CNRS Nantes University US2B US2B
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***    ***

elNémo ID: 2405271640083658787

Job options:

ID        	=	 2405271640083658787
JOBID     	=	 
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:


data_4X90
# 
_entry.id   4X90 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.329 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   4X90         
WWPDB D_1000205001 
# 
loop_
_pdbx_database_related.content_type 
_pdbx_database_related.db_id 
_pdbx_database_related.db_name 
_pdbx_database_related.details 
unspecified 4X91 PDB . 
unspecified 4X92 PDB . 
unspecified 4X93 PDB . 
unspecified 4X94 PDB . 
unspecified 4X95 PDB . 
unspecified 4X96 PDB . 
unspecified 4X97 PDB . 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        4X90 
_pdbx_database_status.recvd_initial_deposition_date   2014-12-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Glukhova, A.'   1 
'Tesmer, J.J.G.' 2 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            6 
_citation.language                  ? 
_citation.page_first                6250 
_citation.page_last                 6250 
_citation.title                     
'Structure and function of lysosomal phospholipase A2 and lecithin:cholesterol acyltransferase.' 
_citation.year                      2015 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/ncomms7250 
_citation.pdbx_database_id_PubMed   25727495 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Glukhova, A.'           1 ? 
primary 'Hinkovska-Galcheva, V.' 2 ? 
primary 'Kelly, R.'              3 ? 
primary 'Abe, A.'                4 ? 
primary 'Shayman, J.A.'          5 ? 
primary 'Tesmer, J.J.'           6 ? 
# 
_cell.angle_alpha                  78.130 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   88.460 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  88.500 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     4X90 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.806 
_cell.length_a_esd                 ? 
_cell.length_b                     91.151 
_cell.length_b_esd                 ? 
_cell.length_c                     100.266 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         4X90 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
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 'Group XV phospholipase A2'                           43121.027 4    2.3.1.- ? 'UNP residues 34-412' ? 
2 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose              221.208   16   ?       ? ?                     ? 
3 non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' 238.305   4    ?       ? ?                     ? 
4 non-polymer syn 'CHLORIDE ION'                                        35.453    4    ?       ? ?                     ? 
5 non-polymer syn 'PHOSPHATE ION'                                       94.971    4    ?       ? ?                     ? 
6 non-polymer syn '(4S)-2-METHYL-2,4-PENTANEDIOL'                       118.174   14   ?       ? ?                     ? 
7 water       nat water                                                 18.015    1065 ?       ? ?                     ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'1-O-acylceramide synthase,ACS,LCAT-like lysophospholipase,LLPL,Lysophospholipase 3,Lysosomal phospholipase A2,LPLA2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GAGRHPPVVLVPGDLGNQLEAKLDKPTVVHYLCSKKTESYFTIWLNLELLLPVIIDCWIDNIRLVYNKTSRATQFPDGVD
VRVPGFGKTFSLEFLDPSKSSVGSYFHTMVESLVGWGYTRGEDVRGAPYDWRRAPNENGPYFLALREMIEEMYQLYGGPV
VLVAHSMGNMYTLYFLQRQPQAWKDKYIRAFVSLGAPWGGVAKTLRVLASGDNNRIPVIGPLKIREQQRSAVSTSWLLPY
NYTWSPEKVFVQTPTINYTLRDYRKFFQDIGFEDGWLMRQDTEGLVEATMPPGVQLHCLYGTGVPTPDSFYYESFPDRDP
KICFGDGDGTVNLKSALQCQAWQSRQEHQVLLQELPGSEHIEMLANATTLAYLKRVLLGP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GAGRHPPVVLVPGDLGNQLEAKLDKPTVVHYLCSKKTESYFTIWLNLELLLPVIIDCWIDNIRLVYNKTSRATQFPDGVD
VRVPGFGKTFSLEFLDPSKSSVGSYFHTMVESLVGWGYTRGEDVRGAPYDWRRAPNENGPYFLALREMIEEMYQLYGGPV
VLVAHSMGNMYTLYFLQRQPQAWKDKYIRAFVSLGAPWGGVAKTLRVLASGDNNRIPVIGPLKIREQQRSAVSTSWLLPY
NYTWSPEKVFVQTPTINYTLRDYRKFFQDIGFEDGWLMRQDTEGLVEATMPPGVQLHCLYGTGVPTPDSFYYESFPDRDP
KICFGDGDGTVNLKSALQCQAWQSRQEHQVLLQELPGSEHIEMLANATTLAYLKRVLLGP
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_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   GLY n 
1 2   ALA n 
1 3   GLY n 
1 4   ARG n 
1 5   HIS n 
1 6   PRO n 
1 7   PRO n 
1 8   VAL n 
1 9   VAL n 
1 10  LEU n 
1 11  VAL n 
1 12  PRO n 
1 13  GLY n 
1 14  ASP n 
1 15  LEU n 
1 16  GLY n 
1 17  ASN n 
1 18  GLN n 
1 19  LEU n 
1 20  GLU n 
1 21  ALA n 
1 22  LYS n 
1 23  LEU n 
1 24  ASP n 
1 25  LYS n 
1 26  PRO n 
1 27  THR n 
1 28  VAL n 
1 29  VAL n 
1 30  HIS n 
1 31  TYR n 
1 32  LEU n 
1 33  CYS n 
1 34  SER n 
1 35  LYS n 
1 36  LYS n 
1 37  THR n 
1 38  GLU n 
1 39  SER n 
1 40  TYR n 
1 41  PHE n 
1 42  THR n 
1 43  ILE n 
1 44  TRP n 
1 45  LEU n 
1 46  ASN n 
1 47  LEU n 
1 48  GLU n 
1 49  LEU n 
1 50  LEU n 
1 51  LEU n 
1 52  PRO n 
1 53  VAL n 
1 54  ILE n 
1 55  ILE n 
1 56  ASP n 
1 57  CYS n 
1 58  TRP n 
1 59  ILE n 
1 60  ASP n 
1 61  ASN n 
1 62  ILE n 
1 63  ARG n 
1 64  LEU n 
1 65  VAL n 
1 66  TYR n 
1 67  ASN n 
1 68  LYS n 
1 69  THR n 
1 70  SER n 
1 71  ARG n 
1 72  ALA n 
1 73  THR n 
1 74  GLN n 
1 75  PHE n 
1 76  PRO n 
1 77  ASP n 
1 78  GLY n 
1 79  VAL n 
1 80  ASP n 
1 81  VAL n 
1 82  ARG n 
1 83  VAL n 
1 84  PRO n 
1 85  GLY n 
1 86  PHE n 
1 87  GLY n 
1 88  LYS n 
1 89  THR n 
1 90  PHE n 
1 91  SER n 
1 92  LEU n 
1 93  GLU n 
1 94  PHE n 
1 95  LEU n 
1 96  ASP n 
1 97  PRO n 
1 98  SER n 
1 99  LYS n 
1 100 SER n 
1 101 SER n 
1 102 VAL n 
1 103 GLY n 
1 104 SER n 
1 105 TYR n 
1 106 PHE n 
1 107 HIS n 
1 108 THR n 
1 109 MET n 
1 110 VAL n 
1 111 GLU n 
1 112 SER n 
1 113 LEU n 
1 114 VAL n 
1 115 GLY n 
1 116 TRP n 
1 117 GLY n 
1 118 TYR n 
1 119 THR n 
1 120 ARG n 
1 121 GLY n 
1 122 GLU n 
1 123 ASP n 
1 124 VAL n 
1 125 ARG n 
1 126 GLY n 
1 127 ALA n 
1 128 PRO n 
1 129 TYR n 
1 130 ASP n 
1 131 TRP n 
1 132 ARG n 
1 133 ARG n 
1 134 ALA n 
1 135 PRO n 
1 136 ASN n 
1 137 GLU n 
1 138 ASN n 
1 139 GLY n 
1 140 PRO n 
1 141 TYR n 
1 142 PHE n 
1 143 LEU n 
1 144 ALA n 
1 145 LEU n 
1 146 ARG n 
1 147 GLU n 
1 148 MET n 
1 149 ILE n 
1 150 GLU n 
1 151 GLU n 
1 152 MET n 
1 153 TYR n 
1 154 GLN n 
1 155 LEU n 
1 156 TYR n 
1 157 GLY n 
1 158 GLY n 
1 159 PRO n 
1 160 VAL n 
1 161 VAL n 
1 162 LEU n 
1 163 VAL n 
1 164 ALA n 
1 165 HIS n 
1 166 SER n 
1 167 MET n 
1 168 GLY n 
1 169 ASN n 
1 170 MET n 
1 171 TYR n 
1 172 THR n 
1 173 LEU n 
1 174 TYR n 
1 175 PHE n 
1 176 LEU n 
1 177 GLN n 
1 178 ARG n 
1 179 GLN n 
1 180 PRO n 
1 181 GLN n 
1 182 ALA n 
1 183 TRP n 
1 184 LYS n 
1 185 ASP n 
1 186 LYS n 
1 187 TYR n 
1 188 ILE n 
1 189 ARG n 
1 190 ALA n 
1 191 PHE n 
1 192 VAL n 
1 193 SER n 
1 194 LEU n 
1 195 GLY n 
1 196 ALA n 
1 197 PRO n 
1 198 TRP n 
1 199 GLY n 
1 200 GLY n 
1 201 VAL n 
1 202 ALA n 
1 203 LYS n 
1 204 THR n 
1 205 LEU n 
1 206 ARG n 
1 207 VAL n 
1 208 LEU n 
1 209 ALA n 
1 210 SER n 
1 211 GLY n 
1 212 ASP n 
1 213 ASN n 
1 214 ASN n 
1 215 ARG n 
1 216 ILE n 
1 217 PRO n 
1 218 VAL n 
1 219 ILE n 
1 220 GLY n 
1 221 PRO n 
1 222 LEU n 
1 223 LYS n 
1 224 ILE n 
1 225 ARG n 
1 226 GLU n 
1 227 GLN n 
1 228 GLN n 
1 229 ARG n 
1 230 SER n 
1 231 ALA n 
1 232 VAL n 
1 233 SER n 
1 234 THR n 
1 235 SER n 
1 236 TRP n 
1 237 LEU n 
1 238 LEU n 
1 239 PRO n 
1 240 TYR n 
1 241 ASN n 
1 242 TYR n 
1 243 THR n 
1 244 TRP n 
1 245 SER n 
1 246 PRO n 
1 247 GLU n 
1 248 LYS n 
1 249 VAL n 
1 250 PHE n 
1 251 VAL n 
1 252 GLN n 
1 253 THR n 
1 254 PRO n 
1 255 THR n 
1 256 ILE n 
1 257 ASN n 
1 258 TYR n 
1 259 THR n 
1 260 LEU n 
1 261 ARG n 
1 262 ASP n 
1 263 TYR n 
1 264 ARG n 
1 265 LYS n 
1 266 PHE n 
1 267 PHE n 
1 268 GLN n 
1 269 ASP n 
1 270 ILE n 
1 271 GLY n 
1 272 PHE n 
1 273 GLU n 
1 274 ASP n 
1 275 GLY n 
1 276 TRP n 
1 277 LEU n 
1 278 MET n 
1 279 ARG n 
1 280 GLN n 
1 281 ASP n 
1 282 THR n 
1 283 GLU n 
1 284 GLY n 
1 285 LEU n 
1 286 VAL n 
1 287 GLU n 
1 288 ALA n 
1 289 THR n 
1 290 MET n 
1 291 PRO n 
1 292 PRO n 
1 293 GLY n 
1 294 VAL n 
1 295 GLN n 
1 296 LEU n 
1 297 HIS n 
1 298 CYS n 
1 299 LEU n 
1 300 TYR n 
1 301 GLY n 
1 302 THR n 
1 303 GLY n 
1 304 VAL n 
1 305 PRO n 
1 306 THR n 
1 307 PRO n 
1 308 ASP n 
1 309 SER n 
1 310 PHE n 
1 311 TYR n 
1 312 TYR n 
1 313 GLU n 
1 314 SER n 
1 315 PHE n 
1 316 PRO n 
1 317 ASP n 
1 318 ARG n 
1 319 ASP n 
1 320 PRO n 
1 321 LYS n 
1 322 ILE n 
1 323 CYS n 
1 324 PHE n 
1 325 GLY n 
1 326 ASP n 
1 327 GLY n 
1 328 ASP n 
1 329 GLY n 
1 330 THR n 
1 331 VAL n 
1 332 ASN n 
1 333 LEU n 
1 334 LYS n 
1 335 SER n 
1 336 ALA n 
1 337 LEU n 
1 338 GLN n 
1 339 CYS n 
1 340 GLN n 
1 341 ALA n 
1 342 TRP n 
1 343 GLN n 
1 344 SER n 
1 345 ARG n 
1 346 GLN n 
1 347 GLU n 
1 348 HIS n 
1 349 GLN n 
1 350 VAL n 
1 351 LEU n 
1 352 LEU n 
1 353 GLN n 
1 354 GLU n 
1 355 LEU n 
1 356 PRO n 
1 357 GLY n 
1 358 SER n 
1 359 GLU n 
1 360 HIS n 
1 361 ILE n 
1 362 GLU n 
1 363 MET n 
1 364 LEU n 
1 365 ALA n 
1 366 ASN n 
1 367 ALA n 
1 368 THR n 
1 369 THR n 
1 370 LEU n 
1 371 ALA n 
1 372 TYR n 
1 373 LEU n 
1 374 LYS n 
1 375 ARG n 
1 376 VAL n 
1 377 LEU n 
1 378 LEU n 
1 379 GLY n 
1 380 PRO 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                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   380 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'PLA2G15, LYPLA3, UNQ341/PRO540' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_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            'HEK293S GnTI-' 
_entity_src_gen.pdbx_host_org_atcc                 CRL-3022 
_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                    PAG15_HUMAN 
_struct_ref.pdbx_db_accession          Q8NCC3 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;AGRHPPVVLVPGDLGNQLEAKLDKPTVVHYLCSKKTESYFTIWLNLELLLPVIIDCWIDNIRLVYNKTSRATQFPDGVDV
RVPGFGKTFSLEFLDPSKSSVGSYFHTMVESLVGWGYTRGEDVRGAPYDWRRAPNENGPYFLALREMIEEMYQLYGGPVV
LVAHSMGNMYTLYFLQRQPQAWKDKYIRAFVSLGAPWGGVAKTLRVLASGDNNRIPVIGPLKIREQQRSAVSTSWLLPYN
YTWSPEKVFVQTPTINYTLRDYRKFFQDIGFEDGWLMRQDTEGLVEATMPPGVQLHCLYGTGVPTPDSFYYESFPDRDPK
ICFGDGDGTVNLKSALQCQAWQSRQEHQVLLQELPGSEHIEMLANATTLAYLKRVLLGP
;
_struct_ref.pdbx_align_begin           34 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 4X90 A 2 ? 380 ? Q8NCC3 34 ? 412 ? 1 379 
2 1 4X90 B 2 ? 380 ? Q8NCC3 34 ? 412 ? 1 379 
3 1 4X90 C 2 ? 380 ? Q8NCC3 34 ? 412 ? 1 379 
4 1 4X90 D 2 ? 380 ? Q8NCC3 34 ? 412 ? 1 379 
# 
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 4X90 GLY A 1 ? UNP Q8NCC3 ? ? 'cloning artifact' 0 1 
2 4X90 GLY B 1 ? UNP Q8NCC3 ? ? 'cloning artifact' 0 2 
3 4X90 GLY C 1 ? UNP Q8NCC3 ? ? 'cloning artifact' 0 3 
4 4X90 GLY D 1 ? UNP Q8NCC3 ? ? 'cloning artifact' 0 4 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking'          y ALANINE                                               ?     'C3 H7 N O2'     89.093  
ARG 'L-peptide linking'          y ARGININE                                              ?     'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking'          y ASPARAGINE                                            ?     'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking'          y 'ASPARTIC ACID'                                       ?     'C4 H7 N O4'     133.103 
CL  non-polymer                  . 'CHLORIDE ION'                                        ?     'Cl -1'          35.453  
CYS 'L-peptide linking'          y CYSTEINE                                              ?     'C3 H7 N O2 S'   121.158 
EPE non-polymer                  . '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' HEPES 'C8 H18 N2 O4 S' 238.305 
GLN 'L-peptide linking'          y GLUTAMINE                                             ?     'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'          y 'GLUTAMIC ACID'                                       ?     'C5 H9 N O4'     147.129 
GLY 'peptide linking'            y GLYCINE                                               ?     'C2 H5 N O2'     75.067  
HIS 'L-peptide linking'          y HISTIDINE                                             ?     'C6 H10 N3 O2 1' 156.162 
HOH non-polymer                  . WATER                                                 ?     'H2 O'           18.015  
ILE 'L-peptide linking'          y ISOLEUCINE                                            ?     'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'          y LEUCINE                                               ?     'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'          y LYSINE                                                ?     'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'          y METHIONINE                                            ?     'C5 H11 N O2 S'  149.211 
MPD non-polymer                  . '(4S)-2-METHYL-2,4-PENTANEDIOL'                       ?     'C6 H14 O2'      118.174 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose              ?     'C8 H15 N O6'    221.208 
PHE 'L-peptide linking'          y PHENYLALANINE                                         ?     'C9 H11 N O2'    165.189 
PO4 non-polymer                  . 'PHOSPHATE ION'                                       ?     'O4 P -3'        94.971  
PRO 'L-peptide linking'          y PROLINE                                               ?     'C5 H9 N O2'     115.130 
SER 'L-peptide linking'          y SERINE                                                ?     'C3 H7 N O3'     105.093 
THR 'L-peptide linking'          y THREONINE                                             ?     'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'          y TRYPTOPHAN                                            ?     'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'          y TYROSINE                                              ?     'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'          y VALINE                                                ?     'C5 H11 N O2'    117.146 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   4X90 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            3.28 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         62.51 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100 mM HEPES pH 7.5, 3.5% PEG 8000, 28% MPD, 300 mM (NH4)2HPO4' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MARMOSAIC 300 mm CCD' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-06-14 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97937 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 23-ID-D' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97937 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   23-ID-D 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         4X90 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.830 
_reflns.d_resolution_low                 30.000 
_reflns.details                          ? 
_reflns.limit_h_max                      ? 
_reflns.limit_h_min                      ? 
_reflns.limit_k_max                      ? 
_reflns.limit_k_min                      ? 
_reflns.limit_l_max                      ? 
_reflns.limit_l_min                      ? 
_reflns.number_all                       ? 
_reflns.number_obs                       183439 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             97.800 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  4.000 
_reflns.pdbx_Rmerge_I_obs                0.095 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         17.917 
_reflns.pdbx_netI_over_sigmaI            6.700 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 1.191 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  ? 
_reflns.pdbx_Rpim_I_all                  ? 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         726111 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_R_split 
1.830 1.860  ? ? ? ? ? 8966 ? 96.400 ? ? ? ? 0.631 ? ? ? ? ? ? ? ? 3.900 ? 0.686 ? ? ? ? 0 1  1 ? ? 
1.860 1.900  ? ? ? ? ? 9080 ? 96.500 ? ? ? ? 0.564 ? ? ? ? ? ? ? ? 3.900 ? 0.726 ? ? ? ? 0 2  1 ? ? 
1.900 1.930  ? ? ? ? ? 9083 ? 96.600 ? ? ? ? 0.472 ? ? ? ? ? ? ? ? 3.900 ? 0.772 ? ? ? ? 0 3  1 ? ? 
1.930 1.970  ? ? ? ? ? 9069 ? 96.800 ? ? ? ? 0.410 ? ? ? ? ? ? ? ? 3.900 ? 0.777 ? ? ? ? 0 4  1 ? ? 
1.970 2.010  ? ? ? ? ? 9128 ? 97.000 ? ? ? ? 0.347 ? ? ? ? ? ? ? ? 3.900 ? 0.790 ? ? ? ? 0 5  1 ? ? 
2.010 2.060  ? ? ? ? ? 9062 ? 97.100 ? ? ? ? 0.305 ? ? ? ? ? ? ? ? 3.900 ? 0.873 ? ? ? ? 0 6  1 ? ? 
2.060 2.110  ? ? ? ? ? 9147 ? 97.200 ? ? ? ? 0.266 ? ? ? ? ? ? ? ? 4.000 ? 0.902 ? ? ? ? 0 7  1 ? ? 
2.110 2.170  ? ? ? ? ? 9066 ? 97.300 ? ? ? ? 0.238 ? ? ? ? ? ? ? ? 4.000 ? 0.903 ? ? ? ? 0 8  1 ? ? 
2.170 2.230  ? ? ? ? ? 9173 ? 97.600 ? ? ? ? 0.212 ? ? ? ? ? ? ? ? 4.000 ? 0.960 ? ? ? ? 0 9  1 ? ? 
2.230 2.310  ? ? ? ? ? 9187 ? 97.700 ? ? ? ? 0.189 ? ? ? ? ? ? ? ? 4.000 ? 0.999 ? ? ? ? 0 10 1 ? ? 
2.310 2.390  ? ? ? ? ? 9178 ? 97.800 ? ? ? ? 0.165 ? ? ? ? ? ? ? ? 4.000 ? 1.012 ? ? ? ? 0 11 1 ? ? 
2.390 2.480  ? ? ? ? ? 9187 ? 98.000 ? ? ? ? 0.148 ? ? ? ? ? ? ? ? 4.000 ? 1.057 ? ? ? ? 0 12 1 ? ? 
2.480 2.600  ? ? ? ? ? 9213 ? 98.200 ? ? ? ? 0.132 ? ? ? ? ? ? ? ? 4.000 ? 1.091 ? ? ? ? 0 13 1 ? ? 
2.600 2.730  ? ? ? ? ? 9204 ? 98.300 ? ? ? ? 0.113 ? ? ? ? ? ? ? ? 4.000 ? 1.187 ? ? ? ? 0 14 1 ? ? 
2.730 2.900  ? ? ? ? ? 9233 ? 98.500 ? ? ? ? 0.100 ? ? ? ? ? ? ? ? 4.000 ? 1.237 ? ? ? ? 0 15 1 ? ? 
2.900 3.130  ? ? ? ? ? 9257 ? 98.600 ? ? ? ? 0.082 ? ? ? ? ? ? ? ? 4.000 ? 1.380 ? ? ? ? 0 16 1 ? ? 
3.130 3.440  ? ? ? ? ? 9290 ? 98.800 ? ? ? ? 0.067 ? ? ? ? ? ? ? ? 4.000 ? 1.617 ? ? ? ? 0 17 1 ? ? 
3.440 3.940  ? ? ? ? ? 9270 ? 99.100 ? ? ? ? 0.058 ? ? ? ? ? ? ? ? 4.000 ? 1.906 ? ? ? ? 0 18 1 ? ? 
3.940 4.960  ? ? ? ? ? 9302 ? 99.200 ? ? ? ? 0.053 ? ? ? ? ? ? ? ? 3.900 ? 2.313 ? ? ? ? 0 19 1 ? ? 
4.960 30.000 ? ? ? ? ? 9344 ? 99.500 ? ? ? ? 0.058 ? ? ? ? ? ? ? ? 3.900 ? 2.536 ? ? ? ? 0 20 1 ? ? 
# 
_refine.aniso_B[1][1]                            1.7100 
_refine.aniso_B[1][2]                            -0.2400 
_refine.aniso_B[1][3]                            0.1300 
_refine.aniso_B[2][2]                            -0.2200 
_refine.aniso_B[2][3]                            0.2000 
_refine.aniso_B[3][3]                            -1.3000 
_refine.B_iso_max                                89.350 
_refine.B_iso_mean                               26.4220 
_refine.B_iso_min                                8.610 
_refine.correlation_coeff_Fo_to_Fc               0.9700 
_refine.correlation_coeff_Fo_to_Fc_free          0.9610 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES      : WITH TLS ADDED' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 4X90 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.8400 
_refine.ls_d_res_low                             30. 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     174210 
_refine.ls_number_reflns_R_free                  9229 
_refine.ls_number_reflns_R_work                  174210 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.8500 
_refine.ls_percent_reflns_R_free                 5.0000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1550 
_refine.ls_R_factor_R_free                       0.1733 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1541 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.1010 
_refine.pdbx_overall_ESU_R_Free                  0.0930 
_refine.pdbx_solvent_vdw_probe_radii             1.2000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             4.5060 
_refine.overall_SU_ML                            0.0660 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.8400 
_refine_hist.d_res_low                        30. 
_refine_hist.pdbx_number_atoms_ligand         476 
_refine_hist.number_atoms_solvent             1065 
_refine_hist.number_atoms_total               13617 
_refine_hist.pdbx_number_residues_total       1504 
_refine_hist.pdbx_B_iso_mean_ligand           42.16 
_refine_hist.pdbx_B_iso_mean_solvent          36.80 
_refine_hist.pdbx_number_atoms_protein        12076 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010  0.019  13498 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  12557 ? r_bond_other_d         ? ? 
'X-RAY DIFFRACTION' ? 1.441  1.991  18501 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 1.168  3.000  28856 ? r_angle_other_deg      ? ? 
'X-RAY DIFFRACTION' ? 5.816  5.006  1624  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 33.364 23.563 609   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 11.529 15.000 2088  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 13.245 15.000 84    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.085  0.200  2015  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.021  15191 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  3170  ? r_gen_planes_other     ? ? 
'X-RAY DIFFRACTION' ? 1.271  1.770  6274  ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 1.271  1.769  6273  ? r_mcbond_other         ? ? 
'X-RAY DIFFRACTION' ? 2.040  2.644  7893  ? r_mcangle_it           ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.pdbx_ens_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.weight_B_iso 
1  'X-RAY DIFFRACTION' 1 1 'interatomic distance' A 23512 0.090 0.050 ? ? ? 
2  'X-RAY DIFFRACTION' 1 2 'interatomic distance' B 23512 0.090 0.050 ? ? ? 
3  'X-RAY DIFFRACTION' 2 1 'interatomic distance' A 23567 0.090 0.050 ? ? ? 
4  'X-RAY DIFFRACTION' 2 2 'interatomic distance' C 23567 0.090 0.050 ? ? ? 
5  'X-RAY DIFFRACTION' 3 1 'interatomic distance' A 24248 0.060 0.050 ? ? ? 
6  'X-RAY DIFFRACTION' 3 2 'interatomic distance' D 24248 0.060 0.050 ? ? ? 
7  'X-RAY DIFFRACTION' 4 1 'interatomic distance' B 24220 0.060 0.050 ? ? ? 
8  'X-RAY DIFFRACTION' 4 2 'interatomic distance' C 24220 0.060 0.050 ? ? ? 
9  'X-RAY DIFFRACTION' 5 1 'interatomic distance' B 23549 0.090 0.050 ? ? ? 
10 'X-RAY DIFFRACTION' 5 2 'interatomic distance' D 23549 0.090 0.050 ? ? ? 
11 'X-RAY DIFFRACTION' 6 1 'interatomic distance' C 23467 0.090 0.050 ? ? ? 
12 'X-RAY DIFFRACTION' 6 2 'interatomic distance' D 23467 0.090 0.050 ? ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.8380 
_refine_ls_shell.d_res_low                        1.8860 
_refine_ls_shell.number_reflns_all                11744 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             586 
_refine_ls_shell.number_reflns_R_work             11158 
_refine_ls_shell.percent_reflns_obs               83.7000 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free                  0.2200 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2170 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
loop_
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.id 
_struct_ncs_dom.details 
1 1 A 
1 2 B 
2 1 A 
2 2 C 
3 1 A 
3 2 D 
4 1 B 
4 2 C 
5 1 B 
5 2 D 
6 1 C 
6 2 D 
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.selection_details 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
1 1 0 0 A 4 A 379 ? ? ? ? ? ? ? ? ? 
1 2 0 0 B 4 B 379 ? ? ? ? ? ? ? ? ? 
2 1 0 0 A 4 A 379 ? ? ? ? ? ? ? ? ? 
2 2 0 0 C 4 C 379 ? ? ? ? ? ? ? ? ? 
3 1 0 0 A 4 A 379 ? ? ? ? ? ? ? ? ? 
3 2 0 0 D 4 D 379 ? ? ? ? ? ? ? ? ? 
4 1 0 0 B 4 B 379 ? ? ? ? ? ? ? ? ? 
4 2 0 0 C 4 C 379 ? ? ? ? ? ? ? ? ? 
5 1 0 0 B 4 B 379 ? ? ? ? ? ? ? ? ? 
5 2 0 0 D 4 D 379 ? ? ? ? ? ? ? ? ? 
6 1 0 0 C 4 C 379 ? ? ? ? ? ? ? ? ? 
6 2 0 0 D 4 D 379 ? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ncs_ens.id 
_struct_ncs_ens.details 
1 ? 
2 ? 
3 ? 
4 ? 
5 ? 
6 ? 
# 
_struct.entry_id                     4X90 
_struct.title                        'Crystal structure of Lysosomal Phospholipase A2' 
_struct.pdbx_descriptor              'Group XV phospholipase A2 (E.C.2.3.1.-)' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        4X90 
_struct_keywords.text            'hydrolase, phospholipase, esterase, acyltransferase, TRANSFERASE' 
_struct_keywords.pdbx_keywords   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 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 2 ? 
F  N N 2 ? 
G  N N 2 ? 
H  N N 2 ? 
I  N N 3 ? 
J  N N 4 ? 
K  N N 5 ? 
L  N N 6 ? 
M  N N 6 ? 
N  N N 6 ? 
O  N N 6 ? 
P  N N 6 ? 
Q  N N 2 ? 
R  N N 2 ? 
S  N N 2 ? 
T  N N 2 ? 
U  N N 3 ? 
V  N N 4 ? 
W  N N 5 ? 
X  N N 6 ? 
Y  N N 6 ? 
Z  N N 2 ? 
AA N N 2 ? 
BA N N 2 ? 
CA N N 2 ? 
DA N N 3 ? 
EA N N 4 ? 
FA N N 5 ? 
GA N N 6 ? 
HA N N 6 ? 
IA N N 6 ? 
JA N N 2 ? 
KA N N 2 ? 
LA N N 2 ? 
MA N N 2 ? 
NA N N 3 ? 
OA N N 4 ? 
PA N N 5 ? 
QA N N 6 ? 
RA N N 6 ? 
SA N N 6 ? 
TA N N 6 ? 
UA N N 7 ? 
VA N N 7 ? 
WA N N 7 ? 
XA N N 7 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 46  ? LEU A 51  ? ASN A 45  LEU A 50  5 ? 6  
HELX_P HELX_P2  AA2 VAL A 53  ? ARG A 63  ? VAL A 52  ARG A 62  1 ? 11 
HELX_P HELX_P3  AA3 THR A 89  ? PHE A 94  ? THR A 88  PHE A 93  1 ? 6  
HELX_P HELX_P4  AA4 SER A 100 ? SER A 104 ? SER A 99  SER A 103 5 ? 5  
HELX_P HELX_P5  AA5 PHE A 106 ? TRP A 116 ? PHE A 105 TRP A 115 1 ? 11 
HELX_P HELX_P6  AA6 ALA A 134 ? GLU A 137 ? ALA A 133 GLU A 136 5 ? 4  
HELX_P HELX_P7  AA7 ASN A 138 ? GLY A 157 ? ASN A 137 GLY A 156 1 ? 20 
HELX_P HELX_P8  AA8 MET A 167 ? ARG A 178 ? MET A 166 ARG A 177 1 ? 12 
HELX_P HELX_P9  AA9 PRO A 180 ? TYR A 187 ? PRO A 179 TYR A 186 1 ? 8  
HELX_P HELX_P10 AB1 ALA A 202 ? GLY A 211 ? ALA A 201 GLY A 210 1 ? 10 
HELX_P HELX_P11 AB2 GLY A 220 ? ALA A 231 ? GLY A 219 ALA A 230 1 ? 12 
HELX_P HELX_P12 AB3 ALA A 231 ? LEU A 237 ? ALA A 230 LEU A 236 1 ? 7  
HELX_P HELX_P13 AB4 ASP A 262 ? ILE A 270 ? ASP A 261 ILE A 269 1 ? 9  
HELX_P HELX_P14 AB5 PHE A 272 ? GLU A 283 ? PHE A 271 GLU A 282 1 ? 12 
HELX_P HELX_P15 AB6 ASN A 332 ? LYS A 334 ? ASN A 331 LYS A 333 5 ? 3  
HELX_P HELX_P16 AB7 SER A 335 ? GLN A 343 ? SER A 334 GLN A 342 1 ? 9  
HELX_P HELX_P17 AB8 ILE A 361 ? ALA A 365 ? ILE A 360 ALA A 364 5 ? 5  
HELX_P HELX_P18 AB9 ASN A 366 ? GLY A 379 ? ASN A 365 GLY A 378 1 ? 14 
HELX_P HELX_P19 AC1 ASN B 46  ? LEU B 51  ? ASN B 45  LEU B 50  5 ? 6  
HELX_P HELX_P20 AC2 VAL B 53  ? ARG B 63  ? VAL B 52  ARG B 62  1 ? 11 
HELX_P HELX_P21 AC3 THR B 89  ? PHE B 94  ? THR B 88  PHE B 93  1 ? 6  
HELX_P HELX_P22 AC4 SER B 100 ? SER B 104 ? SER B 99  SER B 103 5 ? 5  
HELX_P HELX_P23 AC5 PHE B 106 ? TRP B 116 ? PHE B 105 TRP B 115 1 ? 11 
HELX_P HELX_P24 AC6 ALA B 134 ? GLU B 137 ? ALA B 133 GLU B 136 5 ? 4  
HELX_P HELX_P25 AC7 ASN B 138 ? GLY B 157 ? ASN B 137 GLY B 156 1 ? 20 
HELX_P HELX_P26 AC8 MET B 167 ? ARG B 178 ? MET B 166 ARG B 177 1 ? 12 
HELX_P HELX_P27 AC9 PRO B 180 ? TYR B 187 ? PRO B 179 TYR B 186 1 ? 8  
HELX_P HELX_P28 AD1 ALA B 202 ? GLY B 211 ? ALA B 201 GLY B 210 1 ? 10 
HELX_P HELX_P29 AD2 GLY B 220 ? ALA B 231 ? GLY B 219 ALA B 230 1 ? 12 
HELX_P HELX_P30 AD3 ALA B 231 ? LEU B 237 ? ALA B 230 LEU B 236 1 ? 7  
HELX_P HELX_P31 AD4 ASP B 262 ? GLY B 271 ? ASP B 261 GLY B 270 1 ? 10 
HELX_P HELX_P32 AD5 PHE B 272 ? GLU B 283 ? PHE B 271 GLU B 282 1 ? 12 
HELX_P HELX_P33 AD6 ASN B 332 ? LYS B 334 ? ASN B 331 LYS B 333 5 ? 3  
HELX_P HELX_P34 AD7 SER B 335 ? GLN B 343 ? SER B 334 GLN B 342 1 ? 9  
HELX_P HELX_P35 AD8 ILE B 361 ? ALA B 365 ? ILE B 360 ALA B 364 5 ? 5  
HELX_P HELX_P36 AD9 ASN B 366 ? GLY B 379 ? ASN B 365 GLY B 378 1 ? 14 
HELX_P HELX_P37 AE1 ASN C 46  ? LEU C 51  ? ASN C 45  LEU C 50  5 ? 6  
HELX_P HELX_P38 AE2 VAL C 53  ? ARG C 63  ? VAL C 52  ARG C 62  1 ? 11 
HELX_P HELX_P39 AE3 THR C 89  ? PHE C 94  ? THR C 88  PHE C 93  1 ? 6  
HELX_P HELX_P40 AE4 SER C 100 ? SER C 104 ? SER C 99  SER C 103 5 ? 5  
HELX_P HELX_P41 AE5 PHE C 106 ? TRP C 116 ? PHE C 105 TRP C 115 1 ? 11 
HELX_P HELX_P42 AE6 ALA C 134 ? GLU C 137 ? ALA C 133 GLU C 136 5 ? 4  
HELX_P HELX_P43 AE7 ASN C 138 ? GLY C 157 ? ASN C 137 GLY C 156 1 ? 20 
HELX_P HELX_P44 AE8 MET C 167 ? ARG C 178 ? MET C 166 ARG C 177 1 ? 12 
HELX_P HELX_P45 AE9 PRO C 180 ? TYR C 187 ? PRO C 179 TYR C 186 1 ? 8  
HELX_P HELX_P46 AF1 ALA C 202 ? GLY C 211 ? ALA C 201 GLY C 210 1 ? 10 
HELX_P HELX_P47 AF2 GLY C 220 ? ALA C 231 ? GLY C 219 ALA C 230 1 ? 12 
HELX_P HELX_P48 AF3 ALA C 231 ? LEU C 237 ? ALA C 230 LEU C 236 1 ? 7  
HELX_P HELX_P49 AF4 ASP C 262 ? GLY C 271 ? ASP C 261 GLY C 270 1 ? 10 
HELX_P HELX_P50 AF5 GLU C 273 ? GLU C 283 ? GLU C 272 GLU C 282 1 ? 11 
HELX_P HELX_P51 AF6 ASN C 332 ? LYS C 334 ? ASN C 331 LYS C 333 5 ? 3  
HELX_P HELX_P52 AF7 SER C 335 ? GLN C 343 ? SER C 334 GLN C 342 1 ? 9  
HELX_P HELX_P53 AF8 ILE C 361 ? ALA C 365 ? ILE C 360 ALA C 364 5 ? 5  
HELX_P HELX_P54 AF9 ASN C 366 ? GLY C 379 ? ASN C 365 GLY C 378 1 ? 14 
HELX_P HELX_P55 AG1 ASN D 46  ? LEU D 51  ? ASN D 45  LEU D 50  5 ? 6  
HELX_P HELX_P56 AG2 VAL D 53  ? ARG D 63  ? VAL D 52  ARG D 62  1 ? 11 
HELX_P HELX_P57 AG3 THR D 89  ? PHE D 94  ? THR D 88  PHE D 93  1 ? 6  
HELX_P HELX_P58 AG4 SER D 100 ? SER D 104 ? SER D 99  SER D 103 5 ? 5  
HELX_P HELX_P59 AG5 PHE D 106 ? TRP D 116 ? PHE D 105 TRP D 115 1 ? 11 
HELX_P HELX_P60 AG6 ALA D 134 ? GLU D 137 ? ALA D 133 GLU D 136 5 ? 4  
HELX_P HELX_P61 AG7 ASN D 138 ? GLY D 157 ? ASN D 137 GLY D 156 1 ? 20 
HELX_P HELX_P62 AG8 MET D 167 ? ARG D 178 ? MET D 166 ARG D 177 1 ? 12 
HELX_P HELX_P63 AG9 PRO D 180 ? TYR D 187 ? PRO D 179 TYR D 186 1 ? 8  
HELX_P HELX_P64 AH1 ALA D 202 ? GLY D 211 ? ALA D 201 GLY D 210 1 ? 10 
HELX_P HELX_P65 AH2 GLY D 220 ? ALA D 231 ? GLY D 219 ALA D 230 1 ? 12 
HELX_P HELX_P66 AH3 ALA D 231 ? LEU D 237 ? ALA D 230 LEU D 236 1 ? 7  
HELX_P HELX_P67 AH4 ASP D 262 ? ILE D 270 ? ASP D 261 ILE D 269 1 ? 9  
HELX_P HELX_P68 AH5 PHE D 272 ? GLU D 283 ? PHE D 271 GLU D 282 1 ? 12 
HELX_P HELX_P69 AH6 ASN D 332 ? LYS D 334 ? ASN D 331 LYS D 333 5 ? 3  
HELX_P HELX_P70 AH7 SER D 335 ? GLN D 343 ? SER D 334 GLN D 342 1 ? 9  
HELX_P HELX_P71 AH8 ILE D 361 ? ALA D 365 ? ILE D 360 ALA D 364 5 ? 5  
HELX_P HELX_P72 AH9 ASN D 366 ? GLY D 379 ? ASN D 365 GLY D 378 1 ? 14 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?   ? A CYS 33  SG  ? ? ? 1_555 A  CYS 57 SG ? ? A CYS 32  A CYS 56  1_555 ? ? ? ? ? ? ? 2.038 ? ?               
disulf2  disulf ?   ? B CYS 33  SG  ? ? ? 1_555 B  CYS 57 SG ? ? B CYS 32  B CYS 56  1_555 ? ? ? ? ? ? ? 2.046 ? ?               
disulf3  disulf ?   ? C CYS 33  SG  ? ? ? 1_555 C  CYS 57 SG ? ? C CYS 32  C CYS 56  1_555 ? ? ? ? ? ? ? 2.055 ? ?               
disulf4  disulf ?   ? D CYS 33  SG  ? ? ? 1_555 D  CYS 57 SG ? ? D CYS 32  D CYS 56  1_555 ? ? ? ? ? ? ? 2.052 ? ?               
covale1  covale one ? A ASN 67  ND2 ? ? ? 1_555 E  NAG .  C1 ? ? A ASN 66  A NAG 401 1_555 ? ? ? ? ? ? ? 1.445 ? N-Glycosylation 
covale2  covale one ? A ASN 241 ND2 ? ? ? 1_555 F  NAG .  C1 ? ? A ASN 240 A NAG 402 1_555 ? ? ? ? ? ? ? 1.429 ? N-Glycosylation 
covale3  covale one ? A ASN 257 ND2 A ? ? 1_555 G  NAG .  C1 A ? A ASN 256 A NAG 403 1_555 ? ? ? ? ? ? ? 1.449 ? N-Glycosylation 
covale4  covale one ? A ASN 257 ND2 B ? ? 1_555 G  NAG .  C1 B ? A ASN 256 A NAG 403 1_555 ? ? ? ? ? ? ? 1.445 ? N-Glycosylation 
covale5  covale one ? A ASN 366 ND2 ? ? ? 1_555 H  NAG .  C1 ? ? A ASN 365 A NAG 404 1_555 ? ? ? ? ? ? ? 1.432 ? N-Glycosylation 
covale6  covale one ? B ASN 67  ND2 ? ? ? 1_555 Q  NAG .  C1 ? ? B ASN 66  B NAG 401 1_555 ? ? ? ? ? ? ? 1.452 ? N-Glycosylation 
covale7  covale one ? B ASN 241 ND2 ? ? ? 1_555 R  NAG .  C1 ? ? B ASN 240 B NAG 402 1_555 ? ? ? ? ? ? ? 1.438 ? N-Glycosylation 
covale8  covale one ? B ASN 257 ND2 A ? ? 1_555 S  NAG .  C1 A ? B ASN 256 B NAG 403 1_555 ? ? ? ? ? ? ? 1.439 ? N-Glycosylation 
covale9  covale one ? B ASN 257 ND2 B ? ? 1_555 S  NAG .  C1 B ? B ASN 256 B NAG 403 1_555 ? ? ? ? ? ? ? 1.453 ? N-Glycosylation 
covale10 covale one ? B ASN 366 ND2 ? ? ? 1_555 T  NAG .  C1 ? ? B ASN 365 B NAG 404 1_555 ? ? ? ? ? ? ? 1.429 ? N-Glycosylation 
covale11 covale one ? C ASN 67  ND2 ? ? ? 1_555 Z  NAG .  C1 ? ? C ASN 66  C NAG 401 1_555 ? ? ? ? ? ? ? 1.455 ? N-Glycosylation 
covale12 covale one ? C ASN 241 ND2 ? ? ? 1_555 AA NAG .  C1 ? ? C ASN 240 C NAG 402 1_555 ? ? ? ? ? ? ? 1.437 ? N-Glycosylation 
covale13 covale one ? C ASN 257 ND2 A ? ? 1_555 BA NAG .  C1 A ? C ASN 256 C NAG 403 1_555 ? ? ? ? ? ? ? 1.449 ? N-Glycosylation 
covale14 covale one ? C ASN 257 ND2 B ? ? 1_555 BA NAG .  C1 B ? C ASN 256 C NAG 403 1_555 ? ? ? ? ? ? ? 1.436 ? N-Glycosylation 
covale15 covale one ? C ASN 366 ND2 ? ? ? 1_555 CA NAG .  C1 ? ? C ASN 365 C NAG 404 1_555 ? ? ? ? ? ? ? 1.424 ? N-Glycosylation 
covale16 covale one ? D ASN 67  ND2 ? ? ? 1_555 JA NAG .  C1 ? ? D ASN 66  D NAG 402 1_555 ? ? ? ? ? ? ? 1.435 ? N-Glycosylation 
covale17 covale one ? D ASN 241 ND2 ? ? ? 1_555 KA NAG .  C1 ? ? D ASN 240 D NAG 403 1_555 ? ? ? ? ? ? ? 1.433 ? N-Glycosylation 
covale18 covale one ? D ASN 257 ND2 A ? ? 1_555 LA NAG .  C1 A ? D ASN 256 D NAG 404 1_555 ? ? ? ? ? ? ? 1.452 ? N-Glycosylation 
covale19 covale one ? D ASN 257 ND2 B ? ? 1_555 LA NAG .  C1 B ? D ASN 256 D NAG 404 1_555 ? ? ? ? ? ? ? 1.454 ? N-Glycosylation 
covale20 covale one ? D ASN 366 ND2 ? ? ? 1_555 MA NAG .  C1 ? ? D ASN 365 D NAG 405 1_555 ? ? ? ? ? ? ? 1.429 ? N-Glycosylation 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 TRP 44  A . ? TRP 43  A LEU 45  A ? LEU 44  A 1 -0.96 
2 PHE 315 A . ? PHE 314 A PRO 316 A ? PRO 315 A 1 0.82  
3 TRP 44  B . ? TRP 43  B LEU 45  B ? LEU 44  B 1 -1.78 
4 PHE 315 B . ? PHE 314 B PRO 316 B ? PRO 315 B 1 3.23  
5 TRP 44  C . ? TRP 43  C LEU 45  C ? LEU 44  C 1 -1.40 
6 PHE 315 C . ? PHE 314 C PRO 316 C ? PRO 315 C 1 1.93  
7 TRP 44  D . ? TRP 43  D LEU 45  D ? LEU 44  D 1 -0.63 
8 PHE 315 D . ? PHE 314 D PRO 316 D ? PRO 315 D 1 2.66  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 6 ? 
AA6 ? 3 ? 
AA7 ? 2 ? 
AA8 ? 4 ? 
AA9 ? 6 ? 
AB1 ? 3 ? 
AB2 ? 2 ? 
AB3 ? 4 ? 
AB4 ? 6 ? 
AB5 ? 3 ? 
AB6 ? 2 ? 
AB7 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? parallel      
AA4 3 4 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? parallel      
AA5 5 6 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? parallel      
AA8 3 4 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? parallel      
AA9 3 4 ? parallel      
AA9 4 5 ? parallel      
AA9 5 6 ? parallel      
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? parallel      
AB3 3 4 ? anti-parallel 
AB4 1 2 ? parallel      
AB4 2 3 ? parallel      
AB4 3 4 ? parallel      
AB4 4 5 ? parallel      
AB4 5 6 ? parallel      
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? parallel      
AB7 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 124 ? GLY A 126 ? VAL A 123 GLY A 125 
AA1 2 VAL A 8   ? VAL A 11  ? VAL A 7   VAL A 10  
AA1 3 VAL A 160 ? HIS A 165 ? VAL A 159 HIS A 164 
AA1 4 ILE A 188 ? LEU A 194 ? ILE A 187 LEU A 193 
AA1 5 LEU A 296 ? THR A 302 ? LEU A 295 THR A 301 
AA1 6 VAL A 350 ? PRO A 356 ? VAL A 349 PRO A 355 
AA2 1 PHE A 41  ? TRP A 44  ? PHE A 40  TRP A 43  
AA2 2 LEU A 19  ? LEU A 23  ? LEU A 18  LEU A 22  
AA2 3 VAL A 79  ? ARG A 82  ? VAL A 78  ARG A 81  
AA3 1 VAL A 65  ? ASN A 67  ? VAL A 64  ASN A 66  
AA3 2 ALA A 72  ? GLN A 74  ? ALA A 71  GLN A 73  
AA4 1 ASN A 257 ? THR A 259 ? ASN A 256 THR A 258 
AA4 2 VAL A 249 ? GLN A 252 ? VAL A 248 GLN A 251 
AA4 3 THR A 306 ? TYR A 311 ? THR A 305 TYR A 310 
AA4 4 LYS A 321 ? GLY A 325 ? LYS A 320 GLY A 324 
AA5 1 VAL B 124 ? GLY B 126 ? VAL B 123 GLY B 125 
AA5 2 VAL B 8   ? VAL B 11  ? VAL B 7   VAL B 10  
AA5 3 VAL B 160 ? HIS B 165 ? VAL B 159 HIS B 164 
AA5 4 ILE B 188 ? LEU B 194 ? ILE B 187 LEU B 193 
AA5 5 LEU B 296 ? THR B 302 ? LEU B 295 THR B 301 
AA5 6 VAL B 350 ? PRO B 356 ? VAL B 349 PRO B 355 
AA6 1 PHE B 41  ? TRP B 44  ? PHE B 40  TRP B 43  
AA6 2 LEU B 19  ? LEU B 23  ? LEU B 18  LEU B 22  
AA6 3 VAL B 79  ? ARG B 82  ? VAL B 78  ARG B 81  
AA7 1 VAL B 65  ? ASN B 67  ? VAL B 64  ASN B 66  
AA7 2 ALA B 72  ? GLN B 74  ? ALA B 71  GLN B 73  
AA8 1 ASN B 257 ? TYR B 258 ? ASN B 256 TYR B 257 
AA8 2 VAL B 251 ? GLN B 252 ? VAL B 250 GLN B 251 
AA8 3 THR B 306 ? TYR B 311 ? THR B 305 TYR B 310 
AA8 4 LYS B 321 ? GLY B 325 ? LYS B 320 GLY B 324 
AA9 1 VAL C 124 ? GLY C 126 ? VAL C 123 GLY C 125 
AA9 2 VAL C 8   ? VAL C 11  ? VAL C 7   VAL C 10  
AA9 3 VAL C 160 ? HIS C 165 ? VAL C 159 HIS C 164 
AA9 4 ILE C 188 ? LEU C 194 ? ILE C 187 LEU C 193 
AA9 5 LEU C 296 ? THR C 302 ? LEU C 295 THR C 301 
AA9 6 VAL C 350 ? PRO C 356 ? VAL C 349 PRO C 355 
AB1 1 PHE C 41  ? TRP C 44  ? PHE C 40  TRP C 43  
AB1 2 LEU C 19  ? LEU C 23  ? LEU C 18  LEU C 22  
AB1 3 VAL C 79  ? ARG C 82  ? VAL C 78  ARG C 81  
AB2 1 VAL C 65  ? ASN C 67  ? VAL C 64  ASN C 66  
AB2 2 ALA C 72  ? GLN C 74  ? ALA C 71  GLN C 73  
AB3 1 ASN C 257 ? TYR C 258 ? ASN C 256 TYR C 257 
AB3 2 VAL C 251 ? GLN C 252 ? VAL C 250 GLN C 251 
AB3 3 THR C 306 ? TYR C 311 ? THR C 305 TYR C 310 
AB3 4 LYS C 321 ? GLY C 325 ? LYS C 320 GLY C 324 
AB4 1 VAL D 124 ? GLY D 126 ? VAL D 123 GLY D 125 
AB4 2 VAL D 8   ? VAL D 11  ? VAL D 7   VAL D 10  
AB4 3 VAL D 160 ? HIS D 165 ? VAL D 159 HIS D 164 
AB4 4 ILE D 188 ? LEU D 194 ? ILE D 187 LEU D 193 
AB4 5 LEU D 296 ? THR D 302 ? LEU D 295 THR D 301 
AB4 6 VAL D 350 ? PRO D 356 ? VAL D 349 PRO D 355 
AB5 1 PHE D 41  ? TRP D 44  ? PHE D 40  TRP D 43  
AB5 2 LEU D 19  ? LEU D 23  ? LEU D 18  LEU D 22  
AB5 3 VAL D 79  ? ARG D 82  ? VAL D 78  ARG D 81  
AB6 1 VAL D 65  ? ASN D 67  ? VAL D 64  ASN D 66  
AB6 2 ALA D 72  ? GLN D 74  ? ALA D 71  GLN D 73  
AB7 1 ASN D 257 ? THR D 259 ? ASN D 256 THR D 258 
AB7 2 VAL D 249 ? GLN D 252 ? VAL D 248 GLN D 251 
AB7 3 THR D 306 ? TYR D 311 ? THR D 305 TYR D 310 
AB7 4 LYS D 321 ? GLY D 325 ? LYS D 320 GLY D 324 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ARG A 125 ? O ARG A 124 N LEU A 10  ? N LEU A 9   
AA1 2 3 N VAL A 9   ? N VAL A 8   O VAL A 163 ? O VAL A 162 
AA1 3 4 N LEU A 162 ? N LEU A 161 O VAL A 192 ? O VAL A 191 
AA1 4 5 N SER A 193 ? N SER A 192 O HIS A 297 ? O HIS A 296 
AA1 5 6 N CYS A 298 ? N CYS A 297 O LEU A 351 ? O LEU A 350 
AA2 1 2 O PHE A 41  ? O PHE A 40  N ALA A 21  ? N ALA A 20  
AA2 2 3 N GLU A 20  ? N GLU A 19  O ARG A 82  ? O ARG A 81  
AA3 1 2 N VAL A 65  ? N VAL A 64  O GLN A 74  ? O GLN A 73  
AA4 1 2 O TYR A 258 ? O TYR A 257 N VAL A 251 ? N VAL A 250 
AA4 2 3 N GLN A 252 ? N GLN A 251 O PHE A 310 ? O PHE A 309 
AA4 3 4 N ASP A 308 ? N ASP A 307 O CYS A 323 ? O CYS A 322 
AA5 1 2 O ARG B 125 ? O ARG B 124 N LEU B 10  ? N LEU B 9   
AA5 2 3 N VAL B 9   ? N VAL B 8   O VAL B 163 ? O VAL B 162 
AA5 3 4 N LEU B 162 ? N LEU B 161 O VAL B 192 ? O VAL B 191 
AA5 4 5 N SER B 193 ? N SER B 192 O HIS B 297 ? O HIS B 296 
AA5 5 6 N CYS B 298 ? N CYS B 297 O LEU B 351 ? O LEU B 350 
AA6 1 2 O PHE B 41  ? O PHE B 40  N ALA B 21  ? N ALA B 20  
AA6 2 3 N GLU B 20  ? N GLU B 19  O ARG B 82  ? O ARG B 81  
AA7 1 2 N VAL B 65  ? N VAL B 64  O GLN B 74  ? O GLN B 73  
AA8 1 2 O TYR B 258 ? O TYR B 257 N VAL B 251 ? N VAL B 250 
AA8 2 3 N GLN B 252 ? N GLN B 251 O PHE B 310 ? O PHE B 309 
AA8 3 4 N THR B 306 ? N THR B 305 O GLY B 325 ? O GLY B 324 
AA9 1 2 O ARG C 125 ? O ARG C 124 N LEU C 10  ? N LEU C 9   
AA9 2 3 N VAL C 9   ? N VAL C 8   O VAL C 163 ? O VAL C 162 
AA9 3 4 N LEU C 162 ? N LEU C 161 O VAL C 192 ? O VAL C 191 
AA9 4 5 N SER C 193 ? N SER C 192 O HIS C 297 ? O HIS C 296 
AA9 5 6 N CYS C 298 ? N CYS C 297 O LEU C 351 ? O LEU C 350 
AB1 1 2 O PHE C 41  ? O PHE C 40  N ALA C 21  ? N ALA C 20  
AB1 2 3 N GLU C 20  ? N GLU C 19  O ARG C 82  ? O ARG C 81  
AB2 1 2 N VAL C 65  ? N VAL C 64  O GLN C 74  ? O GLN C 73  
AB3 1 2 O TYR C 258 ? O TYR C 257 N VAL C 251 ? N VAL C 250 
AB3 2 3 N GLN C 252 ? N GLN C 251 O PHE C 310 ? O PHE C 309 
AB3 3 4 N ASP C 308 ? N ASP C 307 O CYS C 323 ? O CYS C 322 
AB4 1 2 O ARG D 125 ? O ARG D 124 N LEU D 10  ? N LEU D 9   
AB4 2 3 N VAL D 9   ? N VAL D 8   O VAL D 163 ? O VAL D 162 
AB4 3 4 N LEU D 162 ? N LEU D 161 O VAL D 192 ? O VAL D 191 
AB4 4 5 N SER D 193 ? N SER D 192 O HIS D 297 ? O HIS D 296 
AB4 5 6 N CYS D 298 ? N CYS D 297 O LEU D 351 ? O LEU D 350 
AB5 1 2 O PHE D 41  ? O PHE D 40  N ALA D 21  ? N ALA D 20  
AB5 2 3 N GLU D 20  ? N GLU D 19  O ARG D 82  ? O ARG D 81  
AB6 1 2 N VAL D 65  ? N VAL D 64  O GLN D 74  ? O GLN D 73  
AB7 1 2 O TYR D 258 ? O TYR D 257 N VAL D 251 ? N VAL D 250 
AB7 2 3 N GLN D 252 ? N GLN D 251 O PHE D 310 ? O PHE D 309 
AB7 3 4 N ASP D 308 ? N ASP D 307 O CYS D 323 ? O CYS D 322 
# 
_atom_sites.entry_id                    4X90 
_atom_sites.fract_transf_matrix[1][1]   0.015922 
_atom_sites.fract_transf_matrix[1][2]   -0.000416 
_atom_sites.fract_transf_matrix[1][3]   -0.000349 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010975 
_atom_sites.fract_transf_matrix[2][3]   -0.002300 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.010194 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
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 
ATOM   1     N  N   . HIS A  1 5   ? -19.064 -9.150  0.934   1.00 30.16 ? 4   HIS A N   1 
ATOM   2     C  CA  . HIS A  1 5   ? -18.358 -9.726  2.081   1.00 28.46 ? 4   HIS A CA  1 
ATOM   3     C  C   . HIS A  1 5   ? -17.802 -8.678  3.014   1.00 26.13 ? 4   HIS A C   1 
ATOM   4     O  O   . HIS A  1 5   ? -17.363 -7.626  2.601   1.00 27.47 ? 4   HIS A O   1 
ATOM   5     C  CB  . HIS A  1 5   ? -17.238 -10.637 1.618   1.00 29.08 ? 4   HIS A CB  1 
ATOM   6     C  CG  . HIS A  1 5   ? -16.191 -9.971  0.773   1.00 29.41 ? 4   HIS A CG  1 
ATOM   7     N  ND1 . HIS A  1 5   ? -15.932 -10.385 -0.512  1.00 31.29 ? 4   HIS A ND1 1 
ATOM   8     C  CD2 . HIS A  1 5   ? -15.300 -8.986  1.035   1.00 30.36 ? 4   HIS A CD2 1 
ATOM   9     C  CE1 . HIS A  1 5   ? -14.925 -9.688  -1.008  1.00 31.77 ? 4   HIS A CE1 1 
ATOM   10    N  NE2 . HIS A  1 5   ? -14.527 -8.822  -0.090  1.00 29.90 ? 4   HIS A NE2 1 
ATOM   11    N  N   . PRO A  1 6   ? -17.731 -9.015  4.287   1.00 23.01 ? 5   PRO A N   1 
ATOM   12    C  CA  . PRO A  1 6   ? -17.327 -7.980  5.232   1.00 21.81 ? 5   PRO A CA  1 
ATOM   13    C  C   . PRO A  1 6   ? -15.807 -7.791  5.286   1.00 19.64 ? 5   PRO A C   1 
ATOM   14    O  O   . PRO A  1 6   ? -15.057 -8.751  5.030   1.00 19.35 ? 5   PRO A O   1 
ATOM   15    C  CB  . PRO A  1 6   ? -17.830 -8.533  6.552   1.00 22.43 ? 5   PRO A CB  1 
ATOM   16    C  CG  . PRO A  1 6   ? -17.731 -10.012 6.379   1.00 23.49 ? 5   PRO A CG  1 
ATOM   17    C  CD  . PRO A  1 6   ? -18.090 -10.283 4.944   1.00 23.85 ? 5   PRO A CD  1 
ATOM   18    N  N   . PRO A  1 7   ? -15.357 -6.587  5.645   1.00 18.38 ? 6   PRO A N   1 
ATOM   19    C  CA  . PRO A  1 7   ? -13.906 -6.394  5.876   1.00 17.41 ? 6   PRO A CA  1 
ATOM   20    C  C   . PRO A  1 7   ? -13.365 -7.301  6.984   1.00 17.30 ? 6   PRO A C   1 
ATOM   21    O  O   . PRO A  1 7   ? -14.080 -7.615  7.935   1.00 16.25 ? 6   PRO A O   1 
ATOM   22    C  CB  . PRO A  1 7   ? -13.765 -4.892  6.211   1.00 17.73 ? 6   PRO A CB  1 
ATOM   23    C  CG  . PRO A  1 7   ? -15.153 -4.300  6.177   1.00 19.03 ? 6   PRO A CG  1 
ATOM   24    C  CD  . PRO A  1 7   ? -16.160 -5.399  5.977   1.00 18.71 ? 6   PRO A CD  1 
ATOM   25    N  N   . VAL A  1 8   ? -12.090 -7.665  6.873   1.00 15.99 ? 7   VAL A N   1 
ATOM   26    C  CA  . VAL A  1 8   ? -11.453 -8.610  7.770   1.00 15.29 ? 7   VAL A CA  1 
ATOM   27    C  C   . VAL A  1 8   ? -10.165 -8.010  8.328   1.00 14.61 ? 7   VAL A C   1 
ATOM   28    O  O   . VAL A  1 8   ? -9.363  -7.464  7.560   1.00 13.71 ? 7   VAL A O   1 
ATOM   29    C  CB  . VAL A  1 8   ? -11.127 -9.918  7.033   1.00 15.53 ? 7   VAL A CB  1 
ATOM   30    C  CG1 . VAL A  1 8   ? -10.255 -10.833 7.860   1.00 15.96 ? 7   VAL A CG1 1 
ATOM   31    C  CG2 . VAL A  1 8   ? -12.414 -10.664 6.662   1.00 16.65 ? 7   VAL A CG2 1 
ATOM   32    N  N   . VAL A  1 9   ? -9.978  -8.150  9.642   1.00 14.13 ? 8   VAL A N   1 
ATOM   33    C  CA  . VAL A  1 9   ? -8.720  -7.801  10.301  1.00 15.12 ? 8   VAL A CA  1 
ATOM   34    C  C   . VAL A  1 9   ? -8.131  -9.067  10.930  1.00 15.20 ? 8   VAL A C   1 
ATOM   35    O  O   . VAL A  1 9   ? -8.828  -9.799  11.641  1.00 15.01 ? 8   VAL A O   1 
ATOM   36    C  CB  . VAL A  1 9   ? -8.917  -6.703  11.369  1.00 15.49 ? 8   VAL A CB  1 
ATOM   37    C  CG1 . VAL A  1 9   ? -7.648  -6.498  12.185  1.00 15.42 ? 8   VAL A CG1 1 
ATOM   38    C  CG2 . VAL A  1 9   ? -9.364  -5.378  10.720  1.00 16.44 ? 8   VAL A CG2 1 
ATOM   39    N  N   . LEU A  1 10  ? -6.873  -9.329  10.614  1.00 14.51 ? 9   LEU A N   1 
ATOM   40    C  CA  . LEU A  1 10  ? -6.151  -10.498 11.076  1.00 14.51 ? 9   LEU A CA  1 
ATOM   41    C  C   . LEU A  1 10  ? -5.240  -10.124 12.243  1.00 14.37 ? 9   LEU A C   1 
ATOM   42    O  O   . LEU A  1 10  ? -4.440  -9.160  12.150  1.00 13.86 ? 9   LEU A O   1 
ATOM   43    C  CB  . LEU A  1 10  ? -5.314  -11.089 9.932   1.00 15.04 ? 9   LEU A CB  1 
ATOM   44    C  CG  . LEU A  1 10  ? -6.026  -11.390 8.607   1.00 15.52 ? 9   LEU A CG  1 
ATOM   45    C  CD1 . LEU A  1 10  ? -5.053  -11.816 7.537   1.00 16.44 ? 9   LEU A CD1 1 
ATOM   46    C  CD2 . LEU A  1 10  ? -7.098  -12.466 8.779   1.00 16.18 ? 9   LEU A CD2 1 
ATOM   47    N  N   . VAL A  1 11  ? -5.341  -10.887 13.332  1.00 13.74 ? 10  VAL A N   1 
ATOM   48    C  CA  . VAL A  1 11  ? -4.566  -10.619 14.559  1.00 13.10 ? 10  VAL A CA  1 
ATOM   49    C  C   . VAL A  1 11  ? -3.726  -11.842 14.867  1.00 13.28 ? 10  VAL A C   1 
ATOM   50    O  O   . VAL A  1 11  ? -4.260  -12.918 15.116  1.00 12.83 ? 10  VAL A O   1 
ATOM   51    C  CB  . VAL A  1 11  ? -5.459  -10.266 15.764  1.00 13.04 ? 10  VAL A CB  1 
ATOM   52    C  CG1 . VAL A  1 11  ? -4.612  -9.853  16.961  1.00 12.85 ? 10  VAL A CG1 1 
ATOM   53    C  CG2 . VAL A  1 11  ? -6.454  -9.169  15.408  1.00 13.93 ? 10  VAL A CG2 1 
ATOM   54    N  N   . PRO A  1 12  ? -2.393  -11.688 14.829  1.00 12.89 ? 11  PRO A N   1 
ATOM   55    C  CA  . PRO A  1 12  ? -1.514  -12.839 14.980  1.00 13.10 ? 11  PRO A CA  1 
ATOM   56    C  C   . PRO A  1 12  ? -1.232  -13.202 16.442  1.00 13.54 ? 11  PRO A C   1 
ATOM   57    O  O   . PRO A  1 12  ? -1.556  -12.448 17.331  1.00 13.29 ? 11  PRO A O   1 
ATOM   58    C  CB  . PRO A  1 12  ? -0.221  -12.358 14.340  1.00 12.97 ? 11  PRO A CB  1 
ATOM   59    C  CG  . PRO A  1 12  ? -0.191  -10.889 14.632  1.00 13.05 ? 11  PRO A CG  1 
ATOM   60    C  CD  . PRO A  1 12  ? -1.632  -10.459 14.533  1.00 13.08 ? 11  PRO A CD  1 
ATOM   61    N  N   . GLY A  1 13  ? -0.573  -14.338 16.645  1.00 14.36 ? 12  GLY A N   1 
ATOM   62    C  CA  . GLY A  1 13  ? -0.168  -14.748 17.951  1.00 15.02 ? 12  GLY A CA  1 
ATOM   63    C  C   . GLY A  1 13  ? 1.270   -14.395 18.249  1.00 15.76 ? 12  GLY A C   1 
ATOM   64    O  O   . GLY A  1 13  ? 1.915   -13.612 17.531  1.00 15.82 ? 12  GLY A O   1 
ATOM   65    N  N   . ASP A  1 14  ? 1.771   -14.989 19.331  1.00 16.06 ? 13  ASP A N   1 
ATOM   66    C  CA  . ASP A  1 14  ? 3.173   -14.846 19.730  1.00 17.28 ? 13  ASP A CA  1 
ATOM   67    C  C   . ASP A  1 14  ? 4.083   -15.322 18.593  1.00 17.05 ? 13  ASP A C   1 
ATOM   68    O  O   . ASP A  1 14  ? 3.832   -16.343 17.959  1.00 17.49 ? 13  ASP A O   1 
ATOM   69    C  CB  . ASP A  1 14  ? 3.394   -15.648 21.032  1.00 18.47 ? 13  ASP A CB  1 
ATOM   70    C  CG  . ASP A  1 14  ? 4.583   -15.172 21.859  1.00 20.69 ? 13  ASP A CG  1 
ATOM   71    O  OD1 . ASP A  1 14  ? 5.360   -14.260 21.449  1.00 19.72 ? 13  ASP A OD1 1 
ATOM   72    O  OD2 . ASP A  1 14  ? 4.730   -15.738 22.982  1.00 22.52 ? 13  ASP A OD2 1 
ATOM   73    N  N   . LEU A  1 15  ? 5.147   -14.567 18.333  1.00 16.90 ? 14  LEU A N   1 
ATOM   74    C  CA  . LEU A  1 15  ? 6.071   -14.838 17.224  1.00 17.68 ? 14  LEU A CA  1 
ATOM   75    C  C   . LEU A  1 15  ? 5.437   -14.629 15.846  1.00 16.22 ? 14  LEU A C   1 
ATOM   76    O  O   . LEU A  1 15  ? 6.036   -14.993 14.844  1.00 15.90 ? 14  LEU A O   1 
ATOM   77    C  CB  . LEU A  1 15  ? 6.653   -16.259 17.287  1.00 19.09 ? 14  LEU A CB  1 
ATOM   78    C  CG  . LEU A  1 15  ? 7.226   -16.775 18.610  1.00 22.08 ? 14  LEU A CG  1 
ATOM   79    C  CD1 . LEU A  1 15  ? 7.781   -18.176 18.405  1.00 22.51 ? 14  LEU A CD1 1 
ATOM   80    C  CD2 . LEU A  1 15  ? 8.303   -15.844 19.105  1.00 22.72 ? 14  LEU A CD2 1 
ATOM   81    N  N   . GLY A  1 16  ? 4.244   -14.047 15.811  1.00 14.73 ? 15  GLY A N   1 
ATOM   82    C  CA  . GLY A  1 16  ? 3.381   -14.155 14.653  1.00 14.47 ? 15  GLY A CA  1 
ATOM   83    C  C   . GLY A  1 16  ? 3.432   -13.010 13.658  1.00 14.58 ? 15  GLY A C   1 
ATOM   84    O  O   . GLY A  1 16  ? 2.596   -12.945 12.752  1.00 14.12 ? 15  GLY A O   1 
ATOM   85    N  N   . ASN A  1 17  ? 4.411   -12.113 13.801  1.00 13.59 ? 16  ASN A N   1 
ATOM   86    C  CA  . ASN A  1 17  ? 4.686   -11.142 12.748  1.00 13.62 ? 16  ASN A CA  1 
ATOM   87    C  C   . ASN A  1 17  ? 6.146   -10.759 12.754  1.00 14.28 ? 16  ASN A C   1 
ATOM   88    O  O   . ASN A  1 17  ? 6.852   -10.939 13.762  1.00 13.50 ? 16  ASN A O   1 
ATOM   89    C  CB  . ASN A  1 17  ? 3.761   -9.920  12.800  1.00 13.64 ? 16  ASN A CB  1 
ATOM   90    C  CG  . ASN A  1 17  ? 3.703   -9.248  14.163  1.00 13.87 ? 16  ASN A CG  1 
ATOM   91    O  OD1 . ASN A  1 17  ? 2.671   -9.305  14.863  1.00 14.37 ? 16  ASN A OD1 1 
ATOM   92    N  ND2 . ASN A  1 17  ? 4.784   -8.599  14.551  1.00 13.86 ? 16  ASN A ND2 1 
ATOM   93    N  N   . GLN A  1 18  ? 6.591   -10.232 11.627  1.00 14.81 ? 17  GLN A N   1 
ATOM   94    C  CA  . GLN A  1 18  ? 7.958   -9.768  11.528  1.00 15.06 ? 17  GLN A CA  1 
ATOM   95    C  C   . GLN A  1 18  ? 8.239   -8.666  12.556  1.00 15.23 ? 17  GLN A C   1 
ATOM   96    O  O   . GLN A  1 18  ? 7.345   -7.913  12.921  1.00 13.79 ? 17  GLN A O   1 
ATOM   97    C  CB  . GLN A  1 18  ? 8.224   -9.210  10.137  1.00 16.23 ? 17  GLN A CB  1 
ATOM   98    C  CG  . GLN A  1 18  ? 8.124   -10.228 9.023   1.00 17.03 ? 17  GLN A CG  1 
ATOM   99    C  CD  . GLN A  1 18  ? 8.356   -9.615  7.644   1.00 18.92 ? 17  GLN A CD  1 
ATOM   100   O  OE1 . GLN A  1 18  ? 8.943   -8.528  7.511   1.00 17.87 ? 17  GLN A OE1 1 
ATOM   101   N  NE2 . GLN A  1 18  ? 7.890   -10.302 6.628   1.00 17.95 ? 17  GLN A NE2 1 
ATOM   102   N  N   . LEU A  1 19  ? 9.512   -8.565  12.968  1.00 15.63 ? 18  LEU A N   1 
ATOM   103   C  CA  . LEU A  1 19  ? 10.028  -7.441  13.734  1.00 15.49 ? 18  LEU A CA  1 
ATOM   104   C  C   . LEU A  1 19  ? 11.328  -6.978  13.098  1.00 16.71 ? 18  LEU A C   1 
ATOM   105   O  O   . LEU A  1 19  ? 12.094  -7.790  12.578  1.00 16.23 ? 18  LEU A O   1 
ATOM   106   C  CB  . LEU A  1 19  ? 10.299  -7.809  15.200  1.00 16.12 ? 18  LEU A CB  1 
ATOM   107   C  CG  . LEU A  1 19  ? 9.118   -8.234  16.079  1.00 16.71 ? 18  LEU A CG  1 
ATOM   108   C  CD1 . LEU A  1 19  ? 9.609   -8.618  17.472  1.00 17.37 ? 18  LEU A CD1 1 
ATOM   109   C  CD2 . LEU A  1 19  ? 8.073   -7.147  16.178  1.00 16.77 ? 18  LEU A CD2 1 
ATOM   110   N  N   . GLU A  1 20  ? 11.561  -5.673  13.141  1.00 16.80 ? 19  GLU A N   1 
ATOM   111   C  CA  . GLU A  1 20  ? 12.756  -5.068  12.558  1.00 18.51 ? 19  GLU A CA  1 
ATOM   112   C  C   . GLU A  1 20  ? 13.526  -4.311  13.632  1.00 18.25 ? 19  GLU A C   1 
ATOM   113   O  O   . GLU A  1 20  ? 12.905  -3.778  14.557  1.00 18.28 ? 19  GLU A O   1 
ATOM   114   C  CB  . GLU A  1 20  ? 12.355  -4.083  11.455  1.00 20.17 ? 19  GLU A CB  1 
ATOM   115   C  CG  . GLU A  1 20  ? 11.842  -4.770  10.218  1.00 22.34 ? 19  GLU A CG  1 
ATOM   116   C  CD  . GLU A  1 20  ? 11.305  -3.852  9.147   1.00 23.99 ? 19  GLU A CD  1 
ATOM   117   O  OE1 . GLU A  1 20  ? 11.125  -2.638  9.394   1.00 24.74 ? 19  GLU A OE1 1 
ATOM   118   O  OE2 . GLU A  1 20  ? 11.032  -4.383  8.044   1.00 25.98 ? 19  GLU A OE2 1 
ATOM   119   N  N   . ALA A  1 21  ? 14.851  -4.249  13.501  1.00 17.32 ? 20  ALA A N   1 
ATOM   120   C  CA  . ALA A  1 21  ? 15.665  -3.542  14.460  1.00 17.56 ? 20  ALA A CA  1 
ATOM   121   C  C   . ALA A  1 21  ? 16.643  -2.597  13.768  1.00 18.92 ? 20  ALA A C   1 
ATOM   122   O  O   . ALA A  1 21  ? 17.052  -2.829  12.630  1.00 18.66 ? 20  ALA A O   1 
ATOM   123   C  CB  . ALA A  1 21  ? 16.416  -4.506  15.345  1.00 17.95 ? 20  ALA A CB  1 
ATOM   124   N  N   . LYS A  1 22  ? 17.005  -1.539  14.477  1.00 19.60 ? 21  LYS A N   1 
ATOM   125   C  CA  . LYS A  1 22  ? 18.070  -0.627  14.060  1.00 21.08 ? 21  LYS A CA  1 
ATOM   126   C  C   . LYS A  1 22  ? 18.989  -0.417  15.232  1.00 21.35 ? 21  LYS A C   1 
ATOM   127   O  O   . LYS A  1 22  ? 18.540  -0.306  16.369  1.00 20.43 ? 21  LYS A O   1 
ATOM   128   C  CB  . LYS A  1 22  ? 17.481  0.702   13.568  1.00 23.04 ? 21  LYS A CB  1 
ATOM   129   C  CG  . LYS A  1 22  ? 18.522  1.714   13.109  1.00 25.93 ? 21  LYS A CG  1 
ATOM   130   C  CD  . LYS A  1 22  ? 17.869  2.974   12.561  1.00 29.59 ? 21  LYS A CD  1 
ATOM   131   C  CE  . LYS A  1 22  ? 18.921  3.920   12.004  1.00 35.74 ? 21  LYS A CE  1 
ATOM   132   N  NZ  . LYS A  1 22  ? 18.283  5.009   11.198  1.00 39.15 ? 21  LYS A NZ  1 
ATOM   133   N  N   . LEU A  1 23  ? 20.299  -0.397  14.973  1.00 21.63 ? 22  LEU A N   1 
ATOM   134   C  CA  . LEU A  1 23  ? 21.276  -0.465  16.034  1.00 21.76 ? 22  LEU A CA  1 
ATOM   135   C  C   . LEU A  1 23  ? 22.218  0.730   16.055  1.00 22.81 ? 22  LEU A C   1 
ATOM   136   O  O   . LEU A  1 23  ? 22.643  1.206   15.014  1.00 22.38 ? 22  LEU A O   1 
ATOM   137   C  CB  . LEU A  1 23  ? 22.137  -1.728  15.881  1.00 22.25 ? 22  LEU A CB  1 
ATOM   138   C  CG  . LEU A  1 23  ? 21.425  -3.048  15.666  1.00 21.96 ? 22  LEU A CG  1 
ATOM   139   C  CD1 . LEU A  1 23  ? 22.439  -4.155  15.456  1.00 22.73 ? 22  LEU A CD1 1 
ATOM   140   C  CD2 . LEU A  1 23  ? 20.476  -3.365  16.817  1.00 21.72 ? 22  LEU A CD2 1 
ATOM   141   N  N   . ASP A  1 24  ? 22.548  1.173   17.262  1.00 24.31 ? 23  ASP A N   1 
ATOM   142   C  CA  . ASP A  1 24  ? 23.721  2.053   17.527  1.00 26.48 ? 23  ASP A CA  1 
ATOM   143   C  C   . ASP A  1 24  ? 24.189  1.764   18.962  1.00 26.63 ? 23  ASP A C   1 
ATOM   144   O  O   . ASP A  1 24  ? 24.000  2.565   19.880  1.00 26.10 ? 23  ASP A O   1 
ATOM   145   C  CB  . ASP A  1 24  ? 23.346  3.522   17.347  1.00 29.19 ? 23  ASP A CB  1 
ATOM   146   C  CG  . ASP A  1 24  ? 24.557  4.455   17.381  1.00 33.78 ? 23  ASP A CG  1 
ATOM   147   O  OD1 . ASP A  1 24  ? 25.718  3.976   17.440  1.00 35.05 ? 23  ASP A OD1 1 
ATOM   148   O  OD2 . ASP A  1 24  ? 24.339  5.688   17.338  1.00 39.17 ? 23  ASP A OD2 1 
ATOM   149   N  N   . LYS A  1 25  ? 24.763  0.585   19.153  1.00 25.59 ? 24  LYS A N   1 
ATOM   150   C  CA  . LYS A  1 25  ? 25.007  0.037   20.475  1.00 26.49 ? 24  LYS A CA  1 
ATOM   151   C  C   . LYS A  1 25  ? 26.362  0.483   20.998  1.00 28.05 ? 24  LYS A C   1 
ATOM   152   O  O   . LYS A  1 25  ? 27.305  0.569   20.229  1.00 27.38 ? 24  LYS A O   1 
ATOM   153   C  CB  . LYS A  1 25  ? 24.993  -1.493  20.418  1.00 26.29 ? 24  LYS A CB  1 
ATOM   154   C  CG  . LYS A  1 25  ? 23.669  -2.083  19.943  1.00 25.93 ? 24  LYS A CG  1 
ATOM   155   C  CD  . LYS A  1 25  ? 23.842  -3.508  19.421  1.00 26.58 ? 24  LYS A CD  1 
ATOM   156   C  CE  . LYS A  1 25  ? 24.157  -4.517  20.517  1.00 26.06 ? 24  LYS A CE  1 
ATOM   157   N  NZ  . LYS A  1 25  ? 23.013  -4.848  21.398  1.00 25.34 ? 24  LYS A NZ  1 
ATOM   158   N  N   . PRO A  1 26  ? 26.460  0.748   22.303  1.00 30.25 ? 25  PRO A N   1 
ATOM   159   C  CA  . PRO A  1 26  ? 27.773  1.122   22.851  1.00 32.47 ? 25  PRO A CA  1 
ATOM   160   C  C   . PRO A  1 26  ? 28.762  -0.048  22.884  1.00 32.66 ? 25  PRO A C   1 
ATOM   161   O  O   . PRO A  1 26  ? 29.962  0.171   22.747  1.00 33.25 ? 25  PRO A O   1 
ATOM   162   C  CB  . PRO A  1 26  ? 27.447  1.614   24.271  1.00 32.75 ? 25  PRO A CB  1 
ATOM   163   C  CG  . PRO A  1 26  ? 26.118  1.084   24.589  1.00 32.47 ? 25  PRO A CG  1 
ATOM   164   C  CD  . PRO A  1 26  ? 25.376  0.899   23.290  1.00 30.85 ? 25  PRO A CD  1 
ATOM   165   N  N   . THR A  1 27  ? 28.257  -1.259  23.114  1.00 31.44 ? 26  THR A N   1 
ATOM   166   C  CA  . THR A  1 27  ? 29.080  -2.457  23.187  1.00 33.60 ? 26  THR A CA  1 
ATOM   167   C  C   . THR A  1 27  ? 28.346  -3.634  22.564  1.00 31.86 ? 26  THR A C   1 
ATOM   168   O  O   . THR A  1 27  ? 27.111  -3.627  22.465  1.00 28.81 ? 26  THR A O   1 
ATOM   169   C  CB  . THR A  1 27  ? 29.430  -2.842  24.654  1.00 36.07 ? 26  THR A CB  1 
ATOM   170   O  OG1 . THR A  1 27  ? 28.233  -3.133  25.378  1.00 39.27 ? 26  THR A OG1 1 
ATOM   171   C  CG2 . THR A  1 27  ? 30.158  -1.722  25.360  1.00 38.96 ? 26  THR A CG2 1 
ATOM   172   N  N   . VAL A  1 28  ? 29.102  -4.663  22.183  1.00 30.74 ? 27  VAL A N   1 
ATOM   173   C  CA  . VAL A  1 28  ? 28.498  -5.923  21.705  1.00 29.83 ? 27  VAL A CA  1 
ATOM   174   C  C   . VAL A  1 28  ? 29.071  -7.102  22.483  1.00 28.66 ? 27  VAL A C   1 
ATOM   175   O  O   . VAL A  1 28  ? 30.147  -7.004  23.062  1.00 27.62 ? 27  VAL A O   1 
ATOM   176   C  CB  . VAL A  1 28  ? 28.722  -6.145  20.194  1.00 30.39 ? 27  VAL A CB  1 
ATOM   177   C  CG1 . VAL A  1 28  ? 27.841  -5.215  19.375  1.00 30.74 ? 27  VAL A CG1 1 
ATOM   178   C  CG2 . VAL A  1 28  ? 30.201  -5.967  19.821  1.00 31.47 ? 27  VAL A CG2 1 
ATOM   179   N  N   . VAL A  1 29  ? 28.351  -8.217  22.497  1.00 26.76 ? 28  VAL A N   1 
ATOM   180   C  CA  . VAL A  1 29  ? 28.788  -9.381  23.268  1.00 27.96 ? 28  VAL A CA  1 
ATOM   181   C  C   . VAL A  1 29  ? 29.864  -10.225 22.568  1.00 27.91 ? 28  VAL A C   1 
ATOM   182   O  O   . VAL A  1 29  ? 30.608  -10.941 23.239  1.00 28.22 ? 28  VAL A O   1 
ATOM   183   C  CB  . VAL A  1 29  ? 27.602  -10.283 23.701  1.00 27.58 ? 28  VAL A CB  1 
ATOM   184   C  CG1 . VAL A  1 29  ? 26.625  -9.484  24.551  1.00 28.03 ? 28  VAL A CG1 1 
ATOM   185   C  CG2 . VAL A  1 29  ? 26.903  -10.900 22.510  1.00 27.58 ? 28  VAL A CG2 1 
ATOM   186   N  N   . HIS A  1 30  ? 29.925  -10.159 21.236  1.00 28.22 ? 29  HIS A N   1 
ATOM   187   C  CA  . HIS A  1 30  ? 30.993  -10.781 20.447  1.00 29.78 ? 29  HIS A CA  1 
ATOM   188   C  C   . HIS A  1 30  ? 31.391  -9.813  19.355  1.00 29.06 ? 29  HIS A C   1 
ATOM   189   O  O   . HIS A  1 30  ? 30.560  -9.035  18.854  1.00 26.72 ? 29  HIS A O   1 
ATOM   190   C  CB  . HIS A  1 30  ? 30.554  -12.096 19.758  1.00 30.09 ? 29  HIS A CB  1 
ATOM   191   C  CG  . HIS A  1 30  ? 30.039  -13.145 20.690  1.00 29.99 ? 29  HIS A CG  1 
ATOM   192   N  ND1 . HIS A  1 30  ? 30.754  -13.601 21.773  1.00 30.62 ? 29  HIS A ND1 1 
ATOM   193   C  CD2 . HIS A  1 30  ? 28.862  -13.818 20.707  1.00 30.47 ? 29  HIS A CD2 1 
ATOM   194   C  CE1 . HIS A  1 30  ? 30.045  -14.508 22.427  1.00 30.94 ? 29  HIS A CE1 1 
ATOM   195   N  NE2 . HIS A  1 30  ? 28.890  -14.659 21.798  1.00 31.60 ? 29  HIS A NE2 1 
ATOM   196   N  N   . TYR A  1 31  ? 32.640  -9.904  18.919  1.00 29.29 ? 30  TYR A N   1 
ATOM   197   C  CA  . TYR A  1 31  ? 33.112  -9.083  17.800  1.00 30.28 ? 30  TYR A CA  1 
ATOM   198   C  C   . TYR A  1 31  ? 32.382  -9.319  16.488  1.00 31.34 ? 30  TYR A C   1 
ATOM   199   O  O   . TYR A  1 31  ? 32.300  -8.424  15.666  1.00 32.36 ? 30  TYR A O   1 
ATOM   200   C  CB  . TYR A  1 31  ? 34.625  -9.212  17.629  1.00 30.90 ? 30  TYR A CB  1 
ATOM   201   C  CG  . TYR A  1 31  ? 35.298  -8.379  18.679  1.00 31.05 ? 30  TYR A CG  1 
ATOM   202   C  CD1 . TYR A  1 31  ? 35.498  -7.014  18.495  1.00 31.43 ? 30  TYR A CD1 1 
ATOM   203   C  CD2 . TYR A  1 31  ? 35.696  -8.952  19.873  1.00 31.95 ? 30  TYR A CD2 1 
ATOM   204   C  CE1 . TYR A  1 31  ? 36.128  -6.251  19.465  1.00 33.07 ? 30  TYR A CE1 1 
ATOM   205   C  CE2 . TYR A  1 31  ? 36.331  -8.206  20.849  1.00 33.26 ? 30  TYR A CE2 1 
ATOM   206   C  CZ  . TYR A  1 31  ? 36.538  -6.850  20.646  1.00 33.85 ? 30  TYR A CZ  1 
ATOM   207   O  OH  . TYR A  1 31  ? 37.202  -6.122  21.607  1.00 35.76 ? 30  TYR A OH  1 
ATOM   208   N  N   . LEU A  1 32  ? 31.816  -10.497 16.300  1.00 32.00 ? 31  LEU A N   1 
ATOM   209   C  CA  . LEU A  1 32  ? 31.055  -10.740 15.076  1.00 34.95 ? 31  LEU A CA  1 
ATOM   210   C  C   . LEU A  1 32  ? 29.644  -10.101 15.084  1.00 33.32 ? 31  LEU A C   1 
ATOM   211   O  O   . LEU A  1 32  ? 28.967  -10.118 14.066  1.00 33.24 ? 31  LEU A O   1 
ATOM   212   C  CB  . LEU A  1 32  ? 31.004  -12.239 14.745  1.00 38.94 ? 31  LEU A CB  1 
ATOM   213   C  CG  . LEU A  1 32  ? 30.562  -13.240 15.814  1.00 42.35 ? 31  LEU A CG  1 
ATOM   214   C  CD1 . LEU A  1 32  ? 29.083  -13.117 16.087  1.00 43.69 ? 31  LEU A CD1 1 
ATOM   215   C  CD2 . LEU A  1 32  ? 30.914  -14.660 15.395  1.00 45.75 ? 31  LEU A CD2 1 
ATOM   216   N  N   . CYS A  1 33  ? 29.224  -9.510  16.199  1.00 31.80 ? 32  CYS A N   1 
ATOM   217   C  CA  . CYS A  1 33  ? 27.934  -8.789  16.261  1.00 31.10 ? 32  CYS A CA  1 
ATOM   218   C  C   . CYS A  1 33  ? 28.082  -7.372  15.689  1.00 30.81 ? 32  CYS A C   1 
ATOM   219   O  O   . CYS A  1 33  ? 29.040  -6.670  16.028  1.00 30.48 ? 32  CYS A O   1 
ATOM   220   C  CB  . CYS A  1 33  ? 27.435  -8.684  17.717  1.00 31.08 ? 32  CYS A CB  1 
ATOM   221   S  SG  . CYS A  1 33  ? 27.317  -10.208 18.733  1.00 33.11 ? 32  CYS A SG  1 
ATOM   222   N  N   . SER A  1 34  ? 27.140  -6.916  14.869  1.00 28.57 ? 33  SER A N   1 
ATOM   223   C  CA  . SER A  1 34  ? 27.155  -5.511  14.410  1.00 30.32 ? 33  SER A CA  1 
ATOM   224   C  C   . SER A  1 34  ? 26.822  -4.545  15.560  1.00 29.38 ? 33  SER A C   1 
ATOM   225   O  O   . SER A  1 34  ? 25.862  -4.767  16.323  1.00 26.99 ? 33  SER A O   1 
ATOM   226   C  CB  . SER A  1 34  ? 26.154  -5.277  13.282  1.00 32.08 ? 33  SER A CB  1 
ATOM   227   O  OG  . SER A  1 34  ? 26.507  -6.009  12.123  1.00 35.41 ? 33  SER A OG  1 
ATOM   228   N  N   . LYS A  1 35  ? 27.598  -3.471  15.662  1.00 28.55 ? 34  LYS A N   1 
ATOM   229   C  CA  . LYS A  1 35  ? 27.322  -2.385  16.609  1.00 30.34 ? 34  LYS A CA  1 
ATOM   230   C  C   . LYS A  1 35  ? 26.311  -1.384  16.096  1.00 29.21 ? 34  LYS A C   1 
ATOM   231   O  O   . LYS A  1 35  ? 25.513  -0.826  16.859  1.00 28.21 ? 34  LYS A O   1 
ATOM   232   C  CB  . LYS A  1 35  ? 28.591  -1.591  16.895  1.00 33.51 ? 34  LYS A CB  1 
ATOM   233   C  CG  . LYS A  1 35  ? 29.256  -1.922  18.195  1.00 36.73 ? 34  LYS A CG  1 
ATOM   234   C  CD  . LYS A  1 35  ? 30.428  -0.986  18.432  1.00 40.12 ? 34  LYS A CD  1 
ATOM   235   C  CE  . LYS A  1 35  ? 30.712  -0.907  19.908  1.00 44.34 ? 34  LYS A CE  1 
ATOM   236   N  NZ  . LYS A  1 35  ? 31.961  -0.140  20.175  1.00 47.35 ? 34  LYS A NZ  1 
ATOM   237   N  N   . LYS A  1 36  ? 26.347  -1.139  14.795  1.00 29.61 ? 35  LYS A N   1 
ATOM   238   C  CA  . LYS A  1 36  ? 25.599  -0.036  14.210  1.00 31.58 ? 35  LYS A CA  1 
ATOM   239   C  C   . LYS A  1 36  ? 25.041  -0.455  12.861  1.00 30.87 ? 35  LYS A C   1 
ATOM   240   O  O   . LYS A  1 36  ? 25.729  -1.115  12.087  1.00 32.11 ? 35  LYS A O   1 
ATOM   241   C  CB  . LYS A  1 36  ? 26.546  1.152   14.039  1.00 35.52 ? 35  LYS A CB  1 
ATOM   242   C  CG  . LYS A  1 36  ? 25.875  2.462   13.665  1.00 38.73 ? 35  LYS A CG  1 
ATOM   243   C  CD  . LYS A  1 36  ? 26.917  3.555   13.551  1.00 43.94 ? 35  LYS A CD  1 
ATOM   244   C  CE  . LYS A  1 36  ? 26.363  4.818   12.941  1.00 47.71 ? 35  LYS A CE  1 
ATOM   245   N  NZ  . LYS A  1 36  ? 25.282  5.418   13.763  1.00 49.89 ? 35  LYS A NZ  1 
ATOM   246   N  N   . THR A  1 37  ? 23.805  -0.074  12.580  1.00 29.30 ? 36  THR A N   1 
ATOM   247   C  CA  . THR A  1 37  ? 23.234  -0.227  11.251  1.00 29.67 ? 36  THR A CA  1 
ATOM   248   C  C   . THR A  1 37  ? 22.669  1.126   10.797  1.00 31.35 ? 36  THR A C   1 
ATOM   249   O  O   . THR A  1 37  ? 22.154  1.897   11.604  1.00 30.70 ? 36  THR A O   1 
ATOM   250   C  CB  . THR A  1 37  ? 22.121  -1.297  11.224  1.00 28.38 ? 36  THR A CB  1 
ATOM   251   O  OG1 . THR A  1 37  ? 21.016  -0.881  12.040  1.00 25.49 ? 36  THR A OG1 1 
ATOM   252   C  CG2 . THR A  1 37  ? 22.661  -2.647  11.742  1.00 28.39 ? 36  THR A CG2 1 
ATOM   253   N  N   . GLU A  1 38  ? 22.736  1.400   9.501   1.00 33.81 ? 37  GLU A N   1 
ATOM   254   C  CA  . GLU A  1 38  ? 22.191  2.652   8.960   1.00 37.22 ? 37  GLU A CA  1 
ATOM   255   C  C   . GLU A  1 38  ? 20.679  2.609   8.776   1.00 34.11 ? 37  GLU A C   1 
ATOM   256   O  O   . GLU A  1 38  ? 20.030  3.643   8.728   1.00 33.76 ? 37  GLU A O   1 
ATOM   257   C  CB  . GLU A  1 38  ? 22.879  2.999   7.635   1.00 41.95 ? 37  GLU A CB  1 
ATOM   258   C  CG  . GLU A  1 38  ? 24.397  3.154   7.770   1.00 49.74 ? 37  GLU A CG  1 
ATOM   259   C  CD  . GLU A  1 38  ? 24.811  4.191   8.815   1.00 57.76 ? 37  GLU A CD  1 
ATOM   260   O  OE1 . GLU A  1 38  ? 24.141  5.250   8.916   1.00 65.75 ? 37  GLU A OE1 1 
ATOM   261   O  OE2 . GLU A  1 38  ? 25.814  3.955   9.531   1.00 64.54 ? 37  GLU A OE2 1 
ATOM   262   N  N   . SER A  1 39  ? 20.113  1.412   8.676   1.00 30.83 ? 38  SER A N   1 
ATOM   263   C  CA  . SER A  1 39  ? 18.678  1.270   8.548   1.00 29.74 ? 38  SER A CA  1 
ATOM   264   C  C   . SER A  1 39  ? 18.199  0.077   9.369   1.00 26.15 ? 38  SER A C   1 
ATOM   265   O  O   . SER A  1 39  ? 18.990  -0.612  10.005  1.00 25.57 ? 38  SER A O   1 
ATOM   266   C  CB  . SER A  1 39  ? 18.305  1.094   7.077   1.00 32.72 ? 38  SER A CB  1 
ATOM   267   O  OG  . SER A  1 39  ? 18.964  -0.043  6.564   1.00 38.15 ? 38  SER A OG  1 
ATOM   268   N  N   . TYR A  1 40  ? 16.901  -0.149  9.342   1.00 23.04 ? 39  TYR A N   1 
ATOM   269   C  CA  . TYR A  1 40  ? 16.311  -1.299  10.000  1.00 22.19 ? 39  TYR A CA  1 
ATOM   270   C  C   . TYR A  1 40  ? 16.618  -2.579  9.217   1.00 23.19 ? 39  TYR A C   1 
ATOM   271   O  O   . TYR A  1 40  ? 16.755  -2.531  7.997   1.00 24.03 ? 39  TYR A O   1 
ATOM   272   C  CB  . TYR A  1 40  ? 14.809  -1.104  10.134  1.00 21.53 ? 39  TYR A CB  1 
ATOM   273   C  CG  . TYR A  1 40  ? 14.434  -0.107  11.220  1.00 20.53 ? 39  TYR A CG  1 
ATOM   274   C  CD1 . TYR A  1 40  ? 14.387  1.253   10.954  1.00 22.61 ? 39  TYR A CD1 1 
ATOM   275   C  CD2 . TYR A  1 40  ? 14.139  -0.531  12.509  1.00 19.86 ? 39  TYR A CD2 1 
ATOM   276   C  CE1 . TYR A  1 40  ? 14.055  2.173   11.945  1.00 21.75 ? 39  TYR A CE1 1 
ATOM   277   C  CE2 . TYR A  1 40  ? 13.810  0.370   13.503  1.00 20.24 ? 39  TYR A CE2 1 
ATOM   278   C  CZ  . TYR A  1 40  ? 13.781  1.728   13.215  1.00 21.23 ? 39  TYR A CZ  1 
ATOM   279   O  OH  . TYR A  1 40  ? 13.497  2.630   14.206  1.00 21.39 ? 39  TYR A OH  1 
ATOM   280   N  N   . PHE A  1 41  ? 16.779  -3.694  9.929   1.00 21.34 ? 40  PHE A N   1 
ATOM   281   C  CA  . PHE A  1 41  ? 16.935  -5.015  9.317   1.00 21.83 ? 40  PHE A CA  1 
ATOM   282   C  C   . PHE A  1 41  ? 15.967  -5.956  10.035  1.00 21.37 ? 40  PHE A C   1 
ATOM   283   O  O   . PHE A  1 41  ? 15.512  -5.664  11.147  1.00 19.98 ? 40  PHE A O   1 
ATOM   284   C  CB  . PHE A  1 41  ? 18.366  -5.545  9.424   1.00 22.75 ? 40  PHE A CB  1 
ATOM   285   C  CG  . PHE A  1 41  ? 18.821  -5.828  10.835  1.00 23.70 ? 40  PHE A CG  1 
ATOM   286   C  CD1 . PHE A  1 41  ? 19.304  -4.800  11.636  1.00 24.82 ? 40  PHE A CD1 1 
ATOM   287   C  CD2 . PHE A  1 41  ? 18.794  -7.121  11.358  1.00 24.64 ? 40  PHE A CD2 1 
ATOM   288   C  CE1 . PHE A  1 41  ? 19.731  -5.058  12.931  1.00 25.11 ? 40  PHE A CE1 1 
ATOM   289   C  CE2 . PHE A  1 41  ? 19.207  -7.384  12.667  1.00 25.20 ? 40  PHE A CE2 1 
ATOM   290   C  CZ  . PHE A  1 41  ? 19.669  -6.346  13.455  1.00 25.93 ? 40  PHE A CZ  1 
ATOM   291   N  N   . THR A  1 42  ? 15.641  -7.068  9.399   1.00 19.68 ? 41  THR A N   1 
ATOM   292   C  CA  . THR A  1 42  ? 14.709  -8.020  10.002  1.00 19.56 ? 41  THR A CA  1 
ATOM   293   C  C   . THR A  1 42  ? 15.366  -8.810  11.116  1.00 19.59 ? 41  THR A C   1 
ATOM   294   O  O   . THR A  1 42  ? 16.350  -9.524  10.891  1.00 20.12 ? 41  THR A O   1 
ATOM   295   C  CB  . THR A  1 42  ? 14.162  -8.963  8.919   1.00 20.37 ? 41  THR A CB  1 
ATOM   296   O  OG1 . THR A  1 42  ? 13.509  -8.169  7.925   1.00 20.54 ? 41  THR A OG1 1 
ATOM   297   C  CG2 . THR A  1 42  ? 13.177  -9.974  9.528   1.00 20.19 ? 41  THR A CG2 1 
ATOM   298   N  N   . ILE A  1 43  ? 14.840  -8.667  12.328  1.00 18.76 ? 42  ILE A N   1 
ATOM   299   C  CA  . ILE A  1 43  ? 15.334  -9.408  13.481  1.00 19.62 ? 42  ILE A CA  1 
ATOM   300   C  C   . ILE A  1 43  ? 14.498  -10.660 13.804  1.00 18.98 ? 42  ILE A C   1 
ATOM   301   O  O   . ILE A  1 43  ? 14.981  -11.604 14.419  1.00 20.11 ? 42  ILE A O   1 
ATOM   302   C  CB  . ILE A  1 43  ? 15.524  -8.466  14.700  1.00 20.78 ? 42  ILE A CB  1 
ATOM   303   C  CG1 . ILE A  1 43  ? 16.446  -9.121  15.717  1.00 22.67 ? 42  ILE A CG1 1 
ATOM   304   C  CG2 . ILE A  1 43  ? 14.194  -8.025  15.313  1.00 19.73 ? 42  ILE A CG2 1 
ATOM   305   C  CD1 . ILE A  1 43  ? 16.941  -8.163  16.791  1.00 25.22 ? 42  ILE A CD1 1 
ATOM   306   N  N   . TRP A  1 44  ? 13.265  -10.685 13.329  1.00 17.95 ? 43  TRP A N   1 
ATOM   307   C  CA  . TRP A  1 44  ? 12.426  -11.902 13.344  1.00 16.97 ? 43  TRP A CA  1 
ATOM   308   C  C   . TRP A  1 44  ? 11.573  -11.882 12.065  1.00 16.90 ? 43  TRP A C   1 
ATOM   309   O  O   . TRP A  1 44  ? 10.898  -10.875 11.824  1.00 15.01 ? 43  TRP A O   1 
ATOM   310   C  CB  . TRP A  1 44  ? 11.486  -11.900 14.555  1.00 16.82 ? 43  TRP A CB  1 
ATOM   311   C  CG  . TRP A  1 44  ? 10.625  -13.121 14.621  1.00 16.05 ? 43  TRP A CG  1 
ATOM   312   C  CD1 . TRP A  1 44  ? 9.309   -13.231 14.250  1.00 16.68 ? 43  TRP A CD1 1 
ATOM   313   C  CD2 . TRP A  1 44  ? 11.034  -14.408 15.051  1.00 16.58 ? 43  TRP A CD2 1 
ATOM   314   N  NE1 . TRP A  1 44  ? 8.875   -14.519 14.460  1.00 16.47 ? 43  TRP A NE1 1 
ATOM   315   C  CE2 . TRP A  1 44  ? 9.920   -15.258 14.950  1.00 16.31 ? 43  TRP A CE2 1 
ATOM   316   C  CE3 . TRP A  1 44  ? 12.252  -14.931 15.543  1.00 17.38 ? 43  TRP A CE3 1 
ATOM   317   C  CZ2 . TRP A  1 44  ? 9.975   -16.599 15.319  1.00 17.03 ? 43  TRP A CZ2 1 
ATOM   318   C  CZ3 . TRP A  1 44  ? 12.310  -16.262 15.885  1.00 17.72 ? 43  TRP A CZ3 1 
ATOM   319   C  CH2 . TRP A  1 44  ? 11.181  -17.082 15.767  1.00 18.20 ? 43  TRP A CH2 1 
ATOM   320   N  N   . LEU A  1 45  ? 11.558  -12.932 11.252  1.00 17.15 ? 44  LEU A N   1 
ATOM   321   C  CA  . LEU A  1 45  ? 12.308  -14.180 11.412  1.00 19.54 ? 44  LEU A CA  1 
ATOM   322   C  C   . LEU A  1 45  ? 13.445  -14.214 10.404  1.00 20.85 ? 44  LEU A C   1 
ATOM   323   O  O   . LEU A  1 45  ? 13.225  -14.049 9.194   1.00 21.06 ? 44  LEU A O   1 
ATOM   324   C  CB  . LEU A  1 45  ? 11.375  -15.363 11.165  1.00 20.06 ? 44  LEU A CB  1 
ATOM   325   C  CG  . LEU A  1 45  ? 12.015  -16.761 11.061  1.00 21.35 ? 44  LEU A CG  1 
ATOM   326   C  CD1 . LEU A  1 45  ? 12.709  -17.099 12.368  1.00 22.52 ? 44  LEU A CD1 1 
ATOM   327   C  CD2 . LEU A  1 45  ? 10.928  -17.787 10.763  1.00 23.42 ? 44  LEU A CD2 1 
ATOM   328   N  N   . ASN A  1 46  ? 14.671  -14.360 10.891  1.00 23.22 ? 45  ASN A N   1 
ATOM   329   C  CA  . ASN A  1 46  ? 15.822  -14.559 10.019  1.00 26.92 ? 45  ASN A CA  1 
ATOM   330   C  C   . ASN A  1 46  ? 16.642  -15.661 10.617  1.00 29.01 ? 45  ASN A C   1 
ATOM   331   O  O   . ASN A  1 46  ? 17.229  -15.518 11.700  1.00 26.36 ? 45  ASN A O   1 
ATOM   332   C  CB  . ASN A  1 46  ? 16.653  -13.299 9.826   1.00 30.45 ? 45  ASN A CB  1 
ATOM   333   C  CG  . ASN A  1 46  ? 17.922  -13.552 8.993   1.00 32.35 ? 45  ASN A CG  1 
ATOM   334   O  OD1 . ASN A  1 46  ? 18.308  -14.689 8.726   1.00 34.35 ? 45  ASN A OD1 1 
ATOM   335   N  ND2 . ASN A  1 46  ? 18.565  -12.491 8.599   1.00 34.83 ? 45  ASN A ND2 1 
ATOM   336   N  N   . LEU A  1 47  ? 16.662  -16.786 9.906   1.00 32.35 ? 46  LEU A N   1 
ATOM   337   C  CA  . LEU A  1 47  ? 17.255  -18.024 10.423  1.00 35.98 ? 46  LEU A CA  1 
ATOM   338   C  C   . LEU A  1 47  ? 18.756  -17.905 10.652  1.00 33.86 ? 46  LEU A C   1 
ATOM   339   O  O   . LEU A  1 47  ? 19.302  -18.544 11.540  1.00 34.67 ? 46  LEU A O   1 
ATOM   340   C  CB  . LEU A  1 47  ? 16.995  -19.175 9.442   1.00 39.94 ? 46  LEU A CB  1 
ATOM   341   C  CG  . LEU A  1 47  ? 15.525  -19.543 9.245   1.00 41.85 ? 46  LEU A CG  1 
ATOM   342   C  CD1 . LEU A  1 47  ? 15.438  -20.580 8.134   1.00 44.55 ? 46  LEU A CD1 1 
ATOM   343   C  CD2 . LEU A  1 47  ? 14.942  -20.063 10.551  1.00 43.22 ? 46  LEU A CD2 1 
ATOM   344   N  N   . GLU A  1 48  ? 19.411  -17.062 9.881   1.00 35.23 ? 47  GLU A N   1 
ATOM   345   C  CA  . GLU A  1 48  ? 20.859  -16.923 10.012  1.00 37.89 ? 47  GLU A CA  1 
ATOM   346   C  C   . GLU A  1 48  ? 21.276  -16.261 11.339  1.00 35.88 ? 47  GLU A C   1 
ATOM   347   O  O   . GLU A  1 48  ? 22.421  -16.389 11.749  1.00 33.02 ? 47  GLU A O   1 
ATOM   348   C  CB  . GLU A  1 48  ? 21.407  -16.153 8.827   1.00 42.24 ? 47  GLU A CB  1 
ATOM   349   C  CG  . GLU A  1 48  ? 21.265  -16.957 7.543   1.00 47.84 ? 47  GLU A CG  1 
ATOM   350   C  CD  . GLU A  1 48  ? 21.811  -16.246 6.335   1.00 54.84 ? 47  GLU A CD  1 
ATOM   351   O  OE1 . GLU A  1 48  ? 21.835  -15.000 6.327   1.00 60.86 ? 47  GLU A OE1 1 
ATOM   352   O  OE2 . GLU A  1 48  ? 22.217  -16.945 5.384   1.00 63.08 ? 47  GLU A OE2 1 
ATOM   353   N  N   . LEU A  1 49  ? 20.340  -15.583 12.011  1.00 31.73 ? 48  LEU A N   1 
ATOM   354   C  CA  . LEU A  1 49  ? 20.640  -14.924 13.282  1.00 30.35 ? 48  LEU A CA  1 
ATOM   355   C  C   . LEU A  1 49  ? 20.563  -15.876 14.454  1.00 29.21 ? 48  LEU A C   1 
ATOM   356   O  O   . LEU A  1 49  ? 20.944  -15.514 15.571  1.00 27.12 ? 48  LEU A O   1 
ATOM   357   C  CB  . LEU A  1 49  ? 19.688  -13.736 13.508  1.00 28.72 ? 48  LEU A CB  1 
ATOM   358   C  CG  . LEU A  1 49  ? 19.598  -12.688 12.400  1.00 28.64 ? 48  LEU A CG  1 
ATOM   359   C  CD1 . LEU A  1 49  ? 18.620  -11.596 12.791  1.00 28.29 ? 48  LEU A CD1 1 
ATOM   360   C  CD2 . LEU A  1 49  ? 20.959  -12.086 12.047  1.00 30.61 ? 48  LEU A CD2 1 
ATOM   361   N  N   . LEU A  1 50  ? 20.046  -17.086 14.213  1.00 29.72 ? 49  LEU A N   1 
ATOM   362   C  CA  . LEU A  1 50  ? 19.800  -18.058 15.274  1.00 31.30 ? 49  LEU A CA  1 
ATOM   363   C  C   . LEU A  1 50  ? 20.859  -19.184 15.364  1.00 32.77 ? 49  LEU A C   1 
ATOM   364   O  O   . LEU A  1 50  ? 20.756  -20.073 16.209  1.00 35.45 ? 49  LEU A O   1 
ATOM   365   C  CB  . LEU A  1 50  ? 18.397  -18.658 15.091  1.00 32.30 ? 49  LEU A CB  1 
ATOM   366   C  CG  . LEU A  1 50  ? 17.272  -17.616 14.898  1.00 32.32 ? 49  LEU A CG  1 
ATOM   367   C  CD1 . LEU A  1 50  ? 15.920  -18.272 14.634  1.00 32.33 ? 49  LEU A CD1 1 
ATOM   368   C  CD2 . LEU A  1 50  ? 17.188  -16.721 16.129  1.00 31.37 ? 49  LEU A CD2 1 
ATOM   369   N  N   . LEU A  1 51  ? 21.882  -19.114 14.526  1.00 34.98 ? 50  LEU A N   1 
ATOM   370   C  CA  . LEU A  1 51  ? 22.957  -20.122 14.531  1.00 35.56 ? 50  LEU A CA  1 
ATOM   371   C  C   . LEU A  1 51  ? 23.793  -20.013 15.820  1.00 35.73 ? 50  LEU A C   1 
ATOM   372   O  O   . LEU A  1 51  ? 23.813  -18.959 16.456  1.00 32.44 ? 50  LEU A O   1 
ATOM   373   C  CB  . LEU A  1 51  ? 23.832  -19.927 13.308  1.00 39.17 ? 50  LEU A CB  1 
ATOM   374   C  CG  . LEU A  1 51  ? 23.151  -20.124 11.941  1.00 41.27 ? 50  LEU A CG  1 
ATOM   375   C  CD1 . LEU A  1 51  ? 23.971  -19.520 10.808  1.00 42.09 ? 50  LEU A CD1 1 
ATOM   376   C  CD2 . LEU A  1 51  ? 22.884  -21.598 11.672  1.00 43.19 ? 50  LEU A CD2 1 
ATOM   377   N  N   . PRO A  1 52  ? 24.506  -21.088 16.207  1.00 34.42 ? 51  PRO A N   1 
ATOM   378   C  CA  . PRO A  1 52  ? 25.372  -21.006 17.390  1.00 35.27 ? 51  PRO A CA  1 
ATOM   379   C  C   . PRO A  1 52  ? 26.297  -19.773 17.357  1.00 33.38 ? 51  PRO A C   1 
ATOM   380   O  O   . PRO A  1 52  ? 26.746  -19.381 16.284  1.00 32.16 ? 51  PRO A O   1 
ATOM   381   C  CB  . PRO A  1 52  ? 26.197  -22.300 17.321  1.00 36.96 ? 51  PRO A CB  1 
ATOM   382   C  CG  . PRO A  1 52  ? 25.346  -23.248 16.544  1.00 36.62 ? 51  PRO A CG  1 
ATOM   383   C  CD  . PRO A  1 52  ? 24.561  -22.414 15.567  1.00 36.39 ? 51  PRO A CD  1 
ATOM   384   N  N   . VAL A  1 53  ? 26.541  -19.184 18.529  1.00 32.91 ? 52  VAL A N   1 
ATOM   385   C  CA  . VAL A  1 53  ? 27.365  -17.965 18.709  1.00 32.91 ? 52  VAL A CA  1 
ATOM   386   C  C   . VAL A  1 53  ? 26.670  -16.688 18.226  1.00 31.33 ? 52  VAL A C   1 
ATOM   387   O  O   . VAL A  1 53  ? 26.497  -15.751 18.998  1.00 29.43 ? 52  VAL A O   1 
ATOM   388   C  CB  . VAL A  1 53  ? 28.761  -18.084 18.073  1.00 35.19 ? 52  VAL A CB  1 
ATOM   389   C  CG1 . VAL A  1 53  ? 29.634  -16.874 18.433  1.00 35.87 ? 52  VAL A CG1 1 
ATOM   390   C  CG2 . VAL A  1 53  ? 29.443  -19.369 18.534  1.00 36.45 ? 52  VAL A CG2 1 
ATOM   391   N  N   . ILE A  1 54  ? 26.275  -16.658 16.954  1.00 30.72 ? 53  ILE A N   1 
ATOM   392   C  CA  . ILE A  1 54  ? 25.508  -15.535 16.389  1.00 31.58 ? 53  ILE A CA  1 
ATOM   393   C  C   . ILE A  1 54  ? 24.223  -15.316 17.194  1.00 29.74 ? 53  ILE A C   1 
ATOM   394   O  O   . ILE A  1 54  ? 23.770  -14.181 17.374  1.00 28.14 ? 53  ILE A O   1 
ATOM   395   C  CB  . ILE A  1 54  ? 25.207  -15.778 14.877  1.00 34.08 ? 53  ILE A CB  1 
ATOM   396   C  CG1 . ILE A  1 54  ? 26.527  -15.921 14.090  1.00 37.98 ? 53  ILE A CG1 1 
ATOM   397   C  CG2 . ILE A  1 54  ? 24.396  -14.647 14.256  1.00 34.45 ? 53  ILE A CG2 1 
ATOM   398   C  CD1 . ILE A  1 54  ? 26.416  -16.587 12.732  1.00 40.53 ? 53  ILE A CD1 1 
ATOM   399   N  N   . ILE A  1 55  ? 23.652  -16.399 17.723  1.00 28.46 ? 54  ILE A N   1 
ATOM   400   C  CA  . ILE A  1 55  ? 22.431  -16.282 18.511  1.00 27.76 ? 54  ILE A CA  1 
ATOM   401   C  C   . ILE A  1 55  ? 22.615  -15.394 19.747  1.00 26.11 ? 54  ILE A C   1 
ATOM   402   O  O   . ILE A  1 55  ? 21.657  -14.789 20.215  1.00 23.15 ? 54  ILE A O   1 
ATOM   403   C  CB  . ILE A  1 55  ? 21.848  -17.652 18.913  1.00 29.64 ? 54  ILE A CB  1 
ATOM   404   C  CG1 . ILE A  1 55  ? 20.419  -17.461 19.457  1.00 31.58 ? 54  ILE A CG1 1 
ATOM   405   C  CG2 . ILE A  1 55  ? 22.731  -18.343 19.942  1.00 31.02 ? 54  ILE A CG2 1 
ATOM   406   C  CD1 . ILE A  1 55  ? 19.524  -18.664 19.281  1.00 33.66 ? 54  ILE A CD1 1 
ATOM   407   N  N   . ASP A  1 56  ? 23.837  -15.285 20.270  1.00 25.48 ? 55  ASP A N   1 
ATOM   408   C  CA  . ASP A  1 56  ? 24.065  -14.379 21.406  1.00 25.86 ? 55  ASP A CA  1 
ATOM   409   C  C   . ASP A  1 56  ? 23.838  -12.908 21.002  1.00 23.67 ? 55  ASP A C   1 
ATOM   410   O  O   . ASP A  1 56  ? 23.365  -12.098 21.819  1.00 22.57 ? 55  ASP A O   1 
ATOM   411   C  CB  . ASP A  1 56  ? 25.486  -14.533 21.982  1.00 28.69 ? 55  ASP A CB  1 
ATOM   412   C  CG  . ASP A  1 56  ? 25.753  -15.923 22.570  1.00 30.96 ? 55  ASP A CG  1 
ATOM   413   O  OD1 . ASP A  1 56  ? 24.840  -16.523 23.171  1.00 31.91 ? 55  ASP A OD1 1 
ATOM   414   O  OD2 . ASP A  1 56  ? 26.907  -16.381 22.450  1.00 31.79 ? 55  ASP A OD2 1 
ATOM   415   N  N   . CYS A  1 57  ? 24.234  -12.563 19.780  1.00 23.65 ? 56  CYS A N   1 
ATOM   416   C  CA  . CYS A  1 57  ? 23.980  -11.222 19.228  1.00 24.87 ? 56  CYS A CA  1 
ATOM   417   C  C   . CYS A  1 57  ? 22.464  -10.965 19.166  1.00 23.46 ? 56  CYS A C   1 
ATOM   418   O  O   . CYS A  1 57  ? 21.980  -9.891  19.511  1.00 22.79 ? 56  CYS A O   1 
ATOM   419   C  CB  . CYS A  1 57  ? 24.548  -11.074 17.818  1.00 26.56 ? 56  CYS A CB  1 
ATOM   420   S  SG  . CYS A  1 57  ? 26.274  -11.559 17.619  1.00 32.20 ? 56  CYS A SG  1 
ATOM   421   N  N   . TRP A  1 58  ? 21.742  -11.948 18.655  1.00 21.92 ? 57  TRP A N   1 
ATOM   422   C  CA  . TRP A  1 58  ? 20.290  -11.844 18.503  1.00 21.95 ? 57  TRP A CA  1 
ATOM   423   C  C   . TRP A  1 58  ? 19.629  -11.667 19.857  1.00 21.73 ? 57  TRP A C   1 
ATOM   424   O  O   . TRP A  1 58  ? 18.807  -10.768 20.023  1.00 21.02 ? 57  TRP A O   1 
ATOM   425   C  CB  . TRP A  1 58  ? 19.767  -13.094 17.791  1.00 21.87 ? 57  TRP A CB  1 
ATOM   426   C  CG  . TRP A  1 58  ? 18.298  -13.122 17.575  1.00 20.98 ? 57  TRP A CG  1 
ATOM   427   C  CD1 . TRP A  1 58  ? 17.617  -12.497 16.592  1.00 21.09 ? 57  TRP A CD1 1 
ATOM   428   C  CD2 . TRP A  1 58  ? 17.338  -13.855 18.335  1.00 21.63 ? 57  TRP A CD2 1 
ATOM   429   N  NE1 . TRP A  1 58  ? 16.277  -12.773 16.701  1.00 20.28 ? 57  TRP A NE1 1 
ATOM   430   C  CE2 . TRP A  1 58  ? 16.081  -13.616 17.755  1.00 20.81 ? 57  TRP A CE2 1 
ATOM   431   C  CE3 . TRP A  1 58  ? 17.418  -14.689 19.457  1.00 21.79 ? 57  TRP A CE3 1 
ATOM   432   C  CZ2 . TRP A  1 58  ? 14.905  -14.167 18.270  1.00 22.63 ? 57  TRP A CZ2 1 
ATOM   433   C  CZ3 . TRP A  1 58  ? 16.269  -15.236 19.969  1.00 23.57 ? 57  TRP A CZ3 1 
ATOM   434   C  CH2 . TRP A  1 58  ? 15.014  -14.985 19.366  1.00 23.55 ? 57  TRP A CH2 1 
ATOM   435   N  N   . ILE A  1 59  ? 19.995  -12.511 20.828  1.00 22.07 ? 58  ILE A N   1 
ATOM   436   C  CA  . ILE A  1 59  ? 19.464  -12.394 22.184  1.00 22.45 ? 58  ILE A CA  1 
ATOM   437   C  C   . ILE A  1 59  ? 19.735  -10.991 22.742  1.00 22.80 ? 58  ILE A C   1 
ATOM   438   O  O   . ILE A  1 59  ? 18.850  -10.369 23.343  1.00 21.83 ? 58  ILE A O   1 
ATOM   439   C  CB  . ILE A  1 59  ? 20.047  -13.480 23.129  1.00 23.32 ? 58  ILE A CB  1 
ATOM   440   C  CG1 . ILE A  1 59  ? 19.534  -14.867 22.680  1.00 24.10 ? 58  ILE A CG1 1 
ATOM   441   C  CG2 . ILE A  1 59  ? 19.713  -13.179 24.573  1.00 23.25 ? 58  ILE A CG2 1 
ATOM   442   C  CD1 . ILE A  1 59  ? 20.140  -16.056 23.396  1.00 25.46 ? 58  ILE A CD1 1 
ATOM   443   N  N   . ASP A  1 60  ? 20.946  -10.487 22.523  1.00 22.53 ? 59  ASP A N   1 
ATOM   444   C  CA  . ASP A  1 60  ? 21.310  -9.176  23.064  1.00 22.92 ? 59  ASP A CA  1 
ATOM   445   C  C   . ASP A  1 60  ? 20.477  -8.045  22.471  1.00 22.22 ? 59  ASP A C   1 
ATOM   446   O  O   . ASP A  1 60  ? 20.282  -7.027  23.146  1.00 23.02 ? 59  ASP A O   1 
ATOM   447   C  CB  . ASP A  1 60  ? 22.811  -8.867  22.865  1.00 24.13 ? 59  ASP A CB  1 
ATOM   448   C  CG  . ASP A  1 60  ? 23.297  -7.743  23.784  1.00 25.74 ? 59  ASP A CG  1 
ATOM   449   O  OD1 . ASP A  1 60  ? 23.008  -7.816  24.997  1.00 26.78 ? 59  ASP A OD1 1 
ATOM   450   O  OD2 . ASP A  1 60  ? 23.956  -6.789  23.306  1.00 27.27 ? 59  ASP A OD2 1 
ATOM   451   N  N   . ASN A  1 61  ? 19.966  -8.224  21.243  1.00 20.07 ? 60  ASN A N   1 
ATOM   452   C  CA  . ASN A  1 61  ? 19.143  -7.221  20.586  1.00 20.12 ? 60  ASN A CA  1 
ATOM   453   C  C   . ASN A  1 61  ? 17.633  -7.386  20.812  1.00 19.45 ? 60  ASN A C   1 
ATOM   454   O  O   . ASN A  1 61  ? 16.914  -6.399  20.880  1.00 18.56 ? 60  ASN A O   1 
ATOM   455   C  CB  . ASN A  1 61  ? 19.401  -7.217  19.064  1.00 20.23 ? 60  ASN A CB  1 
ATOM   456   C  CG  . ASN A  1 61  ? 20.770  -6.658  18.706  1.00 21.09 ? 60  ASN A CG  1 
ATOM   457   O  OD1 . ASN A  1 61  ? 21.279  -5.776  19.398  1.00 21.55 ? 60  ASN A OD1 1 
ATOM   458   N  ND2 . ASN A  1 61  ? 21.362  -7.153  17.626  1.00 21.28 ? 60  ASN A ND2 1 
ATOM   459   N  N   . ILE A  1 62  ? 17.177  -8.625  20.898  1.00 18.81 ? 61  ILE A N   1 
ATOM   460   C  CA  . ILE A  1 62  ? 15.719  -8.889  20.956  1.00 19.85 ? 61  ILE A CA  1 
ATOM   461   C  C   . ILE A  1 62  ? 15.183  -9.070  22.387  1.00 19.54 ? 61  ILE A C   1 
ATOM   462   O  O   . ILE A  1 62  ? 13.958  -9.039  22.592  1.00 18.58 ? 61  ILE A O   1 
ATOM   463   C  CB  . ILE A  1 62  ? 15.328  -10.104 20.074  1.00 20.53 ? 61  ILE A CB  1 
ATOM   464   C  CG1 . ILE A  1 62  ? 13.858  -9.987  19.636  1.00 21.78 ? 61  ILE A CG1 1 
ATOM   465   C  CG2 . ILE A  1 62  ? 15.627  -11.396 20.813  1.00 20.89 ? 61  ILE A CG2 1 
ATOM   466   C  CD1 . ILE A  1 62  ? 13.466  -10.952 18.542  1.00 23.60 ? 61  ILE A CD1 1 
ATOM   467   N  N   . ARG A  1 63  ? 16.082  -9.239  23.362  1.00 20.30 ? 62  ARG A N   1 
ATOM   468   C  CA  . ARG A  1 63  ? 15.669  -9.245  24.763  1.00 21.05 ? 62  ARG A CA  1 
ATOM   469   C  C   . ARG A  1 63  ? 15.049  -7.903  25.138  1.00 20.58 ? 62  ARG A C   1 
ATOM   470   O  O   . ARG A  1 63  ? 15.386  -6.867  24.561  1.00 20.29 ? 62  ARG A O   1 
ATOM   471   C  CB  . ARG A  1 63  ? 16.854  -9.550  25.701  1.00 23.01 ? 62  ARG A CB  1 
ATOM   472   C  CG  . ARG A  1 63  ? 17.860  -8.410  25.812  1.00 24.43 ? 62  ARG A CG  1 
ATOM   473   C  CD  . ARG A  1 63  ? 19.150  -8.853  26.475  1.00 27.39 ? 62  ARG A CD  1 
ATOM   474   N  NE  . ARG A  1 63  ? 20.153  -7.794  26.421  1.00 29.63 ? 62  ARG A NE  1 
ATOM   475   C  CZ  . ARG A  1 63  ? 20.311  -6.829  27.324  1.00 31.86 ? 62  ARG A CZ  1 
ATOM   476   N  NH1 . ARG A  1 63  ? 19.574  -6.776  28.433  1.00 32.00 ? 62  ARG A NH1 1 
ATOM   477   N  NH2 . ARG A  1 63  ? 21.262  -5.923  27.129  1.00 34.06 ? 62  ARG A NH2 1 
ATOM   478   N  N   . LEU A  1 64  ? 14.105  -7.935  26.085  1.00 20.45 ? 63  LEU A N   1 
ATOM   479   C  CA  . LEU A  1 64  ? 13.601  -6.741  26.754  1.00 19.86 ? 63  LEU A CA  1 
ATOM   480   C  C   . LEU A  1 64  ? 14.292  -6.571  28.117  1.00 20.13 ? 63  LEU A C   1 
ATOM   481   O  O   . LEU A  1 64  ? 14.641  -7.543  28.784  1.00 20.22 ? 63  LEU A O   1 
ATOM   482   C  CB  . LEU A  1 64  ? 12.084  -6.831  26.946  1.00 20.38 ? 63  LEU A CB  1 
ATOM   483   C  CG  . LEU A  1 64  ? 11.165  -6.835  25.722  1.00 20.56 ? 63  LEU A CG  1 
ATOM   484   C  CD1 . LEU A  1 64  ? 9.716   -7.006  26.179  1.00 20.51 ? 63  LEU A CD1 1 
ATOM   485   C  CD2 . LEU A  1 64  ? 11.326  -5.554  24.937  1.00 21.99 ? 63  LEU A CD2 1 
ATOM   486   N  N   . VAL A  1 65  ? 14.549  -5.334  28.486  1.00 20.77 ? 64  VAL A N   1 
ATOM   487   C  CA  . VAL A  1 65  ? 15.085  -4.987  29.792  1.00 21.88 ? 64  VAL A CA  1 
ATOM   488   C  C   . VAL A  1 65  ? 13.921  -4.570  30.693  1.00 21.57 ? 64  VAL A C   1 
ATOM   489   O  O   . VAL A  1 65  ? 13.150  -3.691  30.320  1.00 21.44 ? 64  VAL A O   1 
ATOM   490   C  CB  . VAL A  1 65  ? 16.059  -3.801  29.661  1.00 23.60 ? 64  VAL A CB  1 
ATOM   491   C  CG1 . VAL A  1 65  ? 16.561  -3.349  31.026  1.00 25.22 ? 64  VAL A CG1 1 
ATOM   492   C  CG2 . VAL A  1 65  ? 17.233  -4.164  28.762  1.00 25.17 ? 64  VAL A CG2 1 
ATOM   493   N  N   . TYR A  1 66  ? 13.782  -5.185  31.862  1.00 21.41 ? 65  TYR A N   1 
ATOM   494   C  CA  . TYR A  1 66  ? 12.722  -4.803  32.784  1.00 21.81 ? 65  TYR A CA  1 
ATOM   495   C  C   . TYR A  1 66  ? 13.252  -3.744  33.766  1.00 23.49 ? 65  TYR A C   1 
ATOM   496   O  O   . TYR A  1 66  ? 14.219  -3.971  34.464  1.00 22.81 ? 65  TYR A O   1 
ATOM   497   C  CB  . TYR A  1 66  ? 12.157  -6.029  33.545  1.00 21.61 ? 65  TYR A CB  1 
ATOM   498   C  CG  . TYR A  1 66  ? 10.889  -5.677  34.298  1.00 21.20 ? 65  TYR A CG  1 
ATOM   499   C  CD1 . TYR A  1 66  ? 9.651   -5.648  33.644  1.00 21.24 ? 65  TYR A CD1 1 
ATOM   500   C  CD2 . TYR A  1 66  ? 10.925  -5.292  35.642  1.00 21.63 ? 65  TYR A CD2 1 
ATOM   501   C  CE1 . TYR A  1 66  ? 8.490   -5.285  34.313  1.00 21.16 ? 65  TYR A CE1 1 
ATOM   502   C  CE2 . TYR A  1 66  ? 9.760   -4.938  36.311  1.00 22.08 ? 65  TYR A CE2 1 
ATOM   503   C  CZ  . TYR A  1 66  ? 8.553   -4.947  35.655  1.00 21.77 ? 65  TYR A CZ  1 
ATOM   504   O  OH  . TYR A  1 66  ? 7.393   -4.570  36.329  1.00 23.95 ? 65  TYR A OH  1 
ATOM   505   N  N   . ASN A  1 67  ? 12.589  -2.606  33.812  1.00 23.75 ? 66  ASN A N   1 
ATOM   506   C  CA  . ASN A  1 67  ? 12.978  -1.512  34.710  1.00 26.40 ? 66  ASN A CA  1 
ATOM   507   C  C   . ASN A  1 67  ? 12.052  -1.507  35.920  1.00 26.80 ? 66  ASN A C   1 
ATOM   508   O  O   . ASN A  1 67  ? 10.853  -1.249  35.798  1.00 26.53 ? 66  ASN A O   1 
ATOM   509   C  CB  . ASN A  1 67  ? 12.882  -0.229  33.915  1.00 27.33 ? 66  ASN A CB  1 
ATOM   510   C  CG  . ASN A  1 67  ? 13.285  0.997   34.706  1.00 30.35 ? 66  ASN A CG  1 
ATOM   511   O  OD1 . ASN A  1 67  ? 13.099  1.071   35.926  1.00 30.19 ? 66  ASN A OD1 1 
ATOM   512   N  ND2 . ASN A  1 67  ? 13.845  1.980   33.989  1.00 33.32 ? 66  ASN A ND2 1 
ATOM   513   N  N   . LYS A  1 68  ? 12.592  -1.863  37.083  1.00 29.16 ? 67  LYS A N   1 
ATOM   514   C  CA  . LYS A  1 68  ? 11.781  -2.021  38.303  1.00 30.93 ? 67  LYS A CA  1 
ATOM   515   C  C   . LYS A  1 68  ? 11.224  -0.691  38.821  1.00 32.26 ? 67  LYS A C   1 
ATOM   516   O  O   . LYS A  1 68  ? 10.203  -0.691  39.489  1.00 31.47 ? 67  LYS A O   1 
ATOM   517   C  CB  . LYS A  1 68  ? 12.590  -2.681  39.421  1.00 33.03 ? 67  LYS A CB  1 
ATOM   518   C  CG  . LYS A  1 68  ? 13.022  -4.116  39.161  1.00 35.16 ? 67  LYS A CG  1 
ATOM   519   C  CD  . LYS A  1 68  ? 13.890  -4.610  40.312  1.00 38.90 ? 67  LYS A CD  1 
ATOM   520   C  CE  . LYS A  1 68  ? 14.158  -6.100  40.257  1.00 41.11 ? 67  LYS A CE  1 
ATOM   521   N  NZ  . LYS A  1 68  ? 15.128  -6.481  39.193  1.00 43.33 ? 67  LYS A NZ  1 
ATOM   522   N  N   . THR A  1 69  ? 11.875  0.420   38.484  1.00 34.90 ? 68  THR A N   1 
ATOM   523   C  CA  . THR A  1 69  ? 11.414  1.766   38.886  1.00 38.34 ? 68  THR A CA  1 
ATOM   524   C  C   . THR A  1 69  ? 10.168  2.179   38.120  1.00 37.13 ? 68  THR A C   1 
ATOM   525   O  O   . THR A  1 69  ? 9.160   2.555   38.707  1.00 40.33 ? 68  THR A O   1 
ATOM   526   C  CB  . THR A  1 69  ? 12.503  2.826   38.639  1.00 39.18 ? 68  THR A CB  1 
ATOM   527   O  OG1 . THR A  1 69  ? 13.710  2.428   39.297  1.00 41.01 ? 68  THR A OG1 1 
ATOM   528   C  CG2 . THR A  1 69  ? 12.061  4.196   39.151  1.00 41.86 ? 68  THR A CG2 1 
ATOM   529   N  N   . SER A  1 70  ? 10.222  2.069   36.800  1.00 36.54 ? 69  SER A N   1 
ATOM   530   C  CA  . SER A  1 70  ? 9.072   2.400   35.981  1.00 32.79 ? 69  SER A CA  1 
ATOM   531   C  C   . SER A  1 70  ? 8.062   1.261   35.880  1.00 30.45 ? 69  SER A C   1 
ATOM   532   O  O   . SER A  1 70  ? 6.964   1.482   35.399  1.00 29.00 ? 69  SER A O   1 
ATOM   533   C  CB  . SER A  1 70  ? 9.530   2.805   34.589  1.00 34.42 ? 69  SER A CB  1 
ATOM   534   O  OG  . SER A  1 70  ? 10.180  1.716   33.951  1.00 35.42 ? 69  SER A OG  1 
ATOM   535   N  N   . ARG A  1 71  ? 8.416   0.051   36.320  1.00 28.71 ? 70  ARG A N   1 
ATOM   536   C  CA  . ARG A  1 71  ? 7.583   -1.140  36.110  1.00 27.82 ? 70  ARG A CA  1 
ATOM   537   C  C   . ARG A  1 71  ? 7.202   -1.259  34.643  1.00 26.66 ? 70  ARG A C   1 
ATOM   538   O  O   . ARG A  1 71  ? 6.045   -1.483  34.292  1.00 25.97 ? 70  ARG A O   1 
ATOM   539   C  CB  . ARG A  1 71  ? 6.320   -1.154  37.006  1.00 28.86 ? 70  ARG A CB  1 
ATOM   540   C  CG  . ARG A  1 71  ? 6.616   -1.124  38.503  1.00 29.99 ? 70  ARG A CG  1 
ATOM   541   C  CD  . ARG A  1 71  ? 7.253   -2.409  39.002  1.00 29.12 ? 70  ARG A CD  1 
ATOM   542   N  NE  . ARG A  1 71  ? 6.323   -3.532  38.903  1.00 29.04 ? 70  ARG A NE  1 
ATOM   543   C  CZ  . ARG A  1 71  ? 5.611   -4.052  39.900  1.00 29.39 ? 70  ARG A CZ  1 
ATOM   544   N  NH1 . ARG A  1 71  ? 5.743   -3.591  41.129  1.00 28.98 ? 70  ARG A NH1 1 
ATOM   545   N  NH2 . ARG A  1 71  ? 4.787   -5.082  39.682  1.00 29.69 ? 70  ARG A NH2 1 
ATOM   546   N  N   . ALA A  1 72  ? 8.202   -1.159  33.784  1.00 26.37 ? 71  ALA A N   1 
ATOM   547   C  CA  . ALA A  1 72  ? 7.983   -1.202  32.355  1.00 25.02 ? 71  ALA A CA  1 
ATOM   548   C  C   . ALA A  1 72  ? 9.205   -1.836  31.697  1.00 24.99 ? 71  ALA A C   1 
ATOM   549   O  O   . ALA A  1 72  ? 10.296  -1.807  32.256  1.00 24.67 ? 71  ALA A O   1 
ATOM   550   C  CB  . ALA A  1 72  ? 7.761   0.198   31.837  1.00 26.19 ? 71  ALA A CB  1 
ATOM   551   N  N   . THR A  1 73  ? 9.029   -2.362  30.485  1.00 23.98 ? 72  THR A N   1 
ATOM   552   C  CA  . THR A  1 73  ? 10.163  -2.864  29.729  1.00 23.37 ? 72  THR A CA  1 
ATOM   553   C  C   . THR A  1 73  ? 10.720  -1.787  28.827  1.00 23.23 ? 72  THR A C   1 
ATOM   554   O  O   . THR A  1 73  ? 10.037  -0.834  28.460  1.00 22.20 ? 72  THR A O   1 
ATOM   555   C  CB  . THR A  1 73  ? 9.810   -4.100  28.881  1.00 22.61 ? 72  THR A CB  1 
ATOM   556   O  OG1 . THR A  1 73  ? 8.674   -3.803  28.041  1.00 22.70 ? 72  THR A OG1 1 
ATOM   557   C  CG2 . THR A  1 73  ? 9.534   -5.238  29.761  1.00 22.62 ? 72  THR A CG2 1 
ATOM   558   N  N   . GLN A  1 74  ? 11.991  -1.939  28.480  1.00 22.69 ? 73  GLN A N   1 
ATOM   559   C  CA  . GLN A  1 74  ? 12.636  -1.055  27.525  1.00 22.12 ? 73  GLN A CA  1 
ATOM   560   C  C   . GLN A  1 74  ? 13.580  -1.885  26.657  1.00 21.31 ? 73  GLN A C   1 
ATOM   561   O  O   . GLN A  1 74  ? 13.921  -3.015  27.000  1.00 19.33 ? 73  GLN A O   1 
ATOM   562   C  CB  . GLN A  1 74  ? 13.362  0.088   28.247  1.00 24.73 ? 73  GLN A CB  1 
ATOM   563   C  CG  . GLN A  1 74  ? 14.151  -0.338  29.458  1.00 26.41 ? 73  GLN A CG  1 
ATOM   564   C  CD  . GLN A  1 74  ? 14.676  0.819   30.306  1.00 27.49 ? 73  GLN A CD  1 
ATOM   565   O  OE1 . GLN A  1 74  ? 13.938  1.500   31.020  1.00 27.98 ? 73  GLN A OE1 1 
ATOM   566   N  NE2 . GLN A  1 74  ? 15.969  1.031   30.223  1.00 28.71 ? 73  GLN A NE2 1 
ATOM   567   N  N   . PHE A  1 75  ? 13.967  -1.342  25.510  1.00 21.30 ? 74  PHE A N   1 
ATOM   568   C  CA  . PHE A  1 75  ? 14.903  -2.030  24.648  1.00 21.09 ? 74  PHE A CA  1 
ATOM   569   C  C   . PHE A  1 75  ? 16.317  -1.853  25.211  1.00 21.78 ? 74  PHE A C   1 
ATOM   570   O  O   . PHE A  1 75  ? 16.582  -0.920  25.960  1.00 21.68 ? 74  PHE A O   1 
ATOM   571   C  CB  . PHE A  1 75  ? 14.845  -1.482  23.220  1.00 22.84 ? 74  PHE A CB  1 
ATOM   572   C  CG  . PHE A  1 75  ? 13.458  -1.415  22.625  1.00 23.33 ? 74  PHE A CG  1 
ATOM   573   C  CD1 . PHE A  1 75  ? 12.497  -2.378  22.917  1.00 23.93 ? 74  PHE A CD1 1 
ATOM   574   C  CD2 . PHE A  1 75  ? 13.116  -0.369  21.779  1.00 24.74 ? 74  PHE A CD2 1 
ATOM   575   C  CE1 . PHE A  1 75  ? 11.210  -2.285  22.381  1.00 24.77 ? 74  PHE A CE1 1 
ATOM   576   C  CE2 . PHE A  1 75  ? 11.848  -0.295  21.206  1.00 24.18 ? 74  PHE A CE2 1 
ATOM   577   C  CZ  . PHE A  1 75  ? 10.898  -1.252  21.506  1.00 24.89 ? 74  PHE A CZ  1 
ATOM   578   N  N   . PRO A  1 76  ? 17.243  -2.763  24.863  1.00 22.32 ? 75  PRO A N   1 
ATOM   579   C  CA  . PRO A  1 76  ? 18.637  -2.525  25.255  1.00 22.54 ? 75  PRO A CA  1 
ATOM   580   C  C   . PRO A  1 76  ? 19.186  -1.198  24.742  1.00 22.96 ? 75  PRO A C   1 
ATOM   581   O  O   . PRO A  1 76  ? 18.672  -0.656  23.764  1.00 20.70 ? 75  PRO A O   1 
ATOM   582   C  CB  . PRO A  1 76  ? 19.379  -3.716  24.634  1.00 23.09 ? 75  PRO A CB  1 
ATOM   583   C  CG  . PRO A  1 76  ? 18.344  -4.769  24.519  1.00 22.63 ? 75  PRO A CG  1 
ATOM   584   C  CD  . PRO A  1 76  ? 17.086  -4.039  24.145  1.00 21.70 ? 75  PRO A CD  1 
ATOM   585   N  N   . ASP A  1 77  ? 20.248  -0.683  25.386  1.00 25.02 ? 76  ASP A N   1 
ATOM   586   C  CA  . ASP A  1 77  ? 20.852  0.567   24.966  1.00 26.42 ? 76  ASP A CA  1 
ATOM   587   C  C   . ASP A  1 77  ? 21.214  0.510   23.503  1.00 24.96 ? 76  ASP A C   1 
ATOM   588   O  O   . ASP A  1 77  ? 21.886  -0.425  23.062  1.00 25.16 ? 76  ASP A O   1 
ATOM   589   C  CB  . ASP A  1 77  ? 22.143  0.880   25.771  1.00 31.93 ? 76  ASP A CB  1 
ATOM   590   C  CG  . ASP A  1 77  ? 21.872  1.115   27.250  1.00 38.89 ? 76  ASP A CG  1 
ATOM   591   O  OD1 . ASP A  1 77  ? 20.694  1.387   27.613  1.00 45.44 ? 76  ASP A OD1 1 
ATOM   592   O  OD2 . ASP A  1 77  ? 22.833  1.017   28.057  1.00 44.71 ? 76  ASP A OD2 1 
ATOM   593   N  N   . GLY A  1 78  ? 20.818  1.544   22.766  1.00 23.49 ? 77  GLY A N   1 
ATOM   594   C  CA  . GLY A  1 78  ? 21.136  1.678   21.351  1.00 23.43 ? 77  GLY A CA  1 
ATOM   595   C  C   . GLY A  1 78  ? 20.393  0.744   20.407  1.00 22.90 ? 77  GLY A C   1 
ATOM   596   O  O   . GLY A  1 78  ? 20.777  0.609   19.254  1.00 23.06 ? 77  GLY A O   1 
ATOM   597   N  N   . VAL A  1 79  ? 19.316  0.118   20.877  1.00 21.59 ? 78  VAL A N   1 
ATOM   598   C  CA  . VAL A  1 79  ? 18.534  -0.759  20.033  1.00 21.22 ? 78  VAL A CA  1 
ATOM   599   C  C   . VAL A  1 79  ? 17.132  -0.175  19.874  1.00 20.84 ? 78  VAL A C   1 
ATOM   600   O  O   . VAL A  1 79  ? 16.519  0.233   20.858  1.00 21.66 ? 78  VAL A O   1 
ATOM   601   C  CB  . VAL A  1 79  ? 18.414  -2.171  20.631  1.00 21.07 ? 78  VAL A CB  1 
ATOM   602   C  CG1 . VAL A  1 79  ? 17.542  -3.050  19.757  1.00 21.38 ? 78  VAL A CG1 1 
ATOM   603   C  CG2 . VAL A  1 79  ? 19.782  -2.802  20.823  1.00 22.32 ? 78  VAL A CG2 1 
ATOM   604   N  N   . ASP A  1 80  ? 16.641  -0.110  18.639  1.00 19.46 ? 79  ASP A N   1 
ATOM   605   C  CA  . ASP A  1 80  ? 15.214  0.142   18.401  1.00 18.94 ? 79  ASP A CA  1 
ATOM   606   C  C   . ASP A  1 80  ? 14.586  -1.034  17.679  1.00 18.69 ? 79  ASP A C   1 
ATOM   607   O  O   . ASP A  1 80  ? 15.178  -1.567  16.747  1.00 19.23 ? 79  ASP A O   1 
ATOM   608   C  CB  . ASP A  1 80  ? 14.945  1.399   17.577  1.00 19.76 ? 79  ASP A CB  1 
ATOM   609   C  CG  . ASP A  1 80  ? 13.461  1.766   17.597  1.00 20.08 ? 79  ASP A CG  1 
ATOM   610   O  OD1 . ASP A  1 80  ? 12.928  1.933   18.738  1.00 21.38 ? 79  ASP A OD1 1 
ATOM   611   O  OD2 . ASP A  1 80  ? 12.824  1.838   16.520  1.00 20.79 ? 79  ASP A OD2 1 
ATOM   612   N  N   . VAL A  1 81  ? 13.377  -1.410  18.092  1.00 17.58 ? 80  VAL A N   1 
ATOM   613   C  CA  . VAL A  1 81  ? 12.635  -2.472  17.446  1.00 16.80 ? 80  VAL A CA  1 
ATOM   614   C  C   . VAL A  1 81  ? 11.276  -1.932  16.987  1.00 17.12 ? 80  VAL A C   1 
ATOM   615   O  O   . VAL A  1 81  ? 10.556  -1.318  17.776  1.00 16.66 ? 80  VAL A O   1 
ATOM   616   C  CB  . VAL A  1 81  ? 12.430  -3.675  18.373  1.00 17.02 ? 80  VAL A CB  1 
ATOM   617   C  CG1 . VAL A  1 81  ? 11.627  -4.776  17.678  1.00 16.67 ? 80  VAL A CG1 1 
ATOM   618   C  CG2 . VAL A  1 81  ? 13.779  -4.253  18.793  1.00 17.73 ? 80  VAL A CG2 1 
ATOM   619   N  N   . ARG A  1 82  ? 10.951  -2.115  15.712  1.00 16.89 ? 81  ARG A N   1 
ATOM   620   C  CA  . ARG A  1 82  ? 9.655   -1.654  15.173  1.00 17.77 ? 81  ARG A CA  1 
ATOM   621   C  C   . ARG A  1 82  ? 8.904   -2.780  14.490  1.00 16.95 ? 81  ARG A C   1 
ATOM   622   O  O   . ARG A  1 82  ? 9.475   -3.804  14.113  1.00 18.30 ? 81  ARG A O   1 
ATOM   623   C  CB  . ARG A  1 82  ? 9.813   -0.478  14.231  1.00 19.79 ? 81  ARG A CB  1 
ATOM   624   C  CG  . ARG A  1 82  ? 10.305  -0.820  12.870  1.00 21.13 ? 81  ARG A CG  1 
ATOM   625   C  CD  . ARG A  1 82  ? 10.233  0.371   11.904  1.00 23.73 ? 81  ARG A CD  1 
ATOM   626   N  NE  . ARG A  1 82  ? 10.801  -0.039  10.629  1.00 24.59 ? 81  ARG A NE  1 
ATOM   627   C  CZ  . ARG A  1 82  ? 11.251  0.772   9.683   1.00 28.13 ? 81  ARG A CZ  1 
ATOM   628   N  NH1 . ARG A  1 82  ? 11.197  2.104   9.828   1.00 27.24 ? 81  ARG A NH1 1 
ATOM   629   N  NH2 . ARG A  1 82  ? 11.768  0.252   8.579   1.00 28.56 ? 81  ARG A NH2 1 
ATOM   630   N  N   . VAL A  1 83  ? 7.608   -2.589  14.374  1.00 16.11 ? 82  VAL A N   1 
ATOM   631   C  CA  . VAL A  1 83  ? 6.706   -3.581  13.801  1.00 15.98 ? 82  VAL A CA  1 
ATOM   632   C  C   . VAL A  1 83  ? 6.330   -3.087  12.412  1.00 15.71 ? 82  VAL A C   1 
ATOM   633   O  O   . VAL A  1 83  ? 5.647   -2.092  12.298  1.00 16.50 ? 82  VAL A O   1 
ATOM   634   C  CB  . VAL A  1 83  ? 5.418   -3.684  14.641  1.00 15.22 ? 82  VAL A CB  1 
ATOM   635   C  CG1 . VAL A  1 83  ? 4.439   -4.684  14.029  1.00 15.92 ? 82  VAL A CG1 1 
ATOM   636   C  CG2 . VAL A  1 83  ? 5.755   -4.080  16.074  1.00 16.07 ? 82  VAL A CG2 1 
ATOM   637   N  N   . PRO A  1 84  ? 6.785   -3.769  11.357  1.00 16.41 ? 83  PRO A N   1 
ATOM   638   C  CA  . PRO A  1 84  ? 6.432   -3.322  10.004  1.00 16.68 ? 83  PRO A CA  1 
ATOM   639   C  C   . PRO A  1 84  ? 5.056   -3.838  9.606   1.00 16.72 ? 83  PRO A C   1 
ATOM   640   O  O   . PRO A  1 84  ? 4.555   -4.759  10.226  1.00 15.88 ? 83  PRO A O   1 
ATOM   641   C  CB  . PRO A  1 84  ? 7.486   -3.977  9.141   1.00 17.06 ? 83  PRO A CB  1 
ATOM   642   C  CG  . PRO A  1 84  ? 7.815   -5.249  9.886   1.00 17.44 ? 83  PRO A CG  1 
ATOM   643   C  CD  . PRO A  1 84  ? 7.731   -4.901  11.336  1.00 16.66 ? 83  PRO A CD  1 
ATOM   644   N  N   . GLY A  1 85  ? 4.456   -3.230  8.587   1.00 18.12 ? 84  GLY A N   1 
ATOM   645   C  CA  . GLY A  1 85  ? 3.291   -3.829  7.914   1.00 17.28 ? 84  GLY A CA  1 
ATOM   646   C  C   . GLY A  1 85  ? 1.956   -3.678  8.598   1.00 17.02 ? 84  GLY A C   1 
ATOM   647   O  O   . GLY A  1 85  ? 1.020   -4.435  8.269   1.00 16.42 ? 84  GLY A O   1 
ATOM   648   N  N   . PHE A  1 86  ? 1.811   -2.708  9.519   1.00 17.07 ? 85  PHE A N   1 
ATOM   649   C  CA  . PHE A  1 86  ? 0.491   -2.474  10.126  1.00 17.05 ? 85  PHE A CA  1 
ATOM   650   C  C   . PHE A  1 86  ? -0.488  -2.000  9.050   1.00 17.94 ? 85  PHE A C   1 
ATOM   651   O  O   . PHE A  1 86  ? -0.198  -1.070  8.285   1.00 16.53 ? 85  PHE A O   1 
ATOM   652   C  CB  . PHE A  1 86  ? 0.543   -1.478  11.301  1.00 17.46 ? 85  PHE A CB  1 
ATOM   653   C  CG  . PHE A  1 86  ? -0.747  -1.402  12.073  1.00 17.72 ? 85  PHE A CG  1 
ATOM   654   C  CD1 . PHE A  1 86  ? -1.000  -2.246  13.150  1.00 18.20 ? 85  PHE A CD1 1 
ATOM   655   C  CD2 . PHE A  1 86  ? -1.736  -0.500  11.695  1.00 19.34 ? 85  PHE A CD2 1 
ATOM   656   C  CE1 . PHE A  1 86  ? -2.207  -2.186  13.838  1.00 18.54 ? 85  PHE A CE1 1 
ATOM   657   C  CE2 . PHE A  1 86  ? -2.935  -0.436  12.377  1.00 19.89 ? 85  PHE A CE2 1 
ATOM   658   C  CZ  . PHE A  1 86  ? -3.182  -1.295  13.434  1.00 19.48 ? 85  PHE A CZ  1 
ATOM   659   N  N   . GLY A  1 87  ? -1.640  -2.650  8.970   1.00 16.09 ? 86  GLY A N   1 
ATOM   660   C  CA  . GLY A  1 87  ? -2.623  -2.338  7.937   1.00 17.51 ? 86  GLY A CA  1 
ATOM   661   C  C   . GLY A  1 87  ? -2.421  -3.140  6.650   1.00 16.88 ? 86  GLY A C   1 
ATOM   662   O  O   . GLY A  1 87  ? -3.270  -3.079  5.747   1.00 17.66 ? 86  GLY A O   1 
ATOM   663   N  N   . LYS A  1 88  ? -1.298  -3.856  6.542   1.00 17.10 ? 87  LYS A N   1 
ATOM   664   C  CA  . LYS A  1 88  ? -0.976  -4.692  5.376   1.00 19.56 ? 87  LYS A CA  1 
ATOM   665   C  C   . LYS A  1 88  ? -1.030  -6.156  5.845   1.00 18.64 ? 87  LYS A C   1 
ATOM   666   O  O   . LYS A  1 88  ? -1.344  -6.404  7.002   1.00 19.58 ? 87  LYS A O   1 
ATOM   667   C  CB  . LYS A  1 88  ? 0.422   -4.354  4.848   1.00 21.28 ? 87  LYS A CB  1 
ATOM   668   C  CG  . LYS A  1 88  ? 0.666   -2.878  4.611   1.00 23.96 ? 87  LYS A CG  1 
ATOM   669   C  CD  . LYS A  1 88  ? -0.291  -2.311  3.577   1.00 28.66 ? 87  LYS A CD  1 
ATOM   670   C  CE  . LYS A  1 88  ? 0.019   -0.836  3.324   1.00 34.05 ? 87  LYS A CE  1 
ATOM   671   N  NZ  . LYS A  1 88  ? -1.143  -0.150  2.690   1.00 35.72 ? 87  LYS A NZ  1 
ATOM   672   N  N   . THR A  1 89  ? -0.706  -7.108  4.982   1.00 17.70 ? 88  THR A N   1 
ATOM   673   C  CA  . THR A  1 89  ? -0.724  -8.506  5.373   1.00 17.75 ? 88  THR A CA  1 
ATOM   674   C  C   . THR A  1 89  ? 0.631   -9.193  5.238   1.00 17.39 ? 88  THR A C   1 
ATOM   675   O  O   . THR A  1 89  ? 0.816   -10.272 5.804   1.00 15.60 ? 88  THR A O   1 
ATOM   676   C  CB  . THR A  1 89  ? -1.784  -9.334  4.582   1.00 19.23 ? 88  THR A CB  1 
ATOM   677   O  OG1 . THR A  1 89  ? -1.451  -9.349  3.192   1.00 21.09 ? 88  THR A OG1 1 
ATOM   678   C  CG2 . THR A  1 89  ? -3.167  -8.750  4.782   1.00 21.10 ? 88  THR A CG2 1 
ATOM   679   N  N   . PHE A  1 90  ? 1.582   -8.581  4.539   1.00 16.94 ? 89  PHE A N   1 
ATOM   680   C  CA  . PHE A  1 90  ? 2.832   -9.270  4.232   1.00 18.06 ? 89  PHE A CA  1 
ATOM   681   C  C   . PHE A  1 90  ? 3.569   -9.752  5.484   1.00 17.52 ? 89  PHE A C   1 
ATOM   682   O  O   . PHE A  1 90  ? 4.186   -10.824 5.473   1.00 17.98 ? 89  PHE A O   1 
ATOM   683   C  CB  . PHE A  1 90  ? 3.750   -8.413  3.338   1.00 19.77 ? 89  PHE A CB  1 
ATOM   684   C  CG  . PHE A  1 90  ? 4.359   -7.219  4.021   1.00 20.27 ? 89  PHE A CG  1 
ATOM   685   C  CD1 . PHE A  1 90  ? 5.557   -7.344  4.735   1.00 21.85 ? 89  PHE A CD1 1 
ATOM   686   C  CD2 . PHE A  1 90  ? 3.757   -5.972  3.943   1.00 21.17 ? 89  PHE A CD2 1 
ATOM   687   C  CE1 . PHE A  1 90  ? 6.133   -6.237  5.367   1.00 22.36 ? 89  PHE A CE1 1 
ATOM   688   C  CE2 . PHE A  1 90  ? 4.340   -4.865  4.554   1.00 22.81 ? 89  PHE A CE2 1 
ATOM   689   C  CZ  . PHE A  1 90  ? 5.521   -5.003  5.280   1.00 22.33 ? 89  PHE A CZ  1 
ATOM   690   N  N   . SER A  1 91  ? 3.531   -8.968  6.559   1.00 17.27 ? 90  SER A N   1 
ATOM   691   C  CA  . SER A  1 91  ? 4.388   -9.257  7.720   1.00 17.31 ? 90  SER A CA  1 
ATOM   692   C  C   . SER A  1 91  ? 3.809   -10.345 8.633   1.00 17.01 ? 90  SER A C   1 
ATOM   693   O  O   . SER A  1 91  ? 4.519   -10.858 9.504   1.00 16.68 ? 90  SER A O   1 
ATOM   694   C  CB  . SER A  1 91  ? 4.685   -8.000  8.523   1.00 17.84 ? 90  SER A CB  1 
ATOM   695   O  OG  . SER A  1 91  ? 3.569   -7.582  9.280   1.00 19.73 ? 90  SER A OG  1 
ATOM   696   N  N   A LEU A  1 92  ? 2.529   -10.665 8.457   0.50 15.94 ? 91  LEU A N   1 
ATOM   697   N  N   B LEU A  1 92  ? 2.536   -10.678 8.424   0.50 16.78 ? 91  LEU A N   1 
ATOM   698   C  CA  A LEU A  1 92  ? 1.968   -11.858 9.094   0.50 16.10 ? 91  LEU A CA  1 
ATOM   699   C  CA  B LEU A  1 92  ? 1.906   -11.845 9.025   0.50 17.48 ? 91  LEU A CA  1 
ATOM   700   C  C   A LEU A  1 92  ? 1.749   -13.039 8.133   0.50 16.08 ? 91  LEU A C   1 
ATOM   701   C  C   B LEU A  1 92  ? 1.792   -13.045 8.120   0.50 16.89 ? 91  LEU A C   1 
ATOM   702   O  O   A LEU A  1 92  ? 1.643   -14.167 8.599   0.50 16.41 ? 91  LEU A O   1 
ATOM   703   O  O   B LEU A  1 92  ? 1.653   -14.167 8.599   0.50 17.14 ? 91  LEU A O   1 
ATOM   704   C  CB  A LEU A  1 92  ? 0.757   -11.585 9.991   0.50 15.96 ? 91  LEU A CB  1 
ATOM   705   C  CB  B LEU A  1 92  ? 0.434   -11.524 9.322   0.50 18.70 ? 91  LEU A CB  1 
ATOM   706   C  CG  A LEU A  1 92  ? -0.304  -10.599 9.571   0.50 15.98 ? 91  LEU A CG  1 
ATOM   707   C  CG  B LEU A  1 92  ? -0.014  -10.713 10.505  0.50 19.23 ? 91  LEU A CG  1 
ATOM   708   C  CD1 A LEU A  1 92  ? -1.064  -11.254 8.416   0.50 16.57 ? 91  LEU A CD1 1 
ATOM   709   C  CD1 B LEU A  1 92  ? 0.516   -9.315  10.391  0.50 19.95 ? 91  LEU A CD1 1 
ATOM   710   C  CD2 A LEU A  1 92  ? -1.208  -10.382 10.771  0.50 16.31 ? 91  LEU A CD2 1 
ATOM   711   C  CD2 B LEU A  1 92  ? -1.516  -10.717 10.452  0.50 20.71 ? 91  LEU A CD2 1 
ATOM   712   N  N   . GLU A  1 93  ? 1.779   -12.829 6.813   1.00 16.04 ? 92  GLU A N   1 
ATOM   713   C  CA  . GLU A  1 93  ? 1.736   -13.965 5.875   1.00 16.30 ? 92  GLU A CA  1 
ATOM   714   C  C   . GLU A  1 93  ? 3.044   -14.749 5.938   1.00 16.70 ? 92  GLU A C   1 
ATOM   715   O  O   . GLU A  1 93  ? 3.037   -15.968 5.940   1.00 16.98 ? 92  GLU A O   1 
ATOM   716   C  CB  . GLU A  1 93  ? 1.472   -13.525 4.414   1.00 16.04 ? 92  GLU A CB  1 
ATOM   717   C  CG  . GLU A  1 93  ? 0.054   -13.051 4.158   1.00 16.72 ? 92  GLU A CG  1 
ATOM   718   C  CD  . GLU A  1 93  ? -0.200  -12.757 2.695   1.00 17.31 ? 92  GLU A CD  1 
ATOM   719   O  OE1 . GLU A  1 93  ? -0.141  -13.697 1.880   1.00 18.02 ? 92  GLU A OE1 1 
ATOM   720   O  OE2 . GLU A  1 93  ? -0.450  -11.577 2.362   1.00 18.33 ? 92  GLU A OE2 1 
ATOM   721   N  N   . PHE A  1 94  ? 4.144   -14.023 5.959   1.00 17.28 ? 93  PHE A N   1 
ATOM   722   C  CA  . PHE A  1 94  ? 5.500   -14.588 5.946   1.00 18.32 ? 93  PHE A CA  1 
ATOM   723   C  C   . PHE A  1 94  ? 6.280   -13.967 7.085   1.00 18.65 ? 93  PHE A C   1 
ATOM   724   O  O   . PHE A  1 94  ? 6.474   -12.763 7.104   1.00 18.34 ? 93  PHE A O   1 
ATOM   725   C  CB  . PHE A  1 94  ? 6.205   -14.251 4.630   1.00 20.45 ? 93  PHE A CB  1 
ATOM   726   C  CG  . PHE A  1 94  ? 5.617   -14.927 3.430   1.00 21.97 ? 93  PHE A CG  1 
ATOM   727   C  CD1 . PHE A  1 94  ? 5.765   -16.284 3.276   1.00 23.37 ? 93  PHE A CD1 1 
ATOM   728   C  CD2 . PHE A  1 94  ? 4.935   -14.196 2.453   1.00 24.46 ? 93  PHE A CD2 1 
ATOM   729   C  CE1 . PHE A  1 94  ? 5.238   -16.925 2.184   1.00 25.36 ? 93  PHE A CE1 1 
ATOM   730   C  CE2 . PHE A  1 94  ? 4.400   -14.846 1.335   1.00 24.38 ? 93  PHE A CE2 1 
ATOM   731   C  CZ  . PHE A  1 94  ? 4.562   -16.212 1.222   1.00 25.14 ? 93  PHE A CZ  1 
ATOM   732   N  N   . LEU A  1 95  ? 6.743   -14.776 8.015   1.00 17.89 ? 94  LEU A N   1 
ATOM   733   C  CA  . LEU A  1 95  ? 7.551   -14.283 9.126   1.00 18.33 ? 94  LEU A CA  1 
ATOM   734   C  C   . LEU A  1 95  ? 8.973   -13.989 8.651   1.00 19.42 ? 94  LEU A C   1 
ATOM   735   O  O   . LEU A  1 95  ? 9.643   -13.094 9.158   1.00 19.15 ? 94  LEU A O   1 
ATOM   736   C  CB  . LEU A  1 95  ? 7.565   -15.294 10.274  1.00 18.38 ? 94  LEU A CB  1 
ATOM   737   C  CG  . LEU A  1 95  ? 6.186   -15.662 10.797  1.00 18.94 ? 94  LEU A CG  1 
ATOM   738   C  CD1 . LEU A  1 95  ? 6.303   -16.700 11.901  1.00 20.22 ? 94  LEU A CD1 1 
ATOM   739   C  CD2 . LEU A  1 95  ? 5.420   -14.435 11.266  1.00 18.99 ? 94  LEU A CD2 1 
ATOM   740   N  N   . ASP A  1 96  ? 9.439   -14.769 7.685   1.00 19.82 ? 95  ASP A N   1 
ATOM   741   C  CA  . ASP A  1 96  ? 10.750  -14.584 7.068   1.00 22.30 ? 95  ASP A CA  1 
ATOM   742   C  C   . ASP A  1 96  ? 10.558  -13.902 5.733   1.00 22.84 ? 95  ASP A C   1 
ATOM   743   O  O   . ASP A  1 96  ? 9.918   -14.467 4.835   1.00 22.74 ? 95  ASP A O   1 
ATOM   744   C  CB  . ASP A  1 96  ? 11.438  -15.951 6.891   1.00 23.79 ? 95  ASP A CB  1 
ATOM   745   C  CG  . ASP A  1 96  ? 12.898  -15.835 6.475   1.00 26.81 ? 95  ASP A CG  1 
ATOM   746   O  OD1 . ASP A  1 96  ? 13.268  -14.843 5.827   1.00 28.42 ? 95  ASP A OD1 1 
ATOM   747   O  OD2 . ASP A  1 96  ? 13.684  -16.752 6.821   1.00 33.44 ? 95  ASP A OD2 1 
ATOM   748   N  N   . PRO A  1 97  ? 11.108  -12.692 5.561   1.00 24.67 ? 96  PRO A N   1 
ATOM   749   C  CA  . PRO A  1 97  ? 10.926  -11.979 4.288   1.00 26.95 ? 96  PRO A CA  1 
ATOM   750   C  C   . PRO A  1 97  ? 11.541  -12.666 3.066   1.00 28.16 ? 96  PRO A C   1 
ATOM   751   O  O   . PRO A  1 97  ? 11.211  -12.279 1.957   1.00 28.41 ? 96  PRO A O   1 
ATOM   752   C  CB  . PRO A  1 97  ? 11.589  -10.601 4.511   1.00 28.26 ? 96  PRO A CB  1 
ATOM   753   C  CG  . PRO A  1 97  ? 12.074  -10.593 5.915   1.00 27.58 ? 96  PRO A CG  1 
ATOM   754   C  CD  . PRO A  1 97  ? 11.969  -11.954 6.501   1.00 26.55 ? 96  PRO A CD  1 
ATOM   755   N  N   . SER A  1 98  ? 12.389  -13.677 3.248   1.00 27.12 ? 97  SER A N   1 
ATOM   756   C  CA  . SER A  1 98  ? 12.799  -14.533 2.130   1.00 30.91 ? 97  SER A CA  1 
ATOM   757   C  C   . SER A  1 98  ? 11.608  -15.352 1.579   1.00 30.28 ? 97  SER A C   1 
ATOM   758   O  O   . SER A  1 98  ? 11.706  -15.939 0.512   1.00 29.28 ? 97  SER A O   1 
ATOM   759   C  CB  . SER A  1 98  ? 13.872  -15.513 2.568   1.00 32.13 ? 97  SER A CB  1 
ATOM   760   O  OG  . SER A  1 98  ? 13.289  -16.553 3.337   1.00 35.23 ? 97  SER A OG  1 
ATOM   761   N  N   . LYS A  1 99  ? 10.516  -15.397 2.344   1.00 29.01 ? 98  LYS A N   1 
ATOM   762   C  CA  . LYS A  1 99  ? 9.291   -16.115 2.007   1.00 29.16 ? 98  LYS A CA  1 
ATOM   763   C  C   . LYS A  1 99  ? 9.478   -17.629 2.047   1.00 29.31 ? 98  LYS A C   1 
ATOM   764   O  O   . LYS A  1 99  ? 8.715   -18.379 1.450   1.00 29.92 ? 98  LYS A O   1 
ATOM   765   C  CB  . LYS A  1 99  ? 8.717   -15.632 0.683   1.00 29.94 ? 98  LYS A CB  1 
ATOM   766   C  CG  . LYS A  1 99  ? 8.408   -14.151 0.691   1.00 32.27 ? 98  LYS A CG  1 
ATOM   767   C  CD  . LYS A  1 99  ? 7.721   -13.727 -0.587  1.00 35.99 ? 98  LYS A CD  1 
ATOM   768   C  CE  . LYS A  1 99  ? 7.327   -12.271 -0.522  1.00 38.23 ? 98  LYS A CE  1 
ATOM   769   N  NZ  . LYS A  1 99  ? 6.583   -11.872 -1.753  1.00 42.57 ? 98  LYS A NZ  1 
ATOM   770   N  N   . SER A  1 100 ? 10.461  -18.061 2.825   1.00 28.54 ? 99  SER A N   1 
ATOM   771   C  CA  . SER A  1 100 ? 10.697  -19.463 3.102   1.00 30.68 ? 99  SER A CA  1 
ATOM   772   C  C   . SER A  1 100 ? 9.514   -20.118 3.812   1.00 28.46 ? 99  SER A C   1 
ATOM   773   O  O   . SER A  1 100 ? 8.805   -19.478 4.607   1.00 26.71 ? 99  SER A O   1 
ATOM   774   C  CB  . SER A  1 100 ? 11.925  -19.594 3.999   1.00 32.08 ? 99  SER A CB  1 
ATOM   775   O  OG  . SER A  1 100 ? 12.039  -20.923 4.468   1.00 37.01 ? 99  SER A OG  1 
ATOM   776   N  N   . SER A  1 101 ? 9.307   -21.404 3.545   1.00 27.80 ? 100 SER A N   1 
ATOM   777   C  CA  . SER A  1 101 ? 8.164   -22.136 4.129   1.00 27.65 ? 100 SER A CA  1 
ATOM   778   C  C   . SER A  1 101 ? 8.215   -22.178 5.644   1.00 27.11 ? 100 SER A C   1 
ATOM   779   O  O   . SER A  1 101 ? 7.170   -22.265 6.292   1.00 25.13 ? 100 SER A O   1 
ATOM   780   C  CB  . SER A  1 101 ? 8.087   -23.561 3.570   1.00 29.94 ? 100 SER A CB  1 
ATOM   781   O  OG  . SER A  1 101 ? 9.248   -24.283 3.889   1.00 32.17 ? 100 SER A OG  1 
ATOM   782   N  N   . VAL A  1 102 ? 9.432   -22.127 6.206   1.00 26.70 ? 101 VAL A N   1 
ATOM   783   C  CA  . VAL A  1 102 ? 9.627   -22.096 7.669   1.00 27.92 ? 101 VAL A CA  1 
ATOM   784   C  C   . VAL A  1 102 ? 8.837   -20.936 8.311   1.00 25.24 ? 101 VAL A C   1 
ATOM   785   O  O   . VAL A  1 102 ? 8.341   -21.058 9.428   1.00 25.51 ? 101 VAL A O   1 
ATOM   786   C  CB  . VAL A  1 102 ? 11.143  -22.025 8.075   1.00 32.27 ? 101 VAL A CB  1 
ATOM   787   C  CG1 . VAL A  1 102 ? 11.727  -20.645 7.796   1.00 34.72 ? 101 VAL A CG1 1 
ATOM   788   C  CG2 . VAL A  1 102 ? 11.309  -22.355 9.549   1.00 34.56 ? 101 VAL A CG2 1 
ATOM   789   N  N   . GLY A  1 103 ? 8.698   -19.830 7.605   1.00 22.02 ? 102 GLY A N   1 
ATOM   790   C  CA  . GLY A  1 103 ? 7.962   -18.718 8.145   1.00 21.07 ? 102 GLY A CA  1 
ATOM   791   C  C   . GLY A  1 103 ? 6.572   -18.507 7.586   1.00 20.82 ? 102 GLY A C   1 
ATOM   792   O  O   . GLY A  1 103 ? 5.967   -17.464 7.829   1.00 20.48 ? 102 GLY A O   1 
ATOM   793   N  N   . SER A  1 104 ? 6.039   -19.473 6.851   1.00 19.44 ? 103 SER A N   1 
ATOM   794   C  CA  . SER A  1 104 ? 4.711   -19.265 6.247   1.00 19.61 ? 103 SER A CA  1 
ATOM   795   C  C   . SER A  1 104 ? 3.672   -19.399 7.345   1.00 19.44 ? 103 SER A C   1 
ATOM   796   O  O   . SER A  1 104 ? 3.551   -20.455 7.959   1.00 19.99 ? 103 SER A O   1 
ATOM   797   C  CB  . SER A  1 104 ? 4.456   -20.277 5.127   1.00 20.13 ? 103 SER A CB  1 
ATOM   798   O  OG  . SER A  1 104 ? 3.151   -20.094 4.575   1.00 20.60 ? 103 SER A OG  1 
ATOM   799   N  N   . TYR A  1 105 ? 2.911   -18.337 7.604   1.00 17.95 ? 104 TYR A N   1 
ATOM   800   C  CA  . TYR A  1 105 ? 2.052   -18.301 8.788   1.00 16.47 ? 104 TYR A CA  1 
ATOM   801   C  C   . TYR A  1 105 ? 0.591   -18.031 8.349   1.00 16.57 ? 104 TYR A C   1 
ATOM   802   O  O   . TYR A  1 105 ? -0.180  -18.969 8.236   1.00 17.75 ? 104 TYR A O   1 
ATOM   803   C  CB  . TYR A  1 105 ? 2.614   -17.289 9.804   1.00 16.29 ? 104 TYR A CB  1 
ATOM   804   C  CG  . TYR A  1 105 ? 1.849   -17.129 11.102  1.00 15.25 ? 104 TYR A CG  1 
ATOM   805   C  CD1 . TYR A  1 105 ? 1.397   -18.231 11.814  1.00 16.19 ? 104 TYR A CD1 1 
ATOM   806   C  CD2 . TYR A  1 105 ? 1.592   -15.870 11.627  1.00 14.71 ? 104 TYR A CD2 1 
ATOM   807   C  CE1 . TYR A  1 105 ? 0.682   -18.075 13.009  1.00 15.98 ? 104 TYR A CE1 1 
ATOM   808   C  CE2 . TYR A  1 105 ? 0.876   -15.710 12.820  1.00 15.44 ? 104 TYR A CE2 1 
ATOM   809   C  CZ  . TYR A  1 105 ? 0.412   -16.806 13.500  1.00 15.71 ? 104 TYR A CZ  1 
ATOM   810   O  OH  . TYR A  1 105 ? -0.291  -16.622 14.689  1.00 15.99 ? 104 TYR A OH  1 
ATOM   811   N  N   . PHE A  1 106 ? 0.221   -16.778 8.086   1.00 16.27 ? 105 PHE A N   1 
ATOM   812   C  CA  . PHE A  1 106 ? -1.112  -16.487 7.546   1.00 15.92 ? 105 PHE A CA  1 
ATOM   813   C  C   . PHE A  1 106 ? -1.195  -16.612 6.004   1.00 16.12 ? 105 PHE A C   1 
ATOM   814   O  O   . PHE A  1 106 ? -2.266  -16.386 5.432   1.00 15.45 ? 105 PHE A O   1 
ATOM   815   C  CB  . PHE A  1 106 ? -1.589  -15.100 7.966   1.00 16.32 ? 105 PHE A CB  1 
ATOM   816   C  CG  . PHE A  1 106 ? -2.311  -15.045 9.280   1.00 16.83 ? 105 PHE A CG  1 
ATOM   817   C  CD1 . PHE A  1 106 ? -1.633  -14.808 10.457  1.00 17.57 ? 105 PHE A CD1 1 
ATOM   818   C  CD2 . PHE A  1 106 ? -3.683  -15.180 9.338   1.00 17.84 ? 105 PHE A CD2 1 
ATOM   819   C  CE1 . PHE A  1 106 ? -2.314  -14.722 11.684  1.00 18.41 ? 105 PHE A CE1 1 
ATOM   820   C  CE2 . PHE A  1 106 ? -4.365  -15.095 10.545  1.00 17.47 ? 105 PHE A CE2 1 
ATOM   821   C  CZ  . PHE A  1 106 ? -3.685  -14.865 11.721  1.00 17.42 ? 105 PHE A CZ  1 
ATOM   822   N  N   . HIS A  1 107 ? -0.095  -16.964 5.330   1.00 15.75 ? 106 HIS A N   1 
ATOM   823   C  CA  . HIS A  1 107 ? -0.096  -16.969 3.845   1.00 15.83 ? 106 HIS A CA  1 
ATOM   824   C  C   . HIS A  1 107 ? -1.183  -17.850 3.226   1.00 15.93 ? 106 HIS A C   1 
ATOM   825   O  O   . HIS A  1 107 ? -1.874  -17.419 2.314   1.00 15.83 ? 106 HIS A O   1 
ATOM   826   C  CB  . HIS A  1 107 ? 1.258   -17.349 3.271   1.00 15.92 ? 106 HIS A CB  1 
ATOM   827   C  CG  . HIS A  1 107 ? 1.367   -17.167 1.777   1.00 17.05 ? 106 HIS A CG  1 
ATOM   828   N  ND1 . HIS A  1 107 ? 1.061   -15.985 1.134   1.00 17.00 ? 106 HIS A ND1 1 
ATOM   829   C  CD2 . HIS A  1 107 ? 1.788   -18.017 0.814   1.00 17.77 ? 106 HIS A CD2 1 
ATOM   830   C  CE1 . HIS A  1 107 ? 1.284   -16.114 -0.159  1.00 17.50 ? 106 HIS A CE1 1 
ATOM   831   N  NE2 . HIS A  1 107 ? 1.736   -17.339 -0.378  1.00 18.09 ? 106 HIS A NE2 1 
ATOM   832   N  N   . THR A  1 108 ? -1.350  -19.065 3.713   1.00 16.14 ? 107 THR A N   1 
ATOM   833   C  CA  . THR A  1 108 ? -2.372  -19.956 3.153   1.00 17.43 ? 107 THR A CA  1 
ATOM   834   C  C   . THR A  1 108 ? -3.773  -19.368 3.299   1.00 16.95 ? 107 THR A C   1 
ATOM   835   O  O   . THR A  1 108 ? -4.590  -19.401 2.359   1.00 16.49 ? 107 THR A O   1 
ATOM   836   C  CB  . THR A  1 108 ? -2.332  -21.357 3.800   1.00 18.17 ? 107 THR A CB  1 
ATOM   837   O  OG1 . THR A  1 108 ? -1.041  -21.928 3.583   1.00 18.67 ? 107 THR A OG1 1 
ATOM   838   C  CG2 . THR A  1 108 ? -3.357  -22.274 3.194   1.00 19.24 ? 107 THR A CG2 1 
ATOM   839   N  N   . MET A  1 109 ? -4.057  -18.813 4.462   1.00 16.68 ? 108 MET A N   1 
ATOM   840   C  CA  . MET A  1 109 ? -5.364  -18.218 4.699   1.00 17.36 ? 108 MET A CA  1 
ATOM   841   C  C   . MET A  1 109 ? -5.613  -16.995 3.803   1.00 17.02 ? 108 MET A C   1 
ATOM   842   O  O   . MET A  1 109 ? -6.706  -16.814 3.286   1.00 17.26 ? 108 MET A O   1 
ATOM   843   C  CB  . MET A  1 109 ? -5.534  -17.827 6.171   1.00 17.68 ? 108 MET A CB  1 
ATOM   844   C  CG  . MET A  1 109 ? -6.848  -17.117 6.483   1.00 19.01 ? 108 MET A CG  1 
ATOM   845   S  SD  . MET A  1 109 ? -7.082  -16.732 8.227   1.00 20.39 ? 108 MET A SD  1 
ATOM   846   C  CE  . MET A  1 109 ? -7.250  -18.367 8.872   1.00 20.97 ? 108 MET A CE  1 
ATOM   847   N  N   . VAL A  1 110 ? -4.616  -16.141 3.654   1.00 15.86 ? 109 VAL A N   1 
ATOM   848   C  CA  . VAL A  1 110 ? -4.767  -14.949 2.827   1.00 16.05 ? 109 VAL A CA  1 
ATOM   849   C  C   . VAL A  1 110 ? -4.911  -15.336 1.349   1.00 16.85 ? 109 VAL A C   1 
ATOM   850   O  O   . VAL A  1 110 ? -5.736  -14.731 0.662   1.00 17.85 ? 109 VAL A O   1 
ATOM   851   C  CB  . VAL A  1 110 ? -3.651  -13.930 3.087   1.00 15.92 ? 109 VAL A CB  1 
ATOM   852   C  CG1 . VAL A  1 110 ? -3.788  -12.717 2.159   1.00 16.19 ? 109 VAL A CG1 1 
ATOM   853   C  CG2 . VAL A  1 110 ? -3.687  -13.438 4.530   1.00 16.08 ? 109 VAL A CG2 1 
ATOM   854   N  N   . GLU A  1 111 ? -4.165  -16.354 0.884   1.00 16.55 ? 110 GLU A N   1 
ATOM   855   C  CA  . GLU A  1 111 ? -4.388  -16.906 -0.483  1.00 17.06 ? 110 GLU A CA  1 
ATOM   856   C  C   . GLU A  1 111 ? -5.863  -17.282 -0.697  1.00 16.94 ? 110 GLU A C   1 
ATOM   857   O  O   . GLU A  1 111 ? -6.466  -16.918 -1.718  1.00 16.19 ? 110 GLU A O   1 
ATOM   858   C  CB  . GLU A  1 111 ? -3.522  -18.116 -0.765  1.00 17.87 ? 110 GLU A CB  1 
ATOM   859   C  CG  . GLU A  1 111 ? -2.057  -17.815 -0.963  1.00 18.51 ? 110 GLU A CG  1 
ATOM   860   C  CD  . GLU A  1 111 ? -1.754  -17.174 -2.274  1.00 18.47 ? 110 GLU A CD  1 
ATOM   861   O  OE1 . GLU A  1 111 ? -1.703  -17.909 -3.284  1.00 18.90 ? 110 GLU A OE1 1 
ATOM   862   O  OE2 . GLU A  1 111 ? -1.563  -15.925 -2.278  1.00 19.52 ? 110 GLU A OE2 1 
ATOM   863   N  N   . SER A  1 112 ? -6.452  -17.976 0.277   1.00 17.19 ? 111 SER A N   1 
ATOM   864   C  CA  . SER A  1 112 ? -7.883  -18.292 0.224   1.00 18.34 ? 111 SER A CA  1 
ATOM   865   C  C   . SER A  1 112 ? -8.812  -17.068 0.206   1.00 18.02 ? 111 SER A C   1 
ATOM   866   O  O   . SER A  1 112 ? -9.730  -16.991 -0.635  1.00 18.47 ? 111 SER A O   1 
ATOM   867   C  CB  . SER A  1 112 ? -8.257  -19.189 1.392   1.00 20.30 ? 111 SER A CB  1 
ATOM   868   O  OG  . SER A  1 112 ? -7.720  -20.499 1.221   1.00 22.56 ? 111 SER A OG  1 
ATOM   869   N  N   . LEU A  1 113 ? -8.566  -16.115 1.107   1.00 17.21 ? 112 LEU A N   1 
ATOM   870   C  CA  . LEU A  1 113 ? -9.362  -14.893 1.152   1.00 17.51 ? 112 LEU A CA  1 
ATOM   871   C  C   . LEU A  1 113 ? -9.331  -14.158 -0.202  1.00 17.29 ? 112 LEU A C   1 
ATOM   872   O  O   . LEU A  1 113 ? -10.360 -13.711 -0.701  1.00 17.22 ? 112 LEU A O   1 
ATOM   873   C  CB  . LEU A  1 113 ? -8.875  -13.966 2.266   1.00 18.50 ? 112 LEU A CB  1 
ATOM   874   C  CG  . LEU A  1 113 ? -9.205  -14.426 3.691   1.00 19.82 ? 112 LEU A CG  1 
ATOM   875   C  CD1 . LEU A  1 113 ? -8.356  -13.696 4.708   1.00 20.64 ? 112 LEU A CD1 1 
ATOM   876   C  CD2 . LEU A  1 113 ? -10.682 -14.181 3.979   1.00 20.70 ? 112 LEU A CD2 1 
ATOM   877   N  N   . VAL A  1 114 ? -8.133  -14.024 -0.772  1.00 16.43 ? 113 VAL A N   1 
ATOM   878   C  CA  . VAL A  1 114 ? -7.986  -13.349 -2.024  1.00 17.01 ? 113 VAL A CA  1 
ATOM   879   C  C   . VAL A  1 114 ? -8.740  -14.108 -3.157  1.00 18.29 ? 113 VAL A C   1 
ATOM   880   O  O   . VAL A  1 114 ? -9.415  -13.489 -4.003  1.00 17.08 ? 113 VAL A O   1 
ATOM   881   C  CB  . VAL A  1 114 ? -6.499  -13.102 -2.303  1.00 17.26 ? 113 VAL A CB  1 
ATOM   882   C  CG1 . VAL A  1 114 ? -6.269  -12.675 -3.748  1.00 18.72 ? 113 VAL A CG1 1 
ATOM   883   C  CG2 . VAL A  1 114 ? -5.970  -12.055 -1.335  1.00 16.58 ? 113 VAL A CG2 1 
ATOM   884   N  N   . GLY A  1 115 ? -8.665  -15.439 -3.150  1.00 18.13 ? 114 GLY A N   1 
ATOM   885   C  CA  . GLY A  1 115 ? -9.429  -16.240 -4.074  1.00 20.35 ? 114 GLY A CA  1 
ATOM   886   C  C   . GLY A  1 115 ? -10.940 -16.035 -3.936  1.00 21.38 ? 114 GLY A C   1 
ATOM   887   O  O   . GLY A  1 115 ? -11.666 -16.200 -4.903  1.00 22.36 ? 114 GLY A O   1 
ATOM   888   N  N   . TRP A  1 116 ? -11.396 -15.677 -2.738  1.00 21.39 ? 115 TRP A N   1 
ATOM   889   C  CA  . TRP A  1 116 ? -12.801 -15.388 -2.468  1.00 21.73 ? 115 TRP A CA  1 
ATOM   890   C  C   . TRP A  1 116 ? -13.189 -13.955 -2.803  1.00 22.72 ? 115 TRP A C   1 
ATOM   891   O  O   . TRP A  1 116 ? -14.353 -13.600 -2.694  1.00 24.96 ? 115 TRP A O   1 
ATOM   892   C  CB  . TRP A  1 116 ? -13.141 -15.658 -1.003  1.00 21.13 ? 115 TRP A CB  1 
ATOM   893   C  CG  . TRP A  1 116 ? -12.866 -17.055 -0.542  1.00 20.87 ? 115 TRP A CG  1 
ATOM   894   C  CD1 . TRP A  1 116 ? -12.774 -18.185 -1.316  1.00 22.33 ? 115 TRP A CD1 1 
ATOM   895   C  CD2 . TRP A  1 116 ? -12.639 -17.468 0.791   1.00 21.02 ? 115 TRP A CD2 1 
ATOM   896   N  NE1 . TRP A  1 116 ? -12.498 -19.289 -0.528  1.00 22.54 ? 115 TRP A NE1 1 
ATOM   897   C  CE2 . TRP A  1 116 ? -12.386 -18.864 0.772   1.00 22.04 ? 115 TRP A CE2 1 
ATOM   898   C  CE3 . TRP A  1 116 ? -12.591 -16.794 2.005   1.00 21.05 ? 115 TRP A CE3 1 
ATOM   899   C  CZ2 . TRP A  1 116 ? -12.120 -19.584 1.923   1.00 21.46 ? 115 TRP A CZ2 1 
ATOM   900   C  CZ3 . TRP A  1 116 ? -12.320 -17.514 3.156   1.00 21.42 ? 115 TRP A CZ3 1 
ATOM   901   C  CH2 . TRP A  1 116 ? -12.073 -18.898 3.098   1.00 21.81 ? 115 TRP A CH2 1 
ATOM   902   N  N   . GLY A  1 117 ? -12.233 -13.128 -3.203  1.00 22.13 ? 116 GLY A N   1 
ATOM   903   C  CA  . GLY A  1 117 ? -12.525 -11.760 -3.630  1.00 22.14 ? 116 GLY A CA  1 
ATOM   904   C  C   . GLY A  1 117 ? -11.986 -10.635 -2.783  1.00 20.99 ? 116 GLY A C   1 
ATOM   905   O  O   . GLY A  1 117 ? -12.244 -9.465  -3.098  1.00 20.88 ? 116 GLY A O   1 
ATOM   906   N  N   . TYR A  1 118 ? -11.225 -10.959 -1.731  1.00 18.78 ? 117 TYR A N   1 
ATOM   907   C  CA  . TYR A  1 118 ? -10.597 -9.954  -0.888  1.00 18.52 ? 117 TYR A CA  1 
ATOM   908   C  C   . TYR A  1 118 ? -9.387  -9.360  -1.575  1.00 18.66 ? 117 TYR A C   1 
ATOM   909   O  O   . TYR A  1 118 ? -8.802  -9.995  -2.460  1.00 19.12 ? 117 TYR A O   1 
ATOM   910   C  CB  . TYR A  1 118 ? -10.186 -10.543 0.488   1.00 17.02 ? 117 TYR A CB  1 
ATOM   911   C  CG  . TYR A  1 118 ? -11.375 -10.684 1.383   1.00 17.40 ? 117 TYR A CG  1 
ATOM   912   C  CD1 . TYR A  1 118 ? -12.197 -11.801 1.306   1.00 18.27 ? 117 TYR A CD1 1 
ATOM   913   C  CD2 . TYR A  1 118 ? -11.703 -9.677  2.304   1.00 17.48 ? 117 TYR A CD2 1 
ATOM   914   C  CE1 . TYR A  1 118 ? -13.325 -11.927 2.112   1.00 18.57 ? 117 TYR A CE1 1 
ATOM   915   C  CE2 . TYR A  1 118 ? -12.831 -9.770  3.100   1.00 17.65 ? 117 TYR A CE2 1 
ATOM   916   C  CZ  . TYR A  1 118 ? -13.637 -10.907 3.012   1.00 18.48 ? 117 TYR A CZ  1 
ATOM   917   O  OH  . TYR A  1 118 ? -14.757 -11.009 3.787   1.00 19.23 ? 117 TYR A OH  1 
ATOM   918   N  N   . THR A  1 119 ? -8.993  -8.180  -1.109  1.00 18.35 ? 118 THR A N   1 
ATOM   919   C  CA  . THR A  1 119 ? -7.837  -7.432  -1.645  1.00 18.42 ? 118 THR A CA  1 
ATOM   920   C  C   . THR A  1 119 ? -6.880  -7.121  -0.508  1.00 17.34 ? 118 THR A C   1 
ATOM   921   O  O   . THR A  1 119 ? -7.245  -6.414  0.445   1.00 16.72 ? 118 THR A O   1 
ATOM   922   C  CB  . THR A  1 119 ? -8.301  -6.114  -2.334  1.00 19.76 ? 118 THR A CB  1 
ATOM   923   O  OG1 . THR A  1 119 ? -9.188  -6.425  -3.402  1.00 22.06 ? 118 THR A OG1 1 
ATOM   924   C  CG2 . THR A  1 119 ? -7.139  -5.309  -2.886  1.00 19.71 ? 118 THR A CG2 1 
ATOM   925   N  N   . ARG A  1 120 ? -5.635  -7.607  -0.609  1.00 16.84 ? 119 ARG A N   1 
ATOM   926   C  CA  . ARG A  1 120 ? -4.610  -7.374  0.423   1.00 16.45 ? 119 ARG A CA  1 
ATOM   927   C  C   . ARG A  1 120 ? -4.397  -5.901  0.699   1.00 17.41 ? 119 ARG A C   1 
ATOM   928   O  O   . ARG A  1 120 ? -4.209  -5.122  -0.238  1.00 17.40 ? 119 ARG A O   1 
ATOM   929   C  CB  . ARG A  1 120 ? -3.252  -7.947  -0.002  1.00 16.19 ? 119 ARG A CB  1 
ATOM   930   C  CG  . ARG A  1 120 ? -3.162  -9.452  0.071   1.00 15.95 ? 119 ARG A CG  1 
ATOM   931   C  CD  . ARG A  1 120 ? -1.850  -9.920  -0.538  1.00 15.75 ? 119 ARG A CD  1 
ATOM   932   N  NE  . ARG A  1 120 ? -1.610  -11.324 -0.262  1.00 15.50 ? 119 ARG A NE  1 
ATOM   933   C  CZ  . ARG A  1 120 ? -1.908  -12.344 -1.059  1.00 15.86 ? 119 ARG A CZ  1 
ATOM   934   N  NH1 . ARG A  1 120 ? -2.444  -12.152 -2.264  1.00 16.87 ? 119 ARG A NH1 1 
ATOM   935   N  NH2 . ARG A  1 120 ? -1.664  -13.558 -0.648  1.00 16.14 ? 119 ARG A NH2 1 
ATOM   936   N  N   . GLY A  1 121 ? -4.451  -5.498  1.967   1.00 17.07 ? 120 GLY A N   1 
ATOM   937   C  CA  . GLY A  1 121 ? -4.175  -4.096  2.362   1.00 17.09 ? 120 GLY A CA  1 
ATOM   938   C  C   . GLY A  1 121 ? -5.384  -3.198  2.264   1.00 17.77 ? 120 GLY A C   1 
ATOM   939   O  O   . GLY A  1 121 ? -5.322  -2.013  2.638   1.00 19.00 ? 120 GLY A O   1 
ATOM   940   N  N   . GLU A  1 122 ? -6.480  -3.738  1.734   1.00 17.59 ? 121 GLU A N   1 
ATOM   941   C  CA  A GLU A  1 122 ? -7.713  -2.979  1.578   0.50 17.81 ? 121 GLU A CA  1 
ATOM   942   C  CA  B GLU A  1 122 ? -7.716  -2.973  1.579   0.50 17.74 ? 121 GLU A CA  1 
ATOM   943   C  C   . GLU A  1 122 ? -8.780  -3.572  2.495   1.00 16.65 ? 121 GLU A C   1 
ATOM   944   O  O   . GLU A  1 122 ? -8.856  -3.192  3.661   1.00 16.20 ? 121 GLU A O   1 
ATOM   945   C  CB  A GLU A  1 122 ? -8.092  -2.895  0.085   0.50 19.18 ? 121 GLU A CB  1 
ATOM   946   C  CB  B GLU A  1 122 ? -8.152  -2.912  0.104   0.50 18.92 ? 121 GLU A CB  1 
ATOM   947   C  CG  A GLU A  1 122 ? -6.953  -2.139  -0.656  0.50 20.84 ? 121 GLU A CG  1 
ATOM   948   C  CG  B GLU A  1 122 ? -7.301  -2.031  -0.780  0.50 20.43 ? 121 GLU A CG  1 
ATOM   949   C  CD  A GLU A  1 122 ? -7.092  -1.792  -2.097  0.50 21.81 ? 121 GLU A CD  1 
ATOM   950   C  CD  B GLU A  1 122 ? -7.771  -0.591  -0.775  0.50 20.89 ? 121 GLU A CD  1 
ATOM   951   O  OE1 A GLU A  1 122 ? -8.155  -2.037  -2.657  0.50 23.50 ? 121 GLU A OE1 1 
ATOM   952   O  OE1 B GLU A  1 122 ? -8.825  -0.290  -0.155  0.50 20.30 ? 121 GLU A OE1 1 
ATOM   953   O  OE2 A GLU A  1 122 ? -6.050  -1.293  -2.644  0.50 23.06 ? 121 GLU A OE2 1 
ATOM   954   O  OE2 B GLU A  1 122 ? -7.050  0.236   -1.378  0.50 21.14 ? 121 GLU A OE2 1 
ATOM   955   N  N   . ASP A  1 123 ? -9.560  -4.523  2.008   1.00 16.01 ? 122 ASP A N   1 
ATOM   956   C  CA  . ASP A  1 123 ? -10.634 -5.089  2.830   1.00 15.90 ? 122 ASP A CA  1 
ATOM   957   C  C   . ASP A  1 123 ? -10.192 -6.319  3.652   1.00 15.20 ? 122 ASP A C   1 
ATOM   958   O  O   . ASP A  1 123 ? -10.987 -6.863  4.395   1.00 13.66 ? 122 ASP A O   1 
ATOM   959   C  CB  . ASP A  1 123 ? -11.914 -5.327  2.023   1.00 16.77 ? 122 ASP A CB  1 
ATOM   960   C  CG  . ASP A  1 123 ? -11.718 -6.211  0.836   1.00 17.94 ? 122 ASP A CG  1 
ATOM   961   O  OD1 . ASP A  1 123 ? -10.586 -6.658  0.550   1.00 18.14 ? 122 ASP A OD1 1 
ATOM   962   O  OD2 . ASP A  1 123 ? -12.721 -6.484  0.179   1.00 18.50 ? 122 ASP A OD2 1 
ATOM   963   N  N   . VAL A  1 124 ? -8.938  -6.742  3.489   1.00 14.31 ? 123 VAL A N   1 
ATOM   964   C  CA  . VAL A  1 124 ? -8.278  -7.608  4.449   1.00 14.73 ? 123 VAL A CA  1 
ATOM   965   C  C   . VAL A  1 124 ? -6.988  -6.925  4.882   1.00 14.69 ? 123 VAL A C   1 
ATOM   966   O  O   . VAL A  1 124 ? -6.164  -6.558  4.019   1.00 14.49 ? 123 VAL A O   1 
ATOM   967   C  CB  . VAL A  1 124 ? -8.051  -9.052  3.958   1.00 15.77 ? 123 VAL A CB  1 
ATOM   968   C  CG1 . VAL A  1 124 ? -7.216  -9.133  2.683   1.00 15.84 ? 123 VAL A CG1 1 
ATOM   969   C  CG2 . VAL A  1 124 ? -7.403  -9.854  5.072   1.00 16.26 ? 123 VAL A CG2 1 
ATOM   970   N  N   . ARG A  1 125 ? -6.852  -6.689  6.193   1.00 13.77 ? 124 ARG A N   1 
ATOM   971   C  CA  . ARG A  1 125 ? -5.662  -6.018  6.745   1.00 13.85 ? 124 ARG A CA  1 
ATOM   972   C  C   . ARG A  1 125 ? -5.143  -6.749  7.945   1.00 14.24 ? 124 ARG A C   1 
ATOM   973   O  O   . ARG A  1 125 ? -5.932  -7.330  8.715   1.00 14.89 ? 124 ARG A O   1 
ATOM   974   C  CB  . ARG A  1 125 ? -5.995  -4.582  7.159   1.00 13.54 ? 124 ARG A CB  1 
ATOM   975   C  CG  . ARG A  1 125 ? -6.514  -3.734  6.001   1.00 14.46 ? 124 ARG A CG  1 
ATOM   976   C  CD  . ARG A  1 125 ? -6.634  -2.265  6.390   1.00 14.81 ? 124 ARG A CD  1 
ATOM   977   N  NE  . ARG A  1 125 ? -7.396  -1.516  5.414   1.00 15.62 ? 124 ARG A NE  1 
ATOM   978   C  CZ  . ARG A  1 125 ? -7.560  -0.206  5.448   1.00 17.29 ? 124 ARG A CZ  1 
ATOM   979   N  NH1 . ARG A  1 125 ? -6.991  0.531   6.409   1.00 18.58 ? 124 ARG A NH1 1 
ATOM   980   N  NH2 . ARG A  1 125 ? -8.309  0.380   4.527   1.00 17.51 ? 124 ARG A NH2 1 
ATOM   981   N  N   . GLY A  1 126 ? -3.833  -6.725  8.123   1.00 13.37 ? 125 GLY A N   1 
ATOM   982   C  CA  . GLY A  1 126 ? -3.231  -7.241  9.347   1.00 14.11 ? 125 GLY A CA  1 
ATOM   983   C  C   . GLY A  1 126 ? -3.081  -6.218  10.446  1.00 14.22 ? 125 GLY A C   1 
ATOM   984   O  O   . GLY A  1 126 ? -2.900  -5.011  10.201  1.00 15.27 ? 125 GLY A O   1 
ATOM   985   N  N   . ALA A  1 127 ? -3.135  -6.704  11.677  1.00 14.29 ? 126 ALA A N   1 
ATOM   986   C  CA  . ALA A  1 127 ? -2.877  -5.899  12.877  1.00 13.73 ? 126 ALA A CA  1 
ATOM   987   C  C   . ALA A  1 127 ? -1.696  -6.496  13.671  1.00 13.71 ? 126 ALA A C   1 
ATOM   988   O  O   . ALA A  1 127 ? -1.863  -7.003  14.790  1.00 14.30 ? 126 ALA A O   1 
ATOM   989   C  CB  . ALA A  1 127 ? -4.132  -5.809  13.711  1.00 14.03 ? 126 ALA A CB  1 
ATOM   990   N  N   . PRO A  1 128 ? -0.477  -6.468  13.076  1.00 13.05 ? 127 PRO A N   1 
ATOM   991   C  CA  . PRO A  1 128 ? 0.709   -6.949  13.785  1.00 12.58 ? 127 PRO A CA  1 
ATOM   992   C  C   . PRO A  1 128 ? 1.080   -6.049  14.988  1.00 13.90 ? 127 PRO A C   1 
ATOM   993   O  O   . PRO A  1 128 ? 0.735   -4.850  15.027  1.00 12.44 ? 127 PRO A O   1 
ATOM   994   C  CB  . PRO A  1 128 ? 1.810   -6.873  12.713  1.00 13.04 ? 127 PRO A CB  1 
ATOM   995   C  CG  . PRO A  1 128 ? 1.370   -5.730  11.849  1.00 12.62 ? 127 PRO A CG  1 
ATOM   996   C  CD  . PRO A  1 128 ? -0.127  -5.910  11.754  1.00 12.86 ? 127 PRO A CD  1 
ATOM   997   N  N   . TYR A  1 129 ? 1.791   -6.630  15.957  1.00 13.95 ? 128 TYR A N   1 
ATOM   998   C  CA  . TYR A  1 129 ? 2.151   -5.907  17.164  1.00 13.60 ? 128 TYR A CA  1 
ATOM   999   C  C   . TYR A  1 129 ? 3.456   -6.451  17.706  1.00 13.57 ? 128 TYR A C   1 
ATOM   1000  O  O   . TYR A  1 129 ? 3.956   -7.493  17.262  1.00 13.02 ? 128 TYR A O   1 
ATOM   1001  C  CB  . TYR A  1 129 ? 1.036   -5.986  18.224  1.00 14.09 ? 128 TYR A CB  1 
ATOM   1002  C  CG  . TYR A  1 129 ? 0.616   -7.392  18.592  1.00 13.59 ? 128 TYR A CG  1 
ATOM   1003  C  CD1 . TYR A  1 129 ? -0.302  -8.095  17.810  1.00 14.41 ? 128 TYR A CD1 1 
ATOM   1004  C  CD2 . TYR A  1 129 ? 1.127   -8.015  19.724  1.00 14.37 ? 128 TYR A CD2 1 
ATOM   1005  C  CE1 . TYR A  1 129 ? -0.663  -9.396  18.145  1.00 14.22 ? 128 TYR A CE1 1 
ATOM   1006  C  CE2 . TYR A  1 129 ? 0.748   -9.302  20.094  1.00 14.20 ? 128 TYR A CE2 1 
ATOM   1007  C  CZ  . TYR A  1 129 ? -0.126  -10.001 19.293  1.00 14.33 ? 128 TYR A CZ  1 
ATOM   1008  O  OH  . TYR A  1 129 ? -0.483  -11.291 19.614  1.00 14.28 ? 128 TYR A OH  1 
ATOM   1009  N  N   . ASP A  1 130 ? 4.011   -5.762  18.704  1.00 14.49 ? 129 ASP A N   1 
ATOM   1010  C  CA  . ASP A  1 130 ? 5.225   -6.261  19.374  1.00 14.75 ? 129 ASP A CA  1 
ATOM   1011  C  C   . ASP A  1 130 ? 4.794   -7.315  20.373  1.00 15.03 ? 129 ASP A C   1 
ATOM   1012  O  O   . ASP A  1 130 ? 4.427   -7.011  21.517  1.00 14.41 ? 129 ASP A O   1 
ATOM   1013  C  CB  . ASP A  1 130 ? 5.983   -5.120  20.075  1.00 16.30 ? 129 ASP A CB  1 
ATOM   1014  C  CG  . ASP A  1 130 ? 7.321   -5.568  20.634  1.00 17.49 ? 129 ASP A CG  1 
ATOM   1015  O  OD1 . ASP A  1 130 ? 7.569   -6.794  20.762  1.00 17.26 ? 129 ASP A OD1 1 
ATOM   1016  O  OD2 . ASP A  1 130 ? 8.157   -4.671  20.885  1.00 19.61 ? 129 ASP A OD2 1 
ATOM   1017  N  N   . TRP A  1 131 ? 4.835   -8.560  19.922  1.00 14.56 ? 130 TRP A N   1 
ATOM   1018  C  CA  . TRP A  1 131 ? 4.313   -9.692  20.681  1.00 14.93 ? 130 TRP A CA  1 
ATOM   1019  C  C   . TRP A  1 131 ? 5.188   -10.097 21.880  1.00 15.55 ? 130 TRP A C   1 
ATOM   1020  O  O   . TRP A  1 131 ? 4.804   -10.985 22.644  1.00 15.62 ? 130 TRP A O   1 
ATOM   1021  C  CB  . TRP A  1 131 ? 4.067   -10.885 19.751  1.00 15.35 ? 130 TRP A CB  1 
ATOM   1022  C  CG  . TRP A  1 131 ? 5.102   -11.018 18.655  1.00 15.75 ? 130 TRP A CG  1 
ATOM   1023  C  CD1 . TRP A  1 131 ? 4.945   -10.678 17.329  1.00 16.11 ? 130 TRP A CD1 1 
ATOM   1024  C  CD2 . TRP A  1 131 ? 6.457   -11.486 18.789  1.00 16.05 ? 130 TRP A CD2 1 
ATOM   1025  N  NE1 . TRP A  1 131 ? 6.085   -10.927 16.641  1.00 16.69 ? 130 TRP A NE1 1 
ATOM   1026  C  CE2 . TRP A  1 131 ? 7.050   -11.391 17.506  1.00 17.17 ? 130 TRP A CE2 1 
ATOM   1027  C  CE3 . TRP A  1 131 ? 7.227   -11.956 19.868  1.00 16.33 ? 130 TRP A CE3 1 
ATOM   1028  C  CZ2 . TRP A  1 131 ? 8.361   -11.777 17.255  1.00 17.24 ? 130 TRP A CZ2 1 
ATOM   1029  C  CZ3 . TRP A  1 131 ? 8.550   -12.343 19.620  1.00 17.33 ? 130 TRP A CZ3 1 
ATOM   1030  C  CH2 . TRP A  1 131 ? 9.106   -12.248 18.316  1.00 17.60 ? 130 TRP A CH2 1 
ATOM   1031  N  N   . ARG A  1 132 ? 6.337   -9.445  22.064  1.00 14.98 ? 131 ARG A N   1 
ATOM   1032  C  CA  . ARG A  1 132 ? 7.137   -9.639  23.281  1.00 16.23 ? 131 ARG A CA  1 
ATOM   1033  C  C   . ARG A  1 132 ? 6.467   -8.998  24.501  1.00 16.97 ? 131 ARG A C   1 
ATOM   1034  O  O   . ARG A  1 132 ? 6.759   -9.378  25.650  1.00 18.18 ? 131 ARG A O   1 
ATOM   1035  C  CB  . ARG A  1 132 ? 8.534   -9.041  23.101  1.00 16.29 ? 131 ARG A CB  1 
ATOM   1036  C  CG  . ARG A  1 132 ? 9.306   -9.689  21.955  1.00 16.61 ? 131 ARG A CG  1 
ATOM   1037  C  CD  . ARG A  1 132 ? 10.576  -8.919  21.625  1.00 16.95 ? 131 ARG A CD  1 
ATOM   1038  N  NE  . ARG A  1 132 ? 10.285  -7.533  21.340  1.00 16.98 ? 131 ARG A NE  1 
ATOM   1039  C  CZ  . ARG A  1 132 ? 11.188  -6.550  21.326  1.00 18.75 ? 131 ARG A CZ  1 
ATOM   1040  N  NH1 . ARG A  1 132 ? 12.460  -6.800  21.602  1.00 20.01 ? 131 ARG A NH1 1 
ATOM   1041  N  NH2 . ARG A  1 132 ? 10.801  -5.295  21.100  1.00 18.35 ? 131 ARG A NH2 1 
ATOM   1042  N  N   . ARG A  1 133 ? 5.609   -8.002  24.258  1.00 16.53 ? 132 ARG A N   1 
ATOM   1043  C  CA  . ARG A  1 133 ? 4.929   -7.277  25.297  1.00 18.11 ? 132 ARG A CA  1 
ATOM   1044  C  C   . ARG A  1 133 ? 3.500   -7.760  25.480  1.00 17.45 ? 132 ARG A C   1 
ATOM   1045  O  O   . ARG A  1 133 ? 2.900   -8.359  24.563  1.00 17.38 ? 132 ARG A O   1 
ATOM   1046  C  CB  . ARG A  1 133 ? 4.951   -5.787  24.972  1.00 20.43 ? 132 ARG A CB  1 
ATOM   1047  C  CG  . ARG A  1 133 ? 6.344   -5.212  25.209  1.00 24.88 ? 132 ARG A CG  1 
ATOM   1048  C  CD  . ARG A  1 133 ? 6.562   -3.859  24.598  1.00 28.29 ? 132 ARG A CD  1 
ATOM   1049  N  NE  . ARG A  1 133 ? 7.630   -3.153  25.314  1.00 32.35 ? 132 ARG A NE  1 
ATOM   1050  C  CZ  . ARG A  1 133 ? 8.154   -1.994  24.939  1.00 36.19 ? 132 ARG A CZ  1 
ATOM   1051  N  NH1 . ARG A  1 133 ? 7.749   -1.389  23.832  1.00 37.29 ? 132 ARG A NH1 1 
ATOM   1052  N  NH2 . ARG A  1 133 ? 9.098   -1.442  25.675  1.00 38.18 ? 132 ARG A NH2 1 
ATOM   1053  N  N   . ALA A  1 134 ? 2.953   -7.469  26.649  1.00 16.70 ? 133 ALA A N   1 
ATOM   1054  C  CA  . ALA A  1 134 ? 1.541   -7.715  26.935  1.00 15.55 ? 133 ALA A CA  1 
ATOM   1055  C  C   . ALA A  1 134 ? 0.761   -6.438  26.666  1.00 15.68 ? 133 ALA A C   1 
ATOM   1056  O  O   . ALA A  1 134 ? 1.359   -5.393  26.382  1.00 16.39 ? 133 ALA A O   1 
ATOM   1057  C  CB  . ALA A  1 134 ? 1.383   -8.141  28.387  1.00 15.73 ? 133 ALA A CB  1 
ATOM   1058  N  N   . PRO A  1 135 ? -0.583  -6.487  26.756  1.00 15.50 ? 134 PRO A N   1 
ATOM   1059  C  CA  . PRO A  1 135 ? -1.354  -5.317  26.317  1.00 15.63 ? 134 PRO A CA  1 
ATOM   1060  C  C   . PRO A  1 135 ? -1.107  -4.014  27.061  1.00 16.83 ? 134 PRO A C   1 
ATOM   1061  O  O   . PRO A  1 135 ? -1.299  -2.931  26.478  1.00 18.27 ? 134 PRO A O   1 
ATOM   1062  C  CB  . PRO A  1 135 ? -2.809  -5.785  26.486  1.00 15.54 ? 134 PRO A CB  1 
ATOM   1063  C  CG  . PRO A  1 135 ? -2.712  -7.242  26.189  1.00 15.39 ? 134 PRO A CG  1 
ATOM   1064  C  CD  . PRO A  1 135 ? -1.434  -7.688  26.838  1.00 15.64 ? 134 PRO A CD  1 
ATOM   1065  N  N   . ASN A  1 136 ? -0.629  -4.094  28.305  1.00 17.37 ? 135 ASN A N   1 
ATOM   1066  C  CA  . ASN A  1 136 ? -0.329  -2.915  29.090  1.00 19.14 ? 135 ASN A CA  1 
ATOM   1067  C  C   . ASN A  1 136 ? 0.765   -2.041  28.489  1.00 20.06 ? 135 ASN A C   1 
ATOM   1068  O  O   . ASN A  1 136 ? 0.820   -0.846  28.793  1.00 20.74 ? 135 ASN A O   1 
ATOM   1069  C  CB  . ASN A  1 136 ? 0.060   -3.266  30.539  1.00 19.29 ? 135 ASN A CB  1 
ATOM   1070  C  CG  . ASN A  1 136 ? 1.304   -4.128  30.628  1.00 19.74 ? 135 ASN A CG  1 
ATOM   1071  O  OD1 . ASN A  1 136 ? 1.519   -5.010  29.810  1.00 20.04 ? 135 ASN A OD1 1 
ATOM   1072  N  ND2 . ASN A  1 136 ? 2.173   -3.822  31.583  1.00 21.49 ? 135 ASN A ND2 1 
ATOM   1073  N  N   . GLU A  1 137 ? 1.613   -2.612  27.642  1.00 19.61 ? 136 GLU A N   1 
ATOM   1074  C  CA  . GLU A  1 137 ? 2.640   -1.844  26.962  1.00 20.62 ? 136 GLU A CA  1 
ATOM   1075  C  C   . GLU A  1 137 ? 2.428   -1.757  25.451  1.00 20.28 ? 136 GLU A C   1 
ATOM   1076  O  O   . GLU A  1 137 ? 3.371   -1.508  24.691  1.00 21.26 ? 136 GLU A O   1 
ATOM   1077  C  CB  . GLU A  1 137 ? 4.011   -2.424  27.290  1.00 21.74 ? 136 GLU A CB  1 
ATOM   1078  C  CG  . GLU A  1 137 ? 4.329   -2.289  28.769  1.00 25.16 ? 136 GLU A CG  1 
ATOM   1079  C  CD  . GLU A  1 137 ? 5.754   -2.723  29.113  1.00 28.63 ? 136 GLU A CD  1 
ATOM   1080  O  OE1 . GLU A  1 137 ? 6.498   -1.807  29.499  1.00 36.46 ? 136 GLU A OE1 1 
ATOM   1081  O  OE2 . GLU A  1 137 ? 6.140   -3.927  28.989  1.00 26.87 ? 136 GLU A OE2 1 
ATOM   1082  N  N   . ASN A  1 138 ? 1.186   -1.894  25.020  1.00 18.73 ? 137 ASN A N   1 
ATOM   1083  C  CA  . ASN A  1 138 ? 0.831   -1.767  23.632  1.00 18.25 ? 137 ASN A CA  1 
ATOM   1084  C  C   . ASN A  1 138 ? -0.382  -0.862  23.439  1.00 18.83 ? 137 ASN A C   1 
ATOM   1085  O  O   . ASN A  1 138 ? -1.176  -1.053  22.512  1.00 18.48 ? 137 ASN A O   1 
ATOM   1086  C  CB  . ASN A  1 138 ? 0.655   -3.163  22.994  1.00 17.93 ? 137 ASN A CB  1 
ATOM   1087  C  CG  . ASN A  1 138 ? 1.904   -3.617  22.242  1.00 19.12 ? 137 ASN A CG  1 
ATOM   1088  O  OD1 . ASN A  1 138 ? 2.517   -2.816  21.549  1.00 22.37 ? 137 ASN A OD1 1 
ATOM   1089  N  ND2 . ASN A  1 138 ? 2.275   -4.885  22.360  1.00 17.88 ? 137 ASN A ND2 1 
ATOM   1090  N  N   . GLY A  1 139 ? -0.478  0.178   24.271  1.00 19.07 ? 138 GLY A N   1 
ATOM   1091  C  CA  . GLY A  1 139 ? -1.557  1.165   24.166  1.00 18.98 ? 138 GLY A CA  1 
ATOM   1092  C  C   . GLY A  1 139 ? -1.711  1.744   22.762  1.00 19.04 ? 138 GLY A C   1 
ATOM   1093  O  O   . GLY A  1 139 ? -2.826  1.794   22.219  1.00 18.18 ? 138 GLY A O   1 
ATOM   1094  N  N   . PRO A  1 140 ? -0.612  2.234   22.167  1.00 19.71 ? 139 PRO A N   1 
ATOM   1095  C  CA  . PRO A  1 140 ? -0.709  2.839   20.828  1.00 19.52 ? 139 PRO A CA  1 
ATOM   1096  C  C   . PRO A  1 140 ? -1.245  1.861   19.757  1.00 19.26 ? 139 PRO A C   1 
ATOM   1097  O  O   . PRO A  1 140 ? -2.032  2.260   18.883  1.00 19.46 ? 139 PRO A O   1 
ATOM   1098  C  CB  . PRO A  1 140 ? 0.745   3.277   20.535  1.00 21.53 ? 139 PRO A CB  1 
ATOM   1099  C  CG  . PRO A  1 140 ? 1.286   3.575   21.897  1.00 21.05 ? 139 PRO A CG  1 
ATOM   1100  C  CD  . PRO A  1 140 ? 0.705   2.501   22.790  1.00 21.36 ? 139 PRO A CD  1 
ATOM   1101  N  N   . TYR A  1 141 ? -0.870  0.588   19.856  1.00 16.53 ? 140 TYR A N   1 
ATOM   1102  C  CA  . TYR A  1 141 ? -1.435  -0.433  18.978  1.00 16.24 ? 140 TYR A CA  1 
ATOM   1103  C  C   . TYR A  1 141 ? -2.973  -0.469  19.038  1.00 15.71 ? 140 TYR A C   1 
ATOM   1104  O  O   . TYR A  1 141 ? -3.634  -0.536  17.996  1.00 15.92 ? 140 TYR A O   1 
ATOM   1105  C  CB  . TYR A  1 141 ? -0.879  -1.804  19.353  1.00 16.05 ? 140 TYR A CB  1 
ATOM   1106  C  CG  . TYR A  1 141 ? -1.588  -2.970  18.728  1.00 15.37 ? 140 TYR A CG  1 
ATOM   1107  C  CD1 . TYR A  1 141 ? -1.303  -3.365  17.426  1.00 15.39 ? 140 TYR A CD1 1 
ATOM   1108  C  CD2 . TYR A  1 141 ? -2.542  -3.720  19.449  1.00 15.88 ? 140 TYR A CD2 1 
ATOM   1109  C  CE1 . TYR A  1 141 ? -1.934  -4.461  16.847  1.00 15.35 ? 140 TYR A CE1 1 
ATOM   1110  C  CE2 . TYR A  1 141 ? -3.145  -4.817  18.879  1.00 15.42 ? 140 TYR A CE2 1 
ATOM   1111  C  CZ  . TYR A  1 141 ? -2.856  -5.175  17.576  1.00 15.39 ? 140 TYR A CZ  1 
ATOM   1112  O  OH  . TYR A  1 141 ? -3.473  -6.272  16.993  1.00 16.37 ? 140 TYR A OH  1 
ATOM   1113  N  N   . PHE A  1 142 ? -3.542  -0.449  20.239  1.00 16.53 ? 141 PHE A N   1 
ATOM   1114  C  CA  . PHE A  1 142 ? -5.002  -0.536  20.385  1.00 16.59 ? 141 PHE A CA  1 
ATOM   1115  C  C   . PHE A  1 142 ? -5.703  0.708   19.846  1.00 17.87 ? 141 PHE A C   1 
ATOM   1116  O  O   . PHE A  1 142 ? -6.801  0.615   19.287  1.00 18.13 ? 141 PHE A O   1 
ATOM   1117  C  CB  . PHE A  1 142 ? -5.417  -0.827  21.827  1.00 17.03 ? 141 PHE A CB  1 
ATOM   1118  C  CG  . PHE A  1 142 ? -4.950  -2.167  22.307  1.00 16.61 ? 141 PHE A CG  1 
ATOM   1119  C  CD1 . PHE A  1 142 ? -5.448  -3.323  21.738  1.00 16.34 ? 141 PHE A CD1 1 
ATOM   1120  C  CD2 . PHE A  1 142 ? -3.965  -2.272  23.279  1.00 17.28 ? 141 PHE A CD2 1 
ATOM   1121  C  CE1 . PHE A  1 142 ? -5.004  -4.565  22.153  1.00 15.97 ? 141 PHE A CE1 1 
ATOM   1122  C  CE2 . PHE A  1 142 ? -3.501  -3.511  23.684  1.00 16.66 ? 141 PHE A CE2 1 
ATOM   1123  C  CZ  . PHE A  1 142 ? -4.034  -4.661  23.118  1.00 16.09 ? 141 PHE A CZ  1 
ATOM   1124  N  N   . LEU A  1 143 ? -5.072  1.870   20.007  1.00 18.97 ? 142 LEU A N   1 
ATOM   1125  C  CA  . LEU A  1 143 ? -5.605  3.083   19.397  1.00 20.55 ? 142 LEU A CA  1 
ATOM   1126  C  C   . LEU A  1 143 ? -5.606  2.964   17.871  1.00 18.22 ? 142 LEU A C   1 
ATOM   1127  O  O   . LEU A  1 143 ? -6.602  3.289   17.215  1.00 19.04 ? 142 LEU A O   1 
ATOM   1128  C  CB  . LEU A  1 143 ? -4.839  4.337   19.872  1.00 22.57 ? 142 LEU A CB  1 
ATOM   1129  C  CG  . LEU A  1 143 ? -4.850  4.637   21.376  1.00 26.54 ? 142 LEU A CG  1 
ATOM   1130  C  CD1 . LEU A  1 143 ? -3.797  5.694   21.742  1.00 28.48 ? 142 LEU A CD1 1 
ATOM   1131  C  CD2 . LEU A  1 143 ? -6.226  5.098   21.789  1.00 28.44 ? 142 LEU A CD2 1 
ATOM   1132  N  N   . ALA A  1 144 ? -4.510  2.476   17.311  1.00 17.38 ? 143 ALA A N   1 
ATOM   1133  C  CA  . ALA A  1 144 ? -4.405  2.289   15.850  1.00 17.31 ? 143 ALA A CA  1 
ATOM   1134  C  C   . ALA A  1 144 ? -5.401  1.250   15.349  1.00 16.54 ? 143 ALA A C   1 
ATOM   1135  O  O   . ALA A  1 144 ? -5.954  1.377   14.258  1.00 16.58 ? 143 ALA A O   1 
ATOM   1136  C  CB  . ALA A  1 144 ? -2.986  1.870   15.459  1.00 18.00 ? 143 ALA A CB  1 
ATOM   1137  N  N   . LEU A  1 145 ? -5.599  0.193   16.119  1.00 16.28 ? 144 LEU A N   1 
ATOM   1138  C  CA  . LEU A  1 145 ? -6.547  -0.862  15.742  1.00 16.05 ? 144 LEU A CA  1 
ATOM   1139  C  C   . LEU A  1 145 ? -7.971  -0.294  15.693  1.00 16.54 ? 144 LEU A C   1 
ATOM   1140  O  O   . LEU A  1 145 ? -8.726  -0.555  14.745  1.00 15.47 ? 144 LEU A O   1 
ATOM   1141  C  CB  . LEU A  1 145 ? -6.451  -2.028  16.725  1.00 16.16 ? 144 LEU A CB  1 
ATOM   1142  C  CG  . LEU A  1 145 ? -7.418  -3.213  16.595  1.00 16.65 ? 144 LEU A CG  1 
ATOM   1143  C  CD1 . LEU A  1 145 ? -7.272  -3.850  15.220  1.00 17.09 ? 144 LEU A CD1 1 
ATOM   1144  C  CD2 . LEU A  1 145 ? -7.173  -4.254  17.671  1.00 17.42 ? 144 LEU A CD2 1 
ATOM   1145  N  N   . ARG A  1 146 ? -8.340  0.471   16.719  1.00 17.21 ? 145 ARG A N   1 
ATOM   1146  C  CA  . ARG A  1 146 ? -9.663  1.091   16.764  1.00 18.32 ? 145 ARG A CA  1 
ATOM   1147  C  C   . ARG A  1 146 ? -9.852  2.011   15.542  1.00 18.01 ? 145 ARG A C   1 
ATOM   1148  O  O   . ARG A  1 146 ? -10.877 1.952   14.861  1.00 17.38 ? 145 ARG A O   1 
ATOM   1149  C  CB  . ARG A  1 146 ? -9.871  1.882   18.052  1.00 20.64 ? 145 ARG A CB  1 
ATOM   1150  C  CG  . ARG A  1 146 ? -11.203 2.601   18.129  1.00 23.41 ? 145 ARG A CG  1 
ATOM   1151  C  CD  . ARG A  1 146 ? -11.362 3.340   19.460  1.00 27.20 ? 145 ARG A CD  1 
ATOM   1152  N  NE  . ARG A  1 146 ? -12.433 4.337   19.405  1.00 29.50 ? 145 ARG A NE  1 
ATOM   1153  C  CZ  . ARG A  1 146 ? -13.590 4.316   20.086  1.00 32.88 ? 145 ARG A CZ  1 
ATOM   1154  N  NH1 . ARG A  1 146 ? -13.908 3.332   20.935  1.00 34.00 ? 145 ARG A NH1 1 
ATOM   1155  N  NH2 . ARG A  1 146 ? -14.461 5.310   19.901  1.00 33.01 ? 145 ARG A NH2 1 
ATOM   1156  N  N   A GLU A  1 147 ? -8.853  2.837   15.259  0.50 18.18 ? 146 GLU A N   1 
ATOM   1157  N  N   B GLU A  1 147 ? -8.851  2.839   15.257  0.50 18.52 ? 146 GLU A N   1 
ATOM   1158  C  CA  A GLU A  1 147 ? -8.906  3.733   14.108  0.50 19.19 ? 146 GLU A CA  1 
ATOM   1159  C  CA  B GLU A  1 147 ? -8.908  3.734   14.102  0.50 19.59 ? 146 GLU A CA  1 
ATOM   1160  C  C   A GLU A  1 147 ? -8.987  2.977   12.772  0.50 18.31 ? 146 GLU A C   1 
ATOM   1161  C  C   B GLU A  1 147 ? -8.987  2.978   12.768  0.50 18.56 ? 146 GLU A C   1 
ATOM   1162  O  O   A GLU A  1 147 ? -9.736  3.379   11.881  0.50 17.78 ? 146 GLU A O   1 
ATOM   1163  O  O   B GLU A  1 147 ? -9.737  3.379   11.879  0.50 17.98 ? 146 GLU A O   1 
ATOM   1164  C  CB  A GLU A  1 147 ? -7.704  4.683   14.124  0.50 20.52 ? 146 GLU A CB  1 
ATOM   1165  C  CB  B GLU A  1 147 ? -7.732  4.720   14.112  0.50 21.48 ? 146 GLU A CB  1 
ATOM   1166  C  CG  A GLU A  1 147 ? -7.641  5.652   12.959  0.50 22.98 ? 146 GLU A CG  1 
ATOM   1167  C  CG  B GLU A  1 147 ? -7.817  5.704   15.273  0.50 24.40 ? 146 GLU A CG  1 
ATOM   1168  C  CD  A GLU A  1 147 ? -8.737  6.711   12.990  0.50 25.13 ? 146 GLU A CD  1 
ATOM   1169  C  CD  B GLU A  1 147 ? -6.579  6.587   15.451  0.50 28.26 ? 146 GLU A CD  1 
ATOM   1170  O  OE1 A GLU A  1 147 ? -9.510  6.770   13.974  0.50 27.45 ? 146 GLU A OE1 1 
ATOM   1171  O  OE1 B GLU A  1 147 ? -5.478  6.226   14.984  0.50 31.93 ? 146 GLU A OE1 1 
ATOM   1172  O  OE2 A GLU A  1 147 ? -8.826  7.486   12.015  0.50 28.56 ? 146 GLU A OE2 1 
ATOM   1173  O  OE2 B GLU A  1 147 ? -6.702  7.654   16.086  0.50 32.09 ? 146 GLU A OE2 1 
ATOM   1174  N  N   . MET A  1 148 ? -8.229  1.889   12.634  1.00 17.26 ? 147 MET A N   1 
ATOM   1175  C  CA  . MET A  1 148 ? -8.233  1.114   11.418  1.00 17.28 ? 147 MET A CA  1 
ATOM   1176  C  C   . MET A  1 148 ? -9.604  0.467   11.180  1.00 16.38 ? 147 MET A C   1 
ATOM   1177  O  O   . MET A  1 148 ? -10.124 0.455   10.059  1.00 15.70 ? 147 MET A O   1 
ATOM   1178  C  CB  . MET A  1 148 ? -7.149  0.031   11.439  1.00 17.35 ? 147 MET A CB  1 
ATOM   1179  C  CG  . MET A  1 148 ? -7.103  -0.797  10.172  1.00 18.95 ? 147 MET A CG  1 
ATOM   1180  S  SD  . MET A  1 148 ? -5.608  -1.818  10.040  1.00 20.82 ? 147 MET A SD  1 
ATOM   1181  C  CE  . MET A  1 148 ? -5.915  -3.061  11.244  1.00 19.42 ? 147 MET A CE  1 
ATOM   1182  N  N   . ILE A  1 149 ? -10.179 -0.063  12.243  1.00 16.22 ? 148 ILE A N   1 
ATOM   1183  C  CA  . ILE A  1 149 ? -11.518 -0.671  12.162  1.00 15.98 ? 148 ILE A CA  1 
ATOM   1184  C  C   . ILE A  1 149 ? -12.552 0.365   11.714  1.00 16.80 ? 148 ILE A C   1 
ATOM   1185  O  O   . ILE A  1 149 ? -13.371 0.094   10.849  1.00 16.32 ? 148 ILE A O   1 
ATOM   1186  C  CB  . ILE A  1 149 ? -11.900 -1.335  13.493  1.00 16.71 ? 148 ILE A CB  1 
ATOM   1187  C  CG1 . ILE A  1 149 ? -11.093 -2.628  13.660  1.00 16.51 ? 148 ILE A CG1 1 
ATOM   1188  C  CG2 . ILE A  1 149 ? -13.392 -1.657  13.539  1.00 17.63 ? 148 ILE A CG2 1 
ATOM   1189  C  CD1 . ILE A  1 149 ? -11.114 -3.182  15.056  1.00 16.60 ? 148 ILE A CD1 1 
ATOM   1190  N  N   . GLU A  1 150 ? -12.517 1.549   12.313  1.00 17.70 ? 149 GLU A N   1 
ATOM   1191  C  CA  . GLU A  1 150 ? -13.435 2.614   11.922  1.00 19.24 ? 149 GLU A CA  1 
ATOM   1192  C  C   . GLU A  1 150 ? -13.247 3.022   10.448  1.00 18.44 ? 149 GLU A C   1 
ATOM   1193  O  O   . GLU A  1 150 ? -14.233 3.234   9.726   1.00 19.00 ? 149 GLU A O   1 
ATOM   1194  C  CB  . GLU A  1 150 ? -13.276 3.817   12.863  1.00 20.90 ? 149 GLU A CB  1 
ATOM   1195  C  CG  . GLU A  1 150 ? -13.696 3.493   14.290  1.00 22.57 ? 149 GLU A CG  1 
ATOM   1196  C  CD  . GLU A  1 150 ? -13.632 4.696   15.230  1.00 26.52 ? 149 GLU A CD  1 
ATOM   1197  O  OE1 . GLU A  1 150 ? -14.104 4.625   16.390  1.00 25.79 ? 149 GLU A OE1 1 
ATOM   1198  O  OE2 . GLU A  1 150 ? -13.099 5.740   14.800  1.00 30.05 ? 149 GLU A OE2 1 
ATOM   1199  N  N   A GLU A  1 151 ? -11.995 3.129   10.005  0.50 18.41 ? 150 GLU A N   1 
ATOM   1200  N  N   B GLU A  1 151 ? -11.994 3.131   10.004  0.50 17.47 ? 150 GLU A N   1 
ATOM   1201  C  CA  A GLU A  1 151 ? -11.695 3.472   8.615   0.50 19.22 ? 150 GLU A CA  1 
ATOM   1202  C  CA  B GLU A  1 151 ? -11.686 3.474   8.611   0.50 17.66 ? 150 GLU A CA  1 
ATOM   1203  C  C   A GLU A  1 151 ? -12.229 2.408   7.658   0.50 18.24 ? 150 GLU A C   1 
ATOM   1204  C  C   B GLU A  1 151 ? -12.227 2.408   7.658   0.50 17.39 ? 150 GLU A C   1 
ATOM   1205  O  O   A GLU A  1 151 ? -12.832 2.724   6.630   0.50 18.25 ? 150 GLU A O   1 
ATOM   1206  O  O   B GLU A  1 151 ? -12.832 2.724   6.630   0.50 17.48 ? 150 GLU A O   1 
ATOM   1207  C  CB  A GLU A  1 151 ? -10.188 3.678   8.411   0.50 20.43 ? 150 GLU A CB  1 
ATOM   1208  C  CB  B GLU A  1 151 ? -10.169 3.655   8.407   0.50 17.51 ? 150 GLU A CB  1 
ATOM   1209  C  CG  A GLU A  1 151 ? -9.655  4.895   9.137   0.50 21.95 ? 150 GLU A CG  1 
ATOM   1210  C  CG  B GLU A  1 151 ? -9.730  3.762   6.940   0.50 17.45 ? 150 GLU A CG  1 
ATOM   1211  C  CD  A GLU A  1 151 ? -8.141  4.996   9.134   0.50 23.83 ? 150 GLU A CD  1 
ATOM   1212  C  CD  B GLU A  1 151 ? -8.209  3.948   6.693   0.50 17.48 ? 150 GLU A CD  1 
ATOM   1213  O  OE1 A GLU A  1 151 ? -7.456  4.014   8.810   0.50 24.88 ? 150 GLU A OE1 1 
ATOM   1214  O  OE1 B GLU A  1 151 ? -7.622  4.835   7.362   0.50 18.72 ? 150 GLU A OE1 1 
ATOM   1215  O  OE2 A GLU A  1 151 ? -7.630  6.078   9.478   0.50 27.84 ? 150 GLU A OE2 1 
ATOM   1216  O  OE2 B GLU A  1 151 ? -7.606  3.274   5.803   0.50 14.87 ? 150 GLU A OE2 1 
ATOM   1217  N  N   . MET A  1 152 ? -12.051 1.142   8.014   1.00 17.21 ? 151 MET A N   1 
ATOM   1218  C  CA  . MET A  1 152 ? -12.522 0.044   7.158   1.00 17.09 ? 151 MET A CA  1 
ATOM   1219  C  C   . MET A  1 152 ? -14.052 0.047   7.074   1.00 17.62 ? 151 MET A C   1 
ATOM   1220  O  O   . MET A  1 152 ? -14.633 -0.194  6.009   1.00 16.99 ? 151 MET A O   1 
ATOM   1221  C  CB  . MET A  1 152 ? -12.008 -1.282  7.663   1.00 16.87 ? 151 MET A CB  1 
ATOM   1222  C  CG  . MET A  1 152 ? -10.492 -1.406  7.520   1.00 17.16 ? 151 MET A CG  1 
ATOM   1223  S  SD  . MET A  1 152 ? -9.829  -2.898  8.289   1.00 17.59 ? 151 MET A SD  1 
ATOM   1224  C  CE  . MET A  1 152 ? -10.209 -4.122  7.025   1.00 17.08 ? 151 MET A CE  1 
ATOM   1225  N  N   . TYR A  1 153 ? -14.696 0.334   8.191   1.00 17.78 ? 152 TYR A N   1 
ATOM   1226  C  CA  . TYR A  1 153 ? -16.165 0.414   8.215   1.00 18.96 ? 152 TYR A CA  1 
ATOM   1227  C  C   . TYR A  1 153 ? -16.652 1.529   7.253   1.00 19.74 ? 152 TYR A C   1 
ATOM   1228  O  O   . TYR A  1 153 ? -17.601 1.333   6.490   1.00 19.99 ? 152 TYR A O   1 
ATOM   1229  C  CB  . TYR A  1 153 ? -16.622 0.677   9.655   1.00 19.39 ? 152 TYR A CB  1 
ATOM   1230  C  CG  . TYR A  1 153 ? -18.081 1.065   9.788   1.00 20.81 ? 152 TYR A CG  1 
ATOM   1231  C  CD1 . TYR A  1 153 ? -18.489 2.377   9.645   1.00 22.00 ? 152 TYR A CD1 1 
ATOM   1232  C  CD2 . TYR A  1 153 ? -19.052 0.103   10.043  1.00 22.53 ? 152 TYR A CD2 1 
ATOM   1233  C  CE1 . TYR A  1 153 ? -19.829 2.731   9.778   1.00 23.97 ? 152 TYR A CE1 1 
ATOM   1234  C  CE2 . TYR A  1 153 ? -20.391 0.445   10.189  1.00 23.75 ? 152 TYR A CE2 1 
ATOM   1235  C  CZ  . TYR A  1 153 ? -20.767 1.754   10.046  1.00 24.83 ? 152 TYR A CZ  1 
ATOM   1236  O  OH  . TYR A  1 153 ? -22.096 2.082   10.174  1.00 27.41 ? 152 TYR A OH  1 
ATOM   1237  N  N   . GLN A  1 154 ? -16.004 2.689   7.309   1.00 20.94 ? 153 GLN A N   1 
ATOM   1238  C  CA  . GLN A  1 154 ? -16.380 3.839   6.486   1.00 23.30 ? 153 GLN A CA  1 
ATOM   1239  C  C   . GLN A  1 154 ? -16.080 3.626   5.020   1.00 21.42 ? 153 GLN A C   1 
ATOM   1240  O  O   . GLN A  1 154 ? -16.921 3.930   4.173   1.00 20.42 ? 153 GLN A O   1 
ATOM   1241  C  CB  . GLN A  1 154 ? -15.667 5.114   6.941   1.00 27.70 ? 153 GLN A CB  1 
ATOM   1242  C  CG  . GLN A  1 154 ? -16.030 5.587   8.339   1.00 35.48 ? 153 GLN A CG  1 
ATOM   1243  C  CD  . GLN A  1 154 ? -15.243 6.811   8.816   1.00 45.46 ? 153 GLN A CD  1 
ATOM   1244  O  OE1 . GLN A  1 154 ? -13.999 6.837   8.841   1.00 50.92 ? 153 GLN A OE1 1 
ATOM   1245  N  NE2 . GLN A  1 154 ? -15.981 7.848   9.208   1.00 52.78 ? 153 GLN A NE2 1 
ATOM   1246  N  N   . LEU A  1 155 ? -14.906 3.061   4.713   1.00 18.73 ? 154 LEU A N   1 
ATOM   1247  C  CA  . LEU A  1 155 ? -14.533 2.803   3.333   1.00 19.21 ? 154 LEU A CA  1 
ATOM   1248  C  C   . LEU A  1 155 ? -15.402 1.727   2.689   1.00 19.02 ? 154 LEU A C   1 
ATOM   1249  O  O   . LEU A  1 155 ? -15.872 1.903   1.559   1.00 19.72 ? 154 LEU A O   1 
ATOM   1250  C  CB  . LEU A  1 155 ? -13.053 2.366   3.220   1.00 17.96 ? 154 LEU A CB  1 
ATOM   1251  C  CG  . LEU A  1 155 ? -12.030 3.476   3.441   1.00 18.51 ? 154 LEU A CG  1 
ATOM   1252  C  CD1 . LEU A  1 155 ? -10.646 2.862   3.575   1.00 18.59 ? 154 LEU A CD1 1 
ATOM   1253  C  CD2 . LEU A  1 155 ? -12.061 4.474   2.289   1.00 19.66 ? 154 LEU A CD2 1 
ATOM   1254  N  N   . TYR A  1 156 ? -15.565 0.605   3.370   1.00 18.59 ? 155 TYR A N   1 
ATOM   1255  C  CA  . TYR A  1 156 ? -16.144 -0.595  2.736   1.00 19.35 ? 155 TYR A CA  1 
ATOM   1256  C  C   . TYR A  1 156 ? -17.614 -0.773  3.046   1.00 21.13 ? 155 TYR A C   1 
ATOM   1257  O  O   . TYR A  1 156 ? -18.230 -1.666  2.506   1.00 22.67 ? 155 TYR A O   1 
ATOM   1258  C  CB  . TYR A  1 156 ? -15.317 -1.861  3.051   1.00 18.23 ? 155 TYR A CB  1 
ATOM   1259  C  CG  . TYR A  1 156 ? -13.822 -1.587  2.815   1.00 16.66 ? 155 TYR A CG  1 
ATOM   1260  C  CD1 . TYR A  1 156 ? -13.356 -1.228  1.551   1.00 16.85 ? 155 TYR A CD1 1 
ATOM   1261  C  CD2 . TYR A  1 156 ? -12.906 -1.683  3.845   1.00 15.66 ? 155 TYR A CD2 1 
ATOM   1262  C  CE1 . TYR A  1 156 ? -11.997 -0.946  1.336   1.00 16.45 ? 155 TYR A CE1 1 
ATOM   1263  C  CE2 . TYR A  1 156 ? -11.565 -1.413  3.641   1.00 15.85 ? 155 TYR A CE2 1 
ATOM   1264  C  CZ  . TYR A  1 156 ? -11.116 -1.025  2.375   1.00 15.94 ? 155 TYR A CZ  1 
ATOM   1265  O  OH  . TYR A  1 156 ? -9.777  -0.744  2.194   1.00 15.46 ? 155 TYR A OH  1 
ATOM   1266  N  N   . GLY A  1 157 ? -18.180 0.074   3.902   1.00 21.29 ? 156 GLY A N   1 
ATOM   1267  C  CA  . GLY A  1 157 ? -19.632 0.132   4.076   1.00 22.41 ? 156 GLY A CA  1 
ATOM   1268  C  C   . GLY A  1 157 ? -20.263 -0.886  5.035   1.00 23.33 ? 156 GLY A C   1 
ATOM   1269  O  O   . GLY A  1 157 ? -21.462 -1.128  4.954   1.00 23.92 ? 156 GLY A O   1 
ATOM   1270  N  N   . GLY A  1 158 ? -19.497 -1.450  5.959   1.00 21.67 ? 157 GLY A N   1 
ATOM   1271  C  CA  . GLY A  1 158 ? -20.076 -2.322  6.989   1.00 22.51 ? 157 GLY A CA  1 
ATOM   1272  C  C   . GLY A  1 158 ? -19.088 -2.774  8.054   1.00 21.32 ? 157 GLY A C   1 
ATOM   1273  O  O   . GLY A  1 158 ? -17.876 -2.497  7.921   1.00 19.91 ? 157 GLY A O   1 
ATOM   1274  N  N   . PRO A  1 159 ? -19.592 -3.453  9.111   1.00 20.47 ? 158 PRO A N   1 
ATOM   1275  C  CA  . PRO A  1 159 ? -18.749 -3.863  10.212  1.00 19.79 ? 158 PRO A CA  1 
ATOM   1276  C  C   . PRO A  1 159 ? -17.752 -4.973  9.860   1.00 19.53 ? 158 PRO A C   1 
ATOM   1277  O  O   . PRO A  1 159 ? -17.968 -5.719  8.913   1.00 19.01 ? 158 PRO A O   1 
ATOM   1278  C  CB  . PRO A  1 159 ? -19.742 -4.324  11.282  1.00 20.58 ? 158 PRO A CB  1 
ATOM   1279  C  CG  . PRO A  1 159 ? -21.018 -4.623  10.563  1.00 21.26 ? 158 PRO A CG  1 
ATOM   1280  C  CD  . PRO A  1 159 ? -21.027 -3.699  9.385   1.00 21.55 ? 158 PRO A CD  1 
ATOM   1281  N  N   . VAL A  1 160 ? -16.692 -5.050  10.654  1.00 19.28 ? 159 VAL A N   1 
ATOM   1282  C  CA  . VAL A  1 160 ? -15.522 -5.899  10.392  1.00 19.59 ? 159 VAL A CA  1 
ATOM   1283  C  C   . VAL A  1 160 ? -15.593 -7.251  11.108  1.00 18.49 ? 159 VAL A C   1 
ATOM   1284  O  O   . VAL A  1 160 ? -16.141 -7.367  12.220  1.00 18.63 ? 159 VAL A O   1 
ATOM   1285  C  CB  . VAL A  1 160 ? -14.167 -5.229  10.767  1.00 20.78 ? 159 VAL A CB  1 
ATOM   1286  C  CG1 . VAL A  1 160 ? -14.120 -3.825  10.199  1.00 22.63 ? 159 VAL A CG1 1 
ATOM   1287  C  CG2 . VAL A  1 160 ? -13.913 -5.249  12.264  1.00 23.64 ? 159 VAL A CG2 1 
ATOM   1288  N  N   . VAL A  1 161 ? -14.983 -8.263  10.501  1.00 17.50 ? 160 VAL A N   1 
ATOM   1289  C  CA  . VAL A  1 161 ? -14.792 -9.559  11.167  1.00 17.44 ? 160 VAL A CA  1 
ATOM   1290  C  C   . VAL A  1 161 ? -13.335 -9.627  11.617  1.00 17.14 ? 160 VAL A C   1 
ATOM   1291  O  O   . VAL A  1 161 ? -12.429 -9.426  10.801  1.00 16.74 ? 160 VAL A O   1 
ATOM   1292  C  CB  . VAL A  1 161 ? -15.126 -10.738 10.233  1.00 17.30 ? 160 VAL A CB  1 
ATOM   1293  C  CG1 . VAL A  1 161 ? -14.754 -12.073 10.864  1.00 17.46 ? 160 VAL A CG1 1 
ATOM   1294  C  CG2 . VAL A  1 161 ? -16.598 -10.707 9.863   1.00 18.33 ? 160 VAL A CG2 1 
ATOM   1295  N  N   . LEU A  1 162 ? -13.132 -9.864  12.914  1.00 16.78 ? 161 LEU A N   1 
ATOM   1296  C  CA  . LEU A  1 162 ? -11.811 -10.052 13.487  1.00 17.24 ? 161 LEU A CA  1 
ATOM   1297  C  C   . LEU A  1 162 ? -11.485 -11.536 13.451  1.00 16.94 ? 161 LEU A C   1 
ATOM   1298  O  O   . LEU A  1 162 ? -12.302 -12.341 13.866  1.00 16.78 ? 161 LEU A O   1 
ATOM   1299  C  CB  . LEU A  1 162 ? -11.786 -9.556  14.930  1.00 18.43 ? 161 LEU A CB  1 
ATOM   1300  C  CG  . LEU A  1 162 ? -12.153 -8.088  15.137  1.00 19.76 ? 161 LEU A CG  1 
ATOM   1301  C  CD1 . LEU A  1 162 ? -12.316 -7.716  16.590  1.00 20.84 ? 161 LEU A CD1 1 
ATOM   1302  C  CD2 . LEU A  1 162 ? -11.090 -7.222  14.515  1.00 21.86 ? 161 LEU A CD2 1 
ATOM   1303  N  N   . VAL A  1 163 ? -10.308 -11.886 12.949  1.00 15.80 ? 162 VAL A N   1 
ATOM   1304  C  CA  . VAL A  1 163 ? -9.887  -13.278 12.902  1.00 15.57 ? 162 VAL A CA  1 
ATOM   1305  C  C   . VAL A  1 163 ? -8.543  -13.317 13.631  1.00 15.07 ? 162 VAL A C   1 
ATOM   1306  O  O   . VAL A  1 163 ? -7.588  -12.680 13.181  1.00 15.94 ? 162 VAL A O   1 
ATOM   1307  C  CB  . VAL A  1 163 ? -9.711  -13.785 11.462  1.00 16.31 ? 162 VAL A CB  1 
ATOM   1308  C  CG1 . VAL A  1 163 ? -9.268  -15.265 11.468  1.00 16.53 ? 162 VAL A CG1 1 
ATOM   1309  C  CG2 . VAL A  1 163 ? -11.003 -13.646 10.677  1.00 17.16 ? 162 VAL A CG2 1 
ATOM   1310  N  N   . ALA A  1 164 ? -8.476  -14.012 14.768  1.00 14.99 ? 163 ALA A N   1 
ATOM   1311  C  CA  . ALA A  1 164 ? -7.272  -14.029 15.604  1.00 14.72 ? 163 ALA A CA  1 
ATOM   1312  C  C   . ALA A  1 164 ? -6.789  -15.442 15.868  1.00 15.00 ? 163 ALA A C   1 
ATOM   1313  O  O   . ALA A  1 164 ? -7.577  -16.371 15.965  1.00 14.69 ? 163 ALA A O   1 
ATOM   1314  C  CB  . ALA A  1 164 ? -7.511  -13.317 16.931  1.00 14.97 ? 163 ALA A CB  1 
ATOM   1315  N  N   . HIS A  1 165 ? -5.471  -15.586 15.968  1.00 14.79 ? 164 HIS A N   1 
ATOM   1316  C  CA  . HIS A  1 165 ? -4.854  -16.868 16.234  1.00 15.22 ? 164 HIS A CA  1 
ATOM   1317  C  C   . HIS A  1 165 ? -4.059  -16.794 17.527  1.00 15.07 ? 164 HIS A C   1 
ATOM   1318  O  O   . HIS A  1 165 ? -3.346  -15.810 17.808  1.00 13.36 ? 164 HIS A O   1 
ATOM   1319  C  CB  . HIS A  1 165 ? -3.919  -17.265 15.105  1.00 16.24 ? 164 HIS A CB  1 
ATOM   1320  C  CG  . HIS A  1 165 ? -3.250  -18.585 15.325  1.00 16.58 ? 164 HIS A CG  1 
ATOM   1321  N  ND1 . HIS A  1 165 ? -1.877  -18.710 15.422  1.00 17.98 ? 164 HIS A ND1 1 
ATOM   1322  C  CD2 . HIS A  1 165 ? -3.756  -19.828 15.464  1.00 17.22 ? 164 HIS A CD2 1 
ATOM   1323  C  CE1 . HIS A  1 165 ? -1.566  -19.978 15.613  1.00 18.03 ? 164 HIS A CE1 1 
ATOM   1324  N  NE2 . HIS A  1 165 ? -2.686  -20.681 15.634  1.00 18.01 ? 164 HIS A NE2 1 
ATOM   1325  N  N   . SER A  1 166 ? -4.224  -17.831 18.330  1.00 15.15 ? 165 SER A N   1 
ATOM   1326  C  CA  . SER A  1 166 ? -3.418  -18.035 19.523  1.00 15.86 ? 165 SER A CA  1 
ATOM   1327  C  C   . SER A  1 166 ? -3.472  -16.807 20.449  1.00 15.30 ? 165 SER A C   1 
ATOM   1328  O  O   . SER A  1 166 ? -4.570  -16.341 20.761  1.00 15.27 ? 165 SER A O   1 
ATOM   1329  C  CB  . SER A  1 166 ? -2.007  -18.447 19.091  1.00 16.89 ? 165 SER A CB  1 
ATOM   1330  O  OG  . SER A  1 166 ? -1.331  -19.073 20.167  1.00 20.30 ? 165 SER A OG  1 
ATOM   1331  N  N   . MET A  1 167 ? -2.326  -16.294 20.900  1.00 14.94 ? 166 MET A N   1 
ATOM   1332  C  CA  . MET A  1 167 ? -2.315  -15.146 21.810  1.00 16.09 ? 166 MET A CA  1 
ATOM   1333  C  C   . MET A  1 167 ? -3.043  -13.928 21.238  1.00 14.66 ? 166 MET A C   1 
ATOM   1334  O  O   . MET A  1 167 ? -3.472  -13.056 21.997  1.00 14.73 ? 166 MET A O   1 
ATOM   1335  C  CB  . MET A  1 167 ? -0.869  -14.761 22.136  1.00 17.80 ? 166 MET A CB  1 
ATOM   1336  C  CG  . MET A  1 167 ? -0.751  -13.623 23.105  1.00 19.96 ? 166 MET A CG  1 
ATOM   1337  S  SD  . MET A  1 167 ? 0.983   -13.400 23.597  1.00 19.83 ? 166 MET A SD  1 
ATOM   1338  C  CE  . MET A  1 167 ? 1.588   -12.330 22.302  1.00 18.87 ? 166 MET A CE  1 
ATOM   1339  N  N   . GLY A  1 168 ? -3.172  -13.852 19.914  1.00 13.87 ? 167 GLY A N   1 
ATOM   1340  C  CA  . GLY A  1 168 ? -3.916  -12.742 19.298  1.00 13.93 ? 167 GLY A CA  1 
ATOM   1341  C  C   . GLY A  1 168 ? -5.331  -12.674 19.821  1.00 13.90 ? 167 GLY A C   1 
ATOM   1342  O  O   . GLY A  1 168 ? -5.944  -11.630 19.837  1.00 14.92 ? 167 GLY A O   1 
ATOM   1343  N  N   . ASN A  1 169 ? -5.862  -13.804 20.268  1.00 14.49 ? 168 ASN A N   1 
ATOM   1344  C  CA  . ASN A  1 169 ? -7.209  -13.818 20.836  1.00 14.88 ? 168 ASN A CA  1 
ATOM   1345  C  C   . ASN A  1 169 ? -7.306  -13.095 22.165  1.00 15.53 ? 168 ASN A C   1 
ATOM   1346  O  O   . ASN A  1 169 ? -8.298  -12.439 22.452  1.00 14.99 ? 168 ASN A O   1 
ATOM   1347  C  CB  . ASN A  1 169 ? -7.676  -15.255 21.011  1.00 15.15 ? 168 ASN A CB  1 
ATOM   1348  C  CG  . ASN A  1 169 ? -7.959  -15.913 19.685  1.00 15.93 ? 168 ASN A CG  1 
ATOM   1349  O  OD1 . ASN A  1 169 ? -8.968  -15.633 19.066  1.00 16.21 ? 168 ASN A OD1 1 
ATOM   1350  N  ND2 . ASN A  1 169 ? -7.071  -16.805 19.244  1.00 15.34 ? 168 ASN A ND2 1 
ATOM   1351  N  N   . MET A  1 170 ? -6.259  -13.192 22.965  1.00 16.16 ? 169 MET A N   1 
ATOM   1352  C  CA  . MET A  1 170 ? -6.208  -12.502 24.243  1.00 16.84 ? 169 MET A CA  1 
ATOM   1353  C  C   . MET A  1 170 ? -5.996  -10.995 24.042  1.00 15.55 ? 169 MET A C   1 
ATOM   1354  O  O   . MET A  1 170 ? -6.593  -10.179 24.755  1.00 15.16 ? 169 MET A O   1 
ATOM   1355  C  CB  . MET A  1 170 ? -5.148  -13.145 25.147  1.00 18.30 ? 169 MET A CB  1 
ATOM   1356  C  CG  . MET A  1 170 ? -5.568  -14.536 25.646  1.00 21.15 ? 169 MET A CG  1 
ATOM   1357  S  SD  . MET A  1 170 ? -6.753  -14.338 27.005  1.00 26.72 ? 169 MET A SD  1 
ATOM   1358  C  CE  . MET A  1 170 ? -5.656  -13.953 28.359  1.00 28.19 ? 169 MET A CE  1 
ATOM   1359  N  N   . TYR A  1 171 ? -5.163  -10.619 23.066  1.00 15.01 ? 170 TYR A N   1 
ATOM   1360  C  CA  . TYR A  1 171 ? -5.063  -9.204  22.635  1.00 14.67 ? 170 TYR A CA  1 
ATOM   1361  C  C   . TYR A  1 171 ? -6.439  -8.670  22.195  1.00 15.32 ? 170 TYR A C   1 
ATOM   1362  O  O   . TYR A  1 171 ? -6.832  -7.568  22.582  1.00 15.34 ? 170 TYR A O   1 
ATOM   1363  C  CB  . TYR A  1 171 ? -4.047  -9.044  21.512  1.00 14.42 ? 170 TYR A CB  1 
ATOM   1364  C  CG  . TYR A  1 171 ? -2.712  -8.571  22.018  1.00 14.91 ? 170 TYR A CG  1 
ATOM   1365  C  CD1 . TYR A  1 171 ? -1.908  -9.380  22.790  1.00 15.00 ? 170 TYR A CD1 1 
ATOM   1366  C  CD2 . TYR A  1 171 ? -2.288  -7.271  21.769  1.00 15.93 ? 170 TYR A CD2 1 
ATOM   1367  C  CE1 . TYR A  1 171 ? -0.684  -8.919  23.283  1.00 15.61 ? 170 TYR A CE1 1 
ATOM   1368  C  CE2 . TYR A  1 171 ? -1.091  -6.802  22.267  1.00 16.88 ? 170 TYR A CE2 1 
ATOM   1369  C  CZ  . TYR A  1 171 ? -0.309  -7.621  23.044  1.00 16.09 ? 170 TYR A CZ  1 
ATOM   1370  O  OH  . TYR A  1 171 ? 0.880   -7.116  23.520  1.00 16.29 ? 170 TYR A OH  1 
ATOM   1371  N  N   . THR A  1 172 ? -7.138  -9.446  21.372  1.00 15.19 ? 171 THR A N   1 
ATOM   1372  C  CA  . THR A  1 172 ? -8.447  -9.041  20.849  1.00 15.59 ? 171 THR A CA  1 
ATOM   1373  C  C   . THR A  1 172 ? -9.493  -8.933  21.985  1.00 16.49 ? 171 THR A C   1 
ATOM   1374  O  O   . THR A  1 172 ? -10.274 -7.959  22.023  1.00 16.60 ? 171 THR A O   1 
ATOM   1375  C  CB  . THR A  1 172 ? -8.907  -9.990  19.732  1.00 16.65 ? 171 THR A CB  1 
ATOM   1376  O  OG1 . THR A  1 172 ? -7.927  -9.995  18.683  1.00 15.60 ? 171 THR A OG1 1 
ATOM   1377  C  CG2 . THR A  1 172 ? -10.252 -9.539  19.153  1.00 17.47 ? 171 THR A CG2 1 
ATOM   1378  N  N   . LEU A  1 173 ? -9.498  -9.900  22.907  1.00 16.15 ? 172 LEU A N   1 
ATOM   1379  C  CA  . LEU A  1 173 ? -10.414 -9.842  24.061  1.00 17.77 ? 172 LEU A CA  1 
ATOM   1380  C  C   . LEU A  1 173 ? -10.157 -8.598  24.932  1.00 17.03 ? 172 LEU A C   1 
ATOM   1381  O  O   . LEU A  1 173 ? -11.094 -7.889  25.321  1.00 16.29 ? 172 LEU A O   1 
ATOM   1382  C  CB  . LEU A  1 173 ? -10.321 -11.122 24.884  1.00 18.75 ? 172 LEU A CB  1 
ATOM   1383  C  CG  . LEU A  1 173 ? -11.229 -11.166 26.132  1.00 19.90 ? 172 LEU A CG  1 
ATOM   1384  C  CD1 . LEU A  1 173 ? -12.696 -11.046 25.759  1.00 19.80 ? 172 LEU A CD1 1 
ATOM   1385  C  CD2 . LEU A  1 173 ? -10.940 -12.449 26.904  1.00 20.62 ? 172 LEU A CD2 1 
ATOM   1386  N  N   . TYR A  1 174 ? -8.882  -8.302  25.185  1.00 16.09 ? 173 TYR A N   1 
ATOM   1387  C  CA  . TYR A  1 174 ? -8.528  -7.106  25.927  1.00 17.11 ? 173 TYR A CA  1 
ATOM   1388  C  C   . TYR A  1 174 ? -9.116  -5.882  25.250  1.00 17.53 ? 173 TYR A C   1 
ATOM   1389  O  O   . TYR A  1 174 ? -9.760  -5.036  25.890  1.00 18.88 ? 173 TYR A O   1 
ATOM   1390  C  CB  . TYR A  1 174 ? -7.004  -6.994  26.034  1.00 16.75 ? 173 TYR A CB  1 
ATOM   1391  C  CG  . TYR A  1 174 ? -6.493  -5.702  26.645  1.00 18.24 ? 173 TYR A CG  1 
ATOM   1392  C  CD1 . TYR A  1 174 ? -6.304  -5.591  28.023  1.00 19.88 ? 173 TYR A CD1 1 
ATOM   1393  C  CD2 . TYR A  1 174 ? -6.212  -4.603  25.861  1.00 18.83 ? 173 TYR A CD2 1 
ATOM   1394  C  CE1 . TYR A  1 174 ? -5.831  -4.422  28.581  1.00 20.97 ? 173 TYR A CE1 1 
ATOM   1395  C  CE2 . TYR A  1 174 ? -5.732  -3.423  26.405  1.00 19.73 ? 173 TYR A CE2 1 
ATOM   1396  C  CZ  . TYR A  1 174 ? -5.545  -3.343  27.766  1.00 22.30 ? 173 TYR A CZ  1 
ATOM   1397  O  OH  . TYR A  1 174 ? -5.066  -2.171  28.317  1.00 24.77 ? 173 TYR A OH  1 
ATOM   1398  N  N   . PHE A  1 175 ? -8.888  -5.787  23.942  1.00 17.14 ? 174 PHE A N   1 
ATOM   1399  C  CA  . PHE A  1 175 ? -9.387  -4.653  23.176  1.00 17.42 ? 174 PHE A CA  1 
ATOM   1400  C  C   . PHE A  1 175 ? -10.919 -4.525  23.291  1.00 18.04 ? 174 PHE A C   1 
ATOM   1401  O  O   . PHE A  1 175 ? -11.454 -3.452  23.584  1.00 17.84 ? 174 PHE A O   1 
ATOM   1402  C  CB  . PHE A  1 175 ? -8.974  -4.806  21.720  1.00 17.33 ? 174 PHE A CB  1 
ATOM   1403  C  CG  . PHE A  1 175 ? -9.570  -3.775  20.797  1.00 17.74 ? 174 PHE A CG  1 
ATOM   1404  C  CD1 . PHE A  1 175 ? -9.126  -2.455  20.829  1.00 18.16 ? 174 PHE A CD1 1 
ATOM   1405  C  CD2 . PHE A  1 175 ? -10.549 -4.131  19.875  1.00 17.63 ? 174 PHE A CD2 1 
ATOM   1406  C  CE1 . PHE A  1 175 ? -9.631  -1.513  19.947  1.00 18.55 ? 174 PHE A CE1 1 
ATOM   1407  C  CE2 . PHE A  1 175 ? -11.077 -3.186  18.999  1.00 18.51 ? 174 PHE A CE2 1 
ATOM   1408  C  CZ  . PHE A  1 175 ? -10.626 -1.877  19.035  1.00 18.89 ? 174 PHE A CZ  1 
ATOM   1409  N  N   . LEU A  1 176 ? -11.610 -5.622  23.038  1.00 17.48 ? 175 LEU A N   1 
ATOM   1410  C  CA  . LEU A  1 176 ? -13.083 -5.606  23.027  1.00 18.60 ? 175 LEU A CA  1 
ATOM   1411  C  C   . LEU A  1 176 ? -13.695 -5.335  24.397  1.00 19.68 ? 175 LEU A C   1 
ATOM   1412  O  O   . LEU A  1 176 ? -14.729 -4.642  24.498  1.00 20.11 ? 175 LEU A O   1 
ATOM   1413  C  CB  . LEU A  1 176 ? -13.632 -6.913  22.437  1.00 18.14 ? 175 LEU A CB  1 
ATOM   1414  C  CG  . LEU A  1 176 ? -13.332 -7.119  20.943  1.00 18.07 ? 175 LEU A CG  1 
ATOM   1415  C  CD1 . LEU A  1 176 ? -13.775 -8.521  20.561  1.00 18.25 ? 175 LEU A CD1 1 
ATOM   1416  C  CD2 . LEU A  1 176 ? -14.010 -6.077  20.056  1.00 18.16 ? 175 LEU A CD2 1 
ATOM   1417  N  N   . GLN A  1 177 ? -13.072 -5.873  25.447  1.00 19.42 ? 176 GLN A N   1 
ATOM   1418  C  CA  . GLN A  1 177 ? -13.537 -5.599  26.815  1.00 21.27 ? 176 GLN A CA  1 
ATOM   1419  C  C   . GLN A  1 177 ? -13.506 -4.100  27.126  1.00 22.39 ? 176 GLN A C   1 
ATOM   1420  O  O   . GLN A  1 177 ? -14.304 -3.606  27.940  1.00 22.80 ? 176 GLN A O   1 
ATOM   1421  C  CB  . GLN A  1 177 ? -12.699 -6.368  27.849  1.00 21.40 ? 176 GLN A CB  1 
ATOM   1422  C  CG  . GLN A  1 177 ? -13.020 -7.855  27.896  1.00 21.73 ? 176 GLN A CG  1 
ATOM   1423  C  CD  . GLN A  1 177 ? -12.232 -8.590  28.964  1.00 22.08 ? 176 GLN A CD  1 
ATOM   1424  O  OE1 . GLN A  1 177 ? -11.236 -8.086  29.464  1.00 22.00 ? 176 GLN A OE1 1 
ATOM   1425  N  NE2 . GLN A  1 177 ? -12.683 -9.779  29.319  1.00 21.78 ? 176 GLN A NE2 1 
ATOM   1426  N  N   . ARG A  1 178 ? -12.608 -3.376  26.485  1.00 22.55 ? 177 ARG A N   1 
ATOM   1427  C  CA  . ARG A  1 178 ? -12.471 -1.956  26.738  1.00 24.72 ? 177 ARG A CA  1 
ATOM   1428  C  C   . ARG A  1 178 ? -13.216 -1.028  25.783  1.00 25.02 ? 177 ARG A C   1 
ATOM   1429  O  O   . ARG A  1 178 ? -13.081 0.172   25.910  1.00 25.77 ? 177 ARG A O   1 
ATOM   1430  C  CB  . ARG A  1 178 ? -10.986 -1.612  26.824  1.00 26.09 ? 177 ARG A CB  1 
ATOM   1431  C  CG  . ARG A  1 178 ? -10.426 -2.187  28.122  1.00 29.01 ? 177 ARG A CG  1 
ATOM   1432  C  CD  . ARG A  1 178 ? -8.922  -2.225  28.193  1.00 30.75 ? 177 ARG A CD  1 
ATOM   1433  N  NE  . ARG A  1 178 ? -8.441  -2.740  29.484  1.00 36.36 ? 177 ARG A NE  1 
ATOM   1434  C  CZ  . ARG A  1 178 ? -8.657  -3.947  29.998  1.00 40.69 ? 177 ARG A CZ  1 
ATOM   1435  N  NH1 . ARG A  1 178 ? -9.393  -4.868  29.355  1.00 42.99 ? 177 ARG A NH1 1 
ATOM   1436  N  NH2 . ARG A  1 178 ? -8.123  -4.241  31.196  1.00 41.21 ? 177 ARG A NH2 1 
ATOM   1437  N  N   . GLN A  1 179 ? -13.986 -1.556  24.823  1.00 23.21 ? 178 GLN A N   1 
ATOM   1438  C  CA  . GLN A  1 179 ? -14.759 -0.688  23.935  1.00 23.30 ? 178 GLN A CA  1 
ATOM   1439  C  C   . GLN A  1 179 ? -16.209 -0.727  24.392  1.00 23.77 ? 178 GLN A C   1 
ATOM   1440  O  O   . GLN A  1 179 ? -16.682 -1.764  24.780  1.00 22.76 ? 178 GLN A O   1 
ATOM   1441  C  CB  . GLN A  1 179 ? -14.683 -1.131  22.466  1.00 23.03 ? 178 GLN A CB  1 
ATOM   1442  C  CG  . GLN A  1 179 ? -13.281 -1.302  21.877  1.00 23.77 ? 178 GLN A CG  1 
ATOM   1443  C  CD  . GLN A  1 179 ? -12.339 -0.193  22.288  1.00 25.01 ? 178 GLN A CD  1 
ATOM   1444  O  OE1 . GLN A  1 179 ? -12.598 0.976   22.028  1.00 25.69 ? 178 GLN A OE1 1 
ATOM   1445  N  NE2 . GLN A  1 179 ? -11.252 -0.549  22.937  1.00 25.92 ? 178 GLN A NE2 1 
ATOM   1446  N  N   . PRO A  1 180 ? -16.907 0.406   24.340  1.00 23.56 ? 179 PRO A N   1 
ATOM   1447  C  CA  . PRO A  1 180 ? -18.334 0.422   24.702  1.00 25.18 ? 179 PRO A CA  1 
ATOM   1448  C  C   . PRO A  1 180 ? -19.146 -0.542  23.831  1.00 24.72 ? 179 PRO A C   1 
ATOM   1449  O  O   . PRO A  1 180 ? -18.818 -0.737  22.649  1.00 22.85 ? 179 PRO A O   1 
ATOM   1450  C  CB  . PRO A  1 180 ? -18.754 1.870   24.405  1.00 25.69 ? 179 PRO A CB  1 
ATOM   1451  C  CG  . PRO A  1 180 ? -17.488 2.655   24.509  1.00 26.29 ? 179 PRO A CG  1 
ATOM   1452  C  CD  . PRO A  1 180 ? -16.400 1.745   24.006  1.00 24.33 ? 179 PRO A CD  1 
ATOM   1453  N  N   . GLN A  1 181 ? -20.209 -1.095  24.398  1.00 24.10 ? 180 GLN A N   1 
ATOM   1454  C  CA  . GLN A  1 181 ? -21.055 -2.025  23.665  1.00 25.04 ? 180 GLN A CA  1 
ATOM   1455  C  C   . GLN A  1 181 ? -21.611 -1.410  22.377  1.00 25.28 ? 180 GLN A C   1 
ATOM   1456  O  O   . GLN A  1 181 ? -21.681 -2.077  21.359  1.00 23.81 ? 180 GLN A O   1 
ATOM   1457  C  CB  . GLN A  1 181 ? -22.212 -2.532  24.555  1.00 26.73 ? 180 GLN A CB  1 
ATOM   1458  C  CG  . GLN A  1 181 ? -23.022 -3.653  23.928  1.00 26.71 ? 180 GLN A CG  1 
ATOM   1459  C  CD  . GLN A  1 181 ? -22.177 -4.905  23.739  1.00 27.25 ? 180 GLN A CD  1 
ATOM   1460  O  OE1 . GLN A  1 181 ? -21.528 -5.366  24.674  1.00 28.92 ? 180 GLN A OE1 1 
ATOM   1461  N  NE2 . GLN A  1 181 ? -22.157 -5.443  22.523  1.00 26.01 ? 180 GLN A NE2 1 
ATOM   1462  N  N   . ALA A  1 182 ? -21.991 -0.132  22.415  1.00 24.79 ? 181 ALA A N   1 
ATOM   1463  C  CA  . ALA A  1 182 ? -22.520 0.526   21.231  1.00 25.29 ? 181 ALA A CA  1 
ATOM   1464  C  C   . ALA A  1 182 ? -21.476 0.618   20.104  1.00 24.03 ? 181 ALA A C   1 
ATOM   1465  O  O   . ALA A  1 182 ? -21.834 0.521   18.928  1.00 23.77 ? 181 ALA A O   1 
ATOM   1466  C  CB  . ALA A  1 182 ? -23.033 1.925   21.572  1.00 25.85 ? 181 ALA A CB  1 
ATOM   1467  N  N   . TRP A  1 183 ? -20.209 0.807   20.464  1.00 22.02 ? 182 TRP A N   1 
ATOM   1468  C  CA  . TRP A  1 183 ? -19.116 0.849   19.478  1.00 21.44 ? 182 TRP A CA  1 
ATOM   1469  C  C   . TRP A  1 183 ? -18.984 -0.526  18.832  1.00 20.52 ? 182 TRP A C   1 
ATOM   1470  O  O   . TRP A  1 183 ? -18.916 -0.631  17.607  1.00 20.25 ? 182 TRP A O   1 
ATOM   1471  C  CB  . TRP A  1 183 ? -17.786 1.243   20.129  1.00 21.17 ? 182 TRP A CB  1 
ATOM   1472  C  CG  . TRP A  1 183 ? -16.691 1.426   19.147  1.00 20.92 ? 182 TRP A CG  1 
ATOM   1473  C  CD1 . TRP A  1 183 ? -16.305 2.591   18.534  1.00 20.98 ? 182 TRP A CD1 1 
ATOM   1474  C  CD2 . TRP A  1 183 ? -15.811 0.401   18.645  1.00 20.24 ? 182 TRP A CD2 1 
ATOM   1475  N  NE1 . TRP A  1 183 ? -15.245 2.351   17.695  1.00 21.13 ? 182 TRP A NE1 1 
ATOM   1476  C  CE2 . TRP A  1 183 ? -14.919 1.020   17.743  1.00 20.24 ? 182 TRP A CE2 1 
ATOM   1477  C  CE3 . TRP A  1 183 ? -15.700 -0.980  18.864  1.00 20.40 ? 182 TRP A CE3 1 
ATOM   1478  C  CZ2 . TRP A  1 183 ? -13.944 0.298   17.044  1.00 18.98 ? 182 TRP A CZ2 1 
ATOM   1479  C  CZ3 . TRP A  1 183 ? -14.721 -1.687  18.199  1.00 19.69 ? 182 TRP A CZ3 1 
ATOM   1480  C  CH2 . TRP A  1 183 ? -13.851 -1.044  17.292  1.00 18.72 ? 182 TRP A CH2 1 
ATOM   1481  N  N   . LYS A  1 184 ? -18.990 -1.580  19.644  1.00 20.28 ? 183 LYS A N   1 
ATOM   1482  C  CA  . LYS A  1 184 ? -18.854 -2.937  19.126  1.00 19.66 ? 183 LYS A CA  1 
ATOM   1483  C  C   . LYS A  1 184 ? -20.020 -3.302  18.223  1.00 20.65 ? 183 LYS A C   1 
ATOM   1484  O  O   . LYS A  1 184 ? -19.839 -3.956  17.205  1.00 19.90 ? 183 LYS A O   1 
ATOM   1485  C  CB  . LYS A  1 184 ? -18.683 -3.940  20.267  1.00 19.60 ? 183 LYS A CB  1 
ATOM   1486  C  CG  . LYS A  1 184 ? -17.352 -3.752  20.984  1.00 19.18 ? 183 LYS A CG  1 
ATOM   1487  C  CD  . LYS A  1 184 ? -17.104 -4.753  22.107  1.00 19.37 ? 183 LYS A CD  1 
ATOM   1488  C  CE  . LYS A  1 184 ? -18.006 -4.552  23.290  1.00 19.95 ? 183 LYS A CE  1 
ATOM   1489  N  NZ  . LYS A  1 184 ? -17.509 -5.257  24.494  1.00 20.27 ? 183 LYS A NZ  1 
ATOM   1490  N  N   . ASP A  1 185 ? -21.224 -2.899  18.606  1.00 21.86 ? 184 ASP A N   1 
ATOM   1491  C  CA  . ASP A  1 185 ? -22.425 -3.218  17.810  1.00 24.31 ? 184 ASP A CA  1 
ATOM   1492  C  C   . ASP A  1 185 ? -22.402 -2.531  16.447  1.00 24.27 ? 184 ASP A C   1 
ATOM   1493  O  O   . ASP A  1 185 ? -22.895 -3.082  15.472  1.00 24.42 ? 184 ASP A O   1 
ATOM   1494  C  CB  . ASP A  1 185 ? -23.695 -2.825  18.566  1.00 27.09 ? 184 ASP A CB  1 
ATOM   1495  C  CG  . ASP A  1 185 ? -23.956 -3.705  19.798  1.00 30.41 ? 184 ASP A CG  1 
ATOM   1496  O  OD1 . ASP A  1 185 ? -23.297 -4.764  19.970  1.00 31.14 ? 184 ASP A OD1 1 
ATOM   1497  O  OD2 . ASP A  1 185 ? -24.831 -3.306  20.599  1.00 34.68 ? 184 ASP A OD2 1 
ATOM   1498  N  N   . LYS A  1 186 ? -21.809 -1.339  16.369  1.00 23.83 ? 185 LYS A N   1 
ATOM   1499  C  CA  . LYS A  1 186 ? -21.679 -0.633  15.104  1.00 24.02 ? 185 LYS A CA  1 
ATOM   1500  C  C   . LYS A  1 186 ? -20.542 -1.188  14.240  1.00 21.55 ? 185 LYS A C   1 
ATOM   1501  O  O   . LYS A  1 186 ? -20.725 -1.418  13.058  1.00 20.38 ? 185 LYS A O   1 
ATOM   1502  C  CB  . LYS A  1 186 ? -21.425 0.846   15.342  1.00 25.78 ? 185 LYS A CB  1 
ATOM   1503  C  CG  . LYS A  1 186 ? -21.204 1.639   14.075  1.00 27.57 ? 185 LYS A CG  1 
ATOM   1504  C  CD  . LYS A  1 186 ? -21.243 3.134   14.367  1.00 30.46 ? 185 LYS A CD  1 
ATOM   1505  C  CE  . LYS A  1 186 ? -21.042 3.944   13.099  1.00 33.07 ? 185 LYS A CE  1 
ATOM   1506  N  NZ  . LYS A  1 186 ? -20.920 5.381   13.450  1.00 36.64 ? 185 LYS A NZ  1 
ATOM   1507  N  N   . TYR A  1 187 ? -19.378 -1.430  14.847  1.00 20.13 ? 186 TYR A N   1 
ATOM   1508  C  CA  . TYR A  1 187 ? -18.153 -1.669  14.064  1.00 19.19 ? 186 TYR A CA  1 
ATOM   1509  C  C   . TYR A  1 187 ? -17.692 -3.118  13.927  1.00 19.16 ? 186 TYR A C   1 
ATOM   1510  O  O   . TYR A  1 187 ? -16.891 -3.407  13.033  1.00 17.79 ? 186 TYR A O   1 
ATOM   1511  C  CB  . TYR A  1 187 ? -17.004 -0.847  14.647  1.00 19.04 ? 186 TYR A CB  1 
ATOM   1512  C  CG  . TYR A  1 187 ? -17.192 0.640   14.440  1.00 19.92 ? 186 TYR A CG  1 
ATOM   1513  C  CD1 . TYR A  1 187 ? -17.024 1.226   13.183  1.00 21.24 ? 186 TYR A CD1 1 
ATOM   1514  C  CD2 . TYR A  1 187 ? -17.511 1.473   15.504  1.00 21.57 ? 186 TYR A CD2 1 
ATOM   1515  C  CE1 . TYR A  1 187 ? -17.176 2.596   12.992  1.00 21.81 ? 186 TYR A CE1 1 
ATOM   1516  C  CE2 . TYR A  1 187 ? -17.679 2.850   15.324  1.00 22.55 ? 186 TYR A CE2 1 
ATOM   1517  C  CZ  . TYR A  1 187 ? -17.513 3.393   14.066  1.00 23.55 ? 186 TYR A CZ  1 
ATOM   1518  O  OH  . TYR A  1 187 ? -17.672 4.748   13.877  1.00 26.16 ? 186 TYR A OH  1 
ATOM   1519  N  N   . ILE A  1 188 ? -18.165 -4.023  14.780  1.00 18.81 ? 187 ILE A N   1 
ATOM   1520  C  CA  . ILE A  1 188 ? -17.697 -5.428  14.778  1.00 19.55 ? 187 ILE A CA  1 
ATOM   1521  C  C   . ILE A  1 188 ? -18.835 -6.321  14.338  1.00 20.87 ? 187 ILE A C   1 
ATOM   1522  O  O   . ILE A  1 188 ? -19.895 -6.348  14.964  1.00 21.73 ? 187 ILE A O   1 
ATOM   1523  C  CB  . ILE A  1 188 ? -17.181 -5.894  16.156  1.00 19.96 ? 187 ILE A CB  1 
ATOM   1524  C  CG1 . ILE A  1 188 ? -16.106 -4.939  16.694  1.00 19.83 ? 187 ILE A CG1 1 
ATOM   1525  C  CG2 . ILE A  1 188 ? -16.650 -7.337  16.100  1.00 20.05 ? 187 ILE A CG2 1 
ATOM   1526  C  CD1 . ILE A  1 188 ? -14.875 -4.797  15.826  1.00 19.24 ? 187 ILE A CD1 1 
ATOM   1527  N  N   . ARG A  1 189 ? -18.624 -7.060  13.251  1.00 20.83 ? 188 ARG A N   1 
ATOM   1528  C  CA  . ARG A  1 189 ? -19.585 -8.041  12.783  1.00 21.44 ? 188 ARG A CA  1 
ATOM   1529  C  C   . ARG A  1 189 ? -19.465 -9.350  13.589  1.00 21.02 ? 188 ARG A C   1 
ATOM   1530  O  O   . ARG A  1 189 ? -20.459 -9.932  14.011  1.00 20.05 ? 188 ARG A O   1 
ATOM   1531  C  CB  . ARG A  1 189 ? -19.396 -8.321  11.289  1.00 23.37 ? 188 ARG A CB  1 
ATOM   1532  C  CG  . ARG A  1 189 ? -20.432 -9.294  10.738  1.00 27.23 ? 188 ARG A CG  1 
ATOM   1533  C  CD  . ARG A  1 189 ? -20.509 -9.481  9.233   1.00 31.04 ? 188 ARG A CD  1 
ATOM   1534  N  NE  . ARG A  1 189 ? -21.111 -8.304  8.662   1.00 36.40 ? 188 ARG A NE  1 
ATOM   1535  C  CZ  . ARG A  1 189 ? -22.418 -8.115  8.456   1.00 39.69 ? 188 ARG A CZ  1 
ATOM   1536  N  NH1 . ARG A  1 189 ? -23.336 -9.049  8.750   1.00 41.05 ? 188 ARG A NH1 1 
ATOM   1537  N  NH2 . ARG A  1 189 ? -22.797 -6.955  7.944   1.00 41.61 ? 188 ARG A NH2 1 
ATOM   1538  N  N   . ALA A  1 190 ? -18.252 -9.849  13.730  1.00 19.11 ? 189 ALA A N   1 
ATOM   1539  C  CA  . ALA A  1 190 ? -18.010 -11.130 14.398  1.00 19.04 ? 189 ALA A CA  1 
ATOM   1540  C  C   . ALA A  1 190 ? -16.540 -11.234 14.743  1.00 17.72 ? 189 ALA A C   1 
ATOM   1541  O  O   . ALA A  1 190 ? -15.711 -10.482 14.224  1.00 17.23 ? 189 ALA A O   1 
ATOM   1542  C  CB  . ALA A  1 190 ? -18.412 -12.300 13.514  1.00 19.57 ? 189 ALA A CB  1 
ATOM   1543  N  N   . PHE A  1 191 ? -16.236 -12.155 15.647  1.00 17.61 ? 190 PHE A N   1 
ATOM   1544  C  CA  . PHE A  1 191 ? -14.869 -12.455 16.101  1.00 16.91 ? 190 PHE A CA  1 
ATOM   1545  C  C   . PHE A  1 191 ? -14.721 -13.969 15.906  1.00 17.68 ? 190 PHE A C   1 
ATOM   1546  O  O   . PHE A  1 191 ? -15.441 -14.759 16.537  1.00 17.99 ? 190 PHE A O   1 
ATOM   1547  C  CB  . PHE A  1 191 ? -14.755 -11.998 17.568  1.00 17.17 ? 190 PHE A CB  1 
ATOM   1548  C  CG  . PHE A  1 191 ? -13.474 -12.379 18.295  1.00 17.05 ? 190 PHE A CG  1 
ATOM   1549  C  CD1 . PHE A  1 191 ? -12.347 -12.840 17.654  1.00 17.36 ? 190 PHE A CD1 1 
ATOM   1550  C  CD2 . PHE A  1 191 ? -13.423 -12.216 19.678  1.00 17.75 ? 190 PHE A CD2 1 
ATOM   1551  C  CE1 . PHE A  1 191 ? -11.198 -13.163 18.376  1.00 17.41 ? 190 PHE A CE1 1 
ATOM   1552  C  CE2 . PHE A  1 191 ? -12.292 -12.542 20.415  1.00 18.32 ? 190 PHE A CE2 1 
ATOM   1553  C  CZ  . PHE A  1 191 ? -11.162 -12.998 19.756  1.00 17.96 ? 190 PHE A CZ  1 
ATOM   1554  N  N   . VAL A  1 192 ? -13.821 -14.358 14.997  1.00 17.24 ? 191 VAL A N   1 
ATOM   1555  C  CA  . VAL A  1 192 ? -13.491 -15.749 14.757  1.00 17.29 ? 191 VAL A CA  1 
ATOM   1556  C  C   . VAL A  1 192 ? -12.171 -16.015 15.518  1.00 17.00 ? 191 VAL A C   1 
ATOM   1557  O  O   . VAL A  1 192 ? -11.129 -15.420 15.220  1.00 16.08 ? 191 VAL A O   1 
ATOM   1558  C  CB  . VAL A  1 192 ? -13.325 -16.048 13.272  1.00 17.83 ? 191 VAL A CB  1 
ATOM   1559  C  CG1 . VAL A  1 192 ? -12.908 -17.503 13.062  1.00 18.88 ? 191 VAL A CG1 1 
ATOM   1560  C  CG2 . VAL A  1 192 ? -14.607 -15.770 12.528  1.00 18.75 ? 191 VAL A CG2 1 
ATOM   1561  N  N   . SER A  1 193 ? -12.262 -16.881 16.522  1.00 17.42 ? 192 SER A N   1 
ATOM   1562  C  CA  . SER A  1 193 ? -11.209 -17.121 17.494  1.00 18.22 ? 192 SER A CA  1 
ATOM   1563  C  C   . SER A  1 193 ? -10.583 -18.484 17.229  1.00 17.75 ? 192 SER A C   1 
ATOM   1564  O  O   . SER A  1 193 ? -11.262 -19.507 17.330  1.00 18.62 ? 192 SER A O   1 
ATOM   1565  C  CB  . SER A  1 193 ? -11.861 -17.098 18.871  1.00 20.06 ? 192 SER A CB  1 
ATOM   1566  O  OG  . SER A  1 193 ? -10.935 -17.277 19.882  1.00 22.18 ? 192 SER A OG  1 
ATOM   1567  N  N   . LEU A  1 194 ? -9.324  -18.503 16.813  1.00 16.74 ? 193 LEU A N   1 
ATOM   1568  C  CA  . LEU A  1 194 ? -8.649  -19.745 16.430  1.00 17.18 ? 193 LEU A CA  1 
ATOM   1569  C  C   . LEU A  1 194 ? -7.575  -20.114 17.435  1.00 16.46 ? 193 LEU A C   1 
ATOM   1570  O  O   . LEU A  1 194 ? -6.535  -19.426 17.565  1.00 14.79 ? 193 LEU A O   1 
ATOM   1571  C  CB  . LEU A  1 194 ? -8.030  -19.592 15.034  1.00 17.96 ? 193 LEU A CB  1 
ATOM   1572  C  CG  . LEU A  1 194 ? -8.912  -19.111 13.895  1.00 20.11 ? 193 LEU A CG  1 
ATOM   1573  C  CD1 . LEU A  1 194 ? -8.103  -18.881 12.633  1.00 21.87 ? 193 LEU A CD1 1 
ATOM   1574  C  CD2 . LEU A  1 194 ? -10.034 -20.069 13.604  1.00 20.62 ? 193 LEU A CD2 1 
ATOM   1575  N  N   . GLY A  1 195 ? -7.787  -21.204 18.180  1.00 16.88 ? 194 GLY A N   1 
ATOM   1576  C  CA  . GLY A  1 195 ? -6.752  -21.678 19.108  1.00 16.15 ? 194 GLY A CA  1 
ATOM   1577  C  C   . GLY A  1 195 ? -6.446  -20.744 20.270  1.00 15.99 ? 194 GLY A C   1 
ATOM   1578  O  O   . GLY A  1 195 ? -5.287  -20.533 20.615  1.00 15.04 ? 194 GLY A O   1 
ATOM   1579  N  N   . ALA A  1 196 ? -7.491  -20.188 20.873  1.00 15.27 ? 195 ALA A N   1 
ATOM   1580  C  CA  . ALA A  1 196 ? -7.317  -19.195 21.934  1.00 15.54 ? 195 ALA A CA  1 
ATOM   1581  C  C   . ALA A  1 196 ? -6.896  -19.808 23.270  1.00 16.47 ? 195 ALA A C   1 
ATOM   1582  O  O   . ALA A  1 196 ? -7.578  -20.730 23.770  1.00 16.40 ? 195 ALA A O   1 
ATOM   1583  C  CB  . ALA A  1 196 ? -8.634  -18.421 22.132  1.00 15.84 ? 195 ALA A CB  1 
ATOM   1584  N  N   . PRO A  1 197 ? -5.802  -19.295 23.877  1.00 16.33 ? 196 PRO A N   1 
ATOM   1585  C  CA  . PRO A  1 197 ? -5.352  -19.751 25.191  1.00 16.84 ? 196 PRO A CA  1 
ATOM   1586  C  C   . PRO A  1 197 ? -6.023  -18.976 26.322  1.00 16.65 ? 196 PRO A C   1 
ATOM   1587  O  O   . PRO A  1 197 ? -5.349  -18.339 27.130  1.00 17.21 ? 196 PRO A O   1 
ATOM   1588  C  CB  . PRO A  1 197 ? -3.838  -19.477 25.145  1.00 16.46 ? 196 PRO A CB  1 
ATOM   1589  C  CG  . PRO A  1 197 ? -3.763  -18.219 24.373  1.00 16.76 ? 196 PRO A CG  1 
ATOM   1590  C  CD  . PRO A  1 197 ? -4.834  -18.340 23.293  1.00 16.86 ? 196 PRO A CD  1 
ATOM   1591  N  N   A TRP A  1 198 ? -7.352  -19.080 26.377  0.80 17.18 ? 197 TRP A N   1 
ATOM   1592  N  N   B TRP A  1 198 ? -7.351  -19.040 26.382  0.20 16.88 ? 197 TRP A N   1 
ATOM   1593  C  CA  A TRP A  1 198 ? -8.121  -18.415 27.373  0.80 18.36 ? 197 TRP A CA  1 
ATOM   1594  C  CA  B TRP A  1 198 ? -8.165  -18.178 27.263  0.20 16.99 ? 197 TRP A CA  1 
ATOM   1595  C  C   A TRP A  1 198 ? -7.656  -19.091 28.672  0.80 18.21 ? 197 TRP A C   1 
ATOM   1596  C  C   B TRP A  1 198 ? -7.704  -17.935 28.725  0.20 16.70 ? 197 TRP A C   1 
ATOM   1597  O  O   A TRP A  1 198 ? -7.596  -20.313 28.807  0.80 17.81 ? 197 TRP A O   1 
ATOM   1598  O  O   B TRP A  1 198 ? -7.647  -16.798 29.175  0.20 16.19 ? 197 TRP A O   1 
ATOM   1599  C  CB  A TRP A  1 198 ? -9.621  -18.689 27.221  0.80 19.20 ? 197 TRP A CB  1 
ATOM   1600  C  CB  B TRP A  1 198 ? -9.614  -18.662 27.226  0.20 17.63 ? 197 TRP A CB  1 
ATOM   1601  C  CG  A TRP A  1 198 ? -10.246 -18.419 25.895  0.80 19.15 ? 197 TRP A CG  1 
ATOM   1602  C  CG  B TRP A  1 198 ? -10.278 -18.406 25.915  0.20 17.78 ? 197 TRP A CG  1 
ATOM   1603  C  CD1 A TRP A  1 198 ? -11.015 -19.290 25.177  0.80 19.86 ? 197 TRP A CD1 1 
ATOM   1604  C  CD1 B TRP A  1 198 ? -11.022 -19.287 25.196  0.20 18.27 ? 197 TRP A CD1 1 
ATOM   1605  C  CD2 A TRP A  1 198 ? -10.261 -17.182 25.165  0.80 19.79 ? 197 TRP A CD2 1 
ATOM   1606  C  CD2 B TRP A  1 198 ? -10.275 -17.180 25.168  0.20 17.79 ? 197 TRP A CD2 1 
ATOM   1607  N  NE1 A TRP A  1 198 ? -11.485 -18.688 24.047  0.80 19.88 ? 197 TRP A NE1 1 
ATOM   1608  N  NE1 B TRP A  1 198 ? -11.487 -18.695 24.052  0.20 18.31 ? 197 TRP A NE1 1 
ATOM   1609  C  CE2 A TRP A  1 198 ? -11.030 -17.398 24.004  0.80 19.35 ? 197 TRP A CE2 1 
ATOM   1610  C  CE2 B TRP A  1 198 ? -11.042 -17.400 24.007  0.20 17.90 ? 197 TRP A CE2 1 
ATOM   1611  C  CE3 A TRP A  1 198 ? -9.678  -15.926 25.362  0.80 19.37 ? 197 TRP A CE3 1 
ATOM   1612  C  CE3 B TRP A  1 198 ? -9.697  -15.921 25.366  0.20 17.46 ? 197 TRP A CE3 1 
ATOM   1613  C  CZ2 A TRP A  1 198 ? -11.248 -16.397 23.043  0.80 20.01 ? 197 TRP A CZ2 1 
ATOM   1614  C  CZ2 B TRP A  1 198 ? -11.249 -16.409 23.044  0.20 17.99 ? 197 TRP A CZ2 1 
ATOM   1615  C  CZ3 A TRP A  1 198 ? -9.905  -14.930 24.395  0.80 20.02 ? 197 TRP A CZ3 1 
ATOM   1616  C  CZ3 B TRP A  1 198 ? -9.908  -14.934 24.407  0.20 17.54 ? 197 TRP A CZ3 1 
ATOM   1617  C  CH2 A TRP A  1 198 ? -10.677 -15.177 23.269  0.80 18.86 ? 197 TRP A CH2 1 
ATOM   1618  C  CH2 B TRP A  1 198 ? -10.676 -15.187 23.266  0.20 17.47 ? 197 TRP A CH2 1 
ATOM   1619  N  N   A GLY A  1 199 ? -7.323  -18.281 29.629  0.80 18.83 ? 198 GLY A N   1 
ATOM   1620  N  N   B GLY A  1 199 ? -7.369  -18.993 29.454  0.20 16.82 ? 198 GLY A N   1 
ATOM   1621  C  CA  A GLY A  1 199 ? -6.879  -18.804 30.901  0.80 18.45 ? 198 GLY A CA  1 
ATOM   1622  C  CA  B GLY A  1 199 ? -6.891  -18.886 30.846  0.20 16.99 ? 198 GLY A CA  1 
ATOM   1623  C  C   A GLY A  1 199 ? -5.447  -19.301 30.989  0.80 17.84 ? 198 GLY A C   1 
ATOM   1624  C  C   B GLY A  1 199 ? -5.449  -19.329 30.978  0.20 16.86 ? 198 GLY A C   1 
ATOM   1625  O  O   A GLY A  1 199 ? -5.082  -19.910 31.994  0.80 17.83 ? 198 GLY A O   1 
ATOM   1626  O  O   B GLY A  1 199 ? -5.078  -19.918 31.988  0.20 16.97 ? 198 GLY A O   1 
ATOM   1627  N  N   . GLY A  1 200 ? -4.641  -19.033 29.959  1.00 16.58 ? 199 GLY A N   1 
ATOM   1628  C  CA  . GLY A  1 200 ? -3.212  -19.362 29.954  1.00 16.41 ? 199 GLY A CA  1 
ATOM   1629  C  C   . GLY A  1 200 ? -2.943  -20.799 29.528  1.00 17.20 ? 199 GLY A C   1 
ATOM   1630  O  O   . GLY A  1 200 ? -3.887  -21.589 29.340  1.00 18.06 ? 199 GLY A O   1 
ATOM   1631  N  N   . VAL A  1 201 ? -1.669  -21.159 29.385  1.00 16.85 ? 200 VAL A N   1 
ATOM   1632  C  CA  . VAL A  1 201 ? -1.301  -22.504 28.975  1.00 17.39 ? 200 VAL A CA  1 
ATOM   1633  C  C   . VAL A  1 201 ? -0.208  -23.069 29.893  1.00 17.63 ? 200 VAL A C   1 
ATOM   1634  O  O   . VAL A  1 201 ? 0.670   -22.361 30.341  1.00 16.45 ? 200 VAL A O   1 
ATOM   1635  C  CB  . VAL A  1 201 ? -0.840  -22.602 27.495  1.00 19.66 ? 200 VAL A CB  1 
ATOM   1636  C  CG1 . VAL A  1 201 ? -1.932  -22.097 26.549  1.00 20.35 ? 200 VAL A CG1 1 
ATOM   1637  C  CG2 . VAL A  1 201 ? 0.437   -21.849 27.262  1.00 20.17 ? 200 VAL A CG2 1 
ATOM   1638  N  N   . ALA A  1 202 ? -0.258  -24.376 30.142  1.00 17.75 ? 201 ALA A N   1 
ATOM   1639  C  CA  . ALA A  1 202 ? 0.648   -24.988 31.101  1.00 17.99 ? 201 ALA A CA  1 
ATOM   1640  C  C   . ALA A  1 202 ? 2.087   -24.898 30.639  1.00 18.33 ? 201 ALA A C   1 
ATOM   1641  O  O   . ALA A  1 202 ? 2.993   -24.781 31.467  1.00 18.59 ? 201 ALA A O   1 
ATOM   1642  C  CB  . ALA A  1 202 ? 0.262   -26.445 31.313  1.00 18.46 ? 201 ALA A CB  1 
ATOM   1643  N  N   . LYS A  1 203 ? 2.335   -24.939 29.334  1.00 20.00 ? 202 LYS A N   1 
ATOM   1644  C  CA  . LYS A  1 203 ? 3.752   -25.000 28.887  1.00 22.29 ? 202 LYS A CA  1 
ATOM   1645  C  C   . LYS A  1 203 ? 4.597   -23.762 29.199  1.00 19.80 ? 202 LYS A C   1 
ATOM   1646  O  O   . LYS A  1 203 ? 5.828   -23.845 29.190  1.00 18.08 ? 202 LYS A O   1 
ATOM   1647  C  CB  . LYS A  1 203 ? 3.870   -25.398 27.432  1.00 27.41 ? 202 LYS A CB  1 
ATOM   1648  C  CG  . LYS A  1 203 ? 3.557   -24.350 26.423  1.00 31.72 ? 202 LYS A CG  1 
ATOM   1649  C  CD  . LYS A  1 203 ? 3.736   -24.885 25.001  1.00 39.38 ? 202 LYS A CD  1 
ATOM   1650  C  CE  . LYS A  1 203 ? 5.157   -25.376 24.783  1.00 44.87 ? 202 LYS A CE  1 
ATOM   1651  N  NZ  . LYS A  1 203 ? 5.522   -25.369 23.341  1.00 48.65 ? 202 LYS A NZ  1 
ATOM   1652  N  N   . THR A  1 204 ? 3.943   -22.646 29.533  1.00 18.69 ? 203 THR A N   1 
ATOM   1653  C  CA  . THR A  1 204 ? 4.653   -21.436 29.975  1.00 18.81 ? 203 THR A CA  1 
ATOM   1654  C  C   . THR A  1 204 ? 5.557   -21.711 31.205  1.00 17.66 ? 203 THR A C   1 
ATOM   1655  O  O   . THR A  1 204 ? 6.635   -21.128 31.345  1.00 16.57 ? 203 THR A O   1 
ATOM   1656  C  CB  . THR A  1 204 ? 3.682   -20.276 30.309  1.00 19.58 ? 203 THR A CB  1 
ATOM   1657  O  OG1 . THR A  1 204 ? 2.747   -20.737 31.267  1.00 24.01 ? 203 THR A OG1 1 
ATOM   1658  C  CG2 . THR A  1 204 ? 2.894   -19.855 29.135  1.00 20.09 ? 203 THR A CG2 1 
ATOM   1659  N  N   . LEU A  1 205 ? 5.143   -22.611 32.092  1.00 17.27 ? 204 LEU A N   1 
ATOM   1660  C  CA  . LEU A  1 205 ? 5.981   -22.916 33.252  1.00 17.80 ? 204 LEU A CA  1 
ATOM   1661  C  C   . LEU A  1 205 ? 7.321   -23.505 32.839  1.00 17.23 ? 204 LEU A C   1 
ATOM   1662  O  O   . LEU A  1 205 ? 8.343   -23.176 33.422  1.00 17.73 ? 204 LEU A O   1 
ATOM   1663  C  CB  . LEU A  1 205 ? 5.292   -23.923 34.196  1.00 19.53 ? 204 LEU A CB  1 
ATOM   1664  C  CG  . LEU A  1 205 ? 4.201   -23.531 35.191  1.00 20.33 ? 204 LEU A CG  1 
ATOM   1665  C  CD1 . LEU A  1 205 ? 4.649   -22.500 36.199  1.00 20.78 ? 204 LEU A CD1 1 
ATOM   1666  C  CD2 . LEU A  1 205 ? 2.940   -23.122 34.512  1.00 20.64 ? 204 LEU A CD2 1 
ATOM   1667  N  N   . ARG A  1 206 ? 7.295   -24.430 31.884  1.00 18.31 ? 205 ARG A N   1 
ATOM   1668  C  CA  . ARG A  1 206 ? 8.537   -25.062 31.450  1.00 19.49 ? 205 ARG A CA  1 
ATOM   1669  C  C   . ARG A  1 206 ? 9.417   -24.039 30.745  1.00 18.69 ? 205 ARG A C   1 
ATOM   1670  O  O   . ARG A  1 206 ? 10.625  -24.000 30.955  1.00 17.88 ? 205 ARG A O   1 
ATOM   1671  C  CB  . ARG A  1 206 ? 8.249   -26.218 30.527  1.00 21.47 ? 205 ARG A CB  1 
ATOM   1672  C  CG  . ARG A  1 206 ? 9.480   -26.836 29.975  1.00 24.76 ? 205 ARG A CG  1 
ATOM   1673  C  CD  . ARG A  1 206 ? 9.000   -27.832 28.951  1.00 29.53 ? 205 ARG A CD  1 
ATOM   1674  N  NE  . ARG A  1 206 ? 10.143  -28.229 28.206  1.00 36.00 ? 205 ARG A NE  1 
ATOM   1675  C  CZ  . ARG A  1 206 ? 10.365  -28.005 26.919  1.00 37.55 ? 205 ARG A CZ  1 
ATOM   1676  N  NH1 . ARG A  1 206 ? 9.440   -27.535 26.083  1.00 38.75 ? 205 ARG A NH1 1 
ATOM   1677  N  NH2 . ARG A  1 206 ? 11.524  -28.403 26.444  1.00 43.42 ? 205 ARG A NH2 1 
ATOM   1678  N  N   . VAL A  1 207 ? 8.801   -23.218 29.902  1.00 18.73 ? 206 VAL A N   1 
ATOM   1679  C  CA  . VAL A  1 207 ? 9.550   -22.161 29.204  1.00 19.21 ? 206 VAL A CA  1 
ATOM   1680  C  C   . VAL A  1 207 ? 10.340  -21.297 30.206  1.00 19.24 ? 206 VAL A C   1 
ATOM   1681  O  O   . VAL A  1 207 ? 11.569  -21.110 30.066  1.00 18.74 ? 206 VAL A O   1 
ATOM   1682  C  CB  . VAL A  1 207 ? 8.613   -21.297 28.326  1.00 19.52 ? 206 VAL A CB  1 
ATOM   1683  C  CG1 . VAL A  1 207 ? 9.386   -20.112 27.735  1.00 20.27 ? 206 VAL A CG1 1 
ATOM   1684  C  CG2 . VAL A  1 207 ? 7.975   -22.124 27.217  1.00 19.82 ? 206 VAL A CG2 1 
ATOM   1685  N  N   . LEU A  1 208 ? 9.648   -20.813 31.240  1.00 18.70 ? 207 LEU A N   1 
ATOM   1686  C  CA  . LEU A  1 208 ? 10.267  -19.917 32.238  1.00 18.75 ? 207 LEU A CA  1 
ATOM   1687  C  C   . LEU A  1 208 ? 11.284  -20.623 33.130  1.00 18.65 ? 207 LEU A C   1 
ATOM   1688  O  O   . LEU A  1 208 ? 12.348  -20.082 33.420  1.00 18.35 ? 207 LEU A O   1 
ATOM   1689  C  CB  . LEU A  1 208 ? 9.213   -19.247 33.094  1.00 18.80 ? 207 LEU A CB  1 
ATOM   1690  C  CG  . LEU A  1 208 ? 8.310   -18.291 32.321  1.00 19.38 ? 207 LEU A CG  1 
ATOM   1691  C  CD1 . LEU A  1 208 ? 7.073   -17.963 33.130  1.00 20.11 ? 207 LEU A CD1 1 
ATOM   1692  C  CD2 . LEU A  1 208 ? 9.055   -17.035 31.969  1.00 19.82 ? 207 LEU A CD2 1 
ATOM   1693  N  N   . ALA A  1 209 ? 10.986  -21.862 33.521  1.00 18.71 ? 208 ALA A N   1 
ATOM   1694  C  CA  . ALA A  1 209 ? 11.897  -22.592 34.415  1.00 19.16 ? 208 ALA A CA  1 
ATOM   1695  C  C   . ALA A  1 209 ? 13.186  -22.986 33.706  1.00 19.54 ? 208 ALA A C   1 
ATOM   1696  O  O   . ALA A  1 209 ? 14.289  -22.665 34.162  1.00 20.15 ? 208 ALA A O   1 
ATOM   1697  C  CB  . ALA A  1 209 ? 11.218  -23.832 34.992  1.00 18.81 ? 208 ALA A CB  1 
ATOM   1698  N  N   . SER A  1 210 ? 13.048  -23.685 32.575  1.00 20.43 ? 209 SER A N   1 
ATOM   1699  C  CA  . SER A  1 210 ? 14.193  -24.382 31.981  1.00 21.36 ? 209 SER A CA  1 
ATOM   1700  C  C   . SER A  1 210 ? 14.433  -24.117 30.498  1.00 21.56 ? 209 SER A C   1 
ATOM   1701  O  O   . SER A  1 210 ? 15.367  -24.685 29.918  1.00 23.67 ? 209 SER A O   1 
ATOM   1702  C  CB  . SER A  1 210 ? 14.081  -25.889 32.244  1.00 22.08 ? 209 SER A CB  1 
ATOM   1703  O  OG  . SER A  1 210 ? 12.812  -26.389 31.900  1.00 22.12 ? 209 SER A OG  1 
ATOM   1704  N  N   . GLY A  1 211 ? 13.624  -23.245 29.891  1.00 21.55 ? 210 GLY A N   1 
ATOM   1705  C  CA  . GLY A  1 211 ? 13.784  -22.864 28.498  1.00 22.43 ? 210 GLY A CA  1 
ATOM   1706  C  C   . GLY A  1 211 ? 13.101  -23.851 27.568  1.00 24.24 ? 210 GLY A C   1 
ATOM   1707  O  O   . GLY A  1 211 ? 12.851  -24.999 27.939  1.00 23.61 ? 210 GLY A O   1 
ATOM   1708  N  N   . ASP A  1 212 ? 12.838  -23.428 26.336  1.00 24.43 ? 211 ASP A N   1 
ATOM   1709  C  CA  . ASP A  1 212 ? 12.255  -24.313 25.322  1.00 27.48 ? 211 ASP A CA  1 
ATOM   1710  C  C   . ASP A  1 212 ? 12.975  -24.101 23.980  1.00 27.71 ? 211 ASP A C   1 
ATOM   1711  O  O   . ASP A  1 212 ? 12.765  -23.073 23.332  1.00 27.68 ? 211 ASP A O   1 
ATOM   1712  C  CB  . ASP A  1 212 ? 10.761  -24.026 25.160  1.00 29.08 ? 211 ASP A CB  1 
ATOM   1713  C  CG  . ASP A  1 212 ? 10.064  -24.987 24.187  1.00 32.35 ? 211 ASP A CG  1 
ATOM   1714  O  OD1 . ASP A  1 212 ? 10.722  -25.903 23.631  1.00 29.64 ? 211 ASP A OD1 1 
ATOM   1715  O  OD2 . ASP A  1 212 ? 8.827   -24.837 24.026  1.00 36.95 ? 211 ASP A OD2 1 
ATOM   1716  N  N   . ASN A  1 213 ? 13.830  -25.053 23.618  1.00 30.87 ? 212 ASN A N   1 
ATOM   1717  C  CA  . ASN A  1 213 ? 14.581  -25.011 22.348  1.00 33.47 ? 212 ASN A CA  1 
ATOM   1718  C  C   . ASN A  1 213 ? 14.003  -25.995 21.318  1.00 40.32 ? 212 ASN A C   1 
ATOM   1719  O  O   . ASN A  1 213 ? 14.648  -26.287 20.296  1.00 44.54 ? 212 ASN A O   1 
ATOM   1720  C  CB  . ASN A  1 213 ? 16.049  -25.360 22.561  1.00 33.29 ? 212 ASN A CB  1 
ATOM   1721  C  CG  . ASN A  1 213 ? 16.267  -26.834 22.838  1.00 36.78 ? 212 ASN A CG  1 
ATOM   1722  O  OD1 . ASN A  1 213 ? 15.325  -27.559 23.154  1.00 37.70 ? 212 ASN A OD1 1 
ATOM   1723  N  ND2 . ASN A  1 213 ? 17.506  -27.286 22.719  1.00 37.71 ? 212 ASN A ND2 1 
ATOM   1724  N  N   . ASN A  1 214 ? 12.784  -26.487 21.553  1.00 42.36 ? 213 ASN A N   1 
ATOM   1725  C  CA  . ASN A  1 214 ? 12.212  -27.549 20.679  1.00 45.44 ? 213 ASN A CA  1 
ATOM   1726  C  C   . ASN A  1 214 ? 12.174  -27.147 19.200  1.00 47.28 ? 213 ASN A C   1 
ATOM   1727  O  O   . ASN A  1 214 ? 12.130  -27.990 18.300  1.00 48.36 ? 213 ASN A O   1 
ATOM   1728  C  CB  . ASN A  1 214 ? 10.793  -27.950 21.110  1.00 46.42 ? 213 ASN A CB  1 
ATOM   1729  C  CG  . ASN A  1 214 ? 10.776  -28.772 22.396  1.00 46.88 ? 213 ASN A CG  1 
ATOM   1730  O  OD1 . ASN A  1 214 ? 11.816  -29.060 22.996  1.00 49.59 ? 213 ASN A OD1 1 
ATOM   1731  N  ND2 . ASN A  1 214 ? 9.583   -29.150 22.825  1.00 47.83 ? 213 ASN A ND2 1 
ATOM   1732  N  N   . ARG A  1 215 ? 12.191  -25.846 18.949  1.00 49.28 ? 214 ARG A N   1 
ATOM   1733  C  CA  . ARG A  1 215 ? 12.129  -25.346 17.581  1.00 51.06 ? 214 ARG A CA  1 
ATOM   1734  C  C   . ARG A  1 215 ? 13.466  -24.755 17.139  1.00 54.08 ? 214 ARG A C   1 
ATOM   1735  O  O   . ARG A  1 215 ? 13.528  -23.972 16.196  1.00 53.07 ? 214 ARG A O   1 
ATOM   1736  C  CB  . ARG A  1 215 ? 10.984  -24.348 17.455  1.00 51.92 ? 214 ARG A CB  1 
ATOM   1737  C  CG  . ARG A  1 215 ? 9.647   -25.056 17.573  1.00 54.71 ? 214 ARG A CG  1 
ATOM   1738  C  CD  . ARG A  1 215 ? 8.473   -24.158 17.228  1.00 58.88 ? 214 ARG A CD  1 
ATOM   1739  N  NE  . ARG A  1 215 ? 7.298   -24.544 17.993  1.00 65.16 ? 214 ARG A NE  1 
ATOM   1740  C  CZ  . ARG A  1 215 ? 6.171   -23.837 18.036  1.00 70.73 ? 214 ARG A CZ  1 
ATOM   1741  N  NH1 . ARG A  1 215 ? 6.051   -22.703 17.346  1.00 70.65 ? 214 ARG A NH1 1 
ATOM   1742  N  NH2 . ARG A  1 215 ? 5.155   -24.272 18.770  1.00 70.20 ? 214 ARG A NH2 1 
ATOM   1743  N  N   . ILE A  1 216 ? 14.536  -25.142 17.831  1.00 54.29 ? 215 ILE A N   1 
ATOM   1744  C  CA  . ILE A  1 216 ? 15.871  -24.631 17.561  1.00 51.22 ? 215 ILE A CA  1 
ATOM   1745  C  C   . ILE A  1 216 ? 16.837  -25.509 18.370  1.00 48.75 ? 215 ILE A C   1 
ATOM   1746  O  O   . ILE A  1 216 ? 17.567  -25.022 19.248  1.00 46.86 ? 215 ILE A O   1 
ATOM   1747  C  CB  . ILE A  1 216 ? 15.983  -23.118 17.928  1.00 52.34 ? 215 ILE A CB  1 
ATOM   1748  C  CG1 . ILE A  1 216 ? 17.414  -22.589 17.801  1.00 52.27 ? 215 ILE A CG1 1 
ATOM   1749  C  CG2 . ILE A  1 216 ? 15.469  -22.843 19.345  1.00 54.59 ? 215 ILE A CG2 1 
ATOM   1750  C  CD1 . ILE A  1 216 ? 17.470  -21.108 17.519  1.00 53.68 ? 215 ILE A CD1 1 
ATOM   1751  N  N   . PRO A  1 217 ? 16.802  -26.835 18.107  1.00 46.28 ? 216 PRO A N   1 
ATOM   1752  C  CA  . PRO A  1 217 ? 17.521  -27.848 18.878  1.00 44.48 ? 216 PRO A CA  1 
ATOM   1753  C  C   . PRO A  1 217 ? 19.048  -27.755 18.843  1.00 46.81 ? 216 PRO A C   1 
ATOM   1754  O  O   . PRO A  1 217 ? 19.713  -28.334 19.698  1.00 47.10 ? 216 PRO A O   1 
ATOM   1755  C  CB  . PRO A  1 217 ? 17.078  -29.162 18.225  1.00 45.75 ? 216 PRO A CB  1 
ATOM   1756  C  CG  . PRO A  1 217 ? 16.657  -28.792 16.858  1.00 45.55 ? 216 PRO A CG  1 
ATOM   1757  C  CD  . PRO A  1 217 ? 16.012  -27.447 17.024  1.00 45.40 ? 216 PRO A CD  1 
ATOM   1758  N  N   . VAL A  1 218 ? 19.604  -27.053 17.866  1.00 46.39 ? 217 VAL A N   1 
ATOM   1759  C  CA  . VAL A  1 218 ? 21.044  -26.822 17.841  1.00 48.13 ? 217 VAL A CA  1 
ATOM   1760  C  C   . VAL A  1 218 ? 21.462  -25.744 18.863  1.00 48.10 ? 217 VAL A C   1 
ATOM   1761  O  O   . VAL A  1 218 ? 22.650  -25.560 19.102  1.00 50.82 ? 217 VAL A O   1 
ATOM   1762  C  CB  . VAL A  1 218 ? 21.532  -26.447 16.421  1.00 48.15 ? 217 VAL A CB  1 
ATOM   1763  C  CG1 . VAL A  1 218 ? 21.194  -25.000 16.075  1.00 48.12 ? 217 VAL A CG1 1 
ATOM   1764  C  CG2 . VAL A  1 218 ? 23.022  -26.715 16.278  1.00 50.77 ? 217 VAL A CG2 1 
ATOM   1765  N  N   . ILE A  1 219 ? 20.494  -25.037 19.457  1.00 43.54 ? 218 ILE A N   1 
ATOM   1766  C  CA  . ILE A  1 219 ? 20.783  -24.111 20.564  1.00 39.31 ? 218 ILE A CA  1 
ATOM   1767  C  C   . ILE A  1 219 ? 20.292  -24.631 21.930  1.00 37.02 ? 218 ILE A C   1 
ATOM   1768  O  O   . ILE A  1 219 ? 19.229  -25.233 22.051  1.00 33.94 ? 218 ILE A O   1 
ATOM   1769  C  CB  . ILE A  1 219 ? 20.187  -22.705 20.332  1.00 38.33 ? 218 ILE A CB  1 
ATOM   1770  C  CG1 . ILE A  1 219 ? 20.609  -22.113 18.945  1.00 38.18 ? 218 ILE A CG1 1 
ATOM   1771  C  CG2 . ILE A  1 219 ? 20.556  -21.806 21.522  1.00 37.94 ? 218 ILE A CG2 1 
ATOM   1772  C  CD1 . ILE A  1 219 ? 22.100  -21.915 18.692  1.00 36.28 ? 218 ILE A CD1 1 
ATOM   1773  N  N   . GLY A  1 220 ? 21.086  -24.345 22.952  1.00 35.98 ? 219 GLY A N   1 
ATOM   1774  C  CA  . GLY A  1 220 ? 20.818  -24.793 24.301  1.00 36.08 ? 219 GLY A CA  1 
ATOM   1775  C  C   . GLY A  1 220 ? 19.519  -24.215 24.857  1.00 33.64 ? 219 GLY A C   1 
ATOM   1776  O  O   . GLY A  1 220 ? 19.205  -23.040 24.633  1.00 32.28 ? 219 GLY A O   1 
ATOM   1777  N  N   . PRO A  1 221 ? 18.741  -25.041 25.574  1.00 32.39 ? 220 PRO A N   1 
ATOM   1778  C  CA  . PRO A  1 221 ? 17.524  -24.491 26.180  1.00 30.41 ? 220 PRO A CA  1 
ATOM   1779  C  C   . PRO A  1 221 ? 17.841  -23.395 27.207  1.00 27.81 ? 220 PRO A C   1 
ATOM   1780  O  O   . PRO A  1 221 ? 17.097  -22.425 27.292  1.00 26.85 ? 220 PRO A O   1 
ATOM   1781  C  CB  . PRO A  1 221 ? 16.869  -25.711 26.833  1.00 30.34 ? 220 PRO A CB  1 
ATOM   1782  C  CG  . PRO A  1 221 ? 18.011  -26.644 27.101  1.00 32.61 ? 220 PRO A CG  1 
ATOM   1783  C  CD  . PRO A  1 221 ? 18.947  -26.460 25.931  1.00 33.09 ? 220 PRO A CD  1 
ATOM   1784  N  N   . LEU A  1 222 ? 18.951  -23.506 27.930  1.00 28.81 ? 221 LEU A N   1 
ATOM   1785  C  CA  . LEU A  1 222 ? 19.303  -22.484 28.934  1.00 30.06 ? 221 LEU A CA  1 
ATOM   1786  C  C   . LEU A  1 222 ? 19.722  -21.147 28.317  1.00 30.12 ? 221 LEU A C   1 
ATOM   1787  O  O   . LEU A  1 222 ? 19.564  -20.085 28.928  1.00 30.70 ? 221 LEU A O   1 
ATOM   1788  C  CB  . LEU A  1 222 ? 20.395  -22.980 29.871  1.00 31.90 ? 221 LEU A CB  1 
ATOM   1789  C  CG  . LEU A  1 222 ? 20.082  -24.241 30.672  1.00 32.34 ? 221 LEU A CG  1 
ATOM   1790  C  CD1 . LEU A  1 222 ? 21.212  -24.507 31.649  1.00 33.53 ? 221 LEU A CD1 1 
ATOM   1791  C  CD2 . LEU A  1 222 ? 18.745  -24.129 31.402  1.00 30.97 ? 221 LEU A CD2 1 
ATOM   1792  N  N   . LYS A  1 223 ? 20.249  -21.205 27.101  1.00 31.61 ? 222 LYS A N   1 
ATOM   1793  C  CA  . LYS A  1 223 ? 20.630  -20.003 26.364  1.00 32.25 ? 222 LYS A CA  1 
ATOM   1794  C  C   . LYS A  1 223 ? 19.391  -19.262 25.864  1.00 29.09 ? 222 LYS A C   1 
ATOM   1795  O  O   . LYS A  1 223 ? 19.232  -18.065 26.100  1.00 30.49 ? 222 LYS A O   1 
ATOM   1796  C  CB  . LYS A  1 223 ? 21.542  -20.407 25.201  1.00 33.96 ? 222 LYS A CB  1 
ATOM   1797  C  CG  . LYS A  1 223 ? 22.091  -19.234 24.396  1.00 34.50 ? 222 LYS A CG  1 
ATOM   1798  C  CD  . LYS A  1 223 ? 23.183  -19.664 23.426  1.00 36.59 ? 222 LYS A CD  1 
ATOM   1799  C  CE  . LYS A  1 223 ? 24.609  -19.769 24.007  1.00 38.16 ? 222 LYS A CE  1 
ATOM   1800  N  NZ  . LYS A  1 223 ? 24.835  -18.937 25.220  1.00 39.56 ? 222 LYS A NZ  1 
ATOM   1801  N  N   . ILE A  1 224 ? 18.482  -19.970 25.203  1.00 27.95 ? 223 ILE A N   1 
ATOM   1802  C  CA  . ILE A  1 224 ? 17.267  -19.342 24.695  1.00 26.81 ? 223 ILE A CA  1 
ATOM   1803  C  C   . ILE A  1 224 ? 16.305  -18.888 25.827  1.00 26.55 ? 223 ILE A C   1 
ATOM   1804  O  O   . ILE A  1 224 ? 15.482  -17.982 25.626  1.00 24.61 ? 223 ILE A O   1 
ATOM   1805  C  CB  . ILE A  1 224 ? 16.533  -20.252 23.675  1.00 28.63 ? 223 ILE A CB  1 
ATOM   1806  C  CG1 . ILE A  1 224 ? 15.482  -19.491 22.876  1.00 28.76 ? 223 ILE A CG1 1 
ATOM   1807  C  CG2 . ILE A  1 224 ? 15.866  -21.446 24.348  1.00 29.09 ? 223 ILE A CG2 1 
ATOM   1808  C  CD1 . ILE A  1 224 ? 16.060  -18.389 22.015  1.00 31.46 ? 223 ILE A CD1 1 
ATOM   1809  N  N   . ARG A  1 225 ? 16.413  -19.517 26.994  1.00 24.33 ? 224 ARG A N   1 
ATOM   1810  C  CA  . ARG A  1 225 ? 15.598  -19.158 28.153  1.00 23.67 ? 224 ARG A CA  1 
ATOM   1811  C  C   . ARG A  1 225 ? 15.755  -17.676 28.508  1.00 25.23 ? 224 ARG A C   1 
ATOM   1812  O  O   . ARG A  1 225 ? 14.798  -17.033 28.941  1.00 23.36 ? 224 ARG A O   1 
ATOM   1813  C  CB  . ARG A  1 225 ? 15.980  -20.039 29.346  1.00 22.26 ? 224 ARG A CB  1 
ATOM   1814  C  CG  . ARG A  1 225 ? 15.077  -19.871 30.571  1.00 22.23 ? 224 ARG A CG  1 
ATOM   1815  C  CD  . ARG A  1 225 ? 15.525  -20.731 31.727  1.00 21.42 ? 224 ARG A CD  1 
ATOM   1816  N  NE  . ARG A  1 225 ? 16.847  -20.354 32.217  1.00 23.23 ? 224 ARG A NE  1 
ATOM   1817  C  CZ  . ARG A  1 225 ? 17.521  -21.007 33.160  1.00 22.97 ? 224 ARG A CZ  1 
ATOM   1818  N  NH1 . ARG A  1 225 ? 16.989  -22.047 33.783  1.00 22.37 ? 224 ARG A NH1 1 
ATOM   1819  N  NH2 . ARG A  1 225 ? 18.742  -20.615 33.500  1.00 24.21 ? 224 ARG A NH2 1 
ATOM   1820  N  N   . GLU A  1 226 ? 16.956  -17.147 28.291  1.00 27.33 ? 225 GLU A N   1 
ATOM   1821  C  CA  . GLU A  1 226 ? 17.249  -15.724 28.517  1.00 30.38 ? 225 GLU A CA  1 
ATOM   1822  C  C   . GLU A  1 226 ? 16.284  -14.820 27.781  1.00 27.96 ? 225 GLU A C   1 
ATOM   1823  O  O   . GLU A  1 226 ? 15.698  -13.897 28.367  1.00 27.52 ? 225 GLU A O   1 
ATOM   1824  C  CB  . GLU A  1 226 ? 18.676  -15.394 28.039  1.00 35.03 ? 225 GLU A CB  1 
ATOM   1825  C  CG  . GLU A  1 226 ? 19.781  -16.156 28.749  1.00 40.26 ? 225 GLU A CG  1 
ATOM   1826  C  CD  . GLU A  1 226 ? 21.129  -16.156 27.971  1.00 47.92 ? 225 GLU A CD  1 
ATOM   1827  O  OE1 . GLU A  1 226 ? 21.202  -15.598 26.845  1.00 48.19 ? 225 GLU A OE1 1 
ATOM   1828  O  OE2 . GLU A  1 226 ? 22.132  -16.720 28.487  1.00 53.86 ? 225 GLU A OE2 1 
ATOM   1829  N  N   . GLN A  1 227 ? 16.054  -15.101 26.503  1.00 27.82 ? 226 GLN A N   1 
ATOM   1830  C  CA  . GLN A  1 227 ? 15.114  -14.307 25.731  1.00 28.09 ? 226 GLN A CA  1 
ATOM   1831  C  C   . GLN A  1 227 ? 13.699  -14.560 26.145  1.00 23.87 ? 226 GLN A C   1 
ATOM   1832  O  O   . GLN A  1 227 ? 12.893  -13.639 26.261  1.00 22.93 ? 226 GLN A O   1 
ATOM   1833  C  CB  . GLN A  1 227 ? 15.227  -14.578 24.213  1.00 29.25 ? 226 GLN A CB  1 
ATOM   1834  C  CG  . GLN A  1 227 ? 14.311  -13.712 23.353  1.00 30.12 ? 226 GLN A CG  1 
ATOM   1835  C  CD  . GLN A  1 227 ? 12.865  -14.176 23.243  1.00 31.20 ? 226 GLN A CD  1 
ATOM   1836  O  OE1 . GLN A  1 227 ? 11.927  -13.364 23.212  1.00 34.76 ? 226 GLN A OE1 1 
ATOM   1837  N  NE2 . GLN A  1 227 ? 12.677  -15.471 23.124  1.00 33.34 ? 226 GLN A NE2 1 
ATOM   1838  N  N   . GLN A  1 228 ? 13.372  -15.829 26.334  1.00 22.48 ? 227 GLN A N   1 
ATOM   1839  C  CA  . GLN A  1 228 ? 11.988  -16.205 26.620  1.00 20.86 ? 227 GLN A CA  1 
ATOM   1840  C  C   . GLN A  1 228 ? 11.504  -15.575 27.926  1.00 18.51 ? 227 GLN A C   1 
ATOM   1841  O  O   . GLN A  1 228 ? 10.370  -15.093 28.021  1.00 17.54 ? 227 GLN A O   1 
ATOM   1842  C  CB  . GLN A  1 228 ? 11.866  -17.733 26.629  1.00 21.83 ? 227 GLN A CB  1 
ATOM   1843  C  CG  . GLN A  1 228 ? 12.060  -18.329 25.226  1.00 23.13 ? 227 GLN A CG  1 
ATOM   1844  C  CD  . GLN A  1 228 ? 12.295  -19.827 25.183  1.00 24.76 ? 227 GLN A CD  1 
ATOM   1845  O  OE1 . GLN A  1 228 ? 12.849  -20.438 26.112  1.00 22.21 ? 227 GLN A OE1 1 
ATOM   1846  N  NE2 . GLN A  1 228 ? 11.884  -20.436 24.071  1.00 27.70 ? 227 GLN A NE2 1 
ATOM   1847  N  N   . ARG A  1 229 ? 12.365  -15.552 28.936  1.00 18.58 ? 228 ARG A N   1 
ATOM   1848  C  CA  . ARG A  1 229 ? 12.000  -14.926 30.228  1.00 17.24 ? 228 ARG A CA  1 
ATOM   1849  C  C   . ARG A  1 229 ? 11.770  -13.445 30.078  1.00 17.23 ? 228 ARG A C   1 
ATOM   1850  O  O   . ARG A  1 229 ? 10.932  -12.871 30.792  1.00 18.29 ? 228 ARG A O   1 
ATOM   1851  C  CB  . ARG A  1 229 ? 13.094  -15.148 31.263  1.00 18.14 ? 228 ARG A CB  1 
ATOM   1852  C  CG  . ARG A  1 229 ? 13.097  -16.539 31.858  1.00 17.87 ? 228 ARG A CG  1 
ATOM   1853  C  CD  . ARG A  1 229 ? 14.280  -16.734 32.795  1.00 19.34 ? 228 ARG A CD  1 
ATOM   1854  N  NE  . ARG A  1 229 ? 14.201  -18.037 33.481  1.00 18.67 ? 228 ARG A NE  1 
ATOM   1855  C  CZ  . ARG A  1 229 ? 15.041  -18.444 34.428  1.00 19.96 ? 228 ARG A CZ  1 
ATOM   1856  N  NH1 . ARG A  1 229 ? 16.069  -17.690 34.802  1.00 20.81 ? 228 ARG A NH1 1 
ATOM   1857  N  NH2 . ARG A  1 229 ? 14.867  -19.621 35.006  1.00 19.53 ? 228 ARG A NH2 1 
ATOM   1858  N  N   . SER A  1 230 ? 12.546  -12.819 29.193  1.00 16.46 ? 229 SER A N   1 
ATOM   1859  C  CA  . SER A  1 230 ? 12.509  -11.359 29.027  1.00 17.45 ? 229 SER A CA  1 
ATOM   1860  C  C   . SER A  1 230 ? 11.199  -10.859 28.401  1.00 17.88 ? 229 SER A C   1 
ATOM   1861  O  O   . SER A  1 230 ? 10.866  -9.688  28.571  1.00 17.93 ? 229 SER A O   1 
ATOM   1862  C  CB  . SER A  1 230 ? 13.727  -10.863 28.211  1.00 17.87 ? 229 SER A CB  1 
ATOM   1863  O  OG  . SER A  1 230 ? 13.565  -11.078 26.831  1.00 18.93 ? 229 SER A OG  1 
ATOM   1864  N  N   . ALA A  1 231 ? 10.513  -11.715 27.651  1.00 17.19 ? 230 ALA A N   1 
ATOM   1865  C  CA  . ALA A  1 231 ? 9.237   -11.353 27.013  1.00 17.88 ? 230 ALA A CA  1 
ATOM   1866  C  C   . ALA A  1 231 ? 8.086   -11.403 28.024  1.00 18.07 ? 230 ALA A C   1 
ATOM   1867  O  O   . ALA A  1 231 ? 7.731   -12.461 28.538  1.00 19.96 ? 230 ALA A O   1 
ATOM   1868  C  CB  . ALA A  1 231 ? 8.958   -12.251 25.828  1.00 18.00 ? 230 ALA A CB  1 
ATOM   1869  N  N   . VAL A  1 232 ? 7.521   -10.257 28.301  1.00 17.75 ? 231 VAL A N   1 
ATOM   1870  C  CA  . VAL A  1 232 ? 6.428   -10.108 29.271  1.00 18.61 ? 231 VAL A CA  1 
ATOM   1871  C  C   . VAL A  1 232 ? 5.248   -11.007 28.903  1.00 18.04 ? 231 VAL A C   1 
ATOM   1872  O  O   . VAL A  1 232 ? 4.586   -11.553 29.794  1.00 17.56 ? 231 VAL A O   1 
ATOM   1873  C  CB  . VAL A  1 232 ? 5.923   -8.650  29.362  1.00 19.50 ? 231 VAL A CB  1 
ATOM   1874  C  CG1 . VAL A  1 232 ? 4.869   -8.516  30.454  1.00 19.16 ? 231 VAL A CG1 1 
ATOM   1875  C  CG2 . VAL A  1 232 ? 7.079   -7.694  29.642  1.00 20.68 ? 231 VAL A CG2 1 
ATOM   1876  N  N   . SER A  1 233 ? 5.004   -11.183 27.604  1.00 17.49 ? 232 SER A N   1 
ATOM   1877  C  CA  . SER A  1 233 ? 3.870   -11.994 27.147  1.00 17.37 ? 232 SER A CA  1 
ATOM   1878  C  C   . SER A  1 233 ? 3.954   -13.424 27.659  1.00 17.44 ? 232 SER A C   1 
ATOM   1879  O  O   . SER A  1 233 ? 2.935   -14.076 27.822  1.00 16.97 ? 232 SER A O   1 
ATOM   1880  C  CB  . SER A  1 233 ? 3.758   -11.964 25.605  1.00 17.35 ? 232 SER A CB  1 
ATOM   1881  O  OG  . SER A  1 233 ? 4.987   -12.311 24.990  1.00 16.62 ? 232 SER A OG  1 
ATOM   1882  N  N   . THR A  1 234 ? 5.157   -13.942 27.900  1.00 17.74 ? 233 THR A N   1 
ATOM   1883  C  CA  . THR A  1 234 ? 5.284   -15.304 28.458  1.00 18.85 ? 233 THR A CA  1 
ATOM   1884  C  C   . THR A  1 234 ? 4.676   -15.428 29.857  1.00 17.62 ? 233 THR A C   1 
ATOM   1885  O  O   . THR A  1 234 ? 3.883   -16.332 30.104  1.00 18.73 ? 233 THR A O   1 
ATOM   1886  C  CB  . THR A  1 234 ? 6.765   -15.733 28.507  1.00 20.68 ? 233 THR A CB  1 
ATOM   1887  O  OG1 . THR A  1 234 ? 7.287   -15.577 27.172  1.00 23.77 ? 233 THR A OG1 1 
ATOM   1888  C  CG2 . THR A  1 234 ? 6.926   -17.165 28.926  1.00 20.73 ? 233 THR A CG2 1 
ATOM   1889  N  N   . SER A  1 235 ? 5.038   -14.523 30.751  1.00 16.52 ? 234 SER A N   1 
ATOM   1890  C  CA  . SER A  1 235 ? 4.509   -14.510 32.118  1.00 16.30 ? 234 SER A CA  1 
ATOM   1891  C  C   . SER A  1 235 ? 3.014   -14.174 32.146  1.00 15.88 ? 234 SER A C   1 
ATOM   1892  O  O   . SER A  1 235 ? 2.279   -14.687 32.991  1.00 14.76 ? 234 SER A O   1 
ATOM   1893  C  CB  . SER A  1 235 ? 5.286   -13.528 33.011  1.00 17.20 ? 234 SER A CB  1 
ATOM   1894  O  OG  . SER A  1 235 ? 6.629   -13.980 33.226  1.00 17.61 ? 234 SER A OG  1 
ATOM   1895  N  N   . TRP A  1 236 ? 2.563   -13.334 31.216  1.00 14.88 ? 235 TRP A N   1 
ATOM   1896  C  CA  . TRP A  1 236 ? 1.133   -13.016 31.071  1.00 14.96 ? 235 TRP A CA  1 
ATOM   1897  C  C   . TRP A  1 236 ? 0.276   -14.266 30.798  1.00 15.49 ? 235 TRP A C   1 
ATOM   1898  O  O   . TRP A  1 236 ? -0.887  -14.338 31.200  1.00 16.47 ? 235 TRP A O   1 
ATOM   1899  C  CB  . TRP A  1 236 ? 0.972   -12.023 29.924  1.00 15.00 ? 235 TRP A CB  1 
ATOM   1900  C  CG  . TRP A  1 236 ? -0.416  -11.570 29.638  1.00 14.97 ? 235 TRP A CG  1 
ATOM   1901  C  CD1 . TRP A  1 236 ? -1.376  -11.234 30.544  1.00 15.49 ? 235 TRP A CD1 1 
ATOM   1902  C  CD2 . TRP A  1 236 ? -1.006  -11.389 28.343  1.00 15.66 ? 235 TRP A CD2 1 
ATOM   1903  N  NE1 . TRP A  1 236 ? -2.536  -10.868 29.904  1.00 15.81 ? 235 TRP A NE1 1 
ATOM   1904  C  CE2 . TRP A  1 236 ? -2.338  -10.945 28.549  1.00 16.13 ? 235 TRP A CE2 1 
ATOM   1905  C  CE3 . TRP A  1 236 ? -0.548  -11.558 27.031  1.00 15.42 ? 235 TRP A CE3 1 
ATOM   1906  C  CZ2 . TRP A  1 236 ? -3.206  -10.682 27.492  1.00 16.24 ? 235 TRP A CZ2 1 
ATOM   1907  C  CZ3 . TRP A  1 236 ? -1.424  -11.302 25.978  1.00 15.37 ? 235 TRP A CZ3 1 
ATOM   1908  C  CH2 . TRP A  1 236 ? -2.730  -10.861 26.219  1.00 16.21 ? 235 TRP A CH2 1 
ATOM   1909  N  N   . LEU A  1 237 ? 0.849   -15.246 30.107  1.00 16.19 ? 236 LEU A N   1 
ATOM   1910  C  CA  . LEU A  1 237 ? 0.102   -16.447 29.756  1.00 16.93 ? 236 LEU A CA  1 
ATOM   1911  C  C   . LEU A  1 237 ? 0.296   -17.650 30.709  1.00 15.98 ? 236 LEU A C   1 
ATOM   1912  O  O   . LEU A  1 237 ? -0.132  -18.764 30.368  1.00 16.11 ? 236 LEU A O   1 
ATOM   1913  C  CB  . LEU A  1 237 ? 0.403   -16.827 28.313  1.00 19.53 ? 236 LEU A CB  1 
ATOM   1914  C  CG  . LEU A  1 237 ? -0.151  -15.801 27.296  1.00 22.89 ? 236 LEU A CG  1 
ATOM   1915  C  CD1 . LEU A  1 237 ? 0.169   -16.312 25.917  1.00 26.03 ? 236 LEU A CD1 1 
ATOM   1916  C  CD2 . LEU A  1 237 ? -1.632  -15.573 27.463  1.00 26.13 ? 236 LEU A CD2 1 
ATOM   1917  N  N   . LEU A  1 238 ? 0.869   -17.440 31.895  1.00 14.98 ? 237 LEU A N   1 
ATOM   1918  C  CA  . LEU A  1 238 ? 0.801   -18.473 32.941  1.00 14.79 ? 237 LEU A CA  1 
ATOM   1919  C  C   . LEU A  1 238 ? -0.665  -18.765 33.274  1.00 14.81 ? 237 LEU A C   1 
ATOM   1920  O  O   . LEU A  1 238 ? -1.523  -17.877 33.197  1.00 13.34 ? 237 LEU A O   1 
ATOM   1921  C  CB  . LEU A  1 238 ? 1.539   -18.056 34.226  1.00 15.49 ? 237 LEU A CB  1 
ATOM   1922  C  CG  . LEU A  1 238 ? 3.068   -17.993 34.182  1.00 15.98 ? 237 LEU A CG  1 
ATOM   1923  C  CD1 . LEU A  1 238 ? 3.598   -17.165 35.346  1.00 17.09 ? 237 LEU A CD1 1 
ATOM   1924  C  CD2 . LEU A  1 238 ? 3.625   -19.402 34.243  1.00 17.34 ? 237 LEU A CD2 1 
ATOM   1925  N  N   . PRO A  1 239 ? -0.968  -20.025 33.614  1.00 14.76 ? 238 PRO A N   1 
ATOM   1926  C  CA  . PRO A  1 239 ? -2.313  -20.427 33.973  1.00 15.29 ? 238 PRO A CA  1 
ATOM   1927  C  C   . PRO A  1 239 ? -3.031  -19.498 34.938  1.00 16.30 ? 238 PRO A C   1 
ATOM   1928  O  O   . PRO A  1 239 ? -2.441  -19.045 35.942  1.00 15.49 ? 238 PRO A O   1 
ATOM   1929  C  CB  . PRO A  1 239 ? -2.095  -21.804 34.575  1.00 15.40 ? 238 PRO A CB  1 
ATOM   1930  C  CG  . PRO A  1 239 ? -0.940  -22.343 33.799  1.00 15.78 ? 238 PRO A CG  1 
ATOM   1931  C  CD  . PRO A  1 239 ? -0.033  -21.162 33.614  1.00 15.03 ? 238 PRO A CD  1 
ATOM   1932  N  N   . TYR A  1 240 ? -4.316  -19.275 34.660  1.00 17.05 ? 239 TYR A N   1 
ATOM   1933  C  CA  . TYR A  1 240 ? -5.207  -18.496 35.496  1.00 17.44 ? 239 TYR A CA  1 
ATOM   1934  C  C   . TYR A  1 240 ? -6.242  -19.350 36.237  1.00 18.62 ? 239 TYR A C   1 
ATOM   1935  O  O   . TYR A  1 240 ? -6.697  -20.390 35.726  1.00 17.52 ? 239 TYR A O   1 
ATOM   1936  C  CB  . TYR A  1 240 ? -5.970  -17.505 34.635  1.00 17.39 ? 239 TYR A CB  1 
ATOM   1937  C  CG  . TYR A  1 240 ? -5.115  -16.354 34.128  1.00 17.39 ? 239 TYR A CG  1 
ATOM   1938  C  CD1 . TYR A  1 240 ? -4.300  -16.515 33.014  1.00 17.46 ? 239 TYR A CD1 1 
ATOM   1939  C  CD2 . TYR A  1 240 ? -5.143  -15.107 34.756  1.00 17.27 ? 239 TYR A CD2 1 
ATOM   1940  C  CE1 . TYR A  1 240 ? -3.499  -15.470 32.559  1.00 16.98 ? 239 TYR A CE1 1 
ATOM   1941  C  CE2 . TYR A  1 240 ? -4.368  -14.055 34.302  1.00 18.06 ? 239 TYR A CE2 1 
ATOM   1942  C  CZ  . TYR A  1 240 ? -3.559  -14.235 33.182  1.00 17.60 ? 239 TYR A CZ  1 
ATOM   1943  O  OH  . TYR A  1 240 ? -2.779  -13.186 32.744  1.00 17.98 ? 239 TYR A OH  1 
ATOM   1944  N  N   . ASN A  1 241 ? -6.680  -18.864 37.392  1.00 18.54 ? 240 ASN A N   1 
ATOM   1945  C  CA  . ASN A  1 241 ? -7.682  -19.591 38.197  1.00 20.80 ? 240 ASN A CA  1 
ATOM   1946  C  C   . ASN A  1 241 ? -9.113  -19.582 37.683  1.00 21.70 ? 240 ASN A C   1 
ATOM   1947  O  O   . ASN A  1 241 ? -9.958  -20.262 38.270  1.00 24.19 ? 240 ASN A O   1 
ATOM   1948  C  CB  . ASN A  1 241 ? -7.694  -19.140 39.663  1.00 23.10 ? 240 ASN A CB  1 
ATOM   1949  C  CG  . ASN A  1 241 ? -7.930  -17.662 39.832  1.00 24.64 ? 240 ASN A CG  1 
ATOM   1950  O  OD1 . ASN A  1 241 ? -8.466  -16.980 38.954  1.00 23.85 ? 240 ASN A OD1 1 
ATOM   1951  N  ND2 . ASN A  1 241 ? -7.519  -17.147 40.974  1.00 26.67 ? 240 ASN A ND2 1 
ATOM   1952  N  N   . TYR A  1 242 ? -9.412  -18.844 36.628  1.00 20.59 ? 241 TYR A N   1 
ATOM   1953  C  CA  . TYR A  1 242 ? -10.771 -18.936 36.084  1.00 23.00 ? 241 TYR A CA  1 
ATOM   1954  C  C   . TYR A  1 242 ? -10.918 -20.109 35.099  1.00 24.28 ? 241 TYR A C   1 
ATOM   1955  O  O   . TYR A  1 242 ? -12.028 -20.462 34.719  1.00 24.52 ? 241 TYR A O   1 
ATOM   1956  C  CB  . TYR A  1 242 ? -11.215 -17.630 35.470  1.00 24.00 ? 241 TYR A CB  1 
ATOM   1957  C  CG  . TYR A  1 242 ? -10.305 -17.036 34.418  1.00 24.58 ? 241 TYR A CG  1 
ATOM   1958  C  CD1 . TYR A  1 242 ? -10.308 -17.529 33.124  1.00 25.78 ? 241 TYR A CD1 1 
ATOM   1959  C  CD2 . TYR A  1 242 ? -9.455  -15.976 34.715  1.00 24.77 ? 241 TYR A CD2 1 
ATOM   1960  C  CE1 . TYR A  1 242 ? -9.512  -16.978 32.154  1.00 26.75 ? 241 TYR A CE1 1 
ATOM   1961  C  CE2 . TYR A  1 242 ? -8.639  -15.416 33.739  1.00 26.62 ? 241 TYR A CE2 1 
ATOM   1962  C  CZ  . TYR A  1 242 ? -8.678  -15.934 32.465  1.00 26.62 ? 241 TYR A CZ  1 
ATOM   1963  O  OH  . TYR A  1 242 ? -7.906  -15.413 31.478  1.00 29.76 ? 241 TYR A OH  1 
ATOM   1964  N  N   . THR A  1 243 ? -9.798  -20.741 34.759  1.00 22.81 ? 242 THR A N   1 
ATOM   1965  C  CA  . THR A  1 243 ? -9.762  -21.958 33.953  1.00 25.07 ? 242 THR A CA  1 
ATOM   1966  C  C   . THR A  1 243 ? -9.291  -23.180 34.723  1.00 24.02 ? 242 THR A C   1 
ATOM   1967  O  O   . THR A  1 243 ? -9.850  -24.261 34.594  1.00 25.82 ? 242 THR A O   1 
ATOM   1968  C  CB  . THR A  1 243 ? -8.801  -21.734 32.770  1.00 25.49 ? 242 THR A CB  1 
ATOM   1969  O  OG1 . THR A  1 243 ? -9.402  -20.782 31.900  1.00 28.10 ? 242 THR A OG1 1 
ATOM   1970  C  CG2 . THR A  1 243 ? -8.550  -22.984 32.003  1.00 28.44 ? 242 THR A CG2 1 
ATOM   1971  N  N   A TRP A  1 244 ? -8.249  -23.007 35.528  0.50 21.55 ? 243 TRP A N   1 
ATOM   1972  N  N   B TRP A  1 244 ? -8.252  -23.009 35.533  0.50 23.45 ? 243 TRP A N   1 
ATOM   1973  C  CA  A TRP A  1 244 ? -7.587  -24.098 36.191  0.50 20.48 ? 243 TRP A CA  1 
ATOM   1974  C  CA  B TRP A  1 244 ? -7.616  -24.111 36.215  0.50 23.49 ? 243 TRP A CA  1 
ATOM   1975  C  C   A TRP A  1 244 ? -7.894  -24.073 37.692  0.50 21.36 ? 243 TRP A C   1 
ATOM   1976  C  C   B TRP A  1 244 ? -7.908  -24.073 37.700  0.50 23.06 ? 243 TRP A C   1 
ATOM   1977  O  O   A TRP A  1 244 ? -8.045  -23.006 38.287  0.50 20.87 ? 243 TRP A O   1 
ATOM   1978  O  O   B TRP A  1 244 ? -8.046  -23.006 38.289  0.50 22.37 ? 243 TRP A O   1 
ATOM   1979  C  CB  A TRP A  1 244 ? -6.076  -23.939 35.995  0.50 19.04 ? 243 TRP A CB  1 
ATOM   1980  C  CB  B TRP A  1 244 ? -6.112  -24.019 36.026  0.50 24.07 ? 243 TRP A CB  1 
ATOM   1981  C  CG  A TRP A  1 244 ? -5.598  -23.877 34.542  0.50 17.67 ? 243 TRP A CG  1 
ATOM   1982  C  CG  B TRP A  1 244 ? -5.629  -24.791 34.853  0.50 25.43 ? 243 TRP A CG  1 
ATOM   1983  C  CD1 A TRP A  1 244 ? -5.549  -22.773 33.747  0.50 16.93 ? 243 TRP A CD1 1 
ATOM   1984  C  CD1 B TRP A  1 244 ? -5.519  -26.157 34.790  0.50 26.12 ? 243 TRP A CD1 1 
ATOM   1985  C  CD2 A TRP A  1 244 ? -5.066  -24.952 33.763  0.50 16.99 ? 243 TRP A CD2 1 
ATOM   1986  C  CD2 B TRP A  1 244 ? -5.137  -24.297 33.628  0.50 24.62 ? 243 TRP A CD2 1 
ATOM   1987  N  NE1 A TRP A  1 244 ? -5.026  -23.092 32.517  0.50 16.22 ? 243 TRP A NE1 1 
ATOM   1988  N  NE1 B TRP A  1 244 ? -5.004  -26.537 33.588  0.50 26.49 ? 243 TRP A NE1 1 
ATOM   1989  C  CE2 A TRP A  1 244 ? -4.728  -24.427 32.500  0.50 16.54 ? 243 TRP A CE2 1 
ATOM   1990  C  CE2 B TRP A  1 244 ? -4.755  -25.411 32.849  0.50 25.64 ? 243 TRP A CE2 1 
ATOM   1991  C  CE3 A TRP A  1 244 ? -4.848  -26.311 34.007  0.50 17.65 ? 243 TRP A CE3 1 
ATOM   1992  C  CE3 B TRP A  1 244 ? -4.989  -23.026 33.096  0.50 24.26 ? 243 TRP A CE3 1 
ATOM   1993  C  CZ2 A TRP A  1 244 ? -4.190  -25.208 31.500  0.50 16.56 ? 243 TRP A CZ2 1 
ATOM   1994  C  CZ2 B TRP A  1 244 ? -4.234  -25.277 31.572  0.50 25.08 ? 243 TRP A CZ2 1 
ATOM   1995  C  CZ3 A TRP A  1 244 ? -4.303  -27.092 33.000  0.50 17.56 ? 243 TRP A CZ3 1 
ATOM   1996  C  CZ3 B TRP A  1 244 ? -4.483  -22.907 31.855  0.50 23.97 ? 243 TRP A CZ3 1 
ATOM   1997  C  CH2 A TRP A  1 244 ? -3.980  -26.531 31.764  0.50 16.79 ? 243 TRP A CH2 1 
ATOM   1998  C  CH2 B TRP A  1 244 ? -4.110  -24.018 31.101  0.50 24.93 ? 243 TRP A CH2 1 
ATOM   1999  N  N   . SER A  1 245 ? -7.955  -25.248 38.302  1.00 22.12 ? 244 SER A N   1 
ATOM   2000  C  CA  . SER A  1 245 ? -8.070  -25.362 39.735  1.00 23.34 ? 244 SER A CA  1 
ATOM   2001  C  C   . SER A  1 245 ? -6.837  -24.719 40.403  1.00 22.79 ? 244 SER A C   1 
ATOM   2002  O  O   . SER A  1 245 ? -5.699  -24.999 40.025  1.00 21.88 ? 244 SER A O   1 
ATOM   2003  C  CB  . SER A  1 245 ? -8.141  -26.830 40.140  1.00 24.25 ? 244 SER A CB  1 
ATOM   2004  O  OG  . SER A  1 245 ? -8.041  -26.943 41.532  1.00 25.38 ? 244 SER A OG  1 
ATOM   2005  N  N   . PRO A  1 246 ? -7.058  -23.910 41.438  1.00 24.39 ? 245 PRO A N   1 
ATOM   2006  C  CA  . PRO A  1 246 ? -5.908  -23.376 42.181  1.00 25.25 ? 245 PRO A CA  1 
ATOM   2007  C  C   . PRO A  1 246 ? -5.028  -24.415 42.860  1.00 25.49 ? 245 PRO A C   1 
ATOM   2008  O  O   . PRO A  1 246 ? -3.893  -24.115 43.216  1.00 27.33 ? 245 PRO A O   1 
ATOM   2009  C  CB  . PRO A  1 246 ? -6.558  -22.459 43.233  1.00 26.12 ? 245 PRO A CB  1 
ATOM   2010  C  CG  . PRO A  1 246 ? -7.874  -22.071 42.605  1.00 27.43 ? 245 PRO A CG  1 
ATOM   2011  C  CD  . PRO A  1 246 ? -8.331  -23.353 41.941  1.00 26.80 ? 245 PRO A CD  1 
ATOM   2012  N  N   . GLU A  1 247 ? -5.516  -25.637 43.004  1.00 25.40 ? 246 GLU A N   1 
ATOM   2013  C  CA  . GLU A  1 247 ? -4.720  -26.701 43.594  1.00 27.63 ? 246 GLU A CA  1 
ATOM   2014  C  C   . GLU A  1 247 ? -4.028  -27.632 42.573  1.00 26.42 ? 246 GLU A C   1 
ATOM   2015  O  O   . GLU A  1 247 ? -3.326  -28.559 42.962  1.00 27.00 ? 246 GLU A O   1 
ATOM   2016  C  CB  . GLU A  1 247 ? -5.593  -27.525 44.517  1.00 31.05 ? 246 GLU A CB  1 
ATOM   2017  C  CG  . GLU A  1 247 ? -6.094  -26.735 45.720  1.00 35.12 ? 246 GLU A CG  1 
ATOM   2018  C  CD  . GLU A  1 247 ? -7.159  -25.665 45.431  1.00 38.69 ? 246 GLU A CD  1 
ATOM   2019  O  OE1 . GLU A  1 247 ? -8.056  -25.900 44.583  1.00 42.91 ? 246 GLU A OE1 1 
ATOM   2020  O  OE2 . GLU A  1 247 ? -7.142  -24.587 46.073  1.00 43.99 ? 246 GLU A OE2 1 
ATOM   2021  N  N   . LYS A  1 248 ? -4.233  -27.414 41.281  1.00 24.44 ? 247 LYS A N   1 
ATOM   2022  C  CA  . LYS A  1 248 ? -3.550  -28.242 40.288  1.00 24.69 ? 247 LYS A CA  1 
ATOM   2023  C  C   . LYS A  1 248 ? -2.032  -27.966 40.333  1.00 22.17 ? 247 LYS A C   1 
ATOM   2024  O  O   . LYS A  1 248 ? -1.605  -26.818 40.257  1.00 21.19 ? 247 LYS A O   1 
ATOM   2025  C  CB  . LYS A  1 248 ? -4.053  -27.973 38.870  1.00 26.70 ? 247 LYS A CB  1 
ATOM   2026  C  CG  . LYS A  1 248 ? -3.166  -28.722 37.868  1.00 29.44 ? 247 LYS A CG  1 
ATOM   2027  C  CD  . LYS A  1 248 ? -3.680  -28.821 36.473  1.00 32.68 ? 247 LYS A CD  1 
ATOM   2028  C  CE  . LYS A  1 248 ? -2.654  -29.546 35.601  1.00 32.92 ? 247 LYS A CE  1 
ATOM   2029  N  NZ  . LYS A  1 248 ? -2.579  -30.992 35.944  1.00 35.93 ? 247 LYS A NZ  1 
ATOM   2030  N  N   . VAL A  1 249 ? -1.239  -29.011 40.409  1.00 21.21 ? 248 VAL A N   1 
ATOM   2031  C  CA  . VAL A  1 249 ? 0.222   -28.879 40.410  1.00 21.34 ? 248 VAL A CA  1 
ATOM   2032  C  C   . VAL A  1 249 ? 0.730   -28.871 38.980  1.00 20.86 ? 248 VAL A C   1 
ATOM   2033  O  O   . VAL A  1 249 ? 0.498   -29.826 38.243  1.00 22.14 ? 248 VAL A O   1 
ATOM   2034  C  CB  . VAL A  1 249 ? 0.889   -30.035 41.176  1.00 22.65 ? 248 VAL A CB  1 
ATOM   2035  C  CG1 . VAL A  1 249 ? 2.413   -29.948 41.094  1.00 22.98 ? 248 VAL A CG1 1 
ATOM   2036  C  CG2 . VAL A  1 249 ? 0.437   -30.014 42.621  1.00 24.32 ? 248 VAL A CG2 1 
ATOM   2037  N  N   . PHE A  1 250 ? 1.393   -27.799 38.578  1.00 19.19 ? 249 PHE A N   1 
ATOM   2038  C  CA  . PHE A  1 250 ? 1.961   -27.686 37.236  1.00 19.62 ? 249 PHE A CA  1 
ATOM   2039  C  C   . PHE A  1 250 ? 3.412   -28.131 37.180  1.00 19.50 ? 249 PHE A C   1 
ATOM   2040  O  O   . PHE A  1 250 ? 3.887   -28.571 36.128  1.00 19.56 ? 249 PHE A O   1 
ATOM   2041  C  CB  . PHE A  1 250 ? 1.862   -26.234 36.740  1.00 18.83 ? 249 PHE A CB  1 
ATOM   2042  C  CG  . PHE A  1 250 ? 0.461   -25.819 36.388  1.00 18.69 ? 249 PHE A CG  1 
ATOM   2043  C  CD1 . PHE A  1 250 ? -0.126  -26.264 35.222  1.00 18.80 ? 249 PHE A CD1 1 
ATOM   2044  C  CD2 . PHE A  1 250 ? -0.265  -24.984 37.221  1.00 18.50 ? 249 PHE A CD2 1 
ATOM   2045  C  CE1 . PHE A  1 250 ? -1.427  -25.903 34.894  1.00 19.34 ? 249 PHE A CE1 1 
ATOM   2046  C  CE2 . PHE A  1 250 ? -1.553  -24.626 36.903  1.00 18.31 ? 249 PHE A CE2 1 
ATOM   2047  C  CZ  . PHE A  1 250 ? -2.134  -25.070 35.739  1.00 18.64 ? 249 PHE A CZ  1 
ATOM   2048  N  N   . VAL A  1 251 ? 4.125   -27.957 38.289  1.00 18.47 ? 250 VAL A N   1 
ATOM   2049  C  CA  . VAL A  1 251 ? 5.533   -28.267 38.358  1.00 18.37 ? 250 VAL A CA  1 
ATOM   2050  C  C   . VAL A  1 251 ? 5.807   -29.016 39.665  1.00 19.68 ? 250 VAL A C   1 
ATOM   2051  O  O   . VAL A  1 251 ? 5.503   -28.485 40.748  1.00 18.44 ? 250 VAL A O   1 
ATOM   2052  C  CB  . VAL A  1 251 ? 6.424   -26.991 38.292  1.00 18.16 ? 250 VAL A CB  1 
ATOM   2053  C  CG1 . VAL A  1 251 ? 7.898   -27.338 38.526  1.00 18.68 ? 250 VAL A CG1 1 
ATOM   2054  C  CG2 . VAL A  1 251 ? 6.303   -26.304 36.944  1.00 18.08 ? 250 VAL A CG2 1 
ATOM   2055  N  N   . GLN A  1 252 ? 6.378   -30.217 39.548  1.00 20.59 ? 251 GLN A N   1 
ATOM   2056  C  CA  . GLN A  1 252 ? 6.858   -30.962 40.699  1.00 22.76 ? 251 GLN A CA  1 
ATOM   2057  C  C   . GLN A  1 252 ? 8.364   -31.090 40.635  1.00 23.03 ? 251 GLN A C   1 
ATOM   2058  O  O   . GLN A  1 252 ? 8.906   -31.363 39.587  1.00 22.82 ? 251 GLN A O   1 
ATOM   2059  C  CB  . GLN A  1 252 ? 6.330   -32.400 40.710  1.00 25.75 ? 251 GLN A CB  1 
ATOM   2060  C  CG  . GLN A  1 252 ? 4.851   -32.593 40.879  1.00 29.78 ? 251 GLN A CG  1 
ATOM   2061  C  CD  . GLN A  1 252 ? 4.518   -34.082 40.985  1.00 33.00 ? 251 GLN A CD  1 
ATOM   2062  O  OE1 . GLN A  1 252 ? 4.987   -34.798 41.870  1.00 32.54 ? 251 GLN A OE1 1 
ATOM   2063  N  NE2 . GLN A  1 252 ? 3.754   -34.554 40.034  1.00 36.33 ? 251 GLN A NE2 1 
ATOM   2064  N  N   . THR A  1 253 ? 9.010   -30.982 41.786  1.00 24.87 ? 252 THR A N   1 
ATOM   2065  C  CA  . THR A  1 253 ? 10.442  -31.204 41.917  1.00 27.72 ? 252 THR A CA  1 
ATOM   2066  C  C   . THR A  1 253 ? 10.625  -32.128 43.126  1.00 30.86 ? 252 THR A C   1 
ATOM   2067  O  O   . THR A  1 253 ? 9.652   -32.439 43.816  1.00 32.83 ? 252 THR A O   1 
ATOM   2068  C  CB  . THR A  1 253 ? 11.212  -29.895 42.168  1.00 28.40 ? 252 THR A CB  1 
ATOM   2069  O  OG1 . THR A  1 253 ? 11.182  -29.568 43.572  1.00 30.54 ? 252 THR A OG1 1 
ATOM   2070  C  CG2 . THR A  1 253 ? 10.638  -28.763 41.367  1.00 27.59 ? 252 THR A CG2 1 
ATOM   2071  N  N   . PRO A  1 254 ? 11.865  -32.572 43.393  1.00 36.44 ? 253 PRO A N   1 
ATOM   2072  C  CA  . PRO A  1 254 ? 12.050  -33.472 44.561  1.00 39.98 ? 253 PRO A CA  1 
ATOM   2073  C  C   . PRO A  1 254 ? 11.705  -32.842 45.905  1.00 40.18 ? 253 PRO A C   1 
ATOM   2074  O  O   . PRO A  1 254 ? 11.364  -33.570 46.843  1.00 44.24 ? 253 PRO A O   1 
ATOM   2075  C  CB  . PRO A  1 254 ? 13.546  -33.823 44.513  1.00 40.20 ? 253 PRO A CB  1 
ATOM   2076  C  CG  . PRO A  1 254 ? 13.966  -33.527 43.112  1.00 40.29 ? 253 PRO A CG  1 
ATOM   2077  C  CD  . PRO A  1 254 ? 13.133  -32.346 42.692  1.00 36.95 ? 253 PRO A CD  1 
ATOM   2078  N  N   . THR A  1 255 ? 11.740  -31.511 45.999  1.00 38.39 ? 254 THR A N   1 
ATOM   2079  C  CA  . THR A  1 255 ? 11.512  -30.840 47.287  1.00 38.70 ? 254 THR A CA  1 
ATOM   2080  C  C   . THR A  1 255 ? 10.327  -29.877 47.366  1.00 36.40 ? 254 THR A C   1 
ATOM   2081  O  O   . THR A  1 255 ? 10.024  -29.371 48.436  1.00 40.07 ? 254 THR A O   1 
ATOM   2082  C  CB  . THR A  1 255 ? 12.739  -30.016 47.676  1.00 39.85 ? 254 THR A CB  1 
ATOM   2083  O  OG1 . THR A  1 255 ? 13.044  -29.111 46.617  1.00 43.27 ? 254 THR A OG1 1 
ATOM   2084  C  CG2 . THR A  1 255 ? 13.933  -30.939 47.937  1.00 41.98 ? 254 THR A CG2 1 
ATOM   2085  N  N   . ILE A  1 256 ? 9.663   -29.589 46.264  1.00 30.61 ? 255 ILE A N   1 
ATOM   2086  C  CA  . ILE A  1 256 ? 8.598   -28.598 46.284  1.00 28.37 ? 255 ILE A CA  1 
ATOM   2087  C  C   . ILE A  1 256 ? 7.698   -28.761 45.052  1.00 25.26 ? 255 ILE A C   1 
ATOM   2088  O  O   . ILE A  1 256 ? 8.147   -29.220 43.987  1.00 27.24 ? 255 ILE A O   1 
ATOM   2089  C  CB  . ILE A  1 256 ? 9.214   -27.172 46.350  1.00 30.37 ? 255 ILE A CB  1 
ATOM   2090  C  CG1 . ILE A  1 256 ? 8.158   -26.106 46.586  1.00 30.48 ? 255 ILE A CG1 1 
ATOM   2091  C  CG2 . ILE A  1 256 ? 10.003  -26.855 45.084  1.00 33.25 ? 255 ILE A CG2 1 
ATOM   2092  C  CD1 . ILE A  1 256 ? 8.764   -24.742 46.855  1.00 30.05 ? 255 ILE A CD1 1 
ATOM   2093  N  N   A ASN A  1 257 ? 6.412   -28.430 45.233  0.50 23.31 ? 256 ASN A N   1 
ATOM   2094  N  N   B ASN A  1 257 ? 6.439   -28.414 45.185  0.50 22.66 ? 256 ASN A N   1 
ATOM   2095  C  CA  A ASN A  1 257 ? 5.388   -28.375 44.189  0.50 22.65 ? 256 ASN A CA  1 
ATOM   2096  C  CA  B ASN A  1 257 ? 5.670   -28.277 43.968  0.50 21.46 ? 256 ASN A CA  1 
ATOM   2097  C  C   A ASN A  1 257 ? 4.995   -26.920 43.887  0.50 20.82 ? 256 ASN A C   1 
ATOM   2098  C  C   B ASN A  1 257 ? 5.031   -26.906 43.858  0.50 20.24 ? 256 ASN A C   1 
ATOM   2099  O  O   A ASN A  1 257 ? 5.029   -26.080 44.789  0.50 21.02 ? 256 ASN A O   1 
ATOM   2100  O  O   B ASN A  1 257 ? 5.014   -26.099 44.800  0.50 20.41 ? 256 ASN A O   1 
ATOM   2101  C  CB  A ASN A  1 257 ? 4.123   -29.099 44.679  0.50 22.42 ? 256 ASN A CB  1 
ATOM   2102  C  CB  B ASN A  1 257 ? 4.701   -29.440 43.699  0.50 21.07 ? 256 ASN A CB  1 
ATOM   2103  C  CG  A ASN A  1 257 ? 4.281   -30.604 44.651  0.50 23.00 ? 256 ASN A CG  1 
ATOM   2104  C  CG  B ASN A  1 257 ? 3.585   -29.529 44.694  0.50 20.94 ? 256 ASN A CG  1 
ATOM   2105  O  OD1 A ASN A  1 257 ? 5.029   -31.128 43.854  0.50 23.32 ? 256 ASN A OD1 1 
ATOM   2106  O  OD1 B ASN A  1 257 ? 2.888   -28.556 44.948  0.50 19.40 ? 256 ASN A OD1 1 
ATOM   2107  N  ND2 A ASN A  1 257 ? 3.588   -31.299 45.508  0.50 23.71 ? 256 ASN A ND2 1 
ATOM   2108  N  ND2 B ASN A  1 257 ? 3.396   -30.723 45.256  0.50 21.36 ? 256 ASN A ND2 1 
ATOM   2109  N  N   . TYR A  1 258 ? 4.584   -26.631 42.650  1.00 19.20 ? 257 TYR A N   1 
ATOM   2110  C  CA  . TYR A  1 258 ? 4.063   -25.300 42.306  1.00 18.14 ? 257 TYR A CA  1 
ATOM   2111  C  C   . TYR A  1 258 ? 2.726   -25.405 41.584  1.00 18.08 ? 257 TYR A C   1 
ATOM   2112  O  O   . TYR A  1 258 ? 2.617   -26.069 40.538  1.00 18.40 ? 257 TYR A O   1 
ATOM   2113  C  CB  . TYR A  1 258 ? 5.035   -24.532 41.425  1.00 17.46 ? 257 TYR A CB  1 
ATOM   2114  C  CG  . TYR A  1 258 ? 6.420   -24.373 42.000  1.00 17.66 ? 257 TYR A CG  1 
ATOM   2115  C  CD1 . TYR A  1 258 ? 6.735   -23.338 42.886  1.00 17.77 ? 257 TYR A CD1 1 
ATOM   2116  C  CD2 . TYR A  1 258 ? 7.420   -25.246 41.651  1.00 18.83 ? 257 TYR A CD2 1 
ATOM   2117  C  CE1 . TYR A  1 258 ? 8.013   -23.181 43.394  1.00 18.31 ? 257 TYR A CE1 1 
ATOM   2118  C  CE2 . TYR A  1 258 ? 8.692   -25.113 42.169  1.00 19.49 ? 257 TYR A CE2 1 
ATOM   2119  C  CZ  . TYR A  1 258 ? 8.994   -24.072 43.026  1.00 19.64 ? 257 TYR A CZ  1 
ATOM   2120  O  OH  . TYR A  1 258 ? 10.278  -23.948 43.509  1.00 21.14 ? 257 TYR A OH  1 
ATOM   2121  N  N   . THR A  1 259 ? 1.740   -24.722 42.158  1.00 17.23 ? 258 THR A N   1 
ATOM   2122  C  CA  . THR A  1 259 ? 0.425   -24.491 41.599  1.00 16.85 ? 258 THR A CA  1 
ATOM   2123  C  C   . THR A  1 259 ? 0.338   -23.040 41.119  1.00 16.63 ? 258 THR A C   1 
ATOM   2124  O  O   . THR A  1 259 ? 1.280   -22.247 41.314  1.00 15.36 ? 258 THR A O   1 
ATOM   2125  C  CB  . THR A  1 259 ? -0.685  -24.707 42.652  1.00 17.06 ? 258 THR A CB  1 
ATOM   2126  O  OG1 . THR A  1 259 ? -0.695  -23.627 43.611  1.00 16.82 ? 258 THR A OG1 1 
ATOM   2127  C  CG2 . THR A  1 259 ? -0.525  -26.029 43.413  1.00 17.98 ? 258 THR A CG2 1 
ATOM   2128  N  N   . LEU A  1 260 ? -0.817  -22.645 40.567  1.00 16.03 ? 259 LEU A N   1 
ATOM   2129  C  CA  . LEU A  1 260 ? -0.979  -21.268 40.139  1.00 16.40 ? 259 LEU A CA  1 
ATOM   2130  C  C   . LEU A  1 260 ? -1.066  -20.268 41.303  1.00 16.20 ? 259 LEU A C   1 
ATOM   2131  O  O   . LEU A  1 260 ? -1.036  -19.040 41.095  1.00 17.87 ? 259 LEU A O   1 
ATOM   2132  C  CB  . LEU A  1 260 ? -2.200  -21.088 39.219  1.00 16.75 ? 259 LEU A CB  1 
ATOM   2133  C  CG  . LEU A  1 260 ? -3.585  -21.366 39.788  1.00 17.85 ? 259 LEU A CG  1 
ATOM   2134  C  CD1 . LEU A  1 260 ? -4.141  -20.185 40.563  1.00 18.26 ? 259 LEU A CD1 1 
ATOM   2135  C  CD2 . LEU A  1 260 ? -4.523  -21.699 38.631  1.00 18.95 ? 259 LEU A CD2 1 
ATOM   2136  N  N   . ARG A  1 261 ? -1.189  -20.762 42.516  1.00 15.65 ? 260 ARG A N   1 
ATOM   2137  C  CA  . ARG A  1 261 ? -1.118  -19.908 43.710  1.00 16.16 ? 260 ARG A CA  1 
ATOM   2138  C  C   . ARG A  1 261 ? 0.308   -19.696 44.215  1.00 16.44 ? 260 ARG A C   1 
ATOM   2139  O  O   . ARG A  1 261 ? 0.510   -19.028 45.254  1.00 16.58 ? 260 ARG A O   1 
ATOM   2140  C  CB  . ARG A  1 261 ? -1.973  -20.496 44.837  1.00 16.35 ? 260 ARG A CB  1 
ATOM   2141  C  CG  . ARG A  1 261 ? -3.458  -20.570 44.487  1.00 16.75 ? 260 ARG A CG  1 
ATOM   2142  C  CD  . ARG A  1 261 ? -4.358  -20.672 45.694  1.00 17.53 ? 260 ARG A CD  1 
ATOM   2143  N  NE  . ARG A  1 261 ? -4.192  -21.944 46.388  1.00 17.98 ? 260 ARG A NE  1 
ATOM   2144  C  CZ  . ARG A  1 261 ? -4.803  -22.256 47.524  1.00 18.78 ? 260 ARG A CZ  1 
ATOM   2145  N  NH1 . ARG A  1 261 ? -5.652  -21.409 48.093  1.00 19.90 ? 260 ARG A NH1 1 
ATOM   2146  N  NH2 . ARG A  1 261 ? -4.556  -23.421 48.118  1.00 19.53 ? 260 ARG A NH2 1 
ATOM   2147  N  N   . ASP A  1 262 ? 1.271   -20.261 43.509  1.00 15.48 ? 261 ASP A N   1 
ATOM   2148  C  CA  . ASP A  1 262 ? 2.662   -20.286 43.958  1.00 15.94 ? 261 ASP A CA  1 
ATOM   2149  C  C   . ASP A  1 262 ? 3.630   -19.558 43.058  1.00 15.33 ? 261 ASP A C   1 
ATOM   2150  O  O   . ASP A  1 262 ? 4.858   -19.817 43.119  1.00 15.29 ? 261 ASP A O   1 
ATOM   2151  C  CB  . ASP A  1 262 ? 3.131   -21.740 44.123  1.00 16.68 ? 261 ASP A CB  1 
ATOM   2152  C  CG  . ASP A  1 262 ? 2.312   -22.514 45.137  1.00 17.01 ? 261 ASP A CG  1 
ATOM   2153  O  OD1 . ASP A  1 262 ? 2.064   -22.003 46.253  1.00 17.36 ? 261 ASP A OD1 1 
ATOM   2154  O  OD2 . ASP A  1 262 ? 1.924   -23.665 44.806  1.00 18.69 ? 261 ASP A OD2 1 
ATOM   2155  N  N   . TYR A  1 263 ? 3.132   -18.630 42.233  1.00 15.42 ? 262 TYR A N   1 
ATOM   2156  C  CA  . TYR A  1 263 ? 4.014   -17.966 41.282  1.00 15.63 ? 262 TYR A CA  1 
ATOM   2157  C  C   . TYR A  1 263 ? 5.128   -17.135 41.934  1.00 16.53 ? 262 TYR A C   1 
ATOM   2158  O  O   . TYR A  1 263 ? 6.237   -17.084 41.392  1.00 16.36 ? 262 TYR A O   1 
ATOM   2159  C  CB  . TYR A  1 263 ? 3.250   -17.131 40.241  1.00 15.68 ? 262 TYR A CB  1 
ATOM   2160  C  CG  . TYR A  1 263 ? 2.371   -17.932 39.272  1.00 14.99 ? 262 TYR A CG  1 
ATOM   2161  C  CD1 . TYR A  1 263 ? 2.736   -19.210 38.823  1.00 16.17 ? 262 TYR A CD1 1 
ATOM   2162  C  CD2 . TYR A  1 263 ? 1.169   -17.430 38.843  1.00 15.41 ? 262 TYR A CD2 1 
ATOM   2163  C  CE1 . TYR A  1 263 ? 1.911   -19.958 37.964  1.00 16.30 ? 262 TYR A CE1 1 
ATOM   2164  C  CE2 . TYR A  1 263 ? 0.348   -18.156 37.984  1.00 15.12 ? 262 TYR A CE2 1 
ATOM   2165  C  CZ  . TYR A  1 263 ? 0.722   -19.412 37.535  1.00 15.52 ? 262 TYR A CZ  1 
ATOM   2166  O  OH  . TYR A  1 263 ? -0.106  -20.132 36.693  1.00 15.45 ? 262 TYR A OH  1 
ATOM   2167  N  N   . ARG A  1 264 ? 4.842   -16.461 43.043  1.00 16.36 ? 263 ARG A N   1 
ATOM   2168  C  CA  . ARG A  1 264 ? 5.889   -15.676 43.681  1.00 17.93 ? 263 ARG A CA  1 
ATOM   2169  C  C   . ARG A  1 264 ? 7.065   -16.582 44.094  1.00 17.84 ? 263 ARG A C   1 
ATOM   2170  O  O   . ARG A  1 264 ? 8.211   -16.255 43.792  1.00 17.45 ? 263 ARG A O   1 
ATOM   2171  C  CB  . ARG A  1 264 ? 5.354   -14.871 44.857  1.00 19.06 ? 263 ARG A CB  1 
ATOM   2172  C  CG  . ARG A  1 264 ? 6.316   -13.780 45.343  1.00 21.24 ? 263 ARG A CG  1 
ATOM   2173  C  CD  . ARG A  1 264 ? 5.693   -13.022 46.514  1.00 23.35 ? 263 ARG A CD  1 
ATOM   2174  N  NE  . ARG A  1 264 ? 6.359   -11.774 46.905  1.00 26.77 ? 263 ARG A NE  1 
ATOM   2175  C  CZ  . ARG A  1 264 ? 7.375   -11.670 47.766  1.00 29.66 ? 263 ARG A CZ  1 
ATOM   2176  N  NH1 . ARG A  1 264 ? 7.926   -12.748 48.320  1.00 30.65 ? 263 ARG A NH1 1 
ATOM   2177  N  NH2 . ARG A  1 264 ? 7.867   -10.462 48.054  1.00 28.82 ? 263 ARG A NH2 1 
ATOM   2178  N  N   . LYS A  1 265 ? 6.773   -17.725 44.715  1.00 17.30 ? 264 LYS A N   1 
ATOM   2179  C  CA  . LYS A  1 265 ? 7.799   -18.718 45.089  1.00 18.97 ? 264 LYS A CA  1 
ATOM   2180  C  C   . LYS A  1 265 ? 8.528   -19.243 43.865  1.00 18.13 ? 264 LYS A C   1 
ATOM   2181  O  O   . LYS A  1 265 ? 9.733   -19.439 43.901  1.00 18.31 ? 264 LYS A O   1 
ATOM   2182  C  CB  . LYS A  1 265 ? 7.202   -19.972 45.776  1.00 19.80 ? 264 LYS A CB  1 
ATOM   2183  C  CG  . LYS A  1 265 ? 6.493   -19.753 47.065  1.00 21.79 ? 264 LYS A CG  1 
ATOM   2184  C  CD  . LYS A  1 265 ? 6.336   -21.050 47.864  1.00 21.00 ? 264 LYS A CD  1 
ATOM   2185  C  CE  . LYS A  1 265 ? 5.446   -22.085 47.212  1.00 20.93 ? 264 LYS A CE  1 
ATOM   2186  N  NZ  . LYS A  1 265 ? 5.063   -23.085 48.247  1.00 20.19 ? 264 LYS A NZ  1 
ATOM   2187  N  N   . PHE A  1 266 ? 7.773   -19.569 42.821  1.00 17.83 ? 265 PHE A N   1 
ATOM   2188  C  CA  . PHE A  1 266 ? 8.320   -20.099 41.567  1.00 17.94 ? 265 PHE A CA  1 
ATOM   2189  C  C   . PHE A  1 266 ? 9.359   -19.146 40.989  1.00 18.37 ? 265 PHE A C   1 
ATOM   2190  O  O   . PHE A  1 266 ? 10.480  -19.554 40.673  1.00 18.49 ? 265 PHE A O   1 
ATOM   2191  C  CB  . PHE A  1 266 ? 7.182   -20.333 40.581  1.00 18.52 ? 265 PHE A CB  1 
ATOM   2192  C  CG  . PHE A  1 266 ? 7.626   -20.789 39.213  1.00 18.37 ? 265 PHE A CG  1 
ATOM   2193  C  CD1 . PHE A  1 266 ? 8.008   -22.103 38.994  1.00 18.99 ? 265 PHE A CD1 1 
ATOM   2194  C  CD2 . PHE A  1 266 ? 7.613   -19.908 38.140  1.00 18.89 ? 265 PHE A CD2 1 
ATOM   2195  C  CE1 . PHE A  1 266 ? 8.374   -22.532 37.719  1.00 19.76 ? 265 PHE A CE1 1 
ATOM   2196  C  CE2 . PHE A  1 266 ? 7.989   -20.326 36.869  1.00 18.88 ? 265 PHE A CE2 1 
ATOM   2197  C  CZ  . PHE A  1 266 ? 8.377   -21.644 36.667  1.00 18.96 ? 265 PHE A CZ  1 
ATOM   2198  N  N   . PHE A  1 267 ? 9.004   -17.874 40.903  1.00 17.40 ? 266 PHE A N   1 
ATOM   2199  C  CA  . PHE A  1 267 ? 9.932   -16.887 40.337  1.00 18.40 ? 266 PHE A CA  1 
ATOM   2200  C  C   . PHE A  1 267 ? 11.148  -16.666 41.215  1.00 20.30 ? 266 PHE A C   1 
ATOM   2201  O  O   . PHE A  1 267 ? 12.279  -16.553 40.680  1.00 21.16 ? 266 PHE A O   1 
ATOM   2202  C  CB  . PHE A  1 267 ? 9.193   -15.590 40.024  1.00 18.14 ? 266 PHE A CB  1 
ATOM   2203  C  CG  . PHE A  1 267 ? 8.359   -15.666 38.758  1.00 18.62 ? 266 PHE A CG  1 
ATOM   2204  C  CD1 . PHE A  1 267 ? 8.970   -15.851 37.517  1.00 19.20 ? 266 PHE A CD1 1 
ATOM   2205  C  CD2 . PHE A  1 267 ? 6.992   -15.513 38.795  1.00 18.02 ? 266 PHE A CD2 1 
ATOM   2206  C  CE1 . PHE A  1 267 ? 8.211   -15.904 36.354  1.00 19.92 ? 266 PHE A CE1 1 
ATOM   2207  C  CE2 . PHE A  1 267 ? 6.230   -15.533 37.637  1.00 18.37 ? 266 PHE A CE2 1 
ATOM   2208  C  CZ  . PHE A  1 267 ? 6.832   -15.725 36.415  1.00 19.23 ? 266 PHE A CZ  1 
ATOM   2209  N  N   . GLN A  1 268 ? 10.959  -16.684 42.539  1.00 20.62 ? 267 GLN A N   1 
ATOM   2210  C  CA  . GLN A  1 268 ? 12.099  -16.663 43.460  1.00 22.07 ? 267 GLN A CA  1 
ATOM   2211  C  C   . GLN A  1 268 ? 13.004  -17.873 43.266  1.00 21.88 ? 267 GLN A C   1 
ATOM   2212  O  O   . GLN A  1 268 ? 14.227  -17.732 43.139  1.00 22.02 ? 267 GLN A O   1 
ATOM   2213  C  CB  . GLN A  1 268 ? 11.663  -16.652 44.931  1.00 22.81 ? 267 GLN A CB  1 
ATOM   2214  C  CG  . GLN A  1 268 ? 10.977  -15.379 45.380  1.00 24.85 ? 267 GLN A CG  1 
ATOM   2215  C  CD  . GLN A  1 268 ? 10.521  -15.467 46.837  1.00 27.94 ? 267 GLN A CD  1 
ATOM   2216  O  OE1 . GLN A  1 268 ? 9.919   -16.461 47.272  1.00 27.41 ? 267 GLN A OE1 1 
ATOM   2217  N  NE2 . GLN A  1 268 ? 10.856  -14.452 47.608  1.00 30.29 ? 267 GLN A NE2 1 
ATOM   2218  N  N   . ASP A  1 269 ? 12.398  -19.054 43.158  1.00 20.84 ? 268 ASP A N   1 
ATOM   2219  C  CA  . ASP A  1 269 ? 13.162  -20.297 43.130  1.00 21.93 ? 268 ASP A CA  1 
ATOM   2220  C  C   . ASP A  1 269 ? 13.879  -20.589 41.786  1.00 23.72 ? 268 ASP A C   1 
ATOM   2221  O  O   . ASP A  1 269 ? 14.857  -21.340 41.754  1.00 24.24 ? 268 ASP A O   1 
ATOM   2222  C  CB  . ASP A  1 269 ? 12.285  -21.478 43.502  1.00 21.20 ? 268 ASP A CB  1 
ATOM   2223  C  CG  . ASP A  1 269 ? 11.794  -21.421 44.954  1.00 21.67 ? 268 ASP A CG  1 
ATOM   2224  O  OD1 . ASP A  1 269 ? 12.288  -20.592 45.736  1.00 20.16 ? 268 ASP A OD1 1 
ATOM   2225  O  OD2 . ASP A  1 269 ? 10.902  -22.218 45.317  1.00 20.14 ? 268 ASP A OD2 1 
ATOM   2226  N  N   . ILE A  1 270 ? 13.392  -20.039 40.680  1.00 24.86 ? 269 ILE A N   1 
ATOM   2227  C  CA  . ILE A  1 270 ? 14.101  -20.175 39.381  1.00 26.72 ? 269 ILE A CA  1 
ATOM   2228  C  C   . ILE A  1 270 ? 15.133  -19.068 39.162  1.00 28.81 ? 269 ILE A C   1 
ATOM   2229  O  O   . ILE A  1 270 ? 15.824  -19.077 38.139  1.00 31.18 ? 269 ILE A O   1 
ATOM   2230  C  CB  . ILE A  1 270 ? 13.150  -20.241 38.167  1.00 25.08 ? 269 ILE A CB  1 
ATOM   2231  C  CG1 . ILE A  1 270 ? 12.440  -18.905 37.917  1.00 23.58 ? 269 ILE A CG1 1 
ATOM   2232  C  CG2 . ILE A  1 270 ? 12.158  -21.391 38.305  1.00 26.34 ? 269 ILE A CG2 1 
ATOM   2233  C  CD1 . ILE A  1 270 ? 11.482  -18.920 36.744  1.00 23.20 ? 269 ILE A CD1 1 
ATOM   2234  N  N   . GLY A  1 271 ? 15.184  -18.105 40.079  1.00 28.54 ? 270 GLY A N   1 
ATOM   2235  C  CA  . GLY A  1 271 ? 16.118  -16.999 40.000  1.00 30.32 ? 270 GLY A CA  1 
ATOM   2236  C  C   . GLY A  1 271 ? 15.698  -15.908 39.029  1.00 29.69 ? 270 GLY A C   1 
ATOM   2237  O  O   . GLY A  1 271 ? 16.541  -15.335 38.349  1.00 29.29 ? 270 GLY A O   1 
ATOM   2238  N  N   . PHE A  1 272 ? 14.395  -15.620 38.945  1.00 25.71 ? 271 PHE A N   1 
ATOM   2239  C  CA  . PHE A  1 272 ? 13.900  -14.629 38.012  1.00 23.95 ? 271 PHE A CA  1 
ATOM   2240  C  C   . PHE A  1 272 ? 12.788  -13.794 38.642  1.00 24.05 ? 271 PHE A C   1 
ATOM   2241  O  O   . PHE A  1 272 ? 11.612  -13.915 38.278  1.00 21.00 ? 271 PHE A O   1 
ATOM   2242  C  CB  . PHE A  1 272 ? 13.417  -15.295 36.700  1.00 24.12 ? 271 PHE A CB  1 
ATOM   2243  C  CG  . PHE A  1 272 ? 12.986  -14.312 35.641  1.00 23.83 ? 271 PHE A CG  1 
ATOM   2244  C  CD1 . PHE A  1 272 ? 13.850  -13.289 35.250  1.00 24.83 ? 271 PHE A CD1 1 
ATOM   2245  C  CD2 . PHE A  1 272 ? 11.743  -14.402 35.032  1.00 22.46 ? 271 PHE A CD2 1 
ATOM   2246  C  CE1 . PHE A  1 272 ? 13.467  -12.375 34.267  1.00 24.49 ? 271 PHE A CE1 1 
ATOM   2247  C  CE2 . PHE A  1 272 ? 11.353  -13.471 34.068  1.00 23.25 ? 271 PHE A CE2 1 
ATOM   2248  C  CZ  . PHE A  1 272 ? 12.213  -12.455 33.699  1.00 22.92 ? 271 PHE A CZ  1 
ATOM   2249  N  N   . GLU A  1 273 ? 13.178  -12.956 39.591  1.00 25.39 ? 272 GLU A N   1 
ATOM   2250  C  CA  . GLU A  1 273 ? 12.216  -12.180 40.351  1.00 27.01 ? 272 GLU A CA  1 
ATOM   2251  C  C   . GLU A  1 273 ? 11.452  -11.172 39.491  1.00 24.32 ? 272 GLU A C   1 
ATOM   2252  O  O   . GLU A  1 273 ? 10.291  -10.917 39.771  1.00 22.91 ? 272 GLU A O   1 
ATOM   2253  C  CB  . GLU A  1 273 ? 12.893  -11.544 41.574  1.00 32.92 ? 272 GLU A CB  1 
ATOM   2254  C  CG  . GLU A  1 273 ? 13.241  -12.622 42.623  1.00 40.37 ? 272 GLU A CG  1 
ATOM   2255  C  CD  . GLU A  1 273 ? 13.997  -12.104 43.847  1.00 49.71 ? 272 GLU A CD  1 
ATOM   2256  O  OE1 . GLU A  1 273 ? 14.298  -10.884 43.931  1.00 54.12 ? 272 GLU A OE1 1 
ATOM   2257  O  OE2 . GLU A  1 273 ? 14.306  -12.938 44.734  1.00 56.54 ? 272 GLU A OE2 1 
ATOM   2258  N  N   . ASP A  1 274 ? 12.049  -10.676 38.403  1.00 24.25 ? 273 ASP A N   1 
ATOM   2259  C  CA  . ASP A  1 274 ? 11.329  -9.776  37.474  1.00 23.58 ? 273 ASP A CA  1 
ATOM   2260  C  C   . ASP A  1 274 ? 10.069  -10.403 36.897  1.00 21.96 ? 273 ASP A C   1 
ATOM   2261  O  O   . ASP A  1 274 ? 9.114   -9.706  36.599  1.00 20.66 ? 273 ASP A O   1 
ATOM   2262  C  CB  . ASP A  1 274 ? 12.194  -9.358  36.291  1.00 25.96 ? 273 ASP A CB  1 
ATOM   2263  C  CG  . ASP A  1 274 ? 13.267  -8.324  36.648  1.00 28.87 ? 273 ASP A CG  1 
ATOM   2264  O  OD1 . ASP A  1 274 ? 13.220  -7.731  37.736  1.00 31.26 ? 273 ASP A OD1 1 
ATOM   2265  O  OD2 . ASP A  1 274 ? 14.149  -8.110  35.788  1.00 31.99 ? 273 ASP A OD2 1 
ATOM   2266  N  N   . GLY A  1 275 ? 10.067  -11.724 36.725  1.00 20.14 ? 274 GLY A N   1 
ATOM   2267  C  CA  . GLY A  1 275 ? 8.884   -12.390 36.224  1.00 19.65 ? 274 GLY A CA  1 
ATOM   2268  C  C   . GLY A  1 275 ? 7.671   -12.238 37.110  1.00 18.97 ? 274 GLY A C   1 
ATOM   2269  O  O   . GLY A  1 275 ? 6.555   -12.155 36.600  1.00 18.59 ? 274 GLY A O   1 
ATOM   2270  N  N   . TRP A  1 276 ? 7.883   -12.186 38.427  1.00 18.18 ? 275 TRP A N   1 
ATOM   2271  C  CA  . TRP A  1 276 ? 6.793   -11.955 39.381  1.00 18.92 ? 275 TRP A CA  1 
ATOM   2272  C  C   . TRP A  1 276 ? 6.234   -10.558 39.190  1.00 18.20 ? 275 TRP A C   1 
ATOM   2273  O  O   . TRP A  1 276 ? 5.024   -10.367 39.193  1.00 17.12 ? 275 TRP A O   1 
ATOM   2274  C  CB  . TRP A  1 276 ? 7.263   -12.189 40.847  1.00 19.44 ? 275 TRP A CB  1 
ATOM   2275  C  CG  . TRP A  1 276 ? 6.308   -11.764 41.880  1.00 20.45 ? 275 TRP A CG  1 
ATOM   2276  C  CD1 . TRP A  1 276 ? 6.497   -10.777 42.835  1.00 21.66 ? 275 TRP A CD1 1 
ATOM   2277  C  CD2 . TRP A  1 276 ? 4.983   -12.279 42.081  1.00 19.93 ? 275 TRP A CD2 1 
ATOM   2278  N  NE1 . TRP A  1 276 ? 5.362   -10.683 43.614  1.00 21.13 ? 275 TRP A NE1 1 
ATOM   2279  C  CE2 . TRP A  1 276 ? 4.429   -11.589 43.175  1.00 21.66 ? 275 TRP A CE2 1 
ATOM   2280  C  CE3 . TRP A  1 276 ? 4.221   -13.268 41.449  1.00 20.64 ? 275 TRP A CE3 1 
ATOM   2281  C  CZ2 . TRP A  1 276 ? 3.118   -11.855 43.657  1.00 22.42 ? 275 TRP A CZ2 1 
ATOM   2282  C  CZ3 . TRP A  1 276 ? 2.914   -13.538 41.929  1.00 21.71 ? 275 TRP A CZ3 1 
ATOM   2283  C  CH2 . TRP A  1 276 ? 2.392   -12.831 43.029  1.00 21.70 ? 275 TRP A CH2 1 
ATOM   2284  N  N   . LEU A  1 277 ? 7.127   -9.587  39.006  1.00 18.46 ? 276 LEU A N   1 
ATOM   2285  C  CA  . LEU A  1 277 ? 6.705   -8.206  38.759  1.00 19.01 ? 276 LEU A CA  1 
ATOM   2286  C  C   . LEU A  1 277 ? 5.919   -8.108  37.433  1.00 18.64 ? 276 LEU A C   1 
ATOM   2287  O  O   . LEU A  1 277 ? 4.873   -7.479  37.391  1.00 18.90 ? 276 LEU A O   1 
ATOM   2288  C  CB  . LEU A  1 277 ? 7.899   -7.260  38.772  1.00 20.00 ? 276 LEU A CB  1 
ATOM   2289  C  CG  . LEU A  1 277 ? 8.779   -7.267  40.031  1.00 20.94 ? 276 LEU A CG  1 
ATOM   2290  C  CD1 . LEU A  1 277 ? 9.964   -6.316  39.878  1.00 21.98 ? 276 LEU A CD1 1 
ATOM   2291  C  CD2 . LEU A  1 277 ? 7.973   -6.920  41.273  1.00 21.79 ? 276 LEU A CD2 1 
ATOM   2292  N  N   . MET A  1 278 ? 6.373   -8.815  36.405  1.00 18.80 ? 277 MET A N   1 
ATOM   2293  C  CA  . MET A  1 278 ? 5.627   -8.896  35.122  1.00 18.93 ? 277 MET A CA  1 
ATOM   2294  C  C   . MET A  1 278 ? 4.250   -9.546  35.278  1.00 18.60 ? 277 MET A C   1 
ATOM   2295  O  O   . MET A  1 278 ? 3.265   -9.064  34.718  1.00 18.27 ? 277 MET A O   1 
ATOM   2296  C  CB  . MET A  1 278 ? 6.408   -9.690  34.098  1.00 20.63 ? 277 MET A CB  1 
ATOM   2297  C  CG  . MET A  1 278 ? 7.704   -9.040  33.634  1.00 22.46 ? 277 MET A CG  1 
ATOM   2298  S  SD  . MET A  1 278 ? 8.575   -10.238 32.589  1.00 27.06 ? 277 MET A SD  1 
ATOM   2299  C  CE  . MET A  1 278 ? 10.063  -9.333  32.231  1.00 28.54 ? 277 MET A CE  1 
ATOM   2300  N  N   . ARG A  1 279 ? 4.181   -10.615 36.052  1.00 17.38 ? 278 ARG A N   1 
ATOM   2301  C  CA  . ARG A  1 279 ? 2.896   -11.258 36.310  1.00 17.59 ? 278 ARG A CA  1 
ATOM   2302  C  C   . ARG A  1 279 ? 1.952   -10.323 37.060  1.00 18.73 ? 278 ARG A C   1 
ATOM   2303  O  O   . ARG A  1 279 ? 0.771   -10.201 36.690  1.00 18.43 ? 278 ARG A O   1 
ATOM   2304  C  CB  . ARG A  1 279 ? 3.086   -12.577 37.048  1.00 17.75 ? 278 ARG A CB  1 
ATOM   2305  C  CG  . ARG A  1 279 ? 1.783   -13.321 37.338  1.00 17.68 ? 278 ARG A CG  1 
ATOM   2306  C  CD  . ARG A  1 279 ? 1.062   -13.735 36.065  1.00 17.16 ? 278 ARG A CD  1 
ATOM   2307  N  NE  . ARG A  1 279 ? -0.116  -14.575 36.350  1.00 17.37 ? 278 ARG A NE  1 
ATOM   2308  C  CZ  . ARG A  1 279 ? -0.820  -15.239 35.424  1.00 18.58 ? 278 ARG A CZ  1 
ATOM   2309  N  NH1 . ARG A  1 279 ? -0.461  -15.214 34.136  1.00 18.74 ? 278 ARG A NH1 1 
ATOM   2310  N  NH2 . ARG A  1 279 ? -1.860  -15.986 35.773  1.00 18.41 ? 278 ARG A NH2 1 
ATOM   2311  N  N   . GLN A  1 280 ? 2.452   -9.638  38.095  1.00 19.70 ? 279 GLN A N   1 
ATOM   2312  C  CA  . GLN A  1 280 ? 1.641   -8.652  38.789  1.00 21.19 ? 279 GLN A CA  1 
ATOM   2313  C  C   . GLN A  1 280 ? 1.161   -7.552  37.847  1.00 21.76 ? 279 GLN A C   1 
ATOM   2314  O  O   . GLN A  1 280 ? 0.036   -7.105  37.990  1.00 21.81 ? 279 GLN A O   1 
ATOM   2315  C  CB  . GLN A  1 280 ? 2.404   -7.979  39.929  1.00 23.38 ? 279 GLN A CB  1 
ATOM   2316  C  CG  . GLN A  1 280 ? 2.688   -8.899  41.083  1.00 24.90 ? 279 GLN A CG  1 
ATOM   2317  C  CD  . GLN A  1 280 ? 3.336   -8.144  42.221  1.00 29.23 ? 279 GLN A CD  1 
ATOM   2318  O  OE1 . GLN A  1 280 ? 4.338   -7.439  42.032  1.00 32.83 ? 279 GLN A OE1 1 
ATOM   2319  N  NE2 . GLN A  1 280 ? 2.722   -8.210  43.380  1.00 29.83 ? 279 GLN A NE2 1 
ATOM   2320  N  N   . ASP A  1 281 ? 2.027   -7.105  36.934  1.00 21.50 ? 280 ASP A N   1 
ATOM   2321  C  CA  . ASP A  1 281 ? 1.691   -6.042  35.991  1.00 22.20 ? 280 ASP A CA  1 
ATOM   2322  C  C   . ASP A  1 281 ? 0.552   -6.479  35.046  1.00 22.43 ? 280 ASP A C   1 
ATOM   2323  O  O   . ASP A  1 281 ? -0.184  -5.636  34.541  1.00 21.96 ? 280 ASP A O   1 
ATOM   2324  C  CB  . ASP A  1 281 ? 2.866   -5.682  35.050  1.00 23.11 ? 280 ASP A CB  1 
ATOM   2325  C  CG  . ASP A  1 281 ? 4.071   -5.027  35.733  1.00 25.22 ? 280 ASP A CG  1 
ATOM   2326  O  OD1 . ASP A  1 281 ? 3.967   -4.510  36.873  1.00 25.73 ? 280 ASP A OD1 1 
ATOM   2327  O  OD2 . ASP A  1 281 ? 5.169   -5.049  35.071  1.00 24.92 ? 280 ASP A OD2 1 
ATOM   2328  N  N   . THR A  1 282 ? 0.468   -7.770  34.735  1.00 18.89 ? 281 THR A N   1 
ATOM   2329  C  CA  . THR A  1 282 ? -0.356  -8.227  33.623  1.00 19.04 ? 281 THR A CA  1 
ATOM   2330  C  C   . THR A  1 282 ? -1.552  -9.123  33.984  1.00 19.63 ? 281 THR A C   1 
ATOM   2331  O  O   . THR A  1 282 ? -2.484  -9.246  33.179  1.00 19.42 ? 281 THR A O   1 
ATOM   2332  C  CB  . THR A  1 282 ? 0.492   -8.974  32.576  1.00 18.19 ? 281 THR A CB  1 
ATOM   2333  O  OG1 . THR A  1 282 ? 1.088   -10.151 33.161  1.00 18.26 ? 281 THR A OG1 1 
ATOM   2334  C  CG2 . THR A  1 282 ? 1.583   -8.094  32.045  1.00 18.50 ? 281 THR A CG2 1 
ATOM   2335  N  N   . GLU A  1 283 ? -1.554  -9.710  35.187  1.00 20.40 ? 282 GLU A N   1 
ATOM   2336  C  CA  . GLU A  1 283 ? -2.587  -10.698 35.566  1.00 21.03 ? 282 GLU A CA  1 
ATOM   2337  C  C   . GLU A  1 283 ? -4.005  -10.134 35.588  1.00 20.85 ? 282 GLU A C   1 
ATOM   2338  O  O   . GLU A  1 283 ? -4.968  -10.886 35.434  1.00 21.61 ? 282 GLU A O   1 
ATOM   2339  C  CB  . GLU A  1 283 ? -2.268  -11.341 36.929  1.00 23.30 ? 282 GLU A CB  1 
ATOM   2340  C  CG  . GLU A  1 283 ? -2.318  -10.364 38.100  1.00 27.70 ? 282 GLU A CG  1 
ATOM   2341  C  CD  . GLU A  1 283 ? -1.931  -10.982 39.438  1.00 33.77 ? 282 GLU A CD  1 
ATOM   2342  O  OE1 . GLU A  1 283 ? -1.627  -12.202 39.492  1.00 39.25 ? 282 GLU A OE1 1 
ATOM   2343  O  OE2 . GLU A  1 283 ? -1.931  -10.231 40.437  1.00 37.54 ? 282 GLU A OE2 1 
ATOM   2344  N  N   . GLY A  1 284 ? -4.146  -8.834  35.784  1.00 19.17 ? 283 GLY A N   1 
ATOM   2345  C  CA  . GLY A  1 284 ? -5.463  -8.221  35.830  1.00 20.61 ? 283 GLY A CA  1 
ATOM   2346  C  C   . GLY A  1 284 ? -5.926  -7.563  34.538  1.00 20.36 ? 283 GLY A C   1 
ATOM   2347  O  O   . GLY A  1 284 ? -7.013  -7.001  34.509  1.00 21.21 ? 283 GLY A O   1 
ATOM   2348  N  N   . LEU A  1 285 ? -5.142  -7.649  33.461  1.00 19.40 ? 284 LEU A N   1 
ATOM   2349  C  CA  . LEU A  1 285 ? -5.463  -6.914  32.234  1.00 19.90 ? 284 LEU A CA  1 
ATOM   2350  C  C   . LEU A  1 285 ? -6.754  -7.405  31.589  1.00 20.88 ? 284 LEU A C   1 
ATOM   2351  O  O   . LEU A  1 285 ? -7.585  -6.603  31.182  1.00 21.56 ? 284 LEU A O   1 
ATOM   2352  C  CB  . LEU A  1 285 ? -4.341  -7.022  31.211  1.00 19.21 ? 284 LEU A CB  1 
ATOM   2353  C  CG  . LEU A  1 285 ? -3.021  -6.370  31.606  1.00 19.75 ? 284 LEU A CG  1 
ATOM   2354  C  CD1 . LEU A  1 285 ? -1.930  -6.723  30.607  1.00 19.16 ? 284 LEU A CD1 1 
ATOM   2355  C  CD2 . LEU A  1 285 ? -3.212  -4.874  31.753  1.00 22.25 ? 284 LEU A CD2 1 
ATOM   2356  N  N   . VAL A  1 286 ? -6.904  -8.715  31.482  1.00 21.47 ? 285 VAL A N   1 
ATOM   2357  C  CA  . VAL A  1 286 ? -8.103  -9.316  30.892  1.00 23.71 ? 285 VAL A CA  1 
ATOM   2358  C  C   . VAL A  1 286 ? -9.068  -9.680  32.013  1.00 27.39 ? 285 VAL A C   1 
ATOM   2359  O  O   . VAL A  1 286 ? -8.726  -10.417 32.920  1.00 27.43 ? 285 VAL A O   1 
ATOM   2360  C  CB  . VAL A  1 286 ? -7.722  -10.532 30.041  1.00 25.13 ? 285 VAL A CB  1 
ATOM   2361  C  CG1 . VAL A  1 286 ? -8.940  -11.351 29.628  1.00 27.79 ? 285 VAL A CG1 1 
ATOM   2362  C  CG2 . VAL A  1 286 ? -6.976  -10.062 28.809  1.00 24.82 ? 285 VAL A CG2 1 
ATOM   2363  N  N   . GLU A  1 287 ? -10.275 -9.132  31.956  1.00 29.99 ? 286 GLU A N   1 
ATOM   2364  C  CA  . GLU A  1 287 ? -11.259 -9.381  33.000  1.00 32.68 ? 286 GLU A CA  1 
ATOM   2365  C  C   . GLU A  1 287 ? -11.697 -10.848 32.924  1.00 32.58 ? 286 GLU A C   1 
ATOM   2366  O  O   . GLU A  1 287 ? -12.210 -11.333 31.899  1.00 29.68 ? 286 GLU A O   1 
ATOM   2367  C  CB  . GLU A  1 287 ? -12.439 -8.415  32.880  1.00 35.34 ? 286 GLU A CB  1 
ATOM   2368  C  CG  . GLU A  1 287 ? -13.023 -7.979  34.219  1.00 41.00 ? 286 GLU A CG  1 
ATOM   2369  C  CD  . GLU A  1 287 ? -13.746 -9.101  34.948  1.00 43.66 ? 286 GLU A CD  1 
ATOM   2370  O  OE1 . GLU A  1 287 ? -14.441 -9.903  34.289  1.00 42.36 ? 286 GLU A OE1 1 
ATOM   2371  O  OE2 . GLU A  1 287 ? -13.598 -9.196  36.182  1.00 48.32 ? 286 GLU A OE2 1 
ATOM   2372  N  N   . ALA A  1 288 ? -11.529 -11.519 34.059  1.00 32.66 ? 287 ALA A N   1 
ATOM   2373  C  CA  . ALA A  1 288 ? -11.724 -12.958 34.194  1.00 34.49 ? 287 ALA A CA  1 
ATOM   2374  C  C   . ALA A  1 288 ? -13.030 -13.510 33.618  1.00 34.58 ? 287 ALA A C   1 
ATOM   2375  O  O   . ALA A  1 288 ? -13.030 -14.561 32.961  1.00 36.70 ? 287 ALA A O   1 
ATOM   2376  C  CB  . ALA A  1 288 ? -11.593 -13.346 35.664  1.00 35.43 ? 287 ALA A CB  1 
ATOM   2377  N  N   . THR A  1 289 ? -14.136 -12.806 33.843  1.00 35.25 ? 288 THR A N   1 
ATOM   2378  C  CA  . THR A  1 289 ? -15.450 -13.341 33.475  1.00 36.97 ? 288 THR A CA  1 
ATOM   2379  C  C   . THR A  1 289 ? -16.132 -12.636 32.297  1.00 36.17 ? 288 THR A C   1 
ATOM   2380  O  O   . THR A  1 289 ? -17.070 -13.206 31.707  1.00 36.33 ? 288 THR A O   1 
ATOM   2381  C  CB  . THR A  1 289 ? -16.414 -13.302 34.693  1.00 39.96 ? 288 THR A CB  1 
ATOM   2382  O  OG1 . THR A  1 289 ? -16.575 -11.951 35.134  1.00 40.92 ? 288 THR A OG1 1 
ATOM   2383  C  CG2 . THR A  1 289 ? -15.857 -14.133 35.842  1.00 39.87 ? 288 THR A CG2 1 
ATOM   2384  N  N   . MET A  1 290 ? -15.700 -11.408 31.989  1.00 32.87 ? 289 MET A N   1 
ATOM   2385  C  CA  . MET A  1 290 ? -16.395 -10.555 31.034  1.00 32.33 ? 289 MET A CA  1 
ATOM   2386  C  C   . MET A  1 290 ? -16.242 -11.096 29.604  1.00 28.56 ? 289 MET A C   1 
ATOM   2387  O  O   . MET A  1 290 ? -15.123 -11.223 29.101  1.00 25.38 ? 289 MET A O   1 
ATOM   2388  C  CB  . MET A  1 290 ? -15.851 -9.126  31.110  1.00 32.89 ? 289 MET A CB  1 
ATOM   2389  C  CG  . MET A  1 290 ? -16.614 -8.110  30.288  1.00 36.69 ? 289 MET A CG  1 
ATOM   2390  S  SD  . MET A  1 290 ? -15.737 -6.536  30.305  1.00 39.76 ? 289 MET A SD  1 
ATOM   2391  C  CE  . MET A  1 290 ? -16.853 -5.502  29.360  1.00 39.98 ? 289 MET A CE  1 
ATOM   2392  N  N   . PRO A  1 291 ? -17.374 -11.374 28.930  1.00 26.54 ? 290 PRO A N   1 
ATOM   2393  C  CA  . PRO A  1 291 ? -17.333 -11.853 27.549  1.00 25.42 ? 290 PRO A CA  1 
ATOM   2394  C  C   . PRO A  1 291 ? -16.934 -10.730 26.590  1.00 24.06 ? 290 PRO A C   1 
ATOM   2395  O  O   . PRO A  1 291 ? -17.000 -9.563  26.954  1.00 23.27 ? 290 PRO A O   1 
ATOM   2396  C  CB  . PRO A  1 291 ? -18.778 -12.319 27.303  1.00 26.62 ? 290 PRO A CB  1 
ATOM   2397  C  CG  . PRO A  1 291 ? -19.601 -11.422 28.171  1.00 27.31 ? 290 PRO A CG  1 
ATOM   2398  C  CD  . PRO A  1 291 ? -18.755 -11.090 29.373  1.00 27.89 ? 290 PRO A CD  1 
ATOM   2399  N  N   . PRO A  1 292 ? -16.582 -11.064 25.348  1.00 22.56 ? 291 PRO A N   1 
ATOM   2400  C  CA  . PRO A  1 292 ? -16.208 -10.003 24.420  1.00 21.76 ? 291 PRO A CA  1 
ATOM   2401  C  C   . PRO A  1 292 ? -17.366 -9.097  23.986  1.00 21.99 ? 291 PRO A C   1 
ATOM   2402  O  O   . PRO A  1 292 ? -17.144 -7.981  23.565  1.00 20.81 ? 291 PRO A O   1 
ATOM   2403  C  CB  . PRO A  1 292 ? -15.641 -10.774 23.225  1.00 22.14 ? 291 PRO A CB  1 
ATOM   2404  C  CG  . PRO A  1 292 ? -16.300 -12.108 23.299  1.00 22.41 ? 291 PRO A CG  1 
ATOM   2405  C  CD  . PRO A  1 292 ? -16.387 -12.403 24.764  1.00 22.43 ? 291 PRO A CD  1 
ATOM   2406  N  N   . GLY A  1 293 ? -18.601 -9.582  24.056  1.00 22.10 ? 292 GLY A N   1 
ATOM   2407  C  CA  . GLY A  1 293 ? -19.750 -8.776  23.650  1.00 22.26 ? 292 GLY A CA  1 
ATOM   2408  C  C   . GLY A  1 293 ? -19.922 -8.632  22.146  1.00 21.86 ? 292 GLY A C   1 
ATOM   2409  O  O   . GLY A  1 293 ? -20.571 -7.691  21.667  1.00 24.01 ? 292 GLY A O   1 
ATOM   2410  N  N   . VAL A  1 294 ? -19.452 -9.627  21.395  1.00 20.32 ? 293 VAL A N   1 
ATOM   2411  C  CA  . VAL A  1 294 ? -19.691 -9.710  19.961  1.00 19.91 ? 293 VAL A CA  1 
ATOM   2412  C  C   . VAL A  1 294 ? -19.984 -11.155 19.582  1.00 19.75 ? 293 VAL A C   1 
ATOM   2413  O  O   . VAL A  1 294 ? -19.732 -12.073 20.354  1.00 18.88 ? 293 VAL A O   1 
ATOM   2414  C  CB  . VAL A  1 294 ? -18.473 -9.220  19.158  1.00 19.09 ? 293 VAL A CB  1 
ATOM   2415  C  CG1 . VAL A  1 294 ? -18.122 -7.799  19.543  1.00 19.16 ? 293 VAL A CG1 1 
ATOM   2416  C  CG2 . VAL A  1 294 ? -17.302 -10.144 19.337  1.00 18.50 ? 293 VAL A CG2 1 
ATOM   2417  N  N   . GLN A  1 295 ? -20.550 -11.349 18.400  1.00 20.04 ? 294 GLN A N   1 
ATOM   2418  C  CA  . GLN A  1 295 ? -20.759 -12.706 17.877  1.00 21.43 ? 294 GLN A CA  1 
ATOM   2419  C  C   . GLN A  1 295 ? -19.432 -13.408 17.809  1.00 20.84 ? 294 GLN A C   1 
ATOM   2420  O  O   . GLN A  1 295 ? -18.491 -12.877 17.229  1.00 19.71 ? 294 GLN A O   1 
ATOM   2421  C  CB  . GLN A  1 295 ? -21.364 -12.679 16.485  1.00 23.30 ? 294 GLN A CB  1 
ATOM   2422  C  CG  . GLN A  1 295 ? -21.631 -14.067 15.941  1.00 25.63 ? 294 GLN A CG  1 
ATOM   2423  C  CD  . GLN A  1 295 ? -22.179 -14.011 14.532  1.00 28.76 ? 294 GLN A CD  1 
ATOM   2424  O  OE1 . GLN A  1 295 ? -21.490 -14.327 13.566  1.00 30.92 ? 294 GLN A OE1 1 
ATOM   2425  N  NE2 . GLN A  1 295 ? -23.428 -13.627 14.421  1.00 31.28 ? 294 GLN A NE2 1 
ATOM   2426  N  N   . LEU A  1 296 ? -19.343 -14.570 18.450  1.00 20.95 ? 295 LEU A N   1 
ATOM   2427  C  CA  . LEU A  1 296 ? -18.060 -15.249 18.635  1.00 20.63 ? 295 LEU A CA  1 
ATOM   2428  C  C   . LEU A  1 296 ? -18.117 -16.676 18.086  1.00 21.07 ? 295 LEU A C   1 
ATOM   2429  O  O   . LEU A  1 296 ? -19.062 -17.418 18.369  1.00 22.17 ? 295 LEU A O   1 
ATOM   2430  C  CB  . LEU A  1 296 ? -17.715 -15.262 20.129  1.00 21.45 ? 295 LEU A CB  1 
ATOM   2431  C  CG  . LEU A  1 296 ? -16.484 -16.047 20.561  1.00 22.00 ? 295 LEU A CG  1 
ATOM   2432  C  CD1 . LEU A  1 296 ? -15.214 -15.370 20.063  1.00 21.85 ? 295 LEU A CD1 1 
ATOM   2433  C  CD2 . LEU A  1 296 ? -16.468 -16.145 22.069  1.00 23.76 ? 295 LEU A CD2 1 
ATOM   2434  N  N   . HIS A  1 297 ? -17.108 -17.043 17.301  1.00 20.41 ? 296 HIS A N   1 
ATOM   2435  C  CA  . HIS A  1 297 ? -16.934 -18.392 16.795  1.00 20.95 ? 296 HIS A CA  1 
ATOM   2436  C  C   . HIS A  1 297 ? -15.639 -18.899 17.411  1.00 21.67 ? 296 HIS A C   1 
ATOM   2437  O  O   . HIS A  1 297 ? -14.558 -18.430 17.070  1.00 19.95 ? 296 HIS A O   1 
ATOM   2438  C  CB  . HIS A  1 297 ? -16.833 -18.391 15.271  1.00 22.04 ? 296 HIS A CB  1 
ATOM   2439  C  CG  . HIS A  1 297 ? -18.026 -17.806 14.591  1.00 23.33 ? 296 HIS A CG  1 
ATOM   2440  N  ND1 . HIS A  1 297 ? -19.030 -18.580 14.058  1.00 24.95 ? 296 HIS A ND1 1 
ATOM   2441  C  CD2 . HIS A  1 297 ? -18.393 -16.519 14.381  1.00 23.66 ? 296 HIS A CD2 1 
ATOM   2442  C  CE1 . HIS A  1 297 ? -19.954 -17.801 13.531  1.00 25.34 ? 296 HIS A CE1 1 
ATOM   2443  N  NE2 . HIS A  1 297 ? -19.577 -16.546 13.693  1.00 24.58 ? 296 HIS A NE2 1 
ATOM   2444  N  N   . CYS A  1 298 ? -15.768 -19.853 18.317  1.00 21.63 ? 297 CYS A N   1 
ATOM   2445  C  CA  A CYS A  1 298 ? -14.632 -20.394 19.062  0.50 22.38 ? 297 CYS A CA  1 
ATOM   2446  C  CA  B CYS A  1 298 ? -14.636 -20.372 19.061  0.50 23.12 ? 297 CYS A CA  1 
ATOM   2447  C  C   . CYS A  1 298 ? -14.190 -21.708 18.480  1.00 22.55 ? 297 CYS A C   1 
ATOM   2448  O  O   . CYS A  1 298 ? -14.852 -22.732 18.664  1.00 21.85 ? 297 CYS A O   1 
ATOM   2449  C  CB  A CYS A  1 298 ? -15.029 -20.616 20.518  0.50 24.09 ? 297 CYS A CB  1 
ATOM   2450  C  CB  B CYS A  1 298 ? -15.048 -20.498 20.521  0.50 25.76 ? 297 CYS A CB  1 
ATOM   2451  S  SG  A CYS A  1 298 ? -15.047 -19.075 21.421  0.50 26.46 ? 297 CYS A SG  1 
ATOM   2452  S  SG  B CYS A  1 298 ? -13.843 -21.272 21.597  0.50 31.25 ? 297 CYS A SG  1 
ATOM   2453  N  N   . LEU A  1 299 ? -13.066 -21.687 17.773  1.00 20.59 ? 298 LEU A N   1 
ATOM   2454  C  CA  . LEU A  1 299 ? -12.550 -22.870 17.134  1.00 20.86 ? 298 LEU A CA  1 
ATOM   2455  C  C   . LEU A  1 299 ? -11.351 -23.391 17.930  1.00 20.52 ? 298 LEU A C   1 
ATOM   2456  O  O   . LEU A  1 299 ? -10.384 -22.661 18.164  1.00 19.25 ? 298 LEU A O   1 
ATOM   2457  C  CB  . LEU A  1 299 ? -12.155 -22.556 15.683  1.00 21.25 ? 298 LEU A CB  1 
ATOM   2458  C  CG  . LEU A  1 299 ? -13.292 -22.619 14.651  1.00 23.27 ? 298 LEU A CG  1 
ATOM   2459  C  CD1 . LEU A  1 299 ? -14.366 -21.585 14.939  1.00 24.31 ? 298 LEU A CD1 1 
ATOM   2460  C  CD2 . LEU A  1 299 ? -12.757 -22.417 13.244  1.00 23.37 ? 298 LEU A CD2 1 
ATOM   2461  N  N   . TYR A  1 300 ? -11.412 -24.649 18.354  1.00 20.72 ? 299 TYR A N   1 
ATOM   2462  C  CA  . TYR A  1 300 ? -10.387 -25.202 19.237  1.00 21.00 ? 299 TYR A CA  1 
ATOM   2463  C  C   . TYR A  1 300 ? -10.016 -26.624 18.791  1.00 21.32 ? 299 TYR A C   1 
ATOM   2464  O  O   . TYR A  1 300 ? -10.892 -27.416 18.436  1.00 21.91 ? 299 TYR A O   1 
ATOM   2465  C  CB  . TYR A  1 300 ? -10.843 -25.161 20.713  1.00 21.67 ? 299 TYR A CB  1 
ATOM   2466  C  CG  . TYR A  1 300 ? -12.096 -25.945 21.001  1.00 23.64 ? 299 TYR A CG  1 
ATOM   2467  C  CD1 . TYR A  1 300 ? -13.356 -25.394 20.789  1.00 25.23 ? 299 TYR A CD1 1 
ATOM   2468  C  CD2 . TYR A  1 300 ? -12.022 -27.246 21.475  1.00 24.93 ? 299 TYR A CD2 1 
ATOM   2469  C  CE1 . TYR A  1 300 ? -14.502 -26.129 21.026  1.00 26.00 ? 299 TYR A CE1 1 
ATOM   2470  C  CE2 . TYR A  1 300 ? -13.157 -27.990 21.705  1.00 26.15 ? 299 TYR A CE2 1 
ATOM   2471  C  CZ  . TYR A  1 300 ? -14.393 -27.422 21.476  1.00 27.50 ? 299 TYR A CZ  1 
ATOM   2472  O  OH  . TYR A  1 300 ? -15.523 -28.169 21.731  1.00 29.31 ? 299 TYR A OH  1 
ATOM   2473  N  N   . GLY A  1 301 ? -8.728  -26.924 18.789  1.00 20.20 ? 300 GLY A N   1 
ATOM   2474  C  CA  . GLY A  1 301 ? -8.259  -28.253 18.453  1.00 21.55 ? 300 GLY A CA  1 
ATOM   2475  C  C   . GLY A  1 301 ? -8.305  -29.230 19.619  1.00 22.79 ? 300 GLY A C   1 
ATOM   2476  O  O   . GLY A  1 301 ? -8.090  -28.851 20.791  1.00 23.01 ? 300 GLY A O   1 
ATOM   2477  N  N   . THR A  1 302 ? -8.543  -30.499 19.295  1.00 23.07 ? 301 THR A N   1 
ATOM   2478  C  CA  . THR A  1 302 ? -8.499  -31.593 20.272  1.00 24.66 ? 301 THR A CA  1 
ATOM   2479  C  C   . THR A  1 302 ? -7.746  -32.771 19.676  1.00 24.44 ? 301 THR A C   1 
ATOM   2480  O  O   . THR A  1 302 ? -7.430  -32.776 18.475  1.00 23.26 ? 301 THR A O   1 
ATOM   2481  C  CB  . THR A  1 302 ? -9.909  -32.079 20.674  1.00 26.35 ? 301 THR A CB  1 
ATOM   2482  O  OG1 . THR A  1 302 ? -10.605 -32.574 19.521  1.00 26.84 ? 301 THR A OG1 1 
ATOM   2483  C  CG2 . THR A  1 302 ? -10.687 -30.957 21.290  1.00 27.48 ? 301 THR A CG2 1 
ATOM   2484  N  N   . GLY A  1 303 ? -7.456  -33.755 20.517  1.00 25.63 ? 302 GLY A N   1 
ATOM   2485  C  CA  . GLY A  1 303 ? -6.866  -35.020 20.066  1.00 25.45 ? 302 GLY A CA  1 
ATOM   2486  C  C   . GLY A  1 303 ? -5.377  -34.948 19.839  1.00 26.06 ? 302 GLY A C   1 
ATOM   2487  O  O   . GLY A  1 303 ? -4.811  -35.858 19.251  1.00 27.34 ? 302 GLY A O   1 
ATOM   2488  N  N   . VAL A  1 304 ? -4.730  -33.874 20.294  1.00 23.73 ? 303 VAL A N   1 
ATOM   2489  C  CA  . VAL A  1 304 ? -3.281  -33.719 20.148  1.00 23.85 ? 303 VAL A CA  1 
ATOM   2490  C  C   . VAL A  1 304 ? -2.686  -33.684 21.579  1.00 23.52 ? 303 VAL A C   1 
ATOM   2491  O  O   . VAL A  1 304 ? -3.104  -32.858 22.375  1.00 22.78 ? 303 VAL A O   1 
ATOM   2492  C  CB  . VAL A  1 304 ? -2.931  -32.414 19.401  1.00 23.94 ? 303 VAL A CB  1 
ATOM   2493  C  CG1 . VAL A  1 304 ? -1.434  -32.295 19.224  1.00 23.43 ? 303 VAL A CG1 1 
ATOM   2494  C  CG2 . VAL A  1 304 ? -3.658  -32.333 18.052  1.00 24.81 ? 303 VAL A CG2 1 
ATOM   2495  N  N   . PRO A  1 305 ? -1.727  -34.579 21.915  1.00 23.58 ? 304 PRO A N   1 
ATOM   2496  C  CA  . PRO A  1 305 ? -1.142  -34.507 23.250  1.00 23.05 ? 304 PRO A CA  1 
ATOM   2497  C  C   . PRO A  1 305 ? -0.583  -33.109 23.553  1.00 21.29 ? 304 PRO A C   1 
ATOM   2498  O  O   . PRO A  1 305 ? 0.187   -32.563 22.770  1.00 20.75 ? 304 PRO A O   1 
ATOM   2499  C  CB  . PRO A  1 305 ? -0.044  -35.570 23.212  1.00 24.49 ? 304 PRO A CB  1 
ATOM   2500  C  CG  . PRO A  1 305 ? -0.485  -36.516 22.118  1.00 25.99 ? 304 PRO A CG  1 
ATOM   2501  C  CD  . PRO A  1 305 ? -1.060  -35.602 21.091  1.00 25.16 ? 304 PRO A CD  1 
ATOM   2502  N  N   . THR A  1 306 ? -1.021  -32.540 24.669  1.00 19.53 ? 305 THR A N   1 
ATOM   2503  C  CA  . THR A  1 306 ? -0.701  -31.172 25.037  1.00 18.50 ? 305 THR A CA  1 
ATOM   2504  C  C   . THR A  1 306 ? -0.090  -31.146 26.437  1.00 18.71 ? 305 THR A C   1 
ATOM   2505  O  O   . THR A  1 306 ? -0.693  -31.680 27.370  1.00 17.76 ? 305 THR A O   1 
ATOM   2506  C  CB  . THR A  1 306 ? -1.983  -30.336 25.015  1.00 18.12 ? 305 THR A CB  1 
ATOM   2507  O  OG1 . THR A  1 306 ? -2.634  -30.507 23.738  1.00 18.29 ? 305 THR A OG1 1 
ATOM   2508  C  CG2 . THR A  1 306 ? -1.668  -28.871 25.269  1.00 17.82 ? 305 THR A CG2 1 
ATOM   2509  N  N   . PRO A  1 307 ? 1.093   -30.514 26.600  1.00 19.18 ? 306 PRO A N   1 
ATOM   2510  C  CA  . PRO A  1 307 ? 1.718   -30.506 27.933  1.00 19.66 ? 306 PRO A CA  1 
ATOM   2511  C  C   . PRO A  1 307 ? 0.795   -29.948 28.991  1.00 20.09 ? 306 PRO A C   1 
ATOM   2512  O  O   . PRO A  1 307 ? 0.213   -28.879 28.785  1.00 19.34 ? 306 PRO A O   1 
ATOM   2513  C  CB  . PRO A  1 307 ? 2.947   -29.615 27.741  1.00 19.41 ? 306 PRO A CB  1 
ATOM   2514  C  CG  . PRO A  1 307 ? 3.271   -29.767 26.283  1.00 20.38 ? 306 PRO A CG  1 
ATOM   2515  C  CD  . PRO A  1 307 ? 1.930   -29.802 25.616  1.00 19.63 ? 306 PRO A CD  1 
ATOM   2516  N  N   . ASP A  1 308 ? 0.666   -30.689 30.098  1.00 20.56 ? 307 ASP A N   1 
ATOM   2517  C  CA  . ASP A  1 308 ? -0.228  -30.367 31.201  1.00 22.47 ? 307 ASP A CA  1 
ATOM   2518  C  C   . ASP A  1 308 ? 0.553   -30.070 32.510  1.00 21.91 ? 307 ASP A C   1 
ATOM   2519  O  O   . ASP A  1 308 ? 0.124   -29.249 33.308  1.00 20.95 ? 307 ASP A O   1 
ATOM   2520  C  CB  . ASP A  1 308 ? -1.192  -31.539 31.394  1.00 24.32 ? 307 ASP A CB  1 
ATOM   2521  C  CG  . ASP A  1 308 ? -1.920  -31.497 32.731  1.00 27.18 ? 307 ASP A CG  1 
ATOM   2522  O  OD1 . ASP A  1 308 ? -3.006  -30.901 32.773  1.00 27.66 ? 307 ASP A OD1 1 
ATOM   2523  O  OD2 . ASP A  1 308 ? -1.420  -32.103 33.708  1.00 27.95 ? 307 ASP A OD2 1 
ATOM   2524  N  N   . SER A  1 309 ? 1.650   -30.790 32.747  1.00 20.76 ? 308 SER A N   1 
ATOM   2525  C  CA  . SER A  1 309 ? 2.444   -30.624 33.963  1.00 21.32 ? 308 SER A CA  1 
ATOM   2526  C  C   . SER A  1 309 ? 3.814   -31.230 33.751  1.00 20.76 ? 308 SER A C   1 
ATOM   2527  O  O   . SER A  1 309 ? 4.017   -31.976 32.788  1.00 20.44 ? 308 SER A O   1 
ATOM   2528  C  CB  . SER A  1 309 ? 1.759   -31.236 35.178  1.00 22.01 ? 308 SER A CB  1 
ATOM   2529  O  OG  . SER A  1 309 ? 1.385   -32.561 34.914  1.00 24.37 ? 308 SER A OG  1 
ATOM   2530  N  N   . PHE A  1 310 ? 4.739   -30.880 34.642  1.00 19.53 ? 309 PHE A N   1 
ATOM   2531  C  CA  . PHE A  1 310 ? 6.160   -31.175 34.465  1.00 19.68 ? 309 PHE A CA  1 
ATOM   2532  C  C   . PHE A  1 310 ? 6.775   -31.717 35.750  1.00 20.97 ? 309 PHE A C   1 
ATOM   2533  O  O   . PHE A  1 310 ? 6.468   -31.225 36.852  1.00 20.46 ? 309 PHE A O   1 
ATOM   2534  C  CB  . PHE A  1 310 ? 6.887   -29.910 34.053  1.00 19.24 ? 309 PHE A CB  1 
ATOM   2535  C  CG  . PHE A  1 310 ? 6.267   -29.246 32.850  1.00 19.59 ? 309 PHE A CG  1 
ATOM   2536  C  CD1 . PHE A  1 310 ? 6.535   -29.728 31.582  1.00 20.27 ? 309 PHE A CD1 1 
ATOM   2537  C  CD2 . PHE A  1 310 ? 5.346   -28.223 32.995  1.00 19.32 ? 309 PHE A CD2 1 
ATOM   2538  C  CE1 . PHE A  1 310 ? 5.931   -29.187 30.460  1.00 20.41 ? 309 PHE A CE1 1 
ATOM   2539  C  CE2 . PHE A  1 310 ? 4.728   -27.668 31.874  1.00 19.75 ? 309 PHE A CE2 1 
ATOM   2540  C  CZ  . PHE A  1 310 ? 5.041   -28.141 30.599  1.00 20.18 ? 309 PHE A CZ  1 
ATOM   2541  N  N   . TYR A  1 311 ? 7.614   -32.729 35.607  1.00 21.72 ? 310 TYR A N   1 
ATOM   2542  C  CA  . TYR A  1 311 ? 8.325   -33.312 36.739  1.00 24.53 ? 310 TYR A CA  1 
ATOM   2543  C  C   . TYR A  1 311 ? 9.819   -33.111 36.534  1.00 24.20 ? 310 TYR A C   1 
ATOM   2544  O  O   . TYR A  1 311 ? 10.371  -33.607 35.563  1.00 23.33 ? 310 TYR A O   1 
ATOM   2545  C  CB  . TYR A  1 311 ? 8.039   -34.815 36.903  1.00 27.92 ? 310 TYR A CB  1 
ATOM   2546  C  CG  . TYR A  1 311 ? 8.830   -35.350 38.099  1.00 33.91 ? 310 TYR A CG  1 
ATOM   2547  C  CD1 . TYR A  1 311 ? 8.438   -35.063 39.398  1.00 36.49 ? 310 TYR A CD1 1 
ATOM   2548  C  CD2 . TYR A  1 311 ? 10.026  -36.062 37.926  1.00 37.87 ? 310 TYR A CD2 1 
ATOM   2549  C  CE1 . TYR A  1 311 ? 9.172   -35.489 40.498  1.00 40.59 ? 310 TYR A CE1 1 
ATOM   2550  C  CE2 . TYR A  1 311 ? 10.763  -36.506 39.026  1.00 41.92 ? 310 TYR A CE2 1 
ATOM   2551  C  CZ  . TYR A  1 311 ? 10.334  -36.214 40.306  1.00 43.66 ? 310 TYR A CZ  1 
ATOM   2552  O  OH  . TYR A  1 311 ? 11.089  -36.631 41.387  1.00 51.58 ? 310 TYR A OH  1 
ATOM   2553  N  N   . TYR A  1 312 ? 10.448  -32.397 37.456  1.00 24.19 ? 311 TYR A N   1 
ATOM   2554  C  CA  . TYR A  1 312 ? 11.876  -32.091 37.373  1.00 25.06 ? 311 TYR A CA  1 
ATOM   2555  C  C   . TYR A  1 312 ? 12.674  -32.917 38.359  1.00 28.12 ? 311 TYR A C   1 
ATOM   2556  O  O   . TYR A  1 312 ? 12.454  -32.810 39.554  1.00 28.85 ? 311 TYR A O   1 
ATOM   2557  C  CB  . TYR A  1 312 ? 12.121  -30.607 37.665  1.00 23.82 ? 311 TYR A CB  1 
ATOM   2558  C  CG  . TYR A  1 312 ? 11.759  -29.678 36.555  1.00 22.03 ? 311 TYR A CG  1 
ATOM   2559  C  CD1 . TYR A  1 312 ? 10.456  -29.182 36.414  1.00 21.24 ? 311 TYR A CD1 1 
ATOM   2560  C  CD2 . TYR A  1 312 ? 12.723  -29.198 35.691  1.00 22.37 ? 311 TYR A CD2 1 
ATOM   2561  C  CE1 . TYR A  1 312 ? 10.127  -28.287 35.404  1.00 19.98 ? 311 TYR A CE1 1 
ATOM   2562  C  CE2 . TYR A  1 312 ? 12.404  -28.297 34.689  1.00 20.99 ? 311 TYR A CE2 1 
ATOM   2563  C  CZ  . TYR A  1 312 ? 11.100  -27.845 34.552  1.00 19.81 ? 311 TYR A CZ  1 
ATOM   2564  O  OH  . TYR A  1 312 ? 10.780  -27.005 33.539  1.00 18.65 ? 311 TYR A OH  1 
ATOM   2565  N  N   . GLU A  1 313 ? 13.585  -33.741 37.859  1.00 31.72 ? 312 GLU A N   1 
ATOM   2566  C  CA  . GLU A  1 313 ? 14.510  -34.472 38.730  1.00 37.14 ? 312 GLU A CA  1 
ATOM   2567  C  C   . GLU A  1 313 ? 15.616  -33.550 39.208  1.00 35.87 ? 312 GLU A C   1 
ATOM   2568  O  O   . GLU A  1 313 ? 16.129  -33.725 40.299  1.00 39.43 ? 312 GLU A O   1 
ATOM   2569  C  CB  . GLU A  1 313 ? 15.080  -35.690 38.004  1.00 43.95 ? 312 GLU A CB  1 
ATOM   2570  C  CG  . GLU A  1 313 ? 13.981  -36.699 37.694  1.00 51.98 ? 312 GLU A CG  1 
ATOM   2571  C  CD  . GLU A  1 313 ? 14.380  -37.804 36.728  1.00 62.71 ? 312 GLU A CD  1 
ATOM   2572  O  OE1 . GLU A  1 313 ? 15.590  -38.016 36.491  1.00 66.03 ? 312 GLU A OE1 1 
ATOM   2573  O  OE2 . GLU A  1 313 ? 13.459  -38.472 36.210  1.00 70.53 ? 312 GLU A OE2 1 
ATOM   2574  N  N   . SER A  1 314 ? 15.951  -32.556 38.396  1.00 32.57 ? 313 SER A N   1 
ATOM   2575  C  CA  . SER A  1 314 ? 16.857  -31.484 38.774  1.00 32.01 ? 313 SER A CA  1 
ATOM   2576  C  C   . SER A  1 314 ? 16.269  -30.146 38.273  1.00 29.55 ? 313 SER A C   1 
ATOM   2577  O  O   . SER A  1 314 ? 16.114  -29.952 37.078  1.00 29.07 ? 313 SER A O   1 
ATOM   2578  C  CB  . SER A  1 314 ? 18.217  -31.734 38.141  1.00 34.56 ? 313 SER A CB  1 
ATOM   2579  O  OG  . SER A  1 314 ? 19.060  -30.620 38.317  1.00 36.28 ? 313 SER A OG  1 
ATOM   2580  N  N   . PHE A  1 315 ? 15.970  -29.233 39.189  1.00 28.36 ? 314 PHE A N   1 
ATOM   2581  C  CA  . PHE A  1 315 ? 15.222  -28.003 38.893  1.00 26.56 ? 314 PHE A CA  1 
ATOM   2582  C  C   . PHE A  1 315 ? 16.089  -26.796 39.238  1.00 26.50 ? 314 PHE A C   1 
ATOM   2583  O  O   . PHE A  1 315 ? 16.676  -26.799 40.308  1.00 25.71 ? 314 PHE A O   1 
ATOM   2584  C  CB  . PHE A  1 315 ? 13.978  -27.981 39.781  1.00 24.79 ? 314 PHE A CB  1 
ATOM   2585  C  CG  . PHE A  1 315 ? 13.085  -26.761 39.611  1.00 23.41 ? 314 PHE A CG  1 
ATOM   2586  C  CD1 . PHE A  1 315 ? 12.183  -26.682 38.547  1.00 22.75 ? 314 PHE A CD1 1 
ATOM   2587  C  CD2 . PHE A  1 315 ? 13.087  -25.729 40.554  1.00 23.13 ? 314 PHE A CD2 1 
ATOM   2588  C  CE1 . PHE A  1 315 ? 11.348  -25.583 38.415  1.00 21.82 ? 314 PHE A CE1 1 
ATOM   2589  C  CE2 . PHE A  1 315 ? 12.245  -24.632 40.436  1.00 21.98 ? 314 PHE A CE2 1 
ATOM   2590  C  CZ  . PHE A  1 315 ? 11.367  -24.564 39.366  1.00 21.78 ? 314 PHE A CZ  1 
ATOM   2591  N  N   . PRO A  1 316 ? 16.128  -25.744 38.415  1.00 26.30 ? 315 PRO A N   1 
ATOM   2592  C  CA  . PRO A  1 316 ? 15.377  -25.608 37.158  1.00 26.28 ? 315 PRO A CA  1 
ATOM   2593  C  C   . PRO A  1 316 ? 16.229  -25.785 35.899  1.00 27.49 ? 315 PRO A C   1 
ATOM   2594  O  O   . PRO A  1 316 ? 15.731  -25.502 34.808  1.00 28.78 ? 315 PRO A O   1 
ATOM   2595  C  CB  . PRO A  1 316 ? 14.927  -24.150 37.222  1.00 26.32 ? 315 PRO A CB  1 
ATOM   2596  C  CG  . PRO A  1 316 ? 16.114  -23.456 37.844  1.00 26.25 ? 315 PRO A CG  1 
ATOM   2597  C  CD  . PRO A  1 316 ? 16.684  -24.443 38.843  1.00 27.18 ? 315 PRO A CD  1 
ATOM   2598  N  N   . ASP A  1 317 ? 17.468  -26.254 36.016  1.00 28.49 ? 316 ASP A N   1 
ATOM   2599  C  CA  . ASP A  1 317 ? 18.399  -26.209 34.883  1.00 32.37 ? 316 ASP A CA  1 
ATOM   2600  C  C   . ASP A  1 317 ? 18.524  -27.489 34.043  1.00 33.28 ? 316 ASP A C   1 
ATOM   2601  O  O   . ASP A  1 317 ? 19.461  -27.617 33.254  1.00 34.88 ? 316 ASP A O   1 
ATOM   2602  C  CB  . ASP A  1 317 ? 19.792  -25.766 35.351  1.00 35.01 ? 316 ASP A CB  1 
ATOM   2603  C  CG  . ASP A  1 317 ? 19.842  -24.295 35.777  1.00 38.27 ? 316 ASP A CG  1 
ATOM   2604  O  OD1 . ASP A  1 317 ? 18.980  -23.475 35.375  1.00 34.08 ? 316 ASP A OD1 1 
ATOM   2605  O  OD2 . ASP A  1 317 ? 20.759  -23.967 36.555  1.00 43.00 ? 316 ASP A OD2 1 
ATOM   2606  N  N   . ARG A  1 318 ? 17.598  -28.423 34.202  1.00 33.15 ? 317 ARG A N   1 
ATOM   2607  C  CA  . ARG A  1 318 ? 17.518  -29.615 33.350  1.00 34.55 ? 317 ARG A CA  1 
ATOM   2608  C  C   . ARG A  1 318 ? 16.098  -29.798 32.831  1.00 32.10 ? 317 ARG A C   1 
ATOM   2609  O  O   . ARG A  1 318 ? 15.151  -29.417 33.503  1.00 29.30 ? 317 ARG A O   1 
ATOM   2610  C  CB  . ARG A  1 318 ? 17.926  -30.817 34.168  1.00 38.64 ? 317 ARG A CB  1 
ATOM   2611  C  CG  . ARG A  1 318 ? 19.443  -30.838 34.400  1.00 45.74 ? 317 ARG A CG  1 
ATOM   2612  C  CD  . ARG A  1 318 ? 20.227  -31.442 33.202  1.00 52.01 ? 317 ARG A CD  1 
ATOM   2613  N  NE  . ARG A  1 318 ? 21.500  -32.070 33.599  1.00 61.23 ? 317 ARG A NE  1 
ATOM   2614  C  CZ  . ARG A  1 318 ? 22.626  -31.399 33.856  1.00 66.70 ? 317 ARG A CZ  1 
ATOM   2615  N  NH1 . ARG A  1 318 ? 22.675  -30.070 33.764  1.00 69.45 ? 317 ARG A NH1 1 
ATOM   2616  N  NH2 . ARG A  1 318 ? 23.725  -32.063 34.207  1.00 70.07 ? 317 ARG A NH2 1 
ATOM   2617  N  N   . ASP A  1 319 ? 15.950  -30.374 31.641  1.00 29.81 ? 318 ASP A N   1 
ATOM   2618  C  CA  . ASP A  1 319 ? 14.629  -30.572 31.054  1.00 29.29 ? 318 ASP A CA  1 
ATOM   2619  C  C   . ASP A  1 319 ? 13.780  -31.515 31.925  1.00 27.39 ? 318 ASP A C   1 
ATOM   2620  O  O   . ASP A  1 319 ? 14.273  -32.496 32.460  1.00 27.04 ? 318 ASP A O   1 
ATOM   2621  C  CB  . ASP A  1 319 ? 14.719  -31.119 29.629  1.00 30.43 ? 318 ASP A CB  1 
ATOM   2622  C  CG  . ASP A  1 319 ? 15.230  -30.095 28.620  1.00 33.67 ? 318 ASP A CG  1 
ATOM   2623  O  OD1 . ASP A  1 319 ? 15.075  -28.855 28.812  1.00 32.59 ? 318 ASP A OD1 1 
ATOM   2624  O  OD2 . ASP A  1 319 ? 15.780  -30.550 27.596  1.00 37.13 ? 318 ASP A OD2 1 
ATOM   2625  N  N   . PRO A  1 320 ? 12.486  -31.229 32.043  1.00 24.54 ? 319 PRO A N   1 
ATOM   2626  C  CA  . PRO A  1 320 ? 11.612  -32.102 32.819  1.00 24.22 ? 319 PRO A CA  1 
ATOM   2627  C  C   . PRO A  1 320 ? 11.017  -33.268 32.028  1.00 25.77 ? 319 PRO A C   1 
ATOM   2628  O  O   . PRO A  1 320 ? 11.030  -33.266 30.804  1.00 23.60 ? 319 PRO A O   1 
ATOM   2629  C  CB  . PRO A  1 320 ? 10.485  -31.154 33.206  1.00 23.03 ? 319 PRO A CB  1 
ATOM   2630  C  CG  . PRO A  1 320 ? 10.365  -30.250 32.025  1.00 22.66 ? 319 PRO A CG  1 
ATOM   2631  C  CD  . PRO A  1 320 ? 11.768  -30.048 31.542  1.00 23.26 ? 319 PRO A CD  1 
ATOM   2632  N  N   . LYS A  1 321 ? 10.452  -34.231 32.752  1.00 26.40 ? 320 LYS A N   1 
ATOM   2633  C  CA  . LYS A  1 321 ? 9.521   -35.187 32.165  1.00 28.73 ? 320 LYS A CA  1 
ATOM   2634  C  C   . LYS A  1 321 ? 8.183   -34.473 32.003  1.00 25.24 ? 320 LYS A C   1 
ATOM   2635  O  O   . LYS A  1 321 ? 7.822   -33.667 32.838  1.00 23.60 ? 320 LYS A O   1 
ATOM   2636  C  CB  . LYS A  1 321 ? 9.314   -36.395 33.089  1.00 33.09 ? 320 LYS A CB  1 
ATOM   2637  C  CG  . LYS A  1 321 ? 10.584  -37.030 33.609  1.00 40.88 ? 320 LYS A CG  1 
ATOM   2638  C  CD  . LYS A  1 321 ? 11.580  -37.313 32.510  1.00 46.89 ? 320 LYS A CD  1 
ATOM   2639  C  CE  . LYS A  1 321 ? 12.895  -37.732 33.151  1.00 53.53 ? 320 LYS A CE  1 
ATOM   2640  N  NZ  . LYS A  1 321 ? 13.863  -38.077 32.086  1.00 57.49 ? 320 LYS A NZ  1 
ATOM   2641  N  N   . ILE A  1 322 ? 7.429   -34.827 30.976  1.00 24.01 ? 321 ILE A N   1 
ATOM   2642  C  CA  . ILE A  1 322 ? 6.192   -34.134 30.667  1.00 22.67 ? 321 ILE A CA  1 
ATOM   2643  C  C   . ILE A  1 322 ? 4.989   -35.056 30.783  1.00 22.93 ? 321 ILE A C   1 
ATOM   2644  O  O   . ILE A  1 322 ? 5.003   -36.215 30.323  1.00 22.57 ? 321 ILE A O   1 
ATOM   2645  C  CB  . ILE A  1 322 ? 6.235   -33.544 29.253  1.00 22.30 ? 321 ILE A CB  1 
ATOM   2646  C  CG1 . ILE A  1 322 ? 7.450   -32.627 29.133  1.00 22.78 ? 321 ILE A CG1 1 
ATOM   2647  C  CG2 . ILE A  1 322 ? 4.959   -32.790 28.959  1.00 22.10 ? 321 ILE A CG2 1 
ATOM   2648  C  CD1 . ILE A  1 322 ? 7.634   -32.032 27.762  1.00 24.99 ? 321 ILE A CD1 1 
ATOM   2649  N  N   . CYS A  1 323 ? 3.960   -34.538 31.443  1.00 22.25 ? 322 CYS A N   1 
ATOM   2650  C  CA  A CYS A  1 323 ? 2.671   -35.191 31.501  0.50 22.32 ? 322 CYS A CA  1 
ATOM   2651  C  CA  B CYS A  1 323 ? 2.656   -35.193 31.505  0.50 23.35 ? 322 CYS A CA  1 
ATOM   2652  C  C   . CYS A  1 323 ? 1.730   -34.462 30.524  1.00 21.57 ? 322 CYS A C   1 
ATOM   2653  O  O   . CYS A  1 323 ? 1.659   -33.234 30.531  1.00 20.41 ? 322 CYS A O   1 
ATOM   2654  C  CB  A CYS A  1 323 ? 2.158   -35.106 32.927  0.50 23.02 ? 322 CYS A CB  1 
ATOM   2655  C  CB  B CYS A  1 323 ? 2.103   -35.135 32.934  0.50 25.33 ? 322 CYS A CB  1 
ATOM   2656  S  SG  A CYS A  1 323 ? 0.749   -36.141 33.215  0.50 25.08 ? 322 CYS A SG  1 
ATOM   2657  S  SG  B CYS A  1 323 ? 2.576   -36.563 33.951  0.50 31.64 ? 322 CYS A SG  1 
ATOM   2658  N  N   . PHE A  1 324 ? 1.014   -35.212 29.693  1.00 20.60 ? 323 PHE A N   1 
ATOM   2659  C  CA  . PHE A  1 324 ? 0.211   -34.638 28.621  1.00 19.70 ? 323 PHE A CA  1 
ATOM   2660  C  C   . PHE A  1 324 ? -1.271  -34.827 28.849  1.00 20.74 ? 323 PHE A C   1 
ATOM   2661  O  O   . PHE A  1 324 ? -1.716  -35.883 29.309  1.00 20.10 ? 323 PHE A O   1 
ATOM   2662  C  CB  . PHE A  1 324 ? 0.547   -35.296 27.259  1.00 20.40 ? 323 PHE A CB  1 
ATOM   2663  C  CG  . PHE A  1 324 ? 1.925   -34.992 26.758  1.00 19.59 ? 323 PHE A CG  1 
ATOM   2664  C  CD1 . PHE A  1 324 ? 3.000   -35.759 27.152  1.00 20.42 ? 323 PHE A CD1 1 
ATOM   2665  C  CD2 . PHE A  1 324 ? 2.150   -33.920 25.910  1.00 19.42 ? 323 PHE A CD2 1 
ATOM   2666  C  CE1 . PHE A  1 324 ? 4.286   -35.481 26.695  1.00 20.14 ? 323 PHE A CE1 1 
ATOM   2667  C  CE2 . PHE A  1 324 ? 3.433   -33.619 25.460  1.00 19.61 ? 323 PHE A CE2 1 
ATOM   2668  C  CZ  . PHE A  1 324 ? 4.503   -34.424 25.838  1.00 20.00 ? 323 PHE A CZ  1 
ATOM   2669  N  N   . GLY A  1 325 ? -2.038  -33.809 28.480  1.00 20.37 ? 324 GLY A N   1 
ATOM   2670  C  CA  . GLY A  1 325 ? -3.498  -33.910 28.434  1.00 21.60 ? 324 GLY A CA  1 
ATOM   2671  C  C   . GLY A  1 325 ? -4.014  -33.618 27.036  1.00 22.31 ? 324 GLY A C   1 
ATOM   2672  O  O   . GLY A  1 325 ? -3.263  -33.650 26.071  1.00 21.81 ? 324 GLY A O   1 
ATOM   2673  N  N   . ASP A  1 326 ? -5.299  -33.296 26.933  1.00 22.45 ? 325 ASP A N   1 
ATOM   2674  C  CA  . ASP A  1 326 ? -5.916  -33.055 25.630  1.00 23.29 ? 325 ASP A CA  1 
ATOM   2675  C  C   . ASP A  1 326 ? -5.801  -31.585 25.254  1.00 21.85 ? 325 ASP A C   1 
ATOM   2676  O  O   . ASP A  1 326 ? -5.588  -30.704 26.115  1.00 21.22 ? 325 ASP A O   1 
ATOM   2677  C  CB  . ASP A  1 326 ? -7.386  -33.518 25.659  1.00 25.17 ? 325 ASP A CB  1 
ATOM   2678  C  CG  . ASP A  1 326 ? -7.951  -33.847 24.271  1.00 27.44 ? 325 ASP A CG  1 
ATOM   2679  O  OD1 . ASP A  1 326 ? -7.317  -33.585 23.229  1.00 27.39 ? 325 ASP A OD1 1 
ATOM   2680  O  OD2 . ASP A  1 326 ? -9.085  -34.361 24.239  1.00 29.01 ? 325 ASP A OD2 1 
ATOM   2681  N  N   . GLY A  1 327 ? -5.948  -31.311 23.963  1.00 21.94 ? 326 GLY A N   1 
ATOM   2682  C  CA  . GLY A  1 327 ? -5.831  -29.940 23.409  1.00 20.40 ? 326 GLY A CA  1 
ATOM   2683  C  C   . GLY A  1 327 ? -5.307  -30.014 21.990  1.00 20.31 ? 326 GLY A C   1 
ATOM   2684  O  O   . GLY A  1 327 ? -5.503  -31.018 21.281  1.00 19.94 ? 326 GLY A O   1 
ATOM   2685  N  N   . ASP A  1 328 ? -4.632  -28.954 21.569  1.00 19.19 ? 327 ASP A N   1 
ATOM   2686  C  CA  . ASP A  1 328 ? -4.129  -28.840 20.185  1.00 19.64 ? 327 ASP A CA  1 
ATOM   2687  C  C   . ASP A  1 328 ? -2.595  -28.917 20.080  1.00 19.13 ? 327 ASP A C   1 
ATOM   2688  O  O   . ASP A  1 328 ? -2.043  -28.616 19.021  1.00 19.88 ? 327 ASP A O   1 
ATOM   2689  C  CB  . ASP A  1 328 ? -4.652  -27.558 19.510  1.00 19.69 ? 327 ASP A CB  1 
ATOM   2690  C  CG  . ASP A  1 328 ? -4.016  -26.284 20.060  1.00 19.88 ? 327 ASP A CG  1 
ATOM   2691  O  OD1 . ASP A  1 328 ? -3.053  -26.363 20.860  1.00 20.41 ? 327 ASP A OD1 1 
ATOM   2692  O  OD2 . ASP A  1 328 ? -4.490  -25.163 19.685  1.00 21.74 ? 327 ASP A OD2 1 
ATOM   2693  N  N   . GLY A  1 329 ? -1.931  -29.368 21.141  1.00 19.31 ? 328 GLY A N   1 
ATOM   2694  C  CA  . GLY A  1 329 ? -0.483  -29.430 21.202  1.00 19.50 ? 328 GLY A CA  1 
ATOM   2695  C  C   . GLY A  1 329 ? 0.126   -28.319 22.024  1.00 19.62 ? 328 GLY A C   1 
ATOM   2696  O  O   . GLY A  1 329 ? 1.205   -28.476 22.575  1.00 20.73 ? 328 GLY A O   1 
ATOM   2697  N  N   . THR A  1 330 ? -0.579  -27.195 22.137  1.00 19.58 ? 329 THR A N   1 
ATOM   2698  C  CA  . THR A  1 330 ? -0.093  -26.012 22.839  1.00 20.62 ? 329 THR A CA  1 
ATOM   2699  C  C   . THR A  1 330 ? -1.144  -25.525 23.834  1.00 19.30 ? 329 THR A C   1 
ATOM   2700  O  O   . THR A  1 330 ? -0.868  -25.386 25.010  1.00 19.42 ? 329 THR A O   1 
ATOM   2701  C  CB  . THR A  1 330 ? 0.219   -24.881 21.821  1.00 21.83 ? 329 THR A CB  1 
ATOM   2702  O  OG1 . THR A  1 330 ? 1.264   -25.329 20.950  1.00 23.28 ? 329 THR A OG1 1 
ATOM   2703  C  CG2 . THR A  1 330 ? 0.644   -23.599 22.522  1.00 22.98 ? 329 THR A CG2 1 
ATOM   2704  N  N   . VAL A  1 331 ? -2.358  -25.296 23.344  1.00 18.94 ? 330 VAL A N   1 
ATOM   2705  C  CA  . VAL A  1 331 ? -3.470  -24.847 24.172  1.00 19.18 ? 330 VAL A CA  1 
ATOM   2706  C  C   . VAL A  1 331 ? -4.211  -26.040 24.774  1.00 19.46 ? 330 VAL A C   1 
ATOM   2707  O  O   . VAL A  1 331 ? -4.693  -26.907 24.065  1.00 19.59 ? 330 VAL A O   1 
ATOM   2708  C  CB  . VAL A  1 331 ? -4.443  -24.007 23.330  1.00 19.63 ? 330 VAL A CB  1 
ATOM   2709  C  CG1 . VAL A  1 331 ? -5.666  -23.609 24.126  1.00 20.89 ? 330 VAL A CG1 1 
ATOM   2710  C  CG2 . VAL A  1 331 ? -3.712  -22.789 22.788  1.00 19.41 ? 330 VAL A CG2 1 
ATOM   2711  N  N   . ASN A  1 332 ? -4.281  -26.055 26.099  1.00 19.22 ? 331 ASN A N   1 
ATOM   2712  C  CA  . ASN A  1 332 ? -4.941  -27.113 26.822  1.00 20.10 ? 331 ASN A CA  1 
ATOM   2713  C  C   . ASN A  1 332 ? -6.447  -27.015 26.526  1.00 20.55 ? 331 ASN A C   1 
ATOM   2714  O  O   . ASN A  1 332 ? -6.995  -25.910 26.417  1.00 20.03 ? 331 ASN A O   1 
ATOM   2715  C  CB  . ASN A  1 332 ? -4.643  -26.965 28.321  1.00 19.98 ? 331 ASN A CB  1 
ATOM   2716  C  CG  . ASN A  1 332 ? -3.153  -27.006 28.626  1.00 19.00 ? 331 ASN A CG  1 
ATOM   2717  O  OD1 . ASN A  1 332 ? -2.472  -25.978 28.659  1.00 18.41 ? 331 ASN A OD1 1 
ATOM   2718  N  ND2 . ASN A  1 332 ? -2.637  -28.190 28.805  1.00 19.63 ? 331 ASN A ND2 1 
ATOM   2719  N  N   . LEU A  1 333 ? -7.090  -28.154 26.403  1.00 21.01 ? 332 LEU A N   1 
ATOM   2720  C  CA  . LEU A  1 333 ? -8.521  -28.201 26.123  1.00 23.42 ? 332 LEU A CA  1 
ATOM   2721  C  C   . LEU A  1 333 ? -9.353  -27.351 27.083  1.00 24.43 ? 332 LEU A C   1 
ATOM   2722  O  O   . LEU A  1 333 ? -10.325 -26.691 26.673  1.00 25.83 ? 332 LEU A O   1 
ATOM   2723  C  CB  . LEU A  1 333 ? -9.030  -29.639 26.166  1.00 24.43 ? 332 LEU A CB  1 
ATOM   2724  C  CG  . LEU A  1 333 ? -10.506 -29.831 25.851  1.00 26.48 ? 332 LEU A CG  1 
ATOM   2725  C  CD1 . LEU A  1 333 ? -10.871 -29.199 24.516  1.00 27.12 ? 332 LEU A CD1 1 
ATOM   2726  C  CD2 . LEU A  1 333 ? -10.823 -31.322 25.868  1.00 28.32 ? 332 LEU A CD2 1 
ATOM   2727  N  N   . LYS A  1 334 ? -8.998  -27.334 28.353  1.00 24.79 ? 333 LYS A N   1 
ATOM   2728  C  CA  . LYS A  1 334 ? -9.833  -26.547 29.253  1.00 28.11 ? 333 LYS A CA  1 
ATOM   2729  C  C   . LYS A  1 334 ? -9.875  -25.046 29.004  1.00 26.03 ? 333 LYS A C   1 
ATOM   2730  O  O   . LYS A  1 334 ? -10.778 -24.416 29.432  1.00 25.66 ? 333 LYS A O   1 
ATOM   2731  C  CB  . LYS A  1 334 ? -9.529  -26.775 30.681  1.00 31.28 ? 333 LYS A CB  1 
ATOM   2732  C  CG  . LYS A  1 334 ? -8.104  -26.532 31.086  1.00 32.98 ? 333 LYS A CG  1 
ATOM   2733  C  CD  . LYS A  1 334 ? -8.007  -26.838 32.569  1.00 38.92 ? 333 LYS A CD  1 
ATOM   2734  C  CE  . LYS A  1 334 ? -7.919  -28.332 32.824  1.00 40.88 ? 333 LYS A CE  1 
ATOM   2735  N  NZ  . LYS A  1 334 ? -8.761  -28.676 33.999  1.00 47.61 ? 333 LYS A NZ  1 
ATOM   2736  N  N   A SER A  1 335 ? -9.036  -24.520 28.134  0.80 26.42 ? 334 SER A N   1 
ATOM   2737  N  N   B SER A  1 335 ? -8.802  -24.503 28.433  0.20 24.06 ? 334 SER A N   1 
ATOM   2738  C  CA  A SER A  1 335 ? -9.353  -23.172 27.569  0.80 25.64 ? 334 SER A CA  1 
ATOM   2739  C  CA  B SER A  1 335 ? -8.508  -23.082 28.474  0.20 22.58 ? 334 SER A CA  1 
ATOM   2740  C  C   A SER A  1 335 ? -10.784 -23.029 26.916  0.80 26.52 ? 334 SER A C   1 
ATOM   2741  C  C   B SER A  1 335 ? -9.119  -22.549 27.196  0.20 21.62 ? 334 SER A C   1 
ATOM   2742  O  O   A SER A  1 335 ? -11.425 -21.982 27.062  0.80 25.99 ? 334 SER A O   1 
ATOM   2743  O  O   B SER A  1 335 ? -9.377  -21.361 27.066  0.20 21.31 ? 334 SER A O   1 
ATOM   2744  C  CB  A SER A  1 335 ? -8.256  -22.728 26.621  0.80 25.24 ? 334 SER A CB  1 
ATOM   2745  C  CB  B SER A  1 335 ? -6.993  -22.867 28.613  0.20 21.80 ? 334 SER A CB  1 
ATOM   2746  O  OG  A SER A  1 335 ? -7.047  -22.474 27.337  0.80 25.06 ? 334 SER A OG  1 
ATOM   2747  O  OG  B SER A  1 335 ? -6.550  -21.635 28.073  0.20 20.54 ? 334 SER A OG  1 
ATOM   2748  N  N   A ALA A  1 336 ? -11.275 -24.053 26.210  0.80 24.77 ? 335 ALA A N   1 
ATOM   2749  N  N   B ALA A  1 336 ? -9.428  -23.484 26.296  0.20 21.48 ? 335 ALA A N   1 
ATOM   2750  C  CA  A ALA A  1 336 ? -12.598 -23.981 25.572  0.80 28.53 ? 335 ALA A CA  1 
ATOM   2751  C  CA  B ALA A  1 336 ? -10.232 -23.210 25.100  0.20 21.26 ? 335 ALA A CA  1 
ATOM   2752  C  C   A ALA A  1 336 ? -13.772 -23.758 26.531  0.80 30.35 ? 335 ALA A C   1 
ATOM   2753  C  C   B ALA A  1 336 ? -11.685 -23.009 25.502  0.20 21.39 ? 335 ALA A C   1 
ATOM   2754  O  O   A ALA A  1 336 ? -14.819 -23.253 26.124  0.80 33.13 ? 335 ALA A O   1 
ATOM   2755  O  O   B ALA A  1 336 ? -12.382 -22.200 24.888  0.20 21.11 ? 335 ALA A O   1 
ATOM   2756  C  CB  A ALA A  1 336 ? -12.857 -25.224 24.733  0.80 29.44 ? 335 ALA A CB  1 
ATOM   2757  C  CB  B ALA A  1 336 ? -10.143 -24.345 24.071  0.20 21.70 ? 335 ALA A CB  1 
ATOM   2758  N  N   A LEU A  1 337 ? -13.619 -24.136 27.793  0.80 31.39 ? 336 LEU A N   1 
ATOM   2759  N  N   B LEU A  1 337 ? -12.145 -23.737 26.526  0.20 21.58 ? 336 LEU A N   1 
ATOM   2760  C  CA  A LEU A  1 337 ? -14.704 -23.957 28.768  0.80 34.44 ? 336 LEU A CA  1 
ATOM   2761  C  CA  B LEU A  1 337 ? -13.592 -23.798 26.845  0.20 22.04 ? 336 LEU A CA  1 
ATOM   2762  C  C   A LEU A  1 337 ? -14.967 -22.472 28.988  0.80 32.40 ? 336 LEU A C   1 
ATOM   2763  C  C   B LEU A  1 337 ? -14.253 -22.648 27.636  0.20 21.87 ? 336 LEU A C   1 
ATOM   2764  O  O   A LEU A  1 337 ? -16.084 -22.092 29.348  0.80 29.13 ? 336 LEU A O   1 
ATOM   2765  O  O   B LEU A  1 337 ? -15.475 -22.663 27.802  0.20 22.27 ? 336 LEU A O   1 
ATOM   2766  C  CB  A LEU A  1 337 ? -14.392 -24.628 30.106  0.80 36.96 ? 336 LEU A CB  1 
ATOM   2767  C  CB  B LEU A  1 337 ? -13.875 -25.139 27.528  0.20 22.70 ? 336 LEU A CB  1 
ATOM   2768  C  CG  A LEU A  1 337 ? -14.500 -26.163 30.137  0.80 39.86 ? 336 LEU A CG  1 
ATOM   2769  C  CG  B LEU A  1 337 ? -13.513 -26.332 26.644  0.20 22.86 ? 336 LEU A CG  1 
ATOM   2770  C  CD1 A LEU A  1 337 ? -13.926 -26.722 31.429  0.80 40.00 ? 336 LEU A CD1 1 
ATOM   2771  C  CD1 B LEU A  1 337 ? -13.964 -27.659 27.248  0.20 23.54 ? 336 LEU A CD1 1 
ATOM   2772  C  CD2 A LEU A  1 337 ? -15.941 -26.621 29.949  0.80 41.39 ? 336 LEU A CD2 1 
ATOM   2773  C  CD2 B LEU A  1 337 ? -14.098 -26.170 25.249  0.20 23.20 ? 336 LEU A CD2 1 
ATOM   2774  N  N   A GLN A  1 338 ? -13.947 -21.645 28.735  0.80 31.28 ? 337 GLN A N   1 
ATOM   2775  N  N   B GLN A  1 338 ? -13.477 -21.662 28.093  0.20 20.98 ? 337 GLN A N   1 
ATOM   2776  C  CA  A GLN A  1 338 ? -14.137 -20.223 28.837  0.80 32.48 ? 337 GLN A CA  1 
ATOM   2777  C  CA  B GLN A  1 338 ? -14.005 -20.388 28.650  0.20 21.15 ? 337 GLN A CA  1 
ATOM   2778  C  C   A GLN A  1 338 ? -15.159 -19.748 27.824  0.80 31.45 ? 337 GLN A C   1 
ATOM   2779  C  C   B GLN A  1 338 ? -15.110 -19.814 27.753  0.20 22.24 ? 337 GLN A C   1 
ATOM   2780  O  O   A GLN A  1 338 ? -16.077 -19.028 28.177  0.80 29.99 ? 337 GLN A O   1 
ATOM   2781  O  O   B GLN A  1 338 ? -16.022 -19.065 28.196  0.20 22.34 ? 337 GLN A O   1 
ATOM   2782  C  CB  A GLN A  1 338 ? -12.825 -19.451 28.724  0.80 34.92 ? 337 GLN A CB  1 
ATOM   2783  C  CB  B GLN A  1 338 ? -12.801 -19.438 28.736  0.20 20.11 ? 337 GLN A CB  1 
ATOM   2784  C  CG  A GLN A  1 338 ? -13.053 -17.969 29.009  0.80 39.13 ? 337 GLN A CG  1 
ATOM   2785  C  CG  B GLN A  1 338 ? -13.007 -17.940 28.948  0.20 19.61 ? 337 GLN A CG  1 
ATOM   2786  C  CD  A GLN A  1 338 ? -13.695 -17.823 30.432  0.80 43.17 ? 337 GLN A CD  1 
ATOM   2787  C  CD  B GLN A  1 338 ? -13.222 -17.505 30.389  0.20 19.19 ? 337 GLN A CD  1 
ATOM   2788  O  OE1 A GLN A  1 338 ? -13.287 -18.531 31.331  0.80 45.15 ? 337 GLN A OE1 1 
ATOM   2789  O  OE1 B GLN A  1 338 ? -13.345 -18.332 31.282  0.20 19.51 ? 337 GLN A OE1 1 
ATOM   2790  N  NE2 A GLN A  1 338 ? -14.787 -17.046 30.596  0.80 48.64 ? 337 GLN A NE2 1 
ATOM   2791  N  NE2 B GLN A  1 338 ? -13.261 -16.193 30.617  0.20 18.55 ? 337 GLN A NE2 1 
ATOM   2792  N  N   A CYS A  1 339 ? -15.038 -20.136 26.562  0.80 30.39 ? 338 CYS A N   1 
ATOM   2793  N  N   B CYS A  1 339 ? -15.043 -20.162 26.474  0.20 23.22 ? 338 CYS A N   1 
ATOM   2794  C  CA  A CYS A  1 339 ? -16.091 -19.729 25.643  0.80 32.03 ? 338 CYS A CA  1 
ATOM   2795  C  CA  B CYS A  1 339 ? -16.099 -19.737 25.583  0.20 24.75 ? 338 CYS A CA  1 
ATOM   2796  C  C   A CYS A  1 339 ? -17.421 -20.223 26.034  0.80 32.00 ? 338 CYS A C   1 
ATOM   2797  C  C   B CYS A  1 339 ? -17.420 -20.213 26.042  0.20 27.70 ? 338 CYS A C   1 
ATOM   2798  O  O   A CYS A  1 339 ? -18.393 -19.543 25.800  0.80 32.42 ? 338 CYS A O   1 
ATOM   2799  O  O   B CYS A  1 339 ? -18.395 -19.537 25.805  0.20 28.28 ? 338 CYS A O   1 
ATOM   2800  C  CB  A CYS A  1 339 ? -15.916 -20.268 24.251  0.80 35.51 ? 338 CYS A CB  1 
ATOM   2801  C  CB  B CYS A  1 339 ? -16.054 -20.383 24.208  0.20 24.60 ? 338 CYS A CB  1 
ATOM   2802  S  SG  A CYS A  1 339 ? -14.347 -19.982 23.583  0.80 35.51 ? 338 CYS A SG  1 
ATOM   2803  S  SG  B CYS A  1 339 ? -14.620 -21.336 23.738  0.20 22.23 ? 338 CYS A SG  1 
ATOM   2804  N  N   . GLN A  1 340 ? -17.471 -21.441 26.551  1.00 31.12 ? 339 GLN A N   1 
ATOM   2805  C  CA  . GLN A  1 340 ? -18.735 -22.018 26.959  1.00 33.67 ? 339 GLN A CA  1 
ATOM   2806  C  C   . GLN A  1 340 ? -19.367 -21.177 28.066  1.00 32.03 ? 339 GLN A C   1 
ATOM   2807  O  O   . GLN A  1 340 ? -20.562 -20.923 28.034  1.00 31.40 ? 339 GLN A O   1 
ATOM   2808  C  CB  . GLN A  1 340 ? -18.545 -23.454 27.395  1.00 38.38 ? 339 GLN A CB  1 
ATOM   2809  C  CG  . GLN A  1 340 ? -19.837 -24.124 27.783  1.00 44.85 ? 339 GLN A CG  1 
ATOM   2810  C  CD  . GLN A  1 340 ? -19.600 -25.552 28.228  1.00 52.43 ? 339 GLN A CD  1 
ATOM   2811  O  OE1 . GLN A  1 340 ? -18.849 -25.803 29.178  1.00 58.58 ? 339 GLN A OE1 1 
ATOM   2812  N  NE2 . GLN A  1 340 ? -20.224 -26.497 27.539  1.00 57.00 ? 339 GLN A NE2 1 
ATOM   2813  N  N   . ALA A  1 341 ? -18.549 -20.683 28.990  1.00 29.36 ? 340 ALA A N   1 
ATOM   2814  C  CA  . ALA A  1 341 ? -19.030 -19.808 30.070  1.00 29.74 ? 340 ALA A CA  1 
ATOM   2815  C  C   . ALA A  1 341 ? -19.609 -18.493 29.540  1.00 29.29 ? 340 ALA A C   1 
ATOM   2816  O  O   . ALA A  1 341 ? -20.556 -17.954 30.101  1.00 28.65 ? 340 ALA A O   1 
ATOM   2817  C  CB  . ALA A  1 341 ? -17.912 -19.521 31.063  1.00 29.51 ? 340 ALA A CB  1 
ATOM   2818  N  N   . TRP A  1 342 ? -19.071 -17.995 28.430  1.00 26.93 ? 341 TRP A N   1 
ATOM   2819  C  CA  . TRP A  1 342 ? -19.558 -16.746 27.864  1.00 26.67 ? 341 TRP A CA  1 
ATOM   2820  C  C   . TRP A  1 342 ? -20.954 -16.829 27.235  1.00 28.39 ? 341 TRP A C   1 
ATOM   2821  O  O   . TRP A  1 342 ? -21.643 -15.826 27.167  1.00 27.02 ? 341 TRP A O   1 
ATOM   2822  C  CB  . TRP A  1 342 ? -18.572 -16.206 26.836  1.00 25.29 ? 341 TRP A CB  1 
ATOM   2823  C  CG  . TRP A  1 342 ? -17.283 -15.712 27.419  1.00 25.06 ? 341 TRP A CG  1 
ATOM   2824  C  CD1 . TRP A  1 342 ? -17.052 -15.204 28.685  1.00 24.56 ? 341 TRP A CD1 1 
ATOM   2825  C  CD2 . TRP A  1 342 ? -16.037 -15.633 26.727  1.00 23.19 ? 341 TRP A CD2 1 
ATOM   2826  N  NE1 . TRP A  1 342 ? -15.729 -14.829 28.806  1.00 24.88 ? 341 TRP A NE1 1 
ATOM   2827  C  CE2 . TRP A  1 342 ? -15.094 -15.083 27.613  1.00 24.00 ? 341 TRP A CE2 1 
ATOM   2828  C  CE3 . TRP A  1 342 ? -15.636 -15.972 25.440  1.00 24.29 ? 341 TRP A CE3 1 
ATOM   2829  C  CZ2 . TRP A  1 342 ? -13.760 -14.879 27.250  1.00 23.55 ? 341 TRP A CZ2 1 
ATOM   2830  C  CZ3 . TRP A  1 342 ? -14.310 -15.763 25.078  1.00 22.73 ? 341 TRP A CZ3 1 
ATOM   2831  C  CH2 . TRP A  1 342 ? -13.394 -15.231 25.981  1.00 23.36 ? 341 TRP A CH2 1 
ATOM   2832  N  N   . GLN A  1 343 ? -21.371 -18.014 26.810  1.00 31.08 ? 342 GLN A N   1 
ATOM   2833  C  CA  . GLN A  1 343 ? -22.698 -18.208 26.239  1.00 35.95 ? 342 GLN A CA  1 
ATOM   2834  C  C   . GLN A  1 343 ? -23.830 -17.630 27.093  1.00 36.54 ? 342 GLN A C   1 
ATOM   2835  O  O   . GLN A  1 343 ? -24.754 -17.022 26.558  1.00 38.66 ? 342 GLN A O   1 
ATOM   2836  C  CB  . GLN A  1 343 ? -22.992 -19.689 26.028  1.00 40.65 ? 342 GLN A CB  1 
ATOM   2837  C  CG  . GLN A  1 343 ? -22.138 -20.345 24.970  1.00 42.48 ? 342 GLN A CG  1 
ATOM   2838  C  CD  . GLN A  1 343 ? -22.594 -21.765 24.675  1.00 46.96 ? 342 GLN A CD  1 
ATOM   2839  O  OE1 . GLN A  1 343 ? -22.688 -22.600 25.583  1.00 53.12 ? 342 GLN A OE1 1 
ATOM   2840  N  NE2 . GLN A  1 343 ? -22.867 -22.052 23.407  1.00 47.16 ? 342 GLN A NE2 1 
ATOM   2841  N  N   . SER A  1 344 ? -23.753 -17.794 28.408  1.00 34.61 ? 343 SER A N   1 
ATOM   2842  C  CA  . SER A  1 344 ? -24.816 -17.311 29.281  1.00 37.82 ? 343 SER A CA  1 
ATOM   2843  C  C   . SER A  1 344 ? -24.586 -15.881 29.774  1.00 36.90 ? 343 SER A C   1 
ATOM   2844  O  O   . SER A  1 344 ? -25.461 -15.316 30.432  1.00 36.73 ? 343 SER A O   1 
ATOM   2845  C  CB  . SER A  1 344 ? -25.007 -18.261 30.470  1.00 39.39 ? 343 SER A CB  1 
ATOM   2846  O  OG  . SER A  1 344 ? -23.874 -18.227 31.312  1.00 41.56 ? 343 SER A OG  1 
ATOM   2847  N  N   . ARG A  1 345 ? -23.454 -15.274 29.420  1.00 32.68 ? 344 ARG A N   1 
ATOM   2848  C  CA  . ARG A  1 345 ? -23.108 -13.928 29.882  1.00 32.39 ? 344 ARG A CA  1 
ATOM   2849  C  C   . ARG A  1 345 ? -23.214 -12.830 28.821  1.00 32.42 ? 344 ARG A C   1 
ATOM   2850  O  O   . ARG A  1 345 ? -23.023 -11.645 29.135  1.00 33.51 ? 344 ARG A O   1 
ATOM   2851  C  CB  . ARG A  1 345 ? -21.678 -13.920 30.421  1.00 33.32 ? 344 ARG A CB  1 
ATOM   2852  C  CG  . ARG A  1 345 ? -21.518 -14.703 31.709  1.00 35.42 ? 344 ARG A CG  1 
ATOM   2853  C  CD  . ARG A  1 345 ? -20.060 -14.728 32.118  1.00 37.68 ? 344 ARG A CD  1 
ATOM   2854  N  NE  . ARG A  1 345 ? -19.805 -15.789 33.078  1.00 38.60 ? 344 ARG A NE  1 
ATOM   2855  C  CZ  . ARG A  1 345 ? -18.632 -16.400 33.246  1.00 41.78 ? 344 ARG A CZ  1 
ATOM   2856  N  NH1 . ARG A  1 345 ? -17.556 -16.077 32.508  1.00 40.08 ? 344 ARG A NH1 1 
ATOM   2857  N  NH2 . ARG A  1 345 ? -18.533 -17.362 34.157  1.00 41.95 ? 344 ARG A NH2 1 
ATOM   2858  N  N   . GLN A  1 346 ? -23.478 -13.187 27.567  1.00 29.60 ? 345 GLN A N   1 
ATOM   2859  C  CA  . GLN A  1 346 ? -23.679 -12.158 26.542  1.00 28.24 ? 345 GLN A CA  1 
ATOM   2860  C  C   . GLN A  1 346 ? -24.880 -12.534 25.692  1.00 28.58 ? 345 GLN A C   1 
ATOM   2861  O  O   . GLN A  1 346 ? -25.255 -13.705 25.637  1.00 28.91 ? 345 GLN A O   1 
ATOM   2862  C  CB  . GLN A  1 346 ? -22.411 -11.934 25.693  1.00 27.02 ? 345 GLN A CB  1 
ATOM   2863  C  CG  . GLN A  1 346 ? -21.941 -13.134 24.899  1.00 25.97 ? 345 GLN A CG  1 
ATOM   2864  C  CD  . GLN A  1 346 ? -20.857 -12.793 23.875  1.00 24.75 ? 345 GLN A CD  1 
ATOM   2865  O  OE1 . GLN A  1 346 ? -19.870 -12.149 24.191  1.00 24.04 ? 345 GLN A OE1 1 
ATOM   2866  N  NE2 . GLN A  1 346 ? -21.065 -13.204 22.644  1.00 23.85 ? 345 GLN A NE2 1 
ATOM   2867  N  N   . GLU A  1 347 ? -25.521 -11.522 25.115  1.00 29.52 ? 346 GLU A N   1 
ATOM   2868  C  CA  . GLU A  1 347 ? -26.674 -11.687 24.222  1.00 30.48 ? 346 GLU A CA  1 
ATOM   2869  C  C   . GLU A  1 347 ? -26.242 -12.159 22.831  1.00 28.95 ? 346 GLU A C   1 
ATOM   2870  O  O   . GLU A  1 347 ? -26.928 -12.955 22.205  1.00 27.85 ? 346 GLU A O   1 
ATOM   2871  C  CB  . GLU A  1 347 ? -27.434 -10.345 24.142  1.00 33.54 ? 346 GLU A CB  1 
ATOM   2872  C  CG  . GLU A  1 347 ? -28.566 -10.231 23.135  1.00 37.84 ? 346 GLU A CG  1 
ATOM   2873  C  CD  . GLU A  1 347 ? -29.440 -8.978  23.333  1.00 43.98 ? 346 GLU A CD  1 
ATOM   2874  O  OE1 . GLU A  1 347 ? -29.471 -8.409  24.453  1.00 46.86 ? 346 GLU A OE1 1 
ATOM   2875  O  OE2 . GLU A  1 347 ? -30.115 -8.560  22.359  1.00 45.65 ? 346 GLU A OE2 1 
ATOM   2876  N  N   . HIS A  1 348 ? -25.107 -11.666 22.325  1.00 26.57 ? 347 HIS A N   1 
ATOM   2877  C  CA  A HIS A  1 348 ? -24.604 -12.114 21.024  0.70 26.22 ? 347 HIS A CA  1 
ATOM   2878  C  CA  B HIS A  1 348 ? -24.607 -12.142 21.036  0.30 26.30 ? 347 HIS A CA  1 
ATOM   2879  C  C   . HIS A  1 348 ? -24.301 -13.628 21.100  1.00 26.08 ? 347 HIS A C   1 
ATOM   2880  O  O   . HIS A  1 348 ? -23.842 -14.141 22.129  1.00 25.28 ? 347 HIS A O   1 
ATOM   2881  C  CB  A HIS A  1 348 ? -23.305 -11.390 20.616  0.70 25.41 ? 347 HIS A CB  1 
ATOM   2882  C  CB  B HIS A  1 348 ? -23.349 -11.396 20.616  0.30 25.43 ? 347 HIS A CB  1 
ATOM   2883  C  CG  A HIS A  1 348 ? -23.447 -10.031 20.003  0.70 25.61 ? 347 HIS A CG  1 
ATOM   2884  C  CG  B HIS A  1 348 ? -23.619 -10.092 19.958  0.30 25.62 ? 347 HIS A CG  1 
ATOM   2885  N  ND1 A HIS A  1 348 ? -23.093 -8.860  20.655  0.70 26.36 ? 347 HIS A ND1 1 
ATOM   2886  N  ND1 B HIS A  1 348 ? -23.873 -9.990  18.608  0.30 25.77 ? 347 HIS A ND1 1 
ATOM   2887  C  CD2 A HIS A  1 348 ? -23.776 -9.668  18.743  0.70 26.15 ? 347 HIS A CD2 1 
ATOM   2888  C  CD2 B HIS A  1 348 ? -23.683 -8.836  20.453  0.30 26.02 ? 347 HIS A CD2 1 
ATOM   2889  C  CE1 A HIS A  1 348 ? -23.257 -7.837  19.833  0.70 25.77 ? 347 HIS A CE1 1 
ATOM   2890  C  CE1 B HIS A  1 348 ? -24.080 -8.724  18.299  0.30 26.23 ? 347 HIS A CE1 1 
ATOM   2891  N  NE2 A HIS A  1 348 ? -23.672 -8.298  18.668  0.70 26.61 ? 347 HIS A NE2 1 
ATOM   2892  N  NE2 B HIS A  1 348 ? -23.968 -8.005  19.400  0.30 26.10 ? 347 HIS A NE2 1 
ATOM   2893  N  N   . GLN A  1 349 ? -24.531 -14.326 19.995  1.00 26.98 ? 348 GLN A N   1 
ATOM   2894  C  CA  . GLN A  1 349 ? -24.290 -15.762 19.951  1.00 29.22 ? 348 GLN A CA  1 
ATOM   2895  C  C   . GLN A  1 349 ? -22.823 -16.130 20.149  1.00 26.60 ? 348 GLN A C   1 
ATOM   2896  O  O   . GLN A  1 349 ? -21.915 -15.421 19.687  1.00 24.79 ? 348 GLN A O   1 
ATOM   2897  C  CB  . GLN A  1 349 ? -24.677 -16.350 18.605  1.00 33.06 ? 348 GLN A CB  1 
ATOM   2898  C  CG  . GLN A  1 349 ? -26.110 -16.208 18.204  1.00 40.43 ? 348 GLN A CG  1 
ATOM   2899  C  CD  . GLN A  1 349 ? -26.321 -16.818 16.835  1.00 46.27 ? 348 GLN A CD  1 
ATOM   2900  O  OE1 . GLN A  1 349 ? -26.190 -18.038 16.663  1.00 49.97 ? 348 GLN A OE1 1 
ATOM   2901  N  NE2 . GLN A  1 349 ? -26.594 -15.973 15.843  1.00 48.22 ? 348 GLN A NE2 1 
ATOM   2902  N  N   . VAL A  1 350 ? -22.606 -17.258 20.819  1.00 26.05 ? 349 VAL A N   1 
ATOM   2903  C  CA  . VAL A  1 350 ? -21.288 -17.889 20.932  1.00 25.57 ? 349 VAL A CA  1 
ATOM   2904  C  C   . VAL A  1 350 ? -21.408 -19.284 20.315  1.00 27.16 ? 349 VAL A C   1 
ATOM   2905  O  O   . VAL A  1 350 ? -22.184 -20.118 20.814  1.00 28.12 ? 349 VAL A O   1 
ATOM   2906  C  CB  . VAL A  1 350 ? -20.825 -18.011 22.390  1.00 25.57 ? 349 VAL A CB  1 
ATOM   2907  C  CG1 . VAL A  1 350 ? -19.480 -18.741 22.491  1.00 25.10 ? 349 VAL A CG1 1 
ATOM   2908  C  CG2 . VAL A  1 350 ? -20.739 -16.641 23.063  1.00 25.75 ? 349 VAL A CG2 1 
ATOM   2909  N  N   A LEU A  1 351 ? -20.674 -19.538 19.236  0.50 26.39 ? 350 LEU A N   1 
ATOM   2910  N  N   B LEU A  1 351 ? -20.674 -19.536 19.238  0.50 26.38 ? 350 LEU A N   1 
ATOM   2911  C  CA  A LEU A  1 351 ? -20.679 -20.849 18.582  0.50 27.70 ? 350 LEU A CA  1 
ATOM   2912  C  CA  B LEU A  1 351 ? -20.683 -20.841 18.578  0.50 27.67 ? 350 LEU A CA  1 
ATOM   2913  C  C   A LEU A  1 351 ? -19.364 -21.550 18.870  0.50 27.76 ? 350 LEU A C   1 
ATOM   2914  C  C   B LEU A  1 351 ? -19.366 -21.550 18.864  0.50 27.75 ? 350 LEU A C   1 
ATOM   2915  O  O   A LEU A  1 351 ? -18.295 -20.977 18.652  0.50 27.51 ? 350 LEU A O   1 
ATOM   2916  O  O   B LEU A  1 351 ? -18.295 -20.977 18.651  0.50 27.50 ? 350 LEU A O   1 
ATOM   2917  C  CB  A LEU A  1 351 ? -20.838 -20.701 17.074  0.50 28.72 ? 350 LEU A CB  1 
ATOM   2918  C  CB  B LEU A  1 351 ? -20.864 -20.666 17.073  0.50 28.75 ? 350 LEU A CB  1 
ATOM   2919  C  CG  A LEU A  1 351 ? -22.044 -19.937 16.529  0.50 29.96 ? 350 LEU A CG  1 
ATOM   2920  C  CG  B LEU A  1 351 ? -22.091 -19.855 16.577  0.50 30.00 ? 350 LEU A CG  1 
ATOM   2921  C  CD1 A LEU A  1 351 ? -23.318 -20.358 17.234  0.50 30.70 ? 350 LEU A CD1 1 
ATOM   2922  C  CD1 B LEU A  1 351 ? -21.813 -18.354 16.578  0.50 30.38 ? 350 LEU A CD1 1 
ATOM   2923  C  CD2 A LEU A  1 351 ? -21.789 -18.448 16.676  0.50 30.35 ? 350 LEU A CD2 1 
ATOM   2924  C  CD2 B LEU A  1 351 ? -22.539 -20.272 15.180  0.50 30.56 ? 350 LEU A CD2 1 
ATOM   2925  N  N   . LEU A  1 352 ? -19.435 -22.775 19.377  1.00 28.07 ? 351 LEU A N   1 
ATOM   2926  C  CA  . LEU A  1 352 ? -18.241 -23.568 19.647  1.00 28.88 ? 351 LEU A CA  1 
ATOM   2927  C  C   . LEU A  1 352 ? -18.030 -24.543 18.510  1.00 29.07 ? 351 LEU A C   1 
ATOM   2928  O  O   . LEU A  1 352 ? -18.980 -25.176 18.060  1.00 31.05 ? 351 LEU A O   1 
ATOM   2929  C  CB  . LEU A  1 352 ? -18.356 -24.307 20.979  1.00 32.57 ? 351 LEU A CB  1 
ATOM   2930  C  CG  . LEU A  1 352 ? -17.685 -23.545 22.143  1.00 34.94 ? 351 LEU A CG  1 
ATOM   2931  C  CD1 . LEU A  1 352 ? -18.496 -22.313 22.510  1.00 35.64 ? 351 LEU A CD1 1 
ATOM   2932  C  CD2 . LEU A  1 352 ? -17.508 -24.453 23.347  1.00 37.04 ? 351 LEU A CD2 1 
ATOM   2933  N  N   . GLN A  1 353 ? -16.805 -24.651 18.020  1.00 26.32 ? 352 GLN A N   1 
ATOM   2934  C  CA  . GLN A  1 353 ? -16.502 -25.614 16.984  1.00 27.80 ? 352 GLN A CA  1 
ATOM   2935  C  C   . GLN A  1 353 ? -15.235 -26.389 17.303  1.00 26.92 ? 352 GLN A C   1 
ATOM   2936  O  O   . GLN A  1 353 ? -14.115 -25.847 17.237  1.00 24.68 ? 352 GLN A O   1 
ATOM   2937  C  CB  . GLN A  1 353 ? -16.363 -24.924 15.618  1.00 28.80 ? 352 GLN A CB  1 
ATOM   2938  C  CG  . GLN A  1 353 ? -16.001 -25.887 14.498  1.00 29.68 ? 352 GLN A CG  1 
ATOM   2939  C  CD  . GLN A  1 353 ? -17.092 -26.906 14.269  1.00 31.89 ? 352 GLN A CD  1 
ATOM   2940  O  OE1 . GLN A  1 353 ? -18.191 -26.535 13.882  1.00 33.70 ? 352 GLN A OE1 1 
ATOM   2941  N  NE2 . GLN A  1 353 ? -16.811 -28.183 14.529  1.00 31.40 ? 352 GLN A NE2 1 
ATOM   2942  N  N   . GLU A  1 354 ? -15.413 -27.664 17.643  1.00 26.27 ? 353 GLU A N   1 
ATOM   2943  C  CA  . GLU A  1 354 ? -14.289 -28.564 17.845  1.00 26.60 ? 353 GLU A CA  1 
ATOM   2944  C  C   . GLU A  1 354 ? -13.623 -28.910 16.520  1.00 25.90 ? 353 GLU A C   1 
ATOM   2945  O  O   . GLU A  1 354 ? -14.305 -29.144 15.506  1.00 25.20 ? 353 GLU A O   1 
ATOM   2946  C  CB  . GLU A  1 354 ? -14.755 -29.849 18.543  1.00 29.04 ? 353 GLU A CB  1 
ATOM   2947  C  CG  . GLU A  1 354 ? -13.613 -30.709 19.050  1.00 30.23 ? 353 GLU A CG  1 
ATOM   2948  C  CD  . GLU A  1 354 ? -14.066 -32.066 19.561  1.00 34.06 ? 353 GLU A CD  1 
ATOM   2949  O  OE1 . GLU A  1 354 ? -15.304 -32.293 19.616  1.00 35.95 ? 353 GLU A OE1 1 
ATOM   2950  O  OE2 . GLU A  1 354 ? -13.178 -32.895 19.887  1.00 33.57 ? 353 GLU A OE2 1 
ATOM   2951  N  N   . LEU A  1 355 ? -12.290 -28.954 16.533  1.00 25.02 ? 354 LEU A N   1 
ATOM   2952  C  CA  . LEU A  1 355 ? -11.482 -29.374 15.397  1.00 25.50 ? 354 LEU A CA  1 
ATOM   2953  C  C   . LEU A  1 355 ? -10.645 -30.581 15.827  1.00 26.59 ? 354 LEU A C   1 
ATOM   2954  O  O   . LEU A  1 355 ? -9.474  -30.440 16.216  1.00 24.48 ? 354 LEU A O   1 
ATOM   2955  C  CB  . LEU A  1 355 ? -10.570 -28.244 14.922  1.00 24.94 ? 354 LEU A CB  1 
ATOM   2956  C  CG  . LEU A  1 355 ? -11.290 -26.920 14.587  1.00 25.64 ? 354 LEU A CG  1 
ATOM   2957  C  CD1 . LEU A  1 355 ? -10.284 -25.816 14.360  1.00 25.38 ? 354 LEU A CD1 1 
ATOM   2958  C  CD2 . LEU A  1 355 ? -12.215 -27.085 13.387  1.00 26.60 ? 354 LEU A CD2 1 
ATOM   2959  N  N   . PRO A  1 356 ? -11.240 -31.782 15.772  1.00 28.43 ? 355 PRO A N   1 
ATOM   2960  C  CA  . PRO A  1 356 ? -10.474 -32.953 16.219  1.00 29.35 ? 355 PRO A CA  1 
ATOM   2961  C  C   . PRO A  1 356 ? -9.281  -33.250 15.320  1.00 28.85 ? 355 PRO A C   1 
ATOM   2962  O  O   . PRO A  1 356 ? -9.416  -33.292 14.093  1.00 27.77 ? 355 PRO A O   1 
ATOM   2963  C  CB  . PRO A  1 356 ? -11.490 -34.105 16.193  1.00 31.34 ? 355 PRO A CB  1 
ATOM   2964  C  CG  . PRO A  1 356 ? -12.774 -33.539 15.731  1.00 32.37 ? 355 PRO A CG  1 
ATOM   2965  C  CD  . PRO A  1 356 ? -12.545 -32.149 15.204  1.00 31.28 ? 355 PRO A CD  1 
ATOM   2966  N  N   . GLY A  1 357 ? -8.120  -33.426 15.936  1.00 27.84 ? 356 GLY A N   1 
ATOM   2967  C  CA  . GLY A  1 357 ? -6.893  -33.745 15.234  1.00 28.60 ? 356 GLY A CA  1 
ATOM   2968  C  C   . GLY A  1 357 ? -6.210  -32.528 14.645  1.00 28.84 ? 356 GLY A C   1 
ATOM   2969  O  O   . GLY A  1 357 ? -5.283  -32.672 13.856  1.00 29.62 ? 356 GLY A O   1 
ATOM   2970  N  N   . SER A  1 358 ? -6.663  -31.321 14.986  1.00 27.45 ? 357 SER A N   1 
ATOM   2971  C  CA  . SER A  1 358 ? -6.088  -30.122 14.375  1.00 26.73 ? 357 SER A CA  1 
ATOM   2972  C  C   . SER A  1 358 ? -5.044  -29.512 15.316  1.00 25.26 ? 357 SER A C   1 
ATOM   2973  O  O   . SER A  1 358 ? -5.370  -29.033 16.408  1.00 24.83 ? 357 SER A O   1 
ATOM   2974  C  CB  . SER A  1 358 ? -7.197  -29.120 14.045  1.00 27.32 ? 357 SER A CB  1 
ATOM   2975  O  OG  . SER A  1 358 ? -6.696  -28.013 13.333  1.00 28.53 ? 357 SER A OG  1 
ATOM   2976  N  N   . GLU A  1 359 ? -3.785  -29.550 14.902  1.00 23.75 ? 358 GLU A N   1 
ATOM   2977  C  CA  . GLU A  1 359 ? -2.696  -28.991 15.690  1.00 23.13 ? 358 GLU A CA  1 
ATOM   2978  C  C   . GLU A  1 359 ? -2.680  -27.454 15.644  1.00 21.32 ? 358 GLU A C   1 
ATOM   2979  O  O   . GLU A  1 359 ? -3.141  -26.804 14.690  1.00 20.74 ? 358 GLU A O   1 
ATOM   2980  C  CB  . GLU A  1 359 ? -1.355  -29.600 15.218  1.00 25.40 ? 358 GLU A CB  1 
ATOM   2981  C  CG  . GLU A  1 359 ? -0.124  -29.243 16.048  1.00 27.28 ? 358 GLU A CG  1 
ATOM   2982  C  CD  . GLU A  1 359 ? 0.507   -27.917 15.647  1.00 29.65 ? 358 GLU A CD  1 
ATOM   2983  O  OE1 . GLU A  1 359 ? 0.370   -27.515 14.448  1.00 31.37 ? 358 GLU A OE1 1 
ATOM   2984  O  OE2 . GLU A  1 359 ? 1.125   -27.259 16.519  1.00 29.15 ? 358 GLU A OE2 1 
ATOM   2985  N  N   . HIS A  1 360 ? -2.138  -26.885 16.704  1.00 20.45 ? 359 HIS A N   1 
ATOM   2986  C  CA  . HIS A  1 360 ? -2.202  -25.451 16.991  1.00 20.08 ? 359 HIS A CA  1 
ATOM   2987  C  C   . HIS A  1 360 ? -1.830  -24.535 15.821  1.00 21.30 ? 359 HIS A C   1 
ATOM   2988  O  O   . HIS A  1 360 ? -2.536  -23.582 15.537  1.00 20.76 ? 359 HIS A O   1 
ATOM   2989  C  CB  . HIS A  1 360 ? -1.270  -25.139 18.156  1.00 19.25 ? 359 HIS A CB  1 
ATOM   2990  C  CG  . HIS A  1 360 ? -1.409  -23.744 18.670  1.00 18.64 ? 359 HIS A CG  1 
ATOM   2991  N  ND1 . HIS A  1 360 ? -2.580  -23.278 19.236  1.00 19.13 ? 359 HIS A ND1 1 
ATOM   2992  C  CD2 . HIS A  1 360 ? -0.550  -22.707 18.676  1.00 18.72 ? 359 HIS A CD2 1 
ATOM   2993  C  CE1 . HIS A  1 360 ? -2.416  -22.022 19.600  1.00 19.00 ? 359 HIS A CE1 1 
ATOM   2994  N  NE2 . HIS A  1 360 ? -1.196  -21.652 19.271  1.00 18.38 ? 359 HIS A NE2 1 
ATOM   2995  N  N   . ILE A  1 361 ? -0.691  -24.784 15.202  1.00 23.72 ? 360 ILE A N   1 
ATOM   2996  C  CA  . ILE A  1 361 ? -0.268  -23.987 14.045  1.00 27.65 ? 360 ILE A CA  1 
ATOM   2997  C  C   . ILE A  1 361 ? -0.887  -24.448 12.729  1.00 27.85 ? 360 ILE A C   1 
ATOM   2998  O  O   . ILE A  1 361 ? -1.314  -23.622 11.895  1.00 27.14 ? 360 ILE A O   1 
ATOM   2999  C  CB  . ILE A  1 361 ? 1.256   -24.010 13.896  1.00 32.40 ? 360 ILE A CB  1 
ATOM   3000  C  CG1 . ILE A  1 361 ? 1.887   -23.384 15.136  1.00 34.60 ? 360 ILE A CG1 1 
ATOM   3001  C  CG2 . ILE A  1 361 ? 1.662   -23.238 12.637  1.00 33.74 ? 360 ILE A CG2 1 
ATOM   3002  C  CD1 . ILE A  1 361 ? 3.390   -23.544 15.193  1.00 38.21 ? 360 ILE A CD1 1 
ATOM   3003  N  N   . GLU A  1 362 ? -0.968  -25.750 12.536  1.00 26.73 ? 361 GLU A N   1 
ATOM   3004  C  CA  . GLU A  1 362 ? -1.511  -26.279 11.292  1.00 28.77 ? 361 GLU A CA  1 
ATOM   3005  C  C   . GLU A  1 362 ? -2.956  -25.819 11.055  1.00 27.55 ? 361 GLU A C   1 
ATOM   3006  O  O   . GLU A  1 362 ? -3.409  -25.793 9.916   1.00 25.06 ? 361 GLU A O   1 
ATOM   3007  C  CB  . GLU A  1 362 ? -1.406  -27.803 11.275  1.00 33.39 ? 361 GLU A CB  1 
ATOM   3008  C  CG  . GLU A  1 362 ? 0.045   -28.257 11.161  1.00 39.22 ? 361 GLU A CG  1 
ATOM   3009  C  CD  . GLU A  1 362 ? 0.246   -29.761 11.271  1.00 46.26 ? 361 GLU A CD  1 
ATOM   3010  O  OE1 . GLU A  1 362 ? -0.748  -30.532 11.299  1.00 50.96 ? 361 GLU A OE1 1 
ATOM   3011  O  OE2 . GLU A  1 362 ? 1.425   -30.175 11.331  1.00 54.37 ? 361 GLU A OE2 1 
ATOM   3012  N  N   . MET A  1 363 ? -3.687  -25.478 12.120  1.00 25.20 ? 362 MET A N   1 
ATOM   3013  C  CA  . MET A  1 363 ? -5.100  -25.102 11.958  1.00 25.26 ? 362 MET A CA  1 
ATOM   3014  C  C   . MET A  1 363 ? -5.278  -23.882 11.055  1.00 24.67 ? 362 MET A C   1 
ATOM   3015  O  O   . MET A  1 363 ? -6.310  -23.753 10.427  1.00 23.85 ? 362 MET A O   1 
ATOM   3016  C  CB  . MET A  1 363 ? -5.826  -24.909 13.303  1.00 26.49 ? 362 MET A CB  1 
ATOM   3017  C  CG  . MET A  1 363 ? -5.537  -23.653 14.075  1.00 29.04 ? 362 MET A CG  1 
ATOM   3018  S  SD  . MET A  1 363 ? -6.779  -23.445 15.421  1.00 33.09 ? 362 MET A SD  1 
ATOM   3019  C  CE  . MET A  1 363 ? -6.498  -24.913 16.438  1.00 32.53 ? 362 MET A CE  1 
ATOM   3020  N  N   . LEU A  1 364 ? -4.256  -23.027 10.979  1.00 24.54 ? 363 LEU A N   1 
ATOM   3021  C  CA  . LEU A  1 364 ? -4.286  -21.848 10.112  1.00 25.56 ? 363 LEU A CA  1 
ATOM   3022  C  C   . LEU A  1 364 ? -4.252  -22.120 8.616   1.00 24.62 ? 363 LEU A C   1 
ATOM   3023  O  O   . LEU A  1 364 ? -4.620  -21.244 7.821   1.00 24.24 ? 363 LEU A O   1 
ATOM   3024  C  CB  . LEU A  1 364 ? -3.112  -20.924 10.423  1.00 26.64 ? 363 LEU A CB  1 
ATOM   3025  C  CG  . LEU A  1 364 ? -3.260  -20.015 11.619  1.00 28.00 ? 363 LEU A CG  1 
ATOM   3026  C  CD1 . LEU A  1 364 ? -2.073  -19.062 11.592  1.00 29.36 ? 363 LEU A CD1 1 
ATOM   3027  C  CD2 . LEU A  1 364 ? -4.551  -19.204 11.585  1.00 27.44 ? 363 LEU A CD2 1 
ATOM   3028  N  N   . ALA A  1 365 ? -3.781  -23.300 8.230   1.00 23.91 ? 364 ALA A N   1 
ATOM   3029  C  CA  . ALA A  1 365 ? -3.694  -23.679 6.812   1.00 25.54 ? 364 ALA A CA  1 
ATOM   3030  C  C   . ALA A  1 365 ? -4.583  -24.863 6.512   1.00 26.22 ? 364 ALA A C   1 
ATOM   3031  O  O   . ALA A  1 365 ? -4.511  -25.445 5.444   1.00 29.64 ? 364 ALA A O   1 
ATOM   3032  C  CB  . ALA A  1 365 ? -2.244  -23.994 6.447   1.00 25.22 ? 364 ALA A CB  1 
ATOM   3033  N  N   . ASN A  1 366 ? -5.441  -25.225 7.452   1.00 24.83 ? 365 ASN A N   1 
ATOM   3034  C  CA  . ASN A  1 366 ? -6.237  -26.434 7.333   1.00 25.46 ? 365 ASN A CA  1 
ATOM   3035  C  C   . ASN A  1 366 ? -7.544  -26.147 6.591   1.00 25.14 ? 365 ASN A C   1 
ATOM   3036  O  O   . ASN A  1 366 ? -8.218  -25.166 6.858   1.00 22.99 ? 365 ASN A O   1 
ATOM   3037  C  CB  . ASN A  1 366 ? -6.466  -26.966 8.745   1.00 26.44 ? 365 ASN A CB  1 
ATOM   3038  C  CG  . ASN A  1 366 ? -7.312  -28.209 8.799   1.00 28.30 ? 365 ASN A CG  1 
ATOM   3039  O  OD1 . ASN A  1 366 ? -8.441  -28.258 8.299   1.00 30.61 ? 365 ASN A OD1 1 
ATOM   3040  N  ND2 . ASN A  1 366 ? -6.770  -29.239 9.442   1.00 29.03 ? 365 ASN A ND2 1 
ATOM   3041  N  N   . ALA A  1 367 ? -7.862  -27.001 5.629   1.00 25.77 ? 366 ALA A N   1 
ATOM   3042  C  CA  . ALA A  1 367 ? -9.022  -26.825 4.747   1.00 26.31 ? 366 ALA A CA  1 
ATOM   3043  C  C   . ALA A  1 367 ? -10.345 -26.728 5.500   1.00 25.64 ? 366 ALA A C   1 
ATOM   3044  O  O   . ALA A  1 367 ? -11.242 -26.018 5.063   1.00 26.22 ? 366 ALA A O   1 
ATOM   3045  C  CB  . ALA A  1 367 ? -9.075  -27.949 3.700   1.00 27.78 ? 366 ALA A CB  1 
ATOM   3046  N  N   . THR A  1 368 ? -10.487 -27.462 6.597   1.00 26.56 ? 367 THR A N   1 
ATOM   3047  C  CA  A THR A  1 368 ? -11.711 -27.401 7.404   0.50 26.54 ? 367 THR A CA  1 
ATOM   3048  C  CA  B THR A  1 368 ? -11.704 -27.402 7.396   0.50 25.63 ? 367 THR A CA  1 
ATOM   3049  C  C   . THR A  1 368 ? -11.834 -26.052 8.108   1.00 25.02 ? 367 THR A C   1 
ATOM   3050  O  O   . THR A  1 368 ? -12.912 -25.480 8.172   1.00 23.56 ? 367 THR A O   1 
ATOM   3051  C  CB  A THR A  1 368 ? -11.818 -28.550 8.429   0.50 28.58 ? 367 THR A CB  1 
ATOM   3052  C  CB  B THR A  1 368 ? -11.725 -28.565 8.388   0.50 26.47 ? 367 THR A CB  1 
ATOM   3053  O  OG1 A THR A  1 368 ? -10.663 -28.576 9.285   0.50 29.64 ? 367 THR A OG1 1 
ATOM   3054  O  OG1 B THR A  1 368 ? -11.622 -29.779 7.648   0.50 27.02 ? 367 THR A OG1 1 
ATOM   3055  C  CG2 A THR A  1 368 ? -11.947 -29.850 7.713   0.50 29.67 ? 367 THR A CG2 1 
ATOM   3056  C  CG2 B THR A  1 368 ? -12.995 -28.552 9.248   0.50 26.17 ? 367 THR A CG2 1 
ATOM   3057  N  N   . THR A  1 369 ? -10.721 -25.525 8.606   1.00 23.17 ? 368 THR A N   1 
ATOM   3058  C  CA  . THR A  1 369 ? -10.722 -24.189 9.201   1.00 22.41 ? 368 THR A CA  1 
ATOM   3059  C  C   . THR A  1 369 ? -11.124 -23.145 8.167   1.00 21.55 ? 368 THR A C   1 
ATOM   3060  O  O   . THR A  1 369 ? -11.935 -22.253 8.440   1.00 20.42 ? 368 THR A O   1 
ATOM   3061  C  CB  . THR A  1 369 ? -9.330  -23.789 9.735   1.00 22.27 ? 368 THR A CB  1 
ATOM   3062  O  OG1 . THR A  1 369 ? -8.840  -24.780 10.646  1.00 23.23 ? 368 THR A OG1 1 
ATOM   3063  C  CG2 . THR A  1 369 ? -9.387  -22.442 10.431  1.00 22.65 ? 368 THR A CG2 1 
ATOM   3064  N  N   . LEU A  1 370 ? -10.559 -23.267 6.980   1.00 21.61 ? 369 LEU A N   1 
ATOM   3065  C  CA  . LEU A  1 370 ? -10.808 -22.289 5.924   1.00 21.97 ? 369 LEU A CA  1 
ATOM   3066  C  C   . LEU A  1 370 ? -12.260 -22.390 5.417   1.00 22.41 ? 369 LEU A C   1 
ATOM   3067  O  O   . LEU A  1 370 ? -12.880 -21.379 5.122   1.00 21.76 ? 369 LEU A O   1 
ATOM   3068  C  CB  . LEU A  1 370 ? -9.799  -22.475 4.801   1.00 22.87 ? 369 LEU A CB  1 
ATOM   3069  C  CG  . LEU A  1 370 ? -8.351  -22.207 5.232   1.00 23.17 ? 369 LEU A CG  1 
ATOM   3070  C  CD1 . LEU A  1 370 ? -7.350  -22.602 4.145   1.00 25.11 ? 369 LEU A CD1 1 
ATOM   3071  C  CD2 . LEU A  1 370 ? -8.165  -20.770 5.623   1.00 23.44 ? 369 LEU A CD2 1 
ATOM   3072  N  N   . ALA A  1 371 ? -12.796 -23.604 5.349   1.00 22.50 ? 370 ALA A N   1 
ATOM   3073  C  CA  . ALA A  1 371 ? -14.202 -23.793 4.959   1.00 23.73 ? 370 ALA A CA  1 
ATOM   3074  C  C   . ALA A  1 371 ? -15.152 -23.158 5.977   1.00 23.35 ? 370 ALA A C   1 
ATOM   3075  O  O   . ALA A  1 371 ? -16.176 -22.579 5.601   1.00 24.54 ? 370 ALA A O   1 
ATOM   3076  C  CB  . ALA A  1 371 ? -14.525 -25.279 4.798   1.00 24.63 ? 370 ALA A CB  1 
ATOM   3077  N  N   . TYR A  1 372 ? -14.816 -23.256 7.259   1.00 22.87 ? 371 TYR A N   1 
ATOM   3078  C  CA  . TYR A  1 372 ? -15.610 -22.599 8.304   1.00 23.06 ? 371 TYR A CA  1 
ATOM   3079  C  C   . TYR A  1 372 ? -15.574 -21.069 8.145   1.00 20.99 ? 371 TYR A C   1 
ATOM   3080  O  O   . TYR A  1 372 ? -16.593 -20.390 8.165   1.00 20.27 ? 371 TYR A O   1 
ATOM   3081  C  CB  . TYR A  1 372 ? -15.121 -23.003 9.707   1.00 23.30 ? 371 TYR A CB  1 
ATOM   3082  C  CG  . TYR A  1 372 ? -16.061 -22.569 10.807  1.00 24.50 ? 371 TYR A CG  1 
ATOM   3083  C  CD1 . TYR A  1 372 ? -16.072 -21.252 11.264  1.00 24.50 ? 371 TYR A CD1 1 
ATOM   3084  C  CD2 . TYR A  1 372 ? -16.949 -23.472 11.394  1.00 26.80 ? 371 TYR A CD2 1 
ATOM   3085  C  CE1 . TYR A  1 372 ? -16.950 -20.843 12.257  1.00 25.04 ? 371 TYR A CE1 1 
ATOM   3086  C  CE2 . TYR A  1 372 ? -17.820 -23.074 12.398  1.00 27.23 ? 371 TYR A CE2 1 
ATOM   3087  C  CZ  . TYR A  1 372 ? -17.829 -21.752 12.814  1.00 26.80 ? 371 TYR A CZ  1 
ATOM   3088  O  OH  . TYR A  1 372 ? -18.708 -21.334 13.789  1.00 26.18 ? 371 TYR A OH  1 
ATOM   3089  N  N   . LEU A  1 373 ? -14.381 -20.529 7.977   1.00 20.43 ? 372 LEU A N   1 
ATOM   3090  C  CA  . LEU A  1 373 ? -14.239 -19.102 7.753   1.00 20.31 ? 372 LEU A CA  1 
ATOM   3091  C  C   . LEU A  1 373 ? -15.014 -18.617 6.519   1.00 20.51 ? 372 LEU A C   1 
ATOM   3092  O  O   . LEU A  1 373 ? -15.633 -17.554 6.538   1.00 20.05 ? 372 LEU A O   1 
ATOM   3093  C  CB  . LEU A  1 373 ? -12.749 -18.736 7.675   1.00 20.34 ? 372 LEU A CB  1 
ATOM   3094  C  CG  . LEU A  1 373 ? -12.436 -17.261 7.479   1.00 20.63 ? 372 LEU A CG  1 
ATOM   3095  C  CD1 . LEU A  1 373 ? -12.915 -16.403 8.649   1.00 20.82 ? 372 LEU A CD1 1 
ATOM   3096  C  CD2 . LEU A  1 373 ? -10.931 -17.084 7.260   1.00 20.91 ? 372 LEU A CD2 1 
ATOM   3097  N  N   . LYS A  1 374 ? -14.963 -19.388 5.442   1.00 21.55 ? 373 LYS A N   1 
ATOM   3098  C  CA  . LYS A  1 374 ? -15.686 -19.038 4.230   1.00 22.71 ? 373 LYS A CA  1 
ATOM   3099  C  C   . LYS A  1 374 ? -17.188 -18.879 4.471   1.00 24.74 ? 373 LYS A C   1 
ATOM   3100  O  O   . LYS A  1 374 ? -17.809 -17.931 3.962   1.00 23.70 ? 373 LYS A O   1 
ATOM   3101  C  CB  . LYS A  1 374 ? -15.467 -20.087 3.151   1.00 23.94 ? 373 LYS A CB  1 
ATOM   3102  C  CG  . LYS A  1 374 ? -15.956 -19.605 1.790   1.00 25.05 ? 373 LYS A CG  1 
ATOM   3103  C  CD  . LYS A  1 374 ? -15.788 -20.662 0.730   1.00 26.59 ? 373 LYS A CD  1 
ATOM   3104  C  CE  . LYS A  1 374 ? -16.144 -20.097 -0.635  1.00 28.13 ? 373 LYS A CE  1 
ATOM   3105  N  NZ  . LYS A  1 374 ? -15.901 -21.152 -1.647  1.00 29.63 ? 373 LYS A NZ  1 
ATOM   3106  N  N   . ARG A  1 375 ? -17.755 -19.789 5.262   1.00 25.74 ? 374 ARG A N   1 
ATOM   3107  C  CA  A ARG A  1 375 ? -19.166 -19.720 5.624   0.50 27.64 ? 374 ARG A CA  1 
ATOM   3108  C  CA  B ARG A  1 375 ? -19.171 -19.722 5.632   0.50 27.64 ? 374 ARG A CA  1 
ATOM   3109  C  C   . ARG A  1 375 ? -19.466 -18.463 6.458   1.00 26.68 ? 374 ARG A C   1 
ATOM   3110  O  O   . ARG A  1 375 ? -20.491 -17.814 6.250   1.00 26.51 ? 374 ARG A O   1 
ATOM   3111  C  CB  A ARG A  1 375 ? -19.567 -20.997 6.365   0.50 30.02 ? 374 ARG A CB  1 
ATOM   3112  C  CB  B ARG A  1 375 ? -19.576 -20.991 6.395   0.50 30.26 ? 374 ARG A CB  1 
ATOM   3113  C  CG  A ARG A  1 375 ? -21.023 -21.049 6.801   0.50 33.51 ? 374 ARG A CG  1 
ATOM   3114  C  CG  B ARG A  1 375 ? -20.998 -21.001 6.970   0.50 33.86 ? 374 ARG A CG  1 
ATOM   3115  C  CD  A ARG A  1 375 ? -21.980 -21.025 5.621   0.50 35.75 ? 374 ARG A CD  1 
ATOM   3116  C  CD  B ARG A  1 375 ? -21.134 -22.083 8.043   0.50 36.26 ? 374 ARG A CD  1 
ATOM   3117  N  NE  A ARG A  1 375 ? -23.366 -21.007 6.084   0.50 39.04 ? 374 ARG A NE  1 
ATOM   3118  N  NE  B ARG A  1 375 ? -22.026 -21.727 9.160   0.50 37.89 ? 374 ARG A NE  1 
ATOM   3119  C  CZ  A ARG A  1 375 ? -23.959 -19.937 6.606   0.50 40.81 ? 374 ARG A CZ  1 
ATOM   3120  C  CZ  B ARG A  1 375 ? -21.635 -21.061 10.244  0.50 37.85 ? 374 ARG A CZ  1 
ATOM   3121  N  NH1 A ARG A  1 375 ? -25.214 -20.007 7.016   0.50 43.78 ? 374 ARG A NH1 1 
ATOM   3122  N  NH1 B ARG A  1 375 ? -22.493 -20.787 11.212  0.50 39.06 ? 374 ARG A NH1 1 
ATOM   3123  N  NH2 A ARG A  1 375 ? -23.295 -18.796 6.731   0.50 41.03 ? 374 ARG A NH2 1 
ATOM   3124  N  NH2 B ARG A  1 375 ? -20.384 -20.653 10.353  0.50 37.45 ? 374 ARG A NH2 1 
ATOM   3125  N  N   . VAL A  1 376 ? -18.573 -18.112 7.390   1.00 24.51 ? 375 VAL A N   1 
ATOM   3126  C  CA  . VAL A  1 376 ? -18.754 -16.903 8.208   1.00 24.05 ? 375 VAL A CA  1 
ATOM   3127  C  C   . VAL A  1 376 ? -18.765 -15.652 7.311   1.00 24.85 ? 375 VAL A C   1 
ATOM   3128  O  O   . VAL A  1 376 ? -19.613 -14.772 7.468   1.00 23.56 ? 375 VAL A O   1 
ATOM   3129  C  CB  . VAL A  1 376 ? -17.661 -16.766 9.301   1.00 24.16 ? 375 VAL A CB  1 
ATOM   3130  C  CG1 . VAL A  1 376 ? -17.759 -15.432 10.028  1.00 24.17 ? 375 VAL A CG1 1 
ATOM   3131  C  CG2 . VAL A  1 376 ? -17.771 -17.885 10.320  1.00 24.88 ? 375 VAL A CG2 1 
ATOM   3132  N  N   . LEU A  1 377 ? -17.804 -15.564 6.383   1.00 22.87 ? 376 LEU A N   1 
ATOM   3133  C  CA  . LEU A  1 377 ? -17.633 -14.374 5.560   1.00 23.02 ? 376 LEU A CA  1 
ATOM   3134  C  C   . LEU A  1 377 ? -18.606 -14.235 4.380   1.00 25.77 ? 376 LEU A C   1 
ATOM   3135  O  O   . LEU A  1 377 ? -19.133 -13.145 4.137   1.00 25.49 ? 376 LEU A O   1 
ATOM   3136  C  CB  . LEU A  1 377 ? -16.210 -14.345 5.008   1.00 22.22 ? 376 LEU A CB  1 
ATOM   3137  C  CG  . LEU A  1 377 ? -15.107 -14.296 6.060   1.00 21.90 ? 376 LEU A CG  1 
ATOM   3138  C  CD1 . LEU A  1 377 ? -13.744 -14.232 5.389   1.00 21.88 ? 376 LEU A CD1 1 
ATOM   3139  C  CD2 . LEU A  1 377 ? -15.278 -13.091 6.993   1.00 21.97 ? 376 LEU A CD2 1 
ATOM   3140  N  N   . LEU A  1 378 ? -18.858 -15.346 3.679   1.00 27.71 ? 377 LEU A N   1 
ATOM   3141  C  CA  . LEU A  1 378 ? -19.597 -15.309 2.418   1.00 30.45 ? 377 LEU A CA  1 
ATOM   3142  C  C   . LEU A  1 378 ? -21.020 -15.831 2.561   1.00 33.19 ? 377 LEU A C   1 
ATOM   3143  O  O   . LEU A  1 378 ? -21.812 -15.666 1.652   1.00 34.36 ? 377 LEU A O   1 
ATOM   3144  C  CB  . LEU A  1 378 ? -18.871 -16.116 1.346   1.00 32.36 ? 377 LEU A CB  1 
ATOM   3145  C  CG  . LEU A  1 378 ? -17.723 -15.501 0.526   1.00 34.13 ? 377 LEU A CG  1 
ATOM   3146  C  CD1 . LEU A  1 378 ? -16.837 -14.566 1.312   1.00 33.60 ? 377 LEU A CD1 1 
ATOM   3147  C  CD2 . LEU A  1 378 ? -16.902 -16.609 -0.112  1.00 35.25 ? 377 LEU A CD2 1 
ATOM   3148  N  N   . GLY A  1 379 ? -21.352 -16.450 3.684   1.00 37.03 ? 378 GLY A N   1 
ATOM   3149  C  CA  . GLY A  1 379 ? -22.737 -16.830 3.962   1.00 44.02 ? 378 GLY A CA  1 
ATOM   3150  C  C   . GLY A  1 379 ? -23.042 -18.213 3.439   1.00 50.46 ? 378 GLY A C   1 
ATOM   3151  O  O   . GLY A  1 379 ? -22.141 -18.893 2.941   1.00 50.54 ? 378 GLY A O   1 
ATOM   3152  N  N   . PRO A  1 380 ? -24.323 -18.637 3.543   1.00 59.61 ? 379 PRO A N   1 
ATOM   3153  C  CA  . PRO A  1 380 ? -24.735 -20.013 3.247   1.00 64.63 ? 379 PRO A CA  1 
ATOM   3154  C  C   . PRO A  1 380 ? -24.636 -20.369 1.762   1.00 68.51 ? 379 PRO A C   1 
ATOM   3155  O  O   . PRO A  1 380 ? -24.653 -19.479 0.910   1.00 71.40 ? 379 PRO A O   1 
ATOM   3156  C  CB  . PRO A  1 380 ? -26.194 -20.058 3.730   1.00 66.12 ? 379 PRO A CB  1 
ATOM   3157  C  CG  . PRO A  1 380 ? -26.671 -18.643 3.672   1.00 64.73 ? 379 PRO A CG  1 
ATOM   3158  C  CD  . PRO A  1 380 ? -25.468 -17.776 3.911   1.00 62.24 ? 379 PRO A CD  1 
ATOM   3159  N  N   . HIS B  1 5   ? 15.388  15.756  5.951   1.00 40.40 ? 4   HIS B N   1 
ATOM   3160  C  CA  . HIS B  1 5   ? 13.900  15.979  5.988   1.00 37.29 ? 4   HIS B CA  1 
ATOM   3161  C  C   . HIS B  1 5   ? 13.316  15.301  7.249   1.00 30.87 ? 4   HIS B C   1 
ATOM   3162  O  O   . HIS B  1 5   ? 12.637  14.293  7.180   1.00 28.70 ? 4   HIS B O   1 
ATOM   3163  C  CB  . HIS B  1 5   ? 13.315  15.448  4.697   1.00 41.88 ? 4   HIS B CB  1 
ATOM   3164  C  CG  . HIS B  1 5   ? 11.865  15.741  4.506   1.00 41.97 ? 4   HIS B CG  1 
ATOM   3165  N  ND1 . HIS B  1 5   ? 11.400  16.654  3.584   1.00 43.32 ? 4   HIS B ND1 1 
ATOM   3166  C  CD2 . HIS B  1 5   ? 10.775  15.180  5.069   1.00 42.48 ? 4   HIS B CD2 1 
ATOM   3167  C  CE1 . HIS B  1 5   ? 10.081  16.647  3.600   1.00 43.36 ? 4   HIS B CE1 1 
ATOM   3168  N  NE2 . HIS B  1 5   ? 9.680   15.755  4.487   1.00 42.66 ? 4   HIS B NE2 1 
ATOM   3169  N  N   . PRO B  1 6   ? 13.648  15.823  8.429   1.00 26.06 ? 5   PRO B N   1 
ATOM   3170  C  CA  . PRO B  1 6   ? 13.217  15.108  9.634   1.00 23.57 ? 5   PRO B CA  1 
ATOM   3171  C  C   . PRO B  1 6   ? 11.741  15.369  9.927   1.00 21.21 ? 5   PRO B C   1 
ATOM   3172  O  O   . PRO B  1 6   ? 11.225  16.422  9.567   1.00 20.63 ? 5   PRO B O   1 
ATOM   3173  C  CB  . PRO B  1 6   ? 14.081  15.721  10.740  1.00 24.47 ? 5   PRO B CB  1 
ATOM   3174  C  CG  . PRO B  1 6   ? 14.312  17.111  10.264  1.00 25.93 ? 5   PRO B CG  1 
ATOM   3175  C  CD  . PRO B  1 6   ? 14.469  16.996  8.762   1.00 26.44 ? 5   PRO B CD  1 
ATOM   3176  N  N   . PRO B  1 7   ? 11.096  14.449  10.631  1.00 20.11 ? 6   PRO B N   1 
ATOM   3177  C  CA  . PRO B  1 7   ? 9.710   14.703  11.057  1.00 19.26 ? 6   PRO B CA  1 
ATOM   3178  C  C   . PRO B  1 7   ? 9.594   15.895  12.013  1.00 19.20 ? 6   PRO B C   1 
ATOM   3179  O  O   . PRO B  1 7   ? 10.529  16.194  12.785  1.00 18.74 ? 6   PRO B O   1 
ATOM   3180  C  CB  . PRO B  1 7   ? 9.290   13.415  11.750  1.00 19.86 ? 6   PRO B CB  1 
ATOM   3181  C  CG  . PRO B  1 7   ? 10.486  12.528  11.791  1.00 20.93 ? 6   PRO B CG  1 
ATOM   3182  C  CD  . PRO B  1 7   ? 11.662  13.198  11.181  1.00 20.49 ? 6   PRO B CD  1 
ATOM   3183  N  N   . VAL B  1 8   ? 8.452   16.579  11.945  1.00 18.34 ? 7   VAL B N   1 
ATOM   3184  C  CA  . VAL B  1 8   ? 8.256   17.815  12.661  1.00 18.30 ? 7   VAL B CA  1 
ATOM   3185  C  C   . VAL B  1 8   ? 6.973   17.750  13.468  1.00 17.20 ? 7   VAL B C   1 
ATOM   3186  O  O   . VAL B  1 8   ? 5.933   17.314  12.944  1.00 16.12 ? 7   VAL B O   1 
ATOM   3187  C  CB  . VAL B  1 8   ? 8.149   19.002  11.683  1.00 18.53 ? 7   VAL B CB  1 
ATOM   3188  C  CG1 . VAL B  1 8   ? 7.700   20.265  12.390  1.00 19.24 ? 7   VAL B CG1 1 
ATOM   3189  C  CG2 . VAL B  1 8   ? 9.475   19.253  11.003  1.00 20.17 ? 7   VAL B CG2 1 
ATOM   3190  N  N   . VAL B  1 9   ? 7.055   18.168  14.728  1.00 16.98 ? 8   VAL B N   1 
ATOM   3191  C  CA  . VAL B  1 9   ? 5.885   18.334  15.596  1.00 16.77 ? 8   VAL B CA  1 
ATOM   3192  C  C   . VAL B  1 9   ? 5.752   19.818  15.972  1.00 17.38 ? 8   VAL B C   1 
ATOM   3193  O  O   . VAL B  1 9   ? 6.712   20.447  16.436  1.00 16.74 ? 8   VAL B O   1 
ATOM   3194  C  CB  . VAL B  1 9   ? 5.986   17.468  16.870  1.00 16.85 ? 8   VAL B CB  1 
ATOM   3195  C  CG1 . VAL B  1 9   ? 4.861   17.789  17.835  1.00 16.83 ? 8   VAL B CG1 1 
ATOM   3196  C  CG2 . VAL B  1 9   ? 5.956   15.972  16.500  1.00 17.22 ? 8   VAL B CG2 1 
ATOM   3197  N  N   . LEU B  1 10  ? 4.543   20.341  15.779  1.00 16.46 ? 9   LEU B N   1 
ATOM   3198  C  CA  . LEU B  1 10  ? 4.230   21.754  16.045  1.00 17.12 ? 9   LEU B CA  1 
ATOM   3199  C  C   . LEU B  1 10  ? 3.464   21.889  17.357  1.00 16.76 ? 9   LEU B C   1 
ATOM   3200  O  O   . LEU B  1 10  ? 2.456   21.203  17.567  1.00 17.05 ? 9   LEU B O   1 
ATOM   3201  C  CB  . LEU B  1 10  ? 3.402   22.341  14.913  1.00 17.24 ? 9   LEU B CB  1 
ATOM   3202  C  CG  . LEU B  1 10  ? 3.951   22.154  13.497  1.00 18.80 ? 9   LEU B CG  1 
ATOM   3203  C  CD1 . LEU B  1 10  ? 2.930   22.658  12.469  1.00 19.37 ? 9   LEU B CD1 1 
ATOM   3204  C  CD2 . LEU B  1 10  ? 5.251   22.891  13.306  1.00 19.23 ? 9   LEU B CD2 1 
ATOM   3205  N  N   . VAL B  1 11  ? 3.930   22.790  18.230  1.00 16.45 ? 10  VAL B N   1 
ATOM   3206  C  CA  . VAL B  1 11  ? 3.331   23.013  19.546  1.00 15.92 ? 10  VAL B CA  1 
ATOM   3207  C  C   . VAL B  1 11  ? 2.893   24.485  19.661  1.00 16.13 ? 10  VAL B C   1 
ATOM   3208  O  O   . VAL B  1 11  ? 3.737   25.389  19.601  1.00 15.26 ? 10  VAL B O   1 
ATOM   3209  C  CB  . VAL B  1 11  ? 4.312   22.678  20.700  1.00 16.50 ? 10  VAL B CB  1 
ATOM   3210  C  CG1 . VAL B  1 11  ? 3.598   22.774  22.037  1.00 16.23 ? 10  VAL B CG1 1 
ATOM   3211  C  CG2 . VAL B  1 11  ? 4.917   21.280  20.518  1.00 17.03 ? 10  VAL B CG2 1 
ATOM   3212  N  N   . PRO B  1 12  ? 1.577   24.724  19.777  1.00 15.83 ? 11  PRO B N   1 
ATOM   3213  C  CA  . PRO B  1 12  ? 1.055   26.079  19.766  1.00 15.93 ? 11  PRO B CA  1 
ATOM   3214  C  C   . PRO B  1 12  ? 1.122   26.766  21.118  1.00 15.67 ? 11  PRO B C   1 
ATOM   3215  O  O   . PRO B  1 12  ? 1.401   26.138  22.121  1.00 16.02 ? 11  PRO B O   1 
ATOM   3216  C  CB  . PRO B  1 12  ? -0.422  25.869  19.404  1.00 16.24 ? 11  PRO B CB  1 
ATOM   3217  C  CG  . PRO B  1 12  ? -0.764  24.562  20.026  1.00 16.17 ? 11  PRO B CG  1 
ATOM   3218  C  CD  . PRO B  1 12  ? 0.490   23.726  19.868  1.00 15.99 ? 11  PRO B CD  1 
ATOM   3219  N  N   . GLY B  1 13  ? 0.842   28.070  21.123  1.00 16.69 ? 12  GLY B N   1 
ATOM   3220  C  CA  . GLY B  1 13  ? 0.770   28.835  22.366  1.00 16.68 ? 12  GLY B CA  1 
ATOM   3221  C  C   . GLY B  1 13  ? -0.659  28.971  22.881  1.00 17.78 ? 12  GLY B C   1 
ATOM   3222  O  O   . GLY B  1 13  ? -1.586  28.267  22.447  1.00 17.63 ? 12  GLY B O   1 
ATOM   3223  N  N   . ASP B  1 14  ? -0.830  29.893  23.825  1.00 19.12 ? 13  ASP B N   1 
ATOM   3224  C  CA  . ASP B  1 14  ? -2.127  30.190  24.414  1.00 18.34 ? 13  ASP B CA  1 
ATOM   3225  C  C   . ASP B  1 14  ? -3.101  30.694  23.342  1.00 19.77 ? 13  ASP B C   1 
ATOM   3226  O  O   . ASP B  1 14  ? -2.724  31.454  22.446  1.00 20.59 ? 13  ASP B O   1 
ATOM   3227  C  CB  . ASP B  1 14  ? -1.920  31.234  25.525  1.00 19.58 ? 13  ASP B CB  1 
ATOM   3228  C  CG  . ASP B  1 14  ? -3.048  31.263  26.565  1.00 20.44 ? 13  ASP B CG  1 
ATOM   3229  O  OD1 . ASP B  1 14  ? -4.082  30.549  26.448  1.00 20.39 ? 13  ASP B OD1 1 
ATOM   3230  O  OD2 . ASP B  1 14  ? -2.870  32.045  27.542  1.00 20.77 ? 13  ASP B OD2 1 
ATOM   3231  N  N   . LEU B  1 15  ? -4.348  30.232  23.392  1.00 19.46 ? 14  LEU B N   1 
ATOM   3232  C  CA  . LEU B  1 15  ? -5.341  30.500  22.348  1.00 19.70 ? 14  LEU B CA  1 
ATOM   3233  C  C   . LEU B  1 15  ? -5.005  29.871  20.999  1.00 18.67 ? 14  LEU B C   1 
ATOM   3234  O  O   . LEU B  1 15  ? -5.664  30.178  20.004  1.00 18.79 ? 14  LEU B O   1 
ATOM   3235  C  CB  . LEU B  1 15  ? -5.558  32.006  22.149  1.00 20.95 ? 14  LEU B CB  1 
ATOM   3236  C  CG  . LEU B  1 15  ? -5.777  32.886  23.386  1.00 22.62 ? 14  LEU B CG  1 
ATOM   3237  C  CD1 . LEU B  1 15  ? -6.008  34.326  22.946  1.00 23.95 ? 14  LEU B CD1 1 
ATOM   3238  C  CD2 . LEU B  1 15  ? -6.963  32.380  24.172  1.00 23.21 ? 14  LEU B CD2 1 
ATOM   3239  N  N   . GLY B  1 16  ? -4.004  28.990  20.963  1.00 18.09 ? 15  GLY B N   1 
ATOM   3240  C  CA  . GLY B  1 16  ? -3.334  28.616  19.720  1.00 17.41 ? 15  GLY B CA  1 
ATOM   3241  C  C   . GLY B  1 16  ? -3.826  27.368  19.031  1.00 17.53 ? 15  GLY B C   1 
ATOM   3242  O  O   . GLY B  1 16  ? -3.227  26.913  18.064  1.00 17.08 ? 15  GLY B O   1 
ATOM   3243  N  N   . ASN B  1 17  ? -4.966  26.835  19.468  1.00 17.68 ? 16  ASN B N   1 
ATOM   3244  C  CA  . ASN B  1 17  ? -5.638  25.815  18.700  1.00 17.50 ? 16  ASN B CA  1 
ATOM   3245  C  C   . ASN B  1 17  ? -7.130  25.834  18.967  1.00 18.34 ? 16  ASN B C   1 
ATOM   3246  O  O   . ASN B  1 17  ? -7.600  26.363  19.985  1.00 17.74 ? 16  ASN B O   1 
ATOM   3247  C  CB  . ASN B  1 17  ? -5.037  24.409  18.926  1.00 17.06 ? 16  ASN B CB  1 
ATOM   3248  C  CG  . ASN B  1 17  ? -4.937  24.015  20.399  1.00 16.83 ? 16  ASN B CG  1 
ATOM   3249  O  OD1 . ASN B  1 17  ? -3.831  23.882  20.938  1.00 16.57 ? 16  ASN B OD1 1 
ATOM   3250  N  ND2 . ASN B  1 17  ? -6.078  23.739  21.030  1.00 16.04 ? 16  ASN B ND2 1 
ATOM   3251  N  N   . GLN B  1 18  ? -7.869  25.252  18.039  1.00 18.74 ? 17  GLN B N   1 
ATOM   3252  C  CA  . GLN B  1 18  ? -9.330  25.160  18.201  1.00 20.34 ? 17  GLN B CA  1 
ATOM   3253  C  C   . GLN B  1 18  ? -9.689  24.383  19.481  1.00 19.73 ? 17  GLN B C   1 
ATOM   3254  O  O   . GLN B  1 18  ? -8.961  23.486  19.890  1.00 18.58 ? 17  GLN B O   1 
ATOM   3255  C  CB  . GLN B  1 18  ? -9.958  24.462  17.007  1.00 21.27 ? 17  GLN B CB  1 
ATOM   3256  C  CG  . GLN B  1 18  ? -9.794  25.204  15.692  1.00 23.46 ? 17  GLN B CG  1 
ATOM   3257  C  CD  . GLN B  1 18  ? -10.399 24.469  14.516  1.00 24.85 ? 17  GLN B CD  1 
ATOM   3258  O  OE1 . GLN B  1 18  ? -11.238 23.564  14.675  1.00 25.57 ? 17  GLN B OE1 1 
ATOM   3259  N  NE2 . GLN B  1 18  ? -9.931  24.815  13.318  1.00 25.58 ? 17  GLN B NE2 1 
ATOM   3260  N  N   . LEU B  1 19  ? -10.842 24.716  20.063  1.00 20.89 ? 18  LEU B N   1 
ATOM   3261  C  CA  . LEU B  1 19  ? -11.472 23.917  21.112  1.00 21.62 ? 18  LEU B CA  1 
ATOM   3262  C  C   . LEU B  1 19  ? -12.935 23.707  20.748  1.00 22.49 ? 18  LEU B C   1 
ATOM   3263  O  O   . LEU B  1 19  ? -13.566 24.587  20.137  1.00 22.28 ? 18  LEU B O   1 
ATOM   3264  C  CB  . LEU B  1 19  ? -11.406 24.610  22.474  1.00 21.98 ? 18  LEU B CB  1 
ATOM   3265  C  CG  . LEU B  1 19  ? -10.022 24.858  23.092  1.00 21.89 ? 18  LEU B CG  1 
ATOM   3266  C  CD1 . LEU B  1 19  ? -10.185 25.601  24.413  1.00 23.00 ? 18  LEU B CD1 1 
ATOM   3267  C  CD2 . LEU B  1 19  ? -9.285  23.552  23.320  1.00 21.37 ? 18  LEU B CD2 1 
ATOM   3268  N  N   . GLU B  1 20  ? -13.463 22.544  21.120  1.00 22.93 ? 19  GLU B N   1 
ATOM   3269  C  CA  . GLU B  1 20  ? -14.860 22.190  20.846  1.00 24.59 ? 19  GLU B CA  1 
ATOM   3270  C  C   . GLU B  1 20  ? -15.591 21.878  22.144  1.00 24.88 ? 19  GLU B C   1 
ATOM   3271  O  O   . GLU B  1 20  ? -14.988 21.388  23.088  1.00 24.23 ? 19  GLU B O   1 
ATOM   3272  C  CB  . GLU B  1 20  ? -14.924 20.955  19.937  1.00 27.69 ? 19  GLU B CB  1 
ATOM   3273  C  CG  . GLU B  1 20  ? -14.490 21.248  18.519  1.00 29.81 ? 19  GLU B CG  1 
ATOM   3274  C  CD  . GLU B  1 20  ? -14.394 20.016  17.636  1.00 33.63 ? 19  GLU B CD  1 
ATOM   3275  O  OE1 . GLU B  1 20  ? -14.496 18.862  18.137  1.00 33.74 ? 19  GLU B OE1 1 
ATOM   3276  O  OE2 . GLU B  1 20  ? -14.189 20.226  16.423  1.00 37.70 ? 19  GLU B OE2 1 
ATOM   3277  N  N   . ALA B  1 21  ? -16.888 22.156  22.188  1.00 25.22 ? 20  ALA B N   1 
ATOM   3278  C  CA  . ALA B  1 21  ? -17.681 21.902  23.367  1.00 26.13 ? 20  ALA B CA  1 
ATOM   3279  C  C   . ALA B  1 21  ? -18.973 21.170  23.024  1.00 26.99 ? 20  ALA B C   1 
ATOM   3280  O  O   . ALA B  1 21  ? -19.515 21.325  21.940  1.00 27.06 ? 20  ALA B O   1 
ATOM   3281  C  CB  . ALA B  1 21  ? -18.016 23.209  24.086  1.00 26.58 ? 20  ALA B CB  1 
ATOM   3282  N  N   . LYS B  1 22  ? -19.466 20.410  23.995  1.00 29.17 ? 21  LYS B N   1 
ATOM   3283  C  CA  . LYS B  1 22  ? -20.804 19.800  23.927  1.00 31.90 ? 21  LYS B CA  1 
ATOM   3284  C  C   . LYS B  1 22  ? -21.517 20.102  25.238  1.00 32.27 ? 21  LYS B C   1 
ATOM   3285  O  O   . LYS B  1 22  ? -20.911 20.052  26.304  1.00 31.07 ? 21  LYS B O   1 
ATOM   3286  C  CB  . LYS B  1 22  ? -20.691 18.293  23.688  1.00 33.43 ? 21  LYS B CB  1 
ATOM   3287  C  CG  . LYS B  1 22  ? -22.039 17.576  23.587  1.00 36.25 ? 21  LYS B CG  1 
ATOM   3288  C  CD  . LYS B  1 22  ? -21.859 16.105  23.249  1.00 38.65 ? 21  LYS B CD  1 
ATOM   3289  C  CE  . LYS B  1 22  ? -23.208 15.427  23.033  1.00 42.95 ? 21  LYS B CE  1 
ATOM   3290  N  NZ  . LYS B  1 22  ? -23.031 14.093  22.405  1.00 45.22 ? 21  LYS B NZ  1 
ATOM   3291  N  N   . LEU B  1 23  ? -22.808 20.389  25.159  1.00 33.11 ? 22  LEU B N   1 
ATOM   3292  C  CA  . LEU B  1 23  ? -23.549 20.906  26.291  1.00 34.15 ? 22  LEU B CA  1 
ATOM   3293  C  C   . LEU B  1 23  ? -24.738 20.030  26.688  1.00 36.11 ? 22  LEU B C   1 
ATOM   3294  O  O   . LEU B  1 23  ? -25.447 19.515  25.827  1.00 37.95 ? 22  LEU B O   1 
ATOM   3295  C  CB  . LEU B  1 23  ? -24.093 22.295  25.959  1.00 33.93 ? 22  LEU B CB  1 
ATOM   3296  C  CG  . LEU B  1 23  ? -23.123 23.305  25.355  1.00 33.19 ? 22  LEU B CG  1 
ATOM   3297  C  CD1 . LEU B  1 23  ? -23.864 24.594  25.047  1.00 33.67 ? 22  LEU B CD1 1 
ATOM   3298  C  CD2 . LEU B  1 23  ? -21.938 23.549  26.283  1.00 31.38 ? 22  LEU B CD2 1 
ATOM   3299  N  N   . ASP B  1 24  ? -24.942 19.903  27.998  1.00 36.91 ? 23  ASP B N   1 
ATOM   3300  C  CA  . ASP B  1 24  ? -26.218 19.434  28.587  1.00 38.76 ? 23  ASP B CA  1 
ATOM   3301  C  C   . ASP B  1 24  ? -26.338 20.090  29.966  1.00 38.44 ? 23  ASP B C   1 
ATOM   3302  O  O   . ASP B  1 24  ? -26.187 19.443  30.999  1.00 38.54 ? 23  ASP B O   1 
ATOM   3303  C  CB  . ASP B  1 24  ? -26.238 17.902  28.678  1.00 39.67 ? 23  ASP B CB  1 
ATOM   3304  C  CG  . ASP B  1 24  ? -27.606 17.350  29.072  1.00 42.68 ? 23  ASP B CG  1 
ATOM   3305  O  OD1 . ASP B  1 24  ? -28.585 18.128  29.178  1.00 43.48 ? 23  ASP B OD1 1 
ATOM   3306  O  OD2 . ASP B  1 24  ? -27.703 16.120  29.258  1.00 44.99 ? 23  ASP B OD2 1 
ATOM   3307  N  N   . LYS B  1 25  ? -26.569 21.401  29.965  1.00 37.97 ? 24  LYS B N   1 
ATOM   3308  C  CA  . LYS B  1 25  ? -26.433 22.226  31.160  1.00 37.65 ? 24  LYS B CA  1 
ATOM   3309  C  C   . LYS B  1 25  ? -27.745 22.258  31.939  1.00 40.54 ? 24  LYS B C   1 
ATOM   3310  O  O   . LYS B  1 25  ? -28.806 22.308  31.332  1.00 40.16 ? 24  LYS B O   1 
ATOM   3311  C  CB  . LYS B  1 25  ? -26.065 23.657  30.764  1.00 36.56 ? 24  LYS B CB  1 
ATOM   3312  C  CG  . LYS B  1 25  ? -24.743 23.778  30.003  1.00 35.26 ? 24  LYS B CG  1 
ATOM   3313  C  CD  . LYS B  1 25  ? -24.666 25.076  29.208  1.00 35.98 ? 24  LYS B CD  1 
ATOM   3314  C  CE  . LYS B  1 25  ? -24.533 26.319  30.076  1.00 35.65 ? 24  LYS B CE  1 
ATOM   3315  N  NZ  . LYS B  1 25  ? -23.201 26.483  30.705  1.00 35.75 ? 24  LYS B NZ  1 
ATOM   3316  N  N   . PRO B  1 26  ? -27.673 22.273  33.280  1.00 41.91 ? 25  PRO B N   1 
ATOM   3317  C  CA  . PRO B  1 26  ? -28.903 22.404  34.064  1.00 44.12 ? 25  PRO B CA  1 
ATOM   3318  C  C   . PRO B  1 26  ? -29.539 23.793  33.980  1.00 45.09 ? 25  PRO B C   1 
ATOM   3319  O  O   . PRO B  1 26  ? -30.764 23.905  34.035  1.00 43.14 ? 25  PRO B O   1 
ATOM   3320  C  CB  . PRO B  1 26  ? -28.452 22.103  35.498  1.00 44.46 ? 25  PRO B CB  1 
ATOM   3321  C  CG  . PRO B  1 26  ? -26.987 22.309  35.507  1.00 43.13 ? 25  PRO B CG  1 
ATOM   3322  C  CD  . PRO B  1 26  ? -26.492 22.030  34.125  1.00 41.40 ? 25  PRO B CD  1 
ATOM   3323  N  N   . THR B  1 27  ? -28.719 24.832  33.854  1.00 43.77 ? 26  THR B N   1 
ATOM   3324  C  CA  . THR B  1 27  ? -29.208 26.213  33.750  1.00 46.18 ? 26  THR B CA  1 
ATOM   3325  C  C   . THR B  1 27  ? -28.351 27.018  32.781  1.00 45.45 ? 26  THR B C   1 
ATOM   3326  O  O   . THR B  1 27  ? -27.191 26.654  32.522  1.00 43.30 ? 26  THR B O   1 
ATOM   3327  C  CB  . THR B  1 27  ? -29.172 26.939  35.117  1.00 47.63 ? 26  THR B CB  1 
ATOM   3328  O  OG1 . THR B  1 27  ? -27.823 27.021  35.587  1.00 48.74 ? 26  THR B OG1 1 
ATOM   3329  C  CG2 . THR B  1 27  ? -29.998 26.215  36.149  1.00 49.33 ? 26  THR B CG2 1 
ATOM   3330  N  N   . VAL B  1 28  ? -28.907 28.118  32.270  1.00 45.00 ? 27  VAL B N   1 
ATOM   3331  C  CA  . VAL B  1 28  ? -28.136 29.068  31.452  1.00 45.61 ? 27  VAL B CA  1 
ATOM   3332  C  C   . VAL B  1 28  ? -28.259 30.491  32.003  1.00 46.91 ? 27  VAL B C   1 
ATOM   3333  O  O   . VAL B  1 28  ? -29.201 30.801  32.718  1.00 48.13 ? 27  VAL B O   1 
ATOM   3334  C  CB  . VAL B  1 28  ? -28.572 29.055  29.971  1.00 45.87 ? 27  VAL B CB  1 
ATOM   3335  C  CG1 . VAL B  1 28  ? -28.085 27.784  29.283  1.00 46.03 ? 27  VAL B CG1 1 
ATOM   3336  C  CG2 . VAL B  1 28  ? -30.083 29.211  29.829  1.00 46.36 ? 27  VAL B CG2 1 
ATOM   3337  N  N   . VAL B  1 29  ? -27.310 31.356  31.661  1.00 46.30 ? 28  VAL B N   1 
ATOM   3338  C  CA  . VAL B  1 29  ? -27.311 32.735  32.159  1.00 46.46 ? 28  VAL B CA  1 
ATOM   3339  C  C   . VAL B  1 29  ? -28.271 33.685  31.411  1.00 48.63 ? 28  VAL B C   1 
ATOM   3340  O  O   . VAL B  1 29  ? -28.677 34.691  31.974  1.00 51.64 ? 28  VAL B O   1 
ATOM   3341  C  CB  . VAL B  1 29  ? -25.883 33.335  32.205  1.00 45.81 ? 28  VAL B CB  1 
ATOM   3342  C  CG1 . VAL B  1 29  ? -24.976 32.482  33.088  1.00 44.98 ? 28  VAL B CG1 1 
ATOM   3343  C  CG2 . VAL B  1 29  ? -25.279 33.482  30.816  1.00 46.10 ? 28  VAL B CG2 1 
ATOM   3344  N  N   . HIS B  1 30  ? -28.589 33.385  30.154  1.00 49.23 ? 29  HIS B N   1 
ATOM   3345  C  CA  . HIS B  1 30  ? -29.594 34.111  29.368  1.00 51.64 ? 29  HIS B CA  1 
ATOM   3346  C  C   . HIS B  1 30  ? -30.421 33.099  28.583  1.00 54.12 ? 29  HIS B C   1 
ATOM   3347  O  O   . HIS B  1 30  ? -29.908 32.026  28.217  1.00 52.26 ? 29  HIS B O   1 
ATOM   3348  C  CB  . HIS B  1 30  ? -28.968 35.073  28.343  1.00 50.86 ? 29  HIS B CB  1 
ATOM   3349  C  CG  . HIS B  1 30  ? -28.051 36.095  28.929  1.00 50.61 ? 29  HIS B CG  1 
ATOM   3350  N  ND1 . HIS B  1 30  ? -28.436 36.955  29.934  1.00 51.21 ? 29  HIS B ND1 1 
ATOM   3351  C  CD2 . HIS B  1 30  ? -26.764 36.409  28.638  1.00 48.68 ? 29  HIS B CD2 1 
ATOM   3352  C  CE1 . HIS B  1 30  ? -27.420 37.739  30.255  1.00 50.76 ? 29  HIS B CE1 1 
ATOM   3353  N  NE2 . HIS B  1 30  ? -26.391 37.424  29.487  1.00 49.14 ? 29  HIS B NE2 1 
ATOM   3354  N  N   . TYR B  1 31  ? -31.680 33.455  28.301  1.00 57.20 ? 30  TYR B N   1 
ATOM   3355  C  CA  . TYR B  1 31  ? -32.580 32.607  27.507  1.00 59.09 ? 30  TYR B CA  1 
ATOM   3356  C  C   . TYR B  1 31  ? -32.032 32.330  26.111  1.00 57.91 ? 30  TYR B C   1 
ATOM   3357  O  O   . TYR B  1 31  ? -32.281 31.266  25.545  1.00 58.75 ? 30  TYR B O   1 
ATOM   3358  C  CB  . TYR B  1 31  ? -34.007 33.224  27.365  1.00 64.09 ? 30  TYR B CB  1 
ATOM   3359  C  CG  . TYR B  1 31  ? -34.971 33.005  28.506  1.00 66.11 ? 30  TYR B CG  1 
ATOM   3360  C  CD1 . TYR B  1 31  ? -35.570 31.762  28.700  1.00 66.55 ? 30  TYR B CD1 1 
ATOM   3361  C  CD2 . TYR B  1 31  ? -35.348 34.061  29.351  1.00 68.51 ? 30  TYR B CD2 1 
ATOM   3362  C  CE1 . TYR B  1 31  ? -36.479 31.561  29.729  1.00 68.29 ? 30  TYR B CE1 1 
ATOM   3363  C  CE2 . TYR B  1 31  ? -36.261 33.872  30.380  1.00 68.84 ? 30  TYR B CE2 1 
ATOM   3364  C  CZ  . TYR B  1 31  ? -36.820 32.624  30.568  1.00 68.76 ? 30  TYR B CZ  1 
ATOM   3365  O  OH  . TYR B  1 31  ? -37.720 32.437  31.594  1.00 71.37 ? 30  TYR B OH  1 
ATOM   3366  N  N   . LEU B  1 32  ? -31.243 33.248  25.562  1.00 58.16 ? 31  LEU B N   1 
ATOM   3367  C  CA  . LEU B  1 32  ? -30.665 33.019  24.232  1.00 58.62 ? 31  LEU B CA  1 
ATOM   3368  C  C   . LEU B  1 32  ? -29.476 32.025  24.223  1.00 54.83 ? 31  LEU B C   1 
ATOM   3369  O  O   . LEU B  1 32  ? -29.016 31.645  23.151  1.00 54.55 ? 31  LEU B O   1 
ATOM   3370  C  CB  . LEU B  1 32  ? -30.304 34.344  23.539  1.00 60.35 ? 31  LEU B CB  1 
ATOM   3371  C  CG  . LEU B  1 32  ? -29.442 35.378  24.270  1.00 62.04 ? 31  LEU B CG  1 
ATOM   3372  C  CD1 . LEU B  1 32  ? -28.000 34.901  24.373  1.00 61.99 ? 31  LEU B CD1 1 
ATOM   3373  C  CD2 . LEU B  1 32  ? -29.511 36.725  23.573  1.00 63.32 ? 31  LEU B CD2 1 
ATOM   3374  N  N   . CYS B  1 33  ? -28.997 31.590  25.391  1.00 52.09 ? 32  CYS B N   1 
ATOM   3375  C  CA  . CYS B  1 33  ? -27.911 30.586  25.462  1.00 50.77 ? 32  CYS B CA  1 
ATOM   3376  C  C   . CYS B  1 33  ? -28.470 29.166  25.269  1.00 50.35 ? 32  CYS B C   1 
ATOM   3377  O  O   . CYS B  1 33  ? -29.477 28.818  25.876  1.00 52.49 ? 32  CYS B O   1 
ATOM   3378  C  CB  . CYS B  1 33  ? -27.193 30.630  26.825  1.00 49.09 ? 32  CYS B CB  1 
ATOM   3379  S  SG  . CYS B  1 33  ? -26.522 32.210  27.416  1.00 50.51 ? 32  CYS B SG  1 
ATOM   3380  N  N   . SER B  1 34  ? -27.813 28.335  24.461  1.00 48.59 ? 33  SER B N   1 
ATOM   3381  C  CA  . SER B  1 34  ? -28.228 26.931  24.334  1.00 48.34 ? 33  SER B CA  1 
ATOM   3382  C  C   . SER B  1 34  ? -27.930 26.142  25.616  1.00 46.12 ? 33  SER B C   1 
ATOM   3383  O  O   . SER B  1 34  ? -26.839 26.246  26.188  1.00 43.45 ? 33  SER B O   1 
ATOM   3384  C  CB  . SER B  1 34  ? -27.522 26.253  23.168  1.00 49.50 ? 33  SER B CB  1 
ATOM   3385  O  OG  . SER B  1 34  ? -27.874 26.831  21.924  1.00 52.08 ? 33  SER B OG  1 
ATOM   3386  N  N   . LYS B  1 35  ? -28.905 25.355  26.053  1.00 45.17 ? 34  LYS B N   1 
ATOM   3387  C  CA  . LYS B  1 35  ? -28.745 24.442  27.187  1.00 44.66 ? 34  LYS B CA  1 
ATOM   3388  C  C   . LYS B  1 35  ? -28.109 23.132  26.781  1.00 43.29 ? 34  LYS B C   1 
ATOM   3389  O  O   . LYS B  1 35  ? -27.355 22.531  27.542  1.00 42.79 ? 34  LYS B O   1 
ATOM   3390  C  CB  . LYS B  1 35  ? -30.102 24.090  27.799  1.00 47.39 ? 34  LYS B CB  1 
ATOM   3391  C  CG  . LYS B  1 35  ? -30.427 24.827  29.066  1.00 48.43 ? 34  LYS B CG  1 
ATOM   3392  C  CD  . LYS B  1 35  ? -31.727 24.308  29.659  1.00 49.94 ? 34  LYS B CD  1 
ATOM   3393  C  CE  . LYS B  1 35  ? -31.752 24.587  31.138  1.00 51.17 ? 34  LYS B CE  1 
ATOM   3394  N  NZ  . LYS B  1 35  ? -33.076 24.248  31.733  1.00 52.88 ? 34  LYS B NZ  1 
ATOM   3395  N  N   . LYS B  1 36  ? -28.437 22.677  25.584  1.00 43.29 ? 35  LYS B N   1 
ATOM   3396  C  CA  . LYS B  1 36  ? -28.109 21.336  25.165  1.00 44.38 ? 35  LYS B CA  1 
ATOM   3397  C  C   . LYS B  1 36  ? -27.731 21.351  23.695  1.00 44.52 ? 35  LYS B C   1 
ATOM   3398  O  O   . LYS B  1 36  ? -28.372 22.024  22.891  1.00 46.75 ? 35  LYS B O   1 
ATOM   3399  C  CB  . LYS B  1 36  ? -29.329 20.440  25.380  1.00 47.91 ? 35  LYS B CB  1 
ATOM   3400  C  CG  . LYS B  1 36  ? -29.069 18.958  25.215  1.00 49.48 ? 35  LYS B CG  1 
ATOM   3401  C  CD  . LYS B  1 36  ? -30.350 18.180  25.483  1.00 53.92 ? 35  LYS B CD  1 
ATOM   3402  C  CE  . LYS B  1 36  ? -30.235 16.733  25.077  1.00 55.47 ? 35  LYS B CE  1 
ATOM   3403  N  NZ  . LYS B  1 36  ? -29.204 16.008  25.863  1.00 56.41 ? 35  LYS B NZ  1 
ATOM   3404  N  N   . THR B  1 37  ? -26.691 20.609  23.344  1.00 41.45 ? 36  THR B N   1 
ATOM   3405  C  CA  . THR B  1 37  ? -26.350 20.390  21.938  1.00 42.27 ? 36  THR B CA  1 
ATOM   3406  C  C   . THR B  1 37  ? -26.234 18.894  21.707  1.00 44.46 ? 36  THR B C   1 
ATOM   3407  O  O   . THR B  1 37  ? -25.787 18.160  22.588  1.00 43.30 ? 36  THR B O   1 
ATOM   3408  C  CB  . THR B  1 37  ? -25.017 21.085  21.541  1.00 39.03 ? 36  THR B CB  1 
ATOM   3409  O  OG1 . THR B  1 37  ? -23.931 20.518  22.287  1.00 36.33 ? 36  THR B OG1 1 
ATOM   3410  C  CG2 . THR B  1 37  ? -25.093 22.580  21.809  1.00 38.74 ? 36  THR B CG2 1 
ATOM   3411  N  N   . GLU B  1 38  ? -26.624 18.443  20.520  1.00 49.14 ? 37  GLU B N   1 
ATOM   3412  C  CA  . GLU B  1 38  ? -26.530 17.016  20.183  1.00 52.75 ? 37  GLU B CA  1 
ATOM   3413  C  C   . GLU B  1 38  ? -25.118 16.589  19.807  1.00 48.46 ? 37  GLU B C   1 
ATOM   3414  O  O   . GLU B  1 38  ? -24.773 15.412  19.919  1.00 49.20 ? 37  GLU B O   1 
ATOM   3415  C  CB  . GLU B  1 38  ? -27.510 16.664  19.059  1.00 57.49 ? 37  GLU B CB  1 
ATOM   3416  C  CG  . GLU B  1 38  ? -28.960 16.966  19.416  1.00 65.12 ? 37  GLU B CG  1 
ATOM   3417  C  CD  . GLU B  1 38  ? -29.429 16.265  20.694  1.00 71.34 ? 37  GLU B CD  1 
ATOM   3418  O  OE1 . GLU B  1 38  ? -29.046 15.088  20.911  1.00 76.92 ? 37  GLU B OE1 1 
ATOM   3419  O  OE2 . GLU B  1 38  ? -30.177 16.890  21.489  1.00 75.33 ? 37  GLU B OE2 1 
ATOM   3420  N  N   . SER B  1 39  ? -24.287 17.537  19.392  1.00 45.73 ? 38  SER B N   1 
ATOM   3421  C  CA  . SER B  1 39  ? -22.888 17.234  19.070  1.00 43.20 ? 38  SER B CA  1 
ATOM   3422  C  C   . SER B  1 39  ? -21.977 18.357  19.532  1.00 39.30 ? 38  SER B C   1 
ATOM   3423  O  O   . SER B  1 39  ? -22.430 19.348  20.106  1.00 38.42 ? 38  SER B O   1 
ATOM   3424  C  CB  . SER B  1 39  ? -22.735 17.029  17.571  1.00 46.14 ? 38  SER B CB  1 
ATOM   3425  O  OG  . SER B  1 39  ? -23.150 18.200  16.897  1.00 49.12 ? 38  SER B OG  1 
ATOM   3426  N  N   . TYR B  1 40  ? -20.682 18.171  19.325  1.00 36.77 ? 39  TYR B N   1 
ATOM   3427  C  CA  . TYR B  1 40  ? -19.698 19.190  19.642  1.00 34.80 ? 39  TYR B CA  1 
ATOM   3428  C  C   . TYR B  1 40  ? -19.781 20.327  18.633  1.00 35.50 ? 39  TYR B C   1 
ATOM   3429  O  O   . TYR B  1 40  ? -20.127 20.105  17.473  1.00 36.22 ? 39  TYR B O   1 
ATOM   3430  C  CB  . TYR B  1 40  ? -18.291 18.600  19.662  1.00 33.29 ? 39  TYR B CB  1 
ATOM   3431  C  CG  . TYR B  1 40  ? -18.021 17.773  20.891  1.00 33.02 ? 39  TYR B CG  1 
ATOM   3432  C  CD1 . TYR B  1 40  ? -18.420 16.437  20.957  1.00 34.83 ? 39  TYR B CD1 1 
ATOM   3433  C  CD2 . TYR B  1 40  ? -17.399 18.326  22.001  1.00 31.88 ? 39  TYR B CD2 1 
ATOM   3434  C  CE1 . TYR B  1 40  ? -18.185 15.680  22.097  1.00 34.52 ? 39  TYR B CE1 1 
ATOM   3435  C  CE2 . TYR B  1 40  ? -17.167 17.578  23.141  1.00 32.22 ? 39  TYR B CE2 1 
ATOM   3436  C  CZ  . TYR B  1 40  ? -17.565 16.258  23.178  1.00 34.08 ? 39  TYR B CZ  1 
ATOM   3437  O  OH  . TYR B  1 40  ? -17.318 15.518  24.301  1.00 35.51 ? 39  TYR B OH  1 
ATOM   3438  N  N   . PHE B  1 41  ? -19.517 21.547  19.093  1.00 33.12 ? 40  PHE B N   1 
ATOM   3439  C  CA  . PHE B  1 41  ? -19.428 22.708  18.220  1.00 32.11 ? 40  PHE B CA  1 
ATOM   3440  C  C   . PHE B  1 41  ? -18.149 23.441  18.559  1.00 29.83 ? 40  PHE B C   1 
ATOM   3441  O  O   . PHE B  1 41  ? -17.595 23.255  19.653  1.00 27.68 ? 40  PHE B O   1 
ATOM   3442  C  CB  . PHE B  1 41  ? -20.642 23.632  18.388  1.00 33.01 ? 40  PHE B CB  1 
ATOM   3443  C  CG  . PHE B  1 41  ? -20.748 24.281  19.747  1.00 33.48 ? 40  PHE B CG  1 
ATOM   3444  C  CD1 . PHE B  1 41  ? -21.340 23.609  20.815  1.00 34.11 ? 40  PHE B CD1 1 
ATOM   3445  C  CD2 . PHE B  1 41  ? -20.291 25.582  19.955  1.00 32.54 ? 40  PHE B CD2 1 
ATOM   3446  C  CE1 . PHE B  1 41  ? -21.444 24.197  22.064  1.00 33.91 ? 40  PHE B CE1 1 
ATOM   3447  C  CE2 . PHE B  1 41  ? -20.377 26.169  21.203  1.00 32.89 ? 40  PHE B CE2 1 
ATOM   3448  C  CZ  . PHE B  1 41  ? -20.963 25.481  22.265  1.00 33.80 ? 40  PHE B CZ  1 
ATOM   3449  N  N   . THR B  1 42  ? -17.684 24.283  17.643  1.00 28.90 ? 41  THR B N   1 
ATOM   3450  C  CA  . THR B  1 42  ? -16.441 25.034  17.878  1.00 27.67 ? 41  THR B CA  1 
ATOM   3451  C  C   . THR B  1 42  ? -16.681 26.170  18.869  1.00 27.87 ? 41  THR B C   1 
ATOM   3452  O  O   . THR B  1 42  ? -17.475 27.080  18.608  1.00 28.88 ? 41  THR B O   1 
ATOM   3453  C  CB  . THR B  1 42  ? -15.879 25.577  16.543  1.00 27.65 ? 41  THR B CB  1 
ATOM   3454  O  OG1 . THR B  1 42  ? -15.618 24.471  15.673  1.00 26.79 ? 41  THR B OG1 1 
ATOM   3455  C  CG2 . THR B  1 42  ? -14.592 26.369  16.765  1.00 27.04 ? 41  THR B CG2 1 
ATOM   3456  N  N   . ILE B  1 43  ? -16.000 26.113  20.014  1.00 26.30 ? 42  ILE B N   1 
ATOM   3457  C  CA  . ILE B  1 43  ? -16.097 27.170  21.028  1.00 26.32 ? 42  ILE B CA  1 
ATOM   3458  C  C   . ILE B  1 43  ? -14.945 28.180  20.953  1.00 25.07 ? 42  ILE B C   1 
ATOM   3459  O  O   . ILE B  1 43  ? -15.088 29.331  21.388  1.00 25.48 ? 42  ILE B O   1 
ATOM   3460  C  CB  . ILE B  1 43  ? -16.304 26.567  22.443  1.00 27.12 ? 42  ILE B CB  1 
ATOM   3461  C  CG1 . ILE B  1 43  ? -16.856 27.629  23.391  1.00 28.95 ? 42  ILE B CG1 1 
ATOM   3462  C  CG2 . ILE B  1 43  ? -15.040 25.907  22.983  1.00 25.73 ? 42  ILE B CG2 1 
ATOM   3463  C  CD1 . ILE B  1 43  ? -17.388 27.081  24.707  1.00 30.90 ? 42  ILE B CD1 1 
ATOM   3464  N  N   . TRP B  1 44  ? -13.832 27.774  20.353  1.00 23.57 ? 43  TRP B N   1 
ATOM   3465  C  CA  . TRP B  1 44  ? -12.752 28.706  19.970  1.00 22.77 ? 43  TRP B CA  1 
ATOM   3466  C  C   . TRP B  1 44  ? -12.161 28.220  18.643  1.00 22.81 ? 43  TRP B C   1 
ATOM   3467  O  O   . TRP B  1 44  ? -11.804 27.045  18.552  1.00 21.34 ? 43  TRP B O   1 
ATOM   3468  C  CB  . TRP B  1 44  ? -11.654 28.690  21.030  1.00 22.67 ? 43  TRP B CB  1 
ATOM   3469  C  CG  . TRP B  1 44  ? -10.537 29.615  20.733  1.00 22.10 ? 43  TRP B CG  1 
ATOM   3470  C  CD1 . TRP B  1 44  ? -9.309  29.292  20.209  1.00 22.55 ? 43  TRP B CD1 1 
ATOM   3471  C  CD2 . TRP B  1 44  ? -10.552 31.028  20.886  1.00 22.61 ? 43  TRP B CD2 1 
ATOM   3472  N  NE1 . TRP B  1 44  ? -8.549  30.428  20.050  1.00 22.30 ? 43  TRP B NE1 1 
ATOM   3473  C  CE2 . TRP B  1 44  ? -9.295  31.512  20.444  1.00 23.16 ? 43  TRP B CE2 1 
ATOM   3474  C  CE3 . TRP B  1 44  ? -11.518 31.948  21.338  1.00 24.56 ? 43  TRP B CE3 1 
ATOM   3475  C  CZ2 . TRP B  1 44  ? -8.964  32.872  20.484  1.00 23.85 ? 43  TRP B CZ2 1 
ATOM   3476  C  CZ3 . TRP B  1 44  ? -11.194 33.289  21.375  1.00 24.31 ? 43  TRP B CZ3 1 
ATOM   3477  C  CH2 . TRP B  1 44  ? -9.921  33.741  20.958  1.00 24.30 ? 43  TRP B CH2 1 
ATOM   3478  N  N   . LEU B  1 45  ? -12.030 29.057  17.611  1.00 24.33 ? 44  LEU B N   1 
ATOM   3479  C  CA  . LEU B  1 45  ? -12.432 30.463  17.559  1.00 26.29 ? 44  LEU B CA  1 
ATOM   3480  C  C   . LEU B  1 45  ? -13.691 30.586  16.702  1.00 28.58 ? 44  LEU B C   1 
ATOM   3481  O  O   . LEU B  1 45  ? -13.716 30.187  15.540  1.00 27.10 ? 44  LEU B O   1 
ATOM   3482  C  CB  . LEU B  1 45  ? -11.302 31.301  16.942  1.00 27.38 ? 44  LEU B CB  1 
ATOM   3483  C  CG  . LEU B  1 45  ? -11.588 32.770  16.605  1.00 29.03 ? 44  LEU B CG  1 
ATOM   3484  C  CD1 . LEU B  1 45  ? -11.977 33.525  17.865  1.00 28.62 ? 44  LEU B CD1 1 
ATOM   3485  C  CD2 . LEU B  1 45  ? -10.371 33.410  15.965  1.00 28.98 ? 44  LEU B CD2 1 
ATOM   3486  N  N   . ASN B  1 46  ? -14.741 31.152  17.281  1.00 31.39 ? 45  ASN B N   1 
ATOM   3487  C  CA  . ASN B  1 46  ? -15.941 31.508  16.520  1.00 34.52 ? 45  ASN B CA  1 
ATOM   3488  C  C   . ASN B  1 46  ? -16.370 32.894  16.957  1.00 38.13 ? 45  ASN B C   1 
ATOM   3489  O  O   . ASN B  1 46  ? -16.791 33.110  18.107  1.00 35.28 ? 45  ASN B O   1 
ATOM   3490  C  CB  . ASN B  1 46  ? -17.058 30.512  16.737  1.00 36.89 ? 45  ASN B CB  1 
ATOM   3491  C  CG  . ASN B  1 46  ? -18.355 30.927  16.038  1.00 40.34 ? 45  ASN B CG  1 
ATOM   3492  O  OD1 . ASN B  1 46  ? -18.506 32.052  15.555  1.00 42.55 ? 45  ASN B OD1 1 
ATOM   3493  N  ND2 . ASN B  1 46  ? -19.281 30.015  15.973  1.00 41.15 ? 45  ASN B ND2 1 
ATOM   3494  N  N   . LEU B  1 47  ? -16.248 33.831  16.024  1.00 44.34 ? 46  LEU B N   1 
ATOM   3495  C  CA  . LEU B  1 47  ? -16.440 35.250  16.310  1.00 49.60 ? 46  LEU B CA  1 
ATOM   3496  C  C   . LEU B  1 47  ? -17.865 35.572  16.743  1.00 49.29 ? 46  LEU B C   1 
ATOM   3497  O  O   . LEU B  1 47  ? -18.094 36.494  17.509  1.00 52.19 ? 46  LEU B O   1 
ATOM   3498  C  CB  . LEU B  1 47  ? -16.082 36.081  15.077  1.00 53.25 ? 46  LEU B CB  1 
ATOM   3499  C  CG  . LEU B  1 47  ? -14.619 36.015  14.634  1.00 54.89 ? 46  LEU B CG  1 
ATOM   3500  C  CD1 . LEU B  1 47  ? -14.479 36.765  13.314  1.00 58.46 ? 46  LEU B CD1 1 
ATOM   3501  C  CD2 . LEU B  1 47  ? -13.716 36.598  15.710  1.00 53.98 ? 46  LEU B CD2 1 
ATOM   3502  N  N   . GLU B  1 48  ? -18.820 34.796  16.273  1.00 51.35 ? 47  GLU B N   1 
ATOM   3503  C  CA  . GLU B  1 48  ? -20.217 35.066  16.596  1.00 55.37 ? 47  GLU B CA  1 
ATOM   3504  C  C   . GLU B  1 48  ? -20.561 34.797  18.064  1.00 52.22 ? 47  GLU B C   1 
ATOM   3505  O  O   . GLU B  1 48  ? -21.557 35.308  18.563  1.00 50.51 ? 47  GLU B O   1 
ATOM   3506  C  CB  . GLU B  1 48  ? -21.123 34.268  15.673  1.00 60.21 ? 47  GLU B CB  1 
ATOM   3507  C  CG  . GLU B  1 48  ? -21.019 34.754  14.238  1.00 66.34 ? 47  GLU B CG  1 
ATOM   3508  C  CD  . GLU B  1 48  ? -21.921 34.003  13.294  1.00 71.41 ? 47  GLU B CD  1 
ATOM   3509  O  OE1 . GLU B  1 48  ? -22.218 32.817  13.563  1.00 76.38 ? 47  GLU B OE1 1 
ATOM   3510  O  OE2 . GLU B  1 48  ? -22.319 34.601  12.273  1.00 79.28 ? 47  GLU B OE2 1 
ATOM   3511  N  N   . LEU B  1 49  ? -19.721 34.030  18.761  1.00 46.19 ? 48  LEU B N   1 
ATOM   3512  C  CA  . LEU B  1 49  ? -19.951 33.741  20.176  1.00 42.41 ? 48  LEU B CA  1 
ATOM   3513  C  C   . LEU B  1 49  ? -19.448 34.859  21.083  1.00 40.73 ? 48  LEU B C   1 
ATOM   3514  O  O   . LEU B  1 49  ? -19.709 34.845  22.293  1.00 38.22 ? 48  LEU B O   1 
ATOM   3515  C  CB  . LEU B  1 49  ? -19.276 32.419  20.560  1.00 41.85 ? 48  LEU B CB  1 
ATOM   3516  C  CG  . LEU B  1 49  ? -19.606 31.194  19.707  1.00 42.14 ? 48  LEU B CG  1 
ATOM   3517  C  CD1 . LEU B  1 49  ? -18.850 29.985  20.235  1.00 41.11 ? 48  LEU B CD1 1 
ATOM   3518  C  CD2 . LEU B  1 49  ? -21.105 30.913  19.663  1.00 44.55 ? 48  LEU B CD2 1 
ATOM   3519  N  N   . LEU B  1 50  ? -18.708 35.812  20.513  1.00 41.42 ? 49  LEU B N   1 
ATOM   3520  C  CA  . LEU B  1 50  ? -18.064 36.873  21.287  1.00 42.99 ? 49  LEU B CA  1 
ATOM   3521  C  C   . LEU B  1 50  ? -18.810 38.225  21.236  1.00 43.64 ? 49  LEU B C   1 
ATOM   3522  O  O   . LEU B  1 50  ? -18.364 39.204  21.835  1.00 44.71 ? 49  LEU B O   1 
ATOM   3523  C  CB  . LEU B  1 50  ? -16.611 37.035  20.812  1.00 43.26 ? 49  LEU B CB  1 
ATOM   3524  C  CG  . LEU B  1 50  ? -15.807 35.717  20.732  1.00 43.62 ? 49  LEU B CG  1 
ATOM   3525  C  CD1 . LEU B  1 50  ? -14.405 35.923  20.166  1.00 42.07 ? 49  LEU B CD1 1 
ATOM   3526  C  CD2 . LEU B  1 50  ? -15.727 35.083  22.109  1.00 42.25 ? 49  LEU B CD2 1 
ATOM   3527  N  N   . LEU B  1 51  ? -19.945 38.271  20.551  1.00 46.43 ? 50  LEU B N   1 
ATOM   3528  C  CA  . LEU B  1 51  ? -20.742 39.508  20.454  1.00 48.91 ? 50  LEU B CA  1 
ATOM   3529  C  C   . LEU B  1 51  ? -21.360 39.877  21.812  1.00 48.64 ? 50  LEU B C   1 
ATOM   3530  O  O   . LEU B  1 51  ? -21.498 39.016  22.684  1.00 46.40 ? 50  LEU B O   1 
ATOM   3531  C  CB  . LEU B  1 51  ? -21.837 39.330  19.415  1.00 51.44 ? 50  LEU B CB  1 
ATOM   3532  C  CG  . LEU B  1 51  ? -21.362 39.066  17.975  1.00 54.76 ? 50  LEU B CG  1 
ATOM   3533  C  CD1 . LEU B  1 51  ? -22.481 38.492  17.114  1.00 55.14 ? 50  LEU B CD1 1 
ATOM   3534  C  CD2 . LEU B  1 51  ? -20.794 40.333  17.350  1.00 55.77 ? 50  LEU B CD2 1 
ATOM   3535  N  N   . PRO B  1 52  ? -21.718 41.162  22.013  1.00 48.86 ? 51  PRO B N   1 
ATOM   3536  C  CA  . PRO B  1 52  ? -22.335 41.553  23.285  1.00 47.44 ? 51  PRO B CA  1 
ATOM   3537  C  C   . PRO B  1 52  ? -23.512 40.642  23.665  1.00 45.65 ? 51  PRO B C   1 
ATOM   3538  O  O   . PRO B  1 52  ? -24.230 40.177  22.779  1.00 46.16 ? 51  PRO B O   1 
ATOM   3539  C  CB  . PRO B  1 52  ? -22.830 42.983  23.012  1.00 51.06 ? 51  PRO B CB  1 
ATOM   3540  C  CG  . PRO B  1 52  ? -21.937 43.498  21.933  1.00 51.61 ? 51  PRO B CG  1 
ATOM   3541  C  CD  . PRO B  1 52  ? -21.544 42.310  21.100  1.00 50.92 ? 51  PRO B CD  1 
ATOM   3542  N  N   . VAL B  1 53  ? -23.670 40.384  24.963  1.00 44.49 ? 52  VAL B N   1 
ATOM   3543  C  CA  . VAL B  1 53  ? -24.712 39.503  25.532  1.00 46.45 ? 52  VAL B CA  1 
ATOM   3544  C  C   . VAL B  1 53  ? -24.451 38.015  25.288  1.00 45.01 ? 52  VAL B C   1 
ATOM   3545  O  O   . VAL B  1 53  ? -24.351 37.239  26.236  1.00 43.66 ? 52  VAL B O   1 
ATOM   3546  C  CB  . VAL B  1 53  ? -26.141 39.868  25.059  1.00 49.82 ? 52  VAL B CB  1 
ATOM   3547  C  CG1 . VAL B  1 53  ? -27.186 39.038  25.803  1.00 50.96 ? 52  VAL B CG1 1 
ATOM   3548  C  CG2 . VAL B  1 53  ? -26.400 41.352  25.286  1.00 50.55 ? 52  VAL B CG2 1 
ATOM   3549  N  N   . ILE B  1 54  ? -24.335 37.618  24.028  1.00 44.02 ? 53  ILE B N   1 
ATOM   3550  C  CA  . ILE B  1 54  ? -23.966 36.238  23.722  1.00 44.53 ? 53  ILE B CA  1 
ATOM   3551  C  C   . ILE B  1 54  ? -22.621 35.856  24.357  1.00 41.14 ? 53  ILE B C   1 
ATOM   3552  O  O   . ILE B  1 54  ? -22.413 34.700  24.706  1.00 39.96 ? 53  ILE B O   1 
ATOM   3553  C  CB  . ILE B  1 54  ? -23.958 35.939  22.234  1.00 46.97 ? 53  ILE B CB  1 
ATOM   3554  C  CG1 . ILE B  1 54  ? -23.646 34.450  22.010  1.00 47.60 ? 53  ILE B CG1 1 
ATOM   3555  C  CG2 . ILE B  1 54  ? -22.916 36.796  21.584  1.00 48.06 ? 53  ILE B CG2 1 
ATOM   3556  C  CD1 . ILE B  1 54  ? -23.937 33.934  20.625  1.00 49.81 ? 53  ILE B CD1 1 
ATOM   3557  N  N   . ILE B  1 55  ? -21.715 36.819  24.508  1.00 38.88 ? 54  ILE B N   1 
ATOM   3558  C  CA  . ILE B  1 55  ? -20.433 36.537  25.141  1.00 36.71 ? 54  ILE B CA  1 
ATOM   3559  C  C   . ILE B  1 55  ? -20.594 35.985  26.569  1.00 35.11 ? 54  ILE B C   1 
ATOM   3560  O  O   . ILE B  1 55  ? -19.727 35.255  27.044  1.00 30.64 ? 54  ILE B O   1 
ATOM   3561  C  CB  . ILE B  1 55  ? -19.480 37.760  25.141  1.00 38.61 ? 54  ILE B CB  1 
ATOM   3562  C  CG1 . ILE B  1 55  ? -18.059 37.322  25.535  1.00 39.88 ? 54  ILE B CG1 1 
ATOM   3563  C  CG2 . ILE B  1 55  ? -19.982 38.853  26.070  1.00 39.71 ? 54  ILE B CG2 1 
ATOM   3564  C  CD1 . ILE B  1 55  ? -16.944 38.189  24.981  1.00 42.43 ? 54  ILE B CD1 1 
ATOM   3565  N  N   . ASP B  1 56  ? -21.694 36.317  27.249  1.00 34.69 ? 55  ASP B N   1 
ATOM   3566  C  CA  . ASP B  1 56  ? -21.931 35.754  28.585  1.00 34.65 ? 55  ASP B CA  1 
ATOM   3567  C  C   . ASP B  1 56  ? -22.151 34.232  28.520  1.00 34.09 ? 55  ASP B C   1 
ATOM   3568  O  O   . ASP B  1 56  ? -21.713 33.505  29.429  1.00 32.98 ? 55  ASP B O   1 
ATOM   3569  C  CB  . ASP B  1 56  ? -23.142 36.399  29.272  1.00 36.71 ? 55  ASP B CB  1 
ATOM   3570  C  CG  . ASP B  1 56  ? -22.945 37.880  29.562  1.00 38.59 ? 55  ASP B CG  1 
ATOM   3571  O  OD1 . ASP B  1 56  ? -21.809 38.307  29.875  1.00 38.26 ? 55  ASP B OD1 1 
ATOM   3572  O  OD2 . ASP B  1 56  ? -23.953 38.621  29.474  1.00 39.96 ? 55  ASP B OD2 1 
ATOM   3573  N  N   . CYS B  1 57  ? -22.818 33.770  27.458  1.00 34.10 ? 56  CYS B N   1 
ATOM   3574  C  CA  . CYS B  1 57  ? -22.987 32.336  27.197  1.00 35.53 ? 56  CYS B CA  1 
ATOM   3575  C  C   . CYS B  1 57  ? -21.627 31.658  26.983  1.00 32.42 ? 56  CYS B C   1 
ATOM   3576  O  O   . CYS B  1 57  ? -21.345 30.600  27.542  1.00 31.55 ? 56  CYS B O   1 
ATOM   3577  C  CB  . CYS B  1 57  ? -23.841 32.087  25.956  1.00 39.19 ? 56  CYS B CB  1 
ATOM   3578  S  SG  . CYS B  1 57  ? -25.417 32.985  25.878  1.00 46.52 ? 56  CYS B SG  1 
ATOM   3579  N  N   . TRP B  1 58  ? -20.783 32.296  26.177  1.00 30.47 ? 57  TRP B N   1 
ATOM   3580  C  CA  . TRP B  1 58  ? -19.440 31.790  25.889  1.00 29.02 ? 57  TRP B CA  1 
ATOM   3581  C  C   . TRP B  1 58  ? -18.607 31.683  27.157  1.00 27.44 ? 57  TRP B C   1 
ATOM   3582  O  O   . TRP B  1 58  ? -18.007 30.644  27.417  1.00 26.87 ? 57  TRP B O   1 
ATOM   3583  C  CB  . TRP B  1 58  ? -18.761 32.696  24.861  1.00 28.32 ? 57  TRP B CB  1 
ATOM   3584  C  CG  . TRP B  1 58  ? -17.400 32.288  24.465  1.00 27.36 ? 57  TRP B CG  1 
ATOM   3585  C  CD1 . TRP B  1 58  ? -17.060 31.291  23.576  1.00 26.84 ? 57  TRP B CD1 1 
ATOM   3586  C  CD2 . TRP B  1 58  ? -16.173 32.854  24.910  1.00 26.57 ? 57  TRP B CD2 1 
ATOM   3587  N  NE1 . TRP B  1 58  ? -15.712 31.220  23.452  1.00 26.27 ? 57  TRP B NE1 1 
ATOM   3588  C  CE2 . TRP B  1 58  ? -15.134 32.171  24.246  1.00 25.55 ? 57  TRP B CE2 1 
ATOM   3589  C  CE3 . TRP B  1 58  ? -15.845 33.889  25.782  1.00 26.39 ? 57  TRP B CE3 1 
ATOM   3590  C  CZ2 . TRP B  1 58  ? -13.791 32.476  24.447  1.00 25.35 ? 57  TRP B CZ2 1 
ATOM   3591  C  CZ3 . TRP B  1 58  ? -14.513 34.186  25.988  1.00 25.62 ? 57  TRP B CZ3 1 
ATOM   3592  C  CH2 . TRP B  1 58  ? -13.503 33.477  25.330  1.00 24.72 ? 57  TRP B CH2 1 
ATOM   3593  N  N   . ILE B  1 59  ? -18.565 32.760  27.938  1.00 27.67 ? 58  ILE B N   1 
ATOM   3594  C  CA  A ILE B  1 59  ? -17.833 32.770  29.197  0.50 27.78 ? 58  ILE B CA  1 
ATOM   3595  C  CA  B ILE B  1 59  ? -17.836 32.780  29.201  0.50 27.46 ? 58  ILE B CA  1 
ATOM   3596  C  C   . ILE B  1 59  ? -18.329 31.646  30.108  1.00 28.68 ? 58  ILE B C   1 
ATOM   3597  O  O   . ILE B  1 59  ? -17.524 30.931  30.722  1.00 27.50 ? 58  ILE B O   1 
ATOM   3598  C  CB  A ILE B  1 59  ? -17.948 34.134  29.922  0.50 29.06 ? 58  ILE B CB  1 
ATOM   3599  C  CB  B ILE B  1 59  ? -18.025 34.114  29.982  0.50 28.24 ? 58  ILE B CB  1 
ATOM   3600  C  CG1 A ILE B  1 59  ? -17.203 35.219  29.108  0.50 29.57 ? 58  ILE B CG1 1 
ATOM   3601  C  CG1 B ILE B  1 59  ? -17.397 35.324  29.314  0.50 28.38 ? 58  ILE B CG1 1 
ATOM   3602  C  CG2 A ILE B  1 59  ? -17.375 34.035  31.333  0.50 28.90 ? 58  ILE B CG2 1 
ATOM   3603  C  CG2 B ILE B  1 59  ? -17.387 34.028  31.352  0.50 28.03 ? 58  ILE B CG2 1 
ATOM   3604  C  CD1 A ILE B  1 59  ? -17.365 36.648  29.608  0.50 30.39 ? 58  ILE B CD1 1 
ATOM   3605  C  CD1 B ILE B  1 59  ? -15.922 35.230  29.079  0.50 26.94 ? 58  ILE B CD1 1 
ATOM   3606  N  N   . ASP B  1 60  ? -19.654 31.473  30.189  1.00 28.70 ? 59  ASP B N   1 
ATOM   3607  C  CA  . ASP B  1 60  ? -20.212 30.447  31.057  1.00 29.66 ? 59  ASP B CA  1 
ATOM   3608  C  C   . ASP B  1 60  ? -19.777 29.030  30.648  1.00 29.35 ? 59  ASP B C   1 
ATOM   3609  O  O   . ASP B  1 60  ? -19.737 28.138  31.505  1.00 30.39 ? 59  ASP B O   1 
ATOM   3610  C  CB  . ASP B  1 60  ? -21.761 30.519  31.123  1.00 32.42 ? 59  ASP B CB  1 
ATOM   3611  C  CG  . ASP B  1 60  ? -22.330 29.771  32.329  1.00 34.15 ? 59  ASP B CG  1 
ATOM   3612  O  OD1 . ASP B  1 60  ? -21.823 29.996  33.440  1.00 36.07 ? 59  ASP B OD1 1 
ATOM   3613  O  OD2 . ASP B  1 60  ? -23.277 28.964  32.169  1.00 36.29 ? 59  ASP B OD2 1 
ATOM   3614  N  N   . ASN B  1 61  ? -19.488 28.820  29.360  1.00 27.36 ? 60  ASN B N   1 
ATOM   3615  C  CA  . ASN B  1 61  ? -19.075 27.504  28.855  1.00 27.10 ? 60  ASN B CA  1 
ATOM   3616  C  C   . ASN B  1 61  ? -17.561 27.289  28.851  1.00 26.28 ? 60  ASN B C   1 
ATOM   3617  O  O   . ASN B  1 61  ? -17.097 26.164  29.058  1.00 27.02 ? 60  ASN B O   1 
ATOM   3618  C  CB  . ASN B  1 61  ? -19.595 27.280  27.434  1.00 26.89 ? 60  ASN B CB  1 
ATOM   3619  C  CG  . ASN B  1 61  ? -21.102 27.060  27.399  1.00 28.92 ? 60  ASN B CG  1 
ATOM   3620  O  OD1 . ASN B  1 61  ? -21.672 26.509  28.337  1.00 28.30 ? 60  ASN B OD1 1 
ATOM   3621  N  ND2 . ASN B  1 61  ? -21.743 27.498  26.327  1.00 28.88 ? 60  ASN B ND2 1 
ATOM   3622  N  N   . ILE B  1 62  ? -16.803 28.342  28.568  1.00 25.05 ? 61  ILE B N   1 
ATOM   3623  C  CA  . ILE B  1 62  ? -15.351 28.197  28.383  1.00 25.25 ? 61  ILE B CA  1 
ATOM   3624  C  C   . ILE B  1 62  ? -14.540 28.479  29.652  1.00 24.26 ? 61  ILE B C   1 
ATOM   3625  O  O   . ILE B  1 62  ? -13.332 28.153  29.719  1.00 23.25 ? 61  ILE B O   1 
ATOM   3626  C  CB  . ILE B  1 62  ? -14.836 29.071  27.219  1.00 26.69 ? 61  ILE B CB  1 
ATOM   3627  C  CG1 . ILE B  1 62  ? -13.537 28.473  26.646  1.00 27.10 ? 61  ILE B CG1 1 
ATOM   3628  C  CG2 . ILE B  1 62  ? -14.656 30.516  27.657  1.00 26.97 ? 61  ILE B CG2 1 
ATOM   3629  C  CD1 . ILE B  1 62  ? -13.109 29.064  25.320  1.00 29.61 ? 61  ILE B CD1 1 
ATOM   3630  N  N   . ARG B  1 63  ? -15.173 29.082  30.657  1.00 23.94 ? 62  ARG B N   1 
ATOM   3631  C  CA  . ARG B  1 63  ? -14.503 29.252  31.945  1.00 24.31 ? 62  ARG B CA  1 
ATOM   3632  C  C   . ARG B  1 63  ? -14.161 27.891  32.547  1.00 24.55 ? 62  ARG B C   1 
ATOM   3633  O  O   . ARG B  1 63  ? -14.864 26.893  32.311  1.00 24.85 ? 62  ARG B O   1 
ATOM   3634  C  CB  . ARG B  1 63  ? -15.378 30.049  32.926  1.00 26.10 ? 62  ARG B CB  1 
ATOM   3635  C  CG  . ARG B  1 63  ? -16.598 29.280  33.437  1.00 27.86 ? 62  ARG B CG  1 
ATOM   3636  C  CD  . ARG B  1 63  ? -17.606 30.183  34.123  1.00 31.08 ? 62  ARG B CD  1 
ATOM   3637  N  NE  . ARG B  1 63  ? -18.826 29.438  34.433  1.00 33.14 ? 62  ARG B NE  1 
ATOM   3638  C  CZ  . ARG B  1 63  ? -19.068 28.782  35.570  1.00 35.59 ? 62  ARG B CZ  1 
ATOM   3639  N  NH1 . ARG B  1 63  ? -18.186 28.770  36.564  1.00 35.72 ? 62  ARG B NH1 1 
ATOM   3640  N  NH2 . ARG B  1 63  ? -20.231 28.152  35.721  1.00 38.57 ? 62  ARG B NH2 1 
ATOM   3641  N  N   . LEU B  1 64  ? -13.077 27.857  33.318  1.00 24.34 ? 63  LEU B N   1 
ATOM   3642  C  CA  . LEU B  1 64  ? -12.794 26.745  34.216  1.00 24.20 ? 63  LEU B CA  1 
ATOM   3643  C  C   . LEU B  1 64  ? -13.288 27.069  35.646  1.00 24.89 ? 63  LEU B C   1 
ATOM   3644  O  O   . LEU B  1 64  ? -13.244 28.224  36.086  1.00 24.57 ? 63  LEU B O   1 
ATOM   3645  C  CB  . LEU B  1 64  ? -11.304 26.472  34.243  1.00 22.74 ? 63  LEU B CB  1 
ATOM   3646  C  CG  . LEU B  1 64  ? -10.632 25.970  32.957  1.00 22.99 ? 63  LEU B CG  1 
ATOM   3647  C  CD1 . LEU B  1 64  ? -9.145  25.836  33.213  1.00 23.00 ? 63  LEU B CD1 1 
ATOM   3648  C  CD2 . LEU B  1 64  ? -11.224 24.636  32.533  1.00 23.81 ? 63  LEU B CD2 1 
ATOM   3649  N  N   . VAL B  1 65  ? -13.767 26.043  36.350  1.00 24.84 ? 64  VAL B N   1 
ATOM   3650  C  CA  . VAL B  1 65  ? -14.156 26.147  37.753  1.00 26.05 ? 64  VAL B CA  1 
ATOM   3651  C  C   . VAL B  1 65  ? -12.980 25.665  38.607  1.00 26.08 ? 64  VAL B C   1 
ATOM   3652  O  O   . VAL B  1 65  ? -12.513 24.542  38.409  1.00 26.17 ? 64  VAL B O   1 
ATOM   3653  C  CB  . VAL B  1 65  ? -15.381 25.264  38.043  1.00 28.48 ? 64  VAL B CB  1 
ATOM   3654  C  CG1 . VAL B  1 65  ? -15.752 25.295  39.523  1.00 29.61 ? 64  VAL B CG1 1 
ATOM   3655  C  CG2 . VAL B  1 65  ? -16.562 25.720  37.196  1.00 29.43 ? 64  VAL B CG2 1 
ATOM   3656  N  N   . TYR B  1 66  ? -12.491 26.504  39.525  1.00 24.97 ? 65  TYR B N   1 
ATOM   3657  C  CA  . TYR B  1 66  ? -11.407 26.100  40.411  1.00 25.01 ? 65  TYR B CA  1 
ATOM   3658  C  C   . TYR B  1 66  ? -11.981 25.491  41.686  1.00 26.93 ? 65  TYR B C   1 
ATOM   3659  O  O   . TYR B  1 66  ? -12.764 26.119  42.389  1.00 28.02 ? 65  TYR B O   1 
ATOM   3660  C  CB  . TYR B  1 66  ? -10.466 27.266  40.733  1.00 24.58 ? 65  TYR B CB  1 
ATOM   3661  C  CG  . TYR B  1 66  ? -9.210  26.769  41.424  1.00 23.71 ? 65  TYR B CG  1 
ATOM   3662  C  CD1 . TYR B  1 66  ? -8.147  26.254  40.689  1.00 22.42 ? 65  TYR B CD1 1 
ATOM   3663  C  CD2 . TYR B  1 66  ? -9.109  26.758  42.813  1.00 24.79 ? 65  TYR B CD2 1 
ATOM   3664  C  CE1 . TYR B  1 66  ? -7.021  25.757  41.309  1.00 22.05 ? 65  TYR B CE1 1 
ATOM   3665  C  CE2 . TYR B  1 66  ? -7.970  26.260  43.444  1.00 24.15 ? 65  TYR B CE2 1 
ATOM   3666  C  CZ  . TYR B  1 66  ? -6.930  25.777  42.687  1.00 23.11 ? 65  TYR B CZ  1 
ATOM   3667  O  OH  . TYR B  1 66  ? -5.813  25.263  43.313  1.00 23.61 ? 65  TYR B OH  1 
ATOM   3668  N  N   . ASN B  1 67  ? -11.619 24.252  41.968  1.00 27.90 ? 66  ASN B N   1 
ATOM   3669  C  CA  . ASN B  1 67  ? -12.098 23.555  43.159  1.00 30.71 ? 66  ASN B CA  1 
ATOM   3670  C  C   . ASN B  1 67  ? -11.004 23.619  44.222  1.00 30.52 ? 66  ASN B C   1 
ATOM   3671  O  O   . ASN B  1 67  ? -9.951  22.992  44.071  1.00 28.14 ? 66  ASN B O   1 
ATOM   3672  C  CB  . ASN B  1 67  ? -12.441 22.121  42.764  1.00 32.44 ? 66  ASN B CB  1 
ATOM   3673  C  CG  . ASN B  1 67  ? -12.964 21.287  43.914  1.00 36.10 ? 66  ASN B CG  1 
ATOM   3674  O  OD1 . ASN B  1 67  ? -12.605 21.477  45.085  1.00 33.27 ? 66  ASN B OD1 1 
ATOM   3675  N  ND2 . ASN B  1 67  ? -13.827 20.331  43.572  1.00 40.04 ? 66  ASN B ND2 1 
ATOM   3676  N  N   . LYS B  1 68  ? -11.254 24.383  45.287  1.00 32.87 ? 67  LYS B N   1 
ATOM   3677  C  CA  . LYS B  1 68  ? -10.244 24.615  46.335  1.00 35.07 ? 67  LYS B CA  1 
ATOM   3678  C  C   . LYS B  1 68  ? -9.911  23.360  47.143  1.00 36.46 ? 67  LYS B C   1 
ATOM   3679  O  O   . LYS B  1 68  ? -8.826  23.254  47.685  1.00 38.92 ? 67  LYS B O   1 
ATOM   3680  C  CB  . LYS B  1 68  ? -10.699 25.711  47.305  1.00 37.37 ? 67  LYS B CB  1 
ATOM   3681  C  CG  . LYS B  1 68  ? -10.828 27.098  46.709  1.00 39.27 ? 67  LYS B CG  1 
ATOM   3682  C  CD  . LYS B  1 68  ? -11.367 28.061  47.753  1.00 41.82 ? 67  LYS B CD  1 
ATOM   3683  C  CE  . LYS B  1 68  ? -11.282 29.509  47.308  1.00 44.88 ? 67  LYS B CE  1 
ATOM   3684  N  NZ  . LYS B  1 68  ? -12.299 29.855  46.271  1.00 47.30 ? 67  LYS B NZ  1 
ATOM   3685  N  N   . THR B  1 69  ? -10.843 22.420  47.222  1.00 37.96 ? 68  THR B N   1 
ATOM   3686  C  CA  . THR B  1 69  ? -10.631 21.165  47.954  1.00 39.40 ? 68  THR B CA  1 
ATOM   3687  C  C   . THR B  1 69  ? -9.665  20.248  47.221  1.00 38.38 ? 68  THR B C   1 
ATOM   3688  O  O   . THR B  1 69  ? -8.713  19.748  47.801  1.00 40.91 ? 68  THR B O   1 
ATOM   3689  C  CB  . THR B  1 69  ? -11.970 20.417  48.151  1.00 39.92 ? 68  THR B CB  1 
ATOM   3690  O  OG1 . THR B  1 69  ? -12.907 21.303  48.773  1.00 41.11 ? 68  THR B OG1 1 
ATOM   3691  C  CG2 . THR B  1 69  ? -11.792 19.168  49.006  1.00 41.44 ? 68  THR B CG2 1 
ATOM   3692  N  N   . SER B  1 70  ? -9.923  20.007  45.940  1.00 36.25 ? 69  SER B N   1 
ATOM   3693  C  CA  . SER B  1 70  ? -9.057  19.161  45.152  1.00 34.44 ? 69  SER B CA  1 
ATOM   3694  C  C   . SER B  1 70  ? -7.833  19.914  44.618  1.00 32.57 ? 69  SER B C   1 
ATOM   3695  O  O   . SER B  1 70  ? -6.931  19.284  44.107  1.00 30.64 ? 69  SER B O   1 
ATOM   3696  C  CB  . SER B  1 70  ? -9.828  18.564  43.971  1.00 34.06 ? 69  SER B CB  1 
ATOM   3697  O  OG  . SER B  1 70  ? -10.304 19.585  43.112  1.00 33.46 ? 69  SER B OG  1 
ATOM   3698  N  N   . ARG B  1 71  ? -7.828  21.249  44.704  1.00 30.87 ? 70  ARG B N   1 
ATOM   3699  C  CA  . ARG B  1 71  ? -6.793  22.084  44.064  1.00 30.70 ? 70  ARG B CA  1 
ATOM   3700  C  C   . ARG B  1 71  ? -6.647  21.740  42.590  1.00 29.00 ? 70  ARG B C   1 
ATOM   3701  O  O   . ARG B  1 71  ? -5.551  21.517  42.092  1.00 28.40 ? 70  ARG B O   1 
ATOM   3702  C  CB  . ARG B  1 71  ? -5.434  21.963  44.795  1.00 31.55 ? 70  ARG B CB  1 
ATOM   3703  C  CG  . ARG B  1 71  ? -5.471  22.359  46.273  1.00 32.17 ? 70  ARG B CG  1 
ATOM   3704  C  CD  . ARG B  1 71  ? -5.704  23.844  46.455  1.00 32.46 ? 70  ARG B CD  1 
ATOM   3705  N  NE  . ARG B  1 71  ? -4.570  24.617  45.955  1.00 31.49 ? 70  ARG B NE  1 
ATOM   3706  C  CZ  . ARG B  1 71  ? -3.620  25.160  46.708  1.00 31.53 ? 70  ARG B CZ  1 
ATOM   3707  N  NH1 . ARG B  1 71  ? -3.650  25.068  48.032  1.00 31.18 ? 70  ARG B NH1 1 
ATOM   3708  N  NH2 . ARG B  1 71  ? -2.656  25.854  46.134  1.00 31.29 ? 70  ARG B NH2 1 
ATOM   3709  N  N   . ALA B  1 72  ? -7.777  21.685  41.893  1.00 28.60 ? 71  ALA B N   1 
ATOM   3710  C  CA  . ALA B  1 72  ? -7.810  21.304  40.485  1.00 26.72 ? 71  ALA B CA  1 
ATOM   3711  C  C   . ALA B  1 72  ? -8.972  22.014  39.802  1.00 26.98 ? 71  ALA B C   1 
ATOM   3712  O  O   . ALA B  1 72  ? -9.906  22.458  40.465  1.00 26.41 ? 71  ALA B O   1 
ATOM   3713  C  CB  . ALA B  1 72  ? -7.999  19.810  40.368  1.00 28.02 ? 71  ALA B CB  1 
ATOM   3714  N  N   . THR B  1 73  ? -8.912  22.140  38.483  1.00 25.46 ? 72  THR B N   1 
ATOM   3715  C  CA  . THR B  1 73  ? -9.994  22.785  37.749  1.00 26.76 ? 72  THR B CA  1 
ATOM   3716  C  C   . THR B  1 73  ? -10.942 21.729  37.238  1.00 28.06 ? 72  THR B C   1 
ATOM   3717  O  O   . THR B  1 73  ? -10.547 20.581  37.029  1.00 27.88 ? 72  THR B O   1 
ATOM   3718  C  CB  . THR B  1 73  ? -9.506  23.659  36.570  1.00 27.05 ? 72  THR B CB  1 
ATOM   3719  O  OG1 . THR B  1 73  ? -8.620  22.915  35.711  1.00 26.19 ? 72  THR B OG1 1 
ATOM   3720  C  CG2 . THR B  1 73  ? -8.793  24.876  37.087  1.00 27.05 ? 72  THR B CG2 1 
ATOM   3721  N  N   . GLN B  1 74  ? -12.179 22.141  37.012  1.00 28.22 ? 73  GLN B N   1 
ATOM   3722  C  CA  . GLN B  1 74  ? -13.161 21.299  36.363  1.00 29.55 ? 73  GLN B CA  1 
ATOM   3723  C  C   . GLN B  1 74  ? -13.987 22.153  35.391  1.00 28.35 ? 73  GLN B C   1 
ATOM   3724  O  O   . GLN B  1 74  ? -13.950 23.374  35.452  1.00 27.27 ? 73  GLN B O   1 
ATOM   3725  C  CB  . GLN B  1 74  ? -14.019 20.581  37.421  1.00 33.34 ? 73  GLN B CB  1 
ATOM   3726  C  CG  . GLN B  1 74  ? -14.413 21.462  38.585  1.00 36.02 ? 73  GLN B CG  1 
ATOM   3727  C  CD  . GLN B  1 74  ? -15.030 20.702  39.756  1.00 38.75 ? 73  GLN B CD  1 
ATOM   3728  O  OE1 . GLN B  1 74  ? -14.339 20.054  40.549  1.00 39.48 ? 73  GLN B OE1 1 
ATOM   3729  N  NE2 . GLN B  1 74  ? -16.326 20.820  39.886  1.00 39.35 ? 73  GLN B NE2 1 
ATOM   3730  N  N   . PHE B  1 75  ? -14.704 21.512  34.465  1.00 28.55 ? 74  PHE B N   1 
ATOM   3731  C  CA  . PHE B  1 75  ? -15.575 22.240  33.543  1.00 28.37 ? 74  PHE B CA  1 
ATOM   3732  C  C   . PHE B  1 75  ? -16.875 22.574  34.278  1.00 29.35 ? 74  PHE B C   1 
ATOM   3733  O  O   . PHE B  1 75  ? -17.206 21.917  35.255  1.00 28.75 ? 74  PHE B O   1 
ATOM   3734  C  CB  . PHE B  1 75  ? -15.884 21.428  32.277  1.00 28.63 ? 74  PHE B CB  1 
ATOM   3735  C  CG  . PHE B  1 75  ? -14.657 20.867  31.566  1.00 27.78 ? 74  PHE B CG  1 
ATOM   3736  C  CD1 . PHE B  1 75  ? -13.459 21.559  31.530  1.00 27.15 ? 74  PHE B CD1 1 
ATOM   3737  C  CD2 . PHE B  1 75  ? -14.730 19.643  30.931  1.00 27.92 ? 74  PHE B CD2 1 
ATOM   3738  C  CE1 . PHE B  1 75  ? -12.356 21.027  30.865  1.00 27.92 ? 74  PHE B CE1 1 
ATOM   3739  C  CE2 . PHE B  1 75  ? -13.640 19.105  30.262  1.00 28.59 ? 74  PHE B CE2 1 
ATOM   3740  C  CZ  . PHE B  1 75  ? -12.448 19.794  30.221  1.00 27.87 ? 74  PHE B CZ  1 
ATOM   3741  N  N   . PRO B  1 76  ? -17.613 23.589  33.810  1.00 28.96 ? 75  PRO B N   1 
ATOM   3742  C  CA  . PRO B  1 76  ? -18.927 23.831  34.406  1.00 30.88 ? 75  PRO B CA  1 
ATOM   3743  C  C   . PRO B  1 76  ? -19.864 22.619  34.271  1.00 32.40 ? 75  PRO B C   1 
ATOM   3744  O  O   . PRO B  1 76  ? -19.659 21.780  33.404  1.00 31.33 ? 75  PRO B O   1 
ATOM   3745  C  CB  . PRO B  1 76  ? -19.454 25.032  33.617  1.00 31.35 ? 75  PRO B CB  1 
ATOM   3746  C  CG  . PRO B  1 76  ? -18.206 25.725  33.121  1.00 29.86 ? 75  PRO B CG  1 
ATOM   3747  C  CD  . PRO B  1 76  ? -17.264 24.612  32.809  1.00 28.40 ? 75  PRO B CD  1 
ATOM   3748  N  N   . ASP B  1 77  ? -20.872 22.533  35.141  1.00 34.62 ? 76  ASP B N   1 
ATOM   3749  C  CA  . ASP B  1 77  ? -21.822 21.420  35.100  1.00 36.81 ? 76  ASP B CA  1 
ATOM   3750  C  C   . ASP B  1 77  ? -22.431 21.283  33.713  1.00 34.78 ? 76  ASP B C   1 
ATOM   3751  O  O   . ASP B  1 77  ? -22.889 22.271  33.142  1.00 34.63 ? 76  ASP B O   1 
ATOM   3752  C  CB  . ASP B  1 77  ? -22.968 21.631  36.106  1.00 42.04 ? 76  ASP B CB  1 
ATOM   3753  C  CG  . ASP B  1 77  ? -22.501 21.605  37.554  1.00 45.97 ? 76  ASP B CG  1 
ATOM   3754  O  OD1 . ASP B  1 77  ? -21.400 21.083  37.826  1.00 51.02 ? 76  ASP B OD1 1 
ATOM   3755  O  OD2 . ASP B  1 77  ? -23.233 22.129  38.423  1.00 51.90 ? 76  ASP B OD2 1 
ATOM   3756  N  N   . GLY B  1 78  ? -22.426 20.060  33.189  1.00 33.76 ? 77  GLY B N   1 
ATOM   3757  C  CA  . GLY B  1 78  ? -22.993 19.756  31.885  1.00 34.02 ? 77  GLY B CA  1 
ATOM   3758  C  C   . GLY B  1 78  ? -22.207 20.246  30.677  1.00 32.73 ? 77  GLY B C   1 
ATOM   3759  O  O   . GLY B  1 78  ? -22.750 20.303  29.570  1.00 34.75 ? 77  GLY B O   1 
ATOM   3760  N  N   . VAL B  1 79  ? -20.948 20.624  30.862  1.00 31.10 ? 78  VAL B N   1 
ATOM   3761  C  CA  . VAL B  1 79  ? -20.134 21.091  29.743  1.00 30.23 ? 78  VAL B CA  1 
ATOM   3762  C  C   . VAL B  1 79  ? -18.967 20.133  29.560  1.00 30.02 ? 78  VAL B C   1 
ATOM   3763  O  O   . VAL B  1 79  ? -18.292 19.799  30.530  1.00 29.84 ? 78  VAL B O   1 
ATOM   3764  C  CB  . VAL B  1 79  ? -19.571 22.513  29.990  1.00 29.75 ? 78  VAL B CB  1 
ATOM   3765  C  CG1 . VAL B  1 79  ? -18.678 22.955  28.836  1.00 28.64 ? 78  VAL B CG1 1 
ATOM   3766  C  CG2 . VAL B  1 79  ? -20.695 23.531  30.201  1.00 31.27 ? 78  VAL B CG2 1 
ATOM   3767  N  N   . ASP B  1 80  ? -18.740 19.692  28.325  1.00 29.82 ? 79  ASP B N   1 
ATOM   3768  C  CA  . ASP B  1 80  ? -17.487 19.031  27.991  1.00 30.17 ? 79  ASP B CA  1 
ATOM   3769  C  C   . ASP B  1 80  ? -16.733 19.831  26.941  1.00 27.44 ? 79  ASP B C   1 
ATOM   3770  O  O   . ASP B  1 80  ? -17.330 20.347  25.995  1.00 26.97 ? 79  ASP B O   1 
ATOM   3771  C  CB  . ASP B  1 80  ? -17.677 17.622  27.452  1.00 31.86 ? 79  ASP B CB  1 
ATOM   3772  C  CG  . ASP B  1 80  ? -16.333 16.883  27.348  1.00 35.25 ? 79  ASP B CG  1 
ATOM   3773  O  OD1 . ASP B  1 80  ? -15.599 16.843  28.377  1.00 35.77 ? 79  ASP B OD1 1 
ATOM   3774  O  OD2 . ASP B  1 80  ? -15.975 16.433  26.236  1.00 36.29 ? 79  ASP B OD2 1 
ATOM   3775  N  N   . VAL B  1 81  ? -15.417 19.929  27.119  1.00 27.22 ? 80  VAL B N   1 
ATOM   3776  C  CA  . VAL B  1 81  ? -14.545 20.615  26.153  1.00 26.58 ? 80  VAL B CA  1 
ATOM   3777  C  C   . VAL B  1 81  ? -13.449 19.653  25.682  1.00 27.10 ? 80  VAL B C   1 
ATOM   3778  O  O   . VAL B  1 81  ? -12.780 19.034  26.495  1.00 28.50 ? 80  VAL B O   1 
ATOM   3779  C  CB  . VAL B  1 81  ? -13.904 21.875  26.748  1.00 26.25 ? 80  VAL B CB  1 
ATOM   3780  C  CG1 . VAL B  1 81  ? -12.986 22.564  25.737  1.00 25.61 ? 80  VAL B CG1 1 
ATOM   3781  C  CG2 . VAL B  1 81  ? -14.975 22.863  27.186  1.00 27.06 ? 80  VAL B CG2 1 
ATOM   3782  N  N   . ARG B  1 82  ? -13.298 19.505  24.367  1.00 26.10 ? 81  ARG B N   1 
ATOM   3783  C  CA  . ARG B  1 82  ? -12.285 18.628  23.811  1.00 26.05 ? 81  ARG B CA  1 
ATOM   3784  C  C   . ARG B  1 82  ? -11.401 19.365  22.812  1.00 23.62 ? 81  ARG B C   1 
ATOM   3785  O  O   . ARG B  1 82  ? -11.792 20.393  22.255  1.00 22.73 ? 81  ARG B O   1 
ATOM   3786  C  CB  . ARG B  1 82  ? -12.930 17.379  23.194  1.00 28.10 ? 81  ARG B CB  1 
ATOM   3787  C  CG  . ARG B  1 82  ? -13.581 17.603  21.856  1.00 31.38 ? 81  ARG B CG  1 
ATOM   3788  C  CD  . ARG B  1 82  ? -14.041 16.298  21.219  1.00 34.78 ? 81  ARG B CD  1 
ATOM   3789  N  NE  . ARG B  1 82  ? -14.711 16.608  19.957  1.00 38.34 ? 81  ARG B NE  1 
ATOM   3790  C  CZ  . ARG B  1 82  ? -15.521 15.779  19.283  1.00 43.38 ? 81  ARG B CZ  1 
ATOM   3791  N  NH1 . ARG B  1 82  ? -15.806 14.560  19.741  1.00 41.76 ? 81  ARG B NH1 1 
ATOM   3792  N  NH2 . ARG B  1 82  ? -16.060 16.191  18.139  1.00 43.27 ? 81  ARG B NH2 1 
ATOM   3793  N  N   . VAL B  1 83  ? -10.223 18.804  22.579  1.00 21.86 ? 82  VAL B N   1 
ATOM   3794  C  CA  . VAL B  1 83  ? -9.225  19.375  21.675  1.00 21.92 ? 82  VAL B CA  1 
ATOM   3795  C  C   . VAL B  1 83  ? -9.251  18.560  20.386  1.00 22.10 ? 82  VAL B C   1 
ATOM   3796  O  O   . VAL B  1 83  ? -8.851  17.409  20.398  1.00 22.26 ? 82  VAL B O   1 
ATOM   3797  C  CB  . VAL B  1 83  ? -7.828  19.276  22.295  1.00 21.07 ? 82  VAL B CB  1 
ATOM   3798  C  CG1 . VAL B  1 83  ? -6.771  19.834  21.360  1.00 21.44 ? 82  VAL B CG1 1 
ATOM   3799  C  CG2 . VAL B  1 83  ? -7.817  20.009  23.636  1.00 21.93 ? 82  VAL B CG2 1 
ATOM   3800  N  N   . PRO B  1 84  ? -9.760  19.130  19.280  1.00 22.84 ? 83  PRO B N   1 
ATOM   3801  C  CA  . PRO B  1 84  ? -9.727  18.384  18.013  1.00 22.69 ? 83  PRO B CA  1 
ATOM   3802  C  C   . PRO B  1 84  ? -8.351  18.409  17.348  1.00 22.04 ? 83  PRO B C   1 
ATOM   3803  O  O   . PRO B  1 84  ? -7.537  19.268  17.664  1.00 21.38 ? 83  PRO B O   1 
ATOM   3804  C  CB  . PRO B  1 84  ? -10.729 19.144  17.140  1.00 23.65 ? 83  PRO B CB  1 
ATOM   3805  C  CG  . PRO B  1 84  ? -10.610 20.550  17.617  1.00 23.53 ? 83  PRO B CG  1 
ATOM   3806  C  CD  . PRO B  1 84  ? -10.364 20.464  19.105  1.00 23.04 ? 83  PRO B CD  1 
ATOM   3807  N  N   . GLY B  1 85  ? -8.091  17.462  16.435  1.00 21.18 ? 84  GLY B N   1 
ATOM   3808  C  CA  . GLY B  1 85  ? -6.959  17.594  15.518  1.00 20.93 ? 84  GLY B CA  1 
ATOM   3809  C  C   . GLY B  1 85  ? -5.596  17.189  16.027  1.00 20.29 ? 84  GLY B C   1 
ATOM   3810  O  O   . GLY B  1 85  ? -4.575  17.589  15.441  1.00 20.00 ? 84  GLY B O   1 
ATOM   3811  N  N   . PHE B  1 86  ? -5.543  16.429  17.126  1.00 19.47 ? 85  PHE B N   1 
ATOM   3812  C  CA  . PHE B  1 86  ? -4.259  15.948  17.619  1.00 19.24 ? 85  PHE B CA  1 
ATOM   3813  C  C   . PHE B  1 86  ? -3.642  15.015  16.563  1.00 19.56 ? 85  PHE B C   1 
ATOM   3814  O  O   . PHE B  1 86  ? -4.276  14.095  16.086  1.00 19.31 ? 85  PHE B O   1 
ATOM   3815  C  CB  . PHE B  1 86  ? -4.372  15.235  18.991  1.00 19.62 ? 85  PHE B CB  1 
ATOM   3816  C  CG  . PHE B  1 86  ? -3.025  14.940  19.620  1.00 18.48 ? 85  PHE B CG  1 
ATOM   3817  C  CD1 . PHE B  1 86  ? -2.400  15.866  20.446  1.00 19.13 ? 85  PHE B CD1 1 
ATOM   3818  C  CD2 . PHE B  1 86  ? -2.370  13.765  19.338  1.00 18.95 ? 85  PHE B CD2 1 
ATOM   3819  C  CE1 . PHE B  1 86  ? -1.152  15.610  20.998  1.00 18.01 ? 85  PHE B CE1 1 
ATOM   3820  C  CE2 . PHE B  1 86  ? -1.114  13.504  19.873  1.00 18.74 ? 85  PHE B CE2 1 
ATOM   3821  C  CZ  . PHE B  1 86  ? -0.512  14.415  20.714  1.00 18.42 ? 85  PHE B CZ  1 
ATOM   3822  N  N   . GLY B  1 87  ? -2.402  15.280  16.203  1.00 19.33 ? 86  GLY B N   1 
ATOM   3823  C  CA  . GLY B  1 87  ? -1.718  14.495  15.191  1.00 19.82 ? 86  GLY B CA  1 
ATOM   3824  C  C   . GLY B  1 87  ? -1.948  15.025  13.793  1.00 20.57 ? 86  GLY B C   1 
ATOM   3825  O  O   . GLY B  1 87  ? -1.305  14.553  12.873  1.00 21.15 ? 86  GLY B O   1 
ATOM   3826  N  N   . LYS B  1 88  ? -2.829  16.031  13.648  1.00 21.19 ? 87  LYS B N   1 
ATOM   3827  C  CA  . LYS B  1 88  ? -3.110  16.718  12.386  1.00 23.21 ? 87  LYS B CA  1 
ATOM   3828  C  C   . LYS B  1 88  ? -2.633  18.172  12.527  1.00 22.20 ? 87  LYS B C   1 
ATOM   3829  O  O   . LYS B  1 88  ? -2.041  18.523  13.546  1.00 21.33 ? 87  LYS B O   1 
ATOM   3830  C  CB  . LYS B  1 88  ? -4.614  16.714  12.100  1.00 26.32 ? 87  LYS B CB  1 
ATOM   3831  C  CG  . LYS B  1 88  ? -5.280  15.355  12.209  1.00 29.67 ? 87  LYS B CG  1 
ATOM   3832  C  CD  . LYS B  1 88  ? -4.701  14.374  11.220  1.00 32.26 ? 87  LYS B CD  1 
ATOM   3833  C  CE  . LYS B  1 88  ? -5.444  13.036  11.264  1.00 36.54 ? 87  LYS B CE  1 
ATOM   3834  N  NZ  . LYS B  1 88  ? -4.623  11.954  10.648  1.00 37.89 ? 87  LYS B NZ  1 
ATOM   3835  N  N   . THR B  1 89  ? -2.885  19.014  11.535  1.00 22.09 ? 88  THR B N   1 
ATOM   3836  C  CA  . THR B  1 89  ? -2.443  20.423  11.615  1.00 21.82 ? 88  THR B CA  1 
ATOM   3837  C  C   . THR B  1 89  ? -3.566  21.436  11.455  1.00 20.92 ? 88  THR B C   1 
ATOM   3838  O  O   . THR B  1 89  ? -3.395  22.606  11.803  1.00 20.47 ? 88  THR B O   1 
ATOM   3839  C  CB  . THR B  1 89  ? -1.350  20.743  10.580  1.00 23.47 ? 88  THR B CB  1 
ATOM   3840  O  OG1 . THR B  1 89  ? -1.895  20.597  9.275   1.00 24.64 ? 88  THR B OG1 1 
ATOM   3841  C  CG2 . THR B  1 89  ? -0.138  19.802  10.734  1.00 23.58 ? 88  THR B CG2 1 
ATOM   3842  N  N   . PHE B  1 90  ? -4.741  20.998  11.011  1.00 21.27 ? 89  PHE B N   1 
ATOM   3843  C  CA  . PHE B  1 90  ? -5.810  21.938  10.696  1.00 21.81 ? 89  PHE B CA  1 
ATOM   3844  C  C   . PHE B  1 90  ? -6.190  22.834  11.874  1.00 21.08 ? 89  PHE B C   1 
ATOM   3845  O  O   . PHE B  1 90  ? -6.510  24.032  11.676  1.00 21.03 ? 89  PHE B O   1 
ATOM   3846  C  CB  . PHE B  1 90  ? -7.046  21.216  10.121  1.00 23.54 ? 89  PHE B CB  1 
ATOM   3847  C  CG  . PHE B  1 90  ? -7.812  20.389  11.127  1.00 25.74 ? 89  PHE B CG  1 
ATOM   3848  C  CD1 . PHE B  1 90  ? -8.796  20.968  11.915  1.00 27.41 ? 89  PHE B CD1 1 
ATOM   3849  C  CD2 . PHE B  1 90  ? -7.591  19.018  11.238  1.00 26.95 ? 89  PHE B CD2 1 
ATOM   3850  C  CE1 . PHE B  1 90  ? -9.511  20.212  12.831  1.00 28.23 ? 89  PHE B CE1 1 
ATOM   3851  C  CE2 . PHE B  1 90  ? -8.307  18.255  12.148  1.00 26.86 ? 89  PHE B CE2 1 
ATOM   3852  C  CZ  . PHE B  1 90  ? -9.266  18.856  12.950  1.00 28.01 ? 89  PHE B CZ  1 
ATOM   3853  N  N   . SER B  1 91  ? -6.163  22.281  13.085  1.00 20.16 ? 90  SER B N   1 
ATOM   3854  C  CA  . SER B  1 91  ? -6.702  23.007  14.234  1.00 20.48 ? 90  SER B CA  1 
ATOM   3855  C  C   . SER B  1 91  ? -5.741  24.053  14.792  1.00 20.81 ? 90  SER B C   1 
ATOM   3856  O  O   . SER B  1 91  ? -6.143  24.897  15.607  1.00 19.80 ? 90  SER B O   1 
ATOM   3857  C  CB  . SER B  1 91  ? -7.154  22.047  15.335  1.00 20.97 ? 90  SER B CB  1 
ATOM   3858  O  OG  . SER B  1 91  ? -6.070  21.491  16.045  1.00 19.89 ? 90  SER B OG  1 
ATOM   3859  N  N   . LEU B  1 92  ? -4.464  23.970  14.403  1.00 19.99 ? 91  LEU B N   1 
ATOM   3860  C  CA  A LEU B  1 92  ? -3.483  25.015  14.652  0.50 20.84 ? 91  LEU B CA  1 
ATOM   3861  C  CA  B LEU B  1 92  ? -3.539  25.065  14.706  0.50 20.34 ? 91  LEU B CA  1 
ATOM   3862  C  C   . LEU B  1 92  ? -3.244  25.967  13.495  1.00 20.87 ? 91  LEU B C   1 
ATOM   3863  O  O   . LEU B  1 92  ? -2.726  27.074  13.683  1.00 21.32 ? 91  LEU B O   1 
ATOM   3864  C  CB  A LEU B  1 92  ? -2.119  24.337  14.850  0.50 21.81 ? 91  LEU B CB  1 
ATOM   3865  C  CB  B LEU B  1 92  ? -2.282  24.620  15.484  0.50 20.44 ? 91  LEU B CB  1 
ATOM   3866  C  CG  A LEU B  1 92  ? -1.664  23.645  16.107  0.50 22.22 ? 91  LEU B CG  1 
ATOM   3867  C  CG  B LEU B  1 92  ? -1.561  23.305  15.211  0.50 20.18 ? 91  LEU B CG  1 
ATOM   3868  C  CD1 A LEU B  1 92  ? -2.539  22.452  16.371  0.50 22.85 ? 91  LEU B CD1 1 
ATOM   3869  C  CD1 B LEU B  1 92  ? -0.877  23.473  13.872  0.50 21.02 ? 91  LEU B CD1 1 
ATOM   3870  C  CD2 A LEU B  1 92  ? -0.230  23.194  15.888  0.50 22.75 ? 91  LEU B CD2 1 
ATOM   3871  C  CD2 B LEU B  1 92  ? -0.527  23.041  16.300  0.50 20.78 ? 91  LEU B CD2 1 
ATOM   3872  N  N   . GLU B  1 93  ? -3.558  25.528  12.278  1.00 20.58 ? 92  GLU B N   1 
ATOM   3873  C  CA  . GLU B  1 93  ? -3.338  26.403  11.112  1.00 21.24 ? 92  GLU B CA  1 
ATOM   3874  C  C   . GLU B  1 93  ? -4.340  27.545  11.106  1.00 22.67 ? 92  GLU B C   1 
ATOM   3875  O  O   . GLU B  1 93  ? -3.994  28.688  10.864  1.00 22.03 ? 92  GLU B O   1 
ATOM   3876  C  CB  . GLU B  1 93  ? -3.441  25.635  9.796   1.00 21.50 ? 92  GLU B CB  1 
ATOM   3877  C  CG  . GLU B  1 93  ? -2.278  24.712  9.506   1.00 21.70 ? 92  GLU B CG  1 
ATOM   3878  C  CD  . GLU B  1 93  ? -2.426  24.063  8.148   1.00 23.02 ? 92  GLU B CD  1 
ATOM   3879  O  OE1 . GLU B  1 93  ? -2.332  24.803  7.132   1.00 23.37 ? 92  GLU B OE1 1 
ATOM   3880  O  OE2 . GLU B  1 93  ? -2.574  22.811  8.097   1.00 23.64 ? 92  GLU B OE2 1 
ATOM   3881  N  N   . PHE B  1 94  ? -5.588  27.195  11.388  1.00 23.56 ? 93  PHE B N   1 
ATOM   3882  C  CA  . PHE B  1 94  ? -6.705  28.130  11.414  1.00 25.25 ? 93  PHE B CA  1 
ATOM   3883  C  C   . PHE B  1 94  ? -7.466  27.942  12.719  1.00 25.02 ? 93  PHE B C   1 
ATOM   3884  O  O   . PHE B  1 94  ? -7.935  26.838  13.031  1.00 26.45 ? 93  PHE B O   1 
ATOM   3885  C  CB  . PHE B  1 94  ? -7.644  27.820  10.275  1.00 27.91 ? 93  PHE B CB  1 
ATOM   3886  C  CG  . PHE B  1 94  ? -7.075  28.133  8.917   1.00 29.83 ? 93  PHE B CG  1 
ATOM   3887  C  CD1 . PHE B  1 94  ? -6.918  29.434  8.502   1.00 32.68 ? 93  PHE B CD1 1 
ATOM   3888  C  CD2 . PHE B  1 94  ? -6.717  27.123  8.065   1.00 32.51 ? 93  PHE B CD2 1 
ATOM   3889  C  CE1 . PHE B  1 94  ? -6.414  29.722  7.230   1.00 35.42 ? 93  PHE B CE1 1 
ATOM   3890  C  CE2 . PHE B  1 94  ? -6.213  27.395  6.799   1.00 35.37 ? 93  PHE B CE2 1 
ATOM   3891  C  CZ  . PHE B  1 94  ? -6.051  28.701  6.385   1.00 33.33 ? 93  PHE B CZ  1 
ATOM   3892  N  N   . LEU B  1 95  ? -7.560  29.004  13.495  1.00 24.05 ? 94  LEU B N   1 
ATOM   3893  C  CA  . LEU B  1 95  ? -8.268  28.928  14.776  1.00 24.50 ? 94  LEU B CA  1 
ATOM   3894  C  C   . LEU B  1 95  ? -9.777  28.942  14.534  1.00 25.96 ? 94  LEU B C   1 
ATOM   3895  O  O   . LEU B  1 95  ? -10.537 28.349  15.300  1.00 25.43 ? 94  LEU B O   1 
ATOM   3896  C  CB  . LEU B  1 95  ? -7.843  30.071  15.678  1.00 24.36 ? 94  LEU B CB  1 
ATOM   3897  C  CG  . LEU B  1 95  ? -6.338  30.131  15.959  1.00 24.53 ? 94  LEU B CG  1 
ATOM   3898  C  CD1 . LEU B  1 95  ? -6.016  31.336  16.817  1.00 25.00 ? 94  LEU B CD1 1 
ATOM   3899  C  CD2 . LEU B  1 95  ? -5.822  28.846  16.608  1.00 24.25 ? 94  LEU B CD2 1 
ATOM   3900  N  N   . ASP B  1 96  ? -10.181 29.625  13.473  1.00 28.32 ? 95  ASP B N   1 
ATOM   3901  C  CA  . ASP B  1 96  ? -11.582 29.693  13.066  1.00 33.42 ? 95  ASP B CA  1 
ATOM   3902  C  C   . ASP B  1 96  ? -11.787 28.757  11.883  1.00 34.51 ? 95  ASP B C   1 
ATOM   3903  O  O   . ASP B  1 96  ? -11.159 28.948  10.841  1.00 33.95 ? 95  ASP B O   1 
ATOM   3904  C  CB  . ASP B  1 96  ? -11.934 31.135  12.674  1.00 36.64 ? 95  ASP B CB  1 
ATOM   3905  C  CG  . ASP B  1 96  ? -13.415 31.334  12.470  1.00 42.18 ? 95  ASP B CG  1 
ATOM   3906  O  OD1 . ASP B  1 96  ? -14.110 30.368  12.084  1.00 45.33 ? 95  ASP B OD1 1 
ATOM   3907  O  OD2 . ASP B  1 96  ? -13.890 32.465  12.685  1.00 48.18 ? 95  ASP B OD2 1 
ATOM   3908  N  N   . PRO B  1 97  ? -12.641 27.730  12.044  1.00 36.17 ? 96  PRO B N   1 
ATOM   3909  C  CA  . PRO B  1 97  ? -12.802 26.760  10.958  1.00 39.41 ? 96  PRO B CA  1 
ATOM   3910  C  C   . PRO B  1 97  ? -13.398 27.348  9.668   1.00 39.76 ? 96  PRO B C   1 
ATOM   3911  O  O   . PRO B  1 97  ? -13.343 26.689  8.652   1.00 39.41 ? 96  PRO B O   1 
ATOM   3912  C  CB  . PRO B  1 97  ? -13.730 25.675  11.550  1.00 41.33 ? 96  PRO B CB  1 
ATOM   3913  C  CG  . PRO B  1 97  ? -13.978 26.034  12.978  1.00 40.18 ? 96  PRO B CG  1 
ATOM   3914  C  CD  . PRO B  1 97  ? -13.461 27.414  13.229  1.00 38.56 ? 96  PRO B CD  1 
ATOM   3915  N  N   . SER B  1 98  ? -13.935 28.568  9.708   1.00 40.82 ? 97  SER B N   1 
ATOM   3916  C  CA  . SER B  1 98  ? -14.275 29.293  8.480   1.00 44.80 ? 97  SER B CA  1 
ATOM   3917  C  C   . SER B  1 98  ? -13.029 29.635  7.655   1.00 47.66 ? 97  SER B C   1 
ATOM   3918  O  O   . SER B  1 98  ? -13.144 30.011  6.492   1.00 47.37 ? 97  SER B O   1 
ATOM   3919  C  CB  . SER B  1 98  ? -14.991 30.598  8.802   1.00 46.07 ? 97  SER B CB  1 
ATOM   3920  O  OG  . SER B  1 98  ? -14.059 31.559  9.281   1.00 47.63 ? 97  SER B OG  1 
ATOM   3921  N  N   . LYS B  1 99  ? -11.851 29.528  8.277   1.00 46.60 ? 98  LYS B N   1 
ATOM   3922  C  CA  . LYS B  1 99  ? -10.555 29.801  7.652   1.00 47.58 ? 98  LYS B CA  1 
ATOM   3923  C  C   . LYS B  1 99  ? -10.374 31.272  7.340   1.00 47.66 ? 98  LYS B C   1 
ATOM   3924  O  O   . LYS B  1 99  ? -9.583  31.650  6.488   1.00 46.97 ? 98  LYS B O   1 
ATOM   3925  C  CB  . LYS B  1 99  ? -10.321 28.933  6.422   1.00 50.88 ? 98  LYS B CB  1 
ATOM   3926  C  CG  . LYS B  1 99  ? -10.380 27.457  6.748   1.00 52.67 ? 98  LYS B CG  1 
ATOM   3927  C  CD  . LYS B  1 99  ? -10.005 26.622  5.548   1.00 57.23 ? 98  LYS B CD  1 
ATOM   3928  C  CE  . LYS B  1 99  ? -9.935  25.155  5.927   1.00 60.55 ? 98  LYS B CE  1 
ATOM   3929  N  NZ  . LYS B  1 99  ? -9.496  24.331  4.767   1.00 63.95 ? 98  LYS B NZ  1 
ATOM   3930  N  N   . SER B  1 100 ? -11.069 32.094  8.104   1.00 49.44 ? 99  SER B N   1 
ATOM   3931  C  CA  . SER B  1 100 ? -10.878 33.522  8.070   1.00 52.41 ? 99  SER B CA  1 
ATOM   3932  C  C   . SER B  1 100 ? -9.435  33.908  8.430   1.00 54.23 ? 99  SER B C   1 
ATOM   3933  O  O   . SER B  1 100 ? -8.802  33.289  9.311   1.00 50.92 ? 99  SER B O   1 
ATOM   3934  C  CB  . SER B  1 100 ? -11.840 34.169  9.067   1.00 54.73 ? 99  SER B CB  1 
ATOM   3935  O  OG  . SER B  1 100 ? -11.541 35.540  9.204   1.00 58.71 ? 99  SER B OG  1 
ATOM   3936  N  N   . SER B  1 101 ? -8.942  34.976  7.805   1.00 52.97 ? 100 SER B N   1 
ATOM   3937  C  CA  . SER B  1 101 ? -7.577  35.466  8.057   1.00 51.05 ? 100 SER B CA  1 
ATOM   3938  C  C   . SER B  1 101 ? -7.356  35.886  9.510   1.00 46.89 ? 100 SER B C   1 
ATOM   3939  O  O   . SER B  1 101 ? -6.242  35.781  10.030  1.00 41.15 ? 100 SER B O   1 
ATOM   3940  C  CB  . SER B  1 101 ? -7.243  36.638  7.143   1.00 53.58 ? 100 SER B CB  1 
ATOM   3941  O  OG  . SER B  1 101 ? -8.094  37.734  7.415   1.00 55.86 ? 100 SER B OG  1 
ATOM   3942  N  N   . VAL B  1 102 ? -8.421  36.311  10.181  1.00 43.73 ? 101 VAL B N   1 
ATOM   3943  C  CA  . VAL B  1 102 ? -8.353  36.648  11.598  1.00 42.55 ? 101 VAL B CA  1 
ATOM   3944  C  C   . VAL B  1 102 ? -7.796  35.476  12.434  1.00 37.24 ? 101 VAL B C   1 
ATOM   3945  O  O   . VAL B  1 102 ? -7.147  35.694  13.449  1.00 38.51 ? 101 VAL B O   1 
ATOM   3946  C  CB  . VAL B  1 102 ? -9.756  37.040  12.125  1.00 44.22 ? 101 VAL B CB  1 
ATOM   3947  C  CG1 . VAL B  1 102 ? -9.707  37.419  13.590  1.00 45.77 ? 101 VAL B CG1 1 
ATOM   3948  C  CG2 . VAL B  1 102 ? -10.379 38.179  11.318  1.00 47.99 ? 101 VAL B CG2 1 
ATOM   3949  N  N   . GLY B  1 103 ? -8.095  34.241  12.058  1.00 33.44 ? 102 GLY B N   1 
ATOM   3950  C  CA  . GLY B  1 103 ? -7.632  33.080  12.838  1.00 30.86 ? 102 GLY B CA  1 
ATOM   3951  C  C   . GLY B  1 103 ? -6.434  32.371  12.218  1.00 27.69 ? 102 GLY B C   1 
ATOM   3952  O  O   . GLY B  1 103 ? -6.092  31.289  12.660  1.00 26.35 ? 102 GLY B O   1 
ATOM   3953  N  N   . SER B  1 104 ? -5.776  32.968  11.219  1.00 26.81 ? 103 SER B N   1 
ATOM   3954  C  CA  . SER B  1 104 ? -4.637  32.308  10.558  1.00 26.25 ? 103 SER B CA  1 
ATOM   3955  C  C   . SER B  1 104 ? -3.435  32.351  11.489  1.00 25.24 ? 103 SER B C   1 
ATOM   3956  O  O   . SER B  1 104 ? -2.974  33.427  11.844  1.00 27.69 ? 103 SER B O   1 
ATOM   3957  C  CB  . SER B  1 104 ? -4.306  32.969  9.214   1.00 27.42 ? 103 SER B CB  1 
ATOM   3958  O  OG  . SER B  1 104 ? -3.200  32.329  8.601   1.00 26.70 ? 103 SER B OG  1 
ATOM   3959  N  N   . TYR B  1 105 ? -2.967  31.191  11.940  1.00 23.02 ? 104 TYR B N   1 
ATOM   3960  C  CA  . TYR B  1 105 ? -1.983  31.123  13.008  1.00 21.96 ? 104 TYR B CA  1 
ATOM   3961  C  C   . TYR B  1 105 ? -0.740  30.363  12.510  1.00 21.48 ? 104 TYR B C   1 
ATOM   3962  O  O   . TYR B  1 105 ? 0.222   30.990  12.088  1.00 21.84 ? 104 TYR B O   1 
ATOM   3963  C  CB  . TYR B  1 105 ? -2.622  30.521  14.272  1.00 20.84 ? 104 TYR B CB  1 
ATOM   3964  C  CG  . TYR B  1 105 ? -1.711  30.378  15.457  1.00 20.88 ? 104 TYR B CG  1 
ATOM   3965  C  CD1 . TYR B  1 105 ? -0.871  31.431  15.861  1.00 21.64 ? 104 TYR B CD1 1 
ATOM   3966  C  CD2 . TYR B  1 105 ? -1.704  29.210  16.215  1.00 20.02 ? 104 TYR B CD2 1 
ATOM   3967  C  CE1 . TYR B  1 105 ? -0.040  31.299  16.957  1.00 21.97 ? 104 TYR B CE1 1 
ATOM   3968  C  CE2 . TYR B  1 105 ? -0.882  29.067  17.316  1.00 19.97 ? 104 TYR B CE2 1 
ATOM   3969  C  CZ  . TYR B  1 105 ? -0.037  30.102  17.692  1.00 21.19 ? 104 TYR B CZ  1 
ATOM   3970  O  OH  . TYR B  1 105 ? 0.791   29.947  18.775  1.00 19.81 ? 104 TYR B OH  1 
ATOM   3971  N  N   . PHE B  1 106 ? -0.771  29.029  12.480  1.00 20.44 ? 105 PHE B N   1 
ATOM   3972  C  CA  . PHE B  1 106 ? 0.338   28.271  11.892  1.00 20.15 ? 105 PHE B CA  1 
ATOM   3973  C  C   . PHE B  1 106 ? 0.209   28.057  10.384  1.00 20.40 ? 105 PHE B C   1 
ATOM   3974  O  O   . PHE B  1 106 ? 1.067   27.393  9.775   1.00 19.61 ? 105 PHE B O   1 
ATOM   3975  C  CB  . PHE B  1 106 ? 0.486   26.886  12.576  1.00 20.81 ? 105 PHE B CB  1 
ATOM   3976  C  CG  . PHE B  1 106 ? 1.418   26.867  13.748  1.00 21.74 ? 105 PHE B CG  1 
ATOM   3977  C  CD1 . PHE B  1 106 ? 2.778   26.593  13.590  1.00 25.10 ? 105 PHE B CD1 1 
ATOM   3978  C  CD2 . PHE B  1 106 ? 0.947   27.094  15.007  1.00 25.00 ? 105 PHE B CD2 1 
ATOM   3979  C  CE1 . PHE B  1 106 ? 3.640   26.559  14.688  1.00 25.96 ? 105 PHE B CE1 1 
ATOM   3980  C  CE2 . PHE B  1 106 ? 1.798   27.050  16.119  1.00 25.69 ? 105 PHE B CE2 1 
ATOM   3981  C  CZ  . PHE B  1 106 ? 3.135   26.772  15.965  1.00 24.05 ? 105 PHE B CZ  1 
ATOM   3982  N  N   . HIS B  1 107 ? -0.844  28.584  9.757   1.00 20.85 ? 106 HIS B N   1 
ATOM   3983  C  CA  . HIS B  1 107 ? -1.087  28.289  8.350   1.00 21.38 ? 106 HIS B CA  1 
ATOM   3984  C  C   . HIS B  1 107 ? 0.082   28.644  7.428   1.00 21.28 ? 106 HIS B C   1 
ATOM   3985  O  O   . HIS B  1 107 ? 0.435   27.850  6.566   1.00 19.76 ? 106 HIS B O   1 
ATOM   3986  C  CB  . HIS B  1 107 ? -2.354  28.955  7.820   1.00 22.80 ? 106 HIS B CB  1 
ATOM   3987  C  CG  . HIS B  1 107 ? -2.679  28.572  6.412   1.00 24.35 ? 106 HIS B CG  1 
ATOM   3988  N  ND1 . HIS B  1 107 ? -2.805  27.257  6.017   1.00 25.29 ? 106 HIS B ND1 1 
ATOM   3989  C  CD2 . HIS B  1 107 ? -2.863  29.321  5.301   1.00 26.01 ? 106 HIS B CD2 1 
ATOM   3990  C  CE1 . HIS B  1 107 ? -3.085  27.216  4.726   1.00 26.66 ? 106 HIS B CE1 1 
ATOM   3991  N  NE2 . HIS B  1 107 ? -3.113  28.455  4.265   1.00 27.74 ? 106 HIS B NE2 1 
ATOM   3992  N  N   . THR B  1 108 ? 0.643   29.830  7.584   1.00 21.33 ? 107 THR B N   1 
ATOM   3993  C  CA  . THR B  1 108 ? 1.724   30.244  6.684   1.00 22.25 ? 107 THR B CA  1 
ATOM   3994  C  C   . THR B  1 108 ? 2.915   29.289  6.839   1.00 21.47 ? 107 THR B C   1 
ATOM   3995  O  O   . THR B  1 108 ? 3.502   28.889  5.846   1.00 22.25 ? 107 THR B O   1 
ATOM   3996  C  CB  . THR B  1 108 ? 2.157   31.707  6.945   1.00 22.98 ? 107 THR B CB  1 
ATOM   3997  O  OG1 . THR B  1 108 ? 1.036   32.573  6.728   1.00 23.67 ? 107 THR B OG1 1 
ATOM   3998  C  CG2 . THR B  1 108 ? 3.276   32.124  6.019   1.00 24.21 ? 107 THR B CG2 1 
ATOM   3999  N  N   . MET B  1 109 ? 3.245   28.917  8.069   1.00 20.54 ? 108 MET B N   1 
ATOM   4000  C  CA  . MET B  1 109 ? 4.362   28.008  8.313   1.00 21.40 ? 108 MET B CA  1 
ATOM   4001  C  C   . MET B  1 109 ? 4.105   26.599  7.754   1.00 20.66 ? 108 MET B C   1 
ATOM   4002  O  O   . MET B  1 109 ? 4.969   26.032  7.111   1.00 21.27 ? 108 MET B O   1 
ATOM   4003  C  CB  . MET B  1 109 ? 4.685   27.898  9.798   1.00 21.58 ? 108 MET B CB  1 
ATOM   4004  C  CG  . MET B  1 109 ? 5.800   26.904  10.094  1.00 22.78 ? 108 MET B CG  1 
ATOM   4005  S  SD  . MET B  1 109 ? 6.242   26.841  11.850  1.00 26.52 ? 108 MET B SD  1 
ATOM   4006  C  CE  . MET B  1 109 ? 6.916   28.466  12.006  1.00 26.19 ? 108 MET B CE  1 
ATOM   4007  N  N   . VAL B  1 110 ? 2.901   26.067  7.951   1.00 20.31 ? 109 VAL B N   1 
ATOM   4008  C  CA  . VAL B  1 110 ? 2.569   24.754  7.402   1.00 20.82 ? 109 VAL B CA  1 
ATOM   4009  C  C   . VAL B  1 110 ? 2.543   24.770  5.878   1.00 21.38 ? 109 VAL B C   1 
ATOM   4010  O  O   . VAL B  1 110 ? 3.032   23.818  5.253   1.00 20.92 ? 109 VAL B O   1 
ATOM   4011  C  CB  . VAL B  1 110 ? 1.265   24.183  7.972   1.00 20.46 ? 109 VAL B CB  1 
ATOM   4012  C  CG1 . VAL B  1 110 ? 0.912   22.832  7.334   1.00 21.19 ? 109 VAL B CG1 1 
ATOM   4013  C  CG2 . VAL B  1 110 ? 1.427   24.009  9.456   1.00 20.50 ? 109 VAL B CG2 1 
ATOM   4014  N  N   . GLU B  1 111 ? 2.009   25.832  5.266   1.00 23.10 ? 110 GLU B N   1 
ATOM   4015  C  CA  . GLU B  1 111 ? 2.082   25.973  3.814   1.00 26.06 ? 110 GLU B CA  1 
ATOM   4016  C  C   . GLU B  1 111 ? 3.520   25.887  3.339   1.00 24.57 ? 110 GLU B C   1 
ATOM   4017  O  O   . GLU B  1 111 ? 3.791   25.263  2.320   1.00 22.31 ? 110 GLU B O   1 
ATOM   4018  C  CB  . GLU B  1 111 ? 1.490   27.298  3.319   1.00 31.06 ? 110 GLU B CB  1 
ATOM   4019  C  CG  . GLU B  1 111 ? -0.020  27.297  3.337   1.00 36.45 ? 110 GLU B CG  1 
ATOM   4020  C  CD  . GLU B  1 111 ? -0.617  26.482  2.211   1.00 42.11 ? 110 GLU B CD  1 
ATOM   4021  O  OE1 . GLU B  1 111 ? -0.667  27.002  1.073   1.00 53.98 ? 110 GLU B OE1 1 
ATOM   4022  O  OE2 . GLU B  1 111 ? -1.083  25.361  2.457   1.00 40.42 ? 110 GLU B OE2 1 
ATOM   4023  N  N   . SER B  1 112 ? 4.425   26.576  4.035   1.00 23.35 ? 111 SER B N   1 
ATOM   4024  C  CA  . SER B  1 112 ? 5.856   26.525  3.676   1.00 23.88 ? 111 SER B CA  1 
ATOM   4025  C  C   . SER B  1 112 ? 6.415   25.109  3.792   1.00 21.91 ? 111 SER B C   1 
ATOM   4026  O  O   . SER B  1 112 ? 7.085   24.629  2.868   1.00 22.08 ? 111 SER B O   1 
ATOM   4027  C  CB  . SER B  1 112 ? 6.672   27.463  4.541   1.00 25.27 ? 111 SER B CB  1 
ATOM   4028  O  OG  . SER B  1 112 ? 6.375   28.804  4.198   1.00 28.18 ? 111 SER B OG  1 
ATOM   4029  N  N   . LEU B  1 113 ? 6.132   24.457  4.922   1.00 20.15 ? 112 LEU B N   1 
ATOM   4030  C  CA  . LEU B  1 113 ? 6.592   23.070  5.143   1.00 20.25 ? 112 LEU B CA  1 
ATOM   4031  C  C   . LEU B  1 113 ? 6.100   22.144  4.039   1.00 19.65 ? 112 LEU B C   1 
ATOM   4032  O  O   . LEU B  1 113 ? 6.868   21.361  3.484   1.00 19.00 ? 112 LEU B O   1 
ATOM   4033  C  CB  . LEU B  1 113 ? 6.138   22.556  6.491   1.00 20.11 ? 112 LEU B CB  1 
ATOM   4034  C  CG  . LEU B  1 113 ? 6.855   23.163  7.699   1.00 21.59 ? 112 LEU B CG  1 
ATOM   4035  C  CD1 . LEU B  1 113 ? 6.054   22.919  8.964   1.00 22.05 ? 112 LEU B CD1 1 
ATOM   4036  C  CD2 . LEU B  1 113 ? 8.234   22.560  7.846   1.00 22.68 ? 112 LEU B CD2 1 
ATOM   4037  N  N   . VAL B  1 114 ? 4.821   22.270  3.695   1.00 20.02 ? 113 VAL B N   1 
ATOM   4038  C  CA  . VAL B  1 114 ? 4.219   21.450  2.648   1.00 21.32 ? 113 VAL B CA  1 
ATOM   4039  C  C   . VAL B  1 114 ? 4.864   21.763  1.273   1.00 22.43 ? 113 VAL B C   1 
ATOM   4040  O  O   . VAL B  1 114 ? 5.203   20.857  0.511   1.00 22.48 ? 113 VAL B O   1 
ATOM   4041  C  CB  . VAL B  1 114 ? 2.683   21.609  2.670   1.00 21.29 ? 113 VAL B CB  1 
ATOM   4042  C  CG1 . VAL B  1 114 ? 2.064   21.046  1.397   1.00 22.59 ? 113 VAL B CG1 1 
ATOM   4043  C  CG2 . VAL B  1 114 ? 2.129   20.934  3.909   1.00 20.50 ? 113 VAL B CG2 1 
ATOM   4044  N  N   . GLY B  1 115 ? 5.130   23.042  0.999   1.00 23.36 ? 114 GLY B N   1 
ATOM   4045  C  CA  . GLY B  1 115 ? 5.888   23.415  -0.193  1.00 25.12 ? 114 GLY B CA  1 
ATOM   4046  C  C   . GLY B  1 115 ? 7.296   22.825  -0.235  1.00 25.37 ? 114 GLY B C   1 
ATOM   4047  O  O   . GLY B  1 115 ? 7.821   22.592  -1.304  1.00 28.09 ? 114 GLY B O   1 
ATOM   4048  N  N   . TRP B  1 116 ? 7.908   22.581  0.931   1.00 24.53 ? 115 TRP B N   1 
ATOM   4049  C  CA  . TRP B  1 116 ? 9.230   21.930  1.048   1.00 24.50 ? 115 TRP B CA  1 
ATOM   4050  C  C   . TRP B  1 116 ? 9.161   20.420  1.004   1.00 24.09 ? 115 TRP B C   1 
ATOM   4051  O  O   . TRP B  1 116 ? 10.203  19.761  1.081   1.00 25.42 ? 115 TRP B O   1 
ATOM   4052  C  CB  . TRP B  1 116 ? 9.952   22.326  2.355   1.00 24.40 ? 115 TRP B CB  1 
ATOM   4053  C  CG  . TRP B  1 116 ? 10.113  23.789  2.513   1.00 25.63 ? 115 TRP B CG  1 
ATOM   4054  C  CD1 . TRP B  1 116 ? 10.174  24.732  1.520   1.00 26.69 ? 115 TRP B CD1 1 
ATOM   4055  C  CD2 . TRP B  1 116 ? 10.257  24.492  3.745   1.00 25.28 ? 115 TRP B CD2 1 
ATOM   4056  N  NE1 . TRP B  1 116 ? 10.319  25.984  2.073   1.00 28.32 ? 115 TRP B NE1 1 
ATOM   4057  C  CE2 . TRP B  1 116 ? 10.376  25.864  3.435   1.00 26.87 ? 115 TRP B CE2 1 
ATOM   4058  C  CE3 . TRP B  1 116 ? 10.313  24.095  5.079   1.00 25.64 ? 115 TRP B CE3 1 
ATOM   4059  C  CZ2 . TRP B  1 116 ? 10.530  26.845  4.424   1.00 27.28 ? 115 TRP B CZ2 1 
ATOM   4060  C  CZ3 . TRP B  1 116 ? 10.439  25.066  6.064   1.00 25.76 ? 115 TRP B CZ3 1 
ATOM   4061  C  CH2 . TRP B  1 116 ? 10.555  26.429  5.724   1.00 26.28 ? 115 TRP B CH2 1 
ATOM   4062  N  N   . GLY B  1 117 ? 7.956   19.863  0.914   1.00 22.66 ? 116 GLY B N   1 
ATOM   4063  C  CA  . GLY B  1 117 ? 7.793   18.429  0.767   1.00 22.26 ? 116 GLY B CA  1 
ATOM   4064  C  C   . GLY B  1 117 ? 7.138   17.670  1.903   1.00 20.80 ? 116 GLY B C   1 
ATOM   4065  O  O   . GLY B  1 117 ? 7.039   16.432  1.816   1.00 21.14 ? 116 GLY B O   1 
ATOM   4066  N  N   . TYR B  1 118 ? 6.706   18.373  2.959   1.00 20.29 ? 117 TYR B N   1 
ATOM   4067  C  CA  . TYR B  1 118 ? 6.042   17.742  4.097   1.00 19.39 ? 117 TYR B CA  1 
ATOM   4068  C  C   . TYR B  1 118 ? 4.600   17.423  3.758   1.00 19.48 ? 117 TYR B C   1 
ATOM   4069  O  O   . TYR B  1 118 ? 4.042   18.020  2.840   1.00 19.42 ? 117 TYR B O   1 
ATOM   4070  C  CB  . TYR B  1 118 ? 6.116   18.634  5.353   1.00 20.21 ? 117 TYR B CB  1 
ATOM   4071  C  CG  . TYR B  1 118 ? 7.483   18.571  6.020   1.00 20.17 ? 117 TYR B CG  1 
ATOM   4072  C  CD1 . TYR B  1 118 ? 8.538   19.368  5.589   1.00 21.23 ? 117 TYR B CD1 1 
ATOM   4073  C  CD2 . TYR B  1 118 ? 7.728   17.682  7.062   1.00 21.03 ? 117 TYR B CD2 1 
ATOM   4074  C  CE1 . TYR B  1 118 ? 9.792   19.289  6.186   1.00 21.33 ? 117 TYR B CE1 1 
ATOM   4075  C  CE2 . TYR B  1 118 ? 8.980   17.611  7.682   1.00 20.33 ? 117 TYR B CE2 1 
ATOM   4076  C  CZ  . TYR B  1 118 ? 10.021  18.394  7.217   1.00 21.45 ? 117 TYR B CZ  1 
ATOM   4077  O  OH  . TYR B  1 118 ? 11.285  18.326  7.836   1.00 21.51 ? 117 TYR B OH  1 
ATOM   4078  N  N   . THR B  1 119 ? 4.033   16.483  4.513   1.00 18.55 ? 118 THR B N   1 
ATOM   4079  C  CA  . THR B  1 119 ? 2.684   15.954  4.314   1.00 18.37 ? 118 THR B CA  1 
ATOM   4080  C  C   . THR B  1 119 ? 1.903   16.048  5.651   1.00 17.99 ? 118 THR B C   1 
ATOM   4081  O  O   . THR B  1 119 ? 2.311   15.451  6.640   1.00 17.71 ? 118 THR B O   1 
ATOM   4082  C  CB  . THR B  1 119 ? 2.745   14.490  3.832   1.00 18.43 ? 118 THR B CB  1 
ATOM   4083  O  OG1 . THR B  1 119 ? 3.402   14.428  2.557   1.00 18.64 ? 118 THR B OG1 1 
ATOM   4084  C  CG2 . THR B  1 119 ? 1.340   13.897  3.662   1.00 18.64 ? 118 THR B CG2 1 
ATOM   4085  N  N   . ARG B  1 120 ? 0.810   16.808  5.656   1.00 18.04 ? 119 ARG B N   1 
ATOM   4086  C  CA  . ARG B  1 120 ? 0.019   17.030  6.855   1.00 18.97 ? 119 ARG B CA  1 
ATOM   4087  C  C   . ARG B  1 120 ? -0.440  15.695  7.419   1.00 18.84 ? 119 ARG B C   1 
ATOM   4088  O  O   . ARG B  1 120 ? -0.969  14.847  6.695   1.00 17.99 ? 119 ARG B O   1 
ATOM   4089  C  CB  . ARG B  1 120 ? -1.192  17.902  6.570   1.00 20.35 ? 119 ARG B CB  1 
ATOM   4090  C  CG  . ARG B  1 120 ? -0.903  19.377  6.290   1.00 20.19 ? 119 ARG B CG  1 
ATOM   4091  C  CD  . ARG B  1 120 ? -2.194  20.048  5.809   1.00 21.66 ? 119 ARG B CD  1 
ATOM   4092  N  NE  . ARG B  1 120 ? -2.041  21.485  5.664   1.00 21.79 ? 119 ARG B NE  1 
ATOM   4093  C  CZ  . ARG B  1 120 ? -1.688  22.117  4.545   1.00 23.25 ? 119 ARG B CZ  1 
ATOM   4094  N  NH1 . ARG B  1 120 ? -1.443  21.465  3.416   1.00 24.65 ? 119 ARG B NH1 1 
ATOM   4095  N  NH2 . ARG B  1 120 ? -1.602  23.454  4.557   1.00 23.74 ? 119 ARG B NH2 1 
ATOM   4096  N  N   . GLY B  1 121 ? -0.219  15.516  8.702   1.00 18.12 ? 120 GLY B N   1 
ATOM   4097  C  CA  . GLY B  1 121 ? -0.701  14.330  9.381   1.00 19.19 ? 120 GLY B CA  1 
ATOM   4098  C  C   . GLY B  1 121 ? 0.231   13.150  9.274   1.00 20.41 ? 120 GLY B C   1 
ATOM   4099  O  O   . GLY B  1 121 ? -0.029  12.112  9.887   1.00 19.94 ? 120 GLY B O   1 
ATOM   4100  N  N   . GLU B  1 122 ? 1.303   13.296  8.492   1.00 21.06 ? 121 GLU B N   1 
ATOM   4101  C  CA  . GLU B  1 122 ? 2.297   12.248  8.324   1.00 21.75 ? 121 GLU B CA  1 
ATOM   4102  C  C   . GLU B  1 122 ? 3.612   12.735  8.948   1.00 19.94 ? 121 GLU B C   1 
ATOM   4103  O  O   . GLU B  1 122 ? 3.802   12.584  10.164  1.00 19.09 ? 121 GLU B O   1 
ATOM   4104  C  CB  . GLU B  1 122 ? 2.407   11.824  6.860   1.00 25.13 ? 121 GLU B CB  1 
ATOM   4105  C  CG  . GLU B  1 122 ? 1.108   11.139  6.356   1.00 29.30 ? 121 GLU B CG  1 
ATOM   4106  C  CD  . GLU B  1 122 ? 1.310   10.347  5.040   1.00 36.96 ? 121 GLU B CD  1 
ATOM   4107  O  OE1 . GLU B  1 122 ? 0.345   9.999   4.284   1.00 41.77 ? 121 GLU B OE1 1 
ATOM   4108  O  OE2 . GLU B  1 122 ? 2.489   10.064  4.706   1.00 42.24 ? 121 GLU B OE2 1 
ATOM   4109  N  N   . ASP B  1 123 ? 4.474   13.370  8.169   1.00 18.58 ? 122 ASP B N   1 
ATOM   4110  C  CA  . ASP B  1 123 ? 5.763   13.815  8.721   1.00 18.66 ? 122 ASP B CA  1 
ATOM   4111  C  C   . ASP B  1 123 ? 5.752   15.235  9.312   1.00 17.89 ? 122 ASP B C   1 
ATOM   4112  O  O   . ASP B  1 123 ? 6.774   15.690  9.834   1.00 17.37 ? 122 ASP B O   1 
ATOM   4113  C  CB  . ASP B  1 123 ? 6.896   13.593  7.721   1.00 20.19 ? 122 ASP B CB  1 
ATOM   4114  C  CG  . ASP B  1 123 ? 6.650   14.263  6.375   1.00 21.63 ? 122 ASP B CG  1 
ATOM   4115  O  OD1 . ASP B  1 123 ? 5.599   14.926  6.211   1.00 22.21 ? 122 ASP B OD1 1 
ATOM   4116  O  OD2 . ASP B  1 123 ? 7.494   14.105  5.487   1.00 23.74 ? 122 ASP B OD2 1 
ATOM   4117  N  N   . VAL B  1 124 ? 4.619   15.937  9.223   1.00 16.87 ? 123 VAL B N   1 
ATOM   4118  C  CA  . VAL B  1 124 ? 4.377   17.130  10.040  1.00 17.01 ? 123 VAL B CA  1 
ATOM   4119  C  C   . VAL B  1 124 ? 3.049   16.940  10.761  1.00 16.86 ? 123 VAL B C   1 
ATOM   4120  O  O   . VAL B  1 124 ? 2.014   16.663  10.143  1.00 17.94 ? 123 VAL B O   1 
ATOM   4121  C  CB  . VAL B  1 124 ? 4.422   18.475  9.288   1.00 18.02 ? 123 VAL B CB  1 
ATOM   4122  C  CG1 . VAL B  1 124 ? 3.403   18.532  8.156   1.00 19.04 ? 123 VAL B CG1 1 
ATOM   4123  C  CG2 . VAL B  1 124 ? 4.214   19.628  10.272  1.00 18.11 ? 123 VAL B CG2 1 
ATOM   4124  N  N   . ARG B  1 125 ? 3.097   17.012  12.080  1.00 16.45 ? 124 ARG B N   1 
ATOM   4125  C  CA  . ARG B  1 125 ? 1.907   16.797  12.904  1.00 17.05 ? 124 ARG B CA  1 
ATOM   4126  C  C   . ARG B  1 125 ? 1.819   17.888  13.985  1.00 17.19 ? 124 ARG B C   1 
ATOM   4127  O  O   . ARG B  1 125 ? 2.831   18.349  14.501  1.00 16.92 ? 124 ARG B O   1 
ATOM   4128  C  CB  . ARG B  1 125 ? 1.940   15.427  13.572  1.00 17.21 ? 124 ARG B CB  1 
ATOM   4129  C  CG  . ARG B  1 125 ? 2.045   14.259  12.611  1.00 18.72 ? 124 ARG B CG  1 
ATOM   4130  C  CD  . ARG B  1 125 ? 1.843   12.917  13.275  1.00 18.86 ? 124 ARG B CD  1 
ATOM   4131  N  NE  . ARG B  1 125 ? 2.253   11.823  12.395  1.00 19.41 ? 124 ARG B NE  1 
ATOM   4132  C  CZ  . ARG B  1 125 ? 2.099   10.530  12.673  1.00 21.59 ? 124 ARG B CZ  1 
ATOM   4133  N  NH1 . ARG B  1 125 ? 1.513   10.169  13.818  1.00 22.39 ? 124 ARG B NH1 1 
ATOM   4134  N  NH2 . ARG B  1 125 ? 2.533   9.601   11.818  1.00 21.68 ? 124 ARG B NH2 1 
ATOM   4135  N  N   . GLY B  1 126 ? 0.605   18.293  14.300  1.00 16.96 ? 125 GLY B N   1 
ATOM   4136  C  CA  . GLY B  1 126 ? 0.360   19.200  15.424  1.00 17.62 ? 125 GLY B CA  1 
ATOM   4137  C  C   . GLY B  1 126 ? 0.147   18.477  16.748  1.00 17.54 ? 125 GLY B C   1 
ATOM   4138  O  O   . GLY B  1 126 ? -0.379  17.343  16.786  1.00 17.41 ? 125 GLY B O   1 
ATOM   4139  N  N   . ALA B  1 127 ? 0.539   19.156  17.826  1.00 15.80 ? 126 ALA B N   1 
ATOM   4140  C  CA  . ALA B  1 127 ? 0.287   18.722  19.181  1.00 15.77 ? 126 ALA B CA  1 
ATOM   4141  C  C   . ALA B  1 127 ? -0.545  19.787  19.933  1.00 15.76 ? 126 ALA B C   1 
ATOM   4142  O  O   . ALA B  1 127 ? -0.077  20.420  20.882  1.00 16.07 ? 126 ALA B O   1 
ATOM   4143  C  CB  . ALA B  1 127 ? 1.596   18.445  19.877  1.00 15.17 ? 126 ALA B CB  1 
ATOM   4144  N  N   . PRO B  1 128 ? -1.792  20.013  19.472  1.00 16.21 ? 127 PRO B N   1 
ATOM   4145  C  CA  . PRO B  1 128 ? -2.701  20.910  20.206  1.00 16.52 ? 127 PRO B CA  1 
ATOM   4146  C  C   . PRO B  1 128 ? -3.074  20.398  21.615  1.00 16.52 ? 127 PRO B C   1 
ATOM   4147  O  O   . PRO B  1 128 ? -3.054  19.189  21.881  1.00 15.98 ? 127 PRO B O   1 
ATOM   4148  C  CB  . PRO B  1 128 ? -3.964  20.941  19.314  1.00 16.39 ? 127 PRO B CB  1 
ATOM   4149  C  CG  . PRO B  1 128 ? -3.964  19.595  18.669  1.00 16.69 ? 127 PRO B CG  1 
ATOM   4150  C  CD  . PRO B  1 128 ? -2.503  19.315  18.384  1.00 15.82 ? 127 PRO B CD  1 
ATOM   4151  N  N   . TYR B  1 129 ? -3.447  21.325  22.498  1.00 16.23 ? 128 TYR B N   1 
ATOM   4152  C  CA  . TYR B  1 129 ? -3.784  20.979  23.869  1.00 16.65 ? 128 TYR B CA  1 
ATOM   4153  C  C   . TYR B  1 129 ? -4.802  21.962  24.442  1.00 16.19 ? 128 TYR B C   1 
ATOM   4154  O  O   . TYR B  1 129 ? -5.101  22.980  23.821  1.00 15.70 ? 128 TYR B O   1 
ATOM   4155  C  CB  . TYR B  1 129 ? -2.514  20.929  24.749  1.00 16.22 ? 128 TYR B CB  1 
ATOM   4156  C  CG  . TYR B  1 129 ? -1.711  22.213  24.741  1.00 15.99 ? 128 TYR B CG  1 
ATOM   4157  C  CD1 . TYR B  1 129 ? -0.810  22.495  23.711  1.00 16.28 ? 128 TYR B CD1 1 
ATOM   4158  C  CD2 . TYR B  1 129 ? -1.829  23.150  25.782  1.00 15.78 ? 128 TYR B CD2 1 
ATOM   4159  C  CE1 . TYR B  1 129 ? -0.070  23.678  23.709  1.00 16.45 ? 128 TYR B CE1 1 
ATOM   4160  C  CE2 . TYR B  1 129 ? -1.113  24.329  25.770  1.00 15.22 ? 128 TYR B CE2 1 
ATOM   4161  C  CZ  . TYR B  1 129 ? -0.230  24.602  24.741  1.00 16.41 ? 128 TYR B CZ  1 
ATOM   4162  O  OH  . TYR B  1 129 ? 0.490   25.797  24.715  1.00 16.35 ? 128 TYR B OH  1 
ATOM   4163  N  N   . ASP B  1 130 ? -5.340  21.636  25.625  1.00 16.09 ? 129 ASP B N   1 
ATOM   4164  C  CA  . ASP B  1 130 ? -6.270  22.536  26.296  1.00 17.29 ? 129 ASP B CA  1 
ATOM   4165  C  C   . ASP B  1 130 ? -5.428  23.622  26.981  1.00 16.42 ? 129 ASP B C   1 
ATOM   4166  O  O   . ASP B  1 130 ? -4.953  23.453  28.110  1.00 17.28 ? 129 ASP B O   1 
ATOM   4167  C  CB  . ASP B  1 130 ? -7.127  21.796  27.308  1.00 18.35 ? 129 ASP B CB  1 
ATOM   4168  C  CG  . ASP B  1 130 ? -8.207  22.679  27.894  1.00 20.83 ? 129 ASP B CG  1 
ATOM   4169  O  OD1 . ASP B  1 130 ? -8.113  23.941  27.781  1.00 20.27 ? 129 ASP B OD1 1 
ATOM   4170  O  OD2 . ASP B  1 130 ? -9.169  22.108  28.458  1.00 21.51 ? 129 ASP B OD2 1 
ATOM   4171  N  N   . TRP B  1 131 ? -5.199  24.700  26.248  1.00 15.82 ? 130 TRP B N   1 
ATOM   4172  C  CA  . TRP B  1 131 ? -4.303  25.776  26.663  1.00 15.87 ? 130 TRP B CA  1 
ATOM   4173  C  C   . TRP B  1 131 ? -4.843  26.631  27.813  1.00 16.84 ? 130 TRP B C   1 
ATOM   4174  O  O   . TRP B  1 131 ? -4.145  27.532  28.276  1.00 16.75 ? 130 TRP B O   1 
ATOM   4175  C  CB  . TRP B  1 131 ? -3.942  26.674  25.455  1.00 16.47 ? 130 TRP B CB  1 
ATOM   4176  C  CG  . TRP B  1 131 ? -5.071  26.864  24.491  1.00 16.37 ? 130 TRP B CG  1 
ATOM   4177  C  CD1 . TRP B  1 131 ? -5.220  26.247  23.276  1.00 16.61 ? 130 TRP B CD1 1 
ATOM   4178  C  CD2 . TRP B  1 131 ? -6.236  27.688  24.660  1.00 16.73 ? 130 TRP B CD2 1 
ATOM   4179  N  NE1 . TRP B  1 131 ? -6.375  26.646  22.682  1.00 17.37 ? 130 TRP B NE1 1 
ATOM   4180  C  CE2 . TRP B  1 131 ? -7.029  27.523  23.505  1.00 17.02 ? 130 TRP B CE2 1 
ATOM   4181  C  CE3 . TRP B  1 131 ? -6.687  28.551  25.675  1.00 17.63 ? 130 TRP B CE3 1 
ATOM   4182  C  CZ2 . TRP B  1 131 ? -8.246  28.185  23.323  1.00 17.83 ? 130 TRP B CZ2 1 
ATOM   4183  C  CZ3 . TRP B  1 131 ? -7.896  29.222  25.493  1.00 18.12 ? 130 TRP B CZ3 1 
ATOM   4184  C  CH2 . TRP B  1 131 ? -8.656  29.049  24.319  1.00 18.33 ? 130 TRP B CH2 1 
ATOM   4185  N  N   . ARG B  1 132 ? -6.069  26.349  28.288  1.00 16.94 ? 131 ARG B N   1 
ATOM   4186  C  CA  . ARG B  1 132 ? -6.588  26.996  29.494  1.00 17.94 ? 131 ARG B CA  1 
ATOM   4187  C  C   . ARG B  1 132 ? -5.908  26.471  30.753  1.00 18.14 ? 131 ARG B C   1 
ATOM   4188  O  O   . ARG B  1 132 ? -5.874  27.145  31.782  1.00 17.85 ? 131 ARG B O   1 
ATOM   4189  C  CB  . ARG B  1 132 ? -8.101  26.783  29.607  1.00 19.13 ? 131 ARG B CB  1 
ATOM   4190  C  CG  . ARG B  1 132 ? -8.876  27.368  28.438  1.00 19.73 ? 131 ARG B CG  1 
ATOM   4191  C  CD  . ARG B  1 132 ? -10.327 26.921  28.439  1.00 20.41 ? 131 ARG B CD  1 
ATOM   4192  N  NE  . ARG B  1 132 ? -10.423 25.470  28.465  1.00 20.65 ? 131 ARG B NE  1 
ATOM   4193  C  CZ  . ARG B  1 132 ? -11.521 24.794  28.785  1.00 22.48 ? 131 ARG B CZ  1 
ATOM   4194  N  NH1 . ARG B  1 132 ? -12.647 25.435  29.106  1.00 22.55 ? 131 ARG B NH1 1 
ATOM   4195  N  NH2 . ARG B  1 132 ? -11.495 23.463  28.809  1.00 23.07 ? 131 ARG B NH2 1 
ATOM   4196  N  N   . ARG B  1 133 ? -5.358  25.263  30.657  1.00 17.65 ? 132 ARG B N   1 
ATOM   4197  C  CA  . ARG B  1 133 ? -4.726  24.603  31.756  1.00 19.09 ? 132 ARG B CA  1 
ATOM   4198  C  C   . ARG B  1 133 ? -3.214  24.682  31.646  1.00 18.32 ? 132 ARG B C   1 
ATOM   4199  O  O   . ARG B  1 133 ? -2.652  24.917  30.565  1.00 18.66 ? 132 ARG B O   1 
ATOM   4200  C  CB  . ARG B  1 133 ? -5.169  23.140  31.819  1.00 20.31 ? 132 ARG B CB  1 
ATOM   4201  C  CG  . ARG B  1 133 ? -6.583  23.028  32.363  1.00 22.42 ? 132 ARG B CG  1 
ATOM   4202  C  CD  . ARG B  1 133 ? -7.217  21.676  32.128  1.00 26.08 ? 132 ARG B CD  1 
ATOM   4203  N  NE  . ARG B  1 133 ? -8.255  21.437  33.135  1.00 27.74 ? 132 ARG B NE  1 
ATOM   4204  C  CZ  . ARG B  1 133 ? -9.108  20.426  33.107  1.00 30.23 ? 132 ARG B CZ  1 
ATOM   4205  N  NH1 . ARG B  1 133 ? -9.068  19.532  32.128  1.00 31.75 ? 132 ARG B NH1 1 
ATOM   4206  N  NH2 . ARG B  1 133 ? -9.996  20.306  34.070  1.00 31.68 ? 132 ARG B NH2 1 
ATOM   4207  N  N   . ALA B  1 134 ? -2.566  24.516  32.788  1.00 17.93 ? 133 ALA B N   1 
ATOM   4208  C  CA  . ALA B  1 134 ? -1.116  24.433  32.848  1.00 18.43 ? 133 ALA B CA  1 
ATOM   4209  C  C   . ALA B  1 134 ? -0.729  22.961  32.798  1.00 18.34 ? 133 ALA B C   1 
ATOM   4210  O  O   . ALA B  1 134 ? -1.589  22.082  32.862  1.00 18.67 ? 133 ALA B O   1 
ATOM   4211  C  CB  . ALA B  1 134 ? -0.600  25.084  34.124  1.00 19.32 ? 133 ALA B CB  1 
ATOM   4212  N  N   . PRO B  1 135 ? 0.565   22.674  32.681  1.00 17.80 ? 134 PRO B N   1 
ATOM   4213  C  CA  . PRO B  1 135 ? 0.946   21.260  32.474  1.00 18.74 ? 134 PRO B CA  1 
ATOM   4214  C  C   . PRO B  1 135 ? 0.501   20.251  33.545  1.00 19.52 ? 134 PRO B C   1 
ATOM   4215  O  O   . PRO B  1 135 ? 0.352   19.046  33.224  1.00 20.06 ? 134 PRO B O   1 
ATOM   4216  C  CB  . PRO B  1 135 ? 2.463   21.332  32.371  1.00 17.97 ? 134 PRO B CB  1 
ATOM   4217  C  CG  . PRO B  1 135 ? 2.685   22.670  31.762  1.00 17.94 ? 134 PRO B CG  1 
ATOM   4218  C  CD  . PRO B  1 135 ? 1.694   23.577  32.422  1.00 17.81 ? 134 PRO B CD  1 
ATOM   4219  N  N   . ASN B  1 136 ? 0.305   20.714  34.784  1.00 20.32 ? 135 ASN B N   1 
ATOM   4220  C  CA  . ASN B  1 136 ? -0.107  19.832  35.873  1.00 22.04 ? 135 ASN B CA  1 
ATOM   4221  C  C   . ASN B  1 136 ? -1.444  19.159  35.612  1.00 22.51 ? 135 ASN B C   1 
ATOM   4222  O  O   . ASN B  1 136 ? -1.727  18.118  36.210  1.00 23.66 ? 135 ASN B O   1 
ATOM   4223  C  CB  . ASN B  1 136 ? -0.158  20.567  37.237  1.00 22.79 ? 135 ASN B CB  1 
ATOM   4224  C  CG  . ASN B  1 136 ? -1.132  21.730  37.252  1.00 23.68 ? 135 ASN B CG  1 
ATOM   4225  O  OD1 . ASN B  1 136 ? -1.240  22.485  36.291  1.00 25.00 ? 135 ASN B OD1 1 
ATOM   4226  N  ND2 . ASN B  1 136 ? -1.831  21.913  38.375  1.00 25.45 ? 135 ASN B ND2 1 
ATOM   4227  N  N   . GLU B  1 137 ? -2.270  19.749  34.752  1.00 21.68 ? 136 GLU B N   1 
ATOM   4228  C  CA  . GLU B  1 137 ? -3.561  19.173  34.416  1.00 22.89 ? 136 GLU B CA  1 
ATOM   4229  C  C   . GLU B  1 137 ? -3.662  18.724  32.944  1.00 24.05 ? 136 GLU B C   1 
ATOM   4230  O  O   . GLU B  1 137 ? -4.751  18.627  32.401  1.00 26.07 ? 136 GLU B O   1 
ATOM   4231  C  CB  . GLU B  1 137 ? -4.662  20.179  34.760  1.00 23.63 ? 136 GLU B CB  1 
ATOM   4232  C  CG  . GLU B  1 137 ? -4.736  20.421  36.260  1.00 25.62 ? 136 GLU B CG  1 
ATOM   4233  C  CD  . GLU B  1 137 ? -5.931  21.254  36.686  1.00 28.74 ? 136 GLU B CD  1 
ATOM   4234  O  OE1 . GLU B  1 137 ? -6.021  22.466  36.351  1.00 27.49 ? 136 GLU B OE1 1 
ATOM   4235  O  OE2 . GLU B  1 137 ? -6.776  20.685  37.406  1.00 34.25 ? 136 GLU B OE2 1 
ATOM   4236  N  N   . ASN B  1 138 ? -2.525  18.429  32.320  1.00 22.19 ? 137 ASN B N   1 
ATOM   4237  C  CA  . ASN B  1 138 ? -2.498  17.959  30.951  1.00 21.07 ? 137 ASN B CA  1 
ATOM   4238  C  C   . ASN B  1 138 ? -1.627  16.708  30.813  1.00 21.99 ? 137 ASN B C   1 
ATOM   4239  O  O   . ASN B  1 138 ? -0.977  16.498  29.797  1.00 20.66 ? 137 ASN B O   1 
ATOM   4240  C  CB  . ASN B  1 138 ? -2.077  19.100  30.004  1.00 21.35 ? 137 ASN B CB  1 
ATOM   4241  C  CG  . ASN B  1 138 ? -3.268  19.742  29.325  1.00 22.42 ? 137 ASN B CG  1 
ATOM   4242  O  OD1 . ASN B  1 138 ? -4.193  19.030  28.942  1.00 26.92 ? 137 ASN B OD1 1 
ATOM   4243  N  ND2 . ASN B  1 138 ? -3.282  21.049  29.198  1.00 20.12 ? 137 ASN B ND2 1 
ATOM   4244  N  N   . GLY B  1 139 ? -1.658  15.856  31.845  1.00 23.03 ? 138 GLY B N   1 
ATOM   4245  C  CA  . GLY B  1 139 ? -0.913  14.590  31.831  1.00 22.81 ? 138 GLY B CA  1 
ATOM   4246  C  C   . GLY B  1 139 ? -1.156  13.739  30.596  1.00 21.97 ? 138 GLY B C   1 
ATOM   4247  O  O   . GLY B  1 139 ? -0.200  13.291  29.953  1.00 21.74 ? 138 GLY B O   1 
ATOM   4248  N  N   . PRO B  1 140 ? -2.439  13.498  30.243  1.00 21.97 ? 139 PRO B N   1 
ATOM   4249  C  CA  . PRO B  1 140 ? -2.724  12.666  29.063  1.00 21.13 ? 139 PRO B CA  1 
ATOM   4250  C  C   . PRO B  1 140 ? -2.123  13.223  27.752  1.00 20.14 ? 139 PRO B C   1 
ATOM   4251  O  O   . PRO B  1 140 ? -1.617  12.455  26.907  1.00 18.57 ? 139 PRO B O   1 
ATOM   4252  C  CB  . PRO B  1 140 ? -4.257  12.627  29.037  1.00 22.33 ? 139 PRO B CB  1 
ATOM   4253  C  CG  . PRO B  1 140 ? -4.631  12.755  30.504  1.00 23.45 ? 139 PRO B CG  1 
ATOM   4254  C  CD  . PRO B  1 140 ? -3.652  13.754  31.051  1.00 22.42 ? 139 PRO B CD  1 
ATOM   4255  N  N   . TYR B  1 141 ? -2.123  14.542  27.608  1.00 18.25 ? 140 TYR B N   1 
ATOM   4256  C  CA  . TYR B  1 141 ? -1.450  15.179  26.471  1.00 17.98 ? 140 TYR B CA  1 
ATOM   4257  C  C   . TYR B  1 141 ? 0.010   14.799  26.350  1.00 16.93 ? 140 TYR B C   1 
ATOM   4258  O  O   . TYR B  1 141 ? 0.478   14.475  25.250  1.00 16.99 ? 140 TYR B O   1 
ATOM   4259  C  CB  . TYR B  1 141 ? -1.575  16.701  26.584  1.00 17.31 ? 140 TYR B CB  1 
ATOM   4260  C  CG  . TYR B  1 141 ? -0.705  17.482  25.634  1.00 16.75 ? 140 TYR B CG  1 
ATOM   4261  C  CD1 . TYR B  1 141 ? -1.094  17.673  24.301  1.00 17.35 ? 140 TYR B CD1 1 
ATOM   4262  C  CD2 . TYR B  1 141 ? 0.489   18.038  26.049  1.00 15.55 ? 140 TYR B CD2 1 
ATOM   4263  C  CE1 . TYR B  1 141 ? -0.310  18.412  23.427  1.00 16.46 ? 140 TYR B CE1 1 
ATOM   4264  C  CE2 . TYR B  1 141 ? 1.256   18.785  25.185  1.00 15.74 ? 140 TYR B CE2 1 
ATOM   4265  C  CZ  . TYR B  1 141 ? 0.862   18.948  23.863  1.00 15.61 ? 140 TYR B CZ  1 
ATOM   4266  O  OH  . TYR B  1 141 ? 1.638   19.722  23.002  1.00 16.14 ? 140 TYR B OH  1 
ATOM   4267  N  N   . PHE B  1 142 ? 0.745   14.838  27.460  1.00 16.90 ? 141 PHE B N   1 
ATOM   4268  C  CA  . PHE B  1 142 ? 2.170   14.540  27.420  1.00 16.19 ? 141 PHE B CA  1 
ATOM   4269  C  C   . PHE B  1 142 ? 2.429   13.066  27.100  1.00 17.12 ? 141 PHE B C   1 
ATOM   4270  O  O   . PHE B  1 142 ? 3.417   12.753  26.430  1.00 15.98 ? 141 PHE B O   1 
ATOM   4271  C  CB  . PHE B  1 142 ? 2.877   14.964  28.702  1.00 17.11 ? 141 PHE B CB  1 
ATOM   4272  C  CG  . PHE B  1 142 ? 2.866   16.447  28.915  1.00 16.88 ? 141 PHE B CG  1 
ATOM   4273  C  CD1 . PHE B  1 142 ? 3.537   17.281  28.060  1.00 17.04 ? 141 PHE B CD1 1 
ATOM   4274  C  CD2 . PHE B  1 142 ? 2.110   17.014  29.944  1.00 17.75 ? 141 PHE B CD2 1 
ATOM   4275  C  CE1 . PHE B  1 142 ? 3.502   18.655  28.232  1.00 17.40 ? 141 PHE B CE1 1 
ATOM   4276  C  CE2 . PHE B  1 142 ? 2.070   18.386  30.125  1.00 17.38 ? 141 PHE B CE2 1 
ATOM   4277  C  CZ  . PHE B  1 142 ? 2.769   19.208  29.265  1.00 17.28 ? 141 PHE B CZ  1 
ATOM   4278  N  N   . LEU B  1 143 ? 1.554   12.168  27.563  1.00 16.42 ? 142 LEU B N   1 
ATOM   4279  C  CA  . LEU B  1 143 ? 1.688   10.758  27.159  1.00 19.21 ? 142 LEU B CA  1 
ATOM   4280  C  C   . LEU B  1 143 ? 1.481   10.598  25.658  1.00 18.08 ? 142 LEU B C   1 
ATOM   4281  O  O   . LEU B  1 143 ? 2.247   9.915   25.014  1.00 17.32 ? 142 LEU B O   1 
ATOM   4282  C  CB  . LEU B  1 143 ? 0.728   9.864   27.936  1.00 22.20 ? 142 LEU B CB  1 
ATOM   4283  C  CG  . LEU B  1 143 ? 0.748   8.373   27.556  1.00 25.83 ? 142 LEU B CG  1 
ATOM   4284  C  CD1 . LEU B  1 143 ? 2.147   7.773   27.730  1.00 27.64 ? 142 LEU B CD1 1 
ATOM   4285  C  CD2 . LEU B  1 143 ? -0.286  7.501   28.288  1.00 28.06 ? 142 LEU B CD2 1 
ATOM   4286  N  N   . ALA B  1 144 ? 0.443   11.241  25.115  1.00 17.49 ? 143 ALA B N   1 
ATOM   4287  C  CA  . ALA B  1 144 ? 0.163   11.190  23.685  1.00 17.67 ? 143 ALA B CA  1 
ATOM   4288  C  C   . ALA B  1 144 ? 1.298   11.825  22.874  1.00 17.53 ? 143 ALA B C   1 
ATOM   4289  O  O   . ALA B  1 144 ? 1.637   11.320  21.811  1.00 17.39 ? 143 ALA B O   1 
ATOM   4290  C  CB  . ALA B  1 144 ? -1.136  11.891  23.363  1.00 18.58 ? 143 ALA B CB  1 
ATOM   4291  N  N   . LEU B  1 145 ? 1.859   12.922  23.367  1.00 16.19 ? 144 LEU B N   1 
ATOM   4292  C  CA  . LEU B  1 145 ? 2.979   13.555  22.693  1.00 16.19 ? 144 LEU B CA  1 
ATOM   4293  C  C   . LEU B  1 145 ? 4.206   12.635  22.621  1.00 16.85 ? 144 LEU B C   1 
ATOM   4294  O  O   . LEU B  1 145 ? 4.817   12.463  21.547  1.00 15.59 ? 144 LEU B O   1 
ATOM   4295  C  CB  . LEU B  1 145 ? 3.334   14.856  23.397  1.00 16.37 ? 144 LEU B CB  1 
ATOM   4296  C  CG  . LEU B  1 145 ? 4.532   15.664  22.892  1.00 16.72 ? 144 LEU B CG  1 
ATOM   4297  C  CD1 . LEU B  1 145 ? 4.335   16.047  21.446  1.00 16.92 ? 144 LEU B CD1 1 
ATOM   4298  C  CD2 . LEU B  1 145 ? 4.745   16.910  23.728  1.00 17.78 ? 144 LEU B CD2 1 
ATOM   4299  N  N   . ARG B  1 146 ? 4.530   12.000  23.751  1.00 17.10 ? 145 ARG B N   1 
ATOM   4300  C  CA  . ARG B  1 146 ? 5.626   11.036  23.778  1.00 19.19 ? 145 ARG B CA  1 
ATOM   4301  C  C   . ARG B  1 146 ? 5.388   9.904   22.776  1.00 18.40 ? 145 ARG B C   1 
ATOM   4302  O  O   . ARG B  1 146 ? 6.272   9.537   22.025  1.00 17.99 ? 145 ARG B O   1 
ATOM   4303  C  CB  . ARG B  1 146 ? 5.828   10.489  25.194  1.00 21.74 ? 145 ARG B CB  1 
ATOM   4304  C  CG  . ARG B  1 146 ? 6.932   9.464   25.317  1.00 26.63 ? 145 ARG B CG  1 
ATOM   4305  C  CD  . ARG B  1 146 ? 7.082   8.992   26.761  1.00 30.29 ? 145 ARG B CD  1 
ATOM   4306  N  NE  . ARG B  1 146 ? 7.836   7.739   26.818  1.00 37.37 ? 145 ARG B NE  1 
ATOM   4307  C  CZ  . ARG B  1 146 ? 9.018   7.552   27.432  1.00 42.10 ? 145 ARG B CZ  1 
ATOM   4308  N  NH1 . ARG B  1 146 ? 9.664   8.544   28.076  1.00 41.44 ? 145 ARG B NH1 1 
ATOM   4309  N  NH2 . ARG B  1 146 ? 9.572   6.333   27.404  1.00 43.63 ? 145 ARG B NH2 1 
ATOM   4310  N  N   . GLU B  1 147 ? 4.199   9.331   22.790  1.00 17.83 ? 146 GLU B N   1 
ATOM   4311  C  CA  . GLU B  1 147 ? 3.865   8.269   21.863  1.00 19.77 ? 146 GLU B CA  1 
ATOM   4312  C  C   . GLU B  1 147 ? 3.936   8.696   20.390  1.00 18.12 ? 146 GLU B C   1 
ATOM   4313  O  O   . GLU B  1 147 ? 4.376   7.917   19.554  1.00 17.92 ? 146 GLU B O   1 
ATOM   4314  C  CB  . GLU B  1 147 ? 2.494   7.661   22.214  1.00 21.83 ? 146 GLU B CB  1 
ATOM   4315  C  CG  . GLU B  1 147 ? 2.545   6.939   23.570  1.00 25.47 ? 146 GLU B CG  1 
ATOM   4316  C  CD  . GLU B  1 147 ? 1.193   6.452   24.095  1.00 31.24 ? 146 GLU B CD  1 
ATOM   4317  O  OE1 . GLU B  1 147 ? 0.134   7.001   23.711  1.00 34.77 ? 146 GLU B OE1 1 
ATOM   4318  O  OE2 . GLU B  1 147 ? 1.215   5.514   24.925  1.00 38.14 ? 146 GLU B OE2 1 
ATOM   4319  N  N   . MET B  1 148 ? 3.443   9.893   20.085  1.00 17.30 ? 147 MET B N   1 
ATOM   4320  C  CA  . MET B  1 148 ? 3.425   10.371  18.712  1.00 17.47 ? 147 MET B CA  1 
ATOM   4321  C  C   . MET B  1 148 ? 4.848   10.578  18.215  1.00 16.37 ? 147 MET B C   1 
ATOM   4322  O  O   . MET B  1 148 ? 5.183   10.208  17.088  1.00 16.22 ? 147 MET B O   1 
ATOM   4323  C  CB  . MET B  1 148 ? 2.660   11.677  18.621  1.00 17.83 ? 147 MET B CB  1 
ATOM   4324  C  CG  . MET B  1 148 ? 2.596   12.205  17.209  1.00 19.82 ? 147 MET B CG  1 
ATOM   4325  S  SD  . MET B  1 148 ? 1.388   13.535  17.024  1.00 20.99 ? 147 MET B SD  1 
ATOM   4326  C  CE  . MET B  1 148 ? 2.172   14.873  17.886  1.00 20.73 ? 147 MET B CE  1 
ATOM   4327  N  N   . ILE B  1 149 ? 5.695   11.132  19.077  1.00 15.74 ? 148 ILE B N   1 
ATOM   4328  C  CA  . ILE B  1 149 ? 7.108   11.307  18.743  1.00 16.06 ? 148 ILE B CA  1 
ATOM   4329  C  C   . ILE B  1 149 ? 7.776   9.958   18.453  1.00 16.97 ? 148 ILE B C   1 
ATOM   4330  O  O   . ILE B  1 149 ? 8.495   9.824   17.465  1.00 16.88 ? 148 ILE B O   1 
ATOM   4331  C  CB  . ILE B  1 149 ? 7.852   12.074  19.840  1.00 15.48 ? 148 ILE B CB  1 
ATOM   4332  C  CG1 . ILE B  1 149 ? 7.426   13.536  19.806  1.00 15.22 ? 148 ILE B CG1 1 
ATOM   4333  C  CG2 . ILE B  1 149 ? 9.357   11.957  19.683  1.00 16.06 ? 148 ILE B CG2 1 
ATOM   4334  C  CD1 . ILE B  1 149 ? 7.823   14.308  21.038  1.00 14.66 ? 148 ILE B CD1 1 
ATOM   4335  N  N   . GLU B  1 150 ? 7.538   8.965   19.308  1.00 17.48 ? 149 GLU B N   1 
ATOM   4336  C  CA  . GLU B  1 150 ? 8.110   7.644   19.089  1.00 18.36 ? 149 GLU B CA  1 
ATOM   4337  C  C   . GLU B  1 150 ? 7.644   7.035   17.765  1.00 19.31 ? 149 GLU B C   1 
ATOM   4338  O  O   . GLU B  1 150 ? 8.434   6.420   17.020  1.00 19.58 ? 149 GLU B O   1 
ATOM   4339  C  CB  . GLU B  1 150 ? 7.804   6.740   20.286  1.00 19.61 ? 149 GLU B CB  1 
ATOM   4340  C  CG  . GLU B  1 150 ? 8.480   7.216   21.575  1.00 21.00 ? 149 GLU B CG  1 
ATOM   4341  C  CD  . GLU B  1 150 ? 8.267   6.290   22.771  1.00 24.68 ? 149 GLU B CD  1 
ATOM   4342  O  OE1 . GLU B  1 150 ? 7.626   5.229   22.582  1.00 29.52 ? 149 GLU B OE1 1 
ATOM   4343  O  OE2 . GLU B  1 150 ? 8.802   6.562   23.872  1.00 23.58 ? 149 GLU B OE2 1 
ATOM   4344  N  N   . GLU B  1 151 ? 6.353   7.168   17.463  1.00 19.09 ? 150 GLU B N   1 
ATOM   4345  C  CA  A GLU B  1 151 ? 5.806   6.647   16.219  0.50 19.22 ? 150 GLU B CA  1 
ATOM   4346  C  CA  B GLU B  1 151 ? 5.814   6.649   16.213  0.50 19.53 ? 150 GLU B CA  1 
ATOM   4347  C  C   . GLU B  1 151 ? 6.438   7.320   14.996  1.00 18.90 ? 150 GLU B C   1 
ATOM   4348  O  O   . GLU B  1 151 ? 6.780   6.643   14.007  1.00 17.72 ? 150 GLU B O   1 
ATOM   4349  C  CB  A GLU B  1 151 ? 4.278   6.840   16.211  0.50 20.46 ? 150 GLU B CB  1 
ATOM   4350  C  CB  B GLU B  1 151 ? 4.290   6.803   16.185  0.50 21.32 ? 150 GLU B CB  1 
ATOM   4351  C  CG  A GLU B  1 151 ? 3.612   6.533   14.866  0.50 21.96 ? 150 GLU B CG  1 
ATOM   4352  C  CG  B GLU B  1 151 ? 3.620   5.888   17.184  0.50 23.64 ? 150 GLU B CG  1 
ATOM   4353  C  CD  A GLU B  1 151 ? 2.097   6.700   14.865  0.50 23.55 ? 150 GLU B CD  1 
ATOM   4354  C  CD  B GLU B  1 151 ? 2.119   6.011   17.160  0.50 25.46 ? 150 GLU B CD  1 
ATOM   4355  O  OE1 A GLU B  1 151 ? 1.447   6.164   15.771  0.50 25.22 ? 150 GLU B OE1 1 
ATOM   4356  O  OE1 B GLU B  1 151 ? 1.623   7.128   16.867  0.50 28.94 ? 150 GLU B OE1 1 
ATOM   4357  O  OE2 A GLU B  1 151 ? 1.545   7.315   13.926  0.50 24.51 ? 150 GLU B OE2 1 
ATOM   4358  O  OE2 B GLU B  1 151 ? 1.458   4.985   17.418  0.50 27.70 ? 150 GLU B OE2 1 
ATOM   4359  N  N   . MET B  1 152 ? 6.591   8.640   15.057  1.00 16.49 ? 151 MET B N   1 
ATOM   4360  C  CA  . MET B  1 152 ? 7.144   9.364   13.942  1.00 17.48 ? 151 MET B CA  1 
ATOM   4361  C  C   . MET B  1 152 ? 8.612   8.965   13.714  1.00 17.49 ? 151 MET B C   1 
ATOM   4362  O  O   . MET B  1 152 ? 9.059   8.836   12.583  1.00 18.14 ? 151 MET B O   1 
ATOM   4363  C  CB  . MET B  1 152 ? 7.016   10.859  14.163  1.00 17.33 ? 151 MET B CB  1 
ATOM   4364  C  CG  . MET B  1 152 ? 5.565   11.346  14.132  1.00 18.23 ? 151 MET B CG  1 
ATOM   4365  S  SD  . MET B  1 152 ? 5.380   13.082  14.567  1.00 19.28 ? 151 MET B SD  1 
ATOM   4366  C  CE  . MET B  1 152 ? 5.840   13.855  13.041  1.00 19.22 ? 151 MET B CE  1 
ATOM   4367  N  N   . TYR B  1 153 ? 9.335   8.757   14.811  1.00 17.49 ? 152 TYR B N   1 
ATOM   4368  C  CA  . TYR B  1 153 ? 10.737  8.317   14.754  1.00 18.21 ? 152 TYR B CA  1 
ATOM   4369  C  C   . TYR B  1 153 ? 10.830  6.969   14.008  1.00 18.88 ? 152 TYR B C   1 
ATOM   4370  O  O   . TYR B  1 153 ? 11.671  6.763   13.120  1.00 19.06 ? 152 TYR B O   1 
ATOM   4371  C  CB  . TYR B  1 153 ? 11.277  8.200   16.170  1.00 18.32 ? 152 TYR B CB  1 
ATOM   4372  C  CG  . TYR B  1 153 ? 12.566  7.460   16.322  1.00 19.59 ? 152 TYR B CG  1 
ATOM   4373  C  CD1 . TYR B  1 153 ? 13.778  8.104   16.195  1.00 20.59 ? 152 TYR B CD1 1 
ATOM   4374  C  CD2 . TYR B  1 153 ? 12.566  6.088   16.562  1.00 20.56 ? 152 TYR B CD2 1 
ATOM   4375  C  CE1 . TYR B  1 153 ? 14.971  7.410   16.307  1.00 22.05 ? 152 TYR B CE1 1 
ATOM   4376  C  CE2 . TYR B  1 153 ? 13.741  5.393   16.680  1.00 21.99 ? 152 TYR B CE2 1 
ATOM   4377  C  CZ  . TYR B  1 153 ? 14.939  6.050   16.569  1.00 22.79 ? 152 TYR B CZ  1 
ATOM   4378  O  OH  . TYR B  1 153 ? 16.091  5.339   16.657  1.00 25.28 ? 152 TYR B OH  1 
ATOM   4379  N  N   . GLN B  1 154 ? 9.945   6.053   14.362  1.00 19.64 ? 153 GLN B N   1 
ATOM   4380  C  CA  . GLN B  1 154 ? 9.947   4.750   13.736  1.00 20.02 ? 153 GLN B CA  1 
ATOM   4381  C  C   . GLN B  1 154 ? 9.501   4.765   12.289  1.00 21.83 ? 153 GLN B C   1 
ATOM   4382  O  O   . GLN B  1 154 ? 10.079  4.044   11.458  1.00 21.69 ? 153 GLN B O   1 
ATOM   4383  C  CB  . GLN B  1 154 ? 9.083   3.788   14.539  1.00 20.59 ? 153 GLN B CB  1 
ATOM   4384  C  CG  . GLN B  1 154 ? 9.704   3.524   15.883  1.00 20.87 ? 153 GLN B CG  1 
ATOM   4385  C  CD  . GLN B  1 154 ? 9.185   2.250   16.508  1.00 22.65 ? 153 GLN B CD  1 
ATOM   4386  O  OE1 . GLN B  1 154 ? 7.983   1.984   16.462  1.00 24.86 ? 153 GLN B OE1 1 
ATOM   4387  N  NE2 . GLN B  1 154 ? 10.083  1.437   17.046  1.00 22.02 ? 153 GLN B NE2 1 
ATOM   4388  N  N   . LEU B  1 155 ? 8.458   5.535   11.985  1.00 21.96 ? 154 LEU B N   1 
ATOM   4389  C  CA  . LEU B  1 155 ? 7.922   5.591   10.630  1.00 24.62 ? 154 LEU B CA  1 
ATOM   4390  C  C   . LEU B  1 155 ? 8.845   6.299   9.659   1.00 24.84 ? 154 LEU B C   1 
ATOM   4391  O  O   . LEU B  1 155 ? 9.049   5.824   8.543   1.00 25.43 ? 154 LEU B O   1 
ATOM   4392  C  CB  . LEU B  1 155 ? 6.570   6.293   10.596  1.00 25.56 ? 154 LEU B CB  1 
ATOM   4393  C  CG  . LEU B  1 155 ? 5.371   5.533   11.124  1.00 29.17 ? 154 LEU B CG  1 
ATOM   4394  C  CD1 . LEU B  1 155 ? 4.181   6.470   11.254  1.00 30.93 ? 154 LEU B CD1 1 
ATOM   4395  C  CD2 . LEU B  1 155 ? 5.024   4.370   10.209  1.00 31.27 ? 154 LEU B CD2 1 
ATOM   4396  N  N   . TYR B  1 156 ? 9.413   7.417   10.079  1.00 25.02 ? 155 TYR B N   1 
ATOM   4397  C  CA  . TYR B  1 156 ? 10.158  8.269   9.155   1.00 26.56 ? 155 TYR B CA  1 
ATOM   4398  C  C   . TYR B  1 156 ? 11.682  8.109   9.315   1.00 28.47 ? 155 TYR B C   1 
ATOM   4399  O  O   . TYR B  1 156 ? 12.422  8.720   8.592   1.00 31.24 ? 155 TYR B O   1 
ATOM   4400  C  CB  . TYR B  1 156 ? 9.654   9.733   9.225   1.00 25.75 ? 155 TYR B CB  1 
ATOM   4401  C  CG  . TYR B  1 156 ? 8.125   9.800   9.170   1.00 24.51 ? 155 TYR B CG  1 
ATOM   4402  C  CD1 . TYR B  1 156 ? 7.413   9.344   8.047   1.00 25.55 ? 155 TYR B CD1 1 
ATOM   4403  C  CD2 . TYR B  1 156 ? 7.391   10.234  10.253  1.00 23.12 ? 155 TYR B CD2 1 
ATOM   4404  C  CE1 . TYR B  1 156 ? 6.011   9.324   8.031   1.00 24.64 ? 155 TYR B CE1 1 
ATOM   4405  C  CE2 . TYR B  1 156 ? 5.998   10.228  10.241  1.00 22.76 ? 155 TYR B CE2 1 
ATOM   4406  C  CZ  . TYR B  1 156 ? 5.315   9.757   9.127   1.00 23.98 ? 155 TYR B CZ  1 
ATOM   4407  O  OH  . TYR B  1 156 ? 3.920   9.761   9.130   1.00 24.17 ? 155 TYR B OH  1 
ATOM   4408  N  N   . GLY B  1 157 ? 12.119  7.253   10.231  1.00 29.28 ? 156 GLY B N   1 
ATOM   4409  C  CA  . GLY B  1 157 ? 13.503  6.782   10.271  1.00 29.65 ? 156 GLY B CA  1 
ATOM   4410  C  C   . GLY B  1 157 ? 14.498  7.704   10.948  1.00 28.54 ? 156 GLY B C   1 
ATOM   4411  O  O   . GLY B  1 157 ? 15.704  7.579   10.730  1.00 31.66 ? 156 GLY B O   1 
ATOM   4412  N  N   . GLY B  1 158 ? 14.020  8.640   11.762  1.00 25.16 ? 157 GLY B N   1 
ATOM   4413  C  CA  . GLY B  1 158 ? 14.926  9.443   12.545  1.00 23.71 ? 157 GLY B CA  1 
ATOM   4414  C  C   . GLY B  1 158 ? 14.246  10.346  13.550  1.00 21.97 ? 157 GLY B C   1 
ATOM   4415  O  O   . GLY B  1 158 ? 13.008  10.468  13.584  1.00 21.02 ? 157 GLY B O   1 
ATOM   4416  N  N   . PRO B  1 159 ? 15.058  11.004  14.379  1.00 20.77 ? 158 PRO B N   1 
ATOM   4417  C  CA  . PRO B  1 159 ? 14.520  11.819  15.422  1.00 20.75 ? 158 PRO B CA  1 
ATOM   4418  C  C   . PRO B  1 159 ? 13.781  13.080  14.922  1.00 20.39 ? 158 PRO B C   1 
ATOM   4419  O  O   . PRO B  1 159 ? 13.978  13.530  13.781  1.00 20.28 ? 158 PRO B O   1 
ATOM   4420  C  CB  . PRO B  1 159 ? 15.749  12.179  16.263  1.00 20.71 ? 158 PRO B CB  1 
ATOM   4421  C  CG  . PRO B  1 159 ? 16.918  11.963  15.370  1.00 22.05 ? 158 PRO B CG  1 
ATOM   4422  C  CD  . PRO B  1 159 ? 16.534  10.860  14.462  1.00 22.11 ? 158 PRO B CD  1 
ATOM   4423  N  N   . VAL B  1 160 ? 12.946  13.614  15.799  1.00 20.28 ? 159 VAL B N   1 
ATOM   4424  C  CA  . VAL B  1 160 ? 11.951  14.633  15.472  1.00 20.85 ? 159 VAL B CA  1 
ATOM   4425  C  C   . VAL B  1 160 ? 12.435  16.046  15.830  1.00 19.48 ? 159 VAL B C   1 
ATOM   4426  O  O   . VAL B  1 160 ? 13.180  16.226  16.808  1.00 19.33 ? 159 VAL B O   1 
ATOM   4427  C  CB  . VAL B  1 160 ? 10.659  14.322  16.259  1.00 22.91 ? 159 VAL B CB  1 
ATOM   4428  C  CG1 . VAL B  1 160 ? 9.615   15.408  16.118  1.00 25.74 ? 159 VAL B CG1 1 
ATOM   4429  C  CG2 . VAL B  1 160 ? 10.110  12.967  15.849  1.00 24.20 ? 159 VAL B CG2 1 
ATOM   4430  N  N   . VAL B  1 161 ? 12.015  17.030  15.044  1.00 17.14 ? 160 VAL B N   1 
ATOM   4431  C  CA  . VAL B  1 161 ? 12.251  18.424  15.379  1.00 16.89 ? 160 VAL B CA  1 
ATOM   4432  C  C   . VAL B  1 161 ? 10.962  18.981  15.963  1.00 17.09 ? 160 VAL B C   1 
ATOM   4433  O  O   . VAL B  1 161 ? 9.906   18.909  15.318  1.00 17.34 ? 160 VAL B O   1 
ATOM   4434  C  CB  . VAL B  1 161 ? 12.681  19.248  14.149  1.00 17.35 ? 160 VAL B CB  1 
ATOM   4435  C  CG1 . VAL B  1 161 ? 12.775  20.754  14.501  1.00 17.66 ? 160 VAL B CG1 1 
ATOM   4436  C  CG2 . VAL B  1 161 ? 14.021  18.750  13.633  1.00 17.81 ? 160 VAL B CG2 1 
ATOM   4437  N  N   . LEU B  1 162 ? 11.050  19.506  17.181  1.00 17.10 ? 161 LEU B N   1 
ATOM   4438  C  CA  . LEU B  1 162 ? 9.927   20.182  17.856  1.00 18.07 ? 161 LEU B CA  1 
ATOM   4439  C  C   . LEU B  1 162 ? 9.982   21.660  17.526  1.00 17.21 ? 161 LEU B C   1 
ATOM   4440  O  O   . LEU B  1 162 ? 11.038  22.275  17.642  1.00 17.70 ? 161 LEU B O   1 
ATOM   4441  C  CB  . LEU B  1 162 ? 10.035  20.028  19.370  1.00 19.12 ? 161 LEU B CB  1 
ATOM   4442  C  CG  . LEU B  1 162 ? 10.052  18.593  19.876  1.00 21.72 ? 161 LEU B CG  1 
ATOM   4443  C  CD1 . LEU B  1 162 ? 10.358  18.477  21.351  1.00 22.32 ? 161 LEU B CD1 1 
ATOM   4444  C  CD2 . LEU B  1 162 ? 8.708   17.971  19.575  1.00 24.34 ? 161 LEU B CD2 1 
ATOM   4445  N  N   . VAL B  1 163 ? 8.864   22.225  17.086  1.00 16.24 ? 162 VAL B N   1 
ATOM   4446  C  CA  . VAL B  1 163 ? 8.797   23.654  16.789  1.00 16.39 ? 162 VAL B CA  1 
ATOM   4447  C  C   . VAL B  1 163 ? 7.673   24.205  17.637  1.00 16.28 ? 162 VAL B C   1 
ATOM   4448  O  O   . VAL B  1 163 ? 6.517   23.798  17.445  1.00 16.97 ? 162 VAL B O   1 
ATOM   4449  C  CB  . VAL B  1 163 ? 8.518   23.923  15.293  1.00 16.99 ? 162 VAL B CB  1 
ATOM   4450  C  CG1 . VAL B  1 163 ? 8.476   25.444  15.025  1.00 17.67 ? 162 VAL B CG1 1 
ATOM   4451  C  CG2 . VAL B  1 163 ? 9.572   23.273  14.408  1.00 17.66 ? 162 VAL B CG2 1 
ATOM   4452  N  N   . ALA B  1 164 ? 7.975   25.129  18.569  1.00 15.63 ? 163 ALA B N   1 
ATOM   4453  C  CA  . ALA B  1 164 ? 6.970   25.639  19.482  1.00 15.64 ? 163 ALA B CA  1 
ATOM   4454  C  C   . ALA B  1 164 ? 6.900   27.165  19.473  1.00 15.71 ? 163 ALA B C   1 
ATOM   4455  O  O   . ALA B  1 164 ? 7.902   27.831  19.257  1.00 15.34 ? 163 ALA B O   1 
ATOM   4456  C  CB  . ALA B  1 164 ? 7.228   25.151  20.892  1.00 16.08 ? 163 ALA B CB  1 
ATOM   4457  N  N   . HIS B  1 165 ? 5.696   27.691  19.677  1.00 15.55 ? 164 HIS B N   1 
ATOM   4458  C  CA  . HIS B  1 165 ? 5.487   29.131  19.705  1.00 16.48 ? 164 HIS B CA  1 
ATOM   4459  C  C   . HIS B  1 165 ? 4.943   29.538  21.073  1.00 16.33 ? 164 HIS B C   1 
ATOM   4460  O  O   . HIS B  1 165 ? 4.055   28.896  21.627  1.00 15.41 ? 164 HIS B O   1 
ATOM   4461  C  CB  . HIS B  1 165 ? 4.519   29.576  18.632  1.00 16.98 ? 164 HIS B CB  1 
ATOM   4462  C  CG  . HIS B  1 165 ? 4.263   31.045  18.622  1.00 17.52 ? 164 HIS B CG  1 
ATOM   4463  N  ND1 . HIS B  1 165 ? 3.020   31.579  18.847  1.00 18.42 ? 164 HIS B ND1 1 
ATOM   4464  C  CD2 . HIS B  1 165 ? 5.092   32.097  18.406  1.00 18.27 ? 164 HIS B CD2 1 
ATOM   4465  C  CE1 . HIS B  1 165 ? 3.090   32.901  18.790  1.00 19.28 ? 164 HIS B CE1 1 
ATOM   4466  N  NE2 . HIS B  1 165 ? 4.337   33.239  18.505  1.00 19.14 ? 164 HIS B NE2 1 
ATOM   4467  N  N   . SER B  1 166 ? 5.501   30.634  21.586  1.00 17.08 ? 165 SER B N   1 
ATOM   4468  C  CA  . SER B  1 166 ? 5.001   31.295  22.767  1.00 18.02 ? 165 SER B CA  1 
ATOM   4469  C  C   . SER B  1 166 ? 4.885   30.333  23.952  1.00 17.12 ? 165 SER B C   1 
ATOM   4470  O  O   . SER B  1 166 ? 5.861   29.614  24.233  1.00 15.99 ? 165 SER B O   1 
ATOM   4471  C  CB  . SER B  1 166 ? 3.696   32.010  22.414  1.00 20.43 ? 165 SER B CB  1 
ATOM   4472  O  OG  . SER B  1 166 ? 3.407   33.002  23.378  1.00 22.35 ? 165 SER B OG  1 
ATOM   4473  N  N   . MET B  1 167 ? 3.717   30.254  24.609  1.00 16.67 ? 166 MET B N   1 
ATOM   4474  C  CA  . MET B  1 167 ? 3.552   29.356  25.754  1.00 18.31 ? 166 MET B CA  1 
ATOM   4475  C  C   . MET B  1 167 ? 3.819   27.877  25.412  1.00 16.67 ? 166 MET B C   1 
ATOM   4476  O  O   . MET B  1 167 ? 4.177   27.084  26.283  1.00 15.06 ? 166 MET B O   1 
ATOM   4477  C  CB  . MET B  1 167 ? 2.130   29.461  26.306  1.00 19.70 ? 166 MET B CB  1 
ATOM   4478  C  CG  . MET B  1 167 ? 1.897   28.600  27.524  1.00 21.78 ? 166 MET B CG  1 
ATOM   4479  S  SD  . MET B  1 167 ? 0.261   28.969  28.223  1.00 22.22 ? 166 MET B SD  1 
ATOM   4480  C  CE  . MET B  1 167 ? -0.787  27.875  27.297  1.00 20.97 ? 166 MET B CE  1 
ATOM   4481  N  N   . GLY B  1 168 ? 3.674   27.513  24.142  1.00 16.17 ? 167 GLY B N   1 
ATOM   4482  C  CA  . GLY B  1 168 ? 4.036   26.148  23.722  1.00 15.53 ? 167 GLY B CA  1 
ATOM   4483  C  C   . GLY B  1 168 ? 5.460   25.784  24.074  1.00 15.59 ? 167 GLY B C   1 
ATOM   4484  O  O   . GLY B  1 168 ? 5.798   24.603  24.274  1.00 15.73 ? 167 GLY B O   1 
ATOM   4485  N  N   . ASN B  1 169 ? 6.346   26.772  24.127  1.00 15.47 ? 168 ASN B N   1 
ATOM   4486  C  CA  . ASN B  1 169 ? 7.727   26.497  24.565  1.00 15.65 ? 168 ASN B CA  1 
ATOM   4487  C  C   . ASN B  1 169 ? 7.840   26.031  26.018  1.00 15.92 ? 168 ASN B C   1 
ATOM   4488  O  O   . ASN B  1 169 ? 8.684   25.214  26.353  1.00 15.93 ? 168 ASN B O   1 
ATOM   4489  C  CB  . ASN B  1 169 ? 8.580   27.735  24.376  1.00 16.68 ? 168 ASN B CB  1 
ATOM   4490  C  CG  . ASN B  1 169 ? 8.815   28.034  22.921  1.00 17.11 ? 168 ASN B CG  1 
ATOM   4491  O  OD1 . ASN B  1 169 ? 9.577   27.345  22.277  1.00 19.49 ? 168 ASN B OD1 1 
ATOM   4492  N  ND2 . ASN B  1 169 ? 8.128   29.024  22.389  1.00 17.67 ? 168 ASN B ND2 1 
ATOM   4493  N  N   . MET B  1 170 ? 7.005   26.584  26.883  1.00 17.35 ? 169 MET B N   1 
ATOM   4494  C  CA  . MET B  1 170 ? 7.003   26.214  28.291  1.00 18.23 ? 169 MET B CA  1 
ATOM   4495  C  C   . MET B  1 170 ? 6.371   24.818  28.480  1.00 16.88 ? 169 MET B C   1 
ATOM   4496  O  O   . MET B  1 170 ? 6.868   24.035  29.281  1.00 16.62 ? 169 MET B O   1 
ATOM   4497  C  CB  . MET B  1 170 ? 6.301   27.312  29.105  1.00 20.62 ? 169 MET B CB  1 
ATOM   4498  C  CG  . MET B  1 170 ? 7.157   28.591  29.211  1.00 24.13 ? 169 MET B CG  1 
ATOM   4499  S  SD  . MET B  1 170 ? 8.462   28.366  30.426  1.00 30.22 ? 169 MET B SD  1 
ATOM   4500  C  CE  . MET B  1 170 ? 7.563   28.583  31.972  1.00 29.99 ? 169 MET B CE  1 
ATOM   4501  N  N   . TYR B  1 171 ? 5.317   24.505  27.722  1.00 16.38 ? 170 TYR B N   1 
ATOM   4502  C  CA  . TYR B  1 171 ? 4.802   23.114  27.630  1.00 16.41 ? 170 TYR B CA  1 
ATOM   4503  C  C   . TYR B  1 171 ? 5.892   22.129  27.179  1.00 16.44 ? 170 TYR B C   1 
ATOM   4504  O  O   . TYR B  1 171 ? 6.071   21.081  27.780  1.00 16.45 ? 170 TYR B O   1 
ATOM   4505  C  CB  . TYR B  1 171 ? 3.590   23.027  26.684  1.00 17.26 ? 170 TYR B CB  1 
ATOM   4506  C  CG  . TYR B  1 171 ? 2.298   23.053  27.438  1.00 17.09 ? 170 TYR B CG  1 
ATOM   4507  C  CD1 . TYR B  1 171 ? 1.859   24.209  28.076  1.00 16.61 ? 170 TYR B CD1 1 
ATOM   4508  C  CD2 . TYR B  1 171 ? 1.543   21.918  27.564  1.00 18.17 ? 170 TYR B CD2 1 
ATOM   4509  C  CE1 . TYR B  1 171 ? 0.674   24.221  28.797  1.00 16.59 ? 170 TYR B CE1 1 
ATOM   4510  C  CE2 . TYR B  1 171 ? 0.378   21.920  28.284  1.00 18.00 ? 170 TYR B CE2 1 
ATOM   4511  C  CZ  . TYR B  1 171 ? -0.047  23.074  28.902  1.00 17.95 ? 170 TYR B CZ  1 
ATOM   4512  O  OH  . TYR B  1 171 ? -1.214  22.999  29.635  1.00 17.40 ? 170 TYR B OH  1 
ATOM   4513  N  N   . THR B  1 172 ? 6.641   22.497  26.143  1.00 16.45 ? 171 THR B N   1 
ATOM   4514  C  CA  . THR B  1 172 ? 7.710   21.654  25.607  1.00 16.30 ? 171 THR B CA  1 
ATOM   4515  C  C   . THR B  1 172 ? 8.865   21.486  26.595  1.00 17.27 ? 171 THR B C   1 
ATOM   4516  O  O   . THR B  1 172 ? 9.374   20.363  26.777  1.00 16.23 ? 171 THR B O   1 
ATOM   4517  C  CB  . THR B  1 172 ? 8.191   22.179  24.242  1.00 16.83 ? 171 THR B CB  1 
ATOM   4518  O  OG1 . THR B  1 172 ? 7.083   22.273  23.336  1.00 17.21 ? 171 THR B OG1 1 
ATOM   4519  C  CG2 . THR B  1 172 ? 9.252   21.269  23.642  1.00 18.03 ? 171 THR B CG2 1 
ATOM   4520  N  N   . LEU B  1 173 ? 9.267   22.582  27.267  1.00 16.88 ? 172 LEU B N   1 
ATOM   4521  C  CA  . LEU B  1 173 ? 10.306  22.484  28.276  1.00 18.22 ? 172 LEU B CA  1 
ATOM   4522  C  C   . LEU B  1 173 ? 9.889   21.575  29.448  1.00 18.53 ? 172 LEU B C   1 
ATOM   4523  O  O   . LEU B  1 173 ? 10.678  20.720  29.908  1.00 18.39 ? 172 LEU B O   1 
ATOM   4524  C  CB  . LEU B  1 173 ? 10.703  23.868  28.794  1.00 18.21 ? 172 LEU B CB  1 
ATOM   4525  C  CG  . LEU B  1 173 ? 11.782  23.890  29.880  1.00 19.55 ? 172 LEU B CG  1 
ATOM   4526  C  CD1 . LEU B  1 173 ? 13.098  23.290  29.388  1.00 20.52 ? 172 LEU B CD1 1 
ATOM   4527  C  CD2 . LEU B  1 173 ? 11.975  25.331  30.349  1.00 19.89 ? 172 LEU B CD2 1 
ATOM   4528  N  N   . TYR B  1 174 ? 8.652   21.736  29.907  1.00 17.95 ? 173 TYR B N   1 
ATOM   4529  C  CA  . TYR B  1 174 ? 8.123   20.852  30.942  1.00 17.96 ? 173 TYR B CA  1 
ATOM   4530  C  C   . TYR B  1 174 ? 8.255   19.400  30.492  1.00 17.62 ? 173 TYR B C   1 
ATOM   4531  O  O   . TYR B  1 174 ? 8.753   18.546  31.252  1.00 18.40 ? 173 TYR B O   1 
ATOM   4532  C  CB  . TYR B  1 174 ? 6.661   21.192  31.231  1.00 18.48 ? 173 TYR B CB  1 
ATOM   4533  C  CG  . TYR B  1 174 ? 5.956   20.235  32.192  1.00 19.38 ? 173 TYR B CG  1 
ATOM   4534  C  CD1 . TYR B  1 174 ? 5.293   19.109  31.728  1.00 21.05 ? 173 TYR B CD1 1 
ATOM   4535  C  CD2 . TYR B  1 174 ? 5.923   20.491  33.562  1.00 21.16 ? 173 TYR B CD2 1 
ATOM   4536  C  CE1 . TYR B  1 174 ? 4.623   18.259  32.592  1.00 21.16 ? 173 TYR B CE1 1 
ATOM   4537  C  CE2 . TYR B  1 174 ? 5.259   19.645  34.436  1.00 22.36 ? 173 TYR B CE2 1 
ATOM   4538  C  CZ  . TYR B  1 174 ? 4.603   18.541  33.941  1.00 22.96 ? 173 TYR B CZ  1 
ATOM   4539  O  OH  . TYR B  1 174 ? 3.940   17.700  34.809  1.00 24.34 ? 173 TYR B OH  1 
ATOM   4540  N  N   . PHE B  1 175 ? 7.780   19.114  29.288  1.00 17.13 ? 174 PHE B N   1 
ATOM   4541  C  CA  . PHE B  1 175 ? 7.838   17.742  28.741  1.00 16.92 ? 174 PHE B CA  1 
ATOM   4542  C  C   . PHE B  1 175 ? 9.282   17.217  28.738  1.00 17.97 ? 174 PHE B C   1 
ATOM   4543  O  O   . PHE B  1 175 ? 9.561   16.122  29.261  1.00 17.53 ? 174 PHE B O   1 
ATOM   4544  C  CB  . PHE B  1 175 ? 7.257   17.734  27.338  1.00 17.70 ? 174 PHE B CB  1 
ATOM   4545  C  CG  . PHE B  1 175 ? 7.390   16.426  26.613  1.00 17.63 ? 174 PHE B CG  1 
ATOM   4546  C  CD1 . PHE B  1 175 ? 6.638   15.323  27.001  1.00 18.22 ? 174 PHE B CD1 1 
ATOM   4547  C  CD2 . PHE B  1 175 ? 8.273   16.299  25.554  1.00 17.62 ? 174 PHE B CD2 1 
ATOM   4548  C  CE1 . PHE B  1 175 ? 6.780   14.112  26.337  1.00 19.04 ? 174 PHE B CE1 1 
ATOM   4549  C  CE2 . PHE B  1 175 ? 8.421   15.089  24.883  1.00 18.26 ? 174 PHE B CE2 1 
ATOM   4550  C  CZ  . PHE B  1 175 ? 7.664   14.010  25.271  1.00 19.06 ? 174 PHE B CZ  1 
ATOM   4551  N  N   . LEU B  1 176 ? 10.200  17.993  28.173  1.00 17.54 ? 175 LEU B N   1 
ATOM   4552  C  CA  . LEU B  1 176 ? 11.584  17.559  28.029  1.00 18.86 ? 175 LEU B CA  1 
ATOM   4553  C  C   . LEU B  1 176 ? 12.309  17.394  29.360  1.00 19.69 ? 175 LEU B C   1 
ATOM   4554  O  O   . LEU B  1 176 ? 13.127  16.482  29.527  1.00 20.54 ? 175 LEU B O   1 
ATOM   4555  C  CB  . LEU B  1 176 ? 12.357  18.500  27.092  1.00 19.30 ? 175 LEU B CB  1 
ATOM   4556  C  CG  . LEU B  1 176 ? 11.908  18.493  25.633  1.00 19.38 ? 175 LEU B CG  1 
ATOM   4557  C  CD1 . LEU B  1 176 ? 12.618  19.597  24.878  1.00 19.76 ? 175 LEU B CD1 1 
ATOM   4558  C  CD2 . LEU B  1 176 ? 12.147  17.150  24.945  1.00 20.07 ? 175 LEU B CD2 1 
ATOM   4559  N  N   . GLN B  1 177 ? 12.040  18.278  30.311  1.00 20.74 ? 176 GLN B N   1 
ATOM   4560  C  CA  . GLN B  1 177 ? 12.650  18.155  31.657  1.00 21.86 ? 176 GLN B CA  1 
ATOM   4561  C  C   . GLN B  1 177 ? 12.258  16.843  32.342  1.00 22.80 ? 176 GLN B C   1 
ATOM   4562  O  O   . GLN B  1 177 ? 13.014  16.323  33.151  1.00 23.61 ? 176 GLN B O   1 
ATOM   4563  C  CB  . GLN B  1 177 ? 12.234  19.332  32.544  1.00 22.45 ? 176 GLN B CB  1 
ATOM   4564  C  CG  . GLN B  1 177 ? 12.951  20.625  32.185  1.00 22.29 ? 176 GLN B CG  1 
ATOM   4565  C  CD  . GLN B  1 177 ? 12.583  21.754  33.125  1.00 23.32 ? 176 GLN B CD  1 
ATOM   4566  O  OE1 . GLN B  1 177 ? 11.580  21.691  33.841  1.00 23.57 ? 176 GLN B OE1 1 
ATOM   4567  N  NE2 . GLN B  1 177 ? 13.391  22.817  33.120  1.00 23.99 ? 176 GLN B NE2 1 
ATOM   4568  N  N   . ARG B  1 178 ? 11.091  16.308  31.984  1.00 22.29 ? 177 ARG B N   1 
ATOM   4569  C  CA  . ARG B  1 178 ? 10.596  15.066  32.570  1.00 24.76 ? 177 ARG B CA  1 
ATOM   4570  C  C   . ARG B  1 178 ? 10.869  13.808  31.774  1.00 24.43 ? 177 ARG B C   1 
ATOM   4571  O  O   . ARG B  1 178 ? 10.476  12.737  32.212  1.00 25.16 ? 177 ARG B O   1 
ATOM   4572  C  CB  . ARG B  1 178 ? 9.119   15.200  32.882  1.00 27.08 ? 177 ARG B CB  1 
ATOM   4573  C  CG  . ARG B  1 178 ? 8.989   16.161  34.044  1.00 32.03 ? 177 ARG B CG  1 
ATOM   4574  C  CD  . ARG B  1 178 ? 7.616   16.704  34.251  1.00 35.56 ? 177 ARG B CD  1 
ATOM   4575  N  NE  . ARG B  1 178 ? 7.768   17.879  35.127  1.00 40.54 ? 177 ARG B NE  1 
ATOM   4576  C  CZ  . ARG B  1 178 ? 7.438   17.954  36.415  1.00 45.44 ? 177 ARG B CZ  1 
ATOM   4577  N  NH1 . ARG B  1 178 ? 6.880   16.915  37.050  1.00 49.41 ? 177 ARG B NH1 1 
ATOM   4578  N  NH2 . ARG B  1 178 ? 7.643   19.104  37.070  1.00 42.99 ? 177 ARG B NH2 1 
ATOM   4579  N  N   . GLN B  1 179 ? 11.587  13.896  30.657  1.00 22.63 ? 178 GLN B N   1 
ATOM   4580  C  CA  . GLN B  1 179 ? 11.987  12.689  29.934  1.00 22.79 ? 178 GLN B CA  1 
ATOM   4581  C  C   . GLN B  1 179 ? 13.441  12.398  30.262  1.00 23.99 ? 178 GLN B C   1 
ATOM   4582  O  O   . GLN B  1 179 ? 14.245  13.313  30.316  1.00 23.26 ? 178 GLN B O   1 
ATOM   4583  C  CB  . GLN B  1 179 ? 11.831  12.842  28.408  1.00 22.67 ? 178 GLN B CB  1 
ATOM   4584  C  CG  . GLN B  1 179 ? 10.453  13.263  27.908  1.00 23.49 ? 178 GLN B CG  1 
ATOM   4585  C  CD  . GLN B  1 179 ? 9.320   12.570  28.655  1.00 25.83 ? 178 GLN B CD  1 
ATOM   4586  O  OE1 . GLN B  1 179 ? 9.225   11.361  28.652  1.00 26.13 ? 178 GLN B OE1 1 
ATOM   4587  N  NE2 . GLN B  1 179 ? 8.472   13.349  29.319  1.00 28.42 ? 178 GLN B NE2 1 
ATOM   4588  N  N   . PRO B  1 180 ? 13.793  11.117  30.457  1.00 23.95 ? 179 PRO B N   1 
ATOM   4589  C  CA  . PRO B  1 180 ? 15.188  10.752  30.630  1.00 25.39 ? 179 PRO B CA  1 
ATOM   4590  C  C   . PRO B  1 180 ? 16.087  11.245  29.489  1.00 24.81 ? 179 PRO B C   1 
ATOM   4591  O  O   . PRO B  1 180 ? 15.669  11.311  28.333  1.00 22.95 ? 179 PRO B O   1 
ATOM   4592  C  CB  . PRO B  1 180 ? 15.157  9.223   30.643  1.00 26.07 ? 179 PRO B CB  1 
ATOM   4593  C  CG  . PRO B  1 180 ? 13.771  8.876   31.040  1.00 26.21 ? 179 PRO B CG  1 
ATOM   4594  C  CD  . PRO B  1 180 ? 12.913  9.937   30.443  1.00 24.86 ? 179 PRO B CD  1 
ATOM   4595  N  N   . GLN B  1 181 ? 17.329  11.585  29.830  1.00 25.59 ? 180 GLN B N   1 
ATOM   4596  C  CA  . GLN B  1 181 ? 18.282  12.056  28.829  1.00 25.71 ? 180 GLN B CA  1 
ATOM   4597  C  C   . GLN B  1 181 ? 18.449  11.050  27.689  1.00 24.79 ? 180 GLN B C   1 
ATOM   4598  O  O   . GLN B  1 181 ? 18.550  11.439  26.521  1.00 24.68 ? 180 GLN B O   1 
ATOM   4599  C  CB  . GLN B  1 181 ? 19.641  12.380  29.477  1.00 27.31 ? 180 GLN B CB  1 
ATOM   4600  C  CG  . GLN B  1 181 ? 20.639  13.032  28.525  1.00 28.72 ? 180 GLN B CG  1 
ATOM   4601  C  CD  . GLN B  1 181 ? 20.197  14.412  28.078  1.00 28.22 ? 180 GLN B CD  1 
ATOM   4602  O  OE1 . GLN B  1 181 ? 19.824  15.240  28.899  1.00 31.36 ? 180 GLN B OE1 1 
ATOM   4603  N  NE2 . GLN B  1 181 ? 20.189  14.654  26.780  1.00 27.79 ? 180 GLN B NE2 1 
ATOM   4604  N  N   . ALA B  1 182 ? 18.485  9.754   27.996  1.00 24.52 ? 181 ALA B N   1 
ATOM   4605  C  CA  . ALA B  1 182 ? 18.620  8.737   26.948  1.00 24.13 ? 181 ALA B CA  1 
ATOM   4606  C  C   . ALA B  1 182 ? 17.442  8.760   25.951  1.00 22.52 ? 181 ALA B C   1 
ATOM   4607  O  O   . ALA B  1 182 ? 17.617  8.507   24.765  1.00 22.25 ? 181 ALA B O   1 
ATOM   4608  C  CB  . ALA B  1 182 ? 18.778  7.344   27.550  1.00 25.21 ? 181 ALA B CB  1 
ATOM   4609  N  N   . TRP B  1 183 ? 16.254  9.075   26.445  1.00 21.39 ? 182 TRP B N   1 
ATOM   4610  C  CA  . TRP B  1 183 ? 15.061  9.164   25.586  1.00 20.47 ? 182 TRP B CA  1 
ATOM   4611  C  C   . TRP B  1 183 ? 15.224  10.358  24.634  1.00 19.97 ? 182 TRP B C   1 
ATOM   4612  O  O   . TRP B  1 183 ? 15.006  10.249  23.428  1.00 19.39 ? 182 TRP B O   1 
ATOM   4613  C  CB  . TRP B  1 183 ? 13.791  9.315   26.440  1.00 20.04 ? 182 TRP B CB  1 
ATOM   4614  C  CG  . TRP B  1 183 ? 12.505  9.301   25.622  1.00 19.41 ? 182 TRP B CG  1 
ATOM   4615  C  CD1 . TRP B  1 183 ? 11.742  8.201   25.329  1.00 19.39 ? 182 TRP B CD1 1 
ATOM   4616  C  CD2 . TRP B  1 183 ? 11.899  10.399  24.944  1.00 18.72 ? 182 TRP B CD2 1 
ATOM   4617  N  NE1 . TRP B  1 183 ? 10.681  8.558   24.538  1.00 18.84 ? 182 TRP B NE1 1 
ATOM   4618  C  CE2 . TRP B  1 183 ? 10.764  9.904   24.278  1.00 18.95 ? 182 TRP B CE2 1 
ATOM   4619  C  CE3 . TRP B  1 183 ? 12.198  11.765  24.844  1.00 18.61 ? 182 TRP B CE3 1 
ATOM   4620  C  CZ2 . TRP B  1 183 ? 9.945   10.713  23.506  1.00 17.88 ? 182 TRP B CZ2 1 
ATOM   4621  C  CZ3 . TRP B  1 183 ? 11.370  12.573  24.092  1.00 18.12 ? 182 TRP B CZ3 1 
ATOM   4622  C  CH2 . TRP B  1 183 ? 10.249  12.039  23.427  1.00 17.79 ? 182 TRP B CH2 1 
ATOM   4623  N  N   . LYS B  1 184 ? 15.633  11.495  25.188  1.00 20.50 ? 183 LYS B N   1 
ATOM   4624  C  CA  . LYS B  1 184 ? 15.791  12.708  24.363  1.00 20.10 ? 183 LYS B CA  1 
ATOM   4625  C  C   . LYS B  1 184 ? 16.902  12.538  23.312  1.00 20.91 ? 183 LYS B C   1 
ATOM   4626  O  O   . LYS B  1 184 ? 16.748  12.968  22.153  1.00 20.92 ? 183 LYS B O   1 
ATOM   4627  C  CB  . LYS B  1 184 ? 16.064  13.901  25.256  1.00 19.74 ? 183 LYS B CB  1 
ATOM   4628  C  CG  . LYS B  1 184 ? 14.856  14.242  26.110  1.00 19.71 ? 183 LYS B CG  1 
ATOM   4629  C  CD  . LYS B  1 184 ? 15.050  15.461  26.988  1.00 19.72 ? 183 LYS B CD  1 
ATOM   4630  C  CE  . LYS B  1 184 ? 16.048  15.226  28.095  1.00 20.46 ? 183 LYS B CE  1 
ATOM   4631  N  NZ  . LYS B  1 184 ? 15.930  16.279  29.128  1.00 20.77 ? 183 LYS B NZ  1 
ATOM   4632  N  N   . ASP B  1 185 ? 17.989  11.871  23.701  1.00 22.05 ? 184 ASP B N   1 
ATOM   4633  C  CA  . ASP B  1 185 ? 19.103  11.603  22.772  1.00 23.99 ? 184 ASP B CA  1 
ATOM   4634  C  C   . ASP B  1 185 ? 18.672  10.736  21.598  1.00 23.54 ? 184 ASP B C   1 
ATOM   4635  O  O   . ASP B  1 185 ? 19.151  10.898  20.481  1.00 22.41 ? 184 ASP B O   1 
ATOM   4636  C  CB  . ASP B  1 185 ? 20.287  10.923  23.485  1.00 26.27 ? 184 ASP B CB  1 
ATOM   4637  C  CG  . ASP B  1 185 ? 20.984  11.828  24.482  1.00 29.40 ? 184 ASP B CG  1 
ATOM   4638  O  OD1 . ASP B  1 185 ? 20.770  13.067  24.477  1.00 30.07 ? 184 ASP B OD1 1 
ATOM   4639  O  OD2 . ASP B  1 185 ? 21.784  11.299  25.290  1.00 31.94 ? 184 ASP B OD2 1 
ATOM   4640  N  N   . LYS B  1 186 ? 17.748  9.816   21.836  1.00 21.99 ? 185 LYS B N   1 
ATOM   4641  C  CA  . LYS B  1 186 ? 17.261  8.969   20.760  1.00 21.76 ? 185 LYS B CA  1 
ATOM   4642  C  C   . LYS B  1 186 ? 16.219  9.667   19.868  1.00 20.47 ? 185 LYS B C   1 
ATOM   4643  O  O   . LYS B  1 186 ? 16.290  9.576   18.645  1.00 20.43 ? 185 LYS B O   1 
ATOM   4644  C  CB  . LYS B  1 186 ? 16.653  7.699   21.366  1.00 21.47 ? 185 LYS B CB  1 
ATOM   4645  C  CG  . LYS B  1 186 ? 16.007  6.765   20.363  1.00 21.55 ? 185 LYS B CG  1 
ATOM   4646  C  CD  . LYS B  1 186 ? 15.701  5.412   21.018  1.00 22.24 ? 185 LYS B CD  1 
ATOM   4647  C  CE  . LYS B  1 186 ? 15.080  4.441   20.042  1.00 22.01 ? 185 LYS B CE  1 
ATOM   4648  N  NZ  . LYS B  1 186 ? 14.656  3.220   20.768  1.00 22.90 ? 185 LYS B NZ  1 
ATOM   4649  N  N   . TYR B  1 187 ? 15.238  10.322  20.494  1.00 19.92 ? 186 TYR B N   1 
ATOM   4650  C  CA  . TYR B  1 187 ? 14.026  10.713  19.787  1.00 19.03 ? 186 TYR B CA  1 
ATOM   4651  C  C   . TYR B  1 187 ? 13.946  12.158  19.313  1.00 18.27 ? 186 TYR B C   1 
ATOM   4652  O  O   . TYR B  1 187 ? 13.095  12.468  18.476  1.00 18.34 ? 186 TYR B O   1 
ATOM   4653  C  CB  . TYR B  1 187 ? 12.785  10.408  20.645  1.00 17.83 ? 186 TYR B CB  1 
ATOM   4654  C  CG  . TYR B  1 187 ? 12.514  8.942   20.812  1.00 17.93 ? 186 TYR B CG  1 
ATOM   4655  C  CD1 . TYR B  1 187 ? 12.028  8.180   19.758  1.00 18.21 ? 186 TYR B CD1 1 
ATOM   4656  C  CD2 . TYR B  1 187 ? 12.768  8.302   22.032  1.00 18.12 ? 186 TYR B CD2 1 
ATOM   4657  C  CE1 . TYR B  1 187 ? 11.817  6.810   19.903  1.00 18.60 ? 186 TYR B CE1 1 
ATOM   4658  C  CE2 . TYR B  1 187 ? 12.539  6.941   22.188  1.00 18.68 ? 186 TYR B CE2 1 
ATOM   4659  C  CZ  . TYR B  1 187 ? 12.051  6.203   21.132  1.00 18.81 ? 186 TYR B CZ  1 
ATOM   4660  O  OH  . TYR B  1 187 ? 11.835  4.844   21.327  1.00 20.18 ? 186 TYR B OH  1 
ATOM   4661  N  N   . ILE B  1 188 ? 14.758  13.036  19.877  1.00 19.02 ? 187 ILE B N   1 
ATOM   4662  C  CA  . ILE B  1 188 ? 14.648  14.480  19.575  1.00 19.18 ? 187 ILE B CA  1 
ATOM   4663  C  C   . ILE B  1 188 ? 15.874  14.938  18.809  1.00 20.30 ? 187 ILE B C   1 
ATOM   4664  O  O   . ILE B  1 188 ? 17.001  14.750  19.279  1.00 20.54 ? 187 ILE B O   1 
ATOM   4665  C  CB  . ILE B  1 188 ? 14.494  15.324  20.852  1.00 19.26 ? 187 ILE B CB  1 
ATOM   4666  C  CG1 . ILE B  1 188 ? 13.307  14.857  21.717  1.00 19.33 ? 187 ILE B CG1 1 
ATOM   4667  C  CG2 . ILE B  1 188 ? 14.339  16.816  20.508  1.00 19.47 ? 187 ILE B CG2 1 
ATOM   4668  C  CD1 . ILE B  1 188 ? 11.959  14.896  21.038  1.00 18.83 ? 187 ILE B CD1 1 
ATOM   4669  N  N   . ARG B  1 189 ? 15.658  15.480  17.611  1.00 20.90 ? 188 ARG B N   1 
ATOM   4670  C  CA  . ARG B  1 189 ? 16.736  16.015  16.788  1.00 21.99 ? 188 ARG B CA  1 
ATOM   4671  C  C   . ARG B  1 189 ? 17.070  17.436  17.229  1.00 20.49 ? 188 ARG B C   1 
ATOM   4672  O  O   . ARG B  1 189 ? 18.229  17.767  17.432  1.00 20.87 ? 188 ARG B O   1 
ATOM   4673  C  CB  . ARG B  1 189 ? 16.352  16.018  15.322  1.00 23.46 ? 188 ARG B CB  1 
ATOM   4674  C  CG  . ARG B  1 189 ? 17.466  16.507  14.420  1.00 28.13 ? 188 ARG B CG  1 
ATOM   4675  C  CD  . ARG B  1 189 ? 17.076  16.359  12.961  1.00 32.74 ? 188 ARG B CD  1 
ATOM   4676  N  NE  . ARG B  1 189 ? 18.236  16.449  12.094  1.00 42.12 ? 188 ARG B NE  1 
ATOM   4677  C  CZ  . ARG B  1 189 ? 19.009  15.417  11.756  1.00 49.02 ? 188 ARG B CZ  1 
ATOM   4678  N  NH1 . ARG B  1 189 ? 18.744  14.170  12.182  1.00 52.81 ? 188 ARG B NH1 1 
ATOM   4679  N  NH2 . ARG B  1 189 ? 20.057  15.638  10.976  1.00 52.95 ? 188 ARG B NH2 1 
ATOM   4680  N  N   . ALA B  1 190 ? 16.045  18.263  17.386  1.00 18.72 ? 189 ALA B N   1 
ATOM   4681  C  CA  . ALA B  1 190 ? 16.238  19.646  17.802  1.00 19.14 ? 189 ALA B CA  1 
ATOM   4682  C  C   . ALA B  1 190 ? 14.937  20.217  18.289  1.00 18.27 ? 189 ALA B C   1 
ATOM   4683  O  O   . ALA B  1 190 ? 13.871  19.654  18.043  1.00 18.49 ? 189 ALA B O   1 
ATOM   4684  C  CB  . ALA B  1 190 ? 16.774  20.463  16.628  1.00 19.55 ? 189 ALA B CB  1 
ATOM   4685  N  N   . PHE B  1 191 ? 15.040  21.323  19.015  1.00 19.04 ? 190 PHE B N   1 
ATOM   4686  C  CA  . PHE B  1 191 ? 13.901  22.089  19.537  1.00 18.36 ? 190 PHE B CA  1 
ATOM   4687  C  C   . PHE B  1 191 ? 14.093  23.522  19.020  1.00 19.08 ? 190 PHE B C   1 
ATOM   4688  O  O   . PHE B  1 191 ? 15.091  24.175  19.341  1.00 19.49 ? 190 PHE B O   1 
ATOM   4689  C  CB  . PHE B  1 191 ? 13.920  21.982  21.061  1.00 18.74 ? 190 PHE B CB  1 
ATOM   4690  C  CG  . PHE B  1 191 ? 12.909  22.834  21.812  1.00 18.45 ? 190 PHE B CG  1 
ATOM   4691  C  CD1 . PHE B  1 191 ? 11.832  23.447  21.202  1.00 18.78 ? 190 PHE B CD1 1 
ATOM   4692  C  CD2 . PHE B  1 191 ? 13.057  22.979  23.178  1.00 18.80 ? 190 PHE B CD2 1 
ATOM   4693  C  CE1 . PHE B  1 191 ? 10.952  24.241  21.935  1.00 19.05 ? 190 PHE B CE1 1 
ATOM   4694  C  CE2 . PHE B  1 191 ? 12.168  23.721  23.921  1.00 19.35 ? 190 PHE B CE2 1 
ATOM   4695  C  CZ  . PHE B  1 191 ? 11.110  24.362  23.300  1.00 18.63 ? 190 PHE B CZ  1 
ATOM   4696  N  N   . VAL B  1 192 ? 13.183  23.952  18.148  1.00 18.93 ? 191 VAL B N   1 
ATOM   4697  C  CA  . VAL B  1 192 ? 13.170  25.314  17.615  1.00 18.88 ? 191 VAL B CA  1 
ATOM   4698  C  C   . VAL B  1 192 ? 12.124  26.070  18.442  1.00 18.11 ? 191 VAL B C   1 
ATOM   4699  O  O   . VAL B  1 192 ? 10.934  25.774  18.391  1.00 16.82 ? 191 VAL B O   1 
ATOM   4700  C  CB  . VAL B  1 192 ? 12.838  25.346  16.111  1.00 19.72 ? 191 VAL B CB  1 
ATOM   4701  C  CG1 . VAL B  1 192 ? 12.761  26.779  15.593  1.00 21.18 ? 191 VAL B CG1 1 
ATOM   4702  C  CG2 . VAL B  1 192 ? 13.868  24.576  15.302  1.00 20.88 ? 191 VAL B CG2 1 
ATOM   4703  N  N   . SER B  1 193 ? 12.599  27.061  19.187  1.00 18.40 ? 192 SER B N   1 
ATOM   4704  C  CA  . SER B  1 193 ? 11.810  27.777  20.170  1.00 18.59 ? 192 SER B CA  1 
ATOM   4705  C  C   . SER B  1 193 ? 11.517  29.179  19.642  1.00 18.47 ? 192 SER B C   1 
ATOM   4706  O  O   . SER B  1 193 ? 12.453  29.968  19.424  1.00 18.85 ? 192 SER B O   1 
ATOM   4707  C  CB  . SER B  1 193 ? 12.662  27.844  21.432  1.00 21.78 ? 192 SER B CB  1 
ATOM   4708  O  OG  . SER B  1 193 ? 11.996  28.490  22.461  1.00 24.20 ? 192 SER B OG  1 
ATOM   4709  N  N   . LEU B  1 194 ? 10.249  29.484  19.375  1.00 17.44 ? 193 LEU B N   1 
ATOM   4710  C  CA  . LEU B  1 194 ? 9.866   30.771  18.792  1.00 18.79 ? 193 LEU B CA  1 
ATOM   4711  C  C   . LEU B  1 194 ? 9.112   31.655  19.803  1.00 18.56 ? 193 LEU B C   1 
ATOM   4712  O  O   . LEU B  1 194 ? 7.979   31.327  20.206  1.00 17.79 ? 193 LEU B O   1 
ATOM   4713  C  CB  . LEU B  1 194 ? 8.991   30.544  17.552  1.00 19.23 ? 193 LEU B CB  1 
ATOM   4714  C  CG  . LEU B  1 194 ? 9.525   29.617  16.459  1.00 20.44 ? 193 LEU B CG  1 
ATOM   4715  C  CD1 . LEU B  1 194 ? 8.479   29.406  15.379  1.00 21.53 ? 193 LEU B CD1 1 
ATOM   4716  C  CD2 . LEU B  1 194 ? 10.796  30.125  15.835  1.00 21.37 ? 193 LEU B CD2 1 
ATOM   4717  N  N   . GLY B  1 195 ? 9.733   32.756  20.232  1.00 19.36 ? 194 GLY B N   1 
ATOM   4718  C  CA  . GLY B  1 195 ? 9.052   33.699  21.120  1.00 18.93 ? 194 GLY B CA  1 
ATOM   4719  C  C   . GLY B  1 195 ? 8.716   33.131  22.491  1.00 18.53 ? 194 GLY B C   1 
ATOM   4720  O  O   . GLY B  1 195 ? 7.605   33.329  23.003  1.00 17.10 ? 194 GLY B O   1 
ATOM   4721  N  N   . ALA B  1 196 ? 9.661   32.397  23.082  1.00 18.23 ? 195 ALA B N   1 
ATOM   4722  C  CA  . ALA B  1 196 ? 9.427   31.718  24.367  1.00 18.10 ? 195 ALA B CA  1 
ATOM   4723  C  C   . ALA B  1 196 ? 9.408   32.700  25.560  1.00 18.53 ? 195 ALA B C   1 
ATOM   4724  O  O   . ALA B  1 196 ? 10.372  33.453  25.766  1.00 18.51 ? 195 ALA B O   1 
ATOM   4725  C  CB  . ALA B  1 196 ? 10.488  30.668  24.615  1.00 17.38 ? 195 ALA B CB  1 
ATOM   4726  N  N   . PRO B  1 197 ? 8.327   32.665  26.374  1.00 18.15 ? 196 PRO B N   1 
ATOM   4727  C  CA  . PRO B  1 197 ? 8.240   33.490  27.605  1.00 18.70 ? 196 PRO B CA  1 
ATOM   4728  C  C   . PRO B  1 197 ? 8.860   32.795  28.816  1.00 19.03 ? 196 PRO B C   1 
ATOM   4729  O  O   . PRO B  1 197 ? 8.186   32.556  29.820  1.00 20.79 ? 196 PRO B O   1 
ATOM   4730  C  CB  . PRO B  1 197 ? 6.721   33.665  27.777  1.00 18.16 ? 196 PRO B CB  1 
ATOM   4731  C  CG  . PRO B  1 197 ? 6.189   32.346  27.334  1.00 18.25 ? 196 PRO B CG  1 
ATOM   4732  C  CD  . PRO B  1 197 ? 7.063   31.935  26.151  1.00 18.53 ? 196 PRO B CD  1 
ATOM   4733  N  N   A TRP B  1 198 ? 10.157  32.503  28.708  0.80 20.35 ? 197 TRP B N   1 
ATOM   4734  N  N   B TRP B  1 198 ? 10.148  32.469  28.726  0.20 18.98 ? 197 TRP B N   1 
ATOM   4735  C  CA  A TRP B  1 198 ? 10.873  31.852  29.760  0.80 20.38 ? 197 TRP B CA  1 
ATOM   4736  C  CA  B TRP B  1 198 ? 10.836  31.607  29.713  0.20 18.45 ? 197 TRP B CA  1 
ATOM   4737  C  C   A TRP B  1 198 ? 10.827  32.882  30.902  0.80 20.60 ? 197 TRP B C   1 
ATOM   4738  C  C   B TRP B  1 198 ? 10.580  31.818  31.238  0.20 17.99 ? 197 TRP B C   1 
ATOM   4739  O  O   A TRP B  1 198 ? 11.133  34.079  30.753  0.80 23.55 ? 197 TRP B O   1 
ATOM   4740  O  O   B TRP B  1 198 ? 10.306  30.861  31.961  0.20 17.00 ? 197 TRP B O   1 
ATOM   4741  C  CB  A TRP B  1 198 ? 12.338  31.638  29.413  0.80 20.68 ? 197 TRP B CB  1 
ATOM   4742  C  CB  B TRP B  1 198 ? 12.334  31.612  29.422  0.20 19.03 ? 197 TRP B CB  1 
ATOM   4743  C  CG  A TRP B  1 198 ? 12.669  30.930  28.094  0.80 20.83 ? 197 TRP B CG  1 
ATOM   4744  C  CG  B TRP B  1 198 ? 12.697  30.917  28.111  0.20 19.24 ? 197 TRP B CG  1 
ATOM   4745  C  CD1 A TRP B  1 198 ? 13.496  31.395  27.125  0.80 20.86 ? 197 TRP B CD1 1 
ATOM   4746  C  CD1 B TRP B  1 198 ? 13.513  31.395  27.126  0.20 19.60 ? 197 TRP B CD1 1 
ATOM   4747  C  CD2 A TRP B  1 198 ? 12.243  29.629  27.663  0.80 21.29 ? 197 TRP B CD2 1 
ATOM   4748  C  CD2 B TRP B  1 198 ? 12.253  29.623  27.666  0.20 19.19 ? 197 TRP B CD2 1 
ATOM   4749  N  NE1 A TRP B  1 198 ? 13.599  30.487  26.109  0.80 21.85 ? 197 TRP B NE1 1 
ATOM   4750  N  NE1 B TRP B  1 198 ? 13.608  30.481  26.103  0.20 19.85 ? 197 TRP B NE1 1 
ATOM   4751  C  CE2 A TRP B  1 198 ? 12.841  29.391  26.414  0.80 21.73 ? 197 TRP B CE2 1 
ATOM   4752  C  CE2 B TRP B  1 198 ? 12.847  29.386  26.411  0.20 19.50 ? 197 TRP B CE2 1 
ATOM   4753  C  CE3 A TRP B  1 198 ? 11.398  28.653  28.206  0.80 22.30 ? 197 TRP B CE3 1 
ATOM   4754  C  CE3 B TRP B  1 198 ? 11.414  28.645  28.210  0.20 19.16 ? 197 TRP B CE3 1 
ATOM   4755  C  CZ2 A TRP B  1 198 ? 12.631  28.200  25.685  0.80 22.82 ? 197 TRP B CZ2 1 
ATOM   4756  C  CZ2 B TRP B  1 198 ? 12.626  28.207  25.684  0.20 19.65 ? 197 TRP B CZ2 1 
ATOM   4757  C  CZ3 A TRP B  1 198 ? 11.185  27.473  27.476  0.80 21.56 ? 197 TRP B CZ3 1 
ATOM   4758  C  CZ3 B TRP B  1 198 ? 11.197  27.475  27.486  0.20 18.92 ? 197 TRP B CZ3 1 
ATOM   4759  C  CH2 A TRP B  1 198 ? 11.795  27.267  26.246  0.80 21.30 ? 197 TRP B CH2 1 
ATOM   4760  C  CH2 B TRP B  1 198 ? 11.799  27.270  26.243  0.20 19.03 ? 197 TRP B CH2 1 
ATOM   4761  N  N   A GLY B  1 199 ? 10.469  32.421  32.057  0.80 20.86 ? 198 GLY B N   1 
ATOM   4762  N  N   B GLY B  1 199 ? 10.679  33.056  31.716  0.20 18.20 ? 198 GLY B N   1 
ATOM   4763  C  CA  A GLY B  1 199 ? 10.410  33.333  33.211  0.80 20.64 ? 198 GLY B CA  1 
ATOM   4764  C  CA  B GLY B  1 199 ? 10.436  33.404  33.136  0.20 18.68 ? 198 GLY B CA  1 
ATOM   4765  C  C   A GLY B  1 199 ? 9.191   34.255  33.300  0.80 19.43 ? 198 GLY B C   1 
ATOM   4766  C  C   B GLY B  1 199 ? 9.201   34.278  33.281  0.20 18.62 ? 198 GLY B C   1 
ATOM   4767  O  O   A GLY B  1 199 ? 9.162   35.127  34.155  0.80 18.33 ? 198 GLY B O   1 
ATOM   4768  O  O   B GLY B  1 199 ? 9.157   35.136  34.154  0.20 18.49 ? 198 GLY B O   1 
ATOM   4769  N  N   . GLY B  1 200 ? 8.197   34.036  32.437  1.00 18.80 ? 199 GLY B N   1 
ATOM   4770  C  CA  . GLY B  1 200 ? 6.913   34.754  32.475  1.00 19.03 ? 199 GLY B CA  1 
ATOM   4771  C  C   . GLY B  1 200 ? 6.970   36.098  31.763  1.00 20.08 ? 199 GLY B C   1 
ATOM   4772  O  O   . GLY B  1 200 ? 8.044   36.509  31.309  1.00 20.34 ? 199 GLY B O   1 
ATOM   4773  N  N   . VAL B  1 201 ? 5.830   36.783  31.678  1.00 18.83 ? 200 VAL B N   1 
ATOM   4774  C  CA  . VAL B  1 201 ? 5.783   38.075  30.989  1.00 19.96 ? 200 VAL B CA  1 
ATOM   4775  C  C   . VAL B  1 201 ? 5.071   39.120  31.835  1.00 19.38 ? 200 VAL B C   1 
ATOM   4776  O  O   . VAL B  1 201 ? 4.097   38.803  32.516  1.00 18.17 ? 200 VAL B O   1 
ATOM   4777  C  CB  . VAL B  1 201 ? 5.143   37.993  29.586  1.00 23.08 ? 200 VAL B CB  1 
ATOM   4778  C  CG1 . VAL B  1 201 ? 5.886   36.992  28.679  1.00 24.13 ? 200 VAL B CG1 1 
ATOM   4779  C  CG2 . VAL B  1 201 ? 3.689   37.622  29.656  1.00 22.75 ? 200 VAL B CG2 1 
ATOM   4780  N  N   . ALA B  1 202 ? 5.528   40.367  31.770  1.00 19.17 ? 201 ALA B N   1 
ATOM   4781  C  CA  . ALA B  1 202 ? 4.986   41.419  32.608  1.00 19.82 ? 201 ALA B CA  1 
ATOM   4782  C  C   . ALA B  1 202 ? 3.507   41.673  32.311  1.00 20.32 ? 201 ALA B C   1 
ATOM   4783  O  O   . ALA B  1 202 ? 2.745   41.996  33.208  1.00 20.58 ? 201 ALA B O   1 
ATOM   4784  C  CB  . ALA B  1 202 ? 5.767   42.705  32.410  1.00 19.78 ? 201 ALA B CB  1 
ATOM   4785  N  N   . LYS B  1 203 ? 3.085   41.543  31.061  1.00 20.97 ? 202 LYS B N   1 
ATOM   4786  C  CA  . LYS B  1 203 ? 1.698   41.915  30.743  1.00 22.70 ? 202 LYS B CA  1 
ATOM   4787  C  C   . LYS B  1 203 ? 0.621   41.030  31.396  1.00 21.35 ? 202 LYS B C   1 
ATOM   4788  O  O   . LYS B  1 203 ? -0.550  41.418  31.450  1.00 19.96 ? 202 LYS B O   1 
ATOM   4789  C  CB  . LYS B  1 203 ? 1.464   42.054  29.245  1.00 27.42 ? 202 LYS B CB  1 
ATOM   4790  C  CG  . LYS B  1 203 ? 1.312   40.783  28.478  1.00 32.27 ? 202 LYS B CG  1 
ATOM   4791  C  CD  . LYS B  1 203 ? 1.030   41.069  27.007  1.00 39.09 ? 202 LYS B CD  1 
ATOM   4792  C  CE  . LYS B  1 203 ? -0.204  41.932  26.825  1.00 42.75 ? 202 LYS B CE  1 
ATOM   4793  N  NZ  . LYS B  1 203 ? -0.794  41.790  25.469  1.00 47.34 ? 202 LYS B NZ  1 
ATOM   4794  N  N   . THR B  1 204 ? 1.018   39.871  31.914  1.00 19.82 ? 203 THR B N   1 
ATOM   4795  C  CA  . THR B  1 204 ? 0.127   38.998  32.679  1.00 20.48 ? 203 THR B CA  1 
ATOM   4796  C  C   . THR B  1 204 ? -0.512  39.737  33.883  1.00 19.77 ? 203 THR B C   1 
ATOM   4797  O  O   . THR B  1 204 ? -1.680  39.518  34.207  1.00 18.22 ? 203 THR B O   1 
ATOM   4798  C  CB  . THR B  1 204 ? 0.904   37.788  33.207  1.00 22.10 ? 203 THR B CB  1 
ATOM   4799  O  OG1 . THR B  1 204 ? 1.580   37.125  32.119  1.00 24.25 ? 203 THR B OG1 1 
ATOM   4800  C  CG2 . THR B  1 204 ? -0.020  36.818  33.841  1.00 23.38 ? 203 THR B CG2 1 
ATOM   4801  N  N   . LEU B  1 205 ? 0.242   40.631  34.512  1.00 19.91 ? 204 LEU B N   1 
ATOM   4802  C  CA  . LEU B  1 205 ? -0.317  41.437  35.607  1.00 21.24 ? 204 LEU B CA  1 
ATOM   4803  C  C   . LEU B  1 205 ? -1.492  42.294  35.138  1.00 21.30 ? 204 LEU B C   1 
ATOM   4804  O  O   . LEU B  1 205 ? -2.514  42.354  35.806  1.00 20.27 ? 204 LEU B O   1 
ATOM   4805  C  CB  . LEU B  1 205 ? 0.723   42.377  36.198  1.00 22.63 ? 204 LEU B CB  1 
ATOM   4806  C  CG  . LEU B  1 205 ? 1.792   41.881  37.182  1.00 25.50 ? 204 LEU B CG  1 
ATOM   4807  C  CD1 . LEU B  1 205 ? 1.242   41.323  38.483  1.00 27.05 ? 204 LEU B CD1 1 
ATOM   4808  C  CD2 . LEU B  1 205 ? 2.751   40.904  36.570  1.00 24.17 ? 204 LEU B CD2 1 
ATOM   4809  N  N   . ARG B  1 206 ? -1.367  42.944  33.987  1.00 21.23 ? 205 ARG B N   1 
ATOM   4810  C  CA  . ARG B  1 206 ? -2.458  43.776  33.463  1.00 22.31 ? 205 ARG B CA  1 
ATOM   4811  C  C   . ARG B  1 206 ? -3.664  42.916  33.079  1.00 21.62 ? 205 ARG B C   1 
ATOM   4812  O  O   . ARG B  1 206 ? -4.800  43.286  33.349  1.00 21.37 ? 205 ARG B O   1 
ATOM   4813  C  CB  . ARG B  1 206 ? -2.011  44.618  32.260  1.00 25.28 ? 205 ARG B CB  1 
ATOM   4814  C  CG  . ARG B  1 206 ? -3.131  45.454  31.646  1.00 28.96 ? 205 ARG B CG  1 
ATOM   4815  C  CD  . ARG B  1 206 ? -2.619  46.184  30.410  1.00 35.00 ? 205 ARG B CD  1 
ATOM   4816  N  NE  . ARG B  1 206 ? -3.564  47.131  29.813  1.00 41.03 ? 205 ARG B NE  1 
ATOM   4817  C  CZ  . ARG B  1 206 ? -4.492  46.825  28.910  1.00 45.46 ? 205 ARG B CZ  1 
ATOM   4818  N  NH1 . ARG B  1 206 ? -4.640  45.582  28.466  1.00 46.31 ? 205 ARG B NH1 1 
ATOM   4819  N  NH2 . ARG B  1 206 ? -5.293  47.783  28.451  1.00 46.95 ? 205 ARG B NH2 1 
ATOM   4820  N  N   . VAL B  1 207 ? -3.408  41.773  32.428  1.00 20.99 ? 206 VAL B N   1 
ATOM   4821  C  CA  . VAL B  1 207 ? -4.474  40.843  32.042  1.00 21.22 ? 206 VAL B CA  1 
ATOM   4822  C  C   . VAL B  1 207 ? -5.324  40.484  33.265  1.00 20.30 ? 206 VAL B C   1 
ATOM   4823  O  O   . VAL B  1 207 ? -6.557  40.623  33.242  1.00 21.69 ? 206 VAL B O   1 
ATOM   4824  C  CB  . VAL B  1 207 ? -3.916  39.558  31.361  1.00 20.66 ? 206 VAL B CB  1 
ATOM   4825  C  CG1 . VAL B  1 207 ? -5.015  38.529  31.130  1.00 22.42 ? 206 VAL B CG1 1 
ATOM   4826  C  CG2 . VAL B  1 207 ? -3.240  39.914  30.049  1.00 21.90 ? 206 VAL B CG2 1 
ATOM   4827  N  N   . LEU B  1 208 ? -4.669  40.040  34.328  1.00 18.98 ? 207 LEU B N   1 
ATOM   4828  C  CA  . LEU B  1 208 ? -5.369  39.580  35.523  1.00 19.38 ? 207 LEU B CA  1 
ATOM   4829  C  C   . LEU B  1 208 ? -6.054  40.736  36.249  1.00 20.06 ? 207 LEU B C   1 
ATOM   4830  O  O   . LEU B  1 208 ? -7.149  40.569  36.765  1.00 19.13 ? 207 LEU B O   1 
ATOM   4831  C  CB  . LEU B  1 208 ? -4.394  38.864  36.466  1.00 19.68 ? 207 LEU B CB  1 
ATOM   4832  C  CG  . LEU B  1 208 ? -3.888  37.520  35.935  1.00 19.13 ? 207 LEU B CG  1 
ATOM   4833  C  CD1 . LEU B  1 208 ? -2.681  37.052  36.707  1.00 19.71 ? 207 LEU B CD1 1 
ATOM   4834  C  CD2 . LEU B  1 208 ? -4.992  36.474  36.015  1.00 19.93 ? 207 LEU B CD2 1 
ATOM   4835  N  N   . ALA B  1 209 ? -5.395  41.892  36.317  1.00 19.24 ? 208 ALA B N   1 
ATOM   4836  C  CA  . ALA B  1 209 ? -5.940  43.026  37.060  1.00 20.44 ? 208 ALA B CA  1 
ATOM   4837  C  C   . ALA B  1 209 ? -7.160  43.609  36.363  1.00 21.98 ? 208 ALA B C   1 
ATOM   4838  O  O   . ALA B  1 209 ? -8.220  43.732  36.982  1.00 22.18 ? 208 ALA B O   1 
ATOM   4839  C  CB  . ALA B  1 209 ? -4.877  44.120  37.280  1.00 19.92 ? 208 ALA B CB  1 
ATOM   4840  N  N   . SER B  1 210 ? -7.005  43.979  35.094  1.00 22.63 ? 209 SER B N   1 
ATOM   4841  C  CA  . SER B  1 210 ? -7.979  44.807  34.420  1.00 24.96 ? 209 SER B CA  1 
ATOM   4842  C  C   . SER B  1 210 ? -8.476  44.268  33.077  1.00 26.37 ? 209 SER B C   1 
ATOM   4843  O  O   . SER B  1 210 ? -9.292  44.907  32.432  1.00 28.13 ? 209 SER B O   1 
ATOM   4844  C  CB  . SER B  1 210 ? -7.439  46.266  34.329  1.00 26.83 ? 209 SER B CB  1 
ATOM   4845  O  OG  . SER B  1 210 ? -6.141  46.360  33.818  1.00 26.91 ? 209 SER B OG  1 
ATOM   4846  N  N   . GLY B  1 211 ? -8.018  43.079  32.672  1.00 26.36 ? 210 GLY B N   1 
ATOM   4847  C  CA  . GLY B  1 211 ? -8.465  42.437  31.434  1.00 27.94 ? 210 GLY B CA  1 
ATOM   4848  C  C   . GLY B  1 211 ? -7.704  42.954  30.226  1.00 30.48 ? 210 GLY B C   1 
ATOM   4849  O  O   . GLY B  1 211 ? -7.093  44.021  30.263  1.00 30.30 ? 210 GLY B O   1 
ATOM   4850  N  N   . ASP B  1 212 ? -7.733  42.184  29.149  1.00 33.48 ? 211 ASP B N   1 
ATOM   4851  C  CA  . ASP B  1 212 ? -7.086  42.583  27.912  1.00 35.32 ? 211 ASP B CA  1 
ATOM   4852  C  C   . ASP B  1 212 ? -8.012  42.211  26.757  1.00 37.41 ? 211 ASP B C   1 
ATOM   4853  O  O   . ASP B  1 212 ? -8.125  41.040  26.394  1.00 36.21 ? 211 ASP B O   1 
ATOM   4854  C  CB  . ASP B  1 212 ? -5.731  41.876  27.763  1.00 35.46 ? 211 ASP B CB  1 
ATOM   4855  C  CG  . ASP B  1 212 ? -4.945  42.337  26.532  1.00 39.12 ? 211 ASP B CG  1 
ATOM   4856  O  OD1 . ASP B  1 212 ? -5.417  43.210  25.771  1.00 39.72 ? 211 ASP B OD1 1 
ATOM   4857  O  OD2 . ASP B  1 212 ? -3.832  41.812  26.334  1.00 45.33 ? 211 ASP B OD2 1 
ATOM   4858  N  N   . ASN B  1 213 ? -8.655  43.216  26.177  1.00 39.31 ? 212 ASN B N   1 
ATOM   4859  C  CA  . ASN B  1 213 ? -9.542  43.002  25.025  1.00 44.81 ? 212 ASN B CA  1 
ATOM   4860  C  C   . ASN B  1 213 ? -8.849  43.220  23.683  1.00 50.12 ? 212 ASN B C   1 
ATOM   4861  O  O   . ASN B  1 213 ? -9.527  43.347  22.657  1.00 49.34 ? 212 ASN B O   1 
ATOM   4862  C  CB  . ASN B  1 213 ? -10.803 43.857  25.161  1.00 46.47 ? 212 ASN B CB  1 
ATOM   4863  C  CG  . ASN B  1 213 ? -10.519 45.331  24.966  1.00 48.99 ? 212 ASN B CG  1 
ATOM   4864  O  OD1 . ASN B  1 213 ? -9.363  45.731  24.842  1.00 47.79 ? 212 ASN B OD1 1 
ATOM   4865  N  ND2 . ASN B  1 213 ? -11.558 46.148  24.944  1.00 51.58 ? 212 ASN B ND2 1 
ATOM   4866  N  N   . ASN B  1 214 ? -7.515  43.312  23.699  1.00 53.07 ? 213 ASN B N   1 
ATOM   4867  C  CA  . ASN B  1 214 ? -6.709  43.240  22.495  1.00 59.19 ? 213 ASN B CA  1 
ATOM   4868  C  C   . ASN B  1 214 ? -7.042  44.283  21.453  1.00 62.53 ? 213 ASN B C   1 
ATOM   4869  O  O   . ASN B  1 214 ? -6.737  44.066  20.299  1.00 63.96 ? 213 ASN B O   1 
ATOM   4870  C  CB  . ASN B  1 214 ? -6.896  41.846  21.905  1.00 63.07 ? 213 ASN B CB  1 
ATOM   4871  C  CG  . ASN B  1 214 ? -5.807  41.450  20.926  1.00 65.83 ? 213 ASN B CG  1 
ATOM   4872  O  OD1 . ASN B  1 214 ? -4.847  42.187  20.687  1.00 69.10 ? 213 ASN B OD1 1 
ATOM   4873  N  ND2 . ASN B  1 214 ? -5.944  40.258  20.369  1.00 67.14 ? 213 ASN B ND2 1 
ATOM   4874  N  N   . ARG B  1 215 ? -7.673  45.390  21.865  1.00 70.31 ? 214 ARG B N   1 
ATOM   4875  C  CA  . ARG B  1 215 ? -8.134  46.488  20.976  1.00 76.75 ? 214 ARG B CA  1 
ATOM   4876  C  C   . ARG B  1 215 ? -9.329  46.087  20.087  1.00 76.96 ? 214 ARG B C   1 
ATOM   4877  O  O   . ARG B  1 215 ? -9.566  46.675  19.028  1.00 82.89 ? 214 ARG B O   1 
ATOM   4878  C  CB  . ARG B  1 215 ? -6.968  47.095  20.171  1.00 79.96 ? 214 ARG B CB  1 
ATOM   4879  C  CG  . ARG B  1 215 ? -5.900  47.780  21.020  1.00 81.87 ? 214 ARG B CG  1 
ATOM   4880  C  CD  . ARG B  1 215 ? -4.620  47.981  20.254  1.00 84.82 ? 214 ARG B CD  1 
ATOM   4881  N  NE  . ARG B  1 215 ? -3.841  46.730  20.092  1.00 86.07 ? 214 ARG B NE  1 
ATOM   4882  C  CZ  . ARG B  1 215 ? -3.850  45.912  19.026  1.00 87.65 ? 214 ARG B CZ  1 
ATOM   4883  N  NH1 . ARG B  1 215 ? -4.625  46.126  17.959  1.00 89.31 ? 214 ARG B NH1 1 
ATOM   4884  N  NH2 . ARG B  1 215 ? -3.071  44.826  19.035  1.00 85.86 ? 214 ARG B NH2 1 
ATOM   4885  N  N   . ILE B  1 216 ? -10.065 45.075  20.549  1.00 74.32 ? 215 ILE B N   1 
ATOM   4886  C  CA  . ILE B  1 216 ? -11.403 44.738  20.084  1.00 70.76 ? 215 ILE B CA  1 
ATOM   4887  C  C   . ILE B  1 216 ? -12.380 45.462  21.013  1.00 72.57 ? 215 ILE B C   1 
ATOM   4888  O  O   . ILE B  1 216 ? -12.802 44.871  22.000  1.00 75.73 ? 215 ILE B O   1 
ATOM   4889  C  CB  . ILE B  1 216 ? -11.624 43.215  20.121  1.00 67.65 ? 215 ILE B CB  1 
ATOM   4890  C  CG1 . ILE B  1 216 ? -10.612 42.544  19.196  1.00 63.50 ? 215 ILE B CG1 1 
ATOM   4891  C  CG2 . ILE B  1 216 ? -13.049 42.843  19.697  1.00 69.10 ? 215 ILE B CG2 1 
ATOM   4892  C  CD1 . ILE B  1 216 ? -10.309 41.122  19.579  1.00 61.23 ? 215 ILE B CD1 1 
ATOM   4893  N  N   . PRO B  1 217 ? -12.717 46.749  20.723  1.00 73.46 ? 216 PRO B N   1 
ATOM   4894  C  CA  . PRO B  1 217 ? -13.551 47.575  21.622  1.00 73.71 ? 216 PRO B CA  1 
ATOM   4895  C  C   . PRO B  1 217 ? -14.978 47.078  21.859  1.00 72.37 ? 216 PRO B C   1 
ATOM   4896  O  O   . PRO B  1 217 ? -15.616 47.502  22.828  1.00 75.19 ? 216 PRO B O   1 
ATOM   4897  C  CB  . PRO B  1 217 ? -13.602 48.939  20.907  1.00 76.81 ? 216 PRO B CB  1 
ATOM   4898  C  CG  . PRO B  1 217 ? -13.334 48.629  19.478  1.00 75.62 ? 216 PRO B CG  1 
ATOM   4899  C  CD  . PRO B  1 217 ? -12.320 47.524  19.533  1.00 75.46 ? 216 PRO B CD  1 
ATOM   4900  N  N   . VAL B  1 218 ? -15.488 46.219  20.981  1.00 68.32 ? 217 VAL B N   1 
ATOM   4901  C  CA  . VAL B  1 218 ? -16.808 45.642  21.198  1.00 66.45 ? 217 VAL B CA  1 
ATOM   4902  C  C   . VAL B  1 218 ? -16.782 44.586  22.315  1.00 62.79 ? 217 VAL B C   1 
ATOM   4903  O  O   . VAL B  1 218 ? -17.830 44.115  22.745  1.00 61.40 ? 217 VAL B O   1 
ATOM   4904  C  CB  . VAL B  1 218 ? -17.403 45.064  19.892  1.00 67.88 ? 217 VAL B CB  1 
ATOM   4905  C  CG1 . VAL B  1 218 ? -16.772 43.721  19.538  1.00 67.13 ? 217 VAL B CG1 1 
ATOM   4906  C  CG2 . VAL B  1 218 ? -18.920 44.948  20.001  1.00 69.65 ? 217 VAL B CG2 1 
ATOM   4907  N  N   . ILE B  1 219 ? -15.589 44.189  22.765  1.00 58.16 ? 218 ILE B N   1 
ATOM   4908  C  CA  . ILE B  1 219 ? -15.472 43.334  23.955  1.00 55.72 ? 218 ILE B CA  1 
ATOM   4909  C  C   . ILE B  1 219 ? -14.972 44.181  25.114  1.00 51.00 ? 218 ILE B C   1 
ATOM   4910  O  O   . ILE B  1 219 ? -13.889 44.716  25.027  1.00 48.74 ? 218 ILE B O   1 
ATOM   4911  C  CB  . ILE B  1 219 ? -14.491 42.161  23.720  1.00 53.94 ? 218 ILE B CB  1 
ATOM   4912  C  CG1 . ILE B  1 219 ? -14.831 41.444  22.425  1.00 54.25 ? 218 ILE B CG1 1 
ATOM   4913  C  CG2 . ILE B  1 219 ? -14.537 41.164  24.866  1.00 54.99 ? 218 ILE B CG2 1 
ATOM   4914  C  CD1 . ILE B  1 219 ? -13.826 40.387  22.043  1.00 54.43 ? 218 ILE B CD1 1 
ATOM   4915  N  N   . GLY B  1 220 ? -15.761 44.331  26.176  1.00 48.57 ? 219 GLY B N   1 
ATOM   4916  C  CA  . GLY B  1 220 ? -15.301 45.069  27.349  1.00 48.90 ? 219 GLY B CA  1 
ATOM   4917  C  C   . GLY B  1 220 ? -14.118 44.329  27.959  1.00 47.00 ? 219 GLY B C   1 
ATOM   4918  O  O   . GLY B  1 220 ? -14.136 43.093  28.034  1.00 44.54 ? 219 GLY B O   1 
ATOM   4919  N  N   . PRO B  1 221 ? -13.068 45.065  28.366  1.00 45.30 ? 220 PRO B N   1 
ATOM   4920  C  CA  . PRO B  1 221 ? -11.960 44.367  29.010  1.00 42.04 ? 220 PRO B CA  1 
ATOM   4921  C  C   . PRO B  1 221 ? -12.400 43.679  30.316  1.00 41.15 ? 220 PRO B C   1 
ATOM   4922  O  O   . PRO B  1 221 ? -11.904 42.613  30.625  1.00 36.37 ? 220 PRO B O   1 
ATOM   4923  C  CB  . PRO B  1 221 ? -10.940 45.486  29.270  1.00 43.00 ? 220 PRO B CB  1 
ATOM   4924  C  CG  . PRO B  1 221 ? -11.759 46.735  29.356  1.00 45.67 ? 220 PRO B CG  1 
ATOM   4925  C  CD  . PRO B  1 221 ? -12.865 46.527  28.353  1.00 46.03 ? 220 PRO B CD  1 
ATOM   4926  N  N   . LEU B  1 222 ? -13.321 44.278  31.072  1.00 41.98 ? 221 LEU B N   1 
ATOM   4927  C  CA  . LEU B  1 222 ? -13.766 43.687  32.343  1.00 43.05 ? 221 LEU B CA  1 
ATOM   4928  C  C   . LEU B  1 222 ? -14.594 42.412  32.143  1.00 42.29 ? 221 LEU B C   1 
ATOM   4929  O  O   . LEU B  1 222 ? -14.623 41.551  33.012  1.00 40.74 ? 221 LEU B O   1 
ATOM   4930  C  CB  . LEU B  1 222 ? -14.532 44.708  33.191  1.00 44.54 ? 221 LEU B CB  1 
ATOM   4931  C  CG  . LEU B  1 222 ? -13.781 45.985  33.616  1.00 46.50 ? 221 LEU B CG  1 
ATOM   4932  C  CD1 . LEU B  1 222 ? -14.639 46.812  34.565  1.00 47.74 ? 221 LEU B CD1 1 
ATOM   4933  C  CD2 . LEU B  1 222 ? -12.428 45.689  34.256  1.00 46.77 ? 221 LEU B CD2 1 
ATOM   4934  N  N   . LYS B  1 223 ? -15.250 42.293  30.995  1.00 42.56 ? 222 LYS B N   1 
ATOM   4935  C  CA  . LYS B  1 223 ? -16.027 41.102  30.636  1.00 41.83 ? 222 LYS B CA  1 
ATOM   4936  C  C   . LYS B  1 223 ? -15.085 39.950  30.289  1.00 38.92 ? 222 LYS B C   1 
ATOM   4937  O  O   . LYS B  1 223 ? -15.189 38.866  30.857  1.00 38.44 ? 222 LYS B O   1 
ATOM   4938  C  CB  . LYS B  1 223 ? -16.962 41.450  29.460  1.00 44.50 ? 222 LYS B CB  1 
ATOM   4939  C  CG  . LYS B  1 223 ? -17.879 40.373  28.898  1.00 46.46 ? 222 LYS B CG  1 
ATOM   4940  C  CD  . LYS B  1 223 ? -18.730 39.672  29.956  1.00 46.60 ? 222 LYS B CD  1 
ATOM   4941  C  CE  . LYS B  1 223 ? -19.598 40.560  30.805  1.00 48.91 ? 222 LYS B CE  1 
ATOM   4942  N  NZ  . LYS B  1 223 ? -20.922 40.875  30.229  1.00 49.70 ? 222 LYS B NZ  1 
ATOM   4943  N  N   . ILE B  1 224 ? -14.136 40.190  29.387  1.00 37.76 ? 223 ILE B N   1 
ATOM   4944  C  CA  . ILE B  1 224 ? -13.190 39.147  28.979  1.00 35.41 ? 223 ILE B CA  1 
ATOM   4945  C  C   . ILE B  1 224 ? -12.209 38.741  30.109  1.00 33.36 ? 223 ILE B C   1 
ATOM   4946  O  O   . ILE B  1 224 ? -11.701 37.615  30.133  1.00 29.81 ? 223 ILE B O   1 
ATOM   4947  C  CB  . ILE B  1 224 ? -12.401 39.559  27.709  1.00 38.38 ? 223 ILE B CB  1 
ATOM   4948  C  CG1 . ILE B  1 224 ? -11.708 38.358  27.078  1.00 40.51 ? 223 ILE B CG1 1 
ATOM   4949  C  CG2 . ILE B  1 224 ? -11.374 40.643  27.991  1.00 38.38 ? 223 ILE B CG2 1 
ATOM   4950  C  CD1 . ILE B  1 224 ? -12.692 37.310  26.582  1.00 42.53 ? 223 ILE B CD1 1 
ATOM   4951  N  N   . ARG B  1 225 ? -11.980 39.652  31.050  1.00 28.72 ? 224 ARG B N   1 
ATOM   4952  C  CA  . ARG B  1 225 ? -11.124 39.364  32.213  1.00 27.18 ? 224 ARG B CA  1 
ATOM   4953  C  C   . ARG B  1 225 ? -11.611 38.102  32.945  1.00 26.45 ? 224 ARG B C   1 
ATOM   4954  O  O   . ARG B  1 225 ? -10.813 37.342  33.480  1.00 25.29 ? 224 ARG B O   1 
ATOM   4955  C  CB  . ARG B  1 225 ? -11.134 40.571  33.152  1.00 27.01 ? 224 ARG B CB  1 
ATOM   4956  C  CG  . ARG B  1 225 ? -10.154 40.457  34.316  1.00 26.50 ? 224 ARG B CG  1 
ATOM   4957  C  CD  . ARG B  1 225 ? -10.233 41.681  35.216  1.00 26.33 ? 224 ARG B CD  1 
ATOM   4958  N  NE  . ARG B  1 225 ? -11.541 41.818  35.867  1.00 27.30 ? 224 ARG B NE  1 
ATOM   4959  C  CZ  . ARG B  1 225 ? -11.885 42.833  36.664  1.00 28.18 ? 224 ARG B CZ  1 
ATOM   4960  N  NH1 . ARG B  1 225 ? -11.027 43.813  36.954  1.00 27.41 ? 224 ARG B NH1 1 
ATOM   4961  N  NH2 . ARG B  1 225 ? -13.096 42.877  37.177  1.00 30.06 ? 224 ARG B NH2 1 
ATOM   4962  N  N   . GLU B  1 226 ? -12.929 37.895  32.962  1.00 26.99 ? 225 GLU B N   1 
ATOM   4963  C  CA  . GLU B  1 226 ? -13.530 36.725  33.613  1.00 28.77 ? 225 GLU B CA  1 
ATOM   4964  C  C   . GLU B  1 226 ? -12.937 35.426  33.062  1.00 27.94 ? 225 GLU B C   1 
ATOM   4965  O  O   . GLU B  1 226 ? -12.573 34.531  33.825  1.00 27.21 ? 225 GLU B O   1 
ATOM   4966  C  CB  . GLU B  1 226 ? -15.064 36.731  33.467  1.00 32.10 ? 225 GLU B CB  1 
ATOM   4967  C  CG  . GLU B  1 226 ? -15.768 37.955  34.064  1.00 36.35 ? 225 GLU B CG  1 
ATOM   4968  C  CD  . GLU B  1 226 ? -17.227 38.113  33.643  1.00 42.96 ? 225 GLU B CD  1 
ATOM   4969  O  OE1 . GLU B  1 226 ? -17.784 37.145  33.137  1.00 45.47 ? 225 GLU B OE1 1 
ATOM   4970  O  OE2 . GLU B  1 226 ? -17.855 39.183  33.848  1.00 46.13 ? 225 GLU B OE2 1 
ATOM   4971  N  N   . GLN B  1 227 ? -12.852 35.309  31.743  1.00 27.23 ? 226 GLN B N   1 
ATOM   4972  C  CA  . GLN B  1 227 ? -12.286 34.102  31.136  1.00 26.41 ? 226 GLN B CA  1 
ATOM   4973  C  C   . GLN B  1 227 ? -10.788 34.038  31.358  1.00 25.25 ? 226 GLN B C   1 
ATOM   4974  O  O   . GLN B  1 227 ? -10.259 32.979  31.685  1.00 23.24 ? 226 GLN B O   1 
ATOM   4975  C  CB  . GLN B  1 227 ? -12.565 34.042  29.635  1.00 27.74 ? 226 GLN B CB  1 
ATOM   4976  C  CG  . GLN B  1 227 ? -12.028 32.775  28.959  1.00 27.11 ? 226 GLN B CG  1 
ATOM   4977  C  CD  . GLN B  1 227 ? -10.544 32.767  28.608  1.00 27.45 ? 226 GLN B CD  1 
ATOM   4978  O  OE1 . GLN B  1 227 ? -9.871  31.732  28.722  1.00 27.71 ? 226 GLN B OE1 1 
ATOM   4979  N  NE2 . GLN B  1 227 ? -10.029 33.885  28.179  1.00 26.74 ? 226 GLN B NE2 1 
ATOM   4980  N  N   . GLN B  1 228 ? -10.118 35.179  31.220  1.00 23.17 ? 227 GLN B N   1 
ATOM   4981  C  CA  . GLN B  1 228 ? -8.652  35.213  31.335  1.00 22.34 ? 227 GLN B CA  1 
ATOM   4982  C  C   . GLN B  1 228 ? -8.183  34.783  32.734  1.00 20.22 ? 227 GLN B C   1 
ATOM   4983  O  O   . GLN B  1 228 ? -7.238  34.037  32.877  1.00 19.01 ? 227 GLN B O   1 
ATOM   4984  C  CB  . GLN B  1 228 ? -8.142  36.605  30.928  1.00 24.12 ? 227 GLN B CB  1 
ATOM   4985  C  CG  . GLN B  1 228 ? -8.378  36.884  29.442  1.00 26.89 ? 227 GLN B CG  1 
ATOM   4986  C  CD  . GLN B  1 228 ? -8.210  38.356  29.014  1.00 29.20 ? 227 GLN B CD  1 
ATOM   4987  O  OE1 . GLN B  1 228 ? -8.510  39.300  29.757  1.00 28.68 ? 227 GLN B OE1 1 
ATOM   4988  N  NE2 . GLN B  1 228 ? -7.803  38.544  27.759  1.00 30.43 ? 227 GLN B NE2 1 
ATOM   4989  N  N   . ARG B  1 229 ? -8.892  35.211  33.761  1.00 20.28 ? 228 ARG B N   1 
ATOM   4990  C  CA  . ARG B  1 229 ? -8.582  34.812  35.127  1.00 19.74 ? 228 ARG B CA  1 
ATOM   4991  C  C   . ARG B  1 229 ? -8.830  33.341  35.368  1.00 20.01 ? 228 ARG B C   1 
ATOM   4992  O  O   . ARG B  1 229 ? -8.098  32.712  36.128  1.00 20.10 ? 228 ARG B O   1 
ATOM   4993  C  CB  . ARG B  1 229 ? -9.421  35.612  36.126  1.00 20.94 ? 228 ARG B CB  1 
ATOM   4994  C  CG  . ARG B  1 229 ? -8.981  37.065  36.310  1.00 20.37 ? 228 ARG B CG  1 
ATOM   4995  C  CD  . ARG B  1 229 ? -9.941  37.808  37.211  1.00 21.65 ? 228 ARG B CD  1 
ATOM   4996  N  NE  . ARG B  1 229 ? -9.442  39.142  37.518  1.00 20.55 ? 228 ARG B NE  1 
ATOM   4997  C  CZ  . ARG B  1 229 ? -10.007 39.985  38.376  1.00 21.09 ? 228 ARG B CZ  1 
ATOM   4998  N  NH1 . ARG B  1 229 ? -11.132 39.664  39.008  1.00 21.23 ? 228 ARG B NH1 1 
ATOM   4999  N  NH2 . ARG B  1 229 ? -9.459  41.180  38.577  1.00 20.44 ? 228 ARG B NH2 1 
ATOM   5000  N  N   . SER B  1 230 ? -9.884  32.788  34.754  1.00 20.46 ? 229 SER B N   1 
ATOM   5001  C  CA  . SER B  1 230 ? -10.283 31.387  34.993  1.00 21.09 ? 229 SER B CA  1 
ATOM   5002  C  C   . SER B  1 230 ? -9.298  30.375  34.427  1.00 20.97 ? 229 SER B C   1 
ATOM   5003  O  O   . SER B  1 230 ? -9.227  29.208  34.895  1.00 22.06 ? 229 SER B O   1 
ATOM   5004  C  CB  . SER B  1 230 ? -11.686 31.101  34.434  1.00 21.62 ? 229 SER B CB  1 
ATOM   5005  O  OG  . SER B  1 230 ? -11.663 30.935  33.028  1.00 20.66 ? 229 SER B OG  1 
ATOM   5006  N  N   . ALA B  1 231 ? -8.512  30.820  33.449  1.00 20.57 ? 230 ALA B N   1 
ATOM   5007  C  CA  . ALA B  1 231 ? -7.504  29.973  32.838  1.00 21.01 ? 230 ALA B CA  1 
ATOM   5008  C  C   . ALA B  1 231 ? -6.232  29.924  33.698  1.00 20.76 ? 230 ALA B C   1 
ATOM   5009  O  O   . ALA B  1 231 ? -5.537  30.916  33.876  1.00 20.36 ? 230 ALA B O   1 
ATOM   5010  C  CB  . ALA B  1 231 ? -7.200  30.468  31.436  1.00 21.68 ? 230 ALA B CB  1 
ATOM   5011  N  N   . VAL B  1 232 ? -5.937  28.741  34.211  1.00 20.36 ? 231 VAL B N   1 
ATOM   5012  C  CA  . VAL B  1 232 ? -4.758  28.520  35.047  1.00 20.50 ? 231 VAL B CA  1 
ATOM   5013  C  C   . VAL B  1 232 ? -3.479  28.992  34.346  1.00 19.86 ? 231 VAL B C   1 
ATOM   5014  O  O   . VAL B  1 232 ? -2.546  29.493  34.984  1.00 18.94 ? 231 VAL B O   1 
ATOM   5015  C  CB  . VAL B  1 232 ? -4.612  27.037  35.451  1.00 21.12 ? 231 VAL B CB  1 
ATOM   5016  C  CG1 . VAL B  1 232 ? -3.448  26.853  36.414  1.00 20.65 ? 231 VAL B CG1 1 
ATOM   5017  C  CG2 . VAL B  1 232 ? -5.893  26.509  36.076  1.00 22.36 ? 231 VAL B CG2 1 
ATOM   5018  N  N   . SER B  1 233 ? -3.423  28.813  33.033  1.00 19.31 ? 232 SER B N   1 
ATOM   5019  C  CA  . SER B  1 233 ? -2.226  29.154  32.271  1.00 19.48 ? 232 SER B CA  1 
ATOM   5020  C  C   . SER B  1 233 ? -1.865  30.644  32.381  1.00 18.77 ? 232 SER B C   1 
ATOM   5021  O  O   . SER B  1 233 ? -0.698  31.007  32.271  1.00 19.66 ? 232 SER B O   1 
ATOM   5022  C  CB  . SER B  1 233 ? -2.380  28.747  30.792  1.00 19.25 ? 232 SER B CB  1 
ATOM   5023  O  OG  . SER B  1 233 ? -3.580  29.269  30.250  1.00 19.68 ? 232 SER B OG  1 
ATOM   5024  N  N   . THR B  1 234 ? -2.847  31.506  32.612  1.00 18.95 ? 233 THR B N   1 
ATOM   5025  C  CA  . THR B  1 234 ? -2.545  32.940  32.799  1.00 19.59 ? 233 THR B CA  1 
ATOM   5026  C  C   . THR B  1 234 ? -1.694  33.216  34.053  1.00 19.04 ? 233 THR B C   1 
ATOM   5027  O  O   . THR B  1 234 ? -0.633  33.849  33.966  1.00 19.14 ? 233 THR B O   1 
ATOM   5028  C  CB  . THR B  1 234 ? -3.813  33.774  32.878  1.00 20.05 ? 233 THR B CB  1 
ATOM   5029  O  OG1 . THR B  1 234 ? -4.640  33.468  31.749  1.00 20.00 ? 233 THR B OG1 1 
ATOM   5030  C  CG2 . THR B  1 234 ? -3.462  35.240  32.873  1.00 21.29 ? 233 THR B CG2 1 
ATOM   5031  N  N   . SER B  1 235 ? -2.107  32.654  35.190  1.00 18.40 ? 234 SER B N   1 
ATOM   5032  C  CA  . SER B  1 235 ? -1.337  32.811  36.434  1.00 17.75 ? 234 SER B CA  1 
ATOM   5033  C  C   . SER B  1 235 ? 0.008   32.108  36.380  1.00 17.66 ? 234 SER B C   1 
ATOM   5034  O  O   . SER B  1 235 ? 0.971   32.551  36.994  1.00 16.69 ? 234 SER B O   1 
ATOM   5035  C  CB  . SER B  1 235 ? -2.165  32.308  37.614  1.00 18.89 ? 234 SER B CB  1 
ATOM   5036  O  OG  . SER B  1 235 ? -3.265  33.180  37.792  1.00 20.88 ? 234 SER B OG  1 
ATOM   5037  N  N   . TRP B  1 236 ? 0.068   30.986  35.661  1.00 17.53 ? 235 TRP B N   1 
ATOM   5038  C  CA  . TRP B  1 236 ? 1.326   30.257  35.471  1.00 16.53 ? 235 TRP B CA  1 
ATOM   5039  C  C   . TRP B  1 236 ? 2.415   31.138  34.835  1.00 17.25 ? 235 TRP B C   1 
ATOM   5040  O  O   . TRP B  1 236 ? 3.606   30.941  35.078  1.00 18.56 ? 235 TRP B O   1 
ATOM   5041  C  CB  . TRP B  1 236 ? 1.030   29.023  34.582  1.00 16.89 ? 235 TRP B CB  1 
ATOM   5042  C  CG  . TRP B  1 236 ? 2.200   28.133  34.270  1.00 16.64 ? 235 TRP B CG  1 
ATOM   5043  C  CD1 . TRP B  1 236 ? 3.192   27.759  35.118  1.00 17.60 ? 235 TRP B CD1 1 
ATOM   5044  C  CD2 . TRP B  1 236 ? 2.489   27.514  33.021  1.00 17.18 ? 235 TRP B CD2 1 
ATOM   5045  N  NE1 . TRP B  1 236 ? 4.084   26.918  34.480  1.00 17.83 ? 235 TRP B NE1 1 
ATOM   5046  C  CE2 . TRP B  1 236 ? 3.691   26.780  33.179  1.00 18.71 ? 235 TRP B CE2 1 
ATOM   5047  C  CE3 . TRP B  1 236 ? 1.879   27.527  31.781  1.00 18.34 ? 235 TRP B CE3 1 
ATOM   5048  C  CZ2 . TRP B  1 236 ? 4.256   26.043  32.143  1.00 18.53 ? 235 TRP B CZ2 1 
ATOM   5049  C  CZ3 . TRP B  1 236 ? 2.447   26.807  30.755  1.00 18.22 ? 235 TRP B CZ3 1 
ATOM   5050  C  CH2 . TRP B  1 236 ? 3.612   26.058  30.950  1.00 18.60 ? 235 TRP B CH2 1 
ATOM   5051  N  N   . LEU B  1 237 ? 2.008   32.086  34.000  1.00 17.61 ? 236 LEU B N   1 
ATOM   5052  C  CA  . LEU B  1 237 ? 2.957   32.933  33.273  1.00 19.15 ? 236 LEU B CA  1 
ATOM   5053  C  C   . LEU B  1 237 ? 3.249   34.292  33.905  1.00 18.36 ? 236 LEU B C   1 
ATOM   5054  O  O   . LEU B  1 237 ? 3.848   35.160  33.257  1.00 17.38 ? 236 LEU B O   1 
ATOM   5055  C  CB  . LEU B  1 237 ? 2.507   33.067  31.817  1.00 21.47 ? 236 LEU B CB  1 
ATOM   5056  C  CG  . LEU B  1 237 ? 2.598   31.725  31.055  1.00 25.41 ? 236 LEU B CG  1 
ATOM   5057  C  CD1 . LEU B  1 237 ? 2.192   31.986  29.635  1.00 28.17 ? 236 LEU B CD1 1 
ATOM   5058  C  CD2 . LEU B  1 237 ? 3.989   31.111  31.112  1.00 28.24 ? 236 LEU B CD2 1 
ATOM   5059  N  N   . LEU B  1 238 ? 2.865   34.489  35.171  1.00 17.12 ? 237 LEU B N   1 
ATOM   5060  C  CA  . LEU B  1 238 ? 3.343   35.687  35.900  1.00 17.34 ? 237 LEU B CA  1 
ATOM   5061  C  C   . LEU B  1 238 ? 4.881   35.616  35.994  1.00 16.63 ? 237 LEU B C   1 
ATOM   5062  O  O   . LEU B  1 238 ? 5.443   34.506  36.083  1.00 17.30 ? 237 LEU B O   1 
ATOM   5063  C  CB  . LEU B  1 238 ? 2.766   35.779  37.309  1.00 17.27 ? 237 LEU B CB  1 
ATOM   5064  C  CG  . LEU B  1 238 ? 1.286   36.148  37.406  1.00 17.75 ? 237 LEU B CG  1 
ATOM   5065  C  CD1 . LEU B  1 238 ? 0.752   35.766  38.785  1.00 19.43 ? 237 LEU B CD1 1 
ATOM   5066  C  CD2 . LEU B  1 238 ? 1.140   37.643  37.182  1.00 18.56 ? 237 LEU B CD2 1 
ATOM   5067  N  N   . PRO B  1 239 ? 5.551   36.786  36.019  1.00 16.12 ? 238 PRO B N   1 
ATOM   5068  C  CA  . PRO B  1 239 ? 7.000   36.858  36.181  1.00 16.75 ? 238 PRO B CA  1 
ATOM   5069  C  C   . PRO B  1 239 ? 7.596   35.991  37.293  1.00 17.33 ? 238 PRO B C   1 
ATOM   5070  O  O   . PRO B  1 239 ? 7.058   35.926  38.400  1.00 18.07 ? 238 PRO B O   1 
ATOM   5071  C  CB  . PRO B  1 239 ? 7.241   38.336  36.466  1.00 16.44 ? 238 PRO B CB  1 
ATOM   5072  C  CG  . PRO B  1 239 ? 6.181   39.009  35.698  1.00 16.40 ? 238 PRO B CG  1 
ATOM   5073  C  CD  . PRO B  1 239 ? 4.969   38.131  35.867  1.00 16.06 ? 238 PRO B CD  1 
ATOM   5074  N  N   . TYR B  1 240 ? 8.712   35.331  36.970  1.00 18.35 ? 239 TYR B N   1 
ATOM   5075  C  CA  . TYR B  1 240 ? 9.456   34.482  37.894  1.00 19.06 ? 239 TYR B CA  1 
ATOM   5076  C  C   . TYR B  1 240 ? 10.759  35.123  38.346  1.00 19.54 ? 239 TYR B C   1 
ATOM   5077  O  O   . TYR B  1 240 ? 11.368  35.886  37.586  1.00 19.21 ? 239 TYR B O   1 
ATOM   5078  C  CB  . TYR B  1 240 ? 9.797   33.156  37.227  1.00 19.91 ? 239 TYR B CB  1 
ATOM   5079  C  CG  . TYR B  1 240 ? 8.628   32.232  37.055  1.00 19.58 ? 239 TYR B CG  1 
ATOM   5080  C  CD1 . TYR B  1 240 ? 7.746   32.372  35.995  1.00 19.29 ? 239 TYR B CD1 1 
ATOM   5081  C  CD2 . TYR B  1 240 ? 8.427   31.177  37.952  1.00 20.74 ? 239 TYR B CD2 1 
ATOM   5082  C  CE1 . TYR B  1 240 ? 6.652   31.505  35.834  1.00 19.54 ? 239 TYR B CE1 1 
ATOM   5083  C  CE2 . TYR B  1 240 ? 7.346   30.312  37.802  1.00 20.17 ? 239 TYR B CE2 1 
ATOM   5084  C  CZ  . TYR B  1 240 ? 6.469   30.473  36.739  1.00 20.07 ? 239 TYR B CZ  1 
ATOM   5085  O  OH  . TYR B  1 240 ? 5.382   29.632  36.624  1.00 20.83 ? 239 TYR B OH  1 
ATOM   5086  N  N   . ASN B  1 241 ? 11.189  34.797  39.572  1.00 21.42 ? 240 ASN B N   1 
ATOM   5087  C  CA  . ASN B  1 241 ? 12.448  35.354  40.122  1.00 23.89 ? 240 ASN B CA  1 
ATOM   5088  C  C   . ASN B  1 241 ? 13.725  34.829  39.508  1.00 25.97 ? 240 ASN B C   1 
ATOM   5089  O  O   . ASN B  1 241 ? 14.793  35.327  39.837  1.00 27.29 ? 240 ASN B O   1 
ATOM   5090  C  CB  . ASN B  1 241 ? 12.553  35.236  41.649  1.00 26.97 ? 240 ASN B CB  1 
ATOM   5091  C  CG  . ASN B  1 241 ? 12.369  33.820  42.139  1.00 29.00 ? 240 ASN B CG  1 
ATOM   5092  O  OD1 . ASN B  1 241 ? 12.562  32.850  41.397  1.00 27.29 ? 240 ASN B OD1 1 
ATOM   5093  N  ND2 . ASN B  1 241 ? 11.983  33.699  43.415  1.00 31.44 ? 240 ASN B ND2 1 
ATOM   5094  N  N   . TYR B  1 242 ? 13.669  33.829  38.638  1.00 24.58 ? 241 TYR B N   1 
ATOM   5095  C  CA  . TYR B  1 242 ? 14.910  33.422  37.943  1.00 27.94 ? 241 TYR B CA  1 
ATOM   5096  C  C   . TYR B  1 242 ? 15.231  34.297  36.723  1.00 29.21 ? 241 TYR B C   1 
ATOM   5097  O  O   . TYR B  1 242 ? 16.316  34.196  36.152  1.00 29.12 ? 241 TYR B O   1 
ATOM   5098  C  CB  . TYR B  1 242 ? 14.913  31.934  37.590  1.00 27.74 ? 241 TYR B CB  1 
ATOM   5099  C  CG  . TYR B  1 242 ? 13.739  31.432  36.804  1.00 28.57 ? 241 TYR B CG  1 
ATOM   5100  C  CD1 . TYR B  1 242 ? 13.671  31.627  35.412  1.00 29.56 ? 241 TYR B CD1 1 
ATOM   5101  C  CD2 . TYR B  1 242 ? 12.722  30.720  37.418  1.00 29.64 ? 241 TYR B CD2 1 
ATOM   5102  C  CE1 . TYR B  1 242 ? 12.602  31.145  34.661  1.00 29.87 ? 241 TYR B CE1 1 
ATOM   5103  C  CE2 . TYR B  1 242 ? 11.653  30.230  36.667  1.00 30.10 ? 241 TYR B CE2 1 
ATOM   5104  C  CZ  . TYR B  1 242 ? 11.594  30.454  35.303  1.00 29.26 ? 241 TYR B CZ  1 
ATOM   5105  O  OH  . TYR B  1 242 ? 10.552  29.984  34.544  1.00 31.84 ? 241 TYR B OH  1 
ATOM   5106  N  N   . THR B  1 243 ? 14.279  35.149  36.337  1.00 27.04 ? 242 THR B N   1 
ATOM   5107  C  CA  . THR B  1 243 ? 14.439  36.083  35.248  1.00 27.71 ? 242 THR B CA  1 
ATOM   5108  C  C   . THR B  1 243 ? 14.433  37.511  35.740  1.00 27.35 ? 242 THR B C   1 
ATOM   5109  O  O   . THR B  1 243 ? 15.221  38.328  35.284  1.00 28.62 ? 242 THR B O   1 
ATOM   5110  C  CB  . THR B  1 243 ? 13.293  35.885  34.220  1.00 28.95 ? 242 THR B CB  1 
ATOM   5111  O  OG1 . THR B  1 243 ? 13.481  34.651  33.536  1.00 31.41 ? 242 THR B OG1 1 
ATOM   5112  C  CG2 . THR B  1 243 ? 13.268  36.989  33.172  1.00 30.49 ? 242 THR B CG2 1 
ATOM   5113  N  N   A TRP B  1 244 ? 13.531  37.818  36.668  0.50 23.98 ? 243 TRP B N   1 
ATOM   5114  N  N   B TRP B  1 244 ? 13.543  37.826  36.673  0.50 26.77 ? 243 TRP B N   1 
ATOM   5115  C  CA  A TRP B  1 244 ? 13.305  39.171  37.110  0.50 22.52 ? 243 TRP B CA  1 
ATOM   5116  C  CA  B TRP B  1 244 ? 13.394  39.194  37.122  0.50 26.91 ? 243 TRP B CA  1 
ATOM   5117  C  C   A TRP B  1 244 ? 13.791  39.383  38.542  0.50 23.40 ? 243 TRP B C   1 
ATOM   5118  C  C   B TRP B  1 244 ? 13.811  39.384  38.550  0.50 25.83 ? 243 TRP B C   1 
ATOM   5119  O  O   A TRP B  1 244 ? 13.737  38.464  39.361  0.50 22.90 ? 243 TRP B O   1 
ATOM   5120  O  O   B TRP B  1 244 ? 13.734  38.468  39.364  0.50 25.08 ? 243 TRP B O   1 
ATOM   5121  C  CB  A TRP B  1 244 ? 11.797  39.430  37.058  0.50 20.71 ? 243 TRP B CB  1 
ATOM   5122  C  CB  B TRP B  1 244 ? 11.966  39.621  36.957  0.50 28.32 ? 243 TRP B CB  1 
ATOM   5123  C  CG  A TRP B  1 244 ? 11.110  39.200  35.669  0.50 18.42 ? 243 TRP B CG  1 
ATOM   5124  C  CG  B TRP B  1 244 ? 11.706  40.275  35.702  0.50 29.58 ? 243 TRP B CG  1 
ATOM   5125  C  CD1 A TRP B  1 244 ? 10.642  38.002  35.161  0.50 17.54 ? 243 TRP B CD1 1 
ATOM   5126  C  CD1 B TRP B  1 244 ? 12.131  41.525  35.294  0.50 30.64 ? 243 TRP B CD1 1 
ATOM   5127  C  CD2 A TRP B  1 244 ? 10.783  40.192  34.691  0.50 17.60 ? 243 TRP B CD2 1 
ATOM   5128  C  CD2 B TRP B  1 244 ? 10.899  39.770  34.686  0.50 28.77 ? 243 TRP B CD2 1 
ATOM   5129  N  NE1 A TRP B  1 244 ? 10.065  38.200  33.918  0.50 16.89 ? 243 TRP B NE1 1 
ATOM   5130  N  NE1 B TRP B  1 244 ? 11.631  41.796  34.039  0.50 29.95 ? 243 TRP B NE1 1 
ATOM   5131  C  CE2 A TRP B  1 244 ? 10.128  39.536  33.615  0.50 17.30 ? 243 TRP B CE2 1 
ATOM   5132  C  CE2 B TRP B  1 244 ? 10.868  40.724  33.650  0.50 29.81 ? 243 TRP B CE2 1 
ATOM   5133  C  CE3 A TRP B  1 244 ? 10.983  41.576  34.613  0.50 18.23 ? 243 TRP B CE3 1 
ATOM   5134  C  CE3 B TRP B  1 244 ? 10.207  38.575  34.530  0.50 29.70 ? 243 TRP B CE3 1 
ATOM   5135  C  CZ2 A TRP B  1 244 ? 9.689   40.220  32.488  0.50 17.01 ? 243 TRP B CZ2 1 
ATOM   5136  C  CZ2 B TRP B  1 244 ? 10.165  40.509  32.494  0.50 29.31 ? 243 TRP B CZ2 1 
ATOM   5137  C  CZ3 A TRP B  1 244 ? 10.557  42.245  33.481  0.50 17.96 ? 243 TRP B CZ3 1 
ATOM   5138  C  CZ3 B TRP B  1 244 ? 9.520   38.378  33.411  0.50 28.59 ? 243 TRP B CZ3 1 
ATOM   5139  C  CH2 A TRP B  1 244 ? 9.912   41.572  32.441  0.50 17.81 ? 243 TRP B CH2 1 
ATOM   5140  C  CH2 B TRP B  1 244 ? 9.490   39.326  32.401  0.50 29.46 ? 243 TRP B CH2 1 
ATOM   5141  N  N   . SER B  1 245 ? 14.257  40.593  38.840  1.00 24.92 ? 244 SER B N   1 
ATOM   5142  C  CA  . SER B  1 245 ? 14.615  40.977  40.188  1.00 26.69 ? 244 SER B CA  1 
ATOM   5143  C  C   . SER B  1 245 ? 13.387  40.927  41.113  1.00 26.85 ? 244 SER B C   1 
ATOM   5144  O  O   . SER B  1 245 ? 12.307  41.399  40.734  1.00 23.83 ? 244 SER B O   1 
ATOM   5145  C  CB  . SER B  1 245 ? 15.145  42.389  40.195  1.00 28.23 ? 244 SER B CB  1 
ATOM   5146  O  OG  . SER B  1 245 ? 15.299  42.818  41.516  1.00 29.56 ? 244 SER B OG  1 
ATOM   5147  N  N   . PRO B  1 246 ? 13.551  40.365  42.320  1.00 29.74 ? 245 PRO B N   1 
ATOM   5148  C  CA  . PRO B  1 246 ? 12.402  40.334  43.230  1.00 30.81 ? 245 PRO B CA  1 
ATOM   5149  C  C   . PRO B  1 246 ? 11.953  41.734  43.675  1.00 31.79 ? 245 PRO B C   1 
ATOM   5150  O  O   . PRO B  1 246 ? 10.861  41.854  44.213  1.00 32.90 ? 245 PRO B O   1 
ATOM   5151  C  CB  . PRO B  1 246 ? 12.920  39.503  44.419  1.00 32.89 ? 245 PRO B CB  1 
ATOM   5152  C  CG  . PRO B  1 246 ? 13.950  38.592  43.795  1.00 34.28 ? 245 PRO B CG  1 
ATOM   5153  C  CD  . PRO B  1 246 ? 14.649  39.510  42.811  1.00 32.07 ? 245 PRO B CD  1 
ATOM   5154  N  N   . GLU B  1 247 ? 12.782  42.753  43.451  1.00 29.06 ? 246 GLU B N   1 
ATOM   5155  C  CA  . GLU B  1 247 ? 12.449  44.119  43.779  1.00 31.77 ? 246 GLU B CA  1 
ATOM   5156  C  C   . GLU B  1 247 ? 11.886  44.951  42.598  1.00 27.55 ? 246 GLU B C   1 
ATOM   5157  O  O   . GLU B  1 247 ? 11.490  46.089  42.803  1.00 26.18 ? 246 GLU B O   1 
ATOM   5158  C  CB  . GLU B  1 247 ? 13.672  44.856  44.359  1.00 36.22 ? 246 GLU B CB  1 
ATOM   5159  C  CG  . GLU B  1 247 ? 14.337  44.237  45.608  1.00 42.82 ? 246 GLU B CG  1 
ATOM   5160  C  CD  . GLU B  1 247 ? 13.351  43.578  46.543  1.00 47.96 ? 246 GLU B CD  1 
ATOM   5161  O  OE1 . GLU B  1 247 ? 12.465  44.281  47.101  1.00 53.45 ? 246 GLU B OE1 1 
ATOM   5162  O  OE2 . GLU B  1 247 ? 13.479  42.342  46.711  1.00 52.38 ? 246 GLU B OE2 1 
ATOM   5163  N  N   . LYS B  1 248 ? 11.801  44.391  41.396  1.00 25.36 ? 247 LYS B N   1 
ATOM   5164  C  CA  . LYS B  1 248 ? 11.184  45.122  40.295  1.00 25.00 ? 247 LYS B CA  1 
ATOM   5165  C  C   . LYS B  1 248 ? 9.670   45.301  40.542  1.00 23.05 ? 247 LYS B C   1 
ATOM   5166  O  O   . LYS B  1 248 ? 8.961   44.337  40.811  1.00 20.83 ? 247 LYS B O   1 
ATOM   5167  C  CB  . LYS B  1 248 ? 11.371  44.419  38.960  1.00 26.80 ? 247 LYS B CB  1 
ATOM   5168  C  CG  . LYS B  1 248 ? 10.596  45.175  37.890  1.00 27.59 ? 247 LYS B CG  1 
ATOM   5169  C  CD  . LYS B  1 248 ? 10.923  44.803  36.477  1.00 31.62 ? 247 LYS B CD  1 
ATOM   5170  C  CE  . LYS B  1 248 ? 10.030  45.586  35.521  1.00 31.49 ? 247 LYS B CE  1 
ATOM   5171  N  NZ  . LYS B  1 248 ? 10.403  47.021  35.497  1.00 33.23 ? 247 LYS B NZ  1 
ATOM   5172  N  N   . VAL B  1 249 ? 9.196   46.529  40.442  1.00 22.13 ? 248 VAL B N   1 
ATOM   5173  C  CA  . VAL B  1 249 ? 7.770   46.829  40.616  1.00 22.28 ? 248 VAL B CA  1 
ATOM   5174  C  C   . VAL B  1 249 ? 7.088   46.665  39.268  1.00 22.07 ? 248 VAL B C   1 
ATOM   5175  O  O   . VAL B  1 249 ? 7.459   47.342  38.309  1.00 22.39 ? 248 VAL B O   1 
ATOM   5176  C  CB  . VAL B  1 249 ? 7.558   48.250  41.157  1.00 23.43 ? 248 VAL B CB  1 
ATOM   5177  C  CG1 . VAL B  1 249 ? 6.076   48.584  41.236  1.00 23.79 ? 248 VAL B CG1 1 
ATOM   5178  C  CG2 . VAL B  1 249 ? 8.210   48.390  42.513  1.00 24.77 ? 248 VAL B CG2 1 
ATOM   5179  N  N   . PHE B  1 250 ? 6.141   45.721  39.184  1.00 20.77 ? 249 PHE B N   1 
ATOM   5180  C  CA  . PHE B  1 250 ? 5.366   45.497  37.955  1.00 20.03 ? 249 PHE B CA  1 
ATOM   5181  C  C   . PHE B  1 250 ? 4.088   46.306  37.914  1.00 20.23 ? 249 PHE B C   1 
ATOM   5182  O  O   . PHE B  1 250 ? 3.632   46.712  36.832  1.00 20.19 ? 249 PHE B O   1 
ATOM   5183  C  CB  . PHE B  1 250 ? 5.000   44.037  37.836  1.00 19.83 ? 249 PHE B CB  1 
ATOM   5184  C  CG  . PHE B  1 250 ? 6.170   43.170  37.497  1.00 20.43 ? 249 PHE B CG  1 
ATOM   5185  C  CD1 . PHE B  1 250 ? 6.705   43.202  36.217  1.00 19.97 ? 249 PHE B CD1 1 
ATOM   5186  C  CD2 . PHE B  1 250 ? 6.747   42.350  38.456  1.00 20.70 ? 249 PHE B CD2 1 
ATOM   5187  C  CE1 . PHE B  1 250 ? 7.766   42.379  35.880  1.00 20.15 ? 249 PHE B CE1 1 
ATOM   5188  C  CE2 . PHE B  1 250 ? 7.823   41.546  38.133  1.00 20.65 ? 249 PHE B CE2 1 
ATOM   5189  C  CZ  . PHE B  1 250 ? 8.338   41.577  36.839  1.00 19.72 ? 249 PHE B CZ  1 
ATOM   5190  N  N   . VAL B  1 251 ? 3.512   46.549  39.086  1.00 19.59 ? 250 VAL B N   1 
ATOM   5191  C  CA  . VAL B  1 251 ? 2.273   47.317  39.198  1.00 19.67 ? 250 VAL B CA  1 
ATOM   5192  C  C   . VAL B  1 251 ? 2.427   48.329  40.320  1.00 20.40 ? 250 VAL B C   1 
ATOM   5193  O  O   . VAL B  1 251 ? 2.722   47.991  41.472  1.00 20.22 ? 250 VAL B O   1 
ATOM   5194  C  CB  . VAL B  1 251 ? 1.062   46.418  39.475  1.00 19.86 ? 250 VAL B CB  1 
ATOM   5195  C  CG1 . VAL B  1 251 ? -0.196  47.236  39.742  1.00 19.97 ? 250 VAL B CG1 1 
ATOM   5196  C  CG2 . VAL B  1 251 ? 0.820   45.481  38.307  1.00 20.66 ? 250 VAL B CG2 1 
ATOM   5197  N  N   . GLN B  1 252 ? 2.242   49.594  39.979  1.00 21.22 ? 251 GLN B N   1 
ATOM   5198  C  CA  . GLN B  1 252 ? 2.236   50.657  40.970  1.00 22.27 ? 251 GLN B CA  1 
ATOM   5199  C  C   . GLN B  1 252 ? 0.877   51.352  40.987  1.00 22.85 ? 251 GLN B C   1 
ATOM   5200  O  O   . GLN B  1 252 ? 0.240   51.537  39.949  1.00 22.39 ? 251 GLN B O   1 
ATOM   5201  C  CB  . GLN B  1 252 ? 3.408   51.611  40.715  1.00 24.66 ? 251 GLN B CB  1 
ATOM   5202  C  CG  . GLN B  1 252 ? 3.475   52.819  41.625  1.00 27.98 ? 251 GLN B CG  1 
ATOM   5203  C  CD  . GLN B  1 252 ? 4.726   53.631  41.345  1.00 31.39 ? 251 GLN B CD  1 
ATOM   5204  O  OE1 . GLN B  1 252 ? 4.944   54.112  40.241  1.00 34.46 ? 251 GLN B OE1 1 
ATOM   5205  N  NE2 . GLN B  1 252 ? 5.576   53.735  42.328  1.00 34.02 ? 251 GLN B NE2 1 
ATOM   5206  N  N   . THR B  1 253 ? 0.405   51.677  42.194  1.00 23.50 ? 252 THR B N   1 
ATOM   5207  C  CA  . THR B  1 253 ? -0.847  52.405  42.385  1.00 24.97 ? 252 THR B CA  1 
ATOM   5208  C  C   . THR B  1 253 ? -0.519  53.539  43.365  1.00 27.16 ? 252 THR B C   1 
ATOM   5209  O  O   . THR B  1 253 ? 0.583   53.570  43.901  1.00 27.39 ? 252 THR B O   1 
ATOM   5210  C  CB  . THR B  1 253 ? -1.974  51.501  42.947  1.00 26.53 ? 252 THR B CB  1 
ATOM   5211  O  OG1 . THR B  1 253 ? -1.850  51.425  44.368  1.00 27.69 ? 252 THR B OG1 1 
ATOM   5212  C  CG2 . THR B  1 253 ? -1.921  50.070  42.385  1.00 25.87 ? 252 THR B CG2 1 
ATOM   5213  N  N   . PRO B  1 254 ? -1.465  54.454  43.622  1.00 28.63 ? 253 PRO B N   1 
ATOM   5214  C  CA  . PRO B  1 254 ? -1.198  55.510  44.598  1.00 31.81 ? 253 PRO B CA  1 
ATOM   5215  C  C   . PRO B  1 254 ? -0.903  55.022  46.018  1.00 33.23 ? 253 PRO B C   1 
ATOM   5216  O  O   . PRO B  1 254 ? -0.241  55.733  46.769  1.00 35.50 ? 253 PRO B O   1 
ATOM   5217  C  CB  . PRO B  1 254 ? -2.483  56.361  44.566  1.00 32.40 ? 253 PRO B CB  1 
ATOM   5218  C  CG  . PRO B  1 254 ? -3.169  56.003  43.277  1.00 32.36 ? 253 PRO B CG  1 
ATOM   5219  C  CD  . PRO B  1 254 ? -2.833  54.549  43.079  1.00 30.38 ? 253 PRO B CD  1 
ATOM   5220  N  N   . THR B  1 255 ? -1.362  53.823  46.379  1.00 33.03 ? 254 THR B N   1 
ATOM   5221  C  CA  . THR B  1 255 ? -1.245  53.349  47.758  1.00 33.24 ? 254 THR B CA  1 
ATOM   5222  C  C   . THR B  1 255 ? -0.447  52.072  47.949  1.00 32.26 ? 254 THR B C   1 
ATOM   5223  O  O   . THR B  1 255 ? -0.222  51.683  49.086  1.00 31.67 ? 254 THR B O   1 
ATOM   5224  C  CB  . THR B  1 255 ? -2.633  53.088  48.352  1.00 35.73 ? 254 THR B CB  1 
ATOM   5225  O  OG1 . THR B  1 255 ? -3.359  52.193  47.499  1.00 35.25 ? 254 THR B OG1 1 
ATOM   5226  C  CG2 . THR B  1 255 ? -3.409  54.408  48.492  1.00 38.42 ? 254 THR B CG2 1 
ATOM   5227  N  N   . ILE B  1 256 ? -0.030  51.405  46.871  1.00 27.43 ? 255 ILE B N   1 
ATOM   5228  C  CA  . ILE B  1 256 ? 0.653   50.145  47.009  1.00 26.82 ? 255 ILE B CA  1 
ATOM   5229  C  C   . ILE B  1 256 ? 1.432   49.791  45.747  1.00 26.18 ? 255 ILE B C   1 
ATOM   5230  O  O   . ILE B  1 256 ? 1.014   50.138  44.636  1.00 25.86 ? 255 ILE B O   1 
ATOM   5231  C  CB  . ILE B  1 256 ? -0.375  49.044  47.417  1.00 27.92 ? 255 ILE B CB  1 
ATOM   5232  C  CG1 . ILE B  1 256 ? 0.306   47.771  47.838  1.00 29.36 ? 255 ILE B CG1 1 
ATOM   5233  C  CG2 . ILE B  1 256 ? -1.369  48.767  46.290  1.00 28.97 ? 255 ILE B CG2 1 
ATOM   5234  C  CD1 . ILE B  1 256 ? -0.667  46.767  48.432  1.00 30.27 ? 255 ILE B CD1 1 
ATOM   5235  N  N   A ASN B  1 257 ? 2.565   49.115  45.940  0.50 25.65 ? 256 ASN B N   1 
ATOM   5236  N  N   B ASN B  1 257 ? 2.550   49.099  45.939  0.50 25.59 ? 256 ASN B N   1 
ATOM   5237  C  CA  A ASN B  1 257 ? 3.369   48.568  44.864  0.50 25.18 ? 256 ASN B CA  1 
ATOM   5238  C  CA  B ASN B  1 257 ? 3.355   48.560  44.869  0.50 25.07 ? 256 ASN B CA  1 
ATOM   5239  C  C   A ASN B  1 257 ? 3.243   47.048  44.873  0.50 24.24 ? 256 ASN B C   1 
ATOM   5240  C  C   B ASN B  1 257 ? 3.259   47.049  44.875  0.50 24.20 ? 256 ASN B C   1 
ATOM   5241  O  O   A ASN B  1 257 ? 3.056   46.456  45.938  0.50 25.88 ? 256 ASN B O   1 
ATOM   5242  O  O   B ASN B  1 257 ? 3.063   46.472  45.937  0.50 25.89 ? 256 ASN B O   1 
ATOM   5243  C  CB  A ASN B  1 257 ? 4.841   48.864  45.100  0.50 25.77 ? 256 ASN B CB  1 
ATOM   5244  C  CB  B ASN B  1 257 ? 4.788   48.978  45.108  0.50 25.61 ? 256 ASN B CB  1 
ATOM   5245  C  CG  A ASN B  1 257 ? 5.275   50.233  44.666  0.50 26.64 ? 256 ASN B CG  1 
ATOM   5246  C  CG  B ASN B  1 257 ? 4.970   50.472  44.929  0.50 26.01 ? 256 ASN B CG  1 
ATOM   5247  O  OD1 A ASN B  1 257 ? 4.544   50.998  44.001  0.50 27.52 ? 256 ASN B OD1 1 
ATOM   5248  O  OD1 B ASN B  1 257 ? 4.515   51.023  43.935  0.50 27.40 ? 256 ASN B OD1 1 
ATOM   5249  N  ND2 A ASN B  1 257 ? 6.527   50.534  45.045  0.50 27.68 ? 256 ASN B ND2 1 
ATOM   5250  N  ND2 B ASN B  1 257 ? 5.615   51.129  45.893  0.50 27.60 ? 256 ASN B ND2 1 
ATOM   5251  N  N   . TYR B  1 258 ? 3.365   46.419  43.709  1.00 21.29 ? 257 TYR B N   1 
ATOM   5252  C  CA  . TYR B  1 258 ? 3.434   44.969  43.623  1.00 19.64 ? 257 TYR B CA  1 
ATOM   5253  C  C   . TYR B  1 258 ? 4.657   44.537  42.817  1.00 19.31 ? 257 TYR B C   1 
ATOM   5254  O  O   . TYR B  1 258 ? 4.799   44.882  41.625  1.00 18.93 ? 257 TYR B O   1 
ATOM   5255  C  CB  . TYR B  1 258 ? 2.182   44.364  42.994  1.00 19.06 ? 257 TYR B CB  1 
ATOM   5256  C  CG  . TYR B  1 258 ? 0.874   44.744  43.658  1.00 18.62 ? 257 TYR B CG  1 
ATOM   5257  C  CD1 . TYR B  1 258 ? 0.394   44.055  44.752  1.00 18.50 ? 257 TYR B CD1 1 
ATOM   5258  C  CD2 . TYR B  1 258 ? 0.122   45.795  43.182  1.00 19.52 ? 257 TYR B CD2 1 
ATOM   5259  C  CE1 . TYR B  1 258 ? -0.803  44.402  45.352  1.00 18.81 ? 257 TYR B CE1 1 
ATOM   5260  C  CE2 . TYR B  1 258 ? -1.080  46.157  43.769  1.00 19.61 ? 257 TYR B CE2 1 
ATOM   5261  C  CZ  . TYR B  1 258 ? -1.536  45.465  44.858  1.00 19.46 ? 257 TYR B CZ  1 
ATOM   5262  O  OH  . TYR B  1 258 ? -2.739  45.842  45.425  1.00 21.01 ? 257 TYR B OH  1 
ATOM   5263  N  N   . THR B  1 259 ? 5.514   43.769  43.500  1.00 19.06 ? 258 THR B N   1 
ATOM   5264  C  CA  . THR B  1 259 ? 6.626   43.033  42.915  1.00 18.04 ? 258 THR B CA  1 
ATOM   5265  C  C   . THR B  1 259 ? 6.255   41.555  42.816  1.00 17.41 ? 258 THR B C   1 
ATOM   5266  O  O   . THR B  1 259 ? 5.178   41.135  43.239  1.00 17.40 ? 258 THR B O   1 
ATOM   5267  C  CB  . THR B  1 259 ? 7.901   43.148  43.784  1.00 18.97 ? 258 THR B CB  1 
ATOM   5268  O  OG1 . THR B  1 259 ? 7.749   42.375  44.991  1.00 19.27 ? 258 THR B OG1 1 
ATOM   5269  C  CG2 . THR B  1 259 ? 8.198   44.594  44.172  1.00 19.64 ? 258 THR B CG2 1 
ATOM   5270  N  N   . LEU B  1 260 ? 7.143   40.737  42.283  1.00 17.50 ? 259 LEU B N   1 
ATOM   5271  C  CA  . LEU B  1 260 ? 6.866   39.293  42.213  1.00 18.11 ? 259 LEU B CA  1 
ATOM   5272  C  C   . LEU B  1 260 ? 6.881   38.608  43.583  1.00 17.52 ? 259 LEU B C   1 
ATOM   5273  O  O   . LEU B  1 260 ? 6.517   37.439  43.691  1.00 17.95 ? 259 LEU B O   1 
ATOM   5274  C  CB  . LEU B  1 260 ? 7.825   38.578  41.250  1.00 19.00 ? 259 LEU B CB  1 
ATOM   5275  C  CG  . LEU B  1 260 ? 9.307   38.574  41.608  1.00 20.29 ? 259 LEU B CG  1 
ATOM   5276  C  CD1 . LEU B  1 260 ? 9.641   37.488  42.599  1.00 20.70 ? 259 LEU B CD1 1 
ATOM   5277  C  CD2 . LEU B  1 260 ? 10.074  38.346  40.297  1.00 22.56 ? 259 LEU B CD2 1 
ATOM   5278  N  N   . ARG B  1 261 ? 7.313   39.325  44.615  1.00 17.43 ? 260 ARG B N   1 
ATOM   5279  C  CA  . ARG B  1 261 ? 7.169   38.835  45.992  1.00 17.36 ? 260 ARG B CA  1 
ATOM   5280  C  C   . ARG B  1 261 ? 5.806   39.153  46.606  1.00 16.73 ? 260 ARG B C   1 
ATOM   5281  O  O   . ARG B  1 261 ? 5.551   38.789  47.762  1.00 17.17 ? 260 ARG B O   1 
ATOM   5282  C  CB  . ARG B  1 261 ? 8.291   39.368  46.868  1.00 18.33 ? 260 ARG B CB  1 
ATOM   5283  C  CG  . ARG B  1 261 ? 9.687   38.942  46.409  1.00 19.68 ? 260 ARG B CG  1 
ATOM   5284  C  CD  . ARG B  1 261 ? 10.699  39.021  47.559  1.00 20.66 ? 260 ARG B CD  1 
ATOM   5285  N  NE  . ARG B  1 261 ? 10.902  40.373  48.085  1.00 20.43 ? 260 ARG B NE  1 
ATOM   5286  C  CZ  . ARG B  1 261 ? 11.597  40.702  49.168  1.00 21.00 ? 260 ARG B CZ  1 
ATOM   5287  N  NH1 . ARG B  1 261 ? 12.110  39.768  49.959  1.00 22.13 ? 260 ARG B NH1 1 
ATOM   5288  N  NH2 . ARG B  1 261 ? 11.740  41.978  49.500  1.00 22.16 ? 260 ARG B NH2 1 
ATOM   5289  N  N   . ASP B  1 262 ? 4.929   39.782  45.840  1.00 16.25 ? 261 ASP B N   1 
ATOM   5290  C  CA  . ASP B  1 262 ? 3.658   40.284  46.344  1.00 16.61 ? 261 ASP B CA  1 
ATOM   5291  C  C   . ASP B  1 262 ? 2.430   39.697  45.674  1.00 16.29 ? 261 ASP B C   1 
ATOM   5292  O  O   . ASP B  1 262 ? 1.326   40.315  45.713  1.00 15.99 ? 261 ASP B O   1 
ATOM   5293  C  CB  . ASP B  1 262 ? 3.620   41.804  46.195  1.00 17.19 ? 261 ASP B CB  1 
ATOM   5294  C  CG  . ASP B  1 262 ? 4.737   42.499  46.951  1.00 17.94 ? 261 ASP B CG  1 
ATOM   5295  O  OD1 . ASP B  1 262 ? 4.952   42.205  48.139  1.00 18.07 ? 261 ASP B OD1 1 
ATOM   5296  O  OD2 . ASP B  1 262 ? 5.392   43.376  46.336  1.00 19.46 ? 261 ASP B OD2 1 
ATOM   5297  N  N   . TYR B  1 263 ? 2.554   38.507  45.076  1.00 16.04 ? 262 TYR B N   1 
ATOM   5298  C  CA  . TYR B  1 263 ? 1.420   37.960  44.330  1.00 16.15 ? 262 TYR B CA  1 
ATOM   5299  C  C   . TYR B  1 263 ? 0.215   37.632  45.199  1.00 16.43 ? 262 TYR B C   1 
ATOM   5300  O  O   . TYR B  1 263 ? -0.927  37.781  44.754  1.00 16.56 ? 262 TYR B O   1 
ATOM   5301  C  CB  . TYR B  1 263 ? 1.818   36.727  43.488  1.00 16.37 ? 262 TYR B CB  1 
ATOM   5302  C  CG  . TYR B  1 263 ? 2.748   37.022  42.318  1.00 16.84 ? 262 TYR B CG  1 
ATOM   5303  C  CD1 . TYR B  1 263 ? 2.672   38.223  41.604  1.00 18.78 ? 262 TYR B CD1 1 
ATOM   5304  C  CD2 . TYR B  1 263 ? 3.675   36.074  41.901  1.00 18.40 ? 262 TYR B CD2 1 
ATOM   5305  C  CE1 . TYR B  1 263 ? 3.504   38.478  40.538  1.00 19.18 ? 262 TYR B CE1 1 
ATOM   5306  C  CE2 . TYR B  1 263 ? 4.525   36.318  40.839  1.00 17.97 ? 262 TYR B CE2 1 
ATOM   5307  C  CZ  . TYR B  1 263 ? 4.433   37.506  40.159  1.00 18.71 ? 262 TYR B CZ  1 
ATOM   5308  O  OH  . TYR B  1 263 ? 5.257   37.767  39.093  1.00 17.36 ? 262 TYR B OH  1 
ATOM   5309  N  N   . ARG B  1 264 ? 0.432   37.178  46.421  1.00 16.91 ? 263 ARG B N   1 
ATOM   5310  C  CA  . ARG B  1 264 ? -0.711  36.857  47.291  1.00 18.82 ? 263 ARG B CA  1 
ATOM   5311  C  C   . ARG B  1 264 ? -1.573  38.111  47.535  1.00 18.85 ? 263 ARG B C   1 
ATOM   5312  O  O   . ARG B  1 264 ? -2.792  38.054  47.375  1.00 19.11 ? 263 ARG B O   1 
ATOM   5313  C  CB  . ARG B  1 264 ? -0.266  36.198  48.591  1.00 19.93 ? 263 ARG B CB  1 
ATOM   5314  C  CG  . ARG B  1 264 ? -1.402  35.564  49.378  1.00 22.12 ? 263 ARG B CG  1 
ATOM   5315  C  CD  . ARG B  1 264 ? -0.874  34.951  50.665  1.00 23.78 ? 263 ARG B CD  1 
ATOM   5316  N  NE  . ARG B  1 264 ? -1.843  34.049  51.288  1.00 26.87 ? 263 ARG B NE  1 
ATOM   5317  C  CZ  . ARG B  1 264 ? -2.805  34.403  52.147  1.00 29.24 ? 263 ARG B CZ  1 
ATOM   5318  N  NH1 . ARG B  1 264 ? -2.990  35.673  52.497  1.00 29.86 ? 263 ARG B NH1 1 
ATOM   5319  N  NH2 . ARG B  1 264 ? -3.605  33.465  52.668  1.00 30.61 ? 263 ARG B NH2 1 
ATOM   5320  N  N   . LYS B  1 265 ? -0.934  39.226  47.870  1.00 18.73 ? 264 LYS B N   1 
ATOM   5321  C  CA  . LYS B  1 265 ? -1.607  40.523  48.035  1.00 20.93 ? 264 LYS B CA  1 
ATOM   5322  C  C   . LYS B  1 265 ? -2.295  40.989  46.763  1.00 19.72 ? 264 LYS B C   1 
ATOM   5323  O  O   . LYS B  1 265 ? -3.398  41.540  46.820  1.00 19.82 ? 264 LYS B O   1 
ATOM   5324  C  CB  . LYS B  1 265 ? -0.601  41.676  48.365  1.00 22.43 ? 264 LYS B CB  1 
ATOM   5325  C  CG  . LYS B  1 265 ? 0.169   41.522  49.619  1.00 25.40 ? 264 LYS B CG  1 
ATOM   5326  C  CD  . LYS B  1 265 ? 0.751   42.835  50.099  1.00 24.44 ? 264 LYS B CD  1 
ATOM   5327  C  CE  . LYS B  1 265 ? 1.813   43.406  49.214  1.00 23.74 ? 264 LYS B CE  1 
ATOM   5328  N  NZ  . LYS B  1 265 ? 2.540   44.430  50.002  1.00 22.11 ? 264 LYS B NZ  1 
ATOM   5329  N  N   . PHE B  1 266 ? -1.585  40.873  45.649  1.00 18.13 ? 265 PHE B N   1 
ATOM   5330  C  CA  . PHE B  1 266 ? -2.108  41.225  44.326  1.00 18.46 ? 265 PHE B CA  1 
ATOM   5331  C  C   . PHE B  1 266 ? -3.424  40.493  44.038  1.00 17.83 ? 265 PHE B C   1 
ATOM   5332  O  O   . PHE B  1 266 ? -4.434  41.103  43.713  1.00 17.81 ? 265 PHE B O   1 
ATOM   5333  C  CB  . PHE B  1 266 ? -1.069  40.900  43.259  1.00 18.60 ? 265 PHE B CB  1 
ATOM   5334  C  CG  . PHE B  1 266 ? -1.535  41.158  41.854  1.00 19.47 ? 265 PHE B CG  1 
ATOM   5335  C  CD1 . PHE B  1 266 ? -1.598  42.449  41.363  1.00 19.96 ? 265 PHE B CD1 1 
ATOM   5336  C  CD2 . PHE B  1 266 ? -1.936  40.111  41.050  1.00 19.71 ? 265 PHE B CD2 1 
ATOM   5337  C  CE1 . PHE B  1 266 ? -2.024  42.688  40.061  1.00 20.56 ? 265 PHE B CE1 1 
ATOM   5338  C  CE2 . PHE B  1 266 ? -2.370  40.338  39.748  1.00 20.47 ? 265 PHE B CE2 1 
ATOM   5339  C  CZ  . PHE B  1 266 ? -2.416  41.634  39.254  1.00 20.37 ? 265 PHE B CZ  1 
ATOM   5340  N  N   . PHE B  1 267 ? -3.421  39.187  44.233  1.00 18.31 ? 266 PHE B N   1 
ATOM   5341  C  CA  . PHE B  1 267 ? -4.646  38.405  44.005  1.00 19.05 ? 266 PHE B CA  1 
ATOM   5342  C  C   . PHE B  1 267 ? -5.786  38.768  44.967  1.00 20.30 ? 266 PHE B C   1 
ATOM   5343  O  O   . PHE B  1 267 ? -6.960  38.835  44.569  1.00 21.67 ? 266 PHE B O   1 
ATOM   5344  C  CB  . PHE B  1 267 ? -4.325  36.920  44.015  1.00 18.87 ? 266 PHE B CB  1 
ATOM   5345  C  CG  . PHE B  1 267 ? -3.693  36.438  42.742  1.00 19.34 ? 266 PHE B CG  1 
ATOM   5346  C  CD1 . PHE B  1 267 ? -4.403  36.489  41.546  1.00 19.73 ? 266 PHE B CD1 1 
ATOM   5347  C  CD2 . PHE B  1 267 ? -2.383  35.950  42.724  1.00 18.97 ? 266 PHE B CD2 1 
ATOM   5348  C  CE1 . PHE B  1 267 ? -3.834  36.037  40.371  1.00 19.51 ? 266 PHE B CE1 1 
ATOM   5349  C  CE2 . PHE B  1 267 ? -1.813  35.484  41.544  1.00 19.60 ? 266 PHE B CE2 1 
ATOM   5350  C  CZ  . PHE B  1 267 ? -2.553  35.499  40.373  1.00 18.91 ? 266 PHE B CZ  1 
ATOM   5351  N  N   . GLN B  1 268 ? -5.459  39.038  46.224  1.00 20.30 ? 267 GLN B N   1 
ATOM   5352  C  CA  . GLN B  1 268 ? -6.463  39.551  47.157  1.00 22.03 ? 267 GLN B CA  1 
ATOM   5353  C  C   . GLN B  1 268 ? -7.026  40.868  46.675  1.00 21.87 ? 267 GLN B C   1 
ATOM   5354  O  O   . GLN B  1 268 ? -8.246  41.073  46.707  1.00 21.92 ? 267 GLN B O   1 
ATOM   5355  C  CB  . GLN B  1 268 ? -5.885  39.750  48.566  1.00 22.75 ? 267 GLN B CB  1 
ATOM   5356  C  CG  . GLN B  1 268 ? -5.502  38.457  49.260  1.00 25.36 ? 267 GLN B CG  1 
ATOM   5357  C  CD  . GLN B  1 268 ? -4.864  38.713  50.627  1.00 27.47 ? 267 GLN B CD  1 
ATOM   5358  O  OE1 . GLN B  1 268 ? -3.955  39.530  50.767  1.00 29.49 ? 267 GLN B OE1 1 
ATOM   5359  N  NE2 . GLN B  1 268 ? -5.344  38.015  51.633  1.00 31.19 ? 267 GLN B NE2 1 
ATOM   5360  N  N   . ASP B  1 269 ? -6.152  41.765  46.246  1.00 20.60 ? 268 ASP B N   1 
ATOM   5361  C  CA  . ASP B  1 269 ? -6.560  43.137  45.975  1.00 21.13 ? 268 ASP B CA  1 
ATOM   5362  C  C   . ASP B  1 269 ? -7.315  43.295  44.659  1.00 23.10 ? 268 ASP B C   1 
ATOM   5363  O  O   . ASP B  1 269 ? -8.064  44.262  44.501  1.00 22.84 ? 268 ASP B O   1 
ATOM   5364  C  CB  . ASP B  1 269 ? -5.350  44.069  46.006  1.00 20.98 ? 268 ASP B CB  1 
ATOM   5365  C  CG  . ASP B  1 269 ? -4.767  44.224  47.420  1.00 20.96 ? 268 ASP B CG  1 
ATOM   5366  O  OD1 . ASP B  1 269 ? -5.450  43.785  48.371  1.00 20.77 ? 268 ASP B OD1 1 
ATOM   5367  O  OD2 . ASP B  1 269 ? -3.633  44.780  47.567  1.00 21.02 ? 268 ASP B OD2 1 
ATOM   5368  N  N   . ILE B  1 270 ? -7.115  42.367  43.720  1.00 22.59 ? 269 ILE B N   1 
ATOM   5369  C  CA  . ILE B  1 270 ? -7.911  42.399  42.502  1.00 23.75 ? 269 ILE B CA  1 
ATOM   5370  C  C   . ILE B  1 270 ? -9.228  41.634  42.647  1.00 25.72 ? 269 ILE B C   1 
ATOM   5371  O  O   . ILE B  1 270 ? -10.037 41.632  41.739  1.00 28.41 ? 269 ILE B O   1 
ATOM   5372  C  CB  . ILE B  1 270 ? -7.144  41.916  41.269  1.00 23.04 ? 269 ILE B CB  1 
ATOM   5373  C  CG1 . ILE B  1 270 ? -6.866  40.414  41.342  1.00 21.72 ? 269 ILE B CG1 1 
ATOM   5374  C  CG2 . ILE B  1 270 ? -5.873  42.751  41.075  1.00 22.89 ? 269 ILE B CG2 1 
ATOM   5375  C  CD1 . ILE B  1 270 ? -6.115  39.885  40.148  1.00 21.11 ? 269 ILE B CD1 1 
ATOM   5376  N  N   . GLY B  1 271 ? -9.426  40.964  43.766  1.00 26.13 ? 270 GLY B N   1 
ATOM   5377  C  CA  . GLY B  1 271 ? -10.635 40.197  44.028  1.00 26.98 ? 270 GLY B CA  1 
ATOM   5378  C  C   . GLY B  1 271 ? -10.629 38.842  43.355  1.00 27.97 ? 270 GLY B C   1 
ATOM   5379  O  O   . GLY B  1 271 ? -11.681 38.361  42.948  1.00 28.40 ? 270 GLY B O   1 
ATOM   5380  N  N   . PHE B  1 272 ? -9.460  38.203  43.264  1.00 25.55 ? 271 PHE B N   1 
ATOM   5381  C  CA  . PHE B  1 272 ? -9.355  36.896  42.641  1.00 24.65 ? 271 PHE B CA  1 
ATOM   5382  C  C   . PHE B  1 272 ? -8.403  35.985  43.416  1.00 24.46 ? 271 PHE B C   1 
ATOM   5383  O  O   . PHE B  1 272 ? -7.311  35.643  42.957  1.00 21.93 ? 271 PHE B O   1 
ATOM   5384  C  CB  . PHE B  1 272 ? -8.922  37.050  41.181  1.00 24.42 ? 271 PHE B CB  1 
ATOM   5385  C  CG  . PHE B  1 272 ? -8.916  35.751  40.423  1.00 24.59 ? 271 PHE B CG  1 
ATOM   5386  C  CD1 . PHE B  1 272 ? -10.050 34.951  40.403  1.00 26.88 ? 271 PHE B CD1 1 
ATOM   5387  C  CD2 . PHE B  1 272 ? -7.796  35.340  39.745  1.00 25.54 ? 271 PHE B CD2 1 
ATOM   5388  C  CE1 . PHE B  1 272 ? -10.054 33.744  39.715  1.00 27.72 ? 271 PHE B CE1 1 
ATOM   5389  C  CE2 . PHE B  1 272 ? -7.785  34.125  39.079  1.00 26.31 ? 271 PHE B CE2 1 
ATOM   5390  C  CZ  . PHE B  1 272 ? -8.918  33.335  39.078  1.00 26.31 ? 271 PHE B CZ  1 
ATOM   5391  N  N   . GLU B  1 273 ? -8.850  35.545  44.586  1.00 25.66 ? 272 GLU B N   1 
ATOM   5392  C  CA  . GLU B  1 273 ? -8.032  34.723  45.465  1.00 27.87 ? 272 GLU B CA  1 
ATOM   5393  C  C   . GLU B  1 273 ? -7.650  33.369  44.869  1.00 26.92 ? 272 GLU B C   1 
ATOM   5394  O  O   . GLU B  1 273 ? -6.565  32.846  45.163  1.00 26.95 ? 272 GLU B O   1 
ATOM   5395  C  CB  . GLU B  1 273 ? -8.712  34.578  46.841  1.00 33.28 ? 272 GLU B CB  1 
ATOM   5396  C  CG  . GLU B  1 273 ? -8.705  35.928  47.565  1.00 39.32 ? 272 GLU B CG  1 
ATOM   5397  C  CD  . GLU B  1 273 ? -9.441  35.967  48.901  1.00 47.81 ? 272 GLU B CD  1 
ATOM   5398  O  OE1 . GLU B  1 273 ? -10.029 34.938  49.321  1.00 53.63 ? 272 GLU B OE1 1 
ATOM   5399  O  OE2 . GLU B  1 273 ? -9.430  37.058  49.532  1.00 54.66 ? 272 GLU B OE2 1 
ATOM   5400  N  N   . ASP B  1 274 ? -8.506  32.796  44.023  1.00 24.17 ? 273 ASP B N   1 
ATOM   5401  C  CA  . ASP B  1 274 ? -8.179  31.524  43.376  1.00 24.49 ? 273 ASP B CA  1 
ATOM   5402  C  C   . ASP B  1 274 ? -6.895  31.611  42.544  1.00 21.87 ? 273 ASP B C   1 
ATOM   5403  O  O   . ASP B  1 274 ? -6.210  30.608  42.360  1.00 22.28 ? 273 ASP B O   1 
ATOM   5404  C  CB  . ASP B  1 274 ? -9.297  31.080  42.425  1.00 26.92 ? 273 ASP B CB  1 
ATOM   5405  C  CG  . ASP B  1 274 ? -10.504 30.488  43.143  1.00 31.59 ? 273 ASP B CG  1 
ATOM   5406  O  OD1 . ASP B  1 274 ? -10.425 30.176  44.354  1.00 31.97 ? 273 ASP B OD1 1 
ATOM   5407  O  OD2 . ASP B  1 274 ? -11.538 30.312  42.451  1.00 35.48 ? 273 ASP B OD2 1 
ATOM   5408  N  N   . GLY B  1 275 ? -6.599  32.780  42.000  1.00 20.45 ? 274 GLY B N   1 
ATOM   5409  C  CA  . GLY B  1 275 ? -5.385  32.953  41.215  1.00 20.53 ? 274 GLY B CA  1 
ATOM   5410  C  C   . GLY B  1 275 ? -4.133  32.663  42.003  1.00 20.00 ? 274 GLY B C   1 
ATOM   5411  O  O   . GLY B  1 275 ? -3.157  32.149  41.457  1.00 19.63 ? 274 GLY B O   1 
ATOM   5412  N  N   . TRP B  1 276 ? -4.151  32.990  43.295  1.00 20.25 ? 275 TRP B N   1 
ATOM   5413  C  CA  . TRP B  1 276 ? -3.000  32.693  44.160  1.00 20.09 ? 275 TRP B CA  1 
ATOM   5414  C  C   . TRP B  1 276 ? -2.820  31.199  44.321  1.00 19.63 ? 275 TRP B C   1 
ATOM   5415  O  O   . TRP B  1 276 ? -1.703  30.677  44.280  1.00 18.31 ? 275 TRP B O   1 
ATOM   5416  C  CB  . TRP B  1 276 ? -3.168  33.374  45.527  1.00 20.88 ? 275 TRP B CB  1 
ATOM   5417  C  CG  . TRP B  1 276 ? -2.182  32.913  46.570  1.00 20.94 ? 275 TRP B CG  1 
ATOM   5418  C  CD1 . TRP B  1 276 ? -2.462  32.247  47.725  1.00 22.66 ? 275 TRP B CD1 1 
ATOM   5419  C  CD2 . TRP B  1 276 ? -0.775  33.092  46.546  1.00 20.65 ? 275 TRP B CD2 1 
ATOM   5420  N  NE1 . TRP B  1 276 ? -1.311  32.001  48.432  1.00 23.12 ? 275 TRP B NE1 1 
ATOM   5421  C  CE2 . TRP B  1 276 ? -0.257  32.515  47.724  1.00 22.31 ? 275 TRP B CE2 1 
ATOM   5422  C  CE3 . TRP B  1 276 ? 0.100   33.680  45.643  1.00 21.00 ? 275 TRP B CE3 1 
ATOM   5423  C  CZ2 . TRP B  1 276 ? 1.096   32.515  48.027  1.00 23.37 ? 275 TRP B CZ2 1 
ATOM   5424  C  CZ3 . TRP B  1 276 ? 1.464   33.652  45.932  1.00 22.24 ? 275 TRP B CZ3 1 
ATOM   5425  C  CH2 . TRP B  1 276 ? 1.943   33.107  47.122  1.00 22.75 ? 275 TRP B CH2 1 
ATOM   5426  N  N   . LEU B  1 277 ? -3.936  30.502  44.493  1.00 20.03 ? 276 LEU B N   1 
ATOM   5427  C  CA  . LEU B  1 277 ? -3.890  29.049  44.591  1.00 20.79 ? 276 LEU B CA  1 
ATOM   5428  C  C   . LEU B  1 277 ? -3.377  28.429  43.273  1.00 19.98 ? 276 LEU B C   1 
ATOM   5429  O  O   . LEU B  1 277 ? -2.549  27.514  43.288  1.00 20.15 ? 276 LEU B O   1 
ATOM   5430  C  CB  . LEU B  1 277 ? -5.266  28.499  44.972  1.00 22.29 ? 276 LEU B CB  1 
ATOM   5431  C  CG  . LEU B  1 277 ? -5.902  29.050  46.256  1.00 24.02 ? 276 LEU B CG  1 
ATOM   5432  C  CD1 . LEU B  1 277 ? -7.283  28.453  46.478  1.00 25.45 ? 276 LEU B CD1 1 
ATOM   5433  C  CD2 . LEU B  1 277 ? -5.007  28.767  47.460  1.00 25.94 ? 276 LEU B CD2 1 
ATOM   5434  N  N   . MET B  1 278 ? -3.829  28.953  42.149  1.00 19.32 ? 277 MET B N   1 
ATOM   5435  C  CA  . MET B  1 278 ? -3.313  28.522  40.840  1.00 19.34 ? 277 MET B CA  1 
ATOM   5436  C  C   . MET B  1 278 ? -1.800  28.766  40.680  1.00 18.61 ? 277 MET B C   1 
ATOM   5437  O  O   . MET B  1 278 ? -1.069  27.911  40.152  1.00 17.77 ? 277 MET B O   1 
ATOM   5438  C  CB  . MET B  1 278 ? -4.039  29.238  39.715  1.00 20.18 ? 277 MET B CB  1 
ATOM   5439  C  CG  . MET B  1 278 ? -5.512  28.892  39.569  1.00 22.18 ? 277 MET B CG  1 
ATOM   5440  S  SD  . MET B  1 278 ? -6.221  30.014  38.342  1.00 25.37 ? 277 MET B SD  1 
ATOM   5441  C  CE  . MET B  1 278 ? -7.929  29.474  38.365  1.00 27.66 ? 277 MET B CE  1 
ATOM   5442  N  N   . ARG B  1 279 ? -1.342  29.919  41.142  1.00 17.79 ? 278 ARG B N   1 
ATOM   5443  C  CA  . ARG B  1 279 ? 0.080   30.232  41.094  1.00 17.98 ? 278 ARG B CA  1 
ATOM   5444  C  C   . ARG B  1 279 ? 0.869   29.261  41.960  1.00 18.48 ? 278 ARG B C   1 
ATOM   5445  O  O   . ARG B  1 279 ? 1.899   28.723  41.526  1.00 18.15 ? 278 ARG B O   1 
ATOM   5446  C  CB  . ARG B  1 279 ? 0.344   31.696  41.491  1.00 17.83 ? 278 ARG B CB  1 
ATOM   5447  C  CG  . ARG B  1 279 ? 1.821   32.091  41.466  1.00 17.81 ? 278 ARG B CG  1 
ATOM   5448  C  CD  . ARG B  1 279 ? 2.412   31.962  40.080  1.00 17.38 ? 278 ARG B CD  1 
ATOM   5449  N  NE  . ARG B  1 279 ? 3.782   32.468  40.036  1.00 17.28 ? 278 ARG B NE  1 
ATOM   5450  C  CZ  . ARG B  1 279 ? 4.452   32.722  38.914  1.00 17.29 ? 278 ARG B CZ  1 
ATOM   5451  N  NH1 . ARG B  1 279 ? 3.905   32.492  37.725  1.00 17.22 ? 278 ARG B NH1 1 
ATOM   5452  N  NH2 . ARG B  1 279 ? 5.694   33.171  38.983  1.00 18.45 ? 278 ARG B NH2 1 
ATOM   5453  N  N   . GLN B  1 280 ? 0.381   28.988  43.170  1.00 20.40 ? 279 GLN B N   1 
ATOM   5454  C  CA  . GLN B  1 280 ? 1.045   27.985  44.012  1.00 22.20 ? 279 GLN B CA  1 
ATOM   5455  C  C   . GLN B  1 280 ? 1.078   26.612  43.344  1.00 21.29 ? 279 GLN B C   1 
ATOM   5456  O  O   . GLN B  1 280 ? 2.044   25.901  43.504  1.00 21.50 ? 279 GLN B O   1 
ATOM   5457  C  CB  . GLN B  1 280 ? 0.360   27.855  45.351  1.00 24.52 ? 279 GLN B CB  1 
ATOM   5458  C  CG  . GLN B  1 280 ? 0.514   29.066  46.244  1.00 27.03 ? 279 GLN B CG  1 
ATOM   5459  C  CD  . GLN B  1 280 ? -0.104  28.793  47.599  1.00 31.44 ? 279 GLN B CD  1 
ATOM   5460  O  OE1 . GLN B  1 280 ? -1.277  28.411  47.702  1.00 33.83 ? 279 GLN B OE1 1 
ATOM   5461  N  NE2 . GLN B  1 280 ? 0.675   28.978  48.649  1.00 34.56 ? 279 GLN B NE2 1 
ATOM   5462  N  N   . ASP B  1 281 ? -0.006  26.232  42.662  1.00 20.93 ? 280 ASP B N   1 
ATOM   5463  C  CA  . ASP B  1 281 ? -0.095  24.912  42.005  1.00 21.87 ? 280 ASP B CA  1 
ATOM   5464  C  C   . ASP B  1 281 ? 0.954   24.781  40.874  1.00 21.97 ? 280 ASP B C   1 
ATOM   5465  O  O   . ASP B  1 281 ? 1.367   23.672  40.531  1.00 22.86 ? 280 ASP B O   1 
ATOM   5466  C  CB  . ASP B  1 281 ? -1.454  24.693  41.320  1.00 23.61 ? 280 ASP B CB  1 
ATOM   5467  C  CG  . ASP B  1 281 ? -2.650  24.608  42.280  1.00 27.14 ? 280 ASP B CG  1 
ATOM   5468  O  OD1 . ASP B  1 281 ? -2.469  24.372  43.508  1.00 27.82 ? 280 ASP B OD1 1 
ATOM   5469  O  OD2 . ASP B  1 281 ? -3.794  24.781  41.752  1.00 27.98 ? 280 ASP B OD2 1 
ATOM   5470  N  N   . THR B  1 282 ? 1.285   25.896  40.225  1.00 19.83 ? 281 THR B N   1 
ATOM   5471  C  CA  . THR B  1 282 ? 1.984   25.845  38.953  1.00 19.07 ? 281 THR B CA  1 
ATOM   5472  C  C   . THR B  1 282 ? 3.413   26.400  38.969  1.00 19.93 ? 281 THR B C   1 
ATOM   5473  O  O   . THR B  1 282 ? 4.186   26.099  38.051  1.00 20.00 ? 281 THR B O   1 
ATOM   5474  C  CB  . THR B  1 282 ? 1.175   26.555  37.856  1.00 17.93 ? 281 THR B CB  1 
ATOM   5475  O  OG1 . THR B  1 282 ? 0.998   27.944  38.168  1.00 18.59 ? 281 THR B OG1 1 
ATOM   5476  C  CG2 . THR B  1 282 ? -0.156  25.889  37.679  1.00 18.12 ? 281 THR B CG2 1 
ATOM   5477  N  N   . GLU B  1 283 ? 3.760   27.198  39.986  1.00 20.89 ? 282 GLU B N   1 
ATOM   5478  C  CA  . GLU B  1 283 ? 5.048   27.934  39.982  1.00 22.68 ? 282 GLU B CA  1 
ATOM   5479  C  C   . GLU B  1 283 ? 6.265   27.013  39.990  1.00 22.66 ? 282 GLU B C   1 
ATOM   5480  O  O   . GLU B  1 283 ? 7.334   27.413  39.562  1.00 21.99 ? 282 GLU B O   1 
ATOM   5481  C  CB  . GLU B  1 283 ? 5.124   28.935  41.165  1.00 24.19 ? 282 GLU B CB  1 
ATOM   5482  C  CG  . GLU B  1 283 ? 5.145   28.275  42.530  1.00 27.44 ? 282 GLU B CG  1 
ATOM   5483  C  CD  . GLU B  1 283 ? 5.144   29.258  43.699  1.00 33.19 ? 282 GLU B CD  1 
ATOM   5484  O  OE1 . GLU B  1 283 ? 5.175   30.495  43.472  1.00 40.03 ? 282 GLU B OE1 1 
ATOM   5485  O  OE2 . GLU B  1 283 ? 5.121   28.783  44.855  1.00 38.82 ? 282 GLU B OE2 1 
ATOM   5486  N  N   . GLY B  1 284 ? 6.106   25.791  40.484  1.00 22.29 ? 283 GLY B N   1 
ATOM   5487  C  CA  . GLY B  1 284 ? 7.212   24.848  40.548  1.00 23.08 ? 283 GLY B CA  1 
ATOM   5488  C  C   . GLY B  1 284 ? 7.277   23.833  39.409  1.00 23.33 ? 283 GLY B C   1 
ATOM   5489  O  O   . GLY B  1 284 ? 8.149   22.974  39.413  1.00 22.98 ? 283 GLY B O   1 
ATOM   5490  N  N   . LEU B  1 285 ? 6.371   23.911  38.436  1.00 21.81 ? 284 LEU B N   1 
ATOM   5491  C  CA  . LEU B  1 285 ? 6.293   22.866  37.404  1.00 22.14 ? 284 LEU B CA  1 
ATOM   5492  C  C   . LEU B  1 285 ? 7.539   22.814  36.528  1.00 22.75 ? 284 LEU B C   1 
ATOM   5493  O  O   . LEU B  1 285 ? 8.033   21.735  36.212  1.00 22.60 ? 284 LEU B O   1 
ATOM   5494  C  CB  . LEU B  1 285 ? 5.075   23.069  36.505  1.00 21.87 ? 284 LEU B CB  1 
ATOM   5495  C  CG  . LEU B  1 285 ? 3.727   22.900  37.203  1.00 22.23 ? 284 LEU B CG  1 
ATOM   5496  C  CD1 . LEU B  1 285 ? 2.593   23.324  36.272  1.00 21.45 ? 284 LEU B CD1 1 
ATOM   5497  C  CD2 . LEU B  1 285 ? 3.566   21.470  37.695  1.00 23.97 ? 284 LEU B CD2 1 
ATOM   5498  N  N   . VAL B  1 286 ? 7.986   23.973  36.083  1.00 24.15 ? 285 VAL B N   1 
ATOM   5499  C  CA  . VAL B  1 286 ? 9.158   24.065  35.237  1.00 25.56 ? 285 VAL B CA  1 
ATOM   5500  C  C   . VAL B  1 286 ? 10.363  24.364  36.118  1.00 29.24 ? 285 VAL B C   1 
ATOM   5501  O  O   . VAL B  1 286 ? 10.375  25.343  36.847  1.00 29.28 ? 285 VAL B O   1 
ATOM   5502  C  CB  . VAL B  1 286 ? 8.954   25.139  34.158  1.00 25.83 ? 285 VAL B CB  1 
ATOM   5503  C  CG1 . VAL B  1 286 ? 10.253  25.461  33.441  1.00 27.12 ? 285 VAL B CG1 1 
ATOM   5504  C  CG2 . VAL B  1 286 ? 7.914   24.648  33.156  1.00 26.53 ? 285 VAL B CG2 1 
ATOM   5505  N  N   . GLU B  1 287 ? 11.366  23.505  36.057  1.00 32.28 ? 286 GLU B N   1 
ATOM   5506  C  CA  . GLU B  1 287 ? 12.535  23.653  36.904  1.00 36.02 ? 286 GLU B CA  1 
ATOM   5507  C  C   . GLU B  1 287 ? 13.339  24.864  36.434  1.00 37.06 ? 286 GLU B C   1 
ATOM   5508  O  O   . GLU B  1 287 ? 13.764  24.959  35.280  1.00 31.12 ? 286 GLU B O   1 
ATOM   5509  C  CB  . GLU B  1 287 ? 13.361  22.370  36.921  1.00 39.42 ? 286 GLU B CB  1 
ATOM   5510  C  CG  . GLU B  1 287 ? 14.014  22.067  38.262  1.00 45.69 ? 286 GLU B CG  1 
ATOM   5511  C  CD  . GLU B  1 287 ? 15.110  23.057  38.622  1.00 50.60 ? 286 GLU B CD  1 
ATOM   5512  O  OE1 . GLU B  1 287 ? 15.883  23.457  37.719  1.00 51.51 ? 286 GLU B OE1 1 
ATOM   5513  O  OE2 . GLU B  1 287 ? 15.192  23.435  39.815  1.00 53.30 ? 286 GLU B OE2 1 
ATOM   5514  N  N   . ALA B  1 288 ? 13.523  25.775  37.383  1.00 39.83 ? 287 ALA B N   1 
ATOM   5515  C  CA  . ALA B  1 288 ? 14.075  27.098  37.173  1.00 41.36 ? 287 ALA B CA  1 
ATOM   5516  C  C   . ALA B  1 288 ? 15.363  27.100  36.351  1.00 43.32 ? 287 ALA B C   1 
ATOM   5517  O  O   . ALA B  1 288 ? 15.526  27.966  35.496  1.00 48.80 ? 287 ALA B O   1 
ATOM   5518  C  CB  . ALA B  1 288 ? 14.294  27.783  38.531  1.00 40.62 ? 287 ALA B CB  1 
ATOM   5519  N  N   . THR B  1 289 ? 16.272  26.155  36.610  1.00 39.47 ? 288 THR B N   1 
ATOM   5520  C  CA  . THR B  1 289 ? 17.603  26.180  36.008  1.00 41.41 ? 288 THR B CA  1 
ATOM   5521  C  C   . THR B  1 289 ? 17.894  25.069  34.982  1.00 43.20 ? 288 THR B C   1 
ATOM   5522  O  O   . THR B  1 289 ? 18.835  25.202  34.199  1.00 46.01 ? 288 THR B O   1 
ATOM   5523  C  CB  . THR B  1 289 ? 18.702  26.111  37.111  1.00 44.42 ? 288 THR B CB  1 
ATOM   5524  O  OG1 . THR B  1 289 ? 18.578  24.898  37.853  1.00 43.50 ? 288 THR B OG1 1 
ATOM   5525  C  CG2 . THR B  1 289 ? 18.581  27.293  38.089  1.00 45.49 ? 288 THR B CG2 1 
ATOM   5526  N  N   . MET B  1 290 ? 17.108  23.986  34.999  1.00 37.09 ? 289 MET B N   1 
ATOM   5527  C  CA  . MET B  1 290 ? 17.391  22.789  34.215  1.00 35.40 ? 289 MET B CA  1 
ATOM   5528  C  C   . MET B  1 290 ? 17.147  23.024  32.716  1.00 32.58 ? 289 MET B C   1 
ATOM   5529  O  O   . MET B  1 290 ? 16.043  23.396  32.322  1.00 29.15 ? 289 MET B O   1 
ATOM   5530  C  CB  . MET B  1 290 ? 16.507  21.651  34.698  1.00 36.35 ? 289 MET B CB  1 
ATOM   5531  C  CG  . MET B  1 290 ? 16.812  20.302  34.072  1.00 41.07 ? 289 MET B CG  1 
ATOM   5532  S  SD  . MET B  1 290 ? 15.572  19.099  34.588  1.00 44.94 ? 289 MET B SD  1 
ATOM   5533  C  CE  . MET B  1 290 ? 16.191  17.606  33.814  1.00 45.04 ? 289 MET B CE  1 
ATOM   5534  N  N   . PRO B  1 291 ? 18.182  22.806  31.881  1.00 30.78 ? 290 PRO B N   1 
ATOM   5535  C  CA  . PRO B  1 291 ? 18.064  23.023  30.444  1.00 29.66 ? 290 PRO B CA  1 
ATOM   5536  C  C   . PRO B  1 291 ? 17.268  21.883  29.807  1.00 27.71 ? 290 PRO B C   1 
ATOM   5537  O  O   . PRO B  1 291 ? 17.048  20.865  30.451  1.00 26.70 ? 290 PRO B O   1 
ATOM   5538  C  CB  . PRO B  1 291 ? 19.516  22.990  29.959  1.00 30.63 ? 290 PRO B CB  1 
ATOM   5539  C  CG  . PRO B  1 291 ? 20.200  22.086  30.918  1.00 32.50 ? 290 PRO B CG  1 
ATOM   5540  C  CD  . PRO B  1 291 ? 19.499  22.253  32.248  1.00 32.42 ? 290 PRO B CD  1 
ATOM   5541  N  N   . PRO B  1 292 ? 16.821  22.068  28.563  1.00 26.16 ? 291 PRO B N   1 
ATOM   5542  C  CA  . PRO B  1 292 ? 15.989  21.015  27.963  1.00 25.20 ? 291 PRO B CA  1 
ATOM   5543  C  C   . PRO B  1 292 ? 16.789  19.762  27.617  1.00 24.42 ? 291 PRO B C   1 
ATOM   5544  O  O   . PRO B  1 292 ? 16.213  18.710  27.535  1.00 24.22 ? 291 PRO B O   1 
ATOM   5545  C  CB  . PRO B  1 292 ? 15.432  21.674  26.712  1.00 25.03 ? 291 PRO B CB  1 
ATOM   5546  C  CG  . PRO B  1 292 ? 16.409  22.750  26.396  1.00 26.07 ? 291 PRO B CG  1 
ATOM   5547  C  CD  . PRO B  1 292 ? 16.834  23.281  27.734  1.00 26.30 ? 291 PRO B CD  1 
ATOM   5548  N  N   . GLY B  1 293 ? 18.104  19.867  27.443  1.00 23.40 ? 292 GLY B N   1 
ATOM   5549  C  CA  . GLY B  1 293 ? 18.935  18.706  27.168  1.00 23.74 ? 292 GLY B CA  1 
ATOM   5550  C  C   . GLY B  1 293 ? 18.869  18.210  25.721  1.00 23.31 ? 292 GLY B C   1 
ATOM   5551  O  O   . GLY B  1 293 ? 19.134  17.037  25.443  1.00 23.26 ? 292 GLY B O   1 
ATOM   5552  N  N   . VAL B  1 294 ? 18.515  19.110  24.808  1.00 22.37 ? 293 VAL B N   1 
ATOM   5553  C  CA  . VAL B  1 294 ? 18.519  18.852  23.370  1.00 22.33 ? 293 VAL B CA  1 
ATOM   5554  C  C   . VAL B  1 294 ? 19.119  20.066  22.632  1.00 22.63 ? 293 VAL B C   1 
ATOM   5555  O  O   . VAL B  1 294 ? 19.201  21.154  23.197  1.00 21.46 ? 293 VAL B O   1 
ATOM   5556  C  CB  . VAL B  1 294 ? 17.083  18.592  22.838  1.00 22.33 ? 293 VAL B CB  1 
ATOM   5557  C  CG1 . VAL B  1 294 ? 16.443  17.442  23.604  1.00 22.66 ? 293 VAL B CG1 1 
ATOM   5558  C  CG2 . VAL B  1 294 ? 16.217  19.831  22.922  1.00 22.26 ? 293 VAL B CG2 1 
ATOM   5559  N  N   . GLN B  1 295 ? 19.495  19.878  21.373  1.00 22.41 ? 294 GLN B N   1 
ATOM   5560  C  CA  . GLN B  1 295 ? 19.903  20.989  20.530  1.00 23.14 ? 294 GLN B CA  1 
ATOM   5561  C  C   . GLN B  1 295 ? 18.770  22.003  20.469  1.00 22.43 ? 294 GLN B C   1 
ATOM   5562  O  O   . GLN B  1 295 ? 17.638  21.656  20.115  1.00 20.12 ? 294 GLN B O   1 
ATOM   5563  C  CB  . GLN B  1 295 ? 20.222  20.518  19.120  1.00 24.96 ? 294 GLN B CB  1 
ATOM   5564  C  CG  . GLN B  1 295 ? 20.732  21.650  18.247  1.00 27.12 ? 294 GLN B CG  1 
ATOM   5565  C  CD  . GLN B  1 295 ? 21.012  21.196  16.848  1.00 28.63 ? 294 GLN B CD  1 
ATOM   5566  O  OE1 . GLN B  1 295 ? 20.252  21.475  15.923  1.00 30.06 ? 294 GLN B OE1 1 
ATOM   5567  N  NE2 . GLN B  1 295 ? 22.088  20.455  16.688  1.00 32.37 ? 294 GLN B NE2 1 
ATOM   5568  N  N   . LEU B  1 296 ? 19.067  23.241  20.831  1.00 21.61 ? 295 LEU B N   1 
ATOM   5569  C  CA  . LEU B  1 296 ? 18.050  24.269  21.000  1.00 21.60 ? 295 LEU B CA  1 
ATOM   5570  C  C   . LEU B  1 296 ? 18.362  25.488  20.130  1.00 21.83 ? 295 LEU B C   1 
ATOM   5571  O  O   . LEU B  1 296 ? 19.507  25.972  20.114  1.00 24.00 ? 295 LEU B O   1 
ATOM   5572  C  CB  . LEU B  1 296 ? 17.982  24.677  22.464  1.00 21.88 ? 295 LEU B CB  1 
ATOM   5573  C  CG  . LEU B  1 296 ? 17.075  25.838  22.820  1.00 23.17 ? 295 LEU B CG  1 
ATOM   5574  C  CD1 . LEU B  1 296 ? 15.615  25.478  22.623  1.00 23.05 ? 295 LEU B CD1 1 
ATOM   5575  C  CD2 . LEU B  1 296 ? 17.344  26.244  24.257  1.00 24.79 ? 295 LEU B CD2 1 
ATOM   5576  N  N   . HIS B  1 297 ? 17.365  25.948  19.378  1.00 20.80 ? 296 HIS B N   1 
ATOM   5577  C  CA  . HIS B  1 297 ? 17.471  27.168  18.581  1.00 21.47 ? 296 HIS B CA  1 
ATOM   5578  C  C   . HIS B  1 297 ? 16.479  28.144  19.198  1.00 21.72 ? 296 HIS B C   1 
ATOM   5579  O  O   . HIS B  1 297 ? 15.265  27.963  19.072  1.00 21.08 ? 296 HIS B O   1 
ATOM   5580  C  CB  . HIS B  1 297 ? 17.130  26.911  17.109  1.00 21.18 ? 296 HIS B CB  1 
ATOM   5581  C  CG  . HIS B  1 297 ? 18.004  25.888  16.454  1.00 22.73 ? 296 HIS B CG  1 
ATOM   5582  N  ND1 . HIS B  1 297 ? 19.056  26.222  15.633  1.00 23.60 ? 296 HIS B ND1 1 
ATOM   5583  C  CD2 . HIS B  1 297 ? 17.995  24.535  16.515  1.00 23.39 ? 296 HIS B CD2 1 
ATOM   5584  C  CE1 . HIS B  1 297 ? 19.657  25.122  15.210  1.00 24.91 ? 296 HIS B CE1 1 
ATOM   5585  N  NE2 . HIS B  1 297 ? 19.041  24.083  15.742  1.00 23.54 ? 296 HIS B NE2 1 
ATOM   5586  N  N   . CYS B  1 298 ? 17.000  29.180  19.838  1.00 22.57 ? 297 CYS B N   1 
ATOM   5587  C  CA  A CYS B  1 298 ? 16.174  30.145  20.550  0.50 24.43 ? 297 CYS B CA  1 
ATOM   5588  C  CA  B CYS B  1 298 ? 16.174  30.170  20.548  0.50 23.81 ? 297 CYS B CA  1 
ATOM   5589  C  C   . CYS B  1 298 ? 15.985  31.424  19.729  1.00 23.66 ? 297 CYS B C   1 
ATOM   5590  O  O   . CYS B  1 298 ? 16.904  32.219  19.591  1.00 23.93 ? 297 CYS B O   1 
ATOM   5591  C  CB  A CYS B  1 298 ? 16.827  30.410  21.885  0.50 26.53 ? 297 CYS B CB  1 
ATOM   5592  C  CB  B CYS B  1 298 ? 16.836  30.548  21.857  0.50 25.25 ? 297 CYS B CB  1 
ATOM   5593  S  SG  A CYS B  1 298 ? 16.027  31.653  22.875  0.50 32.45 ? 297 CYS B SG  1 
ATOM   5594  S  SG  B CYS B  1 298 ? 16.604  29.283  23.081  0.50 28.37 ? 297 CYS B SG  1 
ATOM   5595  N  N   . LEU B  1 299 ? 14.795  31.580  19.155  1.00 21.68 ? 298 LEU B N   1 
ATOM   5596  C  CA  . LEU B  1 299 ? 14.500  32.713  18.302  1.00 22.13 ? 298 LEU B CA  1 
ATOM   5597  C  C   . LEU B  1 299 ? 13.639  33.705  19.081  1.00 21.35 ? 298 LEU B C   1 
ATOM   5598  O  O   . LEU B  1 299 ? 12.585  33.351  19.581  1.00 20.03 ? 298 LEU B O   1 
ATOM   5599  C  CB  . LEU B  1 299 ? 13.805  32.262  17.012  1.00 23.29 ? 298 LEU B CB  1 
ATOM   5600  C  CG  . LEU B  1 299 ? 14.734  31.767  15.880  1.00 26.02 ? 298 LEU B CG  1 
ATOM   5601  C  CD1 . LEU B  1 299 ? 15.531  30.539  16.296  1.00 26.66 ? 298 LEU B CD1 1 
ATOM   5602  C  CD2 . LEU B  1 299 ? 13.939  31.457  14.630  1.00 27.21 ? 298 LEU B CD2 1 
ATOM   5603  N  N   . TYR B  1 300 ? 14.095  34.954  19.165  1.00 21.74 ? 299 TYR B N   1 
ATOM   5604  C  CA  . TYR B  1 300 ? 13.417  35.948  20.006  1.00 21.94 ? 299 TYR B CA  1 
ATOM   5605  C  C   . TYR B  1 300 ? 13.385  37.281  19.283  1.00 22.29 ? 299 TYR B C   1 
ATOM   5606  O  O   . TYR B  1 300 ? 14.374  37.697  18.662  1.00 21.62 ? 299 TYR B O   1 
ATOM   5607  C  CB  . TYR B  1 300 ? 14.098  36.058  21.396  1.00 22.98 ? 299 TYR B CB  1 
ATOM   5608  C  CG  . TYR B  1 300 ? 15.550  36.471  21.349  1.00 24.08 ? 299 TYR B CG  1 
ATOM   5609  C  CD1 . TYR B  1 300 ? 16.564  35.542  21.159  1.00 25.27 ? 299 TYR B CD1 1 
ATOM   5610  C  CD2 . TYR B  1 300 ? 15.914  37.794  21.501  1.00 26.30 ? 299 TYR B CD2 1 
ATOM   5611  C  CE1 . TYR B  1 300 ? 17.896  35.939  21.087  1.00 27.46 ? 299 TYR B CE1 1 
ATOM   5612  C  CE2 . TYR B  1 300 ? 17.239  38.197  21.426  1.00 27.79 ? 299 TYR B CE2 1 
ATOM   5613  C  CZ  . TYR B  1 300 ? 18.224  37.266  21.237  1.00 29.07 ? 299 TYR B CZ  1 
ATOM   5614  O  OH  . TYR B  1 300 ? 19.535  37.690  21.181  1.00 34.78 ? 299 TYR B OH  1 
ATOM   5615  N  N   . GLY B  1 301 ? 12.244  37.945  19.361  1.00 21.42 ? 300 GLY B N   1 
ATOM   5616  C  CA  . GLY B  1 301 ? 12.103  39.265  18.751  1.00 22.51 ? 300 GLY B CA  1 
ATOM   5617  C  C   . GLY B  1 301 ? 12.625  40.386  19.635  1.00 22.99 ? 300 GLY B C   1 
ATOM   5618  O  O   . GLY B  1 301 ? 12.521  40.328  20.876  1.00 23.15 ? 300 GLY B O   1 
ATOM   5619  N  N   . THR B  1 302 ? 13.144  41.429  18.990  1.00 24.54 ? 301 THR B N   1 
ATOM   5620  C  CA  . THR B  1 302 ? 13.556  42.645  19.670  1.00 24.86 ? 301 THR B CA  1 
ATOM   5621  C  C   . THR B  1 302 ? 13.064  43.847  18.895  1.00 25.66 ? 301 THR B C   1 
ATOM   5622  O  O   . THR B  1 302 ? 12.560  43.723  17.777  1.00 24.99 ? 301 THR B O   1 
ATOM   5623  C  CB  . THR B  1 302 ? 15.089  42.758  19.801  1.00 26.24 ? 301 THR B CB  1 
ATOM   5624  O  OG1 . THR B  1 302 ? 15.689  42.786  18.493  1.00 26.95 ? 301 THR B OG1 1 
ATOM   5625  C  CG2 . THR B  1 302 ? 15.632  41.608  20.596  1.00 26.02 ? 301 THR B CG2 1 
ATOM   5626  N  N   . GLY B  1 303 ? 13.215  45.019  19.506  1.00 26.49 ? 302 GLY B N   1 
ATOM   5627  C  CA  . GLY B  1 303 ? 12.913  46.290  18.834  1.00 27.93 ? 302 GLY B CA  1 
ATOM   5628  C  C   . GLY B  1 303 ? 11.436  46.624  18.781  1.00 28.73 ? 302 GLY B C   1 
ATOM   5629  O  O   . GLY B  1 303 ? 11.048  47.533  18.053  1.00 29.57 ? 302 GLY B O   1 
ATOM   5630  N  N   . VAL B  1 304 ? 10.609  45.891  19.528  1.00 25.00 ? 303 VAL B N   1 
ATOM   5631  C  CA  . VAL B  1 304 ? 9.187   46.145  19.565  1.00 25.52 ? 303 VAL B CA  1 
ATOM   5632  C  C   . VAL B  1 304 ? 8.862   46.571  20.994  1.00 24.48 ? 303 VAL B C   1 
ATOM   5633  O  O   . VAL B  1 304 ? 9.190   45.860  21.925  1.00 23.70 ? 303 VAL B O   1 
ATOM   5634  C  CB  . VAL B  1 304 ? 8.362   44.882  19.214  1.00 25.33 ? 303 VAL B CB  1 
ATOM   5635  C  CG1 . VAL B  1 304 ? 6.877   45.204  19.237  1.00 25.69 ? 303 VAL B CG1 1 
ATOM   5636  C  CG2 . VAL B  1 304 ? 8.789   44.321  17.855  1.00 25.78 ? 303 VAL B CG2 1 
ATOM   5637  N  N   . PRO B  1 305 ? 8.248   47.761  21.183  1.00 24.51 ? 304 PRO B N   1 
ATOM   5638  C  CA  . PRO B  1 305 ? 7.954   48.162  22.556  1.00 23.55 ? 304 PRO B CA  1 
ATOM   5639  C  C   . PRO B  1 305 ? 7.094   47.113  23.268  1.00 22.23 ? 304 PRO B C   1 
ATOM   5640  O  O   . PRO B  1 305 ? 6.068   46.683  22.741  1.00 21.68 ? 304 PRO B O   1 
ATOM   5641  C  CB  . PRO B  1 305 ? 7.208   49.495  22.382  1.00 24.30 ? 304 PRO B CB  1 
ATOM   5642  C  CG  . PRO B  1 305 ? 7.667   50.008  21.067  1.00 25.93 ? 304 PRO B CG  1 
ATOM   5643  C  CD  . PRO B  1 305 ? 7.767   48.768  20.222  1.00 25.55 ? 304 PRO B CD  1 
ATOM   5644  N  N   . THR B  1 306 ? 7.555   46.662  24.422  1.00 21.37 ? 305 THR B N   1 
ATOM   5645  C  CA  . THR B  1 306 ? 6.927   45.559  25.151  1.00 21.38 ? 305 THR B CA  1 
ATOM   5646  C  C   . THR B  1 306 ? 6.574   46.016  26.570  1.00 20.89 ? 305 THR B C   1 
ATOM   5647  O  O   . THR B  1 306 ? 7.450   46.500  27.277  1.00 20.60 ? 305 THR B O   1 
ATOM   5648  C  CB  . THR B  1 306 ? 7.900   44.379  25.216  1.00 20.83 ? 305 THR B CB  1 
ATOM   5649  O  OG1 . THR B  1 306 ? 8.335   44.081  23.874  1.00 21.34 ? 305 THR B OG1 1 
ATOM   5650  C  CG2 . THR B  1 306 ? 7.247   43.175  25.856  1.00 20.27 ? 305 THR B CG2 1 
ATOM   5651  N  N   . PRO B  1 307 ? 5.295   45.923  26.961  1.00 21.08 ? 306 PRO B N   1 
ATOM   5652  C  CA  . PRO B  1 307 ? 4.915   46.318  28.320  1.00 21.86 ? 306 PRO B CA  1 
ATOM   5653  C  C   . PRO B  1 307 ? 5.796   45.682  29.400  1.00 22.25 ? 306 PRO B C   1 
ATOM   5654  O  O   . PRO B  1 307 ? 6.025   44.461  29.386  1.00 19.49 ? 306 PRO B O   1 
ATOM   5655  C  CB  . PRO B  1 307 ? 3.472   45.817  28.441  1.00 22.28 ? 306 PRO B CB  1 
ATOM   5656  C  CG  . PRO B  1 307 ? 2.980   45.789  27.046  1.00 23.15 ? 306 PRO B CG  1 
ATOM   5657  C  CD  . PRO B  1 307 ? 4.163   45.280  26.263  1.00 23.12 ? 306 PRO B CD  1 
ATOM   5658  N  N   . ASP B  1 308 ? 6.322   46.535  30.271  1.00 23.04 ? 307 ASP B N   1 
ATOM   5659  C  CA  . ASP B  1 308 ? 7.278   46.179  31.310  1.00 26.64 ? 307 ASP B CA  1 
ATOM   5660  C  C   . ASP B  1 308 ? 6.692   46.419  32.722  1.00 24.64 ? 307 ASP B C   1 
ATOM   5661  O  O   . ASP B  1 308 ? 6.990   45.679  33.652  1.00 23.57 ? 307 ASP B O   1 
ATOM   5662  C  CB  . ASP B  1 308 ? 8.550   47.023  31.099  1.00 33.50 ? 307 ASP B CB  1 
ATOM   5663  C  CG  . ASP B  1 308 ? 9.457   47.058  32.313  1.00 41.46 ? 307 ASP B CG  1 
ATOM   5664  O  OD1 . ASP B  1 308 ? 10.313  46.149  32.425  1.00 50.55 ? 307 ASP B OD1 1 
ATOM   5665  O  OD2 . ASP B  1 308 ? 9.293   47.972  33.179  1.00 47.38 ? 307 ASP B OD2 1 
ATOM   5666  N  N   . SER B  1 309 ? 5.869   47.455  32.872  1.00 22.09 ? 308 SER B N   1 
ATOM   5667  C  CA  . SER B  1 309 ? 5.245   47.785  34.145  1.00 21.75 ? 308 SER B CA  1 
ATOM   5668  C  C   . SER B  1 309 ? 4.097   48.758  33.917  1.00 21.15 ? 308 SER B C   1 
ATOM   5669  O  O   . SER B  1 309 ? 3.955   49.309  32.818  1.00 20.13 ? 308 SER B O   1 
ATOM   5670  C  CB  . SER B  1 309 ? 6.242   48.392  35.131  1.00 22.89 ? 308 SER B CB  1 
ATOM   5671  O  OG  . SER B  1 309 ? 6.931   49.451  34.537  1.00 24.18 ? 308 SER B OG  1 
ATOM   5672  N  N   . PHE B  1 310 ? 3.248   48.891  34.940  1.00 19.66 ? 309 PHE B N   1 
ATOM   5673  C  CA  . PHE B  1 310 ? 1.938   49.534  34.821  1.00 19.76 ? 309 PHE B CA  1 
ATOM   5674  C  C   . PHE B  1 310 ? 1.714   50.447  35.993  1.00 21.32 ? 309 PHE B C   1 
ATOM   5675  O  O   . PHE B  1 310 ? 1.994   50.073  37.135  1.00 22.13 ? 309 PHE B O   1 
ATOM   5676  C  CB  . PHE B  1 310 ? 0.835   48.479  34.764  1.00 20.22 ? 309 PHE B CB  1 
ATOM   5677  C  CG  . PHE B  1 310 ? 1.060   47.452  33.698  1.00 19.78 ? 309 PHE B CG  1 
ATOM   5678  C  CD1 . PHE B  1 310 ? 0.700   47.717  32.383  1.00 20.34 ? 309 PHE B CD1 1 
ATOM   5679  C  CD2 . PHE B  1 310 ? 1.678   46.261  33.996  1.00 19.55 ? 309 PHE B CD2 1 
ATOM   5680  C  CE1 . PHE B  1 310 ? 0.962   46.804  31.375  1.00 20.52 ? 309 PHE B CE1 1 
ATOM   5681  C  CE2 . PHE B  1 310 ? 1.920   45.332  33.008  1.00 19.84 ? 309 PHE B CE2 1 
ATOM   5682  C  CZ  . PHE B  1 310 ? 1.554   45.608  31.690  1.00 19.47 ? 309 PHE B CZ  1 
ATOM   5683  N  N   . TYR B  1 311 ? 1.173   51.621  35.713  1.00 22.96 ? 310 TYR B N   1 
ATOM   5684  C  CA  . TYR B  1 311 ? 0.770   52.551  36.759  1.00 25.06 ? 310 TYR B CA  1 
ATOM   5685  C  C   . TYR B  1 311 ? -0.747  52.711  36.711  1.00 24.80 ? 310 TYR B C   1 
ATOM   5686  O  O   . TYR B  1 311 ? -1.301  53.121  35.699  1.00 24.69 ? 310 TYR B O   1 
ATOM   5687  C  CB  . TYR B  1 311 ? 1.443   53.896  36.591  1.00 28.04 ? 310 TYR B CB  1 
ATOM   5688  C  CG  . TYR B  1 311 ? 1.204   54.729  37.812  1.00 32.15 ? 310 TYR B CG  1 
ATOM   5689  C  CD1 . TYR B  1 311 ? 0.008   55.423  38.014  1.00 36.83 ? 310 TYR B CD1 1 
ATOM   5690  C  CD2 . TYR B  1 311 ? 2.150   54.741  38.819  1.00 34.73 ? 310 TYR B CD2 1 
ATOM   5691  C  CE1 . TYR B  1 311 ? -0.202  56.157  39.180  1.00 39.44 ? 310 TYR B CE1 1 
ATOM   5692  C  CE2 . TYR B  1 311 ? 1.954   55.462  39.978  1.00 38.64 ? 310 TYR B CE2 1 
ATOM   5693  C  CZ  . TYR B  1 311 ? 0.782   56.165  40.159  1.00 40.96 ? 310 TYR B CZ  1 
ATOM   5694  O  OH  . TYR B  1 311 ? 0.625   56.882  41.333  1.00 44.60 ? 310 TYR B OH  1 
ATOM   5695  N  N   . TYR B  1 312 ? -1.417  52.383  37.814  1.00 24.90 ? 311 TYR B N   1 
ATOM   5696  C  CA  . TYR B  1 312 ? -2.877  52.477  37.891  1.00 26.31 ? 311 TYR B CA  1 
ATOM   5697  C  C   . TYR B  1 312 ? -3.248  53.651  38.765  1.00 28.84 ? 311 TYR B C   1 
ATOM   5698  O  O   . TYR B  1 312 ? -2.893  53.692  39.927  1.00 30.50 ? 311 TYR B O   1 
ATOM   5699  C  CB  . TYR B  1 312 ? -3.473  51.224  38.494  1.00 25.83 ? 311 TYR B CB  1 
ATOM   5700  C  CG  . TYR B  1 312 ? -3.539  50.023  37.600  1.00 23.56 ? 311 TYR B CG  1 
ATOM   5701  C  CD1 . TYR B  1 312 ? -2.439  49.198  37.437  1.00 23.44 ? 311 TYR B CD1 1 
ATOM   5702  C  CD2 . TYR B  1 312 ? -4.715  49.697  36.932  1.00 23.83 ? 311 TYR B CD2 1 
ATOM   5703  C  CE1 . TYR B  1 312 ? -2.504  48.076  36.633  1.00 22.49 ? 311 TYR B CE1 1 
ATOM   5704  C  CE2 . TYR B  1 312 ? -4.803  48.586  36.126  1.00 22.78 ? 311 TYR B CE2 1 
ATOM   5705  C  CZ  . TYR B  1 312 ? -3.697  47.770  35.978  1.00 22.87 ? 311 TYR B CZ  1 
ATOM   5706  O  OH  . TYR B  1 312 ? -3.791  46.686  35.142  1.00 23.19 ? 311 TYR B OH  1 
ATOM   5707  N  N   . GLU B  1 313 ? -3.947  54.615  38.201  1.00 30.66 ? 312 GLU B N   1 
ATOM   5708  C  CA  . GLU B  1 313 ? -4.498  55.704  39.007  1.00 35.55 ? 312 GLU B CA  1 
ATOM   5709  C  C   . GLU B  1 313 ? -5.713  55.211  39.779  1.00 34.65 ? 312 GLU B C   1 
ATOM   5710  O  O   . GLU B  1 313 ? -6.006  55.712  40.849  1.00 36.27 ? 312 GLU B O   1 
ATOM   5711  C  CB  . GLU B  1 313 ? -4.837  56.900  38.117  1.00 38.01 ? 312 GLU B CB  1 
ATOM   5712  C  CG  . GLU B  1 313 ? -3.566  57.486  37.508  1.00 43.78 ? 312 GLU B CG  1 
ATOM   5713  C  CD  . GLU B  1 313 ? -3.801  58.475  36.376  1.00 48.88 ? 312 GLU B CD  1 
ATOM   5714  O  OE1 . GLU B  1 313 ? -4.937  58.981  36.218  1.00 52.56 ? 312 GLU B OE1 1 
ATOM   5715  O  OE2 . GLU B  1 313 ? -2.826  58.753  35.646  1.00 52.88 ? 312 GLU B OE2 1 
ATOM   5716  N  N   . SER B  1 314 ? -6.421  54.246  39.204  1.00 35.48 ? 313 SER B N   1 
ATOM   5717  C  CA  . SER B  1 314 ? -7.545  53.594  39.852  1.00 37.37 ? 313 SER B CA  1 
ATOM   5718  C  C   . SER B  1 314 ? -7.438  52.094  39.581  1.00 33.41 ? 313 SER B C   1 
ATOM   5719  O  O   . SER B  1 314 ? -7.561  51.650  38.437  1.00 36.40 ? 313 SER B O   1 
ATOM   5720  C  CB  . SER B  1 314 ? -8.864  54.153  39.296  1.00 39.84 ? 313 SER B CB  1 
ATOM   5721  O  OG  . SER B  1 314 ? -9.965  53.410  39.775  1.00 44.73 ? 313 SER B OG  1 
ATOM   5722  N  N   . PHE B  1 315 ? -7.237  51.320  40.635  1.00 31.19 ? 314 PHE B N   1 
ATOM   5723  C  CA  . PHE B  1 315 ? -6.918  49.899  40.517  1.00 29.82 ? 314 PHE B CA  1 
ATOM   5724  C  C   . PHE B  1 315 ? -8.041  49.082  41.146  1.00 30.73 ? 314 PHE B C   1 
ATOM   5725  O  O   . PHE B  1 315 ? -8.486  49.446  42.212  1.00 31.72 ? 314 PHE B O   1 
ATOM   5726  C  CB  . PHE B  1 315 ? -5.623  49.684  41.280  1.00 28.10 ? 314 PHE B CB  1 
ATOM   5727  C  CG  . PHE B  1 315 ? -5.130  48.270  41.305  1.00 26.86 ? 314 PHE B CG  1 
ATOM   5728  C  CD1 . PHE B  1 315 ? -4.438  47.760  40.243  1.00 26.69 ? 314 PHE B CD1 1 
ATOM   5729  C  CD2 . PHE B  1 315 ? -5.297  47.484  42.440  1.00 26.91 ? 314 PHE B CD2 1 
ATOM   5730  C  CE1 . PHE B  1 315 ? -3.945  46.472  40.273  1.00 26.09 ? 314 PHE B CE1 1 
ATOM   5731  C  CE2 . PHE B  1 315 ? -4.807  46.206  42.482  1.00 25.69 ? 314 PHE B CE2 1 
ATOM   5732  C  CZ  . PHE B  1 315 ? -4.129  45.697  41.402  1.00 26.13 ? 314 PHE B CZ  1 
ATOM   5733  N  N   . PRO B  1 316 ? -8.503  47.989  40.541  1.00 31.28 ? 315 PRO B N   1 
ATOM   5734  C  CA  . PRO B  1 316 ? -7.987  47.406  39.296  1.00 33.10 ? 315 PRO B CA  1 
ATOM   5735  C  C   . PRO B  1 316 ? -8.917  47.580  38.070  1.00 35.41 ? 315 PRO B C   1 
ATOM   5736  O  O   . PRO B  1 316 ? -8.694  46.937  37.055  1.00 37.07 ? 315 PRO B O   1 
ATOM   5737  C  CB  . PRO B  1 316 ? -7.954  45.918  39.638  1.00 32.01 ? 315 PRO B CB  1 
ATOM   5738  C  CG  . PRO B  1 316 ? -9.195  45.743  40.481  1.00 32.15 ? 315 PRO B CG  1 
ATOM   5739  C  CD  . PRO B  1 316 ? -9.358  47.031  41.272  1.00 32.48 ? 315 PRO B CD  1 
ATOM   5740  N  N   . ASP B  1 317 ? -9.970  48.384  38.160  1.00 37.09 ? 316 ASP B N   1 
ATOM   5741  C  CA  . ASP B  1 317 ? -11.022 48.347  37.119  1.00 41.67 ? 316 ASP B CA  1 
ATOM   5742  C  C   . ASP B  1 317 ? -10.894 49.436  36.049  1.00 45.88 ? 316 ASP B C   1 
ATOM   5743  O  O   . ASP B  1 317 ? -11.841 49.631  35.278  1.00 51.36 ? 316 ASP B O   1 
ATOM   5744  C  CB  . ASP B  1 317 ? -12.429 48.430  37.750  1.00 44.97 ? 316 ASP B CB  1 
ATOM   5745  C  CG  . ASP B  1 317 ? -12.814 47.170  38.528  1.00 46.70 ? 316 ASP B CG  1 
ATOM   5746  O  OD1 . ASP B  1 317 ? -12.272 46.069  38.279  1.00 44.89 ? 316 ASP B OD1 1 
ATOM   5747  O  OD2 . ASP B  1 317 ? -13.684 47.293  39.414  1.00 53.41 ? 316 ASP B OD2 1 
ATOM   5748  N  N   . ARG B  1 318 ? -9.761  50.136  36.005  1.00 42.75 ? 317 ARG B N   1 
ATOM   5749  C  CA  . ARG B  1 318 ? -9.483  51.126  34.971  1.00 44.70 ? 317 ARG B CA  1 
ATOM   5750  C  C   . ARG B  1 318 ? -8.157  50.773  34.306  1.00 40.70 ? 317 ARG B C   1 
ATOM   5751  O  O   . ARG B  1 318 ? -7.269  50.232  34.956  1.00 37.59 ? 317 ARG B O   1 
ATOM   5752  C  CB  . ARG B  1 318 ? -9.385  52.521  35.579  1.00 50.17 ? 317 ARG B CB  1 
ATOM   5753  C  CG  . ARG B  1 318 ? -10.706 53.190  35.891  1.00 57.94 ? 317 ARG B CG  1 
ATOM   5754  C  CD  . ARG B  1 318 ? -10.935 54.336  34.957  1.00 65.34 ? 317 ARG B CD  1 
ATOM   5755  N  NE  . ARG B  1 318 ? -9.866  55.321  35.109  1.00 70.79 ? 317 ARG B NE  1 
ATOM   5756  C  CZ  . ARG B  1 318 ? -9.788  56.239  36.073  1.00 74.73 ? 317 ARG B CZ  1 
ATOM   5757  N  NH1 . ARG B  1 318 ? -10.739 56.344  37.000  1.00 74.89 ? 317 ARG B NH1 1 
ATOM   5758  N  NH2 . ARG B  1 318 ? -8.749  57.070  36.106  1.00 76.87 ? 317 ARG B NH2 1 
ATOM   5759  N  N   . ASP B  1 319 ? -8.028  51.069  33.016  1.00 37.91 ? 318 ASP B N   1 
ATOM   5760  C  CA  . ASP B  1 319 ? -6.812  50.738  32.270  1.00 36.79 ? 318 ASP B CA  1 
ATOM   5761  C  C   . ASP B  1 319 ? -5.612  51.542  32.789  1.00 31.55 ? 318 ASP B C   1 
ATOM   5762  O  O   . ASP B  1 319 ? -5.754  52.696  33.150  1.00 32.00 ? 318 ASP B O   1 
ATOM   5763  C  CB  . ASP B  1 319 ? -6.990  51.001  30.773  1.00 41.43 ? 318 ASP B CB  1 
ATOM   5764  C  CG  . ASP B  1 319 ? -7.933  50.010  30.101  1.00 45.42 ? 318 ASP B CG  1 
ATOM   5765  O  OD1 . ASP B  1 319 ? -8.106  48.854  30.573  1.00 50.09 ? 318 ASP B OD1 1 
ATOM   5766  O  OD2 . ASP B  1 319 ? -8.507  50.383  29.064  1.00 51.70 ? 318 ASP B OD2 1 
ATOM   5767  N  N   . PRO B  1 320 ? -4.439  50.914  32.874  1.00 26.70 ? 319 PRO B N   1 
ATOM   5768  C  CA  . PRO B  1 320 ? -3.274  51.591  33.416  1.00 25.57 ? 319 PRO B CA  1 
ATOM   5769  C  C   . PRO B  1 320 ? -2.485  52.382  32.377  1.00 25.13 ? 319 PRO B C   1 
ATOM   5770  O  O   . PRO B  1 320 ? -2.692  52.193  31.181  1.00 24.76 ? 319 PRO B O   1 
ATOM   5771  C  CB  . PRO B  1 320 ? -2.423  50.432  33.915  1.00 24.74 ? 319 PRO B CB  1 
ATOM   5772  C  CG  . PRO B  1 320 ? -2.721  49.336  32.965  1.00 24.84 ? 319 PRO B CG  1 
ATOM   5773  C  CD  . PRO B  1 320 ? -4.176  49.483  32.633  1.00 25.90 ? 319 PRO B CD  1 
ATOM   5774  N  N   . LYS B  1 321 ? -1.596  53.249  32.854  1.00 24.24 ? 320 LYS B N   1 
ATOM   5775  C  CA  . LYS B  1 321 ? -0.529  53.814  32.027  1.00 24.31 ? 320 LYS B CA  1 
ATOM   5776  C  C   . LYS B  1 321 ? 0.560   52.774  31.911  1.00 22.95 ? 320 LYS B C   1 
ATOM   5777  O  O   . LYS B  1 321 ? 0.749   51.993  32.836  1.00 22.41 ? 320 LYS B O   1 
ATOM   5778  C  CB  . LYS B  1 321 ? 0.072   55.052  32.673  1.00 25.69 ? 320 LYS B CB  1 
ATOM   5779  C  CG  . LYS B  1 321 ? -0.913  56.099  33.154  1.00 27.85 ? 320 LYS B CG  1 
ATOM   5780  C  CD  . LYS B  1 321 ? -1.939  56.463  32.104  1.00 29.12 ? 320 LYS B CD  1 
ATOM   5781  C  CE  . LYS B  1 321 ? -2.989  57.332  32.767  1.00 31.32 ? 320 LYS B CE  1 
ATOM   5782  N  NZ  . LYS B  1 321 ? -3.974  57.732  31.763  1.00 33.77 ? 320 LYS B NZ  1 
ATOM   5783  N  N   . ILE B  1 322 ? 1.274   52.744  30.795  1.00 22.22 ? 321 ILE B N   1 
ATOM   5784  C  CA  . ILE B  1 322 ? 2.206   51.665  30.530  1.00 21.64 ? 321 ILE B CA  1 
ATOM   5785  C  C   . ILE B  1 322 ? 3.632   52.154  30.339  1.00 22.25 ? 321 ILE B C   1 
ATOM   5786  O  O   . ILE B  1 322 ? 3.874   53.137  29.619  1.00 22.12 ? 321 ILE B O   1 
ATOM   5787  C  CB  . ILE B  1 322 ? 1.762   50.849  29.291  1.00 22.36 ? 321 ILE B CB  1 
ATOM   5788  C  CG1 . ILE B  1 322 ? 0.334   50.308  29.473  1.00 23.50 ? 321 ILE B CG1 1 
ATOM   5789  C  CG2 . ILE B  1 322 ? 2.709   49.678  29.040  1.00 22.14 ? 321 ILE B CG2 1 
ATOM   5790  C  CD1 . ILE B  1 322 ? -0.208  49.565  28.261  1.00 25.63 ? 321 ILE B CD1 1 
ATOM   5791  N  N   . CYS B  1 323 ? 4.563   51.454  30.973  1.00 21.96 ? 322 CYS B N   1 
ATOM   5792  C  CA  A CYS B  1 323 ? 5.994   51.627  30.715  0.50 22.98 ? 322 CYS B CA  1 
ATOM   5793  C  CA  B CYS B  1 323 ? 6.006   51.614  30.714  0.50 23.15 ? 322 CYS B CA  1 
ATOM   5794  C  C   . CYS B  1 323 ? 6.481   50.465  29.831  1.00 22.88 ? 322 CYS B C   1 
ATOM   5795  O  O   . CYS B  1 323 ? 6.158   49.298  30.100  1.00 21.95 ? 322 CYS B O   1 
ATOM   5796  C  CB  A CYS B  1 323 ? 6.750   51.644  32.036  0.50 23.64 ? 322 CYS B CB  1 
ATOM   5797  C  CB  B CYS B  1 323 ? 6.806   51.571  32.014  0.50 24.00 ? 322 CYS B CB  1 
ATOM   5798  S  SG  A CYS B  1 323 ? 8.533   51.972  31.870  0.50 25.73 ? 322 CYS B SG  1 
ATOM   5799  S  SG  B CYS B  1 323 ? 6.713   53.092  32.950  0.50 26.60 ? 322 CYS B SG  1 
ATOM   5800  N  N   . PHE B  1 324 ? 7.256   50.775  28.794  1.00 23.16 ? 323 PHE B N   1 
ATOM   5801  C  CA  . PHE B  1 324 ? 7.678   49.785  27.816  1.00 23.40 ? 323 PHE B CA  1 
ATOM   5802  C  C   . PHE B  1 324 ? 9.168   49.494  27.898  1.00 24.38 ? 323 PHE B C   1 
ATOM   5803  O  O   . PHE B  1 324 ? 9.969   50.413  28.102  1.00 25.41 ? 323 PHE B O   1 
ATOM   5804  C  CB  . PHE B  1 324 ? 7.382   50.276  26.390  1.00 23.74 ? 323 PHE B CB  1 
ATOM   5805  C  CG  . PHE B  1 324 ? 5.920   50.443  26.099  1.00 23.47 ? 323 PHE B CG  1 
ATOM   5806  C  CD1 . PHE B  1 324 ? 5.180   49.379  25.671  1.00 23.04 ? 323 PHE B CD1 1 
ATOM   5807  C  CD2 . PHE B  1 324 ? 5.284   51.670  26.281  1.00 23.82 ? 323 PHE B CD2 1 
ATOM   5808  C  CE1 . PHE B  1 324 ? 3.825   49.495  25.404  1.00 23.41 ? 323 PHE B CE1 1 
ATOM   5809  C  CE2 . PHE B  1 324 ? 3.918   51.793  26.014  1.00 24.50 ? 323 PHE B CE2 1 
ATOM   5810  C  CZ  . PHE B  1 324 ? 3.189   50.703  25.581  1.00 23.90 ? 323 PHE B CZ  1 
ATOM   5811  N  N   . GLY B  1 325 ? 9.527   48.233  27.689  1.00 23.62 ? 324 GLY B N   1 
ATOM   5812  C  CA  . GLY B  1 325 ? 10.921  47.845  27.487  1.00 23.70 ? 324 GLY B CA  1 
ATOM   5813  C  C   . GLY B  1 325 ? 11.081  47.137  26.153  1.00 24.12 ? 324 GLY B C   1 
ATOM   5814  O  O   . GLY B  1 325 ? 10.222  47.224  25.283  1.00 23.94 ? 324 GLY B O   1 
ATOM   5815  N  N   . ASP B  1 326 ? 12.194  46.440  25.995  1.00 24.11 ? 325 ASP B N   1 
ATOM   5816  C  CA  . ASP B  1 326 ? 12.496  45.796  24.734  1.00 24.26 ? 325 ASP B CA  1 
ATOM   5817  C  C   . ASP B  1 326 ? 11.920  44.378  24.757  1.00 22.90 ? 325 ASP B C   1 
ATOM   5818  O  O   . ASP B  1 326 ? 11.608  43.828  25.818  1.00 23.05 ? 325 ASP B O   1 
ATOM   5819  C  CB  . ASP B  1 326 ? 14.008  45.798  24.502  1.00 25.93 ? 325 ASP B CB  1 
ATOM   5820  C  CG  . ASP B  1 326 ? 14.392  45.636  23.045  1.00 28.28 ? 325 ASP B CG  1 
ATOM   5821  O  OD1 . ASP B  1 326 ? 13.527  45.395  22.169  1.00 28.03 ? 325 ASP B OD1 1 
ATOM   5822  O  OD2 . ASP B  1 326 ? 15.600  45.786  22.771  1.00 30.87 ? 325 ASP B OD2 1 
ATOM   5823  N  N   . GLY B  1 327 ? 11.739  43.827  23.564  1.00 22.77 ? 326 GLY B N   1 
ATOM   5824  C  CA  . GLY B  1 327 ? 11.147  42.492  23.358  1.00 21.70 ? 326 GLY B CA  1 
ATOM   5825  C  C   . GLY B  1 327 ? 10.396  42.451  22.035  1.00 21.52 ? 326 GLY B C   1 
ATOM   5826  O  O   . GLY B  1 327 ? 10.742  43.189  21.088  1.00 20.90 ? 326 GLY B O   1 
ATOM   5827  N  N   . ASP B  1 328 ? 9.387   41.581  21.961  1.00 20.30 ? 327 ASP B N   1 
ATOM   5828  C  CA  . ASP B  1 328 ? 8.652   41.343  20.713  1.00 21.43 ? 327 ASP B CA  1 
ATOM   5829  C  C   . ASP B  1 328 ? 7.215   41.865  20.759  1.00 21.67 ? 327 ASP B C   1 
ATOM   5830  O  O   . ASP B  1 328 ? 6.415   41.542  19.881  1.00 21.91 ? 327 ASP B O   1 
ATOM   5831  C  CB  . ASP B  1 328 ? 8.680   39.849  20.324  1.00 21.06 ? 327 ASP B CB  1 
ATOM   5832  C  CG  . ASP B  1 328 ? 7.837   38.961  21.244  1.00 21.35 ? 327 ASP B CG  1 
ATOM   5833  O  OD1 . ASP B  1 328 ? 7.098   39.507  22.106  1.00 20.63 ? 327 ASP B OD1 1 
ATOM   5834  O  OD2 . ASP B  1 328 ? 7.903   37.706  21.088  1.00 21.53 ? 327 ASP B OD2 1 
ATOM   5835  N  N   . GLY B  1 329 ? 6.923   42.723  21.737  1.00 21.45 ? 328 GLY B N   1 
ATOM   5836  C  CA  . GLY B  1 329 ? 5.577   43.231  21.934  1.00 22.09 ? 328 GLY B CA  1 
ATOM   5837  C  C   . GLY B  1 329 ? 4.840   42.535  23.056  1.00 22.62 ? 328 GLY B C   1 
ATOM   5838  O  O   . GLY B  1 329 ? 3.962   43.125  23.659  1.00 23.27 ? 328 GLY B O   1 
ATOM   5839  N  N   . THR B  1 330 ? 5.212   41.291  23.349  1.00 21.69 ? 329 THR B N   1 
ATOM   5840  C  CA  . THR B  1 330 ? 4.570   40.468  24.382  1.00 22.60 ? 329 THR B CA  1 
ATOM   5841  C  C   . THR B  1 330 ? 5.617   39.910  25.338  1.00 21.90 ? 329 THR B C   1 
ATOM   5842  O  O   . THR B  1 330 ? 5.526   40.105  26.544  1.00 23.15 ? 329 THR B O   1 
ATOM   5843  C  CB  . THR B  1 330 ? 3.784   39.317  23.720  1.00 23.98 ? 329 THR B CB  1 
ATOM   5844  O  OG1 . THR B  1 330 ? 2.755   39.866  22.887  1.00 25.07 ? 329 THR B OG1 1 
ATOM   5845  C  CG2 . THR B  1 330 ? 3.169   38.388  24.736  1.00 26.12 ? 329 THR B CG2 1 
ATOM   5846  N  N   . VAL B  1 331 ? 6.613   39.221  24.800  1.00 20.48 ? 330 VAL B N   1 
ATOM   5847  C  CA  . VAL B  1 331 ? 7.675   38.626  25.575  1.00 19.80 ? 330 VAL B CA  1 
ATOM   5848  C  C   . VAL B  1 331 ? 8.803   39.626  25.793  1.00 20.28 ? 330 VAL B C   1 
ATOM   5849  O  O   . VAL B  1 331 ? 9.388   40.142  24.850  1.00 19.89 ? 330 VAL B O   1 
ATOM   5850  C  CB  . VAL B  1 331 ? 8.221   37.375  24.874  1.00 19.85 ? 330 VAL B CB  1 
ATOM   5851  C  CG1 . VAL B  1 331 ? 9.400   36.793  25.625  1.00 20.34 ? 330 VAL B CG1 1 
ATOM   5852  C  CG2 . VAL B  1 331 ? 7.106   36.350  24.722  1.00 20.00 ? 330 VAL B CG2 1 
ATOM   5853  N  N   . ASN B  1 332 ? 9.086   39.892  27.057  1.00 20.41 ? 331 ASN B N   1 
ATOM   5854  C  CA  . ASN B  1 332 ? 10.123  40.824  27.430  1.00 22.09 ? 331 ASN B CA  1 
ATOM   5855  C  C   . ASN B  1 332 ? 11.463  40.229  27.049  1.00 23.83 ? 331 ASN B C   1 
ATOM   5856  O  O   . ASN B  1 332 ? 11.664  39.004  27.157  1.00 22.77 ? 331 ASN B O   1 
ATOM   5857  C  CB  . ASN B  1 332 ? 10.046  41.110  28.937  1.00 21.99 ? 331 ASN B CB  1 
ATOM   5858  C  CG  . ASN B  1 332 ? 8.683   41.652  29.359  1.00 22.57 ? 331 ASN B CG  1 
ATOM   5859  O  OD1 . ASN B  1 332 ? 7.776   40.889  29.737  1.00 20.69 ? 331 ASN B OD1 1 
ATOM   5860  N  ND2 . ASN B  1 332 ? 8.536   42.968  29.314  1.00 22.42 ? 331 ASN B ND2 1 
ATOM   5861  N  N   . LEU B  1 333 ? 12.373  41.082  26.589  1.00 25.02 ? 332 LEU B N   1 
ATOM   5862  C  CA  . LEU B  1 333 ? 13.695  40.629  26.168  1.00 26.63 ? 332 LEU B CA  1 
ATOM   5863  C  C   . LEU B  1 333 ? 14.417  39.785  27.229  1.00 28.31 ? 332 LEU B C   1 
ATOM   5864  O  O   . LEU B  1 333 ? 15.074  38.794  26.894  1.00 29.56 ? 332 LEU B O   1 
ATOM   5865  C  CB  . LEU B  1 333 ? 14.575  41.809  25.799  1.00 28.05 ? 332 LEU B CB  1 
ATOM   5866  C  CG  . LEU B  1 333 ? 15.973  41.479  25.283  1.00 29.00 ? 332 LEU B CG  1 
ATOM   5867  C  CD1 . LEU B  1 333 ? 15.892  40.516  24.100  1.00 30.96 ? 332 LEU B CD1 1 
ATOM   5868  C  CD2 . LEU B  1 333 ? 16.689  42.759  24.906  1.00 30.63 ? 332 LEU B CD2 1 
ATOM   5869  N  N   . LYS B  1 334 ? 14.267  40.132  28.495  1.00 28.35 ? 333 LYS B N   1 
ATOM   5870  C  CA  . LYS B  1 334 ? 14.954  39.377  29.547  1.00 31.48 ? 333 LYS B CA  1 
ATOM   5871  C  C   . LYS B  1 334 ? 14.551  37.888  29.620  1.00 27.67 ? 333 LYS B C   1 
ATOM   5872  O  O   . LYS B  1 334 ? 15.320  37.083  30.056  1.00 26.55 ? 333 LYS B O   1 
ATOM   5873  C  CB  . LYS B  1 334 ? 14.814  40.082  30.913  1.00 38.10 ? 333 LYS B CB  1 
ATOM   5874  C  CG  . LYS B  1 334 ? 15.543  41.410  30.913  1.00 46.55 ? 333 LYS B CG  1 
ATOM   5875  C  CD  . LYS B  1 334 ? 15.405  42.098  32.258  1.00 54.08 ? 333 LYS B CD  1 
ATOM   5876  C  CE  . LYS B  1 334 ? 16.392  41.525  33.259  1.00 58.62 ? 333 LYS B CE  1 
ATOM   5877  N  NZ  . LYS B  1 334 ? 15.729  41.420  34.581  1.00 63.32 ? 333 LYS B NZ  1 
ATOM   5878  N  N   A SER B  1 335 ? 13.483  37.466  28.961  0.80 29.00 ? 334 SER B N   1 
ATOM   5879  N  N   B SER B  1 335 ? 13.282  37.617  29.292  0.20 23.05 ? 334 SER B N   1 
ATOM   5880  C  CA  A SER B  1 335 ? 13.339  35.990  28.699  0.80 28.00 ? 334 SER B CA  1 
ATOM   5881  C  CA  B SER B  1 335 ? 12.578  36.416  29.662  0.20 20.01 ? 334 SER B CA  1 
ATOM   5882  C  C   A SER B  1 335 ? 14.536  35.296  27.963  0.80 30.22 ? 334 SER B C   1 
ATOM   5883  C  C   B SER B  1 335 ? 13.019  35.514  28.573  0.20 18.29 ? 334 SER B C   1 
ATOM   5884  O  O   A SER B  1 335 ? 14.891  34.148  28.298  0.80 29.78 ? 334 SER B O   1 
ATOM   5885  O  O   B SER B  1 335 ? 13.443  34.396  28.806  0.20 17.93 ? 334 SER B O   1 
ATOM   5886  C  CB  A SER B  1 335 ? 12.031  35.703  27.991  0.80 28.05 ? 334 SER B CB  1 
ATOM   5887  C  CB  B SER B  1 335 ? 11.049  36.629  29.562  0.20 18.80 ? 334 SER B CB  1 
ATOM   5888  O  OG  A SER B  1 335 ? 10.930  35.973  28.868  0.80 28.21 ? 334 SER B OG  1 
ATOM   5889  O  OG  B SER B  1 335 ? 10.293  35.499  29.990  0.20 17.56 ? 334 SER B OG  1 
ATOM   5890  N  N   A ALA B  1 336 ? 15.159  35.959  26.982  0.80 28.27 ? 335 ALA B N   1 
ATOM   5891  N  N   B ALA B  1 336 ? 12.950  36.076  27.372  0.20 17.02 ? 335 ALA B N   1 
ATOM   5892  C  CA  A ALA B  1 336 ? 16.269  35.364  26.227  0.80 32.91 ? 335 ALA B CA  1 
ATOM   5893  C  CA  B ALA B  1 336 ? 13.423  35.429  26.177  0.20 16.54 ? 335 ALA B CA  1 
ATOM   5894  C  C   A ALA B  1 336 ? 17.500  35.015  27.075  0.80 33.59 ? 335 ALA B C   1 
ATOM   5895  C  C   B ALA B  1 336 ? 14.865  34.980  26.382  0.20 16.48 ? 335 ALA B C   1 
ATOM   5896  O  O   A ALA B  1 336 ? 18.268  34.141  26.704  0.80 35.19 ? 335 ALA B O   1 
ATOM   5897  O  O   B ALA B  1 336 ? 15.240  33.904  25.933  0.20 15.70 ? 335 ALA B O   1 
ATOM   5898  C  CB  A ALA B  1 336 ? 16.691  36.275  25.081  0.80 34.10 ? 335 ALA B CB  1 
ATOM   5899  C  CB  B ALA B  1 336 ? 13.313  36.390  25.011  0.20 16.83 ? 335 ALA B CB  1 
ATOM   5900  N  N   A LEU B  1 337 ? 17.685  35.678  28.206  0.80 34.68 ? 336 LEU B N   1 
ATOM   5901  N  N   B LEU B  1 337 ? 15.654  35.764  27.117  0.20 16.59 ? 336 LEU B N   1 
ATOM   5902  C  CA  A LEU B  1 337 ? 18.828  35.383  29.075  0.80 35.85 ? 336 LEU B CA  1 
ATOM   5903  C  CA  B LEU B  1 337 ? 17.096  35.507  27.197  0.20 17.58 ? 336 LEU B CA  1 
ATOM   5904  C  C   A LEU B  1 337 ? 18.721  33.960  29.605  0.80 34.57 ? 336 LEU B C   1 
ATOM   5905  C  C   B LEU B  1 337 ? 17.531  34.457  28.236  0.20 17.92 ? 336 LEU B C   1 
ATOM   5906  O  O   A LEU B  1 337 ? 19.738  33.354  29.949  0.80 33.75 ? 336 LEU B O   1 
ATOM   5907  O  O   B LEU B  1 337 ? 18.728  34.286  28.467  0.20 18.11 ? 336 LEU B O   1 
ATOM   5908  C  CB  A LEU B  1 337 ? 18.941  36.369  30.254  0.80 37.55 ? 336 LEU B CB  1 
ATOM   5909  C  CB  B LEU B  1 337 ? 17.868  36.814  27.414  0.20 18.12 ? 336 LEU B CB  1 
ATOM   5910  C  CG  A LEU B  1 337 ? 19.446  37.785  29.918  0.80 38.77 ? 336 LEU B CG  1 
ATOM   5911  C  CG  B LEU B  1 337 ? 18.105  37.664  26.159  0.20 18.62 ? 336 LEU B CG  1 
ATOM   5912  C  CD1 A LEU B  1 337 ? 19.271  38.729  31.098  0.80 39.73 ? 336 LEU B CD1 1 
ATOM   5913  C  CD1 B LEU B  1 337 ? 18.830  38.960  26.505  0.20 19.24 ? 336 LEU B CD1 1 
ATOM   5914  C  CD2 A LEU B  1 337 ? 20.897  37.754  29.470  0.80 40.62 ? 336 LEU B CD2 1 
ATOM   5915  C  CD2 B LEU B  1 337 ? 18.883  36.880  25.112  0.20 19.08 ? 336 LEU B CD2 1 
ATOM   5916  N  N   A GLN B  1 338 ? 17.493  33.441  29.704  0.80 33.15 ? 337 GLN B N   1 
ATOM   5917  N  N   B GLN B  1 338 ? 16.581  33.742  28.841  0.20 17.89 ? 337 GLN B N   1 
ATOM   5918  C  CA  A GLN B  1 338 ? 17.311  32.078  30.149  0.80 33.96 ? 337 GLN B CA  1 
ATOM   5919  C  CA  B GLN B  1 338 ? 16.927  32.647  29.762  0.20 18.76 ? 337 GLN B CA  1 
ATOM   5920  C  C   A GLN B  1 338 ? 17.951  31.116  29.166  0.80 32.83 ? 337 GLN B C   1 
ATOM   5921  C  C   B GLN B  1 338 ? 17.734  31.523  29.089  0.20 19.91 ? 337 GLN B C   1 
ATOM   5922  O  O   A GLN B  1 338 ? 18.722  30.259  29.575  0.80 34.36 ? 337 GLN B O   1 
ATOM   5923  O  O   B GLN B  1 338 ? 18.401  30.764  29.784  0.20 20.08 ? 337 GLN B O   1 
ATOM   5924  C  CB  A GLN B  1 338 ? 15.828  31.747  30.382  0.80 35.65 ? 337 GLN B CB  1 
ATOM   5925  C  CB  B GLN B  1 338 ? 15.674  32.008  30.383  0.20 17.95 ? 337 GLN B CB  1 
ATOM   5926  C  CG  A GLN B  1 338 ? 15.621  30.343  30.920  0.80 37.41 ? 337 GLN B CG  1 
ATOM   5927  C  CG  B GLN B  1 338 ? 14.996  32.740  31.523  0.20 17.71 ? 337 GLN B CG  1 
ATOM   5928  C  CD  A GLN B  1 338 ? 16.002  30.190  32.374  0.80 40.08 ? 337 GLN B CD  1 
ATOM   5929  C  CD  B GLN B  1 338 ? 15.933  33.526  32.419  0.20 18.29 ? 337 GLN B CD  1 
ATOM   5930  O  OE1 A GLN B  1 338 ? 16.462  31.135  33.055  0.80 40.28 ? 337 GLN B OE1 1 
ATOM   5931  O  OE1 B GLN B  1 338 ? 16.635  32.962  33.260  0.20 18.32 ? 337 GLN B OE1 1 
ATOM   5932  N  NE2 A GLN B  1 338 ? 15.800  28.972  32.868  0.80 42.05 ? 337 GLN B NE2 1 
ATOM   5933  N  NE2 B GLN B  1 338 ? 15.900  34.846  32.280  0.20 18.26 ? 337 GLN B NE2 1 
ATOM   5934  N  N   A CYS B  1 339 ? 17.677  31.231  27.866  0.80 32.25 ? 338 CYS B N   1 
ATOM   5935  N  N   B CYS B  1 339 ? 17.632  31.401  27.759  0.20 21.45 ? 338 CYS B N   1 
ATOM   5936  C  CA  A CYS B  1 339 ? 18.381  30.345  26.922  0.80 33.63 ? 338 CYS B CA  1 
ATOM   5937  C  CA  B CYS B  1 339 ? 18.406  30.422  26.939  0.20 23.44 ? 338 CYS B CA  1 
ATOM   5938  C  C   A CYS B  1 339 ? 19.888  30.553  26.987  0.80 30.93 ? 338 CYS B C   1 
ATOM   5939  C  C   B CYS B  1 339 ? 19.891  30.558  27.049  0.20 26.51 ? 338 CYS B C   1 
ATOM   5940  O  O   A CYS B  1 339 ? 20.634  29.592  26.878  0.80 30.58 ? 338 CYS B O   1 
ATOM   5941  O  O   B CYS B  1 339 ? 20.629  29.588  26.883  0.20 27.05 ? 338 CYS B O   1 
ATOM   5942  C  CB  A CYS B  1 339 ? 17.876  30.373  25.466  0.80 35.48 ? 338 CYS B CB  1 
ATOM   5943  C  CB  B CYS B  1 339 ? 18.149  30.668  25.460  0.20 23.13 ? 338 CYS B CB  1 
ATOM   5944  S  SG  A CYS B  1 339 ? 17.227  31.932  24.936  0.80 41.18 ? 338 CYS B SG  1 
ATOM   5945  S  SG  B CYS B  1 339 ? 16.436  30.737  24.976  0.20 20.75 ? 338 CYS B SG  1 
ATOM   5946  N  N   . GLN B  1 340 ? 20.342  31.786  27.231  1.00 30.91 ? 339 GLN B N   1 
ATOM   5947  C  CA  . GLN B  1 340 ? 21.777  32.033  27.356  1.00 34.00 ? 339 GLN B CA  1 
ATOM   5948  C  C   . GLN B  1 340 ? 22.356  31.265  28.545  1.00 32.92 ? 339 GLN B C   1 
ATOM   5949  O  O   . GLN B  1 340 ? 23.442  30.696  28.454  1.00 35.99 ? 339 GLN B O   1 
ATOM   5950  C  CB  . GLN B  1 340 ? 22.065  33.520  27.461  1.00 38.96 ? 339 GLN B CB  1 
ATOM   5951  C  CG  . GLN B  1 340 ? 23.539  33.843  27.529  1.00 45.08 ? 339 GLN B CG  1 
ATOM   5952  C  CD  . GLN B  1 340 ? 23.770  35.334  27.651  1.00 51.27 ? 339 GLN B CD  1 
ATOM   5953  O  OE1 . GLN B  1 340 ? 23.298  35.975  28.600  1.00 54.76 ? 339 GLN B OE1 1 
ATOM   5954  N  NE2 . GLN B  1 340 ? 24.497  35.899  26.695  1.00 56.44 ? 339 GLN B NE2 1 
ATOM   5955  N  N   . ALA B  1 341 ? 21.620  31.220  29.649  1.00 31.45 ? 340 ALA B N   1 
ATOM   5956  C  CA  . ALA B  1 341 ? 22.075  30.505  30.842  1.00 31.47 ? 340 ALA B CA  1 
ATOM   5957  C  C   . ALA B  1 341 ? 22.211  28.995  30.577  1.00 31.63 ? 340 ALA B C   1 
ATOM   5958  O  O   . ALA B  1 341 ? 23.057  28.335  31.170  1.00 30.00 ? 340 ALA B O   1 
ATOM   5959  C  CB  . ALA B  1 341 ? 21.124  30.763  32.002  1.00 32.14 ? 340 ALA B CB  1 
ATOM   5960  N  N   . TRP B  1 342 ? 21.367  28.451  29.697  1.00 28.47 ? 341 TRP B N   1 
ATOM   5961  C  CA  . TRP B  1 342 ? 21.420  27.023  29.401  1.00 28.52 ? 341 TRP B CA  1 
ATOM   5962  C  C   . TRP B  1 342 ? 22.674  26.592  28.627  1.00 31.25 ? 341 TRP B C   1 
ATOM   5963  O  O   . TRP B  1 342 ? 23.080  25.448  28.720  1.00 31.11 ? 341 TRP B O   1 
ATOM   5964  C  CB  . TRP B  1 342 ? 20.179  26.594  28.643  1.00 27.19 ? 341 TRP B CB  1 
ATOM   5965  C  CG  . TRP B  1 342 ? 18.909  26.633  29.456  1.00 25.54 ? 341 TRP B CG  1 
ATOM   5966  C  CD1 . TRP B  1 342 ? 18.775  26.487  30.826  1.00 25.93 ? 341 TRP B CD1 1 
ATOM   5967  C  CD2 . TRP B  1 342 ? 17.588  26.792  28.942  1.00 24.53 ? 341 TRP B CD2 1 
ATOM   5968  N  NE1 . TRP B  1 342 ? 17.428  26.555  31.170  1.00 25.25 ? 341 TRP B NE1 1 
ATOM   5969  C  CE2 . TRP B  1 342 ? 16.693  26.746  30.033  1.00 23.43 ? 341 TRP B CE2 1 
ATOM   5970  C  CE3 . TRP B  1 342 ? 17.076  26.973  27.662  1.00 24.93 ? 341 TRP B CE3 1 
ATOM   5971  C  CZ2 . TRP B  1 342 ? 15.324  26.899  29.874  1.00 23.63 ? 341 TRP B CZ2 1 
ATOM   5972  C  CZ3 . TRP B  1 342 ? 15.710  27.119  27.510  1.00 24.29 ? 341 TRP B CZ3 1 
ATOM   5973  C  CH2 . TRP B  1 342 ? 14.857  27.076  28.607  1.00 23.83 ? 341 TRP B CH2 1 
ATOM   5974  N  N   . GLN B  1 343 ? 23.296  27.505  27.897  1.00 35.81 ? 342 GLN B N   1 
ATOM   5975  C  CA  . GLN B  1 343 ? 24.526  27.190  27.158  1.00 41.30 ? 342 GLN B CA  1 
ATOM   5976  C  C   . GLN B  1 343 ? 25.594  26.491  28.011  1.00 42.83 ? 342 GLN B C   1 
ATOM   5977  O  O   . GLN B  1 343 ? 26.257  25.572  27.543  1.00 43.47 ? 342 GLN B O   1 
ATOM   5978  C  CB  . GLN B  1 343 ? 25.138  28.454  26.566  1.00 46.07 ? 342 GLN B CB  1 
ATOM   5979  C  CG  . GLN B  1 343 ? 24.302  29.113  25.483  1.00 49.72 ? 342 GLN B CG  1 
ATOM   5980  C  CD  . GLN B  1 343 ? 25.044  30.264  24.815  1.00 55.01 ? 342 GLN B CD  1 
ATOM   5981  O  OE1 . GLN B  1 343 ? 25.509  31.186  25.481  1.00 56.84 ? 342 GLN B OE1 1 
ATOM   5982  N  NE2 . GLN B  1 343 ? 25.154  30.213  23.490  1.00 56.52 ? 342 GLN B NE2 1 
ATOM   5983  N  N   . SER B  1 344 ? 25.772  26.929  29.254  1.00 42.65 ? 343 SER B N   1 
ATOM   5984  C  CA  . SER B  1 344 ? 26.814  26.359  30.093  1.00 46.22 ? 343 SER B CA  1 
ATOM   5985  C  C   . SER B  1 344 ? 26.326  25.172  30.924  1.00 45.55 ? 343 SER B C   1 
ATOM   5986  O  O   . SER B  1 344 ? 27.128  24.536  31.598  1.00 45.89 ? 343 SER B O   1 
ATOM   5987  C  CB  . SER B  1 344 ? 27.423  27.433  30.995  1.00 48.70 ? 343 SER B CB  1 
ATOM   5988  O  OG  . SER B  1 344 ? 26.478  27.887  31.943  1.00 49.64 ? 343 SER B OG  1 
ATOM   5989  N  N   . ARG B  1 345 ? 25.036  24.849  30.847  1.00 40.22 ? 344 ARG B N   1 
ATOM   5990  C  CA  . ARG B  1 345 ? 24.460  23.771  31.646  1.00 41.40 ? 344 ARG B CA  1 
ATOM   5991  C  C   . ARG B  1 345 ? 24.145  22.483  30.871  1.00 39.50 ? 344 ARG B C   1 
ATOM   5992  O  O   . ARG B  1 345 ? 23.689  21.505  31.460  1.00 39.48 ? 344 ARG B O   1 
ATOM   5993  C  CB  . ARG B  1 345 ? 23.181  24.270  32.316  1.00 42.66 ? 344 ARG B CB  1 
ATOM   5994  C  CG  . ARG B  1 345 ? 23.432  25.313  33.391  1.00 45.47 ? 344 ARG B CG  1 
ATOM   5995  C  CD  . ARG B  1 345 ? 22.118  25.842  33.932  1.00 47.88 ? 344 ARG B CD  1 
ATOM   5996  N  NE  . ARG B  1 345 ? 22.310  27.108  34.638  1.00 52.05 ? 344 ARG B NE  1 
ATOM   5997  C  CZ  . ARG B  1 345 ? 21.389  28.062  34.767  1.00 53.71 ? 344 ARG B CZ  1 
ATOM   5998  N  NH1 . ARG B  1 345 ? 20.168  27.927  34.237  1.00 51.48 ? 344 ARG B NH1 1 
ATOM   5999  N  NH2 . ARG B  1 345 ? 21.701  29.175  35.429  1.00 56.07 ? 344 ARG B NH2 1 
ATOM   6000  N  N   . GLN B  1 346 ? 24.297  22.493  29.553  1.00 37.39 ? 345 GLN B N   1 
ATOM   6001  C  CA  . GLN B  1 346 ? 24.047  21.281  28.771  1.00 34.83 ? 345 GLN B CA  1 
ATOM   6002  C  C   . GLN B  1 346 ? 25.153  21.136  27.748  1.00 35.07 ? 345 GLN B C   1 
ATOM   6003  O  O   . GLN B  1 346 ? 25.762  22.137  27.359  1.00 32.92 ? 345 GLN B O   1 
ATOM   6004  C  CB  . GLN B  1 346 ? 22.634  21.277  28.130  1.00 33.37 ? 345 GLN B CB  1 
ATOM   6005  C  CG  . GLN B  1 346 ? 22.344  22.374  27.121  1.00 31.90 ? 345 GLN B CG  1 
ATOM   6006  C  CD  . GLN B  1 346 ? 21.075  22.132  26.328  1.00 30.71 ? 345 GLN B CD  1 
ATOM   6007  O  OE1 . GLN B  1 346 ? 20.000  21.910  26.885  1.00 30.67 ? 345 GLN B OE1 1 
ATOM   6008  N  NE2 . GLN B  1 346 ? 21.182  22.220  25.006  1.00 31.03 ? 345 GLN B NE2 1 
ATOM   6009  N  N   . GLU B  1 347 ? 25.402  19.897  27.332  1.00 35.71 ? 346 GLU B N   1 
ATOM   6010  C  CA  . GLU B  1 347 ? 26.369  19.603  26.270  1.00 38.97 ? 346 GLU B CA  1 
ATOM   6011  C  C   . GLU B  1 347 ? 25.852  19.897  24.868  1.00 35.99 ? 346 GLU B C   1 
ATOM   6012  O  O   . GLU B  1 347 ? 26.610  20.319  24.002  1.00 35.88 ? 346 GLU B O   1 
ATOM   6013  C  CB  . GLU B  1 347 ? 26.872  18.162  26.303  1.00 45.06 ? 346 GLU B CB  1 
ATOM   6014  C  CG  . GLU B  1 347 ? 27.772  17.865  27.486  1.00 53.41 ? 346 GLU B CG  1 
ATOM   6015  C  CD  . GLU B  1 347 ? 28.199  16.402  27.561  1.00 59.89 ? 346 GLU B CD  1 
ATOM   6016  O  OE1 . GLU B  1 347 ? 27.485  15.520  27.017  1.00 66.53 ? 346 GLU B OE1 1 
ATOM   6017  O  OE2 . GLU B  1 347 ? 29.252  16.136  28.177  1.00 65.35 ? 346 GLU B OE2 1 
ATOM   6018  N  N   . HIS B  1 348 ? 24.574  19.645  24.616  1.00 32.81 ? 347 HIS B N   1 
ATOM   6019  C  CA  A HIS B  1 348 ? 23.986  19.981  23.319  0.70 31.98 ? 347 HIS B CA  1 
ATOM   6020  C  CA  B HIS B  1 348 ? 23.988  19.986  23.321  0.30 31.60 ? 347 HIS B CA  1 
ATOM   6021  C  C   . HIS B  1 348 ? 24.057  21.486  23.073  1.00 30.44 ? 347 HIS B C   1 
ATOM   6022  O  O   . HIS B  1 348 ? 23.948  22.278  24.004  1.00 29.18 ? 347 HIS B O   1 
ATOM   6023  C  CB  A HIS B  1 348 ? 22.523  19.530  23.230  0.70 31.25 ? 347 HIS B CB  1 
ATOM   6024  C  CB  B HIS B  1 348 ? 22.542  19.494  23.225  0.30 30.60 ? 347 HIS B CB  1 
ATOM   6025  C  CG  A HIS B  1 348 ? 22.358  18.060  23.038  0.70 32.66 ? 347 HIS B CG  1 
ATOM   6026  C  CG  B HIS B  1 348 ? 22.450  18.014  22.984  0.30 31.13 ? 347 HIS B CG  1 
ATOM   6027  N  ND1 A HIS B  1 348 ? 22.467  17.170  24.079  0.70 33.66 ? 347 HIS B ND1 1 
ATOM   6028  N  ND1 B HIS B  1 348 ? 22.661  17.452  21.742  0.30 31.90 ? 347 HIS B ND1 1 
ATOM   6029  C  CD2 A HIS B  1 348 ? 22.081  17.322  21.936  0.70 34.18 ? 347 HIS B CD2 1 
ATOM   6030  C  CD2 B HIS B  1 348 ? 22.227  16.979  23.830  0.30 31.41 ? 347 HIS B CD2 1 
ATOM   6031  C  CE1 A HIS B  1 348 ? 22.276  15.942  23.632  0.70 34.85 ? 347 HIS B CE1 1 
ATOM   6032  C  CE1 B HIS B  1 348 ? 22.547  16.138  21.827  0.30 31.91 ? 347 HIS B CE1 1 
ATOM   6033  N  NE2 A HIS B  1 348 ? 22.042  16.006  22.333  0.70 35.17 ? 347 HIS B NE2 1 
ATOM   6034  N  NE2 B HIS B  1 348 ? 22.282  15.824  23.083  0.30 32.08 ? 347 HIS B NE2 1 
ATOM   6035  N  N   . GLN B  1 349 ? 24.211  21.861  21.810  1.00 30.41 ? 348 GLN B N   1 
ATOM   6036  C  CA  . GLN B  1 349 ? 24.337  23.269  21.448  1.00 32.97 ? 348 GLN B CA  1 
ATOM   6037  C  C   . GLN B  1 349 ? 23.068  24.057  21.722  1.00 28.76 ? 348 GLN B C   1 
ATOM   6038  O  O   . GLN B  1 349 ? 21.955  23.547  21.541  1.00 27.08 ? 348 GLN B O   1 
ATOM   6039  C  CB  . GLN B  1 349 ? 24.641  23.441  19.965  1.00 35.42 ? 348 GLN B CB  1 
ATOM   6040  C  CG  . GLN B  1 349 ? 25.917  22.830  19.468  1.00 42.49 ? 348 GLN B CG  1 
ATOM   6041  C  CD  . GLN B  1 349 ? 26.049  23.075  17.978  1.00 47.18 ? 348 GLN B CD  1 
ATOM   6042  O  OE1 . GLN B  1 349 ? 26.201  24.220  17.542  1.00 52.33 ? 348 GLN B OE1 1 
ATOM   6043  N  NE2 . GLN B  1 349 ? 25.927  22.017  17.190  1.00 49.83 ? 348 GLN B NE2 1 
ATOM   6044  N  N   . VAL B  1 350 ? 23.254  25.305  22.135  1.00 27.59 ? 349 VAL B N   1 
ATOM   6045  C  CA  . VAL B  1 350 ? 22.179  26.280  22.245  1.00 27.10 ? 349 VAL B CA  1 
ATOM   6046  C  C   . VAL B  1 350 ? 22.548  27.427  21.308  1.00 28.44 ? 349 VAL B C   1 
ATOM   6047  O  O   . VAL B  1 350 ? 23.578  28.070  21.509  1.00 27.93 ? 349 VAL B O   1 
ATOM   6048  C  CB  . VAL B  1 350 ? 22.010  26.797  23.690  1.00 27.40 ? 349 VAL B CB  1 
ATOM   6049  C  CG1 . VAL B  1 350 ? 20.926  27.882  23.772  1.00 26.18 ? 349 VAL B CG1 1 
ATOM   6050  C  CG2 . VAL B  1 350 ? 21.703  25.654  24.663  1.00 27.05 ? 349 VAL B CG2 1 
ATOM   6051  N  N   A LEU B  1 351 ? 21.730  27.661  20.282  0.50 28.12 ? 350 LEU B N   1 
ATOM   6052  N  N   B LEU B  1 351 ? 21.729  27.661  20.285  0.50 27.56 ? 350 LEU B N   1 
ATOM   6053  C  CA  A LEU B  1 351 ? 21.964  28.760  19.339  0.50 29.91 ? 350 LEU B CA  1 
ATOM   6054  C  CA  B LEU B  1 351 ? 21.965  28.752  19.340  0.50 28.93 ? 350 LEU B CA  1 
ATOM   6055  C  C   A LEU B  1 351 ? 20.939  29.848  19.609  0.50 29.55 ? 350 LEU B C   1 
ATOM   6056  C  C   B LEU B  1 351 ? 20.939  29.847  19.605  0.50 28.99 ? 350 LEU B C   1 
ATOM   6057  O  O   A LEU B  1 351 ? 19.739  29.576  19.644  0.50 28.50 ? 350 LEU B O   1 
ATOM   6058  O  O   B LEU B  1 351 ? 19.740  29.577  19.644  0.50 27.97 ? 350 LEU B O   1 
ATOM   6059  C  CB  A LEU B  1 351 ? 21.825  28.295  17.890  0.50 31.14 ? 350 LEU B CB  1 
ATOM   6060  C  CB  B LEU B  1 351 ? 21.840  28.256  17.901  0.50 29.47 ? 350 LEU B CB  1 
ATOM   6061  C  CG  A LEU B  1 351 ? 22.697  27.135  17.410  0.50 33.24 ? 350 LEU B CG  1 
ATOM   6062  C  CG  B LEU B  1 351 ? 22.728  27.055  17.489  0.50 30.76 ? 350 LEU B CG  1 
ATOM   6063  C  CD1 A LEU B  1 351 ? 24.136  27.311  17.862  0.50 34.58 ? 350 LEU B CD1 1 
ATOM   6064  C  CD1 B LEU B  1 351 ? 22.069  25.734  17.868  0.50 31.48 ? 350 LEU B CD1 1 
ATOM   6065  C  CD2 A LEU B  1 351 ? 22.085  25.849  17.938  0.50 34.02 ? 350 LEU B CD2 1 
ATOM   6066  C  CD2 B LEU B  1 351 ? 23.026  27.043  16.005  0.50 30.59 ? 350 LEU B CD2 1 
ATOM   6067  N  N   . LEU B  1 352 ? 21.408  31.074  19.799  1.00 29.28 ? 351 LEU B N   1 
ATOM   6068  C  CA  . LEU B  1 352 ? 20.523  32.214  19.997  1.00 30.12 ? 351 LEU B CA  1 
ATOM   6069  C  C   . LEU B  1 352 ? 20.392  32.976  18.698  1.00 30.66 ? 351 LEU B C   1 
ATOM   6070  O  O   . LEU B  1 352 ? 21.385  33.198  18.018  1.00 32.84 ? 351 LEU B O   1 
ATOM   6071  C  CB  . LEU B  1 352 ? 21.045  33.122  21.104  1.00 32.16 ? 351 LEU B CB  1 
ATOM   6072  C  CG  . LEU B  1 352 ? 20.405  32.833  22.469  1.00 34.06 ? 351 LEU B CG  1 
ATOM   6073  C  CD1 . LEU B  1 352 ? 20.905  31.518  23.039  1.00 35.60 ? 351 LEU B CD1 1 
ATOM   6074  C  CD2 . LEU B  1 352 ? 20.684  33.972  23.437  1.00 36.26 ? 351 LEU B CD2 1 
ATOM   6075  N  N   . GLN B  1 353 ? 19.170  33.323  18.317  1.00 27.48 ? 352 GLN B N   1 
ATOM   6076  C  CA  . GLN B  1 353 ? 18.956  34.091  17.108  1.00 27.47 ? 352 GLN B CA  1 
ATOM   6077  C  C   . GLN B  1 353 ? 18.009  35.255  17.368  1.00 26.67 ? 352 GLN B C   1 
ATOM   6078  O  O   . GLN B  1 353 ? 16.802  35.060  17.532  1.00 24.69 ? 352 GLN B O   1 
ATOM   6079  C  CB  . GLN B  1 353 ? 18.418  33.214  15.974  1.00 27.79 ? 352 GLN B CB  1 
ATOM   6080  C  CG  . GLN B  1 353 ? 18.141  33.991  14.685  1.00 29.32 ? 352 GLN B CG  1 
ATOM   6081  C  CD  . GLN B  1 353 ? 19.408  34.569  14.115  1.00 31.12 ? 352 GLN B CD  1 
ATOM   6082  O  OE1 . GLN B  1 353 ? 20.291  33.824  13.719  1.00 33.99 ? 352 GLN B OE1 1 
ATOM   6083  N  NE2 . GLN B  1 353 ? 19.525  35.890  14.098  1.00 32.07 ? 352 GLN B NE2 1 
ATOM   6084  N  N   . GLU B  1 354 ? 18.570  36.455  17.374  1.00 26.87 ? 353 GLU B N   1 
ATOM   6085  C  CA  . GLU B  1 354 ? 17.792  37.668  17.458  1.00 27.91 ? 353 GLU B CA  1 
ATOM   6086  C  C   . GLU B  1 354 ? 17.032  37.936  16.149  1.00 27.33 ? 353 GLU B C   1 
ATOM   6087  O  O   . GLU B  1 354 ? 17.570  37.733  15.051  1.00 27.75 ? 353 GLU B O   1 
ATOM   6088  C  CB  . GLU B  1 354 ? 18.708  38.849  17.780  1.00 29.90 ? 353 GLU B CB  1 
ATOM   6089  C  CG  . GLU B  1 354 ? 17.947  40.090  18.181  1.00 31.46 ? 353 GLU B CG  1 
ATOM   6090  C  CD  . GLU B  1 354 ? 18.821  41.320  18.309  1.00 34.56 ? 353 GLU B CD  1 
ATOM   6091  O  OE1 . GLU B  1 354 ? 20.051  41.195  18.171  1.00 37.84 ? 353 GLU B OE1 1 
ATOM   6092  O  OE2 . GLU B  1 354 ? 18.264  42.421  18.507  1.00 34.86 ? 353 GLU B OE2 1 
ATOM   6093  N  N   . LEU B  1 355 ? 15.793  38.389  16.288  1.00 25.71 ? 354 LEU B N   1 
ATOM   6094  C  CA  . LEU B  1 355 ? 14.938  38.782  15.168  1.00 26.57 ? 354 LEU B CA  1 
ATOM   6095  C  C   . LEU B  1 355 ? 14.526  40.242  15.362  1.00 27.25 ? 354 LEU B C   1 
ATOM   6096  O  O   . LEU B  1 355 ? 13.455  40.517  15.922  1.00 26.02 ? 354 LEU B O   1 
ATOM   6097  C  CB  . LEU B  1 355 ? 13.695  37.886  15.098  1.00 26.26 ? 354 LEU B CB  1 
ATOM   6098  C  CG  . LEU B  1 355 ? 13.973  36.367  15.013  1.00 26.85 ? 354 LEU B CG  1 
ATOM   6099  C  CD1 . LEU B  1 355 ? 12.678  35.578  15.171  1.00 26.99 ? 354 LEU B CD1 1 
ATOM   6100  C  CD2 . LEU B  1 355 ? 14.683  36.014  13.724  1.00 27.74 ? 354 LEU B CD2 1 
ATOM   6101  N  N   . PRO B  1 356 ? 15.388  41.180  14.946  1.00 28.98 ? 355 PRO B N   1 
ATOM   6102  C  CA  . PRO B  1 356 ? 15.078  42.581  15.218  1.00 30.27 ? 355 PRO B CA  1 
ATOM   6103  C  C   . PRO B  1 356 ? 13.873  43.043  14.405  1.00 30.03 ? 355 PRO B C   1 
ATOM   6104  O  O   . PRO B  1 356 ? 13.802  42.795  13.213  1.00 30.10 ? 355 PRO B O   1 
ATOM   6105  C  CB  . PRO B  1 356 ? 16.352  43.341  14.828  1.00 31.79 ? 355 PRO B CB  1 
ATOM   6106  C  CG  . PRO B  1 356 ? 17.331  42.328  14.374  1.00 32.34 ? 355 PRO B CG  1 
ATOM   6107  C  CD  . PRO B  1 356 ? 16.648  41.007  14.208  1.00 30.86 ? 355 PRO B CD  1 
ATOM   6108  N  N   . GLY B  1 357 ? 12.928  43.664  15.088  1.00 30.14 ? 356 GLY B N   1 
ATOM   6109  C  CA  . GLY B  1 357 ? 11.717  44.171  14.475  1.00 31.21 ? 356 GLY B CA  1 
ATOM   6110  C  C   . GLY B  1 357 ? 10.646  43.117  14.271  1.00 30.75 ? 356 GLY B C   1 
ATOM   6111  O  O   . GLY B  1 357 ? 9.669   43.372  13.581  1.00 32.57 ? 356 GLY B O   1 
ATOM   6112  N  N   . SER B  1 358 ? 10.818  41.924  14.837  1.00 29.23 ? 357 SER B N   1 
ATOM   6113  C  CA  . SER B  1 358 ? 9.855   40.849  14.613  1.00 28.75 ? 357 SER B CA  1 
ATOM   6114  C  C   . SER B  1 358 ? 8.859   40.755  15.779  1.00 27.21 ? 357 SER B C   1 
ATOM   6115  O  O   . SER B  1 358 ? 9.226   40.432  16.900  1.00 26.00 ? 357 SER B O   1 
ATOM   6116  C  CB  . SER B  1 358 ? 10.587  39.523  14.401  1.00 29.58 ? 357 SER B CB  1 
ATOM   6117  O  OG  . SER B  1 358 ? 9.693   38.492  14.033  1.00 31.68 ? 357 SER B OG  1 
ATOM   6118  N  N   . GLU B  1 359 ? 7.595   41.046  15.498  1.00 26.53 ? 358 GLU B N   1 
ATOM   6119  C  CA  . GLU B  1 359 ? 6.554   41.020  16.518  1.00 26.53 ? 358 GLU B CA  1 
ATOM   6120  C  C   . GLU B  1 359 ? 6.125   39.579  16.863  1.00 24.88 ? 358 GLU B C   1 
ATOM   6121  O  O   . GLU B  1 359 ? 6.229   38.652  16.044  1.00 24.52 ? 358 GLU B O   1 
ATOM   6122  C  CB  . GLU B  1 359 ? 5.369   41.894  16.079  1.00 28.71 ? 358 GLU B CB  1 
ATOM   6123  C  CG  . GLU B  1 359 ? 4.252   42.088  17.092  1.00 30.73 ? 358 GLU B CG  1 
ATOM   6124  C  CD  . GLU B  1 359 ? 3.235   40.952  17.093  1.00 32.65 ? 358 GLU B CD  1 
ATOM   6125  O  OE1 . GLU B  1 359 ? 3.046   40.311  16.030  1.00 34.35 ? 358 GLU B OE1 1 
ATOM   6126  O  OE2 . GLU B  1 359 ? 2.616   40.702  18.162  1.00 32.96 ? 358 GLU B OE2 1 
ATOM   6127  N  N   . HIS B  1 360 ? 5.638   39.424  18.089  1.00 23.21 ? 359 HIS B N   1 
ATOM   6128  C  CA  . HIS B  1 360 ? 5.363   38.133  18.688  1.00 22.69 ? 359 HIS B CA  1 
ATOM   6129  C  C   . HIS B  1 360 ? 4.577   37.154  17.801  1.00 23.07 ? 359 HIS B C   1 
ATOM   6130  O  O   . HIS B  1 360 ? 4.940   35.986  17.700  1.00 23.15 ? 359 HIS B O   1 
ATOM   6131  C  CB  . HIS B  1 360 ? 4.597   38.340  19.998  1.00 22.26 ? 359 HIS B CB  1 
ATOM   6132  C  CG  . HIS B  1 360 ? 4.443   37.086  20.802  1.00 21.21 ? 359 HIS B CG  1 
ATOM   6133  N  ND1 . HIS B  1 360 ? 5.521   36.420  21.338  1.00 21.80 ? 359 HIS B ND1 1 
ATOM   6134  C  CD2 . HIS B  1 360 ? 3.345   36.381  21.169  1.00 21.35 ? 359 HIS B CD2 1 
ATOM   6135  C  CE1 . HIS B  1 360 ? 5.103   35.360  22.009  1.00 20.82 ? 359 HIS B CE1 1 
ATOM   6136  N  NE2 . HIS B  1 360 ? 3.787   35.315  21.925  1.00 21.41 ? 359 HIS B NE2 1 
ATOM   6137  N  N   . ILE B  1 361 ? 3.478   37.608  17.226  1.00 24.16 ? 360 ILE B N   1 
ATOM   6138  C  CA  . ILE B  1 361 ? 2.662   36.752  16.377  1.00 27.71 ? 360 ILE B CA  1 
ATOM   6139  C  C   . ILE B  1 361 ? 3.156   36.759  14.932  1.00 27.91 ? 360 ILE B C   1 
ATOM   6140  O  O   . ILE B  1 361 ? 3.190   35.715  14.287  1.00 27.76 ? 360 ILE B O   1 
ATOM   6141  C  CB  . ILE B  1 361 ? 1.192   37.181  16.411  1.00 31.54 ? 360 ILE B CB  1 
ATOM   6142  C  CG1 . ILE B  1 361 ? 0.632   37.011  17.820  1.00 34.17 ? 360 ILE B CG1 1 
ATOM   6143  C  CG2 . ILE B  1 361 ? 0.386   36.342  15.432  1.00 34.01 ? 360 ILE B CG2 1 
ATOM   6144  C  CD1 . ILE B  1 361 ? -0.744  37.622  18.006  1.00 37.83 ? 360 ILE B CD1 1 
ATOM   6145  N  N   . GLU B  1 362 ? 3.563   37.926  14.442  1.00 27.92 ? 361 GLU B N   1 
ATOM   6146  C  CA  . GLU B  1 362 ? 3.997   38.041  13.060  1.00 30.74 ? 361 GLU B CA  1 
ATOM   6147  C  C   . GLU B  1 362 ? 5.223   37.180  12.766  1.00 29.04 ? 361 GLU B C   1 
ATOM   6148  O  O   . GLU B  1 362 ? 5.413   36.757  11.623  1.00 27.83 ? 361 GLU B O   1 
ATOM   6149  C  CB  . GLU B  1 362 ? 4.264   39.490  12.694  1.00 34.59 ? 361 GLU B CB  1 
ATOM   6150  C  CG  . GLU B  1 362 ? 2.985   40.305  12.639  1.00 41.24 ? 361 GLU B CG  1 
ATOM   6151  C  CD  . GLU B  1 362 ? 3.211   41.792  12.415  1.00 47.24 ? 361 GLU B CD  1 
ATOM   6152  O  OE1 . GLU B  1 362 ? 4.355   42.219  12.157  1.00 52.80 ? 361 GLU B OE1 1 
ATOM   6153  O  OE2 . GLU B  1 362 ? 2.219   42.546  12.502  1.00 56.32 ? 361 GLU B OE2 1 
ATOM   6154  N  N   . MET B  1 363 ? 6.009   36.853  13.788  1.00 27.04 ? 362 MET B N   1 
ATOM   6155  C  CA  . MET B  1 363 ? 7.190   36.025  13.565  1.00 27.25 ? 362 MET B CA  1 
ATOM   6156  C  C   . MET B  1 363 ? 6.857   34.659  12.946  1.00 25.92 ? 362 MET B C   1 
ATOM   6157  O  O   . MET B  1 363 ? 7.694   34.078  12.271  1.00 24.42 ? 362 MET B O   1 
ATOM   6158  C  CB  . MET B  1 363 ? 8.039   35.857  14.830  1.00 29.09 ? 362 MET B CB  1 
ATOM   6159  C  CG  . MET B  1 363 ? 7.563   34.910  15.910  1.00 31.09 ? 362 MET B CG  1 
ATOM   6160  S  SD  . MET B  1 363 ? 8.871   34.594  17.144  1.00 34.88 ? 362 MET B SD  1 
ATOM   6161  C  CE  . MET B  1 363 ? 9.198   36.249  17.795  1.00 34.93 ? 362 MET B CE  1 
ATOM   6162  N  N   . LEU B  1 364 ? 5.645   34.161  13.175  1.00 25.12 ? 363 LEU B N   1 
ATOM   6163  C  CA  . LEU B  1 364 ? 5.219   32.857  12.632  1.00 27.12 ? 363 LEU B CA  1 
ATOM   6164  C  C   . LEU B  1 364 ? 4.984   32.816  11.123  1.00 27.86 ? 363 LEU B C   1 
ATOM   6165  O  O   . LEU B  1 364 ? 4.976   31.728  10.558  1.00 28.50 ? 363 LEU B O   1 
ATOM   6166  C  CB  . LEU B  1 364 ? 3.930   32.392  13.315  1.00 28.69 ? 363 LEU B CB  1 
ATOM   6167  C  CG  . LEU B  1 364 ? 4.037   31.732  14.681  1.00 29.95 ? 363 LEU B CG  1 
ATOM   6168  C  CD1 . LEU B  1 364 ? 2.652   31.194  15.035  1.00 32.48 ? 363 LEU B CD1 1 
ATOM   6169  C  CD2 . LEU B  1 364 ? 5.027   30.572  14.697  1.00 29.41 ? 363 LEU B CD2 1 
ATOM   6170  N  N   . ALA B  1 365 ? 4.788   33.977  10.503  1.00 26.41 ? 364 ALA B N   1 
ATOM   6171  C  CA  . ALA B  1 365 ? 4.565   34.105  9.083   1.00 29.37 ? 364 ALA B CA  1 
ATOM   6172  C  C   . ALA B  1 365 ? 5.674   34.899  8.411   1.00 29.57 ? 364 ALA B C   1 
ATOM   6173  O  O   . ALA B  1 365 ? 5.576   35.235  7.252   1.00 31.69 ? 364 ALA B O   1 
ATOM   6174  C  CB  . ALA B  1 365 ? 3.215   34.755  8.818   1.00 29.25 ? 364 ALA B CB  1 
ATOM   6175  N  N   . ASN B  1 366 ? 6.750   35.149  9.128   1.00 28.56 ? 365 ASN B N   1 
ATOM   6176  C  CA  . ASN B  1 366 ? 7.815   36.019  8.643   1.00 29.00 ? 365 ASN B CA  1 
ATOM   6177  C  C   . ASN B  1 366 ? 8.839   35.206  7.850   1.00 28.97 ? 365 ASN B C   1 
ATOM   6178  O  O   . ASN B  1 366 ? 9.275   34.138  8.303   1.00 26.90 ? 365 ASN B O   1 
ATOM   6179  C  CB  . ASN B  1 366 ? 8.423   36.722  9.860   1.00 30.14 ? 365 ASN B CB  1 
ATOM   6180  C  CG  . ASN B  1 366 ? 9.558   37.657  9.515   1.00 33.13 ? 365 ASN B CG  1 
ATOM   6181  O  OD1 . ASN B  1 366 ? 10.547  37.248  8.908   1.00 33.71 ? 365 ASN B OD1 1 
ATOM   6182  N  ND2 . ASN B  1 366 ? 9.432   38.927  9.916   1.00 32.31 ? 365 ASN B ND2 1 
ATOM   6183  N  N   . ALA B  1 367 ? 9.219   35.718  6.674   1.00 28.73 ? 366 ALA B N   1 
ATOM   6184  C  CA  . ALA B  1 367 ? 10.108  35.024  5.746   1.00 29.97 ? 366 ALA B CA  1 
ATOM   6185  C  C   . ALA B  1 367 ? 11.476  34.703  6.338   1.00 28.82 ? 366 ALA B C   1 
ATOM   6186  O  O   . ALA B  1 367 ? 12.053  33.669  6.026   1.00 27.38 ? 366 ALA B O   1 
ATOM   6187  C  CB  . ALA B  1 367 ? 10.264  35.825  4.465   1.00 32.04 ? 366 ALA B CB  1 
ATOM   6188  N  N   . THR B  1 368 ? 11.981  35.567  7.212   1.00 28.66 ? 367 THR B N   1 
ATOM   6189  C  CA  A THR B  1 368 ? 13.256  35.301  7.897   0.50 28.80 ? 367 THR B CA  1 
ATOM   6190  C  CA  B THR B  1 368 ? 13.248  35.305  7.893   0.50 28.65 ? 367 THR B CA  1 
ATOM   6191  C  C   . THR B  1 368 ? 13.144  34.145  8.893   1.00 26.49 ? 367 THR B C   1 
ATOM   6192  O  O   . THR B  1 368 ? 14.036  33.311  8.984   1.00 25.23 ? 367 THR B O   1 
ATOM   6193  C  CB  A THR B  1 368 ? 13.833  36.551  8.601   0.50 29.89 ? 367 THR B CB  1 
ATOM   6194  C  CB  B THR B  1 368 ? 13.740  36.586  8.583   0.50 29.53 ? 367 THR B CB  1 
ATOM   6195  O  OG1 A THR B  1 368 ? 12.896  37.069  9.557   0.50 29.87 ? 367 THR B OG1 1 
ATOM   6196  O  OG1 B THR B  1 368 ? 13.855  37.605  7.589   0.50 30.96 ? 367 THR B OG1 1 
ATOM   6197  C  CG2 A THR B  1 368 ? 14.175  37.600  7.561   0.50 31.32 ? 367 THR B CG2 1 
ATOM   6198  C  CG2 B THR B  1 368 ? 15.084  36.376  9.279   0.50 29.75 ? 367 THR B CG2 1 
ATOM   6199  N  N   . THR B  1 369 ? 12.042  34.077  9.619   1.00 25.75 ? 368 THR B N   1 
ATOM   6200  C  CA  . THR B  1 369 ? 11.801  32.961  10.528  1.00 24.83 ? 368 THR B CA  1 
ATOM   6201  C  C   . THR B  1 369 ? 11.753  31.660  9.731   1.00 24.09 ? 368 THR B C   1 
ATOM   6202  O  O   . THR B  1 369 ? 12.319  30.633  10.136  1.00 22.62 ? 368 THR B O   1 
ATOM   6203  C  CB  . THR B  1 369 ? 10.465  33.090  11.281  1.00 24.41 ? 368 THR B CB  1 
ATOM   6204  O  OG1 . THR B  1 369 ? 10.404  34.331  11.977  1.00 25.03 ? 368 THR B OG1 1 
ATOM   6205  C  CG2 . THR B  1 369 ? 10.284  31.948  12.272  1.00 24.28 ? 368 THR B CG2 1 
ATOM   6206  N  N   . LEU B  1 370 ? 11.017  31.694  8.624   1.00 24.00 ? 369 LEU B N   1 
ATOM   6207  C  CA  . LEU B  1 370 ? 10.799  30.488  7.827   1.00 23.98 ? 369 LEU B CA  1 
ATOM   6208  C  C   . LEU B  1 370 ? 12.096  30.059  7.154   1.00 25.20 ? 369 LEU B C   1 
ATOM   6209  O  O   . LEU B  1 370 ? 12.358  28.858  7.041   1.00 24.36 ? 369 LEU B O   1 
ATOM   6210  C  CB  . LEU B  1 370 ? 9.678   30.724  6.809   1.00 25.66 ? 369 LEU B CB  1 
ATOM   6211  C  CG  . LEU B  1 370 ? 8.315   31.007  7.451   1.00 26.28 ? 369 LEU B CG  1 
ATOM   6212  C  CD1 . LEU B  1 370 ? 7.281   31.466  6.423   1.00 28.51 ? 369 LEU B CD1 1 
ATOM   6213  C  CD2 . LEU B  1 370 ? 7.823   29.806  8.207   1.00 26.35 ? 369 LEU B CD2 1 
ATOM   6214  N  N   . ALA B  1 371 ? 12.924  31.017  6.724   1.00 24.90 ? 370 ALA B N   1 
ATOM   6215  C  CA  . ALA B  1 371 ? 14.230  30.697  6.163   1.00 26.23 ? 370 ALA B CA  1 
ATOM   6216  C  C   . ALA B  1 371 ? 15.121  30.018  7.189   1.00 26.12 ? 370 ALA B C   1 
ATOM   6217  O  O   . ALA B  1 371 ? 15.883  29.120  6.843   1.00 26.44 ? 370 ALA B O   1 
ATOM   6218  C  CB  . ALA B  1 371 ? 14.929  31.957  5.604   1.00 27.55 ? 370 ALA B CB  1 
ATOM   6219  N  N   . TYR B  1 372 ? 15.054  30.462  8.445   1.00 25.36 ? 371 TYR B N   1 
ATOM   6220  C  CA  . TYR B  1 372 ? 15.846  29.840  9.512   1.00 25.11 ? 371 TYR B CA  1 
ATOM   6221  C  C   . TYR B  1 372 ? 15.387  28.381  9.725   1.00 24.24 ? 371 TYR B C   1 
ATOM   6222  O  O   . TYR B  1 372 ? 16.191  27.459  9.789   1.00 23.87 ? 371 TYR B O   1 
ATOM   6223  C  CB  . TYR B  1 372 ? 15.738  30.636  10.828  1.00 24.75 ? 371 TYR B CB  1 
ATOM   6224  C  CG  . TYR B  1 372 ? 16.707  30.164  11.889  1.00 25.35 ? 371 TYR B CG  1 
ATOM   6225  C  CD1 . TYR B  1 372 ? 16.440  29.025  12.653  1.00 24.71 ? 371 TYR B CD1 1 
ATOM   6226  C  CD2 . TYR B  1 372 ? 17.899  30.858  12.135  1.00 27.52 ? 371 TYR B CD2 1 
ATOM   6227  C  CE1 . TYR B  1 372 ? 17.341  28.578  13.612  1.00 25.36 ? 371 TYR B CE1 1 
ATOM   6228  C  CE2 . TYR B  1 372 ? 18.797  30.433  13.111  1.00 27.81 ? 371 TYR B CE2 1 
ATOM   6229  C  CZ  . TYR B  1 372 ? 18.513  29.286  13.845  1.00 26.87 ? 371 TYR B CZ  1 
ATOM   6230  O  OH  . TYR B  1 372 ? 19.411  28.838  14.786  1.00 27.04 ? 371 TYR B OH  1 
ATOM   6231  N  N   . LEU B  1 373 ? 14.087  28.192  9.822   1.00 22.37 ? 372 LEU B N   1 
ATOM   6232  C  CA  . LEU B  1 373 ? 13.545  26.857  9.981   1.00 22.88 ? 372 LEU B CA  1 
ATOM   6233  C  C   . LEU B  1 373 ? 13.920  25.943  8.811   1.00 23.27 ? 372 LEU B C   1 
ATOM   6234  O  O   . LEU B  1 373 ? 14.269  24.771  8.998   1.00 23.94 ? 372 LEU B O   1 
ATOM   6235  C  CB  . LEU B  1 373 ? 12.019  26.947  10.151  1.00 22.11 ? 372 LEU B CB  1 
ATOM   6236  C  CG  . LEU B  1 373 ? 11.313  25.609  10.329  1.00 22.31 ? 372 LEU B CG  1 
ATOM   6237  C  CD1 . LEU B  1 373 ? 11.756  24.887  11.589  1.00 21.79 ? 372 LEU B CD1 1 
ATOM   6238  C  CD2 . LEU B  1 373 ? 9.794   25.842  10.328  1.00 22.09 ? 372 LEU B CD2 1 
ATOM   6239  N  N   . LYS B  1 374 ? 13.850  26.465  7.598   1.00 24.25 ? 373 LYS B N   1 
ATOM   6240  C  CA  . LYS B  1 374 ? 14.238  25.699  6.425   1.00 26.23 ? 373 LYS B CA  1 
ATOM   6241  C  C   . LYS B  1 374 ? 15.673  25.158  6.539   1.00 27.10 ? 373 LYS B C   1 
ATOM   6242  O  O   . LYS B  1 374 ? 15.928  24.014  6.156   1.00 26.77 ? 373 LYS B O   1 
ATOM   6243  C  CB  . LYS B  1 374 ? 14.104  26.538  5.148   1.00 28.48 ? 373 LYS B CB  1 
ATOM   6244  C  CG  . LYS B  1 374 ? 14.185  25.701  3.880   1.00 29.60 ? 373 LYS B CG  1 
ATOM   6245  C  CD  . LYS B  1 374 ? 14.077  26.547  2.634   1.00 32.13 ? 373 LYS B CD  1 
ATOM   6246  C  CE  . LYS B  1 374 ? 13.991  25.654  1.411   1.00 34.63 ? 373 LYS B CE  1 
ATOM   6247  N  NZ  . LYS B  1 374 ? 13.827  26.514  0.218   1.00 37.04 ? 373 LYS B NZ  1 
ATOM   6248  N  N   . ARG B  1 375 ? 16.597  26.003  7.001   1.00 27.70 ? 374 ARG B N   1 
ATOM   6249  C  CA  A ARG B  1 375 ? 17.991  25.610  7.184   0.50 29.41 ? 374 ARG B CA  1 
ATOM   6250  C  CA  B ARG B  1 375 ? 17.996  25.611  7.193   0.50 29.95 ? 374 ARG B CA  1 
ATOM   6251  C  C   . ARG B  1 375 ? 18.127  24.513  8.243   1.00 28.12 ? 374 ARG B C   1 
ATOM   6252  O  O   . ARG B  1 375 ? 18.887  23.562  8.050   1.00 28.71 ? 374 ARG B O   1 
ATOM   6253  C  CB  A ARG B  1 375 ? 18.846  26.832  7.547   0.50 31.94 ? 374 ARG B CB  1 
ATOM   6254  C  CB  B ARG B  1 375 ? 18.854  26.829  7.589   0.50 33.62 ? 374 ARG B CB  1 
ATOM   6255  C  CG  A ARG B  1 375 ? 20.324  26.543  7.796   0.50 35.32 ? 374 ARG B CG  1 
ATOM   6256  C  CG  B ARG B  1 375 ? 20.285  26.524  8.047   0.50 38.34 ? 374 ARG B CG  1 
ATOM   6257  C  CD  A ARG B  1 375 ? 21.032  26.017  6.560   0.50 37.85 ? 374 ARG B CD  1 
ATOM   6258  C  CD  B ARG B  1 375 ? 20.896  27.733  8.760   0.50 42.26 ? 374 ARG B CD  1 
ATOM   6259  N  NE  A ARG B  1 375 ? 22.419  25.668  6.847   0.50 40.17 ? 374 ARG B NE  1 
ATOM   6260  N  NE  B ARG B  1 375 ? 21.600  27.411  10.014  0.50 44.69 ? 374 ARG B NE  1 
ATOM   6261  C  CZ  A ARG B  1 375 ? 22.790  24.573  7.501   0.50 41.06 ? 374 ARG B CZ  1 
ATOM   6262  C  CZ  B ARG B  1 375 ? 20.998  27.193  11.182  0.50 43.42 ? 374 ARG B CZ  1 
ATOM   6263  N  NH1 A ARG B  1 375 ? 24.068  24.336  7.723   0.50 43.63 ? 374 ARG B NH1 1 
ATOM   6264  N  NH1 B ARG B  1 375 ? 21.709  26.921  12.266  0.50 43.67 ? 374 ARG B NH1 1 
ATOM   6265  N  NH2 A ARG B  1 375 ? 21.883  23.720  7.943   0.50 40.97 ? 374 ARG B NH2 1 
ATOM   6266  N  NH2 B ARG B  1 375 ? 19.684  27.236  11.263  0.50 43.45 ? 374 ARG B NH2 1 
ATOM   6267  N  N   . VAL B  1 376 ? 17.372  24.628  9.346   1.00 25.64 ? 375 VAL B N   1 
ATOM   6268  C  CA  . VAL B  1 376 ? 17.367  23.607  10.397  1.00 24.89 ? 375 VAL B CA  1 
ATOM   6269  C  C   . VAL B  1 376 ? 16.893  22.261  9.815   1.00 24.83 ? 375 VAL B C   1 
ATOM   6270  O  O   . VAL B  1 376 ? 17.490  21.231  10.075  1.00 24.92 ? 375 VAL B O   1 
ATOM   6271  C  CB  . VAL B  1 376 ? 16.483  24.003  11.618  1.00 24.92 ? 375 VAL B CB  1 
ATOM   6272  C  CG1 . VAL B  1 376 ? 16.351  22.856  12.621  1.00 24.75 ? 375 VAL B CG1 1 
ATOM   6273  C  CG2 . VAL B  1 376 ? 17.052  25.215  12.333  1.00 25.11 ? 375 VAL B CG2 1 
ATOM   6274  N  N   . LEU B  1 377 ? 15.825  22.281  9.020   1.00 25.11 ? 376 LEU B N   1 
ATOM   6275  C  CA  . LEU B  1 377 ? 15.203  21.042  8.521   1.00 26.38 ? 376 LEU B CA  1 
ATOM   6276  C  C   . LEU B  1 377 ? 15.917  20.414  7.321   1.00 29.75 ? 376 LEU B C   1 
ATOM   6277  O  O   . LEU B  1 377 ? 16.096  19.206  7.273   1.00 28.15 ? 376 LEU B O   1 
ATOM   6278  C  CB  . LEU B  1 377 ? 13.737  21.308  8.154   1.00 25.44 ? 376 LEU B CB  1 
ATOM   6279  C  CG  . LEU B  1 377 ? 12.845  21.772  9.297   1.00 24.75 ? 376 LEU B CG  1 
ATOM   6280  C  CD1 . LEU B  1 377 ? 11.414  21.988  8.805   1.00 24.81 ? 376 LEU B CD1 1 
ATOM   6281  C  CD2 . LEU B  1 377 ? 12.857  20.782  10.463  1.00 25.16 ? 376 LEU B CD2 1 
ATOM   6282  N  N   . LEU B  1 378 ? 16.270  21.237  6.339   1.00 31.81 ? 377 LEU B N   1 
ATOM   6283  C  CA  . LEU B  1 378 ? 16.698  20.760  5.033   1.00 36.74 ? 377 LEU B CA  1 
ATOM   6284  C  C   . LEU B  1 378 ? 18.203  20.870  4.855   1.00 40.68 ? 377 LEU B C   1 
ATOM   6285  O  O   . LEU B  1 378 ? 18.735  20.341  3.884   1.00 40.74 ? 377 LEU B O   1 
ATOM   6286  C  CB  . LEU B  1 378 ? 15.988  21.528  3.898   1.00 38.70 ? 377 LEU B CB  1 
ATOM   6287  C  CG  . LEU B  1 378 ? 14.588  21.129  3.382   1.00 40.99 ? 377 LEU B CG  1 
ATOM   6288  C  CD1 . LEU B  1 378 ? 13.654  20.642  4.459   1.00 42.21 ? 377 LEU B CD1 1 
ATOM   6289  C  CD2 . LEU B  1 378 ? 13.956  22.280  2.613   1.00 42.34 ? 377 LEU B CD2 1 
ATOM   6290  N  N   . GLY B  1 379 ? 18.887  21.566  5.756   1.00 42.31 ? 378 GLY B N   1 
ATOM   6291  C  CA  . GLY B  1 379 ? 20.341  21.570  5.759   1.00 49.74 ? 378 GLY B CA  1 
ATOM   6292  C  C   . GLY B  1 379 ? 20.903  22.692  4.912   1.00 57.54 ? 378 GLY B C   1 
ATOM   6293  O  O   . GLY B  1 379 ? 20.140  23.513  4.397   1.00 56.66 ? 378 GLY B O   1 
ATOM   6294  N  N   . PRO B  1 380 ? 22.247  22.724  4.749   1.00 68.52 ? 379 PRO B N   1 
ATOM   6295  C  CA  . PRO B  1 380 ? 22.962  23.849  4.116   1.00 74.06 ? 379 PRO B CA  1 
ATOM   6296  C  C   . PRO B  1 380 ? 22.728  23.966  2.611   1.00 75.77 ? 379 PRO B C   1 
ATOM   6297  O  O   . PRO B  1 380 ? 22.324  22.992  1.978   1.00 80.92 ? 379 PRO B O   1 
ATOM   6298  C  CB  . PRO B  1 380 ? 24.440  23.537  4.405   1.00 74.53 ? 379 PRO B CB  1 
ATOM   6299  C  CG  . PRO B  1 380 ? 24.498  22.057  4.591   1.00 73.28 ? 379 PRO B CG  1 
ATOM   6300  C  CD  . PRO B  1 380 ? 23.166  21.639  5.155   1.00 69.81 ? 379 PRO B CD  1 
ATOM   6301  N  N   . HIS C  1 5   ? 14.172  -16.126 -6.547  1.00 39.05 ? 4   HIS C N   1 
ATOM   6302  C  CA  . HIS C  1 5   ? 12.678  -16.279 -6.513  1.00 34.69 ? 4   HIS C CA  1 
ATOM   6303  C  C   . HIS C  1 5   ? 12.066  -15.566 -7.742  1.00 28.98 ? 4   HIS C C   1 
ATOM   6304  O  O   . HIS C  1 5   ? 11.437  -14.533 -7.637  1.00 27.58 ? 4   HIS C O   1 
ATOM   6305  C  CB  . HIS C  1 5   ? 12.180  -15.732 -5.197  1.00 38.74 ? 4   HIS C CB  1 
ATOM   6306  C  CG  . HIS C  1 5   ? 10.724  -15.958 -4.943  1.00 38.56 ? 4   HIS C CG  1 
ATOM   6307  N  ND1 . HIS C  1 5   ? 10.256  -16.841 -3.992  1.00 39.02 ? 4   HIS C ND1 1 
ATOM   6308  C  CD2 . HIS C  1 5   ? 9.638   -15.343 -5.456  1.00 39.25 ? 4   HIS C CD2 1 
ATOM   6309  C  CE1 . HIS C  1 5   ? 8.938   -16.768 -3.950  1.00 39.65 ? 4   HIS C CE1 1 
ATOM   6310  N  NE2 . HIS C  1 5   ? 8.542   -15.863 -4.826  1.00 38.63 ? 4   HIS C NE2 1 
ATOM   6311  N  N   . PRO C  1 6   ? 12.309  -16.097 -8.942  1.00 23.98 ? 5   PRO C N   1 
ATOM   6312  C  CA  . PRO C  1 6   ? 11.850  -15.361 -10.124 1.00 21.66 ? 5   PRO C CA  1 
ATOM   6313  C  C   . PRO C  1 6   ? 10.345  -15.557 -10.347 1.00 19.78 ? 5   PRO C C   1 
ATOM   6314  O  O   . PRO C  1 6   ? 9.807   -16.595 -9.956  1.00 18.80 ? 5   PRO C O   1 
ATOM   6315  C  CB  . PRO C  1 6   ? 12.636  -16.008 -11.268 1.00 22.58 ? 5   PRO C CB  1 
ATOM   6316  C  CG  . PRO C  1 6   ? 12.832  -17.408 -10.802 1.00 24.07 ? 5   PRO C CG  1 
ATOM   6317  C  CD  . PRO C  1 6   ? 13.056  -17.312 -9.312  1.00 24.58 ? 5   PRO C CD  1 
ATOM   6318  N  N   . PRO C  1 7   ? 9.705   -14.616 -11.026 1.00 17.83 ? 6   PRO C N   1 
ATOM   6319  C  CA  . PRO C  1 7   ? 8.288   -14.804 -11.389 1.00 17.37 ? 6   PRO C CA  1 
ATOM   6320  C  C   . PRO C  1 7   ? 8.073   -15.969 -12.347 1.00 17.10 ? 6   PRO C C   1 
ATOM   6321  O  O   . PRO C  1 7   ? 8.969   -16.322 -13.144 1.00 16.01 ? 6   PRO C O   1 
ATOM   6322  C  CB  . PRO C  1 7   ? 7.899   -13.497 -12.059 1.00 17.86 ? 6   PRO C CB  1 
ATOM   6323  C  CG  . PRO C  1 7   ? 9.130   -12.674 -12.157 1.00 18.75 ? 6   PRO C CG  1 
ATOM   6324  C  CD  . PRO C  1 7   ? 10.296  -13.390 -11.598 1.00 18.28 ? 6   PRO C CD  1 
ATOM   6325  N  N   . VAL C  1 8   ? 6.906   -16.608 -12.221 1.00 16.42 ? 7   VAL C N   1 
ATOM   6326  C  CA  . VAL C  1 8   ? 6.644   -17.842 -12.921 1.00 16.45 ? 7   VAL C CA  1 
ATOM   6327  C  C   . VAL C  1 8   ? 5.323   -17.717 -13.668 1.00 15.82 ? 7   VAL C C   1 
ATOM   6328  O  O   . VAL C  1 8   ? 4.318   -17.242 -13.098 1.00 14.49 ? 7   VAL C O   1 
ATOM   6329  C  CB  . VAL C  1 8   ? 6.536   -19.023 -11.933 1.00 17.26 ? 7   VAL C CB  1 
ATOM   6330  C  CG1 . VAL C  1 8   ? 5.993   -20.262 -12.616 1.00 17.50 ? 7   VAL C CG1 1 
ATOM   6331  C  CG2 . VAL C  1 8   ? 7.871   -19.342 -11.307 1.00 18.50 ? 7   VAL C CG2 1 
ATOM   6332  N  N   . VAL C  1 9   ? 5.337   -18.131 -14.923 1.00 15.58 ? 8   VAL C N   1 
ATOM   6333  C  CA  . VAL C  1 9   ? 4.113   -18.261 -15.739 1.00 15.10 ? 8   VAL C CA  1 
ATOM   6334  C  C   . VAL C  1 9   ? 3.909   -19.735 -16.088 1.00 15.31 ? 8   VAL C C   1 
ATOM   6335  O  O   . VAL C  1 9   ? 4.817   -20.399 -16.615 1.00 15.86 ? 8   VAL C O   1 
ATOM   6336  C  CB  . VAL C  1 9   ? 4.194   -17.398 -17.019 1.00 15.19 ? 8   VAL C CB  1 
ATOM   6337  C  CG1 . VAL C  1 9   ? 3.006   -17.670 -17.940 1.00 15.25 ? 8   VAL C CG1 1 
ATOM   6338  C  CG2 . VAL C  1 9   ? 4.249   -15.901 -16.653 1.00 15.42 ? 8   VAL C CG2 1 
ATOM   6339  N  N   . LEU C  1 10  ? 2.689   -20.222 -15.846 1.00 14.92 ? 9   LEU C N   1 
ATOM   6340  C  CA  . LEU C  1 10  ? 2.300   -21.593 -16.113 1.00 15.17 ? 9   LEU C CA  1 
ATOM   6341  C  C   . LEU C  1 10  ? 1.458   -21.696 -17.390 1.00 15.01 ? 9   LEU C C   1 
ATOM   6342  O  O   . LEU C  1 10  ? 0.468   -20.970 -17.557 1.00 14.56 ? 9   LEU C O   1 
ATOM   6343  C  CB  . LEU C  1 10  ? 1.491   -22.150 -14.940 1.00 15.54 ? 9   LEU C CB  1 
ATOM   6344  C  CG  . LEU C  1 10  ? 2.120   -21.985 -13.546 1.00 16.98 ? 9   LEU C CG  1 
ATOM   6345  C  CD1 . LEU C  1 10  ? 1.129   -22.440 -12.481 1.00 17.53 ? 9   LEU C CD1 1 
ATOM   6346  C  CD2 . LEU C  1 10  ? 3.396   -22.780 -13.417 1.00 17.28 ? 9   LEU C CD2 1 
ATOM   6347  N  N   . VAL C  1 11  ? 1.840   -22.627 -18.276 1.00 14.37 ? 10  VAL C N   1 
ATOM   6348  C  CA  . VAL C  1 11  ? 1.182   -22.811 -19.564 1.00 13.90 ? 10  VAL C CA  1 
ATOM   6349  C  C   . VAL C  1 11  ? 0.674   -24.258 -19.655 1.00 14.01 ? 10  VAL C C   1 
ATOM   6350  O  O   . VAL C  1 11  ? 1.474   -25.201 -19.636 1.00 13.47 ? 10  VAL C O   1 
ATOM   6351  C  CB  . VAL C  1 11  ? 2.120   -22.510 -20.758 1.00 14.30 ? 10  VAL C CB  1 
ATOM   6352  C  CG1 . VAL C  1 11  ? 1.335   -22.569 -22.076 1.00 14.40 ? 10  VAL C CG1 1 
ATOM   6353  C  CG2 . VAL C  1 11  ? 2.787   -21.137 -20.612 1.00 14.55 ? 10  VAL C CG2 1 
ATOM   6354  N  N   . PRO C  1 12  ? -0.662  -24.443 -19.705 1.00 13.64 ? 11  PRO C N   1 
ATOM   6355  C  CA  . PRO C  1 12  ? -1.239  -25.766 -19.685 1.00 13.73 ? 11  PRO C CA  1 
ATOM   6356  C  C   . PRO C  1 12  ? -1.268  -26.467 -21.040 1.00 13.68 ? 11  PRO C C   1 
ATOM   6357  O  O   . PRO C  1 12  ? -0.997  -25.851 -22.059 1.00 13.55 ? 11  PRO C O   1 
ATOM   6358  C  CB  . PRO C  1 12  ? -2.690  -25.495 -19.248 1.00 13.95 ? 11  PRO C CB  1 
ATOM   6359  C  CG  . PRO C  1 12  ? -3.005  -24.190 -19.858 1.00 13.85 ? 11  PRO C CG  1 
ATOM   6360  C  CD  . PRO C  1 12  ? -1.701  -23.399 -19.767 1.00 13.88 ? 11  PRO C CD  1 
ATOM   6361  N  N   . GLY C  1 13  ? -1.610  -27.752 -21.031 1.00 13.75 ? 12  GLY C N   1 
ATOM   6362  C  CA  . GLY C  1 13  ? -1.747  -28.514 -22.268 1.00 14.08 ? 12  GLY C CA  1 
ATOM   6363  C  C   . GLY C  1 13  ? -3.202  -28.595 -22.711 1.00 15.10 ? 12  GLY C C   1 
ATOM   6364  O  O   . GLY C  1 13  ? -4.081  -27.852 -22.231 1.00 15.16 ? 12  GLY C O   1 
ATOM   6365  N  N   . ASP C  1 14  ? -3.451  -29.517 -23.640 1.00 16.31 ? 13  ASP C N   1 
ATOM   6366  C  CA  . ASP C  1 14  ? -4.791  -29.761 -24.172 1.00 16.23 ? 13  ASP C CA  1 
ATOM   6367  C  C   . ASP C  1 14  ? -5.721  -30.222 -23.045 1.00 16.36 ? 13  ASP C C   1 
ATOM   6368  O  O   . ASP C  1 14  ? -5.325  -30.984 -22.166 1.00 16.73 ? 13  ASP C O   1 
ATOM   6369  C  CB  . ASP C  1 14  ? -4.672  -30.801 -25.296 1.00 17.59 ? 13  ASP C CB  1 
ATOM   6370  C  CG  . ASP C  1 14  ? -5.843  -30.782 -26.287 1.00 18.92 ? 13  ASP C CG  1 
ATOM   6371  O  OD1 . ASP C  1 14  ? -6.838  -30.035 -26.114 1.00 18.40 ? 13  ASP C OD1 1 
ATOM   6372  O  OD2 . ASP C  1 14  ? -5.747  -31.589 -27.268 1.00 19.51 ? 13  ASP C OD2 1 
ATOM   6373  N  N   . LEU C  1 15  ? -6.948  -29.716 -23.035 1.00 16.83 ? 14  LEU C N   1 
ATOM   6374  C  CA  . LEU C  1 15  ? -7.899  -29.946 -21.945 1.00 17.50 ? 14  LEU C CA  1 
ATOM   6375  C  C   . LEU C  1 15  ? -7.477  -29.328 -20.609 1.00 16.45 ? 14  LEU C C   1 
ATOM   6376  O  O   . LEU C  1 15  ? -8.087  -29.600 -19.580 1.00 16.08 ? 14  LEU C O   1 
ATOM   6377  C  CB  . LEU C  1 15  ? -8.152  -31.436 -21.728 1.00 18.71 ? 14  LEU C CB  1 
ATOM   6378  C  CG  . LEU C  1 15  ? -8.467  -32.305 -22.953 1.00 20.47 ? 14  LEU C CG  1 
ATOM   6379  C  CD1 . LEU C  1 15  ? -8.708  -33.732 -22.498 1.00 21.03 ? 14  LEU C CD1 1 
ATOM   6380  C  CD2 . LEU C  1 15  ? -9.666  -31.758 -23.674 1.00 20.76 ? 14  LEU C CD2 1 
ATOM   6381  N  N   . GLY C  1 16  ? -6.456  -28.481 -20.631 1.00 15.90 ? 15  GLY C N   1 
ATOM   6382  C  CA  . GLY C  1 16  ? -5.712  -28.142 -19.416 1.00 15.75 ? 15  GLY C CA  1 
ATOM   6383  C  C   . GLY C  1 16  ? -6.119  -26.871 -18.697 1.00 15.25 ? 15  GLY C C   1 
ATOM   6384  O  O   . GLY C  1 16  ? -5.445  -26.434 -17.768 1.00 15.10 ? 15  GLY C O   1 
ATOM   6385  N  N   . ASN C  1 17  ? -7.249  -26.288 -19.077 1.00 15.34 ? 16  ASN C N   1 
ATOM   6386  C  CA  . ASN C  1 17  ? -7.837  -25.243 -18.293 1.00 15.07 ? 16  ASN C CA  1 
ATOM   6387  C  C   . ASN C  1 17  ? -9.339  -25.200 -18.493 1.00 15.90 ? 16  ASN C C   1 
ATOM   6388  O  O   . ASN C  1 17  ? -9.874  -25.723 -19.485 1.00 15.57 ? 16  ASN C O   1 
ATOM   6389  C  CB  . ASN C  1 17  ? -7.189  -23.855 -18.549 1.00 14.94 ? 16  ASN C CB  1 
ATOM   6390  C  CG  . ASN C  1 17  ? -7.146  -23.447 -20.028 1.00 14.93 ? 16  ASN C CG  1 
ATOM   6391  O  OD1 . ASN C  1 17  ? -6.064  -23.372 -20.626 1.00 14.69 ? 16  ASN C OD1 1 
ATOM   6392  N  ND2 . ASN C  1 17  ? -8.304  -23.145 -20.607 1.00 14.21 ? 16  ASN C ND2 1 
ATOM   6393  N  N   . GLN C  1 18  ? -10.015 -24.590 -17.533 1.00 16.02 ? 17  GLN C N   1 
ATOM   6394  C  CA  . GLN C  1 18  ? -11.476 -24.451 -17.622 1.00 17.28 ? 17  GLN C CA  1 
ATOM   6395  C  C   . GLN C  1 18  ? -11.864 -23.661 -18.880 1.00 17.14 ? 17  GLN C C   1 
ATOM   6396  O  O   . GLN C  1 18  ? -11.124 -22.791 -19.331 1.00 16.86 ? 17  GLN C O   1 
ATOM   6397  C  CB  . GLN C  1 18  ? -12.026 -23.733 -16.393 1.00 18.66 ? 17  GLN C CB  1 
ATOM   6398  C  CG  . GLN C  1 18  ? -11.828 -24.474 -15.084 1.00 20.31 ? 17  GLN C CG  1 
ATOM   6399  C  CD  . GLN C  1 18  ? -12.333 -23.700 -13.890 1.00 22.15 ? 17  GLN C CD  1 
ATOM   6400  O  OE1 . GLN C  1 18  ? -13.152 -22.765 -14.018 1.00 22.18 ? 17  GLN C OE1 1 
ATOM   6401  N  NE2 . GLN C  1 18  ? -11.829 -24.062 -12.711 1.00 22.50 ? 17  GLN C NE2 1 
ATOM   6402  N  N   . LEU C  1 19  ? -13.061 -23.937 -19.405 1.00 17.91 ? 18  LEU C N   1 
ATOM   6403  C  CA  . LEU C  1 19  ? -13.699 -23.125 -20.417 1.00 18.68 ? 18  LEU C CA  1 
ATOM   6404  C  C   . LEU C  1 19  ? -15.139 -22.878 -19.990 1.00 19.03 ? 18  LEU C C   1 
ATOM   6405  O  O   . LEU C  1 19  ? -15.770 -23.738 -19.354 1.00 18.65 ? 18  LEU C O   1 
ATOM   6406  C  CB  . LEU C  1 19  ? -13.727 -23.831 -21.790 1.00 19.05 ? 18  LEU C CB  1 
ATOM   6407  C  CG  . LEU C  1 19  ? -12.391 -24.129 -22.474 1.00 19.31 ? 18  LEU C CG  1 
ATOM   6408  C  CD1 . LEU C  1 19  ? -12.641 -24.865 -23.788 1.00 20.56 ? 18  LEU C CD1 1 
ATOM   6409  C  CD2 . LEU C  1 19  ? -11.627 -22.848 -22.748 1.00 19.02 ? 18  LEU C CD2 1 
ATOM   6410  N  N   . GLU C  1 20  ? -15.649 -21.708 -20.358 1.00 19.91 ? 19  GLU C N   1 
ATOM   6411  C  CA  . GLU C  1 20  ? -17.019 -21.305 -20.017 1.00 21.00 ? 19  GLU C CA  1 
ATOM   6412  C  C   . GLU C  1 20  ? -17.796 -20.985 -21.284 1.00 20.80 ? 19  GLU C C   1 
ATOM   6413  O  O   . GLU C  1 20  ? -17.226 -20.505 -22.256 1.00 19.99 ? 19  GLU C O   1 
ATOM   6414  C  CB  . GLU C  1 20  ? -17.003 -20.075 -19.117 1.00 23.73 ? 19  GLU C CB  1 
ATOM   6415  C  CG  . GLU C  1 20  ? -16.509 -20.370 -17.726 1.00 25.72 ? 19  GLU C CG  1 
ATOM   6416  C  CD  . GLU C  1 20  ? -16.326 -19.142 -16.858 1.00 29.41 ? 19  GLU C CD  1 
ATOM   6417  O  OE1 . GLU C  1 20  ? -16.423 -17.988 -17.350 1.00 31.15 ? 19  GLU C OE1 1 
ATOM   6418  O  OE2 . GLU C  1 20  ? -16.059 -19.354 -15.647 1.00 33.38 ? 19  GLU C OE2 1 
ATOM   6419  N  N   . ALA C  1 21  ? -19.104 -21.233 -21.270 1.00 21.14 ? 20  ALA C N   1 
ATOM   6420  C  CA  . ALA C  1 21  ? -19.946 -20.946 -22.415 1.00 21.97 ? 20  ALA C CA  1 
ATOM   6421  C  C   . ALA C  1 21  ? -21.212 -20.177 -22.023 1.00 22.54 ? 20  ALA C C   1 
ATOM   6422  O  O   . ALA C  1 21  ? -21.695 -20.300 -20.909 1.00 22.19 ? 20  ALA C O   1 
ATOM   6423  C  CB  . ALA C  1 21  ? -20.351 -22.237 -23.111 1.00 22.23 ? 20  ALA C CB  1 
ATOM   6424  N  N   . LYS C  1 22  ? -21.730 -19.410 -22.979 1.00 24.10 ? 21  LYS C N   1 
ATOM   6425  C  CA  . LYS C  1 22  ? -23.042 -18.756 -22.855 1.00 25.74 ? 21  LYS C CA  1 
ATOM   6426  C  C   . LYS C  1 22  ? -23.816 -19.029 -24.132 1.00 25.67 ? 21  LYS C C   1 
ATOM   6427  O  O   . LYS C  1 22  ? -23.254 -19.006 -25.215 1.00 25.30 ? 21  LYS C O   1 
ATOM   6428  C  CB  . LYS C  1 22  ? -22.871 -17.251 -22.609 1.00 27.72 ? 21  LYS C CB  1 
ATOM   6429  C  CG  . LYS C  1 22  ? -24.197 -16.502 -22.458 1.00 30.45 ? 21  LYS C CG  1 
ATOM   6430  C  CD  . LYS C  1 22  ? -23.977 -15.033 -22.138 1.00 32.75 ? 21  LYS C CD  1 
ATOM   6431  C  CE  . LYS C  1 22  ? -25.306 -14.327 -21.883 1.00 35.35 ? 21  LYS C CE  1 
ATOM   6432  N  NZ  . LYS C  1 22  ? -25.082 -12.997 -21.268 1.00 37.81 ? 21  LYS C NZ  1 
ATOM   6433  N  N   . LEU C  1 23  ? -25.111 -19.295 -23.996 1.00 25.47 ? 22  LEU C N   1 
ATOM   6434  C  CA  . LEU C  1 23  ? -25.912 -19.795 -25.089 1.00 26.35 ? 22  LEU C CA  1 
ATOM   6435  C  C   . LEU C  1 23  ? -27.102 -18.897 -25.437 1.00 27.98 ? 22  LEU C C   1 
ATOM   6436  O  O   . LEU C  1 23  ? -27.760 -18.368 -24.552 1.00 28.30 ? 22  LEU C O   1 
ATOM   6437  C  CB  . LEU C  1 23  ? -26.484 -21.167 -24.727 1.00 26.69 ? 22  LEU C CB  1 
ATOM   6438  C  CG  . LEU C  1 23  ? -25.506 -22.194 -24.156 1.00 25.90 ? 22  LEU C CG  1 
ATOM   6439  C  CD1 . LEU C  1 23  ? -26.269 -23.462 -23.811 1.00 26.20 ? 22  LEU C CD1 1 
ATOM   6440  C  CD2 . LEU C  1 23  ? -24.370 -22.474 -25.125 1.00 25.05 ? 22  LEU C CD2 1 
ATOM   6441  N  N   . ASP C  1 24  ? -27.360 -18.772 -26.740 1.00 29.07 ? 23  ASP C N   1 
ATOM   6442  C  CA  . ASP C  1 24  ? -28.650 -18.270 -27.283 1.00 31.63 ? 23  ASP C CA  1 
ATOM   6443  C  C   . ASP C  1 24  ? -28.839 -18.933 -28.656 1.00 31.62 ? 23  ASP C C   1 
ATOM   6444  O  O   . ASP C  1 24  ? -28.717 -18.293 -29.698 1.00 32.64 ? 23  ASP C O   1 
ATOM   6445  C  CB  . ASP C  1 24  ? -28.637 -16.739 -27.378 1.00 32.47 ? 23  ASP C CB  1 
ATOM   6446  C  CG  . ASP C  1 24  ? -30.013 -16.154 -27.721 1.00 36.05 ? 23  ASP C CG  1 
ATOM   6447  O  OD1 . ASP C  1 24  ? -31.016 -16.909 -27.781 1.00 35.96 ? 23  ASP C OD1 1 
ATOM   6448  O  OD2 . ASP C  1 24  ? -30.089 -14.928 -27.911 1.00 37.83 ? 23  ASP C OD2 1 
ATOM   6449  N  N   . LYS C  1 25  ? -29.094 -20.243 -28.645 1.00 30.91 ? 24  LYS C N   1 
ATOM   6450  C  CA  . LYS C  1 25  ? -29.032 -21.069 -29.847 1.00 30.17 ? 24  LYS C CA  1 
ATOM   6451  C  C   . LYS C  1 25  ? -30.367 -21.085 -30.586 1.00 32.24 ? 24  LYS C C   1 
ATOM   6452  O  O   . LYS C  1 25  ? -31.403 -21.114 -29.949 1.00 31.90 ? 24  LYS C O   1 
ATOM   6453  C  CB  . LYS C  1 25  ? -28.675 -22.508 -29.463 1.00 29.58 ? 24  LYS C CB  1 
ATOM   6454  C  CG  . LYS C  1 25  ? -27.332 -22.651 -28.741 1.00 28.64 ? 24  LYS C CG  1 
ATOM   6455  C  CD  . LYS C  1 25  ? -27.258 -23.944 -27.938 1.00 28.39 ? 24  LYS C CD  1 
ATOM   6456  C  CE  . LYS C  1 25  ? -27.191 -25.191 -28.797 1.00 27.98 ? 24  LYS C CE  1 
ATOM   6457  N  NZ  . LYS C  1 25  ? -25.892 -25.391 -29.480 1.00 27.98 ? 24  LYS C NZ  1 
ATOM   6458  N  N   . PRO C  1 26  ? -30.341 -21.114 -31.932 1.00 33.30 ? 25  PRO C N   1 
ATOM   6459  C  CA  . PRO C  1 26  ? -31.596 -21.239 -32.684 1.00 35.45 ? 25  PRO C CA  1 
ATOM   6460  C  C   . PRO C  1 26  ? -32.226 -22.626 -32.574 1.00 35.24 ? 25  PRO C C   1 
ATOM   6461  O  O   . PRO C  1 26  ? -33.445 -22.727 -32.594 1.00 35.29 ? 25  PRO C O   1 
ATOM   6462  C  CB  . PRO C  1 26  ? -31.184 -20.958 -34.139 1.00 35.40 ? 25  PRO C CB  1 
ATOM   6463  C  CG  . PRO C  1 26  ? -29.729 -21.171 -34.188 1.00 34.85 ? 25  PRO C CG  1 
ATOM   6464  C  CD  . PRO C  1 26  ? -29.182 -20.890 -32.815 1.00 33.37 ? 25  PRO C CD  1 
ATOM   6465  N  N   . THR C  1 27  ? -31.408 -23.674 -32.465 1.00 33.74 ? 26  THR C N   1 
ATOM   6466  C  CA  . THR C  1 27  ? -31.909 -25.045 -32.344 1.00 34.64 ? 26  THR C CA  1 
ATOM   6467  C  C   . THR C  1 27  ? -31.053 -25.860 -31.405 1.00 33.45 ? 26  THR C C   1 
ATOM   6468  O  O   . THR C  1 27  ? -29.878 -25.507 -31.167 1.00 32.08 ? 26  THR C O   1 
ATOM   6469  C  CB  . THR C  1 27  ? -31.916 -25.782 -33.705 1.00 36.95 ? 26  THR C CB  1 
ATOM   6470  O  OG1 . THR C  1 27  ? -30.583 -25.879 -34.200 1.00 38.34 ? 26  THR C OG1 1 
ATOM   6471  C  CG2 . THR C  1 27  ? -32.764 -25.065 -34.719 1.00 39.53 ? 26  THR C CG2 1 
ATOM   6472  N  N   . VAL C  1 28  ? -31.622 -26.945 -30.876 1.00 31.98 ? 27  VAL C N   1 
ATOM   6473  C  CA  . VAL C  1 28  ? -30.861 -27.892 -30.050 1.00 31.00 ? 27  VAL C CA  1 
ATOM   6474  C  C   . VAL C  1 28  ? -31.050 -29.311 -30.582 1.00 31.44 ? 27  VAL C C   1 
ATOM   6475  O  O   . VAL C  1 28  ? -32.039 -29.607 -31.250 1.00 31.73 ? 27  VAL C O   1 
ATOM   6476  C  CB  . VAL C  1 28  ? -31.243 -27.840 -28.551 1.00 31.35 ? 27  VAL C CB  1 
ATOM   6477  C  CG1 . VAL C  1 28  ? -30.709 -26.576 -27.885 1.00 31.13 ? 27  VAL C CG1 1 
ATOM   6478  C  CG2 . VAL C  1 28  ? -32.758 -27.951 -28.345 1.00 32.50 ? 27  VAL C CG2 1 
ATOM   6479  N  N   . VAL C  1 29  ? -30.110 -30.195 -30.272 1.00 29.89 ? 28  VAL C N   1 
ATOM   6480  C  CA  . VAL C  1 29  ? -30.190 -31.585 -30.738 1.00 30.08 ? 28  VAL C CA  1 
ATOM   6481  C  C   . VAL C  1 29  ? -31.149 -32.486 -29.928 1.00 30.91 ? 28  VAL C C   1 
ATOM   6482  O  O   . VAL C  1 29  ? -31.639 -33.480 -30.453 1.00 31.81 ? 28  VAL C O   1 
ATOM   6483  C  CB  . VAL C  1 29  ? -28.788 -32.226 -30.833 1.00 29.58 ? 28  VAL C CB  1 
ATOM   6484  C  CG1 . VAL C  1 29  ? -27.900 -31.409 -31.765 1.00 29.79 ? 28  VAL C CG1 1 
ATOM   6485  C  CG2 . VAL C  1 29  ? -28.137 -32.356 -29.472 1.00 29.55 ? 28  VAL C CG2 1 
ATOM   6486  N  N   . HIS C  1 30  ? -31.398 -32.158 -28.661 1.00 31.15 ? 29  HIS C N   1 
ATOM   6487  C  CA  . HIS C  1 30  ? -32.413 -32.822 -27.824 1.00 32.48 ? 29  HIS C CA  1 
ATOM   6488  C  C   . HIS C  1 30  ? -33.142 -31.750 -27.031 1.00 33.94 ? 29  HIS C C   1 
ATOM   6489  O  O   . HIS C  1 30  ? -32.563 -30.717 -26.686 1.00 32.37 ? 29  HIS C O   1 
ATOM   6490  C  CB  . HIS C  1 30  ? -31.804 -33.789 -26.800 1.00 32.17 ? 29  HIS C CB  1 
ATOM   6491  C  CG  . HIS C  1 30  ? -30.962 -34.866 -27.408 1.00 31.59 ? 29  HIS C CG  1 
ATOM   6492  N  ND1 . HIS C  1 30  ? -31.430 -35.724 -28.383 1.00 32.37 ? 29  HIS C ND1 1 
ATOM   6493  C  CD2 . HIS C  1 30  ? -29.669 -35.205 -27.193 1.00 30.85 ? 29  HIS C CD2 1 
ATOM   6494  C  CE1 . HIS C  1 30  ? -30.455 -36.541 -28.750 1.00 31.84 ? 29  HIS C CE1 1 
ATOM   6495  N  NE2 . HIS C  1 30  ? -29.381 -36.254 -28.036 1.00 30.95 ? 29  HIS C NE2 1 
ATOM   6496  N  N   . TYR C  1 31  ? -34.385 -32.016 -26.680 1.00 34.35 ? 30  TYR C N   1 
ATOM   6497  C  CA  . TYR C  1 31  ? -35.106 -31.042 -25.872 1.00 36.48 ? 30  TYR C CA  1 
ATOM   6498  C  C   . TYR C  1 31  ? -34.513 -30.808 -24.513 1.00 36.25 ? 30  TYR C C   1 
ATOM   6499  O  O   . TYR C  1 31  ? -34.763 -29.778 -23.929 1.00 36.22 ? 30  TYR C O   1 
ATOM   6500  C  CB  . TYR C  1 31  ? -36.556 -31.359 -25.654 1.00 37.52 ? 30  TYR C CB  1 
ATOM   6501  C  CG  . TYR C  1 31  ? -37.333 -30.115 -25.194 1.00 38.65 ? 30  TYR C CG  1 
ATOM   6502  C  CD1 . TYR C  1 31  ? -37.348 -28.949 -25.966 1.00 38.70 ? 30  TYR C CD1 1 
ATOM   6503  C  CD2 . TYR C  1 31  ? -37.993 -30.079 -23.956 1.00 39.91 ? 30  TYR C CD2 1 
ATOM   6504  C  CE1 . TYR C  1 31  ? -38.044 -27.807 -25.550 1.00 40.41 ? 30  TYR C CE1 1 
ATOM   6505  C  CE2 . TYR C  1 31  ? -38.683 -28.938 -23.532 1.00 40.56 ? 30  TYR C CE2 1 
ATOM   6506  C  CZ  . TYR C  1 31  ? -38.706 -27.807 -24.330 1.00 40.22 ? 30  TYR C CZ  1 
ATOM   6507  O  OH  . TYR C  1 31  ? -39.381 -26.677 -23.907 1.00 41.36 ? 30  TYR C OH  1 
ATOM   6508  N  N   . LEU C  1 32  ? -33.805 -31.785 -23.969 1.00 37.09 ? 31  LEU C N   1 
ATOM   6509  C  CA  . LEU C  1 32  ? -33.200 -31.586 -22.650 1.00 38.18 ? 31  LEU C CA  1 
ATOM   6510  C  C   . LEU C  1 32  ? -31.981 -30.663 -22.703 1.00 35.70 ? 31  LEU C C   1 
ATOM   6511  O  O   . LEU C  1 32  ? -31.458 -30.301 -21.656 1.00 35.91 ? 31  LEU C O   1 
ATOM   6512  C  CB  . LEU C  1 32  ? -32.875 -32.933 -21.961 1.00 40.52 ? 31  LEU C CB  1 
ATOM   6513  C  CG  . LEU C  1 32  ? -32.088 -34.011 -22.717 1.00 41.80 ? 31  LEU C CG  1 
ATOM   6514  C  CD1 . LEU C  1 32  ? -30.642 -33.600 -22.886 1.00 41.93 ? 31  LEU C CD1 1 
ATOM   6515  C  CD2 . LEU C  1 32  ? -32.184 -35.351 -21.998 1.00 43.56 ? 31  LEU C CD2 1 
ATOM   6516  N  N   . CYS C  1 33  ? -31.537 -30.266 -23.898 1.00 34.75 ? 32  CYS C N   1 
ATOM   6517  C  CA  . CYS C  1 33  ? -30.420 -29.313 -24.031 1.00 34.50 ? 32  CYS C CA  1 
ATOM   6518  C  C   . CYS C  1 33  ? -30.941 -27.884 -23.828 1.00 34.87 ? 32  CYS C C   1 
ATOM   6519  O  O   . CYS C  1 33  ? -31.960 -27.512 -24.409 1.00 35.47 ? 32  CYS C O   1 
ATOM   6520  C  CB  . CYS C  1 33  ? -29.773 -29.392 -25.423 1.00 34.81 ? 32  CYS C CB  1 
ATOM   6521  S  SG  . CYS C  1 33  ? -29.185 -31.002 -26.026 1.00 37.37 ? 32  CYS C SG  1 
ATOM   6522  N  N   . SER C  1 34  ? -30.246 -27.074 -23.034 1.00 33.52 ? 33  SER C N   1 
ATOM   6523  C  CA  . SER C  1 34  ? -30.644 -25.672 -22.895 1.00 34.07 ? 33  SER C CA  1 
ATOM   6524  C  C   . SER C  1 34  ? -30.389 -24.900 -24.207 1.00 33.08 ? 33  SER C C   1 
ATOM   6525  O  O   . SER C  1 34  ? -29.317 -25.032 -24.827 1.00 29.38 ? 33  SER C O   1 
ATOM   6526  C  CB  . SER C  1 34  ? -29.872 -24.997 -21.776 1.00 34.98 ? 33  SER C CB  1 
ATOM   6527  O  OG  . SER C  1 34  ? -30.154 -25.552 -20.509 1.00 36.26 ? 33  SER C OG  1 
ATOM   6528  N  N   . LYS C  1 35  ? -31.367 -24.104 -24.622 1.00 32.18 ? 34  LYS C N   1 
ATOM   6529  C  CA  . LYS C  1 35  ? -31.229 -23.201 -25.767 1.00 33.62 ? 34  LYS C CA  1 
ATOM   6530  C  C   . LYS C  1 35  ? -30.553 -21.907 -25.396 1.00 33.08 ? 34  LYS C C   1 
ATOM   6531  O  O   . LYS C  1 35  ? -29.820 -21.326 -26.188 1.00 33.53 ? 34  LYS C O   1 
ATOM   6532  C  CB  . LYS C  1 35  ? -32.601 -22.822 -26.342 1.00 36.26 ? 34  LYS C CB  1 
ATOM   6533  C  CG  . LYS C  1 35  ? -32.974 -23.566 -27.590 1.00 37.95 ? 34  LYS C CG  1 
ATOM   6534  C  CD  . LYS C  1 35  ? -34.269 -23.052 -28.172 1.00 40.65 ? 34  LYS C CD  1 
ATOM   6535  C  CE  . LYS C  1 35  ? -34.339 -23.357 -29.653 1.00 41.81 ? 34  LYS C CE  1 
ATOM   6536  N  NZ  . LYS C  1 35  ? -35.666 -23.006 -30.225 1.00 45.00 ? 34  LYS C NZ  1 
ATOM   6537  N  N   . LYS C  1 36  ? -30.813 -21.447 -24.187 1.00 34.44 ? 35  LYS C N   1 
ATOM   6538  C  CA  . LYS C  1 36  ? -30.429 -20.116 -23.774 1.00 35.90 ? 35  LYS C CA  1 
ATOM   6539  C  C   . LYS C  1 36  ? -29.989 -20.136 -22.320 1.00 35.52 ? 35  LYS C C   1 
ATOM   6540  O  O   . LYS C  1 36  ? -30.619 -20.776 -21.489 1.00 35.87 ? 35  LYS C O   1 
ATOM   6541  C  CB  . LYS C  1 36  ? -31.639 -19.188 -23.947 1.00 40.14 ? 35  LYS C CB  1 
ATOM   6542  C  CG  . LYS C  1 36  ? -31.335 -17.713 -23.793 1.00 43.86 ? 35  LYS C CG  1 
ATOM   6543  C  CD  . LYS C  1 36  ? -32.611 -16.905 -24.001 1.00 48.72 ? 35  LYS C CD  1 
ATOM   6544  C  CE  . LYS C  1 36  ? -32.440 -15.463 -23.611 1.00 52.90 ? 35  LYS C CE  1 
ATOM   6545  N  NZ  . LYS C  1 36  ? -31.430 -14.764 -24.449 1.00 54.65 ? 35  LYS C NZ  1 
ATOM   6546  N  N   . THR C  1 37  ? -28.914 -19.423 -22.009 1.00 33.83 ? 36  THR C N   1 
ATOM   6547  C  CA  . THR C  1 37  ? -28.509 -19.207 -20.618 1.00 34.83 ? 36  THR C CA  1 
ATOM   6548  C  C   . THR C  1 37  ? -28.344 -17.708 -20.390 1.00 37.33 ? 36  THR C C   1 
ATOM   6549  O  O   . THR C  1 37  ? -27.922 -16.982 -21.298 1.00 37.48 ? 36  THR C O   1 
ATOM   6550  C  CB  . THR C  1 37  ? -27.171 -19.923 -20.274 1.00 33.14 ? 36  THR C CB  1 
ATOM   6551  O  OG1 . THR C  1 37  ? -26.109 -19.379 -21.068 1.00 29.28 ? 36  THR C OG1 1 
ATOM   6552  C  CG2 . THR C  1 37  ? -27.298 -21.419 -20.534 1.00 32.88 ? 36  THR C CG2 1 
ATOM   6553  N  N   . GLU C  1 38  ? -28.656 -17.251 -19.184 1.00 41.81 ? 37  GLU C N   1 
ATOM   6554  C  CA  . GLU C  1 38  ? -28.514 -15.829 -18.862 1.00 45.22 ? 37  GLU C CA  1 
ATOM   6555  C  C   . GLU C  1 38  ? -27.070 -15.434 -18.568 1.00 41.63 ? 37  GLU C C   1 
ATOM   6556  O  O   . GLU C  1 38  ? -26.707 -14.266 -18.695 1.00 41.87 ? 37  GLU C O   1 
ATOM   6557  C  CB  . GLU C  1 38  ? -29.434 -15.448 -17.704 1.00 50.62 ? 37  GLU C CB  1 
ATOM   6558  C  CG  . GLU C  1 38  ? -30.905 -15.714 -18.001 1.00 59.20 ? 37  GLU C CG  1 
ATOM   6559  C  CD  . GLU C  1 38  ? -31.410 -15.011 -19.267 1.00 65.61 ? 37  GLU C CD  1 
ATOM   6560  O  OE1 . GLU C  1 38  ? -31.012 -13.845 -19.509 1.00 72.61 ? 37  GLU C OE1 1 
ATOM   6561  O  OE2 . GLU C  1 38  ? -32.211 -15.619 -20.023 1.00 71.11 ? 37  GLU C OE2 1 
ATOM   6562  N  N   . SER C  1 39  ? -26.240 -16.397 -18.187 1.00 37.89 ? 38  SER C N   1 
ATOM   6563  C  CA  . SER C  1 39  ? -24.833 -16.117 -17.920 1.00 36.28 ? 38  SER C CA  1 
ATOM   6564  C  C   . SER C  1 39  ? -23.970 -17.266 -18.417 1.00 32.79 ? 38  SER C C   1 
ATOM   6565  O  O   . SER C  1 39  ? -24.474 -18.245 -18.964 1.00 30.76 ? 38  SER C O   1 
ATOM   6566  C  CB  . SER C  1 39  ? -24.608 -15.912 -16.432 1.00 39.45 ? 38  SER C CB  1 
ATOM   6567  O  OG  . SER C  1 39  ? -25.015 -17.073 -15.734 1.00 42.30 ? 38  SER C OG  1 
ATOM   6568  N  N   . TYR C  1 40  ? -22.671 -17.114 -18.259 1.00 29.97 ? 39  TYR C N   1 
ATOM   6569  C  CA  . TYR C  1 40  ? -21.726 -18.169 -18.618 1.00 29.44 ? 39  TYR C CA  1 
ATOM   6570  C  C   . TYR C  1 40  ? -21.805 -19.296 -17.606 1.00 29.22 ? 39  TYR C C   1 
ATOM   6571  O  O   . TYR C  1 40  ? -22.073 -19.055 -16.434 1.00 30.27 ? 39  TYR C O   1 
ATOM   6572  C  CB  . TYR C  1 40  ? -20.303 -17.621 -18.696 1.00 28.20 ? 39  TYR C CB  1 
ATOM   6573  C  CG  . TYR C  1 40  ? -20.068 -16.803 -19.943 1.00 28.90 ? 39  TYR C CG  1 
ATOM   6574  C  CD1 . TYR C  1 40  ? -20.445 -15.454 -19.996 1.00 30.70 ? 39  TYR C CD1 1 
ATOM   6575  C  CD2 . TYR C  1 40  ? -19.502 -17.370 -21.074 1.00 28.19 ? 39  TYR C CD2 1 
ATOM   6576  C  CE1 . TYR C  1 40  ? -20.241 -14.711 -21.148 1.00 30.80 ? 39  TYR C CE1 1 
ATOM   6577  C  CE2 . TYR C  1 40  ? -19.294 -16.632 -22.226 1.00 28.04 ? 39  TYR C CE2 1 
ATOM   6578  C  CZ  . TYR C  1 40  ? -19.674 -15.311 -22.256 1.00 30.07 ? 39  TYR C CZ  1 
ATOM   6579  O  OH  . TYR C  1 40  ? -19.455 -14.578 -23.384 1.00 30.79 ? 39  TYR C OH  1 
ATOM   6580  N  N   . PHE C  1 41  ? -21.587 -20.525 -18.069 1.00 27.13 ? 40  PHE C N   1 
ATOM   6581  C  CA  . PHE C  1 41  ? -21.485 -21.671 -17.192 1.00 26.16 ? 40  PHE C CA  1 
ATOM   6582  C  C   . PHE C  1 41  ? -20.224 -22.438 -17.586 1.00 24.73 ? 40  PHE C C   1 
ATOM   6583  O  O   . PHE C  1 41  ? -19.731 -22.278 -18.696 1.00 23.37 ? 40  PHE C O   1 
ATOM   6584  C  CB  . PHE C  1 41  ? -22.725 -22.567 -17.288 1.00 26.94 ? 40  PHE C CB  1 
ATOM   6585  C  CG  . PHE C  1 41  ? -22.921 -23.217 -18.631 1.00 27.74 ? 40  PHE C CG  1 
ATOM   6586  C  CD1 . PHE C  1 41  ? -23.535 -22.530 -19.676 1.00 28.15 ? 40  PHE C CD1 1 
ATOM   6587  C  CD2 . PHE C  1 41  ? -22.501 -24.521 -18.857 1.00 27.58 ? 40  PHE C CD2 1 
ATOM   6588  C  CE1 . PHE C  1 41  ? -23.718 -23.127 -20.920 1.00 29.13 ? 40  PHE C CE1 1 
ATOM   6589  C  CE2 . PHE C  1 41  ? -22.679 -25.118 -20.098 1.00 28.45 ? 40  PHE C CE2 1 
ATOM   6590  C  CZ  . PHE C  1 41  ? -23.288 -24.421 -21.135 1.00 29.05 ? 40  PHE C CZ  1 
ATOM   6591  N  N   . THR C  1 42  ? -19.745 -23.296 -16.691 1.00 23.46 ? 41  THR C N   1 
ATOM   6592  C  CA  . THR C  1 42  ? -18.557 -24.092 -16.966 1.00 23.22 ? 41  THR C CA  1 
ATOM   6593  C  C   . THR C  1 42  ? -18.871 -25.226 -17.936 1.00 23.07 ? 41  THR C C   1 
ATOM   6594  O  O   . THR C  1 42  ? -19.691 -26.107 -17.640 1.00 23.74 ? 41  THR C O   1 
ATOM   6595  C  CB  . THR C  1 42  ? -17.959 -24.645 -15.653 1.00 23.64 ? 41  THR C CB  1 
ATOM   6596  O  OG1 . THR C  1 42  ? -17.623 -23.546 -14.809 1.00 23.89 ? 41  THR C OG1 1 
ATOM   6597  C  CG2 . THR C  1 42  ? -16.699 -25.484 -15.936 1.00 22.53 ? 41  THR C CG2 1 
ATOM   6598  N  N   . ILE C  1 43  ? -18.251 -25.184 -19.116 1.00 21.60 ? 42  ILE C N   1 
ATOM   6599  C  CA  . ILE C  1 43  ? -18.431 -26.235 -20.119 1.00 21.60 ? 42  ILE C CA  1 
ATOM   6600  C  C   . ILE C  1 43  ? -17.312 -27.286 -20.089 1.00 20.89 ? 42  ILE C C   1 
ATOM   6601  O  O   . ILE C  1 43  ? -17.501 -28.434 -20.517 1.00 20.70 ? 42  ILE C O   1 
ATOM   6602  C  CB  . ILE C  1 43  ? -18.681 -25.629 -21.526 1.00 22.26 ? 42  ILE C CB  1 
ATOM   6603  C  CG1 . ILE C  1 43  ? -19.300 -26.681 -22.443 1.00 23.25 ? 42  ILE C CG1 1 
ATOM   6604  C  CG2 . ILE C  1 43  ? -17.426 -25.014 -22.137 1.00 21.69 ? 42  ILE C CG2 1 
ATOM   6605  C  CD1 . ILE C  1 43  ? -19.872 -26.118 -23.729 1.00 24.50 ? 42  ILE C CD1 1 
ATOM   6606  N  N   . TRP C  1 44  ? -16.162 -26.905 -19.539 1.00 19.97 ? 43  TRP C N   1 
ATOM   6607  C  CA  . TRP C  1 44  ? -15.094 -27.874 -19.211 1.00 19.29 ? 43  TRP C CA  1 
ATOM   6608  C  C   . TRP C  1 44  ? -14.429 -27.408 -17.919 1.00 19.05 ? 43  TRP C C   1 
ATOM   6609  O  O   . TRP C  1 44  ? -14.032 -26.252 -17.847 1.00 17.40 ? 43  TRP C O   1 
ATOM   6610  C  CB  . TRP C  1 44  ? -14.052 -27.899 -20.319 1.00 19.16 ? 43  TRP C CB  1 
ATOM   6611  C  CG  . TRP C  1 44  ? -12.946 -28.866 -20.057 1.00 18.35 ? 43  TRP C CG  1 
ATOM   6612  C  CD1 . TRP C  1 44  ? -11.702 -28.587 -19.589 1.00 18.49 ? 43  TRP C CD1 1 
ATOM   6613  C  CD2 . TRP C  1 44  ? -13.015 -30.282 -20.206 1.00 18.98 ? 43  TRP C CD2 1 
ATOM   6614  N  NE1 . TRP C  1 44  ? -10.961 -29.743 -19.488 1.00 18.14 ? 43  TRP C NE1 1 
ATOM   6615  C  CE2 . TRP C  1 44  ? -11.756 -30.804 -19.844 1.00 19.16 ? 43  TRP C CE2 1 
ATOM   6616  C  CE3 . TRP C  1 44  ? -14.021 -31.166 -20.632 1.00 20.59 ? 43  TRP C CE3 1 
ATOM   6617  C  CZ2 . TRP C  1 44  ? -11.476 -32.173 -19.896 1.00 19.63 ? 43  TRP C CZ2 1 
ATOM   6618  C  CZ3 . TRP C  1 44  ? -13.739 -32.517 -20.699 1.00 20.77 ? 43  TRP C CZ3 1 
ATOM   6619  C  CH2 . TRP C  1 44  ? -12.476 -33.009 -20.332 1.00 20.58 ? 43  TRP C CH2 1 
ATOM   6620  N  N   . LEU C  1 45  ? -14.286 -28.253 -16.899 1.00 20.90 ? 44  LEU C N   1 
ATOM   6621  C  CA  . LEU C  1 45  ? -14.730 -29.654 -16.826 1.00 22.42 ? 44  LEU C CA  1 
ATOM   6622  C  C   . LEU C  1 45  ? -15.953 -29.730 -15.908 1.00 24.75 ? 44  LEU C C   1 
ATOM   6623  O  O   . LEU C  1 45  ? -15.911 -29.328 -14.744 1.00 23.18 ? 44  LEU C O   1 
ATOM   6624  C  CB  . LEU C  1 45  ? -13.608 -30.531 -16.249 1.00 24.62 ? 44  LEU C CB  1 
ATOM   6625  C  CG  . LEU C  1 45  ? -13.924 -31.991 -15.896 1.00 25.71 ? 44  LEU C CG  1 
ATOM   6626  C  CD1 . LEU C  1 45  ? -14.381 -32.732 -17.138 1.00 26.44 ? 44  LEU C CD1 1 
ATOM   6627  C  CD2 . LEU C  1 45  ? -12.697 -32.668 -15.308 1.00 26.77 ? 44  LEU C CD2 1 
ATOM   6628  N  N   . ASN C  1 46  ? -17.042 -30.261 -16.440 1.00 26.30 ? 45  ASN C N   1 
ATOM   6629  C  CA  . ASN C  1 46  ? -18.222 -30.580 -15.616 1.00 29.20 ? 45  ASN C CA  1 
ATOM   6630  C  C   . ASN C  1 46  ? -18.704 -31.951 -16.026 1.00 31.74 ? 45  ASN C C   1 
ATOM   6631  O  O   . ASN C  1 46  ? -19.174 -32.162 -17.157 1.00 28.22 ? 45  ASN C O   1 
ATOM   6632  C  CB  . ASN C  1 46  ? -19.312 -29.551 -15.775 1.00 30.71 ? 45  ASN C CB  1 
ATOM   6633  C  CG  . ASN C  1 46  ? -20.583 -29.922 -15.013 1.00 33.40 ? 45  ASN C CG  1 
ATOM   6634  O  OD1 . ASN C  1 46  ? -20.745 -31.046 -14.525 1.00 36.09 ? 45  ASN C OD1 1 
ATOM   6635  N  ND2 . ASN C  1 46  ? -21.474 -28.992 -14.921 1.00 33.42 ? 45  ASN C ND2 1 
ATOM   6636  N  N   . LEU C  1 47  ? -18.559 -32.893 -15.097 1.00 36.48 ? 46  LEU C N   1 
ATOM   6637  C  CA  . LEU C  1 47  ? -18.795 -34.307 -15.372 1.00 41.49 ? 46  LEU C CA  1 
ATOM   6638  C  C   . LEU C  1 47  ? -20.247 -34.594 -15.734 1.00 40.01 ? 46  LEU C C   1 
ATOM   6639  O  O   . LEU C  1 47  ? -20.534 -35.508 -16.488 1.00 42.18 ? 46  LEU C O   1 
ATOM   6640  C  CB  . LEU C  1 47  ? -18.416 -35.149 -14.149 1.00 44.25 ? 46  LEU C CB  1 
ATOM   6641  C  CG  . LEU C  1 47  ? -16.935 -35.128 -13.779 1.00 46.63 ? 46  LEU C CG  1 
ATOM   6642  C  CD1 . LEU C  1 47  ? -16.766 -35.885 -12.464 1.00 50.11 ? 46  LEU C CD1 1 
ATOM   6643  C  CD2 . LEU C  1 47  ? -16.106 -35.743 -14.895 1.00 46.13 ? 46  LEU C CD2 1 
ATOM   6644  N  N   . GLU C  1 48  ? -21.156 -33.793 -15.221 1.00 42.47 ? 47  GLU C N   1 
ATOM   6645  C  CA  . GLU C  1 48  ? -22.570 -34.026 -15.481 1.00 45.28 ? 47  GLU C CA  1 
ATOM   6646  C  C   . GLU C  1 48  ? -22.964 -33.759 -16.936 1.00 43.24 ? 47  GLU C C   1 
ATOM   6647  O  O   . GLU C  1 48  ? -24.008 -34.232 -17.390 1.00 42.47 ? 47  GLU C O   1 
ATOM   6648  C  CB  . GLU C  1 48  ? -23.411 -33.196 -14.526 1.00 49.26 ? 47  GLU C CB  1 
ATOM   6649  C  CG  . GLU C  1 48  ? -23.253 -33.678 -13.093 1.00 55.75 ? 47  GLU C CG  1 
ATOM   6650  C  CD  . GLU C  1 48  ? -24.093 -32.902 -12.114 1.00 62.41 ? 47  GLU C CD  1 
ATOM   6651  O  OE1 . GLU C  1 48  ? -24.369 -31.705 -12.373 1.00 69.46 ? 47  GLU C OE1 1 
ATOM   6652  O  OE2 . GLU C  1 48  ? -24.471 -33.494 -11.076 1.00 71.65 ? 47  GLU C OE2 1 
ATOM   6653  N  N   . LEU C  1 49  ? -22.132 -33.016 -17.670 1.00 36.89 ? 48  LEU C N   1 
ATOM   6654  C  CA  . LEU C  1 49  ? -22.412 -32.715 -19.074 1.00 34.85 ? 48  LEU C CA  1 
ATOM   6655  C  C   . LEU C  1 49  ? -21.987 -33.844 -19.994 1.00 33.75 ? 48  LEU C C   1 
ATOM   6656  O  O   . LEU C  1 49  ? -22.302 -33.825 -21.189 1.00 32.85 ? 48  LEU C O   1 
ATOM   6657  C  CB  . LEU C  1 49  ? -21.719 -31.408 -19.492 1.00 32.42 ? 48  LEU C CB  1 
ATOM   6658  C  CG  . LEU C  1 49  ? -21.984 -30.174 -18.643 1.00 32.95 ? 48  LEU C CG  1 
ATOM   6659  C  CD1 . LEU C  1 49  ? -21.224 -28.983 -19.202 1.00 32.36 ? 48  LEU C CD1 1 
ATOM   6660  C  CD2 . LEU C  1 49  ? -23.480 -29.852 -18.531 1.00 34.48 ? 48  LEU C CD2 1 
ATOM   6661  N  N   . LEU C  1 50  ? -21.252 -34.820 -19.457 1.00 34.07 ? 49  LEU C N   1 
ATOM   6662  C  CA  . LEU C  1 50  ? -20.678 -35.903 -20.255 1.00 34.62 ? 49  LEU C CA  1 
ATOM   6663  C  C   . LEU C  1 50  ? -21.454 -37.245 -20.148 1.00 35.81 ? 49  LEU C C   1 
ATOM   6664  O  O   . LEU C  1 50  ? -21.078 -38.237 -20.775 1.00 35.89 ? 49  LEU C O   1 
ATOM   6665  C  CB  . LEU C  1 50  ? -19.205 -36.105 -19.853 1.00 35.48 ? 49  LEU C CB  1 
ATOM   6666  C  CG  . LEU C  1 50  ? -18.363 -34.812 -19.822 1.00 36.56 ? 49  LEU C CG  1 
ATOM   6667  C  CD1 . LEU C  1 50  ? -16.944 -35.061 -19.323 1.00 36.17 ? 49  LEU C CD1 1 
ATOM   6668  C  CD2 . LEU C  1 50  ? -18.336 -34.191 -21.202 1.00 34.70 ? 49  LEU C CD2 1 
ATOM   6669  N  N   . LEU C  1 51  ? -22.555 -37.256 -19.416 1.00 37.31 ? 50  LEU C N   1 
ATOM   6670  C  CA  . LEU C  1 51  ? -23.385 -38.464 -19.278 1.00 38.27 ? 50  LEU C CA  1 
ATOM   6671  C  C   . LEU C  1 51  ? -24.091 -38.811 -20.605 1.00 38.71 ? 50  LEU C C   1 
ATOM   6672  O  O   . LEU C  1 51  ? -24.234 -37.951 -21.474 1.00 37.16 ? 50  LEU C O   1 
ATOM   6673  C  CB  . LEU C  1 51  ? -24.429 -38.238 -18.193 1.00 40.78 ? 50  LEU C CB  1 
ATOM   6674  C  CG  . LEU C  1 51  ? -23.887 -37.986 -16.777 1.00 42.74 ? 50  LEU C CG  1 
ATOM   6675  C  CD1 . LEU C  1 51  ? -24.946 -37.371 -15.875 1.00 43.49 ? 50  LEU C CD1 1 
ATOM   6676  C  CD2 . LEU C  1 51  ? -23.342 -39.269 -16.173 1.00 44.52 ? 50  LEU C CD2 1 
ATOM   6677  N  N   . PRO C  1 52  ? -24.522 -40.082 -20.782 1.00 38.86 ? 51  PRO C N   1 
ATOM   6678  C  CA  . PRO C  1 52  ? -25.211 -40.456 -22.026 1.00 37.50 ? 51  PRO C CA  1 
ATOM   6679  C  C   . PRO C  1 52  ? -26.358 -39.502 -22.346 1.00 34.74 ? 51  PRO C C   1 
ATOM   6680  O  O   . PRO C  1 52  ? -27.005 -39.011 -21.434 1.00 34.63 ? 51  PRO C O   1 
ATOM   6681  C  CB  . PRO C  1 52  ? -25.749 -41.862 -21.727 1.00 39.69 ? 51  PRO C CB  1 
ATOM   6682  C  CG  . PRO C  1 52  ? -24.827 -42.405 -20.683 1.00 40.36 ? 51  PRO C CG  1 
ATOM   6683  C  CD  . PRO C  1 52  ? -24.344 -41.233 -19.874 1.00 39.88 ? 51  PRO C CD  1 
ATOM   6684  N  N   . VAL C  1 53  ? -26.558 -39.232 -23.636 1.00 34.06 ? 52  VAL C N   1 
ATOM   6685  C  CA  . VAL C  1 53  ? -27.588 -38.311 -24.155 1.00 33.94 ? 52  VAL C CA  1 
ATOM   6686  C  C   . VAL C  1 53  ? -27.241 -36.840 -23.930 1.00 32.05 ? 52  VAL C C   1 
ATOM   6687  O  O   . VAL C  1 53  ? -27.177 -36.072 -24.885 1.00 30.51 ? 52  VAL C O   1 
ATOM   6688  C  CB  . VAL C  1 53  ? -29.004 -38.631 -23.618 1.00 36.83 ? 52  VAL C CB  1 
ATOM   6689  C  CG1 . VAL C  1 53  ? -30.062 -37.770 -24.311 1.00 37.99 ? 52  VAL C CG1 1 
ATOM   6690  C  CG2 . VAL C  1 53  ? -29.329 -40.106 -23.830 1.00 37.99 ? 52  VAL C CG2 1 
ATOM   6691  N  N   . ILE C  1 54  ? -27.043 -36.454 -22.677 1.00 31.79 ? 53  ILE C N   1 
ATOM   6692  C  CA  . ILE C  1 54  ? -26.615 -35.098 -22.327 1.00 32.12 ? 53  ILE C CA  1 
ATOM   6693  C  C   . ILE C  1 54  ? -25.301 -34.750 -23.055 1.00 29.52 ? 53  ILE C C   1 
ATOM   6694  O  O   . ILE C  1 54  ? -25.082 -33.606 -23.464 1.00 28.18 ? 53  ILE C O   1 
ATOM   6695  C  CB  . ILE C  1 54  ? -26.462 -34.944 -20.782 1.00 34.85 ? 53  ILE C CB  1 
ATOM   6696  C  CG1 . ILE C  1 54  ? -27.809 -35.234 -20.080 1.00 40.45 ? 53  ILE C CG1 1 
ATOM   6697  C  CG2 . ILE C  1 54  ? -26.001 -33.547 -20.384 1.00 34.92 ? 53  ILE C CG2 1 
ATOM   6698  C  CD1 . ILE C  1 54  ? -27.731 -35.553 -18.598 1.00 43.60 ? 53  ILE C CD1 1 
ATOM   6699  N  N   . ILE C  1 55  ? -24.455 -35.741 -23.269 1.00 27.64 ? 54  ILE C N   1 
ATOM   6700  C  CA  . ILE C  1 55  ? -23.199 -35.504 -23.982 1.00 27.02 ? 54  ILE C CA  1 
ATOM   6701  C  C   . ILE C  1 55  ? -23.404 -34.954 -25.400 1.00 25.33 ? 54  ILE C C   1 
ATOM   6702  O  O   . ILE C  1 55  ? -22.539 -34.247 -25.919 1.00 23.58 ? 54  ILE C O   1 
ATOM   6703  C  CB  . ILE C  1 55  ? -22.297 -36.769 -24.028 1.00 28.15 ? 54  ILE C CB  1 
ATOM   6704  C  CG1 . ILE C  1 55  ? -20.894 -36.375 -24.496 1.00 29.18 ? 54  ILE C CG1 1 
ATOM   6705  C  CG2 . ILE C  1 55  ? -22.883 -37.844 -24.926 1.00 29.15 ? 54  ILE C CG2 1 
ATOM   6706  C  CD1 . ILE C  1 55  ? -19.787 -37.272 -23.991 1.00 31.41 ? 54  ILE C CD1 1 
ATOM   6707  N  N   . ASP C  1 56  ? -24.534 -35.259 -26.031 1.00 24.95 ? 55  ASP C N   1 
ATOM   6708  C  CA  . ASP C  1 56  ? -24.808 -34.701 -27.365 1.00 25.38 ? 55  ASP C CA  1 
ATOM   6709  C  C   . ASP C  1 56  ? -24.968 -33.169 -27.293 1.00 24.95 ? 55  ASP C C   1 
ATOM   6710  O  O   . ASP C  1 56  ? -24.556 -32.456 -28.219 1.00 24.28 ? 55  ASP C O   1 
ATOM   6711  C  CB  . ASP C  1 56  ? -26.075 -35.309 -27.986 1.00 27.28 ? 55  ASP C CB  1 
ATOM   6712  C  CG  . ASP C  1 56  ? -25.960 -36.793 -28.254 1.00 28.87 ? 55  ASP C CG  1 
ATOM   6713  O  OD1 . ASP C  1 56  ? -24.865 -37.265 -28.629 1.00 29.36 ? 55  ASP C OD1 1 
ATOM   6714  O  OD2 . ASP C  1 56  ? -26.985 -37.496 -28.123 1.00 30.06 ? 55  ASP C OD2 1 
ATOM   6715  N  N   . CYS C  1 57  ? -25.579 -32.685 -26.203 1.00 25.38 ? 56  CYS C N   1 
ATOM   6716  C  CA  . CYS C  1 57  ? -25.679 -31.243 -25.946 1.00 26.24 ? 56  CYS C CA  1 
ATOM   6717  C  C   . CYS C  1 57  ? -24.286 -30.608 -25.796 1.00 24.66 ? 56  CYS C C   1 
ATOM   6718  O  O   . CYS C  1 57  ? -24.004 -29.550 -26.374 1.00 23.61 ? 56  CYS C O   1 
ATOM   6719  C  CB  . CYS C  1 57  ? -26.452 -30.958 -24.669 1.00 28.47 ? 56  CYS C CB  1 
ATOM   6720  S  SG  . CYS C  1 57  ? -28.048 -31.800 -24.511 1.00 33.62 ? 56  CYS C SG  1 
ATOM   6721  N  N   . TRP C  1 58  ? -23.437 -31.261 -25.009 1.00 23.00 ? 57  TRP C N   1 
ATOM   6722  C  CA  . TRP C  1 58  ? -22.072 -30.788 -24.789 1.00 22.60 ? 57  TRP C CA  1 
ATOM   6723  C  C   . TRP C  1 58  ? -21.295 -30.712 -26.104 1.00 21.87 ? 57  TRP C C   1 
ATOM   6724  O  O   . TRP C  1 58  ? -20.691 -29.686 -26.406 1.00 22.17 ? 57  TRP C O   1 
ATOM   6725  C  CB  . TRP C  1 58  ? -21.377 -31.709 -23.796 1.00 22.47 ? 57  TRP C CB  1 
ATOM   6726  C  CG  . TRP C  1 58  ? -20.004 -31.338 -23.469 1.00 21.37 ? 57  TRP C CG  1 
ATOM   6727  C  CD1 . TRP C  1 58  ? -19.602 -30.367 -22.604 1.00 21.39 ? 57  TRP C CD1 1 
ATOM   6728  C  CD2 . TRP C  1 58  ? -18.804 -31.944 -23.977 1.00 21.25 ? 57  TRP C CD2 1 
ATOM   6729  N  NE1 . TRP C  1 58  ? -18.240 -30.322 -22.555 1.00 21.06 ? 57  TRP C NE1 1 
ATOM   6730  C  CE2 . TRP C  1 58  ? -17.718 -31.277 -23.377 1.00 20.64 ? 57  TRP C CE2 1 
ATOM   6731  C  CE3 . TRP C  1 58  ? -18.551 -32.993 -24.858 1.00 20.93 ? 57  TRP C CE3 1 
ATOM   6732  C  CZ2 . TRP C  1 58  ? -16.390 -31.632 -23.625 1.00 20.48 ? 57  TRP C CZ2 1 
ATOM   6733  C  CZ3 . TRP C  1 58  ? -17.249 -33.333 -25.117 1.00 21.22 ? 57  TRP C CZ3 1 
ATOM   6734  C  CH2 . TRP C  1 58  ? -16.177 -32.644 -24.513 1.00 20.25 ? 57  TRP C CH2 1 
ATOM   6735  N  N   . ILE C  1 59  ? -21.328 -31.790 -26.887 1.00 21.50 ? 58  ILE C N   1 
ATOM   6736  C  CA  A ILE C  1 59  ? -20.667 -31.823 -28.184 0.50 21.27 ? 58  ILE C CA  1 
ATOM   6737  C  CA  B ILE C  1 59  ? -20.670 -31.824 -28.185 0.50 21.34 ? 58  ILE C CA  1 
ATOM   6738  C  C   . ILE C  1 59  ? -21.172 -30.680 -29.073 1.00 21.79 ? 58  ILE C C   1 
ATOM   6739  O  O   . ILE C  1 59  ? -20.380 -29.983 -29.729 1.00 20.37 ? 58  ILE C O   1 
ATOM   6740  C  CB  A ILE C  1 59  ? -20.873 -33.178 -28.896 0.50 22.05 ? 58  ILE C CB  1 
ATOM   6741  C  CB  B ILE C  1 59  ? -20.926 -33.156 -28.926 0.50 22.19 ? 58  ILE C CB  1 
ATOM   6742  C  CG1 A ILE C  1 59  ? -20.135 -34.296 -28.120 0.50 22.22 ? 58  ILE C CG1 1 
ATOM   6743  C  CG1 B ILE C  1 59  ? -20.259 -34.337 -28.238 0.50 22.50 ? 58  ILE C CG1 1 
ATOM   6744  C  CG2 A ILE C  1 59  ? -20.394 -33.093 -30.332 0.50 22.11 ? 58  ILE C CG2 1 
ATOM   6745  C  CG2 B ILE C  1 59  ? -20.380 -33.088 -30.326 0.50 22.23 ? 58  ILE C CG2 1 
ATOM   6746  C  CD1 A ILE C  1 59  ? -20.393 -35.713 -28.613 0.50 22.47 ? 58  ILE C CD1 1 
ATOM   6747  C  CD1 B ILE C  1 59  ? -18.779 -34.212 -28.133 0.50 21.71 ? 58  ILE C CD1 1 
ATOM   6748  N  N   . ASP C  1 60  ? -22.495 -30.467 -29.087 1.00 21.51 ? 59  ASP C N   1 
ATOM   6749  C  CA  . ASP C  1 60  ? -23.054 -29.429 -29.932 1.00 22.55 ? 59  ASP C CA  1 
ATOM   6750  C  C   . ASP C  1 60  ? -22.578 -28.029 -29.555 1.00 22.45 ? 59  ASP C C   1 
ATOM   6751  O  O   . ASP C  1 60  ? -22.531 -27.140 -30.424 1.00 23.99 ? 59  ASP C O   1 
ATOM   6752  C  CB  . ASP C  1 60  ? -24.605 -29.467 -29.931 1.00 24.35 ? 59  ASP C CB  1 
ATOM   6753  C  CG  . ASP C  1 60  ? -25.194 -28.709 -31.113 1.00 26.11 ? 59  ASP C CG  1 
ATOM   6754  O  OD1 . ASP C  1 60  ? -24.742 -28.952 -32.255 1.00 27.22 ? 59  ASP C OD1 1 
ATOM   6755  O  OD2 . ASP C  1 60  ? -26.108 -27.883 -30.926 1.00 27.47 ? 59  ASP C OD2 1 
ATOM   6756  N  N   . ASN C  1 61  ? -22.218 -27.819 -28.284 1.00 21.92 ? 60  ASN C N   1 
ATOM   6757  C  CA  . ASN C  1 61  ? -21.743 -26.519 -27.812 1.00 21.47 ? 60  ASN C CA  1 
ATOM   6758  C  C   . ASN C  1 61  ? -20.231 -26.343 -27.889 1.00 21.13 ? 60  ASN C C   1 
ATOM   6759  O  O   . ASN C  1 61  ? -19.741 -25.233 -28.116 1.00 21.38 ? 60  ASN C O   1 
ATOM   6760  C  CB  . ASN C  1 61  ? -22.187 -26.277 -26.364 1.00 21.88 ? 60  ASN C CB  1 
ATOM   6761  C  CG  . ASN C  1 61  ? -23.678 -26.014 -26.256 1.00 23.08 ? 60  ASN C CG  1 
ATOM   6762  O  OD1 . ASN C  1 61  ? -24.275 -25.449 -27.179 1.00 23.39 ? 60  ASN C OD1 1 
ATOM   6763  N  ND2 . ASN C  1 61  ? -24.282 -26.437 -25.166 1.00 23.06 ? 60  ASN C ND2 1 
ATOM   6764  N  N   . ILE C  1 62  ? -19.493 -27.416 -27.640 1.00 20.98 ? 61  ILE C N   1 
ATOM   6765  C  CA  . ILE C  1 62  ? -18.035 -27.295 -27.513 1.00 20.76 ? 61  ILE C CA  1 
ATOM   6766  C  C   . ILE C  1 62  ? -17.300 -27.589 -28.819 1.00 20.68 ? 61  ILE C C   1 
ATOM   6767  O  O   . ILE C  1 62  ? -16.085 -27.316 -28.935 1.00 20.99 ? 61  ILE C O   1 
ATOM   6768  C  CB  . ILE C  1 62  ? -17.501 -28.182 -26.362 1.00 22.12 ? 61  ILE C CB  1 
ATOM   6769  C  CG1 . ILE C  1 62  ? -16.161 -27.623 -25.846 1.00 22.90 ? 61  ILE C CG1 1 
ATOM   6770  C  CG2 . ILE C  1 62  ? -17.379 -29.641 -26.802 1.00 21.86 ? 61  ILE C CG2 1 
ATOM   6771  C  CD1 . ILE C  1 62  ? -15.691 -28.241 -24.544 1.00 24.43 ? 61  ILE C CD1 1 
ATOM   6772  N  N   . ARG C  1 63  ? -17.989 -28.166 -29.793 1.00 20.42 ? 62  ARG C N   1 
ATOM   6773  C  CA  . ARG C  1 63  ? -17.392 -28.370 -31.104 1.00 20.70 ? 62  ARG C CA  1 
ATOM   6774  C  C   . ARG C  1 63  ? -17.041 -27.020 -31.735 1.00 20.57 ? 62  ARG C C   1 
ATOM   6775  O  O   . ARG C  1 63  ? -17.684 -26.013 -31.470 1.00 19.56 ? 62  ARG C O   1 
ATOM   6776  C  CB  . ARG C  1 63  ? -18.331 -29.146 -32.032 1.00 22.11 ? 62  ARG C CB  1 
ATOM   6777  C  CG  . ARG C  1 63  ? -19.543 -28.344 -32.486 1.00 23.94 ? 62  ARG C CG  1 
ATOM   6778  C  CD  . ARG C  1 63  ? -20.596 -29.223 -33.131 1.00 26.84 ? 62  ARG C CD  1 
ATOM   6779  N  NE  . ARG C  1 63  ? -21.814 -28.445 -33.389 1.00 28.97 ? 62  ARG C NE  1 
ATOM   6780  C  CZ  . ARG C  1 63  ? -22.095 -27.789 -34.515 1.00 31.07 ? 62  ARG C CZ  1 
ATOM   6781  N  NH1 . ARG C  1 63  ? -21.261 -27.794 -35.551 1.00 31.46 ? 62  ARG C NH1 1 
ATOM   6782  N  NH2 . ARG C  1 63  ? -23.245 -27.125 -34.613 1.00 33.75 ? 62  ARG C NH2 1 
ATOM   6783  N  N   . LEU C  1 64  ? -15.979 -27.020 -32.548 1.00 21.14 ? 63  LEU C N   1 
ATOM   6784  C  CA  . LEU C  1 64  ? -15.712 -25.929 -33.462 1.00 21.21 ? 63  LEU C CA  1 
ATOM   6785  C  C   . LEU C  1 64  ? -16.303 -26.235 -34.856 1.00 21.92 ? 63  LEU C C   1 
ATOM   6786  O  O   . LEU C  1 64  ? -16.313 -27.387 -35.298 1.00 22.23 ? 63  LEU C O   1 
ATOM   6787  C  CB  . LEU C  1 64  ? -14.214 -25.704 -33.571 1.00 20.19 ? 63  LEU C CB  1 
ATOM   6788  C  CG  . LEU C  1 64  ? -13.472 -25.225 -32.315 1.00 20.55 ? 63  LEU C CG  1 
ATOM   6789  C  CD1 . LEU C  1 64  ? -11.998 -25.134 -32.640 1.00 20.99 ? 63  LEU C CD1 1 
ATOM   6790  C  CD2 . LEU C  1 64  ? -14.000 -23.867 -31.866 1.00 21.10 ? 63  LEU C CD2 1 
ATOM   6791  N  N   . VAL C  1 65  ? -16.769 -25.193 -35.536 1.00 22.09 ? 64  VAL C N   1 
ATOM   6792  C  CA  . VAL C  1 65  ? -17.220 -25.275 -36.925 1.00 23.95 ? 64  VAL C CA  1 
ATOM   6793  C  C   . VAL C  1 65  ? -16.074 -24.810 -37.833 1.00 24.03 ? 64  VAL C C   1 
ATOM   6794  O  O   . VAL C  1 65  ? -15.569 -23.701 -37.670 1.00 24.92 ? 64  VAL C O   1 
ATOM   6795  C  CB  . VAL C  1 65  ? -18.428 -24.350 -37.157 1.00 26.63 ? 64  VAL C CB  1 
ATOM   6796  C  CG1 . VAL C  1 65  ? -18.867 -24.361 -38.625 1.00 27.74 ? 64  VAL C CG1 1 
ATOM   6797  C  CG2 . VAL C  1 65  ? -19.592 -24.772 -36.260 1.00 27.58 ? 64  VAL C CG2 1 
ATOM   6798  N  N   . TYR C  1 66  ? -15.650 -25.656 -38.770 1.00 24.13 ? 65  TYR C N   1 
ATOM   6799  C  CA  . TYR C  1 66  ? -14.598 -25.275 -39.712 1.00 23.85 ? 65  TYR C CA  1 
ATOM   6800  C  C   . TYR C  1 66  ? -15.228 -24.635 -40.965 1.00 25.95 ? 65  TYR C C   1 
ATOM   6801  O  O   . TYR C  1 66  ? -16.063 -25.232 -41.627 1.00 26.54 ? 65  TYR C O   1 
ATOM   6802  C  CB  . TYR C  1 66  ? -13.722 -26.476 -40.090 1.00 23.58 ? 65  TYR C CB  1 
ATOM   6803  C  CG  . TYR C  1 66  ? -12.481 -26.029 -40.836 1.00 22.77 ? 65  TYR C CG  1 
ATOM   6804  C  CD1 . TYR C  1 66  ? -11.368 -25.562 -40.146 1.00 21.86 ? 65  TYR C CD1 1 
ATOM   6805  C  CD2 . TYR C  1 66  ? -12.444 -26.012 -42.231 1.00 22.77 ? 65  TYR C CD2 1 
ATOM   6806  C  CE1 . TYR C  1 66  ? -10.245 -25.109 -40.822 1.00 21.38 ? 65  TYR C CE1 1 
ATOM   6807  C  CE2 . TYR C  1 66  ? -11.313 -25.565 -42.907 1.00 22.36 ? 65  TYR C CE2 1 
ATOM   6808  C  CZ  . TYR C  1 66  ? -10.225 -25.115 -42.202 1.00 21.83 ? 65  TYR C CZ  1 
ATOM   6809  O  OH  . TYR C  1 66  ? -9.120  -24.639 -42.874 1.00 23.00 ? 65  TYR C OH  1 
ATOM   6810  N  N   . ASN C  1 67  ? -14.826 -23.413 -41.280 1.00 26.74 ? 66  ASN C N   1 
ATOM   6811  C  CA  . ASN C  1 67  ? -15.329 -22.698 -42.441 1.00 29.42 ? 66  ASN C CA  1 
ATOM   6812  C  C   . ASN C  1 67  ? -14.280 -22.801 -43.548 1.00 29.23 ? 66  ASN C C   1 
ATOM   6813  O  O   . ASN C  1 67  ? -13.203 -22.214 -43.445 1.00 28.60 ? 66  ASN C O   1 
ATOM   6814  C  CB  . ASN C  1 67  ? -15.609 -21.246 -42.029 1.00 30.58 ? 66  ASN C CB  1 
ATOM   6815  C  CG  . ASN C  1 67  ? -16.142 -20.378 -43.169 1.00 33.56 ? 66  ASN C CG  1 
ATOM   6816  O  OD1 . ASN C  1 67  ? -15.833 -20.595 -44.336 1.00 32.80 ? 66  ASN C OD1 1 
ATOM   6817  N  ND2 . ASN C  1 67  ? -16.945 -19.378 -42.828 1.00 36.90 ? 66  ASN C ND2 1 
ATOM   6818  N  N   . LYS C  1 68  ? -14.601 -23.551 -44.596 1.00 31.46 ? 67  LYS C N   1 
ATOM   6819  C  CA  . LYS C  1 68  ? -13.660 -23.807 -45.695 1.00 34.03 ? 67  LYS C CA  1 
ATOM   6820  C  C   . LYS C  1 68  ? -13.321 -22.561 -46.520 1.00 35.47 ? 67  LYS C C   1 
ATOM   6821  O  O   . LYS C  1 68  ? -12.252 -22.494 -47.107 1.00 37.62 ? 67  LYS C O   1 
ATOM   6822  C  CB  . LYS C  1 68  ? -14.200 -24.880 -46.642 1.00 36.19 ? 67  LYS C CB  1 
ATOM   6823  C  CG  . LYS C  1 68  ? -14.362 -26.260 -46.040 1.00 38.73 ? 67  LYS C CG  1 
ATOM   6824  C  CD  . LYS C  1 68  ? -14.987 -27.198 -47.063 1.00 41.96 ? 67  LYS C CD  1 
ATOM   6825  C  CE  . LYS C  1 68  ? -14.947 -28.647 -46.622 1.00 45.01 ? 67  LYS C CE  1 
ATOM   6826  N  NZ  . LYS C  1 68  ? -15.935 -28.953 -45.543 1.00 46.98 ? 67  LYS C NZ  1 
ATOM   6827  N  N   . THR C  1 69  ? -14.216 -21.579 -46.553 1.00 36.15 ? 68  THR C N   1 
ATOM   6828  C  CA  . THR C  1 69  ? -13.978 -20.333 -47.288 1.00 36.77 ? 68  THR C CA  1 
ATOM   6829  C  C   . THR C  1 69  ? -12.943 -19.462 -46.594 1.00 35.98 ? 68  THR C C   1 
ATOM   6830  O  O   . THR C  1 69  ? -11.998 -18.992 -47.209 1.00 38.41 ? 68  THR C O   1 
ATOM   6831  C  CB  . THR C  1 69  ? -15.291 -19.526 -47.422 1.00 38.92 ? 68  THR C CB  1 
ATOM   6832  O  OG1 . THR C  1 69  ? -16.294 -20.364 -48.007 1.00 39.94 ? 68  THR C OG1 1 
ATOM   6833  C  CG2 . THR C  1 69  ? -15.094 -18.281 -48.278 1.00 40.25 ? 68  THR C CG2 1 
ATOM   6834  N  N   . SER C  1 70  ? -13.131 -19.227 -45.301 1.00 34.70 ? 69  SER C N   1 
ATOM   6835  C  CA  . SER C  1 70  ? -12.199 -18.424 -44.550 1.00 31.43 ? 69  SER C CA  1 
ATOM   6836  C  C   . SER C  1 70  ? -10.986 -19.221 -44.083 1.00 30.65 ? 69  SER C C   1 
ATOM   6837  O  O   . SER C  1 70  ? -10.041 -18.622 -43.596 1.00 29.01 ? 69  SER C O   1 
ATOM   6838  C  CB  . SER C  1 70  ? -12.894 -17.809 -43.332 1.00 32.02 ? 69  SER C CB  1 
ATOM   6839  O  OG  . SER C  1 70  ? -13.381 -18.808 -42.457 1.00 30.85 ? 69  SER C OG  1 
ATOM   6840  N  N   . ARG C  1 71  ? -11.033 -20.553 -44.183 1.00 28.86 ? 70  ARG C N   1 
ATOM   6841  C  CA  . ARG C  1 71  ? -10.010 -21.429 -43.594 1.00 29.28 ? 70  ARG C CA  1 
ATOM   6842  C  C   . ARG C  1 71  ? -9.789  -21.093 -42.115 1.00 28.05 ? 70  ARG C C   1 
ATOM   6843  O  O   . ARG C  1 71  ? -8.668  -20.912 -41.665 1.00 27.53 ? 70  ARG C O   1 
ATOM   6844  C  CB  . ARG C  1 71  ? -8.683  -21.351 -44.374 1.00 30.57 ? 70  ARG C CB  1 
ATOM   6845  C  CG  . ARG C  1 71  ? -8.802  -21.735 -45.852 1.00 31.45 ? 70  ARG C CG  1 
ATOM   6846  C  CD  . ARG C  1 71  ? -9.094  -23.207 -46.022 1.00 31.93 ? 70  ARG C CD  1 
ATOM   6847  N  NE  . ARG C  1 71  ? -7.960  -24.006 -45.573 1.00 30.61 ? 70  ARG C NE  1 
ATOM   6848  C  CZ  . ARG C  1 71  ? -7.085  -24.607 -46.374 1.00 30.25 ? 70  ARG C CZ  1 
ATOM   6849  N  NH1 . ARG C  1 71  ? -7.179  -24.516 -47.695 1.00 29.26 ? 70  ARG C NH1 1 
ATOM   6850  N  NH2 . ARG C  1 71  ? -6.122  -25.342 -45.845 1.00 30.18 ? 70  ARG C NH2 1 
ATOM   6851  N  N   . ALA C  1 72  ? -10.881 -21.005 -41.367 1.00 27.08 ? 71  ALA C N   1 
ATOM   6852  C  CA  . ALA C  1 72  ? -10.842 -20.622 -39.955 1.00 25.98 ? 71  ALA C CA  1 
ATOM   6853  C  C   . ALA C  1 72  ? -11.997 -21.304 -39.224 1.00 26.22 ? 71  ALA C C   1 
ATOM   6854  O  O   . ALA C  1 72  ? -12.974 -21.710 -39.846 1.00 26.68 ? 71  ALA C O   1 
ATOM   6855  C  CB  . ALA C  1 72  ? -10.974 -19.127 -39.822 1.00 26.53 ? 71  ALA C CB  1 
ATOM   6856  N  N   . THR C  1 73  ? -11.889 -21.433 -37.909 1.00 25.38 ? 72  THR C N   1 
ATOM   6857  C  CA  . THR C  1 73  ? -12.958 -22.037 -37.126 1.00 25.17 ? 72  THR C CA  1 
ATOM   6858  C  C   . THR C  1 73  ? -13.845 -20.953 -36.565 1.00 26.26 ? 72  THR C C   1 
ATOM   6859  O  O   . THR C  1 73  ? -13.404 -19.825 -36.375 1.00 26.78 ? 72  THR C O   1 
ATOM   6860  C  CB  . THR C  1 73  ? -12.442 -22.930 -35.973 1.00 24.62 ? 72  THR C CB  1 
ATOM   6861  O  OG1 . THR C  1 73  ? -11.487 -22.220 -35.155 1.00 22.93 ? 72  THR C OG1 1 
ATOM   6862  C  CG2 . THR C  1 73  ? -11.794 -24.169 -36.526 1.00 24.66 ? 72  THR C CG2 1 
ATOM   6863  N  N   . GLN C  1 74  ? -15.083 -21.327 -36.278 1.00 25.96 ? 73  GLN C N   1 
ATOM   6864  C  CA  . GLN C  1 74  ? -15.999 -20.455 -35.576 1.00 27.26 ? 73  GLN C CA  1 
ATOM   6865  C  C   . GLN C  1 74  ? -16.804 -21.288 -34.571 1.00 25.67 ? 73  GLN C C   1 
ATOM   6866  O  O   . GLN C  1 74  ? -16.814 -22.510 -34.646 1.00 25.79 ? 73  GLN C O   1 
ATOM   6867  C  CB  . GLN C  1 74  ? -16.882 -19.709 -36.594 1.00 30.91 ? 73  GLN C CB  1 
ATOM   6868  C  CG  . GLN C  1 74  ? -17.356 -20.567 -37.737 1.00 33.34 ? 73  GLN C CG  1 
ATOM   6869  C  CD  . GLN C  1 74  ? -18.005 -19.779 -38.879 1.00 36.38 ? 73  GLN C CD  1 
ATOM   6870  O  OE1 . GLN C  1 74  ? -17.332 -19.151 -39.702 1.00 37.19 ? 73  GLN C OE1 1 
ATOM   6871  N  NE2 . GLN C  1 74  ? -19.313 -19.857 -38.949 1.00 37.43 ? 73  GLN C NE2 1 
ATOM   6872  N  N   . PHE C  1 75  ? -17.469 -20.634 -33.624 1.00 24.14 ? 74  PHE C N   1 
ATOM   6873  C  CA  . PHE C  1 75  ? -18.308 -21.336 -32.660 1.00 24.21 ? 74  PHE C CA  1 
ATOM   6874  C  C   . PHE C  1 75  ? -19.667 -21.618 -33.319 1.00 25.36 ? 74  PHE C C   1 
ATOM   6875  O  O   . PHE C  1 75  ? -20.019 -20.955 -34.287 1.00 25.33 ? 74  PHE C O   1 
ATOM   6876  C  CB  . PHE C  1 75  ? -18.521 -20.516 -31.372 1.00 24.33 ? 74  PHE C CB  1 
ATOM   6877  C  CG  . PHE C  1 75  ? -17.249 -19.994 -30.729 1.00 24.31 ? 74  PHE C CG  1 
ATOM   6878  C  CD1 . PHE C  1 75  ? -16.068 -20.718 -30.759 1.00 24.29 ? 74  PHE C CD1 1 
ATOM   6879  C  CD2 . PHE C  1 75  ? -17.262 -18.774 -30.076 1.00 24.81 ? 74  PHE C CD2 1 
ATOM   6880  C  CE1 . PHE C  1 75  ? -14.920 -20.218 -30.156 1.00 24.74 ? 74  PHE C CE1 1 
ATOM   6881  C  CE2 . PHE C  1 75  ? -16.135 -18.271 -29.467 1.00 25.71 ? 74  PHE C CE2 1 
ATOM   6882  C  CZ  . PHE C  1 75  ? -14.957 -18.996 -29.500 1.00 25.46 ? 74  PHE C CZ  1 
ATOM   6883  N  N   . PRO C  1 76  ? -20.405 -22.619 -32.822 1.00 25.39 ? 75  PRO C N   1 
ATOM   6884  C  CA  . PRO C  1 76  ? -21.741 -22.840 -33.366 1.00 26.88 ? 75  PRO C CA  1 
ATOM   6885  C  C   . PRO C  1 76  ? -22.635 -21.616 -33.193 1.00 27.72 ? 75  PRO C C   1 
ATOM   6886  O  O   . PRO C  1 76  ? -22.369 -20.778 -32.332 1.00 26.93 ? 75  PRO C O   1 
ATOM   6887  C  CB  . PRO C  1 76  ? -22.264 -24.036 -32.555 1.00 27.10 ? 75  PRO C CB  1 
ATOM   6888  C  CG  . PRO C  1 76  ? -21.018 -24.756 -32.117 1.00 25.99 ? 75  PRO C CG  1 
ATOM   6889  C  CD  . PRO C  1 76  ? -20.027 -23.663 -31.849 1.00 25.13 ? 75  PRO C CD  1 
ATOM   6890  N  N   . ASP C  1 77  ? -23.661 -21.495 -34.034 1.00 29.05 ? 76  ASP C N   1 
ATOM   6891  C  CA  . ASP C  1 77  ? -24.562 -20.352 -33.957 1.00 30.93 ? 76  ASP C CA  1 
ATOM   6892  C  C   . ASP C  1 77  ? -25.112 -20.208 -32.549 1.00 29.60 ? 76  ASP C C   1 
ATOM   6893  O  O   . ASP C  1 77  ? -25.576 -21.192 -31.962 1.00 28.99 ? 76  ASP C O   1 
ATOM   6894  C  CB  . ASP C  1 77  ? -25.736 -20.518 -34.918 1.00 35.76 ? 76  ASP C CB  1 
ATOM   6895  C  CG  . ASP C  1 77  ? -25.317 -20.475 -36.381 1.00 39.57 ? 76  ASP C CG  1 
ATOM   6896  O  OD1 . ASP C  1 77  ? -24.204 -19.983 -36.678 1.00 45.34 ? 76  ASP C OD1 1 
ATOM   6897  O  OD2 . ASP C  1 77  ? -26.095 -20.950 -37.239 1.00 45.26 ? 76  ASP C OD2 1 
ATOM   6898  N  N   . GLY C  1 78  ? -25.049 -18.988 -32.021 1.00 28.07 ? 77  GLY C N   1 
ATOM   6899  C  CA  . GLY C  1 78  ? -25.567 -18.670 -30.703 1.00 28.41 ? 77  GLY C CA  1 
ATOM   6900  C  C   . GLY C  1 78  ? -24.753 -19.194 -29.524 1.00 27.79 ? 77  GLY C C   1 
ATOM   6901  O  O   . GLY C  1 78  ? -25.254 -19.224 -28.394 1.00 28.91 ? 77  GLY C O   1 
ATOM   6902  N  N   . VAL C  1 79  ? -23.507 -19.600 -29.752 1.00 25.95 ? 78  VAL C N   1 
ATOM   6903  C  CA  . VAL C  1 79  ? -22.655 -20.085 -28.669 1.00 25.40 ? 78  VAL C CA  1 
ATOM   6904  C  C   . VAL C  1 79  ? -21.452 -19.142 -28.543 1.00 25.30 ? 78  VAL C C   1 
ATOM   6905  O  O   . VAL C  1 79  ? -20.815 -18.826 -29.538 1.00 24.53 ? 78  VAL C O   1 
ATOM   6906  C  CB  . VAL C  1 79  ? -22.138 -21.518 -28.937 1.00 24.68 ? 78  VAL C CB  1 
ATOM   6907  C  CG1 . VAL C  1 79  ? -21.211 -21.978 -27.821 1.00 24.31 ? 78  VAL C CG1 1 
ATOM   6908  C  CG2 . VAL C  1 79  ? -23.292 -22.502 -29.094 1.00 25.78 ? 78  VAL C CG2 1 
ATOM   6909  N  N   . ASP C  1 80  ? -21.168 -18.691 -27.326 1.00 25.94 ? 79  ASP C N   1 
ATOM   6910  C  CA  . ASP C  1 80  ? -19.873 -18.070 -27.043 1.00 27.10 ? 79  ASP C CA  1 
ATOM   6911  C  C   . ASP C  1 80  ? -19.093 -18.885 -26.025 1.00 24.99 ? 79  ASP C C   1 
ATOM   6912  O  O   . ASP C  1 80  ? -19.671 -19.403 -25.062 1.00 24.46 ? 79  ASP C O   1 
ATOM   6913  C  CB  . ASP C  1 80  ? -20.003 -16.660 -26.500 1.00 29.88 ? 79  ASP C CB  1 
ATOM   6914  C  CG  . ASP C  1 80  ? -18.639 -15.962 -26.458 1.00 33.20 ? 79  ASP C CG  1 
ATOM   6915  O  OD1 . ASP C  1 80  ? -17.946 -15.949 -27.520 1.00 33.10 ? 79  ASP C OD1 1 
ATOM   6916  O  OD2 . ASP C  1 80  ? -18.216 -15.524 -25.367 1.00 35.94 ? 79  ASP C OD2 1 
ATOM   6917  N  N   . VAL C  1 81  ? -17.779 -19.002 -26.241 1.00 25.07 ? 80  VAL C N   1 
ATOM   6918  C  CA  . VAL C  1 81  ? -16.896 -19.732 -25.326 1.00 24.07 ? 80  VAL C CA  1 
ATOM   6919  C  C   . VAL C  1 81  ? -15.742 -18.824 -24.914 1.00 24.39 ? 80  VAL C C   1 
ATOM   6920  O  O   . VAL C  1 81  ? -15.112 -18.212 -25.765 1.00 24.90 ? 80  VAL C O   1 
ATOM   6921  C  CB  . VAL C  1 81  ? -16.334 -21.023 -25.953 1.00 24.25 ? 80  VAL C CB  1 
ATOM   6922  C  CG1 . VAL C  1 81  ? -15.392 -21.739 -24.989 1.00 23.54 ? 80  VAL C CG1 1 
ATOM   6923  C  CG2 . VAL C  1 81  ? -17.442 -21.976 -26.344 1.00 24.22 ? 80  VAL C CG2 1 
ATOM   6924  N  N   . ARG C  1 82  ? -15.524 -18.680 -23.610 1.00 22.67 ? 81  ARG C N   1 
ATOM   6925  C  CA  . ARG C  1 82  ? -14.470 -17.829 -23.104 1.00 22.77 ? 81  ARG C CA  1 
ATOM   6926  C  C   . ARG C  1 82  ? -13.562 -18.586 -22.133 1.00 20.85 ? 81  ARG C C   1 
ATOM   6927  O  O   . ARG C  1 82  ? -13.953 -19.608 -21.575 1.00 20.14 ? 81  ARG C O   1 
ATOM   6928  C  CB  . ARG C  1 82  ? -15.042 -16.564 -22.471 1.00 24.49 ? 81  ARG C CB  1 
ATOM   6929  C  CG  . ARG C  1 82  ? -15.646 -16.761 -21.103 1.00 28.03 ? 81  ARG C CG  1 
ATOM   6930  C  CD  . ARG C  1 82  ? -16.049 -15.438 -20.453 1.00 31.01 ? 81  ARG C CD  1 
ATOM   6931  N  NE  . ARG C  1 82  ? -16.665 -15.728 -19.157 1.00 34.18 ? 81  ARG C NE  1 
ATOM   6932  C  CZ  . ARG C  1 82  ? -17.430 -14.879 -18.454 1.00 37.78 ? 81  ARG C CZ  1 
ATOM   6933  N  NH1 . ARG C  1 82  ? -17.699 -13.654 -18.901 1.00 36.00 ? 81  ARG C NH1 1 
ATOM   6934  N  NH2 . ARG C  1 82  ? -17.928 -15.278 -17.288 1.00 39.07 ? 81  ARG C NH2 1 
ATOM   6935  N  N   . VAL C  1 83  ? -12.360 -18.059 -21.952 1.00 19.71 ? 82  VAL C N   1 
ATOM   6936  C  CA  . VAL C  1 83  ? -11.333 -18.681 -21.113 1.00 19.69 ? 82  VAL C CA  1 
ATOM   6937  C  C   . VAL C  1 83  ? -11.245 -17.863 -19.826 1.00 19.39 ? 82  VAL C C   1 
ATOM   6938  O  O   . VAL C  1 83  ? -10.821 -16.714 -19.877 1.00 20.26 ? 82  VAL C O   1 
ATOM   6939  C  CB  . VAL C  1 83  ? -9.958  -18.620 -21.809 1.00 19.32 ? 82  VAL C CB  1 
ATOM   6940  C  CG1 . VAL C  1 83  ? -8.880  -19.210 -20.922 1.00 19.38 ? 82  VAL C CG1 1 
ATOM   6941  C  CG2 . VAL C  1 83  ? -10.035 -19.353 -23.145 1.00 20.14 ? 82  VAL C CG2 1 
ATOM   6942  N  N   . PRO C  1 84  ? -11.668 -18.421 -18.688 1.00 19.46 ? 83  PRO C N   1 
ATOM   6943  C  CA  . PRO C  1 84  ? -11.589 -17.654 -17.432 1.00 19.69 ? 83  PRO C CA  1 
ATOM   6944  C  C   . PRO C  1 84  ? -10.184 -17.738 -16.834 1.00 19.51 ? 83  PRO C C   1 
ATOM   6945  O  O   . PRO C  1 84  ? -9.434  -18.621 -17.204 1.00 19.04 ? 83  PRO C O   1 
ATOM   6946  C  CB  . PRO C  1 84  ? -12.584 -18.365 -16.523 1.00 20.13 ? 83  PRO C CB  1 
ATOM   6947  C  CG  . PRO C  1 84  ? -12.549 -19.785 -17.002 1.00 20.15 ? 83  PRO C CG  1 
ATOM   6948  C  CD  . PRO C  1 84  ? -12.366 -19.710 -18.492 1.00 19.84 ? 83  PRO C CD  1 
ATOM   6949  N  N   . GLY C  1 85  ? -9.844  -16.805 -15.937 1.00 18.98 ? 84  GLY C N   1 
ATOM   6950  C  CA  . GLY C  1 85  ? -8.682  -16.971 -15.076 1.00 19.04 ? 84  GLY C CA  1 
ATOM   6951  C  C   . GLY C  1 85  ? -7.329  -16.622 -15.662 1.00 18.15 ? 84  GLY C C   1 
ATOM   6952  O  O   . GLY C  1 85  ? -6.304  -17.060 -15.119 1.00 17.86 ? 84  GLY C O   1 
ATOM   6953  N  N   . PHE C  1 86  ? -7.294  -15.860 -16.760 1.00 17.81 ? 85  PHE C N   1 
ATOM   6954  C  CA  . PHE C  1 86  ? -6.013  -15.419 -17.312 1.00 17.79 ? 85  PHE C CA  1 
ATOM   6955  C  C   . PHE C  1 86  ? -5.297  -14.516 -16.294 1.00 18.09 ? 85  PHE C C   1 
ATOM   6956  O  O   . PHE C  1 86  ? -5.883  -13.575 -15.780 1.00 17.39 ? 85  PHE C O   1 
ATOM   6957  C  CB  . PHE C  1 86  ? -6.161  -14.699 -18.673 1.00 18.15 ? 85  PHE C CB  1 
ATOM   6958  C  CG  . PHE C  1 86  ? -4.830  -14.455 -19.366 1.00 17.76 ? 85  PHE C CG  1 
ATOM   6959  C  CD1 . PHE C  1 86  ? -4.282  -15.408 -20.217 1.00 17.85 ? 85  PHE C CD1 1 
ATOM   6960  C  CD2 . PHE C  1 86  ? -4.110  -13.306 -19.114 1.00 17.80 ? 85  PHE C CD2 1 
ATOM   6961  C  CE1 . PHE C  1 86  ? -3.041  -15.206 -20.822 1.00 17.60 ? 85  PHE C CE1 1 
ATOM   6962  C  CE2 . PHE C  1 86  ? -2.870  -13.097 -19.708 1.00 17.71 ? 85  PHE C CE2 1 
ATOM   6963  C  CZ  . PHE C  1 86  ? -2.331  -14.050 -20.547 1.00 17.72 ? 85  PHE C CZ  1 
ATOM   6964  N  N   . GLY C  1 87  ? -4.054  -14.837 -15.986 1.00 17.32 ? 86  GLY C N   1 
ATOM   6965  C  CA  . GLY C  1 87  ? -3.306  -14.090 -15.001 1.00 18.49 ? 86  GLY C CA  1 
ATOM   6966  C  C   . GLY C  1 87  ? -3.503  -14.611 -13.592 1.00 19.53 ? 86  GLY C C   1 
ATOM   6967  O  O   . GLY C  1 87  ? -2.783  -14.168 -12.702 1.00 20.94 ? 86  GLY C O   1 
ATOM   6968  N  N   . LYS C  1 88  ? -4.414  -15.585 -13.406 1.00 18.91 ? 87  LYS C N   1 
ATOM   6969  C  CA  . LYS C  1 88  ? -4.661  -16.256 -12.131 1.00 20.51 ? 87  LYS C CA  1 
ATOM   6970  C  C   . LYS C  1 88  ? -4.267  -17.725 -12.298 1.00 19.10 ? 87  LYS C C   1 
ATOM   6971  O  O   . LYS C  1 88  ? -3.721  -18.097 -13.337 1.00 18.43 ? 87  LYS C O   1 
ATOM   6972  C  CB  . LYS C  1 88  ? -6.152  -16.180 -11.773 1.00 22.67 ? 87  LYS C CB  1 
ATOM   6973  C  CG  . LYS C  1 88  ? -6.753  -14.791 -11.852 1.00 25.88 ? 87  LYS C CG  1 
ATOM   6974  C  CD  . LYS C  1 88  ? -6.086  -13.840 -10.897 1.00 29.45 ? 87  LYS C CD  1 
ATOM   6975  C  CE  . LYS C  1 88  ? -6.771  -12.470 -10.915 1.00 33.67 ? 87  LYS C CE  1 
ATOM   6976  N  NZ  . LYS C  1 88  ? -5.868  -11.424 -10.342 1.00 34.61 ? 87  LYS C NZ  1 
ATOM   6977  N  N   . THR C  1 89  ? -4.508  -18.555 -11.292 1.00 18.88 ? 88  THR C N   1 
ATOM   6978  C  CA  . THR C  1 89  ? -4.118  -19.980 -11.398 1.00 19.19 ? 88  THR C CA  1 
ATOM   6979  C  C   . THR C  1 89  ? -5.263  -20.942 -11.192 1.00 18.52 ? 88  THR C C   1 
ATOM   6980  O  O   . THR C  1 89  ? -5.148  -22.121 -11.533 1.00 18.68 ? 88  THR C O   1 
ATOM   6981  C  CB  . THR C  1 89  ? -2.986  -20.344 -10.417 1.00 20.29 ? 88  THR C CB  1 
ATOM   6982  O  OG1 . THR C  1 89  ? -3.446  -20.179 -9.087  1.00 21.71 ? 88  THR C OG1 1 
ATOM   6983  C  CG2 . THR C  1 89  ? -1.742  -19.456 -10.628 1.00 20.91 ? 88  THR C CG2 1 
ATOM   6984  N  N   . PHE C  1 90  ? -6.387  -20.461 -10.670 1.00 18.88 ? 89  PHE C N   1 
ATOM   6985  C  CA  . PHE C  1 90  ? -7.474  -21.352 -10.297 1.00 19.57 ? 89  PHE C CA  1 
ATOM   6986  C  C   . PHE C  1 90  ? -7.950  -22.247 -11.463 1.00 19.17 ? 89  PHE C C   1 
ATOM   6987  O  O   . PHE C  1 90  ? -8.306  -23.420 -11.243 1.00 19.22 ? 89  PHE C O   1 
ATOM   6988  C  CB  . PHE C  1 90  ? -8.652  -20.572 -9.679  1.00 21.48 ? 89  PHE C CB  1 
ATOM   6989  C  CG  . PHE C  1 90  ? -9.426  -19.727 -10.658 1.00 22.54 ? 89  PHE C CG  1 
ATOM   6990  C  CD1 . PHE C  1 90  ? -10.478 -20.269 -11.395 1.00 24.17 ? 89  PHE C CD1 1 
ATOM   6991  C  CD2 . PHE C  1 90  ? -9.161  -18.364 -10.785 1.00 23.85 ? 89  PHE C CD2 1 
ATOM   6992  C  CE1 . PHE C  1 90  ? -11.207 -19.482 -12.278 1.00 24.26 ? 89  PHE C CE1 1 
ATOM   6993  C  CE2 . PHE C  1 90  ? -9.903  -17.569 -11.641 1.00 23.98 ? 89  PHE C CE2 1 
ATOM   6994  C  CZ  . PHE C  1 90  ? -10.922 -18.134 -12.406 1.00 24.63 ? 89  PHE C CZ  1 
ATOM   6995  N  N   . SER C  1 91  ? -7.969  -21.695 -12.678 1.00 18.27 ? 90  SER C N   1 
ATOM   6996  C  CA  . SER C  1 91  ? -8.583  -22.399 -13.801 1.00 18.91 ? 90  SER C CA  1 
ATOM   6997  C  C   . SER C  1 91  ? -7.692  -23.492 -14.395 1.00 18.83 ? 90  SER C C   1 
ATOM   6998  O  O   . SER C  1 91  ? -8.171  -24.306 -15.184 1.00 18.08 ? 90  SER C O   1 
ATOM   6999  C  CB  . SER C  1 91  ? -9.051  -21.429 -14.883 1.00 18.71 ? 90  SER C CB  1 
ATOM   7000  O  OG  . SER C  1 91  ? -7.991  -20.899 -15.639 1.00 18.93 ? 90  SER C OG  1 
ATOM   7001  N  N   . LEU C  1 92  ? -6.398  -23.449 -14.076 1.00 18.04 ? 91  LEU C N   1 
ATOM   7002  C  CA  A LEU C  1 92  ? -5.522  -24.573 -14.408 0.50 17.82 ? 91  LEU C CA  1 
ATOM   7003  C  CA  B LEU C  1 92  ? -5.432  -24.514 -14.352 0.50 18.13 ? 91  LEU C CA  1 
ATOM   7004  C  C   . LEU C  1 92  ? -5.205  -25.485 -13.210 1.00 18.40 ? 91  LEU C C   1 
ATOM   7005  O  O   . LEU C  1 92  ? -4.760  -26.616 -13.414 1.00 18.59 ? 91  LEU C O   1 
ATOM   7006  C  CB  A LEU C  1 92  ? -4.295  -24.172 -15.245 0.50 17.62 ? 91  LEU C CB  1 
ATOM   7007  C  CB  B LEU C  1 92  ? -4.058  -23.878 -14.564 0.50 18.43 ? 91  LEU C CB  1 
ATOM   7008  C  CG  A LEU C  1 92  ? -3.520  -22.891 -15.012 0.50 17.52 ? 91  LEU C CG  1 
ATOM   7009  C  CG  B LEU C  1 92  ? -3.664  -23.194 -15.847 0.50 18.62 ? 91  LEU C CG  1 
ATOM   7010  C  CD1 A LEU C  1 92  ? -2.774  -23.091 -13.709 0.50 17.75 ? 91  LEU C CD1 1 
ATOM   7011  C  CD1 B LEU C  1 92  ? -4.473  -21.948 -16.100 0.50 18.95 ? 91  LEU C CD1 1 
ATOM   7012  C  CD2 A LEU C  1 92  ? -2.525  -22.674 -16.150 0.50 17.64 ? 91  LEU C CD2 1 
ATOM   7013  C  CD2 B LEU C  1 92  ? -2.197  -22.825 -15.689 0.50 18.73 ? 91  LEU C CD2 1 
ATOM   7014  N  N   . GLU C  1 93  ? -5.446  -25.033 -11.981 1.00 18.12 ? 92  GLU C N   1 
ATOM   7015  C  CA  . GLU C  1 93  ? -5.219  -25.909 -10.834 1.00 18.69 ? 92  GLU C CA  1 
ATOM   7016  C  C   . GLU C  1 93  ? -6.261  -27.013 -10.773 1.00 19.30 ? 92  GLU C C   1 
ATOM   7017  O  O   . GLU C  1 93  ? -5.953  -28.173 -10.537 1.00 18.91 ? 92  GLU C O   1 
ATOM   7018  C  CB  . GLU C  1 93  ? -5.234  -25.136 -9.504  1.00 18.95 ? 92  GLU C CB  1 
ATOM   7019  C  CG  . GLU C  1 93  ? -4.017  -24.256 -9.251  1.00 19.07 ? 92  GLU C CG  1 
ATOM   7020  C  CD  . GLU C  1 93  ? -4.118  -23.591 -7.865  1.00 19.81 ? 92  GLU C CD  1 
ATOM   7021  O  OE1 . GLU C  1 93  ? -4.265  -22.337 -7.800  1.00 20.59 ? 92  GLU C OE1 1 
ATOM   7022  O  OE2 . GLU C  1 93  ? -4.086  -24.302 -6.816  1.00 21.04 ? 92  GLU C OE2 1 
ATOM   7023  N  N   . PHE C  1 94  ? -7.502  -26.616 -10.985 1.00 19.87 ? 93  PHE C N   1 
ATOM   7024  C  CA  . PHE C  1 94  ? -8.651  -27.515 -10.942 1.00 21.88 ? 93  PHE C CA  1 
ATOM   7025  C  C   . PHE C  1 94  ? -9.457  -27.299 -12.213 1.00 21.65 ? 93  PHE C C   1 
ATOM   7026  O  O   . PHE C  1 94  ? -9.901  -26.173 -12.512 1.00 23.03 ? 93  PHE C O   1 
ATOM   7027  C  CB  . PHE C  1 94  ? -9.527  -27.174 -9.765  1.00 24.21 ? 93  PHE C CB  1 
ATOM   7028  C  CG  . PHE C  1 94  ? -8.922  -27.527 -8.436  1.00 26.22 ? 93  PHE C CG  1 
ATOM   7029  C  CD1 . PHE C  1 94  ? -8.786  -28.832 -8.039  1.00 27.98 ? 93  PHE C CD1 1 
ATOM   7030  C  CD2 . PHE C  1 94  ? -8.480  -26.537 -7.602  1.00 29.61 ? 93  PHE C CD2 1 
ATOM   7031  C  CE1 . PHE C  1 94  ? -8.228  -29.142 -6.794  1.00 30.62 ? 93  PHE C CE1 1 
ATOM   7032  C  CE2 . PHE C  1 94  ? -7.926  -26.832 -6.363  1.00 30.99 ? 93  PHE C CE2 1 
ATOM   7033  C  CZ  . PHE C  1 94  ? -7.796  -28.133 -5.965  1.00 29.74 ? 93  PHE C CZ  1 
ATOM   7034  N  N   . LEU C  1 95  ? -9.617  -28.352 -12.986 1.00 20.83 ? 94  LEU C N   1 
ATOM   7035  C  CA  . LEU C  1 95  ? -10.393 -28.253 -14.234 1.00 21.08 ? 94  LEU C CA  1 
ATOM   7036  C  C   . LEU C  1 95  ? -11.888 -28.217 -13.929 1.00 22.33 ? 94  LEU C C   1 
ATOM   7037  O  O   . LEU C  1 95  ? -12.660 -27.593 -14.660 1.00 21.48 ? 94  LEU C O   1 
ATOM   7038  C  CB  . LEU C  1 95  ? -10.064 -29.416 -15.149 1.00 20.84 ? 94  LEU C CB  1 
ATOM   7039  C  CG  . LEU C  1 95  ? -8.580  -29.529 -15.502 1.00 20.94 ? 94  LEU C CG  1 
ATOM   7040  C  CD1 . LEU C  1 95  ? -8.341  -30.744 -16.370 1.00 21.91 ? 94  LEU C CD1 1 
ATOM   7041  C  CD2 . LEU C  1 95  ? -8.046  -28.263 -16.179 1.00 21.28 ? 94  LEU C CD2 1 
ATOM   7042  N  N   . ASP C  1 96  ? -12.269 -28.886 -12.848 1.00 24.60 ? 95  ASP C N   1 
ATOM   7043  C  CA  . ASP C  1 96  ? -13.654 -28.905 -12.371 1.00 28.48 ? 95  ASP C CA  1 
ATOM   7044  C  C   . ASP C  1 96  ? -13.763 -27.960 -11.180 1.00 29.97 ? 95  ASP C C   1 
ATOM   7045  O  O   . ASP C  1 96  ? -13.099 -28.180 -10.166 1.00 29.48 ? 95  ASP C O   1 
ATOM   7046  C  CB  . ASP C  1 96  ? -14.036 -30.330 -11.960 1.00 31.80 ? 95  ASP C CB  1 
ATOM   7047  C  CG  . ASP C  1 96  ? -15.515 -30.478 -11.686 1.00 37.26 ? 95  ASP C CG  1 
ATOM   7048  O  OD1 . ASP C  1 96  ? -16.159 -29.486 -11.275 1.00 39.66 ? 95  ASP C OD1 1 
ATOM   7049  O  OD2 . ASP C  1 96  ? -16.035 -31.592 -11.879 1.00 43.50 ? 95  ASP C OD2 1 
ATOM   7050  N  N   . PRO C  1 97  ? -14.573 -26.894 -11.303 1.00 31.39 ? 96  PRO C N   1 
ATOM   7051  C  CA  . PRO C  1 97  ? -14.659 -25.925 -10.210 1.00 34.00 ? 96  PRO C CA  1 
ATOM   7052  C  C   . PRO C  1 97  ? -15.229 -26.499 -8.894  1.00 35.20 ? 96  PRO C C   1 
ATOM   7053  O  O   . PRO C  1 97  ? -15.101 -25.849 -7.881  1.00 36.19 ? 96  PRO C O   1 
ATOM   7054  C  CB  . PRO C  1 97  ? -15.572 -24.808 -10.765 1.00 35.38 ? 96  PRO C CB  1 
ATOM   7055  C  CG  . PRO C  1 97  ? -15.899 -25.157 -12.176 1.00 34.54 ? 96  PRO C CG  1 
ATOM   7056  C  CD  . PRO C  1 97  ? -15.442 -26.554 -12.448 1.00 33.36 ? 96  PRO C CD  1 
ATOM   7057  N  N   . SER C  1 98  ? -15.815 -27.698 -8.910  1.00 35.73 ? 97  SER C N   1 
ATOM   7058  C  CA  . SER C  1 98  ? -16.118 -28.416 -7.670  1.00 39.17 ? 97  SER C CA  1 
ATOM   7059  C  C   . SER C  1 98  ? -14.845 -28.806 -6.898  1.00 43.00 ? 97  SER C C   1 
ATOM   7060  O  O   . SER C  1 98  ? -14.922 -29.179 -5.726  1.00 42.61 ? 97  SER C O   1 
ATOM   7061  C  CB  . SER C  1 98  ? -16.885 -29.691 -7.959  1.00 39.84 ? 97  SER C CB  1 
ATOM   7062  O  OG  . SER C  1 98  ? -16.006 -30.686 -8.478  1.00 41.02 ? 97  SER C OG  1 
ATOM   7063  N  N   . LYS C  1 99  ? -13.694 -28.752 -7.575  1.00 40.90 ? 98  LYS C N   1 
ATOM   7064  C  CA  . LYS C  1 99  ? -12.385 -29.074 -7.011  1.00 42.32 ? 98  LYS C CA  1 
ATOM   7065  C  C   . LYS C  1 99  ? -12.243 -30.547 -6.707  1.00 41.97 ? 98  LYS C C   1 
ATOM   7066  O  O   . LYS C  1 99  ? -11.431 -30.956 -5.888  1.00 42.00 ? 98  LYS C O   1 
ATOM   7067  C  CB  . LYS C  1 99  ? -12.059 -28.212 -5.797  1.00 45.15 ? 98  LYS C CB  1 
ATOM   7068  C  CG  . LYS C  1 99  ? -12.085 -26.732 -6.120  1.00 47.72 ? 98  LYS C CG  1 
ATOM   7069  C  CD  . LYS C  1 99  ? -11.623 -25.910 -4.941  1.00 51.40 ? 98  LYS C CD  1 
ATOM   7070  C  CE  . LYS C  1 99  ? -11.519 -24.450 -5.324  1.00 54.49 ? 98  LYS C CE  1 
ATOM   7071  N  NZ  . LYS C  1 99  ? -10.994 -23.647 -4.180  1.00 60.17 ? 98  LYS C NZ  1 
ATOM   7072  N  N   . SER C  1 100 ? -12.991 -31.342 -7.450  1.00 42.49 ? 99  SER C N   1 
ATOM   7073  C  CA  . SER C  1 100 ? -12.857 -32.778 -7.422  1.00 45.22 ? 99  SER C CA  1 
ATOM   7074  C  C   . SER C  1 100 ? -11.450 -33.220 -7.849  1.00 45.15 ? 99  SER C C   1 
ATOM   7075  O  O   . SER C  1 100 ? -10.836 -32.618 -8.752  1.00 41.02 ? 99  SER C O   1 
ATOM   7076  C  CB  . SER C  1 100 ? -13.889 -33.387 -8.373  1.00 46.60 ? 99  SER C CB  1 
ATOM   7077  O  OG  . SER C  1 100 ? -13.640 -34.765 -8.530  1.00 50.40 ? 99  SER C OG  1 
ATOM   7078  N  N   . SER C  1 101 ? -10.969 -34.307 -7.245  1.00 45.20 ? 100 SER C N   1 
ATOM   7079  C  CA  . SER C  1 101 ? -9.633  -34.840 -7.554  1.00 43.62 ? 100 SER C CA  1 
ATOM   7080  C  C   . SER C  1 101 ? -9.488  -35.252 -9.014  1.00 41.03 ? 100 SER C C   1 
ATOM   7081  O  O   . SER C  1 101 ? -8.392  -35.190 -9.578  1.00 36.24 ? 100 SER C O   1 
ATOM   7082  C  CB  . SER C  1 101 ? -9.298  -36.025 -6.657  1.00 46.40 ? 100 SER C CB  1 
ATOM   7083  O  OG  . SER C  1 101 ? -10.190 -37.093 -6.897  1.00 48.44 ? 100 SER C OG  1 
ATOM   7084  N  N   . VAL C  1 102 ? -10.597 -35.636 -9.643  1.00 39.33 ? 101 VAL C N   1 
ATOM   7085  C  CA  . VAL C  1 102 ? -10.592 -35.981 -11.058 1.00 37.87 ? 101 VAL C CA  1 
ATOM   7086  C  C   . VAL C  1 102 ? -10.043 -34.832 -11.923 1.00 33.02 ? 101 VAL C C   1 
ATOM   7087  O  O   . VAL C  1 102 ? -9.424  -35.068 -12.954 1.00 34.42 ? 101 VAL C O   1 
ATOM   7088  C  CB  . VAL C  1 102 ? -12.024 -36.331 -11.523 1.00 40.82 ? 101 VAL C CB  1 
ATOM   7089  C  CG1 . VAL C  1 102 ? -12.040 -36.711 -12.985 1.00 42.42 ? 101 VAL C CG1 1 
ATOM   7090  C  CG2 . VAL C  1 102 ? -12.645 -37.451 -10.686 1.00 44.28 ? 101 VAL C CG2 1 
ATOM   7091  N  N   . GLY C  1 103 ? -10.293 -33.590 -11.538 1.00 29.49 ? 102 GLY C N   1 
ATOM   7092  C  CA  . GLY C  1 103 ? -9.826  -32.446 -12.327 1.00 26.40 ? 102 GLY C CA  1 
ATOM   7093  C  C   . GLY C  1 103 ? -8.575  -31.780 -11.765 1.00 23.60 ? 102 GLY C C   1 
ATOM   7094  O  O   . GLY C  1 103 ? -8.219  -30.704 -12.219 1.00 21.58 ? 102 GLY C O   1 
ATOM   7095  N  N   . SER C  1 104 ? -7.900  -32.401 -10.799 1.00 22.22 ? 103 SER C N   1 
ATOM   7096  C  CA  . SER C  1 104 ? -6.710  -31.779 -10.189 1.00 22.69 ? 103 SER C CA  1 
ATOM   7097  C  C   . SER C  1 104 ? -5.558  -31.864 -11.178 1.00 22.34 ? 103 SER C C   1 
ATOM   7098  O  O   . SER C  1 104 ? -5.135  -32.958 -11.537 1.00 23.99 ? 103 SER C O   1 
ATOM   7099  C  CB  . SER C  1 104 ? -6.339  -32.448 -8.861  1.00 23.39 ? 103 SER C CB  1 
ATOM   7100  O  OG  . SER C  1 104 ? -5.176  -31.849 -8.303  1.00 23.62 ? 103 SER C OG  1 
ATOM   7101  N  N   . TYR C  1 105 ? -5.074  -30.725 -11.657 1.00 20.20 ? 104 TYR C N   1 
ATOM   7102  C  CA  . TYR C  1 105 ? -4.144  -30.700 -12.774 1.00 19.36 ? 104 TYR C CA  1 
ATOM   7103  C  C   . TYR C  1 105 ? -2.843  -29.986 -12.358 1.00 18.89 ? 104 TYR C C   1 
ATOM   7104  O  O   . TYR C  1 105 ? -1.882  -30.646 -11.979 1.00 18.63 ? 104 TYR C O   1 
ATOM   7105  C  CB  . TYR C  1 105 ? -4.817  -30.068 -13.993 1.00 18.63 ? 104 TYR C CB  1 
ATOM   7106  C  CG  . TYR C  1 105 ? -3.966  -29.963 -15.227 1.00 18.06 ? 104 TYR C CG  1 
ATOM   7107  C  CD1 . TYR C  1 105 ? -3.211  -31.048 -15.678 1.00 18.88 ? 104 TYR C CD1 1 
ATOM   7108  C  CD2 . TYR C  1 105 ? -3.930  -28.788 -15.974 1.00 17.86 ? 104 TYR C CD2 1 
ATOM   7109  C  CE1 . TYR C  1 105 ? -2.434  -30.952 -16.832 1.00 18.77 ? 104 TYR C CE1 1 
ATOM   7110  C  CE2 . TYR C  1 105 ? -3.154  -28.674 -17.123 1.00 17.76 ? 104 TYR C CE2 1 
ATOM   7111  C  CZ  . TYR C  1 105 ? -2.403  -29.752 -17.555 1.00 18.22 ? 104 TYR C CZ  1 
ATOM   7112  O  OH  . TYR C  1 105 ? -1.620  -29.635 -18.685 1.00 17.80 ? 104 TYR C OH  1 
ATOM   7113  N  N   . PHE C  1 106 ? -2.833  -28.667 -12.321 1.00 17.72 ? 105 PHE C N   1 
ATOM   7114  C  CA  . PHE C  1 106 ? -1.674  -27.940 -11.793 1.00 17.97 ? 105 PHE C CA  1 
ATOM   7115  C  C   . PHE C  1 106 ? -1.721  -27.717 -10.278 1.00 17.75 ? 105 PHE C C   1 
ATOM   7116  O  O   . PHE C  1 106 ? -0.808  -27.091 -9.712  1.00 18.09 ? 105 PHE C O   1 
ATOM   7117  C  CB  . PHE C  1 106 ? -1.512  -26.566 -12.476 1.00 18.82 ? 105 PHE C CB  1 
ATOM   7118  C  CG  . PHE C  1 106 ? -0.636  -26.580 -13.697 1.00 20.11 ? 105 PHE C CG  1 
ATOM   7119  C  CD1 . PHE C  1 106 ? -1.171  -26.802 -14.919 1.00 22.50 ? 105 PHE C CD1 1 
ATOM   7120  C  CD2 . PHE C  1 106 ? 0.736   -26.340 -13.610 1.00 21.98 ? 105 PHE C CD2 1 
ATOM   7121  C  CE1 . PHE C  1 106 ? -0.375  -26.790 -16.073 1.00 23.53 ? 105 PHE C CE1 1 
ATOM   7122  C  CE2 . PHE C  1 106 ? 1.539   -26.330 -14.741 1.00 23.07 ? 105 PHE C CE2 1 
ATOM   7123  C  CZ  . PHE C  1 106 ? 0.970   -26.560 -15.989 1.00 22.57 ? 105 PHE C CZ  1 
ATOM   7124  N  N   . HIS C  1 107 ? -2.768  -28.190 -9.599  1.00 17.87 ? 106 HIS C N   1 
ATOM   7125  C  CA  . HIS C  1 107 ? -2.915  -27.889 -8.177  1.00 18.39 ? 106 HIS C CA  1 
ATOM   7126  C  C   . HIS C  1 107 ? -1.716  -28.299 -7.324  1.00 18.31 ? 106 HIS C C   1 
ATOM   7127  O  O   . HIS C  1 107 ? -1.297  -27.524 -6.467  1.00 17.21 ? 106 HIS C O   1 
ATOM   7128  C  CB  . HIS C  1 107 ? -4.172  -28.510 -7.580  1.00 19.48 ? 106 HIS C CB  1 
ATOM   7129  C  CG  . HIS C  1 107 ? -4.405  -28.118 -6.152  1.00 21.12 ? 106 HIS C CG  1 
ATOM   7130  N  ND1 . HIS C  1 107 ? -4.481  -26.802 -5.751  1.00 21.22 ? 106 HIS C ND1 1 
ATOM   7131  C  CD2 . HIS C  1 107 ? -4.582  -28.866 -5.037  1.00 22.53 ? 106 HIS C CD2 1 
ATOM   7132  C  CE1 . HIS C  1 107 ? -4.684  -26.754 -4.448  1.00 22.62 ? 106 HIS C CE1 1 
ATOM   7133  N  NE2 . HIS C  1 107 ? -4.748  -27.997 -3.990  1.00 23.48 ? 106 HIS C NE2 1 
ATOM   7134  N  N   . THR C  1 108 ? -1.206  -29.513 -7.507  1.00 17.94 ? 107 THR C N   1 
ATOM   7135  C  CA  . THR C  1 108 ? -0.122  -29.972 -6.659  1.00 18.82 ? 107 THR C CA  1 
ATOM   7136  C  C   . THR C  1 108 ? 1.078   -29.058 -6.861  1.00 18.82 ? 107 THR C C   1 
ATOM   7137  O  O   . THR C  1 108 ? 1.727   -28.695 -5.894  1.00 19.10 ? 107 THR C O   1 
ATOM   7138  C  CB  . THR C  1 108 ? 0.235   -31.460 -6.931  1.00 19.77 ? 107 THR C CB  1 
ATOM   7139  O  OG1 . THR C  1 108 ? -0.914  -32.268 -6.658  1.00 19.45 ? 107 THR C OG1 1 
ATOM   7140  C  CG2 . THR C  1 108 ? 1.367   -31.926 -6.054  1.00 20.59 ? 107 THR C CG2 1 
ATOM   7141  N  N   . MET C  1 109 ? 1.372   -28.694 -8.108  1.00 18.71 ? 108 MET C N   1 
ATOM   7142  C  CA  . MET C  1 109 ? 2.516   -27.837 -8.396  1.00 18.44 ? 108 MET C CA  1 
ATOM   7143  C  C   . MET C  1 109 ? 2.346   -26.420 -7.823  1.00 18.28 ? 108 MET C C   1 
ATOM   7144  O  O   . MET C  1 109 ? 3.261   -25.899 -7.216  1.00 17.88 ? 108 MET C O   1 
ATOM   7145  C  CB  . MET C  1 109 ? 2.774   -27.741 -9.884  1.00 18.79 ? 108 MET C CB  1 
ATOM   7146  C  CG  . MET C  1 109 ? 3.914   -26.799 -10.234 1.00 19.61 ? 108 MET C CG  1 
ATOM   7147  S  SD  . MET C  1 109 ? 4.266   -26.751 -12.015 1.00 23.16 ? 108 MET C SD  1 
ATOM   7148  C  CE  . MET C  1 109 ? 4.864   -28.406 -12.201 1.00 21.90 ? 108 MET C CE  1 
ATOM   7149  N  N   . VAL C  1 110 ? 1.158   -25.835 -7.968  1.00 17.44 ? 109 VAL C N   1 
ATOM   7150  C  CA  . VAL C  1 110 ? 0.898   -24.509 -7.402  1.00 17.88 ? 109 VAL C CA  1 
ATOM   7151  C  C   . VAL C  1 110 ? 0.925   -24.525 -5.880  1.00 18.73 ? 109 VAL C C   1 
ATOM   7152  O  O   . VAL C  1 110 ? 1.490   -23.609 -5.270  1.00 17.94 ? 109 VAL C O   1 
ATOM   7153  C  CB  . VAL C  1 110 ? -0.408  -23.896 -7.916  1.00 17.70 ? 109 VAL C CB  1 
ATOM   7154  C  CG1 . VAL C  1 110 ? -0.676  -22.517 -7.264  1.00 18.42 ? 109 VAL C CG1 1 
ATOM   7155  C  CG2 . VAL C  1 110 ? -0.291  -23.723 -9.410  1.00 17.32 ? 109 VAL C CG2 1 
ATOM   7156  N  N   . GLU C  1 111 ? 0.375   -25.564 -5.256  1.00 20.26 ? 110 GLU C N   1 
ATOM   7157  C  CA  . GLU C  1 111 ? 0.504   -25.707 -3.800  1.00 23.77 ? 110 GLU C CA  1 
ATOM   7158  C  C   . GLU C  1 111 ? 1.972   -25.683 -3.392  1.00 22.47 ? 110 GLU C C   1 
ATOM   7159  O  O   . GLU C  1 111 ? 2.319   -25.086 -2.379  1.00 21.04 ? 110 GLU C O   1 
ATOM   7160  C  CB  . GLU C  1 111 ? -0.108  -27.009 -3.285  1.00 28.16 ? 110 GLU C CB  1 
ATOM   7161  C  CG  . GLU C  1 111 ? -1.610  -26.893 -3.204  1.00 33.37 ? 110 GLU C CG  1 
ATOM   7162  C  CD  . GLU C  1 111 ? -2.044  -25.791 -2.172  1.00 37.66 ? 110 GLU C CD  1 
ATOM   7163  O  OE1 . GLU C  1 111 ? -2.875  -24.927 -2.503  1.00 38.85 ? 110 GLU C OE1 1 
ATOM   7164  O  OE2 . GLU C  1 111 ? -1.521  -25.690 -1.034  1.00 45.10 ? 110 GLU C OE2 1 
ATOM   7165  N  N   . SER C  1 112 ? 2.809   -26.418 -4.123  1.00 21.17 ? 111 SER C N   1 
ATOM   7166  C  CA  . SER C  1 112 ? 4.254   -26.435 -3.833  1.00 21.34 ? 111 SER C CA  1 
ATOM   7167  C  C   . SER C  1 112 ? 4.876   -25.048 -3.974  1.00 19.97 ? 111 SER C C   1 
ATOM   7168  O  O   . SER C  1 112 ? 5.606   -24.605 -3.071  1.00 19.72 ? 111 SER C O   1 
ATOM   7169  C  CB  . SER C  1 112 ? 4.991   -27.416 -4.730  1.00 22.73 ? 111 SER C CB  1 
ATOM   7170  O  OG  . SER C  1 112 ? 4.654   -28.751 -4.369  1.00 25.30 ? 111 SER C OG  1 
ATOM   7171  N  N   . LEU C  1 113 ? 4.574   -24.375 -5.083  1.00 18.20 ? 112 LEU C N   1 
ATOM   7172  C  CA  . LEU C  1 113 ? 5.084   -23.023 -5.334  1.00 18.36 ? 112 LEU C CA  1 
ATOM   7173  C  C   . LEU C  1 113 ? 4.672   -22.067 -4.210  1.00 18.18 ? 112 LEU C C   1 
ATOM   7174  O  O   . LEU C  1 113 ? 5.494   -21.331 -3.679  1.00 17.73 ? 112 LEU C O   1 
ATOM   7175  C  CB  . LEU C  1 113 ? 4.597   -22.488 -6.667  1.00 18.12 ? 112 LEU C CB  1 
ATOM   7176  C  CG  . LEU C  1 113 ? 5.242   -23.126 -7.897  1.00 19.35 ? 112 LEU C CG  1 
ATOM   7177  C  CD1 . LEU C  1 113 ? 4.393   -22.841 -9.122  1.00 19.18 ? 112 LEU C CD1 1 
ATOM   7178  C  CD2 . LEU C  1 113 ? 6.630   -22.588 -8.102  1.00 20.08 ? 112 LEU C CD2 1 
ATOM   7179  N  N   . VAL C  1 114 ? 3.403   -22.128 -3.816  1.00 18.11 ? 113 VAL C N   1 
ATOM   7180  C  CA  . VAL C  1 114 ? 2.896   -21.292 -2.734  1.00 19.14 ? 113 VAL C CA  1 
ATOM   7181  C  C   . VAL C  1 114 ? 3.587   -21.631 -1.386  1.00 20.29 ? 113 VAL C C   1 
ATOM   7182  O  O   . VAL C  1 114 ? 4.003   -20.741 -0.635  1.00 20.33 ? 113 VAL C O   1 
ATOM   7183  C  CB  . VAL C  1 114 ? 1.360   -21.379 -2.686  1.00 19.37 ? 113 VAL C CB  1 
ATOM   7184  C  CG1 . VAL C  1 114 ? 0.820   -20.779 -1.395  1.00 20.59 ? 113 VAL C CG1 1 
ATOM   7185  C  CG2 . VAL C  1 114 ? 0.784   -20.679 -3.915  1.00 18.74 ? 113 VAL C CG2 1 
ATOM   7186  N  N   . GLY C  1 115 ? 3.805   -22.924 -1.124  1.00 20.60 ? 114 GLY C N   1 
ATOM   7187  C  CA  . GLY C  1 115 ? 4.585   -23.341 0.040   1.00 21.84 ? 114 GLY C CA  1 
ATOM   7188  C  C   . GLY C  1 115 ? 6.018   -22.829 0.011   1.00 22.38 ? 114 GLY C C   1 
ATOM   7189  O  O   . GLY C  1 115 ? 6.607   -22.629 1.059   1.00 23.53 ? 114 GLY C O   1 
ATOM   7190  N  N   . TRP C  1 116 ? 6.570   -22.591 -1.184  1.00 21.80 ? 115 TRP C N   1 
ATOM   7191  C  CA  . TRP C  1 116 ? 7.923   -22.009 -1.351  1.00 22.28 ? 115 TRP C CA  1 
ATOM   7192  C  C   . TRP C  1 116 ? 7.929   -20.489 -1.317  1.00 21.84 ? 115 TRP C C   1 
ATOM   7193  O  O   . TRP C  1 116 ? 8.989   -19.881 -1.428  1.00 23.77 ? 115 TRP C O   1 
ATOM   7194  C  CB  . TRP C  1 116 ? 8.563   -22.446 -2.683  1.00 22.65 ? 115 TRP C CB  1 
ATOM   7195  C  CG  . TRP C  1 116 ? 8.684   -23.895 -2.852  1.00 23.30 ? 115 TRP C CG  1 
ATOM   7196  C  CD1 . TRP C  1 116 ? 8.739   -24.839 -1.868  1.00 24.56 ? 115 TRP C CD1 1 
ATOM   7197  C  CD2 . TRP C  1 116 ? 8.756   -24.600 -4.090  1.00 22.98 ? 115 TRP C CD2 1 
ATOM   7198  N  NE1 . TRP C  1 116 ? 8.805   -26.091 -2.431  1.00 25.43 ? 115 TRP C NE1 1 
ATOM   7199  C  CE2 . TRP C  1 116 ? 8.821   -25.974 -3.788  1.00 24.16 ? 115 TRP C CE2 1 
ATOM   7200  C  CE3 . TRP C  1 116 ? 8.748   -24.204 -5.431  1.00 23.10 ? 115 TRP C CE3 1 
ATOM   7201  C  CZ2 . TRP C  1 116 ? 8.899   -26.965 -4.785  1.00 24.67 ? 115 TRP C CZ2 1 
ATOM   7202  C  CZ3 . TRP C  1 116 ? 8.806   -25.182 -6.420  1.00 22.81 ? 115 TRP C CZ3 1 
ATOM   7203  C  CH2 . TRP C  1 116 ? 8.878   -26.550 -6.084  1.00 23.73 ? 115 TRP C CH2 1 
ATOM   7204  N  N   . GLY C  1 117 ? 6.761   -19.868 -1.175  1.00 20.73 ? 116 GLY C N   1 
ATOM   7205  C  CA  . GLY C  1 117 ? 6.685   -18.434 -1.016  1.00 20.50 ? 116 GLY C CA  1 
ATOM   7206  C  C   . GLY C  1 117 ? 6.034   -17.648 -2.132  1.00 19.34 ? 116 GLY C C   1 
ATOM   7207  O  O   . GLY C  1 117 ? 5.981   -16.414 -2.039  1.00 19.80 ? 116 GLY C O   1 
ATOM   7208  N  N   . TYR C  1 118 ? 5.509   -18.331 -3.152  1.00 18.56 ? 117 TYR C N   1 
ATOM   7209  C  CA  . TYR C  1 118 ? 4.819   -17.672 -4.258  1.00 17.32 ? 117 TYR C CA  1 
ATOM   7210  C  C   . TYR C  1 118 ? 3.407   -17.285 -3.867  1.00 17.50 ? 117 TYR C C   1 
ATOM   7211  O  O   . TYR C  1 118 ? 2.849   -17.861 -2.942  1.00 17.00 ? 117 TYR C O   1 
ATOM   7212  C  CB  . TYR C  1 118 ? 4.801   -18.569 -5.520  1.00 17.33 ? 117 TYR C CB  1 
ATOM   7213  C  CG  . TYR C  1 118 ? 6.132   -18.570 -6.250  1.00 17.68 ? 117 TYR C CG  1 
ATOM   7214  C  CD1 . TYR C  1 118 ? 7.171   -19.415 -5.859  1.00 18.43 ? 117 TYR C CD1 1 
ATOM   7215  C  CD2 . TYR C  1 118 ? 6.369   -17.696 -7.299  1.00 18.10 ? 117 TYR C CD2 1 
ATOM   7216  C  CE1 . TYR C  1 118 ? 8.403   -19.409 -6.514  1.00 19.29 ? 117 TYR C CE1 1 
ATOM   7217  C  CE2 . TYR C  1 118 ? 7.603   -17.688 -7.972  1.00 18.51 ? 117 TYR C CE2 1 
ATOM   7218  C  CZ  . TYR C  1 118 ? 8.630   -18.517 -7.555  1.00 19.35 ? 117 TYR C CZ  1 
ATOM   7219  O  OH  . TYR C  1 118 ? 9.877   -18.500 -8.218  1.00 19.96 ? 117 TYR C OH  1 
ATOM   7220  N  N   . THR C  1 119 ? 2.860   -16.329 -4.609  1.00 16.52 ? 118 THR C N   1 
ATOM   7221  C  CA  . THR C  1 119 ? 1.544   -15.734 -4.345  1.00 16.41 ? 118 THR C CA  1 
ATOM   7222  C  C   . THR C  1 119 ? 0.703   -15.782 -5.636  1.00 15.90 ? 118 THR C C   1 
ATOM   7223  O  O   . THR C  1 119 ? 1.105   -15.216 -6.645  1.00 15.54 ? 118 THR C O   1 
ATOM   7224  C  CB  . THR C  1 119 ? 1.697   -14.275 -3.863  1.00 16.52 ? 118 THR C CB  1 
ATOM   7225  O  OG1 . THR C  1 119 ? 2.424   -14.255 -2.626  1.00 16.82 ? 118 THR C OG1 1 
ATOM   7226  C  CG2 . THR C  1 119 ? 0.337   -13.633 -3.622  1.00 16.86 ? 118 THR C CG2 1 
ATOM   7227  N  N   . ARG C  1 120 ? -0.424  -16.485 -5.596  1.00 16.02 ? 119 ARG C N   1 
ATOM   7228  C  CA  . ARG C  1 120 ? -1.271  -16.661 -6.761  1.00 16.70 ? 119 ARG C CA  1 
ATOM   7229  C  C   . ARG C  1 120 ? -1.698  -15.319 -7.303  1.00 16.75 ? 119 ARG C C   1 
ATOM   7230  O  O   . ARG C  1 120 ? -2.150  -14.452 -6.562  1.00 17.21 ? 119 ARG C O   1 
ATOM   7231  C  CB  . ARG C  1 120 ? -2.509  -17.495 -6.418  1.00 17.87 ? 119 ARG C CB  1 
ATOM   7232  C  CG  . ARG C  1 120 ? -2.280  -18.979 -6.153  1.00 18.04 ? 119 ARG C CG  1 
ATOM   7233  C  CD  . ARG C  1 120 ? -3.586  -19.596 -5.614  1.00 19.03 ? 119 ARG C CD  1 
ATOM   7234  N  NE  . ARG C  1 120 ? -3.495  -21.034 -5.470  1.00 19.56 ? 119 ARG C NE  1 
ATOM   7235  C  CZ  . ARG C  1 120 ? -3.128  -21.686 -4.369  1.00 21.18 ? 119 ARG C CZ  1 
ATOM   7236  N  NH1 . ARG C  1 120 ? -2.779  -21.048 -3.252  1.00 22.42 ? 119 ARG C NH1 1 
ATOM   7237  N  NH2 . ARG C  1 120 ? -3.104  -23.025 -4.385  1.00 22.08 ? 119 ARG C NH2 1 
ATOM   7238  N  N   . GLY C  1 121 ? -1.533  -15.146 -8.594  1.00 16.26 ? 120 GLY C N   1 
ATOM   7239  C  CA  . GLY C  1 121 ? -1.989  -13.935 -9.244  1.00 16.98 ? 120 GLY C CA  1 
ATOM   7240  C  C   . GLY C  1 121 ? -0.997  -12.808 -9.198  1.00 18.23 ? 120 GLY C C   1 
ATOM   7241  O  O   . GLY C  1 121 ? -1.249  -11.761 -9.788  1.00 17.91 ? 120 GLY C O   1 
ATOM   7242  N  N   . GLU C  1 122 ? 0.105   -12.993 -8.458  1.00 18.79 ? 121 GLU C N   1 
ATOM   7243  C  CA  . GLU C  1 122 ? 1.135   -11.987 -8.329  1.00 19.61 ? 121 GLU C CA  1 
ATOM   7244  C  C   . GLU C  1 122 ? 2.400   -12.533 -9.009  1.00 17.84 ? 121 GLU C C   1 
ATOM   7245  O  O   . GLU C  1 122 ? 2.524   -12.403 -10.234 1.00 16.91 ? 121 GLU C O   1 
ATOM   7246  C  CB  . GLU C  1 122 ? 1.344   -11.585 -6.864  1.00 22.99 ? 121 GLU C CB  1 
ATOM   7247  C  CG  . GLU C  1 122 ? 0.115   -10.848 -6.317  1.00 27.27 ? 121 GLU C CG  1 
ATOM   7248  C  CD  . GLU C  1 122 ? 0.422   -10.075 -5.039  1.00 35.65 ? 121 GLU C CD  1 
ATOM   7249  O  OE1 . GLU C  1 122 ? 1.615   -10.022 -4.660  1.00 43.25 ? 121 GLU C OE1 1 
ATOM   7250  O  OE2 . GLU C  1 122 ? -0.499  -9.541  -4.374  1.00 39.70 ? 121 GLU C OE2 1 
ATOM   7251  N  N   . ASP C  1 123 ? 3.265   -13.216 -8.268  1.00 16.55 ? 122 ASP C N   1 
ATOM   7252  C  CA  . ASP C  1 123 ? 4.510   -13.728 -8.874  1.00 16.65 ? 122 ASP C CA  1 
ATOM   7253  C  C   . ASP C  1 123 ? 4.407   -15.153 -9.448  1.00 16.10 ? 122 ASP C C   1 
ATOM   7254  O  O   . ASP C  1 123 ? 5.379   -15.657 -10.025 1.00 15.31 ? 122 ASP C O   1 
ATOM   7255  C  CB  . ASP C  1 123 ? 5.697   -13.560 -7.927  1.00 17.63 ? 122 ASP C CB  1 
ATOM   7256  C  CG  . ASP C  1 123 ? 5.488   -14.222 -6.581  1.00 18.68 ? 122 ASP C CG  1 
ATOM   7257  O  OD1 . ASP C  1 123 ? 4.418   -14.835 -6.362  1.00 19.05 ? 122 ASP C OD1 1 
ATOM   7258  O  OD2 . ASP C  1 123 ? 6.388   -14.101 -5.733  1.00 20.01 ? 122 ASP C OD2 1 
ATOM   7259  N  N   . VAL C  1 124 ? 3.243   -15.802 -9.312  1.00 15.14 ? 123 VAL C N   1 
ATOM   7260  C  CA  . VAL C  1 124 ? 2.912   -16.979 -10.125 1.00 15.20 ? 123 VAL C CA  1 
ATOM   7261  C  C   . VAL C  1 124 ? 1.564   -16.732 -10.783 1.00 15.12 ? 123 VAL C C   1 
ATOM   7262  O  O   . VAL C  1 124 ? 0.573   -16.415 -10.120 1.00 15.03 ? 123 VAL C O   1 
ATOM   7263  C  CB  . VAL C  1 124 ? 2.933   -18.338 -9.373  1.00 16.12 ? 123 VAL C CB  1 
ATOM   7264  C  CG1 . VAL C  1 124 ? 1.966   -18.341 -8.189  1.00 17.17 ? 123 VAL C CG1 1 
ATOM   7265  C  CG2 . VAL C  1 124 ? 2.632   -19.467 -10.340 1.00 16.02 ? 123 VAL C CG2 1 
ATOM   7266  N  N   . ARG C  1 125 ? 1.545   -16.809 -12.106 1.00 14.54 ? 124 ARG C N   1 
ATOM   7267  C  CA  . ARG C  1 125 ? 0.328   -16.550 -12.877 1.00 15.04 ? 124 ARG C CA  1 
ATOM   7268  C  C   . ARG C  1 125 ? 0.139   -17.619 -13.955 1.00 14.84 ? 124 ARG C C   1 
ATOM   7269  O  O   . ARG C  1 125 ? 1.111   -18.132 -14.514 1.00 15.24 ? 124 ARG C O   1 
ATOM   7270  C  CB  . ARG C  1 125 ? 0.380   -15.177 -13.541 1.00 15.24 ? 124 ARG C CB  1 
ATOM   7271  C  CG  . ARG C  1 125 ? 0.574   -14.017 -12.583 1.00 16.80 ? 124 ARG C CG  1 
ATOM   7272  C  CD  . ARG C  1 125 ? 0.405   -12.660 -13.245 1.00 17.23 ? 124 ARG C CD  1 
ATOM   7273  N  NE  . ARG C  1 125 ? 0.895   -11.592 -12.384 1.00 18.25 ? 124 ARG C NE  1 
ATOM   7274  C  CZ  . ARG C  1 125 ? 0.803   -10.293 -12.663 1.00 19.78 ? 124 ARG C CZ  1 
ATOM   7275  N  NH1 . ARG C  1 125 ? 0.197   -9.914  -13.784 1.00 21.34 ? 124 ARG C NH1 1 
ATOM   7276  N  NH2 . ARG C  1 125 ? 1.324   -9.380  -11.839 1.00 19.80 ? 124 ARG C NH2 1 
ATOM   7277  N  N   . GLY C  1 126 ? -1.111  -17.961 -14.224 1.00 14.74 ? 125 GLY C N   1 
ATOM   7278  C  CA  . GLY C  1 126 ? -1.442  -18.863 -15.328 1.00 15.11 ? 125 GLY C CA  1 
ATOM   7279  C  C   . GLY C  1 126 ? -1.694  -18.148 -16.638 1.00 14.78 ? 125 GLY C C   1 
ATOM   7280  O  O   . GLY C  1 126 ? -2.161  -16.992 -16.661 1.00 14.53 ? 125 GLY C O   1 
ATOM   7281  N  N   . ALA C  1 127 ? -1.404  -18.861 -17.733 1.00 13.78 ? 126 ALA C N   1 
ATOM   7282  C  CA  . ALA C  1 127 ? -1.681  -18.399 -19.066 1.00 13.90 ? 126 ALA C CA  1 
ATOM   7283  C  C   . ALA C  1 127 ? -2.586  -19.414 -19.783 1.00 13.99 ? 126 ALA C C   1 
ATOM   7284  O  O   . ALA C  1 127 ? -2.177  -20.069 -20.752 1.00 14.30 ? 126 ALA C O   1 
ATOM   7285  C  CB  . ALA C  1 127 ? -0.389  -18.159 -19.823 1.00 13.84 ? 126 ALA C CB  1 
ATOM   7286  N  N   . PRO C  1 128 ? -3.823  -19.585 -19.270 1.00 14.03 ? 127 PRO C N   1 
ATOM   7287  C  CA  . PRO C  1 128 ? -4.809  -20.452 -19.957 1.00 14.25 ? 127 PRO C CA  1 
ATOM   7288  C  C   . PRO C  1 128 ? -5.234  -19.924 -21.339 1.00 14.17 ? 127 PRO C C   1 
ATOM   7289  O  O   . PRO C  1 128 ? -5.160  -18.721 -21.612 1.00 14.20 ? 127 PRO C O   1 
ATOM   7290  C  CB  . PRO C  1 128 ? -6.018  -20.435 -18.996 1.00 14.30 ? 127 PRO C CB  1 
ATOM   7291  C  CG  . PRO C  1 128 ? -5.937  -19.086 -18.371 1.00 14.57 ? 127 PRO C CG  1 
ATOM   7292  C  CD  . PRO C  1 128 ? -4.453  -18.867 -18.147 1.00 14.23 ? 127 PRO C CD  1 
ATOM   7293  N  N   . TYR C  1 129 ? -5.687  -20.835 -22.197 1.00 13.91 ? 128 TYR C N   1 
ATOM   7294  C  CA  . TYR C  1 129 ? -6.057  -20.476 -23.561 1.00 14.51 ? 128 TYR C CA  1 
ATOM   7295  C  C   . TYR C  1 129 ? -7.131  -21.404 -24.077 1.00 14.69 ? 128 TYR C C   1 
ATOM   7296  O  O   . TYR C  1 129 ? -7.442  -22.428 -23.443 1.00 14.02 ? 128 TYR C O   1 
ATOM   7297  C  CB  . TYR C  1 129 ? -4.829  -20.472 -24.501 1.00 14.25 ? 128 TYR C CB  1 
ATOM   7298  C  CG  . TYR C  1 129 ? -4.074  -21.781 -24.536 1.00 14.21 ? 128 TYR C CG  1 
ATOM   7299  C  CD1 . TYR C  1 129 ? -3.143  -22.101 -23.544 1.00 14.39 ? 128 TYR C CD1 1 
ATOM   7300  C  CD2 . TYR C  1 129 ? -4.288  -22.725 -25.554 1.00 13.81 ? 128 TYR C CD2 1 
ATOM   7301  C  CE1 . TYR C  1 129 ? -2.456  -23.317 -23.577 1.00 15.00 ? 128 TYR C CE1 1 
ATOM   7302  C  CE2 . TYR C  1 129 ? -3.616  -23.935 -25.580 1.00 13.49 ? 128 TYR C CE2 1 
ATOM   7303  C  CZ  . TYR C  1 129 ? -2.694  -24.236 -24.604 1.00 14.56 ? 128 TYR C CZ  1 
ATOM   7304  O  OH  . TYR C  1 129 ? -2.023  -25.468 -24.598 1.00 14.89 ? 128 TYR C OH  1 
ATOM   7305  N  N   . ASP C  1 130 ? -7.705  -21.053 -25.229 1.00 14.73 ? 129 ASP C N   1 
ATOM   7306  C  CA  . ASP C  1 130 ? -8.690  -21.934 -25.856 1.00 15.37 ? 129 ASP C CA  1 
ATOM   7307  C  C   . ASP C  1 130 ? -7.903  -23.046 -26.573 1.00 14.74 ? 129 ASP C C   1 
ATOM   7308  O  O   . ASP C  1 130 ? -7.497  -22.907 -27.735 1.00 14.69 ? 129 ASP C O   1 
ATOM   7309  C  CB  . ASP C  1 130 ? -9.572  -21.161 -26.834 1.00 16.70 ? 129 ASP C CB  1 
ATOM   7310  C  CG  . ASP C  1 130 ? -10.702 -22.012 -27.381 1.00 18.11 ? 129 ASP C CG  1 
ATOM   7311  O  OD1 . ASP C  1 130 ? -10.653 -23.279 -27.254 1.00 17.41 ? 129 ASP C OD1 1 
ATOM   7312  O  OD2 . ASP C  1 130 ? -11.664 -21.411 -27.911 1.00 19.10 ? 129 ASP C OD2 1 
ATOM   7313  N  N   . TRP C  1 131 ? -7.704  -24.145 -25.856 1.00 14.46 ? 130 TRP C N   1 
ATOM   7314  C  CA  . TRP C  1 131 ? -6.871  -25.260 -26.309 1.00 14.53 ? 130 TRP C CA  1 
ATOM   7315  C  C   . TRP C  1 131 ? -7.501  -26.092 -27.444 1.00 14.90 ? 130 TRP C C   1 
ATOM   7316  O  O   . TRP C  1 131 ? -6.867  -27.026 -27.939 1.00 14.37 ? 130 TRP C O   1 
ATOM   7317  C  CB  . TRP C  1 131 ? -6.488  -26.165 -25.125 1.00 15.15 ? 130 TRP C CB  1 
ATOM   7318  C  CG  . TRP C  1 131 ? -7.569  -26.323 -24.111 1.00 15.28 ? 130 TRP C CG  1 
ATOM   7319  C  CD1 . TRP C  1 131 ? -7.647  -25.682 -22.885 1.00 15.81 ? 130 TRP C CD1 1 
ATOM   7320  C  CD2 . TRP C  1 131 ? -8.771  -27.089 -24.232 1.00 15.26 ? 130 TRP C CD2 1 
ATOM   7321  N  NE1 . TRP C  1 131 ? -8.781  -26.048 -22.237 1.00 15.66 ? 130 TRP C NE1 1 
ATOM   7322  C  CE2 . TRP C  1 131 ? -9.502  -26.900 -23.031 1.00 15.42 ? 130 TRP C CE2 1 
ATOM   7323  C  CE3 . TRP C  1 131 ? -9.294  -27.954 -25.220 1.00 15.42 ? 130 TRP C CE3 1 
ATOM   7324  C  CZ2 . TRP C  1 131 ? -10.747 -27.503 -22.795 1.00 15.79 ? 130 TRP C CZ2 1 
ATOM   7325  C  CZ3 . TRP C  1 131 ? -10.530 -28.584 -24.973 1.00 16.55 ? 130 TRP C CZ3 1 
ATOM   7326  C  CH2 . TRP C  1 131 ? -11.241 -28.346 -23.772 1.00 16.58 ? 130 TRP C CH2 1 
ATOM   7327  N  N   . ARG C  1 132 ? -8.726  -25.748 -27.870 1.00 14.94 ? 131 ARG C N   1 
ATOM   7328  C  CA  . ARG C  1 132 ? -9.325  -26.388 -29.037 1.00 15.85 ? 131 ARG C CA  1 
ATOM   7329  C  C   . ARG C  1 132 ? -8.687  -25.889 -30.323 1.00 16.05 ? 131 ARG C C   1 
ATOM   7330  O  O   . ARG C  1 132 ? -8.737  -26.564 -31.356 1.00 15.91 ? 131 ARG C O   1 
ATOM   7331  C  CB  . ARG C  1 132 ? -10.832 -26.122 -29.075 1.00 16.49 ? 131 ARG C CB  1 
ATOM   7332  C  CG  . ARG C  1 132 ? -11.573 -26.682 -27.865 1.00 16.86 ? 131 ARG C CG  1 
ATOM   7333  C  CD  . ARG C  1 132 ? -13.002 -26.178 -27.801 1.00 16.98 ? 131 ARG C CD  1 
ATOM   7334  N  NE  . ARG C  1 132 ? -13.057 -24.721 -27.823 1.00 17.80 ? 131 ARG C NE  1 
ATOM   7335  C  CZ  . ARG C  1 132 ? -14.142 -24.003 -28.098 1.00 20.03 ? 131 ARG C CZ  1 
ATOM   7336  N  NH1 . ARG C  1 132 ? -15.302 -24.604 -28.368 1.00 20.07 ? 131 ARG C NH1 1 
ATOM   7337  N  NH2 . ARG C  1 132 ? -14.065 -22.672 -28.123 1.00 20.94 ? 131 ARG C NH2 1 
ATOM   7338  N  N   . ARG C  1 133 ? -8.096  -24.700 -30.261 1.00 16.57 ? 132 ARG C N   1 
ATOM   7339  C  CA  . ARG C  1 133 ? -7.482  -24.062 -31.395 1.00 17.40 ? 132 ARG C CA  1 
ATOM   7340  C  C   . ARG C  1 133 ? -5.967  -24.216 -31.352 1.00 17.43 ? 132 ARG C C   1 
ATOM   7341  O  O   . ARG C  1 133 ? -5.377  -24.461 -30.295 1.00 17.52 ? 132 ARG C O   1 
ATOM   7342  C  CB  . ARG C  1 133 ? -7.869  -22.582 -31.437 1.00 18.80 ? 132 ARG C CB  1 
ATOM   7343  C  CG  . ARG C  1 133 ? -9.298  -22.413 -31.907 1.00 21.02 ? 132 ARG C CG  1 
ATOM   7344  C  CD  . ARG C  1 133 ? -9.872  -21.043 -31.634 1.00 23.97 ? 132 ARG C CD  1 
ATOM   7345  N  NE  . ARG C  1 133 ? -10.951 -20.771 -32.590 1.00 25.39 ? 132 ARG C NE  1 
ATOM   7346  C  CZ  . ARG C  1 133 ? -11.761 -19.727 -32.529 1.00 28.25 ? 132 ARG C CZ  1 
ATOM   7347  N  NH1 . ARG C  1 133 ? -11.654 -18.843 -31.547 1.00 29.61 ? 132 ARG C NH1 1 
ATOM   7348  N  NH2 . ARG C  1 133 ? -12.692 -19.574 -33.453 1.00 29.31 ? 132 ARG C NH2 1 
ATOM   7349  N  N   . ALA C  1 134 ? -5.362  -24.065 -32.523 1.00 16.93 ? 133 ALA C N   1 
ATOM   7350  C  CA  . ALA C  1 134 ? -3.930  -24.033 -32.648 1.00 17.17 ? 133 ALA C CA  1 
ATOM   7351  C  C   . ALA C  1 134 ? -3.492  -22.586 -32.606 1.00 17.49 ? 133 ALA C C   1 
ATOM   7352  O  O   . ALA C  1 134 ? -4.324  -21.657 -32.630 1.00 17.69 ? 133 ALA C O   1 
ATOM   7353  C  CB  . ALA C  1 134 ? -3.499  -24.702 -33.950 1.00 17.89 ? 133 ALA C CB  1 
ATOM   7354  N  N   . PRO C  1 135 ? -2.187  -22.345 -32.552 1.00 16.81 ? 134 PRO C N   1 
ATOM   7355  C  CA  . PRO C  1 135 ? -1.754  -20.943 -32.378 1.00 17.19 ? 134 PRO C CA  1 
ATOM   7356  C  C   . PRO C  1 135 ? -2.194  -19.917 -33.416 1.00 18.10 ? 134 PRO C C   1 
ATOM   7357  O  O   . PRO C  1 135 ? -2.270  -18.702 -33.084 1.00 18.72 ? 134 PRO C O   1 
ATOM   7358  C  CB  . PRO C  1 135 ? -0.225  -21.061 -32.338 1.00 16.64 ? 134 PRO C CB  1 
ATOM   7359  C  CG  . PRO C  1 135 ? -0.023  -22.415 -31.738 1.00 16.62 ? 134 PRO C CG  1 
ATOM   7360  C  CD  . PRO C  1 135 ? -1.080  -23.286 -32.344 1.00 16.52 ? 134 PRO C CD  1 
ATOM   7361  N  N   . ASN C  1 136 ? -2.472  -20.364 -34.645 1.00 19.04 ? 135 ASN C N   1 
ATOM   7362  C  CA  . ASN C  1 136 ? -2.886  -19.458 -35.708 1.00 20.63 ? 135 ASN C CA  1 
ATOM   7363  C  C   . ASN C  1 136 ? -4.191  -18.727 -35.389 1.00 21.38 ? 135 ASN C C   1 
ATOM   7364  O  O   . ASN C  1 136 ? -4.451  -17.680 -35.965 1.00 21.36 ? 135 ASN C O   1 
ATOM   7365  C  CB  . ASN C  1 136 ? -3.025  -20.185 -37.066 1.00 21.23 ? 135 ASN C CB  1 
ATOM   7366  C  CG  . ASN C  1 136 ? -4.038  -21.329 -37.039 1.00 21.81 ? 135 ASN C CG  1 
ATOM   7367  O  OD1 . ASN C  1 136 ? -4.139  -22.073 -36.073 1.00 21.57 ? 135 ASN C OD1 1 
ATOM   7368  N  ND2 . ASN C  1 136 ? -4.782  -21.491 -38.130 1.00 22.58 ? 135 ASN C ND2 1 
ATOM   7369  N  N   . GLU C  1 137 ? -5.000  -19.290 -34.490 1.00 20.91 ? 136 GLU C N   1 
ATOM   7370  C  CA  . GLU C  1 137 ? -6.244  -18.663 -34.095 1.00 22.47 ? 136 GLU C CA  1 
ATOM   7371  C  C   . GLU C  1 137 ? -6.259  -18.202 -32.624 1.00 22.37 ? 136 GLU C C   1 
ATOM   7372  O  O   . GLU C  1 137 ? -7.319  -18.066 -32.029 1.00 24.09 ? 136 GLU C O   1 
ATOM   7373  C  CB  . GLU C  1 137 ? -7.403  -19.623 -34.394 1.00 23.25 ? 136 GLU C CB  1 
ATOM   7374  C  CG  . GLU C  1 137 ? -7.544  -19.873 -35.892 1.00 25.74 ? 136 GLU C CG  1 
ATOM   7375  C  CD  . GLU C  1 137 ? -8.780  -20.668 -36.272 1.00 28.16 ? 136 GLU C CD  1 
ATOM   7376  O  OE1 . GLU C  1 137 ? -8.910  -21.867 -35.921 1.00 28.38 ? 136 GLU C OE1 1 
ATOM   7377  O  OE2 . GLU C  1 137 ? -9.640  -20.067 -36.934 1.00 32.68 ? 136 GLU C OE2 1 
ATOM   7378  N  N   . ASN C  1 138 ? -5.090  -17.956 -32.054 1.00 20.77 ? 137 ASN C N   1 
ATOM   7379  C  CA  . ASN C  1 138 ? -4.974  -17.488 -30.691 1.00 19.91 ? 137 ASN C CA  1 
ATOM   7380  C  C   . ASN C  1 138 ? -4.030  -16.281 -30.591 1.00 20.23 ? 137 ASN C C   1 
ATOM   7381  O  O   . ASN C  1 138 ? -3.327  -16.106 -29.608 1.00 19.67 ? 137 ASN C O   1 
ATOM   7382  C  CB  . ASN C  1 138 ? -4.554  -18.652 -29.763 1.00 19.60 ? 137 ASN C CB  1 
ATOM   7383  C  CG  . ASN C  1 138 ? -5.728  -19.244 -29.022 1.00 20.72 ? 137 ASN C CG  1 
ATOM   7384  O  OD1 . ASN C  1 138 ? -6.613  -18.497 -28.601 1.00 24.16 ? 137 ASN C OD1 1 
ATOM   7385  N  ND2 . ASN C  1 138 ? -5.782  -20.563 -28.890 1.00 18.87 ? 137 ASN C ND2 1 
ATOM   7386  N  N   . GLY C  1 139 ? -4.060  -15.431 -31.619 1.00 20.87 ? 138 GLY C N   1 
ATOM   7387  C  CA  . GLY C  1 139 ? -3.261  -14.197 -31.653 1.00 20.90 ? 138 GLY C CA  1 
ATOM   7388  C  C   . GLY C  1 139 ? -3.409  -13.336 -30.411 1.00 20.27 ? 138 GLY C C   1 
ATOM   7389  O  O   . GLY C  1 139 ? -2.407  -12.928 -29.814 1.00 19.88 ? 138 GLY C O   1 
ATOM   7390  N  N   . PRO C  1 140 ? -4.657  -13.037 -30.006 1.00 20.16 ? 139 PRO C N   1 
ATOM   7391  C  CA  . PRO C  1 140 ? -4.850  -12.195 -28.809 1.00 20.16 ? 139 PRO C CA  1 
ATOM   7392  C  C   . PRO C  1 140 ? -4.211  -12.773 -27.519 1.00 18.82 ? 139 PRO C C   1 
ATOM   7393  O  O   . PRO C  1 140 ? -3.640  -12.026 -26.702 1.00 17.23 ? 139 PRO C O   1 
ATOM   7394  C  CB  . PRO C  1 140 ? -6.372  -12.084 -28.714 1.00 21.12 ? 139 PRO C CB  1 
ATOM   7395  C  CG  . PRO C  1 140 ? -6.817  -12.193 -30.155 1.00 22.09 ? 139 PRO C CG  1 
ATOM   7396  C  CD  . PRO C  1 140 ? -5.918  -13.240 -30.752 1.00 21.25 ? 139 PRO C CD  1 
ATOM   7397  N  N   . TYR C  1 141 ? -4.264  -14.094 -27.371 1.00 17.11 ? 140 TYR C N   1 
ATOM   7398  C  CA  . TYR C  1 141 ? -3.592  -14.761 -26.264 1.00 16.77 ? 140 TYR C CA  1 
ATOM   7399  C  C   . TYR C  1 141 ? -2.109  -14.442 -26.222 1.00 16.02 ? 140 TYR C C   1 
ATOM   7400  O  O   . TYR C  1 141 ? -1.567  -14.137 -25.144 1.00 15.95 ? 140 TYR C O   1 
ATOM   7401  C  CB  . TYR C  1 141 ? -3.788  -16.278 -26.372 1.00 16.19 ? 140 TYR C CB  1 
ATOM   7402  C  CG  . TYR C  1 141 ? -2.918  -17.105 -25.467 1.00 15.51 ? 140 TYR C CG  1 
ATOM   7403  C  CD1 . TYR C  1 141 ? -3.252  -17.278 -24.109 1.00 15.01 ? 140 TYR C CD1 1 
ATOM   7404  C  CD2 . TYR C  1 141 ? -1.751  -17.701 -25.934 1.00 14.75 ? 140 TYR C CD2 1 
ATOM   7405  C  CE1 . TYR C  1 141 ? -2.454  -18.033 -23.278 1.00 14.80 ? 140 TYR C CE1 1 
ATOM   7406  C  CE2 . TYR C  1 141 ? -0.959  -18.465 -25.100 1.00 14.24 ? 140 TYR C CE2 1 
ATOM   7407  C  CZ  . TYR C  1 141 ? -1.313  -18.636 -23.776 1.00 14.17 ? 140 TYR C CZ  1 
ATOM   7408  O  OH  . TYR C  1 141 ? -0.541  -19.432 -22.950 1.00 14.31 ? 140 TYR C OH  1 
ATOM   7409  N  N   . PHE C  1 142 ? -1.440  -14.503 -27.373 1.00 15.66 ? 141 PHE C N   1 
ATOM   7410  C  CA  . PHE C  1 142 ? 0.016   -14.282 -27.391 1.00 15.42 ? 141 PHE C CA  1 
ATOM   7411  C  C   . PHE C  1 142 ? 0.353   -12.830 -27.077 1.00 16.35 ? 141 PHE C C   1 
ATOM   7412  O  O   . PHE C  1 142 ? 1.395   -12.552 -26.450 1.00 15.38 ? 141 PHE C O   1 
ATOM   7413  C  CB  . PHE C  1 142 ? 0.650   -14.729 -28.697 1.00 15.95 ? 141 PHE C CB  1 
ATOM   7414  C  CG  . PHE C  1 142 ? 0.561   -16.208 -28.915 1.00 15.47 ? 141 PHE C CG  1 
ATOM   7415  C  CD1 . PHE C  1 142 ? 1.247   -17.075 -28.097 1.00 15.51 ? 141 PHE C CD1 1 
ATOM   7416  C  CD2 . PHE C  1 142 ? -0.273  -16.735 -29.890 1.00 16.20 ? 141 PHE C CD2 1 
ATOM   7417  C  CE1 . PHE C  1 142 ? 1.123   -18.444 -28.251 1.00 15.51 ? 141 PHE C CE1 1 
ATOM   7418  C  CE2 . PHE C  1 142 ? -0.389  -18.110 -30.066 1.00 15.89 ? 141 PHE C CE2 1 
ATOM   7419  C  CZ  . PHE C  1 142 ? 0.319   -18.964 -29.242 1.00 15.51 ? 141 PHE C CZ  1 
ATOM   7420  N  N   . LEU C  1 143 ? -0.497  -11.900 -27.503 1.00 16.35 ? 142 LEU C N   1 
ATOM   7421  C  CA  . LEU C  1 143 ? -0.288  -10.492 -27.102 1.00 18.81 ? 142 LEU C CA  1 
ATOM   7422  C  C   . LEU C  1 143 ? -0.422  -10.307 -25.592 1.00 17.87 ? 142 LEU C C   1 
ATOM   7423  O  O   . LEU C  1 143 ? 0.410   -9.657  -24.982 1.00 17.07 ? 142 LEU C O   1 
ATOM   7424  C  CB  . LEU C  1 143 ? -1.240  -9.555  -27.831 1.00 21.60 ? 142 LEU C CB  1 
ATOM   7425  C  CG  . LEU C  1 143 ? -1.142  -8.063  -27.448 1.00 25.16 ? 142 LEU C CG  1 
ATOM   7426  C  CD1 . LEU C  1 143 ? 0.267   -7.514  -27.693 1.00 27.19 ? 142 LEU C CD1 1 
ATOM   7427  C  CD2 . LEU C  1 143 ? -2.173  -7.141  -28.126 1.00 27.73 ? 142 LEU C CD2 1 
ATOM   7428  N  N   . ALA C  1 144 ? -1.455  -10.903 -25.005 1.00 16.68 ? 143 ALA C N   1 
ATOM   7429  C  CA  . ALA C  1 144 ? -1.661  -10.836 -23.557 1.00 16.74 ? 143 ALA C CA  1 
ATOM   7430  C  C   . ALA C  1 144 ? -0.524  -11.514 -22.797 1.00 16.84 ? 143 ALA C C   1 
ATOM   7431  O  O   . ALA C  1 144 ? -0.114  -11.026 -21.748 1.00 16.98 ? 143 ALA C O   1 
ATOM   7432  C  CB  . ALA C  1 144 ? -2.975  -11.483 -23.187 1.00 17.02 ? 143 ALA C CB  1 
ATOM   7433  N  N   . LEU C  1 145 ? -0.037  -12.639 -23.306 1.00 15.63 ? 144 LEU C N   1 
ATOM   7434  C  CA  . LEU C  1 145 ? 1.092   -13.320 -22.685 1.00 15.74 ? 144 LEU C CA  1 
ATOM   7435  C  C   . LEU C  1 145 ? 2.347   -12.458 -22.676 1.00 16.15 ? 144 LEU C C   1 
ATOM   7436  O  O   . LEU C  1 145 ? 3.030   -12.320 -21.641 1.00 15.43 ? 144 LEU C O   1 
ATOM   7437  C  CB  . LEU C  1 145 ? 1.357   -14.645 -23.413 1.00 16.02 ? 144 LEU C CB  1 
ATOM   7438  C  CG  . LEU C  1 145 ? 2.539   -15.508 -22.967 1.00 16.62 ? 144 LEU C CG  1 
ATOM   7439  C  CD1 . LEU C  1 145 ? 2.383   -15.882 -21.513 1.00 16.99 ? 144 LEU C CD1 1 
ATOM   7440  C  CD2 . LEU C  1 145 ? 2.664   -16.761 -23.826 1.00 17.55 ? 144 LEU C CD2 1 
ATOM   7441  N  N   . ARG C  1 146 ? 2.638   -11.846 -23.814 1.00 16.12 ? 145 ARG C N   1 
ATOM   7442  C  CA  . ARG C  1 146 ? 3.782   -10.940 -23.885 1.00 18.31 ? 145 ARG C CA  1 
ATOM   7443  C  C   . ARG C  1 146 ? 3.642   -9.790  -22.881 1.00 17.29 ? 145 ARG C C   1 
ATOM   7444  O  O   . ARG C  1 146 ? 4.582   -9.452  -22.177 1.00 15.88 ? 145 ARG C O   1 
ATOM   7445  C  CB  . ARG C  1 146 ? 3.951   -10.393 -25.315 1.00 21.20 ? 145 ARG C CB  1 
ATOM   7446  C  CG  . ARG C  1 146 ? 5.088   -9.402  -25.487 1.00 25.30 ? 145 ARG C CG  1 
ATOM   7447  C  CD  . ARG C  1 146 ? 5.204   -8.934  -26.940 1.00 29.38 ? 145 ARG C CD  1 
ATOM   7448  N  NE  . ARG C  1 146 ? 6.017   -7.718  -27.026 1.00 36.28 ? 145 ARG C NE  1 
ATOM   7449  C  CZ  . ARG C  1 146 ? 7.179   -7.581  -27.692 1.00 41.31 ? 145 ARG C CZ  1 
ATOM   7450  N  NH1 . ARG C  1 146 ? 7.752   -8.597  -28.366 1.00 40.29 ? 145 ARG C NH1 1 
ATOM   7451  N  NH2 . ARG C  1 146 ? 7.781   -6.389  -27.691 1.00 42.99 ? 145 ARG C NH2 1 
ATOM   7452  N  N   . GLU C  1 147 ? 2.481   -9.169  -22.845 1.00 17.42 ? 146 GLU C N   1 
ATOM   7453  C  CA  . GLU C  1 147 ? 2.239   -8.079  -21.920 1.00 18.61 ? 146 GLU C CA  1 
ATOM   7454  C  C   . GLU C  1 147 ? 2.354   -8.511  -20.459 1.00 17.38 ? 146 GLU C C   1 
ATOM   7455  O  O   . GLU C  1 147 ? 2.880   -7.758  -19.638 1.00 16.95 ? 146 GLU C O   1 
ATOM   7456  C  CB  . GLU C  1 147 ? 0.890   -7.406  -22.210 1.00 20.86 ? 146 GLU C CB  1 
ATOM   7457  C  CG  . GLU C  1 147 ? 0.903   -6.698  -23.562 1.00 24.44 ? 146 GLU C CG  1 
ATOM   7458  C  CD  . GLU C  1 147 ? -0.449  -6.152  -24.024 1.00 29.40 ? 146 GLU C CD  1 
ATOM   7459  O  OE1 . GLU C  1 147 ? -1.514  -6.648  -23.590 1.00 34.19 ? 146 GLU C OE1 1 
ATOM   7460  O  OE2 . GLU C  1 147 ? -0.428  -5.216  -24.857 1.00 36.36 ? 146 GLU C OE2 1 
ATOM   7461  N  N   . MET C  1 148 ? 1.827   -9.689  -20.135 1.00 16.17 ? 147 MET C N   1 
ATOM   7462  C  CA  . MET C  1 148 ? 1.868   -10.186 -18.756 1.00 16.45 ? 147 MET C CA  1 
ATOM   7463  C  C   . MET C  1 148 ? 3.309   -10.450 -18.319 1.00 15.49 ? 147 MET C C   1 
ATOM   7464  O  O   . MET C  1 148 ? 3.707   -10.093 -17.203 1.00 15.52 ? 147 MET C O   1 
ATOM   7465  C  CB  . MET C  1 148 ? 1.053   -11.463 -18.620 1.00 16.50 ? 147 MET C CB  1 
ATOM   7466  C  CG  . MET C  1 148 ? 1.037   -11.994 -17.212 1.00 17.97 ? 147 MET C CG  1 
ATOM   7467  S  SD  . MET C  1 148 ? -0.231  -13.250 -16.972 1.00 19.59 ? 147 MET C SD  1 
ATOM   7468  C  CE  . MET C  1 148 ? 0.449   -14.633 -17.854 1.00 18.75 ? 147 MET C CE  1 
ATOM   7469  N  N   . ILE C  1 149 ? 4.086   -11.040 -19.207 1.00 15.01 ? 148 ILE C N   1 
ATOM   7470  C  CA  . ILE C  1 149 ? 5.505   -11.276 -18.947 1.00 15.05 ? 148 ILE C CA  1 
ATOM   7471  C  C   . ILE C  1 149 ? 6.243   -9.959  -18.685 1.00 15.83 ? 148 ILE C C   1 
ATOM   7472  O  O   . ILE C  1 149 ? 7.009   -9.864  -17.725 1.00 15.58 ? 148 ILE C O   1 
ATOM   7473  C  CB  . ILE C  1 149 ? 6.157   -12.070 -20.075 1.00 14.61 ? 148 ILE C CB  1 
ATOM   7474  C  CG1 . ILE C  1 149 ? 5.678   -13.518 -20.017 1.00 13.89 ? 148 ILE C CG1 1 
ATOM   7475  C  CG2 . ILE C  1 149 ? 7.676   -12.019 -19.991 1.00 15.21 ? 148 ILE C CG2 1 
ATOM   7476  C  CD1 . ILE C  1 149 ? 5.974   -14.307 -21.266 1.00 13.52 ? 148 ILE C CD1 1 
ATOM   7477  N  N   . GLU C  1 150 ? 6.015   -8.962  -19.540 1.00 16.33 ? 149 GLU C N   1 
ATOM   7478  C  CA  . GLU C  1 150 ? 6.658   -7.654  -19.352 1.00 17.82 ? 149 GLU C CA  1 
ATOM   7479  C  C   . GLU C  1 150 ? 6.274   -7.026  -18.003 1.00 17.92 ? 149 GLU C C   1 
ATOM   7480  O  O   . GLU C  1 150 ? 7.129   -6.473  -17.280 1.00 17.85 ? 149 GLU C O   1 
ATOM   7481  C  CB  . GLU C  1 150 ? 6.334   -6.736  -20.522 1.00 19.28 ? 149 GLU C CB  1 
ATOM   7482  C  CG  . GLU C  1 150 ? 6.924   -7.244  -21.833 1.00 20.82 ? 149 GLU C CG  1 
ATOM   7483  C  CD  . GLU C  1 150 ? 6.713   -6.300  -23.017 1.00 23.68 ? 149 GLU C CD  1 
ATOM   7484  O  OE1 . GLU C  1 150 ? 6.127   -5.218  -22.804 1.00 28.19 ? 149 GLU C OE1 1 
ATOM   7485  O  OE2 . GLU C  1 150 ? 7.187   -6.599  -24.138 1.00 23.52 ? 149 GLU C OE2 1 
ATOM   7486  N  N   A GLU C  1 151 ? 4.995   -7.109  -17.648 0.50 17.37 ? 150 GLU C N   1 
ATOM   7487  N  N   B GLU C  1 151 ? 4.992   -7.114  -17.645 0.50 17.88 ? 150 GLU C N   1 
ATOM   7488  C  CA  A GLU C  1 151 ? 4.535   -6.568  -16.372 0.50 17.62 ? 150 GLU C CA  1 
ATOM   7489  C  CA  B GLU C  1 151 ? 4.538   -6.576  -16.359 0.50 18.40 ? 150 GLU C CA  1 
ATOM   7490  C  C   A GLU C  1 151 ? 5.181   -7.277  -15.173 0.50 16.90 ? 150 GLU C C   1 
ATOM   7491  C  C   B GLU C  1 151 ? 5.181   -7.281  -15.168 0.50 17.31 ? 150 GLU C C   1 
ATOM   7492  O  O   A GLU C  1 151 ? 5.589   -6.624  -14.207 0.50 16.66 ? 150 GLU C O   1 
ATOM   7493  O  O   B GLU C  1 151 ? 5.587   -6.630  -14.207 0.50 17.01 ? 150 GLU C O   1 
ATOM   7494  C  CB  A GLU C  1 151 ? 3.010   -6.697  -16.299 0.50 18.39 ? 150 GLU C CB  1 
ATOM   7495  C  CB  B GLU C  1 151 ? 3.008   -6.644  -16.256 0.50 19.86 ? 150 GLU C CB  1 
ATOM   7496  C  CG  A GLU C  1 151 ? 2.402   -6.362  -14.951 0.50 19.79 ? 150 GLU C CG  1 
ATOM   7497  C  CG  B GLU C  1 151 ? 2.389   -5.593  -17.159 0.50 22.44 ? 150 GLU C CG  1 
ATOM   7498  C  CD  A GLU C  1 151 ? 0.899   -6.549  -14.973 0.50 20.72 ? 150 GLU C CD  1 
ATOM   7499  C  CD  B GLU C  1 151 ? 1.014   -5.114  -16.714 0.50 24.37 ? 150 GLU C CD  1 
ATOM   7500  O  OE1 A GLU C  1 151 ? 0.271   -6.200  -16.036 0.50 22.61 ? 150 GLU C OE1 1 
ATOM   7501  O  OE1 B GLU C  1 151 ? 0.721   -5.112  -15.480 0.50 27.65 ? 150 GLU C OE1 1 
ATOM   7502  O  OE2 A GLU C  1 151 ? 0.379   -7.061  -13.945 0.50 21.39 ? 150 GLU C OE2 1 
ATOM   7503  O  OE2 B GLU C  1 151 ? 0.254   -4.692  -17.606 0.50 25.32 ? 150 GLU C OE2 1 
ATOM   7504  N  N   . MET C  1 152 ? 5.276   -8.609  -15.240 1.00 15.74 ? 151 MET C N   1 
ATOM   7505  C  CA  . MET C  1 152 ? 5.837   -9.370  -14.149 1.00 16.17 ? 151 MET C CA  1 
ATOM   7506  C  C   . MET C  1 152 ? 7.343   -9.048  -13.988 1.00 16.50 ? 151 MET C C   1 
ATOM   7507  O  O   . MET C  1 152 ? 7.842   -8.919  -12.887 1.00 17.18 ? 151 MET C O   1 
ATOM   7508  C  CB  . MET C  1 152 ? 5.627   -10.861 -14.374 1.00 16.02 ? 151 MET C CB  1 
ATOM   7509  C  CG  . MET C  1 152 ? 4.159   -11.276 -14.279 1.00 16.22 ? 151 MET C CG  1 
ATOM   7510  S  SD  . MET C  1 152 ? 3.876   -12.998 -14.694 1.00 17.25 ? 151 MET C SD  1 
ATOM   7511  C  CE  . MET C  1 152 ? 4.361   -13.768 -13.188 1.00 17.00 ? 151 MET C CE  1 
ATOM   7512  N  N   . TYR C  1 153 ? 8.032   -8.897  -15.116 1.00 16.61 ? 152 TYR C N   1 
ATOM   7513  C  CA  . TYR C  1 153 ? 9.438   -8.486  -15.118 1.00 16.78 ? 152 TYR C CA  1 
ATOM   7514  C  C   . TYR C  1 153 ? 9.616   -7.154  -14.377 1.00 17.65 ? 152 TYR C C   1 
ATOM   7515  O  O   . TYR C  1 153 ? 10.518  -6.974  -13.537 1.00 18.16 ? 152 TYR C O   1 
ATOM   7516  C  CB  . TYR C  1 153 ? 9.921   -8.380  -16.561 1.00 16.75 ? 152 TYR C CB  1 
ATOM   7517  C  CG  . TYR C  1 153 ? 11.244  -7.695  -16.753 1.00 18.01 ? 152 TYR C CG  1 
ATOM   7518  C  CD1 . TYR C  1 153 ? 12.431  -8.398  -16.686 1.00 19.02 ? 152 TYR C CD1 1 
ATOM   7519  C  CD2 . TYR C  1 153 ? 11.296  -6.329  -16.991 1.00 18.63 ? 152 TYR C CD2 1 
ATOM   7520  C  CE1 . TYR C  1 153 ? 13.650  -7.753  -16.852 1.00 20.09 ? 152 TYR C CE1 1 
ATOM   7521  C  CE2 . TYR C  1 153 ? 12.488  -5.695  -17.180 1.00 20.37 ? 152 TYR C CE2 1 
ATOM   7522  C  CZ  . TYR C  1 153 ? 13.661  -6.398  -17.106 1.00 20.51 ? 152 TYR C CZ  1 
ATOM   7523  O  OH  . TYR C  1 153 ? 14.831  -5.731  -17.241 1.00 23.31 ? 152 TYR C OH  1 
ATOM   7524  N  N   . GLN C  1 154 ? 8.759   -6.194  -14.691 1.00 18.69 ? 153 GLN C N   1 
ATOM   7525  C  CA  . GLN C  1 154 ? 8.865   -4.891  -14.064 1.00 19.59 ? 153 GLN C CA  1 
ATOM   7526  C  C   . GLN C  1 154 ? 8.483   -4.893  -12.592 1.00 21.76 ? 153 GLN C C   1 
ATOM   7527  O  O   . GLN C  1 154 ? 9.118   -4.191  -11.787 1.00 22.67 ? 153 GLN C O   1 
ATOM   7528  C  CB  . GLN C  1 154 ? 8.020   -3.885  -14.818 1.00 19.68 ? 153 GLN C CB  1 
ATOM   7529  C  CG  . GLN C  1 154 ? 8.593   -3.646  -16.195 1.00 19.93 ? 153 GLN C CG  1 
ATOM   7530  C  CD  . GLN C  1 154 ? 8.135   -2.316  -16.782 1.00 21.06 ? 153 GLN C CD  1 
ATOM   7531  O  OE1 . GLN C  1 154 ? 6.964   -1.960  -16.662 1.00 22.49 ? 153 GLN C OE1 1 
ATOM   7532  N  NE2 . GLN C  1 154 ? 9.059   -1.569  -17.360 1.00 21.10 ? 153 GLN C NE2 1 
ATOM   7533  N  N   . LEU C  1 155 ? 7.413   -5.605  -12.246 1.00 21.56 ? 154 LEU C N   1 
ATOM   7534  C  CA  . LEU C  1 155 ? 6.938   -5.636  -10.870 1.00 23.61 ? 154 LEU C CA  1 
ATOM   7535  C  C   . LEU C  1 155 ? 7.866   -6.379  -9.950  1.00 24.13 ? 154 LEU C C   1 
ATOM   7536  O  O   . LEU C  1 155 ? 8.139   -5.919  -8.840  1.00 24.55 ? 154 LEU C O   1 
ATOM   7537  C  CB  . LEU C  1 155 ? 5.555   -6.275  -10.779 1.00 24.25 ? 154 LEU C CB  1 
ATOM   7538  C  CG  . LEU C  1 155 ? 4.375   -5.451  -11.265 1.00 26.70 ? 154 LEU C CG  1 
ATOM   7539  C  CD1 . LEU C  1 155 ? 3.137   -6.322  -11.347 1.00 27.81 ? 154 LEU C CD1 1 
ATOM   7540  C  CD2 . LEU C  1 155 ? 4.115   -4.265  -10.335 1.00 28.58 ? 154 LEU C CD2 1 
ATOM   7541  N  N   . TYR C  1 156 ? 8.369   -7.523  -10.400 1.00 23.88 ? 155 TYR C N   1 
ATOM   7542  C  CA  . TYR C  1 156 ? 9.100   -8.398  -9.504  1.00 25.16 ? 155 TYR C CA  1 
ATOM   7543  C  C   . TYR C  1 156 ? 10.626  -8.299  -9.712  1.00 27.41 ? 155 TYR C C   1 
ATOM   7544  O  O   . TYR C  1 156 ? 11.362  -8.940  -9.017  1.00 29.70 ? 155 TYR C O   1 
ATOM   7545  C  CB  . TYR C  1 156 ? 8.532   -9.830  -9.559  1.00 24.51 ? 155 TYR C CB  1 
ATOM   7546  C  CG  . TYR C  1 156 ? 7.004   -9.820  -9.439  1.00 23.61 ? 155 TYR C CG  1 
ATOM   7547  C  CD1 . TYR C  1 156 ? 6.364   -9.320  -8.282  1.00 24.14 ? 155 TYR C CD1 1 
ATOM   7548  C  CD2 . TYR C  1 156 ? 6.208   -10.221 -10.487 1.00 22.11 ? 155 TYR C CD2 1 
ATOM   7549  C  CE1 . TYR C  1 156 ? 4.971   -9.257  -8.197  1.00 23.84 ? 155 TYR C CE1 1 
ATOM   7550  C  CE2 . TYR C  1 156 ? 4.815   -10.163 -10.411 1.00 22.22 ? 155 TYR C CE2 1 
ATOM   7551  C  CZ  . TYR C  1 156 ? 4.204   -9.665  -9.264  1.00 23.29 ? 155 TYR C CZ  1 
ATOM   7552  O  OH  . TYR C  1 156 ? 2.819   -9.593  -9.204  1.00 23.42 ? 155 TYR C OH  1 
ATOM   7553  N  N   . GLY C  1 157 ? 11.066  -7.473  -10.659 1.00 27.76 ? 156 GLY C N   1 
ATOM   7554  C  CA  . GLY C  1 157 ? 12.471  -7.077  -10.765 1.00 27.69 ? 156 GLY C CA  1 
ATOM   7555  C  C   . GLY C  1 157 ? 13.394  -8.061  -11.467 1.00 26.34 ? 156 GLY C C   1 
ATOM   7556  O  O   . GLY C  1 157 ? 14.606  -7.998  -11.286 1.00 25.70 ? 156 GLY C O   1 
ATOM   7557  N  N   . GLY C  1 158 ? 12.837  -8.972  -12.263 1.00 22.95 ? 157 GLY C N   1 
ATOM   7558  C  CA  . GLY C  1 158 ? 13.667  -9.796  -13.097 1.00 21.93 ? 157 GLY C CA  1 
ATOM   7559  C  C   . GLY C  1 158 ? 12.902  -10.663 -14.072 1.00 20.39 ? 157 GLY C C   1 
ATOM   7560  O  O   . GLY C  1 158 ? 11.663  -10.721 -14.052 1.00 19.40 ? 157 GLY C O   1 
ATOM   7561  N  N   . PRO C  1 159 ? 13.649  -11.373 -14.929 1.00 19.49 ? 158 PRO C N   1 
ATOM   7562  C  CA  . PRO C  1 159 ? 13.025  -12.153 -15.962 1.00 19.08 ? 158 PRO C CA  1 
ATOM   7563  C  C   . PRO C  1 159 ? 12.261  -13.374 -15.431 1.00 18.84 ? 158 PRO C C   1 
ATOM   7564  O  O   . PRO C  1 159 ? 12.483  -13.825 -14.293 1.00 18.98 ? 158 PRO C O   1 
ATOM   7565  C  CB  . PRO C  1 159 ? 14.197  -12.552 -16.859 1.00 19.47 ? 158 PRO C CB  1 
ATOM   7566  C  CG  . PRO C  1 159 ? 15.418  -12.391 -16.033 1.00 20.55 ? 158 PRO C CG  1 
ATOM   7567  C  CD  . PRO C  1 159 ? 15.120  -11.269 -15.098 1.00 20.50 ? 158 PRO C CD  1 
ATOM   7568  N  N   . VAL C  1 160 ? 11.361  -13.868 -16.268 1.00 18.12 ? 159 VAL C N   1 
ATOM   7569  C  CA  . VAL C  1 160 ? 10.328  -14.834 -15.890 1.00 18.55 ? 159 VAL C CA  1 
ATOM   7570  C  C   . VAL C  1 160 ? 10.733  -16.264 -16.266 1.00 17.20 ? 159 VAL C C   1 
ATOM   7571  O  O   . VAL C  1 160 ? 11.418  -16.472 -17.278 1.00 17.57 ? 159 VAL C O   1 
ATOM   7572  C  CB  . VAL C  1 160 ? 9.024   -14.465 -16.618 1.00 19.25 ? 159 VAL C CB  1 
ATOM   7573  C  CG1 . VAL C  1 160 ? 7.931   -15.497 -16.426 1.00 20.60 ? 159 VAL C CG1 1 
ATOM   7574  C  CG2 . VAL C  1 160 ? 8.553   -13.083 -16.189 1.00 20.85 ? 159 VAL C CG2 1 
ATOM   7575  N  N   . VAL C  1 161 ? 10.314  -17.231 -15.459 1.00 16.17 ? 160 VAL C N   1 
ATOM   7576  C  CA  . VAL C  1 161 ? 10.471  -18.635 -15.801 1.00 15.66 ? 160 VAL C CA  1 
ATOM   7577  C  C   . VAL C  1 161 ? 9.138   -19.134 -16.325 1.00 16.17 ? 160 VAL C C   1 
ATOM   7578  O  O   . VAL C  1 161 ? 8.118   -19.014 -15.638 1.00 16.41 ? 160 VAL C O   1 
ATOM   7579  C  CB  . VAL C  1 161 ? 10.925  -19.479 -14.596 1.00 15.89 ? 160 VAL C CB  1 
ATOM   7580  C  CG1 . VAL C  1 161 ? 10.936  -20.978 -14.957 1.00 15.87 ? 160 VAL C CG1 1 
ATOM   7581  C  CG2 . VAL C  1 161 ? 12.315  -19.033 -14.148 1.00 16.91 ? 160 VAL C CG2 1 
ATOM   7582  N  N   . LEU C  1 162 ? 9.146   -19.672 -17.546 1.00 16.09 ? 161 LEU C N   1 
ATOM   7583  C  CA  . LEU C  1 162 ? 7.973   -20.283 -18.165 1.00 16.10 ? 161 LEU C CA  1 
ATOM   7584  C  C   . LEU C  1 162 ? 7.974   -21.757 -17.829 1.00 15.18 ? 161 LEU C C   1 
ATOM   7585  O  O   . LEU C  1 162 ? 8.987   -22.419 -18.009 1.00 15.11 ? 161 LEU C O   1 
ATOM   7586  C  CB  . LEU C  1 162 ? 8.007   -20.130 -19.688 1.00 17.25 ? 161 LEU C CB  1 
ATOM   7587  C  CG  . LEU C  1 162 ? 8.055   -18.687 -20.199 1.00 19.12 ? 161 LEU C CG  1 
ATOM   7588  C  CD1 . LEU C  1 162 ? 8.295   -18.576 -21.693 1.00 19.05 ? 161 LEU C CD1 1 
ATOM   7589  C  CD2 . LEU C  1 162 ? 6.767   -18.008 -19.835 1.00 21.06 ? 161 LEU C CD2 1 
ATOM   7590  N  N   . VAL C  1 163 ? 6.852   -22.272 -17.338 1.00 13.87 ? 162 VAL C N   1 
ATOM   7591  C  CA  . VAL C  1 163 ? 6.725   -23.710 -17.048 1.00 14.38 ? 162 VAL C CA  1 
ATOM   7592  C  C   . VAL C  1 163 ? 5.542   -24.209 -17.848 1.00 14.33 ? 162 VAL C C   1 
ATOM   7593  O  O   . VAL C  1 163 ? 4.414   -23.731 -17.616 1.00 15.03 ? 162 VAL C O   1 
ATOM   7594  C  CB  . VAL C  1 163 ? 6.499   -23.964 -15.547 1.00 15.19 ? 162 VAL C CB  1 
ATOM   7595  C  CG1 . VAL C  1 163 ? 6.414   -25.465 -15.269 1.00 15.71 ? 162 VAL C CG1 1 
ATOM   7596  C  CG2 . VAL C  1 163 ? 7.636   -23.347 -14.713 1.00 15.43 ? 162 VAL C CG2 1 
ATOM   7597  N  N   . ALA C  1 164 ? 5.751   -25.144 -18.786 1.00 13.72 ? 163 ALA C N   1 
ATOM   7598  C  CA  . ALA C  1 164 ? 4.678   -25.601 -19.665 1.00 13.70 ? 163 ALA C CA  1 
ATOM   7599  C  C   . ALA C  1 164 ? 4.548   -27.118 -19.661 1.00 13.66 ? 163 ALA C C   1 
ATOM   7600  O  O   . ALA C  1 164 ? 5.538   -27.829 -19.491 1.00 14.02 ? 163 ALA C O   1 
ATOM   7601  C  CB  . ALA C  1 164 ? 4.895   -25.116 -21.087 1.00 13.52 ? 163 ALA C CB  1 
ATOM   7602  N  N   . HIS C  1 165 ? 3.312   -27.594 -19.802 1.00 13.74 ? 164 HIS C N   1 
ATOM   7603  C  CA  . HIS C  1 165 ? 3.053   -29.032 -19.825 1.00 14.23 ? 164 HIS C CA  1 
ATOM   7604  C  C   . HIS C  1 165 ? 2.449   -29.398 -21.175 1.00 14.12 ? 164 HIS C C   1 
ATOM   7605  O  O   . HIS C  1 165 ? 1.550   -28.721 -21.679 1.00 13.50 ? 164 HIS C O   1 
ATOM   7606  C  CB  . HIS C  1 165 ? 2.103   -29.436 -18.720 1.00 14.82 ? 164 HIS C CB  1 
ATOM   7607  C  CG  . HIS C  1 165 ? 1.785   -30.896 -18.703 1.00 15.59 ? 164 HIS C CG  1 
ATOM   7608  N  ND1 . HIS C  1 165 ? 0.509   -31.378 -18.887 1.00 16.47 ? 164 HIS C ND1 1 
ATOM   7609  C  CD2 . HIS C  1 165 ? 2.581   -31.979 -18.528 1.00 16.22 ? 164 HIS C CD2 1 
ATOM   7610  C  CE1 . HIS C  1 165 ? 0.528   -32.698 -18.817 1.00 17.34 ? 164 HIS C CE1 1 
ATOM   7611  N  NE2 . HIS C  1 165 ? 1.775   -33.087 -18.595 1.00 17.74 ? 164 HIS C NE2 1 
ATOM   7612  N  N   . SER C  1 166 ? 2.932   -30.521 -21.707 1.00 14.82 ? 165 SER C N   1 
ATOM   7613  C  CA  . SER C  1 166 ? 2.343   -31.164 -22.861 1.00 15.81 ? 165 SER C CA  1 
ATOM   7614  C  C   . SER C  1 166 ? 2.227   -30.189 -24.034 1.00 15.27 ? 165 SER C C   1 
ATOM   7615  O  O   . SER C  1 166 ? 3.211   -29.515 -24.357 1.00 15.20 ? 165 SER C O   1 
ATOM   7616  C  CB  . SER C  1 166 ? 1.029   -31.819 -22.444 1.00 17.52 ? 165 SER C CB  1 
ATOM   7617  O  OG  . SER C  1 166 ? 0.648   -32.791 -23.395 1.00 19.76 ? 165 SER C OG  1 
ATOM   7618  N  N   . MET C  1 167 ? 1.046   -30.047 -24.645 1.00 14.60 ? 166 MET C N   1 
ATOM   7619  C  CA  . MET C  1 167 ? 0.871   -29.132 -25.771 1.00 15.87 ? 166 MET C CA  1 
ATOM   7620  C  C   . MET C  1 167 ? 1.192   -27.662 -25.447 1.00 14.13 ? 166 MET C C   1 
ATOM   7621  O  O   . MET C  1 167 ? 1.533   -26.901 -26.331 1.00 13.83 ? 166 MET C O   1 
ATOM   7622  C  CB  . MET C  1 167 ? -0.583  -29.185 -26.272 1.00 17.24 ? 166 MET C CB  1 
ATOM   7623  C  CG  . MET C  1 167 ? -0.841  -28.326 -27.467 1.00 19.16 ? 166 MET C CG  1 
ATOM   7624  S  SD  . MET C  1 167 ? -2.529  -28.616 -28.086 1.00 20.10 ? 166 MET C SD  1 
ATOM   7625  C  CE  . MET C  1 167 ? -3.488  -27.485 -27.112 1.00 20.17 ? 166 MET C CE  1 
ATOM   7626  N  N   . GLY C  1 168 ? 1.135   -27.296 -24.167 1.00 13.64 ? 167 GLY C N   1 
ATOM   7627  C  CA  . GLY C  1 168 ? 1.552   -25.948 -23.772 1.00 13.46 ? 167 GLY C CA  1 
ATOM   7628  C  C   . GLY C  1 168 ? 2.975   -25.644 -24.199 1.00 13.79 ? 167 GLY C C   1 
ATOM   7629  O  O   . GLY C  1 168 ? 3.343   -24.495 -24.406 1.00 14.62 ? 167 GLY C O   1 
ATOM   7630  N  N   . ASN C  1 169 ? 3.816   -26.673 -24.297 1.00 14.14 ? 168 ASN C N   1 
ATOM   7631  C  CA  . ASN C  1 169 ? 5.186   -26.465 -24.798 1.00 14.47 ? 168 ASN C CA  1 
ATOM   7632  C  C   . ASN C  1 169 ? 5.257   -26.010 -26.252 1.00 14.97 ? 168 ASN C C   1 
ATOM   7633  O  O   . ASN C  1 169 ? 6.108   -25.209 -26.614 1.00 14.52 ? 168 ASN C O   1 
ATOM   7634  C  CB  . ASN C  1 169 ? 5.978   -27.743 -24.636 1.00 15.14 ? 168 ASN C CB  1 
ATOM   7635  C  CG  . ASN C  1 169 ? 6.260   -28.042 -23.188 1.00 15.64 ? 168 ASN C CG  1 
ATOM   7636  O  OD1 . ASN C  1 169 ? 7.084   -27.400 -22.587 1.00 17.09 ? 168 ASN C OD1 1 
ATOM   7637  N  ND2 . ASN C  1 169 ? 5.555   -29.000 -22.624 1.00 16.13 ? 168 ASN C ND2 1 
ATOM   7638  N  N   . MET C  1 170 ? 4.361   -26.526 -27.081 1.00 15.86 ? 169 MET C N   1 
ATOM   7639  C  CA  . MET C  1 170 ? 4.300   -26.154 -28.486 1.00 16.27 ? 169 MET C CA  1 
ATOM   7640  C  C   . MET C  1 170 ? 3.720   -24.728 -28.631 1.00 15.44 ? 169 MET C C   1 
ATOM   7641  O  O   . MET C  1 170 ? 4.208   -23.955 -29.461 1.00 15.23 ? 169 MET C O   1 
ATOM   7642  C  CB  . MET C  1 170 ? 3.529   -27.217 -29.264 1.00 18.78 ? 169 MET C CB  1 
ATOM   7643  C  CG  . MET C  1 170 ? 4.317   -28.534 -29.409 1.00 21.63 ? 169 MET C CG  1 
ATOM   7644  S  SD  . MET C  1 170 ? 5.573   -28.342 -30.695 1.00 26.75 ? 169 MET C SD  1 
ATOM   7645  C  CE  . MET C  1 170 ? 4.589   -28.530 -32.188 1.00 26.63 ? 169 MET C CE  1 
ATOM   7646  N  N   . TYR C  1 171 ? 2.716   -24.374 -27.832 1.00 14.53 ? 170 TYR C N   1 
ATOM   7647  C  CA  . TYR C  1 171 ? 2.267   -22.964 -27.718 1.00 14.86 ? 170 TYR C CA  1 
ATOM   7648  C  C   . TYR C  1 171 ? 3.424   -22.029 -27.327 1.00 14.99 ? 170 TYR C C   1 
ATOM   7649  O  O   . TYR C  1 171 ? 3.611   -20.972 -27.924 1.00 14.64 ? 170 TYR C O   1 
ATOM   7650  C  CB  . TYR C  1 171 ? 1.113   -22.832 -26.713 1.00 15.18 ? 170 TYR C CB  1 
ATOM   7651  C  CG  . TYR C  1 171 ? -0.226  -22.799 -27.414 1.00 14.99 ? 170 TYR C CG  1 
ATOM   7652  C  CD1 . TYR C  1 171 ? -0.750  -23.942 -28.011 1.00 14.76 ? 170 TYR C CD1 1 
ATOM   7653  C  CD2 . TYR C  1 171 ? -0.934  -21.641 -27.496 1.00 14.97 ? 170 TYR C CD2 1 
ATOM   7654  C  CE1 . TYR C  1 171 ? -1.955  -23.901 -28.691 1.00 14.33 ? 170 TYR C CE1 1 
ATOM   7655  C  CE2 . TYR C  1 171 ? -2.134  -21.591 -28.161 1.00 15.49 ? 170 TYR C CE2 1 
ATOM   7656  C  CZ  . TYR C  1 171 ? -2.637  -22.725 -28.756 1.00 15.10 ? 170 TYR C CZ  1 
ATOM   7657  O  OH  . TYR C  1 171 ? -3.825  -22.596 -29.426 1.00 15.29 ? 170 TYR C OH  1 
ATOM   7658  N  N   . THR C  1 172 ? 4.187   -22.423 -26.320 1.00 15.02 ? 171 THR C N   1 
ATOM   7659  C  CA  . THR C  1 172 ? 5.305   -21.621 -25.831 1.00 15.01 ? 171 THR C CA  1 
ATOM   7660  C  C   . THR C  1 172 ? 6.417   -21.500 -26.870 1.00 15.79 ? 171 THR C C   1 
ATOM   7661  O  O   . THR C  1 172 ? 6.970   -20.400 -27.079 1.00 15.36 ? 171 THR C O   1 
ATOM   7662  C  CB  . THR C  1 172 ? 5.832   -22.168 -24.489 1.00 15.89 ? 171 THR C CB  1 
ATOM   7663  O  OG1 . THR C  1 172 ? 4.761   -22.222 -23.531 1.00 16.25 ? 171 THR C OG1 1 
ATOM   7664  C  CG2 . THR C  1 172 ? 6.958   -21.323 -23.931 1.00 16.92 ? 171 THR C CG2 1 
ATOM   7665  N  N   . LEU C  1 173 ? 6.753   -22.609 -27.545 1.00 15.88 ? 172 LEU C N   1 
ATOM   7666  C  CA  . LEU C  1 173 ? 7.748   -22.554 -28.617 1.00 16.19 ? 172 LEU C CA  1 
ATOM   7667  C  C   . LEU C  1 173 ? 7.317   -21.618 -29.765 1.00 16.62 ? 172 LEU C C   1 
ATOM   7668  O  O   . LEU C  1 173 ? 8.108   -20.804 -30.274 1.00 16.41 ? 172 LEU C O   1 
ATOM   7669  C  CB  . LEU C  1 173 ? 8.057   -23.946 -29.146 1.00 16.46 ? 172 LEU C CB  1 
ATOM   7670  C  CG  . LEU C  1 173 ? 9.086   -24.020 -30.291 1.00 17.86 ? 172 LEU C CG  1 
ATOM   7671  C  CD1 . LEU C  1 173 ? 10.430  -23.472 -29.870 1.00 18.84 ? 172 LEU C CD1 1 
ATOM   7672  C  CD2 . LEU C  1 173 ? 9.198   -25.467 -30.769 1.00 18.21 ? 172 LEU C CD2 1 
ATOM   7673  N  N   . TYR C  1 174 ? 6.056   -21.731 -30.172 1.00 15.99 ? 173 TYR C N   1 
ATOM   7674  C  CA  . TYR C  1 174 ? 5.524   -20.835 -31.180 1.00 16.57 ? 173 TYR C CA  1 
ATOM   7675  C  C   . TYR C  1 174 ? 5.723   -19.389 -30.749 1.00 16.08 ? 173 TYR C C   1 
ATOM   7676  O  O   . TYR C  1 174 ? 6.221   -18.543 -31.536 1.00 17.51 ? 173 TYR C O   1 
ATOM   7677  C  CB  . TYR C  1 174 ? 4.041   -21.110 -31.393 1.00 16.67 ? 173 TYR C CB  1 
ATOM   7678  C  CG  . TYR C  1 174 ? 3.351   -20.126 -32.321 1.00 17.81 ? 173 TYR C CG  1 
ATOM   7679  C  CD1 . TYR C  1 174 ? 3.269   -20.377 -33.695 1.00 19.33 ? 173 TYR C CD1 1 
ATOM   7680  C  CD2 . TYR C  1 174 ? 2.716   -18.996 -31.823 1.00 18.83 ? 173 TYR C CD2 1 
ATOM   7681  C  CE1 . TYR C  1 174 ? 2.595   -19.517 -34.536 1.00 20.37 ? 173 TYR C CE1 1 
ATOM   7682  C  CE2 . TYR C  1 174 ? 2.058   -18.119 -32.660 1.00 19.42 ? 173 TYR C CE2 1 
ATOM   7683  C  CZ  . TYR C  1 174 ? 1.999   -18.388 -34.013 1.00 20.96 ? 173 TYR C CZ  1 
ATOM   7684  O  OH  . TYR C  1 174 ? 1.326   -17.518 -34.845 1.00 22.74 ? 173 TYR C OH  1 
ATOM   7685  N  N   . PHE C  1 175 ? 5.335   -19.092 -29.521 1.00 15.53 ? 174 PHE C N   1 
ATOM   7686  C  CA  . PHE C  1 175 ? 5.482   -17.725 -28.986 1.00 15.17 ? 174 PHE C CA  1 
ATOM   7687  C  C   . PHE C  1 175 ? 6.946   -17.256 -29.060 1.00 15.80 ? 174 PHE C C   1 
ATOM   7688  O  O   . PHE C  1 175 ? 7.239   -16.166 -29.569 1.00 16.53 ? 174 PHE C O   1 
ATOM   7689  C  CB  . PHE C  1 175 ? 4.969   -17.685 -27.554 1.00 15.49 ? 174 PHE C CB  1 
ATOM   7690  C  CG  . PHE C  1 175 ? 5.204   -16.384 -26.846 1.00 15.65 ? 174 PHE C CG  1 
ATOM   7691  C  CD1 . PHE C  1 175 ? 4.464   -15.256 -27.175 1.00 16.23 ? 174 PHE C CD1 1 
ATOM   7692  C  CD2 . PHE C  1 175 ? 6.133   -16.299 -25.822 1.00 15.64 ? 174 PHE C CD2 1 
ATOM   7693  C  CE1 . PHE C  1 175 ? 4.708   -14.043 -26.521 1.00 16.76 ? 174 PHE C CE1 1 
ATOM   7694  C  CE2 . PHE C  1 175 ? 6.351   -15.101 -25.141 1.00 16.10 ? 174 PHE C CE2 1 
ATOM   7695  C  CZ  . PHE C  1 175 ? 5.644   -13.984 -25.505 1.00 16.56 ? 174 PHE C CZ  1 
ATOM   7696  N  N   . LEU C  1 176 ? 7.844   -18.063 -28.519 1.00 15.39 ? 175 LEU C N   1 
ATOM   7697  C  CA  . LEU C  1 176 ? 9.252   -17.692 -28.426 1.00 16.93 ? 175 LEU C CA  1 
ATOM   7698  C  C   . LEU C  1 176 ? 9.917   -17.557 -29.793 1.00 17.94 ? 175 LEU C C   1 
ATOM   7699  O  O   . LEU C  1 176 ? 10.766  -16.675 -29.998 1.00 19.01 ? 175 LEU C O   1 
ATOM   7700  C  CB  . LEU C  1 176 ? 10.001  -18.675 -27.530 1.00 16.69 ? 175 LEU C CB  1 
ATOM   7701  C  CG  . LEU C  1 176 ? 9.620   -18.664 -26.052 1.00 16.36 ? 175 LEU C CG  1 
ATOM   7702  C  CD1 . LEU C  1 176 ? 10.334  -19.786 -25.327 1.00 16.78 ? 175 LEU C CD1 1 
ATOM   7703  C  CD2 . LEU C  1 176 ? 9.951   -17.330 -25.374 1.00 17.14 ? 175 LEU C CD2 1 
ATOM   7704  N  N   . GLN C  1 177 ? 9.570   -18.431 -30.736 1.00 18.86 ? 176 GLN C N   1 
ATOM   7705  C  CA  . GLN C  1 177 ? 10.106  -18.329 -32.110 1.00 20.24 ? 176 GLN C CA  1 
ATOM   7706  C  C   . GLN C  1 177 ? 9.751   -16.985 -32.773 1.00 21.44 ? 176 GLN C C   1 
ATOM   7707  O  O   . GLN C  1 177 ? 10.494  -16.497 -33.608 1.00 22.67 ? 176 GLN C O   1 
ATOM   7708  C  CB  . GLN C  1 177 ? 9.605   -19.479 -32.986 1.00 20.36 ? 176 GLN C CB  1 
ATOM   7709  C  CG  . GLN C  1 177 ? 10.267  -20.800 -32.662 1.00 20.64 ? 176 GLN C CG  1 
ATOM   7710  C  CD  . GLN C  1 177 ? 9.805   -21.915 -33.581 1.00 21.55 ? 176 GLN C CD  1 
ATOM   7711  O  OE1 . GLN C  1 177 ? 8.770   -21.811 -34.242 1.00 22.81 ? 176 GLN C OE1 1 
ATOM   7712  N  NE2 . GLN C  1 177 ? 10.559  -23.008 -33.611 1.00 22.29 ? 176 GLN C NE2 1 
ATOM   7713  N  N   . ARG C  1 178 ? 8.644   -16.390 -32.363 1.00 21.05 ? 177 ARG C N   1 
ATOM   7714  C  CA  . ARG C  1 178 ? 8.181   -15.130 -32.927 1.00 23.36 ? 177 ARG C CA  1 
ATOM   7715  C  C   . ARG C  1 178 ? 8.545   -13.892 -32.140 1.00 22.82 ? 177 ARG C C   1 
ATOM   7716  O  O   . ARG C  1 178 ? 8.162   -12.801 -32.541 1.00 23.36 ? 177 ARG C O   1 
ATOM   7717  C  CB  . ARG C  1 178 ? 6.686   -15.204 -33.163 1.00 25.45 ? 177 ARG C CB  1 
ATOM   7718  C  CG  . ARG C  1 178 ? 6.459   -16.150 -34.324 1.00 29.30 ? 177 ARG C CG  1 
ATOM   7719  C  CD  . ARG C  1 178 ? 5.052   -16.634 -34.473 1.00 32.77 ? 177 ARG C CD  1 
ATOM   7720  N  NE  . ARG C  1 178 ? 5.103   -17.813 -35.352 1.00 38.39 ? 177 ARG C NE  1 
ATOM   7721  C  CZ  . ARG C  1 178 ? 4.706   -17.874 -36.620 1.00 42.86 ? 177 ARG C CZ  1 
ATOM   7722  N  NH1 . ARG C  1 178 ? 4.176   -16.809 -37.237 1.00 46.20 ? 177 ARG C NH1 1 
ATOM   7723  N  NH2 . ARG C  1 178 ? 4.818   -19.038 -37.271 1.00 42.65 ? 177 ARG C NH2 1 
ATOM   7724  N  N   . GLN C  1 179 ? 9.310   -14.022 -31.057 1.00 21.14 ? 178 GLN C N   1 
ATOM   7725  C  CA  . GLN C  1 179 ? 9.793   -12.839 -30.345 1.00 21.20 ? 178 GLN C CA  1 
ATOM   7726  C  C   . GLN C  1 179 ? 11.246  -12.618 -30.730 1.00 21.78 ? 178 GLN C C   1 
ATOM   7727  O  O   . GLN C  1 179 ? 11.994  -13.568 -30.843 1.00 20.75 ? 178 GLN C O   1 
ATOM   7728  C  CB  . GLN C  1 179 ? 9.700   -12.991 -28.812 1.00 21.37 ? 178 GLN C CB  1 
ATOM   7729  C  CG  . GLN C  1 179 ? 8.323   -13.352 -28.256 1.00 21.63 ? 178 GLN C CG  1 
ATOM   7730  C  CD  . GLN C  1 179 ? 7.203   -12.602 -28.960 1.00 24.09 ? 178 GLN C CD  1 
ATOM   7731  O  OE1 . GLN C  1 179 ? 7.158   -11.384 -28.928 1.00 26.03 ? 178 GLN C OE1 1 
ATOM   7732  N  NE2 . GLN C  1 179 ? 6.294   -13.327 -29.584 1.00 26.15 ? 178 GLN C NE2 1 
ATOM   7733  N  N   . PRO C  1 180 ? 11.656  -11.352 -30.905 1.00 21.81 ? 179 PRO C N   1 
ATOM   7734  C  CA  . PRO C  1 180 ? 13.058  -11.052 -31.173 1.00 22.43 ? 179 PRO C CA  1 
ATOM   7735  C  C   . PRO C  1 180 ? 13.972  -11.592 -30.076 1.00 22.32 ? 179 PRO C C   1 
ATOM   7736  O  O   . PRO C  1 180 ? 13.599  -11.646 -28.904 1.00 21.16 ? 179 PRO C O   1 
ATOM   7737  C  CB  . PRO C  1 180 ? 13.097  -9.518  -31.173 1.00 23.11 ? 179 PRO C CB  1 
ATOM   7738  C  CG  . PRO C  1 180 ? 11.703  -9.104  -31.510 1.00 22.95 ? 179 PRO C CG  1 
ATOM   7739  C  CD  . PRO C  1 180 ? 10.825  -10.135 -30.866 1.00 21.98 ? 179 PRO C CD  1 
ATOM   7740  N  N   . GLN C  1 181 ? 15.180  -11.971 -30.462 1.00 23.32 ? 180 GLN C N   1 
ATOM   7741  C  CA  . GLN C  1 181 ? 16.150  -12.496 -29.511 1.00 23.98 ? 180 GLN C CA  1 
ATOM   7742  C  C   . GLN C  1 181 ? 16.421  -11.513 -28.376 1.00 22.96 ? 180 GLN C C   1 
ATOM   7743  O  O   . GLN C  1 181 ? 16.548  -11.916 -27.230 1.00 22.35 ? 180 GLN C O   1 
ATOM   7744  C  CB  . GLN C  1 181 ? 17.466  -12.877 -30.230 1.00 25.80 ? 180 GLN C CB  1 
ATOM   7745  C  CG  . GLN C  1 181 ? 18.467  -13.581 -29.330 1.00 26.81 ? 180 GLN C CG  1 
ATOM   7746  C  CD  . GLN C  1 181 ? 17.959  -14.937 -28.867 1.00 26.87 ? 180 GLN C CD  1 
ATOM   7747  O  OE1 . GLN C  1 181 ? 17.522  -15.743 -29.670 1.00 30.37 ? 180 GLN C OE1 1 
ATOM   7748  N  NE2 . GLN C  1 181 ? 18.003  -15.188 -27.571 1.00 26.74 ? 180 GLN C NE2 1 
ATOM   7749  N  N   . ALA C  1 182 ? 16.499  -10.217 -28.675 1.00 23.28 ? 181 ALA C N   1 
ATOM   7750  C  CA  . ALA C  1 182 ? 16.733  -9.204  -27.630 1.00 22.86 ? 181 ALA C CA  1 
ATOM   7751  C  C   . ALA C  1 182 ? 15.607  -9.178  -26.593 1.00 21.35 ? 181 ALA C C   1 
ATOM   7752  O  O   . ALA C  1 182 ? 15.850  -8.955  -25.417 1.00 20.01 ? 181 ALA C O   1 
ATOM   7753  C  CB  . ALA C  1 182 ? 16.923  -7.814  -28.238 1.00 23.95 ? 181 ALA C CB  1 
ATOM   7754  N  N   . TRP C  1 183 ? 14.378  -9.432  -27.038 1.00 20.56 ? 182 TRP C N   1 
ATOM   7755  C  CA  . TRP C  1 183 ? 13.236  -9.481  -26.136 1.00 19.29 ? 182 TRP C CA  1 
ATOM   7756  C  C   . TRP C  1 183 ? 13.392  -10.677 -25.194 1.00 18.76 ? 182 TRP C C   1 
ATOM   7757  O  O   . TRP C  1 183 ? 13.217  -10.560 -23.981 1.00 18.39 ? 182 TRP C O   1 
ATOM   7758  C  CB  . TRP C  1 183 ? 11.923  -9.577  -26.930 1.00 19.14 ? 182 TRP C CB  1 
ATOM   7759  C  CG  . TRP C  1 183 ? 10.682  -9.495  -26.045 1.00 18.66 ? 182 TRP C CG  1 
ATOM   7760  C  CD1 . TRP C  1 183 ? 9.979   -8.365  -25.729 1.00 18.55 ? 182 TRP C CD1 1 
ATOM   7761  C  CD2 . TRP C  1 183 ? 10.049  -10.569 -25.347 1.00 18.12 ? 182 TRP C CD2 1 
ATOM   7762  N  NE1 . TRP C  1 183 ? 8.943   -8.674  -24.885 1.00 18.09 ? 182 TRP C NE1 1 
ATOM   7763  C  CE2 . TRP C  1 183 ? 8.962   -10.020 -24.632 1.00 17.77 ? 182 TRP C CE2 1 
ATOM   7764  C  CE3 . TRP C  1 183 ? 10.275  -11.946 -25.278 1.00 17.63 ? 182 TRP C CE3 1 
ATOM   7765  C  CZ2 . TRP C  1 183 ? 8.131   -10.787 -23.830 1.00 17.15 ? 182 TRP C CZ2 1 
ATOM   7766  C  CZ3 . TRP C  1 183 ? 9.438   -12.716 -24.477 1.00 17.40 ? 182 TRP C CZ3 1 
ATOM   7767  C  CH2 . TRP C  1 183 ? 8.376   -12.129 -23.759 1.00 17.03 ? 182 TRP C CH2 1 
ATOM   7768  N  N   . LYS C  1 184 ? 13.730  -11.830 -25.756 1.00 18.75 ? 183 LYS C N   1 
ATOM   7769  C  CA  . LYS C  1 184 ? 13.858  -13.041 -24.952 1.00 18.02 ? 183 LYS C CA  1 
ATOM   7770  C  C   . LYS C  1 184 ? 15.016  -12.957 -23.955 1.00 18.79 ? 183 LYS C C   1 
ATOM   7771  O  O   . LYS C  1 184 ? 14.888  -13.373 -22.790 1.00 18.14 ? 183 LYS C O   1 
ATOM   7772  C  CB  . LYS C  1 184 ? 14.007  -14.253 -25.861 1.00 17.68 ? 183 LYS C CB  1 
ATOM   7773  C  CG  . LYS C  1 184 ? 12.737  -14.539 -26.652 1.00 17.54 ? 183 LYS C CG  1 
ATOM   7774  C  CD  . LYS C  1 184 ? 12.843  -15.763 -27.547 1.00 17.67 ? 183 LYS C CD  1 
ATOM   7775  C  CE  . LYS C  1 184 ? 13.807  -15.570 -28.697 1.00 18.19 ? 183 LYS C CE  1 
ATOM   7776  N  NZ  . LYS C  1 184 ? 13.588  -16.613 -29.729 1.00 18.18 ? 183 LYS C NZ  1 
ATOM   7777  N  N   . ASP C  1 185 ? 16.117  -12.344 -24.393 1.00 20.19 ? 184 ASP C N   1 
ATOM   7778  C  CA  . ASP C  1 185 ? 17.268  -12.123 -23.521 1.00 22.01 ? 184 ASP C CA  1 
ATOM   7779  C  C   . ASP C  1 185 ? 16.932  -11.241 -22.326 1.00 21.97 ? 184 ASP C C   1 
ATOM   7780  O  O   . ASP C  1 185 ? 17.464  -11.431 -21.234 1.00 22.17 ? 184 ASP C O   1 
ATOM   7781  C  CB  . ASP C  1 185 ? 18.452  -11.498 -24.282 1.00 24.02 ? 184 ASP C CB  1 
ATOM   7782  C  CG  . ASP C  1 185 ? 19.064  -12.435 -25.303 1.00 26.33 ? 184 ASP C CG  1 
ATOM   7783  O  OD1 . ASP C  1 185 ? 18.777  -13.652 -25.292 1.00 27.04 ? 184 ASP C OD1 1 
ATOM   7784  O  OD2 . ASP C  1 185 ? 19.849  -11.939 -26.146 1.00 29.17 ? 184 ASP C OD2 1 
ATOM   7785  N  N   . LYS C  1 186 ? 16.047  -10.272 -22.520 1.00 20.47 ? 185 LYS C N   1 
ATOM   7786  C  CA  . LYS C  1 186 ? 15.647  -9.409  -21.425 1.00 20.53 ? 185 LYS C CA  1 
ATOM   7787  C  C   . LYS C  1 186 ? 14.607  -10.052 -20.489 1.00 18.65 ? 185 LYS C C   1 
ATOM   7788  O  O   . LYS C  1 186 ? 14.741  -9.984  -19.268 1.00 18.37 ? 185 LYS C O   1 
ATOM   7789  C  CB  . LYS C  1 186 ? 15.071  -8.105  -21.999 1.00 20.97 ? 185 LYS C CB  1 
ATOM   7790  C  CG  . LYS C  1 186 ? 14.533  -7.146  -20.955 1.00 21.74 ? 185 LYS C CG  1 
ATOM   7791  C  CD  . LYS C  1 186 ? 14.265  -5.780  -21.590 1.00 22.68 ? 185 LYS C CD  1 
ATOM   7792  C  CE  . LYS C  1 186 ? 13.730  -4.790  -20.581 1.00 23.17 ? 185 LYS C CE  1 
ATOM   7793  N  NZ  . LYS C  1 186 ? 13.315  -3.543  -21.272 1.00 23.82 ? 185 LYS C NZ  1 
ATOM   7794  N  N   . TYR C  1 187 ? 13.572  -10.654 -21.073 1.00 18.34 ? 186 TYR C N   1 
ATOM   7795  C  CA  . TYR C  1 187 ? 12.375  -10.988 -20.308 1.00 17.50 ? 186 TYR C CA  1 
ATOM   7796  C  C   . TYR C  1 187 ? 12.258  -12.430 -19.827 1.00 17.09 ? 186 TYR C C   1 
ATOM   7797  O  O   . TYR C  1 187 ? 11.432  -12.702 -18.942 1.00 17.57 ? 186 TYR C O   1 
ATOM   7798  C  CB  . TYR C  1 187 ? 11.115  -10.625 -21.101 1.00 16.89 ? 186 TYR C CB  1 
ATOM   7799  C  CG  . TYR C  1 187 ? 10.906  -9.151  -21.255 1.00 17.16 ? 186 TYR C CG  1 
ATOM   7800  C  CD1 . TYR C  1 187 ? 10.518  -8.363  -20.174 1.00 17.44 ? 186 TYR C CD1 1 
ATOM   7801  C  CD2 . TYR C  1 187 ? 11.131  -8.523  -22.487 1.00 17.75 ? 186 TYR C CD2 1 
ATOM   7802  C  CE1 . TYR C  1 187 ? 10.368  -6.991  -20.313 1.00 17.56 ? 186 TYR C CE1 1 
ATOM   7803  C  CE2 . TYR C  1 187 ? 10.973  -7.147  -22.632 1.00 17.92 ? 186 TYR C CE2 1 
ATOM   7804  C  CZ  . TYR C  1 187 ? 10.573  -6.397  -21.557 1.00 17.84 ? 186 TYR C CZ  1 
ATOM   7805  O  OH  . TYR C  1 187 ? 10.404  -5.031  -21.762 1.00 19.01 ? 186 TYR C OH  1 
ATOM   7806  N  N   . ILE C  1 188 ? 13.006  -13.351 -20.423 1.00 17.15 ? 187 ILE C N   1 
ATOM   7807  C  CA  . ILE C  1 188 ? 12.846  -14.780 -20.111 1.00 17.17 ? 187 ILE C CA  1 
ATOM   7808  C  C   . ILE C  1 188 ? 14.081  -15.297 -19.391 1.00 18.23 ? 187 ILE C C   1 
ATOM   7809  O  O   . ILE C  1 188 ? 15.187  -15.155 -19.905 1.00 18.79 ? 187 ILE C O   1 
ATOM   7810  C  CB  . ILE C  1 188 ? 12.590  -15.629 -21.378 1.00 17.07 ? 187 ILE C CB  1 
ATOM   7811  C  CG1 . ILE C  1 188 ? 11.390  -15.101 -22.187 1.00 16.96 ? 187 ILE C CG1 1 
ATOM   7812  C  CG2 . ILE C  1 188 ? 12.386  -17.108 -21.023 1.00 16.88 ? 187 ILE C CG2 1 
ATOM   7813  C  CD1 . ILE C  1 188 ? 10.074  -15.083 -21.445 1.00 16.83 ? 187 ILE C CD1 1 
ATOM   7814  N  N   . ARG C  1 189 ? 13.887  -15.836 -18.183 1.00 19.03 ? 188 ARG C N   1 
ATOM   7815  C  CA  . ARG C  1 189 ? 14.971  -16.429 -17.421 1.00 20.46 ? 188 ARG C CA  1 
ATOM   7816  C  C   . ARG C  1 189 ? 15.227  -17.857 -17.888 1.00 19.33 ? 188 ARG C C   1 
ATOM   7817  O  O   . ARG C  1 189 ? 16.362  -18.242 -18.133 1.00 19.02 ? 188 ARG C O   1 
ATOM   7818  C  CB  . ARG C  1 189 ? 14.665  -16.417 -15.937 1.00 22.36 ? 188 ARG C CB  1 
ATOM   7819  C  CG  . ARG C  1 189 ? 15.809  -16.955 -15.093 1.00 26.77 ? 188 ARG C CG  1 
ATOM   7820  C  CD  . ARG C  1 189 ? 15.497  -16.783 -13.618 1.00 31.37 ? 188 ARG C CD  1 
ATOM   7821  N  NE  . ARG C  1 189 ? 16.699  -16.917 -12.821 1.00 40.41 ? 188 ARG C NE  1 
ATOM   7822  C  CZ  . ARG C  1 189 ? 17.539  -15.922 -12.535 1.00 47.96 ? 188 ARG C CZ  1 
ATOM   7823  N  NH1 . ARG C  1 189 ? 17.298  -14.662 -12.934 1.00 51.71 ? 188 ARG C NH1 1 
ATOM   7824  N  NH2 . ARG C  1 189 ? 18.636  -16.192 -11.833 1.00 51.72 ? 188 ARG C NH2 1 
ATOM   7825  N  N   . ALA C  1 190 ? 14.157  -18.635 -18.004 1.00 17.74 ? 189 ALA C N   1 
ATOM   7826  C  CA  . ALA C  1 190 ? 14.280  -20.029 -18.419 1.00 17.91 ? 189 ALA C CA  1 
ATOM   7827  C  C   . ALA C  1 190 ? 12.931  -20.544 -18.836 1.00 16.76 ? 189 ALA C C   1 
ATOM   7828  O  O   . ALA C  1 190 ? 11.903  -19.922 -18.547 1.00 16.31 ? 189 ALA C O   1 
ATOM   7829  C  CB  . ALA C  1 190 ? 14.831  -20.863 -17.283 1.00 18.49 ? 189 ALA C CB  1 
ATOM   7830  N  N   . PHE C  1 191 ? 12.947  -21.648 -19.575 1.00 16.84 ? 190 PHE C N   1 
ATOM   7831  C  CA  . PHE C  1 191 ? 11.753  -22.351 -20.038 1.00 16.31 ? 190 PHE C CA  1 
ATOM   7832  C  C   . PHE C  1 191 ? 11.893  -23.791 -19.548 1.00 16.79 ? 190 PHE C C   1 
ATOM   7833  O  O   . PHE C  1 191 ? 12.854  -24.491 -19.921 1.00 17.24 ? 190 PHE C O   1 
ATOM   7834  C  CB  . PHE C  1 191 ? 11.703  -22.237 -21.574 1.00 16.36 ? 190 PHE C CB  1 
ATOM   7835  C  CG  . PHE C  1 191 ? 10.635  -23.032 -22.277 1.00 16.50 ? 190 PHE C CG  1 
ATOM   7836  C  CD1 . PHE C  1 191 ? 9.562   -23.611 -21.613 1.00 16.26 ? 190 PHE C CD1 1 
ATOM   7837  C  CD2 . PHE C  1 191 ? 10.703  -23.160 -23.660 1.00 16.54 ? 190 PHE C CD2 1 
ATOM   7838  C  CE1 . PHE C  1 191 ? 8.627   -24.365 -22.310 1.00 16.64 ? 190 PHE C CE1 1 
ATOM   7839  C  CE2 . PHE C  1 191 ? 9.766   -23.875 -24.366 1.00 16.89 ? 190 PHE C CE2 1 
ATOM   7840  C  CZ  . PHE C  1 191 ? 8.707   -24.490 -23.687 1.00 16.67 ? 190 PHE C CZ  1 
ATOM   7841  N  N   . VAL C  1 192 ? 11.001  -24.192 -18.638 1.00 16.50 ? 191 VAL C N   1 
ATOM   7842  C  CA  . VAL C  1 192 ? 10.962  -25.554 -18.100 1.00 16.91 ? 191 VAL C CA  1 
ATOM   7843  C  C   . VAL C  1 192 ? 9.848   -26.264 -18.862 1.00 16.48 ? 191 VAL C C   1 
ATOM   7844  O  O   . VAL C  1 192 ? 8.676   -25.903 -18.752 1.00 15.04 ? 191 VAL C O   1 
ATOM   7845  C  CB  . VAL C  1 192 ? 10.706  -25.568 -16.584 1.00 17.60 ? 191 VAL C CB  1 
ATOM   7846  C  CG1 . VAL C  1 192 ? 10.602  -26.993 -16.061 1.00 18.97 ? 191 VAL C CG1 1 
ATOM   7847  C  CG2 . VAL C  1 192 ? 11.822  -24.850 -15.826 1.00 19.14 ? 191 VAL C CG2 1 
ATOM   7848  N  N   . SER C  1 193 ? 10.243  -27.283 -19.626 1.00 16.79 ? 192 SER C N   1 
ATOM   7849  C  CA  . SER C  1 193 ? 9.384   -27.959 -20.576 1.00 17.63 ? 192 SER C CA  1 
ATOM   7850  C  C   . SER C  1 193 ? 9.067   -29.343 -20.041 1.00 17.04 ? 192 SER C C   1 
ATOM   7851  O  O   . SER C  1 193 ? 9.981   -30.172 -19.875 1.00 16.91 ? 192 SER C O   1 
ATOM   7852  C  CB  . SER C  1 193 ? 10.170  -28.051 -21.887 1.00 20.10 ? 192 SER C CB  1 
ATOM   7853  O  OG  . SER C  1 193 ? 9.438   -28.655 -22.888 1.00 22.50 ? 192 SER C OG  1 
ATOM   7854  N  N   . LEU C  1 194 ? 7.806   -29.598 -19.718 1.00 15.84 ? 193 LEU C N   1 
ATOM   7855  C  CA  . LEU C  1 194 ? 7.394   -30.865 -19.125 1.00 16.94 ? 193 LEU C CA  1 
ATOM   7856  C  C   . LEU C  1 194 ? 6.553   -31.708 -20.101 1.00 16.46 ? 193 LEU C C   1 
ATOM   7857  O  O   . LEU C  1 194 ? 5.435   -31.323 -20.451 1.00 14.65 ? 193 LEU C O   1 
ATOM   7858  C  CB  . LEU C  1 194 ? 6.586   -30.604 -17.851 1.00 17.79 ? 193 LEU C CB  1 
ATOM   7859  C  CG  . LEU C  1 194 ? 7.214   -29.696 -16.783 1.00 19.41 ? 193 LEU C CG  1 
ATOM   7860  C  CD1 . LEU C  1 194 ? 6.227   -29.437 -15.655 1.00 20.49 ? 193 LEU C CD1 1 
ATOM   7861  C  CD2 . LEU C  1 194 ? 8.482   -30.256 -16.217 1.00 20.74 ? 193 LEU C CD2 1 
ATOM   7862  N  N   . GLY C  1 195 ? 7.104   -32.836 -20.563 1.00 17.16 ? 194 GLY C N   1 
ATOM   7863  C  CA  . GLY C  1 195 ? 6.348   -33.737 -21.413 1.00 17.05 ? 194 GLY C CA  1 
ATOM   7864  C  C   . GLY C  1 195 ? 5.979   -33.159 -22.773 1.00 16.56 ? 194 GLY C C   1 
ATOM   7865  O  O   . GLY C  1 195 ? 4.833   -33.300 -23.231 1.00 15.51 ? 194 GLY C O   1 
ATOM   7866  N  N   . ALA C  1 196 ? 6.922   -32.458 -23.397 1.00 15.72 ? 195 ALA C N   1 
ATOM   7867  C  CA  . ALA C  1 196 ? 6.646   -31.773 -24.678 1.00 15.71 ? 195 ALA C CA  1 
ATOM   7868  C  C   . ALA C  1 196 ? 6.528   -32.741 -25.861 1.00 16.00 ? 195 ALA C C   1 
ATOM   7869  O  O   . ALA C  1 196 ? 7.458   -33.545 -26.109 1.00 16.07 ? 195 ALA C O   1 
ATOM   7870  C  CB  . ALA C  1 196 ? 7.743   -30.767 -24.984 1.00 16.08 ? 195 ALA C CB  1 
ATOM   7871  N  N   . PRO C  1 197 ? 5.424   -32.646 -26.636 1.00 15.76 ? 196 PRO C N   1 
ATOM   7872  C  CA  . PRO C  1 197 ? 5.251   -33.471 -27.857 1.00 16.41 ? 196 PRO C CA  1 
ATOM   7873  C  C   . PRO C  1 197 ? 5.846   -32.799 -29.086 1.00 16.75 ? 196 PRO C C   1 
ATOM   7874  O  O   . PRO C  1 197 ? 5.138   -32.528 -30.057 1.00 18.52 ? 196 PRO C O   1 
ATOM   7875  C  CB  . PRO C  1 197 ? 3.721   -33.588 -27.952 1.00 16.17 ? 196 PRO C CB  1 
ATOM   7876  C  CG  . PRO C  1 197 ? 3.259   -32.243 -27.481 1.00 15.57 ? 196 PRO C CG  1 
ATOM   7877  C  CD  . PRO C  1 197 ? 4.197   -31.873 -26.347 1.00 16.00 ? 196 PRO C CD  1 
ATOM   7878  N  N   A TRP C  1 198 ? 7.158   -32.571 -29.041 0.80 17.60 ? 197 TRP C N   1 
ATOM   7879  N  N   B TRP C  1 198 ? 7.152   -32.533 -29.058 0.20 16.54 ? 197 TRP C N   1 
ATOM   7880  C  CA  A TRP C  1 198 ? 7.847   -31.943 -30.125 0.80 18.19 ? 197 TRP C CA  1 
ATOM   7881  C  CA  B TRP C  1 198 ? 7.829   -31.688 -30.072 0.20 16.18 ? 197 TRP C CA  1 
ATOM   7882  C  C   A TRP C  1 198 ? 7.712   -32.965 -31.263 0.80 18.69 ? 197 TRP C C   1 
ATOM   7883  C  C   B TRP C  1 198 ? 7.511   -31.900 -31.578 0.20 15.71 ? 197 TRP C C   1 
ATOM   7884  O  O   A TRP C  1 198 ? 7.964   -34.184 -31.130 0.80 21.36 ? 197 TRP C O   1 
ATOM   7885  O  O   B TRP C  1 198 ? 7.265   -30.929 -32.296 0.20 14.93 ? 197 TRP C O   1 
ATOM   7886  C  CB  A TRP C  1 198 ? 9.334   -31.779 -29.846 0.80 18.50 ? 197 TRP C CB  1 
ATOM   7887  C  CB  B TRP C  1 198 ? 9.338   -31.741 -29.856 0.20 16.66 ? 197 TRP C CB  1 
ATOM   7888  C  CG  A TRP C  1 198 ? 9.752   -31.095 -28.548 0.80 18.07 ? 197 TRP C CG  1 
ATOM   7889  C  CG  B TRP C  1 198 ? 9.785   -31.075 -28.569 0.20 16.71 ? 197 TRP C CG  1 
ATOM   7890  C  CD1 A TRP C  1 198 ? 10.597  -31.604 -27.615 0.80 18.16 ? 197 TRP C CD1 1 
ATOM   7891  C  CD1 B TRP C  1 198 ? 10.620  -31.595 -27.622 0.20 17.01 ? 197 TRP C CD1 1 
ATOM   7892  C  CD2 A TRP C  1 198 ? 9.418   -29.773 -28.103 0.80 18.24 ? 197 TRP C CD2 1 
ATOM   7893  C  CD2 B TRP C  1 198 ? 9.421   -29.768 -28.104 0.20 16.64 ? 197 TRP C CD2 1 
ATOM   7894  N  NE1 A TRP C  1 198 ? 10.785  -30.702 -26.605 0.80 18.43 ? 197 TRP C NE1 1 
ATOM   7895  N  NE1 B TRP C  1 198 ? 10.798  -30.692 -26.602 0.20 17.09 ? 197 TRP C NE1 1 
ATOM   7896  C  CE2 A TRP C  1 198 ? 10.071  -29.571 -26.877 0.80 17.99 ? 197 TRP C CE2 1 
ATOM   7897  C  CE2 B TRP C  1 198 ? 10.074  -29.563 -26.875 0.20 16.75 ? 197 TRP C CE2 1 
ATOM   7898  C  CE3 A TRP C  1 198 ? 8.576   -28.764 -28.597 0.80 18.91 ? 197 TRP C CE3 1 
ATOM   7899  C  CE3 B TRP C  1 198 ? 8.597   -28.754 -28.606 0.20 16.59 ? 197 TRP C CE3 1 
ATOM   7900  C  CZ2 A TRP C  1 198 ? 9.941   -28.379 -26.136 0.80 18.79 ? 197 TRP C CZ2 1 
ATOM   7901  C  CZ2 B TRP C  1 198 ? 9.934   -28.383 -26.138 0.20 16.86 ? 197 TRP C CZ2 1 
ATOM   7902  C  CZ3 A TRP C  1 198 ? 8.456   -27.572 -27.858 0.80 18.35 ? 197 TRP C CZ3 1 
ATOM   7903  C  CZ3 B TRP C  1 198 ? 8.463   -27.579 -27.871 0.20 16.42 ? 197 TRP C CZ3 1 
ATOM   7904  C  CH2 A TRP C  1 198 ? 9.119   -27.402 -26.656 0.80 17.78 ? 197 TRP C CH2 1 
ATOM   7905  C  CH2 B TRP C  1 198 ? 9.124   -27.408 -26.657 0.20 16.42 ? 197 TRP C CH2 1 
ATOM   7906  N  N   A GLY C  1 199 ? 7.318   -32.495 -32.391 0.80 18.97 ? 198 GLY C N   1 
ATOM   7907  N  N   B GLY C  1 199 ? 7.533   -33.151 -32.044 0.20 16.08 ? 198 GLY C N   1 
ATOM   7908  C  CA  A GLY C  1 199 ? 7.174   -33.417 -33.531 0.80 18.19 ? 198 GLY C CA  1 
ATOM   7909  C  CA  B GLY C  1 199 ? 7.208   -33.501 -33.443 0.20 16.56 ? 198 GLY C CA  1 
ATOM   7910  C  C   A GLY C  1 199 ? 5.912   -34.282 -33.568 0.80 17.72 ? 198 GLY C C   1 
ATOM   7911  C  C   B GLY C  1 199 ? 5.926   -34.310 -33.544 0.20 16.81 ? 198 GLY C C   1 
ATOM   7912  O  O   A GLY C  1 199 ? 5.810   -35.157 -34.427 0.80 17.19 ? 198 GLY C O   1 
ATOM   7913  O  O   B GLY C  1 199 ? 5.806   -35.164 -34.420 0.20 16.82 ? 198 GLY C O   1 
ATOM   7914  N  N   . GLY C  1 200 ? 4.967   -34.019 -32.662 1.00 17.19 ? 199 GLY C N   1 
ATOM   7915  C  CA  . GLY C  1 200 ? 3.659   -34.687 -32.648 1.00 17.56 ? 199 GLY C CA  1 
ATOM   7916  C  C   . GLY C  1 200 ? 3.696   -36.016 -31.923 1.00 17.99 ? 199 GLY C C   1 
ATOM   7917  O  O   . GLY C  1 200 ? 4.776   -36.482 -31.526 1.00 19.08 ? 199 GLY C O   1 
ATOM   7918  N  N   . VAL C  1 201 ? 2.544   -36.665 -31.802 1.00 17.35 ? 200 VAL C N   1 
ATOM   7919  C  CA  . VAL C  1 201 ? 2.469   -37.958 -31.115 1.00 17.85 ? 200 VAL C CA  1 
ATOM   7920  C  C   . VAL C  1 201 ? 1.671   -38.975 -31.916 1.00 17.21 ? 200 VAL C C   1 
ATOM   7921  O  O   . VAL C  1 201 ? 0.689   -38.617 -32.566 1.00 16.04 ? 200 VAL C O   1 
ATOM   7922  C  CB  . VAL C  1 201 ? 1.891   -37.857 -29.690 1.00 19.80 ? 200 VAL C CB  1 
ATOM   7923  C  CG1 . VAL C  1 201 ? 2.716   -36.895 -28.821 1.00 20.69 ? 200 VAL C CG1 1 
ATOM   7924  C  CG2 . VAL C  1 201 ? 0.450   -37.420 -29.702 1.00 19.90 ? 200 VAL C CG2 1 
ATOM   7925  N  N   . ALA C  1 202 ? 2.084   -40.237 -31.872 1.00 16.62 ? 201 ALA C N   1 
ATOM   7926  C  CA  . ALA C  1 202 ? 1.467   -41.258 -32.704 1.00 16.91 ? 201 ALA C CA  1 
ATOM   7927  C  C   . ALA C  1 202 ? -0.009  -41.452 -32.345 1.00 17.51 ? 201 ALA C C   1 
ATOM   7928  O  O   . ALA C  1 202 ? -0.822  -41.748 -33.215 1.00 16.84 ? 201 ALA C O   1 
ATOM   7929  C  CB  . ALA C  1 202 ? 2.201   -42.575 -32.552 1.00 17.66 ? 201 ALA C CB  1 
ATOM   7930  N  N   . LYS C  1 203 ? -0.363  -41.313 -31.080 1.00 18.03 ? 202 LYS C N   1 
ATOM   7931  C  CA  . LYS C  1 203 ? -1.753  -41.617 -30.700 1.00 19.77 ? 202 LYS C CA  1 
ATOM   7932  C  C   . LYS C  1 203 ? -2.814  -40.690 -31.297 1.00 18.68 ? 202 LYS C C   1 
ATOM   7933  O  O   . LYS C  1 203 ? -3.997  -41.039 -31.304 1.00 17.64 ? 202 LYS C O   1 
ATOM   7934  C  CB  . LYS C  1 203 ? -1.923  -41.760 -29.187 1.00 24.00 ? 202 LYS C CB  1 
ATOM   7935  C  CG  . LYS C  1 203 ? -1.989  -40.488 -28.415 1.00 28.48 ? 202 LYS C CG  1 
ATOM   7936  C  CD  . LYS C  1 203 ? -2.215  -40.761 -26.931 1.00 35.31 ? 202 LYS C CD  1 
ATOM   7937  C  CE  . LYS C  1 203 ? -3.463  -41.579 -26.690 1.00 39.26 ? 202 LYS C CE  1 
ATOM   7938  N  NZ  . LYS C  1 203 ? -3.978  -41.414 -25.303 1.00 43.45 ? 202 LYS C NZ  1 
ATOM   7939  N  N   . THR C  1 204 ? -2.400  -39.552 -31.838 1.00 18.05 ? 203 THR C N   1 
ATOM   7940  C  CA  . THR C  1 204 ? -3.290  -38.646 -32.555 1.00 18.50 ? 203 THR C CA  1 
ATOM   7941  C  C   . THR C  1 204 ? -4.004  -39.360 -33.717 1.00 17.74 ? 203 THR C C   1 
ATOM   7942  O  O   . THR C  1 204 ? -5.174  -39.079 -34.004 1.00 17.34 ? 203 THR C O   1 
ATOM   7943  C  CB  . THR C  1 204 ? -2.486  -37.470 -33.122 1.00 20.09 ? 203 THR C CB  1 
ATOM   7944  O  OG1 . THR C  1 204 ? -1.737  -36.833 -32.063 1.00 23.19 ? 203 THR C OG1 1 
ATOM   7945  C  CG2 . THR C  1 204 ? -3.389  -36.455 -33.713 1.00 21.47 ? 203 THR C CG2 1 
ATOM   7946  N  N   . LEU C  1 205 ? -3.322  -40.293 -34.372 1.00 16.62 ? 204 LEU C N   1 
ATOM   7947  C  CA  . LEU C  1 205 ? -3.953  -41.052 -35.449 1.00 17.84 ? 204 LEU C CA  1 
ATOM   7948  C  C   . LEU C  1 205 ? -5.133  -41.856 -34.937 1.00 17.54 ? 204 LEU C C   1 
ATOM   7949  O  O   . LEU C  1 205 ? -6.188  -41.873 -35.571 1.00 16.82 ? 204 LEU C O   1 
ATOM   7950  C  CB  . LEU C  1 205 ? -2.978  -42.028 -36.103 1.00 19.14 ? 204 LEU C CB  1 
ATOM   7951  C  CG  . LEU C  1 205 ? -1.947  -41.574 -37.136 1.00 21.80 ? 204 LEU C CG  1 
ATOM   7952  C  CD1 . LEU C  1 205 ? -2.528  -40.983 -38.411 1.00 23.49 ? 204 LEU C CD1 1 
ATOM   7953  C  CD2 . LEU C  1 205 ? -0.921  -40.641 -36.571 1.00 21.35 ? 204 LEU C CD2 1 
ATOM   7954  N  N   . ARG C  1 206 ? -4.980  -42.512 -33.795 1.00 17.78 ? 205 ARG C N   1 
ATOM   7955  C  CA  . ARG C  1 206 ? -6.072  -43.300 -33.226 1.00 19.42 ? 205 ARG C CA  1 
ATOM   7956  C  C   . ARG C  1 206 ? -7.231  -42.382 -32.788 1.00 18.48 ? 205 ARG C C   1 
ATOM   7957  O  O   . ARG C  1 206 ? -8.396  -42.706 -33.013 1.00 19.07 ? 205 ARG C O   1 
ATOM   7958  C  CB  . ARG C  1 206 ? -5.613  -44.169 -32.055 1.00 22.18 ? 205 ARG C CB  1 
ATOM   7959  C  CG  . ARG C  1 206 ? -6.739  -44.960 -31.387 1.00 26.32 ? 205 ARG C CG  1 
ATOM   7960  C  CD  . ARG C  1 206 ? -6.202  -45.718 -30.177 1.00 32.82 ? 205 ARG C CD  1 
ATOM   7961  N  NE  . ARG C  1 206 ? -7.151  -46.630 -29.530 1.00 37.76 ? 205 ARG C NE  1 
ATOM   7962  C  CZ  . ARG C  1 206 ? -8.013  -46.294 -28.579 1.00 43.48 ? 205 ARG C CZ  1 
ATOM   7963  N  NH1 . ARG C  1 206 ? -8.073  -45.054 -28.124 1.00 46.58 ? 205 ARG C NH1 1 
ATOM   7964  N  NH2 . ARG C  1 206 ? -8.835  -47.216 -28.080 1.00 45.51 ? 205 ARG C NH2 1 
ATOM   7965  N  N   . VAL C  1 207 ? -6.899  -41.268 -32.147 1.00 18.10 ? 206 VAL C N   1 
ATOM   7966  C  CA  . VAL C  1 207 ? -7.900  -40.299 -31.720 1.00 18.51 ? 206 VAL C CA  1 
ATOM   7967  C  C   . VAL C  1 207 ? -8.790  -39.897 -32.897 1.00 17.85 ? 206 VAL C C   1 
ATOM   7968  O  O   . VAL C  1 207 ? -10.034 -39.984 -32.810 1.00 18.30 ? 206 VAL C O   1 
ATOM   7969  C  CB  . VAL C  1 207 ? -7.265  -39.044 -31.057 1.00 18.59 ? 206 VAL C CB  1 
ATOM   7970  C  CG1 . VAL C  1 207 ? -8.309  -37.972 -30.786 1.00 19.21 ? 206 VAL C CG1 1 
ATOM   7971  C  CG2 . VAL C  1 207 ? -6.549  -39.439 -29.781 1.00 19.05 ? 206 VAL C CG2 1 
ATOM   7972  N  N   . LEU C  1 208 ? -8.171  -39.474 -33.989 1.00 16.60 ? 207 LEU C N   1 
ATOM   7973  C  CA  . LEU C  1 208 ? -8.919  -38.989 -35.155 1.00 16.86 ? 207 LEU C CA  1 
ATOM   7974  C  C   . LEU C  1 208 ? -9.679  -40.113 -35.853 1.00 17.50 ? 207 LEU C C   1 
ATOM   7975  O  O   . LEU C  1 208 ? -10.789 -39.903 -36.309 1.00 16.29 ? 207 LEU C O   1 
ATOM   7976  C  CB  . LEU C  1 208 ? -7.966  -38.300 -36.133 1.00 17.21 ? 207 LEU C CB  1 
ATOM   7977  C  CG  . LEU C  1 208 ? -7.377  -36.991 -35.622 1.00 16.82 ? 207 LEU C CG  1 
ATOM   7978  C  CD1 . LEU C  1 208 ? -6.189  -36.564 -36.445 1.00 17.27 ? 207 LEU C CD1 1 
ATOM   7979  C  CD2 . LEU C  1 208 ? -8.433  -35.898 -35.643 1.00 17.36 ? 207 LEU C CD2 1 
ATOM   7980  N  N   . ALA C  1 209 ? -9.069  -41.297 -35.958 1.00 17.31 ? 208 ALA C N   1 
ATOM   7981  C  CA  . ALA C  1 209 ? -9.698  -42.408 -36.677 1.00 18.64 ? 208 ALA C CA  1 
ATOM   7982  C  C   . ALA C  1 209 ? -10.905 -42.945 -35.932 1.00 19.69 ? 208 ALA C C   1 
ATOM   7983  O  O   . ALA C  1 209 ? -12.008 -43.016 -36.493 1.00 19.38 ? 208 ALA C O   1 
ATOM   7984  C  CB  . ALA C  1 209 ? -8.692  -43.536 -36.951 1.00 17.97 ? 208 ALA C CB  1 
ATOM   7985  N  N   . SER C  1 210 ? -10.710 -43.309 -34.671 1.00 20.25 ? 209 SER C N   1 
ATOM   7986  C  CA  . SER C  1 210 ? -11.685 -44.101 -33.951 1.00 21.87 ? 209 SER C CA  1 
ATOM   7987  C  C   . SER C  1 210 ? -12.079 -43.566 -32.581 1.00 23.10 ? 209 SER C C   1 
ATOM   7988  O  O   . SER C  1 210 ? -12.889 -44.187 -31.897 1.00 24.66 ? 209 SER C O   1 
ATOM   7989  C  CB  . SER C  1 210 ? -11.205 -45.579 -33.889 1.00 23.58 ? 209 SER C CB  1 
ATOM   7990  O  OG  . SER C  1 210 ? -9.895  -45.721 -33.423 1.00 24.21 ? 209 SER C OG  1 
ATOM   7991  N  N   . GLY C  1 211 ? -11.551 -42.404 -32.187 1.00 22.40 ? 210 GLY C N   1 
ATOM   7992  C  CA  . GLY C  1 211 ? -11.900 -41.758 -30.923 1.00 23.12 ? 210 GLY C CA  1 
ATOM   7993  C  C   . GLY C  1 211 ? -11.089 -42.302 -29.758 1.00 26.01 ? 210 GLY C C   1 
ATOM   7994  O  O   . GLY C  1 211 ? -10.540 -43.401 -29.828 1.00 26.26 ? 210 GLY C O   1 
ATOM   7995  N  N   . ASP C  1 212 ? -11.034 -41.546 -28.673 1.00 27.75 ? 211 ASP C N   1 
ATOM   7996  C  CA  . ASP C  1 212 ? -10.351 -41.980 -27.473 1.00 29.45 ? 211 ASP C CA  1 
ATOM   7997  C  C   . ASP C  1 212 ? -11.192 -41.592 -26.261 1.00 31.70 ? 211 ASP C C   1 
ATOM   7998  O  O   . ASP C  1 212 ? -11.240 -40.415 -25.881 1.00 31.36 ? 211 ASP C O   1 
ATOM   7999  C  CB  . ASP C  1 212 ? -8.969  -41.328 -27.389 1.00 30.84 ? 211 ASP C CB  1 
ATOM   8000  C  CG  . ASP C  1 212 ? -8.153  -41.813 -26.198 1.00 34.81 ? 211 ASP C CG  1 
ATOM   8001  O  OD1 . ASP C  1 212 ? -8.612  -42.674 -25.418 1.00 34.72 ? 211 ASP C OD1 1 
ATOM   8002  O  OD2 . ASP C  1 212 ? -7.026  -41.313 -26.041 1.00 39.07 ? 211 ASP C OD2 1 
ATOM   8003  N  N   . ASN C  1 213 ? -11.839 -42.581 -25.659 1.00 33.21 ? 212 ASN C N   1 
ATOM   8004  C  CA  . ASN C  1 213 ? -12.648 -42.348 -24.461 1.00 38.17 ? 212 ASN C CA  1 
ATOM   8005  C  C   . ASN C  1 213 ? -11.892 -42.609 -23.161 1.00 45.52 ? 212 ASN C C   1 
ATOM   8006  O  O   . ASN C  1 213 ? -12.517 -42.712 -22.098 1.00 45.32 ? 212 ASN C O   1 
ATOM   8007  C  CB  . ASN C  1 213 ? -13.944 -43.157 -24.530 1.00 40.04 ? 212 ASN C CB  1 
ATOM   8008  C  CG  . ASN C  1 213 ? -13.704 -44.649 -24.363 1.00 42.07 ? 212 ASN C CG  1 
ATOM   8009  O  OD1 . ASN C  1 213 ? -12.563 -45.092 -24.317 1.00 42.07 ? 212 ASN C OD1 1 
ATOM   8010  N  ND2 . ASN C  1 213 ? -14.765 -45.423 -24.284 1.00 42.15 ? 212 ASN C ND2 1 
ATOM   8011  N  N   . ASN C  1 214 ? -10.566 -42.759 -23.254 1.00 48.29 ? 213 ASN C N   1 
ATOM   8012  C  CA  . ASN C  1 214 ? -9.692  -42.727 -22.097 1.00 54.18 ? 213 ASN C CA  1 
ATOM   8013  C  C   . ASN C  1 214 ? -10.009 -43.768 -21.048 1.00 55.82 ? 213 ASN C C   1 
ATOM   8014  O  O   . ASN C  1 214 ? -9.621  -43.583 -19.918 1.00 56.84 ? 213 ASN C O   1 
ATOM   8015  C  CB  . ASN C  1 214 ? -9.786  -41.332 -21.483 1.00 58.19 ? 213 ASN C CB  1 
ATOM   8016  C  CG  . ASN C  1 214 ? -8.620  -40.988 -20.572 1.00 62.17 ? 213 ASN C CG  1 
ATOM   8017  O  OD1 . ASN C  1 214 ? -7.677  -41.764 -20.399 1.00 65.45 ? 213 ASN C OD1 1 
ATOM   8018  N  ND2 . ASN C  1 214 ? -8.674  -39.796 -19.996 1.00 62.51 ? 213 ASN C ND2 1 
ATOM   8019  N  N   . ARG C  1 215 ? -10.711 -44.839 -21.433 1.00 60.46 ? 214 ARG C N   1 
ATOM   8020  C  CA  . ARG C  1 215 ? -11.166 -45.921 -20.526 1.00 66.86 ? 214 ARG C CA  1 
ATOM   8021  C  C   . ARG C  1 215 ? -12.275 -45.490 -19.558 1.00 66.05 ? 214 ARG C C   1 
ATOM   8022  O  O   . ARG C  1 215 ? -12.458 -46.077 -18.492 1.00 69.87 ? 214 ARG C O   1 
ATOM   8023  C  CB  . ARG C  1 215 ? -9.984  -46.600 -19.826 1.00 70.56 ? 214 ARG C CB  1 
ATOM   8024  C  CG  . ARG C  1 215 ? -9.146  -47.370 -20.834 1.00 74.28 ? 214 ARG C CG  1 
ATOM   8025  C  CD  . ARG C  1 215 ? -8.087  -48.252 -20.184 1.00 79.29 ? 214 ARG C CD  1 
ATOM   8026  N  NE  . ARG C  1 215 ? -6.921  -48.392 -21.049 1.00 83.26 ? 214 ARG C NE  1 
ATOM   8027  C  CZ  . ARG C  1 215 ? -5.780  -48.968 -20.684 1.00 85.57 ? 214 ARG C CZ  1 
ATOM   8028  N  NH1 . ARG C  1 215 ? -5.635  -49.469 -19.463 1.00 86.36 ? 214 ARG C NH1 1 
ATOM   8029  N  NH2 . ARG C  1 215 ? -4.776  -49.043 -21.550 1.00 89.35 ? 214 ARG C NH2 1 
ATOM   8030  N  N   . ILE C  1 216 ? -12.996 -44.446 -19.969 1.00 64.84 ? 215 ILE C N   1 
ATOM   8031  C  CA  . ILE C  1 216 ? -14.291 -44.058 -19.425 1.00 60.59 ? 215 ILE C CA  1 
ATOM   8032  C  C   . ILE C  1 216 ? -15.344 -44.738 -20.307 1.00 62.59 ? 215 ILE C C   1 
ATOM   8033  O  O   . ILE C  1 216 ? -15.791 -44.124 -21.268 1.00 66.89 ? 215 ILE C O   1 
ATOM   8034  C  CB  . ILE C  1 216 ? -14.449 -42.527 -19.442 1.00 59.81 ? 215 ILE C CB  1 
ATOM   8035  C  CG1 . ILE C  1 216 ? -13.361 -41.903 -18.568 1.00 56.93 ? 215 ILE C CG1 1 
ATOM   8036  C  CG2 . ILE C  1 216 ? -15.829 -42.102 -18.937 1.00 61.35 ? 215 ILE C CG2 1 
ATOM   8037  C  CD1 . ILE C  1 216 ? -13.025 -40.491 -18.955 1.00 55.08 ? 215 ILE C CD1 1 
ATOM   8038  N  N   . PRO C  1 217 ? -15.715 -46.013 -20.009 1.00 64.71 ? 216 PRO C N   1 
ATOM   8039  C  CA  . PRO C  1 217 ? -16.625 -46.801 -20.863 1.00 64.91 ? 216 PRO C CA  1 
ATOM   8040  C  C   . PRO C  1 217 ? -18.040 -46.249 -21.012 1.00 64.36 ? 216 PRO C C   1 
ATOM   8041  O  O   . PRO C  1 217 ? -18.749 -46.639 -21.946 1.00 66.03 ? 216 PRO C O   1 
ATOM   8042  C  CB  . PRO C  1 217 ? -16.690 -48.166 -20.152 1.00 67.59 ? 216 PRO C CB  1 
ATOM   8043  C  CG  . PRO C  1 217 ? -16.334 -47.877 -18.740 1.00 66.99 ? 216 PRO C CG  1 
ATOM   8044  C  CD  . PRO C  1 217 ? -15.279 -46.811 -18.846 1.00 66.08 ? 216 PRO C CD  1 
ATOM   8045  N  N   . VAL C  1 218 ? -18.461 -45.373 -20.102 1.00 59.97 ? 217 VAL C N   1 
ATOM   8046  C  CA  . VAL C  1 218 ? -19.763 -44.742 -20.245 1.00 58.12 ? 217 VAL C CA  1 
ATOM   8047  C  C   . VAL C  1 218 ? -19.756 -43.688 -21.366 1.00 53.86 ? 217 VAL C C   1 
ATOM   8048  O  O   . VAL C  1 218 ? -20.805 -43.167 -21.727 1.00 50.21 ? 217 VAL C O   1 
ATOM   8049  C  CB  . VAL C  1 218 ? -20.260 -44.147 -18.902 1.00 60.23 ? 217 VAL C CB  1 
ATOM   8050  C  CG1 . VAL C  1 218 ? -19.565 -42.829 -18.579 1.00 60.52 ? 217 VAL C CG1 1 
ATOM   8051  C  CG2 . VAL C  1 218 ? -21.772 -43.974 -18.923 1.00 62.98 ? 217 VAL C CG2 1 
ATOM   8052  N  N   . ILE C  1 219 ? -18.577 -43.339 -21.884 1.00 47.84 ? 218 ILE C N   1 
ATOM   8053  C  CA  . ILE C  1 219 ? -18.491 -42.479 -23.072 1.00 47.22 ? 218 ILE C CA  1 
ATOM   8054  C  C   . ILE C  1 219 ? -18.090 -43.331 -24.267 1.00 43.10 ? 218 ILE C C   1 
ATOM   8055  O  O   . ILE C  1 219 ? -17.035 -43.910 -24.236 1.00 42.36 ? 218 ILE C O   1 
ATOM   8056  C  CB  . ILE C  1 219 ? -17.453 -41.342 -22.876 1.00 48.19 ? 218 ILE C CB  1 
ATOM   8057  C  CG1 . ILE C  1 219 ? -17.694 -40.612 -21.561 1.00 47.50 ? 218 ILE C CG1 1 
ATOM   8058  C  CG2 . ILE C  1 219 ? -17.512 -40.332 -24.017 1.00 49.93 ? 218 ILE C CG2 1 
ATOM   8059  C  CD1 . ILE C  1 219 ? -16.630 -39.594 -21.221 1.00 48.05 ? 218 ILE C CD1 1 
ATOM   8060  N  N   . GLY C  1 220 ? -18.937 -43.444 -25.285 1.00 40.64 ? 219 GLY C N   1 
ATOM   8061  C  CA  . GLY C  1 220 ? -18.585 -44.186 -26.493 1.00 40.49 ? 219 GLY C CA  1 
ATOM   8062  C  C   . GLY C  1 220 ? -17.418 -43.484 -27.176 1.00 38.39 ? 219 GLY C C   1 
ATOM   8063  O  O   . GLY C  1 220 ? -17.372 -42.249 -27.220 1.00 35.19 ? 219 GLY C O   1 
ATOM   8064  N  N   . PRO C  1 221 ? -16.435 -44.257 -27.655 1.00 37.05 ? 220 PRO C N   1 
ATOM   8065  C  CA  . PRO C  1 221 ? -15.325 -43.590 -28.337 1.00 33.83 ? 220 PRO C CA  1 
ATOM   8066  C  C   . PRO C  1 221 ? -15.807 -42.874 -29.613 1.00 31.58 ? 220 PRO C C   1 
ATOM   8067  O  O   . PRO C  1 221 ? -15.290 -41.821 -29.936 1.00 29.49 ? 220 PRO C O   1 
ATOM   8068  C  CB  . PRO C  1 221 ? -14.367 -44.750 -28.656 1.00 34.94 ? 220 PRO C CB  1 
ATOM   8069  C  CG  . PRO C  1 221 ? -15.239 -45.963 -28.707 1.00 36.36 ? 220 PRO C CG  1 
ATOM   8070  C  CD  . PRO C  1 221 ? -16.276 -45.724 -27.638 1.00 37.79 ? 220 PRO C CD  1 
ATOM   8071  N  N   . LEU C  1 222 ? -16.784 -43.433 -30.324 1.00 33.18 ? 221 LEU C N   1 
ATOM   8072  C  CA  . LEU C  1 222 ? -17.276 -42.822 -31.570 1.00 34.04 ? 221 LEU C CA  1 
ATOM   8073  C  C   . LEU C  1 222 ? -18.037 -41.522 -31.316 1.00 34.13 ? 221 LEU C C   1 
ATOM   8074  O  O   . LEU C  1 222 ? -18.087 -40.648 -32.177 1.00 31.96 ? 221 LEU C O   1 
ATOM   8075  C  CB  . LEU C  1 222 ? -18.134 -43.789 -32.374 1.00 35.17 ? 221 LEU C CB  1 
ATOM   8076  C  CG  . LEU C  1 222 ? -17.468 -45.086 -32.855 1.00 36.95 ? 221 LEU C CG  1 
ATOM   8077  C  CD1 . LEU C  1 222 ? -18.415 -45.859 -33.762 1.00 37.97 ? 221 LEU C CD1 1 
ATOM   8078  C  CD2 . LEU C  1 222 ? -16.143 -44.832 -33.569 1.00 36.28 ? 221 LEU C CD2 1 
ATOM   8079  N  N   . LYS C  1 223 ? -18.600 -41.392 -30.123 1.00 34.36 ? 222 LYS C N   1 
ATOM   8080  C  CA  . LYS C  1 223 ? -19.298 -40.177 -29.717 1.00 35.10 ? 222 LYS C CA  1 
ATOM   8081  C  C   . LYS C  1 223 ? -18.308 -39.061 -29.419 1.00 32.58 ? 222 LYS C C   1 
ATOM   8082  O  O   . LYS C  1 223 ? -18.400 -37.976 -29.982 1.00 31.74 ? 222 LYS C O   1 
ATOM   8083  C  CB  . LYS C  1 223 ? -20.176 -40.510 -28.493 1.00 37.92 ? 222 LYS C CB  1 
ATOM   8084  C  CG  . LYS C  1 223 ? -21.014 -39.408 -27.877 1.00 39.01 ? 222 LYS C CG  1 
ATOM   8085  C  CD  . LYS C  1 223 ? -21.897 -38.687 -28.892 1.00 39.64 ? 222 LYS C CD  1 
ATOM   8086  C  CE  . LYS C  1 223 ? -22.839 -39.552 -29.688 1.00 41.42 ? 222 LYS C CE  1 
ATOM   8087  N  NZ  . LYS C  1 223 ? -24.135 -39.851 -29.036 1.00 40.74 ? 222 LYS C NZ  1 
ATOM   8088  N  N   . ILE C  1 224 ? -17.329 -39.332 -28.566 1.00 30.16 ? 223 ILE C N   1 
ATOM   8089  C  CA  . ILE C  1 224 ? -16.329 -38.327 -28.205 1.00 29.66 ? 223 ILE C CA  1 
ATOM   8090  C  C   . ILE C  1 224 ? -15.399 -37.959 -29.383 1.00 27.38 ? 223 ILE C C   1 
ATOM   8091  O  O   . ILE C  1 224 ? -14.855 -36.844 -29.430 1.00 27.08 ? 223 ILE C O   1 
ATOM   8092  C  CB  . ILE C  1 224 ? -15.495 -38.773 -26.981 1.00 31.43 ? 223 ILE C CB  1 
ATOM   8093  C  CG1 . ILE C  1 224 ? -14.726 -37.604 -26.380 1.00 34.17 ? 223 ILE C CG1 1 
ATOM   8094  C  CG2 . ILE C  1 224 ? -14.533 -39.896 -27.322 1.00 31.32 ? 223 ILE C CG2 1 
ATOM   8095  C  CD1 . ILE C  1 224 ? -15.632 -36.522 -25.823 1.00 36.45 ? 223 ILE C CD1 1 
ATOM   8096  N  N   . ARG C  1 225 ? -15.261 -38.872 -30.344 1.00 24.15 ? 224 ARG C N   1 
ATOM   8097  C  CA  . ARG C  1 225 ? -14.474 -38.603 -31.559 1.00 23.29 ? 224 ARG C CA  1 
ATOM   8098  C  C   . ARG C  1 225 ? -14.946 -37.324 -32.257 1.00 22.86 ? 224 ARG C C   1 
ATOM   8099  O  O   . ARG C  1 225 ? -14.154 -36.581 -32.827 1.00 21.84 ? 224 ARG C O   1 
ATOM   8100  C  CB  . ARG C  1 225 ? -14.583 -39.791 -32.503 1.00 22.97 ? 224 ARG C CB  1 
ATOM   8101  C  CG  . ARG C  1 225 ? -13.661 -39.699 -33.711 1.00 22.55 ? 224 ARG C CG  1 
ATOM   8102  C  CD  . ARG C  1 225 ? -13.835 -40.903 -34.618 1.00 22.29 ? 224 ARG C CD  1 
ATOM   8103  N  NE  . ARG C  1 225 ? -15.172 -40.974 -35.213 1.00 22.39 ? 224 ARG C NE  1 
ATOM   8104  C  CZ  . ARG C  1 225 ? -15.597 -41.965 -35.999 1.00 23.88 ? 224 ARG C CZ  1 
ATOM   8105  N  NH1 . ARG C  1 225 ? -14.801 -42.978 -36.333 1.00 22.17 ? 224 ARG C NH1 1 
ATOM   8106  N  NH2 . ARG C  1 225 ? -16.846 -41.971 -36.437 1.00 25.56 ? 224 ARG C NH2 1 
ATOM   8107  N  N   . GLU C  1 226 ? -16.252 -37.070 -32.194 1.00 23.87 ? 225 GLU C N   1 
ATOM   8108  C  CA  . GLU C  1 226 ? -16.829 -35.874 -32.817 1.00 25.86 ? 225 GLU C CA  1 
ATOM   8109  C  C   . GLU C  1 226 ? -16.163 -34.602 -32.297 1.00 24.10 ? 225 GLU C C   1 
ATOM   8110  O  O   . GLU C  1 226 ? -15.799 -33.714 -33.074 1.00 25.39 ? 225 GLU C O   1 
ATOM   8111  C  CB  . GLU C  1 226 ? -18.345 -35.822 -32.589 1.00 28.16 ? 225 GLU C CB  1 
ATOM   8112  C  CG  . GLU C  1 226 ? -19.161 -36.999 -33.113 1.00 32.29 ? 225 GLU C CG  1 
ATOM   8113  C  CD  . GLU C  1 226 ? -20.599 -37.018 -32.578 1.00 37.77 ? 225 GLU C CD  1 
ATOM   8114  O  OE1 . GLU C  1 226 ? -21.296 -38.064 -32.590 1.00 40.32 ? 225 GLU C OE1 1 
ATOM   8115  O  OE2 . GLU C  1 226 ? -21.043 -35.936 -32.183 1.00 39.79 ? 225 GLU C OE2 1 
ATOM   8116  N  N   . GLN C  1 227 ? -16.000 -34.492 -30.985 1.00 23.60 ? 226 GLN C N   1 
ATOM   8117  C  CA  . GLN C  1 227 ? -15.355 -33.313 -30.410 1.00 22.51 ? 226 GLN C CA  1 
ATOM   8118  C  C   . GLN C  1 227 ? -13.873 -33.302 -30.708 1.00 21.04 ? 226 GLN C C   1 
ATOM   8119  O  O   . GLN C  1 227 ? -13.320 -32.254 -31.046 1.00 19.61 ? 226 GLN C O   1 
ATOM   8120  C  CB  . GLN C  1 227 ? -15.529 -33.245 -28.892 1.00 23.91 ? 226 GLN C CB  1 
ATOM   8121  C  CG  . GLN C  1 227 ? -14.911 -31.992 -28.240 1.00 23.77 ? 226 GLN C CG  1 
ATOM   8122  C  CD  . GLN C  1 227 ? -13.418 -32.045 -27.959 1.00 24.93 ? 226 GLN C CD  1 
ATOM   8123  O  OE1 . GLN C  1 227 ? -12.715 -31.033 -28.091 1.00 26.38 ? 226 GLN C OE1 1 
ATOM   8124  N  NE2 . GLN C  1 227 ? -12.926 -33.187 -27.551 1.00 23.86 ? 226 GLN C NE2 1 
ATOM   8125  N  N   . GLN C  1 228 ? -13.246 -34.465 -30.609 1.00 19.43 ? 227 GLN C N   1 
ATOM   8126  C  CA  . GLN C  1 228 ? -11.796 -34.544 -30.777 1.00 19.65 ? 227 GLN C CA  1 
ATOM   8127  C  C   . GLN C  1 228 ? -11.386 -34.128 -32.201 1.00 18.13 ? 227 GLN C C   1 
ATOM   8128  O  O   . GLN C  1 228 ? -10.425 -33.396 -32.394 1.00 17.23 ? 227 GLN C O   1 
ATOM   8129  C  CB  . GLN C  1 228 ? -11.317 -35.956 -30.401 1.00 20.81 ? 227 GLN C CB  1 
ATOM   8130  C  CG  . GLN C  1 228 ? -11.476 -36.235 -28.905 1.00 22.50 ? 227 GLN C CG  1 
ATOM   8131  C  CD  . GLN C  1 228 ? -11.354 -37.712 -28.492 1.00 24.80 ? 227 GLN C CD  1 
ATOM   8132  O  OE1 . GLN C  1 228 ? -11.722 -38.643 -29.226 1.00 24.25 ? 227 GLN C OE1 1 
ATOM   8133  N  NE2 . GLN C  1 228 ? -10.890 -37.923 -27.254 1.00 26.56 ? 227 GLN C NE2 1 
ATOM   8134  N  N   . ARG C  1 229 ? -12.152 -34.539 -33.191 1.00 17.03 ? 228 ARG C N   1 
ATOM   8135  C  CA  . ARG C  1 229 ? -11.893 -34.132 -34.572 1.00 17.32 ? 228 ARG C CA  1 
ATOM   8136  C  C   . ARG C  1 229 ? -12.090 -32.638 -34.796 1.00 18.00 ? 228 ARG C C   1 
ATOM   8137  O  O   . ARG C  1 229 ? -11.376 -32.029 -35.601 1.00 17.83 ? 228 ARG C O   1 
ATOM   8138  C  CB  . ARG C  1 229 ? -12.825 -34.884 -35.536 1.00 17.63 ? 228 ARG C CB  1 
ATOM   8139  C  CG  . ARG C  1 229 ? -12.453 -36.347 -35.750 1.00 17.11 ? 228 ARG C CG  1 
ATOM   8140  C  CD  . ARG C  1 229 ? -13.481 -37.040 -36.617 1.00 17.76 ? 228 ARG C CD  1 
ATOM   8141  N  NE  . ARG C  1 229 ? -13.061 -38.379 -36.957 1.00 17.52 ? 228 ARG C NE  1 
ATOM   8142  C  CZ  . ARG C  1 229 ? -13.699 -39.184 -37.789 1.00 18.23 ? 228 ARG C CZ  1 
ATOM   8143  N  NH1 . ARG C  1 229 ? -14.841 -38.810 -38.367 1.00 18.13 ? 228 ARG C NH1 1 
ATOM   8144  N  NH2 . ARG C  1 229 ? -13.207 -40.385 -38.029 1.00 18.45 ? 228 ARG C NH2 1 
ATOM   8145  N  N   . SER C  1 230 ? -13.091 -32.052 -34.128 1.00 18.20 ? 229 SER C N   1 
ATOM   8146  C  CA  . SER C  1 230 ? -13.447 -30.638 -34.350 1.00 18.64 ? 229 SER C CA  1 
ATOM   8147  C  C   . SER C  1 230 ? -12.408 -29.665 -33.816 1.00 18.71 ? 229 SER C C   1 
ATOM   8148  O  O   . SER C  1 230 ? -12.297 -28.499 -34.299 1.00 20.25 ? 229 SER C O   1 
ATOM   8149  C  CB  . SER C  1 230 ? -14.800 -30.318 -33.720 1.00 19.30 ? 229 SER C CB  1 
ATOM   8150  O  OG  . SER C  1 230 ? -14.689 -30.149 -32.315 1.00 19.25 ? 229 SER C OG  1 
ATOM   8151  N  N   . ALA C  1 231 ? -11.606 -30.138 -32.865 1.00 18.27 ? 230 ALA C N   1 
ATOM   8152  C  CA  . ALA C  1 231 ? -10.532 -29.334 -32.319 1.00 17.95 ? 230 ALA C CA  1 
ATOM   8153  C  C   . ALA C  1 231 ? -9.296  -29.330 -33.247 1.00 18.05 ? 230 ALA C C   1 
ATOM   8154  O  O   . ALA C  1 231 ? -8.647  -30.337 -33.464 1.00 17.89 ? 230 ALA C O   1 
ATOM   8155  C  CB  . ALA C  1 231 ? -10.174 -29.830 -30.928 1.00 18.51 ? 230 ALA C CB  1 
ATOM   8156  N  N   . VAL C  1 232 ? -8.976  -28.153 -33.778 1.00 18.22 ? 231 VAL C N   1 
ATOM   8157  C  CA  . VAL C  1 232 ? -7.820  -27.963 -34.671 1.00 17.78 ? 231 VAL C CA  1 
ATOM   8158  C  C   . VAL C  1 232 ? -6.526  -28.462 -34.029 1.00 17.69 ? 231 VAL C C   1 
ATOM   8159  O  O   . VAL C  1 232 ? -5.656  -29.029 -34.708 1.00 17.58 ? 231 VAL C O   1 
ATOM   8160  C  CB  . VAL C  1 232 ? -7.637  -26.487 -35.078 1.00 19.07 ? 231 VAL C CB  1 
ATOM   8161  C  CG1 . VAL C  1 232 ? -6.518  -26.342 -36.098 1.00 18.46 ? 231 VAL C CG1 1 
ATOM   8162  C  CG2 . VAL C  1 232 ? -8.926  -25.915 -35.650 1.00 20.06 ? 231 VAL C CG2 1 
ATOM   8163  N  N   . SER C  1 233 ? -6.410  -28.300 -32.717 1.00 17.02 ? 232 SER C N   1 
ATOM   8164  C  CA  . SER C  1 233 ? -5.203  -28.699 -32.012 1.00 17.13 ? 232 SER C CA  1 
ATOM   8165  C  C   . SER C  1 233 ? -4.921  -30.208 -32.133 1.00 16.75 ? 232 SER C C   1 
ATOM   8166  O  O   . SER C  1 233 ? -3.762  -30.625 -32.094 1.00 16.60 ? 232 SER C O   1 
ATOM   8167  C  CB  . SER C  1 233 ? -5.278  -28.295 -30.531 1.00 17.42 ? 232 SER C CB  1 
ATOM   8168  O  OG  . SER C  1 233 ? -6.460  -28.786 -29.935 1.00 18.44 ? 232 SER C OG  1 
ATOM   8169  N  N   . THR C  1 234 ? -5.959  -31.028 -32.332 1.00 16.90 ? 233 THR C N   1 
ATOM   8170  C  CA  . THR C  1 234 ? -5.721  -32.474 -32.535 1.00 17.63 ? 233 THR C CA  1 
ATOM   8171  C  C   . THR C  1 234 ? -4.927  -32.780 -33.829 1.00 17.29 ? 233 THR C C   1 
ATOM   8172  O  O   . THR C  1 234 ? -3.891  -33.455 -33.796 1.00 17.94 ? 233 THR C O   1 
ATOM   8173  C  CB  . THR C  1 234 ? -7.023  -33.257 -32.564 1.00 18.52 ? 233 THR C CB  1 
ATOM   8174  O  OG1 . THR C  1 234 ? -7.775  -32.927 -31.400 1.00 18.27 ? 233 THR C OG1 1 
ATOM   8175  C  CG2 . THR C  1 234 ? -6.734  -34.748 -32.579 1.00 19.31 ? 233 THR C CG2 1 
ATOM   8176  N  N   . SER C  1 235 ? -5.368  -32.210 -34.947 1.00 16.68 ? 234 SER C N   1 
ATOM   8177  C  CA  . SER C  1 235 ? -4.663  -32.386 -36.222 1.00 16.80 ? 234 SER C CA  1 
ATOM   8178  C  C   . SER C  1 235 ? -3.279  -31.729 -36.235 1.00 16.10 ? 234 SER C C   1 
ATOM   8179  O  O   . SER C  1 235 ? -2.364  -32.215 -36.893 1.00 15.89 ? 234 SER C O   1 
ATOM   8180  C  CB  . SER C  1 235 ? -5.510  -31.838 -37.366 1.00 17.58 ? 234 SER C CB  1 
ATOM   8181  O  OG  . SER C  1 235 ? -6.667  -32.664 -37.492 1.00 18.75 ? 234 SER C OG  1 
ATOM   8182  N  N   . TRP C  1 236 ? -3.142  -30.617 -35.516 1.00 15.78 ? 235 TRP C N   1 
ATOM   8183  C  CA  . TRP C  1 236 ? -1.851  -29.952 -35.375 1.00 15.92 ? 235 TRP C CA  1 
ATOM   8184  C  C   . TRP C  1 236 ? -0.773  -30.872 -34.786 1.00 15.95 ? 235 TRP C C   1 
ATOM   8185  O  O   . TRP C  1 236 ? 0.416   -30.717 -35.093 1.00 16.84 ? 235 TRP C O   1 
ATOM   8186  C  CB  . TRP C  1 236 ? -2.055  -28.705 -34.479 1.00 16.03 ? 235 TRP C CB  1 
ATOM   8187  C  CG  . TRP C  1 236 ? -0.831  -27.870 -34.223 1.00 15.29 ? 235 TRP C CG  1 
ATOM   8188  C  CD1 . TRP C  1 236 ? 0.103   -27.503 -35.114 1.00 16.00 ? 235 TRP C CD1 1 
ATOM   8189  C  CD2 . TRP C  1 236 ? -0.473  -27.255 -32.987 1.00 15.52 ? 235 TRP C CD2 1 
ATOM   8190  N  NE1 . TRP C  1 236 ? 1.057   -26.729 -34.514 1.00 16.70 ? 235 TRP C NE1 1 
ATOM   8191  C  CE2 . TRP C  1 236 ? 0.728   -26.567 -33.198 1.00 16.49 ? 235 TRP C CE2 1 
ATOM   8192  C  CE3 . TRP C  1 236 ? -1.024  -27.255 -31.722 1.00 15.47 ? 235 TRP C CE3 1 
ATOM   8193  C  CZ2 . TRP C  1 236 ? 1.372   -25.851 -32.187 1.00 16.79 ? 235 TRP C CZ2 1 
ATOM   8194  C  CZ3 . TRP C  1 236 ? -0.388  -26.542 -30.720 1.00 16.25 ? 235 TRP C CZ3 1 
ATOM   8195  C  CH2 . TRP C  1 236 ? 0.791   -25.845 -30.967 1.00 16.18 ? 235 TRP C CH2 1 
ATOM   8196  N  N   . LEU C  1 237 ? -1.176  -31.810 -33.938 1.00 16.09 ? 236 LEU C N   1 
ATOM   8197  C  CA  . LEU C  1 237 ? -0.242  -32.693 -33.262 1.00 17.07 ? 236 LEU C CA  1 
ATOM   8198  C  C   . LEU C  1 237 ? -0.024  -34.066 -33.912 1.00 16.26 ? 236 LEU C C   1 
ATOM   8199  O  O   . LEU C  1 237 ? 0.562   -34.965 -33.292 1.00 16.07 ? 236 LEU C O   1 
ATOM   8200  C  CB  . LEU C  1 237 ? -0.638  -32.808 -31.790 1.00 19.37 ? 236 LEU C CB  1 
ATOM   8201  C  CG  . LEU C  1 237 ? -0.446  -31.478 -31.035 1.00 22.93 ? 236 LEU C CG  1 
ATOM   8202  C  CD1 . LEU C  1 237 ? -0.800  -31.717 -29.589 1.00 25.30 ? 236 LEU C CD1 1 
ATOM   8203  C  CD2 . LEU C  1 237 ? 0.962   -30.918 -31.152 1.00 25.02 ? 236 LEU C CD2 1 
ATOM   8204  N  N   . LEU C  1 238 ? -0.466  -34.249 -35.154 1.00 15.19 ? 237 LEU C N   1 
ATOM   8205  C  CA  . LEU C  1 238 ? -0.071  -35.448 -35.905 1.00 15.17 ? 237 LEU C CA  1 
ATOM   8206  C  C   . LEU C  1 238 ? 1.457   -35.446 -36.069 1.00 14.73 ? 237 LEU C C   1 
ATOM   8207  O  O   . LEU C  1 238 ? 2.055   -34.367 -36.180 1.00 14.53 ? 237 LEU C O   1 
ATOM   8208  C  CB  . LEU C  1 238 ? -0.727  -35.510 -37.290 1.00 15.60 ? 237 LEU C CB  1 
ATOM   8209  C  CG  . LEU C  1 238 ? -2.212  -35.829 -37.318 1.00 15.98 ? 237 LEU C CG  1 
ATOM   8210  C  CD1 . LEU C  1 238 ? -2.798  -35.420 -38.679 1.00 17.17 ? 237 LEU C CD1 1 
ATOM   8211  C  CD2 . LEU C  1 238 ? -2.398  -37.312 -37.097 1.00 16.83 ? 237 LEU C CD2 1 
ATOM   8212  N  N   . PRO C  1 239 ? 2.069   -36.648 -36.111 1.00 14.44 ? 238 PRO C N   1 
ATOM   8213  C  CA  . PRO C  1 239 ? 3.502   -36.785 -36.353 1.00 14.97 ? 238 PRO C CA  1 
ATOM   8214  C  C   . PRO C  1 239 ? 4.075   -35.936 -37.493 1.00 15.59 ? 238 PRO C C   1 
ATOM   8215  O  O   . PRO C  1 239 ? 3.491   -35.840 -38.572 1.00 15.84 ? 238 PRO C O   1 
ATOM   8216  C  CB  . PRO C  1 239 ? 3.669   -38.277 -36.648 1.00 15.22 ? 238 PRO C CB  1 
ATOM   8217  C  CG  . PRO C  1 239 ? 2.607   -38.904 -35.834 1.00 14.70 ? 238 PRO C CG  1 
ATOM   8218  C  CD  . PRO C  1 239 ? 1.438   -37.965 -35.942 1.00 14.47 ? 238 PRO C CD  1 
ATOM   8219  N  N   . TYR C  1 240 ? 5.239   -35.343 -37.220 1.00 16.16 ? 239 TYR C N   1 
ATOM   8220  C  CA  . TYR C  1 240 ? 5.971   -34.517 -38.172 1.00 17.04 ? 239 TYR C CA  1 
ATOM   8221  C  C   . TYR C  1 240 ? 7.230   -35.199 -38.685 1.00 17.57 ? 239 TYR C C   1 
ATOM   8222  O  O   . TYR C  1 240 ? 7.827   -35.999 -37.964 1.00 17.55 ? 239 TYR C O   1 
ATOM   8223  C  CB  . TYR C  1 240 ? 6.402   -33.215 -37.516 1.00 17.13 ? 239 TYR C CB  1 
ATOM   8224  C  CG  . TYR C  1 240 ? 5.286   -32.228 -37.289 1.00 17.44 ? 239 TYR C CG  1 
ATOM   8225  C  CD1 . TYR C  1 240 ? 4.446   -32.333 -36.178 1.00 17.51 ? 239 TYR C CD1 1 
ATOM   8226  C  CD2 . TYR C  1 240 ? 5.081   -31.173 -38.178 1.00 17.90 ? 239 TYR C CD2 1 
ATOM   8227  C  CE1 . TYR C  1 240 ? 3.393   -31.421 -35.976 1.00 17.60 ? 239 TYR C CE1 1 
ATOM   8228  C  CE2 . TYR C  1 240 ? 4.059   -30.261 -37.967 1.00 18.55 ? 239 TYR C CE2 1 
ATOM   8229  C  CZ  . TYR C  1 240 ? 3.223   -30.386 -36.870 1.00 18.37 ? 239 TYR C CZ  1 
ATOM   8230  O  OH  . TYR C  1 240 ? 2.175   -29.483 -36.705 1.00 19.13 ? 239 TYR C OH  1 
ATOM   8231  N  N   . ASN C  1 241 ? 7.620   -34.881 -39.926 1.00 19.24 ? 240 ASN C N   1 
ATOM   8232  C  CA  . ASN C  1 241 ? 8.813   -35.495 -40.547 1.00 21.39 ? 240 ASN C CA  1 
ATOM   8233  C  C   . ASN C  1 241 ? 10.142  -35.019 -40.005 1.00 23.24 ? 240 ASN C C   1 
ATOM   8234  O  O   . ASN C  1 241 ? 11.165  -35.572 -40.380 1.00 24.02 ? 240 ASN C O   1 
ATOM   8235  C  CB  . ASN C  1 241 ? 8.841   -35.383 -42.072 1.00 24.10 ? 240 ASN C CB  1 
ATOM   8236  C  CG  . ASN C  1 241 ? 8.699   -33.967 -42.558 1.00 25.63 ? 240 ASN C CG  1 
ATOM   8237  O  OD1 . ASN C  1 241 ? 8.957   -32.999 -41.829 1.00 25.42 ? 240 ASN C OD1 1 
ATOM   8238  N  ND2 . ASN C  1 241 ? 8.276   -33.837 -43.810 1.00 29.08 ? 240 ASN C ND2 1 
ATOM   8239  N  N   . TYR C  1 242 ? 10.164  -34.037 -39.117 1.00 22.27 ? 241 TYR C N   1 
ATOM   8240  C  CA  . TYR C  1 242 ? 11.448  -33.688 -38.484 1.00 25.11 ? 241 TYR C CA  1 
ATOM   8241  C  C   . TYR C  1 242 ? 11.780  -34.575 -37.280 1.00 25.68 ? 241 TYR C C   1 
ATOM   8242  O  O   . TYR C  1 242 ? 12.891  -34.523 -36.764 1.00 25.50 ? 241 TYR C O   1 
ATOM   8243  C  CB  . TYR C  1 242 ? 11.532  -32.204 -38.142 1.00 25.64 ? 241 TYR C CB  1 
ATOM   8244  C  CG  . TYR C  1 242 ? 10.418  -31.657 -37.300 1.00 25.75 ? 241 TYR C CG  1 
ATOM   8245  C  CD1 . TYR C  1 242 ? 10.403  -31.848 -35.907 1.00 26.34 ? 241 TYR C CD1 1 
ATOM   8246  C  CD2 . TYR C  1 242 ? 9.401   -30.901 -37.867 1.00 25.99 ? 241 TYR C CD2 1 
ATOM   8247  C  CE1 . TYR C  1 242 ? 9.380   -31.321 -35.109 1.00 27.12 ? 241 TYR C CE1 1 
ATOM   8248  C  CE2 . TYR C  1 242 ? 8.383   -30.371 -37.064 1.00 27.40 ? 241 TYR C CE2 1 
ATOM   8249  C  CZ  . TYR C  1 242 ? 8.379   -30.591 -35.697 1.00 26.72 ? 241 TYR C CZ  1 
ATOM   8250  O  OH  . TYR C  1 242 ? 7.394   -30.070 -34.891 1.00 30.29 ? 241 TYR C OH  1 
ATOM   8251  N  N   . THR C  1 243 ? 10.815  -35.391 -36.854 1.00 23.48 ? 242 THR C N   1 
ATOM   8252  C  CA  . THR C  1 243 ? 10.987  -36.344 -35.784 1.00 24.04 ? 242 THR C CA  1 
ATOM   8253  C  C   . THR C  1 243 ? 10.909  -37.773 -36.286 1.00 24.40 ? 242 THR C C   1 
ATOM   8254  O  O   . THR C  1 243 ? 11.680  -38.613 -35.876 1.00 24.67 ? 242 THR C O   1 
ATOM   8255  C  CB  . THR C  1 243 ? 9.905   -36.103 -34.702 1.00 24.29 ? 242 THR C CB  1 
ATOM   8256  O  OG1 . THR C  1 243 ? 10.162  -34.866 -34.027 1.00 25.16 ? 242 THR C OG1 1 
ATOM   8257  C  CG2 . THR C  1 243 ? 9.882   -37.201 -33.662 1.00 25.48 ? 242 THR C CG2 1 
ATOM   8258  N  N   A TRP C  1 244 ? 9.956   -38.039 -37.168 0.50 22.41 ? 243 TRP C N   1 
ATOM   8259  N  N   B TRP C  1 244 ? 9.952   -38.061 -37.165 0.50 23.90 ? 243 TRP C N   1 
ATOM   8260  C  CA  A TRP C  1 244 ? 9.656   -39.377 -37.597 0.50 21.29 ? 243 TRP C CA  1 
ATOM   8261  C  CA  B TRP C  1 244 ? 9.749   -39.432 -37.622 0.50 23.65 ? 243 TRP C CA  1 
ATOM   8262  C  C   A TRP C  1 244 ? 10.070  -39.602 -39.052 0.50 22.11 ? 243 TRP C C   1 
ATOM   8263  C  C   B TRP C  1 244 ? 10.102  -39.607 -39.063 0.50 23.44 ? 243 TRP C C   1 
ATOM   8264  O  O   A TRP C  1 244 ? 10.010  -38.674 -39.859 0.50 21.51 ? 243 TRP C O   1 
ATOM   8265  O  O   B TRP C  1 244 ? 10.004  -38.685 -39.866 0.50 22.64 ? 243 TRP C O   1 
ATOM   8266  C  CB  A TRP C  1 244 ? 8.136   -39.565 -37.477 0.50 19.81 ? 243 TRP C CB  1 
ATOM   8267  C  CB  B TRP C  1 244 ? 8.305   -39.897 -37.448 0.50 23.94 ? 243 TRP C CB  1 
ATOM   8268  C  CG  A TRP C  1 244 ? 7.514   -39.306 -36.054 0.50 17.77 ? 243 TRP C CG  1 
ATOM   8269  C  CG  B TRP C  1 244 ? 8.076   -40.568 -36.169 0.50 23.78 ? 243 TRP C CG  1 
ATOM   8270  C  CD1 A TRP C  1 244 ? 7.118   -38.092 -35.524 0.50 16.97 ? 243 TRP C CD1 1 
ATOM   8271  C  CD1 B TRP C  1 244 ? 8.447   -41.834 -35.797 0.50 23.75 ? 243 TRP C CD1 1 
ATOM   8272  C  CD2 A TRP C  1 244 ? 7.200   -40.287 -35.061 0.50 17.23 ? 243 TRP C CD2 1 
ATOM   8273  C  CD2 B TRP C  1 244 ? 7.392   -40.008 -35.083 0.50 22.60 ? 243 TRP C CD2 1 
ATOM   8274  N  NE1 A TRP C  1 244 ? 6.587   -38.265 -34.254 0.50 16.28 ? 243 TRP C NE1 1 
ATOM   8275  N  NE1 B TRP C  1 244 ? 8.021   -42.087 -34.511 0.50 23.26 ? 243 TRP C NE1 1 
ATOM   8276  C  CE2 A TRP C  1 244 ? 6.619   -39.603 -33.951 0.50 16.72 ? 243 TRP C CE2 1 
ATOM   8277  C  CE2 B TRP C  1 244 ? 7.373   -40.968 -34.051 0.50 23.11 ? 243 TRP C CE2 1 
ATOM   8278  C  CE3 A TRP C  1 244 ? 7.342   -41.682 -34.998 0.50 17.62 ? 243 TRP C CE3 1 
ATOM   8279  C  CE3 B TRP C  1 244 ? 6.792   -38.769 -34.869 0.50 22.71 ? 243 TRP C CE3 1 
ATOM   8280  C  CZ2 A TRP C  1 244 ? 6.199   -40.267 -32.807 0.50 16.57 ? 243 TRP C CZ2 1 
ATOM   8281  C  CZ2 B TRP C  1 244 ? 6.765   -40.720 -32.836 0.50 22.72 ? 243 TRP C CZ2 1 
ATOM   8282  C  CZ3 A TRP C  1 244 ? 6.938   -42.339 -33.845 0.50 17.52 ? 243 TRP C CZ3 1 
ATOM   8283  C  CZ3 B TRP C  1 244 ? 6.201   -38.535 -33.683 0.50 21.55 ? 243 TRP C CZ3 1 
ATOM   8284  C  CH2 A TRP C  1 244 ? 6.366   -41.631 -32.766 0.50 17.22 ? 243 TRP C CH2 1 
ATOM   8285  C  CH2 B TRP C  1 244 ? 6.182   -39.498 -32.678 0.50 21.86 ? 243 TRP C CH2 1 
ATOM   8286  N  N   . SER C  1 245 ? 10.470  -40.834 -39.380 1.00 23.36 ? 244 SER C N   1 
ATOM   8287  C  CA  . SER C  1 245 ? 10.753  -41.223 -40.732 1.00 24.53 ? 244 SER C CA  1 
ATOM   8288  C  C   . SER C  1 245 ? 9.482   -41.122 -41.592 1.00 25.62 ? 244 SER C C   1 
ATOM   8289  O  O   . SER C  1 245 ? 8.407   -41.546 -41.166 1.00 21.94 ? 244 SER C O   1 
ATOM   8290  C  CB  . SER C  1 245 ? 11.219  -42.663 -40.765 1.00 26.14 ? 244 SER C CB  1 
ATOM   8291  O  OG  . SER C  1 245 ? 11.297  -43.086 -42.103 1.00 26.89 ? 244 SER C OG  1 
ATOM   8292  N  N   . PRO C  1 246 ? 9.603   -40.547 -42.798 1.00 28.97 ? 245 PRO C N   1 
ATOM   8293  C  CA  . PRO C  1 246 ? 8.416   -40.467 -43.657 1.00 29.82 ? 245 PRO C CA  1 
ATOM   8294  C  C   . PRO C  1 246 ? 7.895   -41.846 -44.088 1.00 29.90 ? 245 PRO C C   1 
ATOM   8295  O  O   . PRO C  1 246 ? 6.770   -41.919 -44.568 1.00 31.42 ? 245 PRO C O   1 
ATOM   8296  C  CB  . PRO C  1 246 ? 8.913   -39.656 -44.871 1.00 32.27 ? 245 PRO C CB  1 
ATOM   8297  C  CG  . PRO C  1 246 ? 10.009  -38.793 -44.293 1.00 33.80 ? 245 PRO C CG  1 
ATOM   8298  C  CD  . PRO C  1 246 ? 10.716  -39.742 -43.345 1.00 32.00 ? 245 PRO C CD  1 
ATOM   8299  N  N   . GLU C  1 247 ? 8.688   -42.900 -43.915 1.00 28.62 ? 246 GLU C N   1 
ATOM   8300  C  CA  . GLU C  1 247 ? 8.278   -44.255 -44.229 1.00 31.53 ? 246 GLU C CA  1 
ATOM   8301  C  C   . GLU C  1 247 ? 7.712   -45.067 -43.028 1.00 28.03 ? 246 GLU C C   1 
ATOM   8302  O  O   . GLU C  1 247 ? 7.268   -46.186 -43.213 1.00 25.33 ? 246 GLU C O   1 
ATOM   8303  C  CB  . GLU C  1 247 ? 9.438   -45.048 -44.853 1.00 36.43 ? 246 GLU C CB  1 
ATOM   8304  C  CG  . GLU C  1 247 ? 10.070  -44.458 -46.135 1.00 43.50 ? 246 GLU C CG  1 
ATOM   8305  C  CD  . GLU C  1 247 ? 9.064   -43.760 -47.020 1.00 49.10 ? 246 GLU C CD  1 
ATOM   8306  O  OE1 . GLU C  1 247 ? 8.117   -44.423 -47.526 1.00 55.74 ? 246 GLU C OE1 1 
ATOM   8307  O  OE2 . GLU C  1 247 ? 9.238   -42.530 -47.198 1.00 57.11 ? 246 GLU C OE2 1 
ATOM   8308  N  N   . LYS C  1 248 ? 7.718   -44.515 -41.821 1.00 25.61 ? 247 LYS C N   1 
ATOM   8309  C  CA  . LYS C  1 248 ? 7.121   -45.225 -40.692 1.00 24.15 ? 247 LYS C CA  1 
ATOM   8310  C  C   . LYS C  1 248 ? 5.606   -45.340 -40.875 1.00 22.05 ? 247 LYS C C   1 
ATOM   8311  O  O   . LYS C  1 248 ? 4.924   -44.336 -41.100 1.00 21.17 ? 247 LYS C O   1 
ATOM   8312  C  CB  . LYS C  1 248 ? 7.408   -44.520 -39.361 1.00 25.41 ? 247 LYS C CB  1 
ATOM   8313  C  CG  . LYS C  1 248 ? 6.655   -45.240 -38.248 1.00 26.40 ? 247 LYS C CG  1 
ATOM   8314  C  CD  . LYS C  1 248 ? 7.070   -44.901 -36.854 1.00 29.46 ? 247 LYS C CD  1 
ATOM   8315  C  CE  . LYS C  1 248 ? 6.187   -45.645 -35.858 1.00 30.71 ? 247 LYS C CE  1 
ATOM   8316  N  NZ  . LYS C  1 248 ? 6.489   -47.097 -35.857 1.00 32.45 ? 247 LYS C NZ  1 
ATOM   8317  N  N   . VAL C  1 249 ? 5.085   -46.546 -40.742 1.00 21.04 ? 248 VAL C N   1 
ATOM   8318  C  CA  . VAL C  1 249 ? 3.632   -46.789 -40.839 1.00 20.94 ? 248 VAL C CA  1 
ATOM   8319  C  C   . VAL C  1 249 ? 3.018   -46.604 -39.474 1.00 20.07 ? 248 VAL C C   1 
ATOM   8320  O  O   . VAL C  1 249 ? 3.411   -47.292 -38.533 1.00 20.56 ? 248 VAL C O   1 
ATOM   8321  C  CB  . VAL C  1 249 ? 3.334   -48.197 -41.371 1.00 21.86 ? 248 VAL C CB  1 
ATOM   8322  C  CG1 . VAL C  1 249 ? 1.840   -48.454 -41.388 1.00 22.52 ? 248 VAL C CG1 1 
ATOM   8323  C  CG2 . VAL C  1 249 ? 3.918   -48.352 -42.761 1.00 22.98 ? 248 VAL C CG2 1 
ATOM   8324  N  N   . PHE C  1 250 ? 2.119   -45.616 -39.347 1.00 18.64 ? 249 PHE C N   1 
ATOM   8325  C  CA  . PHE C  1 250 ? 1.428   -45.348 -38.081 1.00 18.01 ? 249 PHE C CA  1 
ATOM   8326  C  C   . PHE C  1 250 ? 0.121   -46.101 -37.970 1.00 18.14 ? 249 PHE C C   1 
ATOM   8327  O  O   . PHE C  1 250 ? -0.297  -46.483 -36.870 1.00 17.59 ? 249 PHE C O   1 
ATOM   8328  C  CB  . PHE C  1 250 ? 1.121   -43.869 -37.947 1.00 17.72 ? 249 PHE C CB  1 
ATOM   8329  C  CG  . PHE C  1 250 ? 2.332   -43.049 -37.655 1.00 17.95 ? 249 PHE C CG  1 
ATOM   8330  C  CD1 . PHE C  1 250 ? 2.912   -43.096 -36.392 1.00 18.00 ? 249 PHE C CD1 1 
ATOM   8331  C  CD2 . PHE C  1 250 ? 2.903   -42.256 -38.633 1.00 18.47 ? 249 PHE C CD2 1 
ATOM   8332  C  CE1 . PHE C  1 250 ? 4.049   -42.354 -36.114 1.00 17.88 ? 249 PHE C CE1 1 
ATOM   8333  C  CE2 . PHE C  1 250 ? 4.045   -41.521 -38.365 1.00 18.00 ? 249 PHE C CE2 1 
ATOM   8334  C  CZ  . PHE C  1 250 ? 4.610   -41.574 -37.100 1.00 17.58 ? 249 PHE C CZ  1 
ATOM   8335  N  N   . VAL C  1 251 ? -0.527  -46.312 -39.109 1.00 17.55 ? 250 VAL C N   1 
ATOM   8336  C  CA  . VAL C  1 251 ? -1.800  -47.021 -39.168 1.00 17.51 ? 250 VAL C CA  1 
ATOM   8337  C  C   . VAL C  1 251 ? -1.731  -48.034 -40.301 1.00 18.16 ? 250 VAL C C   1 
ATOM   8338  O  O   . VAL C  1 251 ? -1.494  -47.704 -41.464 1.00 18.86 ? 250 VAL C O   1 
ATOM   8339  C  CB  . VAL C  1 251 ? -2.980  -46.066 -39.400 1.00 17.16 ? 250 VAL C CB  1 
ATOM   8340  C  CG1 . VAL C  1 251 ? -4.283  -46.820 -39.619 1.00 17.43 ? 250 VAL C CG1 1 
ATOM   8341  C  CG2 . VAL C  1 251 ? -3.135  -45.116 -38.218 1.00 17.93 ? 250 VAL C CG2 1 
ATOM   8342  N  N   . GLN C  1 252 ? -1.968  -49.287 -39.962 1.00 19.29 ? 251 GLN C N   1 
ATOM   8343  C  CA  . GLN C  1 252 ? -2.068  -50.356 -40.949 1.00 20.40 ? 251 GLN C CA  1 
ATOM   8344  C  C   . GLN C  1 252 ? -3.470  -50.969 -40.904 1.00 21.22 ? 251 GLN C C   1 
ATOM   8345  O  O   . GLN C  1 252 ? -4.064  -51.134 -39.836 1.00 20.57 ? 251 GLN C O   1 
ATOM   8346  C  CB  . GLN C  1 252 ? -0.948  -51.370 -40.751 1.00 22.67 ? 251 GLN C CB  1 
ATOM   8347  C  CG  . GLN C  1 252 ? -0.997  -52.579 -41.668 1.00 25.51 ? 251 GLN C CG  1 
ATOM   8348  C  CD  . GLN C  1 252 ? 0.253   -53.447 -41.557 1.00 28.29 ? 251 GLN C CD  1 
ATOM   8349  O  OE1 . GLN C  1 252 ? 0.980   -53.586 -42.513 1.00 33.30 ? 251 GLN C OE1 1 
ATOM   8350  N  NE2 . GLN C  1 252 ? 0.521   -53.982 -40.402 1.00 29.23 ? 251 GLN C NE2 1 
ATOM   8351  N  N   . THR C  1 253 ? -4.011  -51.254 -42.091 1.00 22.04 ? 252 THR C N   1 
ATOM   8352  C  CA  . THR C  1 253 ? -5.298  -51.934 -42.226 1.00 23.59 ? 252 THR C CA  1 
ATOM   8353  C  C   . THR C  1 253 ? -5.075  -53.076 -43.228 1.00 25.22 ? 252 THR C C   1 
ATOM   8354  O  O   . THR C  1 253 ? -4.009  -53.158 -43.818 1.00 24.55 ? 252 THR C O   1 
ATOM   8355  C  CB  . THR C  1 253 ? -6.407  -50.982 -42.729 1.00 24.40 ? 252 THR C CB  1 
ATOM   8356  O  OG1 . THR C  1 253 ? -6.351  -50.905 -44.154 1.00 25.48 ? 252 THR C OG1 1 
ATOM   8357  C  CG2 . THR C  1 253 ? -6.260  -49.562 -42.158 1.00 23.72 ? 252 THR C CG2 1 
ATOM   8358  N  N   . PRO C  1 254 ? -6.080  -53.934 -43.446 1.00 27.22 ? 253 PRO C N   1 
ATOM   8359  C  CA  . PRO C  1 254 ? -5.900  -55.005 -44.427 1.00 30.47 ? 253 PRO C CA  1 
ATOM   8360  C  C   . PRO C  1 254 ? -5.667  -54.526 -45.862 1.00 32.27 ? 253 PRO C C   1 
ATOM   8361  O  O   . PRO C  1 254 ? -5.072  -55.268 -46.653 1.00 34.22 ? 253 PRO C O   1 
ATOM   8362  C  CB  . PRO C  1 254 ? -7.215  -55.805 -44.334 1.00 30.75 ? 253 PRO C CB  1 
ATOM   8363  C  CG  . PRO C  1 254 ? -7.821  -55.418 -43.017 1.00 30.42 ? 253 PRO C CG  1 
ATOM   8364  C  CD  . PRO C  1 254 ? -7.418  -53.978 -42.833 1.00 28.67 ? 253 PRO C CD  1 
ATOM   8365  N  N   . THR C  1 255 ? -6.096  -53.309 -46.193 1.00 31.90 ? 254 THR C N   1 
ATOM   8366  C  CA  . THR C  1 255 ? -6.028  -52.823 -47.570 1.00 33.32 ? 254 THR C CA  1 
ATOM   8367  C  C   . THR C  1 255 ? -5.194  -51.583 -47.801 1.00 31.64 ? 254 THR C C   1 
ATOM   8368  O  O   . THR C  1 255 ? -5.005  -51.209 -48.954 1.00 31.76 ? 254 THR C O   1 
ATOM   8369  C  CB  . THR C  1 255 ? -7.430  -52.499 -48.098 1.00 36.28 ? 254 THR C CB  1 
ATOM   8370  O  OG1 . THR C  1 255 ? -8.070  -51.580 -47.202 1.00 37.12 ? 254 THR C OG1 1 
ATOM   8371  C  CG2 . THR C  1 255 ? -8.264  -53.785 -48.208 1.00 38.91 ? 254 THR C CG2 1 
ATOM   8372  N  N   . ILE C  1 256 ? -4.677  -50.948 -46.748 1.00 27.32 ? 255 ILE C N   1 
ATOM   8373  C  CA  . ILE C  1 256 ? -3.937  -49.731 -46.918 1.00 26.04 ? 255 ILE C CA  1 
ATOM   8374  C  C   . ILE C  1 256 ? -3.082  -49.411 -45.692 1.00 25.54 ? 255 ILE C C   1 
ATOM   8375  O  O   . ILE C  1 256 ? -3.455  -49.750 -44.558 1.00 25.82 ? 255 ILE C O   1 
ATOM   8376  C  CB  . ILE C  1 256 ? -4.932  -48.586 -47.266 1.00 27.26 ? 255 ILE C CB  1 
ATOM   8377  C  CG1 . ILE C  1 256 ? -4.209  -47.345 -47.717 1.00 28.22 ? 255 ILE C CG1 1 
ATOM   8378  C  CG2 . ILE C  1 256 ? -5.851  -48.265 -46.088 1.00 28.52 ? 255 ILE C CG2 1 
ATOM   8379  C  CD1 . ILE C  1 256 ? -5.160  -46.299 -48.268 1.00 28.42 ? 255 ILE C CD1 1 
ATOM   8380  N  N   A ASN C  1 257 ? -1.942  -48.775 -45.933 0.50 24.58 ? 256 ASN C N   1 
ATOM   8381  N  N   B ASN C  1 257 ? -1.925  -48.791 -45.939 0.50 24.61 ? 256 ASN C N   1 
ATOM   8382  C  CA  A ASN C  1 257 ? -1.060  -48.292 -44.893 0.50 24.05 ? 256 ASN C CA  1 
ATOM   8383  C  CA  B ASN C  1 257 ? -1.032  -48.293 -44.902 0.50 24.07 ? 256 ASN C CA  1 
ATOM   8384  C  C   A ASN C  1 257 ? -1.078  -46.777 -44.889 0.50 23.09 ? 256 ASN C C   1 
ATOM   8385  C  C   B ASN C  1 257 ? -1.092  -46.768 -44.889 0.50 23.07 ? 256 ASN C C   1 
ATOM   8386  O  O   A ASN C  1 257 ? -1.300  -46.184 -45.943 0.50 24.15 ? 256 ASN C O   1 
ATOM   8387  O  O   B ASN C  1 257 ? -1.297  -46.153 -45.945 0.50 23.98 ? 256 ASN C O   1 
ATOM   8388  C  CB  A ASN C  1 257 ? 0.336   -48.781 -45.198 0.50 24.77 ? 256 ASN C CB  1 
ATOM   8389  C  CB  B ASN C  1 257 ? 0.420   -48.622 -45.228 0.50 24.89 ? 256 ASN C CB  1 
ATOM   8390  C  CG  A ASN C  1 257 ? 0.450   -50.286 -45.034 0.50 26.02 ? 256 ASN C CG  1 
ATOM   8391  C  CG  B ASN C  1 257 ? 0.822   -50.030 -44.903 0.50 26.43 ? 256 ASN C CG  1 
ATOM   8392  O  OD1 A ASN C  1 257 ? 0.036   -50.813 -44.015 0.50 26.78 ? 256 ASN C OD1 1 
ATOM   8393  O  OD1 B ASN C  1 257 ? 0.088   -50.792 -44.276 0.50 26.71 ? 256 ASN C OD1 1 
ATOM   8394  N  ND2 A ASN C  1 257 ? 0.989   -50.977 -46.039 0.50 27.58 ? 256 ASN C ND2 1 
ATOM   8395  N  ND2 B ASN C  1 257 ? 2.037   -50.376 -45.340 0.50 27.55 ? 256 ASN C ND2 1 
ATOM   8396  N  N   . TYR C  1 258 ? -0.877  -46.161 -43.728 1.00 20.37 ? 257 TYR C N   1 
ATOM   8397  C  CA  . TYR C  1 258 ? -0.743  -44.710 -43.638 1.00 18.85 ? 257 TYR C CA  1 
ATOM   8398  C  C   . TYR C  1 258 ? 0.526   -44.329 -42.889 1.00 18.39 ? 257 TYR C C   1 
ATOM   8399  O  O   . TYR C  1 258 ? 0.706   -44.691 -41.708 1.00 18.03 ? 257 TYR C O   1 
ATOM   8400  C  CB  . TYR C  1 258 ? -1.930  -44.054 -42.958 1.00 18.17 ? 257 TYR C CB  1 
ATOM   8401  C  CG  . TYR C  1 258 ? -3.283  -44.375 -43.562 1.00 17.51 ? 257 TYR C CG  1 
ATOM   8402  C  CD1 . TYR C  1 258 ? -3.793  -43.652 -44.639 1.00 17.81 ? 257 TYR C CD1 1 
ATOM   8403  C  CD2 . TYR C  1 258 ? -4.069  -45.367 -43.033 1.00 18.39 ? 257 TYR C CD2 1 
ATOM   8404  C  CE1 . TYR C  1 258 ? -5.034  -43.940 -45.183 1.00 17.58 ? 257 TYR C CE1 1 
ATOM   8405  C  CE2 . TYR C  1 258 ? -5.311  -45.665 -43.577 1.00 18.41 ? 257 TYR C CE2 1 
ATOM   8406  C  CZ  . TYR C  1 258 ? -5.786  -44.948 -44.644 1.00 18.00 ? 257 TYR C CZ  1 
ATOM   8407  O  OH  . TYR C  1 258 ? -7.030  -45.289 -45.156 1.00 18.80 ? 257 TYR C OH  1 
ATOM   8408  N  N   . THR C  1 259 ? 1.388   -43.603 -43.610 1.00 17.64 ? 258 THR C N   1 
ATOM   8409  C  CA  . THR C  1 259 ? 2.561   -42.929 -43.073 1.00 16.79 ? 258 THR C CA  1 
ATOM   8410  C  C   . THR C  1 259 ? 2.258   -41.432 -42.958 1.00 16.65 ? 258 THR C C   1 
ATOM   8411  O  O   . THR C  1 259 ? 1.172   -40.963 -43.330 1.00 16.48 ? 258 THR C O   1 
ATOM   8412  C  CB  . THR C  1 259 ? 3.778   -43.097 -44.006 1.00 17.47 ? 258 THR C CB  1 
ATOM   8413  O  OG1 . THR C  1 259 ? 3.602   -42.312 -45.197 1.00 17.62 ? 258 THR C OG1 1 
ATOM   8414  C  CG2 . THR C  1 259 ? 3.989   -44.556 -44.417 1.00 18.18 ? 258 THR C CG2 1 
ATOM   8415  N  N   . LEU C  1 260 ? 3.206   -40.650 -42.468 1.00 16.75 ? 259 LEU C N   1 
ATOM   8416  C  CA  . LEU C  1 260 ? 2.995   -39.192 -42.392 1.00 17.03 ? 259 LEU C CA  1 
ATOM   8417  C  C   . LEU C  1 260 ? 2.967   -38.508 -43.754 1.00 17.06 ? 259 LEU C C   1 
ATOM   8418  O  O   . LEU C  1 260 ? 2.656   -37.319 -43.843 1.00 17.68 ? 259 LEU C O   1 
ATOM   8419  C  CB  . LEU C  1 260 ? 4.025   -38.516 -41.477 1.00 18.09 ? 259 LEU C CB  1 
ATOM   8420  C  CG  . LEU C  1 260 ? 5.489   -38.584 -41.888 1.00 19.75 ? 259 LEU C CG  1 
ATOM   8421  C  CD1 . LEU C  1 260 ? 5.832   -37.507 -42.904 1.00 20.69 ? 259 LEU C CD1 1 
ATOM   8422  C  CD2 . LEU C  1 260 ? 6.319   -38.393 -40.616 1.00 21.51 ? 259 LEU C CD2 1 
ATOM   8423  N  N   . ARG C  1 261 ? 3.292   -39.249 -44.808 1.00 16.85 ? 260 ARG C N   1 
ATOM   8424  C  CA  . ARG C  1 261 ? 3.126   -38.744 -46.181 1.00 16.64 ? 260 ARG C CA  1 
ATOM   8425  C  C   . ARG C  1 261 ? 1.727   -38.994 -46.728 1.00 16.17 ? 260 ARG C C   1 
ATOM   8426  O  O   . ARG C  1 261 ? 1.445   -38.638 -47.879 1.00 16.76 ? 260 ARG C O   1 
ATOM   8427  C  CB  . ARG C  1 261 ? 4.181   -39.338 -47.097 1.00 17.53 ? 260 ARG C CB  1 
ATOM   8428  C  CG  . ARG C  1 261 ? 5.621   -38.974 -46.702 1.00 18.68 ? 260 ARG C CG  1 
ATOM   8429  C  CD  . ARG C  1 261 ? 6.573   -39.089 -47.904 1.00 19.72 ? 260 ARG C CD  1 
ATOM   8430  N  NE  . ARG C  1 261 ? 6.680   -40.459 -48.441 1.00 19.81 ? 260 ARG C NE  1 
ATOM   8431  C  CZ  . ARG C  1 261 ? 7.299   -40.823 -49.554 1.00 20.55 ? 260 ARG C CZ  1 
ATOM   8432  N  NH1 . ARG C  1 261 ? 7.833   -39.922 -50.359 1.00 21.24 ? 260 ARG C NH1 1 
ATOM   8433  N  NH2 . ARG C  1 261 ? 7.370   -42.110 -49.882 1.00 21.62 ? 260 ARG C NH2 1 
ATOM   8434  N  N   . ASP C  1 262 ? 0.859   -39.574 -45.922 1.00 15.48 ? 261 ASP C N   1 
ATOM   8435  C  CA  . ASP C  1 262 ? -0.448  -40.027 -46.375 1.00 16.03 ? 261 ASP C CA  1 
ATOM   8436  C  C   . ASP C  1 262 ? -1.613  -39.395 -45.636 1.00 16.27 ? 261 ASP C C   1 
ATOM   8437  O  O   . ASP C  1 262 ? -2.741  -39.955 -45.630 1.00 15.65 ? 261 ASP C O   1 
ATOM   8438  C  CB  . ASP C  1 262 ? -0.547  -41.546 -46.223 1.00 16.53 ? 261 ASP C CB  1 
ATOM   8439  C  CG  . ASP C  1 262 ? 0.496   -42.293 -47.020 1.00 17.53 ? 261 ASP C CG  1 
ATOM   8440  O  OD1 . ASP C  1 262 ? 0.677   -42.014 -48.223 1.00 17.78 ? 261 ASP C OD1 1 
ATOM   8441  O  OD2 . ASP C  1 262 ? 1.138   -43.204 -46.439 1.00 18.99 ? 261 ASP C OD2 1 
ATOM   8442  N  N   . TYR C  1 263 ? -1.396  -38.221 -45.026 1.00 16.05 ? 262 TYR C N   1 
ATOM   8443  C  CA  . TYR C  1 263 ? -2.472  -37.607 -44.251 1.00 16.09 ? 262 TYR C CA  1 
ATOM   8444  C  C   . TYR C  1 263 ? -3.689  -37.222 -45.072 1.00 16.37 ? 262 TYR C C   1 
ATOM   8445  O  O   . TYR C  1 263 ? -4.823  -37.320 -44.576 1.00 15.87 ? 262 TYR C O   1 
ATOM   8446  C  CB  . TYR C  1 263 ? -1.982  -36.397 -43.434 1.00 16.15 ? 262 TYR C CB  1 
ATOM   8447  C  CG  . TYR C  1 263 ? -1.016  -36.736 -42.307 1.00 16.25 ? 262 TYR C CG  1 
ATOM   8448  C  CD1 . TYR C  1 263 ? -1.107  -37.932 -41.591 1.00 17.57 ? 262 TYR C CD1 1 
ATOM   8449  C  CD2 . TYR C  1 263 ? -0.024  -35.836 -41.931 1.00 17.55 ? 262 TYR C CD2 1 
ATOM   8450  C  CE1 . TYR C  1 263 ? -0.245  -38.213 -40.547 1.00 17.67 ? 262 TYR C CE1 1 
ATOM   8451  C  CE2 . TYR C  1 263 ? 0.863   -36.123 -40.905 1.00 16.59 ? 262 TYR C CE2 1 
ATOM   8452  C  CZ  . TYR C  1 263 ? 0.732   -37.297 -40.207 1.00 17.42 ? 262 TYR C CZ  1 
ATOM   8453  O  OH  . TYR C  1 263 ? 1.605   -37.601 -39.182 1.00 16.70 ? 262 TYR C OH  1 
ATOM   8454  N  N   . ARG C  1 264 ? -3.504  -36.774 -46.307 1.00 16.60 ? 263 ARG C N   1 
ATOM   8455  C  CA  . ARG C  1 264 ? -4.683  -36.398 -47.113 1.00 18.09 ? 263 ARG C CA  1 
ATOM   8456  C  C   . ARG C  1 264 ? -5.616  -37.608 -47.316 1.00 17.64 ? 263 ARG C C   1 
ATOM   8457  O  O   . ARG C  1 264 ? -6.829  -37.498 -47.103 1.00 17.14 ? 263 ARG C O   1 
ATOM   8458  C  CB  . ARG C  1 264 ? -4.269  -35.756 -48.445 1.00 19.29 ? 263 ARG C CB  1 
ATOM   8459  C  CG  . ARG C  1 264 ? -5.415  -35.056 -49.154 1.00 21.43 ? 263 ARG C CG  1 
ATOM   8460  C  CD  . ARG C  1 264 ? -4.935  -34.459 -50.462 1.00 23.18 ? 263 ARG C CD  1 
ATOM   8461  N  NE  . ARG C  1 264 ? -5.883  -33.511 -51.027 1.00 25.22 ? 263 ARG C NE  1 
ATOM   8462  C  CZ  . ARG C  1 264 ? -6.902  -33.804 -51.836 1.00 28.36 ? 263 ARG C CZ  1 
ATOM   8463  N  NH1 . ARG C  1 264 ? -7.180  -35.063 -52.172 1.00 27.96 ? 263 ARG C NH1 1 
ATOM   8464  N  NH2 . ARG C  1 264 ? -7.676  -32.815 -52.312 1.00 29.41 ? 263 ARG C NH2 1 
ATOM   8465  N  N   . LYS C  1 265 ? -5.043  -38.761 -47.668 1.00 17.52 ? 264 LYS C N   1 
ATOM   8466  C  CA  . LYS C  1 265 ? -5.797  -40.026 -47.815 1.00 18.92 ? 264 LYS C CA  1 
ATOM   8467  C  C   . LYS C  1 265 ? -6.432  -40.467 -46.520 1.00 18.08 ? 264 LYS C C   1 
ATOM   8468  O  O   . LYS C  1 265 ? -7.560  -40.953 -46.514 1.00 18.65 ? 264 LYS C O   1 
ATOM   8469  C  CB  . LYS C  1 265 ? -4.862  -41.221 -48.203 1.00 20.12 ? 264 LYS C CB  1 
ATOM   8470  C  CG  . LYS C  1 265 ? -4.152  -41.096 -49.490 1.00 21.96 ? 264 LYS C CG  1 
ATOM   8471  C  CD  . LYS C  1 265 ? -3.640  -42.436 -49.990 1.00 21.42 ? 264 LYS C CD  1 
ATOM   8472  C  CE  . LYS C  1 265 ? -2.562  -43.064 -49.155 1.00 21.05 ? 264 LYS C CE  1 
ATOM   8473  N  NZ  . LYS C  1 265 ? -1.915  -44.114 -49.979 1.00 19.95 ? 264 LYS C NZ  1 
ATOM   8474  N  N   . PHE C  1 266 ? -5.665  -40.378 -45.440 1.00 17.31 ? 265 PHE C N   1 
ATOM   8475  C  CA  . PHE C  1 266 ? -6.141  -40.722 -44.087 1.00 17.29 ? 265 PHE C CA  1 
ATOM   8476  C  C   . PHE C  1 266 ? -7.402  -39.932 -43.733 1.00 16.68 ? 265 PHE C C   1 
ATOM   8477  O  O   . PHE C  1 266 ? -8.431  -40.499 -43.366 1.00 16.99 ? 265 PHE C O   1 
ATOM   8478  C  CB  . PHE C  1 266 ? -5.035  -40.446 -43.072 1.00 17.09 ? 265 PHE C CB  1 
ATOM   8479  C  CG  . PHE C  1 266 ? -5.437  -40.688 -41.650 1.00 17.45 ? 265 PHE C CG  1 
ATOM   8480  C  CD1 . PHE C  1 266 ? -5.527  -41.974 -41.161 1.00 17.98 ? 265 PHE C CD1 1 
ATOM   8481  C  CD2 . PHE C  1 266 ? -5.736  -39.628 -40.822 1.00 17.78 ? 265 PHE C CD2 1 
ATOM   8482  C  CE1 . PHE C  1 266 ? -5.925  -42.201 -39.840 1.00 18.48 ? 265 PHE C CE1 1 
ATOM   8483  C  CE2 . PHE C  1 266 ? -6.152  -39.845 -39.518 1.00 18.76 ? 265 PHE C CE2 1 
ATOM   8484  C  CZ  . PHE C  1 266 ? -6.228  -41.137 -39.021 1.00 18.31 ? 265 PHE C CZ  1 
ATOM   8485  N  N   . PHE C  1 267 ? -7.355  -38.629 -43.942 1.00 16.58 ? 266 PHE C N   1 
ATOM   8486  C  CA  . PHE C  1 267 ? -8.533  -37.799 -43.645 1.00 17.16 ? 266 PHE C CA  1 
ATOM   8487  C  C   . PHE C  1 267 ? -9.732  -38.115 -44.541 1.00 18.15 ? 266 PHE C C   1 
ATOM   8488  O  O   . PHE C  1 267 ? -10.891 -38.121 -44.088 1.00 18.98 ? 266 PHE C O   1 
ATOM   8489  C  CB  . PHE C  1 267 ? -8.161  -36.324 -43.675 1.00 16.90 ? 266 PHE C CB  1 
ATOM   8490  C  CG  . PHE C  1 267 ? -7.451  -35.865 -42.425 1.00 17.24 ? 266 PHE C CG  1 
ATOM   8491  C  CD1 . PHE C  1 267 ? -8.108  -35.887 -41.202 1.00 16.95 ? 266 PHE C CD1 1 
ATOM   8492  C  CD2 . PHE C  1 267 ? -6.123  -35.423 -42.470 1.00 16.65 ? 266 PHE C CD2 1 
ATOM   8493  C  CE1 . PHE C  1 267 ? -7.479  -35.461 -40.055 1.00 16.72 ? 266 PHE C CE1 1 
ATOM   8494  C  CE2 . PHE C  1 267 ? -5.488  -34.984 -41.324 1.00 17.13 ? 266 PHE C CE2 1 
ATOM   8495  C  CZ  . PHE C  1 267 ? -6.162  -34.985 -40.113 1.00 16.71 ? 266 PHE C CZ  1 
ATOM   8496  N  N   . GLN C  1 268 ? -9.481  -38.384 -45.815 1.00 18.48 ? 267 GLN C N   1 
ATOM   8497  C  CA  . GLN C  1 268 ? -10.552 -38.839 -46.695 1.00 20.19 ? 267 GLN C CA  1 
ATOM   8498  C  C   . GLN C  1 268 ? -11.151 -40.135 -46.181 1.00 20.16 ? 267 GLN C C   1 
ATOM   8499  O  O   . GLN C  1 268 ? -12.373 -40.286 -46.172 1.00 20.22 ? 267 GLN C O   1 
ATOM   8500  C  CB  . GLN C  1 268 ? -10.053 -39.047 -48.129 1.00 21.09 ? 267 GLN C CB  1 
ATOM   8501  C  CG  . GLN C  1 268 ? -9.651  -37.767 -48.835 1.00 23.34 ? 267 GLN C CG  1 
ATOM   8502  C  CD  . GLN C  1 268 ? -9.089  -38.030 -50.231 1.00 25.33 ? 267 GLN C CD  1 
ATOM   8503  O  OE1 . GLN C  1 268 ? -8.223  -38.896 -50.433 1.00 27.52 ? 267 GLN C OE1 1 
ATOM   8504  N  NE2 . GLN C  1 268 ? -9.590  -37.297 -51.205 1.00 28.21 ? 267 GLN C NE2 1 
ATOM   8505  N  N   . ASP C  1 269 ? -10.296 -41.078 -45.804 1.00 19.31 ? 268 ASP C N   1 
ATOM   8506  C  CA  . ASP C  1 269 ? -10.741 -42.423 -45.526 1.00 19.97 ? 268 ASP C CA  1 
ATOM   8507  C  C   . ASP C  1 269 ? -11.439 -42.569 -44.175 1.00 21.19 ? 268 ASP C C   1 
ATOM   8508  O  O   . ASP C  1 269 ? -12.213 -43.503 -43.992 1.00 21.90 ? 268 ASP C O   1 
ATOM   8509  C  CB  . ASP C  1 269 ? -9.574  -43.407 -45.621 1.00 20.22 ? 268 ASP C CB  1 
ATOM   8510  C  CG  . ASP C  1 269 ? -9.075  -43.590 -47.058 1.00 19.85 ? 268 ASP C CG  1 
ATOM   8511  O  OD1 . ASP C  1 269 ? -9.763  -43.090 -47.982 1.00 19.54 ? 268 ASP C OD1 1 
ATOM   8512  O  OD2 . ASP C  1 269 ? -7.976  -44.189 -47.254 1.00 19.92 ? 268 ASP C OD2 1 
ATOM   8513  N  N   . ILE C  1 270 ? -11.163 -41.660 -43.246 1.00 20.91 ? 269 ILE C N   1 
ATOM   8514  C  CA  . ILE C  1 270 ? -11.895 -41.650 -41.997 1.00 21.68 ? 269 ILE C CA  1 
ATOM   8515  C  C   . ILE C  1 270 ? -13.176 -40.823 -42.068 1.00 23.12 ? 269 ILE C C   1 
ATOM   8516  O  O   . ILE C  1 270 ? -13.945 -40.819 -41.136 1.00 25.24 ? 269 ILE C O   1 
ATOM   8517  C  CB  . ILE C  1 270 ? -11.041 -41.205 -40.802 1.00 20.60 ? 269 ILE C CB  1 
ATOM   8518  C  CG1 . ILE C  1 270 ? -10.712 -39.714 -40.882 1.00 19.69 ? 269 ILE C CG1 1 
ATOM   8519  C  CG2 . ILE C  1 270 ? -9.802  -42.096 -40.685 1.00 20.40 ? 269 ILE C CG2 1 
ATOM   8520  C  CD1 . ILE C  1 270 ? -9.887  -39.237 -39.729 1.00 19.21 ? 269 ILE C CD1 1 
ATOM   8521  N  N   . GLY C  1 271 ? -13.406 -40.147 -43.175 1.00 24.21 ? 270 GLY C N   1 
ATOM   8522  C  CA  . GLY C  1 271 ? -14.601 -39.348 -43.384 1.00 24.87 ? 270 GLY C CA  1 
ATOM   8523  C  C   . GLY C  1 271 ? -14.502 -38.004 -42.688 1.00 26.00 ? 270 GLY C C   1 
ATOM   8524  O  O   . GLY C  1 271 ? -15.515 -37.479 -42.238 1.00 26.45 ? 270 GLY C O   1 
ATOM   8525  N  N   . PHE C  1 272 ? -13.301 -37.413 -42.658 1.00 23.97 ? 271 PHE C N   1 
ATOM   8526  C  CA  . PHE C  1 272 ? -13.114 -36.112 -42.050 1.00 23.74 ? 271 PHE C CA  1 
ATOM   8527  C  C   . PHE C  1 272 ? -12.166 -35.233 -42.868 1.00 23.77 ? 271 PHE C C   1 
ATOM   8528  O  O   . PHE C  1 272 ? -11.037 -34.932 -42.463 1.00 21.09 ? 271 PHE C O   1 
ATOM   8529  C  CB  . PHE C  1 272 ? -12.623 -36.290 -40.611 1.00 23.25 ? 271 PHE C CB  1 
ATOM   8530  C  CG  . PHE C  1 272 ? -12.535 -34.999 -39.858 1.00 23.71 ? 271 PHE C CG  1 
ATOM   8531  C  CD1 . PHE C  1 272 ? -13.637 -34.160 -39.776 1.00 25.27 ? 271 PHE C CD1 1 
ATOM   8532  C  CD2 . PHE C  1 272 ? -11.364 -34.640 -39.223 1.00 24.52 ? 271 PHE C CD2 1 
ATOM   8533  C  CE1 . PHE C  1 272 ? -13.559 -32.959 -39.091 1.00 26.16 ? 271 PHE C CE1 1 
ATOM   8534  C  CE2 . PHE C  1 272 ? -11.276 -33.432 -38.562 1.00 24.71 ? 271 PHE C CE2 1 
ATOM   8535  C  CZ  . PHE C  1 272 ? -12.363 -32.598 -38.510 1.00 24.36 ? 271 PHE C CZ  1 
ATOM   8536  N  N   . GLU C  1 273 ? -12.656 -34.771 -44.013 1.00 25.49 ? 272 GLU C N   1 
ATOM   8537  C  CA  . GLU C  1 273 ? -11.846 -33.976 -44.937 1.00 26.71 ? 272 GLU C CA  1 
ATOM   8538  C  C   . GLU C  1 273 ? -11.371 -32.649 -44.359 1.00 25.26 ? 272 GLU C C   1 
ATOM   8539  O  O   . GLU C  1 273 ? -10.281 -32.174 -44.709 1.00 23.31 ? 272 GLU C O   1 
ATOM   8540  C  CB  . GLU C  1 273 ? -12.596 -33.794 -46.266 1.00 32.51 ? 272 GLU C CB  1 
ATOM   8541  C  CG  . GLU C  1 273 ? -12.680 -35.139 -46.993 1.00 37.19 ? 272 GLU C CG  1 
ATOM   8542  C  CD  . GLU C  1 273 ? -13.502 -35.142 -48.281 1.00 45.46 ? 272 GLU C CD  1 
ATOM   8543  O  OE1 . GLU C  1 273 ? -14.097 -34.094 -48.644 1.00 49.16 ? 272 GLU C OE1 1 
ATOM   8544  O  OE2 . GLU C  1 273 ? -13.546 -36.228 -48.928 1.00 50.20 ? 272 GLU C OE2 1 
ATOM   8545  N  N   . ASP C  1 274 ? -12.160 -32.049 -43.464 1.00 23.03 ? 273 ASP C N   1 
ATOM   8546  C  CA  . ASP C  1 274 ? -11.754 -30.787 -42.825 1.00 23.59 ? 273 ASP C CA  1 
ATOM   8547  C  C   . ASP C  1 274 ? -10.438 -30.928 -42.068 1.00 20.51 ? 273 ASP C C   1 
ATOM   8548  O  O   . ASP C  1 274 ? -9.708  -29.959 -41.913 1.00 20.50 ? 273 ASP C O   1 
ATOM   8549  C  CB  . ASP C  1 274 ? -12.808 -30.306 -41.826 1.00 25.13 ? 273 ASP C CB  1 
ATOM   8550  C  CG  . ASP C  1 274 ? -14.032 -29.669 -42.500 1.00 29.13 ? 273 ASP C CG  1 
ATOM   8551  O  OD1 . ASP C  1 274 ? -13.987 -29.360 -43.712 1.00 29.71 ? 273 ASP C OD1 1 
ATOM   8552  O  OD2 . ASP C  1 274 ? -15.022 -29.456 -41.768 1.00 31.53 ? 273 ASP C OD2 1 
ATOM   8553  N  N   . GLY C  1 275 ? -10.163 -32.116 -41.543 1.00 19.28 ? 274 GLY C N   1 
ATOM   8554  C  CA  . GLY C  1 275 ? -8.924  -32.340 -40.815 1.00 19.09 ? 274 GLY C CA  1 
ATOM   8555  C  C   . GLY C  1 275 ? -7.700  -32.076 -41.670 1.00 19.04 ? 274 GLY C C   1 
ATOM   8556  O  O   . GLY C  1 275 ? -6.673  -31.623 -41.167 1.00 19.03 ? 274 GLY C O   1 
ATOM   8557  N  N   . TRP C  1 276 ? -7.782  -32.407 -42.962 1.00 18.66 ? 275 TRP C N   1 
ATOM   8558  C  CA  . TRP C  1 276 ? -6.658  -32.165 -43.870 1.00 18.72 ? 275 TRP C CA  1 
ATOM   8559  C  C   . TRP C  1 276 ? -6.422  -30.676 -44.038 1.00 18.21 ? 275 TRP C C   1 
ATOM   8560  O  O   . TRP C  1 276 ? -5.277  -30.200 -44.044 1.00 17.30 ? 275 TRP C O   1 
ATOM   8561  C  CB  . TRP C  1 276 ? -6.914  -32.831 -45.230 1.00 19.54 ? 275 TRP C CB  1 
ATOM   8562  C  CG  . TRP C  1 276 ? -5.952  -32.396 -46.311 1.00 19.97 ? 275 TRP C CG  1 
ATOM   8563  C  CD1 . TRP C  1 276 ? -6.256  -31.711 -47.461 1.00 21.63 ? 275 TRP C CD1 1 
ATOM   8564  C  CD2 . TRP C  1 276 ? -4.552  -32.637 -46.358 1.00 19.65 ? 275 TRP C CD2 1 
ATOM   8565  N  NE1 . TRP C  1 276 ? -5.131  -31.513 -48.215 1.00 21.63 ? 275 TRP C NE1 1 
ATOM   8566  C  CE2 . TRP C  1 276 ? -4.065  -32.071 -47.556 1.00 20.47 ? 275 TRP C CE2 1 
ATOM   8567  C  CE3 . TRP C  1 276 ? -3.660  -33.264 -45.499 1.00 19.40 ? 275 TRP C CE3 1 
ATOM   8568  C  CZ2 . TRP C  1 276 ? -2.718  -32.121 -47.920 1.00 20.54 ? 275 TRP C CZ2 1 
ATOM   8569  C  CZ3 . TRP C  1 276 ? -2.310  -33.294 -45.851 1.00 20.22 ? 275 TRP C CZ3 1 
ATOM   8570  C  CH2 . TRP C  1 276 ? -1.857  -32.745 -47.054 1.00 19.94 ? 275 TRP C CH2 1 
ATOM   8571  N  N   . LEU C  1 277 ? -7.512  -29.939 -44.158 1.00 17.83 ? 276 LEU C N   1 
ATOM   8572  C  CA  . LEU C  1 277 ? -7.422  -28.490 -44.252 1.00 18.94 ? 276 LEU C CA  1 
ATOM   8573  C  C   . LEU C  1 277 ? -6.832  -27.893 -42.962 1.00 18.41 ? 276 LEU C C   1 
ATOM   8574  O  O   . LEU C  1 277 ? -5.954  -27.013 -43.013 1.00 18.77 ? 276 LEU C O   1 
ATOM   8575  C  CB  . LEU C  1 277 ? -8.792  -27.894 -44.564 1.00 19.98 ? 276 LEU C CB  1 
ATOM   8576  C  CG  . LEU C  1 277 ? -9.503  -28.415 -45.821 1.00 21.81 ? 276 LEU C CG  1 
ATOM   8577  C  CD1 . LEU C  1 277 ? -10.871 -27.762 -45.980 1.00 23.01 ? 276 LEU C CD1 1 
ATOM   8578  C  CD2 . LEU C  1 277 ? -8.650  -28.165 -47.058 1.00 22.68 ? 276 LEU C CD2 1 
ATOM   8579  N  N   . MET C  1 278 ? -7.241  -28.418 -41.822 1.00 18.22 ? 277 MET C N   1 
ATOM   8580  C  CA  . MET C  1 278 ? -6.644  -28.008 -40.531 1.00 18.19 ? 277 MET C CA  1 
ATOM   8581  C  C   . MET C  1 278 ? -5.147  -28.304 -40.443 1.00 17.40 ? 277 MET C C   1 
ATOM   8582  O  O   . MET C  1 278 ? -4.362  -27.482 -39.952 1.00 16.45 ? 277 MET C O   1 
ATOM   8583  C  CB  . MET C  1 278 ? -7.349  -28.696 -39.369 1.00 19.14 ? 277 MET C CB  1 
ATOM   8584  C  CG  . MET C  1 278 ? -8.801  -28.295 -39.154 1.00 20.50 ? 277 MET C CG  1 
ATOM   8585  S  SD  . MET C  1 278 ? -9.485  -29.397 -37.887 1.00 23.32 ? 277 MET C SD  1 
ATOM   8586  C  CE  . MET C  1 278 ? -11.177 -28.790 -37.833 1.00 25.97 ? 277 MET C CE  1 
ATOM   8587  N  N   . ARG C  1 279 ? -4.754  -29.483 -40.916 1.00 17.04 ? 278 ARG C N   1 
ATOM   8588  C  CA  . ARG C  1 279 ? -3.342  -29.845 -40.945 1.00 17.09 ? 278 ARG C CA  1 
ATOM   8589  C  C   . ARG C  1 279 ? -2.559  -28.910 -41.838 1.00 17.95 ? 278 ARG C C   1 
ATOM   8590  O  O   . ARG C  1 279 ? -1.478  -28.414 -41.446 1.00 17.76 ? 278 ARG C O   1 
ATOM   8591  C  CB  . ARG C  1 279 ? -3.153  -31.318 -41.358 1.00 16.89 ? 278 ARG C CB  1 
ATOM   8592  C  CG  . ARG C  1 279 ? -1.693  -31.771 -41.396 1.00 16.97 ? 278 ARG C CG  1 
ATOM   8593  C  CD  . ARG C  1 279 ? -1.035  -31.681 -40.029 1.00 16.65 ? 278 ARG C CD  1 
ATOM   8594  N  NE  . ARG C  1 279 ? 0.311   -32.252 -40.044 1.00 16.66 ? 278 ARG C NE  1 
ATOM   8595  C  CZ  . ARG C  1 279 ? 1.020   -32.531 -38.954 1.00 16.60 ? 278 ARG C CZ  1 
ATOM   8596  N  NH1 . ARG C  1 279 ? 0.526   -32.293 -37.743 1.00 16.49 ? 278 ARG C NH1 1 
ATOM   8597  N  NH2 . ARG C  1 279 ? 2.235   -33.033 -39.077 1.00 17.08 ? 278 ARG C NH2 1 
ATOM   8598  N  N   . GLN C  1 280 ? -3.083  -28.615 -43.022 1.00 19.10 ? 279 GLN C N   1 
ATOM   8599  C  CA  . GLN C  1 280 ? -2.420  -27.640 -43.899 1.00 20.89 ? 279 GLN C CA  1 
ATOM   8600  C  C   . GLN C  1 280 ? -2.298  -26.275 -43.236 1.00 20.27 ? 279 GLN C C   1 
ATOM   8601  O  O   . GLN C  1 280 ? -1.299  -25.608 -43.433 1.00 20.37 ? 279 GLN C O   1 
ATOM   8602  C  CB  . GLN C  1 280 ? -3.161  -27.469 -45.209 1.00 22.90 ? 279 GLN C CB  1 
ATOM   8603  C  CG  . GLN C  1 280 ? -3.090  -28.669 -46.111 1.00 26.31 ? 279 GLN C CG  1 
ATOM   8604  C  CD  . GLN C  1 280 ? -3.762  -28.370 -47.436 1.00 29.42 ? 279 GLN C CD  1 
ATOM   8605  O  OE1 . GLN C  1 280 ? -4.922  -27.943 -47.479 1.00 33.43 ? 279 GLN C OE1 1 
ATOM   8606  N  NE2 . GLN C  1 280 ? -3.045  -28.577 -48.515 1.00 32.60 ? 279 GLN C NE2 1 
ATOM   8607  N  N   . ASP C  1 281 ? -3.330  -25.853 -42.502 1.00 19.81 ? 280 ASP C N   1 
ATOM   8608  C  CA  . ASP C  1 281 ? -3.339  -24.532 -41.847 1.00 20.63 ? 280 ASP C CA  1 
ATOM   8609  C  C   . ASP C  1 281 ? -2.242  -24.443 -40.760 1.00 20.63 ? 280 ASP C C   1 
ATOM   8610  O  O   . ASP C  1 281 ? -1.769  -23.356 -40.441 1.00 21.71 ? 280 ASP C O   1 
ATOM   8611  C  CB  . ASP C  1 281 ? -4.663  -24.250 -41.104 1.00 21.88 ? 280 ASP C CB  1 
ATOM   8612  C  CG  . ASP C  1 281 ? -5.886  -24.109 -42.003 1.00 24.07 ? 280 ASP C CG  1 
ATOM   8613  O  OD1 . ASP C  1 281 ? -5.754  -23.866 -43.233 1.00 23.83 ? 280 ASP C OD1 1 
ATOM   8614  O  OD2 . ASP C  1 281 ? -7.015  -24.239 -41.416 1.00 25.58 ? 280 ASP C OD2 1 
ATOM   8615  N  N   . THR C  1 282 ? -1.937  -25.566 -40.119 1.00 18.45 ? 281 THR C N   1 
ATOM   8616  C  CA  . THR C  1 282 ? -1.171  -25.555 -38.888 1.00 17.88 ? 281 THR C CA  1 
ATOM   8617  C  C   . THR C  1 282 ? 0.230   -26.177 -38.968 1.00 19.01 ? 281 THR C C   1 
ATOM   8618  O  O   . THR C  1 282 ? 1.055   -25.908 -38.086 1.00 18.86 ? 281 THR C O   1 
ATOM   8619  C  CB  . THR C  1 282 ? -1.957  -26.240 -37.753 1.00 17.00 ? 281 THR C CB  1 
ATOM   8620  O  OG1 . THR C  1 282 ? -2.208  -27.612 -38.070 1.00 17.28 ? 281 THR C OG1 1 
ATOM   8621  C  CG2 . THR C  1 282 ? -3.258  -25.520 -37.515 1.00 16.79 ? 281 THR C CG2 1 
ATOM   8622  N  N   . GLU C  1 283 ? 0.495   -26.999 -39.988 1.00 20.09 ? 282 GLU C N   1 
ATOM   8623  C  CA  . GLU C  1 283 ? 1.749   -27.775 -40.046 1.00 21.33 ? 282 GLU C CA  1 
ATOM   8624  C  C   . GLU C  1 283 ? 3.002   -26.906 -40.113 1.00 21.59 ? 282 GLU C C   1 
ATOM   8625  O  O   . GLU C  1 283 ? 4.082   -27.349 -39.730 1.00 20.56 ? 282 GLU C O   1 
ATOM   8626  C  CB  . GLU C  1 283 ? 1.738   -28.773 -41.238 1.00 23.00 ? 282 GLU C CB  1 
ATOM   8627  C  CG  . GLU C  1 283 ? 1.723   -28.106 -42.597 1.00 26.65 ? 282 GLU C CG  1 
ATOM   8628  C  CD  . GLU C  1 283 ? 1.633   -29.081 -43.771 1.00 33.09 ? 282 GLU C CD  1 
ATOM   8629  O  OE1 . GLU C  1 283 ? 1.623   -30.319 -43.553 1.00 38.43 ? 282 GLU C OE1 1 
ATOM   8630  O  OE2 . GLU C  1 283 ? 1.582   -28.588 -44.925 1.00 38.15 ? 282 GLU C OE2 1 
ATOM   8631  N  N   . GLY C  1 284 ? 2.869   -25.676 -40.597 1.00 20.63 ? 283 GLY C N   1 
ATOM   8632  C  CA  . GLY C  1 284 ? 4.008   -24.788 -40.717 1.00 21.46 ? 283 GLY C CA  1 
ATOM   8633  C  C   . GLY C  1 284 ? 4.162   -23.766 -39.588 1.00 21.86 ? 283 GLY C C   1 
ATOM   8634  O  O   . GLY C  1 284 ? 5.067   -22.938 -39.641 1.00 20.94 ? 283 GLY C O   1 
ATOM   8635  N  N   . LEU C  1 285 ? 3.298   -23.804 -38.571 1.00 20.15 ? 284 LEU C N   1 
ATOM   8636  C  CA  . LEU C  1 285 ? 3.297   -22.740 -37.539 1.00 20.93 ? 284 LEU C CA  1 
ATOM   8637  C  C   . LEU C  1 285 ? 4.579   -22.740 -36.716 1.00 22.18 ? 284 LEU C C   1 
ATOM   8638  O  O   . LEU C  1 285 ? 5.131   -21.682 -36.429 1.00 21.83 ? 284 LEU C O   1 
ATOM   8639  C  CB  . LEU C  1 285 ? 2.121   -22.900 -36.584 1.00 20.60 ? 284 LEU C CB  1 
ATOM   8640  C  CG  . LEU C  1 285 ? 0.752   -22.689 -37.219 1.00 20.67 ? 284 LEU C CG  1 
ATOM   8641  C  CD1 . LEU C  1 285 ? -0.355  -23.064 -36.237 1.00 19.95 ? 284 LEU C CD1 1 
ATOM   8642  C  CD2 . LEU C  1 285 ? 0.625   -21.250 -37.706 1.00 22.73 ? 284 LEU C CD2 1 
ATOM   8643  N  N   . VAL C  1 286 ? 5.001   -23.920 -36.293 1.00 23.13 ? 285 VAL C N   1 
ATOM   8644  C  CA  . VAL C  1 286 ? 6.204   -24.070 -35.503 1.00 24.53 ? 285 VAL C CA  1 
ATOM   8645  C  C   . VAL C  1 286 ? 7.345   -24.430 -36.440 1.00 27.76 ? 285 VAL C C   1 
ATOM   8646  O  O   . VAL C  1 286 ? 7.278   -25.402 -37.179 1.00 29.32 ? 285 VAL C O   1 
ATOM   8647  C  CB  . VAL C  1 286 ? 6.010   -25.131 -34.417 1.00 24.33 ? 285 VAL C CB  1 
ATOM   8648  C  CG1 . VAL C  1 286 ? 7.321   -25.515 -33.771 1.00 25.29 ? 285 VAL C CG1 1 
ATOM   8649  C  CG2 . VAL C  1 286 ? 5.040   -24.608 -33.375 1.00 24.44 ? 285 VAL C CG2 1 
ATOM   8650  N  N   . GLU C  1 287 ? 8.376   -23.612 -36.441 1.00 30.70 ? 286 GLU C N   1 
ATOM   8651  C  CA  . GLU C  1 287 ? 9.485   -23.812 -37.355 1.00 35.20 ? 286 GLU C CA  1 
ATOM   8652  C  C   . GLU C  1 287 ? 10.259  -25.056 -36.927 1.00 35.96 ? 286 GLU C C   1 
ATOM   8653  O  O   . GLU C  1 287 ? 10.746  -25.167 -35.791 1.00 30.90 ? 286 GLU C O   1 
ATOM   8654  C  CB  . GLU C  1 287 ? 10.363  -22.563 -37.416 1.00 38.29 ? 286 GLU C CB  1 
ATOM   8655  C  CG  . GLU C  1 287 ? 10.946  -22.288 -38.790 1.00 45.91 ? 286 GLU C CG  1 
ATOM   8656  C  CD  . GLU C  1 287 ? 11.976  -23.322 -39.205 1.00 49.73 ? 286 GLU C CD  1 
ATOM   8657  O  OE1 . GLU C  1 287 ? 12.785  -23.747 -38.341 1.00 51.45 ? 286 GLU C OE1 1 
ATOM   8658  O  OE2 . GLU C  1 287 ? 11.988  -23.693 -40.403 1.00 54.10 ? 286 GLU C OE2 1 
ATOM   8659  N  N   . ALA C  1 288 ? 10.355  -25.972 -37.885 1.00 38.78 ? 287 ALA C N   1 
ATOM   8660  C  CA  . ALA C  1 288 ? 10.875  -27.314 -37.704 1.00 40.54 ? 287 ALA C CA  1 
ATOM   8661  C  C   . ALA C  1 288 ? 12.202  -27.370 -36.948 1.00 42.30 ? 287 ALA C C   1 
ATOM   8662  O  O   . ALA C  1 288 ? 12.373  -28.244 -36.103 1.00 45.72 ? 287 ALA C O   1 
ATOM   8663  C  CB  . ALA C  1 288 ? 11.004  -28.007 -39.070 1.00 41.51 ? 287 ALA C CB  1 
ATOM   8664  N  N   . THR C  1 289 ? 13.134  -26.460 -37.255 1.00 37.31 ? 288 THR C N   1 
ATOM   8665  C  CA  . THR C  1 289 ? 14.485  -26.534 -36.722 1.00 38.06 ? 288 THR C CA  1 
ATOM   8666  C  C   . THR C  1 289 ? 14.872  -25.434 -35.717 1.00 38.45 ? 288 THR C C   1 
ATOM   8667  O  O   . THR C  1 289 ? 15.847  -25.601 -34.979 1.00 41.78 ? 288 THR C O   1 
ATOM   8668  C  CB  . THR C  1 289 ? 15.537  -26.499 -37.880 1.00 40.33 ? 288 THR C CB  1 
ATOM   8669  O  OG1 . THR C  1 289 ? 15.418  -25.279 -38.611 1.00 39.40 ? 288 THR C OG1 1 
ATOM   8670  C  CG2 . THR C  1 289 ? 15.323  -27.669 -38.852 1.00 40.83 ? 288 THR C CG2 1 
ATOM   8671  N  N   . MET C  1 290 ? 14.133  -24.322 -35.698 1.00 32.60 ? 289 MET C N   1 
ATOM   8672  C  CA  . MET C  1 290 ? 14.499  -23.145 -34.924 1.00 30.96 ? 289 MET C CA  1 
ATOM   8673  C  C   . MET C  1 290 ? 14.324  -23.382 -33.416 1.00 28.05 ? 289 MET C C   1 
ATOM   8674  O  O   . MET C  1 290 ? 13.222  -23.703 -32.960 1.00 26.31 ? 289 MET C O   1 
ATOM   8675  C  CB  . MET C  1 290 ? 13.641  -21.970 -35.357 1.00 32.35 ? 289 MET C CB  1 
ATOM   8676  C  CG  . MET C  1 290 ? 14.033  -20.634 -34.747 1.00 36.13 ? 289 MET C CG  1 
ATOM   8677  S  SD  . MET C  1 290 ? 12.817  -19.377 -35.213 1.00 41.97 ? 289 MET C SD  1 
ATOM   8678  C  CE  . MET C  1 290 ? 13.552  -17.919 -34.454 1.00 41.86 ? 289 MET C CE  1 
ATOM   8679  N  N   . PRO C  1 291 ? 15.406  -23.205 -32.632 1.00 26.34 ? 290 PRO C N   1 
ATOM   8680  C  CA  . PRO C  1 291 ? 15.339  -23.410 -31.188 1.00 24.94 ? 290 PRO C CA  1 
ATOM   8681  C  C   . PRO C  1 291 ? 14.615  -22.249 -30.504 1.00 23.26 ? 290 PRO C C   1 
ATOM   8682  O  O   . PRO C  1 291 ? 14.407  -21.210 -31.130 1.00 22.87 ? 290 PRO C O   1 
ATOM   8683  C  CB  . PRO C  1 291 ? 16.804  -23.429 -30.768 1.00 25.52 ? 290 PRO C CB  1 
ATOM   8684  C  CG  . PRO C  1 291 ? 17.472  -22.539 -31.751 1.00 27.16 ? 290 PRO C CG  1 
ATOM   8685  C  CD  . PRO C  1 291 ? 16.718  -22.678 -33.049 1.00 27.15 ? 290 PRO C CD  1 
ATOM   8686  N  N   . PRO C  1 292 ? 14.263  -22.408 -29.223 1.00 22.14 ? 291 PRO C N   1 
ATOM   8687  C  CA  . PRO C  1 292 ? 13.485  -21.325 -28.584 1.00 21.16 ? 291 PRO C CA  1 
ATOM   8688  C  C   . PRO C  1 292 ? 14.346  -20.109 -28.268 1.00 21.15 ? 291 PRO C C   1 
ATOM   8689  O  O   . PRO C  1 292 ? 13.823  -19.050 -28.153 1.00 21.53 ? 291 PRO C O   1 
ATOM   8690  C  CB  . PRO C  1 292 ? 12.953  -21.976 -27.309 1.00 20.93 ? 291 PRO C CB  1 
ATOM   8691  C  CG  . PRO C  1 292 ? 13.900  -23.109 -27.050 1.00 22.18 ? 291 PRO C CG  1 
ATOM   8692  C  CD  . PRO C  1 292 ? 14.233  -23.637 -28.408 1.00 22.00 ? 291 PRO C CD  1 
ATOM   8693  N  N   . GLY C  1 293 ? 15.663  -20.271 -28.137 1.00 20.98 ? 292 GLY C N   1 
ATOM   8694  C  CA  . GLY C  1 293 ? 16.551  -19.170 -27.891 1.00 20.95 ? 292 GLY C CA  1 
ATOM   8695  C  C   . GLY C  1 293 ? 16.584  -18.683 -26.448 1.00 21.14 ? 292 GLY C C   1 
ATOM   8696  O  O   . GLY C  1 293 ? 16.917  -17.518 -26.184 1.00 21.63 ? 292 GLY C O   1 
ATOM   8697  N  N   . VAL C  1 294 ? 16.231  -19.574 -25.524 1.00 20.01 ? 293 VAL C N   1 
ATOM   8698  C  CA  . VAL C  1 294 ? 16.310  -19.315 -24.088 1.00 19.48 ? 293 VAL C CA  1 
ATOM   8699  C  C   . VAL C  1 294 ? 16.851  -20.559 -23.382 1.00 19.44 ? 293 VAL C C   1 
ATOM   8700  O  O   . VAL C  1 294 ? 16.880  -21.642 -23.968 1.00 18.69 ? 293 VAL C O   1 
ATOM   8701  C  CB  . VAL C  1 294 ? 14.918  -18.988 -23.493 1.00 19.11 ? 293 VAL C CB  1 
ATOM   8702  C  CG1 . VAL C  1 294 ? 14.305  -17.803 -24.227 1.00 19.61 ? 293 VAL C CG1 1 
ATOM   8703  C  CG2 . VAL C  1 294 ? 13.991  -20.182 -23.545 1.00 18.90 ? 293 VAL C CG2 1 
ATOM   8704  N  N   . GLN C  1 295 ? 17.292  -20.394 -22.140 1.00 19.13 ? 294 GLN C N   1 
ATOM   8705  C  CA  . GLN C  1 295 ? 17.712  -21.523 -21.335 1.00 19.83 ? 294 GLN C CA  1 
ATOM   8706  C  C   . GLN C  1 295 ? 16.545  -22.489 -21.223 1.00 19.39 ? 294 GLN C C   1 
ATOM   8707  O  O   . GLN C  1 295 ? 15.465  -22.092 -20.815 1.00 18.45 ? 294 GLN C O   1 
ATOM   8708  C  CB  . GLN C  1 295 ? 18.135  -21.079 -19.948 1.00 21.33 ? 294 GLN C CB  1 
ATOM   8709  C  CG  . GLN C  1 295 ? 18.641  -22.248 -19.113 1.00 22.72 ? 294 GLN C CG  1 
ATOM   8710  C  CD  . GLN C  1 295 ? 19.020  -21.815 -17.727 1.00 24.30 ? 294 GLN C CD  1 
ATOM   8711  O  OE1 . GLN C  1 295 ? 18.291  -22.048 -16.760 1.00 25.74 ? 294 GLN C OE1 1 
ATOM   8712  N  NE2 . GLN C  1 295 ? 20.133  -21.132 -17.625 1.00 25.92 ? 294 GLN C NE2 1 
ATOM   8713  N  N   . LEU C  1 296 ? 16.766  -23.739 -21.614 1.00 18.92 ? 295 LEU C N   1 
ATOM   8714  C  CA  . LEU C  1 296 ? 15.713  -24.728 -21.721 1.00 19.21 ? 295 LEU C CA  1 
ATOM   8715  C  C   . LEU C  1 296 ? 16.020  -25.956 -20.871 1.00 19.63 ? 295 LEU C C   1 
ATOM   8716  O  O   . LEU C  1 296 ? 17.136  -26.494 -20.927 1.00 20.76 ? 295 LEU C O   1 
ATOM   8717  C  CB  . LEU C  1 296 ? 15.550  -25.130 -23.191 1.00 19.88 ? 295 LEU C CB  1 
ATOM   8718  C  CG  . LEU C  1 296 ? 14.575  -26.243 -23.506 1.00 21.75 ? 295 LEU C CG  1 
ATOM   8719  C  CD1 . LEU C  1 296 ? 13.150  -25.811 -23.232 1.00 21.51 ? 295 LEU C CD1 1 
ATOM   8720  C  CD2 . LEU C  1 296 ? 14.754  -26.655 -24.953 1.00 22.75 ? 295 LEU C CD2 1 
ATOM   8721  N  N   . HIS C  1 297 ? 15.048  -26.376 -20.068 1.00 18.49 ? 296 HIS C N   1 
ATOM   8722  C  CA  . HIS C  1 297 ? 15.135  -27.604 -19.283 1.00 19.12 ? 296 HIS C CA  1 
ATOM   8723  C  C   . HIS C  1 297 ? 14.070  -28.531 -19.846 1.00 19.48 ? 296 HIS C C   1 
ATOM   8724  O  O   . HIS C  1 297 ? 12.882  -28.282 -19.676 1.00 19.09 ? 296 HIS C O   1 
ATOM   8725  C  CB  . HIS C  1 297 ? 14.877  -27.333 -17.797 1.00 19.28 ? 296 HIS C CB  1 
ATOM   8726  C  CG  . HIS C  1 297 ? 15.829  -26.347 -17.189 1.00 19.97 ? 296 HIS C CG  1 
ATOM   8727  N  ND1 . HIS C  1 297 ? 16.889  -26.726 -16.407 1.00 20.68 ? 296 HIS C ND1 1 
ATOM   8728  C  CD2 . HIS C  1 297 ? 15.875  -24.996 -17.248 1.00 20.46 ? 296 HIS C CD2 1 
ATOM   8729  C  CE1 . HIS C  1 297 ? 17.572  -25.658 -16.027 1.00 21.40 ? 296 HIS C CE1 1 
ATOM   8730  N  NE2 . HIS C  1 297 ? 16.985  -24.594 -16.536 1.00 20.59 ? 296 HIS C NE2 1 
ATOM   8731  N  N   . CYS C  1 298 ? 14.512  -29.583 -20.508 1.00 20.62 ? 297 CYS C N   1 
ATOM   8732  C  CA  A CYS C  1 298 ? 13.618  -30.530 -21.186 0.50 21.38 ? 297 CYS C CA  1 
ATOM   8733  C  CA  B CYS C  1 298 ? 13.618  -30.503 -21.199 0.50 21.49 ? 297 CYS C CA  1 
ATOM   8734  C  C   . CYS C  1 298 ? 13.421  -31.780 -20.368 1.00 20.78 ? 297 CYS C C   1 
ATOM   8735  O  O   . CYS C  1 298 ? 14.317  -32.607 -20.269 1.00 20.71 ? 297 CYS C O   1 
ATOM   8736  C  CB  A CYS C  1 298 ? 14.212  -30.928 -22.523 0.50 22.81 ? 297 CYS C CB  1 
ATOM   8737  C  CB  B CYS C  1 298 ? 14.202  -30.768 -22.585 0.50 22.93 ? 297 CYS C CB  1 
ATOM   8738  S  SG  A CYS C  1 298 ? 13.990  -29.662 -23.740 0.50 25.97 ? 297 CYS C SG  1 
ATOM   8739  S  SG  B CYS C  1 298 ? 13.215  -31.836 -23.637 0.50 26.89 ? 297 CYS C SG  1 
ATOM   8740  N  N   . LEU C  1 299 ? 12.262  -31.886 -19.733 1.00 19.09 ? 298 LEU C N   1 
ATOM   8741  C  CA  . LEU C  1 299 ? 11.959  -33.003 -18.856 1.00 19.34 ? 298 LEU C CA  1 
ATOM   8742  C  C   . LEU C  1 299 ? 11.010  -33.963 -19.584 1.00 19.03 ? 298 LEU C C   1 
ATOM   8743  O  O   . LEU C  1 299 ? 9.949   -33.554 -20.036 1.00 17.59 ? 298 LEU C O   1 
ATOM   8744  C  CB  . LEU C  1 299 ? 11.350  -32.509 -17.535 1.00 19.51 ? 298 LEU C CB  1 
ATOM   8745  C  CG  . LEU C  1 299 ? 12.353  -32.062 -16.452 1.00 21.51 ? 298 LEU C CG  1 
ATOM   8746  C  CD1 . LEU C  1 299 ? 13.183  -30.875 -16.904 1.00 22.06 ? 298 LEU C CD1 1 
ATOM   8747  C  CD2 . LEU C  1 299 ? 11.636  -31.721 -15.156 1.00 22.34 ? 298 LEU C CD2 1 
ATOM   8748  N  N   . TYR C  1 300 ? 11.409  -35.226 -19.700 1.00 19.40 ? 299 TYR C N   1 
ATOM   8749  C  CA  . TYR C  1 300 ? 10.670  -36.180 -20.515 1.00 19.36 ? 299 TYR C CA  1 
ATOM   8750  C  C   . TYR C  1 300 ? 10.616  -37.515 -19.800 1.00 19.76 ? 299 TYR C C   1 
ATOM   8751  O  O   . TYR C  1 300 ? 11.615  -37.968 -19.216 1.00 19.94 ? 299 TYR C O   1 
ATOM   8752  C  CB  . TYR C  1 300 ? 11.274  -36.305 -21.926 1.00 20.93 ? 299 TYR C CB  1 
ATOM   8753  C  CG  . TYR C  1 300 ? 12.698  -36.788 -21.958 1.00 21.53 ? 299 TYR C CG  1 
ATOM   8754  C  CD1 . TYR C  1 300 ? 13.761  -35.903 -21.815 1.00 23.54 ? 299 TYR C CD1 1 
ATOM   8755  C  CD2 . TYR C  1 300 ? 12.998  -38.125 -22.120 1.00 23.24 ? 299 TYR C CD2 1 
ATOM   8756  C  CE1 . TYR C  1 300 ? 15.083  -36.357 -21.800 1.00 24.46 ? 299 TYR C CE1 1 
ATOM   8757  C  CE2 . TYR C  1 300 ? 14.314  -38.580 -22.120 1.00 24.59 ? 299 TYR C CE2 1 
ATOM   8758  C  CZ  . TYR C  1 300 ? 15.347  -37.692 -21.969 1.00 26.17 ? 299 TYR C CZ  1 
ATOM   8759  O  OH  . TYR C  1 300 ? 16.651  -38.172 -21.978 1.00 30.15 ? 299 TYR C OH  1 
ATOM   8760  N  N   . GLY C  1 301 ? 9.443   -38.127 -19.816 1.00 18.69 ? 300 GLY C N   1 
ATOM   8761  C  CA  . GLY C  1 301 ? 9.284   -39.428 -19.196 1.00 19.69 ? 300 GLY C CA  1 
ATOM   8762  C  C   . GLY C  1 301 ? 9.716   -40.572 -20.102 1.00 20.21 ? 300 GLY C C   1 
ATOM   8763  O  O   . GLY C  1 301 ? 9.553   -40.506 -21.343 1.00 20.11 ? 300 GLY C O   1 
ATOM   8764  N  N   . THR C  1 302 ? 10.232  -41.634 -19.483 1.00 21.34 ? 301 THR C N   1 
ATOM   8765  C  CA  . THR C  1 302 ? 10.560  -42.873 -20.177 1.00 22.20 ? 301 THR C CA  1 
ATOM   8766  C  C   . THR C  1 302 ? 10.064  -44.059 -19.367 1.00 22.84 ? 301 THR C C   1 
ATOM   8767  O  O   . THR C  1 302 ? 9.605   -43.914 -18.236 1.00 22.91 ? 301 THR C O   1 
ATOM   8768  C  CB  . THR C  1 302 ? 12.073  -43.054 -20.385 1.00 23.69 ? 301 THR C CB  1 
ATOM   8769  O  OG1 . THR C  1 302 ? 12.729  -43.106 -19.106 1.00 24.34 ? 301 THR C OG1 1 
ATOM   8770  C  CG2 . THR C  1 302 ? 12.624  -41.924 -21.203 1.00 24.07 ? 301 THR C CG2 1 
ATOM   8771  N  N   . GLY C  1 303 ? 10.125  -45.238 -19.986 1.00 23.90 ? 302 GLY C N   1 
ATOM   8772  C  CA  . GLY C  1 303 ? 9.804   -46.493 -19.303 1.00 24.55 ? 302 GLY C CA  1 
ATOM   8773  C  C   . GLY C  1 303 ? 8.322   -46.764 -19.174 1.00 24.60 ? 302 GLY C C   1 
ATOM   8774  O  O   . GLY C  1 303 ? 7.931   -47.662 -18.426 1.00 24.65 ? 302 GLY C O   1 
ATOM   8775  N  N   . VAL C  1 304 ? 7.490   -45.996 -19.875 1.00 22.33 ? 303 VAL C N   1 
ATOM   8776  C  CA  . VAL C  1 304 ? 6.052   -46.196 -19.857 1.00 22.60 ? 303 VAL C CA  1 
ATOM   8777  C  C   . VAL C  1 304 ? 5.630   -46.599 -21.281 1.00 21.68 ? 303 VAL C C   1 
ATOM   8778  O  O   . VAL C  1 304 ? 5.950   -45.894 -22.224 1.00 20.88 ? 303 VAL C O   1 
ATOM   8779  C  CB  . VAL C  1 304 ? 5.299   -44.897 -19.470 1.00 22.47 ? 303 VAL C CB  1 
ATOM   8780  C  CG1 . VAL C  1 304 ? 3.804   -45.150 -19.422 1.00 22.90 ? 303 VAL C CG1 1 
ATOM   8781  C  CG2 . VAL C  1 304 ? 5.809   -44.352 -18.131 1.00 23.31 ? 303 VAL C CG2 1 
ATOM   8782  N  N   . PRO C  1 305 ? 4.959   -47.766 -21.453 1.00 21.83 ? 304 PRO C N   1 
ATOM   8783  C  CA  . PRO C  1 305 ? 4.579   -48.152 -22.812 1.00 21.06 ? 304 PRO C CA  1 
ATOM   8784  C  C   . PRO C  1 305 ? 3.730   -47.076 -23.481 1.00 19.57 ? 304 PRO C C   1 
ATOM   8785  O  O   . PRO C  1 305 ? 2.763   -46.586 -22.888 1.00 19.24 ? 304 PRO C O   1 
ATOM   8786  C  CB  . PRO C  1 305 ? 3.783   -49.455 -22.594 1.00 22.19 ? 304 PRO C CB  1 
ATOM   8787  C  CG  . PRO C  1 305 ? 4.288   -49.978 -21.302 1.00 23.26 ? 304 PRO C CG  1 
ATOM   8788  C  CD  . PRO C  1 305 ? 4.483   -48.756 -20.469 1.00 22.74 ? 304 PRO C CD  1 
ATOM   8789  N  N   . THR C  1 306 ? 4.162   -46.637 -24.660 1.00 18.49 ? 305 THR C N   1 
ATOM   8790  C  CA  . THR C  1 306 ? 3.559   -45.500 -25.349 1.00 18.30 ? 305 THR C CA  1 
ATOM   8791  C  C   . THR C  1 306 ? 3.132   -45.939 -26.751 1.00 18.28 ? 305 THR C C   1 
ATOM   8792  O  O   . THR C  1 306 ? 3.951   -46.455 -27.490 1.00 17.96 ? 305 THR C O   1 
ATOM   8793  C  CB  . THR C  1 306 ? 4.575   -44.355 -25.450 1.00 18.10 ? 305 THR C CB  1 
ATOM   8794  O  OG1 . THR C  1 306 ? 5.087   -44.081 -24.133 1.00 18.23 ? 305 THR C OG1 1 
ATOM   8795  C  CG2 . THR C  1 306 ? 3.940   -43.127 -26.051 1.00 17.57 ? 305 THR C CG2 1 
ATOM   8796  N  N   . PRO C  1 307 ? 1.845   -45.784 -27.084 1.00 18.85 ? 306 PRO C N   1 
ATOM   8797  C  CA  . PRO C  1 307 ? 1.396   -46.163 -28.419 1.00 19.70 ? 306 PRO C CA  1 
ATOM   8798  C  C   . PRO C  1 307 ? 2.264   -45.564 -29.529 1.00 20.29 ? 306 PRO C C   1 
ATOM   8799  O  O   . PRO C  1 307 ? 2.524   -44.357 -29.536 1.00 17.78 ? 306 PRO C O   1 
ATOM   8800  C  CB  . PRO C  1 307 ? -0.035  -45.605 -28.476 1.00 20.34 ? 306 PRO C CB  1 
ATOM   8801  C  CG  . PRO C  1 307 ? -0.471  -45.557 -27.064 1.00 21.00 ? 306 PRO C CG  1 
ATOM   8802  C  CD  . PRO C  1 307 ? 0.769   -45.104 -26.335 1.00 20.53 ? 306 PRO C CD  1 
ATOM   8803  N  N   . ASP C  1 308 ? 2.702   -46.437 -30.432 1.00 20.89 ? 307 ASP C N   1 
ATOM   8804  C  CA  . ASP C  1 308 ? 3.618   -46.120 -31.517 1.00 24.44 ? 307 ASP C CA  1 
ATOM   8805  C  C   . ASP C  1 308 ? 2.952   -46.334 -32.902 1.00 21.69 ? 307 ASP C C   1 
ATOM   8806  O  O   . ASP C  1 308 ? 3.246   -45.609 -33.847 1.00 20.99 ? 307 ASP C O   1 
ATOM   8807  C  CB  . ASP C  1 308 ? 4.855   -47.021 -31.373 1.00 30.28 ? 307 ASP C CB  1 
ATOM   8808  C  CG  . ASP C  1 308 ? 5.698   -47.095 -32.629 1.00 38.74 ? 307 ASP C CG  1 
ATOM   8809  O  OD1 . ASP C  1 308 ? 6.591   -46.231 -32.782 1.00 46.74 ? 307 ASP C OD1 1 
ATOM   8810  O  OD2 . ASP C  1 308 ? 5.458   -47.995 -33.486 1.00 42.96 ? 307 ASP C OD2 1 
ATOM   8811  N  N   . SER C  1 309 ? 2.066   -47.324 -33.012 1.00 19.45 ? 308 SER C N   1 
ATOM   8812  C  CA  . SER C  1 309 ? 1.375   -47.620 -34.255 1.00 18.69 ? 308 SER C CA  1 
ATOM   8813  C  C   . SER C  1 309 ? 0.197   -48.525 -33.974 1.00 18.07 ? 308 SER C C   1 
ATOM   8814  O  O   . SER C  1 309 ? 0.089   -49.083 -32.876 1.00 17.29 ? 308 SER C O   1 
ATOM   8815  C  CB  . SER C  1 309 ? 2.306   -48.276 -35.285 1.00 20.17 ? 308 SER C CB  1 
ATOM   8816  O  OG  . SER C  1 309 ? 2.966   -49.364 -34.727 1.00 21.54 ? 308 SER C OG  1 
ATOM   8817  N  N   . PHE C  1 310 ? -0.691  -48.631 -34.962 1.00 17.28 ? 309 PHE C N   1 
ATOM   8818  C  CA  . PHE C  1 310 ? -2.017  -49.231 -34.798 1.00 17.62 ? 309 PHE C CA  1 
ATOM   8819  C  C   . PHE C  1 310 ? -2.335  -50.136 -35.962 1.00 18.77 ? 309 PHE C C   1 
ATOM   8820  O  O   . PHE C  1 310 ? -2.102  -49.770 -37.114 1.00 19.84 ? 309 PHE C O   1 
ATOM   8821  C  CB  . PHE C  1 310 ? -3.063  -48.129 -34.695 1.00 17.41 ? 309 PHE C CB  1 
ATOM   8822  C  CG  . PHE C  1 310 ? -2.743  -47.121 -33.633 1.00 17.48 ? 309 PHE C CG  1 
ATOM   8823  C  CD1 . PHE C  1 310 ? -3.033  -47.386 -32.297 1.00 17.90 ? 309 PHE C CD1 1 
ATOM   8824  C  CD2 . PHE C  1 310 ? -2.094  -45.951 -33.954 1.00 17.75 ? 309 PHE C CD2 1 
ATOM   8825  C  CE1 . PHE C  1 310 ? -2.721  -46.480 -31.307 1.00 18.55 ? 309 PHE C CE1 1 
ATOM   8826  C  CE2 . PHE C  1 310 ? -1.761  -45.039 -32.971 1.00 17.81 ? 309 PHE C CE2 1 
ATOM   8827  C  CZ  . PHE C  1 310 ? -2.087  -45.302 -31.642 1.00 17.52 ? 309 PHE C CZ  1 
ATOM   8828  N  N   . TYR C  1 311 ? -2.916  -51.279 -35.659 1.00 19.89 ? 310 TYR C N   1 
ATOM   8829  C  CA  . TYR C  1 311 ? -3.415  -52.186 -36.675 1.00 21.84 ? 310 TYR C CA  1 
ATOM   8830  C  C   . TYR C  1 311 ? -4.938  -52.256 -36.550 1.00 21.84 ? 310 TYR C C   1 
ATOM   8831  O  O   . TYR C  1 311 ? -5.459  -52.661 -35.518 1.00 21.69 ? 310 TYR C O   1 
ATOM   8832  C  CB  . TYR C  1 311 ? -2.812  -53.573 -36.526 1.00 24.35 ? 310 TYR C CB  1 
ATOM   8833  C  CG  . TYR C  1 311 ? -3.153  -54.399 -37.727 1.00 28.60 ? 310 TYR C CG  1 
ATOM   8834  C  CD1 . TYR C  1 311 ? -4.382  -55.031 -37.875 1.00 32.89 ? 310 TYR C CD1 1 
ATOM   8835  C  CD2 . TYR C  1 311 ? -2.259  -54.458 -38.779 1.00 31.35 ? 310 TYR C CD2 1 
ATOM   8836  C  CE1 . TYR C  1 311 ? -4.681  -55.750 -39.036 1.00 35.71 ? 310 TYR C CE1 1 
ATOM   8837  C  CE2 . TYR C  1 311 ? -2.540  -55.169 -39.927 1.00 35.14 ? 310 TYR C CE2 1 
ATOM   8838  C  CZ  . TYR C  1 311 ? -3.754  -55.805 -40.059 1.00 36.86 ? 310 TYR C CZ  1 
ATOM   8839  O  OH  . TYR C  1 311 ? -3.999  -56.506 -41.233 1.00 42.42 ? 310 TYR C OH  1 
ATOM   8840  N  N   . TYR C  1 312 ? -5.644  -51.896 -37.618 1.00 21.83 ? 311 TYR C N   1 
ATOM   8841  C  CA  . TYR C  1 312 ? -7.109  -51.938 -37.640 1.00 24.01 ? 311 TYR C CA  1 
ATOM   8842  C  C   . TYR C  1 312 ? -7.588  -53.101 -38.497 1.00 27.10 ? 311 TYR C C   1 
ATOM   8843  O  O   . TYR C  1 312 ? -7.288  -53.161 -39.674 1.00 30.12 ? 311 TYR C O   1 
ATOM   8844  C  CB  . TYR C  1 312 ? -7.676  -50.671 -38.227 1.00 23.15 ? 311 TYR C CB  1 
ATOM   8845  C  CG  . TYR C  1 312 ? -7.651  -49.473 -37.332 1.00 21.22 ? 311 TYR C CG  1 
ATOM   8846  C  CD1 . TYR C  1 312 ? -6.516  -48.692 -37.224 1.00 20.93 ? 311 TYR C CD1 1 
ATOM   8847  C  CD2 . TYR C  1 312 ? -8.777  -49.105 -36.611 1.00 21.10 ? 311 TYR C CD2 1 
ATOM   8848  C  CE1 . TYR C  1 312 ? -6.482  -47.579 -36.400 1.00 19.92 ? 311 TYR C CE1 1 
ATOM   8849  C  CE2 . TYR C  1 312 ? -8.768  -47.990 -35.788 1.00 20.12 ? 311 TYR C CE2 1 
ATOM   8850  C  CZ  . TYR C  1 312 ? -7.626  -47.227 -35.690 1.00 20.11 ? 311 TYR C CZ  1 
ATOM   8851  O  OH  . TYR C  1 312 ? -7.637  -46.142 -34.852 1.00 20.11 ? 311 TYR C OH  1 
ATOM   8852  N  N   . GLU C  1 313 ? -8.305  -54.032 -37.901 1.00 30.48 ? 312 GLU C N   1 
ATOM   8853  C  CA  . GLU C  1 313 ? -8.941  -55.102 -38.678 1.00 34.69 ? 312 GLU C CA  1 
ATOM   8854  C  C   . GLU C  1 313 ? -10.176 -54.568 -39.390 1.00 34.32 ? 312 GLU C C   1 
ATOM   8855  O  O   . GLU C  1 313 ? -10.531 -55.051 -40.453 1.00 34.61 ? 312 GLU C O   1 
ATOM   8856  C  CB  . GLU C  1 313 ? -9.288  -56.275 -37.772 1.00 38.82 ? 312 GLU C CB  1 
ATOM   8857  C  CG  . GLU C  1 313 ? -8.017  -56.916 -37.216 1.00 45.85 ? 312 GLU C CG  1 
ATOM   8858  C  CD  . GLU C  1 313 ? -8.248  -57.882 -36.068 1.00 51.50 ? 312 GLU C CD  1 
ATOM   8859  O  OE1 . GLU C  1 313 ? -9.392  -58.344 -35.861 1.00 56.25 ? 312 GLU C OE1 1 
ATOM   8860  O  OE2 . GLU C  1 313 ? -7.257  -58.199 -35.372 1.00 55.56 ? 312 GLU C OE2 1 
ATOM   8861  N  N   . SER C  1 314 ? -10.810 -53.566 -38.788 1.00 33.99 ? 313 SER C N   1 
ATOM   8862  C  CA  . SER C  1 314 ? -11.933 -52.859 -39.380 1.00 35.55 ? 313 SER C CA  1 
ATOM   8863  C  C   . SER C  1 314 ? -11.747 -51.366 -39.114 1.00 32.35 ? 313 SER C C   1 
ATOM   8864  O  O   . SER C  1 314 ? -11.777 -50.921 -37.963 1.00 35.67 ? 313 SER C O   1 
ATOM   8865  C  CB  . SER C  1 314 ? -13.236 -53.354 -38.759 1.00 37.61 ? 313 SER C CB  1 
ATOM   8866  O  OG  . SER C  1 314 ? -14.329 -52.556 -39.177 1.00 42.51 ? 313 SER C OG  1 
ATOM   8867  N  N   . PHE C  1 315 ? -11.556 -50.601 -40.177 1.00 29.70 ? 314 PHE C N   1 
ATOM   8868  C  CA  . PHE C  1 315 ? -11.169 -49.202 -40.089 1.00 28.05 ? 314 PHE C CA  1 
ATOM   8869  C  C   . PHE C  1 315 ? -12.264 -48.323 -40.677 1.00 28.78 ? 314 PHE C C   1 
ATOM   8870  O  O   . PHE C  1 315 ? -12.780 -48.667 -41.719 1.00 29.48 ? 314 PHE C O   1 
ATOM   8871  C  CB  . PHE C  1 315 ? -9.902  -49.042 -40.906 1.00 26.51 ? 314 PHE C CB  1 
ATOM   8872  C  CG  . PHE C  1 315 ? -9.350  -47.647 -40.950 1.00 23.97 ? 314 PHE C CG  1 
ATOM   8873  C  CD1 . PHE C  1 315 ? -8.583  -47.168 -39.918 1.00 23.02 ? 314 PHE C CD1 1 
ATOM   8874  C  CD2 . PHE C  1 315 ? -9.519  -46.858 -42.075 1.00 23.76 ? 314 PHE C CD2 1 
ATOM   8875  C  CE1 . PHE C  1 315 ? -8.023  -45.911 -39.972 1.00 22.36 ? 314 PHE C CE1 1 
ATOM   8876  C  CE2 . PHE C  1 315 ? -8.971  -45.598 -42.139 1.00 22.90 ? 314 PHE C CE2 1 
ATOM   8877  C  CZ  . PHE C  1 315 ? -8.219  -45.121 -41.090 1.00 22.13 ? 314 PHE C CZ  1 
ATOM   8878  N  N   . PRO C  1 316 ? -12.630 -47.200 -40.059 1.00 28.84 ? 315 PRO C N   1 
ATOM   8879  C  CA  . PRO C  1 316 ? -12.049 -46.658 -38.833 1.00 29.91 ? 315 PRO C CA  1 
ATOM   8880  C  C   . PRO C  1 316 ? -12.926 -46.808 -37.567 1.00 32.49 ? 315 PRO C C   1 
ATOM   8881  O  O   . PRO C  1 316 ? -12.620 -46.188 -36.552 1.00 33.80 ? 315 PRO C O   1 
ATOM   8882  C  CB  . PRO C  1 316 ? -11.971 -45.174 -39.166 1.00 29.25 ? 315 PRO C CB  1 
ATOM   8883  C  CG  . PRO C  1 316 ? -13.235 -44.941 -39.946 1.00 29.60 ? 315 PRO C CG  1 
ATOM   8884  C  CD  . PRO C  1 316 ? -13.489 -46.209 -40.735 1.00 29.76 ? 315 PRO C CD  1 
ATOM   8885  N  N   . ASP C  1 317 ? -14.014 -47.576 -37.609 1.00 33.77 ? 316 ASP C N   1 
ATOM   8886  C  CA  . ASP C  1 317 ? -15.011 -47.505 -36.519 1.00 37.90 ? 316 ASP C CA  1 
ATOM   8887  C  C   . ASP C  1 317 ? -14.884 -48.590 -35.444 1.00 41.22 ? 316 ASP C C   1 
ATOM   8888  O  O   . ASP C  1 317 ? -15.817 -48.766 -34.650 1.00 45.32 ? 316 ASP C O   1 
ATOM   8889  C  CB  . ASP C  1 317 ? -16.452 -47.527 -37.083 1.00 40.41 ? 316 ASP C CB  1 
ATOM   8890  C  CG  . ASP C  1 317 ? -16.820 -46.247 -37.829 1.00 42.34 ? 316 ASP C CG  1 
ATOM   8891  O  OD1 . ASP C  1 317 ? -16.216 -45.167 -37.596 1.00 40.52 ? 316 ASP C OD1 1 
ATOM   8892  O  OD2 . ASP C  1 317 ? -17.733 -46.320 -38.676 1.00 47.07 ? 316 ASP C OD2 1 
ATOM   8893  N  N   . ARG C  1 318 ? -13.769 -49.316 -35.425 1.00 37.60 ? 317 ARG C N   1 
ATOM   8894  C  CA  . ARG C  1 318 ? -13.499 -50.313 -34.398 1.00 40.06 ? 317 ARG C CA  1 
ATOM   8895  C  C   . ARG C  1 318 ? -12.129 -50.016 -33.797 1.00 35.98 ? 317 ARG C C   1 
ATOM   8896  O  O   . ARG C  1 318 ? -11.243 -49.532 -34.497 1.00 33.62 ? 317 ARG C O   1 
ATOM   8897  C  CB  . ARG C  1 318 ? -13.493 -51.712 -35.011 1.00 45.63 ? 317 ARG C CB  1 
ATOM   8898  C  CG  . ARG C  1 318 ? -14.856 -52.330 -35.260 1.00 53.71 ? 317 ARG C CG  1 
ATOM   8899  C  CD  . ARG C  1 318 ? -15.093 -53.464 -34.312 1.00 60.44 ? 317 ARG C CD  1 
ATOM   8900  N  NE  . ARG C  1 318 ? -14.083 -54.501 -34.519 1.00 66.80 ? 317 ARG C NE  1 
ATOM   8901  C  CZ  . ARG C  1 318 ? -14.095 -55.411 -35.493 1.00 71.08 ? 317 ARG C CZ  1 
ATOM   8902  N  NH1 . ARG C  1 318 ? -15.093 -55.463 -36.374 1.00 72.83 ? 317 ARG C NH1 1 
ATOM   8903  N  NH2 . ARG C  1 318 ? -13.100 -56.288 -35.582 1.00 72.55 ? 317 ARG C NH2 1 
ATOM   8904  N  N   . ASP C  1 319 ? -11.951 -50.325 -32.519 1.00 33.82 ? 318 ASP C N   1 
ATOM   8905  C  CA  . ASP C  1 319 ? -10.685 -50.046 -31.833 1.00 32.19 ? 318 ASP C CA  1 
ATOM   8906  C  C   . ASP C  1 319 ? -9.552  -50.896 -32.413 1.00 28.31 ? 318 ASP C C   1 
ATOM   8907  O  O   . ASP C  1 319 ? -9.756  -52.054 -32.755 1.00 28.19 ? 318 ASP C O   1 
ATOM   8908  C  CB  . ASP C  1 319 ? -10.798 -50.312 -30.333 1.00 35.82 ? 318 ASP C CB  1 
ATOM   8909  C  CG  . ASP C  1 319 ? -11.661 -49.277 -29.602 1.00 39.39 ? 318 ASP C CG  1 
ATOM   8910  O  OD1 . ASP C  1 319 ? -11.797 -48.107 -30.066 1.00 41.06 ? 318 ASP C OD1 1 
ATOM   8911  O  OD2 . ASP C  1 319 ? -12.191 -49.648 -28.533 1.00 41.35 ? 318 ASP C OD2 1 
ATOM   8912  N  N   . PRO C  1 320 ? -8.363  -50.313 -32.562 1.00 23.49 ? 319 PRO C N   1 
ATOM   8913  C  CA  . PRO C  1 320 ? -7.261  -51.045 -33.151 1.00 22.34 ? 319 PRO C CA  1 
ATOM   8914  C  C   . PRO C  1 320 ? -6.459  -51.869 -32.150 1.00 22.49 ? 319 PRO C C   1 
ATOM   8915  O  O   . PRO C  1 320 ? -6.591  -51.669 -30.940 1.00 22.44 ? 319 PRO C O   1 
ATOM   8916  C  CB  . PRO C  1 320 ? -6.371  -49.924 -33.689 1.00 21.78 ? 319 PRO C CB  1 
ATOM   8917  C  CG  . PRO C  1 320 ? -6.571  -48.820 -32.720 1.00 21.22 ? 319 PRO C CG  1 
ATOM   8918  C  CD  . PRO C  1 320 ? -8.017  -48.902 -32.323 1.00 22.24 ? 319 PRO C CD  1 
ATOM   8919  N  N   . LYS C  1 321 ? -5.624  -52.767 -32.667 1.00 22.04 ? 320 LYS C N   1 
ATOM   8920  C  CA  . LYS C  1 321 ? -4.539  -53.384 -31.886 1.00 22.41 ? 320 LYS C CA  1 
ATOM   8921  C  C   . LYS C  1 321 ? -3.387  -52.412 -31.833 1.00 21.25 ? 320 LYS C C   1 
ATOM   8922  O  O   . LYS C  1 321 ? -3.221  -51.637 -32.765 1.00 19.84 ? 320 LYS C O   1 
ATOM   8923  C  CB  . LYS C  1 321 ? -4.036  -54.657 -32.559 1.00 23.89 ? 320 LYS C CB  1 
ATOM   8924  C  CG  . LYS C  1 321 ? -5.101  -55.645 -32.977 1.00 26.08 ? 320 LYS C CG  1 
ATOM   8925  C  CD  . LYS C  1 321 ? -6.101  -55.942 -31.888 1.00 27.77 ? 320 LYS C CD  1 
ATOM   8926  C  CE  . LYS C  1 321 ? -7.235  -56.745 -32.503 1.00 29.99 ? 320 LYS C CE  1 
ATOM   8927  N  NZ  . LYS C  1 321 ? -8.200  -57.081 -31.454 1.00 32.26 ? 320 LYS C NZ  1 
ATOM   8928  N  N   . ILE C  1 322 ? -2.607  -52.420 -30.754 1.00 19.99 ? 321 ILE C N   1 
ATOM   8929  C  CA  . ILE C  1 322 ? -1.636  -51.386 -30.525 1.00 19.81 ? 321 ILE C CA  1 
ATOM   8930  C  C   . ILE C  1 322 ? -0.223  -51.934 -30.393 1.00 20.32 ? 321 ILE C C   1 
ATOM   8931  O  O   . ILE C  1 322 ? 0.006   -52.935 -29.696 1.00 19.97 ? 321 ILE C O   1 
ATOM   8932  C  CB  . ILE C  1 322 ? -1.996  -50.556 -29.254 1.00 20.31 ? 321 ILE C CB  1 
ATOM   8933  C  CG1 . ILE C  1 322 ? -3.409  -49.956 -29.379 1.00 21.10 ? 321 ILE C CG1 1 
ATOM   8934  C  CG2 . ILE C  1 322 ? -0.993  -49.430 -29.032 1.00 20.63 ? 321 ILE C CG2 1 
ATOM   8935  C  CD1 . ILE C  1 322 ? -3.868  -49.190 -28.137 1.00 22.96 ? 321 ILE C CD1 1 
ATOM   8936  N  N   . CYS C  1 323 ? 0.705   -51.265 -31.060 1.00 19.98 ? 322 CYS C N   1 
ATOM   8937  C  CA  A CYS C  1 323 ? 2.134   -51.506 -30.871 0.50 20.61 ? 322 CYS C CA  1 
ATOM   8938  C  CA  B CYS C  1 323 ? 2.148   -51.494 -30.870 0.50 20.57 ? 322 CYS C CA  1 
ATOM   8939  C  C   . CYS C  1 323 ? 2.713   -50.373 -30.007 1.00 20.37 ? 322 CYS C C   1 
ATOM   8940  O  O   . CYS C  1 323 ? 2.421   -49.192 -30.252 1.00 20.05 ? 322 CYS C O   1 
ATOM   8941  C  CB  A CYS C  1 323 ? 2.824   -51.555 -32.228 0.50 21.50 ? 322 CYS C CB  1 
ATOM   8942  C  CB  B CYS C  1 323 ? 2.893   -51.480 -32.202 0.50 21.41 ? 322 CYS C CB  1 
ATOM   8943  S  SG  A CYS C  1 323 ? 4.603   -51.949 -32.153 0.50 23.58 ? 322 CYS C SG  1 
ATOM   8944  S  SG  B CYS C  1 323 ? 2.696   -52.969 -33.167 0.50 23.21 ? 322 CYS C SG  1 
ATOM   8945  N  N   . PHE C  1 324 ? 3.531   -50.726 -29.017 1.00 20.33 ? 323 PHE C N   1 
ATOM   8946  C  CA  . PHE C  1 324 ? 4.031   -49.749 -28.045 1.00 20.66 ? 323 PHE C CA  1 
ATOM   8947  C  C   . PHE C  1 324 ? 5.519   -49.529 -28.182 1.00 20.90 ? 323 PHE C C   1 
ATOM   8948  O  O   . PHE C  1 324 ? 6.272   -50.484 -28.421 1.00 22.01 ? 323 PHE C O   1 
ATOM   8949  C  CB  . PHE C  1 324 ? 3.768   -50.232 -26.609 1.00 20.79 ? 323 PHE C CB  1 
ATOM   8950  C  CG  . PHE C  1 324 ? 2.309   -50.331 -26.254 1.00 20.73 ? 323 PHE C CG  1 
ATOM   8951  C  CD1 . PHE C  1 324 ? 1.635   -49.229 -25.777 1.00 20.77 ? 323 PHE C CD1 1 
ATOM   8952  C  CD2 . PHE C  1 324 ? 1.618   -51.516 -26.411 1.00 21.69 ? 323 PHE C CD2 1 
ATOM   8953  C  CE1 . PHE C  1 324 ? 0.294   -49.282 -25.450 1.00 21.16 ? 323 PHE C CE1 1 
ATOM   8954  C  CE2 . PHE C  1 324 ? 0.265   -51.578 -26.083 1.00 22.08 ? 323 PHE C CE2 1 
ATOM   8955  C  CZ  . PHE C  1 324 ? -0.396  -50.464 -25.598 1.00 21.77 ? 323 PHE C CZ  1 
ATOM   8956  N  N   . GLY C  1 325 ? 5.938   -48.291 -27.989 1.00 20.52 ? 324 GLY C N   1 
ATOM   8957  C  CA  . GLY C  1 325 ? 7.357   -47.954 -27.848 1.00 21.20 ? 324 GLY C CA  1 
ATOM   8958  C  C   . GLY C  1 325 ? 7.602   -47.244 -26.530 1.00 21.70 ? 324 GLY C C   1 
ATOM   8959  O  O   . GLY C  1 325 ? 6.767   -47.284 -25.632 1.00 20.52 ? 324 GLY C O   1 
ATOM   8960  N  N   . ASP C  1 326 ? 8.759   -46.604 -26.417 1.00 21.44 ? 325 ASP C N   1 
ATOM   8961  C  CA  . ASP C  1 326 ? 9.141   -45.972 -25.173 1.00 21.72 ? 325 ASP C CA  1 
ATOM   8962  C  C   . ASP C  1 326 ? 8.627   -44.518 -25.170 1.00 20.36 ? 325 ASP C C   1 
ATOM   8963  O  O   . ASP C  1 326 ? 8.270   -43.955 -26.217 1.00 19.85 ? 325 ASP C O   1 
ATOM   8964  C  CB  . ASP C  1 326 ? 10.652  -46.035 -25.012 1.00 23.98 ? 325 ASP C CB  1 
ATOM   8965  C  CG  . ASP C  1 326 ? 11.112  -45.876 -23.577 1.00 25.94 ? 325 ASP C CG  1 
ATOM   8966  O  OD1 . ASP C  1 326 ? 10.298  -45.595 -22.663 1.00 26.21 ? 325 ASP C OD1 1 
ATOM   8967  O  OD2 . ASP C  1 326 ? 12.326  -46.073 -23.360 1.00 29.16 ? 325 ASP C OD2 1 
ATOM   8968  N  N   . GLY C  1 327 ? 8.520   -43.968 -23.975 1.00 19.77 ? 326 GLY C N   1 
ATOM   8969  C  CA  . GLY C  1 327 ? 7.988   -42.616 -23.736 1.00 19.20 ? 326 GLY C CA  1 
ATOM   8970  C  C   . GLY C  1 327 ? 7.315   -42.536 -22.374 1.00 19.17 ? 326 GLY C C   1 
ATOM   8971  O  O   . GLY C  1 327 ? 7.657   -43.295 -21.451 1.00 19.14 ? 326 GLY C O   1 
ATOM   8972  N  N   . ASP C  1 328 ? 6.341   -41.635 -22.257 1.00 18.56 ? 327 ASP C N   1 
ATOM   8973  C  CA  . ASP C  1 328 ? 5.660   -41.373 -20.984 1.00 19.33 ? 327 ASP C CA  1 
ATOM   8974  C  C   . ASP C  1 328 ? 4.214   -41.828 -20.962 1.00 19.18 ? 327 ASP C C   1 
ATOM   8975  O  O   . ASP C  1 328 ? 3.466   -41.471 -20.051 1.00 19.35 ? 327 ASP C O   1 
ATOM   8976  C  CB  . ASP C  1 328 ? 5.763   -39.874 -20.603 1.00 18.77 ? 327 ASP C CB  1 
ATOM   8977  C  CG  . ASP C  1 328 ? 4.920   -38.957 -21.471 1.00 19.69 ? 327 ASP C CG  1 
ATOM   8978  O  OD1 . ASP C  1 328 ? 4.107   -39.457 -22.300 1.00 19.94 ? 327 ASP C OD1 1 
ATOM   8979  O  OD2 . ASP C  1 328 ? 5.043   -37.697 -21.326 1.00 19.61 ? 327 ASP C OD2 1 
ATOM   8980  N  N   . GLY C  1 329 ? 3.835   -42.658 -21.938 1.00 19.40 ? 328 GLY C N   1 
ATOM   8981  C  CA  . GLY C  1 329 ? 2.455   -43.117 -22.055 1.00 19.54 ? 328 GLY C CA  1 
ATOM   8982  C  C   . GLY C  1 329 ? 1.686   -42.400 -23.136 1.00 20.32 ? 328 GLY C C   1 
ATOM   8983  O  O   . GLY C  1 329 ? 0.769   -42.960 -23.706 1.00 20.46 ? 328 GLY C O   1 
ATOM   8984  N  N   . THR C  1 330 ? 2.096   -41.180 -23.459 1.00 19.61 ? 329 THR C N   1 
ATOM   8985  C  CA  . THR C  1 330 ? 1.450   -40.324 -24.457 1.00 20.79 ? 329 THR C CA  1 
ATOM   8986  C  C   . THR C  1 330 ? 2.465   -39.803 -25.471 1.00 19.76 ? 329 THR C C   1 
ATOM   8987  O  O   . THR C  1 330 ? 2.318   -39.992 -26.667 1.00 21.05 ? 329 THR C O   1 
ATOM   8988  C  CB  . THR C  1 330 ? 0.750   -39.131 -23.755 1.00 21.79 ? 329 THR C CB  1 
ATOM   8989  O  OG1 . THR C  1 330 ? -0.259  -39.633 -22.880 1.00 24.18 ? 329 THR C OG1 1 
ATOM   8990  C  CG2 . THR C  1 330 ? 0.115   -38.180 -24.740 1.00 23.11 ? 329 THR C CG2 1 
ATOM   8991  N  N   . VAL C  1 331 ? 3.511   -39.160 -24.980 1.00 18.63 ? 330 VAL C N   1 
ATOM   8992  C  CA  . VAL C  1 331 ? 4.553   -38.613 -25.804 1.00 17.75 ? 330 VAL C CA  1 
ATOM   8993  C  C   . VAL C  1 331 ? 5.624   -39.664 -26.076 1.00 18.04 ? 330 VAL C C   1 
ATOM   8994  O  O   . VAL C  1 331 ? 6.240   -40.194 -25.157 1.00 17.81 ? 330 VAL C O   1 
ATOM   8995  C  CB  . VAL C  1 331 ? 5.174   -37.380 -25.126 1.00 18.25 ? 330 VAL C CB  1 
ATOM   8996  C  CG1 . VAL C  1 331 ? 6.346   -36.838 -25.931 1.00 18.58 ? 330 VAL C CG1 1 
ATOM   8997  C  CG2 . VAL C  1 331 ? 4.110   -36.307 -24.918 1.00 18.15 ? 330 VAL C CG2 1 
ATOM   8998  N  N   . ASN C  1 332 ? 5.834   -39.949 -27.352 1.00 18.45 ? 331 ASN C N   1 
ATOM   8999  C  CA  . ASN C  1 332 ? 6.826   -40.909 -27.772 1.00 19.29 ? 331 ASN C CA  1 
ATOM   9000  C  C   . ASN C  1 332 ? 8.203   -40.359 -27.441 1.00 20.05 ? 331 ASN C C   1 
ATOM   9001  O  O   . ASN C  1 332 ? 8.447   -39.144 -27.572 1.00 19.44 ? 331 ASN C O   1 
ATOM   9002  C  CB  . ASN C  1 332 ? 6.683   -41.172 -29.268 1.00 19.14 ? 331 ASN C CB  1 
ATOM   9003  C  CG  . ASN C  1 332 ? 5.286   -41.671 -29.636 1.00 19.59 ? 331 ASN C CG  1 
ATOM   9004  O  OD1 . ASN C  1 332 ? 4.387   -40.863 -29.966 1.00 18.95 ? 331 ASN C OD1 1 
ATOM   9005  N  ND2 . ASN C  1 332 ? 5.099   -42.973 -29.583 1.00 19.03 ? 331 ASN C ND2 1 
ATOM   9006  N  N   . LEU C  1 333 ? 9.102   -41.249 -27.027 1.00 20.64 ? 332 LEU C N   1 
ATOM   9007  C  CA  . LEU C  1 333 ? 10.465  -40.850 -26.679 1.00 21.95 ? 332 LEU C CA  1 
ATOM   9008  C  C   . LEU C  1 333 ? 11.156  -40.028 -27.780 1.00 23.58 ? 332 LEU C C   1 
ATOM   9009  O  O   . LEU C  1 333 ? 11.873  -39.069 -27.477 1.00 24.62 ? 332 LEU C O   1 
ATOM   9010  C  CB  . LEU C  1 333 ? 11.314  -42.066 -26.346 1.00 23.04 ? 332 LEU C CB  1 
ATOM   9011  C  CG  . LEU C  1 333 ? 12.754  -41.786 -25.905 1.00 24.21 ? 332 LEU C CG  1 
ATOM   9012  C  CD1 . LEU C  1 333 ? 12.771  -40.828 -24.723 1.00 25.31 ? 332 LEU C CD1 1 
ATOM   9013  C  CD2 . LEU C  1 333 ? 13.426  -43.106 -25.557 1.00 25.13 ? 332 LEU C CD2 1 
ATOM   9014  N  N   . LYS C  1 334 ? 10.940  -40.376 -29.035 1.00 24.14 ? 333 LYS C N   1 
ATOM   9015  C  CA  . LYS C  1 334 ? 11.603  -39.653 -30.124 1.00 27.42 ? 333 LYS C CA  1 
ATOM   9016  C  C   . LYS C  1 334 ? 11.231  -38.152 -30.201 1.00 23.93 ? 333 LYS C C   1 
ATOM   9017  O  O   . LYS C  1 334 ? 12.030  -37.363 -30.636 1.00 22.65 ? 333 LYS C O   1 
ATOM   9018  C  CB  . LYS C  1 334 ? 11.370  -40.353 -31.475 1.00 33.43 ? 333 LYS C CB  1 
ATOM   9019  C  CG  . LYS C  1 334 ? 12.046  -41.705 -31.506 1.00 40.08 ? 333 LYS C CG  1 
ATOM   9020  C  CD  . LYS C  1 334 ? 11.816  -42.385 -32.842 1.00 47.48 ? 333 LYS C CD  1 
ATOM   9021  C  CE  . LYS C  1 334 ? 12.778  -41.856 -33.887 1.00 53.20 ? 333 LYS C CE  1 
ATOM   9022  N  NZ  . LYS C  1 334 ? 12.063  -41.727 -35.181 1.00 60.46 ? 333 LYS C NZ  1 
ATOM   9023  N  N   A SER C  1 335 ? 10.216  -37.684 -29.489 0.80 28.21 ? 334 SER C N   1 
ATOM   9024  N  N   B SER C  1 335 ? 9.916   -37.933 -30.071 0.20 18.64 ? 334 SER C N   1 
ATOM   9025  C  CA  A SER C  1 335 ? 10.157  -36.192 -29.202 0.80 28.35 ? 334 SER C CA  1 
ATOM   9026  C  CA  B SER C  1 335 ? 9.279   -36.631 -30.175 0.20 15.68 ? 334 SER C CA  1 
ATOM   9027  C  C   A SER C  1 335 ? 11.424  -35.546 -28.518 0.80 31.30 ? 334 SER C C   1 
ATOM   9028  C  C   B SER C  1 335 ? 9.828   -35.785 -29.064 0.20 14.35 ? 334 SER C C   1 
ATOM   9029  O  O   A SER C  1 335 ? 11.811  -34.415 -28.862 0.80 30.67 ? 334 SER C O   1 
ATOM   9030  O  O   B SER C  1 335 ? 10.249  -34.665 -29.280 0.20 13.80 ? 334 SER C O   1 
ATOM   9031  C  CB  A SER C  1 335 ? 8.912   -35.852 -28.422 0.80 29.91 ? 334 SER C CB  1 
ATOM   9032  C  CB  B SER C  1 335 ? 7.753   -36.755 -30.000 0.20 14.67 ? 334 SER C CB  1 
ATOM   9033  O  OG  A SER C  1 335 ? 7.758   -36.073 -29.239 0.80 32.04 ? 334 SER C OG  1 
ATOM   9034  O  OG  B SER C  1 335 ? 7.079   -35.554 -30.358 0.20 13.33 ? 334 SER C OG  1 
ATOM   9035  N  N   A ALA C  1 336 ? 12.068  -36.238 -27.573 0.80 29.82 ? 335 ALA C N   1 
ATOM   9036  N  N   B ALA C  1 336 ? 9.811   -36.362 -27.871 0.20 13.43 ? 335 ALA C N   1 
ATOM   9037  C  CA  A ALA C  1 336 ? 13.231  -35.689 -26.878 0.80 34.36 ? 335 ALA C CA  1 
ATOM   9038  C  CA  B ALA C  1 336 ? 10.329  -35.713 -26.682 0.20 13.12 ? 335 ALA C CA  1 
ATOM   9039  C  C   A ALA C  1 336 ? 14.429  -35.383 -27.789 0.80 35.47 ? 335 ALA C C   1 
ATOM   9040  C  C   B ALA C  1 336 ? 11.775  -35.274 -26.893 0.20 13.15 ? 335 ALA C C   1 
ATOM   9041  O  O   A ALA C  1 336 ? 15.257  -34.553 -27.450 0.80 37.52 ? 335 ALA C O   1 
ATOM   9042  O  O   B ALA C  1 336 ? 12.167  -34.197 -26.446 0.20 12.62 ? 335 ALA C O   1 
ATOM   9043  C  CB  A ALA C  1 336 ? 13.672  -36.621 -25.748 0.80 35.82 ? 335 ALA C CB  1 
ATOM   9044  C  CB  B ALA C  1 336 ? 10.227  -36.657 -25.499 0.20 13.38 ? 335 ALA C CB  1 
ATOM   9045  N  N   A LEU C  1 337 ? 14.535  -36.050 -28.927 0.80 37.24 ? 336 LEU C N   1 
ATOM   9046  N  N   B LEU C  1 337 ? 12.550  -36.082 -27.618 0.20 13.34 ? 336 LEU C N   1 
ATOM   9047  C  CA  A LEU C  1 337 ? 15.641  -35.804 -29.851 0.80 39.55 ? 336 LEU C CA  1 
ATOM   9048  C  CA  B LEU C  1 337 ? 13.997  -35.869 -27.699 0.20 14.09 ? 336 LEU C CA  1 
ATOM   9049  C  C   A LEU C  1 337 ? 15.562  -34.380 -30.373 0.80 37.22 ? 336 LEU C C   1 
ATOM   9050  C  C   B LEU C  1 337 ? 14.404  -34.852 -28.753 0.20 14.31 ? 336 LEU C C   1 
ATOM   9051  O  O   A LEU C  1 337 ? 16.586  -33.812 -30.779 0.80 36.17 ? 336 LEU C O   1 
ATOM   9052  O  O   B LEU C  1 337 ? 15.591  -34.663 -29.015 0.20 14.57 ? 336 LEU C O   1 
ATOM   9053  C  CB  A LEU C  1 337 ? 15.654  -36.794 -31.034 0.80 42.34 ? 336 LEU C CB  1 
ATOM   9054  C  CB  B LEU C  1 337 ? 14.718  -37.188 -27.972 0.20 14.53 ? 336 LEU C CB  1 
ATOM   9055  C  CG  A LEU C  1 337 ? 16.128  -38.229 -30.728 0.80 44.25 ? 336 LEU C CG  1 
ATOM   9056  C  CG  B LEU C  1 337 ? 14.858  -38.131 -26.776 0.20 14.84 ? 336 LEU C CG  1 
ATOM   9057  C  CD1 A LEU C  1 337 ? 15.856  -39.157 -31.902 0.80 44.58 ? 336 LEU C CD1 1 
ATOM   9058  C  CD1 B LEU C  1 337 ? 15.594  -39.404 -27.181 0.20 15.44 ? 336 LEU C CD1 1 
ATOM   9059  C  CD2 A LEU C  1 337 ? 17.599  -38.257 -30.354 0.80 45.11 ? 336 LEU C CD2 1 
ATOM   9060  C  CD2 B LEU C  1 337 ? 15.558  -37.442 -25.619 0.20 15.11 ? 336 LEU C CD2 1 
ATOM   9061  N  N   A GLN C  1 338 ? 14.352  -33.809 -30.396 0.80 34.29 ? 337 GLN C N   1 
ATOM   9062  N  N   B GLN C  1 338 ? 13.425  -34.181 -29.345 0.20 14.27 ? 337 GLN C N   1 
ATOM   9063  C  CA  A GLN C  1 338 ? 14.212  -32.446 -30.840 0.80 33.46 ? 337 GLN C CA  1 
ATOM   9064  C  CA  B GLN C  1 338 ? 13.715  -33.232 -30.397 0.20 14.98 ? 337 GLN C CA  1 
ATOM   9065  C  C   A GLN C  1 338 ? 14.943  -31.512 -29.898 0.80 31.30 ? 337 GLN C C   1 
ATOM   9066  C  C   B GLN C  1 338 ? 14.580  -32.068 -29.879 0.20 16.12 ? 337 GLN C C   1 
ATOM   9067  O  O   A GLN C  1 338 ? 15.718  -30.677 -30.353 0.80 31.53 ? 337 GLN C O   1 
ATOM   9068  O  O   B GLN C  1 338 ? 15.252  -31.425 -30.677 0.20 16.05 ? 337 GLN C O   1 
ATOM   9069  C  CB  A GLN C  1 338 ? 12.741  -32.042 -30.992 0.80 35.02 ? 337 GLN C CB  1 
ATOM   9070  C  CB  B GLN C  1 338 ? 12.408  -32.741 -31.047 0.20 14.37 ? 337 GLN C CB  1 
ATOM   9071  C  CG  A GLN C  1 338 ? 12.576  -30.629 -31.528 0.80 36.41 ? 337 GLN C CG  1 
ATOM   9072  C  CG  B GLN C  1 338 ? 12.554  -31.650 -32.099 0.20 14.36 ? 337 GLN C CG  1 
ATOM   9073  C  CD  A GLN C  1 338 ? 12.914  -30.488 -32.997 0.80 39.93 ? 337 GLN C CD  1 
ATOM   9074  C  CD  B GLN C  1 338 ? 13.402  -32.029 -33.306 0.20 14.74 ? 337 GLN C CD  1 
ATOM   9075  O  OE1 A GLN C  1 338 ? 13.287  -31.449 -33.697 0.80 39.83 ? 337 GLN C OE1 1 
ATOM   9076  O  OE1 B GLN C  1 338 ? 13.560  -33.202 -33.646 0.20 14.90 ? 337 GLN C OE1 1 
ATOM   9077  N  NE2 A GLN C  1 338 ? 12.749  -29.261 -33.485 0.80 43.60 ? 337 GLN C NE2 1 
ATOM   9078  N  NE2 B GLN C  1 338 ? 13.934  -31.010 -33.978 0.20 14.89 ? 337 GLN C NE2 1 
ATOM   9079  N  N   A CYS C  1 339 ? 14.725  -31.617 -28.586 0.80 30.38 ? 338 CYS C N   1 
ATOM   9080  N  N   B CYS C  1 339 ? 14.585  -31.814 -28.559 0.20 17.60 ? 338 CYS C N   1 
ATOM   9081  C  CA  A CYS C  1 339 ? 15.507  -30.759 -27.681 0.80 31.83 ? 338 CYS C CA  1 
ATOM   9082  C  CA  B CYS C  1 339 ? 15.415  -30.721 -27.974 0.20 19.64 ? 338 CYS C CA  1 
ATOM   9083  C  C   A CYS C  1 339 ? 16.971  -31.017 -27.838 0.80 28.23 ? 338 CYS C C   1 
ATOM   9084  C  C   B CYS C  1 339 ? 16.933  -31.007 -27.939 0.20 22.54 ? 338 CYS C C   1 
ATOM   9085  O  O   A CYS C  1 339 ? 17.770  -30.093 -27.768 0.80 28.49 ? 338 CYS C O   1 
ATOM   9086  O  O   B CYS C  1 339 ? 17.732  -30.087 -27.767 0.20 23.13 ? 338 CYS C O   1 
ATOM   9087  C  CB  A CYS C  1 339 ? 15.082  -30.788 -26.201 0.80 34.79 ? 338 CYS C CB  1 
ATOM   9088  C  CB  B CYS C  1 339 ? 14.943  -30.272 -26.571 0.20 19.15 ? 338 CYS C CB  1 
ATOM   9089  S  SG  A CYS C  1 339 ? 14.417  -32.315 -25.627 0.80 40.47 ? 338 CYS C SG  1 
ATOM   9090  S  SG  B CYS C  1 339 ? 13.800  -31.337 -25.697 0.20 17.82 ? 338 CYS C SG  1 
ATOM   9091  N  N   . GLN C  1 340 ? 17.353  -32.263 -28.109 1.00 26.93 ? 339 GLN C N   1 
ATOM   9092  C  CA  . GLN C  1 340 ? 18.769  -32.556 -28.289 1.00 29.43 ? 339 GLN C CA  1 
ATOM   9093  C  C   . GLN C  1 340 ? 19.313  -31.793 -29.515 1.00 29.99 ? 339 GLN C C   1 
ATOM   9094  O  O   . GLN C  1 340 ? 20.438  -31.292 -29.494 1.00 28.83 ? 339 GLN C O   1 
ATOM   9095  C  CB  . GLN C  1 340 ? 19.018  -34.059 -28.413 1.00 34.01 ? 339 GLN C CB  1 
ATOM   9096  C  CG  . GLN C  1 340 ? 20.476  -34.434 -28.570 1.00 39.72 ? 339 GLN C CG  1 
ATOM   9097  C  CD  . GLN C  1 340 ? 20.659  -35.937 -28.712 1.00 46.25 ? 339 GLN C CD  1 
ATOM   9098  O  OE1 . GLN C  1 340 ? 20.110  -36.560 -29.630 1.00 48.85 ? 339 GLN C OE1 1 
ATOM   9099  N  NE2 . GLN C  1 340 ? 21.428  -36.530 -27.800 1.00 49.68 ? 339 GLN C NE2 1 
ATOM   9100  N  N   . ALA C  1 341 ? 18.518  -31.722 -30.589 1.00 28.51 ? 340 ALA C N   1 
ATOM   9101  C  CA  . ALA C  1 341 ? 18.960  -31.031 -31.816 1.00 28.51 ? 340 ALA C CA  1 
ATOM   9102  C  C   . ALA C  1 341 ? 19.170  -29.528 -31.588 1.00 27.21 ? 340 ALA C C   1 
ATOM   9103  O  O   . ALA C  1 341 ? 20.049  -28.909 -32.185 1.00 27.38 ? 340 ALA C O   1 
ATOM   9104  C  CB  . ALA C  1 341 ? 17.952  -31.263 -32.915 1.00 30.10 ? 340 ALA C CB  1 
ATOM   9105  N  N   . TRP C  1 342 ? 18.419  -28.960 -30.653 1.00 24.11 ? 341 TRP C N   1 
ATOM   9106  C  CA  . TRP C  1 342 ? 18.570  -27.545 -30.336 1.00 23.36 ? 341 TRP C CA  1 
ATOM   9107  C  C   . TRP C  1 342 ? 19.875  -27.179 -29.639 1.00 24.29 ? 341 TRP C C   1 
ATOM   9108  O  O   . TRP C  1 342 ? 20.300  -26.034 -29.697 1.00 23.59 ? 341 TRP C O   1 
ATOM   9109  C  CB  . TRP C  1 342 ? 17.384  -27.069 -29.505 1.00 22.99 ? 341 TRP C CB  1 
ATOM   9110  C  CG  . TRP C  1 342 ? 16.087  -27.052 -30.252 1.00 22.10 ? 341 TRP C CG  1 
ATOM   9111  C  CD1 . TRP C  1 342 ? 15.892  -26.899 -31.611 1.00 22.13 ? 341 TRP C CD1 1 
ATOM   9112  C  CD2 . TRP C  1 342 ? 14.786  -27.167 -29.672 1.00 21.27 ? 341 TRP C CD2 1 
ATOM   9113  N  NE1 . TRP C  1 342 ? 14.537  -26.903 -31.889 1.00 21.48 ? 341 TRP C NE1 1 
ATOM   9114  C  CE2 . TRP C  1 342 ? 13.846  -27.083 -30.718 1.00 21.09 ? 341 TRP C CE2 1 
ATOM   9115  C  CE3 . TRP C  1 342 ? 14.328  -27.355 -28.368 1.00 21.73 ? 341 TRP C CE3 1 
ATOM   9116  C  CZ2 . TRP C  1 342 ? 12.482  -27.170 -30.487 1.00 21.15 ? 341 TRP C CZ2 1 
ATOM   9117  C  CZ3 . TRP C  1 342 ? 12.970  -27.432 -28.144 1.00 21.33 ? 341 TRP C CZ3 1 
ATOM   9118  C  CH2 . TRP C  1 342 ? 12.071  -27.347 -29.192 1.00 20.84 ? 341 TRP C CH2 1 
ATOM   9119  N  N   . GLN C  1 343 ? 20.499  -28.133 -28.957 1.00 24.72 ? 342 GLN C N   1 
ATOM   9120  C  CA  . GLN C  1 343 ? 21.734  -27.868 -28.231 1.00 26.33 ? 342 GLN C CA  1 
ATOM   9121  C  C   . GLN C  1 343 ? 22.792  -27.169 -29.092 1.00 27.30 ? 342 GLN C C   1 
ATOM   9122  O  O   . GLN C  1 343 ? 23.491  -26.282 -28.617 1.00 27.52 ? 342 GLN C O   1 
ATOM   9123  C  CB  . GLN C  1 343 ? 22.331  -29.178 -27.675 1.00 27.61 ? 342 GLN C CB  1 
ATOM   9124  C  CG  . GLN C  1 343 ? 21.491  -29.797 -26.570 1.00 28.18 ? 342 GLN C CG  1 
ATOM   9125  C  CD  . GLN C  1 343 ? 22.011  -31.081 -25.967 1.00 29.79 ? 342 GLN C CD  1 
ATOM   9126  O  OE1 . GLN C  1 343 ? 22.635  -31.893 -26.618 1.00 29.61 ? 342 GLN C OE1 1 
ATOM   9127  N  NE2 . GLN C  1 343 ? 21.733  -31.251 -24.686 1.00 32.05 ? 342 GLN C NE2 1 
ATOM   9128  N  N   . SER C  1 344 ? 22.927  -27.586 -30.341 1.00 27.90 ? 343 SER C N   1 
ATOM   9129  C  CA  . SER C  1 344 ? 23.975  -27.020 -31.186 1.00 30.04 ? 343 SER C CA  1 
ATOM   9130  C  C   . SER C  1 344 ? 23.492  -25.788 -31.961 1.00 30.26 ? 343 SER C C   1 
ATOM   9131  O  O   . SER C  1 344 ? 24.278  -25.167 -32.657 1.00 30.07 ? 343 SER C O   1 
ATOM   9132  C  CB  . SER C  1 344 ? 24.525  -28.084 -32.140 1.00 30.95 ? 343 SER C CB  1 
ATOM   9133  O  OG  . SER C  1 344 ? 23.543  -28.482 -33.073 1.00 31.68 ? 343 SER C OG  1 
ATOM   9134  N  N   . ARG C  1 345 ? 22.205  -25.455 -31.855 1.00 28.47 ? 344 ARG C N   1 
ATOM   9135  C  CA  . ARG C  1 345 ? 21.626  -24.368 -32.645 1.00 29.72 ? 344 ARG C CA  1 
ATOM   9136  C  C   . ARG C  1 345 ? 21.368  -23.088 -31.853 1.00 29.23 ? 344 ARG C C   1 
ATOM   9137  O  O   . ARG C  1 345 ? 20.946  -22.094 -32.428 1.00 29.26 ? 344 ARG C O   1 
ATOM   9138  C  CB  . ARG C  1 345 ? 20.306  -24.829 -33.272 1.00 31.19 ? 344 ARG C CB  1 
ATOM   9139  C  CG  . ARG C  1 345 ? 20.482  -25.882 -34.361 1.00 33.14 ? 344 ARG C CG  1 
ATOM   9140  C  CD  . ARG C  1 345 ? 19.125  -26.359 -34.853 1.00 34.49 ? 344 ARG C CD  1 
ATOM   9141  N  NE  . ARG C  1 345 ? 19.240  -27.631 -35.563 1.00 38.85 ? 344 ARG C NE  1 
ATOM   9142  C  CZ  . ARG C  1 345 ? 18.275  -28.552 -35.654 1.00 42.61 ? 344 ARG C CZ  1 
ATOM   9143  N  NH1 . ARG C  1 345 ? 17.069  -28.367 -35.089 1.00 43.50 ? 344 ARG C NH1 1 
ATOM   9144  N  NH2 . ARG C  1 345 ? 18.514  -29.671 -36.331 1.00 43.99 ? 344 ARG C NH2 1 
ATOM   9145  N  N   . GLN C  1 346 ? 21.576  -23.107 -30.543 1.00 28.29 ? 345 GLN C N   1 
ATOM   9146  C  CA  . GLN C  1 346 ? 21.421  -21.903 -29.750 1.00 27.76 ? 345 GLN C CA  1 
ATOM   9147  C  C   . GLN C  1 346 ? 22.560  -21.834 -28.771 1.00 28.84 ? 345 GLN C C   1 
ATOM   9148  O  O   . GLN C  1 346 ? 23.160  -22.860 -28.436 1.00 28.57 ? 345 GLN C O   1 
ATOM   9149  C  CB  . GLN C  1 346 ? 20.046  -21.848 -29.050 1.00 26.02 ? 345 GLN C CB  1 
ATOM   9150  C  CG  . GLN C  1 346 ? 19.764  -22.953 -28.046 1.00 24.62 ? 345 GLN C CG  1 
ATOM   9151  C  CD  . GLN C  1 346 ? 18.548  -22.662 -27.187 1.00 23.68 ? 345 GLN C CD  1 
ATOM   9152  O  OE1 . GLN C  1 346 ? 17.463  -22.407 -27.697 1.00 22.66 ? 345 GLN C OE1 1 
ATOM   9153  N  NE2 . GLN C  1 346 ? 18.711  -22.762 -25.881 1.00 23.70 ? 345 GLN C NE2 1 
ATOM   9154  N  N   . GLU C  1 347 ? 22.878  -20.615 -28.350 1.00 29.66 ? 346 GLU C N   1 
ATOM   9155  C  CA  . GLU C  1 347 ? 23.921  -20.360 -27.364 1.00 32.33 ? 346 GLU C CA  1 
ATOM   9156  C  C   . GLU C  1 347 ? 23.479  -20.654 -25.930 1.00 29.20 ? 346 GLU C C   1 
ATOM   9157  O  O   . GLU C  1 347 ? 24.259  -21.130 -25.109 1.00 27.63 ? 346 GLU C O   1 
ATOM   9158  C  CB  . GLU C  1 347 ? 24.368  -18.889 -27.502 1.00 37.29 ? 346 GLU C CB  1 
ATOM   9159  C  CG  . GLU C  1 347 ? 25.342  -18.349 -26.471 1.00 46.38 ? 346 GLU C CG  1 
ATOM   9160  C  CD  . GLU C  1 347 ? 25.948  -16.998 -26.871 1.00 56.38 ? 346 GLU C CD  1 
ATOM   9161  O  OE1 . GLU C  1 347 ? 25.982  -16.664 -28.090 1.00 64.27 ? 346 GLU C OE1 1 
ATOM   9162  O  OE2 . GLU C  1 347 ? 26.408  -16.266 -25.958 1.00 64.38 ? 346 GLU C OE2 1 
ATOM   9163  N  N   . HIS C  1 348 ? 22.226  -20.353 -25.608 1.00 25.94 ? 347 HIS C N   1 
ATOM   9164  C  CA  A HIS C  1 348 ? 21.700  -20.679 -24.286 0.70 25.54 ? 347 HIS C CA  1 
ATOM   9165  C  CA  B HIS C  1 348 ? 21.701  -20.692 -24.289 0.30 25.25 ? 347 HIS C CA  1 
ATOM   9166  C  C   . HIS C  1 348 ? 21.706  -22.198 -24.064 1.00 24.77 ? 347 HIS C C   1 
ATOM   9167  O  O   . HIS C  1 348 ? 21.511  -22.968 -24.999 1.00 23.54 ? 347 HIS C O   1 
ATOM   9168  C  CB  A HIS C  1 348 ? 20.264  -20.165 -24.126 0.70 25.61 ? 347 HIS C CB  1 
ATOM   9169  C  CB  B HIS C  1 348 ? 20.294  -20.127 -24.104 0.30 24.57 ? 347 HIS C CB  1 
ATOM   9170  C  CG  A HIS C  1 348 ? 20.174  -18.696 -23.921 0.70 26.54 ? 347 HIS C CG  1 
ATOM   9171  C  CG  B HIS C  1 348 ? 20.311  -18.679 -23.724 0.30 24.82 ? 347 HIS C CG  1 
ATOM   9172  N  ND1 A HIS C  1 348 ? 20.287  -17.806 -24.963 0.70 28.46 ? 347 HIS C ND1 1 
ATOM   9173  N  ND1 B HIS C  1 348 ? 20.627  -18.256 -22.449 0.30 25.29 ? 347 HIS C ND1 1 
ATOM   9174  C  CD2 A HIS C  1 348 ? 19.983  -17.954 -22.808 0.70 28.02 ? 347 HIS C CD2 1 
ATOM   9175  C  CD2 B HIS C  1 348 ? 20.147  -17.556 -24.462 0.30 25.42 ? 347 HIS C CD2 1 
ATOM   9176  C  CE1 A HIS C  1 348 ? 20.172  -16.574 -24.502 0.70 28.73 ? 347 HIS C CE1 1 
ATOM   9177  C  CE1 B HIS C  1 348 ? 20.610  -16.935 -22.407 0.30 25.42 ? 347 HIS C CE1 1 
ATOM   9178  N  NE2 A HIS C  1 348 ? 19.975  -16.637 -23.196 0.70 28.80 ? 347 HIS C NE2 1 
ATOM   9179  N  NE2 B HIS C  1 348 ? 20.321  -16.485 -23.615 0.30 25.76 ? 347 HIS C NE2 1 
ATOM   9180  N  N   . GLN C  1 349 ? 21.912  -22.605 -22.820 1.00 24.86 ? 348 GLN C N   1 
ATOM   9181  C  CA  . GLN C  1 349 ? 21.993  -24.024 -22.485 1.00 25.90 ? 348 GLN C CA  1 
ATOM   9182  C  C   . GLN C  1 349 ? 20.675  -24.745 -22.720 1.00 24.06 ? 348 GLN C C   1 
ATOM   9183  O  O   . GLN C  1 349 ? 19.592  -24.171 -22.470 1.00 21.75 ? 348 GLN C O   1 
ATOM   9184  C  CB  . GLN C  1 349 ? 22.359  -24.222 -21.028 1.00 28.91 ? 348 GLN C CB  1 
ATOM   9185  C  CG  . GLN C  1 349 ? 23.687  -23.665 -20.586 1.00 35.25 ? 348 GLN C CG  1 
ATOM   9186  C  CD  . GLN C  1 349 ? 23.875  -23.918 -19.102 1.00 39.78 ? 348 GLN C CD  1 
ATOM   9187  O  OE1 . GLN C  1 349 ? 24.003  -25.068 -18.675 1.00 45.59 ? 348 GLN C OE1 1 
ATOM   9188  N  NE2 . GLN C  1 349 ? 23.831  -22.861 -18.307 1.00 43.34 ? 348 GLN C NE2 1 
ATOM   9189  N  N   . VAL C  1 350 ? 20.774  -25.997 -23.155 1.00 22.77 ? 349 VAL C N   1 
ATOM   9190  C  CA  . VAL C  1 350 ? 19.652  -26.921 -23.224 1.00 22.61 ? 349 VAL C CA  1 
ATOM   9191  C  C   . VAL C  1 350 ? 19.989  -28.117 -22.338 1.00 24.70 ? 349 VAL C C   1 
ATOM   9192  O  O   . VAL C  1 350 ? 21.023  -28.774 -22.561 1.00 26.21 ? 349 VAL C O   1 
ATOM   9193  C  CB  . VAL C  1 350 ? 19.396  -27.401 -24.651 1.00 22.55 ? 349 VAL C CB  1 
ATOM   9194  C  CG1 . VAL C  1 350 ? 18.275  -28.437 -24.676 1.00 21.65 ? 349 VAL C CG1 1 
ATOM   9195  C  CG2 . VAL C  1 350 ? 19.107  -26.234 -25.591 1.00 21.70 ? 349 VAL C CG2 1 
ATOM   9196  N  N   . LEU C  1 351 ? 19.245  -28.295 -21.244 1.00 23.65 ? 350 LEU C N   1 
ATOM   9197  C  CA  . LEU C  1 351 ? 19.511  -29.374 -20.290 1.00 24.95 ? 350 LEU C CA  1 
ATOM   9198  C  C   . LEU C  1 351 ? 18.439  -30.424 -20.501 1.00 25.48 ? 350 LEU C C   1 
ATOM   9199  O  O   . LEU C  1 351 ? 17.248  -30.096 -20.472 1.00 24.07 ? 350 LEU C O   1 
ATOM   9200  C  CB  . LEU C  1 351 ? 19.466  -28.881 -18.844 1.00 26.30 ? 350 LEU C CB  1 
ATOM   9201  C  CG  . LEU C  1 351 ? 20.420  -27.730 -18.467 1.00 28.48 ? 350 LEU C CG  1 
ATOM   9202  C  CD1 . LEU C  1 351 ? 19.808  -26.380 -18.805 1.00 29.23 ? 350 LEU C CD1 1 
ATOM   9203  C  CD2 . LEU C  1 351 ? 20.801  -27.725 -16.993 1.00 30.74 ? 350 LEU C CD2 1 
ATOM   9204  N  N   . LEU C  1 352 ? 18.850  -31.655 -20.740 1.00 25.44 ? 351 LEU C N   1 
ATOM   9205  C  CA  . LEU C  1 352 ? 17.916  -32.757 -20.884 1.00 27.13 ? 351 LEU C CA  1 
ATOM   9206  C  C   . LEU C  1 352 ? 17.807  -33.501 -19.574 1.00 26.87 ? 351 LEU C C   1 
ATOM   9207  O  O   . LEU C  1 352 ? 18.825  -33.759 -18.931 1.00 28.69 ? 351 LEU C O   1 
ATOM   9208  C  CB  . LEU C  1 352 ? 18.350  -33.684 -22.011 1.00 29.51 ? 351 LEU C CB  1 
ATOM   9209  C  CG  . LEU C  1 352 ? 17.643  -33.362 -23.337 1.00 31.82 ? 351 LEU C CG  1 
ATOM   9210  C  CD1 . LEU C  1 352 ? 18.159  -32.069 -23.932 1.00 33.62 ? 351 LEU C CD1 1 
ATOM   9211  C  CD2 . LEU C  1 352 ? 17.834  -34.508 -24.314 1.00 35.23 ? 351 LEU C CD2 1 
ATOM   9212  N  N   . GLN C  1 353 ? 16.593  -33.786 -19.122 1.00 23.30 ? 352 GLN C N   1 
ATOM   9213  C  CA  . GLN C  1 353 ? 16.410  -34.552 -17.898 1.00 24.12 ? 352 GLN C CA  1 
ATOM   9214  C  C   . GLN C  1 353 ? 15.412  -35.671 -18.113 1.00 23.09 ? 352 GLN C C   1 
ATOM   9215  O  O   . GLN C  1 353 ? 14.199  -35.431 -18.208 1.00 21.24 ? 352 GLN C O   1 
ATOM   9216  C  CB  . GLN C  1 353 ? 15.959  -33.664 -16.729 1.00 25.15 ? 352 GLN C CB  1 
ATOM   9217  C  CG  . GLN C  1 353 ? 15.713  -34.432 -15.427 1.00 27.08 ? 352 GLN C CG  1 
ATOM   9218  C  CD  . GLN C  1 353 ? 16.979  -35.062 -14.903 1.00 28.91 ? 352 GLN C CD  1 
ATOM   9219  O  OE1 . GLN C  1 353 ? 17.908  -34.357 -14.548 1.00 32.43 ? 352 GLN C OE1 1 
ATOM   9220  N  NE2 . GLN C  1 353 ? 17.042  -36.387 -14.885 1.00 29.93 ? 352 GLN C NE2 1 
ATOM   9221  N  N   . GLU C  1 354 ? 15.925  -36.888 -18.144 1.00 22.77 ? 353 GLU C N   1 
ATOM   9222  C  CA  . GLU C  1 354 ? 15.102  -38.065 -18.182 1.00 23.96 ? 353 GLU C CA  1 
ATOM   9223  C  C   . GLU C  1 354 ? 14.386  -38.305 -16.834 1.00 23.84 ? 353 GLU C C   1 
ATOM   9224  O  O   . GLU C  1 354 ? 14.977  -38.130 -15.768 1.00 23.67 ? 353 GLU C O   1 
ATOM   9225  C  CB  . GLU C  1 354 ? 15.954  -39.296 -18.542 1.00 26.02 ? 353 GLU C CB  1 
ATOM   9226  C  CG  . GLU C  1 354 ? 15.112  -40.502 -18.899 1.00 27.90 ? 353 GLU C CG  1 
ATOM   9227  C  CD  . GLU C  1 354 ? 15.926  -41.773 -19.072 1.00 31.76 ? 353 GLU C CD  1 
ATOM   9228  O  OE1 . GLU C  1 354 ? 17.162  -41.702 -19.002 1.00 35.58 ? 353 GLU C OE1 1 
ATOM   9229  O  OE2 . GLU C  1 354 ? 15.315  -42.847 -19.238 1.00 32.24 ? 353 GLU C OE2 1 
ATOM   9230  N  N   . LEU C  1 355 ? 13.116  -38.697 -16.913 1.00 22.75 ? 354 LEU C N   1 
ATOM   9231  C  CA  . LEU C  1 355 ? 12.296  -39.064 -15.754 1.00 23.51 ? 354 LEU C CA  1 
ATOM   9232  C  C   . LEU C  1 355 ? 11.818  -40.508 -15.922 1.00 23.83 ? 354 LEU C C   1 
ATOM   9233  O  O   . LEU C  1 355 ? 10.716  -40.741 -16.438 1.00 22.49 ? 354 LEU C O   1 
ATOM   9234  C  CB  . LEU C  1 355 ? 11.096  -38.130 -15.619 1.00 23.40 ? 354 LEU C CB  1 
ATOM   9235  C  CG  . LEU C  1 355 ? 11.445  -36.624 -15.551 1.00 24.36 ? 354 LEU C CG  1 
ATOM   9236  C  CD1 . LEU C  1 355 ? 10.176  -35.786 -15.642 1.00 24.48 ? 354 LEU C CD1 1 
ATOM   9237  C  CD2 . LEU C  1 355 ? 12.237  -36.303 -14.294 1.00 25.59 ? 354 LEU C CD2 1 
ATOM   9238  N  N   . PRO C  1 356 ? 12.659  -41.478 -15.531 1.00 25.29 ? 355 PRO C N   1 
ATOM   9239  C  CA  . PRO C  1 356 ? 12.290  -42.873 -15.805 1.00 26.27 ? 355 PRO C CA  1 
ATOM   9240  C  C   . PRO C  1 356 ? 11.115  -43.281 -14.935 1.00 26.10 ? 355 PRO C C   1 
ATOM   9241  O  O   . PRO C  1 356 ? 11.105  -43.013 -13.743 1.00 26.26 ? 355 PRO C O   1 
ATOM   9242  C  CB  . PRO C  1 356 ? 13.551  -43.682 -15.464 1.00 27.85 ? 355 PRO C CB  1 
ATOM   9243  C  CG  . PRO C  1 356 ? 14.590  -42.712 -15.068 1.00 28.30 ? 355 PRO C CG  1 
ATOM   9244  C  CD  . PRO C  1 356 ? 13.971  -41.362 -14.873 1.00 27.09 ? 355 PRO C CD  1 
ATOM   9245  N  N   . GLY C  1 357 ? 10.109  -43.862 -15.571 1.00 26.09 ? 356 GLY C N   1 
ATOM   9246  C  CA  . GLY C  1 357 ? 8.907   -44.316 -14.893 1.00 26.73 ? 356 GLY C CA  1 
ATOM   9247  C  C   . GLY C  1 357 ? 7.894   -43.220 -14.635 1.00 26.40 ? 356 GLY C C   1 
ATOM   9248  O  O   . GLY C  1 357 ? 6.945   -43.437 -13.897 1.00 28.56 ? 356 GLY C O   1 
ATOM   9249  N  N   . SER C  1 358 ? 8.076   -42.038 -15.221 1.00 24.79 ? 357 SER C N   1 
ATOM   9250  C  CA  . SER C  1 358 ? 7.158   -40.925 -14.959 1.00 24.40 ? 357 SER C CA  1 
ATOM   9251  C  C   . SER C  1 358 ? 6.115   -40.788 -16.080 1.00 23.07 ? 357 SER C C   1 
ATOM   9252  O  O   . SER C  1 358 ? 6.447   -40.485 -17.209 1.00 23.15 ? 357 SER C O   1 
ATOM   9253  C  CB  . SER C  1 358 ? 7.948   -39.634 -14.783 1.00 24.64 ? 357 SER C CB  1 
ATOM   9254  O  OG  . SER C  1 358 ? 7.130   -38.570 -14.358 1.00 26.45 ? 357 SER C OG  1 
ATOM   9255  N  N   . GLU C  1 359 ? 4.859   -41.027 -15.743 1.00 22.51 ? 358 GLU C N   1 
ATOM   9256  C  CA  . GLU C  1 359 ? 3.773   -40.959 -16.704 1.00 22.52 ? 358 GLU C CA  1 
ATOM   9257  C  C   . GLU C  1 359 ? 3.394   -39.496 -17.028 1.00 21.04 ? 358 GLU C C   1 
ATOM   9258  O  O   . GLU C  1 359 ? 3.571   -38.579 -16.212 1.00 20.10 ? 358 GLU C O   1 
ATOM   9259  C  CB  . GLU C  1 359 ? 2.578   -41.783 -16.199 1.00 24.35 ? 358 GLU C CB  1 
ATOM   9260  C  CG  . GLU C  1 359 ? 1.410   -41.929 -17.161 1.00 26.29 ? 358 GLU C CG  1 
ATOM   9261  C  CD  . GLU C  1 359 ? 0.438   -40.755 -17.108 1.00 28.03 ? 358 GLU C CD  1 
ATOM   9262  O  OE1 . GLU C  1 359 ? 0.329   -40.106 -16.034 1.00 29.32 ? 358 GLU C OE1 1 
ATOM   9263  O  OE2 . GLU C  1 359 ? -0.222  -40.473 -18.142 1.00 29.43 ? 358 GLU C OE2 1 
ATOM   9264  N  N   . HIS C  1 360 ? 2.863   -39.319 -18.231 1.00 19.79 ? 359 HIS C N   1 
ATOM   9265  C  CA  . HIS C  1 360 ? 2.597   -38.009 -18.807 1.00 19.25 ? 359 HIS C CA  1 
ATOM   9266  C  C   . HIS C  1 360 ? 1.897   -36.995 -17.880 1.00 19.94 ? 359 HIS C C   1 
ATOM   9267  O  O   . HIS C  1 360 ? 2.316   -35.849 -17.796 1.00 19.58 ? 359 HIS C O   1 
ATOM   9268  C  CB  . HIS C  1 360 ? 1.764   -38.181 -20.073 1.00 18.83 ? 359 HIS C CB  1 
ATOM   9269  C  CG  . HIS C  1 360 ? 1.621   -36.922 -20.870 1.00 18.59 ? 359 HIS C CG  1 
ATOM   9270  N  ND1 . HIS C  1 360 ? 2.699   -36.303 -21.466 1.00 18.41 ? 359 HIS C ND1 1 
ATOM   9271  C  CD2 . HIS C  1 360 ? 0.536   -36.172 -21.180 1.00 18.38 ? 359 HIS C CD2 1 
ATOM   9272  C  CE1 . HIS C  1 360 ? 2.289   -35.226 -22.113 1.00 18.01 ? 359 HIS C CE1 1 
ATOM   9273  N  NE2 . HIS C  1 360 ? 0.978   -35.129 -21.968 1.00 18.52 ? 359 HIS C NE2 1 
ATOM   9274  N  N   . ILE C  1 361 ? 0.809   -37.400 -17.258 1.00 20.89 ? 360 ILE C N   1 
ATOM   9275  C  CA  . ILE C  1 361 ? 0.066   -36.516 -16.366 1.00 23.35 ? 360 ILE C CA  1 
ATOM   9276  C  C   . ILE C  1 361 ? 0.627   -36.547 -14.949 1.00 24.03 ? 360 ILE C C   1 
ATOM   9277  O  O   . ILE C  1 361 ? 0.742   -35.508 -14.303 1.00 23.55 ? 360 ILE C O   1 
ATOM   9278  C  CB  . ILE C  1 361 ? -1.420  -36.896 -16.332 1.00 26.15 ? 360 ILE C CB  1 
ATOM   9279  C  CG1 . ILE C  1 361 ? -2.032  -36.707 -17.710 1.00 28.65 ? 360 ILE C CG1 1 
ATOM   9280  C  CG2 . ILE C  1 361 ? -2.141  -36.020 -15.317 1.00 28.33 ? 360 ILE C CG2 1 
ATOM   9281  C  CD1 . ILE C  1 361 ? -3.438  -37.263 -17.827 1.00 32.43 ? 360 ILE C CD1 1 
ATOM   9282  N  N   . GLU C  1 362 ? 1.010   -37.731 -14.482 1.00 24.71 ? 361 GLU C N   1 
ATOM   9283  C  CA  . GLU C  1 362 ? 1.513   -37.872 -13.110 1.00 27.51 ? 361 GLU C CA  1 
ATOM   9284  C  C   . GLU C  1 362 ? 2.777   -37.067 -12.880 1.00 25.51 ? 361 GLU C C   1 
ATOM   9285  O  O   . GLU C  1 362 ? 3.044   -36.652 -11.754 1.00 24.57 ? 361 GLU C O   1 
ATOM   9286  C  CB  . GLU C  1 362 ? 1.741   -39.337 -12.759 1.00 30.87 ? 361 GLU C CB  1 
ATOM   9287  C  CG  . GLU C  1 362 ? 0.433   -40.100 -12.649 1.00 36.83 ? 361 GLU C CG  1 
ATOM   9288  C  CD  . GLU C  1 362 ? 0.603   -41.594 -12.438 1.00 42.25 ? 361 GLU C CD  1 
ATOM   9289  O  OE1 . GLU C  1 362 ? 1.741   -42.070 -12.234 1.00 48.50 ? 361 GLU C OE1 1 
ATOM   9290  O  OE2 . GLU C  1 362 ? -0.423  -42.302 -12.481 1.00 48.90 ? 361 GLU C OE2 1 
ATOM   9291  N  N   . MET C  1 363 ? 3.521   -36.772 -13.946 1.00 24.57 ? 362 MET C N   1 
ATOM   9292  C  CA  . MET C  1 363 ? 4.760   -35.984 -13.778 1.00 24.47 ? 362 MET C CA  1 
ATOM   9293  C  C   . MET C  1 363 ? 4.521   -34.604 -13.154 1.00 23.59 ? 362 MET C C   1 
ATOM   9294  O  O   . MET C  1 363 ? 5.411   -34.074 -12.511 1.00 21.64 ? 362 MET C O   1 
ATOM   9295  C  CB  . MET C  1 363 ? 5.552   -35.857 -15.085 1.00 26.69 ? 362 MET C CB  1 
ATOM   9296  C  CG  . MET C  1 363 ? 5.062   -34.892 -16.141 1.00 28.67 ? 362 MET C CG  1 
ATOM   9297  S  SD  . MET C  1 363 ? 6.350   -34.633 -17.421 1.00 32.41 ? 362 MET C SD  1 
ATOM   9298  C  CE  . MET C  1 363 ? 6.556   -36.299 -18.092 1.00 31.66 ? 362 MET C CE  1 
ATOM   9299  N  N   . LEU C  1 364 ? 3.318   -34.056 -13.317 1.00 22.63 ? 363 LEU C N   1 
ATOM   9300  C  CA  . LEU C  1 364 ? 2.970   -32.752 -12.756 1.00 24.03 ? 363 LEU C CA  1 
ATOM   9301  C  C   . LEU C  1 364 ? 2.817   -32.700 -11.241 1.00 24.55 ? 363 LEU C C   1 
ATOM   9302  O  O   . LEU C  1 364 ? 2.870   -31.604 -10.678 1.00 26.69 ? 363 LEU C O   1 
ATOM   9303  C  CB  . LEU C  1 364 ? 1.671   -32.227 -13.376 1.00 26.05 ? 363 LEU C CB  1 
ATOM   9304  C  CG  . LEU C  1 364 ? 1.737   -31.564 -14.746 1.00 26.75 ? 363 LEU C CG  1 
ATOM   9305  C  CD1 . LEU C  1 364 ? 0.359   -30.972 -15.038 1.00 29.51 ? 363 LEU C CD1 1 
ATOM   9306  C  CD2 . LEU C  1 364 ? 2.761   -30.442 -14.811 1.00 26.54 ? 363 LEU C CD2 1 
ATOM   9307  N  N   . ALA C  1 365 ? 2.605   -33.851 -10.610 1.00 23.15 ? 364 ALA C N   1 
ATOM   9308  C  CA  . ALA C  1 365 ? 2.431   -33.960 -9.182  1.00 26.07 ? 364 ALA C CA  1 
ATOM   9309  C  C   . ALA C  1 365 ? 3.529   -34.802 -8.558  1.00 26.97 ? 364 ALA C C   1 
ATOM   9310  O  O   . ALA C  1 365 ? 3.468   -35.134 -7.391  1.00 29.69 ? 364 ALA C O   1 
ATOM   9311  C  CB  . ALA C  1 365 ? 1.068   -34.543 -8.857  1.00 26.15 ? 364 ALA C CB  1 
ATOM   9312  N  N   . ASN C  1 366 ? 4.561   -35.105 -9.323  1.00 25.64 ? 365 ASN C N   1 
ATOM   9313  C  CA  . ASN C  1 366 ? 5.607   -36.017 -8.886  1.00 25.75 ? 365 ASN C CA  1 
ATOM   9314  C  C   . ASN C  1 366 ? 6.704   -35.249 -8.145  1.00 25.25 ? 365 ASN C C   1 
ATOM   9315  O  O   . ASN C  1 366 ? 7.158   -34.204 -8.609  1.00 23.59 ? 365 ASN C O   1 
ATOM   9316  C  CB  . ASN C  1 366 ? 6.132   -36.750 -10.131 1.00 26.45 ? 365 ASN C CB  1 
ATOM   9317  C  CG  . ASN C  1 366 ? 7.247   -37.724 -9.835  1.00 29.16 ? 365 ASN C CG  1 
ATOM   9318  O  OD1 . ASN C  1 366 ? 8.279   -37.357 -9.273  1.00 31.37 ? 365 ASN C OD1 1 
ATOM   9319  N  ND2 . ASN C  1 366 ? 7.051   -38.985 -10.225 1.00 29.02 ? 365 ASN C ND2 1 
ATOM   9320  N  N   . ALA C  1 367 ? 7.102   -35.773 -6.987  1.00 24.92 ? 366 ALA C N   1 
ATOM   9321  C  CA  . ALA C  1 367 ? 8.063   -35.118 -6.098  1.00 25.77 ? 366 ALA C CA  1 
ATOM   9322  C  C   . ALA C  1 367 ? 9.418   -34.863 -6.744  1.00 25.02 ? 366 ALA C C   1 
ATOM   9323  O  O   . ALA C  1 367 ? 10.051  -33.848 -6.466  1.00 24.82 ? 366 ALA C O   1 
ATOM   9324  C  CB  . ALA C  1 367 ? 8.245   -35.927 -4.826  1.00 27.30 ? 366 ALA C CB  1 
ATOM   9325  N  N   . THR C  1 368 ? 9.852   -35.753 -7.629  1.00 25.20 ? 367 THR C N   1 
ATOM   9326  C  CA  . THR C  1 368 ? 11.088  -35.533 -8.382  1.00 25.83 ? 367 THR C CA  1 
ATOM   9327  C  C   . THR C  1 368 ? 10.983  -34.367 -9.368  1.00 23.76 ? 367 THR C C   1 
ATOM   9328  O  O   . THR C  1 368 ? 11.912  -33.573 -9.506  1.00 23.23 ? 367 THR C O   1 
ATOM   9329  C  CB  . THR C  1 368 ? 11.498  -36.824 -9.110  1.00 28.49 ? 367 THR C CB  1 
ATOM   9330  O  OG1 . THR C  1 368 ? 11.637  -37.854 -8.118  1.00 29.82 ? 367 THR C OG1 1 
ATOM   9331  C  CG2 . THR C  1 368 ? 12.813  -36.665 -9.878  1.00 29.65 ? 367 THR C CG2 1 
ATOM   9332  N  N   . THR C  1 369 ? 9.851   -34.246 -10.043 1.00 22.44 ? 368 THR C N   1 
ATOM   9333  C  CA  . THR C  1 369 ? 9.617   -33.114 -10.933 1.00 21.79 ? 368 THR C CA  1 
ATOM   9334  C  C   . THR C  1 369 ? 9.652   -31.813 -10.150 1.00 21.37 ? 368 THR C C   1 
ATOM   9335  O  O   . THR C  1 369 ? 10.255  -30.825 -10.575 1.00 20.39 ? 368 THR C O   1 
ATOM   9336  C  CB  . THR C  1 369 ? 8.247   -33.196 -11.632 1.00 21.57 ? 368 THR C CB  1 
ATOM   9337  O  OG1 . THR C  1 369 ? 8.120   -34.442 -12.326 1.00 21.87 ? 368 THR C OG1 1 
ATOM   9338  C  CG2 . THR C  1 369 ? 8.064   -32.053 -12.616 1.00 21.23 ? 368 THR C CG2 1 
ATOM   9339  N  N   . LEU C  1 370 ? 8.967   -31.818 -9.011  1.00 21.57 ? 369 LEU C N   1 
ATOM   9340  C  CA  . LEU C  1 370 ? 8.839   -30.615 -8.195  1.00 21.79 ? 369 LEU C CA  1 
ATOM   9341  C  C   . LEU C  1 370 ? 10.200  -30.244 -7.569  1.00 21.84 ? 369 LEU C C   1 
ATOM   9342  O  O   . LEU C  1 370 ? 10.521  -29.065 -7.475  1.00 22.01 ? 369 LEU C O   1 
ATOM   9343  C  CB  . LEU C  1 370 ? 7.761   -30.807 -7.132  1.00 22.80 ? 369 LEU C CB  1 
ATOM   9344  C  CG  . LEU C  1 370 ? 6.369   -31.029 -7.717  1.00 23.40 ? 369 LEU C CG  1 
ATOM   9345  C  CD1 . LEU C  1 370 ? 5.361   -31.436 -6.644  1.00 24.79 ? 369 LEU C CD1 1 
ATOM   9346  C  CD2 . LEU C  1 370 ? 5.899   -29.797 -8.454  1.00 24.08 ? 369 LEU C CD2 1 
ATOM   9347  N  N   . ALA C  1 371 ? 11.004  -31.239 -7.189  1.00 22.30 ? 370 ALA C N   1 
ATOM   9348  C  CA  . ALA C  1 371 ? 12.353  -30.983 -6.687  1.00 22.65 ? 370 ALA C CA  1 
ATOM   9349  C  C   . ALA C  1 371 ? 13.216  -30.337 -7.766  1.00 22.34 ? 370 ALA C C   1 
ATOM   9350  O  O   . ALA C  1 371 ? 14.031  -29.480 -7.457  1.00 22.50 ? 370 ALA C O   1 
ATOM   9351  C  CB  . ALA C  1 371 ? 13.009  -32.277 -6.171  1.00 23.99 ? 370 ALA C CB  1 
ATOM   9352  N  N   . TYR C  1 372 ? 13.063  -30.771 -9.020  1.00 21.67 ? 371 TYR C N   1 
ATOM   9353  C  CA  . TYR C  1 372 ? 13.827  -30.194 -10.137 1.00 21.66 ? 371 TYR C CA  1 
ATOM   9354  C  C   . TYR C  1 372 ? 13.423  -28.719 -10.326 1.00 21.00 ? 371 TYR C C   1 
ATOM   9355  O  O   . TYR C  1 372 ? 14.267  -27.828 -10.418 1.00 20.71 ? 371 TYR C O   1 
ATOM   9356  C  CB  . TYR C  1 372 ? 13.626  -30.977 -11.429 1.00 21.55 ? 371 TYR C CB  1 
ATOM   9357  C  CG  . TYR C  1 372 ? 14.557  -30.547 -12.540 1.00 22.74 ? 371 TYR C CG  1 
ATOM   9358  C  CD1 . TYR C  1 372 ? 14.311  -29.396 -13.288 1.00 22.00 ? 371 TYR C CD1 1 
ATOM   9359  C  CD2 . TYR C  1 372 ? 15.715  -31.283 -12.835 1.00 24.07 ? 371 TYR C CD2 1 
ATOM   9360  C  CE1 . TYR C  1 372 ? 15.183  -28.997 -14.291 1.00 23.05 ? 371 TYR C CE1 1 
ATOM   9361  C  CE2 . TYR C  1 372 ? 16.567  -30.898 -13.861 1.00 24.68 ? 371 TYR C CE2 1 
ATOM   9362  C  CZ  . TYR C  1 372 ? 16.310  -29.745 -14.575 1.00 23.77 ? 371 TYR C CZ  1 
ATOM   9363  O  OH  . TYR C  1 372 ? 17.188  -29.344 -15.584 1.00 24.97 ? 371 TYR C OH  1 
ATOM   9364  N  N   . LEU C  1 373 ? 12.133  -28.470 -10.359 1.00 19.80 ? 372 LEU C N   1 
ATOM   9365  C  CA  . LEU C  1 373 ? 11.638  -27.110 -10.481 1.00 20.15 ? 372 LEU C CA  1 
ATOM   9366  C  C   . LEU C  1 373 ? 12.117  -26.210 -9.321  1.00 20.53 ? 372 LEU C C   1 
ATOM   9367  O  O   . LEU C  1 373 ? 12.511  -25.065 -9.536  1.00 20.13 ? 372 LEU C O   1 
ATOM   9368  C  CB  . LEU C  1 373 ? 10.106  -27.135 -10.573 1.00 19.93 ? 372 LEU C CB  1 
ATOM   9369  C  CG  . LEU C  1 373 ? 9.452   -25.769 -10.715 1.00 20.39 ? 372 LEU C CG  1 
ATOM   9370  C  CD1 . LEU C  1 373 ? 9.866   -25.063 -12.001 1.00 20.45 ? 372 LEU C CD1 1 
ATOM   9371  C  CD2 . LEU C  1 373 ? 7.936   -25.938 -10.650 1.00 20.39 ? 372 LEU C CD2 1 
ATOM   9372  N  N   . LYS C  1 374 ? 12.090  -26.736 -8.101  1.00 21.49 ? 373 LYS C N   1 
ATOM   9373  C  CA  . LYS C  1 374 ? 12.568  -25.995 -6.948  1.00 23.28 ? 373 LYS C CA  1 
ATOM   9374  C  C   . LYS C  1 374 ? 14.023  -25.526 -7.132  1.00 24.31 ? 373 LYS C C   1 
ATOM   9375  O  O   . LYS C  1 374 ? 14.355  -24.389 -6.787  1.00 24.04 ? 373 LYS C O   1 
ATOM   9376  C  CB  . LYS C  1 374 ? 12.462  -26.822 -5.670  1.00 24.79 ? 373 LYS C CB  1 
ATOM   9377  C  CG  . LYS C  1 374 ? 12.631  -25.967 -4.419  1.00 25.65 ? 373 LYS C CG  1 
ATOM   9378  C  CD  . LYS C  1 374 ? 12.536  -26.791 -3.163  1.00 27.50 ? 373 LYS C CD  1 
ATOM   9379  C  CE  . LYS C  1 374 ? 12.538  -25.876 -1.944  1.00 28.99 ? 373 LYS C CE  1 
ATOM   9380  N  NZ  . LYS C  1 374 ? 12.397  -26.724 -0.739  1.00 30.95 ? 373 LYS C NZ  1 
ATOM   9381  N  N   . ARG C  1 375 ? 14.875  -26.408 -7.641  1.00 25.05 ? 374 ARG C N   1 
ATOM   9382  C  CA  A ARG C  1 375 ? 16.278  -26.077 -7.905  0.50 26.58 ? 374 ARG C CA  1 
ATOM   9383  C  CA  B ARG C  1 375 ? 16.281  -26.079 -7.908  0.50 26.95 ? 374 ARG C CA  1 
ATOM   9384  C  C   . ARG C  1 375 ? 16.406  -24.985 -8.977  1.00 24.98 ? 374 ARG C C   1 
ATOM   9385  O  O   . ARG C  1 375 ? 17.219  -24.073 -8.838  1.00 24.98 ? 374 ARG C O   1 
ATOM   9386  C  CB  A ARG C  1 375 ? 17.053  -27.336 -8.317  0.50 28.72 ? 374 ARG C CB  1 
ATOM   9387  C  CB  B ARG C  1 375 ? 17.066  -27.333 -8.334  0.50 29.92 ? 374 ARG C CB  1 
ATOM   9388  C  CG  A ARG C  1 375 ? 18.527  -27.125 -8.648  0.50 31.47 ? 374 ARG C CG  1 
ATOM   9389  C  CG  B ARG C  1 375 ? 18.529  -27.076 -8.725  0.50 33.66 ? 374 ARG C CG  1 
ATOM   9390  C  CD  A ARG C  1 375 ? 19.325  -26.640 -7.456  0.50 33.89 ? 374 ARG C CD  1 
ATOM   9391  C  CD  B ARG C  1 375 ? 19.129  -28.226 -9.535  0.50 36.98 ? 374 ARG C CD  1 
ATOM   9392  N  NE  A ARG C  1 375 ? 20.712  -26.360 -7.822  0.50 36.24 ? 374 ARG C NE  1 
ATOM   9393  N  NE  B ARG C  1 375 ? 19.675  -27.787 -10.830 0.50 39.06 ? 374 ARG C NE  1 
ATOM   9394  C  CZ  A ARG C  1 375 ? 21.102  -25.282 -8.499  0.50 37.55 ? 374 ARG C CZ  1 
ATOM   9395  C  CZ  B ARG C  1 375 ? 18.955  -27.656 -11.944 0.50 39.16 ? 374 ARG C CZ  1 
ATOM   9396  N  NH1 A ARG C  1 375 ? 22.380  -25.107 -8.788  0.50 39.58 ? 374 ARG C NH1 1 
ATOM   9397  N  NH1 B ARG C  1 375 ? 19.523  -27.251 -13.070 0.50 39.48 ? 374 ARG C NH1 1 
ATOM   9398  N  NH2 A ARG C  1 375 ? 20.214  -24.383 -8.897  0.50 37.25 ? 374 ARG C NH2 1 
ATOM   9399  N  NH2 B ARG C  1 375 ? 17.660  -27.928 -11.931 0.50 39.06 ? 374 ARG C NH2 1 
ATOM   9400  N  N   . VAL C  1 376 ? 15.590  -25.063 -10.034 1.00 23.55 ? 375 VAL C N   1 
ATOM   9401  C  CA  . VAL C  1 376 ? 15.584  -24.034 -11.089 1.00 22.77 ? 375 VAL C CA  1 
ATOM   9402  C  C   . VAL C  1 376 ? 15.200  -22.671 -10.493 1.00 22.91 ? 375 VAL C C   1 
ATOM   9403  O  O   . VAL C  1 376 ? 15.831  -21.665 -10.788 1.00 23.47 ? 375 VAL C O   1 
ATOM   9404  C  CB  . VAL C  1 376 ? 14.624  -24.390 -12.271 1.00 22.71 ? 375 VAL C CB  1 
ATOM   9405  C  CG1 . VAL C  1 376 ? 14.499  -23.238 -13.263 1.00 22.55 ? 375 VAL C CG1 1 
ATOM   9406  C  CG2 . VAL C  1 376 ? 15.101  -25.623 -13.008 1.00 23.44 ? 375 VAL C CG2 1 
ATOM   9407  N  N   . LEU C  1 377 ? 14.166  -22.642 -9.651  1.00 22.96 ? 376 LEU C N   1 
ATOM   9408  C  CA  . LEU C  1 377 ? 13.629  -21.384 -9.118  1.00 23.53 ? 376 LEU C CA  1 
ATOM   9409  C  C   . LEU C  1 377 ? 14.445  -20.786 -7.974  1.00 26.68 ? 376 LEU C C   1 
ATOM   9410  O  O   . LEU C  1 377 ? 14.692  -19.589 -7.947  1.00 25.69 ? 376 LEU C O   1 
ATOM   9411  C  CB  . LEU C  1 377 ? 12.181  -21.585 -8.658  1.00 22.84 ? 376 LEU C CB  1 
ATOM   9412  C  CG  . LEU C  1 377 ? 11.202  -22.004 -9.747  1.00 21.64 ? 376 LEU C CG  1 
ATOM   9413  C  CD1 . LEU C  1 377 ? 9.791   -22.152 -9.193  1.00 21.90 ? 376 LEU C CD1 1 
ATOM   9414  C  CD2 . LEU C  1 377 ? 11.205  -21.015 -10.918 1.00 21.80 ? 376 LEU C CD2 1 
ATOM   9415  N  N   . LEU C  1 378 ? 14.822  -21.623 -7.019  1.00 28.80 ? 377 LEU C N   1 
ATOM   9416  C  CA  . LEU C  1 378 ? 15.361  -21.171 -5.748  1.00 33.52 ? 377 LEU C CA  1 
ATOM   9417  C  C   . LEU C  1 378 ? 16.857  -21.354 -5.632  1.00 38.15 ? 377 LEU C C   1 
ATOM   9418  O  O   . LEU C  1 378 ? 17.457  -20.858 -4.677  1.00 39.09 ? 377 LEU C O   1 
ATOM   9419  C  CB  . LEU C  1 378 ? 14.678  -21.913 -4.599  1.00 34.30 ? 377 LEU C CB  1 
ATOM   9420  C  CG  . LEU C  1 378 ? 13.216  -21.532 -4.373  1.00 36.94 ? 377 LEU C CG  1 
ATOM   9421  C  CD1 . LEU C  1 378 ? 12.672  -22.385 -3.247  1.00 38.10 ? 377 LEU C CD1 1 
ATOM   9422  C  CD2 . LEU C  1 378 ? 12.967  -20.058 -4.095  1.00 39.85 ? 377 LEU C CD2 1 
ATOM   9423  N  N   . GLY C  1 379 ? 17.461  -22.087 -6.558  1.00 39.73 ? 378 GLY C N   1 
ATOM   9424  C  CA  . GLY C  1 379 ? 18.906  -22.156 -6.630  1.00 45.81 ? 378 GLY C CA  1 
ATOM   9425  C  C   . GLY C  1 379 ? 19.452  -23.301 -5.808  1.00 53.22 ? 378 GLY C C   1 
ATOM   9426  O  O   . GLY C  1 379 ? 18.675  -24.087 -5.256  1.00 53.21 ? 378 GLY C O   1 
ATOM   9427  N  N   . PRO C  1 380 ? 20.801  -23.403 -5.721  1.00 62.22 ? 379 PRO C N   1 
ATOM   9428  C  CA  . PRO C  1 380 ? 21.489  -24.564 -5.130  1.00 66.13 ? 379 PRO C CA  1 
ATOM   9429  C  C   . PRO C  1 380 ? 21.325  -24.674 -3.615  1.00 68.64 ? 379 PRO C C   1 
ATOM   9430  O  O   . PRO C  1 380 ? 21.005  -23.682 -2.962  1.00 74.54 ? 379 PRO C O   1 
ATOM   9431  C  CB  . PRO C  1 380 ? 22.962  -24.326 -5.496  1.00 66.68 ? 379 PRO C CB  1 
ATOM   9432  C  CG  . PRO C  1 380 ? 23.084  -22.850 -5.689  1.00 66.62 ? 379 PRO C CG  1 
ATOM   9433  C  CD  . PRO C  1 380 ? 21.750  -22.365 -6.182  1.00 62.81 ? 379 PRO C CD  1 
ATOM   9434  N  N   . HIS D  1 5   ? -18.549 10.717  -0.015  1.00 32.88 ? 4   HIS D N   1 
ATOM   9435  C  CA  . HIS D  1 5   ? -17.860 11.259  -1.192  1.00 30.18 ? 4   HIS D CA  1 
ATOM   9436  C  C   . HIS D  1 5   ? -17.396 10.177  -2.146  1.00 28.18 ? 4   HIS D C   1 
ATOM   9437  O  O   . HIS D  1 5   ? -17.005 9.102   -1.745  1.00 28.68 ? 4   HIS D O   1 
ATOM   9438  C  CB  . HIS D  1 5   ? -16.674 12.104  -0.774  1.00 31.33 ? 4   HIS D CB  1 
ATOM   9439  C  CG  . HIS D  1 5   ? -15.625 11.375  0.015   1.00 32.48 ? 4   HIS D CG  1 
ATOM   9440  N  ND1 . HIS D  1 5   ? -15.279 11.767  1.285   1.00 33.53 ? 4   HIS D ND1 1 
ATOM   9441  C  CD2 . HIS D  1 5   ? -14.820 10.329  -0.287  1.00 32.08 ? 4   HIS D CD2 1 
ATOM   9442  C  CE1 . HIS D  1 5   ? -14.301 11.000  1.735   1.00 34.88 ? 4   HIS D CE1 1 
ATOM   9443  N  NE2 . HIS D  1 5   ? -14.007 10.112  0.800   1.00 32.86 ? 4   HIS D NE2 1 
ATOM   9444  N  N   . PRO D  1 6   ? -17.384 10.493  -3.428  1.00 24.61 ? 5   PRO D N   1 
ATOM   9445  C  CA  . PRO D  1 6   ? -17.094 9.445   -4.393  1.00 23.71 ? 5   PRO D CA  1 
ATOM   9446  C  C   . PRO D  1 6   ? -15.596 9.165   -4.534  1.00 20.86 ? 5   PRO D C   1 
ATOM   9447  O  O   . PRO D  1 6   ? -14.774 10.077  -4.293  1.00 20.87 ? 5   PRO D O   1 
ATOM   9448  C  CB  . PRO D  1 6   ? -17.629 10.036  -5.681  1.00 24.55 ? 5   PRO D CB  1 
ATOM   9449  C  CG  . PRO D  1 6   ? -17.413 11.510  -5.507  1.00 25.29 ? 5   PRO D CG  1 
ATOM   9450  C  CD  . PRO D  1 6   ? -17.689 11.789  -4.061  1.00 26.19 ? 5   PRO D CD  1 
ATOM   9451  N  N   . PRO D  1 7   ? -15.238 7.939   -4.920  1.00 19.39 ? 6   PRO D N   1 
ATOM   9452  C  CA  . PRO D  1 7   ? -13.818 7.652   -5.196  1.00 18.13 ? 6   PRO D CA  1 
ATOM   9453  C  C   . PRO D  1 7   ? -13.269 8.502   -6.339  1.00 17.52 ? 6   PRO D C   1 
ATOM   9454  O  O   . PRO D  1 7   ? -14.011 8.881   -7.249  1.00 16.41 ? 6   PRO D O   1 
ATOM   9455  C  CB  . PRO D  1 7   ? -13.786 6.143   -5.521  1.00 18.80 ? 6   PRO D CB  1 
ATOM   9456  C  CG  . PRO D  1 7   ? -15.201 5.644   -5.449  1.00 20.27 ? 6   PRO D CG  1 
ATOM   9457  C  CD  . PRO D  1 7   ? -16.124 6.800   -5.206  1.00 19.83 ? 6   PRO D CD  1 
ATOM   9458  N  N   . VAL D  1 8   ? -11.974 8.789   -6.282  1.00 16.43 ? 7   VAL D N   1 
ATOM   9459  C  CA  . VAL D  1 8   ? -11.330 9.706   -7.208  1.00 15.96 ? 7   VAL D CA  1 
ATOM   9460  C  C   . VAL D  1 8   ? -10.112 9.026   -7.817  1.00 15.14 ? 7   VAL D C   1 
ATOM   9461  O  O   . VAL D  1 8   ? -9.299  8.443   -7.082  1.00 14.06 ? 7   VAL D O   1 
ATOM   9462  C  CB  . VAL D  1 8   ? -10.889 10.990  -6.485  1.00 16.25 ? 7   VAL D CB  1 
ATOM   9463  C  CG1 . VAL D  1 8   ? -10.004 11.856  -7.360  1.00 16.31 ? 7   VAL D CG1 1 
ATOM   9464  C  CG2 . VAL D  1 8   ? -12.098 11.817  -6.051  1.00 17.51 ? 7   VAL D CG2 1 
ATOM   9465  N  N   . VAL D  1 9   ? -9.979  9.148   -9.137  1.00 14.83 ? 8   VAL D N   1 
ATOM   9466  C  CA  . VAL D  1 9   ? -8.773  8.742   -9.851  1.00 15.02 ? 8   VAL D CA  1 
ATOM   9467  C  C   . VAL D  1 9   ? -8.132  9.983   -10.513 1.00 15.21 ? 8   VAL D C   1 
ATOM   9468  O  O   . VAL D  1 9   ? -8.815  10.746  -11.193 1.00 15.05 ? 8   VAL D O   1 
ATOM   9469  C  CB  . VAL D  1 9   ? -9.076  7.670   -10.909 1.00 15.07 ? 8   VAL D CB  1 
ATOM   9470  C  CG1 . VAL D  1 9   ? -7.870  7.396   -11.780 1.00 15.15 ? 8   VAL D CG1 1 
ATOM   9471  C  CG2 . VAL D  1 9   ? -9.565  6.373   -10.244 1.00 15.57 ? 8   VAL D CG2 1 
ATOM   9472  N  N   . LEU D  1 10  ? -6.841  10.172  -10.259 1.00 14.75 ? 9   LEU D N   1 
ATOM   9473  C  CA  . LEU D  1 10  ? -6.068  11.300  -10.746 1.00 15.09 ? 9   LEU D CA  1 
ATOM   9474  C  C   . LEU D  1 10  ? -5.218  10.872  -11.953 1.00 14.74 ? 9   LEU D C   1 
ATOM   9475  O  O   . LEU D  1 10  ? -4.495  9.846   -11.892 1.00 14.03 ? 9   LEU D O   1 
ATOM   9476  C  CB  . LEU D  1 10  ? -5.148  11.832  -9.640  1.00 15.94 ? 9   LEU D CB  1 
ATOM   9477  C  CG  . LEU D  1 10  ? -5.784  12.169  -8.282  1.00 16.76 ? 9   LEU D CG  1 
ATOM   9478  C  CD1 . LEU D  1 10  ? -4.735  12.533  -7.255  1.00 17.98 ? 9   LEU D CD1 1 
ATOM   9479  C  CD2 . LEU D  1 10  ? -6.790  13.297  -8.407  1.00 17.80 ? 9   LEU D CD2 1 
ATOM   9480  N  N   . VAL D  1 11  ? -5.324  11.635  -13.045 1.00 14.25 ? 10  VAL D N   1 
ATOM   9481  C  CA  . VAL D  1 11  ? -4.641  11.307  -14.298 1.00 13.45 ? 10  VAL D CA  1 
ATOM   9482  C  C   . VAL D  1 11  ? -3.733  12.483  -14.661 1.00 13.42 ? 10  VAL D C   1 
ATOM   9483  O  O   . VAL D  1 11  ? -4.217  13.596  -14.870 1.00 13.02 ? 10  VAL D O   1 
ATOM   9484  C  CB  . VAL D  1 11  ? -5.617  11.006  -15.455 1.00 13.79 ? 10  VAL D CB  1 
ATOM   9485  C  CG1 . VAL D  1 11  ? -4.850  10.554  -16.680 1.00 13.51 ? 10  VAL D CG1 1 
ATOM   9486  C  CG2 . VAL D  1 11  ? -6.658  9.968   -15.050 1.00 14.48 ? 10  VAL D CG2 1 
ATOM   9487  N  N   . PRO D  1 12  ? -2.415  12.249  -14.678 1.00 12.53 ? 11  PRO D N   1 
ATOM   9488  C  CA  . PRO D  1 12  ? -1.479  13.349  -14.852 1.00 12.70 ? 11  PRO D CA  1 
ATOM   9489  C  C   . PRO D  1 12  ? -1.251  13.703  -16.316 1.00 13.34 ? 11  PRO D C   1 
ATOM   9490  O  O   . PRO D  1 12  ? -1.652  12.960  -17.197 1.00 12.92 ? 11  PRO D O   1 
ATOM   9491  C  CB  . PRO D  1 12  ? -0.170  12.777  -14.268 1.00 12.71 ? 11  PRO D CB  1 
ATOM   9492  C  CG  . PRO D  1 12  ? -0.244  11.322  -14.558 1.00 12.90 ? 11  PRO D CG  1 
ATOM   9493  C  CD  . PRO D  1 12  ? -1.720  10.983  -14.399 1.00 12.77 ? 11  PRO D CD  1 
ATOM   9494  N  N   . GLY D  1 13  ? -0.537  14.797  -16.549 1.00 14.03 ? 12  GLY D N   1 
ATOM   9495  C  CA  . GLY D  1 13  ? -0.151  15.179  -17.886 1.00 15.29 ? 12  GLY D CA  1 
ATOM   9496  C  C   . GLY D  1 13  ? 1.264   14.749  -18.234 1.00 16.09 ? 12  GLY D C   1 
ATOM   9497  O  O   . GLY D  1 13  ? 1.885   13.924  -17.550 1.00 15.85 ? 12  GLY D O   1 
ATOM   9498  N  N   . ASP D  1 14  ? 1.757   15.320  -19.332 1.00 16.44 ? 13  ASP D N   1 
ATOM   9499  C  CA  . ASP D  1 14  ? 3.121   15.088  -19.799 1.00 17.16 ? 13  ASP D CA  1 
ATOM   9500  C  C   . ASP D  1 14  ? 4.117   15.506  -18.711 1.00 16.56 ? 13  ASP D C   1 
ATOM   9501  O  O   . ASP D  1 14  ? 3.953   16.536  -18.059 1.00 17.05 ? 13  ASP D O   1 
ATOM   9502  C  CB  . ASP D  1 14  ? 3.320   15.874  -21.113 1.00 17.71 ? 13  ASP D CB  1 
ATOM   9503  C  CG  . ASP D  1 14  ? 4.450   15.337  -21.994 1.00 19.68 ? 13  ASP D CG  1 
ATOM   9504  O  OD1 . ASP D  1 14  ? 5.190   14.377  -21.620 1.00 19.04 ? 13  ASP D OD1 1 
ATOM   9505  O  OD2 . ASP D  1 14  ? 4.577   15.895  -23.126 1.00 21.80 ? 13  ASP D OD2 1 
ATOM   9506  N  N   . LEU D  1 15  ? 5.149   14.697  -18.502 1.00 16.71 ? 14  LEU D N   1 
ATOM   9507  C  CA  . LEU D  1 15  ? 6.131   14.897  -17.439 1.00 16.76 ? 14  LEU D CA  1 
ATOM   9508  C  C   . LEU D  1 15  ? 5.549   14.716  -16.035 1.00 15.95 ? 14  LEU D C   1 
ATOM   9509  O  O   . LEU D  1 15  ? 6.211   15.039  -15.057 1.00 16.29 ? 14  LEU D O   1 
ATOM   9510  C  CB  . LEU D  1 15  ? 6.789   16.289  -17.511 1.00 18.15 ? 14  LEU D CB  1 
ATOM   9511  C  CG  . LEU D  1 15  ? 7.327   16.764  -18.866 1.00 20.72 ? 14  LEU D CG  1 
ATOM   9512  C  CD1 . LEU D  1 15  ? 7.990   18.116  -18.686 1.00 21.33 ? 14  LEU D CD1 1 
ATOM   9513  C  CD2 . LEU D  1 15  ? 8.323   15.763  -19.408 1.00 22.07 ? 14  LEU D CD2 1 
ATOM   9514  N  N   . GLY D  1 16  ? 4.314   14.230  -15.949 1.00 14.83 ? 15  GLY D N   1 
ATOM   9515  C  CA  . GLY D  1 16  ? 3.509   14.377  -14.735 1.00 14.90 ? 15  GLY D CA  1 
ATOM   9516  C  C   . GLY D  1 16  ? 3.534   13.224  -13.744 1.00 14.87 ? 15  GLY D C   1 
ATOM   9517  O  O   . GLY D  1 16  ? 2.748   13.204  -12.802 1.00 14.88 ? 15  GLY D O   1 
ATOM   9518  N  N   . ASN D  1 17  ? 4.447   12.267  -13.930 1.00 13.99 ? 16  ASN D N   1 
ATOM   9519  C  CA  . ASN D  1 17  ? 4.712   11.281  -12.893 1.00 14.17 ? 16  ASN D CA  1 
ATOM   9520  C  C   . ASN D  1 17  ? 6.156   10.803  -12.963 1.00 14.39 ? 16  ASN D C   1 
ATOM   9521  O  O   . ASN D  1 17  ? 6.821   10.949  -13.999 1.00 14.03 ? 16  ASN D O   1 
ATOM   9522  C  CB  . ASN D  1 17  ? 3.702   10.114  -12.895 1.00 13.78 ? 16  ASN D CB  1 
ATOM   9523  C  CG  . ASN D  1 17  ? 3.543   9.452   -14.248 1.00 13.43 ? 16  ASN D CG  1 
ATOM   9524  O  OD1 . ASN D  1 17  ? 2.500   9.574   -14.905 1.00 13.85 ? 16  ASN D OD1 1 
ATOM   9525  N  ND2 . ASN D  1 17  ? 4.584   8.737   -14.692 1.00 13.19 ? 16  ASN D ND2 1 
ATOM   9526  N  N   . GLN D  1 18  ? 6.626   10.259  -11.852 1.00 15.01 ? 17  GLN D N   1 
ATOM   9527  C  CA  . GLN D  1 18  ? 7.965   9.708   -11.798 1.00 15.28 ? 17  GLN D CA  1 
ATOM   9528  C  C   . GLN D  1 18  ? 8.132   8.592   -12.841 1.00 15.28 ? 17  GLN D C   1 
ATOM   9529  O  O   . GLN D  1 18  ? 7.160   7.897   -13.172 1.00 14.20 ? 17  GLN D O   1 
ATOM   9530  C  CB  . GLN D  1 18  ? 8.244   9.121   -10.428 1.00 16.79 ? 17  GLN D CB  1 
ATOM   9531  C  CG  . GLN D  1 18  ? 8.278   10.139  -9.304  1.00 17.66 ? 17  GLN D CG  1 
ATOM   9532  C  CD  . GLN D  1 18  ? 8.503   9.500   -7.946  1.00 18.84 ? 17  GLN D CD  1 
ATOM   9533  O  OE1 . GLN D  1 18  ? 9.025   8.387   -7.834  1.00 18.91 ? 17  GLN D OE1 1 
ATOM   9534  N  NE2 . GLN D  1 18  ? 8.123   10.209  -6.913  1.00 19.17 ? 17  GLN D NE2 1 
ATOM   9535  N  N   . LEU D  1 19  ? 9.363   8.428   -13.324 1.00 15.25 ? 18  LEU D N   1 
ATOM   9536  C  CA  . LEU D  1 19  ? 9.772   7.273   -14.104 1.00 15.74 ? 18  LEU D CA  1 
ATOM   9537  C  C   . LEU D  1 19  ? 11.064  6.723   -13.526 1.00 16.92 ? 18  LEU D C   1 
ATOM   9538  O  O   . LEU D  1 19  ? 11.911  7.478   -13.047 1.00 16.79 ? 18  LEU D O   1 
ATOM   9539  C  CB  . LEU D  1 19  ? 10.000  7.619   -15.573 1.00 15.95 ? 18  LEU D CB  1 
ATOM   9540  C  CG  . LEU D  1 19  ? 8.809   8.124   -16.400 1.00 16.92 ? 18  LEU D CG  1 
ATOM   9541  C  CD1 . LEU D  1 19  ? 9.282   8.478   -17.807 1.00 17.66 ? 18  LEU D CD1 1 
ATOM   9542  C  CD2 . LEU D  1 19  ? 7.706   7.105   -16.459 1.00 17.47 ? 18  LEU D CD2 1 
ATOM   9543  N  N   . GLU D  1 20  ? 11.213  5.405   -13.581 1.00 17.10 ? 19  GLU D N   1 
ATOM   9544  C  CA  . GLU D  1 20  ? 12.396  4.725   -13.041 1.00 18.72 ? 19  GLU D CA  1 
ATOM   9545  C  C   . GLU D  1 20  ? 13.061  3.920   -14.137 1.00 18.39 ? 19  GLU D C   1 
ATOM   9546  O  O   . GLU D  1 20  ? 12.368  3.424   -15.035 1.00 17.69 ? 19  GLU D O   1 
ATOM   9547  C  CB  . GLU D  1 20  ? 11.977  3.772   -11.917 1.00 20.73 ? 19  GLU D CB  1 
ATOM   9548  C  CG  . GLU D  1 20  ? 11.567  4.497   -10.659 1.00 23.00 ? 19  GLU D CG  1 
ATOM   9549  C  CD  . GLU D  1 20  ? 11.017  3.613   -9.567  1.00 24.86 ? 19  GLU D CD  1 
ATOM   9550  O  OE1 . GLU D  1 20  ? 10.747  2.410   -9.804  1.00 26.99 ? 19  GLU D OE1 1 
ATOM   9551  O  OE2 . GLU D  1 20  ? 10.819  4.157   -8.458  1.00 27.77 ? 19  GLU D OE2 1 
ATOM   9552  N  N   . ALA D  1 21  ? 14.388  3.788   -14.077 1.00 18.08 ? 20  ALA D N   1 
ATOM   9553  C  CA  . ALA D  1 21  ? 15.119  3.021   -15.063 1.00 18.20 ? 20  ALA D CA  1 
ATOM   9554  C  C   . ALA D  1 21  ? 16.052  2.003   -14.418 1.00 19.22 ? 20  ALA D C   1 
ATOM   9555  O  O   . ALA D  1 21  ? 16.532  2.202   -13.302 1.00 19.65 ? 20  ALA D O   1 
ATOM   9556  C  CB  . ALA D  1 21  ? 15.900  3.930   -15.987 1.00 18.62 ? 20  ALA D CB  1 
ATOM   9557  N  N   . LYS D  1 22  ? 16.315  0.927   -15.144 1.00 19.81 ? 21  LYS D N   1 
ATOM   9558  C  CA  . LYS D  1 22  ? 17.334  -0.060  -14.764 1.00 21.54 ? 21  LYS D CA  1 
ATOM   9559  C  C   . LYS D  1 22  ? 18.194  -0.337  -15.982 1.00 21.24 ? 21  LYS D C   1 
ATOM   9560  O  O   . LYS D  1 22  ? 17.692  -0.421  -17.100 1.00 20.46 ? 21  LYS D O   1 
ATOM   9561  C  CB  . LYS D  1 22  ? 16.685  -1.340  -14.245 1.00 23.35 ? 21  LYS D CB  1 
ATOM   9562  C  CG  . LYS D  1 22  ? 17.674  -2.419  -13.836 1.00 25.98 ? 21  LYS D CG  1 
ATOM   9563  C  CD  . LYS D  1 22  ? 16.954  -3.633  -13.252 1.00 29.68 ? 21  LYS D CD  1 
ATOM   9564  C  CE  . LYS D  1 22  ? 17.961  -4.651  -12.739 1.00 35.31 ? 21  LYS D CE  1 
ATOM   9565  N  NZ  . LYS D  1 22  ? 17.287  -5.695  -11.901 1.00 38.78 ? 21  LYS D NZ  1 
ATOM   9566  N  N   . LEU D  1 23  ? 19.502  -0.447  -15.780 1.00 21.85 ? 22  LEU D N   1 
ATOM   9567  C  CA  . LEU D  1 23  ? 20.443  -0.457  -16.886 1.00 21.80 ? 22  LEU D CA  1 
ATOM   9568  C  C   . LEU D  1 23  ? 21.302  -1.716  -16.943 1.00 23.60 ? 22  LEU D C   1 
ATOM   9569  O  O   . LEU D  1 23  ? 21.732  -2.216  -15.921 1.00 23.40 ? 22  LEU D O   1 
ATOM   9570  C  CB  . LEU D  1 23  ? 21.387  0.747   -16.767 1.00 22.57 ? 22  LEU D CB  1 
ATOM   9571  C  CG  . LEU D  1 23  ? 20.776  2.121   -16.528 1.00 21.64 ? 22  LEU D CG  1 
ATOM   9572  C  CD1 . LEU D  1 23  ? 21.894  3.154   -16.380 1.00 22.66 ? 22  LEU D CD1 1 
ATOM   9573  C  CD2 . LEU D  1 23  ? 19.802  2.507   -17.634 1.00 21.14 ? 22  LEU D CD2 1 
ATOM   9574  N  N   . ASP D  1 24  ? 21.548  -2.189  -18.153 1.00 25.35 ? 23  ASP D N   1 
ATOM   9575  C  CA  . ASP D  1 24  ? 22.633  -3.138  -18.472 1.00 27.72 ? 23  ASP D CA  1 
ATOM   9576  C  C   . ASP D  1 24  ? 23.055  -2.882  -19.925 1.00 27.41 ? 23  ASP D C   1 
ATOM   9577  O  O   . ASP D  1 24  ? 22.755  -3.664  -20.829 1.00 27.45 ? 23  ASP D O   1 
ATOM   9578  C  CB  . ASP D  1 24  ? 22.166  -4.583  -18.276 1.00 29.27 ? 23  ASP D CB  1 
ATOM   9579  C  CG  . ASP D  1 24  ? 23.317  -5.594  -18.350 1.00 33.27 ? 23  ASP D CG  1 
ATOM   9580  O  OD1 . ASP D  1 24  ? 24.494  -5.190  -18.471 1.00 34.23 ? 23  ASP D OD1 1 
ATOM   9581  O  OD2 . ASP D  1 24  ? 23.035  -6.810  -18.291 1.00 35.92 ? 23  ASP D OD2 1 
ATOM   9582  N  N   . LYS D  1 25  ? 23.709  -1.751  -20.152 1.00 27.12 ? 24  LYS D N   1 
ATOM   9583  C  CA  . LYS D  1 25  ? 23.913  -1.218  -21.496 1.00 27.78 ? 24  LYS D CA  1 
ATOM   9584  C  C   . LYS D  1 25  ? 25.209  -1.752  -22.090 1.00 30.65 ? 24  LYS D C   1 
ATOM   9585  O  O   . LYS D  1 25  ? 26.185  -1.903  -21.372 1.00 29.92 ? 24  LYS D O   1 
ATOM   9586  C  CB  . LYS D  1 25  ? 24.001  0.312   -21.453 1.00 27.32 ? 24  LYS D CB  1 
ATOM   9587  C  CG  . LYS D  1 25  ? 22.748  1.004   -20.917 1.00 26.57 ? 24  LYS D CG  1 
ATOM   9588  C  CD  . LYS D  1 25  ? 23.057  2.416   -20.416 1.00 26.99 ? 24  LYS D CD  1 
ATOM   9589  C  CE  . LYS D  1 25  ? 23.389  3.395   -21.530 1.00 27.09 ? 24  LYS D CE  1 
ATOM   9590  N  NZ  . LYS D  1 25  ? 22.219  3.810   -22.359 1.00 27.10 ? 24  LYS D NZ  1 
ATOM   9591  N  N   . PRO D  1 26  ? 25.219  -2.049  -23.397 1.00 32.67 ? 25  PRO D N   1 
ATOM   9592  C  CA  . PRO D  1 26  ? 26.471  -2.518  -24.008 1.00 34.87 ? 25  PRO D CA  1 
ATOM   9593  C  C   . PRO D  1 26  ? 27.528  -1.419  -24.123 1.00 35.62 ? 25  PRO D C   1 
ATOM   9594  O  O   . PRO D  1 26  ? 28.722  -1.713  -24.043 1.00 35.32 ? 25  PRO D O   1 
ATOM   9595  C  CB  . PRO D  1 26  ? 26.035  -2.994  -25.402 1.00 35.53 ? 25  PRO D CB  1 
ATOM   9596  C  CG  . PRO D  1 26  ? 24.728  -2.364  -25.655 1.00 35.06 ? 25  PRO D CG  1 
ATOM   9597  C  CD  . PRO D  1 26  ? 24.079  -2.121  -24.322 1.00 33.29 ? 25  PRO D CD  1 
ATOM   9598  N  N   . THR D  1 27  ? 27.088  -0.178  -24.341 1.00 35.01 ? 26  THR D N   1 
ATOM   9599  C  CA  . THR D  1 27  ? 27.993  0.965   -24.467 1.00 36.97 ? 26  THR D CA  1 
ATOM   9600  C  C   . THR D  1 27  ? 27.375  2.197   -23.819 1.00 34.48 ? 26  THR D C   1 
ATOM   9601  O  O   . THR D  1 27  ? 26.145  2.288   -23.649 1.00 31.71 ? 26  THR D O   1 
ATOM   9602  C  CB  . THR D  1 27  ? 28.285  1.310   -25.951 1.00 39.46 ? 26  THR D CB  1 
ATOM   9603  O  OG1 . THR D  1 27  ? 27.067  1.686   -26.608 1.00 42.31 ? 26  THR D OG1 1 
ATOM   9604  C  CG2 . THR D  1 27  ? 28.887  0.142   -26.680 1.00 41.49 ? 26  THR D CG2 1 
ATOM   9605  N  N   . VAL D  1 28  ? 28.221  3.166   -23.487 1.00 33.49 ? 27  VAL D N   1 
ATOM   9606  C  CA  . VAL D  1 28  ? 27.745  4.465   -22.984 1.00 32.11 ? 27  VAL D CA  1 
ATOM   9607  C  C   . VAL D  1 28  ? 28.343  5.600   -23.802 1.00 32.16 ? 27  VAL D C   1 
ATOM   9608  O  O   . VAL D  1 28  ? 29.389  5.424   -24.430 1.00 32.24 ? 27  VAL D O   1 
ATOM   9609  C  CB  . VAL D  1 28  ? 28.074  4.675   -21.487 1.00 31.95 ? 27  VAL D CB  1 
ATOM   9610  C  CG1 . VAL D  1 28  ? 27.175  3.816   -20.608 1.00 31.19 ? 27  VAL D CG1 1 
ATOM   9611  C  CG2 . VAL D  1 28  ? 29.556  4.399   -21.187 1.00 34.05 ? 27  VAL D CG2 1 
ATOM   9612  N  N   . VAL D  1 29  ? 27.702  6.767   -23.777 1.00 30.48 ? 28  VAL D N   1 
ATOM   9613  C  CA  . VAL D  1 29  ? 28.174  7.909   -24.565 1.00 32.30 ? 28  VAL D CA  1 
ATOM   9614  C  C   . VAL D  1 29  ? 29.360  8.661   -23.935 1.00 33.48 ? 28  VAL D C   1 
ATOM   9615  O  O   . VAL D  1 29  ? 30.104  9.325   -24.652 1.00 35.07 ? 28  VAL D O   1 
ATOM   9616  C  CB  . VAL D  1 29  ? 27.039  8.898   -24.927 1.00 31.64 ? 28  VAL D CB  1 
ATOM   9617  C  CG1 . VAL D  1 29  ? 25.969  8.177   -25.723 1.00 31.52 ? 28  VAL D CG1 1 
ATOM   9618  C  CG2 . VAL D  1 29  ? 26.449  9.565   -23.694 1.00 31.53 ? 28  VAL D CG2 1 
ATOM   9619  N  N   . HIS D  1 30  ? 29.499  8.590   -22.615 1.00 33.80 ? 29  HIS D N   1 
ATOM   9620  C  CA  . HIS D  1 30  ? 30.637  9.158   -21.889 1.00 35.91 ? 29  HIS D CA  1 
ATOM   9621  C  C   . HIS D  1 30  ? 31.050  8.178   -20.812 1.00 35.15 ? 29  HIS D C   1 
ATOM   9622  O  O   . HIS D  1 30  ? 30.210  7.439   -20.263 1.00 33.33 ? 29  HIS D O   1 
ATOM   9623  C  CB  . HIS D  1 30  ? 30.296  10.488  -21.177 1.00 36.71 ? 29  HIS D CB  1 
ATOM   9624  C  CG  . HIS D  1 30  ? 29.798  11.569  -22.083 1.00 37.93 ? 29  HIS D CG  1 
ATOM   9625  N  ND1 . HIS D  1 30  ? 30.475  11.971  -23.213 1.00 38.52 ? 29  HIS D ND1 1 
ATOM   9626  C  CD2 . HIS D  1 30  ? 28.685  12.342  -22.015 1.00 38.28 ? 29  HIS D CD2 1 
ATOM   9627  C  CE1 . HIS D  1 30  ? 29.800  12.938  -23.810 1.00 39.47 ? 29  HIS D CE1 1 
ATOM   9628  N  NE2 . HIS D  1 30  ? 28.709  13.181  -23.103 1.00 39.35 ? 29  HIS D NE2 1 
ATOM   9629  N  N   . TYR D  1 31  ? 32.325  8.242   -20.449 1.00 35.94 ? 30  TYR D N   1 
ATOM   9630  C  CA  . TYR D  1 31  ? 32.871  7.415   -19.383 1.00 37.40 ? 30  TYR D CA  1 
ATOM   9631  C  C   . TYR D  1 31  ? 32.174  7.609   -18.042 1.00 36.86 ? 30  TYR D C   1 
ATOM   9632  O  O   . TYR D  1 31  ? 32.086  6.687   -17.230 1.00 39.11 ? 30  TYR D O   1 
ATOM   9633  C  CB  . TYR D  1 31  ? 34.375  7.770   -19.225 1.00 39.03 ? 30  TYR D CB  1 
ATOM   9634  C  CG  . TYR D  1 31  ? 34.630  9.116   -18.561 1.00 38.85 ? 30  TYR D CG  1 
ATOM   9635  C  CD1 . TYR D  1 31  ? 34.600  10.314  -19.288 1.00 39.60 ? 30  TYR D CD1 1 
ATOM   9636  C  CD2 . TYR D  1 31  ? 34.870  9.193   -17.201 1.00 40.57 ? 30  TYR D CD2 1 
ATOM   9637  C  CE1 . TYR D  1 31  ? 34.814  11.542  -18.665 1.00 40.18 ? 30  TYR D CE1 1 
ATOM   9638  C  CE2 . TYR D  1 31  ? 35.088  10.409  -16.565 1.00 41.05 ? 30  TYR D CE2 1 
ATOM   9639  C  CZ  . TYR D  1 31  ? 35.050  11.584  -17.299 1.00 41.62 ? 30  TYR D CZ  1 
ATOM   9640  O  OH  . TYR D  1 31  ? 35.282  12.790  -16.665 1.00 43.42 ? 30  TYR D OH  1 
ATOM   9641  N  N   . LEU D  1 32  ? 31.658  8.804   -17.806 1.00 36.18 ? 31  LEU D N   1 
ATOM   9642  C  CA  . LEU D  1 32  ? 30.994  9.078   -16.536 1.00 37.21 ? 31  LEU D CA  1 
ATOM   9643  C  C   . LEU D  1 32  ? 29.545  8.524   -16.460 1.00 35.97 ? 31  LEU D C   1 
ATOM   9644  O  O   . LEU D  1 32  ? 28.937  8.586   -15.405 1.00 34.31 ? 31  LEU D O   1 
ATOM   9645  C  CB  . LEU D  1 32  ? 31.059  10.581  -16.190 1.00 40.20 ? 31  LEU D CB  1 
ATOM   9646  C  CG  . LEU D  1 32  ? 30.629  11.627  -17.222 1.00 41.96 ? 31  LEU D CG  1 
ATOM   9647  C  CD1 . LEU D  1 32  ? 29.122  11.603  -17.407 1.00 42.26 ? 31  LEU D CD1 1 
ATOM   9648  C  CD2 . LEU D  1 32  ? 31.092  13.022  -16.815 1.00 42.95 ? 31  LEU D CD2 1 
ATOM   9649  N  N   . CYS D  1 33  ? 29.021  7.970   -17.554 1.00 33.89 ? 32  CYS D N   1 
ATOM   9650  C  CA  . CYS D  1 33  ? 27.663  7.365   -17.545 1.00 32.91 ? 32  CYS D CA  1 
ATOM   9651  C  C   . CYS D  1 33  ? 27.716  5.936   -16.988 1.00 32.39 ? 32  CYS D C   1 
ATOM   9652  O  O   . CYS D  1 33  ? 28.619  5.170   -17.354 1.00 32.18 ? 32  CYS D O   1 
ATOM   9653  C  CB  . CYS D  1 33  ? 27.094  7.302   -18.968 1.00 33.08 ? 32  CYS D CB  1 
ATOM   9654  S  SG  . CYS D  1 33  ? 27.025  8.823   -19.967 1.00 35.78 ? 32  CYS D SG  1 
ATOM   9655  N  N   . SER D  1 34  ? 26.788  5.556   -16.113 1.00 31.45 ? 33  SER D N   1 
ATOM   9656  C  CA  . SER D  1 34  ? 26.727  4.160   -15.615 1.00 32.85 ? 33  SER D CA  1 
ATOM   9657  C  C   . SER D  1 34  ? 26.264  3.216   -16.724 1.00 31.77 ? 33  SER D C   1 
ATOM   9658  O  O   . SER D  1 34  ? 25.300  3.516   -17.447 1.00 29.14 ? 33  SER D O   1 
ATOM   9659  C  CB  . SER D  1 34  ? 25.781  4.009   -14.428 1.00 34.67 ? 33  SER D CB  1 
ATOM   9660  O  OG  . SER D  1 34  ? 26.264  4.716   -13.302 1.00 38.54 ? 33  SER D OG  1 
ATOM   9661  N  N   . LYS D  1 35  ? 26.947  2.082   -16.844 1.00 30.99 ? 34  LYS D N   1 
ATOM   9662  C  CA  . LYS D  1 35  ? 26.557  1.026   -17.770 1.00 32.03 ? 34  LYS D CA  1 
ATOM   9663  C  C   . LYS D  1 35  ? 25.491  0.102   -17.193 1.00 31.20 ? 34  LYS D C   1 
ATOM   9664  O  O   . LYS D  1 35  ? 24.644  -0.399  -17.919 1.00 29.67 ? 34  LYS D O   1 
ATOM   9665  C  CB  . LYS D  1 35  ? 27.760  0.145   -18.116 1.00 33.96 ? 34  LYS D CB  1 
ATOM   9666  C  CG  . LYS D  1 35  ? 28.386  0.442   -19.451 1.00 36.34 ? 34  LYS D CG  1 
ATOM   9667  C  CD  . LYS D  1 35  ? 29.485  -0.563  -19.752 1.00 39.19 ? 34  LYS D CD  1 
ATOM   9668  C  CE  . LYS D  1 35  ? 29.689  -0.661  -21.245 1.00 42.11 ? 34  LYS D CE  1 
ATOM   9669  N  NZ  . LYS D  1 35  ? 30.872  -1.504  -21.578 1.00 45.05 ? 34  LYS D NZ  1 
ATOM   9670  N  N   . LYS D  1 36  ? 25.568  -0.140  -15.894 1.00 32.09 ? 35  LYS D N   1 
ATOM   9671  C  CA  . LYS D  1 36  ? 24.794  -1.193  -15.260 1.00 33.04 ? 35  LYS D CA  1 
ATOM   9672  C  C   . LYS D  1 36  ? 24.336  -0.742  -13.886 1.00 32.52 ? 35  LYS D C   1 
ATOM   9673  O  O   . LYS D  1 36  ? 25.099  -0.113  -13.158 1.00 32.38 ? 35  LYS D O   1 
ATOM   9674  C  CB  . LYS D  1 36  ? 25.668  -2.441  -15.129 1.00 37.82 ? 35  LYS D CB  1 
ATOM   9675  C  CG  . LYS D  1 36  ? 24.926  -3.696  -14.704 1.00 41.44 ? 35  LYS D CG  1 
ATOM   9676  C  CD  . LYS D  1 36  ? 25.875  -4.880  -14.584 1.00 48.28 ? 35  LYS D CD  1 
ATOM   9677  C  CE  . LYS D  1 36  ? 25.215  -6.084  -13.837 1.00 52.80 ? 35  LYS D CE  1 
ATOM   9678  N  NZ  . LYS D  1 36  ? 25.393  -7.393  -14.555 1.00 57.06 ? 35  LYS D NZ  1 
ATOM   9679  N  N   . THR D  1 37  ? 23.089  -1.042  -13.543 1.00 29.19 ? 36  THR D N   1 
ATOM   9680  C  CA  . THR D  1 37  ? 22.588  -0.834  -12.194 1.00 29.50 ? 36  THR D CA  1 
ATOM   9681  C  C   . THR D  1 37  ? 21.954  -2.144  -11.707 1.00 31.11 ? 36  THR D C   1 
ATOM   9682  O  O   . THR D  1 37  ? 21.339  -2.866  -12.489 1.00 32.79 ? 36  THR D O   1 
ATOM   9683  C  CB  . THR D  1 37  ? 21.561  0.320   -12.123 1.00 27.98 ? 36  THR D CB  1 
ATOM   9684  O  OG1 . THR D  1 37  ? 20.385  -0.012  -12.886 1.00 25.84 ? 36  THR D OG1 1 
ATOM   9685  C  CG2 . THR D  1 37  ? 22.169  1.633   -12.674 1.00 27.84 ? 36  THR D CG2 1 
ATOM   9686  N  N   . GLU D  1 38  ? 22.061  -2.424  -10.420 1.00 33.04 ? 37  GLU D N   1 
ATOM   9687  C  CA  . GLU D  1 38  ? 21.454  -3.629  -9.848  1.00 35.89 ? 37  GLU D CA  1 
ATOM   9688  C  C   . GLU D  1 38  ? 19.954  -3.479  -9.590  1.00 32.94 ? 37  GLU D C   1 
ATOM   9689  O  O   . GLU D  1 38  ? 19.239  -4.462  -9.513  1.00 33.25 ? 37  GLU D O   1 
ATOM   9690  C  CB  . GLU D  1 38  ? 22.182  -4.025  -8.564  1.00 41.97 ? 37  GLU D CB  1 
ATOM   9691  C  CG  . GLU D  1 38  ? 23.674  -4.278  -8.775  1.00 49.97 ? 37  GLU D CG  1 
ATOM   9692  C  CD  . GLU D  1 38  ? 23.970  -5.338  -9.835  1.00 57.25 ? 37  GLU D CD  1 
ATOM   9693  O  OE1 . GLU D  1 38  ? 23.228  -6.345  -9.920  1.00 64.89 ? 37  GLU D OE1 1 
ATOM   9694  O  OE2 . GLU D  1 38  ? 24.954  -5.176  -10.592 1.00 65.36 ? 37  GLU D OE2 1 
ATOM   9695  N  N   . SER D  1 39  ? 19.477  -2.247  -9.474  1.00 29.88 ? 38  SER D N   1 
ATOM   9696  C  CA  . SER D  1 39  ? 18.059  -1.996  -9.278  1.00 28.61 ? 38  SER D CA  1 
ATOM   9697  C  C   . SER D  1 39  ? 17.633  -0.767  -10.065 1.00 26.08 ? 38  SER D C   1 
ATOM   9698  O  O   . SER D  1 39  ? 18.443  -0.137  -10.750 1.00 25.34 ? 38  SER D O   1 
ATOM   9699  C  CB  . SER D  1 39  ? 17.778  -1.787  -7.793  1.00 31.32 ? 38  SER D CB  1 
ATOM   9700  O  OG  . SER D  1 39  ? 18.539  -0.686  -7.327  1.00 34.58 ? 38  SER D OG  1 
ATOM   9701  N  N   . TYR D  1 40  ? 16.348  -0.454  -9.981  1.00 23.49 ? 39  TYR D N   1 
ATOM   9702  C  CA  . TYR D  1 40  ? 15.814  0.731   -10.622 1.00 22.20 ? 39  TYR D CA  1 
ATOM   9703  C  C   . TYR D  1 40  ? 16.239  1.979   -9.860  1.00 23.06 ? 39  TYR D C   1 
ATOM   9704  O  O   . TYR D  1 40  ? 16.412  1.928   -8.648  1.00 24.22 ? 39  TYR D O   1 
ATOM   9705  C  CB  . TYR D  1 40  ? 14.301  0.644   -10.693 1.00 20.65 ? 39  TYR D CB  1 
ATOM   9706  C  CG  . TYR D  1 40  ? 13.815  -0.328  -11.765 1.00 19.82 ? 39  TYR D CG  1 
ATOM   9707  C  CD1 . TYR D  1 40  ? 13.672  -1.687  -11.489 1.00 20.59 ? 39  TYR D CD1 1 
ATOM   9708  C  CD2 . TYR D  1 40  ? 13.496  0.124   -13.055 1.00 19.09 ? 39  TYR D CD2 1 
ATOM   9709  C  CE1 . TYR D  1 40  ? 13.268  -2.580  -12.474 1.00 20.58 ? 39  TYR D CE1 1 
ATOM   9710  C  CE2 . TYR D  1 40  ? 13.057  -0.757  -14.031 1.00 18.84 ? 39  TYR D CE2 1 
ATOM   9711  C  CZ  . TYR D  1 40  ? 12.931  -2.106  -13.726 1.00 19.73 ? 39  TYR D CZ  1 
ATOM   9712  O  OH  . TYR D  1 40  ? 12.558  -2.991  -14.702 1.00 20.20 ? 39  TYR D OH  1 
ATOM   9713  N  N   . PHE D  1 41  ? 16.440  3.075   -10.584 1.00 22.08 ? 40  PHE D N   1 
ATOM   9714  C  CA  . PHE D  1 41  ? 16.702  4.376   -9.982  1.00 22.61 ? 40  PHE D CA  1 
ATOM   9715  C  C   . PHE D  1 41  ? 15.760  5.371   -10.661 1.00 21.75 ? 40  PHE D C   1 
ATOM   9716  O  O   . PHE D  1 41  ? 15.253  5.122   -11.755 1.00 20.90 ? 40  PHE D O   1 
ATOM   9717  C  CB  . PHE D  1 41  ? 18.151  4.819   -10.166 1.00 23.14 ? 40  PHE D CB  1 
ATOM   9718  C  CG  . PHE D  1 41  ? 18.555  5.066   -11.602 1.00 23.52 ? 40  PHE D CG  1 
ATOM   9719  C  CD1 . PHE D  1 41  ? 18.955  4.011   -12.419 1.00 23.49 ? 40  PHE D CD1 1 
ATOM   9720  C  CD2 . PHE D  1 41  ? 18.583  6.354   -12.130 1.00 24.99 ? 40  PHE D CD2 1 
ATOM   9721  C  CE1 . PHE D  1 41  ? 19.327  4.233   -13.732 1.00 24.21 ? 40  PHE D CE1 1 
ATOM   9722  C  CE2 . PHE D  1 41  ? 18.959  6.589   -13.454 1.00 25.29 ? 40  PHE D CE2 1 
ATOM   9723  C  CZ  . PHE D  1 41  ? 19.329  5.517   -14.261 1.00 25.42 ? 40  PHE D CZ  1 
ATOM   9724  N  N   . THR D  1 42  ? 15.546  6.515   -10.023 1.00 20.86 ? 41  THR D N   1 
ATOM   9725  C  CA  . THR D  1 42  ? 14.640  7.523   -10.587 1.00 20.21 ? 41  THR D CA  1 
ATOM   9726  C  C   . THR D  1 42  ? 15.297  8.276   -11.732 1.00 20.55 ? 41  THR D C   1 
ATOM   9727  O  O   . THR D  1 42  ? 16.339  8.927   -11.551 1.00 20.71 ? 41  THR D O   1 
ATOM   9728  C  CB  . THR D  1 42  ? 14.216  8.504   -9.481  1.00 21.19 ? 41  THR D CB  1 
ATOM   9729  O  OG1 . THR D  1 42  ? 13.569  7.755   -8.450  1.00 21.11 ? 41  THR D OG1 1 
ATOM   9730  C  CG2 . THR D  1 42  ? 13.266  9.573   -10.045 1.00 20.76 ? 41  THR D CG2 1 
ATOM   9731  N  N   . ILE D  1 43  ? 14.713  8.171   -12.916 1.00 19.21 ? 42  ILE D N   1 
ATOM   9732  C  CA  . ILE D  1 43  ? 15.200  8.882   -14.096 1.00 19.32 ? 42  ILE D CA  1 
ATOM   9733  C  C   . ILE D  1 43  ? 14.443  10.186  -14.374 1.00 18.88 ? 42  ILE D C   1 
ATOM   9734  O  O   . ILE D  1 43  ? 14.965  11.092  -15.023 1.00 19.67 ? 42  ILE D O   1 
ATOM   9735  C  CB  . ILE D  1 43  ? 15.277  7.935   -15.315 1.00 20.57 ? 42  ILE D CB  1 
ATOM   9736  C  CG1 . ILE D  1 43  ? 16.197  8.522   -16.379 1.00 22.09 ? 42  ILE D CG1 1 
ATOM   9737  C  CG2 . ILE D  1 43  ? 13.896  7.582   -15.875 1.00 19.89 ? 42  ILE D CG2 1 
ATOM   9738  C  CD1 . ILE D  1 43  ? 16.590  7.528   -17.469 1.00 23.70 ? 42  ILE D CD1 1 
ATOM   9739  N  N   . TRP D  1 44  ? 13.227  10.292  -13.852 1.00 17.49 ? 43  TRP D N   1 
ATOM   9740  C  CA  . TRP D  1 44  ? 12.471  11.544  -13.826 1.00 16.84 ? 43  TRP D CA  1 
ATOM   9741  C  C   . TRP D  1 44  ? 11.675  11.577  -12.516 1.00 17.19 ? 43  TRP D C   1 
ATOM   9742  O  O   . TRP D  1 44  ? 10.945  10.623  -12.236 1.00 15.20 ? 43  TRP D O   1 
ATOM   9743  C  CB  . TRP D  1 44  ? 11.485  11.616  -14.994 1.00 16.71 ? 43  TRP D CB  1 
ATOM   9744  C  CG  . TRP D  1 44  ? 10.700  12.876  -15.035 1.00 15.82 ? 43  TRP D CG  1 
ATOM   9745  C  CD1 . TRP D  1 44  ? 9.403   13.067  -14.617 1.00 15.66 ? 43  TRP D CD1 1 
ATOM   9746  C  CD2 . TRP D  1 44  ? 11.176  14.138  -15.474 1.00 16.05 ? 43  TRP D CD2 1 
ATOM   9747  N  NE1 . TRP D  1 44  ? 9.041   14.378  -14.803 1.00 15.95 ? 43  TRP D NE1 1 
ATOM   9748  C  CE2 . TRP D  1 44  ? 10.115  15.053  -15.341 1.00 16.32 ? 43  TRP D CE2 1 
ATOM   9749  C  CE3 . TRP D  1 44  ? 12.406  14.585  -16.004 1.00 17.33 ? 43  TRP D CE3 1 
ATOM   9750  C  CZ2 . TRP D  1 44  ? 10.241  16.392  -15.702 1.00 16.91 ? 43  TRP D CZ2 1 
ATOM   9751  C  CZ3 . TRP D  1 44  ? 12.531  15.913  -16.363 1.00 18.19 ? 43  TRP D CZ3 1 
ATOM   9752  C  CH2 . TRP D  1 44  ? 11.454  16.805  -16.197 1.00 18.14 ? 43  TRP D CH2 1 
ATOM   9753  N  N   . LEU D  1 45  ? 11.774  12.625  -11.696 1.00 18.27 ? 44  LEU D N   1 
ATOM   9754  C  CA  . LEU D  1 45  ? 12.606  13.815  -11.894 1.00 20.31 ? 44  LEU D CA  1 
ATOM   9755  C  C   . LEU D  1 45  ? 13.786  13.763  -10.938 1.00 22.16 ? 44  LEU D C   1 
ATOM   9756  O  O   . LEU D  1 45  ? 13.605  13.625  -9.721  1.00 22.89 ? 44  LEU D O   1 
ATOM   9757  C  CB  . LEU D  1 45  ? 11.761  15.061  -11.610 1.00 20.34 ? 44  LEU D CB  1 
ATOM   9758  C  CG  . LEU D  1 45  ? 12.492  16.413  -11.531 1.00 21.56 ? 44  LEU D CG  1 
ATOM   9759  C  CD1 . LEU D  1 45  ? 13.157  16.712  -12.865 1.00 21.98 ? 44  LEU D CD1 1 
ATOM   9760  C  CD2 . LEU D  1 45  ? 11.486  17.510  -11.190 1.00 22.33 ? 44  LEU D CD2 1 
ATOM   9761  N  N   . ASN D  1 46  ? 14.992  13.843  -11.481 1.00 24.74 ? 45  ASN D N   1 
ATOM   9762  C  CA  . ASN D  1 46  ? 16.196  13.965  -10.663 1.00 27.65 ? 45  ASN D CA  1 
ATOM   9763  C  C   . ASN D  1 46  ? 17.063  15.014  -11.306 1.00 29.57 ? 45  ASN D C   1 
ATOM   9764  O  O   . ASN D  1 46  ? 17.595  14.832  -12.407 1.00 27.55 ? 45  ASN D O   1 
ATOM   9765  C  CB  . ASN D  1 46  ? 16.945  12.655  -10.515 1.00 30.38 ? 45  ASN D CB  1 
ATOM   9766  C  CG  . ASN D  1 46  ? 18.278  12.825  -9.748  1.00 33.22 ? 45  ASN D CG  1 
ATOM   9767  O  OD1 . ASN D  1 46  ? 18.742  13.932  -9.494  1.00 38.67 ? 45  ASN D OD1 1 
ATOM   9768  N  ND2 . ASN D  1 46  ? 18.863  11.734  -9.379  1.00 36.19 ? 45  ASN D ND2 1 
ATOM   9769  N  N   . LEU D  1 47  ? 17.185  16.134  -10.604 1.00 33.60 ? 46  LEU D N   1 
ATOM   9770  C  CA  . LEU D  1 47  ? 17.840  17.330  -11.147 1.00 36.85 ? 46  LEU D CA  1 
ATOM   9771  C  C   . LEU D  1 47  ? 19.329  17.114  -11.442 1.00 36.43 ? 46  LEU D C   1 
ATOM   9772  O  O   . LEU D  1 47  ? 19.878  17.714  -12.350 1.00 36.65 ? 46  LEU D O   1 
ATOM   9773  C  CB  . LEU D  1 47  ? 17.690  18.493  -10.157 1.00 39.18 ? 46  LEU D CB  1 
ATOM   9774  C  CG  . LEU D  1 47  ? 16.261  18.959  -9.890  1.00 40.43 ? 46  LEU D CG  1 
ATOM   9775  C  CD1 . LEU D  1 47  ? 16.283  19.998  -8.773  1.00 41.57 ? 46  LEU D CD1 1 
ATOM   9776  C  CD2 . LEU D  1 47  ? 15.649  19.517  -11.164 1.00 41.42 ? 46  LEU D CD2 1 
ATOM   9777  N  N   . GLU D  1 48  ? 19.958  16.221  -10.703 1.00 38.88 ? 47  GLU D N   1 
ATOM   9778  C  CA  . GLU D  1 48  ? 21.388  15.979  -10.898 1.00 42.24 ? 47  GLU D CA  1 
ATOM   9779  C  C   . GLU D  1 48  ? 21.703  15.282  -12.227 1.00 39.98 ? 47  GLU D C   1 
ATOM   9780  O  O   . GLU D  1 48  ? 22.833  15.345  -12.704 1.00 38.92 ? 47  GLU D O   1 
ATOM   9781  C  CB  . GLU D  1 48  ? 21.932  15.191  -9.731  1.00 46.46 ? 47  GLU D CB  1 
ATOM   9782  C  CG  . GLU D  1 48  ? 21.897  16.016  -8.458  1.00 52.59 ? 47  GLU D CG  1 
ATOM   9783  C  CD  . GLU D  1 48  ? 22.449  15.280  -7.267  1.00 59.01 ? 47  GLU D CD  1 
ATOM   9784  O  OE1 . GLU D  1 48  ? 22.374  14.035  -7.243  1.00 67.34 ? 47  GLU D OE1 1 
ATOM   9785  O  OE2 . GLU D  1 48  ? 22.952  15.957  -6.348  1.00 66.21 ? 47  GLU D OE2 1 
ATOM   9786  N  N   . LEU D  1 49  ? 20.693  14.661  -12.852 1.00 35.46 ? 48  LEU D N   1 
ATOM   9787  C  CA  . LEU D  1 49  ? 20.900  13.989  -14.137 1.00 33.48 ? 48  LEU D CA  1 
ATOM   9788  C  C   . LEU D  1 49  ? 20.833  14.960  -15.312 1.00 31.78 ? 48  LEU D C   1 
ATOM   9789  O  O   . LEU D  1 49  ? 21.137  14.579  -16.452 1.00 29.40 ? 48  LEU D O   1 
ATOM   9790  C  CB  . LEU D  1 49  ? 19.865  12.874  -14.324 1.00 33.39 ? 48  LEU D CB  1 
ATOM   9791  C  CG  . LEU D  1 49  ? 19.742  11.844  -13.202 1.00 33.33 ? 48  LEU D CG  1 
ATOM   9792  C  CD1 . LEU D  1 49  ? 18.664  10.823  -13.553 1.00 33.80 ? 48  LEU D CD1 1 
ATOM   9793  C  CD2 . LEU D  1 49  ? 21.072  11.148  -12.919 1.00 34.18 ? 48  LEU D CD2 1 
ATOM   9794  N  N   . LEU D  1 50  ? 20.404  16.202  -15.051 1.00 31.83 ? 49  LEU D N   1 
ATOM   9795  C  CA  . LEU D  1 50  ? 20.162  17.189  -16.109 1.00 32.83 ? 49  LEU D CA  1 
ATOM   9796  C  C   . LEU D  1 50  ? 21.281  18.249  -16.242 1.00 35.27 ? 49  LEU D C   1 
ATOM   9797  O  O   . LEU D  1 50  ? 21.207  19.142  -17.092 1.00 37.18 ? 49  LEU D O   1 
ATOM   9798  C  CB  . LEU D  1 50  ? 18.812  17.879  -15.861 1.00 32.86 ? 49  LEU D CB  1 
ATOM   9799  C  CG  . LEU D  1 50  ? 17.634  16.920  -15.606 1.00 32.26 ? 49  LEU D CG  1 
ATOM   9800  C  CD1 . LEU D  1 50  ? 16.340  17.663  -15.282 1.00 31.45 ? 49  LEU D CD1 1 
ATOM   9801  C  CD2 . LEU D  1 50  ? 17.439  16.034  -16.830 1.00 31.35 ? 49  LEU D CD2 1 
ATOM   9802  N  N   . LEU D  1 51  ? 22.334  18.108  -15.452 1.00 36.62 ? 50  LEU D N   1 
ATOM   9803  C  CA  . LEU D  1 51  ? 23.483  19.034  -15.524 1.00 38.63 ? 50  LEU D CA  1 
ATOM   9804  C  C   . LEU D  1 51  ? 24.248  18.874  -16.848 1.00 38.47 ? 50  LEU D C   1 
ATOM   9805  O  O   . LEU D  1 51  ? 24.177  17.823  -17.484 1.00 36.32 ? 50  LEU D O   1 
ATOM   9806  C  CB  . LEU D  1 51  ? 24.411  18.780  -14.342 1.00 40.46 ? 50  LEU D CB  1 
ATOM   9807  C  CG  . LEU D  1 51  ? 23.811  19.021  -12.946 1.00 42.36 ? 50  LEU D CG  1 
ATOM   9808  C  CD1 . LEU D  1 51  ? 24.639  18.361  -11.851 1.00 42.97 ? 50  LEU D CD1 1 
ATOM   9809  C  CD2 . LEU D  1 51  ? 23.650  20.511  -12.670 1.00 43.93 ? 50  LEU D CD2 1 
ATOM   9810  N  N   . PRO D  1 52  ? 25.008  19.906  -17.270 1.00 38.65 ? 51  PRO D N   1 
ATOM   9811  C  CA  . PRO D  1 52  ? 25.814  19.762  -18.490 1.00 38.69 ? 51  PRO D CA  1 
ATOM   9812  C  C   . PRO D  1 52  ? 26.667  18.474  -18.509 1.00 37.87 ? 51  PRO D C   1 
ATOM   9813  O  O   . PRO D  1 52  ? 27.147  18.052  -17.459 1.00 36.87 ? 51  PRO D O   1 
ATOM   9814  C  CB  . PRO D  1 52  ? 26.718  21.004  -18.466 1.00 40.22 ? 51  PRO D CB  1 
ATOM   9815  C  CG  . PRO D  1 52  ? 25.961  22.004  -17.657 1.00 40.16 ? 51  PRO D CG  1 
ATOM   9816  C  CD  . PRO D  1 52  ? 25.176  21.228  -16.643 1.00 39.51 ? 51  PRO D CD  1 
ATOM   9817  N  N   . VAL D  1 53  ? 26.821  17.869  -19.697 1.00 36.92 ? 52  VAL D N   1 
ATOM   9818  C  CA  . VAL D  1 53  ? 27.558  16.601  -19.918 1.00 37.81 ? 52  VAL D CA  1 
ATOM   9819  C  C   . VAL D  1 53  ? 26.813  15.365  -19.392 1.00 35.96 ? 52  VAL D C   1 
ATOM   9820  O  O   . VAL D  1 53  ? 26.540  14.439  -20.160 1.00 34.86 ? 52  VAL D O   1 
ATOM   9821  C  CB  . VAL D  1 53  ? 28.992  16.623  -19.346 1.00 40.12 ? 52  VAL D CB  1 
ATOM   9822  C  CG1 . VAL D  1 53  ? 29.765  15.362  -19.747 1.00 41.06 ? 52  VAL D CG1 1 
ATOM   9823  C  CG2 . VAL D  1 53  ? 29.731  17.866  -19.841 1.00 41.67 ? 52  VAL D CG2 1 
ATOM   9824  N  N   . ILE D  1 54  ? 26.498  15.352  -18.095 1.00 35.19 ? 53  ILE D N   1 
ATOM   9825  C  CA  . ILE D  1 54  ? 25.690  14.286  -17.488 1.00 35.50 ? 53  ILE D CA  1 
ATOM   9826  C  C   . ILE D  1 54  ? 24.351  14.150  -18.242 1.00 33.00 ? 53  ILE D C   1 
ATOM   9827  O  O   . ILE D  1 54  ? 23.813  13.043  -18.392 1.00 31.82 ? 53  ILE D O   1 
ATOM   9828  C  CB  . ILE D  1 54  ? 25.428  14.572  -15.967 1.00 36.85 ? 53  ILE D CB  1 
ATOM   9829  C  CG1 . ILE D  1 54  ? 26.724  14.817  -15.166 1.00 39.81 ? 53  ILE D CG1 1 
ATOM   9830  C  CG2 . ILE D  1 54  ? 24.595  13.485  -15.308 1.00 37.45 ? 53  ILE D CG2 1 
ATOM   9831  C  CD1 . ILE D  1 54  ? 27.875  13.931  -15.531 1.00 42.02 ? 53  ILE D CD1 1 
ATOM   9832  N  N   . ILE D  1 55  ? 23.817  15.269  -18.736 1.00 31.09 ? 54  ILE D N   1 
ATOM   9833  C  CA  . ILE D  1 55  ? 22.550  15.235  -19.466 1.00 30.44 ? 54  ILE D CA  1 
ATOM   9834  C  C   . ILE D  1 55  ? 22.619  14.332  -20.701 1.00 28.63 ? 54  ILE D C   1 
ATOM   9835  O  O   . ILE D  1 55  ? 21.599  13.810  -21.127 1.00 25.73 ? 54  ILE D O   1 
ATOM   9836  C  CB  . ILE D  1 55  ? 22.026  16.648  -19.846 1.00 32.45 ? 54  ILE D CB  1 
ATOM   9837  C  CG1 . ILE D  1 55  ? 20.566  16.554  -20.319 1.00 34.38 ? 54  ILE D CG1 1 
ATOM   9838  C  CG2 . ILE D  1 55  ? 22.897  17.286  -20.917 1.00 33.68 ? 54  ILE D CG2 1 
ATOM   9839  C  CD1 . ILE D  1 55  ? 19.758  17.815  -20.103 1.00 36.52 ? 54  ILE D CD1 1 
ATOM   9840  N  N   . ASP D  1 56  ? 23.808  14.142  -21.286 1.00 28.19 ? 55  ASP D N   1 
ATOM   9841  C  CA  . ASP D  1 56  ? 23.913  13.238  -22.433 1.00 28.18 ? 55  ASP D CA  1 
ATOM   9842  C  C   . ASP D  1 56  ? 23.608  11.782  -22.011 1.00 26.05 ? 55  ASP D C   1 
ATOM   9843  O  O   . ASP D  1 56  ? 23.035  11.016  -22.807 1.00 24.49 ? 55  ASP D O   1 
ATOM   9844  C  CB  . ASP D  1 56  ? 25.304  13.291  -23.094 1.00 30.76 ? 55  ASP D CB  1 
ATOM   9845  C  CG  . ASP D  1 56  ? 25.631  14.661  -23.700 1.00 33.49 ? 55  ASP D CG  1 
ATOM   9846  O  OD1 . ASP D  1 56  ? 24.733  15.337  -24.238 1.00 34.90 ? 55  ASP D OD1 1 
ATOM   9847  O  OD2 . ASP D  1 56  ? 26.817  15.038  -23.639 1.00 37.03 ? 55  ASP D OD2 1 
ATOM   9848  N  N   . CYS D  1 57  ? 24.039  11.406  -20.805 1.00 25.51 ? 56  CYS D N   1 
ATOM   9849  C  CA  . CYS D  1 57  ? 23.730  10.086  -20.242 1.00 26.04 ? 56  CYS D CA  1 
ATOM   9850  C  C   . CYS D  1 57  ? 22.203  9.934   -20.082 1.00 24.65 ? 56  CYS D C   1 
ATOM   9851  O  O   . CYS D  1 57  ? 21.618  8.909   -20.423 1.00 23.39 ? 56  CYS D O   1 
ATOM   9852  C  CB  . CYS D  1 57  ? 24.372  9.896   -18.872 1.00 28.35 ? 56  CYS D CB  1 
ATOM   9853  S  SG  . CYS D  1 57  ? 26.147  10.252  -18.784 1.00 32.42 ? 56  CYS D SG  1 
ATOM   9854  N  N   . TRP D  1 58  ? 21.576  10.973  -19.548 1.00 23.43 ? 57  TRP D N   1 
ATOM   9855  C  CA  . TRP D  1 58  ? 20.135  10.975  -19.334 1.00 22.77 ? 57  TRP D CA  1 
ATOM   9856  C  C   . TRP D  1 58  ? 19.381  10.843  -20.659 1.00 22.81 ? 57  TRP D C   1 
ATOM   9857  O  O   . TRP D  1 58  ? 18.485  10.006  -20.776 1.00 22.97 ? 57  TRP D O   1 
ATOM   9858  C  CB  . TRP D  1 58  ? 19.734  12.248  -18.596 1.00 22.72 ? 57  TRP D CB  1 
ATOM   9859  C  CG  . TRP D  1 58  ? 18.265  12.378  -18.310 1.00 22.68 ? 57  TRP D CG  1 
ATOM   9860  C  CD1 . TRP D  1 58  ? 17.570  11.776  -17.300 1.00 22.55 ? 57  TRP D CD1 1 
ATOM   9861  C  CD2 . TRP D  1 58  ? 17.324  13.178  -19.027 1.00 22.65 ? 57  TRP D CD2 1 
ATOM   9862  N  NE1 . TRP D  1 58  ? 16.253  12.156  -17.345 1.00 21.48 ? 57  TRP D NE1 1 
ATOM   9863  C  CE2 . TRP D  1 58  ? 16.072  13.017  -18.393 1.00 21.95 ? 57  TRP D CE2 1 
ATOM   9864  C  CE3 . TRP D  1 58  ? 17.409  14.006  -20.158 1.00 23.29 ? 57  TRP D CE3 1 
ATOM   9865  C  CZ2 . TRP D  1 58  ? 14.909  13.661  -18.853 1.00 23.31 ? 57  TRP D CZ2 1 
ATOM   9866  C  CZ3 . TRP D  1 58  ? 16.260  14.638  -20.623 1.00 23.89 ? 57  TRP D CZ3 1 
ATOM   9867  C  CH2 . TRP D  1 58  ? 15.022  14.471  -19.966 1.00 23.78 ? 57  TRP D CH2 1 
ATOM   9868  N  N   . ILE D  1 59  ? 19.744  11.663  -21.643 1.00 22.52 ? 58  ILE D N   1 
ATOM   9869  C  CA  . ILE D  1 59  ? 19.156  11.586  -22.982 1.00 22.83 ? 58  ILE D CA  1 
ATOM   9870  C  C   . ILE D  1 59  ? 19.308  10.173  -23.557 1.00 23.36 ? 58  ILE D C   1 
ATOM   9871  O  O   . ILE D  1 59  ? 18.345  9.612   -24.113 1.00 22.86 ? 58  ILE D O   1 
ATOM   9872  C  CB  . ILE D  1 59  ? 19.773  12.633  -23.960 1.00 24.41 ? 58  ILE D CB  1 
ATOM   9873  C  CG1 . ILE D  1 59  ? 19.367  14.044  -23.486 1.00 25.35 ? 58  ILE D CG1 1 
ATOM   9874  C  CG2 . ILE D  1 59  ? 19.339  12.358  -25.402 1.00 24.50 ? 58  ILE D CG2 1 
ATOM   9875  C  CD1 . ILE D  1 59  ? 20.003  15.191  -24.246 1.00 27.14 ? 58  ILE D CD1 1 
ATOM   9876  N  N   . ASP D  1 60  ? 20.490  9.587   -23.399 1.00 22.48 ? 59  ASP D N   1 
ATOM   9877  C  CA  . ASP D  1 60  ? 20.738  8.253   -23.945 1.00 22.96 ? 59  ASP D CA  1 
ATOM   9878  C  C   . ASP D  1 60  ? 19.847  7.185   -23.309 1.00 22.25 ? 59  ASP D C   1 
ATOM   9879  O  O   . ASP D  1 60  ? 19.562  6.181   -23.968 1.00 22.82 ? 59  ASP D O   1 
ATOM   9880  C  CB  . ASP D  1 60  ? 22.217  7.838   -23.821 1.00 24.29 ? 59  ASP D CB  1 
ATOM   9881  C  CG  . ASP D  1 60  ? 22.584  6.685   -24.757 1.00 25.66 ? 59  ASP D CG  1 
ATOM   9882  O  OD1 . ASP D  1 60  ? 22.241  6.766   -25.948 1.00 26.00 ? 59  ASP D OD1 1 
ATOM   9883  O  OD2 . ASP D  1 60  ? 23.189  5.683   -24.303 1.00 27.77 ? 59  ASP D OD2 1 
ATOM   9884  N  N   . ASN D  1 61  ? 19.399  7.409   -22.067 1.00 20.57 ? 60  ASN D N   1 
ATOM   9885  C  CA  . ASN D  1 61  ? 18.555  6.459   -21.357 1.00 20.25 ? 60  ASN D CA  1 
ATOM   9886  C  C   . ASN D  1 61  ? 17.049  6.724   -21.510 1.00 19.93 ? 60  ASN D C   1 
ATOM   9887  O  O   . ASN D  1 61  ? 16.268  5.777   -21.543 1.00 18.62 ? 60  ASN D O   1 
ATOM   9888  C  CB  . ASN D  1 61  ? 18.897  6.434   -19.856 1.00 20.21 ? 60  ASN D CB  1 
ATOM   9889  C  CG  . ASN D  1 61  ? 20.249  5.785   -19.572 1.00 21.02 ? 60  ASN D CG  1 
ATOM   9890  O  OD1 . ASN D  1 61  ? 20.658  4.858   -20.271 1.00 21.11 ? 60  ASN D OD1 1 
ATOM   9891  N  ND2 . ASN D  1 61  ? 20.916  6.229   -18.514 1.00 20.89 ? 60  ASN D ND2 1 
ATOM   9892  N  N   . ILE D  1 62  ? 16.664  7.993   -21.582 1.00 19.74 ? 61  ILE D N   1 
ATOM   9893  C  CA  . ILE D  1 62  ? 15.236  8.356   -21.572 1.00 20.59 ? 61  ILE D CA  1 
ATOM   9894  C  C   . ILE D  1 62  ? 14.655  8.585   -22.972 1.00 20.35 ? 61  ILE D C   1 
ATOM   9895  O  O   . ILE D  1 62  ? 13.406  8.623   -23.129 1.00 20.55 ? 61  ILE D O   1 
ATOM   9896  C  CB  . ILE D  1 62  ? 14.963  9.583   -20.675 1.00 21.28 ? 61  ILE D CB  1 
ATOM   9897  C  CG1 . ILE D  1 62  ? 13.508  9.561   -20.171 1.00 21.93 ? 61  ILE D CG1 1 
ATOM   9898  C  CG2 . ILE D  1 62  ? 15.313  10.862  -21.427 1.00 21.89 ? 61  ILE D CG2 1 
ATOM   9899  C  CD1 . ILE D  1 62  ? 13.224  10.551  -19.064 1.00 23.15 ? 61  ILE D CD1 1 
ATOM   9900  N  N   . ARG D  1 63  ? 15.518  8.687   -23.985 1.00 20.22 ? 62  ARG D N   1 
ATOM   9901  C  CA  . ARG D  1 63  ? 15.041  8.712   -25.376 1.00 21.42 ? 62  ARG D CA  1 
ATOM   9902  C  C   . ARG D  1 63  ? 14.317  7.415   -25.726 1.00 20.97 ? 62  ARG D C   1 
ATOM   9903  O  O   . ARG D  1 63  ? 14.598  6.358   -25.150 1.00 20.29 ? 62  ARG D O   1 
ATOM   9904  C  CB  . ARG D  1 63  ? 16.194  8.937   -26.364 1.00 23.46 ? 62  ARG D CB  1 
ATOM   9905  C  CG  . ARG D  1 63  ? 17.103  7.728   -26.525 1.00 25.48 ? 62  ARG D CG  1 
ATOM   9906  C  CD  . ARG D  1 63  ? 18.396  8.078   -27.252 1.00 28.83 ? 62  ARG D CD  1 
ATOM   9907  N  NE  . ARG D  1 63  ? 19.328  6.950   -27.235 1.00 30.69 ? 62  ARG D NE  1 
ATOM   9908  C  CZ  . ARG D  1 63  ? 19.384  5.976   -28.142 1.00 33.01 ? 62  ARG D CZ  1 
ATOM   9909  N  NH1 . ARG D  1 63  ? 18.595  5.973   -29.214 1.00 33.32 ? 62  ARG D NH1 1 
ATOM   9910  N  NH2 . ARG D  1 63  ? 20.278  5.007   -27.989 1.00 35.63 ? 62  ARG D NH2 1 
ATOM   9911  N  N   . LEU D  1 64  ? 13.344  7.515   -26.641 1.00 20.90 ? 63  LEU D N   1 
ATOM   9912  C  CA  . LEU D  1 64  ? 12.718  6.359   -27.272 1.00 19.95 ? 63  LEU D CA  1 
ATOM   9913  C  C   . LEU D  1 64  ? 13.327  6.136   -28.662 1.00 20.32 ? 63  LEU D C   1 
ATOM   9914  O  O   . LEU D  1 64  ? 13.710  7.087   -29.346 1.00 20.49 ? 63  LEU D O   1 
ATOM   9915  C  CB  . LEU D  1 64  ? 11.201  6.556   -27.385 1.00 19.48 ? 63  LEU D CB  1 
ATOM   9916  C  CG  . LEU D  1 64  ? 10.340  6.601   -26.125 1.00 20.24 ? 63  LEU D CG  1 
ATOM   9917  C  CD1 . LEU D  1 64  ? 8.877   6.861   -26.513 1.00 19.44 ? 63  LEU D CD1 1 
ATOM   9918  C  CD2 . LEU D  1 64  ? 10.453  5.308   -25.344 1.00 21.30 ? 63  LEU D CD2 1 
ATOM   9919  N  N   . VAL D  1 65  ? 13.487  4.886   -29.039 1.00 20.73 ? 64  VAL D N   1 
ATOM   9920  C  CA  . VAL D  1 65  ? 13.951  4.508   -30.368 1.00 21.62 ? 64  VAL D CA  1 
ATOM   9921  C  C   . VAL D  1 65  ? 12.722  4.174   -31.216 1.00 21.72 ? 64  VAL D C   1 
ATOM   9922  O  O   . VAL D  1 65  ? 11.908  3.349   -30.804 1.00 22.69 ? 64  VAL D O   1 
ATOM   9923  C  CB  . VAL D  1 65  ? 14.845  3.261   -30.280 1.00 23.24 ? 64  VAL D CB  1 
ATOM   9924  C  CG1 . VAL D  1 65  ? 15.264  2.778   -31.662 1.00 25.10 ? 64  VAL D CG1 1 
ATOM   9925  C  CG2 . VAL D  1 65  ? 16.079  3.542   -29.425 1.00 24.21 ? 64  VAL D CG2 1 
ATOM   9926  N  N   . TYR D  1 66  ? 12.567  4.803   -32.374 1.00 21.25 ? 65  TYR D N   1 
ATOM   9927  C  CA  . TYR D  1 66  ? 11.442  4.491   -33.257 1.00 21.11 ? 65  TYR D CA  1 
ATOM   9928  C  C   . TYR D  1 66  ? 11.850  3.410   -34.273 1.00 22.41 ? 65  TYR D C   1 
ATOM   9929  O  O   . TYR D  1 66  ? 12.813  3.558   -34.997 1.00 22.15 ? 65  TYR D O   1 
ATOM   9930  C  CB  . TYR D  1 66  ? 10.922  5.742   -33.989 1.00 21.14 ? 65  TYR D CB  1 
ATOM   9931  C  CG  . TYR D  1 66  ? 9.594   5.468   -34.686 1.00 20.85 ? 65  TYR D CG  1 
ATOM   9932  C  CD1 . TYR D  1 66  ? 8.390   5.511   -33.975 1.00 20.99 ? 65  TYR D CD1 1 
ATOM   9933  C  CD2 . TYR D  1 66  ? 9.551   5.070   -36.022 1.00 21.47 ? 65  TYR D CD2 1 
ATOM   9934  C  CE1 . TYR D  1 66  ? 7.182   5.199   -34.582 1.00 21.39 ? 65  TYR D CE1 1 
ATOM   9935  C  CE2 . TYR D  1 66  ? 8.340   4.792   -36.637 1.00 22.23 ? 65  TYR D CE2 1 
ATOM   9936  C  CZ  . TYR D  1 66  ? 7.160   4.859   -35.922 1.00 21.57 ? 65  TYR D CZ  1 
ATOM   9937  O  OH  . TYR D  1 66  ? 5.964   4.560   -36.546 1.00 22.89 ? 65  TYR D OH  1 
ATOM   9938  N  N   . ASN D  1 67  ? 11.116  2.317   -34.283 1.00 22.27 ? 66  ASN D N   1 
ATOM   9939  C  CA  . ASN D  1 67  ? 11.397  1.201   -35.178 1.00 24.76 ? 66  ASN D CA  1 
ATOM   9940  C  C   . ASN D  1 67  ? 10.418  1.254   -36.340 1.00 25.14 ? 66  ASN D C   1 
ATOM   9941  O  O   . ASN D  1 67  ? 9.220   1.051   -36.162 1.00 25.16 ? 66  ASN D O   1 
ATOM   9942  C  CB  . ASN D  1 67  ? 11.259  -0.069  -34.363 1.00 25.03 ? 66  ASN D CB  1 
ATOM   9943  C  CG  . ASN D  1 67  ? 11.572  -1.315  -35.137 1.00 27.73 ? 66  ASN D CG  1 
ATOM   9944  O  OD1 . ASN D  1 67  ? 11.320  -1.412  -36.365 1.00 26.84 ? 66  ASN D OD1 1 
ATOM   9945  N  ND2 . ASN D  1 67  ? 12.134  -2.293  -34.411 1.00 29.18 ? 66  ASN D ND2 1 
ATOM   9946  N  N   . LYS D  1 68  ? 10.925  1.573   -37.524 1.00 28.04 ? 67  LYS D N   1 
ATOM   9947  C  CA  . LYS D  1 68  ? 10.080  1.775   -38.709 1.00 30.06 ? 67  LYS D CA  1 
ATOM   9948  C  C   . LYS D  1 68  ? 9.423   0.477   -39.200 1.00 32.89 ? 67  LYS D C   1 
ATOM   9949  O  O   . LYS D  1 68  ? 8.377   0.533   -39.822 1.00 32.87 ? 67  LYS D O   1 
ATOM   9950  C  CB  . LYS D  1 68  ? 10.885  2.372   -39.867 1.00 33.04 ? 67  LYS D CB  1 
ATOM   9951  C  CG  . LYS D  1 68  ? 11.419  3.773   -39.633 1.00 34.43 ? 67  LYS D CG  1 
ATOM   9952  C  CD  . LYS D  1 68  ? 12.256  4.208   -40.824 1.00 37.65 ? 67  LYS D CD  1 
ATOM   9953  C  CE  . LYS D  1 68  ? 12.614  5.684   -40.788 1.00 40.37 ? 67  LYS D CE  1 
ATOM   9954  N  NZ  . LYS D  1 68  ? 13.653  5.998   -39.767 1.00 42.81 ? 67  LYS D NZ  1 
ATOM   9955  N  N   . THR D  1 69  ? 10.024  -0.673  -38.895 1.00 34.36 ? 68  THR D N   1 
ATOM   9956  C  CA  . THR D  1 69  ? 9.460   -1.988  -39.260 1.00 37.58 ? 68  THR D CA  1 
ATOM   9957  C  C   . THR D  1 69  ? 8.227   -2.329  -38.432 1.00 36.75 ? 68  THR D C   1 
ATOM   9958  O  O   . THR D  1 69  ? 7.173   -2.653  -38.974 1.00 39.77 ? 68  THR D O   1 
ATOM   9959  C  CB  . THR D  1 69  ? 10.496  -3.118  -39.057 1.00 37.88 ? 68  THR D CB  1 
ATOM   9960  O  OG1 . THR D  1 69  ? 11.690  -2.795  -39.771 1.00 39.92 ? 68  THR D OG1 1 
ATOM   9961  C  CG2 . THR D  1 69  ? 9.952   -4.465  -39.544 1.00 40.05 ? 68  THR D CG2 1 
ATOM   9962  N  N   . SER D  1 70  ? 8.345   -2.224  -37.118 1.00 34.95 ? 69  SER D N   1 
ATOM   9963  C  CA  . SER D  1 70  ? 7.218   -2.484  -36.251 1.00 31.49 ? 69  SER D CA  1 
ATOM   9964  C  C   . SER D  1 70  ? 6.278   -1.283  -36.119 1.00 29.89 ? 69  SER D C   1 
ATOM   9965  O  O   . SER D  1 70  ? 5.196   -1.443  -35.593 1.00 28.62 ? 69  SER D O   1 
ATOM   9966  C  CB  . SER D  1 70  ? 7.706   -2.905  -34.880 1.00 32.42 ? 69  SER D CB  1 
ATOM   9967  O  OG  . SER D  1 70  ? 8.449   -1.860  -34.280 1.00 31.87 ? 69  SER D OG  1 
ATOM   9968  N  N   . ARG D  1 71  ? 6.683   -0.098  -36.583 1.00 28.01 ? 70  ARG D N   1 
ATOM   9969  C  CA  . ARG D  1 71  ? 5.938   1.143   -36.344 1.00 27.91 ? 70  ARG D CA  1 
ATOM   9970  C  C   . ARG D  1 71  ? 5.631   1.309   -34.852 1.00 26.45 ? 70  ARG D C   1 
ATOM   9971  O  O   . ARG D  1 71  ? 4.506   1.571   -34.457 1.00 26.70 ? 70  ARG D O   1 
ATOM   9972  C  CB  . ARG D  1 71  ? 4.649   1.228   -37.181 1.00 28.46 ? 70  ARG D CB  1 
ATOM   9973  C  CG  . ARG D  1 71  ? 4.876   1.181   -38.688 1.00 29.43 ? 70  ARG D CG  1 
ATOM   9974  C  CD  . ARG D  1 71  ? 5.555   2.426   -39.215 1.00 29.51 ? 70  ARG D CD  1 
ATOM   9975  N  NE  . ARG D  1 71  ? 4.699   3.607   -39.074 1.00 29.09 ? 70  ARG D NE  1 
ATOM   9976  C  CZ  . ARG D  1 71  ? 3.982   4.175   -40.040 1.00 29.55 ? 70  ARG D CZ  1 
ATOM   9977  N  NH1 . ARG D  1 71  ? 4.029   3.712   -41.278 1.00 29.51 ? 70  ARG D NH1 1 
ATOM   9978  N  NH2 . ARG D  1 71  ? 3.251   5.258   -39.786 1.00 29.25 ? 70  ARG D NH2 1 
ATOM   9979  N  N   . ALA D  1 72  ? 6.659   1.144   -34.033 1.00 25.01 ? 71  ALA D N   1 
ATOM   9980  C  CA  . ALA D  1 72  ? 6.514   1.197   -32.595 1.00 23.38 ? 71  ALA D CA  1 
ATOM   9981  C  C   . ALA D  1 72  ? 7.799   1.766   -31.992 1.00 23.41 ? 71  ALA D C   1 
ATOM   9982  O  O   . ALA D  1 72  ? 8.855   1.648   -32.597 1.00 23.29 ? 71  ALA D O   1 
ATOM   9983  C  CB  . ALA D  1 72  ? 6.233   -0.194  -32.065 1.00 24.44 ? 71  ALA D CB  1 
ATOM   9984  N  N   . THR D  1 73  ? 7.711   2.304   -30.770 1.00 22.61 ? 72  THR D N   1 
ATOM   9985  C  CA  . THR D  1 73  ? 8.898   2.724   -30.059 1.00 22.02 ? 72  THR D CA  1 
ATOM   9986  C  C   . THR D  1 73  ? 9.424   1.616   -29.185 1.00 22.76 ? 72  THR D C   1 
ATOM   9987  O  O   . THR D  1 73  ? 8.698   0.702   -28.800 1.00 23.69 ? 72  THR D O   1 
ATOM   9988  C  CB  . THR D  1 73  ? 8.670   3.970   -29.202 1.00 21.86 ? 72  THR D CB  1 
ATOM   9989  O  OG1 . THR D  1 73  ? 7.559   3.750   -28.312 1.00 22.10 ? 72  THR D OG1 1 
ATOM   9990  C  CG2 . THR D  1 73  ? 8.426   5.129   -30.081 1.00 21.95 ? 72  THR D CG2 1 
ATOM   9991  N  N   . GLN D  1 74  ? 10.723  1.669   -28.911 1.00 22.47 ? 73  GLN D N   1 
ATOM   9992  C  CA  . GLN D  1 74  ? 11.351  0.739   -27.990 1.00 22.39 ? 73  GLN D CA  1 
ATOM   9993  C  C   . GLN D  1 74  ? 12.372  1.505   -27.163 1.00 21.35 ? 73  GLN D C   1 
ATOM   9994  O  O   . GLN D  1 74  ? 12.774  2.620   -27.515 1.00 20.23 ? 73  GLN D O   1 
ATOM   9995  C  CB  . GLN D  1 74  ? 11.970  -0.460  -28.740 1.00 25.12 ? 73  GLN D CB  1 
ATOM   9996  C  CG  . GLN D  1 74  ? 12.725  -0.086  -29.988 1.00 27.03 ? 73  GLN D CG  1 
ATOM   9997  C  CD  . GLN D  1 74  ? 13.129  -1.265  -30.855 1.00 27.23 ? 73  GLN D CD  1 
ATOM   9998  O  OE1 . GLN D  1 74  ? 12.316  -1.896  -31.531 1.00 27.22 ? 73  GLN D OE1 1 
ATOM   9999  N  NE2 . GLN D  1 74  ? 14.412  -1.556  -30.841 1.00 28.01 ? 73  GLN D NE2 1 
ATOM   10000 N  N   . PHE D  1 75  ? 12.760  0.941   -26.028 1.00 21.42 ? 74  PHE D N   1 
ATOM   10001 C  CA  . PHE D  1 75  ? 13.792  1.574   -25.203 1.00 21.54 ? 74  PHE D CA  1 
ATOM   10002 C  C   . PHE D  1 75  ? 15.167  1.302   -25.841 1.00 21.84 ? 74  PHE D C   1 
ATOM   10003 O  O   . PHE D  1 75  ? 15.329  0.348   -26.592 1.00 22.86 ? 74  PHE D O   1 
ATOM   10004 C  CB  . PHE D  1 75  ? 13.761  1.030   -23.771 1.00 22.35 ? 74  PHE D CB  1 
ATOM   10005 C  CG  . PHE D  1 75  ? 12.392  1.053   -23.119 1.00 22.60 ? 74  PHE D CG  1 
ATOM   10006 C  CD1 . PHE D  1 75  ? 11.497  2.083   -23.362 1.00 23.20 ? 74  PHE D CD1 1 
ATOM   10007 C  CD2 . PHE D  1 75  ? 12.016  0.030   -22.261 1.00 23.81 ? 74  PHE D CD2 1 
ATOM   10008 C  CE1 . PHE D  1 75  ? 10.239  2.073   -22.777 1.00 24.02 ? 74  PHE D CE1 1 
ATOM   10009 C  CE2 . PHE D  1 75  ? 10.776  0.038   -21.633 1.00 23.41 ? 74  PHE D CE2 1 
ATOM   10010 C  CZ  . PHE D  1 75  ? 9.887   1.044   -21.903 1.00 24.45 ? 74  PHE D CZ  1 
ATOM   10011 N  N   . PRO D  1 76  ? 16.173  2.142   -25.548 1.00 22.47 ? 75  PRO D N   1 
ATOM   10012 C  CA  . PRO D  1 76  ? 17.529  1.805   -25.991 1.00 22.63 ? 75  PRO D CA  1 
ATOM   10013 C  C   . PRO D  1 76  ? 18.005  0.441   -25.488 1.00 23.04 ? 75  PRO D C   1 
ATOM   10014 O  O   . PRO D  1 76  ? 17.500  -0.062  -24.485 1.00 21.22 ? 75  PRO D O   1 
ATOM   10015 C  CB  . PRO D  1 76  ? 18.377  2.925   -25.408 1.00 23.32 ? 75  PRO D CB  1 
ATOM   10016 C  CG  . PRO D  1 76  ? 17.419  4.059   -25.238 1.00 22.64 ? 75  PRO D CG  1 
ATOM   10017 C  CD  . PRO D  1 76  ? 16.134  3.416   -24.814 1.00 21.77 ? 75  PRO D CD  1 
ATOM   10018 N  N   . ASP D  1 77  ? 18.978  -0.154  -26.183 1.00 24.78 ? 76  ASP D N   1 
ATOM   10019 C  CA  . ASP D  1 77  ? 19.515  -1.440  -25.786 1.00 27.69 ? 76  ASP D CA  1 
ATOM   10020 C  C   . ASP D  1 77  ? 19.946  -1.408  -24.334 1.00 25.65 ? 76  ASP D C   1 
ATOM   10021 O  O   . ASP D  1 77  ? 20.698  -0.530  -23.931 1.00 25.33 ? 76  ASP D O   1 
ATOM   10022 C  CB  . ASP D  1 77  ? 20.742  -1.843  -26.644 1.00 33.78 ? 76  ASP D CB  1 
ATOM   10023 C  CG  . ASP D  1 77  ? 20.395  -2.053  -28.114 1.00 40.21 ? 76  ASP D CG  1 
ATOM   10024 O  OD1 . ASP D  1 77  ? 19.195  -2.259  -28.430 1.00 45.67 ? 76  ASP D OD1 1 
ATOM   10025 O  OD2 . ASP D  1 77  ? 21.326  -2.021  -28.958 1.00 48.57 ? 76  ASP D OD2 1 
ATOM   10026 N  N   . GLY D  1 78  ? 19.516  -2.410  -23.579 1.00 24.01 ? 77  GLY D N   1 
ATOM   10027 C  CA  . GLY D  1 78  ? 19.900  -2.579  -22.181 1.00 24.02 ? 77  GLY D CA  1 
ATOM   10028 C  C   . GLY D  1 78  ? 19.271  -1.596  -21.204 1.00 23.53 ? 77  GLY D C   1 
ATOM   10029 O  O   . GLY D  1 78  ? 19.726  -1.485  -20.070 1.00 23.46 ? 77  GLY D O   1 
ATOM   10030 N  N   . VAL D  1 79  ? 18.209  -0.902  -21.618 1.00 21.22 ? 78  VAL D N   1 
ATOM   10031 C  CA  . VAL D  1 79  ? 17.535  0.031   -20.746 1.00 21.07 ? 78  VAL D CA  1 
ATOM   10032 C  C   . VAL D  1 79  ? 16.105  -0.450  -20.520 1.00 20.10 ? 78  VAL D C   1 
ATOM   10033 O  O   . VAL D  1 79  ? 15.420  -0.803  -21.475 1.00 20.86 ? 78  VAL D O   1 
ATOM   10034 C  CB  . VAL D  1 79  ? 17.479  1.453   -21.343 1.00 20.94 ? 78  VAL D CB  1 
ATOM   10035 C  CG1 . VAL D  1 79  ? 16.715  2.400   -20.432 1.00 21.21 ? 78  VAL D CG1 1 
ATOM   10036 C  CG2 . VAL D  1 79  ? 18.882  1.990   -21.607 1.00 22.30 ? 78  VAL D CG2 1 
ATOM   10037 N  N   . ASP D  1 80  ? 15.667  -0.468  -19.264 1.00 18.98 ? 79  ASP D N   1 
ATOM   10038 C  CA  . ASP D  1 80  ? 14.254  -0.619  -18.972 1.00 17.78 ? 79  ASP D CA  1 
ATOM   10039 C  C   . ASP D  1 80  ? 13.746  0.600   -18.241 1.00 17.45 ? 79  ASP D C   1 
ATOM   10040 O  O   . ASP D  1 80  ? 14.404  1.081   -17.327 1.00 17.86 ? 79  ASP D O   1 
ATOM   10041 C  CB  . ASP D  1 80  ? 13.937  -1.845  -18.122 1.00 18.02 ? 79  ASP D CB  1 
ATOM   10042 C  CG  . ASP D  1 80  ? 12.418  -2.110  -18.079 1.00 17.90 ? 79  ASP D CG  1 
ATOM   10043 O  OD1 . ASP D  1 80  ? 11.828  -2.234  -19.198 1.00 18.38 ? 79  ASP D OD1 1 
ATOM   10044 O  OD2 . ASP D  1 80  ? 11.818  -2.159  -16.986 1.00 18.00 ? 79  ASP D OD2 1 
ATOM   10045 N  N   . VAL D  1 81  ? 12.535  1.036   -18.583 1.00 16.50 ? 80  VAL D N   1 
ATOM   10046 C  CA  . VAL D  1 81  ? 11.895  2.144   -17.906 1.00 16.20 ? 80  VAL D CA  1 
ATOM   10047 C  C   . VAL D  1 81  ? 10.517  1.684   -17.388 1.00 16.60 ? 80  VAL D C   1 
ATOM   10048 O  O   . VAL D  1 81  ? 9.715   1.139   -18.148 1.00 16.77 ? 80  VAL D O   1 
ATOM   10049 C  CB  . VAL D  1 81  ? 11.727  3.361   -18.830 1.00 16.41 ? 80  VAL D CB  1 
ATOM   10050 C  CG1 . VAL D  1 81  ? 11.020  4.514   -18.109 1.00 16.02 ? 80  VAL D CG1 1 
ATOM   10051 C  CG2 . VAL D  1 81  ? 13.081  3.857   -19.318 1.00 17.01 ? 80  VAL D CG2 1 
ATOM   10052 N  N   . ARG D  1 82  ? 10.263  1.880   -16.106 1.00 16.63 ? 81  ARG D N   1 
ATOM   10053 C  CA  . ARG D  1 82  ? 8.970   1.523   -15.507 1.00 17.10 ? 81  ARG D CA  1 
ATOM   10054 C  C   . ARG D  1 82  ? 8.324   2.687   -14.793 1.00 16.16 ? 81  ARG D C   1 
ATOM   10055 O  O   . ARG D  1 82  ? 8.971   3.673   -14.450 1.00 16.34 ? 81  ARG D O   1 
ATOM   10056 C  CB  . ARG D  1 82  ? 9.094   0.346   -14.577 1.00 19.07 ? 81  ARG D CB  1 
ATOM   10057 C  CG  . ARG D  1 82  ? 9.661   0.652   -13.240 1.00 20.91 ? 81  ARG D CG  1 
ATOM   10058 C  CD  . ARG D  1 82  ? 9.548   -0.538  -12.282 1.00 22.82 ? 81  ARG D CD  1 
ATOM   10059 N  NE  . ARG D  1 82  ? 10.182  -0.157  -11.031 1.00 24.35 ? 81  ARG D NE  1 
ATOM   10060 C  CZ  . ARG D  1 82  ? 10.627  -0.998  -10.103 1.00 26.79 ? 81  ARG D CZ  1 
ATOM   10061 N  NH1 . ARG D  1 82  ? 10.485  -2.322  -10.239 1.00 25.95 ? 81  ARG D NH1 1 
ATOM   10062 N  NH2 . ARG D  1 82  ? 11.224  -0.511  -9.018  1.00 28.34 ? 81  ARG D NH2 1 
ATOM   10063 N  N   . VAL D  1 83  ? 7.013   2.572   -14.622 1.00 15.38 ? 82  VAL D N   1 
ATOM   10064 C  CA  . VAL D  1 83  ? 6.208   3.623   -14.025 1.00 15.30 ? 82  VAL D CA  1 
ATOM   10065 C  C   . VAL D  1 83  ? 5.880   3.139   -12.622 1.00 15.25 ? 82  VAL D C   1 
ATOM   10066 O  O   . VAL D  1 83  ? 5.136   2.194   -12.476 1.00 15.27 ? 82  VAL D O   1 
ATOM   10067 C  CB  . VAL D  1 83  ? 4.884   3.808   -14.806 1.00 14.90 ? 82  VAL D CB  1 
ATOM   10068 C  CG1 . VAL D  1 83  ? 3.995   4.861   -14.151 1.00 15.52 ? 82  VAL D CG1 1 
ATOM   10069 C  CG2 . VAL D  1 83  ? 5.183   4.188   -16.250 1.00 15.23 ? 82  VAL D CG2 1 
ATOM   10070 N  N   . PRO D  1 84  ? 6.427   3.789   -11.585 1.00 16.07 ? 83  PRO D N   1 
ATOM   10071 C  CA  . PRO D  1 84  ? 6.092   3.375   -10.218 1.00 16.47 ? 83  PRO D CA  1 
ATOM   10072 C  C   . PRO D  1 84  ? 4.754   3.966   -9.769  1.00 16.72 ? 83  PRO D C   1 
ATOM   10073 O  O   . PRO D  1 84  ? 4.289   4.921   -10.363 1.00 16.51 ? 83  PRO D O   1 
ATOM   10074 C  CB  . PRO D  1 84  ? 7.222   3.972   -9.391  1.00 16.98 ? 83  PRO D CB  1 
ATOM   10075 C  CG  . PRO D  1 84  ? 7.597   5.211   -10.144 1.00 16.93 ? 83  PRO D CG  1 
ATOM   10076 C  CD  . PRO D  1 84  ? 7.430   4.872   -11.603 1.00 16.27 ? 83  PRO D CD  1 
ATOM   10077 N  N   . GLY D  1 85  ? 4.146   3.387   -8.730  1.00 17.21 ? 84  GLY D N   1 
ATOM   10078 C  CA  . GLY D  1 85  ? 3.067   4.064   -8.006  1.00 16.59 ? 84  GLY D CA  1 
ATOM   10079 C  C   . GLY D  1 85  ? 1.687   3.986   -8.618  1.00 16.74 ? 84  GLY D C   1 
ATOM   10080 O  O   . GLY D  1 85  ? 0.820   4.806   -8.252  1.00 16.08 ? 84  GLY D O   1 
ATOM   10081 N  N   . PHE D  1 86  ? 1.448   3.032   -9.525  1.00 16.40 ? 85  PHE D N   1 
ATOM   10082 C  CA  . PHE D  1 86  ? 0.100   2.879   -10.093 1.00 16.47 ? 85  PHE D CA  1 
ATOM   10083 C  C   . PHE D  1 86  ? -0.860  2.457   -8.973  1.00 16.96 ? 85  PHE D C   1 
ATOM   10084 O  O   . PHE D  1 86  ? -0.592  1.516   -8.220  1.00 16.12 ? 85  PHE D O   1 
ATOM   10085 C  CB  . PHE D  1 86  ? 0.058   1.880   -11.267 1.00 17.29 ? 85  PHE D CB  1 
ATOM   10086 C  CG  . PHE D  1 86  ? -1.269  1.868   -11.982 1.00 17.49 ? 85  PHE D CG  1 
ATOM   10087 C  CD1 . PHE D  1 86  ? -2.297  1.051   -11.521 1.00 18.58 ? 85  PHE D CD1 1 
ATOM   10088 C  CD2 . PHE D  1 86  ? -1.527  2.710   -13.055 1.00 17.64 ? 85  PHE D CD2 1 
ATOM   10089 C  CE1 . PHE D  1 86  ? -3.544  1.049   -12.151 1.00 19.36 ? 85  PHE D CE1 1 
ATOM   10090 C  CE2 . PHE D  1 86  ? -2.770  2.721   -13.674 1.00 17.94 ? 85  PHE D CE2 1 
ATOM   10091 C  CZ  . PHE D  1 86  ? -3.787  1.905   -13.212 1.00 18.61 ? 85  PHE D CZ  1 
ATOM   10092 N  N   . GLY D  1 87  ? -1.966  3.177   -8.838  1.00 16.08 ? 86  GLY D N   1 
ATOM   10093 C  CA  . GLY D  1 87  ? -2.920  2.931   -7.758  1.00 17.16 ? 86  GLY D CA  1 
ATOM   10094 C  C   . GLY D  1 87  ? -2.614  3.707   -6.482  1.00 17.11 ? 86  GLY D C   1 
ATOM   10095 O  O   . GLY D  1 87  ? -3.414  3.687   -5.539  1.00 17.78 ? 86  GLY D O   1 
ATOM   10096 N  N   . LYS D  1 88  ? -1.442  4.356   -6.427  1.00 17.12 ? 87  LYS D N   1 
ATOM   10097 C  CA  . LYS D  1 88  ? -1.005  5.161   -5.282  1.00 19.40 ? 87  LYS D CA  1 
ATOM   10098 C  C   . LYS D  1 88  ? -0.975  6.631   -5.759  1.00 18.75 ? 87  LYS D C   1 
ATOM   10099 O  O   . LYS D  1 88  ? -1.343  6.901   -6.889  1.00 18.40 ? 87  LYS D O   1 
ATOM   10100 C  CB  . LYS D  1 88  ? 0.374   4.733   -4.819  1.00 21.03 ? 87  LYS D CB  1 
ATOM   10101 C  CG  . LYS D  1 88  ? 0.545   3.246   -4.583  1.00 23.19 ? 87  LYS D CG  1 
ATOM   10102 C  CD  . LYS D  1 88  ? -0.389  2.741   -3.504  1.00 27.80 ? 87  LYS D CD  1 
ATOM   10103 C  CE  . LYS D  1 88  ? -0.154  1.248   -3.241  1.00 31.77 ? 87  LYS D CE  1 
ATOM   10104 N  NZ  . LYS D  1 88  ? -1.334  0.639   -2.553  1.00 33.76 ? 87  LYS D NZ  1 
ATOM   10105 N  N   . THR D  1 89  ? -0.558  7.556   -4.913  1.00 18.79 ? 88  THR D N   1 
ATOM   10106 C  CA  . THR D  1 89  ? -0.507  8.961   -5.297  1.00 19.16 ? 88  THR D CA  1 
ATOM   10107 C  C   . THR D  1 89  ? 0.883   9.563   -5.211  1.00 18.89 ? 88  THR D C   1 
ATOM   10108 O  O   . THR D  1 89  ? 1.116   10.625  -5.787  1.00 16.87 ? 88  THR D O   1 
ATOM   10109 C  CB  . THR D  1 89  ? -1.477  9.844   -4.457  1.00 21.02 ? 88  THR D CB  1 
ATOM   10110 O  OG1 . THR D  1 89  ? -1.083  9.830   -3.080  1.00 21.74 ? 88  THR D OG1 1 
ATOM   10111 C  CG2 . THR D  1 89  ? -2.916  9.339   -4.586  1.00 22.12 ? 88  THR D CG2 1 
ATOM   10112 N  N   . PHE D  1 90  ? 1.823   8.884   -4.556  1.00 18.62 ? 89  PHE D N   1 
ATOM   10113 C  CA  . PHE D  1 90  ? 3.123   9.499   -4.299  1.00 19.50 ? 89  PHE D CA  1 
ATOM   10114 C  C   . PHE D  1 90  ? 3.852   9.938   -5.586  1.00 19.06 ? 89  PHE D C   1 
ATOM   10115 O  O   . PHE D  1 90  ? 4.525   10.963  -5.598  1.00 19.13 ? 89  PHE D O   1 
ATOM   10116 C  CB  . PHE D  1 90  ? 4.011   8.577   -3.450  1.00 20.89 ? 89  PHE D CB  1 
ATOM   10117 C  CG  . PHE D  1 90  ? 4.515   7.353   -4.170  1.00 21.72 ? 89  PHE D CG  1 
ATOM   10118 C  CD1 . PHE D  1 90  ? 5.693   7.404   -4.925  1.00 22.77 ? 89  PHE D CD1 1 
ATOM   10119 C  CD2 . PHE D  1 90  ? 3.858   6.142   -4.055  1.00 22.55 ? 89  PHE D CD2 1 
ATOM   10120 C  CE1 . PHE D  1 90  ? 6.177   6.265   -5.573  1.00 23.16 ? 89  PHE D CE1 1 
ATOM   10121 C  CE2 . PHE D  1 90  ? 4.356   4.997   -4.676  1.00 23.27 ? 89  PHE D CE2 1 
ATOM   10122 C  CZ  . PHE D  1 90  ? 5.505   5.066   -5.454  1.00 23.02 ? 89  PHE D CZ  1 
ATOM   10123 N  N   . SER D  1 91  ? 3.712   9.164   -6.660  1.00 18.58 ? 90  SER D N   1 
ATOM   10124 C  CA  . SER D  1 91  ? 4.522   9.396   -7.863  1.00 18.96 ? 90  SER D CA  1 
ATOM   10125 C  C   . SER D  1 91  ? 3.979   10.514  -8.751  1.00 18.30 ? 90  SER D C   1 
ATOM   10126 O  O   . SER D  1 91  ? 4.695   10.990  -9.646  1.00 16.56 ? 90  SER D O   1 
ATOM   10127 C  CB  . SER D  1 91  ? 4.703   8.128   -8.672  1.00 18.76 ? 90  SER D CB  1 
ATOM   10128 O  OG  . SER D  1 91  ? 3.528   7.788   -9.376  1.00 19.54 ? 90  SER D OG  1 
ATOM   10129 N  N   . LEU D  1 92  ? 2.730   10.922  -8.513  1.00 17.68 ? 91  LEU D N   1 
ATOM   10130 C  CA  . LEU D  1 92  ? 2.218   12.142  -9.116  1.00 18.58 ? 91  LEU D CA  1 
ATOM   10131 C  C   . LEU D  1 92  ? 2.143   13.340  -8.156  1.00 17.44 ? 91  LEU D C   1 
ATOM   10132 O  O   . LEU D  1 92  ? 2.073   14.473  -8.620  1.00 17.42 ? 91  LEU D O   1 
ATOM   10133 C  CB  . LEU D  1 92  ? 0.940   11.958  -9.947  1.00 21.24 ? 91  LEU D CB  1 
ATOM   10134 C  CG  . LEU D  1 92  ? -0.152  11.058  -9.512  1.00 23.77 ? 91  LEU D CG  1 
ATOM   10135 C  CD1 . LEU D  1 92  ? -0.818  11.725  -8.298  1.00 26.93 ? 91  LEU D CD1 1 
ATOM   10136 C  CD2 . LEU D  1 92  ? -1.144  10.901  -10.653 1.00 23.97 ? 91  LEU D CD2 1 
ATOM   10137 N  N   . GLU D  1 93  ? 2.203   13.127  -6.841  1.00 16.47 ? 92  GLU D N   1 
ATOM   10138 C  CA  . GLU D  1 93  ? 2.271   14.262  -5.899  1.00 17.11 ? 92  GLU D CA  1 
ATOM   10139 C  C   . GLU D  1 93  ? 3.613   14.965  -6.026  1.00 17.17 ? 92  GLU D C   1 
ATOM   10140 O  O   . GLU D  1 93  ? 3.680   16.181  -6.037  1.00 17.45 ? 92  GLU D O   1 
ATOM   10141 C  CB  . GLU D  1 93  ? 2.049   13.825  -4.435  1.00 17.02 ? 92  GLU D CB  1 
ATOM   10142 C  CG  . GLU D  1 93  ? 0.620   13.428  -4.109  1.00 17.61 ? 92  GLU D CG  1 
ATOM   10143 C  CD  . GLU D  1 93  ? 0.418   13.142  -2.641  1.00 18.05 ? 92  GLU D CD  1 
ATOM   10144 O  OE1 . GLU D  1 93  ? 0.564   14.083  -1.837  1.00 18.91 ? 92  GLU D OE1 1 
ATOM   10145 O  OE2 . GLU D  1 93  ? 0.107   11.984  -2.296  1.00 18.56 ? 92  GLU D OE2 1 
ATOM   10146 N  N   . PHE D  1 94  ? 4.671   14.173  -6.093  1.00 17.85 ? 93  PHE D N   1 
ATOM   10147 C  CA  . PHE D  1 94  ? 6.055   14.650  -6.138  1.00 19.39 ? 93  PHE D CA  1 
ATOM   10148 C  C   . PHE D  1 94  ? 6.768   13.988  -7.304  1.00 19.40 ? 93  PHE D C   1 
ATOM   10149 O  O   . PHE D  1 94  ? 6.867   12.766  -7.337  1.00 18.45 ? 93  PHE D O   1 
ATOM   10150 C  CB  . PHE D  1 94  ? 6.788   14.269  -4.858  1.00 21.62 ? 93  PHE D CB  1 
ATOM   10151 C  CG  . PHE D  1 94  ? 6.304   14.989  -3.637  1.00 23.80 ? 93  PHE D CG  1 
ATOM   10152 C  CD1 . PHE D  1 94  ? 6.546   16.335  -3.498  1.00 24.80 ? 93  PHE D CD1 1 
ATOM   10153 C  CD2 . PHE D  1 94  ? 5.616   14.304  -2.627  1.00 25.71 ? 93  PHE D CD2 1 
ATOM   10154 C  CE1 . PHE D  1 94  ? 6.104   17.006  -2.385  1.00 26.59 ? 93  PHE D CE1 1 
ATOM   10155 C  CE2 . PHE D  1 94  ? 5.189   14.979  -1.487  1.00 26.35 ? 93  PHE D CE2 1 
ATOM   10156 C  CZ  . PHE D  1 94  ? 5.434   16.329  -1.387  1.00 26.72 ? 93  PHE D CZ  1 
ATOM   10157 N  N   . LEU D  1 95  ? 7.251   14.774  -8.256  1.00 18.61 ? 94  LEU D N   1 
ATOM   10158 C  CA  . LEU D  1 95  ? 7.969   14.234  -9.399  1.00 18.51 ? 94  LEU D CA  1 
ATOM   10159 C  C   . LEU D  1 95  ? 9.385   13.856  -8.994  1.00 19.92 ? 94  LEU D C   1 
ATOM   10160 O  O   . LEU D  1 95  ? 9.963   12.906  -9.526  1.00 20.00 ? 94  LEU D O   1 
ATOM   10161 C  CB  . LEU D  1 95  ? 7.983   15.228  -10.549 1.00 18.79 ? 94  LEU D CB  1 
ATOM   10162 C  CG  . LEU D  1 95  ? 6.609   15.683  -11.017 1.00 19.12 ? 94  LEU D CG  1 
ATOM   10163 C  CD1 . LEU D  1 95  ? 6.740   16.710  -12.134 1.00 20.05 ? 94  LEU D CD1 1 
ATOM   10164 C  CD2 . LEU D  1 95  ? 5.742   14.515  -11.449 1.00 19.88 ? 94  LEU D CD2 1 
ATOM   10165 N  N   . ASP D  1 96  ? 9.937   14.598  -8.041  1.00 20.03 ? 95  ASP D N   1 
ATOM   10166 C  CA  . ASP D  1 96  ? 11.262  14.330  -7.489  1.00 22.86 ? 95  ASP D CA  1 
ATOM   10167 C  C   . ASP D  1 96  ? 11.071  13.651  -6.144  1.00 23.00 ? 95  ASP D C   1 
ATOM   10168 O  O   . ASP D  1 96  ? 10.500  14.255  -5.224  1.00 23.63 ? 95  ASP D O   1 
ATOM   10169 C  CB  . ASP D  1 96  ? 12.043  15.644  -7.339  1.00 24.68 ? 95  ASP D CB  1 
ATOM   10170 C  CG  . ASP D  1 96  ? 13.506  15.430  -6.990  1.00 28.83 ? 95  ASP D CG  1 
ATOM   10171 O  OD1 . ASP D  1 96  ? 13.832  14.404  -6.359  1.00 30.43 ? 95  ASP D OD1 1 
ATOM   10172 O  OD2 . ASP D  1 96  ? 14.333  16.296  -7.381  1.00 33.10 ? 95  ASP D OD2 1 
ATOM   10173 N  N   . PRO D  1 97  ? 11.528  12.398  -6.000  1.00 25.02 ? 96  PRO D N   1 
ATOM   10174 C  CA  . PRO D  1 97  ? 11.367  11.700  -4.716  1.00 27.03 ? 96  PRO D CA  1 
ATOM   10175 C  C   . PRO D  1 97  ? 12.085  12.349  -3.522  1.00 28.21 ? 96  PRO D C   1 
ATOM   10176 O  O   . PRO D  1 97  ? 11.785  11.991  -2.399  1.00 29.23 ? 96  PRO D O   1 
ATOM   10177 C  CB  . PRO D  1 97  ? 11.934  10.287  -4.967  1.00 27.82 ? 96  PRO D CB  1 
ATOM   10178 C  CG  . PRO D  1 97  ? 12.348  10.244  -6.380  1.00 26.72 ? 96  PRO D CG  1 
ATOM   10179 C  CD  . PRO D  1 97  ? 12.304  11.609  -6.971  1.00 26.67 ? 96  PRO D CD  1 
ATOM   10180 N  N   . SER D  1 98  ? 12.978  13.304  -3.742  1.00 28.04 ? 97  SER D N   1 
ATOM   10181 C  CA  . SER D  1 98  ? 13.486  14.135  -2.638  1.00 32.40 ? 97  SER D CA  1 
ATOM   10182 C  C   . SER D  1 98  ? 12.375  15.026  -2.033  1.00 31.67 ? 97  SER D C   1 
ATOM   10183 O  O   . SER D  1 98  ? 12.566  15.615  -0.977  1.00 30.21 ? 97  SER D O   1 
ATOM   10184 C  CB  . SER D  1 98  ? 14.605  15.046  -3.121  1.00 32.91 ? 97  SER D CB  1 
ATOM   10185 O  OG  . SER D  1 98  ? 14.057  16.117  -3.875  1.00 36.02 ? 97  SER D OG  1 
ATOM   10186 N  N   . LYS D  1 99  ? 11.255  15.142  -2.753  1.00 30.43 ? 98  LYS D N   1 
ATOM   10187 C  CA  . LYS D  1 99  ? 10.096  15.938  -2.376  1.00 29.87 ? 98  LYS D CA  1 
ATOM   10188 C  C   . LYS D  1 99  ? 10.369  17.436  -2.440  1.00 30.24 ? 98  LYS D C   1 
ATOM   10189 O  O   . LYS D  1 99  ? 9.693   18.231  -1.801  1.00 30.66 ? 98  LYS D O   1 
ATOM   10190 C  CB  . LYS D  1 99  ? 9.551   15.492  -1.021  1.00 30.73 ? 98  LYS D CB  1 
ATOM   10191 C  CG  . LYS D  1 99  ? 9.150   14.030  -1.017  1.00 31.56 ? 98  LYS D CG  1 
ATOM   10192 C  CD  . LYS D  1 99  ? 8.501   13.644  0.288   1.00 34.11 ? 98  LYS D CD  1 
ATOM   10193 C  CE  . LYS D  1 99  ? 8.018   12.214  0.235   1.00 35.65 ? 98  LYS D CE  1 
ATOM   10194 N  NZ  . LYS D  1 99  ? 7.321   11.851  1.503   1.00 39.32 ? 98  LYS D NZ  1 
ATOM   10195 N  N   . SER D  1 100 ? 11.355  17.807  -3.249  1.00 30.03 ? 99  SER D N   1 
ATOM   10196 C  CA  . SER D  1 100 ? 11.671  19.192  -3.527  1.00 31.06 ? 99  SER D CA  1 
ATOM   10197 C  C   . SER D  1 100 ? 10.490  19.923  -4.177  1.00 28.48 ? 99  SER D C   1 
ATOM   10198 O  O   . SER D  1 100 ? 9.724   19.331  -4.954  1.00 25.76 ? 99  SER D O   1 
ATOM   10199 C  CB  . SER D  1 100 ? 12.865  19.247  -4.477  1.00 33.22 ? 99  SER D CB  1 
ATOM   10200 O  OG  . SER D  1 100 ? 13.045  20.562  -4.950  1.00 39.16 ? 99  SER D OG  1 
ATOM   10201 N  N   . SER D  1 101 ? 10.364  21.213  -3.887  1.00 27.49 ? 100 SER D N   1 
ATOM   10202 C  CA  . SER D  1 101 ? 9.267   22.026  -4.446  1.00 27.81 ? 100 SER D CA  1 
ATOM   10203 C  C   . SER D  1 101 ? 9.264   22.068  -5.968  1.00 27.22 ? 100 SER D C   1 
ATOM   10204 O  O   . SER D  1 101 ? 8.202   22.209  -6.572  1.00 25.53 ? 100 SER D O   1 
ATOM   10205 C  CB  . SER D  1 101 ? 9.310   23.452  -3.895  1.00 30.79 ? 100 SER D CB  1 
ATOM   10206 O  OG  . SER D  1 101 ? 10.501  24.091  -4.269  1.00 31.98 ? 100 SER D OG  1 
ATOM   10207 N  N   . VAL D  1 102 ? 10.449  21.944  -6.578  1.00 27.77 ? 101 VAL D N   1 
ATOM   10208 C  CA  . VAL D  1 102 ? 10.588  21.887  -8.049  1.00 28.61 ? 101 VAL D CA  1 
ATOM   10209 C  C   . VAL D  1 102 ? 9.698   20.779  -8.648  1.00 26.48 ? 101 VAL D C   1 
ATOM   10210 O  O   . VAL D  1 102 ? 9.163   20.937  -9.742  1.00 26.86 ? 101 VAL D O   1 
ATOM   10211 C  CB  . VAL D  1 102 ? 12.081  21.714  -8.522  1.00 31.20 ? 101 VAL D CB  1 
ATOM   10212 C  CG1 . VAL D  1 102 ? 12.592  20.300  -8.268  1.00 33.02 ? 101 VAL D CG1 1 
ATOM   10213 C  CG2 . VAL D  1 102 ? 12.209  22.033  -10.000 1.00 32.88 ? 101 VAL D CG2 1 
ATOM   10214 N  N   . GLY D  1 103 ? 9.507   19.685  -7.932  1.00 23.38 ? 102 GLY D N   1 
ATOM   10215 C  CA  . GLY D  1 103 ? 8.683   18.625  -8.449  1.00 22.32 ? 102 GLY D CA  1 
ATOM   10216 C  C   . GLY D  1 103 ? 7.297   18.507  -7.843  1.00 21.68 ? 102 GLY D C   1 
ATOM   10217 O  O   . GLY D  1 103 ? 6.620   17.498  -8.050  1.00 20.75 ? 102 GLY D O   1 
ATOM   10218 N  N   . SER D  1 104 ? 6.853   19.504  -7.085  1.00 20.22 ? 103 SER D N   1 
ATOM   10219 C  CA  . SER D  1 104 ? 5.543   19.370  -6.422  1.00 20.33 ? 103 SER D CA  1 
ATOM   10220 C  C   . SER D  1 104 ? 4.471   19.564  -7.483  1.00 19.62 ? 103 SER D C   1 
ATOM   10221 O  O   . SER D  1 104 ? 4.397   20.623  -8.096  1.00 20.68 ? 103 SER D O   1 
ATOM   10222 C  CB  . SER D  1 104 ? 5.395   20.404  -5.298  1.00 21.22 ? 103 SER D CB  1 
ATOM   10223 O  OG  . SER D  1 104 ? 4.099   20.291  -4.694  1.00 21.74 ? 103 SER D OG  1 
ATOM   10224 N  N   . TYR D  1 105 ? 3.637   18.552  -7.708  1.00 18.36 ? 104 TYR D N   1 
ATOM   10225 C  CA  . TYR D  1 105 ? 2.714   18.569  -8.832  1.00 16.55 ? 104 TYR D CA  1 
ATOM   10226 C  C   . TYR D  1 105 ? 1.270   18.385  -8.311  1.00 16.61 ? 104 TYR D C   1 
ATOM   10227 O  O   . TYR D  1 105 ? 0.548   19.360  -8.175  1.00 17.54 ? 104 TYR D O   1 
ATOM   10228 C  CB  . TYR D  1 105 ? 3.159   17.521  -9.873  1.00 16.16 ? 104 TYR D CB  1 
ATOM   10229 C  CG  . TYR D  1 105 ? 2.317   17.410  -11.113 1.00 15.16 ? 104 TYR D CG  1 
ATOM   10230 C  CD1 . TYR D  1 105 ? 1.896   18.543  -11.806 1.00 15.91 ? 104 TYR D CD1 1 
ATOM   10231 C  CD2 . TYR D  1 105 ? 1.979   16.176  -11.636 1.00 14.68 ? 104 TYR D CD2 1 
ATOM   10232 C  CE1 . TYR D  1 105 ? 1.134   18.434  -12.985 1.00 15.63 ? 104 TYR D CE1 1 
ATOM   10233 C  CE2 . TYR D  1 105 ? 1.196   16.069  -12.786 1.00 15.33 ? 104 TYR D CE2 1 
ATOM   10234 C  CZ  . TYR D  1 105 ? 0.768   17.200  -13.454 1.00 15.53 ? 104 TYR D CZ  1 
ATOM   10235 O  OH  . TYR D  1 105 ? 0.004   17.050  -14.615 1.00 16.70 ? 104 TYR D OH  1 
ATOM   10236 N  N   . PHE D  1 106 ? 0.838   17.155  -8.040  1.00 17.00 ? 105 PHE D N   1 
ATOM   10237 C  CA  . PHE D  1 106 ? -0.506  16.941  -7.442  1.00 16.45 ? 105 PHE D CA  1 
ATOM   10238 C  C   . PHE D  1 106 ? -0.510  17.060  -5.904  1.00 16.41 ? 105 PHE D C   1 
ATOM   10239 O  O   . PHE D  1 106 ? -1.555  16.907  -5.291  1.00 16.03 ? 105 PHE D O   1 
ATOM   10240 C  CB  . PHE D  1 106 ? -1.077  15.585  -7.844  1.00 17.09 ? 105 PHE D CB  1 
ATOM   10241 C  CG  . PHE D  1 106 ? -1.869  15.581  -9.115  1.00 17.74 ? 105 PHE D CG  1 
ATOM   10242 C  CD1 . PHE D  1 106 ? -3.240  15.806  -9.104  1.00 18.68 ? 105 PHE D CD1 1 
ATOM   10243 C  CD2 . PHE D  1 106 ? -1.273  15.308  -10.324 1.00 18.68 ? 105 PHE D CD2 1 
ATOM   10244 C  CE1 . PHE D  1 106 ? -3.988  15.771  -10.282 1.00 18.51 ? 105 PHE D CE1 1 
ATOM   10245 C  CE2 . PHE D  1 106 ? -2.017  15.285  -11.520 1.00 19.51 ? 105 PHE D CE2 1 
ATOM   10246 C  CZ  . PHE D  1 106 ? -3.381  15.505  -11.493 1.00 18.56 ? 105 PHE D CZ  1 
ATOM   10247 N  N   . HIS D  1 107 ? 0.647   17.358  -5.281  1.00 16.39 ? 106 HIS D N   1 
ATOM   10248 C  CA  . HIS D  1 107 ? 0.713   17.353  -3.796  1.00 16.51 ? 106 HIS D CA  1 
ATOM   10249 C  C   . HIS D  1 107 ? -0.300  18.293  -3.128  1.00 16.52 ? 106 HIS D C   1 
ATOM   10250 O  O   . HIS D  1 107 ? -0.965  17.897  -2.182  1.00 16.45 ? 106 HIS D O   1 
ATOM   10251 C  CB  . HIS D  1 107 ? 2.123   17.653  -3.283  1.00 16.36 ? 106 HIS D CB  1 
ATOM   10252 C  CG  . HIS D  1 107 ? 2.289   17.468  -1.801  1.00 18.08 ? 106 HIS D CG  1 
ATOM   10253 N  ND1 . HIS D  1 107 ? 1.940   16.304  -1.147  1.00 17.97 ? 106 HIS D ND1 1 
ATOM   10254 C  CD2 . HIS D  1 107 ? 2.807   18.284  -0.858  1.00 18.75 ? 106 HIS D CD2 1 
ATOM   10255 C  CE1 . HIS D  1 107 ? 2.207   16.422  0.138   1.00 18.72 ? 106 HIS D CE1 1 
ATOM   10256 N  NE2 . HIS D  1 107 ? 2.751   17.607  0.337   1.00 19.28 ? 106 HIS D NE2 1 
ATOM   10257 N  N   . THR D  1 108 ? -0.404  19.523  -3.595  1.00 16.69 ? 107 THR D N   1 
ATOM   10258 C  CA  . THR D  1 108 ? -1.346  20.467  -2.993  1.00 18.07 ? 107 THR D CA  1 
ATOM   10259 C  C   . THR D  1 108 ? -2.792  19.970  -3.081  1.00 17.92 ? 107 THR D C   1 
ATOM   10260 O  O   . THR D  1 108 ? -3.550  20.036  -2.111  1.00 18.22 ? 107 THR D O   1 
ATOM   10261 C  CB  . THR D  1 108 ? -1.246  21.852  -3.647  1.00 19.19 ? 107 THR D CB  1 
ATOM   10262 O  OG1 . THR D  1 108 ? 0.087   22.344  -3.495  1.00 20.05 ? 107 THR D OG1 1 
ATOM   10263 C  CG2 . THR D  1 108 ? -2.184  22.836  -3.001  1.00 20.72 ? 107 THR D CG2 1 
ATOM   10264 N  N   . MET D  1 109 ? -3.166  19.435  -4.231  1.00 17.71 ? 108 MET D N   1 
ATOM   10265 C  CA  . MET D  1 109 ? -4.516  18.928  -4.411  1.00 18.10 ? 108 MET D CA  1 
ATOM   10266 C  C   . MET D  1 109 ? -4.780  17.724  -3.494  1.00 18.17 ? 108 MET D C   1 
ATOM   10267 O  O   . MET D  1 109 ? -5.860  17.594  -2.939  1.00 18.89 ? 108 MET D O   1 
ATOM   10268 C  CB  . MET D  1 109 ? -4.776  18.551  -5.874  1.00 18.67 ? 108 MET D CB  1 
ATOM   10269 C  CG  . MET D  1 109 ? -6.141  17.912  -6.129  1.00 20.13 ? 108 MET D CG  1 
ATOM   10270 S  SD  . MET D  1 109 ? -6.483  17.549  -7.861  1.00 21.61 ? 108 MET D SD  1 
ATOM   10271 C  CE  . MET D  1 109 ? -6.582  19.201  -8.503  1.00 21.16 ? 108 MET D CE  1 
ATOM   10272 N  N   . VAL D  1 110 ? -3.826  16.811  -3.398  1.00 17.21 ? 109 VAL D N   1 
ATOM   10273 C  CA  . VAL D  1 110 ? -4.019  15.623  -2.575  1.00 17.15 ? 109 VAL D CA  1 
ATOM   10274 C  C   . VAL D  1 110 ? -4.080  16.007  -1.087  1.00 17.90 ? 109 VAL D C   1 
ATOM   10275 O  O   . VAL D  1 110 ? -4.902  15.438  -0.363  1.00 18.53 ? 109 VAL D O   1 
ATOM   10276 C  CB  . VAL D  1 110 ? -2.977  14.527  -2.883  1.00 16.90 ? 109 VAL D CB  1 
ATOM   10277 C  CG1 . VAL D  1 110 ? -3.148  13.333  -1.957  1.00 16.86 ? 109 VAL D CG1 1 
ATOM   10278 C  CG2 . VAL D  1 110 ? -3.119  14.044  -4.322  1.00 16.17 ? 109 VAL D CG2 1 
ATOM   10279 N  N   . GLU D  1 111 ? -3.260  16.969  -0.654  1.00 17.46 ? 110 GLU D N   1 
ATOM   10280 C  CA  . GLU D  1 111 ? -3.378  17.520  0.716   1.00 17.92 ? 110 GLU D CA  1 
ATOM   10281 C  C   . GLU D  1 111 ? -4.818  18.001  0.998   1.00 18.27 ? 110 GLU D C   1 
ATOM   10282 O  O   . GLU D  1 111 ? -5.384  17.675  2.048   1.00 17.56 ? 110 GLU D O   1 
ATOM   10283 C  CB  . GLU D  1 111 ? -2.420  18.669  0.965   1.00 19.03 ? 110 GLU D CB  1 
ATOM   10284 C  CG  . GLU D  1 111 ? -0.972  18.274  1.108   1.00 19.66 ? 110 GLU D CG  1 
ATOM   10285 C  CD  . GLU D  1 111 ? -0.646  17.616  2.412   1.00 20.30 ? 110 GLU D CD  1 
ATOM   10286 O  OE1 . GLU D  1 111 ? -0.533  18.340  3.425   1.00 20.96 ? 110 GLU D OE1 1 
ATOM   10287 O  OE2 . GLU D  1 111 ? -0.542  16.360  2.414   1.00 21.49 ? 110 GLU D OE2 1 
ATOM   10288 N  N   . SER D  1 112 ? -5.409  18.718  0.045   1.00 18.34 ? 111 SER D N   1 
ATOM   10289 C  CA  . SER D  1 112 ? -6.813  19.136  0.160   1.00 19.54 ? 111 SER D CA  1 
ATOM   10290 C  C   . SER D  1 112 ? -7.804  17.967  0.239   1.00 19.52 ? 111 SER D C   1 
ATOM   10291 O  O   . SER D  1 112 ? -8.669  17.943  1.123   1.00 20.12 ? 111 SER D O   1 
ATOM   10292 C  CB  . SER D  1 112 ? -7.183  20.050  -0.997  1.00 20.53 ? 111 SER D CB  1 
ATOM   10293 O  OG  . SER D  1 112 ? -6.549  21.316  -0.857  1.00 23.09 ? 111 SER D OG  1 
ATOM   10294 N  N   . LEU D  1 113 ? -7.670  17.013  -0.680  1.00 18.83 ? 112 LEU D N   1 
ATOM   10295 C  CA  . LEU D  1 113 ? -8.530  15.840  -0.686  1.00 19.61 ? 112 LEU D CA  1 
ATOM   10296 C  C   . LEU D  1 113 ? -8.484  15.089  0.656   1.00 19.40 ? 112 LEU D C   1 
ATOM   10297 O  O   . LEU D  1 113 ? -9.513  14.711  1.209   1.00 19.57 ? 112 LEU D O   1 
ATOM   10298 C  CB  . LEU D  1 113 ? -8.155  14.889  -1.825  1.00 20.16 ? 112 LEU D CB  1 
ATOM   10299 C  CG  . LEU D  1 113 ? -8.533  15.370  -3.227  1.00 21.45 ? 112 LEU D CG  1 
ATOM   10300 C  CD1 . LEU D  1 113 ? -7.777  14.592  -4.288  1.00 22.31 ? 112 LEU D CD1 1 
ATOM   10301 C  CD2 . LEU D  1 113 ? -10.024 15.217  -3.447  1.00 22.08 ? 112 LEU D CD2 1 
ATOM   10302 N  N   . VAL D  1 114 ? -7.279  14.872  1.163   1.00 18.83 ? 113 VAL D N   1 
ATOM   10303 C  CA  . VAL D  1 114 ? -7.112  14.187  2.418   1.00 19.27 ? 113 VAL D CA  1 
ATOM   10304 C  C   . VAL D  1 114 ? -7.752  14.995  3.577   1.00 20.80 ? 113 VAL D C   1 
ATOM   10305 O  O   . VAL D  1 114 ? -8.420  14.422  4.457   1.00 20.49 ? 113 VAL D O   1 
ATOM   10306 C  CB  . VAL D  1 114 ? -5.625  13.855  2.627   1.00 19.17 ? 113 VAL D CB  1 
ATOM   10307 C  CG1 . VAL D  1 114 ? -5.345  13.412  4.058   1.00 20.65 ? 113 VAL D CG1 1 
ATOM   10308 C  CG2 . VAL D  1 114 ? -5.207  12.776  1.634   1.00 18.28 ? 113 VAL D CG2 1 
ATOM   10309 N  N   . GLY D  1 115 ? -7.572  16.319  3.570   1.00 20.97 ? 114 GLY D N   1 
ATOM   10310 C  CA  . GLY D  1 115 ? -8.253  17.164  4.532   1.00 22.83 ? 114 GLY D CA  1 
ATOM   10311 C  C   . GLY D  1 115 ? -9.776  17.054  4.467   1.00 23.56 ? 114 GLY D C   1 
ATOM   10312 O  O   . GLY D  1 115 ? -10.442 17.250  5.476   1.00 25.64 ? 114 GLY D O   1 
ATOM   10313 N  N   . TRP D  1 116 ? -10.314 16.745  3.293   1.00 22.72 ? 115 TRP D N   1 
ATOM   10314 C  CA  . TRP D  1 116 ? -11.743 16.540  3.090   1.00 23.10 ? 115 TRP D CA  1 
ATOM   10315 C  C   . TRP D  1 116 ? -12.206 15.130  3.435   1.00 24.09 ? 115 TRP D C   1 
ATOM   10316 O  O   . TRP D  1 116 ? -13.401 14.850  3.373   1.00 25.62 ? 115 TRP D O   1 
ATOM   10317 C  CB  . TRP D  1 116 ? -12.142 16.835  1.636   1.00 23.13 ? 115 TRP D CB  1 
ATOM   10318 C  CG  . TRP D  1 116 ? -11.786 18.199  1.166   1.00 22.75 ? 115 TRP D CG  1 
ATOM   10319 C  CD1 . TRP D  1 116 ? -11.606 19.325  1.939   1.00 24.02 ? 115 TRP D CD1 1 
ATOM   10320 C  CD2 . TRP D  1 116 ? -11.613 18.608  -0.179  1.00 22.61 ? 115 TRP D CD2 1 
ATOM   10321 N  NE1 . TRP D  1 116 ? -11.301 20.403  1.142   1.00 24.17 ? 115 TRP D NE1 1 
ATOM   10322 C  CE2 . TRP D  1 116 ? -11.271 19.982  -0.165  1.00 23.24 ? 115 TRP D CE2 1 
ATOM   10323 C  CE3 . TRP D  1 116 ? -11.661 17.938  -1.394  1.00 22.55 ? 115 TRP D CE3 1 
ATOM   10324 C  CZ2 . TRP D  1 116 ? -11.015 20.695  -1.324  1.00 23.46 ? 115 TRP D CZ2 1 
ATOM   10325 C  CZ3 . TRP D  1 116 ? -11.398 18.637  -2.546  1.00 22.77 ? 115 TRP D CZ3 1 
ATOM   10326 C  CH2 . TRP D  1 116 ? -11.079 20.018  -2.499  1.00 23.58 ? 115 TRP D CH2 1 
ATOM   10327 N  N   . GLY D  1 117 ? -11.287 14.245  3.805   1.00 22.99 ? 116 GLY D N   1 
ATOM   10328 C  CA  . GLY D  1 117 ? -11.653 12.906  4.256   1.00 23.39 ? 116 GLY D CA  1 
ATOM   10329 C  C   . GLY D  1 117 ? -11.232 11.756  3.380   1.00 22.07 ? 116 GLY D C   1 
ATOM   10330 O  O   . GLY D  1 117 ? -11.572 10.612  3.697   1.00 22.09 ? 116 GLY D O   1 
ATOM   10331 N  N   . TYR D  1 118 ? -10.486 12.025  2.296   1.00 20.72 ? 117 TYR D N   1 
ATOM   10332 C  CA  . TYR D  1 118 ? -9.984  10.985  1.418   1.00 19.54 ? 117 TYR D CA  1 
ATOM   10333 C  C   . TYR D  1 118 ? -8.785  10.313  2.046   1.00 20.17 ? 117 TYR D C   1 
ATOM   10334 O  O   . TYR D  1 118 ? -8.114  10.912  2.894   1.00 20.22 ? 117 TYR D O   1 
ATOM   10335 C  CB  . TYR D  1 118 ? -9.599  11.546  0.014   1.00 18.80 ? 117 TYR D CB  1 
ATOM   10336 C  CG  . TYR D  1 118 ? -10.809 11.766  -0.839  1.00 19.03 ? 117 TYR D CG  1 
ATOM   10337 C  CD1 . TYR D  1 118 ? -11.561 12.929  -0.723  1.00 20.04 ? 117 TYR D CD1 1 
ATOM   10338 C  CD2 . TYR D  1 118 ? -11.245 10.777  -1.728  1.00 19.07 ? 117 TYR D CD2 1 
ATOM   10339 C  CE1 . TYR D  1 118 ? -12.704 13.130  -1.474  1.00 19.96 ? 117 TYR D CE1 1 
ATOM   10340 C  CE2 . TYR D  1 118 ? -12.390 10.961  -2.495  1.00 19.13 ? 117 TYR D CE2 1 
ATOM   10341 C  CZ  . TYR D  1 118 ? -13.128 12.130  -2.348  1.00 19.84 ? 117 TYR D CZ  1 
ATOM   10342 O  OH  . TYR D  1 118 ? -14.278 12.320  -3.064  1.00 20.57 ? 117 TYR D OH  1 
ATOM   10343 N  N   . THR D  1 119 ? -8.481  9.106   1.556   1.00 19.53 ? 118 THR D N   1 
ATOM   10344 C  CA  . THR D  1 119 ? -7.369  8.293   2.039   1.00 19.66 ? 118 THR D CA  1 
ATOM   10345 C  C   . THR D  1 119 ? -6.469  7.904   0.863   1.00 18.46 ? 118 THR D C   1 
ATOM   10346 O  O   . THR D  1 119 ? -6.923  7.226   -0.061  1.00 17.60 ? 118 THR D O   1 
ATOM   10347 C  CB  . THR D  1 119 ? -7.897  7.016   2.750   1.00 20.79 ? 118 THR D CB  1 
ATOM   10348 O  OG1 . THR D  1 119 ? -8.708  7.392   3.860   1.00 22.55 ? 118 THR D OG1 1 
ATOM   10349 C  CG2 . THR D  1 119 ? -6.770  6.140   3.255   1.00 20.95 ? 118 THR D CG2 1 
ATOM   10350 N  N   . ARG D  1 120 ? -5.188  8.323   0.904   1.00 17.82 ? 119 ARG D N   1 
ATOM   10351 C  CA  . ARG D  1 120 ? -4.221  8.033   -0.158  1.00 17.26 ? 119 ARG D CA  1 
ATOM   10352 C  C   . ARG D  1 120 ? -4.106  6.551   -0.440  1.00 17.64 ? 119 ARG D C   1 
ATOM   10353 O  O   . ARG D  1 120 ? -3.964  5.751   0.489   1.00 17.70 ? 119 ARG D O   1 
ATOM   10354 C  CB  . ARG D  1 120 ? -2.813  8.522   0.196   1.00 17.37 ? 119 ARG D CB  1 
ATOM   10355 C  CG  . ARG D  1 120 ? -2.626  10.022  0.108   1.00 17.11 ? 119 ARG D CG  1 
ATOM   10356 C  CD  . ARG D  1 120 ? -1.259  10.390  0.656   1.00 16.86 ? 119 ARG D CD  1 
ATOM   10357 N  NE  . ARG D  1 120 ? -0.937  11.781  0.374   1.00 16.97 ? 119 ARG D NE  1 
ATOM   10358 C  CZ  . ARG D  1 120 ? -1.143  12.815  1.183   1.00 17.58 ? 119 ARG D CZ  1 
ATOM   10359 N  NH1 . ARG D  1 120 ? -1.642  12.652  2.404   1.00 18.18 ? 119 ARG D NH1 1 
ATOM   10360 N  NH2 . ARG D  1 120 ? -0.828  14.012  0.771   1.00 18.09 ? 119 ARG D NH2 1 
ATOM   10361 N  N   . GLY D  1 121 ? -4.252  6.165   -1.705  1.00 17.30 ? 120 GLY D N   1 
ATOM   10362 C  CA  . GLY D  1 121 ? -4.106  4.734   -2.116  1.00 17.85 ? 120 GLY D CA  1 
ATOM   10363 C  C   . GLY D  1 121 ? -5.359  3.911   -1.958  1.00 18.36 ? 120 GLY D C   1 
ATOM   10364 O  O   . GLY D  1 121 ? -5.398  2.720   -2.316  1.00 19.76 ? 120 GLY D O   1 
ATOM   10365 N  N   A GLU D  1 122 ? -6.392  4.506   -1.361  0.50 17.54 ? 121 GLU D N   1 
ATOM   10366 N  N   B GLU D  1 122 ? -6.393  4.538   -1.435  0.50 18.76 ? 121 GLU D N   1 
ATOM   10367 C  CA  A GLU D  1 122 ? -7.667  3.831   -1.155  0.50 17.01 ? 121 GLU D CA  1 
ATOM   10368 C  CA  B GLU D  1 122 ? -7.613  3.832   -1.206  0.50 18.90 ? 121 GLU D CA  1 
ATOM   10369 C  C   A GLU D  1 122 ? -8.728  4.506   -2.032  0.50 16.64 ? 121 GLU D C   1 
ATOM   10370 C  C   B GLU D  1 122 ? -8.700  4.537   -2.045  0.50 17.59 ? 121 GLU D C   1 
ATOM   10371 O  O   A GLU D  1 122 ? -8.894  4.118   -3.187  0.50 16.31 ? 121 GLU D O   1 
ATOM   10372 O  O   B GLU D  1 122 ? -8.802  4.234   -3.236  0.50 16.90 ? 121 GLU D O   1 
ATOM   10373 C  CB  A GLU D  1 122 ? -8.049  3.801   0.340   0.50 17.17 ? 121 GLU D CB  1 
ATOM   10374 C  CB  B GLU D  1 122 ? -7.787  3.641   0.318   0.50 20.68 ? 121 GLU D CB  1 
ATOM   10375 C  CG  A GLU D  1 122 ? -7.227  2.857   1.194   0.50 16.83 ? 121 GLU D CG  1 
ATOM   10376 C  CG  B GLU D  1 122 ? -6.490  2.990   0.888   0.50 21.88 ? 121 GLU D CG  1 
ATOM   10377 C  CD  A GLU D  1 122 ? -7.734  1.425   1.175   0.50 16.71 ? 121 GLU D CD  1 
ATOM   10378 C  CD  B GLU D  1 122 ? -6.548  2.472   2.323   0.50 24.25 ? 121 GLU D CD  1 
ATOM   10379 O  OE1 A GLU D  1 122 ? -8.849  1.169   0.611   0.50 16.08 ? 121 GLU D OE1 1 
ATOM   10380 O  OE1 B GLU D  1 122 ? -7.612  2.680   2.954   0.50 26.83 ? 121 GLU D OE1 1 
ATOM   10381 O  OE2 A GLU D  1 122 ? -7.006  0.547   1.714   0.50 16.33 ? 121 GLU D OE2 1 
ATOM   10382 O  OE2 B GLU D  1 122 ? -5.521  1.855   2.817   0.50 23.35 ? 121 GLU D OE2 1 
ATOM   10383 N  N   . ASP D  1 123 ? -9.431  5.511   -1.515  1.00 17.04 ? 122 ASP D N   1 
ATOM   10384 C  CA  . ASP D  1 123 ? -10.500 6.137   -2.289  1.00 17.05 ? 122 ASP D CA  1 
ATOM   10385 C  C   . ASP D  1 123 ? -10.013 7.330   -3.151  1.00 16.06 ? 122 ASP D C   1 
ATOM   10386 O  O   . ASP D  1 123 ? -10.802 7.936   -3.843  1.00 14.97 ? 122 ASP D O   1 
ATOM   10387 C  CB  . ASP D  1 123 ? -11.726 6.459   -1.432  1.00 18.04 ? 122 ASP D CB  1 
ATOM   10388 C  CG  . ASP D  1 123 ? -11.425 7.331   -0.262  1.00 19.23 ? 122 ASP D CG  1 
ATOM   10389 O  OD1 . ASP D  1 123 ? -10.249 7.707   -0.025  1.00 20.47 ? 122 ASP D OD1 1 
ATOM   10390 O  OD2 . ASP D  1 123 ? -12.381 7.665   0.448   1.00 19.91 ? 122 ASP D OD2 1 
ATOM   10391 N  N   . VAL D  1 124 ? -8.728  7.677   -3.033  1.00 15.28 ? 123 VAL D N   1 
ATOM   10392 C  CA  . VAL D  1 124 ? -8.065  8.506   -4.018  1.00 15.82 ? 123 VAL D CA  1 
ATOM   10393 C  C   . VAL D  1 124 ? -6.852  7.732   -4.497  1.00 14.97 ? 123 VAL D C   1 
ATOM   10394 O  O   . VAL D  1 124 ? -6.006  7.340   -3.682  1.00 15.41 ? 123 VAL D O   1 
ATOM   10395 C  CB  . VAL D  1 124 ? -7.721  9.938   -3.548  1.00 16.21 ? 123 VAL D CB  1 
ATOM   10396 C  CG1 . VAL D  1 124 ? -6.832  9.968   -2.303  1.00 16.33 ? 123 VAL D CG1 1 
ATOM   10397 C  CG2 . VAL D  1 124 ? -7.084  10.696  -4.693  1.00 16.07 ? 123 VAL D CG2 1 
ATOM   10398 N  N   . ARG D  1 125 ? -6.789  7.498   -5.812  1.00 14.59 ? 124 ARG D N   1 
ATOM   10399 C  CA  . ARG D  1 125 ? -5.662  6.757   -6.434  1.00 14.71 ? 124 ARG D CA  1 
ATOM   10400 C  C   . ARG D  1 125 ? -5.153  7.462   -7.665  1.00 14.93 ? 124 ARG D C   1 
ATOM   10401 O  O   . ARG D  1 125 ? -5.942  8.107   -8.391  1.00 15.29 ? 124 ARG D O   1 
ATOM   10402 C  CB  . ARG D  1 125 ? -6.100  5.359   -6.826  1.00 14.39 ? 124 ARG D CB  1 
ATOM   10403 C  CG  . ARG D  1 125 ? -6.606  4.546   -5.638  1.00 15.25 ? 124 ARG D CG  1 
ATOM   10404 C  CD  . ARG D  1 125 ? -6.843  3.092   -6.017  1.00 15.38 ? 124 ARG D CD  1 
ATOM   10405 N  NE  . ARG D  1 125 ? -7.603  2.384   -5.011  1.00 15.84 ? 124 ARG D NE  1 
ATOM   10406 C  CZ  . ARG D  1 125 ? -7.836  1.077   -5.033  1.00 17.03 ? 124 ARG D CZ  1 
ATOM   10407 N  NH1 . ARG D  1 125 ? -7.360  0.305   -6.022  1.00 17.59 ? 124 ARG D NH1 1 
ATOM   10408 N  NH2 . ARG D  1 125 ? -8.558  0.528   -4.076  1.00 17.58 ? 124 ARG D NH2 1 
ATOM   10409 N  N   . GLY D  1 126 ? -3.854  7.347   -7.905  1.00 14.49 ? 125 GLY D N   1 
ATOM   10410 C  CA  . GLY D  1 126 ? -3.283  7.855   -9.151  1.00 14.56 ? 125 GLY D CA  1 
ATOM   10411 C  C   . GLY D  1 126 ? -3.239  6.832   -10.258 1.00 14.68 ? 125 GLY D C   1 
ATOM   10412 O  O   . GLY D  1 126 ? -3.133  5.611   -10.010 1.00 14.62 ? 125 GLY D O   1 
ATOM   10413 N  N   . ALA D  1 127 ? -3.316  7.326   -11.484 1.00 14.33 ? 126 ALA D N   1 
ATOM   10414 C  CA  . ALA D  1 127 ? -3.162  6.507   -12.687 1.00 13.95 ? 126 ALA D CA  1 
ATOM   10415 C  C   . ALA D  1 127 ? -1.979  7.042   -13.533 1.00 13.90 ? 126 ALA D C   1 
ATOM   10416 O  O   . ALA D  1 127 ? -2.168  7.556   -14.637 1.00 14.36 ? 126 ALA D O   1 
ATOM   10417 C  CB  . ALA D  1 127 ? -4.469  6.489   -13.465 1.00 14.40 ? 126 ALA D CB  1 
ATOM   10418 N  N   . PRO D  1 128 ? -0.750  6.931   -12.996 1.00 13.36 ? 127 PRO D N   1 
ATOM   10419 C  CA  . PRO D  1 128 ? 0.447   7.323   -13.753 1.00 12.95 ? 127 PRO D CA  1 
ATOM   10420 C  C   . PRO D  1 128 ? 0.712   6.416   -14.963 1.00 13.33 ? 127 PRO D C   1 
ATOM   10421 O  O   . PRO D  1 128 ? 0.281   5.241   -14.987 1.00 13.11 ? 127 PRO D O   1 
ATOM   10422 C  CB  . PRO D  1 128 ? 1.571   7.181   -12.726 1.00 13.18 ? 127 PRO D CB  1 
ATOM   10423 C  CG  . PRO D  1 128 ? 1.096   6.073   -11.838 1.00 13.27 ? 127 PRO D CG  1 
ATOM   10424 C  CD  . PRO D  1 128 ? -0.390  6.348   -11.692 1.00 13.16 ? 127 PRO D CD  1 
ATOM   10425 N  N   . TYR D  1 129 ? 1.414   6.960   -15.964 1.00 13.29 ? 128 TYR D N   1 
ATOM   10426 C  CA  . TYR D  1 129 ? 1.679   6.225   -17.182 1.00 12.96 ? 128 TYR D CA  1 
ATOM   10427 C  C   . TYR D  1 129 ? 2.984   6.699   -17.789 1.00 13.43 ? 128 TYR D C   1 
ATOM   10428 O  O   . TYR D  1 129 ? 3.564   7.700   -17.357 1.00 12.95 ? 128 TYR D O   1 
ATOM   10429 C  CB  . TYR D  1 129 ? 0.518   6.356   -18.183 1.00 13.27 ? 128 TYR D CB  1 
ATOM   10430 C  CG  . TYR D  1 129 ? 0.172   7.790   -18.537 1.00 12.76 ? 128 TYR D CG  1 
ATOM   10431 C  CD1 . TYR D  1 129 ? -0.658  8.552   -17.712 1.00 13.26 ? 128 TYR D CD1 1 
ATOM   10432 C  CD2 . TYR D  1 129 ? 0.670   8.382   -19.682 1.00 13.44 ? 128 TYR D CD2 1 
ATOM   10433 C  CE1 . TYR D  1 129 ? -0.966  9.868   -18.034 1.00 13.49 ? 128 TYR D CE1 1 
ATOM   10434 C  CE2 . TYR D  1 129 ? 0.350   9.694   -20.029 1.00 13.12 ? 128 TYR D CE2 1 
ATOM   10435 C  CZ  . TYR D  1 129 ? -0.441  10.435  -19.199 1.00 13.52 ? 128 TYR D CZ  1 
ATOM   10436 O  OH  . TYR D  1 129 ? -0.755  11.753  -19.519 1.00 13.63 ? 128 TYR D OH  1 
ATOM   10437 N  N   . ASP D  1 130 ? 3.457   5.978   -18.800 1.00 13.52 ? 129 ASP D N   1 
ATOM   10438 C  CA  . ASP D  1 130 ? 4.665   6.398   -19.524 1.00 14.85 ? 129 ASP D CA  1 
ATOM   10439 C  C   . ASP D  1 130 ? 4.241   7.484   -20.515 1.00 14.39 ? 129 ASP D C   1 
ATOM   10440 O  O   . ASP D  1 130 ? 3.798   7.200   -21.628 1.00 13.92 ? 129 ASP D O   1 
ATOM   10441 C  CB  . ASP D  1 130 ? 5.308   5.216   -20.257 1.00 16.27 ? 129 ASP D CB  1 
ATOM   10442 C  CG  . ASP D  1 130 ? 6.651   5.585   -20.880 1.00 18.24 ? 129 ASP D CG  1 
ATOM   10443 O  OD1 . ASP D  1 130 ? 6.971   6.786   -21.013 1.00 17.06 ? 129 ASP D OD1 1 
ATOM   10444 O  OD2 . ASP D  1 130 ? 7.416   4.644   -21.172 1.00 19.78 ? 129 ASP D OD2 1 
ATOM   10445 N  N   . TRP D  1 131 ? 4.370   8.717   -20.066 1.00 14.01 ? 130 TRP D N   1 
ATOM   10446 C  CA  . TRP D  1 131 ? 3.878   9.878   -20.789 1.00 14.28 ? 130 TRP D CA  1 
ATOM   10447 C  C   . TRP D  1 131 ? 4.745   10.240  -22.026 1.00 14.67 ? 130 TRP D C   1 
ATOM   10448 O  O   . TRP D  1 131 ? 4.384   11.146  -22.779 1.00 14.72 ? 130 TRP D O   1 
ATOM   10449 C  CB  . TRP D  1 131 ? 3.765   11.075  -19.851 1.00 14.39 ? 130 TRP D CB  1 
ATOM   10450 C  CG  . TRP D  1 131 ? 4.863   11.138  -18.812 1.00 14.66 ? 130 TRP D CG  1 
ATOM   10451 C  CD1 . TRP D  1 131 ? 4.749   10.816  -17.487 1.00 14.94 ? 130 TRP D CD1 1 
ATOM   10452 C  CD2 . TRP D  1 131 ? 6.247   11.532  -19.008 1.00 15.13 ? 130 TRP D CD2 1 
ATOM   10453 N  NE1 . TRP D  1 131 ? 5.941   10.984  -16.857 1.00 15.62 ? 130 TRP D NE1 1 
ATOM   10454 C  CE2 . TRP D  1 131 ? 6.887   11.408  -17.758 1.00 15.51 ? 130 TRP D CE2 1 
ATOM   10455 C  CE3 . TRP D  1 131 ? 6.982   11.978  -20.110 1.00 15.21 ? 130 TRP D CE3 1 
ATOM   10456 C  CZ2 . TRP D  1 131 ? 8.230   11.713  -17.565 1.00 16.14 ? 130 TRP D CZ2 1 
ATOM   10457 C  CZ3 . TRP D  1 131 ? 8.336   12.290  -19.926 1.00 16.40 ? 130 TRP D CZ3 1 
ATOM   10458 C  CH2 . TRP D  1 131 ? 8.948   12.152  -18.646 1.00 16.26 ? 130 TRP D CH2 1 
ATOM   10459 N  N   . ARG D  1 132 ? 5.823   9.496   -22.275 1.00 14.56 ? 131 ARG D N   1 
ATOM   10460 C  CA  . ARG D  1 132 ? 6.577   9.651   -23.514 1.00 15.52 ? 131 ARG D CA  1 
ATOM   10461 C  C   . ARG D  1 132 ? 5.816   9.068   -24.702 1.00 15.62 ? 131 ARG D C   1 
ATOM   10462 O  O   . ARG D  1 132 ? 6.093   9.414   -25.860 1.00 16.34 ? 131 ARG D O   1 
ATOM   10463 C  CB  . ARG D  1 132 ? 7.956   8.978   -23.390 1.00 15.84 ? 131 ARG D CB  1 
ATOM   10464 C  CG  . ARG D  1 132 ? 8.821   9.568   -22.280 1.00 16.72 ? 131 ARG D CG  1 
ATOM   10465 C  CD  . ARG D  1 132 ? 10.056  8.727   -22.002 1.00 16.94 ? 131 ARG D CD  1 
ATOM   10466 N  NE  . ARG D  1 132 ? 9.700   7.351   -21.688 1.00 16.98 ? 131 ARG D NE  1 
ATOM   10467 C  CZ  . ARG D  1 132 ? 10.533  6.319   -21.733 1.00 18.69 ? 131 ARG D CZ  1 
ATOM   10468 N  NH1 . ARG D  1 132 ? 11.822  6.489   -22.058 1.00 20.09 ? 131 ARG D NH1 1 
ATOM   10469 N  NH2 . ARG D  1 132 ? 10.082  5.098   -21.491 1.00 19.01 ? 131 ARG D NH2 1 
ATOM   10470 N  N   . ARG D  1 133 ? 4.912   8.124   -24.421 1.00 15.79 ? 132 ARG D N   1 
ATOM   10471 C  CA  . ARG D  1 133 ? 4.158   7.437   -25.432 1.00 16.40 ? 132 ARG D CA  1 
ATOM   10472 C  C   . ARG D  1 133 ? 2.739   7.986   -25.541 1.00 15.86 ? 132 ARG D C   1 
ATOM   10473 O  O   . ARG D  1 133 ? 2.227   8.616   -24.608 1.00 15.37 ? 132 ARG D O   1 
ATOM   10474 C  CB  . ARG D  1 133 ? 4.116   5.949   -25.095 1.00 19.21 ? 132 ARG D CB  1 
ATOM   10475 C  CG  . ARG D  1 133 ? 5.453   5.295   -25.395 1.00 23.15 ? 132 ARG D CG  1 
ATOM   10476 C  CD  . ARG D  1 133 ? 5.605   3.927   -24.784 1.00 27.58 ? 132 ARG D CD  1 
ATOM   10477 N  NE  . ARG D  1 133 ? 6.593   3.155   -25.543 1.00 31.81 ? 132 ARG D NE  1 
ATOM   10478 C  CZ  . ARG D  1 133 ? 7.063   1.964   -25.188 1.00 34.53 ? 132 ARG D CZ  1 
ATOM   10479 N  NH1 . ARG D  1 133 ? 6.666   1.382   -24.064 1.00 36.01 ? 132 ARG D NH1 1 
ATOM   10480 N  NH2 . ARG D  1 133 ? 7.927   1.353   -25.971 1.00 36.03 ? 132 ARG D NH2 1 
ATOM   10481 N  N   . ALA D  1 134 ? 2.119   7.715   -26.686 1.00 15.40 ? 133 ALA D N   1 
ATOM   10482 C  CA  . ALA D  1 134 ? 0.713   8.049   -26.912 1.00 15.25 ? 133 ALA D CA  1 
ATOM   10483 C  C   . ALA D  1 134 ? -0.128  6.816   -26.610 1.00 14.81 ? 133 ALA D C   1 
ATOM   10484 O  O   . ALA D  1 134 ? 0.420   5.747   -26.343 1.00 14.52 ? 133 ALA D O   1 
ATOM   10485 C  CB  . ALA D  1 134 ? 0.518   8.494   -28.349 1.00 15.45 ? 133 ALA D CB  1 
ATOM   10486 N  N   . PRO D  1 135 ? -1.466  6.952   -26.626 1.00 15.29 ? 134 PRO D N   1 
ATOM   10487 C  CA  . PRO D  1 135 ? -2.288  5.834   -26.168 1.00 15.50 ? 134 PRO D CA  1 
ATOM   10488 C  C   . PRO D  1 135 ? -2.158  4.520   -26.927 1.00 16.50 ? 134 PRO D C   1 
ATOM   10489 O  O   . PRO D  1 135 ? -2.384  3.457   -26.326 1.00 16.66 ? 134 PRO D O   1 
ATOM   10490 C  CB  . PRO D  1 135 ? -3.714  6.396   -26.269 1.00 15.68 ? 134 PRO D CB  1 
ATOM   10491 C  CG  . PRO D  1 135 ? -3.512  7.841   -25.978 1.00 15.33 ? 134 PRO D CG  1 
ATOM   10492 C  CD  . PRO D  1 135 ? -2.243  8.209   -26.673 1.00 15.30 ? 134 PRO D CD  1 
ATOM   10493 N  N   . ASN D  1 136 ? -1.733  4.573   -28.191 1.00 16.86 ? 135 ASN D N   1 
ATOM   10494 C  CA  . ASN D  1 136 ? -1.537  3.378   -28.972 1.00 18.29 ? 135 ASN D CA  1 
ATOM   10495 C  C   . ASN D  1 136 ? -0.475  2.440   -28.416 1.00 19.34 ? 135 ASN D C   1 
ATOM   10496 O  O   . ASN D  1 136 ? -0.498  1.244   -28.727 1.00 19.99 ? 135 ASN D O   1 
ATOM   10497 C  CB  . ASN D  1 136 ? -1.189  3.711   -30.434 1.00 18.30 ? 135 ASN D CB  1 
ATOM   10498 C  CG  . ASN D  1 136 ? 0.111   4.488   -30.573 1.00 18.90 ? 135 ASN D CG  1 
ATOM   10499 O  OD1 . ASN D  1 136 ? 0.411   5.360   -29.773 1.00 19.05 ? 135 ASN D OD1 1 
ATOM   10500 N  ND2 . ASN D  1 136 ? 0.912   4.136   -31.563 1.00 21.73 ? 135 ASN D ND2 1 
ATOM   10501 N  N   . GLU D  1 137 ? 0.446   2.958   -27.601 1.00 19.01 ? 136 GLU D N   1 
ATOM   10502 C  CA  . GLU D  1 137 ? 1.451   2.128   -26.962 1.00 19.81 ? 136 GLU D CA  1 
ATOM   10503 C  C   . GLU D  1 137 ? 1.301   2.053   -25.442 1.00 19.81 ? 136 GLU D C   1 
ATOM   10504 O  O   . GLU D  1 137 ? 2.257   1.775   -24.723 1.00 21.78 ? 136 GLU D O   1 
ATOM   10505 C  CB  . GLU D  1 137 ? 2.844   2.623   -27.353 1.00 21.44 ? 136 GLU D CB  1 
ATOM   10506 C  CG  . GLU D  1 137 ? 3.086   2.461   -28.843 1.00 24.48 ? 136 GLU D CG  1 
ATOM   10507 C  CD  . GLU D  1 137 ? 4.516   2.772   -29.256 1.00 28.83 ? 136 GLU D CD  1 
ATOM   10508 O  OE1 . GLU D  1 137 ? 4.980   3.930   -29.176 1.00 27.10 ? 136 GLU D OE1 1 
ATOM   10509 O  OE2 . GLU D  1 137 ? 5.181   1.811   -29.664 1.00 36.55 ? 136 GLU D OE2 1 
ATOM   10510 N  N   . ASN D  1 138 ? 0.083   2.249   -24.967 1.00 19.05 ? 137 ASN D N   1 
ATOM   10511 C  CA  . ASN D  1 138 ? -0.222  2.148   -23.558 1.00 18.29 ? 137 ASN D CA  1 
ATOM   10512 C  C   . ASN D  1 138 ? -1.493  1.342   -23.330 1.00 18.45 ? 137 ASN D C   1 
ATOM   10513 O  O   . ASN D  1 138 ? -2.235  1.581   -22.375 1.00 18.39 ? 137 ASN D O   1 
ATOM   10514 C  CB  . ASN D  1 138 ? -0.276  3.558   -22.930 1.00 18.13 ? 137 ASN D CB  1 
ATOM   10515 C  CG  . ASN D  1 138 ? 1.041   3.928   -22.242 1.00 19.89 ? 137 ASN D CG  1 
ATOM   10516 O  OD1 . ASN D  1 138 ? 1.621   3.099   -21.564 1.00 22.05 ? 137 ASN D OD1 1 
ATOM   10517 N  ND2 . ASN D  1 138 ? 1.497   5.172   -22.394 1.00 17.87 ? 137 ASN D ND2 1 
ATOM   10518 N  N   . GLY D  1 139 ? -1.680  0.300   -24.152 1.00 19.05 ? 138 GLY D N   1 
ATOM   10519 C  CA  . GLY D  1 139 ? -2.816  -0.619  -24.010 1.00 19.19 ? 138 GLY D CA  1 
ATOM   10520 C  C   . GLY D  1 139 ? -2.946  -1.206  -22.605 1.00 18.96 ? 138 GLY D C   1 
ATOM   10521 O  O   . GLY D  1 139 ? -4.034  -1.169  -22.003 1.00 18.02 ? 138 GLY D O   1 
ATOM   10522 N  N   . PRO D  1 140 ? -1.853  -1.757  -22.062 1.00 19.32 ? 139 PRO D N   1 
ATOM   10523 C  CA  . PRO D  1 140 ? -1.926  -2.340  -20.705 1.00 19.28 ? 139 PRO D CA  1 
ATOM   10524 C  C   . PRO D  1 140 ? -2.352  -1.338  -19.601 1.00 18.70 ? 139 PRO D C   1 
ATOM   10525 O  O   . PRO D  1 140 ? -3.136  -1.691  -18.705 1.00 18.78 ? 139 PRO D O   1 
ATOM   10526 C  CB  . PRO D  1 140 ? -0.504  -2.874  -20.478 1.00 20.22 ? 139 PRO D CB  1 
ATOM   10527 C  CG  . PRO D  1 140 ? -0.047  -3.208  -21.878 1.00 20.37 ? 139 PRO D CG  1 
ATOM   10528 C  CD  . PRO D  1 140 ? -0.580  -2.095  -22.733 1.00 20.17 ? 139 PRO D CD  1 
ATOM   10529 N  N   . TYR D  1 141 ? -1.910  -0.087  -19.717 1.00 16.66 ? 140 TYR D N   1 
ATOM   10530 C  CA  . TYR D  1 141 ? -2.370  0.978   -18.825 1.00 16.10 ? 140 TYR D CA  1 
ATOM   10531 C  C   . TYR D  1 141 ? -3.906  1.116   -18.826 1.00 15.56 ? 140 TYR D C   1 
ATOM   10532 O  O   . TYR D  1 141 ? -4.517  1.202   -17.757 1.00 15.36 ? 140 TYR D O   1 
ATOM   10533 C  CB  . TYR D  1 141 ? -1.745  2.306   -19.230 1.00 15.49 ? 140 TYR D CB  1 
ATOM   10534 C  CG  . TYR D  1 141 ? -2.348  3.519   -18.571 1.00 14.61 ? 140 TYR D CG  1 
ATOM   10535 C  CD1 . TYR D  1 141 ? -1.966  3.898   -17.288 1.00 14.51 ? 140 TYR D CD1 1 
ATOM   10536 C  CD2 . TYR D  1 141 ? -3.267  4.318   -19.242 1.00 14.78 ? 140 TYR D CD2 1 
ATOM   10537 C  CE1 . TYR D  1 141 ? -2.501  5.025   -16.689 1.00 14.25 ? 140 TYR D CE1 1 
ATOM   10538 C  CE2 . TYR D  1 141 ? -3.788  5.449   -18.639 1.00 15.10 ? 140 TYR D CE2 1 
ATOM   10539 C  CZ  . TYR D  1 141 ? -3.410  5.788   -17.364 1.00 14.43 ? 140 TYR D CZ  1 
ATOM   10540 O  OH  . TYR D  1 141 ? -3.926  6.927   -16.766 1.00 15.52 ? 140 TYR D OH  1 
ATOM   10541 N  N   . PHE D  1 142 ? -4.526  1.129   -20.002 1.00 15.81 ? 141 PHE D N   1 
ATOM   10542 C  CA  . PHE D  1 142 ? -5.981  1.295   -20.084 1.00 16.39 ? 141 PHE D CA  1 
ATOM   10543 C  C   . PHE D  1 142 ? -6.740  0.098   -19.509 1.00 17.48 ? 141 PHE D C   1 
ATOM   10544 O  O   . PHE D  1 142 ? -7.810  0.267   -18.891 1.00 17.38 ? 141 PHE D O   1 
ATOM   10545 C  CB  . PHE D  1 142 ? -6.436  1.603   -21.506 1.00 16.78 ? 141 PHE D CB  1 
ATOM   10546 C  CG  . PHE D  1 142 ? -5.895  2.917   -22.009 1.00 16.83 ? 141 PHE D CG  1 
ATOM   10547 C  CD1 . PHE D  1 142 ? -6.309  4.097   -21.428 1.00 16.53 ? 141 PHE D CD1 1 
ATOM   10548 C  CD2 . PHE D  1 142 ? -4.955  2.964   -23.023 1.00 16.77 ? 141 PHE D CD2 1 
ATOM   10549 C  CE1 . PHE D  1 142 ? -5.813  5.303   -21.850 1.00 16.44 ? 141 PHE D CE1 1 
ATOM   10550 C  CE2 . PHE D  1 142 ? -4.437  4.171   -23.446 1.00 16.27 ? 141 PHE D CE2 1 
ATOM   10551 C  CZ  . PHE D  1 142 ? -4.871  5.342   -22.860 1.00 16.38 ? 141 PHE D CZ  1 
ATOM   10552 N  N   . LEU D  1 143 ? -6.205  -1.111  -19.711 1.00 18.34 ? 142 LEU D N   1 
ATOM   10553 C  CA  . LEU D  1 143 ? -6.781  -2.291  -19.064 1.00 20.01 ? 142 LEU D CA  1 
ATOM   10554 C  C   . LEU D  1 143 ? -6.699  -2.176  -17.537 1.00 18.05 ? 142 LEU D C   1 
ATOM   10555 O  O   . LEU D  1 143 ? -7.692  -2.424  -16.839 1.00 18.27 ? 142 LEU D O   1 
ATOM   10556 C  CB  . LEU D  1 143 ? -6.116  -3.593  -19.551 1.00 22.08 ? 142 LEU D CB  1 
ATOM   10557 C  CG  . LEU D  1 143 ? -6.217  -3.882  -21.053 1.00 26.52 ? 142 LEU D CG  1 
ATOM   10558 C  CD1 . LEU D  1 143 ? -5.251  -5.001  -21.476 1.00 29.03 ? 142 LEU D CD1 1 
ATOM   10559 C  CD2 . LEU D  1 143 ? -7.637  -4.244  -21.400 1.00 28.69 ? 142 LEU D CD2 1 
ATOM   10560 N  N   . ALA D  1 144 ? -5.544  -1.773  -17.017 1.00 16.76 ? 143 ALA D N   1 
ATOM   10561 C  CA  . ALA D  1 144 ? -5.369  -1.583  -15.575 1.00 16.59 ? 143 ALA D CA  1 
ATOM   10562 C  C   . ALA D  1 144 ? -6.278  -0.482  -15.029 1.00 15.74 ? 143 ALA D C   1 
ATOM   10563 O  O   . ALA D  1 144 ? -6.776  -0.577  -13.914 1.00 15.76 ? 143 ALA D O   1 
ATOM   10564 C  CB  . ALA D  1 144 ? -3.908  -1.249  -15.246 1.00 16.99 ? 143 ALA D CB  1 
ATOM   10565 N  N   . LEU D  1 145 ? -6.430  0.593   -15.783 1.00 15.30 ? 144 LEU D N   1 
ATOM   10566 C  CA  . LEU D  1 145 ? -7.291  1.704   -15.368 1.00 15.35 ? 144 LEU D CA  1 
ATOM   10567 C  C   . LEU D  1 145 ? -8.759  1.239   -15.256 1.00 15.88 ? 144 LEU D C   1 
ATOM   10568 O  O   . LEU D  1 145 ? -9.447  1.537   -14.269 1.00 15.59 ? 144 LEU D O   1 
ATOM   10569 C  CB  . LEU D  1 145 ? -7.165  2.862   -16.343 1.00 15.47 ? 144 LEU D CB  1 
ATOM   10570 C  CG  . LEU D  1 145 ? -8.045  4.102   -16.165 1.00 16.04 ? 144 LEU D CG  1 
ATOM   10571 C  CD1 . LEU D  1 145 ? -7.795  4.732   -14.805 1.00 16.38 ? 144 LEU D CD1 1 
ATOM   10572 C  CD2 . LEU D  1 145 ? -7.794  5.137   -17.255 1.00 16.28 ? 144 LEU D CD2 1 
ATOM   10573 N  N   . ARG D  1 146 ? -9.222  0.508   -16.260 1.00 16.58 ? 145 ARG D N   1 
ATOM   10574 C  CA  . ARG D  1 146 ? -10.578 -0.047  -16.242 1.00 17.85 ? 145 ARG D CA  1 
ATOM   10575 C  C   . ARG D  1 146 ? -10.769 -0.952  -15.008 1.00 17.94 ? 145 ARG D C   1 
ATOM   10576 O  O   . ARG D  1 146 ? -11.759 -0.822  -14.282 1.00 17.86 ? 145 ARG D O   1 
ATOM   10577 C  CB  . ARG D  1 146 ? -10.890 -0.826  -17.513 1.00 19.08 ? 145 ARG D CB  1 
ATOM   10578 C  CG  . ARG D  1 146 ? -12.274 -1.462  -17.529 1.00 21.82 ? 145 ARG D CG  1 
ATOM   10579 C  CD  . ARG D  1 146 ? -12.522 -2.206  -18.845 1.00 25.41 ? 145 ARG D CD  1 
ATOM   10580 N  NE  . ARG D  1 146 ? -13.647 -3.139  -18.749 1.00 28.41 ? 145 ARG D NE  1 
ATOM   10581 C  CZ  . ARG D  1 146 ? -14.823 -3.041  -19.377 1.00 31.31 ? 145 ARG D CZ  1 
ATOM   10582 N  NH1 . ARG D  1 146 ? -15.096 -2.046  -20.221 1.00 32.51 ? 145 ARG D NH1 1 
ATOM   10583 N  NH2 . ARG D  1 146 ? -15.753 -3.961  -19.145 1.00 32.90 ? 145 ARG D NH2 1 
ATOM   10584 N  N   A GLU D  1 147 ? -9.818  -1.849  -14.772 0.50 17.73 ? 146 GLU D N   1 
ATOM   10585 N  N   B GLU D  1 147 ? -9.818  -1.843  -14.767 0.50 18.34 ? 146 GLU D N   1 
ATOM   10586 C  CA  A GLU D  1 147 ? -9.881  -2.736  -13.626 0.50 19.09 ? 146 GLU D CA  1 
ATOM   10587 C  CA  B GLU D  1 147 ? -9.882  -2.734  -13.622 0.50 20.03 ? 146 GLU D CA  1 
ATOM   10588 C  C   A GLU D  1 147 ? -9.849  -1.977  -12.296 0.50 18.29 ? 146 GLU D C   1 
ATOM   10589 C  C   B GLU D  1 147 ? -9.843  -1.981  -12.287 0.50 18.82 ? 146 GLU D C   1 
ATOM   10590 O  O   A GLU D  1 147 ? -10.586 -2.322  -11.389 0.50 17.55 ? 146 GLU D O   1 
ATOM   10591 O  O   B GLU D  1 147 ? -10.575 -2.327  -11.372 0.50 17.99 ? 146 GLU D O   1 
ATOM   10592 C  CB  A GLU D  1 147 ? -8.765  -3.784  -13.651 0.50 20.10 ? 146 GLU D CB  1 
ATOM   10593 C  CB  B GLU D  1 147 ? -8.774  -3.789  -13.684 0.50 21.98 ? 146 GLU D CB  1 
ATOM   10594 C  CG  A GLU D  1 147 ? -8.788  -4.694  -12.435 0.50 21.94 ? 146 GLU D CG  1 
ATOM   10595 C  CG  B GLU D  1 147 ? -8.980  -4.759  -14.839 0.50 25.21 ? 146 GLU D CG  1 
ATOM   10596 C  CD  A GLU D  1 147 ? -10.107 -5.449  -12.278 0.50 24.36 ? 146 GLU D CD  1 
ATOM   10597 C  CD  B GLU D  1 147 ? -7.833  -5.737  -15.045 0.50 29.17 ? 146 GLU D CD  1 
ATOM   10598 O  OE1 A GLU D  1 147 ? -10.661 -5.926  -13.304 0.50 26.33 ? 146 GLU D OE1 1 
ATOM   10599 O  OE1 B GLU D  1 147 ? -6.680  -5.436  -14.667 0.50 33.16 ? 146 GLU D OE1 1 
ATOM   10600 O  OE2 A GLU D  1 147 ? -10.606 -5.549  -11.127 0.50 25.45 ? 146 GLU D OE2 1 
ATOM   10601 O  OE2 B GLU D  1 147 ? -8.082  -6.810  -15.629 0.50 32.13 ? 146 GLU D OE2 1 
ATOM   10602 N  N   . MET D  1 148 ? -9.010  -0.949  -12.191 1.00 17.44 ? 147 MET D N   1 
ATOM   10603 C  CA  . MET D  1 148 ? -8.907  -0.172  -10.969 1.00 17.48 ? 147 MET D CA  1 
ATOM   10604 C  C   . MET D  1 148 ? -10.232 0.560   -10.674 1.00 16.98 ? 147 MET D C   1 
ATOM   10605 O  O   . MET D  1 148 ? -10.684 0.610   -9.533  1.00 15.82 ? 147 MET D O   1 
ATOM   10606 C  CB  . MET D  1 148 ? -7.759  0.838   -11.043 1.00 17.84 ? 147 MET D CB  1 
ATOM   10607 C  CG  . MET D  1 148 ? -7.602  1.669   -9.783  1.00 19.60 ? 147 MET D CG  1 
ATOM   10608 S  SD  . MET D  1 148 ? -6.052  2.584   -9.725  1.00 21.55 ? 147 MET D SD  1 
ATOM   10609 C  CE  . MET D  1 148 ? -6.302  3.855   -10.915 1.00 19.83 ? 147 MET D CE  1 
ATOM   10610 N  N   . ILE D  1 149 ? -10.826 1.136   -11.711 1.00 16.63 ? 148 ILE D N   1 
ATOM   10611 C  CA  . ILE D  1 149 ? -12.107 1.817   -11.581 1.00 16.32 ? 148 ILE D CA  1 
ATOM   10612 C  C   . ILE D  1 149 ? -13.195 0.853   -11.078 1.00 17.03 ? 148 ILE D C   1 
ATOM   10613 O  O   . ILE D  1 149 ? -13.943 1.190   -10.172 1.00 17.04 ? 148 ILE D O   1 
ATOM   10614 C  CB  . ILE D  1 149 ? -12.511 2.508   -12.897 1.00 16.81 ? 148 ILE D CB  1 
ATOM   10615 C  CG1 . ILE D  1 149 ? -11.641 3.746   -13.093 1.00 16.88 ? 148 ILE D CG1 1 
ATOM   10616 C  CG2 . ILE D  1 149 ? -13.993 2.916   -12.872 1.00 17.51 ? 148 ILE D CG2 1 
ATOM   10617 C  CD1 . ILE D  1 149 ? -11.698 4.309   -14.495 1.00 16.99 ? 148 ILE D CD1 1 
ATOM   10618 N  N   . GLU D  1 150 ? -13.268 -0.335  -11.677 1.00 17.48 ? 149 GLU D N   1 
ATOM   10619 C  CA  A GLU D  1 150 ? -14.230 -1.337  -11.244 0.50 18.45 ? 149 GLU D CA  1 
ATOM   10620 C  CA  B GLU D  1 150 ? -14.201 -1.384  -11.260 0.50 19.04 ? 149 GLU D CA  1 
ATOM   10621 C  C   . GLU D  1 150 ? -13.987 -1.773  -9.784  1.00 18.60 ? 149 GLU D C   1 
ATOM   10622 O  O   . GLU D  1 150 ? -14.952 -1.903  -9.009  1.00 18.56 ? 149 GLU D O   1 
ATOM   10623 C  CB  A GLU D  1 150 ? -14.196 -2.536  -12.182 0.50 18.97 ? 149 GLU D CB  1 
ATOM   10624 C  CB  B GLU D  1 150 ? -14.048 -2.608  -12.179 0.50 20.34 ? 149 GLU D CB  1 
ATOM   10625 C  CG  A GLU D  1 150 ? -14.666 -2.182  -13.582 0.50 19.25 ? 149 GLU D CG  1 
ATOM   10626 C  CG  B GLU D  1 150 ? -14.560 -2.335  -13.591 0.50 21.53 ? 149 GLU D CG  1 
ATOM   10627 C  CD  A GLU D  1 150 ? -14.804 -3.391  -14.491 0.50 20.14 ? 149 GLU D CD  1 
ATOM   10628 C  CD  B GLU D  1 150 ? -14.184 -3.385  -14.634 0.50 23.40 ? 149 GLU D CD  1 
ATOM   10629 O  OE1 A GLU D  1 150 ? -14.531 -4.519  -14.013 0.50 19.40 ? 149 GLU D OE1 1 
ATOM   10630 O  OE1 B GLU D  1 150 ? -14.871 -3.410  -15.688 0.50 24.87 ? 149 GLU D OE1 1 
ATOM   10631 O  OE2 A GLU D  1 150 ? -15.146 -3.199  -15.693 0.50 20.60 ? 149 GLU D OE2 1 
ATOM   10632 O  OE2 B GLU D  1 150 ? -13.232 -4.181  -14.427 0.50 23.77 ? 149 GLU D OE2 1 
ATOM   10633 N  N   A GLU D  1 151 ? -12.718 -1.986  -9.408  0.50 17.63 ? 150 GLU D N   1 
ATOM   10634 N  N   B GLU D  1 151 ? -12.727 -1.950  -9.402  0.50 18.14 ? 150 GLU D N   1 
ATOM   10635 C  CA  A GLU D  1 151 ? -12.353 -2.333  -8.015  0.50 18.24 ? 150 GLU D CA  1 
ATOM   10636 C  CA  B GLU D  1 151 ? -12.384 -2.307  -8.031  0.50 18.97 ? 150 GLU D CA  1 
ATOM   10637 C  C   A GLU D  1 151 ? -12.770 -1.231  -7.038  0.50 17.75 ? 150 GLU D C   1 
ATOM   10638 C  C   B GLU D  1 151 ? -12.799 -1.220  -7.051  0.50 18.17 ? 150 GLU D C   1 
ATOM   10639 O  O   A GLU D  1 151 ? -13.310 -1.530  -5.967  0.50 17.42 ? 150 GLU D O   1 
ATOM   10640 O  O   B GLU D  1 151 ? -13.362 -1.508  -5.998  0.50 17.77 ? 150 GLU D O   1 
ATOM   10641 C  CB  A GLU D  1 151 ? -10.840 -2.668  -7.860  0.50 18.54 ? 150 GLU D CB  1 
ATOM   10642 C  CB  B GLU D  1 151 ? -10.886 -2.604  -7.898  0.50 19.96 ? 150 GLU D CB  1 
ATOM   10643 C  CG  A GLU D  1 151 ? -10.278 -2.497  -6.428  0.50 19.12 ? 150 GLU D CG  1 
ATOM   10644 C  CG  B GLU D  1 151 ? -10.474 -3.855  -8.632  0.50 20.95 ? 150 GLU D CG  1 
ATOM   10645 C  CD  A GLU D  1 151 ? -8.817  -2.966  -6.229  0.50 19.09 ? 150 GLU D CD  1 
ATOM   10646 C  CD  B GLU D  1 151 ? -8.976  -4.085  -8.719  0.50 23.34 ? 150 GLU D CD  1 
ATOM   10647 O  OE1 A GLU D  1 151 ? -8.433  -3.976  -6.891  0.50 20.93 ? 150 GLU D OE1 1 
ATOM   10648 O  OE1 B GLU D  1 151 ? -8.173  -3.186  -8.373  0.50 24.21 ? 150 GLU D OE1 1 
ATOM   10649 O  OE2 A GLU D  1 151 ? -8.068  -2.372  -5.391  0.50 16.43 ? 150 GLU D OE2 1 
ATOM   10650 O  OE2 B GLU D  1 151 ? -8.600  -5.189  -9.174  0.50 27.06 ? 150 GLU D OE2 1 
ATOM   10651 N  N   . MET D  1 152 ? -12.550 0.037   -7.410  1.00 16.96 ? 151 MET D N   1 
ATOM   10652 C  CA  . MET D  1 152 ? -12.897 1.142   -6.541  1.00 16.72 ? 151 MET D CA  1 
ATOM   10653 C  C   . MET D  1 152 ? -14.418 1.227   -6.375  1.00 17.38 ? 151 MET D C   1 
ATOM   10654 O  O   . MET D  1 152 ? -14.921 1.512   -5.282  1.00 16.84 ? 151 MET D O   1 
ATOM   10655 C  CB  . MET D  1 152 ? -12.331 2.446   -7.061  1.00 16.68 ? 151 MET D CB  1 
ATOM   10656 C  CG  . MET D  1 152 ? -10.810 2.480   -6.977  1.00 16.47 ? 151 MET D CG  1 
ATOM   10657 S  SD  . MET D  1 152 ? -10.100 3.928   -7.778  1.00 17.61 ? 151 MET D SD  1 
ATOM   10658 C  CE  . MET D  1 152 ? -10.317 5.161   -6.494  1.00 17.66 ? 151 MET D CE  1 
ATOM   10659 N  N   . TYR D  1 153 ? -15.141 0.997   -7.464  1.00 17.43 ? 152 TYR D N   1 
ATOM   10660 C  CA  . TYR D  1 153 ? -16.615 1.017   -7.412  1.00 18.69 ? 152 TYR D CA  1 
ATOM   10661 C  C   . TYR D  1 153 ? -17.117 -0.056  -6.433  1.00 19.74 ? 152 TYR D C   1 
ATOM   10662 O  O   . TYR D  1 153 ? -18.016 0.193   -5.624  1.00 20.29 ? 152 TYR D O   1 
ATOM   10663 C  CB  . TYR D  1 153 ? -17.164 0.797   -8.830  1.00 19.16 ? 152 TYR D CB  1 
ATOM   10664 C  CG  . TYR D  1 153 ? -18.653 0.523   -8.904  1.00 20.47 ? 152 TYR D CG  1 
ATOM   10665 C  CD1 . TYR D  1 153 ? -19.152 -0.767  -8.741  1.00 21.70 ? 152 TYR D CD1 1 
ATOM   10666 C  CD2 . TYR D  1 153 ? -19.558 1.551   -9.138  1.00 22.09 ? 152 TYR D CD2 1 
ATOM   10667 C  CE1 . TYR D  1 153 ? -20.510 -1.018  -8.800  1.00 23.28 ? 152 TYR D CE1 1 
ATOM   10668 C  CE2 . TYR D  1 153 ? -20.928 1.306   -9.234  1.00 23.08 ? 152 TYR D CE2 1 
ATOM   10669 C  CZ  . TYR D  1 153 ? -21.390 0.029   -9.052  1.00 24.19 ? 152 TYR D CZ  1 
ATOM   10670 O  OH  . TYR D  1 153 ? -22.746 -0.192  -9.121  1.00 26.21 ? 152 TYR D OH  1 
ATOM   10671 N  N   . GLN D  1 154 ? -16.540 -1.246  -6.512  1.00 21.01 ? 153 GLN D N   1 
ATOM   10672 C  CA  . GLN D  1 154 ? -16.950 -2.364  -5.664  1.00 23.81 ? 153 GLN D CA  1 
ATOM   10673 C  C   . GLN D  1 154 ? -16.561 -2.163  -4.201  1.00 21.92 ? 153 GLN D C   1 
ATOM   10674 O  O   . GLN D  1 154 ? -17.364 -2.436  -3.304  1.00 20.83 ? 153 GLN D O   1 
ATOM   10675 C  CB  . GLN D  1 154 ? -16.354 -3.682  -6.150  1.00 28.40 ? 153 GLN D CB  1 
ATOM   10676 C  CG  . GLN D  1 154 ? -16.833 -4.135  -7.525  1.00 36.73 ? 153 GLN D CG  1 
ATOM   10677 C  CD  . GLN D  1 154 ? -16.164 -5.421  -8.020  1.00 46.21 ? 153 GLN D CD  1 
ATOM   10678 O  OE1 . GLN D  1 154 ? -14.922 -5.526  -8.137  1.00 53.40 ? 153 GLN D OE1 1 
ATOM   10679 N  NE2 . GLN D  1 154 ? -16.991 -6.403  -8.352  1.00 51.00 ? 153 GLN D NE2 1 
ATOM   10680 N  N   . LEU D  1 155 ? -15.341 -1.687  -3.961  1.00 18.95 ? 154 LEU D N   1 
ATOM   10681 C  CA  . LEU D  1 155 ? -14.866 -1.470  -2.600  1.00 18.66 ? 154 LEU D CA  1 
ATOM   10682 C  C   . LEU D  1 155 ? -15.619 -0.342  -1.912  1.00 18.56 ? 154 LEU D C   1 
ATOM   10683 O  O   . LEU D  1 155 ? -16.045 -0.487  -0.768  1.00 19.04 ? 154 LEU D O   1 
ATOM   10684 C  CB  . LEU D  1 155 ? -13.358 -1.142  -2.579  1.00 17.83 ? 154 LEU D CB  1 
ATOM   10685 C  CG  . LEU D  1 155 ? -12.420 -2.327  -2.863  1.00 17.79 ? 154 LEU D CG  1 
ATOM   10686 C  CD1 . LEU D  1 155 ? -11.013 -1.809  -3.068  1.00 17.77 ? 154 LEU D CD1 1 
ATOM   10687 C  CD2 . LEU D  1 155 ? -12.463 -3.325  -1.717  1.00 18.61 ? 154 LEU D CD2 1 
ATOM   10688 N  N   . TYR D  1 156 ? -15.760 0.782   -2.595  1.00 18.08 ? 155 TYR D N   1 
ATOM   10689 C  CA  . TYR D  1 156 ? -16.225 2.014   -1.954  1.00 18.99 ? 155 TYR D CA  1 
ATOM   10690 C  C   . TYR D  1 156 ? -17.693 2.314   -2.216  1.00 20.56 ? 155 TYR D C   1 
ATOM   10691 O  O   . TYR D  1 156 ? -18.236 3.256   -1.648  1.00 22.21 ? 155 TYR D O   1 
ATOM   10692 C  CB  . TYR D  1 156 ? -15.332 3.213   -2.310  1.00 18.02 ? 155 TYR D CB  1 
ATOM   10693 C  CG  . TYR D  1 156 ? -13.861 2.854   -2.143  1.00 17.23 ? 155 TYR D CG  1 
ATOM   10694 C  CD1 . TYR D  1 156 ? -13.360 2.453   -0.908  1.00 17.59 ? 155 TYR D CD1 1 
ATOM   10695 C  CD2 . TYR D  1 156 ? -12.990 2.886   -3.223  1.00 16.58 ? 155 TYR D CD2 1 
ATOM   10696 C  CE1 . TYR D  1 156 ? -12.025 2.079   -0.756  1.00 17.11 ? 155 TYR D CE1 1 
ATOM   10697 C  CE2 . TYR D  1 156 ? -11.661 2.525   -3.077  1.00 16.18 ? 155 TYR D CE2 1 
ATOM   10698 C  CZ  . TYR D  1 156 ? -11.190 2.104   -1.835  1.00 16.75 ? 155 TYR D CZ  1 
ATOM   10699 O  OH  . TYR D  1 156 ? -9.875  1.732   -1.692  1.00 16.40 ? 155 TYR D OH  1 
ATOM   10700 N  N   . GLY D  1 157 ? -18.353 1.494   -3.024  1.00 21.50 ? 156 GLY D N   1 
ATOM   10701 C  CA  . GLY D  1 157 ? -19.821 1.521   -3.120  1.00 22.55 ? 156 GLY D CA  1 
ATOM   10702 C  C   . GLY D  1 157 ? -20.433 2.571   -4.046  1.00 23.08 ? 156 GLY D C   1 
ATOM   10703 O  O   . GLY D  1 157 ? -21.612 2.892   -3.911  1.00 24.00 ? 156 GLY D O   1 
ATOM   10704 N  N   . GLY D  1 158 ? -19.674 3.094   -5.001  1.00 21.80 ? 157 GLY D N   1 
ATOM   10705 C  CA  . GLY D  1 158 ? -20.252 4.004   -5.999  1.00 22.28 ? 157 GLY D CA  1 
ATOM   10706 C  C   . GLY D  1 158 ? -19.306 4.387   -7.119  1.00 21.32 ? 157 GLY D C   1 
ATOM   10707 O  O   . GLY D  1 158 ? -18.113 4.045   -7.059  1.00 21.58 ? 157 GLY D O   1 
ATOM   10708 N  N   . PRO D  1 159 ? -19.827 5.095   -8.143  1.00 21.03 ? 158 PRO D N   1 
ATOM   10709 C  CA  . PRO D  1 159 ? -19.028 5.464   -9.296  1.00 20.40 ? 158 PRO D CA  1 
ATOM   10710 C  C   . PRO D  1 159 ? -17.956 6.515   -9.005  1.00 19.74 ? 158 PRO D C   1 
ATOM   10711 O  O   . PRO D  1 159 ? -18.051 7.258   -8.040  1.00 18.81 ? 158 PRO D O   1 
ATOM   10712 C  CB  . PRO D  1 159 ? -20.050 5.991   -10.309 1.00 21.10 ? 158 PRO D CB  1 
ATOM   10713 C  CG  . PRO D  1 159 ? -21.249 6.362   -9.531  1.00 21.89 ? 158 PRO D CG  1 
ATOM   10714 C  CD  . PRO D  1 159 ? -21.258 5.436   -8.332  1.00 22.68 ? 158 PRO D CD  1 
ATOM   10715 N  N   . VAL D  1 160 ? -16.951 6.529   -9.864  1.00 19.92 ? 159 VAL D N   1 
ATOM   10716 C  CA  . VAL D  1 160 ? -15.694 7.242   -9.647  1.00 20.44 ? 159 VAL D CA  1 
ATOM   10717 C  C   . VAL D  1 160 ? -15.664 8.600   -10.376 1.00 19.31 ? 159 VAL D C   1 
ATOM   10718 O  O   . VAL D  1 160 ? -16.281 8.775   -11.441 1.00 19.68 ? 159 VAL D O   1 
ATOM   10719 C  CB  . VAL D  1 160 ? -14.548 6.348   -10.189 1.00 21.26 ? 159 VAL D CB  1 
ATOM   10720 C  CG1 . VAL D  1 160 ? -13.222 7.054   -10.170 1.00 24.11 ? 159 VAL D CG1 1 
ATOM   10721 C  CG2 . VAL D  1 160 ? -14.498 5.016   -9.452  1.00 22.63 ? 159 VAL D CG2 1 
ATOM   10722 N  N   . VAL D  1 161 ? -14.974 9.576   -9.790  1.00 18.21 ? 160 VAL D N   1 
ATOM   10723 C  CA  . VAL D  1 161 ? -14.744 10.877  -10.451 1.00 17.70 ? 160 VAL D CA  1 
ATOM   10724 C  C   . VAL D  1 161 ? -13.320 10.855  -10.970 1.00 17.45 ? 160 VAL D C   1 
ATOM   10725 O  O   . VAL D  1 161 ? -12.388 10.585  -10.191 1.00 16.69 ? 160 VAL D O   1 
ATOM   10726 C  CB  . VAL D  1 161 ? -14.959 12.070  -9.494  1.00 17.59 ? 160 VAL D CB  1 
ATOM   10727 C  CG1 . VAL D  1 161 ? -14.542 13.383  -10.142 1.00 17.73 ? 160 VAL D CG1 1 
ATOM   10728 C  CG2 . VAL D  1 161 ? -16.417 12.143  -9.057  1.00 18.37 ? 160 VAL D CG2 1 
ATOM   10729 N  N   . LEU D  1 162 ? -13.167 11.087  -12.273 1.00 16.75 ? 161 LEU D N   1 
ATOM   10730 C  CA  . LEU D  1 162 ? -11.855 11.185  -12.911 1.00 17.27 ? 161 LEU D CA  1 
ATOM   10731 C  C   . LEU D  1 162 ? -11.425 12.633  -12.918 1.00 16.78 ? 161 LEU D C   1 
ATOM   10732 O  O   . LEU D  1 162 ? -12.210 13.496  -13.268 1.00 17.09 ? 161 LEU D O   1 
ATOM   10733 C  CB  . LEU D  1 162 ? -11.945 10.693  -14.343 1.00 18.80 ? 161 LEU D CB  1 
ATOM   10734 C  CG  . LEU D  1 162 ? -12.408 9.244   -14.531 1.00 20.95 ? 161 LEU D CG  1 
ATOM   10735 C  CD1 . LEU D  1 162 ? -12.684 8.878   -15.967 1.00 20.83 ? 161 LEU D CD1 1 
ATOM   10736 C  CD2 . LEU D  1 162 ? -11.373 8.315   -13.956 1.00 23.22 ? 161 LEU D CD2 1 
ATOM   10737 N  N   . VAL D  1 163 ? -10.210 12.914  -12.452 1.00 16.34 ? 162 VAL D N   1 
ATOM   10738 C  CA  . VAL D  1 163 ? -9.711  14.280  -12.417 1.00 16.06 ? 162 VAL D CA  1 
ATOM   10739 C  C   . VAL D  1 163 ? -8.392  14.251  -13.196 1.00 15.95 ? 162 VAL D C   1 
ATOM   10740 O  O   . VAL D  1 163 ? -7.464  13.545  -12.788 1.00 16.01 ? 162 VAL D O   1 
ATOM   10741 C  CB  . VAL D  1 163 ? -9.442  14.784  -10.984 1.00 17.02 ? 162 VAL D CB  1 
ATOM   10742 C  CG1 . VAL D  1 163 ? -8.912  16.229  -11.014 1.00 17.02 ? 162 VAL D CG1 1 
ATOM   10743 C  CG2 . VAL D  1 163 ? -10.705 14.729  -10.130 1.00 17.78 ? 162 VAL D CG2 1 
ATOM   10744 N  N   . ALA D  1 164 ? -8.326  14.958  -14.328 1.00 15.57 ? 163 ALA D N   1 
ATOM   10745 C  CA  . ALA D  1 164 ? -7.175  14.879  -15.216 1.00 14.85 ? 163 ALA D CA  1 
ATOM   10746 C  C   . ALA D  1 164 ? -6.618  16.255  -15.510 1.00 15.41 ? 163 ALA D C   1 
ATOM   10747 O  O   . ALA D  1 164 ? -7.357  17.237  -15.565 1.00 14.70 ? 163 ALA D O   1 
ATOM   10748 C  CB  . ALA D  1 164 ? -7.531  14.176  -16.529 1.00 15.21 ? 163 ALA D CB  1 
ATOM   10749 N  N   . HIS D  1 165 ? -5.301  16.313  -15.665 1.00 15.13 ? 164 HIS D N   1 
ATOM   10750 C  CA  . HIS D  1 165 ? -4.622  17.565  -15.969 1.00 15.58 ? 164 HIS D CA  1 
ATOM   10751 C  C   . HIS D  1 165 ? -3.913  17.442  -17.293 1.00 15.39 ? 164 HIS D C   1 
ATOM   10752 O  O   . HIS D  1 165 ? -3.257  16.424  -17.601 1.00 14.24 ? 164 HIS D O   1 
ATOM   10753 C  CB  . HIS D  1 165 ? -3.611  17.902  -14.874 1.00 16.46 ? 164 HIS D CB  1 
ATOM   10754 C  CG  . HIS D  1 165 ? -2.872  19.176  -15.116 1.00 16.54 ? 164 HIS D CG  1 
ATOM   10755 N  ND1 . HIS D  1 165 ? -1.503  19.216  -15.286 1.00 17.79 ? 164 HIS D ND1 1 
ATOM   10756 C  CD2 . HIS D  1 165 ? -3.307  20.445  -15.243 1.00 16.92 ? 164 HIS D CD2 1 
ATOM   10757 C  CE1 . HIS D  1 165 ? -1.127  20.462  -15.496 1.00 17.75 ? 164 HIS D CE1 1 
ATOM   10758 N  NE2 . HIS D  1 165 ? -2.203  21.227  -15.472 1.00 16.68 ? 164 HIS D NE2 1 
ATOM   10759 N  N   . SER D  1 166 ? -4.038  18.492  -18.087 1.00 16.21 ? 165 SER D N   1 
ATOM   10760 C  CA  . SER D  1 166 ? -3.269  18.652  -19.321 1.00 16.42 ? 165 SER D CA  1 
ATOM   10761 C  C   . SER D  1 166 ? -3.447  17.453  -20.252 1.00 15.70 ? 165 SE