LEU K CB  
21258 C CG  . LEU L 69  ? 2.6720 3.9875 2.8279 -1.3063 -0.1277 -0.5396 69  LEU K CG  
21259 C CD1 . LEU L 69  ? 2.6251 3.9268 2.7886 -1.3016 -0.1176 -0.5405 69  LEU K CD1 
21260 C CD2 . LEU L 69  ? 2.6489 3.9970 2.8118 -1.3101 -0.1108 -0.5585 69  LEU K CD2 
21261 N N   . SER L 70  ? 2.7580 4.1112 2.9377 -1.2908 -0.1714 -0.5650 70  SER K N   
21262 C CA  . SER L 70  ? 2.7055 4.0648 2.8975 -1.2822 -0.1874 -0.5740 70  SER K CA  
21263 C C   . SER L 70  ? 2.6193 4.0041 2.8315 -1.2772 -0.1699 -0.5972 70  SER K C   
21264 O O   . SER L 70  ? 2.5803 3.9820 2.7957 -1.2813 -0.1468 -0.6077 70  SER K O   
21265 C CB  . SER L 70  ? 2.7624 4.1319 2.9506 -1.2839 -0.2050 -0.5754 70  SER K CB  
21266 O OG  . SER L 70  ? 2.7131 4.1113 2.9046 -1.2894 -0.1897 -0.5890 70  SER K OG  
21267 N N   . LEU L 71  ? 2.7060 4.0935 2.9313 -1.2684 -0.1813 -0.6056 71  LEU K N   
21268 C CA  . LEU L 71  ? 2.6577 4.0695 2.9020 -1.2633 -0.1666 -0.6284 71  LEU K CA  
21269 C C   . LEU L 71  ? 2.6665 4.0988 2.9244 -1.2569 -0.1821 -0.6432 71  LEU K C   
21270 O O   . LEU L 71  ? 2.6896 4.1069 2.9476 -1.2508 -0.2069 -0.6362 71  LEU K O   
21271 C CB  . LEU L 71  ? 2.6268 4.0210 2.8752 -1.2584 -0.1638 -0.6258 71  LEU K CB  
21272 C CG  . LEU L 71  ? 2.6130 3.9863 2.8513 -1.2631 -0.1485 -0.6140 71  LEU K CG  
21273 C CD1 . LEU L 71  ? 2.6151 3.9615 2.8526 -1.2576 -0.1590 -0.6035 71  LEU K CD1 
21274 C CD2 . LEU L 71  ? 2.5731 3.9665 2.8189 -1.2659 -0.1203 -0.6315 71  LEU K CD2 
21275 N N   . ASP L 72  ? 2.7957 4.2615 3.0650 -1.2576 -0.1686 -0.6639 72  ASP K N   
21276 C CA  . ASP L 72  ? 2.8044 4.2925 3.0886 -1.2509 -0.1825 -0.6804 72  ASP K CA  
21277 C C   . ASP L 72  ? 2.7600 4.2652 3.0631 -1.2440 -0.1716 -0.7005 72  ASP K C   
21278 O O   . ASP L 72  ? 2.7286 4.2589 3.0401 -1.2463 -0.1468 -0.7184 72  ASP K O   
21279 C CB  . ASP L 72  ? 2.8204 4.3357 3.1061 -1.2555 -0.1767 -0.6915 72  ASP K CB  
21280 C CG  . ASP L 72  ? 2.8475 4.3763 3.1435 -1.2488 -0.2004 -0.7016 72  ASP K CG  
21281 O OD1 . ASP L 72  ? 2.8820 4.4106 3.1907 -1.2393 -0.2142 -0.7092 72  ASP K OD1 
21282 O OD2 . ASP L 72  ? 2.8862 4.4250 3.1772 -1.2529 -0.2064 -0.7021 72  ASP K OD2 
21283 N N   . LYS L 73  ? 2.7038 4.1954 3.0127 -1.2360 -0.1899 -0.6983 73  LYS K N   
21284 C CA  . LYS L 73  ? 2.6693 4.1757 2.9951 -1.2299 -0.1805 -0.7169 73  LYS K CA  
21285 C C   . LYS L 73  ? 2.6678 4.2110 3.0129 -1.2244 -0.1824 -0.7426 73  LYS K C   
21286 O O   . LYS L 73  ? 2.6402 4.2054 3.0001 -1.2212 -0.1676 -0.7633 73  LYS K O   
21287 C CB  . LYS L 73  ? 2.6755 4.1552 3.0010 -1.2231 -0.2001 -0.7062 73  LYS K CB  
21288 C CG  . LYS L 73  ? 2.6972 4.1403 3.0049 -1.2276 -0.1988 -0.6815 73  LYS K CG  
21289 C CD  . LYS L 73  ? 2.7259 4.1443 3.0342 -1.2203 -0.2188 -0.6726 73  LYS K CD  
21290 C CE  . LYS L 73  ? 2.7527 4.1629 3.0613 -1.2134 -0.2525 -0.6678 73  LYS K CE  
21291 N NZ  . LYS L 73  ? 2.7286 4.1140 3.0378 -1.2056 -0.2726 -0.6599 73  LYS K NZ  
21292 N N   . SER L 74  ? 2.8270 4.3770 3.1713 -1.2235 -0.2003 -0.7421 74  SER K N   
21293 C CA  . SER L 74  ? 2.8451 4.4291 3.2074 -1.2178 -0.2052 -0.7659 74  SER K CA  
21294 C C   . SER L 74  ? 2.8248 4.4407 3.1912 -1.2243 -0.1764 -0.7821 74  SER K C   
21295 O O   . SER L 74  ? 2.8100 4.4591 3.1941 -1.2205 -0.1651 -0.8074 74  SER K O   
21296 C CB  . SER L 74  ? 2.8458 4.4207 3.2038 -1.2142 -0.2383 -0.7581 74  SER K CB  
21297 O OG  . SER L 74  ? 2.8585 4.4220 3.1980 -1.2238 -0.2366 -0.7416 74  SER K OG  
21298 N N   . LYS L 75  ? 2.6714 4.2777 3.0214 -1.2340 -0.1642 -0.7685 75  LYS K N   
21299 C CA  . LYS L 75  ? 2.6539 4.2867 3.0051 -1.2406 -0.1376 -0.7818 75  LYS K CA  
21300 C C   . LYS L 75  ? 2.6174 4.2470 2.9642 -1.2458 -0.1080 -0.7833 75  LYS K C   
21301 O O   . LYS L 75  ? 2.6013 4.2517 2.9489 -1.2510 -0.0840 -0.7959 75  LYS K O   
21302 C CB  . LYS L 75  ? 2.6864 4.3125 3.0220 -1.2483 -0.1430 -0.7677 75  LYS K CB  
21303 C CG  . LYS L 75  ? 2.7311 4.3593 3.0679 -1.2449 -0.1719 -0.7661 75  LYS K CG  
21304 C CD  . LYS L 75  ? 2.7667 4.3885 3.0858 -1.2545 -0.1728 -0.7525 75  LYS K CD  
21305 C CE  . LYS L 75  ? 2.8192 4.4402 3.1366 -1.2523 -0.2024 -0.7501 75  LYS K CE  
21306 N NZ  . LYS L 75  ? 2.8595 4.4744 3.1581 -1.2630 -0.2021 -0.7370 75  LYS K NZ  
21307 N N   . ASN L 76  ? 2.6498 4.2527 2.9915 -1.2444 -0.1104 -0.7709 76  ASN K N   
21308 C CA  . ASN L 76  ? 2.5700 4.1647 2.9066 -1.2488 -0.0858 -0.7709 76  ASN K CA  
21309 C C   . ASN L 76  ? 2.5459 4.1347 2.8676 -1.2580 -0.0697 -0.7619 76  ASN K C   
21310 O O   . ASN L 76  ? 2.5137 4.1216 2.8375 -1.2622 -0.0451 -0.7768 76  ASN K O   
21311 C CB  . ASN L 76  ? 2.5475 4.1720 2.9002 -1.2464 -0.0652 -0.7988 76  ASN K CB  
21312 C CG  . ASN L 76  ? 2.5033 4.1146 2.8506 -1.2499 -0.0444 -0.7986 76  ASN K CG  
21313 O OD1 . ASN L 76  ? 2.4684 4.0627 2.8168 -1.2464 -0.0508 -0.7936 76  ASN K OD1 
21314 N ND2 . ASN L 76  ? 2.4819 4.0997 2.8227 -1.2569 -0.0203 -0.8042 76  ASN K ND2 
21315 N N   . LEU L 77  ? 2.5674 4.1294 2.8737 -1.2613 -0.0843 -0.7377 77  LEU K N   
21316 C CA  . LEU L 77  ? 2.5469 4.1017 2.8388 -1.2698 -0.0715 -0.7278 77  LEU K CA  
21317 C C   . LEU L 77  ? 2.5577 4.0753 2.8329 -1.2723 -0.0860 -0.6999 77  LEU K C   
21318 O O   . LEU L 77  ? 2.5898 4.0882 2.8636 -1.2676 -0.1080 -0.6877 77  LEU K O   
21319 C CB  . LEU L 77  ? 2.5968 4.1753 2.8885 -1.2737 -0.0708 -0.7351 77  LEU K CB  
21320 C CG  . LEU L 77  ? 2.6137 4.1941 2.9057 -1.2712 -0.0974 -0.7299 77  LEU K CG  
21321 C CD1 . LEU L 77  ? 2.6022 4.1532 2.8747 -1.2765 -0.1133 -0.7035 77  LEU K CD1 
21322 C CD2 . LEU L 77  ? 2.6063 4.2209 2.9062 -1.2728 -0.0910 -0.7481 77  LEU K CD2 
21323 N N   . VAL L 78  ? 2.4072 3.9151 2.6700 -1.2795 -0.0732 -0.6908 78  VAL K N   
21324 C CA  . VAL L 78  ? 2.4086 3.8838 2.6549 -1.2830 -0.0831 -0.6657 78  VAL K CA  
21325 C C   . VAL L 78  ? 2.4168 3.8969 2.6518 -1.2902 -0.0863 -0.6585 78  VAL K C   
21326 O O   . VAL L 78  ? 2.4170 3.9199 2.6539 -1.2945 -0.0699 -0.6714 78  VAL K O   
21327 C CB  . VAL L 78  ? 2.4005 3.8587 2.6421 -1.2854 -0.0662 -0.6612 78  VAL K CB  
21328 C CG1 . VAL L 78  ? 2.4019 3.8257 2.6283 -1.2877 -0.0784 -0.6355 78  VAL K CG1 
21329 C CG2 . VAL L 78  ? 2.3937 3.8526 2.6465 -1.2799 -0.0585 -0.6727 78  VAL K CG2 
21330 N N   . SER L 79  ? 2.3970 3.8556 2.6193 -1.2919 -0.1068 -0.6385 79  SER K N   
21331 C CA  . SER L 79  ? 2.4980 3.9598 2.7073 -1.2998 -0.1112 -0.6307 79  SER K CA  
21332 C C   . SER L 79  ? 2.5414 3.9771 2.7337 -1.3060 -0.1098 -0.6105 79  SER K C   
21333 O O   . SER L 79  ? 2.4914 3.9031 2.6814 -1.3032 -0.1120 -0.5996 79  SER K O   
21334 C CB  . SER L 79  ? 2.5338 3.9942 2.7406 -1.2980 -0.1371 -0.6256 79  SER K CB  
21335 O OG  . SER L 79  ? 2.6686 4.1288 2.8599 -1.3069 -0.1420 -0.6163 79  SER K OG  
21336 N N   . LEU L 80  ? 2.5383 3.9795 2.7186 -1.3148 -0.1062 -0.6060 80  LEU K N   
21337 C CA  . LEU L 80  ? 2.5652 3.9849 2.7295 -1.3215 -0.1046 -0.5884 80  LEU K CA  
21338 C C   . LEU L 80  ? 2.6910 4.1131 2.8390 -1.3308 -0.1128 -0.5795 80  LEU K C   
21339 O O   . LEU L 80  ? 2.7469 4.1934 2.8971 -1.3342 -0.1085 -0.5914 80  LEU K O   
21340 C CB  . LEU L 80  ? 2.5190 3.9447 2.6876 -1.3235 -0.0801 -0.5968 80  LEU K CB  
21341 C CG  . LEU L 80  ? 2.5279 3.9355 2.6835 -1.3299 -0.0755 -0.5826 80  LEU K CG  
21342 C CD1 . LEU L 80  ? 2.5011 3.8988 2.6647 -1.3263 -0.0612 -0.5859 80  LEU K CD1 
21343 C CD2 . LEU L 80  ? 2.6537 4.0796 2.8023 -1.3390 -0.0651 -0.5875 80  LEU K CD2 
21344 N N   . ARG L 81  ? 2.5242 3.9206 2.6551 -1.3354 -0.1247 -0.5586 81  ARG K N   
21345 C CA  . ARG L 81  ? 2.6705 4.0657 2.7825 -1.3459 -0.1325 -0.5483 81  ARG K CA  
21346 C C   . ARG L 81  ? 2.6910 4.0677 2.7878 -1.3531 -0.1277 -0.5329 81  ARG K C   
21347 O O   . ARG L 81  ? 2.6372 3.9892 2.7316 -1.3495 -0.1333 -0.5204 81  ARG K O   
21348 C CB  . ARG L 81  ? 2.7102 4.0936 2.8137 -1.3450 -0.1587 -0.5384 81  ARG K CB  
21349 C CG  . ARG L 81  ? 2.6698 4.0759 2.7868 -1.3400 -0.1648 -0.5549 81  ARG K CG  
21350 C CD  . ARG L 81  ? 2.7343 4.1260 2.8428 -1.3387 -0.1930 -0.5452 81  ARG K CD  
21351 N NE  . ARG L 81  ? 2.8237 4.2051 2.9074 -1.3510 -0.2011 -0.5304 81  ARG K NE  
21352 C CZ  . ARG L 81  ? 2.8819 4.2347 2.9464 -1.3554 -0.2120 -0.5098 81  ARG K CZ  
21353 N NH1 . ARG L 81  ? 2.9174 4.2631 2.9582 -1.3679 -0.2178 -0.4977 81  ARG K NH1 
21354 N NH2 . ARG L 81  ? 2.9195 4.2507 2.9875 -1.3479 -0.2168 -0.5013 81  ARG K NH2 
21355 N N   . LEU L 82  ? 2.4958 3.8851 2.5829 -1.3633 -0.1171 -0.5345 82  LEU K N   
21356 C CA  . LEU L 82  ? 2.4997 3.8760 2.5730 -1.3713 -0.1114 -0.5225 82  LEU K CA  
21357 C C   . LEU L 82  ? 2.5196 3.8995 2.5716 -1.3843 -0.1174 -0.5147 82  LEU K C   
21358 O O   . LEU L 82  ? 2.5246 3.9283 2.5764 -1.3905 -0.1066 -0.5262 82  LEU K O   
21359 C CB  . LEU L 82  ? 2.4884 3.8776 2.5731 -1.3710 -0.0880 -0.5354 82  LEU K CB  
21360 C CG  . LEU L 82  ? 2.4909 3.8694 2.5663 -1.3779 -0.0806 -0.5265 82  LEU K CG  
21361 C CD1 . LEU L 82  ? 2.4882 3.8351 2.5585 -1.3745 -0.0921 -0.5086 82  LEU K CD1 
21362 C CD2 . LEU L 82  ? 2.4806 3.8740 2.5701 -1.3765 -0.0586 -0.5425 82  LEU K CD2 
21363 N N   . THR L 83  A 2.6202 3.9765 2.6534 -1.3890 -0.1340 -0.4953 82  THR K N   
21364 C CA  . THR L 83  A 2.7471 4.1035 2.7567 -1.4026 -0.1410 -0.4861 82  THR K CA  
21365 C C   . THR L 83  A 2.8021 4.1566 2.8000 -1.4127 -0.1284 -0.4806 82  THR K C   
21366 O O   . THR L 83  A 2.7609 4.1010 2.7630 -1.4091 -0.1237 -0.4749 82  THR K O   
21367 C CB  . THR L 83  A 2.7778 4.1084 2.7707 -1.4035 -0.1658 -0.4680 82  THR K CB  
21368 O OG1 . THR L 83  A 2.7308 4.0634 2.7367 -1.3932 -0.1788 -0.4746 82  THR K OG1 
21369 C CG2 . THR L 83  A 2.8752 4.2041 2.8409 -1.4188 -0.1739 -0.4580 82  THR K CG2 
21370 N N   . GLY L 84  B 2.7163 4.0857 2.6998 -1.4255 -0.1235 -0.4827 82  GLY K N   
21371 C CA  . GLY L 84  B 2.7285 4.0993 2.7007 -1.4361 -0.1116 -0.4793 82  GLY K CA  
21372 C C   . GLY L 84  B 2.7034 4.0875 2.6950 -1.4315 -0.0903 -0.4934 82  GLY K C   
21373 O O   . GLY L 84  B 2.7073 4.0773 2.7013 -1.4298 -0.0866 -0.4875 82  GLY K O   
21374 N N   . VAL L 85  C 2.6017 4.0119 2.6069 -1.4295 -0.0768 -0.5123 82  VAL K N   
21375 C CA  . VAL L 85  C 2.5868 4.0093 2.6105 -1.4247 -0.0569 -0.5270 82  VAL K CA  
21376 C C   . VAL L 85  C 2.5966 4.0296 2.6113 -1.4363 -0.0444 -0.5297 82  VAL K C   
21377 O O   . VAL L 85  C 2.6148 4.0560 2.6108 -1.4488 -0.0466 -0.5265 82  VAL K O   
21378 C CB  . VAL L 85  C 2.5767 4.0230 2.6183 -1.4177 -0.0472 -0.5469 82  VAL K CB  
21379 C CG1 . VAL L 85  C 2.5646 4.0012 2.6191 -1.4050 -0.0572 -0.5466 82  VAL K CG1 
21380 C CG2 . VAL L 85  C 2.5916 4.0590 2.6224 -1.4269 -0.0477 -0.5527 82  VAL K CG2 
21381 N N   . THR L 86  ? 2.5402 3.9723 2.5686 -1.4324 -0.0316 -0.5360 83  THR K N   
21382 C CA  . THR L 86  ? 2.5505 3.9935 2.5757 -1.4415 -0.0185 -0.5415 83  THR K CA  
21383 C C   . THR L 86  ? 2.4992 3.9590 2.5465 -1.4350 0.0002  -0.5616 83  THR K C   
21384 O O   . THR L 86  ? 2.4640 3.9294 2.5259 -1.4253 0.0034  -0.5714 83  THR K O   
21385 C CB  . THR L 86  ? 2.5439 3.9648 2.5624 -1.4443 -0.0239 -0.5270 83  THR K CB  
21386 O OG1 . THR L 86  ? 2.5291 3.9314 2.5646 -1.4315 -0.0261 -0.5243 83  THR K OG1 
21387 C CG2 . THR L 86  ? 2.5798 3.9851 2.5729 -1.4530 -0.0411 -0.5075 83  THR K CG2 
21388 N N   . ALA L 87  ? 2.4041 3.8711 2.4544 -1.4402 0.0123  -0.5681 84  ALA K N   
21389 C CA  . ALA L 87  ? 2.3929 3.8748 2.4637 -1.4347 0.0296  -0.5873 84  ALA K CA  
21390 C C   . ALA L 87  ? 2.3759 3.8396 2.4659 -1.4222 0.0299  -0.5870 84  ALA K C   
21391 O O   . ALA L 87  ? 2.3656 3.8384 2.4729 -1.4158 0.0424  -0.6025 84  ALA K O   
21392 C CB  . ALA L 87  ? 2.4021 3.8975 2.4715 -1.4441 0.0417  -0.5951 84  ALA K CB  
21393 N N   . ALA L 88  ? 2.5963 4.0337 2.6824 -1.4192 0.0163  -0.5698 85  ALA K N   
21394 C CA  . ALA L 88  ? 2.5332 3.9507 2.6357 -1.4081 0.0151  -0.5677 85  ALA K CA  
21395 C C   . ALA L 88  ? 2.4577 3.8720 2.5676 -1.3981 0.0117  -0.5703 85  ALA K C   
21396 O O   . ALA L 88  ? 2.3804 3.7831 2.5053 -1.3890 0.0144  -0.5733 85  ALA K O   
21397 C CB  . ALA L 88  ? 2.5483 3.9390 2.6436 -1.4088 0.0016  -0.5482 85  ALA K CB  
21398 N N   . ASP L 89  ? 2.5433 3.9676 2.6430 -1.4001 0.0056  -0.5696 86  ASP K N   
21399 C CA  . ASP L 89  ? 2.4839 3.9077 2.5906 -1.3913 0.0014  -0.5729 86  ASP K CA  
21400 C C   . ASP L 89  ? 2.4431 3.8913 2.5631 -1.3880 0.0172  -0.5947 86  ASP K C   
21401 O O   . ASP L 89  ? 2.3660 3.8170 2.4937 -1.3808 0.0162  -0.6005 86  ASP K O   
21402 C CB  . ASP L 89  ? 2.5121 3.9356 2.6032 -1.3948 -0.0140 -0.5626 86  ASP K CB  
21403 C CG  . ASP L 89  ? 2.5763 3.9732 2.6534 -1.3970 -0.0311 -0.5406 86  ASP K CG  
21404 O OD1 . ASP L 89  ? 2.5219 3.8975 2.6052 -1.3913 -0.0337 -0.5331 86  ASP K OD1 
21405 O OD2 . ASP L 89  ? 2.6096 4.0062 2.6687 -1.4047 -0.0421 -0.5309 86  ASP K OD2 
21406 N N   . SER L 90  ? 2.5282 3.9941 2.6512 -1.3932 0.0319  -0.6072 87  SER K N   
21407 C CA  . SER L 90  ? 2.4829 3.9724 2.6176 -1.3911 0.0483  -0.6286 87  SER K CA  
21408 C C   . SER L 90  ? 2.3782 3.8580 2.5304 -1.3817 0.0562  -0.6363 87  SER K C   
21409 O O   . SER L 90  ? 2.3759 3.8472 2.5356 -1.3814 0.0625  -0.6377 87  SER K O   
21410 C CB  . SER L 90  ? 2.5020 4.0107 2.6338 -1.3999 0.0607  -0.6384 87  SER K CB  
21411 O OG  . SER L 90  ? 2.4475 3.9783 2.5904 -1.3979 0.0770  -0.6594 87  SER K OG  
21412 N N   . ALA L 91  ? 2.5382 3.9481 2.4050 -1.0816 0.1033  -0.4831 88  ALA K N   
21413 C CA  . ALA L 91  ? 2.4831 3.8481 2.3586 -0.9990 0.1240  -0.4845 88  ALA K CA  
21414 C C   . ALA L 91  ? 2.4298 3.6755 2.3275 -0.9780 0.1323  -0.4485 88  ALA K C   
21415 O O   . ALA L 91  ? 2.4298 3.6368 2.3377 -1.0251 0.1222  -0.4272 88  ALA K O   
21416 C CB  . ALA L 91  ? 2.4873 3.8568 2.3430 -0.9723 0.1201  -0.4899 88  ALA K CB  
21417 N N   . ILE L 92  ? 2.4879 3.6751 2.3935 -0.9055 0.1514  -0.4424 89  ILE K N   
21418 C CA  . ILE L 92  ? 2.4506 3.5213 2.3798 -0.8756 0.1630  -0.4094 89  ILE K CA  
21419 C C   . ILE L 92  ? 2.4870 3.4825 2.4038 -0.8624 0.1572  -0.3833 89  ILE K C   
21420 O O   . ILE L 92  ? 2.5133 3.5112 2.4170 -0.8082 0.1671  -0.3927 89  ILE K O   
21421 C CB  . ILE L 92  ? 2.4447 3.5002 2.3949 -0.8001 0.1925  -0.4206 89  ILE K CB  
21422 C CG1 . ILE L 92  ? 2.4105 3.5495 2.3717 -0.8107 0.1978  -0.4500 89  ILE K CG1 
21423 C CG2 . ILE L 92  ? 2.4248 3.3594 2.4043 -0.7708 0.2059  -0.3866 89  ILE K CG2 
21424 C CD1 . ILE L 92  ? 2.4386 3.5679 2.4210 -0.7370 0.2271  -0.4628 89  ILE K CD1 
21425 N N   . TYR L 93  ? 2.6046 3.5333 2.5242 -0.9101 0.1409  -0.3510 90  TYR K N   
21426 C CA  . TYR L 93  ? 2.6167 3.4742 2.5240 -0.9061 0.1323  -0.3246 90  TYR K CA  
21427 C C   . TYR L 93  ? 2.5510 3.2912 2.4786 -0.8503 0.1508  -0.2955 90  TYR K C   
21428 O O   . TYR L 93  ? 2.5241 3.2033 2.4787 -0.8591 0.1557  -0.2762 90  TYR K O   
21429 C CB  . TYR L 93  ? 2.7083 3.5522 2.6073 -0.9872 0.1049  -0.3038 90  TYR K CB  
21430 C CG  . TYR L 93  ? 2.7561 3.7052 2.6326 -1.0444 0.0859  -0.3276 90  TYR K CG  
21431 C CD1 . TYR L 93  ? 2.7609 3.7880 2.6404 -1.0823 0.0832  -0.3486 90  TYR K CD1 
21432 C CD2 . TYR L 93  ? 2.7516 3.7205 2.6051 -1.0612 0.0707  -0.3286 90  TYR K CD2 
21433 C CE1 . TYR L 93  ? 2.8107 3.9326 2.6705 -1.1344 0.0675  -0.3697 90  TYR K CE1 
21434 C CE2 . TYR L 93  ? 2.8044 3.8678 2.6409 -1.1133 0.0546  -0.3503 90  TYR K CE2 
21435 C CZ  . TYR L 93  ? 2.8411 3.9803 2.6807 -1.1500 0.0537  -0.3704 90  TYR K CZ  
21436 O OH  . TYR L 93  ? 2.8830 4.1152 2.7066 -1.2019 0.0393  -0.3915 90  TYR K OH  
21437 N N   . TYR L 94  ? 2.6591 3.3679 2.5745 -0.7917 0.1616  -0.2931 91  TYR K N   
21438 C CA  . TYR L 94  ? 2.6645 3.2619 2.5962 -0.7341 0.1811  -0.2654 91  TYR K CA  
21439 C C   . TYR L 94  ? 2.7010 3.2276 2.6180 -0.7484 0.1661  -0.2354 91  TYR K C   
21440 O O   . TYR L 94  ? 2.7063 3.2789 2.5962 -0.7767 0.1462  -0.2436 91  TYR K O   
21441 C CB  . TYR L 94  ? 2.6524 3.2549 2.5812 -0.6460 0.2091  -0.2824 91  TYR K CB  
21442 C CG  . TYR L 94  ? 2.6014 3.2671 2.5454 -0.6206 0.2274  -0.3117 91  TYR K CG  
21443 C CD1 . TYR L 94  ? 2.5679 3.1774 2.5474 -0.5913 0.2495  -0.3010 91  TYR K CD1 
21444 C CD2 . TYR L 94  ? 2.6205 3.4002 2.5450 -0.6220 0.2237  -0.3505 91  TYR K CD2 
21445 C CE1 . TYR L 94  ? 2.5403 3.2063 2.5351 -0.5672 0.2663  -0.3276 91  TYR K CE1 
21446 C CE2 . TYR L 94  ? 2.6261 3.4628 2.5643 -0.5975 0.2406  -0.3771 91  TYR K CE2 
21447 C CZ  . TYR L 94  ? 2.5854 3.3645 2.5583 -0.5699 0.2618  -0.3653 91  TYR K CZ  
21448 O OH  . TYR L 94  ? 2.5867 3.4216 2.5748 -0.5455 0.2784  -0.3916 91  TYR K OH  
21449 N N   . CYS L 95  ? 2.9123 3.3266 2.8498 -0.7292 0.1756  -0.2011 92  CYS K N   
21450 C CA  . CYS L 95  ? 2.9210 3.2509 2.8489 -0.7312 0.1661  -0.1690 92  CYS K CA  
21451 C C   . CYS L 95  ? 2.9074 3.1567 2.8429 -0.6455 0.1948  -0.1556 92  CYS K C   
21452 O O   . CYS L 95  ? 2.8875 3.0833 2.8541 -0.6121 0.2178  -0.1462 92  CYS K O   
21453 C CB  . CYS L 95  ? 2.8707 3.1372 2.8146 -0.7948 0.1486  -0.1378 92  CYS K CB  
21454 S SG  . CYS L 95  ? 3.1373 3.3031 3.1276 -0.7782 0.1675  -0.1123 92  CYS K SG  
21455 N N   . ALA L 96  ? 2.7541 2.9959 2.6621 -0.6081 0.1945  -0.1557 93  ALA K N   
21456 C CA  . ALA L 96  ? 2.8238 2.9953 2.7332 -0.5223 0.2228  -0.1451 93  ALA K CA  
21457 C C   . ALA L 96  ? 2.8512 2.9543 2.7401 -0.5102 0.2135  -0.1198 93  ALA K C   
21458 O O   . ALA L 96  ? 2.8350 2.9779 2.6985 -0.5509 0.1866  -0.1246 93  ALA K O   
21459 C CB  . ALA L 96  ? 2.8850 3.1312 2.7777 -0.4620 0.2400  -0.1810 93  ALA K CB  
21460 N N   . THR L 97  ? 2.7775 2.7757 2.6791 -0.4539 0.2367  -0.0924 94  THR K N   
21461 C CA  . THR L 97  ? 2.8203 2.7469 2.7023 -0.4324 0.2316  -0.0676 94  THR K CA  
21462 C C   . THR L 97  ? 2.8888 2.8738 2.7324 -0.3857 0.2309  -0.0933 94  THR K C   
21463 O O   . THR L 97  ? 2.9316 2.9833 2.7690 -0.3464 0.2456  -0.1243 94  THR K O   
21464 C CB  . THR L 97  ? 2.8549 2.6594 2.7609 -0.3753 0.2614  -0.0350 94  THR K CB  
21465 O OG1 . THR L 97  ? 2.7806 2.5235 2.7209 -0.4255 0.2557  -0.0085 94  THR K OG1 
21466 C CG2 . THR L 97  ? 2.9256 2.6581 2.8075 -0.3299 0.2642  -0.0133 94  THR K CG2 
21467 N N   . THR L 98  ? 2.7594 2.7194 2.5773 -0.3888 0.2131  -0.0813 95  THR K N   
21468 C CA  . THR L 98  ? 2.8233 2.8396 2.6047 -0.3476 0.2084  -0.1069 95  THR K CA  
21469 C C   . THR L 98  ? 2.9053 2.8364 2.6668 -0.2940 0.2134  -0.0832 95  THR K C   
21470 O O   . THR L 98  ? 2.8865 2.7583 2.6477 -0.3297 0.1960  -0.0548 95  THR K O   
21471 C CB  . THR L 98  ? 2.7684 2.8820 2.5331 -0.4183 0.1725  -0.1298 95  THR K CB  
21472 O OG1 . THR L 98  ? 2.7011 2.8932 2.4830 -0.4678 0.1688  -0.1511 95  THR K OG1 
21473 C CG2 . THR L 98  ? 2.8334 3.0128 2.5642 -0.3763 0.1666  -0.1609 95  THR K CG2 
21474 N N   . LYS L 99  ? 2.6986 2.6217 2.4427 -0.2077 0.2375  -0.0944 96  LYS K N   
21475 C CA  . LYS L 99  ? 2.7907 2.6435 2.5095 -0.1483 0.2429  -0.0770 96  LYS K CA  
21476 C C   . LYS L 99  ? 2.8438 2.7793 2.5241 -0.1259 0.2262  -0.1114 96  LYS K C   
21477 O O   . LYS L 99  ? 2.8496 2.8715 2.5218 -0.1041 0.2322  -0.1482 96  LYS K O   
21478 C CB  . LYS L 99  ? 2.8636 2.6276 2.5902 -0.0617 0.2845  -0.0585 96  LYS K CB  
21479 C CG  . LYS L 99  ? 2.8122 2.4819 2.5802 -0.0807 0.3007  -0.0218 96  LYS K CG  
21480 C CD  . LYS L 99  ? 2.8754 2.4502 2.6511 0.0078  0.3428  -0.0013 96  LYS K CD  
21481 C CE  . LYS L 99  ? 2.8129 2.2959 2.6349 -0.0097 0.3601  0.0326  96  LYS K CE  
21482 N NZ  . LYS L 99  ? 2.7222 2.2588 2.5790 -0.0678 0.3554  0.0189  96  LYS K NZ  
21483 N N   . HIS L 100 ? 2.5843 2.4934 2.2423 -0.1311 0.2048  -0.1002 97  HIS K N   
21484 C CA  . HIS L 100 ? 2.6243 2.6063 2.2483 -0.1151 0.1843  -0.1313 97  HIS K CA  
21485 C C   . HIS L 100 ? 2.7603 2.6982 2.3552 -0.0125 0.2060  -0.1324 97  HIS K C   
21486 O O   . HIS L 100 ? 2.8139 2.6480 2.4122 0.0379  0.2318  -0.1004 97  HIS K O   
21487 C CB  . HIS L 100 ? 2.5647 2.5459 2.1801 -0.1756 0.1473  -0.1210 97  HIS K CB  
21488 C CG  . HIS L 100 ? 2.6185 2.4805 2.2303 -0.1571 0.1497  -0.0781 97  HIS K CG  
21489 N ND1 . HIS L 100 ? 2.5644 2.3469 2.2027 -0.2029 0.1503  -0.0393 97  HIS K ND1 
21490 C CD2 . HIS L 100 ? 2.7260 2.5347 2.3101 -0.0956 0.1515  -0.0685 97  HIS K CD2 
21491 C CE1 . HIS L 100 ? 2.6343 2.3199 2.2623 -0.1715 0.1528  -0.0074 97  HIS K CE1 
21492 N NE2 . HIS L 100 ? 2.7359 2.4349 2.3305 -0.1060 0.1538  -0.0239 97  HIS K NE2 
21493 N N   . GLY L 101 ? 2.5893 2.6069 2.1551 0.0191  0.1955  -0.1701 98  GLY K N   
21494 C CA  . GLY L 101 ? 2.7252 2.7096 2.2581 0.1161  0.2121  -0.1750 98  GLY K CA  
21495 C C   . GLY L 101 ? 2.7439 2.7988 2.2473 0.1133  0.1797  -0.2050 98  GLY K C   
21496 O O   . GLY L 101 ? 2.6667 2.8154 2.1772 0.0473  0.1519  -0.2314 98  GLY K O   
21497 N N   . ARG L 102 ? 2.8193 2.8277 2.2903 0.1871  0.1839  -0.2013 99  ARG K N   
21498 C CA  . ARG L 102 ? 2.7336 2.7992 2.1768 0.1921  0.1528  -0.2288 99  ARG K CA  
21499 C C   . ARG L 102 ? 2.7800 2.8713 2.1881 0.2904  0.1680  -0.2589 99  ARG K C   
21500 O O   . ARG L 102 ? 2.8225 2.8290 2.2097 0.3708  0.1930  -0.2387 99  ARG K O   
21501 C CB  . ARG L 102 ? 2.6761 2.6589 2.1138 0.1743  0.1352  -0.1933 99  ARG K CB  
21502 C CG  . ARG L 102 ? 2.5492 2.5925 1.9924 0.0929  0.0915  -0.2054 99  ARG K CG  
21503 C CD  . ARG L 102 ? 2.5562 2.5034 1.9974 0.0780  0.0802  -0.1645 99  ARG K CD  
21504 N NE  . ARG L 102 ? 2.6700 2.5401 2.1386 0.0564  0.1041  -0.1261 99  ARG K NE  
21505 C CZ  . ARG L 102 ? 2.7481 2.5234 2.2282 0.0296  0.1026  -0.0826 99  ARG K CZ  
21506 N NH1 . ARG L 102 ? 2.8385 2.5513 2.3464 0.0121  0.1251  -0.0525 99  ARG K NH1 
21507 N NH2 . ARG L 102 ? 2.7080 2.4510 2.1731 0.0213  0.0785  -0.0701 99  ARG K NH2 
21508 N N   . ARG L 103 ? 2.6070 2.8150 2.0083 0.2832  0.1527  -0.3072 100 ARG K N   
21509 C CA  . ARG L 103 ? 2.6459 2.8984 2.0144 0.3691  0.1624  -0.3439 100 ARG K CA  
21510 C C   . ARG L 103 ? 2.6133 2.8885 1.9516 0.3933  0.1326  -0.3637 100 ARG K C   
21511 O O   . ARG L 103 ? 2.5994 2.9575 1.9458 0.3334  0.0981  -0.3902 100 ARG K O   
21512 C CB  . ARG L 103 ? 2.6738 3.0416 2.0546 0.3476  0.1632  -0.3865 100 ARG K CB  
21513 C CG  . ARG L 103 ? 2.7081 3.1304 2.0577 0.4320  0.1736  -0.4274 100 ARG K CG  
21514 C CD  . ARG L 103 ? 2.8127 3.1469 2.1453 0.5242  0.2159  -0.4055 100 ARG K CD  
21515 N NE  . ARG L 103 ? 2.8587 3.2528 2.1665 0.5974  0.2303  -0.4453 100 ARG K NE  
21516 C CZ  . ARG L 103 ? 2.8581 3.2654 2.1257 0.6704  0.2237  -0.4694 100 ARG K CZ  
21517 N NH1 . ARG L 103 ? 2.8119 3.1771 2.0601 0.6803  0.2025  -0.4579 100 ARG K NH1 
21518 N NH2 . ARG L 103 ? 2.9040 3.3663 2.1504 0.7348  0.2379  -0.5057 100 ARG K NH2 
21519 N N   . ILE L 104 A 2.8796 3.0807 2.1838 0.4808  0.1458  -0.3511 100 ILE K N   
21520 C CA  . ILE L 104 A 2.8185 3.0315 2.0916 0.5144  0.1189  -0.3687 100 ILE K CA  
21521 C C   . ILE L 104 A 2.8604 3.1377 2.1009 0.5963  0.1249  -0.4146 100 ILE K C   
21522 O O   . ILE L 104 A 2.9436 3.1795 2.1650 0.6758  0.1601  -0.4097 100 ILE K O   
21523 C CB  . ILE L 104 A 2.8151 2.9038 2.0683 0.5583  0.1259  -0.3253 100 ILE K CB  
21524 C CG1 . ILE L 104 A 2.7562 2.7857 2.0404 0.4735  0.1137  -0.2826 100 ILE K CG1 
21525 C CG2 . ILE L 104 A 2.7820 2.8867 1.9964 0.6141  0.1021  -0.3496 100 ILE K CG2 
21526 C CD1 . ILE L 104 A 2.8863 2.8377 2.1974 0.4586  0.1479  -0.2413 100 ILE K CD1 
21527 N N   . TYR L 105 B 2.6000 2.9793 1.8355 0.5768  0.0908  -0.4601 100 TYR K N   
21528 C CA  . TYR L 105 B 2.6229 3.0738 1.8288 0.6485  0.0905  -0.5090 100 TYR K CA  
21529 C C   . TYR L 105 B 2.6511 3.1180 1.8285 0.6841  0.0593  -0.5318 100 TYR K C   
21530 O O   . TYR L 105 B 2.6829 3.1710 1.8248 0.7697  0.0637  -0.5620 100 TYR K O   
21531 C CB  . TYR L 105 B 2.5937 3.1741 1.8233 0.5964  0.0795  -0.5541 100 TYR K CB  
21532 C CG  . TYR L 105 B 2.5654 3.2209 1.8253 0.4951  0.0394  -0.5697 100 TYR K CG  
21533 C CD1 . TYR L 105 B 2.5765 3.3052 1.8264 0.4979  0.0048  -0.6107 100 TYR K CD1 
21534 C CD2 . TYR L 105 B 2.5291 3.1828 1.8280 0.3983  0.0364  -0.5447 100 TYR K CD2 
21535 C CE1 . TYR L 105 B 2.5520 3.3484 1.8316 0.4064  -0.0300 -0.6250 100 TYR K CE1 
21536 C CE2 . TYR L 105 B 2.5059 3.2267 1.8310 0.3073  0.0016  -0.5582 100 TYR K CE2 
21537 C CZ  . TYR L 105 B 2.5173 3.3089 1.8335 0.3115  -0.0307 -0.5979 100 TYR K CZ  
21538 O OH  . TYR L 105 B 2.4953 3.3529 1.8399 0.2218  -0.0637 -0.6115 100 TYR K OH  
21539 N N   . GLY L 106 C 2.6340 3.0908 1.8258 0.6221  0.0278  -0.5187 100 GLY K N   
21540 C CA  . GLY L 106 C 2.6569 3.1334 1.8282 0.6447  -0.0058 -0.5410 100 GLY K CA  
21541 C C   . GLY L 106 C 2.6858 3.0434 1.8320 0.6904  -0.0025 -0.4998 100 GLY K C   
21542 O O   . GLY L 106 C 2.7127 2.9856 1.8312 0.7697  0.0307  -0.4753 100 GLY K O   
21543 N N   . VAL L 107 D 2.6302 2.9798 1.7863 0.6412  -0.0359 -0.4914 100 VAL K N   
21544 C CA  . VAL L 107 D 2.6575 2.9013 1.7899 0.6807  -0.0381 -0.4554 100 VAL K CA  
21545 C C   . VAL L 107 D 2.6320 2.8047 1.7946 0.5996  -0.0406 -0.4042 100 VAL K C   
21546 O O   . VAL L 107 D 2.6460 2.7497 1.7987 0.6035  -0.0541 -0.3779 100 VAL K O   
21547 C CB  . VAL L 107 D 2.6812 2.9657 1.7933 0.7082  -0.0760 -0.4893 100 VAL K CB  
21548 C CG1 . VAL L 107 D 2.7152 3.0460 1.7891 0.8073  -0.0695 -0.5341 100 VAL K CG1 
21549 C CG2 . VAL L 107 D 2.6486 3.0311 1.7991 0.6090  -0.1156 -0.5169 100 VAL K CG2 
21550 N N   . VAL L 108 E 2.7254 2.9152 1.9244 0.5264  -0.0287 -0.3908 100 VAL K N   
21551 C CA  . VAL L 108 E 2.7002 2.8237 1.9290 0.4489  -0.0284 -0.3428 100 VAL K CA  
21552 C C   . VAL L 108 E 2.6884 2.8337 1.9330 0.3758  -0.0705 -0.3429 100 VAL K C   
21553 O O   . VAL L 108 E 2.6544 2.8408 1.9348 0.2792  -0.0855 -0.3399 100 VAL K O   
21554 C CB  . VAL L 108 E 2.7216 2.7061 1.9332 0.5046  0.0027  -0.2904 100 VAL K CB  
21555 C CG1 . VAL L 108 E 2.6937 2.6131 1.9391 0.4233  0.0040  -0.2429 100 VAL K CG1 
21556 C CG2 . VAL L 108 E 2.7370 2.6956 1.9324 0.5832  0.0460  -0.2900 100 VAL K CG2 
21557 N N   . ALA L 109 F 2.7678 2.8860 1.9856 0.4226  -0.0897 -0.3468 100 ALA K N   
21558 C CA  . ALA L 109 F 2.7725 2.8998 2.0045 0.3598  -0.1287 -0.3437 100 ALA K CA  
21559 C C   . ALA L 109 F 2.7777 3.0341 2.0377 0.2874  -0.1602 -0.3891 100 ALA K C   
21560 O O   . ALA L 109 F 2.8322 3.1040 2.1193 0.2028  -0.1865 -0.3806 100 ALA K O   
21561 C CB  . ALA L 109 F 2.8089 2.8901 2.0045 0.4343  -0.1429 -0.3452 100 ALA K CB  
21562 N N   . PHE L 110 G 2.5395 2.8891 1.7947 0.3173  -0.1573 -0.4371 100 PHE K N   
21563 C CA  . PHE L 110 G 2.5170 2.9912 1.8005 0.2506  -0.1852 -0.4818 100 PHE K CA  
21564 C C   . PHE L 110 G 2.4806 3.0008 1.7973 0.1757  -0.1715 -0.4791 100 PHE K C   
21565 O O   . PHE L 110 G 2.4651 3.0953 1.8000 0.1410  -0.1829 -0.5216 100 PHE K O   
21566 C CB  . PHE L 110 G 2.5380 3.0992 1.8021 0.3166  -0.1949 -0.5404 100 PHE K CB  
21567 C CG  . PHE L 110 G 2.5637 3.1291 1.8115 0.3509  -0.2271 -0.5601 100 PHE K CG  
21568 C CD1 . PHE L 110 G 2.5489 3.1921 1.8258 0.2829  -0.2653 -0.5878 100 PHE K CD1 
21569 C CD2 . PHE L 110 G 2.6038 3.0989 1.8080 0.4523  -0.2191 -0.5532 100 PHE K CD2 
21570 C CE1 . PHE L 110 G 2.5718 3.2217 1.8371 0.3139  -0.2960 -0.6081 100 PHE K CE1 
21571 C CE2 . PHE L 110 G 2.6281 3.1294 1.8174 0.4850  -0.2501 -0.5731 100 PHE K CE2 
21572 C CZ  . PHE L 110 G 2.6113 3.1908 1.8323 0.4154  -0.2893 -0.6012 100 PHE K CZ  
21573 N N   . LYS L 111 H 2.6306 3.0682 1.9557 0.1517  -0.1472 -0.4307 100 LYS K N   
21574 C CA  . LYS L 111 H 2.5973 3.0665 1.9529 0.0822  -0.1331 -0.4233 100 LYS K CA  
21575 C C   . LYS L 111 H 2.5953 3.1447 1.9470 0.1181  -0.1151 -0.4630 100 LYS K C   
21576 O O   . LYS L 111 H 2.5722 3.1965 1.9503 0.0565  -0.1152 -0.4796 100 LYS K O   
21577 C CB  . LYS L 111 H 2.5771 3.1075 1.9672 -0.0267 -0.1642 -0.4294 100 LYS K CB  
21578 C CG  . LYS L 111 H 2.5774 3.0230 1.9733 -0.0687 -0.1795 -0.3855 100 LYS K CG  
21579 C CD  . LYS L 111 H 2.6238 3.1281 2.0528 -0.1752 -0.2091 -0.3908 100 LYS K CD  
21580 C CE  . LYS L 111 H 2.6337 3.0498 2.0671 -0.2147 -0.2234 -0.3460 100 LYS K CE  
21581 N NZ  . LYS L 111 H 2.7176 3.1786 2.1841 -0.3240 -0.2465 -0.3430 100 LYS K NZ  
21582 N N   . GLU L 112 I 2.4726 3.0046 1.7898 0.2201  -0.0993 -0.4780 100 GLU K N   
21583 C CA  . GLU L 112 I 2.4761 3.0764 1.7838 0.2689  -0.0809 -0.5159 100 GLU K CA  
21584 C C   . GLU L 112 I 2.4684 3.0112 1.7783 0.2875  -0.0398 -0.4859 100 GLU K C   
21585 O O   . GLU L 112 I 2.4916 2.9953 1.7746 0.3752  -0.0117 -0.4850 100 GLU K O   
21586 C CB  . GLU L 112 I 2.5149 3.1209 1.7827 0.3711  -0.0837 -0.5458 100 GLU K CB  
21587 C CG  . GLU L 112 I 2.5221 3.2015 1.7910 0.3566  -0.1252 -0.5850 100 GLU K CG  
21588 C CD  . GLU L 112 I 2.5628 3.2453 1.7906 0.4621  -0.1287 -0.6154 100 GLU K CD  
21589 O OE1 . GLU L 112 I 2.5901 3.1900 1.7842 0.5462  -0.1009 -0.5935 100 GLU K OE1 
21590 O OE2 . GLU L 112 I 2.5688 3.3351 1.7983 0.4620  -0.1593 -0.6614 100 GLU K OE2 
21591 N N   . TRP L 113 J 2.6197 3.1574 1.9635 0.2030  -0.0364 -0.4614 100 TRP K N   
21592 C CA  . TRP L 113 J 2.6141 3.1006 1.9678 0.2079  -0.0004 -0.4329 100 TRP K CA  
21593 C C   . TRP L 113 J 2.6684 3.2114 2.0609 0.1069  -0.0064 -0.4329 100 TRP K C   
21594 O O   . TRP L 113 J 2.6314 3.2427 2.0414 0.0343  -0.0369 -0.4502 100 TRP K O   
21595 C CB  . TRP L 113 J 2.6497 2.9977 1.9953 0.2361  0.0176  -0.3774 100 TRP K CB  
21596 C CG  . TRP L 113 J 2.7074 3.0090 2.0723 0.1583  -0.0052 -0.3432 100 TRP K CG  
21597 C CD1 . TRP L 113 J 2.7549 3.1218 2.1382 0.0766  -0.0410 -0.3579 100 TRP K CD1 
21598 C CD2 . TRP L 113 J 2.7116 2.8893 2.0768 0.1613  0.0057  -0.2898 100 TRP K CD2 
21599 N NE1 . TRP L 113 J 2.7493 3.0417 2.1444 0.0259  -0.0525 -0.3163 100 TRP K NE1 
21600 C CE2 . TRP L 113 J 2.7086 2.8848 2.0927 0.0766  -0.0250 -0.2744 100 TRP K CE2 
21601 C CE3 . TRP L 113 J 2.7188 2.7866 2.0718 0.2262  0.0396  -0.2533 100 TRP K CE3 
21602 C CZ2 . TRP L 113 J 2.6978 2.7676 2.0879 0.0552  -0.0242 -0.2248 100 TRP K CZ2 
21603 C CZ3 . TRP L 113 J 2.6761 2.6384 2.0369 0.2046  0.0409  -0.2041 100 TRP K CZ3 
21604 C CH2 . TRP L 113 J 2.6660 2.6304 2.0446 0.1198  0.0087  -0.1906 100 TRP K CH2 
21605 N N   . PHE L 114 K 2.6498 3.1634 2.0564 0.1036  0.0234  -0.4136 100 PHE K N   
21606 C CA  . PHE L 114 K 2.6918 3.2489 2.1333 0.0121  0.0202  -0.4100 100 PHE K CA  
21607 C C   . PHE L 114 K 2.6419 3.1135 2.0977 0.0149  0.0521  -0.3693 100 PHE K C   
21608 O O   . PHE L 114 K 2.5838 2.9988 2.0248 0.0936  0.0826  -0.3594 100 PHE K O   
21609 C CB  . PHE L 114 K 2.7069 3.3907 2.1567 -0.0048 0.0171  -0.4595 100 PHE K CB  
21610 C CG  . PHE L 114 K 2.6730 3.3662 2.1108 0.0692  0.0495  -0.4753 100 PHE K CG  
21611 C CD1 . PHE L 114 K 2.6073 3.3148 2.0130 0.1600  0.0558  -0.5027 100 PHE K CD1 
21612 C CD2 . PHE L 114 K 2.6176 3.3078 2.0768 0.0471  0.0733  -0.4639 100 PHE K CD2 
21613 C CE1 . PHE L 114 K 2.5300 3.2461 1.9245 0.2273  0.0865  -0.5169 100 PHE K CE1 
21614 C CE2 . PHE L 114 K 2.5553 3.2550 2.0058 0.1131  0.1035  -0.4783 100 PHE K CE2 
21615 C CZ  . PHE L 114 K 2.5273 3.2396 1.9450 0.2030  0.1107  -0.5044 100 PHE K CZ  
21616 N N   . THR L 115 L 2.4271 2.8893 1.9125 -0.0714 0.0449  -0.3461 100 THR K N   
21617 C CA  . THR L 115 L 2.4150 2.7991 1.9200 -0.0812 0.0709  -0.3079 100 THR K CA  
21618 C C   . THR L 115 L 2.3933 2.8448 1.9178 -0.1016 0.0866  -0.3283 100 THR K C   
21619 O O   . THR L 115 L 2.3747 2.9217 1.9119 -0.1655 0.0678  -0.3550 100 THR K O   
21620 C CB  . THR L 115 L 2.4001 2.7316 1.9258 -0.1630 0.0533  -0.2704 100 THR K CB  
21621 O OG1 . THR L 115 L 2.3821 2.8065 1.9204 -0.2468 0.0229  -0.2931 100 THR K OG1 
21622 C CG2 . THR L 115 L 2.4213 2.6647 1.9298 -0.1369 0.0438  -0.2419 100 THR K CG2 
21623 N N   . TYR L 116 M 2.4480 2.8497 1.9752 -0.0467 0.1215  -0.3161 100 TYR K N   
21624 C CA  . TYR L 116 M 2.4282 2.8832 1.9748 -0.0591 0.1393  -0.3325 100 TYR K CA  
21625 C C   . TYR L 116 M 2.4125 2.7867 1.9886 -0.0900 0.1566  -0.2918 100 TYR K C   
21626 O O   . TYR L 116 M 2.4249 2.6900 2.0006 -0.0564 0.1716  -0.2543 100 TYR K O   
21627 C CB  . TYR L 116 M 2.4447 2.9200 1.9724 0.0335  0.1666  -0.3580 100 TYR K CB  
21628 C CG  . TYR L 116 M 2.4691 2.8316 1.9839 0.1189  0.1976  -0.3278 100 TYR K CG  
21629 C CD1 . TYR L 116 M 2.4997 2.8162 1.9825 0.1785  0.1936  -0.3228 100 TYR K CD1 
21630 C CD2 . TYR L 116 M 2.4628 2.7648 1.9979 0.1412  0.2315  -0.3049 100 TYR K CD2 
21631 C CE1 . TYR L 116 M 2.5245 2.7367 1.9940 0.2577  0.2234  -0.2944 100 TYR K CE1 
21632 C CE2 . TYR L 116 M 2.4864 2.6843 2.0117 0.2192  0.2619  -0.2770 100 TYR K CE2 
21633 C CZ  . TYR L 116 M 2.5178 2.6707 2.0091 0.2773  0.2583  -0.2712 100 TYR K CZ  
21634 O OH  . TYR L 116 M 2.5436 2.5915 2.0237 0.3563  0.2901  -0.2425 100 TYR K OH  
21635 N N   . PHE L 117 N 2.4279 2.8555 2.0300 -0.1523 0.1549  -0.2998 100 PHE K N   
21636 C CA  . PHE L 117 N 2.4112 2.7741 2.0441 -0.1862 0.1690  -0.2664 100 PHE K CA  
21637 C C   . PHE L 117 N 2.4021 2.7841 2.0501 -0.1520 0.1994  -0.2790 100 PHE K C   
21638 O O   . PHE L 117 N 2.3977 2.8746 2.0392 -0.1411 0.2007  -0.3180 100 PHE K O   
21639 C CB  . PHE L 117 N 2.3886 2.7853 2.0413 -0.2909 0.1419  -0.2601 100 PHE K CB  
21640 C CG  . PHE L 117 N 2.3952 2.7603 2.0389 -0.3319 0.1135  -0.2411 100 PHE K CG  
21641 C CD1 . PHE L 117 N 2.3987 2.6520 2.0514 -0.3398 0.1160  -0.1961 100 PHE K CD1 
21642 C CD2 . PHE L 117 N 2.3981 2.8433 2.0263 -0.3623 0.0848  -0.2683 100 PHE K CD2 
21643 C CE1 . PHE L 117 N 2.4047 2.6264 2.0493 -0.3774 0.0900  -0.1778 100 PHE K CE1 
21644 C CE2 . PHE L 117 N 2.4041 2.8183 2.0261 -0.4000 0.0589  -0.2504 100 PHE K CE2 
21645 C CZ  . PHE L 117 N 2.4073 2.7095 2.0365 -0.4076 0.0614  -0.2047 100 PHE K CZ  
21646 N N   . TYR L 118 O 2.7690 3.0614 2.4403 -0.1401 0.2229  -0.2458 100 TYR K N   
21647 C CA  . TYR L 118 O 2.7219 3.0203 2.4136 -0.1101 0.2529  -0.2531 100 TYR K CA  
21648 C C   . TYR L 118 O 2.6654 2.8856 2.3943 -0.1445 0.2637  -0.2175 100 TYR K C   
21649 O O   . TYR L 118 O 2.6415 2.7607 2.3762 -0.1407 0.2664  -0.1800 100 TYR K O   
21650 C CB  . TYR L 118 O 2.7136 2.9794 2.3864 -0.0047 0.2845  -0.2592 100 TYR K CB  
21651 C CG  . TYR L 118 O 2.6974 2.8395 2.3624 0.0492  0.3002  -0.2209 100 TYR K CG  
21652 C CD1 . TYR L 118 O 2.7393 2.8639 2.3722 0.0673  0.2826  -0.2176 100 TYR K CD1 
21653 C CD2 . TYR L 118 O 2.6293 2.6741 2.3190 0.0840  0.3327  -0.1896 100 TYR K CD2 
21654 C CE1 . TYR L 118 O 2.7055 2.7196 2.3287 0.1174  0.2963  -0.1833 100 TYR K CE1 
21655 C CE2 . TYR L 118 O 2.5928 2.5250 2.2748 0.1340  0.3479  -0.1546 100 TYR K CE2 
21656 C CZ  . TYR L 118 O 2.6276 2.5451 2.2748 0.1506  0.3295  -0.1514 100 TYR K CZ  
21657 O OH  . TYR L 118 O 2.5786 2.3844 2.2167 0.2008  0.3447  -0.1165 100 TYR K OH  
21658 N N   . MET L 119 P 2.6405 2.9103 2.3948 -0.1786 0.2689  -0.2309 100 MET K N   
21659 C CA  . MET L 119 P 2.5848 2.7931 2.3774 -0.2121 0.2783  -0.2034 100 MET K CA  
21660 C C   . MET L 119 P 2.5363 2.6844 2.3471 -0.1365 0.3190  -0.1950 100 MET K C   
21661 O O   . MET L 119 P 2.5313 2.7343 2.3362 -0.0895 0.3369  -0.2235 100 MET K O   
21662 C CB  . MET L 119 P 2.5700 2.8622 2.3810 -0.2875 0.2624  -0.2224 100 MET K CB  
21663 C CG  . MET L 119 P 2.6119 2.9531 2.4114 -0.3710 0.2242  -0.2251 100 MET K CG  
21664 S SD  . MET L 119 P 2.6796 3.1100 2.4373 -0.3588 0.2037  -0.2591 100 MET K SD  
21665 C CE  . MET L 119 P 2.6379 3.1849 2.3941 -0.3328 0.2172  -0.3078 100 MET K CE  
21666 N N   . ASP L 120 Q 2.8407 2.8767 2.6751 -0.1257 0.3338  -0.1563 100 ASP K N   
21667 C CA  . ASP L 120 Q 2.8207 2.7858 2.6773 -0.0550 0.3742  -0.1435 100 ASP K CA  
21668 C C   . ASP L 120 Q 2.8037 2.7407 2.7086 -0.0904 0.3837  -0.1313 100 ASP K C   
21669 O O   . ASP L 120 Q 2.7820 2.7213 2.7094 -0.0502 0.4121  -0.1410 100 ASP K O   
21670 C CB  . ASP L 120 Q 2.7819 2.6304 2.6302 -0.0008 0.3900  -0.1083 100 ASP K CB  
21671 C CG  . ASP L 120 Q 2.7496 2.5239 2.6118 -0.0583 0.3701  -0.0720 100 ASP K CG  
21672 O OD1 . ASP L 120 Q 2.8128 2.6387 2.6685 -0.1351 0.3350  -0.0780 100 ASP K OD1 
21673 O OD2 . ASP L 120 Q 2.6649 2.3287 2.5450 -0.0270 0.3902  -0.0376 100 ASP K OD2 
21674 N N   . VAL L 121 R 2.9533 2.8648 2.8746 -0.1648 0.3595  -0.1111 100 VAL K N   
21675 C CA  . VAL L 121 R 2.9431 2.8234 2.9098 -0.2059 0.3628  -0.0979 100 VAL K CA  
21676 C C   . VAL L 121 R 2.9172 2.8931 2.8822 -0.2911 0.3303  -0.1189 100 VAL K C   
21677 O O   . VAL L 121 R 2.9261 2.9105 2.8756 -0.3519 0.2992  -0.1101 100 VAL K O   
21678 C CB  . VAL L 121 R 2.9345 2.6947 2.9223 -0.2190 0.3627  -0.0542 100 VAL K CB  
21679 C CG1 . VAL L 121 R 2.9232 2.6516 2.9598 -0.2606 0.3648  -0.0426 100 VAL K CG1 
21680 C CG2 . VAL L 121 R 2.8406 2.5061 2.8264 -0.1334 0.3953  -0.0326 100 VAL K CG2 
21681 N N   . TRP L 122 ? 2.8239 2.8715 2.8039 -0.2943 0.3383  -0.1465 101 TRP K N   
21682 C CA  . TRP L 122 ? 2.8381 2.9816 2.8175 -0.3679 0.3124  -0.1694 101 TRP K CA  
21683 C C   . TRP L 122 ? 2.8271 2.9338 2.8472 -0.4180 0.3083  -0.1533 101 TRP K C   
21684 O O   . TRP L 122 ? 2.8282 2.8385 2.8806 -0.3939 0.3265  -0.1269 101 TRP K O   
21685 C CB  . TRP L 122 ? 2.8222 3.0697 2.7928 -0.3422 0.3225  -0.2107 101 TRP K CB  
21686 C CG  . TRP L 122 ? 2.8626 3.1663 2.7913 -0.3070 0.3192  -0.2327 101 TRP K CG  
21687 C CD1 . TRP L 122 ? 2.8948 3.1517 2.8042 -0.2330 0.3373  -0.2263 101 TRP K CD1 
21688 C CD2 . TRP L 122 ? 2.8813 3.3000 2.7823 -0.3441 0.2957  -0.2659 101 TRP K CD2 
21689 N NE1 . TRP L 122 ? 2.9383 3.2755 2.8092 -0.2210 0.3250  -0.2549 101 TRP K NE1 
21690 C CE2 . TRP L 122 ? 2.9275 3.3651 2.7945 -0.2892 0.2996  -0.2799 101 TRP K CE2 
21691 C CE3 . TRP L 122 ? 2.8583 3.3655 2.7605 -0.4176 0.2723  -0.2856 101 TRP K CE3 
21692 C CZ2 . TRP L 122 ? 2.9484 3.4911 2.7859 -0.3065 0.2802  -0.3139 101 TRP K CZ2 
21693 C CZ3 . TRP L 122 ? 2.8761 3.4861 2.7487 -0.4352 0.2548  -0.3178 101 TRP K CZ3 
21694 C CH2 . TRP L 122 ? 2.9189 3.5466 2.7611 -0.3804 0.2584  -0.3323 101 TRP K CH2 
21695 N N   . GLY L 123 ? 2.9631 3.1479 2.9815 -0.4885 0.2837  -0.1700 102 GLY K N   
21696 C CA  . GLY L 123 ? 2.9839 3.1490 3.0368 -0.5385 0.2767  -0.1603 102 GLY K CA  
21697 C C   . GLY L 123 ? 2.9295 3.1713 3.0003 -0.5378 0.2862  -0.1911 102 GLY K C   
21698 O O   . GLY L 123 ? 2.8673 3.1823 2.9232 -0.5019 0.2976  -0.2207 102 GLY K O   
21699 N N   . LYS L 124 ? 2.8674 3.0901 2.9712 -0.5783 0.2806  -0.1838 103 LYS K N   
21700 C CA  . LYS L 124 ? 2.8048 3.0944 2.9295 -0.5821 0.2878  -0.2110 103 LYS K CA  
21701 C C   . LYS L 124 ? 2.8218 3.2368 2.9155 -0.6283 0.2667  -0.2432 103 LYS K C   
21702 O O   . LYS L 124 ? 2.8255 3.3155 2.9211 -0.6067 0.2782  -0.2738 103 LYS K O   
21703 C CB  . LYS L 124 ? 2.7811 3.0147 2.9479 -0.6156 0.2839  -0.1943 103 LYS K CB  
21704 C CG  . LYS L 124 ? 2.7867 2.9983 2.9979 -0.5641 0.3138  -0.2025 103 LYS K CG  
21705 C CD  . LYS L 124 ? 2.8038 2.9535 3.0600 -0.5943 0.3093  -0.1860 103 LYS K CD  
21706 C CE  . LYS L 124 ? 2.8293 2.9583 3.1335 -0.5411 0.3399  -0.1958 103 LYS K CE  
21707 N NZ  . LYS L 124 ? 2.8664 2.9609 3.2151 -0.5757 0.3319  -0.1896 103 LYS K NZ  
21708 N N   . GLY L 125 ? 2.6358 3.0745 2.7024 -0.6914 0.2370  -0.2371 104 GLY K N   
21709 C CA  . GLY L 125 ? 2.6332 3.1848 2.6702 -0.7409 0.2160  -0.2643 104 GLY K CA  
21710 C C   . GLY L 125 ? 2.6232 3.2064 2.6722 -0.8099 0.1977  -0.2669 104 GLY K C   
21711 O O   . GLY L 125 ? 2.6147 3.1557 2.6984 -0.8078 0.2057  -0.2593 104 GLY K O   
21712 N N   . THR L 126 ? 2.7824 3.4395 2.8025 -0.8719 0.1727  -0.2779 105 THR K N   
21713 C CA  . THR L 126 ? 2.7776 3.4771 2.8002 -0.9406 0.1538  -0.2827 105 THR K CA  
21714 C C   . THR L 126 ? 2.7822 3.6085 2.7840 -0.9596 0.1492  -0.3203 105 THR K C   
21715 O O   . THR L 126 ? 2.7545 3.6361 2.7318 -0.9416 0.1504  -0.3381 105 THR K O   
21716 C CB  . THR L 126 ? 2.6993 3.3645 2.7062 -1.0087 0.1263  -0.2569 105 THR K CB  
21717 O OG1 . THR L 126 ? 2.7123 3.3893 2.6887 -1.0099 0.1177  -0.2544 105 THR K OG1 
21718 C CG2 . THR L 126 ? 2.6700 3.2171 2.7040 -1.0066 0.1272  -0.2217 105 THR K CG2 
21719 N N   . SER L 127 ? 2.6980 3.5706 2.7099 -0.9953 0.1436  -0.3331 106 SER K N   
21720 C CA  . SER L 127 ? 2.6293 3.6218 2.6232 -1.0168 0.1395  -0.3682 106 SER K CA  
21721 C C   . SER L 127 ? 2.7133 3.7428 2.6832 -1.0988 0.1120  -0.3630 106 SER K C   
21722 O O   . SER L 127 ? 2.7620 3.7470 2.7405 -1.1419 0.0993  -0.3428 106 SER K O   
21723 C CB  . SER L 127 ? 2.6294 3.6554 2.6486 -1.0005 0.1523  -0.3879 106 SER K CB  
21724 O OG  . SER L 127 ? 2.6858 3.6702 2.7306 -0.9251 0.1791  -0.3904 106 SER K OG  
21725 N N   . VAL L 128 ? 2.4668 3.5758 2.4074 -1.1196 0.1032  -0.3814 107 VAL K N   
21726 C CA  . VAL L 128 ? 2.5260 3.6781 2.4430 -1.1963 0.0794  -0.3788 107 VAL K CA  
21727 C C   . VAL L 128 ? 2.5759 3.8526 2.4786 -1.2135 0.0795  -0.4165 107 VAL K C   
21728 O O   . VAL L 128 ? 2.5811 3.9151 2.4735 -1.1812 0.0872  -0.4405 107 VAL K O   
21729 C CB  . VAL L 128 ? 2.5392 3.6600 2.4364 -1.2127 0.0664  -0.3609 107 VAL K CB  
21730 C CG1 . VAL L 128 ? 2.6074 3.7833 2.4812 -1.2905 0.0443  -0.3619 107 VAL K CG1 
21731 C CG2 . VAL L 128 ? 2.5346 3.5303 2.4458 -1.2003 0.0654  -0.3220 107 VAL K CG2 
21732 N N   . THR L 129 ? 2.5361 3.8543 2.4375 -1.2631 0.0708  -0.4222 108 THR K N   
21733 C CA  . THR L 129 ? 2.5930 4.0238 2.4797 -1.2802 0.0714  -0.4552 108 THR K CA  
21734 C C   . THR L 129 ? 2.6982 4.1188 2.5385 -1.3069 0.0592  -0.4338 108 THR K C   
21735 O O   . THR L 129 ? 2.7271 4.0735 2.5551 -1.3212 0.0502  -0.4013 108 THR K O   
21736 C CB  . THR L 129 ? 2.5771 4.0341 2.4849 -1.2704 0.0810  -0.4709 108 THR K CB  
21737 O OG1 . THR L 129 ? 2.5076 3.9182 2.4407 -1.1971 0.1015  -0.4725 108 THR K OG1 
21738 C CG2 . THR L 129 ? 2.6403 4.2044 2.5289 -1.2728 0.0852  -0.5029 108 THR K CG2 
21739 N N   . VAL L 130 ? 2.4983 3.9936 2.3156 -1.3122 0.0598  -0.4529 109 VAL K N   
21740 C CA  . VAL L 130 ? 2.5345 4.0305 2.3121 -1.3383 0.0526  -0.4362 109 VAL K CA  
21741 C C   . VAL L 130 ? 2.5437 4.1136 2.3079 -1.3458 0.0608  -0.4561 109 VAL K C   
21742 O O   . VAL L 130 ? 2.5318 4.1926 2.3001 -1.3345 0.0707  -0.4912 109 VAL K O   
21743 C CB  . VAL L 130 ? 2.5427 4.0672 2.3060 -1.3416 0.0490  -0.4419 109 VAL K CB  
21744 C CG1 . VAL L 130 ? 2.5797 4.1102 2.3067 -1.3694 0.0447  -0.4269 109 VAL K CG1 
21745 C CG2 . VAL L 130 ? 2.5355 3.9836 2.3101 -1.3352 0.0401  -0.4205 109 VAL K CG2 
21746 N N   . SER L 131 ? 2.5384 4.0700 2.2860 -1.3635 0.0566  -0.4345 110 SER K N   
21747 C CA  . SER L 131 ? 2.5511 4.1447 2.2831 -1.3739 0.0638  -0.4494 110 SER K CA  
21748 C C   . SER L 131 ? 2.5868 4.1267 2.2882 -1.4007 0.0549  -0.4175 110 SER K C   
21749 O O   . SER L 131 ? 2.5926 4.0431 2.2959 -1.4031 0.0437  -0.3873 110 SER K O   
21750 C CB  . SER L 131 ? 2.5247 4.1473 2.2851 -1.3544 0.0720  -0.4717 110 SER K CB  
21751 O OG  . SER L 131 ? 2.5381 4.2223 2.2818 -1.3645 0.0789  -0.4861 110 SER K OG  
21752 N N   . SER L 132 ? 2.7476 4.3430 2.4211 -1.4201 0.0603  -0.4249 111 SER K N   
21753 C CA  . SER L 132 ? 2.8195 4.3733 2.4614 -1.4467 0.0529  -0.3975 111 SER K CA  
21754 C C   . SER L 132 ? 2.8574 4.3953 2.5024 -1.4472 0.0517  -0.3945 111 SER K C   
21755 O O   . SER L 132 ? 2.9183 4.4313 2.5360 -1.4687 0.0463  -0.3756 111 SER K O   
21756 C CB  . SER L 132 ? 2.8233 4.4404 2.4334 -1.4704 0.0600  -0.4050 111 SER K CB  
21757 O OG  . SER L 132 ? 2.7714 4.4819 2.3856 -1.4655 0.0744  -0.4385 111 SER K OG  
21758 N N   . ALA L 133 ? 2.9261 4.4792 2.6042 -1.4238 0.0564  -0.4138 112 ALA K N   
21759 C CA  . ALA L 133 ? 2.9206 4.4610 2.6083 -1.4210 0.0550  -0.4144 112 ALA K CA  
21760 C C   . ALA L 133 ? 2.9083 4.3452 2.6132 -1.4145 0.0416  -0.3863 112 ALA K C   
21761 O O   . ALA L 133 ? 2.8898 4.2735 2.6114 -1.4033 0.0369  -0.3738 112 ALA K O   
21762 C CB  . ALA L 133 ? 2.8871 4.4951 2.6059 -1.3974 0.0669  -0.4504 112 ALA K CB  
21763 N N   . SER L 134 ? 3.1650 4.5741 2.8666 -1.4210 0.0356  -0.3769 113 SER K N   
21764 C CA  . SER L 134 ? 3.1136 4.4257 2.8325 -1.4144 0.0225  -0.3513 113 SER K CA  
21765 C C   . SER L 134 ? 3.0405 4.3357 2.8109 -1.3862 0.0261  -0.3650 113 SER K C   
21766 O O   . SER L 134 ? 2.9687 4.3316 2.7604 -1.3719 0.0384  -0.3960 113 SER K O   
21767 C CB  . SER L 134 ? 3.1477 4.4394 2.8451 -1.4313 0.0141  -0.3384 113 SER K CB  
21768 O OG  . SER L 134 ? 3.0512 4.2449 2.7547 -1.4293 -0.0007 -0.3083 113 SER K OG  
21769 N N   . THR L 135 ? 3.3469 4.5492 3.1385 -1.3775 0.0157  -0.3412 114 THR K N   
21770 C CA  . THR L 135 ? 3.2023 4.3692 3.0461 -1.3525 0.0188  -0.3480 114 THR K CA  
21771 C C   . THR L 135 ? 3.2411 4.4038 3.1021 -1.3496 0.0152  -0.3551 114 THR K C   
21772 O O   . THR L 135 ? 3.3112 4.4387 3.1498 -1.3639 0.0029  -0.3367 114 THR K O   
21773 C CB  . THR L 135 ? 3.0519 4.1177 2.9109 -1.3443 0.0102  -0.3177 114 THR K CB  
21774 O OG1 . THR L 135 ? 2.9649 4.0381 2.8037 -1.3490 0.0120  -0.3113 114 THR K OG1 
21775 C CG2 . THR L 135 ? 2.8759 3.9094 2.7905 -1.3190 0.0181  -0.3258 114 THR K CG2 
21776 N N   . LYS L 136 ? 3.2337 4.4337 3.1354 -1.3305 0.0260  -0.3827 115 LYS K N   
21777 C CA  . LYS L 136 ? 3.1820 4.3829 3.1068 -1.3247 0.0233  -0.3937 115 LYS K CA  
21778 C C   . LYS L 136 ? 3.0738 4.2154 3.0592 -1.3006 0.0260  -0.3944 115 LYS K C   
21779 O O   . LYS L 136 ? 2.9421 4.0956 2.9602 -1.2834 0.0399  -0.4078 115 LYS K O   
21780 C CB  . LYS L 136 ? 3.1612 4.4681 3.0835 -1.3226 0.0348  -0.4299 115 LYS K CB  
21781 C CG  . LYS L 136 ? 3.0624 4.3753 3.0002 -1.3203 0.0297  -0.4406 115 LYS K CG  
21782 C CD  . LYS L 136 ? 3.0437 4.4628 2.9775 -1.3165 0.0413  -0.4762 115 LYS K CD  
21783 C CE  . LYS L 136 ? 3.1474 4.5740 3.0898 -1.3169 0.0344  -0.4855 115 LYS K CE  
21784 N NZ  . LYS L 136 ? 3.1061 4.4696 3.1052 -1.2972 0.0298  -0.4853 115 LYS K NZ  
21785 N N   . GLY L 137 ? 3.2582 4.3363 3.2602 -1.2993 0.0137  -0.3808 116 GLY K N   
21786 C CA  . GLY L 137 ? 3.1539 4.1724 3.2167 -1.2769 0.0169  -0.3814 116 GLY K CA  
21787 C C   . GLY L 137 ? 3.1254 4.2119 3.2282 -1.2611 0.0310  -0.4193 116 GLY K C   
21788 O O   . GLY L 137 ? 3.1619 4.3120 3.2489 -1.2677 0.0287  -0.4382 116 GLY K O   
21789 N N   . PRO L 138 ? 3.0948 4.1683 3.2520 -1.2389 0.0475  -0.4314 117 PRO K N   
21790 C CA  . PRO L 138 ? 3.0090 4.1484 3.2121 -1.2201 0.0640  -0.4697 117 PRO K CA  
21791 C C   . PRO L 138 ? 3.0805 4.1938 3.3192 -1.2128 0.0563  -0.4767 117 PRO K C   
21792 O O   . PRO L 138 ? 3.1283 4.1561 3.3722 -1.2165 0.0407  -0.4516 117 PRO K O   
21793 C CB  . PRO L 138 ? 2.9172 4.0244 3.1663 -1.1888 0.0866  -0.4716 117 PRO K CB  
21794 C CG  . PRO L 138 ? 2.8986 3.9031 3.1487 -1.2037 0.0768  -0.4354 117 PRO K CG  
21795 C CD  . PRO L 138 ? 2.9856 3.9848 3.1654 -1.2293 0.0543  -0.4108 117 PRO K CD  
21796 N N   . SER L 139 ? 2.9116 4.1035 3.1760 -1.2003 0.0668  -0.5131 118 SER K N   
21797 C CA  . SER L 139 ? 2.9255 4.1061 3.2311 -1.1898 0.0617  -0.5272 118 SER K CA  
21798 C C   . SER L 139 ? 2.8419 4.0136 3.2095 -1.1325 0.0878  -0.5453 118 SER K C   
21799 O O   . SER L 139 ? 2.8114 4.0557 3.1773 -1.1032 0.1050  -0.5694 118 SER K O   
21800 C CB  . SER L 139 ? 2.9745 4.2334 3.2422 -1.2008 0.0514  -0.5448 118 SER K CB  
21801 O OG  . SER L 139 ? 3.0101 4.2521 3.2105 -1.2284 0.0328  -0.5180 118 SER K OG  
21802 N N   . VAL L 140 ? 2.9261 3.9975 3.3430 -1.1060 0.0919  -0.5291 119 VAL K N   
21803 C CA  . VAL L 140 ? 2.8715 3.9029 3.3464 -1.0389 0.1189  -0.5356 119 VAL K CA  
21804 C C   . VAL L 140 ? 2.9225 3.9766 3.4417 -1.0187 0.1191  -0.5619 119 VAL K C   
21805 O O   . VAL L 140 ? 2.8786 3.9079 3.4101 -1.0462 0.0975  -0.5609 119 VAL K O   
21806 C CB  . VAL L 140 ? 2.7991 3.7092 3.3075 -1.0207 0.1246  -0.5044 119 VAL K CB  
21807 C CG1 . VAL L 140 ? 2.7421 3.6116 3.3079 -0.9496 0.1562  -0.5098 119 VAL K CG1 
21808 C CG2 . VAL L 140 ? 2.7280 3.6187 3.1896 -1.0448 0.1212  -0.4788 119 VAL K CG2 
21809 N N   . PHE L 141 ? 2.7679 3.8705 3.3104 -0.9703 0.1426  -0.5865 120 PHE K N   
21810 C CA  . PHE L 141 ? 2.7689 3.8934 3.3585 -0.9450 0.1454  -0.6130 120 PHE K CA  
21811 C C   . PHE L 141 ? 2.7369 3.8154 3.3905 -0.8752 0.1765  -0.6181 120 PHE K C   
21812 O O   . PHE L 141 ? 2.6768 3.7674 3.3240 -0.8384 0.2014  -0.6182 120 PHE K O   
21813 C CB  . PHE L 141 ? 2.7888 4.0356 3.3433 -0.9606 0.1406  -0.6440 120 PHE K CB  
21814 C CG  . PHE L 141 ? 2.8666 4.1599 3.3620 -1.0285 0.1113  -0.6406 120 PHE K CG  
21815 C CD1 . PHE L 141 ? 2.9091 4.1892 3.4106 -1.0611 0.0861  -0.6424 120 PHE K CD1 
21816 C CD2 . PHE L 141 ? 2.8941 4.2426 3.3285 -1.0589 0.1093  -0.6358 120 PHE K CD2 
21817 C CE1 . PHE L 141 ? 3.0046 4.3246 3.4498 -1.1222 0.0608  -0.6381 120 PHE K CE1 
21818 C CE2 . PHE L 141 ? 2.9712 4.3607 3.3529 -1.1213 0.0845  -0.6318 120 PHE K CE2 
21819 C CZ  . PHE L 141 ? 3.0504 4.4245 3.4360 -1.1523 0.0609  -0.6320 120 PHE K CZ  
21820 N N   . PRO L 142 ? 2.7692 3.7938 3.4857 -0.8546 0.1762  -0.6228 121 PRO K N   
21821 C CA  . PRO L 142 ? 2.7218 3.6928 3.5060 -0.7886 0.2068  -0.6258 121 PRO K CA  
21822 C C   . PRO L 142 ? 2.7058 3.7546 3.5070 -0.7465 0.2278  -0.6585 121 PRO K C   
21823 O O   . PRO L 142 ? 2.7518 3.8796 3.5433 -0.7636 0.2144  -0.6848 121 PRO K O   
21824 C CB  . PRO L 142 ? 2.7335 3.6295 3.5772 -0.7908 0.1938  -0.6227 121 PRO K CB  
21825 C CG  . PRO L 142 ? 2.7893 3.7436 3.6000 -0.8448 0.1597  -0.6361 121 PRO K CG  
21826 C CD  . PRO L 142 ? 2.7682 3.7761 3.4968 -0.8919 0.1468  -0.6255 121 PRO K CD  
21827 N N   . LEU L 143 ? 2.7514 3.7763 3.5769 -0.6898 0.2614  -0.6562 122 LEU K N   
21828 C CA  . LEU L 143 ? 2.7470 3.8333 3.5942 -0.6416 0.2858  -0.6849 122 LEU K CA  
21829 C C   . LEU L 143 ? 2.7128 3.7354 3.6461 -0.5925 0.3044  -0.6911 122 LEU K C   
21830 O O   . LEU L 143 ? 2.6731 3.6092 3.6437 -0.5537 0.3277  -0.6715 122 LEU K O   
21831 C CB  . LEU L 143 ? 2.7018 3.8086 3.5156 -0.6095 0.3113  -0.6801 122 LEU K CB  
21832 C CG  . LEU L 143 ? 2.7107 3.8912 3.4435 -0.6574 0.2930  -0.6790 122 LEU K CG  
21833 C CD1 . LEU L 143 ? 2.6889 3.8910 3.3898 -0.6236 0.3167  -0.6767 122 LEU K CD1 
21834 C CD2 . LEU L 143 ? 2.6887 3.9761 3.3951 -0.6923 0.2730  -0.7085 122 LEU K CD2 
21835 N N   . ALA L 144 ? 2.7784 3.8441 3.7437 -0.5937 0.2946  -0.7186 123 ALA K N   
21836 C CA  . ALA L 144 ? 2.7593 3.7704 3.8106 -0.5517 0.3088  -0.7279 123 ALA K CA  
21837 C C   . ALA L 144 ? 2.7797 3.7788 3.8694 -0.4818 0.3510  -0.7337 123 ALA K C   
21838 O O   . ALA L 144 ? 2.8081 3.8836 3.8639 -0.4639 0.3650  -0.7491 123 ALA K O   
21839 C CB  . ALA L 144 ? 2.7225 3.7970 3.7933 -0.5675 0.2883  -0.7598 123 ALA K CB  
21840 N N   . PRO L 145 ? 2.8470 3.7505 4.0079 -0.4406 0.3724  -0.7220 124 PRO K N   
21841 C CA  . PRO L 145 ? 2.8455 3.7296 4.0480 -0.3711 0.4151  -0.7263 124 PRO K CA  
21842 C C   . PRO L 145 ? 2.9537 3.9138 4.1869 -0.3414 0.4257  -0.7633 124 PRO K C   
21843 O O   . PRO L 145 ? 2.9692 3.9525 4.2362 -0.3576 0.4065  -0.7840 124 PRO K O   
21844 C CB  . PRO L 145 ? 2.7736 3.5349 4.0513 -0.3444 0.4297  -0.7058 124 PRO K CB  
21845 C CG  . PRO L 145 ? 2.7531 3.4645 4.0078 -0.3997 0.3975  -0.6823 124 PRO K CG  
21846 C CD  . PRO L 145 ? 2.8140 3.6169 4.0175 -0.4568 0.3595  -0.7011 124 PRO K CD  
21847 N N   . SER L 146 ? 3.0058 4.0043 4.2268 -0.2961 0.4563  -0.7721 125 SER K N   
21848 C CA  . SER L 146 ? 3.0473 4.1173 4.2971 -0.2633 0.4697  -0.8067 125 SER K CA  
21849 C C   . SER L 146 ? 3.0587 4.1150 4.3202 -0.1964 0.5141  -0.8047 125 SER K C   
21850 O O   . SER L 146 ? 3.0887 4.1925 4.2877 -0.1915 0.5218  -0.8031 125 SER K O   
21851 C CB  . SER L 146 ? 3.0433 4.2353 4.2316 -0.3037 0.4437  -0.8319 125 SER K CB  
21852 O OG  . SER L 146 ? 3.0422 4.2451 4.2231 -0.3611 0.4046  -0.8349 125 SER K OG  
21853 N N   . SER L 147 ? 2.8661 3.8580 4.2080 -0.1449 0.5428  -0.8057 126 SER K N   
21854 C CA  . SER L 147 ? 2.8268 3.7961 4.1891 -0.0759 0.5883  -0.8036 126 SER K CA  
21855 C C   . SER L 147 ? 2.7811 3.7040 4.0932 -0.0637 0.6038  -0.7725 126 SER K C   
21856 O O   . SER L 147 ? 2.7969 3.7555 4.0729 -0.0284 0.6268  -0.7762 126 SER K O   
21857 C CB  . SER L 147 ? 2.9115 3.9881 4.2545 -0.0534 0.5979  -0.8371 126 SER K CB  
21858 O OG  . SER L 147 ? 2.9577 4.0716 4.3547 -0.0551 0.5884  -0.8662 126 SER K OG  
21859 N N   . GLY L 152 ? 2.7532 3.4327 4.2934 0.2623  0.7675  -0.7491 131 GLY K N   
21860 C CA  . GLY L 152 ? 2.7587 3.3881 4.2373 0.2918  0.7841  -0.7138 131 GLY K CA  
21861 C C   . GLY L 152 ? 2.7438 3.2575 4.2521 0.2916  0.7929  -0.6801 131 GLY K C   
21862 O O   . GLY L 152 ? 2.7622 3.2114 4.2228 0.3224  0.8047  -0.6431 131 GLY K O   
21863 N N   . GLY L 153 ? 2.8611 3.3493 4.4472 0.2565  0.7850  -0.6928 132 GLY K N   
21864 C CA  . GLY L 153 ? 2.8474 3.2249 4.4669 0.2516  0.7905  -0.6614 132 GLY K CA  
21865 C C   . GLY L 153 ? 2.7680 3.1576 4.3855 0.2207  0.7993  -0.6677 132 GLY K C   
21866 O O   . GLY L 153 ? 2.7494 3.0463 4.3948 0.2141  0.8035  -0.6416 132 GLY K O   
21867 N N   . THR L 154 ? 2.7938 3.2843 4.3437 0.1921  0.7838  -0.6864 133 THR K N   
21868 C CA  . THR L 154 ? 2.7489 3.2453 4.2204 0.1430  0.7540  -0.6667 133 THR K CA  
21869 C C   . THR L 154 ? 2.7208 3.3056 4.1569 0.0725  0.7044  -0.6874 133 THR K C   
21870 O O   . THR L 154 ? 2.7371 3.3914 4.1967 0.0668  0.6952  -0.7188 133 THR K O   
21871 C CB  . THR L 154 ? 2.7469 3.2765 4.1423 0.1713  0.7715  -0.6601 133 THR K CB  
21872 O OG1 . THR L 154 ? 2.7661 3.4038 4.1373 0.1844  0.7737  -0.6936 133 THR K OG1 
21873 C CG2 . THR L 154 ? 2.7754 3.2110 4.2002 0.2412  0.8203  -0.6365 133 THR K CG2 
21874 N N   . ALA L 155 ? 2.6780 3.2587 4.0571 0.0188  0.6729  -0.6692 134 ALA K N   
21875 C CA  . ALA L 155 ? 2.6552 3.3136 3.9948 -0.0501 0.6264  -0.6849 134 ALA K CA  
21876 C C   . ALA L 155 ? 2.6150 3.2910 3.8677 -0.0923 0.6040  -0.6660 134 ALA K C   
21877 O O   . ALA L 155 ? 2.5962 3.1997 3.8336 -0.0780 0.6173  -0.6361 134 ALA K O   
21878 C CB  . ALA L 155 ? 2.6523 3.2644 4.0505 -0.0851 0.6020  -0.6847 134 ALA K CB  
21879 N N   . ALA L 156 ? 2.5707 3.3436 3.7679 -0.1439 0.5702  -0.6841 135 ALA K N   
21880 C CA  . ALA L 156 ? 2.5322 3.3363 3.6473 -0.1905 0.5454  -0.6709 135 ALA K CA  
21881 C C   . ALA L 156 ? 2.5108 3.3005 3.6202 -0.2591 0.5046  -0.6623 135 ALA K C   
21882 O O   . ALA L 156 ? 2.5297 3.3353 3.6779 -0.2790 0.4877  -0.6793 135 ALA K O   
21883 C CB  . ALA L 156 ? 2.5351 3.4619 3.5876 -0.1993 0.5386  -0.6972 135 ALA K CB  
21884 N N   . LEU L 157 ? 2.7560 3.5163 3.8154 -0.2944 0.4883  -0.6362 136 LEU K N   
21885 C CA  . LEU L 157 ? 2.7336 3.4746 3.7810 -0.3595 0.4503  -0.6246 136 LEU K CA  
21886 C C   . LEU L 157 ? 2.6865 3.4416 3.6557 -0.3992 0.4327  -0.6051 136 LEU K C   
21887 O O   . LEU L 157 ? 2.6647 3.3834 3.6132 -0.3697 0.4531  -0.5866 136 LEU K O   
21888 C CB  . LEU L 157 ? 2.7337 3.3574 3.8500 -0.3495 0.4551  -0.6036 136 LEU K CB  
21889 C CG  . LEU L 157 ? 2.7417 3.3353 3.8672 -0.4079 0.4179  -0.5961 136 LEU K CG  
21890 C CD1 . LEU L 157 ? 2.8301 3.3328 4.0451 -0.3824 0.4284  -0.5920 136 LEU K CD1 
21891 C CD2 . LEU L 157 ? 2.6639 3.2173 3.7359 -0.4489 0.3996  -0.5647 136 LEU K CD2 
21892 N N   . GLY L 158 ? 2.7486 3.5542 3.6754 -0.4645 0.3957  -0.6091 137 GLY K N   
21893 C CA  . GLY L 158 ? 2.6994 3.5214 3.5544 -0.5051 0.3783  -0.5919 137 GLY K CA  
21894 C C   . GLY L 158 ? 2.6713 3.5203 3.4944 -0.5789 0.3374  -0.5902 137 GLY K C   
21895 O O   . GLY L 158 ? 2.6898 3.5388 3.5462 -0.5985 0.3212  -0.6013 137 GLY K O   
21896 N N   . CYS L 159 ? 2.7515 3.6263 3.5080 -0.6188 0.3211  -0.5773 138 CYS K N   
21897 C CA  . CYS L 159 ? 2.7257 3.6301 3.4406 -0.6910 0.2838  -0.5733 138 CYS K CA  
21898 C C   . CYS L 159 ? 2.7360 3.7509 3.3830 -0.7183 0.2747  -0.5898 138 CYS K C   
21899 O O   . CYS L 159 ? 2.7369 3.7995 3.3703 -0.6810 0.2961  -0.6033 138 CYS K O   
21900 C CB  . CYS L 159 ? 2.7558 3.5694 3.4592 -0.7193 0.2710  -0.5366 138 CYS K CB  
21901 S SG  . CYS L 159 ? 3.3794 4.0590 4.1630 -0.6957 0.2776  -0.5160 138 CYS K SG  
21902 N N   . LEU L 160 ? 2.7246 3.7801 3.3289 -0.7832 0.2434  -0.5888 139 LEU K N   
21903 C CA  . LEU L 160 ? 2.6614 3.8215 3.2025 -0.8160 0.2330  -0.6039 139 LEU K CA  
21904 C C   . LEU L 160 ? 2.6990 3.8552 3.1910 -0.8830 0.2041  -0.5842 139 LEU K C   
21905 O O   . LEU L 160 ? 2.7137 3.8430 3.2131 -0.9212 0.1818  -0.5772 139 LEU K O   
21906 C CB  . LEU L 160 ? 2.6591 3.9166 3.2014 -0.8210 0.2284  -0.6393 139 LEU K CB  
21907 C CG  . LEU L 160 ? 2.6734 4.0381 3.1506 -0.8653 0.2137  -0.6540 139 LEU K CG  
21908 C CD1 . LEU L 160 ? 2.5659 4.0246 3.0445 -0.8379 0.2270  -0.6887 139 LEU K CD1 
21909 C CD2 . LEU L 160 ? 2.7808 4.1720 3.2308 -0.9321 0.1815  -0.6529 139 LEU K CD2 
21910 N N   . VAL L 161 ? 2.8073 3.9875 3.2511 -0.8957 0.2046  -0.5754 140 VAL K N   
21911 C CA  . VAL L 161 ? 2.8411 4.0275 3.2344 -0.9592 0.1792  -0.5580 140 VAL K CA  
21912 C C   . VAL L 161 ? 2.9015 4.2081 3.2448 -0.9922 0.1703  -0.5820 140 VAL K C   
21913 O O   . VAL L 161 ? 2.8994 4.2579 3.2198 -0.9714 0.1841  -0.5932 140 VAL K O   
21914 C CB  . VAL L 161 ? 2.7810 3.9015 3.1586 -0.9526 0.1847  -0.5291 140 VAL K CB  
21915 C CG1 . VAL L 161 ? 2.8000 3.9281 3.1284 -1.0195 0.1582  -0.5120 140 VAL K CG1 
21916 C CG2 . VAL L 161 ? 2.7610 3.7627 3.1898 -0.9181 0.1955  -0.5057 140 VAL K CG2 
21917 N N   . LYS L 162 ? 2.7278 4.0796 3.0533 -1.0424 0.1479  -0.5905 141 LYS K N   
21918 C CA  . LYS L 162 ? 2.7891 4.2566 3.0718 -1.0727 0.1410  -0.6150 141 LYS K CA  
21919 C C   . LYS L 162 ? 2.8701 4.3553 3.0999 -1.1393 0.1186  -0.5995 141 LYS K C   
21920 O O   . LYS L 162 ? 2.8582 4.2884 3.0852 -1.1774 0.0993  -0.5786 141 LYS K O   
21921 C CB  . LYS L 162 ? 2.8281 4.3431 3.1287 -1.0777 0.1341  -0.6393 141 LYS K CB  
21922 C CG  . LYS L 162 ? 2.8802 4.5144 3.1416 -1.1074 0.1274  -0.6663 141 LYS K CG  
21923 C CD  . LYS L 162 ? 2.9708 4.6331 3.2537 -1.1115 0.1185  -0.6858 141 LYS K CD  
21924 C CE  . LYS L 162 ? 3.0068 4.7849 3.2503 -1.1432 0.1111  -0.7116 141 LYS K CE  
21925 N NZ  . LYS L 162 ? 2.9243 4.7812 3.1632 -1.1076 0.1321  -0.7374 141 LYS K NZ  
21926 N N   . ASP L 163 ? 3.7218 3.5269 3.0551 -1.8169 -0.2249 0.4768  142 ASP K N   
21927 C CA  . ASP L 163 ? 3.8266 3.6175 3.0977 -1.8408 -0.2246 0.5098  142 ASP K CA  
21928 C C   . ASP L 163 ? 3.8497 3.5118 3.1008 -1.8218 -0.1871 0.5557  142 ASP K C   
21929 O O   . ASP L 163 ? 3.8132 3.4951 3.1028 -1.8182 -0.1801 0.5949  142 ASP K O   
21930 C CB  . ASP L 163 ? 3.8700 3.8187 3.1652 -1.8709 -0.2594 0.5195  142 ASP K CB  
21931 C CG  . ASP L 163 ? 3.9419 3.9959 3.2171 -1.8890 -0.2941 0.4737  142 ASP K CG  
21932 O OD1 . ASP L 163 ? 3.8938 3.9307 3.1709 -1.8735 -0.2953 0.4309  142 ASP K OD1 
21933 O OD2 . ASP L 163 ? 4.0580 4.1955 3.3039 -1.9163 -0.3168 0.4813  142 ASP K OD2 
21934 N N   . TYR L 164 ? 4.1051 3.6381 3.2953 -1.8066 -0.1629 0.5498  143 TYR K N   
21935 C CA  . TYR L 164 ? 4.1424 3.5537 3.3093 -1.7830 -0.1272 0.5874  143 TYR K CA  
21936 C C   . TYR L 164 ? 4.2215 3.5538 3.3024 -1.7888 -0.1204 0.5779  143 TYR K C   
21937 O O   . TYR L 164 ? 4.2132 3.5624 3.2552 -1.8038 -0.1372 0.5404  143 TYR K O   
21938 C CB  . TYR L 164 ? 4.0747 3.3896 3.2880 -1.7363 -0.0927 0.5921  143 TYR K CB  
21939 C CG  . TYR L 164 ? 4.0271 3.2638 3.2199 -1.7146 -0.0810 0.5530  143 TYR K CG  
21940 C CD1 . TYR L 164 ? 3.8897 3.1839 3.1197 -1.7157 -0.0984 0.5141  143 TYR K CD1 
21941 C CD2 . TYR L 164 ? 4.0692 3.1786 3.2107 -1.6902 -0.0524 0.5542  143 TYR K CD2 
21942 C CE1 . TYR L 164 ? 3.8173 3.0418 3.0292 -1.6947 -0.0877 0.4782  143 TYR K CE1 
21943 C CE2 . TYR L 164 ? 3.9886 3.0309 3.1127 -1.6690 -0.0421 0.5189  143 TYR K CE2 
21944 C CZ  . TYR L 164 ? 3.8828 2.9810 3.0408 -1.6716 -0.0595 0.4816  143 TYR K CZ  
21945 O OH  . TYR L 164 ? 3.8747 2.9075 3.0160 -1.6492 -0.0490 0.4469  143 TYR K OH  
21946 N N   . PHE L 165 ? 4.1040 3.3515 3.1583 -1.7745 -0.0951 0.6116  144 PHE K N   
21947 C CA  . PHE L 165 ? 4.2372 3.4086 3.2151 -1.7777 -0.0870 0.6066  144 PHE K CA  
21948 C C   . PHE L 165 ? 4.2914 3.3561 3.2644 -1.7459 -0.0505 0.6429  144 PHE K C   
21949 O O   . PHE L 165 ? 4.2484 3.3363 3.2527 -1.7442 -0.0449 0.6802  144 PHE K O   
21950 C CB  . PHE L 165 ? 4.3166 3.5813 3.2491 -1.8256 -0.1211 0.6057  144 PHE K CB  
21951 C CG  . PHE L 165 ? 4.4395 3.6400 3.2921 -1.8346 -0.1181 0.5972  144 PHE K CG  
21952 C CD1 . PHE L 165 ? 4.3945 3.5822 3.2026 -1.8423 -0.1285 0.5558  144 PHE K CD1 
21953 C CD2 . PHE L 165 ? 4.5340 3.6907 3.3576 -1.8352 -0.1055 0.6304  144 PHE K CD2 
21954 C CE1 . PHE L 165 ? 4.4611 3.5922 3.1961 -1.8511 -0.1264 0.5482  144 PHE K CE1 
21955 C CE2 . PHE L 165 ? 4.5940 3.6949 3.3473 -1.8438 -0.1036 0.6220  144 PHE K CE2 
21956 C CZ  . PHE L 165 ? 4.5594 3.6475 3.2679 -1.8523 -0.1144 0.5811  144 PHE K CZ  
21957 N N   . PRO L 166 ? 4.5507 3.5027 3.4870 -1.7191 -0.0258 0.6316  145 PRO K N   
21958 C CA  . PRO L 166 ? 4.5061 3.4268 3.4066 -1.7177 -0.0306 0.5882  145 PRO K CA  
21959 C C   . PRO L 166 ? 4.4167 3.2715 3.3601 -1.6744 -0.0064 0.5729  145 PRO K C   
21960 O O   . PRO L 166 ? 4.3358 3.1870 3.3415 -1.6506 0.0089  0.5931  145 PRO K O   
21961 C CB  . PRO L 166 ? 4.5283 3.3693 3.3624 -1.7150 -0.0181 0.5909  145 PRO K CB  
21962 C CG  . PRO L 166 ? 4.5494 3.3274 3.4099 -1.6847 0.0131  0.6326  145 PRO K CG  
21963 C CD  . PRO L 166 ? 4.5714 3.4296 3.4894 -1.6941 0.0047  0.6610  145 PRO K CD  
21964 N N   . GLU L 167 ? 4.2881 3.0930 3.1987 -1.6640 -0.0032 0.5379  146 GLU K N   
21965 C CA  . GLU L 167 ? 4.1663 2.9047 3.1126 -1.6215 0.0198  0.5212  146 GLU K CA  
21966 C C   . GLU L 167 ? 4.2044 2.8365 3.1674 -1.5750 0.0599  0.5494  146 GLU K C   
21967 O O   . GLU L 167 ? 4.2579 2.8530 3.1867 -1.5762 0.0696  0.5713  146 GLU K O   
21968 C CB  . GLU L 167 ? 4.1507 2.8672 3.0514 -1.6240 0.0114  0.4769  146 GLU K CB  
21969 C CG  . GLU L 167 ? 4.0928 2.9131 2.9907 -1.6599 -0.0251 0.4428  146 GLU K CG  
21970 C CD  . GLU L 167 ? 4.0293 2.8749 2.9928 -1.6409 -0.0253 0.4227  146 GLU K CD  
21971 O OE1 . GLU L 167 ? 4.0148 2.8560 3.0406 -1.6201 -0.0108 0.4463  146 GLU K OE1 
21972 O OE2 . GLU L 167 ? 3.9933 2.8641 2.9471 -1.6459 -0.0398 0.3827  146 GLU K OE2 
21973 N N   . PRO L 168 ? 4.4096 2.9959 3.4285 -1.5329 0.0832  0.5489  147 PRO K N   
21974 C CA  . PRO L 168 ? 4.3124 2.9359 3.3814 -1.5259 0.0754  0.5257  147 PRO K CA  
21975 C C   . PRO L 168 ? 4.2432 2.9008 3.3872 -1.5141 0.0822  0.5527  147 PRO K C   
21976 O O   . PRO L 168 ? 4.1959 2.8629 3.3506 -1.5174 0.0887  0.5900  147 PRO K O   
21977 C CB  . PRO L 168 ? 4.2583 2.7897 3.3309 -1.4814 0.1007  0.5066  147 PRO K CB  
21978 C CG  . PRO L 168 ? 4.2846 2.7351 3.3557 -1.4497 0.1320  0.5404  147 PRO K CG  
21979 C CD  . PRO L 168 ? 4.3831 2.8643 3.4105 -1.4848 0.1200  0.5636  147 PRO K CD  
21980 N N   . VAL L 169 ? 4.1505 2.8266 3.3468 -1.4996 0.0808  0.5333  148 VAL K N   
21981 C CA  . VAL L 169 ? 4.0950 2.7977 3.3671 -1.4841 0.0886  0.5549  148 VAL K CA  
21982 C C   . VAL L 169 ? 4.0278 2.6716 3.3482 -1.4385 0.1106  0.5390  148 VAL K C   
21983 O O   . VAL L 169 ? 3.9879 2.6467 3.3079 -1.4413 0.0978  0.5003  148 VAL K O   
21984 C CB  . VAL L 169 ? 4.0637 2.8941 3.3627 -1.5266 0.0522  0.5479  148 VAL K CB  
21985 C CG1 . VAL L 169 ? 3.9901 2.8435 3.3720 -1.5061 0.0596  0.5588  148 VAL K CG1 
21986 C CG2 . VAL L 169 ? 4.1279 3.0180 3.3988 -1.5630 0.0359  0.5764  148 VAL K CG2 
21987 N N   . THR L 170 ? 4.1275 2.7078 3.4917 -1.3956 0.1431  0.5685  149 THR K N   
21988 C CA  . THR L 170 ? 4.0685 2.5944 3.4857 -1.3486 0.1654  0.5586  149 THR K CA  
21989 C C   . THR L 170 ? 4.0025 2.5895 3.4906 -1.3505 0.1569  0.5598  149 THR K C   
21990 O O   . THR L 170 ? 4.0032 2.6229 3.5227 -1.3561 0.1591  0.5926  149 THR K O   
21991 C CB  . THR L 170 ? 4.0861 2.5218 3.5225 -1.2995 0.2030  0.5895  149 THR K CB  
21992 O OG1 . THR L 170 ? 4.1046 2.5566 3.5684 -1.2998 0.2126  0.6314  149 THR K OG1 
21993 C CG2 . THR L 170 ? 4.1451 2.5244 3.5170 -1.2968 0.2098  0.5860  149 THR K CG2 
21994 N N   . VAL L 171 ? 3.9172 2.5216 3.4322 -1.3455 0.1471  0.5241  150 VAL K N   
21995 C CA  . VAL L 171 ? 3.8572 2.5251 3.4425 -1.3486 0.1359  0.5193  150 VAL K CA  
21996 C C   . VAL L 171 ? 3.8342 2.4394 3.4748 -1.2977 0.1603  0.5096  150 VAL K C   
21997 O O   . VAL L 171 ? 3.8238 2.3947 3.4505 -1.2824 0.1614  0.4768  150 VAL K O   
21998 C CB  . VAL L 171 ? 3.8043 2.5785 3.3837 -1.3947 0.0944  0.4824  150 VAL K CB  
21999 C CG1 . VAL L 171 ? 3.7366 2.5801 3.3984 -1.3945 0.0823  0.4750  150 VAL K CG1 
22000 C CG2 . VAL L 171 ? 3.8210 2.6700 3.3538 -1.4443 0.0681  0.4942  150 VAL K CG2 
22001 N N   . SER L 172 ? 3.8514 2.4442 3.5555 -1.2708 0.1793  0.5386  151 SER K N   
22002 C CA  . SER L 172 ? 3.8255 2.3678 3.5924 -1.2217 0.2015  0.5343  151 SER K CA  
22003 C C   . SER L 172 ? 3.7692 2.3803 3.6057 -1.2309 0.1891  0.5330  151 SER K C   
22004 O O   . SER L 172 ? 3.7564 2.4485 3.5977 -1.2692 0.1677  0.5455  151 SER K O   
22005 C CB  . SER L 172 ? 3.8660 2.3240 3.6534 -1.1724 0.2384  0.5721  151 SER K CB  
22006 O OG  . SER L 172 ? 3.8858 2.3623 3.6903 -1.1784 0.2468  0.6130  151 SER K OG  
22007 N N   . TRP L 173 ? 3.7390 2.3229 3.6334 -1.1949 0.2007  0.5183  152 TRP K N   
22008 C CA  . TRP L 173 ? 3.6819 2.3255 3.6487 -1.1987 0.1898  0.5124  152 TRP K CA  
22009 C C   . TRP L 173 ? 3.6675 2.2523 3.6995 -1.1474 0.2232  0.5415  152 TRP K C   
22010 O O   . TRP L 173 ? 3.6701 2.1784 3.7166 -1.1003 0.2456  0.5415  152 TRP K O   
22011 C CB  . TRP L 173 ? 3.6399 2.3218 3.6216 -1.2077 0.1671  0.4614  152 TRP K CB  
22012 C CG  . TRP L 173 ? 3.6447 2.4112 3.5767 -1.2621 0.1290  0.4335  152 TRP K CG  
22013 C CD1 . TRP L 173 ? 3.6879 2.4324 3.5428 -1.2767 0.1236  0.4184  152 TRP K CD1 
22014 C CD2 . TRP L 173 ? 3.5996 2.4952 3.5645 -1.3055 0.0889  0.4139  152 TRP K CD2 
22015 N NE1 . TRP L 173 ? 3.6780 2.5261 3.5117 -1.3267 0.0844  0.3927  152 TRP K NE1 
22016 C CE2 . TRP L 173 ? 3.6211 2.5682 3.5246 -1.3441 0.0617  0.3887  152 TRP K CE2 
22017 C CE3 . TRP L 173 ? 3.5406 2.5218 3.5864 -1.3140 0.0716  0.4156  152 TRP K CE3 
22018 C CZ2 . TRP L 173 ? 3.5843 2.6695 3.5074 -1.3877 0.0184  0.3642  152 TRP K CZ2 
22019 C CZ3 . TRP L 173 ? 3.4995 2.6227 3.5684 -1.3579 0.0268  0.3913  152 TRP K CZ3 
22020 C CH2 . TRP L 173 ? 3.5210 2.6967 3.5296 -1.3927 0.0011  0.3652  152 TRP K CH2 
22021 N N   . ASN L 174 ? 3.7194 2.3499 3.7944 -1.1571 0.2220  0.5673  153 ASN K N   
22022 C CA  . ASN L 174 ? 3.7402 2.3258 3.8784 -1.1126 0.2533  0.5972  153 ASN K CA  
22023 C C   . ASN L 174 ? 3.7784 2.2746 3.9032 -1.0697 0.2868  0.6303  153 ASN K C   
22024 O O   . ASN L 174 ? 3.7963 2.2391 3.9745 -1.0187 0.3059  0.6432  153 ASN K O   
22025 C CB  . ASN L 174 ? 3.6622 2.2372 3.8668 -1.0821 0.2569  0.5709  153 ASN K CB  
22026 C CG  . ASN L 174 ? 3.6396 2.2939 3.9028 -1.1027 0.2394  0.5669  153 ASN K CG  
22027 O OD1 . ASN L 174 ? 3.6950 2.3895 3.9700 -1.1186 0.2362  0.5985  153 ASN K OD1 
22028 N ND2 . ASN L 174 ? 3.5508 2.2351 3.8566 -1.1013 0.2234  0.5293  153 ASN K ND2 
22029 N N   . SER L 175 ? 3.5776 2.0701 3.6388 -1.0917 0.2854  0.6470  154 SER K N   
22030 C CA  . SER L 175 ? 3.6274 2.0502 3.6750 -1.0580 0.3099  0.6786  154 SER K CA  
22031 C C   . SER L 175 ? 3.6236 1.9889 3.6752 -1.0210 0.3115  0.6631  154 SER K C   
22032 O O   . SER L 175 ? 3.6410 1.9579 3.7174 -0.9814 0.3221  0.6908  154 SER K O   
22033 C CB  . SER L 175 ? 3.6359 2.0408 3.7418 -1.0258 0.3356  0.7226  154 SER K CB  
22034 O OG  . SER L 175 ? 3.5934 1.9819 3.7797 -0.9843 0.3412  0.7241  154 SER K OG  
22035 N N   . GLY L 176 ? 3.6758 2.0547 3.7022 -1.0368 0.2936  0.6193  155 GLY K N   
22036 C CA  . GLY L 176 ? 3.6712 2.0033 3.6904 -1.0078 0.2911  0.5985  155 GLY K CA  
22037 C C   . GLY L 176 ? 3.6218 1.9438 3.7104 -0.9707 0.2861  0.5879  155 GLY K C   
22038 O O   . GLY L 176 ? 3.6207 1.9014 3.7065 -0.9409 0.2806  0.5785  155 GLY K O   
22039 N N   . ALA L 177 ? 3.7236 2.0841 3.8712 -0.9728 0.2843  0.5887  156 ALA K N   
22040 C CA  . ALA L 177 ? 3.6965 2.0511 3.9091 -0.9402 0.2715  0.5804  156 ALA K CA  
22041 C C   . ALA L 177 ? 3.6374 2.0255 3.8477 -0.9585 0.2589  0.5276  156 ALA K C   
22042 O O   . ALA L 177 ? 3.6036 2.0042 3.8707 -0.9419 0.2464  0.5167  156 ALA K O   
22043 C CB  . ALA L 177 ? 3.6904 2.0708 3.9643 -0.9271 0.2701  0.6093  156 ALA K CB  
22044 N N   . LEU L 178 ? 3.6356 2.0420 3.7779 -0.9947 0.2535  0.4960  157 LEU K N   
22045 C CA  . LEU L 178 ? 3.5804 2.0275 3.7171 -1.0161 0.2342  0.4451  157 LEU K CA  
22046 C C   . LEU L 178 ? 3.5950 2.0322 3.6473 -1.0384 0.2258  0.4209  157 LEU K C   
22047 O O   . LEU L 178 ? 3.6018 2.0764 3.5995 -1.0831 0.2150  0.4205  157 LEU K O   
22048 C CB  . LEU L 178 ? 3.5282 2.0617 3.6894 -1.0594 0.2177  0.4311  157 LEU K CB  
22049 C CG  . LEU L 178 ? 3.4649 2.0570 3.6365 -1.0811 0.1910  0.3779  157 LEU K CG  
22050 C CD1 . LEU L 178 ? 3.4077 2.0688 3.6565 -1.0913 0.1790  0.3701  157 LEU K CD1 
22051 C CD2 . LEU L 178 ? 3.4728 2.1226 3.5736 -1.1337 0.1637  0.3535  157 LEU K CD2 
22052 N N   . THR L 179 ? 3.7044 2.0947 3.7462 -1.0074 0.2274  0.4031  158 THR K N   
22053 C CA  . THR L 179 ? 3.7197 2.0929 3.6848 -1.0218 0.2221  0.3798  158 THR K CA  
22054 C C   . THR L 179 ? 3.6751 2.0693 3.6380 -1.0242 0.2058  0.3296  158 THR K C   
22055 O O   . THR L 179 ? 3.6849 2.0662 3.5867 -1.0340 0.2003  0.3069  158 THR K O   
22056 C CB  . THR L 179 ? 3.7745 2.0744 3.7186 -0.9844 0.2383  0.4040  158 THR K CB  
22057 O OG1 . THR L 179 ? 3.7883 2.0719 3.6576 -0.9992 0.2340  0.3800  158 THR K OG1 
22058 C CG2 . THR L 179 ? 3.7776 2.0438 3.7795 -0.9328 0.2391  0.4058  158 THR K CG2 
22059 N N   . SER L 180 ? 3.5721 1.9992 3.6013 -1.0148 0.1976  0.3117  159 SER K N   
22060 C CA  . SER L 180 ? 3.5477 1.9994 3.5869 -1.0129 0.1816  0.2639  159 SER K CA  
22061 C C   . SER L 180 ? 3.5210 2.0658 3.5584 -1.0644 0.1556  0.2313  159 SER K C   
22062 O O   . SER L 180 ? 3.4897 2.0884 3.5781 -1.0805 0.1484  0.2380  159 SER K O   
22063 C CB  . SER L 180 ? 3.5203 1.9530 3.6368 -0.9670 0.1837  0.2638  159 SER K CB  
22064 O OG  . SER L 180 ? 3.4917 1.9575 3.6719 -0.9711 0.1837  0.2825  159 SER K OG  
22065 N N   . GLY L 181 ? 3.4603 2.0321 3.4410 -1.0903 0.1380  0.1967  160 GLY K N   
22066 C CA  . GLY L 181 ? 3.4189 2.0934 3.3969 -1.1380 0.1048  0.1628  160 GLY K CA  
22067 C C   . GLY L 181 ? 3.4487 2.1730 3.3734 -1.1880 0.0894  0.1784  160 GLY K C   
22068 O O   . GLY L 181 ? 3.4069 2.2363 3.3430 -1.2275 0.0570  0.1563  160 GLY K O   
22069 N N   . VAL L 182 ? 3.4198 2.0806 3.2917 -1.1856 0.1089  0.2154  161 VAL K N   
22070 C CA  . VAL L 182 ? 3.4540 2.1545 3.2733 -1.2301 0.0961  0.2352  161 VAL K CA  
22071 C C   . VAL L 182 ? 3.4786 2.1793 3.2151 -1.2521 0.0831  0.2120  161 VAL K C   
22072 O O   . VAL L 182 ? 3.5118 2.1332 3.2101 -1.2247 0.1015  0.2093  161 VAL K O   
22073 C CB  . VAL L 182 ? 3.5119 2.1460 3.3236 -1.2134 0.1246  0.2886  161 VAL K CB  
22074 C CG1 . VAL L 182 ? 3.4869 2.1523 3.3722 -1.2094 0.1286  0.3145  161 VAL K CG1 
22075 C CG2 . VAL L 182 ? 3.5447 2.0721 3.3508 -1.1604 0.1562  0.2998  161 VAL K CG2 
22076 N N   . HIS L 183 ? 3.7780 2.5754 3.4906 -1.3001 0.0496  0.1943  162 HIS K N   
22077 C CA  . HIS L 183 ? 3.7976 2.6078 3.4320 -1.3249 0.0340  0.1724  162 HIS K CA  
22078 C C   . HIS L 183 ? 3.8307 2.7024 3.4263 -1.3715 0.0153  0.1944  162 HIS K C   
22079 O O   . HIS L 183 ? 3.8020 2.7884 3.4255 -1.4040 -0.0163 0.1820  162 HIS K O   
22080 C CB  . HIS L 183 ? 3.7581 2.6383 3.4073 -1.3303 0.0076  0.1189  162 HIS K CB  
22081 C CG  . HIS L 183 ? 3.7562 2.5707 3.4294 -1.2849 0.0256  0.0966  162 HIS K CG  
22082 N ND1 . HIS L 183 ? 3.7802 2.5136 3.3975 -1.2635 0.0424  0.0905  162 HIS K ND1 
22083 C CD2 . HIS L 183 ? 3.7411 2.5641 3.4905 -1.2561 0.0282  0.0791  162 HIS K CD2 
22084 C CE1 . HIS L 183 ? 3.7491 2.4460 3.4074 -1.2231 0.0542  0.0717  162 HIS K CE1 
22085 N NE2 . HIS L 183 ? 3.7301 2.4777 3.4681 -1.2177 0.0462  0.0644  162 HIS K NE2 
22086 N N   . THR L 184 ? 3.7883 2.5895 3.3238 -1.3719 0.0338  0.2265  163 THR K N   
22087 C CA  . THR L 184 ? 3.8340 2.6783 3.3255 -1.4123 0.0200  0.2513  163 THR K CA  
22088 C C   . THR L 184 ? 3.8740 2.7457 3.2897 -1.4419 -0.0008 0.2256  163 THR K C   
22089 O O   . THR L 184 ? 3.9073 2.7021 3.2722 -1.4244 0.0140  0.2156  163 THR K O   
22090 C CB  . THR L 184 ? 3.8826 2.6389 3.3545 -1.3941 0.0513  0.2997  163 THR K CB  
22091 O OG1 . THR L 184 ? 3.8701 2.6075 3.4150 -1.3657 0.0702  0.3244  163 THR K OG1 
22092 C CG2 . THR L 184 ? 3.9256 2.7288 3.3538 -1.4356 0.0363  0.3254  163 THR K CG2 
22093 N N   . PHE L 185 ? 3.9807 2.9732 3.3917 -1.4865 -0.0375 0.2142  164 PHE K N   
22094 C CA  . PHE L 185 ? 3.9927 3.0305 3.3386 -1.5158 -0.0611 0.1889  164 PHE K CA  
22095 C C   . PHE L 185 ? 4.0539 3.0684 3.3280 -1.5421 -0.0592 0.2204  164 PHE K C   
22096 O O   . PHE L 185 ? 4.0910 3.1092 3.3773 -1.5515 -0.0536 0.2596  164 PHE K O   
22097 C CB  . PHE L 185 ? 3.9377 3.1247 3.3219 -1.5425 -0.1013 0.1593  164 PHE K CB  
22098 C CG  . PHE L 185 ? 3.8821 3.1070 3.3323 -1.5176 -0.1089 0.1195  164 PHE K CG  
22099 C CD1 . PHE L 185 ? 3.8328 3.0846 3.3690 -1.5018 -0.1064 0.1251  164 PHE K CD1 
22100 C CD2 . PHE L 185 ? 3.8526 3.0915 3.2804 -1.5089 -0.1194 0.0759  164 PHE K CD2 
22101 C CE1 . PHE L 185 ? 3.7495 3.0385 3.3483 -1.4776 -0.1145 0.0866  164 PHE K CE1 
22102 C CE2 . PHE L 185 ? 3.7848 3.0611 3.2750 -1.4829 -0.1267 0.0385  164 PHE K CE2 
22103 C CZ  . PHE L 185 ? 3.7308 3.0324 3.3069 -1.4675 -0.1248 0.0430  164 PHE K CZ  
22104 N N   . PRO L 186 ? 3.9288 2.9198 3.1298 -1.5518 -0.0636 0.2022  165 PRO K N   
22105 C CA  . PRO L 186 ? 3.9900 2.9643 3.1180 -1.5786 -0.0652 0.2257  165 PRO K CA  
22106 C C   . PRO L 186 ? 3.9677 3.0637 3.0972 -1.6227 -0.0979 0.2334  165 PRO K C   
22107 O O   . PRO L 186 ? 3.9025 3.1091 3.0658 -1.6366 -0.1267 0.2051  165 PRO K O   
22108 C CB  . PRO L 186 ? 4.0087 2.9467 3.0688 -1.5776 -0.0668 0.1950  165 PRO K CB  
22109 C CG  . PRO L 186 ? 3.9399 2.9297 3.0402 -1.5651 -0.0804 0.1516  165 PRO K CG  
22110 C CD  . PRO L 186 ? 3.9058 2.8834 3.0891 -1.5365 -0.0667 0.1588  165 PRO K CD  
22111 N N   . ALA L 187 ? 4.0677 3.1471 3.1636 -1.6409 -0.0932 0.2717  166 ALA K N   
22112 C CA  . ALA L 187 ? 4.0968 3.2903 3.1951 -1.6810 -0.1225 0.2845  166 ALA K CA  
22113 C C   . ALA L 187 ? 4.1283 3.3926 3.1729 -1.7102 -0.1515 0.2539  166 ALA K C   
22114 O O   . ALA L 187 ? 4.1843 3.3964 3.1792 -1.7019 -0.1462 0.2287  166 ALA K O   
22115 C CB  . ALA L 187 ? 4.1603 3.3119 3.2334 -1.6902 -0.1085 0.3336  166 ALA K CB  
22116 N N   . VAL L 188 ? 3.9642 3.3521 3.0209 -1.7421 -0.1817 0.2573  167 VAL K N   
22117 C CA  . VAL L 188 ? 3.9904 3.4628 3.0023 -1.7686 -0.2103 0.2332  167 VAL K CA  
22118 C C   . VAL L 188 ? 4.0765 3.5830 3.0496 -1.8033 -0.2207 0.2682  167 VAL K C   
22119 O O   . VAL L 188 ? 4.0859 3.6374 3.1018 -1.8119 -0.2242 0.2988  167 VAL K O   
22120 C CB  . VAL L 188 ? 3.9148 3.5248 2.9867 -1.7654 -0.2395 0.1969  167 VAL K CB  
22121 C CG1 . VAL L 188 ? 3.8636 3.5567 3.0149 -1.7674 -0.2497 0.2157  167 VAL K CG1 
22122 C CG2 . VAL L 188 ? 3.9580 3.6605 2.9861 -1.7874 -0.2662 0.1788  167 VAL K CG2 
22123 N N   . LEU L 189 ? 4.0299 3.5129 2.9232 -1.8221 -0.2248 0.2654  168 LEU K N   
22124 C CA  . LEU L 189 ? 4.1844 3.7007 3.0379 -1.8554 -0.2359 0.2969  168 LEU K CA  
22125 C C   . LEU L 189 ? 4.1487 3.8228 3.0218 -1.8783 -0.2718 0.2830  168 LEU K C   
22126 O O   . LEU L 189 ? 4.1515 3.8721 2.9942 -1.8820 -0.2866 0.2513  168 LEU K O   
22127 C CB  . LEU L 189 ? 4.2768 3.7122 3.0384 -1.8661 -0.2277 0.2976  168 LEU K CB  
22128 C CG  . LEU L 189 ? 4.3104 3.7694 3.0229 -1.9001 -0.2384 0.3283  168 LEU K CG  
22129 C CD1 . LEU L 189 ? 4.3325 3.7523 3.0717 -1.8970 -0.2219 0.3754  168 LEU K CD1 
22130 C CD2 . LEU L 189 ? 4.2501 3.6443 2.8732 -1.9107 -0.2351 0.3192  168 LEU K CD2 
22131 N N   . GLN L 190 ? 3.9232 3.6834 2.8502 -1.8886 -0.2843 0.3065  169 GLN K N   
22132 C CA  . GLN L 190 ? 3.9178 3.8310 2.8639 -1.9036 -0.3171 0.2921  169 GLN K CA  
22133 C C   . GLN L 190 ? 3.9660 3.9002 2.8373 -1.9364 -0.3290 0.3069  169 GLN K C   
22134 O O   . GLN L 190 ? 4.0306 3.8654 2.8394 -1.9493 -0.3138 0.3291  169 GLN K O   
22135 C CB  . GLN L 190 ? 3.8875 3.9064 2.9163 -1.9027 -0.3308 0.3085  169 GLN K CB  
22136 C CG  . GLN L 190 ? 3.7752 3.8048 2.8903 -1.8714 -0.3251 0.2928  169 GLN K CG  
22137 C CD  . GLN L 190 ? 3.7554 3.8936 2.9457 -1.8738 -0.3398 0.3138  169 GLN K CD  
22138 O OE1 . GLN L 190 ? 3.8309 4.0254 3.0061 -1.8987 -0.3515 0.3432  169 GLN K OE1 
22139 N NE2 . GLN L 190 ? 3.6659 3.8424 2.9388 -1.8467 -0.3410 0.2968  169 GLN K NE2 
22140 N N   . SER L 191 ? 3.9769 4.0445 2.8584 -1.9454 -0.3553 0.2939  170 SER K N   
22141 C CA  . SER L 191 ? 3.9979 4.0995 2.8130 -1.9754 -0.3677 0.3069  170 SER K CA  
22142 C C   . SER L 191 ? 4.0540 4.1543 2.8620 -2.0023 -0.3691 0.3552  170 SER K C   
22143 O O   . SER L 191 ? 4.0953 4.1817 2.8382 -2.0290 -0.3733 0.3733  170 SER K O   
22144 C CB  . SER L 191 ? 3.9250 4.1699 2.7636 -1.9677 -0.3899 0.2814  170 SER K CB  
22145 O OG  . SER L 191 ? 3.8874 4.2392 2.8067 -1.9574 -0.4032 0.2877  170 SER K OG  
22146 N N   . SER L 192 ? 3.9777 4.0929 2.8535 -1.9941 -0.3650 0.3772  171 SER K N   
22147 C CA  . SER L 192 ? 4.0296 4.1419 2.9062 -2.0139 -0.3628 0.4256  171 SER K CA  
22148 C C   . SER L 192 ? 4.1077 4.0627 2.9381 -2.0116 -0.3327 0.4516  171 SER K C   
22149 O O   . SER L 192 ? 4.1605 4.0963 2.9737 -2.0261 -0.3280 0.4907  171 SER K O   
22150 C CB  . SER L 192 ? 4.0037 4.1832 2.9715 -2.0012 -0.3654 0.4421  171 SER K CB  
22151 O OG  . SER L 192 ? 4.0003 4.0982 3.0103 -1.9716 -0.3427 0.4335  171 SER K OG  
22152 N N   . GLY L 193 ? 4.2195 4.0642 3.0324 -1.9887 -0.3110 0.4299  172 GLY K N   
22153 C CA  . GLY L 193 ? 4.2888 3.9823 3.0619 -1.9755 -0.2792 0.4494  172 GLY K CA  
22154 C C   . GLY L 193 ? 4.3131 3.9340 3.1441 -1.9432 -0.2506 0.4702  172 GLY K C   
22155 O O   . GLY L 193 ? 4.4049 3.9185 3.2169 -1.9284 -0.2231 0.4985  172 GLY K O   
22156 N N   . LEU L 194 ? 4.1447 3.8234 3.0479 -1.9286 -0.2557 0.4564  173 LEU K N   
22157 C CA  . LEU L 194 ? 4.0869 3.7118 3.0534 -1.8973 -0.2308 0.4739  173 LEU K CA  
22158 C C   . LEU L 194 ? 3.9899 3.5780 2.9845 -1.8693 -0.2220 0.4358  173 LEU K C   
22159 O O   . LEU L 194 ? 3.9385 3.6051 2.9410 -1.8754 -0.2450 0.3963  173 LEU K O   
22160 C CB  . LEU L 194 ? 4.0649 3.8058 3.1029 -1.9062 -0.2469 0.4965  173 LEU K CB  
22161 C CG  . LEU L 194 ? 4.1606 3.9357 3.1775 -1.9304 -0.2533 0.5386  173 LEU K CG  
22162 C CD1 . LEU L 194 ? 4.1352 4.0436 3.2226 -1.9404 -0.2737 0.5566  173 LEU K CD1 
22163 C CD2 . LEU L 194 ? 4.2115 3.8520 3.2052 -1.9103 -0.2172 0.5762  173 LEU K CD2 
22164 N N   . TYR L 195 ? 4.1197 3.5896 3.1309 -1.8344 -0.1876 0.4472  174 TYR K N   
22165 C CA  . TYR L 195 ? 4.0361 3.4570 3.0760 -1.8036 -0.1748 0.4153  174 TYR K CA  
22166 C C   . TYR L 195 ? 3.9509 3.4449 3.0838 -1.7917 -0.1812 0.4138  174 TYR K C   
22167 O O   . TYR L 195 ? 3.9584 3.5142 3.1336 -1.8008 -0.1872 0.4446  174 TYR K O   
22168 C CB  . TYR L 195 ? 4.0488 3.3112 3.0641 -1.7675 -0.1344 0.4269  174 TYR K CB  
22169 C CG  . TYR L 195 ? 4.1197 3.3071 3.0485 -1.7739 -0.1273 0.4229  174 TYR K CG  
22170 C CD1 . TYR L 195 ? 4.1056 3.2724 2.9927 -1.7729 -0.1330 0.3822  174 TYR K CD1 
22171 C CD2 . TYR L 195 ? 4.1877 3.3241 3.0795 -1.7780 -0.1141 0.4589  174 TYR K CD2 
22172 C CE1 . TYR L 195 ? 4.1654 3.2660 2.9752 -1.7783 -0.1269 0.3779  174 TYR K CE1 
22173 C CE2 . TYR L 195 ? 4.2449 3.3154 3.0618 -1.7828 -0.1084 0.4534  174 TYR K CE2 
22174 C CZ  . TYR L 195 ? 4.2334 3.2864 3.0091 -1.7837 -0.1151 0.4131  174 TYR K CZ  
22175 O OH  . TYR L 195 ? 4.2910 3.2807 2.9933 -1.7886 -0.1097 0.4080  174 TYR K OH  
22176 N N   . SER L 196 ? 3.9996 3.4863 3.1653 -1.7698 -0.1798 0.3770  175 SER K N   
22177 C CA  . SER L 196 ? 3.8879 3.4430 3.1444 -1.7552 -0.1870 0.3670  175 SER K CA  
22178 C C   . SER L 196 ? 3.8215 3.3043 3.0981 -1.7207 -0.1702 0.3345  175 SER K C   
22179 O O   . SER L 196 ? 3.7836 3.2676 3.0271 -1.7202 -0.1796 0.2953  175 SER K O   
22180 C CB  . SER L 196 ? 3.8340 3.5586 3.1243 -1.7786 -0.2289 0.3427  175 SER K CB  
22181 O OG  . SER L 196 ? 3.7994 3.5560 3.0326 -1.7926 -0.2475 0.3087  175 SER K OG  
22182 N N   . LEU L 197 ? 3.8861 3.3080 3.2171 -1.6902 -0.1452 0.3508  176 LEU K N   
22183 C CA  . LEU L 197 ? 3.8289 3.1762 3.1851 -1.6536 -0.1260 0.3246  176 LEU K CA  
22184 C C   . LEU L 197 ? 3.7649 3.1878 3.2172 -1.6406 -0.1365 0.3108  176 LEU K C   
22185 O O   . LEU L 197 ? 3.7677 3.3042 3.2692 -1.6585 -0.1590 0.3208  176 LEU K O   
22186 C CB  . LEU L 197 ? 3.8752 3.0745 3.2197 -1.6189 -0.0824 0.3572  176 LEU K CB  
22187 C CG  . LEU L 197 ? 3.9466 3.0218 3.2211 -1.6053 -0.0533 0.3804  176 LEU K CG  
22188 C CD1 . LEU L 197 ? 3.9349 2.9157 3.2493 -1.5628 -0.0157 0.4121  176 LEU K CD1 
22189 C CD2 . LEU L 197 ? 3.9310 2.9403 3.1520 -1.5933 -0.0469 0.3469  176 LEU K CD2 
22190 N N   . SER L 198 ? 3.6972 3.0584 3.1776 -1.6070 -0.1204 0.2863  177 SER K N   
22191 C CA  . SER L 198 ? 3.6117 3.0232 3.1838 -1.5877 -0.1256 0.2702  177 SER K CA  
22192 C C   . SER L 198 ? 3.6059 2.8863 3.1908 -1.5442 -0.0892 0.2692  177 SER K C   
22193 O O   . SER L 198 ? 3.6561 2.8379 3.1821 -1.5291 -0.0703 0.2609  177 SER K O   
22194 C CB  . SER L 198 ? 3.5362 3.0733 3.1388 -1.5953 -0.1625 0.2172  177 SER K CB  
22195 O OG  . SER L 198 ? 3.5952 3.2603 3.1893 -1.6283 -0.1959 0.2165  177 SER K OG  
22196 N N   . SER L 199 ? 3.6014 2.8848 3.2657 -1.5219 -0.0799 0.2775  178 SER K N   
22197 C CA  . SER L 199 ? 3.5839 2.7512 3.2709 -1.4764 -0.0454 0.2776  178 SER K CA  
22198 C C   . SER L 199 ? 3.4995 2.7255 3.2804 -1.4603 -0.0551 0.2551  178 SER K C   
22199 O O   . SER L 199 ? 3.4646 2.7543 3.3066 -1.4669 -0.0627 0.2764  178 SER K O   
22200 C CB  . SER L 199 ? 3.6250 2.6872 3.3016 -1.4542 -0.0082 0.3300  178 SER K CB  
22201 O OG  . SER L 199 ? 3.6121 2.5659 3.3103 -1.4055 0.0256  0.3296  178 SER K OG  
22202 N N   . VAL L 200 ? 3.4682 2.6749 3.2641 -1.4374 -0.0547 0.2131  179 VAL K N   
22203 C CA  . VAL L 200 ? 3.3932 2.6576 3.2801 -1.4200 -0.0652 0.1872  179 VAL K CA  
22204 C C   . VAL L 200 ? 3.4094 2.5519 3.3230 -1.3725 -0.0280 0.1932  179 VAL K C   
22205 O O   . VAL L 200 ? 3.4638 2.4910 3.3238 -1.3487 -0.0000 0.1990  179 VAL K O   
22206 C CB  . VAL L 200 ? 3.3364 2.7020 3.2355 -1.4275 -0.0996 0.1290  179 VAL K CB  
22207 C CG1 . VAL L 200 ? 3.3344 2.8374 3.2217 -1.4663 -0.1377 0.1223  179 VAL K CG1 
22208 C CG2 . VAL L 200 ? 3.3744 2.6541 3.2078 -1.4118 -0.0866 0.1037  179 VAL K CG2 
22209 N N   . VAL L 201 ? 3.4335 2.6087 3.4348 -1.3560 -0.0287 0.1916  180 VAL K N   
22210 C CA  . VAL L 201 ? 3.4249 2.5002 3.4659 -1.3087 0.0040  0.1959  180 VAL K CA  
22211 C C   . VAL L 201 ? 3.3669 2.5141 3.4878 -1.2971 -0.0156 0.1522  180 VAL K C   
22212 O O   . VAL L 201 ? 3.3104 2.5765 3.4968 -1.3156 -0.0438 0.1451  180 VAL K O   
22213 C CB  . VAL L 201 ? 3.4876 2.5092 3.5604 -1.2916 0.0312  0.2484  180 VAL K CB  
22214 C CG1 . VAL L 201 ? 3.4147 2.3396 3.5318 -1.2381 0.0641  0.2503  180 VAL K CG1 
22215 C CG2 . VAL L 201 ? 3.5906 2.5457 3.5902 -1.2980 0.0507  0.2900  180 VAL K CG2 
22216 N N   . THR L 202 ? 3.2964 2.3781 3.4170 -1.2636 -0.0018 0.1234  181 THR K N   
22217 C CA  . THR L 202 ? 3.2208 2.3563 3.4169 -1.2454 -0.0163 0.0811  181 THR K CA  
22218 C C   . THR L 202 ? 3.2123 2.2974 3.4814 -1.2128 0.0078  0.1046  181 THR K C   
22219 O O   . THR L 202 ? 3.2546 2.2173 3.5124 -1.1728 0.0443  0.1241  181 THR K O   
22220 C CB  . THR L 202 ? 3.2176 2.3061 3.3823 -1.2218 -0.0121 0.0425  181 THR K CB  
22221 O OG1 . THR L 202 ? 3.2806 2.2261 3.4074 -1.1853 0.0277  0.0688  181 THR K OG1 
22222 C CG2 . THR L 202 ? 3.2198 2.3682 3.3170 -1.2531 -0.0383 0.0171  181 THR K CG2 
22223 N N   . VAL L 203 ? 3.3952 2.5802 3.7438 -1.2254 -0.0136 0.1035  182 VAL K N   
22224 C CA  . VAL L 203 ? 3.4005 2.5396 3.8198 -1.1951 0.0083  0.1279  182 VAL K CA  
22225 C C   . VAL L 203 ? 3.3299 2.5620 3.8456 -1.1800 -0.0154 0.0861  182 VAL K C   
22226 O O   . VAL L 203 ? 3.2577 2.6295 3.8004 -1.1954 -0.0548 0.0468  182 VAL K O   
22227 C CB  . VAL L 203 ? 3.3378 2.4984 3.7729 -1.2127 0.0101  0.1803  182 VAL K CB  
22228 C CG1 . VAL L 203 ? 3.3355 2.3872 3.6858 -1.2091 0.0426  0.2232  182 VAL K CG1 
22229 C CG2 . VAL L 203 ? 3.1928 2.5323 3.6598 -1.2374 -0.0341 0.1656  182 VAL K CG2 
22230 N N   . PRO L 204 ? 3.4237 2.5933 3.9981 -1.1347 0.0089  0.0909  183 PRO K N   
22231 C CA  . PRO L 204 ? 3.3397 2.6091 4.0168 -1.1013 -0.0110 0.0511  183 PRO K CA  
22232 C C   . PRO L 204 ? 3.3021 2.7358 4.0552 -1.1000 -0.0432 0.0522  183 PRO K C   
22233 O O   . PRO L 204 ? 3.3008 2.7423 4.0524 -1.1056 -0.0371 0.0958  183 PRO K O   
22234 C CB  . PRO L 204 ? 3.3245 2.4749 4.0404 -1.0545 0.0279  0.0705  183 PRO K CB  
22235 C CG  . PRO L 204 ? 3.3795 2.4061 4.0342 -1.0618 0.0627  0.1292  183 PRO K CG  
22236 C CD  . PRO L 204 ? 3.4103 2.4191 3.9627 -1.1036 0.0570  0.1312  183 PRO K CD  
22237 N N   . SER L 205 ? 3.4487 3.0164 4.2687 -1.0927 -0.0782 0.0031  184 SER K N   
22238 C CA  . SER L 205 ? 3.4011 3.1344 4.2942 -1.0922 -0.1119 -0.0007 184 SER K CA  
22239 C C   . SER L 205 ? 3.4291 3.1507 4.3964 -1.0533 -0.0931 0.0350  184 SER K C   
22240 O O   . SER L 205 ? 3.4247 3.2466 4.4326 -1.0559 -0.1098 0.0537  184 SER K O   
22241 C CB  . SER L 205 ? 3.3093 3.1793 4.2671 -1.0860 -0.1502 -0.0615 184 SER K CB  
22242 O OG  . SER L 205 ? 3.2604 3.1438 4.1511 -1.1216 -0.1683 -0.0960 184 SER K OG  
22243 N N   . SER L 206 ? 3.2531 2.8536 4.2390 -1.0170 -0.0584 0.0447  185 SER K N   
22244 C CA  . SER L 206 ? 3.2346 2.8082 4.2883 -0.9781 -0.0368 0.0794  185 SER K CA  
22245 C C   . SER L 206 ? 3.2594 2.7579 4.2543 -0.9950 -0.0133 0.1396  185 SER K C   
22246 O O   . SER L 206 ? 3.2860 2.6300 4.2315 -0.9875 0.0261  0.1731  185 SER K O   
22247 C CB  . SER L 206 ? 3.2124 2.6670 4.2921 -0.9375 -0.0045 0.0739  185 SER K CB  
22248 O OG  . SER L 206 ? 3.2443 2.5371 4.2287 -0.9503 0.0284  0.0910  185 SER K OG  
22249 N N   . SER L 207 ? 3.1200 2.7305 4.1198 -1.0186 -0.0383 0.1536  186 SER K N   
22250 C CA  . SER L 207 ? 3.1905 2.7450 4.1389 -1.0362 -0.0195 0.2103  186 SER K CA  
22251 C C   . SER L 207 ? 3.1414 2.8266 4.1651 -1.0272 -0.0399 0.2271  186 SER K C   
22252 O O   . SER L 207 ? 3.1583 2.9018 4.1526 -1.0567 -0.0534 0.2509  186 SER K O   
22253 C CB  . SER L 207 ? 3.2451 2.7812 4.0872 -1.0878 -0.0271 0.2148  186 SER K CB  
22254 O OG  . SER L 207 ? 3.2903 2.7067 4.0619 -1.0965 -0.0089 0.1980  186 SER K OG  
22255 N N   . LEU L 208 ? 3.1732 2.9059 4.2976 -0.9847 -0.0422 0.2141  187 LEU K N   
22256 C CA  . LEU L 208 ? 3.1773 3.0224 4.3802 -0.9697 -0.0574 0.2319  187 LEU K CA  
22257 C C   . LEU L 208 ? 3.2351 2.9869 4.4089 -0.9676 -0.0250 0.2959  187 LEU K C   
22258 O O   . LEU L 208 ? 3.2346 3.0600 4.4119 -0.9832 -0.0373 0.3236  187 LEU K O   
22259 C CB  . LEU L 208 ? 3.1025 3.0050 4.4176 -0.9231 -0.0641 0.2040  187 LEU K CB  
22260 C CG  . LEU L 208 ? 3.0030 3.0663 4.4124 -0.9093 -0.0935 0.2019  187 LEU K CG  
22261 C CD1 . LEU L 208 ? 3.0488 3.0743 4.4848 -0.8898 -0.0698 0.2576  187 LEU K CD1 
22262 C CD2 . LEU L 208 ? 2.9859 3.1905 4.3716 -0.9506 -0.1346 0.1848  187 LEU K CD2 
22263 N N   . GLY L 209 ? 3.1910 2.7800 4.3373 -0.9475 0.0170  0.3195  188 GLY K N   
22264 C CA  . GLY L 209 ? 3.2324 2.7018 4.3367 -0.9462 0.0535  0.3791  188 GLY K CA  
22265 C C   . GLY L 209 ? 3.3250 2.8459 4.4802 -0.9335 0.0550  0.4211  188 GLY K C   
22266 O O   . GLY L 209 ? 3.3950 2.9261 4.6332 -0.8929 0.0634  0.4262  188 GLY K O   
22267 N N   . THR L 210 ? 3.2731 2.8253 4.3783 -0.9682 0.0472  0.4517  189 THR K N   
22268 C CA  . THR L 210 ? 3.2623 2.8128 4.2736 -1.0166 0.0344  0.4425  189 THR K CA  
22269 C C   . THR L 210 ? 3.3369 2.7063 4.2496 -1.0299 0.0721  0.4669  189 THR K C   
22270 O O   . THR L 210 ? 3.4225 2.6971 4.2993 -1.0311 0.1011  0.5180  189 THR K O   
22271 C CB  . THR L 210 ? 3.2222 2.8728 4.2163 -1.0491 0.0125  0.4682  189 THR K CB  
22272 O OG1 . THR L 210 ? 3.2409 2.8149 4.2249 -1.0413 0.0420  0.5277  189 THR K OG1 
22273 C CG2 . THR L 210 ? 3.1217 2.9591 4.2076 -1.0396 -0.0280 0.4401  189 THR K CG2 
22274 N N   . GLN L 211 ? 3.3320 2.6545 4.2017 -1.0395 0.0712  0.4294  190 GLN K N   
22275 C CA  . GLN L 211 ? 3.3500 2.5101 4.1201 -1.0567 0.1028  0.4472  190 GLN K CA  
22276 C C   . GLN L 211 ? 3.3929 2.5694 4.0782 -1.1071 0.0917  0.4671  190 GLN K C   
22277 O O   . GLN L 211 ? 3.3886 2.6135 4.0298 -1.1391 0.0676  0.4338  190 GLN K O   
22278 C CB  . GLN L 211 ? 3.2510 2.3617 4.0006 -1.0526 0.1037  0.4000  190 GLN K CB  
22279 C CG  . GLN L 211 ? 3.2588 2.1864 3.9772 -1.0281 0.1494  0.4181  190 GLN K CG  
22280 C CD  . GLN L 211 ? 3.3328 2.1364 3.9181 -1.0396 0.1840  0.4424  190 GLN K CD  
22281 O OE1 . GLN L 211 ? 3.3706 2.2072 3.9096 -1.0810 0.1695  0.4513  190 GLN K OE1 
22282 N NE2 . GLN L 211 ? 3.4219 2.0924 3.9283 -0.9990 0.2209  0.4512  190 GLN K NE2 
22283 N N   . THR L 212 ? 3.0998 2.2384 3.7634 -1.1142 0.1088  0.5211  191 THR K N   
22284 C CA  . THR L 212 ? 3.1422 2.3087 3.7372 -1.1595 0.0978  0.5462  191 THR K CA  
22285 C C   . THR L 212 ? 3.2082 2.2776 3.6945 -1.1955 0.1066  0.5395  191 THR K C   
22286 O O   . THR L 212 ? 3.2766 2.2050 3.7072 -1.1667 0.1503  0.5503  191 THR K O   
22287 C CB  . THR L 212 ? 3.1938 2.3088 3.7868 -1.1539 0.1223  0.6087  191 THR K CB  
22288 O OG1 . THR L 212 ? 3.1362 2.3204 3.8315 -1.1148 0.1194  0.6148  191 THR K OG1 
22289 C CG2 . THR L 212 ? 3.2147 2.4033 3.7636 -1.1965 0.1028  0.6322  191 THR K CG2 
22290 N N   . TYR L 213 ? 3.1979 2.3630 3.6544 -1.2308 0.0724  0.5055  192 TYR K N   
22291 C CA  . TYR L 213 ? 3.2527 2.3520 3.6074 -1.2622 0.0761  0.4932  192 TYR K CA  
22292 C C   . TYR L 213 ? 3.2972 2.4262 3.5940 -1.2948 0.0702  0.5257  192 TYR K C   
22293 O O   . TYR L 213 ? 3.2563 2.5189 3.5662 -1.3345 0.0315  0.5197  192 TYR K O   
22294 C CB  . TYR L 213 ? 3.1935 2.3763 3.5535 -1.2812 0.0418  0.4342  192 TYR K CB  
22295 C CG  . TYR L 213 ? 3.1542 2.2999 3.5644 -1.2422 0.0509  0.3982  192 TYR K CG  
22296 C CD1 . TYR L 213 ? 3.2002 2.1989 3.6026 -1.2009 0.0952  0.4142  192 TYR K CD1 
22297 C CD2 . TYR L 213 ? 3.0662 2.3348 3.5370 -1.2334 0.0178  0.3442  192 TYR K CD2 
22298 C CE1 . TYR L 213 ? 3.1651 2.1288 3.6139 -1.1675 0.1036  0.3835  192 TYR K CE1 
22299 C CE2 . TYR L 213 ? 3.0297 2.2654 3.5486 -1.1974 0.0262  0.3120  192 TYR K CE2 
22300 C CZ  . TYR L 213 ? 3.0811 2.1604 3.5879 -1.1693 0.0682  0.3341  192 TYR K CZ  
22301 O OH  . TYR L 213 ? 3.0455 2.0912 3.6001 -1.1333 0.0771  0.3029  192 TYR K OH  
22302 N N   . ILE L 214 ? 3.3615 2.3740 3.5990 -1.2710 0.1094  0.5568  193 ILE K N   
22303 C CA  . ILE L 214 ? 3.4128 2.4343 3.5922 -1.2950 0.1094  0.5898  193 ILE K CA  
22304 C C   . ILE L 214 ? 3.4736 2.4117 3.5608 -1.2931 0.1249  0.5778  193 ILE K C   
22305 O O   . ILE L 214 ? 3.5192 2.3383 3.5857 -1.2495 0.1636  0.5845  193 ILE K O   
22306 C CB  . ILE L 214 ? 3.4514 2.4218 3.6507 -1.2668 0.1405  0.6408  193 ILE K CB  
22307 C CG1 . ILE L 214 ? 3.3881 2.4531 3.6831 -1.2699 0.1208  0.6568  193 ILE K CG1 
22308 C CG2 . ILE L 214 ? 3.5095 2.4769 3.6465 -1.2865 0.1443  0.6737  193 ILE K CG2 
22309 C CD1 . ILE L 214 ? 3.4226 2.4421 3.7400 -1.2405 0.1504  0.7053  193 ILE K CD1 
22310 N N   . CYS L 215 ? 3.6551 2.6636 3.6935 -1.3379 0.0936  0.5605  194 CYS K N   
22311 C CA  . CYS L 215 ? 3.7163 2.6588 3.6672 -1.3410 0.1027  0.5506  194 CYS K CA  
22312 C C   . CYS L 215 ? 3.7817 2.6874 3.6866 -1.3430 0.1197  0.5947  194 CYS K C   
22313 O O   . CYS L 215 ? 3.7827 2.7682 3.6995 -1.3716 0.1020  0.6204  194 CYS K O   
22314 C CB  . CYS L 215 ? 3.7087 2.7442 3.6271 -1.3869 0.0618  0.5104  194 CYS K CB  
22315 S SG  . CYS L 215 ? 3.6813 2.8921 3.6138 -1.4473 0.0136  0.5198  194 CYS K SG  
22316 N N   . ASN L 216 ? 3.8258 2.6189 3.6821 -1.3122 0.1519  0.6027  195 ASN K N   
22317 C CA  . ASN L 216 ? 3.8914 2.6435 3.7068 -1.3091 0.1701  0.6419  195 ASN K CA  
22318 C C   . ASN L 216 ? 3.9465 2.7042 3.6796 -1.3411 0.1538  0.6278  195 ASN K C   
22319 O O   . ASN L 216 ? 3.9622 2.6566 3.6578 -1.3257 0.1629  0.6042  195 ASN K O   
22320 C CB  . ASN L 216 ? 3.9092 2.5452 3.7391 -1.2505 0.2160  0.6642  195 ASN K CB  
22321 C CG  . ASN L 216 ? 3.8611 2.4841 3.7714 -1.2149 0.2355  0.6784  195 ASN K CG  
22322 O OD1 . ASN L 216 ? 3.8102 2.5042 3.7662 -1.2321 0.2148  0.6673  195 ASN K OD1 
22323 N ND2 . ASN L 216 ? 3.8766 2.4164 3.8095 -1.1651 0.2736  0.7047  195 ASN K ND2 
22324 N N   . VAL L 217 ? 3.8587 2.6932 3.5655 -1.3839 0.1299  0.6440  196 VAL K N   
22325 C CA  . VAL L 217 ? 3.9174 2.7698 3.5477 -1.4188 0.1115  0.6336  196 VAL K CA  
22326 C C   . VAL L 217 ? 3.9933 2.7889 3.5848 -1.4095 0.1337  0.6720  196 VAL K C   
22327 O O   . VAL L 217 ? 3.9999 2.8201 3.6183 -1.4099 0.1390  0.7085  196 VAL K O   
22328 C CB  . VAL L 217 ? 3.9037 2.8964 3.5359 -1.4741 0.0657  0.6222  196 VAL K CB  
22329 C CG1 . VAL L 217 ? 3.9693 2.9817 3.5231 -1.5092 0.0469  0.6113  196 VAL K CG1 
22330 C CG2 . VAL L 217 ? 3.8245 2.8844 3.5063 -1.4812 0.0428  0.5824  196 VAL K CG2 
22331 N N   . ASN L 218 ? 4.0900 2.8132 3.6213 -1.4007 0.1459  0.6635  197 ASN K N   
22332 C CA  . ASN L 218 ? 4.1642 2.8341 3.6604 -1.3911 0.1662  0.6964  197 ASN K CA  
22333 C C   . ASN L 218 ? 4.2310 2.9191 3.6488 -1.4289 0.1450  0.6832  197 ASN K C   
22334 O O   . ASN L 218 ? 4.2273 2.9041 3.6090 -1.4369 0.1341  0.6471  197 ASN K O   
22335 C CB  . ASN L 218 ? 4.1652 2.7210 3.6767 -1.3337 0.2074  0.7063  197 ASN K CB  
22336 C CG  . ASN L 218 ? 4.2395 2.7436 3.7177 -1.3232 0.2272  0.7373  197 ASN K CG  
22337 O OD1 . ASN L 218 ? 4.2985 2.8418 3.7341 -1.3586 0.2115  0.7494  197 ASN K OD1 
22338 N ND2 . ASN L 218 ? 4.2356 2.6569 3.7393 -1.2736 0.2606  0.7506  197 ASN K ND2 
22339 N N   . HIS L 219 ? 4.0225 2.7377 3.4145 -1.4510 0.1399  0.7127  198 HIS K N   
22340 C CA  . HIS L 219 ? 4.0973 2.8297 3.4162 -1.4866 0.1211  0.7056  198 HIS K CA  
22341 C C   . HIS L 219 ? 4.1718 2.8415 3.4687 -1.4695 0.1462  0.7407  198 HIS K C   
22342 O O   . HIS L 219 ? 4.2121 2.9212 3.5184 -1.4825 0.1437  0.7734  198 HIS K O   
22343 C CB  . HIS L 219 ? 4.1051 2.9643 3.4184 -1.5402 0.0801  0.7037  198 HIS K CB  
22344 C CG  . HIS L 219 ? 4.1754 3.0661 3.4163 -1.5800 0.0554  0.6887  198 HIS K CG  
22345 N ND1 . HIS L 219 ? 4.2613 3.0933 3.4492 -1.5782 0.0684  0.7043  198 HIS K ND1 
22346 C CD2 . HIS L 219 ? 4.1764 3.1576 3.3926 -1.6230 0.0177  0.6604  198 HIS K CD2 
22347 C CE1 . HIS L 219 ? 4.3138 3.1936 3.4446 -1.6186 0.0401  0.6863  198 HIS K CE1 
22348 N NE2 . HIS L 219 ? 4.2638 3.2350 3.4101 -1.6459 0.0094  0.6596  198 HIS K NE2 
22349 N N   . LYS L 220 ? 4.1815 2.7588 3.4512 -1.4406 0.1690  0.7327  199 LYS K N   
22350 C CA  . LYS L 220 ? 4.2451 2.7596 3.5008 -1.4197 0.1946  0.7635  199 LYS K CA  
22351 C C   . LYS L 220 ? 4.3380 2.8920 3.5408 -1.4594 0.1767  0.7780  199 LYS K C   
22352 O O   . LYS L 220 ? 4.3861 2.9298 3.6010 -1.4508 0.1919  0.8145  199 LYS K O   
22353 C CB  . LYS L 220 ? 4.2458 2.6665 3.4860 -1.3834 0.2175  0.7489  199 LYS K CB  
22354 C CG  . LYS L 220 ? 4.1631 2.5419 3.4609 -1.3389 0.2374  0.7393  199 LYS K CG  
22355 C CD  . LYS L 220 ? 4.1677 2.4669 3.4481 -1.3072 0.2546  0.7249  199 LYS K CD  
22356 C CE  . LYS L 220 ? 4.0939 2.3568 3.4325 -1.2630 0.2713  0.7146  199 LYS K CE  
22357 N NZ  . LYS L 220 ? 4.0841 2.3311 3.3905 -1.2652 0.2599  0.6720  199 LYS K NZ  
22358 N N   . PRO L 221 ? 4.1428 2.7421 3.2888 -1.5017 0.1458  0.7523  200 PRO K N   
22359 C CA  . PRO L 221 ? 4.1786 2.8155 3.2768 -1.5380 0.1293  0.7683  200 PRO K CA  
22360 C C   . PRO L 221 ? 4.1631 2.8828 3.2926 -1.5593 0.1163  0.7992  200 PRO K C   
22361 O O   . PRO L 221 ? 4.1988 2.9369 3.3030 -1.5775 0.1120  0.8233  200 PRO K O   
22362 C CB  . PRO L 221 ? 4.1651 2.8439 3.2058 -1.5776 0.0966  0.7299  200 PRO K CB  
22363 C CG  . PRO L 221 ? 4.1494 2.7654 3.1934 -1.5486 0.1093  0.6970  200 PRO K CG  
22364 C CD  . PRO L 221 ? 4.1159 2.7184 3.2335 -1.5129 0.1289  0.7075  200 PRO K CD  
22365 N N   . SER L 222 ? 4.1416 2.9141 3.3268 -1.5573 0.1095  0.7994  201 SER K N   
22366 C CA  . SER L 222 ? 4.1228 2.9766 3.3449 -1.5739 0.0979  0.8300  201 SER K CA  
22367 C C   . SER L 222 ? 4.1183 2.9246 3.4052 -1.5286 0.1307  0.8541  201 SER K C   
22368 O O   . SER L 222 ? 4.1026 2.9634 3.4302 -1.5327 0.1278  0.8822  201 SER K O   
22369 C CB  . SER L 222 ? 4.0560 3.0310 3.2966 -1.6128 0.0580  0.8104  201 SER K CB  
22370 O OG  . SER L 222 ? 4.0524 3.0865 3.2384 -1.6563 0.0251  0.7875  201 SER K OG  
22371 N N   . ASN L 223 ? 4.4117 3.1192 3.7097 -1.4847 0.1618  0.8437  202 ASN K N   
22372 C CA  . ASN L 223 ? 4.3595 3.0099 3.7194 -1.4353 0.1966  0.8622  202 ASN K CA  
22373 C C   . ASN L 223 ? 4.2811 3.0022 3.6994 -1.4410 0.1834  0.8626  202 ASN K C   
22374 O O   . ASN L 223 ? 4.2420 2.9453 3.7140 -1.4110 0.2058  0.8872  202 ASN K O   
22375 C CB  . ASN L 223 ? 4.4173 3.0228 3.7848 -1.4122 0.2251  0.9034  202 ASN K CB  
22376 C CG  . ASN L 223 ? 4.4875 3.0240 3.8039 -1.4046 0.2381  0.9024  202 ASN K CG  
22377 O OD1 . ASN L 223 ? 4.4681 2.9240 3.7932 -1.3661 0.2637  0.8960  202 ASN K OD1 
22378 N ND2 . ASN L 223 ? 4.5672 3.1420 3.8323 -1.4428 0.2179  0.9081  202 ASN K ND2 
22379 N N   . THR L 224 ? 4.1231 2.9115 3.5361 -1.4718 0.1511  0.8299  203 THR K N   
22380 C CA  . THR L 224 ? 4.0739 2.9518 3.5418 -1.4865 0.1298  0.8261  203 THR K CA  
22381 C C   . THR L 224 ? 3.9702 2.8032 3.4768 -1.4547 0.1430  0.7996  203 THR K C   
22382 O O   . THR L 224 ? 3.9491 2.7556 3.4264 -1.4561 0.1373  0.7637  203 THR K O   
22383 C CB  . THR L 224 ? 4.1421 3.1411 3.5875 -1.5427 0.0828  0.8078  203 THR K CB  
22384 O OG1 . THR L 224 ? 4.1723 3.2052 3.5775 -1.5698 0.0722  0.8321  203 THR K OG1 
22385 C CG2 . THR L 224 ? 4.1208 3.2283 3.6339 -1.5576 0.0594  0.8086  203 THR K CG2 
22386 N N   . LYS L 225 ? 3.9867 2.8130 3.5596 -1.4260 0.1603  0.8174  204 LYS K N   
22387 C CA  . LYS L 225 ? 3.8993 2.6876 3.5206 -1.3929 0.1743  0.7972  204 LYS K CA  
22388 C C   . LYS L 225 ? 3.8611 2.7476 3.5448 -1.4102 0.1504  0.7951  204 LYS K C   
22389 O O   . LYS L 225 ? 3.8113 2.7149 3.5420 -1.3977 0.1604  0.8268  204 LYS K O   
22390 C CB  . LYS L 225 ? 3.9083 2.5970 3.5598 -1.3374 0.2203  0.8241  204 LYS K CB  
22391 C CG  . LYS L 225 ? 3.9633 2.5557 3.5735 -1.3106 0.2462  0.8250  204 LYS K CG  
22392 C CD  . LYS L 225 ? 3.9807 2.4923 3.6402 -1.2530 0.2888  0.8495  204 LYS K CD  
22393 C CE  . LYS L 225 ? 4.0251 2.4530 3.6584 -1.2238 0.3112  0.8515  204 LYS K CE  
22394 N NZ  . LYS L 225 ? 4.0300 2.3968 3.7255 -1.1677 0.3476  0.8768  204 LYS K NZ  
22395 N N   . VAL L 226 ? 3.7944 2.7408 3.4852 -1.4334 0.1213  0.7567  205 VAL K N   
22396 C CA  . VAL L 226 ? 3.7206 2.7793 3.4767 -1.4539 0.0924  0.7495  205 VAL K CA  
22397 C C   . VAL L 226 ? 3.6753 2.7071 3.4823 -1.4266 0.0997  0.7205  205 VAL K C   
22398 O O   . VAL L 226 ? 3.6671 2.6695 3.4488 -1.4252 0.0961  0.6822  205 VAL K O   
22399 C CB  . VAL L 226 ? 3.6821 2.8687 3.4175 -1.5093 0.0452  0.7279  205 VAL K CB  
22400 C CG1 . VAL L 226 ? 3.5958 2.9123 3.4101 -1.5274 0.0136  0.7161  205 VAL K CG1 
22401 C CG2 . VAL L 226 ? 3.7227 2.9463 3.4116 -1.5379 0.0354  0.7571  205 VAL K CG2 
22402 N N   . ASP L 227 ? 3.8386 2.8851 3.7188 -1.4056 0.1084  0.7387  206 ASP K N   
22403 C CA  . ASP L 227 ? 3.7729 2.8077 3.7151 -1.3803 0.1132  0.7160  206 ASP K CA  
22404 C C   . ASP L 227 ? 3.7456 2.9323 3.7477 -1.4171 0.0688  0.7022  206 ASP K C   
22405 O O   . ASP L 227 ? 3.7415 3.0032 3.7913 -1.4259 0.0584  0.7328  206 ASP K O   
22406 C CB  . ASP L 227 ? 3.7083 2.6604 3.6950 -1.3301 0.1530  0.7450  206 ASP K CB  
22407 C CG  . ASP L 227 ? 3.7137 2.5309 3.6545 -1.2895 0.1971  0.7571  206 ASP K CG  
22408 O OD1 . ASP L 227 ? 3.7613 2.5427 3.6412 -1.2970 0.1958  0.7382  206 ASP K OD1 
22409 O OD2 . ASP L 227 ? 3.6655 2.4182 3.6355 -1.2488 0.2323  0.7849  206 ASP K OD2 
22410 N N   . LYS L 228 ? 3.6787 2.9157 3.6891 -1.4335 0.0435  0.6557  207 LYS K N   
22411 C CA  . LYS L 228 ? 3.6237 3.0212 3.6972 -1.4666 -0.0013 0.6351  207 LYS K CA  
22412 C C   . LYS L 228 ? 3.5334 2.9437 3.6863 -1.4436 -0.0041 0.6073  207 LYS K C   
22413 O O   . LYS L 228 ? 3.5602 2.8816 3.6945 -1.4200 0.0130  0.5781  207 LYS K O   
22414 C CB  . LYS L 228 ? 3.6408 3.1032 3.6586 -1.5056 -0.0321 0.5988  207 LYS K CB  
22415 C CG  . LYS L 228 ? 3.5752 3.2180 3.6382 -1.5429 -0.0809 0.5736  207 LYS K CG  
22416 C CD  . LYS L 228 ? 3.6122 3.3364 3.6980 -1.5600 -0.0907 0.6182  207 LYS K CD  
22417 C CE  . LYS L 228 ? 3.5684 3.4582 3.6590 -1.6004 -0.1357 0.5994  207 LYS K CE  
22418 N NZ  . LYS L 228 ? 3.6113 3.5894 3.7253 -1.6144 -0.1463 0.6418  207 LYS K NZ  
22419 N N   . ARG L 229 ? 3.4675 2.9964 3.7130 -1.4386 -0.0253 0.6111  208 ARG K N   
22420 C CA  . ARG L 229 ? 3.3699 2.9376 3.7042 -1.3950 -0.0298 0.5763  208 ARG K CA  
22421 C C   . ARG L 229 ? 3.2641 2.9912 3.6433 -1.4010 -0.0741 0.5191  208 ARG K C   
22422 O O   . ARG L 229 ? 3.2294 3.0972 3.6291 -1.4205 -0.1063 0.5170  208 ARG K O   
22423 C CB  . ARG L 229 ? 3.3338 2.9299 3.7510 -1.3581 -0.0196 0.6080  208 ARG K CB  
22424 C CG  . ARG L 229 ? 3.2377 2.8739 3.7512 -1.3116 -0.0233 0.5754  208 ARG K CG  
22425 C CD  . ARG L 229 ? 3.2065 2.8553 3.7936 -1.2768 -0.0095 0.6126  208 ARG K CD  
22426 N NE  . ARG L 229 ? 3.1482 2.8381 3.8302 -1.2321 -0.0134 0.5827  208 ARG K NE  
22427 C CZ  . ARG L 229 ? 3.1594 2.8609 3.9165 -1.1956 -0.0021 0.6063  208 ARG K CZ  
22428 N NH1 . ARG L 229 ? 3.1155 2.8549 3.9573 -1.1561 -0.0067 0.5759  208 ARG K NH1 
22429 N NH2 . ARG L 229 ? 3.1928 2.8692 3.9412 -1.1985 0.0137  0.6602  208 ARG K NH2 
22430 N N   . VAL L 230 ? 3.3253 3.0301 3.7204 -1.3837 -0.0755 0.4732  209 VAL K N   
22431 C CA  . VAL L 230 ? 3.1986 3.0394 3.6350 -1.3868 -0.1151 0.4146  209 VAL K CA  
22432 C C   . VAL L 230 ? 3.0886 3.0157 3.6387 -1.3423 -0.1258 0.3934  209 VAL K C   
22433 O O   . VAL L 230 ? 3.0880 2.9271 3.6720 -1.3047 -0.0999 0.3936  209 VAL K O   
22434 C CB  . VAL L 230 ? 3.1813 2.9502 3.5628 -1.3977 -0.1124 0.3740  209 VAL K CB  
22435 C CG1 . VAL L 230 ? 3.0910 3.0022 3.5211 -1.3982 -0.1530 0.3132  209 VAL K CG1 
22436 C CG2 . VAL L 230 ? 3.2882 2.9851 3.5591 -1.4436 -0.1059 0.3910  209 VAL K CG2 
22437 N N   . GLU L 231 ? 3.1620 3.2616 3.7722 -1.3460 -0.1640 0.3752  210 GLU K N   
22438 C CA  . GLU L 231 ? 3.0404 3.2372 3.7610 -1.3059 -0.1785 0.3523  210 GLU K CA  
22439 C C   . GLU L 231 ? 2.8974 3.2513 3.6516 -1.3180 -0.2241 0.2954  210 GLU K C   
22440 O O   . GLU L 231 ? 2.8871 3.3302 3.6054 -1.3559 -0.2511 0.2908  210 GLU K O   
22441 C CB  . GLU L 231 ? 3.0512 3.3103 3.8295 -1.2905 -0.1782 0.3934  210 GLU K CB  
22442 C CG  . GLU L 231 ? 3.1753 3.2889 3.9306 -1.2754 -0.1340 0.4510  210 GLU K CG  
22443 C CD  . GLU L 231 ? 3.1785 3.3608 3.9844 -1.2651 -0.1361 0.4922  210 GLU K CD  
22444 O OE1 . GLU L 231 ? 3.0981 3.4401 3.9472 -1.2746 -0.1722 0.4784  210 GLU K OE1 
22445 O OE2 . GLU L 231 ? 3.2511 3.3278 4.0532 -1.2475 -0.1015 0.5385  210 GLU K OE2 
22446 N N   . PRO L 232 ? 3.0917 3.4844 3.9158 -1.2865 -0.2339 0.2512  211 PRO K N   
22447 C CA  . PRO L 232 ? 2.9544 3.4971 3.8168 -1.2948 -0.2773 0.1946  211 PRO K CA  
22448 C C   . PRO L 232 ? 2.8816 3.6014 3.7974 -1.3033 -0.3137 0.1951  211 PRO K C   
22449 O O   . PRO L 232 ? 2.8569 3.5998 3.8216 -1.2836 -0.3063 0.2296  211 PRO K O   
22450 C CB  . PRO L 232 ? 2.8597 3.3912 3.7986 -1.2503 -0.2726 0.1594  211 PRO K CB  
22451 C CG  . PRO L 232 ? 2.9115 3.2570 3.8160 -1.2307 -0.2253 0.1889  211 PRO K CG  
22452 C CD  . PRO L 232 ? 3.0463 3.3333 3.9116 -1.2422 -0.2031 0.2512  211 PRO K CD  
# 
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   ALA 1   31  31  ALA ALA A . n 
A 1 2   GLU 2   32  32  GLU GLU A . n 
A 1 3   ASN 3   33  33  ASN ASN A . n 
A 1 4   LEU 4   34  34  LEU LEU A . n 
A 1 5   TRP 5   35  35  TRP TRP A . n 
A 1 6   VAL 6   36  36  VAL VAL A . n 
A 1 7   THR 7   37  37  THR THR A . n 
A 1 8   VAL 8   38  38  VAL VAL A . n 
A 1 9   TYR 9   39  39  TYR TYR A . n 
A 1 10  TYR 10  40  40  TYR TYR A . n 
A 1 11  GLY 11  41  41  GLY GLY A . n 
A 1 12  VAL 12  42  42  VAL VAL A . n 
A 1 13  PRO 13  43  43  PRO PRO A . n 
A 1 14  VAL 14  44  44  VAL VAL A . n 
A 1 15  TRP 15  45  45  TRP TRP A . n 
A 1 16  LYS 16  46  46  LYS LYS A . n 
A 1 17  ASP 17  47  47  ASP ASP A . n 
A 1 18  ALA 18  48  48  ALA ALA A . n 
A 1 19  GLU 19  49  49  GLU GLU A . n 
A 1 20  THR 20  50  50  THR THR A . n 
A 1 21  THR 21  51  51  THR THR A . n 
A 1 22  LEU 22  52  52  LEU LEU A . n 
A 1 23  PHE 23  53  53  PHE PHE A . n 
A 1 24  CYS 24  54  54  CYS CYS A . n 
A 1 25  ALA 25  55  55  ALA ALA A . n 
A 1 26  SER 26  56  56  SER SER A . n 
A 1 27  ASP 27  57  57  ASP ASP A . n 
A 1 28  ALA 28  58  58  ALA ALA A . n 
A 1 29  LYS 29  59  59  LYS LYS A . n 
A 1 30  ALA 30  60  60  ALA ALA A . n 
A 1 31  TYR 31  61  61  TYR TYR A . n 
A 1 32  GLU 32  62  62  GLU GLU A . n 
A 1 33  THR 33  63  63  THR THR A . n 
A 1 34  GLU 34  64  64  GLU GLU A . n 
A 1 35  LYS 35  65  65  LYS LYS A . n 
A 1 36  HIS 36  66  66  HIS HIS A . n 
A 1 37  ASN 37  67  67  ASN ASN A . n 
A 1 38  VAL 38  68  68  VAL VAL A . n 
A 1 39  TRP 39  69  69  TRP TRP A . n 
A 1 40  ALA 40  70  70  ALA ALA A . n 
A 1 41  THR 41  71  71  THR THR A . n 
A 1 42  HIS 42  72  72  HIS HIS A . n 
A 1 43  ALA 43  73  73  ALA ALA A . n 
A 1 44  CYS 44  74  74  CYS CYS A . n 
A 1 45  VAL 45  75  75  VAL VAL A . n 
A 1 46  PRO 46  76  76  PRO PRO A . n 
A 1 47  THR 47  77  77  THR THR A . n 
A 1 48  ASP 48  78  78  ASP ASP A . n 
A 1 49  PRO 49  79  79  PRO PRO A . n 
A 1 50  ASN 50  80  80  ASN ASN A . n 
A 1 51  PRO 51  81  81  PRO PRO A . n 
A 1 52  GLN 52  82  82  GLN GLN A . n 
A 1 53  GLU 53  83  83  GLU GLU A . n 
A 1 54  ILE 54  84  84  ILE ILE A . n 
A 1 55  HIS 55  85  85  HIS HIS A . n 
A 1 56  LEU 56  86  86  LEU LEU A . n 
A 1 57  GLU 57  87  87  GLU GLU A . n 
A 1 58  ASN 58  88  88  ASN ASN A . n 
A 1 59  VAL 59  89  89  VAL VAL A . n 
A 1 60  THR 60  90  90  THR THR A . n 
A 1 61  GLU 61  91  91  GLU GLU A . n 
A 1 62  GLU 62  92  92  GLU GLU A . n 
A 1 63  PHE 63  93  93  PHE PHE A . n 
A 1 64  ASN 64  94  94  ASN ASN A . n 
A 1 65  MET 65  95  95  MET MET A . n 
A 1 66  TRP 66  96  96  TRP TRP A . n 
A 1 67  LYS 67  97  97  LYS LYS A . n 
A 1 68  ASN 68  98  98  ASN ASN A . n 
A 1 69  ASN 69  99  99  ASN ASN A . n 
A 1 70  MET 70  100 100 MET MET A . n 
A 1 71  VAL 71  101 101 VAL VAL A . n 
A 1 72  GLU 72  102 102 GLU GLU A . n 
A 1 73  GLN 73  103 103 GLN GLN A . n 
A 1 74  MET 74  104 104 MET MET A . n 
A 1 75  HIS 75  105 105 HIS HIS A . n 
A 1 76  THR 76  106 106 THR THR A . n 
A 1 77  ASP 77  107 107 ASP ASP A . n 
A 1 78  ILE 78  108 108 ILE ILE A . n 
A 1 79  ILE 79  109 109 ILE ILE A . n 
A 1 80  SER 80  110 110 SER SER A . n 
A 1 81  LEU 81  111 111 LEU LEU A . n 
A 1 82  TRP 82  112 112 TRP TRP A . n 
A 1 83  ASP 83  113 113 ASP ASP A . n 
A 1 84  GLN 84  114 114 GLN GLN A . n 
A 1 85  SER 85  115 115 SER SER A . n 
A 1 86  LEU 86  116 116 LEU LEU A . n 
A 1 87  LYS 87  117 117 LYS LYS A . n 
A 1 88  PRO 88  118 118 PRO PRO A . n 
A 1 89  CYS 89  119 119 CYS CYS A . n 
A 1 90  VAL 90  120 120 VAL VAL A . n 
A 1 91  LYS 91  121 121 LYS LYS A . n 
A 1 92  LEU 92  122 122 LEU LEU A . n 
A 1 93  THR 93  123 123 THR THR A . n 
A 1 94  PRO 94  124 124 PRO PRO A . n 
A 1 95  LEU 95  125 125 LEU LEU A . n 
A 1 96  CYS 96  126 126 CYS CYS A . n 
A 1 97  VAL 97  127 127 VAL VAL A . n 
A 1 98  THR 98  128 128 THR THR A . n 
A 1 99  LEU 99  129 129 LEU LEU A . n 
A 1 100 GLN 100 130 130 GLN GLN A . n 
A 1 101 CYS 101 131 131 CYS CYS A . n 
A 1 102 THR 102 132 132 THR THR A . n 
A 1 103 ASN 103 133 133 ASN ASN A . n 
A 1 104 VAL 104 134 134 VAL VAL A . n 
A 1 105 THR 105 135 135 THR THR A . n 
A 1 106 ASN 106 136 136 ASN ASN A . n 
A 1 107 ASN 107 137 137 ASN ASN A . n 
A 1 108 ILE 108 138 138 ILE ILE A . n 
A 1 109 THR 109 139 139 THR THR A . n 
A 1 110 ASP 110 140 140 ASP ASP A . n 
A 1 111 ASP 111 141 141 ASP ASP A . n 
A 1 112 MET 112 150 150 MET MET A . n 
A 1 113 ARG 113 151 151 ARG ARG A . n 
A 1 114 GLY 114 152 152 GLY GLY A . n 
A 1 115 GLU 115 153 153 GLU GLU A . n 
A 1 116 LEU 116 154 154 LEU LEU A . n 
A 1 117 LYS 117 155 155 LYS LYS A . n 
A 1 118 ASN 118 156 156 ASN ASN A . n 
A 1 119 CYS 119 157 157 CYS CYS A . n 
A 1 120 SER 120 158 158 SER SER A . n 
A 1 121 PHE 121 159 159 PHE PHE A . n 
A 1 122 ASN 122 160 160 ASN ASN A . n 
A 1 123 MET 123 161 161 MET MET A . n 
A 1 124 THR 124 162 162 THR THR A . n 
A 1 125 THR 125 163 163 THR THR A . n 
A 1 126 GLU 126 164 164 GLU GLU A . n 
A 1 127 LEU 127 165 165 LEU LEU A . n 
A 1 128 ARG 128 166 166 ARG ARG A . n 
A 1 129 ASP 129 167 167 ASP ASP A . n 
A 1 130 LYS 130 168 168 LYS LYS A . n 
A 1 131 LYS 131 169 169 LYS LYS A . n 
A 1 132 GLN 132 170 170 GLN GLN A . n 
A 1 133 LYS 133 171 171 LYS LYS A . n 
A 1 134 VAL 134 172 172 VAL VAL A . n 
A 1 135 TYR 135 173 173 TYR TYR A . n 
A 1 136 SER 136 174 174 SER SER A . n 
A 1 137 LEU 137 175 175 LEU LEU A . n 
A 1 138 PHE 138 176 176 PHE PHE A . n 
A 1 139 TYR 139 177 177 TYR TYR A . n 
A 1 140 ARG 140 178 178 ARG ARG A . n 
A 1 141 LEU 141 179 179 LEU LEU A . n 
A 1 142 ASP 142 180 180 ASP ASP A . n 
A 1 143 VAL 143 181 181 VAL VAL A . n 
A 1 144 VAL 144 182 182 VAL VAL A . n 
A 1 145 GLN 145 183 183 GLN GLN A . n 
A 1 146 ILE 146 184 184 ILE ILE A . n 
A 1 147 ASN 147 185 185 ASN ASN A . n 
A 1 148 GLU 148 185 ?   ?   ?   A A n 
A 1 149 ASN 149 185 ?   ?   ?   A B n 
A 1 150 GLN 150 185 ?   ?   ?   A C n 
A 1 151 GLY 151 185 ?   ?   ?   A D n 
A 1 152 ASN 152 185 ?   ?   ?   A E n 
A 1 153 ARG 153 185 ?   ?   ?   A F n 
A 1 154 SER 154 185 ?   ?   ?   A G n 
A 1 155 ASN 155 185 ?   ?   ?   A H n 
A 1 156 ASN 156 185 ?   ?   ?   A I n 
A 1 157 SER 157 187 187 SER SER A . n 
A 1 158 ASN 158 188 188 ASN ASN A . n 
A 1 159 LYS 159 189 189 LYS LYS A . n 
A 1 160 GLU 160 190 190 GLU GLU A . n 
A 1 161 TYR 161 191 191 TYR TYR A . n 
A 1 162 ARG 162 192 192 ARG ARG A . n 
A 1 163 LEU 163 193 193 LEU LEU A . n 
A 1 164 ILE 164 194 194 ILE ILE A . n 
A 1 165 ASN 165 195 195 ASN ASN A . n 
A 1 166 CYS 166 196 196 CYS CYS A . n 
A 1 167 ASN 167 197 197 ASN ASN A . n 
A 1 168 THR 168 198 198 THR THR A . n 
A 1 169 SER 169 199 199 SER SER A . n 
A 1 170 ALA 170 200 200 ALA ALA A . n 
A 1 171 ILE 171 201 201 ILE ILE A . n 
A 1 172 THR 172 202 202 THR THR A . n 
A 1 173 GLN 173 203 203 GLN GLN A . n 
A 1 174 ALA 174 204 204 ALA ALA A . n 
A 1 175 CYS 175 205 205 CYS CYS A . n 
A 1 176 PRO 176 206 206 PRO PRO A . n 
A 1 177 LYS 177 207 207 LYS LYS A . n 
A 1 178 VAL 178 208 208 VAL VAL A . n 
A 1 179 SER 179 209 209 SER SER A . n 
A 1 180 PHE 180 210 210 PHE PHE A . n 
A 1 181 GLU 181 211 211 GLU GLU A . n 
A 1 182 PRO 182 212 212 PRO PRO A . n 
A 1 183 ILE 183 213 213 ILE ILE A . n 
A 1 184 PRO 184 214 214 PRO PRO A . n 
A 1 185 ILE 185 215 215 ILE ILE A . n 
A 1 186 HIS 186 216 216 HIS HIS A . n 
A 1 187 TYR 187 217 217 TYR TYR A . n 
A 1 188 CYS 188 218 218 CYS CYS A . n 
A 1 189 ALA 189 219 219 ALA ALA A . n 
A 1 190 PRO 190 220 220 PRO PRO A . n 
A 1 191 ALA 191 221 221 ALA ALA A . n 
A 1 192 GLY 192 222 222 GLY GLY A . n 
A 1 193 PHE 193 223 223 PHE PHE A . n 
A 1 194 ALA 194 224 224 ALA ALA A . n 
A 1 195 ILE 195 225 225 ILE ILE A . n 
A 1 196 LEU 196 226 226 LEU LEU A . n 
A 1 197 LYS 197 227 227 LYS LYS A . n 
A 1 198 CYS 198 228 228 CYS CYS A . n 
A 1 199 LYS 199 229 229 LYS LYS A . n 
A 1 200 ASP 200 230 230 ASP ASP A . n 
A 1 201 LYS 201 231 231 LYS LYS A . n 
A 1 202 LYS 202 232 232 LYS LYS A . n 
A 1 203 PHE 203 233 233 PHE PHE A . n 
A 1 204 ASN 204 234 234 ASN ASN A . n 
A 1 205 GLY 205 235 235 GLY GLY A . n 
A 1 206 THR 206 236 236 THR THR A . n 
A 1 207 GLY 207 237 237 GLY GLY A . n 
A 1 208 PRO 208 238 238 PRO PRO A . n 
A 1 209 CYS 209 239 239 CYS CYS A . n 
A 1 210 PRO 210 240 240 PRO PRO A . n 
A 1 211 SER 211 241 241 SER SER A . n 
A 1 212 VAL 212 242 242 VAL VAL A . n 
A 1 213 SER 213 243 243 SER SER A . n 
A 1 214 THR 214 244 244 THR THR A . n 
A 1 215 VAL 215 245 245 VAL VAL A . n 
A 1 216 GLN 216 246 246 GLN GLN A . n 
A 1 217 CYS 217 247 247 CYS CYS A . n 
A 1 218 THR 218 248 248 THR THR A . n 
A 1 219 HIS 219 249 249 HIS HIS A . n 
A 1 220 GLY 220 250 250 GLY GLY A . n 
A 1 221 ILE 221 251 251 ILE ILE A . n 
A 1 222 LYS 222 252 252 LYS LYS A . n 
A 1 223 PRO 223 253 253 PRO PRO A . n 
A 1 224 VAL 224 254 254 VAL VAL A . n 
A 1 225 VAL 225 255 255 VAL VAL A . n 
A 1 226 SER 226 256 256 SER SER A . n 
A 1 227 THR 227 257 257 THR THR A . n 
A 1 228 GLN 228 258 258 GLN GLN A . n 
A 1 229 LEU 229 259 259 LEU LEU A . n 
A 1 230 LEU 230 260 260 LEU LEU A . n 
A 1 231 LEU 231 261 261 LEU LEU A . n 
A 1 232 ASN 232 262 262 ASN ASN A . n 
A 1 233 GLY 233 263 263 GLY GLY A . n 
A 1 234 SER 234 264 264 SER SER A . n 
A 1 235 LEU 235 265 265 LEU LEU A . n 
A 1 236 ALA 236 266 266 ALA ALA A . n 
A 1 237 GLU 237 267 267 GLU GLU A . n 
A 1 238 GLU 238 268 268 GLU GLU A . n 
A 1 239 GLU 239 269 269 GLU GLU A . n 
A 1 240 VAL 240 270 270 VAL VAL A . n 
A 1 241 MET 241 271 271 MET MET A . n 
A 1 242 ILE 242 272 272 ILE ILE A . n 
A 1 243 ARG 243 273 273 ARG ARG A . n 
A 1 244 SER 244 274 274 SER SER A . n 
A 1 245 GLU 245 275 275 GLU GLU A . n 
A 1 246 ASN 246 276 276 ASN ASN A . n 
A 1 247 ILE 247 277 277 ILE ILE A . n 
A 1 248 THR 248 278 278 THR THR A . n 
A 1 249 ASN 249 279 279 ASN ASN A . n 
A 1 250 ASN 250 280 280 ASN ASN A . n 
A 1 251 ALA 251 281 281 ALA ALA A . n 
A 1 252 LYS 252 282 282 LYS LYS A . n 
A 1 253 ASN 253 283 283 ASN ASN A . n 
A 1 254 ILE 254 284 284 ILE ILE A . n 
A 1 255 LEU 255 285 285 LEU LEU A . n 
A 1 256 VAL 256 286 286 VAL VAL A . n 
A 1 257 GLN 257 287 287 GLN GLN A . n 
A 1 258 PHE 258 288 288 PHE PHE A . n 
A 1 259 ASN 259 289 289 ASN ASN A . n 
A 1 260 THR 260 290 290 THR THR A . n 
A 1 261 PRO 261 291 291 PRO PRO A . n 
A 1 262 VAL 262 292 292 VAL VAL A . n 
A 1 263 GLN 263 293 293 GLN GLN A . n 
A 1 264 ILE 264 294 294 ILE ILE A . n 
A 1 265 ASN 265 295 295 ASN ASN A . n 
A 1 266 CYS 266 296 296 CYS CYS A . n 
A 1 267 THR 267 297 297 THR THR A . n 
A 1 268 ARG 268 298 298 ARG ARG A . n 
A 1 269 PRO 269 299 299 PRO PRO A . n 
A 1 270 ASN 270 300 300 ASN ASN A . n 
A 1 271 ASN 271 301 301 ASN ASN A . n 
A 1 272 ASN 272 302 302 ASN ASN A . n 
A 1 273 THR 273 303 303 THR THR A . n 
A 1 274 ARG 274 304 304 ARG ARG A . n 
A 1 275 LYS 275 305 305 LYS LYS A . n 
A 1 276 SER 276 306 306 SER SER A . n 
A 1 277 ILE 277 307 307 ILE ILE A . n 
A 1 278 ARG 278 308 308 ARG ARG A . n 
A 1 279 ILE 279 309 309 ILE ILE A . n 
A 1 280 GLY 280 312 312 GLY GLY A . n 
A 1 281 PRO 281 313 313 PRO PRO A . n 
A 1 282 GLY 282 314 314 GLY GLY A . n 
A 1 283 GLN 283 315 315 GLN GLN A . n 
A 1 284 ALA 284 316 316 ALA ALA A . n 
A 1 285 PHE 285 317 317 PHE PHE A . n 
A 1 286 TYR 286 318 318 TYR TYR A . n 
A 1 287 ALA 287 319 319 ALA ALA A . n 
A 1 288 THR 288 320 320 THR THR A . n 
A 1 289 GLY 289 321 321 GLY GLY A . n 
A 1 290 ASP 290 321 321 ASP ASP A A n 
A 1 291 ILE 291 322 322 ILE ILE A . n 
A 1 292 ILE 292 323 323 ILE ILE A . n 
A 1 293 GLY 293 324 324 GLY GLY A . n 
A 1 294 ASP 294 325 325 ASP ASP A . n 
A 1 295 ILE 295 326 326 ILE ILE A . n 
A 1 296 ARG 296 327 327 ARG ARG A . n 
A 1 297 GLN 297 328 328 GLN GLN A . n 
A 1 298 ALA 298 329 329 ALA ALA A . n 
A 1 299 HIS 299 330 330 HIS HIS A . n 
A 1 300 CYS 300 331 331 CYS CYS A . n 
A 1 301 ASN 301 332 332 ASN ASN A . n 
A 1 302 VAL 302 333 333 VAL VAL A . n 
A 1 303 SER 303 334 334 SER SER A . n 
A 1 304 LYS 304 335 335 LYS LYS A . n 
A 1 305 ALA 305 336 336 ALA ALA A . n 
A 1 306 THR 306 337 337 THR THR A . n 
A 1 307 TRP 307 338 338 TRP TRP A . n 
A 1 308 ASN 308 339 339 ASN ASN A . n 
A 1 309 GLU 309 340 340 GLU GLU A . n 
A 1 310 THR 310 341 341 THR THR A . n 
A 1 311 LEU 311 342 342 LEU LEU A . n 
A 1 312 GLY 312 343 343 GLY GLY A . n 
A 1 313 LYS 313 344 344 LYS LYS A . n 
A 1 314 VAL 314 345 345 VAL VAL A . n 
A 1 315 VAL 315 346 346 VAL VAL A . n 
A 1 316 LYS 316 347 347 LYS LYS A . n 
A 1 317 GLN 317 348 348 GLN GLN A . n 
A 1 318 LEU 318 349 349 LEU LEU A . n 
A 1 319 ARG 319 350 350 ARG ARG A . n 
A 1 320 LYS 320 351 351 LYS LYS A . n 
A 1 321 HIS 321 352 352 HIS HIS A . n 
A 1 322 PHE 322 353 353 PHE PHE A . n 
A 1 323 GLY 323 354 354 GLY GLY A . n 
A 1 324 ASN 324 355 355 ASN ASN A . n 
A 1 325 ASN 325 356 356 ASN ASN A . n 
A 1 326 THR 326 357 357 THR THR A . n 
A 1 327 ILE 327 358 358 ILE ILE A . n 
A 1 328 ILE 328 359 359 ILE ILE A . n 
A 1 329 ARG 329 360 360 ARG ARG A . n 
A 1 330 PHE 330 361 361 PHE PHE A . n 
A 1 331 ALA 331 362 362 ALA ALA A . n 
A 1 332 ASN 332 363 363 ASN ASN A . n 
A 1 333 SER 333 364 364 SER SER A . n 
A 1 334 SER 334 365 365 SER SER A . n 
A 1 335 GLY 335 366 366 GLY GLY A . n 
A 1 336 GLY 336 367 367 GLY GLY A . n 
A 1 337 ASP 337 368 368 ASP ASP A . n 
A 1 338 LEU 338 369 369 LEU LEU A . n 
A 1 339 GLU 339 370 370 GLU GLU A . n 
A 1 340 VAL 340 371 371 VAL VAL A . n 
A 1 341 THR 341 372 372 THR THR A . n 
A 1 342 THR 342 373 373 THR THR A . n 
A 1 343 HIS 343 374 374 HIS HIS A . n 
A 1 344 SER 344 375 375 SER SER A . n 
A 1 345 PHE 345 376 376 PHE PHE A . n 
A 1 346 ASN 346 377 377 ASN ASN A . n 
A 1 347 CYS 347 378 378 CYS CYS A . n 
A 1 348 GLY 348 379 379 GLY GLY A . n 
A 1 349 GLY 349 380 380 GLY GLY A . n 
A 1 350 GLU 350 381 381 GLU GLU A . n 
A 1 351 PHE 351 382 382 PHE PHE A . n 
A 1 352 PHE 352 383 383 PHE PHE A . n 
A 1 353 TYR 353 384 384 TYR TYR A . n 
A 1 354 CYS 354 385 385 CYS CYS A . n 
A 1 355 ASN 355 386 386 ASN ASN A . n 
A 1 356 THR 356 387 387 THR THR A . n 
A 1 357 SER 357 388 388 SER SER A . n 
A 1 358 GLY 358 389 389 GLY GLY A . n 
A 1 359 LEU 359 390 390 LEU LEU A . n 
A 1 360 PHE 360 391 391 PHE PHE A . n 
A 1 361 ASN 361 392 392 ASN ASN A . n 
A 1 362 SER 362 393 393 SER SER A . n 
A 1 363 THR 363 394 394 THR THR A . n 
A 1 364 TRP 364 395 395 TRP TRP A . n 
A 1 365 ILE 365 396 396 ILE ILE A . n 
A 1 366 SER 366 397 397 SER SER A . n 
A 1 367 ASN 367 398 398 ASN ASN A . n 
A 1 368 THR 368 400 ?   ?   ?   A . n 
A 1 369 SER 369 401 ?   ?   ?   A . n 
A 1 370 VAL 370 402 ?   ?   ?   A . n 
A 1 371 GLN 371 403 ?   ?   ?   A . n 
A 1 372 GLY 372 404 ?   ?   ?   A . n 
A 1 373 SER 373 405 ?   ?   ?   A . n 
A 1 374 ASN 374 406 ?   ?   ?   A . n 
A 1 375 SER 375 407 ?   ?   ?   A . n 
A 1 376 THR 376 408 ?   ?   ?   A . n 
A 1 377 GLY 377 409 ?   ?   ?   A . n 
A 1 378 SER 378 410 ?   ?   ?   A . n 
A 1 379 ASN 379 411 411 ASN ASN A . n 
A 1 380 ASP 380 412 412 ASP ASP A . n 
A 1 381 SER 381 413 413 SER SER A . n 
A 1 382 ILE 382 414 414 ILE ILE A . n 
A 1 383 THR 383 415 415 THR THR A . n 
A 1 384 LEU 384 416 416 LEU LEU A . n 
A 1 385 PRO 385 417 417 PRO PRO A . n 
A 1 386 CYS 386 418 418 CYS CYS A . n 
A 1 387 ARG 387 419 419 ARG ARG A . n 
A 1 388 ILE 388 420 420 ILE ILE A . n 
A 1 389 LYS 389 421 421 LYS LYS A . n 
A 1 390 GLN 390 422 422 GLN GLN A . n 
A 1 391 ILE 391 423 423 ILE ILE A . n 
A 1 392 ILE 392 424 424 ILE ILE A . n 
A 1 393 ASN 393 425 425 ASN ASN A . n 
A 1 394 MET 394 426 426 MET MET A . n 
A 1 395 TRP 395 427 427 TRP TRP A . n 
A 1 396 GLN 396 428 428 GLN GLN A . n 
A 1 397 ARG 397 429 429 ARG ARG A . n 
A 1 398 ILE 398 430 430 ILE ILE A . n 
A 1 399 GLY 399 431 431 GLY GLY A . n 
A 1 400 GLN 400 432 432 GLN GLN A . n 
A 1 401 ALA 401 433 433 ALA ALA A . n 
A 1 402 MET 402 434 434 MET MET A . n 
A 1 403 TYR 403 435 435 TYR TYR A . n 
A 1 404 ALA 404 436 436 ALA ALA A . n 
A 1 405 PRO 405 437 437 PRO PRO A . n 
A 1 406 PRO 406 438 438 PRO PRO A . n 
A 1 407 ILE 407 439 439 ILE ILE A . n 
A 1 408 GLN 408 440 440 GLN GLN A . n 
A 1 409 GLY 409 441 441 GLY GLY A . n 
A 1 410 VAL 410 442 442 VAL VAL A . n 
A 1 411 ILE 411 443 443 ILE ILE A . n 
A 1 412 ARG 412 444 444 ARG ARG A . n 
A 1 413 CYS 413 445 445 CYS CYS A . n 
A 1 414 VAL 414 446 446 VAL VAL A . n 
A 1 415 SER 415 447 447 SER SER A . n 
A 1 416 ASN 416 448 448 ASN ASN A . n 
A 1 417 ILE 417 449 449 ILE ILE A . n 
A 1 418 THR 418 450 450 THR THR A . n 
A 1 419 GLY 419 451 451 GLY GLY A . n 
A 1 420 LEU 420 452 452 LEU LEU A . n 
A 1 421 ILE 421 453 453 ILE ILE A . n 
A 1 422 LEU 422 454 454 LEU LEU A . n 
A 1 423 THR 423 455 455 THR THR A . n 
A 1 424 ARG 424 456 456 ARG ARG A . n 
A 1 425 ASP 425 457 457 ASP ASP A . n 
A 1 426 GLY 426 458 458 GLY GLY A . n 
A 1 427 GLY 427 459 459 GLY GLY A . n 
A 1 428 SER 428 460 460 SER SER A . n 
A 1 429 THR 429 461 461 THR THR A . n 
A 1 430 ASN 430 462 462 ASN ASN A . n 
A 1 431 SER 431 463 463 SER SER A . n 
A 1 432 THR 432 464 464 THR THR A . n 
A 1 433 THR 433 465 465 THR THR A . n 
A 1 434 GLU 434 466 466 GLU GLU A . n 
A 1 435 THR 435 467 467 THR THR A . n 
A 1 436 PHE 436 468 468 PHE PHE A . n 
A 1 437 ARG 437 469 469 ARG ARG A . n 
A 1 438 PRO 438 470 470 PRO PRO A . n 
A 1 439 GLY 439 471 471 GLY GLY A . n 
A 1 440 GLY 440 472 472 GLY GLY A . n 
A 1 441 GLY 441 473 473 GLY GLY A . n 
A 1 442 ASP 442 474 474 ASP ASP A . n 
A 1 443 MET 443 475 475 MET MET A . n 
A 1 444 ARG 444 476 476 ARG ARG A . n 
A 1 445 ASP 445 477 477 ASP ASP A . n 
A 1 446 ASN 446 478 478 ASN ASN A . n 
A 1 447 TRP 447 479 479 TRP TRP A . n 
A 1 448 ARG 448 480 480 ARG ARG A . n 
A 1 449 SER 449 481 481 SER SER A . n 
A 1 450 GLU 450 482 482 GLU GLU A . n 
A 1 451 LEU 451 483 483 LEU LEU A . n 
A 1 452 TYR 452 484 484 TYR TYR A . n 
A 1 453 LYS 453 485 485 LYS LYS A . n 
A 1 454 TYR 454 486 486 TYR TYR A . n 
A 1 455 LYS 455 487 487 LYS LYS A . n 
A 1 456 VAL 456 488 488 VAL VAL A . n 
A 1 457 VAL 457 489 489 VAL VAL A . n 
A 1 458 LYS 458 490 490 LYS LYS A . n 
A 1 459 ILE 459 491 491 ILE ILE A . n 
A 1 460 GLU 460 492 492 GLU GLU A . n 
A 1 461 PRO 461 493 493 PRO PRO A . n 
A 1 462 LEU 462 494 494 LEU LEU A . n 
A 1 463 GLY 463 495 495 GLY GLY A . n 
A 1 464 VAL 464 496 496 VAL VAL A . n 
A 1 465 ALA 465 497 497 ALA ALA A . n 
A 1 466 PRO 466 498 498 PRO PRO A . n 
A 1 467 THR 467 499 499 THR THR A . n 
A 1 468 ARG 468 500 500 ARG ARG A . n 
A 1 469 CYS 469 501 501 CYS CYS A . n 
A 1 470 LYS 470 502 502 LYS LYS A . n 
A 1 471 ARG 471 503 503 ARG ARG A . n 
A 1 472 ARG 472 504 504 ARG ARG A . n 
A 1 473 VAL 473 505 505 VAL VAL A . n 
A 1 474 VAL 474 506 506 VAL VAL A . n 
A 1 475 GLY 475 507 507 GLY GLY A . n 
A 1 476 ARG 476 508 ?   ?   ?   A . n 
A 1 477 ARG 477 509 ?   ?   ?   A . n 
A 1 478 ARG 478 510 ?   ?   ?   A . n 
A 1 479 ARG 479 511 ?   ?   ?   A . n 
A 1 480 ARG 480 512 ?   ?   ?   A . n 
A 1 481 ARG 481 513 ?   ?   ?   A . n 
B 2 1   ALA 1   512 512 ALA ALA B . n 
B 2 2   VAL 2   513 513 VAL VAL B . n 
B 2 3   GLY 3   514 514 GLY GLY B . n 
B 2 4   ILE 4   515 515 ILE ILE B . n 
B 2 5   GLY 5   516 516 GLY GLY B . n 
B 2 6   ALA 6   517 517 ALA ALA B . n 
B 2 7   VAL 7   518 518 VAL VAL B . n 
B 2 8   PHE 8   519 519 PHE PHE B . n 
B 2 9   LEU 9   520 520 LEU LEU B . n 
B 2 10  GLY 10  521 521 GLY GLY B . n 
B 2 11  PHE 11  522 522 PHE PHE B . n 
B 2 12  LEU 12  523 523 LEU LEU B . n 
B 2 13  GLY 13  524 524 GLY GLY B . n 
B 2 14  ALA 14  525 525 ALA ALA B . n 
B 2 15  ALA 15  526 526 ALA ALA B . n 
B 2 16  GLY 16  527 527 GLY GLY B . n 
B 2 17  SER 17  528 528 SER SER B . n 
B 2 18  THR 18  529 529 THR THR B . n 
B 2 19  MET 19  530 530 MET MET B . n 
B 2 20  GLY 20  531 531 GLY GLY B . n 
B 2 21  ALA 21  532 532 ALA ALA B . n 
B 2 22  ALA 22  533 533 ALA ALA B . n 
B 2 23  SER 23  534 534 SER SER B . n 
B 2 24  MET 24  535 535 MET MET B . n 
B 2 25  THR 25  536 536 THR THR B . n 
B 2 26  LEU 26  537 537 LEU LEU B . n 
B 2 27  THR 27  538 538 THR THR B . n 
B 2 28  VAL 28  539 539 VAL VAL B . n 
B 2 29  GLN 29  540 540 GLN GLN B . n 
B 2 30  ALA 30  541 541 ALA ALA B . n 
B 2 31  ARG 31  542 542 ARG ARG B . n 
B 2 32  ASN 32  543 543 ASN ASN B . n 
B 2 33  LEU 33  544 544 LEU LEU B . n 
B 2 34  LEU 34  545 545 LEU LEU B . n 
B 2 35  SER 35  546 546 SER SER B . n 
B 2 36  GLY 36  547 547 GLY GLY B . n 
B 2 37  ILE 37  548 ?   ?   ?   B . n 
B 2 38  VAL 38  549 ?   ?   ?   B . n 
B 2 39  GLN 39  550 ?   ?   ?   B . n 
B 2 40  GLN 40  551 ?   ?   ?   B . n 
B 2 41  GLN 41  552 ?   ?   ?   B . n 
B 2 42  SER 42  553 ?   ?   ?   B . n 
B 2 43  ASN 43  554 ?   ?   ?   B . n 
B 2 44  LEU 44  555 ?   ?   ?   B . n 
B 2 45  LEU 45  556 ?   ?   ?   B . n 
B 2 46  ARG 46  557 ?   ?   ?   B . n 
B 2 47  ALA 47  558 ?   ?   ?   B . n 
B 2 48  ILE 48  559 ?   ?   ?   B . n 
B 2 49  GLU 49  560 ?   ?   ?   B . n 
B 2 50  ALA 50  561 ?   ?   ?   B . n 
B 2 51  GLN 51  562 ?   ?   ?   B . n 
B 2 52  GLN 52  563 ?   ?   ?   B . n 
B 2 53  HIS 53  564 ?   ?   ?   B . n 
B 2 54  LEU 54  565 ?   ?   ?   B . n 
B 2 55  LEU 55  566 ?   ?   ?   B . n 
B 2 56  LYS 56  567 ?   ?   ?   B . n 
B 2 57  LEU 57  568 ?   ?   ?   B . n 
B 2 58  THR 58  569 569 THR THR B . n 
B 2 59  VAL 59  570 570 VAL VAL B . n 
B 2 60  TRP 60  571 571 TRP TRP B . n 
B 2 61  GLY 61  572 572 GLY GLY B . n 
B 2 62  ILE 62  573 573 ILE ILE B . n 
B 2 63  LYS 63  574 574 LYS LYS B . n 
B 2 64  GLN 64  575 575 GLN GLN B . n 
B 2 65  LEU 65  576 576 LEU LEU B . n 
B 2 66  GLN 66  577 577 GLN GLN B . n 
B 2 67  ALA 67  578 578 ALA ALA B . n 
B 2 68  ARG 68  579 579 ARG ARG B . n 
B 2 69  VAL 69  580 580 VAL VAL B . n 
B 2 70  LEU 70  581 581 LEU LEU B . n 
B 2 71  ALA 71  582 582 ALA ALA B . n 
B 2 72  VAL 72  583 583 VAL VAL B . n 
B 2 73  GLU 73  584 584 GLU GLU B . n 
B 2 74  ARG 74  585 585 ARG ARG B . n 
B 2 75  TYR 75  586 586 TYR TYR B . n 
B 2 76  LEU 76  587 587 LEU LEU B . n 
B 2 77  ARG 77  588 588 ARG ARG B . n 
B 2 78  ASP 78  589 589 ASP ASP B . n 
B 2 79  GLN 79  590 590 GLN GLN B . n 
B 2 80  GLN 80  591 591 GLN GLN B . n 
B 2 81  LEU 81  592 592 LEU LEU B . n 
B 2 82  LEU 82  593 593 LEU LEU B . n 
B 2 83  GLY 83  594 594 GLY GLY B . n 
B 2 84  ILE 84  595 595 ILE ILE B . n 
B 2 85  TRP 85  596 596 TRP TRP B . n 
B 2 86  GLY 86  597 597 GLY GLY B . n 
B 2 87  CYS 87  598 598 CYS CYS B . n 
B 2 88  SER 88  599 599 SER SER B . n 
B 2 89  GLY 89  600 600 GLY GLY B . n 
B 2 90  LYS 90  601 601 LYS LYS B . n 
B 2 91  LEU 91  602 602 LEU LEU B . n 
B 2 92  ILE 92  603 603 ILE ILE B . n 
B 2 93  CYS 93  604 604 CYS CYS B . n 
B 2 94  CYS 94  605 605 CYS CYS B . n 
B 2 95  THR 95  606 606 THR THR B . n 
B 2 96  ASN 96  607 607 ASN ASN B . n 
B 2 97  VAL 97  608 608 VAL VAL B . n 
B 2 98  PRO 98  609 609 PRO PRO B . n 
B 2 99  TRP 99  610 610 TRP TRP B . n 
B 2 100 ASN 100 611 611 ASN ASN B . n 
B 2 101 SER 101 612 612 SER SER B . n 
B 2 102 SER 102 613 613 SER SER B . n 
B 2 103 TRP 103 614 614 TRP TRP B . n 
B 2 104 SER 104 615 615 SER SER B . n 
B 2 105 ASN 105 616 616 ASN ASN B . n 
B 2 106 ARG 106 617 617 ARG ARG B . n 
B 2 107 ASN 107 618 618 ASN ASN B . n 
B 2 108 LEU 108 619 619 LEU LEU B . n 
B 2 109 SER 109 620 620 SER SER B . n 
B 2 110 GLU 110 621 621 GLU GLU B . n 
B 2 111 ILE 111 622 622 ILE ILE B . n 
B 2 112 TRP 112 623 623 TRP TRP B . n 
B 2 113 ASP 113 624 624 ASP ASP B . n 
B 2 114 ASN 114 625 625 ASN ASN B . n 
B 2 115 MET 115 626 626 MET MET B . n 
B 2 116 THR 116 627 627 THR THR B . n 
B 2 117 TRP 117 628 628 TRP TRP B . n 
B 2 118 LEU 118 629 629 LEU LEU B . n 
B 2 119 GLN 119 630 630 GLN GLN B . n 
B 2 120 TRP 120 631 631 TRP TRP B . n 
B 2 121 ASP 121 632 632 ASP ASP B . n 
B 2 122 LYS 122 633 633 LYS LYS B . n 
B 2 123 GLU 123 634 634 GLU GLU B . n 
B 2 124 ILE 124 635 635 ILE ILE B . n 
B 2 125 SER 125 636 636 SER SER B . n 
B 2 126 ASN 126 637 637 ASN ASN B . n 
B 2 127 TYR 127 638 638 TYR TYR B . n 
B 2 128 THR 128 639 639 THR THR B . n 
B 2 129 GLN 129 640 640 GLN GLN B . n 
B 2 130 ILE 130 641 641 ILE ILE B . n 
B 2 131 ILE 131 642 642 ILE ILE B . n 
B 2 132 TYR 132 643 643 TYR TYR B . n 
B 2 133 GLY 133 644 644 GLY GLY B . n 
B 2 134 LEU 134 645 645 LEU LEU B . n 
B 2 135 LEU 135 646 646 LEU LEU B . n 
B 2 136 GLU 136 647 647 GLU GLU B . n 
B 2 137 GLU 137 648 648 GLU GLU B . n 
B 2 138 SER 138 649 649 SER SER B . n 
B 2 139 GLN 139 650 650 GLN GLN B . n 
B 2 140 ASN 140 651 651 ASN ASN B . n 
B 2 141 GLN 141 652 652 GLN GLN B . n 
B 2 142 GLN 142 653 653 GLN GLN B . n 
B 2 143 GLU 143 654 654 GLU GLU B . n 
B 2 144 LYS 144 655 655 LYS LYS B . n 
B 2 145 ASN 145 656 656 ASN ASN B . n 
B 2 146 GLU 146 657 657 GLU GLU B . n 
B 2 147 GLN 147 658 658 GLN GLN B . n 
B 2 148 ASP 148 659 659 ASP ASP B . n 
B 2 149 LEU 149 660 660 LEU LEU B . n 
B 2 150 LEU 150 661 661 LEU LEU B . n 
B 2 151 ALA 151 662 662 ALA ALA B . n 
B 2 152 LEU 152 663 663 LEU LEU B . n 
B 2 153 ASP 153 664 664 ASP ASP B . n 
C 1 1   ALA 1   31  31  ALA ALA C . n 
C 1 2   GLU 2   32  32  GLU GLU C . n 
C 1 3   ASN 3   33  33  ASN ASN C . n 
C 1 4   LEU 4   34  34  LEU LEU C . n 
C 1 5   TRP 5   35  35  TRP TRP C . n 
C 1 6   VAL 6   36  36  VAL VAL C . n 
C 1 7   THR 7   37  37  THR THR C . n 
C 1 8   VAL 8   38  38  VAL VAL C . n 
C 1 9   TYR 9   39  39  TYR TYR C . n 
C 1 10  TYR 10  40  40  TYR TYR C . n 
C 1 11  GLY 11  41  41  GLY GLY C . n 
C 1 12  VAL 12  42  42  VAL VAL C . n 
C 1 13  PRO 13  43  43  PRO PRO C . n 
C 1 14  VAL 14  44  44  VAL VAL C . n 
C 1 15  TRP 15  45  45  TRP TRP C . n 
C 1 16  LYS 16  46  46  LYS LYS C . n 
C 1 17  ASP 17  47  47  ASP ASP C . n 
C 1 18  ALA 18  48  48  ALA ALA C . n 
C 1 19  GLU 19  49  49  GLU GLU C . n 
C 1 20  THR 20  50  50  THR THR C . n 
C 1 21  THR 21  51  51  THR THR C . n 
C 1 22  LEU 22  52  52  LEU LEU C . n 
C 1 23  PHE 23  53  53  PHE PHE C . n 
C 1 24  CYS 24  54  54  CYS CYS C . n 
C 1 25  ALA 25  55  55  ALA ALA C . n 
C 1 26  SER 26  56  56  SER SER C . n 
C 1 27  ASP 27  57  57  ASP ASP C . n 
C 1 28  ALA 28  58  58  ALA ALA C . n 
C 1 29  LYS 29  59  59  LYS LYS C . n 
C 1 30  ALA 30  60  60  ALA ALA C . n 
C 1 31  TYR 31  61  61  TYR TYR C . n 
C 1 32  GLU 32  62  62  GLU GLU C . n 
C 1 33  THR 33  63  63  THR THR C . n 
C 1 34  GLU 34  64  64  GLU GLU C . n 
C 1 35  LYS 35  65  65  LYS LYS C . n 
C 1 36  HIS 36  66  66  HIS HIS C . n 
C 1 37  ASN 37  67  67  ASN ASN C . n 
C 1 38  VAL 38  68  68  VAL VAL C . n 
C 1 39  TRP 39  69  69  TRP TRP C . n 
C 1 40  ALA 40  70  70  ALA ALA C . n 
C 1 41  THR 41  71  71  THR THR C . n 
C 1 42  HIS 42  72  72  HIS HIS C . n 
C 1 43  ALA 43  73  73  ALA ALA C . n 
C 1 44  CYS 44  74  74  CYS CYS C . n 
C 1 45  VAL 45  75  75  VAL VAL C . n 
C 1 46  PRO 46  76  76  PRO PRO C . n 
C 1 47  THR 47  77  77  THR THR C . n 
C 1 48  ASP 48  78  78  ASP ASP C . n 
C 1 49  PRO 49  79  79  PRO PRO C . n 
C 1 50  ASN 50  80  80  ASN ASN C . n 
C 1 51  PRO 51  81  81  PRO PRO C . n 
C 1 52  GLN 52  82  82  GLN GLN C . n 
C 1 53  GLU 53  83  83  GLU GLU C . n 
C 1 54  ILE 54  84  84  ILE ILE C . n 
C 1 55  HIS 55  85  85  HIS HIS C . n 
C 1 56  LEU 56  86  86  LEU LEU C . n 
C 1 57  GLU 57  87  87  GLU GLU C . n 
C 1 58  ASN 58  88  88  ASN ASN C . n 
C 1 59  VAL 59  89  89  VAL VAL C . n 
C 1 60  THR 60  90  90  THR THR C . n 
C 1 61  GLU 61  91  91  GLU GLU C . n 
C 1 62  GLU 62  92  92  GLU GLU C . n 
C 1 63  PHE 63  93  93  PHE PHE C . n 
C 1 64  ASN 64  94  94  ASN ASN C . n 
C 1 65  MET 65  95  95  MET MET C . n 
C 1 66  TRP 66  96  96  TRP TRP C . n 
C 1 67  LYS 67  97  97  LYS LYS C . n 
C 1 68  ASN 68  98  98  ASN ASN C . n 
C 1 69  ASN 69  99  99  ASN ASN C . n 
C 1 70  MET 70  100 100 MET MET C . n 
C 1 71  VAL 71  101 101 VAL VAL C . n 
C 1 72  GLU 72  102 102 GLU GLU C . n 
C 1 73  GLN 73  103 103 GLN GLN C . n 
C 1 74  MET 74  104 104 MET MET C . n 
C 1 75  HIS 75  105 105 HIS HIS C . n 
C 1 76  THR 76  106 106 THR THR C . n 
C 1 77  ASP 77  107 107 ASP ASP C . n 
C 1 78  ILE 78  108 108 ILE ILE C . n 
C 1 79  ILE 79  109 109 ILE ILE C . n 
C 1 80  SER 80  110 110 SER SER C . n 
C 1 81  LEU 81  111 111 LEU LEU C . n 
C 1 82  TRP 82  112 112 TRP TRP C . n 
C 1 83  ASP 83  113 113 ASP ASP C . n 
C 1 84  GLN 84  114 114 GLN GLN C . n 
C 1 85  SER 85  115 115 SER SER C . n 
C 1 86  LEU 86  116 116 LEU LEU C . n 
C 1 87  LYS 87  117 117 LYS LYS C . n 
C 1 88  PRO 88  118 118 PRO PRO C . n 
C 1 89  CYS 89  119 119 CYS CYS C . n 
C 1 90  VAL 90  120 120 VAL VAL C . n 
C 1 91  LYS 91  121 121 LYS LYS C . n 
C 1 92  LEU 92  122 122 LEU LEU C . n 
C 1 93  THR 93  123 123 THR THR C . n 
C 1 94  PRO 94  124 124 PRO PRO C . n 
C 1 95  LEU 95  125 125 LEU LEU C . n 
C 1 96  CYS 96  126 126 CYS CYS C . n 
C 1 97  VAL 97  127 127 VAL VAL C . n 
C 1 98  THR 98  128 128 THR THR C . n 
C 1 99  LEU 99  129 129 LEU LEU C . n 
C 1 100 GLN 100 130 130 GLN GLN C . n 
C 1 101 CYS 101 131 131 CYS CYS C . n 
C 1 102 THR 102 132 132 THR THR C . n 
C 1 103 ASN 103 133 133 ASN ASN C . n 
C 1 104 VAL 104 134 134 VAL VAL C . n 
C 1 105 THR 105 135 135 THR THR C . n 
C 1 106 ASN 106 136 136 ASN ASN C . n 
C 1 107 ASN 107 137 137 ASN ASN C . n 
C 1 108 ILE 108 138 138 ILE ILE C . n 
C 1 109 THR 109 139 139 THR THR C . n 
C 1 110 ASP 110 140 140 ASP ASP C . n 
C 1 111 ASP 111 141 141 ASP ASP C . n 
C 1 112 MET 112 150 150 MET MET C . n 
C 1 113 ARG 113 151 151 ARG ARG C . n 
C 1 114 GLY 114 152 152 GLY GLY C . n 
C 1 115 GLU 115 153 153 GLU GLU C . n 
C 1 116 LEU 116 154 154 LEU LEU C . n 
C 1 117 LYS 117 155 155 LYS LYS C . n 
C 1 118 ASN 118 156 156 ASN ASN C . n 
C 1 119 CYS 119 157 157 CYS CYS C . n 
C 1 120 SER 120 158 158 SER SER C . n 
C 1 121 PHE 121 159 159 PHE PHE C . n 
C 1 122 ASN 122 160 160 ASN ASN C . n 
C 1 123 MET 123 161 161 MET MET C . n 
C 1 124 THR 124 162 162 THR THR C . n 
C 1 125 THR 125 163 163 THR THR C . n 
C 1 126 GLU 126 164 164 GLU GLU C . n 
C 1 127 LEU 127 165 165 LEU LEU C . n 
C 1 128 ARG 128 166 166 ARG ARG C . n 
C 1 129 ASP 129 167 167 ASP ASP C . n 
C 1 130 LYS 130 168 168 LYS LYS C . n 
C 1 131 LYS 131 169 169 LYS LYS C . n 
C 1 132 GLN 132 170 170 GLN GLN C . n 
C 1 133 LYS 133 171 171 LYS LYS C . n 
C 1 134 VAL 134 172 172 VAL VAL C . n 
C 1 135 TYR 135 173 173 TYR TYR C . n 
C 1 136 SER 136 174 174 SER SER C . n 
C 1 137 LEU 137 175 175 LEU LEU C . n 
C 1 138 PHE 138 176 176 PHE PHE C . n 
C 1 139 TYR 139 177 177 TYR TYR C . n 
C 1 140 ARG 140 178 178 ARG ARG C . n 
C 1 141 LEU 141 179 179 LEU LEU C . n 
C 1 142 ASP 142 180 180 ASP ASP C . n 
C 1 143 VAL 143 181 181 VAL VAL C . n 
C 1 144 VAL 144 182 182 VAL VAL C . n 
C 1 145 GLN 145 183 183 GLN GLN C . n 
C 1 146 ILE 146 184 184 ILE ILE C . n 
C 1 147 ASN 147 185 185 ASN ASN C . n 
C 1 148 GLU 148 185 ?   ?   ?   C A n 
C 1 149 ASN 149 185 ?   ?   ?   C B n 
C 1 150 GLN 150 185 ?   ?   ?   C C n 
C 1 151 GLY 151 185 ?   ?   ?   C D n 
C 1 152 ASN 152 185 ?   ?   ?   C E n 
C 1 153 ARG 153 185 ?   ?   ?   C F n 
C 1 154 SER 154 185 ?   ?   ?   C G n 
C 1 155 ASN 155 185 ?   ?   ?   C H n 
C 1 156 ASN 156 185 ?   ?   ?   C I n 
C 1 157 SER 157 185 ?   ?   ?   C J n 
C 1 158 ASN 158 185 ?   ?   ?   C K n 
C 1 159 LYS 159 185 ?   ?   ?   C L n 
C 1 160 GLU 160 190 190 GLU GLU C . n 
C 1 161 TYR 161 191 191 TYR TYR C . n 
C 1 162 ARG 162 192 192 ARG ARG C . n 
C 1 163 LEU 163 193 193 LEU LEU C . n 
C 1 164 ILE 164 194 194 ILE ILE C . n 
C 1 165 ASN 165 195 195 ASN ASN C . n 
C 1 166 CYS 166 196 196 CYS CYS C . n 
C 1 167 ASN 167 197 197 ASN ASN C . n 
C 1 168 THR 168 198 198 THR THR C . n 
C 1 169 SER 169 199 199 SER SER C . n 
C 1 170 ALA 170 200 200 ALA ALA C . n 
C 1 171 ILE 171 201 201 ILE ILE C . n 
C 1 172 THR 172 202 202 THR THR C . n 
C 1 173 GLN 173 203 203 GLN GLN C . n 
C 1 174 ALA 174 204 204 ALA ALA C . n 
C 1 175 CYS 175 205 205 CYS CYS C . n 
C 1 176 PRO 176 206 206 PRO PRO C . n 
C 1 177 LYS 177 207 207 LYS LYS C . n 
C 1 178 VAL 178 208 208 VAL VAL C . n 
C 1 179 SER 179 209 209 SER SER C . n 
C 1 180 PHE 180 210 210 PHE PHE C . n 
C 1 181 GLU 181 211 211 GLU GLU C . n 
C 1 182 PRO 182 212 212 PRO PRO C . n 
C 1 183 ILE 183 213 213 ILE ILE C . n 
C 1 184 PRO 184 214 214 PRO PRO C . n 
C 1 185 ILE 185 215 215 ILE ILE C . n 
C 1 186 HIS 186 216 216 HIS HIS C . n 
C 1 187 TYR 187 217 217 TYR TYR C . n 
C 1 188 CYS 188 218 218 CYS CYS C . n 
C 1 189 ALA 189 219 219 ALA ALA C . n 
C 1 190 PRO 190 220 220 PRO PRO C . n 
C 1 191 ALA 191 221 221 ALA ALA C . n 
C 1 192 GLY 192 222 222 GLY GLY C . n 
C 1 193 PHE 193 223 223 PHE PHE C . n 
C 1 194 ALA 194 224 224 ALA ALA C . n 
C 1 195 ILE 195 225 225 ILE ILE C . n 
C 1 196 LEU 196 226 226 LEU LEU C . n 
C 1 197 LYS 197 227 227 LYS LYS C . n 
C 1 198 CYS 198 228 228 CYS CYS C . n 
C 1 199 LYS 199 229 229 LYS LYS C . n 
C 1 200 ASP 200 230 230 ASP ASP C . n 
C 1 201 LYS 201 231 231 LYS LYS C . n 
C 1 202 LYS 202 232 232 LYS LYS C . n 
C 1 203 PHE 203 233 233 PHE PHE C . n 
C 1 204 ASN 204 234 234 ASN ASN C . n 
C 1 205 GLY 205 235 235 GLY GLY C . n 
C 1 206 THR 206 236 236 THR THR C . n 
C 1 207 GLY 207 237 237 GLY GLY C . n 
C 1 208 PRO 208 238 238 PRO PRO C . n 
C 1 209 CYS 209 239 239 CYS CYS C . n 
C 1 210 PRO 210 240 240 PRO PRO C . n 
C 1 211 SER 211 241 241 SER SER C . n 
C 1 212 VAL 212 242 242 VAL VAL C . n 
C 1 213 SER 213 243 243 SER SER C . n 
C 1 214 THR 214 244 244 THR THR C . n 
C 1 215 VAL 215 245 245 VAL VAL C . n 
C 1 216 GLN 216 246 246 GLN GLN C . n 
C 1 217 CYS 217 247 247 CYS CYS C . n 
C 1 218 THR 218 248 248 THR THR C . n 
C 1 219 HIS 219 249 249 HIS HIS C . n 
C 1 220 GLY 220 250 250 GLY GLY C . n 
C 1 221 ILE 221 251 251 ILE ILE C . n 
C 1 222 LYS 222 252 252 LYS LYS C . n 
C 1 223 PRO 223 253 253 PRO PRO C . n 
C 1 224 VAL 224 254 254 VAL VAL C . n 
C 1 225 VAL 225 255 255 VAL VAL C . n 
C 1 226 SER 226 256 256 SER SER C . n 
C 1 227 THR 227 257 257 THR THR C . n 
C 1 228 GLN 228 258 258 GLN GLN C . n 
C 1 229 LEU 229 259 259 LEU LEU C . n 
C 1 230 LEU 230 260 260 LEU LEU C . n 
C 1 231 LEU 231 261 261 LEU LEU C . n 
C 1 232 ASN 232 262 262 ASN ASN C . n 
C 1 233 GLY 233 263 263 GLY GLY C . n 
C 1 234 SER 234 264 264 SER SER C . n 
C 1 235 LEU 235 265 265 LEU LEU C . n 
C 1 236 ALA 236 266 266 ALA ALA C . n 
C 1 237 GLU 237 267 267 GLU GLU C . n 
C 1 238 GLU 238 268 268 GLU GLU C . n 
C 1 239 GLU 239 269 269 GLU GLU C . n 
C 1 240 VAL 240 270 270 VAL VAL C . n 
C 1 241 MET 241 271 271 MET MET C . n 
C 1 242 ILE 242 272 272 ILE ILE C . n 
C 1 243 ARG 243 273 273 ARG ARG C . n 
C 1 244 SER 244 274 274 SER SER C . n 
C 1 245 GLU 245 275 275 GLU GLU C . n 
C 1 246 ASN 246 276 276 ASN ASN C . n 
C 1 247 ILE 247 277 277 ILE ILE C . n 
C 1 248 THR 248 278 278 THR THR C . n 
C 1 249 ASN 249 279 279 ASN ASN C . n 
C 1 250 ASN 250 280 280 ASN ASN C . n 
C 1 251 ALA 251 281 281 ALA ALA C . n 
C 1 252 LYS 252 282 282 LYS LYS C . n 
C 1 253 ASN 253 283 283 ASN ASN C . n 
C 1 254 ILE 254 284 284 ILE ILE C . n 
C 1 255 LEU 255 285 285 LEU LEU C . n 
C 1 256 VAL 256 286 286 VAL VAL C . n 
C 1 257 GLN 257 287 287 GLN GLN C . n 
C 1 258 PHE 258 288 288 PHE PHE C . n 
C 1 259 ASN 259 289 289 ASN ASN C . n 
C 1 260 THR 260 290 290 THR THR C . n 
C 1 261 PRO 261 291 291 PRO PRO C . n 
C 1 262 VAL 262 292 292 VAL VAL C . n 
C 1 263 GLN 263 293 293 GLN GLN C . n 
C 1 264 ILE 264 294 294 ILE ILE C . n 
C 1 265 ASN 265 295 295 ASN ASN C . n 
C 1 266 CYS 266 296 296 CYS CYS C . n 
C 1 267 THR 267 297 297 THR THR C . n 
C 1 268 ARG 268 298 298 ARG ARG C . n 
C 1 269 PRO 269 299 299 PRO PRO C . n 
C 1 270 ASN 270 300 300 ASN ASN C . n 
C 1 271 ASN 271 301 301 ASN ASN C . n 
C 1 272 ASN 272 302 302 ASN ASN C . n 
C 1 273 THR 273 303 303 THR THR C . n 
C 1 274 ARG 274 304 304 ARG ARG C . n 
C 1 275 LYS 275 305 305 LYS LYS C . n 
C 1 276 SER 276 306 306 SER SER C . n 
C 1 277 ILE 277 307 307 ILE ILE C . n 
C 1 278 ARG 278 308 308 ARG ARG C . n 
C 1 279 ILE 279 309 309 ILE ILE C . n 
C 1 280 GLY 280 312 312 GLY GLY C . n 
C 1 281 PRO 281 313 313 PRO PRO C . n 
C 1 282 GLY 282 314 314 GLY GLY C . n 
C 1 283 GLN 283 315 315 GLN GLN C . n 
C 1 284 ALA 284 316 316 ALA ALA C . n 
C 1 285 PHE 285 317 317 PHE PHE C . n 
C 1 286 TYR 286 318 318 TYR TYR C . n 
C 1 287 ALA 287 319 319 ALA ALA C . n 
C 1 288 THR 288 320 320 THR THR C . n 
C 1 289 GLY 289 321 321 GLY GLY C . n 
C 1 290 ASP 290 321 321 ASP ASP C A n 
C 1 291 ILE 291 322 322 ILE ILE C . n 
C 1 292 ILE 292 323 323 ILE ILE C . n 
C 1 293 GLY 293 324 324 GLY GLY C . n 
C 1 294 ASP 294 325 325 ASP ASP C . n 
C 1 295 ILE 295 326 326 ILE ILE C . n 
C 1 296 ARG 296 327 327 ARG ARG C . n 
C 1 297 GLN 297 328 328 GLN GLN C . n 
C 1 298 ALA 298 329 329 ALA ALA C . n 
C 1 299 HIS 299 330 330 HIS HIS C . n 
C 1 300 CYS 300 331 331 CYS CYS C . n 
C 1 301 ASN 301 332 332 ASN ASN C . n 
C 1 302 VAL 302 333 333 VAL VAL C . n 
C 1 303 SER 303 334 334 SER SER C . n 
C 1 304 LYS 304 335 335 LYS LYS C . n 
C 1 305 ALA 305 336 336 ALA ALA C . n 
C 1 306 THR 306 337 337 THR THR C . n 
C 1 307 TRP 307 338 338 TRP TRP C . n 
C 1 308 ASN 308 339 339 ASN ASN C . n 
C 1 309 GLU 309 340 340 GLU GLU C . n 
C 1 310 THR 310 341 341 THR THR C . n 
C 1 311 LEU 311 342 342 LEU LEU C . n 
C 1 312 GLY 312 343 343 GLY GLY C . n 
C 1 313 LYS 313 344 344 LYS LYS C . n 
C 1 314 VAL 314 345 345 VAL VAL C . n 
C 1 315 VAL 315 346 346 VAL VAL C . n 
C 1 316 LYS 316 347 347 LYS LYS C . n 
C 1 317 GLN 317 348 348 GLN GLN C . n 
C 1 318 LEU 318 349 349 LEU LEU C . n 
C 1 319 ARG 319 350 350 ARG ARG C . n 
C 1 320 LYS 320 351 351 LYS LYS C . n 
C 1 321 HIS 321 352 352 HIS HIS C . n 
C 1 322 PHE 322 353 353 PHE PHE C . n 
C 1 323 GLY 323 354 354 GLY GLY C . n 
C 1 324 ASN 324 355 355 ASN ASN C . n 
C 1 325 ASN 325 356 356 ASN ASN C . n 
C 1 326 THR 326 357 357 THR THR C . n 
C 1 327 ILE 327 358 358 ILE ILE C . n 
C 1 328 ILE 328 359 359 ILE ILE C . n 
C 1 329 ARG 329 360 360 ARG ARG C . n 
C 1 330 PHE 330 361 361 PHE PHE C . n 
C 1 331 ALA 331 362 362 ALA ALA C . n 
C 1 332 ASN 332 363 363 ASN ASN C . n 
C 1 333 SER 333 364 364 SER SER C . n 
C 1 334 SER 334 365 365 SER SER C . n 
C 1 335 GLY 335 366 366 GLY GLY C . n 
C 1 336 GLY 336 367 367 GLY GLY C . n 
C 1 337 ASP 337 368 368 ASP ASP C . n 
C 1 338 LEU 338 369 369 LEU LEU C . n 
C 1 339 GLU 339 370 370 GLU GLU C . n 
C 1 340 VAL 340 371 371 VAL VAL C . n 
C 1 341 THR 341 372 372 THR THR C . n 
C 1 342 THR 342 373 373 THR THR C . n 
C 1 343 HIS 343 374 374 HIS HIS C . n 
C 1 344 SER 344 375 375 SER SER C . n 
C 1 345 PHE 345 376 376 PHE PHE C . n 
C 1 346 ASN 346 377 377 ASN ASN C . n 
C 1 347 CYS 347 378 378 CYS CYS C . n 
C 1 348 GLY 348 379 379 GLY GLY C . n 
C 1 349 GLY 349 380 380 GLY GLY C . n 
C 1 350 GLU 350 381 381 GLU GLU C . n 
C 1 351 PHE 351 382 382 PHE PHE C . n 
C 1 352 PHE 352 383 383 PHE PHE C . n 
C 1 353 TYR 353 384 384 TYR TYR C . n 
C 1 354 CYS 354 385 385 CYS CYS C . n 
C 1 355 ASN 355 386 386 ASN ASN C . n 
C 1 356 THR 356 387 387 THR THR C . n 
C 1 357 SER 357 388 388 SER SER C . n 
C 1 358 GLY 358 389 389 GLY GLY C . n 
C 1 359 LEU 359 390 390 LEU LEU C . n 
C 1 360 PHE 360 391 391 PHE PHE C . n 
C 1 361 ASN 361 392 392 ASN ASN C . n 
C 1 362 SER 362 393 393 SER SER C . n 
C 1 363 THR 363 394 394 THR THR C . n 
C 1 364 TRP 364 395 395 TRP TRP C . n 
C 1 365 ILE 365 396 396 ILE ILE C . n 
C 1 366 SER 366 397 397 SER SER C . n 
C 1 367 ASN 367 398 398 ASN ASN C . n 
C 1 368 THR 368 400 ?   ?   ?   C . n 
C 1 369 SER 369 401 ?   ?   ?   C . n 
C 1 370 VAL 370 402 ?   ?   ?   C . n 
C 1 371 GLN 371 403 ?   ?   ?   C . n 
C 1 372 GLY 372 404 ?   ?   ?   C . n 
C 1 373 SER 373 405 ?   ?   ?   C . n 
C 1 374 ASN 374 406 ?   ?   ?   C . n 
C 1 375 SER 375 407 ?   ?   ?   C . n 
C 1 376 THR 376 408 ?   ?   ?   C . n 
C 1 377 GLY 377 409 ?   ?   ?   C . n 
C 1 378 SER 378 410 ?   ?   ?   C . n 
C 1 379 ASN 379 411 411 ASN ASN C . n 
C 1 380 ASP 380 412 412 ASP ASP C . n 
C 1 381 SER 381 413 413 SER SER C . n 
C 1 382 ILE 382 414 414 ILE ILE C . n 
C 1 383 THR 383 415 415 THR THR C . n 
C 1 384 LEU 384 416 416 LEU LEU C . n 
C 1 385 PRO 385 417 417 PRO PRO C . n 
C 1 386 CYS 386 418 418 CYS CYS C . n 
C 1 387 ARG 387 419 419 ARG ARG C . n 
C 1 388 ILE 388 420 420 ILE ILE C . n 
C 1 389 LYS 389 421 421 LYS LYS C . n 
C 1 390 GLN 390 422 422 GLN GLN C . n 
C 1 391 ILE 391 423 423 ILE ILE C . n 
C 1 392 ILE 392 424 424 ILE ILE C . n 
C 1 393 ASN 393 425 425 ASN ASN C . n 
C 1 394 MET 394 426 426 MET MET C . n 
C 1 395 TRP 395 427 427 TRP TRP C . n 
C 1 396 GLN 396 428 428 GLN GLN C . n 
C 1 397 ARG 397 429 429 ARG ARG C . n 
C 1 398 ILE 398 430 430 ILE ILE C . n 
C 1 399 GLY 399 431 431 GLY GLY C . n 
C 1 400 GLN 400 432 432 GLN GLN C . n 
C 1 401 ALA 401 433 433 ALA ALA C . n 
C 1 402 MET 402 434 434 MET MET C . n 
C 1 403 TYR 403 435 435 TYR TYR C . n 
C 1 404 ALA 404 436 436 ALA ALA C . n 
C 1 405 PRO 405 437 437 PRO PRO C . n 
C 1 406 PRO 406 438 438 PRO PRO C . n 
C 1 407 ILE 407 439 439 ILE ILE C . n 
C 1 408 GLN 408 440 440 GLN GLN C . n 
C 1 409 GLY 409 441 441 GLY GLY C . n 
C 1 410 VAL 410 442 442 VAL VAL C . n 
C 1 411 ILE 411 443 443 ILE ILE C . n 
C 1 412 ARG 412 444 444 ARG ARG C . n 
C 1 413 CYS 413 445 445 CYS CYS C . n 
C 1 414 VAL 414 446 446 VAL VAL C . n 
C 1 415 SER 415 447 447 SER SER C . n 
C 1 416 ASN 416 448 448 ASN ASN C . n 
C 1 417 ILE 417 449 449 ILE ILE C . n 
C 1 418 THR 418 450 450 THR THR C . n 
C 1 419 GLY 419 451 451 GLY GLY C . n 
C 1 420 LEU 420 452 452 LEU LEU C . n 
C 1 421 ILE 421 453 453 ILE ILE C . n 
C 1 422 LEU 422 454 454 LEU LEU C . n 
C 1 423 THR 423 455 455 THR THR C . n 
C 1 424 ARG 424 456 456 ARG ARG C . n 
C 1 425 ASP 425 457 457 ASP ASP C . n 
C 1 426 GLY 426 458 458 GLY GLY C . n 
C 1 427 GLY 427 459 459 GLY GLY C . n 
C 1 428 SER 428 460 460 SER SER C . n 
C 1 429 THR 429 461 461 THR THR C . n 
C 1 430 ASN 430 462 462 ASN ASN C . n 
C 1 431 SER 431 463 463 SER SER C . n 
C 1 432 THR 432 464 464 THR THR C . n 
C 1 433 THR 433 465 465 THR THR C . n 
C 1 434 GLU 434 466 466 GLU GLU C . n 
C 1 435 THR 435 467 467 THR THR C . n 
C 1 436 PHE 436 468 468 PHE PHE C . n 
C 1 437 ARG 437 469 469 ARG ARG C . n 
C 1 438 PRO 438 470 470 PRO PRO C . n 
C 1 439 GLY 439 471 471 GLY GLY C . n 
C 1 440 GLY 440 472 472 GLY GLY C . n 
C 1 441 GLY 441 473 473 GLY GLY C . n 
C 1 442 ASP 442 474 474 ASP ASP C . n 
C 1 443 MET 443 475 475 MET MET C . n 
C 1 444 ARG 444 476 476 ARG ARG C . n 
C 1 445 ASP 445 477 477 ASP ASP C . n 
C 1 446 ASN 446 478 478 ASN ASN C . n 
C 1 447 TRP 447 479 479 TRP TRP C . n 
C 1 448 ARG 448 480 480 ARG ARG C . n 
C 1 449 SER 449 481 481 SER SER C . n 
C 1 450 GLU 450 482 482 GLU GLU C . n 
C 1 451 LEU 451 483 483 LEU LEU C . n 
C 1 452 TYR 452 484 484 TYR TYR C . n 
C 1 453 LYS 453 485 485 LYS LYS C . n 
C 1 454 TYR 454 486 486 TYR TYR C . n 
C 1 455 LYS 455 487 487 LYS LYS C . n 
C 1 456 VAL 456 488 488 VAL VAL C . n 
C 1 457 VAL 457 489 489 VAL VAL C . n 
C 1 458 LYS 458 490 490 LYS LYS C . n 
C 1 459 ILE 459 491 491 ILE ILE C . n 
C 1 460 GLU 460 492 492 GLU GLU C . n 
C 1 461 PRO 461 493 493 PRO PRO C . n 
C 1 462 LEU 462 494 494 LEU LEU C . n 
C 1 463 GLY 463 495 495 GLY GLY C . n 
C 1 464 VAL 464 496 496 VAL VAL C . n 
C 1 465 ALA 465 497 497 ALA ALA C . n 
C 1 466 PRO 466 498 498 PRO PRO C . n 
C 1 467 THR 467 499 499 THR THR C . n 
C 1 468 ARG 468 500 500 ARG ARG C . n 
C 1 469 CYS 469 501 501 CYS CYS C . n 
C 1 470 LYS 470 502 502 LYS LYS C . n 
C 1 471 ARG 471 503 503 ARG ARG C . n 
C 1 472 ARG 472 504 504 ARG ARG C . n 
C 1 473 VAL 473 505 505 VAL VAL C . n 
C 1 474 VAL 474 506 ?   ?   ?   C . n 
C 1 475 GLY 475 507 ?   ?   ?   C . n 
C 1 476 ARG 476 508 ?   ?   ?   C . n 
C 1 477 ARG 477 509 ?   ?   ?   C . n 
C 1 478 ARG 478 510 ?   ?   ?   C . n 
C 1 479 ARG 479 511 ?   ?   ?   C . n 
C 1 480 ARG 480 512 ?   ?   ?   C . n 
C 1 481 ARG 481 513 ?   ?   ?   C . n 
D 3 1   ALA 1   6   6   ALA ALA L . n 
D 3 2   PRO 2   7   7   PRO PRO L . n 
D 3 3   THR 3   8   8   THR THR L . n 
D 3 4   PHE 4   9   9   PHE PHE L . n 
D 3 5   VAL 5   11  11  VAL VAL L . n 
D 3 6   SER 6   12  12  SER SER L . n 
D 3 7   VAL 7   13  13  VAL VAL L . n 
D 3 8   ALA 8   14  14  ALA ALA L . n 
D 3 9   PRO 9   15  15  PRO PRO L . n 
D 3 10  GLY 10  16  16  GLY GLY L . n 
D 3 11  GLN 11  17  17  GLN GLN L . n 
D 3 12  THR 12  18  18  THR THR L . n 
D 3 13  ALA 13  19  19  ALA ALA L . n 
D 3 14  ARG 14  20  20  ARG ARG L . n 
D 3 15  ILE 15  21  21  ILE ILE L . n 
D 3 16  THR 16  22  22  THR THR L . n 
D 3 17  CYS 17  23  23  CYS CYS L . n 
D 3 18  GLY 18  24  24  GLY GLY L . n 
D 3 19  GLU 19  25  25  GLU GLU L . n 
D 3 20  GLU 20  26  26  GLU GLU L . n 
D 3 21  SER 21  27  27  SER SER L . n 
D 3 22  LEU 22  28  28  LEU LEU L . n 
D 3 23  GLY 23  29  29  GLY GLY L . n 
D 3 24  SER 24  30  30  SER SER L . n 
D 3 25  ARG 25  31  31  ARG ARG L . n 
D 3 26  SER 26  32  32  SER SER L . n 
D 3 27  VAL 27  33  33  VAL VAL L . n 
D 3 28  ILE 28  34  34  ILE ILE L . n 
D 3 29  TRP 29  35  35  TRP TRP L . n 
D 3 30  TYR 30  36  36  TYR TYR L . n 
D 3 31  GLN 31  37  37  GLN GLN L . n 
D 3 32  GLN 32  38  38  GLN GLN L . n 
D 3 33  ARG 33  39  39  ARG ARG L . n 
D 3 34  PRO 34  40  40  PRO PRO L . n 
D 3 35  GLY 35  41  41  GLY GLY L . n 
D 3 36  GLN 36  42  42  GLN GLN L . n 
D 3 37  ALA 37  43  43  ALA ALA L . n 
D 3 38  PRO 38  44  44  PRO PRO L . n 
D 3 39  SER 39  45  45  SER SER L . n 
D 3 40  LEU 40  46  46  LEU LEU L . n 
D 3 41  ILE 41  47  47  ILE ILE L . n 
D 3 42  ILE 42  48  48  ILE ILE L . n 
D 3 43  TYR 43  49  49  TYR TYR L . n 
D 3 44  ASN 44  50  50  ASN ASN L . n 
D 3 45  ASN 45  51  51  ASN ASN L . n 
D 3 46  ASN 46  52  52  ASN ASN L . n 
D 3 47  ASP 47  53  53  ASP ASP L . n 
D 3 48  ARG 48  54  54  ARG ARG L . n 
D 3 49  PRO 49  55  55  PRO PRO L . n 
D 3 50  SER 50  56  56  SER SER L . n 
D 3 51  GLY 51  57  57  GLY GLY L . n 
D 3 52  ILE 52  58  58  ILE ILE L . n 
D 3 53  PRO 53  59  59  PRO PRO L . n 
D 3 54  ASP 54  60  60  ASP ASP L . n 
D 3 55  ARG 55  61  61  ARG ARG L . n 
D 3 56  PHE 56  62  62  PHE PHE L . n 
D 3 57  SER 57  63  63  SER SER L . n 
D 3 58  GLY 58  64  64  GLY GLY L . n 
D 3 59  SER 59  65  65  SER SER L . n 
D 3 60  PRO 60  66  66  PRO PRO L . n 
D 3 61  GLY 61  67  67  GLY GLY L . n 
D 3 62  SER 62  67  67  SER SER L A n 
D 3 63  THR 63  67  67  THR THR L B n 
D 3 64  PHE 64  67  67  PHE PHE L C n 
D 3 65  GLY 65  68  68  GLY GLY L . n 
D 3 66  THR 66  69  69  THR THR L . n 
D 3 67  THR 67  70  70  THR THR L . n 
D 3 68  ALA 68  71  71  ALA ALA L . n 
D 3 69  THR 69  72  72  THR THR L . n 
D 3 70  LEU 70  73  73  LEU LEU L . n 
D 3 71  THR 71  74  74  THR THR L . n 
D 3 72  ILE 72  75  75  ILE ILE L . n 
D 3 73  THR 73  76  76  THR THR L . n 
D 3 74  SER 74  77  77  SER SER L . n 
D 3 75  VAL 75  78  78  VAL VAL L . n 
D 3 76  GLU 76  79  79  GLU GLU L . n 
D 3 77  ALA 77  80  80  ALA ALA L . n 
D 3 78  GLY 78  81  81  GLY GLY L . n 
D 3 79  ASP 79  82  82  ASP ASP L . n 
D 3 80  GLU 80  83  83  GLU GLU L . n 
D 3 81  ALA 81  84  84  ALA ALA L . n 
D 3 82  ASP 82  85  85  ASP ASP L . n 
D 3 83  TYR 83  86  86  TYR TYR L . n 
D 3 84  TYR 84  87  87  TYR TYR L . n 
D 3 85  CYS 85  88  88  CYS CYS L . n 
D 3 86  HIS 86  89  89  HIS HIS L . n 
D 3 87  ILE 87  90  90  ILE ILE L . n 
D 3 88  TRP 88  91  91  TRP TRP L . n 
D 3 89  ASP 89  92  92  ASP ASP L . n 
D 3 90  SER 90  93  93  SER SER L . n 
D 3 91  ARG 91  94  94  ARG ARG L . n 
D 3 92  ARG 92  95  95  ARG ARG L . n 
D 3 93  PRO 93  95  95  PRO PRO L A n 
D 3 94  THR 94  95  95  THR THR L B n 
D 3 95  ASN 95  95  95  ASN ASN L C n 
D 3 96  TRP 96  96  96  TRP TRP L . n 
D 3 97  VAL 97  97  97  VAL VAL L . n 
D 3 98  PHE 98  98  98  PHE PHE L . n 
D 3 99  GLY 99  99  99  GLY GLY L . n 
D 3 100 GLU 100 100 100 GLU GLU L . n 
D 3 101 GLY 101 101 101 GLY GLY L . n 
D 3 102 THR 102 102 102 THR THR L . n 
D 3 103 THR 103 103 103 THR THR L . n 
D 3 104 LEU 104 104 104 LEU LEU L . n 
D 3 105 ILE 105 105 105 ILE ILE L . n 
D 3 106 VAL 106 106 106 VAL VAL L . n 
D 3 107 LEU 107 107 107 LEU LEU L . n 
D 3 108 SER 108 108 108 SER SER L . n 
D 3 109 GLN 109 109 109 GLN GLN L . n 
D 3 110 PRO 110 110 110 PRO PRO L . n 
D 3 111 LYS 111 111 111 LYS LYS L . n 
D 3 112 ALA 112 112 112 ALA ALA L . n 
D 3 113 ALA 113 113 113 ALA ALA L . n 
D 3 114 PRO 114 114 114 PRO PRO L . n 
D 3 115 SER 115 115 115 SER SER L . n 
D 3 116 VAL 116 116 116 VAL VAL L . n 
D 3 117 THR 117 117 117 THR THR L . n 
D 3 118 LEU 118 118 118 LEU LEU L . n 
D 3 119 PHE 119 119 119 PHE PHE L . n 
D 3 120 PRO 120 120 120 PRO PRO L . n 
D 3 121 PRO 121 121 121 PRO PRO L . n 
D 3 122 SER 122 122 122 SER SER L . n 
D 3 123 SER 123 123 123 SER SER L . n 
D 3 124 GLU 124 124 124 GLU GLU L . n 
D 3 125 GLU 125 125 125 GLU GLU L . n 
D 3 126 LEU 126 126 126 LEU LEU L . n 
D 3 127 GLN 127 127 127 GLN GLN L . n 
D 3 128 ALA 128 128 128 ALA ALA L . n 
D 3 129 ASN 129 129 129 ASN ASN L . n 
D 3 130 LYS 130 130 130 LYS LYS L . n 
D 3 131 ALA 131 131 131 ALA ALA L . n 
D 3 132 THR 132 132 132 THR THR L . n 
D 3 133 LEU 133 133 133 LEU LEU L . n 
D 3 134 VAL 134 134 134 VAL VAL L . n 
D 3 135 CYS 135 135 135 CYS CYS L . n 
D 3 136 LEU 136 136 136 LEU LEU L . n 
D 3 137 ILE 137 137 137 ILE ILE L . n 
D 3 138 SER 138 138 138 SER SER L . n 
D 3 139 ASP 139 139 139 ASP ASP L . n 
D 3 140 PHE 140 140 140 PHE PHE L . n 
D 3 141 TYR 141 141 141 TYR TYR L . n 
D 3 142 PRO 142 142 142 PRO PRO L . n 
D 3 143 GLY 143 143 143 GLY GLY L . n 
D 3 144 ALA 144 144 144 ALA ALA L . n 
D 3 145 VAL 145 145 145 VAL VAL L . n 
D 3 146 THR 146 146 146 THR THR L . n 
D 3 147 VAL 147 147 147 VAL VAL L . n 
D 3 148 ALA 148 148 148 ALA ALA L . n 
D 3 149 TRP 149 149 149 TRP TRP L . n 
D 3 150 LYS 150 150 150 LYS LYS L . n 
D 3 151 ALA 151 151 151 ALA ALA L . n 
D 3 152 ASP 152 152 152 ASP ASP L . n 
D 3 153 SER 153 153 153 SER SER L . n 
D 3 154 SER 154 154 154 SER SER L . n 
D 3 155 PRO 155 155 155 PRO PRO L . n 
D 3 156 VAL 156 156 156 VAL VAL L . n 
D 3 157 LYS 157 157 157 LYS LYS L . n 
D 3 158 ALA 158 158 158 ALA ALA L . n 
D 3 159 GLY 159 159 159 GLY GLY L . n 
D 3 160 VAL 160 160 160 VAL VAL L . n 
D 3 161 GLU 161 161 161 GLU GLU L . n 
D 3 162 THR 162 162 162 THR THR L . n 
D 3 163 THR 163 163 163 THR THR L . n 
D 3 164 THR 164 164 164 THR THR L . n 
D 3 165 PRO 165 165 165 PRO PRO L . n 
D 3 166 SER 166 166 166 SER SER L . n 
D 3 167 LYS 167 167 167 LYS LYS L . n 
D 3 168 GLN 168 168 168 GLN GLN L . n 
D 3 169 SER 169 169 169 SER SER L . n 
D 3 170 ASN 170 170 170 ASN ASN L . n 
D 3 171 ASN 171 171 171 ASN ASN L . n 
D 3 172 LYS 172 172 172 LYS LYS L . n 
D 3 173 TYR 173 173 173 TYR TYR L . n 
D 3 174 ALA 174 174 174 ALA ALA L . n 
D 3 175 ALA 175 175 175 ALA ALA L . n 
D 3 176 SER 176 176 176 SER SER L . n 
D 3 177 SER 177 177 177 SER SER L . n 
D 3 178 TYR 178 178 178 TYR TYR L . n 
D 3 179 LEU 179 179 179 LEU LEU L . n 
D 3 180 SER 180 180 180 SER SER L . n 
D 3 181 LEU 181 181 181 LEU LEU L . n 
D 3 182 THR 182 182 182 THR THR L . n 
D 3 183 PRO 183 183 183 PRO PRO L . n 
D 3 184 GLU 184 184 184 GLU GLU L . n 
D 3 185 GLN 185 185 185 GLN GLN L . n 
D 3 186 TRP 186 186 186 TRP TRP L . n 
D 3 187 LYS 187 187 187 LYS LYS L . n 
D 3 188 SER 188 188 188 SER SER L . n 
D 3 189 HIS 189 189 189 HIS HIS L . n 
D 3 190 LYS 190 190 190 LYS LYS L . n 
D 3 191 SER 191 191 191 SER SER L . n 
D 3 192 TYR 192 192 192 TYR TYR L . n 
D 3 193 SER 193 193 193 SER SER L . n 
D 3 194 CYS 194 194 194 CYS CYS L . n 
D 3 195 GLN 195 195 195 GLN GLN L . n 
D 3 196 VAL 196 196 196 VAL VAL L . n 
D 3 197 THR 197 197 197 THR THR L . n 
D 3 198 HIS 198 198 198 HIS HIS L . n 
D 3 199 GLU 199 199 199 GLU GLU L . n 
D 3 200 GLY 200 200 200 GLY GLY L . n 
D 3 201 SER 201 201 201 SER SER L . n 
D 3 202 THR 202 202 202 THR THR L . n 
D 3 203 VAL 203 203 203 VAL VAL L . n 
D 3 204 GLU 204 204 204 GLU GLU L . n 
D 3 205 LYS 205 205 205 LYS LYS L . n 
D 3 206 THR 206 206 206 THR THR L . n 
D 3 207 VAL 207 207 207 VAL VAL L . n 
D 3 208 ALA 208 208 208 ALA ALA L . n 
D 3 209 PRO 209 209 209 PRO PRO L . n 
D 3 210 THR 210 210 210 THR THR L . n 
E 4 1   GLN 1   1   1   GLN GLN E . n 
E 4 2   GLU 2   2   2   GLU GLU E . n 
E 4 3   VAL 3   3   3   VAL VAL E . n 
E 4 4   LEU 4   4   4   LEU LEU E . n 
E 4 5   VAL 5   5   5   VAL VAL E . n 
E 4 6   GLN 6   6   6   GLN GLN E . n 
E 4 7   SER 7   7   7   SER SER E . n 
E 4 8   GLY 8   8   8   GLY GLY E . n 
E 4 9   ALA 9   9   9   ALA ALA E . n 
E 4 10  GLU 10  10  10  GLU GLU E . n 
E 4 11  VAL 11  11  11  VAL VAL E . n 
E 4 12  LYS 12  12  12  LYS LYS E . n 
E 4 13  LYS 13  13  13  LYS LYS E . n 
E 4 14  PRO 14  14  14  PRO PRO E . n 
E 4 15  GLY 15  15  15  GLY GLY E . n 
E 4 16  ALA 16  16  16  ALA ALA E . n 
E 4 17  SER 17  17  17  SER SER E . n 
E 4 18  VAL 18  18  18  VAL VAL E . n 
E 4 19  LYS 19  19  19  LYS LYS E . n 
E 4 20  VAL 20  20  20  VAL VAL E . n 
E 4 21  SER 21  21  21  SER SER E . n 
E 4 22  CYS 22  22  22  CYS CYS E . n 
E 4 23  ARG 23  23  23  ARG ARG E . n 
E 4 24  ALA 24  24  24  ALA ALA E . n 
E 4 25  PHE 25  25  25  PHE PHE E . n 
E 4 26  GLY 26  26  26  GLY GLY E . n 
E 4 27  TYR 27  27  27  TYR TYR E . n 
E 4 28  THR 28  28  28  THR THR E . n 
E 4 29  PHE 29  29  29  PHE PHE E . n 
E 4 30  THR 30  30  30  THR THR E . n 
E 4 31  GLY 31  31  31  GLY GLY E . n 
E 4 32  ASN 32  32  32  ASN ASN E . n 
E 4 33  ALA 33  33  33  ALA ALA E . n 
E 4 34  LEU 34  34  34  LEU LEU E . n 
E 4 35  HIS 35  35  35  HIS HIS E . n 
E 4 36  TRP 36  36  36  TRP TRP E . n 
E 4 37  VAL 37  37  37  VAL VAL E . n 
E 4 38  ARG 38  38  38  ARG ARG E . n 
E 4 39  GLN 39  39  39  GLN GLN E . n 
E 4 40  ALA 40  40  40  ALA ALA E . n 
E 4 41  PRO 41  41  41  PRO PRO E . n 
E 4 42  GLY 42  42  42  GLY GLY E . n 
E 4 43  GLN 43  43  43  GLN GLN E . n 
E 4 44  GLY 44  44  44  GLY GLY E . n 
E 4 45  LEU 45  45  45  LEU LEU E . n 
E 4 46  GLU 46  46  46  GLU GLU E . n 
E 4 47  TRP 47  47  47  TRP TRP E . n 
E 4 48  LEU 48  48  48  LEU LEU E . n 
E 4 49  GLY 49  49  49  GLY GLY E . n 
E 4 50  TRP 50  50  50  TRP TRP E . n 
E 4 51  ILE 51  51  51  ILE ILE E . n 
E 4 52  ASN 52  52  52  ASN ASN E . n 
E 4 53  PRO 53  52  52  PRO PRO E A n 
E 4 54  HIS 54  53  53  HIS HIS E . n 
E 4 55  SER 55  54  54  SER SER E . n 
E 4 56  GLY 56  55  55  GLY GLY E . n 
E 4 57  ASP 57  56  56  ASP ASP E . n 
E 4 58  THR 58  57  57  THR THR E . n 
E 4 59  THR 59  58  58  THR THR E . n 
E 4 60  THR 60  59  59  THR THR E . n 
E 4 61  SER 61  60  60  SER SER E . n 
E 4 62  GLN 62  61  61  GLN GLN E . n 
E 4 63  LYS 63  62  62  LYS LYS E . n 
E 4 64  PHE 64  63  63  PHE PHE E . n 
E 4 65  GLN 65  64  64  GLN GLN E . n 
E 4 66  GLY 66  65  65  GLY GLY E . n 
E 4 67  ARG 67  66  66  ARG ARG E . n 
E 4 68  VAL 68  67  67  VAL VAL E . n 
E 4 69  TYR 69  68  68  TYR TYR E . n 
E 4 70  MET 70  69  69  MET MET E . n 
E 4 71  THR 71  70  70  THR THR E . n 
E 4 72  ARG 72  71  71  ARG ARG E . n 
E 4 73  ASP 73  72  72  ASP ASP E . n 
E 4 74  LYS 74  73  73  LYS LYS E . n 
E 4 75  SER 75  74  74  SER SER E . n 
E 4 76  ILE 76  75  75  ILE ILE E . n 
E 4 77  ASN 77  76  76  ASN ASN E . n 
E 4 78  THR 78  77  77  THR THR E . n 
E 4 79  ALA 79  78  78  ALA ALA E . n 
E 4 80  PHE 80  79  79  PHE PHE E . n 
E 4 81  LEU 81  80  80  LEU LEU E . n 
E 4 82  ASP 82  81  81  ASP ASP E . n 
E 4 83  VAL 83  82  82  VAL VAL E . n 
E 4 84  THR 84  82  82  THR THR E A n 
E 4 85  ARG 85  82  82  ARG ARG E B n 
E 4 86  LEU 86  82  82  LEU LEU E C n 
E 4 87  THR 87  83  83  THR THR E . n 
E 4 88  SER 88  84  84  SER SER E . n 
E 4 89  ASP 89  85  85  ASP ASP E . n 
E 4 90  ASP 90  86  86  ASP ASP E . n 
E 4 91  THR 91  87  87  THR THR E . n 
E 4 92  GLY 92  88  88  GLY GLY E . n 
E 4 93  ILE 93  89  89  ILE ILE E . n 
E 4 94  TYR 94  90  90  TYR TYR E . n 
E 4 95  TYR 95  91  91  TYR TYR E . n 
E 4 96  CYS 96  92  92  CYS CYS E . n 
E 4 97  ALA 97  93  93  ALA ALA E . n 
E 4 98  ARG 98  94  94  ARG ARG E . n 
E 4 99  ASP 99  95  95  ASP ASP E . n 
E 4 100 LYS 100 96  96  LYS LYS E . n 
E 4 101 TYR 101 97  97  TYR TYR E . n 
E 4 102 TYR 102 98  98  TYR TYR E . n 
E 4 103 GLY 103 99  99  GLY GLY E . n 
E 4 104 ASN 104 100 100 ASN ASN E . n 
E 4 105 GLU 105 100 100 GLU GLU E A n 
E 4 106 ALA 106 100 100 ALA ALA E B n 
E 4 107 VAL 107 100 100 VAL VAL E C n 
E 4 108 GLY 108 100 100 GLY GLY E D n 
E 4 109 MET 109 100 100 MET MET E E n 
E 4 110 ASP 110 101 101 ASP ASP E . n 
E 4 111 VAL 111 102 102 VAL VAL E . n 
E 4 112 TRP 112 103 103 TRP TRP E . n 
E 4 113 GLY 113 104 104 GLY GLY E . n 
E 4 114 GLN 114 105 105 GLN GLN E . n 
E 4 115 GLY 115 106 106 GLY GLY E . n 
E 4 116 THR 116 107 107 THR THR E . n 
E 4 117 SER 117 108 108 SER SER E . n 
E 4 118 VAL 118 109 109 VAL VAL E . n 
E 4 119 THR 119 110 110 THR THR E . n 
E 4 120 VAL 120 111 111 VAL VAL E . n 
E 4 121 SER 121 112 112 SER SER E . n 
E 4 122 SER 122 113 113 SER SER E . n 
E 4 123 ALA 123 114 114 ALA ALA E . n 
E 4 124 SER 124 115 115 SER SER E . n 
E 4 125 THR 125 116 116 THR THR E . n 
E 4 126 LYS 126 117 117 LYS LYS E . n 
E 4 127 GLY 127 118 118 GLY GLY E . n 
E 4 128 PRO 128 119 119 PRO PRO E . n 
E 4 129 SER 129 120 120 SER SER E . n 
E 4 130 VAL 130 121 121 VAL VAL E . n 
E 4 131 PHE 131 122 122 PHE PHE E . n 
E 4 132 PRO 132 123 123 PRO PRO E . n 
E 4 133 LEU 133 124 124 LEU LEU E . n 
E 4 134 ALA 134 125 125 ALA ALA E . n 
E 4 135 PRO 135 126 126 PRO PRO E . n 
E 4 136 SER 136 127 127 SER SER E . n 
E 4 137 SER 137 128 128 SER SER E . n 
E 4 138 LYS 138 129 129 LYS LYS E . n 
E 4 139 SER 139 130 130 SER SER E . n 
E 4 140 THR 140 131 131 THR THR E . n 
E 4 141 SER 141 132 132 SER SER E . n 
E 4 142 GLY 142 133 133 GLY GLY E . n 
E 4 143 GLY 143 134 134 GLY GLY E . n 
E 4 144 THR 144 135 135 THR THR E . n 
E 4 145 ALA 145 136 136 ALA ALA E . n 
E 4 146 ALA 146 137 137 ALA ALA E . n 
E 4 147 LEU 147 138 138 LEU LEU E . n 
E 4 148 GLY 148 139 139 GLY GLY E . n 
E 4 149 CYS 149 140 140 CYS CYS E . n 
E 4 150 LEU 150 141 141 LEU LEU E . n 
E 4 151 VAL 151 142 142 VAL VAL E . n 
E 4 152 LYS 152 143 143 LYS LYS E . n 
E 4 153 ASP 153 144 144 ASP ASP E . n 
E 4 154 TYR 154 145 145 TYR TYR E . n 
E 4 155 PHE 155 146 146 PHE PHE E . n 
E 4 156 PRO 156 147 147 PRO PRO E . n 
E 4 157 GLU 157 148 148 GLU GLU E . n 
E 4 158 PRO 158 149 149 PRO PRO E . n 
E 4 159 VAL 159 150 150 VAL VAL E . n 
E 4 160 THR 160 151 151 THR THR E . n 
E 4 161 VAL 161 152 152 VAL VAL E . n 
E 4 162 SER 162 153 153 SER SER E . n 
E 4 163 TRP 163 154 154 TRP TRP E . n 
E 4 164 ASN 164 155 155 ASN ASN E . n 
E 4 165 SER 165 156 156 SER SER E . n 
E 4 166 GLY 166 157 157 GLY GLY E . n 
E 4 167 ALA 167 158 158 ALA ALA E . n 
E 4 168 LEU 168 159 159 LEU LEU E . n 
E 4 169 THR 169 160 160 THR THR E . n 
E 4 170 SER 170 161 161 SER SER E . n 
E 4 171 GLY 171 162 162 GLY GLY E . n 
E 4 172 VAL 172 163 163 VAL VAL E . n 
E 4 173 HIS 173 164 164 HIS HIS E . n 
E 4 174 THR 174 165 165 THR THR E . n 
E 4 175 PHE 175 166 166 PHE PHE E . n 
E 4 176 PRO 176 167 167 PRO PRO E . n 
E 4 177 ALA 177 168 168 ALA ALA E . n 
E 4 178 VAL 178 169 169 VAL VAL E . n 
E 4 179 LEU 179 170 170 LEU LEU E . n 
E 4 180 GLN 180 171 171 GLN GLN E . n 
E 4 181 SER 181 172 172 SER SER E . n 
E 4 182 SER 182 173 173 SER SER E . n 
E 4 183 GLY 183 174 174 GLY GLY E . n 
E 4 184 LEU 184 175 175 LEU LEU E . n 
E 4 185 TYR 185 176 176 TYR TYR E . n 
E 4 186 SER 186 177 177 SER SER E . n 
E 4 187 LEU 187 178 178 LEU LEU E . n 
E 4 188 SER 188 179 179 SER SER E . n 
E 4 189 SER 189 180 180 SER SER E . n 
E 4 190 VAL 190 181 181 VAL VAL E . n 
E 4 191 VAL 191 182 182 VAL VAL E . n 
E 4 192 THR 192 183 183 THR THR E . n 
E 4 193 VAL 193 184 184 VAL VAL E . n 
E 4 194 PRO 194 185 185 PRO PRO E . n 
E 4 195 SER 195 186 186 SER SER E . n 
E 4 196 SER 196 187 187 SER SER E . n 
E 4 197 SER 197 188 188 SER SER E . n 
E 4 198 LEU 198 189 189 LEU LEU E . n 
E 4 199 GLY 199 190 190 GLY GLY E . n 
E 4 200 THR 200 191 191 THR THR E . n 
E 4 201 GLN 201 192 192 GLN GLN E . n 
E 4 202 THR 202 193 193 THR THR E . n 
E 4 203 TYR 203 194 194 TYR TYR E . n 
E 4 204 ILE 204 195 195 ILE ILE E . n 
E 4 205 CYS 205 196 196 CYS CYS E . n 
E 4 206 ASN 206 197 197 ASN ASN E . n 
E 4 207 VAL 207 198 198 VAL VAL E . n 
E 4 208 ASN 208 199 199 ASN ASN E . n 
E 4 209 HIS 209 200 200 HIS HIS E . n 
E 4 210 LYS 210 201 201 LYS LYS E . n 
E 4 211 PRO 211 202 202 PRO PRO E . n 
E 4 212 SER 212 203 203 SER SER E . n 
E 4 213 ASN 213 204 204 ASN ASN E . n 
E 4 214 THR 214 205 205 THR THR E . n 
E 4 215 LYS 215 206 206 LYS LYS E . n 
E 4 216 VAL 216 207 207 VAL VAL E . n 
E 4 217 ASP 217 208 208 ASP ASP E . n 
E 4 218 LYS 218 209 209 LYS LYS E . n 
E 4 219 LYS 219 210 210 LYS LYS E . n 
E 4 220 VAL 220 211 211 VAL VAL E . n 
E 4 221 GLU 221 212 212 GLU GLU E . n 
E 4 222 PRO 222 213 213 PRO PRO E . n 
E 4 223 LYS 223 214 214 LYS LYS E . n 
F 5 1   ASP 1   1   1   ASP ASP F . n 
F 5 2   ILE 2   2   2   ILE ILE F . n 
F 5 3   GLN 3   3   3   GLN GLN F . n 
F 5 4   LEU 4   4   4   LEU LEU F . n 
F 5 5   THR 5   5   5   THR THR F . n 
F 5 6   GLN 6   6   6   GLN GLN F . n 
F 5 7   SER 7   7   7   SER SER F . n 
F 5 8   PRO 8   8   8   PRO PRO F . n 
F 5 9   SER 9   9   9   SER SER F . n 
F 5 10  PHE 10  10  10  PHE PHE F . n 
F 5 11  LEU 11  11  11  LEU LEU F . n 
F 5 12  SER 12  12  12  SER SER F . n 
F 5 13  ALA 13  13  13  ALA ALA F . n 
F 5 14  SER 14  14  14  SER SER F . n 
F 5 15  VAL 15  15  15  VAL VAL F . n 
F 5 16  GLY 16  16  16  GLY GLY F . n 
F 5 17  ASP 17  17  17  ASP ASP F . n 
F 5 18  LYS 18  18  18  LYS LYS F . n 
F 5 19  VAL 19  19  19  VAL VAL F . n 
F 5 20  THR 20  20  20  THR THR F . n 
F 5 21  ILE 21  21  21  ILE ILE F . n 
F 5 22  THR 22  22  22  THR THR F . n 
F 5 23  CYS 23  23  23  CYS CYS F . n 
F 5 24  ARG 24  24  24  ARG ARG F . n 
F 5 25  ALA 25  25  25  ALA ALA F . n 
F 5 26  SER 26  26  26  SER SER F . n 
F 5 27  GLN 27  27  27  GLN GLN F . n 
F 5 28  GLY 28  28  28  GLY GLY F . n 
F 5 29  VAL 29  29  29  VAL VAL F . n 
F 5 30  ARG 30  30  30  ARG ARG F . n 
F 5 31  ASN 31  31  31  ASN ASN F . n 
F 5 32  GLU 32  32  32  GLU GLU F . n 
F 5 33  LEU 33  33  33  LEU LEU F . n 
F 5 34  ALA 34  34  34  ALA ALA F . n 
F 5 35  TRP 35  35  35  TRP TRP F . n 
F 5 36  TYR 36  36  36  TYR TYR F . n 
F 5 37  GLN 37  37  37  GLN GLN F . n 
F 5 38  GLN 38  38  38  GLN GLN F . n 
F 5 39  LYS 39  39  39  LYS LYS F . n 
F 5 40  PRO 40  40  40  PRO PRO F . n 
F 5 41  GLY 41  41  41  GLY GLY F . n 
F 5 42  LYS 42  42  42  LYS LYS F . n 
F 5 43  ALA 43  43  43  ALA ALA F . n 
F 5 44  PRO 44  44  44  PRO PRO F . n 
F 5 45  ASN 45  45  45  ASN ASN F . n 
F 5 46  LEU 46  46  46  LEU LEU F . n 
F 5 47  LEU 47  47  47  LEU LEU F . n 
F 5 48  ILE 48  48  48  ILE ILE F . n 
F 5 49  TYR 49  49  49  TYR TYR F . n 
F 5 50  TYR 50  50  50  TYR TYR F . n 
F 5 51  ALA 51  51  51  ALA ALA F . n 
F 5 52  SER 52  52  52  SER SER F . n 
F 5 53  THR 53  53  53  THR THR F . n 
F 5 54  LEU 54  54  54  LEU LEU F . n 
F 5 55  GLN 55  55  55  GLN GLN F . n 
F 5 56  SER 56  56  56  SER SER F . n 
F 5 57  GLY 57  57  57  GLY GLY F . n 
F 5 58  VAL 58  58  58  VAL VAL F . n 
F 5 59  PRO 59  59  59  PRO PRO F . n 
F 5 60  SER 60  60  60  SER SER F . n 
F 5 61  ARG 61  61  61  ARG ARG F . n 
F 5 62  PHE 62  62  62  PHE PHE F . n 
F 5 63  SER 63  63  63  SER SER F . n 
F 5 64  ALA 64  64  64  ALA ALA F . n 
F 5 65  THR 65  65  65  THR THR F . n 
F 5 66  GLY 66  66  66  GLY GLY F . n 
F 5 67  SER 67  67  67  SER SER F . n 
F 5 68  GLY 68  68  68  GLY GLY F . n 
F 5 69  THR 69  69  69  THR THR F . n 
F 5 70  HIS 70  70  70  HIS HIS F . n 
F 5 71  PHE 71  71  71  PHE PHE F . n 
F 5 72  THR 72  72  72  THR THR F . n 
F 5 73  LEU 73  73  73  LEU LEU F . n 
F 5 74  THR 74  74  74  THR THR F . n 
F 5 75  VAL 75  75  75  VAL VAL F . n 
F 5 76  SER 76  76  76  SER SER F . n 
F 5 77  SER 77  77  77  SER SER F . n 
F 5 78  LEU 78  78  78  LEU LEU F . n 
F 5 79  GLN 79  79  79  GLN GLN F . n 
F 5 80  PRO 80  80  80  PRO PRO F . n 
F 5 81  GLU 81  81  81  GLU GLU F . n 
F 5 82  ASP 82  82  82  ASP ASP F . n 
F 5 83  PHE 83  83  83  PHE PHE F . n 
F 5 84  ALA 84  84  84  ALA ALA F . n 
F 5 85  THR 85  85  85  THR THR F . n 
F 5 86  TYR 86  86  86  TYR TYR F . n 
F 5 87  PHE 87  87  87  PHE PHE F . n 
F 5 88  CYS 88  88  88  CYS CYS F . n 
F 5 89  GLN 89  89  89  GLN GLN F . n 
F 5 90  HIS 90  90  90  HIS HIS F . n 
F 5 91  MET 91  91  91  MET MET F . n 
F 5 92  SER 92  92  92  SER SER F . n 
F 5 93  SER 93  93  93  SER SER F . n 
F 5 94  TYR 94  94  94  TYR TYR F . n 
F 5 95  PRO 95  95  95  PRO PRO F . n 
F 5 96  LEU 96  96  96  LEU LEU F . n 
F 5 97  THR 97  97  97  THR THR F . n 
F 5 98  PHE 98  98  98  PHE PHE F . n 
F 5 99  GLY 99  99  99  GLY GLY F . n 
F 5 100 GLY 100 100 100 GLY GLY F . n 
F 5 101 GLY 101 101 101 GLY GLY F . n 
F 5 102 THR 102 102 102 THR THR F . n 
F 5 103 LYS 103 103 103 LYS LYS F . n 
F 5 104 VAL 104 104 104 VAL VAL F . n 
F 5 105 GLU 105 105 105 GLU GLU F . n 
F 5 106 ILE 106 106 106 ILE ILE F . n 
F 5 107 LYS 107 107 107 LYS LYS F . n 
F 5 108 ARG 108 108 108 ARG ARG F . n 
F 5 109 THR 109 109 109 THR THR F . n 
F 5 110 VAL 110 110 110 VAL VAL F . n 
F 5 111 ALA 111 111 111 ALA ALA F . n 
F 5 112 ALA 112 112 112 ALA ALA F . n 
F 5 113 PRO 113 113 113 PRO PRO F . n 
F 5 114 SER 114 114 114 SER SER F . n 
F 5 115 VAL 115 115 115 VAL VAL F . n 
F 5 116 PHE 116 116 116 PHE PHE F . n 
F 5 117 ILE 117 117 117 ILE ILE F . n 
F 5 118 PHE 118 118 118 PHE PHE F . n 
F 5 119 PRO 119 119 119 PRO PRO F . n 
F 5 120 PRO 120 120 120 PRO PRO F . n 
F 5 121 SER 121 121 121 SER SER F . n 
F 5 122 ASP 122 122 122 ASP ASP F . n 
F 5 123 GLU 123 123 123 GLU GLU F . n 
F 5 124 GLN 124 124 124 GLN GLN F . n 
F 5 125 LEU 125 125 125 LEU LEU F . n 
F 5 126 LYS 126 126 126 LYS LYS F . n 
F 5 127 SER 127 127 127 SER SER F . n 
F 5 128 GLY 128 128 128 GLY GLY F . n 
F 5 129 THR 129 129 129 THR THR F . n 
F 5 130 ALA 130 130 130 ALA ALA F . n 
F 5 131 SER 131 131 131 SER SER F . n 
F 5 132 VAL 132 132 132 VAL VAL F . n 
F 5 133 VAL 133 133 133 VAL VAL F . n 
F 5 134 CYS 134 134 134 CYS CYS F . n 
F 5 135 LEU 135 135 135 LEU LEU F . n 
F 5 136 LEU 136 136 136 LEU LEU F . n 
F 5 137 ASN 137 137 137 ASN ASN F . n 
F 5 138 ASN 138 138 138 ASN ASN F . n 
F 5 139 PHE 139 139 139 PHE PHE F . n 
F 5 140 TYR 140 140 140 TYR TYR F . n 
F 5 141 PRO 141 141 141 PRO PRO F . n 
F 5 142 ARG 142 142 142 ARG ARG F . n 
F 5 143 GLU 143 143 143 GLU GLU F . n 
F 5 144 ALA 144 144 144 ALA ALA F . n 
F 5 145 LYS 145 145 145 LYS LYS F . n 
F 5 146 VAL 146 146 146 VAL VAL F . n 
F 5 147 GLN 147 147 147 GLN GLN F . n 
F 5 148 TRP 148 148 148 TRP TRP F . n 
F 5 149 LYS 149 149 149 LYS LYS F . n 
F 5 150 VAL 150 150 150 VAL VAL F . n 
F 5 151 ASP 151 151 151 ASP ASP F . n 
F 5 152 ASN 152 152 152 ASN ASN F . n 
F 5 153 ALA 153 153 153 ALA ALA F . n 
F 5 154 LEU 154 154 154 LEU LEU F . n 
F 5 155 GLN 155 155 155 GLN GLN F . n 
F 5 156 SER 156 156 156 SER SER F . n 
F 5 157 GLY 157 157 157 GLY GLY F . n 
F 5 158 ASN 158 158 158 ASN ASN F . n 
F 5 159 SER 159 159 159 SER SER F . n 
F 5 160 GLN 160 160 160 GLN GLN F . n 
F 5 161 GLU 161 161 161 GLU GLU F . n 
F 5 162 SER 162 162 162 SER SER F . n 
F 5 163 VAL 163 163 163 VAL VAL F . n 
F 5 164 THR 164 164 164 THR THR F . n 
F 5 165 GLU 165 165 165 GLU GLU F . n 
F 5 166 GLN 166 166 166 GLN GLN F . n 
F 5 167 ASP 167 167 167 ASP ASP F . n 
F 5 168 SER 168 168 168 SER SER F . n 
F 5 169 LYS 169 169 169 LYS LYS F . n 
F 5 170 ASP 170 170 170 ASP ASP F . n 
F 5 171 SER 171 171 171 SER SER F . n 
F 5 172 THR 172 172 172 THR THR F . n 
F 5 173 TYR 173 173 173 TYR TYR F . n 
F 5 174 SER 174 174 174 SER SER F . n 
F 5 175 LEU 175 175 175 LEU LEU F . n 
F 5 176 SER 176 176 176 SER SER F . n 
F 5 177 SER 177 177 177 SER SER F . n 
F 5 178 THR 178 178 178 THR THR F . n 
F 5 179 LEU 179 179 179 LEU LEU F . n 
F 5 180 THR 180 180 180 THR THR F . n 
F 5 181 LEU 181 181 181 LEU LEU F . n 
F 5 182 SER 182 182 182 SER SER F . n 
F 5 183 LYS 183 183 183 LYS LYS F . n 
F 5 184 ALA 184 184 184 ALA ALA F . n 
F 5 185 ASP 185 185 185 ASP ASP F . n 
F 5 186 TYR 186 186 186 TYR TYR F . n 
F 5 187 GLU 187 187 187 GLU GLU F . n 
F 5 188 LYS 188 188 188 LYS LYS F . n 
F 5 189 HIS 189 189 189 HIS HIS F . n 
F 5 190 LYS 190 190 190 LYS LYS F . n 
F 5 191 VAL 191 191 191 VAL VAL F . n 
F 5 192 TYR 192 192 192 TYR TYR F . n 
F 5 193 ALA 193 193 193 ALA ALA F . n 
F 5 194 CYS 194 194 194 CYS CYS F . n 
F 5 195 GLU 195 195 195 GLU GLU F . n 
F 5 196 VAL 196 196 196 VAL VAL F . n 
F 5 197 THR 197 197 197 THR THR F . n 
F 5 198 HIS 198 198 198 HIS HIS F . n 
F 5 199 GLN 199 199 199 GLN GLN F . n 
F 5 200 GLY 200 200 200 GLY GLY F . n 
F 5 201 LEU 201 201 201 LEU LEU F . n 
F 5 202 SER 202 202 202 SER SER F . n 
F 5 203 SER 203 203 203 SER SER F . n 
F 5 204 PRO 204 204 204 PRO PRO F . n 
F 5 205 VAL 205 205 205 VAL VAL F . n 
F 5 206 THR 206 206 206 THR THR F . n 
F 5 207 LYS 207 207 207 LYS LYS F . n 
F 5 208 SER 208 208 208 SER SER F . n 
F 5 209 PHE 209 209 209 PHE PHE F . n 
F 5 210 ASN 210 210 210 ASN ASN F . n 
F 5 211 ARG 211 211 211 ARG ARG F . n 
F 5 212 GLY 212 212 212 GLY GLY F . n 
G 4 1   GLN 1   1   1   GLN GLN G . n 
G 4 2   GLU 2   2   2   GLU GLU G . n 
G 4 3   VAL 3   3   3   VAL VAL G . n 
G 4 4   LEU 4   4   4   LEU LEU G . n 
G 4 5   VAL 5   5   5   VAL VAL G . n 
G 4 6   GLN 6   6   6   GLN GLN G . n 
G 4 7   SER 7   7   7   SER SER G . n 
G 4 8   GLY 8   8   8   GLY GLY G . n 
G 4 9   ALA 9   9   9   ALA ALA G . n 
G 4 10  GLU 10  10  10  GLU GLU G . n 
G 4 11  VAL 11  11  11  VAL VAL G . n 
G 4 12  LYS 12  12  12  LYS LYS G . n 
G 4 13  LYS 13  13  13  LYS LYS G . n 
G 4 14  PRO 14  14  14  PRO PRO G . n 
G 4 15  GLY 15  15  15  GLY GLY G . n 
G 4 16  ALA 16  16  16  ALA ALA G . n 
G 4 17  SER 17  17  17  SER SER G . n 
G 4 18  VAL 18  18  18  VAL VAL G . n 
G 4 19  LYS 19  19  19  LYS LYS G . n 
G 4 20  VAL 20  20  20  VAL VAL G . n 
G 4 21  SER 21  21  21  SER SER G . n 
G 4 22  CYS 22  22  22  CYS CYS G . n 
G 4 23  ARG 23  23  23  ARG ARG G . n 
G 4 24  ALA 24  24  24  ALA ALA G . n 
G 4 25  PHE 25  25  25  PHE PHE G . n 
G 4 26  GLY 26  26  26  GLY GLY G . n 
G 4 27  TYR 27  27  27  TYR TYR G . n 
G 4 28  THR 28  28  28  THR THR G . n 
G 4 29  PHE 29  29  29  PHE PHE G . n 
G 4 30  THR 30  30  30  THR THR G . n 
G 4 31  GLY 31  31  31  GLY GLY G . n 
G 4 32  ASN 32  32  32  ASN ASN G . n 
G 4 33  ALA 33  33  33  ALA ALA G . n 
G 4 34  LEU 34  34  34  LEU LEU G . n 
G 4 35  HIS 35  35  35  HIS HIS G . n 
G 4 36  TRP 36  36  36  TRP TRP G . n 
G 4 37  VAL 37  37  37  VAL VAL G . n 
G 4 38  ARG 38  38  38  ARG ARG G . n 
G 4 39  GLN 39  39  39  GLN GLN G . n 
G 4 40  ALA 40  40  40  ALA ALA G . n 
G 4 41  PRO 41  41  41  PRO PRO G . n 
G 4 42  GLY 42  42  42  GLY GLY G . n 
G 4 43  GLN 43  43  43  GLN GLN G . n 
G 4 44  GLY 44  44  44  GLY GLY G . n 
G 4 45  LEU 45  45  45  LEU LEU G . n 
G 4 46  GLU 46  46  46  GLU GLU G . n 
G 4 47  TRP 47  47  47  TRP TRP G . n 
G 4 48  LEU 48  48  48  LEU LEU G . n 
G 4 49  GLY 49  49  49  GLY GLY G . n 
G 4 50  TRP 50  50  50  TRP TRP G . n 
G 4 51  ILE 51  51  51  ILE ILE G . n 
G 4 52  ASN 52  52  52  ASN ASN G . n 
G 4 53  PRO 53  52  52  PRO PRO G A n 
G 4 54  HIS 54  53  53  HIS HIS G . n 
G 4 55  SER 55  54  54  SER SER G . n 
G 4 56  GLY 56  55  55  GLY GLY G . n 
G 4 57  ASP 57  56  56  ASP ASP G . n 
G 4 58  THR 58  57  57  THR THR G . n 
G 4 59  THR 59  58  58  THR THR G . n 
G 4 60  THR 60  59  59  THR THR G . n 
G 4 61  SER 61  60  60  SER SER G . n 
G 4 62  GLN 62  61  61  GLN GLN G . n 
G 4 63  LYS 63  62  62  LYS LYS G . n 
G 4 64  PHE 64  63  63  PHE PHE G . n 
G 4 65  GLN 65  64  64  GLN GLN G . n 
G 4 66  GLY 66  65  65  GLY GLY G . n 
G 4 67  ARG 67  66  66  ARG ARG G . n 
G 4 68  VAL 68  67  67  VAL VAL G . n 
G 4 69  TYR 69  68  68  TYR TYR G . n 
G 4 70  MET 70  69  69  MET MET G . n 
G 4 71  THR 71  70  70  THR THR G . n 
G 4 72  ARG 72  71  71  ARG ARG G . n 
G 4 73  ASP 73  72  72  ASP ASP G . n 
G 4 74  LYS 74  73  73  LYS LYS G . n 
G 4 75  SER 75  74  74  SER SER G . n 
G 4 76  ILE 76  75  75  ILE ILE G . n 
G 4 77  ASN 77  76  76  ASN ASN G . n 
G 4 78  THR 78  77  77  THR THR G . n 
G 4 79  ALA 79  78  78  ALA ALA G . n 
G 4 80  PHE 80  79  79  PHE PHE G . n 
G 4 81  LEU 81  80  80  LEU LEU G . n 
G 4 82  ASP 82  81  81  ASP ASP G . n 
G 4 83  VAL 83  82  82  VAL VAL G . n 
G 4 84  THR 84  82  82  THR THR G A n 
G 4 85  ARG 85  82  82  ARG ARG G B n 
G 4 86  LEU 86  82  82  LEU LEU G C n 
G 4 87  THR 87  83  83  THR THR G . n 
G 4 88  SER 88  84  84  SER SER G . n 
G 4 89  ASP 89  85  85  ASP ASP G . n 
G 4 90  ASP 90  86  86  ASP ASP G . n 
G 4 91  THR 91  87  87  THR THR G . n 
G 4 92  GLY 92  88  88  GLY GLY G . n 
G 4 93  ILE 93  89  89  ILE ILE G . n 
G 4 94  TYR 94  90  90  TYR TYR G . n 
G 4 95  TYR 95  91  91  TYR TYR G . n 
G 4 96  CYS 96  92  92  CYS CYS G . n 
G 4 97  ALA 97  93  93  ALA ALA G . n 
G 4 98  ARG 98  94  94  ARG ARG G . n 
G 4 99  ASP 99  95  95  ASP ASP G . n 
G 4 100 LYS 100 96  96  LYS LYS G . n 
G 4 101 TYR 101 97  97  TYR TYR G . n 
G 4 102 TYR 102 98  98  TYR TYR G . n 
G 4 103 GLY 103 99  99  GLY GLY G . n 
G 4 104 ASN 104 100 100 ASN ASN G . n 
G 4 105 GLU 105 100 100 GLU GLU G A n 
G 4 106 ALA 106 100 100 ALA ALA G B n 
G 4 107 VAL 107 100 100 VAL VAL G C n 
G 4 108 GLY 108 100 100 GLY GLY G D n 
G 4 109 MET 109 100 100 MET MET G E n 
G 4 110 ASP 110 101 101 ASP ASP G . n 
G 4 111 VAL 111 102 102 VAL VAL G . n 
G 4 112 TRP 112 103 103 TRP TRP G . n 
G 4 113 GLY 113 104 104 GLY GLY G . n 
G 4 114 GLN 114 105 105 GLN GLN G . n 
G 4 115 GLY 115 106 106 GLY GLY G . n 
G 4 116 THR 116 107 107 THR THR G . n 
G 4 117 SER 117 108 108 SER SER G . n 
G 4 118 VAL 118 109 109 VAL VAL G . n 
G 4 119 THR 119 110 110 THR THR G . n 
G 4 120 VAL 120 111 111 VAL VAL G . n 
G 4 121 SER 121 112 112 SER SER G . n 
G 4 122 SER 122 113 113 SER SER G . n 
G 4 123 ALA 123 114 114 ALA ALA G . n 
G 4 124 SER 124 115 115 SER SER G . n 
G 4 125 THR 125 116 116 THR THR G . n 
G 4 126 LYS 126 117 117 LYS LYS G . n 
G 4 127 GLY 127 118 118 GLY GLY G . n 
G 4 128 PRO 128 119 119 PRO PRO G . n 
G 4 129 SER 129 120 120 SER SER G . n 
G 4 130 VAL 130 121 121 VAL VAL G . n 
G 4 131 PHE 131 122 122 PHE PHE G . n 
G 4 132 PRO 132 123 123 PRO PRO G . n 
G 4 133 LEU 133 124 124 LEU LEU G . n 
G 4 134 ALA 134 125 125 ALA ALA G . n 
G 4 135 PRO 135 126 126 PRO PRO G . n 
G 4 136 SER 136 127 127 SER SER G . n 
G 4 137 SER 137 128 128 SER SER G . n 
G 4 138 LYS 138 129 129 LYS LYS G . n 
G 4 139 SER 139 130 130 SER SER G . n 
G 4 140 THR 140 131 131 THR THR G . n 
G 4 141 SER 141 132 132 SER SER G . n 
G 4 142 GLY 142 133 133 GLY GLY G . n 
G 4 143 GLY 143 134 134 GLY GLY G . n 
G 4 144 THR 144 135 135 THR THR G . n 
G 4 145 ALA 145 136 136 ALA ALA G . n 
G 4 146 ALA 146 137 137 ALA ALA G . n 
G 4 147 LEU 147 138 138 LEU LEU G . n 
G 4 148 GLY 148 139 139 GLY GLY G . n 
G 4 149 CYS 149 140 140 CYS CYS G . n 
G 4 150 LEU 150 141 141 LEU LEU G . n 
G 4 151 VAL 151 142 142 VAL VAL G . n 
G 4 152 LYS 152 143 143 LYS LYS G . n 
G 4 153 ASP 153 144 144 ASP ASP G . n 
G 4 154 TYR 154 145 145 TYR TYR G . n 
G 4 155 PHE 155 146 146 PHE PHE G . n 
G 4 156 PRO 156 147 147 PRO PRO G . n 
G 4 157 GLU 157 148 148 GLU GLU G . n 
G 4 158 PRO 158 149 149 PRO PRO G . n 
G 4 159 VAL 159 150 150 VAL VAL G . n 
G 4 160 THR 160 151 151 THR THR G . n 
G 4 161 VAL 161 152 152 VAL VAL G . n 
G 4 162 SER 162 153 153 SER SER G . n 
G 4 163 TRP 163 154 154 TRP TRP G . n 
G 4 164 ASN 164 155 155 ASN ASN G . n 
G 4 165 SER 165 156 156 SER SER G . n 
G 4 166 GLY 166 157 157 GLY GLY G . n 
G 4 167 ALA 167 158 158 ALA ALA G . n 
G 4 168 LEU 168 159 159 LEU LEU G . n 
G 4 169 THR 169 160 160 THR THR G . n 
G 4 170 SER 170 161 161 SER SER G . n 
G 4 171 GLY 171 162 162 GLY GLY G . n 
G 4 172 VAL 172 163 163 VAL VAL G . n 
G 4 173 HIS 173 164 164 HIS HIS G . n 
G 4 174 THR 174 165 165 THR THR G . n 
G 4 175 PHE 175 166 166 PHE PHE G . n 
G 4 176 PRO 176 167 167 PRO PRO G . n 
G 4 177 ALA 177 168 168 ALA ALA G . n 
G 4 178 VAL 178 169 169 VAL VAL G . n 
G 4 179 LEU 179 170 170 LEU LEU G . n 
G 4 180 GLN 180 171 171 GLN GLN G . n 
G 4 181 SER 181 172 172 SER SER G . n 
G 4 182 SER 182 173 173 SER SER G . n 
G 4 183 GLY 183 174 174 GLY GLY G . n 
G 4 184 LEU 184 175 175 LEU LEU G . n 
G 4 185 TYR 185 176 176 TYR TYR G . n 
G 4 186 SER 186 177 177 SER SER G . n 
G 4 187 LEU 187 178 178 LEU LEU G . n 
G 4 188 SER 188 179 179 SER SER G . n 
G 4 189 SER 189 180 180 SER SER G . n 
G 4 190 VAL 190 181 181 VAL VAL G . n 
G 4 191 VAL 191 182 182 VAL VAL G . n 
G 4 192 THR 192 183 183 THR THR G . n 
G 4 193 VAL 193 184 184 VAL VAL G . n 
G 4 194 PRO 194 185 185 PRO PRO G . n 
G 4 195 SER 195 186 186 SER SER G . n 
G 4 196 SER 196 187 187 SER SER G . n 
G 4 197 SER 197 188 188 SER SER G . n 
G 4 198 LEU 198 189 189 LEU LEU G . n 
G 4 199 GLY 199 190 190 GLY GLY G . n 
G 4 200 THR 200 191 191 THR THR G . n 
G 4 201 GLN 201 192 192 GLN GLN G . n 
G 4 202 THR 202 193 193 THR THR G . n 
G 4 203 TYR 203 194 194 TYR TYR G . n 
G 4 204 ILE 204 195 195 ILE ILE G . n 
G 4 205 CYS 205 196 196 CYS CYS G . n 
G 4 206 ASN 206 197 197 ASN ASN G . n 
G 4 207 VAL 207 198 198 VAL VAL G . n 
G 4 208 ASN 208 199 199 ASN ASN G . n 
G 4 209 HIS 209 200 200 HIS HIS G . n 
G 4 210 LYS 210 201 201 LYS LYS G . n 
G 4 211 PRO 211 202 202 PRO PRO G . n 
G 4 212 SER 212 203 203 SER SER G . n 
G 4 213 ASN 213 204 204 ASN ASN G . n 
G 4 214 THR 214 205 205 THR THR G . n 
G 4 215 LYS 215 206 206 LYS LYS G . n 
G 4 216 VAL 216 207 207 VAL VAL G . n 
G 4 217 ASP 217 208 208 ASP ASP G . n 
G 4 218 LYS 218 209 209 LYS LYS G . n 
G 4 219 LYS 219 210 210 LYS LYS G . n 
G 4 220 VAL 220 211 211 VAL VAL G . n 
G 4 221 GLU 221 212 212 GLU GLU G . n 
G 4 222 PRO 222 213 213 PRO PRO G . n 
G 4 223 LYS 223 214 214 LYS LYS G . n 
H 2 1   ALA 1   512 512 ALA ALA D . n 
H 2 2   VAL 2   513 513 VAL VAL D . n 
H 2 3   GLY 3   514 514 GLY GLY D . n 
H 2 4   ILE 4   515 515 ILE ILE D . n 
H 2 5   GLY 5   516 516 GLY GLY D . n 
H 2 6   ALA 6   517 517 ALA ALA D . n 
H 2 7   VAL 7   518 518 VAL VAL D . n 
H 2 8   PHE 8   519 519 PHE PHE D . n 
H 2 9   LEU 9   520 520 LEU LEU D . n 
H 2 10  GLY 10  521 521 GLY GLY D . n 
H 2 11  PHE 11  522 522 PHE PHE D . n 
H 2 12  LEU 12  523 523 LEU LEU D . n 
H 2 13  GLY 13  524 524 GLY GLY D . n 
H 2 14  ALA 14  525 525 ALA ALA D . n 
H 2 15  ALA 15  526 526 ALA ALA D . n 
H 2 16  GLY 16  527 527 GLY GLY D . n 
H 2 17  SER 17  528 528 SER SER D . n 
H 2 18  THR 18  529 529 THR THR D . n 
H 2 19  MET 19  530 530 MET MET D . n 
H 2 20  GLY 20  531 531 GLY GLY D . n 
H 2 21  ALA 21  532 532 ALA ALA D . n 
H 2 22  ALA 22  533 533 ALA ALA D . n 
H 2 23  SER 23  534 534 SER SER D . n 
H 2 24  MET 24  535 535 MET MET D . n 
H 2 25  THR 25  536 536 THR THR D . n 
H 2 26  LEU 26  537 537 LEU LEU D . n 
H 2 27  THR 27  538 538 THR THR D . n 
H 2 28  VAL 28  539 539 VAL VAL D . n 
H 2 29  GLN 29  540 540 GLN GLN D . n 
H 2 30  ALA 30  541 541 ALA ALA D . n 
H 2 31  ARG 31  542 542 ARG ARG D . n 
H 2 32  ASN 32  543 543 ASN ASN D . n 
H 2 33  LEU 33  544 544 LEU LEU D . n 
H 2 34  LEU 34  545 545 LEU LEU D . n 
H 2 35  SER 35  546 546 SER SER D . n 
H 2 36  GLY 36  547 547 GLY GLY D . n 
H 2 37  ILE 37  548 ?   ?   ?   D . n 
H 2 38  VAL 38  549 ?   ?   ?   D . n 
H 2 39  GLN 39  550 ?   ?   ?   D . n 
H 2 40  GLN 40  551 ?   ?   ?   D . n 
H 2 41  GLN 41  552 ?   ?   ?   D . n 
H 2 42  SER 42  553 ?   ?   ?   D . n 
H 2 43  ASN 43  554 ?   ?   ?   D . n 
H 2 44  LEU 44  555 ?   ?   ?   D . n 
H 2 45  LEU 45  556 ?   ?   ?   D . n 
H 2 46  ARG 46  557 ?   ?   ?   D . n 
H 2 47  ALA 47  558 ?   ?   ?   D . n 
H 2 48  ILE 48  559 ?   ?   ?   D . n 
H 2 49  GLU 49  560 ?   ?   ?   D . n 
H 2 50  ALA 50  561 ?   ?   ?   D . n 
H 2 51  GLN 51  562 ?   ?   ?   D . n 
H 2 52  GLN 52  563 ?   ?   ?   D . n 
H 2 53  HIS 53  564 ?   ?   ?   D . n 
H 2 54  LEU 54  565 ?   ?   ?   D . n 
H 2 55  LEU 55  566 ?   ?   ?   D . n 
H 2 56  LYS 56  567 ?   ?   ?   D . n 
H 2 57  LEU 57  568 ?   ?   ?   D . n 
H 2 58  THR 58  569 569 THR THR D . n 
H 2 59  VAL 59  570 570 VAL VAL D . n 
H 2 60  TRP 60  571 571 TRP TRP D . n 
H 2 61  GLY 61  572 572 GLY GLY D . n 
H 2 62  ILE 62  573 573 ILE ILE D . n 
H 2 63  LYS 63  574 574 LYS LYS D . n 
H 2 64  GLN 64  575 575 GLN GLN D . n 
H 2 65  LEU 65  576 576 LEU LEU D . n 
H 2 66  GLN 66  577 577 GLN GLN D . n 
H 2 67  ALA 67  578 578 ALA ALA D . n 
H 2 68  ARG 68  579 579 ARG ARG D . n 
H 2 69  VAL 69  580 580 VAL VAL D . n 
H 2 70  LEU 70  581 581 LEU LEU D . n 
H 2 71  ALA 71  582 582 ALA ALA D . n 
H 2 72  VAL 72  583 583 VAL VAL D . n 
H 2 73  GLU 73  584 584 GLU GLU D . n 
H 2 74  ARG 74  585 585 ARG ARG D . n 
H 2 75  TYR 75  586 586 TYR TYR D . n 
H 2 76  LEU 76  587 587 LEU LEU D . n 
H 2 77  ARG 77  588 588 ARG ARG D . n 
H 2 78  ASP 78  589 589 ASP ASP D . n 
H 2 79  GLN 79  590 590 GLN GLN D . n 
H 2 80  GLN 80  591 591 GLN GLN D . n 
H 2 81  LEU 81  592 592 LEU LEU D . n 
H 2 82  LEU 82  593 593 LEU LEU D . n 
H 2 83  GLY 83  594 594 GLY GLY D . n 
H 2 84  ILE 84  595 595 ILE ILE D . n 
H 2 85  TRP 85  596 596 TRP TRP D . n 
H 2 86  GLY 86  597 597 GLY GLY D . n 
H 2 87  CYS 87  598 598 CYS CYS D . n 
H 2 88  SER 88  599 599 SER SER D . n 
H 2 89  GLY 89  600 600 GLY GLY D . n 
H 2 90  LYS 90  601 601 LYS LYS D . n 
H 2 91  LEU 91  602 602 LEU LEU D . n 
H 2 92  ILE 92  603 603 ILE ILE D . n 
H 2 93  CYS 93  604 604 CYS CYS D . n 
H 2 94  CYS 94  605 605 CYS CYS D . n 
H 2 95  THR 95  606 606 THR THR D . n 
H 2 96  ASN 96  607 607 ASN ASN D . n 
H 2 97  VAL 97  608 608 VAL VAL D . n 
H 2 98  PRO 98  609 609 PRO PRO D . n 
H 2 99  TRP 99  610 610 TRP TRP D . n 
H 2 100 ASN 100 611 611 ASN ASN D . n 
H 2 101 SER 101 612 612 SER SER D . n 
H 2 102 SER 102 613 613 SER SER D . n 
H 2 103 TRP 103 614 614 TRP TRP D . n 
H 2 104 SER 104 615 615 SER SER D . n 
H 2 105 ASN 105 616 616 ASN ASN D . n 
H 2 106 ARG 106 617 617 ARG ARG D . n 
H 2 107 ASN 107 618 618 ASN ASN D . n 
H 2 108 LEU 108 619 619 LEU LEU D . n 
H 2 109 SER 109 620 620 SER SER D . n 
H 2 110 GLU 110 621 621 GLU GLU D . n 
H 2 111 ILE 111 622 622 ILE ILE D . n 
H 2 112 TRP 112 623 623 TRP TRP D . n 
H 2 113 ASP 113 624 624 ASP ASP D . n 
H 2 114 ASN 114 625 625 ASN ASN D . n 
H 2 115 MET 115 626 626 MET MET D . n 
H 2 116 THR 116 627 627 THR THR D . n 
H 2 117 TRP 117 628 628 TRP TRP D . n 
H 2 118 LEU 118 629 629 LEU LEU D . n 
H 2 119 GLN 119 630 630 GLN GLN D . n 
H 2 120 TRP 120 631 631 TRP TRP D . n 
H 2 121 ASP 121 632 632 ASP ASP D . n 
H 2 122 LYS 122 633 633 LYS LYS D . n 
H 2 123 GLU 123 634 634 GLU GLU D . n 
H 2 124 ILE 124 635 635 ILE ILE D . n 
H 2 125 SER 125 636 636 SER SER D . n 
H 2 126 ASN 126 637 637 ASN ASN D . n 
H 2 127 TYR 127 638 638 TYR TYR D . n 
H 2 128 THR 128 639 639 THR THR D . n 
H 2 129 GLN 129 640 640 GLN GLN D . n 
H 2 130 ILE 130 641 641 ILE ILE D . n 
H 2 131 ILE 131 642 642 ILE ILE D . n 
H 2 132 TYR 132 643 643 TYR TYR D . n 
H 2 133 GLY 133 644 644 GLY GLY D . n 
H 2 134 LEU 134 645 645 LEU LEU D . n 
H 2 135 LEU 135 646 646 LEU LEU D . n 
H 2 136 GLU 136 647 647 GLU GLU D . n 
H 2 137 GLU 137 648 648 GLU GLU D . n 
H 2 138 SER 138 649 649 SER SER D . n 
H 2 139 GLN 139 650 650 GLN GLN D . n 
H 2 140 ASN 140 651 651 ASN ASN D . n 
H 2 141 GLN 141 652 652 GLN GLN D . n 
H 2 142 GLN 142 653 653 GLN GLN D . n 
H 2 143 GLU 143 654 654 GLU GLU D . n 
H 2 144 LYS 144 655 655 LYS LYS D . n 
H 2 145 ASN 145 656 656 ASN ASN D . n 
H 2 146 GLU 146 657 657 GLU GLU D . n 
H 2 147 GLN 147 658 658 GLN GLN D . n 
H 2 148 ASP 148 659 659 ASP ASP D . n 
H 2 149 LEU 149 660 660 LEU LEU D . n 
H 2 150 LEU 150 661 661 LEU LEU D . n 
H 2 151 ALA 151 662 662 ALA ALA D . n 
H 2 152 LEU 152 663 663 LEU LEU D . n 
H 2 153 ASP 153 664 664 ASP ASP D . n 
I 5 1   ASP 1   1   1   ASP ASP H . n 
I 5 2   ILE 2   2   2   ILE ILE H . n 
I 5 3   GLN 3   3   3   GLN GLN H . n 
I 5 4   LEU 4   4   4   LEU LEU H . n 
I 5 5   THR 5   5   5   THR THR H . n 
I 5 6   GLN 6   6   6   GLN GLN H . n 
I 5 7   SER 7   7   7   SER SER H . n 
I 5 8   PRO 8   8   8   PRO PRO H . n 
I 5 9   SER 9   9   9   SER SER H . n 
I 5 10  PHE 10  10  10  PHE PHE H . n 
I 5 11  LEU 11  11  11  LEU LEU H . n 
I 5 12  SER 12  12  12  SER SER H . n 
I 5 13  ALA 13  13  13  ALA ALA H . n 
I 5 14  SER 14  14  14  SER SER H . n 
I 5 15  VAL 15  15  15  VAL VAL H . n 
I 5 16  GLY 16  16  16  GLY GLY H . n 
I 5 17  ASP 17  17  17  ASP ASP H . n 
I 5 18  LYS 18  18  18  LYS LYS H . n 
I 5 19  VAL 19  19  19  VAL VAL H . n 
I 5 20  THR 20  20  20  THR THR H . n 
I 5 21  ILE 21  21  21  ILE ILE H . n 
I 5 22  THR 22  22  22  THR THR H . n 
I 5 23  CYS 23  23  23  CYS CYS H . n 
I 5 24  ARG 24  24  24  ARG ARG H . n 
I 5 25  ALA 25  25  25  ALA ALA H . n 
I 5 26  SER 26  26  26  SER SER H . n 
I 5 27  GLN 27  27  27  GLN GLN H . n 
I 5 28  GLY 28  28  28  GLY GLY H . n 
I 5 29  VAL 29  29  29  VAL VAL H . n 
I 5 30  ARG 30  30  30  ARG ARG H . n 
I 5 31  ASN 31  31  31  ASN ASN H . n 
I 5 32  GLU 32  32  32  GLU GLU H . n 
I 5 33  LEU 33  33  33  LEU LEU H . n 
I 5 34  ALA 34  34  34  ALA ALA H . n 
I 5 35  TRP 35  35  35  TRP TRP H . n 
I 5 36  TYR 36  36  36  TYR TYR H . n 
I 5 37  GLN 37  37  37  GLN GLN H . n 
I 5 38  GLN 38  38  38  GLN GLN H . n 
I 5 39  LYS 39  39  39  LYS LYS H . n 
I 5 40  PRO 40  40  40  PRO PRO H . n 
I 5 41  GLY 41  41  41  GLY GLY H . n 
I 5 42  LYS 42  42  42  LYS LYS H . n 
I 5 43  ALA 43  43  43  ALA ALA H . n 
I 5 44  PRO 44  44  44  PRO PRO H . n 
I 5 45  ASN 45  45  45  ASN ASN H . n 
I 5 46  LEU 46  46  46  LEU LEU H . n 
I 5 47  LEU 47  47  47  LEU LEU H . n 
I 5 48  ILE 48  48  48  ILE ILE H . n 
I 5 49  TYR 49  49  49  TYR TYR H . n 
I 5 50  TYR 50  50  50  TYR TYR H . n 
I 5 51  ALA 51  51  51  ALA ALA H . n 
I 5 52  SER 52  52  52  SER SER H . n 
I 5 53  THR 53  53  53  THR THR H . n 
I 5 54  LEU 54  54  54  LEU LEU H . n 
I 5 55  GLN 55  55  55  GLN GLN H . n 
I 5 56  SER 56  56  56  SER SER H . n 
I 5 57  GLY 57  57  57  GLY GLY H . n 
I 5 58  VAL 58  58  58  VAL VAL H . n 
I 5 59  PRO 59  59  59  PRO PRO H . n 
I 5 60  SER 60  60  60  SER SER H . n 
I 5 61  ARG 61  61  61  ARG ARG H . n 
I 5 62  PHE 62  62  62  PHE PHE H . n 
I 5 63  SER 63  63  63  SER SER H . n 
I 5 64  ALA 64  64  64  ALA ALA H . n 
I 5 65  THR 65  65  65  THR THR H . n 
I 5 66  GLY 66  66  66  GLY GLY H . n 
I 5 67  SER 67  67  67  SER SER H . n 
I 5 68  GLY 68  68  68  GLY GLY H . n 
I 5 69  THR 69  69  69  THR THR H . n 
I 5 70  HIS 70  70  70  HIS HIS H . n 
I 5 71  PHE 71  71  71  PHE PHE H . n 
I 5 72  THR 72  72  72  THR THR H . n 
I 5 73  LEU 73  73  73  LEU LEU H . n 
I 5 74  THR 74  74  74  THR THR H . n 
I 5 75  VAL 75  75  75  VAL VAL H . n 
I 5 76  SER 76  76  76  SER SER H . n 
I 5 77  SER 77  77  77  SER SER H . n 
I 5 78  LEU 78  78  78  LEU LEU H . n 
I 5 79  GLN 79  79  79  GLN GLN H . n 
I 5 80  PRO 80  80  80  PRO PRO H . n 
I 5 81  GLU 81  81  81  GLU GLU H . n 
I 5 82  ASP 82  82  82  ASP ASP H . n 
I 5 83  PHE 83  83  83  PHE PHE H . n 
I 5 84  ALA 84  84  84  ALA ALA H . n 
I 5 85  THR 85  85  85  THR THR H . n 
I 5 86  TYR 86  86  86  TYR TYR H . n 
I 5 87  PHE 87  87  87  PHE PHE H . n 
I 5 88  CYS 88  88  88  CYS CYS H . n 
I 5 89  GLN 89  89  89  GLN GLN H . n 
I 5 90  HIS 90  90  90  HIS HIS H . n 
I 5 91  MET 91  91  91  MET MET H . n 
I 5 92  SER 92  92  92  SER SER H . n 
I 5 93  SER 93  93  93  SER SER H . n 
I 5 94  TYR 94  94  94  TYR TYR H . n 
I 5 95  PRO 95  95  95  PRO PRO H . n 
I 5 96  LEU 96  96  96  LEU LEU H . n 
I 5 97  THR 97  97  97  THR THR H . n 
I 5 98  PHE 98  98  98  PHE PHE H . n 
I 5 99  GLY 99  99  99  GLY GLY H . n 
I 5 100 GLY 100 100 100 GLY GLY H . n 
I 5 101 GLY 101 101 101 GLY GLY H . n 
I 5 102 THR 102 102 102 THR THR H . n 
I 5 103 LYS 103 103 103 LYS LYS H . n 
I 5 104 VAL 104 104 104 VAL VAL H . n 
I 5 105 GLU 105 105 105 GLU GLU H . n 
I 5 106 ILE 106 106 106 ILE ILE H . n 
I 5 107 LYS 107 107 107 LYS LYS H . n 
I 5 108 ARG 108 108 108 ARG ARG H . n 
I 5 109 THR 109 109 109 THR THR H . n 
I 5 110 VAL 110 110 110 VAL VAL H . n 
I 5 111 ALA 111 111 111 ALA ALA H . n 
I 5 112 ALA 112 112 112 ALA ALA H . n 
I 5 113 PRO 113 113 113 PRO PRO H . n 
I 5 114 SER 114 114 114 SER SER H . n 
I 5 115 VAL 115 115 115 VAL VAL H . n 
I 5 116 PHE 116 116 116 PHE PHE H . n 
I 5 117 ILE 117 117 117 ILE ILE H . n 
I 5 118 PHE 118 118 118 PHE PHE H . n 
I 5 119 PRO 119 119 119 PRO PRO H . n 
I 5 120 PRO 120 120 120 PRO PRO H . n 
I 5 121 SER 121 121 121 SER SER H . n 
I 5 122 ASP 122 122 122 ASP ASP H . n 
I 5 123 GLU 123 123 123 GLU GLU H . n 
I 5 124 GLN 124 124 124 GLN GLN H . n 
I 5 125 LEU 125 125 125 LEU LEU H . n 
I 5 126 LYS 126 126 126 LYS LYS H . n 
I 5 127 SER 127 127 127 SER SER H . n 
I 5 128 GLY 128 128 128 GLY GLY H . n 
I 5 129 THR 129 129 129 THR THR H . n 
I 5 130 ALA 130 130 130 ALA ALA H . n 
I 5 131 SER 131 131 131 SER SER H . n 
I 5 132 VAL 132 132 132 VAL VAL H . n 
I 5 133 VAL 133 133 133 VAL VAL H . n 
I 5 134 CYS 134 134 134 CYS CYS H . n 
I 5 135 LEU 135 135 135 LEU LEU H . n 
I 5 136 LEU 136 136 136 LEU LEU H . n 
I 5 137 ASN 137 137 137 ASN ASN H . n 
I 5 138 ASN 138 138 138 ASN ASN H . n 
I 5 139 PHE 139 139 139 PHE PHE H . n 
I 5 140 TYR 140 140 140 TYR TYR H . n 
I 5 141 PRO 141 141 141 PRO PRO H . n 
I 5 142 ARG 142 142 142 ARG ARG H . n 
I 5 143 GLU 143 143 143 GLU GLU H . n 
I 5 144 ALA 144 144 144 ALA ALA H . n 
I 5 145 LYS 145 145 145 LYS LYS H . n 
I 5 146 VAL 146 146 146 VAL VAL H . n 
I 5 147 GLN 147 147 147 GLN GLN H . n 
I 5 148 TRP 148 148 148 TRP TRP H . n 
I 5 149 LYS 149 149 149 LYS LYS H . n 
I 5 150 VAL 150 150 150 VAL VAL H . n 
I 5 151 ASP 151 151 151 ASP ASP H . n 
I 5 152 ASN 152 152 152 ASN ASN H . n 
I 5 153 ALA 153 153 153 ALA ALA H . n 
I 5 154 LEU 154 154 154 LEU LEU H . n 
I 5 155 GLN 155 155 155 GLN GLN H . n 
I 5 156 SER 156 156 156 SER SER H . n 
I 5 157 GLY 157 157 157 GLY GLY H . n 
I 5 158 ASN 158 158 158 ASN ASN H . n 
I 5 159 SER 159 159 159 SER SER H . n 
I 5 160 GLN 160 160 160 GLN GLN H . n 
I 5 161 GLU 161 161 161 GLU GLU H . n 
I 5 162 SER 162 162 162 SER SER H . n 
I 5 163 VAL 163 163 163 VAL VAL H . n 
I 5 164 THR 164 164 164 THR THR H . n 
I 5 165 GLU 165 165 165 GLU GLU H . n 
I 5 166 GLN 166 166 166 GLN GLN H . n 
I 5 167 ASP 167 167 167 ASP ASP H . n 
I 5 168 SER 168 168 168 SER SER H . n 
I 5 169 LYS 169 169 169 LYS LYS H . n 
I 5 170 ASP 170 170 170 ASP ASP H . n 
I 5 171 SER 171 171 171 SER SER H . n 
I 5 172 THR 172 172 172 THR THR H . n 
I 5 173 TYR 173 173 173 TYR TYR H . n 
I 5 174 SER 174 174 174 SER SER H . n 
I 5 175 LEU 175 175 175 LEU LEU H . n 
I 5 176 SER 176 176 176 SER SER H . n 
I 5 177 SER 177 177 177 SER SER H . n 
I 5 178 THR 178 178 178 THR THR H . n 
I 5 179 LEU 179 179 179 LEU LEU H . n 
I 5 180 THR 180 180 180 THR THR H . n 
I 5 181 LEU 181 181 181 LEU LEU H . n 
I 5 182 SER 182 182 182 SER SER H . n 
I 5 183 LYS 183 183 183 LYS LYS H . n 
I 5 184 ALA 184 184 184 ALA ALA H . n 
I 5 185 ASP 185 185 185 ASP ASP H . n 
I 5 186 TYR 186 186 186 TYR TYR H . n 
I 5 187 GLU 187 187 187 GLU GLU H . n 
I 5 188 LYS 188 188 188 LYS LYS H . n 
I 5 189 HIS 189 189 189 HIS HIS H . n 
I 5 190 LYS 190 190 190 LYS LYS H . n 
I 5 191 VAL 191 191 191 VAL VAL H . n 
I 5 192 TYR 192 192 192 TYR TYR H . n 
I 5 193 ALA 193 193 193 ALA ALA H . n 
I 5 194 CYS 194 194 194 CYS CYS H . n 
I 5 195 GLU 195 195 195 GLU GLU H . n 
I 5 196 VAL 196 196 196 VAL VAL H . n 
I 5 197 THR 197 197 197 THR THR H . n 
I 5 198 HIS 198 198 198 HIS HIS H . n 
I 5 199 GLN 199 199 199 GLN GLN H . n 
I 5 200 GLY 200 200 200 GLY GLY H . n 
I 5 201 LEU 201 201 201 LEU LEU H . n 
I 5 202 SER 202 202 202 SER SER H . n 
I 5 203 SER 203 203 203 SER SER H . n 
I 5 204 PRO 204 204 204 PRO PRO H . n 
I 5 205 VAL 205 205 205 VAL VAL H . n 
I 5 206 THR 206 206 206 THR THR H . n 
I 5 207 LYS 207 207 207 LYS LYS H . n 
I 5 208 SER 208 208 208 SER SER H . n 
I 5 209 PHE 209 209 209 PHE PHE H . n 
I 5 210 ASN 210 210 210 ASN ASN H . n 
I 5 211 ARG 211 211 211 ARG ARG H . n 
I 5 212 GLY 212 212 212 GLY GLY H . n 
J 6 1   GLN 1   1   1   GLN GLN I . n 
J 6 2   VAL 2   2   2   VAL VAL I . n 
J 6 3   HIS 3   3   3   HIS HIS I . n 
J 6 4   LEU 4   4   4   LEU LEU I . n 
J 6 5   GLN 5   5   5   GLN GLN I . n 
J 6 6   GLU 6   6   6   GLU GLU I . n 
J 6 7   SER 7   7   7   SER SER I . n 
J 6 8   GLY 8   8   8   GLY GLY I . n 
J 6 9   PRO 9   9   9   PRO PRO I . n 
J 6 10  GLY 10  10  10  GLY GLY I . n 
J 6 11  LEU 11  11  11  LEU LEU I . n 
J 6 12  VAL 12  12  12  VAL VAL I . n 
J 6 13  LYS 13  13  13  LYS LYS I . n 
J 6 14  PRO 14  14  14  PRO PRO I . n 
J 6 15  SER 15  15  15  SER SER I . n 
J 6 16  GLU 16  16  16  GLU GLU I . n 
J 6 17  THR 17  17  17  THR THR I . n 
J 6 18  LEU 18  18  18  LEU LEU I . n 
J 6 19  SER 19  19  19  SER SER I . n 
J 6 20  LEU 20  20  20  LEU LEU I . n 
J 6 21  THR 21  21  21  THR THR I . n 
J 6 22  CYS 22  22  22  CYS CYS I . n 
J 6 23  ASN 23  23  23  ASN ASN I . n 
J 6 24  VAL 24  24  24  VAL VAL I . n 
J 6 25  SER 25  25  25  SER SER I . n 
J 6 26  GLY 26  26  26  GLY GLY I . n 
J 6 27  THR 27  27  27  THR THR I . n 
J 6 28  LEU 28  28  28  LEU LEU I . n 
J 6 29  VAL 29  29  29  VAL VAL I . n 
J 6 30  ARG 30  30  30  ARG ARG I . n 
J 6 31  ASP 31  31  31  ASP ASP I . n 
J 6 32  ASN 32  32  32  ASN ASN I . n 
J 6 33  TYR 33  33  33  TYR TYR I . n 
J 6 34  TRP 34  34  34  TRP TRP I . n 
J 6 35  SER 35  35  35  SER SER I . n 
J 6 36  TRP 36  36  36  TRP TRP I . n 
J 6 37  ILE 37  37  37  ILE ILE I . n 
J 6 38  ARG 38  38  38  ARG ARG I . n 
J 6 39  GLN 39  39  39  GLN GLN I . n 
J 6 40  PRO 40  40  40  PRO PRO I . n 
J 6 41  LEU 41  41  41  LEU LEU I . n 
J 6 42  GLY 42  42  42  GLY GLY I . n 
J 6 43  LYS 43  43  43  LYS LYS I . n 
J 6 44  GLN 44  44  44  GLN GLN I . n 
J 6 45  PRO 45  45  45  PRO PRO I . n 
J 6 46  GLU 46  46  46  GLU GLU I . n 
J 6 47  TRP 47  47  47  TRP TRP I . n 
J 6 48  ILE 48  48  48  ILE ILE I . n 
J 6 49  GLY 49  49  49  GLY GLY I . n 
J 6 50  TYR 50  50  50  TYR TYR I . n 
J 6 51  VAL 51  51  51  VAL VAL I . n 
J 6 52  HIS 52  52  52  HIS HIS I . n 
J 6 53  ASP 53  53  53  ASP ASP I . n 
J 6 54  SER 54  54  54  SER SER I . n 
J 6 55  GLY 55  55  55  GLY GLY I . n 
J 6 56  ASP 56  56  56  ASP ASP I . n 
J 6 57  THR 57  57  57  THR THR I . n 
J 6 58  ASN 58  58  58  ASN ASN I . n 
J 6 59  TYR 59  59  59  TYR TYR I . n 
J 6 60  ASN 60  60  60  ASN ASN I . n 
J 6 61  PRO 61  61  61  PRO PRO I . n 
J 6 62  SER 62  62  62  SER SER I . n 
J 6 63  LEU 63  63  63  LEU LEU I . n 
J 6 64  LYS 64  64  64  LYS LYS I . n 
J 6 65  SER 65  65  65  SER SER I . n 
J 6 66  ARG 66  66  66  ARG ARG I . n 
J 6 67  VAL 67  67  67  VAL VAL I . n 
J 6 68  HIS 68  68  68  HIS HIS I . n 
J 6 69  LEU 69  69  69  LEU LEU I . n 
J 6 70  SER 70  70  70  SER SER I . n 
J 6 71  LEU 71  71  71  LEU LEU I . n 
J 6 72  ASP 72  72  72  ASP ASP I . n 
J 6 73  LYS 73  73  73  LYS LYS I . n 
J 6 74  SER 74  74  74  SER SER I . n 
J 6 75  LYS 75  75  75  LYS LYS I . n 
J 6 76  ASN 76  76  76  ASN ASN I . n 
J 6 77  LEU 77  77  77  LEU LEU I . n 
J 6 78  VAL 78  78  78  VAL VAL I . n 
J 6 79  SER 79  79  79  SER SER I . n 
J 6 80  LEU 80  80  80  LEU LEU I . n 
J 6 81  ARG 81  81  81  ARG ARG I . n 
J 6 82  LEU 82  82  82  LEU LEU I . n 
J 6 83  THR 83  82  82  THR THR I A n 
J 6 84  GLY 84  82  82  GLY GLY I B n 
J 6 85  VAL 85  82  82  VAL VAL I C n 
J 6 86  THR 86  83  83  THR THR I . n 
J 6 87  ALA 87  84  84  ALA ALA I . n 
J 6 88  ALA 88  85  85  ALA ALA I . n 
J 6 89  ASP 89  86  86  ASP ASP I . n 
J 6 90  SER 90  87  87  SER SER I . n 
J 6 91  ALA 91  88  88  ALA ALA I . n 
J 6 92  ILE 92  89  89  ILE ILE I . n 
J 6 93  TYR 93  90  90  TYR TYR I . n 
J 6 94  TYR 94  91  91  TYR TYR I . n 
J 6 95  CYS 95  92  92  CYS CYS I . n 
J 6 96  ALA 96  93  93  ALA ALA I . n 
J 6 97  THR 97  94  94  THR THR I . n 
J 6 98  THR 98  95  95  THR THR I . n 
J 6 99  LYS 99  96  96  LYS LYS I . n 
J 6 100 HIS 100 97  97  HIS HIS I . n 
J 6 101 GLY 101 98  98  GLY GLY I . n 
J 6 102 ARG 102 99  99  ARG ARG I . n 
J 6 103 ARG 103 100 100 ARG ARG I . n 
J 6 104 ILE 104 100 100 ILE ILE I A n 
J 6 105 TYR 105 100 100 TYR TYR I B n 
J 6 106 GLY 106 100 100 GLY GLY I C n 
J 6 107 VAL 107 100 100 VAL VAL I D n 
J 6 108 VAL 108 100 100 VAL VAL I E n 
J 6 109 ALA 109 100 100 ALA ALA I F n 
J 6 110 PHE 110 100 100 PHE PHE I G n 
J 6 111 LYS 111 100 100 LYS LYS I H n 
J 6 112 GLU 112 100 100 GLU GLU I I n 
J 6 113 TRP 113 100 100 TRP TRP I J n 
J 6 114 PHE 114 100 100 PHE PHE I K n 
J 6 115 THR 115 100 100 THR THR I L n 
J 6 116 TYR 116 100 100 TYR TYR I M n 
J 6 117 PHE 117 100 100 PHE PHE I N n 
J 6 118 TYR 118 100 100 TYR TYR I O n 
J 6 119 MET 119 100 100 MET MET I P n 
J 6 120 ASP 120 100 100 ASP ASP I Q n 
J 6 121 VAL 121 100 100 VAL VAL I R n 
J 6 122 TRP 122 101 101 TRP TRP I . n 
J 6 123 GLY 123 102 102 GLY GLY I . n 
J 6 124 LYS 124 103 103 LYS LYS I . n 
J 6 125 GLY 125 104 104 GLY GLY I . n 
J 6 126 THR 126 105 105 THR THR I . n 
J 6 127 SER 127 106 106 SER SER I . n 
J 6 128 VAL 128 107 107 VAL VAL I . n 
J 6 129 THR 129 108 108 THR THR I . n 
J 6 130 VAL 130 109 109 VAL VAL I . n 
J 6 131 SER 131 110 110 SER SER I . n 
J 6 132 SER 132 111 111 SER SER I . n 
J 6 133 ALA 133 112 112 ALA ALA I . n 
J 6 134 SER 134 113 113 SER SER I . n 
J 6 135 THR 135 114 114 THR THR I . n 
J 6 136 LYS 136 115 115 LYS LYS I . n 
J 6 137 GLY 137 116 116 GLY GLY I . n 
J 6 138 PRO 138 117 117 PRO PRO I . n 
J 6 139 SER 139 118 118 SER SER I . n 
J 6 140 VAL 140 119 119 VAL VAL I . n 
J 6 141 PHE 141 120 120 PHE PHE I . n 
J 6 142 PRO 142 121 121 PRO PRO I . n 
J 6 143 LEU 143 122 122 LEU LEU I . n 
J 6 144 ALA 144 123 123 ALA ALA I . n 
J 6 145 PRO 145 124 124 PRO PRO I . n 
J 6 146 SER 146 125 125 SER SER I . n 
J 6 147 SER 147 126 126 SER SER I . n 
J 6 148 LYS 148 127 ?   ?   ?   I . n 
J 6 149 SER 149 128 ?   ?   ?   I . n 
J 6 150 THR 150 129 ?   ?   ?   I . n 
J 6 151 SER 151 130 ?   ?   ?   I . n 
J 6 152 GLY 152 131 131 GLY GLY I . n 
J 6 153 GLY 153 132 132 GLY GLY I . n 
J 6 154 THR 154 133 133 THR THR I . n 
J 6 155 ALA 155 134 134 ALA ALA I . n 
J 6 156 ALA 156 135 135 ALA ALA I . n 
J 6 157 LEU 157 136 136 LEU LEU I . n 
J 6 158 GLY 158 137 137 GLY GLY I . n 
J 6 159 CYS 159 138 138 CYS CYS I . n 
J 6 160 LEU 160 139 139 LEU LEU I . n 
J 6 161 VAL 161 140 140 VAL VAL I . n 
J 6 162 LYS 162 141 141 LYS LYS I . n 
J 6 163 ASP 163 142 142 ASP ASP I . n 
J 6 164 TYR 164 143 143 TYR TYR I . n 
J 6 165 PHE 165 144 144 PHE PHE I . n 
J 6 166 PRO 166 145 145 PRO PRO I . n 
J 6 167 GLU 167 146 146 GLU GLU I . n 
J 6 168 PRO 168 147 147 PRO PRO I . n 
J 6 169 VAL 169 148 148 VAL VAL I . n 
J 6 170 THR 170 149 149 THR THR I . n 
J 6 171 VAL 171 150 150 VAL VAL I . n 
J 6 172 SER 172 151 151 SER SER I . n 
J 6 173 TRP 173 152 152 TRP TRP I . n 
J 6 174 ASN 174 153 153 ASN ASN I . n 
J 6 175 SER 175 154 154 SER SER I . n 
J 6 176 GLY 176 155 155 GLY GLY I . n 
J 6 177 ALA 177 156 156 ALA ALA I . n 
J 6 178 LEU 178 157 157 LEU LEU I . n 
J 6 179 THR 179 158 158 THR THR I . n 
J 6 180 SER 180 159 159 SER SER I . n 
J 6 181 GLY 181 160 160 GLY GLY I . n 
J 6 182 VAL 182 161 161 VAL VAL I . n 
J 6 183 HIS 183 162 162 HIS HIS I . n 
J 6 184 THR 184 163 163 THR THR I . n 
J 6 185 PHE 185 164 164 PHE PHE I . n 
J 6 186 PRO 186 165 165 PRO PRO I . n 
J 6 187 ALA 187 166 166 ALA ALA I . n 
J 6 188 VAL 188 167 167 VAL VAL I . n 
J 6 189 LEU 189 168 168 LEU LEU I . n 
J 6 190 GLN 190 169 169 GLN GLN I . n 
J 6 191 SER 191 170 170 SER SER I . n 
J 6 192 SER 192 171 171 SER SER I . n 
J 6 193 GLY 193 172 172 GLY GLY I . n 
J 6 194 LEU 194 173 173 LEU LEU I . n 
J 6 195 TYR 195 174 174 TYR TYR I . n 
J 6 196 SER 196 175 175 SER SER I . n 
J 6 197 LEU 197 176 176 LEU LEU I . n 
J 6 198 SER 198 177 177 SER SER I . n 
J 6 199 SER 199 178 178 SER SER I . n 
J 6 200 VAL 200 179 179 VAL VAL I . n 
J 6 201 VAL 201 180 180 VAL VAL I . n 
J 6 202 THR 202 181 181 THR THR I . n 
J 6 203 VAL 203 182 182 VAL VAL I . n 
J 6 204 PRO 204 183 183 PRO PRO I . n 
J 6 205 SER 205 184 184 SER SER I . n 
J 6 206 SER 206 185 185 SER SER I . n 
J 6 207 SER 207 186 186 SER SER I . n 
J 6 208 LEU 208 187 187 LEU LEU I . n 
J 6 209 GLY 209 188 188 GLY GLY I . n 
J 6 210 THR 210 189 189 THR THR I . n 
J 6 211 GLN 211 190 190 GLN GLN I . n 
J 6 212 THR 212 191 191 THR THR I . n 
J 6 213 TYR 213 192 192 TYR TYR I . n 
J 6 214 ILE 214 193 193 ILE ILE I . n 
J 6 215 CYS 215 194 194 CYS CYS I . n 
J 6 216 ASN 216 195 195 ASN ASN I . n 
J 6 217 VAL 217 196 196 VAL VAL I . n 
J 6 218 ASN 218 197 197 ASN ASN I . n 
J 6 219 HIS 219 198 198 HIS HIS I . n 
J 6 220 LYS 220 199 199 LYS LYS I . n 
J 6 221 PRO 221 200 200 PRO PRO I . n 
J 6 222 SER 222 201 201 SER SER I . n 
J 6 223 ASN 223 202 202 ASN ASN I . n 
J 6 224 THR 224 203 203 THR THR I . n 
J 6 225 LYS 225 204 204 LYS LYS I . n 
J 6 226 VAL 226 205 205 VAL VAL I . n 
J 6 227 ASP 227 206 206 ASP ASP I . n 
J 6 228 LYS 228 207 207 LYS LYS I . n 
J 6 229 ARG 229 208 208 ARG ARG I . n 
J 6 230 VAL 230 209 209 VAL VAL I . n 
J 6 231 GLU 231 210 210 GLU GLU I . n 
J 6 232 PRO 232 211 211 PRO PRO I . n 
J 6 233 LYS 233 212 ?   ?   ?   I . n 
J 6 234 SER 234 213 ?   ?   ?   I . n 
J 6 235 CYS 235 214 ?   ?   ?   I . n 
K 3 1   ALA 1   6   6   ALA ALA J . n 
K 3 2   PRO 2   7   7   PRO PRO J . n 
K 3 3   THR 3   8   8   THR THR J . n 
K 3 4   PHE 4   9   9   PHE PHE J . n 
K 3 5   VAL 5   11  11  VAL VAL J . n 
K 3 6   SER 6   12  12  SER SER J . n 
K 3 7   VAL 7   13  13  VAL VAL J . n 
K 3 8   ALA 8   14  14  ALA ALA J . n 
K 3 9   PRO 9   15  15  PRO PRO J . n 
K 3 10  GLY 10  16  16  GLY GLY J . n 
K 3 11  GLN 11  17  17  GLN GLN J . n 
K 3 12  THR 12  18  18  THR THR J . n 
K 3 13  ALA 13  19  19  ALA ALA J . n 
K 3 14  ARG 14  20  20  ARG ARG J . n 
K 3 15  ILE 15  21  21  ILE ILE J . n 
K 3 16  THR 16  22  22  THR THR J . n 
K 3 17  CYS 17  23  23  CYS CYS J . n 
K 3 18  GLY 18  24  24  GLY GLY J . n 
K 3 19  GLU 19  25  25  GLU GLU J . n 
K 3 20  GLU 20  26  26  GLU GLU J . n 
K 3 21  SER 21  27  27  SER SER J . n 
K 3 22  LEU 22  28  28  LEU LEU J . n 
K 3 23  GLY 23  29  29  GLY GLY J . n 
K 3 24  SER 24  30  30  SER SER J . n 
K 3 25  ARG 25  31  31  ARG ARG J . n 
K 3 26  SER 26  32  32  SER SER J . n 
K 3 27  VAL 27  33  33  VAL VAL J . n 
K 3 28  ILE 28  34  34  ILE ILE J . n 
K 3 29  TRP 29  35  35  TRP TRP J . n 
K 3 30  TYR 30  36  36  TYR TYR J . n 
K 3 31  GLN 31  37  37  GLN GLN J . n 
K 3 32  GLN 32  38  38  GLN GLN J . n 
K 3 33  ARG 33  39  39  ARG ARG J . n 
K 3 34  PRO 34  40  40  PRO PRO J . n 
K 3 35  GLY 35  41  41  GLY GLY J . n 
K 3 36  GLN 36  42  42  GLN GLN J . n 
K 3 37  ALA 37  43  43  ALA ALA J . n 
K 3 38  PRO 38  44  44  PRO PRO J . n 
K 3 39  SER 39  45  45  SER SER J . n 
K 3 40  LEU 40  46  46  LEU LEU J . n 
K 3 41  ILE 41  47  47  ILE ILE J . n 
K 3 42  ILE 42  48  48  ILE ILE J . n 
K 3 43  TYR 43  49  49  TYR TYR J . n 
K 3 44  ASN 44  50  50  ASN ASN J . n 
K 3 45  ASN 45  51  51  ASN ASN J . n 
K 3 46  ASN 46  52  52  ASN ASN J . n 
K 3 47  ASP 47  53  53  ASP ASP J . n 
K 3 48  ARG 48  54  54  ARG ARG J . n 
K 3 49  PRO 49  55  55  PRO PRO J . n 
K 3 50  SER 50  56  56  SER SER J . n 
K 3 51  GLY 51  57  57  GLY GLY J . n 
K 3 52  ILE 52  58  58  ILE ILE J . n 
K 3 53  PRO 53  59  59  PRO PRO J . n 
K 3 54  ASP 54  60  60  ASP ASP J . n 
K 3 55  ARG 55  61  61  ARG ARG J . n 
K 3 56  PHE 56  62  62  PHE PHE J . n 
K 3 57  SER 57  63  63  SER SER J . n 
K 3 58  GLY 58  64  64  GLY GLY J . n 
K 3 59  SER 59  65  65  SER SER J . n 
K 3 60  PRO 60  66  66  PRO PRO J . n 
K 3 61  GLY 61  67  67  GLY GLY J . n 
K 3 62  SER 62  67  67  SER SER J A n 
K 3 63  THR 63  67  67  THR THR J B n 
K 3 64  PHE 64  67  67  PHE PHE J C n 
K 3 65  GLY 65  68  68  GLY GLY J . n 
K 3 66  THR 66  69  69  THR THR J . n 
K 3 67  THR 67  70  70  THR THR J . n 
K 3 68  ALA 68  71  71  ALA ALA J . n 
K 3 69  THR 69  72  72  THR THR J . n 
K 3 70  LEU 70  73  73  LEU LEU J . n 
K 3 71  THR 71  74  74  THR THR J . n 
K 3 72  ILE 72  75  75  ILE ILE J . n 
K 3 73  THR 73  76  76  THR THR J . n 
K 3 74  SER 74  77  77  SER SER J . n 
K 3 75  VAL 75  78  78  VAL VAL J . n 
K 3 76  GLU 76  79  79  GLU GLU J . n 
K 3 77  ALA 77  80  80  ALA ALA J . n 
K 3 78  GLY 78  81  81  GLY GLY J . n 
K 3 79  ASP 79  82  82  ASP ASP J . n 
K 3 80  GLU 80  83  83  GLU GLU J . n 
K 3 81  ALA 81  84  84  ALA ALA J . n 
K 3 82  ASP 82  85  85  ASP ASP J . n 
K 3 83  TYR 83  86  86  TYR TYR J . n 
K 3 84  TYR 84  87  87  TYR TYR J . n 
K 3 85  CYS 85  88  88  CYS CYS J . n 
K 3 86  HIS 86  89  89  HIS HIS J . n 
K 3 87  ILE 87  90  90  ILE ILE J . n 
K 3 88  TRP 88  91  91  TRP TRP J . n 
K 3 89  ASP 89  92  92  ASP ASP J . n 
K 3 90  SER 90  93  93  SER SER J . n 
K 3 91  ARG 91  94  94  ARG ARG J . n 
K 3 92  ARG 92  95  95  ARG ARG J . n 
K 3 93  PRO 93  95  95  PRO PRO J A n 
K 3 94  THR 94  95  95  THR THR J B n 
K 3 95  ASN 95  95  95  ASN ASN J C n 
K 3 96  TRP 96  96  96  TRP TRP J . n 
K 3 97  VAL 97  97  97  VAL VAL J . n 
K 3 98  PHE 98  98  98  PHE PHE J . n 
K 3 99  GLY 99  99  99  GLY GLY J . n 
K 3 100 GLU 100 100 100 GLU GLU J . n 
K 3 101 GLY 101 101 101 GLY GLY J . n 
K 3 102 THR 102 102 102 THR THR J . n 
K 3 103 THR 103 103 103 THR THR J . n 
K 3 104 LEU 104 104 104 LEU LEU J . n 
K 3 105 ILE 105 105 105 ILE ILE J . n 
K 3 106 VAL 106 106 106 VAL VAL J . n 
K 3 107 LEU 107 107 107 LEU LEU J . n 
K 3 108 SER 108 108 108 SER SER J . n 
K 3 109 GLN 109 109 109 GLN GLN J . n 
K 3 110 PRO 110 110 110 PRO PRO J . n 
K 3 111 LYS 111 111 111 LYS LYS J . n 
K 3 112 ALA 112 112 112 ALA ALA J . n 
K 3 113 ALA 113 113 113 ALA ALA J . n 
K 3 114 PRO 114 114 114 PRO PRO J . n 
K 3 115 SER 115 115 115 SER SER J . n 
K 3 116 VAL 116 116 116 VAL VAL J . n 
K 3 117 THR 117 117 117 THR THR J . n 
K 3 118 LEU 118 118 118 LEU LEU J . n 
K 3 119 PHE 119 119 119 PHE PHE J . n 
K 3 120 PRO 120 120 120 PRO PRO J . n 
K 3 121 PRO 121 121 121 PRO PRO J . n 
K 3 122 SER 122 122 122 SER SER J . n 
K 3 123 SER 123 123 123 SER SER J . n 
K 3 124 GLU 124 124 124 GLU GLU J . n 
K 3 125 GLU 125 125 125 GLU GLU J . n 
K 3 126 LEU 126 126 126 LEU LEU J . n 
K 3 127 GLN 127 127 127 GLN GLN J . n 
K 3 128 ALA 128 128 128 ALA ALA J . n 
K 3 129 ASN 129 129 129 ASN ASN J . n 
K 3 130 LYS 130 130 130 LYS LYS J . n 
K 3 131 ALA 131 131 131 ALA ALA J . n 
K 3 132 THR 132 132 132 THR THR J . n 
K 3 133 LEU 133 133 133 LEU LEU J . n 
K 3 134 VAL 134 134 134 VAL VAL J . n 
K 3 135 CYS 135 135 135 CYS CYS J . n 
K 3 136 LEU 136 136 136 LEU LEU J . n 
K 3 137 ILE 137 137 137 ILE ILE J . n 
K 3 138 SER 138 138 138 SER SER J . n 
K 3 139 ASP 139 139 139 ASP ASP J . n 
K 3 140 PHE 140 140 140 PHE PHE J . n 
K 3 141 TYR 141 141 141 TYR TYR J . n 
K 3 142 PRO 142 142 142 PRO PRO J . n 
K 3 143 GLY 143 143 143 GLY GLY J . n 
K 3 144 ALA 144 144 144 ALA ALA J . n 
K 3 145 VAL 145 145 145 VAL VAL J . n 
K 3 146 THR 146 146 146 THR THR J . n 
K 3 147 VAL 147 147 147 VAL VAL J . n 
K 3 148 ALA 148 148 148 ALA ALA J . n 
K 3 149 TRP 149 149 149 TRP TRP J . n 
K 3 150 LYS 150 150 150 LYS LYS J . n 
K 3 151 ALA 151 151 151 ALA ALA J . n 
K 3 152 ASP 152 152 152 ASP ASP J . n 
K 3 153 SER 153 153 153 SER SER J . n 
K 3 154 SER 154 154 154 SER SER J . n 
K 3 155 PRO 155 155 155 PRO PRO J . n 
K 3 156 VAL 156 156 156 VAL VAL J . n 
K 3 157 LYS 157 157 157 LYS LYS J . n 
K 3 158 ALA 158 158 158 ALA ALA J . n 
K 3 159 GLY 159 159 159 GLY GLY J . n 
K 3 160 VAL 160 160 160 VAL VAL J . n 
K 3 161 GLU 161 161 161 GLU GLU J . n 
K 3 162 THR 162 162 162 THR THR J . n 
K 3 163 THR 163 163 163 THR THR J . n 
K 3 164 THR 164 164 164 THR THR J . n 
K 3 165 PRO 165 165 165 PRO PRO J . n 
K 3 166 SER 166 166 166 SER SER J . n 
K 3 167 LYS 167 167 167 LYS LYS J . n 
K 3 168 GLN 168 168 168 GLN GLN J . n 
K 3 169 SER 169 169 169 SER SER J . n 
K 3 170 ASN 170 170 170 ASN ASN J . n 
K 3 171 ASN 171 171 171 ASN ASN J . n 
K 3 172 LYS 172 172 172 LYS LYS J . n 
K 3 173 TYR 173 173 173 TYR TYR J . n 
K 3 174 ALA 174 174 174 ALA ALA J . n 
K 3 175 ALA 175 175 175 ALA ALA J . n 
K 3 176 SER 176 176 176 SER SER J . n 
K 3 177 SER 177 177 177 SER SER J . n 
K 3 178 TYR 178 178 178 TYR TYR J . n 
K 3 179 LEU 179 179 179 LEU LEU J . n 
K 3 180 SER 180 180 180 SER SER J . n 
K 3 181 LEU 181 181 181 LEU LEU J . n 
K 3 182 THR 182 182 182 THR THR J . n 
K 3 183 PRO 183 183 183 PRO PRO J . n 
K 3 184 GLU 184 184 184 GLU GLU J . n 
K 3 185 GLN 185 185 185 GLN GLN J . n 
K 3 186 TRP 186 186 186 TRP TRP J . n 
K 3 187 LYS 187 187 187 LYS LYS J . n 
K 3 188 SER 188 188 188 SER SER J . n 
K 3 189 HIS 189 189 189 HIS HIS J . n 
K 3 190 LYS 190 190 190 LYS LYS J . n 
K 3 191 SER 191 191 191 SER SER J . n 
K 3 192 TYR 192 192 192 TYR TYR J . n 
K 3 193 SER 193 193 193 SER SER J . n 
K 3 194 CYS 194 194 194 CYS CYS J . n 
K 3 195 GLN 195 195 195 GLN GLN J . n 
K 3 196 VAL 196 196 196 VAL VAL J . n 
K 3 197 THR 197 197 197 THR THR J . n 
K 3 198 HIS 198 198 198 HIS HIS J . n 
K 3 199 GLU 199 199 199 GLU GLU J . n 
K 3 200 GLY 200 200 200 GLY GLY J . n 
K 3 201 SER 201 201 201 SER SER J . n 
K 3 202 THR 202 202 202 THR THR J . n 
K 3 203 VAL 203 203 203 VAL VAL J . n 
K 3 204 GLU 204 204 204 GLU GLU J . n 
K 3 205 LYS 205 205 205 LYS LYS J . n 
K 3 206 THR 206 206 206 THR THR J . n 
K 3 207 VAL 207 207 207 VAL VAL J . n 
K 3 208 ALA 208 208 208 ALA ALA J . n 
K 3 209 PRO 209 209 209 PRO PRO J . n 
K 3 210 THR 210 210 210 THR THR J . n 
L 6 1   GLN 1   1   1   GLN GLN K . n 
L 6 2   VAL 2   2   2   VAL VAL K . n 
L 6 3   HIS 3   3   3   HIS HIS K . n 
L 6 4   LEU 4   4   4   LEU LEU K . n 
L 6 5   GLN 5   5   5   GLN GLN K . n 
L 6 6   GLU 6   6   6   GLU GLU K . n 
L 6 7   SER 7   7   7   SER SER K . n 
L 6 8   GLY 8   8   8   GLY GLY K . n 
L 6 9   PRO 9   9   9   PRO PRO K . n 
L 6 10  GLY 10  10  10  GLY GLY K . n 
L 6 11  LEU 11  11  11  LEU LEU K . n 
L 6 12  VAL 12  12  12  VAL VAL K . n 
L 6 13  LYS 13  13  13  LYS LYS K . n 
L 6 14  PRO 14  14  14  PRO PRO K . n 
L 6 15  SER 15  15  15  SER SER K . n 
L 6 16  GLU 16  16  16  GLU GLU K . n 
L 6 17  THR 17  17  17  THR THR K . n 
L 6 18  LEU 18  18  18  LEU LEU K . n 
L 6 19  SER 19  19  19  SER SER K . n 
L 6 20  LEU 20  20  20  LEU LEU K . n 
L 6 21  THR 21  21  21  THR THR K . n 
L 6 22  CYS 22  22  22  CYS CYS K . n 
L 6 23  ASN 23  23  23  ASN ASN K . n 
L 6 24  VAL 24  24  24  VAL VAL K . n 
L 6 25  SER 25  25  25  SER SER K . n 
L 6 26  GLY 26  26  26  GLY GLY K . n 
L 6 27  THR 27  27  27  THR THR K . n 
L 6 28  LEU 28  28  28  LEU LEU K . n 
L 6 29  VAL 29  29  29  VAL VAL K . n 
L 6 30  ARG 30  30  30  ARG ARG K . n 
L 6 31  ASP 31  31  31  ASP ASP K . n 
L 6 32  ASN 32  32  32  ASN ASN K . n 
L 6 33  TYR 33  33  33  TYR TYR K . n 
L 6 34  TRP 34  34  34  TRP TRP K . n 
L 6 35  SER 35  35  35  SER SER K . n 
L 6 36  TRP 36  36  36  TRP TRP K . n 
L 6 37  ILE 37  37  37  ILE ILE K . n 
L 6 38  ARG 38  38  38  ARG ARG K . n 
L 6 39  GLN 39  39  39  GLN GLN K . n 
L 6 40  PRO 40  40  40  PRO PRO K . n 
L 6 41  LEU 41  41  41  LEU LEU K . n 
L 6 42  GLY 42  42  42  GLY GLY K . n 
L 6 43  LYS 43  43  43  LYS LYS K . n 
L 6 44  GLN 44  44  44  GLN GLN K . n 
L 6 45  PRO 45  45  45  PRO PRO K . n 
L 6 46  GLU 46  46  46  GLU GLU K . n 
L 6 47  TRP 47  47  47  TRP TRP K . n 
L 6 48  ILE 48  48  48  ILE ILE K . n 
L 6 49  GLY 49  49  49  GLY GLY K . n 
L 6 50  TYR 50  50  50  TYR TYR K . n 
L 6 51  VAL 51  51  51  VAL VAL K . n 
L 6 52  HIS 52  52  52  HIS HIS K . n 
L 6 53  ASP 53  53  53  ASP ASP K . n 
L 6 54  SER 54  54  54  SER SER K . n 
L 6 55  GLY 55  55  55  GLY GLY K . n 
L 6 56  ASP 56  56  56  ASP ASP K . n 
L 6 57  THR 57  57  57  THR THR K . n 
L 6 58  ASN 58  58  58  ASN ASN K . n 
L 6 59  TYR 59  59  59  TYR TYR K . n 
L 6 60  ASN 60  60  60  ASN ASN K . n 
L 6 61  PRO 61  61  61  PRO PRO K . n 
L 6 62  SER 62  62  62  SER SER K . n 
L 6 63  LEU 63  63  63  LEU LEU K . n 
L 6 64  LYS 64  64  64  LYS LYS K . n 
L 6 65  SER 65  65  65  SER SER K . n 
L 6 66  ARG 66  66  66  ARG ARG K . n 
L 6 67  VAL 67  67  67  VAL VAL K . n 
L 6 68  HIS 68  68  68  HIS HIS K . n 
L 6 69  LEU 69  69  69  LEU LEU K . n 
L 6 70  SER 70  70  70  SER SER K . n 
L 6 71  LEU 71  71  71  LEU LEU K . n 
L 6 72  ASP 72  72  72  ASP ASP K . n 
L 6 73  LYS 73  73  73  LYS LYS K . n 
L 6 74  SER 74  74  74  SER SER K . n 
L 6 75  LYS 75  75  75  LYS LYS K . n 
L 6 76  ASN 76  76  76  ASN ASN K . n 
L 6 77  LEU 77  77  77  LEU LEU K . n 
L 6 78  VAL 78  78  78  VAL VAL K . n 
L 6 79  SER 79  79  79  SER SER K . n 
L 6 80  LEU 80  80  80  LEU LEU K . n 
L 6 81  ARG 81  81  81  ARG ARG K . n 
L 6 82  LEU 82  82  82  LEU LEU K . n 
L 6 83  THR 83  82  82  THR THR K A n 
L 6 84  GLY 84  82  82  GLY GLY K B n 
L 6 85  VAL 85  82  82  VAL VAL K C n 
L 6 86  THR 86  83  83  THR THR K . n 
L 6 87  ALA 87  84  84  ALA ALA K . n 
L 6 88  ALA 88  85  85  ALA ALA K . n 
L 6 89  ASP 89  86  86  ASP ASP K . n 
L 6 90  SER 90  87  87  SER SER K . n 
L 6 91  ALA 91  88  88  ALA ALA K . n 
L 6 92  ILE 92  89  89  ILE ILE K . n 
L 6 93  TYR 93  90  90  TYR TYR K . n 
L 6 94  TYR 94  91  91  TYR TYR K . n 
L 6 95  CYS 95  92  92  CYS CYS K . n 
L 6 96  ALA 96  93  93  ALA ALA K . n 
L 6 97  THR 97  94  94  THR THR K . n 
L 6 98  THR 98  95  95  THR THR K . n 
L 6 99  LYS 99  96  96  LYS LYS K . n 
L 6 100 HIS 100 97  97  HIS HIS K . n 
L 6 101 GLY 101 98  98  GLY GLY K . n 
L 6 102 ARG 102 99  99  ARG ARG K . n 
L 6 103 ARG 103 100 100 ARG ARG K . n 
L 6 104 ILE 104 100 100 ILE ILE K A n 
L 6 105 TYR 105 100 100 TYR TYR K B n 
L 6 106 GLY 106 100 100 GLY GLY K C n 
L 6 107 VAL 107 100 100 VAL VAL K D n 
L 6 108 VAL 108 100 100 VAL VAL K E n 
L 6 109 ALA 109 100 100 ALA ALA K F n 
L 6 110 PHE 110 100 100 PHE PHE K G n 
L 6 111 LYS 111 100 100 LYS LYS K H n 
L 6 112 GLU 112 100 100 GLU GLU K I n 
L 6 113 TRP 113 100 100 TRP TRP K J n 
L 6 114 PHE 114 100 100 PHE PHE K K n 
L 6 115 THR 115 100 100 THR THR K L n 
L 6 116 TYR 116 100 100 TYR TYR K M n 
L 6 117 PHE 117 100 100 PHE PHE K N n 
L 6 118 TYR 118 100 100 TYR TYR K O n 
L 6 119 MET 119 100 100 MET MET K P n 
L 6 120 ASP 120 100 100 ASP ASP K Q n 
L 6 121 VAL 121 100 100 VAL VAL K R n 
L 6 122 TRP 122 101 101 TRP TRP K . n 
L 6 123 GLY 123 102 102 GLY GLY K . n 
L 6 124 LYS 124 103 103 LYS LYS K . n 
L 6 125 GLY 125 104 104 GLY GLY K . n 
L 6 126 THR 126 105 105 THR THR K . n 
L 6 127 SER 127 106 106 SER SER K . n 
L 6 128 VAL 128 107 107 VAL VAL K . n 
L 6 129 THR 129 108 108 THR THR K . n 
L 6 130 VAL 130 109 109 VAL VAL K . n 
L 6 131 SER 131 110 110 SER SER K . n 
L 6 132 SER 132 111 111 SER SER K . n 
L 6 133 ALA 133 112 112 ALA ALA K . n 
L 6 134 SER 134 113 113 SER SER K . n 
L 6 135 THR 135 114 114 THR THR K . n 
L 6 136 LYS 136 115 115 LYS LYS K . n 
L 6 137 GLY 137 116 116 GLY GLY K . n 
L 6 138 PRO 138 117 117 PRO PRO K . n 
L 6 139 SER 139 118 118 SER SER K . n 
L 6 140 VAL 140 119 119 VAL VAL K . n 
L 6 141 PHE 141 120 120 PHE PHE K . n 
L 6 142 PRO 142 121 121 PRO PRO K . n 
L 6 143 LEU 143 122 122 LEU LEU K . n 
L 6 144 ALA 144 123 123 ALA ALA K . n 
L 6 145 PRO 145 124 124 PRO PRO K . n 
L 6 146 SER 146 125 125 SER SER K . n 
L 6 147 SER 147 126 126 SER SER K . n 
L 6 148 LYS 148 127 ?   ?   ?   K . n 
L 6 149 SER 149 128 ?   ?   ?   K . n 
L 6 150 THR 150 129 ?   ?   ?   K . n 
L 6 151 SER 151 130 ?   ?   ?   K . n 
L 6 152 GLY 152 131 131 GLY GLY K . n 
L 6 153 GLY 153 132 132 GLY GLY K . n 
L 6 154 THR 154 133 133 THR THR K . n 
L 6 155 ALA 155 134 134 ALA ALA K . n 
L 6 156 ALA 156 135 135 ALA ALA K . n 
L 6 157 LEU 157 136 136 LEU LEU K . n 
L 6 158 GLY 158 137 137 GLY GLY K . n 
L 6 159 CYS 159 138 138 CYS CYS K . n 
L 6 160 LEU 160 139 139 LEU LEU K . n 
L 6 161 VAL 161 140 140 VAL VAL K . n 
L 6 162 LYS 162 141 141 LYS LYS K . n 
L 6 163 ASP 163 142 142 ASP ASP K . n 
L 6 164 TYR 164 143 143 TYR TYR K . n 
L 6 165 PHE 165 144 144 PHE PHE K . n 
L 6 166 PRO 166 145 145 PRO PRO K . n 
L 6 167 GLU 167 146 146 GLU GLU K . n 
L 6 168 PRO 168 147 147 PRO PRO K . n 
L 6 169 VAL 169 148 148 VAL VAL K . n 
L 6 170 THR 170 149 149 THR THR K . n 
L 6 171 VAL 171 150 150 VAL VAL K . n 
L 6 172 SER 172 151 151 SER SER K . n 
L 6 173 TRP 173 152 152 TRP TRP K . n 
L 6 174 ASN 174 153 153 ASN ASN K . n 
L 6 175 SER 175 154 154 SER SER K . n 
L 6 176 GLY 176 155 155 GLY GLY K . n 
L 6 177 ALA 177 156 156 ALA ALA K . n 
L 6 178 LEU 178 157 157 LEU LEU K . n 
L 6 179 THR 179 158 158 THR THR K . n 
L 6 180 SER 180 159 159 SER SER K . n 
L 6 181 GLY 181 160 160 GLY GLY K . n 
L 6 182 VAL 182 161 161 VAL VAL K . n 
L 6 183 HIS 183 162 162 HIS HIS K . n 
L 6 184 THR 184 163 163 THR THR K . n 
L 6 185 PHE 185 164 164 PHE PHE K . n 
L 6 186 PRO 186 165 165 PRO PRO K . n 
L 6 187 ALA 187 166 166 ALA ALA K . n 
L 6 188 VAL 188 167 167 VAL VAL K . n 
L 6 189 LEU 189 168 168 LEU LEU K . n 
L 6 190 GLN 190 169 169 GLN GLN K . n 
L 6 191 SER 191 170 170 SER SER K . n 
L 6 192 SER 192 171 171 SER SER K . n 
L 6 193 GLY 193 172 172 GLY GLY K . n 
L 6 194 LEU 194 173 173 LEU LEU K . n 
L 6 195 TYR 195 174 174 TYR TYR K . n 
L 6 196 SER 196 175 175 SER SER K . n 
L 6 197 LEU 197 176 176 LEU LEU K . n 
L 6 198 SER 198 177 177 SER SER K . n 
L 6 199 SER 199 178 178 SER SER K . n 
L 6 200 VAL 200 179 179 VAL VAL K . n 
L 6 201 VAL 201 180 180 VAL VAL K . n 
L 6 202 THR 202 181 181 THR THR K . n 
L 6 203 VAL 203 182 182 VAL VAL K . n 
L 6 204 PRO 204 183 183 PRO PRO K . n 
L 6 205 SER 205 184 184 SER SER K . n 
L 6 206 SER 206 185 185 SER SER K . n 
L 6 207 SER 207 186 186 SER SER K . n 
L 6 208 LEU 208 187 187 LEU LEU K . n 
L 6 209 GLY 209 188 188 GLY GLY K . n 
L 6 210 THR 210 189 189 THR THR K . n 
L 6 211 GLN 211 190 190 GLN GLN K . n 
L 6 212 THR 212 191 191 THR THR K . n 
L 6 213 TYR 213 192 192 TYR TYR K . n 
L 6 214 ILE 214 193 193 ILE ILE K . n 
L 6 215 CYS 215 194 194 CYS CYS K . n 
L 6 216 ASN 216 195 195 ASN ASN K . n 
L 6 217 VAL 217 196 196 VAL VAL K . n 
L 6 218 ASN 218 197 197 ASN ASN K . n 
L 6 219 HIS 219 198 198 HIS HIS K . n 
L 6 220 LYS 220 199 199 LYS LYS K . n 
L 6 221 PRO 221 200 200 PRO PRO K . n 
L 6 222 SER 222 201 201 SER SER K . n 
L 6 223 ASN 223 202 202 ASN ASN K . n 
L 6 224 THR 224 203 203 THR THR K . n 
L 6 225 LYS 225 204 204 LYS LYS K . n 
L 6 226 VAL 226 205 205 VAL VAL K . n 
L 6 227 ASP 227 206 206 ASP ASP K . n 
L 6 228 LYS 228 207 207 LYS LYS K . n 
L 6 229 ARG 229 208 208 ARG ARG K . n 
L 6 230 VAL 230 209 209 VAL VAL K . n 
L 6 231 GLU 231 210 210 GLU GLU K . n 
L 6 232 PRO 232 211 211 PRO PRO K . n 
L 6 233 LYS 233 212 ?   ?   ?   K . n 
L 6 234 SER 234 213 ?   ?   ?   K . n 
L 6 235 CYS 235 214 ?   ?   ?   K . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
M  7 NAG 1  901 1088 NAG NAG A . 
N  7 NAG 2  902 1089 NAG NAG A . 
O  8 BMA 3  903 1090 BMA BMA A . 
P  9 MAN 4  904 1091 MAN MAN A . 
Q  9 MAN 5  905 1092 MAN MAN A . 
R  9 MAN 6  906 1093 MAN MAN A . 
S  9 MAN 7  907 1094 MAN MAN A . 
T  7 NAG 1  908 1133 NAG NAG A . 
U  7 NAG 1  909 1156 NAG NAG A . 
V  7 NAG 2  910 1157 NAG NAG A . 
W  8 BMA 3  911 1158 BMA BMA A . 
X  9 MAN 4  912 1159 MAN MAN A . 
Y  9 MAN 5  913 1169 MAN MAN A . 
Z  7 NAG 1  914 1160 NAG NAG A . 
AA 7 NAG 2  915 1161 NAG NAG A . 
BA 7 NAG 1  916 1197 NAG NAG A . 
CA 7 NAG 2  917 1198 NAG NAG A . 
DA 7 NAG 1  918 1234 NAG NAG A . 
EA 7 NAG 2  919 1235 NAG NAG A . 
FA 7 NAG 1  920 1262 NAG NAG A . 
GA 7 NAG 2  921 1263 NAG NAG A . 
HA 8 BMA 3  922 1264 BMA BMA A . 
IA 9 MAN 4  923 1265 MAN MAN A . 
JA 9 MAN 5  924 1268 MAN MAN A . 
KA 9 MAN 6  925 1269 MAN MAN A . 
LA 7 NAG 1  926 1276 NAG NAG A . 
MA 7 NAG 1  927 1295 NAG NAG A . 
NA 7 NAG 2  928 1296 NAG NAG A . 
OA 8 BMA 3  929 1297 BMA BMA A . 
PA 7 NAG 1  930 1301 NAG NAG A . 
QA 7 NAG 2  931 1302 NAG NAG A . 
RA 7 NAG 1  932 1331 NAG NAG A . 
SA 7 NAG 2  933 1332 NAG NAG A . 
TA 8 BMA 3  934 1333 BMA BMA A . 
UA 9 MAN 4  935 1334 MAN MAN A . 
VA 9 MAN 5  936 1335 MAN MAN A . 
WA 9 MAN 6  937 1336 MAN MAN A . 
XA 9 MAN 7  938 1337 MAN MAN A . 
YA 9 MAN 8  939 1338 MAN MAN A . 
ZA 9 MAN 9  940 1339 MAN MAN A . 
AB 9 MAN 10 941 1340 MAN MAN A . 
BB 7 NAG 1  942 1355 NAG NAG A . 
CB 7 NAG 1  943 1363 NAG NAG A . 
DB 7 NAG 2  944 1364 NAG NAG A . 
EB 7 NAG 1  945 1386 NAG NAG A . 
FB 7 NAG 2  946 1387 NAG NAG A . 
GB 7 NAG 1  947 1392 NAG NAG A . 
HB 7 NAG 2  948 1393 NAG NAG A . 
IB 7 NAG 1  949 1448 NAG NAG A . 
JB 7 NAG 2  950 1449 NAG NAG A . 
KB 8 BMA 3  951 1450 BMA BMA A . 
LB 7 NAG 1  952 1839 NAG NAG A . 
MB 7 NAG 1  901 1611 NAG NAG B . 
NB 7 NAG 1  902 1618 NAG NAG B . 
OB 7 NAG 1  903 1637 NAG NAG B . 
PB 7 NAG 1  901 1088 NAG NAG C . 
QB 7 NAG 2  902 1089 NAG NAG C . 
RB 8 BMA 3  903 1090 BMA BMA C . 
SB 9 MAN 4  904 1091 MAN MAN C . 
TB 9 MAN 5  905 1092 MAN MAN C . 
UB 9 MAN 6  906 1093 MAN MAN C . 
VB 9 MAN 7  907 1094 MAN MAN C . 
WB 7 NAG 1  908 1133 NAG NAG C . 
XB 7 NAG 1  909 1137 NAG NAG C . 
YB 7 NAG 1  910 1156 NAG NAG C . 
ZB 7 NAG 2  911 1157 NAG NAG C . 
AC 8 BMA 3  912 1158 BMA BMA C . 
BC 9 MAN 4  913 1159 MAN MAN C . 
CC 9 MAN 5  914 1169 MAN MAN C . 
DC 7 NAG 1  915 1160 NAG NAG C . 
EC 7 NAG 2  916 1161 NAG NAG C . 
FC 7 NAG 1  917 1197 NAG NAG C . 
GC 7 NAG 2  918 1198 NAG NAG C . 
HC 7 NAG 1  919 1234 NAG NAG C . 
IC 7 NAG 2  920 1235 NAG NAG C . 
JC 7 NAG 1  921 1262 NAG NAG C . 
KC 7 NAG 2  922 1263 NAG NAG C . 
LC 8 BMA 3  923 1264 BMA BMA C . 
MC 9 MAN 4  924 1265 MAN MAN C . 
NC 9 MAN 5  925 1268 MAN MAN C . 
OC 9 MAN 6  926 1269 MAN MAN C . 
PC 7 NAG 1  927 1276 NAG NAG C . 
QC 7 NAG 1  928 1295 NAG NAG C . 
RC 7 NAG 2  929 1296 NAG NAG C . 
SC 7 NAG 1  930 1301 NAG NAG C . 
TC 7 NAG 2  931 1302 NAG NAG C . 
UC 7 NAG 1  932 1331 NAG NAG C . 
VC 7 NAG 2  933 1332 NAG NAG C . 
WC 8 BMA 3  934 1333 BMA BMA C . 
XC 9 MAN 4  935 1334 MAN MAN C . 
YC 9 MAN 5  936 1335 MAN MAN C . 
ZC 9 MAN 6  937 1336 MAN MAN C . 
AD 9 MAN 7  938 1337 MAN MAN C . 
BD 9 MAN 8  939 1338 MAN MAN C . 
CD 9 MAN 9  940 1339 MAN MAN C . 
DD 9 MAN 10 941 1340 MAN MAN C . 
ED 7 NAG 1  942 1355 NAG NAG C . 
FD 7 NAG 1  943 1363 NAG NAG C . 
GD 7 NAG 2  944 1364 NAG NAG C . 
HD 7 NAG 1  945 1386 NAG NAG C . 
ID 7 NAG 2  946 1387 NAG NAG C . 
JD 7 NAG 1  947 1392 NAG NAG C . 
KD 7 NAG 2  948 1393 NAG NAG C . 
LD 8 BMA 3  949 1394 BMA BMA C . 
MD 7 NAG 1  950 1448 NAG NAG C . 
ND 7 NAG 2  951 1449 NAG NAG C . 
OD 8 BMA 3  952 1450 BMA BMA C . 
PD 7 NAG 1  953 1839 NAG NAG C . 
QD 7 NAG 1  901 1611 NAG NAG D . 
RD 7 NAG 1  902 1637 NAG NAG D . 
SD 7 NAG 1  301 1137 NAG NAG I . 
TD 7 NAG 2  302 1138 NAG NAG I . 
UD 8 BMA 3  303 1139 BMA BMA I . 
VD 9 MAN 4  304 1140 MAN MAN I . 
WD 7 NAG 1  305 523  NAG NAG I . 
XD 7 NAG 1  301 523  NAG NAG K . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? octadecameric 18 
2 author_defined_assembly ? octadecameric 18 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1,2,4 
;A,B,E,F,J,K,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA,MA,NA,OA,PA,QA,RA,SA,TA,UA,VA,WA,XA,YA,ZA,AB,BB,CB,DB,EB,FB,GB,HB,IB,JB,KB,LB,MB,NB,OB,SD,TD,UD,VD,WD
;
2 1,3,5 
;C,D,G,H,I,L,PB,QB,RB,SB,TB,UB,VB,WB,XB,YB,ZB,AC,BC,CC,DC,EC,FC,GC,HC,IC,JC,KC,LC,MC,NC,OC,PC,QC,RC,SC,TC,UC,VC,WC,XC,YC,ZC,AD,BD,CD,DD,ED,FD,GD,HD,ID,JD,KD,LD,MD,ND,OD,PD,QD,RD,XD
;
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z         1.0000000000  0.0000000000  0.0000000000 0.0000000000   0.0000000000  
1.0000000000  0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_555 -y,x-y,z      -0.5000000000 -0.8660254038 0.0000000000 0.0000000000   0.8660254038  
-0.5000000000 0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000 0.0000000000 
3 'crystal symmetry operation' 2_655 -y+1,x-y,z    -0.5000000000 -0.8660254038 0.0000000000 252.2960000000 0.8660254038  
-0.5000000000 0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000 0.0000000000 
4 'crystal symmetry operation' 3_555 -x+y,-x,z     -0.5000000000 0.8660254038  0.0000000000 0.0000000000   -0.8660254038 
-0.5000000000 0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000 0.0000000000 
5 'crystal symmetry operation' 3_665 -x+y+1,-x+1,z -0.5000000000 0.8660254038  0.0000000000 126.1480000000 -0.8660254038 
-0.5000000000 0.0000000000 218.4947452732 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
# 
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 2016-05-25 
2 'Structure model' 1 1 2016-06-01 
3 'Structure model' 1 2 2017-09-20 
# 
_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         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Derived calculations'       
2 3 'Structure model' 'Author supporting evidence' 
3 3 'Structure model' 'Derived calculations'       
# 
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 3 'Structure model' pdbx_audit_support    
2 3 'Structure model' pdbx_struct_oper_list 
# 
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 3 'Structure model' '_pdbx_audit_support.funding_organization'  
2 3 'Structure model' '_pdbx_struct_oper_list.symmetry_operation' 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1  ? refined 9.1765   17.5424 175.5241 1.3588 0.7561 1.2942 -0.0213 -0.0195 0.0823  1.4590 1.2205 1.5166  
0.8303  -0.6492 0.5971  -0.9617 1.1664  0.0539  -0.5094 0.2383  0.7124  -0.1293 0.4316  -0.6765 
'X-RAY DIFFRACTION' 2  ? refined 12.4120  16.9977 209.8937 1.1398 0.9251 1.4382 0.0588  -0.0205 0.0337  1.9886 1.0079 1.3786  
0.5026  0.8205  1.2018  0.0239  -0.5773 -0.0005 -0.6708 0.1932  -0.4454 0.0593  0.0733  0.1648  
'X-RAY DIFFRACTION' 3  ? refined 14.3695  30.9310 192.8374 1.9478 0.4495 1.2340 -0.1569 -0.0475 -0.0725 0.3577 1.4506 1.3577  
1.0868  -0.3826 0.5652  0.1117  0.2602  0.0270  -1.3709 -0.1800 0.4027  0.2505  -1.4442 0.1078  
'X-RAY DIFFRACTION' 4  ? refined 19.6829  22.1830 151.7039 1.5706 0.9617 2.0796 -1.0469 -0.8452 -0.4377 0.4434 0.3425 0.2290  
0.2110  -0.2544 -0.1575 -0.2135 0.1023  0.3505  0.3615  0.1317  0.1478  -0.1849 -0.1919 -0.0084 
'X-RAY DIFFRACTION' 5  ? refined 9.1080   19.0878 154.2002 0.9647 0.6457 1.4792 0.5308  -0.2657 -0.2038 0.2014 1.8452 2.0644  
0.6226  -0.0821 0.0753  0.8174  0.2817  0.4683  -0.1771 -1.1563 -0.0456 -0.2710 -0.8010 0.4160  
'X-RAY DIFFRACTION' 6  ? refined 6.9790   5.9893  179.2107 1.7997 0.4333 1.6579 -0.9459 -0.0518 -1.0193 0.3606 0.8977 0.1068  
-0.1424 0.1187  -0.2935 -0.0978 0.0974  -0.2167 -0.1063 0.3057  -0.3944 -0.2132 -0.1409 -0.0379 
'X-RAY DIFFRACTION' 7  ? refined -1.6298  6.7392  164.5561 1.1898 0.3490 1.3394 -0.5615 0.2125  0.0057  5.0469 0.2179 0.2384  
-0.0136 -1.0566 0.0430  -0.3016 0.1177  -0.3220 1.0107  0.3288  0.4646  1.0370  -0.1710 -0.2320 
'X-RAY DIFFRACTION' 8  ? refined -4.7746  12.7405 146.5430 2.1617 1.4364 1.8052 -0.5209 0.4474  0.9349  0.1259 1.3907 0.9048  
0.4199  0.3316  1.1179  -1.0023 0.1760  -0.6776 0.2484  -1.0473 -0.5795 -0.7109 -0.3538 0.8613  
'X-RAY DIFFRACTION' 9  ? refined -7.2796  29.9378 145.5735 1.7527 1.3816 2.7531 0.4235  -0.3315 -0.0010 0.0536 0.0324 0.0613  
-0.0410 0.0462  -0.0209 -0.4846 0.0437  -0.0012 0.3158  0.2928  0.8298  0.8428  -0.2645 -0.4233 
'X-RAY DIFFRACTION' 10 ? refined -1.7093  28.0003 153.4910 2.2882 1.2913 1.6244 1.5509  -0.3020 0.2892  0.5256 1.1566 0.4198  
-0.7831 -0.4732 0.6968  0.3005  0.3260  1.5985  0.0031  0.0853  -0.1039 -0.3390 -0.2191 -0.2366 
'X-RAY DIFFRACTION' 11 ? refined -13.7082 15.5960 151.8569 1.7329 2.9638 2.1322 0.8271  1.3060  1.5987  0.5246 1.1621 1.0984  
-0.6687 -0.2186 0.8323  -0.1991 -0.0381 0.0435  -0.5107 -0.7354 0.5927  0.7042  0.3082  -0.5521 
'X-RAY DIFFRACTION' 12 ? refined -15.0470 -0.2212 139.7060 2.4432 1.9174 2.7469 -0.5460 0.0541  1.1738  1.1625 0.9575 0.9952  
-0.8954 -1.0042 0.9528  0.6654  1.0721  0.2936  -0.4537 0.1014  -0.3645 -0.5308 0.2221  -0.4999 
'X-RAY DIFFRACTION' 13 ? refined 104.8691 72.2717 258.3064 1.6461 1.2434 1.3752 0.1331  -0.0795 -0.1672 0.2313 0.2167 2.5382  
0.6379  0.9476  1.8228  -0.4748 0.3511  0.0749  0.0633  0.0323  0.1738  0.0727  -0.2578 -0.3286 
'X-RAY DIFFRACTION' 14 ? refined 91.5871  76.0849 256.2911 1.1896 0.9890 1.2761 0.4894  -0.2299 -0.2421 1.2789 0.1073 2.6684  
-0.2155 0.2704  -0.7074 -0.3085 0.1271  -0.0074 0.3209  -0.2210 -0.3635 -0.2337 -0.7363 0.0372  
'X-RAY DIFFRACTION' 15 ? refined 85.4519  34.9837 217.1914 2.7052 2.1688 2.6264 0.4506  0.0469  -0.2348 0.0735 0.0148 0.1866  
-0.0296 -0.0420 0.0093  0.8338  -1.0869 0.0000  0.7351  -0.3647 -0.2112 0.9138  0.9094  -1.1520 
'X-RAY DIFFRACTION' 16 ? refined 77.2593  41.7161 219.8098 2.2026 2.2263 1.7164 -0.5258 0.1984  -0.3169 0.2399 0.3273 0.1444  
-0.2584 0.1303  -0.2315 -0.4125 1.4548  0.0002  0.8733  -0.5549 -1.2415 0.1197  0.6841  -0.0410 
'X-RAY DIFFRACTION' 17 ? refined 78.6434  31.3582 194.4003 1.1338 2.6463 2.2778 0.3905  -0.1409 -0.7887 0.0385 1.0841 0.3386  
0.2915  0.1135  0.5205  0.7386  0.4810  0.0274  1.0656  -0.7561 -0.7579 0.4087  -0.2626 0.0586  
'X-RAY DIFFRACTION' 18 ? refined 77.8318  20.8333 178.4362 1.5899 3.4851 2.2741 -0.0959 -0.0432 -1.0529 0.0182 0.1069 0.0750  
-0.0752 0.0668  -0.1015 0.4490  -1.4112 -0.0087 0.5992  -0.9012 -1.4614 0.6283  0.4061  0.1729  
'X-RAY DIFFRACTION' 19 ? refined 36.7385  28.3363 154.7600 1.0741 0.9587 0.8401 -2.1013 -0.3856 -0.3167 1.0867 2.7595 1.1098  
-0.0723 0.2524  -0.5153 0.3792  0.8839  1.0929  0.1454  -0.0776 0.7445  0.0980  -0.1933 0.4522  
'X-RAY DIFFRACTION' 20 ? refined 56.8079  51.6864 173.1813 3.0189 1.5554 1.2806 -1.2266 -0.2502 -1.0417 0.5978 0.3406 0.5579  
-0.2056 0.1469  0.0835  -0.3852 -0.1130 0.1191  1.3617  -0.1012 0.9638  0.3765  -1.7749 0.2577  
'X-RAY DIFFRACTION' 21 ? refined 31.9834  48.7384 143.4935 3.5738 1.3112 0.9290 -0.7372 0.1571  0.1003  0.9250 1.2071 0.0544  
-0.1839 0.0386  0.2075  -0.2964 0.2843  0.0630  0.6753  0.3220  -0.5740 0.0088  -0.7059 -0.0264 
'X-RAY DIFFRACTION' 22 ? refined 36.2232  50.2680 153.4181 2.5928 2.0870 0.6870 -1.2862 0.1120  0.3567  1.7247 3.8034 0.2824  
-0.7752 -0.5310 0.5500  -0.6026 0.0236  -1.5609 -0.1344 0.2349  1.5005  -1.6421 -1.7699 0.3498  
'X-RAY DIFFRACTION' 23 ? refined 60.7307  60.9057 159.1909 4.4183 2.7426 2.3924 -1.8416 -0.6815 0.4302  2.2361 1.0156 3.2008  
-0.4680 -2.6024 0.8709  -0.9038 0.9984  0.0820  1.9829  -0.3951 -1.3428 -0.1938 1.6746  -1.9033 
'X-RAY DIFFRACTION' 24 ? refined 83.8207  54.3500 295.8594 0.3161 2.5914 1.3934 -0.0739 -0.2438 -0.0566 0.7723 3.9194 0.1527  
-0.0551 0.0017  0.3040  0.4981  -0.2483 -0.2436 -0.3570 -0.8955 -0.5283 -0.7325 0.2836  -0.6556 
'X-RAY DIFFRACTION' 25 ? refined 53.6010  48.0733 277.5068 1.9635 2.5381 1.8740 0.0066  -0.6326 0.0833  0.3664 0.9783 0.4006  
0.5671  0.1567  0.4760  0.5433  -1.1131 -0.0001 -0.1359 0.0129  0.3739  -0.2103 0.1501  -0.5542 
'X-RAY DIFFRACTION' 26 ? refined 97.3791  66.4418 298.9690 1.3862 1.7997 1.9014 1.3320  -1.1655 -0.0644 0.0661 0.0443 0.1586  
-0.0422 -0.0884 0.0780  0.5468  0.6092  2.1719  -0.1505 -0.7660 0.5801  -0.2154 0.3739  -0.2929 
'X-RAY DIFFRACTION' 27 ? refined 105.1801 74.3556 296.6287 0.7219 1.1801 1.7224 1.1239  0.0856  -0.2538 1.4437 0.0022 2.2883  
-0.0014 1.8200  0.0040  -0.2864 -0.4485 -1.2809 -0.2846 0.3407  -0.1548 0.3186  -0.2394 -0.5870 
'X-RAY DIFFRACTION' 28 ? refined 117.3739 69.9270 271.3935 0.6754 2.1494 1.4190 0.7186  -0.0377 0.1575  0.3307 0.9081 0.5603  
0.4799  0.3369  0.2701  -0.1241 0.1111  -0.1776 -0.8485 0.3012  0.6693  -0.0029 -0.2061 0.2054  
'X-RAY DIFFRACTION' 29 ? refined 118.3077 82.2980 294.9184 1.2390 0.6881 1.1345 0.0268  0.6223  0.0039  0.7645 0.6735 1.2007  
-0.5806 0.9214  -0.7079 -0.7675 -0.4979 -0.4232 0.8398  0.5916  -0.3229 0.8512  -1.1581 0.2463  
'X-RAY DIFFRACTION' 30 ? refined 100.3619 91.0886 306.8661 2.1668 2.0775 3.2193 0.1976  -0.0561 -1.6437 0.1568 0.0435 0.1578  
-0.0533 -0.1599 0.0540  0.2708  -0.0805 0.3294  0.2433  -0.2085 0.4905  0.0008  -0.0892 -0.1640 
'X-RAY DIFFRACTION' 31 ? refined 102.7532 88.1511 297.3953 1.7570 2.4434 2.1270 0.2726  -0.6040 -1.0120 0.6077 2.0920 1.1456  
-0.7723 0.7642  -0.5073 0.0806  1.6280  0.1552  -1.2108 0.0640  0.8972  -0.1805 -0.9679 -0.7583 
'X-RAY DIFFRACTION' 32 ? refined 119.3676 92.4677 298.9632 1.7819 0.5022 1.9426 0.1358  1.2337  -0.2126 0.1850 0.2428 -0.0041 
-0.2057 0.0047  -0.0043 0.1244  0.1476  -0.0649 0.1867  0.1530  -0.6140 -0.3969 -0.2512 0.2222  
'X-RAY DIFFRACTION' 33 ? refined 133.9458 85.9461 311.0011 3.5902 0.9798 2.1786 0.0827  1.3609  0.1858  0.9033 0.2263 0.2774  
0.1194  0.4969  0.0887  0.2343  0.4445  0.8262  -0.3023 -0.4125 0.3911  0.0102  -0.1793 -0.1783 
'X-RAY DIFFRACTION' 34 ? refined 62.6982  67.8026 305.6541 1.7028 3.3666 2.4046 0.7647  0.0640  0.0253  0.2596 0.3558 0.2928  
0.3020  0.2372  0.2815  0.4648  -1.4372 -0.0544 -0.4670 -0.8701 -0.1347 0.1042  0.7021  -1.6797 
'X-RAY DIFFRACTION' 35 ? refined 72.5861  68.4955 308.7630 1.3666 2.3262 0.5008 0.6869  0.3410  -0.4320 2.9072 1.4019 0.2744  
2.0048  -0.9011 -0.6175 -0.2827 -0.6283 -0.7186 -1.4848 -0.4107 -0.0652 -0.7364 0.2418  -0.0053 
'X-RAY DIFFRACTION' 36 ? refined 74.9063  72.6661 297.3233 0.5277 2.3888 1.3467 0.7678  -0.0857 -0.3469 0.1661 0.0907 -0.0039 
-0.1170 -0.0158 0.0079  0.5486  -0.5125 -0.5756 0.8485  0.1285  -0.2616 -0.3984 0.2695  0.3630  
'X-RAY DIFFRACTION' 37 ? refined 70.6677  69.3938 304.2881 1.6484 2.8653 1.4132 1.7341  0.1937  -0.5694 0.6073 0.7155 1.0121  
0.0061  -0.4728 -0.0773 -0.3504 -0.7531 -1.7172 -0.1082 -0.7415 0.7167  -0.8351 -0.4797 -0.2426 
'X-RAY DIFFRACTION' 38 ? refined 49.8196  68.0201 294.3482 2.5917 3.7341 2.5588 0.5133  -1.3215 -0.5416 0.0602 0.0491 0.0873  
-0.0292 -0.0616 -0.0106 -0.5120 -0.4604 0.0011  -0.3160 -0.4277 -0.0397 0.3705  -0.3152 0.3364  
'X-RAY DIFFRACTION' 39 ? refined 44.8231  47.7158 287.9251 2.0855 4.5873 1.8852 -0.4351 0.2574  0.3264  0.2851 0.2309 0.0723  
-0.0139 -0.0426 -0.1251 -0.1466 0.3779  -0.0014 0.2852  -0.2672 0.1637  1.0921  0.0545  -1.7734 
'X-RAY DIFFRACTION' 40 ? refined 49.1417  53.4417 292.1957 0.9966 3.8277 1.6762 0.9770  -0.3288 0.9661  0.9316 0.4864 0.4226  
-0.4974 0.0031  0.3024  -0.0258 0.3685  0.6826  -0.8446 0.6324  -0.2741 0.4601  0.1369  -0.5846 
'X-RAY DIFFRACTION' 41 ? refined 39.4838  44.2544 290.7866 1.2287 3.9662 2.3183 -1.5927 0.0361  0.0924  0.3850 0.2837 0.7377  
-0.2054 0.3741  -0.4591 0.0856  -0.8345 -0.3200 -1.0915 -0.4745 -0.3305 0.7220  -0.4016 0.3377  
'X-RAY DIFFRACTION' 42 ? refined 43.0635  40.0234 245.9912 2.8051 2.0401 2.0394 -0.6051 -0.4040 -0.0193 0.5601 0.2679 0.0449  
-0.2160 -0.0159 0.0988  -0.1640 -1.0084 0.0008  -0.3403 0.3732  -1.3518 0.4022  -1.3442 -0.9044 
'X-RAY DIFFRACTION' 43 ? refined 35.5924  39.7931 248.5024 1.9519 2.6868 1.8181 -0.3189 -0.4975 -0.3937 0.0587 0.0673 0.1124  
0.0377  -0.0066 0.0660  0.6106  0.5185  -0.0007 -0.6002 -0.8220 -0.1499 0.4696  0.1295  -0.8067 
'X-RAY DIFFRACTION' 44 ? refined 49.7005  34.0954 245.6412 0.4230 2.2357 2.3677 -0.3859 -0.8124 0.3715  0.1789 1.7972 0.9296  
0.3546  0.4831  0.5094  -0.3507 0.0914  -0.1378 -0.2473 -0.4207 0.5938  -0.7209 1.6932  -0.9644 
'X-RAY DIFFRACTION' 45 ? refined 65.2707  34.2699 263.3984 1.7926 3.3302 2.7636 -0.4145 -0.0313 -0.3797 0.1772 0.5342 0.5182  
0.2649  0.2840  0.2277  2.7486  -2.5171 0.0037  -0.2312 0.2240  -0.4845 2.2068  1.0367  0.0664  
'X-RAY DIFFRACTION' 46 ? refined 51.4194  22.6026 232.5063 1.2202 2.7445 2.0270 0.0097  -0.4950 -0.2547 0.3780 0.1032 0.0431  
-0.1869 0.1211  -0.0657 0.0681  -0.2540 0.0001  0.0730  -0.1385 -0.1763 -0.6654 0.2029  -0.0421 
'X-RAY DIFFRACTION' 47 ? refined 68.4997  17.6587 267.2367 3.2714 3.1361 2.6444 -0.4551 -0.9942 0.1897  0.1635 0.4040 0.1677  
-0.2633 0.1194  -0.2497 1.4211  0.5781  0.0317  -0.9681 -0.3756 -1.0258 2.4368  0.2925  -1.5356 
'X-RAY DIFFRACTION' 48 ? refined 70.6588  59.1217 203.6285 0.7277 3.4579 1.9545 -2.7704 -0.5805 -1.2340 0.2019 0.9912 1.2892  
0.4345  0.4956  0.9701  -0.5525 -0.2469 -1.2198 0.7796  -0.3173 0.1506  -0.0715 -0.6063 -0.5913 
'X-RAY DIFFRACTION' 49 ? refined 71.3393  47.9558 204.7792 1.8532 2.4975 1.8157 -0.5718 0.2510  -0.3148 0.8017 1.3357 0.1130  
-1.1699 -0.2807 0.6144  -1.2574 1.3680  0.1002  0.6042  -0.2838 0.5631  0.3143  -0.1400 2.2672  
'X-RAY DIFFRACTION' 50 ? refined 63.4555  34.7103 186.8987 3.2202 2.1724 2.8633 -1.6351 0.0162  0.5167  0.5556 0.1065 0.0034  
-0.2346 0.0526  -0.0337 0.1657  0.5057  0.0112  2.0745  0.3423  1.1971  1.0479  -1.7021 0.9818  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1  1  A 31  A 117 
;chain 'A' and (resid 31 through 117 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 2  2  A 118 A 235 
;chain 'A' and (resid 118 through 235 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 3  3  A 236 A 507 
;chain 'A' and (resid 236 through 507 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 4  4  B 512 B 523 
;chain 'B' and (resid 512 through 523 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 5  5  B 524 B 544 
;chain 'B' and (resid 524 through 544 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 6  6  B 545 B 575 
;chain 'B' and (resid 545 through 575 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 7  7  B 576 B 595 
;chain 'B' and (resid 576 through 595 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 8  8  B 596 B 610 
;chain 'B' and (resid 596 through 610 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 9  9  B 611 B 622 
;chain 'B' and (resid 611 through 622 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 10 10 B 623 B 637 
;chain 'B' and (resid 623 through 637 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 11 11 B 638 B 650 
;chain 'B' and (resid 638 through 650 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 12 12 B 651 B 664 
;chain 'B' and (resid 651 through 664 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 13 13 C 31  C 258 
;chain 'C' and (resid 31 through 258 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 14 14 C 259 C 505 
;chain 'C' and (resid 259 through 505 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 15 15 L 6   L 26  
;chain 'L' and (resid 6 through 26 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 16 16 L 27  L 89  
;chain 'L' and (resid 27 through 89 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 17 17 L 90  L 174 
;chain 'L' and (resid 90 through 174 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 18 18 L 175 L 210 
;chain 'L' and (resid 175 through 210 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 19 19 E 1   E 111 
;chain 'E' and (resid 1 through 111 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 20 20 E 112 E 214 
;chain 'E' and (resid 112 through 214 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 21 21 F 1   F 38  
;chain 'F' and (resid 1 through 38 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 22 22 F 39  F 128 
;chain 'F' and (resid 39 through 128 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 23 23 F 129 F 212 
;chain 'F' and (resid 129 through 212 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 24 24 G 1   G 111 
;chain 'G' and (resid 1 through 111 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 25 25 G 112 G 214 
;chain 'G' and (resid 112 through 214 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 26 26 D 512 D 523 
;chain 'D' and (resid 512 through 523 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 27 27 D 524 D 544 
;chain 'D' and (resid 524 through 544 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 28 28 D 545 D 575 
;chain 'D' and (resid 545 through 575 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 29 29 D 576 D 615 
;chain 'D' and (resid 576 through 615 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 30 30 D 616 D 622 
;chain 'D' and (resid 616 through 622 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 31 31 D 623 D 637 
;chain 'D' and (resid 623 through 637 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 32 32 D 638 D 650 
;chain 'D' and (resid 638 through 650 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 33 33 D 651 D 664 
;chain 'D' and (resid 651 through 664 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 34 34 H 1   H 18  
;chain 'H' and (resid 1 through 18 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 35 35 H 19  H 38  
;chain 'H' and (resid 19 through 38 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 36 36 H 39  H 61  
;chain 'H' and (resid 39 through 61 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 37 37 H 62  H 102 
;chain 'H' and (resid 62 through 102 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 38 38 H 103 H 113 
;chain 'H' and (resid 103 through 113 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 39 39 H 114 H 150 
;chain 'H' and (resid 114 through 150 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 40 40 H 151 H 174 
;chain 'H' and (resid 151 through 174 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 41 41 H 175 H 212 
;chain 'H' and (resid 175 through 212 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 42 42 I 1   I 56  
;chain 'I' and (resid 1 through 56 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 43 43 I 57  I 87  
;chain 'I' and (resid 57 through 87 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 44 44 I 88  I 141 
;chain 'I' and (resid 88 through 141 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 45 45 I 142 I 211 
;chain 'I' and (resid 142 through 211 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 46 46 J 6   J 114 
;chain 'J' and (resid 6 through 114 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 47 47 J 115 J 210 
;chain 'J' and (resid 115 through 210 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 48 48 K 1   K 87  
;chain 'K' and (resid 1 through 87 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 49 49 K 88  K 141 
;chain 'K' and (resid 88 through 141 )
;
? ? ? ? ? 
'X-RAY DIFFRACTION' 50 50 K 142 K 211 
;chain 'K' and (resid 142 through 211 )
;
? ? ? ? ? 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? .    1 
? 'data collection' ? ? ? ? ? ? ? ? ? ? ? HKL-2000    ? ? ? .    2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? HKL-2000    ? ? ? .    3 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.20 4 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? HKL-2000    ? ? ? .    5 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .    6 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 NH2 I ARG 99  ? ? O4  I MAN 304 ? ? 2.03 
2  1 NH2 A ARG 350 ? ? O   A ILE 396 ? ? 2.04 
3  1 NH2 C ARG 350 ? ? O   C ILE 396 ? ? 2.09 
4  1 O4  C NAG 902 ? ? C2  C BMA 903 ? ? 2.15 
5  1 O   D LEU 645 ? ? OG  D SER 649 ? ? 2.17 
6  1 O   J GLU 184 ? ? OG  J SER 188 ? ? 2.18 
7  1 NE  J ARG 54  ? ? O   J ILE 58  ? ? 2.18 
8  1 O   A ALA 219 ? ? NE2 A GLN 246 ? ? 2.19 
9  1 NZ  C LYS 155 ? ? OH  C TYR 191 ? ? 2.19 
10 1 ND1 A HIS 249 ? ? OH  A TYR 486 ? ? 2.19 
11 1 C6  A MAN 905 ? ? C1  A MAN 906 ? ? 2.19 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CD L ARG 54 ? ? NE  L ARG 54 ? ? 1.340 1.460 -0.120 0.017 N 
2 1 NE L ARG 54 ? ? CZ  L ARG 54 ? ? 1.208 1.326 -0.118 0.013 N 
3 1 CZ L ARG 54 ? ? NH1 L ARG 54 ? ? 1.181 1.326 -0.145 0.013 N 
4 1 CZ L ARG 54 ? ? NH2 L ARG 54 ? ? 1.234 1.326 -0.092 0.013 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CG1 A ILE 138 ? ? CB A ILE 138 ? ? CG2 A ILE 138 ? ? 91.35  111.40 -20.05 2.20 N 
2 1 CA  A ARG 166 ? ? CB A ARG 166 ? ? CG  A ARG 166 ? ? 126.66 113.40 13.26  2.20 N 
3 1 CA  A LYS 490 ? ? CB A LYS 490 ? ? CG  A LYS 490 ? ? 127.77 113.40 14.37  2.20 N 
4 1 CG1 C ILE 138 ? ? CB C ILE 138 ? ? CG2 C ILE 138 ? ? 93.68  111.40 -17.72 2.20 N 
5 1 CA  I LEU 176 ? ? CB I LEU 176 ? ? CG  I LEU 176 ? ? 136.48 115.30 21.18  2.30 N 
6 1 CA  K LEU 176 ? ? CB K LEU 176 ? ? CG  K LEU 176 ? ? 134.65 115.30 19.35  2.30 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1   1 PRO A 43  ? ? -68.86  75.55   
2   1 SER A 56  ? ? -152.91 62.54   
3   1 ASP A 57  ? ? 52.83   -160.07 
4   1 GLU A 64  ? ? 36.71   -112.63 
5   1 ASN A 67  ? ? 58.73   89.00   
6   1 TRP A 69  ? ? 57.80   -100.79 
7   1 THR A 71  ? ? -54.26  89.32   
8   1 HIS A 72  ? ? -123.04 -63.15  
9   1 LEU A 122 ? ? -95.03  42.31   
10  1 PRO A 124 ? ? -91.68  44.36   
11  1 ILE A 138 ? ? 47.33   -168.37 
12  1 ARG A 151 ? ? 34.02   38.67   
13  1 GLU A 153 ? ? 63.17   -56.03  
14  1 ASP A 167 ? ? -120.75 -93.72  
15  1 LYS A 169 ? ? -83.92  -158.96 
16  1 PHE A 210 ? ? -98.28  35.52   
17  1 GLN A 258 ? ? 57.93   -59.69  
18  1 GLU A 268 ? ? 55.65   -113.10 
19  1 SER A 306 ? ? -104.47 76.04   
20  1 ASN A 356 ? ? -107.68 74.88   
21  1 THR A 387 ? ? -103.27 44.08   
22  1 ASN A 392 ? ? -119.48 72.12   
23  1 ASP A 412 ? ? -152.69 -143.57 
24  1 THR A 464 ? ? -101.31 -86.13  
25  1 ARG A 504 ? ? -94.32  -159.64 
26  1 VAL A 505 ? ? -151.96 14.34   
27  1 ALA B 525 ? ? -87.04  48.17   
28  1 SER B 546 ? ? 53.62   78.04   
29  1 TRP B 571 ? ? 66.07   -23.46  
30  1 CYS B 598 ? ? -131.95 -76.91  
31  1 SER B 599 ? ? 61.35   -63.89  
32  1 LYS B 601 ? ? -71.60  -159.10 
33  1 LEU B 602 ? ? 60.60   -84.00  
34  1 ASN B 607 ? ? -96.73  54.44   
35  1 SER B 615 ? ? 56.83   85.51   
36  1 ASN B 616 ? ? -67.18  95.26   
37  1 ASN B 625 ? ? -161.51 21.15   
38  1 GLN B 650 ? ? -95.93  -92.02  
39  1 PRO C 43  ? ? -68.99  75.49   
40  1 SER C 56  ? ? -152.58 62.65   
41  1 ASP C 57  ? ? 52.92   -159.91 
42  1 GLU C 64  ? ? 34.90   -111.33 
43  1 ASN C 67  ? ? 58.62   88.43   
44  1 TRP C 69  ? ? 58.04   -100.14 
45  1 THR C 71  ? ? -54.42  88.67   
46  1 HIS C 72  ? ? -123.29 -64.13  
47  1 LEU C 122 ? ? -94.80  42.60   
48  1 PRO C 124 ? ? -91.24  44.25   
49  1 ILE C 138 ? ? 47.30   -168.72 
50  1 ARG C 151 ? ? 34.87   37.80   
51  1 GLU C 153 ? ? 63.22   -55.95  
52  1 ASP C 167 ? ? -118.76 -93.51  
53  1 LYS C 169 ? ? -85.76  -157.11 
54  1 PHE C 210 ? ? -98.15  35.04   
55  1 GLN C 258 ? ? 58.18   -60.61  
56  1 GLU C 268 ? ? 54.84   -111.92 
57  1 SER C 306 ? ? -104.07 76.24   
58  1 ASN C 356 ? ? -108.07 75.10   
59  1 THR C 387 ? ? -103.22 44.75   
60  1 ASN C 392 ? ? -119.31 72.86   
61  1 ASP C 412 ? ? -153.14 -144.67 
62  1 THR C 464 ? ? -101.64 -86.43  
63  1 ARG C 503 ? ? -79.76  -162.84 
64  1 GLN L 17  ? ? -87.61  -152.17 
65  1 ASN L 51  ? ? 62.72   -58.36  
66  1 ASN L 52  ? ? -146.09 36.47   
67  1 ASP L 152 ? ? 58.54   -100.59 
68  1 ASN L 170 ? ? -167.33 -169.41 
69  1 SER L 188 ? ? -74.31  -76.02  
70  1 GLU L 199 ? ? 55.85   -92.97  
71  1 VAL E 100 C ? -127.74 -50.10  
72  1 ASP E 144 ? ? 61.90   61.40   
73  1 ARG F 30  ? ? 58.15   -133.02 
74  1 ALA F 51  ? ? 65.46   -29.84  
75  1 ALA F 84  ? ? -172.23 -177.25 
76  1 LYS F 190 ? ? -108.36 -61.01  
77  1 ASP G 144 ? ? 61.86   60.80   
78  1 THR G 160 ? ? -131.44 -40.70  
79  1 ALA D 525 ? ? -86.58  48.33   
80  1 SER D 546 ? ? 53.63   78.12   
81  1 TRP D 571 ? ? 66.60   -22.75  
82  1 CYS D 598 ? ? -131.85 -77.90  
83  1 SER D 599 ? ? 60.46   -64.25  
84  1 LYS D 601 ? ? -70.66  -159.66 
85  1 LEU D 602 ? ? 60.40   -84.55  
86  1 ASN D 607 ? ? -94.74  54.35   
87  1 SER D 615 ? ? 57.28   85.91   
88  1 ASN D 616 ? ? -66.85  95.06   
89  1 ASN D 625 ? ? -161.18 22.59   
90  1 GLN D 650 ? ? -95.73  -90.66  
91  1 ARG H 30  ? ? 59.22   -134.48 
92  1 ALA H 51  ? ? 66.92   -28.93  
93  1 ALA H 84  ? ? -172.80 -173.17 
94  1 LYS H 169 ? ? -91.27  -60.04  
95  1 VAL I 100 E ? 60.04   -57.35  
96  1 ASP I 142 ? ? 55.32   89.92   
97  1 PRO I 145 ? ? -102.02 -167.38 
98  1 PRO I 147 ? ? -108.75 -169.13 
99  1 GLN J 17  ? ? -87.78  -152.90 
100 1 ASN J 51  ? ? 62.56   -58.66  
101 1 ASN J 52  ? ? -146.61 37.73   
102 1 ASP J 152 ? ? 59.22   -101.16 
103 1 ASN J 170 ? ? -168.20 -167.89 
104 1 SER J 188 ? ? -73.31  -74.65  
105 1 GLU J 199 ? ? 55.55   -93.20  
106 1 VAL K 100 E ? 60.23   -57.05  
107 1 ASP K 142 ? ? 54.67   90.21   
108 1 PRO K 145 ? ? -101.66 -167.10 
109 1 PRO K 147 ? ? -109.01 -169.25 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             ASP 
_pdbx_validate_main_chain_plane.auth_asym_id             E 
_pdbx_validate_main_chain_plane.auth_seq_id              208 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   10.35 
# 
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 N 1 A NAG 920 ? O1 ? FA NAG 1 O1 
2 1 N 1 A NAG 943 ? O1 ? CB NAG 1 O1 
# 
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 GLU 185 A A GLU 148 
2   1 Y 1 A ASN 185 B A ASN 149 
3   1 Y 1 A GLN 185 C A GLN 150 
4   1 Y 1 A GLY 185 D A GLY 151 
5   1 Y 1 A ASN 185 E A ASN 152 
6   1 Y 1 A ARG 185 F A ARG 153 
7   1 Y 1 A SER 185 G A SER 154 
8   1 Y 1 A ASN 185 H A ASN 155 
9   1 Y 1 A ASN 185 I A ASN 156 
10  1 Y 1 A THR 400 ? A THR 368 
11  1 Y 1 A SER 401 ? A SER 369 
12  1 Y 1 A VAL 402 ? A VAL 370 
13  1 Y 1 A GLN 403 ? A GLN 371 
14  1 Y 1 A GLY 404 ? A GLY 372 
15  1 Y 1 A SER 405 ? A SER 373 
16  1 Y 1 A ASN 406 ? A ASN 374 
17  1 Y 1 A SER 407 ? A SER 375 
18  1 Y 1 A THR 408 ? A THR 376 
19  1 Y 1 A GLY 409 ? A GLY 377 
20  1 Y 1 A SER 410 ? A SER 378 
21  1 Y 1 A ARG 508 ? A ARG 476 
22  1 Y 1 A ARG 509 ? A ARG 477 
23  1 Y 1 A ARG 510 ? A ARG 478 
24  1 Y 1 A ARG 511 ? A ARG 479 
25  1 Y 1 A ARG 512 ? A ARG 480 
26  1 Y 1 A ARG 513 ? A ARG 481 
27  1 Y 1 B ILE 548 ? B ILE 37  
28  1 Y 1 B VAL 549 ? B VAL 38  
29  1 Y 1 B GLN 550 ? B GLN 39  
30  1 Y 1 B GLN 551 ? B GLN 40  
31  1 Y 1 B GLN 552 ? B GLN 41  
32  1 Y 1 B SER 553 ? B SER 42  
33  1 Y 1 B ASN 554 ? B ASN 43  
34  1 Y 1 B LEU 555 ? B LEU 44  
35  1 Y 1 B LEU 556 ? B LEU 45  
36  1 Y 1 B ARG 557 ? B ARG 46  
37  1 Y 1 B ALA 558 ? B ALA 47  
38  1 Y 1 B ILE 559 ? B ILE 48  
39  1 Y 1 B GLU 560 ? B GLU 49  
40  1 Y 1 B ALA 561 ? B ALA 50  
41  1 Y 1 B GLN 562 ? B GLN 51  
42  1 Y 1 B GLN 563 ? B GLN 52  
43  1 Y 1 B HIS 564 ? B HIS 53  
44  1 Y 1 B LEU 565 ? B LEU 54  
45  1 Y 1 B LEU 566 ? B LEU 55  
46  1 Y 1 B LYS 567 ? B LYS 56  
47  1 Y 1 B LEU 568 ? B LEU 57  
48  1 Y 1 C GLU 185 A C GLU 148 
49  1 Y 1 C ASN 185 B C ASN 149 
50  1 Y 1 C GLN 185 C C GLN 150 
51  1 Y 1 C GLY 185 D C GLY 151 
52  1 Y 1 C ASN 185 E C ASN 152 
53  1 Y 1 C ARG 185 F C ARG 153 
54  1 Y 1 C SER 185 G C SER 154 
55  1 Y 1 C ASN 185 H C ASN 155 
56  1 Y 1 C ASN 185 I C ASN 156 
57  1 Y 1 C SER 185 J C SER 157 
58  1 Y 1 C ASN 185 K C ASN 158 
59  1 Y 1 C LYS 185 L C LYS 159 
60  1 Y 1 C THR 400 ? C THR 368 
61  1 Y 1 C SER 401 ? C SER 369 
62  1 Y 1 C VAL 402 ? C VAL 370 
63  1 Y 1 C GLN 403 ? C GLN 371 
64  1 Y 1 C GLY 404 ? C GLY 372 
65  1 Y 1 C SER 405 ? C SER 373 
66  1 Y 1 C ASN 406 ? C ASN 374 
67  1 Y 1 C SER 407 ? C SER 375 
68  1 Y 1 C THR 408 ? C THR 376 
69  1 Y 1 C GLY 409 ? C GLY 377 
70  1 Y 1 C SER 410 ? C SER 378 
71  1 Y 1 C VAL 506 ? C VAL 474 
72  1 Y 1 C GLY 507 ? C GLY 475 
73  1 Y 1 C ARG 508 ? C ARG 476 
74  1 Y 1 C ARG 509 ? C ARG 477 
75  1 Y 1 C ARG 510 ? C ARG 478 
76  1 Y 1 C ARG 511 ? C ARG 479 
77  1 Y 1 C ARG 512 ? C ARG 480 
78  1 Y 1 C ARG 513 ? C ARG 481 
79  1 Y 1 D ILE 548 ? H ILE 37  
80  1 Y 1 D VAL 549 ? H VAL 38  
81  1 Y 1 D GLN 550 ? H GLN 39  
82  1 Y 1 D GLN 551 ? H GLN 40  
83  1 Y 1 D GLN 552 ? H GLN 41  
84  1 Y 1 D SER 553 ? H SER 42  
85  1 Y 1 D ASN 554 ? H ASN 43  
86  1 Y 1 D LEU 555 ? H LEU 44  
87  1 Y 1 D LEU 556 ? H LEU 45  
88  1 Y 1 D ARG 557 ? H ARG 46  
89  1 Y 1 D ALA 558 ? H ALA 47  
90  1 Y 1 D ILE 559 ? H ILE 48  
91  1 Y 1 D GLU 560 ? H GLU 49  
92  1 Y 1 D ALA 561 ? H ALA 50  
93  1 Y 1 D GLN 562 ? H GLN 51  
94  1 Y 1 D GLN 563 ? H GLN 52  
95  1 Y 1 D HIS 564 ? H HIS 53  
96  1 Y 1 D LEU 565 ? H LEU 54  
97  1 Y 1 D LEU 566 ? H LEU 55  
98  1 Y 1 D LYS 567 ? H LYS 56  
99  1 Y 1 D LEU 568 ? H LEU 57  
100 1 Y 1 I LYS 127 ? J LYS 148 
101 1 Y 1 I SER 128 ? J SER 149 
102 1 Y 1 I THR 129 ? J THR 150 
103 1 Y 1 I SER 130 ? J SER 151 
104 1 Y 1 I LYS 212 ? J LYS 233 
105 1 Y 1 I SER 213 ? J SER 234 
106 1 Y 1 I CYS 214 ? J CYS 235 
107 1 Y 1 K LYS 127 ? L LYS 148 
108 1 Y 1 K SER 128 ? L SER 149 
109 1 Y 1 K THR 129 ? L THR 150 
110 1 Y 1 K SER 130 ? L SER 151 
111 1 Y 1 K LYS 212 ? L LYS 233 
112 1 Y 1 K SER 213 ? L SER 234 
113 1 Y 1 K CYS 214 ? L CYS 235 
# 
_pdbx_audit_support.funding_organization   'National Institutes of Health' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           Intramural 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
7 N-ACETYL-D-GLUCOSAMINE NAG 
8 BETA-D-MANNOSE         BMA 
9 ALPHA-D-MANNOSE        MAN 
# 
