data_1TJP
# 
_entry.id   1TJP 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1TJP         
RCSB  RCSB022695   
WWPDB D_1000022695 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 1QOP 'The same protein complexed with Indole Propanol Phosphate'            unspecified 
PDB 1TJR 'Crystal Structure Of Wild-Type BX1 Complexed With Ammonium Phosphate' unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1TJP 
_pdbx_database_status.recvd_initial_deposition_date   2004-06-07 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Kulik, V.'       1 
'Hartmann, E.'    2 
'Weyand, M.'      3 
'Frey, M.'        4 
'Gierl, A.'       5 
'Niks, D.'        6 
'Dunn, M.F.'      7 
'Schlichting, I.' 8 
# 
_citation.id                        primary 
_citation.title                     
;On the structural basis of the catalytic mechanism and the regulation of the alpha subunit of tryptophan synthase from Salmonella typhimurium and BX1 from maize, two evolutionarily related enzymes.
;
_citation.journal_abbrev            J.Mol.Biol. 
_citation.journal_volume            352 
_citation.page_first                608 
_citation.page_last                 620 
_citation.year                      2005 
_citation.journal_id_ASTM           JMOBAK 
_citation.country                   UK 
_citation.journal_id_ISSN           0022-2836 
_citation.journal_id_CSD            0070 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   16120446 
_citation.pdbx_database_id_DOI      10.1016/j.jmb.2005.07.014 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Kulik, V.'       1 
primary 'Hartmann, E.'    2 
primary 'Weyand, M.'      3 
primary 'Frey, M.'        4 
primary 'Gierl, A.'       5 
primary 'Niks, D.'        6 
primary 'Dunn, M.F.'      7 
primary 'Schlichting, I.' 8 
# 
_cell.entry_id           1TJP 
_cell.length_a           183.0 
_cell.length_b           59.5 
_cell.length_c           67.3 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.8 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1TJP 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
# 
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 'Tryptophan synthase alpha chain'                28698.797 1   4.2.1.20 ? ? ? 
2 polymer     man 'Tryptophan synthase beta chain'                 42787.688 1   4.2.1.20 ? ? ? 
3 non-polymer syn '1-[(2-HYDROXYLPHENYL)AMINO]3-GLYCEROLPHOSPHATE' 279.184   1   ?        ? ? ? 
4 non-polymer syn 'SODIUM ION'                                     22.990    1   ?        ? ? ? 
5 non-polymer syn "PYRIDOXAL-5'-PHOSPHATE"                         247.142   1   ?        ? ? ? 
6 water       nat water                                            18.015    837 ?        ? ? ? 
# 
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 
;MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQ
CFEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADD
DLLRQVASYGRGYTYLLSRSGVTGAENRGALPLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKI
IEKNLASPKQMLAELRSFVSAMKAASRA
;
;MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQ
CFEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADD
DLLRQVASYGRGYTYLLSRSGVTGAENRGALPLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKI
IEKNLASPKQMLAELRSFVSAMKAASRA
;
A ? 
2 'polypeptide(L)' no no 
;TTLLNPYFGEFGGMYVPQILMPALNQLEEAFVSAQKDPEFQAQFADLLKNYAGRPTALTKCQNITAGTRTTLYLKREDLL
HGGAHKTNQVLGQALLAKRMGKSEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVHS
GSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIVREFQRMIGEETKAQILDKEGRLPDAVIACVGGGSNAIGMF
ADFINDTSVGLIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTADGQIEESYSISAGLDFPSVGPQHAYLNSIGR
ADYVSITDDEALEAFKTLCRHEGIIPALESSHALAHALKMMREQPEKEQLLVVNLSGRGDKDIFTVHDILKARGEI
;
;TTLLNPYFGEFGGMYVPQILMPALNQLEEAFVSAQKDPEFQAQFADLLKNYAGRPTALTKCQNITAGTRTTLYLKREDLL
HGGAHKTNQVLGQALLAKRMGKSEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVHS
GSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIVREFQRMIGEETKAQILDKEGRLPDAVIACVGGGSNAIGMF
ADFINDTSVGLIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTADGQIEESYSISAGLDFPSVGPQHAYLNSIGR
ADYVSITDDEALEAFKTLCRHEGIIPALESSHALAHALKMMREQPEKEQLLVVNLSGRGDKDIFTVHDILKARGEI
;
B ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLU n 
1 3   ARG n 
1 4   TYR n 
1 5   GLU n 
1 6   ASN n 
1 7   LEU n 
1 8   PHE n 
1 9   ALA n 
1 10  GLN n 
1 11  LEU n 
1 12  ASN n 
1 13  ASP n 
1 14  ARG n 
1 15  ARG n 
1 16  GLU n 
1 17  GLY n 
1 18  ALA n 
1 19  PHE n 
1 20  VAL n 
1 21  PRO n 
1 22  PHE n 
1 23  VAL n 
1 24  THR n 
1 25  LEU n 
1 26  GLY n 
1 27  ASP n 
1 28  PRO n 
1 29  GLY n 
1 30  ILE n 
1 31  GLU n 
1 32  GLN n 
1 33  SER n 
1 34  LEU n 
1 35  LYS n 
1 36  ILE n 
1 37  ILE n 
1 38  ASP n 
1 39  THR n 
1 40  LEU n 
1 41  ILE n 
1 42  ASP n 
1 43  ALA n 
1 44  GLY n 
1 45  ALA n 
1 46  ASP n 
1 47  ALA n 
1 48  LEU n 
1 49  GLU n 
1 50  LEU n 
1 51  GLY n 
1 52  VAL n 
1 53  PRO n 
1 54  PHE n 
1 55  SER n 
1 56  ASP n 
1 57  PRO n 
1 58  LEU n 
1 59  ALA n 
1 60  ASP n 
1 61  GLY n 
1 62  PRO n 
1 63  THR n 
1 64  ILE n 
1 65  GLN n 
1 66  ASN n 
1 67  ALA n 
1 68  ASN n 
1 69  LEU n 
1 70  ARG n 
1 71  ALA n 
1 72  PHE n 
1 73  ALA n 
1 74  ALA n 
1 75  GLY n 
1 76  VAL n 
1 77  THR n 
1 78  PRO n 
1 79  ALA n 
1 80  GLN n 
1 81  CYS n 
1 82  PHE n 
1 83  GLU n 
1 84  MET n 
1 85  LEU n 
1 86  ALA n 
1 87  LEU n 
1 88  ILE n 
1 89  ARG n 
1 90  GLU n 
1 91  LYS n 
1 92  HIS n 
1 93  PRO n 
1 94  THR n 
1 95  ILE n 
1 96  PRO n 
1 97  ILE n 
1 98  GLY n 
1 99  LEU n 
1 100 LEU n 
1 101 MET n 
1 102 TYR n 
1 103 ALA n 
1 104 ASN n 
1 105 LEU n 
1 106 VAL n 
1 107 PHE n 
1 108 ASN n 
1 109 ASN n 
1 110 GLY n 
1 111 ILE n 
1 112 ASP n 
1 113 ALA n 
1 114 PHE n 
1 115 TYR n 
1 116 ALA n 
1 117 ARG n 
1 118 CYS n 
1 119 GLU n 
1 120 GLN n 
1 121 VAL n 
1 122 GLY n 
1 123 VAL n 
1 124 ASP n 
1 125 SER n 
1 126 VAL n 
1 127 LEU n 
1 128 VAL n 
1 129 ALA n 
1 130 ASP n 
1 131 VAL n 
1 132 PRO n 
1 133 VAL n 
1 134 GLU n 
1 135 GLU n 
1 136 SER n 
1 137 ALA n 
1 138 PRO n 
1 139 PHE n 
1 140 ARG n 
1 141 GLN n 
1 142 ALA n 
1 143 ALA n 
1 144 LEU n 
1 145 ARG n 
1 146 HIS n 
1 147 ASN n 
1 148 ILE n 
1 149 ALA n 
1 150 PRO n 
1 151 ILE n 
1 152 PHE n 
1 153 ILE n 
1 154 CYS n 
1 155 PRO n 
1 156 PRO n 
1 157 ASN n 
1 158 ALA n 
1 159 ASP n 
1 160 ASP n 
1 161 ASP n 
1 162 LEU n 
1 163 LEU n 
1 164 ARG n 
1 165 GLN n 
1 166 VAL n 
1 167 ALA n 
1 168 SER n 
1 169 TYR n 
1 170 GLY n 
1 171 ARG n 
1 172 GLY n 
1 173 TYR n 
1 174 THR n 
1 175 TYR n 
1 176 LEU n 
1 177 LEU n 
1 178 SER n 
1 179 ARG n 
1 180 SER n 
1 181 GLY n 
1 182 VAL n 
1 183 THR n 
1 184 GLY n 
1 185 ALA n 
1 186 GLU n 
1 187 ASN n 
1 188 ARG n 
1 189 GLY n 
1 190 ALA n 
1 191 LEU n 
1 192 PRO n 
1 193 LEU n 
1 194 HIS n 
1 195 HIS n 
1 196 LEU n 
1 197 ILE n 
1 198 GLU n 
1 199 LYS n 
1 200 LEU n 
1 201 LYS n 
1 202 GLU n 
1 203 TYR n 
1 204 HIS n 
1 205 ALA n 
1 206 ALA n 
1 207 PRO n 
1 208 ALA n 
1 209 LEU n 
1 210 GLN n 
1 211 GLY n 
1 212 PHE n 
1 213 GLY n 
1 214 ILE n 
1 215 SER n 
1 216 SER n 
1 217 PRO n 
1 218 GLU n 
1 219 GLN n 
1 220 VAL n 
1 221 SER n 
1 222 ALA n 
1 223 ALA n 
1 224 VAL n 
1 225 ARG n 
1 226 ALA n 
1 227 GLY n 
1 228 ALA n 
1 229 ALA n 
1 230 GLY n 
1 231 ALA n 
1 232 ILE n 
1 233 SER n 
1 234 GLY n 
1 235 SER n 
1 236 ALA n 
1 237 ILE n 
1 238 VAL n 
1 239 LYS n 
1 240 ILE n 
1 241 ILE n 
1 242 GLU n 
1 243 LYS n 
1 244 ASN n 
1 245 LEU n 
1 246 ALA n 
1 247 SER n 
1 248 PRO n 
1 249 LYS n 
1 250 GLN n 
1 251 MET n 
1 252 LEU n 
1 253 ALA n 
1 254 GLU n 
1 255 LEU n 
1 256 ARG n 
1 257 SER n 
1 258 PHE n 
1 259 VAL n 
1 260 SER n 
1 261 ALA n 
1 262 MET n 
1 263 LYS n 
1 264 ALA n 
1 265 ALA n 
1 266 SER n 
1 267 ARG n 
1 268 ALA n 
2 1   THR n 
2 2   THR n 
2 3   LEU n 
2 4   LEU n 
2 5   ASN n 
2 6   PRO n 
2 7   TYR n 
2 8   PHE n 
2 9   GLY n 
2 10  GLU n 
2 11  PHE n 
2 12  GLY n 
2 13  GLY n 
2 14  MET n 
2 15  TYR n 
2 16  VAL n 
2 17  PRO n 
2 18  GLN n 
2 19  ILE n 
2 20  LEU n 
2 21  MET n 
2 22  PRO n 
2 23  ALA n 
2 24  LEU n 
2 25  ASN n 
2 26  GLN n 
2 27  LEU n 
2 28  GLU n 
2 29  GLU n 
2 30  ALA n 
2 31  PHE n 
2 32  VAL n 
2 33  SER n 
2 34  ALA n 
2 35  GLN n 
2 36  LYS n 
2 37  ASP n 
2 38  PRO n 
2 39  GLU n 
2 40  PHE n 
2 41  GLN n 
2 42  ALA n 
2 43  GLN n 
2 44  PHE n 
2 45  ALA n 
2 46  ASP n 
2 47  LEU n 
2 48  LEU n 
2 49  LYS n 
2 50  ASN n 
2 51  TYR n 
2 52  ALA n 
2 53  GLY n 
2 54  ARG n 
2 55  PRO n 
2 56  THR n 
2 57  ALA n 
2 58  LEU n 
2 59  THR n 
2 60  LYS n 
2 61  CYS n 
2 62  GLN n 
2 63  ASN n 
2 64  ILE n 
2 65  THR n 
2 66  ALA n 
2 67  GLY n 
2 68  THR n 
2 69  ARG n 
2 70  THR n 
2 71  THR n 
2 72  LEU n 
2 73  TYR n 
2 74  LEU n 
2 75  LYS n 
2 76  ARG n 
2 77  GLU n 
2 78  ASP n 
2 79  LEU n 
2 80  LEU n 
2 81  HIS n 
2 82  GLY n 
2 83  GLY n 
2 84  ALA n 
2 85  HIS n 
2 86  LYS n 
2 87  THR n 
2 88  ASN n 
2 89  GLN n 
2 90  VAL n 
2 91  LEU n 
2 92  GLY n 
2 93  GLN n 
2 94  ALA n 
2 95  LEU n 
2 96  LEU n 
2 97  ALA n 
2 98  LYS n 
2 99  ARG n 
2 100 MET n 
2 101 GLY n 
2 102 LYS n 
2 103 SER n 
2 104 GLU n 
2 105 ILE n 
2 106 ILE n 
2 107 ALA n 
2 108 GLU n 
2 109 THR n 
2 110 GLY n 
2 111 ALA n 
2 112 GLY n 
2 113 GLN n 
2 114 HIS n 
2 115 GLY n 
2 116 VAL n 
2 117 ALA n 
2 118 SER n 
2 119 ALA n 
2 120 LEU n 
2 121 ALA n 
2 122 SER n 
2 123 ALA n 
2 124 LEU n 
2 125 LEU n 
2 126 GLY n 
2 127 LEU n 
2 128 LYS n 
2 129 CYS n 
2 130 ARG n 
2 131 ILE n 
2 132 TYR n 
2 133 MET n 
2 134 GLY n 
2 135 ALA n 
2 136 LYS n 
2 137 ASP n 
2 138 VAL n 
2 139 GLU n 
2 140 ARG n 
2 141 GLN n 
2 142 SER n 
2 143 PRO n 
2 144 ASN n 
2 145 VAL n 
2 146 PHE n 
2 147 ARG n 
2 148 MET n 
2 149 ARG n 
2 150 LEU n 
2 151 MET n 
2 152 GLY n 
2 153 ALA n 
2 154 GLU n 
2 155 VAL n 
2 156 ILE n 
2 157 PRO n 
2 158 VAL n 
2 159 HIS n 
2 160 SER n 
2 161 GLY n 
2 162 SER n 
2 163 ALA n 
2 164 THR n 
2 165 LEU n 
2 166 LYS n 
2 167 ASP n 
2 168 ALA n 
2 169 CYS n 
2 170 ASN n 
2 171 GLU n 
2 172 ALA n 
2 173 LEU n 
2 174 ARG n 
2 175 ASP n 
2 176 TRP n 
2 177 SER n 
2 178 GLY n 
2 179 SER n 
2 180 TYR n 
2 181 GLU n 
2 182 THR n 
2 183 ALA n 
2 184 HIS n 
2 185 TYR n 
2 186 MET n 
2 187 LEU n 
2 188 GLY n 
2 189 THR n 
2 190 ALA n 
2 191 ALA n 
2 192 GLY n 
2 193 PRO n 
2 194 HIS n 
2 195 PRO n 
2 196 TYR n 
2 197 PRO n 
2 198 THR n 
2 199 ILE n 
2 200 VAL n 
2 201 ARG n 
2 202 GLU n 
2 203 PHE n 
2 204 GLN n 
2 205 ARG n 
2 206 MET n 
2 207 ILE n 
2 208 GLY n 
2 209 GLU n 
2 210 GLU n 
2 211 THR n 
2 212 LYS n 
2 213 ALA n 
2 214 GLN n 
2 215 ILE n 
2 216 LEU n 
2 217 ASP n 
2 218 LYS n 
2 219 GLU n 
2 220 GLY n 
2 221 ARG n 
2 222 LEU n 
2 223 PRO n 
2 224 ASP n 
2 225 ALA n 
2 226 VAL n 
2 227 ILE n 
2 228 ALA n 
2 229 CYS n 
2 230 VAL n 
2 231 GLY n 
2 232 GLY n 
2 233 GLY n 
2 234 SER n 
2 235 ASN n 
2 236 ALA n 
2 237 ILE n 
2 238 GLY n 
2 239 MET n 
2 240 PHE n 
2 241 ALA n 
2 242 ASP n 
2 243 PHE n 
2 244 ILE n 
2 245 ASN n 
2 246 ASP n 
2 247 THR n 
2 248 SER n 
2 249 VAL n 
2 250 GLY n 
2 251 LEU n 
2 252 ILE n 
2 253 GLY n 
2 254 VAL n 
2 255 GLU n 
2 256 PRO n 
2 257 GLY n 
2 258 GLY n 
2 259 HIS n 
2 260 GLY n 
2 261 ILE n 
2 262 GLU n 
2 263 THR n 
2 264 GLY n 
2 265 GLU n 
2 266 HIS n 
2 267 GLY n 
2 268 ALA n 
2 269 PRO n 
2 270 LEU n 
2 271 LYS n 
2 272 HIS n 
2 273 GLY n 
2 274 ARG n 
2 275 VAL n 
2 276 GLY n 
2 277 ILE n 
2 278 TYR n 
2 279 PHE n 
2 280 GLY n 
2 281 MET n 
2 282 LYS n 
2 283 ALA n 
2 284 PRO n 
2 285 MET n 
2 286 MET n 
2 287 GLN n 
2 288 THR n 
2 289 ALA n 
2 290 ASP n 
2 291 GLY n 
2 292 GLN n 
2 293 ILE n 
2 294 GLU n 
2 295 GLU n 
2 296 SER n 
2 297 TYR n 
2 298 SER n 
2 299 ILE n 
2 300 SER n 
2 301 ALA n 
2 302 GLY n 
2 303 LEU n 
2 304 ASP n 
2 305 PHE n 
2 306 PRO n 
2 307 SER n 
2 308 VAL n 
2 309 GLY n 
2 310 PRO n 
2 311 GLN n 
2 312 HIS n 
2 313 ALA n 
2 314 TYR n 
2 315 LEU n 
2 316 ASN n 
2 317 SER n 
2 318 ILE n 
2 319 GLY n 
2 320 ARG n 
2 321 ALA n 
2 322 ASP n 
2 323 TYR n 
2 324 VAL n 
2 325 SER n 
2 326 ILE n 
2 327 THR n 
2 328 ASP n 
2 329 ASP n 
2 330 GLU n 
2 331 ALA n 
2 332 LEU n 
2 333 GLU n 
2 334 ALA n 
2 335 PHE n 
2 336 LYS n 
2 337 THR n 
2 338 LEU n 
2 339 CYS n 
2 340 ARG n 
2 341 HIS n 
2 342 GLU n 
2 343 GLY n 
2 344 ILE n 
2 345 ILE n 
2 346 PRO n 
2 347 ALA n 
2 348 LEU n 
2 349 GLU n 
2 350 SER n 
2 351 SER n 
2 352 HIS n 
2 353 ALA n 
2 354 LEU n 
2 355 ALA n 
2 356 HIS n 
2 357 ALA n 
2 358 LEU n 
2 359 LYS n 
2 360 MET n 
2 361 MET n 
2 362 ARG n 
2 363 GLU n 
2 364 GLN n 
2 365 PRO n 
2 366 GLU n 
2 367 LYS n 
2 368 GLU n 
2 369 GLN n 
2 370 LEU n 
2 371 LEU n 
2 372 VAL n 
2 373 VAL n 
2 374 ASN n 
2 375 LEU n 
2 376 SER n 
2 377 GLY n 
2 378 ARG n 
2 379 GLY n 
2 380 ASP n 
2 381 LYS n 
2 382 ASP n 
2 383 ILE n 
2 384 PHE n 
2 385 THR n 
2 386 VAL n 
2 387 HIS n 
2 388 ASP n 
2 389 ILE n 
2 390 LEU n 
2 391 LYS n 
2 392 ALA n 
2 393 ARG n 
2 394 GLY n 
2 395 GLU n 
2 396 ILE 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 ? ? ? ? Salmonella 'TRPA, STM1727'                 ? ? ? ? ? ? 'Salmonella typhimurium' 602 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 Escherichia ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample ? ? ? ? Salmonella 'TRPB, STM1726, STY1325, T1638' ? ? ? ? ? ? 'Salmonella typhimurium' 602 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 Escherichia ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_db_isoform 
1 UNP TRPA_SALTY P00929 1 
;MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQ
CFEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADD
DLLRQVASYGRGYTYLLSRSGVTGAENRGALPLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKI
IEKNLASPKQMLAELRSFVSAMKAASRA
;
1 ? 
2 UNP TRPB_SALTY P00933 2 
;TTLLNPYFGEFGGMYVPQILMPALNQLEEAFVSAQKDPEFQAQFADLLKNYAGRPTALTKCQNITAGTRTTLYLKREDLL
HGGAHKTNQVLGQALLAKRMGKSEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVHS
GSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIVREFQRMIGEETKAQILDKEGRLPDAVIACVGGGSNAIGMF
ADFINDTSVGLIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTADGQIEESYSISAGLDFPSVGPQHAYLNSIGR
ADYVSITDDEALEAFKTLCRHEGIIPALESSHALAHALKMMREQPEKEQLLVVNLSGRGDKDIFTVHDILKARGEI
;
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 1TJP A 1 ? 268 ? P00929 1 ? 268 ? 1 268 
2 2 1TJP B 1 ? 396 ? P00933 1 ? 396 ? 2 397 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                          ?                      'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                         ?                      'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                       ?                      'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                  ?                      'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                         ?                      'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                                        ?                      'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                  ?                      'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                          ?                      'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                        ?                      'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                            ?                      'H2 O'           18.015  
HPF non-polymer         . '1-[(2-HYDROXYLPHENYL)AMINO]3-GLYCEROLPHOSPHATE' ?                      'C9 H14 N O7 P'  279.184 
ILE 'L-peptide linking' y ISOLEUCINE                                       ?                      'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                          ?                      'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                           ?                      'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                       ?                      'C5 H11 N O2 S'  149.211 
NA  non-polymer         . 'SODIUM ION'                                     ?                      'Na 1'           22.990  
PHE 'L-peptide linking' y PHENYLALANINE                                    ?                      'C9 H11 N O2'    165.189 
PLP non-polymer         . "PYRIDOXAL-5'-PHOSPHATE"                         'VITAMIN B6 Phosphate' 'C8 H10 N O6 P'  247.142 
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.entry_id          1TJP 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.55 
_exptl_crystal.density_percent_sol   51.81 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            296 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.8 
_exptl_crystal_grow.pdbx_details    
;BICINE, EDTA, DITHIOERYTHRITOL, PYRIDOXAL-5'-PHOSPHATE, SPERMINE, PEG 8000, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 296K
;
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 4' 
_diffrn_detector.pdbx_collection_date   ? 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.934 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ESRF BEAMLINE ID14-1' 
_diffrn_source.pdbx_synchrotron_site       ESRF 
_diffrn_source.pdbx_synchrotron_beamline   ID14-1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.934 
# 
_reflns.entry_id                     1TJP 
_reflns.observed_criterion_sigma_I   0.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             20 
_reflns.d_resolution_high            1.4 
_reflns.number_obs                   136709 
_reflns.number_all                   397395 
_reflns.percent_possible_obs         96.4 
_reflns.pdbx_Rmerge_I_obs            0.08 
_reflns.pdbx_Rsym_value              0.125 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        16.8 
_reflns.pdbx_redundancy              ? 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             1.40 
_reflns_shell.d_res_low              1.45 
_reflns_shell.percent_possible_all   91.4 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 1TJP 
_refine.ls_number_reflns_obs                     114597 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               3256299.36 
_refine.pdbx_data_cutoff_low_absF                0.000000 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             19.94 
_refine.ls_d_res_high                            1.50 
_refine.ls_percent_reflns_obs                    99.3 
_refine.ls_R_factor_obs                          0.167 
_refine.ls_R_factor_all                          0.167 
_refine.ls_R_factor_R_work                       0.167 
_refine.ls_R_factor_R_free                       0.193 
_refine.ls_R_factor_R_free_error                 0.003 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  5730 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               18.0 
_refine.aniso_B[1][1]                            -1.45 
_refine.aniso_B[2][2]                            3.27 
_refine.aniso_B[3][3]                            -1.82 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.04 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    'FLAT MODEL' 
_refine.solvent_model_param_ksol                 0.373392 
_refine.solvent_model_param_bsol                 54.9263 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'BULK SOLVENT MODEL USED' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             RESTRAINED 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        1TJP 
_refine_analyze.Luzzati_coordinate_error_obs    0.14 
_refine_analyze.Luzzati_sigma_a_obs             0.09 
_refine_analyze.Luzzati_d_res_low_obs           5.00 
_refine_analyze.Luzzati_coordinate_error_free   0.17 
_refine_analyze.Luzzati_sigma_a_free            0.10 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4961 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         34 
_refine_hist.number_atoms_solvent             837 
_refine_hist.number_atoms_total               5832 
_refine_hist.d_res_high                       1.50 
_refine_hist.d_res_low                        19.94 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
c_bond_d           0.019 ? ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg        1.8   ? ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d 23.1  ? ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d 1.29  ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   6 
_refine_ls_shell.d_res_high                       1.50 
_refine_ls_shell.d_res_low                        1.59 
_refine_ls_shell.number_reflns_R_work             18031 
_refine_ls_shell.R_factor_R_work                  0.208 
_refine_ls_shell.percent_reflns_obs               99.5 
_refine_ls_shell.R_factor_R_free                  0.239 
_refine_ls_shell.R_factor_R_free_error            0.008 
_refine_ls_shell.percent_reflns_R_free            5.0 
_refine_ls_shell.number_reflns_R_free             949 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
loop_
_pdbx_xplor_file.serial_no 
_pdbx_xplor_file.param_file 
_pdbx_xplor_file.topol_file 
_pdbx_xplor_file.pdbx_refine_id 
1 PROTEIN_REP.PARAM PROTEIN.TOP  'X-RAY DIFFRACTION' 
2 TRPS_LIG.PARAM    TRPS_LIG.TOP 'X-RAY DIFFRACTION' 
3 WATER_REP.PARAM   WATER.TOP    'X-RAY DIFFRACTION' 
4 ION.PARAM         ION.TOP      'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  1TJP 
_struct.title                     
'Crystal Structure Of Wild-Type Tryptophan Synthase Complexed With 1-[(2-hydroxylphenyl)amino]3-glycerolphosphate' 
_struct.pdbx_descriptor           'Tryptophan synthase alpha chain (E.C.4.2.1.20), Tryptophan synthase beta chain (E.C.4.2.1.20)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1TJP 
_struct_keywords.pdbx_keywords   LYASE 
_struct_keywords.text            'substrate channeling, transition state analog, enzymatic mechanism, allosteric regulation, LYASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 6 ? 
# 
_struct_biol.id   1 
# 
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  1  GLU A 2   ? ARG A 14  ? GLU A 2   ARG A 14  1 ? 13 
HELX_P HELX_P2  2  GLY A 29  ? ALA A 43  ? GLY A 29  ALA A 43  1 ? 15 
HELX_P HELX_P3  3  GLY A 61  ? ALA A 74  ? GLY A 61  ALA A 74  1 ? 14 
HELX_P HELX_P4  4  THR A 77  ? HIS A 92  ? THR A 77  HIS A 92  1 ? 16 
HELX_P HELX_P5  5  TYR A 102 ? ASN A 108 ? TYR A 102 ASN A 108 1 ? 7  
HELX_P HELX_P6  6  GLY A 110 ? GLY A 122 ? GLY A 110 GLY A 122 1 ? 13 
HELX_P HELX_P7  7  PRO A 132 ? GLU A 135 ? PRO A 132 GLU A 135 5 ? 4  
HELX_P HELX_P8  8  SER A 136 ? HIS A 146 ? SER A 136 HIS A 146 1 ? 11 
HELX_P HELX_P9  9  ASP A 159 ? GLY A 170 ? ASP A 159 GLY A 170 1 ? 12 
HELX_P HELX_P10 10 LEU A 193 ? TYR A 203 ? LEU A 193 TYR A 203 1 ? 11 
HELX_P HELX_P11 11 SER A 216 ? ALA A 226 ? SER A 216 ALA A 226 1 ? 11 
HELX_P HELX_P12 12 GLY A 234 ? ASN A 244 ? GLY A 234 ASN A 244 1 ? 11 
HELX_P HELX_P13 13 SER A 247 ? ALA A 265 ? SER A 247 ALA A 265 1 ? 19 
HELX_P HELX_P14 14 PRO B 17  ? ILE B 19  ? PRO B 18  ILE B 20  5 ? 3  
HELX_P HELX_P15 15 LEU B 20  ? LYS B 36  ? LEU B 21  LYS B 37  1 ? 17 
HELX_P HELX_P16 16 ASP B 37  ? TYR B 51  ? ASP B 38  TYR B 52  1 ? 15 
HELX_P HELX_P17 17 CYS B 61  ? ALA B 66  ? CYS B 62  ALA B 67  1 ? 6  
HELX_P HELX_P18 18 ASP B 78  ? LEU B 80  ? ASP B 79  LEU B 81  5 ? 3  
HELX_P HELX_P19 19 HIS B 85  ? MET B 100 ? HIS B 86  MET B 101 1 ? 16 
HELX_P HELX_P20 20 GLY B 112 ? GLY B 126 ? GLY B 113 GLY B 127 1 ? 15 
HELX_P HELX_P21 21 ALA B 135 ? GLN B 141 ? ALA B 136 GLN B 142 1 ? 7  
HELX_P HELX_P22 22 GLN B 141 ? MET B 151 ? GLN B 142 MET B 152 1 ? 11 
HELX_P HELX_P23 23 THR B 164 ? TYR B 180 ? THR B 165 TYR B 181 1 ? 17 
HELX_P HELX_P24 24 PRO B 195 ? PHE B 203 ? PRO B 196 PHE B 204 1 ? 9  
HELX_P HELX_P25 25 ARG B 205 ? GLY B 220 ? ARG B 206 GLY B 221 1 ? 16 
HELX_P HELX_P26 26 GLY B 233 ? ALA B 241 ? GLY B 234 ALA B 242 1 ? 9  
HELX_P HELX_P27 27 ASP B 242 ? ILE B 244 ? ASP B 243 ILE B 245 5 ? 3  
HELX_P HELX_P28 28 GLY B 260 ? GLY B 264 ? GLY B 261 GLY B 265 5 ? 5  
HELX_P HELX_P29 29 ALA B 268 ? GLY B 273 ? ALA B 269 GLY B 274 1 ? 6  
HELX_P HELX_P30 30 SER B 300 ? ASP B 304 ? SER B 301 ASP B 305 5 ? 5  
HELX_P HELX_P31 31 GLY B 309 ? ILE B 318 ? GLY B 310 ILE B 319 1 ? 10 
HELX_P HELX_P32 32 ASP B 328 ? GLY B 343 ? ASP B 329 GLY B 344 1 ? 16 
HELX_P HELX_P33 33 ALA B 347 ? GLN B 364 ? ALA B 348 GLN B 365 1 ? 18 
HELX_P HELX_P34 34 GLY B 379 ? LYS B 381 ? GLY B 380 LYS B 382 5 ? 3  
HELX_P HELX_P35 35 ASP B 382 ? GLY B 394 ? ASP B 383 GLY B 395 1 ? 13 
# 
_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 
covale1 covale ? ? B LYS 86  NZ ? ? ? 1_555 E PLP .   C4A ? ? B LYS 87   B PLP 1002 1_555 ? ? ? ? ? ? ? 1.357 ? 
metalc1 metalc ? ? D NA  .   NA ? ? ? 1_555 B GLY 231 O   ? ? B NA  1003 B GLY 232  1_555 ? ? ? ? ? ? ? 2.266 ? 
metalc2 metalc ? ? D NA  .   NA ? ? ? 1_555 B PHE 305 O   A ? B NA  1003 B PHE 306  1_555 ? ? ? ? ? ? ? 2.328 ? 
metalc3 metalc ? ? D NA  .   NA ? ? ? 1_555 G HOH .   O   ? ? B NA  1003 B HOH 1039 1_555 ? ? ? ? ? ? ? 2.318 ? 
metalc4 metalc ? ? D NA  .   NA ? ? ? 1_555 G HOH .   O   ? ? B NA  1003 B HOH 1047 1_555 ? ? ? ? ? ? ? 2.417 ? 
metalc5 metalc ? ? D NA  .   NA ? ? ? 1_555 B SER 307 O   ? ? B NA  1003 B SER 308  1_555 ? ? ? ? ? ? ? 2.310 ? 
metalc6 metalc ? ? B PHE 305 O  B ? ? 1_555 D NA  .   NA  ? ? B PHE 306  B NA  1003 1_555 ? ? ? ? ? ? ? 2.641 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
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 ASP 27  A . ? ASP 27  A PRO 28  A ? PRO 28  A 1 0.74  
2 ARG 54  B . ? ARG 55  B PRO 55  B ? PRO 56  B 1 -0.31 
3 HIS 194 B . ? HIS 195 B PRO 195 B ? PRO 196 B 1 2.53  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 9 ? 
B ? 4 ? 
C ? 6 ? 
D ? 4 ? 
# 
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 
A 1 2 ? parallel      
A 2 3 ? parallel      
A 3 4 ? parallel      
A 4 5 ? parallel      
A 5 6 ? parallel      
A 6 7 ? parallel      
A 7 8 ? parallel      
A 8 9 ? parallel      
B 1 2 ? anti-parallel 
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? parallel      
C 3 4 ? parallel      
C 4 5 ? parallel      
C 5 6 ? parallel      
D 1 2 ? parallel      
D 2 3 ? parallel      
D 3 4 ? 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 
A 1 ALA A 149 ? ILE A 151 ? ALA A 149 ILE A 151 
A 2 SER A 125 ? VAL A 128 ? SER A 125 VAL A 128 
A 3 ILE A 97  ? MET A 101 ? ILE A 97  MET A 101 
A 4 LEU A 48  ? GLY A 51  ? LEU A 48  GLY A 51  
A 5 ALA A 18  ? THR A 24  ? ALA A 18  THR A 24  
A 6 GLY A 230 ? SER A 233 ? GLY A 230 SER A 233 
A 7 ALA A 208 ? GLY A 211 ? ALA A 208 GLY A 211 
A 8 THR A 174 ? LEU A 177 ? THR A 174 LEU A 177 
A 9 ILE A 153 ? CYS A 154 ? ILE A 153 CYS A 154 
B 1 TYR B 7   ? PHE B 8   ? TYR B 8   PHE B 9   
B 2 PHE B 11  ? TYR B 15  ? PHE B 12  TYR B 16  
B 3 GLY B 280 ? MET B 285 ? GLY B 281 MET B 286 
B 4 ARG B 274 ? TYR B 278 ? ARG B 275 TYR B 279 
C 1 LEU B 58  ? LYS B 60  ? LEU B 59  LYS B 61  
C 2 THR B 70  ? ARG B 76  ? THR B 71  ARG B 77  
C 3 GLN B 369 ? LEU B 375 ? GLN B 370 LEU B 376 
C 4 ALA B 225 ? CYS B 229 ? ALA B 226 CYS B 230 
C 5 GLY B 250 ? GLY B 258 ? GLY B 251 GLY B 259 
C 6 ASP B 322 ? THR B 327 ? ASP B 323 THR B 328 
D 1 GLU B 154 ? VAL B 158 ? GLU B 155 VAL B 159 
D 2 LYS B 128 ? GLY B 134 ? LYS B 129 GLY B 135 
D 3 GLU B 104 ? THR B 109 ? GLU B 105 THR B 110 
D 4 ALA B 183 ? TYR B 185 ? ALA B 184 TYR B 186 
# 
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 
A 1 2 O ILE A 151 ? O ILE A 151 N VAL A 126 ? N VAL A 126 
A 2 3 O LEU A 127 ? O LEU A 127 N MET A 101 ? N MET A 101 
A 3 4 O GLY A 98  ? O GLY A 98  N LEU A 50  ? N LEU A 50  
A 4 5 O GLY A 51  ? O GLY A 51  N VAL A 23  ? N VAL A 23  
A 5 6 N VAL A 20  ? N VAL A 20  O ALA A 231 ? O ALA A 231 
A 6 7 O ILE A 232 ? O ILE A 232 N GLN A 210 ? N GLN A 210 
A 7 8 O LEU A 209 ? O LEU A 209 N THR A 174 ? N THR A 174 
A 8 9 O TYR A 175 ? O TYR A 175 N CYS A 154 ? N CYS A 154 
B 1 2 N PHE B 8   ? N PHE B 9   O PHE B 11  ? O PHE B 12  
B 2 3 N GLY B 12  ? N GLY B 13  O LYS B 282 ? O LYS B 283 
B 3 4 O ALA B 283 ? O ALA B 284 N GLY B 276 ? N GLY B 277 
C 1 2 N THR B 59  ? N THR B 60  O LEU B 74  ? O LEU B 75  
C 2 3 N THR B 71  ? N THR B 72  O LEU B 371 ? O LEU B 372 
C 3 4 O VAL B 372 ? O VAL B 373 N ILE B 227 ? N ILE B 228 
C 4 5 N ALA B 228 ? N ALA B 229 O VAL B 254 ? O VAL B 255 
C 5 6 N GLY B 257 ? N GLY B 258 O ILE B 326 ? O ILE B 327 
D 1 2 O ILE B 156 ? O ILE B 157 N ILE B 131 ? N ILE B 132 
D 2 3 O LYS B 128 ? O LYS B 129 N ILE B 105 ? N ILE B 106 
D 3 4 N ILE B 106 ? N ILE B 107 O HIS B 184 ? O HIS B 185 
# 
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 ? ? ? ? 5  'BINDING SITE FOR RESIDUE NA B 1003'  
AC2 Software ? ? ? ? 15 'BINDING SITE FOR RESIDUE HPF A 1001' 
AC3 Software ? ? ? ? 18 'BINDING SITE FOR RESIDUE PLP B 1002' 
# 
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 5  GLY B 231 ? GLY B 232  . ? 1_555 ? 
2  AC1 5  PHE B 305 ? PHE B 306  . ? 1_555 ? 
3  AC1 5  SER B 307 ? SER B 308  . ? 1_555 ? 
4  AC1 5  HOH G .   ? HOH B 1039 . ? 1_555 ? 
5  AC1 5  HOH G .   ? HOH B 1047 . ? 1_555 ? 
6  AC2 15 PHE A 22  ? PHE A 22   . ? 1_555 ? 
7  AC2 15 GLU A 49  ? GLU A 49   . ? 1_555 ? 
8  AC2 15 ASP A 60  ? ASP A 60   . ? 1_555 ? 
9  AC2 15 ILE A 64  ? ILE A 64   . ? 1_555 ? 
10 AC2 15 LEU A 100 ? LEU A 100  . ? 1_555 ? 
11 AC2 15 TYR A 175 ? TYR A 175  . ? 1_555 ? 
12 AC2 15 THR A 183 ? THR A 183  . ? 1_555 ? 
13 AC2 15 GLY A 184 ? GLY A 184  . ? 1_555 ? 
14 AC2 15 PHE A 212 ? PHE A 212  . ? 1_555 ? 
15 AC2 15 GLY A 213 ? GLY A 213  . ? 1_555 ? 
16 AC2 15 ILE A 232 ? ILE A 232  . ? 1_555 ? 
17 AC2 15 GLY A 234 ? GLY A 234  . ? 1_555 ? 
18 AC2 15 SER A 235 ? SER A 235  . ? 1_555 ? 
19 AC2 15 HOH F .   ? HOH A 1038 . ? 1_555 ? 
20 AC2 15 HOH F .   ? HOH A 1047 . ? 1_555 ? 
21 AC3 18 HIS B 85  ? HIS B 86   . ? 1_555 ? 
22 AC3 18 LYS B 86  ? LYS B 87   . ? 1_555 ? 
23 AC3 18 GLN B 113 ? GLN B 114  . ? 1_555 ? 
24 AC3 18 THR B 189 ? THR B 190  . ? 1_555 ? 
25 AC3 18 CYS B 229 ? CYS B 230  . ? 1_555 ? 
26 AC3 18 GLY B 231 ? GLY B 232  . ? 1_555 ? 
27 AC3 18 GLY B 232 ? GLY B 233  . ? 1_555 ? 
28 AC3 18 GLY B 233 ? GLY B 234  . ? 1_555 ? 
29 AC3 18 SER B 234 ? SER B 235  . ? 1_555 ? 
30 AC3 18 ASN B 235 ? ASN B 236  . ? 1_555 ? 
31 AC3 18 GLY B 302 ? GLY B 303  . ? 1_555 ? 
32 AC3 18 GLU B 349 ? GLU B 350  . ? 1_555 ? 
33 AC3 18 SER B 376 ? SER B 377  . ? 1_555 ? 
34 AC3 18 GLY B 377 ? GLY B 378  . ? 1_555 ? 
35 AC3 18 HOH G .   ? HOH B 1006 . ? 1_555 ? 
36 AC3 18 HOH G .   ? HOH B 1142 . ? 1_555 ? 
37 AC3 18 HOH G .   ? HOH B 1208 . ? 1_555 ? 
38 AC3 18 HOH G .   ? HOH B 1252 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1TJP 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    1TJP 
_atom_sites.fract_transf_matrix[1][1]   0.005464 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000458 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016797 
_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]   0.014915 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
NA 
O  
P  
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   . MET A 1 1   ? 37.738  23.701  35.117  1.00 37.91 ? 1    MET A N   1 
ATOM   2    C  CA  . MET A 1 1   ? 36.775  24.526  34.335  1.00 36.89 ? 1    MET A CA  1 
ATOM   3    C  C   . MET A 1 1   ? 36.415  23.716  33.096  1.00 34.47 ? 1    MET A C   1 
ATOM   4    O  O   . MET A 1 1   ? 37.029  22.674  32.824  1.00 35.42 ? 1    MET A O   1 
ATOM   5    C  CB  . MET A 1 1   ? 37.415  25.855  33.902  1.00 39.21 ? 1    MET A CB  1 
ATOM   6    C  CG  . MET A 1 1   ? 38.053  26.640  35.033  1.00 41.84 ? 1    MET A CG  1 
ATOM   7    S  SD  . MET A 1 1   ? 36.819  27.075  36.248  1.00 47.08 ? 1    MET A SD  1 
ATOM   8    C  CE  . MET A 1 1   ? 35.907  28.392  35.336  1.00 44.97 ? 1    MET A CE  1 
ATOM   9    N  N   . GLU A 1 2   ? 35.423  24.219  32.358  1.00 30.73 ? 2    GLU A N   1 
ATOM   10   C  CA  . GLU A 1 2   ? 34.902  23.619  31.129  1.00 25.85 ? 2    GLU A CA  1 
ATOM   11   C  C   . GLU A 1 2   ? 34.677  24.757  30.129  1.00 22.56 ? 2    GLU A C   1 
ATOM   12   O  O   . GLU A 1 2   ? 33.621  24.870  29.510  1.00 20.40 ? 2    GLU A O   1 
ATOM   13   C  CB  . GLU A 1 2   ? 33.557  22.940  31.435  1.00 28.34 ? 2    GLU A CB  1 
ATOM   14   N  N   . ARG A 1 3   ? 35.675  25.611  29.939  1.00 18.30 ? 3    ARG A N   1 
ATOM   15   C  CA  . ARG A 1 3   ? 35.434  26.730  29.042  1.00 15.59 ? 3    ARG A CA  1 
ATOM   16   C  C   . ARG A 1 3   ? 35.150  26.397  27.595  1.00 15.93 ? 3    ARG A C   1 
ATOM   17   O  O   . ARG A 1 3   ? 34.349  27.027  26.952  1.00 15.07 ? 3    ARG A O   1 
ATOM   18   C  CB  . ARG A 1 3   ? 36.583  27.748  29.125  1.00 14.18 ? 3    ARG A CB  1 
ATOM   19   C  CG  . ARG A 1 3   ? 36.753  28.373  30.500  1.00 13.71 ? 3    ARG A CG  1 
ATOM   20   C  CD  . ARG A 1 3   ? 37.690  29.607  30.486  1.00 14.31 ? 3    ARG A CD  1 
ATOM   21   N  NE  . ARG A 1 3   ? 37.813  30.195  31.814  1.00 14.95 ? 3    ARG A NE  1 
ATOM   22   C  CZ  . ARG A 1 3   ? 38.676  29.811  32.751  1.00 15.09 ? 3    ARG A CZ  1 
ATOM   23   N  NH1 . ARG A 1 3   ? 39.552  28.812  32.550  1.00 14.69 ? 3    ARG A NH1 1 
ATOM   24   N  NH2 . ARG A 1 3   ? 38.676  30.438  33.933  1.00 17.16 ? 3    ARG A NH2 1 
ATOM   25   N  N   . TYR A 1 4   ? 35.848  25.430  27.029  1.00 14.68 ? 4    TYR A N   1 
ATOM   26   C  CA  . TYR A 1 4   ? 35.600  25.036  25.644  1.00 14.90 ? 4    TYR A CA  1 
ATOM   27   C  C   . TYR A 1 4   ? 34.207  24.424  25.510  1.00 15.60 ? 4    TYR A C   1 
ATOM   28   O  O   . TYR A 1 4   ? 33.491  24.696  24.550  1.00 15.78 ? 4    TYR A O   1 
ATOM   29   C  CB  . TYR A 1 4   ? 36.646  24.022  25.169  1.00 13.98 ? 4    TYR A CB  1 
ATOM   30   C  CG  . TYR A 1 4   ? 37.978  24.628  24.796  1.00 12.44 ? 4    TYR A CG  1 
ATOM   31   C  CD1 . TYR A 1 4   ? 38.132  25.358  23.616  1.00 12.28 ? 4    TYR A CD1 1 
ATOM   32   C  CD2 . TYR A 1 4   ? 39.087  24.477  25.625  1.00 12.63 ? 4    TYR A CD2 1 
ATOM   33   C  CE1 . TYR A 1 4   ? 39.361  25.919  23.270  1.00 13.23 ? 4    TYR A CE1 1 
ATOM   34   C  CE2 . TYR A 1 4   ? 40.316  25.037  25.293  1.00 13.01 ? 4    TYR A CE2 1 
ATOM   35   C  CZ  . TYR A 1 4   ? 40.447  25.754  24.116  1.00 12.91 ? 4    TYR A CZ  1 
ATOM   36   O  OH  . TYR A 1 4   ? 41.664  26.306  23.786  1.00 14.44 ? 4    TYR A OH  1 
ATOM   37   N  N   . GLU A 1 5   ? 33.838  23.610  26.502  1.00 18.26 ? 5    GLU A N   1 
ATOM   38   C  CA  . GLU A 1 5   ? 32.509  22.954  26.432  1.00 18.56 ? 5    GLU A CA  1 
ATOM   39   C  C   . GLU A 1 5   ? 31.424  24.027  26.491  1.00 18.25 ? 5    GLU A C   1 
ATOM   40   O  O   . GLU A 1 5   ? 30.443  23.976  25.733  1.00 18.95 ? 5    GLU A O   1 
ATOM   41   C  CB  . GLU A 1 5   ? 32.371  21.967  27.606  1.00 21.37 ? 5    GLU A CB  1 
ATOM   42   C  CG  A GLU A 1 5   ? 33.344  20.772  27.549  0.80 24.89 ? 5    GLU A CG  1 
ATOM   43   C  CG  B GLU A 1 5   ? 31.024  21.289  27.684  0.20 21.35 ? 5    GLU A CG  1 
ATOM   44   C  CD  A GLU A 1 5   ? 34.830  21.165  27.702  0.80 28.35 ? 5    GLU A CD  1 
ATOM   45   C  CD  B GLU A 1 5   ? 31.008  20.192  28.723  0.20 22.44 ? 5    GLU A CD  1 
ATOM   46   O  OE1 A GLU A 1 5   ? 35.672  20.486  27.049  0.80 28.92 ? 5    GLU A OE1 1 
ATOM   47   O  OE1 B GLU A 1 5   ? 31.566  20.408  29.822  0.20 22.25 ? 5    GLU A OE1 1 
ATOM   48   O  OE2 A GLU A 1 5   ? 35.175  22.130  28.462  0.80 28.37 ? 5    GLU A OE2 1 
ATOM   49   O  OE2 B GLU A 1 5   ? 30.433  19.120  28.439  0.20 23.16 ? 5    GLU A OE2 1 
ATOM   50   N  N   . ASN A 1 6   ? 31.620  25.022  27.359  1.00 17.71 ? 6    ASN A N   1 
ATOM   51   C  CA  . ASN A 1 6   ? 30.614  26.082  27.456  1.00 19.49 ? 6    ASN A CA  1 
ATOM   52   C  C   . ASN A 1 6   ? 30.552  26.885  26.168  1.00 19.21 ? 6    ASN A C   1 
ATOM   53   O  O   . ASN A 1 6   ? 29.463  27.216  25.695  1.00 19.06 ? 6    ASN A O   1 
ATOM   54   C  CB  . ASN A 1 6   ? 30.915  26.998  28.629  1.00 19.24 ? 6    ASN A CB  1 
ATOM   55   C  CG  . ASN A 1 6   ? 30.711  26.314  29.961  1.00 22.45 ? 6    ASN A CG  1 
ATOM   56   O  OD1 . ASN A 1 6   ? 30.120  25.205  30.044  1.00 24.39 ? 6    ASN A OD1 1 
ATOM   57   N  ND2 . ASN A 1 6   ? 31.162  26.966  31.022  1.00 24.09 ? 6    ASN A ND2 1 
ATOM   58   N  N   . LEU A 1 7   ? 31.706  27.233  25.586  1.00 16.57 ? 7    LEU A N   1 
ATOM   59   C  CA  . LEU A 1 7   ? 31.704  27.970  24.339  1.00 15.86 ? 7    LEU A CA  1 
ATOM   60   C  C   . LEU A 1 7   ? 30.990  27.223  23.202  1.00 17.03 ? 7    LEU A C   1 
ATOM   61   O  O   . LEU A 1 7   ? 30.143  27.766  22.490  1.00 17.37 ? 7    LEU A O   1 
ATOM   62   C  CB  . LEU A 1 7   ? 33.149  28.232  23.918  1.00 15.68 ? 7    LEU A CB  1 
ATOM   63   C  CG  . LEU A 1 7   ? 33.278  28.905  22.539  1.00 15.60 ? 7    LEU A CG  1 
ATOM   64   C  CD1 . LEU A 1 7   ? 32.750  30.345  22.564  1.00 17.07 ? 7    LEU A CD1 1 
ATOM   65   C  CD2 . LEU A 1 7   ? 34.754  28.911  22.097  1.00 18.17 ? 7    LEU A CD2 1 
ATOM   66   N  N   . PHE A 1 8   ? 31.366  25.980  22.966  1.00 17.34 ? 8    PHE A N   1 
ATOM   67   C  CA  . PHE A 1 8   ? 30.757  25.229  21.877  1.00 17.75 ? 8    PHE A CA  1 
ATOM   68   C  C   . PHE A 1 8   ? 29.259  25.027  22.070  1.00 18.97 ? 8    PHE A C   1 
ATOM   69   O  O   . PHE A 1 8   ? 28.504  24.992  21.096  1.00 19.20 ? 8    PHE A O   1 
ATOM   70   C  CB  . PHE A 1 8   ? 31.469  23.884  21.697  1.00 17.42 ? 8    PHE A CB  1 
ATOM   71   C  CG  . PHE A 1 8   ? 32.857  24.011  21.134  1.00 17.41 ? 8    PHE A CG  1 
ATOM   72   C  CD1 . PHE A 1 8   ? 33.078  24.718  19.955  1.00 16.81 ? 8    PHE A CD1 1 
ATOM   73   C  CD2 . PHE A 1 8   ? 33.944  23.428  21.779  1.00 16.21 ? 8    PHE A CD2 1 
ATOM   74   C  CE1 . PHE A 1 8   ? 34.361  24.845  19.424  1.00 17.75 ? 8    PHE A CE1 1 
ATOM   75   C  CE2 . PHE A 1 8   ? 35.231  23.547  21.257  1.00 17.27 ? 8    PHE A CE2 1 
ATOM   76   C  CZ  . PHE A 1 8   ? 35.441  24.257  20.077  1.00 16.91 ? 8    PHE A CZ  1 
ATOM   77   N  N   . ALA A 1 9   ? 28.838  24.892  23.337  1.00 17.78 ? 9    ALA A N   1 
ATOM   78   C  CA  . ALA A 1 9   ? 27.382  24.723  23.608  1.00 20.24 ? 9    ALA A CA  1 
ATOM   79   C  C   . ALA A 1 9   ? 26.677  26.022  23.267  1.00 21.66 ? 9    ALA A C   1 
ATOM   80   O  O   . ALA A 1 9   ? 25.607  26.016  22.626  1.00 22.25 ? 9    ALA A O   1 
ATOM   81   C  CB  . ALA A 1 9   ? 27.141  24.370  25.069  1.00 20.37 ? 9    ALA A CB  1 
ATOM   82   N  N   . GLN A 1 10  ? 27.271  27.147  23.643  1.00 21.64 ? 10   GLN A N   1 
ATOM   83   C  CA  . GLN A 1 10  ? 26.684  28.446  23.328  1.00 22.77 ? 10   GLN A CA  1 
ATOM   84   C  C   . GLN A 1 10  ? 26.697  28.683  21.809  1.00 22.59 ? 10   GLN A C   1 
ATOM   85   O  O   . GLN A 1 10  ? 25.732  29.146  21.234  1.00 21.71 ? 10   GLN A O   1 
ATOM   86   C  CB  . GLN A 1 10  ? 27.455  29.579  24.033  1.00 25.13 ? 10   GLN A CB  1 
ATOM   87   C  CG  . GLN A 1 10  ? 27.287  29.569  25.541  1.00 29.78 ? 10   GLN A CG  1 
ATOM   88   C  CD  . GLN A 1 10  ? 28.445  30.230  26.268  1.00 32.16 ? 10   GLN A CD  1 
ATOM   89   O  OE1 . GLN A 1 10  ? 28.582  30.094  27.491  1.00 34.24 ? 10   GLN A OE1 1 
ATOM   90   N  NE2 . GLN A 1 10  ? 29.289  30.952  25.525  1.00 33.55 ? 10   GLN A NE2 1 
ATOM   91   N  N   . LEU A 1 11  ? 27.795  28.375  21.151  1.00 19.85 ? 11   LEU A N   1 
ATOM   92   C  CA  . LEU A 1 11  ? 27.858  28.573  19.716  1.00 21.53 ? 11   LEU A CA  1 
ATOM   93   C  C   . LEU A 1 11  ? 26.834  27.717  18.963  1.00 22.91 ? 11   LEU A C   1 
ATOM   94   O  O   . LEU A 1 11  ? 26.183  28.166  17.994  1.00 23.75 ? 11   LEU A O   1 
ATOM   95   C  CB  . LEU A 1 11  ? 29.278  28.245  19.217  1.00 19.99 ? 11   LEU A CB  1 
ATOM   96   C  CG  . LEU A 1 11  ? 30.332  29.273  19.609  1.00 19.99 ? 11   LEU A CG  1 
ATOM   97   C  CD1 . LEU A 1 11  ? 31.713  28.686  19.170  1.00 19.81 ? 11   LEU A CD1 1 
ATOM   98   C  CD2 . LEU A 1 11  ? 30.104  30.600  18.877  1.00 22.28 ? 11   LEU A CD2 1 
ATOM   99   N  N   . ASN A 1 12  ? 26.692  26.472  19.385  1.00 25.04 ? 12   ASN A N   1 
ATOM   100  C  CA  . ASN A 1 12  ? 25.751  25.589  18.707  1.00 27.91 ? 12   ASN A CA  1 
ATOM   101  C  C   . ASN A 1 12  ? 24.337  26.154  18.872  1.00 29.36 ? 12   ASN A C   1 
ATOM   102  O  O   . ASN A 1 12  ? 23.519  26.093  17.951  1.00 29.85 ? 12   ASN A O   1 
ATOM   103  C  CB  . ASN A 1 12  ? 25.862  24.189  19.291  1.00 28.21 ? 12   ASN A CB  1 
ATOM   104  C  CG  . ASN A 1 12  ? 24.926  23.213  18.623  1.00 31.21 ? 12   ASN A CG  1 
ATOM   105  O  OD1 . ASN A 1 12  ? 25.047  22.943  17.419  1.00 31.16 ? 12   ASN A OD1 1 
ATOM   106  N  ND2 . ASN A 1 12  ? 23.977  22.678  19.401  1.00 32.79 ? 12   ASN A ND2 1 
ATOM   107  N  N   . ASP A 1 13  ? 24.056  26.757  20.021  1.00 30.99 ? 13   ASP A N   1 
ATOM   108  C  CA  . ASP A 1 13  ? 22.721  27.327  20.226  1.00 32.92 ? 13   ASP A CA  1 
ATOM   109  C  C   . ASP A 1 13  ? 22.446  28.474  19.281  1.00 33.50 ? 13   ASP A C   1 
ATOM   110  O  O   . ASP A 1 13  ? 21.279  28.810  19.002  1.00 33.58 ? 13   ASP A O   1 
ATOM   111  C  CB  . ASP A 1 13  ? 22.537  27.799  21.664  1.00 35.65 ? 13   ASP A CB  1 
ATOM   112  C  CG  . ASP A 1 13  ? 22.416  26.654  22.620  1.00 38.36 ? 13   ASP A CG  1 
ATOM   113  O  OD1 . ASP A 1 13  ? 22.044  25.544  22.151  1.00 41.35 ? 13   ASP A OD1 1 
ATOM   114  O  OD2 . ASP A 1 13  ? 22.687  26.852  23.838  1.00 40.89 ? 13   ASP A OD2 1 
ATOM   115  N  N   . ARG A 1 14  ? 23.503  29.111  18.797  1.00 32.46 ? 14   ARG A N   1 
ATOM   116  C  CA  . ARG A 1 14  ? 23.336  30.204  17.865  1.00 32.12 ? 14   ARG A CA  1 
ATOM   117  C  C   . ARG A 1 14  ? 23.659  29.764  16.451  1.00 30.97 ? 14   ARG A C   1 
ATOM   118  O  O   . ARG A 1 14  ? 23.747  30.615  15.572  1.00 32.99 ? 14   ARG A O   1 
ATOM   119  C  CB  . ARG A 1 14  ? 24.234  31.371  18.233  1.00 33.05 ? 14   ARG A CB  1 
ATOM   120  C  CG  . ARG A 1 14  ? 23.958  31.917  19.602  1.00 35.75 ? 14   ARG A CG  1 
ATOM   121  C  CD  . ARG A 1 14  ? 24.737  33.165  19.799  1.00 38.98 ? 14   ARG A CD  1 
ATOM   122  N  NE  . ARG A 1 14  ? 26.139  32.866  19.990  1.00 41.35 ? 14   ARG A NE  1 
ATOM   123  C  CZ  . ARG A 1 14  ? 27.085  33.786  20.095  1.00 42.68 ? 14   ARG A CZ  1 
ATOM   124  N  NH1 . ARG A 1 14  ? 26.757  35.078  20.010  1.00 44.32 ? 14   ARG A NH1 1 
ATOM   125  N  NH2 . ARG A 1 14  ? 28.344  33.413  20.319  1.00 43.08 ? 14   ARG A NH2 1 
ATOM   126  N  N   . ARG A 1 15  ? 23.816  28.458  16.223  1.00 29.70 ? 15   ARG A N   1 
ATOM   127  C  CA  . ARG A 1 15  ? 24.164  27.962  14.876  1.00 29.01 ? 15   ARG A CA  1 
ATOM   128  C  C   . ARG A 1 15  ? 25.378  28.766  14.348  1.00 27.96 ? 15   ARG A C   1 
ATOM   129  O  O   . ARG A 1 15  ? 25.372  29.333  13.239  1.00 28.03 ? 15   ARG A O   1 
ATOM   130  C  CB  . ARG A 1 15  ? 22.941  28.112  13.904  1.00 28.92 ? 15   ARG A CB  1 
ATOM   131  N  N   . GLU A 1 16  ? 26.431  28.823  15.173  1.00 25.42 ? 16   GLU A N   1 
ATOM   132  C  CA  . GLU A 1 16  ? 27.632  29.565  14.827  1.00 23.49 ? 16   GLU A CA  1 
ATOM   133  C  C   . GLU A 1 16  ? 28.855  28.684  14.972  1.00 21.71 ? 16   GLU A C   1 
ATOM   134  O  O   . GLU A 1 16  ? 28.881  27.757  15.790  1.00 21.17 ? 16   GLU A O   1 
ATOM   135  C  CB  . GLU A 1 16  ? 27.864  30.759  15.775  1.00 25.28 ? 16   GLU A CB  1 
ATOM   136  C  CG  . GLU A 1 16  ? 27.424  32.090  15.292  1.00 28.93 ? 16   GLU A CG  1 
ATOM   137  C  CD  . GLU A 1 16  ? 27.532  33.134  16.395  1.00 29.40 ? 16   GLU A CD  1 
ATOM   138  O  OE1 . GLU A 1 16  ? 28.605  33.261  17.053  1.00 25.99 ? 16   GLU A OE1 1 
ATOM   139  O  OE2 . GLU A 1 16  ? 26.525  33.852  16.602  1.00 32.40 ? 16   GLU A OE2 1 
ATOM   140  N  N   . GLY A 1 17  ? 29.859  29.007  14.182  1.00 18.91 ? 17   GLY A N   1 
ATOM   141  C  CA  . GLY A 1 17  ? 31.139  28.319  14.290  1.00 18.87 ? 17   GLY A CA  1 
ATOM   142  C  C   . GLY A 1 17  ? 32.015  29.255  15.124  1.00 17.42 ? 17   GLY A C   1 
ATOM   143  O  O   . GLY A 1 17  ? 31.689  30.412  15.361  1.00 17.33 ? 17   GLY A O   1 
ATOM   144  N  N   . ALA A 1 18  ? 33.107  28.706  15.633  1.00 16.42 ? 18   ALA A N   1 
ATOM   145  C  CA  . ALA A 1 18  ? 34.034  29.507  16.415  1.00 15.79 ? 18   ALA A CA  1 
ATOM   146  C  C   . ALA A 1 18  ? 35.072  30.078  15.457  1.00 14.98 ? 18   ALA A C   1 
ATOM   147  O  O   . ALA A 1 18  ? 35.449  29.452  14.462  1.00 16.19 ? 18   ALA A O   1 
ATOM   148  C  CB  . ALA A 1 18  ? 34.747  28.604  17.446  1.00 14.38 ? 18   ALA A CB  1 
ATOM   149  N  N   . PHE A 1 19  ? 35.528  31.291  15.753  1.00 14.31 ? 19   PHE A N   1 
ATOM   150  C  CA  . PHE A 1 19  ? 36.661  31.861  15.035  1.00 13.92 ? 19   PHE A CA  1 
ATOM   151  C  C   . PHE A 1 19  ? 37.738  32.067  16.084  1.00 14.18 ? 19   PHE A C   1 
ATOM   152  O  O   . PHE A 1 19  ? 37.530  32.772  17.076  1.00 14.20 ? 19   PHE A O   1 
ATOM   153  C  CB  . PHE A 1 19  ? 36.366  33.203  14.377  1.00 15.04 ? 19   PHE A CB  1 
ATOM   154  C  CG  . PHE A 1 19  ? 37.601  33.849  13.817  1.00 14.42 ? 19   PHE A CG  1 
ATOM   155  C  CD1 . PHE A 1 19  ? 38.357  33.192  12.849  1.00 15.41 ? 19   PHE A CD1 1 
ATOM   156  C  CD2 . PHE A 1 19  ? 38.067  35.056  14.325  1.00 15.15 ? 19   PHE A CD2 1 
ATOM   157  C  CE1 . PHE A 1 19  ? 39.566  33.721  12.399  1.00 15.33 ? 19   PHE A CE1 1 
ATOM   158  C  CE2 . PHE A 1 19  ? 39.276  35.596  13.883  1.00 16.11 ? 19   PHE A CE2 1 
ATOM   159  C  CZ  . PHE A 1 19  ? 40.027  34.926  12.919  1.00 15.41 ? 19   PHE A CZ  1 
ATOM   160  N  N   . VAL A 1 20  ? 38.922  31.518  15.820  1.00 11.74 ? 20   VAL A N   1 
ATOM   161  C  CA  . VAL A 1 20  ? 39.979  31.585  16.844  1.00 11.76 ? 20   VAL A CA  1 
ATOM   162  C  C   . VAL A 1 20  ? 41.284  32.089  16.243  1.00 11.75 ? 20   VAL A C   1 
ATOM   163  O  O   . VAL A 1 20  ? 41.886  31.423  15.388  1.00 12.35 ? 20   VAL A O   1 
ATOM   164  C  CB  . VAL A 1 20  ? 40.262  30.141  17.331  1.00 10.77 ? 20   VAL A CB  1 
ATOM   165  C  CG1 . VAL A 1 20  ? 41.353  30.144  18.432  1.00 11.47 ? 20   VAL A CG1 1 
ATOM   166  C  CG2 . VAL A 1 20  ? 38.992  29.505  17.841  1.00 12.91 ? 20   VAL A CG2 1 
ATOM   167  N  N   . PRO A 1 21  ? 41.724  33.281  16.598  1.00 12.11 ? 21   PRO A N   1 
ATOM   168  C  CA  . PRO A 1 21  ? 42.977  33.820  16.100  1.00 11.87 ? 21   PRO A CA  1 
ATOM   169  C  C   . PRO A 1 21  ? 44.157  33.292  16.926  1.00 12.04 ? 21   PRO A C   1 
ATOM   170  O  O   . PRO A 1 21  ? 44.006  32.978  18.116  1.00 10.88 ? 21   PRO A O   1 
ATOM   171  C  CB  . PRO A 1 21  ? 42.789  35.346  16.292  1.00 12.41 ? 21   PRO A CB  1 
ATOM   172  C  CG  . PRO A 1 21  ? 41.944  35.428  17.500  1.00 12.50 ? 21   PRO A CG  1 
ATOM   173  C  CD  . PRO A 1 21  ? 40.953  34.275  17.368  1.00 12.04 ? 21   PRO A CD  1 
ATOM   174  N  N   . PHE A 1 22  ? 45.314  33.289  16.276  1.00 13.61 ? 22   PHE A N   1 
ATOM   175  C  CA  . PHE A 1 22  ? 46.544  32.899  16.945  1.00 13.12 ? 22   PHE A CA  1 
ATOM   176  C  C   . PHE A 1 22  ? 47.572  34.008  16.808  1.00 13.47 ? 22   PHE A C   1 
ATOM   177  O  O   . PHE A 1 22  ? 47.685  34.637  15.753  1.00 14.72 ? 22   PHE A O   1 
ATOM   178  C  CB  . PHE A 1 22  ? 47.139  31.613  16.349  1.00 14.30 ? 22   PHE A CB  1 
ATOM   179  C  CG  . PHE A 1 22  ? 48.611  31.421  16.666  1.00 13.44 ? 22   PHE A CG  1 
ATOM   180  C  CD1 . PHE A 1 22  ? 49.594  32.113  15.955  1.00 14.90 ? 22   PHE A CD1 1 
ATOM   181  C  CD2 . PHE A 1 22  ? 49.008  30.596  17.711  1.00 13.72 ? 22   PHE A CD2 1 
ATOM   182  C  CE1 . PHE A 1 22  ? 50.947  31.985  16.285  1.00 15.13 ? 22   PHE A CE1 1 
ATOM   183  C  CE2 . PHE A 1 22  ? 50.357  30.460  18.049  1.00 13.64 ? 22   PHE A CE2 1 
ATOM   184  C  CZ  . PHE A 1 22  ? 51.328  31.156  17.337  1.00 14.91 ? 22   PHE A CZ  1 
ATOM   185  N  N   . VAL A 1 23  ? 48.232  34.270  17.925  1.00 11.96 ? 23   VAL A N   1 
ATOM   186  C  CA  . VAL A 1 23  ? 49.373  35.194  17.929  1.00 11.75 ? 23   VAL A CA  1 
ATOM   187  C  C   . VAL A 1 23  ? 50.459  34.649  18.832  1.00 12.97 ? 23   VAL A C   1 
ATOM   188  O  O   . VAL A 1 23  ? 50.206  33.789  19.716  1.00 11.79 ? 23   VAL A O   1 
ATOM   189  C  CB  . VAL A 1 23  ? 49.047  36.676  18.434  1.00 12.95 ? 23   VAL A CB  1 
ATOM   190  C  CG1 . VAL A 1 23  ? 48.089  37.372  17.458  1.00 14.88 ? 23   VAL A CG1 1 
ATOM   191  C  CG2 . VAL A 1 23  ? 48.589  36.653  19.888  1.00 14.55 ? 23   VAL A CG2 1 
ATOM   192  N  N   . THR A 1 24  ? 51.685  35.132  18.615  1.00 11.84 ? 24   THR A N   1 
ATOM   193  C  CA  . THR A 1 24  ? 52.803  34.834  19.485  1.00 12.60 ? 24   THR A CA  1 
ATOM   194  C  C   . THR A 1 24  ? 52.808  35.828  20.640  1.00 12.47 ? 24   THR A C   1 
ATOM   195  O  O   . THR A 1 24  ? 52.740  37.071  20.456  1.00 14.54 ? 24   THR A O   1 
ATOM   196  C  CB  . THR A 1 24  ? 54.152  34.901  18.736  1.00 13.04 ? 24   THR A CB  1 
ATOM   197  O  OG1 . THR A 1 24  ? 54.161  33.913  17.681  1.00 14.60 ? 24   THR A OG1 1 
ATOM   198  C  CG2 . THR A 1 24  ? 55.313  34.740  19.683  1.00 14.98 ? 24   THR A CG2 1 
ATOM   199  N  N   . LEU A 1 25  ? 52.810  35.311  21.862  1.00 12.44 ? 25   LEU A N   1 
ATOM   200  C  CA  . LEU A 1 25  ? 52.851  36.159  23.059  1.00 12.89 ? 25   LEU A CA  1 
ATOM   201  C  C   . LEU A 1 25  ? 54.072  37.046  23.063  1.00 14.41 ? 25   LEU A C   1 
ATOM   202  O  O   . LEU A 1 25  ? 55.183  36.581  22.867  1.00 14.45 ? 25   LEU A O   1 
ATOM   203  C  CB  . LEU A 1 25  ? 52.857  35.335  24.353  1.00 13.29 ? 25   LEU A CB  1 
ATOM   204  C  CG  . LEU A 1 25  ? 51.495  34.682  24.647  1.00 14.63 ? 25   LEU A CG  1 
ATOM   205  C  CD1 . LEU A 1 25  ? 51.667  33.626  25.734  1.00 15.13 ? 25   LEU A CD1 1 
ATOM   206  C  CD2 . LEU A 1 25  ? 50.481  35.736  25.149  1.00 16.70 ? 25   LEU A CD2 1 
ATOM   207  N  N   . GLY A 1 26  ? 53.859  38.355  23.286  1.00 14.70 ? 26   GLY A N   1 
ATOM   208  C  CA  . GLY A 1 26  ? 55.003  39.255  23.369  1.00 15.22 ? 26   GLY A CA  1 
ATOM   209  C  C   . GLY A 1 26  ? 55.476  39.795  22.040  1.00 15.11 ? 26   GLY A C   1 
ATOM   210  O  O   . GLY A 1 26  ? 56.515  40.480  21.977  1.00 16.29 ? 26   GLY A O   1 
ATOM   211  N  N   . ASP A 1 27  ? 54.790  39.462  20.961  1.00 13.43 ? 27   ASP A N   1 
ATOM   212  C  CA  . ASP A 1 27  ? 55.164  39.975  19.663  1.00 15.14 ? 27   ASP A CA  1 
ATOM   213  C  C   . ASP A 1 27  ? 54.244  41.196  19.418  1.00 15.35 ? 27   ASP A C   1 
ATOM   214  O  O   . ASP A 1 27  ? 53.040  41.048  19.301  1.00 15.72 ? 27   ASP A O   1 
ATOM   215  C  CB  . ASP A 1 27  ? 54.909  38.910  18.565  1.00 15.25 ? 27   ASP A CB  1 
ATOM   216  C  CG  . ASP A 1 27  ? 55.003  39.500  17.148  1.00 17.04 ? 27   ASP A CG  1 
ATOM   217  O  OD1 . ASP A 1 27  ? 55.703  40.540  17.010  1.00 17.73 ? 27   ASP A OD1 1 
ATOM   218  O  OD2 . ASP A 1 27  ? 54.387  38.967  16.186  1.00 15.81 ? 27   ASP A OD2 1 
ATOM   219  N  N   . PRO A 1 28  ? 54.811  42.402  19.152  1.00 15.81 ? 28   PRO A N   1 
ATOM   220  C  CA  . PRO A 1 28  ? 56.223  42.817  19.026  1.00 15.56 ? 28   PRO A CA  1 
ATOM   221  C  C   . PRO A 1 28  ? 56.842  43.234  20.356  1.00 16.25 ? 28   PRO A C   1 
ATOM   222  O  O   . PRO A 1 28  ? 58.043  43.528  20.438  1.00 18.03 ? 28   PRO A O   1 
ATOM   223  C  CB  . PRO A 1 28  ? 56.157  43.975  18.002  1.00 15.84 ? 28   PRO A CB  1 
ATOM   224  C  CG  . PRO A 1 28  ? 54.833  44.634  18.334  1.00 15.05 ? 28   PRO A CG  1 
ATOM   225  C  CD  . PRO A 1 28  ? 53.881  43.441  18.671  1.00 14.98 ? 28   PRO A CD  1 
ATOM   226  N  N   . GLY A 1 29  ? 56.018  43.275  21.387  1.00 15.40 ? 29   GLY A N   1 
ATOM   227  C  CA  . GLY A 1 29  ? 56.474  43.581  22.739  1.00 16.33 ? 29   GLY A CA  1 
ATOM   228  C  C   . GLY A 1 29  ? 55.365  43.187  23.704  1.00 18.07 ? 29   GLY A C   1 
ATOM   229  O  O   . GLY A 1 29  ? 54.233  42.952  23.257  1.00 17.51 ? 29   GLY A O   1 
ATOM   230  N  N   . ILE A 1 30  ? 55.666  43.133  25.001  1.00 16.21 ? 30   ILE A N   1 
ATOM   231  C  CA  . ILE A 1 30  ? 54.651  42.715  25.995  1.00 17.36 ? 30   ILE A CA  1 
ATOM   232  C  C   . ILE A 1 30  ? 53.413  43.623  25.998  1.00 17.74 ? 30   ILE A C   1 
ATOM   233  O  O   . ILE A 1 30  ? 52.296  43.148  25.802  1.00 15.89 ? 30   ILE A O   1 
ATOM   234  C  CB  . ILE A 1 30  ? 55.260  42.585  27.406  1.00 18.05 ? 30   ILE A CB  1 
ATOM   235  C  CG1 . ILE A 1 30  ? 56.335  41.468  27.404  1.00 20.91 ? 30   ILE A CG1 1 
ATOM   236  C  CG2 . ILE A 1 30  ? 54.129  42.282  28.433  1.00 19.40 ? 30   ILE A CG2 1 
ATOM   237  C  CD1 . ILE A 1 30  ? 57.051  41.250  28.716  1.00 22.91 ? 30   ILE A CD1 1 
ATOM   238  N  N   . GLU A 1 31  ? 53.607  44.945  26.143  1.00 18.70 ? 31   GLU A N   1 
ATOM   239  C  CA  . GLU A 1 31  ? 52.468  45.848  26.182  1.00 19.86 ? 31   GLU A CA  1 
ATOM   240  C  C   . GLU A 1 31  ? 51.618  45.843  24.898  1.00 17.11 ? 31   GLU A C   1 
ATOM   241  O  O   . GLU A 1 31  ? 50.391  45.826  24.941  1.00 16.28 ? 31   GLU A O   1 
ATOM   242  C  CB  . GLU A 1 31  ? 52.984  47.281  26.475  1.00 23.44 ? 31   GLU A CB  1 
ATOM   243  C  CG  A GLU A 1 31  ? 51.949  48.417  26.353  0.50 25.33 ? 31   GLU A CG  1 
ATOM   244  C  CG  B GLU A 1 31  ? 53.679  47.413  27.839  0.50 25.70 ? 31   GLU A CG  1 
ATOM   245  C  CD  A GLU A 1 31  ? 52.509  49.781  26.774  0.50 27.32 ? 31   GLU A CD  1 
ATOM   246  C  CD  B GLU A 1 31  ? 54.281  48.807  28.074  0.50 28.44 ? 31   GLU A CD  1 
ATOM   247  O  OE1 A GLU A 1 31  ? 53.493  50.236  26.165  0.50 29.33 ? 31   GLU A OE1 1 
ATOM   248  O  OE1 B GLU A 1 31  ? 54.996  49.330  27.179  0.50 30.59 ? 31   GLU A OE1 1 
ATOM   249  O  OE2 A GLU A 1 31  ? 51.964  50.394  27.716  0.50 29.57 ? 31   GLU A OE2 1 
ATOM   250  O  OE2 B GLU A 1 31  ? 54.053  49.379  29.167  0.50 30.57 ? 31   GLU A OE2 1 
ATOM   251  N  N   . GLN A 1 32  ? 52.265  45.862  23.748  1.00 15.72 ? 32   GLN A N   1 
ATOM   252  C  CA  . GLN A 1 32  ? 51.533  45.881  22.496  1.00 16.48 ? 32   GLN A CA  1 
ATOM   253  C  C   . GLN A 1 32  ? 50.825  44.544  22.295  1.00 14.22 ? 32   GLN A C   1 
ATOM   254  O  O   . GLN A 1 32  ? 49.735  44.541  21.785  1.00 14.24 ? 32   GLN A O   1 
ATOM   255  C  CB  . GLN A 1 32  ? 52.455  46.236  21.298  1.00 17.91 ? 32   GLN A CB  1 
ATOM   256  C  CG  . GLN A 1 32  ? 51.744  46.345  19.891  1.00 21.67 ? 32   GLN A CG  1 
ATOM   257  C  CD  . GLN A 1 32  ? 50.715  47.480  19.736  1.00 23.94 ? 32   GLN A CD  1 
ATOM   258  O  OE1 . GLN A 1 32  ? 50.585  48.360  20.587  1.00 25.29 ? 32   GLN A OE1 1 
ATOM   259  N  NE2 . GLN A 1 32  ? 49.989  47.465  18.617  1.00 23.80 ? 32   GLN A NE2 1 
ATOM   260  N  N   . SER A 1 33  ? 51.481  43.441  22.681  1.00 14.70 ? 33   SER A N   1 
ATOM   261  C  CA  . SER A 1 33  ? 50.847  42.129  22.530  1.00 14.04 ? 33   SER A CA  1 
ATOM   262  C  C   . SER A 1 33  ? 49.592  42.085  23.396  1.00 12.82 ? 33   SER A C   1 
ATOM   263  O  O   . SER A 1 33  ? 48.551  41.567  22.961  1.00 13.34 ? 33   SER A O   1 
ATOM   264  C  CB  . SER A 1 33  ? 51.860  41.035  22.896  1.00 14.33 ? 33   SER A CB  1 
ATOM   265  O  OG  . SER A 1 33  ? 51.291  39.721  22.787  1.00 14.47 ? 33   SER A OG  1 
ATOM   266  N  N   . LEU A 1 34  ? 49.656  42.620  24.613  1.00 13.19 ? 34   LEU A N   1 
ATOM   267  C  CA  . LEU A 1 34  ? 48.453  42.644  25.460  1.00 14.82 ? 34   LEU A CA  1 
ATOM   268  C  C   . LEU A 1 34  ? 47.332  43.460  24.780  1.00 15.52 ? 34   LEU A C   1 
ATOM   269  O  O   . LEU A 1 34  ? 46.161  43.089  24.825  1.00 15.12 ? 34   LEU A O   1 
ATOM   270  C  CB  . LEU A 1 34  ? 48.757  43.195  26.875  1.00 14.91 ? 34   LEU A CB  1 
ATOM   271  C  CG  . LEU A 1 34  ? 49.573  42.244  27.758  1.00 16.11 ? 34   LEU A CG  1 
ATOM   272  C  CD1 . LEU A 1 34  ? 50.059  42.961  28.991  1.00 17.02 ? 34   LEU A CD1 1 
ATOM   273  C  CD2 . LEU A 1 34  ? 48.764  41.011  28.156  1.00 16.47 ? 34   LEU A CD2 1 
ATOM   274  N  N   . LYS A 1 35  ? 47.698  44.557  24.100  1.00 15.72 ? 35   LYS A N   1 
ATOM   275  C  CA  . LYS A 1 35  ? 46.711  45.371  23.391  1.00 16.90 ? 35   LYS A CA  1 
ATOM   276  C  C   . LYS A 1 35  ? 46.154  44.654  22.170  1.00 14.07 ? 35   LYS A C   1 
ATOM   277  O  O   . LYS A 1 35  ? 44.964  44.715  21.895  1.00 15.63 ? 35   LYS A O   1 
ATOM   278  C  CB  . LYS A 1 35  ? 47.331  46.699  22.973  1.00 17.84 ? 35   LYS A CB  1 
ATOM   279  C  CG  . LYS A 1 35  ? 47.613  47.586  24.142  1.00 20.22 ? 35   LYS A CG  1 
ATOM   280  C  CD  . LYS A 1 35  ? 48.188  48.924  23.610  1.00 24.78 ? 35   LYS A CD  1 
ATOM   281  C  CE  . LYS A 1 35  ? 48.716  49.772  24.759  1.00 25.89 ? 35   LYS A CE  1 
ATOM   282  N  NZ  . LYS A 1 35  ? 49.374  50.987  24.217  1.00 29.38 ? 35   LYS A NZ  1 
ATOM   283  N  N   . ILE A 1 36  ? 47.026  43.958  21.450  1.00 14.70 ? 36   ILE A N   1 
ATOM   284  C  CA  . ILE A 1 36  ? 46.609  43.174  20.288  1.00 14.98 ? 36   ILE A CA  1 
ATOM   285  C  C   . ILE A 1 36  ? 45.581  42.132  20.741  1.00 14.78 ? 36   ILE A C   1 
ATOM   286  O  O   . ILE A 1 36  ? 44.530  41.961  20.141  1.00 14.35 ? 36   ILE A O   1 
ATOM   287  C  CB  . ILE A 1 36  ? 47.842  42.456  19.691  1.00 14.09 ? 36   ILE A CB  1 
ATOM   288  C  CG1 . ILE A 1 36  ? 48.724  43.494  18.942  1.00 16.10 ? 36   ILE A CG1 1 
ATOM   289  C  CG2 . ILE A 1 36  ? 47.429  41.277  18.770  1.00 15.45 ? 36   ILE A CG2 1 
ATOM   290  C  CD1 . ILE A 1 36  ? 50.127  42.988  18.658  1.00 14.66 ? 36   ILE A CD1 1 
ATOM   291  N  N   . ILE A 1 37  ? 45.893  41.435  21.835  1.00 14.30 ? 37   ILE A N   1 
ATOM   292  C  CA  . ILE A 1 37  ? 44.981  40.399  22.281  1.00 14.20 ? 37   ILE A CA  1 
ATOM   293  C  C   . ILE A 1 37  ? 43.600  40.970  22.714  1.00 13.44 ? 37   ILE A C   1 
ATOM   294  O  O   . ILE A 1 37  ? 42.574  40.401  22.375  1.00 13.57 ? 37   ILE A O   1 
ATOM   295  C  CB  . ILE A 1 37  ? 45.681  39.577  23.372  1.00 12.94 ? 37   ILE A CB  1 
ATOM   296  C  CG1 . ILE A 1 37  ? 46.796  38.702  22.737  1.00 13.62 ? 37   ILE A CG1 1 
ATOM   297  C  CG2 . ILE A 1 37  ? 44.665  38.682  24.152  1.00 13.75 ? 37   ILE A CG2 1 
ATOM   298  C  CD1 . ILE A 1 37  ? 47.839  38.151  23.758  1.00 15.29 ? 37   ILE A CD1 1 
ATOM   299  N  N   . ASP A 1 38  ? 43.578  42.107  23.419  1.00 14.37 ? 38   ASP A N   1 
ATOM   300  C  CA  . ASP A 1 38  ? 42.285  42.669  23.785  1.00 14.87 ? 38   ASP A CA  1 
ATOM   301  C  C   . ASP A 1 38  ? 41.480  43.087  22.537  1.00 14.62 ? 38   ASP A C   1 
ATOM   302  O  O   . ASP A 1 38  ? 40.246  42.989  22.518  1.00 15.78 ? 38   ASP A O   1 
ATOM   303  C  CB  . ASP A 1 38  ? 42.474  43.877  24.699  1.00 15.91 ? 38   ASP A CB  1 
ATOM   304  C  CG  . ASP A 1 38  ? 42.818  43.486  26.141  1.00 19.26 ? 38   ASP A CG  1 
ATOM   305  O  OD1 . ASP A 1 38  ? 42.702  42.283  26.515  1.00 18.17 ? 38   ASP A OD1 1 
ATOM   306  O  OD2 . ASP A 1 38  ? 43.232  44.365  26.938  1.00 18.91 ? 38   ASP A OD2 1 
ATOM   307  N  N   . THR A 1 39  ? 42.171  43.543  21.493  1.00 14.98 ? 39   THR A N   1 
ATOM   308  C  CA  . THR A 1 39  ? 41.515  43.951  20.246  1.00 16.67 ? 39   THR A CA  1 
ATOM   309  C  C   . THR A 1 39  ? 40.935  42.713  19.578  1.00 15.63 ? 39   THR A C   1 
ATOM   310  O  O   . THR A 1 39  ? 39.839  42.759  19.041  1.00 16.65 ? 39   THR A O   1 
ATOM   311  C  CB  . THR A 1 39  ? 42.516  44.632  19.289  1.00 19.48 ? 39   THR A CB  1 
ATOM   312  O  OG1 . THR A 1 39  ? 43.033  45.814  19.916  1.00 20.66 ? 39   THR A OG1 1 
ATOM   313  C  CG2 . THR A 1 39  ? 41.848  44.998  17.985  1.00 19.60 ? 39   THR A CG2 1 
ATOM   314  N  N   . LEU A 1 40  ? 41.702  41.606  19.591  1.00 14.33 ? 40   LEU A N   1 
ATOM   315  C  CA  . LEU A 1 40  ? 41.168  40.407  18.957  1.00 15.26 ? 40   LEU A CA  1 
ATOM   316  C  C   . LEU A 1 40  ? 39.897  39.992  19.655  1.00 14.55 ? 40   LEU A C   1 
ATOM   317  O  O   . LEU A 1 40  ? 38.960  39.554  18.985  1.00 15.37 ? 40   LEU A O   1 
ATOM   318  C  CB  . LEU A 1 40  ? 42.162  39.253  19.054  1.00 16.11 ? 40   LEU A CB  1 
ATOM   319  C  CG  . LEU A 1 40  ? 43.569  39.458  18.476  1.00 18.16 ? 40   LEU A CG  1 
ATOM   320  C  CD1 . LEU A 1 40  ? 44.449  38.245  18.813  1.00 19.05 ? 40   LEU A CD1 1 
ATOM   321  C  CD2 . LEU A 1 40  ? 43.490  39.631  16.986  1.00 18.36 ? 40   LEU A CD2 1 
ATOM   322  N  N   . ILE A 1 41  ? 39.876  40.067  20.996  1.00 14.32 ? 41   ILE A N   1 
ATOM   323  C  CA  . ILE A 1 41  ? 38.698  39.660  21.742  1.00 14.45 ? 41   ILE A CA  1 
ATOM   324  C  C   . ILE A 1 41  ? 37.527  40.629  21.453  1.00 14.71 ? 41   ILE A C   1 
ATOM   325  O  O   . ILE A 1 41  ? 36.406  40.220  21.190  1.00 15.88 ? 41   ILE A O   1 
ATOM   326  C  CB  . ILE A 1 41  ? 39.021  39.619  23.235  1.00 15.60 ? 41   ILE A CB  1 
ATOM   327  C  CG1 . ILE A 1 41  ? 39.998  38.470  23.495  1.00 14.55 ? 41   ILE A CG1 1 
ATOM   328  C  CG2 . ILE A 1 41  ? 37.759  39.403  24.063  1.00 15.95 ? 41   ILE A CG2 1 
ATOM   329  C  CD1 . ILE A 1 41  ? 40.608  38.420  24.911  1.00 14.61 ? 41   ILE A CD1 1 
ATOM   330  N  N   . ASP A 1 42  ? 37.825  41.914  21.496  1.00 17.15 ? 42   ASP A N   1 
ATOM   331  C  CA  . ASP A 1 42  ? 36.741  42.871  21.292  1.00 18.86 ? 42   ASP A CA  1 
ATOM   332  C  C   . ASP A 1 42  ? 36.147  42.831  19.899  1.00 19.05 ? 42   ASP A C   1 
ATOM   333  O  O   . ASP A 1 42  ? 34.959  43.164  19.701  1.00 20.93 ? 42   ASP A O   1 
ATOM   334  C  CB  . ASP A 1 42  ? 37.242  44.277  21.615  1.00 19.07 ? 42   ASP A CB  1 
ATOM   335  C  CG  . ASP A 1 42  ? 36.086  45.261  21.811  1.00 22.66 ? 42   ASP A CG  1 
ATOM   336  O  OD1 . ASP A 1 42  ? 35.303  45.060  22.782  1.00 24.71 ? 42   ASP A OD1 1 
ATOM   337  O  OD2 . ASP A 1 42  ? 35.972  46.219  21.012  1.00 24.78 ? 42   ASP A OD2 1 
ATOM   338  N  N   . ALA A 1 43  ? 36.942  42.403  18.927  1.00 18.00 ? 43   ALA A N   1 
ATOM   339  C  CA  . ALA A 1 43  ? 36.515  42.287  17.560  1.00 17.53 ? 43   ALA A CA  1 
ATOM   340  C  C   . ALA A 1 43  ? 35.721  41.006  17.274  1.00 18.56 ? 43   ALA A C   1 
ATOM   341  O  O   . ALA A 1 43  ? 35.178  40.863  16.178  1.00 19.94 ? 43   ALA A O   1 
ATOM   342  C  CB  . ALA A 1 43  ? 37.723  42.388  16.608  1.00 19.69 ? 43   ALA A CB  1 
ATOM   343  N  N   . GLY A 1 44  ? 35.668  40.100  18.256  1.00 17.11 ? 44   GLY A N   1 
ATOM   344  C  CA  . GLY A 1 44  ? 34.867  38.896  18.072  1.00 17.12 ? 44   GLY A CA  1 
ATOM   345  C  C   . GLY A 1 44  ? 35.520  37.522  18.206  1.00 17.31 ? 44   GLY A C   1 
ATOM   346  O  O   . GLY A 1 44  ? 34.848  36.517  17.938  1.00 18.04 ? 44   GLY A O   1 
ATOM   347  N  N   . ALA A 1 45  ? 36.762  37.451  18.641  1.00 15.69 ? 45   ALA A N   1 
ATOM   348  C  CA  . ALA A 1 45  ? 37.399  36.120  18.777  1.00 15.20 ? 45   ALA A CA  1 
ATOM   349  C  C   . ALA A 1 45  ? 36.601  35.314  19.780  1.00 15.48 ? 45   ALA A C   1 
ATOM   350  O  O   . ALA A 1 45  ? 36.274  35.857  20.853  1.00 16.37 ? 45   ALA A O   1 
ATOM   351  C  CB  . ALA A 1 45  ? 38.840  36.306  19.284  1.00 15.07 ? 45   ALA A CB  1 
ATOM   352  N  N   . ASP A 1 46  ? 36.316  34.043  19.469  1.00 13.31 ? 46   ASP A N   1 
ATOM   353  C  CA  . ASP A 1 46  ? 35.570  33.189  20.387  1.00 14.53 ? 46   ASP A CA  1 
ATOM   354  C  C   . ASP A 1 46  ? 36.518  32.502  21.385  1.00 13.59 ? 46   ASP A C   1 
ATOM   355  O  O   . ASP A 1 46  ? 36.095  32.113  22.476  1.00 13.91 ? 46   ASP A O   1 
ATOM   356  C  CB  . ASP A 1 46  ? 34.816  32.123  19.609  1.00 15.16 ? 46   ASP A CB  1 
ATOM   357  C  CG  . ASP A 1 46  ? 33.651  32.711  18.815  1.00 15.75 ? 46   ASP A CG  1 
ATOM   358  O  OD1 . ASP A 1 46  ? 33.650  32.549  17.592  1.00 14.92 ? 46   ASP A OD1 1 
ATOM   359  O  OD2 . ASP A 1 46  ? 32.765  33.358  19.472  1.00 19.30 ? 46   ASP A OD2 1 
ATOM   360  N  N   . ALA A 1 47  ? 37.789  32.322  20.966  1.00 13.79 ? 47   ALA A N   1 
ATOM   361  C  CA  . ALA A 1 47  ? 38.828  31.700  21.807  1.00 11.77 ? 47   ALA A CA  1 
ATOM   362  C  C   . ALA A 1 47  ? 40.158  32.202  21.308  1.00 11.18 ? 47   ALA A C   1 
ATOM   363  O  O   . ALA A 1 47  ? 40.214  32.853  20.233  1.00 14.53 ? 47   ALA A O   1 
ATOM   364  C  CB  . ALA A 1 47  ? 38.746  30.146  21.709  1.00 12.96 ? 47   ALA A CB  1 
ATOM   365  N  N   . LEU A 1 48  ? 41.236  31.898  22.038  1.00 11.60 ? 48   LEU A N   1 
ATOM   366  C  CA  . LEU A 1 48  ? 42.551  32.366  21.640  1.00 11.36 ? 48   LEU A CA  1 
ATOM   367  C  C   . LEU A 1 48  ? 43.520  31.216  21.591  1.00 11.19 ? 48   LEU A C   1 
ATOM   368  O  O   . LEU A 1 48  ? 43.392  30.298  22.386  1.00 12.25 ? 48   LEU A O   1 
ATOM   369  C  CB  . LEU A 1 48  ? 43.122  33.339  22.678  1.00 12.38 ? 48   LEU A CB  1 
ATOM   370  C  CG  . LEU A 1 48  ? 42.381  34.673  22.889  1.00 14.32 ? 48   LEU A CG  1 
ATOM   371  C  CD1 . LEU A 1 48  ? 43.011  35.399  24.100  1.00 15.74 ? 48   LEU A CD1 1 
ATOM   372  C  CD2 . LEU A 1 48  ? 42.392  35.534  21.635  1.00 17.01 ? 48   LEU A CD2 1 
ATOM   373  N  N   . GLU A 1 49  ? 44.454  31.263  20.645  1.00 12.04 ? 49   GLU A N   1 
ATOM   374  C  CA  . GLU A 1 49  ? 45.564  30.288  20.644  1.00 10.50 ? 49   GLU A CA  1 
ATOM   375  C  C   . GLU A 1 49  ? 46.801  31.214  20.769  1.00 9.87  ? 49   GLU A C   1 
ATOM   376  O  O   . GLU A 1 49  ? 46.967  32.191  19.988  1.00 12.62 ? 49   GLU A O   1 
ATOM   377  C  CB  . GLU A 1 49  ? 45.607  29.494  19.350  1.00 11.49 ? 49   GLU A CB  1 
ATOM   378  C  CG  . GLU A 1 49  ? 46.652  28.410  19.434  1.00 12.60 ? 49   GLU A CG  1 
ATOM   379  C  CD  . GLU A 1 49  ? 47.021  27.821  18.079  1.00 14.51 ? 49   GLU A CD  1 
ATOM   380  O  OE1 . GLU A 1 49  ? 46.155  27.697  17.217  1.00 15.85 ? 49   GLU A OE1 1 
ATOM   381  O  OE2 . GLU A 1 49  ? 48.214  27.502  17.924  1.00 15.59 ? 49   GLU A OE2 1 
ATOM   382  N  N   . LEU A 1 50  ? 47.678  30.937  21.726  1.00 10.31 ? 50   LEU A N   1 
ATOM   383  C  CA  . LEU A 1 50  ? 48.782  31.829  22.040  1.00 9.38  ? 50   LEU A CA  1 
ATOM   384  C  C   . LEU A 1 50  ? 50.084  31.058  22.091  1.00 11.44 ? 50   LEU A C   1 
ATOM   385  O  O   . LEU A 1 50  ? 50.229  30.081  22.829  1.00 10.95 ? 50   LEU A O   1 
ATOM   386  C  CB  . LEU A 1 50  ? 48.522  32.501  23.412  1.00 9.82  ? 50   LEU A CB  1 
ATOM   387  C  CG  . LEU A 1 50  ? 47.205  33.288  23.435  1.00 10.66 ? 50   LEU A CG  1 
ATOM   388  C  CD1 . LEU A 1 50  ? 46.938  33.760  24.899  1.00 13.24 ? 50   LEU A CD1 1 
ATOM   389  C  CD2 . LEU A 1 50  ? 47.314  34.537  22.442  1.00 12.08 ? 50   LEU A CD2 1 
ATOM   390  N  N   . GLY A 1 51  ? 51.049  31.547  21.314  1.00 11.35 ? 51   GLY A N   1 
ATOM   391  C  CA  . GLY A 1 51  ? 52.346  30.884  21.240  1.00 12.63 ? 51   GLY A CA  1 
ATOM   392  C  C   . GLY A 1 51  ? 53.363  31.416  22.193  1.00 13.50 ? 51   GLY A C   1 
ATOM   393  O  O   . GLY A 1 51  ? 53.496  32.609  22.396  1.00 14.80 ? 51   GLY A O   1 
ATOM   394  N  N   . VAL A 1 52  ? 54.083  30.539  22.856  1.00 12.53 ? 52   VAL A N   1 
ATOM   395  C  CA  . VAL A 1 52  ? 55.189  30.984  23.703  1.00 11.81 ? 52   VAL A CA  1 
ATOM   396  C  C   . VAL A 1 52  ? 56.449  31.017  22.814  1.00 13.12 ? 52   VAL A C   1 
ATOM   397  O  O   . VAL A 1 52  ? 56.767  30.028  22.149  1.00 14.08 ? 52   VAL A O   1 
ATOM   398  C  CB  . VAL A 1 52  ? 55.412  30.011  24.901  1.00 12.59 ? 52   VAL A CB  1 
ATOM   399  C  CG1 . VAL A 1 52  ? 56.715  30.353  25.688  1.00 13.53 ? 52   VAL A CG1 1 
ATOM   400  C  CG2 . VAL A 1 52  ? 54.193  30.151  25.862  1.00 13.27 ? 52   VAL A CG2 1 
ATOM   401  N  N   . PRO A 1 53  ? 57.197  32.140  22.787  1.00 12.35 ? 53   PRO A N   1 
ATOM   402  C  CA  . PRO A 1 53  ? 58.404  32.214  21.925  1.00 11.33 ? 53   PRO A CA  1 
ATOM   403  C  C   . PRO A 1 53  ? 59.388  31.105  22.163  1.00 11.04 ? 53   PRO A C   1 
ATOM   404  O  O   . PRO A 1 53  ? 59.769  30.840  23.295  1.00 11.70 ? 53   PRO A O   1 
ATOM   405  C  CB  . PRO A 1 53  ? 59.011  33.575  22.259  1.00 11.90 ? 53   PRO A CB  1 
ATOM   406  C  CG  . PRO A 1 53  ? 57.777  34.399  22.654  1.00 13.03 ? 53   PRO A CG  1 
ATOM   407  C  CD  . PRO A 1 53  ? 56.935  33.433  23.484  1.00 12.16 ? 53   PRO A CD  1 
ATOM   408  N  N   . PHE A 1 54  ? 59.776  30.460  21.061  1.00 12.23 ? 54   PHE A N   1 
ATOM   409  C  CA  . PHE A 1 54  ? 60.717  29.347  21.114  1.00 13.24 ? 54   PHE A CA  1 
ATOM   410  C  C   . PHE A 1 54  ? 61.800  29.553  20.060  1.00 13.15 ? 54   PHE A C   1 
ATOM   411  O  O   . PHE A 1 54  ? 61.541  30.083  18.980  1.00 14.62 ? 54   PHE A O   1 
ATOM   412  C  CB  . PHE A 1 54  ? 59.984  28.021  20.879  1.00 12.96 ? 54   PHE A CB  1 
ATOM   413  C  CG  . PHE A 1 54  ? 60.868  26.806  20.994  1.00 12.86 ? 54   PHE A CG  1 
ATOM   414  C  CD1 . PHE A 1 54  ? 61.643  26.594  22.129  1.00 13.44 ? 54   PHE A CD1 1 
ATOM   415  C  CD2 . PHE A 1 54  ? 60.909  25.864  19.971  1.00 12.40 ? 54   PHE A CD2 1 
ATOM   416  C  CE1 . PHE A 1 54  ? 62.450  25.459  22.246  1.00 13.29 ? 54   PHE A CE1 1 
ATOM   417  C  CE2 . PHE A 1 54  ? 61.711  24.725  20.078  1.00 12.79 ? 54   PHE A CE2 1 
ATOM   418  C  CZ  . PHE A 1 54  ? 62.481  24.524  21.217  1.00 12.76 ? 54   PHE A CZ  1 
ATOM   419  N  N   . SER A 1 55  ? 63.009  29.100  20.382  1.00 12.05 ? 55   SER A N   1 
ATOM   420  C  CA  . SER A 1 55  ? 64.164  29.282  19.490  1.00 13.42 ? 55   SER A CA  1 
ATOM   421  C  C   . SER A 1 55  ? 64.067  28.534  18.150  1.00 14.83 ? 55   SER A C   1 
ATOM   422  O  O   . SER A 1 55  ? 64.625  28.996  17.139  1.00 14.76 ? 55   SER A O   1 
ATOM   423  C  CB  . SER A 1 55  ? 65.411  28.781  20.205  1.00 12.83 ? 55   SER A CB  1 
ATOM   424  O  OG  . SER A 1 55  ? 65.276  27.400  20.588  1.00 15.01 ? 55   SER A OG  1 
ATOM   425  N  N   . ASP A 1 56  ? 63.364  27.406  18.165  1.00 13.51 ? 56   ASP A N   1 
ATOM   426  C  CA  . ASP A 1 56  ? 63.290  26.519  17.004  1.00 14.40 ? 56   ASP A CA  1 
ATOM   427  C  C   . ASP A 1 56  ? 61.904  26.005  16.681  1.00 14.83 ? 56   ASP A C   1 
ATOM   428  O  O   . ASP A 1 56  ? 61.635  24.810  16.807  1.00 15.30 ? 56   ASP A O   1 
ATOM   429  C  CB  . ASP A 1 56  ? 64.280  25.375  17.276  1.00 14.95 ? 56   ASP A CB  1 
ATOM   430  C  CG  . ASP A 1 56  ? 65.748  25.901  17.357  1.00 17.23 ? 56   ASP A CG  1 
ATOM   431  O  OD1 . ASP A 1 56  ? 66.384  26.091  16.284  1.00 18.00 ? 56   ASP A OD1 1 
ATOM   432  O  OD2 . ASP A 1 56  ? 66.225  26.204  18.460  1.00 16.77 ? 56   ASP A OD2 1 
ATOM   433  N  N   . PRO A 1 57  ? 61.033  26.880  16.162  1.00 14.24 ? 57   PRO A N   1 
ATOM   434  C  CA  . PRO A 1 57  ? 59.624  26.513  15.823  1.00 14.10 ? 57   PRO A CA  1 
ATOM   435  C  C   . PRO A 1 57  ? 59.515  25.740  14.513  1.00 13.66 ? 57   PRO A C   1 
ATOM   436  O  O   . PRO A 1 57  ? 59.154  26.285  13.473  1.00 15.53 ? 57   PRO A O   1 
ATOM   437  C  CB  . PRO A 1 57  ? 58.905  27.875  15.817  1.00 13.53 ? 57   PRO A CB  1 
ATOM   438  C  CG  . PRO A 1 57  ? 60.047  28.837  15.310  1.00 14.16 ? 57   PRO A CG  1 
ATOM   439  C  CD  . PRO A 1 57  ? 61.335  28.313  15.912  1.00 15.39 ? 57   PRO A CD  1 
ATOM   440  N  N   . LEU A 1 58  ? 59.794  24.432  14.608  1.00 15.04 ? 58   LEU A N   1 
ATOM   441  C  CA  . LEU A 1 58  ? 59.890  23.605  13.412  1.00 16.56 ? 58   LEU A CA  1 
ATOM   442  C  C   . LEU A 1 58  ? 58.590  23.220  12.694  1.00 15.89 ? 58   LEU A C   1 
ATOM   443  O  O   . LEU A 1 58  ? 58.655  22.606  11.619  1.00 16.56 ? 58   LEU A O   1 
ATOM   444  C  CB  . LEU A 1 58  ? 60.801  22.400  13.757  1.00 18.71 ? 58   LEU A CB  1 
ATOM   445  C  CG  . LEU A 1 58  ? 60.342  21.460  14.873  1.00 20.96 ? 58   LEU A CG  1 
ATOM   446  C  CD1 . LEU A 1 58  ? 59.211  20.644  14.349  1.00 21.87 ? 58   LEU A CD1 1 
ATOM   447  C  CD2 . LEU A 1 58  ? 61.487  20.537  15.375  1.00 24.42 ? 58   LEU A CD2 1 
ATOM   448  N  N   . ALA A 1 59  ? 57.414  23.615  13.231  1.00 13.96 ? 59   ALA A N   1 
ATOM   449  C  CA  . ALA A 1 59  ? 56.126  23.403  12.513  1.00 13.89 ? 59   ALA A CA  1 
ATOM   450  C  C   . ALA A 1 59  ? 55.634  24.711  11.923  1.00 13.63 ? 59   ALA A C   1 
ATOM   451  O  O   . ALA A 1 59  ? 54.517  24.791  11.403  1.00 14.19 ? 59   ALA A O   1 
ATOM   452  C  CB  . ALA A 1 59  ? 55.037  22.833  13.474  1.00 14.58 ? 59   ALA A CB  1 
ATOM   453  N  N   . ASP A 1 60  ? 56.459  25.759  12.004  1.00 12.88 ? 60   ASP A N   1 
ATOM   454  C  CA  . ASP A 1 60  ? 56.031  27.069  11.503  1.00 14.01 ? 60   ASP A CA  1 
ATOM   455  C  C   . ASP A 1 60  ? 56.736  27.607  10.269  1.00 14.61 ? 60   ASP A C   1 
ATOM   456  O  O   . ASP A 1 60  ? 57.961  27.487  10.142  1.00 14.47 ? 60   ASP A O   1 
ATOM   457  C  CB  . ASP A 1 60  ? 56.197  28.113  12.628  1.00 13.04 ? 60   ASP A CB  1 
ATOM   458  C  CG  . ASP A 1 60  ? 55.150  27.949  13.730  1.00 12.40 ? 60   ASP A CG  1 
ATOM   459  O  OD1 . ASP A 1 60  ? 53.957  28.154  13.383  1.00 12.83 ? 60   ASP A OD1 1 
ATOM   460  O  OD2 . ASP A 1 60  ? 55.516  27.629  14.913  1.00 14.74 ? 60   ASP A OD2 1 
ATOM   461  N  N   . GLY A 1 61  ? 55.941  28.224  9.389   1.00 13.84 ? 61   GLY A N   1 
ATOM   462  C  CA  . GLY A 1 61  ? 56.474  28.898  8.202   1.00 15.27 ? 61   GLY A CA  1 
ATOM   463  C  C   . GLY A 1 61  ? 57.115  30.242  8.585   1.00 15.88 ? 61   GLY A C   1 
ATOM   464  O  O   . GLY A 1 61  ? 57.155  30.655  9.747   1.00 15.48 ? 61   GLY A O   1 
ATOM   465  N  N   . PRO A 1 62  ? 57.622  30.974  7.582   1.00 14.74 ? 62   PRO A N   1 
ATOM   466  C  CA  . PRO A 1 62  ? 58.281  32.248  7.869   1.00 15.37 ? 62   PRO A CA  1 
ATOM   467  C  C   . PRO A 1 62  ? 57.534  33.313  8.664   1.00 14.20 ? 62   PRO A C   1 
ATOM   468  O  O   . PRO A 1 62  ? 58.121  34.047  9.483   1.00 14.84 ? 62   PRO A O   1 
ATOM   469  C  CB  . PRO A 1 62  ? 58.651  32.785  6.472   1.00 16.47 ? 62   PRO A CB  1 
ATOM   470  C  CG  . PRO A 1 62  ? 58.602  31.567  5.589   1.00 19.68 ? 62   PRO A CG  1 
ATOM   471  C  CD  . PRO A 1 62  ? 57.580  30.653  6.143   1.00 16.09 ? 62   PRO A CD  1 
ATOM   472  N  N   . THR A 1 63  ? 56.236  33.418  8.436   1.00 13.74 ? 63   THR A N   1 
ATOM   473  C  CA  . THR A 1 63  ? 55.500  34.467  9.148   1.00 13.64 ? 63   THR A CA  1 
ATOM   474  C  C   . THR A 1 63  ? 55.603  34.273  10.659  1.00 13.50 ? 63   THR A C   1 
ATOM   475  O  O   . THR A 1 63  ? 55.928  35.218  11.405  1.00 14.58 ? 63   THR A O   1 
ATOM   476  C  CB  . THR A 1 63  ? 54.042  34.493  8.709   1.00 14.70 ? 63   THR A CB  1 
ATOM   477  O  OG1 . THR A 1 63  ? 53.990  34.871  7.309   1.00 18.00 ? 63   THR A OG1 1 
ATOM   478  C  CG2 . THR A 1 63  ? 53.239  35.516  9.517   1.00 15.19 ? 63   THR A CG2 1 
ATOM   479  N  N   . ILE A 1 64  ? 55.328  33.050  11.128  1.00 13.66 ? 64   ILE A N   1 
ATOM   480  C  CA  . ILE A 1 64  ? 55.413  32.815  12.570  1.00 14.09 ? 64   ILE A CA  1 
ATOM   481  C  C   . ILE A 1 64  ? 56.886  32.673  13.035  1.00 13.64 ? 64   ILE A C   1 
ATOM   482  O  O   . ILE A 1 64  ? 57.215  33.043  14.162  1.00 13.86 ? 64   ILE A O   1 
ATOM   483  C  CB  . ILE A 1 64  ? 54.451  31.671  12.961  1.00 13.87 ? 64   ILE A CB  1 
ATOM   484  C  CG1 . ILE A 1 64  ? 53.018  32.234  12.890  1.00 15.60 ? 64   ILE A CG1 1 
ATOM   485  C  CG2 . ILE A 1 64  ? 54.655  31.247  14.420  1.00 12.43 ? 64   ILE A CG2 1 
ATOM   486  C  CD1 . ILE A 1 64  ? 51.960  31.109  12.856  1.00 14.72 ? 64   ILE A CD1 1 
ATOM   487  N  N   . GLN A 1 65  ? 57.792  32.225  12.152  1.00 14.01 ? 65   GLN A N   1 
ATOM   488  C  CA  . GLN A 1 65  ? 59.211  32.222  12.565  1.00 14.25 ? 65   GLN A CA  1 
ATOM   489  C  C   . GLN A 1 65  ? 59.580  33.673  12.948  1.00 15.44 ? 65   GLN A C   1 
ATOM   490  O  O   . GLN A 1 65  ? 60.305  33.914  13.935  1.00 15.29 ? 65   GLN A O   1 
ATOM   491  C  CB  . GLN A 1 65  ? 60.122  31.826  11.416  1.00 15.69 ? 65   GLN A CB  1 
ATOM   492  C  CG  . GLN A 1 65  ? 60.123  30.332  11.095  1.00 16.62 ? 65   GLN A CG  1 
ATOM   493  C  CD  . GLN A 1 65  ? 60.688  30.095  9.694   1.00 16.94 ? 65   GLN A CD  1 
ATOM   494  O  OE1 . GLN A 1 65  ? 61.604  30.830  9.230   1.00 17.92 ? 65   GLN A OE1 1 
ATOM   495  N  NE2 . GLN A 1 65  ? 60.146  29.106  8.994   1.00 15.94 ? 65   GLN A NE2 1 
ATOM   496  N  N   . ASN A 1 66  ? 59.153  34.637  12.123  1.00 15.53 ? 66   ASN A N   1 
ATOM   497  C  CA  . ASN A 1 66  ? 59.472  36.034  12.424  1.00 16.85 ? 66   ASN A CA  1 
ATOM   498  C  C   . ASN A 1 66  ? 58.777  36.598  13.651  1.00 15.92 ? 66   ASN A C   1 
ATOM   499  O  O   . ASN A 1 66  ? 59.305  37.498  14.324  1.00 15.55 ? 66   ASN A O   1 
ATOM   500  C  CB  . ASN A 1 66  ? 59.226  36.909  11.187  1.00 16.06 ? 66   ASN A CB  1 
ATOM   501  C  CG  . ASN A 1 66  ? 60.344  36.786  10.207  1.00 21.39 ? 66   ASN A CG  1 
ATOM   502  O  OD1 . ASN A 1 66  ? 61.528  36.846  10.611  1.00 23.20 ? 66   ASN A OD1 1 
ATOM   503  N  ND2 . ASN A 1 66  ? 60.007  36.614  8.914   1.00 23.13 ? 66   ASN A ND2 1 
ATOM   504  N  N   . ALA A 1 67  ? 57.592  36.076  13.960  1.00 14.82 ? 67   ALA A N   1 
ATOM   505  C  CA  . ALA A 1 67  ? 56.908  36.537  15.173  1.00 15.04 ? 67   ALA A CA  1 
ATOM   506  C  C   . ALA A 1 67  ? 57.707  36.091  16.400  1.00 15.11 ? 67   ALA A C   1 
ATOM   507  O  O   . ALA A 1 67  ? 57.878  36.859  17.361  1.00 14.64 ? 67   ALA A O   1 
ATOM   508  C  CB  . ALA A 1 67  ? 55.457  35.959  15.229  1.00 14.53 ? 67   ALA A CB  1 
ATOM   509  N  N   . ASN A 1 68  ? 58.237  34.853  16.361  1.00 15.31 ? 68   ASN A N   1 
ATOM   510  C  CA  . ASN A 1 68  ? 59.047  34.385  17.473  1.00 15.93 ? 68   ASN A CA  1 
ATOM   511  C  C   . ASN A 1 68  ? 60.318  35.245  17.564  1.00 15.37 ? 68   ASN A C   1 
ATOM   512  O  O   . ASN A 1 68  ? 60.725  35.608  18.659  1.00 15.39 ? 68   ASN A O   1 
ATOM   513  C  CB  . ASN A 1 68  ? 59.434  32.905  17.268  1.00 15.48 ? 68   ASN A CB  1 
ATOM   514  C  CG  . ASN A 1 68  ? 58.270  31.951  17.541  1.00 16.47 ? 68   ASN A CG  1 
ATOM   515  O  OD1 . ASN A 1 68  ? 57.484  31.596  16.621  1.00 20.02 ? 68   ASN A OD1 1 
ATOM   516  N  ND2 . ASN A 1 68  ? 58.156  31.532  18.757  1.00 13.50 ? 68   ASN A ND2 1 
ATOM   517  N  N   . LEU A 1 69  ? 60.913  35.562  16.405  1.00 16.77 ? 69   LEU A N   1 
ATOM   518  C  CA  . LEU A 1 69  ? 62.128  36.420  16.381  1.00 17.25 ? 69   LEU A CA  1 
ATOM   519  C  C   . LEU A 1 69  ? 61.802  37.792  16.971  1.00 16.97 ? 69   LEU A C   1 
ATOM   520  O  O   . LEU A 1 69  ? 62.557  38.287  17.813  1.00 17.12 ? 69   LEU A O   1 
ATOM   521  C  CB  . LEU A 1 69  ? 62.640  36.582  14.966  1.00 19.69 ? 69   LEU A CB  1 
ATOM   522  C  CG  . LEU A 1 69  ? 63.926  37.418  14.783  1.00 23.92 ? 69   LEU A CG  1 
ATOM   523  C  CD1 . LEU A 1 69  ? 65.048  36.720  15.529  1.00 28.19 ? 69   LEU A CD1 1 
ATOM   524  C  CD2 . LEU A 1 69  ? 64.290  37.507  13.291  1.00 25.94 ? 69   LEU A CD2 1 
ATOM   525  N  N   . ARG A 1 70  ? 60.681  38.394  16.580  1.00 15.39 ? 70   ARG A N   1 
ATOM   526  C  CA  . ARG A 1 70  ? 60.383  39.701  17.210  1.00 16.71 ? 70   ARG A CA  1 
ATOM   527  C  C   . ARG A 1 70  ? 60.201  39.639  18.732  1.00 17.02 ? 70   ARG A C   1 
ATOM   528  O  O   . ARG A 1 70  ? 60.622  40.542  19.485  1.00 17.44 ? 70   ARG A O   1 
ATOM   529  C  CB  . ARG A 1 70  ? 59.139  40.330  16.589  1.00 16.14 ? 70   ARG A CB  1 
ATOM   530  C  CG  . ARG A 1 70  ? 59.354  40.732  15.134  1.00 15.97 ? 70   ARG A CG  1 
ATOM   531  C  CD  . ARG A 1 70  ? 58.155  41.545  14.631  1.00 16.62 ? 70   ARG A CD  1 
ATOM   532  N  NE  . ARG A 1 70  ? 56.894  40.764  14.553  1.00 14.61 ? 70   ARG A NE  1 
ATOM   533  C  CZ  . ARG A 1 70  ? 56.510  40.049  13.503  1.00 15.20 ? 70   ARG A CZ  1 
ATOM   534  N  NH1 . ARG A 1 70  ? 57.232  39.968  12.364  1.00 14.95 ? 70   ARG A NH1 1 
ATOM   535  N  NH2 . ARG A 1 70  ? 55.371  39.378  13.587  1.00 14.84 ? 70   ARG A NH2 1 
ATOM   536  N  N   . ALA A 1 71  ? 59.532  38.589  19.217  1.00 15.66 ? 71   ALA A N   1 
ATOM   537  C  CA  . ALA A 1 71  ? 59.326  38.483  20.639  1.00 14.54 ? 71   ALA A CA  1 
ATOM   538  C  C   . ALA A 1 71  ? 60.683  38.327  21.360  1.00 15.98 ? 71   ALA A C   1 
ATOM   539  O  O   . ALA A 1 71  ? 60.885  38.863  22.433  1.00 15.46 ? 71   ALA A O   1 
ATOM   540  C  CB  . ALA A 1 71  ? 58.391  37.276  20.930  1.00 14.82 ? 71   ALA A CB  1 
ATOM   541  N  N   . PHE A 1 72  ? 61.613  37.584  20.771  1.00 17.39 ? 72   PHE A N   1 
ATOM   542  C  CA  . PHE A 1 72  ? 62.923  37.427  21.395  1.00 18.28 ? 72   PHE A CA  1 
ATOM   543  C  C   . PHE A 1 72  ? 63.689  38.743  21.396  1.00 19.23 ? 72   PHE A C   1 
ATOM   544  O  O   . PHE A 1 72  ? 64.446  39.025  22.323  1.00 19.78 ? 72   PHE A O   1 
ATOM   545  C  CB  . PHE A 1 72  ? 63.735  36.345  20.682  1.00 20.39 ? 72   PHE A CB  1 
ATOM   546  C  CG  . PHE A 1 72  ? 63.348  34.949  21.075  1.00 21.15 ? 72   PHE A CG  1 
ATOM   547  C  CD1 . PHE A 1 72  ? 63.339  34.571  22.415  1.00 22.88 ? 72   PHE A CD1 1 
ATOM   548  C  CD2 . PHE A 1 72  ? 62.993  34.013  20.112  1.00 22.89 ? 72   PHE A CD2 1 
ATOM   549  C  CE1 . PHE A 1 72  ? 62.982  33.279  22.790  1.00 23.40 ? 72   PHE A CE1 1 
ATOM   550  C  CE2 . PHE A 1 72  ? 62.636  32.718  20.477  1.00 22.33 ? 72   PHE A CE2 1 
ATOM   551  C  CZ  . PHE A 1 72  ? 62.630  32.352  21.817  1.00 21.38 ? 72   PHE A CZ  1 
ATOM   552  N  N   . ALA A 1 73  ? 63.499  39.513  20.329  1.00 20.45 ? 73   ALA A N   1 
ATOM   553  C  CA  . ALA A 1 73  ? 64.184  40.833  20.252  1.00 20.36 ? 73   ALA A CA  1 
ATOM   554  C  C   . ALA A 1 73  ? 63.680  41.679  21.412  1.00 22.15 ? 73   ALA A C   1 
ATOM   555  O  O   . ALA A 1 73  ? 64.430  42.536  21.938  1.00 21.60 ? 73   ALA A O   1 
ATOM   556  C  CB  . ALA A 1 73  ? 63.875  41.511  18.940  1.00 19.19 ? 73   ALA A CB  1 
ATOM   557  N  N   . ALA A 1 74  ? 62.417  41.463  21.806  1.00 21.23 ? 74   ALA A N   1 
ATOM   558  C  CA  . ALA A 1 74  ? 61.836  42.179  22.940  1.00 19.66 ? 74   ALA A CA  1 
ATOM   559  C  C   . ALA A 1 74  ? 62.184  41.561  24.291  1.00 20.09 ? 74   ALA A C   1 
ATOM   560  O  O   . ALA A 1 74  ? 61.710  42.052  25.313  1.00 21.42 ? 74   ALA A O   1 
ATOM   561  C  CB  . ALA A 1 74  ? 60.320  42.312  22.793  1.00 21.55 ? 74   ALA A CB  1 
ATOM   562  N  N   . GLY A 1 75  ? 62.956  40.468  24.286  1.00 19.10 ? 75   GLY A N   1 
ATOM   563  C  CA  . GLY A 1 75  ? 63.399  39.816  25.515  1.00 19.15 ? 75   GLY A CA  1 
ATOM   564  C  C   . GLY A 1 75  ? 62.357  38.949  26.217  1.00 18.84 ? 75   GLY A C   1 
ATOM   565  O  O   . GLY A 1 75  ? 62.514  38.594  27.373  1.00 20.73 ? 75   GLY A O   1 
ATOM   566  N  N   . VAL A 1 76  ? 61.321  38.576  25.474  1.00 18.95 ? 76   VAL A N   1 
ATOM   567  C  CA  . VAL A 1 76  ? 60.208  37.804  26.039  1.00 18.87 ? 76   VAL A CA  1 
ATOM   568  C  C   . VAL A 1 76  ? 60.592  36.365  26.436  1.00 19.34 ? 76   VAL A C   1 
ATOM   569  O  O   . VAL A 1 76  ? 61.046  35.594  25.602  1.00 22.09 ? 76   VAL A O   1 
ATOM   570  C  CB  . VAL A 1 76  ? 59.037  37.794  25.021  1.00 18.11 ? 76   VAL A CB  1 
ATOM   571  C  CG1 . VAL A 1 76  ? 57.853  36.932  25.565  1.00 17.90 ? 76   VAL A CG1 1 
ATOM   572  C  CG2 . VAL A 1 76  ? 58.542  39.253  24.762  1.00 17.23 ? 76   VAL A CG2 1 
ATOM   573  N  N   . THR A 1 77  ? 60.365  36.043  27.699  1.00 17.50 ? 77   THR A N   1 
ATOM   574  C  CA  . THR A 1 77  ? 60.686  34.741  28.286  1.00 17.86 ? 77   THR A CA  1 
ATOM   575  C  C   . THR A 1 77  ? 59.439  33.979  28.642  1.00 17.83 ? 77   THR A C   1 
ATOM   576  O  O   . THR A 1 77  ? 58.360  34.546  28.672  1.00 16.20 ? 77   THR A O   1 
ATOM   577  C  CB  . THR A 1 77  ? 61.423  34.892  29.600  1.00 19.17 ? 77   THR A CB  1 
ATOM   578  O  OG1 . THR A 1 77  ? 60.580  35.584  30.541  1.00 18.65 ? 77   THR A OG1 1 
ATOM   579  C  CG2 . THR A 1 77  ? 62.757  35.667  29.385  1.00 19.40 ? 77   THR A CG2 1 
ATOM   580  N  N   . PRO A 1 78  ? 59.576  32.668  28.895  1.00 16.44 ? 78   PRO A N   1 
ATOM   581  C  CA  . PRO A 1 78  ? 58.357  31.924  29.253  1.00 16.02 ? 78   PRO A CA  1 
ATOM   582  C  C   . PRO A 1 78  ? 57.744  32.439  30.555  1.00 16.42 ? 78   PRO A C   1 
ATOM   583  O  O   . PRO A 1 78  ? 56.503  32.479  30.707  1.00 16.12 ? 78   PRO A O   1 
ATOM   584  C  CB  . PRO A 1 78  ? 58.852  30.462  29.353  1.00 16.71 ? 78   PRO A CB  1 
ATOM   585  C  CG  . PRO A 1 78  ? 59.929  30.395  28.332  1.00 17.72 ? 78   PRO A CG  1 
ATOM   586  C  CD  . PRO A 1 78  ? 60.673  31.748  28.515  1.00 17.44 ? 78   PRO A CD  1 
ATOM   587  N  N   . ALA A 1 79  ? 58.567  32.892  31.504  1.00 16.46 ? 79   ALA A N   1 
ATOM   588  C  CA  . ALA A 1 79  ? 58.018  33.410  32.763  1.00 17.07 ? 79   ALA A CA  1 
ATOM   589  C  C   . ALA A 1 79  ? 57.191  34.657  32.494  1.00 17.45 ? 79   ALA A C   1 
ATOM   590  O  O   . ALA A 1 79  ? 56.105  34.845  33.082  1.00 17.49 ? 79   ALA A O   1 
ATOM   591  C  CB  . ALA A 1 79  ? 59.136  33.721  33.743  1.00 18.89 ? 79   ALA A CB  1 
ATOM   592  N  N   . GLN A 1 80  ? 57.671  35.514  31.584  1.00 18.16 ? 80   GLN A N   1 
ATOM   593  C  CA  . GLN A 1 80  ? 56.876  36.701  31.264  1.00 16.82 ? 80   GLN A CA  1 
ATOM   594  C  C   . GLN A 1 80  ? 55.587  36.328  30.560  1.00 15.94 ? 80   GLN A C   1 
ATOM   595  O  O   . GLN A 1 80  ? 54.550  36.973  30.725  1.00 16.27 ? 80   GLN A O   1 
ATOM   596  C  CB  . GLN A 1 80  ? 57.686  37.663  30.378  1.00 17.70 ? 80   GLN A CB  1 
ATOM   597  C  CG  . GLN A 1 80  ? 58.785  38.309  31.193  1.00 20.93 ? 80   GLN A CG  1 
ATOM   598  C  CD  . GLN A 1 80  ? 59.685  39.151  30.372  1.00 21.85 ? 80   GLN A CD  1 
ATOM   599  O  OE1 . GLN A 1 80  ? 59.799  38.984  29.152  1.00 23.91 ? 80   GLN A OE1 1 
ATOM   600  N  NE2 . GLN A 1 80  ? 60.342  40.090  31.026  1.00 26.02 ? 80   GLN A NE2 1 
ATOM   601  N  N   . CYS A 1 81  ? 55.628  35.248  29.775  1.00 13.97 ? 81   CYS A N   1 
ATOM   602  C  CA  . CYS A 1 81  ? 54.412  34.814  29.100  1.00 14.31 ? 81   CYS A CA  1 
ATOM   603  C  C   . CYS A 1 81  ? 53.328  34.364  30.089  1.00 12.63 ? 81   CYS A C   1 
ATOM   604  O  O   . CYS A 1 81  ? 52.168  34.616  29.870  1.00 12.47 ? 81   CYS A O   1 
ATOM   605  C  CB  . CYS A 1 81  ? 54.727  33.631  28.167  1.00 14.63 ? 81   CYS A CB  1 
ATOM   606  S  SG  . CYS A 1 81  ? 55.623  34.117  26.649  1.00 15.75 ? 81   CYS A SG  1 
ATOM   607  N  N   . PHE A 1 82  ? 53.722  33.670  31.146  1.00 13.64 ? 82   PHE A N   1 
ATOM   608  C  CA  . PHE A 1 82  ? 52.753  33.222  32.136  1.00 14.23 ? 82   PHE A CA  1 
ATOM   609  C  C   . PHE A 1 82  ? 52.169  34.410  32.893  1.00 14.14 ? 82   PHE A C   1 
ATOM   610  O  O   . PHE A 1 82  ? 51.018  34.372  33.324  1.00 14.95 ? 82   PHE A O   1 
ATOM   611  C  CB  . PHE A 1 82  ? 53.389  32.209  33.094  1.00 15.26 ? 82   PHE A CB  1 
ATOM   612  C  CG  . PHE A 1 82  ? 53.344  30.792  32.585  1.00 16.77 ? 82   PHE A CG  1 
ATOM   613  C  CD1 . PHE A 1 82  ? 52.124  30.142  32.419  1.00 16.13 ? 82   PHE A CD1 1 
ATOM   614  C  CD2 . PHE A 1 82  ? 54.514  30.114  32.253  1.00 18.76 ? 82   PHE A CD2 1 
ATOM   615  C  CE1 . PHE A 1 82  ? 52.067  28.837  31.927  1.00 17.25 ? 82   PHE A CE1 1 
ATOM   616  C  CE2 . PHE A 1 82  ? 54.465  28.808  31.761  1.00 20.29 ? 82   PHE A CE2 1 
ATOM   617  C  CZ  . PHE A 1 82  ? 53.239  28.171  31.598  1.00 18.79 ? 82   PHE A CZ  1 
ATOM   618  N  N   . GLU A 1 83  ? 53.000  35.438  33.122  1.00 14.80 ? 83   GLU A N   1 
ATOM   619  C  CA  . GLU A 1 83  ? 52.460  36.668  33.761  1.00 16.09 ? 83   GLU A CA  1 
ATOM   620  C  C   . GLU A 1 83  ? 51.436  37.306  32.809  1.00 13.75 ? 83   GLU A C   1 
ATOM   621  O  O   . GLU A 1 83  ? 50.354  37.769  33.249  1.00 13.27 ? 83   GLU A O   1 
ATOM   622  C  CB  . GLU A 1 83  ? 53.576  37.672  34.049  1.00 18.70 ? 83   GLU A CB  1 
ATOM   623  C  CG  . GLU A 1 83  ? 54.630  37.107  34.965  1.00 24.31 ? 83   GLU A CG  1 
ATOM   624  C  CD  . GLU A 1 83  ? 55.789  38.085  35.227  1.00 29.73 ? 83   GLU A CD  1 
ATOM   625  O  OE1 . GLU A 1 83  ? 56.236  38.788  34.274  1.00 32.69 ? 83   GLU A OE1 1 
ATOM   626  O  OE2 . GLU A 1 83  ? 56.237  38.140  36.396  1.00 32.34 ? 83   GLU A OE2 1 
ATOM   627  N  N   . MET A 1 84  ? 51.739  37.343  31.510  1.00 12.83 ? 84   MET A N   1 
ATOM   628  C  CA  . MET A 1 84  ? 50.763  37.873  30.544  1.00 11.82 ? 84   MET A CA  1 
ATOM   629  C  C   . MET A 1 84  ? 49.471  37.059  30.561  1.00 12.40 ? 84   MET A C   1 
ATOM   630  O  O   . MET A 1 84  ? 48.373  37.575  30.546  1.00 13.05 ? 84   MET A O   1 
ATOM   631  C  CB  . MET A 1 84  ? 51.302  37.829  29.094  1.00 14.15 ? 84   MET A CB  1 
ATOM   632  C  CG  . MET A 1 84  ? 52.420  38.851  28.785  1.00 14.78 ? 84   MET A CG  1 
ATOM   633  S  SD  . MET A 1 84  ? 53.023  38.657  27.112  1.00 17.27 ? 84   MET A SD  1 
ATOM   634  C  CE  . MET A 1 84  ? 51.754  39.243  26.264  1.00 17.87 ? 84   MET A CE  1 
ATOM   635  N  N   . LEU A 1 85  ? 49.620  35.724  30.571  1.00 12.52 ? 85   LEU A N   1 
ATOM   636  C  CA  . LEU A 1 85  ? 48.458  34.868  30.572  1.00 12.23 ? 85   LEU A CA  1 
ATOM   637  C  C   . LEU A 1 85  ? 47.573  35.085  31.806  1.00 10.58 ? 85   LEU A C   1 
ATOM   638  O  O   . LEU A 1 85  ? 46.336  35.102  31.669  1.00 11.18 ? 85   LEU A O   1 
ATOM   639  C  CB  . LEU A 1 85  ? 48.903  33.388  30.507  1.00 10.84 ? 85   LEU A CB  1 
ATOM   640  C  CG  . LEU A 1 85  ? 49.501  32.940  29.135  1.00 12.45 ? 85   LEU A CG  1 
ATOM   641  C  CD1 . LEU A 1 85  ? 50.298  31.578  29.320  1.00 11.01 ? 85   LEU A CD1 1 
ATOM   642  C  CD2 . LEU A 1 85  ? 48.430  32.824  28.039  1.00 11.28 ? 85   LEU A CD2 1 
ATOM   643  N  N   . ALA A 1 86  ? 48.178  35.253  32.975  1.00 12.31 ? 86   ALA A N   1 
ATOM   644  C  CA  . ALA A 1 86  ? 47.375  35.490  34.174  1.00 11.85 ? 86   ALA A CA  1 
ATOM   645  C  C   . ALA A 1 86  ? 46.575  36.792  33.990  1.00 13.58 ? 86   ALA A C   1 
ATOM   646  O  O   . ALA A 1 86  ? 45.415  36.834  34.360  1.00 13.81 ? 86   ALA A O   1 
ATOM   647  C  CB  . ALA A 1 86  ? 48.228  35.559  35.386  1.00 13.25 ? 86   ALA A CB  1 
ATOM   648  N  N   . LEU A 1 87  ? 47.211  37.813  33.423  1.00 13.16 ? 87   LEU A N   1 
ATOM   649  C  CA  . LEU A 1 87  ? 46.501  39.081  33.240  1.00 14.66 ? 87   LEU A CA  1 
ATOM   650  C  C   . LEU A 1 87  ? 45.392  38.966  32.253  1.00 14.46 ? 87   LEU A C   1 
ATOM   651  O  O   . LEU A 1 87  ? 44.274  39.495  32.415  1.00 13.85 ? 87   LEU A O   1 
ATOM   652  C  CB  . LEU A 1 87  ? 47.483  40.157  32.796  1.00 15.24 ? 87   LEU A CB  1 
ATOM   653  C  CG  . LEU A 1 87  ? 46.771  41.513  32.604  1.00 20.46 ? 87   LEU A CG  1 
ATOM   654  C  CD1 . LEU A 1 87  ? 45.985  41.936  33.891  1.00 21.40 ? 87   LEU A CD1 1 
ATOM   655  C  CD2 . LEU A 1 87  ? 47.877  42.522  32.282  1.00 21.34 ? 87   LEU A CD2 1 
ATOM   656  N  N   . ILE A 1 88  ? 45.639  38.247  31.158  1.00 12.09 ? 88   ILE A N   1 
ATOM   657  C  CA  . ILE A 1 88  ? 44.602  38.093  30.178  1.00 12.80 ? 88   ILE A CA  1 
ATOM   658  C  C   . ILE A 1 88  ? 43.395  37.382  30.794  1.00 13.82 ? 88   ILE A C   1 
ATOM   659  O  O   . ILE A 1 88  ? 42.273  37.797  30.579  1.00 13.39 ? 88   ILE A O   1 
ATOM   660  C  CB  . ILE A 1 88  ? 45.167  37.293  28.955  1.00 12.93 ? 88   ILE A CB  1 
ATOM   661  C  CG1 . ILE A 1 88  ? 46.297  38.115  28.333  1.00 14.40 ? 88   ILE A CG1 1 
ATOM   662  C  CG2 . ILE A 1 88  ? 44.100  36.931  27.988  1.00 12.70 ? 88   ILE A CG2 1 
ATOM   663  C  CD1 . ILE A 1 88  ? 47.229  37.286  27.429  1.00 14.03 ? 88   ILE A CD1 1 
ATOM   664  N  N   . ARG A 1 89  ? 43.615  36.329  31.590  1.00 12.27 ? 89   ARG A N   1 
ATOM   665  C  CA  . ARG A 1 89  ? 42.469  35.628  32.212  1.00 12.15 ? 89   ARG A CA  1 
ATOM   666  C  C   . ARG A 1 89  ? 41.758  36.518  33.226  1.00 12.89 ? 89   ARG A C   1 
ATOM   667  O  O   . ARG A 1 89  ? 40.548  36.456  33.357  1.00 13.16 ? 89   ARG A O   1 
ATOM   668  C  CB  . ARG A 1 89  ? 43.011  34.361  32.891  1.00 12.33 ? 89   ARG A CB  1 
ATOM   669  C  CG  . ARG A 1 89  ? 41.988  33.602  33.756  1.00 12.24 ? 89   ARG A CG  1 
ATOM   670  C  CD  . ARG A 1 89  ? 40.776  33.282  32.923  1.00 12.27 ? 89   ARG A CD  1 
ATOM   671  N  NE  . ARG A 1 89  ? 41.052  32.214  31.950  1.00 13.80 ? 89   ARG A NE  1 
ATOM   672  C  CZ  . ARG A 1 89  ? 40.485  32.073  30.752  1.00 13.04 ? 89   ARG A CZ  1 
ATOM   673  N  NH1 . ARG A 1 89  ? 39.572  32.936  30.252  1.00 11.55 ? 89   ARG A NH1 1 
ATOM   674  N  NH2 . ARG A 1 89  ? 40.815  30.975  30.037  1.00 12.59 ? 89   ARG A NH2 1 
ATOM   675  N  N   . GLU A 1 90  ? 42.527  37.359  33.899  1.00 13.86 ? 90   GLU A N   1 
ATOM   676  C  CA  . GLU A 1 90  ? 41.924  38.253  34.909  1.00 15.17 ? 90   GLU A CA  1 
ATOM   677  C  C   . GLU A 1 90  ? 41.031  39.273  34.238  1.00 15.00 ? 90   GLU A C   1 
ATOM   678  O  O   . GLU A 1 90  ? 40.073  39.762  34.861  1.00 16.77 ? 90   GLU A O   1 
ATOM   679  C  CB  . GLU A 1 90  ? 43.011  38.973  35.710  1.00 15.43 ? 90   GLU A CB  1 
ATOM   680  C  CG  . GLU A 1 90  ? 43.609  38.081  36.765  1.00 22.27 ? 90   GLU A CG  1 
ATOM   681  C  CD  . GLU A 1 90  ? 44.987  38.538  37.218  1.00 28.62 ? 90   GLU A CD  1 
ATOM   682  O  OE1 . GLU A 1 90  ? 45.451  39.626  36.775  1.00 30.53 ? 90   GLU A OE1 1 
ATOM   683  O  OE2 . GLU A 1 90  ? 45.612  37.799  38.032  1.00 33.54 ? 90   GLU A OE2 1 
ATOM   684  N  N   . LYS A 1 91  ? 41.303  39.623  32.989  1.00 12.78 ? 91   LYS A N   1 
ATOM   685  C  CA  . LYS A 1 91  ? 40.466  40.559  32.249  1.00 13.24 ? 91   LYS A CA  1 
ATOM   686  C  C   . LYS A 1 91  ? 39.261  39.893  31.576  1.00 14.60 ? 91   LYS A C   1 
ATOM   687  O  O   . LYS A 1 91  ? 38.204  40.475  31.441  1.00 14.62 ? 91   LYS A O   1 
ATOM   688  C  CB  . LYS A 1 91  ? 41.290  41.225  31.130  1.00 13.23 ? 91   LYS A CB  1 
ATOM   689  C  CG  . LYS A 1 91  ? 42.274  42.240  31.654  1.00 14.89 ? 91   LYS A CG  1 
ATOM   690  C  CD  . LYS A 1 91  ? 42.947  42.979  30.484  1.00 19.89 ? 91   LYS A CD  1 
ATOM   691  C  CE  . LYS A 1 91  ? 43.973  42.122  29.782  1.00 21.47 ? 91   LYS A CE  1 
ATOM   692  N  NZ  . LYS A 1 91  ? 44.838  43.124  29.006  1.00 21.63 ? 91   LYS A NZ  1 
ATOM   693  N  N   . HIS A 1 92  ? 39.473  38.645  31.112  1.00 15.33 ? 92   HIS A N   1 
ATOM   694  C  CA  . HIS A 1 92  ? 38.473  37.891  30.361  1.00 14.49 ? 92   HIS A CA  1 
ATOM   695  C  C   . HIS A 1 92  ? 38.293  36.529  31.021  1.00 15.17 ? 92   HIS A C   1 
ATOM   696  O  O   . HIS A 1 92  ? 39.047  35.593  30.756  1.00 15.03 ? 92   HIS A O   1 
ATOM   697  C  CB  . HIS A 1 92  ? 38.971  37.726  28.926  1.00 14.59 ? 92   HIS A CB  1 
ATOM   698  C  CG  . HIS A 1 92  ? 39.431  39.008  28.300  1.00 13.61 ? 92   HIS A CG  1 
ATOM   699  N  ND1 . HIS A 1 92  ? 38.555  39.960  27.825  1.00 14.40 ? 92   HIS A ND1 1 
ATOM   700  C  CD2 . HIS A 1 92  ? 40.675  39.506  28.095  1.00 12.22 ? 92   HIS A CD2 1 
ATOM   701  C  CE1 . HIS A 1 92  ? 39.238  40.988  27.353  1.00 13.49 ? 92   HIS A CE1 1 
ATOM   702  N  NE2 . HIS A 1 92  ? 40.526  40.738  27.505  1.00 14.51 ? 92   HIS A NE2 1 
ATOM   703  N  N   . PRO A 1 93  ? 37.217  36.404  31.795  1.00 13.73 ? 93   PRO A N   1 
ATOM   704  C  CA  . PRO A 1 93  ? 37.001  35.161  32.499  1.00 13.55 ? 93   PRO A CA  1 
ATOM   705  C  C   . PRO A 1 93  ? 36.484  33.940  31.769  1.00 12.95 ? 93   PRO A C   1 
ATOM   706  O  O   . PRO A 1 93  ? 36.674  32.845  32.310  1.00 14.44 ? 93   PRO A O   1 
ATOM   707  C  CB  . PRO A 1 93  ? 36.058  35.588  33.642  1.00 15.04 ? 93   PRO A CB  1 
ATOM   708  C  CG  . PRO A 1 93  ? 35.210  36.588  32.995  1.00 15.04 ? 93   PRO A CG  1 
ATOM   709  C  CD  . PRO A 1 93  ? 36.176  37.414  32.143  1.00 15.25 ? 93   PRO A CD  1 
ATOM   710  N  N   . THR A 1 94  ? 35.849  34.100  30.625  1.00 12.96 ? 94   THR A N   1 
ATOM   711  C  CA  . THR A 1 94  ? 35.228  32.917  30.020  1.00 14.65 ? 94   THR A CA  1 
ATOM   712  C  C   . THR A 1 94  ? 35.832  32.482  28.717  1.00 13.54 ? 94   THR A C   1 
ATOM   713  O  O   . THR A 1 94  ? 35.576  31.360  28.260  1.00 14.01 ? 94   THR A O   1 
ATOM   714  C  CB  . THR A 1 94  ? 33.703  33.138  29.774  1.00 16.33 ? 94   THR A CB  1 
ATOM   715  O  OG1 . THR A 1 94  ? 33.508  34.233  28.880  1.00 18.43 ? 94   THR A OG1 1 
ATOM   716  C  CG2 . THR A 1 94  ? 32.987  33.473  31.137  1.00 17.90 ? 94   THR A CG2 1 
ATOM   717  N  N   . ILE A 1 95  ? 36.628  33.327  28.102  1.00 13.10 ? 95   ILE A N   1 
ATOM   718  C  CA  . ILE A 1 95  ? 37.171  32.972  26.782  1.00 12.73 ? 95   ILE A CA  1 
ATOM   719  C  C   . ILE A 1 95  ? 38.165  31.813  26.894  1.00 11.69 ? 95   ILE A C   1 
ATOM   720  O  O   . ILE A 1 95  ? 39.030  31.831  27.765  1.00 12.54 ? 95   ILE A O   1 
ATOM   721  C  CB  . ILE A 1 95  ? 37.862  34.195  26.120  1.00 11.65 ? 95   ILE A CB  1 
ATOM   722  C  CG1 . ILE A 1 95  ? 38.183  33.831  24.680  1.00 12.93 ? 95   ILE A CG1 1 
ATOM   723  C  CG2 . ILE A 1 95  ? 39.069  34.697  26.935  1.00 12.72 ? 95   ILE A CG2 1 
ATOM   724  C  CD1 . ILE A 1 95  ? 38.677  34.981  23.884  1.00 13.68 ? 95   ILE A CD1 1 
ATOM   725  N  N   . PRO A 1 96  ? 38.007  30.784  26.051  1.00 12.15 ? 96   PRO A N   1 
ATOM   726  C  CA  . PRO A 1 96  ? 38.992  29.696  26.173  1.00 11.85 ? 96   PRO A CA  1 
ATOM   727  C  C   . PRO A 1 96  ? 40.370  30.183  25.703  1.00 10.68 ? 96   PRO A C   1 
ATOM   728  O  O   . PRO A 1 96  ? 40.478  30.875  24.671  1.00 11.71 ? 96   PRO A O   1 
ATOM   729  C  CB  . PRO A 1 96  ? 38.447  28.654  25.223  1.00 10.71 ? 96   PRO A CB  1 
ATOM   730  C  CG  . PRO A 1 96  ? 36.954  28.856  25.251  1.00 11.76 ? 96   PRO A CG  1 
ATOM   731  C  CD  . PRO A 1 96  ? 36.879  30.373  25.205  1.00 12.10 ? 96   PRO A CD  1 
ATOM   732  N  N   . ILE A 1 97  ? 41.405  29.786  26.439  1.00 10.55 ? 97   ILE A N   1 
ATOM   733  C  CA  . ILE A 1 97  ? 42.778  30.169  26.108  1.00 9.78  ? 97   ILE A CA  1 
ATOM   734  C  C   . ILE A 1 97  ? 43.592  28.882  25.942  1.00 10.58 ? 97   ILE A C   1 
ATOM   735  O  O   . ILE A 1 97  ? 43.721  28.046  26.862  1.00 11.12 ? 97   ILE A O   1 
ATOM   736  C  CB  . ILE A 1 97  ? 43.413  31.040  27.227  1.00 12.29 ? 97   ILE A CB  1 
ATOM   737  C  CG1 . ILE A 1 97  ? 42.693  32.396  27.337  1.00 14.42 ? 97   ILE A CG1 1 
ATOM   738  C  CG2 . ILE A 1 97  ? 44.930  31.299  26.947  1.00 12.93 ? 97   ILE A CG2 1 
ATOM   739  C  CD1 . ILE A 1 97  ? 43.069  33.133  28.569  1.00 15.19 ? 97   ILE A CD1 1 
ATOM   740  N  N   . GLY A 1 98  ? 44.138  28.752  24.740  1.00 10.02 ? 98   GLY A N   1 
ATOM   741  C  CA  . GLY A 1 98  ? 44.965  27.575  24.448  1.00 10.24 ? 98   GLY A CA  1 
ATOM   742  C  C   . GLY A 1 98  ? 46.367  28.050  24.131  1.00 11.17 ? 98   GLY A C   1 
ATOM   743  O  O   . GLY A 1 98  ? 46.560  29.125  23.544  1.00 13.19 ? 98   GLY A O   1 
ATOM   744  N  N   . LEU A 1 99  ? 47.355  27.266  24.526  1.00 9.05  ? 99   LEU A N   1 
ATOM   745  C  CA  . LEU A 1 99  ? 48.773  27.577  24.208  1.00 10.07 ? 99   LEU A CA  1 
ATOM   746  C  C   . LEU A 1 99  ? 49.283  26.694  23.073  1.00 10.09 ? 99   LEU A C   1 
ATOM   747  O  O   . LEU A 1 99  ? 48.794  25.551  22.884  1.00 11.96 ? 99   LEU A O   1 
ATOM   748  C  CB  . LEU A 1 99  ? 49.674  27.284  25.412  1.00 9.67  ? 99   LEU A CB  1 
ATOM   749  C  CG  . LEU A 1 99  ? 49.302  28.046  26.687  1.00 9.55  ? 99   LEU A CG  1 
ATOM   750  C  CD1 . LEU A 1 99  ? 50.375  27.809  27.767  1.00 11.60 ? 99   LEU A CD1 1 
ATOM   751  C  CD2 . LEU A 1 99  ? 49.233  29.564  26.335  1.00 11.60 ? 99   LEU A CD2 1 
ATOM   752  N  N   . LEU A 1 100 ? 50.205  27.253  22.300  1.00 10.07 ? 100  LEU A N   1 
ATOM   753  C  CA  . LEU A 1 100 ? 50.938  26.534  21.265  1.00 10.53 ? 100  LEU A CA  1 
ATOM   754  C  C   . LEU A 1 100 ? 52.362  26.445  21.800  1.00 11.08 ? 100  LEU A C   1 
ATOM   755  O  O   . LEU A 1 100 ? 53.046  27.452  21.935  1.00 11.17 ? 100  LEU A O   1 
ATOM   756  C  CB  . LEU A 1 100 ? 50.875  27.274  19.914  1.00 11.13 ? 100  LEU A CB  1 
ATOM   757  C  CG  . LEU A 1 100 ? 51.552  26.590  18.708  1.00 13.36 ? 100  LEU A CG  1 
ATOM   758  C  CD1 . LEU A 1 100 ? 53.098  26.608  18.809  1.00 14.91 ? 100  LEU A CD1 1 
ATOM   759  C  CD2 . LEU A 1 100 ? 51.042  25.194  18.595  1.00 14.62 ? 100  LEU A CD2 1 
ATOM   760  N  N   . MET A 1 101 ? 52.803  25.225  22.163  1.00 10.03 ? 101  MET A N   1 
ATOM   761  C  CA  . MET A 1 101 ? 54.110  24.987  22.750  1.00 9.62  ? 101  MET A CA  1 
ATOM   762  C  C   . MET A 1 101 ? 54.913  24.048  21.887  1.00 11.06 ? 101  MET A C   1 
ATOM   763  O  O   . MET A 1 101 ? 54.382  23.326  21.052  1.00 12.34 ? 101  MET A O   1 
ATOM   764  C  CB  . MET A 1 101 ? 53.922  24.280  24.123  1.00 10.29 ? 101  MET A CB  1 
ATOM   765  C  CG  . MET A 1 101 ? 53.052  25.015  25.114  1.00 8.72  ? 101  MET A CG  1 
ATOM   766  S  SD  . MET A 1 101 ? 53.702  26.681  25.502  1.00 10.63 ? 101  MET A SD  1 
ATOM   767  C  CE  . MET A 1 101 ? 55.398  26.289  25.977  1.00 11.36 ? 101  MET A CE  1 
ATOM   768  N  N   . TYR A 1 102 ? 56.193  24.013  22.188  1.00 11.45 ? 102  TYR A N   1 
ATOM   769  C  CA  . TYR A 1 102 ? 57.124  23.082  21.581  1.00 10.86 ? 102  TYR A CA  1 
ATOM   770  C  C   . TYR A 1 102 ? 57.596  22.283  22.791  1.00 10.49 ? 102  TYR A C   1 
ATOM   771  O  O   . TYR A 1 102 ? 57.741  22.823  23.891  1.00 10.48 ? 102  TYR A O   1 
ATOM   772  C  CB  . TYR A 1 102 ? 58.254  23.818  20.859  1.00 11.53 ? 102  TYR A CB  1 
ATOM   773  C  CG  . TYR A 1 102 ? 57.841  24.199  19.451  1.00 12.07 ? 102  TYR A CG  1 
ATOM   774  C  CD1 . TYR A 1 102 ? 57.903  23.272  18.408  1.00 13.09 ? 102  TYR A CD1 1 
ATOM   775  C  CD2 . TYR A 1 102 ? 57.317  25.461  19.175  1.00 12.99 ? 102  TYR A CD2 1 
ATOM   776  C  CE1 . TYR A 1 102 ? 57.452  23.593  17.124  1.00 13.10 ? 102  TYR A CE1 1 
ATOM   777  C  CE2 . TYR A 1 102 ? 56.863  25.793  17.895  1.00 13.95 ? 102  TYR A CE2 1 
ATOM   778  C  CZ  . TYR A 1 102 ? 56.935  24.855  16.876  1.00 13.41 ? 102  TYR A CZ  1 
ATOM   779  O  OH  . TYR A 1 102 ? 56.509  25.185  15.605  1.00 14.71 ? 102  TYR A OH  1 
ATOM   780  N  N   . ALA A 1 103 ? 57.882  21.028  22.577  1.00 8.39  ? 103  ALA A N   1 
ATOM   781  C  CA  . ALA A 1 103 ? 58.159  20.151  23.717  1.00 8.75  ? 103  ALA A CA  1 
ATOM   782  C  C   . ALA A 1 103 ? 59.211  20.548  24.711  1.00 9.46  ? 103  ALA A C   1 
ATOM   783  O  O   . ALA A 1 103 ? 59.038  20.328  25.901  1.00 10.01 ? 103  ALA A O   1 
ATOM   784  C  CB  . ALA A 1 103 ? 58.502  18.716  23.171  1.00 10.04 ? 103  ALA A CB  1 
ATOM   785  N  N   . ASN A 1 104 ? 60.305  21.122  24.225  1.00 10.18 ? 104  ASN A N   1 
ATOM   786  C  CA  . ASN A 1 104 ? 61.325  21.392  25.181  1.00 8.81  ? 104  ASN A CA  1 
ATOM   787  C  C   . ASN A 1 104 ? 60.900  22.399  26.255  1.00 9.47  ? 104  ASN A C   1 
ATOM   788  O  O   . ASN A 1 104 ? 61.350  22.308  27.390  1.00 10.75 ? 104  ASN A O   1 
ATOM   789  C  CB  . ASN A 1 104 ? 62.618  21.874  24.536  1.00 9.62  ? 104  ASN A CB  1 
ATOM   790  C  CG  . ASN A 1 104 ? 63.752  21.686  25.505  1.00 10.18 ? 104  ASN A CG  1 
ATOM   791  O  OD1 . ASN A 1 104 ? 63.951  20.577  26.042  1.00 10.46 ? 104  ASN A OD1 1 
ATOM   792  N  ND2 . ASN A 1 104 ? 64.509  22.762  25.781  1.00 11.43 ? 104  ASN A ND2 1 
ATOM   793  N  N   . LEU A 1 105 ? 60.006  23.316  25.860  1.00 9.93  ? 105  LEU A N   1 
ATOM   794  C  CA  . LEU A 1 105 ? 59.561  24.295  26.851  1.00 10.96 ? 105  LEU A CA  1 
ATOM   795  C  C   . LEU A 1 105 ? 58.662  23.700  27.929  1.00 10.94 ? 105  LEU A C   1 
ATOM   796  O  O   . LEU A 1 105 ? 58.595  24.220  29.061  1.00 12.03 ? 105  LEU A O   1 
ATOM   797  C  CB  . LEU A 1 105 ? 58.831  25.494  26.194  1.00 11.01 ? 105  LEU A CB  1 
ATOM   798  C  CG  . LEU A 1 105 ? 59.732  26.348  25.273  1.00 12.25 ? 105  LEU A CG  1 
ATOM   799  C  CD1 . LEU A 1 105 ? 58.941  27.542  24.686  1.00 13.71 ? 105  LEU A CD1 1 
ATOM   800  C  CD2 . LEU A 1 105 ? 60.965  26.846  26.076  1.00 15.27 ? 105  LEU A CD2 1 
ATOM   801  N  N   . VAL A 1 106 ? 57.965  22.617  27.567  1.00 9.51  ? 106  VAL A N   1 
ATOM   802  C  CA  . VAL A 1 106 ? 57.111  21.904  28.511  1.00 10.17 ? 106  VAL A CA  1 
ATOM   803  C  C   . VAL A 1 106 ? 57.915  20.956  29.384  1.00 10.06 ? 106  VAL A C   1 
ATOM   804  O  O   . VAL A 1 106 ? 57.702  20.845  30.589  1.00 12.08 ? 106  VAL A O   1 
ATOM   805  C  CB  . VAL A 1 106 ? 56.018  21.100  27.741  1.00 8.79  ? 106  VAL A CB  1 
ATOM   806  C  CG1 . VAL A 1 106 ? 55.151  20.324  28.718  1.00 10.09 ? 106  VAL A CG1 1 
ATOM   807  C  CG2 . VAL A 1 106 ? 55.158  22.112  26.903  1.00 9.03  ? 106  VAL A CG2 1 
ATOM   808  N  N   . PHE A 1 107 ? 58.884  20.283  28.765  1.00 11.50 ? 107  PHE A N   1 
ATOM   809  C  CA  . PHE A 1 107 ? 59.717  19.306  29.457  1.00 13.91 ? 107  PHE A CA  1 
ATOM   810  C  C   . PHE A 1 107 ? 60.800  19.940  30.331  1.00 16.15 ? 107  PHE A C   1 
ATOM   811  O  O   . PHE A 1 107 ? 61.173  19.383  31.367  1.00 15.68 ? 107  PHE A O   1 
ATOM   812  C  CB  . PHE A 1 107 ? 60.370  18.397  28.415  1.00 12.99 ? 107  PHE A CB  1 
ATOM   813  C  CG  . PHE A 1 107 ? 61.258  17.335  28.993  1.00 13.31 ? 107  PHE A CG  1 
ATOM   814  C  CD1 . PHE A 1 107 ? 60.718  16.178  29.545  1.00 13.80 ? 107  PHE A CD1 1 
ATOM   815  C  CD2 . PHE A 1 107 ? 62.640  17.483  28.966  1.00 14.74 ? 107  PHE A CD2 1 
ATOM   816  C  CE1 . PHE A 1 107 ? 61.543  15.181  30.059  1.00 13.69 ? 107  PHE A CE1 1 
ATOM   817  C  CE2 . PHE A 1 107 ? 63.474  16.492  29.478  1.00 15.09 ? 107  PHE A CE2 1 
ATOM   818  C  CZ  . PHE A 1 107 ? 62.923  15.339  30.024  1.00 13.46 ? 107  PHE A CZ  1 
ATOM   819  N  N   . ASN A 1 108 ? 61.241  21.149  29.943  1.00 21.71 ? 108  ASN A N   1 
ATOM   820  C  CA  . ASN A 1 108 ? 62.337  21.905  30.580  1.00 24.09 ? 108  ASN A CA  1 
ATOM   821  C  C   . ASN A 1 108 ? 62.436  21.868  32.093  1.00 23.13 ? 108  ASN A C   1 
ATOM   822  O  O   . ASN A 1 108 ? 63.457  21.403  32.643  1.00 26.58 ? 108  ASN A O   1 
ATOM   823  C  CB  . ASN A 1 108 ? 62.398  23.401  30.089  1.00 21.69 ? 108  ASN A CB  1 
ATOM   824  C  CG  . ASN A 1 108 ? 63.642  24.125  30.624  1.00 23.48 ? 108  ASN A CG  1 
ATOM   825  O  OD1 . ASN A 1 108 ? 64.723  23.689  30.383  1.00 22.62 ? 108  ASN A OD1 1 
ATOM   826  N  ND2 . ASN A 1 108 ? 63.459  25.224  31.373  1.00 25.00 ? 108  ASN A ND2 1 
ATOM   827  N  N   . ASN A 1 109 ? 61.415  22.351  32.766  1.00 24.61 ? 109  ASN A N   1 
ATOM   828  C  CA  . ASN A 1 109 ? 61.463  22.379  34.225  1.00 24.39 ? 109  ASN A CA  1 
ATOM   829  C  C   . ASN A 1 109 ? 60.509  21.331  34.757  1.00 21.16 ? 109  ASN A C   1 
ATOM   830  O  O   . ASN A 1 109 ? 60.052  21.455  35.874  1.00 23.11 ? 109  ASN A O   1 
ATOM   831  C  CB  . ASN A 1 109 ? 61.047  23.786  34.696  1.00 29.15 ? 109  ASN A CB  1 
ATOM   832  C  CG  . ASN A 1 109 ? 61.164  23.991  36.222  1.00 34.02 ? 109  ASN A CG  1 
ATOM   833  O  OD1 . ASN A 1 109 ? 62.278  24.116  36.777  1.00 37.12 ? 109  ASN A OD1 1 
ATOM   834  N  ND2 . ASN A 1 109 ? 60.009  24.043  36.902  1.00 35.95 ? 109  ASN A ND2 1 
ATOM   835  N  N   . GLY A 1 110 ? 60.186  20.303  33.958  1.00 16.69 ? 110  GLY A N   1 
ATOM   836  C  CA  . GLY A 1 110 ? 59.246  19.299  34.458  1.00 15.41 ? 110  GLY A CA  1 
ATOM   837  C  C   . GLY A 1 110 ? 57.864  19.407  33.833  1.00 13.54 ? 110  GLY A C   1 
ATOM   838  O  O   . GLY A 1 110 ? 57.212  20.471  33.873  1.00 13.24 ? 110  GLY A O   1 
ATOM   839  N  N   . ILE A 1 111 ? 57.425  18.296  33.208  1.00 12.37 ? 111  ILE A N   1 
ATOM   840  C  CA  . ILE A 1 111 ? 56.134  18.313  32.563  1.00 10.97 ? 111  ILE A CA  1 
ATOM   841  C  C   . ILE A 1 111 ? 55.013  18.602  33.504  1.00 11.51 ? 111  ILE A C   1 
ATOM   842  O  O   . ILE A 1 111 ? 54.122  19.413  33.199  1.00 10.58 ? 111  ILE A O   1 
ATOM   843  C  CB  . ILE A 1 111 ? 55.909  16.937  31.862  1.00 10.95 ? 111  ILE A CB  1 
ATOM   844  C  CG1 . ILE A 1 111 ? 56.926  16.803  30.734  1.00 12.18 ? 111  ILE A CG1 1 
ATOM   845  C  CG2 . ILE A 1 111 ? 54.470  16.852  31.332  1.00 11.11 ? 111  ILE A CG2 1 
ATOM   846  C  CD1 . ILE A 1 111 ? 56.794  15.435  30.015  1.00 12.31 ? 111  ILE A CD1 1 
ATOM   847  N  N   . ASP A 1 112 ? 54.999  17.939  34.662  1.00 12.24 ? 112  ASP A N   1 
ATOM   848  C  CA  . ASP A 1 112 ? 53.904  18.165  35.584  1.00 12.95 ? 112  ASP A CA  1 
ATOM   849  C  C   . ASP A 1 112 ? 53.868  19.620  36.050  1.00 12.77 ? 112  ASP A C   1 
ATOM   850  O  O   . ASP A 1 112 ? 52.774  20.220  36.091  1.00 14.47 ? 112  ASP A O   1 
ATOM   851  C  CB  . ASP A 1 112 ? 54.047  17.224  36.794  1.00 15.99 ? 112  ASP A CB  1 
ATOM   852  C  CG  . ASP A 1 112 ? 52.827  17.244  37.659  1.00 21.85 ? 112  ASP A CG  1 
ATOM   853  O  OD1 . ASP A 1 112 ? 51.779  16.663  37.251  1.00 20.49 ? 112  ASP A OD1 1 
ATOM   854  O  OD2 . ASP A 1 112 ? 52.919  17.898  38.725  1.00 24.91 ? 112  ASP A OD2 1 
ATOM   855  N  N   . ALA A 1 113 ? 55.036  20.201  36.354  1.00 12.47 ? 113  ALA A N   1 
ATOM   856  C  CA  . ALA A 1 113 ? 55.124  21.603  36.806  1.00 12.43 ? 113  ALA A CA  1 
ATOM   857  C  C   . ALA A 1 113 ? 54.603  22.547  35.740  1.00 12.22 ? 113  ALA A C   1 
ATOM   858  O  O   . ALA A 1 113 ? 53.999  23.570  36.038  1.00 14.43 ? 113  ALA A O   1 
ATOM   859  C  CB  . ALA A 1 113 ? 56.584  21.973  37.125  1.00 14.94 ? 113  ALA A CB  1 
ATOM   860  N  N   . PHE A 1 114 ? 54.839  22.217  34.477  1.00 11.74 ? 114  PHE A N   1 
ATOM   861  C  CA  . PHE A 1 114 ? 54.370  23.086  33.406  1.00 11.44 ? 114  PHE A CA  1 
ATOM   862  C  C   . PHE A 1 114 ? 52.849  23.168  33.380  1.00 11.34 ? 114  PHE A C   1 
ATOM   863  O  O   . PHE A 1 114 ? 52.271  24.257  33.333  1.00 11.04 ? 114  PHE A O   1 
ATOM   864  C  CB  . PHE A 1 114 ? 54.851  22.591  32.044  1.00 10.46 ? 114  PHE A CB  1 
ATOM   865  C  CG  . PHE A 1 114 ? 54.413  23.469  30.911  1.00 9.87  ? 114  PHE A CG  1 
ATOM   866  C  CD1 . PHE A 1 114 ? 55.110  24.633  30.614  1.00 11.43 ? 114  PHE A CD1 1 
ATOM   867  C  CD2 . PHE A 1 114 ? 53.262  23.172  30.185  1.00 9.73  ? 114  PHE A CD2 1 
ATOM   868  C  CE1 . PHE A 1 114 ? 54.670  25.493  29.614  1.00 11.44 ? 114  PHE A CE1 1 
ATOM   869  C  CE2 . PHE A 1 114 ? 52.812  24.027  29.184  1.00 10.60 ? 114  PHE A CE2 1 
ATOM   870  C  CZ  . PHE A 1 114 ? 53.519  25.192  28.899  1.00 11.55 ? 114  PHE A CZ  1 
ATOM   871  N  N   . TYR A 1 115 ? 52.190  22.016  33.389  1.00 10.21 ? 115  TYR A N   1 
ATOM   872  C  CA  . TYR A 1 115 ? 50.737  22.015  33.357  1.00 10.07 ? 115  TYR A CA  1 
ATOM   873  C  C   . TYR A 1 115 ? 50.138  22.600  34.633  1.00 10.78 ? 115  TYR A C   1 
ATOM   874  O  O   . TYR A 1 115 ? 49.060  23.191  34.599  1.00 11.78 ? 115  TYR A O   1 
ATOM   875  C  CB  . TYR A 1 115 ? 50.223  20.601  33.083  1.00 9.59  ? 115  TYR A CB  1 
ATOM   876  C  CG  . TYR A 1 115 ? 50.440  20.187  31.642  1.00 8.49  ? 115  TYR A CG  1 
ATOM   877  C  CD1 . TYR A 1 115 ? 49.550  20.579  30.642  1.00 9.58  ? 115  TYR A CD1 1 
ATOM   878  C  CD2 . TYR A 1 115 ? 51.557  19.438  31.272  1.00 9.00  ? 115  TYR A CD2 1 
ATOM   879  C  CE1 . TYR A 1 115 ? 49.767  20.233  29.301  1.00 9.43  ? 115  TYR A CE1 1 
ATOM   880  C  CE2 . TYR A 1 115 ? 51.785  19.091  29.941  1.00 8.86  ? 115  TYR A CE2 1 
ATOM   881  C  CZ  . TYR A 1 115 ? 50.889  19.488  28.961  1.00 9.35  ? 115  TYR A CZ  1 
ATOM   882  O  OH  . TYR A 1 115 ? 51.115  19.137  27.647  1.00 9.52  ? 115  TYR A OH  1 
ATOM   883  N  N   . ALA A 1 116 ? 50.829  22.399  35.770  1.00 12.45 ? 116  ALA A N   1 
ATOM   884  C  CA  . ALA A 1 116 ? 50.336  22.999  37.031  1.00 12.24 ? 116  ALA A CA  1 
ATOM   885  C  C   . ALA A 1 116 ? 50.390  24.538  36.909  1.00 13.62 ? 116  ALA A C   1 
ATOM   886  O  O   . ALA A 1 116 ? 49.479  25.226  37.390  1.00 14.67 ? 116  ALA A O   1 
ATOM   887  C  CB  . ALA A 1 116 ? 51.169  22.511  38.165  1.00 14.32 ? 116  ALA A CB  1 
ATOM   888  N  N   . ARG A 1 117 ? 51.421  25.082  36.252  1.00 12.22 ? 117  ARG A N   1 
ATOM   889  C  CA  . ARG A 1 117 ? 51.517  26.546  36.078  1.00 13.28 ? 117  ARG A CA  1 
ATOM   890  C  C   . ARG A 1 117 ? 50.387  27.020  35.145  1.00 12.25 ? 117  ARG A C   1 
ATOM   891  O  O   . ARG A 1 117 ? 49.756  28.085  35.359  1.00 12.57 ? 117  ARG A O   1 
ATOM   892  C  CB  . ARG A 1 117 ? 52.893  26.920  35.534  1.00 13.86 ? 117  ARG A CB  1 
ATOM   893  C  CG  . ARG A 1 117 ? 53.072  28.448  35.388  1.00 18.84 ? 117  ARG A CG  1 
ATOM   894  C  CD  . ARG A 1 117 ? 53.394  29.055  36.745  1.00 20.63 ? 117  ARG A CD  1 
ATOM   895  N  NE  . ARG A 1 117 ? 53.658  30.494  36.583  1.00 21.07 ? 117  ARG A NE  1 
ATOM   896  C  CZ  . ARG A 1 117 ? 52.914  31.452  37.131  1.00 23.79 ? 117  ARG A CZ  1 
ATOM   897  N  NH1 . ARG A 1 117 ? 51.871  31.156  37.899  1.00 24.94 ? 117  ARG A NH1 1 
ATOM   898  N  NH2 . ARG A 1 117 ? 53.185  32.723  36.855  1.00 23.42 ? 117  ARG A NH2 1 
ATOM   899  N  N   . CYS A 1 118 ? 50.102  26.259  34.086  1.00 11.50 ? 118  CYS A N   1 
ATOM   900  C  CA  . CYS A 1 118 ? 49.014  26.583  33.185  1.00 10.96 ? 118  CYS A CA  1 
ATOM   901  C  C   . CYS A 1 118 ? 47.704  26.667  33.981  1.00 11.40 ? 118  CYS A C   1 
ATOM   902  O  O   . CYS A 1 118 ? 46.895  27.559  33.784  1.00 11.34 ? 118  CYS A O   1 
ATOM   903  C  CB  . CYS A 1 118 ? 48.858  25.463  32.121  1.00 11.99 ? 118  CYS A CB  1 
ATOM   904  S  SG  . CYS A 1 118 ? 50.135  25.467  30.837  1.00 11.43 ? 118  CYS A SG  1 
ATOM   905  N  N   . GLU A 1 119 ? 47.457  25.703  34.874  1.00 11.45 ? 119  GLU A N   1 
ATOM   906  C  CA  . GLU A 1 119 ? 46.211  25.712  35.657  1.00 11.97 ? 119  GLU A CA  1 
ATOM   907  C  C   . GLU A 1 119 ? 46.153  26.952  36.564  1.00 11.99 ? 119  GLU A C   1 
ATOM   908  O  O   . GLU A 1 119 ? 45.083  27.602  36.688  1.00 13.79 ? 119  GLU A O   1 
ATOM   909  C  CB  . GLU A 1 119 ? 46.153  24.419  36.509  1.00 13.37 ? 119  GLU A CB  1 
ATOM   910  C  CG  . GLU A 1 119 ? 44.846  24.307  37.275  1.00 15.64 ? 119  GLU A CG  1 
ATOM   911  C  CD  . GLU A 1 119 ? 44.779  23.055  38.151  1.00 16.85 ? 119  GLU A CD  1 
ATOM   912  O  OE1 . GLU A 1 119 ? 45.825  22.519  38.549  1.00 18.85 ? 119  GLU A OE1 1 
ATOM   913  O  OE2 . GLU A 1 119 ? 43.624  22.671  38.443  1.00 22.05 ? 119  GLU A OE2 1 
ATOM   914  N  N   . GLN A 1 120 ? 47.294  27.280  37.139  1.00 11.97 ? 120  GLN A N   1 
ATOM   915  C  CA  . GLN A 1 120 ? 47.356  28.411  38.063  1.00 14.27 ? 120  GLN A CA  1 
ATOM   916  C  C   . GLN A 1 120 ? 46.997  29.718  37.372  1.00 15.09 ? 120  GLN A C   1 
ATOM   917  O  O   . GLN A 1 120 ? 46.279  30.555  37.936  1.00 15.49 ? 120  GLN A O   1 
ATOM   918  C  CB  . GLN A 1 120 ? 48.761  28.491  38.650  1.00 17.43 ? 120  GLN A CB  1 
ATOM   919  C  CG  . GLN A 1 120 ? 49.001  29.571  39.684  1.00 25.18 ? 120  GLN A CG  1 
ATOM   920  C  CD  . GLN A 1 120 ? 50.368  29.389  40.376  1.00 28.44 ? 120  GLN A CD  1 
ATOM   921  O  OE1 . GLN A 1 120 ? 51.362  28.936  39.754  1.00 31.10 ? 120  GLN A OE1 1 
ATOM   922  N  NE2 . GLN A 1 120 ? 50.427  29.753  41.673  1.00 32.20 ? 120  GLN A NE2 1 
ATOM   923  N  N   . VAL A 1 121 ? 47.437  29.897  36.134  1.00 12.65 ? 121  VAL A N   1 
ATOM   924  C  CA  . VAL A 1 121 ? 47.126  31.163  35.455  1.00 13.02 ? 121  VAL A CA  1 
ATOM   925  C  C   . VAL A 1 121 ? 45.803  31.159  34.724  1.00 14.04 ? 121  VAL A C   1 
ATOM   926  O  O   . VAL A 1 121 ? 45.331  32.216  34.250  1.00 16.84 ? 121  VAL A O   1 
ATOM   927  C  CB  . VAL A 1 121 ? 48.269  31.624  34.500  1.00 11.26 ? 121  VAL A CB  1 
ATOM   928  C  CG1 . VAL A 1 121 ? 49.610  31.724  35.274  1.00 15.07 ? 121  VAL A CG1 1 
ATOM   929  C  CG2 . VAL A 1 121 ? 48.409  30.642  33.309  1.00 13.71 ? 121  VAL A CG2 1 
ATOM   930  N  N   . GLY A 1 122 ? 45.179  29.986  34.611  1.00 12.51 ? 122  GLY A N   1 
ATOM   931  C  CA  . GLY A 1 122 ? 43.892  29.905  33.967  1.00 11.37 ? 122  GLY A CA  1 
ATOM   932  C  C   . GLY A 1 122 ? 43.867  29.514  32.486  1.00 11.94 ? 122  GLY A C   1 
ATOM   933  O  O   . GLY A 1 122 ? 42.905  29.798  31.816  1.00 11.98 ? 122  GLY A O   1 
ATOM   934  N  N   . VAL A 1 123 ? 44.942  28.917  31.987  1.00 10.66 ? 123  VAL A N   1 
ATOM   935  C  CA  . VAL A 1 123 ? 44.963  28.396  30.613  1.00 10.30 ? 123  VAL A CA  1 
ATOM   936  C  C   . VAL A 1 123 ? 43.972  27.188  30.540  1.00 10.35 ? 123  VAL A C   1 
ATOM   937  O  O   . VAL A 1 123 ? 43.805  26.446  31.535  1.00 12.38 ? 123  VAL A O   1 
ATOM   938  C  CB  . VAL A 1 123 ? 46.415  27.875  30.334  1.00 11.43 ? 123  VAL A CB  1 
ATOM   939  C  CG1 . VAL A 1 123 ? 46.446  26.904  29.164  1.00 11.50 ? 123  VAL A CG1 1 
ATOM   940  C  CG2 . VAL A 1 123 ? 47.349  29.093  30.035  1.00 12.73 ? 123  VAL A CG2 1 
ATOM   941  N  N   . ASP A 1 124 ? 43.392  26.999  29.363  1.00 9.95  ? 124  ASP A N   1 
ATOM   942  C  CA  . ASP A 1 124 ? 42.418  25.893  29.155  1.00 10.52 ? 124  ASP A CA  1 
ATOM   943  C  C   . ASP A 1 124 ? 42.960  24.695  28.398  1.00 10.99 ? 124  ASP A C   1 
ATOM   944  O  O   . ASP A 1 124 ? 42.513  23.546  28.635  1.00 12.60 ? 124  ASP A O   1 
ATOM   945  C  CB  . ASP A 1 124 ? 41.175  26.411  28.406  1.00 12.12 ? 124  ASP A CB  1 
ATOM   946  C  CG  . ASP A 1 124 ? 40.465  27.464  29.199  1.00 12.70 ? 124  ASP A CG  1 
ATOM   947  O  OD1 . ASP A 1 124 ? 39.911  27.106  30.285  1.00 13.78 ? 124  ASP A OD1 1 
ATOM   948  O  OD2 . ASP A 1 124 ? 40.504  28.638  28.765  1.00 13.37 ? 124  ASP A OD2 1 
ATOM   949  N  N   . SER A 1 125 ? 43.883  24.927  27.482  1.00 8.56  ? 125  SER A N   1 
ATOM   950  C  CA  . SER A 1 125 ? 44.399  23.801  26.675  1.00 9.35  ? 125  SER A CA  1 
ATOM   951  C  C   . SER A 1 125 ? 45.824  24.072  26.277  1.00 9.88  ? 125  SER A C   1 
ATOM   952  O  O   . SER A 1 125 ? 46.304  25.214  26.337  1.00 8.76  ? 125  SER A O   1 
ATOM   953  C  CB  . SER A 1 125 ? 43.573  23.590  25.363  1.00 11.22 ? 125  SER A CB  1 
ATOM   954  O  OG  . SER A 1 125 ? 43.791  24.657  24.423  1.00 11.42 ? 125  SER A OG  1 
ATOM   955  N  N   . VAL A 1 126 ? 46.507  23.007  25.871  1.00 8.36  ? 126  VAL A N   1 
ATOM   956  C  CA  . VAL A 1 126 ? 47.896  23.077  25.378  1.00 8.50  ? 126  VAL A CA  1 
ATOM   957  C  C   . VAL A 1 126 ? 48.073  22.128  24.213  1.00 8.69  ? 126  VAL A C   1 
ATOM   958  O  O   . VAL A 1 126 ? 47.729  20.938  24.336  1.00 9.04  ? 126  VAL A O   1 
ATOM   959  C  CB  . VAL A 1 126 ? 48.918  22.662  26.505  1.00 8.45  ? 126  VAL A CB  1 
ATOM   960  C  CG1 . VAL A 1 126 ? 50.348  22.587  25.955  1.00 8.62  ? 126  VAL A CG1 1 
ATOM   961  C  CG2 . VAL A 1 126 ? 48.890  23.704  27.652  1.00 9.90  ? 126  VAL A CG2 1 
ATOM   962  N  N   . LEU A 1 127 ? 48.567  22.662  23.097  1.00 9.29  ? 127  LEU A N   1 
ATOM   963  C  CA  . LEU A 1 127 ? 48.954  21.887  21.905  1.00 9.03  ? 127  LEU A CA  1 
ATOM   964  C  C   . LEU A 1 127 ? 50.461  21.903  21.875  1.00 9.86  ? 127  LEU A C   1 
ATOM   965  O  O   . LEU A 1 127 ? 51.053  22.966  21.843  1.00 9.89  ? 127  LEU A O   1 
ATOM   966  C  CB  . LEU A 1 127 ? 48.374  22.546  20.640  1.00 10.89 ? 127  LEU A CB  1 
ATOM   967  C  CG  . LEU A 1 127 ? 48.873  21.898  19.337  1.00 15.78 ? 127  LEU A CG  1 
ATOM   968  C  CD1 . LEU A 1 127 ? 48.752  20.381  19.323  1.00 16.10 ? 127  LEU A CD1 1 
ATOM   969  C  CD2 . LEU A 1 127 ? 48.054  22.534  18.188  1.00 16.05 ? 127  LEU A CD2 1 
ATOM   970  N  N   . VAL A 1 128 ? 51.114  20.735  21.949  1.00 8.94  ? 128  VAL A N   1 
ATOM   971  C  CA  . VAL A 1 128 ? 52.595  20.647  21.871  1.00 9.03  ? 128  VAL A CA  1 
ATOM   972  C  C   . VAL A 1 128 ? 52.859  20.166  20.457  1.00 10.03 ? 128  VAL A C   1 
ATOM   973  O  O   . VAL A 1 128 ? 52.574  19.011  20.091  1.00 10.62 ? 128  VAL A O   1 
ATOM   974  C  CB  . VAL A 1 128 ? 53.164  19.671  22.890  1.00 8.68  ? 128  VAL A CB  1 
ATOM   975  C  CG1 . VAL A 1 128 ? 54.719  19.854  22.893  1.00 9.99  ? 128  VAL A CG1 1 
ATOM   976  C  CG2 . VAL A 1 128 ? 52.595  19.917  24.318  1.00 9.21  ? 128  VAL A CG2 1 
ATOM   977  N  N   . ALA A 1 129 ? 53.368  21.073  19.636  1.00 11.08 ? 129  ALA A N   1 
ATOM   978  C  CA  . ALA A 1 129 ? 53.464  20.821  18.209  1.00 11.59 ? 129  ALA A CA  1 
ATOM   979  C  C   . ALA A 1 129 ? 54.301  19.632  17.776  1.00 12.38 ? 129  ALA A C   1 
ATOM   980  O  O   . ALA A 1 129 ? 53.968  19.017  16.743  1.00 13.91 ? 129  ALA A O   1 
ATOM   981  C  CB  . ALA A 1 129 ? 53.940  22.101  17.503  1.00 14.26 ? 129  ALA A CB  1 
ATOM   982  N  N   . ASP A 1 130 ? 55.375  19.363  18.507  1.00 10.50 ? 130  ASP A N   1 
ATOM   983  C  CA  . ASP A 1 130 ? 56.262  18.270  18.144  1.00 10.33 ? 130  ASP A CA  1 
ATOM   984  C  C   . ASP A 1 130 ? 56.140  17.035  19.001  1.00 11.12 ? 130  ASP A C   1 
ATOM   985  O  O   . ASP A 1 130 ? 57.088  16.226  19.162  1.00 11.89 ? 130  ASP A O   1 
ATOM   986  C  CB  . ASP A 1 130 ? 57.715  18.775  18.078  1.00 10.83 ? 130  ASP A CB  1 
ATOM   987  C  CG  . ASP A 1 130 ? 58.183  19.471  19.362  1.00 12.33 ? 130  ASP A CG  1 
ATOM   988  O  OD1 . ASP A 1 130 ? 57.359  19.848  20.226  1.00 11.73 ? 130  ASP A OD1 1 
ATOM   989  O  OD2 . ASP A 1 130 ? 59.403  19.675  19.543  1.00 13.07 ? 130  ASP A OD2 1 
ATOM   990  N  N   . VAL A 1 131 ? 54.960  16.858  19.579  1.00 9.79  ? 131  VAL A N   1 
ATOM   991  C  CA  . VAL A 1 131 ? 54.669  15.637  20.332  1.00 10.28 ? 131  VAL A CA  1 
ATOM   992  C  C   . VAL A 1 131 ? 53.506  14.904  19.646  1.00 10.80 ? 131  VAL A C   1 
ATOM   993  O  O   . VAL A 1 131 ? 52.300  15.315  19.760  1.00 11.72 ? 131  VAL A O   1 
ATOM   994  C  CB  . VAL A 1 131 ? 54.292  15.938  21.791  1.00 10.15 ? 131  VAL A CB  1 
ATOM   995  C  CG1 . VAL A 1 131 ? 53.861  14.617  22.508  1.00 12.60 ? 131  VAL A CG1 1 
ATOM   996  C  CG2 . VAL A 1 131 ? 55.462  16.576  22.500  1.00 11.83 ? 131  VAL A CG2 1 
ATOM   997  N  N   . PRO A 1 132 ? 53.804  13.827  18.895  1.00 9.34  ? 132  PRO A N   1 
ATOM   998  C  CA  . PRO A 1 132 ? 52.737  13.065  18.224  1.00 10.94 ? 132  PRO A CA  1 
ATOM   999  C  C   . PRO A 1 132 ? 52.022  12.211  19.252  1.00 10.87 ? 132  PRO A C   1 
ATOM   1000 O  O   . PRO A 1 132 ? 52.471  12.057  20.381  1.00 10.09 ? 132  PRO A O   1 
ATOM   1001 C  CB  . PRO A 1 132 ? 53.493  12.236  17.199  1.00 9.89  ? 132  PRO A CB  1 
ATOM   1002 C  CG  . PRO A 1 132 ? 54.755  11.856  17.919  1.00 10.67 ? 132  PRO A CG  1 
ATOM   1003 C  CD  . PRO A 1 132 ? 55.136  13.225  18.650  1.00 9.24  ? 132  PRO A CD  1 
ATOM   1004 N  N   . VAL A 1 133 ? 50.850  11.680  18.861  1.00 11.76 ? 133  VAL A N   1 
ATOM   1005 C  CA  . VAL A 1 133 ? 50.111  10.860  19.823  1.00 13.38 ? 133  VAL A CA  1 
ATOM   1006 C  C   . VAL A 1 133 ? 50.970  9.729   20.407  1.00 12.08 ? 133  VAL A C   1 
ATOM   1007 O  O   . VAL A 1 133 ? 50.855  9.398   21.606  1.00 12.20 ? 133  VAL A O   1 
ATOM   1008 C  CB  . VAL A 1 133 ? 48.766  10.252  19.238  1.00 15.14 ? 133  VAL A CB  1 
ATOM   1009 C  CG1 . VAL A 1 133 ? 47.766  11.383  19.007  1.00 19.26 ? 133  VAL A CG1 1 
ATOM   1010 C  CG2 . VAL A 1 133 ? 49.004  9.386   18.019  1.00 16.63 ? 133  VAL A CG2 1 
ATOM   1011 N  N   . GLU A 1 134 ? 51.861  9.195   19.591  1.00 12.88 ? 134  GLU A N   1 
ATOM   1012 C  CA  . GLU A 1 134 ? 52.697  8.112   20.036  1.00 14.00 ? 134  GLU A CA  1 
ATOM   1013 C  C   . GLU A 1 134 ? 53.608  8.450   21.226  1.00 13.18 ? 134  GLU A C   1 
ATOM   1014 O  O   . GLU A 1 134 ? 54.037  7.540   21.975  1.00 16.18 ? 134  GLU A O   1 
ATOM   1015 C  CB  . GLU A 1 134 ? 53.548  7.634   18.857  1.00 14.89 ? 134  GLU A CB  1 
ATOM   1016 C  CG  . GLU A 1 134 ? 52.820  6.980   17.679  1.00 18.07 ? 134  GLU A CG  1 
ATOM   1017 C  CD  . GLU A 1 134 ? 52.101  7.903   16.692  1.00 17.64 ? 134  GLU A CD  1 
ATOM   1018 O  OE1 . GLU A 1 134 ? 52.008  9.142   16.852  1.00 15.95 ? 134  GLU A OE1 1 
ATOM   1019 O  OE2 . GLU A 1 134 ? 51.552  7.361   15.655  1.00 21.23 ? 134  GLU A OE2 1 
ATOM   1020 N  N   . GLU A 1 135 ? 53.950  9.741   21.410  1.00 11.58 ? 135  GLU A N   1 
ATOM   1021 C  CA  . GLU A 1 135 ? 54.844  10.149  22.512  1.00 10.74 ? 135  GLU A CA  1 
ATOM   1022 C  C   . GLU A 1 135 ? 54.085  10.938  23.543  1.00 10.43 ? 135  GLU A C   1 
ATOM   1023 O  O   . GLU A 1 135 ? 54.671  11.514  24.478  1.00 10.82 ? 135  GLU A O   1 
ATOM   1024 C  CB  . GLU A 1 135 ? 55.979  11.098  22.011  1.00 12.23 ? 135  GLU A CB  1 
ATOM   1025 C  CG  . GLU A 1 135 ? 56.996  10.471  21.057  1.00 12.20 ? 135  GLU A CG  1 
ATOM   1026 C  CD  . GLU A 1 135 ? 57.881  9.424   21.731  1.00 11.84 ? 135  GLU A CD  1 
ATOM   1027 O  OE1 . GLU A 1 135 ? 57.749  9.219   22.963  1.00 13.85 ? 135  GLU A OE1 1 
ATOM   1028 O  OE2 . GLU A 1 135 ? 58.697  8.836   20.985  1.00 13.04 ? 135  GLU A OE2 1 
ATOM   1029 N  N   . SER A 1 136 ? 52.768  10.987  23.357  1.00 10.05 ? 136  SER A N   1 
ATOM   1030 C  CA  . SER A 1 136 ? 51.961  11.888  24.223  1.00 9.30  ? 136  SER A CA  1 
ATOM   1031 C  C   . SER A 1 136 ? 51.601  11.519  25.647  1.00 9.53  ? 136  SER A C   1 
ATOM   1032 O  O   . SER A 1 136 ? 51.169  12.362  26.399  1.00 10.50 ? 136  SER A O   1 
ATOM   1033 C  CB  . SER A 1 136 ? 50.641  12.211  23.527  1.00 11.27 ? 136  SER A CB  1 
ATOM   1034 O  OG  . SER A 1 136 ? 49.781  11.087  23.508  1.00 12.63 ? 136  SER A OG  1 
ATOM   1035 N  N   . ALA A 1 137 ? 51.810  10.277  26.037  1.00 9.32  ? 137  ALA A N   1 
ATOM   1036 C  CA  . ALA A 1 137 ? 51.340  9.872   27.362  1.00 9.90  ? 137  ALA A CA  1 
ATOM   1037 C  C   . ALA A 1 137 ? 51.675  10.752  28.555  1.00 10.47 ? 137  ALA A C   1 
ATOM   1038 O  O   . ALA A 1 137 ? 50.765  11.183  29.235  1.00 10.24 ? 137  ALA A O   1 
ATOM   1039 C  CB  . ALA A 1 137 ? 51.786  8.437   27.627  1.00 10.82 ? 137  ALA A CB  1 
ATOM   1040 N  N   . PRO A 1 138 ? 52.929  11.098  28.774  1.00 9.98  ? 138  PRO A N   1 
ATOM   1041 C  CA  . PRO A 1 138 ? 53.168  11.934  29.962  1.00 9.81  ? 138  PRO A CA  1 
ATOM   1042 C  C   . PRO A 1 138 ? 52.584  13.334  29.880  1.00 10.58 ? 138  PRO A C   1 
ATOM   1043 O  O   . PRO A 1 138 ? 52.249  13.939  30.925  1.00 10.80 ? 138  PRO A O   1 
ATOM   1044 C  CB  . PRO A 1 138 ? 54.708  11.966  30.127  1.00 11.24 ? 138  PRO A CB  1 
ATOM   1045 C  CG  . PRO A 1 138 ? 55.179  11.646  28.795  1.00 11.69 ? 138  PRO A CG  1 
ATOM   1046 C  CD  . PRO A 1 138 ? 54.184  10.677  28.128  1.00 10.30 ? 138  PRO A CD  1 
ATOM   1047 N  N   . PHE A 1 139 ? 52.452  13.826  28.663  1.00 9.42  ? 139  PHE A N   1 
ATOM   1048 C  CA  . PHE A 1 139 ? 51.896  15.155  28.466  1.00 10.26 ? 139  PHE A CA  1 
ATOM   1049 C  C   . PHE A 1 139 ? 50.397  15.166  28.708  1.00 10.58 ? 139  PHE A C   1 
ATOM   1050 O  O   . PHE A 1 139 ? 49.894  16.010  29.452  1.00 10.71 ? 139  PHE A O   1 
ATOM   1051 C  CB  . PHE A 1 139 ? 52.198  15.668  27.053  1.00 10.17 ? 139  PHE A CB  1 
ATOM   1052 C  CG  . PHE A 1 139 ? 53.665  15.826  26.768  1.00 10.08 ? 139  PHE A CG  1 
ATOM   1053 C  CD1 . PHE A 1 139 ? 54.421  14.747  26.318  1.00 10.81 ? 139  PHE A CD1 1 
ATOM   1054 C  CD2 . PHE A 1 139 ? 54.298  17.049  26.971  1.00 11.49 ? 139  PHE A CD2 1 
ATOM   1055 C  CE1 . PHE A 1 139 ? 55.790  14.884  26.074  1.00 10.71 ? 139  PHE A CE1 1 
ATOM   1056 C  CE2 . PHE A 1 139 ? 55.666  17.196  26.731  1.00 11.47 ? 139  PHE A CE2 1 
ATOM   1057 C  CZ  . PHE A 1 139 ? 56.412  16.110  26.281  1.00 11.76 ? 139  PHE A CZ  1 
ATOM   1058 N  N   . ARG A 1 140 ? 49.695  14.196  28.109  1.00 10.30 ? 140  ARG A N   1 
ATOM   1059 C  CA  . ARG A 1 140 ? 48.245  14.159  28.272  1.00 10.09 ? 140  ARG A CA  1 
ATOM   1060 C  C   . ARG A 1 140 ? 47.900  13.803  29.712  1.00 10.66 ? 140  ARG A C   1 
ATOM   1061 O  O   . ARG A 1 140 ? 46.928  14.337  30.241  1.00 10.86 ? 140  ARG A O   1 
ATOM   1062 C  CB  . ARG A 1 140 ? 47.572  13.236  27.227  1.00 13.98 ? 140  ARG A CB  1 
ATOM   1063 C  CG  . ARG A 1 140 ? 47.848  11.771  27.363  1.00 16.89 ? 140  ARG A CG  1 
ATOM   1064 C  CD  . ARG A 1 140 ? 47.239  10.984  26.117  1.00 19.78 ? 140  ARG A CD  1 
ATOM   1065 N  NE  . ARG A 1 140 ? 47.131  9.538   26.477  1.00 23.81 ? 140  ARG A NE  1 
ATOM   1066 C  CZ  . ARG A 1 140 ? 47.942  8.594   26.019  1.00 22.93 ? 140  ARG A CZ  1 
ATOM   1067 N  NH1 . ARG A 1 140 ? 48.881  8.923   25.173  1.00 25.14 ? 140  ARG A NH1 1 
ATOM   1068 N  NH2 . ARG A 1 140 ? 47.857  7.333   26.452  1.00 27.33 ? 140  ARG A NH2 1 
ATOM   1069 N  N   . GLN A 1 141 ? 48.660  12.934  30.367  1.00 10.60 ? 141  GLN A N   1 
ATOM   1070 C  CA  . GLN A 1 141 ? 48.372  12.615  31.773  1.00 11.00 ? 141  GLN A CA  1 
ATOM   1071 C  C   . GLN A 1 141 ? 48.519  13.834  32.675  1.00 11.14 ? 141  GLN A C   1 
ATOM   1072 O  O   . GLN A 1 141 ? 47.658  14.093  33.550  1.00 12.08 ? 141  GLN A O   1 
ATOM   1073 C  CB  . GLN A 1 141 ? 49.305  11.524  32.267  1.00 10.72 ? 141  GLN A CB  1 
ATOM   1074 C  CG  . GLN A 1 141 ? 48.997  10.230  31.478  1.00 12.12 ? 141  GLN A CG  1 
ATOM   1075 C  CD  . GLN A 1 141 ? 50.163  9.240   31.414  1.00 12.51 ? 141  GLN A CD  1 
ATOM   1076 O  OE1 . GLN A 1 141 ? 51.257  9.450   31.941  1.00 13.91 ? 141  GLN A OE1 1 
ATOM   1077 N  NE2 . GLN A 1 141 ? 49.867  8.111   30.736  1.00 13.97 ? 141  GLN A NE2 1 
ATOM   1078 N  N   . ALA A 1 142 ? 49.628  14.564  32.492  1.00 10.49 ? 142  ALA A N   1 
ATOM   1079 C  CA  . ALA A 1 142 ? 49.826  15.755  33.292  1.00 10.12 ? 142  ALA A CA  1 
ATOM   1080 C  C   . ALA A 1 142 ? 48.763  16.801  32.994  1.00 11.06 ? 142  ALA A C   1 
ATOM   1081 O  O   . ALA A 1 142 ? 48.312  17.493  33.929  1.00 9.43  ? 142  ALA A O   1 
ATOM   1082 C  CB  . ALA A 1 142 ? 51.221  16.351  33.043  1.00 9.60  ? 142  ALA A CB  1 
ATOM   1083 N  N   . ALA A 1 143 ? 48.410  16.981  31.726  1.00 10.25 ? 143  ALA A N   1 
ATOM   1084 C  CA  . ALA A 1 143 ? 47.352  17.914  31.380  1.00 10.18 ? 143  ALA A CA  1 
ATOM   1085 C  C   . ALA A 1 143 ? 46.078  17.595  32.151  1.00 11.44 ? 143  ALA A C   1 
ATOM   1086 O  O   . ALA A 1 143 ? 45.515  18.464  32.870  1.00 12.22 ? 143  ALA A O   1 
ATOM   1087 C  CB  . ALA A 1 143 ? 47.081  17.893  29.845  1.00 10.35 ? 143  ALA A CB  1 
ATOM   1088 N  N   . LEU A 1 144 ? 45.653  16.332  32.074  1.00 10.63 ? 144  LEU A N   1 
ATOM   1089 C  CA  . LEU A 1 144 ? 44.383  15.964  32.727  1.00 10.40 ? 144  LEU A CA  1 
ATOM   1090 C  C   . LEU A 1 144 ? 44.477  16.101  34.235  1.00 10.41 ? 144  LEU A C   1 
ATOM   1091 O  O   . LEU A 1 144 ? 43.471  16.512  34.838  1.00 13.20 ? 144  LEU A O   1 
ATOM   1092 C  CB  . LEU A 1 144 ? 43.975  14.520  32.310  1.00 12.01 ? 144  LEU A CB  1 
ATOM   1093 C  CG  . LEU A 1 144 ? 43.715  14.368  30.811  1.00 15.14 ? 144  LEU A CG  1 
ATOM   1094 C  CD1 . LEU A 1 144 ? 43.559  12.848  30.541  1.00 17.92 ? 144  LEU A CD1 1 
ATOM   1095 C  CD2 . LEU A 1 144 ? 42.438  15.079  30.360  1.00 16.78 ? 144  LEU A CD2 1 
ATOM   1096 N  N   . ARG A 1 145 ? 45.628  15.811  34.843  1.00 11.55 ? 145  ARG A N   1 
ATOM   1097 C  CA  . ARG A 1 145 ? 45.752  15.978  36.314  1.00 11.14 ? 145  ARG A CA  1 
ATOM   1098 C  C   . ARG A 1 145 ? 45.549  17.406  36.725  1.00 14.10 ? 145  ARG A C   1 
ATOM   1099 O  O   . ARG A 1 145 ? 45.137  17.656  37.885  1.00 16.98 ? 145  ARG A O   1 
ATOM   1100 C  CB  . ARG A 1 145 ? 47.117  15.551  36.845  1.00 11.99 ? 145  ARG A CB  1 
ATOM   1101 C  CG  . ARG A 1 145 ? 47.219  13.997  36.909  1.00 12.43 ? 145  ARG A CG  1 
ATOM   1102 C  CD  . ARG A 1 145 ? 48.429  13.595  37.658  1.00 13.88 ? 145  ARG A CD  1 
ATOM   1103 N  NE  . ARG A 1 145 ? 49.697  14.111  37.135  1.00 14.49 ? 145  ARG A NE  1 
ATOM   1104 C  CZ  . ARG A 1 145 ? 50.427  13.510  36.207  1.00 14.43 ? 145  ARG A CZ  1 
ATOM   1105 N  NH1 . ARG A 1 145 ? 50.046  12.361  35.649  1.00 13.68 ? 145  ARG A NH1 1 
ATOM   1106 N  NH2 . ARG A 1 145 ? 51.591  14.050  35.848  1.00 14.75 ? 145  ARG A NH2 1 
ATOM   1107 N  N   . HIS A 1 146 ? 45.861  18.345  35.832  1.00 13.34 ? 146  HIS A N   1 
ATOM   1108 C  CA  . HIS A 1 146 ? 45.738  19.759  36.165  1.00 13.51 ? 146  HIS A CA  1 
ATOM   1109 C  C   . HIS A 1 146 ? 44.603  20.485  35.459  1.00 13.29 ? 146  HIS A C   1 
ATOM   1110 O  O   . HIS A 1 146 ? 44.626  21.706  35.314  1.00 14.02 ? 146  HIS A O   1 
ATOM   1111 C  CB  . HIS A 1 146 ? 47.070  20.467  35.917  1.00 14.02 ? 146  HIS A CB  1 
ATOM   1112 C  CG  . HIS A 1 146 ? 48.175  19.966  36.792  1.00 15.53 ? 146  HIS A CG  1 
ATOM   1113 N  ND1 . HIS A 1 146 ? 48.998  18.920  36.433  1.00 15.35 ? 146  HIS A ND1 1 
ATOM   1114 C  CD2 . HIS A 1 146 ? 48.544  20.321  38.046  1.00 17.39 ? 146  HIS A CD2 1 
ATOM   1115 C  CE1 . HIS A 1 146 ? 49.825  18.651  37.428  1.00 15.95 ? 146  HIS A CE1 1 
ATOM   1116 N  NE2 . HIS A 1 146 ? 49.570  19.486  38.419  1.00 21.05 ? 146  HIS A NE2 1 
ATOM   1117 N  N   . ASN A 1 147 ? 43.615  19.729  34.985  1.00 13.85 ? 147  ASN A N   1 
ATOM   1118 C  CA  . ASN A 1 147 ? 42.427  20.304  34.360  1.00 14.49 ? 147  ASN A CA  1 
ATOM   1119 C  C   . ASN A 1 147 ? 42.712  21.104  33.113  1.00 13.37 ? 147  ASN A C   1 
ATOM   1120 O  O   . ASN A 1 147 ? 42.004  22.076  32.790  1.00 15.78 ? 147  ASN A O   1 
ATOM   1121 C  CB  . ASN A 1 147 ? 41.666  21.158  35.412  1.00 16.72 ? 147  ASN A CB  1 
ATOM   1122 C  CG  . ASN A 1 147 ? 41.300  20.325  36.613  1.00 19.66 ? 147  ASN A CG  1 
ATOM   1123 O  OD1 . ASN A 1 147 ? 40.586  19.319  36.457  1.00 22.72 ? 147  ASN A OD1 1 
ATOM   1124 N  ND2 . ASN A 1 147 ? 41.819  20.671  37.789  1.00 20.85 ? 147  ASN A ND2 1 
ATOM   1125 N  N   . ILE A 1 148 ? 43.746  20.641  32.387  1.00 11.43 ? 148  ILE A N   1 
ATOM   1126 C  CA  . ILE A 1 148 ? 44.102  21.271  31.112  1.00 9.71  ? 148  ILE A CA  1 
ATOM   1127 C  C   . ILE A 1 148 ? 43.735  20.310  30.001  1.00 11.00 ? 148  ILE A C   1 
ATOM   1128 O  O   . ILE A 1 148 ? 43.972  19.090  30.134  1.00 11.84 ? 148  ILE A O   1 
ATOM   1129 C  CB  . ILE A 1 148 ? 45.625  21.550  31.048  1.00 10.27 ? 148  ILE A CB  1 
ATOM   1130 C  CG1 . ILE A 1 148 ? 46.079  22.415  32.270  1.00 10.19 ? 148  ILE A CG1 1 
ATOM   1131 C  CG2 . ILE A 1 148 ? 46.016  22.148  29.667  1.00 10.42 ? 148  ILE A CG2 1 
ATOM   1132 C  CD1 . ILE A 1 148 ? 45.345  23.809  32.339  1.00 12.31 ? 148  ILE A CD1 1 
ATOM   1133 N  N   . ALA A 1 149 ? 43.179  20.810  28.927  1.00 10.40 ? 149  ALA A N   1 
ATOM   1134 C  CA  . ALA A 1 149 ? 42.830  19.917  27.811  1.00 10.75 ? 149  ALA A CA  1 
ATOM   1135 C  C   . ALA A 1 149 ? 44.065  19.702  26.934  1.00 11.61 ? 149  ALA A C   1 
ATOM   1136 O  O   . ALA A 1 149 ? 44.681  20.646  26.448  1.00 10.77 ? 149  ALA A O   1 
ATOM   1137 C  CB  . ALA A 1 149 ? 41.742  20.559  26.950  1.00 12.94 ? 149  ALA A CB  1 
ATOM   1138 N  N   . PRO A 1 150 ? 44.472  18.442  26.711  1.00 11.33 ? 150  PRO A N   1 
ATOM   1139 C  CA  . PRO A 1 150 ? 45.626  18.195  25.816  1.00 10.15 ? 150  PRO A CA  1 
ATOM   1140 C  C   . PRO A 1 150 ? 45.037  18.143  24.374  1.00 11.76 ? 150  PRO A C   1 
ATOM   1141 O  O   . PRO A 1 150 ? 44.046  17.427  24.123  1.00 12.80 ? 150  PRO A O   1 
ATOM   1142 C  CB  . PRO A 1 150 ? 46.157  16.821  26.278  1.00 12.30 ? 150  PRO A CB  1 
ATOM   1143 C  CG  . PRO A 1 150 ? 44.884  16.116  26.857  1.00 12.41 ? 150  PRO A CG  1 
ATOM   1144 C  CD  . PRO A 1 150 ? 43.943  17.223  27.365  1.00 12.08 ? 150  PRO A CD  1 
ATOM   1145 N  N   . ILE A 1 151 ? 45.604  18.913  23.459  1.00 10.31 ? 151  ILE A N   1 
ATOM   1146 C  CA  . ILE A 1 151 ? 45.093  19.018  22.088  1.00 10.30 ? 151  ILE A CA  1 
ATOM   1147 C  C   . ILE A 1 151 ? 45.969  18.208  21.178  1.00 11.05 ? 151  ILE A C   1 
ATOM   1148 O  O   . ILE A 1 151 ? 47.211  18.235  21.243  1.00 12.45 ? 151  ILE A O   1 
ATOM   1149 C  CB  . ILE A 1 151 ? 45.158  20.507  21.615  1.00 11.02 ? 151  ILE A CB  1 
ATOM   1150 C  CG1 . ILE A 1 151 ? 44.440  21.414  22.628  1.00 11.42 ? 151  ILE A CG1 1 
ATOM   1151 C  CG2 . ILE A 1 151 ? 44.634  20.654  20.221  1.00 11.27 ? 151  ILE A CG2 1 
ATOM   1152 C  CD1 . ILE A 1 151 ? 42.969  21.032  22.805  1.00 10.84 ? 151  ILE A CD1 1 
ATOM   1153 N  N   . PHE A 1 152 ? 45.315  17.511  20.272  1.00 12.60 ? 152  PHE A N   1 
ATOM   1154 C  CA  . PHE A 1 152 ? 46.019  16.698  19.299  1.00 13.75 ? 152  PHE A CA  1 
ATOM   1155 C  C   . PHE A 1 152 ? 45.644  17.075  17.883  1.00 13.17 ? 152  PHE A C   1 
ATOM   1156 O  O   . PHE A 1 152 ? 44.496  17.425  17.597  1.00 13.36 ? 152  PHE A O   1 
ATOM   1157 C  CB  . PHE A 1 152 ? 45.741  15.223  19.559  1.00 16.17 ? 152  PHE A CB  1 
ATOM   1158 C  CG  . PHE A 1 152 ? 46.309  14.745  20.854  1.00 18.56 ? 152  PHE A CG  1 
ATOM   1159 C  CD1 . PHE A 1 152 ? 47.688  14.649  21.024  1.00 21.02 ? 152  PHE A CD1 1 
ATOM   1160 C  CD2 . PHE A 1 152 ? 45.477  14.453  21.928  1.00 19.84 ? 152  PHE A CD2 1 
ATOM   1161 C  CE1 . PHE A 1 152 ? 48.232  14.273  22.250  1.00 22.34 ? 152  PHE A CE1 1 
ATOM   1162 C  CE2 . PHE A 1 152 ? 46.009  14.076  23.159  1.00 21.54 ? 152  PHE A CE2 1 
ATOM   1163 C  CZ  . PHE A 1 152 ? 47.388  13.986  23.321  1.00 23.24 ? 152  PHE A CZ  1 
ATOM   1164 N  N   . ILE A 1 153 ? 46.611  17.010  17.003  1.00 14.74 ? 153  ILE A N   1 
ATOM   1165 C  CA  . ILE A 1 153 ? 46.429  17.352  15.606  1.00 13.94 ? 153  ILE A CA  1 
ATOM   1166 C  C   . ILE A 1 153 ? 46.026  16.080  14.857  1.00 16.94 ? 153  ILE A C   1 
ATOM   1167 O  O   . ILE A 1 153 ? 46.643  15.023  15.006  1.00 17.48 ? 153  ILE A O   1 
ATOM   1168 C  CB  . ILE A 1 153 ? 47.776  17.912  14.994  1.00 15.83 ? 153  ILE A CB  1 
ATOM   1169 C  CG1 . ILE A 1 153 ? 48.018  19.359  15.475  1.00 16.72 ? 153  ILE A CG1 1 
ATOM   1170 C  CG2 . ILE A 1 153 ? 47.722  17.931  13.440  1.00 17.35 ? 153  ILE A CG2 1 
ATOM   1171 C  CD1 . ILE A 1 153 ? 49.396  19.967  15.109  1.00 18.66 ? 153  ILE A CD1 1 
ATOM   1172 N  N   . CYS A 1 154 ? 44.954  16.217  14.075  1.00 14.83 ? 154  CYS A N   1 
ATOM   1173 C  CA  . CYS A 1 154 ? 44.438  15.158  13.227  1.00 16.32 ? 154  CYS A CA  1 
ATOM   1174 C  C   . CYS A 1 154 ? 44.842  15.587  11.794  1.00 18.24 ? 154  CYS A C   1 
ATOM   1175 O  O   . CYS A 1 154 ? 44.282  16.551  11.240  1.00 16.77 ? 154  CYS A O   1 
ATOM   1176 C  CB  . CYS A 1 154 ? 42.922  15.144  13.335  1.00 18.96 ? 154  CYS A CB  1 
ATOM   1177 S  SG  . CYS A 1 154 ? 42.178  13.814  12.348  1.00 23.13 ? 154  CYS A SG  1 
ATOM   1178 N  N   A PRO A 1 155 ? 45.879  14.941  11.223  0.50 19.21 ? 155  PRO A N   1 
ATOM   1179 N  N   B PRO A 1 155 ? 45.735  14.818  11.141  0.50 17.59 ? 155  PRO A N   1 
ATOM   1180 C  CA  A PRO A 1 155 ? 46.415  15.226  9.887   0.50 20.97 ? 155  PRO A CA  1 
ATOM   1181 C  CA  B PRO A 1 155 ? 46.173  15.119  9.768   0.50 18.88 ? 155  PRO A CA  1 
ATOM   1182 C  C   A PRO A 1 155 ? 45.575  14.708  8.742   0.50 22.82 ? 155  PRO A C   1 
ATOM   1183 C  C   B PRO A 1 155 ? 44.969  14.847  8.848   0.50 20.52 ? 155  PRO A C   1 
ATOM   1184 O  O   A PRO A 1 155 ? 44.709  13.858  8.933   0.50 21.46 ? 155  PRO A O   1 
ATOM   1185 O  O   B PRO A 1 155 ? 44.118  14.020  9.182   0.50 19.34 ? 155  PRO A O   1 
ATOM   1186 C  CB  A PRO A 1 155 ? 47.775  14.526  9.924   0.50 21.53 ? 155  PRO A CB  1 
ATOM   1187 C  CB  B PRO A 1 155 ? 47.301  14.102  9.535   0.50 18.26 ? 155  PRO A CB  1 
ATOM   1188 C  CG  A PRO A 1 155 ? 47.411  13.259  10.632  0.50 20.41 ? 155  PRO A CG  1 
ATOM   1189 C  CG  B PRO A 1 155 ? 47.860  13.916  10.916  0.50 18.24 ? 155  PRO A CG  1 
ATOM   1190 C  CD  A PRO A 1 155 ? 46.618  13.812  11.828  0.50 19.91 ? 155  PRO A CD  1 
ATOM   1191 C  CD  B PRO A 1 155 ? 46.602  13.788  11.750  0.50 18.30 ? 155  PRO A CD  1 
ATOM   1192 N  N   A PRO A 1 156 ? 45.829  15.223  7.526   0.50 24.26 ? 156  PRO A N   1 
ATOM   1193 N  N   B PRO A 1 156 ? 44.903  15.521  7.683   0.50 22.24 ? 156  PRO A N   1 
ATOM   1194 C  CA  A PRO A 1 156 ? 45.060  14.754  6.381   0.50 25.97 ? 156  PRO A CA  1 
ATOM   1195 C  CA  B PRO A 1 156 ? 43.837  15.407  6.674   0.50 24.80 ? 156  PRO A CA  1 
ATOM   1196 C  C   A PRO A 1 156 ? 45.442  13.307  6.099   0.50 26.84 ? 156  PRO A C   1 
ATOM   1197 C  C   B PRO A 1 156 ? 43.434  13.982  6.307   0.50 26.58 ? 156  PRO A C   1 
ATOM   1198 O  O   A PRO A 1 156 ? 44.602  12.519  5.686   0.50 27.36 ? 156  PRO A O   1 
ATOM   1199 O  O   B PRO A 1 156 ? 42.248  13.693  6.126   0.50 27.85 ? 156  PRO A O   1 
ATOM   1200 C  CB  A PRO A 1 156 ? 45.513  15.665  5.242   0.50 25.99 ? 156  PRO A CB  1 
ATOM   1201 C  CB  B PRO A 1 156 ? 44.414  16.112  5.451   0.50 25.05 ? 156  PRO A CB  1 
ATOM   1202 C  CG  A PRO A 1 156 ? 46.037  16.829  5.878   0.50 25.55 ? 156  PRO A CG  1 
ATOM   1203 C  CG  B PRO A 1 156 ? 45.397  17.003  5.950   0.50 24.50 ? 156  PRO A CG  1 
ATOM   1204 C  CD  A PRO A 1 156 ? 46.740  16.303  7.119   0.50 24.74 ? 156  PRO A CD  1 
ATOM   1205 C  CD  B PRO A 1 156 ? 46.009  16.351  7.180   0.50 23.62 ? 156  PRO A CD  1 
ATOM   1206 N  N   A ASN A 1 157 ? 46.715  12.962  6.317   0.50 27.02 ? 157  ASN A N   1 
ATOM   1207 N  N   B ASN A 1 157 ? 44.407  13.095  6.137   0.50 27.60 ? 157  ASN A N   1 
ATOM   1208 C  CA  A ASN A 1 157 ? 47.161  11.604  6.051   0.50 28.12 ? 157  ASN A CA  1 
ATOM   1209 C  CA  B ASN A 1 157 ? 44.063  11.711  5.807   0.50 29.02 ? 157  ASN A CA  1 
ATOM   1210 C  C   A ASN A 1 157 ? 46.766  10.604  7.138   0.50 29.10 ? 157  ASN A C   1 
ATOM   1211 C  C   B ASN A 1 157 ? 44.470  10.726  6.884   0.50 28.91 ? 157  ASN A C   1 
ATOM   1212 O  O   A ASN A 1 157 ? 47.362  9.523   7.230   0.50 29.28 ? 157  ASN A O   1 
ATOM   1213 O  O   B ASN A 1 157 ? 45.037  9.660   6.609   0.50 28.10 ? 157  ASN A O   1 
ATOM   1214 C  CB  A ASN A 1 157 ? 48.696  11.546  5.799   0.50 27.44 ? 157  ASN A CB  1 
ATOM   1215 C  CB  B ASN A 1 157 ? 44.644  11.292  4.456   0.50 30.93 ? 157  ASN A CB  1 
ATOM   1216 C  CG  A ASN A 1 157 ? 49.528  11.998  6.998   0.50 26.63 ? 157  ASN A CG  1 
ATOM   1217 C  CG  B ASN A 1 157 ? 43.565  11.195  3.364   0.50 33.57 ? 157  ASN A CG  1 
ATOM   1218 O  OD1 A ASN A 1 157 ? 49.009  12.112  8.092   0.50 26.81 ? 157  ASN A OD1 1 
ATOM   1219 O  OD1 B ASN A 1 157 ? 42.363  11.079  3.667   0.50 34.10 ? 157  ASN A OD1 1 
ATOM   1220 N  ND2 A ASN A 1 157 ? 50.845  12.252  6.784   0.50 22.99 ? 157  ASN A ND2 1 
ATOM   1221 N  ND2 B ASN A 1 157 ? 43.986  11.221  2.098   0.50 34.41 ? 157  ASN A ND2 1 
ATOM   1222 N  N   A ALA A 1 158 ? 45.744  10.948  7.930   0.50 29.53 ? 158  ALA A N   1 
ATOM   1223 N  N   B ALA A 1 158 ? 44.183  11.107  8.126   0.50 28.07 ? 158  ALA A N   1 
ATOM   1224 C  CA  A ALA A 1 158 ? 45.254  10.087  9.011   0.50 29.72 ? 158  ALA A CA  1 
ATOM   1225 C  CA  B ALA A 1 158 ? 44.482  10.268  9.276   0.50 28.88 ? 158  ALA A CA  1 
ATOM   1226 C  C   A ALA A 1 158 ? 44.511  8.826   8.534   0.50 30.05 ? 158  ALA A C   1 
ATOM   1227 C  C   B ALA A 1 158 ? 43.799  8.924   9.062   0.50 29.13 ? 158  ALA A C   1 
ATOM   1228 O  O   A ALA A 1 158 ? 43.984  8.776   7.423   0.50 30.01 ? 158  ALA A O   1 
ATOM   1229 O  O   B ALA A 1 158 ? 42.658  8.882   8.582   0.50 28.53 ? 158  ALA A O   1 
ATOM   1230 C  CB  A ALA A 1 158 ? 44.335  10.892  9.958   0.50 30.42 ? 158  ALA A CB  1 
ATOM   1231 C  CB  B ALA A 1 158 ? 43.939  10.914  10.535  0.50 27.96 ? 158  ALA A CB  1 
ATOM   1232 N  N   . ASP A 1 159 ? 44.475  7.831   9.418   1.00 29.82 ? 159  ASP A N   1 
ATOM   1233 C  CA  . ASP A 1 159 ? 43.818  6.543   9.239   1.00 30.05 ? 159  ASP A CA  1 
ATOM   1234 C  C   . ASP A 1 159 ? 42.904  6.304   10.445  1.00 30.20 ? 159  ASP A C   1 
ATOM   1235 O  O   . ASP A 1 159 ? 42.853  7.101   11.398  1.00 27.13 ? 159  ASP A O   1 
ATOM   1236 C  CB  . ASP A 1 159 ? 44.835  5.386   8.994   1.00 31.30 ? 159  ASP A CB  1 
ATOM   1237 C  CG  . ASP A 1 159 ? 45.675  5.004   10.214  1.00 33.52 ? 159  ASP A CG  1 
ATOM   1238 O  OD1 . ASP A 1 159 ? 46.633  4.206   10.044  1.00 34.29 ? 159  ASP A OD1 1 
ATOM   1239 O  OD2 . ASP A 1 159 ? 45.414  5.462   11.344  1.00 33.34 ? 159  ASP A OD2 1 
ATOM   1240 N  N   . ASP A 1 160 ? 42.139  5.224   10.410  1.00 29.64 ? 160  ASP A N   1 
ATOM   1241 C  CA  . ASP A 1 160 ? 41.193  4.963   11.455  1.00 28.73 ? 160  ASP A CA  1 
ATOM   1242 C  C   . ASP A 1 160 ? 41.759  4.824   12.861  1.00 27.33 ? 160  ASP A C   1 
ATOM   1243 O  O   . ASP A 1 160 ? 41.160  5.321   13.822  1.00 25.99 ? 160  ASP A O   1 
ATOM   1244 C  CB  . ASP A 1 160 ? 40.362  3.729   11.092  1.00 31.35 ? 160  ASP A CB  1 
ATOM   1245 C  CG  . ASP A 1 160 ? 39.067  3.692   11.845  1.00 32.46 ? 160  ASP A CG  1 
ATOM   1246 O  OD1 . ASP A 1 160 ? 38.213  4.576   11.617  1.00 33.61 ? 160  ASP A OD1 1 
ATOM   1247 O  OD2 . ASP A 1 160 ? 38.903  2.797   12.689  1.00 35.06 ? 160  ASP A OD2 1 
ATOM   1248 N  N   . ASP A 1 161 ? 42.902  4.159   12.988  1.00 26.30 ? 161  ASP A N   1 
ATOM   1249 C  CA  . ASP A 1 161 ? 43.512  3.974   14.286  1.00 26.20 ? 161  ASP A CA  1 
ATOM   1250 C  C   . ASP A 1 161 ? 43.880  5.332   14.881  1.00 23.65 ? 161  ASP A C   1 
ATOM   1251 O  O   . ASP A 1 161 ? 43.655  5.564   16.057  1.00 22.46 ? 161  ASP A O   1 
ATOM   1252 C  CB  . ASP A 1 161 ? 44.776  3.122   14.187  1.00 29.08 ? 161  ASP A CB  1 
ATOM   1253 C  CG  . ASP A 1 161 ? 44.472  1.660   13.877  1.00 33.91 ? 161  ASP A CG  1 
ATOM   1254 O  OD1 . ASP A 1 161 ? 43.353  1.183   14.206  1.00 36.45 ? 161  ASP A OD1 1 
ATOM   1255 O  OD2 . ASP A 1 161 ? 45.378  0.992   13.318  1.00 36.87 ? 161  ASP A OD2 1 
ATOM   1256 N  N   . LEU A 1 162 ? 44.466  6.191   14.059  1.00 20.96 ? 162  LEU A N   1 
ATOM   1257 C  CA  . LEU A 1 162 ? 44.853  7.528   14.523  1.00 19.83 ? 162  LEU A CA  1 
ATOM   1258 C  C   . LEU A 1 162 ? 43.575  8.309   14.904  1.00 18.06 ? 162  LEU A C   1 
ATOM   1259 O  O   . LEU A 1 162 ? 43.537  9.013   15.923  1.00 17.79 ? 162  LEU A O   1 
ATOM   1260 C  CB  . LEU A 1 162 ? 45.634  8.257   13.420  1.00 18.47 ? 162  LEU A CB  1 
ATOM   1261 C  CG  . LEU A 1 162 ? 46.071  9.649   13.907  1.00 17.34 ? 162  LEU A CG  1 
ATOM   1262 C  CD1 . LEU A 1 162 ? 46.852  9.528   15.230  1.00 19.04 ? 162  LEU A CD1 1 
ATOM   1263 C  CD2 . LEU A 1 162 ? 46.902  10.286  12.857  1.00 18.18 ? 162  LEU A CD2 1 
ATOM   1264 N  N   . LEU A 1 163 ? 42.539  8.240   14.082  1.00 18.05 ? 163  LEU A N   1 
ATOM   1265 C  CA  . LEU A 1 163 ? 41.304  8.947   14.437  1.00 17.87 ? 163  LEU A CA  1 
ATOM   1266 C  C   . LEU A 1 163 ? 40.729  8.512   15.787  1.00 18.96 ? 163  LEU A C   1 
ATOM   1267 O  O   . LEU A 1 163 ? 40.274  9.343   16.595  1.00 17.54 ? 163  LEU A O   1 
ATOM   1268 C  CB  . LEU A 1 163 ? 40.247  8.780   13.337  1.00 20.53 ? 163  LEU A CB  1 
ATOM   1269 C  CG  . LEU A 1 163 ? 40.527  9.554   12.060  1.00 21.81 ? 163  LEU A CG  1 
ATOM   1270 C  CD1 . LEU A 1 163 ? 39.777  8.909   10.889  1.00 24.52 ? 163  LEU A CD1 1 
ATOM   1271 C  CD2 . LEU A 1 163 ? 40.087  10.985  12.220  1.00 23.01 ? 163  LEU A CD2 1 
ATOM   1272 N  N   . ARG A 1 164 ? 40.714  7.198   16.056  1.00 18.36 ? 164  ARG A N   1 
ATOM   1273 C  CA  . ARG A 1 164 ? 40.242  6.703   17.340  1.00 18.51 ? 164  ARG A CA  1 
ATOM   1274 C  C   . ARG A 1 164 ? 41.123  7.199   18.502  1.00 16.95 ? 164  ARG A C   1 
ATOM   1275 O  O   . ARG A 1 164 ? 40.607  7.515   19.571  1.00 18.84 ? 164  ARG A O   1 
ATOM   1276 C  CB  . ARG A 1 164 ? 40.224  5.174   17.306  1.00 20.99 ? 164  ARG A CB  1 
ATOM   1277 C  CG  . ARG A 1 164 ? 39.122  4.664   16.414  1.00 26.27 ? 164  ARG A CG  1 
ATOM   1278 C  CD  . ARG A 1 164 ? 39.241  3.148   16.224  1.00 29.83 ? 164  ARG A CD  1 
ATOM   1279 N  NE  . ARG A 1 164 ? 38.190  2.667   15.331  1.00 31.92 ? 164  ARG A NE  1 
ATOM   1280 C  CZ  . ARG A 1 164 ? 36.981  2.280   15.730  1.00 33.42 ? 164  ARG A CZ  1 
ATOM   1281 N  NH1 . ARG A 1 164 ? 36.644  2.305   17.026  1.00 33.52 ? 164  ARG A NH1 1 
ATOM   1282 N  NH2 . ARG A 1 164 ? 36.108  1.859   14.820  1.00 34.32 ? 164  ARG A NH2 1 
ATOM   1283 N  N   . GLN A 1 165 ? 42.446  7.252   18.293  1.00 17.66 ? 165  GLN A N   1 
ATOM   1284 C  CA  . GLN A 1 165 ? 43.342  7.738   19.329  1.00 16.32 ? 165  GLN A CA  1 
ATOM   1285 C  C   . GLN A 1 165 ? 43.133  9.233   19.576  1.00 16.23 ? 165  GLN A C   1 
ATOM   1286 O  O   . GLN A 1 165 ? 43.049  9.647   20.718  1.00 17.48 ? 165  GLN A O   1 
ATOM   1287 C  CB  . GLN A 1 165 ? 44.807  7.508   18.969  1.00 19.59 ? 165  GLN A CB  1 
ATOM   1288 C  CG  . GLN A 1 165 ? 45.261  6.065   19.065  1.00 23.01 ? 165  GLN A CG  1 
ATOM   1289 C  CD  . GLN A 1 165 ? 46.718  5.992   18.676  1.00 25.39 ? 165  GLN A CD  1 
ATOM   1290 O  OE1 . GLN A 1 165 ? 47.075  6.168   17.503  1.00 28.06 ? 165  GLN A OE1 1 
ATOM   1291 N  NE2 . GLN A 1 165 ? 47.568  5.797   19.659  1.00 29.30 ? 165  GLN A NE2 1 
ATOM   1292 N  N   . VAL A 1 166 ? 43.127  10.027  18.520  1.00 15.60 ? 166  VAL A N   1 
ATOM   1293 C  CA  . VAL A 1 166 ? 42.899  11.484  18.685  1.00 15.64 ? 166  VAL A CA  1 
ATOM   1294 C  C   . VAL A 1 166 ? 41.550  11.703  19.398  1.00 16.23 ? 166  VAL A C   1 
ATOM   1295 O  O   . VAL A 1 166 ? 41.441  12.541  20.305  1.00 16.46 ? 166  VAL A O   1 
ATOM   1296 C  CB  . VAL A 1 166 ? 42.931  12.157  17.302  1.00 15.40 ? 166  VAL A CB  1 
ATOM   1297 C  CG1 . VAL A 1 166 ? 42.346  13.594  17.329  1.00 18.34 ? 166  VAL A CG1 1 
ATOM   1298 C  CG2 . VAL A 1 166 ? 44.377  12.186  16.807  1.00 16.64 ? 166  VAL A CG2 1 
ATOM   1299 N  N   . ALA A 1 167 ? 40.523  10.926  19.034  1.00 16.29 ? 167  ALA A N   1 
ATOM   1300 C  CA  . ALA A 1 167 ? 39.248  11.084  19.681  1.00 15.57 ? 167  ALA A CA  1 
ATOM   1301 C  C   . ALA A 1 167 ? 39.296  10.709  21.152  1.00 17.71 ? 167  ALA A C   1 
ATOM   1302 O  O   . ALA A 1 167 ? 38.653  11.363  21.999  1.00 19.03 ? 167  ALA A O   1 
ATOM   1303 C  CB  . ALA A 1 167 ? 38.143  10.238  18.975  1.00 17.32 ? 167  ALA A CB  1 
ATOM   1304 N  N   . SER A 1 168 ? 40.026  9.646   21.475  1.00 16.50 ? 168  SER A N   1 
ATOM   1305 C  CA  . SER A 1 168 ? 40.096  9.210   22.853  1.00 18.56 ? 168  SER A CA  1 
ATOM   1306 C  C   . SER A 1 168 ? 40.974  10.093  23.746  1.00 18.36 ? 168  SER A C   1 
ATOM   1307 O  O   . SER A 1 168 ? 40.586  10.366  24.907  1.00 20.31 ? 168  SER A O   1 
ATOM   1308 C  CB  . SER A 1 168 ? 40.658  7.788   22.904  1.00 19.12 ? 168  SER A CB  1 
ATOM   1309 O  OG  . SER A 1 168 ? 40.770  7.398   24.269  1.00 23.70 ? 168  SER A OG  1 
ATOM   1310 N  N   . TYR A 1 169 ? 42.139  10.485  23.232  1.00 18.94 ? 169  TYR A N   1 
ATOM   1311 C  CA  . TYR A 1 169 ? 43.111  11.249  24.013  1.00 18.58 ? 169  TYR A CA  1 
ATOM   1312 C  C   . TYR A 1 169 ? 42.887  12.754  24.118  1.00 19.38 ? 169  TYR A C   1 
ATOM   1313 O  O   . TYR A 1 169 ? 43.254  13.364  25.123  1.00 19.54 ? 169  TYR A O   1 
ATOM   1314 C  CB  . TYR A 1 169 ? 44.524  11.006  23.476  1.00 20.66 ? 169  TYR A CB  1 
ATOM   1315 C  CG  . TYR A 1 169 ? 44.938  9.553   23.457  1.00 22.90 ? 169  TYR A CG  1 
ATOM   1316 C  CD1 . TYR A 1 169 ? 44.602  8.700   24.506  1.00 24.45 ? 169  TYR A CD1 1 
ATOM   1317 C  CD2 . TYR A 1 169 ? 45.684  9.037   22.401  1.00 24.77 ? 169  TYR A CD2 1 
ATOM   1318 C  CE1 . TYR A 1 169 ? 44.998  7.366   24.504  1.00 27.29 ? 169  TYR A CE1 1 
ATOM   1319 C  CE2 . TYR A 1 169 ? 46.088  7.702   22.390  1.00 27.28 ? 169  TYR A CE2 1 
ATOM   1320 C  CZ  . TYR A 1 169 ? 45.739  6.875   23.445  1.00 27.00 ? 169  TYR A CZ  1 
ATOM   1321 O  OH  . TYR A 1 169 ? 46.129  5.554   23.442  1.00 30.04 ? 169  TYR A OH  1 
ATOM   1322 N  N   . GLY A 1 170 ? 42.295  13.362  23.099  1.00 16.98 ? 170  GLY A N   1 
ATOM   1323 C  CA  . GLY A 1 170 ? 42.143  14.806  23.179  1.00 17.85 ? 170  GLY A CA  1 
ATOM   1324 C  C   . GLY A 1 170 ? 40.960  15.282  23.984  1.00 17.34 ? 170  GLY A C   1 
ATOM   1325 O  O   . GLY A 1 170 ? 40.039  14.531  24.310  1.00 20.43 ? 170  GLY A O   1 
ATOM   1326 N  N   . ARG A 1 171 ? 41.006  16.557  24.359  1.00 15.19 ? 171  ARG A N   1 
ATOM   1327 C  CA  . ARG A 1 171 ? 39.879  17.178  25.045  1.00 14.47 ? 171  ARG A CA  1 
ATOM   1328 C  C   . ARG A 1 171 ? 39.796  18.627  24.596  1.00 13.37 ? 171  ARG A C   1 
ATOM   1329 O  O   . ARG A 1 171 ? 40.754  19.163  24.057  1.00 14.36 ? 171  ARG A O   1 
ATOM   1330 C  CB  . ARG A 1 171 ? 40.036  17.190  26.561  1.00 15.78 ? 171  ARG A CB  1 
ATOM   1331 C  CG  . ARG A 1 171 ? 40.165  15.839  27.248  1.00 21.07 ? 171  ARG A CG  1 
ATOM   1332 C  CD  . ARG A 1 171 ? 38.816  15.129  27.287  1.00 24.20 ? 171  ARG A CD  1 
ATOM   1333 N  NE  . ARG A 1 171 ? 38.933  14.063  28.268  1.00 30.27 ? 171  ARG A NE  1 
ATOM   1334 C  CZ  . ARG A 1 171 ? 39.581  12.936  28.044  1.00 30.86 ? 171  ARG A CZ  1 
ATOM   1335 N  NH1 . ARG A 1 171 ? 40.148  12.721  26.855  1.00 30.96 ? 171  ARG A NH1 1 
ATOM   1336 N  NH2 . ARG A 1 171 ? 39.694  12.047  29.032  1.00 32.71 ? 171  ARG A NH2 1 
ATOM   1337 N  N   . GLY A 1 172 ? 38.664  19.261  24.855  1.00 13.36 ? 172  GLY A N   1 
ATOM   1338 C  CA  . GLY A 1 172 ? 38.541  20.694  24.505  1.00 13.41 ? 172  GLY A CA  1 
ATOM   1339 C  C   . GLY A 1 172 ? 38.148  20.883  23.052  1.00 12.07 ? 172  GLY A C   1 
ATOM   1340 O  O   . GLY A 1 172 ? 36.988  21.209  22.733  1.00 14.14 ? 172  GLY A O   1 
ATOM   1341 N  N   . TYR A 1 173 ? 39.106  20.641  22.159  1.00 11.87 ? 173  TYR A N   1 
ATOM   1342 C  CA  . TYR A 1 173 ? 38.840  20.696  20.727  1.00 11.71 ? 173  TYR A CA  1 
ATOM   1343 C  C   . TYR A 1 173 ? 39.851  19.807  20.019  1.00 11.73 ? 173  TYR A C   1 
ATOM   1344 O  O   . TYR A 1 173 ? 40.896  19.476  20.580  1.00 13.23 ? 173  TYR A O   1 
ATOM   1345 C  CB  . TYR A 1 173 ? 38.930  22.143  20.203  1.00 12.75 ? 173  TYR A CB  1 
ATOM   1346 C  CG  . TYR A 1 173 ? 40.331  22.715  20.087  1.00 11.79 ? 173  TYR A CG  1 
ATOM   1347 C  CD1 . TYR A 1 173 ? 41.054  22.606  18.900  1.00 11.93 ? 173  TYR A CD1 1 
ATOM   1348 C  CD2 . TYR A 1 173 ? 40.926  23.370  21.163  1.00 13.19 ? 173  TYR A CD2 1 
ATOM   1349 C  CE1 . TYR A 1 173 ? 42.340  23.141  18.785  1.00 12.26 ? 173  TYR A CE1 1 
ATOM   1350 C  CE2 . TYR A 1 173 ? 42.212  23.907  21.060  1.00 13.55 ? 173  TYR A CE2 1 
ATOM   1351 C  CZ  . TYR A 1 173 ? 42.909  23.788  19.870  1.00 14.35 ? 173  TYR A CZ  1 
ATOM   1352 O  OH  . TYR A 1 173 ? 44.179  24.315  19.763  1.00 14.67 ? 173  TYR A OH  1 
ATOM   1353 N  N   . THR A 1 174 ? 39.516  19.389  18.801  1.00 11.86 ? 174  THR A N   1 
ATOM   1354 C  CA  . THR A 1 174 ? 40.427  18.539  18.024  1.00 12.71 ? 174  THR A CA  1 
ATOM   1355 C  C   . THR A 1 174 ? 41.004  19.479  16.976  1.00 12.90 ? 174  THR A C   1 
ATOM   1356 O  O   . THR A 1 174 ? 40.258  20.240  16.335  1.00 13.03 ? 174  THR A O   1 
ATOM   1357 C  CB  . THR A 1 174 ? 39.677  17.421  17.313  1.00 11.92 ? 174  THR A CB  1 
ATOM   1358 O  OG1 . THR A 1 174 ? 39.071  16.555  18.281  1.00 13.81 ? 174  THR A OG1 1 
ATOM   1359 C  CG2 . THR A 1 174 ? 40.690  16.576  16.463  1.00 14.30 ? 174  THR A CG2 1 
ATOM   1360 N  N   . TYR A 1 175 ? 42.317  19.521  16.817  1.00 11.72 ? 175  TYR A N   1 
ATOM   1361 C  CA  . TYR A 1 175 ? 42.945  20.377  15.820  1.00 11.10 ? 175  TYR A CA  1 
ATOM   1362 C  C   . TYR A 1 175 ? 42.941  19.648  14.484  1.00 12.95 ? 175  TYR A C   1 
ATOM   1363 O  O   . TYR A 1 175 ? 43.693  18.692  14.288  1.00 13.98 ? 175  TYR A O   1 
ATOM   1364 C  CB  . TYR A 1 175 ? 44.384  20.715  16.227  1.00 11.28 ? 175  TYR A CB  1 
ATOM   1365 C  CG  . TYR A 1 175 ? 44.974  21.879  15.456  1.00 10.75 ? 175  TYR A CG  1 
ATOM   1366 C  CD1 . TYR A 1 175 ? 45.222  21.781  14.087  1.00 12.90 ? 175  TYR A CD1 1 
ATOM   1367 C  CD2 . TYR A 1 175 ? 45.256  23.090  16.090  1.00 11.97 ? 175  TYR A CD2 1 
ATOM   1368 C  CE1 . TYR A 1 175 ? 45.730  22.858  13.365  1.00 13.03 ? 175  TYR A CE1 1 
ATOM   1369 C  CE2 . TYR A 1 175 ? 45.764  24.173  15.378  1.00 10.95 ? 175  TYR A CE2 1 
ATOM   1370 C  CZ  . TYR A 1 175 ? 45.996  24.049  14.015  1.00 11.75 ? 175  TYR A CZ  1 
ATOM   1371 O  OH  . TYR A 1 175 ? 46.473  25.118  13.298  1.00 11.77 ? 175  TYR A OH  1 
ATOM   1372 N  N   . LEU A 1 176 ? 42.084  20.117  13.568  1.00 12.73 ? 176  LEU A N   1 
ATOM   1373 C  CA  . LEU A 1 176 ? 41.970  19.462  12.255  1.00 12.86 ? 176  LEU A CA  1 
ATOM   1374 C  C   . LEU A 1 176 ? 42.878  20.172  11.291  1.00 13.88 ? 176  LEU A C   1 
ATOM   1375 O  O   . LEU A 1 176 ? 42.607  21.298  10.923  1.00 14.10 ? 176  LEU A O   1 
ATOM   1376 C  CB  . LEU A 1 176 ? 40.518  19.566  11.794  1.00 14.80 ? 176  LEU A CB  1 
ATOM   1377 C  CG  . LEU A 1 176 ? 40.292  18.951  10.408  1.00 18.58 ? 176  LEU A CG  1 
ATOM   1378 C  CD1 . LEU A 1 176 ? 40.520  17.415  10.459  1.00 20.73 ? 176  LEU A CD1 1 
ATOM   1379 C  CD2 . LEU A 1 176 ? 38.852  19.273  9.982   1.00 20.78 ? 176  LEU A CD2 1 
ATOM   1380 N  N   . LEU A 1 177 ? 43.960  19.533  10.870  1.00 14.45 ? 177  LEU A N   1 
ATOM   1381 C  CA  . LEU A 1 177 ? 44.901  20.138  9.941   1.00 15.72 ? 177  LEU A CA  1 
ATOM   1382 C  C   . LEU A 1 177 ? 44.331  20.269  8.540   1.00 16.82 ? 177  LEU A C   1 
ATOM   1383 O  O   . LEU A 1 177 ? 43.789  19.302  8.018   1.00 18.52 ? 177  LEU A O   1 
ATOM   1384 C  CB  . LEU A 1 177 ? 46.153  19.245  9.807   1.00 19.30 ? 177  LEU A CB  1 
ATOM   1385 C  CG  . LEU A 1 177 ? 47.396  19.472  10.595  1.00 21.95 ? 177  LEU A CG  1 
ATOM   1386 C  CD1 . LEU A 1 177 ? 48.451  18.501  10.055  1.00 19.74 ? 177  LEU A CD1 1 
ATOM   1387 C  CD2 . LEU A 1 177 ? 47.875  20.933  10.486  1.00 18.60 ? 177  LEU A CD2 1 
ATOM   1388 N  N   . SER A 1 178 ? 44.489  21.416  7.909   1.00 14.67 ? 178  SER A N   1 
ATOM   1389 C  CA  . SER A 1 178 ? 43.977  21.604  6.546   1.00 16.34 ? 178  SER A CA  1 
ATOM   1390 C  C   . SER A 1 178 ? 44.831  20.895  5.496   1.00 16.18 ? 178  SER A C   1 
ATOM   1391 O  O   . SER A 1 178 ? 44.322  20.563  4.415   1.00 18.10 ? 178  SER A O   1 
ATOM   1392 C  CB  . SER A 1 178 ? 43.952  23.101  6.179   1.00 16.40 ? 178  SER A CB  1 
ATOM   1393 O  OG  A SER A 1 178 ? 45.222  23.619  5.945   0.50 19.07 ? 178  SER A OG  1 
ATOM   1394 O  OG  B SER A 1 178 ? 43.270  23.929  7.120   0.50 12.94 ? 178  SER A OG  1 
ATOM   1395 N  N   . ARG A 1 179 ? 46.113  20.679  5.796   1.00 16.09 ? 179  ARG A N   1 
ATOM   1396 C  CA  . ARG A 1 179 ? 47.074  20.143  4.821   1.00 15.36 ? 179  ARG A CA  1 
ATOM   1397 C  C   . ARG A 1 179 ? 48.366  19.809  5.529   1.00 16.37 ? 179  ARG A C   1 
ATOM   1398 O  O   . ARG A 1 179 ? 48.566  20.118  6.715   1.00 16.58 ? 179  ARG A O   1 
ATOM   1399 C  CB  . ARG A 1 179 ? 47.429  21.226  3.792   1.00 16.98 ? 179  ARG A CB  1 
ATOM   1400 C  CG  . ARG A 1 179 ? 47.843  22.566  4.481   1.00 16.76 ? 179  ARG A CG  1 
ATOM   1401 C  CD  . ARG A 1 179 ? 48.519  23.531  3.512   1.00 14.98 ? 179  ARG A CD  1 
ATOM   1402 N  NE  . ARG A 1 179 ? 48.807  24.843  4.122   1.00 17.09 ? 179  ARG A NE  1 
ATOM   1403 C  CZ  . ARG A 1 179 ? 49.828  25.092  4.954   1.00 16.84 ? 179  ARG A CZ  1 
ATOM   1404 N  NH1 . ARG A 1 179 ? 50.675  24.108  5.292   1.00 16.18 ? 179  ARG A NH1 1 
ATOM   1405 N  NH2 . ARG A 1 179 ? 50.035  26.336  5.453   1.00 16.96 ? 179  ARG A NH2 1 
ATOM   1406 N  N   . SER A 1 180 ? 49.258  19.196  4.763   1.00 17.00 ? 180  SER A N   1 
ATOM   1407 C  CA  . SER A 1 180 ? 50.596  18.872  5.246   1.00 16.60 ? 180  SER A CA  1 
ATOM   1408 C  C   . SER A 1 180 ? 51.390  20.170  5.170   1.00 16.59 ? 180  SER A C   1 
ATOM   1409 O  O   . SER A 1 180 ? 50.851  21.244  4.813   1.00 18.09 ? 180  SER A O   1 
ATOM   1410 C  CB  . SER A 1 180 ? 51.226  17.799  4.353   1.00 17.52 ? 180  SER A CB  1 
ATOM   1411 O  OG  . SER A 1 180 ? 51.384  18.249  3.025   1.00 19.90 ? 180  SER A OG  1 
ATOM   1412 N  N   . GLY A 1 181 ? 52.683  20.096  5.506   1.00 15.20 ? 181  GLY A N   1 
ATOM   1413 C  CA  . GLY A 1 181 ? 53.505  21.299  5.485   1.00 14.03 ? 181  GLY A CA  1 
ATOM   1414 C  C   . GLY A 1 181 ? 53.560  22.006  6.830   1.00 15.42 ? 181  GLY A C   1 
ATOM   1415 O  O   . GLY A 1 181 ? 53.314  21.383  7.874   1.00 17.45 ? 181  GLY A O   1 
ATOM   1416 N  N   . VAL A 1 182 ? 53.901  23.299  6.811   1.00 14.83 ? 182  VAL A N   1 
ATOM   1417 C  CA  . VAL A 1 182 ? 54.021  24.128  8.044   1.00 13.93 ? 182  VAL A CA  1 
ATOM   1418 C  C   . VAL A 1 182 ? 53.033  25.295  7.981   1.00 14.13 ? 182  VAL A C   1 
ATOM   1419 O  O   . VAL A 1 182 ? 52.414  25.531  6.935   1.00 15.08 ? 182  VAL A O   1 
ATOM   1420 C  CB  . VAL A 1 182 ? 55.485  24.680  8.234   1.00 12.98 ? 182  VAL A CB  1 
ATOM   1421 C  CG1 . VAL A 1 182 ? 56.449  23.456  8.486   1.00 14.47 ? 182  VAL A CG1 1 
ATOM   1422 C  CG2 . VAL A 1 182 ? 55.921  25.511  7.030   1.00 12.99 ? 182  VAL A CG2 1 
ATOM   1423 N  N   . THR A 1 183 ? 52.889  26.033  9.091   1.00 12.99 ? 183  THR A N   1 
ATOM   1424 C  CA  . THR A 1 183 ? 51.924  27.134  9.107   1.00 14.37 ? 183  THR A CA  1 
ATOM   1425 C  C   . THR A 1 183 ? 52.238  28.166  8.014   1.00 15.26 ? 183  THR A C   1 
ATOM   1426 O  O   . THR A 1 183 ? 53.397  28.336  7.620   1.00 14.22 ? 183  THR A O   1 
ATOM   1427 C  CB  . THR A 1 183 ? 51.919  27.857  10.484  1.00 13.51 ? 183  THR A CB  1 
ATOM   1428 O  OG1 . THR A 1 183 ? 53.215  28.433  10.741  1.00 12.26 ? 183  THR A OG1 1 
ATOM   1429 C  CG2 . THR A 1 183 ? 51.560  26.895  11.598  1.00 13.29 ? 183  THR A CG2 1 
ATOM   1430 N  N   . GLY A 1 184 ? 51.187  28.810  7.501   1.00 14.40 ? 184  GLY A N   1 
ATOM   1431 C  CA  . GLY A 1 184 ? 51.396  29.880  6.506   1.00 16.26 ? 184  GLY A CA  1 
ATOM   1432 C  C   . GLY A 1 184 ? 50.139  30.258  5.763   1.00 18.96 ? 184  GLY A C   1 
ATOM   1433 O  O   . GLY A 1 184 ? 49.460  29.369  5.282   1.00 17.89 ? 184  GLY A O   1 
ATOM   1434 N  N   . ALA A 1 185 ? 49.831  31.549  5.673   1.00 19.54 ? 185  ALA A N   1 
ATOM   1435 C  CA  . ALA A 1 185 ? 48.649  32.028  4.981   1.00 23.31 ? 185  ALA A CA  1 
ATOM   1436 C  C   . ALA A 1 185 ? 48.796  31.879  3.465   1.00 26.10 ? 185  ALA A C   1 
ATOM   1437 O  O   . ALA A 1 185 ? 47.803  31.793  2.749   1.00 28.70 ? 185  ALA A O   1 
ATOM   1438 C  CB  . ALA A 1 185 ? 48.398  33.521  5.344   1.00 24.46 ? 185  ALA A CB  1 
ATOM   1439 N  N   . GLU A 1 186 ? 50.028  31.824  2.979   1.00 27.85 ? 186  GLU A N   1 
ATOM   1440 C  CA  . GLU A 1 186 ? 50.231  31.728  1.531   1.00 31.70 ? 186  GLU A CA  1 
ATOM   1441 C  C   . GLU A 1 186 ? 50.059  30.320  0.967   1.00 31.98 ? 186  GLU A C   1 
ATOM   1442 O  O   . GLU A 1 186 ? 50.369  30.075  -0.211  1.00 32.77 ? 186  GLU A O   1 
ATOM   1443 C  CB  . GLU A 1 186 ? 51.617  32.264  1.154   1.00 34.40 ? 186  GLU A CB  1 
ATOM   1444 C  CG  . GLU A 1 186 ? 52.463  32.693  2.338   1.00 39.21 ? 186  GLU A CG  1 
ATOM   1445 C  CD  . GLU A 1 186 ? 52.859  31.510  3.203   1.00 41.02 ? 186  GLU A CD  1 
ATOM   1446 O  OE1 . GLU A 1 186 ? 53.497  31.719  4.253   1.00 42.15 ? 186  GLU A OE1 1 
ATOM   1447 O  OE2 . GLU A 1 186 ? 52.525  30.359  2.824   1.00 43.52 ? 186  GLU A OE2 1 
ATOM   1448 N  N   . ASN A 1 187 ? 49.565  29.391  1.786   1.00 30.36 ? 187  ASN A N   1 
ATOM   1449 C  CA  . ASN A 1 187 ? 49.349  28.034  1.309   1.00 29.34 ? 187  ASN A CA  1 
ATOM   1450 C  C   . ASN A 1 187 ? 47.986  27.512  1.796   1.00 28.44 ? 187  ASN A C   1 
ATOM   1451 O  O   . ASN A 1 187 ? 47.835  27.137  2.959   1.00 24.06 ? 187  ASN A O   1 
ATOM   1452 C  CB  . ASN A 1 187 ? 50.483  27.135  1.808   1.00 31.75 ? 187  ASN A CB  1 
ATOM   1453 C  CG  . ASN A 1 187 ? 50.548  25.841  1.057   1.00 34.94 ? 187  ASN A CG  1 
ATOM   1454 O  OD1 . ASN A 1 187 ? 49.536  25.153  0.894   1.00 36.02 ? 187  ASN A OD1 1 
ATOM   1455 N  ND2 . ASN A 1 187 ? 51.745  25.500  0.554   1.00 38.19 ? 187  ASN A ND2 1 
ATOM   1456 N  N   . ARG A 1 188 ? 46.982  27.496  0.923   1.00 28.27 ? 188  ARG A N   1 
ATOM   1457 C  CA  . ARG A 1 188 ? 45.662  27.043  1.336   1.00 30.59 ? 188  ARG A CA  1 
ATOM   1458 C  C   . ARG A 1 188 ? 45.453  25.545  1.217   1.00 31.30 ? 188  ARG A C   1 
ATOM   1459 O  O   . ARG A 1 188 ? 45.915  24.909  0.268   1.00 32.28 ? 188  ARG A O   1 
ATOM   1460 C  CB  . ARG A 1 188 ? 44.577  27.762  0.529   1.00 31.35 ? 188  ARG A CB  1 
ATOM   1461 C  CG  . ARG A 1 188 ? 44.598  29.272  0.725   1.00 34.12 ? 188  ARG A CG  1 
ATOM   1462 C  CD  . ARG A 1 188 ? 43.377  29.931  0.110   1.00 34.87 ? 188  ARG A CD  1 
ATOM   1463 N  NE  A ARG A 1 188 ? 43.369  31.359  0.401   0.60 35.66 ? 188  ARG A NE  1 
ATOM   1464 N  NE  B ARG A 1 188 ? 42.278  28.978  -0.077  0.40 35.24 ? 188  ARG A NE  1 
ATOM   1465 C  CZ  A ARG A 1 188 ? 42.313  32.148  0.246   0.60 36.44 ? 188  ARG A CZ  1 
ATOM   1466 C  CZ  B ARG A 1 188 ? 41.039  29.317  -0.430  0.40 35.77 ? 188  ARG A CZ  1 
ATOM   1467 N  NH1 A ARG A 1 188 ? 41.167  31.641  -0.199  0.60 37.92 ? 188  ARG A NH1 1 
ATOM   1468 N  NH1 B ARG A 1 188 ? 40.109  28.385  -0.579  0.40 36.07 ? 188  ARG A NH1 1 
ATOM   1469 N  NH2 A ARG A 1 188 ? 42.398  33.435  0.546   0.60 36.23 ? 188  ARG A NH2 1 
ATOM   1470 N  NH2 B ARG A 1 188 ? 40.726  30.592  -0.622  0.40 35.99 ? 188  ARG A NH2 1 
ATOM   1471 N  N   . GLY A 1 189 ? 44.780  24.970  2.197   1.00 32.14 ? 189  GLY A N   1 
ATOM   1472 C  CA  . GLY A 1 189 ? 44.508  23.550  2.137   1.00 33.50 ? 189  GLY A CA  1 
ATOM   1473 C  C   . GLY A 1 189 ? 43.298  23.401  1.236   1.00 36.08 ? 189  GLY A C   1 
ATOM   1474 O  O   . GLY A 1 189 ? 42.361  24.198  1.321   1.00 35.97 ? 189  GLY A O   1 
ATOM   1475 N  N   . ALA A 1 190 ? 43.312  22.402  0.368   1.00 37.38 ? 190  ALA A N   1 
ATOM   1476 C  CA  . ALA A 1 190 ? 42.183  22.198  -0.535  1.00 39.33 ? 190  ALA A CA  1 
ATOM   1477 C  C   . ALA A 1 190 ? 41.611  20.776  -0.470  1.00 39.68 ? 190  ALA A C   1 
ATOM   1478 O  O   . ALA A 1 190 ? 40.741  20.412  -1.280  1.00 41.63 ? 190  ALA A O   1 
ATOM   1479 C  CB  . ALA A 1 190 ? 42.597  22.533  -1.971  1.00 39.41 ? 190  ALA A CB  1 
ATOM   1480 N  N   . LEU A 1 191 ? 42.094  19.964  0.465   1.00 39.30 ? 191  LEU A N   1 
ATOM   1481 C  CA  . LEU A 1 191 ? 41.562  18.613  0.582   1.00 38.80 ? 191  LEU A CA  1 
ATOM   1482 C  C   . LEU A 1 191 ? 40.215  18.650  1.323   1.00 38.43 ? 191  LEU A C   1 
ATOM   1483 O  O   . LEU A 1 191 ? 40.071  19.314  2.356   1.00 37.68 ? 191  LEU A O   1 
ATOM   1484 C  CB  . LEU A 1 191 ? 42.550  17.704  1.322   1.00 38.71 ? 191  LEU A CB  1 
ATOM   1485 N  N   . PRO A 1 192 ? 39.189  17.977  0.769   1.00 37.82 ? 192  PRO A N   1 
ATOM   1486 C  CA  . PRO A 1 192 ? 37.869  17.950  1.422   1.00 37.04 ? 192  PRO A CA  1 
ATOM   1487 C  C   . PRO A 1 192 ? 38.062  17.233  2.762   1.00 35.47 ? 192  PRO A C   1 
ATOM   1488 O  O   . PRO A 1 192 ? 38.604  16.127  2.802   1.00 35.63 ? 192  PRO A O   1 
ATOM   1489 C  CB  . PRO A 1 192 ? 37.008  17.123  0.452   1.00 38.39 ? 192  PRO A CB  1 
ATOM   1490 C  CG  . PRO A 1 192 ? 37.721  17.305  -0.904  1.00 39.31 ? 192  PRO A CG  1 
ATOM   1491 C  CD  . PRO A 1 192 ? 39.182  17.247  -0.518  1.00 38.51 ? 192  PRO A CD  1 
ATOM   1492 N  N   . LEU A 1 193 ? 37.616  17.835  3.854   1.00 33.63 ? 193  LEU A N   1 
ATOM   1493 C  CA  . LEU A 1 193 ? 37.832  17.204  5.151   1.00 32.15 ? 193  LEU A CA  1 
ATOM   1494 C  C   . LEU A 1 193 ? 36.550  16.647  5.738   1.00 32.60 ? 193  LEU A C   1 
ATOM   1495 O  O   . LEU A 1 193 ? 36.470  16.326  6.925   1.00 31.45 ? 193  LEU A O   1 
ATOM   1496 C  CB  . LEU A 1 193 ? 38.448  18.237  6.093   1.00 30.98 ? 193  LEU A CB  1 
ATOM   1497 C  CG  . LEU A 1 193 ? 39.739  18.907  5.584   1.00 30.93 ? 193  LEU A CG  1 
ATOM   1498 C  CD1 . LEU A 1 193 ? 40.250  19.912  6.635   1.00 30.12 ? 193  LEU A CD1 1 
ATOM   1499 C  CD2 . LEU A 1 193 ? 40.815  17.839  5.286   1.00 30.63 ? 193  LEU A CD2 1 
ATOM   1500 N  N   . HIS A 1 194 ? 35.563  16.469  4.869   1.00 37.85 ? 194  HIS A N   1 
ATOM   1501 C  CA  . HIS A 1 194 ? 34.234  16.022  5.267   1.00 39.14 ? 194  HIS A CA  1 
ATOM   1502 C  C   . HIS A 1 194 ? 34.270  14.660  5.955   1.00 38.92 ? 194  HIS A C   1 
ATOM   1503 O  O   . HIS A 1 194 ? 33.634  14.463  6.992   1.00 38.79 ? 194  HIS A O   1 
ATOM   1504 C  CB  . HIS A 1 194 ? 33.319  15.944  4.041   1.00 41.18 ? 194  HIS A CB  1 
ATOM   1505 C  CG  . HIS A 1 194 ? 33.251  17.216  3.253   1.00 43.02 ? 194  HIS A CG  1 
ATOM   1506 N  ND1 . HIS A 1 194 ? 32.540  17.324  2.077   1.00 44.54 ? 194  HIS A ND1 1 
ATOM   1507 C  CD2 . HIS A 1 194 ? 33.807  18.432  3.468   1.00 44.15 ? 194  HIS A CD2 1 
ATOM   1508 C  CE1 . HIS A 1 194 ? 32.661  18.551  1.602   1.00 44.50 ? 194  HIS A CE1 1 
ATOM   1509 N  NE2 . HIS A 1 194 ? 33.425  19.244  2.428   1.00 44.21 ? 194  HIS A NE2 1 
ATOM   1510 N  N   . HIS A 1 195 ? 35.016  13.726  5.373   1.00 38.73 ? 195  HIS A N   1 
ATOM   1511 C  CA  . HIS A 1 195 ? 35.130  12.375  5.915   1.00 38.26 ? 195  HIS A CA  1 
ATOM   1512 C  C   . HIS A 1 195 ? 35.711  12.351  7.327   1.00 37.09 ? 195  HIS A C   1 
ATOM   1513 O  O   . HIS A 1 195 ? 35.147  11.724  8.225   1.00 37.19 ? 195  HIS A O   1 
ATOM   1514 C  CB  . HIS A 1 195 ? 35.992  11.509  4.990   1.00 39.93 ? 195  HIS A CB  1 
ATOM   1515 C  CG  . HIS A 1 195 ? 36.129  10.089  5.447   1.00 40.65 ? 195  HIS A CG  1 
ATOM   1516 N  ND1 . HIS A 1 195 ? 35.046  9.251   5.608   1.00 41.23 ? 195  HIS A ND1 1 
ATOM   1517 C  CD2 . HIS A 1 195 ? 37.221  9.361   5.780   1.00 41.41 ? 195  HIS A CD2 1 
ATOM   1518 C  CE1 . HIS A 1 195 ? 35.466  8.068   6.022   1.00 41.61 ? 195  HIS A CE1 1 
ATOM   1519 N  NE2 . HIS A 1 195 ? 36.781  8.108   6.134   1.00 41.76 ? 195  HIS A NE2 1 
ATOM   1520 N  N   . LEU A 1 196 ? 36.856  13.008  7.522   1.00 31.35 ? 196  LEU A N   1 
ATOM   1521 C  CA  . LEU A 1 196 ? 37.494  13.003  8.842   1.00 29.61 ? 196  LEU A CA  1 
ATOM   1522 C  C   . LEU A 1 196 ? 36.545  13.589  9.850   1.00 28.16 ? 196  LEU A C   1 
ATOM   1523 O  O   . LEU A 1 196 ? 36.333  13.025  10.934  1.00 26.41 ? 196  LEU A O   1 
ATOM   1524 C  CB  . LEU A 1 196 ? 38.758  13.844  8.887   1.00 32.19 ? 196  LEU A CB  1 
ATOM   1525 C  CG  . LEU A 1 196 ? 40.000  13.490  8.097   1.00 34.61 ? 196  LEU A CG  1 
ATOM   1526 C  CD1 . LEU A 1 196 ? 41.031  14.550  8.391   1.00 35.98 ? 196  LEU A CD1 1 
ATOM   1527 C  CD2 . LEU A 1 196 ? 40.507  12.089  8.491   1.00 35.58 ? 196  LEU A CD2 1 
ATOM   1528 N  N   . ILE A 1 197 ? 35.978  14.742  9.492   1.00 26.74 ? 197  ILE A N   1 
ATOM   1529 C  CA  . ILE A 1 197 ? 35.053  15.398  10.400  1.00 25.94 ? 197  ILE A CA  1 
ATOM   1530 C  C   . ILE A 1 197 ? 33.935  14.455  10.835  1.00 26.09 ? 197  ILE A C   1 
ATOM   1531 O  O   . ILE A 1 197 ? 33.550  14.426  12.008  1.00 27.29 ? 197  ILE A O   1 
ATOM   1532 C  CB  . ILE A 1 197 ? 34.489  16.703  9.769   1.00 24.14 ? 197  ILE A CB  1 
ATOM   1533 C  CG1 . ILE A 1 197 ? 35.591  17.764  9.712   1.00 24.00 ? 197  ILE A CG1 1 
ATOM   1534 C  CG2 . ILE A 1 197 ? 33.336  17.265  10.637  1.00 23.50 ? 197  ILE A CG2 1 
ATOM   1535 C  CD1 . ILE A 1 197 ? 35.236  18.957  8.763   1.00 22.42 ? 197  ILE A CD1 1 
ATOM   1536 N  N   . GLU A 1 198 ? 33.412  13.670  9.905   1.00 27.09 ? 198  GLU A N   1 
ATOM   1537 C  CA  . GLU A 1 198 ? 32.349  12.742  10.253  1.00 26.75 ? 198  GLU A CA  1 
ATOM   1538 C  C   . GLU A 1 198 ? 32.815  11.570  11.151  1.00 26.20 ? 198  GLU A C   1 
ATOM   1539 O  O   . GLU A 1 198 ? 32.113  11.200  12.102  1.00 24.95 ? 198  GLU A O   1 
ATOM   1540 C  CB  . GLU A 1 198 ? 31.674  12.235  8.967   1.00 28.56 ? 198  GLU A CB  1 
ATOM   1541 N  N   . LYS A 1 199 ? 34.001  11.026  10.869  1.00 26.65 ? 199  LYS A N   1 
ATOM   1542 C  CA  . LYS A 1 199 ? 34.555  9.940   11.681  1.00 25.61 ? 199  LYS A CA  1 
ATOM   1543 C  C   . LYS A 1 199 ? 34.879  10.472  13.102  1.00 23.69 ? 199  LYS A C   1 
ATOM   1544 O  O   . LYS A 1 199 ? 34.642  9.798   14.092  1.00 23.44 ? 199  LYS A O   1 
ATOM   1545 C  CB  . LYS A 1 199 ? 35.838  9.380   11.047  1.00 28.48 ? 199  LYS A CB  1 
ATOM   1546 C  CG  . LYS A 1 199 ? 35.679  8.636   9.714   1.00 31.75 ? 199  LYS A CG  1 
ATOM   1547 C  CD  . LYS A 1 199 ? 34.670  7.481   9.793   1.00 34.84 ? 199  LYS A CD  1 
ATOM   1548 C  CE  . LYS A 1 199 ? 35.064  6.444   10.821  1.00 35.51 ? 199  LYS A CE  1 
ATOM   1549 N  NZ  . LYS A 1 199 ? 34.300  5.162   10.557  1.00 37.00 ? 199  LYS A NZ  1 
ATOM   1550 N  N   . LEU A 1 200 ? 35.384  11.709  13.201  1.00 22.74 ? 200  LEU A N   1 
ATOM   1551 C  CA  . LEU A 1 200 ? 35.670  12.268  14.538  1.00 21.21 ? 200  LEU A CA  1 
ATOM   1552 C  C   . LEU A 1 200 ? 34.387  12.361  15.372  1.00 20.50 ? 200  LEU A C   1 
ATOM   1553 O  O   . LEU A 1 200 ? 34.361  12.075  16.583  1.00 19.38 ? 200  LEU A O   1 
ATOM   1554 C  CB  . LEU A 1 200 ? 36.306  13.674  14.397  1.00 20.36 ? 200  LEU A CB  1 
ATOM   1555 C  CG  . LEU A 1 200 ? 37.770  13.667  13.922  1.00 19.27 ? 200  LEU A CG  1 
ATOM   1556 C  CD1 . LEU A 1 200 ? 38.198  15.095  13.532  1.00 19.64 ? 200  LEU A CD1 1 
ATOM   1557 C  CD2 . LEU A 1 200 ? 38.680  13.067  15.014  1.00 19.64 ? 200  LEU A CD2 1 
ATOM   1558 N  N   . LYS A 1 201 ? 33.297  12.793  14.727  1.00 20.77 ? 201  LYS A N   1 
ATOM   1559 C  CA  . LYS A 1 201 ? 32.012  12.885  15.427  1.00 22.03 ? 201  LYS A CA  1 
ATOM   1560 C  C   . LYS A 1 201 ? 31.530  11.484  15.835  1.00 22.38 ? 201  LYS A C   1 
ATOM   1561 O  O   . LYS A 1 201 ? 31.062  11.280  16.964  1.00 22.18 ? 201  LYS A O   1 
ATOM   1562 C  CB  . LYS A 1 201 ? 30.979  13.570  14.541  1.00 23.36 ? 201  LYS A CB  1 
ATOM   1563 C  CG  . LYS A 1 201 ? 31.138  15.089  14.540  1.00 26.12 ? 201  LYS A CG  1 
ATOM   1564 C  CD  . LYS A 1 201 ? 30.158  15.757  13.571  1.00 27.04 ? 201  LYS A CD  1 
ATOM   1565 C  CE  . LYS A 1 201 ? 30.393  17.285  13.496  1.00 28.29 ? 201  LYS A CE  1 
ATOM   1566 N  NZ  . LYS A 1 201 ? 29.445  17.936  12.529  1.00 27.40 ? 201  LYS A NZ  1 
ATOM   1567 N  N   . GLU A 1 202 ? 31.715  10.526  14.936  1.00 24.62 ? 202  GLU A N   1 
ATOM   1568 C  CA  . GLU A 1 202 ? 31.343  9.149   15.237  1.00 26.60 ? 202  GLU A CA  1 
ATOM   1569 C  C   . GLU A 1 202 ? 32.043  8.605   16.497  1.00 27.97 ? 202  GLU A C   1 
ATOM   1570 O  O   . GLU A 1 202 ? 31.461  7.828   17.281  1.00 27.51 ? 202  GLU A O   1 
ATOM   1571 C  CB  . GLU A 1 202 ? 31.689  8.245   14.043  1.00 27.76 ? 202  GLU A CB  1 
ATOM   1572 C  CG  . GLU A 1 202 ? 31.296  6.783   14.318  1.00 31.92 ? 202  GLU A CG  1 
ATOM   1573 C  CD  . GLU A 1 202 ? 31.697  5.834   13.209  1.00 33.22 ? 202  GLU A CD  1 
ATOM   1574 O  OE1 . GLU A 1 202 ? 31.777  6.283   12.043  1.00 33.97 ? 202  GLU A OE1 1 
ATOM   1575 O  OE2 . GLU A 1 202 ? 31.915  4.636   13.526  1.00 35.71 ? 202  GLU A OE2 1 
ATOM   1576 N  N   . TYR A 1 203 ? 33.295  9.014   16.705  1.00 24.75 ? 203  TYR A N   1 
ATOM   1577 C  CA  . TYR A 1 203 ? 34.076  8.550   17.845  1.00 24.01 ? 203  TYR A CA  1 
ATOM   1578 C  C   . TYR A 1 203 ? 34.016  9.501   19.037  1.00 23.22 ? 203  TYR A C   1 
ATOM   1579 O  O   . TYR A 1 203 ? 34.825  9.403   19.960  1.00 23.07 ? 203  TYR A O   1 
ATOM   1580 C  CB  . TYR A 1 203 ? 35.533  8.328   17.428  1.00 25.16 ? 203  TYR A CB  1 
ATOM   1581 C  CG  . TYR A 1 203 ? 35.697  7.301   16.329  1.00 26.53 ? 203  TYR A CG  1 
ATOM   1582 C  CD1 . TYR A 1 203 ? 35.027  6.079   16.387  1.00 27.39 ? 203  TYR A CD1 1 
ATOM   1583 C  CD2 . TYR A 1 203 ? 36.527  7.545   15.236  1.00 27.31 ? 203  TYR A CD2 1 
ATOM   1584 C  CE1 . TYR A 1 203 ? 35.178  5.127   15.384  1.00 28.63 ? 203  TYR A CE1 1 
ATOM   1585 C  CE2 . TYR A 1 203 ? 36.686  6.597   14.225  1.00 28.30 ? 203  TYR A CE2 1 
ATOM   1586 C  CZ  . TYR A 1 203 ? 36.008  5.391   14.307  1.00 28.71 ? 203  TYR A CZ  1 
ATOM   1587 O  OH  . TYR A 1 203 ? 36.157  4.448   13.315  1.00 29.22 ? 203  TYR A OH  1 
ATOM   1588 N  N   . HIS A 1 204 ? 33.047  10.412  19.008  1.00 22.37 ? 204  HIS A N   1 
ATOM   1589 C  CA  . HIS A 1 204 ? 32.846  11.385  20.077  1.00 22.15 ? 204  HIS A CA  1 
ATOM   1590 C  C   . HIS A 1 204 ? 34.094  12.200  20.405  1.00 20.31 ? 204  HIS A C   1 
ATOM   1591 O  O   . HIS A 1 204 ? 34.416  12.411  21.573  1.00 19.08 ? 204  HIS A O   1 
ATOM   1592 C  CB  . HIS A 1 204 ? 32.355  10.685  21.347  1.00 25.53 ? 204  HIS A CB  1 
ATOM   1593 C  CG  . HIS A 1 204 ? 31.051  9.968   21.178  1.00 29.53 ? 204  HIS A CG  1 
ATOM   1594 N  ND1 . HIS A 1 204 ? 30.896  8.893   20.330  1.00 31.92 ? 204  HIS A ND1 1 
ATOM   1595 C  CD2 . HIS A 1 204 ? 29.841  10.173  21.751  1.00 31.67 ? 204  HIS A CD2 1 
ATOM   1596 C  CE1 . HIS A 1 204 ? 29.648  8.465   20.387  1.00 32.50 ? 204  HIS A CE1 1 
ATOM   1597 N  NE2 . HIS A 1 204 ? 28.986  9.224   21.242  1.00 33.06 ? 204  HIS A NE2 1 
ATOM   1598 N  N   . ALA A 1 205 ? 34.805  12.634  19.378  1.00 16.07 ? 205  ALA A N   1 
ATOM   1599 C  CA  . ALA A 1 205 ? 36.010  13.472  19.587  1.00 15.29 ? 205  ALA A CA  1 
ATOM   1600 C  C   . ALA A 1 205 ? 35.570  14.875  20.020  1.00 16.29 ? 205  ALA A C   1 
ATOM   1601 O  O   . ALA A 1 205 ? 34.430  15.324  19.764  1.00 16.87 ? 205  ALA A O   1 
ATOM   1602 C  CB  . ALA A 1 205 ? 36.789  13.620  18.312  1.00 13.86 ? 205  ALA A CB  1 
ATOM   1603 N  N   . ALA A 1 206 ? 36.519  15.589  20.613  1.00 15.56 ? 206  ALA A N   1 
ATOM   1604 C  CA  . ALA A 1 206 ? 36.252  16.975  20.972  1.00 15.53 ? 206  ALA A CA  1 
ATOM   1605 C  C   . ALA A 1 206 ? 35.979  17.699  19.647  1.00 15.09 ? 206  ALA A C   1 
ATOM   1606 O  O   . ALA A 1 206 ? 36.502  17.345  18.595  1.00 15.63 ? 206  ALA A O   1 
ATOM   1607 C  CB  . ALA A 1 206 ? 37.478  17.571  21.682  1.00 13.96 ? 206  ALA A CB  1 
ATOM   1608 N  N   . PRO A 1 207 ? 35.121  18.757  19.685  1.00 14.19 ? 207  PRO A N   1 
ATOM   1609 C  CA  . PRO A 1 207 ? 34.777  19.497  18.457  1.00 13.93 ? 207  PRO A CA  1 
ATOM   1610 C  C   . PRO A 1 207 ? 35.969  19.932  17.640  1.00 12.98 ? 207  PRO A C   1 
ATOM   1611 O  O   . PRO A 1 207 ? 36.954  20.425  18.200  1.00 14.00 ? 207  PRO A O   1 
ATOM   1612 C  CB  . PRO A 1 207 ? 33.926  20.686  18.978  1.00 13.64 ? 207  PRO A CB  1 
ATOM   1613 C  CG  . PRO A 1 207 ? 33.278  20.054  20.221  1.00 14.82 ? 207  PRO A CG  1 
ATOM   1614 C  CD  . PRO A 1 207 ? 34.453  19.293  20.873  1.00 15.15 ? 207  PRO A CD  1 
ATOM   1615 N  N   . ALA A 1 208 ? 35.886  19.774  16.313  1.00 13.08 ? 208  ALA A N   1 
ATOM   1616 C  CA  . ALA A 1 208 ? 37.015  20.100  15.432  1.00 12.89 ? 208  ALA A CA  1 
ATOM   1617 C  C   . ALA A 1 208 ? 37.140  21.552  15.062  1.00 14.40 ? 208  ALA A C   1 
ATOM   1618 O  O   . ALA A 1 208 ? 36.149  22.220  14.687  1.00 15.57 ? 208  ALA A O   1 
ATOM   1619 C  CB  . ALA A 1 208 ? 36.953  19.262  14.102  1.00 14.08 ? 208  ALA A CB  1 
ATOM   1620 N  N   . LEU A 1 209 ? 38.365  22.060  15.170  1.00 12.59 ? 209  LEU A N   1 
ATOM   1621 C  CA  . LEU A 1 209 ? 38.693  23.440  14.712  1.00 13.07 ? 209  LEU A CA  1 
ATOM   1622 C  C   . LEU A 1 209 ? 39.701  23.242  13.601  1.00 12.96 ? 209  LEU A C   1 
ATOM   1623 O  O   . LEU A 1 209 ? 40.733  22.580  13.803  1.00 12.80 ? 209  LEU A O   1 
ATOM   1624 C  CB  . LEU A 1 209 ? 39.331  24.315  15.792  1.00 13.74 ? 209  LEU A CB  1 
ATOM   1625 C  CG  . LEU A 1 209 ? 38.392  24.675  16.929  1.00 13.91 ? 209  LEU A CG  1 
ATOM   1626 C  CD1 . LEU A 1 209 ? 39.197  25.520  17.885  1.00 16.28 ? 209  LEU A CD1 1 
ATOM   1627 C  CD2 . LEU A 1 209 ? 37.127  25.431  16.449  1.00 16.10 ? 209  LEU A CD2 1 
ATOM   1628 N  N   . GLN A 1 210 ? 39.398  23.745  12.410  1.00 11.54 ? 210  GLN A N   1 
ATOM   1629 C  CA  . GLN A 1 210 ? 40.336  23.624  11.268  1.00 13.96 ? 210  GLN A CA  1 
ATOM   1630 C  C   . GLN A 1 210 ? 41.397  24.688  11.298  1.00 12.96 ? 210  GLN A C   1 
ATOM   1631 O  O   . GLN A 1 210 ? 41.111  25.876  11.511  1.00 13.84 ? 210  GLN A O   1 
ATOM   1632 C  CB  . GLN A 1 210 ? 39.613  23.717  9.924   1.00 14.69 ? 210  GLN A CB  1 
ATOM   1633 C  CG  . GLN A 1 210 ? 40.495  23.334  8.751   1.00 17.45 ? 210  GLN A CG  1 
ATOM   1634 C  CD  . GLN A 1 210 ? 39.726  23.430  7.466   1.00 19.61 ? 210  GLN A CD  1 
ATOM   1635 O  OE1 . GLN A 1 210 ? 38.507  23.160  7.440   1.00 22.02 ? 210  GLN A OE1 1 
ATOM   1636 N  NE2 . GLN A 1 210 ? 40.412  23.790  6.399   1.00 19.15 ? 210  GLN A NE2 1 
ATOM   1637 N  N   . GLY A 1 211 ? 42.637  24.263  11.086  1.00 12.67 ? 211  GLY A N   1 
ATOM   1638 C  CA  . GLY A 1 211 ? 43.761  25.202  11.079  1.00 12.63 ? 211  GLY A CA  1 
ATOM   1639 C  C   . GLY A 1 211 ? 44.823  24.888  10.051  1.00 14.47 ? 211  GLY A C   1 
ATOM   1640 O  O   . GLY A 1 211 ? 44.995  23.696  9.671   1.00 15.47 ? 211  GLY A O   1 
ATOM   1641 N  N   . PHE A 1 212 ? 45.568  25.952  9.692   1.00 14.22 ? 212  PHE A N   1 
ATOM   1642 C  CA  . PHE A 1 212 ? 46.618  25.973  8.669   1.00 15.17 ? 212  PHE A CA  1 
ATOM   1643 C  C   . PHE A 1 212 ? 46.079  26.540  7.359   1.00 14.89 ? 212  PHE A C   1 
ATOM   1644 O  O   . PHE A 1 212 ? 45.173  25.970  6.747   1.00 15.57 ? 212  PHE A O   1 
ATOM   1645 C  CB  . PHE A 1 212 ? 47.207  24.576  8.410   1.00 15.62 ? 212  PHE A CB  1 
ATOM   1646 C  CG  . PHE A 1 212 ? 48.357  24.213  9.315   1.00 13.54 ? 212  PHE A CG  1 
ATOM   1647 C  CD1 . PHE A 1 212 ? 48.255  24.369  10.692  1.00 14.64 ? 212  PHE A CD1 1 
ATOM   1648 C  CD2 . PHE A 1 212 ? 49.532  23.676  8.787   1.00 14.74 ? 212  PHE A CD2 1 
ATOM   1649 C  CE1 . PHE A 1 212 ? 49.301  23.994  11.535  1.00 14.02 ? 212  PHE A CE1 1 
ATOM   1650 C  CE2 . PHE A 1 212 ? 50.586  23.297  9.621   1.00 14.00 ? 212  PHE A CE2 1 
ATOM   1651 C  CZ  . PHE A 1 212 ? 50.468  23.457  11.001  1.00 13.16 ? 212  PHE A CZ  1 
ATOM   1652 N  N   . GLY A 1 213 ? 46.635  27.684  6.964   1.00 13.11 ? 213  GLY A N   1 
ATOM   1653 C  CA  . GLY A 1 213 ? 46.263  28.316  5.679   1.00 14.97 ? 213  GLY A CA  1 
ATOM   1654 C  C   . GLY A 1 213 ? 44.930  29.055  5.666   1.00 16.83 ? 213  GLY A C   1 
ATOM   1655 O  O   . GLY A 1 213 ? 44.523  29.510  4.583   1.00 18.00 ? 213  GLY A O   1 
ATOM   1656 N  N   . ILE A 1 214 ? 44.238  29.166  6.802   1.00 16.55 ? 214  ILE A N   1 
ATOM   1657 C  CA  . ILE A 1 214 ? 42.923  29.875  6.819   1.00 16.13 ? 214  ILE A CA  1 
ATOM   1658 C  C   . ILE A 1 214 ? 43.192  31.389  6.896   1.00 16.87 ? 214  ILE A C   1 
ATOM   1659 O  O   . ILE A 1 214 ? 43.664  31.906  7.949   1.00 16.37 ? 214  ILE A O   1 
ATOM   1660 C  CB  . ILE A 1 214 ? 42.074  29.481  8.064   1.00 17.63 ? 214  ILE A CB  1 
ATOM   1661 C  CG1 . ILE A 1 214 ? 41.870  27.959  8.123   1.00 19.36 ? 214  ILE A CG1 1 
ATOM   1662 C  CG2 . ILE A 1 214 ? 40.705  30.233  8.031   1.00 17.82 ? 214  ILE A CG2 1 
ATOM   1663 C  CD1 . ILE A 1 214 ? 41.030  27.425  7.004   1.00 21.70 ? 214  ILE A CD1 1 
ATOM   1664 N  N   . SER A 1 215 ? 42.866  32.116  5.814   1.00 15.39 ? 215  SER A N   1 
ATOM   1665 C  CA  . SER A 1 215 ? 43.155  33.549  5.760   1.00 17.02 ? 215  SER A CA  1 
ATOM   1666 C  C   . SER A 1 215 ? 42.031  34.431  5.206   1.00 18.05 ? 215  SER A C   1 
ATOM   1667 O  O   . SER A 1 215 ? 42.207  35.660  5.065   1.00 18.31 ? 215  SER A O   1 
ATOM   1668 C  CB  . SER A 1 215 ? 44.386  33.781  4.879   1.00 19.26 ? 215  SER A CB  1 
ATOM   1669 O  OG  . SER A 1 215 ? 44.077  33.449  3.512   1.00 23.22 ? 215  SER A OG  1 
ATOM   1670 N  N   . SER A 1 216 ? 40.871  33.853  4.961   1.00 17.34 ? 216  SER A N   1 
ATOM   1671 C  CA  . SER A 1 216 ? 39.770  34.600  4.379   1.00 17.74 ? 216  SER A CA  1 
ATOM   1672 C  C   . SER A 1 216 ? 38.452  34.149  4.921   1.00 17.60 ? 216  SER A C   1 
ATOM   1673 O  O   . SER A 1 216 ? 38.274  33.013  5.357   1.00 16.54 ? 216  SER A O   1 
ATOM   1674 C  CB  . SER A 1 216 ? 39.774  34.381  2.864   1.00 17.80 ? 216  SER A CB  1 
ATOM   1675 O  OG  . SER A 1 216 ? 39.463  33.025  2.588   1.00 19.26 ? 216  SER A OG  1 
ATOM   1676 N  N   . PRO A 1 217 ? 37.476  35.043  4.911   1.00 16.11 ? 217  PRO A N   1 
ATOM   1677 C  CA  . PRO A 1 217 ? 36.162  34.706  5.418   1.00 17.29 ? 217  PRO A CA  1 
ATOM   1678 C  C   . PRO A 1 217 ? 35.524  33.487  4.773   1.00 16.45 ? 217  PRO A C   1 
ATOM   1679 O  O   . PRO A 1 217 ? 34.908  32.654  5.475   1.00 18.06 ? 217  PRO A O   1 
ATOM   1680 C  CB  . PRO A 1 217 ? 35.362  35.999  5.182   1.00 17.97 ? 217  PRO A CB  1 
ATOM   1681 C  CG  . PRO A 1 217 ? 36.418  37.034  5.374   1.00 19.56 ? 217  PRO A CG  1 
ATOM   1682 C  CD  . PRO A 1 217 ? 37.620  36.488  4.644   1.00 17.70 ? 217  PRO A CD  1 
ATOM   1683 N  N   . GLU A 1 218 ? 35.695  33.322  3.475   1.00 16.65 ? 218  GLU A N   1 
ATOM   1684 C  CA  . GLU A 1 218 ? 35.014  32.193  2.829   1.00 17.71 ? 218  GLU A CA  1 
ATOM   1685 C  C   . GLU A 1 218 ? 35.570  30.866  3.328   1.00 16.74 ? 218  GLU A C   1 
ATOM   1686 O  O   . GLU A 1 218 ? 34.871  29.853  3.279   1.00 16.11 ? 218  GLU A O   1 
ATOM   1687 C  CB  . GLU A 1 218 ? 35.122  32.297  1.292   1.00 19.95 ? 218  GLU A CB  1 
ATOM   1688 C  CG  . GLU A 1 218 ? 36.471  31.947  0.741   1.00 26.32 ? 218  GLU A CG  1 
ATOM   1689 C  CD  . GLU A 1 218 ? 36.633  32.346  -0.708  1.00 32.09 ? 218  GLU A CD  1 
ATOM   1690 O  OE1 . GLU A 1 218 ? 35.624  32.264  -1.473  1.00 32.63 ? 218  GLU A OE1 1 
ATOM   1691 O  OE2 . GLU A 1 218 ? 37.782  32.733  -1.066  1.00 35.82 ? 218  GLU A OE2 1 
ATOM   1692 N  N   . GLN A 1 219 ? 36.820  30.867  3.796   1.00 15.76 ? 219  GLN A N   1 
ATOM   1693 C  CA  . GLN A 1 219 ? 37.358  29.608  4.334   1.00 14.44 ? 219  GLN A CA  1 
ATOM   1694 C  C   . GLN A 1 219 ? 36.749  29.285  5.687   1.00 16.18 ? 219  GLN A C   1 
ATOM   1695 O  O   . GLN A 1 219 ? 36.627  28.076  6.017   1.00 15.66 ? 219  GLN A O   1 
ATOM   1696 C  CB  . GLN A 1 219 ? 38.881  29.686  4.476   1.00 14.12 ? 219  GLN A CB  1 
ATOM   1697 C  CG  . GLN A 1 219 ? 39.615  29.712  3.154   1.00 16.07 ? 219  GLN A CG  1 
ATOM   1698 C  CD  . GLN A 1 219 ? 41.089  30.008  3.346   1.00 15.28 ? 219  GLN A CD  1 
ATOM   1699 O  OE1 . GLN A 1 219 ? 41.468  31.150  3.566   1.00 16.73 ? 219  GLN A OE1 1 
ATOM   1700 N  NE2 . GLN A 1 219 ? 41.937  28.969  3.280   1.00 18.06 ? 219  GLN A NE2 1 
ATOM   1701 N  N   . VAL A 1 220 ? 36.413  30.299  6.474   1.00 15.71 ? 220  VAL A N   1 
ATOM   1702 C  CA  . VAL A 1 220 ? 35.776  30.082  7.752   1.00 14.32 ? 220  VAL A CA  1 
ATOM   1703 C  C   . VAL A 1 220 ? 34.373  29.481  7.495   1.00 16.30 ? 220  VAL A C   1 
ATOM   1704 O  O   . VAL A 1 220 ? 33.992  28.461  8.104   1.00 15.31 ? 220  VAL A O   1 
ATOM   1705 C  CB  . VAL A 1 220 ? 35.662  31.396  8.569   1.00 13.60 ? 220  VAL A CB  1 
ATOM   1706 C  CG1 . VAL A 1 220 ? 34.850  31.164  9.872   1.00 14.64 ? 220  VAL A CG1 1 
ATOM   1707 C  CG2 . VAL A 1 220 ? 37.083  31.937  8.878   1.00 14.18 ? 220  VAL A CG2 1 
ATOM   1708 N  N   . SER A 1 221 ? 33.592  30.096  6.589   1.00 15.10 ? 221  SER A N   1 
ATOM   1709 C  CA  . SER A 1 221 ? 32.263  29.555  6.298   1.00 15.22 ? 221  SER A CA  1 
ATOM   1710 C  C   . SER A 1 221 ? 32.349  28.131  5.702   1.00 14.98 ? 221  SER A C   1 
ATOM   1711 O  O   . SER A 1 221 ? 31.542  27.281  6.014   1.00 16.05 ? 221  SER A O   1 
ATOM   1712 C  CB  . SER A 1 221 ? 31.479  30.492  5.324   1.00 15.58 ? 221  SER A CB  1 
ATOM   1713 O  OG  A SER A 1 221 ? 32.158  30.706  4.107   0.60 16.35 ? 221  SER A OG  1 
ATOM   1714 O  OG  B SER A 1 221 ? 31.477  31.829  5.788   0.20 13.60 ? 221  SER A OG  1 
ATOM   1715 N  N   . ALA A 1 222 ? 33.314  27.879  4.844   1.00 15.75 ? 222  ALA A N   1 
ATOM   1716 C  CA  . ALA A 1 222 ? 33.483  26.546  4.262   1.00 15.82 ? 222  ALA A CA  1 
ATOM   1717 C  C   . ALA A 1 222 ? 33.814  25.495  5.339   1.00 15.75 ? 222  ALA A C   1 
ATOM   1718 O  O   . ALA A 1 222 ? 33.320  24.365  5.285   1.00 16.10 ? 222  ALA A O   1 
ATOM   1719 C  CB  . ALA A 1 222 ? 34.629  26.590  3.228   1.00 16.19 ? 222  ALA A CB  1 
ATOM   1720 N  N   . ALA A 1 223 ? 34.622  25.866  6.331   1.00 16.26 ? 223  ALA A N   1 
ATOM   1721 C  CA  . ALA A 1 223 ? 34.993  24.883  7.369   1.00 16.56 ? 223  ALA A CA  1 
ATOM   1722 C  C   . ALA A 1 223 ? 33.777  24.480  8.155   1.00 18.85 ? 223  ALA A C   1 
ATOM   1723 O  O   . ALA A 1 223 ? 33.602  23.292  8.417   1.00 18.10 ? 223  ALA A O   1 
ATOM   1724 C  CB  . ALA A 1 223 ? 36.057  25.461  8.323   1.00 16.32 ? 223  ALA A CB  1 
ATOM   1725 N  N   . VAL A 1 224 ? 32.945  25.453  8.552   1.00 18.59 ? 224  VAL A N   1 
ATOM   1726 C  CA  . VAL A 1 224 ? 31.737  25.203  9.335   1.00 19.82 ? 224  VAL A CA  1 
ATOM   1727 C  C   . VAL A 1 224 ? 30.732  24.407  8.484   1.00 19.18 ? 224  VAL A C   1 
ATOM   1728 O  O   . VAL A 1 224 ? 30.062  23.511  8.978   1.00 20.28 ? 224  VAL A O   1 
ATOM   1729 C  CB  . VAL A 1 224 ? 31.132  26.556  9.823   1.00 20.47 ? 224  VAL A CB  1 
ATOM   1730 C  CG1 . VAL A 1 224 ? 29.811  26.349  10.580  1.00 20.77 ? 224  VAL A CG1 1 
ATOM   1731 C  CG2 . VAL A 1 224 ? 32.154  27.279  10.703  1.00 22.02 ? 224  VAL A CG2 1 
ATOM   1732 N  N   . ARG A 1 225 ? 30.641  24.720  7.193   1.00 19.46 ? 225  ARG A N   1 
ATOM   1733 C  CA  . ARG A 1 225 ? 29.706  24.001  6.314   1.00 20.58 ? 225  ARG A CA  1 
ATOM   1734 C  C   . ARG A 1 225 ? 30.127  22.534  6.166   1.00 20.86 ? 225  ARG A C   1 
ATOM   1735 O  O   . ARG A 1 225 ? 29.278  21.635  6.003   1.00 21.63 ? 225  ARG A O   1 
ATOM   1736 C  CB  . ARG A 1 225 ? 29.669  24.701  4.955   1.00 21.27 ? 225  ARG A CB  1 
ATOM   1737 C  CG  . ARG A 1 225 ? 28.678  24.142  4.009   1.00 23.66 ? 225  ARG A CG  1 
ATOM   1738 C  CD  . ARG A 1 225 ? 28.316  25.253  3.009   1.00 25.13 ? 225  ARG A CD  1 
ATOM   1739 N  NE  . ARG A 1 225 ? 29.482  25.718  2.252   1.00 24.74 ? 225  ARG A NE  1 
ATOM   1740 C  CZ  . ARG A 1 225 ? 30.068  26.913  2.377   1.00 21.86 ? 225  ARG A CZ  1 
ATOM   1741 N  NH1 . ARG A 1 225 ? 29.632  27.843  3.238   1.00 23.44 ? 225  ARG A NH1 1 
ATOM   1742 N  NH2 . ARG A 1 225 ? 31.120  27.157  1.619   1.00 23.80 ? 225  ARG A NH2 1 
ATOM   1743 N  N   . ALA A 1 226 ? 31.424  22.276  6.216   1.00 20.03 ? 226  ALA A N   1 
ATOM   1744 C  CA  . ALA A 1 226 ? 31.922  20.893  6.135   1.00 19.48 ? 226  ALA A CA  1 
ATOM   1745 C  C   . ALA A 1 226 ? 31.714  20.113  7.441   1.00 19.93 ? 226  ALA A C   1 
ATOM   1746 O  O   . ALA A 1 226 ? 31.947  18.882  7.485   1.00 22.24 ? 226  ALA A O   1 
ATOM   1747 C  CB  . ALA A 1 226 ? 33.389  20.907  5.760   1.00 19.04 ? 226  ALA A CB  1 
ATOM   1748 N  N   . GLY A 1 227 ? 31.251  20.790  8.481   1.00 19.28 ? 227  GLY A N   1 
ATOM   1749 C  CA  . GLY A 1 227 ? 30.993  20.124  9.739   1.00 20.08 ? 227  GLY A CA  1 
ATOM   1750 C  C   . GLY A 1 227 ? 31.955  20.433  10.875  1.00 20.22 ? 227  GLY A C   1 
ATOM   1751 O  O   . GLY A 1 227 ? 31.773  19.920  11.981  1.00 21.30 ? 227  GLY A O   1 
ATOM   1752 N  N   . ALA A 1 228 ? 32.944  21.288  10.628  1.00 19.13 ? 228  ALA A N   1 
ATOM   1753 C  CA  . ALA A 1 228 ? 33.840  21.628  11.735  1.00 18.23 ? 228  ALA A CA  1 
ATOM   1754 C  C   . ALA A 1 228 ? 33.150  22.630  12.658  1.00 17.89 ? 228  ALA A C   1 
ATOM   1755 O  O   . ALA A 1 228 ? 32.218  23.361  12.256  1.00 18.54 ? 228  ALA A O   1 
ATOM   1756 C  CB  . ALA A 1 228 ? 35.175  22.216  11.206  1.00 18.40 ? 228  ALA A CB  1 
ATOM   1757 N  N   . ALA A 1 229 ? 33.572  22.661  13.909  1.00 16.38 ? 229  ALA A N   1 
ATOM   1758 C  CA  . ALA A 1 229 ? 33.014  23.569  14.875  1.00 15.82 ? 229  ALA A CA  1 
ATOM   1759 C  C   . ALA A 1 229 ? 33.574  24.977  14.740  1.00 16.13 ? 229  ALA A C   1 
ATOM   1760 O  O   . ALA A 1 229 ? 33.085  25.882  15.397  1.00 17.06 ? 229  ALA A O   1 
ATOM   1761 C  CB  . ALA A 1 229 ? 33.250  23.056  16.255  1.00 16.25 ? 229  ALA A CB  1 
ATOM   1762 N  N   . GLY A 1 230 ? 34.575  25.158  13.900  1.00 15.19 ? 230  GLY A N   1 
ATOM   1763 C  CA  . GLY A 1 230 ? 35.158  26.497  13.789  1.00 14.45 ? 230  GLY A CA  1 
ATOM   1764 C  C   . GLY A 1 230 ? 36.470  26.462  13.039  1.00 13.96 ? 230  GLY A C   1 
ATOM   1765 O  O   . GLY A 1 230 ? 36.884  25.426  12.505  1.00 13.29 ? 230  GLY A O   1 
ATOM   1766 N  N   . ALA A 1 231 ? 37.159  27.599  13.033  1.00 13.13 ? 231  ALA A N   1 
ATOM   1767 C  CA  . ALA A 1 231 ? 38.387  27.705  12.264  1.00 13.91 ? 231  ALA A CA  1 
ATOM   1768 C  C   . ALA A 1 231 ? 39.366  28.612  12.978  1.00 13.58 ? 231  ALA A C   1 
ATOM   1769 O  O   . ALA A 1 231 ? 38.985  29.522  13.712  1.00 14.59 ? 231  ALA A O   1 
ATOM   1770 C  CB  . ALA A 1 231 ? 38.099  28.243  10.833  1.00 15.02 ? 231  ALA A CB  1 
ATOM   1771 N  N   . ILE A 1 232 ? 40.655  28.279  12.816  1.00 12.74 ? 232  ILE A N   1 
ATOM   1772 C  CA  . ILE A 1 232 ? 41.769  29.004  13.425  1.00 13.05 ? 232  ILE A CA  1 
ATOM   1773 C  C   . ILE A 1 232 ? 42.562  29.720  12.353  1.00 12.53 ? 232  ILE A C   1 
ATOM   1774 O  O   . ILE A 1 232 ? 42.793  29.187  11.286  1.00 13.48 ? 232  ILE A O   1 
ATOM   1775 C  CB  . ILE A 1 232 ? 42.734  27.996  14.120  1.00 12.66 ? 232  ILE A CB  1 
ATOM   1776 C  CG1 . ILE A 1 232 ? 42.040  27.298  15.269  1.00 13.80 ? 232  ILE A CG1 1 
ATOM   1777 C  CG2 . ILE A 1 232 ? 43.962  28.748  14.668  1.00 12.76 ? 232  ILE A CG2 1 
ATOM   1778 C  CD1 . ILE A 1 232 ? 42.717  25.902  15.615  1.00 15.04 ? 232  ILE A CD1 1 
ATOM   1779 N  N   . SER A 1 233 ? 42.978  30.965  12.633  1.00 12.00 ? 233  SER A N   1 
ATOM   1780 C  CA  . SER A 1 233 ? 43.813  31.720  11.686  1.00 12.73 ? 233  SER A CA  1 
ATOM   1781 C  C   . SER A 1 233 ? 44.960  32.325  12.451  1.00 13.01 ? 233  SER A C   1 
ATOM   1782 O  O   . SER A 1 233 ? 44.734  33.050  13.451  1.00 12.44 ? 233  SER A O   1 
ATOM   1783 C  CB  . SER A 1 233 ? 42.998  32.867  11.022  1.00 12.26 ? 233  SER A CB  1 
ATOM   1784 O  OG  . SER A 1 233 ? 43.817  33.650  10.146  1.00 15.21 ? 233  SER A OG  1 
ATOM   1785 N  N   . GLY A 1 234 ? 46.195  31.982  12.025  1.00 13.78 ? 234  GLY A N   1 
ATOM   1786 C  CA  . GLY A 1 234 ? 47.370  32.533  12.718  1.00 12.88 ? 234  GLY A CA  1 
ATOM   1787 C  C   . GLY A 1 234 ? 48.203  33.428  11.840  1.00 12.60 ? 234  GLY A C   1 
ATOM   1788 O  O   . GLY A 1 234 ? 48.279  34.648  12.104  1.00 13.57 ? 234  GLY A O   1 
ATOM   1789 N  N   . SER A 1 235 ? 48.836  32.842  10.828  1.00 11.99 ? 235  SER A N   1 
ATOM   1790 C  CA  . SER A 1 235 ? 49.718  33.606  9.934   1.00 13.46 ? 235  SER A CA  1 
ATOM   1791 C  C   . SER A 1 235 ? 49.023  34.848  9.361   1.00 13.34 ? 235  SER A C   1 
ATOM   1792 O  O   . SER A 1 235 ? 49.670  35.891  9.301   1.00 12.92 ? 235  SER A O   1 
ATOM   1793 C  CB  . SER A 1 235 ? 50.233  32.709  8.806   1.00 13.83 ? 235  SER A CB  1 
ATOM   1794 O  OG  . SER A 1 235 ? 51.126  31.730  9.319   1.00 15.57 ? 235  SER A OG  1 
ATOM   1795 N  N   . ALA A 1 236 ? 47.748  34.771  8.998   1.00 13.66 ? 236  ALA A N   1 
ATOM   1796 C  CA  . ALA A 1 236 ? 47.063  35.974  8.433   1.00 14.61 ? 236  ALA A CA  1 
ATOM   1797 C  C   . ALA A 1 236 ? 46.981  37.092  9.457   1.00 16.99 ? 236  ALA A C   1 
ATOM   1798 O  O   . ALA A 1 236 ? 47.107  38.280  9.115   1.00 17.13 ? 236  ALA A O   1 
ATOM   1799 C  CB  . ALA A 1 236 ? 45.661  35.600  7.936   1.00 13.63 ? 236  ALA A CB  1 
ATOM   1800 N  N   . ILE A 1 237 ? 46.777  36.733  10.725  1.00 15.28 ? 237  ILE A N   1 
ATOM   1801 C  CA  . ILE A 1 237 ? 46.719  37.699  11.798  1.00 14.56 ? 237  ILE A CA  1 
ATOM   1802 C  C   . ILE A 1 237 ? 48.107  38.288  12.036  1.00 14.92 ? 237  ILE A C   1 
ATOM   1803 O  O   . ILE A 1 237 ? 48.291  39.504  12.198  1.00 16.28 ? 237  ILE A O   1 
ATOM   1804 C  CB  . ILE A 1 237 ? 46.252  37.022  13.133  1.00 15.90 ? 237  ILE A CB  1 
ATOM   1805 C  CG1 . ILE A 1 237 ? 44.833  36.436  12.977  1.00 18.10 ? 237  ILE A CG1 1 
ATOM   1806 C  CG2 . ILE A 1 237 ? 46.369  37.967  14.259  1.00 16.94 ? 237  ILE A CG2 1 
ATOM   1807 C  CD1 . ILE A 1 237 ? 43.693  37.394  13.182  1.00 20.88 ? 237  ILE A CD1 1 
ATOM   1808 N  N   . VAL A 1 238 ? 49.104  37.414  12.092  1.00 13.58 ? 238  VAL A N   1 
ATOM   1809 C  CA  . VAL A 1 238 ? 50.472  37.851  12.381  1.00 13.44 ? 238  VAL A CA  1 
ATOM   1810 C  C   . VAL A 1 238 ? 51.017  38.733  11.255  1.00 14.38 ? 238  VAL A C   1 
ATOM   1811 O  O   . VAL A 1 238 ? 51.833  39.629  11.544  1.00 14.40 ? 238  VAL A O   1 
ATOM   1812 C  CB  . VAL A 1 238 ? 51.394  36.570  12.600  1.00 13.51 ? 238  VAL A CB  1 
ATOM   1813 C  CG1 . VAL A 1 238 ? 52.896  36.955  12.812  1.00 14.90 ? 238  VAL A CG1 1 
ATOM   1814 C  CG2 . VAL A 1 238 ? 50.931  35.857  13.912  1.00 14.39 ? 238  VAL A CG2 1 
ATOM   1815 N  N   . LYS A 1 239 ? 50.602  38.486  10.020  1.00 15.40 ? 239  LYS A N   1 
ATOM   1816 C  CA  . LYS A 1 239 ? 51.079  39.323  8.911   1.00 16.38 ? 239  LYS A CA  1 
ATOM   1817 C  C   . LYS A 1 239 ? 50.622  40.770  9.140   1.00 17.81 ? 239  LYS A C   1 
ATOM   1818 O  O   . LYS A 1 239 ? 51.355  41.695  8.731   1.00 18.07 ? 239  LYS A O   1 
ATOM   1819 C  CB  . LYS A 1 239 ? 50.535  38.820  7.566   1.00 19.74 ? 239  LYS A CB  1 
ATOM   1820 C  CG  . LYS A 1 239 ? 51.242  37.574  6.966   1.00 23.55 ? 239  LYS A CG  1 
ATOM   1821 C  CD  . LYS A 1 239 ? 50.801  37.245  5.504   1.00 29.31 ? 239  LYS A CD  1 
ATOM   1822 C  CE  . LYS A 1 239 ? 51.558  35.988  4.963   1.00 30.79 ? 239  LYS A CE  1 
ATOM   1823 N  NZ  . LYS A 1 239 ? 51.427  35.516  3.506   1.00 32.93 ? 239  LYS A NZ  1 
ATOM   1824 N  N   . ILE A 1 240 ? 49.438  40.975  9.746   1.00 16.29 ? 240  ILE A N   1 
ATOM   1825 C  CA  . ILE A 1 240 ? 48.921  42.338  10.028  1.00 16.02 ? 240  ILE A CA  1 
ATOM   1826 C  C   . ILE A 1 240 ? 49.822  43.010  11.033  1.00 17.73 ? 240  ILE A C   1 
ATOM   1827 O  O   . ILE A 1 240 ? 50.069  44.214  10.928  1.00 17.94 ? 240  ILE A O   1 
ATOM   1828 C  CB  . ILE A 1 240 ? 47.436  42.309  10.485  1.00 16.42 ? 240  ILE A CB  1 
ATOM   1829 C  CG1 . ILE A 1 240 ? 46.572  41.817  9.312   1.00 16.00 ? 240  ILE A CG1 1 
ATOM   1830 C  CG2 . ILE A 1 240 ? 46.993  43.673  10.962  1.00 17.62 ? 240  ILE A CG2 1 
ATOM   1831 C  CD1 . ILE A 1 240 ? 45.151  41.450  9.708   1.00 18.69 ? 240  ILE A CD1 1 
ATOM   1832 N  N   . ILE A 1 241 ? 50.329  42.262  12.016  1.00 16.11 ? 241  ILE A N   1 
ATOM   1833 C  CA  . ILE A 1 241 ? 51.268  42.813  12.988  1.00 16.20 ? 241  ILE A CA  1 
ATOM   1834 C  C   . ILE A 1 241 ? 52.559  43.181  12.261  1.00 17.67 ? 241  ILE A C   1 
ATOM   1835 O  O   . ILE A 1 241 ? 53.063  44.317  12.348  1.00 17.34 ? 241  ILE A O   1 
ATOM   1836 C  CB  . ILE A 1 241 ? 51.558  41.748  14.122  1.00 14.96 ? 241  ILE A CB  1 
ATOM   1837 C  CG1 . ILE A 1 241 ? 50.267  41.540  14.920  1.00 15.10 ? 241  ILE A CG1 1 
ATOM   1838 C  CG2 . ILE A 1 241 ? 52.658  42.260  15.076  1.00 15.27 ? 241  ILE A CG2 1 
ATOM   1839 C  CD1 . ILE A 1 241 ? 50.362  40.336  15.954  1.00 15.73 ? 241  ILE A CD1 1 
ATOM   1840 N  N   . GLU A 1 242 ? 53.095  42.250  11.493  1.00 17.19 ? 242  GLU A N   1 
ATOM   1841 C  CA  . GLU A 1 242 ? 54.341  42.487  10.787  1.00 19.07 ? 242  GLU A CA  1 
ATOM   1842 C  C   . GLU A 1 242 ? 54.259  43.711  9.849   1.00 19.98 ? 242  GLU A C   1 
ATOM   1843 O  O   . GLU A 1 242 ? 55.198  44.540  9.811   1.00 22.34 ? 242  GLU A O   1 
ATOM   1844 C  CB  . GLU A 1 242 ? 54.685  41.246  9.963   1.00 19.38 ? 242  GLU A CB  1 
ATOM   1845 C  CG  . GLU A 1 242 ? 55.987  41.321  9.226   1.00 24.03 ? 242  GLU A CG  1 
ATOM   1846 C  CD  . GLU A 1 242 ? 56.143  40.151  8.268   1.00 28.50 ? 242  GLU A CD  1 
ATOM   1847 O  OE1 . GLU A 1 242 ? 55.440  39.125  8.444   1.00 30.29 ? 242  GLU A OE1 1 
ATOM   1848 O  OE2 . GLU A 1 242 ? 56.961  40.258  7.331   1.00 32.62 ? 242  GLU A OE2 1 
ATOM   1849 N  N   . LYS A 1 243 ? 53.145  43.848  9.159   1.00 19.07 ? 243  LYS A N   1 
ATOM   1850 C  CA  . LYS A 1 243 ? 53.020  44.934  8.181   1.00 20.83 ? 243  LYS A CA  1 
ATOM   1851 C  C   . LYS A 1 243 ? 52.864  46.293  8.838   1.00 21.50 ? 243  LYS A C   1 
ATOM   1852 O  O   . LYS A 1 243 ? 53.210  47.332  8.231   1.00 22.83 ? 243  LYS A O   1 
ATOM   1853 C  CB  . LYS A 1 243 ? 51.823  44.655  7.260   1.00 21.38 ? 243  LYS A CB  1 
ATOM   1854 N  N   . ASN A 1 244 ? 52.399  46.319  10.073  1.00 18.79 ? 244  ASN A N   1 
ATOM   1855 C  CA  . ASN A 1 244 ? 52.130  47.589  10.730  1.00 18.36 ? 244  ASN A CA  1 
ATOM   1856 C  C   . ASN A 1 244 ? 52.974  47.894  11.951  1.00 18.18 ? 244  ASN A C   1 
ATOM   1857 O  O   . ASN A 1 244 ? 52.553  48.653  12.825  1.00 18.53 ? 244  ASN A O   1 
ATOM   1858 C  CB  . ASN A 1 244 ? 50.648  47.635  11.121  1.00 18.73 ? 244  ASN A CB  1 
ATOM   1859 C  CG  . ASN A 1 244 ? 49.711  47.677  9.925   1.00 22.99 ? 244  ASN A CG  1 
ATOM   1860 O  OD1 . ASN A 1 244 ? 49.490  48.747  9.359   1.00 24.95 ? 244  ASN A OD1 1 
ATOM   1861 N  ND2 . ASN A 1 244 ? 49.146  46.540  9.529   1.00 22.87 ? 244  ASN A ND2 1 
ATOM   1862 N  N   . LEU A 1 245 ? 54.174  47.330  12.014  1.00 18.25 ? 245  LEU A N   1 
ATOM   1863 C  CA  . LEU A 1 245 ? 55.001  47.544  13.188  1.00 19.72 ? 245  LEU A CA  1 
ATOM   1864 C  C   . LEU A 1 245 ? 55.239  49.010  13.519  1.00 21.50 ? 245  LEU A C   1 
ATOM   1865 O  O   . LEU A 1 245 ? 55.258  49.411  14.696  1.00 22.49 ? 245  LEU A O   1 
ATOM   1866 C  CB  . LEU A 1 245 ? 56.358  46.855  13.018  1.00 21.48 ? 245  LEU A CB  1 
ATOM   1867 C  CG  . LEU A 1 245 ? 56.345  45.306  12.953  1.00 22.37 ? 245  LEU A CG  1 
ATOM   1868 C  CD1 . LEU A 1 245 ? 57.725  44.811  12.531  1.00 22.59 ? 245  LEU A CD1 1 
ATOM   1869 C  CD2 . LEU A 1 245 ? 55.932  44.716  14.308  1.00 22.19 ? 245  LEU A CD2 1 
ATOM   1870 N  N   . ALA A 1 246 ? 55.402  49.809  12.473  1.00 22.62 ? 246  ALA A N   1 
ATOM   1871 C  CA  . ALA A 1 246 ? 55.698  51.223  12.705  1.00 23.75 ? 246  ALA A CA  1 
ATOM   1872 C  C   . ALA A 1 246 ? 54.476  52.045  13.035  1.00 24.96 ? 246  ALA A C   1 
ATOM   1873 O  O   . ALA A 1 246 ? 54.593  53.237  13.353  1.00 25.30 ? 246  ALA A O   1 
ATOM   1874 C  CB  . ALA A 1 246 ? 56.393  51.793  11.481  1.00 23.90 ? 246  ALA A CB  1 
ATOM   1875 N  N   . SER A 1 247 ? 53.302  51.432  12.975  1.00 24.00 ? 247  SER A N   1 
ATOM   1876 C  CA  . SER A 1 247 ? 52.067  52.156  13.252  1.00 25.72 ? 247  SER A CA  1 
ATOM   1877 C  C   . SER A 1 247 ? 51.142  51.318  14.129  1.00 25.15 ? 247  SER A C   1 
ATOM   1878 O  O   . SER A 1 247 ? 50.182  50.716  13.622  1.00 23.47 ? 247  SER A O   1 
ATOM   1879 C  CB  . SER A 1 247 ? 51.371  52.464  11.933  1.00 28.53 ? 247  SER A CB  1 
ATOM   1880 O  OG  . SER A 1 247 ? 52.318  52.878  10.952  1.00 33.88 ? 247  SER A OG  1 
ATOM   1881 N  N   . PRO A 1 248 ? 51.401  51.307  15.438  1.00 24.89 ? 248  PRO A N   1 
ATOM   1882 C  CA  . PRO A 1 248 ? 50.623  50.541  16.427  1.00 26.27 ? 248  PRO A CA  1 
ATOM   1883 C  C   . PRO A 1 248 ? 49.121  50.770  16.341  1.00 27.07 ? 248  PRO A C   1 
ATOM   1884 O  O   . PRO A 1 248 ? 48.348  49.817  16.478  1.00 26.90 ? 248  PRO A O   1 
ATOM   1885 C  CB  . PRO A 1 248 ? 51.186  50.994  17.772  1.00 26.68 ? 248  PRO A CB  1 
ATOM   1886 C  CG  . PRO A 1 248 ? 52.533  51.483  17.466  1.00 28.10 ? 248  PRO A CG  1 
ATOM   1887 C  CD  . PRO A 1 248 ? 52.473  52.078  16.090  1.00 25.96 ? 248  PRO A CD  1 
ATOM   1888 N  N   . LYS A 1 249 ? 48.688  52.021  16.136  1.00 27.10 ? 249  LYS A N   1 
ATOM   1889 C  CA  . LYS A 1 249 ? 47.248  52.298  16.040  1.00 25.65 ? 249  LYS A CA  1 
ATOM   1890 C  C   . LYS A 1 249 ? 46.639  51.686  14.765  1.00 26.81 ? 249  LYS A C   1 
ATOM   1891 O  O   . LYS A 1 249 ? 45.556  51.057  14.831  1.00 26.67 ? 249  LYS A O   1 
ATOM   1892 C  CB  . LYS A 1 249 ? 46.973  53.840  16.109  1.00 28.72 ? 249  LYS A CB  1 
ATOM   1893 N  N   . GLN A 1 250 ? 47.308  51.840  13.622  1.00 24.76 ? 250  GLN A N   1 
ATOM   1894 C  CA  . GLN A 1 250 ? 46.805  51.267  12.391  1.00 24.57 ? 250  GLN A CA  1 
ATOM   1895 C  C   . GLN A 1 250 ? 46.804  49.734  12.515  1.00 22.77 ? 250  GLN A C   1 
ATOM   1896 O  O   . GLN A 1 250 ? 45.909  49.069  11.982  1.00 22.73 ? 250  GLN A O   1 
ATOM   1897 C  CB  . GLN A 1 250 ? 47.653  51.669  11.196  1.00 26.15 ? 250  GLN A CB  1 
ATOM   1898 C  CG  . GLN A 1 250 ? 47.086  51.204  9.881   1.00 30.83 ? 250  GLN A CG  1 
ATOM   1899 C  CD  . GLN A 1 250 ? 47.696  51.935  8.699   1.00 35.37 ? 250  GLN A CD  1 
ATOM   1900 O  OE1 . GLN A 1 250 ? 48.588  52.799  8.865   1.00 38.84 ? 250  GLN A OE1 1 
ATOM   1901 N  NE2 . GLN A 1 250 ? 47.227  51.608  7.496   1.00 36.91 ? 250  GLN A NE2 1 
ATOM   1902 N  N   . MET A 1 251 ? 47.810  49.197  13.195  1.00 21.29 ? 251  MET A N   1 
ATOM   1903 C  CA  . MET A 1 251 ? 47.871  47.731  13.401  1.00 20.30 ? 251  MET A CA  1 
ATOM   1904 C  C   . MET A 1 251 ? 46.589  47.252  14.111  1.00 21.03 ? 251  MET A C   1 
ATOM   1905 O  O   . MET A 1 251 ? 45.966  46.241  13.691  1.00 18.39 ? 251  MET A O   1 
ATOM   1906 C  CB  . MET A 1 251 ? 49.079  47.361  14.262  1.00 18.87 ? 251  MET A CB  1 
ATOM   1907 C  CG  . MET A 1 251 ? 49.289  45.810  14.415  1.00 19.03 ? 251  MET A CG  1 
ATOM   1908 S  SD  . MET A 1 251 ? 50.424  45.482  15.754  1.00 19.30 ? 251  MET A SD  1 
ATOM   1909 C  CE  . MET A 1 251 ? 51.952  46.183  15.068  1.00 20.53 ? 251  MET A CE  1 
ATOM   1910 N  N   . LEU A 1 252 ? 46.188  47.929  15.191  1.00 20.11 ? 252  LEU A N   1 
ATOM   1911 C  CA  . LEU A 1 252 ? 44.982  47.517  15.903  1.00 19.78 ? 252  LEU A CA  1 
ATOM   1912 C  C   . LEU A 1 252 ? 43.742  47.702  15.049  1.00 21.28 ? 252  LEU A C   1 
ATOM   1913 O  O   . LEU A 1 252 ? 42.855  46.854  15.050  1.00 19.61 ? 252  LEU A O   1 
ATOM   1914 C  CB  . LEU A 1 252 ? 44.842  48.230  17.249  1.00 21.05 ? 252  LEU A CB  1 
ATOM   1915 C  CG  . LEU A 1 252 ? 46.033  48.020  18.207  1.00 21.01 ? 252  LEU A CG  1 
ATOM   1916 C  CD1 . LEU A 1 252 ? 45.777  48.834  19.450  1.00 20.81 ? 252  LEU A CD1 1 
ATOM   1917 C  CD2 . LEU A 1 252 ? 46.195  46.522  18.615  1.00 19.97 ? 252  LEU A CD2 1 
ATOM   1918 N  N   . ALA A 1 253 ? 43.677  48.786  14.269  1.00 21.13 ? 253  ALA A N   1 
ATOM   1919 C  CA  . ALA A 1 253 ? 42.527  48.960  13.414  1.00 21.57 ? 253  ALA A CA  1 
ATOM   1920 C  C   . ALA A 1 253 ? 42.427  47.842  12.380  1.00 20.12 ? 253  ALA A C   1 
ATOM   1921 O  O   . ALA A 1 253 ? 41.313  47.342  12.133  1.00 21.00 ? 253  ALA A O   1 
ATOM   1922 C  CB  . ALA A 1 253 ? 42.612  50.336  12.703  1.00 21.94 ? 253  ALA A CB  1 
ATOM   1923 N  N   . GLU A 1 254 ? 43.541  47.449  11.772  1.00 19.82 ? 254  GLU A N   1 
ATOM   1924 C  CA  . GLU A 1 254 ? 43.488  46.423  10.746  1.00 20.08 ? 254  GLU A CA  1 
ATOM   1925 C  C   . GLU A 1 254 ? 43.169  45.056  11.356  1.00 19.59 ? 254  GLU A C   1 
ATOM   1926 O  O   . GLU A 1 254 ? 42.438  44.282  10.766  1.00 19.20 ? 254  GLU A O   1 
ATOM   1927 C  CB  . GLU A 1 254 ? 44.789  46.393  9.948   1.00 21.87 ? 254  GLU A CB  1 
ATOM   1928 C  CG  . GLU A 1 254 ? 44.759  47.461  8.850   1.00 26.92 ? 254  GLU A CG  1 
ATOM   1929 C  CD  . GLU A 1 254 ? 46.035  47.553  8.035   1.00 30.54 ? 254  GLU A CD  1 
ATOM   1930 O  OE1 . GLU A 1 254 ? 46.648  46.498  7.723   1.00 30.11 ? 254  GLU A OE1 1 
ATOM   1931 O  OE2 . GLU A 1 254 ? 46.392  48.713  7.686   1.00 32.23 ? 254  GLU A OE2 1 
ATOM   1932 N  N   . LEU A 1 255 ? 43.669  44.814  12.562  1.00 18.69 ? 255  LEU A N   1 
ATOM   1933 C  CA  . LEU A 1 255 ? 43.347  43.538  13.231  1.00 17.43 ? 255  LEU A CA  1 
ATOM   1934 C  C   . LEU A 1 255 ? 41.865  43.498  13.505  1.00 18.42 ? 255  LEU A C   1 
ATOM   1935 O  O   . LEU A 1 255 ? 41.238  42.456  13.267  1.00 18.04 ? 255  LEU A O   1 
ATOM   1936 C  CB  . LEU A 1 255 ? 44.127  43.379  14.546  1.00 17.24 ? 255  LEU A CB  1 
ATOM   1937 C  CG  . LEU A 1 255 ? 45.611  43.057  14.338  1.00 17.50 ? 255  LEU A CG  1 
ATOM   1938 C  CD1 . LEU A 1 255 ? 46.374  43.330  15.666  1.00 17.96 ? 255  LEU A CD1 1 
ATOM   1939 C  CD2 . LEU A 1 255 ? 45.789  41.585  13.853  1.00 18.14 ? 255  LEU A CD2 1 
ATOM   1940 N  N   . ARG A 1 256 ? 41.292  44.599  13.993  1.00 18.73 ? 256  ARG A N   1 
ATOM   1941 C  CA  . ARG A 1 256 ? 39.866  44.653  14.281  1.00 19.01 ? 256  ARG A CA  1 
ATOM   1942 C  C   . ARG A 1 256 ? 39.028  44.358  13.033  1.00 19.46 ? 256  ARG A C   1 
ATOM   1943 O  O   . ARG A 1 256 ? 38.085  43.522  13.067  1.00 20.20 ? 256  ARG A O   1 
ATOM   1944 C  CB  . ARG A 1 256 ? 39.494  46.027  14.842  1.00 20.26 ? 256  ARG A CB  1 
ATOM   1945 C  CG  . ARG A 1 256 ? 38.012  46.121  15.097  1.00 22.64 ? 256  ARG A CG  1 
ATOM   1946 C  CD  . ARG A 1 256 ? 37.687  47.451  15.708  1.00 23.85 ? 256  ARG A CD  1 
ATOM   1947 N  NE  . ARG A 1 256 ? 38.252  47.567  17.042  1.00 25.58 ? 256  ARG A NE  1 
ATOM   1948 C  CZ  . ARG A 1 256 ? 37.688  47.097  18.150  1.00 25.73 ? 256  ARG A CZ  1 
ATOM   1949 N  NH1 . ARG A 1 256 ? 38.318  47.285  19.305  1.00 26.55 ? 256  ARG A NH1 1 
ATOM   1950 N  NH2 . ARG A 1 256 ? 36.509  46.432  18.101  1.00 25.80 ? 256  ARG A NH2 1 
ATOM   1951 N  N   . SER A 1 257 ? 39.335  45.029  11.929  1.00 19.68 ? 257  SER A N   1 
ATOM   1952 C  CA  . SER A 1 257 ? 38.602  44.797  10.681  1.00 20.76 ? 257  SER A CA  1 
ATOM   1953 C  C   . SER A 1 257 ? 38.671  43.340  10.226  1.00 20.35 ? 257  SER A C   1 
ATOM   1954 O  O   . SER A 1 257 ? 37.654  42.749  9.828   1.00 18.76 ? 257  SER A O   1 
ATOM   1955 C  CB  . SER A 1 257 ? 39.162  45.685  9.577   1.00 23.26 ? 257  SER A CB  1 
ATOM   1956 O  OG  . SER A 1 257 ? 39.113  47.026  9.986   1.00 28.86 ? 257  SER A OG  1 
ATOM   1957 N  N   . PHE A 1 258 ? 39.860  42.758  10.291  1.00 18.22 ? 258  PHE A N   1 
ATOM   1958 C  CA  . PHE A 1 258 ? 40.050  41.380  9.855   1.00 17.75 ? 258  PHE A CA  1 
ATOM   1959 C  C   . PHE A 1 258 ? 39.294  40.393  10.738  1.00 17.54 ? 258  PHE A C   1 
ATOM   1960 O  O   . PHE A 1 258 ? 38.533  39.563  10.240  1.00 16.15 ? 258  PHE A O   1 
ATOM   1961 C  CB  . PHE A 1 258 ? 41.539  41.023  9.850   1.00 18.75 ? 258  PHE A CB  1 
ATOM   1962 C  CG  . PHE A 1 258 ? 41.831  39.656  9.296   1.00 19.33 ? 258  PHE A CG  1 
ATOM   1963 C  CD1 . PHE A 1 258 ? 41.653  39.387  7.943   1.00 20.86 ? 258  PHE A CD1 1 
ATOM   1964 C  CD2 . PHE A 1 258 ? 42.269  38.633  10.130  1.00 20.35 ? 258  PHE A CD2 1 
ATOM   1965 C  CE1 . PHE A 1 258 ? 41.908  38.116  7.426   1.00 22.12 ? 258  PHE A CE1 1 
ATOM   1966 C  CE2 . PHE A 1 258 ? 42.526  37.359  9.625   1.00 20.58 ? 258  PHE A CE2 1 
ATOM   1967 C  CZ  . PHE A 1 258 ? 42.345  37.100  8.269   1.00 21.10 ? 258  PHE A CZ  1 
ATOM   1968 N  N   . VAL A 1 259 ? 39.480  40.514  12.058  1.00 16.67 ? 259  VAL A N   1 
ATOM   1969 C  CA  . VAL A 1 259 ? 38.819  39.600  12.979  1.00 15.54 ? 259  VAL A CA  1 
ATOM   1970 C  C   . VAL A 1 259 ? 37.320  39.735  12.850  1.00 18.65 ? 259  VAL A C   1 
ATOM   1971 O  O   . VAL A 1 259 ? 36.597  38.736  12.792  1.00 18.51 ? 259  VAL A O   1 
ATOM   1972 C  CB  . VAL A 1 259 ? 39.280  39.840  14.463  1.00 14.89 ? 259  VAL A CB  1 
ATOM   1973 C  CG1 . VAL A 1 259 ? 38.469  39.005  15.406  1.00 15.69 ? 259  VAL A CG1 1 
ATOM   1974 C  CG2 . VAL A 1 259 ? 40.792  39.498  14.604  1.00 17.16 ? 259  VAL A CG2 1 
ATOM   1975 N  N   . SER A 1 260 ? 36.832  40.979  12.798  1.00 17.55 ? 260  SER A N   1 
ATOM   1976 C  CA  . SER A 1 260 ? 35.405  41.163  12.664  1.00 18.26 ? 260  SER A CA  1 
ATOM   1977 C  C   . SER A 1 260 ? 34.866  40.441  11.423  1.00 16.58 ? 260  SER A C   1 
ATOM   1978 O  O   . SER A 1 260 ? 33.789  39.780  11.495  1.00 17.18 ? 260  SER A O   1 
ATOM   1979 C  CB  . SER A 1 260 ? 35.083  42.665  12.592  1.00 20.05 ? 260  SER A CB  1 
ATOM   1980 O  OG  . SER A 1 260 ? 33.685  42.831  12.508  1.00 27.02 ? 260  SER A OG  1 
ATOM   1981 N  N   . ALA A 1 261 ? 35.566  40.531  10.296  1.00 17.66 ? 261  ALA A N   1 
ATOM   1982 C  CA  . ALA A 1 261 ? 35.086  39.889  9.054   1.00 16.12 ? 261  ALA A CA  1 
ATOM   1983 C  C   . ALA A 1 261 ? 35.136  38.370  9.173   1.00 17.53 ? 261  ALA A C   1 
ATOM   1984 O  O   . ALA A 1 261 ? 34.206  37.653  8.707   1.00 17.77 ? 261  ALA A O   1 
ATOM   1985 C  CB  . ALA A 1 261 ? 35.924  40.332  7.843   1.00 16.45 ? 261  ALA A CB  1 
ATOM   1986 N  N   . MET A 1 262 ? 36.229  37.874  9.754   1.00 16.55 ? 262  MET A N   1 
ATOM   1987 C  CA  . MET A 1 262 ? 36.380  36.431  9.908   1.00 15.17 ? 262  MET A CA  1 
ATOM   1988 C  C   . MET A 1 262 ? 35.311  35.892  10.862  1.00 15.35 ? 262  MET A C   1 
ATOM   1989 O  O   . MET A 1 262 ? 34.707  34.839  10.584  1.00 16.23 ? 262  MET A O   1 
ATOM   1990 C  CB  . MET A 1 262 ? 37.796  36.084  10.440  1.00 15.25 ? 262  MET A CB  1 
ATOM   1991 C  CG  . MET A 1 262 ? 38.953  36.430  9.478   1.00 16.29 ? 262  MET A CG  1 
ATOM   1992 S  SD  . MET A 1 262 ? 38.939  35.429  7.975   1.00 16.62 ? 262  MET A SD  1 
ATOM   1993 C  CE  . MET A 1 262 ? 39.869  33.920  8.601   1.00 17.03 ? 262  MET A CE  1 
ATOM   1994 N  N   . LYS A 1 263 ? 35.068  36.567  11.983  1.00 15.95 ? 263  LYS A N   1 
ATOM   1995 C  CA  . LYS A 1 263 ? 34.030  36.109  12.898  1.00 16.25 ? 263  LYS A CA  1 
ATOM   1996 C  C   . LYS A 1 263 ? 32.637  36.176  12.215  1.00 16.59 ? 263  LYS A C   1 
ATOM   1997 O  O   . LYS A 1 263 ? 31.774  35.279  12.407  1.00 16.43 ? 263  LYS A O   1 
ATOM   1998 C  CB  . LYS A 1 263 ? 34.006  36.963  14.187  1.00 17.50 ? 263  LYS A CB  1 
ATOM   1999 C  CG  . LYS A 1 263 ? 32.835  36.622  15.108  1.00 15.84 ? 263  LYS A CG  1 
ATOM   2000 C  CD  . LYS A 1 263 ? 32.821  35.095  15.477  1.00 16.13 ? 263  LYS A CD  1 
ATOM   2001 C  CE  . LYS A 1 263 ? 31.479  34.701  16.070  1.00 17.70 ? 263  LYS A CE  1 
ATOM   2002 N  NZ  . LYS A 1 263 ? 31.358  33.161  16.235  1.00 18.01 ? 263  LYS A NZ  1 
ATOM   2003 N  N   . ALA A 1 264 ? 32.385  37.200  11.402  1.00 18.04 ? 264  ALA A N   1 
ATOM   2004 C  CA  . ALA A 1 264 ? 31.064  37.291  10.768  1.00 18.12 ? 264  ALA A CA  1 
ATOM   2005 C  C   . ALA A 1 264 ? 30.753  36.063  9.889   1.00 17.93 ? 264  ALA A C   1 
ATOM   2006 O  O   . ALA A 1 264 ? 29.608  35.581  9.828   1.00 18.85 ? 264  ALA A O   1 
ATOM   2007 C  CB  . ALA A 1 264 ? 30.965  38.598  9.923   1.00 19.23 ? 264  ALA A CB  1 
ATOM   2008 N  N   . ALA A 1 265 ? 31.776  35.584  9.207   1.00 16.84 ? 265  ALA A N   1 
ATOM   2009 C  CA  . ALA A 1 265 ? 31.678  34.424  8.348   1.00 16.13 ? 265  ALA A CA  1 
ATOM   2010 C  C   . ALA A 1 265 ? 31.341  33.136  9.071   1.00 18.66 ? 265  ALA A C   1 
ATOM   2011 O  O   . ALA A 1 265 ? 30.934  32.172  8.444   1.00 18.45 ? 265  ALA A O   1 
ATOM   2012 C  CB  . ALA A 1 265 ? 32.984  34.234  7.567   1.00 14.79 ? 265  ALA A CB  1 
ATOM   2013 N  N   . SER A 1 266 ? 31.488  33.119  10.391  1.00 18.82 ? 266  SER A N   1 
ATOM   2014 C  CA  . SER A 1 266 ? 31.201  31.893  11.112  1.00 20.05 ? 266  SER A CA  1 
ATOM   2015 C  C   . SER A 1 266 ? 29.735  31.768  11.461  1.00 23.76 ? 266  SER A C   1 
ATOM   2016 O  O   . SER A 1 266 ? 29.310  30.712  11.971  1.00 23.41 ? 266  SER A O   1 
ATOM   2017 C  CB  . SER A 1 266 ? 32.012  31.835  12.399  1.00 21.08 ? 266  SER A CB  1 
ATOM   2018 O  OG  . SER A 1 266 ? 31.528  32.775  13.316  1.00 20.06 ? 266  SER A OG  1 
ATOM   2019 N  N   . ARG A 1 267 ? 28.977  32.837  11.199  1.00 25.89 ? 267  ARG A N   1 
ATOM   2020 C  CA  . ARG A 1 267 ? 27.540  32.888  11.519  1.00 29.45 ? 267  ARG A CA  1 
ATOM   2021 C  C   . ARG A 1 267 ? 26.736  32.421  10.325  1.00 29.80 ? 267  ARG A C   1 
ATOM   2022 O  O   . ARG A 1 267 ? 27.292  32.181  9.245   1.00 31.88 ? 267  ARG A O   1 
ATOM   2023 C  CB  . ARG A 1 267 ? 27.132  34.333  11.916  1.00 29.69 ? 267  ARG A CB  1 
ATOM   2024 C  CG  . ARG A 1 267 ? 27.889  34.903  13.123  1.00 32.61 ? 267  ARG A CG  1 
ATOM   2025 C  CD  . ARG A 1 267 ? 27.384  36.277  13.618  1.00 34.08 ? 267  ARG A CD  1 
ATOM   2026 N  NE  . ARG A 1 267 ? 28.192  36.812  14.732  1.00 35.93 ? 267  ARG A NE  1 
ATOM   2027 C  CZ  . ARG A 1 267 ? 29.131  37.755  14.613  1.00 35.05 ? 267  ARG A CZ  1 
ATOM   2028 N  NH1 . ARG A 1 267 ? 29.403  38.305  13.423  1.00 34.09 ? 267  ARG A NH1 1 
ATOM   2029 N  NH2 . ARG A 1 267 ? 29.818  38.133  15.690  1.00 34.89 ? 267  ARG A NH2 1 
ATOM   2030 N  N   . THR B 2 1   ? 52.416  1.406   16.405  1.00 33.43 ? 2    THR B N   1 
ATOM   2031 C  CA  . THR B 2 1   ? 53.618  1.178   17.189  1.00 30.14 ? 2    THR B CA  1 
ATOM   2032 C  C   . THR B 2 1   ? 54.785  1.191   16.193  1.00 26.37 ? 2    THR B C   1 
ATOM   2033 O  O   . THR B 2 1   ? 54.699  1.879   15.148  1.00 26.48 ? 2    THR B O   1 
ATOM   2034 C  CB  . THR B 2 1   ? 53.513  -0.159  17.961  1.00 32.93 ? 2    THR B CB  1 
ATOM   2035 O  OG1 . THR B 2 1   ? 52.362  -0.103  18.830  1.00 37.49 ? 2    THR B OG1 1 
ATOM   2036 C  CG2 . THR B 2 1   ? 54.770  -0.425  18.831  1.00 35.13 ? 2    THR B CG2 1 
ATOM   2037 N  N   . THR B 2 2   ? 55.881  0.506   16.528  1.00 20.45 ? 3    THR B N   1 
ATOM   2038 C  CA  . THR B 2 2   ? 57.046  0.447   15.609  1.00 16.58 ? 3    THR B CA  1 
ATOM   2039 C  C   . THR B 2 2   ? 57.619  -0.947  15.580  1.00 15.20 ? 3    THR B C   1 
ATOM   2040 O  O   . THR B 2 2   ? 57.335  -1.760  16.460  1.00 16.83 ? 3    THR B O   1 
ATOM   2041 C  CB  . THR B 2 2   ? 58.178  1.427   16.057  1.00 16.87 ? 3    THR B CB  1 
ATOM   2042 O  OG1 . THR B 2 2   ? 58.601  1.104   17.375  1.00 16.14 ? 3    THR B OG1 1 
ATOM   2043 C  CG2 . THR B 2 2   ? 57.676  2.893   15.977  1.00 18.42 ? 3    THR B CG2 1 
ATOM   2044 N  N   . LEU B 2 3   ? 58.462  -1.218  14.588  1.00 12.51 ? 4    LEU B N   1 
ATOM   2045 C  CA  . LEU B 2 3   ? 59.061  -2.547  14.486  1.00 13.32 ? 4    LEU B CA  1 
ATOM   2046 C  C   . LEU B 2 3   ? 60.272  -2.699  15.390  1.00 13.25 ? 4    LEU B C   1 
ATOM   2047 O  O   . LEU B 2 3   ? 60.583  -3.803  15.880  1.00 15.77 ? 4    LEU B O   1 
ATOM   2048 C  CB  . LEU B 2 3   ? 59.526  -2.752  13.052  1.00 13.41 ? 4    LEU B CB  1 
ATOM   2049 C  CG  . LEU B 2 3   ? 58.442  -2.702  11.989  1.00 13.80 ? 4    LEU B CG  1 
ATOM   2050 C  CD1 . LEU B 2 3   ? 59.074  -2.709  10.567  1.00 16.84 ? 4    LEU B CD1 1 
ATOM   2051 C  CD2 . LEU B 2 3   ? 57.560  -3.950  12.180  1.00 15.32 ? 4    LEU B CD2 1 
ATOM   2052 N  N   . LEU B 2 4   ? 60.959  -1.567  15.620  1.00 12.20 ? 5    LEU B N   1 
ATOM   2053 C  CA  . LEU B 2 4   ? 62.177  -1.543  16.438  1.00 12.92 ? 5    LEU B CA  1 
ATOM   2054 C  C   . LEU B 2 4   ? 61.977  -0.555  17.585  1.00 12.20 ? 5    LEU B C   1 
ATOM   2055 O  O   . LEU B 2 4   ? 61.133  0.371   17.523  1.00 12.43 ? 5    LEU B O   1 
ATOM   2056 C  CB  . LEU B 2 4   ? 63.364  -1.055  15.611  1.00 13.18 ? 5    LEU B CB  1 
ATOM   2057 C  CG  . LEU B 2 4   ? 63.611  -1.790  14.288  1.00 14.20 ? 5    LEU B CG  1 
ATOM   2058 C  CD1 . LEU B 2 4   ? 64.740  -1.163  13.510  1.00 14.90 ? 5    LEU B CD1 1 
ATOM   2059 C  CD2 . LEU B 2 4   ? 63.918  -3.289  14.567  1.00 16.68 ? 5    LEU B CD2 1 
ATOM   2060 N  N   . ASN B 2 5   ? 62.756  -0.742  18.631  1.00 13.09 ? 6    ASN B N   1 
ATOM   2061 C  CA  . ASN B 2 5   ? 62.620  0.119   19.801  1.00 11.70 ? 6    ASN B CA  1 
ATOM   2062 C  C   . ASN B 2 5   ? 63.142  1.530   19.466  1.00 10.42 ? 6    ASN B C   1 
ATOM   2063 O  O   . ASN B 2 5   ? 64.293  1.673   19.109  1.00 12.03 ? 6    ASN B O   1 
ATOM   2064 C  CB  . ASN B 2 5   ? 63.471  -0.470  20.929  1.00 13.42 ? 6    ASN B CB  1 
ATOM   2065 C  CG  . ASN B 2 5   ? 63.201  0.180   22.241  1.00 14.78 ? 6    ASN B CG  1 
ATOM   2066 O  OD1 . ASN B 2 5   ? 62.590  1.239   22.328  1.00 13.11 ? 6    ASN B OD1 1 
ATOM   2067 N  ND2 . ASN B 2 5   ? 63.632  -0.486  23.326  1.00 17.91 ? 6    ASN B ND2 1 
ATOM   2068 N  N   . PRO B 2 6   ? 62.320  2.570   19.644  1.00 9.81  ? 7    PRO B N   1 
ATOM   2069 C  CA  . PRO B 2 6   ? 62.774  3.945   19.332  1.00 9.58  ? 7    PRO B CA  1 
ATOM   2070 C  C   . PRO B 2 6   ? 63.624  4.543   20.423  1.00 9.02  ? 7    PRO B C   1 
ATOM   2071 O  O   . PRO B 2 6   ? 64.152  5.651   20.207  1.00 9.43  ? 7    PRO B O   1 
ATOM   2072 C  CB  . PRO B 2 6   ? 61.482  4.757   19.194  1.00 10.50 ? 7    PRO B CB  1 
ATOM   2073 C  CG  . PRO B 2 6   ? 60.364  3.719   19.154  1.00 12.32 ? 7    PRO B CG  1 
ATOM   2074 C  CD  . PRO B 2 6   ? 60.875  2.526   19.922  1.00 9.73  ? 7    PRO B CD  1 
ATOM   2075 N  N   . TYR B 2 7   ? 63.719  3.863   21.555  1.00 9.26  ? 8    TYR B N   1 
ATOM   2076 C  CA  . TYR B 2 7   ? 64.475  4.353   22.703  1.00 8.55  ? 8    TYR B CA  1 
ATOM   2077 C  C   . TYR B 2 7   ? 65.697  3.544   23.114  1.00 9.52  ? 8    TYR B C   1 
ATOM   2078 O  O   . TYR B 2 7   ? 65.766  2.332   22.909  1.00 11.13 ? 8    TYR B O   1 
ATOM   2079 C  CB  . TYR B 2 7   ? 63.546  4.450   23.919  1.00 9.02  ? 8    TYR B CB  1 
ATOM   2080 C  CG  . TYR B 2 7   ? 62.628  5.649   23.912  1.00 9.26  ? 8    TYR B CG  1 
ATOM   2081 C  CD1 . TYR B 2 7   ? 63.050  6.870   24.432  1.00 11.10 ? 8    TYR B CD1 1 
ATOM   2082 C  CD2 . TYR B 2 7   ? 61.343  5.570   23.376  1.00 10.57 ? 8    TYR B CD2 1 
ATOM   2083 C  CE1 . TYR B 2 7   ? 62.221  7.983   24.423  1.00 10.83 ? 8    TYR B CE1 1 
ATOM   2084 C  CE2 . TYR B 2 7   ? 60.503  6.684   23.359  1.00 10.38 ? 8    TYR B CE2 1 
ATOM   2085 C  CZ  . TYR B 2 7   ? 60.951  7.886   23.886  1.00 10.97 ? 8    TYR B CZ  1 
ATOM   2086 O  OH  . TYR B 2 7   ? 60.134  8.992   23.868  1.00 13.29 ? 8    TYR B OH  1 
ATOM   2087 N  N   . PHE B 2 8   ? 66.657  4.251   23.702  1.00 8.61  ? 9    PHE B N   1 
ATOM   2088 C  CA  . PHE B 2 8   ? 67.878  3.666   24.251  1.00 8.53  ? 9    PHE B CA  1 
ATOM   2089 C  C   . PHE B 2 8   ? 67.736  4.138   25.692  1.00 8.72  ? 9    PHE B C   1 
ATOM   2090 O  O   . PHE B 2 8   ? 68.133  5.253   26.039  1.00 8.98  ? 9    PHE B O   1 
ATOM   2091 C  CB  . PHE B 2 8   ? 69.116  4.278   23.591  1.00 7.83  ? 9    PHE B CB  1 
ATOM   2092 C  CG  . PHE B 2 8   ? 69.227  3.981   22.123  1.00 8.06  ? 9    PHE B CG  1 
ATOM   2093 C  CD1 . PHE B 2 8   ? 69.830  2.808   21.676  1.00 9.11  ? 9    PHE B CD1 1 
ATOM   2094 C  CD2 . PHE B 2 8   ? 68.698  4.861   21.187  1.00 8.12  ? 9    PHE B CD2 1 
ATOM   2095 C  CE1 . PHE B 2 8   ? 69.903  2.518   20.312  1.00 8.66  ? 9    PHE B CE1 1 
ATOM   2096 C  CE2 . PHE B 2 8   ? 68.764  4.581   19.822  1.00 9.16  ? 9    PHE B CE2 1 
ATOM   2097 C  CZ  . PHE B 2 8   ? 69.369  3.403   19.385  1.00 9.27  ? 9    PHE B CZ  1 
ATOM   2098 N  N   . GLY B 2 9   ? 67.182  3.236   26.529  1.00 9.16  ? 10   GLY B N   1 
ATOM   2099 C  CA  . GLY B 2 9   ? 66.866  3.688   27.889  1.00 10.43 ? 10   GLY B CA  1 
ATOM   2100 C  C   . GLY B 2 9   ? 65.850  4.829   27.770  1.00 10.00 ? 10   GLY B C   1 
ATOM   2101 O  O   . GLY B 2 9   ? 64.834  4.702   27.082  1.00 11.20 ? 10   GLY B O   1 
ATOM   2102 N  N   . GLU B 2 10  ? 66.108  5.929   28.479  1.00 9.91  ? 11   GLU B N   1 
ATOM   2103 C  CA  . GLU B 2 10  ? 65.183  7.070   28.426  1.00 10.61 ? 11   GLU B CA  1 
ATOM   2104 C  C   . GLU B 2 10  ? 65.364  7.977   27.211  1.00 10.49 ? 11   GLU B C   1 
ATOM   2105 O  O   . GLU B 2 10  ? 64.522  8.814   26.913  1.00 12.02 ? 11   GLU B O   1 
ATOM   2106 C  CB  . GLU B 2 10  ? 65.291  7.908   29.720  1.00 16.23 ? 11   GLU B CB  1 
ATOM   2107 C  CG  . GLU B 2 10  ? 66.522  8.807   29.829  1.00 21.54 ? 11   GLU B CG  1 
ATOM   2108 C  CD  . GLU B 2 10  ? 66.419  10.049  30.873  1.00 27.08 ? 11   GLU B CD  1 
ATOM   2109 O  OE1 . GLU B 2 10  ? 65.340  10.668  31.006  1.00 32.95 ? 11   GLU B OE1 1 
ATOM   2110 O  OE2 . GLU B 2 10  ? 67.441  10.449  31.504  1.00 29.59 ? 11   GLU B OE2 1 
ATOM   2111 N  N   . PHE B 2 11  ? 66.449  7.769   26.497  1.00 9.39  ? 12   PHE B N   1 
ATOM   2112 C  CA  . PHE B 2 11  ? 66.805  8.628   25.370  1.00 7.83  ? 12   PHE B CA  1 
ATOM   2113 C  C   . PHE B 2 11  ? 66.317  8.181   23.999  1.00 8.11  ? 12   PHE B C   1 
ATOM   2114 O  O   . PHE B 2 11  ? 66.267  6.991   23.706  1.00 9.63  ? 12   PHE B O   1 
ATOM   2115 C  CB  . PHE B 2 11  ? 68.326  8.779   25.332  1.00 7.97  ? 12   PHE B CB  1 
ATOM   2116 C  CG  . PHE B 2 11  ? 68.931  9.115   26.665  1.00 9.06  ? 12   PHE B CG  1 
ATOM   2117 C  CD1 . PHE B 2 11  ? 68.835  10.404  27.183  1.00 8.37  ? 12   PHE B CD1 1 
ATOM   2118 C  CD2 . PHE B 2 11  ? 69.576  8.135   27.417  1.00 9.43  ? 12   PHE B CD2 1 
ATOM   2119 C  CE1 . PHE B 2 11  ? 69.374  10.712  28.434  1.00 9.14  ? 12   PHE B CE1 1 
ATOM   2120 C  CE2 . PHE B 2 11  ? 70.118  8.433   28.670  1.00 10.40 ? 12   PHE B CE2 1 
ATOM   2121 C  CZ  . PHE B 2 11  ? 70.016  9.723   29.177  1.00 9.66  ? 12   PHE B CZ  1 
ATOM   2122 N  N   . GLY B 2 12  ? 65.957  9.159   23.174  1.00 7.83  ? 13   GLY B N   1 
ATOM   2123 C  CA  . GLY B 2 12  ? 65.536  8.829   21.797  1.00 7.08  ? 13   GLY B CA  1 
ATOM   2124 C  C   . GLY B 2 12  ? 64.104  9.261   21.531  1.00 7.78  ? 13   GLY B C   1 
ATOM   2125 O  O   . GLY B 2 12  ? 63.666  10.367  21.883  1.00 7.79  ? 13   GLY B O   1 
ATOM   2126 N  N   . GLY B 2 13  ? 63.336  8.373   20.935  1.00 6.87  ? 14   GLY B N   1 
ATOM   2127 C  CA  . GLY B 2 13  ? 61.945  8.693   20.644  1.00 9.14  ? 14   GLY B CA  1 
ATOM   2128 C  C   . GLY B 2 13  ? 61.725  9.259   19.241  1.00 7.96  ? 14   GLY B C   1 
ATOM   2129 O  O   . GLY B 2 13  ? 62.644  9.323   18.394  1.00 7.51  ? 14   GLY B O   1 
ATOM   2130 N  N   . MET B 2 14  ? 60.470  9.714   19.044  1.00 9.14  ? 15   MET B N   1 
ATOM   2131 C  CA  . MET B 2 14  ? 59.993  10.249  17.757  1.00 9.98  ? 15   MET B CA  1 
ATOM   2132 C  C   . MET B 2 14  ? 59.220  11.527  17.999  1.00 9.47  ? 15   MET B C   1 
ATOM   2133 O  O   . MET B 2 14  ? 58.022  11.567  17.798  1.00 11.11 ? 15   MET B O   1 
ATOM   2134 C  CB  . MET B 2 14  ? 59.083  9.186   17.036  1.00 10.88 ? 15   MET B CB  1 
ATOM   2135 C  CG  . MET B 2 14  ? 59.944  7.951   16.741  1.00 10.68 ? 15   MET B CG  1 
ATOM   2136 S  SD  . MET B 2 14  ? 58.897  6.533   16.192  1.00 13.09 ? 15   MET B SD  1 
ATOM   2137 C  CE  . MET B 2 14  ? 58.636  6.830   14.583  1.00 13.42 ? 15   MET B CE  1 
ATOM   2138 N  N   . TYR B 2 15  ? 59.922  12.568  18.425  1.00 10.00 ? 16   TYR B N   1 
ATOM   2139 C  CA  . TYR B 2 15  ? 59.253  13.827  18.717  1.00 9.51  ? 16   TYR B CA  1 
ATOM   2140 C  C   . TYR B 2 15  ? 59.158  14.754  17.515  1.00 10.35 ? 16   TYR B C   1 
ATOM   2141 O  O   . TYR B 2 15  ? 59.858  15.762  17.430  1.00 10.84 ? 16   TYR B O   1 
ATOM   2142 C  CB  . TYR B 2 15  ? 59.953  14.534  19.881  1.00 8.60  ? 16   TYR B CB  1 
ATOM   2143 C  CG  . TYR B 2 15  ? 59.880  13.758  21.178  1.00 9.44  ? 16   TYR B CG  1 
ATOM   2144 C  CD1 . TYR B 2 15  ? 60.838  12.793  21.495  1.00 9.44  ? 16   TYR B CD1 1 
ATOM   2145 C  CD2 . TYR B 2 15  ? 58.847  13.984  22.087  1.00 10.11 ? 16   TYR B CD2 1 
ATOM   2146 C  CE1 . TYR B 2 15  ? 60.769  12.076  22.687  1.00 10.98 ? 16   TYR B CE1 1 
ATOM   2147 C  CE2 . TYR B 2 15  ? 58.771  13.275  23.278  1.00 10.31 ? 16   TYR B CE2 1 
ATOM   2148 C  CZ  . TYR B 2 15  ? 59.734  12.323  23.573  1.00 9.59  ? 16   TYR B CZ  1 
ATOM   2149 O  OH  . TYR B 2 15  ? 59.669  11.630  24.758  1.00 12.35 ? 16   TYR B OH  1 
ATOM   2150 N  N   . VAL B 2 16  ? 58.292  14.365  16.582  1.00 9.78  ? 17   VAL B N   1 
ATOM   2151 C  CA  . VAL B 2 16  ? 58.043  15.174  15.396  1.00 11.13 ? 17   VAL B CA  1 
ATOM   2152 C  C   . VAL B 2 16  ? 56.541  15.447  15.313  1.00 11.39 ? 17   VAL B C   1 
ATOM   2153 O  O   . VAL B 2 16  ? 55.727  14.753  15.927  1.00 11.13 ? 17   VAL B O   1 
ATOM   2154 C  CB  . VAL B 2 16  ? 58.439  14.387  14.066  1.00 11.67 ? 17   VAL B CB  1 
ATOM   2155 C  CG1 . VAL B 2 16  ? 59.981  14.207  14.007  1.00 14.04 ? 17   VAL B CG1 1 
ATOM   2156 C  CG2 . VAL B 2 16  ? 57.683  13.055  13.975  1.00 13.10 ? 17   VAL B CG2 1 
ATOM   2157 N  N   . PRO B 2 17  ? 56.173  16.477  14.528  1.00 11.63 ? 18   PRO B N   1 
ATOM   2158 C  CA  . PRO B 2 17  ? 54.743  16.749  14.365  1.00 11.03 ? 18   PRO B CA  1 
ATOM   2159 C  C   . PRO B 2 17  ? 54.071  15.477  13.794  1.00 11.30 ? 18   PRO B C   1 
ATOM   2160 O  O   . PRO B 2 17  ? 54.675  14.723  12.979  1.00 12.00 ? 18   PRO B O   1 
ATOM   2161 C  CB  . PRO B 2 17  ? 54.737  17.897  13.350  1.00 12.36 ? 18   PRO B CB  1 
ATOM   2162 C  CG  . PRO B 2 17  ? 55.960  18.690  13.740  1.00 12.11 ? 18   PRO B CG  1 
ATOM   2163 C  CD  . PRO B 2 17  ? 57.022  17.586  14.048  1.00 12.34 ? 18   PRO B CD  1 
ATOM   2164 N  N   . GLN B 2 18  ? 52.788  15.286  14.139  1.00 10.81 ? 19   GLN B N   1 
ATOM   2165 C  CA  . GLN B 2 18  ? 52.037  14.111  13.714  1.00 10.12 ? 19   GLN B CA  1 
ATOM   2166 C  C   . GLN B 2 18  ? 52.128  13.857  12.200  1.00 11.14 ? 19   GLN B C   1 
ATOM   2167 O  O   . GLN B 2 18  ? 52.182  12.696  11.741  1.00 12.35 ? 19   GLN B O   1 
ATOM   2168 C  CB  . GLN B 2 18  ? 50.548  14.292  14.093  1.00 11.71 ? 19   GLN B CB  1 
ATOM   2169 C  CG  . GLN B 2 18  ? 49.782  12.973  14.039  1.00 12.31 ? 19   GLN B CG  1 
ATOM   2170 C  CD  . GLN B 2 18  ? 50.198  12.042  15.162  1.00 12.43 ? 19   GLN B CD  1 
ATOM   2171 O  OE1 . GLN B 2 18  ? 50.068  12.382  16.343  1.00 13.94 ? 19   GLN B OE1 1 
ATOM   2172 N  NE2 . GLN B 2 18  ? 50.660  10.869  14.817  1.00 15.20 ? 19   GLN B NE2 1 
ATOM   2173 N  N   . ILE B 2 19  ? 52.088  14.940  11.427  1.00 12.08 ? 20   ILE B N   1 
ATOM   2174 C  CA  . ILE B 2 19  ? 52.116  14.805  9.956   1.00 12.50 ? 20   ILE B CA  1 
ATOM   2175 C  C   . ILE B 2 19  ? 53.333  14.018  9.453   1.00 12.69 ? 20   ILE B C   1 
ATOM   2176 O  O   . ILE B 2 19  ? 53.228  13.403  8.386   1.00 14.05 ? 20   ILE B O   1 
ATOM   2177 C  CB  . ILE B 2 19  ? 52.079  16.231  9.315   1.00 13.49 ? 20   ILE B CB  1 
ATOM   2178 C  CG1 . ILE B 2 19  ? 51.765  16.145  7.803   1.00 14.93 ? 20   ILE B CG1 1 
ATOM   2179 C  CG2 . ILE B 2 19  ? 53.409  16.974  9.543   1.00 14.54 ? 20   ILE B CG2 1 
ATOM   2180 C  CD1 . ILE B 2 19  ? 50.346  15.637  7.497   1.00 18.20 ? 20   ILE B CD1 1 
ATOM   2181 N  N   . LEU B 2 20  ? 54.441  14.000  10.206  1.00 11.38 ? 21   LEU B N   1 
ATOM   2182 C  CA  . LEU B 2 20  ? 55.656  13.260  9.766   1.00 11.52 ? 21   LEU B CA  1 
ATOM   2183 C  C   . LEU B 2 20  ? 55.756  11.838  10.257  1.00 12.65 ? 21   LEU B C   1 
ATOM   2184 O  O   . LEU B 2 20  ? 56.695  11.094  9.886   1.00 12.23 ? 21   LEU B O   1 
ATOM   2185 C  CB  . LEU B 2 20  ? 56.897  14.025  10.190  1.00 12.34 ? 21   LEU B CB  1 
ATOM   2186 C  CG  . LEU B 2 20  ? 57.313  15.186  9.306   1.00 12.85 ? 21   LEU B CG  1 
ATOM   2187 C  CD1 . LEU B 2 20  ? 58.439  15.939  9.931   1.00 13.92 ? 21   LEU B CD1 1 
ATOM   2188 C  CD2 . LEU B 2 20  ? 57.732  14.626  7.875   1.00 14.90 ? 21   LEU B CD2 1 
ATOM   2189 N  N   . MET B 2 21  ? 54.836  11.409  11.106  1.00 10.78 ? 22   MET B N   1 
ATOM   2190 C  CA  . MET B 2 21  ? 54.954  10.034  11.587  1.00 11.47 ? 22   MET B CA  1 
ATOM   2191 C  C   . MET B 2 21  ? 54.866  8.985   10.483  1.00 12.14 ? 22   MET B C   1 
ATOM   2192 O  O   . MET B 2 21  ? 55.615  8.001   10.533  1.00 11.82 ? 22   MET B O   1 
ATOM   2193 C  CB  . MET B 2 21  ? 53.939  9.734   12.669  1.00 11.56 ? 22   MET B CB  1 
ATOM   2194 C  CG  . MET B 2 21  ? 54.234  10.543  13.976  1.00 13.95 ? 22   MET B CG  1 
ATOM   2195 S  SD  . MET B 2 21  ? 55.868  9.988   14.754  1.00 15.01 ? 22   MET B SD  1 
ATOM   2196 C  CE  . MET B 2 21  ? 55.495  8.208   14.935  1.00 18.81 ? 22   MET B CE  1 
ATOM   2197 N  N   . PRO B 2 22  ? 53.972  9.162   9.495   1.00 12.84 ? 23   PRO B N   1 
ATOM   2198 C  CA  . PRO B 2 22  ? 53.961  8.098   8.478   1.00 11.85 ? 23   PRO B CA  1 
ATOM   2199 C  C   . PRO B 2 22  ? 55.302  7.994   7.731   1.00 11.83 ? 23   PRO B C   1 
ATOM   2200 O  O   . PRO B 2 22  ? 55.702  6.846   7.380   1.00 13.46 ? 23   PRO B O   1 
ATOM   2201 C  CB  . PRO B 2 22  ? 52.802  8.483   7.544   1.00 13.77 ? 23   PRO B CB  1 
ATOM   2202 C  CG  . PRO B 2 22  ? 51.803  9.200   8.529   1.00 12.84 ? 23   PRO B CG  1 
ATOM   2203 C  CD  . PRO B 2 22  ? 52.798  10.070  9.371   1.00 11.07 ? 23   PRO B CD  1 
ATOM   2204 N  N   . ALA B 2 23  ? 55.962  9.121   7.482   1.00 11.74 ? 24   ALA B N   1 
ATOM   2205 C  CA  . ALA B 2 23  ? 57.270  9.110   6.807   1.00 12.61 ? 24   ALA B CA  1 
ATOM   2206 C  C   . ALA B 2 23  ? 58.276  8.311   7.686   1.00 12.15 ? 24   ALA B C   1 
ATOM   2207 O  O   . ALA B 2 23  ? 59.058  7.502   7.160   1.00 11.59 ? 24   ALA B O   1 
ATOM   2208 C  CB  . ALA B 2 23  ? 57.782  10.525  6.582   1.00 11.84 ? 24   ALA B CB  1 
ATOM   2209 N  N   . LEU B 2 24  ? 58.271  8.555   9.002   1.00 11.76 ? 25   LEU B N   1 
ATOM   2210 C  CA  . LEU B 2 24  ? 59.208  7.767   9.822   1.00 10.10 ? 25   LEU B CA  1 
ATOM   2211 C  C   . LEU B 2 24  ? 58.859  6.284   9.864   1.00 11.48 ? 25   LEU B C   1 
ATOM   2212 O  O   . LEU B 2 24  ? 59.755  5.447   9.839   1.00 11.16 ? 25   LEU B O   1 
ATOM   2213 C  CB  . LEU B 2 24  ? 59.220  8.342   11.242  1.00 10.89 ? 25   LEU B CB  1 
ATOM   2214 C  CG  . LEU B 2 24  ? 59.704  9.789   11.393  1.00 10.69 ? 25   LEU B CG  1 
ATOM   2215 C  CD1 . LEU B 2 24  ? 59.569  10.132  12.880  1.00 11.29 ? 25   LEU B CD1 1 
ATOM   2216 C  CD2 . LEU B 2 24  ? 61.166  9.922   10.950  1.00 11.13 ? 25   LEU B CD2 1 
ATOM   2217 N  N   . ASN B 2 25  ? 57.563  5.959   9.906   1.00 10.31 ? 26   ASN B N   1 
ATOM   2218 C  CA  . ASN B 2 25  ? 57.179  4.528   9.957   1.00 11.67 ? 26   ASN B CA  1 
ATOM   2219 C  C   . ASN B 2 25  ? 57.550  3.859   8.620   1.00 11.09 ? 26   ASN B C   1 
ATOM   2220 O  O   . ASN B 2 25  ? 58.020  2.719   8.623   1.00 12.26 ? 26   ASN B O   1 
ATOM   2221 C  CB  . ASN B 2 25  ? 55.671  4.420   10.225  1.00 14.23 ? 26   ASN B CB  1 
ATOM   2222 C  CG  . ASN B 2 25  ? 55.286  4.791   11.667  1.00 18.93 ? 26   ASN B CG  1 
ATOM   2223 O  OD1 . ASN B 2 25  ? 54.181  5.320   11.904  1.00 24.01 ? 26   ASN B OD1 1 
ATOM   2224 N  ND2 . ASN B 2 25  ? 56.122  4.467   12.612  1.00 21.96 ? 26   ASN B ND2 1 
ATOM   2225 N  N   . GLN B 2 26  ? 57.338  4.568   7.525   1.00 10.83 ? 27   GLN B N   1 
ATOM   2226 C  CA  . GLN B 2 26  ? 57.680  4.035   6.199   1.00 11.32 ? 27   GLN B CA  1 
ATOM   2227 C  C   . GLN B 2 26  ? 59.194  3.781   6.134   1.00 11.39 ? 27   GLN B C   1 
ATOM   2228 O  O   . GLN B 2 26  ? 59.638  2.710   5.666   1.00 12.90 ? 27   GLN B O   1 
ATOM   2229 C  CB  . GLN B 2 26  ? 57.284  5.013   5.117   1.00 12.73 ? 27   GLN B CB  1 
ATOM   2230 C  CG  . GLN B 2 26  ? 57.811  4.561   3.708   1.00 13.36 ? 27   GLN B CG  1 
ATOM   2231 C  CD  . GLN B 2 26  ? 57.649  5.600   2.640   1.00 15.12 ? 27   GLN B CD  1 
ATOM   2232 O  OE1 . GLN B 2 26  ? 57.925  6.781   2.807   1.00 17.30 ? 27   GLN B OE1 1 
ATOM   2233 N  NE2 . GLN B 2 26  ? 57.196  5.139   1.447   1.00 18.64 ? 27   GLN B NE2 1 
ATOM   2234 N  N   . LEU B 2 27  ? 59.967  4.740   6.588   1.00 10.36 ? 28   LEU B N   1 
ATOM   2235 C  CA  . LEU B 2 27  ? 61.428  4.592   6.595   1.00 10.02 ? 28   LEU B CA  1 
ATOM   2236 C  C   . LEU B 2 27  ? 61.885  3.395   7.456   1.00 9.78  ? 28   LEU B C   1 
ATOM   2237 O  O   . LEU B 2 27  ? 62.779  2.624   7.052   1.00 10.49 ? 28   LEU B O   1 
ATOM   2238 C  CB  . LEU B 2 27  ? 62.060  5.908   7.095   1.00 10.01 ? 28   LEU B CB  1 
ATOM   2239 C  CG  . LEU B 2 27  ? 63.589  5.866   7.209   1.00 9.85  ? 28   LEU B CG  1 
ATOM   2240 C  CD1 . LEU B 2 27  ? 64.245  5.619   5.795   1.00 11.43 ? 28   LEU B CD1 1 
ATOM   2241 C  CD2 . LEU B 2 27  ? 64.024  7.232   7.795   1.00 11.36 ? 28   LEU B CD2 1 
ATOM   2242 N  N   . GLU B 2 28  ? 61.332  3.250   8.656   1.00 9.90  ? 29   GLU B N   1 
ATOM   2243 C  CA  . GLU B 2 28  ? 61.676  2.137   9.493   1.00 9.78  ? 29   GLU B CA  1 
ATOM   2244 C  C   . GLU B 2 28  ? 61.375  0.817   8.807   1.00 11.58 ? 29   GLU B C   1 
ATOM   2245 O  O   . GLU B 2 28  ? 62.229  -0.053  8.822   1.00 11.03 ? 29   GLU B O   1 
ATOM   2246 C  CB  . GLU B 2 28  ? 60.964  2.208   10.847  1.00 10.24 ? 29   GLU B CB  1 
ATOM   2247 C  CG  . GLU B 2 28  ? 61.429  1.113   11.786  1.00 10.84 ? 29   GLU B CG  1 
ATOM   2248 C  CD  . GLU B 2 28  ? 60.475  0.865   12.943  1.00 11.54 ? 29   GLU B CD  1 
ATOM   2249 O  OE1 . GLU B 2 28  ? 59.239  0.695   12.685  1.00 13.71 ? 29   GLU B OE1 1 
ATOM   2250 O  OE2 . GLU B 2 28  ? 60.928  0.787   14.100  1.00 12.61 ? 29   GLU B OE2 1 
ATOM   2251 N  N   . GLU B 2 29  ? 60.168  0.691   8.250   1.00 12.27 ? 30   GLU B N   1 
ATOM   2252 C  CA  . GLU B 2 29  ? 59.811  -0.556  7.566   1.00 14.06 ? 30   GLU B CA  1 
ATOM   2253 C  C   . GLU B 2 29  ? 60.750  -0.835  6.394   1.00 13.27 ? 30   GLU B C   1 
ATOM   2254 O  O   . GLU B 2 29  ? 61.175  -1.988  6.212   1.00 14.09 ? 30   GLU B O   1 
ATOM   2255 C  CB  . GLU B 2 29  ? 58.357  -0.456  7.063   1.00 16.68 ? 30   GLU B CB  1 
ATOM   2256 C  CG  . GLU B 2 29  ? 57.764  -1.863  6.719   1.00 26.12 ? 30   GLU B CG  1 
ATOM   2257 C  CD  . GLU B 2 29  ? 56.302  -1.804  6.278   1.00 31.48 ? 30   GLU B CD  1 
ATOM   2258 O  OE1 . GLU B 2 29  ? 55.440  -1.324  7.060   1.00 36.80 ? 30   GLU B OE1 1 
ATOM   2259 O  OE2 . GLU B 2 29  ? 56.005  -2.245  5.141   1.00 37.99 ? 30   GLU B OE2 1 
ATOM   2260 N  N   . ALA B 2 30  ? 61.106  0.190   5.620   1.00 13.28 ? 31   ALA B N   1 
ATOM   2261 C  CA  . ALA B 2 30  ? 61.985  -0.024  4.447   1.00 12.55 ? 31   ALA B CA  1 
ATOM   2262 C  C   . ALA B 2 30  ? 63.377  -0.461  4.925   1.00 12.25 ? 31   ALA B C   1 
ATOM   2263 O  O   . ALA B 2 30  ? 64.060  -1.281  4.316   1.00 12.33 ? 31   ALA B O   1 
ATOM   2264 C  CB  . ALA B 2 30  ? 62.071  1.266   3.622   1.00 13.93 ? 31   ALA B CB  1 
ATOM   2265 N  N   . PHE B 2 31  ? 63.838  0.135   6.032   1.00 12.02 ? 32   PHE B N   1 
ATOM   2266 C  CA  . PHE B 2 31  ? 65.141  -0.210  6.581   1.00 11.45 ? 32   PHE B CA  1 
ATOM   2267 C  C   . PHE B 2 31  ? 65.170  -1.662  7.053   1.00 11.86 ? 32   PHE B C   1 
ATOM   2268 O  O   . PHE B 2 31  ? 66.116  -2.396  6.762   1.00 12.30 ? 32   PHE B O   1 
ATOM   2269 C  CB  . PHE B 2 31  ? 65.484  0.721   7.750   1.00 11.44 ? 32   PHE B CB  1 
ATOM   2270 C  CG  . PHE B 2 31  ? 66.706  0.305   8.516   1.00 9.90  ? 32   PHE B CG  1 
ATOM   2271 C  CD1 . PHE B 2 31  ? 67.974  0.402   7.945   1.00 10.90 ? 32   PHE B CD1 1 
ATOM   2272 C  CD2 . PHE B 2 31  ? 66.589  -0.197  9.808   1.00 11.29 ? 32   PHE B CD2 1 
ATOM   2273 C  CE1 . PHE B 2 31  ? 69.106  0.006   8.653   1.00 11.36 ? 32   PHE B CE1 1 
ATOM   2274 C  CE2 . PHE B 2 31  ? 67.710  -0.597  10.524  1.00 12.69 ? 32   PHE B CE2 1 
ATOM   2275 C  CZ  . PHE B 2 31  ? 68.974  -0.495  9.946   1.00 11.14 ? 32   PHE B CZ  1 
ATOM   2276 N  N   . VAL B 2 32  ? 64.116  -2.080  7.770   1.00 11.39 ? 33   VAL B N   1 
ATOM   2277 C  CA  . VAL B 2 32  ? 64.061  -3.461  8.283   1.00 11.28 ? 33   VAL B CA  1 
ATOM   2278 C  C   . VAL B 2 32  ? 64.048  -4.425  7.118   1.00 12.59 ? 33   VAL B C   1 
ATOM   2279 O  O   . VAL B 2 32  ? 64.753  -5.443  7.144   1.00 13.44 ? 33   VAL B O   1 
ATOM   2280 C  CB  . VAL B 2 32  ? 62.825  -3.638  9.199   1.00 11.33 ? 33   VAL B CB  1 
ATOM   2281 C  CG1 . VAL B 2 32  ? 62.626  -5.142  9.547   1.00 14.27 ? 33   VAL B CG1 1 
ATOM   2282 C  CG2 . VAL B 2 32  ? 63.090  -2.950  10.541  1.00 13.85 ? 33   VAL B CG2 1 
ATOM   2283 N  N   . SER B 2 33  ? 63.288  -4.073  6.107   1.00 11.95 ? 34   SER B N   1 
ATOM   2284 C  CA  . SER B 2 33  ? 63.246  -4.908  4.877   1.00 13.41 ? 34   SER B CA  1 
ATOM   2285 C  C   . SER B 2 33  ? 64.604  -4.970  4.177   1.00 14.75 ? 34   SER B C   1 
ATOM   2286 O  O   . SER B 2 33  ? 65.112  -6.070  3.838   1.00 13.56 ? 34   SER B O   1 
ATOM   2287 C  CB  . SER B 2 33  ? 62.192  -4.331  3.934   1.00 14.05 ? 34   SER B CB  1 
ATOM   2288 O  OG  . SER B 2 33  ? 62.111  -5.130  2.725   1.00 16.06 ? 34   SER B OG  1 
ATOM   2289 N  N   . ALA B 2 34  ? 65.221  -3.804  3.978   1.00 11.86 ? 35   ALA B N   1 
ATOM   2290 C  CA  . ALA B 2 34  ? 66.520  -3.753  3.308   1.00 11.78 ? 35   ALA B CA  1 
ATOM   2291 C  C   . ALA B 2 34  ? 67.590  -4.565  4.068   1.00 12.13 ? 35   ALA B C   1 
ATOM   2292 O  O   . ALA B 2 34  ? 68.455  -5.208  3.435   1.00 13.40 ? 35   ALA B O   1 
ATOM   2293 C  CB  . ALA B 2 34  ? 66.967  -2.263  3.179   1.00 10.78 ? 35   ALA B CB  1 
ATOM   2294 N  N   . GLN B 2 35  ? 67.584  -4.521  5.406   1.00 12.44 ? 36   GLN B N   1 
ATOM   2295 C  CA  . GLN B 2 35  ? 68.597  -5.241  6.168   1.00 14.34 ? 36   GLN B CA  1 
ATOM   2296 C  C   . GLN B 2 35  ? 68.524  -6.769  6.018   1.00 16.25 ? 36   GLN B C   1 
ATOM   2297 O  O   . GLN B 2 35  ? 69.530  -7.453  6.284   1.00 19.45 ? 36   GLN B O   1 
ATOM   2298 C  CB  . GLN B 2 35  ? 68.514  -4.825  7.649   1.00 15.34 ? 36   GLN B CB  1 
ATOM   2299 C  CG  . GLN B 2 35  ? 68.939  -3.345  7.804   1.00 18.06 ? 36   GLN B CG  1 
ATOM   2300 C  CD  . GLN B 2 35  ? 70.426  -3.141  7.551   1.00 19.63 ? 36   GLN B CD  1 
ATOM   2301 O  OE1 . GLN B 2 35  ? 71.259  -3.287  8.480   1.00 24.67 ? 36   GLN B OE1 1 
ATOM   2302 N  NE2 . GLN B 2 35  ? 70.772  -2.820  6.319   1.00 21.31 ? 36   GLN B NE2 1 
ATOM   2303 N  N   . LYS B 2 36  ? 67.370  -7.267  5.553   1.00 16.52 ? 37   LYS B N   1 
ATOM   2304 C  CA  . LYS B 2 36  ? 67.178  -8.719  5.332   1.00 18.63 ? 37   LYS B CA  1 
ATOM   2305 C  C   . LYS B 2 36  ? 67.312  -9.046  3.844   1.00 18.39 ? 37   LYS B C   1 
ATOM   2306 O  O   . LYS B 2 36  ? 67.221  -10.231 3.432   1.00 20.49 ? 37   LYS B O   1 
ATOM   2307 C  CB  . LYS B 2 36  ? 65.755  -9.163  5.738   1.00 21.82 ? 37   LYS B CB  1 
ATOM   2308 C  CG  . LYS B 2 36  ? 65.357  -8.889  7.138   1.00 26.62 ? 37   LYS B CG  1 
ATOM   2309 C  CD  . LYS B 2 36  ? 66.152  -9.694  8.133   1.00 31.92 ? 37   LYS B CD  1 
ATOM   2310 C  CE  . LYS B 2 36  ? 65.455  -11.025 8.515   1.00 34.39 ? 37   LYS B CE  1 
ATOM   2311 N  NZ  . LYS B 2 36  ? 66.166  -11.790 9.601   1.00 35.18 ? 37   LYS B NZ  1 
ATOM   2312 N  N   . ASP B 2 37  ? 67.515  -8.056  3.015   1.00 15.29 ? 38   ASP B N   1 
ATOM   2313 C  CA  . ASP B 2 37  ? 67.534  -8.270  1.569   1.00 14.67 ? 38   ASP B CA  1 
ATOM   2314 C  C   . ASP B 2 37  ? 68.963  -8.462  1.059   1.00 16.46 ? 38   ASP B C   1 
ATOM   2315 O  O   . ASP B 2 37  ? 69.722  -7.515  0.991   1.00 15.27 ? 38   ASP B O   1 
ATOM   2316 C  CB  . ASP B 2 37  ? 66.856  -7.063  0.922   1.00 14.89 ? 38   ASP B CB  1 
ATOM   2317 C  CG  . ASP B 2 37  ? 66.740  -7.151  -0.607  1.00 16.33 ? 38   ASP B CG  1 
ATOM   2318 O  OD1 . ASP B 2 37  ? 67.304  -8.066  -1.208  1.00 18.75 ? 38   ASP B OD1 1 
ATOM   2319 O  OD2 . ASP B 2 37  ? 66.086  -6.286  -1.218  1.00 20.51 ? 38   ASP B OD2 1 
ATOM   2320 N  N   . PRO B 2 38  ? 69.351  -9.683  0.656   1.00 17.37 ? 39   PRO B N   1 
ATOM   2321 C  CA  . PRO B 2 38  ? 70.742  -9.846  0.179   1.00 17.28 ? 39   PRO B CA  1 
ATOM   2322 C  C   . PRO B 2 38  ? 71.098  -8.995  -1.030  1.00 17.02 ? 39   PRO B C   1 
ATOM   2323 O  O   . PRO B 2 38  ? 72.291  -8.656  -1.250  1.00 16.78 ? 39   PRO B O   1 
ATOM   2324 C  CB  . PRO B 2 38  ? 70.859  -11.360 -0.153  1.00 19.00 ? 39   PRO B CB  1 
ATOM   2325 C  CG  . PRO B 2 38  ? 69.612  -11.963 0.395   1.00 21.39 ? 39   PRO B CG  1 
ATOM   2326 C  CD  . PRO B 2 38  ? 68.551  -10.924 0.491   1.00 19.95 ? 39   PRO B CD  1 
ATOM   2327 N  N   . GLU B 2 39  ? 70.127  -8.621  -1.830  1.00 15.64 ? 40   GLU B N   1 
ATOM   2328 C  CA  . GLU B 2 39  ? 70.388  -7.800  -2.990  1.00 17.61 ? 40   GLU B CA  1 
ATOM   2329 C  C   . GLU B 2 39  ? 70.738  -6.369  -2.588  1.00 17.66 ? 40   GLU B C   1 
ATOM   2330 O  O   . GLU B 2 39  ? 71.598  -5.725  -3.206  1.00 16.82 ? 40   GLU B O   1 
ATOM   2331 C  CB  . GLU B 2 39  ? 69.198  -7.804  -3.930  1.00 21.45 ? 40   GLU B CB  1 
ATOM   2332 C  CG  . GLU B 2 39  ? 69.351  -6.981  -5.133  1.00 28.78 ? 40   GLU B CG  1 
ATOM   2333 C  CD  . GLU B 2 39  ? 68.503  -7.523  -6.274  1.00 34.60 ? 40   GLU B CD  1 
ATOM   2334 O  OE1 . GLU B 2 39  ? 67.442  -8.164  -5.963  1.00 37.00 ? 40   GLU B OE1 1 
ATOM   2335 O  OE2 . GLU B 2 39  ? 68.903  -7.305  -7.463  1.00 36.98 ? 40   GLU B OE2 1 
ATOM   2336 N  N   . PHE B 2 40  ? 70.073  -5.879  -1.558  1.00 15.53 ? 41   PHE B N   1 
ATOM   2337 C  CA  . PHE B 2 40  ? 70.350  -4.533  -1.071  1.00 14.22 ? 41   PHE B CA  1 
ATOM   2338 C  C   . PHE B 2 40  ? 71.745  -4.538  -0.455  1.00 13.80 ? 41   PHE B C   1 
ATOM   2339 O  O   . PHE B 2 40  ? 72.556  -3.644  -0.711  1.00 12.61 ? 41   PHE B O   1 
ATOM   2340 C  CB  . PHE B 2 40  ? 69.304  -4.118  -0.027  1.00 14.28 ? 41   PHE B CB  1 
ATOM   2341 C  CG  . PHE B 2 40  ? 69.517  -2.735  0.535   1.00 14.86 ? 41   PHE B CG  1 
ATOM   2342 C  CD1 . PHE B 2 40  ? 70.448  -2.512  1.544   1.00 14.96 ? 41   PHE B CD1 1 
ATOM   2343 C  CD2 . PHE B 2 40  ? 68.791  -1.654  0.044   1.00 15.16 ? 41   PHE B CD2 1 
ATOM   2344 C  CE1 . PHE B 2 40  ? 70.657  -1.226  2.060   1.00 15.27 ? 41   PHE B CE1 1 
ATOM   2345 C  CE2 . PHE B 2 40  ? 68.989  -0.369  0.549   1.00 15.88 ? 41   PHE B CE2 1 
ATOM   2346 C  CZ  . PHE B 2 40  ? 69.925  -0.155  1.560   1.00 15.53 ? 41   PHE B CZ  1 
ATOM   2347 N  N   . GLN B 2 41  ? 72.012  -5.576  0.331   1.00 13.14 ? 42   GLN B N   1 
ATOM   2348 C  CA  . GLN B 2 41  ? 73.302  -5.692  0.975   1.00 12.09 ? 42   GLN B CA  1 
ATOM   2349 C  C   . GLN B 2 41  ? 74.426  -5.783  -0.053  1.00 14.05 ? 42   GLN B C   1 
ATOM   2350 O  O   . GLN B 2 41  ? 75.495  -5.166  0.129   1.00 14.11 ? 42   GLN B O   1 
ATOM   2351 C  CB  . GLN B 2 41  ? 73.363  -6.903  1.923   1.00 13.71 ? 42   GLN B CB  1 
ATOM   2352 C  CG  . GLN B 2 41  ? 72.367  -6.773  3.112   1.00 16.61 ? 42   GLN B CG  1 
ATOM   2353 C  CD  . GLN B 2 41  ? 72.484  -5.403  3.879   1.00 17.48 ? 42   GLN B CD  1 
ATOM   2354 O  OE1 . GLN B 2 41  ? 73.586  -4.947  4.203   1.00 18.41 ? 42   GLN B OE1 1 
ATOM   2355 N  NE2 . GLN B 2 41  ? 71.352  -4.768  4.149   1.00 19.38 ? 42   GLN B NE2 1 
ATOM   2356 N  N   . ALA B 2 42  ? 74.199  -6.511  -1.137  1.00 13.41 ? 43   ALA B N   1 
ATOM   2357 C  CA  . ALA B 2 42  ? 75.253  -6.633  -2.136  1.00 12.59 ? 43   ALA B CA  1 
ATOM   2358 C  C   . ALA B 2 42  ? 75.456  -5.316  -2.895  1.00 13.04 ? 43   ALA B C   1 
ATOM   2359 O  O   . ALA B 2 42  ? 76.610  -4.940  -3.235  1.00 13.91 ? 43   ALA B O   1 
ATOM   2360 C  CB  . ALA B 2 42  ? 74.873  -7.776  -3.126  1.00 15.80 ? 43   ALA B CB  1 
ATOM   2361 N  N   . GLN B 2 43  ? 74.393  -4.580  -3.181  1.00 12.89 ? 44   GLN B N   1 
ATOM   2362 C  CA  . GLN B 2 43  ? 74.539  -3.310  -3.868  1.00 11.98 ? 44   GLN B CA  1 
ATOM   2363 C  C   . GLN B 2 43  ? 75.296  -2.293  -2.966  1.00 11.65 ? 44   GLN B C   1 
ATOM   2364 O  O   . GLN B 2 43  ? 76.160  -1.562  -3.419  1.00 11.16 ? 44   GLN B O   1 
ATOM   2365 C  CB  . GLN B 2 43  ? 73.185  -2.699  -4.252  1.00 15.54 ? 44   GLN B CB  1 
ATOM   2366 C  CG  . GLN B 2 43  ? 73.337  -1.340  -4.898  1.00 20.29 ? 44   GLN B CG  1 
ATOM   2367 C  CD  . GLN B 2 43  ? 72.112  -0.889  -5.727  1.00 25.32 ? 44   GLN B CD  1 
ATOM   2368 O  OE1 . GLN B 2 43  ? 71.003  -1.357  -5.497  1.00 26.74 ? 44   GLN B OE1 1 
ATOM   2369 N  NE2 . GLN B 2 43  ? 72.333  0.025   -6.692  1.00 27.14 ? 44   GLN B NE2 1 
ATOM   2370 N  N   . PHE B 2 44  ? 74.941  -2.276  -1.693  1.00 10.51 ? 45   PHE B N   1 
ATOM   2371 C  CA  . PHE B 2 44  ? 75.574  -1.369  -0.742  1.00 10.50 ? 45   PHE B CA  1 
ATOM   2372 C  C   . PHE B 2 44  ? 77.059  -1.735  -0.632  1.00 9.00  ? 45   PHE B C   1 
ATOM   2373 O  O   . PHE B 2 44  ? 77.931  -0.866  -0.697  1.00 9.03  ? 45   PHE B O   1 
ATOM   2374 C  CB  . PHE B 2 44  ? 74.848  -1.485  0.608   1.00 9.49  ? 45   PHE B CB  1 
ATOM   2375 C  CG  . PHE B 2 44  ? 75.289  -0.486  1.653   1.00 10.58 ? 45   PHE B CG  1 
ATOM   2376 C  CD1 . PHE B 2 44  ? 75.824  0.749   1.303   1.00 10.14 ? 45   PHE B CD1 1 
ATOM   2377 C  CD2 . PHE B 2 44  ? 75.116  -0.781  3.004   1.00 10.88 ? 45   PHE B CD2 1 
ATOM   2378 C  CE1 . PHE B 2 44  ? 76.184  1.677   2.288   1.00 10.52 ? 45   PHE B CE1 1 
ATOM   2379 C  CE2 . PHE B 2 44  ? 75.470  0.136   3.995   1.00 12.12 ? 45   PHE B CE2 1 
ATOM   2380 C  CZ  . PHE B 2 44  ? 76.005  1.367   3.636   1.00 10.28 ? 45   PHE B CZ  1 
ATOM   2381 N  N   . ALA B 2 45  ? 77.353  -3.026  -0.490  1.00 9.53  ? 46   ALA B N   1 
ATOM   2382 C  CA  . ALA B 2 45  ? 78.755  -3.452  -0.381  1.00 8.92  ? 46   ALA B CA  1 
ATOM   2383 C  C   . ALA B 2 45  ? 79.525  -3.097  -1.632  1.00 9.30  ? 46   ALA B C   1 
ATOM   2384 O  O   . ALA B 2 45  ? 80.724  -2.737  -1.545  1.00 10.97 ? 46   ALA B O   1 
ATOM   2385 C  CB  . ALA B 2 45  ? 78.820  -4.963  -0.128  1.00 11.47 ? 46   ALA B CB  1 
ATOM   2386 N  N   . ASP B 2 46  ? 78.912  -3.259  -2.807  1.00 10.38 ? 47   ASP B N   1 
ATOM   2387 C  CA  . ASP B 2 46  ? 79.611  -2.919  -4.045  1.00 11.30 ? 47   ASP B CA  1 
ATOM   2388 C  C   . ASP B 2 46  ? 79.959  -1.431  -4.105  1.00 10.30 ? 47   ASP B C   1 
ATOM   2389 O  O   . ASP B 2 46  ? 81.070  -1.078  -4.483  1.00 11.01 ? 47   ASP B O   1 
ATOM   2390 C  CB  . ASP B 2 46  ? 78.767  -3.348  -5.261  1.00 14.36 ? 47   ASP B CB  1 
ATOM   2391 C  CG  . ASP B 2 46  ? 79.432  -2.953  -6.562  1.00 21.98 ? 47   ASP B CG  1 
ATOM   2392 O  OD1 . ASP B 2 46  ? 78.930  -2.049  -7.254  1.00 27.65 ? 47   ASP B OD1 1 
ATOM   2393 O  OD2 . ASP B 2 46  ? 80.493  -3.543  -6.838  1.00 25.82 ? 47   ASP B OD2 1 
ATOM   2394 N  N   . LEU B 2 47  ? 79.042  -0.564  -3.692  1.00 9.39  ? 48   LEU B N   1 
ATOM   2395 C  CA  . LEU B 2 47  ? 79.345  0.879   -3.707  1.00 8.27  ? 48   LEU B CA  1 
ATOM   2396 C  C   . LEU B 2 47  ? 80.455  1.181   -2.676  1.00 9.49  ? 48   LEU B C   1 
ATOM   2397 O  O   . LEU B 2 47  ? 81.414  1.931   -2.946  1.00 9.52  ? 48   LEU B O   1 
ATOM   2398 C  CB  . LEU B 2 47  ? 78.097  1.702   -3.321  1.00 11.58 ? 48   LEU B CB  1 
ATOM   2399 C  CG  . LEU B 2 47  ? 76.982  1.579   -4.368  1.00 12.94 ? 48   LEU B CG  1 
ATOM   2400 C  CD1 . LEU B 2 47  ? 75.800  2.407   -3.918  1.00 15.70 ? 48   LEU B CD1 1 
ATOM   2401 C  CD2 . LEU B 2 47  ? 77.506  2.052   -5.715  1.00 19.05 ? 48   LEU B CD2 1 
ATOM   2402 N  N   . LEU B 2 48  ? 80.349  0.561   -1.491  1.00 8.15  ? 49   LEU B N   1 
ATOM   2403 C  CA  . LEU B 2 48  ? 81.372  0.860   -0.488  1.00 8.94  ? 49   LEU B CA  1 
ATOM   2404 C  C   . LEU B 2 48  ? 82.747  0.438   -0.961  1.00 8.58  ? 49   LEU B C   1 
ATOM   2405 O  O   . LEU B 2 48  ? 83.711  1.184   -0.738  1.00 8.76  ? 49   LEU B O   1 
ATOM   2406 C  CB  . LEU B 2 48  ? 81.016  0.139   0.834   1.00 8.19  ? 49   LEU B CB  1 
ATOM   2407 C  CG  . LEU B 2 48  ? 79.765  0.678   1.520   1.00 8.08  ? 49   LEU B CG  1 
ATOM   2408 C  CD1 . LEU B 2 48  ? 79.319  -0.310  2.621   1.00 10.74 ? 49   LEU B CD1 1 
ATOM   2409 C  CD2 . LEU B 2 48  ? 80.040  2.085   2.060   1.00 10.91 ? 49   LEU B CD2 1 
ATOM   2410 N  N   . LYS B 2 49  ? 82.832  -0.731  -1.614  1.00 8.28  ? 50   LYS B N   1 
ATOM   2411 C  CA  . LYS B 2 49  ? 84.138  -1.205  -2.035  1.00 8.31  ? 50   LYS B CA  1 
ATOM   2412 C  C   . LYS B 2 49  ? 84.677  -0.492  -3.275  1.00 9.19  ? 50   LYS B C   1 
ATOM   2413 O  O   . LYS B 2 49  ? 85.841  0.018   -3.284  1.00 10.28 ? 50   LYS B O   1 
ATOM   2414 C  CB  . LYS B 2 49  ? 84.043  -2.729  -2.344  1.00 9.42  ? 50   LYS B CB  1 
ATOM   2415 C  CG  . LYS B 2 49  ? 85.390  -3.340  -2.866  1.00 16.67 ? 50   LYS B CG  1 
ATOM   2416 C  CD  . LYS B 2 49  ? 85.261  -4.864  -3.026  1.00 22.57 ? 50   LYS B CD  1 
ATOM   2417 C  CE  . LYS B 2 49  ? 86.501  -5.462  -3.696  1.00 25.51 ? 50   LYS B CE  1 
ATOM   2418 N  NZ  . LYS B 2 49  ? 86.540  -5.184  -5.184  1.00 30.66 ? 50   LYS B NZ  1 
ATOM   2419 N  N   . ASN B 2 50  ? 83.863  -0.462  -4.340  1.00 9.04  ? 51   ASN B N   1 
ATOM   2420 C  CA  . ASN B 2 50  ? 84.376  -0.017  -5.634  1.00 8.83  ? 51   ASN B CA  1 
ATOM   2421 C  C   . ASN B 2 50  ? 84.210  1.432   -5.944  1.00 9.89  ? 51   ASN B C   1 
ATOM   2422 O  O   . ASN B 2 50  ? 84.842  1.896   -6.892  1.00 10.86 ? 51   ASN B O   1 
ATOM   2423 C  CB  . ASN B 2 50  ? 83.730  -0.892  -6.708  1.00 9.82  ? 51   ASN B CB  1 
ATOM   2424 C  CG  . ASN B 2 50  ? 84.062  -2.346  -6.505  1.00 10.76 ? 51   ASN B CG  1 
ATOM   2425 O  OD1 . ASN B 2 50  ? 85.228  -2.699  -6.380  1.00 13.81 ? 51   ASN B OD1 1 
ATOM   2426 N  ND2 . ASN B 2 50  ? 83.022  -3.214  -6.405  1.00 13.56 ? 51   ASN B ND2 1 
ATOM   2427 N  N   . TYR B 2 51  ? 83.396  2.124   -5.134  1.00 9.03  ? 52   TYR B N   1 
ATOM   2428 C  CA  . TYR B 2 51  ? 83.190  3.553   -5.327  1.00 8.39  ? 52   TYR B CA  1 
ATOM   2429 C  C   . TYR B 2 51  ? 83.813  4.345   -4.178  1.00 8.68  ? 52   TYR B C   1 
ATOM   2430 O  O   . TYR B 2 51  ? 84.555  5.302   -4.406  1.00 9.43  ? 52   TYR B O   1 
ATOM   2431 C  CB  . TYR B 2 51  ? 81.694  3.881   -5.424  1.00 8.20  ? 52   TYR B CB  1 
ATOM   2432 C  CG  . TYR B 2 51  ? 81.404  5.367   -5.547  1.00 7.97  ? 52   TYR B CG  1 
ATOM   2433 C  CD1 . TYR B 2 51  ? 81.651  6.055   -6.735  1.00 9.77  ? 52   TYR B CD1 1 
ATOM   2434 C  CD2 . TYR B 2 51  ? 80.896  6.084   -4.468  1.00 8.53  ? 52   TYR B CD2 1 
ATOM   2435 C  CE1 . TYR B 2 51  ? 81.398  7.428   -6.844  1.00 9.30  ? 52   TYR B CE1 1 
ATOM   2436 C  CE2 . TYR B 2 51  ? 80.640  7.455   -4.566  1.00 8.56  ? 52   TYR B CE2 1 
ATOM   2437 C  CZ  . TYR B 2 51  ? 80.894  8.117   -5.755  1.00 9.07  ? 52   TYR B CZ  1 
ATOM   2438 O  OH  . TYR B 2 51  ? 80.642  9.469   -5.848  1.00 10.85 ? 52   TYR B OH  1 
ATOM   2439 N  N   . ALA B 2 52  ? 83.532  3.910   -2.952  1.00 9.13  ? 53   ALA B N   1 
ATOM   2440 C  CA  . ALA B 2 52  ? 84.058  4.655   -1.807  1.00 8.32  ? 53   ALA B CA  1 
ATOM   2441 C  C   . ALA B 2 52  ? 85.468  4.259   -1.384  1.00 9.74  ? 53   ALA B C   1 
ATOM   2442 O  O   . ALA B 2 52  ? 86.116  5.050   -0.713  1.00 10.45 ? 53   ALA B O   1 
ATOM   2443 C  CB  . ALA B 2 52  ? 83.113  4.541   -0.605  1.00 8.93  ? 53   ALA B CB  1 
ATOM   2444 N  N   . GLY B 2 53  ? 85.884  3.030   -1.730  1.00 8.80  ? 54   GLY B N   1 
ATOM   2445 C  CA  . GLY B 2 53  ? 87.252  2.602   -1.408  1.00 9.98  ? 54   GLY B CA  1 
ATOM   2446 C  C   . GLY B 2 53  ? 87.394  1.781   -0.117  1.00 10.46 ? 54   GLY B C   1 
ATOM   2447 O  O   . GLY B 2 53  ? 88.506  1.675   0.421   1.00 13.27 ? 54   GLY B O   1 
ATOM   2448 N  N   . ARG B 2 54  ? 86.334  1.162   0.376   1.00 7.53  ? 55   ARG B N   1 
ATOM   2449 C  CA  . ARG B 2 54  ? 86.507  0.305   1.585   1.00 6.99  ? 55   ARG B CA  1 
ATOM   2450 C  C   . ARG B 2 54  ? 87.101  -1.053  1.158   1.00 8.32  ? 55   ARG B C   1 
ATOM   2451 O  O   . ARG B 2 54  ? 86.889  -1.524  0.008   1.00 8.93  ? 55   ARG B O   1 
ATOM   2452 C  CB  . ARG B 2 54  ? 85.148  0.028   2.190   1.00 7.83  ? 55   ARG B CB  1 
ATOM   2453 C  CG  . ARG B 2 54  ? 84.406  1.324   2.652   1.00 7.92  ? 55   ARG B CG  1 
ATOM   2454 C  CD  . ARG B 2 54  ? 83.513  1.143   3.908   1.00 7.44  ? 55   ARG B CD  1 
ATOM   2455 N  NE  . ARG B 2 54  ? 84.349  0.888   5.064   1.00 8.44  ? 55   ARG B NE  1 
ATOM   2456 C  CZ  . ARG B 2 54  ? 84.845  1.866   5.821   1.00 7.46  ? 55   ARG B CZ  1 
ATOM   2457 N  NH1 . ARG B 2 54  ? 84.528  3.142   5.559   1.00 7.91  ? 55   ARG B NH1 1 
ATOM   2458 N  NH2 . ARG B 2 54  ? 85.679  1.596   6.814   1.00 8.52  ? 55   ARG B NH2 1 
ATOM   2459 N  N   . PRO B 2 55  ? 87.775  -1.763  2.071   1.00 8.32  ? 56   PRO B N   1 
ATOM   2460 C  CA  . PRO B 2 55  ? 88.013  -1.361  3.467   1.00 8.49  ? 56   PRO B CA  1 
ATOM   2461 C  C   . PRO B 2 55  ? 89.090  -0.274  3.524   1.00 8.16  ? 56   PRO B C   1 
ATOM   2462 O  O   . PRO B 2 55  ? 89.975  -0.198  2.636   1.00 8.31  ? 56   PRO B O   1 
ATOM   2463 C  CB  . PRO B 2 55  ? 88.500  -2.662  4.145   1.00 8.40  ? 56   PRO B CB  1 
ATOM   2464 C  CG  . PRO B 2 55  ? 89.255  -3.343  2.998   1.00 10.93 ? 56   PRO B CG  1 
ATOM   2465 C  CD  . PRO B 2 55  ? 88.360  -3.091  1.796   1.00 9.63  ? 56   PRO B CD  1 
ATOM   2466 N  N   . THR B 2 56  ? 89.010  0.537   4.562   1.00 7.77  ? 57   THR B N   1 
ATOM   2467 C  CA  . THR B 2 56  ? 90.018  1.578   4.813   1.00 7.89  ? 57   THR B CA  1 
ATOM   2468 C  C   . THR B 2 56  ? 91.133  0.968   5.656   1.00 7.27  ? 57   THR B C   1 
ATOM   2469 O  O   . THR B 2 56  ? 90.919  0.027   6.415   1.00 8.36  ? 57   THR B O   1 
ATOM   2470 C  CB  . THR B 2 56  ? 89.430  2.797   5.524   1.00 7.27  ? 57   THR B CB  1 
ATOM   2471 O  OG1 . THR B 2 56  ? 88.868  2.400   6.774   1.00 8.20  ? 57   THR B OG1 1 
ATOM   2472 C  CG2 . THR B 2 56  ? 88.368  3.491   4.652   1.00 9.33  ? 57   THR B CG2 1 
ATOM   2473 N  N   . ALA B 2 57  ? 92.359  1.496   5.500   1.00 7.64  ? 58   ALA B N   1 
ATOM   2474 C  CA  . ALA B 2 57  ? 93.491  0.963   6.242   1.00 7.96  ? 58   ALA B CA  1 
ATOM   2475 C  C   . ALA B 2 57  ? 93.370  1.173   7.775   1.00 7.79  ? 58   ALA B C   1 
ATOM   2476 O  O   . ALA B 2 57  ? 92.608  2.035   8.263   1.00 6.71  ? 58   ALA B O   1 
ATOM   2477 C  CB  . ALA B 2 57  ? 94.748  1.679   5.747   1.00 9.84  ? 58   ALA B CB  1 
ATOM   2478 N  N   . LEU B 2 58  ? 94.168  0.401   8.491   1.00 8.01  ? 59   LEU B N   1 
ATOM   2479 C  CA  . LEU B 2 58  ? 94.341  0.550   9.952   1.00 7.39  ? 59   LEU B CA  1 
ATOM   2480 C  C   . LEU B 2 58  ? 95.859  0.769   10.050  1.00 8.18  ? 59   LEU B C   1 
ATOM   2481 O  O   . LEU B 2 58  ? 96.674  -0.168  9.834   1.00 11.51 ? 59   LEU B O   1 
ATOM   2482 C  CB  . LEU B 2 58  ? 93.864  -0.697  10.704  1.00 8.14  ? 59   LEU B CB  1 
ATOM   2483 C  CG  . LEU B 2 58  ? 93.978  -0.462  12.212  1.00 9.37  ? 59   LEU B CG  1 
ATOM   2484 C  CD1 . LEU B 2 58  ? 92.885  0.446   12.763  1.00 8.21  ? 59   LEU B CD1 1 
ATOM   2485 C  CD2 . LEU B 2 58  ? 93.841  -1.820  12.897  1.00 11.33 ? 59   LEU B CD2 1 
ATOM   2486 N  N   . THR B 2 59  ? 96.260  2.006   10.383  1.00 7.59  ? 60   THR B N   1 
ATOM   2487 C  CA  . THR B 2 59  ? 97.675  2.406   10.350  1.00 8.25  ? 60   THR B CA  1 
ATOM   2488 C  C   . THR B 2 59  ? 98.296  2.433   11.740  1.00 8.79  ? 60   THR B C   1 
ATOM   2489 O  O   . THR B 2 59  ? 97.801  3.141   12.617  1.00 9.19  ? 60   THR B O   1 
ATOM   2490 C  CB  . THR B 2 59  ? 97.746  3.810   9.779   1.00 9.09  ? 60   THR B CB  1 
ATOM   2491 O  OG1 . THR B 2 59  ? 97.188  3.827   8.469   1.00 9.10  ? 60   THR B OG1 1 
ATOM   2492 C  CG2 . THR B 2 59  ? 99.210  4.281   9.644   1.00 10.47 ? 60   THR B CG2 1 
ATOM   2493 N  N   . LYS B 2 60  ? 99.429  1.752   11.903  1.00 9.81  ? 61   LYS B N   1 
ATOM   2494 C  CA  . LYS B 2 60  ? 100.114 1.790   13.217  1.00 10.15 ? 61   LYS B CA  1 
ATOM   2495 C  C   . LYS B 2 60  ? 100.991 3.052   13.257  1.00 11.59 ? 61   LYS B C   1 
ATOM   2496 O  O   . LYS B 2 60  ? 101.710 3.345   12.285  1.00 14.30 ? 61   LYS B O   1 
ATOM   2497 C  CB  . LYS B 2 60  ? 100.988 0.531   13.408  1.00 11.44 ? 61   LYS B CB  1 
ATOM   2498 C  CG  . LYS B 2 60  ? 101.550 0.410   14.857  1.00 12.15 ? 61   LYS B CG  1 
ATOM   2499 C  CD  . LYS B 2 60  ? 102.434 -0.901  14.951  1.00 16.82 ? 61   LYS B CD  1 
ATOM   2500 C  CE  . LYS B 2 60  ? 103.022 -1.084  16.329  1.00 23.88 ? 61   LYS B CE  1 
ATOM   2501 N  NZ  . LYS B 2 60  ? 104.056 -2.171  16.468  1.00 28.01 ? 61   LYS B NZ  1 
ATOM   2502 N  N   . CYS B 2 61  ? 100.952 3.787   14.352  1.00 11.83 ? 62   CYS B N   1 
ATOM   2503 C  CA  . CYS B 2 61  ? 101.722 5.045   14.536  1.00 15.22 ? 62   CYS B CA  1 
ATOM   2504 C  C   . CYS B 2 61  ? 102.939 4.900   15.488  1.00 17.64 ? 62   CYS B C   1 
ATOM   2505 O  O   . CYS B 2 61  ? 102.988 5.470   16.626  1.00 19.26 ? 62   CYS B O   1 
ATOM   2506 C  CB  . CYS B 2 61  ? 100.813 6.109   15.138  1.00 18.76 ? 62   CYS B CB  1 
ATOM   2507 S  SG  . CYS B 2 61  ? 99.563  6.553   13.933  1.00 24.65 ? 62   CYS B SG  1 
ATOM   2508 N  N   . GLN B 2 62  ? 103.922 4.137   15.085  1.00 17.54 ? 63   GLN B N   1 
ATOM   2509 C  CA  . GLN B 2 62  ? 105.119 4.041   15.945  1.00 17.01 ? 63   GLN B CA  1 
ATOM   2510 C  C   . GLN B 2 62  ? 105.892 5.350   16.253  1.00 16.76 ? 63   GLN B C   1 
ATOM   2511 O  O   . GLN B 2 62  ? 106.408 5.461   17.394  1.00 18.05 ? 63   GLN B O   1 
ATOM   2512 C  CB  . GLN B 2 62  ? 106.097 3.004   15.359  1.00 19.66 ? 63   GLN B CB  1 
ATOM   2513 N  N   . ASN B 2 63  ? 105.990 6.338   15.329  1.00 11.94 ? 64   ASN B N   1 
ATOM   2514 C  CA  . ASN B 2 63  ? 106.765 7.531   15.711  1.00 11.55 ? 64   ASN B CA  1 
ATOM   2515 C  C   . ASN B 2 63  ? 106.104 8.263   16.899  1.00 12.48 ? 64   ASN B C   1 
ATOM   2516 O  O   . ASN B 2 63  ? 106.797 8.703   17.811  1.00 14.89 ? 64   ASN B O   1 
ATOM   2517 C  CB  . ASN B 2 63  ? 106.937 8.533   14.550  1.00 13.19 ? 64   ASN B CB  1 
ATOM   2518 C  CG  . ASN B 2 63  ? 107.727 7.970   13.406  1.00 14.07 ? 64   ASN B CG  1 
ATOM   2519 O  OD1 . ASN B 2 63  ? 107.555 8.405   12.238  1.00 15.54 ? 64   ASN B OD1 1 
ATOM   2520 N  ND2 . ASN B 2 63  ? 108.618 7.024   13.687  1.00 13.08 ? 64   ASN B ND2 1 
ATOM   2521 N  N   . ILE B 2 64  ? 104.784 8.357   16.920  1.00 11.85 ? 65   ILE B N   1 
ATOM   2522 C  CA  . ILE B 2 64  ? 104.090 9.081   17.983  1.00 12.83 ? 65   ILE B CA  1 
ATOM   2523 C  C   . ILE B 2 64  ? 104.254 8.425   19.346  1.00 11.55 ? 65   ILE B C   1 
ATOM   2524 O  O   . ILE B 2 64  ? 104.354 9.154   20.337  1.00 13.77 ? 65   ILE B O   1 
ATOM   2525 C  CB  . ILE B 2 64  ? 102.573 9.126   17.669  1.00 14.54 ? 65   ILE B CB  1 
ATOM   2526 C  CG1 . ILE B 2 64  ? 102.355 10.174  16.567  1.00 18.46 ? 65   ILE B CG1 1 
ATOM   2527 C  CG2 . ILE B 2 64  ? 101.750 9.441   18.975  1.00 15.98 ? 65   ILE B CG2 1 
ATOM   2528 C  CD1 . ILE B 2 64  ? 100.908 10.505  16.370  1.00 21.98 ? 65   ILE B CD1 1 
ATOM   2529 N  N   . THR B 2 65  ? 104.323 7.105   19.376  1.00 10.72 ? 66   THR B N   1 
ATOM   2530 C  CA  . THR B 2 65  ? 104.338 6.404   20.675  1.00 11.64 ? 66   THR B CA  1 
ATOM   2531 C  C   . THR B 2 65  ? 105.734 6.027   21.158  1.00 12.71 ? 66   THR B C   1 
ATOM   2532 O  O   . THR B 2 65  ? 105.886 5.389   22.223  1.00 12.39 ? 66   THR B O   1 
ATOM   2533 C  CB  . THR B 2 65  ? 103.505 5.133   20.603  1.00 10.47 ? 66   THR B CB  1 
ATOM   2534 O  OG1 . THR B 2 65  ? 104.030 4.270   19.585  1.00 13.58 ? 66   THR B OG1 1 
ATOM   2535 C  CG2 . THR B 2 65  ? 102.022 5.456   20.278  1.00 10.17 ? 66   THR B CG2 1 
ATOM   2536 N  N   . ALA B 2 66  ? 106.770 6.417   20.426  1.00 13.42 ? 67   ALA B N   1 
ATOM   2537 C  CA  . ALA B 2 66  ? 108.139 6.096   20.817  1.00 15.48 ? 67   ALA B CA  1 
ATOM   2538 C  C   . ALA B 2 66  ? 108.448 6.475   22.283  1.00 15.44 ? 67   ALA B C   1 
ATOM   2539 O  O   . ALA B 2 66  ? 108.112 7.545   22.738  1.00 17.05 ? 67   ALA B O   1 
ATOM   2540 C  CB  . ALA B 2 66  ? 109.102 6.849   19.861  1.00 17.36 ? 67   ALA B CB  1 
ATOM   2541 N  N   . GLY B 2 67  ? 109.036 5.527   23.003  1.00 17.52 ? 68   GLY B N   1 
ATOM   2542 C  CA  . GLY B 2 67  ? 109.404 5.805   24.386  1.00 17.83 ? 68   GLY B CA  1 
ATOM   2543 C  C   . GLY B 2 67  ? 108.313 5.528   25.394  1.00 17.57 ? 68   GLY B C   1 
ATOM   2544 O  O   . GLY B 2 67  ? 108.485 5.797   26.632  1.00 20.21 ? 68   GLY B O   1 
ATOM   2545 N  N   . THR B 2 68  ? 107.181 5.017   24.913  1.00 14.22 ? 69   THR B N   1 
ATOM   2546 C  CA  . THR B 2 68  ? 106.048 4.676   25.824  1.00 12.31 ? 69   THR B CA  1 
ATOM   2547 C  C   . THR B 2 68  ? 105.609 3.239   25.596  1.00 12.40 ? 69   THR B C   1 
ATOM   2548 O  O   . THR B 2 68  ? 106.109 2.569   24.698  1.00 13.72 ? 69   THR B O   1 
ATOM   2549 C  CB  . THR B 2 68  ? 104.784 5.592   25.607  1.00 11.47 ? 69   THR B CB  1 
ATOM   2550 O  OG1 . THR B 2 68  ? 104.090 5.147   24.424  1.00 9.97  ? 69   THR B OG1 1 
ATOM   2551 C  CG2 . THR B 2 68  ? 105.205 7.068   25.475  1.00 11.79 ? 69   THR B CG2 1 
ATOM   2552 N  N   . ARG B 2 69  ? 104.683 2.745   26.439  1.00 10.17 ? 70   ARG B N   1 
ATOM   2553 C  CA  . ARG B 2 69  ? 104.150 1.415   26.284  1.00 10.32 ? 70   ARG B CA  1 
ATOM   2554 C  C   . ARG B 2 69  ? 102.741 1.454   25.620  1.00 9.13  ? 70   ARG B C   1 
ATOM   2555 O  O   . ARG B 2 69  ? 102.030 0.458   25.670  1.00 10.57 ? 70   ARG B O   1 
ATOM   2556 C  CB  . ARG B 2 69  ? 104.091 0.708   27.654  1.00 13.37 ? 70   ARG B CB  1 
ATOM   2557 C  CG  . ARG B 2 69  ? 105.558 0.541   28.207  1.00 14.47 ? 70   ARG B CG  1 
ATOM   2558 C  CD  . ARG B 2 69  ? 105.593 -0.517  29.305  1.00 21.38 ? 70   ARG B CD  1 
ATOM   2559 N  NE  . ARG B 2 69  ? 105.298 -1.844  28.747  1.00 25.60 ? 70   ARG B NE  1 
ATOM   2560 C  CZ  . ARG B 2 69  ? 104.998 -2.928  29.470  1.00 28.76 ? 70   ARG B CZ  1 
ATOM   2561 N  NH1 . ARG B 2 69  ? 104.960 -2.870  30.796  1.00 29.32 ? 70   ARG B NH1 1 
ATOM   2562 N  NH2 . ARG B 2 69  ? 104.680 -4.074  28.860  1.00 30.35 ? 70   ARG B NH2 1 
ATOM   2563 N  N   . THR B 2 70  ? 102.437 2.567   24.924  1.00 9.52  ? 71   THR B N   1 
ATOM   2564 C  CA  . THR B 2 70  ? 101.193 2.672   24.165  1.00 8.90  ? 71   THR B CA  1 
ATOM   2565 C  C   . THR B 2 70  ? 101.473 2.196   22.701  1.00 8.94  ? 71   THR B C   1 
ATOM   2566 O  O   . THR B 2 70  ? 102.520 2.532   22.145  1.00 10.98 ? 71   THR B O   1 
ATOM   2567 C  CB  . THR B 2 70  ? 100.709 4.107   24.087  1.00 9.13  ? 71   THR B CB  1 
ATOM   2568 O  OG1 . THR B 2 70  ? 100.264 4.494   25.403  1.00 10.36 ? 71   THR B OG1 1 
ATOM   2569 C  CG2 . THR B 2 70  ? 99.468  4.231   23.189  1.00 9.47  ? 71   THR B CG2 1 
ATOM   2570 N  N   . THR B 2 71  ? 100.586 1.362   22.164  1.00 9.15  ? 72   THR B N   1 
ATOM   2571 C  CA  . THR B 2 71  ? 100.618 1.005   20.727  1.00 8.16  ? 72   THR B CA  1 
ATOM   2572 C  C   . THR B 2 71  ? 99.343  1.686   20.201  1.00 8.49  ? 72   THR B C   1 
ATOM   2573 O  O   . THR B 2 71  ? 98.240  1.423   20.734  1.00 10.19 ? 72   THR B O   1 
ATOM   2574 C  CB  . THR B 2 71  ? 100.552 -0.493  20.534  1.00 10.05 ? 72   THR B CB  1 
ATOM   2575 O  OG1 . THR B 2 71  ? 101.739 -1.073  21.107  1.00 12.93 ? 72   THR B OG1 1 
ATOM   2576 C  CG2 . THR B 2 71  ? 100.537 -0.818  19.012  1.00 10.47 ? 72   THR B CG2 1 
ATOM   2577 N  N   . LEU B 2 72  ? 99.501  2.565   19.198  1.00 8.41  ? 73   LEU B N   1 
ATOM   2578 C  CA  . LEU B 2 72  ? 98.380  3.330   18.643  1.00 8.41  ? 73   LEU B CA  1 
ATOM   2579 C  C   . LEU B 2 72  ? 98.136  3.051   17.153  1.00 8.71  ? 73   LEU B C   1 
ATOM   2580 O  O   . LEU B 2 72  ? 99.058  3.093   16.364  1.00 10.32 ? 73   LEU B O   1 
ATOM   2581 C  CB  . LEU B 2 72  ? 98.696  4.826   18.812  1.00 10.23 ? 73   LEU B CB  1 
ATOM   2582 C  CG  . LEU B 2 72  ? 97.688  5.794   18.148  1.00 9.38  ? 73   LEU B CG  1 
ATOM   2583 C  CD1 . LEU B 2 72  ? 96.331  5.745   18.854  1.00 11.00 ? 73   LEU B CD1 1 
ATOM   2584 C  CD2 . LEU B 2 72  ? 98.281  7.254   18.291  1.00 13.10 ? 73   LEU B CD2 1 
ATOM   2585 N  N   . TYR B 2 73  ? 96.887  2.745   16.841  1.00 7.65  ? 74   TYR B N   1 
ATOM   2586 C  CA  . TYR B 2 73  ? 96.472  2.511   15.459  1.00 7.65  ? 74   TYR B CA  1 
ATOM   2587 C  C   . TYR B 2 73  ? 95.430  3.559   15.115  1.00 8.60  ? 74   TYR B C   1 
ATOM   2588 O  O   . TYR B 2 73  ? 94.667  3.995   15.981  1.00 8.63  ? 74   TYR B O   1 
ATOM   2589 C  CB  . TYR B 2 73  ? 95.825  1.132   15.298  1.00 8.74  ? 74   TYR B CB  1 
ATOM   2590 C  CG  . TYR B 2 73  ? 96.792  -0.019  15.206  1.00 9.18  ? 74   TYR B CG  1 
ATOM   2591 C  CD1 . TYR B 2 73  ? 97.279  -0.445  13.971  1.00 9.53  ? 74   TYR B CD1 1 
ATOM   2592 C  CD2 . TYR B 2 73  ? 97.220  -0.682  16.351  1.00 10.48 ? 74   TYR B CD2 1 
ATOM   2593 C  CE1 . TYR B 2 73  ? 98.172  -1.511  13.880  1.00 8.55  ? 74   TYR B CE1 1 
ATOM   2594 C  CE2 . TYR B 2 73  ? 98.115  -1.746  16.272  1.00 10.68 ? 74   TYR B CE2 1 
ATOM   2595 C  CZ  . TYR B 2 73  ? 98.584  -2.153  15.035  1.00 11.07 ? 74   TYR B CZ  1 
ATOM   2596 O  OH  . TYR B 2 73  ? 99.469  -3.204  14.963  1.00 11.71 ? 74   TYR B OH  1 
ATOM   2597 N  N   . LEU B 2 74  ? 95.449  3.990   13.863  1.00 6.95  ? 75   LEU B N   1 
ATOM   2598 C  CA  . LEU B 2 74  ? 94.448  4.933   13.364  1.00 7.36  ? 75   LEU B CA  1 
ATOM   2599 C  C   . LEU B 2 74  ? 93.584  4.249   12.309  1.00 7.14  ? 75   LEU B C   1 
ATOM   2600 O  O   . LEU B 2 74  ? 94.133  3.682   11.333  1.00 7.77  ? 75   LEU B O   1 
ATOM   2601 C  CB  . LEU B 2 74  ? 95.094  6.180   12.691  1.00 8.92  ? 75   LEU B CB  1 
ATOM   2602 C  CG  . LEU B 2 74  ? 96.173  6.873   13.482  1.00 11.09 ? 75   LEU B CG  1 
ATOM   2603 C  CD1 . LEU B 2 74  ? 96.703  8.055   12.614  1.00 14.19 ? 75   LEU B CD1 1 
ATOM   2604 C  CD2 . LEU B 2 74  ? 95.658  7.330   14.824  1.00 12.40 ? 75   LEU B CD2 1 
ATOM   2605 N  N   . LYS B 2 75  ? 92.260  4.267   12.532  1.00 6.52  ? 76   LYS B N   1 
ATOM   2606 C  CA  . LYS B 2 75  ? 91.369  3.711   11.501  1.00 6.78  ? 76   LYS B CA  1 
ATOM   2607 C  C   . LYS B 2 75  ? 91.215  4.843   10.474  1.00 7.18  ? 76   LYS B C   1 
ATOM   2608 O  O   . LYS B 2 75  ? 90.742  5.943   10.815  1.00 7.50  ? 76   LYS B O   1 
ATOM   2609 C  CB  . LYS B 2 75  ? 90.039  3.280   12.132  1.00 7.11  ? 76   LYS B CB  1 
ATOM   2610 C  CG  . LYS B 2 75  ? 89.061  2.760   11.105  1.00 7.43  ? 76   LYS B CG  1 
ATOM   2611 C  CD  . LYS B 2 75  ? 89.638  1.584   10.296  1.00 7.13  ? 76   LYS B CD  1 
ATOM   2612 C  CE  . LYS B 2 75  ? 88.471  0.900   9.585   1.00 7.32  ? 76   LYS B CE  1 
ATOM   2613 N  NZ  . LYS B 2 75  ? 89.052  0.000   8.522   1.00 7.23  ? 76   LYS B NZ  1 
ATOM   2614 N  N   . ARG B 2 76  ? 91.567  4.547   9.221   1.00 7.26  ? 77   ARG B N   1 
ATOM   2615 C  CA  . ARG B 2 76  ? 91.715  5.597   8.208   1.00 7.22  ? 77   ARG B CA  1 
ATOM   2616 C  C   . ARG B 2 76  ? 90.494  5.987   7.395   1.00 8.32  ? 77   ARG B C   1 
ATOM   2617 O  O   . ARG B 2 76  ? 90.493  5.850   6.141   1.00 8.39  ? 77   ARG B O   1 
ATOM   2618 C  CB  . ARG B 2 76  ? 92.878  5.193   7.279   1.00 8.25  ? 77   ARG B CB  1 
ATOM   2619 C  CG  . ARG B 2 76  ? 94.236  4.888   7.977   1.00 7.72  ? 77   ARG B CG  1 
ATOM   2620 C  CD  . ARG B 2 76  ? 94.827  6.168   8.657   1.00 7.95  ? 77   ARG B CD  1 
ATOM   2621 N  NE  . ARG B 2 76  ? 95.070  7.251   7.707   1.00 9.41  ? 77   ARG B NE  1 
ATOM   2622 C  CZ  . ARG B 2 76  ? 96.080  7.268   6.862   1.00 7.97  ? 77   ARG B CZ  1 
ATOM   2623 N  NH1 . ARG B 2 76  ? 96.996  6.310   6.861   1.00 8.10  ? 77   ARG B NH1 1 
ATOM   2624 N  NH2 . ARG B 2 76  ? 96.109  8.209   5.901   1.00 8.97  ? 77   ARG B NH2 1 
ATOM   2625 N  N   . GLU B 2 77  ? 89.492  6.529   8.077   1.00 8.29  ? 78   GLU B N   1 
ATOM   2626 C  CA  . GLU B 2 77  ? 88.328  7.011   7.352   1.00 7.52  ? 78   GLU B CA  1 
ATOM   2627 C  C   . GLU B 2 77  ? 88.689  8.290   6.537   1.00 8.24  ? 78   GLU B C   1 
ATOM   2628 O  O   . GLU B 2 77  ? 87.888  8.695   5.654   1.00 9.58  ? 78   GLU B O   1 
ATOM   2629 C  CB  . GLU B 2 77  ? 87.144  7.272   8.308   1.00 9.12  ? 78   GLU B CB  1 
ATOM   2630 C  CG  . GLU B 2 77  ? 86.703  5.971   8.988   1.00 8.07  ? 78   GLU B CG  1 
ATOM   2631 C  CD  . GLU B 2 77  ? 86.219  4.918   7.983   1.00 9.20  ? 78   GLU B CD  1 
ATOM   2632 O  OE1 . GLU B 2 77  ? 85.247  5.141   7.235   1.00 11.32 ? 78   GLU B OE1 1 
ATOM   2633 O  OE2 . GLU B 2 77  ? 86.873  3.839   7.964   1.00 10.11 ? 78   GLU B OE2 1 
ATOM   2634 N  N   . ASP B 2 78  ? 89.850  8.884   6.802   1.00 9.93  ? 79   ASP B N   1 
ATOM   2635 C  CA  . ASP B 2 78  ? 90.330  10.039  6.036   1.00 9.20  ? 79   ASP B CA  1 
ATOM   2636 C  C   . ASP B 2 78  ? 90.616  9.590   4.618   1.00 9.56  ? 79   ASP B C   1 
ATOM   2637 O  O   . ASP B 2 78  ? 90.697  10.447  3.716   1.00 10.84 ? 79   ASP B O   1 
ATOM   2638 C  CB  . ASP B 2 78  ? 91.613  10.649  6.641   1.00 9.57  ? 79   ASP B CB  1 
ATOM   2639 C  CG  . ASP B 2 78  ? 92.777  9.650   6.728   1.00 8.72  ? 79   ASP B CG  1 
ATOM   2640 O  OD1 . ASP B 2 78  ? 92.588  8.575   7.354   1.00 10.14 ? 79   ASP B OD1 1 
ATOM   2641 O  OD2 . ASP B 2 78  ? 93.891  9.950   6.175   1.00 11.25 ? 79   ASP B OD2 1 
ATOM   2642 N  N   . LEU B 2 79  ? 90.797  8.282   4.396   1.00 8.37  ? 80   LEU B N   1 
ATOM   2643 C  CA  . LEU B 2 79  ? 91.069  7.774   3.022   1.00 7.86  ? 80   LEU B CA  1 
ATOM   2644 C  C   . LEU B 2 79  ? 89.802  7.348   2.284   1.00 8.48  ? 80   LEU B C   1 
ATOM   2645 O  O   . LEU B 2 79  ? 89.894  6.917   1.120   1.00 10.51 ? 80   LEU B O   1 
ATOM   2646 C  CB  . LEU B 2 79  ? 92.048  6.565   3.063   1.00 7.91  ? 80   LEU B CB  1 
ATOM   2647 C  CG  . LEU B 2 79  ? 93.409  6.921   3.670   1.00 9.89  ? 80   LEU B CG  1 
ATOM   2648 C  CD1 . LEU B 2 79  ? 94.297  5.673   3.747   1.00 10.99 ? 80   LEU B CD1 1 
ATOM   2649 C  CD2 . LEU B 2 79  ? 94.074  8.103   2.840   1.00 10.91 ? 80   LEU B CD2 1 
ATOM   2650 N  N   . LEU B 2 80  ? 88.637  7.500   2.883   1.00 8.61  ? 81   LEU B N   1 
ATOM   2651 C  CA  . LEU B 2 80  ? 87.388  7.169   2.216   1.00 8.32  ? 81   LEU B CA  1 
ATOM   2652 C  C   . LEU B 2 80  ? 87.084  8.273   1.187   1.00 9.10  ? 81   LEU B C   1 
ATOM   2653 O  O   . LEU B 2 80  ? 87.447  9.426   1.361   1.00 10.34 ? 81   LEU B O   1 
ATOM   2654 C  CB  . LEU B 2 80  ? 86.262  7.133   3.254   1.00 8.66  ? 81   LEU B CB  1 
ATOM   2655 C  CG  . LEU B 2 80  ? 84.919  6.486   2.832   1.00 7.81  ? 81   LEU B CG  1 
ATOM   2656 C  CD1 . LEU B 2 80  ? 85.178  4.964   2.599   1.00 9.81  ? 81   LEU B CD1 1 
ATOM   2657 C  CD2 . LEU B 2 80  ? 83.930  6.616   3.970   1.00 9.54  ? 81   LEU B CD2 1 
ATOM   2658 N  N   . HIS B 2 81  ? 86.384  7.891   0.115   1.00 8.45  ? 82   HIS B N   1 
ATOM   2659 C  CA  . HIS B 2 81  ? 85.993  8.861   -0.902  1.00 8.79  ? 82   HIS B CA  1 
ATOM   2660 C  C   . HIS B 2 81  ? 85.220  9.987   -0.217  1.00 9.82  ? 82   HIS B C   1 
ATOM   2661 O  O   . HIS B 2 81  ? 84.289  9.728   0.548   1.00 10.42 ? 82   HIS B O   1 
ATOM   2662 C  CB  . HIS B 2 81  ? 85.118  8.180   -1.958  1.00 9.05  ? 82   HIS B CB  1 
ATOM   2663 C  CG  . HIS B 2 81  ? 84.560  9.122   -2.979  1.00 11.62 ? 82   HIS B CG  1 
ATOM   2664 N  ND1 . HIS B 2 81  ? 85.358  9.939   -3.751  1.00 11.83 ? 82   HIS B ND1 1 
ATOM   2665 C  CD2 . HIS B 2 81  ? 83.285  9.373   -3.359  1.00 12.61 ? 82   HIS B CD2 1 
ATOM   2666 C  CE1 . HIS B 2 81  ? 84.598  10.652  -4.563  1.00 12.20 ? 82   HIS B CE1 1 
ATOM   2667 N  NE2 . HIS B 2 81  ? 83.337  10.327  -4.346  1.00 11.88 ? 82   HIS B NE2 1 
ATOM   2668 N  N   . GLY B 2 82  ? 85.592  11.233  -0.529  1.00 9.53  ? 83   GLY B N   1 
ATOM   2669 C  CA  . GLY B 2 82  ? 84.983  12.420  0.085   1.00 10.12 ? 83   GLY B CA  1 
ATOM   2670 C  C   . GLY B 2 82  ? 85.825  12.922  1.276   1.00 10.59 ? 83   GLY B C   1 
ATOM   2671 O  O   . GLY B 2 82  ? 85.647  14.080  1.721   1.00 12.35 ? 83   GLY B O   1 
ATOM   2672 N  N   . GLY B 2 83  ? 86.699  12.076  1.812   1.00 9.12  ? 84   GLY B N   1 
ATOM   2673 C  CA  . GLY B 2 83  ? 87.589  12.511  2.892   1.00 10.14 ? 84   GLY B CA  1 
ATOM   2674 C  C   . GLY B 2 83  ? 87.063  12.391  4.295   1.00 8.48  ? 84   GLY B C   1 
ATOM   2675 O  O   . GLY B 2 83  ? 87.744  12.881  5.210   1.00 9.20  ? 84   GLY B O   1 
ATOM   2676 N  N   . ALA B 2 84  ? 85.903  11.766  4.486   1.00 8.43  ? 85   ALA B N   1 
ATOM   2677 C  CA  . ALA B 2 84  ? 85.411  11.553  5.862   1.00 7.75  ? 85   ALA B CA  1 
ATOM   2678 C  C   . ALA B 2 84  ? 84.470  10.356  5.816   1.00 7.92  ? 85   ALA B C   1 
ATOM   2679 O  O   . ALA B 2 84  ? 83.913  9.952   4.761   1.00 9.16  ? 85   ALA B O   1 
ATOM   2680 C  CB  . ALA B 2 84  ? 84.659  12.792  6.359   1.00 9.57  ? 85   ALA B CB  1 
ATOM   2681 N  N   . HIS B 2 85  ? 84.185  9.846   7.021   1.00 6.57  ? 86   HIS B N   1 
ATOM   2682 C  CA  . HIS B 2 85  ? 83.316  8.687   7.211   1.00 6.68  ? 86   HIS B CA  1 
ATOM   2683 C  C   . HIS B 2 85  ? 81.875  8.894   6.746   1.00 6.40  ? 86   HIS B C   1 
ATOM   2684 O  O   . HIS B 2 85  ? 81.161  7.923   6.521   1.00 7.66  ? 86   HIS B O   1 
ATOM   2685 C  CB  . HIS B 2 85  ? 83.263  8.323   8.694   1.00 6.79  ? 86   HIS B CB  1 
ATOM   2686 C  CG  . HIS B 2 85  ? 82.531  9.334   9.518   1.00 7.61  ? 86   HIS B CG  1 
ATOM   2687 N  ND1 . HIS B 2 85  ? 83.034  10.594  9.759   1.00 8.53  ? 86   HIS B ND1 1 
ATOM   2688 C  CD2 . HIS B 2 85  ? 81.302  9.302   10.086  1.00 9.34  ? 86   HIS B CD2 1 
ATOM   2689 C  CE1 . HIS B 2 85  ? 82.145  11.296  10.439  1.00 7.89  ? 86   HIS B CE1 1 
ATOM   2690 N  NE2 . HIS B 2 85  ? 81.085  10.537  10.648  1.00 8.31  ? 86   HIS B NE2 1 
ATOM   2691 N  N   . LYS B 2 86  ? 81.466  10.172  6.568   1.00 7.08  ? 87   LYS B N   1 
ATOM   2692 C  CA  . LYS B 2 86  ? 80.053  10.432  6.228   1.00 7.37  ? 87   LYS B CA  1 
ATOM   2693 C  C   . LYS B 2 86  ? 79.569  9.730   4.960   1.00 7.03  ? 87   LYS B C   1 
ATOM   2694 O  O   . LYS B 2 86  ? 78.382  9.374   4.834   1.00 8.10  ? 87   LYS B O   1 
ATOM   2695 C  CB  . LYS B 2 86  ? 79.843  11.959  6.078   1.00 7.88  ? 87   LYS B CB  1 
ATOM   2696 C  CG  . LYS B 2 86  ? 80.073  12.718  7.457   1.00 11.45 ? 87   LYS B CG  1 
ATOM   2697 C  CD  . LYS B 2 86  ? 79.489  14.171  7.303   1.00 15.44 ? 87   LYS B CD  1 
ATOM   2698 C  CE  . LYS B 2 86  ? 79.341  14.921  8.627   1.00 18.07 ? 87   LYS B CE  1 
ATOM   2699 N  NZ  . LYS B 2 86  ? 80.654  15.335  9.138   1.00 17.29 ? 87   LYS B NZ  1 
ATOM   2700 N  N   . THR B 2 87  ? 80.502  9.508   4.045   1.00 7.57  ? 88   THR B N   1 
ATOM   2701 C  CA  . THR B 2 87  ? 80.181  8.823   2.802   1.00 7.91  ? 88   THR B CA  1 
ATOM   2702 C  C   . THR B 2 87  ? 79.571  7.438   2.982   1.00 8.45  ? 88   THR B C   1 
ATOM   2703 O  O   . THR B 2 87  ? 78.701  7.030   2.210   1.00 8.18  ? 88   THR B O   1 
ATOM   2704 C  CB  . THR B 2 87  ? 81.456  8.710   1.971   1.00 8.25  ? 88   THR B CB  1 
ATOM   2705 O  OG1 . THR B 2 87  ? 81.858  10.040  1.655   1.00 9.60  ? 88   THR B OG1 1 
ATOM   2706 C  CG2 . THR B 2 87  ? 81.235  7.893   0.687   1.00 10.15 ? 88   THR B CG2 1 
ATOM   2707 N  N   . ASN B 2 88  ? 79.945  6.736   4.041   1.00 6.90  ? 89   ASN B N   1 
ATOM   2708 C  CA  . ASN B 2 88  ? 79.367  5.368   4.220   1.00 6.68  ? 89   ASN B CA  1 
ATOM   2709 C  C   . ASN B 2 88  ? 77.851  5.406   4.313   1.00 8.20  ? 89   ASN B C   1 
ATOM   2710 O  O   . ASN B 2 88  ? 77.148  4.654   3.614   1.00 8.95  ? 89   ASN B O   1 
ATOM   2711 C  CB  . ASN B 2 88  ? 79.864  4.702   5.509   1.00 7.06  ? 89   ASN B CB  1 
ATOM   2712 C  CG  . ASN B 2 88  ? 81.374  4.457   5.498   1.00 7.39  ? 89   ASN B CG  1 
ATOM   2713 O  OD1 . ASN B 2 88  ? 81.943  3.986   4.529   1.00 7.71  ? 89   ASN B OD1 1 
ATOM   2714 N  ND2 . ASN B 2 88  ? 82.004  4.800   6.639   1.00 8.04  ? 89   ASN B ND2 1 
ATOM   2715 N  N   . GLN B 2 89  ? 77.356  6.265   5.193   1.00 7.72  ? 90   GLN B N   1 
ATOM   2716 C  CA  . GLN B 2 89  ? 75.933  6.197   5.448   1.00 8.14  ? 90   GLN B CA  1 
ATOM   2717 C  C   . GLN B 2 89  ? 75.080  6.930   4.434   1.00 7.64  ? 90   GLN B C   1 
ATOM   2718 O  O   . GLN B 2 89  ? 73.915  6.540   4.253   1.00 9.51  ? 90   GLN B O   1 
ATOM   2719 C  CB  . GLN B 2 89  ? 75.700  6.620   6.884   1.00 8.61  ? 90   GLN B CB  1 
ATOM   2720 C  CG  . GLN B 2 89  ? 75.787  8.171   7.107   1.00 9.54  ? 90   GLN B CG  1 
ATOM   2721 C  CD  . GLN B 2 89  ? 74.381  8.788   7.163   1.00 10.63 ? 90   GLN B CD  1 
ATOM   2722 O  OE1 . GLN B 2 89  ? 73.395  8.065   7.125   1.00 11.48 ? 90   GLN B OE1 1 
ATOM   2723 N  NE2 . GLN B 2 89  ? 74.318  10.124  7.304   1.00 11.96 ? 90   GLN B NE2 1 
ATOM   2724 N  N   . VAL B 2 90  ? 75.632  7.929   3.741   1.00 7.83  ? 91   VAL B N   1 
ATOM   2725 C  CA  . VAL B 2 90  ? 74.789  8.595   2.708   1.00 8.65  ? 91   VAL B CA  1 
ATOM   2726 C  C   . VAL B 2 90  ? 74.587  7.610   1.545   1.00 9.03  ? 91   VAL B C   1 
ATOM   2727 O  O   . VAL B 2 90  ? 73.534  7.608   0.966   1.00 10.01 ? 91   VAL B O   1 
ATOM   2728 C  CB  . VAL B 2 90  ? 75.400  9.888   2.150   1.00 9.84  ? 91   VAL B CB  1 
ATOM   2729 C  CG1 . VAL B 2 90  ? 75.360  10.962  3.271   1.00 10.90 ? 91   VAL B CG1 1 
ATOM   2730 C  CG2 . VAL B 2 90  ? 76.860  9.680   1.661   1.00 12.11 ? 91   VAL B CG2 1 
ATOM   2731 N  N   . LEU B 2 91  ? 75.530  6.707   1.289   1.00 8.98  ? 92   LEU B N   1 
ATOM   2732 C  CA  . LEU B 2 91  ? 75.324  5.737   0.216   1.00 9.63  ? 92   LEU B CA  1 
ATOM   2733 C  C   . LEU B 2 91  ? 74.191  4.781   0.617   1.00 9.62  ? 92   LEU B C   1 
ATOM   2734 O  O   . LEU B 2 91  ? 73.286  4.478   -0.187  1.00 9.95  ? 92   LEU B O   1 
ATOM   2735 C  CB  . LEU B 2 91  ? 76.624  4.974   -0.067  1.00 10.03 ? 92   LEU B CB  1 
ATOM   2736 C  CG  . LEU B 2 91  ? 77.668  5.849   -0.751  1.00 9.62  ? 92   LEU B CG  1 
ATOM   2737 C  CD1 . LEU B 2 91  ? 78.989  5.090   -0.798  1.00 10.37 ? 92   LEU B CD1 1 
ATOM   2738 C  CD2 . LEU B 2 91  ? 77.222  6.223   -2.196  1.00 10.21 ? 92   LEU B CD2 1 
ATOM   2739 N  N   . GLY B 2 92  ? 74.155  4.381   1.903   1.00 8.71  ? 93   GLY B N   1 
ATOM   2740 C  CA  . GLY B 2 92  ? 73.080  3.478   2.366   1.00 9.05  ? 93   GLY B CA  1 
ATOM   2741 C  C   . GLY B 2 92  ? 71.730  4.201   2.375   1.00 8.73  ? 93   GLY B C   1 
ATOM   2742 O  O   . GLY B 2 92  ? 70.710  3.632   1.935   1.00 9.07  ? 93   GLY B O   1 
ATOM   2743 N  N   . GLN B 2 93  ? 71.711  5.443   2.858   1.00 8.70  ? 94   GLN B N   1 
ATOM   2744 C  CA  . GLN B 2 93  ? 70.433  6.155   2.887   1.00 9.74  ? 94   GLN B CA  1 
ATOM   2745 C  C   . GLN B 2 93  ? 69.957  6.462   1.465   1.00 9.44  ? 94   GLN B C   1 
ATOM   2746 O  O   . GLN B 2 93  ? 68.713  6.477   1.254   1.00 9.68  ? 94   GLN B O   1 
ATOM   2747 C  CB  . GLN B 2 93  ? 70.536  7.474   3.650   1.00 8.02  ? 94   GLN B CB  1 
ATOM   2748 C  CG  . GLN B 2 93  ? 70.517  7.283   5.175   1.00 9.73  ? 94   GLN B CG  1 
ATOM   2749 C  CD  . GLN B 2 93  ? 70.033  8.543   5.872   1.00 11.14 ? 94   GLN B CD  1 
ATOM   2750 O  OE1 . GLN B 2 93  ? 68.923  9.040   5.585   1.00 10.31 ? 94   GLN B OE1 1 
ATOM   2751 N  NE2 . GLN B 2 93  ? 70.861  9.089   6.752   1.00 10.01 ? 94   GLN B NE2 1 
ATOM   2752 N  N   . ALA B 2 94  ? 70.864  6.738   0.525   1.00 9.51  ? 95   ALA B N   1 
ATOM   2753 C  CA  . ALA B 2 94  ? 70.422  6.981   -0.853  1.00 10.89 ? 95   ALA B CA  1 
ATOM   2754 C  C   . ALA B 2 94  ? 69.817  5.692   -1.433  1.00 10.75 ? 95   ALA B C   1 
ATOM   2755 O  O   . ALA B 2 94  ? 68.782  5.761   -2.125  1.00 9.91  ? 95   ALA B O   1 
ATOM   2756 C  CB  . ALA B 2 94  ? 71.604  7.442   -1.715  1.00 10.27 ? 95   ALA B CB  1 
ATOM   2757 N  N   . LEU B 2 95  ? 70.403  4.528   -1.131  1.00 10.72 ? 96   LEU B N   1 
ATOM   2758 C  CA  . LEU B 2 95  ? 69.801  3.280   -1.598  1.00 11.40 ? 96   LEU B CA  1 
ATOM   2759 C  C   . LEU B 2 95  ? 68.427  3.075   -0.938  1.00 12.67 ? 96   LEU B C   1 
ATOM   2760 O  O   . LEU B 2 95  ? 67.502  2.520   -1.566  1.00 13.55 ? 96   LEU B O   1 
ATOM   2761 C  CB  . LEU B 2 95  ? 70.692  2.087   -1.272  1.00 10.53 ? 96   LEU B CB  1 
ATOM   2762 C  CG  . LEU B 2 95  ? 71.915  2.025   -2.152  1.00 10.32 ? 96   LEU B CG  1 
ATOM   2763 C  CD1 . LEU B 2 95  ? 72.766  0.868   -1.663  1.00 13.24 ? 96   LEU B CD1 1 
ATOM   2764 C  CD2 . LEU B 2 95  ? 71.570  1.840   -3.613  1.00 13.89 ? 96   LEU B CD2 1 
ATOM   2765 N  N   . LEU B 2 96  ? 68.259  3.457   0.329   1.00 11.06 ? 97   LEU B N   1 
ATOM   2766 C  CA  . LEU B 2 96  ? 66.949  3.318   0.971   1.00 11.66 ? 97   LEU B CA  1 
ATOM   2767 C  C   . LEU B 2 96  ? 65.928  4.207   0.322   1.00 12.21 ? 97   LEU B C   1 
ATOM   2768 O  O   . LEU B 2 96  ? 64.767  3.818   0.159   1.00 13.15 ? 97   LEU B O   1 
ATOM   2769 C  CB  . LEU B 2 96  ? 66.957  3.667   2.489   1.00 14.12 ? 97   LEU B CB  1 
ATOM   2770 C  CG  . LEU B 2 96  ? 67.581  2.719   3.472   1.00 16.53 ? 97   LEU B CG  1 
ATOM   2771 C  CD1 . LEU B 2 96  ? 67.384  3.286   4.889   1.00 15.86 ? 97   LEU B CD1 1 
ATOM   2772 C  CD2 . LEU B 2 96  ? 66.888  1.306   3.426   1.00 16.56 ? 97   LEU B CD2 1 
ATOM   2773 N  N   . ALA B 2 97  ? 66.292  5.451   0.025   1.00 11.37 ? 98   ALA B N   1 
ATOM   2774 C  CA  . ALA B 2 97  ? 65.391  6.377   -0.649  1.00 12.13 ? 98   ALA B CA  1 
ATOM   2775 C  C   . ALA B 2 97  ? 64.912  5.725   -1.956  1.00 13.76 ? 98   ALA B C   1 
ATOM   2776 O  O   . ALA B 2 97  ? 63.717  5.756   -2.252  1.00 13.73 ? 98   ALA B O   1 
ATOM   2777 C  CB  . ALA B 2 97  ? 66.115  7.700   -0.948  1.00 11.79 ? 98   ALA B CB  1 
ATOM   2778 N  N   . LYS B 2 98  ? 65.829  5.152   -2.718  1.00 13.03 ? 99   LYS B N   1 
ATOM   2779 C  CA  . LYS B 2 98  ? 65.402  4.515   -3.976  1.00 14.09 ? 99   LYS B CA  1 
ATOM   2780 C  C   . LYS B 2 98  ? 64.505  3.282   -3.720  1.00 14.47 ? 99   LYS B C   1 
ATOM   2781 O  O   . LYS B 2 98  ? 63.544  3.014   -4.492  1.00 15.88 ? 99   LYS B O   1 
ATOM   2782 C  CB  . LYS B 2 98  ? 66.665  4.180   -4.784  1.00 14.38 ? 99   LYS B CB  1 
ATOM   2783 C  CG  . LYS B 2 98  ? 67.345  5.470   -5.213  1.00 17.93 ? 99   LYS B CG  1 
ATOM   2784 C  CD  . LYS B 2 98  ? 68.752  5.237   -5.700  1.00 23.82 ? 99   LYS B CD  1 
ATOM   2785 C  CE  . LYS B 2 98  ? 68.762  4.324   -6.916  1.00 26.47 ? 99   LYS B CE  1 
ATOM   2786 N  NZ  . LYS B 2 98  ? 68.665  5.063   -8.213  1.00 27.07 ? 99   LYS B NZ  1 
ATOM   2787 N  N   . ARG B 2 99  ? 64.772  2.528   -2.640  1.00 13.13 ? 100  ARG B N   1 
ATOM   2788 C  CA  . ARG B 2 99  ? 63.983  1.345   -2.327  1.00 13.98 ? 100  ARG B CA  1 
ATOM   2789 C  C   . ARG B 2 99  ? 62.516  1.753   -2.056  1.00 12.72 ? 100  ARG B C   1 
ATOM   2790 O  O   . ARG B 2 99  ? 61.577  1.018   -2.438  1.00 14.98 ? 100  ARG B O   1 
ATOM   2791 C  CB  . ARG B 2 99  ? 64.570  0.660   -1.109  1.00 13.51 ? 100  ARG B CB  1 
ATOM   2792 C  CG  . ARG B 2 99  ? 63.858  -0.642  -0.734  1.00 14.12 ? 100  ARG B CG  1 
ATOM   2793 C  CD  . ARG B 2 99  ? 64.419  -1.208  0.517   1.00 15.74 ? 100  ARG B CD  1 
ATOM   2794 N  NE  . ARG B 2 99  ? 63.905  -2.553  0.819   1.00 17.04 ? 100  ARG B NE  1 
ATOM   2795 C  CZ  . ARG B 2 99  ? 64.416  -3.674  0.313   1.00 14.91 ? 100  ARG B CZ  1 
ATOM   2796 N  NH1 . ARG B 2 99  ? 65.443  -3.650  -0.511  1.00 15.73 ? 100  ARG B NH1 1 
ATOM   2797 N  NH2 . ARG B 2 99  ? 63.911  -4.836  0.671   1.00 17.38 ? 100  ARG B NH2 1 
ATOM   2798 N  N   . MET B 2 100 ? 62.330  2.933   -1.473  1.00 13.45 ? 101  MET B N   1 
ATOM   2799 C  CA  . MET B 2 100 ? 61.001  3.452   -1.155  1.00 14.38 ? 101  MET B CA  1 
ATOM   2800 C  C   . MET B 2 100 ? 60.366  4.143   -2.333  1.00 14.90 ? 101  MET B C   1 
ATOM   2801 O  O   . MET B 2 100 ? 59.168  4.520   -2.274  1.00 15.48 ? 101  MET B O   1 
ATOM   2802 C  CB  . MET B 2 100 ? 61.066  4.445   0.003   1.00 14.92 ? 101  MET B CB  1 
ATOM   2803 C  CG  . MET B 2 100 ? 61.485  3.798   1.301   1.00 14.70 ? 101  MET B CG  1 
ATOM   2804 S  SD  . MET B 2 100 ? 61.404  4.984   2.724   1.00 16.48 ? 101  MET B SD  1 
ATOM   2805 C  CE  . MET B 2 100 ? 62.733  6.097   2.369   1.00 14.45 ? 101  MET B CE  1 
ATOM   2806 N  N   . GLY B 2 101 ? 61.121  4.277   -3.419  1.00 16.15 ? 102  GLY B N   1 
ATOM   2807 C  CA  . GLY B 2 101 ? 60.624  4.945   -4.614  1.00 17.57 ? 102  GLY B CA  1 
ATOM   2808 C  C   . GLY B 2 101 ? 60.725  6.456   -4.602  1.00 17.50 ? 102  GLY B C   1 
ATOM   2809 O  O   . GLY B 2 101 ? 60.055  7.118   -5.398  1.00 19.43 ? 102  GLY B O   1 
ATOM   2810 N  N   . LYS B 2 102 ? 61.504  7.029   -3.681  1.00 17.23 ? 103  LYS B N   1 
ATOM   2811 C  CA  . LYS B 2 102 ? 61.668  8.487   -3.580  1.00 17.24 ? 103  LYS B CA  1 
ATOM   2812 C  C   . LYS B 2 102 ? 62.689  8.945   -4.621  1.00 18.57 ? 103  LYS B C   1 
ATOM   2813 O  O   . LYS B 2 102 ? 63.657  8.225   -4.880  1.00 20.28 ? 103  LYS B O   1 
ATOM   2814 C  CB  . LYS B 2 102 ? 62.184  8.899   -2.178  1.00 18.56 ? 103  LYS B CB  1 
ATOM   2815 C  CG  . LYS B 2 102 ? 61.332  8.535   -0.969  1.00 21.75 ? 103  LYS B CG  1 
ATOM   2816 C  CD  . LYS B 2 102 ? 60.071  9.322   -0.802  1.00 21.81 ? 103  LYS B CD  1 
ATOM   2817 C  CE  . LYS B 2 102 ? 59.281  8.763   0.386   1.00 20.81 ? 103  LYS B CE  1 
ATOM   2818 N  NZ  . LYS B 2 102 ? 59.519  9.525   1.682   1.00 21.36 ? 103  LYS B NZ  1 
ATOM   2819 N  N   . SER B 2 103 ? 62.504  10.147  -5.171  1.00 17.94 ? 104  SER B N   1 
ATOM   2820 C  CA  . SER B 2 103 ? 63.377  10.670  -6.235  1.00 18.98 ? 104  SER B CA  1 
ATOM   2821 C  C   . SER B 2 103 ? 64.144  11.912  -5.846  1.00 17.75 ? 104  SER B C   1 
ATOM   2822 O  O   . SER B 2 103 ? 65.008  12.362  -6.592  1.00 17.78 ? 104  SER B O   1 
ATOM   2823 C  CB  . SER B 2 103 ? 62.572  11.028  -7.529  1.00 20.63 ? 104  SER B CB  1 
ATOM   2824 O  OG  . SER B 2 103 ? 61.684  12.120  -7.267  1.00 23.64 ? 104  SER B OG  1 
ATOM   2825 N  N   . GLU B 2 104 ? 63.860  12.416  -4.652  1.00 16.46 ? 105  GLU B N   1 
ATOM   2826 C  CA  . GLU B 2 104 ? 64.483  13.643  -4.168  1.00 14.56 ? 105  GLU B CA  1 
ATOM   2827 C  C   . GLU B 2 104 ? 65.077  13.438  -2.748  1.00 13.17 ? 105  GLU B C   1 
ATOM   2828 O  O   . GLU B 2 104 ? 64.585  12.598  -1.996  1.00 13.51 ? 105  GLU B O   1 
ATOM   2829 C  CB  . GLU B 2 104 ? 63.460  14.787  -4.124  1.00 17.75 ? 105  GLU B CB  1 
ATOM   2830 C  CG  . GLU B 2 104 ? 62.985  15.121  -5.540  1.00 22.07 ? 105  GLU B CG  1 
ATOM   2831 C  CD  . GLU B 2 104 ? 61.968  16.242  -5.613  1.00 26.69 ? 105  GLU B CD  1 
ATOM   2832 O  OE1 . GLU B 2 104 ? 61.463  16.489  -6.749  1.00 29.55 ? 105  GLU B OE1 1 
ATOM   2833 O  OE2 . GLU B 2 104 ? 61.688  16.849  -4.563  1.00 27.51 ? 105  GLU B OE2 1 
ATOM   2834 N  N   . ILE B 2 105 ? 66.156  14.166  -2.493  1.00 12.25 ? 106  ILE B N   1 
ATOM   2835 C  CA  . ILE B 2 105 ? 66.870  14.109  -1.180  1.00 11.64 ? 106  ILE B CA  1 
ATOM   2836 C  C   . ILE B 2 105 ? 66.932  15.496  -0.595  1.00 12.16 ? 106  ILE B C   1 
ATOM   2837 O  O   . ILE B 2 105 ? 67.263  16.476  -1.270  1.00 13.05 ? 106  ILE B O   1 
ATOM   2838 C  CB  . ILE B 2 105 ? 68.348  13.623  -1.403  1.00 11.33 ? 106  ILE B CB  1 
ATOM   2839 C  CG1 . ILE B 2 105 ? 68.359  12.146  -1.805  1.00 13.19 ? 106  ILE B CG1 1 
ATOM   2840 C  CG2 . ILE B 2 105 ? 69.211  13.875  -0.118  1.00 11.02 ? 106  ILE B CG2 1 
ATOM   2841 C  CD1 . ILE B 2 105 ? 67.859  11.168  -0.682  1.00 15.90 ? 106  ILE B CD1 1 
ATOM   2842 N  N   . ILE B 2 106 ? 66.604  15.571  0.703   1.00 11.66 ? 107  ILE B N   1 
ATOM   2843 C  CA  . ILE B 2 106 ? 66.775  16.803  1.472   1.00 12.17 ? 107  ILE B CA  1 
ATOM   2844 C  C   . ILE B 2 106 ? 67.892  16.493  2.508   1.00 11.45 ? 107  ILE B C   1 
ATOM   2845 O  O   . ILE B 2 106 ? 67.914  15.391  3.085   1.00 12.23 ? 107  ILE B O   1 
ATOM   2846 C  CB  . ILE B 2 106 ? 65.524  17.106  2.326   1.00 11.44 ? 107  ILE B CB  1 
ATOM   2847 C  CG1 . ILE B 2 106 ? 64.328  17.298  1.421   1.00 13.52 ? 107  ILE B CG1 1 
ATOM   2848 C  CG2 . ILE B 2 106 ? 65.794  18.342  3.244   1.00 14.43 ? 107  ILE B CG2 1 
ATOM   2849 C  CD1 . ILE B 2 106 ? 62.975  17.150  2.167   1.00 13.82 ? 107  ILE B CD1 1 
ATOM   2850 N  N   . ALA B 2 107 ? 68.835  17.408  2.686   1.00 12.26 ? 108  ALA B N   1 
ATOM   2851 C  CA  . ALA B 2 107 ? 69.839  17.223  3.731   1.00 13.02 ? 108  ALA B CA  1 
ATOM   2852 C  C   . ALA B 2 107 ? 70.172  18.544  4.367   1.00 14.53 ? 108  ALA B C   1 
ATOM   2853 O  O   . ALA B 2 107 ? 69.961  19.591  3.767   1.00 15.36 ? 108  ALA B O   1 
ATOM   2854 C  CB  . ALA B 2 107 ? 71.132  16.611  3.176   1.00 14.54 ? 108  ALA B CB  1 
ATOM   2855 N  N   . GLU B 2 108 ? 70.645  18.477  5.611   1.00 15.12 ? 109  GLU B N   1 
ATOM   2856 C  CA  . GLU B 2 108 ? 71.096  19.646  6.332   1.00 15.97 ? 109  GLU B CA  1 
ATOM   2857 C  C   . GLU B 2 108 ? 72.620  19.547  6.425   1.00 14.85 ? 109  GLU B C   1 
ATOM   2858 O  O   . GLU B 2 108 ? 73.192  18.441  6.349   1.00 15.49 ? 109  GLU B O   1 
ATOM   2859 C  CB  . GLU B 2 108 ? 70.524  19.658  7.798   1.00 15.89 ? 109  GLU B CB  1 
ATOM   2860 C  CG  . GLU B 2 108 ? 71.291  18.778  8.862   1.00 14.91 ? 109  GLU B CG  1 
ATOM   2861 C  CD  . GLU B 2 108 ? 71.238  17.218  8.672   1.00 16.61 ? 109  GLU B CD  1 
ATOM   2862 O  OE1 . GLU B 2 108 ? 70.307  16.747  8.017   1.00 18.22 ? 109  GLU B OE1 1 
ATOM   2863 O  OE2 . GLU B 2 108 ? 72.144  16.522  9.216   1.00 18.98 ? 109  GLU B OE2 1 
ATOM   2864 N  N   . THR B 2 109 ? 73.294  20.679  6.547   1.00 13.97 ? 110  THR B N   1 
ATOM   2865 C  CA  . THR B 2 109 ? 74.745  20.627  6.792   1.00 12.70 ? 110  THR B CA  1 
ATOM   2866 C  C   . THR B 2 109 ? 75.206  21.879  7.549   1.00 15.14 ? 110  THR B C   1 
ATOM   2867 O  O   . THR B 2 109 ? 74.601  22.956  7.405   1.00 15.01 ? 110  THR B O   1 
ATOM   2868 C  CB  . THR B 2 109 ? 75.550  20.425  5.449   1.00 15.11 ? 110  THR B CB  1 
ATOM   2869 O  OG1 . THR B 2 109 ? 76.901  20.038  5.757   1.00 15.52 ? 110  THR B OG1 1 
ATOM   2870 C  CG2 . THR B 2 109 ? 75.569  21.696  4.629   1.00 14.07 ? 110  THR B CG2 1 
ATOM   2871 N  N   . GLY B 2 110 ? 76.251  21.707  8.354   1.00 15.87 ? 111  GLY B N   1 
ATOM   2872 C  CA  . GLY B 2 110 ? 76.816  22.801  9.152   1.00 17.23 ? 111  GLY B CA  1 
ATOM   2873 C  C   . GLY B 2 110 ? 78.117  23.234  8.500   1.00 17.99 ? 111  GLY B C   1 
ATOM   2874 O  O   . GLY B 2 110 ? 78.161  24.249  7.790   1.00 19.90 ? 111  GLY B O   1 
ATOM   2875 N  N   . ALA B 2 111 ? 79.161  22.429  8.691   1.00 17.11 ? 112  ALA B N   1 
ATOM   2876 C  CA  . ALA B 2 111 ? 80.489  22.717  8.129   1.00 16.68 ? 112  ALA B CA  1 
ATOM   2877 C  C   . ALA B 2 111 ? 80.518  22.380  6.632   1.00 17.05 ? 112  ALA B C   1 
ATOM   2878 O  O   . ALA B 2 111 ? 81.412  22.781  5.910   1.00 18.04 ? 112  ALA B O   1 
ATOM   2879 C  CB  . ALA B 2 111 ? 81.528  21.874  8.843   1.00 17.83 ? 112  ALA B CB  1 
ATOM   2880 N  N   . GLY B 2 112 ? 79.510  21.639  6.174   1.00 15.16 ? 113  GLY B N   1 
ATOM   2881 C  CA  . GLY B 2 112 ? 79.468  21.350  4.752   1.00 15.28 ? 113  GLY B CA  1 
ATOM   2882 C  C   . GLY B 2 112 ? 79.821  19.915  4.369   1.00 13.79 ? 113  GLY B C   1 
ATOM   2883 O  O   . GLY B 2 112 ? 79.488  19.532  3.231   1.00 14.33 ? 113  GLY B O   1 
ATOM   2884 N  N   . GLN B 2 113 ? 80.461  19.125  5.227   1.00 14.52 ? 114  GLN B N   1 
ATOM   2885 C  CA  . GLN B 2 113 ? 80.861  17.773  4.830   1.00 14.59 ? 114  GLN B CA  1 
ATOM   2886 C  C   . GLN B 2 113 ? 79.684  16.883  4.563   1.00 14.64 ? 114  GLN B C   1 
ATOM   2887 O  O   . GLN B 2 113 ? 79.684  16.119  3.589   1.00 13.52 ? 114  GLN B O   1 
ATOM   2888 C  CB  . GLN B 2 113 ? 81.819  17.105  5.860   1.00 16.95 ? 114  GLN B CB  1 
ATOM   2889 C  CG  . GLN B 2 113 ? 82.413  15.735  5.388   1.00 19.13 ? 114  GLN B CG  1 
ATOM   2890 C  CD  . GLN B 2 113 ? 83.239  15.863  4.116   1.00 24.76 ? 114  GLN B CD  1 
ATOM   2891 O  OE1 . GLN B 2 113 ? 83.903  16.891  3.909   1.00 26.39 ? 114  GLN B OE1 1 
ATOM   2892 N  NE2 . GLN B 2 113 ? 83.219  14.821  3.253   1.00 23.21 ? 114  GLN B NE2 1 
ATOM   2893 N  N   . HIS B 2 114 ? 78.632  16.968  5.386   1.00 12.52 ? 115  HIS B N   1 
ATOM   2894 C  CA  . HIS B 2 114 ? 77.485  16.117  5.110   1.00 12.00 ? 115  HIS B CA  1 
ATOM   2895 C  C   . HIS B 2 114 ? 76.810  16.562  3.816   1.00 12.53 ? 115  HIS B C   1 
ATOM   2896 O  O   . HIS B 2 114 ? 76.288  15.737  3.065   1.00 12.13 ? 115  HIS B O   1 
ATOM   2897 C  CB  . HIS B 2 114 ? 76.467  16.141  6.251   1.00 10.94 ? 115  HIS B CB  1 
ATOM   2898 C  CG  . HIS B 2 114 ? 75.295  15.242  6.010   1.00 9.50  ? 115  HIS B CG  1 
ATOM   2899 N  ND1 . HIS B 2 114 ? 75.431  13.883  5.817   1.00 11.30 ? 115  HIS B ND1 1 
ATOM   2900 C  CD2 . HIS B 2 114 ? 73.976  15.511  5.869   1.00 10.10 ? 115  HIS B CD2 1 
ATOM   2901 C  CE1 . HIS B 2 114 ? 74.247  13.356  5.564   1.00 10.31 ? 115  HIS B CE1 1 
ATOM   2902 N  NE2 . HIS B 2 114 ? 73.346  14.323  5.590   1.00 9.76  ? 115  HIS B NE2 1 
ATOM   2903 N  N   . GLY B 2 115 ? 76.766  17.864  3.568   1.00 12.18 ? 116  GLY B N   1 
ATOM   2904 C  CA  . GLY B 2 115 ? 76.199  18.374  2.322   1.00 11.29 ? 116  GLY B CA  1 
ATOM   2905 C  C   . GLY B 2 115 ? 76.976  17.820  1.126   1.00 11.86 ? 116  GLY B C   1 
ATOM   2906 O  O   . GLY B 2 115 ? 76.334  17.373  0.174   1.00 11.81 ? 116  GLY B O   1 
ATOM   2907 N  N   . VAL B 2 116 ? 78.319  17.868  1.170   1.00 11.55 ? 117  VAL B N   1 
ATOM   2908 C  CA  . VAL B 2 116 ? 79.117  17.284  0.090   1.00 11.77 ? 117  VAL B CA  1 
ATOM   2909 C  C   . VAL B 2 116 ? 78.840  15.778  -0.044  1.00 11.40 ? 117  VAL B C   1 
ATOM   2910 O  O   . VAL B 2 116 ? 78.683  15.273  -1.172  1.00 10.91 ? 117  VAL B O   1 
ATOM   2911 C  CB  . VAL B 2 116 ? 80.575  17.572  0.336   1.00 12.89 ? 117  VAL B CB  1 
ATOM   2912 C  CG1 . VAL B 2 116 ? 81.458  16.848  -0.719  1.00 15.69 ? 117  VAL B CG1 1 
ATOM   2913 C  CG2 . VAL B 2 116 ? 80.799  19.062  0.146   1.00 14.78 ? 117  VAL B CG2 1 
ATOM   2914 N  N   . ALA B 2 117 ? 78.811  15.060  1.080   1.00 9.36  ? 118  ALA B N   1 
ATOM   2915 C  CA  . ALA B 2 117 ? 78.584  13.620  0.965   1.00 10.07 ? 118  ALA B CA  1 
ATOM   2916 C  C   . ALA B 2 117 ? 77.180  13.348  0.385   1.00 8.90  ? 118  ALA B C   1 
ATOM   2917 O  O   . ALA B 2 117 ? 77.002  12.401  -0.451  1.00 9.24  ? 118  ALA B O   1 
ATOM   2918 C  CB  . ALA B 2 117 ? 78.703  12.961  2.374   1.00 9.82  ? 118  ALA B CB  1 
ATOM   2919 N  N   . SER B 2 118 ? 76.167  14.134  0.783   1.00 10.26 ? 119  SER B N   1 
ATOM   2920 C  CA  . SER B 2 118 ? 74.822  13.885  0.278   1.00 9.55  ? 119  SER B CA  1 
ATOM   2921 C  C   . SER B 2 118 ? 74.754  14.212  -1.227  1.00 9.74  ? 119  SER B C   1 
ATOM   2922 O  O   . SER B 2 118 ? 74.083  13.495  -1.974  1.00 9.56  ? 119  SER B O   1 
ATOM   2923 C  CB  . SER B 2 118 ? 73.809  14.790  1.003   1.00 11.20 ? 119  SER B CB  1 
ATOM   2924 O  OG  . SER B 2 118 ? 73.760  14.417  2.390   1.00 13.51 ? 119  SER B OG  1 
ATOM   2925 N  N   . ALA B 2 119 ? 75.460  15.267  -1.634  1.00 10.22 ? 120  ALA B N   1 
ATOM   2926 C  CA  . ALA B 2 119 ? 75.445  15.657  -3.043  1.00 10.85 ? 120  ALA B CA  1 
ATOM   2927 C  C   . ALA B 2 119 ? 76.170  14.587  -3.858  1.00 10.52 ? 120  ALA B C   1 
ATOM   2928 O  O   . ALA B 2 119 ? 75.710  14.256  -4.953  1.00 11.85 ? 120  ALA B O   1 
ATOM   2929 C  CB  . ALA B 2 119 ? 76.109  17.011  -3.232  1.00 11.92 ? 120  ALA B CB  1 
ATOM   2930 N  N   . LEU B 2 120 ? 77.273  14.020  -3.359  1.00 10.15 ? 121  LEU B N   1 
ATOM   2931 C  CA  . LEU B 2 120 ? 77.972  13.043  -4.245  1.00 9.17  ? 121  LEU B CA  1 
ATOM   2932 C  C   . LEU B 2 120 ? 77.160  11.746  -4.345  1.00 8.71  ? 121  LEU B C   1 
ATOM   2933 O  O   . LEU B 2 120 ? 77.112  11.135  -5.439  1.00 10.32 ? 121  LEU B O   1 
ATOM   2934 C  CB  . LEU B 2 120 ? 79.410  12.766  -3.778  1.00 10.60 ? 121  LEU B CB  1 
ATOM   2935 C  CG  . LEU B 2 120 ? 79.607  12.081  -2.401  1.00 9.94  ? 121  LEU B CG  1 
ATOM   2936 C  CD1 . LEU B 2 120 ? 79.649  10.549  -2.582  1.00 11.62 ? 121  LEU B CD1 1 
ATOM   2937 C  CD2 . LEU B 2 120 ? 80.961  12.535  -1.805  1.00 12.45 ? 121  LEU B CD2 1 
ATOM   2938 N  N   . ALA B 2 121 ? 76.517  11.310  -3.263  1.00 8.90  ? 122  ALA B N   1 
ATOM   2939 C  CA  . ALA B 2 121 ? 75.716  10.099  -3.332  1.00 9.94  ? 122  ALA B CA  1 
ATOM   2940 C  C   . ALA B 2 121 ? 74.514  10.329  -4.261  1.00 10.97 ? 122  ALA B C   1 
ATOM   2941 O  O   . ALA B 2 121 ? 74.108  9.405   -5.005  1.00 11.64 ? 122  ALA B O   1 
ATOM   2942 C  CB  . ALA B 2 121 ? 75.215  9.712   -1.924  1.00 9.70  ? 122  ALA B CB  1 
ATOM   2943 N  N   . SER B 2 122 ? 73.958  11.537  -4.217  1.00 12.01 ? 123  SER B N   1 
ATOM   2944 C  CA  . SER B 2 122 ? 72.770  11.839  -5.028  1.00 11.71 ? 123  SER B CA  1 
ATOM   2945 C  C   . SER B 2 122 ? 73.179  11.918  -6.502  1.00 11.34 ? 123  SER B C   1 
ATOM   2946 O  O   . SER B 2 122 ? 72.415  11.425  -7.369  1.00 12.68 ? 123  SER B O   1 
ATOM   2947 C  CB  . SER B 2 122 ? 72.160  13.197  -4.598  1.00 10.25 ? 123  SER B CB  1 
ATOM   2948 O  OG  . SER B 2 122 ? 71.610  13.077  -3.281  1.00 12.23 ? 123  SER B OG  1 
ATOM   2949 N  N   . ALA B 2 123 ? 74.362  12.457  -6.776  1.00 11.59 ? 124  ALA B N   1 
ATOM   2950 C  CA  . ALA B 2 123 ? 74.833  12.590  -8.181  1.00 12.17 ? 124  ALA B CA  1 
ATOM   2951 C  C   . ALA B 2 123 ? 75.058  11.165  -8.712  1.00 13.14 ? 124  ALA B C   1 
ATOM   2952 O  O   . ALA B 2 123 ? 74.640  10.841  -9.835  1.00 14.12 ? 124  ALA B O   1 
ATOM   2953 C  CB  . ALA B 2 123 ? 76.138  13.365  -8.224  1.00 11.50 ? 124  ALA B CB  1 
ATOM   2954 N  N   . LEU B 2 124 ? 75.688  10.301  -7.920  1.00 11.74 ? 125  LEU B N   1 
ATOM   2955 C  CA  . LEU B 2 124 ? 75.959  8.940   -8.423  1.00 11.48 ? 125  LEU B CA  1 
ATOM   2956 C  C   . LEU B 2 124 ? 74.678  8.135   -8.637  1.00 11.42 ? 125  LEU B C   1 
ATOM   2957 O  O   . LEU B 2 124 ? 74.548  7.383   -9.636  1.00 12.58 ? 125  LEU B O   1 
ATOM   2958 C  CB  . LEU B 2 124 ? 76.806  8.194   -7.376  1.00 11.68 ? 125  LEU B CB  1 
ATOM   2959 C  CG  . LEU B 2 124 ? 77.111  6.729   -7.696  1.00 11.23 ? 125  LEU B CG  1 
ATOM   2960 C  CD1 . LEU B 2 124 ? 78.003  6.694   -8.949  1.00 12.17 ? 125  LEU B CD1 1 
ATOM   2961 C  CD2 . LEU B 2 124 ? 77.722  6.013   -6.443  1.00 14.07 ? 125  LEU B CD2 1 
ATOM   2962 N  N   . LEU B 2 125 ? 73.719  8.302   -7.735  1.00 11.50 ? 126  LEU B N   1 
ATOM   2963 C  CA  . LEU B 2 125 ? 72.533  7.465   -7.749  1.00 12.43 ? 126  LEU B CA  1 
ATOM   2964 C  C   . LEU B 2 125 ? 71.260  8.022   -8.398  1.00 13.72 ? 126  LEU B C   1 
ATOM   2965 O  O   . LEU B 2 125 ? 70.198  7.402   -8.298  1.00 15.68 ? 126  LEU B O   1 
ATOM   2966 C  CB  . LEU B 2 125 ? 72.273  6.909   -6.303  1.00 12.72 ? 126  LEU B CB  1 
ATOM   2967 C  CG  . LEU B 2 125 ? 73.427  6.027   -5.812  1.00 14.52 ? 126  LEU B CG  1 
ATOM   2968 C  CD1 . LEU B 2 125 ? 73.273  5.684   -4.314  1.00 17.10 ? 126  LEU B CD1 1 
ATOM   2969 C  CD2 . LEU B 2 125 ? 73.445  4.752   -6.620  1.00 16.73 ? 126  LEU B CD2 1 
ATOM   2970 N  N   . GLY B 2 126 ? 71.401  9.176   -9.042  1.00 13.41 ? 127  GLY B N   1 
ATOM   2971 C  CA  . GLY B 2 126 ? 70.280  9.778   -9.793  1.00 14.79 ? 127  GLY B CA  1 
ATOM   2972 C  C   . GLY B 2 126 ? 69.168  10.409  -8.985  1.00 15.62 ? 127  GLY B C   1 
ATOM   2973 O  O   . GLY B 2 126 ? 67.987  10.331  -9.340  1.00 17.70 ? 127  GLY B O   1 
ATOM   2974 N  N   . LEU B 2 127 ? 69.538  11.038  -7.883  1.00 13.42 ? 128  LEU B N   1 
ATOM   2975 C  CA  . LEU B 2 127 ? 68.559  11.671  -7.016  1.00 12.90 ? 128  LEU B CA  1 
ATOM   2976 C  C   . LEU B 2 127 ? 68.738  13.166  -7.077  1.00 11.56 ? 128  LEU B C   1 
ATOM   2977 O  O   . LEU B 2 127 ? 69.857  13.691  -7.210  1.00 14.46 ? 128  LEU B O   1 
ATOM   2978 C  CB  . LEU B 2 127 ? 68.753  11.186  -5.544  1.00 12.35 ? 128  LEU B CB  1 
ATOM   2979 C  CG  . LEU B 2 127 ? 68.468  9.669   -5.374  1.00 15.18 ? 128  LEU B CG  1 
ATOM   2980 C  CD1 . LEU B 2 127 ? 69.048  9.145   -4.071  1.00 14.53 ? 128  LEU B CD1 1 
ATOM   2981 C  CD2 . LEU B 2 127 ? 66.961  9.466   -5.255  1.00 17.55 ? 128  LEU B CD2 1 
ATOM   2982 N  N   . LYS B 2 128 ? 67.631  13.906  -6.992  1.00 13.09 ? 129  LYS B N   1 
ATOM   2983 C  CA  . LYS B 2 128 ? 67.667  15.372  -6.998  1.00 13.25 ? 129  LYS B CA  1 
ATOM   2984 C  C   . LYS B 2 128 ? 67.891  15.833  -5.536  1.00 15.04 ? 129  LYS B C   1 
ATOM   2985 O  O   . LYS B 2 128 ? 67.003  15.655  -4.672  1.00 17.21 ? 129  LYS B O   1 
ATOM   2986 C  CB  . LYS B 2 128 ? 66.315  15.912  -7.467  1.00 15.21 ? 129  LYS B CB  1 
ATOM   2987 N  N   . CYS B 2 129 ? 68.994  16.494  -5.298  1.00 13.85 ? 130  CYS B N   1 
ATOM   2988 C  CA  . CYS B 2 129 ? 69.395  16.859  -3.964  1.00 13.25 ? 130  CYS B CA  1 
ATOM   2989 C  C   . CYS B 2 129 ? 69.289  18.335  -3.645  1.00 13.76 ? 130  CYS B C   1 
ATOM   2990 O  O   . CYS B 2 129 ? 69.773  19.187  -4.428  1.00 14.80 ? 130  CYS B O   1 
ATOM   2991 C  CB  . CYS B 2 129 ? 70.871  16.385  -3.783  1.00 12.26 ? 130  CYS B CB  1 
ATOM   2992 S  SG  . CYS B 2 129 ? 71.590  16.615  -2.155  1.00 15.83 ? 130  CYS B SG  1 
ATOM   2993 N  N   . ARG B 2 130 ? 68.614  18.639  -2.524  1.00 12.83 ? 131  ARG B N   1 
ATOM   2994 C  CA  . ARG B 2 130 ? 68.588  20.024  -2.025  1.00 13.49 ? 131  ARG B CA  1 
ATOM   2995 C  C   . ARG B 2 130 ? 69.146  19.994  -0.593  1.00 13.22 ? 131  ARG B C   1 
ATOM   2996 O  O   . ARG B 2 130 ? 68.787  19.142  0.222   1.00 13.52 ? 131  ARG B O   1 
ATOM   2997 C  CB  . ARG B 2 130 ? 67.196  20.663  -2.089  1.00 15.32 ? 131  ARG B CB  1 
ATOM   2998 C  CG  . ARG B 2 130 ? 66.130  19.918  -1.389  1.00 13.07 ? 131  ARG B CG  1 
ATOM   2999 C  CD  . ARG B 2 130 ? 64.804  20.626  -1.730  1.00 15.05 ? 131  ARG B CD  1 
ATOM   3000 N  NE  . ARG B 2 130 ? 63.621  20.037  -1.148  1.00 14.88 ? 131  ARG B NE  1 
ATOM   3001 C  CZ  . ARG B 2 130 ? 62.897  19.058  -1.682  1.00 14.53 ? 131  ARG B CZ  1 
ATOM   3002 N  NH1 . ARG B 2 130 ? 63.201  18.489  -2.848  1.00 17.82 ? 131  ARG B NH1 1 
ATOM   3003 N  NH2 . ARG B 2 130 ? 61.766  18.682  -1.100  1.00 16.38 ? 131  ARG B NH2 1 
ATOM   3004 N  N   . ILE B 2 131 ? 69.999  20.967  -0.316  1.00 12.73 ? 132  ILE B N   1 
ATOM   3005 C  CA  . ILE B 2 131 ? 70.698  21.047  0.961   1.00 13.34 ? 132  ILE B CA  1 
ATOM   3006 C  C   . ILE B 2 131 ? 70.463  22.358  1.675   1.00 13.68 ? 132  ILE B C   1 
ATOM   3007 O  O   . ILE B 2 131 ? 70.695  23.434  1.112   1.00 16.22 ? 132  ILE B O   1 
ATOM   3008 C  CB  . ILE B 2 131 ? 72.228  20.919  0.703   1.00 13.91 ? 132  ILE B CB  1 
ATOM   3009 C  CG1 . ILE B 2 131 ? 72.475  19.570  0.020   1.00 15.97 ? 132  ILE B CG1 1 
ATOM   3010 C  CG2 . ILE B 2 131 ? 73.027  20.991  2.017   1.00 15.20 ? 132  ILE B CG2 1 
ATOM   3011 C  CD1 . ILE B 2 131 ? 73.825  19.505  -0.561  1.00 17.27 ? 132  ILE B CD1 1 
ATOM   3012 N  N   . TYR B 2 132 ? 70.058  22.257  2.942   1.00 13.60 ? 133  TYR B N   1 
ATOM   3013 C  CA  . TYR B 2 132 ? 69.825  23.434  3.765   1.00 14.40 ? 133  TYR B CA  1 
ATOM   3014 C  C   . TYR B 2 132 ? 71.069  23.690  4.604   1.00 14.68 ? 133  TYR B C   1 
ATOM   3015 O  O   . TYR B 2 132 ? 71.645  22.770  5.189   1.00 14.14 ? 133  TYR B O   1 
ATOM   3016 C  CB  . TYR B 2 132 ? 68.601  23.223  4.651   1.00 13.05 ? 133  TYR B CB  1 
ATOM   3017 C  CG  . TYR B 2 132 ? 67.311  23.288  3.873   1.00 13.36 ? 133  TYR B CG  1 
ATOM   3018 C  CD1 . TYR B 2 132 ? 66.843  24.502  3.367   1.00 13.70 ? 133  TYR B CD1 1 
ATOM   3019 C  CD2 . TYR B 2 132 ? 66.573  22.137  3.611   1.00 13.95 ? 133  TYR B CD2 1 
ATOM   3020 C  CE1 . TYR B 2 132 ? 65.670  24.566  2.622   1.00 13.66 ? 133  TYR B CE1 1 
ATOM   3021 C  CE2 . TYR B 2 132 ? 65.398  22.190  2.863   1.00 15.04 ? 133  TYR B CE2 1 
ATOM   3022 C  CZ  . TYR B 2 132 ? 64.953  23.407  2.375   1.00 14.88 ? 133  TYR B CZ  1 
ATOM   3023 O  OH  . TYR B 2 132 ? 63.786  23.463  1.650   1.00 16.44 ? 133  TYR B OH  1 
ATOM   3024 N  N   . MET B 2 133 ? 71.482  24.938  4.655   1.00 14.74 ? 134  MET B N   1 
ATOM   3025 C  CA  . MET B 2 133 ? 72.704  25.302  5.406   1.00 14.17 ? 134  MET B CA  1 
ATOM   3026 C  C   . MET B 2 133 ? 72.482  26.712  6.001   1.00 14.74 ? 134  MET B C   1 
ATOM   3027 O  O   . MET B 2 133 ? 72.049  27.649  5.284   1.00 15.06 ? 134  MET B O   1 
ATOM   3028 C  CB  . MET B 2 133 ? 73.883  25.308  4.421   1.00 14.95 ? 134  MET B CB  1 
ATOM   3029 C  CG  . MET B 2 133 ? 75.269  25.481  5.055   1.00 15.76 ? 134  MET B CG  1 
ATOM   3030 S  SD  . MET B 2 133 ? 76.439  25.220  3.656   1.00 17.04 ? 134  MET B SD  1 
ATOM   3031 C  CE  . MET B 2 133 ? 78.017  24.974  4.443   1.00 18.76 ? 134  MET B CE  1 
ATOM   3032 N  N   . GLY B 2 134 ? 72.749  26.858  7.298   1.00 14.65 ? 135  GLY B N   1 
ATOM   3033 C  CA  . GLY B 2 134 ? 72.560  28.178  7.915   1.00 16.02 ? 135  GLY B CA  1 
ATOM   3034 C  C   . GLY B 2 134 ? 73.374  29.207  7.142   1.00 16.87 ? 135  GLY B C   1 
ATOM   3035 O  O   . GLY B 2 134 ? 74.499  28.939  6.711   1.00 16.27 ? 135  GLY B O   1 
ATOM   3036 N  N   . ALA B 2 135 ? 72.819  30.406  6.968   1.00 16.77 ? 136  ALA B N   1 
ATOM   3037 C  CA  . ALA B 2 135 ? 73.545  31.427  6.219   1.00 17.09 ? 136  ALA B CA  1 
ATOM   3038 C  C   . ALA B 2 135 ? 74.916  31.804  6.802   1.00 17.84 ? 136  ALA B C   1 
ATOM   3039 O  O   . ALA B 2 135 ? 75.798  32.170  6.027   1.00 17.79 ? 136  ALA B O   1 
ATOM   3040 C  CB  . ALA B 2 135 ? 72.668  32.683  6.058   1.00 18.95 ? 136  ALA B CB  1 
ATOM   3041 N  N   . LYS B 2 136 ? 75.119  31.751  8.131   1.00 17.43 ? 137  LYS B N   1 
ATOM   3042 C  CA  . LYS B 2 136 ? 76.463  32.049  8.681   1.00 19.17 ? 137  LYS B CA  1 
ATOM   3043 C  C   . LYS B 2 136 ? 77.410  30.942  8.248   1.00 19.43 ? 137  LYS B C   1 
ATOM   3044 O  O   . LYS B 2 136 ? 78.585  31.181  7.984   1.00 19.84 ? 137  LYS B O   1 
ATOM   3045 C  CB  . LYS B 2 136 ? 76.453  32.153  10.221  1.00 21.92 ? 137  LYS B CB  1 
ATOM   3046 C  CG  . LYS B 2 136 ? 75.641  33.328  10.736  1.00 27.08 ? 137  LYS B CG  1 
ATOM   3047 C  CD  . LYS B 2 136 ? 75.801  33.453  12.242  1.00 31.08 ? 137  LYS B CD  1 
ATOM   3048 C  CE  . LYS B 2 136 ? 75.227  34.779  12.747  1.00 33.99 ? 137  LYS B CE  1 
ATOM   3049 N  NZ  . LYS B 2 136 ? 73.735  34.886  12.633  1.00 37.25 ? 137  LYS B NZ  1 
ATOM   3050 N  N   . ASP B 2 137 ? 76.892  29.725  8.104   1.00 17.99 ? 138  ASP B N   1 
ATOM   3051 C  CA  . ASP B 2 137 ? 77.767  28.640  7.652   1.00 18.40 ? 138  ASP B CA  1 
ATOM   3052 C  C   . ASP B 2 137 ? 78.067  28.726  6.159   1.00 17.66 ? 138  ASP B C   1 
ATOM   3053 O  O   . ASP B 2 137 ? 79.193  28.437  5.730   1.00 18.49 ? 138  ASP B O   1 
ATOM   3054 C  CB  . ASP B 2 137 ? 77.144  27.275  8.001   1.00 18.78 ? 138  ASP B CB  1 
ATOM   3055 C  CG  . ASP B 2 137 ? 77.243  26.984  9.480   1.00 19.44 ? 138  ASP B CG  1 
ATOM   3056 O  OD1 . ASP B 2 137 ? 78.302  27.299  10.076  1.00 22.19 ? 138  ASP B OD1 1 
ATOM   3057 O  OD2 . ASP B 2 137 ? 76.301  26.430  10.076  1.00 19.42 ? 138  ASP B OD2 1 
ATOM   3058 N  N   . VAL B 2 138 ? 77.083  29.107  5.371   1.00 17.27 ? 139  VAL B N   1 
ATOM   3059 C  CA  . VAL B 2 138 ? 77.280  29.272  3.921   1.00 17.48 ? 139  VAL B CA  1 
ATOM   3060 C  C   . VAL B 2 138 ? 78.419  30.278  3.739   1.00 19.60 ? 139  VAL B C   1 
ATOM   3061 O  O   . VAL B 2 138 ? 79.324  30.086  2.890   1.00 18.88 ? 139  VAL B O   1 
ATOM   3062 C  CB  . VAL B 2 138 ? 75.978  29.808  3.276   1.00 17.94 ? 139  VAL B CB  1 
ATOM   3063 C  CG1 . VAL B 2 138 ? 76.250  30.294  1.833   1.00 17.40 ? 139  VAL B CG1 1 
ATOM   3064 C  CG2 . VAL B 2 138 ? 74.893  28.679  3.259   1.00 17.95 ? 139  VAL B CG2 1 
ATOM   3065 N  N   . GLU B 2 139 ? 78.387  31.337  4.536   1.00 19.76 ? 140  GLU B N   1 
ATOM   3066 C  CA  . GLU B 2 139 ? 79.427  32.378  4.435   1.00 22.15 ? 140  GLU B CA  1 
ATOM   3067 C  C   . GLU B 2 139 ? 80.846  31.896  4.729   1.00 21.98 ? 140  GLU B C   1 
ATOM   3068 O  O   . GLU B 2 139 ? 81.816  32.344  4.066   1.00 23.42 ? 140  GLU B O   1 
ATOM   3069 C  CB  . GLU B 2 139 ? 79.094  33.538  5.395   1.00 25.22 ? 140  GLU B CB  1 
ATOM   3070 C  CG  . GLU B 2 139 ? 80.243  34.561  5.508   1.00 30.94 ? 140  GLU B CG  1 
ATOM   3071 C  CD  . GLU B 2 139 ? 80.415  35.371  4.232   1.00 35.99 ? 140  GLU B CD  1 
ATOM   3072 O  OE1 . GLU B 2 139 ? 79.766  35.013  3.207   1.00 38.30 ? 140  GLU B OE1 1 
ATOM   3073 O  OE2 . GLU B 2 139 ? 81.199  36.362  4.246   1.00 38.35 ? 140  GLU B OE2 1 
ATOM   3074 N  N   . ARG B 2 140 ? 81.003  31.001  5.691   1.00 21.33 ? 141  ARG B N   1 
ATOM   3075 C  CA  . ARG B 2 140 ? 82.328  30.541  6.049   1.00 21.28 ? 141  ARG B CA  1 
ATOM   3076 C  C   . ARG B 2 140 ? 82.737  29.218  5.410   1.00 20.33 ? 141  ARG B C   1 
ATOM   3077 O  O   . ARG B 2 140 ? 83.858  28.715  5.639   1.00 21.34 ? 141  ARG B O   1 
ATOM   3078 C  CB  . ARG B 2 140 ? 82.470  30.474  7.562   1.00 25.43 ? 141  ARG B CB  1 
ATOM   3079 C  CG  . ARG B 2 140 ? 81.509  29.569  8.261   1.00 28.25 ? 141  ARG B CG  1 
ATOM   3080 C  CD  . ARG B 2 140 ? 81.489  29.965  9.737   1.00 30.84 ? 141  ARG B CD  1 
ATOM   3081 N  NE  . ARG B 2 140 ? 80.319  29.401  10.386  1.00 32.86 ? 141  ARG B NE  1 
ATOM   3082 C  CZ  . ARG B 2 140 ? 80.027  29.571  11.671  1.00 34.46 ? 141  ARG B CZ  1 
ATOM   3083 N  NH1 . ARG B 2 140 ? 80.836  30.303  12.440  1.00 33.68 ? 141  ARG B NH1 1 
ATOM   3084 N  NH2 . ARG B 2 140 ? 78.934  29.003  12.189  1.00 33.30 ? 141  ARG B NH2 1 
ATOM   3085 N  N   . GLN B 2 141 ? 81.862  28.678  4.572   1.00 17.68 ? 142  GLN B N   1 
ATOM   3086 C  CA  . GLN B 2 141 ? 82.188  27.394  3.932   1.00 17.08 ? 142  GLN B CA  1 
ATOM   3087 C  C   . GLN B 2 141 ? 82.002  27.443  2.411   1.00 17.28 ? 142  GLN B C   1 
ATOM   3088 O  O   . GLN B 2 141 ? 81.463  26.511  1.782   1.00 17.39 ? 142  GLN B O   1 
ATOM   3089 C  CB  . GLN B 2 141 ? 81.339  26.273  4.534   1.00 17.06 ? 142  GLN B CB  1 
ATOM   3090 C  CG  . GLN B 2 141 ? 81.451  26.123  6.080   1.00 18.36 ? 142  GLN B CG  1 
ATOM   3091 C  CD  . GLN B 2 141 ? 82.793  25.613  6.585   1.00 20.01 ? 142  GLN B CD  1 
ATOM   3092 O  OE1 . GLN B 2 141 ? 83.048  25.612  7.815   1.00 23.51 ? 142  GLN B OE1 1 
ATOM   3093 N  NE2 . GLN B 2 141 ? 83.652  25.187  5.683   1.00 18.72 ? 142  GLN B NE2 1 
ATOM   3094 N  N   . SER B 2 142 ? 82.472  28.534  1.823   1.00 18.84 ? 143  SER B N   1 
ATOM   3095 C  CA  . SER B 2 142 ? 82.401  28.734  0.380   1.00 20.11 ? 143  SER B CA  1 
ATOM   3096 C  C   . SER B 2 142 ? 82.927  27.544  -0.420  1.00 19.95 ? 143  SER B C   1 
ATOM   3097 O  O   . SER B 2 142 ? 82.292  27.147  -1.372  1.00 19.52 ? 143  SER B O   1 
ATOM   3098 C  CB  . SER B 2 142 ? 83.206  29.966  -0.045  1.00 23.53 ? 143  SER B CB  1 
ATOM   3099 O  OG  . SER B 2 142 ? 82.650  31.123  0.555   1.00 30.04 ? 143  SER B OG  1 
ATOM   3100 N  N   . PRO B 2 143 ? 84.081  26.974  -0.034  1.00 20.74 ? 144  PRO B N   1 
ATOM   3101 C  CA  . PRO B 2 143 ? 84.570  25.830  -0.821  1.00 21.02 ? 144  PRO B CA  1 
ATOM   3102 C  C   . PRO B 2 143 ? 83.562  24.676  -0.867  1.00 18.32 ? 144  PRO B C   1 
ATOM   3103 O  O   . PRO B 2 143 ? 83.272  24.134  -1.957  1.00 19.02 ? 144  PRO B O   1 
ATOM   3104 C  CB  . PRO B 2 143 ? 85.874  25.435  -0.118  1.00 21.44 ? 144  PRO B CB  1 
ATOM   3105 C  CG  . PRO B 2 143 ? 86.358  26.784  0.450   1.00 22.81 ? 144  PRO B CG  1 
ATOM   3106 C  CD  . PRO B 2 143 ? 85.055  27.367  1.003   1.00 22.13 ? 144  PRO B CD  1 
ATOM   3107 N  N   . ASN B 2 144 ? 83.042  24.285  0.302   1.00 16.76 ? 145  ASN B N   1 
ATOM   3108 C  CA  . ASN B 2 144 ? 82.105  23.195  0.322   1.00 15.62 ? 145  ASN B CA  1 
ATOM   3109 C  C   . ASN B 2 144 ? 80.808  23.503  -0.436  1.00 16.47 ? 145  ASN B C   1 
ATOM   3110 O  O   . ASN B 2 144 ? 80.214  22.610  -1.069  1.00 14.91 ? 145  ASN B O   1 
ATOM   3111 C  CB  . ASN B 2 144 ? 81.804  22.807  1.758   1.00 16.05 ? 145  ASN B CB  1 
ATOM   3112 C  CG  . ASN B 2 144 ? 82.811  21.819  2.337   1.00 17.66 ? 145  ASN B CG  1 
ATOM   3113 O  OD1 . ASN B 2 144 ? 82.868  21.622  3.586   1.00 19.64 ? 145  ASN B OD1 1 
ATOM   3114 N  ND2 . ASN B 2 144 ? 83.592  21.158  1.456   1.00 16.63 ? 145  ASN B ND2 1 
ATOM   3115 N  N   . VAL B 2 145 ? 80.341  24.752  -0.388  1.00 15.36 ? 146  VAL B N   1 
ATOM   3116 C  CA  . VAL B 2 145 ? 79.130  25.122  -1.114  1.00 15.51 ? 146  VAL B CA  1 
ATOM   3117 C  C   . VAL B 2 145 ? 79.362  24.942  -2.636  1.00 16.18 ? 146  VAL B C   1 
ATOM   3118 O  O   . VAL B 2 145 ? 78.510  24.401  -3.364  1.00 16.39 ? 146  VAL B O   1 
ATOM   3119 C  CB  . VAL B 2 145 ? 78.698  26.592  -0.775  1.00 16.72 ? 146  VAL B CB  1 
ATOM   3120 C  CG1 . VAL B 2 145 ? 77.585  27.045  -1.672  1.00 17.63 ? 146  VAL B CG1 1 
ATOM   3121 C  CG2 . VAL B 2 145 ? 78.202  26.646  0.704   1.00 18.11 ? 146  VAL B CG2 1 
ATOM   3122 N  N   . PHE B 2 146 ? 80.556  25.313  -3.081  1.00 16.49 ? 147  PHE B N   1 
ATOM   3123 C  CA  . PHE B 2 146 ? 80.874  25.188  -4.498  1.00 16.17 ? 147  PHE B CA  1 
ATOM   3124 C  C   . PHE B 2 146 ? 80.934  23.713  -4.901  1.00 15.67 ? 147  PHE B C   1 
ATOM   3125 O  O   . PHE B 2 146 ? 80.486  23.342  -5.989  1.00 15.79 ? 147  PHE B O   1 
ATOM   3126 C  CB  . PHE B 2 146 ? 82.208  25.874  -4.804  1.00 18.00 ? 147  PHE B CB  1 
ATOM   3127 C  CG  . PHE B 2 146 ? 82.538  25.924  -6.269  1.00 19.89 ? 147  PHE B CG  1 
ATOM   3128 C  CD1 . PHE B 2 146 ? 81.658  26.512  -7.172  1.00 21.51 ? 147  PHE B CD1 1 
ATOM   3129 C  CD2 . PHE B 2 146 ? 83.724  25.378  -6.749  1.00 22.28 ? 147  PHE B CD2 1 
ATOM   3130 C  CE1 . PHE B 2 146 ? 81.952  26.555  -8.533  1.00 22.72 ? 147  PHE B CE1 1 
ATOM   3131 C  CE2 . PHE B 2 146 ? 84.029  25.417  -8.110  1.00 22.37 ? 147  PHE B CE2 1 
ATOM   3132 C  CZ  . PHE B 2 146 ? 83.141  26.006  -9.002  1.00 22.40 ? 147  PHE B CZ  1 
ATOM   3133 N  N   . ARG B 2 147 ? 81.540  22.880  -4.040  1.00 14.06 ? 148  ARG B N   1 
ATOM   3134 C  CA  . ARG B 2 147 ? 81.604  21.400  -4.303  1.00 12.76 ? 148  ARG B CA  1 
ATOM   3135 C  C   . ARG B 2 147 ? 80.178  20.861  -4.468  1.00 14.49 ? 148  ARG B C   1 
ATOM   3136 O  O   . ARG B 2 147 ? 79.895  20.074  -5.370  1.00 13.41 ? 148  ARG B O   1 
ATOM   3137 C  CB  . ARG B 2 147 ? 82.276  20.660  -3.146  1.00 15.02 ? 148  ARG B CB  1 
ATOM   3138 C  CG  . ARG B 2 147 ? 83.796  20.900  -3.066  1.00 16.25 ? 148  ARG B CG  1 
ATOM   3139 C  CD  . ARG B 2 147 ? 84.347  20.036  -1.952  1.00 19.89 ? 148  ARG B CD  1 
ATOM   3140 N  NE  . ARG B 2 147 ? 85.798  20.157  -1.853  1.00 23.15 ? 148  ARG B NE  1 
ATOM   3141 C  CZ  . ARG B 2 147 ? 86.464  20.995  -1.061  1.00 27.27 ? 148  ARG B CZ  1 
ATOM   3142 N  NH1 . ARG B 2 147 ? 85.842  21.842  -0.234  1.00 24.77 ? 148  ARG B NH1 1 
ATOM   3143 N  NH2 . ARG B 2 147 ? 87.787  21.008  -1.109  1.00 28.43 ? 148  ARG B NH2 1 
ATOM   3144 N  N   . MET B 2 148 ? 79.281  21.208  -3.546  1.00 14.32 ? 149  MET B N   1 
ATOM   3145 C  CA  . MET B 2 148 ? 77.888  20.732  -3.647  1.00 14.80 ? 149  MET B CA  1 
ATOM   3146 C  C   . MET B 2 148 ? 77.252  21.127  -4.985  1.00 14.60 ? 149  MET B C   1 
ATOM   3147 O  O   . MET B 2 148 ? 76.564  20.322  -5.628  1.00 14.03 ? 149  MET B O   1 
ATOM   3148 C  CB  . MET B 2 148 ? 77.035  21.296  -2.478  1.00 14.34 ? 149  MET B CB  1 
ATOM   3149 C  CG  . MET B 2 148 ? 77.410  20.695  -1.148  1.00 14.33 ? 149  MET B CG  1 
ATOM   3150 S  SD  . MET B 2 148 ? 76.541  21.531  0.256   1.00 16.07 ? 149  MET B SD  1 
ATOM   3151 C  CE  . MET B 2 148 ? 77.910  22.163  1.168   1.00 17.93 ? 149  MET B CE  1 
ATOM   3152 N  N   . ARG B 2 149 ? 77.441  22.400  -5.385  1.00 14.64 ? 150  ARG B N   1 
ATOM   3153 C  CA  . ARG B 2 149 ? 76.866  22.859  -6.634  1.00 15.63 ? 150  ARG B CA  1 
ATOM   3154 C  C   . ARG B 2 149 ? 77.494  22.200  -7.873  1.00 14.12 ? 150  ARG B C   1 
ATOM   3155 O  O   . ARG B 2 149 ? 76.783  21.836  -8.778  1.00 15.38 ? 150  ARG B O   1 
ATOM   3156 C  CB  . ARG B 2 149 ? 76.922  24.390  -6.688  1.00 17.25 ? 150  ARG B CB  1 
ATOM   3157 C  CG  . ARG B 2 149 ? 75.963  24.978  -5.657  1.00 19.56 ? 150  ARG B CG  1 
ATOM   3158 C  CD  . ARG B 2 149 ? 76.035  26.490  -5.537  1.00 23.87 ? 150  ARG B CD  1 
ATOM   3159 N  NE  . ARG B 2 149 ? 74.878  26.965  -4.752  1.00 25.54 ? 150  ARG B NE  1 
ATOM   3160 C  CZ  . ARG B 2 149 ? 74.863  28.094  -4.036  1.00 29.34 ? 150  ARG B CZ  1 
ATOM   3161 N  NH1 . ARG B 2 149 ? 73.758  28.453  -3.358  1.00 28.49 ? 150  ARG B NH1 1 
ATOM   3162 N  NH2 . ARG B 2 149 ? 75.958  28.859  -3.973  1.00 28.49 ? 150  ARG B NH2 1 
ATOM   3163 N  N   . LEU B 2 150 ? 78.805  21.972  -7.838  1.00 13.25 ? 151  LEU B N   1 
ATOM   3164 C  CA  . LEU B 2 150 ? 79.453  21.248  -8.963  1.00 14.29 ? 151  LEU B CA  1 
ATOM   3165 C  C   . LEU B 2 150 ? 78.826  19.860  -9.081  1.00 13.46 ? 151  LEU B C   1 
ATOM   3166 O  O   . LEU B 2 150 ? 78.704  19.334  -10.214 1.00 14.64 ? 151  LEU B O   1 
ATOM   3167 C  CB  . LEU B 2 150 ? 80.954  21.062  -8.700  1.00 14.36 ? 151  LEU B CB  1 
ATOM   3168 C  CG  . LEU B 2 150 ? 81.877  22.279  -8.862  1.00 16.33 ? 151  LEU B CG  1 
ATOM   3169 C  CD1 . LEU B 2 150 ? 83.205  22.016  -8.223  1.00 16.95 ? 151  LEU B CD1 1 
ATOM   3170 C  CD2 . LEU B 2 150 ? 82.001  22.608  -10.330 1.00 18.76 ? 151  LEU B CD2 1 
ATOM   3171 N  N   . MET B 2 151 ? 78.442  19.261  -7.950  1.00 13.05 ? 152  MET B N   1 
ATOM   3172 C  CA  . MET B 2 151 ? 77.783  17.983  -7.988  1.00 12.55 ? 152  MET B CA  1 
ATOM   3173 C  C   . MET B 2 151 ? 76.294  17.973  -8.250  1.00 12.10 ? 152  MET B C   1 
ATOM   3174 O  O   . MET B 2 151 ? 75.628  16.918  -8.196  1.00 13.77 ? 152  MET B O   1 
ATOM   3175 C  CB  . MET B 2 151 ? 78.163  17.185  -6.732  1.00 13.30 ? 152  MET B CB  1 
ATOM   3176 C  CG  A MET B 2 151 ? 79.586  17.110  -6.496  0.50 14.19 ? 152  MET B CG  1 
ATOM   3177 C  CG  B MET B 2 151 ? 79.673  16.738  -6.832  0.50 12.93 ? 152  MET B CG  1 
ATOM   3178 S  SD  A MET B 2 151 ? 79.723  16.246  -4.960  0.50 15.55 ? 152  MET B SD  1 
ATOM   3179 S  SD  B MET B 2 151 ? 80.502  15.760  -5.552  0.50 14.98 ? 152  MET B SD  1 
ATOM   3180 C  CE  A MET B 2 151 ? 81.423  15.672  -5.221  0.50 13.21 ? 152  MET B CE  1 
ATOM   3181 C  CE  B MET B 2 151 ? 80.045  16.755  -4.027  0.50 12.21 ? 152  MET B CE  1 
ATOM   3182 N  N   . GLY B 2 152 ? 75.769  19.164  -8.594  1.00 12.12 ? 153  GLY B N   1 
ATOM   3183 C  CA  . GLY B 2 152 ? 74.386  19.261  -8.982  1.00 14.23 ? 153  GLY B CA  1 
ATOM   3184 C  C   . GLY B 2 152 ? 73.383  19.479  -7.880  1.00 14.92 ? 153  GLY B C   1 
ATOM   3185 O  O   . GLY B 2 152 ? 72.181  19.441  -8.174  1.00 16.54 ? 153  GLY B O   1 
ATOM   3186 N  N   . ALA B 2 153 ? 73.833  19.660  -6.647  1.00 14.21 ? 154  ALA B N   1 
ATOM   3187 C  CA  . ALA B 2 153 ? 72.845  19.893  -5.578  1.00 14.08 ? 154  ALA B CA  1 
ATOM   3188 C  C   . ALA B 2 153 ? 72.450  21.369  -5.495  1.00 15.55 ? 154  ALA B C   1 
ATOM   3189 O  O   . ALA B 2 153 ? 73.232  22.256  -5.827  1.00 17.17 ? 154  ALA B O   1 
ATOM   3190 C  CB  . ALA B 2 153 ? 73.431  19.463  -4.231  1.00 15.40 ? 154  ALA B CB  1 
ATOM   3191 N  N   . GLU B 2 154 ? 71.218  21.615  -5.069  1.00 14.01 ? 155  GLU B N   1 
ATOM   3192 C  CA  . GLU B 2 154 ? 70.737  22.985  -4.828  1.00 16.27 ? 155  GLU B CA  1 
ATOM   3193 C  C   . GLU B 2 154 ? 71.073  23.286  -3.365  1.00 16.18 ? 155  GLU B C   1 
ATOM   3194 O  O   . GLU B 2 154 ? 70.745  22.482  -2.503  1.00 18.47 ? 155  GLU B O   1 
ATOM   3195 C  CB  . GLU B 2 154 ? 69.228  23.031  -5.025  1.00 17.32 ? 155  GLU B CB  1 
ATOM   3196 C  CG  . GLU B 2 154 ? 68.578  24.347  -4.590  1.00 20.82 ? 155  GLU B CG  1 
ATOM   3197 C  CD  . GLU B 2 154 ? 67.079  24.347  -4.873  1.00 25.56 ? 155  GLU B CD  1 
ATOM   3198 O  OE1 . GLU B 2 154 ? 66.482  23.245  -4.979  1.00 26.02 ? 155  GLU B OE1 1 
ATOM   3199 O  OE2 . GLU B 2 154 ? 66.524  25.471  -4.977  1.00 29.00 ? 155  GLU B OE2 1 
ATOM   3200 N  N   . VAL B 2 155 ? 71.778  24.381  -3.088  1.00 14.42 ? 156  VAL B N   1 
ATOM   3201 C  CA  . VAL B 2 155 ? 72.133  24.754  -1.708  1.00 15.07 ? 156  VAL B CA  1 
ATOM   3202 C  C   . VAL B 2 155 ? 71.241  25.949  -1.348  1.00 15.48 ? 156  VAL B C   1 
ATOM   3203 O  O   . VAL B 2 155 ? 71.277  26.981  -2.028  1.00 16.81 ? 156  VAL B O   1 
ATOM   3204 C  CB  . VAL B 2 155 ? 73.654  25.128  -1.614  1.00 16.08 ? 156  VAL B CB  1 
ATOM   3205 C  CG1 . VAL B 2 155 ? 74.018  25.541  -0.189  1.00 19.53 ? 156  VAL B CG1 1 
ATOM   3206 C  CG2 . VAL B 2 155 ? 74.524  23.914  -2.054  1.00 17.64 ? 156  VAL B CG2 1 
ATOM   3207 N  N   . ILE B 2 156 ? 70.493  25.799  -0.253  1.00 14.41 ? 157  ILE B N   1 
ATOM   3208 C  CA  . ILE B 2 156 ? 69.543  26.825  0.181   1.00 15.85 ? 157  ILE B CA  1 
ATOM   3209 C  C   . ILE B 2 156 ? 69.955  27.390  1.558   1.00 14.47 ? 157  ILE B C   1 
ATOM   3210 O  O   . ILE B 2 156 ? 69.908  26.692  2.573   1.00 15.98 ? 157  ILE B O   1 
ATOM   3211 C  CB  . ILE B 2 156 ? 68.158  26.198  0.315   1.00 15.29 ? 157  ILE B CB  1 
ATOM   3212 C  CG1 . ILE B 2 156 ? 67.757  25.522  -1.001  1.00 16.86 ? 157  ILE B CG1 1 
ATOM   3213 C  CG2 . ILE B 2 156 ? 67.106  27.312  0.777   1.00 16.82 ? 157  ILE B CG2 1 
ATOM   3214 C  CD1 . ILE B 2 156 ? 66.480  24.671  -0.940  1.00 17.10 ? 157  ILE B CD1 1 
ATOM   3215 N  N   . PRO B 2 157 ? 70.352  28.664  1.617   1.00 15.05 ? 158  PRO B N   1 
ATOM   3216 C  CA  . PRO B 2 157 ? 70.750  29.291  2.875   1.00 15.70 ? 158  PRO B CA  1 
ATOM   3217 C  C   . PRO B 2 157 ? 69.568  29.475  3.780   1.00 16.44 ? 158  PRO B C   1 
ATOM   3218 O  O   . PRO B 2 157 ? 68.451  29.752  3.311   1.00 17.99 ? 158  PRO B O   1 
ATOM   3219 C  CB  . PRO B 2 157 ? 71.348  30.637  2.455   1.00 16.66 ? 158  PRO B CB  1 
ATOM   3220 C  CG  . PRO B 2 157 ? 71.784  30.384  0.987   1.00 16.43 ? 158  PRO B CG  1 
ATOM   3221 C  CD  . PRO B 2 157 ? 70.663  29.502  0.449   1.00 14.74 ? 158  PRO B CD  1 
ATOM   3222 N  N   . VAL B 2 158 ? 69.809  29.294  5.085   1.00 15.97 ? 159  VAL B N   1 
ATOM   3223 C  CA  . VAL B 2 158 ? 68.756  29.443  6.080   1.00 15.78 ? 159  VAL B CA  1 
ATOM   3224 C  C   . VAL B 2 158 ? 69.124  30.637  6.971   1.00 16.97 ? 159  VAL B C   1 
ATOM   3225 O  O   . VAL B 2 158 ? 70.136  30.639  7.647   1.00 17.32 ? 159  VAL B O   1 
ATOM   3226 C  CB  . VAL B 2 158 ? 68.600  28.107  6.902   1.00 14.69 ? 159  VAL B CB  1 
ATOM   3227 C  CG1 . VAL B 2 158 ? 67.520  28.271  8.004   1.00 17.12 ? 159  VAL B CG1 1 
ATOM   3228 C  CG2 . VAL B 2 158 ? 68.216  26.983  5.938   1.00 17.48 ? 159  VAL B CG2 1 
ATOM   3229 N  N   . HIS B 2 159 ? 68.275  31.670  6.948   1.00 19.37 ? 160  HIS B N   1 
ATOM   3230 C  CA  . HIS B 2 159 ? 68.515  32.895  7.710   1.00 20.15 ? 160  HIS B CA  1 
ATOM   3231 C  C   . HIS B 2 159 ? 67.771  32.986  9.038   1.00 19.59 ? 160  HIS B C   1 
ATOM   3232 O  O   . HIS B 2 159 ? 67.966  33.937  9.795   1.00 21.09 ? 160  HIS B O   1 
ATOM   3233 C  CB  . HIS B 2 159 ? 68.148  34.104  6.847   1.00 22.28 ? 160  HIS B CB  1 
ATOM   3234 C  CG  . HIS B 2 159 ? 68.876  34.156  5.541   1.00 24.50 ? 160  HIS B CG  1 
ATOM   3235 N  ND1 . HIS B 2 159 ? 70.172  34.611  5.429   1.00 26.33 ? 160  HIS B ND1 1 
ATOM   3236 C  CD2 . HIS B 2 159 ? 68.499  33.784  4.296   1.00 26.21 ? 160  HIS B CD2 1 
ATOM   3237 C  CE1 . HIS B 2 159 ? 70.561  34.517  4.169   1.00 26.50 ? 160  HIS B CE1 1 
ATOM   3238 N  NE2 . HIS B 2 159 ? 69.564  34.018  3.461   1.00 26.79 ? 160  HIS B NE2 1 
ATOM   3239 N  N   . SER B 2 160 ? 66.893  32.032  9.303   1.00 18.61 ? 161  SER B N   1 
ATOM   3240 C  CA  . SER B 2 160 ? 66.156  32.026  10.566  1.00 18.36 ? 161  SER B CA  1 
ATOM   3241 C  C   . SER B 2 160 ? 67.012  31.633  11.773  1.00 18.20 ? 161  SER B C   1 
ATOM   3242 O  O   . SER B 2 160 ? 68.092  31.049  11.656  1.00 16.56 ? 161  SER B O   1 
ATOM   3243 C  CB  . SER B 2 160 ? 64.959  31.085  10.449  1.00 19.14 ? 161  SER B CB  1 
ATOM   3244 O  OG  . SER B 2 160 ? 65.350  29.763  10.020  1.00 21.53 ? 161  SER B OG  1 
ATOM   3245 N  N   . GLY B 2 161 ? 66.523  32.014  12.962  1.00 19.05 ? 162  GLY B N   1 
ATOM   3246 C  CA  . GLY B 2 161 ? 67.224  31.687  14.185  1.00 18.17 ? 162  GLY B CA  1 
ATOM   3247 C  C   . GLY B 2 161 ? 68.656  32.169  14.212  1.00 19.86 ? 162  GLY B C   1 
ATOM   3248 O  O   . GLY B 2 161 ? 68.948  33.350  13.934  1.00 22.51 ? 162  GLY B O   1 
ATOM   3249 N  N   . SER B 2 162 ? 69.553  31.266  14.570  1.00 19.11 ? 163  SER B N   1 
ATOM   3250 C  CA  . SER B 2 162 ? 70.970  31.571  14.669  1.00 20.13 ? 163  SER B CA  1 
ATOM   3251 C  C   . SER B 2 162 ? 71.708  31.429  13.306  1.00 18.92 ? 163  SER B C   1 
ATOM   3252 O  O   . SER B 2 162 ? 72.928  31.638  13.221  1.00 18.67 ? 163  SER B O   1 
ATOM   3253 C  CB  . SER B 2 162 ? 71.613  30.697  15.774  1.00 21.81 ? 163  SER B CB  1 
ATOM   3254 O  OG  . SER B 2 162 ? 71.562  29.275  15.530  1.00 24.64 ? 163  SER B OG  1 
ATOM   3255 N  N   . ALA B 2 163 ? 70.952  31.071  12.271  1.00 17.64 ? 164  ALA B N   1 
ATOM   3256 C  CA  . ALA B 2 163 ? 71.468  30.896  10.896  1.00 17.22 ? 164  ALA B CA  1 
ATOM   3257 C  C   . ALA B 2 163 ? 72.651  29.918  10.862  1.00 16.71 ? 164  ALA B C   1 
ATOM   3258 O  O   . ALA B 2 163 ? 73.662  30.124  10.137  1.00 16.35 ? 164  ALA B O   1 
ATOM   3259 C  CB  . ALA B 2 163 ? 71.873  32.268  10.297  1.00 18.16 ? 164  ALA B CB  1 
ATOM   3260 N  N   . THR B 2 164 ? 72.561  28.871  11.690  1.00 15.21 ? 165  THR B N   1 
ATOM   3261 C  CA  . THR B 2 164 ? 73.608  27.848  11.700  1.00 15.60 ? 165  THR B CA  1 
ATOM   3262 C  C   . THR B 2 164 ? 72.959  26.453  11.644  1.00 15.24 ? 165  THR B C   1 
ATOM   3263 O  O   . THR B 2 164 ? 71.790  26.330  11.226  1.00 15.21 ? 165  THR B O   1 
ATOM   3264 C  CB  A THR B 2 164 ? 74.608  27.975  12.904  0.50 15.81 ? 165  THR B CB  1 
ATOM   3265 C  CB  B THR B 2 164 ? 74.507  28.044  12.960  0.50 17.40 ? 165  THR B CB  1 
ATOM   3266 O  OG1 A THR B 2 164 ? 73.912  27.956  14.169  0.50 14.70 ? 165  THR B OG1 1 
ATOM   3267 O  OG1 B THR B 2 164 ? 75.677  27.230  12.887  0.50 19.16 ? 165  THR B OG1 1 
ATOM   3268 C  CG2 A THR B 2 164 ? 75.391  29.266  12.793  0.50 15.15 ? 165  THR B CG2 1 
ATOM   3269 C  CG2 B THR B 2 164 ? 73.736  27.691  14.227  0.50 17.11 ? 165  THR B CG2 1 
ATOM   3270 N  N   . LEU B 2 165 ? 73.690  25.418  12.075  1.00 14.43 ? 166  LEU B N   1 
ATOM   3271 C  CA  . LEU B 2 165 ? 73.216  24.025  11.916  1.00 15.52 ? 166  LEU B CA  1 
ATOM   3272 C  C   . LEU B 2 165 ? 71.853  23.672  12.443  1.00 15.79 ? 166  LEU B C   1 
ATOM   3273 O  O   . LEU B 2 165 ? 71.046  23.097  11.722  1.00 15.46 ? 166  LEU B O   1 
ATOM   3274 C  CB  . LEU B 2 165 ? 74.269  23.062  12.468  1.00 13.98 ? 166  LEU B CB  1 
ATOM   3275 C  CG  . LEU B 2 165 ? 73.936  21.543  12.351  1.00 15.29 ? 166  LEU B CG  1 
ATOM   3276 C  CD1 . LEU B 2 165 ? 73.689  21.163  10.877  1.00 15.28 ? 166  LEU B CD1 1 
ATOM   3277 C  CD2 . LEU B 2 165 ? 75.141  20.754  12.861  1.00 17.59 ? 166  LEU B CD2 1 
ATOM   3278 N  N   . LYS B 2 166 ? 71.566  24.048  13.692  1.00 15.33 ? 167  LYS B N   1 
ATOM   3279 C  CA  . LYS B 2 166 ? 70.231  23.685  14.219  1.00 15.31 ? 167  LYS B CA  1 
ATOM   3280 C  C   . LYS B 2 166 ? 69.118  24.316  13.364  1.00 16.13 ? 167  LYS B C   1 
ATOM   3281 O  O   . LYS B 2 166 ? 68.038  23.745  13.181  1.00 15.89 ? 167  LYS B O   1 
ATOM   3282 C  CB  . LYS B 2 166 ? 70.119  24.091  15.727  1.00 15.01 ? 167  LYS B CB  1 
ATOM   3283 C  CG  . LYS B 2 166 ? 69.930  25.571  15.976  1.00 17.59 ? 167  LYS B CG  1 
ATOM   3284 C  CD  . LYS B 2 166 ? 69.683  25.880  17.478  1.00 18.39 ? 167  LYS B CD  1 
ATOM   3285 C  CE  . LYS B 2 166 ? 69.598  27.416  17.687  1.00 19.34 ? 167  LYS B CE  1 
ATOM   3286 N  NZ  . LYS B 2 166 ? 68.419  28.013  16.994  1.00 20.22 ? 167  LYS B NZ  1 
ATOM   3287 N  N   . ASP B 2 167 ? 69.350  25.516  12.820  1.00 16.25 ? 168  ASP B N   1 
ATOM   3288 C  CA  . ASP B 2 167 ? 68.341  26.198  12.020  1.00 16.58 ? 168  ASP B CA  1 
ATOM   3289 C  C   . ASP B 2 167 ? 68.155  25.515  10.674  1.00 16.58 ? 168  ASP B C   1 
ATOM   3290 O  O   . ASP B 2 167 ? 67.049  25.459  10.136  1.00 16.46 ? 168  ASP B O   1 
ATOM   3291 C  CB  . ASP B 2 167 ? 68.783  27.652  11.893  1.00 16.38 ? 168  ASP B CB  1 
ATOM   3292 C  CG  . ASP B 2 167 ? 69.174  28.207  13.266  1.00 17.53 ? 168  ASP B CG  1 
ATOM   3293 O  OD1 . ASP B 2 167 ? 68.259  28.423  14.109  1.00 18.70 ? 168  ASP B OD1 1 
ATOM   3294 O  OD2 . ASP B 2 167 ? 70.386  28.378  13.545  1.00 16.92 ? 168  ASP B OD2 1 
ATOM   3295 N  N   . ALA B 2 168 ? 69.251  24.993  10.134  1.00 15.37 ? 169  ALA B N   1 
ATOM   3296 C  CA  . ALA B 2 168 ? 69.164  24.213  8.892   1.00 15.63 ? 169  ALA B CA  1 
ATOM   3297 C  C   . ALA B 2 168 ? 68.419  22.885  9.155   1.00 16.22 ? 169  ALA B C   1 
ATOM   3298 O  O   . ALA B 2 168 ? 67.628  22.429  8.293   1.00 16.54 ? 169  ALA B O   1 
ATOM   3299 C  CB  . ALA B 2 168 ? 70.611  23.948  8.363   1.00 13.79 ? 169  ALA B CB  1 
ATOM   3300 N  N   . CYS B 2 169 ? 68.636  22.297  10.340  1.00 14.71 ? 170  CYS B N   1 
ATOM   3301 C  CA  . CYS B 2 169 ? 67.947  21.062  10.753  1.00 16.05 ? 170  CYS B CA  1 
ATOM   3302 C  C   . CYS B 2 169 ? 66.460  21.343  10.781  1.00 17.00 ? 170  CYS B C   1 
ATOM   3303 O  O   . CYS B 2 169 ? 65.632  20.562  10.263  1.00 16.62 ? 170  CYS B O   1 
ATOM   3304 C  CB  . CYS B 2 169 ? 68.385  20.611  12.154  1.00 15.13 ? 170  CYS B CB  1 
ATOM   3305 S  SG  . CYS B 2 169 ? 70.044  19.870  12.283  1.00 18.62 ? 170  CYS B SG  1 
ATOM   3306 N  N   . ASN B 2 170 ? 66.083  22.477  11.396  1.00 15.41 ? 171  ASN B N   1 
ATOM   3307 C  CA  . ASN B 2 170 ? 64.657  22.843  11.418  1.00 16.38 ? 171  ASN B CA  1 
ATOM   3308 C  C   . ASN B 2 170 ? 64.065  22.988  10.017  1.00 16.65 ? 171  ASN B C   1 
ATOM   3309 O  O   . ASN B 2 170 ? 62.945  22.505  9.753   1.00 16.51 ? 171  ASN B O   1 
ATOM   3310 C  CB  . ASN B 2 170 ? 64.412  24.203  12.102  1.00 17.45 ? 171  ASN B CB  1 
ATOM   3311 C  CG  . ASN B 2 170 ? 64.903  24.266  13.525  1.00 19.45 ? 171  ASN B CG  1 
ATOM   3312 O  OD1 . ASN B 2 170 ? 64.996  23.259  14.222  1.00 19.20 ? 171  ASN B OD1 1 
ATOM   3313 N  ND2 . ASN B 2 170 ? 65.222  25.487  13.971  1.00 17.71 ? 171  ASN B ND2 1 
ATOM   3314 N  N   . GLU B 2 171 ? 64.787  23.673  9.123   1.00 15.50 ? 172  GLU B N   1 
ATOM   3315 C  CA  . GLU B 2 171 ? 64.283  23.937  7.787   1.00 17.20 ? 172  GLU B CA  1 
ATOM   3316 C  C   . GLU B 2 171 ? 64.120  22.663  6.990   1.00 16.93 ? 172  GLU B C   1 
ATOM   3317 O  O   . GLU B 2 171 ? 63.130  22.481  6.248   1.00 16.28 ? 172  GLU B O   1 
ATOM   3318 C  CB  . GLU B 2 171 ? 65.181  24.944  7.052   1.00 17.11 ? 172  GLU B CB  1 
ATOM   3319 C  CG  . GLU B 2 171 ? 64.483  25.528  5.830   1.00 18.63 ? 172  GLU B CG  1 
ATOM   3320 C  CD  . GLU B 2 171 ? 63.362  26.501  6.172   1.00 21.38 ? 172  GLU B CD  1 
ATOM   3321 O  OE1 . GLU B 2 171 ? 63.258  26.910  7.365   1.00 20.53 ? 172  GLU B OE1 1 
ATOM   3322 O  OE2 . GLU B 2 171 ? 62.595  26.874  5.242   1.00 24.60 ? 172  GLU B OE2 1 
ATOM   3323 N  N   . ALA B 2 172 ? 65.072  21.757  7.178   1.00 16.47 ? 173  ALA B N   1 
ATOM   3324 C  CA  . ALA B 2 172 ? 64.957  20.481  6.499   1.00 15.93 ? 173  ALA B CA  1 
ATOM   3325 C  C   . ALA B 2 172 ? 63.680  19.781  6.933   1.00 16.21 ? 173  ALA B C   1 
ATOM   3326 O  O   . ALA B 2 172 ? 62.978  19.173  6.100   1.00 15.44 ? 173  ALA B O   1 
ATOM   3327 C  CB  . ALA B 2 172 ? 66.190  19.583  6.793   1.00 18.08 ? 173  ALA B CB  1 
ATOM   3328 N  N   . LEU B 2 173 ? 63.381  19.811  8.238   1.00 15.34 ? 174  LEU B N   1 
ATOM   3329 C  CA  . LEU B 2 173 ? 62.177  19.137  8.712   1.00 15.60 ? 174  LEU B CA  1 
ATOM   3330 C  C   . LEU B 2 173 ? 60.924  19.859  8.243   1.00 13.75 ? 174  LEU B C   1 
ATOM   3331 O  O   . LEU B 2 173 ? 59.922  19.195  7.998   1.00 15.15 ? 174  LEU B O   1 
ATOM   3332 C  CB  . LEU B 2 173 ? 62.195  18.998  10.269  1.00 16.01 ? 174  LEU B CB  1 
ATOM   3333 C  CG  . LEU B 2 173 ? 63.147  17.889  10.821  1.00 19.48 ? 174  LEU B CG  1 
ATOM   3334 C  CD1 . LEU B 2 173 ? 63.245  17.934  12.395  1.00 20.10 ? 174  LEU B CD1 1 
ATOM   3335 C  CD2 . LEU B 2 173 ? 62.612  16.511  10.435  1.00 20.63 ? 174  LEU B CD2 1 
ATOM   3336 N  N   . ARG B 2 174 ? 60.951  21.183  8.118   1.00 13.85 ? 175  ARG B N   1 
ATOM   3337 C  CA  . ARG B 2 174 ? 59.778  21.933  7.630   1.00 14.84 ? 175  ARG B CA  1 
ATOM   3338 C  C   . ARG B 2 174 ? 59.489  21.524  6.202   1.00 13.51 ? 175  ARG B C   1 
ATOM   3339 O  O   . ARG B 2 174 ? 58.341  21.314  5.803   1.00 14.41 ? 175  ARG B O   1 
ATOM   3340 C  CB  . ARG B 2 174 ? 60.019  23.470  7.654   1.00 14.44 ? 175  ARG B CB  1 
ATOM   3341 C  CG  . ARG B 2 174 ? 60.160  24.055  9.115   1.00 15.61 ? 175  ARG B CG  1 
ATOM   3342 C  CD  . ARG B 2 174 ? 60.374  25.550  9.040   1.00 15.27 ? 175  ARG B CD  1 
ATOM   3343 N  NE  . ARG B 2 174 ? 60.536  26.130  10.373  1.00 15.21 ? 175  ARG B NE  1 
ATOM   3344 C  CZ  . ARG B 2 174 ? 61.651  26.680  10.842  1.00 15.49 ? 175  ARG B CZ  1 
ATOM   3345 N  NH1 . ARG B 2 174 ? 62.776  26.755  10.078  1.00 16.23 ? 175  ARG B NH1 1 
ATOM   3346 N  NH2 . ARG B 2 174 ? 61.652  27.126  12.110  1.00 14.62 ? 175  ARG B NH2 1 
ATOM   3347 N  N   . ASP B 2 175 ? 60.540  21.420  5.406   1.00 15.25 ? 176  ASP B N   1 
ATOM   3348 C  CA  . ASP B 2 175 ? 60.389  21.018  4.006   1.00 14.35 ? 176  ASP B CA  1 
ATOM   3349 C  C   . ASP B 2 175 ? 59.835  19.623  3.915   1.00 15.59 ? 176  ASP B C   1 
ATOM   3350 O  O   . ASP B 2 175 ? 58.819  19.370  3.240   1.00 16.40 ? 176  ASP B O   1 
ATOM   3351 C  CB  . ASP B 2 175 ? 61.784  21.112  3.362   1.00 14.88 ? 176  ASP B CB  1 
ATOM   3352 C  CG  . ASP B 2 175 ? 61.800  20.744  1.882   1.00 15.65 ? 176  ASP B CG  1 
ATOM   3353 O  OD1 . ASP B 2 175 ? 60.901  20.018  1.407   1.00 17.20 ? 176  ASP B OD1 1 
ATOM   3354 O  OD2 . ASP B 2 175 ? 62.757  21.170  1.218   1.00 16.93 ? 176  ASP B OD2 1 
ATOM   3355 N  N   . TRP B 2 176 ? 60.449  18.696  4.660   1.00 15.04 ? 177  TRP B N   1 
ATOM   3356 C  CA  . TRP B 2 176 ? 60.001  17.311  4.651   1.00 14.31 ? 177  TRP B CA  1 
ATOM   3357 C  C   . TRP B 2 176 ? 58.547  17.158  5.082   1.00 13.59 ? 177  TRP B C   1 
ATOM   3358 O  O   . TRP B 2 176 ? 57.841  16.286  4.578   1.00 13.34 ? 177  TRP B O   1 
ATOM   3359 C  CB  . TRP B 2 176 ? 60.918  16.467  5.546   1.00 13.30 ? 177  TRP B CB  1 
ATOM   3360 C  CG  . TRP B 2 176 ? 60.933  14.998  5.208   1.00 13.72 ? 177  TRP B CG  1 
ATOM   3361 C  CD1 . TRP B 2 176 ? 60.845  14.440  3.963   1.00 13.51 ? 177  TRP B CD1 1 
ATOM   3362 C  CD2 . TRP B 2 176 ? 61.120  13.911  6.121   1.00 13.06 ? 177  TRP B CD2 1 
ATOM   3363 N  NE1 . TRP B 2 176 ? 60.966  13.071  4.045   1.00 14.02 ? 177  TRP B NE1 1 
ATOM   3364 C  CE2 . TRP B 2 176 ? 61.136  12.720  5.358   1.00 12.76 ? 177  TRP B CE2 1 
ATOM   3365 C  CE3 . TRP B 2 176 ? 61.278  13.826  7.511   1.00 13.33 ? 177  TRP B CE3 1 
ATOM   3366 C  CZ2 . TRP B 2 176 ? 61.305  11.458  5.940   1.00 15.19 ? 177  TRP B CZ2 1 
ATOM   3367 C  CZ3 . TRP B 2 176 ? 61.446  12.571  8.090   1.00 14.41 ? 177  TRP B CZ3 1 
ATOM   3368 C  CH2 . TRP B 2 176 ? 61.457  11.405  7.304   1.00 14.67 ? 177  TRP B CH2 1 
ATOM   3369 N  N   . SER B 2 177 ? 58.102  18.035  6.009   1.00 14.46 ? 178  SER B N   1 
ATOM   3370 C  CA  . SER B 2 177 ? 56.711  17.971  6.460   1.00 14.78 ? 178  SER B CA  1 
ATOM   3371 C  C   . SER B 2 177 ? 55.706  18.237  5.352   1.00 15.55 ? 178  SER B C   1 
ATOM   3372 O  O   . SER B 2 177 ? 54.548  17.823  5.467   1.00 16.25 ? 178  SER B O   1 
ATOM   3373 C  CB  . SER B 2 177 ? 56.442  18.908  7.664   1.00 16.04 ? 178  SER B CB  1 
ATOM   3374 O  OG  A SER B 2 177 ? 56.446  20.251  7.300   0.60 18.59 ? 178  SER B OG  1 
ATOM   3375 O  OG  B SER B 2 177 ? 57.238  18.572  8.767   0.40 14.78 ? 178  SER B OG  1 
ATOM   3376 N  N   . GLY B 2 178 ? 56.155  18.807  4.239   1.00 15.89 ? 179  GLY B N   1 
ATOM   3377 C  CA  . GLY B 2 178 ? 55.250  19.012  3.133   1.00 15.77 ? 179  GLY B CA  1 
ATOM   3378 C  C   . GLY B 2 178 ? 55.669  18.240  1.882   1.00 17.96 ? 179  GLY B C   1 
ATOM   3379 O  O   . GLY B 2 178 ? 54.909  18.196  0.913   1.00 20.31 ? 179  GLY B O   1 
ATOM   3380 N  N   . SER B 2 179 ? 56.843  17.612  1.888   1.00 15.81 ? 180  SER B N   1 
ATOM   3381 C  CA  . SER B 2 179 ? 57.333  16.958  0.661   1.00 16.11 ? 180  SER B CA  1 
ATOM   3382 C  C   . SER B 2 179 ? 57.668  15.485  0.824   1.00 16.36 ? 180  SER B C   1 
ATOM   3383 O  O   . SER B 2 179 ? 58.205  14.870  -0.093  1.00 15.66 ? 180  SER B O   1 
ATOM   3384 C  CB  . SER B 2 179 ? 58.585  17.687  0.189   1.00 17.22 ? 180  SER B CB  1 
ATOM   3385 O  OG  . SER B 2 179 ? 59.670  17.485  1.086   1.00 16.22 ? 180  SER B OG  1 
ATOM   3386 N  N   . TYR B 2 180 ? 57.401  14.915  1.995   1.00 16.05 ? 181  TYR B N   1 
ATOM   3387 C  CA  . TYR B 2 180 ? 57.737  13.520  2.275   1.00 15.77 ? 181  TYR B CA  1 
ATOM   3388 C  C   . TYR B 2 180 ? 57.230  12.503  1.253   1.00 17.50 ? 181  TYR B C   1 
ATOM   3389 O  O   . TYR B 2 180 ? 57.780  11.408  1.143   1.00 16.25 ? 181  TYR B O   1 
ATOM   3390 C  CB  . TYR B 2 180 ? 57.239  13.120  3.672   1.00 17.48 ? 181  TYR B CB  1 
ATOM   3391 C  CG  . TYR B 2 180 ? 55.751  13.303  3.873   1.00 18.12 ? 181  TYR B CG  1 
ATOM   3392 C  CD1 . TYR B 2 180 ? 55.228  14.529  4.287   1.00 20.57 ? 181  TYR B CD1 1 
ATOM   3393 C  CD2 . TYR B 2 180 ? 54.861  12.260  3.614   1.00 21.15 ? 181  TYR B CD2 1 
ATOM   3394 C  CE1 . TYR B 2 180 ? 53.854  14.714  4.436   1.00 21.99 ? 181  TYR B CE1 1 
ATOM   3395 C  CE2 . TYR B 2 180 ? 53.484  12.436  3.759   1.00 22.95 ? 181  TYR B CE2 1 
ATOM   3396 C  CZ  . TYR B 2 180 ? 52.990  13.664  4.169   1.00 22.76 ? 181  TYR B CZ  1 
ATOM   3397 O  OH  . TYR B 2 180 ? 51.631  13.848  4.300   1.00 26.66 ? 181  TYR B OH  1 
ATOM   3398 N  N   . GLU B 2 181 ? 56.187  12.861  0.485   1.00 16.01 ? 182  GLU B N   1 
ATOM   3399 C  CA  . GLU B 2 181 ? 55.697  11.853  -0.454  1.00 19.52 ? 182  GLU B CA  1 
ATOM   3400 C  C   . GLU B 2 181 ? 56.698  11.594  -1.566  1.00 18.95 ? 182  GLU B C   1 
ATOM   3401 O  O   . GLU B 2 181 ? 56.696  10.501  -2.124  1.00 20.61 ? 182  GLU B O   1 
ATOM   3402 C  CB  . GLU B 2 181 ? 54.376  12.277  -1.088  1.00 21.68 ? 182  GLU B CB  1 
ATOM   3403 C  CG  . GLU B 2 181 ? 53.234  12.254  -0.109  1.00 27.33 ? 182  GLU B CG  1 
ATOM   3404 C  CD  A GLU B 2 181 ? 51.958  12.802  -0.711  0.50 28.63 ? 182  GLU B CD  1 
ATOM   3405 C  CD  B GLU B 2 181 ? 52.902  10.836  0.350   0.50 28.36 ? 182  GLU B CD  1 
ATOM   3406 O  OE1 A GLU B 2 181 ? 51.996  13.924  -1.274  0.50 31.91 ? 182  GLU B OE1 1 
ATOM   3407 O  OE1 B GLU B 2 181 ? 52.825  9.912   -0.501  0.50 31.02 ? 182  GLU B OE1 1 
ATOM   3408 O  OE2 A GLU B 2 181 ? 50.923  12.113  -0.609  0.50 30.26 ? 182  GLU B OE2 1 
ATOM   3409 O  OE2 B GLU B 2 181 ? 52.710  10.635  1.561   0.50 30.67 ? 182  GLU B OE2 1 
ATOM   3410 N  N   . THR B 2 182 ? 57.523  12.585  -1.895  1.00 18.05 ? 183  THR B N   1 
ATOM   3411 C  CA  . THR B 2 182 ? 58.478  12.397  -2.982  1.00 18.73 ? 183  THR B CA  1 
ATOM   3412 C  C   . THR B 2 182 ? 59.956  12.523  -2.523  1.00 17.33 ? 183  THR B C   1 
ATOM   3413 O  O   . THR B 2 182 ? 60.865  12.121  -3.257  1.00 15.25 ? 183  THR B O   1 
ATOM   3414 C  CB  . THR B 2 182 ? 58.219  13.439  -4.121  1.00 21.06 ? 183  THR B CB  1 
ATOM   3415 O  OG1 . THR B 2 182 ? 58.269  14.756  -3.589  1.00 23.44 ? 183  THR B OG1 1 
ATOM   3416 C  CG2 . THR B 2 182 ? 56.814  13.228  -4.751  1.00 23.00 ? 183  THR B CG2 1 
ATOM   3417 N  N   . ALA B 2 183 ? 60.192  13.074  -1.309  1.00 15.02 ? 184  ALA B N   1 
ATOM   3418 C  CA  . ALA B 2 183 ? 61.577  13.317  -0.869  1.00 13.70 ? 184  ALA B CA  1 
ATOM   3419 C  C   . ALA B 2 183 ? 61.874  12.535  0.392   1.00 12.11 ? 184  ALA B C   1 
ATOM   3420 O  O   . ALA B 2 183 ? 61.010  12.287  1.223   1.00 13.89 ? 184  ALA B O   1 
ATOM   3421 C  CB  . ALA B 2 183 ? 61.781  14.777  -0.542  1.00 13.43 ? 184  ALA B CB  1 
ATOM   3422 N  N   . HIS B 2 184 ? 63.155  12.148  0.477   1.00 12.64 ? 185  HIS B N   1 
ATOM   3423 C  CA  . HIS B 2 184 ? 63.665  11.469  1.659   1.00 11.53 ? 185  HIS B CA  1 
ATOM   3424 C  C   . HIS B 2 184 ? 64.602  12.435  2.370   1.00 10.64 ? 185  HIS B C   1 
ATOM   3425 O  O   . HIS B 2 184 ? 65.410  13.111  1.730   1.00 11.68 ? 185  HIS B O   1 
ATOM   3426 C  CB  . HIS B 2 184 ? 64.462  10.216  1.292   1.00 12.39 ? 185  HIS B CB  1 
ATOM   3427 C  CG  . HIS B 2 184 ? 65.209  9.630   2.450   1.00 11.41 ? 185  HIS B CG  1 
ATOM   3428 N  ND1 . HIS B 2 184 ? 64.575  9.190   3.592   1.00 11.83 ? 185  HIS B ND1 1 
ATOM   3429 C  CD2 . HIS B 2 184 ? 66.536  9.481   2.675   1.00 12.57 ? 185  HIS B CD2 1 
ATOM   3430 C  CE1 . HIS B 2 184 ? 65.480  8.798   4.473   1.00 12.17 ? 185  HIS B CE1 1 
ATOM   3431 N  NE2 . HIS B 2 184 ? 66.678  8.964   3.941   1.00 11.43 ? 185  HIS B NE2 1 
ATOM   3432 N  N   . TYR B 2 185 ? 64.497  12.501  3.693   1.00 10.96 ? 186  TYR B N   1 
ATOM   3433 C  CA  . TYR B 2 185 ? 65.368  13.373  4.464   1.00 12.33 ? 186  TYR B CA  1 
ATOM   3434 C  C   . TYR B 2 185 ? 66.606  12.584  4.890   1.00 10.80 ? 186  TYR B C   1 
ATOM   3435 O  O   . TYR B 2 185 ? 66.535  11.699  5.740   1.00 10.88 ? 186  TYR B O   1 
ATOM   3436 C  CB  . TYR B 2 185 ? 64.627  13.925  5.686   1.00 13.49 ? 186  TYR B CB  1 
ATOM   3437 C  CG  . TYR B 2 185 ? 65.512  14.720  6.618   1.00 14.23 ? 186  TYR B CG  1 
ATOM   3438 C  CD1 . TYR B 2 185 ? 66.525  15.538  6.118   1.00 14.69 ? 186  TYR B CD1 1 
ATOM   3439 C  CD2 . TYR B 2 185 ? 65.341  14.651  7.999   1.00 15.17 ? 186  TYR B CD2 1 
ATOM   3440 C  CE1 . TYR B 2 185 ? 67.347  16.267  6.967   1.00 14.92 ? 186  TYR B CE1 1 
ATOM   3441 C  CE2 . TYR B 2 185 ? 66.160  15.381  8.861   1.00 16.47 ? 186  TYR B CE2 1 
ATOM   3442 C  CZ  . TYR B 2 185 ? 67.160  16.185  8.335   1.00 16.70 ? 186  TYR B CZ  1 
ATOM   3443 O  OH  . TYR B 2 185 ? 67.980  16.908  9.170   1.00 18.35 ? 186  TYR B OH  1 
ATOM   3444 N  N   . MET B 2 186 ? 67.724  12.924  4.295   1.00 9.59  ? 187  MET B N   1 
ATOM   3445 C  CA  . MET B 2 186 ? 69.010  12.220  4.548   1.00 10.69 ? 187  MET B CA  1 
ATOM   3446 C  C   . MET B 2 186 ? 69.712  12.955  5.715   1.00 10.41 ? 187  MET B C   1 
ATOM   3447 O  O   . MET B 2 186 ? 70.578  13.818  5.498   1.00 11.27 ? 187  MET B O   1 
ATOM   3448 C  CB  . MET B 2 186 ? 69.865  12.274  3.261   1.00 11.97 ? 187  MET B CB  1 
ATOM   3449 C  CG  . MET B 2 186 ? 71.179  11.468  3.318   1.00 14.42 ? 187  MET B CG  1 
ATOM   3450 S  SD  . MET B 2 186 ? 72.066  11.587  1.687   1.00 17.50 ? 187  MET B SD  1 
ATOM   3451 C  CE  . MET B 2 186 ? 71.164  10.252  0.778   1.00 16.54 ? 187  MET B CE  1 
ATOM   3452 N  N   . LEU B 2 187 ? 69.366  12.556  6.940   1.00 9.54  ? 188  LEU B N   1 
ATOM   3453 C  CA  . LEU B 2 187 ? 69.886  13.163  8.171   1.00 9.83  ? 188  LEU B CA  1 
ATOM   3454 C  C   . LEU B 2 187 ? 71.365  12.828  8.252   1.00 9.14  ? 188  LEU B C   1 
ATOM   3455 O  O   . LEU B 2 187 ? 71.768  11.723  7.889   1.00 11.42 ? 188  LEU B O   1 
ATOM   3456 C  CB  . LEU B 2 187 ? 69.052  12.628  9.376   1.00 11.57 ? 188  LEU B CB  1 
ATOM   3457 C  CG  . LEU B 2 187 ? 68.911  13.549  10.577  1.00 16.04 ? 188  LEU B CG  1 
ATOM   3458 C  CD1 . LEU B 2 187 ? 67.624  13.107  11.356  1.00 13.74 ? 188  LEU B CD1 1 
ATOM   3459 C  CD2 . LEU B 2 187 ? 70.162  13.548  11.455  1.00 16.36 ? 188  LEU B CD2 1 
ATOM   3460 N  N   . GLY B 2 188 ? 72.142  13.772  8.776   1.00 7.76  ? 189  GLY B N   1 
ATOM   3461 C  CA  . GLY B 2 188 ? 73.571  13.614  8.783   1.00 9.40  ? 189  GLY B CA  1 
ATOM   3462 C  C   . GLY B 2 188 ? 74.331  13.024  9.929   1.00 10.71 ? 189  GLY B C   1 
ATOM   3463 O  O   . GLY B 2 188 ? 75.569  13.003  9.920   1.00 10.22 ? 189  GLY B O   1 
ATOM   3464 N  N   . THR B 2 189 ? 73.620  12.598  10.965  1.00 9.95  ? 190  THR B N   1 
ATOM   3465 C  CA  . THR B 2 189 ? 74.342  12.021  12.093  1.00 9.30  ? 190  THR B CA  1 
ATOM   3466 C  C   . THR B 2 189 ? 73.444  10.947  12.773  1.00 8.28  ? 190  THR B C   1 
ATOM   3467 O  O   . THR B 2 189 ? 72.300  10.778  12.377  1.00 9.26  ? 190  THR B O   1 
ATOM   3468 C  CB  . THR B 2 189 ? 74.792  13.125  13.115  1.00 7.86  ? 190  THR B CB  1 
ATOM   3469 O  OG1 . THR B 2 189 ? 75.688  12.509  14.075  1.00 8.00  ? 190  THR B OG1 1 
ATOM   3470 C  CG2 . THR B 2 189 ? 73.616  13.804  13.833  1.00 8.41  ? 190  THR B CG2 1 
ATOM   3471 N  N   . ALA B 2 190 ? 73.970  10.281  13.812  1.00 7.64  ? 191  ALA B N   1 
ATOM   3472 C  CA  . ALA B 2 190 ? 73.192  9.246   14.539  1.00 8.19  ? 191  ALA B CA  1 
ATOM   3473 C  C   . ALA B 2 190 ? 72.331  9.879   15.634  1.00 6.99  ? 191  ALA B C   1 
ATOM   3474 O  O   . ALA B 2 190 ? 72.449  9.606   16.817  1.00 8.51  ? 191  ALA B O   1 
ATOM   3475 C  CB  . ALA B 2 190 ? 74.206  8.247   15.168  1.00 8.01  ? 191  ALA B CB  1 
ATOM   3476 N  N   . ALA B 2 191 ? 71.460  10.785  15.187  1.00 7.91  ? 192  ALA B N   1 
ATOM   3477 C  CA  . ALA B 2 191 ? 70.595  11.528  16.103  1.00 8.70  ? 192  ALA B CA  1 
ATOM   3478 C  C   . ALA B 2 191 ? 69.317  11.829  15.367  1.00 8.67  ? 192  ALA B C   1 
ATOM   3479 O  O   . ALA B 2 191 ? 69.095  11.313  14.241  1.00 9.11  ? 192  ALA B O   1 
ATOM   3480 C  CB  . ALA B 2 191 ? 71.301  12.836  16.563  1.00 8.68  ? 192  ALA B CB  1 
ATOM   3481 N  N   . GLY B 2 192 ? 68.464  12.660  15.951  1.00 7.68  ? 193  GLY B N   1 
ATOM   3482 C  CA  . GLY B 2 192 ? 67.162  12.897  15.345  1.00 8.62  ? 193  GLY B CA  1 
ATOM   3483 C  C   . GLY B 2 192 ? 66.139  11.827  15.775  1.00 7.11  ? 193  GLY B C   1 
ATOM   3484 O  O   . GLY B 2 192 ? 66.393  11.010  16.658  1.00 7.79  ? 193  GLY B O   1 
ATOM   3485 N  N   . PRO B 2 193 ? 64.941  11.853  15.200  1.00 7.38  ? 194  PRO B N   1 
ATOM   3486 C  CA  . PRO B 2 193 ? 63.913  10.885  15.561  1.00 7.59  ? 194  PRO B CA  1 
ATOM   3487 C  C   . PRO B 2 193 ? 64.216  9.487   15.055  1.00 6.88  ? 194  PRO B C   1 
ATOM   3488 O  O   . PRO B 2 193 ? 64.824  9.307   13.991  1.00 8.25  ? 194  PRO B O   1 
ATOM   3489 C  CB  . PRO B 2 193 ? 62.654  11.457  14.877  1.00 7.05  ? 194  PRO B CB  1 
ATOM   3490 C  CG  . PRO B 2 193 ? 63.181  12.111  13.607  1.00 8.26  ? 194  PRO B CG  1 
ATOM   3491 C  CD  . PRO B 2 193 ? 64.545  12.725  14.067  1.00 8.08  ? 194  PRO B CD  1 
ATOM   3492 N  N   . HIS B 2 194 ? 63.686  8.500   15.771  1.00 7.60  ? 195  HIS B N   1 
ATOM   3493 C  CA  . HIS B 2 194 ? 63.799  7.111   15.347  1.00 8.39  ? 195  HIS B CA  1 
ATOM   3494 C  C   . HIS B 2 194 ? 63.109  7.116   13.979  1.00 9.62  ? 195  HIS B C   1 
ATOM   3495 O  O   . HIS B 2 194 ? 62.091  7.782   13.800  1.00 9.74  ? 195  HIS B O   1 
ATOM   3496 C  CB  . HIS B 2 194 ? 63.035  6.216   16.324  1.00 8.36  ? 195  HIS B CB  1 
ATOM   3497 C  CG  . HIS B 2 194 ? 62.973  4.778   15.916  1.00 8.90  ? 195  HIS B CG  1 
ATOM   3498 N  ND1 . HIS B 2 194 ? 64.055  3.932   16.009  1.00 8.02  ? 195  HIS B ND1 1 
ATOM   3499 C  CD2 . HIS B 2 194 ? 61.952  4.034   15.427  1.00 11.45 ? 195  HIS B CD2 1 
ATOM   3500 C  CE1 . HIS B 2 194 ? 63.705  2.725   15.595  1.00 10.01 ? 195  HIS B CE1 1 
ATOM   3501 N  NE2 . HIS B 2 194 ? 62.434  2.761   15.236  1.00 10.28 ? 195  HIS B NE2 1 
ATOM   3502 N  N   . PRO B 2 195 ? 63.583  6.354   13.001  1.00 8.78  ? 196  PRO B N   1 
ATOM   3503 C  CA  . PRO B 2 195 ? 64.702  5.423   13.058  1.00 8.90  ? 196  PRO B CA  1 
ATOM   3504 C  C   . PRO B 2 195 ? 66.092  5.859   12.765  1.00 7.54  ? 196  PRO B C   1 
ATOM   3505 O  O   . PRO B 2 195 ? 66.983  5.035   12.657  1.00 7.96  ? 196  PRO B O   1 
ATOM   3506 C  CB  . PRO B 2 195 ? 64.230  4.340   12.064  1.00 8.68  ? 196  PRO B CB  1 
ATOM   3507 C  CG  . PRO B 2 195 ? 63.677  5.228   10.933  1.00 8.67  ? 196  PRO B CG  1 
ATOM   3508 C  CD  . PRO B 2 195 ? 62.876  6.296   11.685  1.00 8.49  ? 196  PRO B CD  1 
ATOM   3509 N  N   . TYR B 2 196 ? 66.316  7.150   12.599  1.00 8.59  ? 197  TYR B N   1 
ATOM   3510 C  CA  . TYR B 2 196 ? 67.644  7.630   12.216  1.00 7.57  ? 197  TYR B CA  1 
ATOM   3511 C  C   . TYR B 2 196 ? 68.853  7.219   13.069  1.00 7.24  ? 197  TYR B C   1 
ATOM   3512 O  O   . TYR B 2 196 ? 69.874  6.803   12.523  1.00 7.63  ? 197  TYR B O   1 
ATOM   3513 C  CB  . TYR B 2 196 ? 67.616  9.149   12.018  1.00 7.78  ? 197  TYR B CB  1 
ATOM   3514 C  CG  . TYR B 2 196 ? 66.859  9.563   10.772  1.00 8.62  ? 197  TYR B CG  1 
ATOM   3515 C  CD1 . TYR B 2 196 ? 67.429  9.422   9.505   1.00 7.93  ? 197  TYR B CD1 1 
ATOM   3516 C  CD2 . TYR B 2 196 ? 65.569  10.079  10.859  1.00 8.96  ? 197  TYR B CD2 1 
ATOM   3517 C  CE1 . TYR B 2 196 ? 66.730  9.793   8.351   1.00 9.49  ? 197  TYR B CE1 1 
ATOM   3518 C  CE2 . TYR B 2 196 ? 64.861  10.449  9.716   1.00 9.98  ? 197  TYR B CE2 1 
ATOM   3519 C  CZ  . TYR B 2 196 ? 65.445  10.307  8.469   1.00 8.93  ? 197  TYR B CZ  1 
ATOM   3520 O  OH  . TYR B 2 196 ? 64.740  10.694  7.351   1.00 11.07 ? 197  TYR B OH  1 
ATOM   3521 N  N   . PRO B 2 197 ? 68.773  7.286   14.421  1.00 7.52  ? 198  PRO B N   1 
ATOM   3522 C  CA  . PRO B 2 197 ? 69.958  6.884   15.186  1.00 7.57  ? 198  PRO B CA  1 
ATOM   3523 C  C   . PRO B 2 197 ? 70.328  5.444   14.907  1.00 7.14  ? 198  PRO B C   1 
ATOM   3524 O  O   . PRO B 2 197 ? 71.498  5.084   14.878  1.00 8.19  ? 198  PRO B O   1 
ATOM   3525 C  CB  . PRO B 2 197 ? 69.551  7.124   16.664  1.00 6.87  ? 198  PRO B CB  1 
ATOM   3526 C  CG  . PRO B 2 197 ? 68.569  8.252   16.554  1.00 8.23  ? 198  PRO B CG  1 
ATOM   3527 C  CD  . PRO B 2 197 ? 67.761  7.955   15.271  1.00 9.18  ? 198  PRO B CD  1 
ATOM   3528 N  N   . THR B 2 198 ? 69.327  4.610   14.716  1.00 6.74  ? 199  THR B N   1 
ATOM   3529 C  CA  . THR B 2 198 ? 69.563  3.208   14.439  1.00 7.15  ? 199  THR B CA  1 
ATOM   3530 C  C   . THR B 2 198 ? 70.087  2.982   13.004  1.00 7.63  ? 199  THR B C   1 
ATOM   3531 O  O   . THR B 2 198 ? 71.072  2.221   12.825  1.00 7.69  ? 199  THR B O   1 
ATOM   3532 C  CB  . THR B 2 198 ? 68.238  2.453   14.614  1.00 7.35  ? 199  THR B CB  1 
ATOM   3533 O  OG1 . THR B 2 198 ? 67.901  2.437   16.031  1.00 9.23  ? 199  THR B OG1 1 
ATOM   3534 C  CG2 . THR B 2 198 ? 68.414  0.973   14.221  1.00 10.02 ? 199  THR B CG2 1 
ATOM   3535 N  N   . ILE B 2 199 ? 69.494  3.658   12.020  1.00 7.89  ? 200  ILE B N   1 
ATOM   3536 C  CA  . ILE B 2 199 ? 69.910  3.485   10.611  1.00 6.56  ? 200  ILE B CA  1 
ATOM   3537 C  C   . ILE B 2 199 ? 71.317  3.963   10.423  1.00 7.64  ? 200  ILE B C   1 
ATOM   3538 O  O   . ILE B 2 199 ? 72.145  3.264   9.819   1.00 8.28  ? 200  ILE B O   1 
ATOM   3539 C  CB  . ILE B 2 199 ? 68.964  4.248   9.713   1.00 7.58  ? 200  ILE B CB  1 
ATOM   3540 C  CG1 . ILE B 2 199 ? 67.604  3.518   9.675   1.00 8.36  ? 200  ILE B CG1 1 
ATOM   3541 C  CG2 . ILE B 2 199 ? 69.523  4.259   8.258   1.00 10.11 ? 200  ILE B CG2 1 
ATOM   3542 C  CD1 . ILE B 2 199 ? 66.561  4.332   8.871   1.00 10.58 ? 200  ILE B CD1 1 
ATOM   3543 N  N   . VAL B 2 200 ? 71.623  5.145   11.003  1.00 6.39  ? 201  VAL B N   1 
ATOM   3544 C  CA  . VAL B 2 200 ? 72.970  5.691   10.790  1.00 7.77  ? 201  VAL B CA  1 
ATOM   3545 C  C   . VAL B 2 200 ? 74.019  4.791   11.454  1.00 7.55  ? 201  VAL B C   1 
ATOM   3546 O  O   . VAL B 2 200 ? 75.109  4.567   10.893  1.00 8.86  ? 201  VAL B O   1 
ATOM   3547 C  CB  . VAL B 2 200 ? 73.006  7.165   11.287  1.00 7.37  ? 201  VAL B CB  1 
ATOM   3548 C  CG1 . VAL B 2 200 ? 74.466  7.708   11.181  1.00 9.08  ? 201  VAL B CG1 1 
ATOM   3549 C  CG2 . VAL B 2 200 ? 72.120  7.992   10.394  1.00 10.21 ? 201  VAL B CG2 1 
ATOM   3550 N  N   . ARG B 2 201 ? 73.757  4.303   12.687  1.00 7.18  ? 202  ARG B N   1 
ATOM   3551 C  CA  . ARG B 2 201 ? 74.707  3.353   13.267  1.00 8.36  ? 202  ARG B CA  1 
ATOM   3552 C  C   . ARG B 2 201 ? 74.900  2.150   12.348  1.00 7.43  ? 202  ARG B C   1 
ATOM   3553 O  O   . ARG B 2 201 ? 76.051  1.761   12.101  1.00 7.57  ? 202  ARG B O   1 
ATOM   3554 C  CB  . ARG B 2 201 ? 74.182  2.851   14.599  1.00 7.92  ? 202  ARG B CB  1 
ATOM   3555 C  CG  . ARG B 2 201 ? 75.080  1.713   15.183  1.00 8.24  ? 202  ARG B CG  1 
ATOM   3556 C  CD  . ARG B 2 201 ? 74.381  1.075   16.403  1.00 9.93  ? 202  ARG B CD  1 
ATOM   3557 N  NE  . ARG B 2 201 ? 73.290  0.167   15.985  1.00 8.98  ? 202  ARG B NE  1 
ATOM   3558 C  CZ  . ARG B 2 201 ? 72.053  0.159   16.469  1.00 9.54  ? 202  ARG B CZ  1 
ATOM   3559 N  NH1 . ARG B 2 201 ? 71.666  1.025   17.420  1.00 10.02 ? 202  ARG B NH1 1 
ATOM   3560 N  NH2 . ARG B 2 201 ? 71.166  -0.746  16.027  1.00 11.17 ? 202  ARG B NH2 1 
ATOM   3561 N  N   . GLU B 2 202 ? 73.808  1.554   11.866  1.00 7.17  ? 203  GLU B N   1 
ATOM   3562 C  CA  . GLU B 2 202 ? 74.000  0.329   11.062  1.00 8.41  ? 203  GLU B CA  1 
ATOM   3563 C  C   . GLU B 2 202 ? 74.704  0.583   9.753   1.00 9.36  ? 203  GLU B C   1 
ATOM   3564 O  O   . GLU B 2 202 ? 75.388  -0.299  9.244   1.00 10.29 ? 203  GLU B O   1 
ATOM   3565 C  CB  . GLU B 2 202 ? 72.616  -0.318  10.806  1.00 8.66  ? 203  GLU B CB  1 
ATOM   3566 C  CG  . GLU B 2 202 ? 72.042  -0.893  12.139  1.00 11.29 ? 203  GLU B CG  1 
ATOM   3567 C  CD  . GLU B 2 202 ? 72.966  -1.932  12.795  1.00 13.04 ? 203  GLU B CD  1 
ATOM   3568 O  OE1 . GLU B 2 202 ? 73.220  -2.964  12.156  1.00 13.72 ? 203  GLU B OE1 1 
ATOM   3569 O  OE2 . GLU B 2 202 ? 73.448  -1.773  13.957  1.00 15.91 ? 203  GLU B OE2 1 
ATOM   3570 N  N   . PHE B 2 203 ? 74.577  1.802   9.227   1.00 7.91  ? 204  PHE B N   1 
ATOM   3571 C  CA  . PHE B 2 203 ? 75.241  2.144   7.975   1.00 7.80  ? 204  PHE B CA  1 
ATOM   3572 C  C   . PHE B 2 203 ? 76.662  2.684   8.189   1.00 7.71  ? 204  PHE B C   1 
ATOM   3573 O  O   . PHE B 2 203 ? 77.325  3.088   7.235   1.00 9.80  ? 204  PHE B O   1 
ATOM   3574 C  CB  . PHE B 2 203 ? 74.405  3.151   7.165   1.00 8.78  ? 204  PHE B CB  1 
ATOM   3575 C  CG  . PHE B 2 203 ? 73.154  2.564   6.549   1.00 8.92  ? 204  PHE B CG  1 
ATOM   3576 C  CD1 . PHE B 2 203 ? 72.955  1.184   6.493   1.00 10.51 ? 204  PHE B CD1 1 
ATOM   3577 C  CD2 . PHE B 2 203 ? 72.189  3.401   5.992   1.00 9.70  ? 204  PHE B CD2 1 
ATOM   3578 C  CE1 . PHE B 2 203 ? 71.810  0.647   5.887   1.00 11.13 ? 204  PHE B CE1 1 
ATOM   3579 C  CE2 . PHE B 2 203 ? 71.046  2.876   5.385   1.00 9.93  ? 204  PHE B CE2 1 
ATOM   3580 C  CZ  . PHE B 2 203 ? 70.857  1.496   5.332   1.00 9.93  ? 204  PHE B CZ  1 
ATOM   3581 N  N   . GLN B 2 204 ? 77.080  2.794   9.471   1.00 6.70  ? 205  GLN B N   1 
ATOM   3582 C  CA  . GLN B 2 204 ? 78.474  3.164   9.780   1.00 7.25  ? 205  GLN B CA  1 
ATOM   3583 C  C   . GLN B 2 204 ? 79.201  2.026   10.532  1.00 7.32  ? 205  GLN B C   1 
ATOM   3584 O  O   . GLN B 2 204 ? 80.410  2.127   10.768  1.00 7.75  ? 205  GLN B O   1 
ATOM   3585 C  CB  . GLN B 2 204 ? 78.571  4.415   10.696  1.00 7.19  ? 205  GLN B CB  1 
ATOM   3586 C  CG  . GLN B 2 204 ? 78.134  5.729   10.022  1.00 6.95  ? 205  GLN B CG  1 
ATOM   3587 C  CD  . GLN B 2 204 ? 79.182  6.165   8.983   1.00 8.25  ? 205  GLN B CD  1 
ATOM   3588 O  OE1 . GLN B 2 204 ? 80.208  5.496   8.835   1.00 7.49  ? 205  GLN B OE1 1 
ATOM   3589 N  NE2 . GLN B 2 204 ? 78.923  7.292   8.294   1.00 7.35  ? 205  GLN B NE2 1 
ATOM   3590 N  N   . ARG B 2 205 ? 78.515  0.905   10.802  1.00 8.53  ? 206  ARG B N   1 
ATOM   3591 C  CA  . ARG B 2 205 ? 79.119  -0.127  11.666  1.00 8.57  ? 206  ARG B CA  1 
ATOM   3592 C  C   . ARG B 2 205 ? 80.271  -0.898  11.025  1.00 7.64  ? 206  ARG B C   1 
ATOM   3593 O  O   . ARG B 2 205 ? 81.018  -1.569  11.745  1.00 7.90  ? 206  ARG B O   1 
ATOM   3594 C  CB  . ARG B 2 205 ? 78.043  -1.074  12.221  1.00 11.42 ? 206  ARG B CB  1 
ATOM   3595 C  CG  . ARG B 2 205 ? 77.499  -1.947  11.284  1.00 15.36 ? 206  ARG B CG  1 
ATOM   3596 C  CD  . ARG B 2 205 ? 76.511  -2.946  12.072  1.00 20.12 ? 206  ARG B CD  1 
ATOM   3597 N  NE  . ARG B 2 205 ? 77.148  -3.698  13.172  1.00 22.28 ? 206  ARG B NE  1 
ATOM   3598 C  CZ  . ARG B 2 205 ? 76.740  -3.770  14.462  1.00 21.99 ? 206  ARG B CZ  1 
ATOM   3599 N  NH1 . ARG B 2 205 ? 75.669  -3.134  14.920  1.00 24.16 ? 206  ARG B NH1 1 
ATOM   3600 N  NH2 . ARG B 2 205 ? 77.410  -4.530  15.325  1.00 23.02 ? 206  ARG B NH2 1 
ATOM   3601 N  N   . MET B 2 206 ? 80.448  -0.737  9.699   1.00 8.08  ? 207  MET B N   1 
ATOM   3602 C  CA  . MET B 2 206 ? 81.591  -1.389  9.085   1.00 8.38  ? 207  MET B CA  1 
ATOM   3603 C  C   . MET B 2 206 ? 82.882  -0.766  9.574   1.00 8.05  ? 207  MET B C   1 
ATOM   3604 O  O   . MET B 2 206 ? 83.920  -1.399  9.479   1.00 8.54  ? 207  MET B O   1 
ATOM   3605 C  CB  . MET B 2 206 ? 81.508  -1.304  7.533   1.00 10.21 ? 207  MET B CB  1 
ATOM   3606 C  CG  . MET B 2 206 ? 81.543  0.135   6.938   1.00 10.34 ? 207  MET B CG  1 
ATOM   3607 S  SD  . MET B 2 206 ? 80.120  1.201   7.210   1.00 10.87 ? 207  MET B SD  1 
ATOM   3608 C  CE  . MET B 2 206 ? 78.862  0.216   6.386   1.00 13.55 ? 207  MET B CE  1 
ATOM   3609 N  N   . ILE B 2 207 ? 82.841  0.448   10.140  1.00 7.77  ? 208  ILE B N   1 
ATOM   3610 C  CA  . ILE B 2 207 ? 84.090  1.026   10.670  1.00 7.32  ? 208  ILE B CA  1 
ATOM   3611 C  C   . ILE B 2 207 ? 84.640  0.102   11.795  1.00 7.90  ? 208  ILE B C   1 
ATOM   3612 O  O   . ILE B 2 207 ? 85.825  -0.336  11.764  1.00 8.25  ? 208  ILE B O   1 
ATOM   3613 C  CB  . ILE B 2 207 ? 83.838  2.441   11.219  1.00 6.92  ? 208  ILE B CB  1 
ATOM   3614 C  CG1 . ILE B 2 207 ? 83.426  3.373   10.070  1.00 9.32  ? 208  ILE B CG1 1 
ATOM   3615 C  CG2 . ILE B 2 207 ? 85.121  2.973   11.880  1.00 7.42  ? 208  ILE B CG2 1 
ATOM   3616 C  CD1 . ILE B 2 207 ? 83.045  4.761   10.520  1.00 8.57  ? 208  ILE B CD1 1 
ATOM   3617 N  N   . GLY B 2 208 ? 83.794  -0.163  12.783  1.00 7.98  ? 209  GLY B N   1 
ATOM   3618 C  CA  . GLY B 2 208 ? 84.244  -1.026  13.865  1.00 7.85  ? 209  GLY B CA  1 
ATOM   3619 C  C   . GLY B 2 208 ? 84.418  -2.492  13.425  1.00 8.86  ? 209  GLY B C   1 
ATOM   3620 O  O   . GLY B 2 208 ? 85.296  -3.163  13.982  1.00 8.08  ? 209  GLY B O   1 
ATOM   3621 N  N   . GLU B 2 209 ? 83.555  -3.006  12.540  1.00 8.60  ? 210  GLU B N   1 
ATOM   3622 C  CA  . GLU B 2 209 ? 83.718  -4.420  12.099  1.00 9.09  ? 210  GLU B CA  1 
ATOM   3623 C  C   . GLU B 2 209 ? 85.098  -4.578  11.421  1.00 8.35  ? 210  GLU B C   1 
ATOM   3624 O  O   . GLU B 2 209 ? 85.818  -5.560  11.647  1.00 9.13  ? 210  GLU B O   1 
ATOM   3625 C  CB  . GLU B 2 209 ? 82.620  -4.766  11.094  1.00 11.80 ? 210  GLU B CB  1 
ATOM   3626 C  CG  . GLU B 2 209 ? 81.304  -4.912  11.730  1.00 13.44 ? 210  GLU B CG  1 
ATOM   3627 C  CD  . GLU B 2 209 ? 80.165  -5.029  10.733  1.00 18.57 ? 210  GLU B CD  1 
ATOM   3628 O  OE1 . GLU B 2 209 ? 80.401  -4.773  9.519   1.00 20.76 ? 210  GLU B OE1 1 
ATOM   3629 O  OE2 . GLU B 2 209 ? 79.016  -5.341  11.207  1.00 19.73 ? 210  GLU B OE2 1 
ATOM   3630 N  N   . GLU B 2 210 ? 85.460  -3.665  10.506  1.00 7.02  ? 211  GLU B N   1 
ATOM   3631 C  CA  . GLU B 2 210 ? 86.779  -3.771  9.858   1.00 7.07  ? 211  GLU B CA  1 
ATOM   3632 C  C   . GLU B 2 210 ? 87.915  -3.629  10.881  1.00 7.80  ? 211  GLU B C   1 
ATOM   3633 O  O   . GLU B 2 210 ? 88.896  -4.398  10.875  1.00 7.89  ? 211  GLU B O   1 
ATOM   3634 C  CB  . GLU B 2 210 ? 86.966  -2.682  8.798   1.00 8.11  ? 211  GLU B CB  1 
ATOM   3635 C  CG  . GLU B 2 210 ? 86.097  -2.919  7.553   1.00 8.94  ? 211  GLU B CG  1 
ATOM   3636 C  CD  . GLU B 2 210 ? 86.205  -1.777  6.569   1.00 9.27  ? 211  GLU B CD  1 
ATOM   3637 O  OE1 . GLU B 2 210 ? 87.119  -0.915  6.680   1.00 8.05  ? 211  GLU B OE1 1 
ATOM   3638 O  OE2 . GLU B 2 210 ? 85.365  -1.759  5.652   1.00 9.49  ? 211  GLU B OE2 1 
ATOM   3639 N  N   . THR B 2 211 ? 87.786  -2.665  11.804  1.00 6.73  ? 212  THR B N   1 
ATOM   3640 C  CA  . THR B 2 211 ? 88.815  -2.407  12.816  1.00 7.12  ? 212  THR B CA  1 
ATOM   3641 C  C   . THR B 2 211 ? 89.018  -3.673  13.645  1.00 8.72  ? 212  THR B C   1 
ATOM   3642 O  O   . THR B 2 211 ? 90.175  -4.026  13.877  1.00 7.86  ? 212  THR B O   1 
ATOM   3643 C  CB  . THR B 2 211 ? 88.390  -1.265  13.778  1.00 8.41  ? 212  THR B CB  1 
ATOM   3644 O  OG1 . THR B 2 211 ? 88.252  -0.044  13.010  1.00 8.18  ? 212  THR B OG1 1 
ATOM   3645 C  CG2 . THR B 2 211 ? 89.444  -1.023  14.902  1.00 8.71  ? 212  THR B CG2 1 
ATOM   3646 N  N   . LYS B 2 212 ? 87.917  -4.348  14.003  1.00 9.18  ? 213  LYS B N   1 
ATOM   3647 C  CA  . LYS B 2 212 ? 88.076  -5.597  14.820  1.00 9.81  ? 213  LYS B CA  1 
ATOM   3648 C  C   . LYS B 2 212 ? 88.856  -6.647  14.013  1.00 10.42 ? 213  LYS B C   1 
ATOM   3649 O  O   . LYS B 2 212 ? 89.822  -7.239  14.533  1.00 10.24 ? 213  LYS B O   1 
ATOM   3650 C  CB  . LYS B 2 212 ? 86.688  -6.115  15.208  1.00 8.76  ? 213  LYS B CB  1 
ATOM   3651 C  CG  . LYS B 2 212 ? 86.813  -7.489  15.948  1.00 11.36 ? 213  LYS B CG  1 
ATOM   3652 C  CD  . LYS B 2 212 ? 85.430  -8.050  16.284  1.00 13.28 ? 213  LYS B CD  1 
ATOM   3653 C  CE  . LYS B 2 212 ? 84.853  -7.311  17.449  1.00 14.92 ? 213  LYS B CE  1 
ATOM   3654 N  NZ  . LYS B 2 212 ? 83.482  -7.862  17.757  1.00 13.74 ? 213  LYS B NZ  1 
ATOM   3655 N  N   . ALA B 2 213 ? 88.518  -6.821  12.732  1.00 9.95  ? 214  ALA B N   1 
ATOM   3656 C  CA  . ALA B 2 213 ? 89.236  -7.837  11.963  1.00 10.16 ? 214  ALA B CA  1 
ATOM   3657 C  C   . ALA B 2 213 ? 90.667  -7.460  11.779  1.00 10.60 ? 214  ALA B C   1 
ATOM   3658 O  O   . ALA B 2 213 ? 91.580  -8.310  11.840  1.00 11.81 ? 214  ALA B O   1 
ATOM   3659 C  CB  . ALA B 2 213 ? 88.584  -8.022  10.586  1.00 10.43 ? 214  ALA B CB  1 
ATOM   3660 N  N   . GLN B 2 214 ? 90.896  -6.177  11.513  1.00 8.74  ? 215  GLN B N   1 
ATOM   3661 C  CA  . GLN B 2 214 ? 92.269  -5.721  11.241  1.00 9.44  ? 215  GLN B CA  1 
ATOM   3662 C  C   . GLN B 2 214 ? 93.171  -5.814  12.474  1.00 9.73  ? 215  GLN B C   1 
ATOM   3663 O  O   . GLN B 2 214 ? 94.328  -6.237  12.378  1.00 10.59 ? 215  GLN B O   1 
ATOM   3664 C  CB  . GLN B 2 214 ? 92.200  -4.273  10.697  1.00 9.49  ? 215  GLN B CB  1 
ATOM   3665 C  CG  . GLN B 2 214 ? 91.644  -4.248  9.272   1.00 8.75  ? 215  GLN B CG  1 
ATOM   3666 C  CD  . GLN B 2 214 ? 91.331  -2.823  8.840   1.00 9.49  ? 215  GLN B CD  1 
ATOM   3667 O  OE1 . GLN B 2 214 ? 90.704  -2.062  9.593   1.00 9.15  ? 215  GLN B OE1 1 
ATOM   3668 N  NE2 . GLN B 2 214 ? 91.725  -2.481  7.611   1.00 10.78 ? 215  GLN B NE2 1 
ATOM   3669 N  N   . ILE B 2 215 ? 92.637  -5.424  13.647  1.00 10.48 ? 216  ILE B N   1 
ATOM   3670 C  CA  . ILE B 2 215 ? 93.454  -5.498  14.868  1.00 10.73 ? 216  ILE B CA  1 
ATOM   3671 C  C   . ILE B 2 215 ? 93.696  -6.947  15.284  1.00 10.85 ? 216  ILE B C   1 
ATOM   3672 O  O   . ILE B 2 215 ? 94.766  -7.258  15.754  1.00 10.82 ? 216  ILE B O   1 
ATOM   3673 C  CB  . ILE B 2 215 ? 92.833  -4.628  15.981  1.00 11.92 ? 216  ILE B CB  1 
ATOM   3674 C  CG1 . ILE B 2 215 ? 93.874  -4.333  17.065  1.00 15.81 ? 216  ILE B CG1 1 
ATOM   3675 C  CG2 . ILE B 2 215 ? 91.689  -5.253  16.586  1.00 14.67 ? 216  ILE B CG2 1 
ATOM   3676 C  CD1 . ILE B 2 215 ? 94.914  -3.362  16.566  1.00 17.04 ? 216  ILE B CD1 1 
ATOM   3677 N  N   . LEU B 2 216 ? 92.717  -7.809  15.080  1.00 10.52 ? 217  LEU B N   1 
ATOM   3678 C  CA  . LEU B 2 216 ? 92.952  -9.240  15.412  1.00 12.85 ? 217  LEU B CA  1 
ATOM   3679 C  C   . LEU B 2 216 ? 94.051  -9.776  14.481  1.00 12.71 ? 217  LEU B C   1 
ATOM   3680 O  O   . LEU B 2 216 ? 94.937  -10.533 14.916  1.00 14.68 ? 217  LEU B O   1 
ATOM   3681 C  CB  . LEU B 2 216 ? 91.657  -10.030 15.253  1.00 12.54 ? 217  LEU B CB  1 
ATOM   3682 C  CG  . LEU B 2 216 ? 90.658  -9.818  16.392  1.00 13.09 ? 217  LEU B CG  1 
ATOM   3683 C  CD1 . LEU B 2 216 ? 89.344  -10.516 16.045  1.00 15.11 ? 217  LEU B CD1 1 
ATOM   3684 C  CD2 . LEU B 2 216 ? 91.273  -10.314 17.713  1.00 15.49 ? 217  LEU B CD2 1 
ATOM   3685 N  N   . ASP B 2 217 ? 94.024  -9.415  13.219  1.00 11.44 ? 218  ASP B N   1 
ATOM   3686 C  CA  . ASP B 2 217 ? 95.051  -9.867  12.297  1.00 13.23 ? 218  ASP B CA  1 
ATOM   3687 C  C   . ASP B 2 217 ? 96.422  -9.371  12.685  1.00 13.85 ? 218  ASP B C   1 
ATOM   3688 O  O   . ASP B 2 217 ? 97.407  -10.146 12.643  1.00 16.27 ? 218  ASP B O   1 
ATOM   3689 C  CB  . ASP B 2 217 ? 94.693  -9.375  10.878  1.00 15.21 ? 218  ASP B CB  1 
ATOM   3690 C  CG  . ASP B 2 217 ? 95.778  -9.704  9.850   1.00 20.69 ? 218  ASP B CG  1 
ATOM   3691 O  OD1 . ASP B 2 217 ? 96.148  -10.906 9.721   1.00 21.55 ? 218  ASP B OD1 1 
ATOM   3692 O  OD2 . ASP B 2 217 ? 96.261  -8.798  9.160   1.00 23.00 ? 218  ASP B OD2 1 
ATOM   3693 N  N   . LYS B 2 218 ? 96.531  -8.099  13.070  1.00 10.57 ? 219  LYS B N   1 
ATOM   3694 C  CA  . LYS B 2 218 ? 97.827  -7.509  13.353  1.00 10.58 ? 219  LYS B CA  1 
ATOM   3695 C  C   . LYS B 2 218 ? 98.371  -7.673  14.767  1.00 12.68 ? 219  LYS B C   1 
ATOM   3696 O  O   . LYS B 2 218 ? 99.605  -7.684  14.927  1.00 15.55 ? 219  LYS B O   1 
ATOM   3697 C  CB  . LYS B 2 218 ? 97.751  -5.999  13.076  1.00 12.94 ? 219  LYS B CB  1 
ATOM   3698 C  CG  A LYS B 2 218 ? 97.632  -5.638  11.600  0.50 13.27 ? 219  LYS B CG  1 
ATOM   3699 C  CG  B LYS B 2 218 ? 97.295  -5.715  11.625  0.50 13.03 ? 219  LYS B CG  1 
ATOM   3700 C  CD  A LYS B 2 218 ? 98.846  -6.115  10.821  0.50 14.52 ? 219  LYS B CD  1 
ATOM   3701 C  CD  B LYS B 2 218 ? 96.914  -4.265  11.435  0.50 13.91 ? 219  LYS B CD  1 
ATOM   3702 C  CE  A LYS B 2 218 ? 98.614  -5.951  9.327   0.50 15.43 ? 219  LYS B CE  1 
ATOM   3703 C  CE  B LYS B 2 218 ? 96.557  -3.961  9.975   0.50 15.59 ? 219  LYS B CE  1 
ATOM   3704 N  NZ  A LYS B 2 218 ? 99.828  -6.387  8.581   0.50 16.54 ? 219  LYS B NZ  1 
ATOM   3705 N  NZ  B LYS B 2 218 ? 97.662  -4.303  9.073   0.50 14.50 ? 219  LYS B NZ  1 
ATOM   3706 N  N   . GLU B 2 219 ? 97.498  -7.802  15.745  1.00 11.84 ? 220  GLU B N   1 
ATOM   3707 C  CA  . GLU B 2 219 ? 97.901  -7.871  17.150  1.00 11.80 ? 220  GLU B CA  1 
ATOM   3708 C  C   . GLU B 2 219 ? 97.430  -9.148  17.851  1.00 12.94 ? 220  GLU B C   1 
ATOM   3709 O  O   . GLU B 2 219 ? 97.870  -9.410  18.995  1.00 14.62 ? 220  GLU B O   1 
ATOM   3710 C  CB  . GLU B 2 219 ? 97.376  -6.644  17.938  1.00 14.47 ? 220  GLU B CB  1 
ATOM   3711 C  CG  . GLU B 2 219 ? 97.971  -5.325  17.454  1.00 14.45 ? 220  GLU B CG  1 
ATOM   3712 C  CD  . GLU B 2 219 ? 99.434  -5.141  17.861  1.00 16.87 ? 220  GLU B CD  1 
ATOM   3713 O  OE1 . GLU B 2 219 ? 99.892  -5.786  18.846  1.00 19.11 ? 220  GLU B OE1 1 
ATOM   3714 O  OE2 . GLU B 2 219 ? 100.120 -4.312  17.225  1.00 15.96 ? 220  GLU B OE2 1 
ATOM   3715 N  N   . GLY B 2 220 ? 96.517  -9.885  17.232  1.00 12.60 ? 221  GLY B N   1 
ATOM   3716 C  CA  . GLY B 2 220 ? 96.012  -11.132 17.800  1.00 13.52 ? 221  GLY B CA  1 
ATOM   3717 C  C   . GLY B 2 220 ? 95.106  -10.982 18.997  1.00 13.63 ? 221  GLY B C   1 
ATOM   3718 O  O   . GLY B 2 220 ? 94.875  -11.944 19.733  1.00 15.35 ? 221  GLY B O   1 
ATOM   3719 N  N   . ARG B 2 221 ? 94.574  -9.763  19.209  1.00 12.80 ? 222  ARG B N   1 
ATOM   3720 C  CA  . ARG B 2 221 ? 93.701  -9.471  20.348  1.00 13.07 ? 222  ARG B CA  1 
ATOM   3721 C  C   . ARG B 2 221 ? 92.940  -8.179  20.074  1.00 12.78 ? 222  ARG B C   1 
ATOM   3722 O  O   . ARG B 2 221 ? 93.252  -7.467  19.118  1.00 14.62 ? 222  ARG B O   1 
ATOM   3723 C  CB  . ARG B 2 221 ? 94.481  -9.286  21.655  1.00 14.23 ? 222  ARG B CB  1 
ATOM   3724 C  CG  . ARG B 2 221 ? 95.564  -8.192  21.465  1.00 17.38 ? 222  ARG B CG  1 
ATOM   3725 C  CD  . ARG B 2 221 ? 96.224  -7.814  22.759  1.00 22.83 ? 222  ARG B CD  1 
ATOM   3726 N  NE  . ARG B 2 221 ? 95.204  -7.110  23.507  1.00 29.86 ? 222  ARG B NE  1 
ATOM   3727 C  CZ  . ARG B 2 221 ? 95.451  -6.138  24.366  1.00 29.28 ? 222  ARG B CZ  1 
ATOM   3728 N  NH1 . ARG B 2 221 ? 96.713  -5.753  24.573  1.00 29.43 ? 222  ARG B NH1 1 
ATOM   3729 N  NH2 . ARG B 2 221 ? 94.430  -5.569  24.987  1.00 27.55 ? 222  ARG B NH2 1 
ATOM   3730 N  N   . LEU B 2 222 ? 91.931  -7.935  20.893  1.00 12.64 ? 223  LEU B N   1 
ATOM   3731 C  CA  . LEU B 2 222 ? 91.132  -6.724  20.739  1.00 11.74 ? 223  LEU B CA  1 
ATOM   3732 C  C   . LEU B 2 222 ? 91.824  -5.537  21.376  1.00 10.89 ? 223  LEU B C   1 
ATOM   3733 O  O   . LEU B 2 222 ? 92.708  -5.662  22.230  1.00 11.86 ? 223  LEU B O   1 
ATOM   3734 C  CB  . LEU B 2 222 ? 89.770  -6.905  21.427  1.00 13.12 ? 223  LEU B CB  1 
ATOM   3735 C  CG  . LEU B 2 222 ? 88.972  -8.082  20.827  1.00 14.77 ? 223  LEU B CG  1 
ATOM   3736 C  CD1 . LEU B 2 222 ? 87.723  -8.325  21.690  1.00 19.01 ? 223  LEU B CD1 1 
ATOM   3737 C  CD2 . LEU B 2 222 ? 88.603  -7.769  19.372  1.00 17.74 ? 223  LEU B CD2 1 
ATOM   3738 N  N   . PRO B 2 223 ? 91.418  -4.331  20.982  1.00 10.98 ? 224  PRO B N   1 
ATOM   3739 C  CA  . PRO B 2 223 ? 92.049  -3.140  21.589  1.00 10.44 ? 224  PRO B CA  1 
ATOM   3740 C  C   . PRO B 2 223 ? 91.683  -3.018  23.076  1.00 10.29 ? 224  PRO B C   1 
ATOM   3741 O  O   . PRO B 2 223 ? 90.627  -3.522  23.493  1.00 10.92 ? 224  PRO B O   1 
ATOM   3742 C  CB  . PRO B 2 223 ? 91.400  -1.932  20.846  1.00 12.37 ? 224  PRO B CB  1 
ATOM   3743 C  CG  . PRO B 2 223 ? 90.724  -2.555  19.611  1.00 12.81 ? 224  PRO B CG  1 
ATOM   3744 C  CD  . PRO B 2 223 ? 90.366  -3.987  20.001  1.00 11.17 ? 224  PRO B CD  1 
ATOM   3745 N  N   . ASP B 2 224 ? 92.491  -2.279  23.820  1.00 9.29  ? 225  ASP B N   1 
ATOM   3746 C  CA  . ASP B 2 224 ? 92.117  -1.942  25.199  1.00 9.22  ? 225  ASP B CA  1 
ATOM   3747 C  C   . ASP B 2 224 ? 91.045  -0.857  25.160  1.00 9.73  ? 225  ASP B C   1 
ATOM   3748 O  O   . ASP B 2 224 ? 90.180  -0.815  26.051  1.00 10.68 ? 225  ASP B O   1 
ATOM   3749 C  CB  . ASP B 2 224 ? 93.328  -1.467  26.021  1.00 10.06 ? 225  ASP B CB  1 
ATOM   3750 C  CG  . ASP B 2 224 ? 94.280  -2.601  26.276  1.00 12.70 ? 225  ASP B CG  1 
ATOM   3751 O  OD1 . ASP B 2 224 ? 93.809  -3.665  26.794  1.00 14.89 ? 225  ASP B OD1 1 
ATOM   3752 O  OD2 . ASP B 2 224 ? 95.471  -2.490  25.953  1.00 12.51 ? 225  ASP B OD2 1 
ATOM   3753 N  N   . ALA B 2 225 ? 91.100  0.021   24.139  1.00 9.56  ? 226  ALA B N   1 
ATOM   3754 C  CA  . ALA B 2 225 ? 90.054  1.046   24.016  1.00 9.14  ? 226  ALA B CA  1 
ATOM   3755 C  C   . ALA B 2 225 ? 90.037  1.527   22.579  1.00 7.63  ? 226  ALA B C   1 
ATOM   3756 O  O   . ALA B 2 225 ? 91.076  1.538   21.899  1.00 8.26  ? 226  ALA B O   1 
ATOM   3757 C  CB  . ALA B 2 225 ? 90.360  2.274   24.920  1.00 9.94  ? 226  ALA B CB  1 
ATOM   3758 N  N   . VAL B 2 226 ? 88.842  1.957   22.177  1.00 8.52  ? 227  VAL B N   1 
ATOM   3759 C  CA  . VAL B 2 226 ? 88.668  2.624   20.858  1.00 7.25  ? 227  VAL B CA  1 
ATOM   3760 C  C   . VAL B 2 226 ? 88.151  4.026   21.195  1.00 8.76  ? 227  VAL B C   1 
ATOM   3761 O  O   . VAL B 2 226 ? 87.339  4.202   22.101  1.00 8.47  ? 227  VAL B O   1 
ATOM   3762 C  CB  . VAL B 2 226 ? 87.756  1.865   19.904  1.00 7.84  ? 227  VAL B CB  1 
ATOM   3763 C  CG1 . VAL B 2 226 ? 88.366  0.467   19.601  1.00 10.27 ? 227  VAL B CG1 1 
ATOM   3764 C  CG2 . VAL B 2 226 ? 86.339  1.698   20.451  1.00 9.41  ? 227  VAL B CG2 1 
ATOM   3765 N  N   . ILE B 2 227 ? 88.679  5.030   20.468  1.00 7.10  ? 228  ILE B N   1 
ATOM   3766 C  CA  . ILE B 2 227 ? 88.440  6.426   20.814  1.00 6.45  ? 228  ILE B CA  1 
ATOM   3767 C  C   . ILE B 2 227 ? 87.964  7.165   19.599  1.00 6.46  ? 228  ILE B C   1 
ATOM   3768 O  O   . ILE B 2 227 ? 88.558  7.062   18.523  1.00 7.26  ? 228  ILE B O   1 
ATOM   3769 C  CB  . ILE B 2 227 ? 89.770  7.069   21.299  1.00 7.58  ? 228  ILE B CB  1 
ATOM   3770 C  CG1 . ILE B 2 227 ? 90.310  6.231   22.477  1.00 9.38  ? 228  ILE B CG1 1 
ATOM   3771 C  CG2 . ILE B 2 227 ? 89.527  8.496   21.759  1.00 9.03  ? 228  ILE B CG2 1 
ATOM   3772 C  CD1 . ILE B 2 227 ? 91.768  5.925   22.339  1.00 14.89 ? 228  ILE B CD1 1 
ATOM   3773 N  N   . ALA B 2 228 ? 86.898  7.927   19.762  1.00 6.56  ? 229  ALA B N   1 
ATOM   3774 C  CA  . ALA B 2 228 ? 86.338  8.698   18.638  1.00 6.52  ? 229  ALA B CA  1 
ATOM   3775 C  C   . ALA B 2 228 ? 85.740  10.016  19.059  1.00 7.06  ? 229  ALA B C   1 
ATOM   3776 O  O   . ALA B 2 228 ? 85.177  10.113  20.162  1.00 7.05  ? 229  ALA B O   1 
ATOM   3777 C  CB  . ALA B 2 228 ? 85.229  7.835   17.925  1.00 8.72  ? 229  ALA B CB  1 
ATOM   3778 N  N   . CYS B 2 229 ? 85.820  11.016  18.202  1.00 6.83  ? 230  CYS B N   1 
ATOM   3779 C  CA  . CYS B 2 229 ? 85.180  12.306  18.489  1.00 7.57  ? 230  CYS B CA  1 
ATOM   3780 C  C   . CYS B 2 229 ? 83.661  12.171  18.325  1.00 7.27  ? 230  CYS B C   1 
ATOM   3781 O  O   . CYS B 2 229 ? 83.158  11.265  17.620  1.00 6.59  ? 230  CYS B O   1 
ATOM   3782 C  CB  . CYS B 2 229 ? 85.723  13.418  17.582  1.00 7.57  ? 230  CYS B CB  1 
ATOM   3783 S  SG  . CYS B 2 229 ? 85.324  13.299  15.820  1.00 8.45  ? 230  CYS B SG  1 
ATOM   3784 N  N   . VAL B 2 230 ? 82.945  13.042  19.030  1.00 6.67  ? 231  VAL B N   1 
ATOM   3785 C  CA  . VAL B 2 230 ? 81.473  13.042  19.055  1.00 6.13  ? 231  VAL B CA  1 
ATOM   3786 C  C   . VAL B 2 230 ? 80.935  14.452  18.842  1.00 9.18  ? 231  VAL B C   1 
ATOM   3787 O  O   . VAL B 2 230 ? 81.013  15.314  19.728  1.00 9.26  ? 231  VAL B O   1 
ATOM   3788 C  CB  . VAL B 2 230 ? 80.991  12.484  20.425  1.00 6.82  ? 231  VAL B CB  1 
ATOM   3789 C  CG1 . VAL B 2 230 ? 79.468  12.591  20.487  1.00 8.52  ? 231  VAL B CG1 1 
ATOM   3790 C  CG2 . VAL B 2 230 ? 81.458  11.035  20.656  1.00 8.10  ? 231  VAL B CG2 1 
ATOM   3791 N  N   . GLY B 2 231 ? 80.414  14.661  17.635  1.00 7.99  ? 232  GLY B N   1 
ATOM   3792 C  CA  . GLY B 2 231 ? 79.744  15.906  17.266  1.00 8.99  ? 232  GLY B CA  1 
ATOM   3793 C  C   . GLY B 2 231 ? 78.269  15.616  17.408  1.00 9.10  ? 232  GLY B C   1 
ATOM   3794 O  O   . GLY B 2 231 ? 77.568  16.165  18.269  1.00 11.54 ? 232  GLY B O   1 
ATOM   3795 N  N   . GLY B 2 232 ? 77.780  14.710  16.557  1.00 8.70  ? 233  GLY B N   1 
ATOM   3796 C  CA  . GLY B 2 232 ? 76.404  14.236  16.671  1.00 7.72  ? 233  GLY B CA  1 
ATOM   3797 C  C   . GLY B 2 232 ? 76.474  12.751  17.084  1.00 9.25  ? 233  GLY B C   1 
ATOM   3798 O  O   . GLY B 2 232 ? 75.486  12.223  17.673  1.00 9.31  ? 233  GLY B O   1 
ATOM   3799 N  N   . GLY B 2 233 ? 77.560  12.033  16.761  1.00 8.22  ? 234  GLY B N   1 
ATOM   3800 C  CA  . GLY B 2 233 ? 77.655  10.634  17.193  1.00 8.58  ? 234  GLY B CA  1 
ATOM   3801 C  C   . GLY B 2 233 ? 77.829  9.531   16.143  1.00 7.30  ? 234  GLY B C   1 
ATOM   3802 O  O   . GLY B 2 233 ? 78.021  8.356   16.526  1.00 6.74  ? 234  GLY B O   1 
ATOM   3803 N  N   . SER B 2 234 ? 77.810  9.879   14.859  1.00 5.69  ? 235  SER B N   1 
ATOM   3804 C  CA  . SER B 2 234 ? 77.897  8.822   13.852  1.00 6.56  ? 235  SER B CA  1 
ATOM   3805 C  C   . SER B 2 234 ? 79.235  8.111   13.715  1.00 6.14  ? 235  SER B C   1 
ATOM   3806 O  O   . SER B 2 234 ? 79.231  6.890   13.655  1.00 7.42  ? 235  SER B O   1 
ATOM   3807 C  CB  . SER B 2 234 ? 77.403  9.343   12.479  1.00 7.62  ? 235  SER B CB  1 
ATOM   3808 O  OG  . SER B 2 234 ? 78.282  10.316  11.893  1.00 8.26  ? 235  SER B OG  1 
ATOM   3809 N  N   . ASN B 2 235 ? 80.355  8.822   13.626  1.00 6.32  ? 236  ASN B N   1 
ATOM   3810 C  CA  . ASN B 2 235 ? 81.572  8.072   13.484  1.00 6.12  ? 236  ASN B CA  1 
ATOM   3811 C  C   . ASN B 2 235 ? 81.869  7.284   14.725  1.00 6.02  ? 236  ASN B C   1 
ATOM   3812 O  O   . ASN B 2 235 ? 82.397  6.181   14.622  1.00 6.63  ? 236  ASN B O   1 
ATOM   3813 C  CB  . ASN B 2 235 ? 82.786  8.943   13.027  1.00 6.52  ? 236  ASN B CB  1 
ATOM   3814 C  CG  . ASN B 2 235 ? 83.486  9.674   14.185  1.00 7.99  ? 236  ASN B CG  1 
ATOM   3815 O  OD1 . ASN B 2 235 ? 83.123  10.845  14.542  1.00 10.23 ? 236  ASN B OD1 1 
ATOM   3816 N  ND2 . ASN B 2 235 ? 84.462  9.022   14.750  1.00 5.12  ? 236  ASN B ND2 1 
ATOM   3817 N  N   . ALA B 2 236 ? 81.517  7.842   15.891  1.00 6.37  ? 237  ALA B N   1 
ATOM   3818 C  CA  . ALA B 2 236 ? 81.811  7.119   17.114  1.00 7.43  ? 237  ALA B CA  1 
ATOM   3819 C  C   . ALA B 2 236 ? 80.960  5.871   17.261  1.00 6.74  ? 237  ALA B C   1 
ATOM   3820 O  O   . ALA B 2 236 ? 81.491  4.836   17.641  1.00 6.96  ? 237  ALA B O   1 
ATOM   3821 C  CB  . ALA B 2 236 ? 81.635  8.066   18.328  1.00 7.98  ? 237  ALA B CB  1 
ATOM   3822 N  N   . ILE B 2 237 ? 79.652  5.963   16.982  1.00 6.34  ? 238  ILE B N   1 
ATOM   3823 C  CA  . ILE B 2 237 ? 78.848  4.776   17.126  1.00 6.38  ? 238  ILE B CA  1 
ATOM   3824 C  C   . ILE B 2 237 ? 79.228  3.786   16.041  1.00 7.21  ? 238  ILE B C   1 
ATOM   3825 O  O   . ILE B 2 237 ? 79.149  2.576   16.287  1.00 7.29  ? 238  ILE B O   1 
ATOM   3826 C  CB  . ILE B 2 237 ? 77.307  5.097   17.179  1.00 6.62  ? 238  ILE B CB  1 
ATOM   3827 C  CG1 . ILE B 2 237 ? 76.526  3.964   17.849  1.00 8.26  ? 238  ILE B CG1 1 
ATOM   3828 C  CG2 . ILE B 2 237 ? 76.741  5.287   15.756  1.00 7.89  ? 238  ILE B CG2 1 
ATOM   3829 C  CD1 . ILE B 2 237 ? 76.806  3.919   19.431  1.00 9.53  ? 238  ILE B CD1 1 
ATOM   3830 N  N   . GLY B 2 238 ? 79.666  4.260   14.882  1.00 6.31  ? 239  GLY B N   1 
ATOM   3831 C  CA  . GLY B 2 238 ? 80.107  3.296   13.870  1.00 7.33  ? 239  GLY B CA  1 
ATOM   3832 C  C   . GLY B 2 238 ? 81.353  2.529   14.325  1.00 6.77  ? 239  GLY B C   1 
ATOM   3833 O  O   . GLY B 2 238 ? 81.495  1.328   14.004  1.00 8.42  ? 239  GLY B O   1 
ATOM   3834 N  N   . MET B 2 239 ? 82.286  3.209   14.977  1.00 7.31  ? 240  MET B N   1 
ATOM   3835 C  CA  . MET B 2 239 ? 83.439  2.487   15.517  1.00 7.17  ? 240  MET B CA  1 
ATOM   3836 C  C   . MET B 2 239 ? 83.036  1.598   16.724  1.00 8.53  ? 240  MET B C   1 
ATOM   3837 O  O   . MET B 2 239 ? 83.496  0.480   16.856  1.00 8.87  ? 240  MET B O   1 
ATOM   3838 C  CB  . MET B 2 239 ? 84.486  3.540   15.983  1.00 8.03  ? 240  MET B CB  1 
ATOM   3839 C  CG  . MET B 2 239 ? 85.649  2.888   16.779  1.00 8.88  ? 240  MET B CG  1 
ATOM   3840 S  SD  . MET B 2 239 ? 86.634  1.681   15.772  1.00 8.82  ? 240  MET B SD  1 
ATOM   3841 C  CE  . MET B 2 239 ? 87.747  2.841   14.854  1.00 10.22 ? 240  MET B CE  1 
ATOM   3842 N  N   . PHE B 2 240 ? 82.189  2.110   17.626  1.00 7.65  ? 241  PHE B N   1 
ATOM   3843 C  CA  . PHE B 2 240 ? 81.780  1.389   18.838  1.00 7.42  ? 241  PHE B CA  1 
ATOM   3844 C  C   . PHE B 2 240 ? 80.912  0.148   18.646  1.00 8.47  ? 241  PHE B C   1 
ATOM   3845 O  O   . PHE B 2 240 ? 81.090  -0.854  19.333  1.00 8.88  ? 241  PHE B O   1 
ATOM   3846 C  CB  . PHE B 2 240 ? 80.948  2.281   19.770  1.00 8.13  ? 241  PHE B CB  1 
ATOM   3847 C  CG  . PHE B 2 240 ? 81.678  3.446   20.380  1.00 6.82  ? 241  PHE B CG  1 
ATOM   3848 C  CD1 . PHE B 2 240 ? 83.044  3.652   20.196  1.00 7.64  ? 241  PHE B CD1 1 
ATOM   3849 C  CD2 . PHE B 2 240 ? 80.963  4.347   21.167  1.00 7.90  ? 241  PHE B CD2 1 
ATOM   3850 C  CE1 . PHE B 2 240 ? 83.682  4.749   20.793  1.00 9.31  ? 241  PHE B CE1 1 
ATOM   3851 C  CE2 . PHE B 2 240 ? 81.587  5.438   21.764  1.00 8.53  ? 241  PHE B CE2 1 
ATOM   3852 C  CZ  . PHE B 2 240 ? 82.947  5.640   21.577  1.00 8.79  ? 241  PHE B CZ  1 
ATOM   3853 N  N   . ALA B 2 241 ? 80.045  0.212   17.634  1.00 8.26  ? 242  ALA B N   1 
ATOM   3854 C  CA  . ALA B 2 241 ? 78.974  -0.803  17.604  1.00 8.86  ? 242  ALA B CA  1 
ATOM   3855 C  C   . ALA B 2 241 ? 79.408  -2.251  17.725  1.00 9.13  ? 242  ALA B C   1 
ATOM   3856 O  O   . ALA B 2 241 ? 78.853  -3.012  18.578  1.00 10.22 ? 242  ALA B O   1 
ATOM   3857 C  CB  . ALA B 2 241 ? 78.128  -0.611  16.359  1.00 9.80  ? 242  ALA B CB  1 
ATOM   3858 N  N   . ASP B 2 242 ? 80.345  -2.648  16.867  1.00 9.20  ? 243  ASP B N   1 
ATOM   3859 C  CA  . ASP B 2 242 ? 80.763  -4.053  16.891  1.00 10.28 ? 243  ASP B CA  1 
ATOM   3860 C  C   . ASP B 2 242 ? 81.533  -4.459  18.126  1.00 10.74 ? 243  ASP B C   1 
ATOM   3861 O  O   . ASP B 2 242 ? 81.783  -5.677  18.315  1.00 11.94 ? 243  ASP B O   1 
ATOM   3862 C  CB  . ASP B 2 242 ? 81.585  -4.367  15.629  1.00 12.16 ? 243  ASP B CB  1 
ATOM   3863 C  CG  . ASP B 2 242 ? 81.518  -5.821  15.257  1.00 15.59 ? 243  ASP B CG  1 
ATOM   3864 O  OD1 . ASP B 2 242 ? 80.376  -6.329  15.113  1.00 18.42 ? 243  ASP B OD1 1 
ATOM   3865 O  OD2 . ASP B 2 242 ? 82.611  -6.404  15.103  1.00 17.95 ? 243  ASP B OD2 1 
ATOM   3866 N  N   . PHE B 2 243 ? 81.924  -3.500  18.969  1.00 10.51 ? 244  PHE B N   1 
ATOM   3867 C  CA  . PHE B 2 243 ? 82.674  -3.784  20.195  1.00 9.58  ? 244  PHE B CA  1 
ATOM   3868 C  C   . PHE B 2 243 ? 81.811  -3.703  21.451  1.00 9.50  ? 244  PHE B C   1 
ATOM   3869 O  O   . PHE B 2 243 ? 82.275  -4.034  22.542  1.00 10.22 ? 244  PHE B O   1 
ATOM   3870 C  CB  . PHE B 2 243 ? 83.836  -2.793  20.363  1.00 9.62  ? 244  PHE B CB  1 
ATOM   3871 C  CG  . PHE B 2 243 ? 84.925  -2.935  19.334  1.00 8.90  ? 244  PHE B CG  1 
ATOM   3872 C  CD1 . PHE B 2 243 ? 85.805  -4.014  19.370  1.00 9.68  ? 244  PHE B CD1 1 
ATOM   3873 C  CD2 . PHE B 2 243 ? 85.080  -1.977  18.337  1.00 9.99  ? 244  PHE B CD2 1 
ATOM   3874 C  CE1 . PHE B 2 243 ? 86.827  -4.135  18.427  1.00 8.68  ? 244  PHE B CE1 1 
ATOM   3875 C  CE2 . PHE B 2 243 ? 86.097  -2.087  17.388  1.00 9.05  ? 244  PHE B CE2 1 
ATOM   3876 C  CZ  . PHE B 2 243 ? 86.973  -3.168  17.433  1.00 10.10 ? 244  PHE B CZ  1 
ATOM   3877 N  N   . ILE B 2 244 ? 80.540  -3.293  21.301  1.00 9.26  ? 245  ILE B N   1 
ATOM   3878 C  CA  . ILE B 2 244 ? 79.694  -3.104  22.489  1.00 10.70 ? 245  ILE B CA  1 
ATOM   3879 C  C   . ILE B 2 244 ? 79.620  -4.379  23.325  1.00 10.94 ? 245  ILE B C   1 
ATOM   3880 O  O   . ILE B 2 244 ? 79.730  -4.322  24.531  1.00 12.03 ? 245  ILE B O   1 
ATOM   3881 C  CB  . ILE B 2 244 ? 78.300  -2.596  22.072  1.00 10.10 ? 245  ILE B CB  1 
ATOM   3882 C  CG1 . ILE B 2 244 ? 78.420  -1.110  21.654  1.00 10.55 ? 245  ILE B CG1 1 
ATOM   3883 C  CG2 . ILE B 2 244 ? 77.307  -2.718  23.271  1.00 12.52 ? 245  ILE B CG2 1 
ATOM   3884 C  CD1 . ILE B 2 244 ? 77.081  -0.553  21.070  1.00 11.11 ? 245  ILE B CD1 1 
ATOM   3885 N  N   . ASN B 2 245 ? 79.501  -5.536  22.682  1.00 11.55 ? 246  ASN B N   1 
ATOM   3886 C  CA  . ASN B 2 245 ? 79.432  -6.778  23.446  1.00 14.00 ? 246  ASN B CA  1 
ATOM   3887 C  C   . ASN B 2 245 ? 80.776  -7.379  23.862  1.00 14.22 ? 246  ASN B C   1 
ATOM   3888 O  O   . ASN B 2 245 ? 80.819  -8.430  24.538  1.00 17.07 ? 246  ASN B O   1 
ATOM   3889 C  CB  . ASN B 2 245 ? 78.608  -7.774  22.664  1.00 17.35 ? 246  ASN B CB  1 
ATOM   3890 C  CG  . ASN B 2 245 ? 77.160  -7.332  22.549  1.00 18.59 ? 246  ASN B CG  1 
ATOM   3891 O  OD1 . ASN B 2 245 ? 76.652  -6.624  23.416  1.00 22.95 ? 246  ASN B OD1 1 
ATOM   3892 N  ND2 . ASN B 2 245 ? 76.490  -7.795  21.509  1.00 25.05 ? 246  ASN B ND2 1 
ATOM   3893 N  N   . ASP B 2 246 ? 81.877  -6.733  23.499  1.00 13.13 ? 247  ASP B N   1 
ATOM   3894 C  CA  . ASP B 2 246 ? 83.238  -7.148  23.918  1.00 14.25 ? 247  ASP B CA  1 
ATOM   3895 C  C   . ASP B 2 246 ? 83.517  -6.278  25.133  1.00 14.13 ? 247  ASP B C   1 
ATOM   3896 O  O   . ASP B 2 246 ? 84.123  -5.190  25.025  1.00 13.17 ? 247  ASP B O   1 
ATOM   3897 C  CB  . ASP B 2 246 ? 84.244  -6.840  22.811  1.00 13.74 ? 247  ASP B CB  1 
ATOM   3898 C  CG  . ASP B 2 246 ? 83.965  -7.644  21.579  1.00 16.79 ? 247  ASP B CG  1 
ATOM   3899 O  OD1 . ASP B 2 246 ? 83.957  -8.912  21.658  1.00 17.47 ? 247  ASP B OD1 1 
ATOM   3900 O  OD2 . ASP B 2 246 ? 83.737  -7.036  20.527  1.00 15.61 ? 247  ASP B OD2 1 
ATOM   3901 N  N   . THR B 2 247 ? 83.099  -6.768  26.299  1.00 15.78 ? 248  THR B N   1 
ATOM   3902 C  CA  . THR B 2 247 ? 83.169  -5.967  27.498  1.00 16.89 ? 248  THR B CA  1 
ATOM   3903 C  C   . THR B 2 247 ? 84.518  -5.440  27.923  1.00 15.45 ? 248  THR B C   1 
ATOM   3904 O  O   . THR B 2 247 ? 84.554  -4.398  28.598  1.00 17.64 ? 248  THR B O   1 
ATOM   3905 C  CB  . THR B 2 247 ? 82.460  -6.691  28.689  1.00 20.75 ? 248  THR B CB  1 
ATOM   3906 O  OG1 . THR B 2 247 ? 83.182  -7.862  29.020  1.00 24.66 ? 248  THR B OG1 1 
ATOM   3907 C  CG2 . THR B 2 247 ? 81.046  -7.041  28.314  1.00 23.69 ? 248  THR B CG2 1 
ATOM   3908 N  N   . SER B 2 248 ? 85.609  -6.097  27.513  1.00 14.31 ? 249  SER B N   1 
ATOM   3909 C  CA  . SER B 2 248 ? 86.960  -5.646  27.854  1.00 15.16 ? 249  SER B CA  1 
ATOM   3910 C  C   . SER B 2 248 ? 87.409  -4.427  27.042  1.00 14.12 ? 249  SER B C   1 
ATOM   3911 O  O   . SER B 2 248 ? 88.435  -3.816  27.373  1.00 14.99 ? 249  SER B O   1 
ATOM   3912 C  CB  . SER B 2 248 ? 88.015  -6.749  27.596  1.00 16.63 ? 249  SER B CB  1 
ATOM   3913 O  OG  . SER B 2 248 ? 88.182  -7.065  26.186  1.00 18.94 ? 249  SER B OG  1 
ATOM   3914 N  N   . VAL B 2 249 ? 86.684  -4.114  25.967  1.00 12.73 ? 250  VAL B N   1 
ATOM   3915 C  CA  . VAL B 2 249 ? 87.122  -3.018  25.118  1.00 11.13 ? 250  VAL B CA  1 
ATOM   3916 C  C   . VAL B 2 249 ? 86.491  -1.722  25.589  1.00 9.54  ? 250  VAL B C   1 
ATOM   3917 O  O   . VAL B 2 249 ? 85.270  -1.609  25.548  1.00 10.28 ? 250  VAL B O   1 
ATOM   3918 C  CB  . VAL B 2 249 ? 86.707  -3.285  23.682  1.00 10.26 ? 250  VAL B CB  1 
ATOM   3919 C  CG1 . VAL B 2 249 ? 87.207  -2.101  22.806  1.00 9.30  ? 250  VAL B CG1 1 
ATOM   3920 C  CG2 . VAL B 2 249 ? 87.293  -4.617  23.178  1.00 11.09 ? 250  VAL B CG2 1 
ATOM   3921 N  N   . GLY B 2 250 ? 87.309  -0.756  25.993  1.00 8.44  ? 251  GLY B N   1 
ATOM   3922 C  CA  . GLY B 2 250 ? 86.809  0.541   26.376  1.00 8.57  ? 251  GLY B CA  1 
ATOM   3923 C  C   . GLY B 2 250 ? 86.329  1.321   25.158  1.00 8.78  ? 251  GLY B C   1 
ATOM   3924 O  O   . GLY B 2 250 ? 86.832  1.162   24.040  1.00 8.48  ? 251  GLY B O   1 
ATOM   3925 N  N   . LEU B 2 251 ? 85.254  2.080   25.369  1.00 7.40  ? 252  LEU B N   1 
ATOM   3926 C  CA  . LEU B 2 251 ? 84.654  2.936   24.320  1.00 7.36  ? 252  LEU B CA  1 
ATOM   3927 C  C   . LEU B 2 251 ? 84.725  4.341   24.872  1.00 8.44  ? 252  LEU B C   1 
ATOM   3928 O  O   . LEU B 2 251 ? 84.094  4.653   25.904  1.00 9.44  ? 252  LEU B O   1 
ATOM   3929 C  CB  . LEU B 2 251 ? 83.179  2.553   24.031  1.00 7.47  ? 252  LEU B CB  1 
ATOM   3930 C  CG  . LEU B 2 251 ? 82.883  1.032   23.836  1.00 6.77  ? 252  LEU B CG  1 
ATOM   3931 C  CD1 . LEU B 2 251 ? 81.351  0.780   23.716  1.00 9.15  ? 252  LEU B CD1 1 
ATOM   3932 C  CD2 . LEU B 2 251 ? 83.581  0.497   22.549  1.00 9.08  ? 252  LEU B CD2 1 
ATOM   3933 N  N   . ILE B 2 252 ? 85.511  5.172   24.215  1.00 7.21  ? 253  ILE B N   1 
ATOM   3934 C  CA  . ILE B 2 252 ? 85.715  6.538   24.664  1.00 6.74  ? 253  ILE B CA  1 
ATOM   3935 C  C   . ILE B 2 252 ? 85.300  7.547   23.605  1.00 6.63  ? 253  ILE B C   1 
ATOM   3936 O  O   . ILE B 2 252 ? 85.866  7.512   22.485  1.00 7.30  ? 253  ILE B O   1 
ATOM   3937 C  CB  . ILE B 2 252 ? 87.215  6.789   25.044  1.00 6.75  ? 253  ILE B CB  1 
ATOM   3938 C  CG1 . ILE B 2 252 ? 87.632  5.762   26.133  1.00 8.81  ? 253  ILE B CG1 1 
ATOM   3939 C  CG2 . ILE B 2 252 ? 87.420  8.209   25.546  1.00 9.18  ? 253  ILE B CG2 1 
ATOM   3940 C  CD1 . ILE B 2 252 ? 89.149  5.734   26.431  1.00 8.78  ? 253  ILE B CD1 1 
ATOM   3941 N  N   . GLY B 2 253 ? 84.305  8.353   23.935  1.00 7.09  ? 254  GLY B N   1 
ATOM   3942 C  CA  . GLY B 2 253 ? 83.837  9.410   23.057  1.00 6.25  ? 254  GLY B CA  1 
ATOM   3943 C  C   . GLY B 2 253 ? 84.383  10.745  23.466  1.00 6.57  ? 254  GLY B C   1 
ATOM   3944 O  O   . GLY B 2 253 ? 84.366  11.043  24.684  1.00 7.33  ? 254  GLY B O   1 
ATOM   3945 N  N   . VAL B 2 254 ? 84.784  11.563  22.503  1.00 6.52  ? 255  VAL B N   1 
ATOM   3946 C  CA  . VAL B 2 254 ? 85.386  12.845  22.840  1.00 6.82  ? 255  VAL B CA  1 
ATOM   3947 C  C   . VAL B 2 254 ? 84.578  14.011  22.293  1.00 7.02  ? 255  VAL B C   1 
ATOM   3948 O  O   . VAL B 2 254 ? 84.540  14.209  21.067  1.00 7.55  ? 255  VAL B O   1 
ATOM   3949 C  CB  . VAL B 2 254 ? 86.840  12.949  22.285  1.00 7.81  ? 255  VAL B CB  1 
ATOM   3950 C  CG1 . VAL B 2 254 ? 87.498  14.250  22.776  1.00 7.58  ? 255  VAL B CG1 1 
ATOM   3951 C  CG2 . VAL B 2 254 ? 87.681  11.722  22.713  1.00 9.02  ? 255  VAL B CG2 1 
ATOM   3952 N  N   . GLU B 2 255 ? 83.967  14.778  23.182  1.00 7.00  ? 256  GLU B N   1 
ATOM   3953 C  CA  . GLU B 2 255 ? 83.234  15.974  22.764  1.00 8.08  ? 256  GLU B CA  1 
ATOM   3954 C  C   . GLU B 2 255 ? 84.186  17.171  22.767  1.00 7.84  ? 256  GLU B C   1 
ATOM   3955 O  O   . GLU B 2 255 ? 85.238  17.187  23.457  1.00 8.78  ? 256  GLU B O   1 
ATOM   3956 C  CB  . GLU B 2 255 ? 82.111  16.314  23.737  1.00 8.48  ? 256  GLU B CB  1 
ATOM   3957 C  CG  . GLU B 2 255 ? 81.057  15.164  23.919  1.00 9.63  ? 256  GLU B CG  1 
ATOM   3958 C  CD  . GLU B 2 255 ? 79.853  15.593  24.771  1.00 9.92  ? 256  GLU B CD  1 
ATOM   3959 O  OE1 . GLU B 2 255 ? 80.027  15.597  26.043  1.00 10.65 ? 256  GLU B OE1 1 
ATOM   3960 O  OE2 . GLU B 2 255 ? 78.758  15.904  24.212  1.00 10.72 ? 256  GLU B OE2 1 
ATOM   3961 N  N   . PRO B 2 256 ? 83.835  18.204  21.985  1.00 8.18  ? 257  PRO B N   1 
ATOM   3962 C  CA  . PRO B 2 256 ? 84.697  19.398  21.974  1.00 7.31  ? 257  PRO B CA  1 
ATOM   3963 C  C   . PRO B 2 256 ? 84.530  20.254  23.227  1.00 8.72  ? 257  PRO B C   1 
ATOM   3964 O  O   . PRO B 2 256 ? 83.385  20.629  23.610  1.00 9.12  ? 257  PRO B O   1 
ATOM   3965 C  CB  . PRO B 2 256 ? 84.224  20.161  20.714  1.00 9.09  ? 257  PRO B CB  1 
ATOM   3966 C  CG  . PRO B 2 256 ? 82.753  19.761  20.575  1.00 7.05  ? 257  PRO B CG  1 
ATOM   3967 C  CD  . PRO B 2 256 ? 82.774  18.258  20.953  1.00 9.55  ? 257  PRO B CD  1 
ATOM   3968 N  N   . GLY B 2 257 ? 85.675  20.558  23.831  1.00 9.07  ? 258  GLY B N   1 
ATOM   3969 C  CA  . GLY B 2 257 ? 85.676  21.416  25.011  1.00 10.01 ? 258  GLY B CA  1 
ATOM   3970 C  C   . GLY B 2 257 ? 85.824  22.872  24.648  1.00 10.11 ? 258  GLY B C   1 
ATOM   3971 O  O   . GLY B 2 257 ? 85.732  23.728  25.572  1.00 9.92  ? 258  GLY B O   1 
ATOM   3972 N  N   . GLY B 2 258 ? 86.019  23.186  23.353  1.00 10.01 ? 259  GLY B N   1 
ATOM   3973 C  CA  . GLY B 2 258 ? 86.094  24.598  22.951  1.00 10.46 ? 259  GLY B CA  1 
ATOM   3974 C  C   . GLY B 2 258 ? 87.190  25.372  23.701  1.00 9.32  ? 259  GLY B C   1 
ATOM   3975 O  O   . GLY B 2 258 ? 88.346  24.992  23.730  1.00 10.52 ? 259  GLY B O   1 
ATOM   3976 N  N   . HIS B 2 259 ? 86.797  26.506  24.281  1.00 11.73 ? 260  HIS B N   1 
ATOM   3977 C  CA  . HIS B 2 259 ? 87.750  27.337  25.010  1.00 11.67 ? 260  HIS B CA  1 
ATOM   3978 C  C   . HIS B 2 259 ? 87.913  26.851  26.444  1.00 13.44 ? 260  HIS B C   1 
ATOM   3979 O  O   . HIS B 2 259 ? 88.708  27.398  27.211  1.00 15.49 ? 260  HIS B O   1 
ATOM   3980 C  CB  . HIS B 2 259 ? 87.290  28.796  25.015  1.00 12.66 ? 260  HIS B CB  1 
ATOM   3981 C  CG  . HIS B 2 259 ? 87.246  29.420  23.655  1.00 14.18 ? 260  HIS B CG  1 
ATOM   3982 N  ND1 . HIS B 2 259 ? 88.300  29.348  22.770  1.00 16.47 ? 260  HIS B ND1 1 
ATOM   3983 C  CD2 . HIS B 2 259 ? 86.288  30.153  23.042  1.00 14.62 ? 260  HIS B CD2 1 
ATOM   3984 C  CE1 . HIS B 2 259 ? 87.992  30.011  21.668  1.00 16.18 ? 260  HIS B CE1 1 
ATOM   3985 N  NE2 . HIS B 2 259 ? 86.777  30.509  21.808  1.00 17.16 ? 260  HIS B NE2 1 
ATOM   3986 N  N   . GLY B 2 260 ? 87.169  25.807  26.801  1.00 9.96  ? 261  GLY B N   1 
ATOM   3987 C  CA  . GLY B 2 260 ? 87.241  25.282  28.151  1.00 12.35 ? 261  GLY B CA  1 
ATOM   3988 C  C   . GLY B 2 260 ? 85.832  25.116  28.683  1.00 10.83 ? 261  GLY B C   1 
ATOM   3989 O  O   . GLY B 2 260 ? 84.966  26.000  28.503  1.00 12.05 ? 261  GLY B O   1 
ATOM   3990 N  N   . ILE B 2 261 ? 85.533  23.982  29.306  1.00 12.47 ? 262  ILE B N   1 
ATOM   3991 C  CA  . ILE B 2 261 ? 84.183  23.772  29.814  1.00 12.67 ? 262  ILE B CA  1 
ATOM   3992 C  C   . ILE B 2 261 ? 83.713  24.920  30.731  1.00 13.84 ? 262  ILE B C   1 
ATOM   3993 O  O   . ILE B 2 261 ? 82.561  25.399  30.627  1.00 14.83 ? 262  ILE B O   1 
ATOM   3994 C  CB  . ILE B 2 261 ? 84.072  22.466  30.617  1.00 13.41 ? 262  ILE B CB  1 
ATOM   3995 C  CG1 . ILE B 2 261 ? 84.359  21.263  29.684  1.00 14.17 ? 262  ILE B CG1 1 
ATOM   3996 C  CG2 . ILE B 2 261 ? 82.629  22.314  31.216  1.00 14.39 ? 262  ILE B CG2 1 
ATOM   3997 C  CD1 . ILE B 2 261 ? 83.519  21.256  28.373  1.00 13.62 ? 262  ILE B CD1 1 
ATOM   3998 N  N   . GLU B 2 262 ? 84.632  25.384  31.581  1.00 14.50 ? 263  GLU B N   1 
ATOM   3999 C  CA  . GLU B 2 262 ? 84.271  26.454  32.537  1.00 17.53 ? 263  GLU B CA  1 
ATOM   4000 C  C   . GLU B 2 262 ? 83.935  27.780  31.893  1.00 17.31 ? 263  GLU B C   1 
ATOM   4001 O  O   . GLU B 2 262 ? 83.333  28.654  32.550  1.00 19.70 ? 263  GLU B O   1 
ATOM   4002 C  CB  . GLU B 2 262 ? 85.410  26.643  33.554  1.00 20.55 ? 263  GLU B CB  1 
ATOM   4003 C  CG  . GLU B 2 262 ? 86.704  27.277  33.005  1.00 23.81 ? 263  GLU B CG  1 
ATOM   4004 C  CD  . GLU B 2 262 ? 87.528  26.414  32.013  1.00 27.38 ? 263  GLU B CD  1 
ATOM   4005 O  OE1 . GLU B 2 262 ? 87.344  25.147  31.946  1.00 24.03 ? 263  GLU B OE1 1 
ATOM   4006 O  OE2 . GLU B 2 262 ? 88.383  27.036  31.321  1.00 27.00 ? 263  GLU B OE2 1 
ATOM   4007 N  N   . THR B 2 263 ? 84.320  27.980  30.634  1.00 14.66 ? 264  THR B N   1 
ATOM   4008 C  CA  . THR B 2 263 ? 83.998  29.225  29.929  1.00 15.11 ? 264  THR B CA  1 
ATOM   4009 C  C   . THR B 2 263 ? 82.589  29.214  29.384  1.00 16.10 ? 264  THR B C   1 
ATOM   4010 O  O   . THR B 2 263 ? 82.091  30.269  28.967  1.00 17.36 ? 264  THR B O   1 
ATOM   4011 C  CB  . THR B 2 263 ? 84.924  29.485  28.701  1.00 16.32 ? 264  THR B CB  1 
ATOM   4012 O  OG1 . THR B 2 263 ? 84.641  28.505  27.674  1.00 14.83 ? 264  THR B OG1 1 
ATOM   4013 C  CG2 . THR B 2 263 ? 86.380  29.387  29.065  1.00 16.13 ? 264  THR B CG2 1 
ATOM   4014 N  N   . GLY B 2 264 ? 81.991  28.019  29.321  1.00 15.00 ? 265  GLY B N   1 
ATOM   4015 C  CA  . GLY B 2 264 ? 80.676  27.869  28.735  1.00 16.56 ? 265  GLY B CA  1 
ATOM   4016 C  C   . GLY B 2 264 ? 80.738  27.828  27.193  1.00 15.57 ? 265  GLY B C   1 
ATOM   4017 O  O   . GLY B 2 264 ? 79.699  27.592  26.562  1.00 16.86 ? 265  GLY B O   1 
ATOM   4018 N  N   . GLU B 2 265 ? 81.904  28.065  26.581  1.00 13.63 ? 266  GLU B N   1 
ATOM   4019 C  CA  . GLU B 2 265 ? 82.036  28.082  25.126  1.00 12.88 ? 266  GLU B CA  1 
ATOM   4020 C  C   . GLU B 2 265 ? 82.615  26.737  24.731  1.00 11.63 ? 266  GLU B C   1 
ATOM   4021 O  O   . GLU B 2 265 ? 83.828  26.568  24.580  1.00 12.03 ? 266  GLU B O   1 
ATOM   4022 C  CB  . GLU B 2 265 ? 82.952  29.248  24.695  1.00 16.20 ? 266  GLU B CB  1 
ATOM   4023 C  CG  . GLU B 2 265 ? 82.315  30.561  25.133  1.00 21.64 ? 266  GLU B CG  1 
ATOM   4024 C  CD  . GLU B 2 265 ? 83.218  31.756  24.888  1.00 26.93 ? 266  GLU B CD  1 
ATOM   4025 O  OE1 . GLU B 2 265 ? 83.842  31.810  23.816  1.00 30.57 ? 266  GLU B OE1 1 
ATOM   4026 O  OE2 . GLU B 2 265 ? 83.274  32.645  25.777  1.00 34.27 ? 266  GLU B OE2 1 
ATOM   4027 N  N   . HIS B 2 266 ? 81.702  25.765  24.614  1.00 12.77 ? 267  HIS B N   1 
ATOM   4028 C  CA  . HIS B 2 266 ? 82.090  24.410  24.246  1.00 11.39 ? 267  HIS B CA  1 
ATOM   4029 C  C   . HIS B 2 266 ? 80.958  23.736  23.481  1.00 11.06 ? 267  HIS B C   1 
ATOM   4030 O  O   . HIS B 2 266 ? 79.955  24.367  23.154  1.00 11.01 ? 267  HIS B O   1 
ATOM   4031 C  CB  . HIS B 2 266 ? 82.410  23.610  25.514  1.00 11.42 ? 267  HIS B CB  1 
ATOM   4032 C  CG  . HIS B 2 266 ? 81.255  23.483  26.462  1.00 11.50 ? 267  HIS B CG  1 
ATOM   4033 N  ND1 . HIS B 2 266 ? 80.224  22.589  26.266  1.00 10.30 ? 267  HIS B ND1 1 
ATOM   4034 C  CD2 . HIS B 2 266 ? 80.971  24.136  27.614  1.00 12.74 ? 267  HIS B CD2 1 
ATOM   4035 C  CE1 . HIS B 2 266 ? 79.357  22.695  27.257  1.00 12.11 ? 267  HIS B CE1 1 
ATOM   4036 N  NE2 . HIS B 2 266 ? 79.786  23.627  28.089  1.00 12.53 ? 267  HIS B NE2 1 
ATOM   4037 N  N   . GLY B 2 267 ? 81.163  22.469  23.162  1.00 10.64 ? 268  GLY B N   1 
ATOM   4038 C  CA  . GLY B 2 267 ? 80.119  21.682  22.487  1.00 9.73  ? 268  GLY B CA  1 
ATOM   4039 C  C   . GLY B 2 267 ? 80.040  20.332  23.118  1.00 9.46  ? 268  GLY B C   1 
ATOM   4040 O  O   . GLY B 2 267 ? 80.030  19.281  22.416  1.00 10.37 ? 268  GLY B O   1 
ATOM   4041 N  N   . ALA B 2 268 ? 79.880  20.292  24.432  1.00 8.67  ? 269  ALA B N   1 
ATOM   4042 C  CA  . ALA B 2 268 ? 79.881  19.025  25.159  1.00 9.51  ? 269  ALA B CA  1 
ATOM   4043 C  C   . ALA B 2 268 ? 78.602  18.819  25.929  1.00 8.24  ? 269  ALA B C   1 
ATOM   4044 O  O   . ALA B 2 268 ? 78.602  18.717  27.164  1.00 9.05  ? 269  ALA B O   1 
ATOM   4045 C  CB  . ALA B 2 268 ? 81.079  18.975  26.142  1.00 10.97 ? 269  ALA B CB  1 
ATOM   4046 N  N   . PRO B 2 269 ? 77.489  18.705  25.198  1.00 8.42  ? 270  PRO B N   1 
ATOM   4047 C  CA  . PRO B 2 269 ? 76.205  18.504  25.885  1.00 9.35  ? 270  PRO B CA  1 
ATOM   4048 C  C   . PRO B 2 269 ? 76.058  17.186  26.619  1.00 9.62  ? 270  PRO B C   1 
ATOM   4049 O  O   . PRO B 2 269 ? 75.343  17.122  27.612  1.00 10.13 ? 270  PRO B O   1 
ATOM   4050 C  CB  . PRO B 2 269 ? 75.152  18.601  24.737  1.00 9.88  ? 270  PRO B CB  1 
ATOM   4051 C  CG  . PRO B 2 269 ? 75.965  18.089  23.536  1.00 9.72  ? 270  PRO B CG  1 
ATOM   4052 C  CD  . PRO B 2 269 ? 77.343  18.771  23.732  1.00 8.61  ? 270  PRO B CD  1 
ATOM   4053 N  N   . LEU B 2 270 ? 76.688  16.108  26.141  1.00 7.99  ? 271  LEU B N   1 
ATOM   4054 C  CA  . LEU B 2 270 ? 76.493  14.830  26.836  1.00 9.03  ? 271  LEU B CA  1 
ATOM   4055 C  C   . LEU B 2 270 ? 76.927  14.915  28.290  1.00 9.35  ? 271  LEU B C   1 
ATOM   4056 O  O   . LEU B 2 270 ? 76.184  14.494  29.175  1.00 11.15 ? 271  LEU B O   1 
ATOM   4057 C  CB  . LEU B 2 270 ? 77.217  13.722  26.101  1.00 9.90  ? 271  LEU B CB  1 
ATOM   4058 C  CG  A LEU B 2 270 ? 76.732  12.285  26.434  0.70 9.99  ? 271  LEU B CG  1 
ATOM   4059 C  CG  B LEU B 2 270 ? 77.110  12.291  26.654  0.30 9.01  ? 271  LEU B CG  1 
ATOM   4060 C  CD1 A LEU B 2 270 ? 77.065  11.304  25.297  0.70 10.37 ? 271  LEU B CD1 1 
ATOM   4061 C  CD1 B LEU B 2 270 ? 75.650  11.944  27.019  0.30 9.15  ? 271  LEU B CD1 1 
ATOM   4062 C  CD2 A LEU B 2 270 ? 77.369  11.796  27.735  0.70 11.76 ? 271  LEU B CD2 1 
ATOM   4063 C  CD2 B LEU B 2 270 ? 77.681  11.316  25.597  0.30 8.87  ? 271  LEU B CD2 1 
ATOM   4064 N  N   . LYS B 2 271 ? 78.128  15.487  28.518  1.00 9.44  ? 272  LYS B N   1 
ATOM   4065 C  CA  . LYS B 2 271 ? 78.588  15.572  29.901  1.00 10.42 ? 272  LYS B CA  1 
ATOM   4066 C  C   . LYS B 2 271 ? 78.349  16.901  30.591  1.00 11.24 ? 272  LYS B C   1 
ATOM   4067 O  O   . LYS B 2 271 ? 78.447  16.936  31.817  1.00 13.70 ? 272  LYS B O   1 
ATOM   4068 C  CB  . LYS B 2 271 ? 80.096  15.269  29.946  1.00 10.34 ? 272  LYS B CB  1 
ATOM   4069 C  CG  . LYS B 2 271 ? 80.452  13.828  29.480  1.00 11.34 ? 272  LYS B CG  1 
ATOM   4070 C  CD  . LYS B 2 271 ? 79.807  12.676  30.287  1.00 11.00 ? 272  LYS B CD  1 
ATOM   4071 C  CE  . LYS B 2 271 ? 80.254  12.663  31.797  1.00 10.65 ? 272  LYS B CE  1 
ATOM   4072 N  NZ  . LYS B 2 271 ? 81.669  12.147  31.924  1.00 12.18 ? 272  LYS B NZ  1 
ATOM   4073 N  N   . HIS B 2 272 ? 78.051  17.937  29.848  1.00 11.57 ? 273  HIS B N   1 
ATOM   4074 C  CA  . HIS B 2 272 ? 77.867  19.257  30.448  1.00 14.12 ? 273  HIS B CA  1 
ATOM   4075 C  C   . HIS B 2 272 ? 76.619  19.995  29.991  1.00 15.91 ? 273  HIS B C   1 
ATOM   4076 O  O   . HIS B 2 272 ? 76.523  21.217  30.122  1.00 19.26 ? 273  HIS B O   1 
ATOM   4077 C  CB  . HIS B 2 272 ? 79.106  20.105  30.176  1.00 13.27 ? 273  HIS B CB  1 
ATOM   4078 C  CG  . HIS B 2 272 ? 80.370  19.480  30.673  1.00 14.41 ? 273  HIS B CG  1 
ATOM   4079 N  ND1 . HIS B 2 272 ? 80.663  19.365  32.015  1.00 15.45 ? 273  HIS B ND1 1 
ATOM   4080 C  CD2 . HIS B 2 272 ? 81.391  18.885  30.012  1.00 15.52 ? 273  HIS B CD2 1 
ATOM   4081 C  CE1 . HIS B 2 272 ? 81.810  18.725  32.158  1.00 15.17 ? 273  HIS B CE1 1 
ATOM   4082 N  NE2 . HIS B 2 272 ? 82.272  18.422  30.958  1.00 16.00 ? 273  HIS B NE2 1 
ATOM   4083 N  N   . GLY B 2 273 ? 75.647  19.294  29.433  1.00 14.50 ? 274  GLY B N   1 
ATOM   4084 C  CA  . GLY B 2 273 ? 74.395  19.943  29.044  1.00 14.94 ? 274  GLY B CA  1 
ATOM   4085 C  C   . GLY B 2 273 ? 73.306  19.442  29.973  1.00 17.15 ? 274  GLY B C   1 
ATOM   4086 O  O   . GLY B 2 273 ? 73.585  19.047  31.101  1.00 19.03 ? 274  GLY B O   1 
ATOM   4087 N  N   . ARG B 2 274 ? 72.056  19.450  29.500  1.00 15.71 ? 275  ARG B N   1 
ATOM   4088 C  CA  . ARG B 2 274 ? 70.903  19.038  30.264  1.00 15.78 ? 275  ARG B CA  1 
ATOM   4089 C  C   . ARG B 2 274 ? 69.947  18.355  29.266  1.00 13.76 ? 275  ARG B C   1 
ATOM   4090 O  O   . ARG B 2 274 ? 69.781  18.824  28.134  1.00 13.53 ? 275  ARG B O   1 
ATOM   4091 C  CB  . ARG B 2 274 ? 70.240  20.308  30.865  1.00 18.61 ? 275  ARG B CB  1 
ATOM   4092 C  CG  . ARG B 2 274 ? 69.174  20.128  31.845  1.00 20.19 ? 275  ARG B CG  1 
ATOM   4093 C  CD  . ARG B 2 274 ? 69.139  21.447  32.686  1.00 19.26 ? 275  ARG B CD  1 
ATOM   4094 N  NE  . ARG B 2 274 ? 68.846  22.657  31.932  1.00 18.56 ? 275  ARG B NE  1 
ATOM   4095 C  CZ  . ARG B 2 274 ? 67.616  22.952  31.547  1.00 19.32 ? 275  ARG B CZ  1 
ATOM   4096 N  NH1 . ARG B 2 274 ? 67.367  24.051  30.858  1.00 18.80 ? 275  ARG B NH1 1 
ATOM   4097 N  NH2 . ARG B 2 274 ? 66.624  22.112  31.854  1.00 20.37 ? 275  ARG B NH2 1 
ATOM   4098 N  N   . VAL B 2 275 ? 69.342  17.277  29.721  1.00 13.68 ? 276  VAL B N   1 
ATOM   4099 C  CA  . VAL B 2 275 ? 68.384  16.590  28.816  1.00 12.86 ? 276  VAL B CA  1 
ATOM   4100 C  C   . VAL B 2 275 ? 67.202  17.506  28.433  1.00 11.51 ? 276  VAL B C   1 
ATOM   4101 O  O   . VAL B 2 275 ? 66.631  18.244  29.263  1.00 12.41 ? 276  VAL B O   1 
ATOM   4102 C  CB  . VAL B 2 275 ? 67.846  15.321  29.463  1.00 14.29 ? 276  VAL B CB  1 
ATOM   4103 C  CG1 A VAL B 2 275 ? 66.874  14.573  28.520  0.80 11.48 ? 276  VAL B CG1 1 
ATOM   4104 C  CG1 B VAL B 2 275 ? 68.971  14.315  29.639  0.20 15.56 ? 276  VAL B CG1 1 
ATOM   4105 C  CG2 A VAL B 2 275 ? 68.997  14.399  29.788  0.80 17.46 ? 276  VAL B CG2 1 
ATOM   4106 C  CG2 B VAL B 2 275 ? 67.170  15.631  30.765  0.20 14.39 ? 276  VAL B CG2 1 
ATOM   4107 N  N   . GLY B 2 276 ? 66.891  17.441  27.144  1.00 9.82  ? 277  GLY B N   1 
ATOM   4108 C  CA  . GLY B 2 276 ? 65.765  18.153  26.601  1.00 9.78  ? 277  GLY B CA  1 
ATOM   4109 C  C   . GLY B 2 276 ? 65.129  17.388  25.466  1.00 9.97  ? 277  GLY B C   1 
ATOM   4110 O  O   . GLY B 2 276 ? 65.513  16.232  25.214  1.00 10.12 ? 277  GLY B O   1 
ATOM   4111 N  N   . ILE B 2 277 ? 64.122  17.989  24.852  1.00 8.70  ? 278  ILE B N   1 
ATOM   4112 C  CA  . ILE B 2 277 ? 63.465  17.360  23.717  1.00 9.09  ? 278  ILE B CA  1 
ATOM   4113 C  C   . ILE B 2 277 ? 63.557  18.334  22.550  1.00 10.43 ? 278  ILE B C   1 
ATOM   4114 O  O   . ILE B 2 277 ? 62.956  19.421  22.562  1.00 11.73 ? 278  ILE B O   1 
ATOM   4115 C  CB  . ILE B 2 277 ? 61.990  17.034  24.036  1.00 8.86  ? 278  ILE B CB  1 
ATOM   4116 C  CG1 . ILE B 2 277 ? 61.920  15.998  25.175  1.00 10.68 ? 278  ILE B CG1 1 
ATOM   4117 C  CG2 . ILE B 2 277 ? 61.300  16.438  22.756  1.00 10.22 ? 278  ILE B CG2 1 
ATOM   4118 C  CD1 . ILE B 2 277 ? 60.409  15.759  25.660  1.00 10.66 ? 278  ILE B CD1 1 
ATOM   4119 N  N   . TYR B 2 278 ? 64.316  17.959  21.540  1.00 10.33 ? 279  TYR B N   1 
ATOM   4120 C  CA  . TYR B 2 278 ? 64.495  18.779  20.356  1.00 11.56 ? 279  TYR B CA  1 
ATOM   4121 C  C   . TYR B 2 278 ? 65.047  17.916  19.227  1.00 11.08 ? 279  TYR B C   1 
ATOM   4122 O  O   . TYR B 2 278 ? 65.609  16.849  19.466  1.00 10.01 ? 279  TYR B O   1 
ATOM   4123 C  CB  . TYR B 2 278 ? 65.446  19.942  20.663  1.00 14.58 ? 279  TYR B CB  1 
ATOM   4124 C  CG  . TYR B 2 278 ? 65.855  20.724  19.438  1.00 19.31 ? 279  TYR B CG  1 
ATOM   4125 C  CD1 . TYR B 2 278 ? 64.908  21.404  18.675  1.00 20.40 ? 279  TYR B CD1 1 
ATOM   4126 C  CD2 . TYR B 2 278 ? 67.182  20.739  19.012  1.00 20.90 ? 279  TYR B CD2 1 
ATOM   4127 C  CE1 . TYR B 2 278 ? 65.271  22.078  17.510  1.00 20.51 ? 279  TYR B CE1 1 
ATOM   4128 C  CE2 . TYR B 2 278 ? 67.557  21.409  17.849  1.00 23.33 ? 279  TYR B CE2 1 
ATOM   4129 C  CZ  . TYR B 2 278 ? 66.595  22.073  17.104  1.00 23.24 ? 279  TYR B CZ  1 
ATOM   4130 O  OH  . TYR B 2 278 ? 66.955  22.719  15.941  1.00 25.33 ? 279  TYR B OH  1 
ATOM   4131 N  N   . PHE B 2 279 ? 64.887  18.394  18.000  1.00 11.71 ? 280  PHE B N   1 
ATOM   4132 C  CA  . PHE B 2 279 ? 65.324  17.675  16.812  1.00 13.39 ? 280  PHE B CA  1 
ATOM   4133 C  C   . PHE B 2 279 ? 64.754  16.259  16.795  1.00 12.50 ? 280  PHE B C   1 
ATOM   4134 O  O   . PHE B 2 279 ? 65.416  15.306  16.377  1.00 12.13 ? 280  PHE B O   1 
ATOM   4135 C  CB  . PHE B 2 279 ? 66.852  17.636  16.708  1.00 17.18 ? 280  PHE B CB  1 
ATOM   4136 C  CG  . PHE B 2 279 ? 67.346  17.210  15.348  1.00 20.14 ? 280  PHE B CG  1 
ATOM   4137 C  CD1 . PHE B 2 279 ? 66.787  17.753  14.192  1.00 21.77 ? 280  PHE B CD1 1 
ATOM   4138 C  CD2 . PHE B 2 279 ? 68.361  16.267  15.221  1.00 21.76 ? 280  PHE B CD2 1 
ATOM   4139 C  CE1 . PHE B 2 279 ? 67.231  17.360  12.927  1.00 22.40 ? 280  PHE B CE1 1 
ATOM   4140 C  CE2 . PHE B 2 279 ? 68.812  15.869  13.961  1.00 22.65 ? 280  PHE B CE2 1 
ATOM   4141 C  CZ  . PHE B 2 279 ? 68.245  16.416  12.813  1.00 22.41 ? 280  PHE B CZ  1 
ATOM   4142 N  N   . GLY B 2 280 ? 63.544  16.119  17.306  1.00 9.66  ? 281  GLY B N   1 
ATOM   4143 C  CA  . GLY B 2 280 ? 62.870  14.843  17.253  1.00 9.96  ? 281  GLY B CA  1 
ATOM   4144 C  C   . GLY B 2 280 ? 63.266  13.812  18.269  1.00 8.32  ? 281  GLY B C   1 
ATOM   4145 O  O   . GLY B 2 280 ? 62.834  12.659  18.214  1.00 9.88  ? 281  GLY B O   1 
ATOM   4146 N  N   . MET B 2 281 ? 64.049  14.228  19.272  1.00 8.80  ? 282  MET B N   1 
ATOM   4147 C  CA  . MET B 2 281 ? 64.525  13.241  20.231  1.00 8.75  ? 282  MET B CA  1 
ATOM   4148 C  C   . MET B 2 281 ? 64.671  13.793  21.642  1.00 7.14  ? 282  MET B C   1 
ATOM   4149 O  O   . MET B 2 281 ? 64.779  15.032  21.805  1.00 9.16  ? 282  MET B O   1 
ATOM   4150 C  CB  . MET B 2 281 ? 65.920  12.731  19.828  1.00 9.60  ? 282  MET B CB  1 
ATOM   4151 C  CG  . MET B 2 281 ? 66.934  13.839  19.638  1.00 8.99  ? 282  MET B CG  1 
ATOM   4152 S  SD  . MET B 2 281 ? 68.610  13.208  19.330  1.00 9.75  ? 282  MET B SD  1 
ATOM   4153 C  CE  . MET B 2 281 ? 69.537  14.655  19.422  1.00 10.29 ? 282  MET B CE  1 
ATOM   4154 N  N   . LYS B 2 282 ? 64.657  12.913  22.630  1.00 7.05  ? 283  LYS B N   1 
ATOM   4155 C  CA  . LYS B 2 282 ? 64.956  13.278  24.008  1.00 8.48  ? 283  LYS B CA  1 
ATOM   4156 C  C   . LYS B 2 282 ? 66.460  12.910  24.171  1.00 8.60  ? 283  LYS B C   1 
ATOM   4157 O  O   . LYS B 2 282 ? 66.883  11.737  24.089  1.00 8.40  ? 283  LYS B O   1 
ATOM   4158 C  CB  . LYS B 2 282 ? 64.071  12.470  24.974  1.00 9.74  ? 283  LYS B CB  1 
ATOM   4159 C  CG  . LYS B 2 282 ? 64.387  12.896  26.397  1.00 9.92  ? 283  LYS B CG  1 
ATOM   4160 C  CD  . LYS B 2 282 ? 63.509  12.094  27.374  1.00 11.87 ? 283  LYS B CD  1 
ATOM   4161 C  CE  . LYS B 2 282 ? 62.096  12.583  27.249  1.00 13.45 ? 283  LYS B CE  1 
ATOM   4162 N  NZ  . LYS B 2 282 ? 61.201  11.836  28.243  1.00 17.00 ? 283  LYS B NZ  1 
ATOM   4163 N  N   . ALA B 2 283 ? 67.262  13.933  24.444  1.00 7.83  ? 284  ALA B N   1 
ATOM   4164 C  CA  . ALA B 2 283 ? 68.705  13.736  24.554  1.00 7.83  ? 284  ALA B CA  1 
ATOM   4165 C  C   . ALA B 2 283 ? 69.339  14.946  25.262  1.00 9.03  ? 284  ALA B C   1 
ATOM   4166 O  O   . ALA B 2 283 ? 68.751  16.006  25.343  1.00 9.64  ? 284  ALA B O   1 
ATOM   4167 C  CB  . ALA B 2 283 ? 69.299  13.654  23.121  1.00 8.66  ? 284  ALA B CB  1 
ATOM   4168 N  N   . PRO B 2 284 ? 70.577  14.802  25.717  1.00 9.38  ? 285  PRO B N   1 
ATOM   4169 C  CA  . PRO B 2 284 ? 71.287  15.933  26.351  1.00 9.77  ? 285  PRO B CA  1 
ATOM   4170 C  C   . PRO B 2 284 ? 71.461  17.057  25.348  1.00 11.15 ? 285  PRO B C   1 
ATOM   4171 O  O   . PRO B 2 284 ? 71.809  16.801  24.185  1.00 11.57 ? 285  PRO B O   1 
ATOM   4172 C  CB  . PRO B 2 284 ? 72.691  15.379  26.642  1.00 12.28 ? 285  PRO B CB  1 
ATOM   4173 C  CG  . PRO B 2 284 ? 72.530  13.892  26.650  1.00 12.30 ? 285  PRO B CG  1 
ATOM   4174 C  CD  . PRO B 2 284 ? 71.362  13.540  25.795  1.00 10.24 ? 285  PRO B CD  1 
ATOM   4175 N  N   . MET B 2 285 ? 71.249  18.322  25.761  1.00 11.20 ? 286  MET B N   1 
ATOM   4176 C  CA  . MET B 2 285 ? 71.508  19.404  24.822  1.00 14.14 ? 286  MET B CA  1 
ATOM   4177 C  C   . MET B 2 285 ? 72.056  20.645  25.442  1.00 13.17 ? 286  MET B C   1 
ATOM   4178 O  O   . MET B 2 285 ? 72.025  20.745  26.646  1.00 14.14 ? 286  MET B O   1 
ATOM   4179 C  CB  A MET B 2 285 ? 70.241  19.759  24.155  0.50 17.52 ? 286  MET B CB  1 
ATOM   4180 C  CB  B MET B 2 285 ? 70.313  19.742  23.963  0.50 17.69 ? 286  MET B CB  1 
ATOM   4181 C  CG  A MET B 2 285 ? 69.669  18.536  23.573  0.50 16.82 ? 286  MET B CG  1 
ATOM   4182 C  CG  B MET B 2 285 ? 69.018  19.611  24.676  0.50 14.25 ? 286  MET B CG  1 
ATOM   4183 S  SD  A MET B 2 285 ? 68.695  19.019  22.399  0.50 12.44 ? 286  MET B SD  1 
ATOM   4184 S  SD  B MET B 2 285 ? 67.597  19.730  23.639  0.50 17.95 ? 286  MET B SD  1 
ATOM   4185 C  CE  A MET B 2 285 ? 67.712  17.498  22.176  0.50 11.29 ? 286  MET B CE  1 
ATOM   4186 C  CE  B MET B 2 285 ? 67.457  17.937  22.998  0.50 14.42 ? 286  MET B CE  1 
ATOM   4187 N  N   . MET B 2 286 ? 72.506  21.522  24.539  1.00 14.80 ? 287  MET B N   1 
ATOM   4188 C  CA  . MET B 2 286 ? 73.030  22.848  24.889  1.00 15.97 ? 287  MET B CA  1 
ATOM   4189 C  C   . MET B 2 286 ? 71.722  23.698  24.874  1.00 13.15 ? 287  MET B C   1 
ATOM   4190 O  O   . MET B 2 286 ? 71.142  23.888  23.804  1.00 15.56 ? 287  MET B O   1 
ATOM   4191 C  CB  . MET B 2 286 ? 73.968  23.372  23.779  1.00 16.79 ? 287  MET B CB  1 
ATOM   4192 C  CG  A MET B 2 286 ? 75.188  22.486  23.384  0.50 17.56 ? 287  MET B CG  1 
ATOM   4193 C  CG  B MET B 2 286 ? 75.195  22.479  23.476  0.50 17.35 ? 287  MET B CG  1 
ATOM   4194 S  SD  A MET B 2 286 ? 76.767  22.812  24.211  0.50 12.86 ? 287  MET B SD  1 
ATOM   4195 S  SD  B MET B 2 286 ? 76.167  22.360  24.929  0.50 12.90 ? 287  MET B SD  1 
ATOM   4196 C  CE  A MET B 2 286 ? 76.627  24.460  25.001  0.50 16.24 ? 287  MET B CE  1 
ATOM   4197 C  CE  B MET B 2 286 ? 77.158  24.042  24.880  0.50 13.26 ? 287  MET B CE  1 
ATOM   4198 N  N   . GLN B 2 287 ? 71.366  24.215  26.027  1.00 15.84 ? 288  GLN B N   1 
ATOM   4199 C  CA  . GLN B 2 287 ? 70.124  25.025  26.151  1.00 14.57 ? 288  GLN B CA  1 
ATOM   4200 C  C   . GLN B 2 287 ? 70.214  26.006  27.318  1.00 16.41 ? 288  GLN B C   1 
ATOM   4201 O  O   . GLN B 2 287 ? 70.981  25.833  28.272  1.00 17.41 ? 288  GLN B O   1 
ATOM   4202 C  CB  . GLN B 2 287 ? 68.908  24.068  26.337  1.00 15.12 ? 288  GLN B CB  1 
ATOM   4203 C  CG  . GLN B 2 287 ? 69.017  23.087  27.524  1.00 14.18 ? 288  GLN B CG  1 
ATOM   4204 C  CD  . GLN B 2 287 ? 67.689  22.331  27.813  1.00 16.99 ? 288  GLN B CD  1 
ATOM   4205 O  OE1 . GLN B 2 287 ? 66.652  22.951  27.744  1.00 15.83 ? 288  GLN B OE1 1 
ATOM   4206 N  NE2 . GLN B 2 287 ? 67.733  21.039  28.173  1.00 14.09 ? 288  GLN B NE2 1 
ATOM   4207 N  N   . THR B 2 288 ? 69.441  27.086  27.205  1.00 16.02 ? 289  THR B N   1 
ATOM   4208 C  CA  . THR B 2 288 ? 69.425  28.068  28.285  1.00 16.72 ? 289  THR B CA  1 
ATOM   4209 C  C   . THR B 2 288 ? 68.643  27.510  29.496  1.00 16.72 ? 289  THR B C   1 
ATOM   4210 O  O   . THR B 2 288 ? 67.958  26.458  29.408  1.00 15.30 ? 289  THR B O   1 
ATOM   4211 C  CB  . THR B 2 288 ? 68.765  29.360  27.815  1.00 15.59 ? 289  THR B CB  1 
ATOM   4212 O  OG1 . THR B 2 288 ? 67.355  29.111  27.564  1.00 14.56 ? 289  THR B OG1 1 
ATOM   4213 C  CG2 . THR B 2 288 ? 69.405  29.887  26.571  1.00 13.96 ? 289  THR B CG2 1 
ATOM   4214 N  N   . ALA B 2 289 ? 68.640  28.234  30.608  1.00 15.95 ? 290  ALA B N   1 
ATOM   4215 C  CA  . ALA B 2 289 ? 67.948  27.763  31.790  1.00 16.58 ? 290  ALA B CA  1 
ATOM   4216 C  C   . ALA B 2 289 ? 66.412  27.712  31.531  1.00 16.53 ? 290  ALA B C   1 
ATOM   4217 O  O   . ALA B 2 289 ? 65.720  26.951  32.212  1.00 20.22 ? 290  ALA B O   1 
ATOM   4218 C  CB  . ALA B 2 289 ? 68.251  28.692  33.014  1.00 19.20 ? 290  ALA B CB  1 
ATOM   4219 N  N   . ASP B 2 290 ? 65.950  28.516  30.552  1.00 16.61 ? 291  ASP B N   1 
ATOM   4220 C  CA  . ASP B 2 290 ? 64.536  28.576  30.136  1.00 17.69 ? 291  ASP B CA  1 
ATOM   4221 C  C   . ASP B 2 290 ? 64.136  27.513  29.132  1.00 17.50 ? 291  ASP B C   1 
ATOM   4222 O  O   . ASP B 2 290 ? 62.952  27.345  28.824  1.00 17.80 ? 291  ASP B O   1 
ATOM   4223 C  CB  . ASP B 2 290 ? 64.210  29.900  29.440  1.00 21.02 ? 291  ASP B CB  1 
ATOM   4224 C  CG  . ASP B 2 290 ? 64.032  31.018  30.382  1.00 25.77 ? 291  ASP B CG  1 
ATOM   4225 O  OD1 . ASP B 2 290 ? 64.020  30.763  31.613  1.00 27.18 ? 291  ASP B OD1 1 
ATOM   4226 O  OD2 . ASP B 2 290 ? 63.923  32.138  29.852  1.00 25.82 ? 291  ASP B OD2 1 
ATOM   4227 N  N   . GLY B 2 291 ? 65.117  26.838  28.565  1.00 14.20 ? 292  GLY B N   1 
ATOM   4228 C  CA  . GLY B 2 291 ? 64.780  25.824  27.590  1.00 13.79 ? 292  GLY B CA  1 
ATOM   4229 C  C   . GLY B 2 291 ? 64.941  26.235  26.146  1.00 14.07 ? 292  GLY B C   1 
ATOM   4230 O  O   . GLY B 2 291 ? 64.456  25.527  25.267  1.00 14.62 ? 292  GLY B O   1 
ATOM   4231 N  N   . GLN B 2 292 ? 65.625  27.360  25.837  1.00 12.46 ? 293  GLN B N   1 
ATOM   4232 C  CA  . GLN B 2 292 ? 65.834  27.726  24.432  1.00 12.40 ? 293  GLN B CA  1 
ATOM   4233 C  C   . GLN B 2 292 ? 67.112  26.981  24.015  1.00 13.77 ? 293  GLN B C   1 
ATOM   4234 O  O   . GLN B 2 292 ? 68.042  26.901  24.798  1.00 15.46 ? 293  GLN B O   1 
ATOM   4235 C  CB  . GLN B 2 292 ? 66.034  29.244  24.299  1.00 12.55 ? 293  GLN B CB  1 
ATOM   4236 C  CG  . GLN B 2 292 ? 64.860  30.037  24.959  1.00 14.90 ? 293  GLN B CG  1 
ATOM   4237 C  CD  . GLN B 2 292 ? 63.511  29.831  24.276  1.00 11.85 ? 293  GLN B CD  1 
ATOM   4238 O  OE1 . GLN B 2 292 ? 63.396  29.160  23.249  1.00 13.08 ? 293  GLN B OE1 1 
ATOM   4239 N  NE2 . GLN B 2 292 ? 62.440  30.481  24.828  1.00 13.71 ? 293  GLN B NE2 1 
ATOM   4240 N  N   A ILE B 2 293 ? 67.137  26.535  22.754  0.60 12.84 ? 294  ILE B N   1 
ATOM   4241 N  N   B ILE B 2 293 ? 67.172  26.416  22.832  0.40 14.14 ? 294  ILE B N   1 
ATOM   4242 C  CA  A ILE B 2 293 ? 68.262  25.778  22.186  0.60 13.29 ? 294  ILE B CA  1 
ATOM   4243 C  CA  B ILE B 2 293 ? 68.389  25.691  22.525  0.40 14.89 ? 294  ILE B CA  1 
ATOM   4244 C  C   A ILE B 2 293 ? 69.380  26.724  21.747  0.60 12.74 ? 294  ILE B C   1 
ATOM   4245 C  C   B ILE B 2 293 ? 69.539  26.707  22.512  0.40 15.15 ? 294  ILE B C   1 
ATOM   4246 O  O   A ILE B 2 293 ? 69.171  27.778  21.097  0.60 12.48 ? 294  ILE B O   1 
ATOM   4247 O  O   B ILE B 2 293 ? 69.372  27.844  22.062  0.40 15.89 ? 294  ILE B O   1 
ATOM   4248 C  CB  A ILE B 2 293 ? 67.823  24.918  20.979  0.60 14.08 ? 294  ILE B CB  1 
ATOM   4249 C  CB  B ILE B 2 293 ? 68.235  24.957  21.204  0.40 15.68 ? 294  ILE B CB  1 
ATOM   4250 C  CG1 A ILE B 2 293 ? 66.520  24.129  21.316  0.60 13.92 ? 294  ILE B CG1 1 
ATOM   4251 C  CG1 B ILE B 2 293 ? 66.956  24.090  21.252  0.40 16.28 ? 294  ILE B CG1 1 
ATOM   4252 C  CG2 A ILE B 2 293 ? 68.969  23.984  20.601  0.60 14.59 ? 294  ILE B CG2 1 
ATOM   4253 C  CG2 B ILE B 2 293 ? 69.462  24.097  20.972  0.40 15.27 ? 294  ILE B CG2 1 
ATOM   4254 C  CD1 A ILE B 2 293 ? 66.577  23.290  22.576  0.60 14.80 ? 294  ILE B CD1 1 
ATOM   4255 C  CD1 B ILE B 2 293 ? 66.959  23.032  22.338  0.40 16.48 ? 294  ILE B CD1 1 
ATOM   4256 N  N   A GLU B 2 294 ? 70.584  26.320  22.118  0.60 13.34 ? 295  GLU B N   1 
ATOM   4257 N  N   B GLU B 2 294 ? 70.680  26.310  23.068  0.40 16.30 ? 295  GLU B N   1 
ATOM   4258 C  CA  A GLU B 2 294 ? 71.785  27.090  21.836  0.60 14.48 ? 295  GLU B CA  1 
ATOM   4259 C  CA  B GLU B 2 294 ? 71.841  27.194  23.125  0.40 17.21 ? 295  GLU B CA  1 
ATOM   4260 C  C   A GLU B 2 294 ? 72.743  26.355  20.905  0.60 14.79 ? 295  GLU B C   1 
ATOM   4261 C  C   B GLU B 2 294 ? 72.830  27.054  22.003  0.40 17.34 ? 295  GLU B C   1 
ATOM   4262 O  O   A GLU B 2 294 ? 72.564  25.174  20.593  0.60 15.09 ? 295  GLU B O   1 
ATOM   4263 O  O   B GLU B 2 294 ? 72.799  26.114  21.209  0.40 17.08 ? 295  GLU B O   1 
ATOM   4264 C  CB  A GLU B 2 294 ? 72.499  27.417  23.151  0.60 16.45 ? 295  GLU B CB  1 
ATOM   4265 C  CB  B GLU B 2 294 ? 72.584  27.004  24.446  0.40 18.05 ? 295  GLU B CB  1 
ATOM   4266 C  CG  A GLU B 2 294 ? 71.665  28.278  24.125  0.60 22.30 ? 295  GLU B CG  1 
ATOM   4267 C  CG  B GLU B 2 294 ? 72.270  28.080  25.482  0.40 22.41 ? 295  GLU B CG  1 
ATOM   4268 C  CD  A GLU B 2 294 ? 72.367  28.541  25.468  0.60 25.46 ? 295  GLU B CD  1 
ATOM   4269 C  CD  B GLU B 2 294 ? 73.032  29.390  25.244  0.40 23.59 ? 295  GLU B CD  1 
ATOM   4270 O  OE1 A GLU B 2 294 ? 72.824  27.570  26.119  0.60 26.19 ? 295  GLU B OE1 1 
ATOM   4271 O  OE1 B GLU B 2 294 ? 73.129  29.859  24.092  0.40 25.09 ? 295  GLU B OE1 1 
ATOM   4272 O  OE2 A GLU B 2 294 ? 72.448  29.728  25.874  0.60 28.22 ? 295  GLU B OE2 1 
ATOM   4273 O  OE2 B GLU B 2 294 ? 73.528  29.955  26.239  0.40 25.98 ? 295  GLU B OE2 1 
ATOM   4274 N  N   A GLU B 2 295 ? 73.781  27.066  20.482  0.60 15.24 ? 296  GLU B N   1 
ATOM   4275 N  N   B GLU B 2 295 ? 73.728  28.022  21.943  0.40 16.32 ? 296  GLU B N   1 
ATOM   4276 C  CA  A GLU B 2 295 ? 74.781  26.492  19.596  0.60 15.26 ? 296  GLU B CA  1 
ATOM   4277 C  CA  B GLU B 2 295 ? 74.750  27.982  20.933  0.40 17.48 ? 296  GLU B CA  1 
ATOM   4278 C  C   A GLU B 2 295 ? 75.915  25.748  20.325  0.60 14.03 ? 296  GLU B C   1 
ATOM   4279 C  C   B GLU B 2 295 ? 75.931  27.210  21.484  0.40 16.56 ? 296  GLU B C   1 
ATOM   4280 O  O   A GLU B 2 295 ? 76.133  25.958  21.513  0.60 14.17 ? 296  GLU B O   1 
ATOM   4281 O  O   B GLU B 2 295 ? 76.304  27.348  22.669  0.40 16.36 ? 296  GLU B O   1 
ATOM   4282 C  CB  A GLU B 2 295 ? 75.422  27.607  18.796  0.60 16.49 ? 296  GLU B CB  1 
ATOM   4283 C  CB  B GLU B 2 295 ? 75.118  29.402  20.518  0.40 18.82 ? 296  GLU B CB  1 
ATOM   4284 C  CG  A GLU B 2 295 ? 74.537  28.284  17.817  0.60 20.03 ? 296  GLU B CG  1 
ATOM   4285 C  CG  B GLU B 2 295 ? 73.854  30.158  20.148  0.40 21.83 ? 296  GLU B CG  1 
ATOM   4286 C  CD  A GLU B 2 295 ? 75.254  29.473  17.210  0.60 22.81 ? 296  GLU B CD  1 
ATOM   4287 C  CD  B GLU B 2 295 ? 74.102  31.329  19.213  0.40 24.36 ? 296  GLU B CD  1 
ATOM   4288 O  OE1 A GLU B 2 295 ? 76.206  29.256  16.416  0.60 25.58 ? 296  GLU B OE1 1 
ATOM   4289 O  OE1 B GLU B 2 295 ? 75.278  31.623  18.896  0.40 26.51 ? 296  GLU B OE1 1 
ATOM   4290 O  OE2 A GLU B 2 295 ? 74.884  30.607  17.559  0.60 25.36 ? 296  GLU B OE2 1 
ATOM   4291 O  OE2 B GLU B 2 295 ? 73.109  31.955  18.801  0.40 25.58 ? 296  GLU B OE2 1 
ATOM   4292 N  N   A SER B 2 296 ? 76.611  24.868  19.606  0.60 14.65 ? 297  SER B N   1 
ATOM   4293 N  N   B SER B 2 296 ? 76.445  26.346  20.611  0.40 17.47 ? 297  SER B N   1 
ATOM   4294 C  CA  A SER B 2 296 ? 77.790  24.234  20.174  0.60 14.82 ? 297  SER B CA  1 
ATOM   4295 C  CA  B SER B 2 296 ? 77.574  25.463  20.852  0.40 18.34 ? 297  SER B CA  1 
ATOM   4296 C  C   A SER B 2 296 ? 79.012  25.050  19.621  0.60 15.32 ? 297  SER B C   1 
ATOM   4297 C  C   B SER B 2 296 ? 78.816  26.117  20.277  0.40 18.34 ? 297  SER B C   1 
ATOM   4298 O  O   A SER B 2 296 ? 78.993  25.368  18.427  0.60 16.34 ? 297  SER B O   1 
ATOM   4299 O  O   B SER B 2 296 ? 78.734  27.156  19.621  0.40 17.28 ? 297  SER B O   1 
ATOM   4300 C  CB  A SER B 2 296 ? 77.892  22.774  19.659  0.60 15.23 ? 297  SER B CB  1 
ATOM   4301 C  CB  B SER B 2 296 ? 77.303  24.132  20.146  0.40 19.40 ? 297  SER B CB  1 
ATOM   4302 O  OG  A SER B 2 296 ? 77.322  21.862  20.576  0.60 14.09 ? 297  SER B OG  1 
ATOM   4303 O  OG  B SER B 2 296 ? 78.386  23.229  20.261  0.40 23.21 ? 297  SER B OG  1 
ATOM   4304 N  N   . TYR B 2 297 ? 79.968  25.488  20.477  1.00 14.83 ? 298  TYR B N   1 
ATOM   4305 C  CA  . TYR B 2 297 ? 81.201  26.081  19.976  1.00 13.51 ? 298  TYR B CA  1 
ATOM   4306 C  C   . TYR B 2 297 ? 82.393  25.138  20.005  1.00 11.40 ? 298  TYR B C   1 
ATOM   4307 O  O   . TYR B 2 297 ? 82.601  24.405  20.971  1.00 11.31 ? 298  TYR B O   1 
ATOM   4308 C  CB  . TYR B 2 297 ? 81.608  27.335  20.759  1.00 13.67 ? 298  TYR B CB  1 
ATOM   4309 C  CG  . TYR B 2 297 ? 83.014  27.754  20.373  1.00 14.27 ? 298  TYR B CG  1 
ATOM   4310 C  CD1 . TYR B 2 297 ? 83.262  28.357  19.138  1.00 13.69 ? 298  TYR B CD1 1 
ATOM   4311 C  CD2 . TYR B 2 297 ? 84.114  27.379  21.152  1.00 14.01 ? 298  TYR B CD2 1 
ATOM   4312 C  CE1 . TYR B 2 297 ? 84.561  28.560  18.679  1.00 13.66 ? 298  TYR B CE1 1 
ATOM   4313 C  CE2 . TYR B 2 297 ? 85.421  27.574  20.699  1.00 13.16 ? 298  TYR B CE2 1 
ATOM   4314 C  CZ  . TYR B 2 297 ? 85.636  28.159  19.460  1.00 13.57 ? 298  TYR B CZ  1 
ATOM   4315 O  OH  . TYR B 2 297 ? 86.915  28.302  18.973  1.00 14.58 ? 298  TYR B OH  1 
ATOM   4316 N  N   . SER B 2 298 ? 83.131  25.148  18.904  1.00 11.32 ? 299  SER B N   1 
ATOM   4317 C  CA  . SER B 2 298 ? 84.388  24.423  18.814  1.00 10.74 ? 299  SER B CA  1 
ATOM   4318 C  C   . SER B 2 298 ? 85.240  25.056  17.692  1.00 11.25 ? 299  SER B C   1 
ATOM   4319 O  O   . SER B 2 298 ? 84.673  25.610  16.720  1.00 13.26 ? 299  SER B O   1 
ATOM   4320 C  CB  . SER B 2 298 ? 84.144  22.932  18.456  1.00 11.60 ? 299  SER B CB  1 
ATOM   4321 O  OG  . SER B 2 298 ? 85.384  22.236  18.231  1.00 10.33 ? 299  SER B OG  1 
ATOM   4322 N  N   . ILE B 2 299 ? 86.564  24.952  17.821  1.00 12.15 ? 300  ILE B N   1 
ATOM   4323 C  CA  . ILE B 2 299 ? 87.417  25.372  16.706  1.00 14.00 ? 300  ILE B CA  1 
ATOM   4324 C  C   . ILE B 2 299 ? 87.063  24.547  15.478  1.00 14.68 ? 300  ILE B C   1 
ATOM   4325 O  O   . ILE B 2 299 ? 87.264  24.994  14.372  1.00 14.75 ? 300  ILE B O   1 
ATOM   4326 C  CB  . ILE B 2 299 ? 88.936  25.170  17.018  1.00 15.20 ? 300  ILE B CB  1 
ATOM   4327 C  CG1 . ILE B 2 299 ? 89.774  25.779  15.883  1.00 16.84 ? 300  ILE B CG1 1 
ATOM   4328 C  CG2 . ILE B 2 299 ? 89.247  23.649  17.341  1.00 15.77 ? 300  ILE B CG2 1 
ATOM   4329 C  CD1 . ILE B 2 299 ? 91.246  25.633  16.159  1.00 20.56 ? 300  ILE B CD1 1 
ATOM   4330 N  N   . SER B 2 300 ? 86.558  23.324  15.671  1.00 12.42 ? 301  SER B N   1 
ATOM   4331 C  CA  . SER B 2 300 ? 86.162  22.469  14.549  1.00 14.42 ? 301  SER B CA  1 
ATOM   4332 C  C   . SER B 2 300 ? 84.657  22.604  14.252  1.00 14.69 ? 301  SER B C   1 
ATOM   4333 O  O   . SER B 2 300 ? 83.778  22.234  15.052  1.00 16.10 ? 301  SER B O   1 
ATOM   4334 C  CB  . SER B 2 300 ? 86.491  21.015  14.879  1.00 13.50 ? 301  SER B CB  1 
ATOM   4335 O  OG  A SER B 2 300 ? 86.047  20.253  13.762  0.60 11.84 ? 301  SER B OG  1 
ATOM   4336 O  OG  B SER B 2 300 ? 85.551  20.474  15.763  0.40 17.24 ? 301  SER B OG  1 
ATOM   4337 N  N   . ALA B 2 301 ? 84.369  23.133  13.075  1.00 17.09 ? 302  ALA B N   1 
ATOM   4338 C  CA  . ALA B 2 301 ? 83.006  23.378  12.699  1.00 18.19 ? 302  ALA B CA  1 
ATOM   4339 C  C   . ALA B 2 301 ? 82.173  22.104  12.647  1.00 16.78 ? 302  ALA B C   1 
ATOM   4340 O  O   . ALA B 2 301 ? 80.968  22.076  12.988  1.00 19.65 ? 302  ALA B O   1 
ATOM   4341 C  CB  . ALA B 2 301 ? 82.998  24.115  11.323  1.00 21.17 ? 302  ALA B CB  1 
ATOM   4342 N  N   . GLY B 2 302 ? 82.823  20.988  12.340  1.00 14.88 ? 303  GLY B N   1 
ATOM   4343 C  CA  . GLY B 2 302 ? 82.055  19.770  12.257  1.00 12.40 ? 303  GLY B CA  1 
ATOM   4344 C  C   . GLY B 2 302 ? 81.574  19.180  13.571  1.00 12.77 ? 303  GLY B C   1 
ATOM   4345 O  O   . GLY B 2 302 ? 80.747  18.257  13.579  1.00 13.07 ? 303  GLY B O   1 
ATOM   4346 N  N   A LEU B 2 303 ? 82.047  19.708  14.687  0.60 11.05 ? 304  LEU B N   1 
ATOM   4347 N  N   B LEU B 2 303 ? 82.114  19.668  14.673  0.40 12.03 ? 304  LEU B N   1 
ATOM   4348 C  CA  A LEU B 2 303 ? 81.544  19.215  15.987  0.60 11.15 ? 304  LEU B CA  1 
ATOM   4349 C  CA  B LEU B 2 303 ? 81.731  19.132  15.978  0.40 12.51 ? 304  LEU B CA  1 
ATOM   4350 C  C   A LEU B 2 303 ? 80.484  20.211  16.540  0.60 11.96 ? 304  LEU B C   1 
ATOM   4351 C  C   B LEU B 2 303 ? 80.823  20.040  16.779  0.40 13.80 ? 304  LEU B C   1 
ATOM   4352 O  O   A LEU B 2 303 ? 80.322  20.353  17.785  0.60 12.26 ? 304  LEU B O   1 
ATOM   4353 O  O   B LEU B 2 303 ? 80.320  19.652  17.852  0.40 13.08 ? 304  LEU B O   1 
ATOM   4354 C  CB  A LEU B 2 303 ? 82.687  19.033  17.001  0.60 10.96 ? 304  LEU B CB  1 
ATOM   4355 C  CB  B LEU B 2 303 ? 82.965  18.873  16.828  0.40 12.71 ? 304  LEU B CB  1 
ATOM   4356 C  CG  A LEU B 2 303 ? 83.781  18.016  16.587  0.60 9.47  ? 304  LEU B CG  1 
ATOM   4357 C  CG  B LEU B 2 303 ? 84.042  17.932  16.304  0.40 11.97 ? 304  LEU B CG  1 
ATOM   4358 C  CD1 A LEU B 2 303 ? 84.861  17.796  17.751  0.60 11.08 ? 304  LEU B CD1 1 
ATOM   4359 C  CD1 B LEU B 2 303 ? 85.199  17.973  17.330  0.40 12.50 ? 304  LEU B CD1 1 
ATOM   4360 C  CD2 A LEU B 2 303 ? 83.135  16.651  16.285  0.60 10.40 ? 304  LEU B CD2 1 
ATOM   4361 C  CD2 B LEU B 2 303 ? 83.511  16.481  16.135  0.40 10.45 ? 304  LEU B CD2 1 
ATOM   4362 N  N   A ASP B 2 304 ? 79.761  20.854  15.617  0.60 12.66 ? 305  ASP B N   1 
ATOM   4363 N  N   B ASP B 2 304 ? 80.592  21.254  16.315  0.40 14.51 ? 305  ASP B N   1 
ATOM   4364 C  CA  A ASP B 2 304 ? 78.717  21.859  15.898  0.60 15.13 ? 305  ASP B CA  1 
ATOM   4365 C  CA  B ASP B 2 304 ? 79.782  22.077  17.170  0.40 16.68 ? 305  ASP B CA  1 
ATOM   4366 C  C   A ASP B 2 304 ? 77.294  21.404  16.262  0.60 15.92 ? 305  ASP B C   1 
ATOM   4367 C  C   B ASP B 2 304 ? 78.298  21.980  16.856  0.40 16.26 ? 305  ASP B C   1 
ATOM   4368 O  O   A ASP B 2 304 ? 76.439  22.251  16.543  0.60 15.87 ? 305  ASP B O   1 
ATOM   4369 O  O   B ASP B 2 304 ? 77.740  22.698  16.019  0.40 19.03 ? 305  ASP B O   1 
ATOM   4370 C  CB  A ASP B 2 304 ? 78.661  22.863  14.702  0.60 16.96 ? 305  ASP B CB  1 
ATOM   4371 C  CB  B ASP B 2 304 ? 80.355  23.506  17.243  0.40 19.74 ? 305  ASP B CB  1 
ATOM   4372 C  CG  A ASP B 2 304 ? 78.303  22.197  13.347  0.60 19.10 ? 305  ASP B CG  1 
ATOM   4373 C  CG  B ASP B 2 304 ? 80.204  24.275  15.976  0.40 21.17 ? 305  ASP B CG  1 
ATOM   4374 O  OD1 A ASP B 2 304 ? 78.462  20.963  13.191  0.60 19.77 ? 305  ASP B OD1 1 
ATOM   4375 O  OD1 B ASP B 2 304 ? 80.283  23.666  14.895  0.40 24.95 ? 305  ASP B OD1 1 
ATOM   4376 O  OD2 A ASP B 2 304 ? 77.880  22.928  12.416  0.60 19.35 ? 305  ASP B OD2 1 
ATOM   4377 O  OD2 B ASP B 2 304 ? 80.027  25.509  16.063  0.40 22.37 ? 305  ASP B OD2 1 
ATOM   4378 N  N   A PHE B 2 305 ? 77.012  20.100  16.268  0.60 14.18 ? 306  PHE B N   1 
ATOM   4379 N  N   B PHE B 2 305 ? 77.674  21.011  17.533  0.40 14.18 ? 306  PHE B N   1 
ATOM   4380 C  CA  A PHE B 2 305 ? 75.678  19.627  16.656  0.60 14.29 ? 306  PHE B CA  1 
ATOM   4381 C  CA  B PHE B 2 305 ? 76.247  20.775  17.371  0.40 14.29 ? 306  PHE B CA  1 
ATOM   4382 C  C   A PHE B 2 305 ? 75.458  19.960  18.139  0.60 14.51 ? 306  PHE B C   1 
ATOM   4383 C  C   B PHE B 2 305 ? 75.693  20.713  18.789  0.40 14.51 ? 306  PHE B C   1 
ATOM   4384 O  O   A PHE B 2 305 ? 76.164  19.447  19.005  0.60 15.38 ? 306  PHE B O   1 
ATOM   4385 O  O   B PHE B 2 305 ? 76.263  20.055  19.661  0.40 15.38 ? 306  PHE B O   1 
ATOM   4386 C  CB  A PHE B 2 305 ? 75.567  18.116  16.420  0.60 14.75 ? 306  PHE B CB  1 
ATOM   4387 C  CB  B PHE B 2 305 ? 75.994  19.448  16.647  0.40 14.75 ? 306  PHE B CB  1 
ATOM   4388 C  CG  A PHE B 2 305 ? 74.155  17.601  16.433  0.60 14.10 ? 306  PHE B CG  1 
ATOM   4389 C  CG  B PHE B 2 305 ? 74.552  19.008  16.661  0.40 14.10 ? 306  PHE B CG  1 
ATOM   4390 C  CD1 A PHE B 2 305 ? 73.226  18.056  15.500  0.60 14.25 ? 306  PHE B CD1 1 
ATOM   4391 C  CD1 B PHE B 2 305 ? 73.564  19.770  16.044  0.40 14.25 ? 306  PHE B CD1 1 
ATOM   4392 C  CD2 A PHE B 2 305 ? 73.753  16.660  17.374  0.60 14.33 ? 306  PHE B CD2 1 
ATOM   4393 C  CD2 B PHE B 2 305 ? 74.185  17.822  17.293  0.40 14.33 ? 306  PHE B CD2 1 
ATOM   4394 C  CE1 A PHE B 2 305 ? 71.917  17.580  15.505  0.60 14.51 ? 306  PHE B CE1 1 
ATOM   4395 C  CE1 B PHE B 2 305 ? 72.229  19.358  16.058  0.40 14.51 ? 306  PHE B CE1 1 
ATOM   4396 C  CE2 A PHE B 2 305 ? 72.447  16.177  17.389  0.60 12.33 ? 306  PHE B CE2 1 
ATOM   4397 C  CE2 B PHE B 2 305 ? 72.855  17.403  17.311  0.40 12.33 ? 306  PHE B CE2 1 
ATOM   4398 C  CZ  A PHE B 2 305 ? 71.527  16.638  16.453  0.60 14.25 ? 306  PHE B CZ  1 
ATOM   4399 C  CZ  B PHE B 2 305 ? 71.877  18.171  16.694  0.40 14.25 ? 306  PHE B CZ  1 
ATOM   4400 N  N   A PRO B 2 306 ? 74.372  20.719  18.395  0.60 12.27 ? 307  PRO B N   1 
ATOM   4401 N  N   B PRO B 2 306 ? 74.679  21.509  19.166  0.40 12.70 ? 307  PRO B N   1 
ATOM   4402 C  CA  A PRO B 2 306 ? 74.080  21.151  19.769  0.60 12.67 ? 307  PRO B CA  1 
ATOM   4403 C  CA  B PRO B 2 306 ? 74.286  21.353  20.566  0.40 13.55 ? 307  PRO B CA  1 
ATOM   4404 C  C   A PRO B 2 306 ? 73.461  20.180  20.776  0.60 11.60 ? 307  PRO B C   1 
ATOM   4405 C  C   B PRO B 2 306 ? 73.688  20.060  21.133  0.40 11.94 ? 307  PRO B C   1 
ATOM   4406 O  O   A PRO B 2 306 ? 73.006  20.520  21.859  0.60 14.05 ? 307  PRO B O   1 
ATOM   4407 O  O   B PRO B 2 306 ? 73.333  20.110  22.321  0.40 14.20 ? 307  PRO B O   1 
ATOM   4408 C  CB  A PRO B 2 306 ? 73.214  22.422  19.561  0.60 13.19 ? 307  PRO B CB  1 
ATOM   4409 C  CB  B PRO B 2 306 ? 73.357  22.549  20.835  0.40 12.63 ? 307  PRO B CB  1 
ATOM   4410 C  CG  A PRO B 2 306 ? 72.498  22.149  18.323  0.60 15.39 ? 307  PRO B CG  1 
ATOM   4411 C  CG  B PRO B 2 306 ? 73.239  23.276  19.610  0.40 14.72 ? 307  PRO B CG  1 
ATOM   4412 C  CD  A PRO B 2 306 ? 73.522  21.425  17.425  0.60 13.35 ? 307  PRO B CD  1 
ATOM   4413 C  CD  B PRO B 2 306 ? 73.880  22.534  18.483  0.40 12.18 ? 307  PRO B CD  1 
ATOM   4414 N  N   . SER B 2 307 ? 73.535  18.953  20.375  1.00 12.84 ? 308  SER B N   1 
ATOM   4415 C  CA  . SER B 2 307 ? 73.029  17.825  21.107  1.00 10.99 ? 308  SER B CA  1 
ATOM   4416 C  C   . SER B 2 307 ? 73.929  16.650  20.784  1.00 9.73  ? 308  SER B C   1 
ATOM   4417 O  O   . SER B 2 307 ? 75.086  16.824  20.385  1.00 10.48 ? 308  SER B O   1 
ATOM   4418 C  CB  . SER B 2 307 ? 71.535  17.585  20.787  1.00 11.45 ? 308  SER B CB  1 
ATOM   4419 O  OG  . SER B 2 307 ? 70.953  16.540  21.572  1.00 10.97 ? 308  SER B OG  1 
ATOM   4420 N  N   . VAL B 2 308 ? 73.397  15.453  20.973  1.00 9.16  ? 309  VAL B N   1 
ATOM   4421 C  CA  . VAL B 2 308 ? 74.196  14.223  20.765  1.00 9.02  ? 309  VAL B CA  1 
ATOM   4422 C  C   . VAL B 2 308 ? 73.242  13.046  20.567  1.00 9.45  ? 309  VAL B C   1 
ATOM   4423 O  O   . VAL B 2 308 ? 72.104  13.093  21.071  1.00 9.50  ? 309  VAL B O   1 
ATOM   4424 C  CB  . VAL B 2 308 ? 75.111  13.991  21.985  1.00 9.38  ? 309  VAL B CB  1 
ATOM   4425 C  CG1 . VAL B 2 308 ? 74.226  13.699  23.231  1.00 11.36 ? 309  VAL B CG1 1 
ATOM   4426 C  CG2 . VAL B 2 308 ? 76.129  12.872  21.704  1.00 9.89  ? 309  VAL B CG2 1 
ATOM   4427 N  N   . GLY B 2 309 ? 73.707  12.024  19.833  1.00 8.70  ? 310  GLY B N   1 
ATOM   4428 C  CA  . GLY B 2 309 ? 72.830  10.872  19.563  1.00 9.03  ? 310  GLY B CA  1 
ATOM   4429 C  C   . GLY B 2 309 ? 72.368  10.215  20.850  1.00 8.31  ? 310  GLY B C   1 
ATOM   4430 O  O   . GLY B 2 309 ? 73.145  10.035  21.815  1.00 7.76  ? 310  GLY B O   1 
ATOM   4431 N  N   . PRO B 2 310 ? 71.126  9.726   20.863  1.00 8.03  ? 311  PRO B N   1 
ATOM   4432 C  CA  . PRO B 2 310 ? 70.615  9.110   22.089  1.00 6.53  ? 311  PRO B CA  1 
ATOM   4433 C  C   . PRO B 2 310 ? 71.305  7.835   22.520  1.00 7.37  ? 311  PRO B C   1 
ATOM   4434 O  O   . PRO B 2 310 ? 71.306  7.535   23.713  1.00 7.49  ? 311  PRO B O   1 
ATOM   4435 C  CB  . PRO B 2 310 ? 69.112  8.883   21.786  1.00 7.10  ? 311  PRO B CB  1 
ATOM   4436 C  CG  . PRO B 2 310 ? 69.103  8.721   20.202  1.00 7.56  ? 311  PRO B CG  1 
ATOM   4437 C  CD  . PRO B 2 310 ? 70.118  9.749   19.763  1.00 8.64  ? 311  PRO B CD  1 
ATOM   4438 N  N   . GLN B 2 311 ? 71.848  7.086   21.574  1.00 6.52  ? 312  GLN B N   1 
ATOM   4439 C  CA  . GLN B 2 311 ? 72.541  5.846   21.989  1.00 6.86  ? 312  GLN B CA  1 
ATOM   4440 C  C   . GLN B 2 311 ? 73.803  6.157   22.788  1.00 7.30  ? 312  GLN B C   1 
ATOM   4441 O  O   . GLN B 2 311 ? 74.158  5.418   23.689  1.00 8.13  ? 312  GLN B O   1 
ATOM   4442 C  CB  . GLN B 2 311 ? 72.833  4.968   20.764  1.00 7.19  ? 312  GLN B CB  1 
ATOM   4443 C  CG  . GLN B 2 311 ? 73.354  3.577   21.246  1.00 8.39  ? 312  GLN B CG  1 
ATOM   4444 C  CD  . GLN B 2 311 ? 73.395  2.561   20.113  1.00 8.57  ? 312  GLN B CD  1 
ATOM   4445 O  OE1 . GLN B 2 311 ? 73.285  2.902   18.930  1.00 8.78  ? 312  GLN B OE1 1 
ATOM   4446 N  NE2 . GLN B 2 311 ? 73.649  1.287   20.475  1.00 10.11 ? 312  GLN B NE2 1 
ATOM   4447 N  N   . HIS B 2 312 ? 74.423  7.303   22.538  1.00 7.92  ? 313  HIS B N   1 
ATOM   4448 C  CA  . HIS B 2 312 ? 75.606  7.679   23.314  1.00 8.08  ? 313  HIS B CA  1 
ATOM   4449 C  C   . HIS B 2 312 ? 75.182  8.066   24.727  1.00 7.67  ? 313  HIS B C   1 
ATOM   4450 O  O   . HIS B 2 312 ? 75.843  7.710   25.703  1.00 7.99  ? 313  HIS B O   1 
ATOM   4451 C  CB  . HIS B 2 312 ? 76.344  8.840   22.647  1.00 7.34  ? 313  HIS B CB  1 
ATOM   4452 C  CG  . HIS B 2 312 ? 77.072  8.443   21.402  1.00 6.62  ? 313  HIS B CG  1 
ATOM   4453 N  ND1 . HIS B 2 312 ? 78.174  7.615   21.421  1.00 7.61  ? 313  HIS B ND1 1 
ATOM   4454 C  CD2 . HIS B 2 312 ? 76.829  8.720   20.099  1.00 8.14  ? 313  HIS B CD2 1 
ATOM   4455 C  CE1 . HIS B 2 312 ? 78.576  7.397   20.181  1.00 8.29  ? 313  HIS B CE1 1 
ATOM   4456 N  NE2 . HIS B 2 312 ? 77.777  8.055   19.361  1.00 8.61  ? 313  HIS B NE2 1 
ATOM   4457 N  N   . ALA B 2 313 ? 74.068  8.826   24.824  1.00 6.14  ? 314  ALA B N   1 
ATOM   4458 C  CA  . ALA B 2 313 ? 73.590  9.195   26.158  1.00 5.99  ? 314  ALA B CA  1 
ATOM   4459 C  C   . ALA B 2 313 ? 73.261  7.937   26.960  1.00 8.08  ? 314  ALA B C   1 
ATOM   4460 O  O   . ALA B 2 313 ? 73.524  7.866   28.164  1.00 8.68  ? 314  ALA B O   1 
ATOM   4461 C  CB  . ALA B 2 313 ? 72.387  10.121  26.016  1.00 7.47  ? 314  ALA B CB  1 
ATOM   4462 N  N   . TYR B 2 314 ? 72.732  6.919   26.285  1.00 7.45  ? 315  TYR B N   1 
ATOM   4463 C  CA  . TYR B 2 314 ? 72.397  5.661   26.942  1.00 7.93  ? 315  TYR B CA  1 
ATOM   4464 C  C   . TYR B 2 314 ? 73.643  4.877   27.367  1.00 7.80  ? 315  TYR B C   1 
ATOM   4465 O  O   . TYR B 2 314 ? 73.741  4.436   28.512  1.00 8.46  ? 315  TYR B O   1 
ATOM   4466 C  CB  . TYR B 2 314 ? 71.538  4.795   26.014  1.00 8.58  ? 315  TYR B CB  1 
ATOM   4467 C  CG  . TYR B 2 314 ? 71.251  3.423   26.569  1.00 9.89  ? 315  TYR B CG  1 
ATOM   4468 C  CD1 . TYR B 2 314 ? 70.471  3.260   27.715  1.00 9.81  ? 315  TYR B CD1 1 
ATOM   4469 C  CD2 . TYR B 2 314 ? 71.782  2.287   25.965  1.00 10.97 ? 315  TYR B CD2 1 
ATOM   4470 C  CE1 . TYR B 2 314 ? 70.229  1.990   28.244  1.00 11.76 ? 315  TYR B CE1 1 
ATOM   4471 C  CE2 . TYR B 2 314 ? 71.549  1.014   26.486  1.00 12.77 ? 315  TYR B CE2 1 
ATOM   4472 C  CZ  . TYR B 2 314 ? 70.773  0.877   27.623  1.00 12.14 ? 315  TYR B CZ  1 
ATOM   4473 O  OH  . TYR B 2 314 ? 70.546  -0.384  28.141  1.00 15.75 ? 315  TYR B OH  1 
ATOM   4474 N  N   . LEU B 2 315 ? 74.597  4.696   26.443  1.00 7.61  ? 316  LEU B N   1 
ATOM   4475 C  CA  . LEU B 2 315 ? 75.831  3.977   26.748  1.00 8.09  ? 316  LEU B CA  1 
ATOM   4476 C  C   . LEU B 2 315 ? 76.572  4.662   27.912  1.00 8.71  ? 316  LEU B C   1 
ATOM   4477 O  O   . LEU B 2 315 ? 77.158  3.947   28.765  1.00 8.53  ? 316  LEU B O   1 
ATOM   4478 C  CB  . LEU B 2 315 ? 76.732  3.920   25.472  1.00 8.08  ? 316  LEU B CB  1 
ATOM   4479 C  CG  . LEU B 2 315 ? 76.207  2.951   24.430  1.00 8.32  ? 316  LEU B CG  1 
ATOM   4480 C  CD1 . LEU B 2 315 ? 77.106  3.203   23.182  1.00 11.94 ? 316  LEU B CD1 1 
ATOM   4481 C  CD2 . LEU B 2 315 ? 76.215  1.464   24.804  1.00 10.29 ? 316  LEU B CD2 1 
ATOM   4482 N  N   . ASN B 2 316 ? 76.527  5.991   27.970  1.00 6.75  ? 317  ASN B N   1 
ATOM   4483 C  CA  . ASN B 2 316 ? 77.104  6.705   29.118  1.00 7.99  ? 317  ASN B CA  1 
ATOM   4484 C  C   . ASN B 2 316 ? 76.352  6.342   30.404  1.00 8.90  ? 317  ASN B C   1 
ATOM   4485 O  O   . ASN B 2 316 ? 76.986  6.009   31.422  1.00 10.03 ? 317  ASN B O   1 
ATOM   4486 C  CB  . ASN B 2 316 ? 76.967  8.212   28.901  1.00 7.86  ? 317  ASN B CB  1 
ATOM   4487 C  CG  . ASN B 2 316 ? 77.573  9.011   30.024  1.00 10.34 ? 317  ASN B CG  1 
ATOM   4488 O  OD1 . ASN B 2 316 ? 76.923  9.909   30.566  1.00 16.38 ? 317  ASN B OD1 1 
ATOM   4489 N  ND2 . ASN B 2 316 ? 78.774  8.712   30.348  1.00 6.86  ? 317  ASN B ND2 1 
ATOM   4490 N  N   . SER B 2 317 ? 75.022  6.418   30.351  1.00 8.55  ? 318  SER B N   1 
ATOM   4491 C  CA  . SER B 2 317 ? 74.255  6.214   31.538  1.00 7.65  ? 318  SER B CA  1 
ATOM   4492 C  C   . SER B 2 317 ? 74.479  4.860   32.195  1.00 8.72  ? 318  SER B C   1 
ATOM   4493 O  O   . SER B 2 317 ? 74.506  4.808   33.444  1.00 8.43  ? 318  SER B O   1 
ATOM   4494 C  CB  . SER B 2 317 ? 72.770  6.456   31.217  1.00 7.92  ? 318  SER B CB  1 
ATOM   4495 O  OG  A SER B 2 317 ? 72.180  5.351   30.561  0.60 9.61  ? 318  SER B OG  1 
ATOM   4496 O  OG  B SER B 2 317 ? 71.963  5.973   32.267  0.40 10.03 ? 318  SER B OG  1 
ATOM   4497 N  N   . ILE B 2 318 ? 74.658  3.824   31.390  1.00 8.30  ? 319  ILE B N   1 
ATOM   4498 C  CA  . ILE B 2 318 ? 74.884  2.483   31.978  1.00 8.23  ? 319  ILE B CA  1 
ATOM   4499 C  C   . ILE B 2 318 ? 76.375  2.188   32.225  1.00 8.01  ? 319  ILE B C   1 
ATOM   4500 O  O   . ILE B 2 318 ? 76.745  1.083   32.684  1.00 9.93  ? 319  ILE B O   1 
ATOM   4501 C  CB  . ILE B 2 318 ? 74.267  1.361   31.099  1.00 8.44  ? 319  ILE B CB  1 
ATOM   4502 C  CG1 . ILE B 2 318 ? 74.976  1.271   29.748  1.00 9.39  ? 319  ILE B CG1 1 
ATOM   4503 C  CG2 . ILE B 2 318 ? 72.736  1.630   30.925  1.00 9.68  ? 319  ILE B CG2 1 
ATOM   4504 C  CD1 . ILE B 2 318 ? 74.395  0.140   28.847  1.00 10.70 ? 319  ILE B CD1 1 
ATOM   4505 N  N   . GLY B 2 319 ? 77.221  3.156   31.904  1.00 7.89  ? 320  GLY B N   1 
ATOM   4506 C  CA  . GLY B 2 319 ? 78.646  2.965   32.112  1.00 9.08  ? 320  GLY B CA  1 
ATOM   4507 C  C   . GLY B 2 319 ? 79.380  2.127   31.095  1.00 9.43  ? 320  GLY B C   1 
ATOM   4508 O  O   . GLY B 2 319 ? 80.548  1.786   31.324  1.00 11.23 ? 320  GLY B O   1 
ATOM   4509 N  N   . ARG B 2 320 ? 78.747  1.825   29.952  1.00 8.68  ? 321  ARG B N   1 
ATOM   4510 C  CA  . ARG B 2 320 ? 79.443  1.010   28.948  1.00 8.66  ? 321  ARG B CA  1 
ATOM   4511 C  C   . ARG B 2 320 ? 80.463  1.839   28.163  1.00 9.77  ? 321  ARG B C   1 
ATOM   4512 O  O   . ARG B 2 320 ? 81.498  1.343   27.795  1.00 9.86  ? 321  ARG B O   1 
ATOM   4513 C  CB  . ARG B 2 320 ? 78.423  0.340   27.991  1.00 8.83  ? 321  ARG B CB  1 
ATOM   4514 C  CG  . ARG B 2 320 ? 79.087  -0.320  26.771  1.00 9.59  ? 321  ARG B CG  1 
ATOM   4515 C  CD  . ARG B 2 320 ? 79.860  -1.573  27.253  1.00 9.83  ? 321  ARG B CD  1 
ATOM   4516 N  NE  . ARG B 2 320 ? 80.687  -2.212  26.226  1.00 9.99  ? 321  ARG B NE  1 
ATOM   4517 C  CZ  . ARG B 2 320 ? 81.991  -1.975  26.066  1.00 9.28  ? 321  ARG B CZ  1 
ATOM   4518 N  NH1 . ARG B 2 320 ? 82.654  -1.095  26.835  1.00 9.40  ? 321  ARG B NH1 1 
ATOM   4519 N  NH2 . ARG B 2 320 ? 82.638  -2.647  25.106  1.00 9.84  ? 321  ARG B NH2 1 
ATOM   4520 N  N   . ALA B 2 321 ? 80.152  3.102   27.933  1.00 8.28  ? 322  ALA B N   1 
ATOM   4521 C  CA  . ALA B 2 321 ? 81.092  4.029   27.255  1.00 8.27  ? 322  ALA B CA  1 
ATOM   4522 C  C   . ALA B 2 321 ? 81.367  5.208   28.186  1.00 8.47  ? 322  ALA B C   1 
ATOM   4523 O  O   . ALA B 2 321 ? 80.506  5.602   29.007  1.00 10.48 ? 322  ALA B O   1 
ATOM   4524 C  CB  . ALA B 2 321 ? 80.488  4.538   25.951  1.00 10.55 ? 322  ALA B CB  1 
ATOM   4525 N  N   . ASP B 2 322 ? 82.552  5.783   28.079  1.00 8.47  ? 323  ASP B N   1 
ATOM   4526 C  CA  . ASP B 2 322 ? 82.970  6.955   28.818  1.00 8.95  ? 323  ASP B CA  1 
ATOM   4527 C  C   . ASP B 2 322 ? 83.155  8.115   27.872  1.00 8.15  ? 323  ASP B C   1 
ATOM   4528 O  O   . ASP B 2 322 ? 83.677  7.928   26.741  1.00 8.75  ? 323  ASP B O   1 
ATOM   4529 C  CB  . ASP B 2 322 ? 84.309  6.666   29.528  1.00 9.82  ? 323  ASP B CB  1 
ATOM   4530 C  CG  . ASP B 2 322 ? 84.149  5.506   30.507  1.00 13.52 ? 323  ASP B CG  1 
ATOM   4531 O  OD1 . ASP B 2 322 ? 83.273  5.576   31.381  1.00 14.19 ? 323  ASP B OD1 1 
ATOM   4532 O  OD2 . ASP B 2 322 ? 84.860  4.492   30.316  1.00 18.17 ? 323  ASP B OD2 1 
ATOM   4533 N  N   . TYR B 2 323 ? 82.734  9.288   28.294  1.00 8.05  ? 324  TYR B N   1 
ATOM   4534 C  CA  . TYR B 2 323 ? 82.863  10.470  27.465  1.00 7.54  ? 324  TYR B CA  1 
ATOM   4535 C  C   . TYR B 2 323 ? 83.681  11.530  28.173  1.00 8.18  ? 324  TYR B C   1 
ATOM   4536 O  O   . TYR B 2 323 ? 83.545  11.743  29.384  1.00 9.46  ? 324  TYR B O   1 
ATOM   4537 C  CB  . TYR B 2 323 ? 81.475  10.987  27.065  1.00 8.44  ? 324  TYR B CB  1 
ATOM   4538 C  CG  . TYR B 2 323 ? 80.711  9.967   26.248  1.00 7.29  ? 324  TYR B CG  1 
ATOM   4539 C  CD1 . TYR B 2 323 ? 80.044  8.911   26.866  1.00 7.75  ? 324  TYR B CD1 1 
ATOM   4540 C  CD2 . TYR B 2 323 ? 80.727  10.009  24.850  1.00 8.25  ? 324  TYR B CD2 1 
ATOM   4541 C  CE1 . TYR B 2 323 ? 79.417  7.917   26.124  1.00 6.78  ? 324  TYR B CE1 1 
ATOM   4542 C  CE2 . TYR B 2 323 ? 80.102  9.012   24.092  1.00 7.70  ? 324  TYR B CE2 1 
ATOM   4543 C  CZ  . TYR B 2 323 ? 79.452  7.970   24.740  1.00 6.83  ? 324  TYR B CZ  1 
ATOM   4544 O  OH  . TYR B 2 323 ? 78.853  6.965   24.013  1.00 8.24  ? 324  TYR B OH  1 
ATOM   4545 N  N   . VAL B 2 324 ? 84.535  12.178  27.398  1.00 7.97  ? 325  VAL B N   1 
ATOM   4546 C  CA  . VAL B 2 324 ? 85.479  13.211  27.869  1.00 7.50  ? 325  VAL B CA  1 
ATOM   4547 C  C   . VAL B 2 324 ? 85.444  14.349  26.911  1.00 7.99  ? 325  VAL B C   1 
ATOM   4548 O  O   . VAL B 2 324 ? 84.737  14.320  25.904  1.00 8.42  ? 325  VAL B O   1 
ATOM   4549 C  CB  . VAL B 2 324 ? 86.924  12.625  27.936  1.00 8.02  ? 325  VAL B CB  1 
ATOM   4550 C  CG1 . VAL B 2 324 ? 86.974  11.430  28.906  1.00 10.66 ? 325  VAL B CG1 1 
ATOM   4551 C  CG2 . VAL B 2 324 ? 87.393  12.114  26.511  1.00 9.12  ? 325  VAL B CG2 1 
ATOM   4552 N  N   . SER B 2 325 ? 86.212  15.400  27.213  1.00 9.06  ? 326  SER B N   1 
ATOM   4553 C  CA  . SER B 2 325 ? 86.267  16.513  26.287  1.00 8.33  ? 326  SER B CA  1 
ATOM   4554 C  C   . SER B 2 325 ? 87.740  16.913  26.082  1.00 7.35  ? 326  SER B C   1 
ATOM   4555 O  O   . SER B 2 325 ? 88.649  16.584  26.885  1.00 9.10  ? 326  SER B O   1 
ATOM   4556 C  CB  . SER B 2 325 ? 85.416  17.710  26.765  1.00 10.48 ? 326  SER B CB  1 
ATOM   4557 O  OG  . SER B 2 325 ? 85.902  18.239  28.024  1.00 13.52 ? 326  SER B OG  1 
ATOM   4558 N  N   . ILE B 2 326 ? 87.960  17.600  24.955  1.00 7.46  ? 327  ILE B N   1 
ATOM   4559 C  CA  . ILE B 2 326 ? 89.317  18.066  24.572  1.00 7.90  ? 327  ILE B CA  1 
ATOM   4560 C  C   . ILE B 2 326 ? 89.117  19.493  24.064  1.00 7.77  ? 327  ILE B C   1 
ATOM   4561 O  O   . ILE B 2 326 ? 88.180  19.783  23.300  1.00 9.11  ? 327  ILE B O   1 
ATOM   4562 C  CB  . ILE B 2 326 ? 89.822  17.144  23.416  1.00 6.96  ? 327  ILE B CB  1 
ATOM   4563 C  CG1 . ILE B 2 326 ? 90.307  15.818  24.020  1.00 8.04  ? 327  ILE B CG1 1 
ATOM   4564 C  CG2 . ILE B 2 326 ? 90.922  17.871  22.520  1.00 7.79  ? 327  ILE B CG2 1 
ATOM   4565 C  CD1 . ILE B 2 326 ? 91.651  15.948  24.840  1.00 8.58  ? 327  ILE B CD1 1 
ATOM   4566 N  N   . THR B 2 327 ? 89.999  20.407  24.528  1.00 7.78  ? 328  THR B N   1 
ATOM   4567 C  CA  . THR B 2 327 ? 89.875  21.798  24.149  1.00 8.73  ? 328  THR B CA  1 
ATOM   4568 C  C   . THR B 2 327 ? 90.443  22.100  22.764  1.00 8.61  ? 328  THR B C   1 
ATOM   4569 O  O   . THR B 2 327 ? 91.134  21.295  22.152  1.00 9.54  ? 328  THR B O   1 
ATOM   4570 C  CB  . THR B 2 327 ? 90.642  22.690  25.100  1.00 9.52  ? 328  THR B CB  1 
ATOM   4571 O  OG1 . THR B 2 327 ? 92.038  22.392  25.020  1.00 10.26 ? 328  THR B OG1 1 
ATOM   4572 C  CG2 . THR B 2 327 ? 90.171  22.520  26.521  1.00 10.27 ? 328  THR B CG2 1 
ATOM   4573 N  N   . ASP B 2 328 ? 90.117  23.282  22.275  1.00 9.15  ? 329  ASP B N   1 
ATOM   4574 C  CA  . ASP B 2 328 ? 90.655  23.720  20.992  1.00 9.22  ? 329  ASP B CA  1 
ATOM   4575 C  C   . ASP B 2 328 ? 92.208  23.578  20.961  1.00 9.87  ? 329  ASP B C   1 
ATOM   4576 O  O   . ASP B 2 328 ? 92.753  23.101  19.976  1.00 10.37 ? 329  ASP B O   1 
ATOM   4577 C  CB  . ASP B 2 328 ? 90.372  25.229  20.772  1.00 10.38 ? 329  ASP B CB  1 
ATOM   4578 C  CG  . ASP B 2 328 ? 88.938  25.568  20.432  1.00 13.03 ? 329  ASP B CG  1 
ATOM   4579 O  OD1 . ASP B 2 328 ? 88.059  24.685  20.272  1.00 11.84 ? 329  ASP B OD1 1 
ATOM   4580 O  OD2 . ASP B 2 328 ? 88.668  26.789  20.242  1.00 13.68 ? 329  ASP B OD2 1 
ATOM   4581 N  N   . ASP B 2 329 ? 92.883  24.046  22.018  1.00 11.22 ? 330  ASP B N   1 
ATOM   4582 C  CA  . ASP B 2 329 ? 94.345  24.008  22.002  1.00 11.20 ? 330  ASP B CA  1 
ATOM   4583 C  C   . ASP B 2 329 ? 94.872  22.585  22.033  1.00 9.74  ? 330  ASP B C   1 
ATOM   4584 O  O   . ASP B 2 329 ? 95.884  22.299  21.390  1.00 10.12 ? 330  ASP B O   1 
ATOM   4585 C  CB  . ASP B 2 329 ? 94.903  24.846  23.150  1.00 12.98 ? 330  ASP B CB  1 
ATOM   4586 C  CG  . ASP B 2 329 ? 94.832  26.347  22.873  1.00 15.27 ? 330  ASP B CG  1 
ATOM   4587 O  OD1 . ASP B 2 329 ? 94.564  26.787  21.749  1.00 17.08 ? 330  ASP B OD1 1 
ATOM   4588 O  OD2 . ASP B 2 329 ? 95.037  27.079  23.854  1.00 19.40 ? 330  ASP B OD2 1 
ATOM   4589 N  N   . GLU B 2 330 ? 94.192  21.699  22.760  1.00 9.69  ? 331  GLU B N   1 
ATOM   4590 C  CA  . GLU B 2 330 ? 94.646  20.312  22.767  1.00 9.49  ? 331  GLU B CA  1 
ATOM   4591 C  C   . GLU B 2 330 ? 94.437  19.694  21.359  1.00 9.71  ? 331  GLU B C   1 
ATOM   4592 O  O   . GLU B 2 330 ? 95.290  18.905  20.910  1.00 9.06  ? 331  GLU B O   1 
ATOM   4593 C  CB  . GLU B 2 330 ? 93.867  19.500  23.792  1.00 9.36  ? 331  GLU B CB  1 
ATOM   4594 C  CG  . GLU B 2 330 ? 94.247  19.878  25.230  1.00 11.17 ? 331  GLU B CG  1 
ATOM   4595 C  CD  . GLU B 2 330 ? 93.317  19.234  26.256  1.00 13.02 ? 331  GLU B CD  1 
ATOM   4596 O  OE1 . GLU B 2 330 ? 92.084  19.209  26.081  1.00 11.99 ? 331  GLU B OE1 1 
ATOM   4597 O  OE2 . GLU B 2 330 ? 93.816  18.737  27.306  1.00 16.72 ? 331  GLU B OE2 1 
ATOM   4598 N  N   . ALA B 2 331 ? 93.304  19.993  20.709  1.00 8.78  ? 332  ALA B N   1 
ATOM   4599 C  CA  . ALA B 2 331 ? 93.072  19.447  19.367  1.00 8.74  ? 332  ALA B CA  1 
ATOM   4600 C  C   . ALA B 2 331 ? 94.112  19.989  18.381  1.00 9.21  ? 332  ALA B C   1 
ATOM   4601 O  O   . ALA B 2 331 ? 94.633  19.243  17.543  1.00 8.85  ? 332  ALA B O   1 
ATOM   4602 C  CB  . ALA B 2 331 ? 91.673  19.806  18.889  1.00 8.40  ? 332  ALA B CB  1 
ATOM   4603 N  N   . LEU B 2 332 ? 94.434  21.301  18.466  1.00 9.89  ? 333  LEU B N   1 
ATOM   4604 C  CA  . LEU B 2 332 ? 95.443  21.877  17.562  1.00 9.51  ? 333  LEU B CA  1 
ATOM   4605 C  C   . LEU B 2 332 ? 96.807  21.218  17.763  1.00 9.22  ? 333  LEU B C   1 
ATOM   4606 O  O   . LEU B 2 332 ? 97.519  20.963  16.786  1.00 9.34  ? 333  LEU B O   1 
ATOM   4607 C  CB  . LEU B 2 332 ? 95.571  23.394  17.814  1.00 12.69 ? 333  LEU B CB  1 
ATOM   4608 C  CG  . LEU B 2 332 ? 94.398  24.212  17.275  1.00 14.15 ? 333  LEU B CG  1 
ATOM   4609 C  CD1 . LEU B 2 332 ? 94.455  25.626  17.915  1.00 17.83 ? 333  LEU B CD1 1 
ATOM   4610 C  CD2 . LEU B 2 332 ? 94.498  24.315  15.728  1.00 16.33 ? 333  LEU B CD2 1 
ATOM   4611 N  N   . GLU B 2 333 ? 97.178  20.931  19.030  1.00 8.85  ? 334  GLU B N   1 
ATOM   4612 C  CA  . GLU B 2 333 ? 98.470  20.285  19.264  1.00 9.09  ? 334  GLU B CA  1 
ATOM   4613 C  C   . GLU B 2 333 ? 98.486  18.875  18.686  1.00 8.40  ? 334  GLU B C   1 
ATOM   4614 O  O   . GLU B 2 333 ? 99.492  18.478  18.134  1.00 10.68 ? 334  GLU B O   1 
ATOM   4615 C  CB  . GLU B 2 333 ? 98.798  20.271  20.755  1.00 11.36 ? 334  GLU B CB  1 
ATOM   4616 C  CG  . GLU B 2 333 ? 100.182 19.703  21.050  1.00 14.06 ? 334  GLU B CG  1 
ATOM   4617 C  CD  . GLU B 2 333 ? 100.255 18.187  21.246  1.00 18.50 ? 334  GLU B CD  1 
ATOM   4618 O  OE1 . GLU B 2 333 ? 99.353  17.608  21.879  1.00 21.73 ? 334  GLU B OE1 1 
ATOM   4619 O  OE2 . GLU B 2 333 ? 101.273 17.558  20.836  1.00 19.80 ? 334  GLU B OE2 1 
ATOM   4620 N  N   . ALA B 2 334 ? 97.366  18.170  18.769  1.00 8.30  ? 335  ALA B N   1 
ATOM   4621 C  CA  . ALA B 2 334 ? 97.322  16.802  18.206  1.00 8.81  ? 335  ALA B CA  1 
ATOM   4622 C  C   . ALA B 2 334 ? 97.434  16.872  16.664  1.00 8.65  ? 335  ALA B C   1 
ATOM   4623 O  O   . ALA B 2 334 ? 98.082  16.037  16.068  1.00 9.43  ? 335  ALA B O   1 
ATOM   4624 C  CB  . ALA B 2 334 ? 96.009  16.104  18.645  1.00 8.92  ? 335  ALA B CB  1 
ATOM   4625 N  N   . PHE B 2 335 ? 96.796  17.873  16.073  1.00 8.13  ? 336  PHE B N   1 
ATOM   4626 C  CA  . PHE B 2 335 ? 96.831  18.075  14.627  1.00 8.74  ? 336  PHE B CA  1 
ATOM   4627 C  C   . PHE B 2 335 ? 98.286  18.263  14.183  1.00 9.91  ? 336  PHE B C   1 
ATOM   4628 O  O   . PHE B 2 335 ? 98.760  17.588  13.264  1.00 9.44  ? 336  PHE B O   1 
ATOM   4629 C  CB  . PHE B 2 335 ? 95.978  19.309  14.272  1.00 9.01  ? 336  PHE B CB  1 
ATOM   4630 C  CG  . PHE B 2 335 ? 96.029  19.712  12.817  1.00 9.69  ? 336  PHE B CG  1 
ATOM   4631 C  CD1 . PHE B 2 335 ? 97.115  20.426  12.316  1.00 10.61 ? 336  PHE B CD1 1 
ATOM   4632 C  CD2 . PHE B 2 335 ? 94.982  19.396  11.956  1.00 11.70 ? 336  PHE B CD2 1 
ATOM   4633 C  CE1 . PHE B 2 335 ? 97.155  20.820  10.977  1.00 11.98 ? 336  PHE B CE1 1 
ATOM   4634 C  CE2 . PHE B 2 335 ? 95.015  19.787  10.614  1.00 11.96 ? 336  PHE B CE2 1 
ATOM   4635 C  CZ  . PHE B 2 335 ? 96.104  20.499  10.127  1.00 13.03 ? 336  PHE B CZ  1 
ATOM   4636 N  N   . LYS B 2 336 ? 98.985  19.167  14.882  1.00 9.60  ? 337  LYS B N   1 
ATOM   4637 C  CA  . LYS B 2 336 ? 100.402 19.433  14.552  1.00 10.57 ? 337  LYS B CA  1 
ATOM   4638 C  C   . LYS B 2 336 ? 101.263 18.184  14.748  1.00 9.50  ? 337  LYS B C   1 
ATOM   4639 O  O   . LYS B 2 336 ? 102.155 17.901  13.928  1.00 10.15 ? 337  LYS B O   1 
ATOM   4640 C  CB  . LYS B 2 336 ? 100.932 20.560  15.452  1.00 12.02 ? 337  LYS B CB  1 
ATOM   4641 C  CG  . LYS B 2 336 ? 100.326 21.865  15.062  1.00 19.20 ? 337  LYS B CG  1 
ATOM   4642 C  CD  . LYS B 2 336 ? 100.646 22.934  16.115  1.00 23.78 ? 337  LYS B CD  1 
ATOM   4643 C  CE  . LYS B 2 336 ? 102.087 23.362  16.063  1.00 29.46 ? 337  LYS B CE  1 
ATOM   4644 N  NZ  . LYS B 2 336 ? 102.388 24.088  14.776  1.00 32.98 ? 337  LYS B NZ  1 
ATOM   4645 N  N   . THR B 2 337 ? 101.031 17.442  15.824  1.00 9.89  ? 338  THR B N   1 
ATOM   4646 C  CA  . THR B 2 337 ? 101.815 16.243  16.128  1.00 10.04 ? 338  THR B CA  1 
ATOM   4647 C  C   . THR B 2 337 ? 101.653 15.165  15.074  1.00 10.15 ? 338  THR B C   1 
ATOM   4648 O  O   . THR B 2 337 ? 102.639 14.566  14.635  1.00 10.01 ? 338  THR B O   1 
ATOM   4649 C  CB  . THR B 2 337 ? 101.416 15.733  17.488  1.00 13.42 ? 338  THR B CB  1 
ATOM   4650 O  OG1 . THR B 2 337 ? 101.871 16.713  18.438  1.00 16.69 ? 338  THR B OG1 1 
ATOM   4651 C  CG2 . THR B 2 337 ? 102.017 14.353  17.821  1.00 14.46 ? 338  THR B CG2 1 
ATOM   4652 N  N   . LEU B 2 338 ? 100.435 14.945  14.599  1.00 9.61  ? 339  LEU B N   1 
ATOM   4653 C  CA  . LEU B 2 338 ? 100.269 13.896  13.583  1.00 8.42  ? 339  LEU B CA  1 
ATOM   4654 C  C   . LEU B 2 338 ? 100.902 14.332  12.246  1.00 8.79  ? 339  LEU B C   1 
ATOM   4655 O  O   . LEU B 2 338 ? 101.519 13.522  11.539  1.00 9.50  ? 339  LEU B O   1 
ATOM   4656 C  CB  . LEU B 2 338 ? 98.750  13.593  13.397  1.00 8.02  ? 339  LEU B CB  1 
ATOM   4657 C  CG  . LEU B 2 338 ? 98.529  12.258  12.626  1.00 8.67  ? 339  LEU B CG  1 
ATOM   4658 C  CD1 . LEU B 2 338 ? 98.939  11.055  13.439  1.00 10.20 ? 339  LEU B CD1 1 
ATOM   4659 C  CD2 . LEU B 2 338 ? 97.019  12.158  12.208  1.00 10.29 ? 339  LEU B CD2 1 
ATOM   4660 N  N   . CYS B 2 339 ? 100.764 15.604  11.905  1.00 9.28  ? 340  CYS B N   1 
ATOM   4661 C  CA  . CYS B 2 339 ? 101.361 16.010  10.628  1.00 9.47  ? 340  CYS B CA  1 
ATOM   4662 C  C   . CYS B 2 339 ? 102.888 15.776  10.642  1.00 10.57 ? 340  CYS B C   1 
ATOM   4663 O  O   . CYS B 2 339 ? 103.478 15.277  9.676   1.00 10.52 ? 340  CYS B O   1 
ATOM   4664 C  CB  . CYS B 2 339 ? 101.162 17.522  10.365  1.00 9.36  ? 340  CYS B CB  1 
ATOM   4665 S  SG  . CYS B 2 339 ? 99.466  18.063  10.037  1.00 11.29 ? 340  CYS B SG  1 
ATOM   4666 N  N   . ARG B 2 340 ? 103.501 16.211  11.752  1.00 10.07 ? 341  ARG B N   1 
ATOM   4667 C  CA  . ARG B 2 340 ? 104.957 16.176  11.838  1.00 10.77 ? 341  ARG B CA  1 
ATOM   4668 C  C   . ARG B 2 340 ? 105.540 14.809  12.021  1.00 11.02 ? 341  ARG B C   1 
ATOM   4669 O  O   . ARG B 2 340 ? 106.630 14.546  11.479  1.00 12.36 ? 341  ARG B O   1 
ATOM   4670 C  CB  . ARG B 2 340 ? 105.402 17.106  12.998  1.00 12.30 ? 341  ARG B CB  1 
ATOM   4671 C  CG  . ARG B 2 340 ? 106.894 17.114  13.223  1.00 13.56 ? 341  ARG B CG  1 
ATOM   4672 C  CD  . ARG B 2 340 ? 107.589 17.814  12.024  1.00 19.28 ? 341  ARG B CD  1 
ATOM   4673 N  NE  . ARG B 2 340 ? 109.071 17.684  12.123  1.00 23.02 ? 341  ARG B NE  1 
ATOM   4674 C  CZ  . ARG B 2 340 ? 109.772 16.715  11.513  1.00 25.60 ? 341  ARG B CZ  1 
ATOM   4675 N  NH1 . ARG B 2 340 ? 109.156 15.769  10.760  1.00 24.98 ? 341  ARG B NH1 1 
ATOM   4676 N  NH2 . ARG B 2 340 ? 111.114 16.706  11.588  1.00 28.10 ? 341  ARG B NH2 1 
ATOM   4677 N  N   . HIS B 2 341 ? 104.881 13.948  12.782  1.00 10.82 ? 342  HIS B N   1 
ATOM   4678 C  CA  . HIS B 2 341 ? 105.412 12.625  13.085  1.00 10.32 ? 342  HIS B CA  1 
ATOM   4679 C  C   . HIS B 2 341 ? 104.916 11.449  12.263  1.00 11.61 ? 342  HIS B C   1 
ATOM   4680 O  O   . HIS B 2 341 ? 105.559 10.404  12.247  1.00 12.25 ? 342  HIS B O   1 
ATOM   4681 C  CB  . HIS B 2 341 ? 105.217 12.337  14.573  1.00 12.49 ? 342  HIS B CB  1 
ATOM   4682 C  CG  . HIS B 2 341 ? 105.985 13.265  15.460  1.00 15.34 ? 342  HIS B CG  1 
ATOM   4683 N  ND1 . HIS B 2 341 ? 107.357 13.211  15.580  1.00 18.21 ? 342  HIS B ND1 1 
ATOM   4684 C  CD2 . HIS B 2 341 ? 105.581 14.307  16.226  1.00 17.08 ? 342  HIS B CD2 1 
ATOM   4685 C  CE1 . HIS B 2 341 ? 107.765 14.180  16.380  1.00 19.21 ? 342  HIS B CE1 1 
ATOM   4686 N  NE2 . HIS B 2 341 ? 106.707 14.860  16.785  1.00 19.74 ? 342  HIS B NE2 1 
ATOM   4687 N  N   . GLU B 2 342 ? 103.763 11.608  11.613  1.00 8.90  ? 343  GLU B N   1 
ATOM   4688 C  CA  . GLU B 2 342 ? 103.284 10.507  10.777  1.00 9.54  ? 343  GLU B CA  1 
ATOM   4689 C  C   . GLU B 2 342 ? 102.993 10.931  9.345   1.00 9.00  ? 343  GLU B C   1 
ATOM   4690 O  O   . GLU B 2 342 ? 102.687 10.073  8.536   1.00 11.16 ? 343  GLU B O   1 
ATOM   4691 C  CB  . GLU B 2 342 ? 102.034 9.860   11.317  1.00 9.99  ? 343  GLU B CB  1 
ATOM   4692 C  CG  . GLU B 2 342 ? 102.209 9.408   12.809  1.00 11.38 ? 343  GLU B CG  1 
ATOM   4693 C  CD  . GLU B 2 342 ? 103.186 8.211   13.010  1.00 12.80 ? 343  GLU B CD  1 
ATOM   4694 O  OE1 . GLU B 2 342 ? 103.550 7.485   12.042  1.00 15.41 ? 343  GLU B OE1 1 
ATOM   4695 O  OE2 . GLU B 2 342 ? 103.616 7.984   14.173  1.00 14.71 ? 343  GLU B OE2 1 
ATOM   4696 N  N   . GLY B 2 343 ? 103.100 12.210  9.016   1.00 8.71  ? 344  GLY B N   1 
ATOM   4697 C  CA  . GLY B 2 343 ? 102.817 12.636  7.632   1.00 8.91  ? 344  GLY B CA  1 
ATOM   4698 C  C   . GLY B 2 343 ? 101.347 12.489  7.256   1.00 8.88  ? 344  GLY B C   1 
ATOM   4699 O  O   . GLY B 2 343 ? 100.992 12.286  6.097   1.00 10.34 ? 344  GLY B O   1 
ATOM   4700 N  N   . ILE B 2 344 ? 100.476 12.577  8.254   1.00 7.72  ? 345  ILE B N   1 
ATOM   4701 C  CA  . ILE B 2 344 ? 99.029  12.513  8.022   1.00 8.97  ? 345  ILE B CA  1 
ATOM   4702 C  C   . ILE B 2 344 ? 98.387  13.808  8.541   1.00 8.78  ? 345  ILE B C   1 
ATOM   4703 O  O   . ILE B 2 344 ? 98.637  14.195  9.696   1.00 8.78  ? 345  ILE B O   1 
ATOM   4704 C  CB  . ILE B 2 344 ? 98.417  11.290  8.745   1.00 8.23  ? 345  ILE B CB  1 
ATOM   4705 C  CG1 . ILE B 2 344 ? 99.030  9.978   8.271   1.00 9.45  ? 345  ILE B CG1 1 
ATOM   4706 C  CG2 . ILE B 2 344 ? 96.886  11.314  8.513   1.00 10.05 ? 345  ILE B CG2 1 
ATOM   4707 C  CD1 . ILE B 2 344 ? 98.627  8.740   9.186   1.00 10.62 ? 345  ILE B CD1 1 
ATOM   4708 N  N   . ILE B 2 345 ? 97.592  14.478  7.698   1.00 9.45  ? 346  ILE B N   1 
ATOM   4709 C  CA  . ILE B 2 345 ? 96.916  15.733  8.121   1.00 9.08  ? 346  ILE B CA  1 
ATOM   4710 C  C   . ILE B 2 345 ? 95.504  15.334  8.541   1.00 9.03  ? 346  ILE B C   1 
ATOM   4711 O  O   . ILE B 2 345 ? 94.652  15.030  7.682   1.00 10.97 ? 346  ILE B O   1 
ATOM   4712 C  CB  . ILE B 2 345 ? 96.899  16.726  6.960   1.00 11.59 ? 346  ILE B CB  1 
ATOM   4713 C  CG1 . ILE B 2 345 ? 98.327  16.924  6.451   1.00 13.90 ? 346  ILE B CG1 1 
ATOM   4714 C  CG2 . ILE B 2 345 ? 96.289  18.083  7.441   1.00 13.35 ? 346  ILE B CG2 1 
ATOM   4715 C  CD1 . ILE B 2 345 ? 98.424  17.999  5.264   1.00 17.35 ? 346  ILE B CD1 1 
ATOM   4716 N  N   . PRO B 2 346 ? 95.210  15.311  9.830   1.00 7.97  ? 347  PRO B N   1 
ATOM   4717 C  CA  . PRO B 2 346 ? 93.864  14.899  10.293  1.00 8.34  ? 347  PRO B CA  1 
ATOM   4718 C  C   . PRO B 2 346 ? 92.859  16.013  10.323  1.00 8.75  ? 347  PRO B C   1 
ATOM   4719 O  O   . PRO B 2 346 ? 93.205  17.189  10.527  1.00 8.93  ? 347  PRO B O   1 
ATOM   4720 C  CB  . PRO B 2 346 ? 94.140  14.429  11.723  1.00 8.26  ? 347  PRO B CB  1 
ATOM   4721 C  CG  . PRO B 2 346 ? 95.226  15.469  12.211  1.00 9.00  ? 347  PRO B CG  1 
ATOM   4722 C  CD  . PRO B 2 346 ? 96.055  15.806  10.949  1.00 9.90  ? 347  PRO B CD  1 
ATOM   4723 N  N   . ALA B 2 347 ? 91.579  15.673  10.182  1.00 8.51  ? 348  ALA B N   1 
ATOM   4724 C  CA  . ALA B 2 347 ? 90.557  16.717  10.351  1.00 7.59  ? 348  ALA B CA  1 
ATOM   4725 C  C   . ALA B 2 347 ? 90.651  17.240  11.806  1.00 7.84  ? 348  ALA B C   1 
ATOM   4726 O  O   . ALA B 2 347 ? 91.014  16.492  12.721  1.00 8.07  ? 348  ALA B O   1 
ATOM   4727 C  CB  . ALA B 2 347 ? 89.161  16.090  10.158  1.00 8.30  ? 348  ALA B CB  1 
ATOM   4728 N  N   . LEU B 2 348 ? 90.311  18.507  12.000  1.00 8.20  ? 349  LEU B N   1 
ATOM   4729 C  CA  . LEU B 2 348 ? 90.308  19.023  13.367  1.00 9.60  ? 349  LEU B CA  1 
ATOM   4730 C  C   . LEU B 2 348 ? 89.272  18.275  14.213  1.00 8.91  ? 349  LEU B C   1 
ATOM   4731 O  O   . LEU B 2 348 ? 89.438  18.205  15.429  1.00 9.38  ? 349  LEU B O   1 
ATOM   4732 C  CB  . LEU B 2 348 ? 90.044  20.535  13.366  1.00 10.75 ? 349  LEU B CB  1 
ATOM   4733 C  CG  . LEU B 2 348 ? 91.289  21.375  13.052  1.00 12.52 ? 349  LEU B CG  1 
ATOM   4734 C  CD1 . LEU B 2 348 ? 90.835  22.838  12.938  1.00 13.96 ? 349  LEU B CD1 1 
ATOM   4735 C  CD2 . LEU B 2 348 ? 92.330  21.227  14.165  1.00 12.60 ? 349  LEU B CD2 1 
ATOM   4736 N  N   . GLU B 2 349 ? 88.190  17.754  13.617  1.00 8.68  ? 350  GLU B N   1 
ATOM   4737 C  CA  . GLU B 2 349 ? 87.228  16.971  14.407  1.00 8.21  ? 350  GLU B CA  1 
ATOM   4738 C  C   . GLU B 2 349 ? 87.985  15.774  14.969  1.00 7.95  ? 350  GLU B C   1 
ATOM   4739 O  O   . GLU B 2 349 ? 88.015  15.558  16.191  1.00 7.97  ? 350  GLU B O   1 
ATOM   4740 C  CB  . GLU B 2 349 ? 86.098  16.404  13.512  1.00 10.23 ? 350  GLU B CB  1 
ATOM   4741 C  CG  . GLU B 2 349 ? 85.123  17.448  12.938  1.00 11.36 ? 350  GLU B CG  1 
ATOM   4742 C  CD  . GLU B 2 349 ? 85.601  18.148  11.657  1.00 13.95 ? 350  GLU B CD  1 
ATOM   4743 O  OE1 . GLU B 2 349 ? 86.772  18.044  11.226  1.00 11.32 ? 350  GLU B OE1 1 
ATOM   4744 O  OE2 . GLU B 2 349 ? 84.742  18.862  11.072  1.00 17.98 ? 350  GLU B OE2 1 
ATOM   4745 N  N   . SER B 2 350 ? 88.614  14.989  14.080  1.00 7.84  ? 351  SER B N   1 
ATOM   4746 C  CA  . SER B 2 350 ? 89.346  13.780  14.470  1.00 7.62  ? 351  SER B CA  1 
ATOM   4747 C  C   . SER B 2 350 ? 90.513  14.041  15.436  1.00 7.58  ? 351  SER B C   1 
ATOM   4748 O  O   . SER B 2 350 ? 90.861  13.200  16.232  1.00 7.95  ? 351  SER B O   1 
ATOM   4749 C  CB  . SER B 2 350 ? 89.914  13.123  13.229  1.00 9.23  ? 351  SER B CB  1 
ATOM   4750 O  OG  . SER B 2 350 ? 88.965  13.166  12.148  1.00 10.20 ? 351  SER B OG  1 
ATOM   4751 N  N   . SER B 2 351 ? 91.088  15.228  15.310  1.00 7.34  ? 352  SER B N   1 
ATOM   4752 C  CA  . SER B 2 351 ? 92.188  15.652  16.161  1.00 7.38  ? 352  SER B CA  1 
ATOM   4753 C  C   . SER B 2 351 ? 91.773  15.675  17.635  1.00 7.50  ? 352  SER B C   1 
ATOM   4754 O  O   . SER B 2 351 ? 92.609  15.536  18.499  1.00 8.03  ? 352  SER B O   1 
ATOM   4755 C  CB  . SER B 2 351 ? 92.678  17.058  15.761  1.00 8.76  ? 352  SER B CB  1 
ATOM   4756 O  OG  . SER B 2 351 ? 93.238  16.983  14.445  1.00 9.54  ? 352  SER B OG  1 
ATOM   4757 N  N   . HIS B 2 352 ? 90.466  15.795  17.897  1.00 6.56  ? 353  HIS B N   1 
ATOM   4758 C  CA  . HIS B 2 352 ? 90.004  15.759  19.277  1.00 6.89  ? 353  HIS B CA  1 
ATOM   4759 C  C   . HIS B 2 352 ? 90.175  14.338  19.826  1.00 7.40  ? 353  HIS B C   1 
ATOM   4760 O  O   . HIS B 2 352 ? 90.571  14.157  20.974  1.00 8.37  ? 353  HIS B O   1 
ATOM   4761 C  CB  . HIS B 2 352 ? 88.536  16.196  19.376  1.00 7.21  ? 353  HIS B CB  1 
ATOM   4762 C  CG  . HIS B 2 352 ? 88.335  17.679  19.278  1.00 8.38  ? 353  HIS B CG  1 
ATOM   4763 N  ND1 . HIS B 2 352 ? 88.443  18.372  18.092  1.00 9.03  ? 353  HIS B ND1 1 
ATOM   4764 C  CD2 . HIS B 2 352 ? 88.035  18.601  20.225  1.00 8.91  ? 353  HIS B CD2 1 
ATOM   4765 C  CE1 . HIS B 2 352 ? 88.217  19.656  18.311  1.00 8.07  ? 353  HIS B CE1 1 
ATOM   4766 N  NE2 . HIS B 2 352 ? 87.967  19.822  19.598  1.00 8.88  ? 353  HIS B NE2 1 
ATOM   4767 N  N   . ALA B 2 353 ? 89.825  13.310  19.026  1.00 7.84  ? 354  ALA B N   1 
ATOM   4768 C  CA  . ALA B 2 353 ? 90.034  11.950  19.474  1.00 7.62  ? 354  ALA B CA  1 
ATOM   4769 C  C   . ALA B 2 353 ? 91.534  11.639  19.641  1.00 7.30  ? 354  ALA B C   1 
ATOM   4770 O  O   . ALA B 2 353 ? 91.943  11.031  20.638  1.00 8.01  ? 354  ALA B O   1 
ATOM   4771 C  CB  . ALA B 2 353 ? 89.417  10.937  18.433  1.00 8.92  ? 354  ALA B CB  1 
ATOM   4772 N  N   . LEU B 2 354 ? 92.341  12.022  18.669  1.00 7.43  ? 355  LEU B N   1 
ATOM   4773 C  CA  . LEU B 2 354 ? 93.778  11.823  18.758  1.00 6.62  ? 355  LEU B CA  1 
ATOM   4774 C  C   . LEU B 2 354 ? 94.350  12.513  20.031  1.00 8.20  ? 355  LEU B C   1 
ATOM   4775 O  O   . LEU B 2 354 ? 95.164  11.910  20.754  1.00 8.31  ? 355  LEU B O   1 
ATOM   4776 C  CB  . LEU B 2 354 ? 94.475  12.376  17.490  1.00 8.20  ? 355  LEU B CB  1 
ATOM   4777 C  CG  . LEU B 2 354 ? 95.995  12.141  17.576  1.00 8.05  ? 355  LEU B CG  1 
ATOM   4778 C  CD1 . LEU B 2 354 ? 96.347  10.637  17.683  1.00 10.69 ? 355  LEU B CD1 1 
ATOM   4779 C  CD2 . LEU B 2 354 ? 96.611  12.721  16.283  1.00 10.93 ? 355  LEU B CD2 1 
ATOM   4780 N  N   . ALA B 2 355 ? 93.933  13.750  20.272  1.00 8.02  ? 356  ALA B N   1 
ATOM   4781 C  CA  . ALA B 2 355 ? 94.419  14.465  21.453  1.00 8.38  ? 356  ALA B CA  1 
ATOM   4782 C  C   . ALA B 2 355 ? 94.126  13.675  22.736  1.00 7.88  ? 356  ALA B C   1 
ATOM   4783 O  O   . ALA B 2 355 ? 94.972  13.609  23.653  1.00 8.30  ? 356  ALA B O   1 
ATOM   4784 C  CB  . ALA B 2 355 ? 93.750  15.841  21.514  1.00 8.23  ? 356  ALA B CB  1 
ATOM   4785 N  N   . HIS B 2 356 ? 92.957  13.067  22.856  1.00 7.51  ? 357  HIS B N   1 
ATOM   4786 C  CA  . HIS B 2 356 ? 92.702  12.314  24.072  1.00 7.27  ? 357  HIS B CA  1 
ATOM   4787 C  C   . HIS B 2 356 ? 93.599  11.070  24.151  1.00 8.99  ? 357  HIS B C   1 
ATOM   4788 O  O   . HIS B 2 356 ? 94.066  10.699  25.230  1.00 9.23  ? 357  HIS B O   1 
ATOM   4789 C  CB  . HIS B 2 356 ? 91.234  11.907  24.184  1.00 8.04  ? 357  HIS B CB  1 
ATOM   4790 C  CG  . HIS B 2 356 ? 90.920  11.255  25.490  1.00 8.45  ? 357  HIS B CG  1 
ATOM   4791 N  ND1 . HIS B 2 356 ? 90.925  11.948  26.681  1.00 9.77  ? 357  HIS B ND1 1 
ATOM   4792 C  CD2 . HIS B 2 356 ? 90.729  9.954   25.811  1.00 8.95  ? 357  HIS B CD2 1 
ATOM   4793 C  CE1 . HIS B 2 356 ? 90.756  11.102  27.680  1.00 9.60  ? 357  HIS B CE1 1 
ATOM   4794 N  NE2 . HIS B 2 356 ? 90.636  9.885   27.180  1.00 9.69  ? 357  HIS B NE2 1 
ATOM   4795 N  N   . ALA B 2 357 ? 93.793  10.372  23.029  1.00 7.03  ? 358  ALA B N   1 
ATOM   4796 C  CA  . ALA B 2 357 ? 94.722  9.244   23.051  1.00 7.71  ? 358  ALA B CA  1 
ATOM   4797 C  C   . ALA B 2 357 ? 96.134  9.695   23.451  1.00 8.36  ? 358  ALA B C   1 
ATOM   4798 O  O   . ALA B 2 357 ? 96.835  8.970   24.160  1.00 8.36  ? 358  ALA B O   1 
ATOM   4799 C  CB  . ALA B 2 357 ? 94.767  8.588   21.600  1.00 8.84  ? 358  ALA B CB  1 
ATOM   4800 N  N   . LEU B 2 358 ? 96.579  10.832  22.954  1.00 8.84  ? 359  LEU B N   1 
ATOM   4801 C  CA  . LEU B 2 358 ? 97.923  11.328  23.302  1.00 8.59  ? 359  LEU B CA  1 
ATOM   4802 C  C   . LEU B 2 358 ? 97.964  11.586  24.825  1.00 9.55  ? 359  LEU B C   1 
ATOM   4803 O  O   . LEU B 2 358 ? 99.015  11.350  25.429  1.00 10.27 ? 359  LEU B O   1 
ATOM   4804 C  CB  . LEU B 2 358 ? 98.201  12.615  22.523  1.00 10.82 ? 359  LEU B CB  1 
ATOM   4805 C  CG  . LEU B 2 358 ? 98.364  12.410  21.005  1.00 10.66 ? 359  LEU B CG  1 
ATOM   4806 C  CD1 . LEU B 2 358 ? 98.610  13.807  20.365  1.00 11.30 ? 359  LEU B CD1 1 
ATOM   4807 C  CD2 . LEU B 2 358 ? 99.599  11.550  20.712  1.00 11.99 ? 359  LEU B CD2 1 
ATOM   4808 N  N   . LYS B 2 359 ? 96.887  12.116  25.397  1.00 8.06  ? 360  LYS B N   1 
ATOM   4809 C  CA  . LYS B 2 359 ? 96.846  12.311  26.856  1.00 9.00  ? 360  LYS B CA  1 
ATOM   4810 C  C   . LYS B 2 359 ? 96.909  10.965  27.575  1.00 9.92  ? 360  LYS B C   1 
ATOM   4811 O  O   . LYS B 2 359 ? 97.607  10.820  28.576  1.00 9.53  ? 360  LYS B O   1 
ATOM   4812 C  CB  . LYS B 2 359 ? 95.535  13.022  27.219  1.00 10.61 ? 360  LYS B CB  1 
ATOM   4813 C  CG  . LYS B 2 359 ? 95.379  13.377  28.630  1.00 15.15 ? 360  LYS B CG  1 
ATOM   4814 C  CD  . LYS B 2 359 ? 94.021  14.171  28.792  1.00 15.97 ? 360  LYS B CD  1 
ATOM   4815 C  CE  . LYS B 2 359 ? 94.035  15.485  28.070  1.00 16.26 ? 360  LYS B CE  1 
ATOM   4816 N  NZ  . LYS B 2 359 ? 92.824  16.349  28.514  1.00 15.87 ? 360  LYS B NZ  1 
ATOM   4817 N  N   . MET B 2 360 ? 96.176  9.947   27.099  1.00 8.38  ? 361  MET B N   1 
ATOM   4818 C  CA  . MET B 2 360 ? 96.219  8.649   27.742  1.00 8.75  ? 361  MET B CA  1 
ATOM   4819 C  C   . MET B 2 360 ? 97.641  8.127   27.784  1.00 8.64  ? 361  MET B C   1 
ATOM   4820 O  O   . MET B 2 360 ? 98.093  7.527   28.765  1.00 9.66  ? 361  MET B O   1 
ATOM   4821 C  CB  . MET B 2 360 ? 95.297  7.676   27.002  1.00 8.79  ? 361  MET B CB  1 
ATOM   4822 C  CG  . MET B 2 360 ? 93.823  8.036   27.144  1.00 8.43  ? 361  MET B CG  1 
ATOM   4823 S  SD  . MET B 2 360 ? 92.770  7.079   26.013  1.00 10.89 ? 361  MET B SD  1 
ATOM   4824 C  CE  . MET B 2 360 ? 92.882  5.389   26.688  1.00 10.08 ? 361  MET B CE  1 
ATOM   4825 N  N   . MET B 2 361 ? 98.352  8.271   26.657  1.00 7.60  ? 362  MET B N   1 
ATOM   4826 C  CA  . MET B 2 361 ? 99.734  7.863   26.575  1.00 8.00  ? 362  MET B CA  1 
ATOM   4827 C  C   . MET B 2 361 ? 100.655 8.716   27.463  1.00 8.30  ? 362  MET B C   1 
ATOM   4828 O  O   . MET B 2 361 ? 101.451 8.175   28.262  1.00 10.89 ? 362  MET B O   1 
ATOM   4829 C  CB  . MET B 2 361 ? 100.174 7.946   25.096  1.00 10.58 ? 362  MET B CB  1 
ATOM   4830 C  CG  . MET B 2 361 ? 101.683 7.757   24.916  1.00 10.35 ? 362  MET B CG  1 
ATOM   4831 S  SD  . MET B 2 361 ? 102.121 7.984   23.153  1.00 12.69 ? 362  MET B SD  1 
ATOM   4832 C  CE  . MET B 2 361 ? 102.195 9.673   23.080  1.00 14.00 ? 362  MET B CE  1 
ATOM   4833 N  N   . ARG B 2 362 ? 100.573 10.014  27.314  1.00 8.97  ? 363  ARG B N   1 
ATOM   4834 C  CA  . ARG B 2 362 ? 101.539 10.878  27.986  1.00 9.05  ? 363  ARG B CA  1 
ATOM   4835 C  C   . ARG B 2 362 ? 101.363 10.901  29.518  1.00 9.79  ? 363  ARG B C   1 
ATOM   4836 O  O   . ARG B 2 362 ? 102.365 11.019  30.253  1.00 11.73 ? 363  ARG B O   1 
ATOM   4837 C  CB  . ARG B 2 362 ? 101.460 12.293  27.448  1.00 9.33  ? 363  ARG B CB  1 
ATOM   4838 C  CG  . ARG B 2 362 ? 101.963 12.441  25.991  1.00 10.31 ? 363  ARG B CG  1 
ATOM   4839 C  CD  . ARG B 2 362 ? 101.451 13.734  25.405  1.00 12.61 ? 363  ARG B CD  1 
ATOM   4840 N  NE  . ARG B 2 362 ? 101.917 13.941  24.017  1.00 12.95 ? 363  ARG B NE  1 
ATOM   4841 C  CZ  . ARG B 2 362 ? 101.408 14.872  23.211  1.00 14.40 ? 363  ARG B CZ  1 
ATOM   4842 N  NH1 . ARG B 2 362 ? 100.411 15.656  23.625  1.00 15.91 ? 363  ARG B NH1 1 
ATOM   4843 N  NH2 . ARG B 2 362 ? 101.920 15.025  21.994  1.00 15.57 ? 363  ARG B NH2 1 
ATOM   4844 N  N   . GLU B 2 363 ? 100.122 10.801  29.956  1.00 8.73  ? 364  GLU B N   1 
ATOM   4845 C  CA  . GLU B 2 363 ? 99.882  10.853  31.406  1.00 8.53  ? 364  GLU B CA  1 
ATOM   4846 C  C   . GLU B 2 363 ? 100.407 9.585   32.086  1.00 9.29  ? 364  GLU B C   1 
ATOM   4847 O  O   . GLU B 2 363 ? 100.764 9.652   33.281  1.00 11.61 ? 364  GLU B O   1 
ATOM   4848 C  CB  . GLU B 2 363 ? 98.397  11.000  31.702  1.00 11.02 ? 364  GLU B CB  1 
ATOM   4849 C  CG  . GLU B 2 363 ? 97.844  12.396  31.381  1.00 12.05 ? 364  GLU B CG  1 
ATOM   4850 C  CD  . GLU B 2 363 ? 96.398  12.589  31.854  1.00 12.85 ? 364  GLU B CD  1 
ATOM   4851 O  OE1 . GLU B 2 363 ? 95.770  11.660  32.369  1.00 15.88 ? 364  GLU B OE1 1 
ATOM   4852 O  OE2 . GLU B 2 363 ? 95.874  13.713  31.663  1.00 19.08 ? 364  GLU B OE2 1 
ATOM   4853 N  N   . GLN B 2 364 ? 100.429 8.427   31.429  1.00 9.44  ? 365  GLN B N   1 
ATOM   4854 C  CA  . GLN B 2 364 ? 100.847 7.138   32.013  1.00 8.47  ? 365  GLN B CA  1 
ATOM   4855 C  C   . GLN B 2 364 ? 101.655 6.453   30.941  1.00 8.61  ? 365  GLN B C   1 
ATOM   4856 O  O   . GLN B 2 364 ? 101.224 5.460   30.397  1.00 9.78  ? 365  GLN B O   1 
ATOM   4857 C  CB  . GLN B 2 364 ? 99.587  6.328   32.370  1.00 9.57  ? 365  GLN B CB  1 
ATOM   4858 C  CG  . GLN B 2 364 ? 98.651  7.167   33.316  1.00 8.63  ? 365  GLN B CG  1 
ATOM   4859 C  CD  . GLN B 2 364 ? 97.483  6.378   33.809  1.00 9.91  ? 365  GLN B CD  1 
ATOM   4860 O  OE1 . GLN B 2 364 ? 96.758  5.763   33.045  1.00 11.30 ? 365  GLN B OE1 1 
ATOM   4861 N  NE2 . GLN B 2 364 ? 97.300  6.352   35.154  1.00 10.11 ? 365  GLN B NE2 1 
ATOM   4862 N  N   . PRO B 2 365 ? 102.897 6.940   30.741  1.00 9.40  ? 366  PRO B N   1 
ATOM   4863 C  CA  . PRO B 2 365 ? 103.749 6.392   29.672  1.00 9.83  ? 366  PRO B CA  1 
ATOM   4864 C  C   . PRO B 2 365 ? 104.255 5.005   29.821  1.00 11.12 ? 366  PRO B C   1 
ATOM   4865 O  O   . PRO B 2 365 ? 104.687 4.429   28.856  1.00 12.47 ? 366  PRO B O   1 
ATOM   4866 C  CB  . PRO B 2 365 ? 104.842 7.414   29.524  1.00 11.43 ? 366  PRO B CB  1 
ATOM   4867 C  CG  . PRO B 2 365 ? 104.986 7.995   30.951  1.00 11.69 ? 366  PRO B CG  1 
ATOM   4868 C  CD  . PRO B 2 365 ? 103.520 8.087   31.403  1.00 8.62  ? 366  PRO B CD  1 
ATOM   4869 N  N   . GLU B 2 366 ? 104.200 4.470   31.025  1.00 8.86  ? 367  GLU B N   1 
ATOM   4870 C  CA  . GLU B 2 366 ? 104.579 3.092   31.251  1.00 10.44 ? 367  GLU B CA  1 
ATOM   4871 C  C   . GLU B 2 366 ? 103.399 2.126   31.348  1.00 9.48  ? 367  GLU B C   1 
ATOM   4872 O  O   . GLU B 2 366 ? 103.561 0.951   31.645  1.00 11.70 ? 367  GLU B O   1 
ATOM   4873 C  CB  . GLU B 2 366 ? 105.492 2.955   32.493  1.00 12.17 ? 367  GLU B CB  1 
ATOM   4874 C  CG  A GLU B 2 366 ? 106.836 3.631   32.283  0.50 16.14 ? 367  GLU B CG  1 
ATOM   4875 C  CG  B GLU B 2 366 ? 106.952 3.310   32.185  0.50 14.86 ? 367  GLU B CG  1 
ATOM   4876 C  CD  A GLU B 2 366 ? 107.600 2.939   31.198  0.50 18.20 ? 367  GLU B CD  1 
ATOM   4877 C  CD  B GLU B 2 366 ? 107.157 4.784   31.979  0.50 16.13 ? 367  GLU B CD  1 
ATOM   4878 O  OE1 A GLU B 2 366 ? 107.670 1.694   31.240  0.50 21.64 ? 367  GLU B OE1 1 
ATOM   4879 O  OE1 B GLU B 2 366 ? 106.861 5.567   32.911  0.50 17.58 ? 367  GLU B OE1 1 
ATOM   4880 O  OE2 A GLU B 2 366 ? 108.128 3.625   30.317  0.50 22.11 ? 367  GLU B OE2 1 
ATOM   4881 O  OE2 B GLU B 2 366 ? 107.644 5.175   30.885  0.50 19.49 ? 367  GLU B OE2 1 
ATOM   4882 N  N   . LYS B 2 367 ? 102.187 2.619   31.052  1.00 9.06  ? 368  LYS B N   1 
ATOM   4883 C  CA  . LYS B 2 367 ? 100.996 1.756   31.023  1.00 9.18  ? 368  LYS B CA  1 
ATOM   4884 C  C   . LYS B 2 367 ? 100.946 1.050   29.661  1.00 9.59  ? 368  LYS B C   1 
ATOM   4885 O  O   . LYS B 2 367 ? 100.926 1.714   28.619  1.00 11.42 ? 368  LYS B O   1 
ATOM   4886 C  CB  . LYS B 2 367 ? 99.719  2.619   31.179  1.00 9.75  ? 368  LYS B CB  1 
ATOM   4887 C  CG  . LYS B 2 367 ? 98.410  1.800   31.206  1.00 9.04  ? 368  LYS B CG  1 
ATOM   4888 C  CD  . LYS B 2 367 ? 97.168  2.690   31.325  1.00 10.18 ? 368  LYS B CD  1 
ATOM   4889 C  CE  . LYS B 2 367 ? 95.927  1.806   31.461  1.00 14.04 ? 368  LYS B CE  1 
ATOM   4890 N  NZ  . LYS B 2 367 ? 94.700  2.705   31.625  1.00 14.82 ? 368  LYS B NZ  1 
ATOM   4891 N  N   . GLU B 2 368 ? 100.877 -0.264  29.672  1.00 9.53  ? 369  GLU B N   1 
ATOM   4892 C  CA  . GLU B 2 368 ? 100.775 -1.022  28.434  1.00 10.13 ? 369  GLU B CA  1 
ATOM   4893 C  C   . GLU B 2 368 ? 99.327  -0.890  27.928  1.00 10.59 ? 369  GLU B C   1 
ATOM   4894 O  O   . GLU B 2 368 ? 98.380  -1.236  28.648  1.00 12.51 ? 369  GLU B O   1 
ATOM   4895 C  CB  . GLU B 2 368 ? 101.105 -2.504  28.679  1.00 14.15 ? 369  GLU B CB  1 
ATOM   4896 C  CG  . GLU B 2 368 ? 101.280 -3.178  27.293  1.00 21.45 ? 369  GLU B CG  1 
ATOM   4897 C  CD  . GLU B 2 368 ? 101.689 -4.633  27.380  1.00 26.32 ? 369  GLU B CD  1 
ATOM   4898 O  OE1 . GLU B 2 368 ? 101.983 -5.098  28.506  1.00 29.57 ? 369  GLU B OE1 1 
ATOM   4899 O  OE2 . GLU B 2 368 ? 101.693 -5.285  26.313  1.00 30.22 ? 369  GLU B OE2 1 
ATOM   4900 N  N   . GLN B 2 369 ? 99.133  -0.318  26.738  1.00 9.23  ? 370  GLN B N   1 
ATOM   4901 C  CA  . GLN B 2 369 ? 97.784  -0.167  26.242  1.00 9.09  ? 370  GLN B CA  1 
ATOM   4902 C  C   . GLN B 2 369 ? 97.779  -0.146  24.709  1.00 8.68  ? 370  GLN B C   1 
ATOM   4903 O  O   . GLN B 2 369 ? 98.668  0.433   24.110  1.00 10.10 ? 370  GLN B O   1 
ATOM   4904 C  CB  . GLN B 2 369 ? 97.091  1.052   26.809  1.00 10.94 ? 370  GLN B CB  1 
ATOM   4905 C  CG  . GLN B 2 369 ? 97.807  2.366   26.553  1.00 12.10 ? 370  GLN B CG  1 
ATOM   4906 C  CD  . GLN B 2 369 ? 97.272  3.537   27.407  1.00 10.91 ? 370  GLN B CD  1 
ATOM   4907 O  OE1 . GLN B 2 369 ? 96.106  3.566   27.755  1.00 12.21 ? 370  GLN B OE1 1 
ATOM   4908 N  NE2 . GLN B 2 369 ? 98.129  4.513   27.724  1.00 12.74 ? 370  GLN B NE2 1 
ATOM   4909 N  N   . LEU B 2 370 ? 96.787  -0.837  24.171  1.00 8.29  ? 371  LEU B N   1 
ATOM   4910 C  CA  . LEU B 2 370 ? 96.582  -0.942  22.705  1.00 7.77  ? 371  LEU B CA  1 
ATOM   4911 C  C   . LEU B 2 370 ? 95.353  -0.115  22.376  1.00 7.39  ? 371  LEU B C   1 
ATOM   4912 O  O   . LEU B 2 370 ? 94.232  -0.436  22.786  1.00 9.10  ? 371  LEU B O   1 
ATOM   4913 C  CB  . LEU B 2 370 ? 96.355  -2.414  22.369  1.00 8.03  ? 371  LEU B CB  1 
ATOM   4914 C  CG  . LEU B 2 370 ? 95.990  -2.665  20.887  1.00 8.85  ? 371  LEU B CG  1 
ATOM   4915 C  CD1 . LEU B 2 370 ? 97.080  -2.114  19.946  1.00 11.15 ? 371  LEU B CD1 1 
ATOM   4916 C  CD2 . LEU B 2 370 ? 95.801  -4.221  20.700  1.00 11.21 ? 371  LEU B CD2 1 
ATOM   4917 N  N   . LEU B 2 371 ? 95.575  0.990   21.677  1.00 7.83  ? 372  LEU B N   1 
ATOM   4918 C  CA  . LEU B 2 371 ? 94.520  1.953   21.412  1.00 7.79  ? 372  LEU B CA  1 
ATOM   4919 C  C   . LEU B 2 371 ? 94.250  2.097   19.926  1.00 7.34  ? 372  LEU B C   1 
ATOM   4920 O  O   . LEU B 2 371 ? 95.179  2.042   19.114  1.00 8.42  ? 372  LEU B O   1 
ATOM   4921 C  CB  . LEU B 2 371 ? 94.957  3.332   21.925  1.00 8.90  ? 372  LEU B CB  1 
ATOM   4922 C  CG  . LEU B 2 371 ? 95.408  3.420   23.395  1.00 9.58  ? 372  LEU B CG  1 
ATOM   4923 C  CD1 . LEU B 2 371 ? 95.716  4.885   23.716  1.00 10.27 ? 372  LEU B CD1 1 
ATOM   4924 C  CD2 . LEU B 2 371 ? 94.284  2.888   24.337  1.00 11.18 ? 372  LEU B CD2 1 
ATOM   4925 N  N   . VAL B 2 372 ? 92.969  2.315   19.598  1.00 6.98  ? 373  VAL B N   1 
ATOM   4926 C  CA  . VAL B 2 372 ? 92.626  2.658   18.173  1.00 7.31  ? 373  VAL B CA  1 
ATOM   4927 C  C   . VAL B 2 372 ? 91.870  3.988   18.244  1.00 8.03  ? 373  VAL B C   1 
ATOM   4928 O  O   . VAL B 2 372 ? 90.882  4.137   19.001  1.00 8.95  ? 373  VAL B O   1 
ATOM   4929 C  CB  . VAL B 2 372 ? 91.677  1.640   17.524  1.00 7.92  ? 373  VAL B CB  1 
ATOM   4930 C  CG1 . VAL B 2 372 ? 91.335  2.115   16.052  1.00 8.82  ? 373  VAL B CG1 1 
ATOM   4931 C  CG2 . VAL B 2 372 ? 92.380  0.309   17.477  1.00 9.48  ? 373  VAL B CG2 1 
ATOM   4932 N  N   . VAL B 2 373 ? 92.329  4.945   17.441  1.00 7.03  ? 374  VAL B N   1 
ATOM   4933 C  CA  . VAL B 2 373 ? 91.642  6.229   17.283  1.00 6.74  ? 374  VAL B CA  1 
ATOM   4934 C  C   . VAL B 2 373 ? 90.946  6.160   15.913  1.00 6.89  ? 374  VAL B C   1 
ATOM   4935 O  O   . VAL B 2 373 ? 91.552  5.746   14.913  1.00 7.94  ? 374  VAL B O   1 
ATOM   4936 C  CB  . VAL B 2 373 ? 92.658  7.381   17.247  1.00 7.15  ? 374  VAL B CB  1 
ATOM   4937 C  CG1 . VAL B 2 373 ? 92.003  8.643   16.681  1.00 9.48  ? 374  VAL B CG1 1 
ATOM   4938 C  CG2 . VAL B 2 373 ? 93.125  7.647   18.720  1.00 9.66  ? 374  VAL B CG2 1 
ATOM   4939 N  N   . ASN B 2 374 ? 89.663  6.527   15.892  1.00 7.00  ? 375  ASN B N   1 
ATOM   4940 C  CA  . ASN B 2 374 ? 88.975  6.610   14.600  1.00 7.08  ? 375  ASN B CA  1 
ATOM   4941 C  C   . ASN B 2 374 ? 89.392  7.928   13.925  1.00 8.60  ? 375  ASN B C   1 
ATOM   4942 O  O   . ASN B 2 374 ? 88.970  8.996   14.389  1.00 8.91  ? 375  ASN B O   1 
ATOM   4943 C  CB  . ASN B 2 374 ? 87.454  6.610   14.801  1.00 7.68  ? 375  ASN B CB  1 
ATOM   4944 C  CG  . ASN B 2 374 ? 86.694  6.240   13.519  1.00 8.79  ? 375  ASN B CG  1 
ATOM   4945 O  OD1 . ASN B 2 374 ? 85.476  6.621   13.418  1.00 12.53 ? 375  ASN B OD1 1 
ATOM   4946 N  ND2 . ASN B 2 374 ? 87.304  5.542   12.612  1.00 7.98  ? 375  ASN B ND2 1 
ATOM   4947 N  N   . LEU B 2 375 ? 90.153  7.884   12.838  1.00 7.01  ? 376  LEU B N   1 
ATOM   4948 C  CA  . LEU B 2 375 ? 90.537  9.156   12.191  1.00 7.88  ? 376  LEU B CA  1 
ATOM   4949 C  C   . LEU B 2 375 ? 89.409  9.396   11.193  1.00 8.53  ? 376  LEU B C   1 
ATOM   4950 O  O   . LEU B 2 375 ? 89.466  8.988   10.017  1.00 8.50  ? 376  LEU B O   1 
ATOM   4951 C  CB  . LEU B 2 375 ? 91.883  8.955   11.486  1.00 9.32  ? 376  LEU B CB  1 
ATOM   4952 C  CG  . LEU B 2 375 ? 92.529  10.303  11.268  1.00 13.34 ? 376  LEU B CG  1 
ATOM   4953 C  CD1 . LEU B 2 375 ? 93.043  10.727  12.615  1.00 14.83 ? 376  LEU B CD1 1 
ATOM   4954 C  CD2 . LEU B 2 375 ? 93.754  10.102  10.333  1.00 13.83 ? 376  LEU B CD2 1 
ATOM   4955 N  N   . SER B 2 376 ? 88.393  10.102  11.679  1.00 7.84  ? 377  SER B N   1 
ATOM   4956 C  CA  . SER B 2 376 ? 87.158  10.247  10.912  1.00 6.63  ? 377  SER B CA  1 
ATOM   4957 C  C   . SER B 2 376 ? 87.284  10.984  9.576   1.00 7.37  ? 377  SER B C   1 
ATOM   4958 O  O   . SER B 2 376 ? 86.444  10.796  8.718   1.00 8.63  ? 377  SER B O   1 
ATOM   4959 C  CB  . SER B 2 376 ? 86.091  10.876  11.817  1.00 8.17  ? 377  SER B CB  1 
ATOM   4960 O  OG  . SER B 2 376 ? 86.517  12.128  12.380  1.00 9.06  ? 377  SER B OG  1 
ATOM   4961 N  N   . GLY B 2 377 ? 88.290  11.862  9.466   1.00 7.35  ? 378  GLY B N   1 
ATOM   4962 C  CA  . GLY B 2 377 ? 88.427  12.559  8.191   1.00 7.90  ? 378  GLY B CA  1 
ATOM   4963 C  C   . GLY B 2 377 ? 89.810  13.170  8.050   1.00 8.36  ? 378  GLY B C   1 
ATOM   4964 O  O   . GLY B 2 377 ? 90.613  13.170  9.002   1.00 8.50  ? 378  GLY B O   1 
ATOM   4965 N  N   . ARG B 2 378 ? 90.067  13.679  6.819   1.00 8.46  ? 379  ARG B N   1 
ATOM   4966 C  CA  . ARG B 2 378 ? 91.334  14.334  6.527   1.00 8.43  ? 379  ARG B CA  1 
ATOM   4967 C  C   . ARG B 2 378 ? 91.209  15.860  6.793   1.00 8.44  ? 379  ARG B C   1 
ATOM   4968 O  O   . ARG B 2 378 ? 90.086  16.410  6.863   1.00 9.39  ? 379  ARG B O   1 
ATOM   4969 C  CB  . ARG B 2 378 ? 91.762  14.034  5.062   1.00 11.04 ? 379  ARG B CB  1 
ATOM   4970 C  CG  . ARG B 2 378 ? 90.793  14.454  4.034   1.00 12.75 ? 379  ARG B CG  1 
ATOM   4971 C  CD  . ARG B 2 378 ? 91.479  14.411  2.622   1.00 19.86 ? 379  ARG B CD  1 
ATOM   4972 N  NE  . ARG B 2 378 ? 90.524  14.891  1.622   1.00 22.30 ? 379  ARG B NE  1 
ATOM   4973 C  CZ  . ARG B 2 378 ? 89.940  14.076  0.787   1.00 21.18 ? 379  ARG B CZ  1 
ATOM   4974 N  NH1 . ARG B 2 378 ? 90.260  12.808  0.835   1.00 24.06 ? 379  ARG B NH1 1 
ATOM   4975 N  NH2 . ARG B 2 378 ? 88.968  14.491  0.009   1.00 22.32 ? 379  ARG B NH2 1 
ATOM   4976 N  N   . GLY B 2 379 ? 92.363  16.512  7.002   1.00 8.76  ? 380  GLY B N   1 
ATOM   4977 C  CA  . GLY B 2 379 ? 92.350  17.906  7.399   1.00 10.55 ? 380  GLY B CA  1 
ATOM   4978 C  C   . GLY B 2 379 ? 92.779  18.934  6.396   1.00 12.93 ? 380  GLY B C   1 
ATOM   4979 O  O   . GLY B 2 379 ? 93.115  20.037  6.800   1.00 11.85 ? 380  GLY B O   1 
ATOM   4980 N  N   . ASP B 2 380 ? 92.806  18.596  5.122   1.00 13.88 ? 381  ASP B N   1 
ATOM   4981 C  CA  . ASP B 2 380 ? 93.145  19.636  4.136   1.00 16.87 ? 381  ASP B CA  1 
ATOM   4982 C  C   . ASP B 2 380 ? 92.217  20.826  4.291   1.00 17.46 ? 381  ASP B C   1 
ATOM   4983 O  O   . ASP B 2 380 ? 92.681  21.993  4.152   1.00 19.46 ? 381  ASP B O   1 
ATOM   4984 C  CB  . ASP B 2 380 ? 93.012  19.030  2.766   1.00 20.32 ? 381  ASP B CB  1 
ATOM   4985 C  CG  . ASP B 2 380 ? 94.010  17.928  2.596   1.00 23.67 ? 381  ASP B CG  1 
ATOM   4986 O  OD1 . ASP B 2 380 ? 95.236  18.230  2.585   1.00 28.38 ? 381  ASP B OD1 1 
ATOM   4987 O  OD2 . ASP B 2 380 ? 93.572  16.758  2.585   1.00 27.14 ? 381  ASP B OD2 1 
ATOM   4988 N  N   . LYS B 2 381 ? 90.939  20.564  4.582   1.00 15.47 ? 382  LYS B N   1 
ATOM   4989 C  CA  . LYS B 2 381 ? 89.937  21.593  4.760   1.00 17.14 ? 382  LYS B CA  1 
ATOM   4990 C  C   . LYS B 2 381 ? 90.243  22.505  5.929   1.00 17.40 ? 382  LYS B C   1 
ATOM   4991 O  O   . LYS B 2 381 ? 89.660  23.623  6.022   1.00 20.04 ? 382  LYS B O   1 
ATOM   4992 C  CB  . LYS B 2 381 ? 88.553  20.965  4.989   1.00 17.27 ? 382  LYS B CB  1 
ATOM   4993 C  CG  . LYS B 2 381 ? 88.444  20.204  6.378   1.00 17.09 ? 382  LYS B CG  1 
ATOM   4994 C  CD  . LYS B 2 381 ? 87.155  19.448  6.540   1.00 17.25 ? 382  LYS B CD  1 
ATOM   4995 C  CE  . LYS B 2 381 ? 87.182  18.603  7.877   1.00 19.60 ? 382  LYS B CE  1 
ATOM   4996 N  NZ  . LYS B 2 381 ? 87.226  19.475  9.015   1.00 19.52 ? 382  LYS B NZ  1 
ATOM   4997 N  N   . ASP B 2 382 ? 91.130  22.088  6.834   1.00 15.53 ? 383  ASP B N   1 
ATOM   4998 C  CA  . ASP B 2 382 ? 91.414  22.896  8.027   1.00 14.63 ? 383  ASP B CA  1 
ATOM   4999 C  C   . ASP B 2 382 ? 92.718  23.641  7.989   1.00 16.79 ? 383  ASP B C   1 
ATOM   5000 O  O   . ASP B 2 382 ? 93.067  24.313  8.952   1.00 17.00 ? 383  ASP B O   1 
ATOM   5001 C  CB  . ASP B 2 382 ? 91.433  21.982  9.274   1.00 15.64 ? 383  ASP B CB  1 
ATOM   5002 C  CG  . ASP B 2 382 ? 90.103  21.337  9.522   1.00 15.41 ? 383  ASP B CG  1 
ATOM   5003 O  OD1 . ASP B 2 382 ? 89.078  22.097  9.551   1.00 16.33 ? 383  ASP B OD1 1 
ATOM   5004 O  OD2 . ASP B 2 382 ? 90.052  20.063  9.627   1.00 13.95 ? 383  ASP B OD2 1 
ATOM   5005 N  N   . ILE B 2 383 ? 93.437  23.516  6.871   1.00 17.31 ? 384  ILE B N   1 
ATOM   5006 C  CA  . ILE B 2 383 ? 94.741  24.153  6.725   1.00 21.43 ? 384  ILE B CA  1 
ATOM   5007 C  C   . ILE B 2 383 ? 94.667  25.671  6.878   1.00 18.93 ? 384  ILE B C   1 
ATOM   5008 O  O   . ILE B 2 383 ? 95.508  26.245  7.555   1.00 21.57 ? 384  ILE B O   1 
ATOM   5009 C  CB  . ILE B 2 383 ? 95.353  23.727  5.352   1.00 22.77 ? 384  ILE B CB  1 
ATOM   5010 C  CG1 . ILE B 2 383 ? 95.786  22.258  5.491   1.00 25.92 ? 384  ILE B CG1 1 
ATOM   5011 C  CG2 . ILE B 2 383 ? 96.516  24.657  4.937   1.00 27.06 ? 384  ILE B CG2 1 
ATOM   5012 C  CD1 . ILE B 2 383 ? 96.847  22.077  6.471   1.00 27.07 ? 384  ILE B CD1 1 
ATOM   5013 N  N   . PHE B 2 384 ? 93.666  26.309  6.287   1.00 23.61 ? 385  PHE B N   1 
ATOM   5014 C  CA  . PHE B 2 384 ? 93.528  27.753  6.446   1.00 25.40 ? 385  PHE B CA  1 
ATOM   5015 C  C   . PHE B 2 384 ? 93.259  28.137  7.897   1.00 24.96 ? 385  PHE B C   1 
ATOM   5016 O  O   . PHE B 2 384 ? 93.846  29.087  8.414   1.00 25.44 ? 385  PHE B O   1 
ATOM   5017 C  CB  . PHE B 2 384 ? 92.401  28.284  5.554   1.00 28.33 ? 385  PHE B CB  1 
ATOM   5018 C  CG  . PHE B 2 384 ? 92.707  28.219  4.086   1.00 32.38 ? 385  PHE B CG  1 
ATOM   5019 C  CD1 . PHE B 2 384 ? 93.855  28.819  3.574   1.00 34.66 ? 385  PHE B CD1 1 
ATOM   5020 C  CD2 . PHE B 2 384 ? 91.846  27.566  3.210   1.00 34.79 ? 385  PHE B CD2 1 
ATOM   5021 C  CE1 . PHE B 2 384 ? 94.142  28.769  2.210   1.00 35.38 ? 385  PHE B CE1 1 
ATOM   5022 C  CE2 . PHE B 2 384 ? 92.123  27.510  1.844   1.00 35.79 ? 385  PHE B CE2 1 
ATOM   5023 C  CZ  . PHE B 2 384 ? 93.274  28.113  1.343   1.00 35.74 ? 385  PHE B CZ  1 
ATOM   5024 N  N   . THR B 2 385 ? 92.346  27.416  8.546   1.00 20.83 ? 386  THR B N   1 
ATOM   5025 C  CA  . THR B 2 385 ? 92.031  27.671  9.951   1.00 21.28 ? 386  THR B CA  1 
ATOM   5026 C  C   . THR B 2 385 ? 93.257  27.573  10.834  1.00 20.54 ? 386  THR B C   1 
ATOM   5027 O  O   . THR B 2 385 ? 93.510  28.424  11.672  1.00 22.27 ? 386  THR B O   1 
ATOM   5028 C  CB  . THR B 2 385 ? 90.980  26.665  10.448  1.00 21.71 ? 386  THR B CB  1 
ATOM   5029 O  OG1 . THR B 2 385 ? 89.741  26.944  9.794   1.00 24.46 ? 386  THR B OG1 1 
ATOM   5030 C  CG2 . THR B 2 385 ? 90.794  26.744  11.977  1.00 23.18 ? 386  THR B CG2 1 
ATOM   5031 N  N   . VAL B 2 386 ? 94.028  26.497  10.685  1.00 19.17 ? 387  VAL B N   1 
ATOM   5032 C  CA  . VAL B 2 386 ? 95.196  26.302  11.491  1.00 18.65 ? 387  VAL B CA  1 
ATOM   5033 C  C   . VAL B 2 386 ? 96.229  27.398  11.204  1.00 19.25 ? 387  VAL B C   1 
ATOM   5034 O  O   . VAL B 2 386 ? 96.832  27.937  12.118  1.00 21.03 ? 387  VAL B O   1 
ATOM   5035 C  CB  . VAL B 2 386 ? 95.803  24.881  11.239  1.00 17.85 ? 387  VAL B CB  1 
ATOM   5036 C  CG1 . VAL B 2 386 ? 97.091  24.731  11.945  1.00 20.07 ? 387  VAL B CG1 1 
ATOM   5037 C  CG2 . VAL B 2 386 ? 94.794  23.800  11.709  1.00 18.16 ? 387  VAL B CG2 1 
ATOM   5038 N  N   . HIS B 2 387 ? 96.424  27.691  9.934   1.00 24.15 ? 388  HIS B N   1 
ATOM   5039 C  CA  . HIS B 2 387 ? 97.390  28.703  9.521   1.00 27.15 ? 388  HIS B CA  1 
ATOM   5040 C  C   . HIS B 2 387 ? 97.092  30.060  10.153  1.00 28.37 ? 388  HIS B C   1 
ATOM   5041 O  O   . HIS B 2 387 ? 97.987  30.711  10.691  1.00 28.88 ? 388  HIS B O   1 
ATOM   5042 C  CB  . HIS B 2 387 ? 97.397  28.820  7.993   1.00 28.65 ? 388  HIS B CB  1 
ATOM   5043 C  CG  . HIS B 2 387 ? 98.359  29.838  7.466   1.00 31.66 ? 388  HIS B CG  1 
ATOM   5044 N  ND1 . HIS B 2 387 ? 98.152  31.195  7.593   1.00 32.85 ? 388  HIS B ND1 1 
ATOM   5045 C  CD2 . HIS B 2 387 ? 99.535  29.697  6.809   1.00 32.91 ? 388  HIS B CD2 1 
ATOM   5046 C  CE1 . HIS B 2 387 ? 99.158  31.846  7.035   1.00 33.73 ? 388  HIS B CE1 1 
ATOM   5047 N  NE2 . HIS B 2 387 ? 100.011 30.960  6.552   1.00 33.79 ? 388  HIS B NE2 1 
ATOM   5048 N  N   . ASP B 2 388 ? 95.833  30.461  10.057  1.00 32.39 ? 389  ASP B N   1 
ATOM   5049 C  CA  . ASP B 2 388 ? 95.369  31.733  10.617  1.00 33.83 ? 389  ASP B CA  1 
ATOM   5050 C  C   . ASP B 2 388 ? 95.633  31.822  12.108  1.00 34.31 ? 389  ASP B C   1 
ATOM   5051 O  O   . ASP B 2 388 ? 96.046  32.869  12.622  1.00 33.36 ? 389  ASP B O   1 
ATOM   5052 C  CB  . ASP B 2 388 ? 93.872  31.881  10.389  1.00 36.04 ? 389  ASP B CB  1 
ATOM   5053 C  CG  . ASP B 2 388 ? 93.537  32.277  8.979   1.00 37.72 ? 389  ASP B CG  1 
ATOM   5054 O  OD1 . ASP B 2 388 ? 94.476  32.410  8.172   1.00 39.85 ? 389  ASP B OD1 1 
ATOM   5055 O  OD2 . ASP B 2 388 ? 92.337  32.457  8.684   1.00 40.53 ? 389  ASP B OD2 1 
ATOM   5056 N  N   . ILE B 2 389 ? 95.382  30.721  12.815  1.00 34.03 ? 390  ILE B N   1 
ATOM   5057 C  CA  . ILE B 2 389 ? 95.584  30.685  14.262  1.00 35.13 ? 390  ILE B CA  1 
ATOM   5058 C  C   . ILE B 2 389 ? 97.027  30.791  14.661  1.00 36.49 ? 390  ILE B C   1 
ATOM   5059 O  O   . ILE B 2 389 ? 97.402  31.643  15.477  1.00 36.08 ? 390  ILE B O   1 
ATOM   5060 C  CB  . ILE B 2 389 ? 95.048  29.389  14.869  1.00 34.81 ? 390  ILE B CB  1 
ATOM   5061 C  CG1 . ILE B 2 389 ? 93.533  29.476  14.971  1.00 34.23 ? 390  ILE B CG1 1 
ATOM   5062 C  CG2 . ILE B 2 389 ? 95.726  29.128  16.214  1.00 35.49 ? 390  ILE B CG2 1 
ATOM   5063 C  CD1 . ILE B 2 389 ? 92.885  28.118  15.105  1.00 33.62 ? 390  ILE B CD1 1 
ATOM   5064 N  N   . LEU B 2 390 ? 97.838  29.910  14.092  1.00 37.84 ? 391  LEU B N   1 
ATOM   5065 C  CA  . LEU B 2 390 ? 99.262  29.894  14.387  1.00 40.57 ? 391  LEU B CA  1 
ATOM   5066 C  C   . LEU B 2 390 ? 99.858  31.262  14.011  1.00 42.19 ? 391  LEU B C   1 
ATOM   5067 O  O   . LEU B 2 390 ? 100.781 31.759  14.671  1.00 42.90 ? 391  LEU B O   1 
ATOM   5068 C  CB  . LEU B 2 390 ? 99.968  28.748  13.615  1.00 39.66 ? 391  LEU B CB  1 
ATOM   5069 C  CG  . LEU B 2 390 ? 99.489  27.298  13.856  1.00 39.98 ? 391  LEU B CG  1 
ATOM   5070 C  CD1 . LEU B 2 390 ? 100.350 26.314  13.065  1.00 39.47 ? 391  LEU B CD1 1 
ATOM   5071 C  CD2 . LEU B 2 390 ? 99.548  26.960  15.333  1.00 39.41 ? 391  LEU B CD2 1 
ATOM   5072 N  N   . LYS B 2 391 ? 99.317  31.890  12.974  1.00 43.95 ? 392  LYS B N   1 
ATOM   5073 C  CA  . LYS B 2 391 ? 99.853  33.188  12.577  1.00 46.01 ? 392  LYS B CA  1 
ATOM   5074 C  C   . LYS B 2 391 ? 99.490  34.232  13.636  1.00 46.90 ? 392  LYS B C   1 
ATOM   5075 O  O   . LYS B 2 391 ? 100.354 35.002  14.070  1.00 47.14 ? 392  LYS B O   1 
ATOM   5076 C  CB  . LYS B 2 391 ? 99.315  33.600  11.202  1.00 46.84 ? 392  LYS B CB  1 
ATOM   5077 C  CG  . LYS B 2 391 ? 100.039 34.796  10.580  1.00 47.94 ? 392  LYS B CG  1 
ATOM   5078 C  CD  . LYS B 2 391 ? 99.454  35.138  9.225   1.00 49.46 ? 392  LYS B CD  1 
ATOM   5079 C  CE  . LYS B 2 391 ? 100.089 36.391  8.640   1.00 50.07 ? 392  LYS B CE  1 
ATOM   5080 N  NZ  . LYS B 2 391 ? 99.496  36.685  7.302   1.00 51.79 ? 392  LYS B NZ  1 
ATOM   5081 N  N   . ALA B 2 392 ? 98.223  34.240  14.056  1.00 47.76 ? 393  ALA B N   1 
ATOM   5082 C  CA  . ALA B 2 392 ? 97.732  35.175  15.074  1.00 48.82 ? 393  ALA B CA  1 
ATOM   5083 C  C   . ALA B 2 392 ? 98.573  35.120  16.353  1.00 49.82 ? 393  ALA B C   1 
ATOM   5084 O  O   . ALA B 2 392 ? 98.691  36.113  17.078  1.00 49.99 ? 393  ALA B O   1 
ATOM   5085 C  CB  . ALA B 2 392 ? 96.275  34.876  15.404  1.00 48.17 ? 393  ALA B CB  1 
ATOM   5086 N  N   . ARG B 2 393 ? 99.147  33.956  16.622  1.00 50.64 ? 394  ARG B N   1 
ATOM   5087 C  CA  . ARG B 2 393 ? 99.969  33.751  17.802  1.00 51.85 ? 394  ARG B CA  1 
ATOM   5088 C  C   . ARG B 2 393 ? 101.432 34.014  17.521  1.00 52.26 ? 394  ARG B C   1 
ATOM   5089 O  O   . ARG B 2 393 ? 102.170 34.397  18.411  1.00 53.05 ? 394  ARG B O   1 
ATOM   5090 C  CB  . ARG B 2 393 ? 99.845  32.313  18.288  1.00 52.27 ? 394  ARG B CB  1 
ATOM   5091 C  CG  . ARG B 2 393 ? 98.475  31.930  18.757  1.00 52.64 ? 394  ARG B CG  1 
ATOM   5092 C  CD  . ARG B 2 393 ? 98.467  30.463  19.105  1.00 52.70 ? 394  ARG B CD  1 
ATOM   5093 N  NE  . ARG B 2 393 ? 97.201  30.087  19.710  1.00 53.04 ? 394  ARG B NE  1 
ATOM   5094 C  CZ  . ARG B 2 393 ? 96.881  28.847  20.059  1.00 52.51 ? 394  ARG B CZ  1 
ATOM   5095 N  NH1 . ARG B 2 393 ? 97.739  27.845  19.862  1.00 51.77 ? 394  ARG B NH1 1 
ATOM   5096 N  NH2 . ARG B 2 393 ? 95.702  28.621  20.608  1.00 52.12 ? 394  ARG B NH2 1 
ATOM   5097 N  N   . GLY B 2 394 ? 101.853 33.782  16.287  1.00 52.70 ? 395  GLY B N   1 
ATOM   5098 C  CA  . GLY B 2 394 ? 103.248 33.977  15.933  1.00 52.89 ? 395  GLY B CA  1 
ATOM   5099 C  C   . GLY B 2 394 ? 103.881 32.674  15.476  1.00 53.22 ? 395  GLY B C   1 
ATOM   5100 O  O   . GLY B 2 394 ? 103.602 31.605  16.030  1.00 53.45 ? 395  GLY B O   1 
HETATM 5101 C  C1  . HPF C 3 .   ? 52.225  25.477  14.792  1.00 12.63 ? 1001 HPF A C1  1 
HETATM 5102 C  C2  . HPF C 3 .   ? 51.632  24.149  14.788  1.00 12.06 ? 1001 HPF A C2  1 
HETATM 5103 C  C3  . HPF C 3 .   ? 50.220  24.130  15.082  1.00 12.51 ? 1001 HPF A C3  1 
HETATM 5104 C  C4  . HPF C 3 .   ? 49.430  25.279  15.340  1.00 11.01 ? 1001 HPF A C4  1 
HETATM 5105 C  C5  . HPF C 3 .   ? 50.082  26.524  15.317  1.00 11.27 ? 1001 HPF A C5  1 
HETATM 5106 C  C6  . HPF C 3 .   ? 51.438  26.630  15.060  1.00 11.83 ? 1001 HPF A C6  1 
HETATM 5107 O  O7  . HPF C 3 .   ? 52.034  27.857  15.060  1.00 13.27 ? 1001 HPF A O7  1 
HETATM 5108 N  N8  . HPF C 3 .   ? 49.305  27.745  15.581  1.00 11.30 ? 1001 HPF A N8  1 
HETATM 5109 C  C9  . HPF C 3 .   ? 48.196  28.058  14.647  1.00 9.49  ? 1001 HPF A C9  1 
HETATM 5110 C  C10 . HPF C 3 .   ? 48.599  28.051  13.164  1.00 11.59 ? 1001 HPF A C10 1 
HETATM 5111 C  C11 . HPF C 3 .   ? 47.448  28.347  12.237  1.00 11.93 ? 1001 HPF A C11 1 
HETATM 5112 O  O12 . HPF C 3 .   ? 47.916  28.060  10.877  1.00 11.31 ? 1001 HPF A O12 1 
HETATM 5113 P  P13 . HPF C 3 .   ? 48.244  29.342  9.952   1.00 12.41 ? 1001 HPF A P13 1 
HETATM 5114 O  O14 . HPF C 3 .   ? 46.886  30.214  9.877   1.00 12.12 ? 1001 HPF A O14 1 
HETATM 5115 O  O15 . HPF C 3 .   ? 49.472  30.197  10.613  1.00 11.44 ? 1001 HPF A O15 1 
HETATM 5116 O  O16 . HPF C 3 .   ? 48.594  28.701  8.656   1.00 13.44 ? 1001 HPF A O16 1 
HETATM 5117 O  O17 . HPF C 3 .   ? 47.110  27.164  14.871  1.00 12.47 ? 1001 HPF A O17 1 
HETATM 5118 O  O18 . HPF C 3 .   ? 49.538  29.163  13.086  1.00 12.34 ? 1001 HPF A O18 1 
HETATM 5119 NA NA  . NA  D 4 .   ? 77.218  17.613  19.976  1.00 10.20 ? 1003 NA  B NA  1 
HETATM 5120 N  N1  . PLP E 5 .   ? 84.588  13.931  11.906  1.00 9.80  ? 1002 PLP B N1  1 
HETATM 5121 C  C2  . PLP E 5 .   ? 84.527  14.392  10.640  1.00 11.23 ? 1002 PLP B C2  1 
HETATM 5122 C  C2A . PLP E 5 .   ? 85.779  14.318  9.763   1.00 12.97 ? 1002 PLP B C2A 1 
HETATM 5123 C  C3  . PLP E 5 .   ? 83.354  14.946  10.182  1.00 13.47 ? 1002 PLP B C3  1 
HETATM 5124 O  O3  . PLP E 5 .   ? 83.269  15.365  8.868   1.00 17.47 ? 1002 PLP B O3  1 
HETATM 5125 C  C4  . PLP E 5 .   ? 82.248  15.049  11.022  1.00 13.75 ? 1002 PLP B C4  1 
HETATM 5126 C  C4A . PLP E 5 .   ? 80.889  15.534  10.460  1.00 19.15 ? 1002 PLP B C4A 1 
HETATM 5127 C  C5  . PLP E 5 .   ? 82.358  14.594  12.329  1.00 9.78  ? 1002 PLP B C5  1 
HETATM 5128 C  C6  . PLP E 5 .   ? 83.514  14.031  12.730  1.00 10.38 ? 1002 PLP B C6  1 
HETATM 5129 C  C5A . PLP E 5 .   ? 81.213  14.808  13.371  1.00 10.92 ? 1002 PLP B C5A 1 
HETATM 5130 O  O4P . PLP E 5 .   ? 79.969  14.063  13.114  1.00 11.03 ? 1002 PLP B O4P 1 
HETATM 5131 P  P   . PLP E 5 .   ? 79.684  12.705  13.861  1.00 8.00  ? 1002 PLP B P   1 
HETATM 5132 O  O1P . PLP E 5 .   ? 78.305  12.426  13.435  1.00 8.19  ? 1002 PLP B O1P 1 
HETATM 5133 O  O2P . PLP E 5 .   ? 79.746  12.986  15.318  1.00 8.46  ? 1002 PLP B O2P 1 
HETATM 5134 O  O3P . PLP E 5 .   ? 80.674  11.666  13.490  1.00 8.93  ? 1002 PLP B O3P 1 
HETATM 5135 O  O   . HOH F 6 .   ? 49.058  19.030  25.826  1.00 14.33 ? 1002 HOH A O   1 
HETATM 5136 O  O   . HOH F 6 .   ? 45.622  24.957  22.342  1.00 15.19 ? 1003 HOH A O   1 
HETATM 5137 O  O   . HOH F 6 .   ? 53.137  13.174  33.400  1.00 15.59 ? 1004 HOH A O   1 
HETATM 5138 O  O   . HOH F 6 .   ? 53.751  31.015  9.554   1.00 13.20 ? 1005 HOH A O   1 
HETATM 5139 O  O   . HOH F 6 .   ? 42.483  17.255  20.849  1.00 14.75 ? 1006 HOH A O   1 
HETATM 5140 O  O   . HOH F 6 .   ? 53.371  7.978   24.840  1.00 17.27 ? 1007 HOH A O   1 
HETATM 5141 O  O   . HOH F 6 .   ? 51.115  39.283  20.080  1.00 15.76 ? 1008 HOH A O   1 
HETATM 5142 O  O   . HOH F 6 .   ? 56.051  27.538  21.792  1.00 19.23 ? 1009 HOH A O   1 
HETATM 5143 O  O   . HOH F 6 .   ? 62.111  31.642  14.381  1.00 19.73 ? 1010 HOH A O   1 
HETATM 5144 O  O   . HOH F 6 .   ? 59.205  23.501  31.579  1.00 24.64 ? 1011 HOH A O   1 
HETATM 5145 O  O   . HOH F 6 .   ? 56.978  28.861  19.178  1.00 18.21 ? 1012 HOH A O   1 
HETATM 5146 O  O   . HOH F 6 .   ? 58.189  27.000  29.680  1.00 19.50 ? 1013 HOH A O   1 
HETATM 5147 O  O   . HOH F 6 .   ? 35.813  36.284  28.694  1.00 18.40 ? 1014 HOH A O   1 
HETATM 5148 O  O   . HOH F 6 .   ? 54.182  20.919  10.512  1.00 22.41 ? 1015 HOH A O   1 
HETATM 5149 O  O   . HOH F 6 .   ? 38.479  24.963  30.996  1.00 22.00 ? 1016 HOH A O   1 
HETATM 5150 O  O   . HOH F 6 .   ? 45.387  41.396  26.990  1.00 22.30 ? 1017 HOH A O   1 
HETATM 5151 O  O   . HOH F 6 .   ? 55.765  37.933  10.871  1.00 15.81 ? 1018 HOH A O   1 
HETATM 5152 O  O   . HOH F 6 .   ? 35.996  39.123  27.861  1.00 28.44 ? 1019 HOH A O   1 
HETATM 5153 O  O   . HOH F 6 .   ? 58.271  44.227  25.778  1.00 25.62 ? 1020 HOH A O   1 
HETATM 5154 O  O   . HOH F 6 .   ? 54.789  31.376  18.640  1.00 18.80 ? 1021 HOH A O   1 
HETATM 5155 O  O   . HOH F 6 .   ? 60.286  43.183  18.915  1.00 20.20 ? 1022 HOH A O   1 
HETATM 5156 O  O   . HOH F 6 .   ? 51.713  19.833  11.190  1.00 18.15 ? 1023 HOH A O   1 
HETATM 5157 O  O   . HOH F 6 .   ? 62.753  31.763  17.056  1.00 16.90 ? 1024 HOH A O   1 
HETATM 5158 O  O   . HOH F 6 .   ? 52.273  37.391  16.852  1.00 16.79 ? 1025 HOH A O   1 
HETATM 5159 O  O   . HOH F 6 .   ? 49.539  18.341  22.561  1.00 16.51 ? 1026 HOH A O   1 
HETATM 5160 O  O   . HOH F 6 .   ? 56.992  11.272  25.915  1.00 17.06 ? 1027 HOH A O   1 
HETATM 5161 O  O   . HOH F 6 .   ? 40.609  15.258  20.050  1.00 19.92 ? 1028 HOH A O   1 
HETATM 5162 O  O   . HOH F 6 .   ? 52.095  33.406  5.897   1.00 20.81 ? 1029 HOH A O   1 
HETATM 5163 O  O   . HOH F 6 .   ? 34.810  20.883  24.360  1.00 20.17 ? 1030 HOH A O   1 
HETATM 5164 O  O   . HOH F 6 .   ? 55.140  46.579  23.427  1.00 20.49 ? 1031 HOH A O   1 
HETATM 5165 O  O   . HOH F 6 .   ? 46.377  44.927  30.109  1.00 30.04 ? 1032 HOH A O   1 
HETATM 5166 O  O   . HOH F 6 .   ? 59.879  32.760  25.516  1.00 20.09 ? 1033 HOH A O   1 
HETATM 5167 O  O   . HOH F 6 .   ? 61.726  36.468  32.813  1.00 27.47 ? 1034 HOH A O   1 
HETATM 5168 O  O   . HOH F 6 .   ? 38.666  43.158  24.912  1.00 21.73 ? 1035 HOH A O   1 
HETATM 5169 O  O   . HOH F 6 .   ? 45.397  31.504  2.964   1.00 37.52 ? 1036 HOH A O   1 
HETATM 5170 O  O   . HOH F 6 .   ? 46.898  39.162  6.558   1.00 24.86 ? 1037 HOH A O   1 
HETATM 5171 O  O   . HOH F 6 .   ? 46.568  32.260  8.259   1.00 16.38 ? 1038 HOH A O   1 
HETATM 5172 O  O   . HOH F 6 .   ? 30.610  25.865  16.918  1.00 20.69 ? 1039 HOH A O   1 
HETATM 5173 O  O   . HOH F 6 .   ? 33.626  29.528  27.953  1.00 16.80 ? 1040 HOH A O   1 
HETATM 5174 O  O   . HOH F 6 .   ? 51.979  10.762  34.248  1.00 18.41 ? 1041 HOH A O   1 
HETATM 5175 O  O   . HOH F 6 .   ? 33.408  19.006  14.560  1.00 29.14 ? 1042 HOH A O   1 
HETATM 5176 O  O   . HOH F 6 .   ? 55.349  29.337  17.041  1.00 22.71 ? 1043 HOH A O   1 
HETATM 5177 O  O   . HOH F 6 .   ? 55.275  49.230  9.587   1.00 28.31 ? 1044 HOH A O   1 
HETATM 5178 O  O   . HOH F 6 .   ? 56.232  46.342  26.259  1.00 28.20 ? 1045 HOH A O   1 
HETATM 5179 O  O   . HOH F 6 .   ? 57.473  9.029   27.248  1.00 26.35 ? 1046 HOH A O   1 
HETATM 5180 O  O   . HOH F 6 .   ? 44.881  28.590  9.612   1.00 13.45 ? 1047 HOH A O   1 
HETATM 5181 O  O   . HOH F 6 .   ? 54.556  31.617  6.916   1.00 16.64 ? 1048 HOH A O   1 
HETATM 5182 O  O   . HOH F 6 .   ? 65.564  31.696  17.254  1.00 22.30 ? 1049 HOH A O   1 
HETATM 5183 O  O   . HOH F 6 .   ? 32.642  29.340  1.662   1.00 24.42 ? 1050 HOH A O   1 
HETATM 5184 O  O   . HOH F 6 .   ? 29.464  22.902  11.678  1.00 24.47 ? 1051 HOH A O   1 
HETATM 5185 O  O   . HOH F 6 .   ? 58.950  45.804  21.427  1.00 28.12 ? 1052 HOH A O   1 
HETATM 5186 O  O   . HOH F 6 .   ? 59.017  15.818  33.321  1.00 19.01 ? 1053 HOH A O   1 
HETATM 5187 O  O   . HOH F 6 .   ? 32.657  29.420  30.637  1.00 24.41 ? 1054 HOH A O   1 
HETATM 5188 O  O   . HOH F 6 .   ? 53.798  8.594   31.569  1.00 30.84 ? 1055 HOH A O   1 
HETATM 5189 O  O   . HOH F 6 .   ? 32.477  23.259  2.807   1.00 24.38 ? 1056 HOH A O   1 
HETATM 5190 O  O   . HOH F 6 .   ? 55.740  33.532  35.505  1.00 19.25 ? 1057 HOH A O   1 
HETATM 5191 O  O   . HOH F 6 .   ? 31.665  40.216  13.349  1.00 25.52 ? 1058 HOH A O   1 
HETATM 5192 O  O   . HOH F 6 .   ? 50.956  19.841  8.372   1.00 16.04 ? 1059 HOH A O   1 
HETATM 5193 O  O   . HOH F 6 .   ? 44.100  11.730  27.388  1.00 32.28 ? 1060 HOH A O   1 
HETATM 5194 O  O   . HOH F 6 .   ? 58.378  6.361   20.221  1.00 25.31 ? 1061 HOH A O   1 
HETATM 5195 O  O   . HOH F 6 .   ? 59.911  40.760  11.527  1.00 28.78 ? 1062 HOH A O   1 
HETATM 5196 O  O   . HOH F 6 .   ? 34.288  33.718  23.898  1.00 21.66 ? 1063 HOH A O   1 
HETATM 5197 O  O   . HOH F 6 .   ? 56.911  15.862  35.471  1.00 23.26 ? 1064 HOH A O   1 
HETATM 5198 O  O   . HOH F 6 .   ? 52.697  5.233   14.470  1.00 26.82 ? 1065 HOH A O   1 
HETATM 5199 O  O   . HOH F 6 .   ? 38.591  14.150  21.781  1.00 24.56 ? 1066 HOH A O   1 
HETATM 5200 O  O   . HOH F 6 .   ? 45.543  20.263  40.069  1.00 31.54 ? 1067 HOH A O   1 
HETATM 5201 O  O   . HOH F 6 .   ? 40.903  16.623  34.004  1.00 27.85 ? 1068 HOH A O   1 
HETATM 5202 O  O   . HOH F 6 .   ? 64.706  20.928  28.757  1.00 21.48 ? 1069 HOH A O   1 
HETATM 5203 O  O   . HOH F 6 .   ? 43.598  26.248  4.410   1.00 20.08 ? 1070 HOH A O   1 
HETATM 5204 O  O   . HOH F 6 .   ? 51.870  5.848   30.320  1.00 22.42 ? 1071 HOH A O   1 
HETATM 5205 O  O   . HOH F 6 .   ? 32.415  36.088  19.026  1.00 22.06 ? 1072 HOH A O   1 
HETATM 5206 O  O   . HOH F 6 .   ? 36.331  20.788  3.645   1.00 34.49 ? 1073 HOH A O   1 
HETATM 5207 O  O   . HOH F 6 .   ? 57.787  29.949  33.114  1.00 27.84 ? 1074 HOH A O   1 
HETATM 5208 O  O   . HOH F 6 .   ? 49.479  16.650  17.635  1.00 21.89 ? 1075 HOH A O   1 
HETATM 5209 O  O   . HOH F 6 .   ? 56.041  47.283  21.187  1.00 33.75 ? 1076 HOH A O   1 
HETATM 5210 O  O   . HOH F 6 .   ? 38.262  6.392   20.321  1.00 27.59 ? 1077 HOH A O   1 
HETATM 5211 O  O   . HOH F 6 .   ? 49.429  53.920  13.545  1.00 37.85 ? 1078 HOH A O   1 
HETATM 5212 O  O   . HOH F 6 .   ? 50.611  7.443   23.750  1.00 31.91 ? 1079 HOH A O   1 
HETATM 5213 O  O   . HOH F 6 .   ? 67.022  38.517  19.959  1.00 34.65 ? 1080 HOH A O   1 
HETATM 5214 O  O   . HOH F 6 .   ? 42.456  44.325  7.945   1.00 30.81 ? 1081 HOH A O   1 
HETATM 5215 O  O   . HOH F 6 .   ? 43.477  46.895  22.753  1.00 34.15 ? 1082 HOH A O   1 
HETATM 5216 O  O   . HOH F 6 .   ? 32.111  33.715  22.195  1.00 26.97 ? 1083 HOH A O   1 
HETATM 5217 O  O   . HOH F 6 .   ? 29.605  24.053  18.499  1.00 23.41 ? 1084 HOH A O   1 
HETATM 5218 O  O   . HOH F 6 .   ? 35.084  37.961  21.862  1.00 23.57 ? 1085 HOH A O   1 
HETATM 5219 O  O   . HOH F 6 .   ? 65.409  38.127  17.834  1.00 34.78 ? 1086 HOH A O   1 
HETATM 5220 O  O   . HOH F 6 .   ? 50.221  38.858  35.821  1.00 28.38 ? 1087 HOH A O   1 
HETATM 5221 O  O   . HOH F 6 .   ? 39.215  35.518  35.531  1.00 25.78 ? 1088 HOH A O   1 
HETATM 5222 O  O   . HOH F 6 .   ? 63.191  18.842  35.279  1.00 39.80 ? 1089 HOH A O   1 
HETATM 5223 O  O   . HOH F 6 .   ? 57.394  18.490  37.187  1.00 19.03 ? 1090 HOH A O   1 
HETATM 5224 O  O   . HOH F 6 .   ? 54.424  24.783  38.555  1.00 24.73 ? 1091 HOH A O   1 
HETATM 5225 O  O   . HOH F 6 .   ? 41.324  24.331  37.855  1.00 32.11 ? 1092 HOH A O   1 
HETATM 5226 O  O   . HOH F 6 .   ? 42.424  26.985  36.160  1.00 30.52 ? 1093 HOH A O   1 
HETATM 5227 O  O   . HOH F 6 .   ? 50.699  17.101  20.303  1.00 22.51 ? 1094 HOH A O   1 
HETATM 5228 O  O   . HOH F 6 .   ? 47.974  18.057  2.373   1.00 29.94 ? 1095 HOH A O   1 
HETATM 5229 O  O   . HOH F 6 .   ? 30.111  13.538  18.561  1.00 37.07 ? 1096 HOH A O   1 
HETATM 5230 O  O   . HOH F 6 .   ? 47.132  36.901  4.649   1.00 39.55 ? 1097 HOH A O   1 
HETATM 5231 O  O   . HOH F 6 .   ? 55.326  47.676  16.838  1.00 28.24 ? 1098 HOH A O   1 
HETATM 5232 O  O   . HOH F 6 .   ? 43.782  26.724  18.527  1.00 22.57 ? 1099 HOH A O   1 
HETATM 5233 O  O   . HOH F 6 .   ? 42.075  27.885  21.886  1.00 24.52 ? 1100 HOH A O   1 
HETATM 5234 O  O   . HOH F 6 .   ? 30.009  21.468  24.366  1.00 28.49 ? 1101 HOH A O   1 
HETATM 5235 O  O   . HOH F 6 .   ? 32.258  20.042  23.632  1.00 27.82 ? 1102 HOH A O   1 
HETATM 5236 O  O   . HOH F 6 .   ? 44.609  34.620  36.178  1.00 26.27 ? 1103 HOH A O   1 
HETATM 5237 O  O   . HOH F 6 .   ? 40.946  48.760  8.832   1.00 40.21 ? 1104 HOH A O   1 
HETATM 5238 O  O   . HOH F 6 .   ? 38.899  48.803  12.373  1.00 28.79 ? 1105 HOH A O   1 
HETATM 5239 O  O   . HOH F 6 .   ? 38.162  26.160  4.597   1.00 22.11 ? 1106 HOH A O   1 
HETATM 5240 O  O   . HOH F 6 .   ? 36.550  35.413  1.632   1.00 21.67 ? 1107 HOH A O   1 
HETATM 5241 O  O   . HOH F 6 .   ? 40.896  26.153  3.699   1.00 24.30 ? 1108 HOH A O   1 
HETATM 5242 O  O   . HOH F 6 .   ? 34.731  16.231  16.562  1.00 23.75 ? 1109 HOH A O   1 
HETATM 5243 O  O   . HOH F 6 .   ? 47.561  28.176  -1.695  1.00 42.07 ? 1110 HOH A O   1 
HETATM 5244 O  O   . HOH F 6 .   ? 54.321  24.214  4.092   1.00 27.23 ? 1111 HOH A O   1 
HETATM 5245 O  O   . HOH F 6 .   ? 52.279  23.283  1.940   1.00 44.73 ? 1112 HOH A O   1 
HETATM 5246 O  O   . HOH F 6 .   ? 51.759  15.732  1.495   1.00 44.97 ? 1113 HOH A O   1 
HETATM 5247 O  O   . HOH F 6 .   ? 49.830  15.848  39.557  1.00 29.24 ? 1114 HOH A O   1 
HETATM 5248 O  O   . HOH F 6 .   ? 46.466  26.125  40.949  1.00 40.84 ? 1115 HOH A O   1 
HETATM 5249 O  O   . HOH F 6 .   ? 48.030  24.142  39.609  1.00 27.14 ? 1116 HOH A O   1 
HETATM 5250 O  O   . HOH F 6 .   ? 49.163  21.810  41.308  1.00 45.95 ? 1117 HOH A O   1 
HETATM 5251 O  O   . HOH F 6 .   ? 62.972  17.822  32.854  1.00 35.77 ? 1118 HOH A O   1 
HETATM 5252 O  O   . HOH F 6 .   ? 57.480  37.239  7.639   1.00 29.62 ? 1119 HOH A O   1 
HETATM 5253 O  O   . HOH F 6 .   ? 34.998  36.279  24.099  1.00 33.74 ? 1120 HOH A O   1 
HETATM 5254 O  O   . HOH F 6 .   ? 51.788  49.559  23.314  1.00 34.04 ? 1121 HOH A O   1 
HETATM 5255 O  O   . HOH F 6 .   ? 37.625  32.776  35.277  1.00 33.46 ? 1122 HOH A O   1 
HETATM 5256 O  O   . HOH F 6 .   ? 62.197  45.066  19.449  1.00 31.54 ? 1123 HOH A O   1 
HETATM 5257 O  O   . HOH F 6 .   ? 35.986  42.921  24.663  1.00 34.09 ? 1124 HOH A O   1 
HETATM 5258 O  O   . HOH F 6 .   ? 34.215  40.862  23.887  1.00 39.33 ? 1125 HOH A O   1 
HETATM 5259 O  O   . HOH F 6 .   ? 32.641  37.684  21.412  1.00 32.18 ? 1126 HOH A O   1 
HETATM 5260 O  O   . HOH F 6 .   ? 66.704  43.508  20.893  1.00 37.96 ? 1127 HOH A O   1 
HETATM 5261 O  O   . HOH F 6 .   ? 62.066  44.747  25.825  1.00 45.92 ? 1128 HOH A O   1 
HETATM 5262 O  O   . HOH F 6 .   ? 62.737  34.250  33.631  1.00 32.72 ? 1129 HOH A O   1 
HETATM 5263 O  O   . HOH F 6 .   ? 55.145  36.269  38.585  1.00 48.44 ? 1130 HOH A O   1 
HETATM 5264 O  O   . HOH F 6 .   ? 43.725  37.594  40.281  1.00 38.63 ? 1131 HOH A O   1 
HETATM 5265 O  O   . HOH F 6 .   ? 39.964  22.816  29.607  1.00 28.88 ? 1132 HOH A O   1 
HETATM 5266 O  O   . HOH F 6 .   ? 56.867  7.383   24.651  1.00 35.52 ? 1133 HOH A O   1 
HETATM 5267 O  O   . HOH F 6 .   ? 39.926  23.118  3.564   1.00 35.76 ? 1134 HOH A O   1 
HETATM 5268 O  O   . HOH F 6 .   ? 34.006  36.275  1.409   1.00 25.57 ? 1135 HOH A O   1 
HETATM 5269 O  O   . HOH F 6 .   ? 37.947  26.375  1.833   1.00 31.64 ? 1136 HOH A O   1 
HETATM 5270 O  O   . HOH F 6 .   ? 39.160  50.731  14.536  1.00 38.47 ? 1137 HOH A O   1 
HETATM 5271 O  O   . HOH F 6 .   ? 54.500  28.271  5.083   1.00 31.53 ? 1138 HOH A O   1 
HETATM 5272 O  O   . HOH F 6 .   ? 34.316  30.148  32.490  1.00 30.32 ? 1139 HOH A O   1 
HETATM 5273 O  O   . HOH F 6 .   ? 52.890  50.300  21.206  1.00 46.14 ? 1140 HOH A O   1 
HETATM 5274 O  O   . HOH F 6 .   ? 32.423  40.529  15.826  1.00 36.92 ? 1141 HOH A O   1 
HETATM 5275 O  O   . HOH F 6 .   ? 30.074  37.127  18.360  1.00 43.65 ? 1142 HOH A O   1 
HETATM 5276 O  O   . HOH F 6 .   ? 56.308  30.757  35.311  1.00 29.24 ? 1143 HOH A O   1 
HETATM 5277 O  O   . HOH F 6 .   ? 33.302  33.289  26.440  1.00 28.87 ? 1144 HOH A O   1 
HETATM 5278 O  O   . HOH F 6 .   ? 57.895  23.074  33.828  1.00 23.65 ? 1145 HOH A O   1 
HETATM 5279 O  O   . HOH F 6 .   ? 51.033  4.594   28.141  1.00 44.24 ? 1146 HOH A O   1 
HETATM 5280 O  O   . HOH F 6 .   ? 37.357  23.727  5.193   1.00 23.15 ? 1147 HOH A O   1 
HETATM 5281 O  O   . HOH F 6 .   ? 31.240  21.008  2.645   1.00 34.40 ? 1148 HOH A O   1 
HETATM 5282 O  O   . HOH F 6 .   ? 34.424  16.709  14.036  1.00 29.19 ? 1149 HOH A O   1 
HETATM 5283 O  O   . HOH F 6 .   ? 42.159  46.570  6.628   1.00 50.33 ? 1150 HOH A O   1 
HETATM 5284 O  O   . HOH F 6 .   ? 29.387  22.953  29.211  1.00 49.40 ? 1151 HOH A O   1 
HETATM 5285 O  O   . HOH F 6 .   ? 31.716  31.065  26.493  1.00 31.61 ? 1152 HOH A O   1 
HETATM 5286 O  O   . HOH F 6 .   ? 28.201  21.551  22.232  1.00 39.46 ? 1153 HOH A O   1 
HETATM 5287 O  O   . HOH F 6 .   ? 24.004  23.476  22.570  1.00 39.11 ? 1154 HOH A O   1 
HETATM 5288 O  O   . HOH F 6 .   ? 59.494  44.323  16.240  1.00 26.23 ? 1155 HOH A O   1 
HETATM 5289 O  O   . HOH F 6 .   ? 58.257  46.907  16.686  1.00 36.71 ? 1156 HOH A O   1 
HETATM 5290 O  O   . HOH F 6 .   ? 54.279  48.344  19.136  1.00 36.12 ? 1157 HOH A O   1 
HETATM 5291 O  O   . HOH F 6 .   ? 60.591  41.283  27.833  1.00 30.38 ? 1158 HOH A O   1 
HETATM 5292 O  O   . HOH F 6 .   ? 52.262  41.190  31.967  1.00 37.58 ? 1159 HOH A O   1 
HETATM 5293 O  O   . HOH F 6 .   ? 54.725  40.094  31.853  1.00 42.80 ? 1160 HOH A O   1 
HETATM 5294 O  O   . HOH F 6 .   ? 49.146  46.893  27.152  1.00 32.60 ? 1161 HOH A O   1 
HETATM 5295 O  O   . HOH F 6 .   ? 44.497  46.602  25.881  1.00 31.27 ? 1162 HOH A O   1 
HETATM 5296 O  O   . HOH F 6 .   ? 41.149  49.336  17.000  1.00 34.80 ? 1163 HOH A O   1 
HETATM 5297 O  O   . HOH F 6 .   ? 41.702  48.267  19.437  1.00 38.29 ? 1164 HOH A O   1 
HETATM 5298 O  O   . HOH F 6 .   ? 63.226  34.742  11.054  1.00 32.71 ? 1165 HOH A O   1 
HETATM 5299 O  O   . HOH F 6 .   ? 62.275  33.458  8.656   1.00 32.04 ? 1166 HOH A O   1 
HETATM 5300 O  O   . HOH F 6 .   ? 66.370  37.456  23.579  1.00 44.25 ? 1167 HOH A O   1 
HETATM 5301 O  O   . HOH F 6 .   ? 60.622  26.000  32.395  1.00 25.95 ? 1168 HOH A O   1 
HETATM 5302 O  O   . HOH F 6 .   ? 45.377  32.266  31.133  1.00 25.64 ? 1169 HOH A O   1 
HETATM 5303 O  O   . HOH F 6 .   ? 48.175  39.713  37.075  1.00 43.93 ? 1170 HOH A O   1 
HETATM 5304 O  O   . HOH F 6 .   ? 39.691  39.465  37.450  1.00 25.21 ? 1171 HOH A O   1 
HETATM 5305 O  O   . HOH F 6 .   ? 31.564  36.418  32.954  1.00 34.69 ? 1172 HOH A O   1 
HETATM 5306 O  O   . HOH F 6 .   ? 51.239  18.023  40.581  1.00 32.80 ? 1173 HOH A O   1 
HETATM 5307 O  O   . HOH F 6 .   ? 42.053  26.597  33.641  1.00 37.95 ? 1174 HOH A O   1 
HETATM 5308 O  O   . HOH F 6 .   ? 40.677  24.180  33.851  1.00 34.49 ? 1175 HOH A O   1 
HETATM 5309 O  O   . HOH F 6 .   ? 54.390  4.892   21.594  1.00 33.51 ? 1176 HOH A O   1 
HETATM 5310 O  O   . HOH F 6 .   ? 57.707  4.641   22.333  1.00 36.84 ? 1177 HOH A O   1 
HETATM 5311 O  O   . HOH F 6 .   ? 58.211  2.371   22.121  1.00 35.75 ? 1178 HOH A O   1 
HETATM 5312 O  O   . HOH F 6 .   ? 42.083  16.868  37.499  1.00 27.98 ? 1179 HOH A O   1 
HETATM 5313 O  O   . HOH F 6 .   ? 40.691  1.105   13.448  1.00 42.72 ? 1180 HOH A O   1 
HETATM 5314 O  O   . HOH F 6 .   ? 36.538  7.980   21.674  1.00 37.41 ? 1181 HOH A O   1 
HETATM 5315 O  O   . HOH F 6 .   ? 37.645  13.960  4.448   1.00 38.50 ? 1182 HOH A O   1 
HETATM 5316 O  O   . HOH F 6 .   ? 31.702  19.229  16.273  1.00 39.40 ? 1183 HOH A O   1 
HETATM 5317 O  O   . HOH F 6 .   ? 37.165  28.793  0.723   1.00 32.72 ? 1184 HOH A O   1 
HETATM 5318 O  O   . HOH F 6 .   ? 29.602  16.752  10.229  1.00 39.88 ? 1185 HOH A O   1 
HETATM 5319 O  O   . HOH F 6 .   ? 44.282  37.372  4.681   1.00 39.45 ? 1186 HOH A O   1 
HETATM 5320 O  O   . HOH F 6 .   ? 56.681  53.582  15.354  1.00 28.70 ? 1187 HOH A O   1 
HETATM 5321 O  O   . HOH F 6 .   ? 36.501  47.828  12.185  1.00 39.09 ? 1188 HOH A O   1 
HETATM 5322 O  O   . HOH F 6 .   ? 37.394  23.363  28.349  1.00 23.46 ? 1189 HOH A O   1 
HETATM 5323 O  O   . HOH F 6 .   ? 24.231  27.078  25.981  1.00 42.66 ? 1190 HOH A O   1 
HETATM 5324 O  O   . HOH F 6 .   ? 46.658  45.953  27.441  1.00 36.16 ? 1191 HOH A O   1 
HETATM 5325 O  O   . HOH F 6 .   ? 41.153  45.787  27.237  1.00 32.08 ? 1192 HOH A O   1 
HETATM 5326 O  O   . HOH F 6 .   ? 34.640  45.347  15.999  1.00 35.63 ? 1193 HOH A O   1 
HETATM 5327 O  O   . HOH F 6 .   ? 41.499  26.818  19.679  1.00 30.58 ? 1194 HOH A O   1 
HETATM 5328 O  O   . HOH F 6 .   ? 55.126  37.245  6.432   1.00 33.71 ? 1195 HOH A O   1 
HETATM 5329 O  O   . HOH F 6 .   ? 63.824  38.610  31.837  1.00 36.43 ? 1196 HOH A O   1 
HETATM 5330 O  O   . HOH F 6 .   ? 42.060  34.646  37.316  1.00 37.86 ? 1197 HOH A O   1 
HETATM 5331 O  O   . HOH F 6 .   ? 52.435  26.282  39.466  1.00 31.80 ? 1198 HOH A O   1 
HETATM 5332 O  O   . HOH F 6 .   ? 43.088  22.145  41.111  1.00 44.92 ? 1199 HOH A O   1 
HETATM 5333 O  O   . HOH F 6 .   ? 47.600  7.426   29.670  1.00 27.32 ? 1200 HOH A O   1 
HETATM 5334 O  O   . HOH F 6 .   ? 41.362  18.417  31.515  1.00 31.75 ? 1201 HOH A O   1 
HETATM 5335 O  O   . HOH F 6 .   ? 48.439  10.476  9.612   1.00 28.09 ? 1202 HOH A O   1 
HETATM 5336 O  O   . HOH F 6 .   ? 38.531  5.448   9.454   1.00 44.80 ? 1203 HOH A O   1 
HETATM 5337 O  O   . HOH F 6 .   ? 44.685  6.744   27.537  1.00 42.24 ? 1204 HOH A O   1 
HETATM 5338 O  O   . HOH F 6 .   ? 38.283  15.110  30.996  1.00 41.87 ? 1205 HOH A O   1 
HETATM 5339 O  O   . HOH F 6 .   ? 36.399  17.618  25.360  1.00 37.54 ? 1206 HOH A O   1 
HETATM 5340 O  O   . HOH F 6 .   ? 41.646  21.234  3.348   1.00 29.12 ? 1207 HOH A O   1 
HETATM 5341 O  O   . HOH F 6 .   ? 32.554  15.106  17.764  1.00 40.06 ? 1208 HOH A O   1 
HETATM 5342 O  O   . HOH F 6 .   ? 36.565  14.354  24.201  1.00 45.31 ? 1209 HOH A O   1 
HETATM 5343 O  O   . HOH F 6 .   ? 33.022  31.605  -1.403  1.00 33.27 ? 1210 HOH A O   1 
HETATM 5344 O  O   . HOH F 6 .   ? 28.887  28.011  7.034   1.00 30.77 ? 1211 HOH A O   1 
HETATM 5345 O  O   . HOH F 6 .   ? 35.654  43.983  8.492   1.00 30.64 ? 1212 HOH A O   1 
HETATM 5346 O  O   . HOH F 6 .   ? 33.269  42.932  8.904   1.00 36.75 ? 1213 HOH A O   1 
HETATM 5347 O  O   . HOH F 6 .   ? 49.107  50.978  20.424  1.00 39.68 ? 1214 HOH A O   1 
HETATM 5348 O  O   . HOH F 6 .   ? 59.662  45.848  23.999  1.00 31.48 ? 1215 HOH A O   1 
HETATM 5349 O  O   . HOH F 6 .   ? 59.521  43.518  28.288  1.00 45.53 ? 1216 HOH A O   1 
HETATM 5350 O  O   . HOH F 6 .   ? 63.906  35.027  25.777  1.00 36.87 ? 1217 HOH A O   1 
HETATM 5351 O  O   . HOH F 6 .   ? 60.294  37.568  34.679  1.00 45.29 ? 1218 HOH A O   1 
HETATM 5352 O  O   . HOH F 6 .   ? 32.584  34.390  34.654  1.00 34.72 ? 1219 HOH A O   1 
HETATM 5353 O  O   . HOH F 6 .   ? 40.822  29.312  35.925  1.00 41.97 ? 1220 HOH A O   1 
HETATM 5354 O  O   . HOH F 6 .   ? 50.074  5.176   16.667  1.00 43.71 ? 1221 HOH A O   1 
HETATM 5355 O  O   . HOH F 6 .   ? 49.894  6.025   21.014  1.00 44.73 ? 1222 HOH A O   1 
HETATM 5356 O  O   . HOH F 6 .   ? 54.875  7.063   29.280  1.00 33.29 ? 1223 HOH A O   1 
HETATM 5357 O  O   . HOH F 6 .   ? 53.763  5.866   25.947  1.00 50.73 ? 1224 HOH A O   1 
HETATM 5358 O  O   . HOH F 6 .   ? 49.710  16.996  24.694  1.00 36.58 ? 1225 HOH A O   1 
HETATM 5359 O  O   . HOH F 6 .   ? 39.397  18.240  29.804  1.00 40.51 ? 1226 HOH A O   1 
HETATM 5360 O  O   . HOH F 6 .   ? 38.517  20.238  33.253  1.00 48.08 ? 1227 HOH A O   1 
HETATM 5361 O  O   . HOH F 6 .   ? 48.188  5.265   13.207  1.00 42.73 ? 1228 HOH A O   1 
HETATM 5362 O  O   . HOH F 6 .   ? 48.767  6.806   11.282  1.00 40.40 ? 1229 HOH A O   1 
HETATM 5363 O  O   . HOH F 6 .   ? 44.131  2.266   10.833  1.00 38.15 ? 1230 HOH A O   1 
HETATM 5364 O  O   . HOH F 6 .   ? 45.082  4.204   25.395  1.00 50.54 ? 1231 HOH A O   1 
HETATM 5365 O  O   . HOH F 6 .   ? 44.859  19.699  1.832   1.00 34.33 ? 1232 HOH A O   1 
HETATM 5366 O  O   . HOH F 6 .   ? 27.120  25.969  7.535   1.00 39.72 ? 1233 HOH A O   1 
HETATM 5367 O  O   . HOH F 6 .   ? 30.996  16.400  7.733   1.00 41.95 ? 1234 HOH A O   1 
HETATM 5368 O  O   . HOH F 6 .   ? 28.380  20.703  12.469  1.00 40.56 ? 1235 HOH A O   1 
HETATM 5369 O  O   . HOH F 6 .   ? 31.128  17.464  18.060  1.00 38.30 ? 1236 HOH A O   1 
HETATM 5370 O  O   . HOH F 6 .   ? 50.989  55.892  14.084  1.00 36.68 ? 1237 HOH A O   1 
HETATM 5371 O  O   . HOH F 6 .   ? 53.841  55.758  13.969  1.00 43.10 ? 1238 HOH A O   1 
HETATM 5372 O  O   . HOH F 6 .   ? 38.061  20.836  28.031  1.00 44.57 ? 1239 HOH A O   1 
HETATM 5373 O  O   . HOH F 6 .   ? 25.717  21.526  22.375  1.00 50.07 ? 1240 HOH A O   1 
HETATM 5374 O  O   . HOH F 6 .   ? 44.093  49.535  22.884  1.00 43.20 ? 1241 HOH A O   1 
HETATM 5375 O  O   . HOH F 6 .   ? 39.237  46.920  22.768  1.00 46.16 ? 1242 HOH A O   1 
HETATM 5376 O  O   . HOH F 6 .   ? 63.062  41.388  15.212  1.00 37.25 ? 1243 HOH A O   1 
HETATM 5377 O  O   . HOH F 6 .   ? 63.468  39.657  29.499  1.00 39.66 ? 1244 HOH A O   1 
HETATM 5378 O  O   . HOH F 6 .   ? 53.679  40.666  36.061  1.00 49.34 ? 1245 HOH A O   1 
HETATM 5379 O  O   . HOH F 6 .   ? 52.623  43.761  31.916  1.00 43.55 ? 1246 HOH A O   1 
HETATM 5380 O  O   . HOH F 6 .   ? 40.175  7.392   7.985   1.00 38.45 ? 1247 HOH A O   1 
HETATM 5381 O  O   . HOH F 6 .   ? 47.390  8.033   9.760   1.00 36.06 ? 1248 HOH A O   1 
HETATM 5382 O  O   . HOH F 6 .   ? 51.579  20.942  1.713   1.00 38.11 ? 1249 HOH A O   1 
HETATM 5383 O  O   . HOH F 6 .   ? 27.420  27.921  4.641   1.00 37.46 ? 1250 HOH A O   1 
HETATM 5384 O  O   . HOH F 6 .   ? 44.564  40.411  5.711   1.00 43.55 ? 1251 HOH A O   1 
HETATM 5385 O  O   . HOH F 6 .   ? 48.477  41.609  5.976   1.00 37.82 ? 1252 HOH A O   1 
HETATM 5386 O  O   . HOH F 6 .   ? 46.221  44.128  6.172   1.00 45.35 ? 1253 HOH A O   1 
HETATM 5387 O  O   . HOH F 6 .   ? 51.116  50.607  8.370   1.00 47.38 ? 1254 HOH A O   1 
HETATM 5388 O  O   . HOH F 6 .   ? 33.974  25.941  33.060  1.00 47.21 ? 1255 HOH A O   1 
HETATM 5389 O  O   . HOH F 6 .   ? 30.226  21.346  18.813  1.00 42.73 ? 1256 HOH A O   1 
HETATM 5390 O  O   . HOH F 6 .   ? 23.764  23.960  26.195  1.00 49.14 ? 1257 HOH A O   1 
HETATM 5391 O  O   . HOH F 6 .   ? 27.180  22.367  28.078  1.00 48.93 ? 1258 HOH A O   1 
HETATM 5392 O  O   . HOH F 6 .   ? 25.937  24.570  28.877  1.00 53.77 ? 1259 HOH A O   1 
HETATM 5393 O  O   . HOH F 6 .   ? 52.905  45.886  29.904  1.00 45.12 ? 1260 HOH A O   1 
HETATM 5394 O  O   . HOH F 6 .   ? 55.516  45.283  30.414  1.00 48.41 ? 1261 HOH A O   1 
HETATM 5395 O  O   . HOH F 6 .   ? 66.366  36.039  29.032  1.00 42.01 ? 1262 HOH A O   1 
HETATM 5396 O  O   . HOH F 6 .   ? 59.652  19.871  38.190  1.00 44.67 ? 1263 HOH A O   1 
HETATM 5397 O  O   . HOH F 6 .   ? 55.826  13.203  33.530  1.00 44.35 ? 1264 HOH A O   1 
HETATM 5398 O  O   . HOH F 6 .   ? 50.466  25.000  41.453  1.00 44.80 ? 1265 HOH A O   1 
HETATM 5399 O  O   . HOH F 6 .   ? 50.102  33.198  39.074  1.00 45.87 ? 1266 HOH A O   1 
HETATM 5400 O  O   . HOH F 6 .   ? 47.447  33.701  38.672  1.00 39.56 ? 1267 HOH A O   1 
HETATM 5401 O  O   . HOH F 6 .   ? 50.755  8.080   12.835  1.00 36.15 ? 1268 HOH A O   1 
HETATM 5402 O  O   . HOH F 6 .   ? 51.307  3.255   13.397  1.00 48.40 ? 1269 HOH A O   1 
HETATM 5403 O  O   . HOH F 6 .   ? 39.682  20.237  30.951  1.00 42.03 ? 1270 HOH A O   1 
HETATM 5404 O  O   . HOH F 6 .   ? 41.754  10.557  28.110  1.00 41.61 ? 1271 HOH A O   1 
HETATM 5405 O  O   . HOH F 6 .   ? 49.098  21.982  -0.108  1.00 51.72 ? 1272 HOH A O   1 
HETATM 5406 O  O   . HOH F 6 .   ? 53.033  41.401  6.469   1.00 43.41 ? 1273 HOH A O   1 
HETATM 5407 O  O   . HOH F 6 .   ? 53.848  55.029  10.842  1.00 40.36 ? 1274 HOH A O   1 
HETATM 5408 O  O   . HOH F 6 .   ? 43.494  51.764  16.595  1.00 34.23 ? 1275 HOH A O   1 
HETATM 5409 O  O   . HOH F 6 .   ? 30.271  30.816  30.642  1.00 42.74 ? 1276 HOH A O   1 
HETATM 5410 O  O   . HOH F 6 .   ? 22.148  20.899  18.329  1.00 49.18 ? 1277 HOH A O   1 
HETATM 5411 O  O   . HOH F 6 .   ? 27.201  25.660  13.487  1.00 38.33 ? 1278 HOH A O   1 
HETATM 5412 O  O   . HOH F 6 .   ? 62.676  45.661  22.156  1.00 49.12 ? 1279 HOH A O   1 
HETATM 5413 O  O   . HOH F 6 .   ? 50.788  46.949  29.364  1.00 45.80 ? 1280 HOH A O   1 
HETATM 5414 O  O   . HOH F 6 .   ? 50.428  45.140  32.753  1.00 47.86 ? 1281 HOH A O   1 
HETATM 5415 O  O   . HOH F 6 .   ? 41.505  47.421  24.003  1.00 47.64 ? 1282 HOH A O   1 
HETATM 5416 O  O   . HOH F 6 .   ? 61.458  44.088  14.519  1.00 39.78 ? 1283 HOH A O   1 
HETATM 5417 O  O   . HOH F 6 .   ? 67.616  41.727  18.548  1.00 52.90 ? 1284 HOH A O   1 
HETATM 5418 O  O   . HOH F 6 .   ? 51.750  35.164  38.104  1.00 47.25 ? 1285 HOH A O   1 
HETATM 5419 O  O   . HOH F 6 .   ? 51.475  41.184  34.384  1.00 43.18 ? 1286 HOH A O   1 
HETATM 5420 O  O   . HOH F 6 .   ? 42.637  31.307  37.080  1.00 42.08 ? 1287 HOH A O   1 
HETATM 5421 O  O   . HOH F 6 .   ? 56.639  28.966  37.581  1.00 40.31 ? 1288 HOH A O   1 
HETATM 5422 O  O   . HOH F 6 .   ? 39.275  18.089  34.991  1.00 41.43 ? 1289 HOH A O   1 
HETATM 5423 O  O   . HOH F 6 .   ? 29.778  14.836  6.161   1.00 46.41 ? 1290 HOH A O   1 
HETATM 5424 O  O   . HOH F 6 .   ? 27.449  17.985  14.823  1.00 44.88 ? 1291 HOH A O   1 
HETATM 5425 O  O   . HOH F 6 .   ? 54.577  43.157  5.894   1.00 38.07 ? 1292 HOH A O   1 
HETATM 5426 O  O   . HOH F 6 .   ? 48.981  48.689  6.260   1.00 46.57 ? 1293 HOH A O   1 
HETATM 5427 O  O   . HOH F 6 .   ? 33.162  43.323  15.790  1.00 47.38 ? 1294 HOH A O   1 
HETATM 5428 O  O   . HOH F 6 .   ? 56.975  25.651  34.501  1.00 36.32 ? 1295 HOH A O   1 
HETATM 5429 O  O   . HOH F 6 .   ? 57.624  27.342  32.375  1.00 31.47 ? 1296 HOH A O   1 
HETATM 5430 O  O   . HOH F 6 .   ? 65.425  21.401  35.291  1.00 42.45 ? 1297 HOH A O   1 
HETATM 5431 O  O   . HOH F 6 .   ? 55.126  19.198  39.806  1.00 46.41 ? 1298 HOH A O   1 
HETATM 5432 O  O   . HOH F 6 .   ? 47.287  35.465  1.852   1.00 44.59 ? 1299 HOH A O   1 
HETATM 5433 O  O   . HOH F 6 .   ? 31.637  17.028  21.634  1.00 44.71 ? 1300 HOH A O   1 
HETATM 5434 O  O   . HOH F 6 .   ? 42.357  50.807  20.545  1.00 45.64 ? 1301 HOH A O   1 
HETATM 5435 O  O   . HOH F 6 .   ? 28.965  30.129  8.630   1.00 49.41 ? 1302 HOH A O   1 
HETATM 5436 O  O   . HOH F 6 .   ? 39.098  45.643  26.021  1.00 38.00 ? 1303 HOH A O   1 
HETATM 5437 O  O   . HOH F 6 .   ? 26.030  25.116  10.425  1.00 40.37 ? 1304 HOH A O   1 
HETATM 5438 O  O   . HOH F 6 .   ? 61.630  16.136  33.623  1.00 38.40 ? 1305 HOH A O   1 
HETATM 5439 O  O   . HOH F 6 .   ? 63.280  38.848  9.690   1.00 38.61 ? 1306 HOH A O   1 
HETATM 5440 O  O   . HOH F 6 .   ? 57.504  4.978   25.520  1.00 43.77 ? 1307 HOH A O   1 
HETATM 5441 O  O   . HOH F 6 .   ? 64.481  23.444  34.191  1.00 34.19 ? 1308 HOH A O   1 
HETATM 5442 O  O   . HOH F 6 .   ? 65.617  36.092  31.851  1.00 41.55 ? 1309 HOH A O   1 
HETATM 5443 O  O   . HOH F 6 .   ? 28.744  16.273  17.723  1.00 42.55 ? 1310 HOH A O   1 
HETATM 5444 O  O   . HOH F 6 .   ? 34.029  14.922  23.050  1.00 42.24 ? 1311 HOH A O   1 
HETATM 5445 O  O   . HOH F 6 .   ? 27.071  19.651  9.869   1.00 42.36 ? 1312 HOH A O   1 
HETATM 5446 O  O   . HOH F 6 .   ? 49.401  7.991   6.316   1.00 41.85 ? 1313 HOH A O   1 
HETATM 5447 O  O   . HOH G 6 .   ? 72.995  5.217   17.353  1.00 8.28  ? 1004 HOH B O   1 
HETATM 5448 O  O   . HOH G 6 .   ? 81.054  -1.269  14.590  1.00 10.13 ? 1005 HOH B O   1 
HETATM 5449 O  O   . HOH G 6 .   ? 80.651  10.555  16.583  1.00 8.63  ? 1006 HOH B O   1 
HETATM 5450 O  O   . HOH G 6 .   ? 65.522  9.245   18.613  1.00 8.02  ? 1007 HOH B O   1 
HETATM 5451 O  O   . HOH G 6 .   ? 66.665  4.906   16.312  1.00 9.63  ? 1008 HOH B O   1 
HETATM 5452 O  O   . HOH G 6 .   ? 73.629  -1.272  19.163  1.00 19.09 ? 1009 HOH B O   1 
HETATM 5453 O  O   . HOH G 6 .   ? 73.876  16.066  -6.206  1.00 12.89 ? 1010 HOH B O   1 
HETATM 5454 O  O   . HOH G 6 .   ? 87.742  -1.896  -7.017  1.00 12.52 ? 1011 HOH B O   1 
HETATM 5455 O  O   . HOH G 6 .   ? 86.825  10.271  15.647  1.00 9.38  ? 1012 HOH B O   1 
HETATM 5456 O  O   . HOH G 6 .   ? 74.055  10.030  29.841  1.00 10.54 ? 1013 HOH B O   1 
HETATM 5457 O  O   . HOH G 6 .   ? 82.418  15.387  27.222  1.00 14.15 ? 1014 HOH B O   1 
HETATM 5458 O  O   . HOH G 6 .   ? 84.231  1.969   28.160  1.00 14.34 ? 1015 HOH B O   1 
HETATM 5459 O  O   . HOH G 6 .   ? 72.620  7.536   18.760  1.00 9.05  ? 1016 HOH B O   1 
HETATM 5460 O  O   . HOH G 6 .   ? 101.328 4.220   27.820  1.00 13.26 ? 1017 HOH B O   1 
HETATM 5461 O  O   . HOH G 6 .   ? 102.199 2.676   18.034  1.00 10.95 ? 1018 HOH B O   1 
HETATM 5462 O  O   . HOH G 6 .   ? 73.063  0.428   23.228  1.00 15.45 ? 1019 HOH B O   1 
HETATM 5463 O  O   . HOH G 6 .   ? 77.716  9.864   9.167   1.00 10.93 ? 1020 HOH B O   1 
HETATM 5464 O  O   . HOH G 6 .   ? 81.302  9.532   30.855  1.00 8.83  ? 1021 HOH B O   1 
HETATM 5465 O  O   . HOH G 6 .   ? 90.420  18.998  28.154  1.00 16.54 ? 1022 HOH B O   1 
HETATM 5466 O  O   . HOH G 6 .   ? 92.589  2.662   2.858   1.00 15.51 ? 1023 HOH B O   1 
HETATM 5467 O  O   . HOH G 6 .   ? 51.262  17.472  12.599  1.00 14.88 ? 1024 HOH B O   1 
HETATM 5468 O  O   . HOH G 6 .   ? 83.522  -3.628  5.295   1.00 20.18 ? 1025 HOH B O   1 
HETATM 5469 O  O   . HOH G 6 .   ? 84.743  10.237  31.475  1.00 14.20 ? 1026 HOH B O   1 
HETATM 5470 O  O   . HOH G 6 .   ? 86.871  22.173  20.672  1.00 9.40  ? 1027 HOH B O   1 
HETATM 5471 O  O   . HOH G 6 .   ? 66.219  6.566   18.503  1.00 9.29  ? 1028 HOH B O   1 
HETATM 5472 O  O   . HOH G 6 .   ? 61.786  9.300   3.282   1.00 15.75 ? 1029 HOH B O   1 
HETATM 5473 O  O   . HOH G 6 .   ? 60.997  21.010  21.425  1.00 12.25 ? 1030 HOH B O   1 
HETATM 5474 O  O   . HOH G 6 .   ? 82.507  12.108  3.334   1.00 14.91 ? 1031 HOH B O   1 
HETATM 5475 O  O   . HOH G 6 .   ? 83.058  8.228   32.542  1.00 13.14 ? 1032 HOH B O   1 
HETATM 5476 O  O   . HOH G 6 .   ? 91.698  25.799  24.103  1.00 16.74 ? 1033 HOH B O   1 
HETATM 5477 O  O   . HOH G 6 .   ? 63.164  29.370  13.053  1.00 17.65 ? 1034 HOH B O   1 
HETATM 5478 O  O   . HOH G 6 .   ? 61.360  17.841  18.495  1.00 15.48 ? 1035 HOH B O   1 
HETATM 5479 O  O   . HOH G 6 .   ? 87.710  22.102  29.607  1.00 13.22 ? 1036 HOH B O   1 
HETATM 5480 O  O   . HOH G 6 .   ? 90.698  7.909   29.241  1.00 16.36 ? 1037 HOH B O   1 
HETATM 5481 O  O   . HOH G 6 .   ? 94.703  4.963   29.709  1.00 12.51 ? 1038 HOH B O   1 
HETATM 5482 O  O   . HOH G 6 .   ? 78.952  19.151  19.982  1.00 21.00 ? 1039 HOH B O   1 
HETATM 5483 O  O   . HOH G 6 .   ? 84.993  -8.197  12.214  1.00 15.04 ? 1040 HOH B O   1 
HETATM 5484 O  O   . HOH G 6 .   ? 90.581  28.693  19.820  1.00 26.94 ? 1041 HOH B O   1 
HETATM 5485 O  O   . HOH G 6 .   ? 96.267  6.996   30.748  1.00 11.66 ? 1042 HOH B O   1 
HETATM 5486 O  O   . HOH G 6 .   ? 86.360  24.809  11.734  1.00 22.10 ? 1043 HOH B O   1 
HETATM 5487 O  O   . HOH G 6 .   ? 60.002  7.573   4.599   1.00 16.83 ? 1044 HOH B O   1 
HETATM 5488 O  O   . HOH G 6 .   ? 69.964  4.287   31.467  1.00 17.43 ? 1045 HOH B O   1 
HETATM 5489 O  O   . HOH G 6 .   ? 63.738  29.511  7.856   1.00 20.48 ? 1046 HOH B O   1 
HETATM 5490 O  O   . HOH G 6 .   ? 78.541  16.198  21.421  1.00 12.15 ? 1047 HOH B O   1 
HETATM 5491 O  O   . HOH G 6 .   ? 74.880  16.825  9.891   1.00 27.94 ? 1048 HOH B O   1 
HETATM 5492 O  O   . HOH G 6 .   ? 57.016  20.393  10.801  1.00 22.81 ? 1049 HOH B O   1 
HETATM 5493 O  O   . HOH G 6 .   ? 103.210 20.177  12.480  1.00 16.45 ? 1050 HOH B O   1 
HETATM 5494 O  O   . HOH G 6 .   ? 104.824 11.711  29.258  1.00 18.22 ? 1051 HOH B O   1 
HETATM 5495 O  O   . HOH G 6 .   ? 106.130 9.393   22.416  1.00 21.80 ? 1052 HOH B O   1 
HETATM 5496 O  O   . HOH G 6 .   ? 64.601  -3.040  18.494  1.00 24.49 ? 1053 HOH B O   1 
HETATM 5497 O  O   . HOH G 6 .   ? 94.010  1.894   28.082  1.00 21.15 ? 1054 HOH B O   1 
HETATM 5498 O  O   . HOH G 6 .   ? 91.013  28.353  23.314  1.00 24.34 ? 1055 HOH B O   1 
HETATM 5499 O  O   . HOH G 6 .   ? 96.138  16.038  24.469  1.00 15.29 ? 1056 HOH B O   1 
HETATM 5500 O  O   . HOH G 6 .   ? 74.183  25.133  8.831   1.00 15.82 ? 1057 HOH B O   1 
HETATM 5501 O  O   . HOH G 6 .   ? 87.086  21.486  11.491  1.00 20.04 ? 1058 HOH B O   1 
HETATM 5502 O  O   . HOH G 6 .   ? 76.659  12.080  7.564   1.00 17.07 ? 1059 HOH B O   1 
HETATM 5503 O  O   . HOH G 6 .   ? 73.882  9.540   32.501  1.00 17.48 ? 1060 HOH B O   1 
HETATM 5504 O  O   . HOH G 6 .   ? 74.024  -1.691  24.846  1.00 23.73 ? 1061 HOH B O   1 
HETATM 5505 O  O   . HOH G 6 .   ? 86.807  -10.010 13.388  1.00 18.79 ? 1062 HOH B O   1 
HETATM 5506 O  O   . HOH G 6 .   ? 65.219  27.475  11.287  1.00 18.31 ? 1063 HOH B O   1 
HETATM 5507 O  O   . HOH G 6 .   ? 90.436  -5.634  25.310  1.00 17.01 ? 1064 HOH B O   1 
HETATM 5508 O  O   . HOH G 6 .   ? 91.058  -10.921 11.357  1.00 17.73 ? 1065 HOH B O   1 
HETATM 5509 O  O   . HOH G 6 .   ? 91.870  9.454   31.254  1.00 25.03 ? 1066 HOH B O   1 
HETATM 5510 O  O   . HOH G 6 .   ? 68.027  5.866   30.637  1.00 21.43 ? 1067 HOH B O   1 
HETATM 5511 O  O   . HOH G 6 .   ? 72.221  12.473  29.892  1.00 22.77 ? 1068 HOH B O   1 
HETATM 5512 O  O   . HOH G 6 .   ? 62.036  8.854   28.026  1.00 22.47 ? 1069 HOH B O   1 
HETATM 5513 O  O   . HOH G 6 .   ? 83.589  16.205  29.560  1.00 17.15 ? 1070 HOH B O   1 
HETATM 5514 O  O   . HOH G 6 .   ? 90.493  14.610  27.785  1.00 12.40 ? 1071 HOH B O   1 
HETATM 5515 O  O   . HOH G 6 .   ? 61.501  32.364  31.935  1.00 22.92 ? 1072 HOH B O   1 
HETATM 5516 O  O   . HOH G 6 .   ? 87.883  20.149  27.655  1.00 15.11 ? 1073 HOH B O   1 
HETATM 5517 O  O   . HOH G 6 .   ? 66.629  31.852  27.456  1.00 25.02 ? 1074 HOH B O   1 
HETATM 5518 O  O   . HOH G 6 .   ? 84.201  24.707  3.047   1.00 19.35 ? 1075 HOH B O   1 
HETATM 5519 O  O   . HOH G 6 .   ? 100.636 -1.834  32.143  1.00 23.12 ? 1076 HOH B O   1 
HETATM 5520 O  O   . HOH G 6 .   ? 88.008  7.392   29.533  1.00 23.40 ? 1077 HOH B O   1 
HETATM 5521 O  O   . HOH G 6 .   ? 51.664  17.386  15.766  1.00 16.23 ? 1078 HOH B O   1 
HETATM 5522 O  O   . HOH G 6 .   ? 83.519  14.332  31.584  1.00 18.80 ? 1079 HOH B O   1 
HETATM 5523 O  O   . HOH G 6 .   ? 70.506  -0.531  22.833  1.00 20.67 ? 1080 HOH B O   1 
HETATM 5524 O  O   . HOH G 6 .   ? 101.601 -1.539  23.801  1.00 15.67 ? 1081 HOH B O   1 
HETATM 5525 O  O   . HOH G 6 .   ? 87.347  15.464  29.932  1.00 15.50 ? 1082 HOH B O   1 
HETATM 5526 O  O   . HOH G 6 .   ? 82.529  3.199   32.617  1.00 21.75 ? 1083 HOH B O   1 
HETATM 5527 O  O   . HOH G 6 .   ? 66.348  -1.826  -2.651  1.00 19.22 ? 1084 HOH B O   1 
HETATM 5528 O  O   . HOH G 6 .   ? 101.073 -3.863  12.876  1.00 20.21 ? 1085 HOH B O   1 
HETATM 5529 O  O   . HOH G 6 .   ? 88.189  11.968  -1.611  1.00 22.11 ? 1086 HOH B O   1 
HETATM 5530 O  O   . HOH G 6 .   ? 82.596  9.043   35.165  1.00 17.91 ? 1087 HOH B O   1 
HETATM 5531 O  O   . HOH G 6 .   ? 54.560  11.619  6.865   1.00 17.82 ? 1088 HOH B O   1 
HETATM 5532 O  O   . HOH G 6 .   ? 88.388  -0.503  -2.352  1.00 21.18 ? 1089 HOH B O   1 
HETATM 5533 O  O   . HOH G 6 .   ? 96.981  17.084  22.123  1.00 14.93 ? 1090 HOH B O   1 
HETATM 5534 O  O   . HOH G 6 .   ? 92.739  28.773  21.244  1.00 38.51 ? 1091 HOH B O   1 
HETATM 5535 O  O   . HOH G 6 .   ? 60.873  27.682  30.349  1.00 23.58 ? 1092 HOH B O   1 
HETATM 5536 O  O   . HOH G 6 .   ? 89.935  17.884  4.318   1.00 17.11 ? 1093 HOH B O   1 
HETATM 5537 O  O   . HOH G 6 .   ? 82.267  -3.530  0.808   1.00 23.90 ? 1094 HOH B O   1 
HETATM 5538 O  O   . HOH G 6 .   ? 91.368  -4.543  27.707  1.00 22.44 ? 1095 HOH B O   1 
HETATM 5539 O  O   . HOH G 6 .   ? 70.768  30.256  30.682  1.00 31.41 ? 1096 HOH B O   1 
HETATM 5540 O  O   . HOH G 6 .   ? 80.642  28.878  -2.988  1.00 27.93 ? 1097 HOH B O   1 
HETATM 5541 O  O   . HOH G 6 .   ? 78.626  -6.783  -3.642  1.00 22.29 ? 1098 HOH B O   1 
HETATM 5542 O  O   . HOH G 6 .   ? 91.344  -9.766  23.106  1.00 28.49 ? 1099 HOH B O   1 
HETATM 5543 O  O   . HOH G 6 .   ? 65.494  28.731  14.412  1.00 20.90 ? 1100 HOH B O   1 
HETATM 5544 O  O   . HOH G 6 .   ? 67.678  0.443   -3.392  1.00 22.41 ? 1101 HOH B O   1 
HETATM 5545 O  O   . HOH G 6 .   ? 57.274  2.049   19.552  1.00 25.67 ? 1102 HOH B O   1 
HETATM 5546 O  O   . HOH G 6 .   ? 70.409  12.063  31.949  1.00 18.19 ? 1103 HOH B O   1 
HETATM 5547 O  O   . HOH G 6 .   ? 88.292  -11.519 11.760  1.00 21.95 ? 1104 HOH B O   1 
HETATM 5548 O  O   . HOH G 6 .   ? 76.192  -2.440  26.727  1.00 26.43 ? 1105 HOH B O   1 
HETATM 5549 O  O   . HOH G 6 .   ? 91.415  2.878   28.902  1.00 23.53 ? 1106 HOH B O   1 
HETATM 5550 O  O   . HOH G 6 .   ? 87.156  8.967   31.587  1.00 20.48 ? 1107 HOH B O   1 
HETATM 5551 O  O   . HOH G 6 .   ? 87.889  11.323  -4.245  1.00 17.39 ? 1108 HOH B O   1 
HETATM 5552 O  O   . HOH G 6 .   ? 68.972  0.251   17.832  1.00 21.70 ? 1109 HOH B O   1 
HETATM 5553 O  O   . HOH G 6 .   ? 82.659  -8.372  13.511  1.00 19.58 ? 1110 HOH B O   1 
HETATM 5554 O  O   . HOH G 6 .   ? 77.273  27.029  27.834  1.00 31.57 ? 1111 HOH B O   1 
HETATM 5555 O  O   . HOH G 6 .   ? 78.470  17.748  14.888  1.00 21.36 ? 1112 HOH B O   1 
HETATM 5556 O  O   . HOH G 6 .   ? 98.755  15.562  25.992  1.00 23.99 ? 1113 HOH B O   1 
HETATM 5557 O  O   . HOH G 6 .   ? 72.168  -2.466  27.207  1.00 24.67 ? 1114 HOH B O   1 
HETATM 5558 O  O   . HOH G 6 .   ? 67.602  31.042  1.179   1.00 27.98 ? 1115 HOH B O   1 
HETATM 5559 O  O   . HOH G 6 .   ? 59.225  11.414  -6.626  1.00 31.55 ? 1116 HOH B O   1 
HETATM 5560 O  O   . HOH G 6 .   ? 73.703  -2.679  5.961   1.00 23.45 ? 1117 HOH B O   1 
HETATM 5561 O  O   . HOH G 6 .   ? 69.791  16.715  32.399  1.00 22.66 ? 1118 HOH B O   1 
HETATM 5562 O  O   . HOH G 6 .   ? 54.419  15.284  0.081   1.00 23.47 ? 1119 HOH B O   1 
HETATM 5563 O  O   . HOH G 6 .   ? 76.259  -4.835  2.865   1.00 31.47 ? 1120 HOH B O   1 
HETATM 5564 O  O   . HOH G 6 .   ? 104.573 14.346  28.459  1.00 31.57 ? 1121 HOH B O   1 
HETATM 5565 O  O   . HOH G 6 .   ? 72.184  26.050  -5.287  1.00 22.69 ? 1122 HOH B O   1 
HETATM 5566 O  O   . HOH G 6 .   ? 85.702  -11.655 15.309  1.00 28.14 ? 1123 HOH B O   1 
HETATM 5567 O  O   . HOH G 6 .   ? 65.543  18.366  -4.442  1.00 22.76 ? 1124 HOH B O   1 
HETATM 5568 O  O   . HOH G 6 .   ? 65.185  -3.000  23.206  1.00 44.33 ? 1125 HOH B O   1 
HETATM 5569 O  O   . HOH G 6 .   ? 75.815  24.710  16.608  1.00 22.55 ? 1126 HOH B O   1 
HETATM 5570 O  O   . HOH G 6 .   ? 78.664  -5.485  19.738  1.00 18.63 ? 1127 HOH B O   1 
HETATM 5571 O  O   . HOH G 6 .   ? 90.255  25.949  7.019   1.00 25.89 ? 1128 HOH B O   1 
HETATM 5572 O  O   . HOH G 6 .   ? 59.815  -4.440  6.922   1.00 23.71 ? 1129 HOH B O   1 
HETATM 5573 O  O   . HOH G 6 .   ? 109.017 11.359  14.563  1.00 23.78 ? 1130 HOH B O   1 
HETATM 5574 O  O   . HOH G 6 .   ? 83.962  30.833  2.912   1.00 26.39 ? 1131 HOH B O   1 
HETATM 5575 O  O   . HOH G 6 .   ? 73.335  25.136  15.617  1.00 19.62 ? 1132 HOH B O   1 
HETATM 5576 O  O   . HOH G 6 .   ? 63.459  32.440  26.935  1.00 20.90 ? 1133 HOH B O   1 
HETATM 5577 O  O   . HOH G 6 .   ? 58.459  13.028  27.795  1.00 22.60 ? 1134 HOH B O   1 
HETATM 5578 O  O   . HOH G 6 .   ? 72.732  11.975  -11.241 1.00 26.60 ? 1135 HOH B O   1 
HETATM 5579 O  O   . HOH G 6 .   ? 76.916  15.956  13.543  1.00 24.98 ? 1136 HOH B O   1 
HETATM 5580 O  O   . HOH G 6 .   ? 88.727  2.485   28.514  1.00 21.39 ? 1137 HOH B O   1 
HETATM 5581 O  O   . HOH G 6 .   ? 63.994  33.466  13.155  1.00 24.12 ? 1138 HOH B O   1 
HETATM 5582 O  O   . HOH G 6 .   ? 99.053  14.826  28.535  1.00 21.15 ? 1139 HOH B O   1 
HETATM 5583 O  O   . HOH G 6 .   ? 74.368  -10.084 -0.023  1.00 24.61 ? 1140 HOH B O   1 
HETATM 5584 O  O   . HOH G 6 .   ? 58.551  8.851   -6.386  1.00 23.07 ? 1141 HOH B O   1 
HETATM 5585 O  O   . HOH G 6 .   ? 83.295  18.377  8.893   1.00 24.27 ? 1142 HOH B O   1 
HETATM 5586 O  O   . HOH G 6 .   ? 88.311  24.552  9.693   1.00 24.91 ? 1143 HOH B O   1 
HETATM 5587 O  O   . HOH G 6 .   ? 106.692 11.549  31.255  1.00 26.88 ? 1144 HOH B O   1 
HETATM 5588 O  O   . HOH G 6 .   ? 65.903  -6.588  9.377   1.00 21.60 ? 1145 HOH B O   1 
HETATM 5589 O  O   . HOH G 6 .   ? 84.247  -10.295 19.362  1.00 24.66 ? 1146 HOH B O   1 
HETATM 5590 O  O   . HOH G 6 .   ? 76.692  -8.582  0.214   1.00 29.27 ? 1147 HOH B O   1 
HETATM 5591 O  O   . HOH G 6 .   ? 86.054  -8.404  25.724  1.00 25.58 ? 1148 HOH B O   1 
HETATM 5592 O  O   . HOH G 6 .   ? 94.800  -6.457  8.418   1.00 31.12 ? 1149 HOH B O   1 
HETATM 5593 O  O   . HOH G 6 .   ? 101.446 -1.501  34.521  1.00 33.66 ? 1150 HOH B O   1 
HETATM 5594 O  O   . HOH G 6 .   ? 70.630  25.094  30.852  1.00 27.69 ? 1151 HOH B O   1 
HETATM 5595 O  O   . HOH G 6 .   ? 105.159 -0.865  32.792  1.00 28.28 ? 1152 HOH B O   1 
HETATM 5596 O  O   . HOH G 6 .   ? 48.436  14.338  17.064  1.00 21.00 ? 1153 HOH B O   1 
HETATM 5597 O  O   . HOH G 6 .   ? 105.238 10.622  24.618  1.00 27.71 ? 1154 HOH B O   1 
HETATM 5598 O  O   . HOH G 6 .   ? 58.243  0.950   3.877   1.00 25.74 ? 1155 HOH B O   1 
HETATM 5599 O  O   . HOH G 6 .   ? 97.342  15.632  30.695  1.00 29.06 ? 1156 HOH B O   1 
HETATM 5600 O  O   . HOH G 6 .   ? 63.585  -8.075  2.634   1.00 21.60 ? 1157 HOH B O   1 
HETATM 5601 O  O   . HOH G 6 .   ? 87.555  4.742   29.794  1.00 24.40 ? 1158 HOH B O   1 
HETATM 5602 O  O   . HOH G 6 .   ? 91.908  5.438   30.012  1.00 23.34 ? 1159 HOH B O   1 
HETATM 5603 O  O   . HOH G 6 .   ? 90.141  -2.009  28.374  1.00 21.62 ? 1160 HOH B O   1 
HETATM 5604 O  O   . HOH G 6 .   ? 78.629  17.961  10.815  1.00 49.39 ? 1161 HOH B O   1 
HETATM 5605 O  O   . HOH G 6 .   ? 76.897  12.422  32.421  1.00 23.91 ? 1162 HOH B O   1 
HETATM 5606 O  O   . HOH G 6 .   ? 106.722 3.109   9.151   1.00 38.05 ? 1163 HOH B O   1 
HETATM 5607 O  O   . HOH G 6 .   ? 74.432  16.918  12.154  1.00 29.20 ? 1164 HOH B O   1 
HETATM 5608 O  O   . HOH G 6 .   ? 107.466 4.964   10.796  1.00 26.33 ? 1165 HOH B O   1 
HETATM 5609 O  O   . HOH G 6 .   ? 85.046  -10.176 23.693  1.00 25.40 ? 1166 HOH B O   1 
HETATM 5610 O  O   . HOH G 6 .   ? 104.442 12.882  23.547  1.00 27.65 ? 1167 HOH B O   1 
HETATM 5611 O  O   . HOH G 6 .   ? 65.981  18.632  31.883  1.00 28.84 ? 1168 HOH B O   1 
HETATM 5612 O  O   . HOH G 6 .   ? 89.511  17.173  29.721  1.00 29.22 ? 1169 HOH B O   1 
HETATM 5613 O  O   . HOH G 6 .   ? 99.534  -7.987  20.621  1.00 30.56 ? 1170 HOH B O   1 
HETATM 5614 O  O   . HOH G 6 .   ? 99.543  -3.396  24.115  1.00 28.98 ? 1171 HOH B O   1 
HETATM 5615 O  O   . HOH G 6 .   ? 78.485  -3.474  7.266   1.00 33.18 ? 1172 HOH B O   1 
HETATM 5616 O  O   . HOH G 6 .   ? 95.542  -5.113  28.319  1.00 31.33 ? 1173 HOH B O   1 
HETATM 5617 O  O   . HOH G 6 .   ? 73.526  -11.003 2.408   1.00 48.15 ? 1174 HOH B O   1 
HETATM 5618 O  O   . HOH G 6 .   ? 78.919  27.402  23.589  1.00 26.68 ? 1175 HOH B O   1 
HETATM 5619 O  O   . HOH G 6 .   ? 92.648  25.585  26.604  1.00 32.76 ? 1176 HOH B O   1 
HETATM 5620 O  O   . HOH G 6 .   ? 84.775  -8.872  9.529   1.00 25.65 ? 1177 HOH B O   1 
HETATM 5621 O  O   . HOH G 6 .   ? 61.680  15.008  -8.713  1.00 46.21 ? 1178 HOH B O   1 
HETATM 5622 O  O   . HOH G 6 .   ? 77.364  26.394  14.797  1.00 26.96 ? 1179 HOH B O   1 
HETATM 5623 O  O   . HOH G 6 .   ? 85.331  21.472  8.985   1.00 40.34 ? 1180 HOH B O   1 
HETATM 5624 O  O   . HOH G 6 .   ? 65.564  28.907  3.890   1.00 34.09 ? 1181 HOH B O   1 
HETATM 5625 O  O   . HOH G 6 .   ? 68.080  30.618  18.033  1.00 29.55 ? 1182 HOH B O   1 
HETATM 5626 O  O   . HOH G 6 .   ? 60.735  28.583  6.079   1.00 22.62 ? 1183 HOH B O   1 
HETATM 5627 O  O   . HOH G 6 .   ? 60.631  29.781  32.409  1.00 28.56 ? 1184 HOH B O   1 
HETATM 5628 O  O   . HOH G 6 .   ? 56.171  5.857   17.851  1.00 33.78 ? 1185 HOH B O   1 
HETATM 5629 O  O   . HOH G 6 .   ? 55.316  3.855   19.106  1.00 38.56 ? 1186 HOH B O   1 
HETATM 5630 O  O   . HOH G 6 .   ? 58.504  12.206  30.382  1.00 31.42 ? 1187 HOH B O   1 
HETATM 5631 O  O   . HOH G 6 .   ? 53.668  4.866   6.869   1.00 25.78 ? 1188 HOH B O   1 
HETATM 5632 O  O   . HOH G 6 .   ? 52.124  5.014   9.324   1.00 31.97 ? 1189 HOH B O   1 
HETATM 5633 O  O   . HOH G 6 .   ? 63.340  -7.684  0.108   1.00 32.25 ? 1190 HOH B O   1 
HETATM 5634 O  O   . HOH G 6 .   ? 76.026  -1.283  -6.310  1.00 33.04 ? 1191 HOH B O   1 
HETATM 5635 O  O   . HOH G 6 .   ? 83.050  -5.965  -5.872  1.00 29.99 ? 1192 HOH B O   1 
HETATM 5636 O  O   . HOH G 6 .   ? 105.603 10.209  27.174  1.00 30.25 ? 1193 HOH B O   1 
HETATM 5637 O  O   . HOH G 6 .   ? 87.325  15.611  6.431   1.00 17.49 ? 1194 HOH B O   1 
HETATM 5638 O  O   . HOH G 6 .   ? 87.019  15.824  3.605   1.00 31.32 ? 1195 HOH B O   1 
HETATM 5639 O  O   . HOH G 6 .   ? 65.350  31.038  6.043   1.00 27.90 ? 1196 HOH B O   1 
HETATM 5640 O  O   . HOH G 6 .   ? 66.029  0.660   17.068  1.00 18.37 ? 1197 HOH B O   1 
HETATM 5641 O  O   . HOH G 6 .   ? 85.116  -6.408  8.207   1.00 29.52 ? 1198 HOH B O   1 
HETATM 5642 O  O   . HOH G 6 .   ? 96.177  -12.999 14.306  1.00 35.90 ? 1199 HOH B O   1 
HETATM 5643 O  O   . HOH G 6 .   ? 101.614 -6.486  13.308  1.00 27.03 ? 1200 HOH B O   1 
HETATM 5644 O  O   . HOH G 6 .   ? 94.940  -0.461  28.981  1.00 43.25 ? 1201 HOH B O   1 
HETATM 5645 O  O   . HOH G 6 .   ? 92.182  1.607   31.323  1.00 32.05 ? 1202 HOH B O   1 
HETATM 5646 O  O   . HOH G 6 .   ? 77.692  -4.678  26.589  1.00 25.45 ? 1203 HOH B O   1 
HETATM 5647 O  O   . HOH G 6 .   ? 89.809  23.643  30.433  1.00 25.97 ? 1204 HOH B O   1 
HETATM 5648 O  O   . HOH G 6 .   ? 87.413  27.792  13.858  1.00 28.56 ? 1205 HOH B O   1 
HETATM 5649 O  O   . HOH G 6 .   ? 97.808  24.355  20.834  1.00 24.56 ? 1206 HOH B O   1 
HETATM 5650 O  O   . HOH G 6 .   ? 88.943  11.219  32.050  1.00 36.30 ? 1207 HOH B O   1 
HETATM 5651 O  O   . HOH G 6 .   ? 84.890  16.454  7.045   1.00 24.48 ? 1208 HOH B O   1 
HETATM 5652 O  O   . HOH G 6 .   ? 92.005  24.747  3.903   1.00 29.51 ? 1209 HOH B O   1 
HETATM 5653 O  O   . HOH G 6 .   ? 100.245 23.393  19.733  1.00 39.01 ? 1210 HOH B O   1 
HETATM 5654 O  O   . HOH G 6 .   ? 98.323  19.432  24.310  1.00 23.12 ? 1211 HOH B O   1 
HETATM 5655 O  O   . HOH G 6 .   ? 96.279  19.163  28.194  1.00 22.02 ? 1212 HOH B O   1 
HETATM 5656 O  O   . HOH G 6 .   ? 96.288  23.243  26.157  1.00 39.04 ? 1213 HOH B O   1 
HETATM 5657 O  O   . HOH G 6 .   ? 97.392  22.085  24.288  1.00 31.73 ? 1214 HOH B O   1 
HETATM 5658 O  O   . HOH G 6 .   ? 90.912  25.631  29.076  1.00 37.71 ? 1215 HOH B O   1 
HETATM 5659 O  O   . HOH G 6 .   ? 89.929  13.646  30.299  1.00 26.35 ? 1216 HOH B O   1 
HETATM 5660 O  O   . HOH G 6 .   ? 87.246  13.739  32.000  1.00 36.04 ? 1217 HOH B O   1 
HETATM 5661 O  O   . HOH G 6 .   ? 70.255  8.023   33.289  1.00 21.35 ? 1218 HOH B O   1 
HETATM 5662 O  O   . HOH G 6 .   ? 85.071  27.808  15.144  1.00 37.87 ? 1219 HOH B O   1 
HETATM 5663 O  O   . HOH G 6 .   ? 73.792  14.695  29.991  1.00 25.91 ? 1220 HOH B O   1 
HETATM 5664 O  O   . HOH G 6 .   ? 83.135  32.859  28.633  1.00 35.48 ? 1221 HOH B O   1 
HETATM 5665 O  O   . HOH G 6 .   ? 80.762  -7.545  20.177  1.00 29.84 ? 1222 HOH B O   1 
HETATM 5666 O  O   . HOH G 6 .   ? 74.464  -5.221  24.861  1.00 42.08 ? 1223 HOH B O   1 
HETATM 5667 O  O   . HOH G 6 .   ? 92.571  -12.797 12.573  1.00 34.66 ? 1224 HOH B O   1 
HETATM 5668 O  O   . HOH G 6 .   ? 82.485  -5.073  7.460   1.00 27.63 ? 1225 HOH B O   1 
HETATM 5669 O  O   . HOH G 6 .   ? 74.145  -3.728  9.676   1.00 33.87 ? 1226 HOH B O   1 
HETATM 5670 O  O   . HOH G 6 .   ? 55.691  15.743  -2.605  1.00 28.94 ? 1227 HOH B O   1 
HETATM 5671 O  O   . HOH G 6 .   ? 71.038  34.704  12.767  1.00 42.32 ? 1228 HOH B O   1 
HETATM 5672 O  O   . HOH G 6 .   ? 69.531  28.824  -3.011  1.00 31.45 ? 1229 HOH B O   1 
HETATM 5673 O  O   . HOH G 6 .   ? 66.749  20.558  -5.886  1.00 35.40 ? 1230 HOH B O   1 
HETATM 5674 O  O   . HOH G 6 .   ? 79.741  31.315  0.459   1.00 37.49 ? 1231 HOH B O   1 
HETATM 5675 O  O   . HOH G 6 .   ? 79.663  33.692  8.866   1.00 35.60 ? 1232 HOH B O   1 
HETATM 5676 O  O   . HOH G 6 .   ? 104.213 0.771   18.057  1.00 26.78 ? 1233 HOH B O   1 
HETATM 5677 O  O   . HOH G 6 .   ? 105.147 5.550   12.370  1.00 21.78 ? 1234 HOH B O   1 
HETATM 5678 O  O   . HOH G 6 .   ? 78.570  -8.621  -1.609  1.00 34.78 ? 1235 HOH B O   1 
HETATM 5679 O  O   . HOH G 6 .   ? 59.995  5.691   27.158  1.00 45.25 ? 1236 HOH B O   1 
HETATM 5680 O  O   . HOH G 6 .   ? 58.685  13.454  32.347  1.00 38.47 ? 1237 HOH B O   1 
HETATM 5681 O  O   . HOH G 6 .   ? 58.582  26.938  5.641   1.00 29.51 ? 1238 HOH B O   1 
HETATM 5682 O  O   . HOH G 6 .   ? 66.409  35.643  11.469  1.00 36.43 ? 1239 HOH B O   1 
HETATM 5683 O  O   . HOH G 6 .   ? 66.692  -1.744  16.973  1.00 28.20 ? 1240 HOH B O   1 
HETATM 5684 O  O   . HOH G 6 .   ? 60.495  1.710   23.892  1.00 27.27 ? 1241 HOH B O   1 
HETATM 5685 O  O   . HOH G 6 .   ? 66.191  -5.038  11.640  1.00 34.62 ? 1242 HOH B O   1 
HETATM 5686 O  O   . HOH G 6 .   ? 63.865  -6.699  13.023  1.00 34.09 ? 1243 HOH B O   1 
HETATM 5687 O  O   . HOH G 6 .   ? 60.396  0.308   0.538   1.00 23.77 ? 1244 HOH B O   1 
HETATM 5688 O  O   . HOH G 6 .   ? 61.200  -2.105  1.726   1.00 18.60 ? 1245 HOH B O   1 
HETATM 5689 O  O   . HOH G 6 .   ? 68.176  -7.922  9.676   1.00 35.50 ? 1246 HOH B O   1 
HETATM 5690 O  O   . HOH G 6 .   ? 70.780  -10.298 4.171   1.00 50.38 ? 1247 HOH B O   1 
HETATM 5691 O  O   . HOH G 6 .   ? 89.337  -4.159  -5.838  1.00 34.00 ? 1248 HOH B O   1 
HETATM 5692 O  O   . HOH G 6 .   ? 87.207  -6.001  -0.307  1.00 42.03 ? 1249 HOH B O   1 
HETATM 5693 O  O   . HOH G 6 .   ? 102.939 3.163   9.035   1.00 40.44 ? 1250 HOH B O   1 
HETATM 5694 O  O   . HOH G 6 .   ? 104.896 0.952   22.439  1.00 37.14 ? 1251 HOH B O   1 
HETATM 5695 O  O   . HOH G 6 .   ? 77.686  14.311  11.303  1.00 32.66 ? 1252 HOH B O   1 
HETATM 5696 O  O   . HOH G 6 .   ? 63.195  4.239   -7.067  1.00 23.50 ? 1253 HOH B O   1 
HETATM 5697 O  O   . HOH G 6 .   ? 68.735  19.647  -7.031  1.00 39.71 ? 1254 HOH B O   1 
HETATM 5698 O  O   . HOH G 6 .   ? 57.769  21.259  1.405   1.00 24.76 ? 1255 HOH B O   1 
HETATM 5699 O  O   . HOH G 6 .   ? 58.552  16.212  -7.090  1.00 45.22 ? 1256 HOH B O   1 
HETATM 5700 O  O   . HOH G 6 .   ? 80.745  -8.818  11.650  1.00 41.91 ? 1257 HOH B O   1 
HETATM 5701 O  O   . HOH G 6 .   ? 102.669 -4.073  17.474  1.00 37.18 ? 1258 HOH B O   1 
HETATM 5702 O  O   . HOH G 6 .   ? 79.740  -8.658  16.096  1.00 37.11 ? 1259 HOH B O   1 
HETATM 5703 O  O   . HOH G 6 .   ? 82.169  -3.296  29.684  1.00 31.56 ? 1260 HOH B O   1 
HETATM 5704 O  O   . HOH G 6 .   ? 85.601  32.091  19.667  1.00 34.40 ? 1261 HOH B O   1 
HETATM 5705 O  O   . HOH G 6 .   ? 83.406  25.583  36.224  1.00 37.27 ? 1262 HOH B O   1 
HETATM 5706 O  O   . HOH G 6 .   ? 77.845  14.655  33.519  1.00 32.89 ? 1263 HOH B O   1 
HETATM 5707 O  O   . HOH G 6 .   ? 69.038  1.717   31.925  1.00 25.58 ? 1264 HOH B O   1 
HETATM 5708 O  O   . HOH G 6 .   ? 86.704  7.520   33.753  1.00 39.73 ? 1265 HOH B O   1 
HETATM 5709 O  O   . HOH G 6 .   ? 56.740  22.351  3.775   1.00 25.05 ? 1266 HOH B O   1 
HETATM 5710 O  O   . HOH G 6 .   ? 61.353  30.567  4.347   1.00 40.96 ? 1267 HOH B O   1 
HETATM 5711 O  O   . HOH G 6 .   ? 66.502  25.225  34.175  1.00 27.99 ? 1268 HOH B O   1 
HETATM 5712 O  O   . HOH G 6 .   ? 60.122  9.597   26.705  1.00 29.71 ? 1269 HOH B O   1 
HETATM 5713 O  O   . HOH G 6 .   ? 54.953  4.640   15.096  1.00 29.43 ? 1270 HOH B O   1 
HETATM 5714 O  O   . HOH G 6 .   ? 56.659  -3.991  17.125  1.00 40.72 ? 1271 HOH B O   1 
HETATM 5715 O  O   . HOH G 6 .   ? 59.087  -5.940  14.879  1.00 34.03 ? 1272 HOH B O   1 
HETATM 5716 O  O   . HOH G 6 .   ? 57.292  0.961   10.826  1.00 24.61 ? 1273 HOH B O   1 
HETATM 5717 O  O   . HOH G 6 .   ? 66.767  1.006   20.407  1.00 25.18 ? 1274 HOH B O   1 
HETATM 5718 O  O   . HOH G 6 .   ? 58.372  -6.023  9.001   1.00 31.47 ? 1275 HOH B O   1 
HETATM 5719 O  O   . HOH G 6 .   ? 60.885  -7.001  6.401   1.00 31.14 ? 1276 HOH B O   1 
HETATM 5720 O  O   . HOH G 6 .   ? 67.846  -3.965  -3.771  1.00 42.79 ? 1277 HOH B O   1 
HETATM 5721 O  O   . HOH G 6 .   ? 75.870  -1.957  7.357   1.00 49.73 ? 1278 HOH B O   1 
HETATM 5722 O  O   . HOH G 6 .   ? 77.270  -7.449  2.707   1.00 29.82 ? 1279 HOH B O   1 
HETATM 5723 O  O   . HOH G 6 .   ? 81.067  -5.981  -3.495  1.00 29.96 ? 1280 HOH B O   1 
HETATM 5724 O  O   . HOH G 6 .   ? 81.174  -4.755  -9.061  1.00 35.57 ? 1281 HOH B O   1 
HETATM 5725 O  O   . HOH G 6 .   ? 85.071  -3.867  0.821   1.00 30.55 ? 1282 HOH B O   1 
HETATM 5726 O  O   . HOH G 6 .   ? 85.396  -5.106  3.254   1.00 41.43 ? 1283 HOH B O   1 
HETATM 5727 O  O   . HOH G 6 .   ? 109.506 9.341   17.565  1.00 31.54 ? 1284 HOH B O   1 
HETATM 5728 O  O   . HOH G 6 .   ? 103.668 -2.405  19.509  1.00 34.29 ? 1285 HOH B O   1 
HETATM 5729 O  O   . HOH G 6 .   ? 88.946  4.754   0.349   1.00 24.64 ? 1286 HOH B O   1 
HETATM 5730 O  O   . HOH G 6 .   ? 65.577  11.582  -9.109  1.00 31.77 ? 1287 HOH B O   1 
HETATM 5731 O  O   . HOH G 6 .   ? 84.561  19.336  4.440   1.00 27.96 ? 1288 HOH B O   1 
HETATM 5732 O  O   . HOH G 6 .   ? 86.161  20.471  2.584   1.00 33.60 ? 1289 HOH B O   1 
HETATM 5733 O  O   . HOH G 6 .   ? 84.685  22.464  6.185   1.00 36.43 ? 1290 HOH B O   1 
HETATM 5734 O  O   . HOH G 6 .   ? 71.183  13.507  -10.013 1.00 32.92 ? 1291 HOH B O   1 
HETATM 5735 O  O   . HOH G 6 .   ? 77.006  25.212  12.407  1.00 32.99 ? 1292 HOH B O   1 
HETATM 5736 O  O   . HOH G 6 .   ? 75.419  33.580  3.756   1.00 34.65 ? 1293 HOH B O   1 
HETATM 5737 O  O   . HOH G 6 .   ? 80.643  26.378  9.476   1.00 31.75 ? 1294 HOH B O   1 
HETATM 5738 O  O   . HOH G 6 .   ? 86.347  23.007  2.777   1.00 39.06 ? 1295 HOH B O   1 
HETATM 5739 O  O   . HOH G 6 .   ? 73.777  22.745  -8.775  1.00 38.57 ? 1296 HOH B O   1 
HETATM 5740 O  O   . HOH G 6 .   ? 70.436  28.164  -5.630  1.00 43.69 ? 1297 HOH B O   1 
HETATM 5741 O  O   . HOH G 6 .   ? 71.254  35.789  7.727   1.00 47.68 ? 1298 HOH B O   1 
HETATM 5742 O  O   . HOH G 6 .   ? 73.694  -5.430  12.992  1.00 30.96 ? 1299 HOH B O   1 
HETATM 5743 O  O   . HOH G 6 .   ? 82.008  -2.649  3.369   1.00 37.12 ? 1300 HOH B O   1 
HETATM 5744 O  O   . HOH G 6 .   ? 91.740  -7.702  8.283   1.00 31.24 ? 1301 HOH B O   1 
HETATM 5745 O  O   . HOH G 6 .   ? 91.199  -11.226 8.752   1.00 45.06 ? 1302 HOH B O   1 
HETATM 5746 O  O   . HOH G 6 .   ? 98.094  -4.997  28.744  1.00 40.34 ? 1303 HOH B O   1 
HETATM 5747 O  O   . HOH G 6 .   ? 97.795  -3.867  26.137  1.00 26.05 ? 1304 HOH B O   1 
HETATM 5748 O  O   . HOH G 6 .   ? 78.764  -9.389  26.198  1.00 31.70 ? 1305 HOH B O   1 
HETATM 5749 O  O   . HOH G 6 .   ? 89.391  31.032  19.448  1.00 38.18 ? 1306 HOH B O   1 
HETATM 5750 O  O   . HOH G 6 .   ? 78.610  24.642  30.421  1.00 33.76 ? 1307 HOH B O   1 
HETATM 5751 O  O   . HOH G 6 .   ? 75.861  23.098  28.315  1.00 33.31 ? 1308 HOH B O   1 
HETATM 5752 O  O   . HOH G 6 .   ? 67.485  31.431  30.391  1.00 38.85 ? 1309 HOH B O   1 
HETATM 5753 O  O   . HOH G 6 .   ? 63.976  28.920  33.969  1.00 44.98 ? 1310 HOH B O   1 
HETATM 5754 O  O   . HOH G 6 .   ? 67.265  33.001  24.992  1.00 46.32 ? 1311 HOH B O   1 
HETATM 5755 O  O   . HOH G 6 .   ? 81.830  26.598  13.246  1.00 32.85 ? 1312 HOH B O   1 
HETATM 5756 O  O   . HOH G 6 .   ? 85.498  17.625  30.496  1.00 31.81 ? 1313 HOH B O   1 
HETATM 5757 O  O   . HOH G 6 .   ? 85.330  12.639  32.558  1.00 32.60 ? 1314 HOH B O   1 
HETATM 5758 O  O   . HOH G 6 .   ? 93.653  23.072  27.036  1.00 25.71 ? 1315 HOH B O   1 
HETATM 5759 O  O   . HOH G 6 .   ? 96.426  18.088  30.731  1.00 36.44 ? 1316 HOH B O   1 
HETATM 5760 O  O   . HOH G 6 .   ? 111.838 19.391  10.815  1.00 35.82 ? 1317 HOH B O   1 
HETATM 5761 O  O   . HOH G 6 .   ? 105.611 14.708  25.542  1.00 55.00 ? 1318 HOH B O   1 
HETATM 5762 O  O   . HOH G 6 .   ? 107.737 9.026   27.668  1.00 29.96 ? 1319 HOH B O   1 
HETATM 5763 O  O   . HOH G 6 .   ? 98.322  -2.197  31.153  1.00 37.89 ? 1320 HOH B O   1 
HETATM 5764 O  O   . HOH G 6 .   ? 96.022  -1.242  33.035  1.00 51.40 ? 1321 HOH B O   1 
HETATM 5765 O  O   . HOH G 6 .   ? 95.923  35.243  11.389  1.00 41.69 ? 1322 HOH B O   1 
HETATM 5766 O  O   . HOH G 6 .   ? 68.463  30.204  20.941  1.00 41.17 ? 1323 HOH B O   1 
HETATM 5767 O  O   . HOH G 6 .   ? 56.811  27.708  4.247   1.00 35.37 ? 1324 HOH B O   1 
HETATM 5768 O  O   . HOH G 6 .   ? 58.376  9.768   30.341  1.00 35.77 ? 1325 HOH B O   1 
HETATM 5769 O  O   . HOH G 6 .   ? 62.122  -5.290  17.383  1.00 36.06 ? 1326 HOH B O   1 
HETATM 5770 O  O   . HOH G 6 .   ? 72.687  -6.629  -5.703  1.00 35.50 ? 1327 HOH B O   1 
HETATM 5771 O  O   . HOH G 6 .   ? 82.446  -6.316  -0.781  1.00 37.73 ? 1328 HOH B O   1 
HETATM 5772 O  O   . HOH G 6 .   ? 88.193  -3.469  -1.764  1.00 39.69 ? 1329 HOH B O   1 
HETATM 5773 O  O   . HOH G 6 .   ? 108.799 9.120   24.970  1.00 44.26 ? 1330 HOH B O   1 
HETATM 5774 O  O   . HOH G 6 .   ? 109.842 2.989   21.862  1.00 34.92 ? 1331 HOH B O   1 
HETATM 5775 O  O   . HOH G 6 .   ? 105.236 -2.193  26.125  1.00 45.57 ? 1332 HOH B O   1 
HETATM 5776 O  O   . HOH G 6 .   ? 65.917  0.610   -5.645  1.00 43.88 ? 1333 HOH B O   1 
HETATM 5777 O  O   . HOH G 6 .   ? 59.818  16.764  -2.948  1.00 36.35 ? 1334 HOH B O   1 
HETATM 5778 O  O   . HOH G 6 .   ? 78.353  20.366  10.663  1.00 28.27 ? 1335 HOH B O   1 
HETATM 5779 O  O   . HOH G 6 .   ? 83.446  20.202  6.524   1.00 35.31 ? 1336 HOH B O   1 
HETATM 5780 O  O   . HOH G 6 .   ? 63.660  27.768  2.785   1.00 37.85 ? 1337 HOH B O   1 
HETATM 5781 O  O   . HOH G 6 .   ? 62.215  25.570  2.888   1.00 38.59 ? 1338 HOH B O   1 
HETATM 5782 O  O   . HOH G 6 .   ? 86.561  27.183  4.506   1.00 41.39 ? 1339 HOH B O   1 
HETATM 5783 O  O   . HOH G 6 .   ? 84.435  18.077  1.372   1.00 38.51 ? 1340 HOH B O   1 
HETATM 5784 O  O   . HOH G 6 .   ? 51.323  9.805   4.360   1.00 37.44 ? 1341 HOH B O   1 
HETATM 5785 O  O   . HOH G 6 .   ? 57.780  8.741   -3.584  1.00 27.54 ? 1342 HOH B O   1 
HETATM 5786 O  O   . HOH G 6 .   ? 54.581  8.626   -1.591  1.00 32.37 ? 1343 HOH B O   1 
HETATM 5787 O  O   . HOH G 6 .   ? 86.493  -10.935 18.355  1.00 34.99 ? 1344 HOH B O   1 
HETATM 5788 O  O   . HOH G 6 .   ? 97.347  -12.915 11.635  1.00 44.92 ? 1345 HOH B O   1 
HETATM 5789 O  O   . HOH G 6 .   ? 98.226  -11.336 21.106  1.00 38.57 ? 1346 HOH B O   1 
HETATM 5790 O  O   . HOH G 6 .   ? 95.221  -14.604 18.860  1.00 40.14 ? 1347 HOH B O   1 
HETATM 5791 O  O   . HOH G 6 .   ? 93.544  -12.552 22.191  1.00 45.46 ? 1348 HOH B O   1 
HETATM 5792 O  O   . HOH G 6 .   ? 77.741  -10.132 19.892  1.00 43.20 ? 1349 HOH B O   1 
HETATM 5793 O  O   . HOH G 6 .   ? 81.492  -11.425 23.767  1.00 45.77 ? 1350 HOH B O   1 
HETATM 5794 O  O   . HOH G 6 .   ? 84.624  0.097   30.121  1.00 37.71 ? 1351 HOH B O   1 
HETATM 5795 O  O   . HOH G 6 .   ? 79.421  29.801  22.448  1.00 40.00 ? 1352 HOH B O   1 
HETATM 5796 O  O   . HOH G 6 .   ? 87.420  29.435  16.846  1.00 38.62 ? 1353 HOH B O   1 
HETATM 5797 O  O   . HOH G 6 .   ? 69.537  -0.695  30.464  1.00 29.32 ? 1354 HOH B O   1 
HETATM 5798 O  O   . HOH G 6 .   ? 96.493  17.628  26.386  1.00 45.32 ? 1355 HOH B O   1 
HETATM 5799 O  O   . HOH G 6 .   ? 106.955 17.602  17.581  1.00 40.59 ? 1356 HOH B O   1 
HETATM 5800 O  O   . HOH G 6 .   ? 101.919 6.117   10.307  1.00 24.40 ? 1357 HOH B O   1 
HETATM 5801 O  O   . HOH G 6 .   ? 94.534  15.609  33.165  1.00 36.21 ? 1358 HOH B O   1 
HETATM 5802 O  O   . HOH G 6 .   ? 58.894  24.849  4.243   1.00 39.98 ? 1359 HOH B O   1 
HETATM 5803 O  O   . HOH G 6 .   ? 65.918  32.509  21.504  1.00 40.34 ? 1360 HOH B O   1 
HETATM 5804 O  O   . HOH G 6 .   ? 64.799  -6.394  16.038  1.00 43.38 ? 1361 HOH B O   1 
HETATM 5805 O  O   . HOH G 6 .   ? 60.897  -6.175  12.734  1.00 39.38 ? 1362 HOH B O   1 
HETATM 5806 O  O   . HOH G 6 .   ? 59.887  -7.372  10.806  1.00 30.18 ? 1363 HOH B O   1 
HETATM 5807 O  O   . HOH G 6 .   ? 63.777  0.469   26.205  1.00 30.59 ? 1364 HOH B O   1 
HETATM 5808 O  O   . HOH G 6 .   ? 63.136  2.641   27.118  1.00 32.86 ? 1365 HOH B O   1 
HETATM 5809 O  O   . HOH G 6 .   ? 66.357  0.612   25.612  1.00 22.23 ? 1366 HOH B O   1 
HETATM 5810 O  O   . HOH G 6 .   ? 67.539  0.146   23.085  1.00 29.29 ? 1367 HOH B O   1 
HETATM 5811 O  O   . HOH G 6 .   ? 50.362  10.549  11.657  1.00 28.88 ? 1368 HOH B O   1 
HETATM 5812 O  O   . HOH G 6 .   ? 70.574  -6.579  10.420  1.00 33.65 ? 1369 HOH B O   1 
HETATM 5813 O  O   . HOH G 6 .   ? 72.282  -6.561  7.274   1.00 39.71 ? 1370 HOH B O   1 
HETATM 5814 O  O   . HOH G 6 .   ? 70.752  -3.962  10.849  1.00 31.70 ? 1371 HOH B O   1 
HETATM 5815 O  O   . HOH G 6 .   ? 68.483  -3.524  12.082  1.00 40.92 ? 1372 HOH B O   1 
HETATM 5816 O  O   . HOH G 6 .   ? 68.991  -10.459 8.714   1.00 40.90 ? 1373 HOH B O   1 
HETATM 5817 O  O   . HOH G 6 .   ? 80.402  -0.849  -9.247  1.00 35.39 ? 1374 HOH B O   1 
HETATM 5818 O  O   . HOH G 6 .   ? 91.510  -2.730  -0.008  0.50 14.76 ? 1375 HOH B O   1 
HETATM 5819 O  O   . HOH G 6 .   ? 103.738 -3.214  24.356  1.00 37.03 ? 1376 HOH B O   1 
HETATM 5820 O  O   . HOH G 6 .   ? 106.013 2.731   20.118  1.00 42.76 ? 1377 HOH B O   1 
HETATM 5821 O  O   . HOH G 6 .   ? 64.112  6.842   -7.034  1.00 38.47 ? 1378 HOH B O   1 
HETATM 5822 O  O   . HOH G 6 .   ? 72.177  7.078   -11.974 1.00 40.18 ? 1379 HOH B O   1 
HETATM 5823 O  O   . HOH G 6 .   ? 71.529  4.454   -10.005 1.00 42.30 ? 1380 HOH B O   1 
HETATM 5824 O  O   . HOH G 6 .   ? 62.659  25.612  0.396   1.00 47.32 ? 1381 HOH B O   1 
HETATM 5825 O  O   . HOH G 6 .   ? 74.994  32.219  15.089  1.00 36.79 ? 1382 HOH B O   1 
HETATM 5826 O  O   . HOH G 6 .   ? 86.437  25.292  7.584   1.00 48.64 ? 1383 HOH B O   1 
HETATM 5827 O  O   . HOH G 6 .   ? 73.650  33.087  2.040   1.00 38.93 ? 1384 HOH B O   1 
HETATM 5828 O  O   . HOH G 6 .   ? 70.228  21.790  -8.550  1.00 44.17 ? 1385 HOH B O   1 
HETATM 5829 O  O   . HOH G 6 .   ? 70.012  35.591  10.004  1.00 34.59 ? 1386 HOH B O   1 
HETATM 5830 O  O   . HOH G 6 .   ? 81.751  -9.122  9.059   1.00 52.10 ? 1387 HOH B O   1 
HETATM 5831 O  O   . HOH G 6 .   ? 86.828  -11.150 9.266   1.00 38.90 ? 1388 HOH B O   1 
HETATM 5832 O  O   . HOH G 6 .   ? 88.247  -6.409  6.686   1.00 45.42 ? 1389 HOH B O   1 
HETATM 5833 O  O   . HOH G 6 .   ? 96.580  -12.640 22.708  1.00 45.63 ? 1390 HOH B O   1 
HETATM 5834 O  O   . HOH G 6 .   ? 92.443  -7.535  24.445  1.00 39.36 ? 1391 HOH B O   1 
HETATM 5835 O  O   . HOH G 6 .   ? 78.627  -7.258  17.900  1.00 40.77 ? 1392 HOH B O   1 
HETATM 5836 O  O   . HOH G 6 .   ? 75.122  -4.711  20.978  1.00 38.43 ? 1393 HOH B O   1 
HETATM 5837 O  O   . HOH G 6 .   ? 88.785  -3.697  30.623  1.00 49.83 ? 1394 HOH B O   1 
HETATM 5838 O  O   . HOH G 6 .   ? 85.921  -1.756  29.262  1.00 32.89 ? 1395 HOH B O   1 
HETATM 5839 O  O   . HOH G 6 .   ? 82.158  -0.897  30.311  1.00 37.41 ? 1396 HOH B O   1 
HETATM 5840 O  O   . HOH G 6 .   ? 82.768  28.253  35.320  1.00 43.62 ? 1397 HOH B O   1 
HETATM 5841 O  O   . HOH G 6 .   ? 75.516  17.482  33.010  1.00 35.26 ? 1398 HOH B O   1 
HETATM 5842 O  O   . HOH G 6 .   ? 72.871  23.058  28.551  1.00 41.40 ? 1399 HOH B O   1 
HETATM 5843 O  O   . HOH G 6 .   ? 79.303  21.046  33.788  1.00 35.68 ? 1400 HOH B O   1 
HETATM 5844 O  O   . HOH G 6 .   ? 71.905  18.170  34.242  1.00 46.17 ? 1401 HOH B O   1 
HETATM 5845 O  O   . HOH G 6 .   ? 69.206  24.565  35.000  1.00 42.24 ? 1402 HOH B O   1 
HETATM 5846 O  O   . HOH G 6 .   ? 77.821  -4.766  29.125  1.00 41.58 ? 1403 HOH B O   1 
HETATM 5847 O  O   . HOH G 6 .   ? 76.771  -2.627  29.867  1.00 39.88 ? 1404 HOH B O   1 
HETATM 5848 O  O   . HOH G 6 .   ? 79.038  -1.706  30.797  1.00 39.55 ? 1405 HOH B O   1 
HETATM 5849 O  O   . HOH G 6 .   ? 72.643  -2.102  32.010  1.00 40.59 ? 1406 HOH B O   1 
HETATM 5850 O  O   . HOH G 6 .   ? 85.038  5.610   34.453  1.00 39.15 ? 1407 HOH B O   1 
HETATM 5851 O  O   . HOH G 6 .   ? 87.210  20.773  32.048  1.00 35.80 ? 1408 HOH B O   1 
HETATM 5852 O  O   . HOH G 6 .   ? 96.473  25.813  26.418  1.00 48.47 ? 1409 HOH B O   1 
HETATM 5853 O  O   . HOH G 6 .   ? 95.152  29.662  24.014  1.00 43.61 ? 1410 HOH B O   1 
HETATM 5854 O  O   . HOH G 6 .   ? 105.587 12.225  19.596  1.00 47.79 ? 1411 HOH B O   1 
HETATM 5855 O  O   . HOH G 6 .   ? 104.336 13.795  20.871  1.00 43.44 ? 1412 HOH B O   1 
HETATM 5856 O  O   . HOH G 6 .   ? 108.616 7.260   31.239  1.00 35.57 ? 1413 HOH B O   1 
HETATM 5857 O  O   . HOH G 6 .   ? 88.864  23.513  1.132   1.00 43.54 ? 1414 HOH B O   1 
HETATM 5858 O  O   . HOH G 6 .   ? 52.209  6.673   11.295  1.00 35.54 ? 1415 HOH B O   1 
HETATM 5859 O  O   . HOH G 6 .   ? 61.514  8.733   30.557  1.00 34.97 ? 1416 HOH B O   1 
HETATM 5860 O  O   . HOH G 6 .   ? 55.611  -1.377  9.842   1.00 41.17 ? 1417 HOH B O   1 
HETATM 5861 O  O   . HOH G 6 .   ? 60.477  3.133   26.293  1.00 36.49 ? 1418 HOH B O   1 
HETATM 5862 O  O   . HOH G 6 .   ? 55.426  1.623   4.487   1.00 36.30 ? 1419 HOH B O   1 
HETATM 5863 O  O   . HOH G 6 .   ? 59.753  -7.073  2.715   1.00 42.77 ? 1420 HOH B O   1 
HETATM 5864 O  O   . HOH G 6 .   ? 73.031  -9.447  -5.941  1.00 45.53 ? 1421 HOH B O   1 
HETATM 5865 O  O   . HOH G 6 .   ? 74.535  1.149   -7.707  1.00 44.84 ? 1422 HOH B O   1 
HETATM 5866 O  O   . HOH G 6 .   ? 75.686  -3.798  -7.490  1.00 39.71 ? 1423 HOH B O   1 
HETATM 5867 O  O   . HOH G 6 .   ? 92.512  0.349   1.960   1.00 23.87 ? 1424 HOH B O   1 
HETATM 5868 O  O   . HOH G 6 .   ? 109.378 5.103   15.243  1.00 41.04 ? 1425 HOH B O   1 
HETATM 5869 O  O   . HOH G 6 .   ? 78.703  18.591  8.066   1.00 26.78 ? 1426 HOH B O   1 
HETATM 5870 O  O   . HOH G 6 .   ? 62.154  19.691  -6.107  1.00 52.43 ? 1427 HOH B O   1 
HETATM 5871 O  O   . HOH G 6 .   ? 71.384  2.064   -7.961  1.00 47.97 ? 1428 HOH B O   1 
HETATM 5872 O  O   . HOH G 6 .   ? 68.889  14.105  -10.866 1.00 45.48 ? 1429 HOH B O   1 
HETATM 5873 O  O   . HOH G 6 .   ? 85.546  28.343  8.747   1.00 45.01 ? 1430 HOH B O   1 
HETATM 5874 O  O   . HOH G 6 .   ? 78.688  28.251  -5.749  1.00 49.01 ? 1431 HOH B O   1 
HETATM 5875 O  O   . HOH G 6 .   ? 72.829  24.673  -7.659  1.00 47.11 ? 1432 HOH B O   1 
HETATM 5876 O  O   . HOH G 6 .   ? 70.425  17.365  -7.769  1.00 31.62 ? 1433 HOH B O   1 
HETATM 5877 O  O   . HOH G 6 .   ? 76.793  30.956  -1.892  1.00 42.87 ? 1434 HOH B O   1 
HETATM 5878 O  O   . HOH G 6 .   ? 73.302  31.080  -2.257  1.00 40.03 ? 1435 HOH B O   1 
HETATM 5879 O  O   . HOH G 6 .   ? 65.823  32.524  4.143   1.00 50.23 ? 1436 HOH B O   1 
HETATM 5880 O  O   . HOH G 6 .   ? 79.795  24.900  11.850  1.00 34.04 ? 1437 HOH B O   1 
HETATM 5881 O  O   . HOH G 6 .   ? 56.497  18.493  -2.481  1.00 46.44 ? 1438 HOH B O   1 
HETATM 5882 O  O   . HOH G 6 .   ? 70.690  -1.225  20.106  1.00 41.06 ? 1439 HOH B O   1 
HETATM 5883 O  O   . HOH G 6 .   ? 74.565  -2.815  17.416  1.00 41.22 ? 1440 HOH B O   1 
HETATM 5884 O  O   . HOH G 6 .   ? 101.282 -4.132  21.028  1.00 40.00 ? 1441 HOH B O   1 
HETATM 5885 O  O   . HOH G 6 .   ? 88.096  -0.545  29.431  1.00 45.92 ? 1442 HOH B O   1 
HETATM 5886 O  O   . HOH G 6 .   ? 73.425  -7.864  22.471  1.00 43.82 ? 1443 HOH B O   1 
HETATM 5887 O  O   . HOH G 6 .   ? 90.874  30.228  24.738  1.00 48.14 ? 1444 HOH B O   1 
HETATM 5888 O  O   . HOH G 6 .   ? 80.390  25.635  32.169  1.00 42.73 ? 1445 HOH B O   1 
HETATM 5889 O  O   . HOH G 6 .   ? 84.218  23.649  34.520  1.00 46.35 ? 1446 HOH B O   1 
HETATM 5890 O  O   . HOH G 6 .   ? 83.607  32.444  31.900  1.00 45.24 ? 1447 HOH B O   1 
HETATM 5891 O  O   . HOH G 6 .   ? 78.813  29.843  19.740  1.00 42.27 ? 1448 HOH B O   1 
HETATM 5892 O  O   . HOH G 6 .   ? 69.272  14.366  33.219  1.00 38.22 ? 1449 HOH B O   1 
HETATM 5893 O  O   . HOH G 6 .   ? 70.948  29.931  20.009  1.00 42.10 ? 1450 HOH B O   1 
HETATM 5894 O  O   . HOH G 6 .   ? 78.807  -0.751  32.972  1.00 40.08 ? 1451 HOH B O   1 
HETATM 5895 O  O   . HOH G 6 .   ? 99.659  26.292  19.004  1.00 53.98 ? 1452 HOH B O   1 
HETATM 5896 O  O   . HOH G 6 .   ? 92.823  16.673  31.294  1.00 43.03 ? 1453 HOH B O   1 
HETATM 5897 O  O   . HOH G 6 .   ? 104.307 18.737  17.233  1.00 45.44 ? 1454 HOH B O   1 
HETATM 5898 O  O   . HOH G 6 .   ? 108.128 11.615  25.594  1.00 49.70 ? 1455 HOH B O   1 
HETATM 5899 O  O   . HOH G 6 .   ? 61.906  13.148  33.187  1.00 39.16 ? 1456 HOH B O   1 
HETATM 5900 O  O   . HOH G 6 .   ? 65.887  4.163   31.723  1.00 37.51 ? 1457 HOH B O   1 
HETATM 5901 O  O   . HOH G 6 .   ? 68.087  8.248   31.849  1.00 19.09 ? 1458 HOH B O   1 
HETATM 5902 O  O   . HOH G 6 .   ? 62.771  11.713  30.868  1.00 29.86 ? 1459 HOH B O   1 
HETATM 5903 O  O   . HOH G 6 .   ? 58.406  -4.165  4.765   1.00 40.43 ? 1460 HOH B O   1 
HETATM 5904 O  O   . HOH G 6 .   ? 58.797  -1.697  3.406   1.00 41.33 ? 1461 HOH B O   1 
HETATM 5905 O  O   . HOH G 6 .   ? 61.608  -8.800  8.248   1.00 43.55 ? 1462 HOH B O   1 
HETATM 5906 O  O   . HOH G 6 .   ? 59.821  -5.458  0.791   1.00 41.92 ? 1463 HOH B O   1 
HETATM 5907 O  O   . HOH G 6 .   ? 63.311  -8.534  -2.230  1.00 47.98 ? 1464 HOH B O   1 
HETATM 5908 O  O   . HOH G 6 .   ? 65.978  -6.045  -4.014  1.00 40.70 ? 1465 HOH B O   1 
HETATM 5909 O  O   . HOH G 6 .   ? 66.157  -9.731  -3.030  1.00 42.32 ? 1466 HOH B O   1 
HETATM 5910 O  O   . HOH G 6 .   ? 67.073  -2.763  -6.341  1.00 43.89 ? 1467 HOH B O   1 
HETATM 5911 O  O   . HOH G 6 .   ? 66.944  -0.035  -7.891  1.00 43.51 ? 1468 HOH B O   1 
HETATM 5912 O  O   . HOH G 6 .   ? 68.865  0.738   -5.853  1.00 34.76 ? 1469 HOH B O   1 
HETATM 5913 O  O   . HOH G 6 .   ? 80.761  -8.049  1.052   1.00 39.55 ? 1470 HOH B O   1 
HETATM 5914 O  O   . HOH G 6 .   ? 78.210  -3.307  4.822   1.00 46.10 ? 1471 HOH B O   1 
HETATM 5915 O  O   . HOH G 6 .   ? 63.324  11.607  -11.323 1.00 44.08 ? 1472 HOH B O   1 
HETATM 5916 O  O   . HOH G 6 .   ? 65.081  8.328   -8.935  1.00 43.14 ? 1473 HOH B O   1 
HETATM 5917 O  O   . HOH G 6 .   ? 66.454  8.181   -11.151 1.00 35.76 ? 1474 HOH B O   1 
HETATM 5918 O  O   . HOH G 6 .   ? 63.049  21.828  -4.966  1.00 47.34 ? 1475 HOH B O   1 
HETATM 5919 O  O   . HOH G 6 .   ? 66.876  19.577  -9.106  1.00 50.09 ? 1476 HOH B O   1 
HETATM 5920 O  O   . HOH G 6 .   ? 69.237  -2.848  14.263  1.00 40.00 ? 1477 HOH B O   1 
HETATM 5921 O  O   . HOH G 6 .   ? 88.286  -13.970 12.433  1.00 42.05 ? 1478 HOH B O   1 
HETATM 5922 O  O   . HOH G 6 .   ? 87.214  -13.815 15.545  1.00 36.47 ? 1479 HOH B O   1 
HETATM 5923 O  O   . HOH G 6 .   ? 90.791  -15.114 12.705  1.00 45.13 ? 1480 HOH B O   1 
HETATM 5924 O  O   . HOH G 6 .   ? 91.157  -17.304 15.014  1.00 50.08 ? 1481 HOH B O   1 
HETATM 5925 O  O   . HOH G 6 .   ? 102.824 -5.400  19.777  1.00 46.76 ? 1482 HOH B O   1 
HETATM 5926 O  O   . HOH G 6 .   ? 98.815  -5.637  23.090  1.00 41.14 ? 1483 HOH B O   1 
HETATM 5927 O  O   . HOH G 6 .   ? 91.576  -6.862  29.186  1.00 46.57 ? 1484 HOH B O   1 
HETATM 5928 O  O   . HOH G 6 .   ? 90.085  29.834  27.144  1.00 42.46 ? 1485 HOH B O   1 
HETATM 5929 O  O   . HOH G 6 .   ? 83.443  21.079  34.798  1.00 47.63 ? 1486 HOH B O   1 
HETATM 5930 O  O   . HOH G 6 .   ? 100.302 -2.980  10.320  1.00 27.53 ? 1487 HOH B O   1 
HETATM 5931 O  O   . HOH G 6 .   ? 77.787  -7.977  29.862  1.00 48.78 ? 1488 HOH B O   1 
HETATM 5932 O  O   . HOH G 6 .   ? 87.018  -5.595  31.590  1.00 48.82 ? 1489 HOH B O   1 
HETATM 5933 O  O   . HOH G 6 .   ? 84.852  28.017  37.015  1.00 48.75 ? 1490 HOH B O   1 
HETATM 5934 O  O   . HOH G 6 .   ? 84.337  27.443  11.883  1.00 47.32 ? 1491 HOH B O   1 
HETATM 5935 O  O   . HOH G 6 .   ? 103.623 18.864  21.166  1.00 41.12 ? 1492 HOH B O   1 
HETATM 5936 O  O   . HOH G 6 .   ? 103.238 18.088  23.765  1.00 44.88 ? 1493 HOH B O   1 
HETATM 5937 O  O   . HOH G 6 .   ? 63.104  4.880   30.580  1.00 43.00 ? 1494 HOH B O   1 
HETATM 5938 O  O   . HOH G 6 .   ? 65.726  -13.659 6.351   1.00 46.99 ? 1495 HOH B O   1 
HETATM 5939 O  O   . HOH G 6 .   ? 67.758  -12.378 5.143   1.00 51.78 ? 1496 HOH B O   1 
HETATM 5940 O  O   . HOH G 6 .   ? 64.570  -10.705 1.544   1.00 48.03 ? 1497 HOH B O   1 
HETATM 5941 O  O   . HOH G 6 .   ? 77.354  -7.091  -6.460  1.00 46.24 ? 1498 HOH B O   1 
HETATM 5942 O  O   . HOH G 6 .   ? 90.676  3.412   1.031   1.00 31.80 ? 1499 HOH B O   1 
HETATM 5943 O  O   . HOH G 6 .   ? 74.649  36.006  5.479   1.00 45.65 ? 1500 HOH B O   1 
HETATM 5944 O  O   . HOH G 6 .   ? 69.562  33.119  17.875  1.00 45.24 ? 1501 HOH B O   1 
HETATM 5945 O  O   . HOH G 6 .   ? 83.018  -10.716 14.588  1.00 46.09 ? 1502 HOH B O   1 
HETATM 5946 O  O   . HOH G 6 .   ? 81.703  -11.244 10.688  1.00 48.77 ? 1503 HOH B O   1 
HETATM 5947 O  O   . HOH G 6 .   ? 90.290  -14.542 16.217  1.00 48.30 ? 1504 HOH B O   1 
HETATM 5948 O  O   . HOH G 6 .   ? 88.686  -18.244 13.583  1.00 46.73 ? 1505 HOH B O   1 
HETATM 5949 O  O   . HOH G 6 .   ? 73.265  -3.377  29.670  1.00 44.40 ? 1506 HOH B O   1 
HETATM 5950 O  O   . HOH G 6 .   ? 88.212  -11.696 20.117  1.00 45.84 ? 1507 HOH B O   1 
HETATM 5951 O  O   . HOH G 6 .   ? 86.132  31.284  32.411  1.00 40.07 ? 1508 HOH B O   1 
HETATM 5952 O  O   . HOH G 6 .   ? 88.266  30.049  32.010  1.00 48.62 ? 1509 HOH B O   1 
HETATM 5953 O  O   . HOH G 6 .   ? 79.486  31.519  27.660  1.00 45.94 ? 1510 HOH B O   1 
HETATM 5954 O  O   . HOH G 6 .   ? 78.926  35.260  27.434  1.00 45.35 ? 1511 HOH B O   1 
HETATM 5955 O  O   . HOH G 6 .   ? 80.289  33.622  25.949  1.00 45.74 ? 1512 HOH B O   1 
HETATM 5956 O  O   . HOH G 6 .   ? 78.671  31.515  24.840  1.00 51.59 ? 1513 HOH B O   1 
HETATM 5957 O  O   . HOH G 6 .   ? 81.648  31.190  21.531  1.00 43.18 ? 1514 HOH B O   1 
HETATM 5958 O  O   . HOH G 6 .   ? 71.506  10.202  33.503  1.00 22.91 ? 1515 HOH B O   1 
HETATM 5959 O  O   . HOH G 6 .   ? 101.829 22.665  22.139  1.00 48.49 ? 1516 HOH B O   1 
HETATM 5960 O  O   . HOH G 6 .   ? 104.720 16.532  19.313  1.00 40.76 ? 1517 HOH B O   1 
HETATM 5961 O  O   . HOH G 6 .   ? 88.231  27.640  6.563   1.00 48.35 ? 1518 HOH B O   1 
HETATM 5962 O  O   . HOH G 6 .   ? 96.160  -2.250  29.693  1.00 43.33 ? 1519 HOH B O   1 
HETATM 5963 O  O   . HOH G 6 .   ? 91.639  30.367  12.462  1.00 41.17 ? 1520 HOH B O   1 
HETATM 5964 O  O   . HOH G 6 .   ? 85.937  13.373  -5.072  1.00 17.99 ? 1521 HOH B O   1 
HETATM 5965 O  O   . HOH G 6 .   ? 107.622 0.078   33.418  1.00 40.07 ? 1522 HOH B O   1 
HETATM 5966 O  O   . HOH G 6 .   ? 77.787  27.152  16.999  1.00 30.40 ? 1523 HOH B O   1 
HETATM 5967 O  O   . HOH G 6 .   ? 79.993  28.625  17.032  1.00 33.91 ? 1524 HOH B O   1 
HETATM 5968 O  O   . HOH G 6 .   ? 73.993  14.755  32.860  1.00 40.15 ? 1525 HOH B O   1 
HETATM 5969 O  O   . HOH G 6 .   ? 103.339 -5.840  15.788  1.00 44.84 ? 1526 HOH B O   1 
HETATM 5970 O  O   . HOH G 6 .   ? 69.989  24.718  -8.301  1.00 42.28 ? 1527 HOH B O   1 
HETATM 5971 O  O   . HOH G 6 .   ? 68.636  22.161  36.216  1.00 42.24 ? 1528 HOH B O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   GLU 2   2   2   GLU ALA A . n 
A 1 3   ARG 3   3   3   ARG ARG A . n 
A 1 4   TYR 4   4   4   TYR TYR A . n 
A 1 5   GLU 5   5   5   GLU GLU A . n 
A 1 6   ASN 6   6   6   ASN ASN A . n 
A 1 7   LEU 7   7   7   LEU LEU A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   ALA 9   9   9   ALA ALA A . n 
A 1 10  GLN 10  10  10  GLN GLN A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  ASN 12  12  12  ASN ASN A . n 
A 1 13  ASP 13  13  13  ASP ASP A . n 
A 1 14  ARG 14  14  14  ARG ARG A . n 
A 1 15  ARG 15  15  15  ARG ALA A . n 
A 1 16  GLU 16  16  16  GLU GLU A . n 
A 1 17  GLY 17  17  17  GLY GLY A . n 
A 1 18  ALA 18  18  18  ALA ALA A . n 
A 1 19  PHE 19  19  19  PHE PHE A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  PHE 22  22  22  PHE PHE A . n 
A 1 23  VAL 23  23  23  VAL VAL A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  ASP 27  27  27  ASP ASP A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  ILE 30  30  30  ILE ILE A . n 
A 1 31  GLU 31  31  31  GLU GLU A . n 
A 1 32  GLN 32  32  32  GLN GLN A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  ILE 37  37  37  ILE ILE A . n 
A 1 38  ASP 38  38  38  ASP ASP A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  LEU 40  40  40  LEU LEU A . n 
A 1 41  ILE 41  41  41  ILE ILE A . n 
A 1 42  ASP 42  42  42  ASP ASP A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  ALA 45  45  45  ALA ALA A . n 
A 1 46  ASP 46  46  46  ASP ASP A . n 
A 1 47  ALA 47  47  47  ALA ALA A . n 
A 1 48  LEU 48  48  48  LEU LEU A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  VAL 52  52  52  VAL VAL A . n 
A 1 53  PRO 53  53  53  PRO PRO A . n 
A 1 54  PHE 54  54  54  PHE PHE A . n 
A 1 55  SER 55  55  55  SER SER A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  PRO 57  57  57  PRO PRO A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  ASP 60  60  60  ASP ASP A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  ILE 64  64  64  ILE ILE A . n 
A 1 65  GLN 65  65  65  GLN GLN A . n 
A 1 66  ASN 66  66  66  ASN ASN A . n 
A 1 67  ALA 67  67  67  ALA ALA A . n 
A 1 68  ASN 68  68  68  ASN ASN A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  ARG 70  70  70  ARG ARG A . n 
A 1 71  ALA 71  71  71  ALA ALA A . n 
A 1 72  PHE 72  72  72  PHE PHE A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  GLY 75  75  75  GLY GLY A . n 
A 1 76  VAL 76  76  76  VAL VAL A . n 
A 1 77  THR 77  77  77  THR THR A . n 
A 1 78  PRO 78  78  78  PRO PRO A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  GLN 80  80  80  GLN GLN A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  PHE 82  82  82  PHE PHE A . n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  MET 84  84  84  MET MET A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  ALA 86  86  86  ALA ALA A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  ILE 88  88  88  ILE ILE A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  GLU 90  90  90  GLU GLU A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  HIS 92  92  92  HIS HIS A . n 
A 1 93  PRO 93  93  93  PRO PRO A . n 
A 1 94  THR 94  94  94  THR THR A . n 
A 1 95  ILE 95  95  95  ILE ILE A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  ILE 97  97  97  ILE ILE A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 MET 101 101 101 MET MET A . n 
A 1 102 TYR 102 102 102 TYR TYR A . n 
A 1 103 ALA 103 103 103 ALA ALA A . n 
A 1 104 ASN 104 104 104 ASN ASN A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 VAL 106 106 106 VAL VAL A . n 
A 1 107 PHE 107 107 107 PHE PHE A . n 
A 1 108 ASN 108 108 108 ASN ASN A . n 
A 1 109 ASN 109 109 109 ASN ASN A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 ILE 111 111 111 ILE ILE A . n 
A 1 112 ASP 112 112 112 ASP ASP A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 PHE 114 114 114 PHE PHE A . n 
A 1 115 TYR 115 115 115 TYR TYR A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 ARG 117 117 117 ARG ARG A . n 
A 1 118 CYS 118 118 118 CYS CYS A . n 
A 1 119 GLU 119 119 119 GLU GLU A . n 
A 1 120 GLN 120 120 120 GLN GLN A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 GLY 122 122 122 GLY GLY A . n 
A 1 123 VAL 123 123 123 VAL VAL A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 SER 125 125 125 SER SER A . n 
A 1 126 VAL 126 126 126 VAL VAL A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 VAL 128 128 128 VAL VAL A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 ASP 130 130 130 ASP ASP A . n 
A 1 131 VAL 131 131 131 VAL VAL A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 VAL 133 133 133 VAL VAL A . n 
A 1 134 GLU 134 134 134 GLU GLU A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 SER 136 136 136 SER SER A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 PRO 138 138 138 PRO PRO A . n 
A 1 139 PHE 139 139 139 PHE PHE A . n 
A 1 140 ARG 140 140 140 ARG ARG A . n 
A 1 141 GLN 141 141 141 GLN GLN A . n 
A 1 142 ALA 142 142 142 ALA ALA A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ARG 145 145 145 ARG ARG A . n 
A 1 146 HIS 146 146 146 HIS HIS A . n 
A 1 147 ASN 147 147 147 ASN ASN A . n 
A 1 148 ILE 148 148 148 ILE ILE A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 PRO 150 150 150 PRO PRO A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 PHE 152 152 152 PHE PHE A . n 
A 1 153 ILE 153 153 153 ILE ILE A . n 
A 1 154 CYS 154 154 154 CYS CYS A . n 
A 1 155 PRO 155 155 155 PRO PRO A . n 
A 1 156 PRO 156 156 156 PRO PRO A . n 
A 1 157 ASN 157 157 157 ASN ASN A . n 
A 1 158 ALA 158 158 158 ALA ALA A . n 
A 1 159 ASP 159 159 159 ASP ASP A . n 
A 1 160 ASP 160 160 160 ASP ASP A . n 
A 1 161 ASP 161 161 161 ASP ASP A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 ARG 164 164 164 ARG ARG A . n 
A 1 165 GLN 165 165 165 GLN GLN A . n 
A 1 166 VAL 166 166 166 VAL VAL A . n 
A 1 167 ALA 167 167 167 ALA ALA A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 TYR 169 169 169 TYR TYR A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 ARG 171 171 171 ARG ARG A . n 
A 1 172 GLY 172 172 172 GLY GLY A . n 
A 1 173 TYR 173 173 173 TYR TYR A . n 
A 1 174 THR 174 174 174 THR THR A . n 
A 1 175 TYR 175 175 175 TYR TYR A . n 
A 1 176 LEU 176 176 176 LEU LEU A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 SER 178 178 178 SER SER A . n 
A 1 179 ARG 179 179 179 ARG ARG A . n 
A 1 180 SER 180 180 180 SER SER A . n 
A 1 181 GLY 181 181 181 GLY GLY A . n 
A 1 182 VAL 182 182 182 VAL VAL A . n 
A 1 183 THR 183 183 183 THR THR A . n 
A 1 184 GLY 184 184 184 GLY GLY A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 ASN 187 187 187 ASN ASN A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 GLY 189 189 189 GLY GLY A . n 
A 1 190 ALA 190 190 190 ALA ALA A . n 
A 1 191 LEU 191 191 191 LEU ALA A . n 
A 1 192 PRO 192 192 192 PRO PRO A . n 
A 1 193 LEU 193 193 193 LEU LEU A . n 
A 1 194 HIS 194 194 194 HIS HIS A . n 
A 1 195 HIS 195 195 195 HIS HIS A . n 
A 1 196 LEU 196 196 196 LEU LEU A . n 
A 1 197 ILE 197 197 197 ILE ILE A . n 
A 1 198 GLU 198 198 198 GLU ALA A . n 
A 1 199 LYS 199 199 199 LYS LYS A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 LYS 201 201 201 LYS LYS A . n 
A 1 202 GLU 202 202 202 GLU GLU A . n 
A 1 203 TYR 203 203 203 TYR TYR A . n 
A 1 204 HIS 204 204 204 HIS HIS A . n 
A 1 205 ALA 205 205 205 ALA ALA A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 PRO 207 207 207 PRO PRO A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 LEU 209 209 209 LEU LEU A . n 
A 1 210 GLN 210 210 210 GLN GLN A . n 
A 1 211 GLY 211 211 211 GLY GLY A . n 
A 1 212 PHE 212 212 212 PHE PHE A . n 
A 1 213 GLY 213 213 213 GLY GLY A . n 
A 1 214 ILE 214 214 214 ILE ILE A . n 
A 1 215 SER 215 215 215 SER SER A . n 
A 1 216 SER 216 216 216 SER SER A . n 
A 1 217 PRO 217 217 217 PRO PRO A . n 
A 1 218 GLU 218 218 218 GLU GLU A . n 
A 1 219 GLN 219 219 219 GLN GLN A . n 
A 1 220 VAL 220 220 220 VAL VAL A . n 
A 1 221 SER 221 221 221 SER SER A . n 
A 1 222 ALA 222 222 222 ALA ALA A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 VAL 224 224 224 VAL VAL A . n 
A 1 225 ARG 225 225 225 ARG ARG A . n 
A 1 226 ALA 226 226 226 ALA ALA A . n 
A 1 227 GLY 227 227 227 GLY GLY A . n 
A 1 228 ALA 228 228 228 ALA ALA A . n 
A 1 229 ALA 229 229 229 ALA ALA A . n 
A 1 230 GLY 230 230 230 GLY GLY A . n 
A 1 231 ALA 231 231 231 ALA ALA A . n 
A 1 232 ILE 232 232 232 ILE ILE A . n 
A 1 233 SER 233 233 233 SER SER A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 SER 235 235 235 SER SER A . n 
A 1 236 ALA 236 236 236 ALA ALA A . n 
A 1 237 ILE 237 237 237 ILE ILE A . n 
A 1 238 VAL 238 238 238 VAL VAL A . n 
A 1 239 LYS 239 239 239 LYS LYS A . n 
A 1 240 ILE 240 240 240 ILE ILE A . n 
A 1 241 ILE 241 241 241 ILE ILE A . n 
A 1 242 GLU 242 242 242 GLU GLU A . n 
A 1 243 LYS 243 243 243 LYS ALA A . n 
A 1 244 ASN 244 244 244 ASN ASN A . n 
A 1 245 LEU 245 245 245 LEU LEU A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 SER 247 247 247 SER SER A . n 
A 1 248 PRO 248 248 248 PRO PRO A . n 
A 1 249 LYS 249 249 249 LYS ALA A . n 
A 1 250 GLN 250 250 250 GLN GLN A . n 
A 1 251 MET 251 251 251 MET MET A . n 
A 1 252 LEU 252 252 252 LEU LEU A . n 
A 1 253 ALA 253 253 253 ALA ALA A . n 
A 1 254 GLU 254 254 254 GLU GLU A . n 
A 1 255 LEU 255 255 255 LEU LEU A . n 
A 1 256 ARG 256 256 256 ARG ARG A . n 
A 1 257 SER 257 257 257 SER SER A . n 
A 1 258 PHE 258 258 258 PHE PHE A . n 
A 1 259 VAL 259 259 259 VAL VAL A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 ALA 261 261 261 ALA ALA A . n 
A 1 262 MET 262 262 262 MET MET A . n 
A 1 263 LYS 263 263 263 LYS LYS A . n 
A 1 264 ALA 264 264 264 ALA ALA A . n 
A 1 265 ALA 265 265 265 ALA ALA A . n 
A 1 266 SER 266 266 266 SER SER A . n 
A 1 267 ARG 267 267 267 ARG ARG A . n 
A 1 268 ALA 268 268 ?   ?   ?   A . n 
B 2 1   THR 1   2   2   THR THR B . n 
B 2 2   THR 2   3   3   THR THR B . n 
B 2 3   LEU 3   4   4   LEU LEU B . n 
B 2 4   LEU 4   5   5   LEU LEU B . n 
B 2 5   ASN 5   6   6   ASN ASN B . n 
B 2 6   PRO 6   7   7   PRO PRO B . n 
B 2 7   TYR 7   8   8   TYR TYR B . n 
B 2 8   PHE 8   9   9   PHE PHE B . n 
B 2 9   GLY 9   10  10  GLY GLY B . n 
B 2 10  GLU 10  11  11  GLU GLU B . n 
B 2 11  PHE 11  12  12  PHE PHE B . n 
B 2 12  GLY 12  13  13  GLY GLY B . n 
B 2 13  GLY 13  14  14  GLY GLY B . n 
B 2 14  MET 14  15  15  MET MET B . n 
B 2 15  TYR 15  16  16  TYR TYR B . n 
B 2 16  VAL 16  17  17  VAL VAL B . n 
B 2 17  PRO 17  18  18  PRO PRO B . n 
B 2 18  GLN 18  19  19  GLN GLN B . n 
B 2 19  ILE 19  20  20  ILE ILE B . n 
B 2 20  LEU 20  21  21  LEU LEU B . n 
B 2 21  MET 21  22  22  MET MET B . n 
B 2 22  PRO 22  23  23  PRO PRO B . n 
B 2 23  ALA 23  24  24  ALA ALA B . n 
B 2 24  LEU 24  25  25  LEU LEU B . n 
B 2 25  ASN 25  26  26  ASN ASN B . n 
B 2 26  GLN 26  27  27  GLN GLN B . n 
B 2 27  LEU 27  28  28  LEU LEU B . n 
B 2 28  GLU 28  29  29  GLU GLU B . n 
B 2 29  GLU 29  30  30  GLU GLU B . n 
B 2 30  ALA 30  31  31  ALA ALA B . n 
B 2 31  PHE 31  32  32  PHE PHE B . n 
B 2 32  VAL 32  33  33  VAL VAL B . n 
B 2 33  SER 33  34  34  SER SER B . n 
B 2 34  ALA 34  35  35  ALA ALA B . n 
B 2 35  GLN 35  36  36  GLN GLN B . n 
B 2 36  LYS 36  37  37  LYS LYS B . n 
B 2 37  ASP 37  38  38  ASP ASP B . n 
B 2 38  PRO 38  39  39  PRO PRO B . n 
B 2 39  GLU 39  40  40  GLU GLU B . n 
B 2 40  PHE 40  41  41  PHE PHE B . n 
B 2 41  GLN 41  42  42  GLN GLN B . n 
B 2 42  ALA 42  43  43  ALA ALA B . n 
B 2 43  GLN 43  44  44  GLN GLN B . n 
B 2 44  PHE 44  45  45  PHE PHE B . n 
B 2 45  ALA 45  46  46  ALA ALA B . n 
B 2 46  ASP 46  47  47  ASP ASP B . n 
B 2 47  LEU 47  48  48  LEU LEU B . n 
B 2 48  LEU 48  49  49  LEU LEU B . n 
B 2 49  LYS 49  50  50  LYS LYS B . n 
B 2 50  ASN 50  51  51  ASN ASN B . n 
B 2 51  TYR 51  52  52  TYR TYR B . n 
B 2 52  ALA 52  53  53  ALA ALA B . n 
B 2 53  GLY 53  54  54  GLY GLY B . n 
B 2 54  ARG 54  55  55  ARG ARG B . n 
B 2 55  PRO 55  56  56  PRO PRO B . n 
B 2 56  THR 56  57  57  THR THR B . n 
B 2 57  ALA 57  58  58  ALA ALA B . n 
B 2 58  LEU 58  59  59  LEU LEU B . n 
B 2 59  THR 59  60  60  THR THR B . n 
B 2 60  LYS 60  61  61  LYS LYS B . n 
B 2 61  CYS 61  62  62  CYS CYS B . n 
B 2 62  GLN 62  63  63  GLN ALA B . n 
B 2 63  ASN 63  64  64  ASN ASN B . n 
B 2 64  ILE 64  65  65  ILE ILE B . n 
B 2 65  THR 65  66  66  THR THR B . n 
B 2 66  ALA 66  67  67  ALA ALA B . n 
B 2 67  GLY 67  68  68  GLY GLY B . n 
B 2 68  THR 68  69  69  THR THR B . n 
B 2 69  ARG 69  70  70  ARG ARG B . n 
B 2 70  THR 70  71  71  THR THR B . n 
B 2 71  THR 71  72  72  THR THR B . n 
B 2 72  LEU 72  73  73  LEU LEU B . n 
B 2 73  TYR 73  74  74  TYR TYR B . n 
B 2 74  LEU 74  75  75  LEU LEU B . n 
B 2 75  LYS 75  76  76  LYS LYS B . n 
B 2 76  ARG 76  77  77  ARG ARG B . n 
B 2 77  GLU 77  78  78  GLU GLU B . n 
B 2 78  ASP 78  79  79  ASP ASP B . n 
B 2 79  LEU 79  80  80  LEU LEU B . n 
B 2 80  LEU 80  81  81  LEU LEU B . n 
B 2 81  HIS 81  82  82  HIS HIS B . n 
B 2 82  GLY 82  83  83  GLY GLY B . n 
B 2 83  GLY 83  84  84  GLY GLY B . n 
B 2 84  ALA 84  85  85  ALA ALA B . n 
B 2 85  HIS 85  86  86  HIS HIS B . n 
B 2 86  LYS 86  87  87  LYS LYS B . n 
B 2 87  THR 87  88  88  THR THR B . n 
B 2 88  ASN 88  89  89  ASN ASN B . n 
B 2 89  GLN 89  90  90  GLN GLN B . n 
B 2 90  VAL 90  91  91  VAL VAL B . n 
B 2 91  LEU 91  92  92  LEU LEU B . n 
B 2 92  GLY 92  93  93  GLY GLY B . n 
B 2 93  GLN 93  94  94  GLN GLN B . n 
B 2 94  ALA 94  95  95  ALA ALA B . n 
B 2 95  LEU 95  96  96  LEU LEU B . n 
B 2 96  LEU 96  97  97  LEU LEU B . n 
B 2 97  ALA 97  98  98  ALA ALA B . n 
B 2 98  LYS 98  99  99  LYS LYS B . n 
B 2 99  ARG 99  100 100 ARG ARG B . n 
B 2 100 MET 100 101 101 MET MET B . n 
B 2 101 GLY 101 102 102 GLY GLY B . n 
B 2 102 LYS 102 103 103 LYS LYS B . n 
B 2 103 SER 103 104 104 SER SER B . n 
B 2 104 GLU 104 105 105 GLU GLU B . n 
B 2 105 ILE 105 106 106 ILE ILE B . n 
B 2 106 ILE 106 107 107 ILE ILE B . n 
B 2 107 ALA 107 108 108 ALA ALA B . n 
B 2 108 GLU 108 109 109 GLU GLU B . n 
B 2 109 THR 109 110 110 THR THR B . n 
B 2 110 GLY 110 111 111 GLY GLY B . n 
B 2 111 ALA 111 112 112 ALA ALA B . n 
B 2 112 GLY 112 113 113 GLY GLY B . n 
B 2 113 GLN 113 114 114 GLN GLN B . n 
B 2 114 HIS 114 115 115 HIS HIS B . n 
B 2 115 GLY 115 116 116 GLY GLY B . n 
B 2 116 VAL 116 117 117 VAL VAL B . n 
B 2 117 ALA 117 118 118 ALA ALA B . n 
B 2 118 SER 118 119 119 SER SER B . n 
B 2 119 ALA 119 120 120 ALA ALA B . n 
B 2 120 LEU 120 121 121 LEU LEU B . n 
B 2 121 ALA 121 122 122 ALA ALA B . n 
B 2 122 SER 122 123 123 SER SER B . n 
B 2 123 ALA 123 124 124 ALA ALA B . n 
B 2 124 LEU 124 125 125 LEU LEU B . n 
B 2 125 LEU 125 126 126 LEU LEU B . n 
B 2 126 GLY 126 127 127 GLY GLY B . n 
B 2 127 LEU 127 128 128 LEU LEU B . n 
B 2 128 LYS 128 129 129 LYS ALA B . n 
B 2 129 CYS 129 130 130 CYS CYS B . n 
B 2 130 ARG 130 131 131 ARG ARG B . n 
B 2 131 ILE 131 132 132 ILE ILE B . n 
B 2 132 TYR 132 133 133 TYR TYR B . n 
B 2 133 MET 133 134 134 MET MET B . n 
B 2 134 GLY 134 135 135 GLY GLY B . n 
B 2 135 ALA 135 136 136 ALA ALA B . n 
B 2 136 LYS 136 137 137 LYS LYS B . n 
B 2 137 ASP 137 138 138 ASP ASP B . n 
B 2 138 VAL 138 139 139 VAL VAL B . n 
B 2 139 GLU 139 140 140 GLU GLU B . n 
B 2 140 ARG 140 141 141 ARG ARG B . n 
B 2 141 GLN 141 142 142 GLN GLN B . n 
B 2 142 SER 142 143 143 SER SER B . n 
B 2 143 PRO 143 144 144 PRO PRO B . n 
B 2 144 ASN 144 145 145 ASN ASN B . n 
B 2 145 VAL 145 146 146 VAL VAL B . n 
B 2 146 PHE 146 147 147 PHE PHE B . n 
B 2 147 ARG 147 148 148 ARG ARG B . n 
B 2 148 MET 148 149 149 MET MET B . n 
B 2 149 ARG 149 150 150 ARG ARG B . n 
B 2 150 LEU 150 151 151 LEU LEU B . n 
B 2 151 MET 151 152 152 MET MET B . n 
B 2 152 GLY 152 153 153 GLY GLY B . n 
B 2 153 ALA 153 154 154 ALA ALA B . n 
B 2 154 GLU 154 155 155 GLU GLU B . n 
B 2 155 VAL 155 156 156 VAL VAL B . n 
B 2 156 ILE 156 157 157 ILE ILE B . n 
B 2 157 PRO 157 158 158 PRO PRO B . n 
B 2 158 VAL 158 159 159 VAL VAL B . n 
B 2 159 HIS 159 160 160 HIS HIS B . n 
B 2 160 SER 160 161 161 SER SER B . n 
B 2 161 GLY 161 162 162 GLY GLY B . n 
B 2 162 SER 162 163 163 SER SER B . n 
B 2 163 ALA 163 164 164 ALA ALA B . n 
B 2 164 THR 164 165 165 THR THR B . n 
B 2 165 LEU 165 166 166 LEU LEU B . n 
B 2 166 LYS 166 167 167 LYS LYS B . n 
B 2 167 ASP 167 168 168 ASP ASP B . n 
B 2 168 ALA 168 169 169 ALA ALA B . n 
B 2 169 CYS 169 170 170 CYS CYS B . n 
B 2 170 ASN 170 171 171 ASN ASN B . n 
B 2 171 GLU 171 172 172 GLU GLU B . n 
B 2 172 ALA 172 173 173 ALA ALA B . n 
B 2 173 LEU 173 174 174 LEU LEU B . n 
B 2 174 ARG 174 175 175 ARG ARG B . n 
B 2 175 ASP 175 176 176 ASP ASP B . n 
B 2 176 TRP 176 177 177 TRP TRP B . n 
B 2 177 SER 177 178 178 SER SER B . n 
B 2 178 GLY 178 179 179 GLY GLY B . n 
B 2 179 SER 179 180 180 SER SER B . n 
B 2 180 TYR 180 181 181 TYR TYR B . n 
B 2 181 GLU 181 182 182 GLU GLU B . n 
B 2 182 THR 182 183 183 THR THR B . n 
B 2 183 ALA 183 184 184 ALA ALA B . n 
B 2 184 HIS 184 185 185 HIS HIS B . n 
B 2 185 TYR 185 186 186 TYR TYR B . n 
B 2 186 MET 186 187 187 MET MET B . n 
B 2 187 LEU 187 188 188 LEU LEU B . n 
B 2 188 GLY 188 189 189 GLY GLY B . n 
B 2 189 THR 189 190 190 THR THR B . n 
B 2 190 ALA 190 191 191 ALA ALA B . n 
B 2 191 ALA 191 192 192 ALA ALA B . n 
B 2 192 GLY 192 193 193 GLY GLY B . n 
B 2 193 PRO 193 194 194 PRO PRO B . n 
B 2 194 HIS 194 195 195 HIS HIS B . n 
B 2 195 PRO 195 196 196 PRO PRO B . n 
B 2 196 TYR 196 197 197 TYR TYR B . n 
B 2 197 PRO 197 198 198 PRO PRO B . n 
B 2 198 THR 198 199 199 THR THR B . n 
B 2 199 ILE 199 200 200 ILE ILE B . n 
B 2 200 VAL 200 201 201 VAL VAL B . n 
B 2 201 ARG 201 202 202 ARG ARG B . n 
B 2 202 GLU 202 203 203 GLU GLU B . n 
B 2 203 PHE 203 204 204 PHE PHE B . n 
B 2 204 GLN 204 205 205 GLN GLN B . n 
B 2 205 ARG 205 206 206 ARG ARG B . n 
B 2 206 MET 206 207 207 MET MET B . n 
B 2 207 ILE 207 208 208 ILE ILE B . n 
B 2 208 GLY 208 209 209 GLY GLY B . n 
B 2 209 GLU 209 210 210 GLU GLU B . n 
B 2 210 GLU 210 211 211 GLU GLU B . n 
B 2 211 THR 211 212 212 THR THR B . n 
B 2 212 LYS 212 213 213 LYS LYS B . n 
B 2 213 ALA 213 214 214 ALA ALA B . n 
B 2 214 GLN 214 215 215 GLN GLN B . n 
B 2 215 ILE 215 216 216 ILE ILE B . n 
B 2 216 LEU 216 217 217 LEU LEU B . n 
B 2 217 ASP 217 218 218 ASP ASP B . n 
B 2 218 LYS 218 219 219 LYS LYS B . n 
B 2 219 GLU 219 220 220 GLU GLU B . n 
B 2 220 GLY 220 221 221 GLY GLY B . n 
B 2 221 ARG 221 222 222 ARG ARG B . n 
B 2 222 LEU 222 223 223 LEU LEU B . n 
B 2 223 PRO 223 224 224 PRO PRO B . n 
B 2 224 ASP 224 225 225 ASP ASP B . n 
B 2 225 ALA 225 226 226 ALA ALA B . n 
B 2 226 VAL 226 227 227 VAL VAL B . n 
B 2 227 ILE 227 228 228 ILE ILE B . n 
B 2 228 ALA 228 229 229 ALA ALA B . n 
B 2 229 CYS 229 230 230 CYS CYS B . n 
B 2 230 VAL 230 231 231 VAL VAL B . n 
B 2 231 GLY 231 232 232 GLY GLY B . n 
B 2 232 GLY 232 233 233 GLY GLY B . n 
B 2 233 GLY 233 234 234 GLY GLY B . n 
B 2 234 SER 234 235 235 SER SER B . n 
B 2 235 ASN 235 236 236 ASN ASN B . n 
B 2 236 ALA 236 237 237 ALA ALA B . n 
B 2 237 ILE 237 238 238 ILE ILE B . n 
B 2 238 GLY 238 239 239 GLY GLY B . n 
B 2 239 MET 239 240 240 MET MET B . n 
B 2 240 PHE 240 241 241 PHE PHE B . n 
B 2 241 ALA 241 242 242 ALA ALA B . n 
B 2 242 ASP 242 243 243 ASP ASP B . n 
B 2 243 PHE 243 244 244 PHE PHE B . n 
B 2 244 ILE 244 245 245 ILE ILE B . n 
B 2 245 ASN 245 246 246 ASN ASN B . n 
B 2 246 ASP 246 247 247 ASP ASP B . n 
B 2 247 THR 247 248 248 THR THR B . n 
B 2 248 SER 248 249 249 SER SER B . n 
B 2 249 VAL 249 250 250 VAL VAL B . n 
B 2 250 GLY 250 251 251 GLY GLY B . n 
B 2 251 LEU 251 252 252 LEU LEU B . n 
B 2 252 ILE 252 253 253 ILE ILE B . n 
B 2 253 GLY 253 254 254 GLY GLY B . n 
B 2 254 VAL 254 255 255 VAL VAL B . n 
B 2 255 GLU 255 256 256 GLU GLU B . n 
B 2 256 PRO 256 257 257 PRO PRO B . n 
B 2 257 GLY 257 258 258 GLY GLY B . n 
B 2 258 GLY 258 259 259 GLY GLY B . n 
B 2 259 HIS 259 260 260 HIS HIS B . n 
B 2 260 GLY 260 261 261 GLY GLY B . n 
B 2 261 ILE 261 262 262 ILE ILE B . n 
B 2 262 GLU 262 263 263 GLU GLU B . n 
B 2 263 THR 263 264 264 THR THR B . n 
B 2 264 GLY 264 265 265 GLY GLY B . n 
B 2 265 GLU 265 266 266 GLU GLU B . n 
B 2 266 HIS 266 267 267 HIS HIS B . n 
B 2 267 GLY 267 268 268 GLY GLY B . n 
B 2 268 ALA 268 269 269 ALA ALA B . n 
B 2 269 PRO 269 270 270 PRO PRO B . n 
B 2 270 LEU 270 271 271 LEU LEU B . n 
B 2 271 LYS 271 272 272 LYS LYS B . n 
B 2 272 HIS 272 273 273 HIS HIS B . n 
B 2 273 GLY 273 274 274 GLY GLY B . n 
B 2 274 ARG 274 275 275 ARG ARG B . n 
B 2 275 VAL 275 276 276 VAL VAL B . n 
B 2 276 GLY 276 277 277 GLY GLY B . n 
B 2 277 ILE 277 278 278 ILE ILE B . n 
B 2 278 TYR 278 279 279 TYR TYR B . n 
B 2 279 PHE 279 280 280 PHE PHE B . n 
B 2 280 GLY 280 281 281 GLY GLY B . n 
B 2 281 MET 281 282 282 MET MET B . n 
B 2 282 LYS 282 283 283 LYS LYS B . n 
B 2 283 ALA 283 284 284 ALA ALA B . n 
B 2 284 PRO 284 285 285 PRO PRO B . n 
B 2 285 MET 285 286 286 MET MET B . n 
B 2 286 MET 286 287 287 MET MET B . n 
B 2 287 GLN 287 288 288 GLN GLN B . n 
B 2 288 THR 288 289 289 THR THR B . n 
B 2 289 ALA 289 290 290 ALA ALA B . n 
B 2 290 ASP 290 291 291 ASP ASP B . n 
B 2 291 GLY 291 292 292 GLY GLY B . n 
B 2 292 GLN 292 293 293 GLN GLN B . n 
B 2 293 ILE 293 294 294 ILE ILE B . n 
B 2 294 GLU 294 295 295 GLU GLU B . n 
B 2 295 GLU 295 296 296 GLU GLU B . n 
B 2 296 SER 296 297 297 SER SER B . n 
B 2 297 TYR 297 298 298 TYR TYR B . n 
B 2 298 SER 298 299 299 SER SER B . n 
B 2 299 ILE 299 300 300 ILE ILE B . n 
B 2 300 SER 300 301 301 SER SER B . n 
B 2 301 ALA 301 302 302 ALA ALA B . n 
B 2 302 GLY 302 303 303 GLY GLY B . n 
B 2 303 LEU 303 304 304 LEU LEU B . n 
B 2 304 ASP 304 305 305 ASP ASP B . n 
B 2 305 PHE 305 306 306 PHE PHE B . n 
B 2 306 PRO 306 307 307 PRO PRO B . n 
B 2 307 SER 307 308 308 SER SER B . n 
B 2 308 VAL 308 309 309 VAL VAL B . n 
B 2 309 GLY 309 310 310 GLY GLY B . n 
B 2 310 PRO 310 311 311 PRO PRO B . n 
B 2 311 GLN 311 312 312 GLN GLN B . n 
B 2 312 HIS 312 313 313 HIS HIS B . n 
B 2 313 ALA 313 314 314 ALA ALA B . n 
B 2 314 TYR 314 315 315 TYR TYR B . n 
B 2 315 LEU 315 316 316 LEU LEU B . n 
B 2 316 ASN 316 317 317 ASN ASN B . n 
B 2 317 SER 317 318 318 SER SER B . n 
B 2 318 ILE 318 319 319 ILE ILE B . n 
B 2 319 GLY 319 320 320 GLY GLY B . n 
B 2 320 ARG 320 321 321 ARG ARG B . n 
B 2 321 ALA 321 322 322 ALA ALA B . n 
B 2 322 ASP 322 323 323 ASP ASP B . n 
B 2 323 TYR 323 324 324 TYR TYR B . n 
B 2 324 VAL 324 325 325 VAL VAL B . n 
B 2 325 SER 325 326 326 SER SER B . n 
B 2 326 ILE 326 327 327 ILE ILE B . n 
B 2 327 THR 327 328 328 THR THR B . n 
B 2 328 ASP 328 329 329 ASP ASP B . n 
B 2 329 ASP 329 330 330 ASP ASP B . n 
B 2 330 GLU 330 331 331 GLU GLU B . n 
B 2 331 ALA 331 332 332 ALA ALA B . n 
B 2 332 LEU 332 333 333 LEU LEU B . n 
B 2 333 GLU 333 334 334 GLU GLU B . n 
B 2 334 ALA 334 335 335 ALA ALA B . n 
B 2 335 PHE 335 336 336 PHE PHE B . n 
B 2 336 LYS 336 337 337 LYS LYS B . n 
B 2 337 THR 337 338 338 THR THR B . n 
B 2 338 LEU 338 339 339 LEU LEU B . n 
B 2 339 CYS 339 340 340 CYS CYS B . n 
B 2 340 ARG 340 341 341 ARG ARG B . n 
B 2 341 HIS 341 342 342 HIS HIS B . n 
B 2 342 GLU 342 343 343 GLU GLU B . n 
B 2 343 GLY 343 344 344 GLY GLY B . n 
B 2 344 ILE 344 345 345 ILE ILE B . n 
B 2 345 ILE 345 346 346 ILE ILE B . n 
B 2 346 PRO 346 347 347 PRO PRO B . n 
B 2 347 ALA 347 348 348 ALA ALA B . n 
B 2 348 LEU 348 349 349 LEU LEU B . n 
B 2 349 GLU 349 350 350 GLU GLU B . n 
B 2 350 SER 350 351 351 SER SER B . n 
B 2 351 SER 351 352 352 SER SER B . n 
B 2 352 HIS 352 353 353 HIS HIS B . n 
B 2 353 ALA 353 354 354 ALA ALA B . n 
B 2 354 LEU 354 355 355 LEU LEU B . n 
B 2 355 ALA 355 356 356 ALA ALA B . n 
B 2 356 HIS 356 357 357 HIS HIS B . n 
B 2 357 ALA 357 358 358 ALA ALA B . n 
B 2 358 LEU 358 359 359 LEU LEU B . n 
B 2 359 LYS 359 360 360 LYS LYS B . n 
B 2 360 MET 360 361 361 MET MET B . n 
B 2 361 MET 361 362 362 MET MET B . n 
B 2 362 ARG 362 363 363 ARG ARG B . n 
B 2 363 GLU 363 364 364 GLU GLU B . n 
B 2 364 GLN 364 365 365 GLN GLN B . n 
B 2 365 PRO 365 366 366 PRO PRO B . n 
B 2 366 GLU 366 367 367 GLU GLU B . n 
B 2 367 LYS 367 368 368 LYS LYS B . n 
B 2 368 GLU 368 369 369 GLU GLU B . n 
B 2 369 GLN 369 370 370 GLN GLN B . n 
B 2 370 LEU 370 371 371 LEU LEU B . n 
B 2 371 LEU 371 372 372 LEU LEU B . n 
B 2 372 VAL 372 373 373 VAL VAL B . n 
B 2 373 VAL 373 374 374 VAL VAL B . n 
B 2 374 ASN 374 375 375 ASN ASN B . n 
B 2 375 LEU 375 376 376 LEU LEU B . n 
B 2 376 SER 376 377 377 SER SER B . n 
B 2 377 GLY 377 378 378 GLY GLY B . n 
B 2 378 ARG 378 379 379 ARG ARG B . n 
B 2 379 GLY 379 380 380 GLY GLY B . n 
B 2 380 ASP 380 381 381 ASP ASP B . n 
B 2 381 LYS 381 382 382 LYS LYS B . n 
B 2 382 ASP 382 383 383 ASP ASP B . n 
B 2 383 ILE 383 384 384 ILE ILE B . n 
B 2 384 PHE 384 385 385 PHE PHE B . n 
B 2 385 THR 385 386 386 THR THR B . n 
B 2 386 VAL 386 387 387 VAL VAL B . n 
B 2 387 HIS 387 388 388 HIS HIS B . n 
B 2 388 ASP 388 389 389 ASP ASP B . n 
B 2 389 ILE 389 390 390 ILE ILE B . n 
B 2 390 LEU 390 391 391 LEU LEU B . n 
B 2 391 LYS 391 392 392 LYS LYS B . n 
B 2 392 ALA 392 393 393 ALA ALA B . n 
B 2 393 ARG 393 394 394 ARG ARG B . n 
B 2 394 GLY 394 395 395 GLY GLY B . n 
B 2 395 GLU 395 396 ?   ?   ?   B . n 
B 2 396 ILE 396 397 ?   ?   ?   B . 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 
C 3 HPF 1   1001 1   HPF AMI A . 
D 4 NA  1   1003 3   NA  NA  B . 
E 5 PLP 1   1002 2   PLP PLP B . 
F 6 HOH 1   1002 7   HOH HOH A . 
F 6 HOH 2   1003 18  HOH HOH A . 
F 6 HOH 3   1004 22  HOH HOH A . 
F 6 HOH 4   1005 23  HOH HOH A . 
F 6 HOH 5   1006 28  HOH HOH A . 
F 6 HOH 6   1007 37  HOH HOH A . 
F 6 HOH 7   1008 38  HOH HOH A . 
F 6 HOH 8   1009 41  HOH HOH A . 
F 6 HOH 9   1010 49  HOH HOH A . 
F 6 HOH 10  1011 52  HOH HOH A . 
F 6 HOH 11  1012 53  HOH HOH A . 
F 6 HOH 12  1013 55  HOH HOH A . 
F 6 HOH 13  1014 56  HOH HOH A . 
F 6 HOH 14  1015 58  HOH HOH A . 
F 6 HOH 15  1016 59  HOH HOH A . 
F 6 HOH 16  1017 61  HOH HOH A . 
F 6 HOH 17  1018 62  HOH HOH A . 
F 6 HOH 18  1019 65  HOH HOH A . 
F 6 HOH 19  1020 71  HOH HOH A . 
F 6 HOH 20  1021 74  HOH HOH A . 
F 6 HOH 21  1022 76  HOH HOH A . 
F 6 HOH 22  1023 77  HOH HOH A . 
F 6 HOH 23  1024 79  HOH HOH A . 
F 6 HOH 24  1025 88  HOH HOH A . 
F 6 HOH 25  1026 89  HOH HOH A . 
F 6 HOH 26  1027 90  HOH HOH A . 
F 6 HOH 27  1028 97  HOH HOH A . 
F 6 HOH 28  1029 98  HOH HOH A . 
F 6 HOH 29  1030 101 HOH HOH A . 
F 6 HOH 30  1031 102 HOH HOH A . 
F 6 HOH 31  1032 103 HOH HOH A . 
F 6 HOH 32  1033 104 HOH HOH A . 
F 6 HOH 33  1034 110 HOH HOH A . 
F 6 HOH 34  1035 112 HOH HOH A . 
F 6 HOH 35  1036 115 HOH HOH A . 
F 6 HOH 36  1037 116 HOH HOH A . 
F 6 HOH 37  1038 117 HOH HOH A . 
F 6 HOH 38  1039 119 HOH HOH A . 
F 6 HOH 39  1040 121 HOH HOH A . 
F 6 HOH 40  1041 122 HOH HOH A . 
F 6 HOH 41  1042 124 HOH HOH A . 
F 6 HOH 42  1043 126 HOH HOH A . 
F 6 HOH 43  1044 132 HOH HOH A . 
F 6 HOH 44  1045 142 HOH HOH A . 
F 6 HOH 45  1046 145 HOH HOH A . 
F 6 HOH 46  1047 146 HOH HOH A . 
F 6 HOH 47  1048 149 HOH HOH A . 
F 6 HOH 48  1049 152 HOH HOH A . 
F 6 HOH 49  1050 155 HOH HOH A . 
F 6 HOH 50  1051 156 HOH HOH A . 
F 6 HOH 51  1052 162 HOH HOH A . 
F 6 HOH 52  1053 164 HOH HOH A . 
F 6 HOH 53  1054 165 HOH HOH A . 
F 6 HOH 54  1055 170 HOH HOH A . 
F 6 HOH 55  1056 171 HOH HOH A . 
F 6 HOH 56  1057 173 HOH HOH A . 
F 6 HOH 57  1058 180 HOH HOH A . 
F 6 HOH 58  1059 182 HOH HOH A . 
F 6 HOH 59  1060 183 HOH HOH A . 
F 6 HOH 60  1061 190 HOH HOH A . 
F 6 HOH 61  1062 192 HOH HOH A . 
F 6 HOH 62  1063 193 HOH HOH A . 
F 6 HOH 63  1064 195 HOH HOH A . 
F 6 HOH 64  1065 201 HOH HOH A . 
F 6 HOH 65  1066 202 HOH HOH A . 
F 6 HOH 66  1067 203 HOH HOH A . 
F 6 HOH 67  1068 204 HOH HOH A . 
F 6 HOH 68  1069 207 HOH HOH A . 
F 6 HOH 69  1070 211 HOH HOH A . 
F 6 HOH 70  1071 214 HOH HOH A . 
F 6 HOH 71  1072 224 HOH HOH A . 
F 6 HOH 72  1073 231 HOH HOH A . 
F 6 HOH 73  1074 235 HOH HOH A . 
F 6 HOH 74  1075 236 HOH HOH A . 
F 6 HOH 75  1076 237 HOH HOH A . 
F 6 HOH 76  1077 242 HOH HOH A . 
F 6 HOH 77  1078 243 HOH HOH A . 
F 6 HOH 78  1079 248 HOH HOH A . 
F 6 HOH 79  1080 250 HOH HOH A . 
F 6 HOH 80  1081 254 HOH HOH A . 
F 6 HOH 81  1082 259 HOH HOH A . 
F 6 HOH 82  1083 261 HOH HOH A . 
F 6 HOH 83  1084 262 HOH HOH A . 
F 6 HOH 84  1085 263 HOH HOH A . 
F 6 HOH 85  1086 266 HOH HOH A . 
F 6 HOH 86  1087 268 HOH HOH A . 
F 6 HOH 87  1088 269 HOH HOH A . 
F 6 HOH 88  1089 270 HOH HOH A . 
F 6 HOH 89  1090 271 HOH HOH A . 
F 6 HOH 90  1091 272 HOH HOH A . 
F 6 HOH 91  1092 273 HOH HOH A . 
F 6 HOH 92  1093 274 HOH HOH A . 
F 6 HOH 93  1094 275 HOH HOH A . 
F 6 HOH 94  1095 279 HOH HOH A . 
F 6 HOH 95  1096 280 HOH HOH A . 
F 6 HOH 96  1097 281 HOH HOH A . 
F 6 HOH 97  1098 282 HOH HOH A . 
F 6 HOH 98  1099 305 HOH HOH A . 
F 6 HOH 99  1100 306 HOH HOH A . 
F 6 HOH 100 1101 307 HOH HOH A . 
F 6 HOH 101 1102 308 HOH HOH A . 
F 6 HOH 102 1103 309 HOH HOH A . 
F 6 HOH 103 1104 337 HOH HOH A . 
F 6 HOH 104 1105 338 HOH HOH A . 
F 6 HOH 105 1106 339 HOH HOH A . 
F 6 HOH 106 1107 340 HOH HOH A . 
F 6 HOH 107 1108 341 HOH HOH A . 
F 6 HOH 108 1109 342 HOH HOH A . 
F 6 HOH 109 1110 343 HOH HOH A . 
F 6 HOH 110 1111 344 HOH HOH A . 
F 6 HOH 111 1112 345 HOH HOH A . 
F 6 HOH 112 1113 346 HOH HOH A . 
F 6 HOH 113 1114 347 HOH HOH A . 
F 6 HOH 114 1115 349 HOH HOH A . 
F 6 HOH 115 1116 350 HOH HOH A . 
F 6 HOH 116 1117 351 HOH HOH A . 
F 6 HOH 117 1118 353 HOH HOH A . 
F 6 HOH 118 1119 354 HOH HOH A . 
F 6 HOH 119 1120 355 HOH HOH A . 
F 6 HOH 120 1121 356 HOH HOH A . 
F 6 HOH 121 1122 357 HOH HOH A . 
F 6 HOH 122 1123 358 HOH HOH A . 
F 6 HOH 123 1124 359 HOH HOH A . 
F 6 HOH 124 1125 360 HOH HOH A . 
F 6 HOH 125 1126 361 HOH HOH A . 
F 6 HOH 126 1127 364 HOH HOH A . 
F 6 HOH 127 1128 365 HOH HOH A . 
F 6 HOH 128 1129 366 HOH HOH A . 
F 6 HOH 129 1130 367 HOH HOH A . 
F 6 HOH 130 1131 368 HOH HOH A . 
F 6 HOH 131 1132 369 HOH HOH A . 
F 6 HOH 132 1133 370 HOH HOH A . 
F 6 HOH 133 1134 371 HOH HOH A . 
F 6 HOH 134 1135 372 HOH HOH A . 
F 6 HOH 135 1136 373 HOH HOH A . 
F 6 HOH 136 1137 374 HOH HOH A . 
F 6 HOH 137 1138 402 HOH HOH A . 
F 6 HOH 138 1139 403 HOH HOH A . 
F 6 HOH 139 1140 404 HOH HOH A . 
F 6 HOH 140 1141 405 HOH HOH A . 
F 6 HOH 141 1142 406 HOH HOH A . 
F 6 HOH 142 1143 407 HOH HOH A . 
F 6 HOH 143 1144 408 HOH HOH A . 
F 6 HOH 144 1145 409 HOH HOH A . 
F 6 HOH 145 1146 410 HOH HOH A . 
F 6 HOH 146 1147 412 HOH HOH A . 
F 6 HOH 147 1148 413 HOH HOH A . 
F 6 HOH 148 1149 414 HOH HOH A . 
F 6 HOH 149 1150 415 HOH HOH A . 
F 6 HOH 150 1151 416 HOH HOH A . 
F 6 HOH 151 1152 417 HOH HOH A . 
F 6 HOH 152 1153 418 HOH HOH A . 
F 6 HOH 153 1154 419 HOH HOH A . 
F 6 HOH 154 1155 420 HOH HOH A . 
F 6 HOH 155 1156 421 HOH HOH A . 
F 6 HOH 156 1157 422 HOH HOH A . 
F 6 HOH 157 1158 423 HOH HOH A . 
F 6 HOH 158 1159 424 HOH HOH A . 
F 6 HOH 159 1160 425 HOH HOH A . 
F 6 HOH 160 1161 426 HOH HOH A . 
F 6 HOH 161 1162 427 HOH HOH A . 
F 6 HOH 162 1163 428 HOH HOH A . 
F 6 HOH 163 1164 429 HOH HOH A . 
F 6 HOH 164 1165 431 HOH HOH A . 
F 6 HOH 165 1166 432 HOH HOH A . 
F 6 HOH 166 1167 433 HOH HOH A . 
F 6 HOH 167 1168 434 HOH HOH A . 
F 6 HOH 168 1169 435 HOH HOH A . 
F 6 HOH 169 1170 436 HOH HOH A . 
F 6 HOH 170 1171 437 HOH HOH A . 
F 6 HOH 171 1172 438 HOH HOH A . 
F 6 HOH 172 1173 440 HOH HOH A . 
F 6 HOH 173 1174 441 HOH HOH A . 
F 6 HOH 174 1175 442 HOH HOH A . 
F 6 HOH 175 1176 443 HOH HOH A . 
F 6 HOH 176 1177 444 HOH HOH A . 
F 6 HOH 177 1178 445 HOH HOH A . 
F 6 HOH 178 1179 446 HOH HOH A . 
F 6 HOH 179 1180 448 HOH HOH A . 
F 6 HOH 180 1181 449 HOH HOH A . 
F 6 HOH 181 1182 450 HOH HOH A . 
F 6 HOH 182 1183 451 HOH HOH A . 
F 6 HOH 183 1184 452 HOH HOH A . 
F 6 HOH 184 1185 453 HOH HOH A . 
F 6 HOH 185 1186 454 HOH HOH A . 
F 6 HOH 186 1187 455 HOH HOH A . 
F 6 HOH 187 1188 456 HOH HOH A . 
F 6 HOH 188 1189 510 HOH HOH A . 
F 6 HOH 189 1190 511 HOH HOH A . 
F 6 HOH 190 1191 512 HOH HOH A . 
F 6 HOH 191 1192 513 HOH HOH A . 
F 6 HOH 192 1193 514 HOH HOH A . 
F 6 HOH 193 1194 515 HOH HOH A . 
F 6 HOH 194 1195 518 HOH HOH A . 
F 6 HOH 195 1196 519 HOH HOH A . 
F 6 HOH 196 1197 520 HOH HOH A . 
F 6 HOH 197 1198 521 HOH HOH A . 
F 6 HOH 198 1199 522 HOH HOH A . 
F 6 HOH 199 1200 524 HOH HOH A . 
F 6 HOH 200 1201 525 HOH HOH A . 
F 6 HOH 201 1202 526 HOH HOH A . 
F 6 HOH 202 1203 527 HOH HOH A . 
F 6 HOH 203 1204 528 HOH HOH A . 
F 6 HOH 204 1205 529 HOH HOH A . 
F 6 HOH 205 1206 530 HOH HOH A . 
F 6 HOH 206 1207 531 HOH HOH A . 
F 6 HOH 207 1208 532 HOH HOH A . 
F 6 HOH 208 1209 533 HOH HOH A . 
F 6 HOH 209 1210 534 HOH HOH A . 
F 6 HOH 210 1211 535 HOH HOH A . 
F 6 HOH 211 1212 536 HOH HOH A . 
F 6 HOH 212 1213 537 HOH HOH A . 
F 6 HOH 213 1214 571 HOH HOH A . 
F 6 HOH 214 1215 573 HOH HOH A . 
F 6 HOH 215 1216 574 HOH HOH A . 
F 6 HOH 216 1217 575 HOH HOH A . 
F 6 HOH 217 1218 576 HOH HOH A . 
F 6 HOH 218 1219 577 HOH HOH A . 
F 6 HOH 219 1220 578 HOH HOH A . 
F 6 HOH 220 1221 579 HOH HOH A . 
F 6 HOH 221 1222 580 HOH HOH A . 
F 6 HOH 222 1223 581 HOH HOH A . 
F 6 HOH 223 1224 582 HOH HOH A . 
F 6 HOH 224 1225 583 HOH HOH A . 
F 6 HOH 225 1226 584 HOH HOH A . 
F 6 HOH 226 1227 585 HOH HOH A . 
F 6 HOH 227 1228 586 HOH HOH A . 
F 6 HOH 228 1229 587 HOH HOH A . 
F 6 HOH 229 1230 588 HOH HOH A . 
F 6 HOH 230 1231 589 HOH HOH A . 
F 6 HOH 231 1232 590 HOH HOH A . 
F 6 HOH 232 1233 591 HOH HOH A . 
F 6 HOH 233 1234 592 HOH HOH A . 
F 6 HOH 234 1235 593 HOH HOH A . 
F 6 HOH 235 1236 594 HOH HOH A . 
F 6 HOH 236 1237 595 HOH HOH A . 
F 6 HOH 237 1238 596 HOH HOH A . 
F 6 HOH 238 1239 597 HOH HOH A . 
F 6 HOH 239 1240 598 HOH HOH A . 
F 6 HOH 240 1241 599 HOH HOH A . 
F 6 HOH 241 1242 600 HOH HOH A . 
F 6 HOH 242 1243 602 HOH HOH A . 
F 6 HOH 243 1244 603 HOH HOH A . 
F 6 HOH 244 1245 604 HOH HOH A . 
F 6 HOH 245 1246 605 HOH HOH A . 
F 6 HOH 246 1247 606 HOH HOH A . 
F 6 HOH 247 1248 607 HOH HOH A . 
F 6 HOH 248 1249 608 HOH HOH A . 
F 6 HOH 249 1250 609 HOH HOH A . 
F 6 HOH 250 1251 610 HOH HOH A . 
F 6 HOH 251 1252 611 HOH HOH A . 
F 6 HOH 252 1253 612 HOH HOH A . 
F 6 HOH 253 1254 613 HOH HOH A . 
F 6 HOH 254 1255 668 HOH HOH A . 
F 6 HOH 255 1256 669 HOH HOH A . 
F 6 HOH 256 1257 670 HOH HOH A . 
F 6 HOH 257 1258 671 HOH HOH A . 
F 6 HOH 258 1259 672 HOH HOH A . 
F 6 HOH 259 1260 673 HOH HOH A . 
F 6 HOH 260 1261 674 HOH HOH A . 
F 6 HOH 261 1262 675 HOH HOH A . 
F 6 HOH 262 1263 676 HOH HOH A . 
F 6 HOH 263 1264 677 HOH HOH A . 
F 6 HOH 264 1265 678 HOH HOH A . 
F 6 HOH 265 1266 679 HOH HOH A . 
F 6 HOH 266 1267 680 HOH HOH A . 
F 6 HOH 267 1268 681 HOH HOH A . 
F 6 HOH 268 1269 682 HOH HOH A . 
F 6 HOH 269 1270 685 HOH HOH A . 
F 6 HOH 270 1271 686 HOH HOH A . 
F 6 HOH 271 1272 687 HOH HOH A . 
F 6 HOH 272 1273 688 HOH HOH A . 
F 6 HOH 273 1274 689 HOH HOH A . 
F 6 HOH 274 1275 690 HOH HOH A . 
F 6 HOH 275 1276 731 HOH HOH A . 
F 6 HOH 276 1277 732 HOH HOH A . 
F 6 HOH 277 1278 733 HOH HOH A . 
F 6 HOH 278 1279 734 HOH HOH A . 
F 6 HOH 279 1280 735 HOH HOH A . 
F 6 HOH 280 1281 736 HOH HOH A . 
F 6 HOH 281 1282 737 HOH HOH A . 
F 6 HOH 282 1283 738 HOH HOH A . 
F 6 HOH 283 1284 739 HOH HOH A . 
F 6 HOH 284 1285 740 HOH HOH A . 
F 6 HOH 285 1286 741 HOH HOH A . 
F 6 HOH 286 1287 742 HOH HOH A . 
F 6 HOH 287 1288 745 HOH HOH A . 
F 6 HOH 288 1289 746 HOH HOH A . 
F 6 HOH 289 1290 747 HOH HOH A . 
F 6 HOH 290 1291 748 HOH HOH A . 
F 6 HOH 291 1292 749 HOH HOH A . 
F 6 HOH 292 1293 750 HOH HOH A . 
F 6 HOH 293 1294 788 HOH HOH A . 
F 6 HOH 294 1295 789 HOH HOH A . 
F 6 HOH 295 1296 790 HOH HOH A . 
F 6 HOH 296 1297 791 HOH HOH A . 
F 6 HOH 297 1298 792 HOH HOH A . 
F 6 HOH 298 1299 793 HOH HOH A . 
F 6 HOH 299 1300 794 HOH HOH A . 
F 6 HOH 300 1301 795 HOH HOH A . 
F 6 HOH 301 1302 796 HOH HOH A . 
F 6 HOH 302 1303 824 HOH HOH A . 
F 6 HOH 303 1304 826 HOH HOH A . 
F 6 HOH 304 1305 827 HOH HOH A . 
F 6 HOH 305 1306 828 HOH HOH A . 
F 6 HOH 306 1307 833 HOH HOH A . 
F 6 HOH 307 1308 835 HOH HOH A . 
F 6 HOH 308 1309 836 HOH HOH A . 
F 6 HOH 309 1310 837 HOH HOH A . 
F 6 HOH 310 1311 838 HOH HOH A . 
F 6 HOH 311 1312 839 HOH HOH A . 
F 6 HOH 312 1313 842 HOH HOH A . 
G 6 HOH 1   1004 1   HOH HOH B . 
G 6 HOH 2   1005 2   HOH HOH B . 
G 6 HOH 3   1006 3   HOH HOH B . 
G 6 HOH 4   1007 4   HOH HOH B . 
G 6 HOH 5   1008 5   HOH HOH B . 
G 6 HOH 6   1009 6   HOH HOH B . 
G 6 HOH 7   1010 8   HOH HOH B . 
G 6 HOH 8   1011 9   HOH HOH B . 
G 6 HOH 9   1012 10  HOH HOH B . 
G 6 HOH 10  1013 11  HOH HOH B . 
G 6 HOH 11  1014 12  HOH HOH B . 
G 6 HOH 12  1015 13  HOH HOH B . 
G 6 HOH 13  1016 14  HOH HOH B . 
G 6 HOH 14  1017 15  HOH HOH B . 
G 6 HOH 15  1018 16  HOH HOH B . 
G 6 HOH 16  1019 17  HOH HOH B . 
G 6 HOH 17  1020 19  HOH HOH B . 
G 6 HOH 18  1021 20  HOH HOH B . 
G 6 HOH 19  1022 21  HOH HOH B . 
G 6 HOH 20  1023 24  HOH HOH B . 
G 6 HOH 21  1024 25  HOH HOH B . 
G 6 HOH 22  1025 26  HOH HOH B . 
G 6 HOH 23  1026 27  HOH HOH B . 
G 6 HOH 24  1027 29  HOH HOH B . 
G 6 HOH 25  1028 30  HOH HOH B . 
G 6 HOH 26  1029 31  HOH HOH B . 
G 6 HOH 27  1030 32  HOH HOH B . 
G 6 HOH 28  1031 33  HOH HOH B . 
G 6 HOH 29  1032 34  HOH HOH B . 
G 6 HOH 30  1033 35  HOH HOH B . 
G 6 HOH 31  1034 36  HOH HOH B . 
G 6 HOH 32  1035 39  HOH HOH B . 
G 6 HOH 33  1036 40  HOH HOH B . 
G 6 HOH 34  1037 42  HOH HOH B . 
G 6 HOH 35  1038 43  HOH HOH B . 
G 6 HOH 36  1039 44  HOH HOH B . 
G 6 HOH 37  1040 45  HOH HOH B . 
G 6 HOH 38  1041 46  HOH HOH B . 
G 6 HOH 39  1042 47  HOH HOH B . 
G 6 HOH 40  1043 48  HOH HOH B . 
G 6 HOH 41  1044 50  HOH HOH B . 
G 6 HOH 42  1045 51  HOH HOH B . 
G 6 HOH 43  1046 54  HOH HOH B . 
G 6 HOH 44  1047 57  HOH HOH B . 
G 6 HOH 45  1048 60  HOH HOH B . 
G 6 HOH 46  1049 63  HOH HOH B . 
G 6 HOH 47  1050 64  HOH HOH B . 
G 6 HOH 48  1051 66  HOH HOH B . 
G 6 HOH 49  1052 67  HOH HOH B . 
G 6 HOH 50  1053 68  HOH HOH B . 
G 6 HOH 51  1054 69  HOH HOH B . 
G 6 HOH 52  1055 70  HOH HOH B . 
G 6 HOH 53  1056 72  HOH HOH B . 
G 6 HOH 54  1057 73  HOH HOH B . 
G 6 HOH 55  1058 75  HOH HOH B . 
G 6 HOH 56  1059 78  HOH HOH B . 
G 6 HOH 57  1060 80  HOH HOH B . 
G 6 HOH 58  1061 81  HOH HOH B . 
G 6 HOH 59  1062 82  HOH HOH B . 
G 6 HOH 60  1063 83  HOH HOH B . 
G 6 HOH 61  1064 84  HOH HOH B . 
G 6 HOH 62  1065 85  HOH HOH B . 
G 6 HOH 63  1066 86  HOH HOH B . 
G 6 HOH 64  1067 87  HOH HOH B . 
G 6 HOH 65  1068 91  HOH HOH B . 
G 6 HOH 66  1069 92  HOH HOH B . 
G 6 HOH 67  1070 94  HOH HOH B . 
G 6 HOH 68  1071 95  HOH HOH B . 
G 6 HOH 69  1072 96  HOH HOH B . 
G 6 HOH 70  1073 99  HOH HOH B . 
G 6 HOH 71  1074 100 HOH HOH B . 
G 6 HOH 72  1075 105 HOH HOH B . 
G 6 HOH 73  1076 106 HOH HOH B . 
G 6 HOH 74  1077 107 HOH HOH B . 
G 6 HOH 75  1078 108 HOH HOH B . 
G 6 HOH 76  1079 109 HOH HOH B . 
G 6 HOH 77  1080 111 HOH HOH B . 
G 6 HOH 78  1081 113 HOH HOH B . 
G 6 HOH 79  1082 114 HOH HOH B . 
G 6 HOH 80  1083 118 HOH HOH B . 
G 6 HOH 81  1084 120 HOH HOH B . 
G 6 HOH 82  1085 123 HOH HOH B . 
G 6 HOH 83  1086 125 HOH HOH B . 
G 6 HOH 84  1087 127 HOH HOH B . 
G 6 HOH 85  1088 128 HOH HOH B . 
G 6 HOH 86  1089 129 HOH HOH B . 
G 6 HOH 87  1090 130 HOH HOH B . 
G 6 HOH 88  1091 131 HOH HOH B . 
G 6 HOH 89  1092 133 HOH HOH B . 
G 6 HOH 90  1093 134 HOH HOH B . 
G 6 HOH 91  1094 135 HOH HOH B . 
G 6 HOH 92  1095 136 HOH HOH B . 
G 6 HOH 93  1096 137 HOH HOH B . 
G 6 HOH 94  1097 138 HOH HOH B . 
G 6 HOH 95  1098 139 HOH HOH B . 
G 6 HOH 96  1099 140 HOH HOH B . 
G 6 HOH 97  1100 141 HOH HOH B . 
G 6 HOH 98  1101 143 HOH HOH B . 
G 6 HOH 99  1102 144 HOH HOH B . 
G 6 HOH 100 1103 147 HOH HOH B . 
G 6 HOH 101 1104 148 HOH HOH B . 
G 6 HOH 102 1105 150 HOH HOH B . 
G 6 HOH 103 1106 151 HOH HOH B . 
G 6 HOH 104 1107 153 HOH HOH B . 
G 6 HOH 105 1108 154 HOH HOH B . 
G 6 HOH 106 1109 157 HOH HOH B . 
G 6 HOH 107 1110 158 HOH HOH B . 
G 6 HOH 108 1111 159 HOH HOH B . 
G 6 HOH 109 1112 160 HOH HOH B . 
G 6 HOH 110 1113 161 HOH HOH B . 
G 6 HOH 111 1114 163 HOH HOH B . 
G 6 HOH 112 1115 166 HOH HOH B . 
G 6 HOH 113 1116 167 HOH HOH B . 
G 6 HOH 114 1117 168 HOH HOH B . 
G 6 HOH 115 1118 169 HOH HOH B . 
G 6 HOH 116 1119 172 HOH HOH B . 
G 6 HOH 117 1120 174 HOH HOH B . 
G 6 HOH 118 1121 175 HOH HOH B . 
G 6 HOH 119 1122 176 HOH HOH B . 
G 6 HOH 120 1123 177 HOH HOH B . 
G 6 HOH 121 1124 178 HOH HOH B . 
G 6 HOH 122 1125 179 HOH HOH B . 
G 6 HOH 123 1126 181 HOH HOH B . 
G 6 HOH 124 1127 184 HOH HOH B . 
G 6 HOH 125 1128 185 HOH HOH B . 
G 6 HOH 126 1129 186 HOH HOH B . 
G 6 HOH 127 1130 187 HOH HOH B . 
G 6 HOH 128 1131 188 HOH HOH B . 
G 6 HOH 129 1132 189 HOH HOH B . 
G 6 HOH 130 1133 191 HOH HOH B . 
G 6 HOH 131 1134 194 HOH HOH B . 
G 6 HOH 132 1135 196 HOH HOH B . 
G 6 HOH 133 1136 197 HOH HOH B . 
G 6 HOH 134 1137 198 HOH HOH B . 
G 6 HOH 135 1138 199 HOH HOH B . 
G 6 HOH 136 1139 200 HOH HOH B . 
G 6 HOH 137 1140 205 HOH HOH B . 
G 6 HOH 138 1141 206 HOH HOH B . 
G 6 HOH 139 1142 208 HOH HOH B . 
G 6 HOH 140 1143 209 HOH HOH B . 
G 6 HOH 141 1144 210 HOH HOH B . 
G 6 HOH 142 1145 212 HOH HOH B . 
G 6 HOH 143 1146 213 HOH HOH B . 
G 6 HOH 144 1147 215 HOH HOH B . 
G 6 HOH 145 1148 216 HOH HOH B . 
G 6 HOH 146 1149 217 HOH HOH B . 
G 6 HOH 147 1150 218 HOH HOH B . 
G 6 HOH 148 1151 219 HOH HOH B . 
G 6 HOH 149 1152 220 HOH HOH B . 
G 6 HOH 150 1153 221 HOH HOH B . 
G 6 HOH 151 1154 222 HOH HOH B . 
G 6 HOH 152 1155 223 HOH HOH B . 
G 6 HOH 153 1156 225 HOH HOH B . 
G 6 HOH 154 1157 226 HOH HOH B . 
G 6 HOH 155 1158 227 HOH HOH B . 
G 6 HOH 156 1159 228 HOH HOH B . 
G 6 HOH 157 1160 229 HOH HOH B . 
G 6 HOH 158 1161 230 HOH HOH B . 
G 6 HOH 159 1162 232 HOH HOH B . 
G 6 HOH 160 1163 233 HOH HOH B . 
G 6 HOH 161 1164 234 HOH HOH B . 
G 6 HOH 162 1165 238 HOH HOH B . 
G 6 HOH 163 1166 239 HOH HOH B . 
G 6 HOH 164 1167 240 HOH HOH B . 
G 6 HOH 165 1168 241 HOH HOH B . 
G 6 HOH 166 1169 244 HOH HOH B . 
G 6 HOH 167 1170 245 HOH HOH B . 
G 6 HOH 168 1171 246 HOH HOH B . 
G 6 HOH 169 1172 247 HOH HOH B . 
G 6 HOH 170 1173 249 HOH HOH B . 
G 6 HOH 171 1174 251 HOH HOH B . 
G 6 HOH 172 1175 252 HOH HOH B . 
G 6 HOH 173 1176 253 HOH HOH B . 
G 6 HOH 174 1177 255 HOH HOH B . 
G 6 HOH 175 1178 256 HOH HOH B . 
G 6 HOH 176 1179 257 HOH HOH B . 
G 6 HOH 177 1180 258 HOH HOH B . 
G 6 HOH 178 1181 260 HOH HOH B . 
G 6 HOH 179 1182 264 HOH HOH B . 
G 6 HOH 180 1183 265 HOH HOH B . 
G 6 HOH 181 1184 267 HOH HOH B . 
G 6 HOH 182 1185 276 HOH HOH B . 
G 6 HOH 183 1186 277 HOH HOH B . 
G 6 HOH 184 1187 278 HOH HOH B . 
G 6 HOH 185 1188 284 HOH HOH B . 
G 6 HOH 186 1189 285 HOH HOH B . 
G 6 HOH 187 1190 286 HOH HOH B . 
G 6 HOH 188 1191 287 HOH HOH B . 
G 6 HOH 189 1192 288 HOH HOH B . 
G 6 HOH 190 1193 289 HOH HOH B . 
G 6 HOH 191 1194 290 HOH HOH B . 
G 6 HOH 192 1195 291 HOH HOH B . 
G 6 HOH 193 1196 292 HOH HOH B . 
G 6 HOH 194 1197 293 HOH HOH B . 
G 6 HOH 195 1198 294 HOH HOH B . 
G 6 HOH 196 1199 295 HOH HOH B . 
G 6 HOH 197 1200 296 HOH HOH B . 
G 6 HOH 198 1201 297 HOH HOH B . 
G 6 HOH 199 1202 298 HOH HOH B . 
G 6 HOH 200 1203 299 HOH HOH B . 
G 6 HOH 201 1204 300 HOH HOH B . 
G 6 HOH 202 1205 301 HOH HOH B . 
G 6 HOH 203 1206 302 HOH HOH B . 
G 6 HOH 204 1207 303 HOH HOH B . 
G 6 HOH 205 1208 304 HOH HOH B . 
G 6 HOH 206 1209 310 HOH HOH B . 
G 6 HOH 207 1210 311 HOH HOH B . 
G 6 HOH 208 1211 312 HOH HOH B . 
G 6 HOH 209 1212 313 HOH HOH B . 
G 6 HOH 210 1213 314 HOH HOH B . 
G 6 HOH 211 1214 315 HOH HOH B . 
G 6 HOH 212 1215 316 HOH HOH B . 
G 6 HOH 213 1216 317 HOH HOH B . 
G 6 HOH 214 1217 318 HOH HOH B . 
G 6 HOH 215 1218 319 HOH HOH B . 
G 6 HOH 216 1219 320 HOH HOH B . 
G 6 HOH 217 1220 321 HOH HOH B . 
G 6 HOH 218 1221 322 HOH HOH B . 
G 6 HOH 219 1222 323 HOH HOH B . 
G 6 HOH 220 1223 324 HOH HOH B . 
G 6 HOH 221 1224 325 HOH HOH B . 
G 6 HOH 222 1225 326 HOH HOH B . 
G 6 HOH 223 1226 327 HOH HOH B . 
G 6 HOH 224 1227 328 HOH HOH B . 
G 6 HOH 225 1228 329 HOH HOH B . 
G 6 HOH 226 1229 330 HOH HOH B . 
G 6 HOH 227 1230 331 HOH HOH B . 
G 6 HOH 228 1231 332 HOH HOH B . 
G 6 HOH 229 1232 333 HOH HOH B . 
G 6 HOH 230 1233 334 HOH HOH B . 
G 6 HOH 231 1234 335 HOH HOH B . 
G 6 HOH 232 1235 336 HOH HOH B . 
G 6 HOH 233 1236 348 HOH HOH B . 
G 6 HOH 234 1237 352 HOH HOH B . 
G 6 HOH 235 1238 362 HOH HOH B . 
G 6 HOH 236 1239 363 HOH HOH B . 
G 6 HOH 237 1240 375 HOH HOH B . 
G 6 HOH 238 1241 376 HOH HOH B . 
G 6 HOH 239 1242 378 HOH HOH B . 
G 6 HOH 240 1243 379 HOH HOH B . 
G 6 HOH 241 1244 380 HOH HOH B . 
G 6 HOH 242 1245 381 HOH HOH B . 
G 6 HOH 243 1246 382 HOH HOH B . 
G 6 HOH 244 1247 383 HOH HOH B . 
G 6 HOH 245 1248 384 HOH HOH B . 
G 6 HOH 246 1249 385 HOH HOH B . 
G 6 HOH 247 1250 386 HOH HOH B . 
G 6 HOH 248 1251 387 HOH HOH B . 
G 6 HOH 249 1252 388 HOH HOH B . 
G 6 HOH 250 1253 389 HOH HOH B . 
G 6 HOH 251 1254 390 HOH HOH B . 
G 6 HOH 252 1255 391 HOH HOH B . 
G 6 HOH 253 1256 392 HOH HOH B . 
G 6 HOH 254 1257 393 HOH HOH B . 
G 6 HOH 255 1258 394 HOH HOH B . 
G 6 HOH 256 1259 395 HOH HOH B . 
G 6 HOH 257 1260 396 HOH HOH B . 
G 6 HOH 258 1261 397 HOH HOH B . 
G 6 HOH 259 1262 398 HOH HOH B . 
G 6 HOH 260 1263 399 HOH HOH B . 
G 6 HOH 261 1264 400 HOH HOH B . 
G 6 HOH 262 1265 401 HOH HOH B . 
G 6 HOH 263 1266 411 HOH HOH B . 
G 6 HOH 264 1267 430 HOH HOH B . 
G 6 HOH 265 1268 439 HOH HOH B . 
G 6 HOH 266 1269 447 HOH HOH B . 
G 6 HOH 267 1270 457 HOH HOH B . 
G 6 HOH 268 1271 458 HOH HOH B . 
G 6 HOH 269 1272 459 HOH HOH B . 
G 6 HOH 270 1273 460 HOH HOH B . 
G 6 HOH 271 1274 461 HOH HOH B . 
G 6 HOH 272 1275 462 HOH HOH B . 
G 6 HOH 273 1276 463 HOH HOH B . 
G 6 HOH 274 1277 464 HOH HOH B . 
G 6 HOH 275 1278 465 HOH HOH B . 
G 6 HOH 276 1279 466 HOH HOH B . 
G 6 HOH 277 1280 467 HOH HOH B . 
G 6 HOH 278 1281 468 HOH HOH B . 
G 6 HOH 279 1282 469 HOH HOH B . 
G 6 HOH 280 1283 470 HOH HOH B . 
G 6 HOH 281 1284 471 HOH HOH B . 
G 6 HOH 282 1285 472 HOH HOH B . 
G 6 HOH 283 1286 473 HOH HOH B . 
G 6 HOH 284 1287 474 HOH HOH B . 
G 6 HOH 285 1288 475 HOH HOH B . 
G 6 HOH 286 1289 476 HOH HOH B . 
G 6 HOH 287 1290 477 HOH HOH B . 
G 6 HOH 288 1291 478 HOH HOH B . 
G 6 HOH 289 1292 479 HOH HOH B . 
G 6 HOH 290 1293 480 HOH HOH B . 
G 6 HOH 291 1294 481 HOH HOH B . 
G 6 HOH 292 1295 482 HOH HOH B . 
G 6 HOH 293 1296 483 HOH HOH B . 
G 6 HOH 294 1297 484 HOH HOH B . 
G 6 HOH 295 1298 485 HOH HOH B . 
G 6 HOH 296 1299 486 HOH HOH B . 
G 6 HOH 297 1300 487 HOH HOH B . 
G 6 HOH 298 1301 488 HOH HOH B . 
G 6 HOH 299 1302 489 HOH HOH B . 
G 6 HOH 300 1303 490 HOH HOH B . 
G 6 HOH 301 1304 491 HOH HOH B . 
G 6 HOH 302 1305 492 HOH HOH B . 
G 6 HOH 303 1306 493 HOH HOH B . 
G 6 HOH 304 1307 494 HOH HOH B . 
G 6 HOH 305 1308 495 HOH HOH B . 
G 6 HOH 306 1309 496 HOH HOH B . 
G 6 HOH 307 1310 497 HOH HOH B . 
G 6 HOH 308 1311 498 HOH HOH B . 
G 6 HOH 309 1312 499 HOH HOH B . 
G 6 HOH 310 1313 500 HOH HOH B . 
G 6 HOH 311 1314 501 HOH HOH B . 
G 6 HOH 312 1315 502 HOH HOH B . 
G 6 HOH 313 1316 503 HOH HOH B . 
G 6 HOH 314 1317 504 HOH HOH B . 
G 6 HOH 315 1318 505 HOH HOH B . 
G 6 HOH 316 1319 506 HOH HOH B . 
G 6 HOH 317 1320 507 HOH HOH B . 
G 6 HOH 318 1321 508 HOH HOH B . 
G 6 HOH 319 1322 509 HOH HOH B . 
G 6 HOH 320 1323 516 HOH HOH B . 
G 6 HOH 321 1324 517 HOH HOH B . 
G 6 HOH 322 1325 523 HOH HOH B . 
G 6 HOH 323 1326 538 HOH HOH B . 
G 6 HOH 324 1327 539 HOH HOH B . 
G 6 HOH 325 1328 540 HOH HOH B . 
G 6 HOH 326 1329 541 HOH HOH B . 
G 6 HOH 327 1330 542 HOH HOH B . 
G 6 HOH 328 1331 543 HOH HOH B . 
G 6 HOH 329 1332 544 HOH HOH B . 
G 6 HOH 330 1333 545 HOH HOH B . 
G 6 HOH 331 1334 546 HOH HOH B . 
G 6 HOH 332 1335 547 HOH HOH B . 
G 6 HOH 333 1336 548 HOH HOH B . 
G 6 HOH 334 1337 549 HOH HOH B . 
G 6 HOH 335 1338 550 HOH HOH B . 
G 6 HOH 336 1339 551 HOH HOH B . 
G 6 HOH 337 1340 552 HOH HOH B . 
G 6 HOH 338 1341 553 HOH HOH B . 
G 6 HOH 339 1342 554 HOH HOH B . 
G 6 HOH 340 1343 555 HOH HOH B . 
G 6 HOH 341 1344 556 HOH HOH B . 
G 6 HOH 342 1345 557 HOH HOH B . 
G 6 HOH 343 1346 558 HOH HOH B . 
G 6 HOH 344 1347 559 HOH HOH B . 
G 6 HOH 345 1348 560 HOH HOH B . 
G 6 HOH 346 1349 561 HOH HOH B . 
G 6 HOH 347 1350 562 HOH HOH B . 
G 6 HOH 348 1351 563 HOH HOH B . 
G 6 HOH 349 1352 564 HOH HOH B . 
G 6 HOH 350 1353 565 HOH HOH B . 
G 6 HOH 351 1354 566 HOH HOH B . 
G 6 HOH 352 1355 567 HOH HOH B . 
G 6 HOH 353 1356 568 HOH HOH B . 
G 6 HOH 354 1357 569 HOH HOH B . 
G 6 HOH 355 1358 570 HOH HOH B . 
G 6 HOH 356 1359 572 HOH HOH B . 
G 6 HOH 357 1360 601 HOH HOH B . 
G 6 HOH 358 1361 614 HOH HOH B . 
G 6 HOH 359 1362 615 HOH HOH B . 
G 6 HOH 360 1363 616 HOH HOH B . 
G 6 HOH 361 1364 617 HOH HOH B . 
G 6 HOH 362 1365 618 HOH HOH B . 
G 6 HOH 363 1366 619 HOH HOH B . 
G 6 HOH 364 1367 620 HOH HOH B . 
G 6 HOH 365 1368 621 HOH HOH B . 
G 6 HOH 366 1369 622 HOH HOH B . 
G 6 HOH 367 1370 623 HOH HOH B . 
G 6 HOH 368 1371 624 HOH HOH B . 
G 6 HOH 369 1372 625 HOH HOH B . 
G 6 HOH 370 1373 626 HOH HOH B . 
G 6 HOH 371 1374 627 HOH HOH B . 
G 6 HOH 372 1375 628 HOH HOH B . 
G 6 HOH 373 1376 629 HOH HOH B . 
G 6 HOH 374 1377 630 HOH HOH B . 
G 6 HOH 375 1378 631 HOH HOH B . 
G 6 HOH 376 1379 632 HOH HOH B . 
G 6 HOH 377 1380 633 HOH HOH B . 
G 6 HOH 378 1381 634 HOH HOH B . 
G 6 HOH 379 1382 635 HOH HOH B . 
G 6 HOH 380 1383 636 HOH HOH B . 
G 6 HOH 381 1384 637 HOH HOH B . 
G 6 HOH 382 1385 638 HOH HOH B . 
G 6 HOH 383 1386 639 HOH HOH B . 
G 6 HOH 384 1387 640 HOH HOH B . 
G 6 HOH 385 1388 641 HOH HOH B . 
G 6 HOH 386 1389 642 HOH HOH B . 
G 6 HOH 387 1390 643 HOH HOH B . 
G 6 HOH 388 1391 644 HOH HOH B . 
G 6 HOH 389 1392 645 HOH HOH B . 
G 6 HOH 390 1393 646 HOH HOH B . 
G 6 HOH 391 1394 647 HOH HOH B . 
G 6 HOH 392 1395 648 HOH HOH B . 
G 6 HOH 393 1396 649 HOH HOH B . 
G 6 HOH 394 1397 650 HOH HOH B . 
G 6 HOH 395 1398 651 HOH HOH B . 
G 6 HOH 396 1399 652 HOH HOH B . 
G 6 HOH 397 1400 653 HOH HOH B . 
G 6 HOH 398 1401 654 HOH HOH B . 
G 6 HOH 399 1402 655 HOH HOH B . 
G 6 HOH 400 1403 656 HOH HOH B . 
G 6 HOH 401 1404 657 HOH HOH B . 
G 6 HOH 402 1405 658 HOH HOH B . 
G 6 HOH 403 1406 659 HOH HOH B . 
G 6 HOH 404 1407 660 HOH HOH B . 
G 6 HOH 405 1408 661 HOH HOH B . 
G 6 HOH 406 1409 662 HOH HOH B . 
G 6 HOH 407 1410 663 HOH HOH B . 
G 6 HOH 408 1411 664 HOH HOH B . 
G 6 HOH 409 1412 665 HOH HOH B . 
G 6 HOH 410 1413 666 HOH HOH B . 
G 6 HOH 411 1414 667 HOH HOH B . 
G 6 HOH 412 1415 683 HOH HOH B . 
G 6 HOH 413 1416 684 HOH HOH B . 
G 6 HOH 414 1417 691 HOH HOH B . 
G 6 HOH 415 1418 692 HOH HOH B . 
G 6 HOH 416 1419 693 HOH HOH B . 
G 6 HOH 417 1420 694 HOH HOH B . 
G 6 HOH 418 1421 695 HOH HOH B . 
G 6 HOH 419 1422 696 HOH HOH B . 
G 6 HOH 420 1423 697 HOH HOH B . 
G 6 HOH 421 1424 698 HOH HOH B . 
G 6 HOH 422 1425 699 HOH HOH B . 
G 6 HOH 423 1426 700 HOH HOH B . 
G 6 HOH 424 1427 701 HOH HOH B . 
G 6 HOH 425 1428 702 HOH HOH B . 
G 6 HOH 426 1429 703 HOH HOH B . 
G 6 HOH 427 1430 704 HOH HOH B . 
G 6 HOH 428 1431 705 HOH HOH B . 
G 6 HOH 429 1432 706 HOH HOH B . 
G 6 HOH 430 1433 707 HOH HOH B . 
G 6 HOH 431 1434 708 HOH HOH B . 
G 6 HOH 432 1435 709 HOH HOH B . 
G 6 HOH 433 1436 710 HOH HOH B . 
G 6 HOH 434 1437 711 HOH HOH B . 
G 6 HOH 435 1438 712 HOH HOH B . 
G 6 HOH 436 1439 713 HOH HOH B . 
G 6 HOH 437 1440 714 HOH HOH B . 
G 6 HOH 438 1441 715 HOH HOH B . 
G 6 HOH 439 1442 716 HOH HOH B . 
G 6 HOH 440 1443 717 HOH HOH B . 
G 6 HOH 441 1444 718 HOH HOH B . 
G 6 HOH 442 1445 719 HOH HOH B . 
G 6 HOH 443 1446 720 HOH HOH B . 
G 6 HOH 444 1447 721 HOH HOH B . 
G 6 HOH 445 1448 722 HOH HOH B . 
G 6 HOH 446 1449 723 HOH HOH B . 
G 6 HOH 447 1450 724 HOH HOH B . 
G 6 HOH 448 1451 725 HOH HOH B . 
G 6 HOH 449 1452 726 HOH HOH B . 
G 6 HOH 450 1453 727 HOH HOH B . 
G 6 HOH 451 1454 728 HOH HOH B . 
G 6 HOH 452 1455 729 HOH HOH B . 
G 6 HOH 453 1456 744 HOH HOH B . 
G 6 HOH 454 1457 751 HOH HOH B . 
G 6 HOH 455 1458 752 HOH HOH B . 
G 6 HOH 456 1459 753 HOH HOH B . 
G 6 HOH 457 1460 754 HOH HOH B . 
G 6 HOH 458 1461 755 HOH HOH B . 
G 6 HOH 459 1462 756 HOH HOH B . 
G 6 HOH 460 1463 757 HOH HOH B . 
G 6 HOH 461 1464 758 HOH HOH B . 
G 6 HOH 462 1465 759 HOH HOH B . 
G 6 HOH 463 1466 760 HOH HOH B . 
G 6 HOH 464 1467 761 HOH HOH B . 
G 6 HOH 465 1468 762 HOH HOH B . 
G 6 HOH 466 1469 763 HOH HOH B . 
G 6 HOH 467 1470 764 HOH HOH B . 
G 6 HOH 468 1471 765 HOH HOH B . 
G 6 HOH 469 1472 766 HOH HOH B . 
G 6 HOH 470 1473 767 HOH HOH B . 
G 6 HOH 471 1474 768 HOH HOH B . 
G 6 HOH 472 1475 769 HOH HOH B . 
G 6 HOH 473 1476 770 HOH HOH B . 
G 6 HOH 474 1477 771 HOH HOH B . 
G 6 HOH 475 1478 772 HOH HOH B . 
G 6 HOH 476 1479 773 HOH HOH B . 
G 6 HOH 477 1480 774 HOH HOH B . 
G 6 HOH 478 1481 775 HOH HOH B . 
G 6 HOH 479 1482 776 HOH HOH B . 
G 6 HOH 480 1483 777 HOH HOH B . 
G 6 HOH 481 1484 778 HOH HOH B . 
G 6 HOH 482 1485 779 HOH HOH B . 
G 6 HOH 483 1486 780 HOH HOH B . 
G 6 HOH 484 1487 781 HOH HOH B . 
G 6 HOH 485 1488 782 HOH HOH B . 
G 6 HOH 486 1489 783 HOH HOH B . 
G 6 HOH 487 1490 784 HOH HOH B . 
G 6 HOH 488 1491 785 HOH HOH B . 
G 6 HOH 489 1492 786 HOH HOH B . 
G 6 HOH 490 1493 787 HOH HOH B . 
G 6 HOH 491 1494 797 HOH HOH B . 
G 6 HOH 492 1495 798 HOH HOH B . 
G 6 HOH 493 1496 799 HOH HOH B . 
G 6 HOH 494 1497 800 HOH HOH B . 
G 6 HOH 495 1498 801 HOH HOH B . 
G 6 HOH 496 1499 802 HOH HOH B . 
G 6 HOH 497 1500 803 HOH HOH B . 
G 6 HOH 498 1501 804 HOH HOH B . 
G 6 HOH 499 1502 805 HOH HOH B . 
G 6 HOH 500 1503 806 HOH HOH B . 
G 6 HOH 501 1504 807 HOH HOH B . 
G 6 HOH 502 1505 808 HOH HOH B . 
G 6 HOH 503 1506 809 HOH HOH B . 
G 6 HOH 504 1507 810 HOH HOH B . 
G 6 HOH 505 1508 811 HOH HOH B . 
G 6 HOH 506 1509 812 HOH HOH B . 
G 6 HOH 507 1510 813 HOH HOH B . 
G 6 HOH 508 1511 814 HOH HOH B . 
G 6 HOH 509 1512 815 HOH HOH B . 
G 6 HOH 510 1513 816 HOH HOH B . 
G 6 HOH 511 1514 817 HOH HOH B . 
G 6 HOH 512 1515 818 HOH HOH B . 
G 6 HOH 513 1516 819 HOH HOH B . 
G 6 HOH 514 1517 820 HOH HOH B . 
G 6 HOH 515 1518 821 HOH HOH B . 
G 6 HOH 516 1519 822 HOH HOH B . 
G 6 HOH 517 1520 823 HOH HOH B . 
G 6 HOH 518 1521 825 HOH HOH B . 
G 6 HOH 519 1522 829 HOH HOH B . 
G 6 HOH 520 1523 830 HOH HOH B . 
G 6 HOH 521 1524 831 HOH HOH B . 
G 6 HOH 522 1525 832 HOH HOH B . 
G 6 HOH 523 1526 834 HOH HOH B . 
G 6 HOH 524 1527 840 HOH HOH B . 
G 6 HOH 525 1528 841 HOH HOH B . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
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_655 -x+1,y,-z -1.0000000000 0.0000000000 0.0000000000 183.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     1375 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   G 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O ? B GLY 231 ? B GLY 232  ? 1_555 NA ? D NA . ? B NA 1003 ? 1_555 O A B PHE 305 ? B PHE 306  ? 1_555 105.0 ? 
2  O ? B GLY 231 ? B GLY 232  ? 1_555 NA ? D NA . ? B NA 1003 ? 1_555 O ? G HOH .   ? B HOH 1039 ? 1_555 108.1 ? 
3  O A B PHE 305 ? B PHE 306  ? 1_555 NA ? D NA . ? B NA 1003 ? 1_555 O ? G HOH .   ? B HOH 1039 ? 1_555 79.5  ? 
4  O ? B GLY 231 ? B GLY 232  ? 1_555 NA ? D NA . ? B NA 1003 ? 1_555 O ? G HOH .   ? B HOH 1047 ? 1_555 89.5  ? 
5  O A B PHE 305 ? B PHE 306  ? 1_555 NA ? D NA . ? B NA 1003 ? 1_555 O ? G HOH .   ? B HOH 1047 ? 1_555 163.5 ? 
6  O ? G HOH .   ? B HOH 1039 ? 1_555 NA ? D NA . ? B NA 1003 ? 1_555 O ? G HOH .   ? B HOH 1047 ? 1_555 88.7  ? 
7  O ? B GLY 231 ? B GLY 232  ? 1_555 NA ? D NA . ? B NA 1003 ? 1_555 O ? B SER 307 ? B SER 308  ? 1_555 93.3  ? 
8  O A B PHE 305 ? B PHE 306  ? 1_555 NA ? D NA . ? B NA 1003 ? 1_555 O ? B SER 307 ? B SER 308  ? 1_555 85.7  ? 
9  O ? G HOH .   ? B HOH 1039 ? 1_555 NA ? D NA . ? B NA 1003 ? 1_555 O ? B SER 307 ? B SER 308  ? 1_555 156.5 ? 
10 O ? G HOH .   ? B HOH 1047 ? 1_555 NA ? D NA . ? B NA 1003 ? 1_555 O ? B SER 307 ? B SER 308  ? 1_555 101.5 ? 
11 O ? B GLY 231 ? B GLY 232  ? 1_555 NA ? D NA . ? B NA 1003 ? 1_555 O B B PHE 305 ? B PHE 306  ? 1_555 123.8 ? 
12 O A B PHE 305 ? B PHE 306  ? 1_555 NA ? D NA . ? B NA 1003 ? 1_555 O B B PHE 305 ? B PHE 306  ? 1_555 19.6  ? 
13 O ? G HOH .   ? B HOH 1039 ? 1_555 NA ? D NA . ? B NA 1003 ? 1_555 O B B PHE 305 ? B PHE 306  ? 1_555 70.0  ? 
14 O ? G HOH .   ? B HOH 1047 ? 1_555 NA ? D NA . ? B NA 1003 ? 1_555 O B B PHE 305 ? B PHE 306  ? 1_555 144.2 ? 
15 O ? B SER 307 ? B SER 308  ? 1_555 NA ? D NA . ? B NA 1003 ? 1_555 O B B PHE 305 ? B PHE 306  ? 1_555 90.2  ? 
# 
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 2005-12-27 
2 'Structure model' 1 1 2008-04-30 
3 'Structure model' 1 2 2011-07-13 
# 
_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' 'Version format compliance' 
2 3 'Structure model' 'Non-polymer description'   
3 3 'Structure model' 'Version format compliance' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
CNS    refinement       1.0 ? 1 
PROCOR 'data reduction' .   ? 2 
XDS    'data scaling'   .   ? 3 
CNS    phasing          .   ? 4 
# 
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 CG B GLU 11  ? ? CD B GLU 11  ? ? 1.626 1.515 0.111  0.015 N 
2 1 CG B MET 286 ? A SD B MET 286 ? A 1.600 1.807 -0.207 0.026 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 NE A ARG 89 ? ? CZ A ARG 89 ? ? NH1 A ARG 89 ? ? 123.51 120.30 3.21  0.50 N 
2 1 NE A ARG 89 ? ? CZ A ARG 89 ? ? NH2 A ARG 89 ? ? 117.24 120.30 -3.06 0.50 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 ASN A 157 ? A -78.08  21.00   
2 1 PHE A 212 ? ? 99.04   115.79  
3 1 CYS B 62  ? ? -105.95 66.43   
4 1 THR B 165 ? ? -132.24 -158.73 
5 1 PRO B 307 ? B -64.74  2.73    
6 1 SER B 308 ? ? -148.38 -157.77 
7 1 SER B 308 ? ? -130.71 -157.77 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    TYR 
_pdbx_validate_planes.auth_asym_id    B 
_pdbx_validate_planes.auth_seq_id     298 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.069 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 2   ? CG  ? A GLU 2   CG  
2  1 Y 1 A GLU 2   ? CD  ? A GLU 2   CD  
3  1 Y 1 A GLU 2   ? OE1 ? A GLU 2   OE1 
4  1 Y 1 A GLU 2   ? OE2 ? A GLU 2   OE2 
5  1 Y 1 A ARG 15  ? CG  ? A ARG 15  CG  
6  1 Y 1 A ARG 15  ? CD  ? A ARG 15  CD  
7  1 Y 1 A ARG 15  ? NE  ? A ARG 15  NE  
8  1 Y 1 A ARG 15  ? CZ  ? A ARG 15  CZ  
9  1 Y 1 A ARG 15  ? NH1 ? A ARG 15  NH1 
10 1 Y 1 A ARG 15  ? NH2 ? A ARG 15  NH2 
11 1 Y 1 A LEU 191 ? CG  ? A LEU 191 CG  
12 1 Y 1 A LEU 191 ? CD1 ? A LEU 191 CD1 
13 1 Y 1 A LEU 191 ? CD2 ? A LEU 191 CD2 
14 1 Y 1 A GLU 198 ? CG  ? A GLU 198 CG  
15 1 Y 1 A GLU 198 ? CD  ? A GLU 198 CD  
16 1 Y 1 A GLU 198 ? OE1 ? A GLU 198 OE1 
17 1 Y 1 A GLU 198 ? OE2 ? A GLU 198 OE2 
18 1 Y 1 A LYS 243 ? CG  ? A LYS 243 CG  
19 1 Y 1 A LYS 243 ? CD  ? A LYS 243 CD  
20 1 Y 1 A LYS 243 ? CE  ? A LYS 243 CE  
21 1 Y 1 A LYS 243 ? NZ  ? A LYS 243 NZ  
22 1 Y 1 A LYS 249 ? CG  ? A LYS 249 CG  
23 1 Y 1 A LYS 249 ? CD  ? A LYS 249 CD  
24 1 Y 1 A LYS 249 ? CE  ? A LYS 249 CE  
25 1 Y 1 A LYS 249 ? NZ  ? A LYS 249 NZ  
26 1 Y 1 B GLN 63  ? CG  ? B GLN 62  CG  
27 1 Y 1 B GLN 63  ? CD  ? B GLN 62  CD  
28 1 Y 1 B GLN 63  ? OE1 ? B GLN 62  OE1 
29 1 Y 1 B GLN 63  ? NE2 ? B GLN 62  NE2 
30 1 Y 1 B LYS 129 ? CG  ? B LYS 128 CG  
31 1 Y 1 B LYS 129 ? CD  ? B LYS 128 CD  
32 1 Y 1 B LYS 129 ? CE  ? B LYS 128 CE  
33 1 Y 1 B LYS 129 ? NZ  ? B LYS 128 NZ  
# 
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 ALA 268 ? A ALA 268 
2 1 Y 1 B GLU 396 ? B GLU 395 
3 1 Y 1 B ILE 397 ? B ILE 396 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 '1-[(2-HYDROXYLPHENYL)AMINO]3-GLYCEROLPHOSPHATE' HPF 
4 'SODIUM ION'                                     NA  
5 "PYRIDOXAL-5'-PHOSPHATE"                         PLP 
6 water                                            HOH 
# 
