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***  [C]_[R]_phosphoglycerate_kinase  ***

elNémo ID: 19100820415586818

Job options:

ID        	=	 19100820415586818
JOBID     	=	 [C]_[R]_phosphoglycerate_kinase
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER [C]_[R]_phosphoglycerate_kinase

data_3PGK
# 
_entry.id   3PGK 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.287 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3PGK         
WWPDB D_1000179105 
# 
_pdbx_database_PDB_obs_spr.id               SPRSDE 
_pdbx_database_PDB_obs_spr.date             1982-09-24 
_pdbx_database_PDB_obs_spr.pdb_id           3PGK 
_pdbx_database_PDB_obs_spr.replace_pdb_id   1PGK 
_pdbx_database_PDB_obs_spr.details          ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3PGK 
_pdbx_database_status.recvd_initial_deposition_date   1982-07-15 
_pdbx_database_status.deposit_site                    ? 
_pdbx_database_status.process_site                    BNL 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Shaw, P.J.'   1 
'Walker, N.P.' 2 
'Watson, H.C.' 3 
# 
loop_
_citation.id 
_citation.title 
_citation.journal_abbrev 
_citation.journal_volume 
_citation.page_first 
_citation.page_last 
_citation.year 
_citation.journal_id_ASTM 
_citation.country 
_citation.journal_id_ISSN 
_citation.journal_id_CSD 
_citation.book_publisher 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_DOI 
primary 'Sequence and structure of yeast phosphoglycerate kinase.'          'Embo J.'          1   1635 1640 1982 EMJODG UK 
0261-4189 0897 ? 6765200 ? 
1       'The Complete Amino Acid Sequence of Yeast Phosphoglycerate Kinase' Biochem.J.         211 199  ?    1983 BIJOAK UK 
0264-6021 0043 ? ?       ? 
2       'Sequence and Structure of Yeast Phosphoglycerate Kinase'           'Embo J.'          1   1635 ?    1982 EMJODG UK 
0261-4189 0897 ? ?       ? 
3       'Structure of Yeast Phosphoglycerate Kinase'                        Nature             257 14   ?    1974 NATUAS UK 
0028-0836 0006 ? ?       ? 
4       'Low Resolution Structure of Yeast Phosphoglycerate Kinase'         'Nature New Biol.' 240 134  ?    1972 NNBYA7 UK 
0369-4887 0192 ? ?       ? 
5       'Crystallographic Study of Yeast Phosphoglycerate Kinase'           J.Mol.Biol.        57  623  ?    1971 JMOBAK UK 
0022-2836 0070 ? ?       ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Watson, H.C.'     1  
primary 'Walker, N.P.'     2  
primary 'Shaw, P.J.'       3  
primary 'Bryant, T.N.'     4  
primary 'Wendell, P.L.'    5  
primary 'Fothergill, L.A.' 6  
primary 'Perkins, R.E.'    7  
primary 'Conroy, S.C.'     8  
primary 'Dobson, M.J.'     9  
primary 'Tuite, M.F.'      10 
1       'Perkins, R.E.'    11 
1       'Conroy, S.C.'     12 
1       'Dunbar, B.'       13 
1       'Fothergill, L.A.' 14 
1       'Tuite, M.F.'      15 
1       'Dobson, M.J.'     16 
1       'Kingsman, S.M.'   17 
1       'Kingsman, A.J.'   18 
2       'Watson, H.C.'     19 
2       'Walker, N.P.C.'   20 
2       'Shaw, P.J.'       21 
2       'Bryant, T.N.'     22 
2       'Wendell, P.L.'    23 
2       'Fothergill, L.A.' 24 
2       'Perkins, R.E.'    25 
2       'Conroy, S.C.'     26 
2       'Dobson, M.J.'     27 
2       'Tuite, M.F.'      28 
2       'Kingsman, A.J.'   29 
2       'Kingsman, S.M.'   30 
3       'Bryant, T.N.'     31 
3       'Watson, H.C.'     32 
3       'Wendell, P.L.'    33 
4       'Wendell, P.L.'    34 
4       'Bryant, T.N.'     35 
4       'Watson, H.C.'     36 
5       'Watson, H.C.'     37 
5       'Wendell, P.L.'    38 
5       'Scopes, R.K.'     39 
# 
_cell.entry_id           3PGK 
_cell.length_a           126.600 
_cell.length_b           54.400 
_cell.length_c           93.000 
_cell.angle_alpha        90.00 
_cell.angle_beta         134.40 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         3PGK 
_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 'PHOSPHOGLYCERATE KINASE'   44652.125 1 2.7.2.3 ? ? ? 
2 non-polymer syn 'MAGNESIUM ION'             24.305    1 ?       ? ? ? 
3 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE" 507.181   1 ?       ? ? ? 
4 non-polymer syn '3-PHOSPHOGLYCERIC ACID'    186.057   1 ?       ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;(ACE)SLSSKLSVQDLDLKDKRVFIRVDFNVPLDGKKITSNQRIVAALPTIKYVLEHHPRYVVLASHLGRPNGERNEKYS
LAPVAKELQSLLGKDVTFLNDCVGPEVEAAVKASAPGSVILLENLRYHIEEEGSRKVDGQKVKASKEDVQKFRHELSSLA
DVYINDAFGTAHRAHSSMVGFDLPQRAAGFLLEKELKYFGKALENPTRPFLAILGGAKVADKIQLIDNLLDKVDSIIIGG
GMAFTFKKVLENTEIGDSIFDKAVGPEIAKLMEKAKAKGVEVVLPVDFIIADAFSASANTKTVTDKEGIPAGWQGLDNGP
ESRKLFAATVAKATVILWNGPPGVFEFEKFAAGTKALLDEVVKSSAAGNTVIIGGGDTATVAKKYGVTDKISHVSTGGGA
SLELLEGKELPGVAFLSEKK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;XSLSSKLSVQDLDLKDKRVFIRVDFNVPLDGKKITSNQRIVAALPTIKYVLEHHPRYVVLASHLGRPNGERNEKYSLAPV
AKELQSLLGKDVTFLNDCVGPEVEAAVKASAPGSVILLENLRYHIEEEGSRKVDGQKVKASKEDVQKFRHELSSLADVYI
NDAFGTAHRAHSSMVGFDLPQRAAGFLLEKELKYFGKALENPTRPFLAILGGAKVADKIQLIDNLLDKVDSIIIGGGMAF
TFKKVLENTEIGDSIFDKAVGPEIAKLMEKAKAKGVEVVLPVDFIIADAFSASANTKTVTDKEGIPAGWQGLDNGPESRK
LFAATVAKATVILWNGPPGVFEFEKFAAGTKALLDEVVKSSAAGNTVIIGGGDTATVAKKYGVTDKISHVSTGGGASLEL
LEGKELPGVAFLSEKK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ACE n 
1 2   SER n 
1 3   LEU n 
1 4   SER n 
1 5   SER n 
1 6   LYS n 
1 7   LEU n 
1 8   SER n 
1 9   VAL n 
1 10  GLN n 
1 11  ASP n 
1 12  LEU n 
1 13  ASP n 
1 14  LEU n 
1 15  LYS n 
1 16  ASP n 
1 17  LYS n 
1 18  ARG n 
1 19  VAL n 
1 20  PHE n 
1 21  ILE n 
1 22  ARG n 
1 23  VAL n 
1 24  ASP n 
1 25  PHE n 
1 26  ASN n 
1 27  VAL n 
1 28  PRO n 
1 29  LEU n 
1 30  ASP n 
1 31  GLY n 
1 32  LYS n 
1 33  LYS n 
1 34  ILE n 
1 35  THR n 
1 36  SER n 
1 37  ASN n 
1 38  GLN n 
1 39  ARG n 
1 40  ILE n 
1 41  VAL n 
1 42  ALA n 
1 43  ALA n 
1 44  LEU n 
1 45  PRO n 
1 46  THR n 
1 47  ILE n 
1 48  LYS n 
1 49  TYR n 
1 50  VAL n 
1 51  LEU n 
1 52  GLU n 
1 53  HIS n 
1 54  HIS n 
1 55  PRO n 
1 56  ARG n 
1 57  TYR n 
1 58  VAL n 
1 59  VAL n 
1 60  LEU n 
1 61  ALA n 
1 62  SER n 
1 63  HIS n 
1 64  LEU n 
1 65  GLY n 
1 66  ARG n 
1 67  PRO n 
1 68  ASN n 
1 69  GLY n 
1 70  GLU n 
1 71  ARG n 
1 72  ASN n 
1 73  GLU n 
1 74  LYS n 
1 75  TYR n 
1 76  SER n 
1 77  LEU n 
1 78  ALA n 
1 79  PRO n 
1 80  VAL n 
1 81  ALA n 
1 82  LYS n 
1 83  GLU n 
1 84  LEU n 
1 85  GLN n 
1 86  SER n 
1 87  LEU n 
1 88  LEU n 
1 89  GLY n 
1 90  LYS n 
1 91  ASP n 
1 92  VAL n 
1 93  THR n 
1 94  PHE n 
1 95  LEU n 
1 96  ASN n 
1 97  ASP n 
1 98  CYS n 
1 99  VAL n 
1 100 GLY n 
1 101 PRO n 
1 102 GLU n 
1 103 VAL n 
1 104 GLU n 
1 105 ALA n 
1 106 ALA n 
1 107 VAL n 
1 108 LYS n 
1 109 ALA n 
1 110 SER n 
1 111 ALA n 
1 112 PRO n 
1 113 GLY n 
1 114 SER n 
1 115 VAL n 
1 116 ILE n 
1 117 LEU n 
1 118 LEU n 
1 119 GLU n 
1 120 ASN n 
1 121 LEU n 
1 122 ARG n 
1 123 TYR n 
1 124 HIS n 
1 125 ILE n 
1 126 GLU n 
1 127 GLU n 
1 128 GLU n 
1 129 GLY n 
1 130 SER n 
1 131 ARG n 
1 132 LYS n 
1 133 VAL n 
1 134 ASP n 
1 135 GLY n 
1 136 GLN n 
1 137 LYS n 
1 138 VAL n 
1 139 LYS n 
1 140 ALA n 
1 141 SER n 
1 142 LYS n 
1 143 GLU n 
1 144 ASP n 
1 145 VAL n 
1 146 GLN n 
1 147 LYS n 
1 148 PHE n 
1 149 ARG n 
1 150 HIS n 
1 151 GLU n 
1 152 LEU n 
1 153 SER n 
1 154 SER n 
1 155 LEU n 
1 156 ALA n 
1 157 ASP n 
1 158 VAL n 
1 159 TYR n 
1 160 ILE n 
1 161 ASN n 
1 162 ASP n 
1 163 ALA n 
1 164 PHE n 
1 165 GLY n 
1 166 THR n 
1 167 ALA n 
1 168 HIS n 
1 169 ARG n 
1 170 ALA n 
1 171 HIS n 
1 172 SER n 
1 173 SER n 
1 174 MET n 
1 175 VAL n 
1 176 GLY n 
1 177 PHE n 
1 178 ASP n 
1 179 LEU n 
1 180 PRO n 
1 181 GLN n 
1 182 ARG n 
1 183 ALA n 
1 184 ALA n 
1 185 GLY n 
1 186 PHE n 
1 187 LEU n 
1 188 LEU n 
1 189 GLU n 
1 190 LYS n 
1 191 GLU n 
1 192 LEU n 
1 193 LYS n 
1 194 TYR n 
1 195 PHE n 
1 196 GLY n 
1 197 LYS n 
1 198 ALA n 
1 199 LEU n 
1 200 GLU n 
1 201 ASN n 
1 202 PRO n 
1 203 THR n 
1 204 ARG n 
1 205 PRO n 
1 206 PHE n 
1 207 LEU n 
1 208 ALA n 
1 209 ILE n 
1 210 LEU n 
1 211 GLY n 
1 212 GLY n 
1 213 ALA n 
1 214 LYS n 
1 215 VAL n 
1 216 ALA n 
1 217 ASP n 
1 218 LYS n 
1 219 ILE n 
1 220 GLN n 
1 221 LEU n 
1 222 ILE n 
1 223 ASP n 
1 224 ASN n 
1 225 LEU n 
1 226 LEU n 
1 227 ASP n 
1 228 LYS n 
1 229 VAL n 
1 230 ASP n 
1 231 SER n 
1 232 ILE n 
1 233 ILE n 
1 234 ILE n 
1 235 GLY n 
1 236 GLY n 
1 237 GLY n 
1 238 MET n 
1 239 ALA n 
1 240 PHE n 
1 241 THR n 
1 242 PHE n 
1 243 LYS n 
1 244 LYS n 
1 245 VAL n 
1 246 LEU n 
1 247 GLU n 
1 248 ASN n 
1 249 THR n 
1 250 GLU n 
1 251 ILE n 
1 252 GLY n 
1 253 ASP n 
1 254 SER n 
1 255 ILE n 
1 256 PHE n 
1 257 ASP n 
1 258 LYS n 
1 259 ALA n 
1 260 VAL n 
1 261 GLY n 
1 262 PRO n 
1 263 GLU n 
1 264 ILE n 
1 265 ALA n 
1 266 LYS n 
1 267 LEU n 
1 268 MET n 
1 269 GLU n 
1 270 LYS n 
1 271 ALA n 
1 272 LYS n 
1 273 ALA n 
1 274 LYS n 
1 275 GLY n 
1 276 VAL n 
1 277 GLU n 
1 278 VAL n 
1 279 VAL n 
1 280 LEU n 
1 281 PRO n 
1 282 VAL n 
1 283 ASP n 
1 284 PHE n 
1 285 ILE n 
1 286 ILE n 
1 287 ALA n 
1 288 ASP n 
1 289 ALA n 
1 290 PHE n 
1 291 SER n 
1 292 ALA n 
1 293 SER n 
1 294 ALA n 
1 295 ASN n 
1 296 THR n 
1 297 LYS n 
1 298 THR n 
1 299 VAL n 
1 300 THR n 
1 301 ASP n 
1 302 LYS n 
1 303 GLU n 
1 304 GLY n 
1 305 ILE n 
1 306 PRO n 
1 307 ALA n 
1 308 GLY n 
1 309 TRP n 
1 310 GLN n 
1 311 GLY n 
1 312 LEU n 
1 313 ASP n 
1 314 ASN n 
1 315 GLY n 
1 316 PRO n 
1 317 GLU n 
1 318 SER n 
1 319 ARG n 
1 320 LYS n 
1 321 LEU n 
1 322 PHE n 
1 323 ALA n 
1 324 ALA n 
1 325 THR n 
1 326 VAL n 
1 327 ALA n 
1 328 LYS n 
1 329 ALA n 
1 330 THR n 
1 331 VAL n 
1 332 ILE n 
1 333 LEU n 
1 334 TRP n 
1 335 ASN n 
1 336 GLY n 
1 337 PRO n 
1 338 PRO n 
1 339 GLY n 
1 340 VAL n 
1 341 PHE n 
1 342 GLU n 
1 343 PHE n 
1 344 GLU n 
1 345 LYS n 
1 346 PHE n 
1 347 ALA n 
1 348 ALA n 
1 349 GLY n 
1 350 THR n 
1 351 LYS n 
1 352 ALA n 
1 353 LEU n 
1 354 LEU n 
1 355 ASP n 
1 356 GLU n 
1 357 VAL n 
1 358 VAL n 
1 359 LYS n 
1 360 SER n 
1 361 SER n 
1 362 ALA n 
1 363 ALA n 
1 364 GLY n 
1 365 ASN n 
1 366 THR n 
1 367 VAL n 
1 368 ILE n 
1 369 ILE n 
1 370 GLY n 
1 371 GLY n 
1 372 GLY n 
1 373 ASP n 
1 374 THR n 
1 375 ALA n 
1 376 THR n 
1 377 VAL n 
1 378 ALA n 
1 379 LYS n 
1 380 LYS n 
1 381 TYR n 
1 382 GLY n 
1 383 VAL n 
1 384 THR n 
1 385 ASP n 
1 386 LYS n 
1 387 ILE n 
1 388 SER n 
1 389 HIS n 
1 390 VAL n 
1 391 SER n 
1 392 THR n 
1 393 GLY n 
1 394 GLY n 
1 395 GLY n 
1 396 ALA n 
1 397 SER n 
1 398 LEU n 
1 399 GLU n 
1 400 LEU n 
1 401 LEU n 
1 402 GLU n 
1 403 GLY n 
1 404 LYS n 
1 405 GLU n 
1 406 LEU n 
1 407 PRO n 
1 408 GLY n 
1 409 VAL n 
1 410 ALA n 
1 411 PHE n 
1 412 LEU n 
1 413 SER n 
1 414 GLU n 
1 415 LYS n 
1 416 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               
;baker's yeast
;
_entity_src_gen.gene_src_genus                     Saccharomyces 
_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      'Saccharomyces cerevisiae' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     4932 
_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                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PGK_YEAST 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_db_accession          P00560 
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_seq_one_letter_code   
;SLSSKLSVQDLDLKDKRVFIRVDFNVPLDGKKITSNQRIVAALPTIKYVLEHHPRYVVLASHLGRPNGERNEKYSLAPVA
KELQSLLGKDVTFLNDCVGPEVEAAVKASAPGSVILLENLRYHIEEEGSRKVDGQKVKASKEDVQKFRHELSSLADVYIN
DAFGTAHRAHSSMVGFDLPQRAAGFLLEKELKYFGKALENPTRPFLAILGGAKVADKIQLIDNLLDKVDSIIIGGGMAFT
FKKVLENTEIGDSIFDKAGAEIVPKLMEKAKAKGVEVVLPVDFIIADAFSADANTKTVTDKEGIPAGWQGLDNGPESRKL
FAATVAKAKTIVWNGPPGVFEFEKFAAGTKALLDEVVKSSAAGNTVIIGGGDTATVAKKYGVTDKISHVSTGGGASLELL
EGKELPGVAFLSEKK
;
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              3PGK 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 416 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00560 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  415 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       415 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 3PGK VAL A 260 ? UNP P00560 ?   ?   INSERTION 259 1 
1 3PGK PRO A 262 ? UNP P00560 ALA 260 CONFLICT  261 2 
1 3PGK ?   A ?   ? UNP P00560 VAL 263 DELETION  ?   3 
1 3PGK ALA A 265 ? UNP P00560 PRO 264 CONFLICT  264 4 
1 3PGK SER A 293 ? UNP P00560 ASP 292 CONFLICT  292 5 
1 3PGK THR A 330 ? UNP P00560 LYS 329 CONFLICT  329 6 
1 3PGK VAL A 331 ? UNP P00560 THR 330 CONFLICT  330 7 
1 3PGK LEU A 333 ? UNP P00560 VAL 332 CONFLICT  332 8 
# 
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 
3PG non-polymer         . '3-PHOSPHOGLYCERIC ACID'    ? 'C3 H7 O7 P'        186.057 
ACE non-polymer         . 'ACETYL GROUP'              ? 'C2 H4 O'           44.053  
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 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O13 P3' 507.181 
CYS 'L-peptide linking' y CYSTEINE                    ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                   ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'             ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                     ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                   ? 'C6 H10 N3 O2 1'    156.162 
ILE 'L-peptide linking' y ISOLEUCINE                  ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                     ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                      ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                  ? 'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'             ? 'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE               ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                     ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                      ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                   ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                  ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                    ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                      ? 'C5 H11 N O2'       117.146 
# 
_exptl.entry_id          3PGK 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   ? 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.56 
_exptl_crystal.density_percent_sol   51.97 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           ? 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.pdbx_diffrn_protocol             ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   . 
_diffrn_radiation_wavelength.wt           1.0 
# 
_refine.entry_id                                 3PGK 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            2.5 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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_overall_ESU_R                       ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        3148 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         43 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               3191 
_refine_hist.d_res_high                       2.5 
_refine_hist.d_res_low                        . 
# 
_struct.entry_id                  3PGK 
_struct.title                     'The structure of yeast phosphoglycerate kinase at 0.25 nm resolution' 
_struct.pdbx_descriptor           'PHOSPHOGLYCERATE KINASE (E.C.2.7.2.3)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3PGK 
_struct_keywords.pdbx_keywords   TRANSFERASE 
_struct_keywords.text            'PHOSPHOTRANSFERASE(CARBOXYL AS ACCEPTOR), TRANSFERASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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  I   GLN A 38  ? GLU A 52  ? GLN A 37  GLU A 51  1 'PRO AT 44'         15 
HELX_P HELX_P2  II  ALA A 78  ? LEU A 88  ? ALA A 77  LEU A 87  1 ?                   11 
HELX_P HELX_P3  III PRO A 101 ? ALA A 109 ? PRO A 100 ALA A 108 1 'OPEN CARBOXYL END' 9  
HELX_P HELX_P4  IV  GLU A 143 ? SER A 153 ? GLU A 142 SER A 152 1 ?                   11 
HELX_P HELX_P5  V   PHE A 186 ? GLU A 200 ? PHE A 185 GLU A 199 1 'OPEN CARBOXYL END' 15 
HELX_P HELX_P6  VI  LYS A 218 ? ASP A 227 ? LYS A 217 ASP A 226 1 ?                   10 
HELX_P HELX_P7  VII MET A 238 ? LYS A 244 ? MET A 237 LYS A 243 1 ?                   7  
HELX_P HELX_P8  IIX GLU A 247 ? GLY A 252 ? GLU A 246 GLY A 251 1 'OPEN CARBOXYL END' 6  
HELX_P HELX_P9  IX  LYS A 258 ? LYS A 274 ? LYS A 257 LYS A 273 1 'PRO AT 261'        17 
HELX_P HELX_P10 X   PRO A 316 ? VAL A 326 ? PRO A 315 VAL A 325 1 ?                   11 
HELX_P HELX_P11 XI  GLY A 349 ? SER A 360 ? GLY A 348 SER A 359 1 ?                   12 
HELX_P HELX_P12 XII ASP A 373 ? TYR A 381 ? ASP A 372 TYR A 380 1 ?                   9  
HELX_P HELX_P13 XII GLY A 394 ? GLU A 402 ? GLY A 393 GLU A 401 1 ?                   9  
HELX_P HELX_P14 XIV PRO A 407 ? PHE A 411 ? PRO A 406 PHE A 410 1 ?                   5  
# 
_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 
metalc1 metalc ? ? B MG . MG ? ? ? 1_555 C ATP .   O3G ? ? A MG 416 A ATP 417 1_555 ? ? ? ? ? ? ? 3.035 ? 
metalc2 metalc ? ? B MG . MG ? ? ? 1_555 C ATP .   O2G ? ? A MG 416 A ATP 417 1_555 ? ? ? ? ? ? ? 2.365 ? 
metalc3 metalc ? ? B MG . MG ? ? ? 1_555 C ATP .   O1G ? ? A MG 416 A ATP 417 1_555 ? ? ? ? ? ? ? 2.431 ? 
metalc4 metalc ? ? B MG . MG ? ? ? 1_555 A ASP 373 OD1 ? ? A MG 416 A ASP 372 1_555 ? ? ? ? ? ? ? 2.319 ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
SHC ? 6 ? 
SHB ? 6 ? 
SH1 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
SHC 1 2 ? parallel      
SHC 2 3 ? parallel      
SHC 3 4 ? parallel      
SHC 4 5 ? parallel      
SHC 5 6 ? parallel      
SHB 1 2 ? parallel      
SHB 2 3 ? parallel      
SHB 3 4 ? parallel      
SHB 4 5 ? parallel      
SHB 5 6 ? parallel      
SH1 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
SHC 1 VAL A 92  ? PHE A 94  ? VAL A 91  PHE A 93  
SHC 2 SER A 114 ? LEU A 117 ? SER A 113 LEU A 116 
SHC 3 VAL A 59  ? LEU A 60  ? VAL A 58  LEU A 59  
SHC 4 ARG A 18  ? ARG A 22  ? ARG A 17  ARG A 21  
SHC 5 VAL A 158 ? ILE A 160 ? VAL A 157 ILE A 159 
SHC 6 ARG A 182 ? ALA A 184 ? ARG A 181 ALA A 183 
SHB 1 GLU A 277 ? LEU A 280 ? GLU A 276 LEU A 279 
SHB 2 ILE A 232 ? GLY A 236 ? ILE A 231 GLY A 235 
SHB 3 PHE A 206 ? LEU A 210 ? PHE A 205 LEU A 209 
SHB 4 ILE A 332 ? TRP A 334 ? ILE A 331 TRP A 333 
SHB 5 VAL A 367 ? ILE A 369 ? VAL A 366 ILE A 368 
SHB 6 SER A 388 ? VAL A 390 ? SER A 387 VAL A 389 
SH1 1 ASN A 295 ? VAL A 299 ? ASN A 294 VAL A 298 
SH1 2 ASP A 283 ? ALA A 287 ? ASP A 282 ALA A 286 
# 
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 
SHC 1 2 N THR A 93  ? N THR A 92  O SER A 114 ? O SER A 113 
SHC 2 3 N VAL A 115 ? N VAL A 114 O VAL A 58  ? O VAL A 57  
SHC 3 4 N VAL A 59  ? N VAL A 58  O VAL A 19  ? O VAL A 18  
SHC 4 5 N PHE A 20  ? N PHE A 19  O VAL A 158 ? O VAL A 157 
SHC 5 6 O TYR A 159 ? O TYR A 158 N ALA A 183 ? N ALA A 182 
SHB 1 2 O GLU A 277 ? O GLU A 276 N ILE A 233 ? N ILE A 232 
SHB 2 3 O ILE A 232 ? O ILE A 231 N ALA A 208 ? N ALA A 207 
SHB 3 4 N LEU A 207 ? N LEU A 206 O VAL A 331 ? O VAL A 330 
SHB 4 5 O ILE A 332 ? O ILE A 331 N ILE A 368 ? N ILE A 367 
SHB 5 6 O VAL A 367 ? O VAL A 366 N HIS A 389 ? N HIS A 388 
SH1 1 2 N THR A 296 ? N THR A 295 O ILE A 286 ? O ILE A 285 
# 
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 ? ? ? ? 2  'BINDING SITE FOR RESIDUE MG A 416'  
AC2 Software ? ? ? ? 23 'BINDING SITE FOR RESIDUE ATP A 417' 
AC3 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE 3PG A 418' 
# 
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 2  ASP A 373 ? ASP A 372 . ? 1_555 ? 
2  AC1 2  ATP C .   ? ATP A 417 . ? 1_555 ? 
3  AC2 23 GLY A 212 ? GLY A 211 . ? 1_555 ? 
4  AC2 23 ALA A 213 ? ALA A 212 . ? 1_555 ? 
5  AC2 23 LYS A 214 ? LYS A 213 . ? 1_555 ? 
6  AC2 23 LYS A 218 ? LYS A 217 . ? 1_555 ? 
7  AC2 23 ILE A 251 ? ILE A 250 . ? 2_656 ? 
8  AC2 23 ILE A 286 ? ILE A 285 . ? 2_656 ? 
9  AC2 23 LYS A 302 ? LYS A 301 . ? 2_656 ? 
10 AC2 23 GLU A 303 ? GLU A 302 . ? 2_656 ? 
11 AC2 23 GLY A 304 ? GLY A 303 . ? 2_656 ? 
12 AC2 23 PRO A 306 ? PRO A 305 . ? 2_656 ? 
13 AC2 23 ALA A 307 ? ALA A 306 . ? 2_656 ? 
14 AC2 23 GLN A 310 ? GLN A 309 . ? 2_656 ? 
15 AC2 23 LEU A 312 ? LEU A 311 . ? 1_555 ? 
16 AC2 23 ASP A 313 ? ASP A 312 . ? 1_555 ? 
17 AC2 23 ASN A 335 ? ASN A 334 . ? 1_555 ? 
18 AC2 23 GLY A 336 ? GLY A 335 . ? 1_555 ? 
19 AC2 23 PRO A 337 ? PRO A 336 . ? 1_555 ? 
20 AC2 23 GLY A 339 ? GLY A 338 . ? 1_555 ? 
21 AC2 23 VAL A 340 ? VAL A 339 . ? 1_555 ? 
22 AC2 23 GLU A 342 ? GLU A 341 . ? 1_555 ? 
23 AC2 23 ASP A 373 ? ASP A 372 . ? 1_555 ? 
24 AC2 23 MG  B .   ? MG  A 416 . ? 1_555 ? 
25 AC2 23 3PG D .   ? 3PG A 418 . ? 1_555 ? 
26 AC3 6  LYS A 6   ? LYS A 5   . ? 4_555 ? 
27 AC3 6  GLY A 371 ? GLY A 370 . ? 1_555 ? 
28 AC3 6  GLY A 393 ? GLY A 392 . ? 1_555 ? 
29 AC3 6  GLY A 394 ? GLY A 393 . ? 1_555 ? 
30 AC3 6  GLY A 395 ? GLY A 394 . ? 1_555 ? 
31 AC3 6  ATP C .   ? ATP A 417 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3PGK 
_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                    3PGK 
_atom_sites.fract_transf_matrix[1][1]   .007899 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   .007735 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   .018382 
_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]   .015050 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
_atom_sites_footnote.id     1 
_atom_sites_footnote.text   'THIS ATOM MAY BE MAGNESIUM OR MANGANESE.' 
# 
loop_
_atom_type.symbol 
C  
MG 
N  
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 
HETATM 1    C  C     . ACE A 1 1   ? 25.205 -25.176 6.140   1.00 0.00 ? 0   ACE A C     1 
HETATM 2    O  O     . ACE A 1 1   ? 24.345 -25.020 7.018   1.00 0.00 ? 0   ACE A O     1 
HETATM 3    C  CH3   . ACE A 1 1   ? 26.650 -25.400 6.500   1.00 0.00 ? 0   ACE A CH3   1 
ATOM   4    N  N     . SER A 1 2   ? 25.058 -25.183 4.822   1.00 0.00 ? 1   SER A N     1 
ATOM   5    C  CA    . SER A 1 2   ? 23.783 -24.986 4.139   1.00 0.00 ? 1   SER A CA    1 
ATOM   6    C  C     . SER A 1 2   ? 23.861 -25.489 2.690   1.00 0.00 ? 1   SER A C     1 
ATOM   7    O  O     . SER A 1 2   ? 22.835 -25.649 2.014   1.00 0.00 ? 1   SER A O     1 
ATOM   8    C  CB    . SER A 1 2   ? 23.423 -23.501 4.124   1.00 0.00 ? 1   SER A CB    1 
ATOM   9    O  OG    . SER A 1 2   ? 24.257 -22.808 3.206   1.00 0.00 ? 1   SER A OG    1 
ATOM   10   N  N     . LEU A 1 3   ? 25.077 -25.729 2.226   1.00 0.00 ? 2   LEU A N     1 
ATOM   11   C  CA    . LEU A 1 3   ? 25.290 -26.255 0.866   1.00 0.00 ? 2   LEU A CA    1 
ATOM   12   C  C     . LEU A 1 3   ? 26.484 -25.611 0.183   1.00 0.00 ? 2   LEU A C     1 
ATOM   13   O  O     . LEU A 1 3   ? 27.642 -25.867 0.545   1.00 0.00 ? 2   LEU A O     1 
ATOM   14   C  CB    . LEU A 1 3   ? 24.083 -25.951 -0.020  1.00 0.00 ? 2   LEU A CB    1 
ATOM   15   C  CG    . LEU A 1 3   ? 24.299 -26.387 -1.468  1.00 0.00 ? 2   LEU A CG    1 
ATOM   16   C  CD1   . LEU A 1 3   ? 24.122 -27.894 -1.669  1.00 0.00 ? 2   LEU A CD1   1 
ATOM   17   C  CD2   . LEU A 1 3   ? 23.329 -25.721 -2.446  1.00 0.00 ? 2   LEU A CD2   1 
ATOM   18   N  N     . SER A 1 4   ? 26.106 -24.804 -0.787  1.00 0.00 ? 3   SER A N     1 
ATOM   19   C  CA    . SER A 1 4   ? 27.026 -24.042 -1.628  1.00 0.00 ? 3   SER A CA    1 
ATOM   20   C  C     . SER A 1 4   ? 28.319 -24.827 -1.854  1.00 0.00 ? 3   SER A C     1 
ATOM   21   O  O     . SER A 1 4   ? 29.417 -24.362 -1.516  1.00 0.00 ? 3   SER A O     1 
ATOM   22   C  CB    . SER A 1 4   ? 27.355 -22.707 -0.956  1.00 0.00 ? 3   SER A CB    1 
ATOM   23   O  OG    . SER A 1 4   ? 26.157 -22.009 -0.650  1.00 0.00 ? 3   SER A OG    1 
ATOM   24   N  N     . SER A 1 5   ? 28.165 -26.013 -2.422  1.00 0.00 ? 4   SER A N     1 
ATOM   25   C  CA    . SER A 1 5   ? 29.318 -26.866 -2.733  1.00 0.00 ? 4   SER A CA    1 
ATOM   26   C  C     . SER A 1 5   ? 30.228 -26.123 -3.690  1.00 0.00 ? 4   SER A C     1 
ATOM   27   O  O     . SER A 1 5   ? 31.103 -25.350 -3.271  1.00 0.00 ? 4   SER A O     1 
ATOM   28   C  CB    . SER A 1 5   ? 28.877 -28.177 -3.393  1.00 0.00 ? 4   SER A CB    1 
ATOM   29   O  OG    . SER A 1 5   ? 27.467 -28.315 -3.309  1.00 0.00 ? 4   SER A OG    1 
ATOM   30   N  N     . LYS A 1 6   ? 29.983 -26.385 -4.947  1.00 0.00 ? 5   LYS A N     1 
ATOM   31   C  CA    . LYS A 1 6   ? 30.740 -25.777 -6.029  1.00 0.00 ? 5   LYS A CA    1 
ATOM   32   C  C     . LYS A 1 6   ? 29.797 -25.264 -7.087  1.00 0.00 ? 5   LYS A C     1 
ATOM   33   O  O     . LYS A 1 6   ? 29.665 -25.859 -8.167  1.00 0.00 ? 5   LYS A O     1 
ATOM   34   C  CB    . LYS A 1 6   ? 31.665 -26.806 -6.661  1.00 0.00 ? 5   LYS A CB    1 
ATOM   35   C  CG    . LYS A 1 6   ? 33.065 -26.777 -6.058  1.00 0.00 ? 5   LYS A CG    1 
ATOM   36   C  CD    . LYS A 1 6   ? 34.063 -27.634 -6.831  1.00 0.00 ? 5   LYS A CD    1 
ATOM   37   C  CE    . LYS A 1 6   ? 35.121 -28.270 -5.929  1.00 0.00 ? 5   LYS A CE    1 
ATOM   38   N  NZ    . LYS A 1 6   ? 36.171 -28.970 -6.682  1.00 0.00 ? 5   LYS A NZ    1 
ATOM   39   N  N     . LEU A 1 7   ? 29.158 -24.178 -6.754  1.00 0.00 ? 6   LEU A N     1 
ATOM   40   C  CA    . LEU A 1 7   ? 28.247 -23.542 -7.684  1.00 0.00 ? 6   LEU A CA    1 
ATOM   41   C  C     . LEU A 1 7   ? 29.030 -23.263 -8.962  1.00 0.00 ? 6   LEU A C     1 
ATOM   42   O  O     . LEU A 1 7   ? 29.350 -24.183 -9.729  1.00 0.00 ? 6   LEU A O     1 
ATOM   43   C  CB    . LEU A 1 7   ? 27.638 -22.308 -7.041  1.00 0.00 ? 6   LEU A CB    1 
ATOM   44   C  CG    . LEU A 1 7   ? 26.467 -22.671 -6.124  1.00 0.00 ? 6   LEU A CG    1 
ATOM   45   C  CD1   . LEU A 1 7   ? 26.207 -21.622 -5.041  1.00 0.00 ? 6   LEU A CD1   1 
ATOM   46   C  CD2   . LEU A 1 7   ? 25.144 -22.828 -6.876  1.00 0.00 ? 6   LEU A CD2   1 
ATOM   47   N  N     . SER A 1 8   ? 29.358 -22.021 -9.232  1.00 0.00 ? 7   SER A N     1 
ATOM   48   C  CA    . SER A 1 8   ? 30.115 -21.735 -10.461 1.00 0.00 ? 7   SER A CA    1 
ATOM   49   C  C     . SER A 1 8   ? 30.698 -20.337 -10.469 1.00 0.00 ? 7   SER A C     1 
ATOM   50   O  O     . SER A 1 8   ? 30.084 -19.386 -9.960  1.00 0.00 ? 7   SER A O     1 
ATOM   51   C  CB    . SER A 1 8   ? 29.224 -21.896 -11.691 1.00 0.00 ? 7   SER A CB    1 
ATOM   52   O  OG    . SER A 1 8   ? 27.979 -21.248 -11.478 1.00 0.00 ? 7   SER A OG    1 
ATOM   53   N  N     . VAL A 1 9   ? 31.871 -20.299 -11.067 1.00 0.00 ? 8   VAL A N     1 
ATOM   54   C  CA    . VAL A 1 9   ? 32.666 -19.085 -11.159 1.00 0.00 ? 8   VAL A CA    1 
ATOM   55   C  C     . VAL A 1 9   ? 33.744 -19.220 -12.221 1.00 0.00 ? 8   VAL A C     1 
ATOM   56   O  O     . VAL A 1 9   ? 34.310 -20.305 -12.425 1.00 0.00 ? 8   VAL A O     1 
ATOM   57   C  CB    . VAL A 1 9   ? 33.349 -18.838 -9.816  1.00 0.00 ? 8   VAL A CB    1 
ATOM   58   C  CG1   . VAL A 1 9   ? 34.198 -17.566 -9.801  1.00 0.00 ? 8   VAL A CG1   1 
ATOM   59   C  CG2   . VAL A 1 9   ? 32.358 -18.690 -8.661  1.00 0.00 ? 8   VAL A CG2   1 
ATOM   60   N  N     . GLN A 1 10  ? 33.987 -18.100 -12.864 1.00 0.00 ? 9   GLN A N     1 
ATOM   61   C  CA    . GLN A 1 10  ? 35.016 -18.027 -13.881 1.00 0.00 ? 9   GLN A CA    1 
ATOM   62   C  C     . GLN A 1 10  ? 34.882 -19.264 -14.763 1.00 0.00 ? 9   GLN A C     1 
ATOM   63   O  O     . GLN A 1 10  ? 35.851 -19.700 -15.403 1.00 0.00 ? 9   GLN A O     1 
ATOM   64   C  CB    . GLN A 1 10  ? 36.372 -18.021 -13.161 1.00 0.00 ? 9   GLN A CB    1 
ATOM   65   C  CG    . GLN A 1 10  ? 36.468 -19.110 -12.077 1.00 0.00 ? 9   GLN A CG    1 
ATOM   66   C  CD    . GLN A 1 10  ? 36.753 -18.563 -10.671 1.00 0.00 ? 9   GLN A CD    1 
ATOM   67   O  OE1   . GLN A 1 10  ? 35.875 -17.962 -10.054 1.00 0.00 ? 9   GLN A OE1   1 
ATOM   68   N  NE2   . GLN A 1 10  ? 37.942 -18.737 -10.124 1.00 0.00 ? 9   GLN A NE2   1 
ATOM   69   N  N     . ASP A 1 11  ? 33.655 -19.764 -14.737 1.00 0.00 ? 10  ASP A N     1 
ATOM   70   C  CA    . ASP A 1 11  ? 33.240 -20.962 -15.475 1.00 0.00 ? 10  ASP A CA    1 
ATOM   71   C  C     . ASP A 1 11  ? 32.436 -20.569 -16.717 1.00 0.00 ? 10  ASP A C     1 
ATOM   72   O  O     . ASP A 1 11  ? 32.553 -21.199 -17.778 1.00 0.00 ? 10  ASP A O     1 
ATOM   73   C  CB    . ASP A 1 11  ? 32.388 -21.853 -14.572 1.00 0.00 ? 10  ASP A CB    1 
ATOM   74   C  CG    . ASP A 1 11  ? 33.223 -22.617 -13.543 1.00 0.00 ? 10  ASP A CG    1 
ATOM   75   O  OD1   . ASP A 1 11  ? 32.665 -23.089 -12.481 1.00 0.00 ? 10  ASP A OD1   1 
ATOM   76   O  OD2   . ASP A 1 11  ? 34.487 -22.789 -13.739 1.00 0.00 ? 10  ASP A OD2   1 
ATOM   77   N  N     . LEU A 1 12  ? 31.629 -19.536 -16.561 1.00 0.00 ? 11  LEU A N     1 
ATOM   78   C  CA    . LEU A 1 12  ? 30.828 -19.010 -17.673 1.00 0.00 ? 11  LEU A CA    1 
ATOM   79   C  C     . LEU A 1 12  ? 31.787 -18.554 -18.775 1.00 0.00 ? 11  LEU A C     1 
ATOM   80   O  O     . LEU A 1 12  ? 32.708 -17.760 -18.532 1.00 0.00 ? 11  LEU A O     1 
ATOM   81   C  CB    . LEU A 1 12  ? 29.966 -17.838 -17.195 1.00 0.00 ? 11  LEU A CB    1 
ATOM   82   C  CG    . LEU A 1 12  ? 28.637 -18.287 -16.579 1.00 0.00 ? 11  LEU A CG    1 
ATOM   83   C  CD1   . LEU A 1 12  ? 27.916 -17.164 -15.831 1.00 0.00 ? 11  LEU A CD1   1 
ATOM   84   C  CD2   . LEU A 1 12  ? 27.639 -18.801 -17.618 1.00 0.00 ? 11  LEU A CD2   1 
ATOM   85   N  N     . ASP A 1 13  ? 31.534 -19.074 -19.958 1.00 0.00 ? 12  ASP A N     1 
ATOM   86   C  CA    . ASP A 1 13  ? 32.365 -18.819 -21.144 1.00 0.00 ? 12  ASP A CA    1 
ATOM   87   C  C     . ASP A 1 13  ? 31.943 -17.541 -21.869 1.00 0.00 ? 12  ASP A C     1 
ATOM   88   O  O     . ASP A 1 13  ? 32.732 -16.937 -22.612 1.00 0.00 ? 12  ASP A O     1 
ATOM   89   C  CB    . ASP A 1 13  ? 32.224 -19.975 -22.129 1.00 0.00 ? 12  ASP A CB    1 
ATOM   90   C  CG    . ASP A 1 13  ? 30.764 -20.298 -22.451 1.00 0.00 ? 12  ASP A CG    1 
ATOM   91   O  OD1   . ASP A 1 13  ? 29.827 -19.503 -22.059 1.00 0.00 ? 12  ASP A OD1   1 
ATOM   92   O  OD2   . ASP A 1 13  ? 30.470 -21.364 -23.114 1.00 0.00 ? 12  ASP A OD2   1 
ATOM   93   N  N     . LEU A 1 14  ? 30.707 -17.154 -21.641 1.00 0.00 ? 13  LEU A N     1 
ATOM   94   C  CA    . LEU A 1 14  ? 30.135 -15.966 -22.286 1.00 0.00 ? 13  LEU A CA    1 
ATOM   95   C  C     . LEU A 1 14  ? 30.256 -16.123 -23.809 1.00 0.00 ? 13  LEU A C     1 
ATOM   96   O  O     . LEU A 1 14  ? 29.906 -17.171 -24.372 1.00 0.00 ? 13  LEU A O     1 
ATOM   97   C  CB    . LEU A 1 14  ? 30.881 -14.712 -21.820 1.00 0.00 ? 13  LEU A CB    1 
ATOM   98   C  CG    . LEU A 1 14  ? 30.776 -14.481 -20.309 1.00 0.00 ? 13  LEU A CG    1 
ATOM   99   C  CD1   . LEU A 1 14  ? 30.969 -13.015 -19.913 1.00 0.00 ? 13  LEU A CD1   1 
ATOM   100  C  CD2   . LEU A 1 14  ? 29.418 -14.890 -19.734 1.00 0.00 ? 13  LEU A CD2   1 
ATOM   101  N  N     . LYS A 1 15  ? 30.750 -15.077 -24.444 1.00 0.00 ? 14  LYS A N     1 
ATOM   102  C  CA    . LYS A 1 15  ? 30.933 -15.048 -25.906 1.00 0.00 ? 14  LYS A CA    1 
ATOM   103  C  C     . LYS A 1 15  ? 29.618 -14.680 -26.595 1.00 0.00 ? 14  LYS A C     1 
ATOM   104  O  O     . LYS A 1 15  ? 28.756 -15.541 -26.825 1.00 0.00 ? 14  LYS A O     1 
ATOM   105  C  CB    . LYS A 1 15  ? 31.367 -16.424 -26.414 1.00 0.00 ? 14  LYS A CB    1 
ATOM   106  C  CG    . LYS A 1 15  ? 32.461 -17.059 -25.556 1.00 0.00 ? 14  LYS A CG    1 
ATOM   107  C  CD    . LYS A 1 15  ? 33.871 -16.708 -26.032 1.00 0.00 ? 14  LYS A CD    1 
ATOM   108  C  CE    . LYS A 1 15  ? 34.913 -17.754 -25.634 1.00 0.00 ? 14  LYS A CE    1 
ATOM   109  N  NZ    . LYS A 1 15  ? 36.280 -17.380 -26.024 1.00 0.00 ? 14  LYS A NZ    1 
ATOM   110  N  N     . ASP A 1 16  ? 29.511 -13.404 -26.904 1.00 0.00 ? 15  ASP A N     1 
ATOM   111  C  CA    . ASP A 1 16  ? 28.329 -12.841 -27.566 1.00 0.00 ? 15  ASP A CA    1 
ATOM   112  C  C     . ASP A 1 16  ? 27.070 -13.319 -26.873 1.00 0.00 ? 15  ASP A C     1 
ATOM   113  O  O     . ASP A 1 16  ? 26.051 -13.599 -27.522 1.00 0.00 ? 15  ASP A O     1 
ATOM   114  C  CB    . ASP A 1 16  ? 28.274 -13.286 -29.024 1.00 0.00 ? 15  ASP A CB    1 
ATOM   115  C  CG    . ASP A 1 16  ? 27.468 -12.330 -29.905 1.00 0.00 ? 15  ASP A CG    1 
ATOM   116  O  OD1   . ASP A 1 16  ? 27.080 -11.193 -29.436 1.00 0.00 ? 15  ASP A OD1   1 
ATOM   117  O  OD2   . ASP A 1 16  ? 27.177 -12.660 -31.118 1.00 0.00 ? 15  ASP A OD2   1 
ATOM   118  N  N     . LYS A 1 17  ? 27.199 -13.397 -25.577 1.00 0.00 ? 16  LYS A N     1 
ATOM   119  C  CA    . LYS A 1 17  ? 26.115 -13.802 -24.702 1.00 0.00 ? 16  LYS A CA    1 
ATOM   120  C  C     . LYS A 1 17  ? 25.653 -12.577 -23.922 1.00 0.00 ? 16  LYS A C     1 
ATOM   121  O  O     . LYS A 1 17  ? 26.284 -11.511 -23.976 1.00 0.00 ? 16  LYS A O     1 
ATOM   122  C  CB    . LYS A 1 17  ? 26.596 -14.924 -23.788 1.00 0.00 ? 16  LYS A CB    1 
ATOM   123  C  CG    . LYS A 1 17  ? 26.982 -16.188 -24.560 1.00 0.00 ? 16  LYS A CG    1 
ATOM   124  C  CD    . LYS A 1 17  ? 26.733 -17.472 -23.764 1.00 0.00 ? 16  LYS A CD    1 
ATOM   125  C  CE    . LYS A 1 17  ? 26.790 -18.733 -24.628 1.00 0.00 ? 16  LYS A CE    1 
ATOM   126  N  NZ    . LYS A 1 17  ? 27.171 -19.932 -23.869 1.00 0.00 ? 16  LYS A NZ    1 
ATOM   127  N  N     . ARG A 1 18  ? 24.570 -12.779 -23.218 1.00 0.00 ? 17  ARG A N     1 
ATOM   128  C  CA    . ARG A 1 18  ? 23.883 -11.725 -22.472 1.00 0.00 ? 17  ARG A CA    1 
ATOM   129  C  C     . ARG A 1 18  ? 23.945 -12.023 -20.985 1.00 0.00 ? 17  ARG A C     1 
ATOM   130  O  O     . ARG A 1 18  ? 23.410 -13.038 -20.515 1.00 0.00 ? 17  ARG A O     1 
ATOM   131  C  CB    . ARG A 1 18  ? 22.432 -11.622 -22.928 1.00 0.00 ? 17  ARG A CB    1 
ATOM   132  C  CG    . ARG A 1 18  ? 22.289 -10.910 -24.272 1.00 0.00 ? 17  ARG A CG    1 
ATOM   133  C  CD    . ARG A 1 18  ? 21.262 -11.571 -25.188 1.00 0.00 ? 17  ARG A CD    1 
ATOM   134  N  NE    . ARG A 1 18  ? 19.884 -11.170 -24.878 1.00 0.00 ? 17  ARG A NE    1 
ATOM   135  C  CZ    . ARG A 1 18  ? 18.874 -11.224 -25.754 1.00 0.00 ? 17  ARG A CZ    1 
ATOM   136  N  NH1   . ARG A 1 18  ? 19.069 -11.663 -27.005 1.00 0.00 ? 17  ARG A NH1   1 
ATOM   137  N  NH2   . ARG A 1 18  ? 17.617 -10.857 -25.472 1.00 0.00 ? 17  ARG A NH2   1 
ATOM   138  N  N     . VAL A 1 19  ? 24.617 -11.078 -20.351 1.00 0.00 ? 18  VAL A N     1 
ATOM   139  C  CA    . VAL A 1 19  ? 24.967 -11.091 -18.923 1.00 0.00 ? 18  VAL A CA    1 
ATOM   140  C  C     . VAL A 1 19  ? 24.372 -9.930  -18.103 1.00 0.00 ? 18  VAL A C     1 
ATOM   141  O  O     . VAL A 1 19  ? 24.605 -8.750  -18.406 1.00 0.00 ? 18  VAL A O     1 
ATOM   142  C  CB    . VAL A 1 19  ? 26.476 -11.025 -18.735 1.00 0.00 ? 18  VAL A CB    1 
ATOM   143  C  CG1   . VAL A 1 19  ? 27.166 -12.367 -18.989 1.00 0.00 ? 18  VAL A CG1   1 
ATOM   144  C  CG2   . VAL A 1 19  ? 27.152 -10.025 -19.674 1.00 0.00 ? 18  VAL A CG2   1 
ATOM   145  N  N     . PHE A 1 20  ? 23.620 -10.377 -17.107 1.00 0.00 ? 19  PHE A N     1 
ATOM   146  C  CA    . PHE A 1 20  ? 22.983 -9.552  -16.059 1.00 0.00 ? 19  PHE A CA    1 
ATOM   147  C  C     . PHE A 1 20  ? 23.573 -9.936  -14.686 1.00 0.00 ? 19  PHE A C     1 
ATOM   148  O  O     . PHE A 1 20  ? 23.489 -11.096 -14.255 1.00 0.00 ? 19  PHE A O     1 
ATOM   149  C  CB    . PHE A 1 20  ? 21.475 -9.764  -16.004 1.00 0.00 ? 19  PHE A CB    1 
ATOM   150  C  CG    . PHE A 1 20  ? 20.760 -8.654  -15.222 1.00 0.00 ? 19  PHE A CG    1 
ATOM   151  C  CD1   . PHE A 1 20  ? 20.353 -7.487  -15.879 1.00 0.00 ? 19  PHE A CD1   1 
ATOM   152  C  CD2   . PHE A 1 20  ? 20.515 -8.802  -13.849 1.00 0.00 ? 19  PHE A CD2   1 
ATOM   153  C  CE1   . PHE A 1 20  ? 19.693 -6.475  -15.171 1.00 0.00 ? 19  PHE A CE1   1 
ATOM   154  C  CE2   . PHE A 1 20  ? 19.855 -7.788  -13.140 1.00 0.00 ? 19  PHE A CE2   1 
ATOM   155  C  CZ    . PHE A 1 20  ? 19.442 -6.626  -13.802 1.00 0.00 ? 19  PHE A CZ    1 
ATOM   156  N  N     . ILE A 1 21  ? 24.160 -8.935  -14.045 1.00 0.00 ? 20  ILE A N     1 
ATOM   157  C  CA    . ILE A 1 21  ? 24.880 -9.086  -12.755 1.00 0.00 ? 20  ILE A CA    1 
ATOM   158  C  C     . ILE A 1 21  ? 24.253 -8.303  -11.579 1.00 0.00 ? 20  ILE A C     1 
ATOM   159  O  O     . ILE A 1 21  ? 24.126 -7.070  -11.626 1.00 0.00 ? 20  ILE A O     1 
ATOM   160  C  CB    . ILE A 1 21  ? 26.303 -8.563  -12.880 1.00 0.00 ? 20  ILE A CB    1 
ATOM   161  C  CG1   . ILE A 1 21  ? 26.354 -7.065  -13.181 1.00 0.00 ? 20  ILE A CG1   1 
ATOM   162  C  CG2   . ILE A 1 21  ? 27.093 -9.244  -13.999 1.00 0.00 ? 20  ILE A CG2   1 
ATOM   163  C  CD1   . ILE A 1 21  ? 27.781 -6.522  -13.267 1.00 0.00 ? 20  ILE A CD1   1 
ATOM   164  N  N     . ARG A 1 22  ? 23.860 -9.058  -10.554 1.00 0.00 ? 21  ARG A N     1 
ATOM   165  C  CA    . ARG A 1 22  ? 23.341 -8.504  -9.278  1.00 0.00 ? 21  ARG A CA    1 
ATOM   166  C  C     . ARG A 1 22  ? 24.525 -8.320  -8.281  1.00 0.00 ? 21  ARG A C     1 
ATOM   167  O  O     . ARG A 1 22  ? 24.826 -9.213  -7.474  1.00 0.00 ? 21  ARG A O     1 
ATOM   168  C  CB    . ARG A 1 22  ? 22.282 -9.452  -8.709  1.00 0.00 ? 21  ARG A CB    1 
ATOM   169  C  CG    . ARG A 1 22  ? 22.633 -9.987  -7.323  1.00 0.00 ? 21  ARG A CG    1 
ATOM   170  C  CD    . ARG A 1 22  ? 22.495 -8.933  -6.224  1.00 0.00 ? 21  ARG A CD    1 
ATOM   171  N  NE    . ARG A 1 22  ? 21.233 -8.182  -6.298  1.00 0.00 ? 21  ARG A NE    1 
ATOM   172  C  CZ    . ARG A 1 22  ? 21.003 -7.044  -5.630  1.00 0.00 ? 21  ARG A CZ    1 
ATOM   173  N  NH1   . ARG A 1 22  ? 21.940 -6.510  -4.835  1.00 0.00 ? 21  ARG A NH1   1 
ATOM   174  N  NH2   . ARG A 1 22  ? 19.854 -6.357  -5.693  1.00 0.00 ? 21  ARG A NH2   1 
ATOM   175  N  N     . VAL A 1 23  ? 25.139 -7.133  -8.390  1.00 0.00 ? 22  VAL A N     1 
ATOM   176  C  CA    . VAL A 1 23  ? 26.355 -6.717  -7.627  1.00 0.00 ? 22  VAL A CA    1 
ATOM   177  C  C     . VAL A 1 23  ? 26.026 -5.981  -6.328  1.00 0.00 ? 22  VAL A C     1 
ATOM   178  O  O     . VAL A 1 23  ? 24.871 -5.961  -5.879  1.00 0.00 ? 22  VAL A O     1 
ATOM   179  C  CB    . VAL A 1 23  ? 27.175 -5.750  -8.482  1.00 0.00 ? 22  VAL A CB    1 
ATOM   180  C  CG1   . VAL A 1 23  ? 27.539 -6.324  -9.852  1.00 0.00 ? 22  VAL A CG1   1 
ATOM   181  C  CG2   . VAL A 1 23  ? 26.443 -4.436  -8.765  1.00 0.00 ? 22  VAL A CG2   1 
ATOM   182  N  N     . ASP A 1 24  ? 27.101 -5.411  -5.800  1.00 0.00 ? 23  ASP A N     1 
ATOM   183  C  CA    . ASP A 1 24  ? 27.100 -4.622  -4.563  1.00 0.00 ? 23  ASP A CA    1 
ATOM   184  C  C     . ASP A 1 24  ? 27.171 -3.138  -4.911  1.00 0.00 ? 23  ASP A C     1 
ATOM   185  O  O     . ASP A 1 24  ? 28.257 -2.539  -4.936  1.00 0.00 ? 23  ASP A O     1 
ATOM   186  C  CB    . ASP A 1 24  ? 28.328 -4.981  -3.720  1.00 0.00 ? 23  ASP A CB    1 
ATOM   187  C  CG    . ASP A 1 24  ? 27.973 -5.600  -2.369  1.00 0.00 ? 23  ASP A CG    1 
ATOM   188  O  OD1   . ASP A 1 24  ? 28.851 -6.293  -1.726  1.00 0.00 ? 23  ASP A OD1   1 
ATOM   189  O  OD2   . ASP A 1 24  ? 26.796 -5.429  -1.870  1.00 0.00 ? 23  ASP A OD2   1 
ATOM   190  N  N     . PHE A 1 25  ? 26.007 -2.579  -5.169  1.00 0.00 ? 24  PHE A N     1 
ATOM   191  C  CA    . PHE A 1 25  ? 25.891 -1.165  -5.543  1.00 0.00 ? 24  PHE A CA    1 
ATOM   192  C  C     . PHE A 1 25  ? 25.025 -0.403  -4.534  1.00 0.00 ? 24  PHE A C     1 
ATOM   193  O  O     . PHE A 1 25  ? 23.845 -0.122  -4.789  1.00 0.00 ? 24  PHE A O     1 
ATOM   194  C  CB    . PHE A 1 25  ? 25.294 -1.042  -6.944  1.00 0.00 ? 24  PHE A CB    1 
ATOM   195  C  CG    . PHE A 1 25  ? 26.367 -0.835  -8.017  1.00 0.00 ? 24  PHE A CG    1 
ATOM   196  C  CD1   . PHE A 1 25  ? 27.038 0.391   -8.107  1.00 0.00 ? 24  PHE A CD1   1 
ATOM   197  C  CD2   . PHE A 1 25  ? 26.682 -1.870  -8.905  1.00 0.00 ? 24  PHE A CD2   1 
ATOM   198  C  CE1   . PHE A 1 25  ? 28.023 0.581   -9.084  1.00 0.00 ? 24  PHE A CE1   1 
ATOM   199  C  CE2   . PHE A 1 25  ? 27.668 -1.680  -9.882  1.00 0.00 ? 24  PHE A CE2   1 
ATOM   200  C  CZ    . PHE A 1 25  ? 28.338 -0.455  -9.971  1.00 0.00 ? 24  PHE A CZ    1 
ATOM   201  N  N     . ASN A 1 26  ? 25.673 -0.108  -3.419  1.00 0.00 ? 25  ASN A N     1 
ATOM   202  C  CA    . ASN A 1 26  ? 25.101 0.669   -2.306  1.00 0.00 ? 25  ASN A CA    1 
ATOM   203  C  C     . ASN A 1 26  ? 26.200 1.569   -1.738  1.00 0.00 ? 25  ASN A C     1 
ATOM   204  O  O     . ASN A 1 26  ? 27.305 1.105   -1.420  1.00 0.00 ? 25  ASN A O     1 
ATOM   205  C  CB    . ASN A 1 26  ? 24.588 -0.258  -1.196  1.00 0.00 ? 25  ASN A CB    1 
ATOM   206  C  CG    . ASN A 1 26  ? 24.555 -1.733  -1.598  1.00 0.00 ? 25  ASN A CG    1 
ATOM   207  O  OD1   . ASN A 1 26  ? 23.488 -2.263  -1.903  1.00 0.00 ? 25  ASN A OD1   1 
ATOM   208  N  ND2   . ASN A 1 26  ? 25.671 -2.437  -1.616  1.00 0.00 ? 25  ASN A ND2   1 
ATOM   209  N  N     . VAL A 1 27  ? 25.878 2.846   -1.618  1.00 0.00 ? 26  VAL A N     1 
ATOM   210  C  CA    . VAL A 1 27  ? 26.848 3.839   -1.128  1.00 0.00 ? 26  VAL A CA    1 
ATOM   211  C  C     . VAL A 1 27  ? 26.177 4.990   -0.383  1.00 0.00 ? 26  VAL A C     1 
ATOM   212  O  O     . VAL A 1 27  ? 24.942 5.073   -0.316  1.00 0.00 ? 26  VAL A O     1 
ATOM   213  C  CB    . VAL A 1 27  ? 27.602 4.459   -2.306  1.00 0.00 ? 26  VAL A CB    1 
ATOM   214  C  CG1   . VAL A 1 27  ? 28.787 3.610   -2.770  1.00 0.00 ? 26  VAL A CG1   1 
ATOM   215  C  CG2   . VAL A 1 27  ? 26.723 4.655   -3.542  1.00 0.00 ? 26  VAL A CG2   1 
ATOM   216  N  N     . PRO A 1 28  ? 26.980 5.909   0.194   1.00 0.00 ? 27  PRO A N     1 
ATOM   217  C  CA    . PRO A 1 28  ? 26.441 7.062   0.892   1.00 0.00 ? 27  PRO A CA    1 
ATOM   218  C  C     . PRO A 1 28  ? 25.546 7.805   -0.062  1.00 0.00 ? 27  PRO A C     1 
ATOM   219  O  O     . PRO A 1 28  ? 25.304 7.298   -1.201  1.00 0.00 ? 27  PRO A O     1 
ATOM   220  C  CB    . PRO A 1 28  ? 27.667 7.819   1.342   1.00 0.00 ? 27  PRO A CB    1 
ATOM   221  C  CG    . PRO A 1 28  ? 28.892 7.043   0.880   1.00 0.00 ? 27  PRO A CG    1 
ATOM   222  C  CD    . PRO A 1 28  ? 28.439 5.816   0.154   1.00 0.00 ? 27  PRO A CD    1 
ATOM   223  N  N     . LEU A 1 29  ? 25.067 8.976   0.345   1.00 0.00 ? 28  LEU A N     1 
ATOM   224  C  CA    . LEU A 1 29  ? 24.066 9.689   -0.477  1.00 0.00 ? 28  LEU A CA    1 
ATOM   225  C  C     . LEU A 1 29  ? 24.314 11.190  -0.698  1.00 0.00 ? 28  LEU A C     1 
ATOM   226  O  O     . LEU A 1 29  ? 23.381 11.958  -0.975  1.00 0.00 ? 28  LEU A O     1 
ATOM   227  C  CB    . LEU A 1 29  ? 22.698 9.604   0.200   1.00 0.00 ? 28  LEU A CB    1 
ATOM   228  C  CG    . LEU A 1 29  ? 22.786 9.162   1.665   1.00 0.00 ? 28  LEU A CG    1 
ATOM   229  C  CD1   . LEU A 1 29  ? 23.850 9.925   2.457   1.00 0.00 ? 28  LEU A CD1   1 
ATOM   230  C  CD2   . LEU A 1 29  ? 21.476 9.364   2.431   1.00 0.00 ? 28  LEU A CD2   1 
ATOM   231  N  N     . ASP A 1 30  ? 25.533 11.649  -0.591  1.00 0.00 ? 29  ASP A N     1 
ATOM   232  C  CA    . ASP A 1 30  ? 25.803 13.083  -0.824  1.00 0.00 ? 29  ASP A CA    1 
ATOM   233  C  C     . ASP A 1 30  ? 25.707 13.373  -2.329  1.00 0.00 ? 29  ASP A C     1 
ATOM   234  O  O     . ASP A 1 30  ? 25.917 12.483  -3.165  1.00 0.00 ? 29  ASP A O     1 
ATOM   235  C  CB    . ASP A 1 30  ? 27.189 13.445  -0.298  1.00 0.00 ? 29  ASP A CB    1 
ATOM   236  C  CG    . ASP A 1 30  ? 27.250 13.466  1.231   1.00 0.00 ? 29  ASP A CG    1 
ATOM   237  O  OD1   . ASP A 1 30  ? 28.389 13.547  1.830   1.00 0.00 ? 29  ASP A OD1   1 
ATOM   238  O  OD2   . ASP A 1 30  ? 26.161 13.403  1.920   1.00 0.00 ? 29  ASP A OD2   1 
ATOM   239  N  N     . GLY A 1 31  ? 25.384 14.623  -2.637  1.00 0.00 ? 30  GLY A N     1 
ATOM   240  C  CA    . GLY A 1 31  ? 25.228 15.076  -4.028  1.00 0.00 ? 30  GLY A CA    1 
ATOM   241  C  C     . GLY A 1 31  ? 25.256 13.858  -4.949  1.00 0.00 ? 30  GLY A C     1 
ATOM   242  O  O     . GLY A 1 31  ? 24.205 13.353  -5.372  1.00 0.00 ? 30  GLY A O     1 
ATOM   243  N  N     . LYS A 1 32  ? 26.472 13.448  -5.217  1.00 0.00 ? 31  LYS A N     1 
ATOM   244  C  CA    . LYS A 1 32  ? 26.788 12.271  -6.027  1.00 0.00 ? 31  LYS A CA    1 
ATOM   245  C  C     . LYS A 1 32  ? 28.028 11.636  -5.420  1.00 0.00 ? 31  LYS A C     1 
ATOM   246  O  O     . LYS A 1 32  ? 28.177 10.405  -5.412  1.00 0.00 ? 31  LYS A O     1 
ATOM   247  C  CB    . LYS A 1 32  ? 27.056 12.682  -7.476  1.00 0.00 ? 31  LYS A CB    1 
ATOM   248  C  CG    . LYS A 1 32  ? 27.768 14.032  -7.596  1.00 0.00 ? 31  LYS A CG    1 
ATOM   249  C  CD    . LYS A 1 32  ? 27.515 14.722  -8.939  1.00 0.00 ? 31  LYS A CD    1 
ATOM   250  C  CE    . LYS A 1 32  ? 28.692 15.584  -9.400  1.00 0.00 ? 31  LYS A CE    1 
ATOM   251  N  NZ    . LYS A 1 32  ? 28.481 16.182  -10.726 1.00 0.00 ? 31  LYS A NZ    1 
ATOM   252  N  N     . LYS A 1 33  ? 28.861 12.549  -4.936  1.00 0.00 ? 32  LYS A N     1 
ATOM   253  C  CA    . LYS A 1 33  ? 30.112 12.222  -4.260  1.00 0.00 ? 32  LYS A CA    1 
ATOM   254  C  C     . LYS A 1 33  ? 29.882 11.000  -3.406  1.00 0.00 ? 32  LYS A C     1 
ATOM   255  O  O     . LYS A 1 33  ? 29.467 11.102  -2.243  1.00 0.00 ? 32  LYS A O     1 
ATOM   256  C  CB    . LYS A 1 33  ? 30.540 13.383  -3.364  1.00 0.00 ? 32  LYS A CB    1 
ATOM   257  C  CG    . LYS A 1 33  ? 31.177 14.533  -4.141  1.00 0.00 ? 32  LYS A CG    1 
ATOM   258  C  CD    . LYS A 1 33  ? 32.626 14.253  -4.542  1.00 0.00 ? 32  LYS A CD    1 
ATOM   259  C  CE    . LYS A 1 33  ? 32.869 14.401  -6.045  1.00 0.00 ? 32  LYS A CE    1 
ATOM   260  N  NZ    . LYS A 1 33  ? 34.203 13.944  -6.458  1.00 0.00 ? 32  LYS A NZ    1 
ATOM   261  N  N     . ILE A 1 34  ? 30.160 9.897   -4.023  1.00 0.00 ? 33  ILE A N     1 
ATOM   262  C  CA    . ILE A 1 34  ? 29.976 8.591   -3.423  1.00 0.00 ? 33  ILE A CA    1 
ATOM   263  C  C     . ILE A 1 34  ? 31.062 8.332   -2.376  1.00 0.00 ? 33  ILE A C     1 
ATOM   264  O  O     . ILE A 1 34  ? 32.196 7.959   -2.709  1.00 0.00 ? 33  ILE A O     1 
ATOM   265  C  CB    . ILE A 1 34  ? 30.019 7.551   -4.535  1.00 0.00 ? 33  ILE A CB    1 
ATOM   266  C  CG1   . ILE A 1 34  ? 31.107 7.842   -5.571  1.00 0.00 ? 33  ILE A CG1   1 
ATOM   267  C  CG2   . ILE A 1 34  ? 28.706 7.458   -5.314  1.00 0.00 ? 33  ILE A CG2   1 
ATOM   268  C  CD1   . ILE A 1 34  ? 30.946 7.026   -6.854  1.00 0.00 ? 33  ILE A CD1   1 
ATOM   269  N  N     . THR A 1 35  ? 30.659 8.543   -1.140  1.00 0.00 ? 34  THR A N     1 
ATOM   270  C  CA    . THR A 1 35  ? 31.521 8.341   0.028   1.00 0.00 ? 34  THR A CA    1 
ATOM   271  C  C     . THR A 1 35  ? 31.736 6.836   0.261   1.00 0.00 ? 34  THR A C     1 
ATOM   272  O  O     . THR A 1 35  ? 30.936 6.174   0.939   1.00 0.00 ? 34  THR A O     1 
ATOM   273  C  CB    . THR A 1 35  ? 30.859 8.958   1.267   1.00 0.00 ? 34  THR A CB    1 
ATOM   274  O  OG1   . THR A 1 35  ? 30.836 10.373  1.153   1.00 0.00 ? 34  THR A OG1   1 
ATOM   275  C  CG2   . THR A 1 35  ? 31.589 8.617   2.568   1.00 0.00 ? 34  THR A CG2   1 
ATOM   276  N  N     . SER A 1 36  ? 32.821 6.304   -0.348  1.00 0.00 ? 35  SER A N     1 
ATOM   277  C  CA    . SER A 1 36  ? 33.211 4.892   -0.188  1.00 0.00 ? 35  SER A CA    1 
ATOM   278  C  C     . SER A 1 36  ? 33.053 4.145   -1.524  1.00 0.00 ? 35  SER A C     1 
ATOM   279  O  O     . SER A 1 36  ? 31.959 4.100   -2.106  1.00 0.00 ? 35  SER A O     1 
ATOM   280  C  CB    . SER A 1 36  ? 32.321 4.223   0.865   1.00 0.00 ? 35  SER A CB    1 
ATOM   281  O  OG    . SER A 1 36  ? 31.709 5.211   1.682   1.00 0.00 ? 35  SER A OG    1 
ATOM   282  N  N     . ASN A 1 37  ? 34.162 3.574   -1.976  1.00 0.00 ? 36  ASN A N     1 
ATOM   283  C  CA    . ASN A 1 37  ? 34.214 2.809   -3.239  1.00 0.00 ? 36  ASN A CA    1 
ATOM   284  C  C     . ASN A 1 37  ? 34.517 1.338   -2.960  1.00 0.00 ? 36  ASN A C     1 
ATOM   285  O  O     . ASN A 1 37  ? 34.783 0.554   -3.883  1.00 0.00 ? 36  ASN A O     1 
ATOM   286  C  CB    . ASN A 1 37  ? 35.324 3.349   -4.155  1.00 0.00 ? 36  ASN A CB    1 
ATOM   287  C  CG    . ASN A 1 37  ? 36.173 4.444   -3.504  1.00 0.00 ? 36  ASN A CG    1 
ATOM   288  O  OD1   . ASN A 1 37  ? 35.627 5.391   -2.940  1.00 0.00 ? 36  ASN A OD1   1 
ATOM   289  N  ND2   . ASN A 1 37  ? 37.490 4.373   -3.548  1.00 0.00 ? 36  ASN A ND2   1 
ATOM   290  N  N     . GLN A 1 38  ? 34.465 1.003   -1.691  1.00 0.00 ? 37  GLN A N     1 
ATOM   291  C  CA    . GLN A 1 38  ? 34.788 -0.347  -1.216  1.00 0.00 ? 37  GLN A CA    1 
ATOM   292  C  C     . GLN A 1 38  ? 33.911 -1.406  -1.901  1.00 0.00 ? 37  GLN A C     1 
ATOM   293  O  O     . GLN A 1 38  ? 34.417 -2.405  -2.434  1.00 0.00 ? 37  GLN A O     1 
ATOM   294  C  CB    . GLN A 1 38  ? 34.536 -0.414  0.295   1.00 0.00 ? 37  GLN A CB    1 
ATOM   295  C  CG    . GLN A 1 38  ? 34.508 -1.840  0.834   1.00 0.00 ? 37  GLN A CG    1 
ATOM   296  C  CD    . GLN A 1 38  ? 35.658 -2.688  0.299   1.00 0.00 ? 37  GLN A CD    1 
ATOM   297  O  OE1   . GLN A 1 38  ? 36.280 -2.321  -0.697  1.00 0.00 ? 37  GLN A OE1   1 
ATOM   298  N  NE2   . GLN A 1 38  ? 35.986 -3.813  0.906   1.00 0.00 ? 37  GLN A NE2   1 
ATOM   299  N  N     . ARG A 1 39  ? 32.620 -1.144  -1.865  1.00 0.00 ? 38  ARG A N     1 
ATOM   300  C  CA    . ARG A 1 39  ? 31.584 -2.027  -2.445  1.00 0.00 ? 38  ARG A CA    1 
ATOM   301  C  C     . ARG A 1 39  ? 31.767 -2.215  -3.973  1.00 0.00 ? 38  ARG A C     1 
ATOM   302  O  O     . ARG A 1 39  ? 31.733 -3.343  -4.486  1.00 0.00 ? 38  ARG A O     1 
ATOM   303  C  CB    . ARG A 1 39  ? 30.207 -1.461  -2.109  1.00 0.00 ? 38  ARG A CB    1 
ATOM   304  C  CG    . ARG A 1 39  ? 29.865 -1.637  -0.625  1.00 0.00 ? 38  ARG A CG    1 
ATOM   305  C  CD    . ARG A 1 39  ? 28.984 -0.520  -0.065  1.00 0.00 ? 38  ARG A CD    1 
ATOM   306  N  NE    . ARG A 1 39  ? 27.635 -0.988  0.287   1.00 0.00 ? 38  ARG A NE    1 
ATOM   307  C  CZ    . ARG A 1 39  ? 26.962 -0.601  1.379   1.00 0.00 ? 38  ARG A CZ    1 
ATOM   308  N  NH1   . ARG A 1 39  ? 27.496 0.268   2.248   1.00 0.00 ? 38  ARG A NH1   1 
ATOM   309  N  NH2   . ARG A 1 39  ? 25.732 -1.032  1.693   1.00 0.00 ? 38  ARG A NH2   1 
ATOM   310  N  N     . ILE A 1 40  ? 31.956 -1.095  -4.655  1.00 0.00 ? 39  ILE A N     1 
ATOM   311  C  CA    . ILE A 1 40  ? 32.156 -1.029  -6.130  1.00 0.00 ? 39  ILE A CA    1 
ATOM   312  C  C     . ILE A 1 40  ? 33.382 -1.837  -6.610  1.00 0.00 ? 39  ILE A C     1 
ATOM   313  O  O     . ILE A 1 40  ? 33.325 -2.539  -7.631  1.00 0.00 ? 39  ILE A O     1 
ATOM   314  C  CB    . ILE A 1 40  ? 32.329 0.414   -6.604  1.00 0.00 ? 39  ILE A CB    1 
ATOM   315  C  CG1   . ILE A 1 40  ? 31.748 0.658   -8.000  1.00 0.00 ? 39  ILE A CG1   1 
ATOM   316  C  CG2   . ILE A 1 40  ? 33.795 0.846   -6.686  1.00 0.00 ? 39  ILE A CG2   1 
ATOM   317  C  CD1   . ILE A 1 40  ? 32.701 0.249   -9.126  1.00 0.00 ? 39  ILE A CD1   1 
ATOM   318  N  N     . VAL A 1 41  ? 34.460 -1.718  -5.858  1.00 0.00 ? 40  VAL A N     1 
ATOM   319  C  CA    . VAL A 1 41  ? 35.774 -2.303  -6.212  1.00 0.00 ? 40  VAL A CA    1 
ATOM   320  C  C     . VAL A 1 41  ? 35.676 -3.799  -6.566  1.00 0.00 ? 40  VAL A C     1 
ATOM   321  O  O     . VAL A 1 41  ? 36.238 -4.256  -7.572  1.00 0.00 ? 40  VAL A O     1 
ATOM   322  C  CB    . VAL A 1 41  ? 36.729 -2.182  -5.018  1.00 0.00 ? 40  VAL A CB    1 
ATOM   323  C  CG1   . VAL A 1 41  ? 38.022 -2.979  -5.202  1.00 0.00 ? 40  VAL A CG1   1 
ATOM   324  C  CG2   . VAL A 1 41  ? 37.166 -0.741  -4.745  1.00 0.00 ? 40  VAL A CG2   1 
ATOM   325  N  N     . ALA A 1 42  ? 34.965 -4.530  -5.738  1.00 0.00 ? 41  ALA A N     1 
ATOM   326  C  CA    . ALA A 1 42  ? 34.759 -5.989  -5.899  1.00 0.00 ? 41  ALA A CA    1 
ATOM   327  C  C     . ALA A 1 42  ? 34.142 -6.327  -7.265  1.00 0.00 ? 41  ALA A C     1 
ATOM   328  O  O     . ALA A 1 42  ? 34.566 -7.277  -7.941  1.00 0.00 ? 41  ALA A O     1 
ATOM   329  C  CB    . ALA A 1 42  ? 33.814 -6.508  -4.813  1.00 0.00 ? 41  ALA A CB    1 
ATOM   330  N  N     . ALA A 1 43  ? 33.159 -5.523  -7.618  1.00 0.00 ? 42  ALA A N     1 
ATOM   331  C  CA    . ALA A 1 43  ? 32.377 -5.684  -8.851  1.00 0.00 ? 42  ALA A CA    1 
ATOM   332  C  C     . ALA A 1 43  ? 33.343 -5.854  -10.019 1.00 0.00 ? 42  ALA A C     1 
ATOM   333  O  O     . ALA A 1 43  ? 33.109 -6.663  -10.930 1.00 0.00 ? 42  ALA A O     1 
ATOM   334  C  CB    . ALA A 1 43  ? 31.496 -4.453  -9.076  1.00 0.00 ? 42  ALA A CB    1 
ATOM   335  N  N     . LEU A 1 44  ? 34.387 -5.074  -9.942  1.00 0.00 ? 43  LEU A N     1 
ATOM   336  C  CA    . LEU A 1 44  ? 35.481 -5.055  -10.921 1.00 0.00 ? 43  LEU A CA    1 
ATOM   337  C  C     . LEU A 1 44  ? 35.939 -6.453  -11.392 1.00 0.00 ? 43  LEU A C     1 
ATOM   338  O  O     . LEU A 1 44  ? 36.050 -6.717  -12.598 1.00 0.00 ? 43  LEU A O     1 
ATOM   339  C  CB    . LEU A 1 44  ? 36.707 -4.378  -10.327 1.00 0.00 ? 43  LEU A CB    1 
ATOM   340  C  CG    . LEU A 1 44  ? 36.871 -2.946  -10.823 1.00 0.00 ? 43  LEU A CG    1 
ATOM   341  C  CD1   . LEU A 1 44  ? 37.439 -2.867  -12.241 1.00 0.00 ? 43  LEU A CD1   1 
ATOM   342  C  CD2   . LEU A 1 44  ? 35.552 -2.172  -10.859 1.00 0.00 ? 43  LEU A CD2   1 
ATOM   343  N  N     . PRO A 1 45  ? 36.243 -7.466  -10.551 1.00 0.00 ? 44  PRO A N     1 
ATOM   344  C  CA    . PRO A 1 45  ? 36.763 -8.705  -11.102 1.00 0.00 ? 44  PRO A CA    1 
ATOM   345  C  C     . PRO A 1 45  ? 35.804 -9.301  -12.110 1.00 0.00 ? 44  PRO A C     1 
ATOM   346  O  O     . PRO A 1 45  ? 36.222 -9.554  -13.283 1.00 0.00 ? 44  PRO A O     1 
ATOM   347  C  CB    . PRO A 1 45  ? 36.955 -9.578  -9.883  1.00 0.00 ? 44  PRO A CB    1 
ATOM   348  C  CG    . PRO A 1 45  ? 36.530 -8.772  -8.660  1.00 0.00 ? 44  PRO A CG    1 
ATOM   349  C  CD    . PRO A 1 45  ? 36.080 -7.412  -9.101  1.00 0.00 ? 44  PRO A CD    1 
ATOM   350  N  N     . THR A 1 46  ? 34.569 -9.522  -11.689 1.00 0.00 ? 45  THR A N     1 
ATOM   351  C  CA    . THR A 1 46  ? 33.506 -10.017 -12.592 1.00 0.00 ? 45  THR A CA    1 
ATOM   352  C  C     . THR A 1 46  ? 33.160 -8.984  -13.662 1.00 0.00 ? 45  THR A C     1 
ATOM   353  O  O     . THR A 1 46  ? 33.077 -9.303  -14.857 1.00 0.00 ? 45  THR A O     1 
ATOM   354  C  CB    . THR A 1 46  ? 32.224 -10.362 -11.836 1.00 0.00 ? 45  THR A CB    1 
ATOM   355  O  OG1   . THR A 1 46  ? 31.140 -9.599  -12.344 1.00 0.00 ? 45  THR A OG1   1 
ATOM   356  C  CG2   . THR A 1 46  ? 32.319 -10.080 -10.335 1.00 0.00 ? 45  THR A CG2   1 
ATOM   357  N  N     . ILE A 1 47  ? 32.971 -7.767  -13.183 1.00 0.00 ? 46  ILE A N     1 
ATOM   358  C  CA    . ILE A 1 47  ? 32.502 -6.656  -14.018 1.00 0.00 ? 46  ILE A CA    1 
ATOM   359  C  C     . ILE A 1 47  ? 33.413 -6.440  -15.226 1.00 0.00 ? 46  ILE A C     1 
ATOM   360  O  O     . ILE A 1 47  ? 32.952 -6.417  -16.376 1.00 0.00 ? 46  ILE A O     1 
ATOM   361  C  CB    . ILE A 1 47  ? 32.497 -5.372  -13.179 1.00 0.00 ? 46  ILE A CB    1 
ATOM   362  C  CG1   . ILE A 1 47  ? 31.518 -4.319  -13.700 1.00 0.00 ? 46  ILE A CG1   1 
ATOM   363  C  CG2   . ILE A 1 47  ? 33.863 -4.683  -13.133 1.00 0.00 ? 46  ILE A CG2   1 
ATOM   364  C  CD1   . ILE A 1 47  ? 31.941 -3.721  -15.043 1.00 0.00 ? 46  ILE A CD1   1 
ATOM   365  N  N     . LYS A 1 48  ? 34.684 -6.291  -14.944 1.00 0.00 ? 47  LYS A N     1 
ATOM   366  C  CA    . LYS A 1 48  ? 35.709 -6.107  -15.980 1.00 0.00 ? 47  LYS A CA    1 
ATOM   367  C  C     . LYS A 1 48  ? 35.844 -7.335  -16.891 1.00 0.00 ? 47  LYS A C     1 
ATOM   368  O  O     . LYS A 1 48  ? 35.853 -7.218  -18.126 1.00 0.00 ? 47  LYS A O     1 
ATOM   369  C  CB    . LYS A 1 48  ? 37.060 -5.803  -15.339 1.00 0.00 ? 47  LYS A CB    1 
ATOM   370  C  CG    . LYS A 1 48  ? 37.297 -4.303  -15.160 1.00 0.00 ? 47  LYS A CG    1 
ATOM   371  C  CD    . LYS A 1 48  ? 38.777 -3.922  -15.136 1.00 0.00 ? 47  LYS A CD    1 
ATOM   372  C  CE    . LYS A 1 48  ? 39.018 -2.519  -14.577 1.00 0.00 ? 47  LYS A CE    1 
ATOM   373  N  NZ    . LYS A 1 48  ? 40.442 -2.155  -14.532 1.00 0.00 ? 47  LYS A NZ    1 
ATOM   374  N  N     . TYR A 1 49  ? 35.945 -8.503  -16.270 1.00 0.00 ? 48  TYR A N     1 
ATOM   375  C  CA    . TYR A 1 49  ? 36.190 -9.755  -17.013 1.00 0.00 ? 48  TYR A CA    1 
ATOM   376  C  C     . TYR A 1 49  ? 35.109 -9.910  -18.077 1.00 0.00 ? 48  TYR A C     1 
ATOM   377  O  O     . TYR A 1 49  ? 35.407 -10.069 -19.270 1.00 0.00 ? 48  TYR A O     1 
ATOM   378  C  CB    . TYR A 1 49  ? 36.125 -10.931 -16.002 1.00 0.00 ? 48  TYR A CB    1 
ATOM   379  C  CG    . TYR A 1 49  ? 36.048 -12.344 -16.621 1.00 0.00 ? 48  TYR A CG    1 
ATOM   380  C  CD1   . TYR A 1 49  ? 34.885 -13.124 -16.471 1.00 0.00 ? 48  TYR A CD1   1 
ATOM   381  C  CD2   . TYR A 1 49  ? 37.142 -12.871 -17.320 1.00 0.00 ? 48  TYR A CD2   1 
ATOM   382  C  CE1   . TYR A 1 49  ? 34.823 -14.415 -17.021 1.00 0.00 ? 48  TYR A CE1   1 
ATOM   383  C  CE2   . TYR A 1 49  ? 37.077 -14.161 -17.867 1.00 0.00 ? 48  TYR A CE2   1 
ATOM   384  C  CZ    . TYR A 1 49  ? 35.920 -14.932 -17.719 1.00 0.00 ? 48  TYR A CZ    1 
ATOM   385  O  OH    . TYR A 1 49  ? 35.860 -16.183 -18.251 1.00 0.00 ? 48  TYR A OH    1 
ATOM   386  N  N     . VAL A 1 50  ? 33.897 -9.853  -17.579 1.00 0.00 ? 49  VAL A N     1 
ATOM   387  C  CA    . VAL A 1 50  ? 32.658 -9.885  -18.373 1.00 0.00 ? 49  VAL A CA    1 
ATOM   388  C  C     . VAL A 1 50  ? 32.497 -8.648  -19.255 1.00 0.00 ? 49  VAL A C     1 
ATOM   389  O  O     . VAL A 1 50  ? 32.136 -8.747  -20.437 1.00 0.00 ? 49  VAL A O     1 
ATOM   390  C  CB    . VAL A 1 50  ? 31.441 -10.004 -17.472 1.00 0.00 ? 49  VAL A CB    1 
ATOM   391  C  CG1   . VAL A 1 50  ? 30.121 -9.909  -18.240 1.00 0.00 ? 49  VAL A CG1   1 
ATOM   392  C  CG2   . VAL A 1 50  ? 31.389 -11.333 -16.716 1.00 0.00 ? 49  VAL A CG2   1 
ATOM   393  N  N     . LEU A 1 51  ? 32.777 -7.519  -18.642 1.00 0.00 ? 50  LEU A N     1 
ATOM   394  C  CA    . LEU A 1 51  ? 32.557 -6.208  -19.253 1.00 0.00 ? 50  LEU A CA    1 
ATOM   395  C  C     . LEU A 1 51  ? 33.155 -6.208  -20.643 1.00 0.00 ? 50  LEU A C     1 
ATOM   396  O  O     . LEU A 1 51  ? 32.550 -5.698  -21.598 1.00 0.00 ? 50  LEU A O     1 
ATOM   397  C  CB    . LEU A 1 51  ? 33.231 -5.112  -18.412 1.00 0.00 ? 50  LEU A CB    1 
ATOM   398  C  CG    . LEU A 1 51  ? 33.090 -3.707  -19.012 1.00 0.00 ? 50  LEU A CG    1 
ATOM   399  C  CD1   . LEU A 1 51  ? 32.434 -2.710  -18.054 1.00 0.00 ? 50  LEU A CD1   1 
ATOM   400  C  CD2   . LEU A 1 51  ? 34.432 -3.085  -19.402 1.00 0.00 ? 50  LEU A CD2   1 
ATOM   401  N  N     . GLU A 1 52  ? 34.329 -6.782  -20.730 1.00 0.00 ? 51  GLU A N     1 
ATOM   402  C  CA    . GLU A 1 52  ? 35.064 -6.838  -21.993 1.00 0.00 ? 51  GLU A CA    1 
ATOM   403  C  C     . GLU A 1 52  ? 35.004 -8.218  -22.691 1.00 0.00 ? 51  GLU A C     1 
ATOM   404  O  O     . GLU A 1 52  ? 34.981 -8.309  -23.927 1.00 0.00 ? 51  GLU A O     1 
ATOM   405  C  CB    . GLU A 1 52  ? 36.524 -6.475  -21.753 1.00 0.00 ? 51  GLU A CB    1 
ATOM   406  C  CG    . GLU A 1 52  ? 36.738 -4.962  -21.696 1.00 0.00 ? 51  GLU A CG    1 
ATOM   407  C  CD    . GLU A 1 52  ? 37.928 -4.553  -20.830 1.00 0.00 ? 51  GLU A CD    1 
ATOM   408  O  OE1   . GLU A 1 52  ? 38.036 -5.004  -19.626 1.00 0.00 ? 51  GLU A OE1   1 
ATOM   409  O  OE2   . GLU A 1 52  ? 38.825 -3.755  -21.303 1.00 0.00 ? 51  GLU A OE2   1 
ATOM   410  N  N     . HIS A 1 53  ? 34.976 -9.318  -21.938 1.00 0.00 ? 52  HIS A N     1 
ATOM   411  C  CA    . HIS A 1 53  ? 34.971 -10.659 -22.585 1.00 0.00 ? 52  HIS A CA    1 
ATOM   412  C  C     . HIS A 1 53  ? 34.427 -10.497 -24.029 1.00 0.00 ? 52  HIS A C     1 
ATOM   413  O  O     . HIS A 1 53  ? 34.999 -11.032 -24.991 1.00 0.00 ? 52  HIS A O     1 
ATOM   414  C  CB    . HIS A 1 53  ? 34.154 -11.682 -21.794 1.00 0.00 ? 52  HIS A CB    1 
ATOM   415  C  CG    . HIS A 1 53  ? 34.895 -13.026 -21.654 1.00 0.00 ? 52  HIS A CG    1 
ATOM   416  N  ND1   . HIS A 1 53  ? 36.218 -13.096 -21.216 1.00 0.00 ? 52  HIS A ND1   1 
ATOM   417  C  CD2   . HIS A 1 53  ? 34.514 -14.312 -21.891 1.00 0.00 ? 52  HIS A CD2   1 
ATOM   418  C  CE1   . HIS A 1 53  ? 36.585 -14.366 -21.199 1.00 0.00 ? 52  HIS A CE1   1 
ATOM   419  N  NE2   . HIS A 1 53  ? 35.582 -15.104 -21.599 1.00 0.00 ? 52  HIS A NE2   1 
ATOM   420  N  N     . HIS A 1 54  ? 33.317 -9.754  -24.159 1.00 0.00 ? 53  HIS A N     1 
ATOM   421  C  CA    . HIS A 1 54  ? 32.696 -9.443  -25.482 1.00 0.00 ? 53  HIS A CA    1 
ATOM   422  C  C     . HIS A 1 54  ? 31.294 -10.092 -25.634 1.00 0.00 ? 53  HIS A C     1 
ATOM   423  O  O     . HIS A 1 54  ? 30.943 -10.610 -26.704 1.00 0.00 ? 53  HIS A O     1 
ATOM   424  C  CB    . HIS A 1 54  ? 33.612 -9.942  -26.605 1.00 0.00 ? 53  HIS A CB    1 
ATOM   425  C  CG    . HIS A 1 54  ? 34.904 -9.123  -26.721 1.00 0.00 ? 53  HIS A CG    1 
ATOM   426  N  ND1   . HIS A 1 54  ? 35.967 -9.525  -27.527 1.00 0.00 ? 53  HIS A ND1   1 
ATOM   427  C  CD2   . HIS A 1 54  ? 35.289 -7.953  -26.145 1.00 0.00 ? 53  HIS A CD2   1 
ATOM   428  C  CE1   . HIS A 1 54  ? 36.928 -8.624  -27.422 1.00 0.00 ? 53  HIS A CE1   1 
ATOM   429  N  NE2   . HIS A 1 54  ? 36.540 -7.681  -26.601 1.00 0.00 ? 53  HIS A NE2   1 
ATOM   430  N  N     . PRO A 1 55  ? 30.451 -10.086 -24.576 1.00 0.00 ? 54  PRO A N     1 
ATOM   431  C  CA    . PRO A 1 55  ? 29.098 -10.681 -24.624 1.00 0.00 ? 54  PRO A CA    1 
ATOM   432  C  C     . PRO A 1 55  ? 28.211 -9.986  -25.651 1.00 0.00 ? 54  PRO A C     1 
ATOM   433  O  O     . PRO A 1 55  ? 27.922 -10.595 -26.728 1.00 0.00 ? 54  PRO A O     1 
ATOM   434  C  CB    . PRO A 1 55  ? 28.567 -10.460 -23.225 1.00 0.00 ? 54  PRO A CB    1 
ATOM   435  C  CG    . PRO A 1 55  ? 29.636 -9.734  -22.418 1.00 0.00 ? 54  PRO A CG    1 
ATOM   436  C  CD    . PRO A 1 55  ? 30.827 -9.491  -23.290 1.00 0.00 ? 54  PRO A CD    1 
ATOM   437  N  N     . ARG A 1 56  ? 27.841 -8.780  -25.252 1.00 0.00 ? 55  ARG A N     1 
ATOM   438  C  CA    . ARG A 1 56  ? 27.011 -7.799  -25.996 1.00 0.00 ? 55  ARG A CA    1 
ATOM   439  C  C     . ARG A 1 56  ? 26.167 -7.039  -24.994 1.00 0.00 ? 55  ARG A C     1 
ATOM   440  O  O     . ARG A 1 56  ? 25.820 -5.868  -25.210 1.00 0.00 ? 55  ARG A O     1 
ATOM   441  C  CB    . ARG A 1 56  ? 26.085 -8.429  -27.027 1.00 0.00 ? 55  ARG A CB    1 
ATOM   442  C  CG    . ARG A 1 56  ? 25.555 -7.379  -28.018 1.00 0.00 ? 55  ARG A CG    1 
ATOM   443  C  CD    . ARG A 1 56  ? 24.077 -7.049  -27.822 1.00 0.00 ? 55  ARG A CD    1 
ATOM   444  N  NE    . ARG A 1 56  ? 23.204 -8.065  -28.419 1.00 0.00 ? 55  ARG A NE    1 
ATOM   445  C  CZ    . ARG A 1 56  ? 22.102 -7.797  -29.129 1.00 0.00 ? 55  ARG A CZ    1 
ATOM   446  N  NH1   . ARG A 1 56  ? 21.708 -6.534  -29.342 1.00 0.00 ? 55  ARG A NH1   1 
ATOM   447  N  NH2   . ARG A 1 56  ? 21.320 -8.736  -29.679 1.00 0.00 ? 55  ARG A NH2   1 
ATOM   448  N  N     . TYR A 1 57  ? 25.875 -7.758  -23.938 1.00 0.00 ? 56  TYR A N     1 
ATOM   449  C  CA    . TYR A 1 57  ? 25.135 -7.227  -22.808 1.00 0.00 ? 56  TYR A CA    1 
ATOM   450  C  C     . TYR A 1 57  ? 26.088 -6.650  -21.802 1.00 0.00 ? 56  TYR A C     1 
ATOM   451  O  O     . TYR A 1 57  ? 27.170 -6.158  -22.156 1.00 0.00 ? 56  TYR A O     1 
ATOM   452  C  CB    . TYR A 1 57  ? 24.433 -8.326  -22.008 1.00 0.00 ? 56  TYR A CB    1 
ATOM   453  C  CG    . TYR A 1 57  ? 22.929 -8.497  -22.241 1.00 0.00 ? 56  TYR A CG    1 
ATOM   454  C  CD1   . TYR A 1 57  ? 22.449 -9.744  -22.639 1.00 0.00 ? 56  TYR A CD1   1 
ATOM   455  C  CD2   . TYR A 1 57  ? 22.032 -7.439  -22.036 1.00 0.00 ? 56  TYR A CD2   1 
ATOM   456  C  CE1   . TYR A 1 57  ? 21.081 -9.943  -22.835 1.00 0.00 ? 56  TYR A CE1   1 
ATOM   457  C  CE2   . TYR A 1 57  ? 20.658 -7.635  -22.230 1.00 0.00 ? 56  TYR A CE2   1 
ATOM   458  C  CZ    . TYR A 1 57  ? 20.184 -8.891  -22.629 1.00 0.00 ? 56  TYR A CZ    1 
ATOM   459  O  OH    . TYR A 1 57  ? 18.851 -9.089  -22.816 1.00 0.00 ? 56  TYR A OH    1 
ATOM   460  N  N     . VAL A 1 58  ? 25.605 -6.772  -20.602 1.00 0.00 ? 57  VAL A N     1 
ATOM   461  C  CA    . VAL A 1 58  ? 26.282 -6.323  -19.406 1.00 0.00 ? 57  VAL A CA    1 
ATOM   462  C  C     . VAL A 1 58  ? 25.404 -5.338  -18.681 1.00 0.00 ? 57  VAL A C     1 
ATOM   463  O  O     . VAL A 1 58  ? 25.570 -4.117  -18.814 1.00 0.00 ? 57  VAL A O     1 
ATOM   464  C  CB    . VAL A 1 58  ? 27.600 -5.640  -19.744 1.00 0.00 ? 57  VAL A CB    1 
ATOM   465  C  CG1   . VAL A 1 58  ? 28.176 -4.844  -18.571 1.00 0.00 ? 57  VAL A CG1   1 
ATOM   466  C  CG2   . VAL A 1 58  ? 28.696 -6.625  -20.155 1.00 0.00 ? 57  VAL A CG2   1 
ATOM   467  N  N     . VAL A 1 59  ? 24.512 -5.910  -17.942 1.00 0.00 ? 58  VAL A N     1 
ATOM   468  C  CA    . VAL A 1 59  ? 23.586 -5.151  -17.134 1.00 0.00 ? 58  VAL A CA    1 
ATOM   469  C  C     . VAL A 1 59  ? 23.870 -5.491  -15.688 1.00 0.00 ? 58  VAL A C     1 
ATOM   470  O  O     . VAL A 1 59  ? 23.656 -6.629  -15.245 1.00 0.00 ? 58  VAL A O     1 
ATOM   471  C  CB    . VAL A 1 59  ? 22.138 -5.497  -17.493 1.00 0.00 ? 58  VAL A CB    1 
ATOM   472  C  CG1   . VAL A 1 59  ? 21.117 -4.614  -16.772 1.00 0.00 ? 58  VAL A CG1   1 
ATOM   473  C  CG2   . VAL A 1 59  ? 21.838 -5.343  -18.986 1.00 0.00 ? 58  VAL A CG2   1 
ATOM   474  N  N     . LEU A 1 60  ? 24.326 -4.470  -15.014 1.00 0.00 ? 59  LEU A N     1 
ATOM   475  C  CA    . LEU A 1 60  ? 24.724 -4.547  -13.619 1.00 0.00 ? 59  LEU A CA    1 
ATOM   476  C  C     . LEU A 1 60  ? 23.713 -3.726  -12.823 1.00 0.00 ? 59  LEU A C     1 
ATOM   477  O  O     . LEU A 1 60  ? 23.636 -2.497  -12.963 1.00 0.00 ? 59  LEU A O     1 
ATOM   478  C  CB    . LEU A 1 60  ? 26.143 -3.974  -13.461 1.00 0.00 ? 59  LEU A CB    1 
ATOM   479  C  CG    . LEU A 1 60  ? 26.935 -3.949  -14.777 1.00 0.00 ? 59  LEU A CG    1 
ATOM   480  C  CD1   . LEU A 1 60  ? 27.751 -2.668  -14.962 1.00 0.00 ? 59  LEU A CD1   1 
ATOM   481  C  CD2   . LEU A 1 60  ? 27.938 -5.098  -14.893 1.00 0.00 ? 59  LEU A CD2   1 
ATOM   482  N  N     . ALA A 1 61  ? 22.971 -4.469  -12.015 1.00 0.00 ? 60  ALA A N     1 
ATOM   483  C  CA    . ALA A 1 61  ? 21.867 -3.947  -11.189 1.00 0.00 ? 60  ALA A CA    1 
ATOM   484  C  C     . ALA A 1 61  ? 22.363 -3.125  -9.994  1.00 0.00 ? 60  ALA A C     1 
ATOM   485  O  O     . ALA A 1 61  ? 23.540 -3.201  -9.610  1.00 0.00 ? 60  ALA A O     1 
ATOM   486  C  CB    . ALA A 1 61  ? 21.029 -5.105  -10.643 1.00 0.00 ? 60  ALA A CB    1 
ATOM   487  N  N     . SER A 1 62  ? 21.400 -2.377  -9.467  1.00 0.00 ? 61  SER A N     1 
ATOM   488  C  CA    . SER A 1 62  ? 21.581 -1.459  -8.330  1.00 0.00 ? 61  SER A CA    1 
ATOM   489  C  C     . SER A 1 62  ? 21.214 -2.139  -7.009  1.00 0.00 ? 61  SER A C     1 
ATOM   490  O  O     . SER A 1 62  ? 21.175 -3.375  -6.916  1.00 0.00 ? 61  SER A O     1 
ATOM   491  C  CB    . SER A 1 62  ? 20.665 -0.247  -8.500  1.00 0.00 ? 61  SER A CB    1 
ATOM   492  O  OG    . SER A 1 62  ? 19.335 -0.676  -8.754  1.00 0.00 ? 61  SER A OG    1 
ATOM   493  N  N     . HIS A 1 63  ? 20.961 -1.284  -6.022  1.00 0.00 ? 62  HIS A N     1 
ATOM   494  C  CA    . HIS A 1 63  ? 20.550 -1.711  -4.673  1.00 0.00 ? 62  HIS A CA    1 
ATOM   495  C  C     . HIS A 1 63  ? 21.238 -0.892  -3.574  1.00 0.00 ? 62  HIS A C     1 
ATOM   496  O  O     . HIS A 1 63  ? 22.323 -1.252  -3.094  1.00 0.00 ? 62  HIS A O     1 
ATOM   497  C  CB    . HIS A 1 63  ? 20.931 -3.167  -4.432  1.00 0.00 ? 62  HIS A CB    1 
ATOM   498  C  CG    . HIS A 1 63  ? 20.406 -3.685  -3.095  1.00 0.00 ? 62  HIS A CG    1 
ATOM   499  N  ND1   . HIS A 1 63  ? 21.057 -3.421  -1.894  1.00 0.00 ? 62  HIS A ND1   1 
ATOM   500  C  CD2   . HIS A 1 63  ? 19.314 -4.429  -2.782  1.00 0.00 ? 62  HIS A CD2   1 
ATOM   501  C  CE1   . HIS A 1 63  ? 20.369 -3.990  -0.922  1.00 0.00 ? 62  HIS A CE1   1 
ATOM   502  N  NE2   . HIS A 1 63  ? 19.327 -4.595  -1.435  1.00 0.00 ? 62  HIS A NE2   1 
ATOM   503  N  N     . LEU A 1 64  ? 20.598 0.196   -3.188  1.00 0.00 ? 63  LEU A N     1 
ATOM   504  C  CA    . LEU A 1 64  ? 21.112 1.062   -2.109  1.00 0.00 ? 63  LEU A CA    1 
ATOM   505  C  C     . LEU A 1 64  ? 20.145 2.216   -1.839  1.00 0.00 ? 63  LEU A C     1 
ATOM   506  O  O     . LEU A 1 64  ? 20.084 3.191   -2.603  1.00 0.00 ? 63  LEU A O     1 
ATOM   507  C  CB    . LEU A 1 64  ? 22.511 1.596   -2.462  1.00 0.00 ? 63  LEU A CB    1 
ATOM   508  C  CG    . LEU A 1 64  ? 22.521 2.645   -3.577  1.00 0.00 ? 63  LEU A CG    1 
ATOM   509  C  CD1   . LEU A 1 64  ? 21.137 3.236   -3.856  1.00 0.00 ? 63  LEU A CD1   1 
ATOM   510  C  CD2   . LEU A 1 64  ? 23.427 3.838   -3.267  1.00 0.00 ? 63  LEU A CD2   1 
ATOM   511  N  N     . GLY A 1 65  ? 19.422 2.042   -0.742  1.00 0.00 ? 64  GLY A N     1 
ATOM   512  C  CA    . GLY A 1 65  ? 18.433 3.016   -0.265  1.00 0.00 ? 64  GLY A CA    1 
ATOM   513  C  C     . GLY A 1 65  ? 17.164 2.308   0.224   1.00 0.00 ? 64  GLY A C     1 
ATOM   514  O  O     . GLY A 1 65  ? 17.038 1.079   0.118   1.00 0.00 ? 64  GLY A O     1 
ATOM   515  N  N     . ARG A 1 66  ? 16.284 3.142   0.743   1.00 0.00 ? 65  ARG A N     1 
ATOM   516  C  CA    . ARG A 1 66  ? 14.977 2.740   1.269   1.00 0.00 ? 65  ARG A CA    1 
ATOM   517  C  C     . ARG A 1 66  ? 13.919 3.722   0.765   1.00 0.00 ? 65  ARG A C     1 
ATOM   518  O  O     . ARG A 1 66  ? 13.325 4.478   1.548   1.00 0.00 ? 65  ARG A O     1 
ATOM   519  C  CB    . ARG A 1 66  ? 14.996 2.783   2.805   1.00 0.00 ? 65  ARG A CB    1 
ATOM   520  C  CG    . ARG A 1 66  ? 15.716 4.018   3.365   1.00 0.00 ? 65  ARG A CG    1 
ATOM   521  C  CD    . ARG A 1 66  ? 14.944 4.712   4.496   1.00 0.00 ? 65  ARG A CD    1 
ATOM   522  N  NE    . ARG A 1 66  ? 15.378 4.290   5.839   1.00 0.00 ? 65  ARG A NE    1 
ATOM   523  C  CZ    . ARG A 1 66  ? 15.469 5.111   6.898   1.00 0.00 ? 65  ARG A CZ    1 
ATOM   524  N  NH1   . ARG A 1 66  ? 15.161 6.411   6.792   1.00 0.00 ? 65  ARG A NH1   1 
ATOM   525  N  NH2   . ARG A 1 66  ? 15.863 4.720   8.117   1.00 0.00 ? 65  ARG A NH2   1 
ATOM   526  N  N     . PRO A 1 67  ? 13.613 3.779   -0.544  1.00 0.00 ? 66  PRO A N     1 
ATOM   527  C  CA    . PRO A 1 67  ? 12.633 4.729   -1.033  1.00 0.00 ? 66  PRO A CA    1 
ATOM   528  C  C     . PRO A 1 67  ? 11.345 4.523   -0.279  1.00 0.00 ? 66  PRO A C     1 
ATOM   529  O  O     . PRO A 1 67  ? 10.436 3.804   -0.800  1.00 0.00 ? 66  PRO A O     1 
ATOM   530  C  CB    . PRO A 1 67  ? 12.553 4.435   -2.513  1.00 0.00 ? 66  PRO A CB    1 
ATOM   531  C  CG    . PRO A 1 67  ? 13.528 3.306   -2.817  1.00 0.00 ? 66  PRO A CG    1 
ATOM   532  C  CD    . PRO A 1 67  ? 14.212 2.900   -1.549  1.00 0.00 ? 66  PRO A CD    1 
ATOM   533  N  N     . ASN A 1 68  ? 11.331 5.157   0.889   1.00 0.00 ? 67  ASN A N     1 
ATOM   534  C  CA    . ASN A 1 68  ? 10.230 5.096   1.876   1.00 0.00 ? 67  ASN A CA    1 
ATOM   535  C  C     . ASN A 1 68  ? 8.979  5.830   1.382   1.00 0.00 ? 67  ASN A C     1 
ATOM   536  O  O     . ASN A 1 68  ? 8.272  5.355   0.480   1.00 0.00 ? 67  ASN A O     1 
ATOM   537  C  CB    . ASN A 1 68  ? 10.682 5.751   3.185   1.00 0.00 ? 67  ASN A CB    1 
ATOM   538  C  CG    . ASN A 1 68  ? 9.870  5.301   4.401   1.00 0.00 ? 67  ASN A CG    1 
ATOM   539  O  OD1   . ASN A 1 68  ? 9.867  5.983   5.425   1.00 0.00 ? 67  ASN A OD1   1 
ATOM   540  N  ND2   . ASN A 1 68  ? 9.173  4.181   4.353   1.00 0.00 ? 67  ASN A ND2   1 
ATOM   541  N  N     . GLY A 1 69  ? 8.742  6.983   1.979   1.00 0.00 ? 68  GLY A N     1 
ATOM   542  C  CA    . GLY A 1 69  ? 7.545  7.794   1.678   1.00 0.00 ? 68  GLY A CA    1 
ATOM   543  C  C     . GLY A 1 69  ? 7.777  8.823   0.546   1.00 0.00 ? 68  GLY A C     1 
ATOM   544  O  O     . GLY A 1 69  ? 8.575  9.761   0.691   1.00 0.00 ? 68  GLY A O     1 
ATOM   545  N  N     . GLU A 1 70  ? 7.052  8.592   -0.575  1.00 0.00 ? 69  GLU A N     1 
ATOM   546  C  CA    . GLU A 1 70  ? 7.016  9.528   -1.742  1.00 0.00 ? 69  GLU A CA    1 
ATOM   547  C  C     . GLU A 1 70  ? 6.881  8.798   -3.132  1.00 0.00 ? 69  GLU A C     1 
ATOM   548  O  O     . GLU A 1 70  ? 6.111  9.223   -4.006  1.00 0.00 ? 69  GLU A O     1 
ATOM   549  C  CB    . GLU A 1 70  ? 8.192  10.510  -1.650  1.00 0.00 ? 69  GLU A CB    1 
ATOM   550  C  CG    . GLU A 1 70  ? 8.055  11.489  -0.471  1.00 0.00 ? 69  GLU A CG    1 
ATOM   551  C  CD    . GLU A 1 70  ? 7.928  12.958  -0.900  1.00 0.00 ? 69  GLU A CD    1 
ATOM   552  O  OE1   . GLU A 1 70  ? 8.892  13.783  -0.667  1.00 0.00 ? 69  GLU A OE1   1 
ATOM   553  O  OE2   . GLU A 1 70  ? 6.858  13.368  -1.492  1.00 0.00 ? 69  GLU A OE2   1 
ATOM   554  N  N     . ARG A 1 71  ? 7.599  7.709   -3.371  1.00 0.00 ? 70  ARG A N     1 
ATOM   555  C  CA    . ARG A 1 71  ? 7.481  6.959   -4.660  1.00 0.00 ? 70  ARG A CA    1 
ATOM   556  C  C     . ARG A 1 71  ? 8.840  6.365   -5.047  1.00 0.00 ? 70  ARG A C     1 
ATOM   557  O  O     . ARG A 1 71  ? 9.547  5.784   -4.210  1.00 0.00 ? 70  ARG A O     1 
ATOM   558  C  CB    . ARG A 1 71  ? 6.962  7.889   -5.789  1.00 0.00 ? 70  ARG A CB    1 
ATOM   559  C  CG    . ARG A 1 71  ? 5.997  8.995   -5.294  1.00 0.00 ? 70  ARG A CG    1 
ATOM   560  C  CD    . ARG A 1 71  ? 4.828  9.292   -6.264  1.00 0.00 ? 70  ARG A CD    1 
ATOM   561  N  NE    . ARG A 1 71  ? 5.077  10.449  -7.157  1.00 0.00 ? 70  ARG A NE    1 
ATOM   562  C  CZ    . ARG A 1 71  ? 4.117  11.156  -7.790  1.00 0.00 ? 70  ARG A CZ    1 
ATOM   563  N  NH1   . ARG A 1 71  ? 2.821  10.850  -7.643  1.00 0.00 ? 70  ARG A NH1   1 
ATOM   564  N  NH2   . ARG A 1 71  ? 4.363  12.194  -8.602  1.00 0.00 ? 70  ARG A NH2   1 
ATOM   565  N  N     . ASN A 1 72  ? 9.173  6.530   -6.307  1.00 0.00 ? 71  ASN A N     1 
ATOM   566  C  CA    . ASN A 1 72  ? 10.428 6.017   -6.865  1.00 0.00 ? 71  ASN A CA    1 
ATOM   567  C  C     . ASN A 1 72  ? 11.559 7.042   -6.654  1.00 0.00 ? 71  ASN A C     1 
ATOM   568  O  O     . ASN A 1 72  ? 12.727 6.779   -6.977  1.00 0.00 ? 71  ASN A O     1 
ATOM   569  C  CB    . ASN A 1 72  ? 10.227 5.717   -8.348  1.00 0.00 ? 71  ASN A CB    1 
ATOM   570  C  CG    . ASN A 1 72  ? 9.203  4.601   -8.584  1.00 0.00 ? 71  ASN A CG    1 
ATOM   571  O  OD1   . ASN A 1 72  ? 9.584  3.455   -8.816  1.00 0.00 ? 71  ASN A OD1   1 
ATOM   572  N  ND2   . ASN A 1 72  ? 7.911  4.870   -8.538  1.00 0.00 ? 71  ASN A ND2   1 
ATOM   573  N  N     . GLU A 1 73  ? 11.163 8.186   -6.113  1.00 0.00 ? 72  GLU A N     1 
ATOM   574  C  CA    . GLU A 1 73  ? 12.076 9.311   -5.797  1.00 0.00 ? 72  GLU A CA    1 
ATOM   575  C  C     . GLU A 1 73  ? 13.424 9.139   -6.505  1.00 0.00 ? 72  GLU A C     1 
ATOM   576  O  O     . GLU A 1 73  ? 14.015 8.049   -6.499  1.00 0.00 ? 72  GLU A O     1 
ATOM   577  C  CB    . GLU A 1 73  ? 12.342 9.356   -4.291  1.00 0.00 ? 72  GLU A CB    1 
ATOM   578  C  CG    . GLU A 1 73  ? 13.183 8.171   -3.805  1.00 0.00 ? 72  GLU A CG    1 
ATOM   579  C  CD    . GLU A 1 73  ? 13.623 8.301   -2.345  1.00 0.00 ? 72  GLU A CD    1 
ATOM   580  O  OE1   . GLU A 1 73  ? 13.809 9.469   -1.829  1.00 0.00 ? 72  GLU A OE1   1 
ATOM   581  O  OE2   . GLU A 1 73  ? 13.808 7.243   -1.631  1.00 0.00 ? 72  GLU A OE2   1 
ATOM   582  N  N     . LYS A 1 74  ? 13.888 10.228  -7.107  1.00 0.00 ? 73  LYS A N     1 
ATOM   583  C  CA    . LYS A 1 74  ? 15.183 10.234  -7.811  1.00 0.00 ? 73  LYS A CA    1 
ATOM   584  C  C     . LYS A 1 74  ? 16.263 9.749   -6.816  1.00 0.00 ? 73  LYS A C     1 
ATOM   585  O  O     . LYS A 1 74  ? 16.116 8.699   -6.175  1.00 0.00 ? 73  LYS A O     1 
ATOM   586  C  CB    . LYS A 1 74  ? 15.453 11.626  -8.408  1.00 0.00 ? 73  LYS A CB    1 
ATOM   587  C  CG    . LYS A 1 74  ? 14.700 11.861  -9.736  1.00 0.00 ? 73  LYS A CG    1 
ATOM   588  C  CD    . LYS A 1 74  ? 15.469 12.736  -10.740 1.00 0.00 ? 73  LYS A CD    1 
ATOM   589  C  CE    . LYS A 1 74  ? 14.807 12.788  -12.124 1.00 0.00 ? 73  LYS A CE    1 
ATOM   590  N  NZ    . LYS A 1 74  ? 15.279 13.911  -12.946 1.00 0.00 ? 73  LYS A NZ    1 
ATOM   591  N  N     . TYR A 1 75  ? 17.348 10.494  -6.663  1.00 0.00 ? 74  TYR A N     1 
ATOM   592  C  CA    . TYR A 1 75  ? 18.439 10.051  -5.762  1.00 0.00 ? 74  TYR A CA    1 
ATOM   593  C  C     . TYR A 1 75  ? 18.862 8.657   -6.255  1.00 0.00 ? 74  TYR A C     1 
ATOM   594  O  O     . TYR A 1 75  ? 19.087 7.737   -5.454  1.00 0.00 ? 74  TYR A O     1 
ATOM   595  C  CB    . TYR A 1 75  ? 17.935 10.125  -4.287  1.00 0.00 ? 74  TYR A CB    1 
ATOM   596  C  CG    . TYR A 1 75  ? 17.981 8.824   -3.444  1.00 0.00 ? 74  TYR A CG    1 
ATOM   597  C  CD1   . TYR A 1 75  ? 19.157 8.056   -3.347  1.00 0.00 ? 74  TYR A CD1   1 
ATOM   598  C  CD2   . TYR A 1 75  ? 16.837 8.411   -2.737  1.00 0.00 ? 74  TYR A CD2   1 
ATOM   599  C  CE1   . TYR A 1 75  ? 19.182 6.888   -2.556  1.00 0.00 ? 74  TYR A CE1   1 
ATOM   600  C  CE2   . TYR A 1 75  ? 16.865 7.246   -1.947  1.00 0.00 ? 74  TYR A CE2   1 
ATOM   601  C  CZ    . TYR A 1 75  ? 18.036 6.485   -1.857  1.00 0.00 ? 74  TYR A CZ    1 
ATOM   602  O  OH    . TYR A 1 75  ? 18.065 5.359   -1.094  1.00 0.00 ? 74  TYR A OH    1 
ATOM   603  N  N     . SER A 1 76  ? 18.945 8.609   -7.592  1.00 0.00 ? 75  SER A N     1 
ATOM   604  C  CA    . SER A 1 76  ? 19.278 7.403   -8.389  1.00 0.00 ? 75  SER A CA    1 
ATOM   605  C  C     . SER A 1 76  ? 20.750 6.999   -8.221  1.00 0.00 ? 75  SER A C     1 
ATOM   606  O  O     . SER A 1 76  ? 21.236 6.808   -7.096  1.00 0.00 ? 75  SER A O     1 
ATOM   607  C  CB    . SER A 1 76  ? 19.018 7.666   -9.874  1.00 0.00 ? 75  SER A CB    1 
ATOM   608  O  OG    . SER A 1 76  ? 18.163 6.663   -10.402 1.00 0.00 ? 75  SER A OG    1 
ATOM   609  N  N     . LEU A 1 77  ? 21.437 6.879   -9.356  1.00 0.00 ? 76  LEU A N     1 
ATOM   610  C  CA    . LEU A 1 77  ? 22.846 6.440   -9.371  1.00 0.00 ? 76  LEU A CA    1 
ATOM   611  C  C     . LEU A 1 77  ? 23.656 7.071   -10.509 1.00 0.00 ? 76  LEU A C     1 
ATOM   612  O  O     . LEU A 1 77  ? 24.577 6.449   -11.059 1.00 0.00 ? 76  LEU A O     1 
ATOM   613  C  CB    . LEU A 1 77  ? 22.913 4.927   -9.589  1.00 0.00 ? 76  LEU A CB    1 
ATOM   614  C  CG    . LEU A 1 77  ? 22.471 4.512   -10.996 1.00 0.00 ? 76  LEU A CG    1 
ATOM   615  C  CD1   . LEU A 1 77  ? 23.317 3.378   -11.579 1.00 0.00 ? 76  LEU A CD1   1 
ATOM   616  C  CD2   . LEU A 1 77  ? 21.024 4.017   -11.048 1.00 0.00 ? 76  LEU A CD2   1 
ATOM   617  N  N     . ALA A 1 78  ? 23.322 8.291   -10.862 1.00 0.00 ? 77  ALA A N     1 
ATOM   618  C  CA    . ALA A 1 78  ? 24.036 8.988   -11.944 1.00 0.00 ? 77  ALA A CA    1 
ATOM   619  C  C     . ALA A 1 78  ? 25.533 9.076   -11.613 1.00 0.00 ? 77  ALA A C     1 
ATOM   620  O  O     . ALA A 1 78  ? 26.391 8.740   -12.443 1.00 0.00 ? 77  ALA A O     1 
ATOM   621  C  CB    . ALA A 1 78  ? 23.484 10.406  -12.106 1.00 0.00 ? 77  ALA A CB    1 
ATOM   622  N  N     . PRO A 1 79  ? 25.881 9.524   -10.395 1.00 0.00 ? 78  PRO A N     1 
ATOM   623  C  CA    . PRO A 1 79  ? 27.269 9.652   -9.963  1.00 0.00 ? 78  PRO A CA    1 
ATOM   624  C  C     . PRO A 1 79  ? 28.018 8.333   -10.062 1.00 0.00 ? 78  PRO A C     1 
ATOM   625  O  O     . PRO A 1 79  ? 29.194 8.326   -10.540 1.00 0.00 ? 78  PRO A O     1 
ATOM   626  C  CB    . PRO A 1 79  ? 27.172 10.178  -8.551  1.00 0.00 ? 78  PRO A CB    1 
ATOM   627  C  CG    . PRO A 1 79  ? 25.698 10.344  -8.214  1.00 0.00 ? 78  PRO A CG    1 
ATOM   628  C  CD    . PRO A 1 79  ? 24.884 9.927   -9.397  1.00 0.00 ? 78  PRO A CD    1 
ATOM   629  N  N     . VAL A 1 80  ? 27.377 7.254   -9.630  1.00 0.00 ? 79  VAL A N     1 
ATOM   630  C  CA    . VAL A 1 80  ? 27.994 5.904   -9.646  1.00 0.00 ? 79  VAL A CA    1 
ATOM   631  C  C     . VAL A 1 80  ? 28.491 5.556   -11.051 1.00 0.00 ? 79  VAL A C     1 
ATOM   632  O  O     . VAL A 1 80  ? 29.613 5.060   -11.228 1.00 0.00 ? 79  VAL A O     1 
ATOM   633  C  CB    . VAL A 1 80  ? 26.975 4.836   -9.240  1.00 0.00 ? 79  VAL A CB    1 
ATOM   634  C  CG1   . VAL A 1 80  ? 25.769 4.772   -10.179 1.00 0.00 ? 79  VAL A CG1   1 
ATOM   635  C  CG2   . VAL A 1 80  ? 27.564 3.424   -9.224  1.00 0.00 ? 79  VAL A CG2   1 
ATOM   636  N  N     . ALA A 1 81  ? 27.632 5.836   -12.009 1.00 0.00 ? 80  ALA A N     1 
ATOM   637  C  CA    . ALA A 1 81  ? 27.922 5.582   -13.416 1.00 0.00 ? 80  ALA A CA    1 
ATOM   638  C  C     . ALA A 1 81  ? 29.269 6.220   -13.689 1.00 0.00 ? 80  ALA A C     1 
ATOM   639  O  O     . ALA A 1 81  ? 30.113 5.651   -14.397 1.00 0.00 ? 80  ALA A O     1 
ATOM   640  C  CB    . ALA A 1 81  ? 26.835 6.203   -14.296 1.00 0.00 ? 80  ALA A CB    1 
ATOM   641  N  N     . LYS A 1 82  ? 29.394 7.392   -13.110 1.00 0.00 ? 81  LYS A N     1 
ATOM   642  C  CA    . LYS A 1 82  ? 30.616 8.187   -13.174 1.00 0.00 ? 81  LYS A CA    1 
ATOM   643  C  C     . LYS A 1 82  ? 31.793 7.356   -12.654 1.00 0.00 ? 81  LYS A C     1 
ATOM   644  O  O     . LYS A 1 82  ? 32.854 7.283   -13.292 1.00 0.00 ? 81  LYS A O     1 
ATOM   645  C  CB    . LYS A 1 82  ? 30.453 9.417   -12.280 1.00 0.00 ? 81  LYS A CB    1 
ATOM   646  C  CG    . LYS A 1 82  ? 31.249 10.625  -12.766 1.00 0.00 ? 81  LYS A CG    1 
ATOM   647  C  CD    . LYS A 1 82  ? 31.448 11.682  -11.681 1.00 0.00 ? 81  LYS A CD    1 
ATOM   648  C  CE    . LYS A 1 82  ? 32.785 12.415  -11.799 1.00 0.00 ? 81  LYS A CE    1 
ATOM   649  N  NZ    . LYS A 1 82  ? 32.755 13.763  -11.214 1.00 0.00 ? 81  LYS A NZ    1 
ATOM   650  N  N     . GLU A 1 83  ? 31.559 6.752   -11.501 1.00 0.00 ? 82  GLU A N     1 
ATOM   651  C  CA    . GLU A 1 83  ? 32.550 5.892   -10.846 1.00 0.00 ? 82  GLU A CA    1 
ATOM   652  C  C     . GLU A 1 83  ? 32.929 4.761   -11.795 1.00 0.00 ? 82  GLU A C     1 
ATOM   653  O  O     . GLU A 1 83  ? 34.117 4.470   -11.999 1.00 0.00 ? 82  GLU A O     1 
ATOM   654  C  CB    . GLU A 1 83  ? 31.966 5.298   -9.561  1.00 0.00 ? 82  GLU A CB    1 
ATOM   655  C  CG    . GLU A 1 83  ? 33.024 4.650   -8.667  1.00 0.00 ? 82  GLU A CG    1 
ATOM   656  C  CD    . GLU A 1 83  ? 34.072 5.646   -8.167  1.00 0.00 ? 82  GLU A CD    1 
ATOM   657  O  OE1   . GLU A 1 83  ? 35.108 5.224   -7.526  1.00 0.00 ? 82  GLU A OE1   1 
ATOM   658  O  OE2   . GLU A 1 83  ? 33.919 6.907   -8.388  1.00 0.00 ? 82  GLU A OE2   1 
ATOM   659  N  N     . LEU A 1 84  ? 31.887 4.163   -12.338 1.00 0.00 ? 83  LEU A N     1 
ATOM   660  C  CA    . LEU A 1 84  ? 32.008 3.052   -13.290 1.00 0.00 ? 83  LEU A CA    1 
ATOM   661  C  C     . LEU A 1 84  ? 32.775 3.462   -14.550 1.00 0.00 ? 83  LEU A C     1 
ATOM   662  O  O     . LEU A 1 84  ? 33.724 2.783   -14.969 1.00 0.00 ? 83  LEU A O     1 
ATOM   663  C  CB    . LEU A 1 84  ? 30.622 2.583   -13.721 1.00 0.00 ? 83  LEU A CB    1 
ATOM   664  C  CG    . LEU A 1 84  ? 30.578 1.087   -14.023 1.00 0.00 ? 83  LEU A CG    1 
ATOM   665  C  CD1   . LEU A 1 84  ? 31.772 0.326   -13.442 1.00 0.00 ? 83  LEU A CD1   1 
ATOM   666  C  CD2   . LEU A 1 84  ? 29.333 0.400   -13.460 1.00 0.00 ? 83  LEU A CD2   1 
ATOM   667  N  N     . GLN A 1 85  ? 32.339 4.570   -15.114 1.00 0.00 ? 84  GLN A N     1 
ATOM   668  C  CA    . GLN A 1 85  ? 32.922 5.109   -16.346 1.00 0.00 ? 84  GLN A CA    1 
ATOM   669  C  C     . GLN A 1 85  ? 34.409 5.345   -16.145 1.00 0.00 ? 84  GLN A C     1 
ATOM   670  O  O     . GLN A 1 85  ? 35.236 4.968   -16.988 1.00 0.00 ? 84  GLN A O     1 
ATOM   671  C  CB    . GLN A 1 85  ? 32.256 6.439   -16.715 1.00 0.00 ? 84  GLN A CB    1 
ATOM   672  C  CG    . GLN A 1 85  ? 33.085 7.274   -17.696 1.00 0.00 ? 84  GLN A CG    1 
ATOM   673  C  CD    . GLN A 1 85  ? 32.432 8.614   -18.047 1.00 0.00 ? 84  GLN A CD    1 
ATOM   674  O  OE1   . GLN A 1 85  ? 32.730 9.188   -19.093 1.00 0.00 ? 84  GLN A OE1   1 
ATOM   675  N  NE2   . GLN A 1 85  ? 31.548 9.153   -17.228 1.00 0.00 ? 84  GLN A NE2   1 
ATOM   676  N  N     . SER A 1 86  ? 34.700 5.968   -15.026 1.00 0.00 ? 85  SER A N     1 
ATOM   677  C  CA    . SER A 1 86  ? 36.070 6.324   -14.668 1.00 0.00 ? 85  SER A CA    1 
ATOM   678  C  C     . SER A 1 86  ? 36.961 5.084   -14.630 1.00 0.00 ? 85  SER A C     1 
ATOM   679  O  O     . SER A 1 86  ? 38.027 5.045   -15.262 1.00 0.00 ? 85  SER A O     1 
ATOM   680  C  CB    . SER A 1 86  ? 36.084 6.959   -13.274 1.00 0.00 ? 85  SER A CB    1 
ATOM   681  O  OG    . SER A 1 86  ? 37.007 8.037   -13.240 1.00 0.00 ? 85  SER A OG    1 
ATOM   682  N  N     . LEU A 1 87  ? 36.511 4.087   -13.890 1.00 0.00 ? 86  LEU A N     1 
ATOM   683  C  CA    . LEU A 1 87  ? 37.272 2.836   -13.749 1.00 0.00 ? 86  LEU A CA    1 
ATOM   684  C  C     . LEU A 1 87  ? 37.427 2.111   -15.099 1.00 0.00 ? 86  LEU A C     1 
ATOM   685  O  O     . LEU A 1 87  ? 38.547 1.822   -15.543 1.00 0.00 ? 86  LEU A O     1 
ATOM   686  C  CB    . LEU A 1 87  ? 36.545 1.891   -12.783 1.00 0.00 ? 86  LEU A CB    1 
ATOM   687  C  CG    . LEU A 1 87  ? 37.004 2.036   -11.329 1.00 0.00 ? 86  LEU A CG    1 
ATOM   688  C  CD1   . LEU A 1 87  ? 36.325 3.197   -10.599 1.00 0.00 ? 86  LEU A CD1   1 
ATOM   689  C  CD2   . LEU A 1 87  ? 36.718 0.793   -10.485 1.00 0.00 ? 86  LEU A CD2   1 
ATOM   690  N  N     . LEU A 1 88  ? 36.277 1.841   -15.712 1.00 0.00 ? 87  LEU A N     1 
ATOM   691  C  CA    . LEU A 1 88  ? 36.182 1.151   -17.024 1.00 0.00 ? 87  LEU A CA    1 
ATOM   692  C  C     . LEU A 1 88  ? 36.748 1.967   -18.195 1.00 0.00 ? 87  LEU A C     1 
ATOM   693  O  O     . LEU A 1 88  ? 37.597 1.485   -18.960 1.00 0.00 ? 87  LEU A O     1 
ATOM   694  C  CB    . LEU A 1 88  ? 34.725 0.839   -17.354 1.00 0.00 ? 87  LEU A CB    1 
ATOM   695  C  CG    . LEU A 1 88  ? 33.825 0.827   -16.119 1.00 0.00 ? 87  LEU A CG    1 
ATOM   696  C  CD1   . LEU A 1 88  ? 32.349 1.051   -16.453 1.00 0.00 ? 87  LEU A CD1   1 
ATOM   697  C  CD2   . LEU A 1 88  ? 33.880 -0.495  -15.351 1.00 0.00 ? 87  LEU A CD2   1 
ATOM   698  N  N     . GLY A 1 89  ? 36.252 3.192   -18.283 1.00 0.00 ? 88  GLY A N     1 
ATOM   699  C  CA    . GLY A 1 89  ? 36.589 4.122   -19.376 1.00 0.00 ? 88  GLY A CA    1 
ATOM   700  C  C     . GLY A 1 89  ? 36.079 3.566   -20.725 1.00 0.00 ? 88  GLY A C     1 
ATOM   701  O  O     . GLY A 1 89  ? 36.664 3.829   -21.786 1.00 0.00 ? 88  GLY A O     1 
ATOM   702  N  N     . LYS A 1 90  ? 34.987 2.806   -20.648 1.00 0.00 ? 89  LYS A N     1 
ATOM   703  C  CA    . LYS A 1 90  ? 34.371 2.164   -21.835 1.00 0.00 ? 89  LYS A CA    1 
ATOM   704  C  C     . LYS A 1 90  ? 32.973 2.714   -22.116 1.00 0.00 ? 89  LYS A C     1 
ATOM   705  O  O     . LYS A 1 90  ? 32.472 2.639   -23.248 1.00 0.00 ? 89  LYS A O     1 
ATOM   706  C  CB    . LYS A 1 90  ? 34.255 0.653   -21.628 1.00 0.00 ? 89  LYS A CB    1 
ATOM   707  C  CG    . LYS A 1 90  ? 33.797 -0.088  -22.887 1.00 0.00 ? 89  LYS A CG    1 
ATOM   708  C  CD    . LYS A 1 90  ? 34.016 -1.600  -22.805 1.00 0.00 ? 89  LYS A CD    1 
ATOM   709  C  CE    . LYS A 1 90  ? 33.714 -2.320  -24.121 1.00 0.00 ? 89  LYS A CE    1 
ATOM   710  N  NZ    . LYS A 1 90  ? 33.715 -3.784  -23.988 1.00 0.00 ? 89  LYS A NZ    1 
ATOM   711  N  N     . ASP A 1 91  ? 32.360 3.254   -21.087 1.00 0.00 ? 90  ASP A N     1 
ATOM   712  C  CA    . ASP A 1 91  ? 31.015 3.834   -21.205 1.00 0.00 ? 90  ASP A CA    1 
ATOM   713  C  C     . ASP A 1 91  ? 29.959 2.906   -20.594 1.00 0.00 ? 90  ASP A C     1 
ATOM   714  O  O     . ASP A 1 91  ? 29.800 1.753   -21.020 1.00 0.00 ? 90  ASP A O     1 
ATOM   715  C  CB    . ASP A 1 91  ? 30.666 4.061   -22.675 1.00 0.00 ? 90  ASP A CB    1 
ATOM   716  C  CG    . ASP A 1 91  ? 30.140 5.471   -22.957 1.00 0.00 ? 90  ASP A CG    1 
ATOM   717  O  OD1   . ASP A 1 91  ? 30.086 5.909   -24.169 1.00 0.00 ? 90  ASP A OD1   1 
ATOM   718  O  OD2   . ASP A 1 91  ? 29.751 6.221   -21.982 1.00 0.00 ? 90  ASP A OD2   1 
ATOM   719  N  N     . VAL A 1 92  ? 29.318 3.509   -19.611 1.00 0.00 ? 91  VAL A N     1 
ATOM   720  C  CA    . VAL A 1 92  ? 28.233 2.945   -18.788 1.00 0.00 ? 91  VAL A CA    1 
ATOM   721  C  C     . VAL A 1 92  ? 26.964 3.807   -18.877 1.00 0.00 ? 91  VAL A C     1 
ATOM   722  O  O     . VAL A 1 92  ? 26.997 5.021   -18.624 1.00 0.00 ? 91  VAL A O     1 
ATOM   723  C  CB    . VAL A 1 92  ? 28.639 2.803   -17.331 1.00 0.00 ? 91  VAL A CB    1 
ATOM   724  C  CG1   . VAL A 1 92  ? 27.655 1.956   -16.521 1.00 0.00 ? 91  VAL A CG1   1 
ATOM   725  C  CG2   . VAL A 1 92  ? 30.005 2.138   -17.155 1.00 0.00 ? 91  VAL A CG2   1 
ATOM   726  N  N     . THR A 1 93  ? 25.907 3.125   -19.244 1.00 0.00 ? 92  THR A N     1 
ATOM   727  C  CA    . THR A 1 93  ? 24.561 3.690   -19.458 1.00 0.00 ? 92  THR A CA    1 
ATOM   728  C  C     . THR A 1 93  ? 23.550 3.168   -18.418 1.00 0.00 ? 92  THR A C     1 
ATOM   729  O  O     . THR A 1 93  ? 23.380 1.952   -18.245 1.00 0.00 ? 92  THR A O     1 
ATOM   730  C  CB    . THR A 1 93  ? 24.025 3.314   -20.831 1.00 0.00 ? 92  THR A CB    1 
ATOM   731  O  OG1   . THR A 1 93  ? 24.745 4.007   -21.839 1.00 0.00 ? 92  THR A OG1   1 
ATOM   732  C  CG2   . THR A 1 93  ? 22.544 3.659   -21.007 1.00 0.00 ? 92  THR A CG2   1 
ATOM   733  N  N     . PHE A 1 94  ? 22.911 4.118   -17.748 1.00 0.00 ? 93  PHE A N     1 
ATOM   734  C  CA    . PHE A 1 94  ? 21.915 3.844   -16.693 1.00 0.00 ? 93  PHE A CA    1 
ATOM   735  C  C     . PHE A 1 94  ? 20.513 4.268   -17.190 1.00 0.00 ? 93  PHE A C     1 
ATOM   736  O  O     . PHE A 1 94  ? 20.247 5.457   -17.418 1.00 0.00 ? 93  PHE A O     1 
ATOM   737  C  CB    . PHE A 1 94  ? 22.346 4.596   -15.416 1.00 0.00 ? 93  PHE A CB    1 
ATOM   738  C  CG    . PHE A 1 94  ? 21.377 5.679   -14.919 1.00 0.00 ? 93  PHE A CG    1 
ATOM   739  C  CD1   . PHE A 1 94  ? 21.319 6.930   -15.551 1.00 0.00 ? 93  PHE A CD1   1 
ATOM   740  C  CD2   . PHE A 1 94  ? 20.560 5.421   -13.811 1.00 0.00 ? 93  PHE A CD2   1 
ATOM   741  C  CE1   . PHE A 1 94  ? 20.446 7.918   -15.073 1.00 0.00 ? 93  PHE A CE1   1 
ATOM   742  C  CE2   . PHE A 1 94  ? 19.690 6.409   -13.334 1.00 0.00 ? 93  PHE A CE2   1 
ATOM   743  C  CZ    . PHE A 1 94  ? 19.633 7.657   -13.964 1.00 0.00 ? 93  PHE A CZ    1 
ATOM   744  N  N     . LEU A 1 95  ? 19.689 3.222   -17.330 1.00 0.00 ? 94  LEU A N     1 
ATOM   745  C  CA    . LEU A 1 95  ? 18.308 3.292   -17.862 1.00 0.00 ? 94  LEU A CA    1 
ATOM   746  C  C     . LEU A 1 95  ? 17.262 2.940   -16.790 1.00 0.00 ? 94  LEU A C     1 
ATOM   747  O  O     . LEU A 1 95  ? 17.096 3.664   -15.797 1.00 0.00 ? 94  LEU A O     1 
ATOM   748  C  CB    . LEU A 1 95  ? 18.185 2.282   -18.992 1.00 0.00 ? 94  LEU A CB    1 
ATOM   749  C  CG    . LEU A 1 95  ? 19.426 1.392   -19.094 1.00 0.00 ? 94  LEU A CG    1 
ATOM   750  C  CD1   . LEU A 1 95  ? 19.099 -0.101  -19.040 1.00 0.00 ? 94  LEU A CD1   1 
ATOM   751  C  CD2   . LEU A 1 95  ? 20.204 1.599   -20.395 1.00 0.00 ? 94  LEU A CD2   1 
ATOM   752  N  N     . ASN A 1 96  ? 16.575 1.822   -17.026 1.00 0.00 ? 95  ASN A N     1 
ATOM   753  C  CA    . ASN A 1 96  ? 15.518 1.342   -16.113 1.00 0.00 ? 95  ASN A CA    1 
ATOM   754  C  C     . ASN A 1 96  ? 15.889 0.030   -15.438 1.00 0.00 ? 95  ASN A C     1 
ATOM   755  O  O     . ASN A 1 96  ? 16.592 -0.811  -16.019 1.00 0.00 ? 95  ASN A O     1 
ATOM   756  C  CB    . ASN A 1 96  ? 14.200 1.121   -16.839 1.00 0.00 ? 95  ASN A CB    1 
ATOM   757  C  CG    . ASN A 1 96  ? 13.035 0.951   -15.861 1.00 0.00 ? 95  ASN A CG    1 
ATOM   758  O  OD1   . ASN A 1 96  ? 12.999 -0.023  -15.111 1.00 0.00 ? 95  ASN A OD1   1 
ATOM   759  N  ND2   . ASN A 1 96  ? 12.069 1.849   -15.823 1.00 0.00 ? 95  ASN A ND2   1 
ATOM   760  N  N     . ASP A 1 97  ? 15.382 -0.067  -14.219 1.00 0.00 ? 96  ASP A N     1 
ATOM   761  C  CA    . ASP A 1 97  ? 15.588 -1.224  -13.344 1.00 0.00 ? 96  ASP A CA    1 
ATOM   762  C  C     . ASP A 1 97  ? 14.706 -2.379  -13.803 1.00 0.00 ? 96  ASP A C     1 
ATOM   763  O  O     . ASP A 1 97  ? 14.915 -3.537  -13.413 1.00 0.00 ? 96  ASP A O     1 
ATOM   764  C  CB    . ASP A 1 97  ? 15.252 -0.858  -11.887 1.00 0.00 ? 96  ASP A CB    1 
ATOM   765  C  CG    . ASP A 1 97  ? 13.862 -0.235  -11.706 1.00 0.00 ? 96  ASP A CG    1 
ATOM   766  O  OD1   . ASP A 1 97  ? 13.616 0.942   -12.173 1.00 0.00 ? 96  ASP A OD1   1 
ATOM   767  O  OD2   . ASP A 1 97  ? 12.939 -0.888  -11.086 1.00 0.00 ? 96  ASP A OD2   1 
ATOM   768  N  N     . CYS A 1 98  ? 13.747 -2.014  -14.624 1.00 0.00 ? 97  CYS A N     1 
ATOM   769  C  CA    . CYS A 1 98  ? 12.792 -2.967  -15.190 1.00 0.00 ? 97  CYS A CA    1 
ATOM   770  C  C     . CYS A 1 98  ? 12.693 -2.793  -16.699 1.00 0.00 ? 97  CYS A C     1 
ATOM   771  O  O     . CYS A 1 98  ? 13.541 -3.290  -17.455 1.00 0.00 ? 97  CYS A O     1 
ATOM   772  C  CB    . CYS A 1 98  ? 11.394 -2.735  -14.611 1.00 0.00 ? 97  CYS A CB    1 
ATOM   773  S  SG    . CYS A 1 98  ? 11.388 -2.602  -12.796 1.00 0.00 ? 97  CYS A SG    1 
ATOM   774  N  N     . VAL A 1 99  ? 11.641 -2.072  -17.071 1.00 0.00 ? 98  VAL A N     1 
ATOM   775  C  CA    . VAL A 1 99  ? 11.303 -1.835  -18.481 1.00 0.00 ? 98  VAL A CA    1 
ATOM   776  C  C     . VAL A 1 99  ? 11.396 -0.370  -18.840 1.00 0.00 ? 98  VAL A C     1 
ATOM   777  O  O     . VAL A 1 99  ? 12.386 0.305   -18.520 1.00 0.00 ? 98  VAL A O     1 
ATOM   778  C  CB    . VAL A 1 99  ? 9.905  -2.375  -18.775 1.00 0.00 ? 98  VAL A CB    1 
ATOM   779  C  CG1   . VAL A 1 99  ? 9.674  -3.777  -18.208 1.00 0.00 ? 98  VAL A CG1   1 
ATOM   780  C  CG2   . VAL A 1 99  ? 8.792  -1.503  -18.191 1.00 0.00 ? 98  VAL A CG2   1 
ATOM   781  N  N     . GLY A 1 100 ? 10.340 0.034   -19.457 1.00 0.00 ? 99  GLY A N     1 
ATOM   782  C  CA    . GLY A 1 100 ? 10.241 1.309   -20.101 1.00 0.00 ? 99  GLY A CA    1 
ATOM   783  C  C     . GLY A 1 100 ? 10.357 0.929   -21.557 1.00 0.00 ? 99  GLY A C     1 
ATOM   784  O  O     . GLY A 1 100 ? 11.298 0.227   -21.960 1.00 0.00 ? 99  GLY A O     1 
ATOM   785  N  N     . PRO A 1 101 ? 9.461  1.347   -22.427 1.00 0.00 ? 100 PRO A N     1 
ATOM   786  C  CA    . PRO A 1 101 ? 9.496  0.884   -23.788 1.00 0.00 ? 100 PRO A CA    1 
ATOM   787  C  C     . PRO A 1 101 ? 10.880 1.113   -24.239 1.00 0.00 ? 100 PRO A C     1 
ATOM   788  O  O     . PRO A 1 101 ? 11.429 0.257   -25.001 1.00 0.00 ? 100 PRO A O     1 
ATOM   789  C  CB    . PRO A 1 101 ? 8.391  1.658   -24.456 1.00 0.00 ? 100 PRO A CB    1 
ATOM   790  C  CG    . PRO A 1 101 ? 7.735  2.537   -23.402 1.00 0.00 ? 100 PRO A CG    1 
ATOM   791  C  CD    . PRO A 1 101 ? 8.416  2.305   -22.090 1.00 0.00 ? 100 PRO A CD    1 
ATOM   792  N  N     . GLU A 1 102 ? 11.347 2.225   -23.768 1.00 0.00 ? 101 GLU A N     1 
ATOM   793  C  CA    . GLU A 1 102 ? 12.717 2.648   -23.953 1.00 0.00 ? 101 GLU A CA    1 
ATOM   794  C  C     . GLU A 1 102 ? 13.680 1.537   -23.464 1.00 0.00 ? 101 GLU A C     1 
ATOM   795  O  O     . GLU A 1 102 ? 14.709 1.258   -24.096 1.00 0.00 ? 101 GLU A O     1 
ATOM   796  C  CB    . GLU A 1 102 ? 12.972 3.946   -23.189 1.00 0.00 ? 101 GLU A CB    1 
ATOM   797  C  CG    . GLU A 1 102 ? 13.282 5.125   -24.116 1.00 0.00 ? 101 GLU A CG    1 
ATOM   798  C  CD    . GLU A 1 102 ? 12.177 6.184   -24.132 1.00 0.00 ? 101 GLU A CD    1 
ATOM   799  O  OE1   . GLU A 1 102 ? 11.823 6.731   -25.245 1.00 0.00 ? 101 GLU A OE1   1 
ATOM   800  O  OE2   . GLU A 1 102 ? 11.599 6.529   -23.031 1.00 0.00 ? 101 GLU A OE2   1 
ATOM   801  N  N     . VAL A 1 103 ? 13.354 0.902   -22.342 1.00 0.00 ? 102 VAL A N     1 
ATOM   802  C  CA    . VAL A 1 103 ? 14.250 -0.111  -21.709 1.00 0.00 ? 102 VAL A CA    1 
ATOM   803  C  C     . VAL A 1 103 ? 14.657 -1.298  -22.612 1.00 0.00 ? 102 VAL A C     1 
ATOM   804  O  O     . VAL A 1 103 ? 15.851 -1.576  -22.802 1.00 0.00 ? 102 VAL A O     1 
ATOM   805  C  CB    . VAL A 1 103 ? 13.543 -0.780  -20.526 1.00 0.00 ? 102 VAL A CB    1 
ATOM   806  C  CG1   . VAL A 1 103 ? 13.944 -2.245  -20.341 1.00 0.00 ? 102 VAL A CG1   1 
ATOM   807  C  CG2   . VAL A 1 103 ? 13.836 -0.097  -19.189 1.00 0.00 ? 102 VAL A CG2   1 
ATOM   808  N  N     . GLU A 1 104 ? 13.682 -1.993  -23.174 1.00 0.00 ? 103 GLU A N     1 
ATOM   809  C  CA    . GLU A 1 104 ? 13.982 -3.152  -24.037 1.00 0.00 ? 103 GLU A CA    1 
ATOM   810  C  C     . GLU A 1 104 ? 14.863 -2.666  -25.172 1.00 0.00 ? 103 GLU A C     1 
ATOM   811  O  O     . GLU A 1 104 ? 15.833 -3.335  -25.559 1.00 0.00 ? 103 GLU A O     1 
ATOM   812  C  CB    . GLU A 1 104 ? 12.713 -3.845  -24.550 1.00 0.00 ? 103 GLU A CB    1 
ATOM   813  C  CG    . GLU A 1 104 ? 12.688 -5.357  -24.238 1.00 0.00 ? 103 GLU A CG    1 
ATOM   814  C  CD    . GLU A 1 104 ? 13.734 -6.172  -25.017 1.00 0.00 ? 103 GLU A CD    1 
ATOM   815  O  OE1   . GLU A 1 104 ? 13.430 -6.687  -26.160 1.00 0.00 ? 103 GLU A OE1   1 
ATOM   816  O  OE2   . GLU A 1 104 ? 14.916 -6.341  -24.529 1.00 0.00 ? 103 GLU A OE2   1 
ATOM   817  N  N     . ALA A 1 105 ? 14.486 -1.517  -25.668 1.00 0.00 ? 104 ALA A N     1 
ATOM   818  C  CA    . ALA A 1 105 ? 15.169 -0.874  -26.793 1.00 0.00 ? 104 ALA A CA    1 
ATOM   819  C  C     . ALA A 1 105 ? 16.668 -0.606  -26.547 1.00 0.00 ? 104 ALA A C     1 
ATOM   820  O  O     . ALA A 1 105 ? 17.523 -0.958  -27.373 1.00 0.00 ? 104 ALA A O     1 
ATOM   821  C  CB    . ALA A 1 105 ? 14.523 0.481   -27.091 1.00 0.00 ? 104 ALA A CB    1 
ATOM   822  N  N     . ALA A 1 106 ? 16.980 0.003   -25.424 1.00 0.00 ? 105 ALA A N     1 
ATOM   823  C  CA    . ALA A 1 106 ? 18.359 0.445   -25.118 1.00 0.00 ? 105 ALA A CA    1 
ATOM   824  C  C     . ALA A 1 106 ? 19.395 -0.679  -25.108 1.00 0.00 ? 105 ALA A C     1 
ATOM   825  O  O     . ALA A 1 106 ? 20.447 -0.585  -25.757 1.00 0.00 ? 105 ALA A O     1 
ATOM   826  C  CB    . ALA A 1 106 ? 18.409 1.095   -23.734 1.00 0.00 ? 105 ALA A CB    1 
ATOM   827  N  N     . VAL A 1 107 ? 19.090 -1.727  -24.386 1.00 0.00 ? 106 VAL A N     1 
ATOM   828  C  CA    . VAL A 1 107 ? 20.040 -2.825  -24.217 1.00 0.00 ? 106 VAL A CA    1 
ATOM   829  C  C     . VAL A 1 107 ? 20.463 -3.346  -25.574 1.00 0.00 ? 106 VAL A C     1 
ATOM   830  O  O     . VAL A 1 107 ? 21.661 -3.504  -25.853 1.00 0.00 ? 106 VAL A O     1 
ATOM   831  C  CB    . VAL A 1 107 ? 19.386 -3.975  -23.446 1.00 0.00 ? 106 VAL A CB    1 
ATOM   832  C  CG1   . VAL A 1 107 ? 20.362 -5.107  -23.117 1.00 0.00 ? 106 VAL A CG1   1 
ATOM   833  C  CG2   . VAL A 1 107 ? 18.793 -3.537  -22.105 1.00 0.00 ? 106 VAL A CG2   1 
ATOM   834  N  N     . LYS A 1 108 ? 19.459 -3.595  -26.371 1.00 0.00 ? 107 LYS A N     1 
ATOM   835  C  CA    . LYS A 1 108 ? 19.631 -4.118  -27.726 1.00 0.00 ? 107 LYS A CA    1 
ATOM   836  C  C     . LYS A 1 108 ? 20.445 -3.175  -28.618 1.00 0.00 ? 107 LYS A C     1 
ATOM   837  O  O     . LYS A 1 108 ? 21.417 -3.589  -29.266 1.00 0.00 ? 107 LYS A O     1 
ATOM   838  C  CB    . LYS A 1 108 ? 18.266 -4.297  -28.380 1.00 0.00 ? 107 LYS A CB    1 
ATOM   839  C  CG    . LYS A 1 108 ? 18.260 -5.374  -29.460 1.00 0.00 ? 107 LYS A CG    1 
ATOM   840  C  CD    . LYS A 1 108 ? 17.048 -6.300  -29.366 1.00 0.00 ? 107 LYS A CD    1 
ATOM   841  C  CE    . LYS A 1 108 ? 16.953 -7.278  -30.538 1.00 0.00 ? 107 LYS A CE    1 
ATOM   842  N  NZ    . LYS A 1 108 ? 15.643 -7.249  -31.205 1.00 0.00 ? 107 LYS A NZ    1 
ATOM   843  N  N     . ALA A 1 109 ? 20.022 -1.928  -28.612 1.00 0.00 ? 108 ALA A N     1 
ATOM   844  C  CA    . ALA A 1 109 ? 20.609 -0.876  -29.457 1.00 0.00 ? 108 ALA A CA    1 
ATOM   845  C  C     . ALA A 1 109 ? 22.134 -0.971  -29.481 1.00 0.00 ? 108 ALA A C     1 
ATOM   846  O  O     . ALA A 1 109 ? 22.719 -1.622  -30.360 1.00 0.00 ? 108 ALA A O     1 
ATOM   847  C  CB    . ALA A 1 109 ? 20.221 0.504   -28.921 1.00 0.00 ? 108 ALA A CB    1 
ATOM   848  N  N     . SER A 1 110 ? 22.712 -0.312  -28.498 1.00 0.00 ? 109 SER A N     1 
ATOM   849  C  CA    . SER A 1 110 ? 24.167 -0.203  -28.334 1.00 0.00 ? 109 SER A CA    1 
ATOM   850  C  C     . SER A 1 110 ? 24.805 -1.535  -27.937 1.00 0.00 ? 109 SER A C     1 
ATOM   851  O  O     . SER A 1 110 ? 24.628 -2.017  -26.808 1.00 0.00 ? 109 SER A O     1 
ATOM   852  C  CB    . SER A 1 110 ? 24.496 0.816   -27.242 1.00 0.00 ? 109 SER A CB    1 
ATOM   853  O  OG    . SER A 1 110 ? 24.114 2.118   -27.661 1.00 0.00 ? 109 SER A OG    1 
ATOM   854  N  N     . ALA A 1 111 ? 25.532 -2.065  -28.900 1.00 0.00 ? 110 ALA A N     1 
ATOM   855  C  CA    . ALA A 1 111 ? 26.241 -3.345  -28.780 1.00 0.00 ? 110 ALA A CA    1 
ATOM   856  C  C     . ALA A 1 111 ? 26.778 -3.556  -27.362 1.00 0.00 ? 110 ALA A C     1 
ATOM   857  O  O     . ALA A 1 111 ? 26.075 -3.312  -26.370 1.00 0.00 ? 110 ALA A O     1 
ATOM   858  C  CB    . ALA A 1 111 ? 27.426 -3.379  -29.748 1.00 0.00 ? 110 ALA A CB    1 
ATOM   859  N  N     . PRO A 1 112 ? 28.033 -4.014  -27.223 1.00 0.00 ? 111 PRO A N     1 
ATOM   860  C  CA    . PRO A 1 112 ? 28.619 -4.286  -25.924 1.00 0.00 ? 111 PRO A CA    1 
ATOM   861  C  C     . PRO A 1 112 ? 28.648 -3.053  -25.089 1.00 0.00 ? 111 PRO A C     1 
ATOM   862  O  O     . PRO A 1 112 ? 29.049 -1.966  -25.608 1.00 0.00 ? 111 PRO A O     1 
ATOM   863  C  CB    . PRO A 1 112 ? 30.013 -4.770  -26.240 1.00 0.00 ? 111 PRO A CB    1 
ATOM   864  C  CG    . PRO A 1 112 ? 30.178 -4.758  -27.753 1.00 0.00 ? 111 PRO A CG    1 
ATOM   865  C  CD    . PRO A 1 112 ? 28.906 -4.273  -28.372 1.00 0.00 ? 111 PRO A CD    1 
ATOM   866  N  N     . GLY A 1 113 ? 28.237 -3.241  -23.857 1.00 0.00 ? 112 GLY A N     1 
ATOM   867  C  CA    . GLY A 1 113 ? 28.189 -2.164  -22.876 1.00 0.00 ? 112 GLY A CA    1 
ATOM   868  C  C     . GLY A 1 113 ? 27.824 -2.715  -21.505 1.00 0.00 ? 112 GLY A C     1 
ATOM   869  O  O     . GLY A 1 113 ? 27.491 -3.901  -21.361 1.00 0.00 ? 112 GLY A O     1 
ATOM   870  N  N     . SER A 1 114 ? 27.925 -1.815  -20.566 1.00 0.00 ? 113 SER A N     1 
ATOM   871  C  CA    . SER A 1 114 ? 27.599 -2.050  -19.163 1.00 0.00 ? 113 SER A CA    1 
ATOM   872  C  C     . SER A 1 114 ? 26.533 -1.053  -18.712 1.00 0.00 ? 113 SER A C     1 
ATOM   873  O  O     . SER A 1 114 ? 26.769 0.163   -18.679 1.00 0.00 ? 113 SER A O     1 
ATOM   874  C  CB    . SER A 1 114 ? 28.847 -1.886  -18.304 1.00 0.00 ? 113 SER A CB    1 
ATOM   875  O  OG    . SER A 1 114 ? 28.848 -0.607  -17.689 1.00 0.00 ? 113 SER A OG    1 
ATOM   876  N  N     . VAL A 1 115 ? 25.410 -1.610  -18.379 1.00 0.00 ? 114 VAL A N     1 
ATOM   877  C  CA    . VAL A 1 115 ? 24.222 -0.873  -17.947 1.00 0.00 ? 114 VAL A CA    1 
ATOM   878  C  C     . VAL A 1 115 ? 23.884 -1.233  -16.506 1.00 0.00 ? 114 VAL A C     1 
ATOM   879  O  O     . VAL A 1 115 ? 23.696 -2.411  -16.169 1.00 0.00 ? 114 VAL A O     1 
ATOM   880  C  CB    . VAL A 1 115 ? 23.009 -1.191  -18.822 1.00 0.00 ? 114 VAL A CB    1 
ATOM   881  C  CG1   . VAL A 1 115 ? 22.386 0.055   -19.456 1.00 0.00 ? 114 VAL A CG1   1 
ATOM   882  C  CG2   . VAL A 1 115 ? 23.339 -2.127  -19.986 1.00 0.00 ? 114 VAL A CG2   1 
ATOM   883  N  N     . ILE A 1 116 ? 23.827 -0.206  -15.693 1.00 0.00 ? 115 ILE A N     1 
ATOM   884  C  CA    . ILE A 1 116 ? 23.507 -0.329  -14.268 1.00 0.00 ? 115 ILE A CA    1 
ATOM   885  C  C     . ILE A 1 116 ? 22.128 0.295   -14.054 1.00 0.00 ? 115 ILE A C     1 
ATOM   886  O  O     . ILE A 1 116 ? 21.934 1.504   -14.249 1.00 0.00 ? 115 ILE A O     1 
ATOM   887  C  CB    . ILE A 1 116 ? 24.553 0.423   -13.438 1.00 0.00 ? 115 ILE A CB    1 
ATOM   888  C  CG1   . ILE A 1 116 ? 24.085 1.813   -13.000 1.00 0.00 ? 115 ILE A CG1   1 
ATOM   889  C  CG2   . ILE A 1 116 ? 25.866 0.646   -14.191 1.00 0.00 ? 115 ILE A CG2   1 
ATOM   890  C  CD1   . ILE A 1 116 ? 24.413 2.904   -14.021 1.00 0.00 ? 115 ILE A CD1   1 
ATOM   891  N  N     . LEU A 1 117 ? 21.192 -0.560  -13.660 1.00 0.00 ? 116 LEU A N     1 
ATOM   892  C  CA    . LEU A 1 117 ? 19.788 -0.145  -13.524 1.00 0.00 ? 116 LEU A CA    1 
ATOM   893  C  C     . LEU A 1 117 ? 18.996 -0.947  -12.490 1.00 0.00 ? 116 LEU A C     1 
ATOM   894  O  O     . LEU A 1 117 ? 19.214 -2.154  -12.313 1.00 0.00 ? 116 LEU A O     1 
ATOM   895  C  CB    . LEU A 1 117 ? 19.074 -0.427  -14.840 1.00 0.00 ? 116 LEU A CB    1 
ATOM   896  C  CG    . LEU A 1 117 ? 19.053 -1.925  -15.167 1.00 0.00 ? 116 LEU A CG    1 
ATOM   897  C  CD1   . LEU A 1 117 ? 17.648 -2.529  -15.122 1.00 0.00 ? 116 LEU A CD1   1 
ATOM   898  C  CD2   . LEU A 1 117 ? 19.595 -2.243  -16.562 1.00 0.00 ? 116 LEU A CD2   1 
ATOM   899  N  N     . LEU A 1 118 ? 18.086 -0.233  -11.823 1.00 0.00 ? 117 LEU A N     1 
ATOM   900  C  CA    . LEU A 1 118 ? 17.129 -0.871  -10.908 1.00 0.00 ? 117 LEU A CA    1 
ATOM   901  C  C     . LEU A 1 118 ? 17.221 -0.374  -9.442  1.00 0.00 ? 117 LEU A C     1 
ATOM   902  O  O     . LEU A 1 118 ? 16.744 0.721   -9.107  1.00 0.00 ? 117 LEU A O     1 
ATOM   903  C  CB    . LEU A 1 118 ? 17.332 -2.393  -11.007 1.00 0.00 ? 117 LEU A CB    1 
ATOM   904  C  CG    . LEU A 1 118 ? 17.487 -3.103  -9.666  1.00 0.00 ? 117 LEU A CG    1 
ATOM   905  C  CD1   . LEU A 1 118 ? 16.224 -3.038  -8.806  1.00 0.00 ? 117 LEU A CD1   1 
ATOM   906  C  CD2   . LEU A 1 118 ? 17.811 -4.591  -9.816  1.00 0.00 ? 117 LEU A CD2   1 
ATOM   907  N  N     . GLU A 1 119 ? 17.833 -1.194  -8.613  1.00 0.00 ? 118 GLU A N     1 
ATOM   908  C  CA    . GLU A 1 119 ? 17.909 -0.989  -7.150  1.00 0.00 ? 118 GLU A CA    1 
ATOM   909  C  C     . GLU A 1 119 ? 16.698 -1.683  -6.523  1.00 0.00 ? 118 GLU A C     1 
ATOM   910  O  O     . GLU A 1 119 ? 16.565 -2.914  -6.586  1.00 0.00 ? 118 GLU A O     1 
ATOM   911  C  CB    . GLU A 1 119 ? 17.845 0.497   -6.734  1.00 0.00 ? 118 GLU A CB    1 
ATOM   912  C  CG    . GLU A 1 119 ? 18.163 1.502   -7.843  1.00 0.00 ? 118 GLU A CG    1 
ATOM   913  C  CD    . GLU A 1 119 ? 17.887 2.951   -7.413  1.00 0.00 ? 118 GLU A CD    1 
ATOM   914  O  OE1   . GLU A 1 119 ? 18.192 3.927   -8.200  1.00 0.00 ? 118 GLU A OE1   1 
ATOM   915  O  OE2   . GLU A 1 119 ? 17.350 3.193   -6.265  1.00 0.00 ? 118 GLU A OE2   1 
ATOM   916  N  N     . ASN A 1 120 ? 15.865 -0.854  -5.938  1.00 0.00 ? 119 ASN A N     1 
ATOM   917  C  CA    . ASN A 1 120 ? 14.595 -1.259  -5.321  1.00 0.00 ? 119 ASN A CA    1 
ATOM   918  C  C     . ASN A 1 120 ? 13.691 -0.043  -5.297  1.00 0.00 ? 119 ASN A C     1 
ATOM   919  O  O     . ASN A 1 120 ? 13.153 0.331   -4.244  1.00 0.00 ? 119 ASN A O     1 
ATOM   920  C  CB    . ASN A 1 120 ? 14.803 -1.803  -3.908  1.00 0.00 ? 119 ASN A CB    1 
ATOM   921  C  CG    . ASN A 1 120 ? 16.270 -2.028  -3.563  1.00 0.00 ? 119 ASN A CG    1 
ATOM   922  O  OD1   . ASN A 1 120 ? 16.692 -3.171  -3.392  1.00 0.00 ? 119 ASN A OD1   1 
ATOM   923  N  ND2   . ASN A 1 120 ? 17.085 -0.998  -3.448  1.00 0.00 ? 119 ASN A ND2   1 
ATOM   924  N  N     . LEU A 1 121 ? 13.615 0.487   -6.500  1.00 0.00 ? 120 LEU A N     1 
ATOM   925  C  CA    . LEU A 1 121 ? 12.804 1.641   -6.852  1.00 0.00 ? 120 LEU A CA    1 
ATOM   926  C  C     . LEU A 1 121 ? 11.422 1.150   -7.227  1.00 0.00 ? 120 LEU A C     1 
ATOM   927  O  O     . LEU A 1 121 ? 10.406 1.670   -6.743  1.00 0.00 ? 120 LEU A O     1 
ATOM   928  C  CB    . LEU A 1 121 ? 13.402 2.336   -8.080  1.00 0.00 ? 120 LEU A CB    1 
ATOM   929  C  CG    . LEU A 1 121 ? 14.311 3.517   -7.739  1.00 0.00 ? 120 LEU A CG    1 
ATOM   930  C  CD1   . LEU A 1 121 ? 15.045 3.342   -6.408  1.00 0.00 ? 120 LEU A CD1   1 
ATOM   931  C  CD2   . LEU A 1 121 ? 15.401 3.754   -8.786  1.00 0.00 ? 120 LEU A CD2   1 
ATOM   932  N  N     . ARG A 1 122 ? 11.446 0.156   -8.092  1.00 0.00 ? 121 ARG A N     1 
ATOM   933  C  CA    . ARG A 1 122 ? 10.225 -0.469  -8.583  1.00 0.00 ? 121 ARG A CA    1 
ATOM   934  C  C     . ARG A 1 122 ? 9.704  -1.449  -7.551  1.00 0.00 ? 121 ARG A C     1 
ATOM   935  O  O     . ARG A 1 122 ? 9.780  -2.673  -7.737  1.00 0.00 ? 121 ARG A O     1 
ATOM   936  C  CB    . ARG A 1 122 ? 10.467 -1.197  -9.904  1.00 0.00 ? 121 ARG A CB    1 
ATOM   937  C  CG    . ARG A 1 122 ? 9.391  -0.881  -10.948 1.00 0.00 ? 121 ARG A CG    1 
ATOM   938  C  CD    . ARG A 1 122 ? 8.612  -2.115  -11.410 1.00 0.00 ? 121 ARG A CD    1 
ATOM   939  N  NE    . ARG A 1 122 ? 8.941  -2.506  -12.790 1.00 0.00 ? 121 ARG A NE    1 
ATOM   940  C  CZ    . ARG A 1 122 ? 8.190  -3.319  -13.546 1.00 0.00 ? 121 ARG A CZ    1 
ATOM   941  N  NH1   . ARG A 1 122 ? 7.051  -3.844  -13.075 1.00 0.00 ? 121 ARG A NH1   1 
ATOM   942  N  NH2   . ARG A 1 122 ? 8.498  -3.671  -14.802 1.00 0.00 ? 121 ARG A NH2   1 
ATOM   943  N  N     . TYR A 1 123 ? 9.188  -0.857  -6.487  1.00 0.00 ? 122 TYR A N     1 
ATOM   944  C  CA    . TYR A 1 123 ? 8.598  -1.623  -5.411  1.00 0.00 ? 122 TYR A CA    1 
ATOM   945  C  C     . TYR A 1 123 ? 8.145  -2.922  -5.984  1.00 0.00 ? 122 TYR A C     1 
ATOM   946  O  O     . TYR A 1 123 ? 6.949  -3.122  -6.245  1.00 0.00 ? 122 TYR A O     1 
ATOM   947  C  CB    . TYR A 1 123 ? 7.342  -0.959  -4.875  1.00 0.00 ? 122 TYR A CB    1 
ATOM   948  C  CG    . TYR A 1 123 ? 6.152  -1.929  -4.866  1.00 0.00 ? 122 TYR A CG    1 
ATOM   949  C  CD1   . TYR A 1 123 ? 4.920  -1.542  -5.409  1.00 0.00 ? 122 TYR A CD1   1 
ATOM   950  C  CD2   . TYR A 1 123 ? 6.297  -3.212  -4.318  1.00 0.00 ? 122 TYR A CD2   1 
ATOM   951  C  CE1   . TYR A 1 123 ? 3.833  -2.428  -5.391  1.00 0.00 ? 122 TYR A CE1   1 
ATOM   952  C  CE2   . TYR A 1 123 ? 5.210  -4.098  -4.299  1.00 0.00 ? 122 TYR A CE2   1 
ATOM   953  C  CZ    . TYR A 1 123 ? 3.977  -3.704  -4.833  1.00 0.00 ? 122 TYR A CZ    1 
ATOM   954  O  OH    . TYR A 1 123 ? 2.919  -4.559  -4.809  1.00 0.00 ? 122 TYR A OH    1 
ATOM   955  N  N     . HIS A 1 124 ? 9.093  -3.757  -6.169  1.00 0.00 ? 123 HIS A N     1 
ATOM   956  C  CA    . HIS A 1 124 ? 8.841  -5.039  -6.762  1.00 0.00 ? 123 HIS A CA    1 
ATOM   957  C  C     . HIS A 1 124 ? 9.977  -5.965  -6.387  1.00 0.00 ? 123 HIS A C     1 
ATOM   958  O  O     . HIS A 1 124 ? 9.856  -7.195  -6.480  1.00 0.00 ? 123 HIS A O     1 
ATOM   959  C  CB    . HIS A 1 124 ? 8.722  -4.846  -8.276  1.00 0.00 ? 123 HIS A CB    1 
ATOM   960  C  CG    . HIS A 1 124 ? 7.282  -4.565  -8.732  1.00 0.00 ? 123 HIS A CG    1 
ATOM   961  N  ND1   . HIS A 1 124 ? 6.969  -3.551  -9.638  1.00 0.00 ? 123 HIS A ND1   1 
ATOM   962  C  CD2   . HIS A 1 124 ? 6.103  -5.160  -8.411  1.00 0.00 ? 123 HIS A CD2   1 
ATOM   963  C  CE1   . HIS A 1 124 ? 5.662  -3.564  -9.836  1.00 0.00 ? 123 HIS A CE1   1 
ATOM   964  N  NE2   . HIS A 1 124 ? 5.133  -4.516  -9.112  1.00 0.00 ? 123 HIS A NE2   1 
ATOM   965  N  N     . ILE A 1 125 ? 11.049 -5.328  -5.970  1.00 0.00 ? 124 ILE A N     1 
ATOM   966  C  CA    . ILE A 1 125 ? 12.257 -6.025  -5.535  1.00 0.00 ? 124 ILE A CA    1 
ATOM   967  C  C     . ILE A 1 125 ? 12.190 -6.306  -4.042  1.00 0.00 ? 124 ILE A C     1 
ATOM   968  O  O     . ILE A 1 125 ? 13.141 -6.835  -3.448  1.00 0.00 ? 124 ILE A O     1 
ATOM   969  C  CB    . ILE A 1 125 ? 13.501 -5.168  -5.781  1.00 0.00 ? 124 ILE A CB    1 
ATOM   970  C  CG1   . ILE A 1 125 ? 14.136 -4.660  -4.483  1.00 0.00 ? 124 ILE A CG1   1 
ATOM   971  C  CG2   . ILE A 1 125 ? 13.214 -3.920  -6.617  1.00 0.00 ? 124 ILE A CG2   1 
ATOM   972  C  CD1   . ILE A 1 125 ? 15.639 -4.405  -4.611  1.00 0.00 ? 124 ILE A CD1   1 
ATOM   973  N  N     . GLU A 1 126 ? 11.068 -5.958  -3.453  1.00 0.00 ? 125 GLU A N     1 
ATOM   974  C  CA    . GLU A 1 126 ? 10.886 -6.135  -2.008  1.00 0.00 ? 125 GLU A CA    1 
ATOM   975  C  C     . GLU A 1 126 ? 9.740  -7.103  -1.690  1.00 0.00 ? 125 GLU A C     1 
ATOM   976  O  O     . GLU A 1 126 ? 9.830  -8.309  -1.961  1.00 0.00 ? 125 GLU A O     1 
ATOM   977  C  CB    . GLU A 1 126 ? 10.561 -4.787  -1.344  1.00 0.00 ? 125 GLU A CB    1 
ATOM   978  C  CG    . GLU A 1 126 ? 10.984 -3.578  -2.188  1.00 0.00 ? 125 GLU A CG    1 
ATOM   979  C  CD    . GLU A 1 126 ? 12.173 -2.816  -1.595  1.00 0.00 ? 125 GLU A CD    1 
ATOM   980  O  OE1   . GLU A 1 126 ? 12.736 -1.871  -2.270  1.00 0.00 ? 125 GLU A OE1   1 
ATOM   981  O  OE2   . GLU A 1 126 ? 12.613 -3.119  -0.421  1.00 0.00 ? 125 GLU A OE2   1 
ATOM   982  N  N     . GLU A 1 127 ? 8.753  -6.460  -1.132  1.00 0.00 ? 126 GLU A N     1 
ATOM   983  C  CA    . GLU A 1 127 ? 7.503  -7.010  -0.619  1.00 0.00 ? 126 GLU A CA    1 
ATOM   984  C  C     . GLU A 1 127 ? 7.002  -5.912  0.344   1.00 0.00 ? 126 GLU A C     1 
ATOM   985  O  O     . GLU A 1 127 ? 7.312  -5.926  1.545   1.00 0.00 ? 126 GLU A O     1 
ATOM   986  C  CB    . GLU A 1 127 ? 7.767  -8.388  0.048   1.00 0.00 ? 126 GLU A CB    1 
ATOM   987  C  CG    . GLU A 1 127 ? 7.979  -9.536  -0.969  1.00 0.00 ? 126 GLU A CG    1 
ATOM   988  C  CD    . GLU A 1 127 ? 7.974  -10.944 -0.342  1.00 0.00 ? 126 GLU A CD    1 
ATOM   989  O  OE1   . GLU A 1 127 ? 7.678  -11.095 0.905   1.00 0.00 ? 126 GLU A OE1   1 
ATOM   990  O  OE2   . GLU A 1 127 ? 8.265  -11.974 -1.063  1.00 0.00 ? 126 GLU A OE2   1 
ATOM   991  N  N     . GLU A 1 128 ? 6.248  -4.991  -0.255  1.00 0.00 ? 127 GLU A N     1 
ATOM   992  C  CA    . GLU A 1 128 ? 5.730  -3.747  0.384   1.00 0.00 ? 127 GLU A CA    1 
ATOM   993  C  C     . GLU A 1 128 ? 5.604  -3.827  1.913   1.00 0.00 ? 127 GLU A C     1 
ATOM   994  O  O     . GLU A 1 128 ? 5.305  -4.892  2.475   1.00 0.00 ? 127 GLU A O     1 
ATOM   995  C  CB    . GLU A 1 128 ? 4.376  -3.349  -0.192  1.00 0.00 ? 127 GLU A CB    1 
ATOM   996  C  CG    . GLU A 1 128 ? 4.408  -1.945  -0.802  1.00 0.00 ? 127 GLU A CG    1 
ATOM   997  C  CD    . GLU A 1 128 ? 5.810  -1.540  -1.274  1.00 0.00 ? 127 GLU A CD    1 
ATOM   998  O  OE1   . GLU A 1 128 ? 6.016  -0.355  -1.741  1.00 0.00 ? 127 GLU A OE1   1 
ATOM   999  O  OE2   . GLU A 1 128 ? 6.783  -2.384  -1.205  1.00 0.00 ? 127 GLU A OE2   1 
ATOM   1000 N  N     . GLY A 1 129 ? 5.856  -2.646  2.488   1.00 0.00 ? 128 GLY A N     1 
ATOM   1001 C  CA    . GLY A 1 129 ? 5.842  -2.392  3.944   1.00 0.00 ? 128 GLY A CA    1 
ATOM   1002 C  C     . GLY A 1 129 ? 4.439  -2.594  4.505   1.00 0.00 ? 128 GLY A C     1 
ATOM   1003 O  O     . GLY A 1 129 ? 3.616  -1.666  4.520   1.00 0.00 ? 128 GLY A O     1 
ATOM   1004 N  N     . SER A 1 130 ? 4.235  -3.812  4.955   1.00 0.00 ? 129 SER A N     1 
ATOM   1005 C  CA    . SER A 1 130 ? 2.953  -4.258  5.496   1.00 0.00 ? 129 SER A CA    1 
ATOM   1006 C  C     . SER A 1 130 ? 2.488  -3.397  6.680   1.00 0.00 ? 129 SER A C     1 
ATOM   1007 O  O     . SER A 1 130 ? 2.584  -2.161  6.648   1.00 0.00 ? 129 SER A O     1 
ATOM   1008 C  CB    . SER A 1 130 ? 3.044  -5.710  5.971   1.00 0.00 ? 129 SER A CB    1 
ATOM   1009 O  OG    . SER A 1 130 ? 4.395  -6.047  6.247   1.00 0.00 ? 129 SER A OG    1 
ATOM   1010 N  N     . ARG A 1 131 ? 2.002  -4.100  7.703   1.00 0.00 ? 130 ARG A N     1 
ATOM   1011 C  CA    . ARG A 1 131 ? 1.358  -3.472  8.875   1.00 0.00 ? 130 ARG A CA    1 
ATOM   1012 C  C     . ARG A 1 131 ? 0.666  -2.202  8.413   1.00 0.00 ? 130 ARG A C     1 
ATOM   1013 O  O     . ARG A 1 131 ? 1.320  -1.209  8.062   1.00 0.00 ? 130 ARG A O     1 
ATOM   1014 C  CB    . ARG A 1 131 ? 2.335  -3.134  10.016  1.00 0.00 ? 130 ARG A CB    1 
ATOM   1015 C  CG    . ARG A 1 131 ? 1.624  -3.088  11.390  1.00 0.00 ? 130 ARG A CG    1 
ATOM   1016 C  CD    . ARG A 1 131 ? 2.313  -2.184  12.426  1.00 0.00 ? 130 ARG A CD    1 
ATOM   1017 N  NE    . ARG A 1 131 ? 3.446  -2.845  13.102  1.00 0.00 ? 130 ARG A NE    1 
ATOM   1018 C  CZ    . ARG A 1 131 ? 3.834  -2.604  14.367  1.00 0.00 ? 130 ARG A CZ    1 
ATOM   1019 N  NH1   . ARG A 1 131 ? 3.189  -1.711  15.130  1.00 0.00 ? 130 ARG A NH1   1 
ATOM   1020 N  NH2   . ARG A 1 131 ? 4.871  -3.211  14.961  1.00 0.00 ? 130 ARG A NH2   1 
ATOM   1021 N  N     . LYS A 1 132 ? -0.646 -2.285  8.424   1.00 0.00 ? 131 LYS A N     1 
ATOM   1022 C  CA    . LYS A 1 132 ? -1.511 -1.178  8.014   1.00 0.00 ? 131 LYS A CA    1 
ATOM   1023 C  C     . LYS A 1 132 ? -0.903 0.153   8.471   1.00 0.00 ? 131 LYS A C     1 
ATOM   1024 O  O     . LYS A 1 132 ? 0.171  0.559   8.000   1.00 0.00 ? 131 LYS A O     1 
ATOM   1025 C  CB    . LYS A 1 132 ? -2.898 -1.341  8.644   1.00 0.00 ? 131 LYS A CB    1 
ATOM   1026 C  CG    . LYS A 1 132 ? -3.133 -2.737  9.229   1.00 0.00 ? 131 LYS A CG    1 
ATOM   1027 C  CD    . LYS A 1 132 ? -4.585 -2.973  9.651   1.00 0.00 ? 131 LYS A CD    1 
ATOM   1028 C  CE    . LYS A 1 132 ? -4.823 -4.374  10.220  1.00 0.00 ? 131 LYS A CE    1 
ATOM   1029 N  NZ    . LYS A 1 132 ? -4.796 -4.410  11.689  1.00 0.00 ? 131 LYS A NZ    1 
ATOM   1030 N  N     . VAL A 1 133 ? -1.622 0.782   9.381   1.00 0.00 ? 132 VAL A N     1 
ATOM   1031 C  CA    . VAL A 1 133 ? -1.256 2.086   9.974   1.00 0.00 ? 132 VAL A CA    1 
ATOM   1032 C  C     . VAL A 1 133 ? 0.267  2.324   9.935   1.00 0.00 ? 132 VAL A C     1 
ATOM   1033 O  O     . VAL A 1 133 ? 1.064  1.390   10.106  1.00 0.00 ? 132 VAL A O     1 
ATOM   1034 C  CB    . VAL A 1 133 ? -1.707 2.128   11.435  1.00 0.00 ? 132 VAL A CB    1 
ATOM   1035 C  CG1   . VAL A 1 133 ? -1.383 3.456   12.123  1.00 0.00 ? 132 VAL A CG1   1 
ATOM   1036 C  CG2   . VAL A 1 133 ? -3.215 1.932   11.602  1.00 0.00 ? 132 VAL A CG2   1 
ATOM   1037 N  N     . ASP A 1 134 ? 0.620  3.594   9.712   1.00 0.00 ? 133 ASP A N     1 
ATOM   1038 C  CA    . ASP A 1 134 ? 2.027  4.056   9.646   1.00 0.00 ? 133 ASP A CA    1 
ATOM   1039 C  C     . ASP A 1 134 ? 2.618  3.721   8.272   1.00 0.00 ? 133 ASP A C     1 
ATOM   1040 O  O     . ASP A 1 134 ? 2.699  2.547   7.881   1.00 0.00 ? 133 ASP A O     1 
ATOM   1041 C  CB    . ASP A 1 134 ? 2.839  3.363   10.736  1.00 0.00 ? 133 ASP A CB    1 
ATOM   1042 C  CG    . ASP A 1 134 ? 4.302  3.796   10.753  1.00 0.00 ? 133 ASP A CG    1 
ATOM   1043 O  OD1   . ASP A 1 134 ? 4.750  4.588   9.839   1.00 0.00 ? 133 ASP A OD1   1 
ATOM   1044 O  OD2   . ASP A 1 134 ? 5.089  3.369   11.681  1.00 0.00 ? 133 ASP A OD2   1 
ATOM   1045 N  N     . GLY A 1 135 ? 3.036  4.761   7.567   1.00 0.00 ? 134 GLY A N     1 
ATOM   1046 C  CA    . GLY A 1 135 ? 3.520  4.612   6.193   1.00 0.00 ? 134 GLY A CA    1 
ATOM   1047 C  C     . GLY A 1 135 ? 2.364  4.002   5.411   1.00 0.00 ? 134 GLY A C     1 
ATOM   1048 O  O     . GLY A 1 135 ? 1.594  3.187   5.940   1.00 0.00 ? 134 GLY A O     1 
ATOM   1049 N  N     . GLN A 1 136 ? 2.223  4.378   4.171   1.00 0.00 ? 135 GLN A N     1 
ATOM   1050 C  CA    . GLN A 1 136 ? 1.103  3.878   3.371   1.00 0.00 ? 135 GLN A CA    1 
ATOM   1051 C  C     . GLN A 1 136 ? 1.499  2.642   2.575   1.00 0.00 ? 135 GLN A C     1 
ATOM   1052 O  O     . GLN A 1 136 ? 2.622  2.132   2.702   1.00 0.00 ? 135 GLN A O     1 
ATOM   1053 C  CB    . GLN A 1 136 ? 0.614  4.961   2.420   1.00 0.00 ? 135 GLN A CB    1 
ATOM   1054 C  CG    . GLN A 1 136 ? -0.811 5.396   2.744   1.00 0.00 ? 135 GLN A CG    1 
ATOM   1055 C  CD    . GLN A 1 136 ? -1.613 4.291   3.437   1.00 0.00 ? 135 GLN A CD    1 
ATOM   1056 O  OE1   . GLN A 1 136 ? -2.127 3.395   2.770   1.00 0.00 ? 135 GLN A OE1   1 
ATOM   1057 N  NE2   . GLN A 1 136 ? -1.752 4.301   4.749   1.00 0.00 ? 135 GLN A NE2   1 
ATOM   1058 N  N     . LYS A 1 137 ? 0.536  2.221   1.788   1.00 0.00 ? 136 LYS A N     1 
ATOM   1059 C  CA    . LYS A 1 137 ? 0.654  1.057   0.913   1.00 0.00 ? 136 LYS A CA    1 
ATOM   1060 C  C     . LYS A 1 137 ? 0.617  -0.217  1.745   1.00 0.00 ? 136 LYS A C     1 
ATOM   1061 O  O     . LYS A 1 137 ? 0.434  -0.175  2.972   1.00 0.00 ? 136 LYS A O     1 
ATOM   1062 C  CB    . LYS A 1 137 ? 1.921  1.164   0.079   1.00 0.00 ? 136 LYS A CB    1 
ATOM   1063 C  CG    . LYS A 1 137 ? 1.718  2.083   -1.129  1.00 0.00 ? 136 LYS A CG    1 
ATOM   1064 C  CD    . LYS A 1 137 ? 0.354  2.786   -1.105  1.00 0.00 ? 136 LYS A CD    1 
ATOM   1065 C  CE    . LYS A 1 137 ? 0.057  3.582   -2.378  1.00 0.00 ? 136 LYS A CE    1 
ATOM   1066 N  NZ    . LYS A 1 137 ? -1.167 4.389   -2.278  1.00 0.00 ? 136 LYS A NZ    1 
ATOM   1067 N  N     . VAL A 1 138 ? 0.799  -1.321  1.048   1.00 0.00 ? 137 VAL A N     1 
ATOM   1068 C  CA    . VAL A 1 138 ? 0.656  -2.640  1.659   1.00 0.00 ? 137 VAL A CA    1 
ATOM   1069 C  C     . VAL A 1 138 ? 1.520  -3.707  0.972   1.00 0.00 ? 137 VAL A C     1 
ATOM   1070 O  O     . VAL A 1 138 ? 1.762  -3.648  -0.242  1.00 0.00 ? 137 VAL A O     1 
ATOM   1071 C  CB    . VAL A 1 138 ? -0.809 -3.052  1.525   1.00 0.00 ? 137 VAL A CB    1 
ATOM   1072 C  CG1   . VAL A 1 138 ? -1.137 -4.353  2.261   1.00 0.00 ? 137 VAL A CG1   1 
ATOM   1073 C  CG2   . VAL A 1 138 ? -1.776 -2.005  2.082   1.00 0.00 ? 137 VAL A CG2   1 
ATOM   1074 N  N     . LYS A 1 139 ? 1.944  -4.649  1.806   1.00 0.00 ? 138 LYS A N     1 
ATOM   1075 C  CA    . LYS A 1 139 ? 2.744  -5.813  1.391   1.00 0.00 ? 138 LYS A CA    1 
ATOM   1076 C  C     . LYS A 1 139 ? 1.986  -6.565  0.293   1.00 0.00 ? 138 LYS A C     1 
ATOM   1077 O  O     . LYS A 1 139 ? 1.513  -5.963  -0.683  1.00 0.00 ? 138 LYS A O     1 
ATOM   1078 C  CB    . LYS A 1 139 ? 2.946  -6.745  2.597   1.00 0.00 ? 138 LYS A CB    1 
ATOM   1079 C  CG    . LYS A 1 139 ? 4.271  -7.519  2.587   1.00 0.00 ? 138 LYS A CG    1 
ATOM   1080 C  CD    . LYS A 1 139 ? 4.435  -8.416  3.823   1.00 0.00 ? 138 LYS A CD    1 
ATOM   1081 C  CE    . LYS A 1 139 ? 5.670  -9.319  3.761   1.00 0.00 ? 138 LYS A CE    1 
ATOM   1082 N  NZ    . LYS A 1 139 ? 5.721  -10.297 4.858   1.00 0.00 ? 138 LYS A NZ    1 
ATOM   1083 N  N     . ALA A 1 140 ? 1.888  -7.868  0.490   1.00 0.00 ? 139 ALA A N     1 
ATOM   1084 C  CA    . ALA A 1 140 ? 1.196  -8.763  -0.450  1.00 0.00 ? 139 ALA A CA    1 
ATOM   1085 C  C     . ALA A 1 140 ? 1.625  -8.430  -1.880  1.00 0.00 ? 139 ALA A C     1 
ATOM   1086 O  O     . ALA A 1 140 ? 2.355  -7.457  -2.117  1.00 0.00 ? 139 ALA A O     1 
ATOM   1087 C  CB    . ALA A 1 140 ? -0.318 -8.581  -0.327  1.00 0.00 ? 139 ALA A CB    1 
ATOM   1088 N  N     . SER A 1 141 ? 1.159  -9.250  -2.797  1.00 0.00 ? 140 SER A N     1 
ATOM   1089 C  CA    . SER A 1 141 ? 1.451  -9.088  -4.227  1.00 0.00 ? 140 SER A CA    1 
ATOM   1090 C  C     . SER A 1 141 ? 1.959  -10.402 -4.799  1.00 0.00 ? 140 SER A C     1 
ATOM   1091 O  O     . SER A 1 141 ? 2.822  -11.065 -4.206  1.00 0.00 ? 140 SER A O     1 
ATOM   1092 C  CB    . SER A 1 141 ? 2.494  -7.991  -4.434  1.00 0.00 ? 140 SER A CB    1 
ATOM   1093 O  OG    . SER A 1 141 ? 2.042  -7.071  -5.416  1.00 0.00 ? 140 SER A OG    1 
ATOM   1094 N  N     . LYS A 1 142 ? 1.407  -10.733 -5.949  1.00 0.00 ? 141 LYS A N     1 
ATOM   1095 C  CA    . LYS A 1 142 ? 1.714  -11.999 -6.623  1.00 0.00 ? 141 LYS A CA    1 
ATOM   1096 C  C     . LYS A 1 142 ? 2.265  -11.782 -8.042  1.00 0.00 ? 141 LYS A C     1 
ATOM   1097 O  O     . LYS A 1 142 ? 3.423  -11.378 -8.222  1.00 0.00 ? 141 LYS A O     1 
ATOM   1098 C  CB    . LYS A 1 142 ? 0.439  -12.845 -6.706  1.00 0.00 ? 141 LYS A CB    1 
ATOM   1099 C  CG    . LYS A 1 142 ? -0.580 -12.491 -5.615  1.00 0.00 ? 141 LYS A CG    1 
ATOM   1100 C  CD    . LYS A 1 142 ? -1.724 -13.504 -5.506  1.00 0.00 ? 141 LYS A CD    1 
ATOM   1101 C  CE    . LYS A 1 142 ? -2.441 -13.453 -4.153  1.00 0.00 ? 141 LYS A CE    1 
ATOM   1102 N  NZ    . LYS A 1 142 ? -3.864 -13.812 -4.243  1.00 0.00 ? 141 LYS A NZ    1 
ATOM   1103 N  N     . GLU A 1 143 ? 1.384  -12.062 -8.979  1.00 0.00 ? 142 GLU A N     1 
ATOM   1104 C  CA    . GLU A 1 143 ? 1.642  -12.030 -10.429 1.00 0.00 ? 142 GLU A CA    1 
ATOM   1105 C  C     . GLU A 1 143 ? 2.207  -10.686 -10.890 1.00 0.00 ? 142 GLU A C     1 
ATOM   1106 O  O     . GLU A 1 143 ? 3.119  -10.630 -11.728 1.00 0.00 ? 142 GLU A O     1 
ATOM   1107 C  CB    . GLU A 1 143 ? 0.353  -12.295 -11.199 1.00 0.00 ? 142 GLU A CB    1 
ATOM   1108 C  CG    . GLU A 1 143 ? -0.602 -11.105 -11.175 1.00 0.00 ? 142 GLU A CG    1 
ATOM   1109 C  CD    . GLU A 1 143 ? -1.508 -11.045 -12.403 1.00 0.00 ? 142 GLU A CD    1 
ATOM   1110 O  OE1   . GLU A 1 143 ? -1.056 -10.572 -13.515 1.00 0.00 ? 142 GLU A OE1   1 
ATOM   1111 O  OE2   . GLU A 1 143 ? -2.724 -11.468 -12.329 1.00 0.00 ? 142 GLU A OE2   1 
ATOM   1112 N  N     . ASP A 1 144 ? 1.672  -9.610  -10.351 1.00 0.00 ? 143 ASP A N     1 
ATOM   1113 C  CA    . ASP A 1 144 ? 2.100  -8.275  -10.775 1.00 0.00 ? 143 ASP A CA    1 
ATOM   1114 C  C     . ASP A 1 144 ? 3.628  -8.289  -10.759 1.00 0.00 ? 143 ASP A C     1 
ATOM   1115 O  O     . ASP A 1 144 ? 4.280  -7.815  -11.701 1.00 0.00 ? 143 ASP A O     1 
ATOM   1116 C  CB    . ASP A 1 144 ? 1.541  -7.235  -9.796  1.00 0.00 ? 143 ASP A CB    1 
ATOM   1117 C  CG    . ASP A 1 144 ? 0.683  -7.858  -8.686  1.00 0.00 ? 143 ASP A CG    1 
ATOM   1118 O  OD1   . ASP A 1 144 ? -0.138 -7.124  -8.016  1.00 0.00 ? 143 ASP A OD1   1 
ATOM   1119 O  OD2   . ASP A 1 144 ? 0.783  -9.117  -8.423  1.00 0.00 ? 143 ASP A OD2   1 
ATOM   1120 N  N     . VAL A 1 145 ? 4.125  -8.839  -9.671  1.00 0.00 ? 144 VAL A N     1 
ATOM   1121 C  CA    . VAL A 1 145 ? 5.551  -9.127  -9.484  1.00 0.00 ? 144 VAL A CA    1 
ATOM   1122 C  C     . VAL A 1 145 ? 5.994  -10.071 -10.625 1.00 0.00 ? 144 VAL A C     1 
ATOM   1123 O  O     . VAL A 1 145 ? 7.096  -9.935  -11.176 1.00 0.00 ? 144 VAL A O     1 
ATOM   1124 C  CB    . VAL A 1 145 ? 5.798  -9.737  -8.103  1.00 0.00 ? 144 VAL A CB    1 
ATOM   1125 C  CG1   . VAL A 1 145 ? 4.521  -10.261 -7.443  1.00 0.00 ? 144 VAL A CG1   1 
ATOM   1126 C  CG2   . VAL A 1 145 ? 6.765  -10.923 -8.135  1.00 0.00 ? 144 VAL A CG2   1 
ATOM   1127 N  N     . GLN A 1 146 ? 5.101  -11.009 -10.936 1.00 0.00 ? 145 GLN A N     1 
ATOM   1128 C  CA    . GLN A 1 146 ? 5.326  -12.039 -11.973 1.00 0.00 ? 145 GLN A CA    1 
ATOM   1129 C  C     . GLN A 1 146 ? 5.763  -11.365 -13.289 1.00 0.00 ? 145 GLN A C     1 
ATOM   1130 O  O     . GLN A 1 146 ? 6.741  -11.784 -13.926 1.00 0.00 ? 145 GLN A O     1 
ATOM   1131 C  CB    . GLN A 1 146 ? 4.012  -12.802 -12.210 1.00 0.00 ? 145 GLN A CB    1 
ATOM   1132 C  CG    . GLN A 1 146 ? 4.139  -13.941 -13.226 1.00 0.00 ? 145 GLN A CG    1 
ATOM   1133 C  CD    . GLN A 1 146 ? 4.244  -13.452 -14.672 1.00 0.00 ? 145 GLN A CD    1 
ATOM   1134 O  OE1   . GLN A 1 146 ? 3.800  -12.347 -14.983 1.00 0.00 ? 145 GLN A OE1   1 
ATOM   1135 N  NE2   . GLN A 1 146 ? 4.811  -14.216 -15.587 1.00 0.00 ? 145 GLN A NE2   1 
ATOM   1136 N  N     . LYS A 1 147 ? 5.022  -10.334 -13.655 1.00 0.00 ? 146 LYS A N     1 
ATOM   1137 C  CA    . LYS A 1 147 ? 5.302  -9.508  -14.851 1.00 0.00 ? 146 LYS A CA    1 
ATOM   1138 C  C     . LYS A 1 147 ? 6.687  -8.832  -14.762 1.00 0.00 ? 146 LYS A C     1 
ATOM   1139 O  O     . LYS A 1 147 ? 7.479  -8.871  -15.715 1.00 0.00 ? 146 LYS A O     1 
ATOM   1140 C  CB    . LYS A 1 147 ? 4.244  -8.416  -14.984 1.00 0.00 ? 146 LYS A CB    1 
ATOM   1141 C  CG    . LYS A 1 147 ? 2.929  -8.777  -14.293 1.00 0.00 ? 146 LYS A CG    1 
ATOM   1142 C  CD    . LYS A 1 147 ? 1.704  -8.200  -15.005 1.00 0.00 ? 146 LYS A CD    1 
ATOM   1143 C  CE    . LYS A 1 147 ? 0.437  -9.025  -14.779 1.00 0.00 ? 146 LYS A CE    1 
ATOM   1144 N  NZ    . LYS A 1 147 ? -0.795 -8.270  -15.046 1.00 0.00 ? 146 LYS A NZ    1 
ATOM   1145 N  N     . PHE A 1 148 ? 6.928  -8.229  -13.603 1.00 0.00 ? 147 PHE A N     1 
ATOM   1146 C  CA    . PHE A 1 148 ? 8.173  -7.489  -13.316 1.00 0.00 ? 147 PHE A CA    1 
ATOM   1147 C  C     . PHE A 1 148 ? 9.374  -8.408  -13.533 1.00 0.00 ? 147 PHE A C     1 
ATOM   1148 O  O     . PHE A 1 148 ? 10.357 -8.031  -14.189 1.00 0.00 ? 147 PHE A O     1 
ATOM   1149 C  CB    . PHE A 1 148 ? 8.138  -6.978  -11.865 1.00 0.00 ? 147 PHE A CB    1 
ATOM   1150 C  CG    . PHE A 1 148 ? 9.523  -6.747  -11.247 1.00 0.00 ? 147 PHE A CG    1 
ATOM   1151 C  CD1   . PHE A 1 148 ? 10.329 -5.690  -11.695 1.00 0.00 ? 147 PHE A CD1   1 
ATOM   1152 C  CD2   . PHE A 1 148 ? 9.981  -7.589  -10.226 1.00 0.00 ? 147 PHE A CD2   1 
ATOM   1153 C  CE1   . PHE A 1 148 ? 11.591 -5.480  -11.124 1.00 0.00 ? 147 PHE A CE1   1 
ATOM   1154 C  CE2   . PHE A 1 148 ? 11.243 -7.377  -9.655  1.00 0.00 ? 147 PHE A CE2   1 
ATOM   1155 C  CZ    . PHE A 1 148 ? 12.048 -6.324  -10.104 1.00 0.00 ? 147 PHE A CZ    1 
ATOM   1156 N  N     . ARG A 1 149 ? 9.256  -9.594  -12.971 1.00 0.00 ? 148 ARG A N     1 
ATOM   1157 C  CA    . ARG A 1 149 ? 10.286 -10.633 -13.092 1.00 0.00 ? 148 ARG A CA    1 
ATOM   1158 C  C     . ARG A 1 149 ? 10.524 -10.982 -14.568 1.00 0.00 ? 148 ARG A C     1 
ATOM   1159 O  O     . ARG A 1 149 ? 11.671 -11.033 -15.036 1.00 0.00 ? 148 ARG A O     1 
ATOM   1160 C  CB    . ARG A 1 149 ? 9.841  -11.894 -12.353 1.00 0.00 ? 148 ARG A CB    1 
ATOM   1161 C  CG    . ARG A 1 149 ? 9.159  -11.591 -11.018 1.00 0.00 ? 148 ARG A CG    1 
ATOM   1162 C  CD    . ARG A 1 149 ? 9.739  -12.398 -9.855  1.00 0.00 ? 148 ARG A CD    1 
ATOM   1163 N  NE    . ARG A 1 149 ? 8.991  -13.634 -9.588  1.00 0.00 ? 148 ARG A NE    1 
ATOM   1164 C  CZ    . ARG A 1 149 ? 8.710  -14.088 -8.359  1.00 0.00 ? 148 ARG A CZ    1 
ATOM   1165 N  NH1   . ARG A 1 149 ? 9.108  -13.418 -7.269  1.00 0.00 ? 148 ARG A NH1   1 
ATOM   1166 N  NH2   . ARG A 1 149 ? 8.027  -15.215 -8.115  1.00 0.00 ? 148 ARG A NH2   1 
ATOM   1167 N  N     . HIS A 1 150 ? 9.419  -11.215 -15.265 1.00 0.00 ? 149 HIS A N     1 
ATOM   1168 C  CA    . HIS A 1 150 ? 9.434  -11.568 -16.698 1.00 0.00 ? 149 HIS A CA    1 
ATOM   1169 C  C     . HIS A 1 150 ? 10.139 -10.468 -17.472 1.00 0.00 ? 149 HIS A C     1 
ATOM   1170 O  O     . HIS A 1 150 ? 11.023 -10.735 -18.299 1.00 0.00 ? 149 HIS A O     1 
ATOM   1171 C  CB    . HIS A 1 150 ? 7.991  -11.699 -17.215 1.00 0.00 ? 149 HIS A CB    1 
ATOM   1172 C  CG    . HIS A 1 150 ? 7.886  -12.112 -18.693 1.00 0.00 ? 149 HIS A CG    1 
ATOM   1173 N  ND1   . HIS A 1 150 ? 8.383  -11.317 -19.725 1.00 0.00 ? 149 HIS A ND1   1 
ATOM   1174 C  CD2   . HIS A 1 150 ? 7.349  -13.210 -19.291 1.00 0.00 ? 149 HIS A CD2   1 
ATOM   1175 C  CE1   . HIS A 1 150 ? 8.143  -11.930 -20.872 1.00 0.00 ? 149 HIS A CE1   1 
ATOM   1176 N  NE2   . HIS A 1 150 ? 7.527  -13.059 -20.631 1.00 0.00 ? 149 HIS A NE2   1 
ATOM   1177 N  N     . GLU A 1 151 ? 9.704  -9.276  -17.155 1.00 0.00 ? 150 GLU A N     1 
ATOM   1178 C  CA    . GLU A 1 151 ? 10.216 -8.050  -17.753 1.00 0.00 ? 150 GLU A CA    1 
ATOM   1179 C  C     . GLU A 1 151 ? 11.731 -7.927  -17.520 1.00 0.00 ? 150 GLU A C     1 
ATOM   1180 O  O     . GLU A 1 151 ? 12.498 -7.632  -18.448 1.00 0.00 ? 150 GLU A O     1 
ATOM   1181 C  CB    . GLU A 1 151 ? 9.496  -6.847  -17.133 1.00 0.00 ? 150 GLU A CB    1 
ATOM   1182 C  CG    . GLU A 1 151 ? 8.087  -7.192  -16.632 1.00 0.00 ? 150 GLU A CG    1 
ATOM   1183 C  CD    . GLU A 1 151 ? 7.271  -5.965  -16.213 1.00 0.00 ? 150 GLU A CD    1 
ATOM   1184 O  OE1   . GLU A 1 151 ? 7.870  -4.915  -15.765 1.00 0.00 ? 150 GLU A OE1   1 
ATOM   1185 O  OE2   . GLU A 1 151 ? 5.984  -5.983  -16.309 1.00 0.00 ? 150 GLU A OE2   1 
ATOM   1186 N  N     . LEU A 1 152 ? 12.131 -8.158  -16.278 1.00 0.00 ? 151 LEU A N     1 
ATOM   1187 C  CA    . LEU A 1 152 ? 13.542 -8.011  -15.833 1.00 0.00 ? 151 LEU A CA    1 
ATOM   1188 C  C     . LEU A 1 152 ? 14.537 -8.914  -16.591 1.00 0.00 ? 151 LEU A C     1 
ATOM   1189 O  O     . LEU A 1 152 ? 15.544 -8.438  -17.137 1.00 0.00 ? 151 LEU A O     1 
ATOM   1190 C  CB    . LEU A 1 152 ? 13.647 -8.388  -14.359 1.00 0.00 ? 151 LEU A CB    1 
ATOM   1191 C  CG    . LEU A 1 152 ? 15.040 -8.152  -13.785 1.00 0.00 ? 151 LEU A CG    1 
ATOM   1192 C  CD1   . LEU A 1 152 ? 16.159 -8.547  -14.751 1.00 0.00 ? 151 LEU A CD1   1 
ATOM   1193 C  CD2   . LEU A 1 152 ? 15.297 -6.687  -13.428 1.00 0.00 ? 151 LEU A CD2   1 
ATOM   1194 N  N     . SER A 1 153 ? 14.222 -10.199 -16.602 1.00 0.00 ? 152 SER A N     1 
ATOM   1195 C  CA    . SER A 1 153 ? 15.032 -11.226 -17.292 1.00 0.00 ? 152 SER A CA    1 
ATOM   1196 C  C     . SER A 1 153 ? 15.115 -10.827 -18.744 1.00 0.00 ? 152 SER A C     1 
ATOM   1197 O  O     . SER A 1 153 ? 16.176 -10.937 -19.376 1.00 0.00 ? 152 SER A O     1 
ATOM   1198 C  CB    . SER A 1 153 ? 14.379 -12.603 -17.166 1.00 0.00 ? 152 SER A CB    1 
ATOM   1199 O  OG    . SER A 1 153 ? 13.248 -12.530 -16.312 1.00 0.00 ? 152 SER A OG    1 
ATOM   1200 N  N     . SER A 1 154 ? 13.936 -10.415 -19.137 1.00 0.00 ? 153 SER A N     1 
ATOM   1201 C  CA    . SER A 1 154 ? 13.594 -9.912  -20.463 1.00 0.00 ? 153 SER A CA    1 
ATOM   1202 C  C     . SER A 1 154 ? 14.812 -9.821  -21.394 1.00 0.00 ? 153 SER A C     1 
ATOM   1203 O  O     . SER A 1 154 ? 14.789 -10.323 -22.526 1.00 0.00 ? 153 SER A O     1 
ATOM   1204 C  CB    . SER A 1 154 ? 12.962 -8.525  -20.330 1.00 0.00 ? 153 SER A CB    1 
ATOM   1205 O  OG    . SER A 1 154 ? 13.237 -7.752  -21.488 1.00 0.00 ? 153 SER A OG    1 
ATOM   1206 N  N     . LEU A 1 155 ? 15.885 -9.192  -20.945 1.00 0.00 ? 154 LEU A N     1 
ATOM   1207 C  CA    . LEU A 1 155 ? 17.080 -9.031  -21.806 1.00 0.00 ? 154 LEU A CA    1 
ATOM   1208 C  C     . LEU A 1 155 ? 18.355 -9.593  -21.150 1.00 0.00 ? 154 LEU A C     1 
ATOM   1209 O  O     . LEU A 1 155 ? 19.237 -8.837  -20.715 1.00 0.00 ? 154 LEU A O     1 
ATOM   1210 C  CB    . LEU A 1 155 ? 17.321 -7.551  -22.114 1.00 0.00 ? 154 LEU A CB    1 
ATOM   1211 C  CG    . LEU A 1 155 ? 17.728 -6.739  -20.883 1.00 0.00 ? 154 LEU A CG    1 
ATOM   1212 C  CD1   . LEU A 1 155 ? 16.760 -6.906  -19.711 1.00 0.00 ? 154 LEU A CD1   1 
ATOM   1213 C  CD2   . LEU A 1 155 ? 19.106 -7.124  -20.341 1.00 0.00 ? 154 LEU A CD2   1 
ATOM   1214 N  N     . ALA A 1 156 ? 18.438 -10.920 -21.094 1.00 0.00 ? 155 ALA A N     1 
ATOM   1215 C  CA    . ALA A 1 156 ? 19.597 -11.614 -20.485 1.00 0.00 ? 155 ALA A CA    1 
ATOM   1216 C  C     . ALA A 1 156 ? 19.810 -12.999 -21.104 1.00 0.00 ? 155 ALA A C     1 
ATOM   1217 O  O     . ALA A 1 156 ? 19.075 -13.413 -22.012 1.00 0.00 ? 155 ALA A O     1 
ATOM   1218 C  CB    . ALA A 1 156 ? 19.367 -11.800 -18.984 1.00 0.00 ? 155 ALA A CB    1 
ATOM   1219 N  N     . ASP A 1 157 ? 20.824 -13.668 -20.576 1.00 0.00 ? 156 ASP A N     1 
ATOM   1220 C  CA    . ASP A 1 157 ? 21.204 -15.030 -20.996 1.00 0.00 ? 156 ASP A CA    1 
ATOM   1221 C  C     . ASP A 1 157 ? 21.599 -15.859 -19.747 1.00 0.00 ? 156 ASP A C     1 
ATOM   1222 O  O     . ASP A 1 157 ? 21.022 -16.923 -19.478 1.00 0.00 ? 156 ASP A O     1 
ATOM   1223 C  CB    . ASP A 1 157 ? 22.371 -14.959 -21.994 1.00 0.00 ? 156 ASP A CB    1 
ATOM   1224 C  CG    . ASP A 1 157 ? 21.911 -14.866 -23.456 1.00 0.00 ? 156 ASP A CG    1 
ATOM   1225 O  OD1   . ASP A 1 157 ? 22.656 -15.335 -24.399 1.00 0.00 ? 156 ASP A OD1   1 
ATOM   1226 O  OD2   . ASP A 1 157 ? 20.778 -14.320 -23.742 1.00 0.00 ? 156 ASP A OD2   1 
ATOM   1227 N  N     . VAL A 1 158 ? 22.592 -15.304 -19.063 1.00 0.00 ? 157 VAL A N     1 
ATOM   1228 C  CA    . VAL A 1 158 ? 23.216 -15.818 -17.805 1.00 0.00 ? 157 VAL A CA    1 
ATOM   1229 C  C     . VAL A 1 158 ? 23.225 -14.746 -16.671 1.00 0.00 ? 157 VAL A C     1 
ATOM   1230 O  O     . VAL A 1 158 ? 23.663 -13.604 -16.873 1.00 0.00 ? 157 VAL A O     1 
ATOM   1231 C  CB    . VAL A 1 158 ? 24.612 -16.340 -18.077 1.00 0.00 ? 157 VAL A CB    1 
ATOM   1232 C  CG1   . VAL A 1 158 ? 24.741 -17.004 -19.449 1.00 0.00 ? 157 VAL A CG1   1 
ATOM   1233 C  CG2   . VAL A 1 158 ? 25.678 -15.245 -18.039 1.00 0.00 ? 157 VAL A CG2   1 
ATOM   1234 N  N     . TYR A 1 159 ? 22.737 -15.129 -15.498 1.00 0.00 ? 158 TYR A N     1 
ATOM   1235 C  CA    . TYR A 1 159 ? 22.601 -14.231 -14.311 1.00 0.00 ? 158 TYR A CA    1 
ATOM   1236 C  C     . TYR A 1 159 ? 23.600 -14.604 -13.186 1.00 0.00 ? 158 TYR A C     1 
ATOM   1237 O  O     . TYR A 1 159 ? 23.603 -15.738 -12.683 1.00 0.00 ? 158 TYR A O     1 
ATOM   1238 C  CB    . TYR A 1 159 ? 21.174 -14.329 -13.753 1.00 0.00 ? 158 TYR A CB    1 
ATOM   1239 C  CG    . TYR A 1 159 ? 21.087 -14.473 -12.225 1.00 0.00 ? 158 TYR A CG    1 
ATOM   1240 C  CD1   . TYR A 1 159 ? 21.473 -13.414 -11.388 1.00 0.00 ? 158 TYR A CD1   1 
ATOM   1241 C  CD2   . TYR A 1 159 ? 20.606 -15.663 -11.661 1.00 0.00 ? 158 TYR A CD2   1 
ATOM   1242 C  CE1   . TYR A 1 159 ? 21.366 -13.544 -9.995  1.00 0.00 ? 158 TYR A CE1   1 
ATOM   1243 C  CE2   . TYR A 1 159 ? 20.499 -15.791 -10.269 1.00 0.00 ? 158 TYR A CE2   1 
ATOM   1244 C  CZ    . TYR A 1 159 ? 20.875 -14.731 -9.437  1.00 0.00 ? 158 TYR A CZ    1 
ATOM   1245 O  OH    . TYR A 1 159 ? 20.764 -14.852 -8.087  1.00 0.00 ? 158 TYR A OH    1 
ATOM   1246 N  N     . ILE A 1 160 ? 24.427 -13.605 -12.841 1.00 0.00 ? 159 ILE A N     1 
ATOM   1247 C  CA    . ILE A 1 160 ? 25.509 -13.744 -11.833 1.00 0.00 ? 159 ILE A CA    1 
ATOM   1248 C  C     . ILE A 1 160 ? 25.292 -12.869 -10.581 1.00 0.00 ? 159 ILE A C     1 
ATOM   1249 O  O     . ILE A 1 160 ? 25.337 -11.632 -10.648 1.00 0.00 ? 159 ILE A O     1 
ATOM   1250 C  CB    . ILE A 1 160 ? 26.830 -13.271 -12.438 1.00 0.00 ? 159 ILE A CB    1 
ATOM   1251 C  CG1   . ILE A 1 160 ? 26.665 -12.728 -13.859 1.00 0.00 ? 159 ILE A CG1   1 
ATOM   1252 C  CG2   . ILE A 1 160 ? 27.878 -14.382 -12.530 1.00 0.00 ? 159 ILE A CG2   1 
ATOM   1253 C  CD1   . ILE A 1 160 ? 27.986 -12.278 -14.486 1.00 0.00 ? 159 ILE A CD1   1 
ATOM   1254 N  N     . ASN A 1 161 ? 25.060 -13.578 -9.481  1.00 0.00 ? 160 ASN A N     1 
ATOM   1255 C  CA    . ASN A 1 161 ? 24.909 -12.986 -8.142  1.00 0.00 ? 160 ASN A CA    1 
ATOM   1256 C  C     . ASN A 1 161 ? 26.312 -12.822 -7.553  1.00 0.00 ? 160 ASN A C     1 
ATOM   1257 O  O     . ASN A 1 161 ? 27.117 -13.765 -7.549  1.00 0.00 ? 160 ASN A O     1 
ATOM   1258 C  CB    . ASN A 1 161 ? 24.104 -13.932 -7.232  1.00 0.00 ? 160 ASN A CB    1 
ATOM   1259 C  CG    . ASN A 1 161 ? 22.589 -13.708 -7.285  1.00 0.00 ? 160 ASN A CG    1 
ATOM   1260 O  OD1   . ASN A 1 161 ? 22.127 -12.771 -7.934  1.00 0.00 ? 160 ASN A OD1   1 
ATOM   1261 N  ND2   . ASN A 1 161 ? 21.778 -14.522 -6.633  1.00 0.00 ? 160 ASN A ND2   1 
ATOM   1262 N  N     . ASP A 1 162 ? 26.602 -11.635 -7.062  1.00 0.00 ? 161 ASP A N     1 
ATOM   1263 C  CA    . ASP A 1 162 ? 27.926 -11.347 -6.488  1.00 0.00 ? 161 ASP A CA    1 
ATOM   1264 C  C     . ASP A 1 162 ? 27.828 -10.288 -5.392  1.00 0.00 ? 161 ASP A C     1 
ATOM   1265 O  O     . ASP A 1 162 ? 28.529 -9.266  -5.428  1.00 0.00 ? 161 ASP A O     1 
ATOM   1266 C  CB    . ASP A 1 162 ? 28.866 -10.837 -7.579  1.00 0.00 ? 161 ASP A CB    1 
ATOM   1267 C  CG    . ASP A 1 162 ? 29.211 -9.357  -7.423  1.00 0.00 ? 161 ASP A CG    1 
ATOM   1268 O  OD1   . ASP A 1 162 ? 28.410 -8.456  -7.882  1.00 0.00 ? 161 ASP A OD1   1 
ATOM   1269 O  OD2   . ASP A 1 162 ? 30.303 -9.008  -6.831  1.00 0.00 ? 161 ASP A OD2   1 
ATOM   1270 N  N     . ALA A 1 163 ? 26.949 -10.614 -4.483  1.00 0.00 ? 162 ALA A N     1 
ATOM   1271 C  CA    . ALA A 1 163 ? 26.641 -9.840  -3.283  1.00 0.00 ? 162 ALA A CA    1 
ATOM   1272 C  C     . ALA A 1 163 ? 25.967 -10.807 -2.319  1.00 0.00 ? 162 ALA A C     1 
ATOM   1273 O  O     . ALA A 1 163 ? 25.385 -11.820 -2.734  1.00 0.00 ? 162 ALA A O     1 
ATOM   1274 C  CB    . ALA A 1 163 ? 25.704 -8.682  -3.634  1.00 0.00 ? 162 ALA A CB    1 
ATOM   1275 N  N     . PHE A 1 164 ? 26.036 -10.512 -1.049  1.00 0.00 ? 163 PHE A N     1 
ATOM   1276 C  CA    . PHE A 1 164 ? 25.438 -11.392 -0.038  1.00 0.00 ? 163 PHE A CA    1 
ATOM   1277 C  C     . PHE A 1 164 ? 23.989 -10.996 0.247   1.00 0.00 ? 163 PHE A C     1 
ATOM   1278 O  O     . PHE A 1 164 ? 23.600 -10.787 1.405   1.00 0.00 ? 163 PHE A O     1 
ATOM   1279 C  CB    . PHE A 1 164 ? 26.221 -11.301 1.273   1.00 0.00 ? 163 PHE A CB    1 
ATOM   1280 C  CG    . PHE A 1 164 ? 26.830 -12.700 1.510   1.00 0.00 ? 163 PHE A CG    1 
ATOM   1281 C  CD1   . PHE A 1 164 ? 26.910 -13.270 2.790   1.00 0.00 ? 163 PHE A CD1   1 
ATOM   1282 C  CD2   . PHE A 1 164 ? 27.280 -13.440 0.400   1.00 0.00 ? 163 PHE A CD2   1 
ATOM   1283 C  CE1   . PHE A 1 164 ? 27.450 -14.560 2.960   1.00 0.00 ? 163 PHE A CE1   1 
ATOM   1284 C  CE2   . PHE A 1 164 ? 27.810 -14.730 0.570   1.00 0.00 ? 163 PHE A CE2   1 
ATOM   1285 C  CZ    . PHE A 1 164 ? 27.890 -15.290 1.850   1.00 0.00 ? 163 PHE A CZ    1 
ATOM   1286 N  N     . GLY A 1 165 ? 23.204 -10.904 -0.814  1.00 0.00 ? 164 GLY A N     1 
ATOM   1287 C  CA    . GLY A 1 165 ? 21.780 -10.541 -0.692  1.00 0.00 ? 164 GLY A CA    1 
ATOM   1288 C  C     . GLY A 1 165 ? 20.878 -11.793 -0.796  1.00 0.00 ? 164 GLY A C     1 
ATOM   1289 O  O     . GLY A 1 165 ? 20.253 -12.213 0.188   1.00 0.00 ? 164 GLY A O     1 
ATOM   1290 N  N     . THR A 1 166 ? 20.817 -12.393 -1.984  1.00 0.00 ? 165 THR A N     1 
ATOM   1291 C  CA    . THR A 1 166 ? 19.942 -13.577 -2.234  1.00 0.00 ? 165 THR A CA    1 
ATOM   1292 C  C     . THR A 1 166 ? 20.474 -14.852 -1.563  1.00 0.00 ? 165 THR A C     1 
ATOM   1293 O  O     . THR A 1 166 ? 20.840 -15.825 -2.238  1.00 0.00 ? 165 THR A O     1 
ATOM   1294 C  CB    . THR A 1 166 ? 19.835 -13.883 -3.730  1.00 0.00 ? 165 THR A CB    1 
ATOM   1295 O  OG1   . THR A 1 166 ? 18.673 -14.659 -3.983  1.00 0.00 ? 165 THR A OG1   1 
ATOM   1296 C  CG2   . THR A 1 166 ? 21.034 -14.666 -4.267  1.00 0.00 ? 165 THR A CG2   1 
ATOM   1297 N  N     . ALA A 1 167 ? 20.498 -14.807 -0.249  1.00 0.00 ? 166 ALA A N     1 
ATOM   1298 C  CA    . ALA A 1 167 ? 20.943 -15.928 0.595   1.00 0.00 ? 166 ALA A CA    1 
ATOM   1299 C  C     . ALA A 1 167 ? 20.263 -15.800 1.949   1.00 0.00 ? 166 ALA A C     1 
ATOM   1300 O  O     . ALA A 1 167 ? 20.761 -16.309 2.965   1.00 0.00 ? 166 ALA A O     1 
ATOM   1301 C  CB    . ALA A 1 167 ? 22.462 -15.885 0.768   1.00 0.00 ? 166 ALA A CB    1 
ATOM   1302 N  N     . HIS A 1 168 ? 19.149 -15.112 1.872   1.00 0.00 ? 167 HIS A N     1 
ATOM   1303 C  CA    . HIS A 1 168 ? 18.289 -14.810 3.010   1.00 0.00 ? 167 HIS A CA    1 
ATOM   1304 C  C     . HIS A 1 168 ? 17.252 -13.786 2.571   1.00 0.00 ? 167 HIS A C     1 
ATOM   1305 O  O     . HIS A 1 168 ? 17.476 -12.570 2.666   1.00 0.00 ? 167 HIS A O     1 
ATOM   1306 C  CB    . HIS A 1 168 ? 19.119 -14.231 4.151   1.00 0.00 ? 167 HIS A CB    1 
ATOM   1307 C  CG    . HIS A 1 168 ? 19.634 -12.825 3.849   1.00 0.00 ? 167 HIS A CG    1 
ATOM   1308 N  ND1   . HIS A 1 168 ? 19.000 -11.689 4.340   1.00 0.00 ? 167 HIS A ND1   1 
ATOM   1309 C  CD2   . HIS A 1 168 ? 20.695 -12.385 3.123   1.00 0.00 ? 167 HIS A CD2   1 
ATOM   1310 C  CE1   . HIS A 1 168 ? 19.667 -10.631 3.917   1.00 0.00 ? 167 HIS A CE1   1 
ATOM   1311 N  NE2   . HIS A 1 168 ? 20.681 -11.029 3.190   1.00 0.00 ? 167 HIS A NE2   1 
ATOM   1312 N  N     . ARG A 1 169 ? 16.154 -14.330 2.110   1.00 0.00 ? 168 ARG A N     1 
ATOM   1313 C  CA    . ARG A 1 169 ? 15.033 -13.551 1.590   1.00 0.00 ? 168 ARG A CA    1 
ATOM   1314 C  C     . ARG A 1 169 ? 14.729 -14.058 0.170   1.00 0.00 ? 168 ARG A C     1 
ATOM   1315 O  O     . ARG A 1 169 ? 14.383 -15.232 -0.029  1.00 0.00 ? 168 ARG A O     1 
ATOM   1316 C  CB    . ARG A 1 169 ? 15.403 -12.054 1.611   1.00 0.00 ? 168 ARG A CB    1 
ATOM   1317 C  CG    . ARG A 1 169 ? 14.920 -11.323 2.880   1.00 0.00 ? 168 ARG A CG    1 
ATOM   1318 C  CD    . ARG A 1 169 ? 16.061 -10.713 3.717   1.00 0.00 ? 168 ARG A CD    1 
ATOM   1319 N  NE    . ARG A 1 169 ? 16.163 -9.244  3.589   1.00 0.00 ? 168 ARG A NE    1 
ATOM   1320 C  CZ    . ARG A 1 169 ? 16.309 -8.394  4.622   1.00 0.00 ? 168 ARG A CZ    1 
ATOM   1321 N  NH1   . ARG A 1 169 ? 16.372 -8.844  5.883   1.00 0.00 ? 168 ARG A NH1   1 
ATOM   1322 N  NH2   . ARG A 1 169 ? 16.404 -7.064  4.492   1.00 0.00 ? 168 ARG A NH2   1 
ATOM   1323 N  N     . ALA A 1 170 ? 14.867 -13.164 -0.784  1.00 0.00 ? 169 ALA A N     1 
ATOM   1324 C  CA    . ALA A 1 170 ? 14.633 -13.460 -2.212  1.00 0.00 ? 169 ALA A CA    1 
ATOM   1325 C  C     . ALA A 1 170 ? 15.069 -12.253 -3.031  1.00 0.00 ? 169 ALA A C     1 
ATOM   1326 O  O     . ALA A 1 170 ? 16.100 -12.288 -3.720  1.00 0.00 ? 169 ALA A O     1 
ATOM   1327 C  CB    . ALA A 1 170 ? 13.147 -13.736 -2.453  1.00 0.00 ? 169 ALA A CB    1 
ATOM   1328 N  N     . HIS A 1 171 ? 14.232 -11.255 -2.904  1.00 0.00 ? 170 HIS A N     1 
ATOM   1329 C  CA    . HIS A 1 171 ? 14.412 -9.937  -3.505  1.00 0.00 ? 170 HIS A CA    1 
ATOM   1330 C  C     . HIS A 1 171 ? 14.935 -10.019 -4.929  1.00 0.00 ? 170 HIS A C     1 
ATOM   1331 O  O     . HIS A 1 171 ? 15.560 -11.014 -5.323  1.00 0.00 ? 170 HIS A O     1 
ATOM   1332 C  CB    . HIS A 1 171 ? 15.336 -9.136  -2.614  1.00 0.00 ? 170 HIS A CB    1 
ATOM   1333 C  CG    . HIS A 1 171 ? 14.604 -8.820  -1.329  1.00 0.00 ? 170 HIS A CG    1 
ATOM   1334 N  ND1   . HIS A 1 171 ? 15.251 -8.419  -0.170  1.00 0.00 ? 170 HIS A ND1   1 
ATOM   1335 C  CD2   . HIS A 1 171 ? 13.279 -8.863  -1.049  1.00 0.00 ? 170 HIS A CD2   1 
ATOM   1336 C  CE1   . HIS A 1 171 ? 14.328 -8.230  0.758   1.00 0.00 ? 170 HIS A CE1   1 
ATOM   1337 N  NE2   . HIS A 1 171 ? 13.148 -8.492  0.247   1.00 0.00 ? 170 HIS A NE2   1 
ATOM   1338 N  N     . SER A 1 172 ? 14.631 -8.936  -5.618  1.00 0.00 ? 171 SER A N     1 
ATOM   1339 C  CA    . SER A 1 172 ? 14.973 -8.732  -7.026  1.00 0.00 ? 171 SER A CA    1 
ATOM   1340 C  C     . SER A 1 172 ? 16.459 -8.963  -7.261  1.00 0.00 ? 171 SER A C     1 
ATOM   1341 O  O     . SER A 1 172 ? 17.291 -8.730  -6.371  1.00 0.00 ? 171 SER A O     1 
ATOM   1342 C  CB    . SER A 1 172 ? 14.631 -7.301  -7.445  1.00 0.00 ? 171 SER A CB    1 
ATOM   1343 O  OG    . SER A 1 172 ? 15.394 -6.933  -8.584  1.00 0.00 ? 171 SER A OG    1 
ATOM   1344 N  N     . SER A 1 173 ? 16.719 -9.419  -8.468  1.00 0.00 ? 172 SER A N     1 
ATOM   1345 C  CA    . SER A 1 173 ? 18.072 -9.701  -8.945  1.00 0.00 ? 172 SER A CA    1 
ATOM   1346 C  C     . SER A 1 173 ? 18.513 -11.112 -8.541  1.00 0.00 ? 172 SER A C     1 
ATOM   1347 O  O     . SER A 1 173 ? 19.519 -11.635 -9.043  1.00 0.00 ? 172 SER A O     1 
ATOM   1348 C  CB    . SER A 1 173 ? 19.057 -8.693  -8.346  1.00 0.00 ? 172 SER A CB    1 
ATOM   1349 O  OG    . SER A 1 173 ? 18.665 -7.370  -8.683  1.00 0.00 ? 172 SER A OG    1 
ATOM   1350 N  N     . MET A 1 174 ? 17.751 -11.721 -7.643  1.00 0.00 ? 173 MET A N     1 
ATOM   1351 C  CA    . MET A 1 174 ? 18.083 -13.065 -7.130  1.00 0.00 ? 173 MET A CA    1 
ATOM   1352 C  C     . MET A 1 174 ? 16.998 -14.108 -7.440  1.00 0.00 ? 173 MET A C     1 
ATOM   1353 O  O     . MET A 1 174 ? 17.216 -15.320 -7.295  1.00 0.00 ? 173 MET A O     1 
ATOM   1354 C  CB    . MET A 1 174 ? 18.260 -13.036 -5.609  1.00 0.00 ? 173 MET A CB    1 
ATOM   1355 C  CG    . MET A 1 174 ? 18.267 -11.618 -5.034  1.00 0.00 ? 173 MET A CG    1 
ATOM   1356 S  SD    . MET A 1 174 ? 19.888 -10.882 -5.021  1.00 0.00 ? 173 MET A SD    1 
ATOM   1357 C  CE    . MET A 1 174 ? 20.990 -11.815 -6.062  1.00 0.00 ? 173 MET A CE    1 
ATOM   1358 N  N     . VAL A 1 175 ? 15.837 -13.652 -7.870  1.00 0.00 ? 174 VAL A N     1 
ATOM   1359 C  CA    . VAL A 1 175 ? 14.716 -14.566 -8.182  1.00 0.00 ? 174 VAL A CA    1 
ATOM   1360 C  C     . VAL A 1 175 ? 14.305 -14.436 -9.674  1.00 0.00 ? 174 VAL A C     1 
ATOM   1361 O  O     . VAL A 1 175 ? 15.006 -14.923 -10.573 1.00 0.00 ? 174 VAL A O     1 
ATOM   1362 C  CB    . VAL A 1 175 ? 13.538 -14.263 -7.248  1.00 0.00 ? 174 VAL A CB    1 
ATOM   1363 C  CG1   . VAL A 1 175 ? 13.050 -15.495 -6.482  1.00 0.00 ? 174 VAL A CG1   1 
ATOM   1364 C  CG2   . VAL A 1 175 ? 13.874 -13.219 -6.180  1.00 0.00 ? 174 VAL A CG2   1 
ATOM   1365 N  N     . GLY A 1 176 ? 13.175 -13.781 -9.889  1.00 0.00 ? 175 GLY A N     1 
ATOM   1366 C  CA    . GLY A 1 176 ? 12.573 -13.539 -11.233 1.00 0.00 ? 175 GLY A CA    1 
ATOM   1367 C  C     . GLY A 1 176 ? 13.484 -13.993 -12.398 1.00 0.00 ? 175 GLY A C     1 
ATOM   1368 O  O     . GLY A 1 176 ? 13.114 -14.871 -13.193 1.00 0.00 ? 175 GLY A O     1 
ATOM   1369 N  N     . PHE A 1 177 ? 14.650 -13.377 -12.462 1.00 0.00 ? 176 PHE A N     1 
ATOM   1370 C  CA    . PHE A 1 177 ? 15.651 -13.625 -13.524 1.00 0.00 ? 176 PHE A CA    1 
ATOM   1371 C  C     . PHE A 1 177 ? 15.564 -15.063 -14.070 1.00 0.00 ? 176 PHE A C     1 
ATOM   1372 O  O     . PHE A 1 177 ? 16.567 -15.791 -14.112 1.00 0.00 ? 176 PHE A O     1 
ATOM   1373 C  CB    . PHE A 1 177 ? 17.067 -13.392 -12.984 1.00 0.00 ? 176 PHE A CB    1 
ATOM   1374 C  CG    . PHE A 1 177 ? 17.643 -12.027 -13.383 1.00 0.00 ? 176 PHE A CG    1 
ATOM   1375 C  CD1   . PHE A 1 177 ? 17.286 -10.878 -12.664 1.00 0.00 ? 176 PHE A CD1   1 
ATOM   1376 C  CD2   . PHE A 1 177 ? 18.526 -11.923 -14.466 1.00 0.00 ? 176 PHE A CD2   1 
ATOM   1377 C  CE1   . PHE A 1 177 ? 17.810 -9.631  -13.027 1.00 0.00 ? 176 PHE A CE1   1 
ATOM   1378 C  CE2   . PHE A 1 177 ? 19.050 -10.675 -14.829 1.00 0.00 ? 176 PHE A CE2   1 
ATOM   1379 C  CZ    . PHE A 1 177 ? 18.691 -9.529  -14.109 1.00 0.00 ? 176 PHE A CZ    1 
ATOM   1380 N  N     . ASP A 1 178 ? 14.353 -15.444 -14.478 1.00 0.00 ? 177 ASP A N     1 
ATOM   1381 C  CA    . ASP A 1 178 ? 14.125 -16.768 -15.079 1.00 0.00 ? 177 ASP A CA    1 
ATOM   1382 C  C     . ASP A 1 178 ? 15.086 -16.897 -16.244 1.00 0.00 ? 177 ASP A C     1 
ATOM   1383 O  O     . ASP A 1 178 ? 15.733 -15.921 -16.651 1.00 0.00 ? 177 ASP A O     1 
ATOM   1384 C  CB    . ASP A 1 178 ? 12.680 -16.925 -15.555 1.00 0.00 ? 177 ASP A CB    1 
ATOM   1385 C  CG    . ASP A 1 178 ? 12.341 -18.368 -15.955 1.00 0.00 ? 177 ASP A CG    1 
ATOM   1386 O  OD1   . ASP A 1 178 ? 11.855 -18.616 -17.124 1.00 0.00 ? 177 ASP A OD1   1 
ATOM   1387 O  OD2   . ASP A 1 178 ? 12.541 -19.333 -15.122 1.00 0.00 ? 177 ASP A OD2   1 
ATOM   1388 N  N     . LEU A 1 179 ? 15.152 -18.078 -16.773 1.00 0.00 ? 178 LEU A N     1 
ATOM   1389 C  CA    . LEU A 1 179 ? 16.135 -18.389 -17.790 1.00 0.00 ? 178 LEU A CA    1 
ATOM   1390 C  C     . LEU A 1 179 ? 17.316 -18.978 -17.021 1.00 0.00 ? 178 LEU A C     1 
ATOM   1391 O  O     . LEU A 1 179 ? 17.708 -18.463 -15.963 1.00 0.00 ? 178 LEU A O     1 
ATOM   1392 C  CB    . LEU A 1 179 ? 16.544 -17.106 -18.526 1.00 0.00 ? 178 LEU A CB    1 
ATOM   1393 C  CG    . LEU A 1 179 ? 17.975 -16.664 -18.212 1.00 0.00 ? 178 LEU A CG    1 
ATOM   1394 C  CD1   . LEU A 1 179 ? 18.417 -15.447 -19.027 1.00 0.00 ? 178 LEU A CD1   1 
ATOM   1395 C  CD2   . LEU A 1 179 ? 18.172 -16.276 -16.745 1.00 0.00 ? 178 LEU A CD2   1 
ATOM   1396 N  N     . PRO A 1 180 ? 17.946 -20.053 -17.472 1.00 0.00 ? 179 PRO A N     1 
ATOM   1397 C  CA    . PRO A 1 180 ? 19.017 -20.673 -16.712 1.00 0.00 ? 179 PRO A CA    1 
ATOM   1398 C  C     . PRO A 1 180 ? 20.188 -19.751 -16.488 1.00 0.00 ? 179 PRO A C     1 
ATOM   1399 O  O     . PRO A 1 180 ? 19.973 -18.507 -16.345 1.00 0.00 ? 179 PRO A O     1 
ATOM   1400 C  CB    . PRO A 1 180 ? 19.439 -21.841 -17.570 1.00 0.00 ? 179 PRO A CB    1 
ATOM   1401 C  CG    . PRO A 1 180 ? 18.572 -21.840 -18.821 1.00 0.00 ? 179 PRO A CG    1 
ATOM   1402 C  CD    . PRO A 1 180 ? 17.619 -20.688 -18.748 1.00 0.00 ? 179 PRO A CD    1 
ATOM   1403 N  N     . GLN A 1 181 ? 21.335 -20.426 -16.465 1.00 0.00 ? 180 GLN A N     1 
ATOM   1404 C  CA    . GLN A 1 181 ? 22.685 -19.843 -16.299 1.00 0.00 ? 180 GLN A CA    1 
ATOM   1405 C  C     . GLN A 1 181 ? 22.829 -19.089 -14.969 1.00 0.00 ? 180 GLN A C     1 
ATOM   1406 O  O     . GLN A 1 181 ? 22.496 -17.898 -14.871 1.00 0.00 ? 180 GLN A O     1 
ATOM   1407 C  CB    . GLN A 1 181 ? 22.997 -18.879 -17.444 1.00 0.00 ? 180 GLN A CB    1 
ATOM   1408 C  CG    . GLN A 1 181 ? 24.337 -19.180 -18.123 1.00 0.00 ? 180 GLN A CG    1 
ATOM   1409 C  CD    . GLN A 1 181 ? 24.683 -20.671 -18.131 1.00 0.00 ? 180 GLN A CD    1 
ATOM   1410 O  OE1   . GLN A 1 181 ? 23.859 -21.496 -17.738 1.00 0.00 ? 180 GLN A OE1   1 
ATOM   1411 N  NE2   . GLN A 1 181 ? 25.865 -21.073 -18.559 1.00 0.00 ? 180 GLN A NE2   1 
ATOM   1412 N  N     . ARG A 1 182 ? 23.332 -19.819 -13.970 1.00 0.00 ? 181 ARG A N     1 
ATOM   1413 C  CA    . ARG A 1 182 ? 23.605 -19.265 -12.629 1.00 0.00 ? 181 ARG A CA    1 
ATOM   1414 C  C     . ARG A 1 182 ? 25.111 -19.355 -12.361 1.00 0.00 ? 181 ARG A C     1 
ATOM   1415 O  O     . ARG A 1 182 ? 25.655 -20.447 -12.143 1.00 0.00 ? 181 ARG A O     1 
ATOM   1416 C  CB    . ARG A 1 182 ? 22.849 -20.047 -11.555 1.00 0.00 ? 181 ARG A CB    1 
ATOM   1417 C  CG    . ARG A 1 182 ? 21.816 -21.013 -12.135 1.00 0.00 ? 181 ARG A CG    1 
ATOM   1418 C  CD    . ARG A 1 182 ? 20.474 -20.343 -12.428 1.00 0.00 ? 181 ARG A CD    1 
ATOM   1419 N  NE    . ARG A 1 182 ? 19.337 -21.268 -12.330 1.00 0.00 ? 181 ARG A NE    1 
ATOM   1420 C  CZ    . ARG A 1 182 ? 18.061 -20.874 -12.231 1.00 0.00 ? 181 ARG A CZ    1 
ATOM   1421 N  NH1   . ARG A 1 182 ? 17.740 -19.573 -12.213 1.00 0.00 ? 181 ARG A NH1   1 
ATOM   1422 N  NH2   . ARG A 1 182 ? 17.022 -21.715 -12.144 1.00 0.00 ? 181 ARG A NH2   1 
ATOM   1423 N  N     . ALA A 1 183 ? 25.624 -18.141 -12.410 1.00 0.00 ? 182 ALA A N     1 
ATOM   1424 C  CA    . ALA A 1 183 ? 27.035 -17.744 -12.297 1.00 0.00 ? 182 ALA A CA    1 
ATOM   1425 C  C     . ALA A 1 183 ? 27.220 -16.765 -11.141 1.00 0.00 ? 182 ALA A C     1 
ATOM   1426 O  O     . ALA A 1 183 ? 26.570 -15.710 -11.088 1.00 0.00 ? 182 ALA A O     1 
ATOM   1427 C  CB    . ALA A 1 183 ? 27.497 -17.072 -13.590 1.00 0.00 ? 182 ALA A CB    1 
ATOM   1428 N  N     . ALA A 1 184 ? 28.097 -17.130 -10.238 1.00 0.00 ? 183 ALA A N     1 
ATOM   1429 C  CA    . ALA A 1 184 ? 28.354 -16.341 -9.025  1.00 0.00 ? 183 ALA A CA    1 
ATOM   1430 C  C     . ALA A 1 184 ? 29.765 -15.740 -9.011  1.00 0.00 ? 183 ALA A C     1 
ATOM   1431 O  O     . ALA A 1 184 ? 30.771 -16.466 -9.015  1.00 0.00 ? 183 ALA A O     1 
ATOM   1432 C  CB    . ALA A 1 184 ? 28.226 -17.229 -7.785  1.00 0.00 ? 183 ALA A CB    1 
ATOM   1433 N  N     . GLY A 1 185 ? 29.786 -14.418 -9.013  1.00 0.00 ? 184 GLY A N     1 
ATOM   1434 C  CA    . GLY A 1 185 ? 31.034 -13.649 -8.934  1.00 0.00 ? 184 GLY A CA    1 
ATOM   1435 C  C     . GLY A 1 185 ? 32.006 -14.353 -7.977  1.00 0.00 ? 184 GLY A C     1 
ATOM   1436 O  O     . GLY A 1 185 ? 31.596 -15.165 -7.133  1.00 0.00 ? 184 GLY A O     1 
ATOM   1437 N  N     . PHE A 1 186 ? 33.265 -14.012 -8.150  1.00 0.00 ? 185 PHE A N     1 
ATOM   1438 C  CA    . PHE A 1 186 ? 34.375 -14.572 -7.363  1.00 0.00 ? 185 PHE A CA    1 
ATOM   1439 C  C     . PHE A 1 186 ? 34.089 -14.401 -5.871  1.00 0.00 ? 185 PHE A C     1 
ATOM   1440 O  O     . PHE A 1 186 ? 34.375 -15.293 -5.059  1.00 0.00 ? 185 PHE A O     1 
ATOM   1441 C  CB    . PHE A 1 186 ? 35.664 -13.881 -7.797  1.00 0.00 ? 185 PHE A CB    1 
ATOM   1442 C  CG    . PHE A 1 186 ? 35.836 -13.912 -9.322  1.00 0.00 ? 185 PHE A CG    1 
ATOM   1443 C  CD1   . PHE A 1 186 ? 35.689 -15.121 -10.017 1.00 0.00 ? 185 PHE A CD1   1 
ATOM   1444 C  CD2   . PHE A 1 186 ? 36.130 -12.738 -10.028 1.00 0.00 ? 185 PHE A CD2   1 
ATOM   1445 C  CE1   . PHE A 1 186 ? 35.837 -15.156 -11.409 1.00 0.00 ? 185 PHE A CE1   1 
ATOM   1446 C  CE2   . PHE A 1 186 ? 36.277 -12.773 -11.421 1.00 0.00 ? 185 PHE A CE2   1 
ATOM   1447 C  CZ    . PHE A 1 186 ? 36.131 -13.982 -12.111 1.00 0.00 ? 185 PHE A CZ    1 
ATOM   1448 N  N     . LEU A 1 187 ? 33.527 -13.244 -5.548  1.00 0.00 ? 186 LEU A N     1 
ATOM   1449 C  CA    . LEU A 1 187 ? 33.213 -12.868 -4.155  1.00 0.00 ? 186 LEU A CA    1 
ATOM   1450 C  C     . LEU A 1 187 ? 32.365 -13.933 -3.446  1.00 0.00 ? 186 LEU A C     1 
ATOM   1451 O  O     . LEU A 1 187 ? 32.706 -14.391 -2.345  1.00 0.00 ? 186 LEU A O     1 
ATOM   1452 C  CB    . LEU A 1 187 ? 32.323 -11.617 -4.130  1.00 0.00 ? 186 LEU A CB    1 
ATOM   1453 C  CG    . LEU A 1 187 ? 33.064 -10.315 -4.421  1.00 0.00 ? 186 LEU A CG    1 
ATOM   1454 C  CD1   . LEU A 1 187 ? 32.717 -9.723  -5.789  1.00 0.00 ? 186 LEU A CD1   1 
ATOM   1455 C  CD2   . LEU A 1 187 ? 32.757 -9.215  -3.403  1.00 0.00 ? 186 LEU A CD2   1 
ATOM   1456 N  N     . LEU A 1 188 ? 31.277 -14.303 -4.093  1.00 0.00 ? 187 LEU A N     1 
ATOM   1457 C  CA    . LEU A 1 188 ? 30.363 -15.334 -3.576  1.00 0.00 ? 187 LEU A CA    1 
ATOM   1458 C  C     . LEU A 1 188 ? 31.142 -16.629 -3.410  1.00 0.00 ? 187 LEU A C     1 
ATOM   1459 O  O     . LEU A 1 188 ? 31.029 -17.316 -2.384  1.00 0.00 ? 187 LEU A O     1 
ATOM   1460 C  CB    . LEU A 1 188 ? 29.192 -15.530 -4.540  1.00 0.00 ? 187 LEU A CB    1 
ATOM   1461 C  CG    . LEU A 1 188 ? 28.114 -14.454 -4.387  1.00 0.00 ? 187 LEU A CG    1 
ATOM   1462 C  CD1   . LEU A 1 188 ? 26.809 -14.993 -3.797  1.00 0.00 ? 187 LEU A CD1   1 
ATOM   1463 C  CD2   . LEU A 1 188 ? 28.541 -13.307 -3.468  1.00 0.00 ? 187 LEU A CD2   1 
ATOM   1464 N  N     . GLU A 1 189 ? 31.893 -16.872 -4.457  1.00 0.00 ? 188 GLU A N     1 
ATOM   1465 C  CA    . GLU A 1 189 ? 32.745 -18.047 -4.614  1.00 0.00 ? 188 GLU A CA    1 
ATOM   1466 C  C     . GLU A 1 189 ? 33.720 -18.168 -3.447  1.00 0.00 ? 188 GLU A C     1 
ATOM   1467 O  O     . GLU A 1 189 ? 33.878 -19.246 -2.855  1.00 0.00 ? 188 GLU A O     1 
ATOM   1468 C  CB    . GLU A 1 189 ? 33.566 -17.886 -5.894  1.00 0.00 ? 188 GLU A CB    1 
ATOM   1469 C  CG    . GLU A 1 189 ? 33.810 -19.194 -6.638  1.00 0.00 ? 188 GLU A CG    1 
ATOM   1470 C  CD    . GLU A 1 189 ? 34.682 -19.003 -7.880  1.00 0.00 ? 188 GLU A CD    1 
ATOM   1471 O  OE1   . GLU A 1 189 ? 35.493 -18.003 -7.952  1.00 0.00 ? 188 GLU A OE1   1 
ATOM   1472 O  OE2   . GLU A 1 189 ? 34.606 -19.843 -8.856  1.00 0.00 ? 188 GLU A OE2   1 
ATOM   1473 N  N     . LYS A 1 190 ? 34.350 -17.054 -3.147  1.00 0.00 ? 189 LYS A N     1 
ATOM   1474 C  CA    . LYS A 1 190 ? 35.352 -16.979 -2.077  1.00 0.00 ? 189 LYS A CA    1 
ATOM   1475 C  C     . LYS A 1 190 ? 34.760 -17.427 -0.737  1.00 0.00 ? 189 LYS A C     1 
ATOM   1476 O  O     . LYS A 1 190 ? 35.358 -18.237 -0.014  1.00 0.00 ? 189 LYS A O     1 
ATOM   1477 C  CB    . LYS A 1 190 ? 35.869 -15.548 -1.929  1.00 0.00 ? 189 LYS A CB    1 
ATOM   1478 C  CG    . LYS A 1 190 ? 37.328 -15.488 -1.471  1.00 0.00 ? 189 LYS A CG    1 
ATOM   1479 C  CD    . LYS A 1 190 ? 37.588 -14.385 -0.444  1.00 0.00 ? 189 LYS A CD    1 
ATOM   1480 C  CE    . LYS A 1 190 ? 37.077 -13.016 -0.897  1.00 0.00 ? 189 LYS A CE    1 
ATOM   1481 N  NZ    . LYS A 1 190 ? 37.063 -12.021 0.185   1.00 0.00 ? 189 LYS A NZ    1 
ATOM   1482 N  N     . GLU A 1 191 ? 33.593 -16.890 -0.434  1.00 0.00 ? 190 GLU A N     1 
ATOM   1483 C  CA    . GLU A 1 191 ? 32.899 -17.170 0.835   1.00 0.00 ? 190 GLU A CA    1 
ATOM   1484 C  C     . GLU A 1 191 ? 32.606 -18.627 1.034   1.00 0.00 ? 190 GLU A C     1 
ATOM   1485 O  O     . GLU A 1 191 ? 32.958 -19.214 2.069   1.00 0.00 ? 190 GLU A O     1 
ATOM   1486 C  CB    . GLU A 1 191 ? 31.488 -16.611 0.815   1.00 0.00 ? 190 GLU A CB    1 
ATOM   1487 C  CG    . GLU A 1 191 ? 31.365 -15.240 1.429   1.00 0.00 ? 190 GLU A CG    1 
ATOM   1488 C  CD    . GLU A 1 191 ? 30.528 -14.315 0.560   1.00 0.00 ? 190 GLU A CD    1 
ATOM   1489 O  OE1   . GLU A 1 191 ? 30.792 -13.053 0.523   1.00 0.00 ? 190 GLU A OE1   1 
ATOM   1490 O  OE2   . GLU A 1 191 ? 29.555 -14.793 -0.140  1.00 0.00 ? 190 GLU A OE2   1 
ATOM   1491 N  N     . LEU A 1 192 ? 31.968 -19.140 0.016   1.00 0.00 ? 191 LEU A N     1 
ATOM   1492 C  CA    . LEU A 1 192 ? 31.517 -20.509 0.012   1.00 0.00 ? 191 LEU A CA    1 
ATOM   1493 C  C     . LEU A 1 192 ? 32.712 -21.394 0.224   1.00 0.00 ? 191 LEU A C     1 
ATOM   1494 O  O     . LEU A 1 192 ? 32.698 -22.293 1.078   1.00 0.00 ? 191 LEU A O     1 
ATOM   1495 C  CB    . LEU A 1 192 ? 30.840 -20.827 -1.323  1.00 0.00 ? 191 LEU A CB    1 
ATOM   1496 C  CG    . LEU A 1 192 ? 29.482 -20.137 -1.486  1.00 0.00 ? 191 LEU A CG    1 
ATOM   1497 C  CD1   . LEU A 1 192 ? 29.300 -18.943 -0.547  1.00 0.00 ? 191 LEU A CD1   1 
ATOM   1498 C  CD2   . LEU A 1 192 ? 29.253 -19.592 -2.898  1.00 0.00 ? 191 LEU A CD2   1 
ATOM   1499 N  N     . LYS A 1 193 ? 33.721 -21.118 -0.563  1.00 0.00 ? 192 LYS A N     1 
ATOM   1500 C  CA    . LYS A 1 193 ? 34.958 -21.875 -0.484  1.00 0.00 ? 192 LYS A CA    1 
ATOM   1501 C  C     . LYS A 1 193 ? 35.614 -21.728 0.891   1.00 0.00 ? 192 LYS A C     1 
ATOM   1502 O  O     . LYS A 1 193 ? 35.880 -22.723 1.581   1.00 0.00 ? 192 LYS A O     1 
ATOM   1503 C  CB    . LYS A 1 193 ? 35.944 -21.359 -1.529  1.00 0.00 ? 192 LYS A CB    1 
ATOM   1504 C  CG    . LYS A 1 193 ? 36.638 -22.479 -2.299  1.00 0.00 ? 192 LYS A CG    1 
ATOM   1505 C  CD    . LYS A 1 193 ? 37.267 -22.000 -3.607  1.00 0.00 ? 192 LYS A CD    1 
ATOM   1506 C  CE    . LYS A 1 193 ? 37.296 -23.081 -4.687  1.00 0.00 ? 192 LYS A CE    1 
ATOM   1507 N  NZ    . LYS A 1 193 ? 38.304 -22.827 -5.726  1.00 0.00 ? 192 LYS A NZ    1 
ATOM   1508 N  N     . TYR A 1 194 ? 35.875 -20.486 1.285   1.00 0.00 ? 193 TYR A N     1 
ATOM   1509 C  CA    . TYR A 1 194 ? 36.501 -20.223 2.594   1.00 0.00 ? 193 TYR A CA    1 
ATOM   1510 C  C     . TYR A 1 194 ? 35.568 -20.639 3.709   1.00 0.00 ? 193 TYR A C     1 
ATOM   1511 O  O     . TYR A 1 194 ? 35.937 -21.431 4.589   1.00 0.00 ? 193 TYR A O     1 
ATOM   1512 C  CB    . TYR A 1 194 ? 36.848 -18.750 2.728   1.00 0.00 ? 193 TYR A CB    1 
ATOM   1513 C  CG    . TYR A 1 194 ? 38.347 -18.526 2.605   1.00 0.00 ? 193 TYR A CG    1 
ATOM   1514 C  CD1   . TYR A 1 194 ? 39.141 -18.486 3.753   1.00 0.00 ? 193 TYR A CD1   1 
ATOM   1515 C  CD2   . TYR A 1 194 ? 38.924 -18.376 1.340   1.00 0.00 ? 193 TYR A CD2   1 
ATOM   1516 C  CE1   . TYR A 1 194 ? 40.521 -18.297 3.638   1.00 0.00 ? 193 TYR A CE1   1 
ATOM   1517 C  CE2   . TYR A 1 194 ? 40.304 -18.189 1.224   1.00 0.00 ? 193 TYR A CE2   1 
ATOM   1518 C  CZ    . TYR A 1 194 ? 41.103 -18.150 2.373   1.00 0.00 ? 193 TYR A CZ    1 
ATOM   1519 O  OH    . TYR A 1 194 ? 42.447 -17.970 2.260   1.00 0.00 ? 193 TYR A OH    1 
ATOM   1520 N  N     . PHE A 1 195 ? 34.405 -20.063 3.581   1.00 0.00 ? 194 PHE A N     1 
ATOM   1521 C  CA    . PHE A 1 195 ? 33.276 -20.286 4.461   1.00 0.00 ? 194 PHE A CA    1 
ATOM   1522 C  C     . PHE A 1 195 ? 32.825 -21.710 4.405   1.00 0.00 ? 194 PHE A C     1 
ATOM   1523 O  O     . PHE A 1 195 ? 32.611 -22.354 5.442   1.00 0.00 ? 194 PHE A O     1 
ATOM   1524 C  CB    . PHE A 1 195 ? 32.059 -19.515 3.969   1.00 0.00 ? 194 PHE A CB    1 
ATOM   1525 C  CG    . PHE A 1 195 ? 31.694 -18.300 4.802   1.00 0.00 ? 194 PHE A CG    1 
ATOM   1526 C  CD1   . PHE A 1 195 ? 32.184 -18.154 6.104   1.00 0.00 ? 194 PHE A CD1   1 
ATOM   1527 C  CD2   . PHE A 1 195 ? 30.858 -17.332 4.242   1.00 0.00 ? 194 PHE A CD2   1 
ATOM   1528 C  CE1   . PHE A 1 195 ? 31.841 -17.019 6.847   1.00 0.00 ? 194 PHE A CE1   1 
ATOM   1529 C  CE2   . PHE A 1 195 ? 30.516 -16.201 4.985   1.00 0.00 ? 194 PHE A CE2   1 
ATOM   1530 C  CZ    . PHE A 1 195 ? 31.008 -16.041 6.286   1.00 0.00 ? 194 PHE A CZ    1 
ATOM   1531 N  N     . GLY A 1 196 ? 32.704 -22.130 3.180   1.00 0.00 ? 195 GLY A N     1 
ATOM   1532 C  CA    . GLY A 1 196 ? 32.054 -23.392 2.852   1.00 0.00 ? 195 GLY A CA    1 
ATOM   1533 C  C     . GLY A 1 196 ? 32.650 -24.626 3.538   1.00 0.00 ? 195 GLY A C     1 
ATOM   1534 O  O     . GLY A 1 196 ? 31.933 -25.403 4.183   1.00 0.00 ? 195 GLY A O     1 
ATOM   1535 N  N     . LYS A 1 197 ? 33.946 -24.806 3.406   1.00 0.00 ? 196 LYS A N     1 
ATOM   1536 C  CA    . LYS A 1 197 ? 34.678 -26.012 3.919   1.00 0.00 ? 196 LYS A CA    1 
ATOM   1537 C  C     . LYS A 1 197 ? 34.759 -26.260 5.442   1.00 0.00 ? 196 LYS A C     1 
ATOM   1538 O  O     . LYS A 1 197 ? 34.515 -27.376 5.923   1.00 0.00 ? 196 LYS A O     1 
ATOM   1539 C  CB    . LYS A 1 197 ? 36.108 -26.052 3.423   1.00 0.00 ? 196 LYS A CB    1 
ATOM   1540 C  CG    . LYS A 1 197 ? 36.831 -24.732 3.604   1.00 0.00 ? 196 LYS A CG    1 
ATOM   1541 C  CD    . LYS A 1 197 ? 38.346 -24.881 3.565   1.00 0.00 ? 196 LYS A CD    1 
ATOM   1542 C  CE    . LYS A 1 197 ? 39.016 -23.846 2.663   1.00 0.00 ? 196 LYS A CE    1 
ATOM   1543 N  NZ    . LYS A 1 197 ? 40.442 -24.120 2.437   1.00 0.00 ? 196 LYS A NZ    1 
ATOM   1544 N  N     . ALA A 1 198 ? 35.092 -25.259 6.243   1.00 0.00 ? 197 ALA A N     1 
ATOM   1545 C  CA    . ALA A 1 198 ? 35.298 -25.535 7.667   1.00 0.00 ? 197 ALA A CA    1 
ATOM   1546 C  C     . ALA A 1 198 ? 34.159 -26.452 7.944   1.00 0.00 ? 197 ALA A C     1 
ATOM   1547 O  O     . ALA A 1 198 ? 34.276 -27.389 8.749   1.00 0.00 ? 197 ALA A O     1 
ATOM   1548 C  CB    . ALA A 1 198 ? 35.241 -24.235 8.471   1.00 0.00 ? 197 ALA A CB    1 
ATOM   1549 N  N     . LEU A 1 199 ? 33.146 -26.070 7.226   1.00 0.00 ? 198 LEU A N     1 
ATOM   1550 C  CA    . LEU A 1 199 ? 31.904 -26.799 7.109   1.00 0.00 ? 198 LEU A CA    1 
ATOM   1551 C  C     . LEU A 1 199 ? 32.174 -28.256 6.639   1.00 0.00 ? 198 LEU A C     1 
ATOM   1552 O  O     . LEU A 1 199 ? 31.617 -29.218 7.188   1.00 0.00 ? 198 LEU A O     1 
ATOM   1553 C  CB    . LEU A 1 199 ? 31.015 -26.108 6.082   1.00 0.00 ? 198 LEU A CB    1 
ATOM   1554 C  CG    . LEU A 1 199 ? 30.805 -24.631 6.390   1.00 0.00 ? 198 LEU A CG    1 
ATOM   1555 C  CD1   . LEU A 1 199 ? 29.370 -24.167 6.133   1.00 0.00 ? 198 LEU A CD1   1 
ATOM   1556 C  CD2   . LEU A 1 199 ? 31.103 -24.276 7.848   1.00 0.00 ? 198 LEU A CD2   1 
ATOM   1557 N  N     . GLU A 1 200 ? 33.027 -28.422 5.619   1.00 0.00 ? 199 GLU A N     1 
ATOM   1558 C  CA    . GLU A 1 200 ? 33.366 -29.773 5.065   1.00 0.00 ? 199 GLU A CA    1 
ATOM   1559 C  C     . GLU A 1 200 ? 34.092 -30.634 6.126   1.00 0.00 ? 199 GLU A C     1 
ATOM   1560 O  O     . GLU A 1 200 ? 33.577 -30.851 7.233   1.00 0.00 ? 199 GLU A O     1 
ATOM   1561 C  CB    . GLU A 1 200 ? 34.246 -29.646 3.811   1.00 0.00 ? 199 GLU A CB    1 
ATOM   1562 C  CG    . GLU A 1 200 ? 33.473 -29.923 2.510   1.00 0.00 ? 199 GLU A CG    1 
ATOM   1563 C  CD    . GLU A 1 200 ? 34.283 -30.698 1.463   1.00 0.00 ? 199 GLU A CD    1 
ATOM   1564 O  OE1   . GLU A 1 200 ? 33.678 -31.318 0.507   1.00 0.00 ? 199 GLU A OE1   1 
ATOM   1565 O  OE2   . GLU A 1 200 ? 35.571 -30.731 1.538   1.00 0.00 ? 199 GLU A OE2   1 
ATOM   1566 N  N     . ASN A 1 201 ? 35.286 -31.115 5.773   1.00 0.00 ? 200 ASN A N     1 
ATOM   1567 C  CA    . ASN A 1 201 ? 36.101 -31.978 6.673   1.00 0.00 ? 200 ASN A CA    1 
ATOM   1568 C  C     . ASN A 1 201 ? 37.514 -31.422 6.858   1.00 0.00 ? 200 ASN A C     1 
ATOM   1569 O  O     . ASN A 1 201 ? 38.502 -32.171 6.850   1.00 0.00 ? 200 ASN A O     1 
ATOM   1570 C  CB    . ASN A 1 201 ? 36.231 -33.387 6.096   1.00 0.00 ? 200 ASN A CB    1 
ATOM   1571 C  CG    . ASN A 1 201 ? 37.415 -34.159 6.684   1.00 0.00 ? 200 ASN A CG    1 
ATOM   1572 O  OD1   . ASN A 1 201 ? 37.729 -34.000 7.863   1.00 0.00 ? 200 ASN A OD1   1 
ATOM   1573 N  ND2   . ASN A 1 201 ? 38.100 -34.995 5.926   1.00 0.00 ? 200 ASN A ND2   1 
ATOM   1574 N  N     . PRO A 1 202 ? 37.687 -30.108 7.031   1.00 0.00 ? 201 PRO A N     1 
ATOM   1575 C  CA    . PRO A 1 202 ? 39.012 -29.533 7.208   1.00 0.00 ? 201 PRO A CA    1 
ATOM   1576 C  C     . PRO A 1 202 ? 39.696 -30.083 8.442   1.00 0.00 ? 201 PRO A C     1 
ATOM   1577 O  O     . PRO A 1 202 ? 39.147 -29.918 9.575   1.00 0.00 ? 201 PRO A O     1 
ATOM   1578 C  CB    . PRO A 1 202 ? 38.746 -28.051 7.346   1.00 0.00 ? 201 PRO A CB    1 
ATOM   1579 C  CG    . PRO A 1 202 ? 37.243 -27.833 7.244   1.00 0.00 ? 201 PRO A CG    1 
ATOM   1580 C  CD    . PRO A 1 202 ? 36.574 -29.157 7.047   1.00 0.00 ? 201 PRO A CD    1 
ATOM   1581 N  N     . THR A 1 203 ? 40.852 -30.720 8.215   1.00 0.00 ? 202 THR A N     1 
ATOM   1582 C  CA    . THR A 1 203 ? 41.679 -31.253 9.311   1.00 0.00 ? 202 THR A CA    1 
ATOM   1583 C  C     . THR A 1 203 ? 42.060 -30.089 10.194  1.00 0.00 ? 202 THR A C     1 
ATOM   1584 O  O     . THR A 1 203 ? 41.577 -29.964 11.329  1.00 0.00 ? 202 THR A O     1 
ATOM   1585 C  CB    . THR A 1 203 ? 42.949 -31.922 8.781   1.00 0.00 ? 202 THR A CB    1 
ATOM   1586 O  OG1   . THR A 1 203 ? 42.783 -33.332 8.761   1.00 0.00 ? 202 THR A OG1   1 
ATOM   1587 C  CG2   . THR A 1 203 ? 44.183 -31.619 9.634   1.00 0.00 ? 202 THR A CG2   1 
ATOM   1588 N  N     . ARG A 1 204 ? 42.937 -29.238 9.671   1.00 0.00 ? 203 ARG A N     1 
ATOM   1589 C  CA    . ARG A 1 204 ? 43.247 -28.056 10.429  1.00 0.00 ? 203 ARG A CA    1 
ATOM   1590 C  C     . ARG A 1 204 ? 41.995 -27.892 11.241  1.00 0.00 ? 203 ARG A C     1 
ATOM   1591 O  O     . ARG A 1 204 ? 40.883 -27.832 10.695  1.00 0.00 ? 203 ARG A O     1 
ATOM   1592 C  CB    . ARG A 1 204 ? 43.544 -26.881 9.498   1.00 0.00 ? 203 ARG A CB    1 
ATOM   1593 C  CG    . ARG A 1 204 ? 42.599 -26.817 8.297   1.00 0.00 ? 203 ARG A CG    1 
ATOM   1594 C  CD    . ARG A 1 204 ? 43.337 -26.716 6.961   1.00 0.00 ? 203 ARG A CD    1 
ATOM   1595 N  NE    . ARG A 1 204 ? 43.890 -25.377 6.711   1.00 0.00 ? 203 ARG A NE    1 
ATOM   1596 C  CZ    . ARG A 1 204 ? 43.980 -24.819 5.497   1.00 0.00 ? 203 ARG A CZ    1 
ATOM   1597 N  NH1   . ARG A 1 204 ? 43.558 -25.471 4.405   1.00 0.00 ? 203 ARG A NH1   1 
ATOM   1598 N  NH2   . ARG A 1 204 ? 44.484 -23.598 5.268   1.00 0.00 ? 203 ARG A NH2   1 
ATOM   1599 N  N     . PRO A 1 205 ? 42.060 -27.810 12.542  1.00 0.00 ? 204 PRO A N     1 
ATOM   1600 C  CA    . PRO A 1 205 ? 40.865 -27.817 13.313  1.00 0.00 ? 204 PRO A CA    1 
ATOM   1601 C  C     . PRO A 1 205 ? 40.006 -26.698 12.921  1.00 0.00 ? 204 PRO A C     1 
ATOM   1602 O  O     . PRO A 1 205 ? 40.437 -25.858 12.072  1.00 0.00 ? 204 PRO A O     1 
ATOM   1603 C  CB    . PRO A 1 205 ? 41.345 -27.664 14.734  1.00 0.00 ? 204 PRO A CB    1 
ATOM   1604 C  CG    . PRO A 1 205 ? 42.863 -27.582 14.701  1.00 0.00 ? 204 PRO A CG    1 
ATOM   1605 C  CD    . PRO A 1 205 ? 43.314 -27.691 13.279  1.00 0.00 ? 204 PRO A CD    1 
ATOM   1606 N  N     . PHE A 1 206 ? 38.870 -26.731 13.513  1.00 0.00 ? 205 PHE A N     1 
ATOM   1607 C  CA    . PHE A 1 206 ? 37.973 -25.640 13.421  1.00 0.00 ? 205 PHE A CA    1 
ATOM   1608 C  C     . PHE A 1 206 ? 37.964 -25.159 14.829  1.00 0.00 ? 205 PHE A C     1 
ATOM   1609 O  O     . PHE A 1 206 ? 37.374 -25.794 15.715  1.00 0.00 ? 205 PHE A O     1 
ATOM   1610 C  CB    . PHE A 1 206 ? 36.591 -26.074 12.923  1.00 0.00 ? 205 PHE A CB    1 
ATOM   1611 C  CG    . PHE A 1 206 ? 35.681 -24.876 12.595  1.00 0.00 ? 205 PHE A CG    1 
ATOM   1612 C  CD1   . PHE A 1 206 ? 36.194 -23.571 12.634  1.00 0.00 ? 205 PHE A CD1   1 
ATOM   1613 C  CD2   . PHE A 1 206 ? 34.336 -25.080 12.256  1.00 0.00 ? 205 PHE A CD2   1 
ATOM   1614 C  CE1   . PHE A 1 206 ? 35.368 -22.479 12.335  1.00 0.00 ? 205 PHE A CE1   1 
ATOM   1615 C  CE2   . PHE A 1 206 ? 33.510 -23.986 11.958  1.00 0.00 ? 205 PHE A CE2   1 
ATOM   1616 C  CZ    . PHE A 1 206 ? 34.027 -22.687 11.997  1.00 0.00 ? 205 PHE A CZ    1 
ATOM   1617 N  N     . LEU A 1 207 ? 38.632 -24.062 14.894  1.00 0.00 ? 206 LEU A N     1 
ATOM   1618 C  CA    . LEU A 1 207 ? 38.903 -23.343 16.092  1.00 0.00 ? 206 LEU A CA    1 
ATOM   1619 C  C     . LEU A 1 207 ? 38.148 -22.090 15.944  1.00 0.00 ? 206 LEU A C     1 
ATOM   1620 O  O     . LEU A 1 207 ? 38.386 -21.311 15.010  1.00 0.00 ? 206 LEU A O     1 
ATOM   1621 C  CB    . LEU A 1 207 ? 40.360 -23.005 16.259  1.00 0.00 ? 206 LEU A CB    1 
ATOM   1622 C  CG    . LEU A 1 207 ? 40.503 -21.625 16.888  1.00 0.00 ? 206 LEU A CG    1 
ATOM   1623 C  CD1   . LEU A 1 207 ? 41.892 -21.374 17.476  1.00 0.00 ? 206 LEU A CD1   1 
ATOM   1624 C  CD2   . LEU A 1 207 ? 40.260 -20.489 15.891  1.00 0.00 ? 206 LEU A CD2   1 
ATOM   1625 N  N     . ALA A 1 208 ? 37.288 -21.992 16.889  1.00 0.00 ? 207 ALA A N     1 
ATOM   1626 C  CA    . ALA A 1 208 ? 36.203 -21.044 16.889  1.00 0.00 ? 207 ALA A CA    1 
ATOM   1627 C  C     . ALA A 1 208 ? 36.302 -19.976 17.950  1.00 0.00 ? 207 ALA A C     1 
ATOM   1628 O  O     . ALA A 1 208 ? 36.380 -20.274 19.151  1.00 0.00 ? 207 ALA A O     1 
ATOM   1629 C  CB    . ALA A 1 208 ? 34.879 -21.770 17.134  1.00 0.00 ? 207 ALA A CB    1 
ATOM   1630 N  N     . ILE A 1 209 ? 36.297 -18.750 17.436  1.00 0.00 ? 208 ILE A N     1 
ATOM   1631 C  CA    . ILE A 1 209 ? 36.316 -17.545 18.283  1.00 0.00 ? 208 ILE A CA    1 
ATOM   1632 C  C     . ILE A 1 209 ? 35.059 -16.654 18.136  1.00 0.00 ? 208 ILE A C     1 
ATOM   1633 O  O     . ILE A 1 209 ? 34.833 -16.037 17.085  1.00 0.00 ? 208 ILE A O     1 
ATOM   1634 C  CB    . ILE A 1 209 ? 37.461 -16.625 17.898  1.00 0.00 ? 208 ILE A CB    1 
ATOM   1635 C  CG1   . ILE A 1 209 ? 38.445 -16.391 19.040  1.00 0.00 ? 208 ILE A CG1   1 
ATOM   1636 C  CG2   . ILE A 1 209 ? 36.988 -15.235 17.467  1.00 0.00 ? 208 ILE A CG2   1 
ATOM   1637 C  CD1   . ILE A 1 209 ? 39.828 -16.984 18.766  1.00 0.00 ? 208 ILE A CD1   1 
ATOM   1638 N  N     . LEU A 1 210 ? 34.278 -16.632 19.224  1.00 0.00 ? 209 LEU A N     1 
ATOM   1639 C  CA    . LEU A 1 210 ? 33.099 -15.732 19.403  1.00 0.00 ? 209 LEU A CA    1 
ATOM   1640 C  C     . LEU A 1 210 ? 33.222 -14.914 20.726  1.00 0.00 ? 209 LEU A C     1 
ATOM   1641 O  O     . LEU A 1 210 ? 33.237 -15.480 21.829  1.00 0.00 ? 209 LEU A O     1 
ATOM   1642 C  CB    . LEU A 1 210 ? 31.800 -16.523 19.387  1.00 0.00 ? 209 LEU A CB    1 
ATOM   1643 C  CG    . LEU A 1 210 ? 30.913 -16.126 18.203  1.00 0.00 ? 209 LEU A CG    1 
ATOM   1644 C  CD1   . LEU A 1 210 ? 29.661 -16.995 18.074  1.00 0.00 ? 209 LEU A CD1   1 
ATOM   1645 C  CD2   . LEU A 1 210 ? 30.409 -14.684 18.291  1.00 0.00 ? 209 LEU A CD2   1 
ATOM   1646 N  N     . GLY A 1 211 ? 33.307 -13.584 20.628  1.00 0.00 ? 210 GLY A N     1 
ATOM   1647 C  CA    . GLY A 1 211 ? 33.441 -12.690 21.829  1.00 0.00 ? 210 GLY A CA    1 
ATOM   1648 C  C     . GLY A 1 211 ? 32.070 -12.161 22.362  1.00 0.00 ? 210 GLY A C     1 
ATOM   1649 O  O     . GLY A 1 211 ? 31.021 -12.354 21.729  1.00 0.00 ? 210 GLY A O     1 
ATOM   1650 N  N     . GLY A 1 212 ? 32.161 -11.503 23.542  1.00 0.00 ? 211 GLY A N     1 
ATOM   1651 C  CA    . GLY A 1 212 ? 31.016 -10.860 24.282  1.00 0.00 ? 211 GLY A CA    1 
ATOM   1652 C  C     . GLY A 1 212 ? 29.907 -11.863 24.569  1.00 0.00 ? 211 GLY A C     1 
ATOM   1653 O  O     . GLY A 1 212 ? 29.866 -12.955 23.982  1.00 0.00 ? 211 GLY A O     1 
ATOM   1654 N  N     . ALA A 1 213 ? 29.046 -11.459 25.470  1.00 0.00 ? 212 ALA A N     1 
ATOM   1655 C  CA    . ALA A 1 213 ? 27.898 -12.266 25.866  1.00 0.00 ? 212 ALA A CA    1 
ATOM   1656 C  C     . ALA A 1 213 ? 26.778 -12.060 24.858  1.00 0.00 ? 212 ALA A C     1 
ATOM   1657 O  O     . ALA A 1 213 ? 26.950 -12.307 23.654  1.00 0.00 ? 212 ALA A O     1 
ATOM   1658 C  CB    . ALA A 1 213 ? 27.414 -11.841 27.253  1.00 0.00 ? 212 ALA A CB    1 
ATOM   1659 N  N     . LYS A 1 214 ? 25.690 -11.620 25.428  1.00 0.00 ? 213 LYS A N     1 
ATOM   1660 C  CA    . LYS A 1 214 ? 24.466 -11.273 24.718  1.00 0.00 ? 213 LYS A CA    1 
ATOM   1661 C  C     . LYS A 1 214 ? 24.312 -12.070 23.426  1.00 0.00 ? 213 LYS A C     1 
ATOM   1662 O  O     . LYS A 1 214 ? 25.239 -12.143 22.605  1.00 0.00 ? 213 LYS A O     1 
ATOM   1663 C  CB    . LYS A 1 214 ? 24.483 -9.778  24.403  1.00 0.00 ? 213 LYS A CB    1 
ATOM   1664 C  CG    . LYS A 1 214 ? 23.738 -9.415  23.123  1.00 0.00 ? 213 LYS A CG    1 
ATOM   1665 C  CD    . LYS A 1 214 ? 24.005 -7.978  22.675  1.00 0.00 ? 213 LYS A CD    1 
ATOM   1666 C  CE    . LYS A 1 214 ? 23.814 -7.776  21.171  1.00 0.00 ? 213 LYS A CE    1 
ATOM   1667 N  NZ    . LYS A 1 214 ? 25.084 -7.633  20.445  1.00 0.00 ? 213 LYS A NZ    1 
ATOM   1668 N  N     . VAL A 1 215 ? 23.118 -12.617 23.351  1.00 0.00 ? 214 VAL A N     1 
ATOM   1669 C  CA    . VAL A 1 215 ? 22.634 -13.391 22.221  1.00 0.00 ? 214 VAL A CA    1 
ATOM   1670 C  C     . VAL A 1 215 ? 21.599 -12.517 21.476  1.00 0.00 ? 214 VAL A C     1 
ATOM   1671 O  O     . VAL A 1 215 ? 21.492 -11.306 21.720  1.00 0.00 ? 214 VAL A O     1 
ATOM   1672 C  CB    . VAL A 1 215 ? 22.038 -14.709 22.737  1.00 0.00 ? 214 VAL A CB    1 
ATOM   1673 C  CG1   . VAL A 1 215 ? 22.064 -15.828 21.694  1.00 0.00 ? 214 VAL A CG1   1 
ATOM   1674 C  CG2   . VAL A 1 215 ? 22.781 -15.263 23.955  1.00 0.00 ? 214 VAL A CG2   1 
ATOM   1675 N  N     . ALA A 1 216 ? 20.874 -13.168 20.628  1.00 0.00 ? 215 ALA A N     1 
ATOM   1676 C  CA    . ALA A 1 216 ? 19.872 -12.605 19.698  1.00 0.00 ? 215 ALA A CA    1 
ATOM   1677 C  C     . ALA A 1 216 ? 19.996 -13.593 18.638  1.00 0.00 ? 215 ALA A C     1 
ATOM   1678 O  O     . ALA A 1 216 ? 21.069 -14.180 18.435  1.00 0.00 ? 215 ALA A O     1 
ATOM   1679 C  CB    . ALA A 1 216 ? 20.272 -11.184 19.294  1.00 0.00 ? 215 ALA A CB    1 
ATOM   1680 N  N     . ASP A 1 217 ? 19.061 -13.936 17.830  1.00 0.00 ? 216 ASP A N     1 
ATOM   1681 C  CA    . ASP A 1 217 ? 19.572 -15.051 17.168  1.00 0.00 ? 216 ASP A CA    1 
ATOM   1682 C  C     . ASP A 1 217 ? 20.851 -15.123 17.964  1.00 0.00 ? 216 ASP A C     1 
ATOM   1683 O  O     . ASP A 1 217 ? 21.725 -15.961 17.697  1.00 0.00 ? 216 ASP A O     1 
ATOM   1684 C  CB    . ASP A 1 217 ? 19.907 -14.830 15.707  1.00 0.00 ? 216 ASP A CB    1 
ATOM   1685 C  CG    . ASP A 1 217 ? 21.079 -15.735 15.283  1.00 0.00 ? 216 ASP A CG    1 
ATOM   1686 O  OD1   . ASP A 1 217 ? 21.453 -15.775 14.049  1.00 0.00 ? 216 ASP A OD1   1 
ATOM   1687 O  OD2   . ASP A 1 217 ? 21.689 -16.457 16.163  1.00 0.00 ? 216 ASP A OD2   1 
ATOM   1688 N  N     . LYS A 1 218 ? 20.863 -14.174 18.942  1.00 0.00 ? 217 LYS A N     1 
ATOM   1689 C  CA    . LYS A 1 218 ? 22.012 -14.011 19.810  1.00 0.00 ? 217 LYS A CA    1 
ATOM   1690 C  C     . LYS A 1 218 ? 22.219 -15.399 20.239  1.00 0.00 ? 217 LYS A C     1 
ATOM   1691 O  O     . LYS A 1 218 ? 23.342 -15.920 20.187  1.00 0.00 ? 217 LYS A O     1 
ATOM   1692 C  CB    . LYS A 1 218 ? 21.663 -13.086 20.985  1.00 0.00 ? 217 LYS A CB    1 
ATOM   1693 C  CG    . LYS A 1 218 ? 22.451 -13.407 22.257  1.00 0.00 ? 217 LYS A CG    1 
ATOM   1694 C  CD    . LYS A 1 218 ? 23.893 -12.902 22.209  1.00 0.00 ? 217 LYS A CD    1 
ATOM   1695 C  CE    . LYS A 1 218 ? 24.783 -13.724 21.274  1.00 0.00 ? 217 LYS A CE    1 
ATOM   1696 N  NZ    . LYS A 1 218 ? 26.105 -13.119 21.060  1.00 0.00 ? 217 LYS A NZ    1 
ATOM   1697 N  N     . ILE A 1 219 ? 21.083 -15.884 20.643  1.00 0.00 ? 218 ILE A N     1 
ATOM   1698 C  CA    . ILE A 1 219 ? 20.854 -17.282 20.868  1.00 0.00 ? 218 ILE A CA    1 
ATOM   1699 C  C     . ILE A 1 219 ? 20.972 -17.993 19.517  1.00 0.00 ? 218 ILE A C     1 
ATOM   1700 O  O     . ILE A 1 219 ? 21.609 -19.050 19.402  1.00 0.00 ? 218 ILE A O     1 
ATOM   1701 C  CB    . ILE A 1 219 ? 19.491 -17.504 21.497  1.00 0.00 ? 218 ILE A CB    1 
ATOM   1702 C  CG1   . ILE A 1 219 ? 19.575 -17.872 22.979  1.00 0.00 ? 218 ILE A CG1   1 
ATOM   1703 C  CG2   . ILE A 1 219 ? 18.702 -18.632 20.829  1.00 0.00 ? 218 ILE A CG2   1 
ATOM   1704 C  CD1   . ILE A 1 219 ? 19.446 -19.376 23.228  1.00 0.00 ? 218 ILE A CD1   1 
ATOM   1705 N  N     . GLN A 1 220 ? 20.341 -17.387 18.505  1.00 0.00 ? 219 GLN A N     1 
ATOM   1706 C  CA    . GLN A 1 220 ? 20.314 -17.981 17.161  1.00 0.00 ? 219 GLN A CA    1 
ATOM   1707 C  C     . GLN A 1 220 ? 21.705 -18.286 16.745  1.00 0.00 ? 219 GLN A C     1 
ATOM   1708 O  O     . GLN A 1 220 ? 21.987 -19.363 16.200  1.00 0.00 ? 219 GLN A O     1 
ATOM   1709 C  CB    . GLN A 1 220 ? 19.777 -17.048 16.074  1.00 0.00 ? 219 GLN A CB    1 
ATOM   1710 C  CG    . GLN A 1 220 ? 20.166 -17.515 14.653  1.00 0.00 ? 219 GLN A CG    1 
ATOM   1711 C  CD    . GLN A 1 220 ? 21.676 -17.743 14.463  1.00 0.00 ? 219 GLN A CD    1 
ATOM   1712 O  OE1   . GLN A 1 220 ? 22.247 -17.293 13.470  1.00 0.00 ? 219 GLN A OE1   1 
ATOM   1713 N  NE2   . GLN A 1 220 ? 22.362 -18.421 15.364  1.00 0.00 ? 219 GLN A NE2   1 
ATOM   1714 N  N     . LEU A 1 221 ? 22.557 -17.344 16.999  1.00 0.00 ? 220 LEU A N     1 
ATOM   1715 C  CA    . LEU A 1 221 ? 23.924 -17.529 16.609  1.00 0.00 ? 220 LEU A CA    1 
ATOM   1716 C  C     . LEU A 1 221 ? 24.427 -18.819 17.176  1.00 0.00 ? 220 LEU A C     1 
ATOM   1717 O  O     . LEU A 1 221 ? 25.071 -19.615 16.477  1.00 0.00 ? 220 LEU A O     1 
ATOM   1718 C  CB    . LEU A 1 221 ? 24.864 -16.485 17.181  1.00 0.00 ? 220 LEU A CB    1 
ATOM   1719 C  CG    . LEU A 1 221 ? 26.283 -17.052 17.314  1.00 0.00 ? 220 LEU A CG    1 
ATOM   1720 C  CD1   . LEU A 1 221 ? 27.159 -16.763 16.093  1.00 0.00 ? 220 LEU A CD1   1 
ATOM   1721 C  CD2   . LEU A 1 221 ? 27.047 -16.487 18.513  1.00 0.00 ? 220 LEU A CD2   1 
ATOM   1722 N  N     . ILE A 1 222 ? 24.118 -18.992 18.429  1.00 0.00 ? 221 ILE A N     1 
ATOM   1723 C  CA    . ILE A 1 222 ? 24.634 -20.118 19.172  1.00 0.00 ? 221 ILE A CA    1 
ATOM   1724 C  C     . ILE A 1 222 ? 24.295 -21.454 18.596  1.00 0.00 ? 221 ILE A C     1 
ATOM   1725 O  O     . ILE A 1 222 ? 25.175 -22.299 18.376  1.00 0.00 ? 221 ILE A O     1 
ATOM   1726 C  CB    . ILE A 1 222 ? 24.100 -20.183 20.594  1.00 0.00 ? 221 ILE A CB    1 
ATOM   1727 C  CG1   . ILE A 1 222 ? 25.218 -20.161 21.639  1.00 0.00 ? 221 ILE A CG1   1 
ATOM   1728 C  CG2   . ILE A 1 222 ? 23.300 -21.458 20.872  1.00 0.00 ? 221 ILE A CG2   1 
ATOM   1729 C  CD1   . ILE A 1 222 ? 26.517 -20.796 21.137  1.00 0.00 ? 221 ILE A CD1   1 
ATOM   1730 N  N     . ASP A 1 223 ? 23.064 -21.753 18.310  1.00 0.00 ? 222 ASP A N     1 
ATOM   1731 C  CA    . ASP A 1 223 ? 22.920 -23.118 17.898  1.00 0.00 ? 222 ASP A CA    1 
ATOM   1732 C  C     . ASP A 1 223 ? 23.707 -23.433 16.663  1.00 0.00 ? 222 ASP A C     1 
ATOM   1733 O  O     . ASP A 1 223 ? 24.492 -24.391 16.632  1.00 0.00 ? 222 ASP A O     1 
ATOM   1734 C  CB    . ASP A 1 223 ? 21.541 -23.638 17.617  1.00 0.00 ? 222 ASP A CB    1 
ATOM   1735 C  CG    . ASP A 1 223 ? 21.635 -25.162 17.428  1.00 0.00 ? 222 ASP A CG    1 
ATOM   1736 O  OD1   . ASP A 1 223 ? 20.578 -25.894 17.528  1.00 0.00 ? 222 ASP A OD1   1 
ATOM   1737 O  OD2   . ASP A 1 223 ? 22.775 -25.710 17.168  1.00 0.00 ? 222 ASP A OD2   1 
ATOM   1738 N  N     . ASN A 1 224 ? 23.574 -22.691 15.591  1.00 0.00 ? 223 ASN A N     1 
ATOM   1739 C  CA    . ASN A 1 224 ? 24.340 -23.159 14.451  1.00 0.00 ? 223 ASN A CA    1 
ATOM   1740 C  C     . ASN A 1 224 ? 25.824 -23.123 14.640  1.00 0.00 ? 223 ASN A C     1 
ATOM   1741 O  O     . ASN A 1 224 ? 26.524 -24.117 14.401  1.00 0.00 ? 223 ASN A O     1 
ATOM   1742 C  CB    . ASN A 1 224 ? 24.169 -22.503 13.139  1.00 0.00 ? 223 ASN A CB    1 
ATOM   1743 C  CG    . ASN A 1 224 ? 24.896 -23.391 12.128  1.00 0.00 ? 223 ASN A CG    1 
ATOM   1744 O  OD1   . ASN A 1 224 ? 25.374 -22.901 11.107  1.00 0.00 ? 223 ASN A OD1   1 
ATOM   1745 N  ND2   . ASN A 1 224 ? 25.011 -24.687 12.354  1.00 0.00 ? 223 ASN A ND2   1 
ATOM   1746 N  N     . LEU A 1 225 ? 26.349 -22.012 15.071  1.00 0.00 ? 224 LEU A N     1 
ATOM   1747 C  CA    . LEU A 1 225 ? 27.771 -22.022 15.247  1.00 0.00 ? 224 LEU A CA    1 
ATOM   1748 C  C     . LEU A 1 225 ? 28.017 -23.249 16.055  1.00 0.00 ? 224 LEU A C     1 
ATOM   1749 O  O     . LEU A 1 225 ? 29.060 -23.904 15.919  1.00 0.00 ? 224 LEU A O     1 
ATOM   1750 C  CB    . LEU A 1 225 ? 28.377 -20.827 15.943  1.00 0.00 ? 224 LEU A CB    1 
ATOM   1751 C  CG    . LEU A 1 225 ? 29.886 -21.051 16.102  1.00 0.00 ? 224 LEU A CG    1 
ATOM   1752 C  CD1   . LEU A 1 225 ? 30.530 -20.114 17.126  1.00 0.00 ? 224 LEU A CD1   1 
ATOM   1753 C  CD2   . LEU A 1 225 ? 30.232 -22.469 16.563  1.00 0.00 ? 224 LEU A CD2   1 
ATOM   1754 N  N     . LEU A 1 226 ? 27.033 -23.514 16.878  1.00 0.00 ? 225 LEU A N     1 
ATOM   1755 C  CA    . LEU A 1 226 ? 27.095 -24.627 17.806  1.00 0.00 ? 225 LEU A CA    1 
ATOM   1756 C  C     . LEU A 1 226 ? 27.503 -25.969 17.140  1.00 0.00 ? 225 LEU A C     1 
ATOM   1757 O  O     . LEU A 1 226 ? 28.324 -26.725 17.678  1.00 0.00 ? 225 LEU A O     1 
ATOM   1758 C  CB    . LEU A 1 226 ? 25.807 -24.808 18.564  1.00 0.00 ? 225 LEU A CB    1 
ATOM   1759 C  CG    . LEU A 1 226 ? 26.116 -25.023 20.040  1.00 0.00 ? 225 LEU A CG    1 
ATOM   1760 C  CD1   . LEU A 1 226 ? 25.296 -26.152 20.666  1.00 0.00 ? 225 LEU A CD1   1 
ATOM   1761 C  CD2   . LEU A 1 226 ? 27.582 -25.384 20.291  1.00 0.00 ? 225 LEU A CD2   1 
ATOM   1762 N  N     . ASP A 1 227 ? 27.002 -26.377 15.981  1.00 0.00 ? 226 ASP A N     1 
ATOM   1763 C  CA    . ASP A 1 227 ? 27.526 -27.657 15.381  1.00 0.00 ? 226 ASP A CA    1 
ATOM   1764 C  C     . ASP A 1 227 ? 28.694 -27.374 14.394  1.00 0.00 ? 226 ASP A C     1 
ATOM   1765 O  O     . ASP A 1 227 ? 28.750 -26.311 13.758  1.00 0.00 ? 226 ASP A O     1 
ATOM   1766 C  CB    . ASP A 1 227 ? 26.443 -28.431 14.640  1.00 0.00 ? 226 ASP A CB    1 
ATOM   1767 C  CG    . ASP A 1 227 ? 26.761 -29.929 14.577  1.00 0.00 ? 226 ASP A CG    1 
ATOM   1768 O  OD1   . ASP A 1 227 ? 26.051 -30.709 13.835  1.00 0.00 ? 226 ASP A OD1   1 
ATOM   1769 O  OD2   . ASP A 1 227 ? 27.739 -30.409 15.267  1.00 0.00 ? 226 ASP A OD2   1 
ATOM   1770 N  N     . LYS A 1 228 ? 29.636 -28.341 14.268  1.00 0.00 ? 227 LYS A N     1 
ATOM   1771 C  CA    . LYS A 1 228 ? 30.812 -28.167 13.357  1.00 0.00 ? 227 LYS A CA    1 
ATOM   1772 C  C     . LYS A 1 228 ? 31.792 -29.349 13.332  1.00 0.00 ? 227 LYS A C     1 
ATOM   1773 O  O     . LYS A 1 228 ? 31.384 -30.519 13.274  1.00 0.00 ? 227 LYS A O     1 
ATOM   1774 C  CB    . LYS A 1 228 ? 31.632 -26.954 13.795  1.00 0.00 ? 227 LYS A CB    1 
ATOM   1775 C  CG    . LYS A 1 228 ? 30.840 -25.650 13.748  1.00 0.00 ? 227 LYS A CG    1 
ATOM   1776 C  CD    . LYS A 1 228 ? 31.175 -24.798 12.524  1.00 0.00 ? 227 LYS A CD    1 
ATOM   1777 C  CE    . LYS A 1 228 ? 30.039 -23.859 12.120  1.00 0.00 ? 227 LYS A CE    1 
ATOM   1778 N  NZ    . LYS A 1 228 ? 30.484 -22.473 11.918  1.00 0.00 ? 227 LYS A NZ    1 
ATOM   1779 N  N     . VAL A 1 229 ? 33.063 -28.974 13.371  1.00 0.00 ? 228 VAL A N     1 
ATOM   1780 C  CA    . VAL A 1 229 ? 34.188 -29.919 13.335  1.00 0.00 ? 228 VAL A CA    1 
ATOM   1781 C  C     . VAL A 1 229 ? 35.005 -29.801 14.627  1.00 0.00 ? 228 VAL A C     1 
ATOM   1782 O  O     . VAL A 1 229 ? 34.710 -30.463 15.632  1.00 0.00 ? 228 VAL A O     1 
ATOM   1783 C  CB    . VAL A 1 229 ? 35.066 -29.625 12.112  1.00 0.00 ? 228 VAL A CB    1 
ATOM   1784 C  CG1   . VAL A 1 229 ? 35.603 -28.193 12.089  1.00 0.00 ? 228 VAL A CG1   1 
ATOM   1785 C  CG2   . VAL A 1 229 ? 36.297 -30.530 12.027  1.00 0.00 ? 228 VAL A CG2   1 
ATOM   1786 N  N     . ASP A 1 230 ? 36.011 -28.959 14.576  1.00 0.00 ? 229 ASP A N     1 
ATOM   1787 C  CA    . ASP A 1 230 ? 36.900 -28.738 15.723  1.00 0.00 ? 229 ASP A CA    1 
ATOM   1788 C  C     . ASP A 1 230 ? 36.178 -28.030 16.786  1.00 0.00 ? 229 ASP A C     1 
ATOM   1789 O  O     . ASP A 1 230 ? 35.749 -26.880 16.607  1.00 0.00 ? 229 ASP A O     1 
ATOM   1790 C  CB    . ASP A 1 230 ? 38.050 -27.820 15.327  1.00 0.00 ? 229 ASP A CB    1 
ATOM   1791 C  CG    . ASP A 1 230 ? 39.183 -28.557 14.610  1.00 0.00 ? 229 ASP A CG    1 
ATOM   1792 O  OD1   . ASP A 1 230 ? 39.023 -29.783 14.241  1.00 0.00 ? 229 ASP A OD1   1 
ATOM   1793 O  OD2   . ASP A 1 230 ? 40.298 -27.953 14.374  1.00 0.00 ? 229 ASP A OD2   1 
ATOM   1794 N  N     . SER A 1 231 ? 36.142 -28.796 17.787  1.00 0.00 ? 230 SER A N     1 
ATOM   1795 C  CA    . SER A 1 231 ? 35.473 -28.524 19.007  1.00 0.00 ? 230 SER A CA    1 
ATOM   1796 C  C     . SER A 1 231 ? 36.089 -27.369 19.798  1.00 0.00 ? 230 SER A C     1 
ATOM   1797 O  O     . SER A 1 231 ? 36.143 -27.402 21.036  1.00 0.00 ? 230 SER A O     1 
ATOM   1798 C  CB    . SER A 1 231 ? 35.608 -29.760 19.887  1.00 0.00 ? 230 SER A CB    1 
ATOM   1799 O  OG    . SER A 1 231 ? 36.828 -30.427 19.596  1.00 0.00 ? 230 SER A OG    1 
ATOM   1800 N  N     . ILE A 1 232 ? 36.579 -26.320 19.155  1.00 0.00 ? 231 ILE A N     1 
ATOM   1801 C  CA    . ILE A 1 232 ? 37.126 -25.174 19.935  1.00 0.00 ? 231 ILE A CA    1 
ATOM   1802 C  C     . ILE A 1 232 ? 36.378 -23.888 19.638  1.00 0.00 ? 231 ILE A C     1 
ATOM   1803 O  O     . ILE A 1 232 ? 36.477 -23.330 18.536  1.00 0.00 ? 231 ILE A O     1 
ATOM   1804 C  CB    . ILE A 1 232 ? 38.576 -24.873 19.594  1.00 0.00 ? 231 ILE A CB    1 
ATOM   1805 C  CG1   . ILE A 1 232 ? 39.373 -26.110 19.199  1.00 0.00 ? 231 ILE A CG1   1 
ATOM   1806 C  CG2   . ILE A 1 232 ? 39.340 -24.237 20.758  1.00 0.00 ? 231 ILE A CG2   1 
ATOM   1807 C  CD1   . ILE A 1 232 ? 40.415 -25.826 18.116  1.00 0.00 ? 231 ILE A CD1   1 
ATOM   1808 N  N     . ILE A 1 233 ? 35.650 -23.467 20.633  1.00 0.00 ? 232 ILE A N     1 
ATOM   1809 C  CA    . ILE A 1 233 ? 34.832 -22.248 20.564  1.00 0.00 ? 232 ILE A CA    1 
ATOM   1810 C  C     . ILE A 1 233 ? 35.142 -21.282 21.676  1.00 0.00 ? 232 ILE A C     1 
ATOM   1811 O  O     . ILE A 1 233 ? 35.062 -21.626 22.865  1.00 0.00 ? 232 ILE A O     1 
ATOM   1812 C  CB    . ILE A 1 233 ? 33.342 -22.538 20.649  1.00 0.00 ? 232 ILE A CB    1 
ATOM   1813 C  CG1   . ILE A 1 233 ? 32.590 -21.534 21.524  1.00 0.00 ? 232 ILE A CG1   1 
ATOM   1814 C  CG2   . ILE A 1 233 ? 33.032 -23.916 21.235  1.00 0.00 ? 232 ILE A CG2   1 
ATOM   1815 C  CD1   . ILE A 1 233 ? 31.912 -20.425 20.716  1.00 0.00 ? 232 ILE A CD1   1 
ATOM   1816 N  N     . ILE A 1 234 ? 35.495 -20.085 21.352  1.00 0.00 ? 233 ILE A N     1 
ATOM   1817 C  CA    . ILE A 1 234 ? 35.716 -19.147 22.426  1.00 0.00 ? 233 ILE A CA    1 
ATOM   1818 C  C     . ILE A 1 234 ? 34.612 -18.094 22.376  1.00 0.00 ? 233 ILE A C     1 
ATOM   1819 O  O     . ILE A 1 234 ? 34.599 -17.222 21.493  1.00 0.00 ? 233 ILE A O     1 
ATOM   1820 C  CB    . ILE A 1 234 ? 37.124 -18.619 22.302  1.00 0.00 ? 233 ILE A CB    1 
ATOM   1821 C  CG1   . ILE A 1 234 ? 38.102 -19.756 21.998  1.00 0.00 ? 233 ILE A CG1   1 
ATOM   1822 C  CG2   . ILE A 1 234 ? 37.611 -17.917 23.571  1.00 0.00 ? 233 ILE A CG2   1 
ATOM   1823 C  CD1   . ILE A 1 234 ? 39.567 -19.348 22.161  1.00 0.00 ? 233 ILE A CD1   1 
ATOM   1824 N  N     . GLY A 1 235 ? 33.814 -18.374 23.405  1.00 0.00 ? 234 GLY A N     1 
ATOM   1825 C  CA    . GLY A 1 235 ? 32.561 -17.725 23.812  1.00 0.00 ? 234 GLY A CA    1 
ATOM   1826 C  C     . GLY A 1 235 ? 32.654 -17.239 25.264  1.00 0.00 ? 234 GLY A C     1 
ATOM   1827 O  O     . GLY A 1 235 ? 32.915 -18.027 26.186  1.00 0.00 ? 234 GLY A O     1 
ATOM   1828 N  N     . GLY A 1 236 ? 32.452 -15.961 25.477  1.00 0.00 ? 235 GLY A N     1 
ATOM   1829 C  CA    . GLY A 1 236 ? 32.505 -15.409 26.841  1.00 0.00 ? 235 GLY A CA    1 
ATOM   1830 C  C     . GLY A 1 236 ? 31.103 -14.940 27.275  1.00 0.00 ? 235 GLY A C     1 
ATOM   1831 O  O     . GLY A 1 236 ? 30.556 -13.971 26.727  1.00 0.00 ? 235 GLY A O     1 
ATOM   1832 N  N     . GLY A 1 237 ? 30.595 -15.685 28.267  1.00 0.00 ? 236 GLY A N     1 
ATOM   1833 C  CA    . GLY A 1 237 ? 29.261 -15.475 28.881  1.00 0.00 ? 236 GLY A CA    1 
ATOM   1834 C  C     . GLY A 1 237 ? 29.355 -15.595 30.418  1.00 0.00 ? 236 GLY A C     1 
ATOM   1835 O  O     . GLY A 1 237 ? 30.214 -16.312 30.952  1.00 0.00 ? 236 GLY A O     1 
ATOM   1836 N  N     . MET A 1 238 ? 28.444 -14.883 31.075  1.00 0.00 ? 237 MET A N     1 
ATOM   1837 C  CA    . MET A 1 238 ? 28.375 -14.782 32.555  1.00 0.00 ? 237 MET A CA    1 
ATOM   1838 C  C     . MET A 1 238 ? 27.801 -16.074 33.224  1.00 0.00 ? 237 MET A C     1 
ATOM   1839 O  O     . MET A 1 238 ? 28.391 -16.622 34.166  1.00 0.00 ? 237 MET A O     1 
ATOM   1840 C  CB    . MET A 1 238 ? 27.472 -13.614 32.958  1.00 0.00 ? 237 MET A CB    1 
ATOM   1841 C  CG    . MET A 1 238 ? 27.820 -12.313 32.233  1.00 0.00 ? 237 MET A CG    1 
ATOM   1842 S  SD    . MET A 1 238 ? 29.021 -11.330 33.105  1.00 0.00 ? 237 MET A SD    1 
ATOM   1843 C  CE    . MET A 1 238 ? 29.977 -12.364 34.194  1.00 0.00 ? 237 MET A CE    1 
ATOM   1844 N  N     . ALA A 1 239 ? 26.658 -16.548 32.738  1.00 0.00 ? 238 ALA A N     1 
ATOM   1845 C  CA    . ALA A 1 239 ? 26.011 -17.791 33.235  1.00 0.00 ? 238 ALA A CA    1 
ATOM   1846 C  C     . ALA A 1 239 ? 26.922 -19.001 33.018  1.00 0.00 ? 238 ALA A C     1 
ATOM   1847 O  O     . ALA A 1 239 ? 27.114 -19.828 33.924  1.00 0.00 ? 238 ALA A O     1 
ATOM   1848 C  CB    . ALA A 1 239 ? 24.699 -18.040 32.490  1.00 0.00 ? 238 ALA A CB    1 
ATOM   1849 N  N     . PHE A 1 240 ? 27.476 -19.052 31.798  1.00 0.00 ? 239 PHE A N     1 
ATOM   1850 C  CA    . PHE A 1 240 ? 28.316 -20.176 31.398  1.00 0.00 ? 239 PHE A CA    1 
ATOM   1851 C  C     . PHE A 1 240 ? 29.264 -20.362 32.535  1.00 0.00 ? 239 PHE A C     1 
ATOM   1852 O  O     . PHE A 1 240 ? 29.497 -21.490 32.995  1.00 0.00 ? 239 PHE A O     1 
ATOM   1853 C  CB    . PHE A 1 240 ? 29.279 -19.830 30.218  1.00 0.00 ? 239 PHE A CB    1 
ATOM   1854 C  CG    . PHE A 1 240 ? 28.692 -19.340 28.874  1.00 0.00 ? 239 PHE A CG    1 
ATOM   1855 C  CD1   . PHE A 1 240 ? 28.332 -20.264 27.880  1.00 0.00 ? 239 PHE A CD1   1 
ATOM   1856 C  CD2   . PHE A 1 240 ? 28.563 -17.966 28.613  1.00 0.00 ? 239 PHE A CD2   1 
ATOM   1857 C  CE1   . PHE A 1 240 ? 27.850 -19.818 26.639  1.00 0.00 ? 239 PHE A CE1   1 
ATOM   1858 C  CE2   . PHE A 1 240 ? 28.083 -17.522 27.370  1.00 0.00 ? 239 PHE A CE2   1 
ATOM   1859 C  CZ    . PHE A 1 240 ? 27.728 -18.447 26.384  1.00 0.00 ? 239 PHE A CZ    1 
ATOM   1860 N  N     . THR A 1 241 ? 29.752 -19.207 32.905  1.00 0.00 ? 240 THR A N     1 
ATOM   1861 C  CA    . THR A 1 241 ? 30.606 -19.071 34.043  1.00 0.00 ? 240 THR A CA    1 
ATOM   1862 C  C     . THR A 1 241 ? 29.822 -19.689 35.165  1.00 0.00 ? 240 THR A C     1 
ATOM   1863 O  O     . THR A 1 241 ? 30.360 -20.465 35.969  1.00 0.00 ? 240 THR A O     1 
ATOM   1864 C  CB    . THR A 1 241 ? 30.861 -17.588 34.320  1.00 0.00 ? 240 THR A CB    1 
ATOM   1865 O  OG1   . THR A 1 241 ? 32.004 -17.148 33.602  1.00 0.00 ? 240 THR A OG1   1 
ATOM   1866 C  CG2   . THR A 1 241 ? 31.109 -17.290 35.801  1.00 0.00 ? 240 THR A CG2   1 
ATOM   1867 N  N     . PHE A 1 242 ? 28.554 -19.299 35.163  1.00 0.00 ? 241 PHE A N     1 
ATOM   1868 C  CA    . PHE A 1 242 ? 27.592 -19.794 36.140  1.00 0.00 ? 241 PHE A CA    1 
ATOM   1869 C  C     . PHE A 1 242 ? 27.497 -21.307 36.058  1.00 0.00 ? 241 PHE A C     1 
ATOM   1870 O  O     . PHE A 1 242 ? 27.686 -22.014 37.059  1.00 0.00 ? 241 PHE A O     1 
ATOM   1871 C  CB    . PHE A 1 242 ? 26.157 -19.361 35.775  1.00 0.00 ? 241 PHE A CB    1 
ATOM   1872 C  CG    . PHE A 1 242 ? 25.889 -17.852 35.680  1.00 0.00 ? 241 PHE A CG    1 
ATOM   1873 C  CD1   . PHE A 1 242 ? 24.571 -17.406 35.511  1.00 0.00 ? 241 PHE A CD1   1 
ATOM   1874 C  CD2   . PHE A 1 242 ? 26.931 -16.921 35.757  1.00 0.00 ? 241 PHE A CD2   1 
ATOM   1875 C  CE1   . PHE A 1 242 ? 24.293 -16.039 35.434  1.00 0.00 ? 241 PHE A CE1   1 
ATOM   1876 C  CE2   . PHE A 1 242 ? 26.653 -15.550 35.679  1.00 0.00 ? 241 PHE A CE2   1 
ATOM   1877 C  CZ    . PHE A 1 242 ? 25.333 -15.110 35.521  1.00 0.00 ? 241 PHE A CZ    1 
ATOM   1878 N  N     . LYS A 1 243 ? 27.214 -21.710 34.839  1.00 0.00 ? 242 LYS A N     1 
ATOM   1879 C  CA    . LYS A 1 243 ? 27.027 -23.103 34.474  1.00 0.00 ? 242 LYS A CA    1 
ATOM   1880 C  C     . LYS A 1 243 ? 28.275 -23.889 34.782  1.00 0.00 ? 242 LYS A C     1 
ATOM   1881 O  O     . LYS A 1 243 ? 28.216 -24.974 35.380  1.00 0.00 ? 242 LYS A O     1 
ATOM   1882 C  CB    . LYS A 1 243 ? 26.744 -23.232 32.974  1.00 0.00 ? 242 LYS A CB    1 
ATOM   1883 C  CG    . LYS A 1 243 ? 25.350 -22.740 32.579  1.00 0.00 ? 242 LYS A CG    1 
ATOM   1884 C  CD    . LYS A 1 243 ? 24.228 -23.642 33.094  1.00 0.00 ? 242 LYS A CD    1 
ATOM   1885 C  CE    . LYS A 1 243 ? 22.907 -22.895 33.288  1.00 0.00 ? 242 LYS A CE    1 
ATOM   1886 N  NZ    . LYS A 1 243 ? 21.918 -23.666 34.056  1.00 0.00 ? 242 LYS A NZ    1 
ATOM   1887 N  N     . LYS A 1 244 ? 29.382 -23.322 34.366  1.00 0.00 ? 243 LYS A N     1 
ATOM   1888 C  CA    . LYS A 1 244 ? 30.665 -24.005 34.483  1.00 0.00 ? 243 LYS A CA    1 
ATOM   1889 C  C     . LYS A 1 244 ? 30.954 -24.402 35.919  1.00 0.00 ? 243 LYS A C     1 
ATOM   1890 O  O     . LYS A 1 244 ? 31.255 -25.569 36.210  1.00 0.00 ? 243 LYS A O     1 
ATOM   1891 C  CB    . LYS A 1 244 ? 31.810 -23.090 34.036  1.00 0.00 ? 243 LYS A CB    1 
ATOM   1892 C  CG    . LYS A 1 244 ? 33.145 -23.438 34.708  1.00 0.00 ? 243 LYS A CG    1 
ATOM   1893 C  CD    . LYS A 1 244 ? 34.324 -22.629 34.160  1.00 0.00 ? 243 LYS A CD    1 
ATOM   1894 C  CE    . LYS A 1 244 ? 35.677 -23.304 34.399  1.00 0.00 ? 243 LYS A CE    1 
ATOM   1895 N  NZ    . LYS A 1 244 ? 36.800 -22.569 33.798  1.00 0.00 ? 243 LYS A NZ    1 
ATOM   1896 N  N     . VAL A 1 245 ? 30.847 -23.429 36.792  1.00 0.00 ? 244 VAL A N     1 
ATOM   1897 C  CA    . VAL A 1 245 ? 31.125 -23.623 38.219  1.00 0.00 ? 244 VAL A CA    1 
ATOM   1898 C  C     . VAL A 1 245 ? 29.884 -23.212 39.023  1.00 0.00 ? 244 VAL A C     1 
ATOM   1899 O  O     . VAL A 1 245 ? 28.873 -23.930 39.048  1.00 0.00 ? 244 VAL A O     1 
ATOM   1900 C  CB    . VAL A 1 245 ? 32.380 -22.842 38.622  1.00 0.00 ? 244 VAL A CB    1 
ATOM   1901 C  CG1   . VAL A 1 245 ? 33.574 -23.113 37.704  1.00 0.00 ? 244 VAL A CG1   1 
ATOM   1902 C  CG2   . VAL A 1 245 ? 32.175 -21.326 38.598  1.00 0.00 ? 244 VAL A CG2   1 
ATOM   1903 N  N     . LEU A 1 246 ? 29.922 -22.065 39.692  1.00 0.00 ? 245 LEU A N     1 
ATOM   1904 C  CA    . LEU A 1 246 ? 28.735 -21.649 40.471  1.00 0.00 ? 245 LEU A CA    1 
ATOM   1905 C  C     . LEU A 1 246 ? 28.925 -20.342 41.257  1.00 0.00 ? 245 LEU A C     1 
ATOM   1906 O  O     . LEU A 1 246 ? 28.174 -19.373 41.076  1.00 0.00 ? 245 LEU A O     1 
ATOM   1907 C  CB    . LEU A 1 246 ? 28.379 -22.736 41.483  1.00 0.00 ? 245 LEU A CB    1 
ATOM   1908 C  CG    . LEU A 1 246 ? 27.224 -22.339 42.401  1.00 0.00 ? 245 LEU A CG    1 
ATOM   1909 C  CD1   . LEU A 1 246 ? 25.861 -22.403 41.709  1.00 0.00 ? 245 LEU A CD1   1 
ATOM   1910 C  CD2   . LEU A 1 246 ? 27.105 -23.237 43.635  1.00 0.00 ? 245 LEU A CD2   1 
ATOM   1911 N  N     . GLU A 1 247 ? 29.922 -20.341 42.111  1.00 0.00 ? 246 GLU A N     1 
ATOM   1912 C  CA    . GLU A 1 247 ? 30.208 -19.205 43.001  1.00 0.00 ? 246 GLU A CA    1 
ATOM   1913 C  C     . GLU A 1 247 ? 30.392 -17.900 42.222  1.00 0.00 ? 246 GLU A C     1 
ATOM   1914 O  O     . GLU A 1 247 ? 29.885 -16.841 42.621  1.00 0.00 ? 246 GLU A O     1 
ATOM   1915 C  CB    . GLU A 1 247 ? 31.459 -19.469 43.839  1.00 0.00 ? 246 GLU A CB    1 
ATOM   1916 C  CG    . GLU A 1 247 ? 32.659 -19.924 43.015  1.00 0.00 ? 246 GLU A CG    1 
ATOM   1917 C  CD    . GLU A 1 247 ? 33.977 -19.802 43.780  1.00 0.00 ? 246 GLU A CD    1 
ATOM   1918 O  OE1   . GLU A 1 247 ? 34.471 -18.637 44.032  1.00 0.00 ? 246 GLU A OE1   1 
ATOM   1919 O  OE2   . GLU A 1 247 ? 34.595 -20.863 44.175  1.00 0.00 ? 246 GLU A OE2   1 
ATOM   1920 N  N     . ASN A 1 248 ? 31.112 -17.974 41.124  1.00 0.00 ? 247 ASN A N     1 
ATOM   1921 C  CA    . ASN A 1 248 ? 31.421 -16.771 40.345  1.00 0.00 ? 247 ASN A CA    1 
ATOM   1922 C  C     . ASN A 1 248 ? 30.112 -16.040 40.078  1.00 0.00 ? 247 ASN A C     1 
ATOM   1923 O  O     . ASN A 1 248 ? 29.997 -14.829 40.318  1.00 0.00 ? 247 ASN A O     1 
ATOM   1924 C  CB    . ASN A 1 248 ? 32.082 -17.200 39.023  1.00 0.00 ? 247 ASN A CB    1 
ATOM   1925 C  CG    . ASN A 1 248 ? 32.358 -16.045 38.054  1.00 0.00 ? 247 ASN A CG    1 
ATOM   1926 O  OD1   . ASN A 1 248 ? 31.886 -14.931 38.274  1.00 0.00 ? 247 ASN A OD1   1 
ATOM   1927 N  ND2   . ASN A 1 248 ? 33.103 -16.247 36.983  1.00 0.00 ? 247 ASN A ND2   1 
ATOM   1928 N  N     . THR A 1 249 ? 29.174 -16.805 39.590  1.00 0.00 ? 248 THR A N     1 
ATOM   1929 C  CA    . THR A 1 249 ? 27.816 -16.332 39.355  1.00 0.00 ? 248 THR A CA    1 
ATOM   1930 C  C     . THR A 1 249 ? 27.123 -15.927 40.653  1.00 0.00 ? 248 THR A C     1 
ATOM   1931 O  O     . THR A 1 249 ? 26.505 -14.855 40.741  1.00 0.00 ? 248 THR A O     1 
ATOM   1932 C  CB    . THR A 1 249 ? 26.947 -17.415 38.714  1.00 0.00 ? 248 THR A CB    1 
ATOM   1933 O  OG1   . THR A 1 249 ? 25.596 -16.980 38.654  1.00 0.00 ? 248 THR A OG1   1 
ATOM   1934 C  CG2   . THR A 1 249 ? 26.968 -18.734 39.488  1.00 0.00 ? 248 THR A CG2   1 
ATOM   1935 N  N     . GLU A 1 250 ? 27.231 -16.790 41.654  1.00 0.00 ? 249 GLU A N     1 
ATOM   1936 C  CA    . GLU A 1 250 ? 26.429 -16.603 42.869  1.00 0.00 ? 249 GLU A CA    1 
ATOM   1937 C  C     . GLU A 1 250 ? 26.669 -15.222 43.535  1.00 0.00 ? 249 GLU A C     1 
ATOM   1938 O  O     . GLU A 1 250 ? 25.737 -14.420 43.695  1.00 0.00 ? 249 GLU A O     1 
ATOM   1939 C  CB    . GLU A 1 250 ? 26.708 -17.763 43.846  1.00 0.00 ? 249 GLU A CB    1 
ATOM   1940 C  CG    . GLU A 1 250 ? 25.585 -18.826 43.829  1.00 0.00 ? 249 GLU A CG    1 
ATOM   1941 C  CD    . GLU A 1 250 ? 26.069 -20.270 44.048  1.00 0.00 ? 249 GLU A CD    1 
ATOM   1942 O  OE1   . GLU A 1 250 ? 26.083 -20.773 45.236  1.00 0.00 ? 249 GLU A OE1   1 
ATOM   1943 O  OE2   . GLU A 1 250 ? 26.460 -20.981 43.044  1.00 0.00 ? 249 GLU A OE2   1 
ATOM   1944 N  N     . ILE A 1 251 ? 27.890 -14.885 43.945  1.00 0.00 ? 250 ILE A N     1 
ATOM   1945 C  CA    . ILE A 1 251 ? 28.171 -13.507 44.445  1.00 0.00 ? 250 ILE A CA    1 
ATOM   1946 C  C     . ILE A 1 251 ? 28.121 -12.507 43.259  1.00 0.00 ? 250 ILE A C     1 
ATOM   1947 O  O     . ILE A 1 251 ? 27.520 -11.428 43.355  1.00 0.00 ? 250 ILE A O     1 
ATOM   1948 C  CB    . ILE A 1 251 ? 29.408 -13.472 45.333  1.00 0.00 ? 250 ILE A CB    1 
ATOM   1949 C  CG1   . ILE A 1 251 ? 30.451 -12.460 44.892  1.00 0.00 ? 250 ILE A CG1   1 
ATOM   1950 C  CG2   . ILE A 1 251 ? 30.148 -14.809 45.382  1.00 0.00 ? 250 ILE A CG2   1 
ATOM   1951 C  CD1   . ILE A 1 251 ? 31.863 -12.825 45.354  1.00 0.00 ? 250 ILE A CD1   1 
ATOM   1952 N  N     . GLY A 1 252 ? 28.763 -12.868 42.148  1.00 0.00 ? 251 GLY A N     1 
ATOM   1953 C  CA    . GLY A 1 252 ? 28.712 -12.029 40.939  1.00 0.00 ? 251 GLY A CA    1 
ATOM   1954 C  C     . GLY A 1 252 ? 27.312 -11.400 40.875  1.00 0.00 ? 251 GLY A C     1 
ATOM   1955 O  O     . GLY A 1 252 ? 27.161 -10.170 40.927  1.00 0.00 ? 251 GLY A O     1 
ATOM   1956 N  N     . ASP A 1 253 ? 26.331 -12.293 40.760  1.00 0.00 ? 252 ASP A N     1 
ATOM   1957 C  CA    . ASP A 1 253 ? 24.894 -11.940 40.767  1.00 0.00 ? 252 ASP A CA    1 
ATOM   1958 C  C     . ASP A 1 253 ? 24.012 -13.180 40.656  1.00 0.00 ? 252 ASP A C     1 
ATOM   1959 O  O     . ASP A 1 253 ? 24.049 -14.070 41.518  1.00 0.00 ? 252 ASP A O     1 
ATOM   1960 C  CB    . ASP A 1 253 ? 24.503 -11.008 39.631  1.00 0.00 ? 252 ASP A CB    1 
ATOM   1961 C  CG    . ASP A 1 253 ? 23.070 -10.488 39.800  1.00 0.00 ? 252 ASP A CG    1 
ATOM   1962 O  OD1   . ASP A 1 253 ? 22.855 -9.376  40.419  1.00 0.00 ? 252 ASP A OD1   1 
ATOM   1963 O  OD2   . ASP A 1 253 ? 22.078 -11.162 39.324  1.00 0.00 ? 252 ASP A OD2   1 
ATOM   1964 N  N     . SER A 1 254 ? 23.225 -13.225 39.579  1.00 0.00 ? 253 SER A N     1 
ATOM   1965 C  CA    . SER A 1 254 ? 22.263 -14.327 39.414  1.00 0.00 ? 253 SER A CA    1 
ATOM   1966 C  C     . SER A 1 254 ? 21.878 -14.664 37.961  1.00 0.00 ? 253 SER A C     1 
ATOM   1967 O  O     . SER A 1 254 ? 21.965 -15.823 37.529  1.00 0.00 ? 253 SER A O     1 
ATOM   1968 C  CB    . SER A 1 254 ? 20.953 -13.983 40.124  1.00 0.00 ? 253 SER A CB    1 
ATOM   1969 O  OG    . SER A 1 254 ? 20.352 -12.852 39.511  1.00 0.00 ? 253 SER A OG    1 
ATOM   1970 N  N     . ILE A 1 255 ? 21.459 -13.677 37.186  1.00 0.00 ? 254 ILE A N     1 
ATOM   1971 C  CA    . ILE A 1 255 ? 20.909 -13.968 35.839  1.00 0.00 ? 254 ILE A CA    1 
ATOM   1972 C  C     . ILE A 1 255 ? 21.674 -13.328 34.665  1.00 0.00 ? 254 ILE A C     1 
ATOM   1973 O  O     . ILE A 1 255 ? 22.157 -12.190 34.761  1.00 0.00 ? 254 ILE A O     1 
ATOM   1974 C  CB    . ILE A 1 255 ? 19.466 -13.465 35.764  1.00 0.00 ? 254 ILE A CB    1 
ATOM   1975 C  CG1   . ILE A 1 255 ? 18.720 -13.967 34.527  1.00 0.00 ? 254 ILE A CG1   1 
ATOM   1976 C  CG2   . ILE A 1 255 ? 19.365 -11.939 35.716  1.00 0.00 ? 254 ILE A CG2   1 
ATOM   1977 C  CD1   . ILE A 1 255 ? 18.993 -15.441 34.222  1.00 0.00 ? 254 ILE A CD1   1 
ATOM   1978 N  N     . PHE A 1 256 ? 21.732 -14.142 33.604  1.00 0.00 ? 255 PHE A N     1 
ATOM   1979 C  CA    . PHE A 1 256 ? 22.306 -13.784 32.292  1.00 0.00 ? 255 PHE A CA    1 
ATOM   1980 C  C     . PHE A 1 256 ? 21.134 -13.594 31.318  1.00 0.00 ? 255 PHE A C     1 
ATOM   1981 O  O     . PHE A 1 256 ? 20.320 -12.671 31.471  1.00 0.00 ? 255 PHE A O     1 
ATOM   1982 C  CB    . PHE A 1 256 ? 23.209 -14.889 31.744  1.00 0.00 ? 255 PHE A CB    1 
ATOM   1983 C  CG    . PHE A 1 256 ? 23.629 -14.625 30.293  1.00 0.00 ? 255 PHE A CG    1 
ATOM   1984 C  CD1   . PHE A 1 256 ? 24.375 -13.482 29.978  1.00 0.00 ? 255 PHE A CD1   1 
ATOM   1985 C  CD2   . PHE A 1 256 ? 23.266 -15.521 29.279  1.00 0.00 ? 255 PHE A CD2   1 
ATOM   1986 C  CE1   . PHE A 1 256 ? 24.757 -13.236 28.653  1.00 0.00 ? 255 PHE A CE1   1 
ATOM   1987 C  CE2   . PHE A 1 256 ? 23.647 -15.274 27.954  1.00 0.00 ? 255 PHE A CE2   1 
ATOM   1988 C  CZ    . PHE A 1 256 ? 24.393 -14.132 27.641  1.00 0.00 ? 255 PHE A CZ    1 
ATOM   1989 N  N     . ASP A 1 257 ? 21.070 -14.459 30.319  1.00 0.00 ? 256 ASP A N     1 
ATOM   1990 C  CA    . ASP A 1 257 ? 19.910 -14.504 29.418  1.00 0.00 ? 256 ASP A CA    1 
ATOM   1991 C  C     . ASP A 1 257 ? 19.065 -15.675 29.915  1.00 0.00 ? 256 ASP A C     1 
ATOM   1992 O  O     . ASP A 1 257 ? 19.480 -16.841 29.832  1.00 0.00 ? 256 ASP A O     1 
ATOM   1993 C  CB    . ASP A 1 257 ? 20.322 -14.644 27.963  1.00 0.00 ? 256 ASP A CB    1 
ATOM   1994 C  CG    . ASP A 1 257 ? 19.273 -14.029 27.035  1.00 0.00 ? 256 ASP A CG    1 
ATOM   1995 O  OD1   . ASP A 1 257 ? 19.612 -13.613 25.862  1.00 0.00 ? 256 ASP A OD1   1 
ATOM   1996 O  OD2   . ASP A 1 257 ? 18.048 -13.926 27.427  1.00 0.00 ? 256 ASP A OD2   1 
ATOM   1997 N  N     . LYS A 1 258 ? 17.893 -15.319 30.414  1.00 0.00 ? 257 LYS A N     1 
ATOM   1998 C  CA    . LYS A 1 258 ? 17.022 -16.253 31.149  1.00 0.00 ? 257 LYS A CA    1 
ATOM   1999 C  C     . LYS A 1 258 ? 16.772 -17.534 30.339  1.00 0.00 ? 257 LYS A C     1 
ATOM   2000 O  O     . LYS A 1 258 ? 16.959 -18.652 30.842  1.00 0.00 ? 257 LYS A O     1 
ATOM   2001 C  CB    . LYS A 1 258 ? 15.699 -15.540 31.480  1.00 0.00 ? 257 LYS A CB    1 
ATOM   2002 C  CG    . LYS A 1 258 ? 15.906 -14.238 32.276  1.00 0.00 ? 257 LYS A CG    1 
ATOM   2003 C  CD    . LYS A 1 258 ? 14.630 -13.396 32.416  1.00 0.00 ? 257 LYS A CD    1 
ATOM   2004 C  CE    . LYS A 1 258 ? 14.760 -12.274 33.453  1.00 0.00 ? 257 LYS A CE    1 
ATOM   2005 N  NZ    . LYS A 1 258 ? 13.551 -11.443 33.556  1.00 0.00 ? 257 LYS A NZ    1 
ATOM   2006 N  N     . ALA A 1 259 ? 16.352 -17.372 29.102  1.00 0.00 ? 258 ALA A N     1 
ATOM   2007 C  CA    . ALA A 1 259 ? 16.191 -18.507 28.171  1.00 0.00 ? 258 ALA A CA    1 
ATOM   2008 C  C     . ALA A 1 259 ? 17.554 -19.158 27.900  1.00 0.00 ? 258 ALA A C     1 
ATOM   2009 O  O     . ALA A 1 259 ? 17.705 -20.386 27.984  1.00 0.00 ? 258 ALA A O     1 
ATOM   2010 C  CB    . ALA A 1 259 ? 15.602 -18.019 26.846  1.00 0.00 ? 258 ALA A CB    1 
ATOM   2011 N  N     . VAL A 1 260 ? 18.481 -18.264 27.584  1.00 0.00 ? 259 VAL A N     1 
ATOM   2012 C  CA    . VAL A 1 260 ? 19.859 -18.606 27.234  1.00 0.00 ? 259 VAL A CA    1 
ATOM   2013 C  C     . VAL A 1 260 ? 20.455 -19.512 28.280  1.00 0.00 ? 259 VAL A C     1 
ATOM   2014 O  O     . VAL A 1 260 ? 21.349 -20.322 27.991  1.00 0.00 ? 259 VAL A O     1 
ATOM   2015 C  CB    . VAL A 1 260 ? 20.726 -17.343 27.150  1.00 0.00 ? 259 VAL A CB    1 
ATOM   2016 C  CG1   . VAL A 1 260 ? 21.322 -16.936 28.500  1.00 0.00 ? 259 VAL A CG1   1 
ATOM   2017 C  CG2   . VAL A 1 260 ? 21.918 -17.497 26.202  1.00 0.00 ? 259 VAL A CG2   1 
ATOM   2018 N  N     . GLY A 1 261 ? 19.974 -19.377 29.490  1.00 0.00 ? 260 GLY A N     1 
ATOM   2019 C  CA    . GLY A 1 261 ? 20.530 -20.184 30.563  1.00 0.00 ? 260 GLY A CA    1 
ATOM   2020 C  C     . GLY A 1 261 ? 20.358 -21.677 30.269  1.00 0.00 ? 260 GLY A C     1 
ATOM   2021 O  O     . GLY A 1 261 ? 21.336 -22.437 30.235  1.00 0.00 ? 260 GLY A O     1 
ATOM   2022 N  N     . PRO A 1 262 ? 19.137 -22.195 30.042  1.00 0.00 ? 261 PRO A N     1 
ATOM   2023 C  CA    . PRO A 1 262 ? 18.964 -23.604 29.729  1.00 0.00 ? 261 PRO A CA    1 
ATOM   2024 C  C     . PRO A 1 262 ? 19.636 -23.986 28.448  1.00 0.00 ? 261 PRO A C     1 
ATOM   2025 O  O     . PRO A 1 262 ? 20.423 -24.983 28.438  1.00 0.00 ? 261 PRO A O     1 
ATOM   2026 C  CB    . PRO A 1 262 ? 17.470 -23.778 29.614  1.00 0.00 ? 261 PRO A CB    1 
ATOM   2027 C  CG    . PRO A 1 262 ? 16.824 -22.422 29.860  1.00 0.00 ? 261 PRO A CG    1 
ATOM   2028 C  CD    . PRO A 1 262 ? 17.901 -21.413 30.119  1.00 0.00 ? 261 PRO A CD    1 
ATOM   2029 N  N     . GLU A 1 263 ? 19.321 -23.205 27.443  1.00 0.00 ? 262 GLU A N     1 
ATOM   2030 C  CA    . GLU A 1 263 ? 19.803 -23.435 26.086  1.00 0.00 ? 262 GLU A CA    1 
ATOM   2031 C  C     . GLU A 1 263 ? 21.332 -23.450 26.065  1.00 0.00 ? 262 GLU A C     1 
ATOM   2032 O  O     . GLU A 1 263 ? 21.953 -24.353 25.485  1.00 0.00 ? 262 GLU A O     1 
ATOM   2033 C  CB    . GLU A 1 263 ? 19.249 -22.343 25.163  1.00 0.00 ? 262 GLU A CB    1 
ATOM   2034 C  CG    . GLU A 1 263 ? 17.737 -22.133 25.343  1.00 0.00 ? 262 GLU A CG    1 
ATOM   2035 C  CD    . GLU A 1 263 ? 17.080 -21.373 24.186  1.00 0.00 ? 262 GLU A CD    1 
ATOM   2036 O  OE1   . GLU A 1 263 ? 17.728 -20.437 23.579  1.00 0.00 ? 262 GLU A OE1   1 
ATOM   2037 O  OE2   . GLU A 1 263 ? 15.879 -21.667 23.820  1.00 0.00 ? 262 GLU A OE2   1 
ATOM   2038 N  N     . ILE A 1 264 ? 21.908 -22.449 26.698  1.00 0.00 ? 263 ILE A N     1 
ATOM   2039 C  CA    . ILE A 1 264 ? 23.373 -22.286 26.760  1.00 0.00 ? 263 ILE A CA    1 
ATOM   2040 C  C     . ILE A 1 264 ? 24.055 -23.486 27.444  1.00 0.00 ? 263 ILE A C     1 
ATOM   2041 O  O     . ILE A 1 264 ? 25.012 -24.068 26.912  1.00 0.00 ? 263 ILE A O     1 
ATOM   2042 C  CB    . ILE A 1 264 ? 23.702 -20.971 27.469  1.00 0.00 ? 263 ILE A CB    1 
ATOM   2043 C  CG1   . ILE A 1 264 ? 24.764 -21.110 28.557  1.00 0.00 ? 263 ILE A CG1   1 
ATOM   2044 C  CG2   . ILE A 1 264 ? 22.488 -20.339 28.152  1.00 0.00 ? 263 ILE A CG2   1 
ATOM   2045 C  CD1   . ILE A 1 264 ? 25.518 -19.806 28.824  1.00 0.00 ? 263 ILE A CD1   1 
ATOM   2046 N  N     . ALA A 1 265 ? 23.575 -23.855 28.610  1.00 0.00 ? 264 ALA A N     1 
ATOM   2047 C  CA    . ALA A 1 265 ? 24.133 -25.010 29.302  1.00 0.00 ? 264 ALA A CA    1 
ATOM   2048 C  C     . ALA A 1 265 ? 23.989 -26.200 28.368  1.00 0.00 ? 264 ALA A C     1 
ATOM   2049 O  O     . ALA A 1 265 ? 24.937 -26.975 28.169  1.00 0.00 ? 264 ALA A O     1 
ATOM   2050 C  CB    . ALA A 1 265 ? 23.374 -25.262 30.607  1.00 0.00 ? 264 ALA A CB    1 
ATOM   2051 N  N     . LYS A 1 266 ? 22.784 -26.286 27.830  1.00 0.00 ? 265 LYS A N     1 
ATOM   2052 C  CA    . LYS A 1 266 ? 22.385 -27.376 26.925  1.00 0.00 ? 265 LYS A CA    1 
ATOM   2053 C  C     . LYS A 1 266 ? 23.205 -27.456 25.631  1.00 0.00 ? 265 LYS A C     1 
ATOM   2054 O  O     . LYS A 1 266 ? 23.787 -28.502 25.307  1.00 0.00 ? 265 LYS A O     1 
ATOM   2055 C  CB    . LYS A 1 266 ? 20.937 -27.198 26.476  1.00 0.00 ? 265 LYS A CB    1 
ATOM   2056 C  CG    . LYS A 1 266 ? 20.063 -26.506 27.515  1.00 0.00 ? 265 LYS A CG    1 
ATOM   2057 C  CD    . LYS A 1 266 ? 18.571 -26.645 27.219  1.00 0.00 ? 265 LYS A CD    1 
ATOM   2058 C  CE    . LYS A 1 266 ? 17.725 -26.815 28.480  1.00 0.00 ? 265 LYS A CE    1 
ATOM   2059 N  NZ    . LYS A 1 266 ? 16.305 -26.506 28.264  1.00 0.00 ? 265 LYS A NZ    1 
ATOM   2060 N  N     . LEU A 1 267 ? 23.244 -26.353 24.901  1.00 0.00 ? 266 LEU A N     1 
ATOM   2061 C  CA    . LEU A 1 267 ? 23.983 -26.301 23.631  1.00 0.00 ? 266 LEU A CA    1 
ATOM   2062 C  C     . LEU A 1 267 ? 25.425 -26.603 23.925  1.00 0.00 ? 266 LEU A C     1 
ATOM   2063 O  O     . LEU A 1 267 ? 26.081 -27.364 23.199  1.00 0.00 ? 266 LEU A O     1 
ATOM   2064 C  CB    . LEU A 1 267 ? 23.822 -24.952 22.927  1.00 0.00 ? 266 LEU A CB    1 
ATOM   2065 C  CG    . LEU A 1 267 ? 24.163 -23.753 23.804  1.00 0.00 ? 266 LEU A CG    1 
ATOM   2066 C  CD1   . LEU A 1 267 ? 25.564 -23.200 23.539  1.00 0.00 ? 266 LEU A CD1   1 
ATOM   2067 C  CD2   . LEU A 1 267 ? 23.206 -22.577 23.601  1.00 0.00 ? 266 LEU A CD2   1 
ATOM   2068 N  N     . MET A 1 268 ? 25.847 -25.981 24.990  1.00 0.00 ? 267 MET A N     1 
ATOM   2069 C  CA    . MET A 1 268 ? 27.204 -26.107 25.469  1.00 0.00 ? 267 MET A CA    1 
ATOM   2070 C  C     . MET A 1 268 ? 27.537 -27.588 25.634  1.00 0.00 ? 267 MET A C     1 
ATOM   2071 O  O     . MET A 1 268 ? 28.607 -28.053 25.213  1.00 0.00 ? 267 MET A O     1 
ATOM   2072 C  CB    . MET A 1 268 ? 27.348 -25.402 26.819  1.00 0.00 ? 267 MET A CB    1 
ATOM   2073 C  CG    . MET A 1 268 ? 27.973 -24.010 26.707  1.00 0.00 ? 267 MET A CG    1 
ATOM   2074 S  SD    . MET A 1 268 ? 28.601 -23.403 28.258  1.00 0.00 ? 267 MET A SD    1 
ATOM   2075 C  CE    . MET A 1 268 ? 27.382 -23.621 29.536  1.00 0.00 ? 267 MET A CE    1 
ATOM   2076 N  N     . GLU A 1 269 ? 26.624 -28.321 26.243  1.00 0.00 ? 268 GLU A N     1 
ATOM   2077 C  CA    . GLU A 1 269 ? 26.823 -29.767 26.487  1.00 0.00 ? 268 GLU A CA    1 
ATOM   2078 C  C     . GLU A 1 269 ? 27.066 -30.531 25.186  1.00 0.00 ? 268 GLU A C     1 
ATOM   2079 O  O     . GLU A 1 269 ? 28.025 -31.309 25.072  1.00 0.00 ? 268 GLU A O     1 
ATOM   2080 C  CB    . GLU A 1 269 ? 25.574 -30.393 27.109  1.00 0.00 ? 268 GLU A CB    1 
ATOM   2081 C  CG    . GLU A 1 269 ? 24.968 -29.547 28.223  1.00 0.00 ? 268 GLU A CG    1 
ATOM   2082 C  CD    . GLU A 1 269 ? 25.833 -29.525 29.482  1.00 0.00 ? 268 GLU A CD    1 
ATOM   2083 O  OE1   . GLU A 1 269 ? 25.277 -29.532 30.646  1.00 0.00 ? 268 GLU A OE1   1 
ATOM   2084 O  OE2   . GLU A 1 269 ? 27.118 -29.499 29.380  1.00 0.00 ? 268 GLU A OE2   1 
ATOM   2085 N  N     . LYS A 1 270 ? 26.178 -30.275 24.251  1.00 0.00 ? 269 LYS A N     1 
ATOM   2086 C  CA    . LYS A 1 270 ? 26.204 -30.904 22.933  1.00 0.00 ? 269 LYS A CA    1 
ATOM   2087 C  C     . LYS A 1 270 ? 27.558 -30.644 22.322  1.00 0.00 ? 269 LYS A C     1 
ATOM   2088 O  O     . LYS A 1 270 ? 28.168 -31.537 21.715  1.00 0.00 ? 269 LYS A O     1 
ATOM   2089 C  CB    . LYS A 1 270 ? 25.098 -30.327 22.057  1.00 0.00 ? 269 LYS A CB    1 
ATOM   2090 C  CG    . LYS A 1 270 ? 23.699 -30.652 22.577  1.00 0.00 ? 269 LYS A CG    1 
ATOM   2091 C  CD    . LYS A 1 270 ? 22.643 -29.653 22.102  1.00 0.00 ? 269 LYS A CD    1 
ATOM   2092 C  CE    . LYS A 1 270 ? 21.224 -30.040 22.519  1.00 0.00 ? 269 LYS A CE    1 
ATOM   2093 N  NZ    . LYS A 1 270 ? 20.208 -29.648 21.531  1.00 0.00 ? 269 LYS A NZ    1 
ATOM   2094 N  N     . ALA A 1 271 ? 27.967 -29.418 22.511  1.00 0.00 ? 270 ALA A N     1 
ATOM   2095 C  CA    . ALA A 1 271 ? 29.243 -28.942 22.013  1.00 0.00 ? 270 ALA A CA    1 
ATOM   2096 C  C     . ALA A 1 271 ? 30.359 -29.866 22.504  1.00 0.00 ? 270 ALA A C     1 
ATOM   2097 O  O     . ALA A 1 271 ? 31.234 -30.278 21.728  1.00 0.00 ? 270 ALA A O     1 
ATOM   2098 C  CB    . ALA A 1 271 ? 29.505 -27.523 22.521  1.00 0.00 ? 270 ALA A CB    1 
ATOM   2099 N  N     . LYS A 1 272 ? 30.333 -30.188 23.786  1.00 0.00 ? 271 LYS A N     1 
ATOM   2100 C  CA    . LYS A 1 272 ? 31.358 -31.077 24.363  1.00 0.00 ? 271 LYS A CA    1 
ATOM   2101 C  C     . LYS A 1 272 ? 31.352 -32.404 23.605  1.00 0.00 ? 271 LYS A C     1 
ATOM   2102 O  O     . LYS A 1 272 ? 32.403 -32.891 23.162  1.00 0.00 ? 271 LYS A O     1 
ATOM   2103 C  CB    . LYS A 1 272 ? 31.059 -31.354 25.853  1.00 0.00 ? 271 LYS A CB    1 
ATOM   2104 C  CG    . LYS A 1 272 ? 31.959 -32.440 26.475  1.00 0.00 ? 271 LYS A CG    1 
ATOM   2105 C  CD    . LYS A 1 272 ? 31.518 -32.858 27.889  1.00 0.00 ? 271 LYS A CD    1 
ATOM   2106 C  CE    . LYS A 1 272 ? 32.554 -33.722 28.620  1.00 0.00 ? 271 LYS A CE    1 
ATOM   2107 N  NZ    . LYS A 1 272 ? 32.079 -34.208 29.924  1.00 0.00 ? 271 LYS A NZ    1 
ATOM   2108 N  N     . ALA A 1 273 ? 30.148 -32.937 23.486  1.00 0.00 ? 272 ALA A N     1 
ATOM   2109 C  CA    . ALA A 1 273 ? 29.892 -34.221 22.811  1.00 0.00 ? 272 ALA A CA    1 
ATOM   2110 C  C     . ALA A 1 273 ? 30.301 -34.196 21.333  1.00 0.00 ? 272 ALA A C     1 
ATOM   2111 O  O     . ALA A 1 273 ? 31.028 -35.080 20.856  1.00 0.00 ? 272 ALA A O     1 
ATOM   2112 C  CB    . ALA A 1 273 ? 28.401 -34.558 22.877  1.00 0.00 ? 272 ALA A CB    1 
ATOM   2113 N  N     . LYS A 1 274 ? 29.820 -33.178 20.645  1.00 0.00 ? 273 LYS A N     1 
ATOM   2114 C  CA    . LYS A 1 274 ? 30.070 -32.999 19.201  1.00 0.00 ? 273 LYS A CA    1 
ATOM   2115 C  C     . LYS A 1 274 ? 31.576 -32.880 18.900  1.00 0.00 ? 273 LYS A C     1 
ATOM   2116 O  O     . LYS A 1 274 ? 32.099 -33.535 17.986  1.00 0.00 ? 273 LYS A O     1 
ATOM   2117 C  CB    . LYS A 1 274 ? 29.334 -31.760 18.688  1.00 0.00 ? 273 LYS A CB    1 
ATOM   2118 C  CG    . LYS A 1 274 ? 27.893 -32.059 18.243  1.00 0.00 ? 273 LYS A CG    1 
ATOM   2119 C  CD    . LYS A 1 274 ? 27.740 -33.421 17.553  1.00 0.00 ? 273 LYS A CD    1 
ATOM   2120 C  CE    . LYS A 1 274 ? 26.289 -33.750 17.185  1.00 0.00 ? 273 LYS A CE    1 
ATOM   2121 N  NZ    . LYS A 1 274 ? 26.161 -34.985 16.399  1.00 0.00 ? 273 LYS A NZ    1 
ATOM   2122 N  N     . GLY A 1 275 ? 32.238 -32.036 19.682  1.00 0.00 ? 274 GLY A N     1 
ATOM   2123 C  CA    . GLY A 1 275 ? 33.681 -31.754 19.530  1.00 0.00 ? 274 GLY A CA    1 
ATOM   2124 C  C     . GLY A 1 275 ? 34.371 -31.907 20.870  1.00 0.00 ? 274 GLY A C     1 
ATOM   2125 O  O     . GLY A 1 275 ? 34.885 -32.985 21.205  1.00 0.00 ? 274 GLY A O     1 
ATOM   2126 N  N     . VAL A 1 276 ? 34.381 -30.824 21.646  1.00 0.00 ? 275 VAL A N     1 
ATOM   2127 C  CA    . VAL A 1 276 ? 35.009 -30.915 22.969  1.00 0.00 ? 275 VAL A CA    1 
ATOM   2128 C  C     . VAL A 1 276 ? 35.015 -29.615 23.815  1.00 0.00 ? 275 VAL A C     1 
ATOM   2129 O  O     . VAL A 1 276 ? 34.368 -29.536 24.869  1.00 0.00 ? 275 VAL A O     1 
ATOM   2130 C  CB    . VAL A 1 276 ? 36.468 -31.367 22.819  1.00 0.00 ? 275 VAL A CB    1 
ATOM   2131 C  CG1   . VAL A 1 276 ? 37.383 -30.269 22.272  1.00 0.00 ? 275 VAL A CG1   1 
ATOM   2132 C  CG2   . VAL A 1 276 ? 37.097 -31.809 24.141  1.00 0.00 ? 275 VAL A CG2   1 
ATOM   2133 N  N     . GLU A 1 277 ? 35.742 -28.608 23.353  1.00 0.00 ? 276 GLU A N     1 
ATOM   2134 C  CA    . GLU A 1 277 ? 36.063 -27.413 24.190  1.00 0.00 ? 276 GLU A CA    1 
ATOM   2135 C  C     . GLU A 1 277 ? 35.678 -25.997 23.708  1.00 0.00 ? 276 GLU A C     1 
ATOM   2136 O  O     . GLU A 1 277 ? 35.959 -25.613 22.563  1.00 0.00 ? 276 GLU A O     1 
ATOM   2137 C  CB    . GLU A 1 277 ? 37.501 -27.405 24.601  1.00 0.00 ? 276 GLU A CB    1 
ATOM   2138 C  CG    . GLU A 1 277 ? 38.324 -26.392 23.875  1.00 0.00 ? 276 GLU A CG    1 
ATOM   2139 C  CD    . GLU A 1 277 ? 39.632 -27.006 23.442  1.00 0.00 ? 276 GLU A CD    1 
ATOM   2140 O  OE1   . GLU A 1 277 ? 40.717 -26.728 24.082  1.00 0.00 ? 276 GLU A OE1   1 
ATOM   2141 O  OE2   . GLU A 1 277 ? 39.662 -27.810 22.434  1.00 0.00 ? 276 GLU A OE2   1 
ATOM   2142 N  N     . VAL A 1 278 ? 35.045 -25.385 24.700  1.00 0.00 ? 277 VAL A N     1 
ATOM   2143 C  CA    . VAL A 1 278 ? 34.575 -23.989 24.758  1.00 0.00 ? 277 VAL A CA    1 
ATOM   2144 C  C     . VAL A 1 278 ? 35.404 -23.235 25.811  1.00 0.00 ? 277 VAL A C     1 
ATOM   2145 O  O     . VAL A 1 278 ? 35.469 -23.638 26.982  1.00 0.00 ? 277 VAL A O     1 
ATOM   2146 C  CB    . VAL A 1 278 ? 33.134 -23.892 25.250  1.00 0.00 ? 277 VAL A CB    1 
ATOM   2147 C  CG1   . VAL A 1 278 ? 32.718 -22.458 25.589  1.00 0.00 ? 277 VAL A CG1   1 
ATOM   2148 C  CG2   . VAL A 1 278 ? 32.115 -24.390 24.225  1.00 0.00 ? 277 VAL A CG2   1 
ATOM   2149 N  N     . VAL A 1 279 ? 36.035 -22.152 25.385  1.00 0.00 ? 278 VAL A N     1 
ATOM   2150 C  CA    . VAL A 1 279 ? 36.934 -21.372 26.263  1.00 0.00 ? 278 VAL A CA    1 
ATOM   2151 C  C     . VAL A 1 279 ? 36.341 -20.016 26.624  1.00 0.00 ? 278 VAL A C     1 
ATOM   2152 O  O     . VAL A 1 279 ? 36.096 -19.172 25.748  1.00 0.00 ? 278 VAL A O     1 
ATOM   2153 C  CB    . VAL A 1 279 ? 38.278 -21.066 25.593  1.00 0.00 ? 278 VAL A CB    1 
ATOM   2154 C  CG1   . VAL A 1 279 ? 38.769 -22.196 24.688  1.00 0.00 ? 278 VAL A CG1   1 
ATOM   2155 C  CG2   . VAL A 1 279 ? 38.235 -19.817 24.710  1.00 0.00 ? 278 VAL A CG2   1 
ATOM   2156 N  N     . LEU A 1 280 ? 36.146 -19.915 27.936  1.00 0.00 ? 279 LEU A N     1 
ATOM   2157 C  CA    . LEU A 1 280 ? 35.593 -18.732 28.607  1.00 0.00 ? 279 LEU A CA    1 
ATOM   2158 C  C     . LEU A 1 280 ? 36.664 -17.945 29.399  1.00 0.00 ? 279 LEU A C     1 
ATOM   2159 O  O     . LEU A 1 280 ? 37.853 -18.299 29.390  1.00 0.00 ? 279 LEU A O     1 
ATOM   2160 C  CB    . LEU A 1 280 ? 34.518 -19.157 29.600  1.00 0.00 ? 279 LEU A CB    1 
ATOM   2161 C  CG    . LEU A 1 280 ? 33.356 -19.892 28.935  1.00 0.00 ? 279 LEU A CG    1 
ATOM   2162 C  CD1   . LEU A 1 280 ? 32.104 -19.024 28.794  1.00 0.00 ? 279 LEU A CD1   1 
ATOM   2163 C  CD2   . LEU A 1 280 ? 33.687 -20.376 27.521  1.00 0.00 ? 279 LEU A CD2   1 
ATOM   2164 N  N     . PRO A 1 281 ? 36.226 -16.870 30.090  1.00 0.00 ? 280 PRO A N     1 
ATOM   2165 C  CA    . PRO A 1 281 ? 37.106 -15.970 30.875  1.00 0.00 ? 280 PRO A CA    1 
ATOM   2166 C  C     . PRO A 1 281 ? 37.872 -16.640 32.037  1.00 0.00 ? 280 PRO A C     1 
ATOM   2167 O  O     . PRO A 1 281 ? 38.791 -17.476 31.770  1.00 0.00 ? 280 PRO A O     1 
ATOM   2168 C  CB    . PRO A 1 281 ? 36.151 -14.926 31.415  1.00 0.00 ? 280 PRO A CB    1 
ATOM   2169 C  CG    . PRO A 1 281 ? 34.747 -15.262 30.928  1.00 0.00 ? 280 PRO A CG    1 
ATOM   2170 C  CD    . PRO A 1 281 ? 34.805 -16.501 30.095  1.00 0.00 ? 280 PRO A CD    1 
ATOM   2171 N  N     . VAL A 1 282 ? 37.461 -16.242 33.248  1.00 0.00 ? 281 VAL A N     1 
ATOM   2172 C  CA    . VAL A 1 282 ? 38.054 -16.611 34.572  1.00 0.00 ? 281 VAL A CA    1 
ATOM   2173 C  C     . VAL A 1 282 ? 38.734 -15.373 35.140  1.00 0.00 ? 281 VAL A C     1 
ATOM   2174 O  O     . VAL A 1 282 ? 38.858 -15.217 36.364  1.00 0.00 ? 281 VAL A O     1 
ATOM   2175 C  CB    . VAL A 1 282 ? 39.123 -17.707 34.464  1.00 0.00 ? 281 VAL A CB    1 
ATOM   2176 C  CG1   . VAL A 1 282 ? 39.825 -17.991 35.794  1.00 0.00 ? 281 VAL A CG1   1 
ATOM   2177 C  CG2   . VAL A 1 282 ? 38.557 -19.050 33.999  1.00 0.00 ? 281 VAL A CG2   1 
ATOM   2178 N  N     . ASP A 1 283 ? 39.152 -14.541 34.209  1.00 0.00 ? 282 ASP A N     1 
ATOM   2179 C  CA    . ASP A 1 283 ? 39.716 -13.235 34.505  1.00 0.00 ? 282 ASP A CA    1 
ATOM   2180 C  C     . ASP A 1 283 ? 39.031 -12.283 33.544  1.00 0.00 ? 282 ASP A C     1 
ATOM   2181 O  O     . ASP A 1 283 ? 39.047 -12.490 32.321  1.00 0.00 ? 282 ASP A O     1 
ATOM   2182 C  CB    . ASP A 1 283 ? 41.238 -13.237 34.320  1.00 0.00 ? 282 ASP A CB    1 
ATOM   2183 C  CG    . ASP A 1 283 ? 41.862 -11.845 34.485  1.00 0.00 ? 282 ASP A CG    1 
ATOM   2184 O  OD1   . ASP A 1 283 ? 41.860 -11.016 33.497  1.00 0.00 ? 282 ASP A OD1   1 
ATOM   2185 O  OD2   . ASP A 1 283 ? 42.389 -11.503 35.612  1.00 0.00 ? 282 ASP A OD2   1 
ATOM   2186 N  N     . PHE A 1 284 ? 38.491 -11.321 34.244  1.00 0.00 ? 283 PHE A N     1 
ATOM   2187 C  CA    . PHE A 1 284 ? 37.585 -10.286 33.750  1.00 0.00 ? 283 PHE A CA    1 
ATOM   2188 C  C     . PHE A 1 284 ? 37.831 -8.955  34.399  1.00 0.00 ? 283 PHE A C     1 
ATOM   2189 O  O     . PHE A 1 284 ? 38.348 -8.881  35.524  1.00 0.00 ? 283 PHE A O     1 
ATOM   2190 C  CB    . PHE A 1 284 ? 36.094 -10.473 34.056  1.00 0.00 ? 283 PHE A CB    1 
ATOM   2191 C  CG    . PHE A 1 284 ? 35.526 -11.883 34.013  1.00 0.00 ? 283 PHE A CG    1 
ATOM   2192 C  CD1   . PHE A 1 284 ? 34.223 -12.069 33.541  1.00 0.00 ? 283 PHE A CD1   1 
ATOM   2193 C  CD2   . PHE A 1 284 ? 36.274 -12.969 34.467  1.00 0.00 ? 283 PHE A CD2   1 
ATOM   2194 C  CE1   . PHE A 1 284 ? 33.656 -13.343 33.545  1.00 0.00 ? 283 PHE A CE1   1 
ATOM   2195 C  CE2   . PHE A 1 284 ? 35.707 -14.244 34.474  1.00 0.00 ? 283 PHE A CE2   1 
ATOM   2196 C  CZ    . PHE A 1 284 ? 34.396 -14.431 34.019  1.00 0.00 ? 283 PHE A CZ    1 
ATOM   2197 N  N     . ILE A 1 285 ? 37.452 -7.963  33.660  1.00 0.00 ? 284 ILE A N     1 
ATOM   2198 C  CA    . ILE A 1 285 ? 37.522 -6.596  34.120  1.00 0.00 ? 284 ILE A CA    1 
ATOM   2199 C  C     . ILE A 1 285 ? 36.113 -5.999  33.981  1.00 0.00 ? 284 ILE A C     1 
ATOM   2200 O  O     . ILE A 1 285 ? 35.459 -6.144  32.938  1.00 0.00 ? 284 ILE A O     1 
ATOM   2201 C  CB    . ILE A 1 285 ? 38.501 -5.814  33.247  1.00 0.00 ? 284 ILE A CB    1 
ATOM   2202 C  CG1   . ILE A 1 285 ? 38.534 -6.310  31.800  1.00 0.00 ? 284 ILE A CG1   1 
ATOM   2203 C  CG2   . ILE A 1 285 ? 39.944 -5.888  33.751  1.00 0.00 ? 284 ILE A CG2   1 
ATOM   2204 C  CD1   . ILE A 1 285 ? 39.951 -6.592  31.296  1.00 0.00 ? 284 ILE A CD1   1 
ATOM   2205 N  N     . ILE A 1 286 ? 35.773 -5.356  35.103  1.00 0.00 ? 285 ILE A N     1 
ATOM   2206 C  CA    . ILE A 1 286 ? 34.454 -4.762  35.417  1.00 0.00 ? 285 ILE A CA    1 
ATOM   2207 C  C     . ILE A 1 286 ? 34.623 -3.394  36.079  1.00 0.00 ? 285 ILE A C     1 
ATOM   2208 O  O     . ILE A 1 286 ? 35.564 -3.173  36.856  1.00 0.00 ? 285 ILE A O     1 
ATOM   2209 C  CB    . ILE A 1 286 ? 33.653 -5.643  36.374  1.00 0.00 ? 285 ILE A CB    1 
ATOM   2210 C  CG1   . ILE A 1 286 ? 32.164 -5.286  36.389  1.00 0.00 ? 285 ILE A CG1   1 
ATOM   2211 C  CG2   . ILE A 1 286 ? 34.132 -5.541  37.824  1.00 0.00 ? 285 ILE A CG2   1 
ATOM   2212 C  CD1   . ILE A 1 286 ? 31.724 -4.509  35.146  1.00 0.00 ? 285 ILE A CD1   1 
ATOM   2213 N  N     . ALA A 1 287 ? 33.693 -2.521  35.728  1.00 0.00 ? 286 ALA A N     1 
ATOM   2214 C  CA    . ALA A 1 287 ? 33.700 -1.112  36.160  1.00 0.00 ? 286 ALA A CA    1 
ATOM   2215 C  C     . ALA A 1 287 ? 32.317 -0.632  36.631  1.00 0.00 ? 286 ALA A C     1 
ATOM   2216 O  O     . ALA A 1 287 ? 31.284 -0.979  36.040  1.00 0.00 ? 286 ALA A O     1 
ATOM   2217 C  CB    . ALA A 1 287 ? 34.114 -0.212  34.994  1.00 0.00 ? 286 ALA A CB    1 
ATOM   2218 N  N     . ASP A 1 288 ? 32.339 0.152   37.701  1.00 0.00 ? 287 ASP A N     1 
ATOM   2219 C  CA    . ASP A 1 288 ? 31.114 0.762   38.260  1.00 0.00 ? 287 ASP A CA    1 
ATOM   2220 C  C     . ASP A 1 288 ? 29.918 0.515   37.306  1.00 0.00 ? 287 ASP A C     1 
ATOM   2221 O  O     . ASP A 1 288 ? 29.225 -0.509  37.402  1.00 0.00 ? 287 ASP A O     1 
ATOM   2222 C  CB    . ASP A 1 288 ? 31.309 2.272   38.456  1.00 0.00 ? 287 ASP A CB    1 
ATOM   2223 C  CG    . ASP A 1 288 ? 30.218 2.909   39.325  1.00 0.00 ? 287 ASP A CG    1 
ATOM   2224 O  OD1   . ASP A 1 288 ? 30.252 4.173   39.580  1.00 0.00 ? 287 ASP A OD1   1 
ATOM   2225 O  OD2   . ASP A 1 288 ? 29.266 2.180   39.801  1.00 0.00 ? 287 ASP A OD2   1 
ATOM   2226 N  N     . ALA A 1 289 ? 29.686 1.454   36.382  1.00 0.00 ? 288 ALA A N     1 
ATOM   2227 C  CA    . ALA A 1 289 ? 28.562 1.371   35.392  1.00 0.00 ? 288 ALA A CA    1 
ATOM   2228 C  C     . ALA A 1 289 ? 28.934 0.454   34.197  1.00 0.00 ? 288 ALA A C     1 
ATOM   2229 O  O     . ALA A 1 289 ? 30.002 -0.175  34.183  1.00 0.00 ? 288 ALA A O     1 
ATOM   2230 C  CB    . ALA A 1 289 ? 28.240 2.765   34.847  1.00 0.00 ? 288 ALA A CB    1 
ATOM   2231 N  N     . PHE A 1 290 ? 28.028 0.389   33.201  1.00 0.00 ? 289 PHE A N     1 
ATOM   2232 C  CA    . PHE A 1 290 ? 28.234 -0.425  31.959  1.00 0.00 ? 289 PHE A CA    1 
ATOM   2233 C  C     . PHE A 1 290 ? 29.132 0.342   30.993  1.00 0.00 ? 289 PHE A C     1 
ATOM   2234 O  O     . PHE A 1 290 ? 29.903 -0.256  30.228  1.00 0.00 ? 289 PHE A O     1 
ATOM   2235 C  CB    . PHE A 1 290 ? 26.898 -0.716  31.234  1.00 0.00 ? 289 PHE A CB    1 
ATOM   2236 C  CG    . PHE A 1 290 ? 27.057 -1.137  29.745  1.00 0.00 ? 289 PHE A CG    1 
ATOM   2237 C  CD1   . PHE A 1 290 ? 26.243 -0.559  28.752  1.00 0.00 ? 289 PHE A CD1   1 
ATOM   2238 C  CD2   . PHE A 1 290 ? 28.007 -2.101  29.365  1.00 0.00 ? 289 PHE A CD2   1 
ATOM   2239 C  CE1   . PHE A 1 290 ? 26.379 -0.940  27.406  1.00 0.00 ? 289 PHE A CE1   1 
ATOM   2240 C  CE2   . PHE A 1 290 ? 28.141 -2.480  28.017  1.00 0.00 ? 289 PHE A CE2   1 
ATOM   2241 C  CZ    . PHE A 1 290 ? 27.327 -1.899  27.039  1.00 0.00 ? 289 PHE A CZ    1 
ATOM   2242 N  N     . SER A 1 291 ? 28.984 1.649   31.079  1.00 0.00 ? 290 SER A N     1 
ATOM   2243 C  CA    . SER A 1 291 ? 29.739 2.603   30.261  1.00 0.00 ? 290 SER A CA    1 
ATOM   2244 C  C     . SER A 1 291 ? 31.236 2.296   30.351  1.00 0.00 ? 290 SER A C     1 
ATOM   2245 O  O     . SER A 1 291 ? 31.642 1.133   30.494  1.00 0.00 ? 290 SER A O     1 
ATOM   2246 C  CB    . SER A 1 291 ? 29.483 4.025   30.765  1.00 0.00 ? 290 SER A CB    1 
ATOM   2247 O  OG    . SER A 1 291 ? 30.342 4.938   30.098  1.00 0.00 ? 290 SER A OG    1 
ATOM   2248 N  N     . ALA A 1 292 ? 32.014 3.362   30.266  1.00 0.00 ? 291 ALA A N     1 
ATOM   2249 C  CA    . ALA A 1 292 ? 33.484 3.293   30.329  1.00 0.00 ? 291 ALA A CA    1 
ATOM   2250 C  C     . ALA A 1 292 ? 34.025 4.364   31.289  1.00 0.00 ? 291 ALA A C     1 
ATOM   2251 O  O     . ALA A 1 292 ? 34.298 5.504   30.884  1.00 0.00 ? 291 ALA A O     1 
ATOM   2252 C  CB    . ALA A 1 292 ? 34.079 3.527   28.939  1.00 0.00 ? 291 ALA A CB    1 
ATOM   2253 N  N     . SER A 1 293 ? 34.162 3.949   32.540  1.00 0.00 ? 292 SER A N     1 
ATOM   2254 C  CA    . SER A 1 293 ? 34.660 4.801   33.643  1.00 0.00 ? 292 SER A CA    1 
ATOM   2255 C  C     . SER A 1 293 ? 34.608 3.999   34.955  1.00 0.00 ? 292 SER A C     1 
ATOM   2256 O  O     . SER A 1 293 ? 33.778 3.093   35.118  1.00 0.00 ? 292 SER A O     1 
ATOM   2257 C  CB    . SER A 1 293 ? 33.782 6.048   33.769  1.00 0.00 ? 292 SER A CB    1 
ATOM   2258 O  OG    . SER A 1 293 ? 34.201 6.827   34.879  1.00 0.00 ? 292 SER A OG    1 
ATOM   2259 N  N     . ALA A 1 294 ? 35.490 4.337   35.893  1.00 0.00 ? 293 ALA A N     1 
ATOM   2260 C  CA    . ALA A 1 294 ? 35.559 3.600   37.171  1.00 0.00 ? 293 ALA A CA    1 
ATOM   2261 C  C     . ALA A 1 294 ? 35.445 2.107   36.839  1.00 0.00 ? 293 ALA A C     1 
ATOM   2262 O  O     . ALA A 1 294 ? 34.351 1.601   36.548  1.00 0.00 ? 293 ALA A O     1 
ATOM   2263 C  CB    . ALA A 1 294 ? 34.417 4.037   38.089  1.00 0.00 ? 293 ALA A CB    1 
ATOM   2264 N  N     . ASN A 1 295 ? 36.609 1.477   36.906  1.00 0.00 ? 294 ASN A N     1 
ATOM   2265 C  CA    . ASN A 1 295 ? 36.826 0.078   36.482  1.00 0.00 ? 294 ASN A CA    1 
ATOM   2266 C  C     . ASN A 1 295 ? 37.736 -0.717  37.425  1.00 0.00 ? 294 ASN A C     1 
ATOM   2267 O  O     . ASN A 1 295 ? 38.680 -0.168  38.014  1.00 0.00 ? 294 ASN A O     1 
ATOM   2268 C  CB    . ASN A 1 295 ? 37.504 0.007   35.127  1.00 0.00 ? 294 ASN A CB    1 
ATOM   2269 C  CG    . ASN A 1 295 ? 38.529 -1.123  35.069  1.00 0.00 ? 294 ASN A CG    1 
ATOM   2270 O  OD1   . ASN A 1 295 ? 38.436 -1.995  34.206  1.00 0.00 ? 294 ASN A OD1   1 
ATOM   2271 N  ND2   . ASN A 1 295 ? 39.515 -1.164  35.945  1.00 0.00 ? 294 ASN A ND2   1 
ATOM   2272 N  N     . THR A 1 296 ? 37.400 -1.996  37.521  1.00 0.00 ? 295 THR A N     1 
ATOM   2273 C  CA    . THR A 1 296 ? 38.127 -2.974  38.353  1.00 0.00 ? 295 THR A CA    1 
ATOM   2274 C  C     . THR A 1 296 ? 38.395 -4.276  37.563  1.00 0.00 ? 295 THR A C     1 
ATOM   2275 O  O     . THR A 1 296 ? 37.520 -4.775  36.840  1.00 0.00 ? 295 THR A O     1 
ATOM   2276 C  CB    . THR A 1 296 ? 37.288 -3.355  39.576  1.00 0.00 ? 295 THR A CB    1 
ATOM   2277 O  OG1   . THR A 1 296 ? 37.247 -2.274  40.494  1.00 0.00 ? 295 THR A OG1   1 
ATOM   2278 C  CG2   . THR A 1 296 ? 37.840 -4.570  40.324  1.00 0.00 ? 295 THR A CG2   1 
ATOM   2279 N  N     . LYS A 1 297 ? 39.629 -4.797  37.723  1.00 0.00 ? 296 LYS A N     1 
ATOM   2280 C  CA    . LYS A 1 297 ? 40.062 -6.057  37.072  1.00 0.00 ? 296 LYS A CA    1 
ATOM   2281 C  C     . LYS A 1 297 ? 40.807 -6.948  38.081  1.00 0.00 ? 296 LYS A C     1 
ATOM   2282 O  O     . LYS A 1 297 ? 41.782 -6.519  38.714  1.00 0.00 ? 296 LYS A O     1 
ATOM   2283 C  CB    . LYS A 1 297 ? 41.042 -5.751  35.954  1.00 0.00 ? 296 LYS A CB    1 
ATOM   2284 C  CG    . LYS A 1 297 ? 42.461 -5.540  36.471  1.00 0.00 ? 296 LYS A CG    1 
ATOM   2285 C  CD    . LYS A 1 297 ? 43.530 -6.032  35.500  1.00 0.00 ? 296 LYS A CD    1 
ATOM   2286 C  CE    . LYS A 1 297 ? 44.944 -5.630  35.918  1.00 0.00 ? 296 LYS A CE    1 
ATOM   2287 N  NZ    . LYS A 1 297 ? 45.783 -5.221  34.784  1.00 0.00 ? 296 LYS A NZ    1 
ATOM   2288 N  N     . THR A 1 298 ? 40.213 -8.102  38.097  1.00 0.00 ? 297 THR A N     1 
ATOM   2289 C  CA    . THR A 1 298 ? 40.445 -9.243  38.983  1.00 0.00 ? 297 THR A CA    1 
ATOM   2290 C  C     . THR A 1 298 ? 40.105 -10.503 38.271  1.00 0.00 ? 297 THR A C     1 
ATOM   2291 O  O     . THR A 1 298 ? 39.493 -10.482 37.192  1.00 0.00 ? 297 THR A O     1 
ATOM   2292 C  CB    . THR A 1 298 ? 39.671 -9.192  40.282  1.00 0.00 ? 297 THR A CB    1 
ATOM   2293 O  OG1   . THR A 1 298 ? 40.346 -9.956  41.272  1.00 0.00 ? 297 THR A OG1   1 
ATOM   2294 C  CG2   . THR A 1 298 ? 38.255 -9.753  40.155  1.00 0.00 ? 297 THR A CG2   1 
ATOM   2295 N  N     . VAL A 1 299 ? 40.491 -11.581 38.843  1.00 0.00 ? 298 VAL A N     1 
ATOM   2296 C  CA    . VAL A 1 299 ? 40.126 -12.808 38.215  1.00 0.00 ? 298 VAL A CA    1 
ATOM   2297 C  C     . VAL A 1 299 ? 39.142 -13.544 39.096  1.00 0.00 ? 298 VAL A C     1 
ATOM   2298 O  O     . VAL A 1 299 ? 39.387 -13.750 40.294  1.00 0.00 ? 298 VAL A O     1 
ATOM   2299 C  CB    . VAL A 1 299 ? 41.319 -13.769 38.211  1.00 0.00 ? 298 VAL A CB    1 
ATOM   2300 C  CG1   . VAL A 1 299 ? 42.559 -13.189 37.528  1.00 0.00 ? 298 VAL A CG1   1 
ATOM   2301 C  CG2   . VAL A 1 299 ? 41.769 -14.161 39.622  1.00 0.00 ? 298 VAL A CG2   1 
ATOM   2302 N  N     . THR A 1 300 ? 38.085 -13.865 38.356  1.00 0.00 ? 299 THR A N     1 
ATOM   2303 C  CA    . THR A 1 300 ? 36.903 -14.607 38.800  1.00 0.00 ? 299 THR A CA    1 
ATOM   2304 C  C     . THR A 1 300 ? 36.020 -13.840 39.809  1.00 0.00 ? 299 THR A C     1 
ATOM   2305 O  O     . THR A 1 300 ? 35.601 -12.701 39.556  1.00 0.00 ? 299 THR A O     1 
ATOM   2306 C  CB    . THR A 1 300 ? 37.351 -15.898 39.464  1.00 0.00 ? 299 THR A CB    1 
ATOM   2307 O  OG1   . THR A 1 300 ? 38.443 -16.456 38.747  1.00 0.00 ? 299 THR A OG1   1 
ATOM   2308 C  CG2   . THR A 1 300 ? 36.248 -16.956 39.517  1.00 0.00 ? 299 THR A CG2   1 
ATOM   2309 N  N     . ASP A 1 301 ? 35.818 -14.563 40.898  1.00 0.00 ? 300 ASP A N     1 
ATOM   2310 C  CA    . ASP A 1 301 ? 34.957 -14.225 42.052  1.00 0.00 ? 300 ASP A CA    1 
ATOM   2311 C  C     . ASP A 1 301 ? 34.977 -12.738 42.510  1.00 0.00 ? 300 ASP A C     1 
ATOM   2312 O  O     . ASP A 1 301 ? 36.047 -12.130 42.659  1.00 0.00 ? 300 ASP A O     1 
ATOM   2313 C  CB    . ASP A 1 301 ? 35.386 -15.030 43.285  1.00 0.00 ? 300 ASP A CB    1 
ATOM   2314 C  CG    . ASP A 1 301 ? 35.528 -16.530 43.010  1.00 0.00 ? 300 ASP A CG    1 
ATOM   2315 O  OD1   . ASP A 1 301 ? 34.941 -17.057 41.990  1.00 0.00 ? 300 ASP A OD1   1 
ATOM   2316 O  OD2   . ASP A 1 301 ? 36.234 -17.266 43.800  1.00 0.00 ? 300 ASP A OD2   1 
ATOM   2317 N  N     . LYS A 1 302 ? 33.748 -12.224 42.710  1.00 0.00 ? 301 LYS A N     1 
ATOM   2318 C  CA    . LYS A 1 302 ? 33.431 -10.846 43.233  1.00 0.00 ? 301 LYS A CA    1 
ATOM   2319 C  C     . LYS A 1 302 ? 32.717 -9.949  42.203  1.00 0.00 ? 301 LYS A C     1 
ATOM   2320 O  O     . LYS A 1 302 ? 33.340 -9.437  41.261  1.00 0.00 ? 301 LYS A O     1 
ATOM   2321 C  CB    . LYS A 1 302 ? 34.665 -10.051 43.676  1.00 0.00 ? 301 LYS A CB    1 
ATOM   2322 C  CG    . LYS A 1 302 ? 34.280 -8.777  44.460  1.00 0.00 ? 301 LYS A CG    1 
ATOM   2323 C  CD    . LYS A 1 302 ? 35.384 -7.709  44.500  1.00 0.00 ? 301 LYS A CD    1 
ATOM   2324 C  CE    . LYS A 1 302 ? 34.906 -6.374  45.087  1.00 0.00 ? 301 LYS A CE    1 
ATOM   2325 N  NZ    . LYS A 1 302 ? 36.012 -5.496  45.497  1.00 0.00 ? 301 LYS A NZ    1 
ATOM   2326 N  N     . GLU A 1 303 ? 31.424 -9.801  42.446  1.00 0.00 ? 302 GLU A N     1 
ATOM   2327 C  CA    . GLU A 1 303 ? 30.501 -8.961  41.650  1.00 0.00 ? 302 GLU A CA    1 
ATOM   2328 C  C     . GLU A 1 303 ? 29.232 -8.740  42.492  1.00 0.00 ? 302 GLU A C     1 
ATOM   2329 O  O     . GLU A 1 303 ? 29.150 -9.174  43.651  1.00 0.00 ? 302 GLU A O     1 
ATOM   2330 C  CB    . GLU A 1 303 ? 30.159 -9.655  40.314  1.00 0.00 ? 302 GLU A CB    1 
ATOM   2331 C  CG    . GLU A 1 303 ? 31.404 -10.051 39.500  1.00 0.00 ? 302 GLU A CG    1 
ATOM   2332 C  CD    . GLU A 1 303 ? 31.190 -10.016 37.978  1.00 0.00 ? 302 GLU A CD    1 
ATOM   2333 O  OE1   . GLU A 1 303 ? 32.194 -9.827  37.189  1.00 0.00 ? 302 GLU A OE1   1 
ATOM   2334 O  OE2   . GLU A 1 303 ? 30.008 -10.177 37.488  1.00 0.00 ? 302 GLU A OE2   1 
ATOM   2335 N  N     . GLY A 1 304 ? 28.257 -8.070  41.905  1.00 0.00 ? 303 GLY A N     1 
ATOM   2336 C  CA    . GLY A 1 304 ? 26.977 -7.790  42.585  1.00 0.00 ? 303 GLY A CA    1 
ATOM   2337 C  C     . GLY A 1 304 ? 26.432 -6.429  42.154  1.00 0.00 ? 303 GLY A C     1 
ATOM   2338 O  O     . GLY A 1 304 ? 26.216 -6.177  40.960  1.00 0.00 ? 303 GLY A O     1 
ATOM   2339 N  N     . ILE A 1 305 ? 26.222 -5.589  43.152  1.00 0.00 ? 304 ILE A N     1 
ATOM   2340 C  CA    . ILE A 1 305 ? 25.713 -4.231  42.943  1.00 0.00 ? 304 ILE A CA    1 
ATOM   2341 C  C     . ILE A 1 305 ? 26.138 -3.751  41.567  1.00 0.00 ? 304 ILE A C     1 
ATOM   2342 O  O     . ILE A 1 305 ? 25.386 -3.870  40.588  1.00 0.00 ? 304 ILE A O     1 
ATOM   2343 C  CB    . ILE A 1 305 ? 26.285 -3.288  44.002  1.00 0.00 ? 304 ILE A CB    1 
ATOM   2344 C  CG1   . ILE A 1 305 ? 26.432 -3.950  45.372  1.00 0.00 ? 304 ILE A CG1   1 
ATOM   2345 C  CG2   . ILE A 1 305 ? 25.417 -2.049  44.230  1.00 0.00 ? 304 ILE A CG2   1 
ATOM   2346 C  CD1   . ILE A 1 305 ? 27.445 -3.241  46.273  1.00 0.00 ? 304 ILE A CD1   1 
ATOM   2347 N  N     . PRO A 1 306 ? 27.342 -3.197  41.426  1.00 0.00 ? 305 PRO A N     1 
ATOM   2348 C  CA    . PRO A 1 306 ? 27.800 -2.743  40.139  1.00 0.00 ? 305 PRO A CA    1 
ATOM   2349 C  C     . PRO A 1 306 ? 27.807 -3.899  39.173  1.00 0.00 ? 305 PRO A C     1 
ATOM   2350 O  O     . PRO A 1 306 ? 28.918 -4.423  38.849  1.00 0.00 ? 305 PRO A O     1 
ATOM   2351 C  CB    . PRO A 1 306 ? 29.184 -2.201  40.419  1.00 0.00 ? 305 PRO A CB    1 
ATOM   2352 C  CG    . PRO A 1 306 ? 29.460 -2.374  41.905  1.00 0.00 ? 305 PRO A CG    1 
ATOM   2353 C  CD    . PRO A 1 306 ? 28.268 -3.012  42.543  1.00 0.00 ? 305 PRO A CD    1 
ATOM   2354 N  N     . ALA A 1 307 ? 26.605 -4.280  38.741  1.00 0.00 ? 306 ALA A N     1 
ATOM   2355 C  CA    . ALA A 1 307 ? 26.438 -5.382  37.772  1.00 0.00 ? 306 ALA A CA    1 
ATOM   2356 C  C     . ALA A 1 307 ? 25.035 -6.016  37.827  1.00 0.00 ? 306 ALA A C     1 
ATOM   2357 O  O     . ALA A 1 307 ? 24.040 -5.339  38.125  1.00 0.00 ? 306 ALA A O     1 
ATOM   2358 C  CB    . ALA A 1 307 ? 27.453 -6.490  38.059  1.00 0.00 ? 306 ALA A CB    1 
ATOM   2359 N  N     . GLY A 1 308 ? 25.056 -7.312  37.533  1.00 0.00 ? 307 GLY A N     1 
ATOM   2360 C  CA    . GLY A 1 308 ? 23.864 -8.173  37.433  1.00 0.00 ? 307 GLY A CA    1 
ATOM   2361 C  C     . GLY A 1 308 ? 23.877 -8.803  36.039  1.00 0.00 ? 307 GLY A C     1 
ATOM   2362 O  O     . GLY A 1 308 ? 22.902 -8.696  35.281  1.00 0.00 ? 307 GLY A O     1 
ATOM   2363 N  N     . TRP A 1 309 ? 25.003 -9.424  35.794  1.00 0.00 ? 308 TRP A N     1 
ATOM   2364 C  CA    . TRP A 1 309 ? 25.359 -10.041 34.524  1.00 0.00 ? 308 TRP A CA    1 
ATOM   2365 C  C     . TRP A 1 309 ? 26.876 -10.289 34.598  1.00 0.00 ? 308 TRP A C     1 
ATOM   2366 O  O     . TRP A 1 309 ? 27.373 -11.341 34.168  1.00 0.00 ? 308 TRP A O     1 
ATOM   2367 C  CB    . TRP A 1 309 ? 24.989 -9.064  33.410  1.00 0.00 ? 308 TRP A CB    1 
ATOM   2368 C  CG    . TRP A 1 309 ? 24.094 -9.644  32.315  1.00 0.00 ? 308 TRP A CG    1 
ATOM   2369 C  CD1   . TRP A 1 309 ? 23.091 -10.532 32.441  1.00 0.00 ? 308 TRP A CD1   1 
ATOM   2370 C  CD2   . TRP A 1 309 ? 24.204 -9.299  30.955  1.00 0.00 ? 308 TRP A CD2   1 
ATOM   2371 N  NE1   . TRP A 1 309 ? 22.562 -10.752 31.123  1.00 0.00 ? 308 TRP A NE1   1 
ATOM   2372 C  CE2   . TRP A 1 309 ? 23.235 -10.017 30.268  1.00 0.00 ? 308 TRP A CE2   1 
ATOM   2373 C  CE3   . TRP A 1 309 ? 25.052 -8.439  30.256  1.00 0.00 ? 308 TRP A CE3   1 
ATOM   2374 C  CZ2   . TRP A 1 309 ? 23.066 -9.924  28.880  1.00 0.00 ? 308 TRP A CZ2   1 
ATOM   2375 C  CZ3   . TRP A 1 309 ? 24.874 -8.351  28.862  1.00 0.00 ? 308 TRP A CZ3   1 
ATOM   2376 C  CH2   . TRP A 1 309 ? 23.927 -9.059  28.207  1.00 0.00 ? 308 TRP A CH2   1 
ATOM   2377 N  N     . GLN A 1 310 ? 27.570 -9.266  35.151  1.00 0.00 ? 309 GLN A N     1 
ATOM   2378 C  CA    . GLN A 1 310 ? 29.016 -9.370  35.464  1.00 0.00 ? 309 GLN A CA    1 
ATOM   2379 C  C     . GLN A 1 310 ? 29.911 -8.087  35.145  1.00 0.00 ? 309 GLN A C     1 
ATOM   2380 O  O     . GLN A 1 310 ? 29.525 -6.948  35.450  1.00 0.00 ? 309 GLN A O     1 
ATOM   2381 C  CB    . GLN A 1 310 ? 29.602 -10.589 34.741  1.00 0.00 ? 309 GLN A CB    1 
ATOM   2382 C  CG    . GLN A 1 310 ? 28.850 -11.890 35.053  1.00 0.00 ? 309 GLN A CG    1 
ATOM   2383 C  CD    . GLN A 1 310 ? 29.469 -12.689 36.206  1.00 0.00 ? 309 GLN A CD    1 
ATOM   2384 O  OE1   . GLN A 1 310 ? 30.666 -12.571 36.463  1.00 0.00 ? 309 GLN A OE1   1 
ATOM   2385 N  NE2   . GLN A 1 310 ? 28.718 -13.505 36.922  1.00 0.00 ? 309 GLN A NE2   1 
ATOM   2386 N  N     . GLY A 1 311 ? 31.111 -8.357  34.511  1.00 0.00 ? 310 GLY A N     1 
ATOM   2387 C  CA    . GLY A 1 311 ? 32.263 -7.380  34.278  1.00 0.00 ? 310 GLY A CA    1 
ATOM   2388 C  C     . GLY A 1 311 ? 32.269 -6.550  32.953  1.00 0.00 ? 310 GLY A C     1 
ATOM   2389 O  O     . GLY A 1 311 ? 32.340 -5.311  32.972  1.00 0.00 ? 310 GLY A O     1 
ATOM   2390 N  N     . LEU A 1 312 ? 32.229 -7.176  31.781  1.00 0.00 ? 311 LEU A N     1 
ATOM   2391 C  CA    . LEU A 1 312 ? 32.191 -6.379  30.520  1.00 0.00 ? 311 LEU A CA    1 
ATOM   2392 C  C     . LEU A 1 312 ? 33.202 -6.853  29.459  1.00 0.00 ? 311 LEU A C     1 
ATOM   2393 O  O     . LEU A 1 312 ? 32.966 -7.838  28.745  1.00 0.00 ? 311 LEU A O     1 
ATOM   2394 C  CB    . LEU A 1 312 ? 32.527 -4.915  30.820  1.00 0.00 ? 311 LEU A CB    1 
ATOM   2395 C  CG    . LEU A 1 312 ? 31.497 -3.932  30.258  1.00 0.00 ? 311 LEU A CG    1 
ATOM   2396 C  CD1   . LEU A 1 312 ? 31.658 -3.691  28.756  1.00 0.00 ? 311 LEU A CD1   1 
ATOM   2397 C  CD2   . LEU A 1 312 ? 30.054 -4.402  30.451  1.00 0.00 ? 311 LEU A CD2   1 
ATOM   2398 N  N     . ASP A 1 313 ? 34.315 -6.129  29.385  1.00 0.00 ? 312 ASP A N     1 
ATOM   2399 C  CA    . ASP A 1 313 ? 35.361 -6.374  28.368  1.00 0.00 ? 312 ASP A CA    1 
ATOM   2400 C  C     . ASP A 1 313 ? 36.358 -7.460  28.769  1.00 0.00 ? 312 ASP A C     1 
ATOM   2401 O  O     . ASP A 1 313 ? 36.637 -7.662  29.960  1.00 0.00 ? 312 ASP A O     1 
ATOM   2402 C  CB    . ASP A 1 313 ? 36.197 -5.120  28.110  1.00 0.00 ? 312 ASP A CB    1 
ATOM   2403 C  CG    . ASP A 1 313 ? 37.457 -5.412  27.284  1.00 0.00 ? 312 ASP A CG    1 
ATOM   2404 O  OD1   . ASP A 1 313 ? 37.415 -5.343  25.997  1.00 0.00 ? 312 ASP A OD1   1 
ATOM   2405 O  OD2   . ASP A 1 313 ? 38.559 -5.726  27.877  1.00 0.00 ? 312 ASP A OD2   1 
ATOM   2406 N  N     . ASN A 1 314 ? 36.829 -8.095  27.710  1.00 0.00 ? 313 ASN A N     1 
ATOM   2407 C  CA    . ASN A 1 314 ? 37.858 -9.137  27.747  1.00 0.00 ? 313 ASN A CA    1 
ATOM   2408 C  C     . ASN A 1 314 ? 39.151 -8.484  28.280  1.00 0.00 ? 313 ASN A C     1 
ATOM   2409 O  O     . ASN A 1 314 ? 39.701 -7.559  27.664  1.00 0.00 ? 313 ASN A O     1 
ATOM   2410 C  CB    . ASN A 1 314 ? 38.031 -9.664  26.314  1.00 0.00 ? 313 ASN A CB    1 
ATOM   2411 C  CG    . ASN A 1 314 ? 38.856 -10.950 26.231  1.00 0.00 ? 313 ASN A CG    1 
ATOM   2412 O  OD1   . ASN A 1 314 ? 38.386 -12.010 26.640  1.00 0.00 ? 313 ASN A OD1   1 
ATOM   2413 N  ND2   . ASN A 1 314 ? 40.073 -10.921 25.720  1.00 0.00 ? 313 ASN A ND2   1 
ATOM   2414 N  N     . GLY A 1 315 ? 39.608 -8.991  29.421  1.00 0.00 ? 314 GLY A N     1 
ATOM   2415 C  CA    . GLY A 1 315 ? 40.775 -8.433  30.141  1.00 0.00 ? 314 GLY A CA    1 
ATOM   2416 C  C     . GLY A 1 315 ? 42.062 -9.231  29.907  1.00 0.00 ? 314 GLY A C     1 
ATOM   2417 O  O     . GLY A 1 315 ? 42.221 -9.900  28.875  1.00 0.00 ? 314 GLY A O     1 
ATOM   2418 N  N     . PRO A 1 316 ? 43.011 -9.181  30.861  1.00 0.00 ? 315 PRO A N     1 
ATOM   2419 C  CA    . PRO A 1 316 ? 44.291 -9.850  30.709  1.00 0.00 ? 315 PRO A CA    1 
ATOM   2420 C  C     . PRO A 1 316 ? 44.170 -11.339 30.532  1.00 0.00 ? 315 PRO A C     1 
ATOM   2421 O  O     . PRO A 1 316 ? 44.740 -11.891 29.540  1.00 0.00 ? 315 PRO A O     1 
ATOM   2422 C  CB    . PRO A 1 316 ? 45.021 -9.541  31.996  1.00 0.00 ? 315 PRO A CB    1 
ATOM   2423 C  CG    . PRO A 1 316 ? 44.106 -8.683  32.857  1.00 0.00 ? 315 PRO A CG    1 
ATOM   2424 C  CD    . PRO A 1 316 ? 42.825 -8.456  32.121  1.00 0.00 ? 315 PRO A CD    1 
ATOM   2425 N  N     . GLU A 1 317 ? 43.458 -11.963 31.451  1.00 0.00 ? 316 GLU A N     1 
ATOM   2426 C  CA    . GLU A 1 317 ? 43.285 -13.427 31.449  1.00 0.00 ? 316 GLU A CA    1 
ATOM   2427 C  C     . GLU A 1 317 ? 42.614 -13.873 30.167  1.00 0.00 ? 316 GLU A C     1 
ATOM   2428 O  O     . GLU A 1 317 ? 43.091 -14.789 29.481  1.00 0.00 ? 316 GLU A O     1 
ATOM   2429 C  CB    . GLU A 1 317 ? 42.405 -13.847 32.631  1.00 0.00 ? 316 GLU A CB    1 
ATOM   2430 C  CG    . GLU A 1 317 ? 42.455 -15.350 32.944  1.00 0.00 ? 316 GLU A CG    1 
ATOM   2431 C  CD    . GLU A 1 317 ? 43.192 -16.175 31.886  1.00 0.00 ? 316 GLU A CD    1 
ATOM   2432 O  OE1   . GLU A 1 317 ? 42.604 -16.476 30.778  1.00 0.00 ? 316 GLU A OE1   1 
ATOM   2433 O  OE2   . GLU A 1 317 ? 44.401 -16.571 32.103  1.00 0.00 ? 316 GLU A OE2   1 
ATOM   2434 N  N     . SER A 1 318 ? 41.531 -13.188 29.912  1.00 0.00 ? 317 SER A N     1 
ATOM   2435 C  CA    . SER A 1 318 ? 40.698 -13.425 28.749  1.00 0.00 ? 317 SER A CA    1 
ATOM   2436 C  C     . SER A 1 318 ? 41.550 -13.276 27.498  1.00 0.00 ? 317 SER A C     1 
ATOM   2437 O  O     . SER A 1 318 ? 41.483 -14.104 26.577  1.00 0.00 ? 317 SER A O     1 
ATOM   2438 C  CB    . SER A 1 318 ? 39.528 -12.441 28.747  1.00 0.00 ? 317 SER A CB    1 
ATOM   2439 O  OG    . SER A 1 318 ? 38.680 -12.695 29.858  1.00 0.00 ? 317 SER A OG    1 
ATOM   2440 N  N     . ARG A 1 319 ? 42.337 -12.217 27.485  1.00 0.00 ? 318 ARG A N     1 
ATOM   2441 C  CA    . ARG A 1 319 ? 43.198 -11.934 26.337  1.00 0.00 ? 318 ARG A CA    1 
ATOM   2442 C  C     . ARG A 1 319 ? 44.128 -13.093 26.056  1.00 0.00 ? 318 ARG A C     1 
ATOM   2443 O  O     . ARG A 1 319 ? 44.228 -13.571 24.916  1.00 0.00 ? 318 ARG A O     1 
ATOM   2444 C  CB    . ARG A 1 319 ? 44.097 -10.711 26.581  1.00 0.00 ? 318 ARG A CB    1 
ATOM   2445 C  CG    . ARG A 1 319 ? 45.415 -10.771 25.788  1.00 0.00 ? 318 ARG A CG    1 
ATOM   2446 C  CD    . ARG A 1 319 ? 46.036 -9.392  25.523  1.00 0.00 ? 318 ARG A CD    1 
ATOM   2447 N  NE    . ARG A 1 319 ? 47.030 -8.999  26.538  1.00 0.00 ? 318 ARG A NE    1 
ATOM   2448 C  CZ    . ARG A 1 319 ? 48.043 -8.145  26.319  1.00 0.00 ? 318 ARG A CZ    1 
ATOM   2449 N  NH1   . ARG A 1 319 ? 48.220 -7.576  25.118  1.00 0.00 ? 318 ARG A NH1   1 
ATOM   2450 N  NH2   . ARG A 1 319 ? 48.940 -7.791  27.250  1.00 0.00 ? 318 ARG A NH2   1 
ATOM   2451 N  N     . LYS A 1 320 ? 44.800 -13.546 27.075  1.00 0.00 ? 319 LYS A N     1 
ATOM   2452 C  CA    . LYS A 1 320 ? 45.774 -14.614 26.885  1.00 0.00 ? 319 LYS A CA    1 
ATOM   2453 C  C     . LYS A 1 320 ? 45.132 -15.885 26.344  1.00 0.00 ? 319 LYS A C     1 
ATOM   2454 O  O     . LYS A 1 320 ? 45.572 -16.440 25.326  1.00 0.00 ? 319 LYS A O     1 
ATOM   2455 C  CB    . LYS A 1 320 ? 46.465 -14.954 28.205  1.00 0.00 ? 319 LYS A CB    1 
ATOM   2456 C  CG    . LYS A 1 320 ? 47.992 -15.015 28.082  1.00 0.00 ? 319 LYS A CG    1 
ATOM   2457 C  CD    . LYS A 1 320 ? 48.716 -14.513 29.335  1.00 0.00 ? 319 LYS A CD    1 
ATOM   2458 C  CE    . LYS A 1 320 ? 50.241 -14.570 29.212  1.00 0.00 ? 319 LYS A CE    1 
ATOM   2459 N  NZ    . LYS A 1 320 ? 50.933 -14.097 30.419  1.00 0.00 ? 319 LYS A NZ    1 
ATOM   2460 N  N     . LEU A 1 321 ? 44.097 -16.337 27.011  1.00 0.00 ? 320 LEU A N     1 
ATOM   2461 C  CA    . LEU A 1 321 ? 43.456 -17.582 26.609  1.00 0.00 ? 320 LEU A CA    1 
ATOM   2462 C  C     . LEU A 1 321 ? 43.035 -17.454 25.168  1.00 0.00 ? 320 LEU A C     1 
ATOM   2463 O  O     . LEU A 1 321 ? 43.251 -18.366 24.356  1.00 0.00 ? 320 LEU A O     1 
ATOM   2464 C  CB    . LEU A 1 321 ? 42.233 -17.906 27.467  1.00 0.00 ? 320 LEU A CB    1 
ATOM   2465 C  CG    . LEU A 1 321 ? 41.493 -19.165 26.987  1.00 0.00 ? 320 LEU A CG    1 
ATOM   2466 C  CD1   . LEU A 1 321 ? 41.132 -19.116 25.501  1.00 0.00 ? 320 LEU A CD1   1 
ATOM   2467 C  CD2   . LEU A 1 321 ? 42.308 -20.447 27.172  1.00 0.00 ? 320 LEU A CD2   1 
ATOM   2468 N  N     . PHE A 1 322 ? 42.440 -16.323 24.877  1.00 0.00 ? 321 PHE A N     1 
ATOM   2469 C  CA    . PHE A 1 322 ? 41.950 -16.055 23.530  1.00 0.00 ? 321 PHE A CA    1 
ATOM   2470 C  C     . PHE A 1 322 ? 43.083 -16.189 22.553  1.00 0.00 ? 321 PHE A C     1 
ATOM   2471 O  O     . PHE A 1 322 ? 42.984 -16.918 21.556  1.00 0.00 ? 321 PHE A O     1 
ATOM   2472 C  CB    . PHE A 1 322 ? 41.444 -14.627 23.457  1.00 0.00 ? 321 PHE A CB    1 
ATOM   2473 C  CG    . PHE A 1 322 ? 40.062 -14.505 24.049  1.00 0.00 ? 321 PHE A CG    1 
ATOM   2474 C  CD1   . PHE A 1 322 ? 39.447 -13.257 24.134  1.00 0.00 ? 321 PHE A CD1   1 
ATOM   2475 C  CD2   . PHE A 1 322 ? 39.421 -15.658 24.502  1.00 0.00 ? 321 PHE A CD2   1 
ATOM   2476 C  CE1   . PHE A 1 322 ? 38.162 -13.161 24.673  1.00 0.00 ? 321 PHE A CE1   1 
ATOM   2477 C  CE2   . PHE A 1 322 ? 38.138 -15.564 25.040  1.00 0.00 ? 321 PHE A CE2   1 
ATOM   2478 C  CZ    . PHE A 1 322 ? 37.506 -14.316 25.123  1.00 0.00 ? 321 PHE A CZ    1 
ATOM   2479 N  N     . ALA A 1 323 ? 44.104 -15.472 22.896  1.00 0.00 ? 322 ALA A N     1 
ATOM   2480 C  CA    . ALA A 1 323 ? 45.339 -15.516 22.179  1.00 0.00 ? 322 ALA A CA    1 
ATOM   2481 C  C     . ALA A 1 323 ? 45.797 -16.952 22.233  1.00 0.00 ? 322 ALA A C     1 
ATOM   2482 O  O     . ALA A 1 323 ? 46.290 -17.503 21.237  1.00 0.00 ? 322 ALA A O     1 
ATOM   2483 C  CB    . ALA A 1 323 ? 46.364 -14.590 22.839  1.00 0.00 ? 322 ALA A CB    1 
ATOM   2484 N  N     . ALA A 1 324 ? 45.617 -17.509 23.423  1.00 0.00 ? 323 ALA A N     1 
ATOM   2485 C  CA    . ALA A 1 324 ? 46.115 -18.854 23.728  1.00 0.00 ? 323 ALA A CA    1 
ATOM   2486 C  C     . ALA A 1 324 ? 45.587 -19.903 22.752  1.00 0.00 ? 323 ALA A C     1 
ATOM   2487 O  O     . ALA A 1 324 ? 46.365 -20.609 22.093  1.00 0.00 ? 323 ALA A O     1 
ATOM   2488 C  CB    . ALA A 1 324 ? 45.668 -19.265 25.133  1.00 0.00 ? 323 ALA A CB    1 
ATOM   2489 N  N     . THR A 1 325 ? 44.281 -20.000 22.668  1.00 0.00 ? 324 THR A N     1 
ATOM   2490 C  CA    . THR A 1 325 ? 43.636 -20.879 21.693  1.00 0.00 ? 324 THR A CA    1 
ATOM   2491 C  C     . THR A 1 325 ? 44.002 -20.371 20.315  1.00 0.00 ? 324 THR A C     1 
ATOM   2492 O  O     . THR A 1 325 ? 44.246 -21.157 19.387  1.00 0.00 ? 324 THR A O     1 
ATOM   2493 C  CB    . THR A 1 325 ? 42.129 -20.989 21.902  1.00 0.00 ? 324 THR A CB    1 
ATOM   2494 O  OG1   . THR A 1 325 ? 41.858 -21.608 23.152  1.00 0.00 ? 324 THR A OG1   1 
ATOM   2495 C  CG2   . THR A 1 325 ? 41.437 -21.822 20.820  1.00 0.00 ? 324 THR A CG2   1 
ATOM   2496 N  N     . VAL A 1 326 ? 44.027 -19.053 20.220  1.00 0.00 ? 325 VAL A N     1 
ATOM   2497 C  CA    . VAL A 1 326 ? 44.269 -18.390 18.947  1.00 0.00 ? 325 VAL A CA    1 
ATOM   2498 C  C     . VAL A 1 326 ? 45.478 -19.027 18.315  1.00 0.00 ? 325 VAL A C     1 
ATOM   2499 O  O     . VAL A 1 326 ? 45.454 -19.412 17.136  1.00 0.00 ? 325 VAL A O     1 
ATOM   2500 C  CB    . VAL A 1 326 ? 44.589 -16.912 19.185  1.00 0.00 ? 325 VAL A CB    1 
ATOM   2501 C  CG1   . VAL A 1 326 ? 45.161 -16.218 17.948  1.00 0.00 ? 325 VAL A CG1   1 
ATOM   2502 C  CG2   . VAL A 1 326 ? 43.364 -16.091 19.592  1.00 0.00 ? 325 VAL A CG2   1 
ATOM   2503 N  N     . ALA A 1 327 ? 46.510 -19.128 19.092  1.00 0.00 ? 326 ALA A N     1 
ATOM   2504 C  CA    . ALA A 1 327 ? 47.673 -19.851 18.655  1.00 0.00 ? 326 ALA A CA    1 
ATOM   2505 C  C     . ALA A 1 327 ? 47.293 -21.304 18.816  1.00 0.00 ? 326 ALA A C     1 
ATOM   2506 O  O     . ALA A 1 327 ? 47.278 -21.839 19.934  1.00 0.00 ? 326 ALA A O     1 
ATOM   2507 C  CB    . ALA A 1 327 ? 48.877 -19.487 19.525  1.00 0.00 ? 326 ALA A CB    1 
ATOM   2508 N  N     . LYS A 1 328 ? 46.982 -21.906 17.712  1.00 0.00 ? 327 LYS A N     1 
ATOM   2509 C  CA    . LYS A 1 328 ? 46.544 -23.290 17.695  1.00 0.00 ? 327 LYS A CA    1 
ATOM   2510 C  C     . LYS A 1 328 ? 45.604 -23.486 16.512  1.00 0.00 ? 327 LYS A C     1 
ATOM   2511 O  O     . LYS A 1 328 ? 44.379 -23.335 16.640  1.00 0.00 ? 327 LYS A O     1 
ATOM   2512 C  CB    . LYS A 1 328 ? 45.794 -23.616 18.989  1.00 0.00 ? 327 LYS A CB    1 
ATOM   2513 C  CG    . LYS A 1 328 ? 46.718 -24.018 20.139  1.00 0.00 ? 327 LYS A CG    1 
ATOM   2514 C  CD    . LYS A 1 328 ? 45.954 -24.448 21.393  1.00 0.00 ? 327 LYS A CD    1 
ATOM   2515 C  CE    . LYS A 1 328 ? 46.875 -24.840 22.551  1.00 0.00 ? 327 LYS A CE    1 
ATOM   2516 N  NZ    . LYS A 1 328 ? 46.183 -24.878 23.847  1.00 0.00 ? 327 LYS A NZ    1 
ATOM   2517 N  N     . ALA A 1 329 ? 46.273 -23.812 15.427  1.00 0.00 ? 328 ALA A N     1 
ATOM   2518 C  CA    . ALA A 1 329 ? 45.690 -24.084 14.108  1.00 0.00 ? 328 ALA A CA    1 
ATOM   2519 C  C     . ALA A 1 329 ? 44.213 -23.745 14.059  1.00 0.00 ? 328 ALA A C     1 
ATOM   2520 O  O     . ALA A 1 329 ? 43.820 -22.575 14.175  1.00 0.00 ? 328 ALA A O     1 
ATOM   2521 C  CB    . ALA A 1 329 ? 45.845 -25.565 13.761  1.00 0.00 ? 328 ALA A CB    1 
ATOM   2522 N  N     . THR A 1 330 ? 43.420 -24.782 13.892  1.00 0.00 ? 329 THR A N     1 
ATOM   2523 C  CA    . THR A 1 330 ? 41.991 -24.589 13.754  1.00 0.00 ? 329 THR A CA    1 
ATOM   2524 C  C     . THR A 1 330 ? 41.775 -23.374 12.873  1.00 0.00 ? 329 THR A C     1 
ATOM   2525 O  O     . THR A 1 330 ? 42.629 -22.477 12.802  1.00 0.00 ? 329 THR A O     1 
ATOM   2526 C  CB    . THR A 1 330 ? 41.382 -24.248 15.116  1.00 0.00 ? 329 THR A CB    1 
ATOM   2527 O  OG1   . THR A 1 330 ? 40.148 -24.932 15.281  1.00 0.00 ? 329 THR A OG1   1 
ATOM   2528 C  CG2   . THR A 1 330 ? 41.103 -22.754 15.289  1.00 0.00 ? 329 THR A CG2   1 
ATOM   2529 N  N     . VAL A 1 331 ? 40.658 -23.352 12.196  1.00 0.00 ? 330 VAL A N     1 
ATOM   2530 C  CA    . VAL A 1 331 ? 40.281 -22.158 11.454  1.00 0.00 ? 330 VAL A CA    1 
ATOM   2531 C  C     . VAL A 1 331 ? 39.663 -21.230 12.481  1.00 0.00 ? 330 VAL A C     1 
ATOM   2532 O  O     . VAL A 1 331 ? 39.125 -21.680 13.504  1.00 0.00 ? 330 VAL A O     1 
ATOM   2533 C  CB    . VAL A 1 331 ? 39.273 -22.477 10.353  1.00 0.00 ? 330 VAL A CB    1 
ATOM   2534 C  CG1   . VAL A 1 331 ? 39.744 -23.590 9.415   1.00 0.00 ? 330 VAL A CG1   1 
ATOM   2535 C  CG2   . VAL A 1 331 ? 37.920 -22.937 10.897  1.00 0.00 ? 330 VAL A CG2   1 
ATOM   2536 N  N     . ILE A 1 332 ? 39.743 -19.957 12.212  1.00 0.00 ? 331 ILE A N     1 
ATOM   2537 C  CA    . ILE A 1 332 ? 39.239 -18.952 13.151  1.00 0.00 ? 331 ILE A CA    1 
ATOM   2538 C  C     . ILE A 1 332 ? 38.167 -18.050 12.553  1.00 0.00 ? 331 ILE A C     1 
ATOM   2539 O  O     . ILE A 1 332 ? 38.417 -17.315 11.587  1.00 0.00 ? 331 ILE A O     1 
ATOM   2540 C  CB    . ILE A 1 332 ? 40.382 -18.140 13.693  1.00 0.00 ? 331 ILE A CB    1 
ATOM   2541 C  CG1   . ILE A 1 332 ? 41.384 -19.025 14.430  1.00 0.00 ? 331 ILE A CG1   1 
ATOM   2542 C  CG2   . ILE A 1 332 ? 39.931 -17.063 14.680  1.00 0.00 ? 331 ILE A CG2   1 
ATOM   2543 C  CD1   . ILE A 1 332 ? 42.545 -18.237 15.038  1.00 0.00 ? 331 ILE A CD1   1 
ATOM   2544 N  N     . LEU A 1 333 ? 37.020 -18.189 13.193  1.00 0.00 ? 332 LEU A N     1 
ATOM   2545 C  CA    . LEU A 1 333 ? 35.790 -17.461 12.886  1.00 0.00 ? 332 LEU A CA    1 
ATOM   2546 C  C     . LEU A 1 333 ? 35.313 -16.633 14.066  1.00 0.00 ? 332 LEU A C     1 
ATOM   2547 O  O     . LEU A 1 333 ? 35.035 -17.165 15.150  1.00 0.00 ? 332 LEU A O     1 
ATOM   2548 C  CB    . LEU A 1 333 ? 34.715 -18.405 12.439  1.00 0.00 ? 332 LEU A CB    1 
ATOM   2549 C  CG    . LEU A 1 333 ? 34.750 -18.560 10.928  1.00 0.00 ? 332 LEU A CG    1 
ATOM   2550 C  CD1   . LEU A 1 333 ? 35.698 -19.668 10.466  1.00 0.00 ? 332 LEU A CD1   1 
ATOM   2551 C  CD2   . LEU A 1 333 ? 33.385 -18.902 10.330  1.00 0.00 ? 332 LEU A CD2   1 
ATOM   2552 N  N     . TRP A 1 334 ? 35.262 -15.384 13.732  1.00 0.00 ? 333 TRP A N     1 
ATOM   2553 C  CA    . TRP A 1 334 ? 34.934 -14.292 14.613  1.00 0.00 ? 333 TRP A CA    1 
ATOM   2554 C  C     . TRP A 1 334 ? 33.698 -13.480 14.164  1.00 0.00 ? 333 TRP A C     1 
ATOM   2555 O  O     . TRP A 1 334 ? 33.679 -12.899 13.069  1.00 0.00 ? 333 TRP A O     1 
ATOM   2556 C  CB    . TRP A 1 334 ? 36.112 -13.430 14.570  1.00 0.00 ? 333 TRP A CB    1 
ATOM   2557 C  CG    . TRP A 1 334 ? 36.288 -12.620 15.778  1.00 0.00 ? 333 TRP A CG    1 
ATOM   2558 C  CD1   . TRP A 1 334 ? 35.707 -12.765 16.976  1.00 0.00 ? 333 TRP A CD1   1 
ATOM   2559 C  CD2   . TRP A 1 334 ? 37.138 -11.560 15.781  1.00 0.00 ? 333 TRP A CD2   1 
ATOM   2560 N  NE1   . TRP A 1 334 ? 36.222 -11.695 17.777  1.00 0.00 ? 333 TRP A NE1   1 
ATOM   2561 C  CE2   . TRP A 1 334 ? 37.060 -10.993 17.034  1.00 0.00 ? 333 TRP A CE2   1 
ATOM   2562 C  CE3   . TRP A 1 334 ? 37.959 -11.024 14.804  1.00 0.00 ? 333 TRP A CE3   1 
ATOM   2563 C  CZ2   . TRP A 1 334 ? 37.783 -9.845  17.369  1.00 0.00 ? 333 TRP A CZ2   1 
ATOM   2564 C  CZ3   . TRP A 1 334 ? 38.686 -9.881  15.149  1.00 0.00 ? 333 TRP A CZ3   1 
ATOM   2565 C  CH2   . TRP A 1 334 ? 38.600 -9.316  16.373  1.00 0.00 ? 333 TRP A CH2   1 
ATOM   2566 N  N     . ASN A 1 335 ? 32.690 -13.467 15.023  1.00 0.00 ? 334 ASN A N     1 
ATOM   2567 C  CA    . ASN A 1 335 ? 31.433 -12.717 14.787  1.00 0.00 ? 334 ASN A CA    1 
ATOM   2568 C  C     . ASN A 1 335 ? 31.490 -11.284 15.384  1.00 0.00 ? 334 ASN A C     1 
ATOM   2569 O  O     . ASN A 1 335 ? 32.024 -10.353 14.761  1.00 0.00 ? 334 ASN A O     1 
ATOM   2570 C  CB    . ASN A 1 335 ? 30.264 -13.468 15.430  1.00 0.00 ? 334 ASN A CB    1 
ATOM   2571 C  CG    . ASN A 1 335 ? 29.030 -12.594 15.659  1.00 0.00 ? 334 ASN A CG    1 
ATOM   2572 O  OD1   . ASN A 1 335 ? 28.483 -12.579 16.760  1.00 0.00 ? 334 ASN A OD1   1 
ATOM   2573 N  ND2   . ASN A 1 335 ? 28.551 -11.856 14.674  1.00 0.00 ? 334 ASN A ND2   1 
ATOM   2574 N  N     . GLY A 1 336 ? 30.933 -11.168 16.588  1.00 0.00 ? 335 GLY A N     1 
ATOM   2575 C  CA    . GLY A 1 336 ? 30.802 -9.884  17.315  1.00 0.00 ? 335 GLY A CA    1 
ATOM   2576 C  C     . GLY A 1 336 ? 32.073 -9.508  18.094  1.00 0.00 ? 335 GLY A C     1 
ATOM   2577 O  O     . GLY A 1 336 ? 33.051 -10.269 18.125  1.00 0.00 ? 335 GLY A O     1 
ATOM   2578 N  N     . PRO A 1 337 ? 32.072 -8.322  18.738  1.00 0.00 ? 336 PRO A N     1 
ATOM   2579 C  CA    . PRO A 1 337 ? 33.224 -7.832  19.502  1.00 0.00 ? 336 PRO A CA    1 
ATOM   2580 C  C     . PRO A 1 337 ? 33.598 -8.780  20.625  1.00 0.00 ? 336 PRO A C     1 
ATOM   2581 O  O     . PRO A 1 337 ? 32.709 -9.554  21.101  1.00 0.00 ? 336 PRO A O     1 
ATOM   2582 C  CB    . PRO A 1 337 ? 32.761 -6.490  20.027  1.00 0.00 ? 336 PRO A CB    1 
ATOM   2583 C  CG    . PRO A 1 337 ? 31.338 -6.255  19.537  1.00 0.00 ? 336 PRO A CG    1 
ATOM   2584 C  CD    . PRO A 1 337 ? 30.909 -7.429  18.717  1.00 0.00 ? 336 PRO A CD    1 
ATOM   2585 N  N     . PRO A 1 338 ? 34.875 -8.784  21.099  1.00 0.00 ? 337 PRO A N     1 
ATOM   2586 C  CA    . PRO A 1 338 ? 35.262 -9.665  22.173  1.00 0.00 ? 337 PRO A CA    1 
ATOM   2587 C  C     . PRO A 1 338 ? 34.364 -9.328  23.281  1.00 0.00 ? 337 PRO A C     1 
ATOM   2588 O  O     . PRO A 1 338 ? 34.173 -10.182 24.201  1.00 0.00 ? 337 PRO A O     1 
ATOM   2589 C  CB    . PRO A 1 338 ? 36.713 -9.321  22.426  1.00 0.00 ? 337 PRO A CB    1 
ATOM   2590 C  CG    . PRO A 1 338 ? 37.108 -8.230  21.442  1.00 0.00 ? 337 PRO A CG    1 
ATOM   2591 C  CD    . PRO A 1 338 ? 35.926 -7.905  20.583  1.00 0.00 ? 337 PRO A CD    1 
ATOM   2592 N  N     . GLY A 1 339 ? 33.889 -8.137  23.098  1.00 0.00 ? 338 GLY A N     1 
ATOM   2593 C  CA    . GLY A 1 339 ? 32.966 -7.497  23.995  1.00 0.00 ? 338 GLY A CA    1 
ATOM   2594 C  C     . GLY A 1 339 ? 32.751 -6.088  23.508  1.00 0.00 ? 338 GLY A C     1 
ATOM   2595 O  O     . GLY A 1 339 ? 32.654 -5.837  22.297  1.00 0.00 ? 338 GLY A O     1 
ATOM   2596 N  N     . VAL A 1 340 ? 32.673 -5.216  24.463  1.00 0.00 ? 339 VAL A N     1 
ATOM   2597 C  CA    . VAL A 1 340 ? 32.493 -3.800  24.196  1.00 0.00 ? 339 VAL A CA    1 
ATOM   2598 C  C     . VAL A 1 340 ? 33.840 -3.233  23.760  1.00 0.00 ? 339 VAL A C     1 
ATOM   2599 O  O     . VAL A 1 340 ? 34.590 -2.670  24.571  1.00 0.00 ? 339 VAL A O     1 
ATOM   2600 C  CB    . VAL A 1 340 ? 31.998 -3.120  25.462  1.00 0.00 ? 339 VAL A CB    1 
ATOM   2601 C  CG1   . VAL A 1 340 ? 32.743 -1.820  25.770  1.00 0.00 ? 339 VAL A CG1   1 
ATOM   2602 C  CG2   . VAL A 1 340 ? 30.516 -2.745  25.395  1.00 0.00 ? 339 VAL A CG2   1 
ATOM   2603 N  N     . PHE A 1 341 ? 34.089 -3.400  22.481  1.00 0.00 ? 340 PHE A N     1 
ATOM   2604 C  CA    . PHE A 1 341 ? 35.369 -3.052  21.842  1.00 0.00 ? 340 PHE A CA    1 
ATOM   2605 C  C     . PHE A 1 341 ? 35.455 -1.569  21.454  1.00 0.00 ? 340 PHE A C     1 
ATOM   2606 O  O     . PHE A 1 341 ? 36.535 -1.056  21.126  1.00 0.00 ? 340 PHE A O     1 
ATOM   2607 C  CB    . PHE A 1 341 ? 35.533 -3.925  20.586  1.00 0.00 ? 340 PHE A CB    1 
ATOM   2608 C  CG    . PHE A 1 341 ? 34.735 -3.435  19.366  1.00 0.00 ? 340 PHE A CG    1 
ATOM   2609 C  CD1   . PHE A 1 341 ? 35.383 -2.696  18.372  1.00 0.00 ? 340 PHE A CD1   1 
ATOM   2610 C  CD2   . PHE A 1 341 ? 33.367 -3.727  19.233  1.00 0.00 ? 340 PHE A CD2   1 
ATOM   2611 C  CE1   . PHE A 1 341 ? 34.673 -2.245  17.252  1.00 0.00 ? 340 PHE A CE1   1 
ATOM   2612 C  CE2   . PHE A 1 341 ? 32.654 -3.277  18.110  1.00 0.00 ? 340 PHE A CE2   1 
ATOM   2613 C  CZ    . PHE A 1 341 ? 33.309 -2.534  17.120  1.00 0.00 ? 340 PHE A CZ    1 
ATOM   2614 N  N     . GLU A 1 342 ? 34.315 -0.931  21.521  1.00 0.00 ? 341 GLU A N     1 
ATOM   2615 C  CA    . GLU A 1 342 ? 34.157 0.463   21.118  1.00 0.00 ? 341 GLU A CA    1 
ATOM   2616 C  C     . GLU A 1 342 ? 34.204 1.433   22.294  1.00 0.00 ? 341 GLU A C     1 
ATOM   2617 O  O     . GLU A 1 342 ? 34.004 2.646   22.131  1.00 0.00 ? 341 GLU A O     1 
ATOM   2618 C  CB    . GLU A 1 342 ? 32.793 0.639   20.483  1.00 0.00 ? 341 GLU A CB    1 
ATOM   2619 C  CG    . GLU A 1 342 ? 31.701 -0.064  21.288  1.00 0.00 ? 341 GLU A CG    1 
ATOM   2620 C  CD    . GLU A 1 342 ? 30.727 -0.843  20.410  1.00 0.00 ? 341 GLU A CD    1 
ATOM   2621 O  OE1   . GLU A 1 342 ? 30.499 -2.090  20.649  1.00 0.00 ? 341 GLU A OE1   1 
ATOM   2622 O  OE2   . GLU A 1 342 ? 30.132 -0.253  19.430  1.00 0.00 ? 341 GLU A OE2   1 
ATOM   2623 N  N     . PHE A 1 343 ? 34.451 0.935   23.474  1.00 0.00 ? 342 PHE A N     1 
ATOM   2624 C  CA    . PHE A 1 343 ? 34.519 1.817   24.644  1.00 0.00 ? 342 PHE A CA    1 
ATOM   2625 C  C     . PHE A 1 343 ? 35.868 1.612   25.344  1.00 0.00 ? 342 PHE A C     1 
ATOM   2626 O  O     . PHE A 1 343 ? 35.949 0.962   26.397  1.00 0.00 ? 342 PHE A O     1 
ATOM   2627 C  CB    . PHE A 1 343 ? 33.290 1.600   25.542  1.00 0.00 ? 342 PHE A CB    1 
ATOM   2628 C  CG    . PHE A 1 343 ? 32.251 2.739   25.384  1.00 0.00 ? 342 PHE A CG    1 
ATOM   2629 C  CD1   . PHE A 1 343 ? 32.304 3.593   24.268  1.00 0.00 ? 342 PHE A CD1   1 
ATOM   2630 C  CD2   . PHE A 1 343 ? 31.250 2.940   26.348  1.00 0.00 ? 342 PHE A CD2   1 
ATOM   2631 C  CE1   . PHE A 1 343 ? 31.376 4.637   24.125  1.00 0.00 ? 342 PHE A CE1   1 
ATOM   2632 C  CE2   . PHE A 1 343 ? 30.322 3.985   26.203  1.00 0.00 ? 342 PHE A CE2   1 
ATOM   2633 C  CZ    . PHE A 1 343 ? 30.388 4.834   25.093  1.00 0.00 ? 342 PHE A CZ    1 
ATOM   2634 N  N     . GLU A 1 344 ? 36.853 2.207   24.673  1.00 0.00 ? 343 GLU A N     1 
ATOM   2635 C  CA    . GLU A 1 344 ? 38.272 2.213   25.066  1.00 0.00 ? 343 GLU A CA    1 
ATOM   2636 C  C     . GLU A 1 344 ? 38.403 2.078   26.582  1.00 0.00 ? 343 GLU A C     1 
ATOM   2637 O  O     . GLU A 1 344 ? 37.730 2.784   27.347  1.00 0.00 ? 343 GLU A O     1 
ATOM   2638 C  CB    . GLU A 1 344 ? 38.913 3.525   24.617  1.00 0.00 ? 343 GLU A CB    1 
ATOM   2639 C  CG    . GLU A 1 344 ? 39.706 3.381   23.323  1.00 0.00 ? 343 GLU A CG    1 
ATOM   2640 C  CD    . GLU A 1 344 ? 41.020 2.630   23.525  1.00 0.00 ? 343 GLU A CD    1 
ATOM   2641 O  OE1   . GLU A 1 344 ? 42.139 3.196   23.224  1.00 0.00 ? 343 GLU A OE1   1 
ATOM   2642 O  OE2   . GLU A 1 344 ? 41.010 1.429   23.997  1.00 0.00 ? 343 GLU A OE2   1 
ATOM   2643 N  N     . LYS A 1 345 ? 39.285 1.182   26.980  1.00 0.00 ? 344 LYS A N     1 
ATOM   2644 C  CA    . LYS A 1 345 ? 39.500 0.866   28.401  1.00 0.00 ? 344 LYS A CA    1 
ATOM   2645 C  C     . LYS A 1 345 ? 38.935 -0.521  28.626  1.00 0.00 ? 344 LYS A C     1 
ATOM   2646 O  O     . LYS A 1 345 ? 39.548 -1.358  29.306  1.00 0.00 ? 344 LYS A O     1 
ATOM   2647 C  CB    . LYS A 1 345 ? 38.727 1.884   29.261  1.00 0.00 ? 344 LYS A CB    1 
ATOM   2648 C  CG    . LYS A 1 345 ? 39.463 2.324   30.534  1.00 0.00 ? 344 LYS A CG    1 
ATOM   2649 C  CD    . LYS A 1 345 ? 38.647 3.308   31.387  1.00 0.00 ? 344 LYS A CD    1 
ATOM   2650 C  CE    . LYS A 1 345 ? 39.301 3.633   32.734  1.00 0.00 ? 344 LYS A CE    1 
ATOM   2651 N  NZ    . LYS A 1 345 ? 38.529 4.598   33.531  1.00 0.00 ? 344 LYS A NZ    1 
ATOM   2652 N  N     . PHE A 1 346 ? 37.787 -0.624  28.011  1.00 0.00 ? 345 PHE A N     1 
ATOM   2653 C  CA    . PHE A 1 346 ? 36.959 -1.807  27.965  1.00 0.00 ? 345 PHE A CA    1 
ATOM   2654 C  C     . PHE A 1 346 ? 36.936 -2.262  26.492  1.00 0.00 ? 345 PHE A C     1 
ATOM   2655 O  O     . PHE A 1 346 ? 35.926 -2.788  26.001  1.00 0.00 ? 345 PHE A O     1 
ATOM   2656 C  CB    . PHE A 1 346 ? 35.582 -1.436  28.543  1.00 0.00 ? 345 PHE A CB    1 
ATOM   2657 C  CG    . PHE A 1 346 ? 35.672 -0.857  29.975  1.00 0.00 ? 345 PHE A CG    1 
ATOM   2658 C  CD1   . PHE A 1 346 ? 34.719 0.070   30.438  1.00 0.00 ? 345 PHE A CD1   1 
ATOM   2659 C  CD2   . PHE A 1 346 ? 36.711 -1.254  30.830  1.00 0.00 ? 345 PHE A CD2   1 
ATOM   2660 C  CE1   . PHE A 1 346 ? 34.805 0.583   31.744  1.00 0.00 ? 345 PHE A CE1   1 
ATOM   2661 C  CE2   . PHE A 1 346 ? 36.794 -0.740  32.133  1.00 0.00 ? 345 PHE A CE2   1 
ATOM   2662 C  CZ    . PHE A 1 346 ? 35.841 0.176   32.591  1.00 0.00 ? 345 PHE A CZ    1 
ATOM   2663 N  N     . ALA A 1 347 ? 38.098 -2.018  25.868  1.00 0.00 ? 346 ALA A N     1 
ATOM   2664 C  CA    . ALA A 1 347 ? 38.383 -2.343  24.452  1.00 0.00 ? 346 ALA A CA    1 
ATOM   2665 C  C     . ALA A 1 347 ? 39.896 -2.216  24.168  1.00 0.00 ? 346 ALA A C     1 
ATOM   2666 O  O     . ALA A 1 347 ? 40.334 -1.320  23.432  1.00 0.00 ? 346 ALA A O     1 
ATOM   2667 C  CB    . ALA A 1 347 ? 37.635 -1.373  23.533  1.00 0.00 ? 346 ALA A CB    1 
ATOM   2668 N  N     . ALA A 1 348 ? 40.666 -3.126  24.762  1.00 0.00 ? 347 ALA A N     1 
ATOM   2669 C  CA    . ALA A 1 348 ? 42.143 -3.142  24.616  1.00 0.00 ? 347 ALA A CA    1 
ATOM   2670 C  C     . ALA A 1 348 ? 42.652 -4.546  24.288  1.00 0.00 ? 347 ALA A C     1 
ATOM   2671 O  O     . ALA A 1 348 ? 43.264 -4.775  23.234  1.00 0.00 ? 347 ALA A O     1 
ATOM   2672 C  CB    . ALA A 1 348 ? 42.803 -2.685  25.919  1.00 0.00 ? 347 ALA A CB    1 
ATOM   2673 N  N     . GLY A 1 349 ? 42.368 -5.427  25.210  1.00 0.00 ? 348 GLY A N     1 
ATOM   2674 C  CA    . GLY A 1 349 ? 42.744 -6.826  25.112  1.00 0.00 ? 348 GLY A CA    1 
ATOM   2675 C  C     . GLY A 1 349 ? 42.249 -7.324  23.774  1.00 0.00 ? 348 GLY A C     1 
ATOM   2676 O  O     . GLY A 1 349 ? 42.922 -8.116  23.096  1.00 0.00 ? 348 GLY A O     1 
ATOM   2677 N  N     . THR A 1 350 ? 41.088 -6.826  23.462  1.00 0.00 ? 349 THR A N     1 
ATOM   2678 C  CA    . THR A 1 350 ? 40.346 -7.194  22.267  1.00 0.00 ? 349 THR A CA    1 
ATOM   2679 C  C     . THR A 1 350 ? 41.196 -7.081  20.999  1.00 0.00 ? 349 THR A C     1 
ATOM   2680 O  O     . THR A 1 350 ? 41.272 -8.022  20.195  1.00 0.00 ? 349 THR A O     1 
ATOM   2681 C  CB    . THR A 1 350 ? 39.203 -6.195  22.097  1.00 0.00 ? 349 THR A CB    1 
ATOM   2682 O  OG1   . THR A 1 350 ? 39.145 -5.749  20.751  1.00 0.00 ? 349 THR A OG1   1 
ATOM   2683 C  CG2   . THR A 1 350 ? 39.359 -4.956  22.983  1.00 0.00 ? 349 THR A CG2   1 
ATOM   2684 N  N     . LYS A 1 351 ? 41.832 -5.945  20.831  1.00 0.00 ? 350 LYS A N     1 
ATOM   2685 C  CA    . LYS A 1 351 ? 42.697 -5.731  19.672  1.00 0.00 ? 350 LYS A CA    1 
ATOM   2686 C  C     . LYS A 1 351 ? 43.696 -6.846  19.666  1.00 0.00 ? 350 LYS A C     1 
ATOM   2687 O  O     . LYS A 1 351 ? 44.043 -7.388  18.606  1.00 0.00 ? 350 LYS A O     1 
ATOM   2688 C  CB    . LYS A 1 351 ? 43.484 -4.422  19.762  1.00 0.00 ? 350 LYS A CB    1 
ATOM   2689 C  CG    . LYS A 1 351 ? 44.926 -4.572  19.242  1.00 0.00 ? 350 LYS A CG    1 
ATOM   2690 C  CD    . LYS A 1 351 ? 45.473 -3.293  18.594  1.00 0.00 ? 350 LYS A CD    1 
ATOM   2691 C  CE    . LYS A 1 351 ? 46.505 -3.565  17.494  1.00 0.00 ? 350 LYS A CE    1 
ATOM   2692 N  NZ    . LYS A 1 351 ? 47.197 -2.350  17.042  1.00 0.00 ? 350 LYS A NZ    1 
ATOM   2693 N  N     . ALA A 1 352 ? 44.111 -7.124  20.880  1.00 0.00 ? 351 ALA A N     1 
ATOM   2694 C  CA    . ALA A 1 352 ? 45.149 -8.104  21.144  1.00 0.00 ? 351 ALA A CA    1 
ATOM   2695 C  C     . ALA A 1 352 ? 44.808 -9.423  20.454  1.00 0.00 ? 351 ALA A C     1 
ATOM   2696 O  O     . ALA A 1 352 ? 45.644 -10.010 19.752  1.00 0.00 ? 351 ALA A O     1 
ATOM   2697 C  CB    . ALA A 1 352 ? 45.262 -8.347  22.651  1.00 0.00 ? 351 ALA A CB    1 
ATOM   2698 N  N     . LEU A 1 353 ? 43.589 -9.869  20.664  1.00 0.00 ? 352 LEU A N     1 
ATOM   2699 C  CA    . LEU A 1 353 ? 43.066 -11.102 20.039  1.00 0.00 ? 352 LEU A CA    1 
ATOM   2700 C  C     . LEU A 1 353 ? 43.039 -10.990 18.514  1.00 0.00 ? 352 LEU A C     1 
ATOM   2701 O  O     . LEU A 1 353 ? 43.490 -11.896 17.798  1.00 0.00 ? 352 LEU A O     1 
ATOM   2702 C  CB    . LEU A 1 353 ? 41.639 -11.374 20.507  1.00 0.00 ? 352 LEU A CB    1 
ATOM   2703 C  CG    . LEU A 1 353 ? 40.934 -12.442 19.668  1.00 0.00 ? 352 LEU A CG    1 
ATOM   2704 C  CD1   . LEU A 1 353 ? 39.630 -11.944 19.041  1.00 0.00 ? 352 LEU A CD1   1 
ATOM   2705 C  CD2   . LEU A 1 353 ? 41.788 -12.947 18.503  1.00 0.00 ? 352 LEU A CD2   1 
ATOM   2706 N  N     . LEU A 1 354 ? 42.508 -9.863  18.101  1.00 0.00 ? 353 LEU A N     1 
ATOM   2707 C  CA    . LEU A 1 354 ? 42.285 -9.535  16.697  1.00 0.00 ? 353 LEU A CA    1 
ATOM   2708 C  C     . LEU A 1 354 ? 43.576 -9.701  15.909  1.00 0.00 ? 353 LEU A C     1 
ATOM   2709 O  O     . LEU A 1 354 ? 43.579 -10.243 14.795  1.00 0.00 ? 353 LEU A O     1 
ATOM   2710 C  CB    . LEU A 1 354 ? 41.793 -8.089  16.563  1.00 0.00 ? 353 LEU A CB    1 
ATOM   2711 C  CG    . LEU A 1 354 ? 41.297 -7.749  15.155  1.00 0.00 ? 353 LEU A CG    1 
ATOM   2712 C  CD1   . LEU A 1 354 ? 41.266 -6.244  14.879  1.00 0.00 ? 353 LEU A CD1   1 
ATOM   2713 C  CD2   . LEU A 1 354 ? 42.167 -8.354  14.052  1.00 0.00 ? 353 LEU A CD2   1 
ATOM   2714 N  N     . ASP A 1 355 ? 44.648 -9.234  16.493  1.00 0.00 ? 354 ASP A N     1 
ATOM   2715 C  CA    . ASP A 1 355 ? 45.963 -9.231  15.830  1.00 0.00 ? 354 ASP A CA    1 
ATOM   2716 C  C     . ASP A 1 355 ? 46.486 -10.606 15.384  1.00 0.00 ? 354 ASP A C     1 
ATOM   2717 O  O     . ASP A 1 355 ? 46.812 -10.815 14.206  1.00 0.00 ? 354 ASP A O     1 
ATOM   2718 C  CB    . ASP A 1 355 ? 47.035 -8.735  16.797  1.00 0.00 ? 354 ASP A CB    1 
ATOM   2719 C  CG    . ASP A 1 355 ? 46.911 -7.250  17.113  1.00 0.00 ? 354 ASP A CG    1 
ATOM   2720 O  OD1   . ASP A 1 355 ? 46.836 -6.874  18.282  1.00 0.00 ? 354 ASP A OD1   1 
ATOM   2721 O  OD2   . ASP A 1 355 ? 46.885 -6.368  16.132  1.00 0.00 ? 354 ASP A OD2   1 
ATOM   2722 N  N     . GLU A 1 356 ? 46.557 -11.533 16.311  1.00 0.00 ? 355 GLU A N     1 
ATOM   2723 C  CA    . GLU A 1 356 ? 47.122 -12.860 16.027  1.00 0.00 ? 355 GLU A CA    1 
ATOM   2724 C  C     . GLU A 1 356 ? 46.347 -13.555 14.921  1.00 0.00 ? 355 GLU A C     1 
ATOM   2725 O  O     . GLU A 1 356 ? 46.934 -14.115 13.982  1.00 0.00 ? 355 GLU A O     1 
ATOM   2726 C  CB    . GLU A 1 356 ? 47.110 -13.751 17.275  1.00 0.00 ? 355 GLU A CB    1 
ATOM   2727 C  CG    . GLU A 1 356 ? 47.793 -13.113 18.499  1.00 0.00 ? 355 GLU A CG    1 
ATOM   2728 C  CD    . GLU A 1 356 ? 49.286 -12.809 18.300  1.00 0.00 ? 355 GLU A CD    1 
ATOM   2729 O  OE1   . GLU A 1 356 ? 49.696 -11.586 18.269  1.00 0.00 ? 355 GLU A OE1   1 
ATOM   2730 O  OE2   . GLU A 1 356 ? 50.130 -13.775 18.164  1.00 0.00 ? 355 GLU A OE2   1 
ATOM   2731 N  N     . VAL A 1 357 ? 45.044 -13.506 15.043  1.00 0.00 ? 356 VAL A N     1 
ATOM   2732 C  CA    . VAL A 1 357 ? 44.179 -14.219 14.114  1.00 0.00 ? 356 VAL A CA    1 
ATOM   2733 C  C     . VAL A 1 357 ? 44.484 -13.823 12.687  1.00 0.00 ? 356 VAL A C     1 
ATOM   2734 O  O     . VAL A 1 357 ? 44.755 -14.679 11.831  1.00 0.00 ? 356 VAL A O     1 
ATOM   2735 C  CB    . VAL A 1 357 ? 42.724 -13.824 14.365  1.00 0.00 ? 356 VAL A CB    1 
ATOM   2736 C  CG1   . VAL A 1 357 ? 42.564 -12.350 14.746  1.00 0.00 ? 356 VAL A CG1   1 
ATOM   2737 C  CG2   . VAL A 1 357 ? 41.828 -14.035 13.143  1.00 0.00 ? 356 VAL A CG2   1 
ATOM   2738 N  N     . VAL A 1 358 ? 44.439 -12.535 12.454  1.00 0.00 ? 357 VAL A N     1 
ATOM   2739 C  CA    . VAL A 1 358 ? 44.744 -12.002 11.135  1.00 0.00 ? 357 VAL A CA    1 
ATOM   2740 C  C     . VAL A 1 358 ? 46.167 -12.331 10.780  1.00 0.00 ? 357 VAL A C     1 
ATOM   2741 O  O     . VAL A 1 358 ? 46.453 -12.831 9.682   1.00 0.00 ? 357 VAL A O     1 
ATOM   2742 C  CB    . VAL A 1 358 ? 44.571 -10.488 11.082  1.00 0.00 ? 357 VAL A CB    1 
ATOM   2743 C  CG1   . VAL A 1 358 ? 45.447 -9.825  10.017  1.00 0.00 ? 357 VAL A CG1   1 
ATOM   2744 C  CG2   . VAL A 1 358 ? 43.136 -10.062 10.764  1.00 0.00 ? 357 VAL A CG2   1 
ATOM   2745 N  N     . LYS A 1 359 ? 47.033 -12.043 11.718  1.00 0.00 ? 358 LYS A N     1 
ATOM   2746 C  CA    . LYS A 1 359 ? 48.444 -12.256 11.490  1.00 0.00 ? 358 LYS A CA    1 
ATOM   2747 C  C     . LYS A 1 359 ? 48.643 -13.690 11.104  1.00 0.00 ? 358 LYS A C     1 
ATOM   2748 O  O     . LYS A 1 359 ? 49.301 -13.996 10.099  1.00 0.00 ? 358 LYS A O     1 
ATOM   2749 C  CB    . LYS A 1 359 ? 49.260 -11.997 12.767  1.00 0.00 ? 358 LYS A CB    1 
ATOM   2750 C  CG    . LYS A 1 359 ? 50.721 -12.467 12.652  1.00 0.00 ? 358 LYS A CG    1 
ATOM   2751 C  CD    . LYS A 1 359 ? 51.160 -13.398 13.792  1.00 0.00 ? 358 LYS A CD    1 
ATOM   2752 C  CE    . LYS A 1 359 ? 52.680 -13.602 13.846  1.00 0.00 ? 358 LYS A CE    1 
ATOM   2753 N  NZ    . LYS A 1 359 ? 53.089 -14.625 14.820  1.00 0.00 ? 358 LYS A NZ    1 
ATOM   2754 N  N     . SER A 1 360 ? 48.059 -14.530 11.912  1.00 0.00 ? 359 SER A N     1 
ATOM   2755 C  CA    . SER A 1 360 ? 48.180 -15.965 11.731  1.00 0.00 ? 359 SER A CA    1 
ATOM   2756 C  C     . SER A 1 360 ? 47.661 -16.402 10.383  1.00 0.00 ? 359 SER A C     1 
ATOM   2757 O  O     . SER A 1 360 ? 48.360 -17.086 9.620   1.00 0.00 ? 359 SER A O     1 
ATOM   2758 C  CB    . SER A 1 360 ? 47.313 -16.704 12.751  1.00 0.00 ? 359 SER A CB    1 
ATOM   2759 O  OG    . SER A 1 360 ? 47.979 -16.768 14.003  1.00 0.00 ? 359 SER A OG    1 
ATOM   2760 N  N     . SER A 1 361 ? 46.442 -15.985 10.106  1.00 0.00 ? 360 SER A N     1 
ATOM   2761 C  CA    . SER A 1 361 ? 45.776 -16.399 8.878   1.00 0.00 ? 360 SER A CA    1 
ATOM   2762 C  C     . SER A 1 361 ? 46.705 -17.377 8.176   1.00 0.00 ? 360 SER A C     1 
ATOM   2763 O  O     . SER A 1 361 ? 46.423 -18.582 8.098   1.00 0.00 ? 360 SER A O     1 
ATOM   2764 C  CB    . SER A 1 361 ? 45.511 -15.187 7.993   1.00 0.00 ? 360 SER A CB    1 
ATOM   2765 O  OG    . SER A 1 361 ? 46.616 -14.297 8.048   1.00 0.00 ? 360 SER A OG    1 
ATOM   2766 N  N     . ALA A 1 362 ? 47.787 -16.804 7.680   1.00 0.00 ? 361 ALA A N     1 
ATOM   2767 C  CA    . ALA A 1 362 ? 48.853 -17.573 7.044   1.00 0.00 ? 361 ALA A CA    1 
ATOM   2768 C  C     . ALA A 1 362 ? 49.344 -18.556 8.079   1.00 0.00 ? 361 ALA A C     1 
ATOM   2769 O  O     . ALA A 1 362 ? 48.835 -19.683 8.180   1.00 0.00 ? 361 ALA A O     1 
ATOM   2770 C  CB    . ALA A 1 362 ? 49.982 -16.638 6.605   1.00 0.00 ? 361 ALA A CB    1 
ATOM   2771 N  N     . ALA A 1 363 ? 50.336 -18.110 8.826   1.00 0.00 ? 362 ALA A N     1 
ATOM   2772 C  CA    . ALA A 1 363 ? 50.765 -18.894 9.958   1.00 0.00 ? 362 ALA A CA    1 
ATOM   2773 C  C     . ALA A 1 363 ? 49.448 -19.335 10.554  1.00 0.00 ? 362 ALA A C     1 
ATOM   2774 O  O     . ALA A 1 363 ? 48.371 -18.964 10.064  1.00 0.00 ? 362 ALA A O     1 
ATOM   2775 C  CB    . ALA A 1 363 ? 51.591 -18.028 10.912  1.00 0.00 ? 362 ALA A CB    1 
ATOM   2776 N  N     . GLY A 1 364 ? 49.468 -20.099 11.596  1.00 0.00 ? 363 GLY A N     1 
ATOM   2777 C  CA    . GLY A 1 364 ? 48.198 -20.582 12.103  1.00 0.00 ? 363 GLY A CA    1 
ATOM   2778 C  C     . GLY A 1 364 ? 47.394 -20.998 10.873  1.00 0.00 ? 363 GLY A C     1 
ATOM   2779 O  O     . GLY A 1 364 ? 47.875 -21.763 10.024  1.00 0.00 ? 363 GLY A O     1 
ATOM   2780 N  N     . ASN A 1 365 ? 46.190 -20.494 10.768  1.00 0.00 ? 364 ASN A N     1 
ATOM   2781 C  CA    . ASN A 1 365 ? 45.344 -20.847 9.631   1.00 0.00 ? 364 ASN A CA    1 
ATOM   2782 C  C     . ASN A 1 365 ? 44.367 -19.739 9.254   1.00 0.00 ? 364 ASN A C     1 
ATOM   2783 O  O     . ASN A 1 365 ? 43.989 -18.908 10.092  1.00 0.00 ? 364 ASN A O     1 
ATOM   2784 C  CB    . ASN A 1 365 ? 44.521 -22.104 9.963   1.00 0.00 ? 364 ASN A CB    1 
ATOM   2785 C  CG    . ASN A 1 365 ? 45.390 -23.319 10.293  1.00 0.00 ? 364 ASN A CG    1 
ATOM   2786 O  OD1   . ASN A 1 365 ? 46.071 -23.328 11.318  1.00 0.00 ? 364 ASN A OD1   1 
ATOM   2787 N  ND2   . ASN A 1 365 ? 45.410 -24.358 9.478   1.00 0.00 ? 364 ASN A ND2   1 
ATOM   2788 N  N     . THR A 1 366 ? 44.011 -19.799 7.980   1.00 0.00 ? 365 THR A N     1 
ATOM   2789 C  CA    . THR A 1 366 ? 43.055 -18.879 7.349   1.00 0.00 ? 365 THR A CA    1 
ATOM   2790 C  C     . THR A 1 366 ? 42.047 -18.386 8.403   1.00 0.00 ? 365 THR A C     1 
ATOM   2791 O  O     . THR A 1 366 ? 41.587 -19.159 9.256   1.00 0.00 ? 365 THR A O     1 
ATOM   2792 C  CB    . THR A 1 366 ? 42.328 -19.623 6.227   1.00 0.00 ? 365 THR A CB    1 
ATOM   2793 O  OG1   . THR A 1 366 ? 41.266 -20.395 6.767   1.00 0.00 ? 365 THR A OG1   1 
ATOM   2794 C  CG2   . THR A 1 366 ? 43.240 -20.578 5.454   1.00 0.00 ? 365 THR A CG2   1 
ATOM   2795 N  N     . VAL A 1 367 ? 41.720 -17.098 8.313   1.00 0.00 ? 366 VAL A N     1 
ATOM   2796 C  CA    . VAL A 1 367 ? 40.809 -16.419 9.278   1.00 0.00 ? 366 VAL A CA    1 
ATOM   2797 C  C     . VAL A 1 367 ? 39.549 -15.807 8.606   1.00 0.00 ? 366 VAL A C     1 
ATOM   2798 O  O     . VAL A 1 367 ? 39.650 -14.895 7.771   1.00 0.00 ? 366 VAL A O     1 
ATOM   2799 C  CB    . VAL A 1 367 ? 41.558 -15.295 9.995   1.00 0.00 ? 366 VAL A CB    1 
ATOM   2800 C  CG1   . VAL A 1 367 ? 40.766 -14.696 11.158  1.00 0.00 ? 366 VAL A CG1   1 
ATOM   2801 C  CG2   . VAL A 1 367 ? 42.891 -15.751 10.592  1.00 0.00 ? 366 VAL A CG2   1 
ATOM   2802 N  N     . ILE A 1 368 ? 38.354 -16.312 8.976   1.00 0.00 ? 367 ILE A N     1 
ATOM   2803 C  CA    . ILE A 1 368 ? 37.074 -15.768 8.435   1.00 0.00 ? 367 ILE A CA    1 
ATOM   2804 C  C     . ILE A 1 368 ? 36.198 -15.167 9.563   1.00 0.00 ? 367 ILE A C     1 
ATOM   2805 O  O     . ILE A 1 368 ? 35.546 -15.899 10.323  1.00 0.00 ? 367 ILE A O     1 
ATOM   2806 C  CB    . ILE A 1 368 ? 36.287 -16.919 7.812   1.00 0.00 ? 367 ILE A CB    1 
ATOM   2807 C  CG1   . ILE A 1 368 ? 37.192 -17.958 7.149   1.00 0.00 ? 367 ILE A CG1   1 
ATOM   2808 C  CG2   . ILE A 1 368 ? 35.305 -16.459 6.732   1.00 0.00 ? 367 ILE A CG2   1 
ATOM   2809 C  CD1   . ILE A 1 368 ? 36.453 -18.837 6.138   1.00 0.00 ? 367 ILE A CD1   1 
ATOM   2810 N  N     . ILE A 1 369 ? 36.264 -13.828 9.584   1.00 0.00 ? 368 ILE A N     1 
ATOM   2811 C  CA    . ILE A 1 369 ? 35.540 -12.924 10.527  1.00 0.00 ? 368 ILE A CA    1 
ATOM   2812 C  C     . ILE A 1 369 ? 34.830 -11.773 9.821   1.00 0.00 ? 368 ILE A C     1 
ATOM   2813 O  O     . ILE A 1 369 ? 35.462 -10.955 9.137   1.00 0.00 ? 368 ILE A O     1 
ATOM   2814 C  CB    . ILE A 1 369 ? 36.491 -12.252 11.502  1.00 0.00 ? 368 ILE A CB    1 
ATOM   2815 C  CG1   . ILE A 1 369 ? 35.954 -10.920 12.032  1.00 0.00 ? 368 ILE A CG1   1 
ATOM   2816 C  CG2   . ILE A 1 369 ? 37.853 -11.933 10.883  1.00 0.00 ? 368 ILE A CG2   1 
ATOM   2817 C  CD1   . ILE A 1 369 ? 36.042 -9.789  11.005  1.00 0.00 ? 368 ILE A CD1   1 
ATOM   2818 N  N     . GLY A 1 370 ? 33.548 -11.645 9.910   1.00 0.00 ? 369 GLY A N     1 
ATOM   2819 C  CA    . GLY A 1 370 ? 32.928 -10.480 9.261   1.00 0.00 ? 369 GLY A CA    1 
ATOM   2820 C  C     . GLY A 1 370 ? 31.527 -10.264 9.760   1.00 0.00 ? 369 GLY A C     1 
ATOM   2821 O  O     . GLY A 1 370 ? 30.803 -11.223 10.065  1.00 0.00 ? 369 GLY A O     1 
ATOM   2822 N  N     . GLY A 1 371 ? 31.149 -9.010  9.825   1.00 0.00 ? 370 GLY A N     1 
ATOM   2823 C  CA    . GLY A 1 371 ? 29.813 -8.694  10.278  1.00 0.00 ? 370 GLY A CA    1 
ATOM   2824 C  C     . GLY A 1 371 ? 29.486 -7.236  10.248  1.00 0.00 ? 370 GLY A C     1 
ATOM   2825 O  O     . GLY A 1 371 ? 29.330 -6.639  9.172   1.00 0.00 ? 370 GLY A O     1 
ATOM   2826 N  N     . GLY A 1 372 ? 29.409 -6.766  11.441  1.00 0.00 ? 371 GLY A N     1 
ATOM   2827 C  CA    . GLY A 1 372 ? 29.153 -5.387  11.724  1.00 0.00 ? 371 GLY A CA    1 
ATOM   2828 C  C     . GLY A 1 372 ? 30.071 -4.966  12.844  1.00 0.00 ? 371 GLY A C     1 
ATOM   2829 O  O     . GLY A 1 372 ? 31.009 -4.181  12.641  1.00 0.00 ? 371 GLY A O     1 
ATOM   2830 N  N     . ASP A 1 373 ? 29.779 -5.510  14.001  1.00 0.00 ? 372 ASP A N     1 
ATOM   2831 C  CA    . ASP A 1 373 ? 30.510 -5.150  15.208  1.00 0.00 ? 372 ASP A CA    1 
ATOM   2832 C  C     . ASP A 1 373 ? 31.999 -5.384  15.021  1.00 0.00 ? 372 ASP A C     1 
ATOM   2833 O  O     . ASP A 1 373 ? 32.820 -4.480  15.239  1.00 0.00 ? 372 ASP A O     1 
ATOM   2834 C  CB    . ASP A 1 373 ? 30.070 -6.046  16.371  1.00 0.00 ? 372 ASP A CB    1 
ATOM   2835 C  CG    . ASP A 1 373 ? 28.579 -5.946  16.694  1.00 0.00 ? 372 ASP A CG    1 
ATOM   2836 O  OD1   . ASP A 1 373 ? 27.703 -6.320  15.823  1.00 0.00 ? 372 ASP A OD1   1 
ATOM   2837 O  OD2   . ASP A 1 373 ? 28.198 -5.488  17.838  1.00 0.00 ? 372 ASP A OD2   1 
ATOM   2838 N  N     . THR A 1 374 ? 32.297 -6.591  14.620  1.00 0.00 ? 373 THR A N     1 
ATOM   2839 C  CA    . THR A 1 374 ? 33.666 -7.013  14.338  1.00 0.00 ? 373 THR A CA    1 
ATOM   2840 C  C     . THR A 1 374 ? 34.238 -6.145  13.206  1.00 0.00 ? 373 THR A C     1 
ATOM   2841 O  O     . THR A 1 374 ? 35.401 -5.719  13.253  1.00 0.00 ? 373 THR A O     1 
ATOM   2842 C  CB    . THR A 1 374 ? 33.718 -8.509  14.027  1.00 0.00 ? 373 THR A CB    1 
ATOM   2843 O  OG1   . THR A 1 374 ? 35.049 -8.893  13.713  1.00 0.00 ? 373 THR A OG1   1 
ATOM   2844 C  CG2   . THR A 1 374 ? 32.835 -8.908  12.844  1.00 0.00 ? 373 THR A CG2   1 
ATOM   2845 N  N     . ALA A 1 375 ? 33.402 -5.902  12.203  1.00 0.00 ? 374 ALA A N     1 
ATOM   2846 C  CA    . ALA A 1 375 ? 33.809 -5.131  11.019  1.00 0.00 ? 374 ALA A CA    1 
ATOM   2847 C  C     . ALA A 1 375 ? 34.444 -3.836  11.498  1.00 0.00 ? 374 ALA A C     1 
ATOM   2848 O  O     . ALA A 1 375 ? 35.505 -3.425  11.006  1.00 0.00 ? 374 ALA A O     1 
ATOM   2849 C  CB    . ALA A 1 375 ? 32.588 -4.822  10.150  1.00 0.00 ? 374 ALA A CB    1 
ATOM   2850 N  N     . THR A 1 376 ? 33.766 -3.232  12.445  1.00 0.00 ? 375 THR A N     1 
ATOM   2851 C  CA    . THR A 1 376 ? 34.258 -2.025  13.097  1.00 0.00 ? 375 THR A CA    1 
ATOM   2852 C  C     . THR A 1 376 ? 35.614 -2.335  13.702  1.00 0.00 ? 375 THR A C     1 
ATOM   2853 O  O     . THR A 1 376 ? 36.576 -1.570  13.540  1.00 0.00 ? 375 THR A O     1 
ATOM   2854 C  CB    . THR A 1 376 ? 33.311 -1.615  14.222  1.00 0.00 ? 375 THR A CB    1 
ATOM   2855 O  OG1   . THR A 1 376 ? 31.981 -1.992  13.897  1.00 0.00 ? 375 THR A OG1   1 
ATOM   2856 C  CG2   . THR A 1 376 ? 33.309 -0.108  14.483  1.00 0.00 ? 375 THR A CG2   1 
ATOM   2857 N  N     . VAL A 1 377 ? 35.620 -3.459  14.382  1.00 0.00 ? 376 VAL A N     1 
ATOM   2858 C  CA    . VAL A 1 377 ? 36.810 -3.954  15.046  1.00 0.00 ? 376 VAL A CA    1 
ATOM   2859 C  C     . VAL A 1 377 ? 37.913 -4.078  14.020  1.00 0.00 ? 376 VAL A C     1 
ATOM   2860 O  O     . VAL A 1 377 ? 39.043 -3.618  14.238  1.00 0.00 ? 376 VAL A O     1 
ATOM   2861 C  CB    . VAL A 1 377 ? 36.536 -5.334  15.652  1.00 0.00 ? 376 VAL A CB    1 
ATOM   2862 C  CG1   . VAL A 1 377 ? 37.710 -5.872  16.472  1.00 0.00 ? 376 VAL A CG1   1 
ATOM   2863 C  CG2   . VAL A 1 377 ? 35.332 -5.345  16.596  1.00 0.00 ? 376 VAL A CG2   1 
ATOM   2864 N  N     . ALA A 1 378 ? 37.554 -4.698  12.923  1.00 0.00 ? 377 ALA A N     1 
ATOM   2865 C  CA    . ALA A 1 378 ? 38.497 -4.922  11.836  1.00 0.00 ? 377 ALA A CA    1 
ATOM   2866 C  C     . ALA A 1 378 ? 39.043 -3.601  11.296  1.00 0.00 ? 377 ALA A C     1 
ATOM   2867 O  O     . ALA A 1 378 ? 40.264 -3.404  11.204  1.00 0.00 ? 377 ALA A O     1 
ATOM   2868 C  CB    . ALA A 1 378 ? 37.806 -5.660  10.687  1.00 0.00 ? 377 ALA A CB    1 
ATOM   2869 N  N     . LYS A 1 379 ? 38.137 -2.702  10.949  1.00 0.00 ? 378 LYS A N     1 
ATOM   2870 C  CA    . LYS A 1 379 ? 38.533 -1.398  10.392  1.00 0.00 ? 378 LYS A CA    1 
ATOM   2871 C  C     . LYS A 1 379 ? 39.391 -0.610  11.391  1.00 0.00 ? 378 LYS A C     1 
ATOM   2872 O  O     . LYS A 1 379 ? 40.469 -0.104  11.046  1.00 0.00 ? 378 LYS A O     1 
ATOM   2873 C  CB    . LYS A 1 379 ? 37.312 -0.538  10.021  1.00 0.00 ? 378 LYS A CB    1 
ATOM   2874 C  CG    . LYS A 1 379 ? 37.641 0.543   8.974   1.00 0.00 ? 378 LYS A CG    1 
ATOM   2875 C  CD    . LYS A 1 379 ? 36.538 1.597   8.808   1.00 0.00 ? 378 LYS A CD    1 
ATOM   2876 C  CE    . LYS A 1 379 ? 36.913 2.711   7.823   1.00 0.00 ? 378 LYS A CE    1 
ATOM   2877 N  NZ    . LYS A 1 379 ? 35.811 3.652   7.572   1.00 0.00 ? 378 LYS A NZ    1 
ATOM   2878 N  N     . LYS A 1 380 ? 38.899 -0.518  12.633  1.00 0.00 ? 379 LYS A N     1 
ATOM   2879 C  CA    . LYS A 1 380 ? 39.591 0.265   13.692  1.00 0.00 ? 379 LYS A CA    1 
ATOM   2880 C  C     . LYS A 1 380 ? 41.006 -0.263  13.991  1.00 0.00 ? 379 LYS A C     1 
ATOM   2881 O  O     . LYS A 1 380 ? 41.988 0.492   13.965  1.00 0.00 ? 379 LYS A O     1 
ATOM   2882 C  CB    . LYS A 1 380 ? 38.797 0.265   14.999  1.00 0.00 ? 379 LYS A CB    1 
ATOM   2883 C  CG    . LYS A 1 380 ? 39.322 1.293   16.009  1.00 0.00 ? 379 LYS A CG    1 
ATOM   2884 C  CD    . LYS A 1 380 ? 38.220 1.935   16.857  1.00 0.00 ? 379 LYS A CD    1 
ATOM   2885 C  CE    . LYS A 1 380 ? 38.741 3.050   17.768  1.00 0.00 ? 379 LYS A CE    1 
ATOM   2886 N  NZ    . LYS A 1 380 ? 37.785 3.428   18.819  1.00 0.00 ? 379 LYS A NZ    1 
ATOM   2887 N  N     . TYR A 1 381 ? 41.104 -1.543  14.275  1.00 0.00 ? 380 TYR A N     1 
ATOM   2888 C  CA    . TYR A 1 381 ? 42.404 -2.201  14.494  1.00 0.00 ? 380 TYR A CA    1 
ATOM   2889 C  C     . TYR A 1 381 ? 43.211 -2.155  13.202  1.00 0.00 ? 380 TYR A C     1 
ATOM   2890 O  O     . TYR A 1 381 ? 44.415 -1.860  13.211  1.00 0.00 ? 380 TYR A O     1 
ATOM   2891 C  CB    . TYR A 1 381 ? 42.161 -3.541  15.138  1.00 0.00 ? 380 TYR A CB    1 
ATOM   2892 C  CG    . TYR A 1 381 ? 41.754 -3.265  16.579  1.00 0.00 ? 380 TYR A CG    1 
ATOM   2893 C  CD1   . TYR A 1 381 ? 42.338 -2.179  17.240  1.00 0.00 ? 380 TYR A CD1   1 
ATOM   2894 C  CD2   . TYR A 1 381 ? 40.798 -4.049  17.225  1.00 0.00 ? 380 TYR A CD2   1 
ATOM   2895 C  CE1   . TYR A 1 381 ? 41.959 -1.868  18.544  1.00 0.00 ? 380 TYR A CE1   1 
ATOM   2896 C  CE2   . TYR A 1 381 ? 40.415 -3.737  18.530  1.00 0.00 ? 380 TYR A CE2   1 
ATOM   2897 C  CZ    . TYR A 1 381 ? 40.993 -2.644  19.188  1.00 0.00 ? 380 TYR A CZ    1 
ATOM   2898 O  OH    . TYR A 1 381 ? 40.610 -2.337  20.456  1.00 0.00 ? 380 TYR A OH    1 
ATOM   2899 N  N     . GLY A 1 382 ? 42.509 -2.456  12.135  1.00 0.00 ? 381 GLY A N     1 
ATOM   2900 C  CA    . GLY A 1 382 ? 43.074 -2.443  10.789  1.00 0.00 ? 381 GLY A CA    1 
ATOM   2901 C  C     . GLY A 1 382 ? 43.241 -3.868  10.297  1.00 0.00 ? 381 GLY A C     1 
ATOM   2902 O  O     . GLY A 1 382 ? 44.168 -4.581  10.709  1.00 0.00 ? 381 GLY A O     1 
ATOM   2903 N  N     . VAL A 1 383 ? 42.329 -4.236  9.431   1.00 0.00 ? 382 VAL A N     1 
ATOM   2904 C  CA    . VAL A 1 383 ? 42.313 -5.566  8.832   1.00 0.00 ? 382 VAL A CA    1 
ATOM   2905 C  C     . VAL A 1 383 ? 43.753 -5.998  8.505   1.00 0.00 ? 382 VAL A C     1 
ATOM   2906 O  O     . VAL A 1 383 ? 44.184 -7.104  8.863   1.00 0.00 ? 382 VAL A O     1 
ATOM   2907 C  CB    . VAL A 1 383 ? 41.479 -5.548  7.549   1.00 0.00 ? 382 VAL A CB    1 
ATOM   2908 C  CG1   . VAL A 1 383 ? 42.291 -5.155  6.313   1.00 0.00 ? 382 VAL A CG1   1 
ATOM   2909 C  CG2   . VAL A 1 383 ? 40.857 -6.907  7.221   1.00 0.00 ? 382 VAL A CG2   1 
ATOM   2910 N  N     . THR A 1 384 ? 44.422 -5.073  7.833   1.00 0.00 ? 383 THR A N     1 
ATOM   2911 C  CA    . THR A 1 384 ? 45.812 -5.217  7.357   1.00 0.00 ? 383 THR A CA    1 
ATOM   2912 C  C     . THR A 1 384 ? 46.202 -6.706  7.270   1.00 0.00 ? 383 THR A C     1 
ATOM   2913 O  O     . THR A 1 384 ? 46.654 -7.306  8.258   1.00 0.00 ? 383 THR A O     1 
ATOM   2914 C  CB    . THR A 1 384 ? 46.761 -4.386  8.225   1.00 0.00 ? 383 THR A CB    1 
ATOM   2915 O  OG1   . THR A 1 384 ? 48.107 -4.629  7.843   1.00 0.00 ? 383 THR A OG1   1 
ATOM   2916 C  CG2   . THR A 1 384 ? 46.644 -4.702  9.716   1.00 0.00 ? 383 THR A CG2   1 
ATOM   2917 N  N     . ASP A 1 385 ? 45.955 -7.130  6.017   1.00 0.00 ? 384 ASP A N     1 
ATOM   2918 C  CA    . ASP A 1 385 ? 46.177 -8.477  5.444   1.00 0.00 ? 384 ASP A CA    1 
ATOM   2919 C  C     . ASP A 1 385 ? 44.942 -9.374  5.681   1.00 0.00 ? 384 ASP A C     1 
ATOM   2920 O  O     . ASP A 1 385 ? 44.741 -10.382 4.986   1.00 0.00 ? 384 ASP A O     1 
ATOM   2921 C  CB    . ASP A 1 385 ? 47.486 -9.050  5.968   1.00 0.00 ? 384 ASP A CB    1 
ATOM   2922 C  CG    . ASP A 1 385 ? 48.685 -8.457  5.213   1.00 0.00 ? 384 ASP A CG    1 
ATOM   2923 O  OD1   . ASP A 1 385 ? 48.549 -7.362  4.543   1.00 0.00 ? 384 ASP A OD1   1 
ATOM   2924 O  OD2   . ASP A 1 385 ? 49.829 -9.052  5.246   1.00 0.00 ? 384 ASP A OD2   1 
ATOM   2925 N  N     . LYS A 1 386 ? 44.147 -8.986  6.662   1.00 0.00 ? 385 LYS A N     1 
ATOM   2926 C  CA    . LYS A 1 386 ? 42.846 -9.636  6.985   1.00 0.00 ? 385 LYS A CA    1 
ATOM   2927 C  C     . LYS A 1 386 ? 42.951 -11.202 6.978   1.00 0.00 ? 385 LYS A C     1 
ATOM   2928 O  O     . LYS A 1 386 ? 42.384 -11.884 7.845   1.00 0.00 ? 385 LYS A O     1 
ATOM   2929 C  CB    . LYS A 1 386 ? 41.804 -9.215  5.921   1.00 0.00 ? 385 LYS A CB    1 
ATOM   2930 C  CG    . LYS A 1 386 ? 42.135 -7.877  5.250   1.00 0.00 ? 385 LYS A CG    1 
ATOM   2931 C  CD    . LYS A 1 386 ? 41.198 -7.541  4.086   1.00 0.00 ? 385 LYS A CD    1 
ATOM   2932 C  CE    . LYS A 1 386 ? 41.386 -6.117  3.557   1.00 0.00 ? 385 LYS A CE    1 
ATOM   2933 N  NZ    . LYS A 1 386 ? 40.580 -5.837  2.360   1.00 0.00 ? 385 LYS A NZ    1 
ATOM   2934 N  N     . ILE A 1 387 ? 43.684 -11.694 5.983   1.00 0.00 ? 386 ILE A N     1 
ATOM   2935 C  CA    . ILE A 1 387 ? 43.974 -13.147 5.687   1.00 0.00 ? 386 ILE A CA    1 
ATOM   2936 C  C     . ILE A 1 387 ? 42.900 -14.139 6.076   1.00 0.00 ? 386 ILE A C     1 
ATOM   2937 O  O     . ILE A 1 387 ? 43.071 -14.934 7.012   1.00 0.00 ? 386 ILE A O     1 
ATOM   2938 C  CB    . ILE A 1 387 ? 45.200 -13.693 6.399   1.00 0.00 ? 386 ILE A CB    1 
ATOM   2939 C  CG1   . ILE A 1 387 ? 45.854 -12.677 7.327   1.00 0.00 ? 386 ILE A CG1   1 
ATOM   2940 C  CG2   . ILE A 1 387 ? 46.299 -14.140 5.433   1.00 0.00 ? 386 ILE A CG2   1 
ATOM   2941 C  CD1   . ILE A 1 387 ? 44.958 -12.282 8.503   1.00 0.00 ? 386 ILE A CD1   1 
ATOM   2942 N  N     . SER A 1 388 ? 41.891 -14.045 5.327   1.00 0.00 ? 387 SER A N     1 
ATOM   2943 C  CA    . SER A 1 388 ? 40.765 -14.913 5.395   1.00 0.00 ? 387 SER A CA    1 
ATOM   2944 C  C     . SER A 1 388 ? 39.636 -14.159 4.820   1.00 0.00 ? 387 SER A C     1 
ATOM   2945 O  O     . SER A 1 388 ? 39.749 -13.573 3.733   1.00 0.00 ? 387 SER A O     1 
ATOM   2946 C  CB    . SER A 1 388 ? 40.486 -15.396 6.823   1.00 0.00 ? 387 SER A CB    1 
ATOM   2947 O  OG    . SER A 1 388 ? 40.059 -16.751 6.801   1.00 0.00 ? 387 SER A OG    1 
ATOM   2948 N  N     . HIS A 1 389 ? 38.624 -14.201 5.577   1.00 0.00 ? 388 HIS A N     1 
ATOM   2949 C  CA    . HIS A 1 389 ? 37.376 -13.670 5.168   1.00 0.00 ? 388 HIS A CA    1 
ATOM   2950 C  C     . HIS A 1 389 ? 36.779 -12.602 6.045   1.00 0.00 ? 388 HIS A C     1 
ATOM   2951 O  O     . HIS A 1 389 ? 36.606 -12.797 7.257   1.00 0.00 ? 388 HIS A O     1 
ATOM   2952 C  CB    . HIS A 1 389 ? 36.340 -14.735 5.026   1.00 0.00 ? 388 HIS A CB    1 
ATOM   2953 C  CG    . HIS A 1 389 ? 35.491 -14.437 3.814   1.00 0.00 ? 388 HIS A CG    1 
ATOM   2954 N  ND1   . HIS A 1 389 ? 35.918 -14.750 2.534   1.00 0.00 ? 388 HIS A ND1   1 
ATOM   2955 C  CD2   . HIS A 1 389 ? 34.276 -13.850 3.691   1.00 0.00 ? 388 HIS A CD2   1 
ATOM   2956 C  CE1   . HIS A 1 389 ? 34.982 -14.365 1.691   1.00 0.00 ? 388 HIS A CE1   1 
ATOM   2957 N  NE2   . HIS A 1 389 ? 33.996 -13.825 2.366   1.00 0.00 ? 388 HIS A NE2   1 
ATOM   2958 N  N     . VAL A 1 390 ? 36.502 -11.510 5.393   1.00 0.00 ? 389 VAL A N     1 
ATOM   2959 C  CA    . VAL A 1 390 ? 35.682 -10.489 5.990   1.00 0.00 ? 389 VAL A CA    1 
ATOM   2960 C  C     . VAL A 1 390 ? 34.417 -10.747 5.205   1.00 0.00 ? 389 VAL A C     1 
ATOM   2961 O  O     . VAL A 1 390 ? 34.305 -10.363 4.031   1.00 0.00 ? 389 VAL A O     1 
ATOM   2962 C  CB    . VAL A 1 390 ? 36.265 -9.096  5.696   1.00 0.00 ? 389 VAL A CB    1 
ATOM   2963 C  CG1   . VAL A 1 390 ? 35.249 -8.147  5.055   1.00 0.00 ? 389 VAL A CG1   1 
ATOM   2964 C  CG2   . VAL A 1 390 ? 36.768 -8.377  6.949   1.00 0.00 ? 389 VAL A CG2   1 
ATOM   2965 N  N     . SER A 1 391 ? 33.523 -11.386 5.934   1.00 0.00 ? 390 SER A N     1 
ATOM   2966 C  CA    . SER A 1 391 ? 32.320 -12.013 5.375   1.00 0.00 ? 390 SER A CA    1 
ATOM   2967 C  C     . SER A 1 391 ? 31.143 -11.085 5.275   1.00 0.00 ? 390 SER A C     1 
ATOM   2968 O  O     . SER A 1 391 ? 29.984 -11.511 5.384   1.00 0.00 ? 390 SER A O     1 
ATOM   2969 C  CB    . SER A 1 391 ? 31.889 -13.184 6.261   1.00 0.00 ? 390 SER A CB    1 
ATOM   2970 O  OG    . SER A 1 391 ? 31.096 -14.094 5.513   1.00 0.00 ? 390 SER A OG    1 
ATOM   2971 N  N     . THR A 1 392 ? 31.423 -9.837  5.065   1.00 0.00 ? 391 THR A N     1 
ATOM   2972 C  CA    . THR A 1 392 ? 30.347 -8.883  4.939   1.00 0.00 ? 391 THR A CA    1 
ATOM   2973 C  C     . THR A 1 392 ? 29.029 -9.642  5.076   1.00 0.00 ? 391 THR A C     1 
ATOM   2974 O  O     . THR A 1 392 ? 29.003 -10.882 5.071   1.00 0.00 ? 391 THR A O     1 
ATOM   2975 C  CB    . THR A 1 392 ? 30.407 -8.209  3.567   1.00 0.00 ? 391 THR A CB    1 
ATOM   2976 O  OG1   . THR A 1 392 ? 29.149 -7.629  3.255   1.00 0.00 ? 391 THR A OG1   1 
ATOM   2977 C  CG2   . THR A 1 392 ? 30.755 -9.181  2.438   1.00 0.00 ? 391 THR A CG2   1 
ATOM   2978 N  N     . GLY A 1 393 ? 27.961 -8.865  5.157   1.00 0.00 ? 392 GLY A N     1 
ATOM   2979 C  CA    . GLY A 1 393 ? 26.660 -9.402  5.495   1.00 0.00 ? 392 GLY A CA    1 
ATOM   2980 C  C     . GLY A 1 393 ? 26.875 -9.848  6.914   1.00 0.00 ? 392 GLY A C     1 
ATOM   2981 O  O     . GLY A 1 393 ? 26.807 -11.046 7.227   1.00 0.00 ? 392 GLY A O     1 
ATOM   2982 N  N     . GLY A 1 394 ? 27.129 -8.864  7.745   1.00 0.00 ? 393 GLY A N     1 
ATOM   2983 C  CA    . GLY A 1 394 ? 27.582 -9.176  9.076   1.00 0.00 ? 393 GLY A CA    1 
ATOM   2984 C  C     . GLY A 1 394 ? 26.638 -10.211 9.631   1.00 0.00 ? 393 GLY A C     1 
ATOM   2985 O  O     . GLY A 1 394 ? 27.067 -11.272 10.106  1.00 0.00 ? 393 GLY A O     1 
ATOM   2986 N  N     . GLY A 1 395 ? 25.367 -9.892  9.568   1.00 0.00 ? 394 GLY A N     1 
ATOM   2987 C  CA    . GLY A 1 395 ? 24.267 -10.821 9.944   1.00 0.00 ? 394 GLY A CA    1 
ATOM   2988 C  C     . GLY A 1 395 ? 23.992 -12.013 8.968   1.00 0.00 ? 394 GLY A C     1 
ATOM   2989 O  O     . GLY A 1 395 ? 24.005 -13.186 9.370   1.00 0.00 ? 394 GLY A O     1 
ATOM   2990 N  N     . ALA A 1 396 ? 23.759 -11.644 7.700   1.00 0.00 ? 395 ALA A N     1 
ATOM   2991 C  CA    . ALA A 1 396 ? 23.270 -12.560 6.632   1.00 0.00 ? 395 ALA A CA    1 
ATOM   2992 C  C     . ALA A 1 396 ? 24.172 -13.752 6.471   1.00 0.00 ? 395 ALA A C     1 
ATOM   2993 O  O     . ALA A 1 396 ? 23.707 -14.899 6.393   1.00 0.00 ? 395 ALA A O     1 
ATOM   2994 C  CB    . ALA A 1 396 ? 23.207 -11.822 5.293   1.00 0.00 ? 395 ALA A CB    1 
ATOM   2995 N  N     . SER A 1 397 ? 25.425 -13.431 6.429   1.00 0.00 ? 396 SER A N     1 
ATOM   2996 C  CA    . SER A 1 397 ? 26.463 -14.427 6.284   1.00 0.00 ? 396 SER A CA    1 
ATOM   2997 C  C     . SER A 1 397 ? 26.362 -15.455 7.408   1.00 0.00 ? 396 SER A C     1 
ATOM   2998 O  O     . SER A 1 397 ? 26.403 -16.670 7.165   1.00 0.00 ? 396 SER A O     1 
ATOM   2999 C  CB    . SER A 1 397 ? 27.839 -13.771 6.374   1.00 0.00 ? 396 SER A CB    1 
ATOM   3000 O  OG    . SER A 1 397 ? 28.553 -14.296 7.483   1.00 0.00 ? 396 SER A OG    1 
ATOM   3001 N  N     . LEU A 1 398 ? 26.230 -14.939 8.628   1.00 0.00 ? 397 LEU A N     1 
ATOM   3002 C  CA    . LEU A 1 398 ? 26.208 -15.784 9.835   1.00 0.00 ? 397 LEU A CA    1 
ATOM   3003 C  C     . LEU A 1 398 ? 25.114 -16.797 9.840   1.00 0.00 ? 397 LEU A C     1 
ATOM   3004 O  O     . LEU A 1 398 ? 25.356 -17.999 10.026  1.00 0.00 ? 397 LEU A O     1 
ATOM   3005 C  CB    . LEU A 1 398 ? 25.837 -15.032 11.089  1.00 0.00 ? 397 LEU A CB    1 
ATOM   3006 C  CG    . LEU A 1 398 ? 24.674 -15.734 11.800  1.00 0.00 ? 397 LEU A CG    1 
ATOM   3007 C  CD1   . LEU A 1 398 ? 23.912 -14.816 12.757  1.00 0.00 ? 397 LEU A CD1   1 
ATOM   3008 C  CD2   . LEU A 1 398 ? 23.624 -16.283 10.830  1.00 0.00 ? 397 LEU A CD2   1 
ATOM   3009 N  N     . GLU A 1 399 ? 23.914 -16.319 9.637   1.00 0.00 ? 398 GLU A N     1 
ATOM   3010 C  CA    . GLU A 1 399 ? 22.840 -17.261 9.610   1.00 0.00 ? 398 GLU A CA    1 
ATOM   3011 C  C     . GLU A 1 399 ? 23.286 -18.226 8.580   1.00 0.00 ? 398 GLU A C     1 
ATOM   3012 O  O     . GLU A 1 399 ? 23.185 -19.447 8.765   1.00 0.00 ? 398 GLU A O     1 
ATOM   3013 C  CB    . GLU A 1 399 ? 21.528 -16.655 9.134   1.00 0.00 ? 398 GLU A CB    1 
ATOM   3014 C  CG    . GLU A 1 399 ? 20.894 -17.522 8.031   1.00 0.00 ? 398 GLU A CG    1 
ATOM   3015 C  CD    . GLU A 1 399 ? 19.366 -17.471 7.997   1.00 0.00 ? 398 GLU A CD    1 
ATOM   3016 O  OE1   . GLU A 1 399 ? 18.744 -16.451 8.484   1.00 0.00 ? 398 GLU A OE1   1 
ATOM   3017 O  OE2   . GLU A 1 399 ? 18.700 -18.447 7.480   1.00 0.00 ? 398 GLU A OE2   1 
ATOM   3018 N  N     . LEU A 1 400 ? 23.759 -17.580 7.529   1.00 0.00 ? 399 LEU A N     1 
ATOM   3019 C  CA    . LEU A 1 400 ? 24.300 -18.259 6.365   1.00 0.00 ? 399 LEU A CA    1 
ATOM   3020 C  C     . LEU A 1 400 ? 25.426 -19.153 6.793   1.00 0.00 ? 399 LEU A C     1 
ATOM   3021 O  O     . LEU A 1 400 ? 25.497 -20.325 6.396   1.00 0.00 ? 399 LEU A O     1 
ATOM   3022 C  CB    . LEU A 1 400 ? 24.898 -17.288 5.367   1.00 0.00 ? 399 LEU A CB    1 
ATOM   3023 C  CG    . LEU A 1 400 ? 25.909 -17.992 4.458   1.00 0.00 ? 399 LEU A CG    1 
ATOM   3024 C  CD1   . LEU A 1 400 ? 27.244 -17.250 4.356   1.00 0.00 ? 399 LEU A CD1   1 
ATOM   3025 C  CD2   . LEU A 1 400 ? 26.256 -19.404 4.934   1.00 0.00 ? 399 LEU A CD2   1 
ATOM   3026 N  N     . LEU A 1 401 ? 26.240 -18.527 7.582   1.00 0.00 ? 400 LEU A N     1 
ATOM   3027 C  CA    . LEU A 1 401 ? 27.406 -19.128 8.176   1.00 0.00 ? 400 LEU A CA    1 
ATOM   3028 C  C     . LEU A 1 401 ? 26.931 -20.367 8.859   1.00 0.00 ? 400 LEU A C     1 
ATOM   3029 O  O     . LEU A 1 401 ? 27.578 -21.423 8.789   1.00 0.00 ? 400 LEU A O     1 
ATOM   3030 C  CB    . LEU A 1 401 ? 27.917 -18.171 9.267   1.00 0.00 ? 400 LEU A CB    1 
ATOM   3031 C  CG    . LEU A 1 401 ? 29.432 -18.170 9.464   1.00 0.00 ? 400 LEU A CG    1 
ATOM   3032 C  CD1   . LEU A 1 401 ? 29.986 -16.783 9.797   1.00 0.00 ? 400 LEU A CD1   1 
ATOM   3033 C  CD2   . LEU A 1 401 ? 29.889 -19.084 10.603  1.00 0.00 ? 400 LEU A CD2   1 
ATOM   3034 N  N     . GLU A 1 402 ? 25.821 -20.096 9.461   1.00 0.00 ? 401 GLU A N     1 
ATOM   3035 C  CA    . GLU A 1 402 ? 25.101 -20.978 10.343  1.00 0.00 ? 401 GLU A CA    1 
ATOM   3036 C  C     . GLU A 1 402 ? 24.842 -22.344 9.697   1.00 0.00 ? 401 GLU A C     1 
ATOM   3037 O  O     . GLU A 1 402 ? 25.089 -23.395 10.307  1.00 0.00 ? 401 GLU A O     1 
ATOM   3038 C  CB    . GLU A 1 402 ? 23.802 -20.258 10.712  1.00 0.00 ? 401 GLU A CB    1 
ATOM   3039 C  CG    . GLU A 1 402 ? 22.664 -21.177 11.128  1.00 0.00 ? 401 GLU A CG    1 
ATOM   3040 C  CD    . GLU A 1 402 ? 21.354 -20.413 11.338  1.00 0.00 ? 401 GLU A CD    1 
ATOM   3041 O  OE1   . GLU A 1 402 ? 21.245 -19.194 10.931  1.00 0.00 ? 401 GLU A OE1   1 
ATOM   3042 O  OE2   . GLU A 1 402 ? 20.359 -20.988 11.924  1.00 0.00 ? 401 GLU A OE2   1 
ATOM   3043 N  N     . GLY A 1 403 ? 24.347 -22.367 8.479   1.00 0.00 ? 402 GLY A N     1 
ATOM   3044 C  CA    . GLY A 1 403 ? 24.102 -23.650 7.796   1.00 0.00 ? 402 GLY A CA    1 
ATOM   3045 C  C     . GLY A 1 403 ? 22.712 -23.712 7.151   1.00 0.00 ? 402 GLY A C     1 
ATOM   3046 O  O     . GLY A 1 403 ? 22.386 -24.666 6.429   1.00 0.00 ? 402 GLY A O     1 
ATOM   3047 N  N     . LYS A 1 404 ? 21.898 -22.705 7.417   1.00 0.00 ? 403 LYS A N     1 
ATOM   3048 C  CA    . LYS A 1 404 ? 20.554 -22.632 6.815   1.00 0.00 ? 403 LYS A CA    1 
ATOM   3049 C  C     . LYS A 1 404 ? 20.706 -22.899 5.307   1.00 0.00 ? 403 LYS A C     1 
ATOM   3050 O  O     . LYS A 1 404 ? 21.827 -23.001 4.787   1.00 0.00 ? 403 LYS A O     1 
ATOM   3051 C  CB    . LYS A 1 404 ? 19.945 -21.247 7.048   1.00 0.00 ? 403 LYS A CB    1 
ATOM   3052 C  CG    . LYS A 1 404 ? 18.457 -21.182 6.695   1.00 0.00 ? 403 LYS A CG    1 
ATOM   3053 C  CD    . LYS A 1 404 ? 17.625 -20.440 7.744   1.00 0.00 ? 403 LYS A CD    1 
ATOM   3054 C  CE    . LYS A 1 404 ? 16.141 -20.811 7.701   1.00 0.00 ? 403 LYS A CE    1 
ATOM   3055 N  NZ    . LYS A 1 404 ? 15.664 -21.417 8.953   1.00 0.00 ? 403 LYS A NZ    1 
ATOM   3056 N  N     . GLU A 1 405 ? 19.579 -22.996 4.625   1.00 0.00 ? 404 GLU A N     1 
ATOM   3057 C  CA    . GLU A 1 405 ? 19.533 -23.319 3.174   1.00 0.00 ? 404 GLU A CA    1 
ATOM   3058 C  C     . GLU A 1 405 ? 20.148 -22.180 2.288   1.00 0.00 ? 404 GLU A C     1 
ATOM   3059 O  O     . GLU A 1 405 ? 20.849 -22.448 1.300   1.00 0.00 ? 404 GLU A O     1 
ATOM   3060 C  CB    . GLU A 1 405 ? 18.071 -23.587 2.754   1.00 0.00 ? 404 GLU A CB    1 
ATOM   3061 C  CG    . GLU A 1 405 ? 17.605 -25.009 3.103   1.00 0.00 ? 404 GLU A CG    1 
ATOM   3062 C  CD    . GLU A 1 405 ? 16.081 -25.178 3.079   1.00 0.00 ? 404 GLU A CD    1 
ATOM   3063 O  OE1   . GLU A 1 405 ? 15.323 -24.276 3.604   1.00 0.00 ? 404 GLU A OE1   1 
ATOM   3064 O  OE2   . GLU A 1 405 ? 15.556 -26.222 2.532   1.00 0.00 ? 404 GLU A OE2   1 
ATOM   3065 N  N     . LEU A 1 406 ? 19.874 -20.922 2.662   1.00 0.00 ? 405 LEU A N     1 
ATOM   3066 C  CA    . LEU A 1 406 ? 20.341 -19.698 1.930   1.00 0.00 ? 405 LEU A CA    1 
ATOM   3067 C  C     . LEU A 1 406 ? 19.582 -19.570 0.599   1.00 0.00 ? 405 LEU A C     1 
ATOM   3068 O  O     . LEU A 1 406 ? 19.833 -20.323 -0.354  1.00 0.00 ? 405 LEU A O     1 
ATOM   3069 C  CB    . LEU A 1 406 ? 21.849 -19.739 1.701   1.00 0.00 ? 405 LEU A CB    1 
ATOM   3070 C  CG    . LEU A 1 406 ? 22.564 -18.581 2.403   1.00 0.00 ? 405 LEU A CG    1 
ATOM   3071 C  CD1   . LEU A 1 406 ? 22.244 -18.499 3.897   1.00 0.00 ? 405 LEU A CD1   1 
ATOM   3072 C  CD2   . LEU A 1 406 ? 24.089 -18.674 2.311   1.00 0.00 ? 405 LEU A CD2   1 
ATOM   3073 N  N     . PRO A 1 407 ? 18.638 -18.618 0.501   1.00 0.00 ? 406 PRO A N     1 
ATOM   3074 C  CA    . PRO A 1 407 ? 17.753 -18.510 -0.669  1.00 0.00 ? 406 PRO A CA    1 
ATOM   3075 C  C     . PRO A 1 407 ? 18.418 -18.246 -2.011  1.00 0.00 ? 406 PRO A C     1 
ATOM   3076 O  O     . PRO A 1 407 ? 18.242 -19.072 -2.960  1.00 0.00 ? 406 PRO A O     1 
ATOM   3077 C  CB    . PRO A 1 407 ? 16.874 -17.326 -0.331  1.00 0.00 ? 406 PRO A CB    1 
ATOM   3078 C  CG    . PRO A 1 407 ? 17.296 -16.793 1.033   1.00 0.00 ? 406 PRO A CG    1 
ATOM   3079 C  CD    . PRO A 1 407 ? 18.423 -17.626 1.555   1.00 0.00 ? 406 PRO A CD    1 
ATOM   3080 N  N     . GLY A 1 408 ? 19.161 -17.155 -2.072  1.00 0.00 ? 407 GLY A N     1 
ATOM   3081 C  CA    . GLY A 1 408 ? 19.845 -16.702 -3.302  1.00 0.00 ? 407 GLY A CA    1 
ATOM   3082 C  C     . GLY A 1 408 ? 20.805 -17.774 -3.783  1.00 0.00 ? 407 GLY A C     1 
ATOM   3083 O  O     . GLY A 1 408 ? 20.852 -18.102 -4.978  1.00 0.00 ? 407 GLY A O     1 
ATOM   3084 N  N     . VAL A 1 409 ? 21.516 -18.251 -2.797  1.00 0.00 ? 408 VAL A N     1 
ATOM   3085 C  CA    . VAL A 1 409 ? 22.553 -19.266 -2.942  1.00 0.00 ? 408 VAL A CA    1 
ATOM   3086 C  C     . VAL A 1 409 ? 21.993 -20.518 -3.638  1.00 0.00 ? 408 VAL A C     1 
ATOM   3087 O  O     . VAL A 1 409 ? 22.620 -21.075 -4.551  1.00 0.00 ? 408 VAL A O     1 
ATOM   3088 C  CB    . VAL A 1 409 ? 23.074 -19.636 -1.554  1.00 0.00 ? 408 VAL A CB    1 
ATOM   3089 C  CG1   . VAL A 1 409 ? 23.613 -21.066 -1.479  1.00 0.00 ? 408 VAL A CG1   1 
ATOM   3090 C  CG2   . VAL A 1 409 ? 24.220 -18.736 -1.087  1.00 0.00 ? 408 VAL A CG2   1 
ATOM   3091 N  N     . ALA A 1 410 ? 20.822 -20.922 -3.181  1.00 0.00 ? 409 ALA A N     1 
ATOM   3092 C  CA    . ALA A 1 410 ? 20.102 -22.107 -3.695  1.00 0.00 ? 409 ALA A CA    1 
ATOM   3093 C  C     . ALA A 1 410 ? 19.891 -22.001 -5.208  1.00 0.00 ? 409 ALA A C     1 
ATOM   3094 O  O     . ALA A 1 410 ? 20.090 -22.974 -5.951  1.00 0.00 ? 409 ALA A O     1 
ATOM   3095 C  CB    . ALA A 1 410 ? 18.733 -22.222 -3.022  1.00 0.00 ? 409 ALA A CB    1 
ATOM   3096 N  N     . PHE A 1 411 ? 19.493 -20.811 -5.618  1.00 0.00 ? 410 PHE A N     1 
ATOM   3097 C  CA    . PHE A 1 411 ? 19.221 -20.520 -7.026  1.00 0.00 ? 410 PHE A CA    1 
ATOM   3098 C  C     . PHE A 1 411 ? 20.433 -20.968 -7.831  1.00 0.00 ? 410 PHE A C     1 
ATOM   3099 O  O     . PHE A 1 411 ? 20.299 -21.547 -8.919  1.00 0.00 ? 410 PHE A O     1 
ATOM   3100 C  CB    . PHE A 1 411 ? 18.937 -19.031 -7.227  1.00 0.00 ? 410 PHE A CB    1 
ATOM   3101 C  CG    . PHE A 1 411 ? 17.581 -18.786 -7.897  1.00 0.00 ? 410 PHE A CG    1 
ATOM   3102 C  CD1   . PHE A 1 411 ? 17.476 -17.890 -8.969  1.00 0.00 ? 410 PHE A CD1   1 
ATOM   3103 C  CD2   . PHE A 1 411 ? 16.443 -19.463 -7.440  1.00 0.00 ? 410 PHE A CD2   1 
ATOM   3104 C  CE1   . PHE A 1 411 ? 16.235 -17.672 -9.582  1.00 0.00 ? 410 PHE A CE1   1 
ATOM   3105 C  CE2   . PHE A 1 411 ? 15.203 -19.246 -8.054  1.00 0.00 ? 410 PHE A CE2   1 
ATOM   3106 C  CZ    . PHE A 1 411 ? 15.099 -18.350 -9.125  1.00 0.00 ? 410 PHE A CZ    1 
ATOM   3107 N  N     . LEU A 1 412 ? 21.589 -20.675 -7.279  1.00 0.00 ? 411 LEU A N     1 
ATOM   3108 C  CA    . LEU A 1 412 ? 22.863 -21.102 -7.866  1.00 0.00 ? 411 LEU A CA    1 
ATOM   3109 C  C     . LEU A 1 412 ? 23.012 -22.624 -7.727  1.00 0.00 ? 411 LEU A C     1 
ATOM   3110 O  O     . LEU A 1 412 ? 22.600 -23.218 -6.719  1.00 0.00 ? 411 LEU A O     1 
ATOM   3111 C  CB    . LEU A 1 412 ? 24.020 -20.406 -7.164  1.00 0.00 ? 411 LEU A CB    1 
ATOM   3112 C  CG    . LEU A 1 412 ? 24.513 -19.188 -7.940  1.00 0.00 ? 411 LEU A CG    1 
ATOM   3113 C  CD1   . LEU A 1 412 ? 23.431 -18.125 -8.134  1.00 0.00 ? 411 LEU A CD1   1 
ATOM   3114 C  CD2   . LEU A 1 412 ? 25.679 -18.474 -7.254  1.00 0.00 ? 411 LEU A CD2   1 
ATOM   3115 N  N     . SER A 1 413 ? 23.605 -23.201 -8.758  1.00 0.00 ? 412 SER A N     1 
ATOM   3116 C  CA    . SER A 1 413 ? 23.814 -24.653 -8.847  1.00 0.00 ? 412 SER A CA    1 
ATOM   3117 C  C     . SER A 1 413 ? 25.254 -24.974 -9.256  1.00 0.00 ? 412 SER A C     1 
ATOM   3118 O  O     . SER A 1 413 ? 25.983 -25.670 -8.533  1.00 0.00 ? 412 SER A O     1 
ATOM   3119 C  CB    . SER A 1 413 ? 22.865 -25.240 -9.895  1.00 0.00 ? 412 SER A CB    1 
ATOM   3120 O  OG    . SER A 1 413 ? 22.945 -26.658 -9.884  1.00 0.00 ? 412 SER A OG    1 
ATOM   3121 N  N     . GLU A 1 414 ? 25.605 -24.446 -10.420 1.00 0.00 ? 413 GLU A N     1 
ATOM   3122 C  CA    . GLU A 1 414 ? 26.930 -24.641 -11.033 1.00 0.00 ? 413 GLU A CA    1 
ATOM   3123 C  C     . GLU A 1 414 ? 26.900 -24.307 -12.541 1.00 0.00 ? 413 GLU A C     1 
ATOM   3124 O  O     . GLU A 1 414 ? 27.494 -25.018 -13.364 1.00 0.00 ? 413 GLU A O     1 
ATOM   3125 C  CB    . GLU A 1 414 ? 27.339 -26.125 -10.969 1.00 0.00 ? 413 GLU A CB    1 
ATOM   3126 C  CG    . GLU A 1 414 ? 27.904 -26.589 -9.625  1.00 0.00 ? 413 GLU A CG    1 
ATOM   3127 C  CD    . GLU A 1 414 ? 28.166 -28.102 -9.597  1.00 0.00 ? 413 GLU A CD    1 
ATOM   3128 O  OE1   . GLU A 1 414 ? 27.384 -28.904 -10.236 1.00 0.00 ? 413 GLU A OE1   1 
ATOM   3129 O  OE2   . GLU A 1 414 ? 29.169 -28.571 -8.934  1.00 0.00 ? 413 GLU A OE2   1 
ATOM   3130 N  N     . LYS A 1 415 ? 26.215 -23.230 -12.927 1.00 0.00 ? 414 LYS A N     1 
ATOM   3131 C  CA    . LYS A 1 415 ? 26.099 -22.877 -14.370 1.00 0.00 ? 414 LYS A CA    1 
ATOM   3132 C  C     . LYS A 1 415 ? 25.319 -24.019 -15.046 1.00 0.00 ? 414 LYS A C     1 
ATOM   3133 O  O     . LYS A 1 415 ? 25.647 -25.203 -14.879 1.00 0.00 ? 414 LYS A O     1 
ATOM   3134 C  CB    . LYS A 1 415 ? 27.544 -22.730 -14.959 1.00 0.00 ? 414 LYS A CB    1 
ATOM   3135 C  CG    . LYS A 1 415 ? 27.683 -22.805 -16.503 1.00 0.00 ? 414 LYS A CG    1 
ATOM   3136 C  CD    . LYS A 1 415 ? 29.147 -22.604 -16.978 1.00 0.00 ? 414 LYS A CD    1 
ATOM   3137 C  CE    . LYS A 1 415 ? 29.366 -22.831 -18.483 1.00 0.00 ? 414 LYS A CE    1 
ATOM   3138 N  NZ    . LYS A 1 415 ? 30.776 -22.704 -18.885 1.00 0.00 ? 414 LYS A NZ    1 
ATOM   3139 N  N     . LYS A 1 416 ? 24.258 -23.711 -15.804 1.00 0.00 ? 415 LYS A N     1 
ATOM   3140 C  CA    . LYS A 1 416 ? 23.547 -24.810 -16.514 1.00 0.00 ? 415 LYS A CA    1 
ATOM   3141 C  C     . LYS A 1 416 ? 22.031 -24.583 -16.815 1.00 0.00 ? 415 LYS A C     1 
ATOM   3142 O  O     . LYS A 1 416 ? 21.157 -24.997 -16.039 1.00 0.00 ? 415 LYS A O     1 
ATOM   3143 C  CB    . LYS A 1 416 ? 23.586 -26.101 -15.667 1.00 0.00 ? 415 LYS A CB    1 
ATOM   3144 C  CG    . LYS A 1 416 ? 24.980 -26.739 -15.558 1.00 0.00 ? 415 LYS A CG    1 
ATOM   3145 C  CD    . LYS A 1 416 ? 24.979 -28.056 -14.764 1.00 0.00 ? 415 LYS A CD    1 
ATOM   3146 C  CE    . LYS A 1 416 ? 26.357 -28.724 -14.695 1.00 0.00 ? 415 LYS A CE    1 
ATOM   3147 N  NZ    . LYS A 1 416 ? 26.317 -30.063 -14.089 1.00 0.00 ? 415 LYS A NZ    1 
ATOM   3148 O  OXT   . LYS A 1 416 ? 21.713 -23.906 -17.936 1.00 0.00 ? 415 LYS A OXT   1 
HETATM 3149 MG MG    . MG  B 2 .   ? 25.800 -5.000  15.700  1.00 0.00 ? 416 MG  A MG    1 
HETATM 3150 P  PG    . ATP C 3 .   ? 26.299 -7.663  15.877  1.00 0.00 ? 417 ATP A PG    1 
HETATM 3151 O  O1G   . ATP C 3 .   ? 26.984 -6.784  16.851  1.00 0.00 ? 417 ATP A O1G   1 
HETATM 3152 O  O2G   . ATP C 3 .   ? 26.302 -7.005  14.551  1.00 0.00 ? 417 ATP A O2G   1 
HETATM 3153 O  O3G   . ATP C 3 .   ? 25.202 -7.867  14.904  1.00 0.00 ? 417 ATP A O3G   1 
HETATM 3154 P  PB    . ATP C 3 .   ? 27.231 -10.276 16.793  1.00 0.00 ? 417 ATP A PB    1 
HETATM 3155 O  O1B   . ATP C 3 .   ? 25.966 -10.686 17.443  1.00 0.00 ? 417 ATP A O1B   1 
HETATM 3156 O  O2B   . ATP C 3 .   ? 27.899 -11.472 16.236  1.00 0.00 ? 417 ATP A O2B   1 
HETATM 3157 O  O3B   . ATP C 3 .   ? 27.069 -9.112  15.786  1.00 0.00 ? 417 ATP A O3B   1 
HETATM 3158 P  PA    . ATP C 3 .   ? 27.839 -9.007  19.234  1.00 0.00 ? 417 ATP A PA    1 
HETATM 3159 O  O1A   . ATP C 3 .   ? 26.579 -8.233  19.223  1.00 0.00 ? 417 ATP A O1A   1 
HETATM 3160 O  O2A   . ATP C 3 .   ? 27.757 -10.065 20.266  1.00 0.00 ? 417 ATP A O2A   1 
HETATM 3161 O  O3A   . ATP C 3 .   ? 28.192 -9.563  17.876  1.00 0.00 ? 417 ATP A O3A   1 
HETATM 3162 O  "O5'" . ATP C 3 .   ? 29.043 -8.062  19.532  1.00 0.00 ? 417 ATP A "O5'" 1 
HETATM 3163 C  "C5'" . ATP C 3 .   ? 29.378 -7.944  20.887  1.00 0.00 ? 417 ATP A "C5'" 1 
HETATM 3164 C  "C4'" . ATP C 3 .   ? 28.508 -6.926  21.566  1.00 0.00 ? 417 ATP A "C4'" 1 
HETATM 3165 O  "O4'" . ATP C 3 .   ? 28.064 -7.493  22.810  1.00 0.00 ? 417 ATP A "O4'" 1 
HETATM 3166 C  "C3'" . ATP C 3 .   ? 29.295 -5.693  21.908  1.00 0.00 ? 417 ATP A "C3'" 1 
HETATM 3167 O  "O3'" . ATP C 3 .   ? 29.297 -4.776  20.797  1.00 0.00 ? 417 ATP A "O3'" 1 
HETATM 3168 C  "C2'" . ATP C 3 .   ? 28.599 -5.217  23.166  1.00 0.00 ? 417 ATP A "C2'" 1 
HETATM 3169 O  "O2'" . ATP C 3 .   ? 27.485 -4.346  22.894  1.00 0.00 ? 417 ATP A "O2'" 1 
HETATM 3170 C  "C1'" . ATP C 3 .   ? 28.134 -6.540  23.798  1.00 0.00 ? 417 ATP A "C1'" 1 
HETATM 3171 N  N9    . ATP C 3 .   ? 29.005 -7.147  24.743  1.00 0.00 ? 417 ATP A N9    1 
HETATM 3172 C  C8    . ATP C 3 .   ? 29.412 -8.433  24.639  1.00 0.00 ? 417 ATP A C8    1 
HETATM 3173 N  N7    . ATP C 3 .   ? 30.147 -8.915  25.551  1.00 0.00 ? 417 ATP A N7    1 
HETATM 3174 C  C5    . ATP C 3 .   ? 30.274 -7.895  26.335  1.00 0.00 ? 417 ATP A C5    1 
HETATM 3175 C  C6    . ATP C 3 .   ? 30.994 -7.827  27.495  1.00 0.00 ? 417 ATP A C6    1 
HETATM 3176 N  N6    . ATP C 3 .   ? 31.688 -8.828  28.028  1.00 0.00 ? 417 ATP A N6    1 
HETATM 3177 N  N1    . ATP C 3 .   ? 30.977 -6.640  28.117  1.00 0.00 ? 417 ATP A N1    1 
HETATM 3178 C  C2    . ATP C 3 .   ? 30.261 -5.607  27.562  1.00 0.00 ? 417 ATP A C2    1 
HETATM 3179 N  N3    . ATP C 3 .   ? 29.556 -5.585  26.474  1.00 0.00 ? 417 ATP A N3    1 
HETATM 3180 C  C4    . ATP C 3 .   ? 29.601 -6.774  25.885  1.00 0.00 ? 417 ATP A C4    1 
HETATM 3181 C  C1    . 3PG D 4 .   ? 24.605 -6.221  10.041  1.00 0.00 ? 418 3PG A C1    1 
HETATM 3182 O  O1    . 3PG D 4 .   ? 24.052 -5.073  9.846   1.00 0.00 ? 418 3PG A O1    1 
HETATM 3183 O  O2    . 3PG D 4 .   ? 24.762 -6.666  11.242  1.00 0.00 ? 418 3PG A O2    1 
HETATM 3184 C  C2    . 3PG D 4 .   ? 25.074 -7.052  8.848   1.00 0.00 ? 418 3PG A C2    1 
HETATM 3185 O  O3    . 3PG D 4 .   ? 26.466 -6.865  8.643   1.00 0.00 ? 418 3PG A O3    1 
HETATM 3186 C  C3    . 3PG D 4 .   ? 24.311 -6.631  7.585   1.00 0.00 ? 418 3PG A C3    1 
HETATM 3187 O  O1P   . 3PG D 4 .   ? 24.619 -5.270  7.220   1.00 0.00 ? 418 3PG A O1P   1 
HETATM 3188 P  P     . 3PG D 4 .   ? 24.213 -4.733  5.765   1.00 0.00 ? 418 3PG A P     1 
HETATM 3189 O  O2P   . 3PG D 4 .   ? 22.839 -4.184  5.792   1.00 0.00 ? 418 3PG A O2P   1 
HETATM 3190 O  O3P   . 3PG D 4 .   ? 24.267 -5.841  4.785   1.00 0.00 ? 418 3PG A O3P   1 
HETATM 3191 O  O4P   . 3PG D 4 .   ? 25.148 -3.668  5.338   1.00 0.00 ? 418 3PG A O4P   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   ACE 1   0   0   ACE ACE A . n 
A 1 2   SER 2   1   1   SER SER A . n 
A 1 3   LEU 3   2   2   LEU LEU A . n 
A 1 4   SER 4   3   3   SER SER A . n 
A 1 5   SER 5   4   4   SER SER A . n 
A 1 6   LYS 6   5   5   LYS LYS A . n 
A 1 7   LEU 7   6   6   LEU LEU A . n 
A 1 8   SER 8   7   7   SER SER A . n 
A 1 9   VAL 9   8   8   VAL VAL A . n 
A 1 10  GLN 10  9   9   GLN GLN A . n 
A 1 11  ASP 11  10  10  ASP ASP A . n 
A 1 12  LEU 12  11  11  LEU LEU A . n 
A 1 13  ASP 13  12  12  ASP ASP A . n 
A 1 14  LEU 14  13  13  LEU LEU A . n 
A 1 15  LYS 15  14  14  LYS LYS A . n 
A 1 16  ASP 16  15  15  ASP ASP A . n 
A 1 17  LYS 17  16  16  LYS LYS A . n 
A 1 18  ARG 18  17  17  ARG ARG A . n 
A 1 19  VAL 19  18  18  VAL VAL A . n 
A 1 20  PHE 20  19  19  PHE PHE A . n 
A 1 21  ILE 21  20  20  ILE ILE A . n 
A 1 22  ARG 22  21  21  ARG ARG A . n 
A 1 23  VAL 23  22  22  VAL VAL A . n 
A 1 24  ASP 24  23  23  ASP ASP A . n 
A 1 25  PHE 25  24  24  PHE PHE A . n 
A 1 26  ASN 26  25  25  ASN ASN A . n 
A 1 27  VAL 27  26  26  VAL VAL A . n 
A 1 28  PRO 28  27  27  PRO PRO A . n 
A 1 29  LEU 29  28  28  LEU LEU A . n 
A 1 30  ASP 30  29  29  ASP ASP A . n 
A 1 31  GLY 31  30  30  GLY GLY A . n 
A 1 32  LYS 32  31  31  LYS LYS A . n 
A 1 33  LYS 33  32  32  LYS LYS A . n 
A 1 34  ILE 34  33  33  ILE ILE A . n 
A 1 35  THR 35  34  34  THR THR A . n 
A 1 36  SER 36  35  35  SER SER A . n 
A 1 37  ASN 37  36  36  ASN ASN A . n 
A 1 38  GLN 38  37  37  GLN GLN A . n 
A 1 39  ARG 39  38  38  ARG ARG A . n 
A 1 40  ILE 40  39  39  ILE ILE A . n 
A 1 41  VAL 41  40  40  VAL VAL A . n 
A 1 42  ALA 42  41  41  ALA ALA A . n 
A 1 43  ALA 43  42  42  ALA ALA A . n 
A 1 44  LEU 44  43  43  LEU LEU A . n 
A 1 45  PRO 45  44  44  PRO PRO A . n 
A 1 46  THR 46  45  45  THR THR A . n 
A 1 47  ILE 47  46  46  ILE ILE A . n 
A 1 48  LYS 48  47  47  LYS LYS A . n 
A 1 49  TYR 49  48  48  TYR TYR A . n 
A 1 50  VAL 50  49  49  VAL VAL A . n 
A 1 51  LEU 51  50  50  LEU LEU A . n 
A 1 52  GLU 52  51  51  GLU GLU A . n 
A 1 53  HIS 53  52  52  HIS HIS A . n 
A 1 54  HIS 54  53  53  HIS HIS A . n 
A 1 55  PRO 55  54  54  PRO PRO A . n 
A 1 56  ARG 56  55  55  ARG ARG A . n 
A 1 57  TYR 57  56  56  TYR TYR A . n 
A 1 58  VAL 58  57  57  VAL VAL A . n 
A 1 59  VAL 59  58  58  VAL VAL A . n 
A 1 60  LEU 60  59  59  LEU LEU A . n 
A 1 61  ALA 61  60  60  ALA ALA A . n 
A 1 62  SER 62  61  61  SER SER A . n 
A 1 63  HIS 63  62  62  HIS HIS A . n 
A 1 64  LEU 64  63  63  LEU LEU A . n 
A 1 65  GLY 65  64  64  GLY GLY A . n 
A 1 66  ARG 66  65  65  ARG ARG A . n 
A 1 67  PRO 67  66  66  PRO PRO A . n 
A 1 68  ASN 68  67  67  ASN ASN A . n 
A 1 69  GLY 69  68  68  GLY GLY A . n 
A 1 70  GLU 70  69  69  GLU GLU A . n 
A 1 71  ARG 71  70  70  ARG ARG A . n 
A 1 72  ASN 72  71  71  ASN ASN A . n 
A 1 73  GLU 73  72  72  GLU GLU A . n 
A 1 74  LYS 74  73  73  LYS LYS A . n 
A 1 75  TYR 75  74  74  TYR TYR A . n 
A 1 76  SER 76  75  75  SER SER A . n 
A 1 77  LEU 77  76  76  LEU LEU A . n 
A 1 78  ALA 78  77  77  ALA ALA A . n 
A 1 79  PRO 79  78  78  PRO PRO A . n 
A 1 80  VAL 80  79  79  VAL VAL A . n 
A 1 81  ALA 81  80  80  ALA ALA A . n 
A 1 82  LYS 82  81  81  LYS LYS A . n 
A 1 83  GLU 83  82  82  GLU GLU A . n 
A 1 84  LEU 84  83  83  LEU LEU A . n 
A 1 85  GLN 85  84  84  GLN GLN A . n 
A 1 86  SER 86  85  85  SER SER A . n 
A 1 87  LEU 87  86  86  LEU LEU A . n 
A 1 88  LEU 88  87  87  LEU LEU A . n 
A 1 89  GLY 89  88  88  GLY GLY A . n 
A 1 90  LYS 90  89  89  LYS LYS A . n 
A 1 91  ASP 91  90  90  ASP ASP A . n 
A 1 92  VAL 92  91  91  VAL VAL A . n 
A 1 93  THR 93  92  92  THR THR A . n 
A 1 94  PHE 94  93  93  PHE PHE A . n 
A 1 95  LEU 95  94  94  LEU LEU A . n 
A 1 96  ASN 96  95  95  ASN ASN A . n 
A 1 97  ASP 97  96  96  ASP ASP A . n 
A 1 98  CYS 98  97  97  CYS CYS A . n 
A 1 99  VAL 99  98  98  VAL VAL A . n 
A 1 100 GLY 100 99  99  GLY GLY A . n 
A 1 101 PRO 101 100 100 PRO PRO A . n 
A 1 102 GLU 102 101 101 GLU GLU A . n 
A 1 103 VAL 103 102 102 VAL VAL A . n 
A 1 104 GLU 104 103 103 GLU GLU A . n 
A 1 105 ALA 105 104 104 ALA ALA A . n 
A 1 106 ALA 106 105 105 ALA ALA A . n 
A 1 107 VAL 107 106 106 VAL VAL A . n 
A 1 108 LYS 108 107 107 LYS LYS A . n 
A 1 109 ALA 109 108 108 ALA ALA A . n 
A 1 110 SER 110 109 109 SER SER A . n 
A 1 111 ALA 111 110 110 ALA ALA A . n 
A 1 112 PRO 112 111 111 PRO PRO A . n 
A 1 113 GLY 113 112 112 GLY GLY A . n 
A 1 114 SER 114 113 113 SER SER A . n 
A 1 115 VAL 115 114 114 VAL VAL A . n 
A 1 116 ILE 116 115 115 ILE ILE A . n 
A 1 117 LEU 117 116 116 LEU LEU A . n 
A 1 118 LEU 118 117 117 LEU LEU A . n 
A 1 119 GLU 119 118 118 GLU GLU A . n 
A 1 120 ASN 120 119 119 ASN ASN A . n 
A 1 121 LEU 121 120 120 LEU LEU A . n 
A 1 122 ARG 122 121 121 ARG ARG A . n 
A 1 123 TYR 123 122 122 TYR TYR A . n 
A 1 124 HIS 124 123 123 HIS HIS A . n 
A 1 125 ILE 125 124 124 ILE ILE A . n 
A 1 126 GLU 126 125 125 GLU GLU A . n 
A 1 127 GLU 127 126 126 GLU GLU A . n 
A 1 128 GLU 128 127 127 GLU GLU A . n 
A 1 129 GLY 129 128 128 GLY GLY A . n 
A 1 130 SER 130 129 129 SER SER A . n 
A 1 131 ARG 131 130 130 ARG ARG A . n 
A 1 132 LYS 132 131 131 LYS LYS A . n 
A 1 133 VAL 133 132 132 VAL VAL A . n 
A 1 134 ASP 134 133 133 ASP ASP A . n 
A 1 135 GLY 135 134 134 GLY GLY A . n 
A 1 136 GLN 136 135 135 GLN GLN A . n 
A 1 137 LYS 137 136 136 LYS LYS A . n 
A 1 138 VAL 138 137 137 VAL VAL A . n 
A 1 139 LYS 139 138 138 LYS LYS A . n 
A 1 140 ALA 140 139 139 ALA ALA A . n 
A 1 141 SER 141 140 140 SER SER A . n 
A 1 142 LYS 142 141 141 LYS LYS A . n 
A 1 143 GLU 143 142 142 GLU GLU A . n 
A 1 144 ASP 144 143 143 ASP ASP A . n 
A 1 145 VAL 145 144 144 VAL VAL A . n 
A 1 146 GLN 146 145 145 GLN GLN A . n 
A 1 147 LYS 147 146 146 LYS LYS A . n 
A 1 148 PHE 148 147 147 PHE PHE A . n 
A 1 149 ARG 149 148 148 ARG ARG A . n 
A 1 150 HIS 150 149 149 HIS HIS A . n 
A 1 151 GLU 151 150 150 GLU GLU A . n 
A 1 152 LEU 152 151 151 LEU LEU A . n 
A 1 153 SER 153 152 152 SER SER A . n 
A 1 154 SER 154 153 153 SER SER A . n 
A 1 155 LEU 155 154 154 LEU LEU A . n 
A 1 156 ALA 156 155 155 ALA ALA A . n 
A 1 157 ASP 157 156 156 ASP ASP A . n 
A 1 158 VAL 158 157 157 VAL VAL A . n 
A 1 159 TYR 159 158 158 TYR TYR A . n 
A 1 160 ILE 160 159 159 ILE ILE A . n 
A 1 161 ASN 161 160 160 ASN ASN A . n 
A 1 162 ASP 162 161 161 ASP ASP A . n 
A 1 163 ALA 163 162 162 ALA ALA A . n 
A 1 164 PHE 164 163 163 PHE PHE A . n 
A 1 165 GLY 165 164 164 GLY GLY A . n 
A 1 166 THR 166 165 165 THR THR A . n 
A 1 167 ALA 167 166 166 ALA ALA A . n 
A 1 168 HIS 168 167 167 HIS HIS A . n 
A 1 169 ARG 169 168 168 ARG ARG A . n 
A 1 170 ALA 170 169 169 ALA ALA A . n 
A 1 171 HIS 171 170 170 HIS HIS A . n 
A 1 172 SER 172 171 171 SER SER A . n 
A 1 173 SER 173 172 172 SER SER A . n 
A 1 174 MET 174 173 173 MET MET A . n 
A 1 175 VAL 175 174 174 VAL VAL A . n 
A 1 176 GLY 176 175 175 GLY GLY A . n 
A 1 177 PHE 177 176 176 PHE PHE A . n 
A 1 178 ASP 178 177 177 ASP ASP A . n 
A 1 179 LEU 179 178 178 LEU LEU A . n 
A 1 180 PRO 180 179 179 PRO PRO A . n 
A 1 181 GLN 181 180 180 GLN GLN A . n 
A 1 182 ARG 182 181 181 ARG ARG A . n 
A 1 183 ALA 183 182 182 ALA ALA A . n 
A 1 184 ALA 184 183 183 ALA ALA A . n 
A 1 185 GLY 185 184 184 GLY GLY A . n 
A 1 186 PHE 186 185 185 PHE PHE A . n 
A 1 187 LEU 187 186 186 LEU LEU A . n 
A 1 188 LEU 188 187 187 LEU LEU A . n 
A 1 189 GLU 189 188 188 GLU GLU A . n 
A 1 190 LYS 190 189 189 LYS LYS A . n 
A 1 191 GLU 191 190 190 GLU GLU A . n 
A 1 192 LEU 192 191 191 LEU LEU A . n 
A 1 193 LYS 193 192 192 LYS LYS A . n 
A 1 194 TYR 194 193 193 TYR TYR A . n 
A 1 195 PHE 195 194 194 PHE PHE A . n 
A 1 196 GLY 196 195 195 GLY GLY A . n 
A 1 197 LYS 197 196 196 LYS LYS A . n 
A 1 198 ALA 198 197 197 ALA ALA A . n 
A 1 199 LEU 199 198 198 LEU LEU A . n 
A 1 200 GLU 200 199 199 GLU GLU A . n 
A 1 201 ASN 201 200 200 ASN ASN A . n 
A 1 202 PRO 202 201 201 PRO PRO A . n 
A 1 203 THR 203 202 202 THR THR A . n 
A 1 204 ARG 204 203 203 ARG ARG A . n 
A 1 205 PRO 205 204 204 PRO PRO A . n 
A 1 206 PHE 206 205 205 PHE PHE A . n 
A 1 207 LEU 207 206 206 LEU LEU A . n 
A 1 208 ALA 208 207 207 ALA ALA A . n 
A 1 209 ILE 209 208 208 ILE ILE A . n 
A 1 210 LEU 210 209 209 LEU LEU A . n 
A 1 211 GLY 211 210 210 GLY GLY A . n 
A 1 212 GLY 212 211 211 GLY GLY A . n 
A 1 213 ALA 213 212 212 ALA ALA A . n 
A 1 214 LYS 214 213 213 LYS LYS A . n 
A 1 215 VAL 215 214 214 VAL VAL A . n 
A 1 216 ALA 216 215 215 ALA ALA A . n 
A 1 217 ASP 217 216 216 ASP ASP A . n 
A 1 218 LYS 218 217 217 LYS LYS A . n 
A 1 219 ILE 219 218 218 ILE ILE A . n 
A 1 220 GLN 220 219 219 GLN GLN A . n 
A 1 221 LEU 221 220 220 LEU LEU A . n 
A 1 222 ILE 222 221 221 ILE ILE A . n 
A 1 223 ASP 223 222 222 ASP ASP A . n 
A 1 224 ASN 224 223 223 ASN ASN A . n 
A 1 225 LEU 225 224 224 LEU LEU A . n 
A 1 226 LEU 226 225 225 LEU LEU A . n 
A 1 227 ASP 227 226 226 ASP ASP A . n 
A 1 228 LYS 228 227 227 LYS LYS A . n 
A 1 229 VAL 229 228 228 VAL VAL A . n 
A 1 230 ASP 230 229 229 ASP ASP A . n 
A 1 231 SER 231 230 230 SER SER A . n 
A 1 232 ILE 232 231 231 ILE ILE A . n 
A 1 233 ILE 233 232 232 ILE ILE A . n 
A 1 234 ILE 234 233 233 ILE ILE A . n 
A 1 235 GLY 235 234 234 GLY GLY A . n 
A 1 236 GLY 236 235 235 GLY GLY A . n 
A 1 237 GLY 237 236 236 GLY GLY A . n 
A 1 238 MET 238 237 237 MET MET A . n 
A 1 239 ALA 239 238 238 ALA ALA A . n 
A 1 240 PHE 240 239 239 PHE PHE A . n 
A 1 241 THR 241 240 240 THR THR A . n 
A 1 242 PHE 242 241 241 PHE PHE A . n 
A 1 243 LYS 243 242 242 LYS LYS A . n 
A 1 244 LYS 244 243 243 LYS LYS A . n 
A 1 245 VAL 245 244 244 VAL VAL A . n 
A 1 246 LEU 246 245 245 LEU LEU A . n 
A 1 247 GLU 247 246 246 GLU GLU A . n 
A 1 248 ASN 248 247 247 ASN ASN A . n 
A 1 249 THR 249 248 248 THR THR A . n 
A 1 250 GLU 250 249 249 GLU GLU A . n 
A 1 251 ILE 251 250 250 ILE ILE A . n 
A 1 252 GLY 252 251 251 GLY GLY A . n 
A 1 253 ASP 253 252 252 ASP ASP A . n 
A 1 254 SER 254 253 253 SER SER A . n 
A 1 255 ILE 255 254 254 ILE ILE A . n 
A 1 256 PHE 256 255 255 PHE PHE A . n 
A 1 257 ASP 257 256 256 ASP ASP A . n 
A 1 258 LYS 258 257 257 LYS LYS A . n 
A 1 259 ALA 259 258 258 ALA ALA A . n 
A 1 260 VAL 260 259 259 VAL VAL A . n 
A 1 261 GLY 261 260 260 GLY GLY A . n 
A 1 262 PRO 262 261 261 PRO PRO A . n 
A 1 263 GLU 263 262 262 GLU GLU A . n 
A 1 264 ILE 264 263 263 ILE ILE A . n 
A 1 265 ALA 265 264 264 ALA ALA A . n 
A 1 266 LYS 266 265 265 LYS LYS A . n 
A 1 267 LEU 267 266 266 LEU LEU A . n 
A 1 268 MET 268 267 267 MET MET A . n 
A 1 269 GLU 269 268 268 GLU GLU A . n 
A 1 270 LYS 270 269 269 LYS LYS A . n 
A 1 271 ALA 271 270 270 ALA ALA A . n 
A 1 272 LYS 272 271 271 LYS LYS A . n 
A 1 273 ALA 273 272 272 ALA ALA A . n 
A 1 274 LYS 274 273 273 LYS LYS A . n 
A 1 275 GLY 275 274 274 GLY GLY A . n 
A 1 276 VAL 276 275 275 VAL VAL A . n 
A 1 277 GLU 277 276 276 GLU GLU A . n 
A 1 278 VAL 278 277 277 VAL VAL A . n 
A 1 279 VAL 279 278 278 VAL VAL A . n 
A 1 280 LEU 280 279 279 LEU LEU A . n 
A 1 281 PRO 281 280 280 PRO PRO A . n 
A 1 282 VAL 282 281 281 VAL VAL A . n 
A 1 283 ASP 283 282 282 ASP ASP A . n 
A 1 284 PHE 284 283 283 PHE PHE A . n 
A 1 285 ILE 285 284 284 ILE ILE A . n 
A 1 286 ILE 286 285 285 ILE ILE A . n 
A 1 287 ALA 287 286 286 ALA ALA A . n 
A 1 288 ASP 288 287 287 ASP ASP A . n 
A 1 289 ALA 289 288 288 ALA ALA A . n 
A 1 290 PHE 290 289 289 PHE PHE A . n 
A 1 291 SER 291 290 290 SER SER A . n 
A 1 292 ALA 292 291 291 ALA ALA A . n 
A 1 293 SER 293 292 292 SER SER A . n 
A 1 294 ALA 294 293 293 ALA ALA A . n 
A 1 295 ASN 295 294 294 ASN ASN A . n 
A 1 296 THR 296 295 295 THR THR A . n 
A 1 297 LYS 297 296 296 LYS LYS A . n 
A 1 298 THR 298 297 297 THR THR A . n 
A 1 299 VAL 299 298 298 VAL VAL A . n 
A 1 300 THR 300 299 299 THR THR A . n 
A 1 301 ASP 301 300 300 ASP ASP A . n 
A 1 302 LYS 302 301 301 LYS LYS A . n 
A 1 303 GLU 303 302 302 GLU GLU A . n 
A 1 304 GLY 304 303 303 GLY GLY A . n 
A 1 305 ILE 305 304 304 ILE ILE A . n 
A 1 306 PRO 306 305 305 PRO PRO A . n 
A 1 307 ALA 307 306 306 ALA ALA A . n 
A 1 308 GLY 308 307 307 GLY GLY A . n 
A 1 309 TRP 309 308 308 TRP TRP A . n 
A 1 310 GLN 310 309 309 GLN GLN A . n 
A 1 311 GLY 311 310 310 GLY GLY A . n 
A 1 312 LEU 312 311 311 LEU LEU A . n 
A 1 313 ASP 313 312 312 ASP ASP A . n 
A 1 314 ASN 314 313 313 ASN ASN A . n 
A 1 315 GLY 315 314 314 GLY GLY A . n 
A 1 316 PRO 316 315 315 PRO PRO A . n 
A 1 317 GLU 317 316 316 GLU GLU A . n 
A 1 318 SER 318 317 317 SER SER A . n 
A 1 319 ARG 319 318 318 ARG ARG A . n 
A 1 320 LYS 320 319 319 LYS LYS A . n 
A 1 321 LEU 321 320 320 LEU LEU A . n 
A 1 322 PHE 322 321 321 PHE PHE A . n 
A 1 323 ALA 323 322 322 ALA ALA A . n 
A 1 324 ALA 324 323 323 ALA ALA A . n 
A 1 325 THR 325 324 324 THR THR A . n 
A 1 326 VAL 326 325 325 VAL VAL A . n 
A 1 327 ALA 327 326 326 ALA ALA A . n 
A 1 328 LYS 328 327 327 LYS LYS A . n 
A 1 329 ALA 329 328 328 ALA ALA A . n 
A 1 330 THR 330 329 329 THR THR A . n 
A 1 331 VAL 331 330 330 VAL VAL A . n 
A 1 332 ILE 332 331 331 ILE ILE A . n 
A 1 333 LEU 333 332 332 LEU LEU A . n 
A 1 334 TRP 334 333 333 TRP TRP A . n 
A 1 335 ASN 335 334 334 ASN ASN A . n 
A 1 336 GLY 336 335 335 GLY GLY A . n 
A 1 337 PRO 337 336 336 PRO PRO A . n 
A 1 338 PRO 338 337 337 PRO PRO A . n 
A 1 339 GLY 339 338 338 GLY GLY A . n 
A 1 340 VAL 340 339 339 VAL VAL A . n 
A 1 341 PHE 341 340 340 PHE PHE A . n 
A 1 342 GLU 342 341 341 GLU GLU A . n 
A 1 343 PHE 343 342 342 PHE PHE A . n 
A 1 344 GLU 344 343 343 GLU GLU A . n 
A 1 345 LYS 345 344 344 LYS LYS A . n 
A 1 346 PHE 346 345 345 PHE PHE A . n 
A 1 347 ALA 347 346 346 ALA ALA A . n 
A 1 348 ALA 348 347 347 ALA ALA A . n 
A 1 349 GLY 349 348 348 GLY GLY A . n 
A 1 350 THR 350 349 349 THR THR A . n 
A 1 351 LYS 351 350 350 LYS LYS A . n 
A 1 352 ALA 352 351 351 ALA ALA A . n 
A 1 353 LEU 353 352 352 LEU LEU A . n 
A 1 354 LEU 354 353 353 LEU LEU A . n 
A 1 355 ASP 355 354 354 ASP ASP A . n 
A 1 356 GLU 356 355 355 GLU GLU A . n 
A 1 357 VAL 357 356 356 VAL VAL A . n 
A 1 358 VAL 358 357 357 VAL VAL A . n 
A 1 359 LYS 359 358 358 LYS LYS A . n 
A 1 360 SER 360 359 359 SER SER A . n 
A 1 361 SER 361 360 360 SER SER A . n 
A 1 362 ALA 362 361 361 ALA ALA A . n 
A 1 363 ALA 363 362 362 ALA ALA A . n 
A 1 364 GLY 364 363 363 GLY GLY A . n 
A 1 365 ASN 365 364 364 ASN ASN A . n 
A 1 366 THR 366 365 365 THR THR A . n 
A 1 367 VAL 367 366 366 VAL VAL A . n 
A 1 368 ILE 368 367 367 ILE ILE A . n 
A 1 369 ILE 369 368 368 ILE ILE A . n 
A 1 370 GLY 370 369 369 GLY GLY A . n 
A 1 371 GLY 371 370 370 GLY GLY A . n 
A 1 372 GLY 372 371 371 GLY GLY A . n 
A 1 373 ASP 373 372 372 ASP ASP A . n 
A 1 374 THR 374 373 373 THR THR A . n 
A 1 375 ALA 375 374 374 ALA ALA A . n 
A 1 376 THR 376 375 375 THR THR A . n 
A 1 377 VAL 377 376 376 VAL VAL A . n 
A 1 378 ALA 378 377 377 ALA ALA A . n 
A 1 379 LYS 379 378 378 LYS LYS A . n 
A 1 380 LYS 380 379 379 LYS LYS A . n 
A 1 381 TYR 381 380 380 TYR TYR A . n 
A 1 382 GLY 382 381 381 GLY GLY A . n 
A 1 383 VAL 383 382 382 VAL VAL A . n 
A 1 384 THR 384 383 383 THR THR A . n 
A 1 385 ASP 385 384 384 ASP ASP A . n 
A 1 386 LYS 386 385 385 LYS LYS A . n 
A 1 387 ILE 387 386 386 ILE ILE A . n 
A 1 388 SER 388 387 387 SER SER A . n 
A 1 389 HIS 389 388 388 HIS HIS A . n 
A 1 390 VAL 390 389 389 VAL VAL A . n 
A 1 391 SER 391 390 390 SER SER A . n 
A 1 392 THR 392 391 391 THR THR A . n 
A 1 393 GLY 393 392 392 GLY GLY A . n 
A 1 394 GLY 394 393 393 GLY GLY A . n 
A 1 395 GLY 395 394 394 GLY GLY A . n 
A 1 396 ALA 396 395 395 ALA ALA A . n 
A 1 397 SER 397 396 396 SER SER A . n 
A 1 398 LEU 398 397 397 LEU LEU A . n 
A 1 399 GLU 399 398 398 GLU GLU A . n 
A 1 400 LEU 400 399 399 LEU LEU A . n 
A 1 401 LEU 401 400 400 LEU LEU A . n 
A 1 402 GLU 402 401 401 GLU GLU A . n 
A 1 403 GLY 403 402 402 GLY GLY A . n 
A 1 404 LYS 404 403 403 LYS LYS A . n 
A 1 405 GLU 405 404 404 GLU GLU A . n 
A 1 406 LEU 406 405 405 LEU LEU A . n 
A 1 407 PRO 407 406 406 PRO PRO A . n 
A 1 408 GLY 408 407 407 GLY GLY A . n 
A 1 409 VAL 409 408 408 VAL VAL A . n 
A 1 410 ALA 410 409 409 ALA ALA A . n 
A 1 411 PHE 411 410 410 PHE PHE A . n 
A 1 412 LEU 412 411 411 LEU LEU A . n 
A 1 413 SER 413 412 412 SER SER A . n 
A 1 414 GLU 414 413 413 GLU GLU A . n 
A 1 415 LYS 415 414 414 LYS LYS A . n 
A 1 416 LYS 416 415 415 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 MG  1 416 2 MG  MG  A . 
C 3 ATP 1 417 1 ATP ATP A . 
D 4 3PG 1 418 3 3PG MP3 A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_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 O3G ? C ATP . ? A ATP 417 ? 1_555 MG ? B MG . ? A MG 416 ? 1_555 O2G ? C ATP .   ? A ATP 417 ? 1_555 27.6 ? 
2 O3G ? C ATP . ? A ATP 417 ? 1_555 MG ? B MG . ? A MG 416 ? 1_555 O1G ? C ATP .   ? A ATP 417 ? 1_555 61.8 ? 
3 O2G ? C ATP . ? A ATP 417 ? 1_555 MG ? B MG . ? A MG 416 ? 1_555 O1G ? C ATP .   ? A ATP 417 ? 1_555 60.3 ? 
4 O3G ? C ATP . ? A ATP 417 ? 1_555 MG ? B MG . ? A MG 416 ? 1_555 OD1 ? A ASP 373 ? A ASP 372 ? 1_555 68.8 ? 
5 O2G ? C ATP . ? A ATP 417 ? 1_555 MG ? B MG . ? A MG 416 ? 1_555 OD1 ? A ASP 373 ? A ASP 372 ? 1_555 50.9 ? 
6 O1G ? C ATP . ? A ATP 417 ? 1_555 MG ? B MG . ? A MG 416 ? 1_555 OD1 ? A ASP 373 ? A ASP 372 ? 1_555 32.6 ? 
# 
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 1982-09-24 
2 'Structure model' 1 1 2008-03-25 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2017-11-29 
# 
_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' 'Version format compliance' 
3 4 'Structure model' 'Derived calculations'      
4 4 'Structure model' Other                       
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' pdbx_database_status 
2 4 'Structure model' struct_conf          
3 4 'Structure model' struct_conf_type     
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    4 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_pdbx_database_status.process_site' 
# 
_pdbx_database_remark.id     700 
_pdbx_database_remark.text   
;SHEET
CAUTION.  THE DEFINITION OF THE BEGINNING AND END OF
HELICES AND SHEET STRANDS GIVEN BELOW DEPENDS SOMEWHAT ON
THE CRITERIA USED TO DEFINE A *GOOD* HYDROGEN BOND.  TURNS
LISTED BELOW ARE THOSE WHERE CA(1)-CA(4) IS LESS THAN 5.7
ANGSTROMS AND O(1)-N(4) IS LESS THAN 3.2 ANGSTROMS.  FULL
TURN DEFINITION MUST AWAIT FURTHER REFINEMENT.
;
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1   1 CA  A VAL 214 ? ? CG    A LYS 217 ? ? 0.19 
2   1 O   A ALA 215 ? ? N     A LYS 217 ? ? 0.55 
3   1 C   A VAL 214 ? ? CB    A LYS 217 ? ? 0.75 
4   1 N   A ALA 215 ? ? CB    A LYS 217 ? ? 0.87 
5   1 OD1 A ASN 223 ? ? O     A GLU 401 ? ? 0.98 
6   1 O   A ALA 215 ? ? C     A ASP 216 ? ? 1.08 
7   1 C   A ALA 215 ? ? N     A LYS 217 ? ? 1.09 
8   1 CB  A PRO 204 ? ? OD2   A ASP 229 ? ? 1.14 
9   1 O   A VAL 259 ? ? CG2   A ILE 263 ? ? 1.15 
10  1 O   A SER 390 ? ? O     A THR 391 ? ? 1.21 
11  1 CA  A PRO 204 ? ? OD2   A ASP 229 ? ? 1.21 
12  1 CD2 A LEU 397 ? ? N     A GLU 398 ? ? 1.23 
13  1 CB  A LEU 206 ? ? CG2   A THR 329 ? ? 1.25 
14  1 O   A GLU 69  ? ? CG    A ARG 70  ? ? 1.31 
15  1 OD1 A ASP 372 ? ? O1G   A ATP 417 ? ? 1.34 
16  1 CA  A VAL 214 ? ? CD    A LYS 217 ? ? 1.35 
17  1 OD1 A ASN 334 ? ? O2B   A ATP 417 ? ? 1.36 
18  1 O   A VAL 366 ? ? CB    A SER 387 ? ? 1.36 
19  1 N   A VAL 214 ? ? CD    A LYS 217 ? ? 1.41 
20  1 CG1 A VAL 214 ? ? N     A ILE 218 ? ? 1.44 
21  1 O   A THR 34  ? ? OG    A SER 35  ? ? 1.44 
22  1 CB  A VAL 214 ? ? CG    A LYS 217 ? ? 1.45 
23  1 C   A VAL 214 ? ? CG    A LYS 217 ? ? 1.46 
24  1 CE  A MET 237 ? ? CG    A GLN 309 ? ? 1.49 
25  1 OD2 A ASP 216 ? ? N     A LEU 220 ? ? 1.50 
26  1 N   A VAL 214 ? ? CG    A LYS 217 ? ? 1.51 
27  1 CG1 A VAL 214 ? ? C     A LYS 217 ? ? 1.52 
28  1 C   A LYS 213 ? ? CD    A LYS 217 ? ? 1.53 
29  1 O   A ACE 0   ? ? CA    A GLY 402 ? ? 1.59 
30  1 OG  A SER 61  ? ? N     A GLU 118 ? ? 1.60 
31  1 O   A LYS 213 ? ? CD    A LYS 217 ? ? 1.60 
32  1 CA  A VAL 214 ? ? CB    A LYS 217 ? ? 1.60 
33  1 OD1 A ASN 223 ? ? C     A GLU 401 ? ? 1.61 
34  1 N   A ALA 215 ? ? CA    A LYS 217 ? ? 1.64 
35  1 O   A VAL 98  ? ? CG2   A VAL 102 ? ? 1.65 
36  1 O   A ALA 215 ? ? CA    A LYS 217 ? ? 1.68 
37  1 CG  A LEU 245 ? ? OE2   A GLU 249 ? ? 1.69 
38  1 NH2 A ARG 121 ? ? OE1   A GLU 150 ? ? 1.69 
39  1 CG  A ASN 334 ? ? O2B   A ATP 417 ? ? 1.69 
40  1 O   A THR 165 ? ? CA    A GLY 407 ? ? 1.70 
41  1 O   A LEU 206 ? ? O     A VAL 330 ? ? 1.72 
42  1 ND2 A ASN 334 ? ? O2B   A ATP 417 ? ? 1.74 
43  1 CG1 A VAL 8   ? ? OE1   A GLN 9   ? ? 1.74 
44  1 CD2 A LEU 397 ? ? CA    A GLU 398 ? ? 1.75 
45  1 O   A LYS 141 ? ? CG1   A VAL 144 ? ? 1.75 
46  1 O   A ASP 216 ? ? N     A LEU 220 ? ? 1.76 
47  1 O   A LEU 311 ? ? N6    A ATP 417 ? ? 1.77 
48  1 N   A LEU 206 ? ? OG1   A THR 329 ? ? 1.79 
49  1 CB  A SER 1   ? ? O     A LYS 403 ? ? 1.80 
50  1 OH  A TYR 158 ? ? ND2   A ASN 160 ? ? 1.80 
51  1 OD1 A ASP 216 ? ? OE1   A GLN 219 ? ? 1.81 
52  1 CG  A ASP 372 ? ? O1G   A ATP 417 ? ? 1.81 
53  1 OH  A TYR 56  ? ? C     A LEU 154 ? ? 1.81 
54  1 O   A PRO 261 ? ? CG    A LYS 265 ? ? 1.82 
55  1 CG  A ASN 223 ? ? O     A GLU 401 ? ? 1.83 
56  1 O   A LYS 196 ? ? N     A GLU 199 ? ? 1.84 
57  1 CB  A VAL 8   ? ? OE2   A GLU 188 ? ? 1.87 
58  1 O   A GLY 175 ? ? N     A ASP 177 ? ? 1.87 
59  1 CE2 A PHE 163 ? ? OE2   A GLU 190 ? ? 1.88 
60  1 SD  A MET 237 ? ? CB    A GLN 309 ? ? 1.89 
61  1 CE  A MET 237 ? ? CB    A GLN 309 ? ? 1.89 
62  1 CB  A ARG 17  ? ? CD1   A TYR 56  ? ? 1.90 
63  1 O   A SER 396 ? ? N     A LEU 400 ? ? 1.91 
64  1 O   A ALA 41  ? ? CD    A PRO 44  ? ? 1.91 
65  1 OD2 A ASP 216 ? ? C     A GLN 219 ? ? 1.92 
66  1 O   A SER 359 ? ? O     A ALA 362 ? ? 1.93 
67  1 OG  A SER 360 ? ? CG1   A ILE 386 ? ? 1.93 
68  1 O   A VAL 214 ? ? CB    A LYS 217 ? ? 1.93 
69  1 C   A PRO 204 ? ? OD2   A ASP 229 ? ? 1.94 
70  1 OD1 A ASP 372 ? ? PG    A ATP 417 ? ? 1.94 
71  1 OD1 A ASN 25  ? ? O     A HIS 62  ? ? 1.95 
72  1 O   A ASP 384 ? ? N     A ILE 386 ? ? 1.96 
73  1 O   A VAL 339 ? ? O     A PHE 345 ? ? 1.96 
74  1 SD  A MET 237 ? ? O     A TRP 308 ? ? 1.96 
75  1 N   A ALA 215 ? ? N     A LYS 217 ? ? 1.96 
76  1 O   A ALA 238 ? ? N     A PHE 241 ? ? 1.97 
77  1 CB  A LEU 206 ? ? CB    A THR 329 ? ? 1.97 
78  1 CG1 A VAL 214 ? ? O     A LYS 217 ? ? 1.98 
79  1 CD2 A PHE 19  ? ? CZ    A PHE 176 ? ? 1.98 
80  1 O   A VAL 357 ? ? CD1   A ILE 386 ? ? 1.98 
81  1 OD2 A ASP 216 ? ? CB    A GLN 219 ? ? 2.00 
82  1 CA  A ALA 215 ? ? N     A LYS 217 ? ? 2.00 
83  1 O   A LYS 146 ? ? CG    A GLU 150 ? ? 2.01 
84  1 CG  A ASP 216 ? ? CB    A GLN 219 ? ? 2.01 
85  1 OD1 A ASP 372 ? ? O2G   A ATP 417 ? ? 2.01 
86  1 CG  A ARG 17  ? ? CD1   A TYR 56  ? ? 2.01 
87  1 NZ  A LYS 213 ? ? O1A   A ATP 417 ? ? 2.02 
88  1 O   A LYS 213 ? ? NZ    A LYS 217 ? ? 2.02 
89  1 OD1 A ASP 216 ? ? CD    A GLN 219 ? ? 2.02 
90  1 O   A ARG 121 ? ? N     A HIS 123 ? ? 2.03 
91  1 OD1 A ASN 119 ? ? CD1   A ILE 124 ? ? 2.03 
92  1 OD2 A ASP 372 ? ? O1G   A ATP 417 ? ? 2.03 
93  1 SD  A MET 237 ? ? CG    A GLN 309 ? ? 2.03 
94  1 OH  A TYR 56  ? ? CA    A LEU 154 ? ? 2.04 
95  1 CD1 A LEU 245 ? ? OE2   A GLU 249 ? ? 2.04 
96  1 O   A SER 359 ? ? N     A ALA 361 ? ? 2.04 
97  1 CG  A LEU 206 ? ? CG2   A THR 329 ? ? 2.05 
98  1 CD1 A ILE 218 ? ? OE1   A GLU 262 ? ? 2.05 
99  1 C   A VAL 366 ? ? CB    A SER 387 ? ? 2.06 
100 1 CG1 A VAL 214 ? ? CA    A ILE 218 ? ? 2.06 
101 1 N   A PHE 205 ? ? OD2   A ASP 229 ? ? 2.07 
102 1 O   A ACE 0   ? ? O     A GLY 402 ? ? 2.08 
103 1 OD1 A ASN 223 ? ? CA    A GLU 401 ? ? 2.09 
104 1 O   A LEU 245 ? ? CG2   A THR 248 ? ? 2.09 
105 1 O   A ALA 238 ? ? N     A LYS 242 ? ? 2.10 
106 1 O   A ACE 0   ? ? C     A GLY 402 ? ? 2.10 
107 1 CZ  A PHE 194 ? ? OG    A SER 390 ? ? 2.10 
108 1 CG  A ASP 216 ? ? CG    A GLN 219 ? ? 2.10 
109 1 C   A VAL 366 ? ? OG    A SER 387 ? ? 2.10 
110 1 CE  A MET 237 ? ? CD    A GLN 309 ? ? 2.10 
111 1 O   A LEU 191 ? ? N     A GLY 195 ? ? 2.11 
112 1 CG  A ARG 17  ? ? CE1   A TYR 56  ? ? 2.11 
113 1 O   A LYS 213 ? ? CE    A LYS 217 ? ? 2.12 
114 1 CB  A ASP 96  ? ? CA    A LEU 117 ? ? 2.12 
115 1 O   A GLU 190 ? ? CB    A PHE 194 ? ? 2.12 
116 1 OD2 A ASP 216 ? ? CD    A GLN 219 ? ? 2.13 
117 1 CD  A PRO 336 ? ? "O5'" A ATP 417 ? ? 2.13 
118 1 O   A VAL 366 ? ? OG    A SER 387 ? ? 2.13 
119 1 O   A GLU 150 ? ? CB    A SER 153 ? ? 2.13 
120 1 O   A ALA 238 ? ? CB    A PHE 241 ? ? 2.14 
121 1 CZ  A TYR 56  ? ? O     A LEU 154 ? ? 2.14 
122 1 OE1 A GLN 9   ? ? OE1   A GLU 188 ? ? 2.14 
123 1 CB  A ASP 282 ? ? CB    A GLU 316 ? ? 2.14 
124 1 O   A ASP 216 ? ? N     A GLN 219 ? ? 2.15 
125 1 O   A THR 165 ? ? N     A GLY 407 ? ? 2.15 
126 1 O   A PHE 205 ? ? O     A ASP 229 ? ? 2.15 
127 1 OH  A TYR 56  ? ? O     A LEU 154 ? ? 2.15 
128 1 N   A PHE 205 ? ? CG    A ASP 229 ? ? 2.15 
129 1 CB  A ARG 17  ? ? CE1   A TYR 56  ? ? 2.16 
130 1 O   A PHE 321 ? ? CG2   A VAL 325 ? ? 2.16 
131 1 CD1 A ILE 20  ? ? CD2   A LEU 59  ? ? 2.17 
132 1 O   A GLU 142 ? ? N     A GLN 145 ? ? 2.17 
133 1 OG  A SER 61  ? ? CA    A GLU 118 ? ? 2.17 
134 1 O   A PHE 205 ? ? CB    A ASP 229 ? ? 2.17 
135 1 CB  A LEU 206 ? ? OG1   A THR 329 ? ? 2.17 
136 1 CA  A LEU 206 ? ? OG1   A THR 329 ? ? 2.18 
137 1 O   A MET 237 ? ? CD2   A PHE 241 ? ? 2.18 
138 1 OD1 A ASN 95  ? ? N     A CYS 97  ? ? 2.18 
139 1 O   A LYS 319 ? ? N     A ALA 323 ? ? 2.18 
140 1 O   A LEU 191 ? ? CA    A GLY 195 ? ? 2.18 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1    1 N   A THR 34  ? ? 1_555 C     A GLU 190 ? ? 4_555 0.12 
2    1 CB  A ILE 115 ? ? 1_555 N     A PHE 205 ? ? 4_555 0.15 
3    1 C   A GLU 82  ? ? 1_555 NZ    A LYS 227 ? ? 4_555 0.17 
4    1 CE1 A PHE 241 ? ? 1_555 CA    A PRO 280 ? ? 2_656 0.20 
5    1 O   A GLY 210 ? ? 1_555 CG1   A ILE 250 ? ? 2_656 0.21 
6    1 N   A GLY 307 ? ? 1_555 C     A ASP 312 ? ? 2_656 0.24 
7    1 CB  A PHE 93  ? ? 1_555 CG2   A THR 329 ? ? 4_555 0.25 
8    1 C   A THR 34  ? ? 1_555 CA    A LEU 191 ? ? 4_555 0.31 
9    1 O   A ASP 252 ? ? 1_555 CZ    A PHE 321 ? ? 2_656 0.31 
10   1 CA  A THR 34  ? ? 1_555 N     A LEU 191 ? ? 4_555 0.34 
11   1 CE2 A PHE 241 ? ? 1_555 CG    A PRO 280 ? ? 2_656 0.36 
12   1 CB  A THR 92  ? ? 1_555 CG2   A ILE 231 ? ? 4_555 0.36 
13   1 C   A VAL 91  ? ? 1_555 O     A ILE 231 ? ? 4_555 0.37 
14   1 CD1 A LEU 83  ? ? 1_555 CB    A LYS 227 ? ? 4_555 0.38 
15   1 CA  A LYS 73  ? ? 1_555 N     A ALA 361 ? ? 4_555 0.39 
16   1 C   A LEU 50  ? ? 1_555 N     A LYS 273 ? ? 4_555 0.40 
17   1 CA  A SER 75  ? ? 1_555 N     A THR 365 ? ? 4_555 0.41 
18   1 CA  A LEU 87  ? ? 1_555 C     A LEU 225 ? ? 4_555 0.41 
19   1 CG  A LYS 89  ? ? 1_555 CB    A ALA 270 ? ? 4_555 0.43 
20   1 CA  A ILE 233 ? ? 1_555 CG    A GLU 249 ? ? 2_656 0.44 
21   1 C   A ILE 233 ? ? 1_555 CB    A GLU 249 ? ? 2_656 0.45 
22   1 C   A SER 85  ? ? 1_555 N     A LEU 224 ? ? 4_555 0.45 
23   1 CA  A GLN 84  ? ? 1_555 CD2   A LEU 224 ? ? 4_555 0.46 
24   1 O   A LEU 94  ? ? 1_555 N     A ALA 328 ? ? 4_555 0.47 
25   1 CA  A LEU 116 ? ? 1_555 CD    A PRO 204 ? ? 4_555 0.47 
26   1 CB  A MET 237 ? ? 1_555 CE1   A PHE 283 ? ? 2_656 0.49 
27   1 CE  A LYS 73  ? ? 1_555 N     A SER 359 ? ? 4_555 0.50 
28   1 CE  A LYS 31  ? ? 1_555 C     A ILE 368 ? ? 4_555 0.50 
29   1 CZ  A PHE 241 ? ? 1_555 CB    A PRO 280 ? ? 2_656 0.53 
30   1 CZ  A PHE 255 ? ? 1_555 CA    A THR 299 ? ? 2_656 0.53 
31   1 CB  A LEU 87  ? ? 1_555 O     A LEU 225 ? ? 4_555 0.55 
32   1 CG  A ASP 256 ? ? 1_555 CG2   A VAL 298 ? ? 2_656 0.55 
33   1 CG  A LYS 379 ? ? 1_555 CB    A LYS 415 ? ? 4_555 0.56 
34   1 N   A LYS 31  ? ? 1_555 CA    A HIS 388 ? ? 4_555 0.56 
35   1 N   A ALA 288 ? ? 1_555 O     A SER 290 ? ? 2_656 0.57 
36   1 CD  A PRO 27  ? ? 1_555 CA    A LYS 192 ? ? 4_555 0.60 
37   1 CB  A PRO 305 ? ? 1_555 CG1   A VAL 339 ? ? 2_656 0.61 
38   1 O   A GLY 30  ? ? 1_555 N     A HIS 388 ? ? 4_555 0.62 
39   1 CD  A PRO 305 ? ? 1_555 C     A VAL 339 ? ? 2_656 0.63 
40   1 CB  A ILE 33  ? ? 1_555 CA    A PHE 194 ? ? 4_555 0.64 
41   1 CD1 A LEU 59  ? ? 1_555 C     A VAL 228 ? ? 4_555 0.64 
42   1 CG  A LYS 242 ? ? 1_555 NZ    A LYS 243 ? ? 2_656 0.65 
43   1 O   A ALA 212 ? ? 1_555 C     A ASP 300 ? ? 2_656 0.65 
44   1 CG1 A ILE 304 ? ? 1_555 CB    A PHE 340 ? ? 2_656 0.65 
45   1 CB  A ILE 304 ? ? 1_555 CA    A PHE 340 ? ? 2_656 0.66 
46   1 CB  A SER 75  ? ? 1_555 C     A ASN 364 ? ? 4_555 0.66 
47   1 CB  A SER 61  ? ? 1_555 CG    A ARG 203 ? ? 4_555 0.66 
48   1 CA  A ILE 115 ? ? 1_555 OD2   A ASP 229 ? ? 4_555 0.67 
49   1 CG  A GLN 84  ? ? 1_555 CD1   A LEU 224 ? ? 4_555 0.68 
50   1 N   A ILE 233 ? ? 1_555 OE1   A GLU 249 ? ? 2_656 0.70 
51   1 CB  A SER 75  ? ? 1_555 O     A ASN 364 ? ? 4_555 0.72 
52   1 CD1 A ILE 254 ? ? 1_555 CG    A GLU 316 ? ? 2_656 0.73 
53   1 CG  A ASP 252 ? ? 1_555 CG    A ASN 313 ? ? 2_656 0.74 
54   1 CB  A VAL 26  ? ? 1_555 O     A LYS 192 ? ? 4_555 0.75 
55   1 O   A PRO 78  ? ? 1_555 CD2   A LEU 332 ? ? 4_555 0.75 
56   1 C   A ILE 232 ? ? 1_555 OE1   A GLU 249 ? ? 2_656 0.76 
57   1 CD2 A PHE 241 ? ? 1_555 CD    A PRO 280 ? ? 2_656 0.76 
58   1 CB  A ALA 286 ? ? 1_555 CB    A PHE 289 ? ? 2_656 0.76 
59   1 CA  A GLY 236 ? ? 1_555 CG    A ASN 247 ? ? 2_656 0.76 
60   1 N   A VAL 22  ? ? 1_555 OD1   A ASN 200 ? ? 4_555 0.76 
61   1 CB  A LYS 379 ? ? 1_555 CG    A LYS 415 ? ? 4_555 0.76 
62   1 CA  A PHE 283 ? ? 1_555 CG    A TRP 308 ? ? 2_656 0.76 
63   1 CA  A PHE 255 ? ? 1_555 N     A ASP 282 ? ? 2_656 0.76 
64   1 OD1 A ASP 252 ? ? 1_555 CB    A ASN 313 ? ? 2_656 0.76 
65   1 CB  A PRO 78  ? ? 1_555 CB    A ILE 367 ? ? 4_555 0.76 
66   1 O   A GLN 309 ? ? 1_555 CA    A LEU 311 ? ? 2_656 0.76 
67   1 CA  A LEU 6   ? ? 1_555 NZ    A LYS 378 ? ? 4_545 0.77 
68   1 CB  A PHE 255 ? ? 1_555 C     A VAL 281 ? ? 2_656 0.77 
69   1 O   A THR 92  ? ? 1_555 CD1   A ILE 231 ? ? 4_555 0.77 
70   1 O   A ILE 254 ? ? 1_555 O     A ASP 282 ? ? 2_656 0.78 
71   1 C   A GLY 30  ? ? 1_555 CA    A HIS 388 ? ? 4_555 0.78 
72   1 CG  A ASP 287 ? ? 1_555 CD2   A PHE 342 ? ? 2_656 0.78 
73   1 CA  A SER 113 ? ? 1_555 CA    A SER 230 ? ? 4_555 0.78 
74   1 O   A ALA 60  ? ? 1_555 O     A PRO 201 ? ? 4_555 0.78 
75   1 N   A GLY 88  ? ? 1_555 CA    A LEU 225 ? ? 4_555 0.78 
76   1 CD1 A LEU 245 ? ? 1_555 N     A VAL 278 ? ? 2_656 0.78 
77   1 CA  A LEU 50  ? ? 1_555 CA    A LYS 273 ? ? 4_555 0.79 
78   1 OG  A SER 253 ? ? 1_555 C     A SER 317 ? ? 2_656 0.80 
79   1 N   A PRO 305 ? ? 1_555 O     A VAL 339 ? ? 2_656 0.80 
80   1 C   A PRO 111 ? ? 1_555 O     A VAL 275 ? ? 4_555 0.80 
81   1 O   A ALA 77  ? ? 1_555 N     A LEU 332 ? ? 4_555 0.81 
82   1 CD  A LYS 89  ? ? 1_555 CA    A ALA 270 ? ? 4_555 0.81 
83   1 C   A ASP 90  ? ? 1_555 CG2   A ILE 232 ? ? 4_555 0.81 
84   1 CB  A GLN 135 ? ? 1_555 NZ    A LYS 136 ? ? 2_555 0.81 
85   1 CB  A LEU 245 ? ? 1_555 CG1   A VAL 277 ? ? 2_656 0.81 
86   1 O   A PRO 78  ? ? 1_555 CG    A LEU 332 ? ? 4_555 0.81 
87   1 CA  A PHE 255 ? ? 1_555 CA    A ASP 282 ? ? 2_656 0.82 
88   1 O   A ALA 286 ? ? 1_555 O     A PHE 289 ? ? 2_656 0.82 
89   1 CA  A VAL 22  ? ? 1_555 OD1   A ASN 200 ? ? 4_555 0.82 
90   1 N   A LYS 73  ? ? 1_555 CA    A ALA 361 ? ? 4_555 0.82 
91   1 N   A PHE 283 ? ? 1_555 CD1   A TRP 308 ? ? 2_656 0.83 
92   1 N   A GLY 112 ? ? 1_555 C     A VAL 275 ? ? 4_555 0.83 
93   1 CG1 A ILE 254 ? ? 1_555 CB    A GLU 316 ? ? 2_656 0.83 
94   1 CD  A LYS 378 ? ? 1_555 O     A SER 412 ? ? 4_555 0.83 
95   1 N   A LYS 73  ? ? 1_555 CB    A ALA 361 ? ? 4_555 0.83 
96   1 N   A ASP 23  ? ? 1_555 CB    A ASN 200 ? ? 4_555 0.83 
97   1 O   A GLY 30  ? ? 1_555 C     A SER 387 ? ? 4_555 0.83 
98   1 O   A PRO 111 ? ? 1_555 O     A VAL 275 ? ? 4_555 0.83 
99   1 C   A PHE 283 ? ? 1_555 CG    A TRP 308 ? ? 2_656 0.84 
100  1 CA  A GLY 210 ? ? 1_555 CA    A ILE 250 ? ? 2_656 0.84 
101  1 O   A ILE 232 ? ? 1_555 OE2   A GLU 249 ? ? 2_656 0.84 
102  1 O   A ALA 212 ? ? 1_555 N     A LYS 301 ? ? 2_656 0.84 
103  1 N   A ILE 254 ? ? 1_555 CA    A SER 317 ? ? 2_656 0.85 
104  1 O   A GLN 309 ? ? 1_555 N     A LEU 311 ? ? 2_656 0.85 
105  1 N   A GLY 303 ? ? 1_555 CA    A GLY 338 ? ? 2_656 0.85 
106  1 CA  A LEU 86  ? ? 1_555 O     A ASN 223 ? ? 4_555 0.86 
107  1 C   A ILE 33  ? ? 1_555 O     A GLU 190 ? ? 4_555 0.86 
108  1 CG1 A VAL 244 ? ? 1_555 SD    A MET 267 ? ? 2_656 0.86 
109  1 CB  A ILE 254 ? ? 1_555 C     A GLU 316 ? ? 2_656 0.86 
110  1 OG  A SER 75  ? ? 1_555 CA    A ASN 364 ? ? 4_555 0.86 
111  1 CB  A ILE 39  ? ? 1_555 CB    A LEU 198 ? ? 4_555 0.86 
112  1 CG  A PHE 24  ? ? 1_555 CG    A PRO 201 ? ? 4_555 0.86 
113  1 CG1 A ILE 254 ? ? 1_555 CA    A GLU 316 ? ? 2_656 0.86 
114  1 O   A SER 113 ? ? 1_555 N     A ILE 231 ? ? 4_555 0.86 
115  1 O   A SER 75  ? ? 1_555 OG1   A THR 365 ? ? 4_555 0.86 
116  1 CB  A PHE 24  ? ? 1_555 CB    A PRO 201 ? ? 4_555 0.86 
117  1 O   A PHE 255 ? ? 1_555 CB    A ASP 282 ? ? 2_656 0.87 
118  1 CG  A MET 237 ? ? 1_555 CD1   A PHE 283 ? ? 2_656 0.88 
119  1 C   A GLU 51  ? ? 1_555 CB    A ALA 272 ? ? 4_555 0.89 
120  1 C   A ALA 286 ? ? 1_555 O     A PHE 289 ? ? 2_656 0.89 
121  1 CG  A LEU 76  ? ? 1_555 CA    A VAL 330 ? ? 4_555 0.89 
122  1 CA  A SER 113 ? ? 1_555 CB    A SER 230 ? ? 4_555 0.89 
123  1 CD1 A ILE 285 ? ? 1_555 CD2   A LEU 311 ? ? 2_656 0.89 
124  1 CB  A VAL 244 ? ? 1_555 SD    A MET 267 ? ? 2_656 0.90 
125  1 CA  A LEU 245 ? ? 1_555 CG1   A VAL 277 ? ? 2_656 0.90 
126  1 C   A LEU 87  ? ? 1_555 CA    A LEU 225 ? ? 4_555 0.90 
127  1 N   A SER 61  ? ? 1_555 C     A THR 202 ? ? 4_555 0.90 
128  1 C   A VAL 91  ? ? 1_555 C     A ILE 231 ? ? 4_555 0.91 
129  1 N   A VAL 79  ? ? 1_555 CD1   A LEU 332 ? ? 4_555 0.91 
130  1 CB  A ALA 139 ? ? 1_555 CB    A ALA 139 ? ? 2_555 0.91 
131  1 CB  A PHE 24  ? ? 1_555 CG    A PRO 201 ? ? 4_555 0.92 
132  1 CB  A ASP 256 ? ? 1_555 CB    A VAL 298 ? ? 2_656 0.92 
133  1 CB  A GLN 84  ? ? 1_555 CD1   A LEU 224 ? ? 4_555 0.92 
134  1 CG  A LYS 242 ? ? 1_555 CE    A LYS 243 ? ? 2_656 0.92 
135  1 CA  A PHE 283 ? ? 1_555 CD1   A TRP 308 ? ? 2_656 0.93 
136  1 CA  A ASP 90  ? ? 1_555 CG2   A ILE 232 ? ? 4_555 0.93 
137  1 C   A LEU 94  ? ? 1_555 C     A LYS 327 ? ? 4_555 0.93 
138  1 CA  A SER 75  ? ? 1_555 C     A ASN 364 ? ? 4_555 0.93 
139  1 C   A LEU 87  ? ? 1_555 CB    A LEU 225 ? ? 4_555 0.93 
140  1 O   A LEU 94  ? ? 1_555 C     A LYS 327 ? ? 4_555 0.93 
141  1 CD1 A ILE 115 ? ? 1_555 N     A LEU 206 ? ? 4_555 0.94 
142  1 CA  A ALA 286 ? ? 1_555 CG    A PHE 289 ? ? 2_656 0.94 
143  1 CB  A SER 253 ? ? 1_555 O     A SER 317 ? ? 2_656 0.95 
144  1 CB  A LEU 50  ? ? 1_555 CB    A LYS 273 ? ? 4_555 0.96 
145  1 CG1 A VAL 79  ? ? 1_555 CG2   A VAL 330 ? ? 4_555 0.96 
146  1 CA  A VAL 26  ? ? 1_555 O     A LYS 192 ? ? 4_555 0.97 
147  1 O   A VAL 49  ? ? 1_555 O     A ALA 272 ? ? 4_555 0.97 
148  1 CA  A GLY 236 ? ? 1_555 OD1   A ASN 247 ? ? 2_656 0.97 
149  1 CA  A GLY 112 ? ? 1_555 C     A VAL 275 ? ? 4_555 0.98 
150  1 CB  A ILE 254 ? ? 1_555 N     A SER 317 ? ? 2_656 0.98 
151  1 O   A LEU 209 ? ? 1_555 N     A ILE 250 ? ? 2_656 0.98 
152  1 CB  A ALA 286 ? ? 1_555 CA    A PHE 289 ? ? 2_656 0.98 
153  1 CG  A ASP 252 ? ? 1_555 CB    A ASN 313 ? ? 2_656 0.99 
154  1 C   A PRO 78  ? ? 1_555 CD1   A LEU 332 ? ? 4_555 0.99 
155  1 C   A PHE 255 ? ? 1_555 CA    A ASP 282 ? ? 2_656 0.99 
156  1 CG1 A ILE 39  ? ? 1_555 CA    A LEU 198 ? ? 4_555 0.99 
157  1 O   A LEU 87  ? ? 1_555 CB    A LEU 225 ? ? 4_555 1.00 
158  1 O   A VAL 79  ? ? 1_555 CZ    A PHE 205 ? ? 4_555 1.00 
159  1 N   A GLY 112 ? ? 1_555 CA    A VAL 275 ? ? 4_555 1.01 
160  1 CG2 A VAL 79  ? ? 1_555 CB    A ALA 197 ? ? 4_555 1.01 
161  1 CA  A LEU 83  ? ? 1_555 CD    A LYS 227 ? ? 4_555 1.01 
162  1 C   A ALA 77  ? ? 1_555 C     A ILE 331 ? ? 4_555 1.02 
163  1 CB  A LYS 242 ? ? 1_555 CD    A LYS 243 ? ? 2_656 1.03 
164  1 CB  A PHE 255 ? ? 1_555 N     A ASP 282 ? ? 2_656 1.03 
165  1 N   A SER 85  ? ? 1_555 CB    A LEU 224 ? ? 4_555 1.03 
166  1 CD1 A LEU 76  ? ? 1_555 N     A VAL 330 ? ? 4_555 1.03 
167  1 CB  A MET 237 ? ? 1_555 CZ    A PHE 283 ? ? 2_656 1.03 
168  1 C   A ILE 115 ? ? 1_555 CB    A PRO 204 ? ? 4_555 1.03 
169  1 CA  A LYS 31  ? ? 1_555 CB    A HIS 388 ? ? 4_555 1.03 
170  1 N   A SER 113 ? ? 1_555 CB    A SER 230 ? ? 4_555 1.03 
171  1 C   A ALA 77  ? ? 1_555 O     A ILE 331 ? ? 4_555 1.04 
172  1 CA  A GLU 51  ? ? 1_555 CB    A ALA 272 ? ? 4_555 1.04 
173  1 CD1 A ILE 254 ? ? 1_555 CD    A GLU 316 ? ? 2_656 1.04 
174  1 O   A ALA 306 ? ? 1_555 CG    A ASP 312 ? ? 2_656 1.04 
175  1 CD2 A PHE 255 ? ? 1_555 O     A VAL 281 ? ? 2_656 1.04 
176  1 O   A GLY 236 ? ? 1_555 CG2   A THR 240 ? ? 2_656 1.05 
177  1 CB  A LEU 50  ? ? 1_555 CA    A LYS 273 ? ? 4_555 1.05 
178  1 CA  A LEU 50  ? ? 1_555 C     A LYS 273 ? ? 4_555 1.05 
179  1 C   A VAL 22  ? ? 1_555 CG    A ASN 200 ? ? 4_555 1.05 
180  1 CD  A PRO 78  ? ? 1_555 N     A ILE 367 ? ? 4_555 1.05 
181  1 N   A LEU 87  ? ? 1_555 N     A ASP 226 ? ? 4_555 1.05 
182  1 CD1 A ILE 304 ? ? 1_555 CG    A PHE 340 ? ? 2_656 1.05 
183  1 CE  A LYS 89  ? ? 1_555 N     A LYS 271 ? ? 4_555 1.06 
184  1 C   A LEU 50  ? ? 1_555 C     A ALA 272 ? ? 4_555 1.06 
185  1 CB  A ILE 39  ? ? 1_555 CA    A LEU 198 ? ? 4_555 1.06 
186  1 C   A PRO 78  ? ? 1_555 CG    A LEU 332 ? ? 4_555 1.06 
187  1 N   A ILE 233 ? ? 1_555 CD    A GLU 249 ? ? 2_656 1.06 
188  1 CA  A GLY 303 ? ? 1_555 N     A GLY 338 ? ? 2_656 1.07 
189  1 CA  A ALA 306 ? ? 1_555 CA    A ASP 312 ? ? 2_656 1.07 
190  1 O   A SER 35  ? ? 1_555 CA    A GLY 195 ? ? 4_555 1.07 
191  1 C   A ALA 306 ? ? 1_555 CB    A ASP 312 ? ? 2_656 1.07 
192  1 N   A ALA 288 ? ? 1_555 C     A SER 290 ? ? 2_656 1.08 
193  1 CA  A VAL 22  ? ? 1_555 CG    A ASN 200 ? ? 4_555 1.08 
194  1 CZ  A PHE 255 ? ? 1_555 N     A THR 299 ? ? 2_656 1.08 
195  1 N   A ASP 23  ? ? 1_555 CA    A ASN 200 ? ? 4_555 1.08 
196  1 CB  A ALA 306 ? ? 1_555 N     A ASP 312 ? ? 2_656 1.09 
197  1 C   A VAL 22  ? ? 1_555 CB    A ASN 200 ? ? 4_555 1.09 
198  1 CD1 A LEU 59  ? ? 1_555 N     A ASP 229 ? ? 4_555 1.09 
199  1 CE1 A PHE 93  ? ? 1_555 CD1   A ILE 331 ? ? 4_555 1.09 
200  1 OD2 A ASP 252 ? ? 1_555 CG    A ASN 313 ? ? 2_656 1.09 
201  1 CA  A GLY 112 ? ? 1_555 N     A GLU 276 ? ? 4_555 1.09 
202  1 CA  A LEU 87  ? ? 1_555 N     A ASP 226 ? ? 4_555 1.10 
203  1 O   A SER 85  ? ? 1_555 N     A LEU 224 ? ? 4_555 1.10 
204  1 O   A PHE 283 ? ? 1_555 CD2   A TRP 308 ? ? 2_656 1.10 
205  1 CG1 A VAL 244 ? ? 1_555 CE    A MET 267 ? ? 2_656 1.10 
206  1 N   A THR 92  ? ? 1_555 C     A ILE 231 ? ? 4_555 1.10 
207  1 CB  A PHE 93  ? ? 1_555 CB    A LEU 206 ? ? 4_555 1.11 
208  1 N   A SER 61  ? ? 1_555 N     A ARG 203 ? ? 4_555 1.11 
209  1 NZ  A LYS 89  ? ? 1_555 N     A LYS 271 ? ? 4_555 1.11 
210  1 CE  A LYS 31  ? ? 1_555 O     A ILE 368 ? ? 4_555 1.11 
211  1 CA  A PHE 241 ? ? 1_555 CB    A LEU 279 ? ? 2_656 1.11 
212  1 O   A ILE 304 ? ? 1_555 O     A PHE 345 ? ? 2_656 1.11 
213  1 N   A LYS 31  ? ? 1_555 CB    A HIS 388 ? ? 4_555 1.11 
214  1 OG  A SER 75  ? ? 1_555 N     A ASN 364 ? ? 4_555 1.12 
215  1 N   A GLY 307 ? ? 1_555 O     A ASP 312 ? ? 2_656 1.12 
216  1 CG2 A ILE 304 ? ? 1_555 C     A PHE 340 ? ? 2_656 1.12 
217  1 OD1 A ASP 256 ? ? 1_555 CG2   A VAL 298 ? ? 2_656 1.12 
218  1 N   A LEU 116 ? ? 1_555 N     A PRO 204 ? ? 4_555 1.12 
219  1 CG  A LYS 378 ? ? 1_555 O     A SER 412 ? ? 4_555 1.13 
220  1 N   A THR 34  ? ? 1_555 O     A GLU 190 ? ? 4_555 1.13 
221  1 C   A SER 85  ? ? 1_555 C     A ASN 223 ? ? 4_555 1.13 
222  1 CB  A PRO 305 ? ? 1_555 CB    A VAL 339 ? ? 2_656 1.13 
223  1 CD  A PRO 305 ? ? 1_555 CA    A VAL 339 ? ? 2_656 1.14 
224  1 CG  A PHE 255 ? ? 1_555 O     A VAL 281 ? ? 2_656 1.14 
225  1 CA  A ILE 39  ? ? 1_555 C     A LEU 198 ? ? 4_555 1.15 
226  1 CA  A ILE 233 ? ? 1_555 CD    A GLU 249 ? ? 2_656 1.15 
227  1 CD2 A LEU 63  ? ? 1_555 CE    A LYS 196 ? ? 4_555 1.15 
228  1 N   A LEU 86  ? ? 1_555 O     A ASN 223 ? ? 4_555 1.16 
229  1 CG1 A ILE 46  ? ? 1_555 O     A LYS 227 ? ? 4_555 1.16 
230  1 N   A SER 35  ? ? 1_555 CA    A LEU 191 ? ? 4_555 1.16 
231  1 NE2 A HIS 123 ? ? 1_555 CE    A LYS 131 ? ? 2_555 1.16 
232  1 O   A PHE 255 ? ? 1_555 CG    A ASP 282 ? ? 2_656 1.16 
233  1 CB  A LEU 87  ? ? 1_555 C     A LEU 225 ? ? 4_555 1.16 
234  1 OE2 A GLU 51  ? ? 1_555 CB    A LYS 269 ? ? 4_555 1.16 
235  1 CA  A GLU 302 ? ? 1_555 N7    A ATP 417 ? ? 2_656 1.16 
236  1 O   A ASP 252 ? ? 1_555 CE1   A PHE 321 ? ? 2_656 1.16 
237  1 CB  A ILE 304 ? ? 1_555 N     A PHE 340 ? ? 2_656 1.16 
238  1 C   A ALA 60  ? ? 1_555 C     A THR 202 ? ? 4_555 1.16 
239  1 N   A LEU 83  ? ? 1_555 NZ    A LYS 227 ? ? 4_555 1.17 
240  1 C   A ALA 212 ? ? 1_555 C     A ASP 300 ? ? 2_656 1.17 
241  1 N   A SER 85  ? ? 1_555 CA    A LEU 224 ? ? 4_555 1.17 
242  1 CE2 A PHE 241 ? ? 1_555 CD    A PRO 280 ? ? 2_656 1.17 
243  1 C   A GLN 84  ? ? 1_555 CB    A LEU 224 ? ? 4_555 1.17 
244  1 CA  A PHE 93  ? ? 1_555 CB    A LEU 206 ? ? 4_555 1.17 
245  1 O   A VAL 91  ? ? 1_555 O     A ILE 231 ? ? 4_555 1.17 
246  1 N   A GLU 51  ? ? 1_555 N     A LYS 273 ? ? 4_555 1.17 
247  1 CA  A GLN 84  ? ? 1_555 CG    A LEU 224 ? ? 4_555 1.18 
248  1 CE  A LYS 31  ? ? 1_555 N     A GLY 369 ? ? 4_555 1.18 
249  1 NZ  A LYS 31  ? ? 1_555 C     A ILE 368 ? ? 4_555 1.18 
250  1 CD  A LYS 73  ? ? 1_555 C     A LYS 358 ? ? 4_555 1.18 
251  1 OD1 A ASP 287 ? ? 1_555 CE2   A PHE 342 ? ? 2_656 1.18 
252  1 CG  A LYS 31  ? ? 1_555 O     A HIS 388 ? ? 4_555 1.19 
253  1 CA  A ALA 139 ? ? 1_555 CB    A ALA 139 ? ? 2_555 1.19 
254  1 O   A LYS 47  ? ? 1_555 CD    A LYS 273 ? ? 4_555 1.19 
255  1 CG1 A ILE 285 ? ? 1_555 CD2   A LEU 311 ? ? 2_656 1.19 
256  1 CG  A PRO 305 ? ? 1_555 CB    A VAL 339 ? ? 2_656 1.19 
257  1 O   A SER 75  ? ? 1_555 CB    A THR 365 ? ? 4_555 1.19 
258  1 CB  A LEU 245 ? ? 1_555 CB    A VAL 277 ? ? 2_656 1.19 
259  1 CD  A LYS 73  ? ? 1_555 N     A SER 359 ? ? 4_555 1.20 
260  1 C   A GLN 309 ? ? 1_555 N     A LEU 311 ? ? 2_656 1.20 
261  1 O   A LEU 83  ? ? 1_555 O     A LEU 224 ? ? 4_555 1.20 
262  1 N   A LEU 76  ? ? 1_555 O     A THR 365 ? ? 4_555 1.20 
263  1 OD2 A ASP 90  ? ? 1_555 CG1   A ILE 232 ? ? 4_555 1.20 
264  1 N   A ALA 80  ? ? 1_555 CE1   A PHE 205 ? ? 4_555 1.20 
265  1 CA  A ALA 60  ? ? 1_555 O     A THR 202 ? ? 4_555 1.20 
266  1 CG  A PRO 78  ? ? 1_555 N     A ILE 367 ? ? 4_555 1.20 
267  1 O   A LYS 213 ? ? 1_555 O     A ASP 300 ? ? 2_656 1.21 
268  1 CA  A GLN 135 ? ? 1_555 NZ    A LYS 136 ? ? 2_555 1.21 
269  1 CD1 A ILE 221 ? ? 1_555 OE2   A GLU 246 ? ? 2_656 1.21 
270  1 C   A GLY 30  ? ? 1_555 N     A HIS 388 ? ? 4_555 1.21 
271  1 CG1 A ILE 304 ? ? 1_555 CA    A PHE 340 ? ? 2_656 1.21 
272  1 O   A ALA 60  ? ? 1_555 C     A PRO 201 ? ? 4_555 1.21 
273  1 O   A THR 375 ? ? 1_555 CE    A LYS 415 ? ? 4_555 1.21 
274  1 C   A ILE 115 ? ? 1_555 CA    A PRO 204 ? ? 4_555 1.21 
275  1 N   A LEU 94  ? ? 1_555 O     A LYS 327 ? ? 4_555 1.22 
276  1 N   A GLY 236 ? ? 1_555 OD1   A ASN 247 ? ? 2_656 1.22 
277  1 C   A ALA 306 ? ? 1_555 CA    A ASP 312 ? ? 2_656 1.22 
278  1 O   A ALA 306 ? ? 1_555 OD2   A ASP 312 ? ? 2_656 1.22 
279  1 C   A PHE 255 ? ? 1_555 CB    A ASP 282 ? ? 2_656 1.22 
280  1 O   A PHE 93  ? ? 1_555 CD1   A LEU 206 ? ? 4_555 1.22 
281  1 N   A LEU 86  ? ? 1_555 C     A ASN 223 ? ? 4_555 1.22 
282  1 CG  A PRO 27  ? ? 1_555 N     A LYS 192 ? ? 4_555 1.22 
283  1 CA  A LYS 73  ? ? 1_555 CA    A ALA 361 ? ? 4_555 1.22 
284  1 CE2 A PHE 255 ? ? 1_555 CA    A THR 299 ? ? 2_656 1.23 
285  1 CD1 A LEU 59  ? ? 1_555 O     A VAL 228 ? ? 4_555 1.23 
286  1 O   A THR 297 ? ? 1_555 CZ2   A TRP 308 ? ? 2_656 1.23 
287  1 CE1 A HIS 123 ? ? 1_555 CE    A LYS 131 ? ? 2_555 1.23 
288  1 C   A LYS 213 ? ? 1_555 O     A ASP 300 ? ? 2_656 1.23 
289  1 CG  A MET 237 ? ? 1_555 CE1   A PHE 283 ? ? 2_656 1.23 
290  1 CG  A PRO 78  ? ? 1_555 CA    A ILE 367 ? ? 4_555 1.23 
291  1 C   A GLY 235 ? ? 1_555 O     A ASN 247 ? ? 2_656 1.23 
292  1 CD2 A PHE 93  ? ? 1_555 O     A THR 329 ? ? 4_555 1.23 
293  1 CB  A ILE 233 ? ? 1_555 CG    A GLU 249 ? ? 2_656 1.24 
294  1 N   A SER 253 ? ? 1_555 OD1   A ASN 313 ? ? 2_656 1.24 
295  1 CD  A PRO 27  ? ? 1_555 N     A LYS 192 ? ? 4_555 1.24 
296  1 CB  A LYS 379 ? ? 1_555 CD    A LYS 415 ? ? 4_555 1.24 
297  1 CD1 A PHE 241 ? ? 1_555 N     A PRO 280 ? ? 2_656 1.24 
298  1 C   A SER 113 ? ? 1_555 N     A SER 230 ? ? 4_555 1.24 
299  1 CE1 A HIS 123 ? ? 1_555 CD    A LYS 131 ? ? 2_555 1.24 
300  1 CA  A ILE 115 ? ? 1_555 CG    A ASP 229 ? ? 4_555 1.24 
301  1 CD2 A LEU 87  ? ? 1_555 C     A ASP 226 ? ? 4_555 1.24 
302  1 O   A SER 113 ? ? 1_555 C     A SER 230 ? ? 4_555 1.25 
303  1 C   A PHE 283 ? ? 1_555 CD2   A TRP 308 ? ? 2_656 1.25 
304  1 CZ  A PHE 241 ? ? 1_555 CA    A PRO 280 ? ? 2_656 1.25 
305  1 O   A ILE 233 ? ? 1_555 CB    A GLU 249 ? ? 2_656 1.25 
306  1 C   A GLU 72  ? ? 1_555 CA    A ALA 361 ? ? 4_555 1.26 
307  1 N   A LYS 136 ? ? 1_555 CD    A LYS 136 ? ? 2_555 1.26 
308  1 CE  A LYS 73  ? ? 1_555 C     A LYS 358 ? ? 4_555 1.26 
309  1 CD2 A LEU 63  ? ? 1_555 NZ    A LYS 196 ? ? 4_555 1.26 
310  1 CA  A LEU 28  ? ? 1_555 CD2   A TYR 193 ? ? 4_555 1.26 
311  1 CG  A LEU 50  ? ? 1_555 CB    A LYS 273 ? ? 4_555 1.26 
312  1 CA  A ALA 77  ? ? 1_555 C     A ILE 331 ? ? 4_555 1.27 
313  1 CG  A LEU 63  ? ? 1_555 NZ    A LYS 196 ? ? 4_555 1.27 
314  1 CD  A LYS 242 ? ? 1_555 NZ    A LYS 243 ? ? 2_656 1.27 
315  1 N   A LEU 116 ? ? 1_555 CD    A PRO 204 ? ? 4_555 1.27 
316  1 CA  A ALA 306 ? ? 1_555 CB    A ASP 312 ? ? 2_656 1.27 
317  1 O   A THR 34  ? ? 1_555 C     A LEU 191 ? ? 4_555 1.27 
318  1 CA  A GLY 234 ? ? 1_555 O     A GLU 246 ? ? 2_656 1.27 
319  1 CE2 A PHE 255 ? ? 1_555 CB    A THR 299 ? ? 2_656 1.27 
320  1 O   A SER 85  ? ? 1_555 C     A ASN 223 ? ? 4_555 1.28 
321  1 CA  A GLY 236 ? ? 1_555 ND2   A ASN 247 ? ? 2_656 1.28 
322  1 CD2 A LEU 87  ? ? 1_555 N     A LYS 227 ? ? 4_555 1.28 
323  1 CD1 A ILE 304 ? ? 1_555 CD2   A PHE 340 ? ? 2_656 1.28 
324  1 C   A GLN 84  ? ? 1_555 CG    A LEU 224 ? ? 4_555 1.28 
325  1 N   A LYS 89  ? ? 1_555 CD2   A LEU 225 ? ? 4_555 1.28 
326  1 CG  A LYS 379 ? ? 1_555 CA    A LYS 415 ? ? 4_555 1.28 
327  1 N   A THR 240 ? ? 1_555 CA    A THR 240 ? ? 2_656 1.28 
328  1 C   A ILE 232 ? ? 1_555 CD    A GLU 249 ? ? 2_656 1.28 
329  1 N   A GLY 210 ? ? 1_555 CB    A ILE 250 ? ? 2_656 1.28 
330  1 CA  A ALA 77  ? ? 1_555 O     A ILE 331 ? ? 4_555 1.28 
331  1 C   A ILE 254 ? ? 1_555 O     A ASP 282 ? ? 2_656 1.28 
332  1 CB  A LYS 242 ? ? 1_555 CE    A LYS 243 ? ? 2_656 1.29 
333  1 CB  A ALA 306 ? ? 1_555 CA    A ASP 312 ? ? 2_656 1.29 
334  1 OD2 A ASP 29  ? ? 1_555 CE    A LYS 189 ? ? 4_555 1.29 
335  1 C   A ASP 252 ? ? 1_555 CE1   A PHE 321 ? ? 2_656 1.29 
336  1 N   A LEU 116 ? ? 1_555 CA    A PRO 204 ? ? 4_555 1.29 
337  1 CA  A ALA 306 ? ? 1_555 N     A ASP 312 ? ? 2_656 1.29 
338  1 CA  A MET 237 ? ? 1_555 CZ    A PHE 283 ? ? 2_656 1.29 
339  1 CG  A ASP 29  ? ? 1_555 CE    A LYS 189 ? ? 4_555 1.30 
340  1 N   A LEU 116 ? ? 1_555 CG    A PRO 204 ? ? 4_555 1.30 
341  1 CA  A ASP 29  ? ? 1_555 CD    A LYS 189 ? ? 4_555 1.30 
342  1 OD2 A ASP 287 ? ? 1_555 CD2   A PHE 342 ? ? 2_656 1.30 
343  1 CG2 A ILE 304 ? ? 1_555 CA    A PHE 340 ? ? 2_656 1.30 
344  1 CE1 A PHE 24  ? ? 1_555 O     A ALA 197 ? ? 4_555 1.31 
345  1 N   A PRO 305 ? ? 1_555 C     A VAL 339 ? ? 2_656 1.31 
346  1 N   A PHE 283 ? ? 1_555 NE1   A TRP 308 ? ? 2_656 1.31 
347  1 CG2 A ILE 115 ? ? 1_555 CA    A PHE 205 ? ? 4_555 1.31 
348  1 OG  A SER 61  ? ? 1_555 CB    A ARG 203 ? ? 4_555 1.31 
349  1 O   A PHE 283 ? ? 1_555 CE2   A TRP 308 ? ? 2_656 1.31 
350  1 C   A GLY 210 ? ? 1_555 CG1   A ILE 250 ? ? 2_656 1.31 
351  1 C   A LYS 73  ? ? 1_555 N     A ALA 361 ? ? 4_555 1.31 
352  1 N   A SER 75  ? ? 1_555 N     A THR 365 ? ? 4_555 1.31 
353  1 CG1 A ILE 33  ? ? 1_555 CD1   A PHE 194 ? ? 4_555 1.32 
354  1 C   A ASP 252 ? ? 1_555 CZ    A PHE 321 ? ? 2_656 1.32 
355  1 C   A THR 34  ? ? 1_555 N     A LEU 191 ? ? 4_555 1.32 
356  1 N   A LEU 116 ? ? 1_555 CB    A PRO 204 ? ? 4_555 1.32 
357  1 N   A THR 92  ? ? 1_555 CA    A ILE 231 ? ? 4_555 1.33 
358  1 C   A LYS 47  ? ? 1_555 CD    A LYS 273 ? ? 4_555 1.33 
359  1 CD  A LYS 89  ? ? 1_555 CB    A ALA 270 ? ? 4_555 1.33 
360  1 CG  A PHE 241 ? ? 1_555 N     A PRO 280 ? ? 2_656 1.33 
361  1 O   A ALA 77  ? ? 1_555 C     A ILE 331 ? ? 4_555 1.33 
362  1 O   A GLU 82  ? ? 1_555 NZ    A LYS 227 ? ? 4_555 1.33 
363  1 O   A ALA 306 ? ? 1_555 CB    A ASP 312 ? ? 2_656 1.33 
364  1 CD2 A LEU 117 ? ? 1_555 CG2   A THR 202 ? ? 4_555 1.33 
365  1 CE2 A PHE 255 ? ? 1_555 OG1   A THR 299 ? ? 2_656 1.33 
366  1 O   A GLY 251 ? ? 1_555 O     A PRO 337 ? ? 2_656 1.33 
367  1 CD  A PRO 27  ? ? 1_555 C     A LYS 192 ? ? 4_555 1.33 
368  1 O   A LYS 378 ? ? 1_555 OG    A SER 412 ? ? 4_555 1.33 
369  1 CG1 A ILE 115 ? ? 1_555 CA    A PHE 205 ? ? 4_555 1.34 
370  1 CA  A GLY 235 ? ? 1_555 O     A ASN 247 ? ? 2_656 1.34 
371  1 OG  A SER 253 ? ? 1_555 O     A SER 317 ? ? 2_656 1.34 
372  1 OD1 A ASP 287 ? ? 1_555 CD2   A PHE 342 ? ? 2_656 1.34 
373  1 OG1 A THR 34  ? ? 1_555 N     A GLU 190 ? ? 4_555 1.34 
374  1 CA  A GLY 235 ? ? 1_555 C     A ASN 247 ? ? 2_656 1.34 
375  1 CB  A GLN 84  ? ? 1_555 CG    A LEU 224 ? ? 4_555 1.34 
376  1 C   A LEU 116 ? ? 1_555 CD    A PRO 204 ? ? 4_555 1.35 
377  1 CE1 A PHE 241 ? ? 1_555 C     A PRO 280 ? ? 2_656 1.35 
378  1 O   A LEU 87  ? ? 1_555 CG    A LEU 225 ? ? 4_555 1.35 
379  1 CB  A ILE 33  ? ? 1_555 CB    A PHE 194 ? ? 4_555 1.35 
380  1 N   A SER 75  ? ? 1_555 CA    A THR 365 ? ? 4_555 1.35 
381  1 C   A SER 113 ? ? 1_555 CA    A SER 230 ? ? 4_555 1.35 
382  1 CB  A LEU 6   ? ? 1_555 NZ    A LYS 378 ? ? 4_545 1.36 
383  1 CB  A ASP 256 ? ? 1_555 CG2   A VAL 298 ? ? 2_656 1.36 
384  1 CB  A SER 113 ? ? 1_555 CA    A SER 230 ? ? 4_555 1.36 
385  1 O   A LEU 50  ? ? 1_555 N     A LYS 273 ? ? 4_555 1.36 
386  1 NZ  A LYS 32  ? ? 1_555 CB    A SER 396 ? ? 4_555 1.36 
387  1 C   A LEU 86  ? ? 1_555 O     A ASN 223 ? ? 4_555 1.36 
388  1 CA  A ALA 286 ? ? 1_555 CD2   A PHE 289 ? ? 2_656 1.36 
389  1 CB  A ILE 115 ? ? 1_555 C     A PRO 204 ? ? 4_555 1.36 
390  1 O   A ILE 115 ? ? 1_555 CA    A THR 329 ? ? 4_555 1.36 
391  1 CA  A LEU 116 ? ? 1_555 CG    A PRO 204 ? ? 4_555 1.36 
392  1 CA  A THR 34  ? ? 1_555 C     A GLU 190 ? ? 4_555 1.37 
393  1 CB  A LEU 76  ? ? 1_555 CB    A VAL 330 ? ? 4_555 1.37 
394  1 C   A THR 34  ? ? 1_555 CB    A LEU 191 ? ? 4_555 1.37 
395  1 N   A GLY 235 ? ? 1_555 C     A ASN 247 ? ? 2_656 1.37 
396  1 N   A PRO 27  ? ? 1_555 C     A LYS 192 ? ? 4_555 1.37 
397  1 C   A ALA 60  ? ? 1_555 CA    A THR 202 ? ? 4_555 1.37 
398  1 CA  A GLY 210 ? ? 1_555 C     A ILE 250 ? ? 2_656 1.37 
399  1 CB  A LEU 116 ? ? 1_555 CG    A PRO 204 ? ? 4_555 1.37 
400  1 CG2 A VAL 57  ? ? 1_555 O     A GLY 274 ? ? 4_555 1.37 
401  1 O   A LYS 31  ? ? 1_555 CG2   A ILE 367 ? ? 4_555 1.37 
402  1 O   A THR 34  ? ? 1_555 CA    A LEU 191 ? ? 4_555 1.37 
403  1 CB  A ILE 115 ? ? 1_555 CA    A PHE 205 ? ? 4_555 1.38 
404  1 N   A GLY 210 ? ? 1_555 CA    A ILE 250 ? ? 2_656 1.38 
405  1 CG  A PRO 78  ? ? 1_555 CB    A ILE 367 ? ? 4_555 1.38 
406  1 N   A THR 92  ? ? 1_555 O     A ILE 231 ? ? 4_555 1.38 
407  1 CB  A ARG 38  ? ? 1_555 CG    A GLU 199 ? ? 4_555 1.38 
408  1 CG  A LYS 379 ? ? 1_555 CG    A LYS 415 ? ? 4_555 1.38 
409  1 OD2 A ASP 287 ? ? 1_555 CG    A PHE 342 ? ? 2_656 1.38 
410  1 CA  A THR 92  ? ? 1_555 CB    A ILE 231 ? ? 4_555 1.38 
411  1 O   A GLN 84  ? ? 1_555 C     A LEU 224 ? ? 4_555 1.38 
412  1 C   A ILE 304 ? ? 1_555 O     A VAL 339 ? ? 2_656 1.38 
413  1 O   A ASP 23  ? ? 1_555 CB    A GLU 199 ? ? 4_555 1.38 
414  1 CA  A ALA 80  ? ? 1_555 CE1   A PHE 205 ? ? 4_555 1.38 
415  1 CG  A LEU 76  ? ? 1_555 N     A VAL 330 ? ? 4_555 1.38 
416  1 CD1 A LEU 245 ? ? 1_555 C     A VAL 277 ? ? 2_656 1.38 
417  1 CA  A ILE 254 ? ? 1_555 N     A SER 317 ? ? 2_656 1.38 
418  1 CB  A PHE 241 ? ? 1_555 CB    A LEU 279 ? ? 2_656 1.39 
419  1 CA  A ALA 286 ? ? 1_555 CB    A PHE 289 ? ? 2_656 1.39 
420  1 N   A PRO 27  ? ? 1_555 CB    A LYS 192 ? ? 4_555 1.39 
421  1 O   A VAL 22  ? ? 1_555 O     A ASN 200 ? ? 4_555 1.39 
422  1 CB  A ALA 288 ? ? 1_555 CA    A ALA 291 ? ? 2_656 1.39 
423  1 CD2 A PHE 93  ? ? 1_555 O     A ALA 328 ? ? 4_555 1.39 
424  1 CA  A SER 85  ? ? 1_555 CA    A LEU 224 ? ? 4_555 1.39 
425  1 CG  A LEU 83  ? ? 1_555 CB    A LYS 227 ? ? 4_555 1.40 
426  1 N   A THR 34  ? ? 1_555 N     A LEU 191 ? ? 4_555 1.40 
427  1 O   A THR 92  ? ? 1_555 CG1   A ILE 231 ? ? 4_555 1.40 
428  1 O   A LEU 50  ? ? 1_555 C     A ALA 272 ? ? 4_555 1.40 
429  1 N   A TYR 48  ? ? 1_555 NZ    A LYS 273 ? ? 4_555 1.40 
430  1 CG1 A ILE 33  ? ? 1_555 CG    A PHE 194 ? ? 4_555 1.40 
431  1 CB  A LYS 89  ? ? 1_555 CB    A ALA 270 ? ? 4_555 1.40 
432  1 C   A ILE 115 ? ? 1_555 OD2   A ASP 229 ? ? 4_555 1.40 
433  1 C   A LYS 73  ? ? 1_555 C     A SER 360 ? ? 4_555 1.40 
434  1 CA  A GLY 235 ? ? 1_555 N     A THR 248 ? ? 2_656 1.40 
435  1 CE2 A PHE 239 ? ? 1_555 CB    A ASN 247 ? ? 2_656 1.40 
436  1 CB  A LYS 379 ? ? 1_555 CB    A LYS 415 ? ? 4_555 1.41 
437  1 C   A LYS 31  ? ? 1_555 CB    A HIS 388 ? ? 4_555 1.41 
438  1 CG  A LYS 32  ? ? 1_555 CA    A SER 390 ? ? 4_555 1.41 
439  1 C   A GLU 302 ? ? 1_555 CA    A GLY 338 ? ? 2_656 1.41 
440  1 O   A THR 34  ? ? 1_555 N     A LYS 192 ? ? 4_555 1.41 
441  1 C   A ILE 33  ? ? 1_555 C     A GLU 190 ? ? 4_555 1.41 
442  1 CA  A LEU 94  ? ? 1_555 CB    A LYS 327 ? ? 4_555 1.41 
443  1 CA  A ALA 77  ? ? 1_555 CA    A ILE 331 ? ? 4_555 1.42 
444  1 N   A LYS 31  ? ? 1_555 C     A HIS 388 ? ? 4_555 1.42 
445  1 O   A GLU 51  ? ? 1_555 CB    A ALA 272 ? ? 4_555 1.42 
446  1 C   A LEU 94  ? ? 1_555 CA    A LYS 327 ? ? 4_555 1.42 
447  1 O   A GLU 82  ? ? 1_555 CE    A LYS 227 ? ? 4_555 1.42 
448  1 CA  A GLY 211 ? ? 1_555 N     A GLU 302 ? ? 2_656 1.42 
449  1 CA  A ASP 256 ? ? 1_555 CB    A VAL 298 ? ? 2_656 1.43 
450  1 CZ  A PHE 24  ? ? 1_555 O     A ALA 197 ? ? 4_555 1.43 
451  1 N   A ALA 286 ? ? 1_555 CD2   A PHE 289 ? ? 2_656 1.43 
452  1 CB  A PRO 111 ? ? 1_555 CG    A LYS 271 ? ? 4_555 1.43 
453  1 N   A GLY 234 ? ? 1_555 CB    A GLU 249 ? ? 2_656 1.43 
454  1 OG  A SER 35  ? ? 1_555 CB    A LEU 191 ? ? 4_555 1.43 
455  1 CE2 A PHE 255 ? ? 1_555 N     A THR 299 ? ? 2_656 1.43 
456  1 C   A GLY 112 ? ? 1_555 N     A VAL 275 ? ? 4_555 1.43 
457  1 OG  A SER 253 ? ? 1_555 N     A ARG 318 ? ? 2_656 1.43 
458  1 C   A GLU 72  ? ? 1_555 CB    A ALA 361 ? ? 4_555 1.43 
459  1 CB  A LYS 73  ? ? 1_555 N     A ALA 361 ? ? 4_555 1.43 
460  1 CB  A ALA 306 ? ? 1_555 C     A LEU 311 ? ? 2_656 1.43 
461  1 O   A LEU 59  ? ? 1_555 OD1   A ASP 229 ? ? 4_555 1.43 
462  1 O   A GLY 235 ? ? 1_555 O     A ASN 247 ? ? 2_656 1.43 
463  1 C   A ASP 23  ? ? 1_555 N     A ASN 200 ? ? 4_555 1.43 
464  1 CA  A ILE 115 ? ? 1_555 N     A PHE 205 ? ? 4_555 1.43 
465  1 CE  A LYS 378 ? ? 1_555 O     A SER 412 ? ? 4_555 1.44 
466  1 C   A LYS 47  ? ? 1_555 CE    A LYS 273 ? ? 4_555 1.44 
467  1 CD1 A LEU 83  ? ? 1_555 CG    A LYS 227 ? ? 4_555 1.44 
468  1 CB  A ILE 254 ? ? 1_555 CA    A GLU 316 ? ? 2_656 1.44 
469  1 CD1 A PHE 241 ? ? 1_555 CA    A PRO 280 ? ? 2_656 1.44 
470  1 N   A ILE 254 ? ? 1_555 CB    A SER 317 ? ? 2_656 1.44 
471  1 C   A GLN 84  ? ? 1_555 CA    A LEU 224 ? ? 4_555 1.45 
472  1 OD2 A ASP 252 ? ? 1_555 OD1   A ASN 313 ? ? 2_656 1.45 
473  1 CG2 A THR 34  ? ? 1_555 O     A LEU 187 ? ? 4_555 1.45 
474  1 CA  A ASP 90  ? ? 1_555 CB    A ILE 232 ? ? 4_555 1.45 
475  1 C   A LEU 94  ? ? 1_555 N     A ALA 328 ? ? 4_555 1.45 
476  1 CA  A PRO 305 ? ? 1_555 CG1   A VAL 339 ? ? 2_656 1.45 
477  1 C   A LYS 47  ? ? 1_555 NZ    A LYS 273 ? ? 4_555 1.46 
478  1 C   A ALA 306 ? ? 1_555 C     A ASP 312 ? ? 2_656 1.46 
479  1 CZ  A PHE 241 ? ? 1_555 CG    A PRO 280 ? ? 2_656 1.46 
480  1 CD1 A PHE 283 ? ? 1_555 O     A TRP 308 ? ? 2_656 1.46 
481  1 CA  A ALA 288 ? ? 1_555 O     A SER 290 ? ? 2_656 1.46 
482  1 C   A GLY 235 ? ? 1_555 C     A ASN 247 ? ? 2_656 1.46 
483  1 CA  A VAL 376 ? ? 1_555 NZ    A LYS 415 ? ? 4_555 1.46 
484  1 O   A THR 375 ? ? 1_555 NZ    A LYS 415 ? ? 4_555 1.46 
485  1 CB  A SER 61  ? ? 1_555 CB    A ARG 203 ? ? 4_555 1.46 
486  1 CA  A ILE 115 ? ? 1_555 CA    A PRO 204 ? ? 4_555 1.46 
487  1 CB  A LEU 94  ? ? 1_555 CB    A LYS 327 ? ? 4_555 1.47 
488  1 N   A THR 92  ? ? 1_555 CB    A ILE 231 ? ? 4_555 1.47 
489  1 C   A PRO 111 ? ? 1_555 C     A VAL 275 ? ? 4_555 1.47 
490  1 CA  A LEU 28  ? ? 1_555 CE2   A TYR 193 ? ? 4_555 1.47 
491  1 N   A GLY 236 ? ? 1_555 CG    A ASN 247 ? ? 2_656 1.47 
492  1 CD1 A PHE 239 ? ? 1_555 CG2   A VAL 244 ? ? 2_656 1.48 
493  1 CB  A LEU 76  ? ? 1_555 CG1   A VAL 330 ? ? 4_555 1.48 
494  1 N   A GLU 51  ? ? 1_555 C     A ALA 272 ? ? 4_555 1.48 
495  1 N   A GLY 307 ? ? 1_555 N     A ASN 313 ? ? 2_656 1.48 
496  1 CD  A LYS 31  ? ? 1_555 C     A ILE 368 ? ? 4_555 1.48 
497  1 CG1 A ILE 115 ? ? 1_555 N     A PHE 205 ? ? 4_555 1.48 
498  1 CG2 A ILE 254 ? ? 1_555 N     A GLU 316 ? ? 2_656 1.48 
499  1 O   A TYR 74  ? ? 1_555 CG2   A THR 365 ? ? 4_555 1.48 
500  1 CD1 A LEU 83  ? ? 1_555 CA    A LYS 227 ? ? 4_555 1.48 
501  1 C   A GLY 236 ? ? 1_555 ND2   A ASN 247 ? ? 2_656 1.48 
502  1 O   A GLY 112 ? ? 1_555 N     A VAL 275 ? ? 4_555 1.48 
503  1 O   A ALA 212 ? ? 1_555 O     A ASP 300 ? ? 2_656 1.48 
504  1 CA  A LEU 94  ? ? 1_555 O     A LYS 327 ? ? 4_555 1.48 
505  1 CD  A LYS 89  ? ? 1_555 N     A ALA 270 ? ? 4_555 1.48 
506  1 CG1 A VAL 26  ? ? 1_555 N     A LYS 196 ? ? 4_555 1.48 
507  1 C   A ASP 287 ? ? 1_555 O     A SER 290 ? ? 2_656 1.49 
508  1 O   A ILE 232 ? ? 1_555 CD    A GLU 249 ? ? 2_656 1.49 
509  1 O   A VAL 57  ? ? 1_555 OG    A SER 230 ? ? 4_555 1.49 
510  1 N   A LYS 32  ? ? 1_555 CD2   A HIS 388 ? ? 4_555 1.49 
511  1 N   A GLY 88  ? ? 1_555 N     A LEU 225 ? ? 4_555 1.49 
512  1 CA  A GLY 307 ? ? 1_555 O     A ASP 312 ? ? 2_656 1.49 
513  1 CA  A GLY 234 ? ? 1_555 C     A GLU 246 ? ? 2_656 1.49 
514  1 N   A PHE 93  ? ? 1_555 CB    A LEU 206 ? ? 4_555 1.49 
515  1 O   A LEU 86  ? ? 1_555 O     A ASP 222 ? ? 4_555 1.49 
516  1 CA  A SER 85  ? ? 1_555 N     A LEU 224 ? ? 4_555 1.49 
517  1 CA  A PHE 241 ? ? 1_555 CG    A LEU 279 ? ? 2_656 1.49 
518  1 C   A GLU 82  ? ? 1_555 CE    A LYS 227 ? ? 4_555 1.49 
519  1 CD1 A ILE 115 ? ? 1_555 C     A PHE 205 ? ? 4_555 1.50 
520  1 C   A LEU 50  ? ? 1_555 CA    A LYS 273 ? ? 4_555 1.50 
521  1 O   A GLY 234 ? ? 1_555 N     A THR 248 ? ? 2_656 1.50 
522  1 N   A GLY 88  ? ? 1_555 CB    A LEU 225 ? ? 4_555 1.50 
523  1 CG  A PRO 305 ? ? 1_555 CG1   A VAL 339 ? ? 2_656 1.51 
524  1 CG  A PHE 255 ? ? 1_555 C     A VAL 281 ? ? 2_656 1.51 
525  1 OE1 A GLU 82  ? ? 1_555 O     A LEU 400 ? ? 4_555 1.51 
526  1 N   A PRO 27  ? ? 1_555 CA    A LYS 192 ? ? 4_555 1.51 
527  1 CA  A GLY 307 ? ? 1_555 C     A ASP 312 ? ? 2_656 1.51 
528  1 CA  A SER 113 ? ? 1_555 N     A SER 230 ? ? 4_555 1.51 
529  1 CE  A LYS 32  ? ? 1_555 O     A SER 390 ? ? 4_555 1.52 
530  1 CA  A LYS 73  ? ? 1_555 C     A SER 360 ? ? 4_555 1.52 
531  1 C   A ALA 212 ? ? 1_555 N     A LYS 301 ? ? 2_656 1.52 
532  1 N   A VAL 376 ? ? 1_555 NZ    A LYS 415 ? ? 4_555 1.52 
533  1 C   A THR 375 ? ? 1_555 NZ    A LYS 415 ? ? 4_555 1.52 
534  1 OD1 A ASP 90  ? ? 1_555 CG    A LEU 245 ? ? 3_454 1.52 
535  1 OD1 A ASP 90  ? ? 1_555 C     A LEU 245 ? ? 3_454 1.52 
536  1 OE2 A GLU 51  ? ? 1_555 CG    A LYS 269 ? ? 4_555 1.52 
537  1 CE  A LYS 32  ? ? 1_555 CB    A SER 390 ? ? 4_555 1.52 
538  1 CA  A ILE 39  ? ? 1_555 O     A LEU 198 ? ? 4_555 1.52 
539  1 C   A ALA 60  ? ? 1_555 O     A THR 202 ? ? 4_555 1.52 
540  1 CG  A ASP 252 ? ? 1_555 OD1   A ASN 313 ? ? 2_656 1.52 
541  1 CB  A LEU 63  ? ? 1_555 NZ    A LYS 196 ? ? 4_555 1.52 
542  1 CD  A PRO 305 ? ? 1_555 O     A VAL 339 ? ? 2_656 1.52 
543  1 N   A GLY 112 ? ? 1_555 O     A VAL 275 ? ? 4_555 1.53 
544  1 CG  A PHE 24  ? ? 1_555 CD    A PRO 201 ? ? 4_555 1.53 
545  1 CG  A PHE 93  ? ? 1_555 CG2   A THR 329 ? ? 4_555 1.53 
546  1 N   A ILE 115 ? ? 1_555 CB    A ASP 229 ? ? 4_555 1.53 
547  1 CG  A PRO 305 ? ? 1_555 CA    A VAL 339 ? ? 2_656 1.53 
548  1 CA  A ILE 33  ? ? 1_555 O     A GLU 190 ? ? 4_555 1.53 
549  1 CA  A LEU 87  ? ? 1_555 O     A LEU 225 ? ? 4_555 1.53 
550  1 C   A ALA 286 ? ? 1_555 C     A PHE 289 ? ? 2_656 1.53 
551  1 CZ  A PHE 255 ? ? 1_555 C     A THR 299 ? ? 2_656 1.53 
552  1 CB  A ILE 33  ? ? 1_555 N     A PHE 194 ? ? 4_555 1.53 
553  1 C   A VAL 376 ? ? 1_555 NZ    A LYS 415 ? ? 4_555 1.53 
554  1 C   A GLN 84  ? ? 1_555 CD2   A LEU 224 ? ? 4_555 1.53 
555  1 CG1 A ILE 115 ? ? 1_555 C     A PRO 204 ? ? 4_555 1.53 
556  1 CG2 A ILE 304 ? ? 1_555 O     A PHE 340 ? ? 2_656 1.53 
557  1 CB  A GLN 135 ? ? 1_555 CE    A LYS 136 ? ? 2_555 1.53 
558  1 C   A SER 75  ? ? 1_555 N     A THR 365 ? ? 4_555 1.53 
559  1 N   A THR 34  ? ? 1_555 CA    A GLU 190 ? ? 4_555 1.54 
560  1 C   A ILE 233 ? ? 1_555 CG    A GLU 249 ? ? 2_656 1.54 
561  1 CA  A LEU 94  ? ? 1_555 C     A LYS 327 ? ? 4_555 1.54 
562  1 CA  A LEU 86  ? ? 1_555 C     A ASN 223 ? ? 4_555 1.54 
563  1 CA  A GLY 235 ? ? 1_555 CA    A THR 248 ? ? 2_656 1.54 
564  1 CD  A LYS 89  ? ? 1_555 C     A ALA 270 ? ? 4_555 1.54 
565  1 CB  A GLU 302 ? ? 1_555 N7    A ATP 417 ? ? 2_656 1.54 
566  1 CG  A LYS 47  ? ? 1_555 OD1   A ASP 226 ? ? 4_555 1.55 
567  1 CG  A ASP 256 ? ? 1_555 CB    A VAL 298 ? ? 2_656 1.55 
568  1 CE  A LYS 32  ? ? 1_555 OG    A SER 390 ? ? 4_555 1.55 
569  1 CB  A LYS 32  ? ? 1_555 CD2   A HIS 388 ? ? 4_555 1.55 
570  1 CA  A GLY 307 ? ? 1_555 N     A ASN 313 ? ? 2_656 1.55 
571  1 OD2 A ASP 252 ? ? 1_555 ND2   A ASN 313 ? ? 2_656 1.55 
572  1 N   A LYS 32  ? ? 1_555 CG    A HIS 388 ? ? 4_555 1.55 
573  1 CA  A PHE 93  ? ? 1_555 CG2   A THR 329 ? ? 4_555 1.55 
574  1 CG  A ASP 90  ? ? 1_555 CG1   A ILE 232 ? ? 4_555 1.55 
575  1 CB  A MET 237 ? ? 1_555 CD1   A PHE 283 ? ? 2_656 1.55 
576  1 N   A GLY 307 ? ? 1_555 CA    A ASP 312 ? ? 2_656 1.56 
577  1 CA  A GLN 135 ? ? 1_555 CE    A LYS 136 ? ? 2_555 1.56 
578  1 C   A SER 113 ? ? 1_555 C     A SER 230 ? ? 4_555 1.56 
579  1 CA  A GLY 112 ? ? 1_555 CA    A VAL 275 ? ? 4_555 1.56 
580  1 CG  A LYS 73  ? ? 1_555 O     A LYS 358 ? ? 4_555 1.56 
581  1 NZ  A LYS 32  ? ? 1_555 OG    A SER 396 ? ? 4_555 1.56 
582  1 CE2 A PHE 241 ? ? 1_555 CB    A PRO 280 ? ? 2_656 1.56 
583  1 N   A ILE 284 ? ? 1_555 CB    A TRP 308 ? ? 2_656 1.56 
584  1 CG  A LYS 73  ? ? 1_555 C     A SER 359 ? ? 4_555 1.56 
585  1 CE1 A PHE 255 ? ? 1_555 N     A THR 299 ? ? 2_656 1.56 
586  1 CD  A LYS 32  ? ? 1_555 OG    A SER 390 ? ? 4_555 1.56 
587  1 CA  A MET 237 ? ? 1_555 CE1   A PHE 283 ? ? 2_656 1.56 
588  1 C   A SER 85  ? ? 1_555 CA    A LEU 224 ? ? 4_555 1.56 
589  1 O   A ALA 77  ? ? 1_555 CA    A LEU 332 ? ? 4_555 1.56 
590  1 N   A PHE 255 ? ? 1_555 N     A ASP 282 ? ? 2_656 1.56 
591  1 O   A GLY 210 ? ? 1_555 CD1   A ILE 250 ? ? 2_656 1.57 
592  1 N   A ASP 29  ? ? 1_555 CD    A LYS 189 ? ? 4_555 1.57 
593  1 CD  A LYS 31  ? ? 1_555 O     A ILE 368 ? ? 4_555 1.57 
594  1 N   A GLY 303 ? ? 1_555 N     A GLY 338 ? ? 2_656 1.57 
595  1 CD  A LYS 31  ? ? 1_555 N     A ILE 368 ? ? 4_555 1.57 
596  1 CB  A LEU 28  ? ? 1_555 CE2   A TYR 193 ? ? 4_555 1.57 
597  1 C   A ILE 304 ? ? 1_555 O     A PHE 345 ? ? 2_656 1.57 
598  1 O   A ILE 232 ? ? 1_555 CG    A LEU 245 ? ? 2_656 1.57 
599  1 CB  A PRO 78  ? ? 1_555 CA    A ILE 367 ? ? 4_555 1.58 
600  1 N   A ALA 306 ? ? 1_555 CB    A ASP 312 ? ? 2_656 1.58 
601  1 CB  A PHE 283 ? ? 1_555 CG    A TRP 308 ? ? 2_656 1.58 
602  1 CB  A ALA 77  ? ? 1_555 O     A ILE 331 ? ? 4_555 1.58 
603  1 CA  A ALA 60  ? ? 1_555 C     A THR 202 ? ? 4_555 1.58 
604  1 CA  A LYS 47  ? ? 1_555 CD    A LYS 273 ? ? 4_555 1.58 
605  1 O   A THR 34  ? ? 1_555 CB    A LEU 191 ? ? 4_555 1.58 
606  1 CG  A PRO 78  ? ? 1_555 CG1   A ILE 367 ? ? 4_555 1.59 
607  1 C   A LYS 31  ? ? 1_555 CG2   A ILE 367 ? ? 4_555 1.59 
608  1 CB  A LYS 32  ? ? 1_555 NE2   A HIS 388 ? ? 4_555 1.59 
609  1 OG  A SER 1   ? ? 1_555 ND2   A ASN 36  ? ? 4_545 1.59 
610  1 O   A SER 85  ? ? 1_555 CA    A ASN 223 ? ? 4_555 1.59 
611  1 C   A GLY 307 ? ? 1_555 O     A ASP 312 ? ? 2_656 1.59 
612  1 O   A ASP 29  ? ? 1_555 ND1   A HIS 388 ? ? 4_555 1.60 
613  1 N   A PRO 78  ? ? 1_555 O     A ILE 331 ? ? 4_555 1.60 
614  1 N   A GLY 235 ? ? 1_555 O     A ASN 247 ? ? 2_656 1.60 
615  1 OG  A SER 75  ? ? 1_555 C     A ASN 364 ? ? 4_555 1.60 
616  1 CG2 A ILE 115 ? ? 1_555 CB    A PHE 205 ? ? 4_555 1.60 
617  1 CA  A ILE 115 ? ? 1_555 C     A PRO 204 ? ? 4_555 1.60 
618  1 OD1 A ASP 252 ? ? 1_555 CG    A ASN 313 ? ? 2_656 1.60 
619  1 CG2 A THR 92  ? ? 1_555 CG2   A ILE 231 ? ? 4_555 1.60 
620  1 N   A LYS 136 ? ? 1_555 CE    A LYS 136 ? ? 2_555 1.60 
621  1 CG2 A ILE 115 ? ? 1_555 N     A PHE 205 ? ? 4_555 1.60 
622  1 C   A LEU 87  ? ? 1_555 C     A LEU 225 ? ? 4_555 1.60 
623  1 CE1 A PHE 241 ? ? 1_555 N     A PRO 280 ? ? 2_656 1.60 
624  1 CA  A GLY 307 ? ? 1_555 CA    A ASN 313 ? ? 2_656 1.60 
625  1 O   A ILE 33  ? ? 1_555 CB    A PHE 194 ? ? 4_555 1.60 
626  1 CA  A VAL 91  ? ? 1_555 C     A ILE 231 ? ? 4_555 1.60 
627  1 CG1 A ILE 115 ? ? 1_555 O     A PRO 204 ? ? 4_555 1.61 
628  1 CA  A GLU 82  ? ? 1_555 NZ    A LYS 227 ? ? 4_555 1.61 
629  1 CE1 A PHE 24  ? ? 1_555 C     A ALA 197 ? ? 4_555 1.61 
630  1 CA  A THR 92  ? ? 1_555 CG2   A ILE 231 ? ? 4_555 1.61 
631  1 N   A ILE 115 ? ? 1_555 CG    A ASP 229 ? ? 4_555 1.61 
632  1 CE1 A PHE 241 ? ? 1_555 CB    A PRO 280 ? ? 2_656 1.61 
633  1 O   A TYR 56  ? ? 1_555 O     A GLY 274 ? ? 4_555 1.61 
634  1 C   A VAL 79  ? ? 1_555 CZ    A PHE 205 ? ? 4_555 1.61 
635  1 C   A GLY 210 ? ? 1_555 C     A ILE 250 ? ? 2_656 1.61 
636  1 OD2 A ASP 287 ? ? 1_555 CB    A PHE 342 ? ? 2_656 1.61 
637  1 CG1 A ILE 33  ? ? 1_555 CB    A PHE 194 ? ? 4_555 1.62 
638  1 O   A ASP 90  ? ? 1_555 CG2   A ILE 232 ? ? 4_555 1.62 
639  1 NZ  A LYS 73  ? ? 1_555 N     A SER 359 ? ? 4_555 1.62 
640  1 N   A LEU 83  ? ? 1_555 CE    A LYS 227 ? ? 4_555 1.62 
641  1 C   A THR 34  ? ? 1_555 C     A LEU 191 ? ? 4_555 1.62 
642  1 N   A GLY 235 ? ? 1_555 N     A THR 248 ? ? 2_656 1.62 
643  1 CA  A GLY 303 ? ? 1_555 CA    A GLY 338 ? ? 2_656 1.62 
644  1 O   A GLY 112 ? ? 1_555 CB    A VAL 275 ? ? 4_555 1.62 
645  1 CD1 A PHE 241 ? ? 1_555 C     A PRO 280 ? ? 2_656 1.62 
646  1 CG2 A ILE 254 ? ? 1_555 N     A SER 317 ? ? 2_656 1.62 
647  1 CG2 A ILE 115 ? ? 1_555 C     A PHE 205 ? ? 4_555 1.62 
648  1 CA  A LEU 87  ? ? 1_555 CA    A LEU 225 ? ? 4_555 1.62 
649  1 CA  A LYS 213 ? ? 1_555 O     A ASP 300 ? ? 2_656 1.62 
650  1 O   A LYS 89  ? ? 1_555 CG2   A VAL 277 ? ? 4_555 1.62 
651  1 CE1 A PHE 93  ? ? 1_555 CG1   A ILE 331 ? ? 4_555 1.62 
652  1 N   A LEU 87  ? ? 1_555 C     A LEU 225 ? ? 4_555 1.63 
653  1 CA  A ILE 115 ? ? 1_555 CB    A PRO 204 ? ? 4_555 1.63 
654  1 O   A ASP 23  ? ? 1_555 N     A ASN 200 ? ? 4_555 1.63 
655  1 N   A GLN 84  ? ? 1_555 CD2   A LEU 224 ? ? 4_555 1.63 
656  1 C   A VAL 79  ? ? 1_555 CE1   A PHE 205 ? ? 4_555 1.63 
657  1 C   A GLY 112 ? ? 1_555 CB    A SER 230 ? ? 4_555 1.63 
658  1 CA  A PHE 255 ? ? 1_555 C     A ASP 282 ? ? 2_656 1.63 
659  1 CE  A LYS 73  ? ? 1_555 CA    A SER 359 ? ? 4_555 1.63 
660  1 CA  A LEU 83  ? ? 1_555 CG    A LYS 227 ? ? 4_555 1.63 
661  1 O   A VAL 22  ? ? 1_555 CG    A ASN 200 ? ? 4_555 1.63 
662  1 O   A LYS 47  ? ? 1_555 CE    A LYS 273 ? ? 4_555 1.63 
663  1 O   A GLY 234 ? ? 1_555 O     A LEU 245 ? ? 2_656 1.64 
664  1 NZ  A LYS 31  ? ? 1_555 N     A GLY 369 ? ? 4_555 1.64 
665  1 O   A ASP 252 ? ? 1_555 CE2   A PHE 321 ? ? 2_656 1.64 
666  1 CD  A LYS 379 ? ? 1_555 CA    A LYS 415 ? ? 4_555 1.64 
667  1 CB  A THR 34  ? ? 1_555 N     A LEU 191 ? ? 4_555 1.64 
668  1 O   A THR 297 ? ? 1_555 CE2   A TRP 308 ? ? 2_656 1.64 
669  1 N   A SER 113 ? ? 1_555 CA    A SER 230 ? ? 4_555 1.64 
670  1 C   A ILE 115 ? ? 1_555 C     A PRO 204 ? ? 4_555 1.64 
671  1 CG1 A VAL 91  ? ? 1_555 O     A ASP 229 ? ? 4_555 1.64 
672  1 N   A GLY 211 ? ? 1_555 C     A ILE 250 ? ? 2_656 1.64 
673  1 C   A SER 253 ? ? 1_555 CA    A SER 317 ? ? 2_656 1.64 
674  1 CG2 A ILE 39  ? ? 1_555 CB    A LEU 198 ? ? 4_555 1.64 
675  1 OE2 A GLU 302 ? ? 1_555 N6    A ATP 417 ? ? 2_656 1.65 
676  1 C   A GLN 84  ? ? 1_555 C     A LEU 224 ? ? 4_555 1.65 
677  1 O   A GLN 84  ? ? 1_555 N     A LEU 225 ? ? 4_555 1.65 
678  1 CA  A ILE 33  ? ? 1_555 CB    A PHE 194 ? ? 4_555 1.65 
679  1 N   A ILE 115 ? ? 1_555 OD2   A ASP 229 ? ? 4_555 1.65 
680  1 OD1 A ASP 90  ? ? 1_555 CB    A LEU 245 ? ? 3_454 1.65 
681  1 OD2 A ASP 90  ? ? 1_555 C     A ILE 232 ? ? 4_555 1.65 
682  1 CD1 A ILE 254 ? ? 1_555 CB    A GLU 316 ? ? 2_656 1.65 
683  1 OD2 A ASP 29  ? ? 1_555 CD    A LYS 189 ? ? 4_555 1.65 
684  1 CD1 A ILE 304 ? ? 1_555 CB    A PHE 340 ? ? 2_656 1.65 
685  1 CA  A PRO 27  ? ? 1_555 CB    A LYS 192 ? ? 4_555 1.65 
686  1 CD1 A PHE 241 ? ? 1_555 C     A LEU 279 ? ? 2_656 1.65 
687  1 CA  A GLY 303 ? ? 1_555 C     A PRO 337 ? ? 2_656 1.65 
688  1 N   A LEU 245 ? ? 1_555 CG1   A VAL 277 ? ? 2_656 1.66 
689  1 CA  A ILE 233 ? ? 1_555 CB    A GLU 249 ? ? 2_656 1.66 
690  1 CD1 A PHE 24  ? ? 1_555 CA    A ALA 197 ? ? 4_555 1.66 
691  1 CG2 A VAL 26  ? ? 1_555 O     A TYR 193 ? ? 4_555 1.66 
692  1 CB  A PHE 24  ? ? 1_555 CA    A PRO 201 ? ? 4_555 1.66 
693  1 CD1 A PHE 24  ? ? 1_555 CG    A PRO 201 ? ? 4_555 1.66 
694  1 CG2 A ILE 33  ? ? 1_555 CA    A PHE 194 ? ? 4_555 1.66 
695  1 C   A SER 75  ? ? 1_555 CA    A THR 365 ? ? 4_555 1.66 
696  1 N   A GLU 302 ? ? 1_555 C8    A ATP 417 ? ? 2_656 1.66 
697  1 C   A VAL 26  ? ? 1_555 C     A LYS 192 ? ? 4_555 1.66 
698  1 O   A PHE 255 ? ? 1_555 CA    A ASP 282 ? ? 2_656 1.67 
699  1 CA  A LYS 32  ? ? 1_555 CD2   A HIS 388 ? ? 4_555 1.67 
700  1 CD  A LYS 31  ? ? 1_555 CA    A ILE 368 ? ? 4_555 1.67 
701  1 CD2 A PHE 239 ? ? 1_555 CB    A ASN 247 ? ? 2_656 1.67 
702  1 CD  A LYS 73  ? ? 1_555 O     A LYS 358 ? ? 4_555 1.67 
703  1 CA  A THR 240 ? ? 1_555 CA    A THR 240 ? ? 2_656 1.67 
704  1 O   A PRO 305 ? ? 1_555 CD1   A LEU 311 ? ? 2_656 1.67 
705  1 N   A ILE 254 ? ? 1_555 N     A SER 317 ? ? 2_656 1.67 
706  1 CA  A THR 34  ? ? 1_555 CA    A LEU 191 ? ? 4_555 1.67 
707  1 O   A LYS 301 ? ? 1_555 C8    A ATP 417 ? ? 2_656 1.67 
708  1 CA  A ASP 23  ? ? 1_555 N     A ASN 200 ? ? 4_555 1.67 
709  1 N   A LEU 86  ? ? 1_555 N     A LEU 224 ? ? 4_555 1.67 
710  1 C   A VAL 22  ? ? 1_555 O     A ASN 200 ? ? 4_555 1.67 
711  1 N   A GLY 211 ? ? 1_555 N     A GLY 251 ? ? 2_656 1.67 
712  1 C   A GLY 234 ? ? 1_555 N     A THR 248 ? ? 2_656 1.68 
713  1 O   A ILE 250 ? ? 1_555 O     A PRO 337 ? ? 2_656 1.68 
714  1 C   A LYS 301 ? ? 1_555 C8    A ATP 417 ? ? 2_656 1.68 
715  1 N   A VAL 91  ? ? 1_555 CB    A ILE 232 ? ? 4_555 1.68 
716  1 CA  A LEU 94  ? ? 1_555 CA    A LYS 327 ? ? 4_555 1.68 
717  1 CB  A VAL 57  ? ? 1_555 O     A GLY 274 ? ? 4_555 1.68 
718  1 C   A ALA 212 ? ? 1_555 O     A ASP 300 ? ? 2_656 1.68 
719  1 CB  A SER 253 ? ? 1_555 C     A SER 317 ? ? 2_656 1.68 
720  1 O   A ASP 23  ? ? 1_555 CA    A GLU 199 ? ? 4_555 1.68 
721  1 CD2 A PHE 241 ? ? 1_555 CG    A PRO 280 ? ? 2_656 1.68 
722  1 CB  A LEU 50  ? ? 1_555 C     A LYS 273 ? ? 4_555 1.68 
723  1 CA  A GLY 307 ? ? 1_555 C     A ASN 313 ? ? 2_656 1.68 
724  1 CB  A ASP 90  ? ? 1_555 CG2   A ILE 232 ? ? 4_555 1.68 
725  1 CA  A LEU 50  ? ? 1_555 N     A LYS 273 ? ? 4_555 1.69 
726  1 C   A ASP 252 ? ? 1_555 OD1   A ASN 313 ? ? 2_656 1.69 
727  1 CA  A SER 113 ? ? 1_555 OG    A SER 230 ? ? 4_555 1.69 
728  1 N   A SER 85  ? ? 1_555 CG    A LEU 224 ? ? 4_555 1.69 
729  1 O   A GLY 210 ? ? 1_555 CB    A ILE 250 ? ? 2_656 1.69 
730  1 O   A LEU 2   ? ? 1_555 N     A GLN 37  ? ? 4_545 1.69 
731  1 O   A ILE 115 ? ? 1_555 CB    A THR 329 ? ? 4_555 1.69 
732  1 O   A GLU 72  ? ? 1_555 C     A ALA 361 ? ? 4_555 1.69 
733  1 CD  A PRO 305 ? ? 1_555 N     A PHE 340 ? ? 2_656 1.69 
734  1 CA  A ASP 256 ? ? 1_555 CG1   A VAL 298 ? ? 2_656 1.69 
735  1 CA  A SER 75  ? ? 1_555 CA    A THR 365 ? ? 4_555 1.69 
736  1 CA  A GLY 210 ? ? 1_555 CB    A ILE 250 ? ? 2_656 1.69 
737  1 CD  A LYS 378 ? ? 1_555 C     A SER 412 ? ? 4_555 1.69 
738  1 N   A ASP 287 ? ? 1_555 O     A PHE 289 ? ? 2_656 1.69 
739  1 CG  A ASP 90  ? ? 1_555 CG    A LEU 245 ? ? 3_454 1.69 
740  1 CD1 A LEU 76  ? ? 1_555 CA    A VAL 330 ? ? 4_555 1.70 
741  1 O   A ARG 55  ? ? 1_555 CG2   A VAL 275 ? ? 4_555 1.70 
742  1 OG1 A THR 92  ? ? 1_555 CG2   A ILE 231 ? ? 4_555 1.70 
743  1 N   A PHE 93  ? ? 1_555 CG    A LEU 206 ? ? 4_555 1.70 
744  1 CB  A ASP 252 ? ? 1_555 OD1   A ASN 313 ? ? 2_656 1.70 
745  1 CG  A LEU 76  ? ? 1_555 CB    A VAL 330 ? ? 4_555 1.70 
746  1 N   A SER 61  ? ? 1_555 CA    A THR 202 ? ? 4_555 1.70 
747  1 CB  A PHE 24  ? ? 1_555 CD    A PRO 201 ? ? 4_555 1.70 
748  1 OE1 A GLN 84  ? ? 1_555 CD1   A LEU 209 ? ? 4_555 1.70 
749  1 OE1 A GLU 118 ? ? 1_555 ND2   A ASN 364 ? ? 4_555 1.70 
750  1 CD2 A LEU 50  ? ? 1_555 CB    A LYS 273 ? ? 4_555 1.70 
751  1 CG2 A ILE 115 ? ? 1_555 O     A PHE 205 ? ? 4_555 1.70 
752  1 CA  A VAL 91  ? ? 1_555 O     A ILE 231 ? ? 4_555 1.71 
753  1 CB  A ASP 29  ? ? 1_555 CE    A LYS 189 ? ? 4_555 1.71 
754  1 O   A VAL 137 ? ? 1_555 CB    A VAL 137 ? ? 2_555 1.71 
755  1 CE1 A PHE 255 ? ? 1_555 CA    A THR 299 ? ? 2_656 1.71 
756  1 CB  A SER 75  ? ? 1_555 CA    A ASN 364 ? ? 4_555 1.71 
757  1 CG  A PHE 241 ? ? 1_555 C     A LEU 279 ? ? 2_656 1.71 
758  1 CA  A GLU 302 ? ? 1_555 C8    A ATP 417 ? ? 2_656 1.71 
759  1 N   A SER 35  ? ? 1_555 CB    A LEU 191 ? ? 4_555 1.71 
760  1 CG  A LEU 86  ? ? 1_555 ND2   A ASN 223 ? ? 4_555 1.71 
761  1 C   A GLY 235 ? ? 1_555 OD1   A ASN 247 ? ? 2_656 1.71 
762  1 NZ  A LYS 73  ? ? 1_555 O     A GLU 355 ? ? 4_555 1.71 
763  1 CG  A GLU 118 ? ? 1_555 NE    A ARG 203 ? ? 4_555 1.71 
764  1 C   A LEU 76  ? ? 1_555 N     A ILE 331 ? ? 4_555 1.71 
765  1 C   A VAL 22  ? ? 1_555 CA    A ASN 200 ? ? 4_555 1.72 
766  1 NZ  A LYS 31  ? ? 1_555 O     A ILE 368 ? ? 4_555 1.72 
767  1 CA  A SER 85  ? ? 1_555 CB    A LEU 224 ? ? 4_555 1.72 
768  1 CD  A LYS 378 ? ? 1_555 CG    A GLU 413 ? ? 4_555 1.72 
769  1 O   A PHE 239 ? ? 1_555 CB    A LYS 243 ? ? 2_656 1.72 
770  1 O   A GLY 112 ? ? 1_555 C     A GLY 274 ? ? 4_555 1.72 
771  1 CG  A GLU 51  ? ? 1_555 O     A LYS 269 ? ? 4_555 1.72 
772  1 NE2 A HIS 123 ? ? 1_555 CD    A LYS 131 ? ? 2_555 1.72 
773  1 CA  A ILE 232 ? ? 1_555 OE1   A GLU 249 ? ? 2_656 1.72 
774  1 O   A GLU 72  ? ? 1_555 CA    A ALA 361 ? ? 4_555 1.72 
775  1 CB  A PHE 93  ? ? 1_555 CB    A THR 329 ? ? 4_555 1.73 
776  1 N   A ALA 77  ? ? 1_555 N     A ILE 331 ? ? 4_555 1.73 
777  1 CG  A PHE 241 ? ? 1_555 CD    A PRO 280 ? ? 2_656 1.73 
778  1 CG  A ASP 287 ? ? 1_555 CE2   A PHE 342 ? ? 2_656 1.73 
779  1 CG  A LYS 301 ? ? 1_555 "O4'" A ATP 417 ? ? 2_656 1.73 
780  1 C   A ILE 33  ? ? 1_555 CB    A PHE 194 ? ? 4_555 1.73 
781  1 CD1 A LEU 43  ? ? 1_555 OD1   A ASP 226 ? ? 4_555 1.73 
782  1 CB  A THR 92  ? ? 1_555 CB    A ILE 231 ? ? 4_555 1.73 
783  1 N   A LYS 213 ? ? 1_555 O     A ASP 300 ? ? 2_656 1.73 
784  1 N   A LYS 73  ? ? 1_555 N     A ALA 361 ? ? 4_555 1.73 
785  1 C   A PHE 93  ? ? 1_555 O     A LYS 327 ? ? 4_555 1.73 
786  1 N   A ALA 139 ? ? 1_555 CB    A ALA 139 ? ? 2_555 1.73 
787  1 O   A LEU 76  ? ? 1_555 N     A ILE 331 ? ? 4_555 1.73 
788  1 CD1 A ILE 115 ? ? 1_555 CA    A PHE 205 ? ? 4_555 1.73 
789  1 O   A ILE 232 ? ? 1_555 CD2   A LEU 245 ? ? 2_656 1.73 
790  1 NZ  A LYS 31  ? ? 1_555 CG1   A ILE 368 ? ? 4_555 1.73 
791  1 CD2 A PHE 241 ? ? 1_555 N     A PRO 280 ? ? 2_656 1.73 
792  1 C   A GLU 72  ? ? 1_555 C     A ALA 361 ? ? 4_555 1.73 
793  1 C   A PHE 283 ? ? 1_555 CD1   A TRP 308 ? ? 2_656 1.74 
794  1 CA  A LEU 83  ? ? 1_555 CE    A LYS 227 ? ? 4_555 1.74 
795  1 OG  A SER 75  ? ? 1_555 CB    A ASN 364 ? ? 4_555 1.74 
796  1 O   A GLY 30  ? ? 1_555 CA    A HIS 388 ? ? 4_555 1.74 
797  1 CE  A LYS 379 ? ? 1_555 CA    A LYS 415 ? ? 4_555 1.74 
798  1 N   A PRO 27  ? ? 1_555 N     A TYR 193 ? ? 4_555 1.74 
799  1 CB  A VAL 26  ? ? 1_555 C     A LYS 192 ? ? 4_555 1.74 
800  1 CB  A ALA 288 ? ? 1_555 N     A SER 292 ? ? 2_656 1.75 
801  1 N   A ILE 284 ? ? 1_555 CG    A TRP 308 ? ? 2_656 1.75 
802  1 CB  A PHE 255 ? ? 1_555 CA    A VAL 281 ? ? 2_656 1.75 
803  1 C   A ALA 77  ? ? 1_555 N     A LEU 332 ? ? 4_555 1.75 
804  1 CB  A ASP 252 ? ? 1_555 CB    A ASN 313 ? ? 2_656 1.75 
805  1 CD  A PRO 27  ? ? 1_555 CB    A LYS 192 ? ? 4_555 1.75 
806  1 CG1 A VAL 79  ? ? 1_555 CB    A VAL 330 ? ? 4_555 1.75 
807  1 CA  A LYS 31  ? ? 1_555 CA    A HIS 388 ? ? 4_555 1.75 
808  1 C   A ALA 306 ? ? 1_555 CG    A ASP 312 ? ? 2_656 1.75 
809  1 N   A ASP 23  ? ? 1_555 N     A ASN 200 ? ? 4_555 1.75 
810  1 CB  A ALA 212 ? ? 1_555 O     A THR 299 ? ? 2_656 1.75 
811  1 N   A LYS 81  ? ? 1_555 CB    A LEU 332 ? ? 4_555 1.75 
812  1 C   A ILE 232 ? ? 1_555 OE2   A GLU 249 ? ? 2_656 1.75 
813  1 CG  A LYS 378 ? ? 1_555 C     A SER 412 ? ? 4_555 1.75 
814  1 NZ  A LYS 31  ? ? 1_555 CD1   A ILE 368 ? ? 4_555 1.76 
815  1 CA  A PRO 78  ? ? 1_555 O     A ILE 367 ? ? 4_555 1.76 
816  1 C   A SER 75  ? ? 1_555 O     A THR 365 ? ? 4_555 1.76 
817  1 CA  A LEU 86  ? ? 1_555 ND2   A ASN 223 ? ? 4_555 1.76 
818  1 CG1 A VAL 57  ? ? 1_555 CA    A GLY 274 ? ? 4_555 1.76 
819  1 C   A ASP 90  ? ? 1_555 CB    A ILE 232 ? ? 4_555 1.76 
820  1 CA  A PHE 283 ? ? 1_555 CB    A TRP 308 ? ? 2_656 1.76 
821  1 CG1 A ILE 254 ? ? 1_555 CG    A GLU 316 ? ? 2_656 1.76 
822  1 OD2 A ASP 29  ? ? 1_555 CG    A LYS 189 ? ? 4_555 1.76 
823  1 CG1 A ILE 254 ? ? 1_555 C     A GLU 316 ? ? 2_656 1.77 
824  1 O   A GLU 302 ? ? 1_555 O     A PRO 336 ? ? 2_656 1.77 
825  1 O   A ASP 23  ? ? 1_555 C     A GLU 199 ? ? 4_555 1.77 
826  1 CG  A LYS 73  ? ? 1_555 O     A SER 359 ? ? 4_555 1.77 
827  1 CD1 A PHE 93  ? ? 1_555 CD2   A LEU 206 ? ? 4_555 1.77 
828  1 CD  A GLU 82  ? ? 1_555 O     A LEU 400 ? ? 4_555 1.77 
829  1 CB  A ASP 29  ? ? 1_555 CD    A LYS 189 ? ? 4_555 1.77 
830  1 O   A ILE 115 ? ? 1_555 OG1   A THR 329 ? ? 4_555 1.77 
831  1 CA  A VAL 22  ? ? 1_555 CB    A ASN 200 ? ? 4_555 1.77 
832  1 C   A GLY 234 ? ? 1_555 N     A GLU 249 ? ? 2_656 1.77 
833  1 O   A LEU 76  ? ? 1_555 C     A VAL 330 ? ? 4_555 1.77 
834  1 CB  A LYS 31  ? ? 1_555 O     A HIS 388 ? ? 4_555 1.77 
835  1 CG2 A ILE 33  ? ? 1_555 N     A PHE 194 ? ? 4_555 1.77 
836  1 CB  A PRO 27  ? ? 1_555 O     A LYS 189 ? ? 4_555 1.77 
837  1 CB  A PHE 255 ? ? 1_555 O     A VAL 281 ? ? 2_656 1.78 
838  1 O   A PHE 255 ? ? 1_555 OD2   A ASP 282 ? ? 2_656 1.78 
839  1 O   A GLN 84  ? ? 1_555 CA    A LEU 224 ? ? 4_555 1.78 
840  1 CD1 A PHE 93  ? ? 1_555 CG1   A ILE 331 ? ? 4_555 1.78 
841  1 O   A ILE 39  ? ? 1_555 O     A LEU 198 ? ? 4_555 1.78 
842  1 O   A GLN 84  ? ? 1_555 CB    A LEU 224 ? ? 4_555 1.78 
843  1 CD1 A ILE 254 ? ? 1_555 OE1   A GLU 316 ? ? 2_656 1.78 
844  1 O   A PRO 78  ? ? 1_555 CD1   A LEU 332 ? ? 4_555 1.78 
845  1 CB  A LYS 31  ? ? 1_555 CA    A ILE 367 ? ? 4_555 1.78 
846  1 CB  A ALA 306 ? ? 1_555 O     A LEU 311 ? ? 2_656 1.78 
847  1 CE1 A PHE 24  ? ? 1_555 CA    A ALA 197 ? ? 4_555 1.78 
848  1 CB  A ALA 105 ? ? 1_555 NZ    A LYS 327 ? ? 4_555 1.79 
849  1 O   A GLY 30  ? ? 1_555 O     A SER 387 ? ? 4_555 1.79 
850  1 CB  A ALA 288 ? ? 1_555 C     A ALA 291 ? ? 2_656 1.79 
851  1 N   A GLU 302 ? ? 1_555 N7    A ATP 417 ? ? 2_656 1.79 
852  1 N   A LEU 83  ? ? 1_555 CD    A LYS 227 ? ? 4_555 1.79 
853  1 OG  A SER 61  ? ? 1_555 CG    A ARG 203 ? ? 4_555 1.79 
854  1 N   A ASP 256 ? ? 1_555 O     A VAL 281 ? ? 2_656 1.79 
855  1 C   A VAL 49  ? ? 1_555 O     A ALA 272 ? ? 4_555 1.79 
856  1 CA  A PHE 24  ? ? 1_555 CG    A PRO 201 ? ? 4_555 1.79 
857  1 CB  A SER 113 ? ? 1_555 N     A SER 230 ? ? 4_555 1.79 
858  1 O   A PRO 27  ? ? 1_555 CD2   A TYR 193 ? ? 4_555 1.79 
859  1 CB  A LEU 59  ? ? 1_555 CG2   A VAL 228 ? ? 4_555 1.79 
860  1 O   A GLY 236 ? ? 1_555 CB    A THR 240 ? ? 2_656 1.79 
861  1 CG  A PRO 111 ? ? 1_555 CG    A LYS 271 ? ? 4_555 1.79 
862  1 C   A GLY 30  ? ? 1_555 C     A SER 387 ? ? 4_555 1.79 
863  1 C   A TYR 74  ? ? 1_555 CA    A THR 365 ? ? 4_555 1.80 
864  1 CB  A PHE 283 ? ? 1_555 CB    A TRP 308 ? ? 2_656 1.80 
865  1 CB  A ALA 60  ? ? 1_555 CA    A THR 202 ? ? 4_555 1.80 
866  1 C   A VAL 22  ? ? 1_555 OD1   A ASN 200 ? ? 4_555 1.80 
867  1 NZ  A LYS 73  ? ? 1_555 CB    A LYS 358 ? ? 4_555 1.80 
868  1 CG  A GLU 302 ? ? 1_555 N7    A ATP 417 ? ? 2_656 1.80 
869  1 O   A ALA 60  ? ? 1_555 N     A THR 202 ? ? 4_555 1.80 
870  1 CB  A ASP 90  ? ? 1_555 CD2   A LEU 245 ? ? 3_454 1.80 
871  1 CG  A GLU 51  ? ? 1_555 CA    A LYS 269 ? ? 4_555 1.80 
872  1 C   A VAL 26  ? ? 1_555 O     A LYS 192 ? ? 4_555 1.80 
873  1 C   A GLY 234 ? ? 1_555 O     A GLU 246 ? ? 2_656 1.80 
874  1 CD  A LYS 32  ? ? 1_555 O     A SER 390 ? ? 4_555 1.80 
875  1 C   A ILE 39  ? ? 1_555 O     A LEU 198 ? ? 4_555 1.80 
876  1 O   A GLY 112 ? ? 1_555 CA    A VAL 275 ? ? 4_555 1.81 
877  1 N   A ILE 254 ? ? 1_555 OG    A SER 317 ? ? 2_656 1.81 
878  1 CG1 A ILE 33  ? ? 1_555 CA    A PHE 194 ? ? 4_555 1.81 
879  1 O   A LEU 87  ? ? 1_555 CD1   A LEU 225 ? ? 4_555 1.81 
880  1 CB  A LEU 116 ? ? 1_555 CD    A PRO 204 ? ? 4_555 1.81 
881  1 CG2 A ILE 115 ? ? 1_555 CB    A ASP 229 ? ? 4_555 1.81 
882  1 CB  A LYS 73  ? ? 1_555 OG    A SER 360 ? ? 4_555 1.81 
883  1 C   A GLY 210 ? ? 1_555 CB    A ILE 250 ? ? 2_656 1.81 
884  1 O   A SER 85  ? ? 1_555 N     A ASN 223 ? ? 4_555 1.81 
885  1 CA  A PHE 93  ? ? 1_555 CB    A THR 329 ? ? 4_555 1.81 
886  1 CG  A PRO 305 ? ? 1_555 CG2   A VAL 339 ? ? 2_656 1.81 
887  1 CA  A LEU 116 ? ? 1_555 N     A PRO 204 ? ? 4_555 1.81 
888  1 CD1 A ILE 46  ? ? 1_555 O     A LYS 227 ? ? 4_555 1.81 
889  1 C   A PHE 255 ? ? 1_555 N     A ASP 282 ? ? 2_656 1.81 
890  1 NZ  A LYS 89  ? ? 1_555 CA    A LYS 271 ? ? 4_555 1.81 
891  1 OG  A SER 113 ? ? 1_555 CA    A SER 230 ? ? 4_555 1.81 
892  1 CD  A GLN 84  ? ? 1_555 CD1   A LEU 224 ? ? 4_555 1.82 
893  1 C   A LYS 73  ? ? 1_555 O     A SER 360 ? ? 4_555 1.82 
894  1 CG  A LEU 245 ? ? 1_555 CA    A VAL 277 ? ? 2_656 1.82 
895  1 CG1 A ILE 304 ? ? 1_555 N     A PHE 340 ? ? 2_656 1.82 
896  1 N   A TYR 74  ? ? 1_555 C     A SER 360 ? ? 4_555 1.82 
897  1 CA  A ILE 33  ? ? 1_555 N     A PHE 194 ? ? 4_555 1.82 
898  1 CA  A VAL 244 ? ? 1_555 SD    A MET 267 ? ? 2_656 1.82 
899  1 C   A PHE 93  ? ? 1_555 CD1   A LEU 206 ? ? 4_555 1.82 
900  1 OE2 A GLU 118 ? ? 1_555 NH2   A ARG 203 ? ? 4_555 1.82 
901  1 O   A GLU 72  ? ? 1_555 O     A ALA 361 ? ? 4_555 1.82 
902  1 CG1 A ILE 304 ? ? 1_555 CG    A PHE 340 ? ? 2_656 1.82 
903  1 O   A MET 237 ? ? 1_555 OG1   A THR 240 ? ? 2_656 1.82 
904  1 C   A LEU 209 ? ? 1_555 N     A ILE 250 ? ? 2_656 1.82 
905  1 C   A ALA 60  ? ? 1_555 N     A THR 202 ? ? 4_555 1.82 
906  1 CB  A PHE 93  ? ? 1_555 CG    A LEU 206 ? ? 4_555 1.82 
907  1 O   A SER 61  ? ? 1_555 N     A THR 202 ? ? 4_555 1.82 
908  1 CE  A LYS 89  ? ? 1_555 C     A ALA 270 ? ? 4_555 1.83 
909  1 O   A ALA 286 ? ? 1_555 C     A PHE 289 ? ? 2_656 1.83 
910  1 O   A SER 75  ? ? 1_555 CA    A THR 365 ? ? 4_555 1.83 
911  1 N   A LEU 28  ? ? 1_555 CD2   A TYR 193 ? ? 4_555 1.83 
912  1 CA  A LYS 47  ? ? 1_555 CE    A LYS 273 ? ? 4_555 1.83 
913  1 CA  A LYS 73  ? ? 1_555 O     A SER 359 ? ? 4_555 1.83 
914  1 CA  A ALA 77  ? ? 1_555 N     A ILE 331 ? ? 4_555 1.83 
915  1 C   A GLY 30  ? ? 1_555 C     A HIS 388 ? ? 4_555 1.83 
916  1 O   A PHE 283 ? ? 1_555 CG    A TRP 308 ? ? 2_656 1.83 
917  1 OG  A SER 61  ? ? 1_555 CA    A ARG 203 ? ? 4_555 1.83 
918  1 CB  A LYS 378 ? ? 1_555 OE1   A GLU 413 ? ? 4_555 1.83 
919  1 CD  A LYS 73  ? ? 1_555 CA    A SER 359 ? ? 4_555 1.83 
920  1 OD2 A ASP 256 ? ? 1_555 CG2   A VAL 298 ? ? 2_656 1.83 
921  1 C   A GLY 112 ? ? 1_555 CA    A VAL 275 ? ? 4_555 1.83 
922  1 C   A GLY 251 ? ? 1_555 O     A PRO 337 ? ? 2_656 1.83 
923  1 CG1 A ILE 39  ? ? 1_555 N     A LEU 198 ? ? 4_555 1.83 
924  1 N   A LYS 213 ? ? 1_555 O     A THR 299 ? ? 2_656 1.83 
925  1 C   A LYS 73  ? ? 1_555 CA    A ALA 361 ? ? 4_555 1.83 
926  1 NZ  A LYS 73  ? ? 1_555 CA    A LYS 358 ? ? 4_555 1.83 
927  1 C   A GLY 88  ? ? 1_555 CD2   A LEU 225 ? ? 4_555 1.84 
928  1 N   A ILE 233 ? ? 1_555 CG    A GLU 249 ? ? 2_656 1.84 
929  1 NZ  A LYS 213 ? ? 1_555 CD    A LYS 301 ? ? 2_656 1.84 
930  1 CG  A LYS 47  ? ? 1_555 CG    A ASP 226 ? ? 4_555 1.84 
931  1 CB  A SER 61  ? ? 1_555 CD    A ARG 203 ? ? 4_555 1.84 
932  1 CG  A PRO 111 ? ? 1_555 CD    A LYS 271 ? ? 4_555 1.84 
933  1 CG  A ASP 252 ? ? 1_555 CA    A ASN 313 ? ? 2_656 1.84 
934  1 CD2 A PHE 255 ? ? 1_555 OG1   A THR 299 ? ? 2_656 1.84 
935  1 N   A VAL 114 ? ? 1_555 N     A SER 230 ? ? 4_555 1.85 
936  1 CG  A ASP 29  ? ? 1_555 CD    A LYS 189 ? ? 4_555 1.85 
937  1 C   A THR 375 ? ? 1_555 CE    A LYS 415 ? ? 4_555 1.85 
938  1 CG  A PRO 27  ? ? 1_555 CA    A LYS 192 ? ? 4_555 1.85 
939  1 N   A SER 113 ? ? 1_555 O     A SER 230 ? ? 4_555 1.85 
940  1 O   A LEU 94  ? ? 1_555 CA    A ALA 328 ? ? 4_555 1.85 
941  1 CD  A GLU 302 ? ? 1_555 N6    A ATP 417 ? ? 2_656 1.85 
942  1 CA  A VAL 26  ? ? 1_555 C     A LYS 192 ? ? 4_555 1.85 
943  1 C   A VAL 22  ? ? 1_555 C     A ASN 200 ? ? 4_555 1.85 
944  1 CA  A ALA 286 ? ? 1_555 CA    A PHE 289 ? ? 2_656 1.85 
945  1 C   A LEU 209 ? ? 1_555 CB    A ILE 250 ? ? 2_656 1.85 
946  1 O   A SER 113 ? ? 1_555 CA    A SER 230 ? ? 4_555 1.85 
947  1 O   A GLU 302 ? ? 1_555 N     A GLY 338 ? ? 2_656 1.85 
948  1 CA  A GLU 51  ? ? 1_555 CA    A ALA 272 ? ? 4_555 1.86 
949  1 CG2 A THR 92  ? ? 1_555 CG2   A THR 324 ? ? 4_555 1.86 
950  1 CB  A ALA 286 ? ? 1_555 C     A PHE 289 ? ? 2_656 1.86 
951  1 N   A LYS 73  ? ? 1_555 C     A ALA 361 ? ? 4_555 1.86 
952  1 CA  A LEU 50  ? ? 1_555 O     A LYS 273 ? ? 4_555 1.86 
953  1 CD2 A PHE 24  ? ? 1_555 CD    A PRO 201 ? ? 4_555 1.86 
954  1 C   A THR 92  ? ? 1_555 CB    A ILE 231 ? ? 4_555 1.86 
955  1 N   A ALA 286 ? ? 1_555 CG    A PHE 289 ? ? 2_656 1.86 
956  1 O   A VAL 22  ? ? 1_555 ND2   A ASN 200 ? ? 4_555 1.86 
957  1 N   A LEU 50  ? ? 1_555 CA    A LYS 273 ? ? 4_555 1.86 
958  1 CA  A VAL 79  ? ? 1_555 CD1   A LEU 332 ? ? 4_555 1.86 
959  1 OD2 A ASP 90  ? ? 1_555 O     A ILE 232 ? ? 4_555 1.87 
960  1 N   A VAL 22  ? ? 1_555 CG    A ASN 200 ? ? 4_555 1.87 
961  1 CB  A LEU 76  ? ? 1_555 CA    A VAL 330 ? ? 4_555 1.87 
962  1 OD1 A ASP 90  ? ? 1_555 N     A GLU 246 ? ? 3_454 1.87 
963  1 C   A LEU 209 ? ? 1_555 CG2   A ILE 250 ? ? 2_656 1.87 
964  1 N   A LEU 87  ? ? 1_555 O     A ASN 223 ? ? 4_555 1.87 
965  1 CA  A GLY 210 ? ? 1_555 O     A ILE 250 ? ? 2_656 1.87 
966  1 CG1 A VAL 114 ? ? 1_555 CG1   A ILE 231 ? ? 4_555 1.87 
967  1 CB  A THR 248 ? ? 1_555 CA    A LEU 279 ? ? 2_656 1.88 
968  1 CG  A MET 237 ? ? 1_555 CG    A PHE 283 ? ? 2_656 1.88 
969  1 SD  A MET 237 ? ? 1_555 CD1   A PHE 283 ? ? 2_656 1.88 
970  1 C   A THR 297 ? ? 1_555 CZ2   A TRP 308 ? ? 2_656 1.88 
971  1 C   A PHE 283 ? ? 1_555 CB    A TRP 308 ? ? 2_656 1.88 
972  1 C   A ALA 60  ? ? 1_555 O     A PRO 201 ? ? 4_555 1.88 
973  1 O   A SER 35  ? ? 1_555 O     A LEU 191 ? ? 4_555 1.88 
974  1 CA  A ASP 90  ? ? 1_555 CG1   A ILE 232 ? ? 4_555 1.88 
975  1 N   A LYS 31  ? ? 1_555 N     A HIS 388 ? ? 4_555 1.89 
976  1 C   A VAL 91  ? ? 1_555 N     A ILE 232 ? ? 4_555 1.89 
977  1 OD1 A ASP 90  ? ? 1_555 CA    A LEU 245 ? ? 3_454 1.89 
978  1 N   A PHE 255 ? ? 1_555 O     A ASP 282 ? ? 2_656 1.89 
979  1 CG  A LYS 89  ? ? 1_555 CA    A ALA 270 ? ? 4_555 1.89 
980  1 CE  A LYS 378 ? ? 1_555 C     A SER 412 ? ? 4_555 1.89 
981  1 CA  A ARG 38  ? ? 1_555 CG    A GLU 199 ? ? 4_555 1.89 
982  1 C   A ARG 21  ? ? 1_555 OD1   A ASN 200 ? ? 4_555 1.89 
983  1 C   A SER 75  ? ? 1_555 C     A THR 365 ? ? 4_555 1.89 
984  1 CA  A ILE 39  ? ? 1_555 CA    A LEU 198 ? ? 4_555 1.89 
985  1 CD1 A ILE 115 ? ? 1_555 OG1   A THR 329 ? ? 4_555 1.89 
986  1 O   A ILE 254 ? ? 1_555 C     A ASP 282 ? ? 2_656 1.89 
987  1 CA  A PHE 24  ? ? 1_555 CD    A PRO 201 ? ? 4_555 1.89 
988  1 CB  A ASP 29  ? ? 1_555 CE1   A HIS 388 ? ? 4_555 1.89 
989  1 CD2 A LEU 87  ? ? 1_555 CA    A ASP 226 ? ? 4_555 1.89 
990  1 N   A VAL 91  ? ? 1_555 CG2   A ILE 232 ? ? 4_555 1.89 
991  1 CB  A PHE 24  ? ? 1_555 N     A PRO 201 ? ? 4_555 1.90 
992  1 N   A TRP 308 ? ? 1_555 O     A ASP 312 ? ? 2_656 1.90 
993  1 N   A PHE 255 ? ? 1_555 CA    A ASP 282 ? ? 2_656 1.90 
994  1 CA  A PRO 78  ? ? 1_555 CG    A LEU 332 ? ? 4_555 1.90 
995  1 CZ  A PHE 255 ? ? 1_555 CB    A THR 299 ? ? 2_656 1.90 
996  1 CA  A ALA 60  ? ? 1_555 CA    A THR 202 ? ? 4_555 1.90 
997  1 CB  A GLN 84  ? ? 1_555 CD2   A LEU 224 ? ? 4_555 1.90 
998  1 CD  A LYS 31  ? ? 1_555 O     A HIS 388 ? ? 4_555 1.90 
999  1 C   A GLY 210 ? ? 1_555 CA    A ILE 250 ? ? 2_656 1.90 
1000 1 CB  A ILE 39  ? ? 1_555 C     A LEU 198 ? ? 4_555 1.90 
1001 1 CB  A LEU 86  ? ? 1_555 ND2   A ASN 223 ? ? 4_555 1.90 
1002 1 O   A ILE 304 ? ? 1_555 C     A PHE 345 ? ? 2_656 1.90 
1003 1 CD  A GLU 51  ? ? 1_555 CB    A LYS 269 ? ? 4_555 1.90 
1004 1 O   A ILE 232 ? ? 1_555 OE1   A GLU 249 ? ? 2_656 1.90 
1005 1 CA  A SER 61  ? ? 1_555 N     A ARG 203 ? ? 4_555 1.90 
1006 1 CD2 A LEU 76  ? ? 1_555 C     A THR 329 ? ? 4_555 1.90 
1007 1 C   A GLY 88  ? ? 1_555 CG    A LEU 225 ? ? 4_555 1.90 
1008 1 OD2 A ASP 256 ? ? 1_555 CG1   A VAL 298 ? ? 2_656 1.90 
1009 1 C   A LEU 50  ? ? 1_555 O     A ALA 272 ? ? 4_555 1.90 
1010 1 C   A GLU 302 ? ? 1_555 N     A GLY 338 ? ? 2_656 1.90 
1011 1 C   A LEU 209 ? ? 1_555 CA    A ILE 250 ? ? 2_656 1.90 
1012 1 OD1 A ASP 90  ? ? 1_555 CG1   A VAL 277 ? ? 4_555 1.90 
1013 1 C   A ASP 282 ? ? 1_555 CD1   A TRP 308 ? ? 2_656 1.90 
1014 1 N   A LYS 32  ? ? 1_555 CB    A HIS 388 ? ? 4_555 1.90 
1015 1 C   A LEU 94  ? ? 1_555 O     A LYS 327 ? ? 4_555 1.91 
1016 1 C   A VAL 114 ? ? 1_555 CB    A ASP 229 ? ? 4_555 1.91 
1017 1 N   A GLY 211 ? ? 1_555 O     A ILE 250 ? ? 2_656 1.91 
1018 1 C   A LEU 59  ? ? 1_555 OD1   A ASP 229 ? ? 4_555 1.91 
1019 1 CB  A LEU 245 ? ? 1_555 CA    A VAL 277 ? ? 2_656 1.91 
1020 1 CG  A ASP 90  ? ? 1_555 O     A ILE 232 ? ? 4_555 1.91 
1021 1 C   A LEU 87  ? ? 1_555 CG    A LEU 225 ? ? 4_555 1.91 
1022 1 CG  A ASP 252 ? ? 1_555 ND2   A ASN 313 ? ? 2_656 1.91 
1023 1 O   A ALA 212 ? ? 1_555 CA    A LYS 301 ? ? 2_656 1.91 
1024 1 N   A SER 290 ? ? 1_555 O     A SER 292 ? ? 2_656 1.91 
1025 1 C   A VAL 114 ? ? 1_555 CG    A ASP 229 ? ? 4_555 1.91 
1026 1 C   A PRO 78  ? ? 1_555 CD2   A LEU 332 ? ? 4_555 1.92 
1027 1 CD1 A LEU 59  ? ? 1_555 CA    A ASP 229 ? ? 4_555 1.92 
1028 1 CB  A ASP 252 ? ? 1_555 CG    A ASN 313 ? ? 2_656 1.92 
1029 1 OD1 A ASP 252 ? ? 1_555 CA    A ASN 313 ? ? 2_656 1.92 
1030 1 CG  A GLU 51  ? ? 1_555 C     A LYS 269 ? ? 4_555 1.92 
1031 1 CG  A LEU 59  ? ? 1_555 C     A VAL 228 ? ? 4_555 1.92 
1032 1 CA  A SER 75  ? ? 1_555 O     A ASN 364 ? ? 4_555 1.92 
1033 1 N   A ILE 33  ? ? 1_555 CG    A PHE 194 ? ? 4_555 1.92 
1034 1 CD2 A PHE 239 ? ? 1_555 ND2   A ASN 247 ? ? 2_656 1.92 
1035 1 CD2 A LEU 76  ? ? 1_555 O     A THR 329 ? ? 4_555 1.92 
1036 1 C   A ASP 29  ? ? 1_555 ND1   A HIS 388 ? ? 4_555 1.92 
1037 1 N   A ALA 288 ? ? 1_555 N     A ALA 291 ? ? 2_656 1.93 
1038 1 C   A LEU 86  ? ? 1_555 N     A ASP 226 ? ? 4_555 1.93 
1039 1 OG  A SER 113 ? ? 1_555 O     A ASP 229 ? ? 4_555 1.93 
1040 1 CB  A ILE 304 ? ? 1_555 C     A VAL 339 ? ? 2_656 1.93 
1041 1 N   A VAL 91  ? ? 1_555 CA    A ILE 232 ? ? 4_555 1.93 
1042 1 NZ  A LYS 89  ? ? 1_555 O     A GLU 268 ? ? 4_555 1.93 
1043 1 CD1 A LEU 245 ? ? 1_555 CA    A VAL 277 ? ? 2_656 1.93 
1044 1 O   A VAL 114 ? ? 1_555 CG    A ASP 229 ? ? 4_555 1.93 
1045 1 N   A SER 61  ? ? 1_555 O     A THR 202 ? ? 4_555 1.93 
1046 1 O   A ALA 374 ? ? 1_555 OE1   A GLU 413 ? ? 4_555 1.93 
1047 1 CB  A LEU 83  ? ? 1_555 CD    A LYS 227 ? ? 4_555 1.93 
1048 1 N   A PHE 24  ? ? 1_555 N     A PRO 201 ? ? 4_555 1.93 
1049 1 CB  A SER 75  ? ? 1_555 N     A THR 365 ? ? 4_555 1.93 
1050 1 C   A ILE 115 ? ? 1_555 CG    A PRO 204 ? ? 4_555 1.93 
1051 1 CG  A PHE 24  ? ? 1_555 CB    A PRO 201 ? ? 4_555 1.93 
1052 1 CA  A PHE 255 ? ? 1_555 C     A VAL 281 ? ? 2_656 1.93 
1053 1 N   A MET 237 ? ? 1_555 CZ    A PHE 283 ? ? 2_656 1.94 
1054 1 C   A THR 92  ? ? 1_555 CD1   A ILE 231 ? ? 4_555 1.94 
1055 1 CA  A ILE 254 ? ? 1_555 CA    A SER 317 ? ? 2_656 1.94 
1056 1 OG  A SER 61  ? ? 1_555 N     A ARG 203 ? ? 4_555 1.94 
1057 1 CA  A PRO 305 ? ? 1_555 O     A VAL 339 ? ? 2_656 1.94 
1058 1 CA  A GLU 72  ? ? 1_555 CB    A ALA 361 ? ? 4_555 1.94 
1059 1 CB  A ALA 288 ? ? 1_555 N     A ALA 291 ? ? 2_656 1.94 
1060 1 O   A THR 92  ? ? 1_555 CB    A ILE 231 ? ? 4_555 1.94 
1061 1 C   A MET 237 ? ? 1_555 CZ    A PHE 283 ? ? 2_656 1.94 
1062 1 N   A ILE 39  ? ? 1_555 N     A GLU 199 ? ? 4_555 1.94 
1063 1 O   A LEU 94  ? ? 1_555 CA    A LYS 327 ? ? 4_555 1.94 
1064 1 CG2 A THR 248 ? ? 1_555 CA    A LEU 279 ? ? 2_656 1.94 
1065 1 O   A LEU 76  ? ? 1_555 CB    A VAL 330 ? ? 4_555 1.94 
1066 1 CG2 A THR 248 ? ? 1_555 CD2   A LEU 279 ? ? 2_656 1.94 
1067 1 CG1 A VAL 114 ? ? 1_555 CD1   A ILE 231 ? ? 4_555 1.95 
1068 1 CB  A ALA 286 ? ? 1_555 N     A PHE 289 ? ? 2_656 1.95 
1069 1 CZ  A PHE 241 ? ? 1_555 N     A PRO 280 ? ? 2_656 1.95 
1070 1 C   A SER 75  ? ? 1_555 OG1   A THR 365 ? ? 4_555 1.95 
1071 1 O   A GLN 309 ? ? 1_555 C     A LEU 311 ? ? 2_656 1.95 
1072 1 O   A ILE 304 ? ? 1_555 OD1   A ASP 312 ? ? 2_656 1.95 
1073 1 N   A SER 113 ? ? 1_555 C     A SER 230 ? ? 4_555 1.95 
1074 1 CG  A ASP 29  ? ? 1_555 CB    A LYS 189 ? ? 4_555 1.95 
1075 1 CA  A PHE 93  ? ? 1_555 CG    A LEU 206 ? ? 4_555 1.95 
1076 1 O   A GLY 234 ? ? 1_555 CG2   A THR 248 ? ? 2_656 1.95 
1077 1 C   A GLY 234 ? ? 1_555 C     A GLU 246 ? ? 2_656 1.95 
1078 1 OG1 A THR 34  ? ? 1_555 O     A LEU 187 ? ? 4_555 1.95 
1079 1 CD1 A LEU 76  ? ? 1_555 CB    A VAL 330 ? ? 4_555 1.95 
1080 1 OE1 A GLN 84  ? ? 1_555 CB    A LEU 209 ? ? 4_555 1.95 
1081 1 C   A ALA 286 ? ? 1_555 CD2   A PHE 289 ? ? 2_656 1.95 
1082 1 N   A LEU 116 ? ? 1_555 OD2   A ASP 229 ? ? 4_555 1.96 
1083 1 CG  A LEU 83  ? ? 1_555 CG    A LYS 227 ? ? 4_555 1.96 
1084 1 O   A GLY 235 ? ? 1_555 OD1   A ASN 247 ? ? 2_656 1.96 
1085 1 N   A ALA 212 ? ? 1_555 C     A LYS 301 ? ? 2_656 1.96 
1086 1 O   A THR 297 ? ? 1_555 NE1   A TRP 308 ? ? 2_656 1.96 
1087 1 OG  A SER 113 ? ? 1_555 N     A SER 230 ? ? 4_555 1.96 
1088 1 CA  A ILE 39  ? ? 1_555 N     A GLU 199 ? ? 4_555 1.96 
1089 1 OG  A SER 113 ? ? 1_555 C     A ASP 229 ? ? 4_555 1.96 
1090 1 CG1 A ILE 221 ? ? 1_555 OE2   A GLU 246 ? ? 2_656 1.96 
1091 1 O   A ILE 33  ? ? 1_555 O     A GLU 190 ? ? 4_555 1.96 
1092 1 CB  A THR 34  ? ? 1_555 N     A GLU 190 ? ? 4_555 1.96 
1093 1 CE  A LYS 31  ? ? 1_555 CA    A ILE 368 ? ? 4_555 1.96 
1094 1 OG  A SER 253 ? ? 1_555 CA    A SER 317 ? ? 2_656 1.96 
1095 1 OG1 A THR 248 ? ? 1_555 CA    A LEU 279 ? ? 2_656 1.96 
1096 1 N   A LEU 6   ? ? 1_555 NZ    A LYS 378 ? ? 4_545 1.96 
1097 1 C   A GLN 309 ? ? 1_555 CA    A LEU 311 ? ? 2_656 1.96 
1098 1 O   A LYS 213 ? ? 1_555 C     A ASP 300 ? ? 2_656 1.96 
1099 1 CA  A GLY 234 ? ? 1_555 CA    A GLU 246 ? ? 2_656 1.96 
1100 1 CA  A LEU 76  ? ? 1_555 O     A THR 365 ? ? 4_555 1.96 
1101 1 CA  A PRO 305 ? ? 1_555 CB    A VAL 339 ? ? 2_656 1.96 
1102 1 CD  A LYS 379 ? ? 1_555 CG    A LYS 415 ? ? 4_555 1.97 
1103 1 CA  A GLY 211 ? ? 1_555 CA    A GLU 302 ? ? 2_656 1.97 
1104 1 N   A VAL 91  ? ? 1_555 N     A ILE 232 ? ? 4_555 1.97 
1105 1 O   A LEU 209 ? ? 1_555 C     A GLU 249 ? ? 2_656 1.97 
1106 1 CG  A LEU 87  ? ? 1_555 O     A LEU 225 ? ? 4_555 1.97 
1107 1 C   A ILE 285 ? ? 1_555 CD2   A PHE 289 ? ? 2_656 1.97 
1108 1 N   A ASN 25  ? ? 1_555 CB    A LYS 196 ? ? 4_555 1.97 
1109 1 N   A VAL 26  ? ? 1_555 CE    A LYS 196 ? ? 4_555 1.97 
1110 1 CA  A ILE 33  ? ? 1_555 CA    A PHE 194 ? ? 4_555 1.97 
1111 1 CE  A LYS 301 ? ? 1_555 "C4'" A ATP 417 ? ? 2_656 1.97 
1112 1 C   A ILE 115 ? ? 1_555 N     A PRO 204 ? ? 4_555 1.97 
1113 1 C   A LYS 31  ? ? 1_555 CG    A HIS 388 ? ? 4_555 1.97 
1114 1 CG  A ASP 90  ? ? 1_555 CD2   A LEU 245 ? ? 3_454 1.97 
1115 1 CB  A ALA 286 ? ? 1_555 CG    A PHE 289 ? ? 2_656 1.97 
1116 1 CB  A LYS 81  ? ? 1_555 CB    A LEU 332 ? ? 4_555 1.98 
1117 1 CB  A ASP 90  ? ? 1_555 CG1   A ILE 232 ? ? 4_555 1.98 
1118 1 CB  A VAL 57  ? ? 1_555 C     A GLY 274 ? ? 4_555 1.98 
1119 1 CD  A PRO 27  ? ? 1_555 N     A TYR 193 ? ? 4_555 1.98 
1120 1 C   A ILE 233 ? ? 1_555 CA    A GLU 249 ? ? 2_656 1.98 
1121 1 N   A GLY 112 ? ? 1_555 CB    A VAL 275 ? ? 4_555 1.98 
1122 1 CG  A LEU 6   ? ? 1_555 NZ    A LYS 378 ? ? 4_545 1.98 
1123 1 CD  A LYS 73  ? ? 1_555 C     A SER 359 ? ? 4_555 1.98 
1124 1 O   A VAL 91  ? ? 1_555 O     A ALA 207 ? ? 4_555 1.98 
1125 1 CB  A ALA 238 ? ? 1_555 CA    A VAL 281 ? ? 2_656 1.98 
1126 1 CG  A GLN 84  ? ? 1_555 CG    A LEU 224 ? ? 4_555 1.98 
1127 1 N   A PRO 305 ? ? 1_555 CA    A VAL 339 ? ? 2_656 1.98 
1128 1 CG  A ASP 287 ? ? 1_555 CG    A PHE 342 ? ? 2_656 1.98 
1129 1 O   A GLY 30  ? ? 1_555 CA    A SER 387 ? ? 4_555 1.98 
1130 1 CB  A ASP 29  ? ? 1_555 NZ    A LYS 189 ? ? 4_555 1.98 
1131 1 O   A PHE 283 ? ? 1_555 NE1   A TRP 308 ? ? 2_656 1.98 
1132 1 N   A GLY 235 ? ? 1_555 C     A THR 248 ? ? 2_656 1.98 
1133 1 O   A LEU 50  ? ? 1_555 N     A ALA 272 ? ? 4_555 1.98 
1134 1 C   A ILE 304 ? ? 1_555 C     A VAL 339 ? ? 2_656 1.98 
1135 1 CE2 A PHE 93  ? ? 1_555 O     A ALA 328 ? ? 4_555 1.98 
1136 1 N   A PHE 283 ? ? 1_555 CG    A TRP 308 ? ? 2_656 1.98 
1137 1 O   A LEU 209 ? ? 1_555 CA    A ILE 250 ? ? 2_656 1.98 
1138 1 CB  A ILE 304 ? ? 1_555 CB    A PHE 340 ? ? 2_656 1.98 
1139 1 CG  A LEU 59  ? ? 1_555 O     A VAL 228 ? ? 4_555 1.99 
1140 1 NZ  A LYS 73  ? ? 1_555 C     A LYS 358 ? ? 4_555 1.99 
1141 1 CG1 A VAL 91  ? ? 1_555 O     A PHE 205 ? ? 4_555 1.99 
1142 1 O   A SER 35  ? ? 1_555 N     A GLY 195 ? ? 4_555 1.99 
1143 1 O   A VAL 91  ? ? 1_555 C     A ILE 231 ? ? 4_555 1.99 
1144 1 O   A LEU 50  ? ? 1_555 CA    A ALA 272 ? ? 4_555 1.99 
1145 1 CD2 A LEU 76  ? ? 1_555 N     A VAL 330 ? ? 4_555 1.99 
1146 1 CA  A GLY 88  ? ? 1_555 O     A ILE 221 ? ? 4_555 1.99 
1147 1 C   A SER 113 ? ? 1_555 N     A ILE 231 ? ? 4_555 1.99 
1148 1 CB  A LYS 47  ? ? 1_555 CE    A LYS 273 ? ? 4_555 1.99 
1149 1 O   A VAL 79  ? ? 1_555 CE2   A PHE 205 ? ? 4_555 1.99 
1150 1 N   A SER 61  ? ? 1_555 N     A THR 202 ? ? 4_555 1.99 
1151 1 CB  A PRO 78  ? ? 1_555 CG1   A ILE 367 ? ? 4_555 1.99 
1152 1 CB  A ILE 304 ? ? 1_555 C     A PHE 340 ? ? 2_656 1.99 
1153 1 CD1 A PHE 241 ? ? 1_555 O     A LEU 279 ? ? 2_656 2.00 
1154 1 CG2 A ILE 254 ? ? 1_555 CA    A GLU 316 ? ? 2_656 2.00 
1155 1 N   A PHE 289 ? ? 1_555 CE1   A PHE 345 ? ? 2_656 2.00 
1156 1 CA  A ASP 252 ? ? 1_555 OD1   A ASN 313 ? ? 2_656 2.00 
1157 1 O   A PRO 27  ? ? 1_555 CG    A TYR 193 ? ? 4_555 2.00 
1158 1 CD  A GLN 84  ? ? 1_555 CD1   A LEU 209 ? ? 4_555 2.00 
1159 1 CD  A LYS 89  ? ? 1_555 N     A LYS 271 ? ? 4_555 2.00 
1160 1 CG1 A VAL 259 ? ? 1_555 OG1   A THR 299 ? ? 2_656 2.00 
1161 1 C   A GLU 51  ? ? 1_555 CA    A ALA 272 ? ? 4_555 2.00 
1162 1 N   A LYS 243 ? ? 1_555 CB    A LYS 243 ? ? 2_656 2.00 
1163 1 N   A LEU 86  ? ? 1_555 CA    A LEU 224 ? ? 4_555 2.00 
1164 1 CB  A ALA 238 ? ? 1_555 CG2   A VAL 281 ? ? 2_656 2.00 
1165 1 O   A GLY 112 ? ? 1_555 CG1   A VAL 275 ? ? 4_555 2.00 
1166 1 O   A PRO 111 ? ? 1_555 C     A VAL 275 ? ? 4_555 2.00 
1167 1 CB  A VAL 244 ? ? 1_555 CG    A MET 267 ? ? 2_656 2.00 
1168 1 C   A ASN 25  ? ? 1_555 CB    A LYS 196 ? ? 4_555 2.00 
1169 1 O   A LYS 32  ? ? 1_555 CA    A GLU 190 ? ? 4_555 2.00 
1170 1 CG2 A THR 248 ? ? 1_555 O     A VAL 278 ? ? 2_656 2.00 
1171 1 C   A ALA 60  ? ? 1_555 C     A PRO 201 ? ? 4_555 2.00 
1172 1 O   A GLY 112 ? ? 1_555 CB    A SER 230 ? ? 4_555 2.00 
1173 1 CD1 A LEU 86  ? ? 1_555 O     A GLU 401 ? ? 4_555 2.00 
1174 1 O   A VAL 91  ? ? 1_555 N     A ALA 207 ? ? 4_555 2.00 
1175 1 CE2 A PHE 241 ? ? 1_555 N     A PRO 280 ? ? 2_656 2.00 
1176 1 CB  A LYS 73  ? ? 1_555 O     A SER 359 ? ? 4_555 2.00 
1177 1 CA  A LYS 379 ? ? 1_555 CD    A LYS 415 ? ? 4_555 2.00 
1178 1 O   A ASN 25  ? ? 1_555 CB    A LYS 196 ? ? 4_555 2.01 
1179 1 O   A LEU 2   ? ? 1_555 CA    A GLN 37  ? ? 4_545 2.01 
1180 1 CG1 A VAL 26  ? ? 1_555 O     A LYS 192 ? ? 4_555 2.01 
1181 1 CD1 A LEU 86  ? ? 1_555 OD1   A ASN 223 ? ? 4_555 2.01 
1182 1 NZ  A LYS 73  ? ? 1_555 N     A LYS 358 ? ? 4_555 2.01 
1183 1 CE  A LYS 32  ? ? 1_555 C     A SER 390 ? ? 4_555 2.01 
1184 1 C   A PRO 27  ? ? 1_555 CD2   A TYR 193 ? ? 4_555 2.01 
1185 1 O   A SER 113 ? ? 1_555 N     A SER 230 ? ? 4_555 2.01 
1186 1 CA  A LYS 136 ? ? 1_555 CD    A LYS 136 ? ? 2_555 2.01 
1187 1 CD  A PRO 305 ? ? 1_555 CB    A VAL 339 ? ? 2_656 2.01 
1188 1 CB  A PRO 27  ? ? 1_555 CB    A LYS 192 ? ? 4_555 2.01 
1189 1 OG1 A THR 248 ? ? 1_555 C     A LEU 279 ? ? 2_656 2.01 
1190 1 C   A LEU 83  ? ? 1_555 O     A LEU 224 ? ? 4_555 2.01 
1191 1 CB  A PRO 305 ? ? 1_555 CG2   A VAL 339 ? ? 2_656 2.01 
1192 1 NZ  A LYS 89  ? ? 1_555 C     A ALA 270 ? ? 4_555 2.01 
1193 1 CD1 A PHE 241 ? ? 1_555 O     A PRO 280 ? ? 2_656 2.01 
1194 1 CB  A VAL 22  ? ? 1_555 OD1   A ASN 200 ? ? 4_555 2.01 
1195 1 CD  A PRO 78  ? ? 1_555 C     A VAL 366 ? ? 4_555 2.01 
1196 1 CB  A ILE 254 ? ? 1_555 CB    A GLU 316 ? ? 2_656 2.01 
1197 1 C   A GLY 236 ? ? 1_555 CG2   A THR 240 ? ? 2_656 2.02 
1198 1 OG  A SER 75  ? ? 1_555 O     A ASN 364 ? ? 4_555 2.02 
1199 1 N   A THR 240 ? ? 1_555 CB    A THR 240 ? ? 2_656 2.02 
1200 1 CA  A PHE 283 ? ? 1_555 CD2   A TRP 308 ? ? 2_656 2.02 
1201 1 CB  A ALA 60  ? ? 1_555 CB    A THR 202 ? ? 4_555 2.02 
1202 1 O   A ILE 254 ? ? 1_555 OG    A SER 317 ? ? 2_656 2.02 
1203 1 N   A GLY 112 ? ? 1_555 N     A GLU 276 ? ? 4_555 2.02 
1204 1 CA  A GLU 302 ? ? 1_555 C5    A ATP 417 ? ? 2_656 2.02 
1205 1 C   A LEU 86  ? ? 1_555 C     A ASN 223 ? ? 4_555 2.02 
1206 1 O   A ASP 29  ? ? 1_555 CG    A HIS 388 ? ? 4_555 2.02 
1207 1 N   A SER 75  ? ? 1_555 C     A ASN 364 ? ? 4_555 2.02 
1208 1 O   A LEU 94  ? ? 1_555 O     A LYS 327 ? ? 4_555 2.02 
1209 1 CB  A MET 237 ? ? 1_555 CE2   A PHE 283 ? ? 2_656 2.02 
1210 1 O   A VAL 114 ? ? 1_555 OD1   A ASP 229 ? ? 4_555 2.02 
1211 1 CD  A GLU 118 ? ? 1_555 NE    A ARG 203 ? ? 4_555 2.02 
1212 1 O   A GLY 307 ? ? 1_555 N     A GLY 314 ? ? 2_656 2.02 
1213 1 CE2 A PHE 93  ? ? 1_555 O     A THR 329 ? ? 4_555 2.02 
1214 1 C   A SER 85  ? ? 1_555 O     A ASN 223 ? ? 4_555 2.02 
1215 1 CA  A SER 113 ? ? 1_555 C     A SER 230 ? ? 4_555 2.02 
1216 1 CB  A LEU 86  ? ? 1_555 O     A ASN 223 ? ? 4_555 2.02 
1217 1 CB  A THR 34  ? ? 1_555 O     A LEU 187 ? ? 4_555 2.02 
1218 1 CA  A LYS 73  ? ? 1_555 C     A ALA 361 ? ? 4_555 2.03 
1219 1 C   A SER 113 ? ? 1_555 C     A ASP 229 ? ? 4_555 2.03 
1220 1 O   A ILE 115 ? ? 1_555 CB    A PRO 204 ? ? 4_555 2.03 
1221 1 CD2 A PHE 239 ? ? 1_555 CG    A ASN 247 ? ? 2_656 2.03 
1222 1 O   A SER 75  ? ? 1_555 CG2   A THR 365 ? ? 4_555 2.03 
1223 1 CG2 A VAL 22  ? ? 1_555 C     A ASN 200 ? ? 4_555 2.03 
1224 1 CZ  A PHE 93  ? ? 1_555 CD1   A ILE 331 ? ? 4_555 2.03 
1225 1 CB  A ALA 238 ? ? 1_555 N     A VAL 281 ? ? 2_656 2.03 
1226 1 O   A PHE 283 ? ? 1_555 CE3   A TRP 308 ? ? 2_656 2.03 
1227 1 CE  A LYS 31  ? ? 1_555 CA    A GLY 369 ? ? 4_555 2.03 
1228 1 OD1 A ASP 90  ? ? 1_555 OE2   A GLU 249 ? ? 3_454 2.03 
1229 1 C   A VAL 22  ? ? 1_555 ND2   A ASN 200 ? ? 4_555 2.03 
1230 1 CE  A LYS 379 ? ? 1_555 N     A LYS 415 ? ? 4_555 2.03 
1231 1 N   A PRO 305 ? ? 1_555 O     A PHE 345 ? ? 2_656 2.04 
1232 1 CB  A THR 240 ? ? 1_555 OG1   A THR 240 ? ? 2_656 2.04 
1233 1 N   A GLY 235 ? ? 1_555 O     A GLU 246 ? ? 2_656 2.04 
1234 1 CG1 A ILE 39  ? ? 1_555 CB    A LEU 198 ? ? 4_555 2.04 
1235 1 N   A LEU 59  ? ? 1_555 OD1   A ASP 229 ? ? 4_555 2.04 
1236 1 O   A ARG 38  ? ? 1_555 CA    A GLU 199 ? ? 4_555 2.04 
1237 1 O   A VAL 79  ? ? 1_555 CE1   A PHE 205 ? ? 4_555 2.04 
1238 1 CA  A SER 61  ? ? 1_555 CG    A ARG 203 ? ? 4_555 2.04 
1239 1 CA  A ILE 254 ? ? 1_555 C     A GLU 316 ? ? 2_656 2.04 
1240 1 CA  A GLY 30  ? ? 1_555 CA    A HIS 388 ? ? 4_555 2.04 
1241 1 O   A TYR 74  ? ? 1_555 CB    A THR 365 ? ? 4_555 2.04 
1242 1 CB  A SER 290 ? ? 1_555 O     A SER 292 ? ? 2_656 2.04 
1243 1 CA  A GLY 112 ? ? 1_555 N     A VAL 275 ? ? 4_555 2.04 
1244 1 C   A GLY 234 ? ? 1_555 C     A ASN 247 ? ? 2_656 2.04 
1245 1 CG  A PRO 111 ? ? 1_555 CE    A LYS 271 ? ? 4_555 2.05 
1246 1 CD2 A PHE 255 ? ? 1_555 N     A THR 299 ? ? 2_656 2.05 
1247 1 O   A GLU 302 ? ? 1_555 C     A PRO 337 ? ? 2_656 2.05 
1248 1 NZ  A LYS 31  ? ? 1_555 CA    A ILE 368 ? ? 4_555 2.05 
1249 1 CA  A ILE 233 ? ? 1_555 OE1   A GLU 249 ? ? 2_656 2.05 
1250 1 O   A PRO 78  ? ? 1_555 CB    A LEU 332 ? ? 4_555 2.05 
1251 1 CD  A LYS 47  ? ? 1_555 OD1   A ASP 226 ? ? 4_555 2.05 
1252 1 CB  A ASP 287 ? ? 1_555 CD2   A PHE 342 ? ? 2_656 2.05 
1253 1 CB  A LEU 83  ? ? 1_555 CE2   A PHE 205 ? ? 4_555 2.05 
1254 1 CD  A LYS 379 ? ? 1_555 N     A LYS 415 ? ? 4_555 2.05 
1255 1 CB  A GLU 118 ? ? 1_555 NE    A ARG 203 ? ? 4_555 2.05 
1256 1 CB  A VAL 22  ? ? 1_555 CA    A ASN 200 ? ? 4_555 2.05 
1257 1 CG  A LYS 47  ? ? 1_555 OD2   A ASP 226 ? ? 4_555 2.05 
1258 1 N   A LYS 213 ? ? 1_555 C     A ASP 300 ? ? 2_656 2.06 
1259 1 CD  A LYS 32  ? ? 1_555 C     A SER 390 ? ? 4_555 2.06 
1260 1 N   A LYS 31  ? ? 1_555 CG    A HIS 388 ? ? 4_555 2.06 
1261 1 CG  A PRO 27  ? ? 1_555 CB    A LYS 192 ? ? 4_555 2.06 
1262 1 O   A LYS 301 ? ? 1_555 N7    A ATP 417 ? ? 2_656 2.06 
1263 1 CB  A ASP 90  ? ? 1_555 CG2   A VAL 277 ? ? 4_555 2.06 
1264 1 CD  A LYS 379 ? ? 1_555 O     A LYS 414 ? ? 4_555 2.06 
1265 1 CD1 A PHE 289 ? ? 1_555 CA    A ASN 294 ? ? 2_656 2.06 
1266 1 O   A LEU 59  ? ? 1_555 CG    A ASP 229 ? ? 4_555 2.06 
1267 1 CA  A ILE 115 ? ? 1_555 CB    A ASP 229 ? ? 4_555 2.06 
1268 1 CG2 A VAL 57  ? ? 1_555 C     A GLY 274 ? ? 4_555 2.06 
1269 1 OD2 A ASP 90  ? ? 1_555 OE1   A GLU 249 ? ? 3_454 2.06 
1270 1 CB  A ILE 254 ? ? 1_555 O     A GLU 316 ? ? 2_656 2.06 
1271 1 OD2 A ASP 90  ? ? 1_555 CB    A ILE 232 ? ? 4_555 2.06 
1272 1 O   A GLY 88  ? ? 1_555 CD1   A LEU 266 ? ? 4_555 2.06 
1273 1 CG2 A ILE 254 ? ? 1_555 C     A GLU 316 ? ? 2_656 2.06 
1274 1 OG1 A THR 34  ? ? 1_555 CA    A GLU 190 ? ? 4_555 2.06 
1275 1 N   A ASP 23  ? ? 1_555 C     A ASN 200 ? ? 4_555 2.06 
1276 1 N   A TYR 74  ? ? 1_555 CB    A SER 360 ? ? 4_555 2.07 
1277 1 CD1 A ILE 285 ? ? 1_555 CG    A LEU 311 ? ? 2_656 2.07 
1278 1 CD  A LYS 32  ? ? 1_555 CA    A SER 390 ? ? 4_555 2.07 
1279 1 CD  A GLU 118 ? ? 1_555 ND2   A ASN 364 ? ? 4_555 2.07 
1280 1 C   A GLN 84  ? ? 1_555 O     A LEU 224 ? ? 4_555 2.07 
1281 1 C   A MET 237 ? ? 1_555 OG1   A THR 240 ? ? 2_656 2.07 
1282 1 O   A PRO 27  ? ? 1_555 CA    A TYR 193 ? ? 4_555 2.07 
1283 1 CG  A LYS 31  ? ? 1_555 C     A HIS 388 ? ? 4_555 2.07 
1284 1 OD2 A ASP 252 ? ? 1_555 CB    A SER 317 ? ? 2_656 2.07 
1285 1 O   A LYS 73  ? ? 1_555 O     A SER 360 ? ? 4_555 2.07 
1286 1 N   A THR 240 ? ? 1_555 OG1   A THR 240 ? ? 2_656 2.07 
1287 1 CB  A SER 113 ? ? 1_555 CB    A SER 230 ? ? 4_555 2.07 
1288 1 O   A LEU 116 ? ? 1_555 CD    A PRO 204 ? ? 4_555 2.07 
1289 1 CA  A LYS 31  ? ? 1_555 CG2   A ILE 367 ? ? 4_555 2.07 
1290 1 CB  A ALA 80  ? ? 1_555 O     A LEU 206 ? ? 4_555 2.07 
1291 1 CA  A LEU 50  ? ? 1_555 N     A GLY 274 ? ? 4_555 2.07 
1292 1 CE  A LYS 89  ? ? 1_555 O     A MET 267 ? ? 4_555 2.07 
1293 1 CB  A PRO 78  ? ? 1_555 CG2   A ILE 367 ? ? 4_555 2.07 
1294 1 CA  A ALA 286 ? ? 1_555 C     A PHE 289 ? ? 2_656 2.08 
1295 1 O   A VAL 91  ? ? 1_555 CA    A ALA 207 ? ? 4_555 2.08 
1296 1 CA  A ALA 77  ? ? 1_555 CB    A ILE 331 ? ? 4_555 2.08 
1297 1 N   A LEU 50  ? ? 1_555 O     A LYS 273 ? ? 4_555 2.08 
1298 1 O   A ALA 77  ? ? 1_555 O     A ILE 331 ? ? 4_555 2.08 
1299 1 CA  A LYS 89  ? ? 1_555 CD2   A LEU 225 ? ? 4_555 2.08 
1300 1 N   A GLY 236 ? ? 1_555 CB    A ASN 247 ? ? 2_656 2.08 
1301 1 CB  A LYS 379 ? ? 1_555 O     A LYS 414 ? ? 4_555 2.08 
1302 1 CG  A PHE 241 ? ? 1_555 CB    A LEU 279 ? ? 2_656 2.08 
1303 1 CA  A ASN 25  ? ? 1_555 CD    A LYS 196 ? ? 4_555 2.08 
1304 1 CG2 A ILE 33  ? ? 1_555 C     A TYR 193 ? ? 4_555 2.08 
1305 1 O   A GLY 234 ? ? 1_555 CA    A THR 248 ? ? 2_656 2.08 
1306 1 OD2 A ASP 90  ? ? 1_555 OE2   A GLU 249 ? ? 3_454 2.08 
1307 1 CG  A GLU 82  ? ? 1_555 CD2   A LEU 198 ? ? 4_555 2.08 
1308 1 OD2 A ASP 90  ? ? 1_555 CD    A GLU 249 ? ? 3_454 2.08 
1309 1 CD2 A LEU 59  ? ? 1_555 O     A VAL 228 ? ? 4_555 2.08 
1310 1 N   A GLY 235 ? ? 1_555 CA    A THR 248 ? ? 2_656 2.08 
1311 1 C   A GLY 236 ? ? 1_555 CG    A ASN 247 ? ? 2_656 2.08 
1312 1 CG  A ASP 256 ? ? 1_555 CG1   A VAL 298 ? ? 2_656 2.08 
1313 1 CB  A GLU 302 ? ? 1_555 C5    A ATP 417 ? ? 2_656 2.08 
1314 1 CD  A LYS 379 ? ? 1_555 CB    A LYS 415 ? ? 4_555 2.08 
1315 1 CD2 A PHE 255 ? ? 1_555 C     A VAL 281 ? ? 2_656 2.09 
1316 1 C   A GLY 112 ? ? 1_555 CG1   A VAL 275 ? ? 4_555 2.09 
1317 1 CA  A ASP 29  ? ? 1_555 CE    A LYS 189 ? ? 4_555 2.09 
1318 1 CA  A ILE 304 ? ? 1_555 CA    A PHE 340 ? ? 2_656 2.09 
1319 1 CA  A ALA 288 ? ? 1_555 C     A SER 290 ? ? 2_656 2.09 
1320 1 CD2 A PHE 93  ? ? 1_555 C     A THR 329 ? ? 4_555 2.09 
1321 1 CB  A LEU 245 ? ? 1_555 CG2   A VAL 277 ? ? 2_656 2.09 
1322 1 N   A GLY 303 ? ? 1_555 C     A PRO 337 ? ? 2_656 2.09 
1323 1 C   A SER 75  ? ? 1_555 CB    A THR 365 ? ? 4_555 2.09 
1324 1 CB  A LEU 87  ? ? 1_555 N     A ASP 226 ? ? 4_555 2.09 
1325 1 C   A ASN 25  ? ? 1_555 CG    A LYS 196 ? ? 4_555 2.09 
1326 1 CG2 A VAL 26  ? ? 1_555 O     A LYS 192 ? ? 4_555 2.09 
1327 1 CA  A VAL 91  ? ? 1_555 N     A ILE 232 ? ? 4_555 2.09 
1328 1 CD2 A LEU 120 ? ? 1_555 O     A GLY 363 ? ? 4_555 2.09 
1329 1 O   A ALA 212 ? ? 1_555 CA    A ASP 300 ? ? 2_656 2.09 
1330 1 OD1 A ASP 287 ? ? 1_555 CZ    A PHE 342 ? ? 2_656 2.09 
1331 1 CA  A LEU 6   ? ? 1_555 CE    A LYS 378 ? ? 4_545 2.09 
1332 1 CA  A PHE 255 ? ? 1_555 CB    A ASP 282 ? ? 2_656 2.09 
1333 1 CB  A GLU 302 ? ? 1_555 N6    A ATP 417 ? ? 2_656 2.09 
1334 1 CD2 A LEU 245 ? ? 1_555 CA    A VAL 277 ? ? 2_656 2.09 
1335 1 NZ  A LYS 89  ? ? 1_555 N     A ALA 272 ? ? 4_555 2.09 
1336 1 C   A LEU 6   ? ? 1_555 NZ    A LYS 378 ? ? 4_545 2.09 
1337 1 CG  A LEU 117 ? ? 1_555 CG2   A THR 202 ? ? 4_555 2.10 
1338 1 CA  A SER 75  ? ? 1_555 CA    A ASN 364 ? ? 4_555 2.10 
1339 1 C   A LEU 83  ? ? 1_555 CG    A LYS 227 ? ? 4_555 2.10 
1340 1 N   A ASP 90  ? ? 1_555 CG2   A ILE 232 ? ? 4_555 2.10 
1341 1 CD1 A ILE 221 ? ? 1_555 CD    A GLU 246 ? ? 2_656 2.10 
1342 1 O   A LYS 73  ? ? 1_555 CA    A ALA 361 ? ? 4_555 2.10 
1343 1 N   A ALA 286 ? ? 1_555 CB    A PHE 289 ? ? 2_656 2.10 
1344 1 CB  A ILE 33  ? ? 1_555 CG    A PHE 194 ? ? 4_555 2.10 
1345 1 CG  A ASP 90  ? ? 1_555 OE2   A GLU 249 ? ? 3_454 2.10 
1346 1 N   A TYR 74  ? ? 1_555 N     A ALA 361 ? ? 4_555 2.10 
1347 1 N   A GLY 236 ? ? 1_555 C     A ASN 247 ? ? 2_656 2.10 
1348 1 CG2 A ILE 254 ? ? 1_555 C     A PRO 315 ? ? 2_656 2.10 
1349 1 CE2 A PHE 239 ? ? 1_555 CG    A ASN 247 ? ? 2_656 2.10 
1350 1 O   A VAL 91  ? ? 1_555 CB    A ALA 207 ? ? 4_555 2.10 
1351 1 O   A GLY 112 ? ? 1_555 O     A GLY 274 ? ? 4_555 2.10 
1352 1 N   A PHE 24  ? ? 1_555 CD    A PRO 201 ? ? 4_555 2.10 
1353 1 CG  A LEU 50  ? ? 1_555 CA    A LYS 273 ? ? 4_555 2.11 
1354 1 OD1 A ASP 252 ? ? 1_555 ND2   A ASN 313 ? ? 2_656 2.11 
1355 1 O   A GLN 309 ? ? 1_555 CB    A LEU 311 ? ? 2_656 2.11 
1356 1 N   A VAL 26  ? ? 1_555 CG    A LYS 196 ? ? 4_555 2.11 
1357 1 C   A GLY 30  ? ? 1_555 O     A SER 387 ? ? 4_555 2.11 
1358 1 N   A ALA 80  ? ? 1_555 CZ    A PHE 205 ? ? 4_555 2.11 
1359 1 CA  A LEU 59  ? ? 1_555 OD1   A ASP 229 ? ? 4_555 2.11 
1360 1 CZ  A PHE 255 ? ? 1_555 C     A VAL 298 ? ? 2_656 2.11 
1361 1 CB  A LEU 83  ? ? 1_555 CG    A LYS 227 ? ? 4_555 2.11 
1362 1 CG  A LEU 63  ? ? 1_555 CE    A LYS 196 ? ? 4_555 2.11 
1363 1 N   A ASP 29  ? ? 1_555 CG    A LYS 189 ? ? 4_555 2.11 
1364 1 O   A LEU 87  ? ? 1_555 CA    A LEU 225 ? ? 4_555 2.11 
1365 1 C   A ALA 288 ? ? 1_555 O     A SER 290 ? ? 2_656 2.11 
1366 1 N   A MET 237 ? ? 1_555 ND2   A ASN 247 ? ? 2_656 2.11 
1367 1 OE1 A GLU 118 ? ? 1_555 CG    A ASN 364 ? ? 4_555 2.11 
1368 1 CB  A SER 61  ? ? 1_555 CA    A ARG 203 ? ? 4_555 2.11 
1369 1 CD1 A ILE 304 ? ? 1_555 CA    A PHE 340 ? ? 2_656 2.11 
1370 1 OE1 A GLN 84  ? ? 1_555 CG    A LEU 209 ? ? 4_555 2.11 
1371 1 CA  A ALA 288 ? ? 1_555 CE1   A PHE 345 ? ? 2_656 2.11 
1372 1 CD  A LYS 301 ? ? 1_555 "O4'" A ATP 417 ? ? 2_656 2.11 
1373 1 CA  A GLY 88  ? ? 1_555 CB    A LEU 225 ? ? 4_555 2.11 
1374 1 CB  A PRO 78  ? ? 1_555 C     A ILE 367 ? ? 4_555 2.11 
1375 1 O   A LEU 209 ? ? 1_555 CG2   A ILE 250 ? ? 2_656 2.11 
1376 1 CB  A ILE 33  ? ? 1_555 C     A PHE 194 ? ? 4_555 2.11 
1377 1 CG  A PRO 305 ? ? 1_555 C     A VAL 339 ? ? 2_656 2.12 
1378 1 O   A ILE 232 ? ? 1_555 CD1   A LEU 245 ? ? 2_656 2.12 
1379 1 CA  A ALA 288 ? ? 1_555 CA    A ALA 291 ? ? 2_656 2.12 
1380 1 CA  A ASP 23  ? ? 1_555 CA    A ASN 200 ? ? 4_555 2.12 
1381 1 CD  A LYS 32  ? ? 1_555 CB    A SER 390 ? ? 4_555 2.12 
1382 1 CG  A LEU 76  ? ? 1_555 CG1   A VAL 330 ? ? 4_555 2.12 
1383 1 N   A ILE 115 ? ? 1_555 CB    A PRO 204 ? ? 4_555 2.12 
1384 1 CB  A ALA 77  ? ? 1_555 C     A ILE 331 ? ? 4_555 2.12 
1385 1 O   A ALA 60  ? ? 1_555 CA    A THR 202 ? ? 4_555 2.12 
1386 1 CD1 A LEU 59  ? ? 1_555 CA    A VAL 228 ? ? 4_555 2.12 
1387 1 CG2 A ILE 304 ? ? 1_555 CB    A ALA 346 ? ? 2_656 2.12 
1388 1 CG2 A ILE 233 ? ? 1_555 CG    A GLU 249 ? ? 2_656 2.12 
1389 1 C   A PHE 283 ? ? 1_555 CE2   A TRP 308 ? ? 2_656 2.12 
1390 1 N   A GLU 51  ? ? 1_555 CA    A LYS 273 ? ? 4_555 2.12 
1391 1 CG  A LEU 116 ? ? 1_555 CG    A PRO 204 ? ? 4_555 2.12 
1392 1 N   A THR 240 ? ? 1_555 N     A THR 240 ? ? 2_656 2.12 
1393 1 CA  A ILE 39  ? ? 1_555 CB    A LEU 198 ? ? 4_555 2.13 
1394 1 O   A TYR 56  ? ? 1_555 CB    A VAL 275 ? ? 4_555 2.13 
1395 1 CD1 A LEU 63  ? ? 1_555 NH1   A ARG 203 ? ? 4_555 2.13 
1396 1 OD1 A ASP 29  ? ? 1_555 CB    A LYS 189 ? ? 4_555 2.13 
1397 1 C   A LYS 378 ? ? 1_555 OG    A SER 412 ? ? 4_555 2.13 
1398 1 C   A ALA 306 ? ? 1_555 O     A ASP 312 ? ? 2_656 2.13 
1399 1 N   A SER 75  ? ? 1_555 O     A SER 360 ? ? 4_555 2.13 
1400 1 CB  A GLU 118 ? ? 1_555 CD    A ARG 203 ? ? 4_555 2.13 
1401 1 N   A PHE 255 ? ? 1_555 C     A ASP 282 ? ? 2_656 2.13 
1402 1 CA  A GLN 84  ? ? 1_555 CD1   A LEU 224 ? ? 4_555 2.13 
1403 1 CG  A GLU 118 ? ? 1_555 ND2   A ASN 364 ? ? 4_555 2.13 
1404 1 CD2 A LEU 83  ? ? 1_555 CD2   A PHE 205 ? ? 4_555 2.13 
1405 1 O   A ARG 21  ? ? 1_555 ND2   A ASN 200 ? ? 4_555 2.13 
1406 1 CG  A LYS 73  ? ? 1_555 CA    A SER 359 ? ? 4_555 2.13 
1407 1 N   A PRO 305 ? ? 1_555 CG1   A VAL 339 ? ? 2_656 2.13 
1408 1 O   A ASP 29  ? ? 1_555 CB    A HIS 388 ? ? 4_555 2.13 
1409 1 CA  A ALA 212 ? ? 1_555 N     A LYS 301 ? ? 2_656 2.13 
1410 1 CA  A GLY 112 ? ? 1_555 O     A VAL 275 ? ? 4_555 2.13 
1411 1 C   A LYS 301 ? ? 1_555 N7    A ATP 417 ? ? 2_656 2.13 
1412 1 N   A LEU 50  ? ? 1_555 C     A LYS 273 ? ? 4_555 2.13 
1413 1 CG  A LYS 379 ? ? 1_555 O     A LYS 414 ? ? 4_555 2.13 
1414 1 CB  A ILE 46  ? ? 1_555 O     A LYS 227 ? ? 4_555 2.14 
1415 1 O   A LEU 76  ? ? 1_555 CA    A VAL 330 ? ? 4_555 2.14 
1416 1 N   A LEU 63  ? ? 1_555 NH1   A ARG 203 ? ? 4_555 2.14 
1417 1 CZ  A PHE 241 ? ? 1_555 CD    A PRO 280 ? ? 2_656 2.14 
1418 1 O   A ILE 250 ? ? 1_555 C     A PRO 337 ? ? 2_656 2.14 
1419 1 N   A GLY 211 ? ? 1_555 CA    A GLY 251 ? ? 2_656 2.14 
1420 1 N   A GLY 235 ? ? 1_555 N     A GLU 249 ? ? 2_656 2.14 
1421 1 C   A PHE 241 ? ? 1_555 CG    A LEU 279 ? ? 2_656 2.14 
1422 1 OD2 A ASP 12  ? ? 1_555 CE1   A PHE 342 ? ? 4_545 2.14 
1423 1 CD1 A PHE 255 ? ? 1_555 N     A THR 299 ? ? 2_656 2.14 
1424 1 CG2 A THR 297 ? ? 1_555 CH2   A TRP 308 ? ? 2_656 2.14 
1425 1 CD1 A PHE 24  ? ? 1_555 C     A ALA 197 ? ? 4_555 2.14 
1426 1 CA  A GLY 88  ? ? 1_555 CG    A LEU 225 ? ? 4_555 2.14 
1427 1 C   A SER 75  ? ? 1_555 C     A ASN 364 ? ? 4_555 2.14 
1428 1 OD2 A ASP 23  ? ? 1_555 OE2   A GLU 199 ? ? 4_555 2.14 
1429 1 CG  A LEU 87  ? ? 1_555 C     A ASP 226 ? ? 4_555 2.14 
1430 1 OD2 A ASP 90  ? ? 1_555 CD1   A ILE 232 ? ? 4_555 2.14 
1431 1 CG  A LYS 73  ? ? 1_555 C     A LYS 358 ? ? 4_555 2.14 
1432 1 O   A GLU 302 ? ? 1_555 CA    A GLY 338 ? ? 2_656 2.14 
1433 1 CD1 A LEU 76  ? ? 1_555 O     A PRO 204 ? ? 4_555 2.14 
1434 1 CA  A GLY 307 ? ? 1_555 N     A GLY 314 ? ? 2_656 2.15 
1435 1 CA  A PHE 283 ? ? 1_555 NE1   A TRP 308 ? ? 2_656 2.15 
1436 1 O   A GLY 112 ? ? 1_555 OG    A SER 230 ? ? 4_555 2.15 
1437 1 CB  A LYS 73  ? ? 1_555 C     A SER 360 ? ? 4_555 2.15 
1438 1 O   A LEU 83  ? ? 1_555 CG    A LYS 227 ? ? 4_555 2.15 
1439 1 CA  A LYS 379 ? ? 1_555 CB    A LYS 415 ? ? 4_555 2.15 
1440 1 O   A VAL 49  ? ? 1_555 C     A ALA 272 ? ? 4_555 2.15 
1441 1 C   A GLY 211 ? ? 1_555 N     A GLU 302 ? ? 2_656 2.15 
1442 1 CB  A ASP 256 ? ? 1_555 CA    A VAL 298 ? ? 2_656 2.15 
1443 1 O   A ILE 115 ? ? 1_555 C     A PRO 204 ? ? 4_555 2.15 
1444 1 CB  A LYS 73  ? ? 1_555 C     A SER 359 ? ? 4_555 2.15 
1445 1 N   A GLN 84  ? ? 1_555 CG    A LEU 224 ? ? 4_555 2.15 
1446 1 O   A THR 34  ? ? 1_555 N     A LEU 191 ? ? 4_555 2.15 
1447 1 N   A ILE 39  ? ? 1_555 C     A LEU 198 ? ? 4_555 2.15 
1448 1 O   A LYS 32  ? ? 1_555 CE1   A HIS 388 ? ? 4_555 2.15 
1449 1 O   A LEU 50  ? ? 1_555 C     A LYS 271 ? ? 4_555 2.15 
1450 1 CE  A LYS 32  ? ? 1_555 CA    A SER 390 ? ? 4_555 2.15 
1451 1 CD  A LYS 73  ? ? 1_555 N     A SER 360 ? ? 4_555 2.16 
1452 1 C   A LEU 245 ? ? 1_555 CG1   A VAL 277 ? ? 2_656 2.16 
1453 1 N   A SER 290 ? ? 1_555 O     A ALA 293 ? ? 2_656 2.16 
1454 1 CB  A ALA 77  ? ? 1_555 CB    A ILE 331 ? ? 4_555 2.16 
1455 1 CG1 A ILE 254 ? ? 1_555 N     A GLU 316 ? ? 2_656 2.16 
1456 1 CA  A ILE 33  ? ? 1_555 CG    A PHE 194 ? ? 4_555 2.16 
1457 1 N   A ASP 23  ? ? 1_555 CG    A ASN 200 ? ? 4_555 2.16 
1458 1 CE  A LYS 47  ? ? 1_555 OD1   A ASP 226 ? ? 4_555 2.16 
1459 1 CB  A ILE 115 ? ? 1_555 OD2   A ASP 229 ? ? 4_555 2.16 
1460 1 N   A GLY 234 ? ? 1_555 N     A GLU 249 ? ? 2_656 2.16 
1461 1 CB  A SER 61  ? ? 1_555 N     A ARG 203 ? ? 4_555 2.16 
1462 1 CD1 A ILE 33  ? ? 1_555 CD1   A PHE 194 ? ? 4_555 2.16 
1463 1 CG2 A VAL 26  ? ? 1_555 C     A TYR 193 ? ? 4_555 2.16 
1464 1 OD2 A ASP 29  ? ? 1_555 CB    A LYS 189 ? ? 4_555 2.16 
1465 1 CD2 A PHE 24  ? ? 1_555 CG    A PRO 201 ? ? 4_555 2.16 
1466 1 C   A ARG 38  ? ? 1_555 CA    A GLU 199 ? ? 4_555 2.16 
1467 1 CB  A GLU 51  ? ? 1_555 CB    A ALA 272 ? ? 4_555 2.16 
1468 1 N   A ASP 256 ? ? 1_555 CA    A ASP 282 ? ? 2_656 2.16 
1469 1 N   A LEU 76  ? ? 1_555 C     A THR 365 ? ? 4_555 2.16 
1470 1 CB  A PHE 255 ? ? 1_555 N     A VAL 281 ? ? 2_656 2.16 
1471 1 OE2 A GLU 82  ? ? 1_555 O     A LEU 400 ? ? 4_555 2.17 
1472 1 CD1 A PHE 24  ? ? 1_555 O     A ALA 197 ? ? 4_555 2.17 
1473 1 O   A SER 113 ? ? 1_555 C     A ASP 229 ? ? 4_555 2.17 
1474 1 CG2 A VAL 259 ? ? 1_555 OG1   A THR 299 ? ? 2_656 2.17 
1475 1 CB  A LEU 94  ? ? 1_555 CG    A LYS 327 ? ? 4_555 2.17 
1476 1 CB  A PHE 241 ? ? 1_555 CA    A LEU 279 ? ? 2_656 2.17 
1477 1 C   A ASP 287 ? ? 1_555 O     A PHE 289 ? ? 2_656 2.17 
1478 1 CA  A GLY 30  ? ? 1_555 N     A VAL 389 ? ? 4_555 2.17 
1479 1 CD1 A PHE 93  ? ? 1_555 CD1   A ILE 331 ? ? 4_555 2.17 
1480 1 CB  A PHE 255 ? ? 1_555 CA    A ASP 282 ? ? 2_656 2.17 
1481 1 CB  A ILE 39  ? ? 1_555 CG    A LEU 198 ? ? 4_555 2.17 
1482 1 CA  A GLU 51  ? ? 1_555 C     A ALA 272 ? ? 4_555 2.17 
1483 1 CA  A ILE 304 ? ? 1_555 N     A PHE 340 ? ? 2_656 2.17 
1484 1 CD2 A LEU 63  ? ? 1_555 CD    A LYS 196 ? ? 4_555 2.17 
1485 1 N   A HIS 52  ? ? 1_555 CB    A ALA 272 ? ? 4_555 2.17 
1486 1 CA  A ILE 233 ? ? 1_555 OE2   A GLU 249 ? ? 2_656 2.18 
1487 1 CB  A ILE 115 ? ? 1_555 CG    A ASP 229 ? ? 4_555 2.18 
1488 1 CG  A ARG 38  ? ? 1_555 CG    A GLU 199 ? ? 4_555 2.18 
1489 1 C   A GLY 210 ? ? 1_555 N     A GLY 251 ? ? 2_656 2.18 
1490 1 C   A TYR 74  ? ? 1_555 N     A THR 365 ? ? 4_555 2.18 
1491 1 CB  A PRO 78  ? ? 1_555 O     A ILE 367 ? ? 4_555 2.18 
1492 1 C   A LEU 86  ? ? 1_555 O     A ASP 222 ? ? 4_555 2.18 
1493 1 CG2 A ILE 39  ? ? 1_555 CG    A LEU 198 ? ? 4_555 2.18 
1494 1 CB  A PHE 283 ? ? 1_555 CA    A TRP 308 ? ? 2_656 2.18 
1495 1 N   A PRO 78  ? ? 1_555 N     A ILE 367 ? ? 4_555 2.18 
1496 1 CG  A LYS 32  ? ? 1_555 C     A SER 390 ? ? 4_555 2.18 
1497 1 O   A GLY 236 ? ? 1_555 OG1   A THR 240 ? ? 2_656 2.18 
1498 1 CD1 A ILE 254 ? ? 1_555 OE2   A GLU 316 ? ? 2_656 2.18 
1499 1 CD  A PRO 27  ? ? 1_555 C     A LEU 191 ? ? 4_555 2.18 
1500 1 N   A LEU 87  ? ? 1_555 N     A LEU 225 ? ? 4_555 2.18 
1501 1 CG  A ASP 29  ? ? 1_555 CG    A LYS 189 ? ? 4_555 2.18 
1502 1 CE1 A PHE 255 ? ? 1_555 O     A THR 299 ? ? 2_656 2.18 
1503 1 CG  A PHE 93  ? ? 1_555 CD2   A LEU 206 ? ? 4_555 2.19 
1504 1 CB  A LYS 31  ? ? 1_555 C     A ILE 367 ? ? 4_555 2.19 
1505 1 C   A ASP 287 ? ? 1_555 C     A SER 290 ? ? 2_656 2.19 
1506 1 O   A SER 3   ? ? 1_555 CB    A SER 35  ? ? 4_545 2.19 
1507 1 CB  A ILE 254 ? ? 1_555 N     A GLU 316 ? ? 2_656 2.19 
1508 1 N   A ASP 256 ? ? 1_555 C     A VAL 281 ? ? 2_656 2.19 
1509 1 CD1 A LEU 76  ? ? 1_555 CG1   A VAL 330 ? ? 4_555 2.19 
1510 1 CA  A LEU 86  ? ? 1_555 CA    A ASN 223 ? ? 4_555 2.19 
1511 1 NZ  A LYS 213 ? ? 1_555 CE    A LYS 301 ? ? 2_656 2.19 
1512 1 CD  A PRO 78  ? ? 1_555 O     A ILE 331 ? ? 4_555 2.19 
1513 1 CA  A PHE 93  ? ? 1_555 CD1   A LEU 206 ? ? 4_555 2.19 
1514 1 CA  A ASP 23  ? ? 1_555 CB    A ASN 200 ? ? 4_555 2.19 
1515 1 CA  A LEU 245 ? ? 1_555 CD2   A LEU 279 ? ? 2_656 2.19 
1516 1 N   A ALA 238 ? ? 1_555 CZ    A PHE 283 ? ? 2_656 2.19 
1517 1 CG  A LEU 245 ? ? 1_555 N     A VAL 278 ? ? 2_656 2.19 
1518 1 CG  A LYS 32  ? ? 1_555 CB    A SER 390 ? ? 4_555 2.19 
1519 1 O   A ALA 77  ? ? 1_555 CB    A LEU 332 ? ? 4_555 2.19 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            C 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            LYS 
_pdbx_validate_rmsd_bond.auth_seq_id_1             415 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            OXT 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            LYS 
_pdbx_validate_rmsd_bond.auth_seq_id_2             415 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.348 
_pdbx_validate_rmsd_bond.bond_target_value         1.229 
_pdbx_validate_rmsd_bond.bond_deviation            0.119 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.019 
_pdbx_validate_rmsd_bond.linker_flag               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 17  ? ? CZ A ARG 17  ? ? NH2 A ARG 17  ? ? 124.02 120.30 3.72   0.50 N 
2  1 NE A ARG 21  ? ? CZ A ARG 21  ? ? NH2 A ARG 21  ? ? 124.01 120.30 3.71   0.50 N 
3  1 NE A ARG 38  ? ? CZ A ARG 38  ? ? NH2 A ARG 38  ? ? 123.98 120.30 3.68   0.50 N 
4  1 NE A ARG 55  ? ? CZ A ARG 55  ? ? NH2 A ARG 55  ? ? 123.92 120.30 3.62   0.50 N 
5  1 NE A ARG 65  ? ? CZ A ARG 65  ? ? NH2 A ARG 65  ? ? 123.99 120.30 3.69   0.50 N 
6  1 NE A ARG 70  ? ? CZ A ARG 70  ? ? NH2 A ARG 70  ? ? 123.99 120.30 3.69   0.50 N 
7  1 NE A ARG 121 ? ? CZ A ARG 121 ? ? NH2 A ARG 121 ? ? 123.99 120.30 3.69   0.50 N 
8  1 NE A ARG 130 ? ? CZ A ARG 130 ? ? NH2 A ARG 130 ? ? 123.98 120.30 3.68   0.50 N 
9  1 NE A ARG 148 ? ? CZ A ARG 148 ? ? NH2 A ARG 148 ? ? 123.97 120.30 3.67   0.50 N 
10 1 NE A ARG 168 ? ? CZ A ARG 168 ? ? NH2 A ARG 168 ? ? 124.07 120.30 3.77   0.50 N 
11 1 CG A MET 173 ? ? SD A MET 173 ? ? CE  A MET 173 ? ? 110.04 100.20 9.84   1.60 N 
12 1 NE A ARG 181 ? ? CZ A ARG 181 ? ? NH2 A ARG 181 ? ? 124.00 120.30 3.70   0.50 N 
13 1 NE A ARG 203 ? ? CZ A ARG 203 ? ? NH2 A ARG 203 ? ? 124.03 120.30 3.73   0.50 N 
14 1 C  A ALA 215 ? ? N  A ASP 216 ? ? CA  A ASP 216 ? ? 104.24 121.70 -17.46 2.50 Y 
15 1 O  A ILE 233 ? ? C  A ILE 233 ? ? N   A GLY 234 ? ? 133.72 123.20 10.52  1.70 Y 
16 1 CG A MET 237 ? ? SD A MET 237 ? ? CE  A MET 237 ? ? 109.95 100.20 9.75   1.60 N 
17 1 CG A MET 267 ? ? SD A MET 267 ? ? CE  A MET 267 ? ? 110.02 100.20 9.82   1.60 N 
18 1 NE A ARG 318 ? ? CZ A ARG 318 ? ? NH2 A ARG 318 ? ? 124.02 120.30 3.72   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 LEU A 2   ? ? 140.11  -109.07 
2   1 SER A 3   ? ? 33.59   58.58   
3   1 SER A 4   ? ? -59.96  -93.02  
4   1 LEU A 6   ? ? -55.60  -107.30 
5   1 GLN A 9   ? ? 44.53   24.39   
6   1 LEU A 13  ? ? 56.27   -131.71 
7   1 LYS A 14  ? ? 82.70   96.76   
8   1 PHE A 24  ? ? -119.73 78.12   
9   1 PRO A 27  ? ? -56.17  -172.96 
10  1 LYS A 31  ? ? -144.35 -35.06  
11  1 LYS A 32  ? ? -38.47  92.15   
12  1 SER A 35  ? ? 113.38  122.06  
13  1 HIS A 52  ? ? -22.86  -46.30  
14  1 HIS A 53  ? ? 114.37  40.77   
15  1 PRO A 54  ? ? -62.22  -72.44  
16  1 ARG A 55  ? ? 145.69  -29.98  
17  1 TYR A 56  ? ? -90.34  -149.04 
18  1 VAL A 57  ? ? 122.13  82.39   
19  1 HIS A 62  ? ? 138.83  90.10   
20  1 LEU A 63  ? ? -177.90 103.45  
21  1 PRO A 66  ? ? -55.56  83.49   
22  1 ASN A 67  ? ? -69.97  -106.77 
23  1 GLU A 69  ? ? 146.02  -42.97  
24  1 ARG A 70  ? ? 146.14  -134.71 
25  1 GLU A 72  ? ? 15.28   134.13  
26  1 LYS A 73  ? ? -54.90  -128.49 
27  1 SER A 75  ? ? -70.35  -125.59 
28  1 LEU A 76  ? ? -147.86 32.99   
29  1 ASP A 90  ? ? 104.27  120.11  
30  1 LEU A 94  ? ? -114.10 -114.40 
31  1 CYS A 97  ? ? -130.20 -98.96  
32  1 VAL A 98  ? ? -116.12 -130.66 
33  1 ALA A 108 ? ? -42.27  -87.38  
34  1 ALA A 110 ? ? -35.22  -135.42 
35  1 LEU A 117 ? ? 119.99  -103.00 
36  1 GLU A 118 ? ? 90.26   -115.42 
37  1 ASN A 119 ? ? -156.44 52.27   
38  1 TYR A 122 ? ? -25.24  77.84   
39  1 HIS A 123 ? ? -159.11 -17.96  
40  1 GLU A 125 ? ? -117.86 -112.11 
41  1 GLU A 126 ? ? 160.11  88.44   
42  1 GLU A 127 ? ? -24.40  146.18  
43  1 SER A 129 ? ? -57.55  -136.26 
44  1 ARG A 130 ? ? 31.67   109.44  
45  1 LYS A 131 ? ? -37.19  -114.19 
46  1 VAL A 132 ? ? -26.00  143.88  
47  1 ASP A 133 ? ? 79.45   119.87  
48  1 LYS A 136 ? ? 73.01   -176.09 
49  1 LYS A 138 ? ? -56.04  -130.89 
50  1 ALA A 139 ? ? 45.69   174.14  
51  1 SER A 140 ? ? 129.16  134.39  
52  1 LYS A 141 ? ? -122.31 -105.25 
53  1 SER A 153 ? ? -3.52   -50.94  
54  1 ASP A 156 ? ? -140.10 -57.69  
55  1 ASP A 161 ? ? -150.24 53.57   
56  1 PHE A 163 ? ? -90.39  52.98   
57  1 ALA A 166 ? ? -154.09 24.06   
58  1 HIS A 167 ? ? 169.44  90.62   
59  1 ARG A 168 ? ? 125.34  -118.47 
60  1 ALA A 169 ? ? -172.40 -72.72  
61  1 HIS A 170 ? ? 41.60   156.41  
62  1 SER A 172 ? ? 85.42   -12.54  
63  1 VAL A 174 ? ? -119.36 -105.49 
64  1 PHE A 176 ? ? -29.22  52.97   
65  1 ASP A 177 ? ? -54.88  170.72  
66  1 LEU A 178 ? ? 93.74   136.77  
67  1 PRO A 179 ? ? -61.17  -147.00 
68  1 GLN A 180 ? ? 60.01   93.82   
69  1 GLU A 199 ? ? -64.11  -123.96 
70  1 THR A 202 ? ? -59.88  -70.90  
71  1 ARG A 203 ? ? -25.87  125.30  
72  1 PRO A 204 ? ? -58.98  174.58  
73  1 ALA A 212 ? ? -82.57  -122.21 
74  1 LYS A 213 ? ? 28.07   130.09  
75  1 VAL A 214 ? ? -107.13 -165.75 
76  1 ALA A 215 ? ? 150.40  151.05  
77  1 ASP A 216 ? ? 4.01    3.40    
78  1 LYS A 227 ? ? 179.69  -136.21 
79  1 VAL A 228 ? ? -118.21 -92.12  
80  1 SER A 230 ? ? -67.01  36.61   
81  1 VAL A 244 ? ? -123.50 -105.97 
82  1 LEU A 245 ? ? 177.08  -57.65  
83  1 ASP A 252 ? ? -178.45 -118.71 
84  1 SER A 253 ? ? -153.64 -52.16  
85  1 PHE A 255 ? ? -106.65 -115.09 
86  1 VAL A 275 ? ? 178.82  -66.10  
87  1 PRO A 280 ? ? -61.05  -111.64 
88  1 VAL A 281 ? ? 109.78  -27.69  
89  1 ASP A 287 ? ? -8.24   -91.34  
90  1 SER A 290 ? ? -51.14  -147.56 
91  1 SER A 292 ? ? 176.97  152.30  
92  1 ALA A 293 ? ? 42.88   103.65  
93  1 THR A 299 ? ? 68.26   -126.30 
94  1 ASP A 300 ? ? -39.71  132.76  
95  1 LYS A 301 ? ? 114.80  104.72  
96  1 ILE A 304 ? ? -28.29  -85.19  
97  1 PRO A 305 ? ? -58.94  74.52   
98  1 ALA A 306 ? ? 157.42  -148.08 
99  1 TRP A 308 ? ? 164.99  -41.67  
100 1 GLN A 309 ? ? 139.35  -135.04 
101 1 LEU A 311 ? ? 132.14  -100.26 
102 1 LYS A 327 ? ? 150.57  88.61   
103 1 ALA A 328 ? ? 8.69    -114.07 
104 1 THR A 329 ? ? 40.86   152.85  
105 1 ASN A 334 ? ? -91.89  -96.82  
106 1 GLU A 343 ? ? -27.56  132.66  
107 1 LYS A 344 ? ? 109.09  -43.12  
108 1 ALA A 346 ? ? -167.37 68.29   
109 1 ALA A 347 ? ? -132.35 -60.49  
110 1 SER A 360 ? ? 3.63    -70.26  
111 1 ALA A 361 ? ? -58.54  -90.52  
112 1 ALA A 362 ? ? -42.42  178.53  
113 1 THR A 365 ? ? -29.02  139.90  
114 1 THR A 383 ? ? 20.91   93.17   
115 1 ASP A 384 ? ? 87.71   -20.81  
116 1 LYS A 385 ? ? 44.68   -41.23  
117 1 ILE A 386 ? ? 30.83   70.97   
118 1 SER A 387 ? ? 156.21  -130.53 
119 1 SER A 390 ? ? -87.90  31.34   
120 1 THR A 391 ? ? -0.83   171.50  
121 1 LYS A 403 ? ? -48.02  173.90  
122 1 LEU A 405 ? ? 71.00   106.55  
123 1 SER A 412 ? ? -132.30 -58.63  
124 1 GLU A 413 ? ? 161.85  41.60   
125 1 LYS A 414 ? ? 64.07   128.71  
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'MAGNESIUM ION'             MG  
3 "ADENOSINE-5'-TRIPHOSPHATE" ATP 
4 '3-PHOSPHOGLYCERIC ACID'    3PG 
# 



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.