data_4KTH
# 
_entry.id   4KTH 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   4KTH         
RCSB  RCSB079774   
WWPDB D_1000079774 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4KW1 . unspecified 
PDB 4KWM . unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4KTH 
_pdbx_database_status.recvd_initial_deposition_date   2013-05-20 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Shore, D.A.'  1 
'Yang, H.'     2 
'Carney, P.J.' 3 
'Chang, J.C.'  4 
'Stevens, J.'  5 
# 
_citation.id                        primary 
_citation.title                     'Structural and Antigenic Variation among Diverse Clade 2 H5N1 Viruses.' 
_citation.journal_abbrev            'Plos One' 
_citation.journal_volume            8 
_citation.page_first                e75209 
_citation.page_last                 e75209 
_citation.year                      2013 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           1932-6203 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   24086467 
_citation.pdbx_database_id_DOI      10.1371/journal.pone.0075209 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Shore, D.A.'      1  
primary 'Yang, H.'         2  
primary 'Balish, A.L.'     3  
primary 'Shepard, S.S.'    4  
primary 'Carney, P.J.'     5  
primary 'Chang, J.C.'      6  
primary 'Davis, C.T.'      7  
primary 'Donis, R.O.'      8  
primary 'Villanueva, J.M.' 9  
primary 'Klimov, A.I.'     10 
primary 'Stevens, J.'      11 
# 
_cell.entry_id           4KTH 
_cell.length_a           174.121 
_cell.length_b           101.585 
_cell.length_c           124.928 
_cell.angle_alpha        90.00 
_cell.angle_beta         121.66 
_cell.angle_gamma        90.00 
_cell.Z_PDB              12 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         4KTH 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Hemagglutinin          37268.066 3  ? ? 'HA1 residues 17-342'  ? 
2 polymer     man Hemagglutinin          20881.105 3  ? ? 'HA2 residues 346-523' ? 
3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208   14 ? ? ?                      ? 
4 water       nat water                  18.015    72 ? ? ?                      ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;ADPGDHICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCDLNGVKPLILKDCSVAGWLLGNPMCDEFINVPEW
SYIVEKANPANDLCYPGNFNDYEELKHLLSRINHFEKIQIIPKNSWSDHEASLGVSAACPYQGKSSFFRNVVWLIKKDNA
YPTIKKGYNNTNQEDLLVLWGIHHPNDEAEQTRLYQNPTTYISIGTSTLNQRLVPKIATRSKINGQSGRIDFFWTILKPN
DAIHFESNGNFIAPEYAYKIVKKGDSTIMKSEVEYGNCNTRCQTPIGAINSSMPFHNIHPLTIGECPKYVKSNKLVLATG
LRNSPQRETR
;
;ADPGDHICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCDLNGVKPLILKDCSVAGWLLGNPMCDEFINVPEW
SYIVEKANPANDLCYPGNFNDYEELKHLLSRINHFEKIQIIPKNSWSDHEASLGVSAACPYQGKSSFFRNVVWLIKKDNA
YPTIKKGYNNTNQEDLLVLWGIHHPNDEAEQTRLYQNPTTYISIGTSTLNQRLVPKIATRSKINGQSGRIDFFWTILKPN
DAIHFESNGNFIAPEYAYKIVKKGDSTIMKSEVEYGNCNTRCQTPIGAINSSMPFHNIHPLTIGECPKYVKSNKLVLATG
LRNSPQRETR
;
A,E,C ? 
2 'polypeptide(L)' no no 
;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL
NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVRNLYDKVRLQLKDNAKELGNGCFEFYHKCDNECMESVRNGTYDYP
QYSEEARLKREEISSGRLVPR
;
;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL
NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVRNLYDKVRLQLKDNAKELGNGCFEFYHKCDNECMESVRNGTYDYP
QYSEEARLKREEISSGRLVPR
;
B,F,D ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   ASP n 
1 3   PRO n 
1 4   GLY n 
1 5   ASP n 
1 6   HIS n 
1 7   ILE n 
1 8   CYS n 
1 9   ILE n 
1 10  GLY n 
1 11  TYR n 
1 12  HIS n 
1 13  ALA n 
1 14  ASN n 
1 15  ASN n 
1 16  SER n 
1 17  THR n 
1 18  GLU n 
1 19  GLN n 
1 20  VAL n 
1 21  ASP n 
1 22  THR n 
1 23  ILE n 
1 24  MET n 
1 25  GLU n 
1 26  LYS n 
1 27  ASN n 
1 28  VAL n 
1 29  THR n 
1 30  VAL n 
1 31  THR n 
1 32  HIS n 
1 33  ALA n 
1 34  GLN n 
1 35  ASP n 
1 36  ILE n 
1 37  LEU n 
1 38  GLU n 
1 39  LYS n 
1 40  THR n 
1 41  HIS n 
1 42  ASN n 
1 43  GLY n 
1 44  LYS n 
1 45  LEU n 
1 46  CYS n 
1 47  ASP n 
1 48  LEU n 
1 49  ASN n 
1 50  GLY n 
1 51  VAL n 
1 52  LYS n 
1 53  PRO n 
1 54  LEU n 
1 55  ILE n 
1 56  LEU n 
1 57  LYS n 
1 58  ASP n 
1 59  CYS n 
1 60  SER n 
1 61  VAL n 
1 62  ALA n 
1 63  GLY n 
1 64  TRP n 
1 65  LEU n 
1 66  LEU n 
1 67  GLY n 
1 68  ASN n 
1 69  PRO n 
1 70  MET n 
1 71  CYS n 
1 72  ASP n 
1 73  GLU n 
1 74  PHE n 
1 75  ILE n 
1 76  ASN n 
1 77  VAL n 
1 78  PRO n 
1 79  GLU n 
1 80  TRP n 
1 81  SER n 
1 82  TYR n 
1 83  ILE n 
1 84  VAL n 
1 85  GLU n 
1 86  LYS n 
1 87  ALA n 
1 88  ASN n 
1 89  PRO n 
1 90  ALA n 
1 91  ASN n 
1 92  ASP n 
1 93  LEU n 
1 94  CYS n 
1 95  TYR n 
1 96  PRO n 
1 97  GLY n 
1 98  ASN n 
1 99  PHE n 
1 100 ASN n 
1 101 ASP n 
1 102 TYR n 
1 103 GLU n 
1 104 GLU n 
1 105 LEU n 
1 106 LYS n 
1 107 HIS n 
1 108 LEU n 
1 109 LEU n 
1 110 SER n 
1 111 ARG n 
1 112 ILE n 
1 113 ASN n 
1 114 HIS n 
1 115 PHE n 
1 116 GLU n 
1 117 LYS n 
1 118 ILE n 
1 119 GLN n 
1 120 ILE n 
1 121 ILE n 
1 122 PRO n 
1 123 LYS n 
1 124 ASN n 
1 125 SER n 
1 126 TRP n 
1 127 SER n 
1 128 ASP n 
1 129 HIS n 
1 130 GLU n 
1 131 ALA n 
1 132 SER n 
1 133 LEU n 
1 134 GLY n 
1 135 VAL n 
1 136 SER n 
1 137 ALA n 
1 138 ALA n 
1 139 CYS n 
1 140 PRO n 
1 141 TYR n 
1 142 GLN n 
1 143 GLY n 
1 144 LYS n 
1 145 SER n 
1 146 SER n 
1 147 PHE n 
1 148 PHE n 
1 149 ARG n 
1 150 ASN n 
1 151 VAL n 
1 152 VAL n 
1 153 TRP n 
1 154 LEU n 
1 155 ILE n 
1 156 LYS n 
1 157 LYS n 
1 158 ASP n 
1 159 ASN n 
1 160 ALA n 
1 161 TYR n 
1 162 PRO n 
1 163 THR n 
1 164 ILE n 
1 165 LYS n 
1 166 LYS n 
1 167 GLY n 
1 168 TYR n 
1 169 ASN n 
1 170 ASN n 
1 171 THR n 
1 172 ASN n 
1 173 GLN n 
1 174 GLU n 
1 175 ASP n 
1 176 LEU n 
1 177 LEU n 
1 178 VAL n 
1 179 LEU n 
1 180 TRP n 
1 181 GLY n 
1 182 ILE n 
1 183 HIS n 
1 184 HIS n 
1 185 PRO n 
1 186 ASN n 
1 187 ASP n 
1 188 GLU n 
1 189 ALA n 
1 190 GLU n 
1 191 GLN n 
1 192 THR n 
1 193 ARG n 
1 194 LEU n 
1 195 TYR n 
1 196 GLN n 
1 197 ASN n 
1 198 PRO n 
1 199 THR n 
1 200 THR n 
1 201 TYR n 
1 202 ILE n 
1 203 SER n 
1 204 ILE n 
1 205 GLY n 
1 206 THR n 
1 207 SER n 
1 208 THR n 
1 209 LEU n 
1 210 ASN n 
1 211 GLN n 
1 212 ARG n 
1 213 LEU n 
1 214 VAL n 
1 215 PRO n 
1 216 LYS n 
1 217 ILE n 
1 218 ALA n 
1 219 THR n 
1 220 ARG n 
1 221 SER n 
1 222 LYS n 
1 223 ILE n 
1 224 ASN n 
1 225 GLY n 
1 226 GLN n 
1 227 SER n 
1 228 GLY n 
1 229 ARG n 
1 230 ILE n 
1 231 ASP n 
1 232 PHE n 
1 233 PHE n 
1 234 TRP n 
1 235 THR n 
1 236 ILE n 
1 237 LEU n 
1 238 LYS n 
1 239 PRO n 
1 240 ASN n 
1 241 ASP n 
1 242 ALA n 
1 243 ILE n 
1 244 HIS n 
1 245 PHE n 
1 246 GLU n 
1 247 SER n 
1 248 ASN n 
1 249 GLY n 
1 250 ASN n 
1 251 PHE n 
1 252 ILE n 
1 253 ALA n 
1 254 PRO n 
1 255 GLU n 
1 256 TYR n 
1 257 ALA n 
1 258 TYR n 
1 259 LYS n 
1 260 ILE n 
1 261 VAL n 
1 262 LYS n 
1 263 LYS n 
1 264 GLY n 
1 265 ASP n 
1 266 SER n 
1 267 THR n 
1 268 ILE n 
1 269 MET n 
1 270 LYS n 
1 271 SER n 
1 272 GLU n 
1 273 VAL n 
1 274 GLU n 
1 275 TYR n 
1 276 GLY n 
1 277 ASN n 
1 278 CYS n 
1 279 ASN n 
1 280 THR n 
1 281 ARG n 
1 282 CYS n 
1 283 GLN n 
1 284 THR n 
1 285 PRO n 
1 286 ILE n 
1 287 GLY n 
1 288 ALA n 
1 289 ILE n 
1 290 ASN n 
1 291 SER n 
1 292 SER n 
1 293 MET n 
1 294 PRO n 
1 295 PHE n 
1 296 HIS n 
1 297 ASN n 
1 298 ILE n 
1 299 HIS n 
1 300 PRO n 
1 301 LEU n 
1 302 THR n 
1 303 ILE n 
1 304 GLY n 
1 305 GLU n 
1 306 CYS n 
1 307 PRO n 
1 308 LYS n 
1 309 TYR n 
1 310 VAL n 
1 311 LYS n 
1 312 SER n 
1 313 ASN n 
1 314 LYS n 
1 315 LEU n 
1 316 VAL n 
1 317 LEU n 
1 318 ALA n 
1 319 THR n 
1 320 GLY n 
1 321 LEU n 
1 322 ARG n 
1 323 ASN n 
1 324 SER n 
1 325 PRO n 
1 326 GLN n 
1 327 ARG n 
1 328 GLU n 
1 329 THR n 
1 330 ARG n 
2 1   GLY n 
2 2   LEU n 
2 3   PHE n 
2 4   GLY n 
2 5   ALA n 
2 6   ILE n 
2 7   ALA n 
2 8   GLY n 
2 9   PHE n 
2 10  ILE n 
2 11  GLU n 
2 12  GLY n 
2 13  GLY n 
2 14  TRP n 
2 15  GLN n 
2 16  GLY n 
2 17  MET n 
2 18  VAL n 
2 19  ASP n 
2 20  GLY n 
2 21  TRP n 
2 22  TYR n 
2 23  GLY n 
2 24  TYR n 
2 25  HIS n 
2 26  HIS n 
2 27  SER n 
2 28  ASN n 
2 29  GLU n 
2 30  GLN n 
2 31  GLY n 
2 32  SER n 
2 33  GLY n 
2 34  TYR n 
2 35  ALA n 
2 36  ALA n 
2 37  ASP n 
2 38  LYS n 
2 39  GLU n 
2 40  SER n 
2 41  THR n 
2 42  GLN n 
2 43  LYS n 
2 44  ALA n 
2 45  ILE n 
2 46  ASP n 
2 47  GLY n 
2 48  VAL n 
2 49  THR n 
2 50  ASN n 
2 51  LYS n 
2 52  VAL n 
2 53  ASN n 
2 54  SER n 
2 55  ILE n 
2 56  ILE n 
2 57  ASP n 
2 58  LYS n 
2 59  MET n 
2 60  ASN n 
2 61  THR n 
2 62  GLN n 
2 63  PHE n 
2 64  GLU n 
2 65  ALA n 
2 66  VAL n 
2 67  GLY n 
2 68  ARG n 
2 69  GLU n 
2 70  PHE n 
2 71  ASN n 
2 72  ASN n 
2 73  LEU n 
2 74  GLU n 
2 75  ARG n 
2 76  ARG n 
2 77  ILE n 
2 78  GLU n 
2 79  ASN n 
2 80  LEU n 
2 81  ASN n 
2 82  LYS n 
2 83  LYS n 
2 84  MET n 
2 85  GLU n 
2 86  ASP n 
2 87  GLY n 
2 88  PHE n 
2 89  LEU n 
2 90  ASP n 
2 91  VAL n 
2 92  TRP n 
2 93  THR n 
2 94  TYR n 
2 95  ASN n 
2 96  ALA n 
2 97  GLU n 
2 98  LEU n 
2 99  LEU n 
2 100 VAL n 
2 101 LEU n 
2 102 MET n 
2 103 GLU n 
2 104 ASN n 
2 105 GLU n 
2 106 ARG n 
2 107 THR n 
2 108 LEU n 
2 109 ASP n 
2 110 PHE n 
2 111 HIS n 
2 112 ASP n 
2 113 SER n 
2 114 ASN n 
2 115 VAL n 
2 116 ARG n 
2 117 ASN n 
2 118 LEU n 
2 119 TYR n 
2 120 ASP n 
2 121 LYS n 
2 122 VAL n 
2 123 ARG n 
2 124 LEU n 
2 125 GLN n 
2 126 LEU n 
2 127 LYS n 
2 128 ASP n 
2 129 ASN n 
2 130 ALA n 
2 131 LYS n 
2 132 GLU n 
2 133 LEU n 
2 134 GLY n 
2 135 ASN n 
2 136 GLY n 
2 137 CYS n 
2 138 PHE n 
2 139 GLU n 
2 140 PHE n 
2 141 TYR n 
2 142 HIS n 
2 143 LYS n 
2 144 CYS n 
2 145 ASP n 
2 146 ASN n 
2 147 GLU n 
2 148 CYS n 
2 149 MET n 
2 150 GLU n 
2 151 SER n 
2 152 VAL n 
2 153 ARG n 
2 154 ASN n 
2 155 GLY n 
2 156 THR n 
2 157 TYR n 
2 158 ASP n 
2 159 TYR n 
2 160 PRO n 
2 161 GLN n 
2 162 TYR n 
2 163 SER n 
2 164 GLU n 
2 165 GLU n 
2 166 ALA n 
2 167 ARG n 
2 168 LEU n 
2 169 LYS n 
2 170 ARG n 
2 171 GLU n 
2 172 GLU n 
2 173 ILE n 
2 174 SER n 
2 175 SER n 
2 176 GLY n 
2 177 ARG n 
2 178 LEU n 
2 179 VAL n 
2 180 PRO n 
2 181 ARG n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample ? ? ? ? ? HA ? 'A/Hubei/1/2010(H5N1)' ? ? ? ? 'Influenza A virus' 1087279 ? ? ? ? ? ? ? 'cabbage looper' 
'Trichoplusia ni' 7111 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample ? ? ? ? ? HA ? 'A/Hubei/1/2010(H5N1)' ? ? ? ? 'Influenza A virus' 1087279 ? ? ? ? ? ? ? 'cabbage looper' 
'Trichoplusia ni' 7111 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_db_isoform 
1 UNP G2U0T8_9INFA G2U0T8 1 
;DHICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCDLNGVKPLILKDCSVAGWLLGNPMCDEFINVPEWSYIV
EKANPANDLCYPGNFNDYEELKHLLSRINHFEKIQIIPKNSWSDHEASLGVSAACPYQGKSSFFRNVVWLIKKDNAYPTI
KKGYNNTNQEDLLVLWGIHHPNDEAEQTRLYQNPTTYISIGTSTLNQRLVPKIATRSKINGQSGRIDFFWTILKPNDAIH
FESNGNFIAPEYAYKIVKKGDSTIMKSEVEYGNCNTRCQTPIGAINSSMPFHNIHPLTIGECPKYVKSNKLVLATGLRNS
PQRERR
;
17  ? 
2 UNP G2U0T8_9INFA G2U0T8 2 
;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL
NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVRNLYDKVRLQLKDNAKELGNGCFEFYHKCDNECMESVRNGTYDYP
QYSEEARLKREEISGVKL
;
346 ? 
# 
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 4KTH A 5 ? 330 ? G2U0T8 17  ? 342 ? 1 326 
2 1 4KTH E 5 ? 330 ? G2U0T8 17  ? 342 ? 1 326 
3 2 4KTH B 1 ? 178 ? G2U0T8 346 ? 523 ? 1 178 
4 1 4KTH C 5 ? 330 ? G2U0T8 17  ? 342 ? 1 326 
5 2 4KTH F 1 ? 178 ? G2U0T8 346 ? 523 ? 1 178 
6 2 4KTH D 1 ? 178 ? G2U0T8 346 ? 523 ? 1 178 
# 
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 4KTH ALA A 1   ? UNP G2U0T8 ?   ?   'EXPRESSION TAG' -3  1  
1 4KTH ASP A 2   ? UNP G2U0T8 ?   ?   'EXPRESSION TAG' -2  2  
1 4KTH PRO A 3   ? UNP G2U0T8 ?   ?   'EXPRESSION TAG' -1  3  
1 4KTH GLY A 4   ? UNP G2U0T8 ?   ?   'EXPRESSION TAG' 0   4  
1 4KTH THR A 329 ? UNP G2U0T8 ARG 341 CONFLICT         325 5  
2 4KTH ALA E 1   ? UNP G2U0T8 ?   ?   'EXPRESSION TAG' -3  6  
2 4KTH ASP E 2   ? UNP G2U0T8 ?   ?   'EXPRESSION TAG' -2  7  
2 4KTH PRO E 3   ? UNP G2U0T8 ?   ?   'EXPRESSION TAG' -1  8  
2 4KTH GLY E 4   ? UNP G2U0T8 ?   ?   'EXPRESSION TAG' 0   9  
2 4KTH THR E 329 ? UNP G2U0T8 ARG 341 CONFLICT         325 10 
3 4KTH SER B 175 ? UNP G2U0T8 GLY 520 CONFLICT         175 11 
3 4KTH GLY B 176 ? UNP G2U0T8 VAL 521 CONFLICT         176 12 
3 4KTH ARG B 177 ? UNP G2U0T8 LYS 522 CONFLICT         177 13 
3 4KTH VAL B 179 ? UNP G2U0T8 ?   ?   'EXPRESSION TAG' 179 14 
3 4KTH PRO B 180 ? UNP G2U0T8 ?   ?   'EXPRESSION TAG' 180 15 
3 4KTH ARG B 181 ? UNP G2U0T8 ?   ?   'EXPRESSION TAG' 181 16 
4 4KTH ALA C 1   ? UNP G2U0T8 ?   ?   'EXPRESSION TAG' -3  17 
4 4KTH ASP C 2   ? UNP G2U0T8 ?   ?   'EXPRESSION TAG' -2  18 
4 4KTH PRO C 3   ? UNP G2U0T8 ?   ?   'EXPRESSION TAG' -1  19 
4 4KTH GLY C 4   ? UNP G2U0T8 ?   ?   'EXPRESSION TAG' 0   20 
4 4KTH THR C 329 ? UNP G2U0T8 ARG 341 CONFLICT         325 21 
5 4KTH SER F 175 ? UNP G2U0T8 GLY 520 CONFLICT         175 22 
5 4KTH GLY F 176 ? UNP G2U0T8 VAL 521 CONFLICT         176 23 
5 4KTH ARG F 177 ? UNP G2U0T8 LYS 522 CONFLICT         177 24 
5 4KTH VAL F 179 ? UNP G2U0T8 ?   ?   'EXPRESSION TAG' 179 25 
5 4KTH PRO F 180 ? UNP G2U0T8 ?   ?   'EXPRESSION TAG' 180 26 
5 4KTH ARG F 181 ? UNP G2U0T8 ?   ?   'EXPRESSION TAG' 181 27 
6 4KTH SER D 175 ? UNP G2U0T8 GLY 520 CONFLICT         175 28 
6 4KTH GLY D 176 ? UNP G2U0T8 VAL 521 CONFLICT         176 29 
6 4KTH ARG D 177 ? UNP G2U0T8 LYS 522 CONFLICT         177 30 
6 4KTH VAL D 179 ? UNP G2U0T8 ?   ?   'EXPRESSION TAG' 179 31 
6 4KTH PRO D 180 ? UNP G2U0T8 ?   ?   'EXPRESSION TAG' 180 32 
6 4KTH ARG D 181 ? UNP G2U0T8 ?   ?   'EXPRESSION TAG' 181 33 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE               ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE             ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'        ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE               ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE              ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'        ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE              ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                  ? 'H2 O'           18.015  
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 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE          ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                 ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE              ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN             ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE               ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                 ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          4KTH 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.70 
_exptl_crystal.density_percent_sol   54.37 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.pdbx_details    '20% PEG MME, 100mM Tris-pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   'MAR scanner 300 mm plate' 
_diffrn_detector.pdbx_collection_date   2011-08-15 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'Si 111 CHANNEL' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'APS BEAMLINE 22-ID' 
_diffrn_source.pdbx_synchrotron_site       APS 
_diffrn_source.pdbx_synchrotron_beamline   22-ID 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.0 
# 
_reflns.entry_id                     4KTH 
_reflns.observed_criterion_sigma_I   2 
_reflns.observed_criterion_sigma_F   2 
_reflns.d_resolution_low             50 
_reflns.d_resolution_high            2.6 
_reflns.number_obs                   53820 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         ? 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.089 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        51.43 
_reflns.pdbx_redundancy              3.7 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             2.60 
_reflns_shell.d_res_low              2.64 
_reflns_shell.percent_possible_all   100 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.648 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_redundancy        3.8 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      2832 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 4KTH 
_refine.ls_number_reflns_obs                     53820 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          2 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             50 
_refine.ls_d_res_high                            2.60 
_refine.ls_percent_reflns_obs                    99.17 
_refine.ls_R_factor_obs                          0.23571 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.23408 
_refine.ls_R_factor_R_free                       0.26634 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  2876 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.926 
_refine.correlation_coeff_Fo_to_Fc_free          0.904 
_refine.B_iso_mean                               44.550 
_refine.aniso_B[1][1]                            -2.72 
_refine.aniso_B[2][2]                            0.53 
_refine.aniso_B[3][3]                            2.07 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.12 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      2FK0 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.887 
_refine.pdbx_overall_ESU_R_Free                  0.333 
_refine.overall_SU_ML                            0.272 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             15.055 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        11719 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         196 
_refine_hist.number_atoms_solvent             72 
_refine_hist.number_atoms_total               11987 
_refine_hist.d_res_high                       2.60 
_refine_hist.d_res_low                        50 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d       0.006  0.020  ? 12213 ? 'X-RAY DIFFRACTION' 
r_bond_other_d         0.003  0.020  ? 8204  ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    1.073  1.955  ? 16558 ? 'X-RAY DIFFRACTION' 
r_angle_other_deg      1.023  3.004  ? 19945 ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 5.536  5.000  ? 1456  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 37.134 25.305 ? 622   ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg 17.939 15.000 ? 2076  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg 17.369 15.000 ? 51    ? 'X-RAY DIFFRACTION' 
r_chiral_restr         0.059  0.200  ? 1780  ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined   0.004  0.020  ? 13580 ? 'X-RAY DIFFRACTION' 
r_gen_planes_other     0.002  0.020  ? 2389  ? 'X-RAY DIFFRACTION' 
# 
loop_
_refine_ls_restr_ncs.dom_id 
_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.pdbx_type 
_refine_ls_restr_ncs.pdbx_ens_id 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.weight_B_iso 
1 A 11422 0.12 0.05 'interatomic distance' 1 1  'X-RAY DIFFRACTION' ? ? ? 
2 E 11422 0.12 0.05 'interatomic distance' 1 2  'X-RAY DIFFRACTION' ? ? ? 
1 A 11347 0.12 0.05 'interatomic distance' 2 3  'X-RAY DIFFRACTION' ? ? ? 
2 C 11347 0.12 0.05 'interatomic distance' 2 4  'X-RAY DIFFRACTION' ? ? ? 
1 E 11461 0.12 0.05 'interatomic distance' 3 5  'X-RAY DIFFRACTION' ? ? ? 
2 C 11461 0.12 0.05 'interatomic distance' 3 6  'X-RAY DIFFRACTION' ? ? ? 
1 B 5630  0.14 0.05 'interatomic distance' 4 7  'X-RAY DIFFRACTION' ? ? ? 
2 F 5630  0.14 0.05 'interatomic distance' 4 8  'X-RAY DIFFRACTION' ? ? ? 
1 B 5809  0.13 0.05 'interatomic distance' 5 9  'X-RAY DIFFRACTION' ? ? ? 
2 D 5809  0.13 0.05 'interatomic distance' 5 10 'X-RAY DIFFRACTION' ? ? ? 
1 F 5703  0.13 0.05 'interatomic distance' 6 11 'X-RAY DIFFRACTION' ? ? ? 
2 D 5703  0.13 0.05 'interatomic distance' 6 12 'X-RAY DIFFRACTION' ? ? ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.599 
_refine_ls_shell.d_res_low                        2.666 
_refine_ls_shell.number_reflns_R_work             3741 
_refine_ls_shell.R_factor_R_work                  0.341 
_refine_ls_shell.percent_reflns_obs               96.42 
_refine_ls_shell.R_factor_R_free                  0.414 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             194 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.details 
_struct_ncs_dom.pdbx_ens_id 
1 A 1 
2 E 1 
1 A 2 
2 C 2 
1 E 3 
2 C 3 
1 B 4 
2 F 4 
1 B 5 
2 D 5 
1 F 6 
2 D 6 
# 
loop_
_struct_ncs_dom_lim.dom_id 
_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.pdbx_component_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_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 
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.selection_details 
1 A 0  A 319 0 0 ? ? ? ? ? ? ? ? 1 ? 
2 E 0  E 319 0 0 ? ? ? ? ? ? ? ? 1 ? 
1 A 0  A 319 0 0 ? ? ? ? ? ? ? ? 2 ? 
2 C 0  C 319 0 0 ? ? ? ? ? ? ? ? 2 ? 
1 E 0  E 320 0 0 ? ? ? ? ? ? ? ? 3 ? 
2 C 0  C 320 0 0 ? ? ? ? ? ? ? ? 3 ? 
1 B 10 B 171 0 0 ? ? ? ? ? ? ? ? 4 ? 
2 F 10 F 171 0 0 ? ? ? ? ? ? ? ? 4 ? 
1 B 10 B 173 0 0 ? ? ? ? ? ? ? ? 5 ? 
2 D 10 D 173 0 0 ? ? ? ? ? ? ? ? 5 ? 
1 F 10 F 171 0 0 ? ? ? ? ? ? ? ? 6 ? 
2 D 10 D 171 0 0 ? ? ? ? ? ? ? ? 6 ? 
# 
loop_
_struct_ncs_ens.id 
_struct_ncs_ens.details 
1 ? 
2 ? 
3 ? 
4 ? 
5 ? 
6 ? 
# 
_struct.entry_id                  4KTH 
_struct.title                     'Structure of A/Hubei/1/2010 H5 HA' 
_struct.pdbx_descriptor           Hemagglutinin 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4KTH 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'hemagglutinin, VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 1 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 3 ? 
M N N 3 ? 
N N N 3 ? 
O N N 3 ? 
P N N 3 ? 
Q N N 3 ? 
R N N 3 ? 
S N N 3 ? 
T N N 3 ? 
U N N 4 ? 
V N N 4 ? 
W N N 4 ? 
X N N 4 ? 
Y N N 4 ? 
Z N N 4 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  SER A 60  ? GLY A 67  ? SER A 56  GLY A 63  1 ? 8  
HELX_P HELX_P2  2  ASP A 101 ? SER A 110 ? ASP A 97  SER A 106 1 ? 10 
HELX_P HELX_P3  3  PRO A 122 ? TRP A 126 ? PRO A 118 TRP A 122 5 ? 5  
HELX_P HELX_P4  4  ASP A 187 ? GLN A 196 ? ASP A 183 GLN A 192 1 ? 10 
HELX_P HELX_P5  5  SER B 60  ? GLY B 67  ? SER E 56  GLY E 63  1 ? 8  
HELX_P HELX_P6  6  ASP B 101 ? LEU B 109 ? ASP E 97  LEU E 105 1 ? 9  
HELX_P HELX_P7  7  PRO B 122 ? TRP B 126 ? PRO E 118 TRP E 122 5 ? 5  
HELX_P HELX_P8  8  ASP B 187 ? GLN B 196 ? ASP E 183 GLN E 192 1 ? 10 
HELX_P HELX_P9  9  ASP C 37  ? LYS C 58  ? ASP B 37  LYS B 58  1 ? 22 
HELX_P HELX_P10 10 GLU C 74  ? LYS C 127 ? GLU B 74  LYS B 127 1 ? 54 
HELX_P HELX_P11 11 ASP C 145 ? GLY C 155 ? ASP B 145 GLY B 155 1 ? 11 
HELX_P HELX_P12 12 ASP C 158 ? GLU C 171 ? ASP B 158 GLU B 171 1 ? 14 
HELX_P HELX_P13 13 SER D 60  ? GLY D 67  ? SER C 56  GLY C 63  1 ? 8  
HELX_P HELX_P14 14 ASP D 101 ? LEU D 109 ? ASP C 97  LEU C 105 1 ? 9  
HELX_P HELX_P15 15 PRO D 122 ? TRP D 126 ? PRO C 118 TRP C 122 5 ? 5  
HELX_P HELX_P16 16 ASP D 187 ? GLN D 196 ? ASP C 183 GLN C 192 1 ? 10 
HELX_P HELX_P17 17 ASP E 37  ? LYS E 58  ? ASP F 37  LYS F 58  1 ? 22 
HELX_P HELX_P18 18 GLU E 74  ? LEU E 124 ? GLU F 74  LEU F 124 1 ? 51 
HELX_P HELX_P19 19 ASP E 145 ? GLY E 155 ? ASP F 145 GLY F 155 1 ? 11 
HELX_P HELX_P20 20 ASP E 158 ? ARG E 170 ? ASP F 158 ARG F 170 1 ? 13 
HELX_P HELX_P21 21 GLY F 8   ? GLY F 12  ? GLY D 8   GLY D 12  5 ? 5  
HELX_P HELX_P22 22 ASP F 37  ? LYS F 58  ? ASP D 37  LYS D 58  1 ? 22 
HELX_P HELX_P23 23 GLU F 74  ? LEU F 124 ? GLU D 74  LEU D 124 1 ? 51 
HELX_P HELX_P24 24 ASP F 145 ? GLY F 155 ? ASP D 145 GLY D 155 1 ? 11 
HELX_P HELX_P25 25 ASP F 158 ? ARG F 170 ? ASP D 158 ARG D 170 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 8   SG  ? ? ? 1_555 C CYS 137 SG ? ? A CYS 4   B CYS 137 1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf2  disulf ? ? A CYS 46  SG  ? ? ? 1_555 A CYS 278 SG ? ? A CYS 42  A CYS 274 1_555 ? ? ? ? ? ? ? 2.033 ? 
disulf3  disulf ? ? A CYS 59  SG  ? ? ? 1_555 A CYS 71  SG ? ? A CYS 55  A CYS 67  1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf4  disulf ? ? A CYS 94  SG  ? ? ? 1_555 A CYS 139 SG ? ? A CYS 90  A CYS 135 1_555 ? ? ? ? ? ? ? 2.049 ? 
disulf5  disulf ? ? A CYS 282 SG  ? ? ? 1_555 A CYS 306 SG ? ? A CYS 278 A CYS 302 1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf6  disulf ? ? B CYS 8   SG  ? ? ? 1_555 E CYS 137 SG ? ? E CYS 4   F CYS 137 1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf7  disulf ? ? B CYS 46  SG  ? ? ? 1_555 B CYS 278 SG ? ? E CYS 42  E CYS 274 1_555 ? ? ? ? ? ? ? 2.041 ? 
disulf8  disulf ? ? B CYS 59  SG  ? ? ? 1_555 B CYS 71  SG ? ? E CYS 55  E CYS 67  1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf9  disulf ? ? B CYS 94  SG  ? ? ? 1_555 B CYS 139 SG ? ? E CYS 90  E CYS 135 1_555 ? ? ? ? ? ? ? 2.047 ? 
disulf10 disulf ? ? B CYS 282 SG  ? ? ? 1_555 B CYS 306 SG ? ? E CYS 278 E CYS 302 1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf11 disulf ? ? C CYS 144 SG  ? ? ? 1_555 C CYS 148 SG ? ? B CYS 144 B CYS 148 1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf12 disulf ? ? D CYS 8   SG  ? ? ? 1_555 F CYS 137 SG ? ? C CYS 4   D CYS 137 1_555 ? ? ? ? ? ? ? 2.045 ? 
disulf13 disulf ? ? D CYS 46  SG  ? ? ? 1_555 D CYS 278 SG ? ? C CYS 42  C CYS 274 1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf14 disulf ? ? D CYS 59  SG  ? ? ? 1_555 D CYS 71  SG ? ? C CYS 55  C CYS 67  1_555 ? ? ? ? ? ? ? 2.020 ? 
disulf15 disulf ? ? D CYS 94  SG  ? ? ? 1_555 D CYS 139 SG ? ? C CYS 90  C CYS 135 1_555 ? ? ? ? ? ? ? 2.047 ? 
disulf16 disulf ? ? D CYS 282 SG  ? ? ? 1_555 D CYS 306 SG ? ? C CYS 278 C CYS 302 1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf17 disulf ? ? E CYS 144 SG  ? ? ? 1_555 E CYS 148 SG ? ? F CYS 144 F CYS 148 1_555 ? ? ? ? ? ? ? 2.044 ? 
disulf18 disulf ? ? F CYS 144 SG  ? ? ? 1_555 F CYS 148 SG ? ? D CYS 144 D CYS 148 1_555 ? ? ? ? ? ? ? 2.041 ? 
covale1  covale ? ? A ASN 27  ND2 ? ? ? 1_555 J NAG .   C1 ? ? A ASN 23  A NAG 404 1_555 ? ? ? ? ? ? ? 1.436 ? 
covale2  covale ? ? J NAG .   O4  ? ? ? 1_555 K NAG .   C1 ? ? A NAG 404 A NAG 405 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale3  covale ? ? D ASN 27  ND2 ? ? ? 1_555 R NAG .   C1 ? ? C ASN 23  C NAG 402 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale4  covale ? ? D ASN 15  ND2 ? ? ? 1_555 S NAG .   C1 ? ? C ASN 11  C NAG 403 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale5  covale ? ? A ASN 290 ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 286 A NAG 401 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale6  covale ? ? H NAG .   O4  ? ? ? 1_555 I NAG .   C1 ? ? A NAG 402 A NAG 403 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale7  covale ? ? A ASN 169 ND2 ? ? ? 1_555 H NAG .   C1 ? ? A ASN 165 A NAG 402 1_555 ? ? ? ? ? ? ? 1.445 ? 
covale8  covale ? ? C ASN 154 ND2 ? ? ? 1_555 O NAG .   C1 ? ? B ASN 154 B NAG 201 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale9  covale ? ? D ASN 169 ND2 ? ? ? 1_555 Q NAG .   C1 ? ? C ASN 165 C NAG 401 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale10 covale ? ? O NAG .   O4  ? ? ? 1_555 P NAG .   C1 ? ? B NAG 201 B NAG 202 1_555 ? ? ? ? ? ? ? 1.447 ? 
covale11 covale ? ? A ASN 15  ND2 ? ? ? 1_555 L NAG .   C1 ? ? A ASN 11  A NAG 406 1_555 ? ? ? ? ? ? ? 1.447 ? 
covale12 covale ? ? B ASN 169 ND2 ? ? ? 1_555 M NAG .   C1 ? ? E ASN 165 E NAG 401 1_555 ? ? ? ? ? ? ? 1.449 ? 
covale13 covale ? ? E ASN 154 ND2 ? ? ? 1_555 T NAG .   C1 ? ? F ASN 154 F NAG 201 1_555 ? ? ? ? ? ? ? 1.451 ? 
covale14 covale ? ? B ASN 27  ND2 ? ? ? 1_555 N NAG .   C1 ? ? E ASN 23  E NAG 402 1_555 ? ? ? ? ? ? ? 1.454 ? 
# 
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 GLU 73 A . ? GLU 69 A PHE 74 A ? PHE 70 A 1 1.47  
2 ILE 75 A . ? ILE 71 A ASN 76 A ? ASN 72 A 1 -5.58 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A  ? 5 ? 
B  ? 2 ? 
C  ? 2 ? 
D  ? 3 ? 
E  ? 2 ? 
F  ? 3 ? 
G  ? 5 ? 
H  ? 4 ? 
I  ? 2 ? 
J  ? 2 ? 
K  ? 4 ? 
L  ? 4 ? 
M  ? 5 ? 
N  ? 2 ? 
O  ? 2 ? 
P  ? 3 ? 
Q  ? 2 ? 
R  ? 3 ? 
S  ? 5 ? 
T  ? 4 ? 
U  ? 2 ? 
V  ? 2 ? 
W  ? 4 ? 
X  ? 4 ? 
Y  ? 5 ? 
Z  ? 2 ? 
AA ? 2 ? 
AB ? 3 ? 
AC ? 2 ? 
AD ? 3 ? 
AE ? 5 ? 
AF ? 4 ? 
AG ? 2 ? 
AH ? 2 ? 
AI ? 4 ? 
AJ ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A  1 2 ? anti-parallel 
A  2 3 ? anti-parallel 
A  3 4 ? anti-parallel 
A  4 5 ? anti-parallel 
B  1 2 ? anti-parallel 
C  1 2 ? anti-parallel 
D  1 2 ? parallel      
D  2 3 ? parallel      
E  1 2 ? parallel      
F  1 2 ? parallel      
F  2 3 ? parallel      
G  1 2 ? anti-parallel 
G  2 3 ? anti-parallel 
G  3 4 ? anti-parallel 
G  4 5 ? anti-parallel 
H  1 2 ? anti-parallel 
H  2 3 ? anti-parallel 
H  3 4 ? anti-parallel 
I  1 2 ? anti-parallel 
J  1 2 ? anti-parallel 
K  1 2 ? anti-parallel 
K  2 3 ? anti-parallel 
K  3 4 ? anti-parallel 
L  1 2 ? anti-parallel 
L  2 3 ? anti-parallel 
L  3 4 ? anti-parallel 
M  1 2 ? anti-parallel 
M  2 3 ? anti-parallel 
M  3 4 ? anti-parallel 
M  4 5 ? anti-parallel 
N  1 2 ? anti-parallel 
O  1 2 ? anti-parallel 
P  1 2 ? parallel      
P  2 3 ? parallel      
Q  1 2 ? parallel      
R  1 2 ? parallel      
R  2 3 ? parallel      
S  1 2 ? anti-parallel 
S  2 3 ? anti-parallel 
S  3 4 ? anti-parallel 
S  4 5 ? anti-parallel 
T  1 2 ? anti-parallel 
T  2 3 ? anti-parallel 
T  3 4 ? anti-parallel 
U  1 2 ? anti-parallel 
V  1 2 ? anti-parallel 
W  1 2 ? anti-parallel 
W  2 3 ? anti-parallel 
W  3 4 ? anti-parallel 
X  1 2 ? anti-parallel 
X  2 3 ? anti-parallel 
X  3 4 ? anti-parallel 
Y  1 2 ? anti-parallel 
Y  2 3 ? anti-parallel 
Y  3 4 ? anti-parallel 
Y  4 5 ? anti-parallel 
Z  1 2 ? anti-parallel 
AA 1 2 ? anti-parallel 
AB 1 2 ? parallel      
AB 2 3 ? parallel      
AC 1 2 ? parallel      
AD 1 2 ? parallel      
AD 2 3 ? parallel      
AE 1 2 ? anti-parallel 
AE 2 3 ? anti-parallel 
AE 3 4 ? anti-parallel 
AE 4 5 ? anti-parallel 
AF 1 2 ? anti-parallel 
AF 2 3 ? anti-parallel 
AF 3 4 ? anti-parallel 
AG 1 2 ? anti-parallel 
AH 1 2 ? anti-parallel 
AI 1 2 ? anti-parallel 
AI 2 3 ? anti-parallel 
AI 3 4 ? anti-parallel 
AJ 1 2 ? anti-parallel 
AJ 2 3 ? anti-parallel 
AJ 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 
A  1 GLY C 31  ? ALA C 36  ? GLY B 31  ALA B 36  
A  2 TYR C 22  ? ASN C 28  ? TYR B 22  ASN B 28  
A  3 HIS A 6   ? TYR A 11  ? HIS A 2   TYR A 7   
A  4 CYS C 137 ? PHE C 140 ? CYS B 137 PHE B 140 
A  5 ALA C 130 ? GLU C 132 ? ALA B 130 GLU B 132 
B  1 GLN A 19  ? VAL A 20  ? GLN A 15  VAL A 16  
B  2 VAL A 28  ? THR A 29  ? VAL A 24  THR A 25  
C  1 ALA A 33  ? ASP A 35  ? ALA A 29  ASP A 31  
C  2 VAL A 316 ? ALA A 318 ? VAL A 312 ALA A 314 
D  1 LEU A 37  ? GLU A 38  ? LEU A 33  GLU A 34  
D  2 PHE A 295 ? HIS A 296 ? PHE A 291 HIS A 292 
D  3 LYS A 308 ? TYR A 309 ? LYS A 304 TYR A 305 
E  1 LEU A 45  ? LEU A 48  ? LEU A 41  LEU A 44  
E  2 TYR A 275 ? THR A 280 ? TYR A 271 THR A 276 
F  1 LEU A 54  ? ILE A 55  ? LEU A 50  ILE A 51  
F  2 ILE A 83  ? GLU A 85  ? ILE A 79  GLU A 81  
F  3 ILE A 268 ? LYS A 270 ? ILE A 264 LYS A 266 
G  1 HIS A 114 ? GLN A 119 ? HIS A 110 GLN A 115 
G  2 TYR A 256 ? VAL A 261 ? TYR A 252 VAL A 257 
G  3 ASP A 175 ? HIS A 184 ? ASP A 171 HIS A 180 
G  4 PHE A 251 ? PRO A 254 ? PHE A 247 PRO A 250 
G  5 VAL A 151 ? TRP A 153 ? VAL A 147 TRP A 149 
H  1 HIS A 114 ? GLN A 119 ? HIS A 110 GLN A 115 
H  2 TYR A 256 ? VAL A 261 ? TYR A 252 VAL A 257 
H  3 ASP A 175 ? HIS A 184 ? ASP A 171 HIS A 180 
H  4 ARG A 229 ? LEU A 237 ? ARG A 225 LEU A 233 
I  1 HIS A 129 ? GLU A 130 ? HIS A 125 GLU A 126 
I  2 ILE A 155 ? LYS A 156 ? ILE A 151 LYS A 152 
J  1 SER A 136 ? PRO A 140 ? SER A 132 PRO A 136 
J  2 SER A 145 ? SER A 146 ? SER A 141 SER A 142 
K  1 ILE A 164 ? ASN A 169 ? ILE A 160 ASN A 165 
K  2 ALA A 242 ? SER A 247 ? ALA A 238 SER A 243 
K  3 ILE A 202 ? GLY A 205 ? ILE A 198 GLY A 201 
K  4 ASN A 210 ? LEU A 213 ? ASN A 206 LEU A 209 
L  1 GLY A 287 ? ALA A 288 ? GLY A 283 ALA A 284 
L  2 CYS A 282 ? THR A 284 ? CYS A 278 THR A 280 
L  3 ILE A 303 ? GLU A 305 ? ILE A 299 GLU A 301 
L  4 PHE C 63  ? ALA C 65  ? PHE B 63  ALA B 65  
M  1 GLY E 31  ? ALA E 36  ? GLY F 31  ALA F 36  
M  2 TYR E 22  ? ASN E 28  ? TYR F 22  ASN F 28  
M  3 HIS B 6   ? TYR B 11  ? HIS E 2   TYR E 7   
M  4 CYS E 137 ? PHE E 140 ? CYS F 137 PHE F 140 
M  5 ALA E 130 ? GLU E 132 ? ALA F 130 GLU F 132 
N  1 GLN B 19  ? VAL B 20  ? GLN E 15  VAL E 16  
N  2 VAL B 28  ? THR B 29  ? VAL E 24  THR E 25  
O  1 ALA B 33  ? ASP B 35  ? ALA E 29  ASP E 31  
O  2 VAL B 316 ? ALA B 318 ? VAL E 312 ALA E 314 
P  1 LEU B 37  ? GLU B 38  ? LEU E 33  GLU E 34  
P  2 PHE B 295 ? HIS B 296 ? PHE E 291 HIS E 292 
P  3 LYS B 308 ? TYR B 309 ? LYS E 304 TYR E 305 
Q  1 LEU B 45  ? LEU B 48  ? LEU E 41  LEU E 44  
Q  2 TYR B 275 ? THR B 280 ? TYR E 271 THR E 276 
R  1 LEU B 54  ? ILE B 55  ? LEU E 50  ILE E 51  
R  2 ILE B 83  ? GLU B 85  ? ILE E 79  GLU E 81  
R  3 ILE B 268 ? LYS B 270 ? ILE E 264 LYS E 266 
S  1 HIS B 114 ? GLN B 119 ? HIS E 110 GLN E 115 
S  2 TYR B 256 ? VAL B 261 ? TYR E 252 VAL E 257 
S  3 ASP B 175 ? HIS B 184 ? ASP E 171 HIS E 180 
S  4 PHE B 251 ? PRO B 254 ? PHE E 247 PRO E 250 
S  5 VAL B 151 ? TRP B 153 ? VAL E 147 TRP E 149 
T  1 HIS B 114 ? GLN B 119 ? HIS E 110 GLN E 115 
T  2 TYR B 256 ? VAL B 261 ? TYR E 252 VAL E 257 
T  3 ASP B 175 ? HIS B 184 ? ASP E 171 HIS E 180 
T  4 ARG B 229 ? LEU B 237 ? ARG E 225 LEU E 233 
U  1 HIS B 129 ? GLU B 130 ? HIS E 125 GLU E 126 
U  2 ILE B 155 ? LYS B 156 ? ILE E 151 LYS E 152 
V  1 SER B 136 ? PRO B 140 ? SER E 132 PRO E 136 
V  2 SER B 145 ? SER B 146 ? SER E 141 SER E 142 
W  1 ILE B 164 ? ASN B 169 ? ILE E 160 ASN E 165 
W  2 ALA B 242 ? SER B 247 ? ALA E 238 SER E 243 
W  3 ILE B 202 ? GLY B 205 ? ILE E 198 GLY E 201 
W  4 ASN B 210 ? LEU B 213 ? ASN E 206 LEU E 209 
X  1 GLY B 287 ? ALA B 288 ? GLY E 283 ALA E 284 
X  2 CYS B 282 ? THR B 284 ? CYS E 278 THR E 280 
X  3 ILE B 303 ? GLU B 305 ? ILE E 299 GLU E 301 
X  4 PHE E 63  ? ALA E 65  ? PHE F 63  ALA F 65  
Y  1 GLY F 31  ? ALA F 36  ? GLY D 31  ALA D 36  
Y  2 TYR F 22  ? ASN F 28  ? TYR D 22  ASN D 28  
Y  3 HIS D 6   ? TYR D 11  ? HIS C 2   TYR C 7   
Y  4 CYS F 137 ? PHE F 140 ? CYS D 137 PHE D 140 
Y  5 ALA F 130 ? GLU F 132 ? ALA D 130 GLU D 132 
Z  1 GLN D 19  ? VAL D 20  ? GLN C 15  VAL C 16  
Z  2 VAL D 28  ? THR D 29  ? VAL C 24  THR C 25  
AA 1 ALA D 33  ? ASP D 35  ? ALA C 29  ASP C 31  
AA 2 VAL D 316 ? ALA D 318 ? VAL C 312 ALA C 314 
AB 1 LEU D 37  ? GLU D 38  ? LEU C 33  GLU C 34  
AB 2 PHE D 295 ? HIS D 296 ? PHE C 291 HIS C 292 
AB 3 LYS D 308 ? TYR D 309 ? LYS C 304 TYR C 305 
AC 1 LEU D 45  ? LEU D 48  ? LEU C 41  LEU C 44  
AC 2 TYR D 275 ? THR D 280 ? TYR C 271 THR C 276 
AD 1 LEU D 54  ? ILE D 55  ? LEU C 50  ILE C 51  
AD 2 ILE D 83  ? GLU D 85  ? ILE C 79  GLU C 81  
AD 3 ILE D 268 ? LYS D 270 ? ILE C 264 LYS C 266 
AE 1 HIS D 114 ? GLN D 119 ? HIS C 110 GLN C 115 
AE 2 TYR D 256 ? VAL D 261 ? TYR C 252 VAL C 257 
AE 3 ASP D 175 ? HIS D 184 ? ASP C 171 HIS C 180 
AE 4 PHE D 251 ? PRO D 254 ? PHE C 247 PRO C 250 
AE 5 VAL D 151 ? TRP D 153 ? VAL C 147 TRP C 149 
AF 1 HIS D 114 ? GLN D 119 ? HIS C 110 GLN C 115 
AF 2 TYR D 256 ? VAL D 261 ? TYR C 252 VAL C 257 
AF 3 ASP D 175 ? HIS D 184 ? ASP C 171 HIS C 180 
AF 4 ARG D 229 ? LEU D 237 ? ARG C 225 LEU C 233 
AG 1 HIS D 129 ? GLU D 130 ? HIS C 125 GLU C 126 
AG 2 ILE D 155 ? LYS D 156 ? ILE C 151 LYS C 152 
AH 1 SER D 136 ? PRO D 140 ? SER C 132 PRO C 136 
AH 2 SER D 145 ? SER D 146 ? SER C 141 SER C 142 
AI 1 ILE D 164 ? ASN D 169 ? ILE C 160 ASN C 165 
AI 2 ALA D 242 ? SER D 247 ? ALA C 238 SER C 243 
AI 3 ILE D 202 ? GLY D 205 ? ILE C 198 GLY C 201 
AI 4 ASN D 210 ? LEU D 213 ? ASN C 206 LEU C 209 
AJ 1 GLY D 287 ? ALA D 288 ? GLY C 283 ALA C 284 
AJ 2 CYS D 282 ? THR D 284 ? CYS C 278 THR C 280 
AJ 3 ILE D 303 ? GLU D 305 ? ILE C 299 GLU C 301 
AJ 4 PHE F 63  ? ALA F 65  ? PHE D 63  ALA D 65  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A  1 2 O ALA C 35  ? O ALA B 35  N TYR C 24  ? N TYR B 24  
A  2 3 O HIS C 25  ? O HIS B 25  N CYS A 8   ? N CYS A 4   
A  3 4 N ILE A 7   ? N ILE A 3   O PHE C 138 ? O PHE B 138 
A  4 5 O GLU C 139 ? O GLU B 139 N LYS C 131 ? N LYS B 131 
B  1 2 N VAL A 20  ? N VAL A 16  O VAL A 28  ? O VAL A 24  
C  1 2 N GLN A 34  ? N GLN A 30  O LEU A 317 ? O LEU A 313 
D  1 2 N GLU A 38  ? N GLU A 34  O PHE A 295 ? O PHE A 291 
D  2 3 N HIS A 296 ? N HIS A 292 O LYS A 308 ? O LYS A 304 
E  1 2 N ASP A 47  ? N ASP A 43  O CYS A 278 ? O CYS A 274 
F  1 2 N LEU A 54  ? N LEU A 50  O VAL A 84  ? O VAL A 80  
F  2 3 N ILE A 83  ? N ILE A 79  O MET A 269 ? O MET A 265 
G  1 2 N GLU A 116 ? N GLU A 112 O LYS A 259 ? O LYS A 255 
G  2 3 O ILE A 260 ? O ILE A 256 N ASP A 175 ? N ASP A 171 
G  3 4 N GLY A 181 ? N GLY A 177 O ILE A 252 ? O ILE A 248 
G  4 5 O ALA A 253 ? O ALA A 249 N VAL A 152 ? N VAL A 148 
H  1 2 N GLU A 116 ? N GLU A 112 O LYS A 259 ? O LYS A 255 
H  2 3 O ILE A 260 ? O ILE A 256 N ASP A 175 ? N ASP A 171 
H  3 4 N LEU A 176 ? N LEU A 172 O LEU A 237 ? O LEU A 233 
I  1 2 N GLU A 130 ? N GLU A 126 O ILE A 155 ? O ILE A 151 
J  1 2 N SER A 136 ? N SER A 132 O SER A 146 ? O SER A 142 
K  1 2 N LYS A 166 ? N LYS A 162 O PHE A 245 ? O PHE A 241 
K  2 3 O GLU A 246 ? O GLU A 242 N SER A 203 ? N SER A 199 
K  3 4 N ILE A 202 ? N ILE A 198 O LEU A 213 ? O LEU A 209 
L  1 2 O GLY A 287 ? O GLY A 283 N THR A 284 ? N THR A 280 
L  2 3 N GLN A 283 ? N GLN A 279 O ILE A 303 ? O ILE A 299 
L  3 4 N GLY A 304 ? N GLY A 300 O GLU C 64  ? O GLU B 64  
M  1 2 O ALA E 35  ? O ALA F 35  N TYR E 24  ? N TYR F 24  
M  2 3 O HIS E 25  ? O HIS F 25  N CYS B 8   ? N CYS E 4   
M  3 4 N ILE B 7   ? N ILE E 3   O PHE E 138 ? O PHE F 138 
M  4 5 O GLU E 139 ? O GLU F 139 N LYS E 131 ? N LYS F 131 
N  1 2 N VAL B 20  ? N VAL E 16  O VAL B 28  ? O VAL E 24  
O  1 2 N GLN B 34  ? N GLN E 30  O LEU B 317 ? O LEU E 313 
P  1 2 N GLU B 38  ? N GLU E 34  O PHE B 295 ? O PHE E 291 
P  2 3 N HIS B 296 ? N HIS E 292 O LYS B 308 ? O LYS E 304 
Q  1 2 N ASP B 47  ? N ASP E 43  O CYS B 278 ? O CYS E 274 
R  1 2 N LEU B 54  ? N LEU E 50  O VAL B 84  ? O VAL E 80  
R  2 3 N ILE B 83  ? N ILE E 79  O MET B 269 ? O MET E 265 
S  1 2 N GLU B 116 ? N GLU E 112 O LYS B 259 ? O LYS E 255 
S  2 3 O ILE B 260 ? O ILE E 256 N ASP B 175 ? N ASP E 171 
S  3 4 N GLY B 181 ? N GLY E 177 O ILE B 252 ? O ILE E 248 
S  4 5 O ALA B 253 ? O ALA E 249 N VAL B 152 ? N VAL E 148 
T  1 2 N GLU B 116 ? N GLU E 112 O LYS B 259 ? O LYS E 255 
T  2 3 O ILE B 260 ? O ILE E 256 N ASP B 175 ? N ASP E 171 
T  3 4 N LEU B 176 ? N LEU E 172 O LEU B 237 ? O LEU E 233 
U  1 2 N GLU B 130 ? N GLU E 126 O ILE B 155 ? O ILE E 151 
V  1 2 N SER B 136 ? N SER E 132 O SER B 146 ? O SER E 142 
W  1 2 N LYS B 166 ? N LYS E 162 O PHE B 245 ? O PHE E 241 
W  2 3 O GLU B 246 ? O GLU E 242 N SER B 203 ? N SER E 199 
W  3 4 N ILE B 202 ? N ILE E 198 O LEU B 213 ? O LEU E 209 
X  1 2 O GLY B 287 ? O GLY E 283 N THR B 284 ? N THR E 280 
X  2 3 N GLN B 283 ? N GLN E 279 O ILE B 303 ? O ILE E 299 
X  3 4 N GLY B 304 ? N GLY E 300 O GLU E 64  ? O GLU F 64  
Y  1 2 O ALA F 35  ? O ALA D 35  N TYR F 24  ? N TYR D 24  
Y  2 3 O HIS F 25  ? O HIS D 25  N CYS D 8   ? N CYS C 4   
Y  3 4 N ILE D 7   ? N ILE C 3   O PHE F 138 ? O PHE D 138 
Y  4 5 O GLU F 139 ? O GLU D 139 N LYS F 131 ? N LYS D 131 
Z  1 2 N VAL D 20  ? N VAL C 16  O VAL D 28  ? O VAL C 24  
AA 1 2 N GLN D 34  ? N GLN C 30  O LEU D 317 ? O LEU C 313 
AB 1 2 N GLU D 38  ? N GLU C 34  O PHE D 295 ? O PHE C 291 
AB 2 3 N HIS D 296 ? N HIS C 292 O LYS D 308 ? O LYS C 304 
AC 1 2 N ASP D 47  ? N ASP C 43  O CYS D 278 ? O CYS C 274 
AD 1 2 N LEU D 54  ? N LEU C 50  O VAL D 84  ? O VAL C 80  
AD 2 3 N ILE D 83  ? N ILE C 79  O MET D 269 ? O MET C 265 
AE 1 2 N GLU D 116 ? N GLU C 112 O LYS D 259 ? O LYS C 255 
AE 2 3 O ILE D 260 ? O ILE C 256 N ASP D 175 ? N ASP C 171 
AE 3 4 N GLY D 181 ? N GLY C 177 O ILE D 252 ? O ILE C 248 
AE 4 5 O ALA D 253 ? O ALA C 249 N VAL D 152 ? N VAL C 148 
AF 1 2 N GLU D 116 ? N GLU C 112 O LYS D 259 ? O LYS C 255 
AF 2 3 O ILE D 260 ? O ILE C 256 N ASP D 175 ? N ASP C 171 
AF 3 4 N LEU D 176 ? N LEU C 172 O LEU D 237 ? O LEU C 233 
AG 1 2 N GLU D 130 ? N GLU C 126 O ILE D 155 ? O ILE C 151 
AH 1 2 N SER D 136 ? N SER C 132 O SER D 146 ? O SER C 142 
AI 1 2 N LYS D 166 ? N LYS C 162 O PHE D 245 ? O PHE C 241 
AI 2 3 O GLU D 246 ? O GLU C 242 N SER D 203 ? N SER C 199 
AI 3 4 N ILE D 202 ? N ILE C 198 O LEU D 213 ? O LEU C 209 
AJ 1 2 O GLY D 287 ? O GLY C 283 N THR D 284 ? N THR C 280 
AJ 2 3 N GLN D 283 ? N GLN C 279 O ILE D 303 ? O ILE C 299 
AJ 3 4 N GLY D 304 ? N GLY C 300 O GLU F 64  ? O GLU D 64  
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 1 'BINDING SITE FOR MONO-SACCHARIDE NAG A 406 BOUND TO ASN A 11'             
AC2 Software ? ? ? ? 1 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 23 RESIDUES 404 TO 405'  
AC3 Software ? ? ? ? 5 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 165 RESIDUES 402 TO 403' 
AC4 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG A 401 BOUND TO ASN A 286'            
AC5 Software ? ? ? ? 2 'BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B 154 RESIDUES 201 TO 202' 
AC6 Software ? ? ? ? 1 'BINDING SITE FOR MONO-SACCHARIDE NAG C 403 BOUND TO ASN C 11'             
AC7 Software ? ? ? ? 1 'BINDING SITE FOR MONO-SACCHARIDE NAG C 402 BOUND TO ASN C 23'             
AC8 Software ? ? ? ? 5 'BINDING SITE FOR MONO-SACCHARIDE NAG C 401 BOUND TO ASN C 165'            
AC9 Software ? ? ? ? 1 'BINDING SITE FOR MONO-SACCHARIDE NAG E 402 BOUND TO ASN E 23'             
BC1 Software ? ? ? ? 5 'BINDING SITE FOR MONO-SACCHARIDE NAG E 401 BOUND TO ASN E 165'            
BC2 Software ? ? ? ? 6 'BINDING SITE FOR MONO-SACCHARIDE NAG F 201 BOUND TO ASN F 154'            
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 1 ASN A 15  ? ASN A 11  . ? 1_555 ? 
2  AC2 1 ASN A 27  ? ASN A 23  . ? 1_555 ? 
3  AC3 5 ASN A 169 ? ASN A 165 . ? 1_555 ? 
4  AC3 5 ASN A 240 ? ASN A 236 . ? 1_555 ? 
5  AC3 5 ASP A 241 ? ASP A 237 . ? 1_555 ? 
6  AC3 5 ALA A 242 ? ALA A 238 . ? 1_555 ? 
7  AC3 5 SER B 221 ? SER E 217 . ? 1_555 ? 
8  AC4 2 ARG A 281 ? ARG A 277 . ? 1_555 ? 
9  AC4 2 ASN A 290 ? ASN A 286 . ? 1_555 ? 
10 AC5 2 GLU C 147 ? GLU B 147 . ? 1_555 ? 
11 AC5 2 ASN C 154 ? ASN B 154 . ? 1_555 ? 
12 AC6 1 ASN D 15  ? ASN C 11  . ? 1_555 ? 
13 AC7 1 ASN D 27  ? ASN C 23  . ? 1_555 ? 
14 AC8 5 SER A 221 ? SER A 217 . ? 1_555 ? 
15 AC8 5 ASN D 169 ? ASN C 165 . ? 1_555 ? 
16 AC8 5 ASN D 240 ? ASN C 236 . ? 1_555 ? 
17 AC8 5 ASP D 241 ? ASP C 237 . ? 1_555 ? 
18 AC8 5 ALA D 242 ? ALA C 238 . ? 1_555 ? 
19 AC9 1 ASN B 27  ? ASN E 23  . ? 1_555 ? 
20 BC1 5 SER D 221 ? SER C 217 . ? 1_555 ? 
21 BC1 5 ASN B 169 ? ASN E 165 . ? 1_555 ? 
22 BC1 5 ASN B 240 ? ASN E 236 . ? 1_555 ? 
23 BC1 5 ASP B 241 ? ASP E 237 . ? 1_555 ? 
24 BC1 5 ALA B 242 ? ALA E 238 . ? 1_555 ? 
25 BC2 6 GLN B 173 ? GLN E 169 . ? 2_555 ? 
26 BC2 6 LYS B 259 ? LYS E 255 . ? 2_555 ? 
27 BC2 6 GLU E 147 ? GLU F 147 . ? 1_555 ? 
28 BC2 6 GLU E 150 ? GLU F 150 . ? 1_555 ? 
29 BC2 6 SER E 151 ? SER F 151 . ? 1_555 ? 
30 BC2 6 ASN E 154 ? ASN F 154 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          4KTH 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    4KTH 
_atom_sites.fract_transf_matrix[1][1]   0.005743 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003542 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009844 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.009405 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N N   . GLY A 1 4   ? -63.441 24.922  25.035  1.00 60.36  ? 0   GLY A N   1 
ATOM   2     C CA  . GLY A 1 4   ? -63.394 23.427  24.979  1.00 61.49  ? 0   GLY A CA  1 
ATOM   3     C C   . GLY A 1 4   ? -62.502 22.802  26.042  1.00 55.64  ? 0   GLY A C   1 
ATOM   4     O O   . GLY A 1 4   ? -61.739 23.495  26.714  1.00 59.93  ? 0   GLY A O   1 
ATOM   5     N N   . ASP A 1 5   ? -62.604 21.484  26.189  1.00 51.92  ? 1   ASP A N   1 
ATOM   6     C CA  . ASP A 1 5   ? -61.807 20.738  27.163  1.00 54.06  ? 1   ASP A CA  1 
ATOM   7     C C   . ASP A 1 5   ? -60.360 20.606  26.694  1.00 53.69  ? 1   ASP A C   1 
ATOM   8     O O   . ASP A 1 5   ? -60.119 20.374  25.511  1.00 47.53  ? 1   ASP A O   1 
ATOM   9     C CB  . ASP A 1 5   ? -62.425 19.354  27.386  1.00 57.48  ? 1   ASP A CB  1 
ATOM   10    C CG  . ASP A 1 5   ? -63.856 19.436  27.914  1.00 62.92  ? 1   ASP A CG  1 
ATOM   11    O OD1 . ASP A 1 5   ? -64.289 18.557  28.697  1.00 53.32  ? 1   ASP A OD1 1 
ATOM   12    O OD2 . ASP A 1 5   ? -64.568 20.402  27.523  1.00 88.69  ? 1   ASP A OD2 1 
ATOM   13    N N   . HIS A 1 6   ? -59.413 20.757  27.623  1.00 50.87  ? 2   HIS A N   1 
ATOM   14    C CA  . HIS A 1 6   ? -57.984 20.756  27.302  1.00 49.23  ? 2   HIS A CA  1 
ATOM   15    C C   . HIS A 1 6   ? -57.224 19.646  27.967  1.00 45.45  ? 2   HIS A C   1 
ATOM   16    O O   . HIS A 1 6   ? -57.579 19.202  29.056  1.00 47.77  ? 2   HIS A O   1 
ATOM   17    C CB  . HIS A 1 6   ? -57.340 22.073  27.723  1.00 57.60  ? 2   HIS A CB  1 
ATOM   18    C CG  . HIS A 1 6   ? -57.931 23.286  27.055  1.00 70.54  ? 2   HIS A CG  1 
ATOM   19    N ND1 . HIS A 1 6   ? -58.214 24.415  27.729  1.00 85.59  ? 2   HIS A ND1 1 
ATOM   20    C CD2 . HIS A 1 6   ? -58.303 23.513  25.736  1.00 76.44  ? 2   HIS A CD2 1 
ATOM   21    C CE1 . HIS A 1 6   ? -58.732 25.324  26.881  1.00 88.69  ? 2   HIS A CE1 1 
ATOM   22    N NE2 . HIS A 1 6   ? -58.786 24.771  25.661  1.00 81.83  ? 2   HIS A NE2 1 
ATOM   23    N N   . ILE A 1 7   ? -56.169 19.189  27.299  1.00 43.78  ? 3   ILE A N   1 
ATOM   24    C CA  . ILE A 1 7   ? -55.109 18.406  27.931  1.00 39.72  ? 3   ILE A CA  1 
ATOM   25    C C   . ILE A 1 7   ? -53.772 18.952  27.427  1.00 39.08  ? 3   ILE A C   1 
ATOM   26    O O   . ILE A 1 7   ? -53.627 19.242  26.243  1.00 37.76  ? 3   ILE A O   1 
ATOM   27    C CB  . ILE A 1 7   ? -55.242 16.892  27.647  1.00 41.65  ? 3   ILE A CB  1 
ATOM   28    C CG1 . ILE A 1 7   ? -54.266 16.098  28.518  1.00 40.66  ? 3   ILE A CG1 1 
ATOM   29    C CG2 . ILE A 1 7   ? -55.016 16.580  26.172  1.00 38.66  ? 3   ILE A CG2 1 
ATOM   30    C CD1 . ILE A 1 7   ? -54.530 14.610  28.522  1.00 40.76  ? 3   ILE A CD1 1 
ATOM   31    N N   . CYS A 1 8   ? -52.811 19.110  28.333  1.00 43.53  ? 4   CYS A N   1 
ATOM   32    C CA  . CYS A 1 8   ? -51.510 19.684  28.001  1.00 40.93  ? 4   CYS A CA  1 
ATOM   33    C C   . CYS A 1 8   ? -50.383 18.754  28.414  1.00 43.67  ? 4   CYS A C   1 
ATOM   34    O O   . CYS A 1 8   ? -50.530 17.982  29.360  1.00 42.74  ? 4   CYS A O   1 
ATOM   35    C CB  . CYS A 1 8   ? -51.327 21.021  28.712  1.00 44.80  ? 4   CYS A CB  1 
ATOM   36    S SG  . CYS A 1 8   ? -52.542 22.277  28.278  1.00 63.26  ? 4   CYS A SG  1 
ATOM   37    N N   . ILE A 1 9   ? -49.261 18.831  27.701  1.00 40.82  ? 5   ILE A N   1 
ATOM   38    C CA  . ILE A 1 9   ? -48.040 18.142  28.105  1.00 35.21  ? 5   ILE A CA  1 
ATOM   39    C C   . ILE A 1 9   ? -47.049 19.192  28.579  1.00 34.59  ? 5   ILE A C   1 
ATOM   40    O O   . ILE A 1 9   ? -46.934 20.269  27.990  1.00 36.86  ? 5   ILE A O   1 
ATOM   41    C CB  . ILE A 1 9   ? -47.413 17.316  26.965  1.00 36.52  ? 5   ILE A CB  1 
ATOM   42    C CG1 . ILE A 1 9   ? -48.284 16.105  26.640  1.00 38.15  ? 5   ILE A CG1 1 
ATOM   43    C CG2 . ILE A 1 9   ? -46.019 16.848  27.349  1.00 36.80  ? 5   ILE A CG2 1 
ATOM   44    C CD1 . ILE A 1 9   ? -49.529 16.457  25.863  1.00 39.64  ? 5   ILE A CD1 1 
ATOM   45    N N   . GLY A 1 10  ? -46.340 18.875  29.654  1.00 33.12  ? 6   GLY A N   1 
ATOM   46    C CA  . GLY A 1 10  ? -45.403 19.811  30.250  1.00 30.70  ? 6   GLY A CA  1 
ATOM   47    C C   . GLY A 1 10  ? -44.477 19.128  31.226  1.00 30.67  ? 6   GLY A C   1 
ATOM   48    O O   . GLY A 1 10  ? -44.465 17.900  31.334  1.00 27.90  ? 6   GLY A O   1 
ATOM   49    N N   . TYR A 1 11  ? -43.713 19.937  31.952  1.00 36.58  ? 7   TYR A N   1 
ATOM   50    C CA  . TYR A 1 11  ? -42.694 19.420  32.852  1.00 41.42  ? 7   TYR A CA  1 
ATOM   51    C C   . TYR A 1 11  ? -42.554 20.240  34.140  1.00 43.46  ? 7   TYR A C   1 
ATOM   52    O O   . TYR A 1 11  ? -43.090 21.337  34.251  1.00 40.69  ? 7   TYR A O   1 
ATOM   53    C CB  . TYR A 1 11  ? -41.352 19.331  32.108  1.00 41.37  ? 7   TYR A CB  1 
ATOM   54    C CG  . TYR A 1 11  ? -40.878 20.630  31.498  1.00 37.42  ? 7   TYR A CG  1 
ATOM   55    C CD1 . TYR A 1 11  ? -40.053 21.483  32.203  1.00 41.87  ? 7   TYR A CD1 1 
ATOM   56    C CD2 . TYR A 1 11  ? -41.240 20.991  30.206  1.00 38.61  ? 7   TYR A CD2 1 
ATOM   57    C CE1 . TYR A 1 11  ? -39.608 22.669  31.642  1.00 43.16  ? 7   TYR A CE1 1 
ATOM   58    C CE2 . TYR A 1 11  ? -40.804 22.176  29.636  1.00 36.80  ? 7   TYR A CE2 1 
ATOM   59    C CZ  . TYR A 1 11  ? -39.987 23.013  30.362  1.00 40.43  ? 7   TYR A CZ  1 
ATOM   60    O OH  . TYR A 1 11  ? -39.538 24.194  29.811  1.00 48.76  ? 7   TYR A OH  1 
ATOM   61    N N   . HIS A 1 12  ? -41.805 19.694  35.094  1.00 48.60  ? 8   HIS A N   1 
ATOM   62    C CA  . HIS A 1 12  ? -41.682 20.260  36.441  1.00 47.14  ? 8   HIS A CA  1 
ATOM   63    C C   . HIS A 1 12  ? -40.947 21.569  36.467  1.00 44.76  ? 8   HIS A C   1 
ATOM   64    O O   . HIS A 1 12  ? -40.082 21.827  35.635  1.00 48.39  ? 8   HIS A O   1 
ATOM   65    C CB  . HIS A 1 12  ? -40.988 19.249  37.354  1.00 51.42  ? 8   HIS A CB  1 
ATOM   66    C CG  . HIS A 1 12  ? -40.775 19.735  38.775  1.00 61.18  ? 8   HIS A CG  1 
ATOM   67    N ND1 . HIS A 1 12  ? -41.793 19.953  39.629  1.00 61.28  ? 8   HIS A ND1 1 
ATOM   68    C CD2 . HIS A 1 12  ? -39.603 20.032  39.479  1.00 66.08  ? 8   HIS A CD2 1 
ATOM   69    C CE1 . HIS A 1 12  ? -41.303 20.373  40.813  1.00 63.87  ? 8   HIS A CE1 1 
ATOM   70    N NE2 . HIS A 1 12  ? -39.967 20.420  40.719  1.00 66.64  ? 8   HIS A NE2 1 
ATOM   71    N N   . ALA A 1 13  ? -41.313 22.416  37.425  1.00 43.24  ? 9   ALA A N   1 
ATOM   72    C CA  . ALA A 1 13  ? -40.623 23.680  37.685  1.00 39.95  ? 9   ALA A CA  1 
ATOM   73    C C   . ALA A 1 13  ? -40.622 23.925  39.190  1.00 38.39  ? 9   ALA A C   1 
ATOM   74    O O   . ALA A 1 13  ? -41.439 23.357  39.912  1.00 47.06  ? 9   ALA A O   1 
ATOM   75    C CB  . ALA A 1 13  ? -41.308 24.824  36.953  1.00 33.91  ? 9   ALA A CB  1 
ATOM   76    N N   . ASN A 1 14  ? -39.695 24.750  39.664  1.00 36.59  ? 10  ASN A N   1 
ATOM   77    C CA  . ASN A 1 14  ? -39.628 25.097  41.082  1.00 35.82  ? 10  ASN A CA  1 
ATOM   78    C C   . ASN A 1 14  ? -39.020 26.490  41.292  1.00 38.23  ? 10  ASN A C   1 
ATOM   79    O O   . ASN A 1 14  ? -38.876 27.252  40.339  1.00 37.10  ? 10  ASN A O   1 
ATOM   80    C CB  . ASN A 1 14  ? -38.867 24.012  41.863  1.00 34.30  ? 10  ASN A CB  1 
ATOM   81    C CG  . ASN A 1 14  ? -37.411 23.893  41.446  1.00 34.10  ? 10  ASN A CG  1 
ATOM   82    O OD1 . ASN A 1 14  ? -36.858 24.790  40.809  1.00 38.27  ? 10  ASN A OD1 1 
ATOM   83    N ND2 . ASN A 1 14  ? -36.783 22.774  41.803  1.00 29.16  ? 10  ASN A ND2 1 
ATOM   84    N N   . ASN A 1 15  ? -38.690 26.823  42.538  1.00 42.33  ? 11  ASN A N   1 
ATOM   85    C CA  . ASN A 1 15  ? -38.178 28.153  42.898  1.00 47.19  ? 11  ASN A CA  1 
ATOM   86    C C   . ASN A 1 15  ? -36.652 28.299  42.780  1.00 42.53  ? 11  ASN A C   1 
ATOM   87    O O   . ASN A 1 15  ? -36.087 29.298  43.232  1.00 42.93  ? 11  ASN A O   1 
ATOM   88    C CB  . ASN A 1 15  ? -38.655 28.528  44.313  1.00 52.35  ? 11  ASN A CB  1 
ATOM   89    C CG  . ASN A 1 15  ? -38.150 27.581  45.380  1.00 60.70  ? 11  ASN A CG  1 
ATOM   90    O OD1 . ASN A 1 15  ? -37.570 26.528  45.076  1.00 64.54  ? 11  ASN A OD1 1 
ATOM   91    N ND2 . ASN A 1 15  ? -38.380 27.957  46.646  1.00 73.33  ? 11  ASN A ND2 1 
ATOM   92    N N   . SER A 1 16  ? -36.003 27.320  42.150  1.00 37.91  ? 12  SER A N   1 
ATOM   93    C CA  . SER A 1 16  ? -34.542 27.285  42.042  1.00 31.36  ? 12  SER A CA  1 
ATOM   94    C C   . SER A 1 16  ? -33.983 28.401  41.156  1.00 29.37  ? 12  SER A C   1 
ATOM   95    O O   . SER A 1 16  ? -34.580 28.762  40.144  1.00 27.44  ? 12  SER A O   1 
ATOM   96    C CB  . SER A 1 16  ? -34.081 25.933  41.499  1.00 29.38  ? 12  SER A CB  1 
ATOM   97    O OG  . SER A 1 16  ? -32.665 25.848  41.468  1.00 31.44  ? 12  SER A OG  1 
ATOM   98    N N   . THR A 1 17  ? -32.842 28.949  41.571  1.00 28.70  ? 13  THR A N   1 
ATOM   99    C CA  . THR A 1 17  ? -32.121 29.967  40.809  1.00 29.44  ? 13  THR A CA  1 
ATOM   100   C C   . THR A 1 17  ? -30.742 29.456  40.368  1.00 31.48  ? 13  THR A C   1 
ATOM   101   O O   . THR A 1 17  ? -29.949 30.208  39.801  1.00 29.00  ? 13  THR A O   1 
ATOM   102   C CB  . THR A 1 17  ? -31.934 31.255  41.642  1.00 29.15  ? 13  THR A CB  1 
ATOM   103   O OG1 . THR A 1 17  ? -31.262 30.940  42.869  1.00 26.34  ? 13  THR A OG1 1 
ATOM   104   C CG2 . THR A 1 17  ? -33.283 31.912  41.947  1.00 25.74  ? 13  THR A CG2 1 
ATOM   105   N N   . GLU A 1 18  ? -30.471 28.175  40.620  1.00 35.38  ? 14  GLU A N   1 
ATOM   106   C CA  . GLU A 1 18  ? -29.204 27.556  40.239  1.00 37.51  ? 14  GLU A CA  1 
ATOM   107   C C   . GLU A 1 18  ? -28.997 27.664  38.730  1.00 33.66  ? 14  GLU A C   1 
ATOM   108   O O   . GLU A 1 18  ? -29.897 27.350  37.951  1.00 28.65  ? 14  GLU A O   1 
ATOM   109   C CB  . GLU A 1 18  ? -29.170 26.080  40.658  1.00 45.85  ? 14  GLU A CB  1 
ATOM   110   C CG  . GLU A 1 18  ? -29.235 25.832  42.162  1.00 52.40  ? 14  GLU A CG  1 
ATOM   111   C CD  . GLU A 1 18  ? -28.013 26.340  42.910  1.00 62.26  ? 14  GLU A CD  1 
ATOM   112   O OE1 . GLU A 1 18  ? -26.882 26.148  42.414  1.00 69.42  ? 14  GLU A OE1 1 
ATOM   113   O OE2 . GLU A 1 18  ? -28.184 26.922  44.004  1.00 65.47  ? 14  GLU A OE2 1 
ATOM   114   N N   . GLN A 1 19  ? -27.813 28.123  38.334  1.00 33.11  ? 15  GLN A N   1 
ATOM   115   C CA  . GLN A 1 19  ? -27.484 28.334  36.927  1.00 31.20  ? 15  GLN A CA  1 
ATOM   116   C C   . GLN A 1 19  ? -26.443 27.330  36.453  1.00 28.55  ? 15  GLN A C   1 
ATOM   117   O O   . GLN A 1 19  ? -25.523 26.970  37.184  1.00 31.78  ? 15  GLN A O   1 
ATOM   118   C CB  . GLN A 1 19  ? -26.970 29.758  36.694  1.00 31.17  ? 15  GLN A CB  1 
ATOM   119   C CG  . GLN A 1 19  ? -28.063 30.807  36.584  1.00 30.22  ? 15  GLN A CG  1 
ATOM   120   C CD  . GLN A 1 19  ? -27.532 32.165  36.168  1.00 29.29  ? 15  GLN A CD  1 
ATOM   121   O OE1 . GLN A 1 19  ? -26.323 32.396  36.147  1.00 30.49  ? 15  GLN A OE1 1 
ATOM   122   N NE2 . GLN A 1 19  ? -28.437 33.070  35.831  1.00 27.28  ? 15  GLN A NE2 1 
ATOM   123   N N   . VAL A 1 20  ? -26.597 26.898  35.209  1.00 28.61  ? 16  VAL A N   1 
ATOM   124   C CA  . VAL A 1 20  ? -25.711 25.925  34.594  1.00 26.93  ? 16  VAL A CA  1 
ATOM   125   C C   . VAL A 1 20  ? -25.301 26.484  33.238  1.00 27.65  ? 16  VAL A C   1 
ATOM   126   O O   . VAL A 1 20  ? -26.001 27.328  32.671  1.00 27.60  ? 16  VAL A O   1 
ATOM   127   C CB  . VAL A 1 20  ? -26.441 24.575  34.430  1.00 26.91  ? 16  VAL A CB  1 
ATOM   128   C CG1 . VAL A 1 20  ? -26.701 24.251  32.965  1.00 27.55  ? 16  VAL A CG1 1 
ATOM   129   C CG2 . VAL A 1 20  ? -25.652 23.462  35.087  1.00 26.58  ? 16  VAL A CG2 1 
ATOM   130   N N   . ASP A 1 21  ? -24.160 26.038  32.726  1.00 30.74  ? 17  ASP A N   1 
ATOM   131   C CA  . ASP A 1 21  ? -23.696 26.462  31.406  1.00 31.98  ? 17  ASP A CA  1 
ATOM   132   C C   . ASP A 1 21  ? -23.673 25.291  30.433  1.00 27.07  ? 17  ASP A C   1 
ATOM   133   O O   . ASP A 1 21  ? -23.359 24.163  30.803  1.00 28.75  ? 17  ASP A O   1 
ATOM   134   C CB  . ASP A 1 21  ? -22.310 27.102  31.506  1.00 38.12  ? 17  ASP A CB  1 
ATOM   135   C CG  . ASP A 1 21  ? -22.372 28.555  31.932  1.00 45.82  ? 17  ASP A CG  1 
ATOM   136   O OD1 . ASP A 1 21  ? -22.691 28.807  33.110  1.00 52.55  ? 17  ASP A OD1 1 
ATOM   137   O OD2 . ASP A 1 21  ? -22.101 29.442  31.091  1.00 51.95  ? 17  ASP A OD2 1 
ATOM   138   N N   . THR A 1 22  ? -24.009 25.586  29.188  1.00 23.32  ? 18  THR A N   1 
ATOM   139   C CA  . THR A 1 22  ? -24.037 24.614  28.111  1.00 23.74  ? 18  THR A CA  1 
ATOM   140   C C   . THR A 1 22  ? -22.980 25.032  27.088  1.00 24.35  ? 18  THR A C   1 
ATOM   141   O O   . THR A 1 22  ? -22.518 26.172  27.097  1.00 22.31  ? 18  THR A O   1 
ATOM   142   C CB  . THR A 1 22  ? -25.449 24.577  27.485  1.00 25.28  ? 18  THR A CB  1 
ATOM   143   O OG1 . THR A 1 22  ? -26.352 23.917  28.384  1.00 28.74  ? 18  THR A OG1 1 
ATOM   144   C CG2 . THR A 1 22  ? -25.484 23.868  26.155  1.00 25.74  ? 18  THR A CG2 1 
ATOM   145   N N   . ILE A 1 23  ? -22.582 24.098  26.228  1.00 24.61  ? 19  ILE A N   1 
ATOM   146   C CA  . ILE A 1 23  ? -21.613 24.375  25.170  1.00 23.12  ? 19  ILE A CA  1 
ATOM   147   C C   . ILE A 1 23  ? -22.122 25.485  24.237  1.00 21.75  ? 19  ILE A C   1 
ATOM   148   O O   . ILE A 1 23  ? -21.331 26.261  23.709  1.00 19.44  ? 19  ILE A O   1 
ATOM   149   C CB  . ILE A 1 23  ? -21.253 23.073  24.394  1.00 25.06  ? 19  ILE A CB  1 
ATOM   150   C CG1 . ILE A 1 23  ? -19.734 22.954  24.192  1.00 26.78  ? 19  ILE A CG1 1 
ATOM   151   C CG2 . ILE A 1 23  ? -22.010 22.966  23.080  1.00 25.45  ? 19  ILE A CG2 1 
ATOM   152   C CD1 . ILE A 1 23  ? -19.150 23.982  23.259  1.00 27.61  ? 19  ILE A CD1 1 
ATOM   153   N N   . MET A 1 24  ? -23.443 25.578  24.080  1.00 23.47  ? 20  MET A N   1 
ATOM   154   C CA  . MET A 1 24  ? -24.082 26.580  23.215  1.00 24.10  ? 20  MET A CA  1 
ATOM   155   C C   . MET A 1 24  ? -24.868 27.684  23.940  1.00 24.51  ? 20  MET A C   1 
ATOM   156   O O   . MET A 1 24  ? -25.230 28.685  23.322  1.00 22.80  ? 20  MET A O   1 
ATOM   157   C CB  . MET A 1 24  ? -25.025 25.877  22.244  1.00 25.79  ? 20  MET A CB  1 
ATOM   158   C CG  . MET A 1 24  ? -24.312 25.063  21.181  1.00 27.23  ? 20  MET A CG  1 
ATOM   159   S SD  . MET A 1 24  ? -25.362 24.825  19.740  1.00 32.04  ? 20  MET A SD  1 
ATOM   160   C CE  . MET A 1 24  ? -26.617 23.754  20.446  1.00 31.63  ? 20  MET A CE  1 
ATOM   161   N N   . GLU A 1 25  ? -25.146 27.504  25.231  1.00 27.58  ? 21  GLU A N   1 
ATOM   162   C CA  . GLU A 1 25  ? -25.923 28.481  25.999  1.00 30.00  ? 21  GLU A CA  1 
ATOM   163   C C   . GLU A 1 25  ? -25.265 28.802  27.331  1.00 27.73  ? 21  GLU A C   1 
ATOM   164   O O   . GLU A 1 25  ? -24.806 27.913  28.043  1.00 24.76  ? 21  GLU A O   1 
ATOM   165   C CB  . GLU A 1 25  ? -27.331 27.959  26.279  1.00 33.21  ? 21  GLU A CB  1 
ATOM   166   C CG  . GLU A 1 25  ? -28.234 27.843  25.068  1.00 37.66  ? 21  GLU A CG  1 
ATOM   167   C CD  . GLU A 1 25  ? -29.541 27.153  25.419  1.00 43.53  ? 21  GLU A CD  1 
ATOM   168   O OE1 . GLU A 1 25  ? -30.225 27.603  26.358  1.00 41.14  ? 21  GLU A OE1 1 
ATOM   169   O OE2 . GLU A 1 25  ? -29.890 26.147  24.773  1.00 49.10  ? 21  GLU A OE2 1 
ATOM   170   N N   . LYS A 1 26  ? -25.253 30.082  27.672  1.00 30.46  ? 22  LYS A N   1 
ATOM   171   C CA  . LYS A 1 26  ? -24.735 30.536  28.949  1.00 32.94  ? 22  LYS A CA  1 
ATOM   172   C C   . LYS A 1 26  ? -25.874 30.753  29.937  1.00 28.67  ? 22  LYS A C   1 
ATOM   173   O O   . LYS A 1 26  ? -26.995 31.062  29.541  1.00 28.07  ? 22  LYS A O   1 
ATOM   174   C CB  . LYS A 1 26  ? -24.000 31.864  28.751  1.00 37.34  ? 22  LYS A CB  1 
ATOM   175   C CG  . LYS A 1 26  ? -22.813 31.799  27.783  1.00 41.51  ? 22  LYS A CG  1 
ATOM   176   C CD  . LYS A 1 26  ? -21.476 31.631  28.487  1.00 44.55  ? 22  LYS A CD  1 
ATOM   177   C CE  . LYS A 1 26  ? -20.329 31.493  27.484  1.00 47.21  ? 22  LYS A CE  1 
ATOM   178   N NZ  . LYS A 1 26  ? -19.068 32.088  28.009  1.00 48.08  ? 22  LYS A NZ  1 
ATOM   179   N N   . ASN A 1 27  ? -25.569 30.598  31.222  1.00 28.75  ? 23  ASN A N   1 
ATOM   180   C CA  . ASN A 1 27  ? -26.474 30.964  32.313  1.00 27.92  ? 23  ASN A CA  1 
ATOM   181   C C   . ASN A 1 27  ? -27.910 30.505  32.111  1.00 25.38  ? 23  ASN A C   1 
ATOM   182   O O   . ASN A 1 27  ? -28.834 31.314  32.005  1.00 23.77  ? 23  ASN A O   1 
ATOM   183   C CB  . ASN A 1 27  ? -26.397 32.473  32.564  1.00 29.82  ? 23  ASN A CB  1 
ATOM   184   C CG  . ASN A 1 27  ? -25.056 32.895  33.114  1.00 33.93  ? 23  ASN A CG  1 
ATOM   185   O OD1 . ASN A 1 27  ? -24.135 32.080  33.256  1.00 33.80  ? 23  ASN A OD1 1 
ATOM   186   N ND2 . ASN A 1 27  ? -24.942 34.178  33.430  1.00 43.57  ? 23  ASN A ND2 1 
ATOM   187   N N   . VAL A 1 28  ? -28.071 29.186  32.047  1.00 23.73  ? 24  VAL A N   1 
ATOM   188   C CA  . VAL A 1 28  ? -29.378 28.556  31.934  1.00 21.72  ? 24  VAL A CA  1 
ATOM   189   C C   . VAL A 1 28  ? -29.867 28.174  33.328  1.00 21.45  ? 24  VAL A C   1 
ATOM   190   O O   . VAL A 1 28  ? -29.222 27.385  34.019  1.00 20.24  ? 24  VAL A O   1 
ATOM   191   C CB  . VAL A 1 28  ? -29.310 27.296  31.058  1.00 19.46  ? 24  VAL A CB  1 
ATOM   192   C CG1 . VAL A 1 28  ? -30.677 26.633  30.984  1.00 18.85  ? 24  VAL A CG1 1 
ATOM   193   C CG2 . VAL A 1 28  ? -28.800 27.648  29.674  1.00 18.73  ? 24  VAL A CG2 1 
ATOM   194   N N   . THR A 1 29  ? -30.994 28.747  33.743  1.00 21.93  ? 25  THR A N   1 
ATOM   195   C CA  . THR A 1 29  ? -31.562 28.441  35.047  1.00 23.05  ? 25  THR A CA  1 
ATOM   196   C C   . THR A 1 29  ? -32.121 27.033  35.001  1.00 22.15  ? 25  THR A C   1 
ATOM   197   O O   . THR A 1 29  ? -32.694 26.618  33.999  1.00 23.21  ? 25  THR A O   1 
ATOM   198   C CB  . THR A 1 29  ? -32.665 29.437  35.454  1.00 24.92  ? 25  THR A CB  1 
ATOM   199   O OG1 . THR A 1 29  ? -32.175 30.769  35.306  1.00 30.86  ? 25  THR A OG1 1 
ATOM   200   C CG2 . THR A 1 29  ? -33.093 29.215  36.905  1.00 22.78  ? 25  THR A CG2 1 
ATOM   201   N N   . VAL A 1 30  ? -31.956 26.309  36.098  1.00 23.13  ? 26  VAL A N   1 
ATOM   202   C CA  . VAL A 1 30  ? -32.234 24.880  36.121  1.00 22.99  ? 26  VAL A CA  1 
ATOM   203   C C   . VAL A 1 30  ? -32.839 24.452  37.470  1.00 22.64  ? 26  VAL A C   1 
ATOM   204   O O   . VAL A 1 30  ? -32.613 25.100  38.495  1.00 23.02  ? 26  VAL A O   1 
ATOM   205   C CB  . VAL A 1 30  ? -30.952 24.101  35.732  1.00 22.08  ? 26  VAL A CB  1 
ATOM   206   C CG1 . VAL A 1 30  ? -30.564 23.076  36.783  1.00 22.50  ? 26  VAL A CG1 1 
ATOM   207   C CG2 . VAL A 1 30  ? -31.124 23.465  34.359  1.00 20.21  ? 26  VAL A CG2 1 
ATOM   208   N N   . THR A 1 31  ? -33.639 23.387  37.452  1.00 22.45  ? 27  THR A N   1 
ATOM   209   C CA  . THR A 1 31  ? -34.394 22.963  38.642  1.00 21.46  ? 27  THR A CA  1 
ATOM   210   C C   . THR A 1 31  ? -33.511 22.302  39.696  1.00 22.91  ? 27  THR A C   1 
ATOM   211   O O   . THR A 1 31  ? -33.699 22.538  40.889  1.00 23.08  ? 27  THR A O   1 
ATOM   212   C CB  . THR A 1 31  ? -35.596 22.046  38.313  1.00 21.47  ? 27  THR A CB  1 
ATOM   213   O OG1 . THR A 1 31  ? -35.157 20.819  37.722  1.00 21.09  ? 27  THR A OG1 1 
ATOM   214   C CG2 . THR A 1 31  ? -36.562 22.740  37.371  1.00 21.83  ? 27  THR A CG2 1 
ATOM   215   N N   . HIS A 1 32  ? -32.556 21.482  39.254  1.00 24.46  ? 28  HIS A N   1 
ATOM   216   C CA  . HIS A 1 32  ? -31.584 20.845  40.144  1.00 26.24  ? 28  HIS A CA  1 
ATOM   217   C C   . HIS A 1 32  ? -30.230 20.785  39.497  1.00 26.99  ? 28  HIS A C   1 
ATOM   218   O O   . HIS A 1 32  ? -30.117 20.609  38.281  1.00 27.62  ? 28  HIS A O   1 
ATOM   219   C CB  . HIS A 1 32  ? -32.048 19.451  40.558  1.00 29.68  ? 28  HIS A CB  1 
ATOM   220   C CG  . HIS A 1 32  ? -33.061 19.467  41.673  1.00 38.52  ? 28  HIS A CG  1 
ATOM   221   N ND1 . HIS A 1 32  ? -32.715 19.410  42.976  1.00 40.31  ? 28  HIS A ND1 1 
ATOM   222   C CD2 . HIS A 1 32  ? -34.447 19.572  41.636  1.00 39.82  ? 28  HIS A CD2 1 
ATOM   223   C CE1 . HIS A 1 32  ? -33.831 19.462  43.733  1.00 41.13  ? 28  HIS A CE1 1 
ATOM   224   N NE2 . HIS A 1 32  ? -34.889 19.563  42.910  1.00 37.65  ? 28  HIS A NE2 1 
ATOM   225   N N   . ALA A 1 33  ? -29.190 20.944  40.307  1.00 26.27  ? 29  ALA A N   1 
ATOM   226   C CA  . ALA A 1 33  ? -27.822 20.860  39.824  1.00 27.59  ? 29  ALA A CA  1 
ATOM   227   C C   . ALA A 1 33  ? -26.891 20.295  40.891  1.00 29.21  ? 29  ALA A C   1 
ATOM   228   O O   . ALA A 1 33  ? -27.145 20.425  42.090  1.00 29.25  ? 29  ALA A O   1 
ATOM   229   C CB  . ALA A 1 33  ? -27.337 22.234  39.381  1.00 28.15  ? 29  ALA A CB  1 
ATOM   230   N N   . GLN A 1 34  ? -25.810 19.670  40.435  1.00 31.59  ? 30  GLN A N   1 
ATOM   231   C CA  . GLN A 1 34  ? -24.803 19.109  41.321  1.00 31.43  ? 30  GLN A CA  1 
ATOM   232   C C   . GLN A 1 34  ? -23.419 19.597  40.909  1.00 29.75  ? 30  GLN A C   1 
ATOM   233   O O   . GLN A 1 34  ? -23.023 19.432  39.761  1.00 27.40  ? 30  GLN A O   1 
ATOM   234   C CB  . GLN A 1 34  ? -24.867 17.581  41.280  1.00 34.52  ? 30  GLN A CB  1 
ATOM   235   C CG  . GLN A 1 34  ? -24.154 16.900  42.442  1.00 36.89  ? 30  GLN A CG  1 
ATOM   236   C CD  . GLN A 1 34  ? -24.543 15.442  42.604  1.00 40.26  ? 30  GLN A CD  1 
ATOM   237   O OE1 . GLN A 1 34  ? -25.647 15.029  42.232  1.00 42.00  ? 30  GLN A OE1 1 
ATOM   238   N NE2 . GLN A 1 34  ? -23.638 14.654  43.178  1.00 40.68  ? 30  GLN A NE2 1 
ATOM   239   N N   . ASP A 1 35  ? -22.699 20.214  41.845  1.00 29.70  ? 31  ASP A N   1 
ATOM   240   C CA  . ASP A 1 35  ? -21.333 20.670  41.590  1.00 27.98  ? 31  ASP A CA  1 
ATOM   241   C C   . ASP A 1 35  ? -20.396 19.487  41.761  1.00 26.75  ? 31  ASP A C   1 
ATOM   242   O O   . ASP A 1 35  ? -20.509 18.732  42.717  1.00 24.78  ? 31  ASP A O   1 
ATOM   243   C CB  . ASP A 1 35  ? -20.936 21.811  42.537  1.00 28.33  ? 31  ASP A CB  1 
ATOM   244   C CG  . ASP A 1 35  ? -19.785 22.666  41.993  1.00 30.19  ? 31  ASP A CG  1 
ATOM   245   O OD1 . ASP A 1 35  ? -18.981 22.172  41.175  1.00 28.69  ? 31  ASP A OD1 1 
ATOM   246   O OD2 . ASP A 1 35  ? -19.678 23.845  42.392  1.00 32.68  ? 31  ASP A OD2 1 
ATOM   247   N N   . ILE A 1 36  ? -19.469 19.338  40.822  1.00 29.40  ? 32  ILE A N   1 
ATOM   248   C CA  . ILE A 1 36  ? -18.574 18.193  40.776  1.00 29.03  ? 32  ILE A CA  1 
ATOM   249   C C   . ILE A 1 36  ? -17.141 18.604  41.175  1.00 27.84  ? 32  ILE A C   1 
ATOM   250   O O   . ILE A 1 36  ? -16.196 17.828  41.022  1.00 29.51  ? 32  ILE A O   1 
ATOM   251   C CB  . ILE A 1 36  ? -18.655 17.563  39.352  1.00 32.47  ? 32  ILE A CB  1 
ATOM   252   C CG1 . ILE A 1 36  ? -18.767 16.042  39.416  1.00 36.29  ? 32  ILE A CG1 1 
ATOM   253   C CG2 . ILE A 1 36  ? -17.513 18.001  38.438  1.00 31.76  ? 32  ILE A CG2 1 
ATOM   254   C CD1 . ILE A 1 36  ? -20.152 15.587  39.828  1.00 37.75  ? 32  ILE A CD1 1 
ATOM   255   N N   . LEU A 1 37  ? -17.002 19.817  41.713  1.00 26.09  ? 33  LEU A N   1 
ATOM   256   C CA  . LEU A 1 37  ? -15.716 20.381  42.113  1.00 26.63  ? 33  LEU A CA  1 
ATOM   257   C C   . LEU A 1 37  ? -15.675 20.570  43.627  1.00 28.13  ? 33  LEU A C   1 
ATOM   258   O O   . LEU A 1 37  ? -16.468 21.331  44.180  1.00 28.29  ? 33  LEU A O   1 
ATOM   259   C CB  . LEU A 1 37  ? -15.502 21.733  41.415  1.00 26.23  ? 33  LEU A CB  1 
ATOM   260   C CG  . LEU A 1 37  ? -14.232 22.514  41.777  1.00 25.83  ? 33  LEU A CG  1 
ATOM   261   C CD1 . LEU A 1 37  ? -12.988 21.715  41.424  1.00 25.00  ? 33  LEU A CD1 1 
ATOM   262   C CD2 . LEU A 1 37  ? -14.205 23.868  41.087  1.00 26.66  ? 33  LEU A CD2 1 
ATOM   263   N N   . GLU A 1 38  ? -14.744 19.890  44.290  1.00 29.73  ? 34  GLU A N   1 
ATOM   264   C CA  . GLU A 1 38  ? -14.585 20.015  45.731  1.00 29.88  ? 34  GLU A CA  1 
ATOM   265   C C   . GLU A 1 38  ? -13.899 21.335  46.077  1.00 32.12  ? 34  GLU A C   1 
ATOM   266   O O   . GLU A 1 38  ? -12.835 21.644  45.543  1.00 33.19  ? 34  GLU A O   1 
ATOM   267   C CB  . GLU A 1 38  ? -13.774 18.846  46.292  1.00 29.97  ? 34  GLU A CB  1 
ATOM   268   C CG  . GLU A 1 38  ? -13.799 18.749  47.812  1.00 31.02  ? 34  GLU A CG  1 
ATOM   269   C CD  . GLU A 1 38  ? -15.210 18.716  48.370  1.00 32.18  ? 34  GLU A CD  1 
ATOM   270   O OE1 . GLU A 1 38  ? -15.938 17.739  48.102  1.00 35.39  ? 34  GLU A OE1 1 
ATOM   271   O OE2 . GLU A 1 38  ? -15.602 19.676  49.065  1.00 32.40  ? 34  GLU A OE2 1 
ATOM   272   N N   . LYS A 1 39  ? -14.518 22.107  46.969  1.00 33.45  ? 35  LYS A N   1 
ATOM   273   C CA  . LYS A 1 39  ? -14.025 23.436  47.334  1.00 34.28  ? 35  LYS A CA  1 
ATOM   274   C C   . LYS A 1 39  ? -13.723 23.578  48.826  1.00 32.74  ? 35  LYS A C   1 
ATOM   275   O O   . LYS A 1 39  ? -13.108 24.563  49.238  1.00 31.92  ? 35  LYS A O   1 
ATOM   276   C CB  . LYS A 1 39  ? -15.061 24.500  46.924  1.00 38.52  ? 35  LYS A CB  1 
ATOM   277   C CG  . LYS A 1 39  ? -15.316 24.653  45.423  1.00 42.59  ? 35  LYS A CG  1 
ATOM   278   C CD  . LYS A 1 39  ? -16.824 24.703  45.098  1.00 47.64  ? 35  LYS A CD  1 
ATOM   279   C CE  . LYS A 1 39  ? -17.384 26.118  44.939  1.00 50.48  ? 35  LYS A CE  1 
ATOM   280   N NZ  . LYS A 1 39  ? -17.596 26.798  46.249  1.00 55.52  ? 35  LYS A NZ  1 
ATOM   281   N N   . THR A 1 40  ? -14.134 22.601  49.635  1.00 36.61  ? 36  THR A N   1 
ATOM   282   C CA  . THR A 1 40  ? -14.089 22.738  51.089  1.00 37.91  ? 36  THR A CA  1 
ATOM   283   C C   . THR A 1 40  ? -13.046 21.822  51.745  1.00 36.84  ? 36  THR A C   1 
ATOM   284   O O   . THR A 1 40  ? -12.934 20.640  51.411  1.00 33.83  ? 36  THR A O   1 
ATOM   285   C CB  . THR A 1 40  ? -15.478 22.473  51.714  1.00 39.12  ? 36  THR A CB  1 
ATOM   286   O OG1 . THR A 1 40  ? -15.450 22.803  53.108  1.00 49.42  ? 36  THR A OG1 1 
ATOM   287   C CG2 . THR A 1 40  ? -15.895 21.022  51.552  1.00 38.57  ? 36  THR A CG2 1 
ATOM   288   N N   . HIS A 1 41  ? -12.292 22.391  52.683  1.00 33.89  ? 37  HIS A N   1 
ATOM   289   C CA  . HIS A 1 41  ? -11.371 21.631  53.526  1.00 31.80  ? 37  HIS A CA  1 
ATOM   290   C C   . HIS A 1 41  ? -11.674 21.926  54.968  1.00 32.01  ? 37  HIS A C   1 
ATOM   291   O O   . HIS A 1 41  ? -12.329 22.921  55.272  1.00 32.27  ? 37  HIS A O   1 
ATOM   292   C CB  . HIS A 1 41  ? -9.922  21.981  53.197  1.00 30.52  ? 37  HIS A CB  1 
ATOM   293   C CG  . HIS A 1 41  ? -9.590  23.445  53.369  1.00 29.13  ? 37  HIS A CG  1 
ATOM   294   N ND1 . HIS A 1 41  ? -9.157  23.957  54.536  1.00 27.53  ? 37  HIS A ND1 1 
ATOM   295   C CD2 . HIS A 1 41  ? -9.648  24.509  52.470  1.00 28.79  ? 37  HIS A CD2 1 
ATOM   296   C CE1 . HIS A 1 41  ? -8.952  25.281  54.397  1.00 27.36  ? 37  HIS A CE1 1 
ATOM   297   N NE2 . HIS A 1 41  ? -9.255  25.619  53.133  1.00 27.95  ? 37  HIS A NE2 1 
ATOM   298   N N   . ASN A 1 42  ? -11.195 21.070  55.871  1.00 31.76  ? 38  ASN A N   1 
ATOM   299   C CA  . ASN A 1 42  ? -11.504 21.199  57.303  1.00 30.31  ? 38  ASN A CA  1 
ATOM   300   C C   . ASN A 1 42  ? -10.549 22.114  58.078  1.00 31.29  ? 38  ASN A C   1 
ATOM   301   O O   . ASN A 1 42  ? -10.700 22.290  59.287  1.00 34.05  ? 38  ASN A O   1 
ATOM   302   C CB  . ASN A 1 42  ? -11.589 19.814  57.970  1.00 28.84  ? 38  ASN A CB  1 
ATOM   303   C CG  . ASN A 1 42  ? -10.231 19.175  58.209  1.00 31.06  ? 38  ASN A CG  1 
ATOM   304   O OD1 . ASN A 1 42  ? -9.186  19.741  57.885  1.00 29.67  ? 38  ASN A OD1 1 
ATOM   305   N ND2 . ASN A 1 42  ? -10.244 17.988  58.807  1.00 31.97  ? 38  ASN A ND2 1 
ATOM   306   N N   . GLY A 1 43  ? -9.559  22.670  57.387  1.00 29.60  ? 39  GLY A N   1 
ATOM   307   C CA  . GLY A 1 43  ? -8.661  23.659  57.978  1.00 28.63  ? 39  GLY A CA  1 
ATOM   308   C C   . GLY A 1 43  ? -7.648  23.109  58.968  1.00 28.56  ? 39  GLY A C   1 
ATOM   309   O O   . GLY A 1 43  ? -7.044  23.876  59.718  1.00 30.08  ? 39  GLY A O   1 
ATOM   310   N N   . LYS A 1 44  ? -7.444  21.793  58.970  1.00 28.25  ? 40  LYS A N   1 
ATOM   311   C CA  . LYS A 1 44  ? -6.554  21.155  59.944  1.00 29.75  ? 40  LYS A CA  1 
ATOM   312   C C   . LYS A 1 44  ? -5.718  20.030  59.321  1.00 28.62  ? 40  LYS A C   1 
ATOM   313   O O   . LYS A 1 44  ? -6.106  19.435  58.320  1.00 29.54  ? 40  LYS A O   1 
ATOM   314   C CB  . LYS A 1 44  ? -7.368  20.626  61.143  1.00 30.66  ? 40  LYS A CB  1 
ATOM   315   C CG  . LYS A 1 44  ? -7.958  21.745  62.042  1.00 32.46  ? 40  LYS A CG  1 
ATOM   316   C CD  . LYS A 1 44  ? -7.952  21.444  63.548  1.00 36.50  ? 40  LYS A CD  1 
ATOM   317   C CE  . LYS A 1 44  ? -7.777  22.679  64.426  1.00 39.95  ? 40  LYS A CE  1 
ATOM   318   N NZ  . LYS A 1 44  ? -8.034  22.387  65.868  1.00 39.07  ? 40  LYS A NZ  1 
ATOM   319   N N   . LEU A 1 45  ? -4.557  19.766  59.919  1.00 28.96  ? 41  LEU A N   1 
ATOM   320   C CA  . LEU A 1 45  ? -3.721  18.626  59.550  1.00 28.88  ? 41  LEU A CA  1 
ATOM   321   C C   . LEU A 1 45  ? -4.251  17.378  60.243  1.00 29.72  ? 41  LEU A C   1 
ATOM   322   O O   . LEU A 1 45  ? -4.688  17.446  61.388  1.00 32.57  ? 41  LEU A O   1 
ATOM   323   C CB  . LEU A 1 45  ? -2.259  18.873  59.945  1.00 29.19  ? 41  LEU A CB  1 
ATOM   324   C CG  . LEU A 1 45  ? -1.622  20.165  59.405  1.00 29.58  ? 41  LEU A CG  1 
ATOM   325   C CD1 . LEU A 1 45  ? -0.118  20.177  59.645  1.00 26.34  ? 41  LEU A CD1 1 
ATOM   326   C CD2 . LEU A 1 45  ? -1.911  20.350  57.919  1.00 29.29  ? 41  LEU A CD2 1 
ATOM   327   N N   . CYS A 1 46  ? -4.199  16.241  59.554  1.00 30.11  ? 42  CYS A N   1 
ATOM   328   C CA  . CYS A 1 46  ? -4.853  15.016  60.022  1.00 31.09  ? 42  CYS A CA  1 
ATOM   329   C C   . CYS A 1 46  ? -3.990  13.780  59.822  1.00 32.27  ? 42  CYS A C   1 
ATOM   330   O O   . CYS A 1 46  ? -2.935  13.839  59.190  1.00 36.55  ? 42  CYS A O   1 
ATOM   331   C CB  . CYS A 1 46  ? -6.155  14.799  59.258  1.00 30.46  ? 42  CYS A CB  1 
ATOM   332   S SG  . CYS A 1 46  ? -7.438  16.050  59.457  1.00 32.29  ? 42  CYS A SG  1 
ATOM   333   N N   . ASP A 1 47  ? -4.468  12.656  60.353  1.00 33.47  ? 43  ASP A N   1 
ATOM   334   C CA  . ASP A 1 47  ? -3.880  11.347  60.079  1.00 35.47  ? 43  ASP A CA  1 
ATOM   335   C C   . ASP A 1 47  ? -4.153  10.972  58.628  1.00 34.60  ? 43  ASP A C   1 
ATOM   336   O O   . ASP A 1 47  ? -5.103  11.477  58.022  1.00 35.75  ? 43  ASP A O   1 
ATOM   337   C CB  . ASP A 1 47  ? -4.474  10.276  60.999  1.00 38.81  ? 43  ASP A CB  1 
ATOM   338   C CG  . ASP A 1 47  ? -4.225  10.556  62.475  1.00 46.25  ? 43  ASP A CG  1 
ATOM   339   O OD1 . ASP A 1 47  ? -3.645  11.614  62.805  1.00 49.75  ? 43  ASP A OD1 1 
ATOM   340   O OD2 . ASP A 1 47  ? -4.614  9.712   63.313  1.00 51.18  ? 43  ASP A OD2 1 
ATOM   341   N N   . LEU A 1 48  ? -3.320  10.092  58.080  1.00 31.45  ? 44  LEU A N   1 
ATOM   342   C CA  . LEU A 1 48  ? -3.450  9.653   56.694  1.00 32.29  ? 44  LEU A CA  1 
ATOM   343   C C   . LEU A 1 48  ? -3.630  8.134   56.670  1.00 31.84  ? 44  LEU A C   1 
ATOM   344   O O   . LEU A 1 48  ? -2.678  7.387   56.895  1.00 36.12  ? 44  LEU A O   1 
ATOM   345   C CB  . LEU A 1 48  ? -2.215  10.083  55.892  1.00 34.43  ? 44  LEU A CB  1 
ATOM   346   C CG  . LEU A 1 48  ? -2.407  10.356  54.401  1.00 36.93  ? 44  LEU A CG  1 
ATOM   347   C CD1 . LEU A 1 48  ? -1.186  11.078  53.847  1.00 40.01  ? 44  LEU A CD1 1 
ATOM   348   C CD2 . LEU A 1 48  ? -2.653  9.072   53.625  1.00 39.02  ? 44  LEU A CD2 1 
ATOM   349   N N   . ASN A 1 49  ? -4.862  7.693   56.414  1.00 33.80  ? 45  ASN A N   1 
ATOM   350   C CA  . ASN A 1 49  ? -5.239  6.275   56.485  1.00 33.91  ? 45  ASN A CA  1 
ATOM   351   C C   . ASN A 1 49  ? -4.893  5.649   57.837  1.00 30.86  ? 45  ASN A C   1 
ATOM   352   O O   . ASN A 1 49  ? -4.293  4.573   57.904  1.00 29.51  ? 45  ASN A O   1 
ATOM   353   C CB  . ASN A 1 49  ? -4.605  5.481   55.337  1.00 36.80  ? 45  ASN A CB  1 
ATOM   354   C CG  . ASN A 1 49  ? -5.063  5.964   53.976  1.00 41.50  ? 45  ASN A CG  1 
ATOM   355   O OD1 . ASN A 1 49  ? -6.257  6.176   53.747  1.00 40.55  ? 45  ASN A OD1 1 
ATOM   356   N ND2 . ASN A 1 49  ? -4.114  6.136   53.059  1.00 46.47  ? 45  ASN A ND2 1 
ATOM   357   N N   . GLY A 1 50  ? -5.265  6.348   58.907  1.00 28.86  ? 46  GLY A N   1 
ATOM   358   C CA  . GLY A 1 50  ? -5.105  5.843   60.268  1.00 28.47  ? 46  GLY A CA  1 
ATOM   359   C C   . GLY A 1 50  ? -3.759  6.095   60.930  1.00 28.05  ? 46  GLY A C   1 
ATOM   360   O O   . GLY A 1 50  ? -3.588  5.774   62.106  1.00 28.54  ? 46  GLY A O   1 
ATOM   361   N N   . VAL A 1 51  ? -2.805  6.667   60.197  1.00 28.12  ? 47  VAL A N   1 
ATOM   362   C CA  . VAL A 1 51  ? -1.458  6.896   60.726  1.00 29.18  ? 47  VAL A CA  1 
ATOM   363   C C   . VAL A 1 51  ? -1.178  8.393   60.872  1.00 29.76  ? 47  VAL A C   1 
ATOM   364   O O   . VAL A 1 51  ? -1.445  9.178   59.963  1.00 28.15  ? 47  VAL A O   1 
ATOM   365   C CB  . VAL A 1 51  ? -0.385  6.257   59.821  1.00 28.22  ? 47  VAL A CB  1 
ATOM   366   C CG1 . VAL A 1 51  ? 0.982   6.333   60.479  1.00 27.23  ? 47  VAL A CG1 1 
ATOM   367   C CG2 . VAL A 1 51  ? -0.741  4.814   59.490  1.00 27.60  ? 47  VAL A CG2 1 
ATOM   368   N N   . LYS A 1 52  ? -0.621  8.773   62.020  1.00 31.17  ? 48  LYS A N   1 
ATOM   369   C CA  . LYS A 1 52  ? -0.423  10.185  62.364  1.00 31.87  ? 48  LYS A CA  1 
ATOM   370   C C   . LYS A 1 52  ? 0.793   10.714  61.615  1.00 27.62  ? 48  LYS A C   1 
ATOM   371   O O   . LYS A 1 52  ? 1.677   9.943   61.265  1.00 27.28  ? 48  LYS A O   1 
ATOM   372   C CB  . LYS A 1 52  ? -0.202  10.382  63.877  1.00 34.81  ? 48  LYS A CB  1 
ATOM   373   C CG  . LYS A 1 52  ? -0.550  9.186   64.762  1.00 39.33  ? 48  LYS A CG  1 
ATOM   374   C CD  . LYS A 1 52  ? -0.936  9.579   66.183  1.00 45.28  ? 48  LYS A CD  1 
ATOM   375   C CE  . LYS A 1 52  ? -2.452  9.692   66.361  1.00 44.63  ? 48  LYS A CE  1 
ATOM   376   N NZ  . LYS A 1 52  ? -2.820  10.273  67.682  1.00 42.03  ? 48  LYS A NZ  1 
ATOM   377   N N   . PRO A 1 53  ? 0.839   12.029  61.357  1.00 25.94  ? 49  PRO A N   1 
ATOM   378   C CA  . PRO A 1 53  ? 2.069   12.609  60.814  1.00 25.64  ? 49  PRO A CA  1 
ATOM   379   C C   . PRO A 1 53  ? 3.106   12.881  61.890  1.00 25.65  ? 49  PRO A C   1 
ATOM   380   O O   . PRO A 1 53  ? 2.759   13.053  63.057  1.00 27.69  ? 49  PRO A O   1 
ATOM   381   C CB  . PRO A 1 53  ? 1.599   13.936  60.219  1.00 26.20  ? 49  PRO A CB  1 
ATOM   382   C CG  . PRO A 1 53  ? 0.386   14.293  61.000  1.00 26.43  ? 49  PRO A CG  1 
ATOM   383   C CD  . PRO A 1 53  ? -0.273  12.995  61.364  1.00 24.88  ? 49  PRO A CD  1 
ATOM   384   N N   . LEU A 1 54  ? 4.371   12.922  61.488  1.00 27.42  ? 50  LEU A N   1 
ATOM   385   C CA  . LEU A 1 54  ? 5.453   13.375  62.357  1.00 26.71  ? 50  LEU A CA  1 
ATOM   386   C C   . LEU A 1 54  ? 5.531   14.899  62.263  1.00 28.59  ? 50  LEU A C   1 
ATOM   387   O O   . LEU A 1 54  ? 5.981   15.442  61.251  1.00 31.20  ? 50  LEU A O   1 
ATOM   388   C CB  . LEU A 1 54  ? 6.778   12.747  61.927  1.00 26.29  ? 50  LEU A CB  1 
ATOM   389   C CG  . LEU A 1 54  ? 8.036   13.130  62.710  1.00 26.56  ? 50  LEU A CG  1 
ATOM   390   C CD1 . LEU A 1 54  ? 7.940   12.622  64.143  1.00 26.10  ? 50  LEU A CD1 1 
ATOM   391   C CD2 . LEU A 1 54  ? 9.272   12.583  62.011  1.00 23.87  ? 50  LEU A CD2 1 
ATOM   392   N N   . ILE A 1 55  ? 5.068   15.579  63.308  1.00 28.47  ? 51  ILE A N   1 
ATOM   393   C CA  . ILE A 1 55  ? 5.040   17.041  63.342  1.00 28.82  ? 51  ILE A CA  1 
ATOM   394   C C   . ILE A 1 55  ? 6.233   17.578  64.129  1.00 30.35  ? 51  ILE A C   1 
ATOM   395   O O   . ILE A 1 55  ? 6.357   17.314  65.327  1.00 29.45  ? 51  ILE A O   1 
ATOM   396   C CB  . ILE A 1 55  ? 3.734   17.559  63.973  1.00 28.71  ? 51  ILE A CB  1 
ATOM   397   C CG1 . ILE A 1 55  ? 2.532   17.102  63.137  1.00 30.30  ? 51  ILE A CG1 1 
ATOM   398   C CG2 . ILE A 1 55  ? 3.753   19.076  64.078  1.00 26.33  ? 51  ILE A CG2 1 
ATOM   399   C CD1 . ILE A 1 55  ? 1.193   17.430  63.755  1.00 30.02  ? 51  ILE A CD1 1 
ATOM   400   N N   . LEU A 1 56  ? 7.103   18.320  63.438  1.00 33.84  ? 52  LEU A N   1 
ATOM   401   C CA  . LEU A 1 56  ? 8.305   18.921  64.031  1.00 34.89  ? 52  LEU A CA  1 
ATOM   402   C C   . LEU A 1 56  ? 8.143   20.431  64.314  1.00 39.93  ? 52  LEU A C   1 
ATOM   403   O O   . LEU A 1 56  ? 8.580   21.271  63.516  1.00 53.84  ? 52  LEU A O   1 
ATOM   404   C CB  . LEU A 1 56  ? 9.500   18.697  63.087  1.00 32.01  ? 52  LEU A CB  1 
ATOM   405   C CG  . LEU A 1 56  ? 9.784   17.268  62.626  1.00 30.00  ? 52  LEU A CG  1 
ATOM   406   C CD1 . LEU A 1 56  ? 10.858  17.238  61.545  1.00 29.11  ? 52  LEU A CD1 1 
ATOM   407   C CD2 . LEU A 1 56  ? 10.193  16.425  63.821  1.00 29.61  ? 52  LEU A CD2 1 
ATOM   408   N N   . LYS A 1 57  ? 7.524   20.761  65.451  1.00 43.29  ? 53  LYS A N   1 
ATOM   409   C CA  . LYS A 1 57  ? 7.249   22.159  65.846  1.00 45.63  ? 53  LYS A CA  1 
ATOM   410   C C   . LYS A 1 57  ? 8.028   23.219  65.036  1.00 43.89  ? 53  LYS A C   1 
ATOM   411   O O   . LYS A 1 57  ? 7.541   23.686  64.007  1.00 44.47  ? 53  LYS A O   1 
ATOM   412   C CB  . LYS A 1 57  ? 7.493   22.348  67.354  1.00 50.09  ? 53  LYS A CB  1 
ATOM   413   C CG  . LYS A 1 57  ? 6.604   21.532  68.278  1.00 55.35  ? 53  LYS A CG  1 
ATOM   414   C CD  . LYS A 1 57  ? 6.181   22.336  69.493  1.00 61.79  ? 53  LYS A CD  1 
ATOM   415   C CE  . LYS A 1 57  ? 5.136   21.597  70.319  1.00 68.45  ? 53  LYS A CE  1 
ATOM   416   N NZ  . LYS A 1 57  ? 5.651   20.313  70.875  1.00 72.84  ? 53  LYS A NZ  1 
ATOM   417   N N   . ASP A 1 58  ? 9.221   23.601  65.493  1.00 42.47  ? 54  ASP A N   1 
ATOM   418   C CA  . ASP A 1 58  ? 10.035  24.602  64.798  1.00 42.93  ? 54  ASP A CA  1 
ATOM   419   C C   . ASP A 1 58  ? 11.412  24.025  64.441  1.00 40.51  ? 54  ASP A C   1 
ATOM   420   O O   . ASP A 1 58  ? 12.362  24.765  64.168  1.00 39.96  ? 54  ASP A O   1 
ATOM   421   C CB  . ASP A 1 58  ? 10.177  25.859  65.671  1.00 47.61  ? 54  ASP A CB  1 
ATOM   422   C CG  . ASP A 1 58  ? 10.095  27.154  64.868  1.00 52.85  ? 54  ASP A CG  1 
ATOM   423   O OD1 . ASP A 1 58  ? 10.534  27.176  63.694  1.00 51.61  ? 54  ASP A OD1 1 
ATOM   424   O OD2 . ASP A 1 58  ? 9.593   28.157  65.422  1.00 52.44  ? 54  ASP A OD2 1 
ATOM   425   N N   . CYS A 1 59  ? 11.497  22.697  64.426  1.00 37.66  ? 55  CYS A N   1 
ATOM   426   C CA  . CYS A 1 59  ? 12.737  21.990  64.138  1.00 40.54  ? 55  CYS A CA  1 
ATOM   427   C C   . CYS A 1 59  ? 12.728  21.409  62.737  1.00 36.26  ? 55  CYS A C   1 
ATOM   428   O O   . CYS A 1 59  ? 11.686  20.980  62.239  1.00 31.53  ? 55  CYS A O   1 
ATOM   429   C CB  . CYS A 1 59  ? 12.960  20.867  65.137  1.00 45.93  ? 55  CYS A CB  1 
ATOM   430   S SG  . CYS A 1 59  ? 13.094  21.457  66.839  1.00 62.45  ? 55  CYS A SG  1 
ATOM   431   N N   . SER A 1 60  ? 13.906  21.394  62.120  1.00 32.60  ? 56  SER A N   1 
ATOM   432   C CA  . SER A 1 60  ? 14.105  20.734  60.843  1.00 29.72  ? 56  SER A CA  1 
ATOM   433   C C   . SER A 1 60  ? 14.357  19.256  61.100  1.00 29.64  ? 56  SER A C   1 
ATOM   434   O O   . SER A 1 60  ? 14.566  18.846  62.247  1.00 30.48  ? 56  SER A O   1 
ATOM   435   C CB  . SER A 1 60  ? 15.298  21.340  60.111  1.00 29.14  ? 56  SER A CB  1 
ATOM   436   O OG  . SER A 1 60  ? 16.515  20.874  60.668  1.00 32.73  ? 56  SER A OG  1 
ATOM   437   N N   . VAL A 1 61  ? 14.351  18.459  60.035  1.00 26.67  ? 57  VAL A N   1 
ATOM   438   C CA  . VAL A 1 61  ? 14.596  17.019  60.161  1.00 24.37  ? 57  VAL A CA  1 
ATOM   439   C C   . VAL A 1 61  ? 16.001  16.755  60.699  1.00 23.10  ? 57  VAL A C   1 
ATOM   440   O O   . VAL A 1 61  ? 16.194  15.879  61.546  1.00 23.93  ? 57  VAL A O   1 
ATOM   441   C CB  . VAL A 1 61  ? 14.419  16.276  58.822  1.00 21.91  ? 57  VAL A CB  1 
ATOM   442   C CG1 . VAL A 1 61  ? 14.788  14.808  58.975  1.00 22.56  ? 57  VAL A CG1 1 
ATOM   443   C CG2 . VAL A 1 61  ? 12.992  16.418  58.310  1.00 20.12  ? 57  VAL A CG2 1 
ATOM   444   N N   . ALA A 1 62  ? 16.971  17.525  60.219  1.00 21.66  ? 58  ALA A N   1 
ATOM   445   C CA  . ALA A 1 62  ? 18.354  17.377  60.664  1.00 20.90  ? 58  ALA A CA  1 
ATOM   446   C C   . ALA A 1 62  ? 18.481  17.652  62.157  1.00 19.74  ? 58  ALA A C   1 
ATOM   447   O O   . ALA A 1 62  ? 19.069  16.859  62.891  1.00 19.57  ? 58  ALA A O   1 
ATOM   448   C CB  . ALA A 1 62  ? 19.260  18.310  59.878  1.00 21.04  ? 58  ALA A CB  1 
ATOM   449   N N   . GLY A 1 63  ? 17.928  18.778  62.597  1.00 20.68  ? 59  GLY A N   1 
ATOM   450   C CA  . GLY A 1 63  ? 17.948  19.156  64.013  1.00 21.69  ? 59  GLY A CA  1 
ATOM   451   C C   . GLY A 1 63  ? 17.321  18.094  64.897  1.00 21.65  ? 59  GLY A C   1 
ATOM   452   O O   . GLY A 1 63  ? 17.851  17.754  65.950  1.00 20.53  ? 59  GLY A O   1 
ATOM   453   N N   . TRP A 1 64  ? 16.192  17.560  64.451  1.00 24.11  ? 60  TRP A N   1 
ATOM   454   C CA  . TRP A 1 64  ? 15.480  16.522  65.186  1.00 24.66  ? 60  TRP A CA  1 
ATOM   455   C C   . TRP A 1 64  ? 16.253  15.226  65.240  1.00 26.26  ? 60  TRP A C   1 
ATOM   456   O O   . TRP A 1 64  ? 16.299  14.581  66.284  1.00 28.54  ? 60  TRP A O   1 
ATOM   457   C CB  . TRP A 1 64  ? 14.095  16.320  64.579  1.00 25.62  ? 60  TRP A CB  1 
ATOM   458   C CG  . TRP A 1 64  ? 13.429  15.020  64.943  1.00 27.27  ? 60  TRP A CG  1 
ATOM   459   C CD1 . TRP A 1 64  ? 12.821  14.674  66.152  1.00 27.39  ? 60  TRP A CD1 1 
ATOM   460   C CD2 . TRP A 1 64  ? 13.262  13.850  64.079  1.00 27.70  ? 60  TRP A CD2 1 
ATOM   461   N NE1 . TRP A 1 64  ? 12.314  13.399  66.092  1.00 27.20  ? 60  TRP A NE1 1 
ATOM   462   C CE2 . TRP A 1 64  ? 12.546  12.848  64.877  1.00 29.57  ? 60  TRP A CE2 1 
ATOM   463   C CE3 . TRP A 1 64  ? 13.622  13.543  62.772  1.00 29.48  ? 60  TRP A CE3 1 
ATOM   464   C CZ2 . TRP A 1 64  ? 12.222  11.598  64.365  1.00 30.63  ? 60  TRP A CZ2 1 
ATOM   465   C CZ3 . TRP A 1 64  ? 13.292  12.281  62.266  1.00 29.85  ? 60  TRP A CZ3 1 
ATOM   466   C CH2 . TRP A 1 64  ? 12.611  11.333  63.045  1.00 31.33  ? 60  TRP A CH2 1 
ATOM   467   N N   . LEU A 1 65  ? 16.875  14.833  64.128  1.00 25.78  ? 61  LEU A N   1 
ATOM   468   C CA  . LEU A 1 65  ? 17.674  13.599  64.086  1.00 25.20  ? 61  LEU A CA  1 
ATOM   469   C C   . LEU A 1 65  ? 18.919  13.669  64.967  1.00 26.67  ? 61  LEU A C   1 
ATOM   470   O O   . LEU A 1 65  ? 19.240  12.719  65.685  1.00 28.00  ? 61  LEU A O   1 
ATOM   471   C CB  . LEU A 1 65  ? 18.120  13.285  62.657  1.00 25.53  ? 61  LEU A CB  1 
ATOM   472   C CG  . LEU A 1 65  ? 17.186  12.460  61.775  1.00 24.00  ? 61  LEU A CG  1 
ATOM   473   C CD1 . LEU A 1 65  ? 17.841  12.264  60.409  1.00 21.81  ? 61  LEU A CD1 1 
ATOM   474   C CD2 . LEU A 1 65  ? 16.858  11.128  62.426  1.00 20.43  ? 61  LEU A CD2 1 
ATOM   475   N N   . LEU A 1 66  ? 19.622  14.795  64.893  1.00 27.26  ? 62  LEU A N   1 
ATOM   476   C CA  . LEU A 1 66  ? 20.903  14.967  65.586  1.00 27.07  ? 62  LEU A CA  1 
ATOM   477   C C   . LEU A 1 66  ? 20.766  15.276  67.075  1.00 25.57  ? 62  LEU A C   1 
ATOM   478   O O   . LEU A 1 66  ? 21.686  15.002  67.842  1.00 25.65  ? 62  LEU A O   1 
ATOM   479   C CB  . LEU A 1 66  ? 21.725  16.068  64.909  1.00 26.55  ? 62  LEU A CB  1 
ATOM   480   C CG  . LEU A 1 66  ? 22.193  15.704  63.498  1.00 26.12  ? 62  LEU A CG  1 
ATOM   481   C CD1 . LEU A 1 66  ? 22.691  16.918  62.726  1.00 26.44  ? 62  LEU A CD1 1 
ATOM   482   C CD2 . LEU A 1 66  ? 23.275  14.638  63.586  1.00 24.83  ? 62  LEU A CD2 1 
ATOM   483   N N   . GLY A 1 67  ? 19.634  15.850  67.477  1.00 26.60  ? 63  GLY A N   1 
ATOM   484   C CA  . GLY A 1 67  ? 19.385  16.165  68.882  1.00 28.20  ? 63  GLY A CA  1 
ATOM   485   C C   . GLY A 1 67  ? 19.745  17.585  69.287  1.00 28.72  ? 63  GLY A C   1 
ATOM   486   O O   . GLY A 1 67  ? 20.173  17.817  70.417  1.00 31.42  ? 63  GLY A O   1 
ATOM   487   N N   . ASN A 1 68  ? 19.578  18.531  68.366  1.00 28.86  ? 64  ASN A N   1 
ATOM   488   C CA  . ASN A 1 68  ? 19.687  19.961  68.672  1.00 30.29  ? 64  ASN A CA  1 
ATOM   489   C C   . ASN A 1 68  ? 19.082  20.278  70.051  1.00 30.19  ? 64  ASN A C   1 
ATOM   490   O O   . ASN A 1 68  ? 17.933  19.912  70.316  1.00 29.70  ? 64  ASN A O   1 
ATOM   491   C CB  . ASN A 1 68  ? 18.975  20.769  67.574  1.00 31.66  ? 64  ASN A CB  1 
ATOM   492   C CG  . ASN A 1 68  ? 19.252  22.264  67.650  1.00 32.15  ? 64  ASN A CG  1 
ATOM   493   O OD1 . ASN A 1 68  ? 19.350  22.842  68.729  1.00 31.39  ? 64  ASN A OD1 1 
ATOM   494   N ND2 . ASN A 1 68  ? 19.351  22.902  66.488  1.00 32.94  ? 64  ASN A ND2 1 
ATOM   495   N N   . PRO A 1 69  ? 19.857  20.934  70.942  1.00 33.27  ? 65  PRO A N   1 
ATOM   496   C CA  . PRO A 1 69  ? 19.376  21.273  72.295  1.00 37.51  ? 65  PRO A CA  1 
ATOM   497   C C   . PRO A 1 69  ? 18.068  22.072  72.340  1.00 41.61  ? 65  PRO A C   1 
ATOM   498   O O   . PRO A 1 69  ? 17.246  21.856  73.230  1.00 48.46  ? 65  PRO A O   1 
ATOM   499   C CB  . PRO A 1 69  ? 20.518  22.115  72.868  1.00 35.13  ? 65  PRO A CB  1 
ATOM   500   C CG  . PRO A 1 69  ? 21.726  21.617  72.170  1.00 35.28  ? 65  PRO A CG  1 
ATOM   501   C CD  . PRO A 1 69  ? 21.278  21.290  70.775  1.00 33.60  ? 65  PRO A CD  1 
ATOM   502   N N   . MET A 1 70  ? 17.888  22.977  71.381  1.00 48.32  ? 66  MET A N   1 
ATOM   503   C CA  . MET A 1 70  ? 16.688  23.818  71.295  1.00 52.25  ? 66  MET A CA  1 
ATOM   504   C C   . MET A 1 70  ? 15.436  23.051  70.853  1.00 51.24  ? 66  MET A C   1 
ATOM   505   O O   . MET A 1 70  ? 14.327  23.578  70.931  1.00 50.73  ? 66  MET A O   1 
ATOM   506   C CB  . MET A 1 70  ? 16.946  24.985  70.339  1.00 62.96  ? 66  MET A CB  1 
ATOM   507   C CG  . MET A 1 70  ? 17.855  26.046  70.905  1.00 72.41  ? 66  MET A CG  1 
ATOM   508   S SD  . MET A 1 70  ? 18.497  27.141  69.626  1.00 83.87  ? 66  MET A SD  1 
ATOM   509   C CE  . MET A 1 70  ? 19.633  28.159  70.561  1.00 77.78  ? 66  MET A CE  1 
ATOM   510   N N   . CYS A 1 71  ? 15.620  21.820  70.378  1.00 52.11  ? 67  CYS A N   1 
ATOM   511   C CA  . CYS A 1 71  ? 14.513  20.927  70.037  1.00 54.12  ? 67  CYS A CA  1 
ATOM   512   C C   . CYS A 1 71  ? 14.188  20.047  71.236  1.00 60.51  ? 67  CYS A C   1 
ATOM   513   O O   . CYS A 1 71  ? 14.790  20.210  72.303  1.00 69.06  ? 67  CYS A O   1 
ATOM   514   C CB  . CYS A 1 71  ? 14.884  20.087  68.806  1.00 51.55  ? 67  CYS A CB  1 
ATOM   515   S SG  . CYS A 1 71  ? 15.043  21.123  67.337  1.00 54.46  ? 67  CYS A SG  1 
ATOM   516   N N   . ASP A 1 72  ? 13.233  19.132  71.071  1.00 66.47  ? 68  ASP A N   1 
ATOM   517   C CA  . ASP A 1 72  ? 12.867  18.205  72.142  1.00 71.82  ? 68  ASP A CA  1 
ATOM   518   C C   . ASP A 1 72  ? 12.855  16.763  71.652  1.00 77.96  ? 68  ASP A C   1 
ATOM   519   O O   . ASP A 1 72  ? 12.646  16.475  70.471  1.00 79.57  ? 68  ASP A O   1 
ATOM   520   C CB  . ASP A 1 72  ? 11.535  18.592  72.808  1.00 65.93  ? 68  ASP A CB  1 
ATOM   521   C CG  . ASP A 1 72  ? 10.400  18.768  71.813  1.00 67.25  ? 68  ASP A CG  1 
ATOM   522   O OD1 . ASP A 1 72  ? 10.427  19.747  71.043  1.00 70.27  ? 68  ASP A OD1 1 
ATOM   523   O OD2 . ASP A 1 72  ? 9.467   17.943  71.816  1.00 61.73  ? 68  ASP A OD2 1 
ATOM   524   N N   . GLU A 1 73  ? 13.100  15.856  72.584  1.00 83.92  ? 69  GLU A N   1 
ATOM   525   C CA  . GLU A 1 73  ? 13.384  14.471  72.253  1.00 90.99  ? 69  GLU A CA  1 
ATOM   526   C C   . GLU A 1 73  ? 12.995  13.639  73.487  1.00 97.97  ? 69  GLU A C   1 
ATOM   527   O O   . GLU A 1 73  ? 12.379  14.197  74.405  1.00 97.12  ? 69  GLU A O   1 
ATOM   528   C CB  . GLU A 1 73  ? 14.854  14.357  71.819  1.00 98.14  ? 69  GLU A CB  1 
ATOM   529   C CG  . GLU A 1 73  ? 15.076  14.596  70.332  1.00 94.93  ? 69  GLU A CG  1 
ATOM   530   C CD  . GLU A 1 73  ? 16.398  14.045  69.830  1.00 84.90  ? 69  GLU A CD  1 
ATOM   531   O OE1 . GLU A 1 73  ? 17.365  13.948  70.615  1.00 77.86  ? 69  GLU A OE1 1 
ATOM   532   O OE2 . GLU A 1 73  ? 16.467  13.705  68.637  1.00 82.76  ? 69  GLU A OE2 1 
ATOM   533   N N   . PHE A 1 74  ? 13.277  12.334  73.539  1.00 109.72 ? 70  PHE A N   1 
ATOM   534   C CA  . PHE A 1 74  ? 13.979  11.558  72.514  1.00 111.45 ? 70  PHE A CA  1 
ATOM   535   C C   . PHE A 1 74  ? 13.125  10.451  71.907  1.00 102.66 ? 70  PHE A C   1 
ATOM   536   O O   . PHE A 1 74  ? 13.597  9.652   71.090  1.00 88.93  ? 70  PHE A O   1 
ATOM   537   C CB  . PHE A 1 74  ? 15.267  10.961  73.115  1.00 124.30 ? 70  PHE A CB  1 
ATOM   538   C CG  . PHE A 1 74  ? 15.035  10.001  74.259  1.00 138.49 ? 70  PHE A CG  1 
ATOM   539   C CD1 . PHE A 1 74  ? 15.028  8.626   74.044  1.00 141.79 ? 70  PHE A CD1 1 
ATOM   540   C CD2 . PHE A 1 74  ? 14.842  10.470  75.556  1.00 142.60 ? 70  PHE A CD2 1 
ATOM   541   C CE1 . PHE A 1 74  ? 14.819  7.743   75.093  1.00 141.23 ? 70  PHE A CE1 1 
ATOM   542   C CE2 . PHE A 1 74  ? 14.631  9.590   76.607  1.00 139.83 ? 70  PHE A CE2 1 
ATOM   543   C CZ  . PHE A 1 74  ? 14.621  8.225   76.376  1.00 139.65 ? 70  PHE A CZ  1 
ATOM   544   N N   . ILE A 1 75  ? 11.860  10.422  72.301  1.00 103.36 ? 71  ILE A N   1 
ATOM   545   C CA  . ILE A 1 75  ? 10.934  9.392   71.847  1.00 99.42  ? 71  ILE A CA  1 
ATOM   546   C C   . ILE A 1 75  ? 9.522   9.988   71.715  1.00 97.27  ? 71  ILE A C   1 
ATOM   547   O O   . ILE A 1 75  ? 9.249   11.073  72.245  1.00 99.57  ? 71  ILE A O   1 
ATOM   548   C CB  . ILE A 1 75  ? 10.945  8.174   72.820  1.00 96.38  ? 71  ILE A CB  1 
ATOM   549   C CG1 . ILE A 1 75  ? 11.019  8.653   74.271  1.00 89.56  ? 71  ILE A CG1 1 
ATOM   550   C CG2 . ILE A 1 75  ? 12.125  7.264   72.515  1.00 97.83  ? 71  ILE A CG2 1 
ATOM   551   C CD1 . ILE A 1 75  ? 10.765  7.564   75.293  1.00 76.19  ? 71  ILE A CD1 1 
ATOM   552   N N   . ASN A 1 76  ? 8.638   9.324   70.970  1.00 91.39  ? 72  ASN A N   1 
ATOM   553   C CA  . ASN A 1 76  ? 8.972   8.142   70.190  1.00 87.15  ? 72  ASN A CA  1 
ATOM   554   C C   . ASN A 1 76  ? 8.431   8.320   68.780  1.00 80.15  ? 72  ASN A C   1 
ATOM   555   O O   . ASN A 1 76  ? 9.195   8.510   67.830  1.00 78.41  ? 72  ASN A O   1 
ATOM   556   C CB  . ASN A 1 76  ? 8.410   6.858   70.832  1.00 88.25  ? 72  ASN A CB  1 
ATOM   557   C CG  . ASN A 1 76  ? 9.234   5.615   70.502  1.00 84.04  ? 72  ASN A CG  1 
ATOM   558   O OD1 . ASN A 1 76  ? 10.347  5.696   69.979  1.00 68.87  ? 72  ASN A OD1 1 
ATOM   559   N ND2 . ASN A 1 76  ? 8.675   4.450   70.808  1.00 90.64  ? 72  ASN A ND2 1 
ATOM   560   N N   . VAL A 1 77  ? 7.105   8.309   68.666  1.00 71.60  ? 73  VAL A N   1 
ATOM   561   C CA  . VAL A 1 77  ? 6.438   8.238   67.378  1.00 69.74  ? 73  VAL A CA  1 
ATOM   562   C C   . VAL A 1 77  ? 7.138   7.141   66.555  1.00 62.77  ? 73  VAL A C   1 
ATOM   563   O O   . VAL A 1 77  ? 8.006   7.443   65.743  1.00 58.95  ? 73  VAL A O   1 
ATOM   564   C CB  . VAL A 1 77  ? 6.472   9.602   66.642  1.00 69.44  ? 73  VAL A CB  1 
ATOM   565   C CG1 . VAL A 1 77  ? 5.774   9.508   65.289  1.00 58.74  ? 73  VAL A CG1 1 
ATOM   566   C CG2 . VAL A 1 77  ? 5.827   10.685  67.496  1.00 67.75  ? 73  VAL A CG2 1 
ATOM   567   N N   . PRO A 1 78  ? 6.799   5.856   66.790  1.00 57.64  ? 74  PRO A N   1 
ATOM   568   C CA  . PRO A 1 78  ? 7.461   4.805   66.005  1.00 54.59  ? 74  PRO A CA  1 
ATOM   569   C C   . PRO A 1 78  ? 6.918   4.675   64.588  1.00 55.13  ? 74  PRO A C   1 
ATOM   570   O O   . PRO A 1 78  ? 7.449   3.898   63.799  1.00 57.82  ? 74  PRO A O   1 
ATOM   571   C CB  . PRO A 1 78  ? 7.129   3.536   66.784  1.00 55.37  ? 74  PRO A CB  1 
ATOM   572   C CG  . PRO A 1 78  ? 5.785   3.823   67.367  1.00 53.28  ? 74  PRO A CG  1 
ATOM   573   C CD  . PRO A 1 78  ? 5.806   5.287   67.724  1.00 53.02  ? 74  PRO A CD  1 
ATOM   574   N N   . GLU A 1 79  ? 5.855   5.402   64.270  1.00 46.08  ? 75  GLU A N   1 
ATOM   575   C CA  . GLU A 1 79  ? 5.304   5.348   62.936  1.00 43.76  ? 75  GLU A CA  1 
ATOM   576   C C   . GLU A 1 79  ? 4.691   6.672   62.513  1.00 39.31  ? 75  GLU A C   1 
ATOM   577   O O   . GLU A 1 79  ? 4.069   7.368   63.311  1.00 42.73  ? 75  GLU A O   1 
ATOM   578   C CB  . GLU A 1 79  ? 4.262   4.253   62.850  1.00 48.30  ? 75  GLU A CB  1 
ATOM   579   C CG  . GLU A 1 79  ? 3.960   3.869   61.424  1.00 54.82  ? 75  GLU A CG  1 
ATOM   580   C CD  . GLU A 1 79  ? 2.707   3.025   61.295  1.00 60.34  ? 75  GLU A CD  1 
ATOM   581   O OE1 . GLU A 1 79  ? 1.840   3.065   62.196  1.00 64.69  ? 75  GLU A OE1 1 
ATOM   582   O OE2 . GLU A 1 79  ? 2.582   2.320   60.281  1.00 62.01  ? 75  GLU A OE2 1 
ATOM   583   N N   . TRP A 1 80  ? 4.875   7.009   61.244  1.00 29.08  ? 76  TRP A N   1 
ATOM   584   C CA  . TRP A 1 80  ? 4.243   8.185   60.667  1.00 24.74  ? 76  TRP A CA  1 
ATOM   585   C C   . TRP A 1 80  ? 4.035   8.035   59.184  1.00 23.61  ? 76  TRP A C   1 
ATOM   586   O O   . TRP A 1 80  ? 4.679   7.210   58.537  1.00 23.68  ? 76  TRP A O   1 
ATOM   587   C CB  . TRP A 1 80  ? 5.042   9.441   60.996  1.00 21.32  ? 76  TRP A CB  1 
ATOM   588   C CG  . TRP A 1 80  ? 6.425   9.467   60.400  1.00 19.62  ? 76  TRP A CG  1 
ATOM   589   C CD1 . TRP A 1 80  ? 6.788   9.861   59.117  1.00 17.61  ? 76  TRP A CD1 1 
ATOM   590   C CD2 . TRP A 1 80  ? 7.688   9.108   61.060  1.00 18.25  ? 76  TRP A CD2 1 
ATOM   591   N NE1 . TRP A 1 80  ? 8.142   9.763   58.943  1.00 16.76  ? 76  TRP A NE1 1 
ATOM   592   C CE2 . TRP A 1 80  ? 8.741   9.317   60.066  1.00 16.98  ? 76  TRP A CE2 1 
ATOM   593   C CE3 . TRP A 1 80  ? 8.036   8.647   62.321  1.00 17.54  ? 76  TRP A CE3 1 
ATOM   594   C CZ2 . TRP A 1 80  ? 10.070  9.066   60.347  1.00 17.18  ? 76  TRP A CZ2 1 
ATOM   595   C CZ3 . TRP A 1 80  ? 9.383   8.398   62.596  1.00 17.58  ? 76  TRP A CZ3 1 
ATOM   596   C CH2 . TRP A 1 80  ? 10.375  8.604   61.632  1.00 17.48  ? 76  TRP A CH2 1 
ATOM   597   N N   . SER A 1 81  ? 3.116   8.832   58.648  1.00 22.86  ? 77  SER A N   1 
ATOM   598   C CA  . SER A 1 81  ? 2.715   8.752   57.242  1.00 24.65  ? 77  SER A CA  1 
ATOM   599   C C   . SER A 1 81  ? 3.304   9.887   56.399  1.00 24.29  ? 77  SER A C   1 
ATOM   600   O O   . SER A 1 81  ? 3.581   9.701   55.222  1.00 25.26  ? 77  SER A O   1 
ATOM   601   C CB  . SER A 1 81  ? 1.192   8.780   57.140  1.00 25.97  ? 77  SER A CB  1 
ATOM   602   O OG  . SER A 1 81  ? 0.664   9.882   57.855  1.00 26.74  ? 77  SER A OG  1 
ATOM   603   N N   . TYR A 1 82  ? 3.462   11.063  56.999  1.00 23.86  ? 78  TYR A N   1 
ATOM   604   C CA  . TYR A 1 82  ? 4.172   12.171  56.368  1.00 22.82  ? 78  TYR A CA  1 
ATOM   605   C C   . TYR A 1 82  ? 4.797   13.058  57.441  1.00 22.81  ? 78  TYR A C   1 
ATOM   606   O O   . TYR A 1 82  ? 4.551   12.864  58.631  1.00 20.09  ? 78  TYR A O   1 
ATOM   607   C CB  . TYR A 1 82  ? 3.253   12.966  55.442  1.00 23.91  ? 78  TYR A CB  1 
ATOM   608   C CG  . TYR A 1 82  ? 2.074   13.637  56.118  1.00 24.93  ? 78  TYR A CG  1 
ATOM   609   C CD1 . TYR A 1 82  ? 2.073   15.009  56.356  1.00 24.43  ? 78  TYR A CD1 1 
ATOM   610   C CD2 . TYR A 1 82  ? 0.952   12.907  56.497  1.00 24.81  ? 78  TYR A CD2 1 
ATOM   611   C CE1 . TYR A 1 82  ? 0.999   15.631  56.963  1.00 24.08  ? 78  TYR A CE1 1 
ATOM   612   C CE2 . TYR A 1 82  ? -0.127  13.519  57.116  1.00 24.86  ? 78  TYR A CE2 1 
ATOM   613   C CZ  . TYR A 1 82  ? -0.098  14.881  57.345  1.00 24.60  ? 78  TYR A CZ  1 
ATOM   614   O OH  . TYR A 1 82  ? -1.167  15.496  57.956  1.00 24.71  ? 78  TYR A OH  1 
ATOM   615   N N   . ILE A 1 83  ? 5.645   13.994  57.020  1.00 23.50  ? 79  ILE A N   1 
ATOM   616   C CA  . ILE A 1 83  ? 6.362   14.867  57.950  1.00 22.17  ? 79  ILE A CA  1 
ATOM   617   C C   . ILE A 1 83  ? 5.935   16.313  57.747  1.00 22.11  ? 79  ILE A C   1 
ATOM   618   O O   . ILE A 1 83  ? 5.822   16.766  56.614  1.00 21.42  ? 79  ILE A O   1 
ATOM   619   C CB  . ILE A 1 83  ? 7.882   14.781  57.747  1.00 20.97  ? 79  ILE A CB  1 
ATOM   620   C CG1 . ILE A 1 83  ? 8.404   13.409  58.176  1.00 21.13  ? 79  ILE A CG1 1 
ATOM   621   C CG2 . ILE A 1 83  ? 8.584   15.883  58.528  1.00 20.52  ? 79  ILE A CG2 1 
ATOM   622   C CD1 . ILE A 1 83  ? 9.895   13.235  57.969  1.00 18.83  ? 79  ILE A CD1 1 
ATOM   623   N N   . VAL A 1 84  ? 5.716   17.032  58.846  1.00 24.44  ? 80  VAL A N   1 
ATOM   624   C CA  . VAL A 1 84  ? 5.375   18.452  58.778  1.00 25.92  ? 80  VAL A CA  1 
ATOM   625   C C   . VAL A 1 84  ? 6.489   19.312  59.366  1.00 26.02  ? 80  VAL A C   1 
ATOM   626   O O   . VAL A 1 84  ? 6.780   19.231  60.560  1.00 25.96  ? 80  VAL A O   1 
ATOM   627   C CB  . VAL A 1 84  ? 4.067   18.776  59.524  1.00 27.63  ? 80  VAL A CB  1 
ATOM   628   C CG1 . VAL A 1 84  ? 3.717   20.247  59.352  1.00 27.96  ? 80  VAL A CG1 1 
ATOM   629   C CG2 . VAL A 1 84  ? 2.929   17.896  59.024  1.00 27.94  ? 80  VAL A CG2 1 
ATOM   630   N N   . GLU A 1 85  ? 7.110   20.121  58.510  1.00 29.18  ? 81  GLU A N   1 
ATOM   631   C CA  . GLU A 1 85  ? 8.050   21.164  58.922  1.00 29.72  ? 81  GLU A CA  1 
ATOM   632   C C   . GLU A 1 85  ? 7.385   22.512  58.691  1.00 30.37  ? 81  GLU A C   1 
ATOM   633   O O   . GLU A 1 85  ? 6.411   22.607  57.943  1.00 30.61  ? 81  GLU A O   1 
ATOM   634   C CB  . GLU A 1 85  ? 9.322   21.130  58.073  1.00 29.28  ? 81  GLU A CB  1 
ATOM   635   C CG  . GLU A 1 85  ? 10.299  20.007  58.362  1.00 29.51  ? 81  GLU A CG  1 
ATOM   636   C CD  . GLU A 1 85  ? 11.577  20.143  57.543  1.00 31.91  ? 81  GLU A CD  1 
ATOM   637   O OE1 . GLU A 1 85  ? 11.506  20.639  56.396  1.00 30.34  ? 81  GLU A OE1 1 
ATOM   638   O OE2 . GLU A 1 85  ? 12.660  19.765  58.045  1.00 35.54  ? 81  GLU A OE2 1 
ATOM   639   N N   . LYS A 1 86  ? 7.916   23.552  59.324  1.00 31.67  ? 82  LYS A N   1 
ATOM   640   C CA  . LYS A 1 86  ? 7.538   24.914  58.983  1.00 34.23  ? 82  LYS A CA  1 
ATOM   641   C C   . LYS A 1 86  ? 8.341   25.332  57.761  1.00 34.22  ? 82  LYS A C   1 
ATOM   642   O O   . LYS A 1 86  ? 9.292   24.649  57.376  1.00 36.53  ? 82  LYS A O   1 
ATOM   643   C CB  . LYS A 1 86  ? 7.798   25.861  60.150  1.00 37.90  ? 82  LYS A CB  1 
ATOM   644   C CG  . LYS A 1 86  ? 7.034   25.468  61.420  1.00 42.99  ? 82  LYS A CG  1 
ATOM   645   C CD  . LYS A 1 86  ? 5.741   26.229  61.634  1.00 49.27  ? 82  LYS A CD  1 
ATOM   646   C CE  . LYS A 1 86  ? 5.269   26.198  63.085  1.00 47.67  ? 82  LYS A CE  1 
ATOM   647   N NZ  . LYS A 1 86  ? 5.043   24.821  63.608  1.00 43.95  ? 82  LYS A NZ  1 
ATOM   648   N N   . ALA A 1 87  ? 7.951   26.447  57.151  1.00 36.26  ? 83  ALA A N   1 
ATOM   649   C CA  . ALA A 1 87  ? 8.628   26.955  55.956  1.00 35.57  ? 83  ALA A CA  1 
ATOM   650   C C   . ALA A 1 87  ? 10.120  27.173  56.211  1.00 37.07  ? 83  ALA A C   1 
ATOM   651   O O   . ALA A 1 87  ? 10.954  26.767  55.403  1.00 40.32  ? 83  ALA A O   1 
ATOM   652   C CB  . ALA A 1 87  ? 7.975   28.245  55.475  1.00 33.53  ? 83  ALA A CB  1 
ATOM   653   N N   . ASN A 1 88  ? 10.444  27.810  57.335  1.00 40.07  ? 84  ASN A N   1 
ATOM   654   C CA  . ASN A 1 88  ? 11.832  28.069  57.718  1.00 43.14  ? 84  ASN A CA  1 
ATOM   655   C C   . ASN A 1 88  ? 12.055  27.770  59.198  1.00 42.39  ? 84  ASN A C   1 
ATOM   656   O O   . ASN A 1 88  ? 11.960  28.669  60.030  1.00 45.97  ? 84  ASN A O   1 
ATOM   657   C CB  . ASN A 1 88  ? 12.198  29.525  57.413  1.00 45.21  ? 84  ASN A CB  1 
ATOM   658   C CG  . ASN A 1 88  ? 12.068  29.860  55.937  1.00 45.44  ? 84  ASN A CG  1 
ATOM   659   O OD1 . ASN A 1 88  ? 12.845  29.382  55.112  1.00 47.79  ? 84  ASN A OD1 1 
ATOM   660   N ND2 . ASN A 1 88  ? 11.076  30.678  55.599  1.00 42.72  ? 84  ASN A ND2 1 
ATOM   661   N N   . PRO A 1 89  ? 12.350  26.499  59.534  1.00 41.53  ? 85  PRO A N   1 
ATOM   662   C CA  . PRO A 1 89  ? 12.538  26.130  60.938  1.00 37.90  ? 85  PRO A CA  1 
ATOM   663   C C   . PRO A 1 89  ? 13.681  26.907  61.580  1.00 38.44  ? 85  PRO A C   1 
ATOM   664   O O   . PRO A 1 89  ? 14.729  27.085  60.958  1.00 40.95  ? 85  PRO A O   1 
ATOM   665   C CB  . PRO A 1 89  ? 12.872  24.633  60.876  1.00 38.68  ? 85  PRO A CB  1 
ATOM   666   C CG  . PRO A 1 89  ? 12.386  24.170  59.545  1.00 40.43  ? 85  PRO A CG  1 
ATOM   667   C CD  . PRO A 1 89  ? 12.531  25.348  58.632  1.00 41.77  ? 85  PRO A CD  1 
ATOM   668   N N   . ALA A 1 90  ? 13.469  27.366  62.811  1.00 39.33  ? 86  ALA A N   1 
ATOM   669   C CA  . ALA A 1 90  ? 14.469  28.160  63.535  1.00 37.38  ? 86  ALA A CA  1 
ATOM   670   C C   . ALA A 1 90  ? 15.587  27.290  64.100  1.00 35.51  ? 86  ALA A C   1 
ATOM   671   O O   . ALA A 1 90  ? 16.716  27.752  64.234  1.00 34.19  ? 86  ALA A O   1 
ATOM   672   C CB  . ALA A 1 90  ? 13.814  28.959  64.654  1.00 38.51  ? 86  ALA A CB  1 
ATOM   673   N N   . ASN A 1 91  ? 15.270  26.037  64.422  1.00 34.50  ? 87  ASN A N   1 
ATOM   674   C CA  . ASN A 1 91  ? 16.239  25.109  65.002  1.00 36.61  ? 87  ASN A CA  1 
ATOM   675   C C   . ASN A 1 91  ? 16.676  24.037  64.003  1.00 40.10  ? 87  ASN A C   1 
ATOM   676   O O   . ASN A 1 91  ? 16.094  22.953  63.941  1.00 36.14  ? 87  ASN A O   1 
ATOM   677   C CB  . ASN A 1 91  ? 15.651  24.458  66.252  1.00 35.77  ? 87  ASN A CB  1 
ATOM   678   C CG  . ASN A 1 91  ? 15.113  25.474  67.237  1.00 34.96  ? 87  ASN A CG  1 
ATOM   679   O OD1 . ASN A 1 91  ? 14.070  25.268  67.853  1.00 34.45  ? 87  ASN A OD1 1 
ATOM   680   N ND2 . ASN A 1 91  ? 15.821  26.584  67.384  1.00 36.65  ? 87  ASN A ND2 1 
ATOM   681   N N   . ASP A 1 92  ? 17.706  24.361  63.221  1.00 43.20  ? 88  ASP A N   1 
ATOM   682   C CA  . ASP A 1 92  ? 18.238  23.456  62.206  1.00 43.53  ? 88  ASP A CA  1 
ATOM   683   C C   . ASP A 1 92  ? 19.580  22.887  62.702  1.00 44.58  ? 88  ASP A C   1 
ATOM   684   O O   . ASP A 1 92  ? 19.584  21.992  63.552  1.00 44.73  ? 88  ASP A O   1 
ATOM   685   C CB  . ASP A 1 92  ? 18.347  24.196  60.861  1.00 48.27  ? 88  ASP A CB  1 
ATOM   686   C CG  . ASP A 1 92  ? 18.669  23.272  59.692  1.00 54.95  ? 88  ASP A CG  1 
ATOM   687   O OD1 . ASP A 1 92  ? 18.689  22.035  59.866  1.00 64.66  ? 88  ASP A OD1 1 
ATOM   688   O OD2 . ASP A 1 92  ? 18.889  23.796  58.579  1.00 61.95  ? 88  ASP A OD2 1 
ATOM   689   N N   . LEU A 1 93  ? 20.701  23.399  62.192  1.00 40.69  ? 89  LEU A N   1 
ATOM   690   C CA  . LEU A 1 93  ? 22.026  23.018  62.670  1.00 36.38  ? 89  LEU A CA  1 
ATOM   691   C C   . LEU A 1 93  ? 22.554  24.131  63.571  1.00 35.40  ? 89  LEU A C   1 
ATOM   692   O O   . LEU A 1 93  ? 23.031  25.155  63.082  1.00 35.40  ? 89  LEU A O   1 
ATOM   693   C CB  . LEU A 1 93  ? 22.978  22.803  61.492  1.00 35.33  ? 89  LEU A CB  1 
ATOM   694   C CG  . LEU A 1 93  ? 22.643  21.666  60.524  1.00 35.84  ? 89  LEU A CG  1 
ATOM   695   C CD1 . LEU A 1 93  ? 23.527  21.735  59.284  1.00 30.72  ? 89  LEU A CD1 1 
ATOM   696   C CD2 . LEU A 1 93  ? 22.791  20.325  61.225  1.00 34.25  ? 89  LEU A CD2 1 
ATOM   697   N N   . CYS A 1 94  ? 22.460  23.935  64.884  1.00 33.59  ? 90  CYS A N   1 
ATOM   698   C CA  . CYS A 1 94  ? 22.870  24.965  65.839  1.00 33.70  ? 90  CYS A CA  1 
ATOM   699   C C   . CYS A 1 94  ? 24.341  25.339  65.629  1.00 31.03  ? 90  CYS A C   1 
ATOM   700   O O   . CYS A 1 94  ? 24.679  26.520  65.543  1.00 29.51  ? 90  CYS A O   1 
ATOM   701   C CB  . CYS A 1 94  ? 22.609  24.524  67.288  1.00 34.22  ? 90  CYS A CB  1 
ATOM   702   S SG  . CYS A 1 94  ? 23.413  22.989  67.793  1.00 39.00  ? 90  CYS A SG  1 
ATOM   703   N N   . TYR A 1 95  ? 25.204  24.330  65.543  1.00 27.53  ? 91  TYR A N   1 
ATOM   704   C CA  . TYR A 1 95  ? 26.573  24.540  65.097  1.00 26.58  ? 91  TYR A CA  1 
ATOM   705   C C   . TYR A 1 95  ? 26.555  24.496  63.570  1.00 25.25  ? 91  TYR A C   1 
ATOM   706   O O   . TYR A 1 95  ? 26.089  23.516  62.994  1.00 26.55  ? 91  TYR A O   1 
ATOM   707   C CB  . TYR A 1 95  ? 27.518  23.473  65.656  1.00 25.80  ? 91  TYR A CB  1 
ATOM   708   C CG  . TYR A 1 95  ? 28.976  23.869  65.566  1.00 25.45  ? 91  TYR A CG  1 
ATOM   709   C CD1 . TYR A 1 95  ? 29.631  24.436  66.655  1.00 23.37  ? 91  TYR A CD1 1 
ATOM   710   C CD2 . TYR A 1 95  ? 29.697  23.691  64.386  1.00 24.92  ? 91  TYR A CD2 1 
ATOM   711   C CE1 . TYR A 1 95  ? 30.962  24.807  66.576  1.00 23.48  ? 91  TYR A CE1 1 
ATOM   712   C CE2 . TYR A 1 95  ? 31.031  24.063  64.297  1.00 24.02  ? 91  TYR A CE2 1 
ATOM   713   C CZ  . TYR A 1 95  ? 31.656  24.622  65.393  1.00 24.75  ? 91  TYR A CZ  1 
ATOM   714   O OH  . TYR A 1 95  ? 32.977  24.991  65.311  1.00 26.34  ? 91  TYR A OH  1 
ATOM   715   N N   . PRO A 1 96  ? 27.063  25.553  62.911  1.00 23.50  ? 92  PRO A N   1 
ATOM   716   C CA  . PRO A 1 96  ? 26.923  25.671  61.459  1.00 24.07  ? 92  PRO A CA  1 
ATOM   717   C C   . PRO A 1 96  ? 27.677  24.590  60.679  1.00 25.47  ? 92  PRO A C   1 
ATOM   718   O O   . PRO A 1 96  ? 28.657  24.036  61.179  1.00 26.48  ? 92  PRO A O   1 
ATOM   719   C CB  . PRO A 1 96  ? 27.510  27.056  61.165  1.00 23.55  ? 92  PRO A CB  1 
ATOM   720   C CG  . PRO A 1 96  ? 28.493  27.287  62.261  1.00 23.09  ? 92  PRO A CG  1 
ATOM   721   C CD  . PRO A 1 96  ? 27.895  26.635  63.472  1.00 23.00  ? 92  PRO A CD  1 
ATOM   722   N N   . GLY A 1 97  ? 27.211  24.303  59.463  1.00 26.55  ? 93  GLY A N   1 
ATOM   723   C CA  . GLY A 1 97  ? 27.840  23.305  58.600  1.00 26.56  ? 93  GLY A CA  1 
ATOM   724   C C   . GLY A 1 97  ? 26.900  22.724  57.559  1.00 29.05  ? 93  GLY A C   1 
ATOM   725   O O   . GLY A 1 97  ? 25.897  23.337  57.200  1.00 32.69  ? 93  GLY A O   1 
ATOM   726   N N   . ASN A 1 98  ? 27.240  21.538  57.063  1.00 31.53  ? 94  ASN A N   1 
ATOM   727   C CA  . ASN A 1 98  ? 26.473  20.871  56.013  1.00 30.96  ? 94  ASN A CA  1 
ATOM   728   C C   . ASN A 1 98  ? 25.941  19.526  56.468  1.00 28.90  ? 94  ASN A C   1 
ATOM   729   O O   . ASN A 1 98  ? 26.456  18.931  57.414  1.00 27.76  ? 94  ASN A O   1 
ATOM   730   C CB  . ASN A 1 98  ? 27.340  20.658  54.765  1.00 34.57  ? 94  ASN A CB  1 
ATOM   731   C CG  . ASN A 1 98  ? 27.496  21.916  53.930  1.00 41.66  ? 94  ASN A CG  1 
ATOM   732   O OD1 . ASN A 1 98  ? 27.001  22.986  54.289  1.00 46.72  ? 94  ASN A OD1 1 
ATOM   733   N ND2 . ASN A 1 98  ? 28.190  21.791  52.801  1.00 47.98  ? 94  ASN A ND2 1 
ATOM   734   N N   . PHE A 1 99  ? 24.902  19.061  55.776  1.00 26.79  ? 95  PHE A N   1 
ATOM   735   C CA  . PHE A 1 99  ? 24.373  17.716  55.948  1.00 24.09  ? 95  PHE A CA  1 
ATOM   736   C C   . PHE A 1 99  ? 24.372  17.077  54.563  1.00 23.64  ? 95  PHE A C   1 
ATOM   737   O O   . PHE A 1 99  ? 23.666  17.527  53.669  1.00 21.05  ? 95  PHE A O   1 
ATOM   738   C CB  . PHE A 1 99  ? 22.968  17.773  56.534  1.00 23.28  ? 95  PHE A CB  1 
ATOM   739   C CG  . PHE A 1 99  ? 22.555  16.524  57.250  1.00 23.43  ? 95  PHE A CG  1 
ATOM   740   C CD1 . PHE A 1 99  ? 22.290  16.548  58.611  1.00 25.59  ? 95  PHE A CD1 1 
ATOM   741   C CD2 . PHE A 1 99  ? 22.423  15.325  56.570  1.00 24.18  ? 95  PHE A CD2 1 
ATOM   742   C CE1 . PHE A 1 99  ? 21.910  15.399  59.283  1.00 25.91  ? 95  PHE A CE1 1 
ATOM   743   C CE2 . PHE A 1 99  ? 22.039  14.173  57.235  1.00 24.50  ? 95  PHE A CE2 1 
ATOM   744   C CZ  . PHE A 1 99  ? 21.781  14.211  58.592  1.00 25.09  ? 95  PHE A CZ  1 
ATOM   745   N N   . ASN A 1 100 ? 25.181  16.038  54.386  1.00 26.06  ? 96  ASN A N   1 
ATOM   746   C CA  . ASN A 1 100 ? 25.356  15.416  53.074  1.00 25.04  ? 96  ASN A CA  1 
ATOM   747   C C   . ASN A 1 100 ? 24.131  14.608  52.656  1.00 25.56  ? 96  ASN A C   1 
ATOM   748   O O   . ASN A 1 100 ? 23.566  13.866  53.465  1.00 24.34  ? 96  ASN A O   1 
ATOM   749   C CB  . ASN A 1 100 ? 26.585  14.509  53.084  1.00 24.73  ? 96  ASN A CB  1 
ATOM   750   C CG  . ASN A 1 100 ? 27.030  14.110  51.699  1.00 24.48  ? 96  ASN A CG  1 
ATOM   751   O OD1 . ASN A 1 100 ? 27.356  14.959  50.876  1.00 25.42  ? 96  ASN A OD1 1 
ATOM   752   N ND2 . ASN A 1 100 ? 27.079  12.810  51.445  1.00 24.29  ? 96  ASN A ND2 1 
ATOM   753   N N   . ASP A 1 101 ? 23.735  14.758  51.392  1.00 26.53  ? 97  ASP A N   1 
ATOM   754   C CA  . ASP A 1 101 ? 22.554  14.087  50.842  1.00 28.55  ? 97  ASP A CA  1 
ATOM   755   C C   . ASP A 1 101 ? 21.339  14.267  51.753  1.00 24.35  ? 97  ASP A C   1 
ATOM   756   O O   . ASP A 1 101 ? 20.606  13.317  52.017  1.00 21.04  ? 97  ASP A O   1 
ATOM   757   C CB  . ASP A 1 101 ? 22.833  12.595  50.601  1.00 32.39  ? 97  ASP A CB  1 
ATOM   758   C CG  . ASP A 1 101 ? 23.803  12.353  49.459  1.00 37.25  ? 97  ASP A CG  1 
ATOM   759   O OD1 . ASP A 1 101 ? 23.872  13.183  48.523  1.00 46.34  ? 97  ASP A OD1 1 
ATOM   760   O OD2 . ASP A 1 101 ? 24.499  11.317  49.492  1.00 45.84  ? 97  ASP A OD2 1 
ATOM   761   N N   . TYR A 1 102 ? 21.137  15.501  52.210  1.00 24.02  ? 98  TYR A N   1 
ATOM   762   C CA  . TYR A 1 102 ? 20.084  15.826  53.160  1.00 25.62  ? 98  TYR A CA  1 
ATOM   763   C C   . TYR A 1 102 ? 18.706  15.557  52.589  1.00 25.96  ? 98  TYR A C   1 
ATOM   764   O O   . TYR A 1 102 ? 17.862  14.949  53.255  1.00 26.37  ? 98  TYR A O   1 
ATOM   765   C CB  . TYR A 1 102 ? 20.186  17.294  53.576  1.00 25.84  ? 98  TYR A CB  1 
ATOM   766   C CG  . TYR A 1 102 ? 19.197  17.742  54.640  1.00 26.04  ? 98  TYR A CG  1 
ATOM   767   C CD1 . TYR A 1 102 ? 18.803  16.892  55.675  1.00 24.50  ? 98  TYR A CD1 1 
ATOM   768   C CD2 . TYR A 1 102 ? 18.685  19.036  54.629  1.00 25.94  ? 98  TYR A CD2 1 
ATOM   769   C CE1 . TYR A 1 102 ? 17.911  17.310  56.651  1.00 23.87  ? 98  TYR A CE1 1 
ATOM   770   C CE2 . TYR A 1 102 ? 17.802  19.464  55.602  1.00 26.05  ? 98  TYR A CE2 1 
ATOM   771   C CZ  . TYR A 1 102 ? 17.420  18.598  56.614  1.00 25.49  ? 98  TYR A CZ  1 
ATOM   772   O OH  . TYR A 1 102 ? 16.540  19.026  57.577  1.00 25.86  ? 98  TYR A OH  1 
ATOM   773   N N   . GLU A 1 103 ? 18.495  15.995  51.354  1.00 25.78  ? 99  GLU A N   1 
ATOM   774   C CA  . GLU A 1 103 ? 17.187  15.899  50.707  1.00 28.48  ? 99  GLU A CA  1 
ATOM   775   C C   . GLU A 1 103 ? 16.760  14.448  50.478  1.00 29.30  ? 99  GLU A C   1 
ATOM   776   O O   . GLU A 1 103 ? 15.586  14.113  50.653  1.00 33.23  ? 99  GLU A O   1 
ATOM   777   C CB  . GLU A 1 103 ? 17.170  16.665  49.381  1.00 30.46  ? 99  GLU A CB  1 
ATOM   778   C CG  . GLU A 1 103 ? 17.278  18.181  49.524  1.00 35.08  ? 99  GLU A CG  1 
ATOM   779   C CD  . GLU A 1 103 ? 18.688  18.680  49.800  1.00 42.01  ? 99  GLU A CD  1 
ATOM   780   O OE1 . GLU A 1 103 ? 19.660  17.900  49.657  1.00 43.08  ? 99  GLU A OE1 1 
ATOM   781   O OE2 . GLU A 1 103 ? 18.823  19.866  50.173  1.00 51.47  ? 99  GLU A OE2 1 
ATOM   782   N N   . GLU A 1 104 ? 17.707  13.593  50.098  1.00 26.81  ? 100 GLU A N   1 
ATOM   783   C CA  . GLU A 1 104 ? 17.425  12.167  49.949  1.00 24.97  ? 100 GLU A CA  1 
ATOM   784   C C   . GLU A 1 104 ? 17.087  11.512  51.294  1.00 25.09  ? 100 GLU A C   1 
ATOM   785   O O   . GLU A 1 104 ? 16.243  10.620  51.351  1.00 22.78  ? 100 GLU A O   1 
ATOM   786   C CB  . GLU A 1 104 ? 18.588  11.445  49.264  1.00 23.91  ? 100 GLU A CB  1 
ATOM   787   C CG  . GLU A 1 104 ? 18.626  11.642  47.753  1.00 25.55  ? 100 GLU A CG  1 
ATOM   788   C CD  . GLU A 1 104 ? 17.448  10.983  47.031  1.00 28.31  ? 100 GLU A CD  1 
ATOM   789   O OE1 . GLU A 1 104 ? 17.192  9.779   47.269  1.00 29.53  ? 100 GLU A OE1 1 
ATOM   790   O OE2 . GLU A 1 104 ? 16.784  11.666  46.213  1.00 24.69  ? 100 GLU A OE2 1 
ATOM   791   N N   . LEU A 1 105 ? 17.730  11.968  52.369  1.00 24.80  ? 101 LEU A N   1 
ATOM   792   C CA  . LEU A 1 105 ? 17.436  11.454  53.706  1.00 24.31  ? 101 LEU A CA  1 
ATOM   793   C C   . LEU A 1 105 ? 16.043  11.883  54.164  1.00 26.58  ? 101 LEU A C   1 
ATOM   794   O O   . LEU A 1 105 ? 15.311  11.084  54.744  1.00 27.01  ? 101 LEU A O   1 
ATOM   795   C CB  . LEU A 1 105 ? 18.488  11.902  54.727  1.00 23.14  ? 101 LEU A CB  1 
ATOM   796   C CG  . LEU A 1 105 ? 18.311  11.369  56.163  1.00 22.60  ? 101 LEU A CG  1 
ATOM   797   C CD1 . LEU A 1 105 ? 18.322  9.848   56.198  1.00 22.04  ? 101 LEU A CD1 1 
ATOM   798   C CD2 . LEU A 1 105 ? 19.372  11.923  57.104  1.00 20.50  ? 101 LEU A CD2 1 
ATOM   799   N N   . LYS A 1 106 ? 15.685  13.142  53.916  1.00 27.48  ? 102 LYS A N   1 
ATOM   800   C CA  . LYS A 1 106 ? 14.343  13.626  54.234  1.00 28.83  ? 102 LYS A CA  1 
ATOM   801   C C   . LYS A 1 106 ? 13.312  12.797  53.488  1.00 26.59  ? 102 LYS A C   1 
ATOM   802   O O   . LYS A 1 106 ? 12.321  12.367  54.065  1.00 27.17  ? 102 LYS A O   1 
ATOM   803   C CB  . LYS A 1 106 ? 14.173  15.100  53.864  1.00 32.81  ? 102 LYS A CB  1 
ATOM   804   C CG  . LYS A 1 106 ? 14.927  16.066  54.763  1.00 34.69  ? 102 LYS A CG  1 
ATOM   805   C CD  . LYS A 1 106 ? 14.956  17.475  54.179  1.00 36.66  ? 102 LYS A CD  1 
ATOM   806   C CE  . LYS A 1 106 ? 13.784  18.316  54.655  1.00 39.86  ? 102 LYS A CE  1 
ATOM   807   N NZ  . LYS A 1 106 ? 13.889  19.734  54.216  1.00 45.92  ? 102 LYS A NZ  1 
ATOM   808   N N   . HIS A 1 107 ? 13.556  12.564  52.205  1.00 26.20  ? 103 HIS A N   1 
ATOM   809   C CA  . HIS A 1 107 ? 12.626  11.791  51.398  1.00 26.13  ? 103 HIS A CA  1 
ATOM   810   C C   . HIS A 1 107 ? 12.468  10.409  51.954  1.00 25.63  ? 103 HIS A C   1 
ATOM   811   O O   . HIS A 1 107 ? 11.348  9.924   52.104  1.00 23.60  ? 103 HIS A O   1 
ATOM   812   C CB  . HIS A 1 107 ? 13.077  11.714  49.949  1.00 25.34  ? 103 HIS A CB  1 
ATOM   813   C CG  . HIS A 1 107 ? 12.074  11.042  49.045  1.00 26.45  ? 103 HIS A CG  1 
ATOM   814   N ND1 . HIS A 1 107 ? 10.909  11.620  48.712  1.00 27.98  ? 103 HIS A ND1 1 
ATOM   815   C CD2 . HIS A 1 107 ? 12.090  9.798   48.421  1.00 26.96  ? 103 HIS A CD2 1 
ATOM   816   C CE1 . HIS A 1 107 ? 10.213  10.797  47.910  1.00 28.72  ? 103 HIS A CE1 1 
ATOM   817   N NE2 . HIS A 1 107 ? 10.937  9.679   47.732  1.00 29.53  ? 103 HIS A NE2 1 
ATOM   818   N N   . LEU A 1 108 ? 13.588  9.768   52.274  1.00 24.77  ? 104 LEU A N   1 
ATOM   819   C CA  . LEU A 1 108 ? 13.560  8.423   52.831  1.00 25.80  ? 104 LEU A CA  1 
ATOM   820   C C   . LEU A 1 108 ? 12.785  8.368   54.146  1.00 23.89  ? 104 LEU A C   1 
ATOM   821   O O   . LEU A 1 108 ? 12.049  7.419   54.387  1.00 23.31  ? 104 LEU A O   1 
ATOM   822   C CB  . LEU A 1 108 ? 14.982  7.899   53.051  1.00 29.44  ? 104 LEU A CB  1 
ATOM   823   C CG  . LEU A 1 108 ? 15.061  6.408   53.398  1.00 30.10  ? 104 LEU A CG  1 
ATOM   824   C CD1 . LEU A 1 108 ? 15.029  5.562   52.130  1.00 31.21  ? 104 LEU A CD1 1 
ATOM   825   C CD2 . LEU A 1 108 ? 16.309  6.125   54.218  1.00 29.52  ? 104 LEU A CD2 1 
ATOM   826   N N   . LEU A 1 109 ? 12.952  9.392   54.981  1.00 22.62  ? 105 LEU A N   1 
ATOM   827   C CA  . LEU A 1 109 ? 12.306  9.450   56.291  1.00 21.00  ? 105 LEU A CA  1 
ATOM   828   C C   . LEU A 1 109 ? 10.888  10.024  56.244  1.00 22.62  ? 105 LEU A C   1 
ATOM   829   O O   . LEU A 1 109 ? 10.249  10.148  57.285  1.00 25.16  ? 105 LEU A O   1 
ATOM   830   C CB  . LEU A 1 109 ? 13.146  10.290  57.260  1.00 19.31  ? 105 LEU A CB  1 
ATOM   831   C CG  . LEU A 1 109 ? 14.493  9.731   57.715  1.00 17.72  ? 105 LEU A CG  1 
ATOM   832   C CD1 . LEU A 1 109 ? 15.293  10.819  58.410  1.00 16.27  ? 105 LEU A CD1 1 
ATOM   833   C CD2 . LEU A 1 109 ? 14.312  8.543   58.647  1.00 18.77  ? 105 LEU A CD2 1 
ATOM   834   N N   . SER A 1 110 ? 10.387  10.365  55.060  1.00 23.49  ? 106 SER A N   1 
ATOM   835   C CA  . SER A 1 110 ? 9.058   10.972  54.940  1.00 26.15  ? 106 SER A CA  1 
ATOM   836   C C   . SER A 1 110 ? 7.932   10.062  55.440  1.00 25.10  ? 106 SER A C   1 
ATOM   837   O O   . SER A 1 110 ? 6.928   10.546  55.948  1.00 23.57  ? 106 SER A O   1 
ATOM   838   C CB  . SER A 1 110 ? 8.777   11.384  53.493  1.00 27.67  ? 106 SER A CB  1 
ATOM   839   O OG  . SER A 1 110 ? 8.677   10.248  52.651  1.00 31.78  ? 106 SER A OG  1 
ATOM   840   N N   . ARG A 1 111 ? 8.097   8.754   55.275  1.00 26.99  ? 107 ARG A N   1 
ATOM   841   C CA  . ARG A 1 111 ? 7.129   7.780   55.769  1.00 30.79  ? 107 ARG A CA  1 
ATOM   842   C C   . ARG A 1 111 ? 7.863   6.549   56.251  1.00 31.00  ? 107 ARG A C   1 
ATOM   843   O O   . ARG A 1 111 ? 8.557   5.895   55.471  1.00 32.79  ? 107 ARG A O   1 
ATOM   844   C CB  . ARG A 1 111 ? 6.140   7.396   54.669  1.00 34.25  ? 107 ARG A CB  1 
ATOM   845   C CG  . ARG A 1 111 ? 5.115   6.336   55.055  1.00 35.23  ? 107 ARG A CG  1 
ATOM   846   C CD  . ARG A 1 111 ? 4.095   6.146   53.969  1.00 40.38  ? 107 ARG A CD  1 
ATOM   847   N NE  . ARG A 1 111 ? 3.570   4.786   53.841  1.00 51.67  ? 107 ARG A NE  1 
ATOM   848   C CZ  . ARG A 1 111 ? 2.757   4.394   52.861  1.00 54.78  ? 107 ARG A CZ  1 
ATOM   849   N NH1 . ARG A 1 111 ? 2.401   5.254   51.908  1.00 55.58  ? 107 ARG A NH1 1 
ATOM   850   N NH2 . ARG A 1 111 ? 2.308   3.139   52.823  1.00 50.70  ? 107 ARG A NH2 1 
ATOM   851   N N   . ILE A 1 112 ? 7.699   6.239   57.534  1.00 29.47  ? 108 ILE A N   1 
ATOM   852   C CA  . ILE A 1 112 ? 8.406   5.136   58.170  1.00 29.73  ? 108 ILE A CA  1 
ATOM   853   C C   . ILE A 1 112 ? 7.425   4.241   58.921  1.00 30.82  ? 108 ILE A C   1 
ATOM   854   O O   . ILE A 1 112 ? 6.497   4.724   59.570  1.00 31.13  ? 108 ILE A O   1 
ATOM   855   C CB  . ILE A 1 112 ? 9.490   5.663   59.135  1.00 30.98  ? 108 ILE A CB  1 
ATOM   856   C CG1 . ILE A 1 112 ? 10.586  6.396   58.354  1.00 34.36  ? 108 ILE A CG1 1 
ATOM   857   C CG2 . ILE A 1 112 ? 10.107  4.530   59.940  1.00 29.46  ? 108 ILE A CG2 1 
ATOM   858   C CD1 . ILE A 1 112 ? 11.364  5.523   57.387  1.00 35.00  ? 108 ILE A CD1 1 
ATOM   859   N N   . ASN A 1 113 ? 7.634   2.933   58.808  1.00 32.36  ? 109 ASN A N   1 
ATOM   860   C CA  . ASN A 1 113 ? 6.784   1.941   59.455  1.00 33.51  ? 109 ASN A CA  1 
ATOM   861   C C   . ASN A 1 113 ? 7.212   1.700   60.900  1.00 33.64  ? 109 ASN A C   1 
ATOM   862   O O   . ASN A 1 113 ? 6.367   1.574   61.782  1.00 31.76  ? 109 ASN A O   1 
ATOM   863   C CB  . ASN A 1 113 ? 6.819   0.635   58.656  1.00 37.22  ? 109 ASN A CB  1 
ATOM   864   C CG  . ASN A 1 113 ? 5.778   -0.368  59.108  1.00 38.62  ? 109 ASN A CG  1 
ATOM   865   O OD1 . ASN A 1 113 ? 6.083   -1.545  59.315  1.00 38.99  ? 109 ASN A OD1 1 
ATOM   866   N ND2 . ASN A 1 113 ? 4.534   0.085   59.232  1.00 38.04  ? 109 ASN A ND2 1 
ATOM   867   N N   . HIS A 1 114 ? 8.522   1.640   61.136  1.00 36.51  ? 110 HIS A N   1 
ATOM   868   C CA  . HIS A 1 114 ? 9.065   1.502   62.494  1.00 33.79  ? 110 HIS A CA  1 
ATOM   869   C C   . HIS A 1 114 ? 10.310  2.327   62.679  1.00 31.73  ? 110 HIS A C   1 
ATOM   870   O O   . HIS A 1 114 ? 11.193  2.325   61.820  1.00 27.11  ? 110 HIS A O   1 
ATOM   871   C CB  . HIS A 1 114 ? 9.357   0.045   62.814  1.00 33.60  ? 110 HIS A CB  1 
ATOM   872   C CG  . HIS A 1 114 ? 9.744   -0.186  64.253  1.00 36.39  ? 110 HIS A CG  1 
ATOM   873   N ND1 . HIS A 1 114 ? 10.948  -0.663  64.609  1.00 40.89  ? 110 HIS A ND1 1 
ATOM   874   C CD2 . HIS A 1 114 ? 9.041   0.038   65.440  1.00 37.06  ? 110 HIS A CD2 1 
ATOM   875   C CE1 . HIS A 1 114 ? 11.014  -0.757  65.950  1.00 41.59  ? 110 HIS A CE1 1 
ATOM   876   N NE2 . HIS A 1 114 ? 9.845   -0.325  66.457  1.00 39.71  ? 110 HIS A NE2 1 
ATOM   877   N N   . PHE A 1 115 ? 10.391  3.027   63.810  1.00 30.57  ? 111 PHE A N   1 
ATOM   878   C CA  . PHE A 1 115 ? 11.496  3.943   64.088  1.00 29.75  ? 111 PHE A CA  1 
ATOM   879   C C   . PHE A 1 115 ? 11.861  3.943   65.574  1.00 31.19  ? 111 PHE A C   1 
ATOM   880   O O   . PHE A 1 115 ? 11.092  4.427   66.405  1.00 33.40  ? 111 PHE A O   1 
ATOM   881   C CB  . PHE A 1 115 ? 11.109  5.354   63.643  1.00 30.32  ? 111 PHE A CB  1 
ATOM   882   C CG  . PHE A 1 115 ? 12.272  6.302   63.543  1.00 30.69  ? 111 PHE A CG  1 
ATOM   883   C CD1 . PHE A 1 115 ? 13.155  6.222   62.477  1.00 29.39  ? 111 PHE A CD1 1 
ATOM   884   C CD2 . PHE A 1 115 ? 12.477  7.283   64.505  1.00 31.41  ? 111 PHE A CD2 1 
ATOM   885   C CE1 . PHE A 1 115 ? 14.228  7.092   62.374  1.00 30.23  ? 111 PHE A CE1 1 
ATOM   886   C CE2 . PHE A 1 115 ? 13.546  8.158   64.410  1.00 32.05  ? 111 PHE A CE2 1 
ATOM   887   C CZ  . PHE A 1 115 ? 14.423  8.063   63.340  1.00 31.60  ? 111 PHE A CZ  1 
ATOM   888   N N   . GLU A 1 116 ? 13.035  3.401   65.901  1.00 31.55  ? 112 GLU A N   1 
ATOM   889   C CA  . GLU A 1 116 ? 13.484  3.306   67.289  1.00 30.10  ? 112 GLU A CA  1 
ATOM   890   C C   . GLU A 1 116 ? 14.938  3.753   67.441  1.00 29.45  ? 112 GLU A C   1 
ATOM   891   O O   . GLU A 1 116 ? 15.840  3.189   66.816  1.00 26.57  ? 112 GLU A O   1 
ATOM   892   C CB  . GLU A 1 116 ? 13.327  1.867   67.793  1.00 31.94  ? 112 GLU A CB  1 
ATOM   893   C CG  . GLU A 1 116 ? 13.533  1.690   69.292  1.00 32.80  ? 112 GLU A CG  1 
ATOM   894   C CD  . GLU A 1 116 ? 13.527  0.232   69.723  1.00 35.66  ? 112 GLU A CD  1 
ATOM   895   O OE1 . GLU A 1 116 ? 12.849  -0.589  69.064  1.00 36.18  ? 112 GLU A OE1 1 
ATOM   896   O OE2 . GLU A 1 116 ? 14.203  -0.095  70.725  1.00 36.94  ? 112 GLU A OE2 1 
ATOM   897   N N   . LYS A 1 117 ? 15.153  4.764   68.283  1.00 31.03  ? 113 LYS A N   1 
ATOM   898   C CA  . LYS A 1 117 ? 16.498  5.211   68.641  1.00 31.69  ? 113 LYS A CA  1 
ATOM   899   C C   . LYS A 1 117 ? 17.186  4.145   69.491  1.00 30.66  ? 113 LYS A C   1 
ATOM   900   O O   . LYS A 1 117 ? 16.583  3.597   70.410  1.00 30.77  ? 113 LYS A O   1 
ATOM   901   C CB  . LYS A 1 117 ? 16.444  6.536   69.411  1.00 35.26  ? 113 LYS A CB  1 
ATOM   902   C CG  . LYS A 1 117 ? 17.810  7.173   69.644  1.00 42.08  ? 113 LYS A CG  1 
ATOM   903   C CD  . LYS A 1 117 ? 17.792  8.224   70.746  1.00 46.60  ? 113 LYS A CD  1 
ATOM   904   C CE  . LYS A 1 117 ? 17.243  9.555   70.262  1.00 50.70  ? 113 LYS A CE  1 
ATOM   905   N NZ  . LYS A 1 117 ? 17.621  10.645  71.206  1.00 51.72  ? 113 LYS A NZ  1 
ATOM   906   N N   . ILE A 1 118 ? 18.449  3.868   69.180  1.00 33.40  ? 114 ILE A N   1 
ATOM   907   C CA  . ILE A 1 118 ? 19.238  2.847   69.875  1.00 36.18  ? 114 ILE A CA  1 
ATOM   908   C C   . ILE A 1 118 ? 20.615  3.408   70.207  1.00 36.10  ? 114 ILE A C   1 
ATOM   909   O O   . ILE A 1 118 ? 21.227  4.072   69.368  1.00 34.11  ? 114 ILE A O   1 
ATOM   910   C CB  . ILE A 1 118 ? 19.435  1.593   68.989  1.00 38.79  ? 114 ILE A CB  1 
ATOM   911   C CG1 . ILE A 1 118 ? 18.100  0.896   68.710  1.00 41.04  ? 114 ILE A CG1 1 
ATOM   912   C CG2 . ILE A 1 118 ? 20.404  0.618   69.641  1.00 38.41  ? 114 ILE A CG2 1 
ATOM   913   C CD1 . ILE A 1 118 ? 17.372  0.425   69.952  1.00 39.37  ? 114 ILE A CD1 1 
ATOM   914   N N   . GLN A 1 119 ? 21.100  3.147   71.421  1.00 36.78  ? 115 GLN A N   1 
ATOM   915   C CA  . GLN A 1 119 ? 22.473  3.502   71.783  1.00 39.73  ? 115 GLN A CA  1 
ATOM   916   C C   . GLN A 1 119 ? 23.421  2.491   71.143  1.00 40.16  ? 115 GLN A C   1 
ATOM   917   O O   . GLN A 1 119 ? 23.329  1.298   71.431  1.00 39.27  ? 115 GLN A O   1 
ATOM   918   C CB  . GLN A 1 119 ? 22.669  3.507   73.300  1.00 41.52  ? 115 GLN A CB  1 
ATOM   919   C CG  . GLN A 1 119 ? 23.973  4.163   73.745  1.00 43.07  ? 115 GLN A CG  1 
ATOM   920   C CD  . GLN A 1 119 ? 24.242  3.999   75.228  1.00 44.35  ? 115 GLN A CD  1 
ATOM   921   O OE1 . GLN A 1 119 ? 24.331  2.879   75.734  1.00 45.37  ? 115 GLN A OE1 1 
ATOM   922   N NE2 . GLN A 1 119 ? 24.387  5.119   75.930  1.00 44.63  ? 115 GLN A NE2 1 
ATOM   923   N N   . ILE A 1 120 ? 24.313  2.967   70.271  1.00 40.80  ? 116 ILE A N   1 
ATOM   924   C CA  . ILE A 1 120 ? 25.280  2.084   69.583  1.00 43.47  ? 116 ILE A CA  1 
ATOM   925   C C   . ILE A 1 120 ? 26.608  1.987   70.332  1.00 43.37  ? 116 ILE A C   1 
ATOM   926   O O   . ILE A 1 120 ? 27.038  0.882   70.699  1.00 52.04  ? 116 ILE A O   1 
ATOM   927   C CB  . ILE A 1 120 ? 25.541  2.518   68.117  1.00 47.70  ? 116 ILE A CB  1 
ATOM   928   C CG1 . ILE A 1 120 ? 24.715  1.676   67.149  1.00 47.11  ? 116 ILE A CG1 1 
ATOM   929   C CG2 . ILE A 1 120 ? 27.012  2.349   67.740  1.00 56.31  ? 116 ILE A CG2 1 
ATOM   930   C CD1 . ILE A 1 120 ? 23.234  1.633   67.475  1.00 48.70  ? 116 ILE A CD1 1 
ATOM   931   N N   . ILE A 1 121 ? 27.233  3.148   70.557  1.00 39.66  ? 117 ILE A N   1 
ATOM   932   C CA  . ILE A 1 121 ? 28.531  3.242   71.238  1.00 41.99  ? 117 ILE A CA  1 
ATOM   933   C C   . ILE A 1 121 ? 28.299  4.205   72.398  1.00 40.20  ? 117 ILE A C   1 
ATOM   934   O O   . ILE A 1 121 ? 27.971  5.365   72.166  1.00 39.53  ? 117 ILE A O   1 
ATOM   935   C CB  . ILE A 1 121 ? 29.684  3.720   70.274  1.00 43.08  ? 117 ILE A CB  1 
ATOM   936   C CG1 . ILE A 1 121 ? 30.761  4.575   70.982  1.00 43.84  ? 117 ILE A CG1 1 
ATOM   937   C CG2 . ILE A 1 121 ? 29.126  4.488   69.087  1.00 41.74  ? 117 ILE A CG2 1 
ATOM   938   C CD1 . ILE A 1 121 ? 31.684  3.763   71.863  1.00 48.00  ? 117 ILE A CD1 1 
ATOM   939   N N   . PRO A 1 122 ? 28.418  3.718   73.647  1.00 42.34  ? 118 PRO A N   1 
ATOM   940   C CA  . PRO A 1 122 ? 28.080  4.577   74.789  1.00 44.35  ? 118 PRO A CA  1 
ATOM   941   C C   . PRO A 1 122 ? 29.121  5.663   75.019  1.00 41.62  ? 118 PRO A C   1 
ATOM   942   O O   . PRO A 1 122 ? 30.304  5.435   74.795  1.00 43.93  ? 118 PRO A O   1 
ATOM   943   C CB  . PRO A 1 122 ? 28.013  3.603   75.975  1.00 45.78  ? 118 PRO A CB  1 
ATOM   944   C CG  . PRO A 1 122 ? 28.782  2.404   75.557  1.00 47.20  ? 118 PRO A CG  1 
ATOM   945   C CD  . PRO A 1 122 ? 28.789  2.350   74.058  1.00 46.51  ? 118 PRO A CD  1 
ATOM   946   N N   . LYS A 1 123 ? 28.671  6.831   75.468  1.00 41.49  ? 119 LYS A N   1 
ATOM   947   C CA  . LYS A 1 123 ? 29.553  7.984   75.679  1.00 44.70  ? 119 LYS A CA  1 
ATOM   948   C C   . LYS A 1 123 ? 30.674  7.692   76.693  1.00 45.87  ? 119 LYS A C   1 
ATOM   949   O O   . LYS A 1 123 ? 31.776  8.229   76.580  1.00 41.23  ? 119 LYS A O   1 
ATOM   950   C CB  . LYS A 1 123 ? 28.731  9.199   76.129  1.00 46.14  ? 119 LYS A CB  1 
ATOM   951   C CG  . LYS A 1 123 ? 29.462  10.531  76.007  1.00 51.47  ? 119 LYS A CG  1 
ATOM   952   C CD  . LYS A 1 123 ? 28.787  11.658  76.796  1.00 53.10  ? 119 LYS A CD  1 
ATOM   953   C CE  . LYS A 1 123 ? 28.456  12.863  75.918  1.00 55.59  ? 119 LYS A CE  1 
ATOM   954   N NZ  . LYS A 1 123 ? 28.201  14.095  76.718  1.00 56.40  ? 119 LYS A NZ  1 
ATOM   955   N N   . ASN A 1 124 ? 30.389  6.833   77.671  1.00 49.05  ? 120 ASN A N   1 
ATOM   956   C CA  . ASN A 1 124 ? 31.387  6.434   78.676  1.00 49.65  ? 120 ASN A CA  1 
ATOM   957   C C   . ASN A 1 124 ? 32.476  5.476   78.157  1.00 52.46  ? 120 ASN A C   1 
ATOM   958   O O   . ASN A 1 124 ? 33.472  5.244   78.834  1.00 54.17  ? 120 ASN A O   1 
ATOM   959   C CB  . ASN A 1 124 ? 30.702  5.836   79.921  1.00 51.14  ? 120 ASN A CB  1 
ATOM   960   C CG  . ASN A 1 124 ? 29.813  4.637   79.610  1.00 51.52  ? 120 ASN A CG  1 
ATOM   961   O OD1 . ASN A 1 124 ? 30.192  3.731   78.868  1.00 49.95  ? 120 ASN A OD1 1 
ATOM   962   N ND2 . ASN A 1 124 ? 28.627  4.617   80.210  1.00 52.38  ? 120 ASN A ND2 1 
ATOM   963   N N   . SER A 1 125 ? 32.279  4.933   76.957  1.00 53.19  ? 121 SER A N   1 
ATOM   964   C CA  . SER A 1 125 ? 33.158  3.925   76.366  1.00 52.08  ? 121 SER A CA  1 
ATOM   965   C C   . SER A 1 125 ? 34.474  4.509   75.816  1.00 45.77  ? 121 SER A C   1 
ATOM   966   O O   . SER A 1 125 ? 35.401  3.765   75.493  1.00 44.68  ? 121 SER A O   1 
ATOM   967   C CB  . SER A 1 125 ? 32.352  3.196   75.276  1.00 56.52  ? 121 SER A CB  1 
ATOM   968   O OG  . SER A 1 125 ? 32.857  1.934   74.879  1.00 64.29  ? 121 SER A OG  1 
ATOM   969   N N   . TRP A 1 126 ? 34.563  5.834   75.731  1.00 42.71  ? 122 TRP A N   1 
ATOM   970   C CA  . TRP A 1 126 ? 35.782  6.503   75.261  1.00 40.62  ? 122 TRP A CA  1 
ATOM   971   C C   . TRP A 1 126 ? 36.717  6.758   76.413  1.00 43.91  ? 122 TRP A C   1 
ATOM   972   O O   . TRP A 1 126 ? 36.557  7.733   77.151  1.00 44.52  ? 122 TRP A O   1 
ATOM   973   C CB  . TRP A 1 126 ? 35.439  7.819   74.571  1.00 35.30  ? 122 TRP A CB  1 
ATOM   974   C CG  . TRP A 1 126 ? 34.495  7.668   73.409  1.00 32.41  ? 122 TRP A CG  1 
ATOM   975   C CD1 . TRP A 1 126 ? 33.148  8.016   73.361  1.00 29.18  ? 122 TRP A CD1 1 
ATOM   976   C CD2 . TRP A 1 126 ? 34.795  7.117   72.080  1.00 30.75  ? 122 TRP A CD2 1 
ATOM   977   N NE1 . TRP A 1 126 ? 32.617  7.730   72.131  1.00 28.97  ? 122 TRP A NE1 1 
ATOM   978   C CE2 . TRP A 1 126 ? 33.549  7.190   71.318  1.00 29.56  ? 122 TRP A CE2 1 
ATOM   979   C CE3 . TRP A 1 126 ? 35.928  6.600   71.469  1.00 30.23  ? 122 TRP A CE3 1 
ATOM   980   C CZ2 . TRP A 1 126 ? 33.465  6.752   70.003  1.00 29.21  ? 122 TRP A CZ2 1 
ATOM   981   C CZ3 . TRP A 1 126 ? 35.832  6.161   70.143  1.00 28.03  ? 122 TRP A CZ3 1 
ATOM   982   C CH2 . TRP A 1 126 ? 34.629  6.234   69.431  1.00 28.78  ? 122 TRP A CH2 1 
ATOM   983   N N   . SER A 1 127 ? 37.703  5.880   76.581  1.00 44.84  ? 123 SER A N   1 
ATOM   984   C CA  . SER A 1 127 ? 38.616  5.953   77.723  1.00 47.24  ? 123 SER A CA  1 
ATOM   985   C C   . SER A 1 127 ? 39.876  6.769   77.419  1.00 46.13  ? 123 SER A C   1 
ATOM   986   O O   . SER A 1 127 ? 40.392  7.452   78.302  1.00 46.52  ? 123 SER A O   1 
ATOM   987   C CB  . SER A 1 127 ? 38.991  4.543   78.194  1.00 48.21  ? 123 SER A CB  1 
ATOM   988   O OG  . SER A 1 127 ? 39.433  3.740   77.116  1.00 55.22  ? 123 SER A OG  1 
ATOM   989   N N   . ASP A 1 128 ? 40.359  6.701   76.178  1.00 43.77  ? 124 ASP A N   1 
ATOM   990   C CA  . ASP A 1 128 ? 41.567  7.427   75.763  1.00 43.61  ? 124 ASP A CA  1 
ATOM   991   C C   . ASP A 1 128 ? 41.273  8.792   75.131  1.00 37.99  ? 124 ASP A C   1 
ATOM   992   O O   . ASP A 1 128 ? 42.190  9.478   74.677  1.00 33.65  ? 124 ASP A O   1 
ATOM   993   C CB  . ASP A 1 128 ? 42.383  6.574   74.786  1.00 46.14  ? 124 ASP A CB  1 
ATOM   994   C CG  . ASP A 1 128 ? 42.849  5.269   75.405  1.00 48.79  ? 124 ASP A CG  1 
ATOM   995   O OD1 . ASP A 1 128 ? 43.581  5.326   76.415  1.00 52.32  ? 124 ASP A OD1 1 
ATOM   996   O OD2 . ASP A 1 128 ? 42.487  4.188   74.887  1.00 50.42  ? 124 ASP A OD2 1 
ATOM   997   N N   . HIS A 1 129 ? 40.001  9.180   75.107  1.00 37.23  ? 125 HIS A N   1 
ATOM   998   C CA  . HIS A 1 129 ? 39.586  10.477  74.575  1.00 36.71  ? 125 HIS A CA  1 
ATOM   999   C C   . HIS A 1 129 ? 38.579  11.110  75.490  1.00 36.43  ? 125 HIS A C   1 
ATOM   1000  O O   . HIS A 1 129 ? 37.917  10.419  76.265  1.00 33.63  ? 125 HIS A O   1 
ATOM   1001  C CB  . HIS A 1 129 ? 38.985  10.312  73.187  1.00 34.85  ? 125 HIS A CB  1 
ATOM   1002  C CG  . HIS A 1 129 ? 39.910  9.648   72.194  1.00 34.13  ? 125 HIS A CG  1 
ATOM   1003  N ND1 . HIS A 1 129 ? 40.077  8.314   72.143  1.00 33.28  ? 125 HIS A ND1 1 
ATOM   1004  C CD2 . HIS A 1 129 ? 40.724  10.185  71.197  1.00 33.70  ? 125 HIS A CD2 1 
ATOM   1005  C CE1 . HIS A 1 129 ? 40.952  8.009   71.169  1.00 34.81  ? 125 HIS A CE1 1 
ATOM   1006  N NE2 . HIS A 1 129 ? 41.348  9.155   70.590  1.00 34.70  ? 125 HIS A NE2 1 
ATOM   1007  N N   . GLU A 1 130 ? 38.464  12.433  75.415  1.00 35.06  ? 126 GLU A N   1 
ATOM   1008  C CA  . GLU A 1 130 ? 37.486  13.169  76.213  1.00 36.71  ? 126 GLU A CA  1 
ATOM   1009  C C   . GLU A 1 130 ? 36.172  13.278  75.447  1.00 36.93  ? 126 GLU A C   1 
ATOM   1010  O O   . GLU A 1 130 ? 36.135  13.844  74.354  1.00 38.63  ? 126 GLU A O   1 
ATOM   1011  C CB  . GLU A 1 130 ? 38.015  14.559  76.560  1.00 38.87  ? 126 GLU A CB  1 
ATOM   1012  C CG  . GLU A 1 130 ? 39.091  14.548  77.640  1.00 43.82  ? 126 GLU A CG  1 
ATOM   1013  C CD  . GLU A 1 130 ? 38.529  14.509  79.057  1.00 47.29  ? 126 GLU A CD  1 
ATOM   1014  O OE1 . GLU A 1 130 ? 37.306  14.308  79.231  1.00 49.46  ? 126 GLU A OE1 1 
ATOM   1015  O OE2 . GLU A 1 130 ? 39.322  14.677  80.009  1.00 50.07  ? 126 GLU A OE2 1 
ATOM   1016  N N   . ALA A 1 131 ? 35.104  12.728  76.023  1.00 33.38  ? 127 ALA A N   1 
ATOM   1017  C CA  . ALA A 1 131 ? 33.784  12.724  75.396  1.00 34.72  ? 127 ALA A CA  1 
ATOM   1018  C C   . ALA A 1 131 ? 32.835  13.784  75.971  1.00 35.42  ? 127 ALA A C   1 
ATOM   1019  O O   . ALA A 1 131 ? 31.691  13.893  75.530  1.00 33.08  ? 127 ALA A O   1 
ATOM   1020  C CB  . ALA A 1 131 ? 33.159  11.345  75.522  1.00 35.61  ? 127 ALA A CB  1 
ATOM   1021  N N   . SER A 1 132 ? 33.312  14.569  76.935  1.00 37.05  ? 128 SER A N   1 
ATOM   1022  C CA  . SER A 1 132 ? 32.461  15.528  77.644  1.00 38.21  ? 128 SER A CA  1 
ATOM   1023  C C   . SER A 1 132 ? 32.897  16.987  77.495  1.00 39.69  ? 128 SER A C   1 
ATOM   1024  O O   . SER A 1 132 ? 32.284  17.872  78.087  1.00 42.44  ? 128 SER A O   1 
ATOM   1025  C CB  . SER A 1 132 ? 32.392  15.158  79.125  1.00 39.77  ? 128 SER A CB  1 
ATOM   1026  O OG  . SER A 1 132 ? 31.726  13.923  79.298  1.00 40.15  ? 128 SER A OG  1 
ATOM   1027  N N   . LEU A 1 133 ? 33.938  17.247  76.706  1.00 43.75  ? 129 LEU A N   1 
ATOM   1028  C CA  . LEU A 1 133 ? 34.393  18.619  76.459  1.00 44.10  ? 129 LEU A CA  1 
ATOM   1029  C C   . LEU A 1 133 ? 33.885  19.166  75.119  1.00 43.02  ? 129 LEU A C   1 
ATOM   1030  O O   . LEU A 1 133 ? 34.069  20.349  74.825  1.00 46.12  ? 129 LEU A O   1 
ATOM   1031  C CB  . LEU A 1 133 ? 35.926  18.696  76.522  1.00 46.06  ? 129 LEU A CB  1 
ATOM   1032  C CG  . LEU A 1 133 ? 36.603  18.688  77.905  1.00 48.61  ? 129 LEU A CG  1 
ATOM   1033  C CD1 . LEU A 1 133 ? 37.122  20.073  78.270  1.00 52.56  ? 129 LEU A CD1 1 
ATOM   1034  C CD2 . LEU A 1 133 ? 35.698  18.139  79.002  1.00 49.02  ? 129 LEU A CD2 1 
ATOM   1035  N N   . GLY A 1 134 ? 33.243  18.316  74.318  1.00 40.50  ? 130 GLY A N   1 
ATOM   1036  C CA  . GLY A 1 134 ? 32.715  18.717  73.015  1.00 38.19  ? 130 GLY A CA  1 
ATOM   1037  C C   . GLY A 1 134 ? 31.424  19.508  73.139  1.00 36.47  ? 130 GLY A C   1 
ATOM   1038  O O   . GLY A 1 134 ? 30.332  18.941  73.085  1.00 35.24  ? 130 GLY A O   1 
ATOM   1039  N N   . VAL A 1 135 ? 31.562  20.826  73.267  1.00 33.15  ? 131 VAL A N   1 
ATOM   1040  C CA  . VAL A 1 135 ? 30.445  21.712  73.587  1.00 32.92  ? 131 VAL A CA  1 
ATOM   1041  C C   . VAL A 1 135 ? 30.702  23.111  73.005  1.00 31.05  ? 131 VAL A C   1 
ATOM   1042  O O   . VAL A 1 135 ? 31.852  23.507  72.820  1.00 30.45  ? 131 VAL A O   1 
ATOM   1043  C CB  . VAL A 1 135 ? 30.251  21.760  75.123  1.00 34.88  ? 131 VAL A CB  1 
ATOM   1044  C CG1 . VAL A 1 135 ? 29.745  23.116  75.585  1.00 37.23  ? 131 VAL A CG1 1 
ATOM   1045  C CG2 . VAL A 1 135 ? 29.330  20.641  75.590  1.00 32.01  ? 131 VAL A CG2 1 
ATOM   1046  N N   . SER A 1 136 ? 29.633  23.842  72.690  1.00 31.49  ? 132 SER A N   1 
ATOM   1047  C CA  . SER A 1 136 ? 29.749  25.134  71.993  1.00 33.56  ? 132 SER A CA  1 
ATOM   1048  C C   . SER A 1 136 ? 28.658  26.129  72.376  1.00 34.75  ? 132 SER A C   1 
ATOM   1049  O O   . SER A 1 136 ? 27.534  25.746  72.709  1.00 35.10  ? 132 SER A O   1 
ATOM   1050  C CB  . SER A 1 136 ? 29.710  24.922  70.475  1.00 35.12  ? 132 SER A CB  1 
ATOM   1051  O OG  . SER A 1 136 ? 29.687  26.161  69.775  1.00 34.98  ? 132 SER A OG  1 
ATOM   1052  N N   . ALA A 1 137 ? 29.003  27.414  72.311  1.00 35.45  ? 133 ALA A N   1 
ATOM   1053  C CA  . ALA A 1 137 ? 28.068  28.497  72.621  1.00 37.00  ? 133 ALA A CA  1 
ATOM   1054  C C   . ALA A 1 137 ? 26.993  28.666  71.541  1.00 39.04  ? 133 ALA A C   1 
ATOM   1055  O O   . ALA A 1 137 ? 25.957  29.287  71.788  1.00 41.30  ? 133 ALA A O   1 
ATOM   1056  C CB  . ALA A 1 137 ? 28.825  29.805  72.818  1.00 36.53  ? 133 ALA A CB  1 
ATOM   1057  N N   . ALA A 1 138 ? 27.248  28.125  70.349  1.00 38.00  ? 134 ALA A N   1 
ATOM   1058  C CA  . ALA A 1 138 ? 26.265  28.124  69.265  1.00 36.15  ? 134 ALA A CA  1 
ATOM   1059  C C   . ALA A 1 138 ? 25.098  27.171  69.538  1.00 37.44  ? 134 ALA A C   1 
ATOM   1060  O O   . ALA A 1 138 ? 24.028  27.321  68.937  1.00 35.64  ? 134 ALA A O   1 
ATOM   1061  C CB  . ALA A 1 138 ? 26.937  27.763  67.943  1.00 34.86  ? 134 ALA A CB  1 
ATOM   1062  N N   . CYS A 1 139 ? 25.304  26.203  70.434  1.00 36.70  ? 135 CYS A N   1 
ATOM   1063  C CA  . CYS A 1 139 ? 24.263  25.248  70.820  1.00 37.27  ? 135 CYS A CA  1 
ATOM   1064  C C   . CYS A 1 139 ? 23.973  25.303  72.326  1.00 39.60  ? 135 CYS A C   1 
ATOM   1065  O O   . CYS A 1 139 ? 24.327  24.377  73.058  1.00 40.77  ? 135 CYS A O   1 
ATOM   1066  C CB  . CYS A 1 139 ? 24.687  23.826  70.435  1.00 37.38  ? 135 CYS A CB  1 
ATOM   1067  S SG  . CYS A 1 139 ? 25.145  23.602  68.701  1.00 37.98  ? 135 CYS A SG  1 
ATOM   1068  N N   . PRO A 1 140 ? 23.315  26.380  72.799  1.00 44.16  ? 136 PRO A N   1 
ATOM   1069  C CA  . PRO A 1 140 ? 22.986  26.470  74.228  1.00 46.53  ? 136 PRO A CA  1 
ATOM   1070  C C   . PRO A 1 140 ? 21.797  25.587  74.613  1.00 47.81  ? 136 PRO A C   1 
ATOM   1071  O O   . PRO A 1 140 ? 20.885  25.412  73.805  1.00 48.62  ? 136 PRO A O   1 
ATOM   1072  C CB  . PRO A 1 140 ? 22.640  27.953  74.424  1.00 45.44  ? 136 PRO A CB  1 
ATOM   1073  C CG  . PRO A 1 140 ? 22.394  28.515  73.060  1.00 45.75  ? 136 PRO A CG  1 
ATOM   1074  C CD  . PRO A 1 140 ? 22.706  27.475  72.025  1.00 44.59  ? 136 PRO A CD  1 
ATOM   1075  N N   . TYR A 1 141 ? 21.816  25.044  75.831  1.00 54.24  ? 137 TYR A N   1 
ATOM   1076  C CA  . TYR A 1 141 ? 20.735  24.175  76.327  1.00 62.37  ? 137 TYR A CA  1 
ATOM   1077  C C   . TYR A 1 141 ? 19.830  24.918  77.324  1.00 67.94  ? 137 TYR A C   1 
ATOM   1078  O O   . TYR A 1 141 ? 18.755  25.382  76.938  1.00 74.44  ? 137 TYR A O   1 
ATOM   1079  C CB  . TYR A 1 141 ? 21.322  22.884  76.917  1.00 68.65  ? 137 TYR A CB  1 
ATOM   1080  C CG  . TYR A 1 141 ? 20.325  21.826  77.334  1.00 77.64  ? 137 TYR A CG  1 
ATOM   1081  C CD1 . TYR A 1 141 ? 19.344  21.386  76.450  1.00 84.48  ? 137 TYR A CD1 1 
ATOM   1082  C CD2 . TYR A 1 141 ? 20.394  21.221  78.592  1.00 85.35  ? 137 TYR A CD2 1 
ATOM   1083  C CE1 . TYR A 1 141 ? 18.436  20.405  76.809  1.00 87.88  ? 137 TYR A CE1 1 
ATOM   1084  C CE2 . TYR A 1 141 ? 19.488  20.235  78.961  1.00 90.11  ? 137 TYR A CE2 1 
ATOM   1085  C CZ  . TYR A 1 141 ? 18.512  19.831  78.065  1.00 92.89  ? 137 TYR A CZ  1 
ATOM   1086  O OH  . TYR A 1 141 ? 17.611  18.854  78.424  1.00 91.92  ? 137 TYR A OH  1 
ATOM   1087  N N   . GLN A 1 142 ? 20.251  25.045  78.585  1.00 68.54  ? 138 GLN A N   1 
ATOM   1088  C CA  . GLN A 1 142 ? 19.524  25.911  79.543  1.00 68.67  ? 138 GLN A CA  1 
ATOM   1089  C C   . GLN A 1 142 ? 20.501  26.975  80.033  1.00 67.71  ? 138 GLN A C   1 
ATOM   1090  O O   . GLN A 1 142 ? 20.826  27.086  81.215  1.00 61.84  ? 138 GLN A O   1 
ATOM   1091  C CB  . GLN A 1 142 ? 18.786  25.141  80.677  1.00 71.90  ? 138 GLN A CB  1 
ATOM   1092  C CG  . GLN A 1 142 ? 19.562  23.981  81.292  1.00 71.43  ? 138 GLN A CG  1 
ATOM   1093  C CD  . GLN A 1 142 ? 18.657  22.894  81.875  1.00 71.23  ? 138 GLN A CD  1 
ATOM   1094  O OE1 . GLN A 1 142 ? 17.729  22.407  81.223  1.00 71.64  ? 138 GLN A OE1 1 
ATOM   1095  N NE2 . GLN A 1 142 ? 18.934  22.508  83.115  1.00 70.81  ? 138 GLN A NE2 1 
ATOM   1096  N N   . GLY A 1 143 ? 20.977  27.752  79.064  1.00 67.49  ? 139 GLY A N   1 
ATOM   1097  C CA  . GLY A 1 143 ? 21.929  28.829  79.312  1.00 66.79  ? 139 GLY A CA  1 
ATOM   1098  C C   . GLY A 1 143 ? 23.376  28.399  79.140  1.00 62.60  ? 139 GLY A C   1 
ATOM   1099  O O   . GLY A 1 143 ? 24.190  29.154  78.597  1.00 63.00  ? 139 GLY A O   1 
ATOM   1100  N N   . LYS A 1 144 ? 23.698  27.193  79.607  1.00 59.66  ? 140 LYS A N   1 
ATOM   1101  C CA  . LYS A 1 144 ? 25.046  26.637  79.453  1.00 60.07  ? 140 LYS A CA  1 
ATOM   1102  C C   . LYS A 1 144 ? 25.239  26.076  78.027  1.00 56.73  ? 140 LYS A C   1 
ATOM   1103  O O   . LYS A 1 144 ? 24.296  25.582  77.379  1.00 59.76  ? 140 LYS A O   1 
ATOM   1104  C CB  . LYS A 1 144 ? 25.356  25.621  80.574  1.00 60.38  ? 140 LYS A CB  1 
ATOM   1105  C CG  . LYS A 1 144 ? 24.638  24.285  80.490  1.00 62.37  ? 140 LYS A CG  1 
ATOM   1106  C CD  . LYS A 1 144 ? 24.559  23.669  81.893  1.00 64.67  ? 140 LYS A CD  1 
ATOM   1107  C CE  . LYS A 1 144 ? 25.914  23.244  82.459  1.00 63.13  ? 140 LYS A CE  1 
ATOM   1108  N NZ  . LYS A 1 144 ? 26.582  22.207  81.627  1.00 63.01  ? 140 LYS A NZ  1 
ATOM   1109  N N   . SER A 1 145 ? 26.458  26.226  77.524  1.00 46.98  ? 141 SER A N   1 
ATOM   1110  C CA  . SER A 1 145 ? 26.798  25.801  76.169  1.00 46.61  ? 141 SER A CA  1 
ATOM   1111  C C   . SER A 1 145 ? 26.784  24.277  76.062  1.00 41.78  ? 141 SER A C   1 
ATOM   1112  O O   . SER A 1 145 ? 27.237  23.587  76.976  1.00 39.23  ? 141 SER A O   1 
ATOM   1113  C CB  . SER A 1 145 ? 28.170  26.353  75.777  1.00 44.78  ? 141 SER A CB  1 
ATOM   1114  O OG  . SER A 1 145 ? 29.149  26.004  76.735  1.00 46.09  ? 141 SER A OG  1 
ATOM   1115  N N   . SER A 1 146 ? 26.266  23.765  74.945  1.00 37.47  ? 142 SER A N   1 
ATOM   1116  C CA  . SER A 1 146 ? 26.066  22.323  74.761  1.00 35.96  ? 142 SER A CA  1 
ATOM   1117  C C   . SER A 1 146 ? 26.313  21.895  73.305  1.00 33.30  ? 142 SER A C   1 
ATOM   1118  O O   . SER A 1 146 ? 27.072  22.543  72.582  1.00 31.71  ? 142 SER A O   1 
ATOM   1119  C CB  . SER A 1 146 ? 24.651  21.935  75.213  1.00 36.81  ? 142 SER A CB  1 
ATOM   1120  O OG  . SER A 1 146 ? 24.499  20.526  75.283  1.00 35.60  ? 142 SER A OG  1 
ATOM   1121  N N   . PHE A 1 147 ? 25.679  20.800  72.887  1.00 29.82  ? 143 PHE A N   1 
ATOM   1122  C CA  . PHE A 1 147 ? 25.892  20.228  71.564  1.00 28.13  ? 143 PHE A CA  1 
ATOM   1123  C C   . PHE A 1 147 ? 24.754  19.265  71.205  1.00 27.65  ? 143 PHE A C   1 
ATOM   1124  O O   . PHE A 1 147 ? 23.936  18.927  72.056  1.00 24.88  ? 143 PHE A O   1 
ATOM   1125  C CB  . PHE A 1 147 ? 27.239  19.489  71.542  1.00 27.20  ? 143 PHE A CB  1 
ATOM   1126  C CG  . PHE A 1 147 ? 27.748  19.174  70.160  1.00 27.58  ? 143 PHE A CG  1 
ATOM   1127  C CD1 . PHE A 1 147 ? 28.069  20.194  69.270  1.00 26.48  ? 143 PHE A CD1 1 
ATOM   1128  C CD2 . PHE A 1 147 ? 27.917  17.857  69.752  1.00 27.83  ? 143 PHE A CD2 1 
ATOM   1129  C CE1 . PHE A 1 147 ? 28.540  19.906  68.000  1.00 27.32  ? 143 PHE A CE1 1 
ATOM   1130  C CE2 . PHE A 1 147 ? 28.388  17.563  68.485  1.00 29.61  ? 143 PHE A CE2 1 
ATOM   1131  C CZ  . PHE A 1 147 ? 28.703  18.588  67.606  1.00 28.97  ? 143 PHE A CZ  1 
ATOM   1132  N N   . PHE A 1 148 ? 24.705  18.839  69.941  1.00 29.41  ? 144 PHE A N   1 
ATOM   1133  C CA  . PHE A 1 148 ? 23.764  17.806  69.497  1.00 28.10  ? 144 PHE A CA  1 
ATOM   1134  C C   . PHE A 1 148 ? 23.853  16.609  70.436  1.00 28.12  ? 144 PHE A C   1 
ATOM   1135  O O   . PHE A 1 148 ? 24.945  16.114  70.711  1.00 34.78  ? 144 PHE A O   1 
ATOM   1136  C CB  . PHE A 1 148 ? 24.074  17.352  68.067  1.00 27.03  ? 144 PHE A CB  1 
ATOM   1137  C CG  . PHE A 1 148 ? 24.034  18.457  67.052  1.00 26.02  ? 144 PHE A CG  1 
ATOM   1138  C CD1 . PHE A 1 148 ? 25.208  19.087  66.644  1.00 26.33  ? 144 PHE A CD1 1 
ATOM   1139  C CD2 . PHE A 1 148 ? 22.835  18.860  66.493  1.00 24.36  ? 144 PHE A CD2 1 
ATOM   1140  C CE1 . PHE A 1 148 ? 25.179  20.102  65.708  1.00 24.64  ? 144 PHE A CE1 1 
ATOM   1141  C CE2 . PHE A 1 148 ? 22.799  19.873  65.553  1.00 23.97  ? 144 PHE A CE2 1 
ATOM   1142  C CZ  . PHE A 1 148 ? 23.970  20.496  65.162  1.00 25.32  ? 144 PHE A CZ  1 
ATOM   1143  N N   . ARG A 1 149 ? 22.707  16.152  70.926  1.00 27.61  ? 145 ARG A N   1 
ATOM   1144  C CA  . ARG A 1 149 ? 22.663  15.146  71.989  1.00 28.82  ? 145 ARG A CA  1 
ATOM   1145  C C   . ARG A 1 149 ? 22.907  13.715  71.513  1.00 25.81  ? 145 ARG A C   1 
ATOM   1146  O O   . ARG A 1 149 ? 23.325  12.867  72.299  1.00 23.27  ? 145 ARG A O   1 
ATOM   1147  C CB  . ARG A 1 149 ? 21.317  15.215  72.722  1.00 31.80  ? 145 ARG A CB  1 
ATOM   1148  C CG  . ARG A 1 149 ? 21.108  16.481  73.539  1.00 34.30  ? 145 ARG A CG  1 
ATOM   1149  C CD  . ARG A 1 149 ? 19.739  16.416  74.230  1.00 39.52  ? 145 ARG A CD  1 
ATOM   1150  N NE  . ARG A 1 149 ? 18.675  16.444  73.217  1.00 40.70  ? 145 ARG A NE  1 
ATOM   1151  C CZ  . ARG A 1 149 ? 17.849  17.463  72.955  1.00 42.17  ? 145 ARG A CZ  1 
ATOM   1152  N NH1 . ARG A 1 149 ? 17.882  18.602  73.648  1.00 44.83  ? 145 ARG A NH1 1 
ATOM   1153  N NH2 . ARG A 1 149 ? 16.949  17.329  71.983  1.00 42.81  ? 145 ARG A NH2 1 
ATOM   1154  N N   . ASN A 1 150 ? 22.637  13.438  70.240  1.00 25.35  ? 146 ASN A N   1 
ATOM   1155  C CA  . ASN A 1 150 ? 22.736  12.071  69.724  1.00 25.17  ? 146 ASN A CA  1 
ATOM   1156  C C   . ASN A 1 150 ? 24.113  11.729  69.166  1.00 24.14  ? 146 ASN A C   1 
ATOM   1157  O O   . ASN A 1 150 ? 24.318  10.627  68.650  1.00 25.23  ? 146 ASN A O   1 
ATOM   1158  C CB  . ASN A 1 150 ? 21.665  11.818  68.657  1.00 25.63  ? 146 ASN A CB  1 
ATOM   1159  C CG  . ASN A 1 150 ? 20.259  12.033  69.177  1.00 26.15  ? 146 ASN A CG  1 
ATOM   1160  O OD1 . ASN A 1 150 ? 19.977  11.798  70.352  1.00 31.76  ? 146 ASN A OD1 1 
ATOM   1161  N ND2 . ASN A 1 150 ? 19.364  12.464  68.299  1.00 25.25  ? 146 ASN A ND2 1 
ATOM   1162  N N   . VAL A 1 151 ? 25.056  12.660  69.296  1.00 23.44  ? 147 VAL A N   1 
ATOM   1163  C CA  . VAL A 1 151 ? 26.355  12.554  68.644  1.00 23.10  ? 147 VAL A CA  1 
ATOM   1164  C C   . VAL A 1 151 ? 27.432  13.163  69.560  1.00 24.10  ? 147 VAL A C   1 
ATOM   1165  O O   . VAL A 1 151 ? 27.165  14.130  70.278  1.00 23.37  ? 147 VAL A O   1 
ATOM   1166  C CB  . VAL A 1 151 ? 26.286  13.232  67.251  1.00 23.88  ? 147 VAL A CB  1 
ATOM   1167  C CG1 . VAL A 1 151 ? 26.771  14.676  67.305  1.00 22.16  ? 147 VAL A CG1 1 
ATOM   1168  C CG2 . VAL A 1 151 ? 27.053  12.423  66.221  1.00 27.15  ? 147 VAL A CG2 1 
ATOM   1169  N N   . VAL A 1 152 ? 28.632  12.579  69.558  1.00 25.34  ? 148 VAL A N   1 
ATOM   1170  C CA  . VAL A 1 152 ? 29.689  12.946  70.516  1.00 25.54  ? 148 VAL A CA  1 
ATOM   1171  C C   . VAL A 1 152 ? 30.896  13.579  69.834  1.00 26.67  ? 148 VAL A C   1 
ATOM   1172  O O   . VAL A 1 152 ? 31.539  12.957  68.989  1.00 27.03  ? 148 VAL A O   1 
ATOM   1173  C CB  . VAL A 1 152 ? 30.200  11.725  71.304  1.00 25.52  ? 148 VAL A CB  1 
ATOM   1174  C CG1 . VAL A 1 152 ? 31.336  12.133  72.232  1.00 27.38  ? 148 VAL A CG1 1 
ATOM   1175  C CG2 . VAL A 1 152 ? 29.076  11.084  72.101  1.00 25.05  ? 148 VAL A CG2 1 
ATOM   1176  N N   . TRP A 1 153 ? 31.209  14.807  70.231  1.00 27.63  ? 149 TRP A N   1 
ATOM   1177  C CA  . TRP A 1 153 ? 32.337  15.552  69.681  1.00 28.44  ? 149 TRP A CA  1 
ATOM   1178  C C   . TRP A 1 153 ? 33.558  15.257  70.505  1.00 30.56  ? 149 TRP A C   1 
ATOM   1179  O O   . TRP A 1 153 ? 33.818  15.922  71.510  1.00 32.96  ? 149 TRP A O   1 
ATOM   1180  C CB  . TRP A 1 153 ? 32.005  17.041  69.693  1.00 29.65  ? 149 TRP A CB  1 
ATOM   1181  C CG  . TRP A 1 153 ? 33.039  17.965  69.099  1.00 31.65  ? 149 TRP A CG  1 
ATOM   1182  C CD1 . TRP A 1 153 ? 34.347  17.669  68.716  1.00 32.41  ? 149 TRP A CD1 1 
ATOM   1183  C CD2 . TRP A 1 153 ? 32.884  19.398  68.830  1.00 33.81  ? 149 TRP A CD2 1 
ATOM   1184  N NE1 . TRP A 1 153 ? 34.980  18.782  68.227  1.00 30.97  ? 149 TRP A NE1 1 
ATOM   1185  C CE2 . TRP A 1 153 ? 34.162  19.852  68.270  1.00 32.59  ? 149 TRP A CE2 1 
ATOM   1186  C CE3 . TRP A 1 153 ? 31.852  20.314  68.982  1.00 32.67  ? 149 TRP A CE3 1 
ATOM   1187  C CZ2 . TRP A 1 153 ? 34.369  21.167  67.887  1.00 34.08  ? 149 TRP A CZ2 1 
ATOM   1188  C CZ3 . TRP A 1 153 ? 32.075  21.640  68.594  1.00 33.84  ? 149 TRP A CZ3 1 
ATOM   1189  C CH2 . TRP A 1 153 ? 33.304  22.054  68.059  1.00 34.86  ? 149 TRP A CH2 1 
ATOM   1190  N N   . LEU A 1 154 ? 34.323  14.254  70.079  1.00 30.98  ? 150 LEU A N   1 
ATOM   1191  C CA  . LEU A 1 154 ? 35.491  13.794  70.827  1.00 33.09  ? 150 LEU A CA  1 
ATOM   1192  C C   . LEU A 1 154 ? 36.643  14.795  70.777  1.00 34.20  ? 150 LEU A C   1 
ATOM   1193  O O   . LEU A 1 154 ? 36.937  15.363  69.726  1.00 38.10  ? 150 LEU A O   1 
ATOM   1194  C CB  . LEU A 1 154 ? 35.963  12.434  70.302  1.00 32.79  ? 150 LEU A CB  1 
ATOM   1195  C CG  . LEU A 1 154 ? 34.967  11.282  70.450  1.00 33.65  ? 150 LEU A CG  1 
ATOM   1196  C CD1 . LEU A 1 154 ? 35.413  10.085  69.623  1.00 34.41  ? 150 LEU A CD1 1 
ATOM   1197  C CD2 . LEU A 1 154 ? 34.794  10.905  71.913  1.00 27.92  ? 150 LEU A CD2 1 
ATOM   1198  N N   . ILE A 1 155 ? 37.279  15.007  71.928  1.00 35.03  ? 151 ILE A N   1 
ATOM   1199  C CA  . ILE A 1 155 ? 38.438  15.894  72.056  1.00 36.63  ? 151 ILE A CA  1 
ATOM   1200  C C   . ILE A 1 155 ? 39.587  15.120  72.703  1.00 35.45  ? 151 ILE A C   1 
ATOM   1201  O O   . ILE A 1 155 ? 39.363  14.101  73.355  1.00 36.49  ? 151 ILE A O   1 
ATOM   1202  C CB  . ILE A 1 155 ? 38.075  17.166  72.873  1.00 38.39  ? 151 ILE A CB  1 
ATOM   1203  C CG1 . ILE A 1 155 ? 37.878  18.363  71.938  1.00 41.84  ? 151 ILE A CG1 1 
ATOM   1204  C CG2 . ILE A 1 155 ? 39.148  17.518  73.894  1.00 34.11  ? 151 ILE A CG2 1 
ATOM   1205  C CD1 . ILE A 1 155 ? 36.695  18.219  71.011  1.00 41.35  ? 151 ILE A CD1 1 
ATOM   1206  N N   . LYS A 1 156 ? 40.811  15.602  72.508  1.00 34.15  ? 152 LYS A N   1 
ATOM   1207  C CA  . LYS A 1 156 ? 42.004  14.944  73.045  1.00 33.25  ? 152 LYS A CA  1 
ATOM   1208  C C   . LYS A 1 156 ? 41.974  14.821  74.573  1.00 35.58  ? 152 LYS A C   1 
ATOM   1209  O O   . LYS A 1 156 ? 41.425  15.680  75.268  1.00 31.57  ? 152 LYS A O   1 
ATOM   1210  C CB  . LYS A 1 156 ? 43.267  15.704  72.622  1.00 31.34  ? 152 LYS A CB  1 
ATOM   1211  C CG  . LYS A 1 156 ? 43.454  17.046  73.312  1.00 28.84  ? 152 LYS A CG  1 
ATOM   1212  C CD  . LYS A 1 156 ? 44.590  17.835  72.688  1.00 28.31  ? 152 LYS A CD  1 
ATOM   1213  C CE  . LYS A 1 156 ? 45.038  18.976  73.592  1.00 28.32  ? 152 LYS A CE  1 
ATOM   1214  N NZ  . LYS A 1 156 ? 45.903  19.975  72.907  1.00 25.98  ? 152 LYS A NZ  1 
ATOM   1215  N N   . LYS A 1 157 ? 42.575  13.747  75.080  1.00 37.78  ? 153 LYS A N   1 
ATOM   1216  C CA  . LYS A 1 157 ? 42.720  13.532  76.515  1.00 39.36  ? 153 LYS A CA  1 
ATOM   1217  C C   . LYS A 1 157 ? 44.178  13.764  76.895  1.00 44.09  ? 153 LYS A C   1 
ATOM   1218  O O   . LYS A 1 157 ? 45.087  13.290  76.205  1.00 40.36  ? 153 LYS A O   1 
ATOM   1219  C CB  . LYS A 1 157 ? 42.290  12.114  76.890  1.00 39.47  ? 153 LYS A CB  1 
ATOM   1220  C CG  . LYS A 1 157 ? 42.028  11.921  78.373  1.00 38.24  ? 153 LYS A CG  1 
ATOM   1221  C CD  . LYS A 1 157 ? 41.448  10.546  78.660  1.00 39.03  ? 153 LYS A CD  1 
ATOM   1222  C CE  . LYS A 1 157 ? 41.020  10.414  80.115  1.00 38.87  ? 153 LYS A CE  1 
ATOM   1223  N NZ  . LYS A 1 157 ? 40.110  9.255   80.337  1.00 38.72  ? 153 LYS A NZ  1 
ATOM   1224  N N   . ASP A 1 158 ? 44.389  14.479  78.000  1.00 51.60  ? 154 ASP A N   1 
ATOM   1225  C CA  . ASP A 1 158 ? 45.714  14.966  78.393  1.00 55.64  ? 154 ASP A CA  1 
ATOM   1226  C C   . ASP A 1 158 ? 46.240  15.876  77.280  1.00 54.37  ? 154 ASP A C   1 
ATOM   1227  O O   . ASP A 1 158 ? 45.714  16.975  77.087  1.00 60.85  ? 154 ASP A O   1 
ATOM   1228  C CB  . ASP A 1 158 ? 46.663  13.800  78.717  1.00 59.63  ? 154 ASP A CB  1 
ATOM   1229  C CG  . ASP A 1 158 ? 46.125  12.903  79.816  1.00 65.56  ? 154 ASP A CG  1 
ATOM   1230  O OD1 . ASP A 1 158 ? 45.702  13.432  80.866  1.00 67.54  ? 154 ASP A OD1 1 
ATOM   1231  O OD2 . ASP A 1 158 ? 46.121  11.669  79.627  1.00 70.32  ? 154 ASP A OD2 1 
ATOM   1232  N N   . ASN A 1 159 ? 47.252  15.425  76.544  1.00 46.20  ? 155 ASN A N   1 
ATOM   1233  C CA  . ASN A 1 159 ? 47.664  16.096  75.317  1.00 45.75  ? 155 ASN A CA  1 
ATOM   1234  C C   . ASN A 1 159 ? 47.986  15.056  74.251  1.00 38.34  ? 155 ASN A C   1 
ATOM   1235  O O   . ASN A 1 159 ? 49.087  15.011  73.708  1.00 36.55  ? 155 ASN A O   1 
ATOM   1236  C CB  . ASN A 1 159 ? 48.855  17.015  75.588  1.00 50.35  ? 155 ASN A CB  1 
ATOM   1237  C CG  . ASN A 1 159 ? 48.435  18.336  76.188  1.00 50.08  ? 155 ASN A CG  1 
ATOM   1238  O OD1 . ASN A 1 159 ? 48.009  19.233  75.470  1.00 50.23  ? 155 ASN A OD1 1 
ATOM   1239  N ND2 . ASN A 1 159 ? 48.554  18.463  77.506  1.00 47.41  ? 155 ASN A ND2 1 
ATOM   1240  N N   . ALA A 1 160 ? 46.998  14.216  73.966  1.00 33.82  ? 156 ALA A N   1 
ATOM   1241  C CA  . ALA A 1 160 ? 47.156  13.124  73.017  1.00 30.82  ? 156 ALA A CA  1 
ATOM   1242  C C   . ALA A 1 160 ? 45.808  12.719  72.428  1.00 30.87  ? 156 ALA A C   1 
ATOM   1243  O O   . ALA A 1 160 ? 44.782  12.747  73.118  1.00 30.53  ? 156 ALA A O   1 
ATOM   1244  C CB  . ALA A 1 160 ? 47.812  11.935  73.696  1.00 29.11  ? 156 ALA A CB  1 
ATOM   1245  N N   . TYR A 1 161 ? 45.819  12.357  71.147  1.00 29.96  ? 157 TYR A N   1 
ATOM   1246  C CA  . TYR A 1 161 ? 44.640  11.830  70.466  1.00 27.29  ? 157 TYR A CA  1 
ATOM   1247  C C   . TYR A 1 161 ? 45.062  10.542  69.766  1.00 26.31  ? 157 TYR A C   1 
ATOM   1248  O O   . TYR A 1 161 ? 45.399  10.552  68.581  1.00 25.29  ? 157 TYR A O   1 
ATOM   1249  C CB  . TYR A 1 161 ? 44.082  12.857  69.475  1.00 26.13  ? 157 TYR A CB  1 
ATOM   1250  C CG  . TYR A 1 161 ? 42.673  12.572  68.963  1.00 26.08  ? 157 TYR A CG  1 
ATOM   1251  C CD1 . TYR A 1 161 ? 41.613  13.423  69.276  1.00 26.88  ? 157 TYR A CD1 1 
ATOM   1252  C CD2 . TYR A 1 161 ? 42.406  11.473  68.155  1.00 25.00  ? 157 TYR A CD2 1 
ATOM   1253  C CE1 . TYR A 1 161 ? 40.332  13.183  68.808  1.00 27.48  ? 157 TYR A CE1 1 
ATOM   1254  C CE2 . TYR A 1 161 ? 41.132  11.228  67.681  1.00 27.56  ? 157 TYR A CE2 1 
ATOM   1255  C CZ  . TYR A 1 161 ? 40.096  12.080  68.008  1.00 29.13  ? 157 TYR A CZ  1 
ATOM   1256  O OH  . TYR A 1 161 ? 38.827  11.824  67.529  1.00 27.22  ? 157 TYR A OH  1 
ATOM   1257  N N   . PRO A 1 162 ? 45.065  9.424   70.508  1.00 28.01  ? 158 PRO A N   1 
ATOM   1258  C CA  . PRO A 1 162 ? 45.406  8.148   69.892  1.00 28.84  ? 158 PRO A CA  1 
ATOM   1259  C C   . PRO A 1 162 ? 44.405  7.772   68.809  1.00 27.14  ? 158 PRO A C   1 
ATOM   1260  O O   . PRO A 1 162 ? 43.230  8.137   68.902  1.00 27.48  ? 158 PRO A O   1 
ATOM   1261  C CB  . PRO A 1 162 ? 45.333  7.151   71.059  1.00 30.57  ? 158 PRO A CB  1 
ATOM   1262  C CG  . PRO A 1 162 ? 45.379  7.977   72.296  1.00 30.84  ? 158 PRO A CG  1 
ATOM   1263  C CD  . PRO A 1 162 ? 44.734  9.275   71.935  1.00 29.63  ? 158 PRO A CD  1 
ATOM   1264  N N   . THR A 1 163 ? 44.870  7.049   67.796  1.00 25.61  ? 159 THR A N   1 
ATOM   1265  C CA  . THR A 1 163 ? 44.017  6.660   66.682  1.00 25.16  ? 159 THR A CA  1 
ATOM   1266  C C   . THR A 1 163 ? 42.859  5.787   67.158  1.00 26.80  ? 159 THR A C   1 
ATOM   1267  O O   . THR A 1 163 ? 43.069  4.774   67.827  1.00 25.35  ? 159 THR A O   1 
ATOM   1268  C CB  . THR A 1 163 ? 44.815  5.907   65.605  1.00 24.14  ? 159 THR A CB  1 
ATOM   1269  O OG1 . THR A 1 163 ? 45.869  6.749   65.120  1.00 24.90  ? 159 THR A OG1 1 
ATOM   1270  C CG2 . THR A 1 163 ? 43.906  5.501   64.446  1.00 23.11  ? 159 THR A CG2 1 
ATOM   1271  N N   . ILE A 1 164 ? 41.642  6.204   66.817  1.00 29.01  ? 160 ILE A N   1 
ATOM   1272  C CA  . ILE A 1 164 ? 40.435  5.456   67.139  1.00 30.84  ? 160 ILE A CA  1 
ATOM   1273  C C   . ILE A 1 164 ? 40.224  4.364   66.100  1.00 31.36  ? 160 ILE A C   1 
ATOM   1274  O O   . ILE A 1 164 ? 40.417  4.590   64.905  1.00 29.58  ? 160 ILE A O   1 
ATOM   1275  C CB  . ILE A 1 164 ? 39.195  6.372   67.148  1.00 32.86  ? 160 ILE A CB  1 
ATOM   1276  C CG1 . ILE A 1 164 ? 39.297  7.397   68.282  1.00 33.28  ? 160 ILE A CG1 1 
ATOM   1277  C CG2 . ILE A 1 164 ? 37.915  5.556   67.283  1.00 32.38  ? 160 ILE A CG2 1 
ATOM   1278  C CD1 . ILE A 1 164 ? 38.299  8.531   68.173  1.00 32.31  ? 160 ILE A CD1 1 
ATOM   1279  N N   . LYS A 1 165 ? 39.839  3.180   66.570  1.00 33.24  ? 161 LYS A N   1 
ATOM   1280  C CA  . LYS A 1 165 ? 39.441  2.080   65.699  1.00 34.38  ? 161 LYS A CA  1 
ATOM   1281  C C   . LYS A 1 165 ? 38.204  1.413   66.285  1.00 34.04  ? 161 LYS A C   1 
ATOM   1282  O O   . LYS A 1 165 ? 38.299  0.362   66.920  1.00 36.59  ? 161 LYS A O   1 
ATOM   1283  C CB  . LYS A 1 165 ? 40.572  1.061   65.575  1.00 36.12  ? 161 LYS A CB  1 
ATOM   1284  C CG  . LYS A 1 165 ? 41.706  1.485   64.667  1.00 36.59  ? 161 LYS A CG  1 
ATOM   1285  C CD  . LYS A 1 165 ? 42.932  0.604   64.876  1.00 35.86  ? 161 LYS A CD  1 
ATOM   1286  C CE  . LYS A 1 165 ? 44.052  0.914   63.896  1.00 35.43  ? 161 LYS A CE  1 
ATOM   1287  N NZ  . LYS A 1 165 ? 44.823  -0.313  63.544  1.00 33.51  ? 161 LYS A NZ  1 
ATOM   1288  N N   . LYS A 1 166 ? 37.050  2.043   66.079  1.00 33.87  ? 162 LYS A N   1 
ATOM   1289  C CA  . LYS A 1 166 ? 35.793  1.567   66.646  1.00 34.82  ? 162 LYS A CA  1 
ATOM   1290  C C   . LYS A 1 166 ? 34.901  0.996   65.554  1.00 32.82  ? 162 LYS A C   1 
ATOM   1291  O O   . LYS A 1 166 ? 34.782  1.577   64.481  1.00 30.74  ? 162 LYS A O   1 
ATOM   1292  C CB  . LYS A 1 166 ? 35.064  2.705   67.368  1.00 36.15  ? 162 LYS A CB  1 
ATOM   1293  C CG  . LYS A 1 166 ? 33.998  2.241   68.353  1.00 37.48  ? 162 LYS A CG  1 
ATOM   1294  C CD  . LYS A 1 166 ? 34.608  1.881   69.702  1.00 39.46  ? 162 LYS A CD  1 
ATOM   1295  C CE  . LYS A 1 166 ? 33.581  1.296   70.658  1.00 42.14  ? 162 LYS A CE  1 
ATOM   1296  N NZ  . LYS A 1 166 ? 33.617  -0.192  70.694  1.00 43.63  ? 162 LYS A NZ  1 
ATOM   1297  N N   . GLY A 1 167 ? 34.281  -0.146  65.842  1.00 33.42  ? 163 GLY A N   1 
ATOM   1298  C CA  . GLY A 1 167 ? 33.364  -0.796  64.911  1.00 32.39  ? 163 GLY A CA  1 
ATOM   1299  C C   . GLY A 1 167 ? 32.065  -1.192  65.586  1.00 31.99  ? 163 GLY A C   1 
ATOM   1300  O O   . GLY A 1 167 ? 32.036  -1.434  66.795  1.00 33.93  ? 163 GLY A O   1 
ATOM   1301  N N   . TYR A 1 168 ? 30.988  -1.246  64.805  1.00 30.56  ? 164 TYR A N   1 
ATOM   1302  C CA  . TYR A 1 168 ? 29.702  -1.722  65.292  1.00 31.74  ? 164 TYR A CA  1 
ATOM   1303  C C   . TYR A 1 168 ? 29.052  -2.669  64.290  1.00 32.99  ? 164 TYR A C   1 
ATOM   1304  O O   . TYR A 1 168 ? 28.851  -2.309  63.133  1.00 30.99  ? 164 TYR A O   1 
ATOM   1305  C CB  . TYR A 1 168 ? 28.751  -0.559  65.574  1.00 32.19  ? 164 TYR A CB  1 
ATOM   1306  C CG  . TYR A 1 168 ? 27.392  -1.030  66.042  1.00 31.21  ? 164 TYR A CG  1 
ATOM   1307  C CD1 . TYR A 1 168 ? 27.174  -1.363  67.378  1.00 32.11  ? 164 TYR A CD1 1 
ATOM   1308  C CD2 . TYR A 1 168 ? 26.335  -1.170  65.149  1.00 29.03  ? 164 TYR A CD2 1 
ATOM   1309  C CE1 . TYR A 1 168 ? 25.935  -1.807  67.813  1.00 32.37  ? 164 TYR A CE1 1 
ATOM   1310  C CE2 . TYR A 1 168 ? 25.096  -1.616  65.572  1.00 29.92  ? 164 TYR A CE2 1 
ATOM   1311  C CZ  . TYR A 1 168 ? 24.899  -1.933  66.905  1.00 31.23  ? 164 TYR A CZ  1 
ATOM   1312  O OH  . TYR A 1 168 ? 23.668  -2.367  67.341  1.00 31.00  ? 164 TYR A OH  1 
ATOM   1313  N N   . ASN A 1 169 ? 28.716  -3.870  64.756  1.00 34.93  ? 165 ASN A N   1 
ATOM   1314  C CA  . ASN A 1 169 ? 27.986  -4.853  63.965  1.00 35.59  ? 165 ASN A CA  1 
ATOM   1315  C C   . ASN A 1 169 ? 26.502  -4.721  64.273  1.00 32.58  ? 165 ASN A C   1 
ATOM   1316  O O   . ASN A 1 169 ? 26.102  -4.729  65.437  1.00 30.71  ? 165 ASN A O   1 
ATOM   1317  C CB  . ASN A 1 169 ? 28.485  -6.267  64.293  1.00 37.95  ? 165 ASN A CB  1 
ATOM   1318  C CG  . ASN A 1 169 ? 27.900  -7.342  63.385  1.00 42.97  ? 165 ASN A CG  1 
ATOM   1319  O OD1 . ASN A 1 169 ? 26.763  -7.244  62.923  1.00 46.75  ? 165 ASN A OD1 1 
ATOM   1320  N ND2 . ASN A 1 169 ? 28.690  -8.385  63.132  1.00 50.41  ? 165 ASN A ND2 1 
ATOM   1321  N N   . ASN A 1 170 ? 25.694  -4.578  63.227  1.00 30.67  ? 166 ASN A N   1 
ATOM   1322  C CA  . ASN A 1 170 ? 24.251  -4.503  63.385  1.00 30.32  ? 166 ASN A CA  1 
ATOM   1323  C C   . ASN A 1 170 ? 23.705  -5.887  63.725  1.00 30.69  ? 166 ASN A C   1 
ATOM   1324  O O   . ASN A 1 170 ? 23.533  -6.727  62.853  1.00 28.44  ? 166 ASN A O   1 
ATOM   1325  C CB  . ASN A 1 170 ? 23.597  -3.945  62.113  1.00 29.79  ? 166 ASN A CB  1 
ATOM   1326  C CG  . ASN A 1 170 ? 22.099  -3.726  62.265  1.00 28.19  ? 166 ASN A CG  1 
ATOM   1327  O OD1 . ASN A 1 170 ? 21.551  -3.790  63.367  1.00 26.62  ? 166 ASN A OD1 1 
ATOM   1328  N ND2 . ASN A 1 170 ? 21.430  -3.466  61.148  1.00 26.48  ? 166 ASN A ND2 1 
ATOM   1329  N N   . THR A 1 171 ? 23.460  -6.117  65.011  1.00 33.38  ? 167 THR A N   1 
ATOM   1330  C CA  . THR A 1 171 ? 22.928  -7.390  65.495  1.00 33.11  ? 167 THR A CA  1 
ATOM   1331  C C   . THR A 1 171 ? 21.399  -7.416  65.459  1.00 34.37  ? 167 THR A C   1 
ATOM   1332  O O   . THR A 1 171 ? 20.787  -8.465  65.659  1.00 35.96  ? 167 THR A O   1 
ATOM   1333  C CB  . THR A 1 171 ? 23.405  -7.672  66.929  1.00 33.40  ? 167 THR A CB  1 
ATOM   1334  O OG1 . THR A 1 171 ? 23.127  -6.537  67.759  1.00 34.20  ? 167 THR A OG1 1 
ATOM   1335  C CG2 . THR A 1 171 ? 24.901  -7.954  66.943  1.00 31.98  ? 167 THR A CG2 1 
ATOM   1336  N N   . ASN A 1 172 ? 20.791  -6.262  65.196  1.00 35.24  ? 168 ASN A N   1 
ATOM   1337  C CA  . ASN A 1 172 ? 19.337  -6.141  65.103  1.00 35.70  ? 168 ASN A CA  1 
ATOM   1338  C C   . ASN A 1 172 ? 18.839  -6.720  63.777  1.00 35.70  ? 168 ASN A C   1 
ATOM   1339  O O   . ASN A 1 172 ? 19.638  -6.992  62.875  1.00 40.34  ? 168 ASN A O   1 
ATOM   1340  C CB  . ASN A 1 172 ? 18.922  -4.670  65.235  1.00 36.35  ? 168 ASN A CB  1 
ATOM   1341  C CG  . ASN A 1 172 ? 19.617  -3.966  66.388  1.00 37.69  ? 168 ASN A CG  1 
ATOM   1342  O OD1 . ASN A 1 172 ? 19.324  -4.223  67.553  1.00 42.42  ? 168 ASN A OD1 1 
ATOM   1343  N ND2 . ASN A 1 172 ? 20.548  -3.074  66.065  1.00 37.41  ? 168 ASN A ND2 1 
ATOM   1344  N N   . GLN A 1 173 ? 17.528  -6.914  63.660  1.00 33.08  ? 169 GLN A N   1 
ATOM   1345  C CA  . GLN A 1 173 ? 16.935  -7.475  62.449  1.00 35.06  ? 169 GLN A CA  1 
ATOM   1346  C C   . GLN A 1 173 ? 16.486  -6.388  61.461  1.00 35.16  ? 169 GLN A C   1 
ATOM   1347  O O   . GLN A 1 173 ? 16.045  -6.702  60.349  1.00 34.13  ? 169 GLN A O   1 
ATOM   1348  C CB  . GLN A 1 173 ? 15.731  -8.369  62.823  1.00 37.94  ? 169 GLN A CB  1 
ATOM   1349  C CG  . GLN A 1 173 ? 15.940  -9.455  63.909  1.00 39.66  ? 169 GLN A CG  1 
ATOM   1350  C CD  . GLN A 1 173 ? 16.958  -10.530 63.549  1.00 40.22  ? 169 GLN A CD  1 
ATOM   1351  O OE1 . GLN A 1 173 ? 17.103  -11.515 64.274  1.00 42.28  ? 169 GLN A OE1 1 
ATOM   1352  N NE2 . GLN A 1 173 ? 17.653  -10.359 62.432  1.00 39.03  ? 169 GLN A NE2 1 
ATOM   1353  N N   . GLU A 1 174 ? 16.612  -5.119  61.854  1.00 35.84  ? 170 GLU A N   1 
ATOM   1354  C CA  . GLU A 1 174 ? 16.204  -3.995  61.011  1.00 36.21  ? 170 GLU A CA  1 
ATOM   1355  C C   . GLU A 1 174 ? 17.398  -3.165  60.547  1.00 33.81  ? 170 GLU A C   1 
ATOM   1356  O O   . GLU A 1 174 ? 18.474  -3.209  61.148  1.00 33.79  ? 170 GLU A O   1 
ATOM   1357  C CB  . GLU A 1 174 ? 15.224  -3.094  61.767  1.00 41.03  ? 170 GLU A CB  1 
ATOM   1358  C CG  . GLU A 1 174 ? 13.837  -3.696  61.958  1.00 43.91  ? 170 GLU A CG  1 
ATOM   1359  C CD  . GLU A 1 174 ? 13.627  -4.341  63.317  1.00 49.58  ? 170 GLU A CD  1 
ATOM   1360  O OE1 . GLU A 1 174 ? 12.446  -4.552  63.683  1.00 54.45  ? 170 GLU A OE1 1 
ATOM   1361  O OE2 . GLU A 1 174 ? 14.626  -4.630  64.020  1.00 54.34  ? 170 GLU A OE2 1 
ATOM   1362  N N   . ASP A 1 175 ? 17.195  -2.406  59.473  1.00 32.49  ? 171 ASP A N   1 
ATOM   1363  C CA  . ASP A 1 175 ? 18.206  -1.469  58.981  1.00 31.05  ? 171 ASP A CA  1 
ATOM   1364  C C   . ASP A 1 175 ? 18.494  -0.400  60.035  1.00 30.83  ? 171 ASP A C   1 
ATOM   1365  O O   . ASP A 1 175 ? 17.590  0.014   60.767  1.00 30.66  ? 171 ASP A O   1 
ATOM   1366  C CB  . ASP A 1 175 ? 17.735  -0.784  57.688  1.00 30.97  ? 171 ASP A CB  1 
ATOM   1367  C CG  . ASP A 1 175 ? 17.697  -1.724  56.492  1.00 31.06  ? 171 ASP A CG  1 
ATOM   1368  O OD1 . ASP A 1 175 ? 18.416  -2.744  56.498  1.00 32.02  ? 171 ASP A OD1 1 
ATOM   1369  O OD2 . ASP A 1 175 ? 16.954  -1.426  55.532  1.00 29.89  ? 171 ASP A OD2 1 
ATOM   1370  N N   . LEU A 1 176 ? 19.749  0.043   60.102  1.00 28.27  ? 172 LEU A N   1 
ATOM   1371  C CA  . LEU A 1 176 ? 20.158  1.099   61.030  1.00 28.25  ? 172 LEU A CA  1 
ATOM   1372  C C   . LEU A 1 176 ? 20.618  2.345   60.286  1.00 27.12  ? 172 LEU A C   1 
ATOM   1373  O O   . LEU A 1 176 ? 21.529  2.280   59.466  1.00 25.19  ? 172 LEU A O   1 
ATOM   1374  C CB  . LEU A 1 176 ? 21.292  0.618   61.935  1.00 29.46  ? 172 LEU A CB  1 
ATOM   1375  C CG  . LEU A 1 176 ? 20.891  -0.042  63.250  1.00 32.66  ? 172 LEU A CG  1 
ATOM   1376  C CD1 . LEU A 1 176 ? 22.118  -0.625  63.926  1.00 34.23  ? 172 LEU A CD1 1 
ATOM   1377  C CD2 . LEU A 1 176 ? 20.204  0.965   64.161  1.00 34.34  ? 172 LEU A CD2 1 
ATOM   1378  N N   . LEU A 1 177 ? 19.987  3.477   60.585  1.00 27.09  ? 173 LEU A N   1 
ATOM   1379  C CA  . LEU A 1 177 ? 20.444  4.769   60.094  1.00 26.12  ? 173 LEU A CA  1 
ATOM   1380  C C   . LEU A 1 177 ? 21.508  5.281   61.053  1.00 26.76  ? 173 LEU A C   1 
ATOM   1381  O O   . LEU A 1 177 ? 21.212  5.554   62.219  1.00 26.40  ? 173 LEU A O   1 
ATOM   1382  C CB  . LEU A 1 177 ? 19.280  5.759   60.009  1.00 26.67  ? 173 LEU A CB  1 
ATOM   1383  C CG  . LEU A 1 177 ? 19.626  7.210   59.666  1.00 28.22  ? 173 LEU A CG  1 
ATOM   1384  C CD1 . LEU A 1 177 ? 20.313  7.324   58.311  1.00 29.73  ? 173 LEU A CD1 1 
ATOM   1385  C CD2 . LEU A 1 177 ? 18.355  8.042   59.691  1.00 27.25  ? 173 LEU A CD2 1 
ATOM   1386  N N   . VAL A 1 178 ? 22.744  5.394   60.564  1.00 27.52  ? 174 VAL A N   1 
ATOM   1387  C CA  . VAL A 1 178 ? 23.870  5.866   61.375  1.00 25.07  ? 174 VAL A CA  1 
ATOM   1388  C C   . VAL A 1 178 ? 24.360  7.215   60.862  1.00 24.58  ? 174 VAL A C   1 
ATOM   1389  O O   . VAL A 1 178 ? 24.524  7.404   59.660  1.00 23.11  ? 174 VAL A O   1 
ATOM   1390  C CB  . VAL A 1 178 ? 25.053  4.882   61.352  1.00 22.99  ? 174 VAL A CB  1 
ATOM   1391  C CG1 . VAL A 1 178 ? 26.140  5.339   62.311  1.00 22.60  ? 174 VAL A CG1 1 
ATOM   1392  C CG2 . VAL A 1 178 ? 24.587  3.481   61.712  1.00 22.01  ? 174 VAL A CG2 1 
ATOM   1393  N N   . LEU A 1 179 ? 24.599  8.134   61.792  1.00 25.54  ? 175 LEU A N   1 
ATOM   1394  C CA  . LEU A 1 179 ? 25.052  9.482   61.483  1.00 24.76  ? 175 LEU A CA  1 
ATOM   1395  C C   . LEU A 1 179 ? 26.406  9.731   62.128  1.00 23.89  ? 175 LEU A C   1 
ATOM   1396  O O   . LEU A 1 179 ? 26.699  9.204   63.198  1.00 21.92  ? 175 LEU A O   1 
ATOM   1397  C CB  . LEU A 1 179 ? 24.056  10.509  62.020  1.00 26.19  ? 175 LEU A CB  1 
ATOM   1398  C CG  . LEU A 1 179 ? 22.600  10.385  61.552  1.00 27.40  ? 175 LEU A CG  1 
ATOM   1399  C CD1 . LEU A 1 179 ? 21.655  10.989  62.582  1.00 27.35  ? 175 LEU A CD1 1 
ATOM   1400  C CD2 . LEU A 1 179 ? 22.397  11.037  60.194  1.00 25.45  ? 175 LEU A CD2 1 
ATOM   1401  N N   . TRP A 1 180 ? 27.230  10.535  61.469  1.00 22.84  ? 176 TRP A N   1 
ATOM   1402  C CA  . TRP A 1 180 ? 28.498  10.970  62.035  1.00 22.91  ? 176 TRP A CA  1 
ATOM   1403  C C   . TRP A 1 180 ? 28.917  12.220  61.331  1.00 24.54  ? 176 TRP A C   1 
ATOM   1404  O O   . TRP A 1 180 ? 28.314  12.586  60.320  1.00 28.32  ? 176 TRP A O   1 
ATOM   1405  C CB  . TRP A 1 180 ? 29.558  9.887   61.883  1.00 22.83  ? 176 TRP A CB  1 
ATOM   1406  C CG  . TRP A 1 180 ? 29.926  9.607   60.446  1.00 21.85  ? 176 TRP A CG  1 
ATOM   1407  C CD1 . TRP A 1 180 ? 30.974  10.153  59.720  1.00 20.63  ? 176 TRP A CD1 1 
ATOM   1408  C CD2 . TRP A 1 180 ? 29.242  8.712   59.508  1.00 22.54  ? 176 TRP A CD2 1 
ATOM   1409  N NE1 . TRP A 1 180 ? 30.985  9.672   58.437  1.00 21.39  ? 176 TRP A NE1 1 
ATOM   1410  C CE2 . TRP A 1 180 ? 29.974  8.807   58.243  1.00 21.34  ? 176 TRP A CE2 1 
ATOM   1411  C CE3 . TRP A 1 180 ? 28.136  7.877   59.585  1.00 24.32  ? 176 TRP A CE3 1 
ATOM   1412  C CZ2 . TRP A 1 180 ? 29.605  8.082   57.126  1.00 21.47  ? 176 TRP A CZ2 1 
ATOM   1413  C CZ3 . TRP A 1 180 ? 27.770  7.154   58.445  1.00 24.37  ? 176 TRP A CZ3 1 
ATOM   1414  C CH2 . TRP A 1 180 ? 28.491  7.257   57.245  1.00 22.71  ? 176 TRP A CH2 1 
ATOM   1415  N N   . GLY A 1 181 ? 29.943  12.893  61.848  1.00 23.43  ? 177 GLY A N   1 
ATOM   1416  C CA  . GLY A 1 181 ? 30.395  14.146  61.252  1.00 21.61  ? 177 GLY A CA  1 
ATOM   1417  C C   . GLY A 1 181 ? 31.878  14.420  61.379  1.00 19.40  ? 177 GLY A C   1 
ATOM   1418  O O   . GLY A 1 181 ? 32.599  13.697  62.062  1.00 16.93  ? 177 GLY A O   1 
ATOM   1419  N N   . ILE A 1 182 ? 32.317  15.475  60.694  1.00 19.26  ? 178 ILE A N   1 
ATOM   1420  C CA  . ILE A 1 182 ? 33.702  15.939  60.730  1.00 19.08  ? 178 ILE A CA  1 
ATOM   1421  C C   . ILE A 1 182 ? 33.715  17.432  61.057  1.00 20.23  ? 178 ILE A C   1 
ATOM   1422  O O   . ILE A 1 182 ? 32.835  18.175  60.616  1.00 20.04  ? 178 ILE A O   1 
ATOM   1423  C CB  . ILE A 1 182 ? 34.432  15.647  59.397  1.00 18.41  ? 178 ILE A CB  1 
ATOM   1424  C CG1 . ILE A 1 182 ? 35.914  16.030  59.479  1.00 19.28  ? 178 ILE A CG1 1 
ATOM   1425  C CG2 . ILE A 1 182 ? 33.756  16.347  58.229  1.00 18.26  ? 178 ILE A CG2 1 
ATOM   1426  C CD1 . ILE A 1 182 ? 36.765  15.455  58.363  1.00 18.98  ? 178 ILE A CD1 1 
ATOM   1427  N N   . HIS A 1 183 ? 34.699  17.850  61.854  1.00 22.40  ? 179 HIS A N   1 
ATOM   1428  C CA  . HIS A 1 183 ? 34.850  19.245  62.262  1.00 21.75  ? 179 HIS A CA  1 
ATOM   1429  C C   . HIS A 1 183 ? 35.927  19.912  61.455  1.00 21.95  ? 179 HIS A C   1 
ATOM   1430  O O   . HIS A 1 183 ? 37.069  19.458  61.437  1.00 18.30  ? 179 HIS A O   1 
ATOM   1431  C CB  . HIS A 1 183 ? 35.184  19.333  63.744  1.00 22.41  ? 179 HIS A CB  1 
ATOM   1432  C CG  . HIS A 1 183 ? 35.526  20.728  64.210  1.00 22.60  ? 179 HIS A CG  1 
ATOM   1433  N ND1 . HIS A 1 183 ? 36.738  21.050  64.695  1.00 23.52  ? 179 HIS A ND1 1 
ATOM   1434  C CD2 . HIS A 1 183 ? 34.768  21.894  64.243  1.00 23.47  ? 179 HIS A CD2 1 
ATOM   1435  C CE1 . HIS A 1 183 ? 36.760  22.354  65.022  1.00 23.79  ? 179 HIS A CE1 1 
ATOM   1436  N NE2 . HIS A 1 183 ? 35.551  22.871  64.746  1.00 23.91  ? 179 HIS A NE2 1 
ATOM   1437  N N   . HIS A 1 184 ? 35.561  20.990  60.768  1.00 23.11  ? 180 HIS A N   1 
ATOM   1438  C CA  . HIS A 1 184 ? 36.514  21.804  60.023  1.00 23.78  ? 180 HIS A CA  1 
ATOM   1439  C C   . HIS A 1 184 ? 36.878  23.008  60.858  1.00 25.41  ? 180 HIS A C   1 
ATOM   1440  O O   . HIS A 1 184 ? 36.072  23.933  60.989  1.00 24.83  ? 180 HIS A O   1 
ATOM   1441  C CB  . HIS A 1 184 ? 35.903  22.258  58.702  1.00 23.49  ? 180 HIS A CB  1 
ATOM   1442  C CG  . HIS A 1 184 ? 35.388  21.130  57.839  1.00 22.85  ? 180 HIS A CG  1 
ATOM   1443  N ND1 . HIS A 1 184 ? 36.199  20.226  57.266  1.00 23.19  ? 180 HIS A ND1 1 
ATOM   1444  C CD2 . HIS A 1 184 ? 34.096  20.802  57.444  1.00 23.09  ? 180 HIS A CD2 1 
ATOM   1445  C CE1 . HIS A 1 184 ? 35.466  19.355  56.549  1.00 23.16  ? 180 HIS A CE1 1 
ATOM   1446  N NE2 . HIS A 1 184 ? 34.178  19.708  56.659  1.00 23.06  ? 180 HIS A NE2 1 
ATOM   1447  N N   . PRO A 1 185 ? 38.089  23.020  61.449  1.00 27.30  ? 181 PRO A N   1 
ATOM   1448  C CA  . PRO A 1 185 ? 38.487  24.150  62.290  1.00 28.66  ? 181 PRO A CA  1 
ATOM   1449  C C   . PRO A 1 185 ? 38.895  25.383  61.486  1.00 31.45  ? 181 PRO A C   1 
ATOM   1450  O O   . PRO A 1 185 ? 39.039  25.315  60.263  1.00 28.65  ? 181 PRO A O   1 
ATOM   1451  C CB  . PRO A 1 185 ? 39.683  23.600  63.063  1.00 28.77  ? 181 PRO A CB  1 
ATOM   1452  C CG  . PRO A 1 185 ? 40.288  22.608  62.141  1.00 28.40  ? 181 PRO A CG  1 
ATOM   1453  C CD  . PRO A 1 185 ? 39.174  22.035  61.312  1.00 27.45  ? 181 PRO A CD  1 
ATOM   1454  N N   . ASN A 1 186 ? 39.082  26.499  62.187  1.00 38.38  ? 182 ASN A N   1 
ATOM   1455  C CA  . ASN A 1 186 ? 39.361  27.789  61.552  1.00 44.63  ? 182 ASN A CA  1 
ATOM   1456  C C   . ASN A 1 186 ? 40.837  27.982  61.188  1.00 43.38  ? 182 ASN A C   1 
ATOM   1457  O O   . ASN A 1 186 ? 41.141  28.653  60.206  1.00 41.07  ? 182 ASN A O   1 
ATOM   1458  C CB  . ASN A 1 186 ? 38.891  28.933  62.465  1.00 53.30  ? 182 ASN A CB  1 
ATOM   1459  C CG  . ASN A 1 186 ? 38.703  30.245  61.721  1.00 63.43  ? 182 ASN A CG  1 
ATOM   1460  O OD1 . ASN A 1 186 ? 38.059  30.294  60.671  1.00 67.98  ? 182 ASN A OD1 1 
ATOM   1461  N ND2 . ASN A 1 186 ? 39.252  31.322  62.275  1.00 67.36  ? 182 ASN A ND2 1 
ATOM   1462  N N   . ASP A 1 187 ? 41.741  27.403  61.981  1.00 42.54  ? 183 ASP A N   1 
ATOM   1463  C CA  . ASP A 1 187 ? 43.184  27.516  61.738  1.00 40.58  ? 183 ASP A CA  1 
ATOM   1464  C C   . ASP A 1 187 ? 43.977  26.360  62.361  1.00 39.96  ? 183 ASP A C   1 
ATOM   1465  O O   . ASP A 1 187 ? 43.421  25.525  63.075  1.00 37.49  ? 183 ASP A O   1 
ATOM   1466  C CB  . ASP A 1 187 ? 43.709  28.865  62.244  1.00 43.78  ? 183 ASP A CB  1 
ATOM   1467  C CG  . ASP A 1 187 ? 43.343  29.135  63.692  1.00 49.30  ? 183 ASP A CG  1 
ATOM   1468  O OD1 . ASP A 1 187 ? 42.776  30.214  63.964  1.00 59.78  ? 183 ASP A OD1 1 
ATOM   1469  O OD2 . ASP A 1 187 ? 43.617  28.278  64.559  1.00 52.50  ? 183 ASP A OD2 1 
ATOM   1470  N N   . GLU A 1 188 ? 45.279  26.329  62.081  1.00 41.10  ? 184 GLU A N   1 
ATOM   1471  C CA  . GLU A 1 188 ? 46.166  25.244  62.516  1.00 41.23  ? 184 GLU A CA  1 
ATOM   1472  C C   . GLU A 1 188 ? 46.336  25.195  64.039  1.00 36.76  ? 184 GLU A C   1 
ATOM   1473  O O   . GLU A 1 188 ? 46.565  24.125  64.607  1.00 31.15  ? 184 GLU A O   1 
ATOM   1474  C CB  . GLU A 1 188 ? 47.548  25.383  61.859  1.00 44.67  ? 184 GLU A CB  1 
ATOM   1475  C CG  . GLU A 1 188 ? 47.554  25.382  60.332  1.00 52.06  ? 184 GLU A CG  1 
ATOM   1476  C CD  . GLU A 1 188 ? 47.630  23.993  59.726  1.00 63.37  ? 184 GLU A CD  1 
ATOM   1477  O OE1 . GLU A 1 188 ? 48.247  23.856  58.644  1.00 71.44  ? 184 GLU A OE1 1 
ATOM   1478  O OE2 . GLU A 1 188 ? 47.082  23.037  60.322  1.00 69.66  ? 184 GLU A OE2 1 
ATOM   1479  N N   . ALA A 1 189 ? 46.227  26.353  64.691  1.00 37.65  ? 185 ALA A N   1 
ATOM   1480  C CA  . ALA A 1 189 ? 46.317  26.437  66.153  1.00 35.41  ? 185 ALA A CA  1 
ATOM   1481  C C   . ALA A 1 189 ? 45.131  25.744  66.814  1.00 33.35  ? 185 ALA A C   1 
ATOM   1482  O O   . ALA A 1 189 ? 45.303  24.968  67.752  1.00 31.05  ? 185 ALA A O   1 
ATOM   1483  C CB  . ALA A 1 189 ? 46.413  27.889  66.607  1.00 31.24  ? 185 ALA A CB  1 
ATOM   1484  N N   . GLU A 1 190 ? 43.935  26.017  66.299  1.00 34.45  ? 186 GLU A N   1 
ATOM   1485  C CA  . GLU A 1 190 ? 42.707  25.364  66.749  1.00 33.63  ? 186 GLU A CA  1 
ATOM   1486  C C   . GLU A 1 190 ? 42.772  23.853  66.523  1.00 30.03  ? 186 GLU A C   1 
ATOM   1487  O O   . GLU A 1 190 ? 42.391  23.068  67.392  1.00 31.86  ? 186 GLU A O   1 
ATOM   1488  C CB  . GLU A 1 190 ? 41.518  25.961  65.999  1.00 39.20  ? 186 GLU A CB  1 
ATOM   1489  C CG  . GLU A 1 190 ? 40.145  25.573  66.535  1.00 45.05  ? 186 GLU A CG  1 
ATOM   1490  C CD  . GLU A 1 190 ? 39.020  26.327  65.843  1.00 51.89  ? 186 GLU A CD  1 
ATOM   1491  O OE1 . GLU A 1 190 ? 38.002  25.694  65.488  1.00 63.95  ? 186 GLU A OE1 1 
ATOM   1492  O OE2 . GLU A 1 190 ? 39.151  27.554  65.643  1.00 57.74  ? 186 GLU A OE2 1 
ATOM   1493  N N   . GLN A 1 191 ? 43.267  23.458  65.353  1.00 27.08  ? 187 GLN A N   1 
ATOM   1494  C CA  . GLN A 1 191 ? 43.428  22.049  64.989  1.00 26.93  ? 187 GLN A CA  1 
ATOM   1495  C C   . GLN A 1 191 ? 44.097  21.258  66.106  1.00 26.48  ? 187 GLN A C   1 
ATOM   1496  O O   . GLN A 1 191 ? 43.610  20.221  66.558  1.00 26.32  ? 187 GLN A O   1 
ATOM   1497  C CB  . GLN A 1 191 ? 44.318  21.944  63.746  1.00 27.95  ? 187 GLN A CB  1 
ATOM   1498  C CG  . GLN A 1 191 ? 43.778  21.083  62.623  1.00 29.94  ? 187 GLN A CG  1 
ATOM   1499  C CD  . GLN A 1 191 ? 43.170  19.782  63.104  1.00 24.35  ? 187 GLN A CD  1 
ATOM   1500  O OE1 . GLN A 1 191 ? 41.958  19.624  63.089  1.00 24.79  ? 187 GLN A OE1 1 
ATOM   1501  N NE2 . GLN A 1 191 ? 44.004  18.860  63.547  1.00 22.25  ? 187 GLN A NE2 1 
ATOM   1502  N N   . THR A 1 192 ? 45.226  21.788  66.541  1.00 26.07  ? 188 THR A N   1 
ATOM   1503  C CA  . THR A 1 192 ? 46.146  21.093  67.401  1.00 24.84  ? 188 THR A CA  1 
ATOM   1504  C C   . THR A 1 192 ? 45.745  21.277  68.878  1.00 27.75  ? 188 THR A C   1 
ATOM   1505  O O   . THR A 1 192 ? 45.983  20.396  69.707  1.00 27.90  ? 188 THR A O   1 
ATOM   1506  C CB  . THR A 1 192 ? 47.563  21.599  67.070  1.00 24.64  ? 188 THR A CB  1 
ATOM   1507  O OG1 . THR A 1 192 ? 48.462  20.495  66.920  1.00 29.17  ? 188 THR A OG1 1 
ATOM   1508  C CG2 . THR A 1 192 ? 48.041  22.579  68.094  1.00 25.07  ? 188 THR A CG2 1 
ATOM   1509  N N   . ARG A 1 193 ? 45.109  22.406  69.196  1.00 30.75  ? 189 ARG A N   1 
ATOM   1510  C CA  . ARG A 1 193 ? 44.476  22.598  70.505  1.00 32.65  ? 189 ARG A CA  1 
ATOM   1511  C C   . ARG A 1 193 ? 43.471  21.493  70.818  1.00 34.99  ? 189 ARG A C   1 
ATOM   1512  O O   . ARG A 1 193 ? 43.464  20.944  71.917  1.00 36.30  ? 189 ARG A O   1 
ATOM   1513  C CB  . ARG A 1 193 ? 43.714  23.934  70.598  1.00 34.55  ? 189 ARG A CB  1 
ATOM   1514  C CG  . ARG A 1 193 ? 44.323  24.935  71.566  1.00 35.68  ? 189 ARG A CG  1 
ATOM   1515  C CD  . ARG A 1 193 ? 43.285  25.745  72.339  1.00 38.79  ? 189 ARG A CD  1 
ATOM   1516  N NE  . ARG A 1 193 ? 42.012  25.946  71.637  1.00 44.35  ? 189 ARG A NE  1 
ATOM   1517  C CZ  . ARG A 1 193 ? 41.820  26.773  70.610  1.00 45.60  ? 189 ARG A CZ  1 
ATOM   1518  N NH1 . ARG A 1 193 ? 42.822  27.496  70.107  1.00 45.09  ? 189 ARG A NH1 1 
ATOM   1519  N NH2 . ARG A 1 193 ? 40.609  26.866  70.071  1.00 41.84  ? 189 ARG A NH2 1 
ATOM   1520  N N   . LEU A 1 194 ? 42.599  21.208  69.857  1.00 32.55  ? 190 LEU A N   1 
ATOM   1521  C CA  . LEU A 1 194 ? 41.489  20.276  70.069  1.00 31.62  ? 190 LEU A CA  1 
ATOM   1522  C C   . LEU A 1 194 ? 41.903  18.812  69.968  1.00 30.26  ? 190 LEU A C   1 
ATOM   1523  O O   . LEU A 1 194 ? 41.492  18.001  70.798  1.00 25.86  ? 190 LEU A O   1 
ATOM   1524  C CB  . LEU A 1 194 ? 40.364  20.554  69.073  1.00 30.56  ? 190 LEU A CB  1 
ATOM   1525  C CG  . LEU A 1 194 ? 39.695  21.916  69.225  1.00 31.41  ? 190 LEU A CG  1 
ATOM   1526  C CD1 . LEU A 1 194 ? 38.665  22.092  68.122  1.00 31.11  ? 190 LEU A CD1 1 
ATOM   1527  C CD2 . LEU A 1 194 ? 39.042  22.055  70.593  1.00 33.71  ? 190 LEU A CD2 1 
ATOM   1528  N N   . TYR A 1 195 ? 42.712  18.476  68.962  1.00 30.17  ? 191 TYR A N   1 
ATOM   1529  C CA  . TYR A 1 195 ? 43.036  17.072  68.681  1.00 30.11  ? 191 TYR A CA  1 
ATOM   1530  C C   . TYR A 1 195 ? 44.535  16.733  68.625  1.00 31.27  ? 191 TYR A C   1 
ATOM   1531  O O   . TYR A 1 195 ? 44.893  15.631  68.205  1.00 29.67  ? 191 TYR A O   1 
ATOM   1532  C CB  . TYR A 1 195 ? 42.369  16.636  67.370  1.00 28.10  ? 191 TYR A CB  1 
ATOM   1533  C CG  . TYR A 1 195 ? 41.026  17.281  67.109  1.00 26.56  ? 191 TYR A CG  1 
ATOM   1534  C CD1 . TYR A 1 195 ? 40.910  18.359  66.241  1.00 27.19  ? 191 TYR A CD1 1 
ATOM   1535  C CD2 . TYR A 1 195 ? 39.873  16.813  67.732  1.00 28.19  ? 191 TYR A CD2 1 
ATOM   1536  C CE1 . TYR A 1 195 ? 39.683  18.951  65.995  1.00 27.73  ? 191 TYR A CE1 1 
ATOM   1537  C CE2 . TYR A 1 195 ? 38.637  17.399  67.494  1.00 28.05  ? 191 TYR A CE2 1 
ATOM   1538  C CZ  . TYR A 1 195 ? 38.548  18.470  66.629  1.00 28.26  ? 191 TYR A CZ  1 
ATOM   1539  O OH  . TYR A 1 195 ? 37.326  19.055  66.399  1.00 27.20  ? 191 TYR A OH  1 
ATOM   1540  N N   . GLN A 1 196 ? 45.402  17.658  69.044  1.00 34.15  ? 192 GLN A N   1 
ATOM   1541  C CA  . GLN A 1 196 ? 46.866  17.445  69.072  1.00 34.73  ? 192 GLN A CA  1 
ATOM   1542  C C   . GLN A 1 196 ? 47.521  17.199  67.709  1.00 33.60  ? 192 GLN A C   1 
ATOM   1543  O O   . GLN A 1 196 ? 48.518  17.842  67.377  1.00 35.12  ? 192 GLN A O   1 
ATOM   1544  C CB  . GLN A 1 196 ? 47.251  16.299  70.020  1.00 36.81  ? 192 GLN A CB  1 
ATOM   1545  C CG  . GLN A 1 196 ? 47.823  16.745  71.357  1.00 39.94  ? 192 GLN A CG  1 
ATOM   1546  C CD  . GLN A 1 196 ? 49.156  17.442  71.260  1.00 37.33  ? 192 GLN A CD  1 
ATOM   1547  O OE1 . GLN A 1 196 ? 49.295  18.570  71.722  1.00 41.66  ? 192 GLN A OE1 1 
ATOM   1548  N NE2 . GLN A 1 196 ? 50.139  16.785  70.662  1.00 36.56  ? 192 GLN A NE2 1 
ATOM   1549  N N   . ASN A 1 197 ? 46.984  16.251  66.946  1.00 30.30  ? 193 ASN A N   1 
ATOM   1550  C CA  . ASN A 1 197 ? 47.568  15.864  65.667  1.00 29.99  ? 193 ASN A CA  1 
ATOM   1551  C C   . ASN A 1 197 ? 47.262  16.906  64.593  1.00 29.61  ? 193 ASN A C   1 
ATOM   1552  O O   . ASN A 1 197 ? 46.108  17.265  64.403  1.00 29.85  ? 193 ASN A O   1 
ATOM   1553  C CB  . ASN A 1 197 ? 47.032  14.496  65.235  1.00 30.82  ? 193 ASN A CB  1 
ATOM   1554  C CG  . ASN A 1 197 ? 47.137  13.447  66.330  1.00 31.82  ? 193 ASN A CG  1 
ATOM   1555  O OD1 . ASN A 1 197 ? 46.206  12.677  66.549  1.00 33.91  ? 193 ASN A OD1 1 
ATOM   1556  N ND2 . ASN A 1 197 ? 48.267  13.418  67.027  1.00 31.17  ? 193 ASN A ND2 1 
ATOM   1557  N N   . PRO A 1 198 ? 48.295  17.395  63.883  1.00 31.89  ? 194 PRO A N   1 
ATOM   1558  C CA  . PRO A 1 198 ? 48.103  18.437  62.862  1.00 32.50  ? 194 PRO A CA  1 
ATOM   1559  C C   . PRO A 1 198 ? 47.480  17.959  61.541  1.00 29.52  ? 194 PRO A C   1 
ATOM   1560  O O   . PRO A 1 198 ? 46.684  18.685  60.950  1.00 26.18  ? 194 PRO A O   1 
ATOM   1561  C CB  . PRO A 1 198 ? 49.526  18.952  62.623  1.00 32.20  ? 194 PRO A CB  1 
ATOM   1562  C CG  . PRO A 1 198 ? 50.394  17.780  62.917  1.00 33.56  ? 194 PRO A CG  1 
ATOM   1563  C CD  . PRO A 1 198 ? 49.714  17.024  64.026  1.00 32.02  ? 194 PRO A CD  1 
ATOM   1564  N N   . THR A 1 199 ? 47.851  16.761  61.087  1.00 31.18  ? 195 THR A N   1 
ATOM   1565  C CA  . THR A 1 199 ? 47.326  16.190  59.843  1.00 30.90  ? 195 THR A CA  1 
ATOM   1566  C C   . THR A 1 199 ? 46.425  15.002  60.154  1.00 27.64  ? 195 THR A C   1 
ATOM   1567  O O   . THR A 1 199 ? 46.875  14.010  60.720  1.00 29.08  ? 195 THR A O   1 
ATOM   1568  C CB  . THR A 1 199 ? 48.462  15.716  58.925  1.00 32.43  ? 195 THR A CB  1 
ATOM   1569  O OG1 . THR A 1 199 ? 49.326  16.819  58.633  1.00 37.27  ? 195 THR A OG1 1 
ATOM   1570  C CG2 . THR A 1 199 ? 47.899  15.139  57.621  1.00 30.11  ? 195 THR A CG2 1 
ATOM   1571  N N   . THR A 1 200 ? 45.167  15.090  59.739  1.00 27.57  ? 196 THR A N   1 
ATOM   1572  C CA  . THR A 1 200 ? 44.130  14.215  60.267  1.00 27.48  ? 196 THR A CA  1 
ATOM   1573  C C   . THR A 1 200 ? 43.148  13.703  59.220  1.00 25.76  ? 196 THR A C   1 
ATOM   1574  O O   . THR A 1 200 ? 43.101  14.206  58.102  1.00 26.86  ? 196 THR A O   1 
ATOM   1575  C CB  . THR A 1 200 ? 43.363  14.945  61.394  1.00 30.59  ? 196 THR A CB  1 
ATOM   1576  O OG1 . THR A 1 200 ? 42.337  14.100  61.934  1.00 36.94  ? 196 THR A OG1 1 
ATOM   1577  C CG2 . THR A 1 200 ? 42.745  16.228  60.872  1.00 28.22  ? 196 THR A CG2 1 
ATOM   1578  N N   . TYR A 1 201 ? 42.370  12.692  59.605  1.00 25.97  ? 197 TYR A N   1 
ATOM   1579  C CA  . TYR A 1 201 ? 41.426  12.028  58.705  1.00 25.35  ? 197 TYR A CA  1 
ATOM   1580  C C   . TYR A 1 201 ? 40.350  11.242  59.461  1.00 25.63  ? 197 TYR A C   1 
ATOM   1581  O O   . TYR A 1 201 ? 40.493  10.954  60.652  1.00 26.73  ? 197 TYR A O   1 
ATOM   1582  C CB  . TYR A 1 201 ? 42.167  11.064  57.772  1.00 25.05  ? 197 TYR A CB  1 
ATOM   1583  C CG  . TYR A 1 201 ? 42.692  9.822   58.468  1.00 26.99  ? 197 TYR A CG  1 
ATOM   1584  C CD1 . TYR A 1 201 ? 41.932  8.655   58.523  1.00 26.96  ? 197 TYR A CD1 1 
ATOM   1585  C CD2 . TYR A 1 201 ? 43.948  9.814   59.078  1.00 28.68  ? 197 TYR A CD2 1 
ATOM   1586  C CE1 . TYR A 1 201 ? 42.402  7.517   59.167  1.00 26.67  ? 197 TYR A CE1 1 
ATOM   1587  C CE2 . TYR A 1 201 ? 44.428  8.680   59.722  1.00 29.02  ? 197 TYR A CE2 1 
ATOM   1588  C CZ  . TYR A 1 201 ? 43.652  7.534   59.765  1.00 27.83  ? 197 TYR A CZ  1 
ATOM   1589  O OH  . TYR A 1 201 ? 44.127  6.405   60.398  1.00 24.38  ? 197 TYR A OH  1 
ATOM   1590  N N   . ILE A 1 202 ? 39.281  10.892  58.749  1.00 24.81  ? 198 ILE A N   1 
ATOM   1591  C CA  . ILE A 1 202 ? 38.303  9.916   59.225  1.00 25.72  ? 198 ILE A CA  1 
ATOM   1592  C C   . ILE A 1 202 ? 37.970  8.974   58.077  1.00 27.39  ? 198 ILE A C   1 
ATOM   1593  O O   . ILE A 1 202 ? 37.579  9.435   57.008  1.00 25.70  ? 198 ILE A O   1 
ATOM   1594  C CB  . ILE A 1 202 ? 36.969  10.557  59.662  1.00 23.90  ? 198 ILE A CB  1 
ATOM   1595  C CG1 . ILE A 1 202 ? 37.194  11.762  60.577  1.00 24.84  ? 198 ILE A CG1 1 
ATOM   1596  C CG2 . ILE A 1 202 ? 36.090  9.518   60.337  1.00 21.94  ? 198 ILE A CG2 1 
ATOM   1597  C CD1 . ILE A 1 202 ? 35.945  12.586  60.812  1.00 24.30  ? 198 ILE A CD1 1 
ATOM   1598  N N   . SER A 1 203 ? 38.105  7.667   58.290  1.00 27.94  ? 199 SER A N   1 
ATOM   1599  C CA  . SER A 1 203 ? 37.624  6.695   57.306  1.00 28.51  ? 199 SER A CA  1 
ATOM   1600  C C   . SER A 1 203 ? 36.437  5.922   57.869  1.00 26.29  ? 199 SER A C   1 
ATOM   1601  O O   . SER A 1 203 ? 36.400  5.610   59.056  1.00 27.43  ? 199 SER A O   1 
ATOM   1602  C CB  . SER A 1 203 ? 38.738  5.747   56.862  1.00 28.83  ? 199 SER A CB  1 
ATOM   1603  O OG  . SER A 1 203 ? 39.321  5.083   57.959  1.00 29.37  ? 199 SER A OG  1 
ATOM   1604  N N   . ILE A 1 204 ? 35.461  5.645   57.011  1.00 25.14  ? 200 ILE A N   1 
ATOM   1605  C CA  . ILE A 1 204 ? 34.254  4.923   57.398  1.00 25.35  ? 200 ILE A CA  1 
ATOM   1606  C C   . ILE A 1 204 ? 34.017  3.789   56.413  1.00 23.42  ? 200 ILE A C   1 
ATOM   1607  O O   . ILE A 1 204 ? 34.007  4.009   55.204  1.00 21.81  ? 200 ILE A O   1 
ATOM   1608  C CB  . ILE A 1 204 ? 33.006  5.835   57.417  1.00 25.90  ? 200 ILE A CB  1 
ATOM   1609  C CG1 . ILE A 1 204 ? 33.308  7.171   58.101  1.00 25.24  ? 200 ILE A CG1 1 
ATOM   1610  C CG2 . ILE A 1 204 ? 31.859  5.132   58.123  1.00 23.63  ? 200 ILE A CG2 1 
ATOM   1611  C CD1 . ILE A 1 204 ? 33.881  8.210   57.166  1.00 26.12  ? 200 ILE A CD1 1 
ATOM   1612  N N   . GLY A 1 205 ? 33.816  2.584   56.941  1.00 25.69  ? 201 GLY A N   1 
ATOM   1613  C CA  . GLY A 1 205 ? 33.674  1.380   56.125  1.00 26.01  ? 201 GLY A CA  1 
ATOM   1614  C C   . GLY A 1 205 ? 32.382  0.631   56.383  1.00 27.64  ? 201 GLY A C   1 
ATOM   1615  O O   . GLY A 1 205 ? 31.840  0.659   57.484  1.00 27.04  ? 201 GLY A O   1 
ATOM   1616  N N   . THR A 1 206 ? 31.879  -0.019  55.339  1.00 29.40  ? 202 THR A N   1 
ATOM   1617  C CA  . THR A 1 206 ? 30.674  -0.814  55.394  1.00 28.25  ? 202 THR A CA  1 
ATOM   1618  C C   . THR A 1 206 ? 30.808  -1.824  54.249  1.00 29.61  ? 202 THR A C   1 
ATOM   1619  O O   . THR A 1 206 ? 31.843  -1.853  53.573  1.00 32.28  ? 202 THR A O   1 
ATOM   1620  C CB  . THR A 1 206 ? 29.488  0.161   55.286  1.00 28.07  ? 202 THR A CB  1 
ATOM   1621  O OG1 . THR A 1 206 ? 29.159  0.633   56.598  1.00 26.06  ? 202 THR A OG1 1 
ATOM   1622  C CG2 . THR A 1 206 ? 28.251  -0.448  54.631  1.00 29.11  ? 202 THR A CG2 1 
ATOM   1623  N N   . SER A 1 207 ? 29.822  -2.693  54.050  1.00 30.09  ? 203 SER A N   1 
ATOM   1624  C CA  . SER A 1 207 ? 29.857  -3.587  52.890  1.00 29.39  ? 203 SER A CA  1 
ATOM   1625  C C   . SER A 1 207 ? 29.848  -2.780  51.574  1.00 29.65  ? 203 SER A C   1 
ATOM   1626  O O   . SER A 1 207 ? 30.340  -3.236  50.533  1.00 27.34  ? 203 SER A O   1 
ATOM   1627  C CB  . SER A 1 207 ? 28.673  -4.552  52.922  1.00 27.02  ? 203 SER A CB  1 
ATOM   1628  O OG  . SER A 1 207 ? 27.444  -3.875  52.757  1.00 25.16  ? 203 SER A OG  1 
ATOM   1629  N N   . THR A 1 208 ? 29.310  -1.564  51.655  1.00 31.50  ? 204 THR A N   1 
ATOM   1630  C CA  . THR A 1 208 ? 28.989  -0.745  50.496  1.00 32.81  ? 204 THR A CA  1 
ATOM   1631  C C   . THR A 1 208 ? 29.609  0.655   50.550  1.00 32.59  ? 204 THR A C   1 
ATOM   1632  O O   . THR A 1 208 ? 29.789  1.275   49.507  1.00 31.32  ? 204 THR A O   1 
ATOM   1633  C CB  . THR A 1 208 ? 27.463  -0.614  50.347  1.00 36.40  ? 204 THR A CB  1 
ATOM   1634  O OG1 . THR A 1 208 ? 27.140  0.007   49.093  1.00 47.63  ? 204 THR A OG1 1 
ATOM   1635  C CG2 . THR A 1 208 ? 26.853  0.194   51.497  1.00 35.90  ? 204 THR A CG2 1 
ATOM   1636  N N   . LEU A 1 209 ? 29.920  1.148   51.753  1.00 33.58  ? 205 LEU A N   1 
ATOM   1637  C CA  . LEU A 1 209 ? 30.511  2.479   51.940  1.00 29.64  ? 205 LEU A CA  1 
ATOM   1638  C C   . LEU A 1 209 ? 32.027  2.394   52.082  1.00 26.52  ? 205 LEU A C   1 
ATOM   1639  O O   . LEU A 1 209 ? 32.544  1.529   52.784  1.00 22.93  ? 205 LEU A O   1 
ATOM   1640  C CB  . LEU A 1 209 ? 29.927  3.150   53.188  1.00 31.05  ? 205 LEU A CB  1 
ATOM   1641  C CG  . LEU A 1 209 ? 30.327  4.596   53.510  1.00 33.66  ? 205 LEU A CG  1 
ATOM   1642  C CD1 . LEU A 1 209 ? 29.629  5.583   52.584  1.00 31.90  ? 205 LEU A CD1 1 
ATOM   1643  C CD2 . LEU A 1 209 ? 30.011  4.907   54.964  1.00 34.86  ? 205 LEU A CD2 1 
ATOM   1644  N N   . ASN A 1 210 ? 32.723  3.306   51.411  1.00 26.73  ? 206 ASN A N   1 
ATOM   1645  C CA  . ASN A 1 210 ? 34.183  3.389   51.459  1.00 26.15  ? 206 ASN A CA  1 
ATOM   1646  C C   . ASN A 1 210 ? 34.603  4.855   51.375  1.00 26.99  ? 206 ASN A C   1 
ATOM   1647  O O   . ASN A 1 210 ? 34.892  5.367   50.294  1.00 30.04  ? 206 ASN A O   1 
ATOM   1648  C CB  . ASN A 1 210 ? 34.796  2.581   50.308  1.00 23.50  ? 206 ASN A CB  1 
ATOM   1649  C CG  . ASN A 1 210 ? 36.304  2.717   50.234  1.00 23.94  ? 206 ASN A CG  1 
ATOM   1650  O OD1 . ASN A 1 210 ? 36.981  2.875   51.258  1.00 24.33  ? 206 ASN A OD1 1 
ATOM   1651  N ND2 . ASN A 1 210 ? 36.844  2.655   49.015  1.00 22.66  ? 206 ASN A ND2 1 
ATOM   1652  N N   . GLN A 1 211 ? 34.623  5.525   52.523  1.00 25.77  ? 207 GLN A N   1 
ATOM   1653  C CA  . GLN A 1 211 ? 34.775  6.973   52.575  1.00 26.32  ? 207 GLN A CA  1 
ATOM   1654  C C   . GLN A 1 211 ? 35.977  7.396   53.416  1.00 24.73  ? 207 GLN A C   1 
ATOM   1655  O O   . GLN A 1 211 ? 36.243  6.802   54.446  1.00 24.41  ? 207 GLN A O   1 
ATOM   1656  C CB  . GLN A 1 211 ? 33.490  7.576   53.140  1.00 28.43  ? 207 GLN A CB  1 
ATOM   1657  C CG  . GLN A 1 211 ? 33.466  9.089   53.253  1.00 30.87  ? 207 GLN A CG  1 
ATOM   1658  C CD  . GLN A 1 211 ? 32.068  9.638   53.432  1.00 34.30  ? 207 GLN A CD  1 
ATOM   1659  O OE1 . GLN A 1 211 ? 31.281  9.113   54.213  1.00 35.16  ? 207 GLN A OE1 1 
ATOM   1660  N NE2 . GLN A 1 211 ? 31.755  10.707  52.707  1.00 37.70  ? 207 GLN A NE2 1 
ATOM   1661  N N   . ARG A 1 212 ? 36.706  8.410   52.954  1.00 24.99  ? 208 ARG A N   1 
ATOM   1662  C CA  . ARG A 1 212 ? 37.785  9.023   53.728  1.00 25.79  ? 208 ARG A CA  1 
ATOM   1663  C C   . ARG A 1 212 ? 37.591  10.535  53.725  1.00 25.92  ? 208 ARG A C   1 
ATOM   1664  O O   . ARG A 1 212 ? 37.556  11.158  52.667  1.00 26.95  ? 208 ARG A O   1 
ATOM   1665  C CB  . ARG A 1 212 ? 39.158  8.665   53.160  1.00 27.20  ? 208 ARG A CB  1 
ATOM   1666  C CG  . ARG A 1 212 ? 40.311  8.989   54.101  1.00 30.53  ? 208 ARG A CG  1 
ATOM   1667  C CD  . ARG A 1 212 ? 41.655  8.617   53.502  1.00 33.70  ? 208 ARG A CD  1 
ATOM   1668  N NE  . ARG A 1 212 ? 42.776  8.939   54.392  1.00 37.57  ? 208 ARG A NE  1 
ATOM   1669  C CZ  . ARG A 1 212 ? 43.308  8.115   55.301  1.00 41.66  ? 208 ARG A CZ  1 
ATOM   1670  N NH1 . ARG A 1 212 ? 42.833  6.884   55.481  1.00 41.10  ? 208 ARG A NH1 1 
ATOM   1671  N NH2 . ARG A 1 212 ? 44.332  8.529   56.047  1.00 41.58  ? 208 ARG A NH2 1 
ATOM   1672  N N   . LEU A 1 213 ? 37.449  11.109  54.916  1.00 26.43  ? 209 LEU A N   1 
ATOM   1673  C CA  . LEU A 1 213 ? 37.187  12.533  55.085  1.00 26.69  ? 209 LEU A CA  1 
ATOM   1674  C C   . LEU A 1 213 ? 38.417  13.203  55.681  1.00 27.64  ? 209 LEU A C   1 
ATOM   1675  O O   . LEU A 1 213 ? 39.029  12.668  56.605  1.00 27.56  ? 209 LEU A O   1 
ATOM   1676  C CB  . LEU A 1 213 ? 35.989  12.743  56.013  1.00 25.38  ? 209 LEU A CB  1 
ATOM   1677  C CG  . LEU A 1 213 ? 34.659  12.139  55.554  1.00 24.71  ? 209 LEU A CG  1 
ATOM   1678  C CD1 . LEU A 1 213 ? 33.673  12.113  56.710  1.00 23.73  ? 209 LEU A CD1 1 
ATOM   1679  C CD2 . LEU A 1 213 ? 34.082  12.891  54.367  1.00 23.99  ? 209 LEU A CD2 1 
ATOM   1680  N N   . VAL A 1 214 ? 38.773  14.366  55.138  1.00 27.65  ? 210 VAL A N   1 
ATOM   1681  C CA  . VAL A 1 214 ? 39.919  15.139  55.601  1.00 26.94  ? 210 VAL A CA  1 
ATOM   1682  C C   . VAL A 1 214 ? 39.430  16.554  55.904  1.00 25.58  ? 210 VAL A C   1 
ATOM   1683  O O   . VAL A 1 214 ? 38.690  17.134  55.108  1.00 28.21  ? 210 VAL A O   1 
ATOM   1684  C CB  . VAL A 1 214 ? 41.037  15.168  54.531  1.00 28.04  ? 210 VAL A CB  1 
ATOM   1685  C CG1 . VAL A 1 214 ? 42.227  15.992  55.008  1.00 28.10  ? 210 VAL A CG1 1 
ATOM   1686  C CG2 . VAL A 1 214 ? 41.485  13.753  54.186  1.00 25.42  ? 210 VAL A CG2 1 
ATOM   1687  N N   . PRO A 1 215 ? 39.808  17.111  57.066  1.00 25.21  ? 211 PRO A N   1 
ATOM   1688  C CA  . PRO A 1 215 ? 39.317  18.459  57.394  1.00 26.92  ? 211 PRO A CA  1 
ATOM   1689  C C   . PRO A 1 215 ? 39.865  19.541  56.465  1.00 27.42  ? 211 PRO A C   1 
ATOM   1690  O O   . PRO A 1 215 ? 40.994  19.439  55.990  1.00 27.75  ? 211 PRO A O   1 
ATOM   1691  C CB  . PRO A 1 215 ? 39.800  18.706  58.831  1.00 24.32  ? 211 PRO A CB  1 
ATOM   1692  C CG  . PRO A 1 215 ? 40.421  17.455  59.298  1.00 24.13  ? 211 PRO A CG  1 
ATOM   1693  C CD  . PRO A 1 215 ? 40.572  16.498  58.161  1.00 25.31  ? 211 PRO A CD  1 
ATOM   1694  N N   . LYS A 1 216 ? 39.064  20.578  56.251  1.00 29.47  ? 212 LYS A N   1 
ATOM   1695  C CA  . LYS A 1 216 ? 39.432  21.709  55.420  1.00 31.50  ? 212 LYS A CA  1 
ATOM   1696  C C   . LYS A 1 216 ? 39.607  22.925  56.324  1.00 34.66  ? 212 LYS A C   1 
ATOM   1697  O O   . LYS A 1 216 ? 38.636  23.444  56.855  1.00 38.76  ? 212 LYS A O   1 
ATOM   1698  C CB  . LYS A 1 216 ? 38.348  21.946  54.370  1.00 30.78  ? 212 LYS A CB  1 
ATOM   1699  C CG  . LYS A 1 216 ? 38.195  20.781  53.400  1.00 33.69  ? 212 LYS A CG  1 
ATOM   1700  C CD  . LYS A 1 216 ? 37.260  21.095  52.242  1.00 36.06  ? 212 LYS A CD  1 
ATOM   1701  C CE  . LYS A 1 216 ? 35.798  20.941  52.619  1.00 40.33  ? 212 LYS A CE  1 
ATOM   1702  N NZ  . LYS A 1 216 ? 35.416  19.507  52.748  1.00 45.92  ? 212 LYS A NZ  1 
ATOM   1703  N N   . ILE A 1 217 ? 40.853  23.352  56.517  1.00 37.81  ? 213 ILE A N   1 
ATOM   1704  C CA  . ILE A 1 217 ? 41.193  24.443  57.432  1.00 39.09  ? 213 ILE A CA  1 
ATOM   1705  C C   . ILE A 1 217 ? 41.265  25.767  56.665  1.00 43.41  ? 213 ILE A C   1 
ATOM   1706  O O   . ILE A 1 217 ? 42.178  25.972  55.865  1.00 47.89  ? 213 ILE A O   1 
ATOM   1707  C CB  . ILE A 1 217 ? 42.543  24.158  58.134  1.00 38.02  ? 213 ILE A CB  1 
ATOM   1708  C CG1 . ILE A 1 217 ? 42.447  22.890  58.992  1.00 42.47  ? 213 ILE A CG1 1 
ATOM   1709  C CG2 . ILE A 1 217 ? 42.967  25.330  59.004  1.00 38.31  ? 213 ILE A CG2 1 
ATOM   1710  C CD1 . ILE A 1 217 ? 43.747  22.122  59.111  1.00 45.60  ? 213 ILE A CD1 1 
ATOM   1711  N N   . ALA A 1 218 ? 40.302  26.657  56.911  1.00 45.96  ? 214 ALA A N   1 
ATOM   1712  C CA  . ALA A 1 218 ? 40.183  27.908  56.150  1.00 50.40  ? 214 ALA A CA  1 
ATOM   1713  C C   . ALA A 1 218 ? 39.506  29.016  56.960  1.00 53.59  ? 214 ALA A C   1 
ATOM   1714  O O   . ALA A 1 218 ? 38.896  28.760  57.999  1.00 49.07  ? 214 ALA A O   1 
ATOM   1715  C CB  . ALA A 1 218 ? 39.422  27.666  54.852  1.00 40.33  ? 214 ALA A CB  1 
ATOM   1716  N N   . THR A 1 219 ? 39.629  30.248  56.466  1.00 60.66  ? 215 THR A N   1 
ATOM   1717  C CA  . THR A 1 219 ? 39.003  31.413  57.085  1.00 57.28  ? 215 THR A CA  1 
ATOM   1718  C C   . THR A 1 219 ? 37.564  31.524  56.606  1.00 54.35  ? 215 THR A C   1 
ATOM   1719  O O   . THR A 1 219 ? 37.303  31.501  55.402  1.00 48.58  ? 215 THR A O   1 
ATOM   1720  C CB  . THR A 1 219 ? 39.745  32.712  56.729  1.00 61.70  ? 215 THR A CB  1 
ATOM   1721  O OG1 . THR A 1 219 ? 41.146  32.551  56.984  1.00 71.74  ? 215 THR A OG1 1 
ATOM   1722  C CG2 . THR A 1 219 ? 39.213  33.875  57.555  1.00 63.97  ? 215 THR A CG2 1 
ATOM   1723  N N   . ARG A 1 220 ? 36.636  31.644  57.554  1.00 51.03  ? 216 ARG A N   1 
ATOM   1724  C CA  . ARG A 1 220 ? 35.209  31.699  57.244  1.00 46.87  ? 216 ARG A CA  1 
ATOM   1725  C C   . ARG A 1 220 ? 34.502  32.787  58.034  1.00 44.99  ? 216 ARG A C   1 
ATOM   1726  O O   . ARG A 1 220 ? 34.947  33.174  59.115  1.00 43.76  ? 216 ARG A O   1 
ATOM   1727  C CB  . ARG A 1 220 ? 34.556  30.354  57.556  1.00 45.73  ? 216 ARG A CB  1 
ATOM   1728  C CG  . ARG A 1 220 ? 34.983  29.246  56.619  1.00 41.84  ? 216 ARG A CG  1 
ATOM   1729  C CD  . ARG A 1 220 ? 34.454  27.895  57.056  1.00 37.78  ? 216 ARG A CD  1 
ATOM   1730  N NE  . ARG A 1 220 ? 35.454  26.861  56.814  1.00 35.08  ? 216 ARG A NE  1 
ATOM   1731  C CZ  . ARG A 1 220 ? 36.224  26.301  57.745  1.00 32.96  ? 216 ARG A CZ  1 
ATOM   1732  N NH1 . ARG A 1 220 ? 36.131  26.637  59.030  1.00 31.55  ? 216 ARG A NH1 1 
ATOM   1733  N NH2 . ARG A 1 220 ? 37.102  25.381  57.376  1.00 32.48  ? 216 ARG A NH2 1 
ATOM   1734  N N   . SER A 1 221 ? 33.388  33.262  57.486  1.00 41.98  ? 217 SER A N   1 
ATOM   1735  C CA  . SER A 1 221 ? 32.536  34.219  58.171  1.00 41.25  ? 217 SER A CA  1 
ATOM   1736  C C   . SER A 1 221 ? 31.873  33.531  59.361  1.00 40.76  ? 217 SER A C   1 
ATOM   1737  O O   . SER A 1 221 ? 31.505  32.359  59.281  1.00 40.32  ? 217 SER A O   1 
ATOM   1738  C CB  . SER A 1 221 ? 31.469  34.759  57.218  1.00 41.76  ? 217 SER A CB  1 
ATOM   1739  O OG  . SER A 1 221 ? 32.053  35.311  56.050  1.00 43.58  ? 217 SER A OG  1 
ATOM   1740  N N   . LYS A 1 222 ? 31.733  34.258  60.465  1.00 40.59  ? 218 LYS A N   1 
ATOM   1741  C CA  . LYS A 1 222 ? 31.097  33.714  61.664  1.00 39.01  ? 218 LYS A CA  1 
ATOM   1742  C C   . LYS A 1 222 ? 29.602  33.527  61.443  1.00 35.37  ? 218 LYS A C   1 
ATOM   1743  O O   . LYS A 1 222 ? 28.966  34.312  60.743  1.00 35.17  ? 218 LYS A O   1 
ATOM   1744  C CB  . LYS A 1 222 ? 31.343  34.615  62.884  1.00 39.99  ? 218 LYS A CB  1 
ATOM   1745  C CG  . LYS A 1 222 ? 32.587  34.242  63.668  1.00 43.41  ? 218 LYS A CG  1 
ATOM   1746  C CD  . LYS A 1 222 ? 32.890  35.231  64.783  1.00 47.23  ? 218 LYS A CD  1 
ATOM   1747  C CE  . LYS A 1 222 ? 33.978  34.680  65.709  1.00 49.89  ? 218 LYS A CE  1 
ATOM   1748  N NZ  . LYS A 1 222 ? 34.514  35.703  66.650  1.00 47.80  ? 218 LYS A NZ  1 
ATOM   1749  N N   . ILE A 1 223 ? 29.059  32.467  62.028  1.00 34.45  ? 219 ILE A N   1 
ATOM   1750  C CA  . ILE A 1 223 ? 27.621  32.215  62.011  1.00 35.57  ? 219 ILE A CA  1 
ATOM   1751  C C   . ILE A 1 223 ? 27.268  31.504  63.314  1.00 36.53  ? 219 ILE A C   1 
ATOM   1752  O O   . ILE A 1 223 ? 27.820  30.448  63.620  1.00 35.39  ? 219 ILE A O   1 
ATOM   1753  C CB  . ILE A 1 223 ? 27.191  31.408  60.764  1.00 37.86  ? 219 ILE A CB  1 
ATOM   1754  C CG1 . ILE A 1 223 ? 25.798  30.803  60.951  1.00 40.44  ? 219 ILE A CG1 1 
ATOM   1755  C CG2 . ILE A 1 223 ? 28.202  30.319  60.438  1.00 38.27  ? 219 ILE A CG2 1 
ATOM   1756  C CD1 . ILE A 1 223 ? 25.214  30.265  59.661  1.00 43.72  ? 219 ILE A CD1 1 
ATOM   1757  N N   . ASN A 1 224 ? 26.357  32.107  64.079  1.00 38.13  ? 220 ASN A N   1 
ATOM   1758  C CA  . ASN A 1 224 ? 26.131  31.752  65.484  1.00 34.98  ? 220 ASN A CA  1 
ATOM   1759  C C   . ASN A 1 224 ? 27.413  31.885  66.306  1.00 35.16  ? 220 ASN A C   1 
ATOM   1760  O O   . ASN A 1 224 ? 27.654  31.117  67.241  1.00 36.77  ? 220 ASN A O   1 
ATOM   1761  C CB  . ASN A 1 224 ? 25.531  30.347  65.608  1.00 34.79  ? 220 ASN A CB  1 
ATOM   1762  C CG  . ASN A 1 224 ? 24.213  30.219  64.878  1.00 35.55  ? 220 ASN A CG  1 
ATOM   1763  O OD1 . ASN A 1 224 ? 23.436  31.168  64.810  1.00 35.61  ? 220 ASN A OD1 1 
ATOM   1764  N ND2 . ASN A 1 224 ? 23.969  29.048  64.299  1.00 35.64  ? 220 ASN A ND2 1 
ATOM   1765  N N   . GLY A 1 225 ? 28.229  32.874  65.944  1.00 34.83  ? 221 GLY A N   1 
ATOM   1766  C CA  . GLY A 1 225 ? 29.495  33.136  66.622  1.00 34.33  ? 221 GLY A CA  1 
ATOM   1767  C C   . GLY A 1 225 ? 30.595  32.120  66.367  1.00 34.19  ? 221 GLY A C   1 
ATOM   1768  O O   . GLY A 1 225 ? 31.588  32.094  67.094  1.00 34.04  ? 221 GLY A O   1 
ATOM   1769  N N   . GLN A 1 226 ? 30.439  31.298  65.329  1.00 35.04  ? 222 GLN A N   1 
ATOM   1770  C CA  . GLN A 1 226 ? 31.411  30.246  65.016  1.00 33.84  ? 222 GLN A CA  1 
ATOM   1771  C C   . GLN A 1 226 ? 31.877  30.328  63.567  1.00 31.28  ? 222 GLN A C   1 
ATOM   1772  O O   . GLN A 1 226 ? 31.059  30.399  62.649  1.00 29.43  ? 222 GLN A O   1 
ATOM   1773  C CB  . GLN A 1 226 ? 30.800  28.866  65.265  1.00 35.09  ? 222 GLN A CB  1 
ATOM   1774  C CG  . GLN A 1 226 ? 30.266  28.648  66.674  1.00 37.35  ? 222 GLN A CG  1 
ATOM   1775  C CD  . GLN A 1 226 ? 31.335  28.745  67.741  1.00 41.89  ? 222 GLN A CD  1 
ATOM   1776  O OE1 . GLN A 1 226 ? 32.467  28.294  67.549  1.00 48.85  ? 222 GLN A OE1 1 
ATOM   1777  N NE2 . GLN A 1 226 ? 30.980  29.328  68.880  1.00 46.16  ? 222 GLN A NE2 1 
ATOM   1778  N N   . SER A 1 227 ? 33.195  30.328  63.373  1.00 32.88  ? 223 SER A N   1 
ATOM   1779  C CA  . SER A 1 227 ? 33.788  30.235  62.037  1.00 36.07  ? 223 SER A CA  1 
ATOM   1780  C C   . SER A 1 227 ? 34.125  28.790  61.684  1.00 37.07  ? 223 SER A C   1 
ATOM   1781  O O   . SER A 1 227 ? 34.357  28.475  60.516  1.00 41.56  ? 223 SER A O   1 
ATOM   1782  C CB  . SER A 1 227 ? 35.037  31.108  61.925  1.00 39.56  ? 223 SER A CB  1 
ATOM   1783  O OG  . SER A 1 227 ? 34.682  32.447  61.633  1.00 41.73  ? 223 SER A OG  1 
ATOM   1784  N N   . GLY A 1 228 ? 34.153  27.917  62.691  1.00 33.64  ? 224 GLY A N   1 
ATOM   1785  C CA  . GLY A 1 228 ? 34.286  26.486  62.459  1.00 30.50  ? 224 GLY A CA  1 
ATOM   1786  C C   . GLY A 1 228 ? 33.017  25.926  61.841  1.00 28.85  ? 224 GLY A C   1 
ATOM   1787  O O   . GLY A 1 228 ? 31.959  26.550  61.902  1.00 29.21  ? 224 GLY A O   1 
ATOM   1788  N N   . ARG A 1 229 ? 33.128  24.752  61.227  1.00 28.56  ? 225 ARG A N   1 
ATOM   1789  C CA  . ARG A 1 229 ? 31.986  24.081  60.610  1.00 26.34  ? 225 ARG A CA  1 
ATOM   1790  C C   . ARG A 1 229 ? 32.014  22.607  60.953  1.00 27.22  ? 225 ARG A C   1 
ATOM   1791  O O   . ARG A 1 229 ? 33.075  22.052  61.228  1.00 27.01  ? 225 ARG A O   1 
ATOM   1792  C CB  . ARG A 1 229 ? 32.030  24.233  59.094  1.00 26.36  ? 225 ARG A CB  1 
ATOM   1793  C CG  . ARG A 1 229 ? 31.931  25.664  58.592  1.00 26.59  ? 225 ARG A CG  1 
ATOM   1794  C CD  . ARG A 1 229 ? 30.515  26.194  58.683  1.00 28.76  ? 225 ARG A CD  1 
ATOM   1795  N NE  . ARG A 1 229 ? 30.428  27.546  58.140  1.00 31.20  ? 225 ARG A NE  1 
ATOM   1796  C CZ  . ARG A 1 229 ? 30.713  28.662  58.811  1.00 32.06  ? 225 ARG A CZ  1 
ATOM   1797  N NH1 . ARG A 1 229 ? 31.107  28.623  60.082  1.00 31.79  ? 225 ARG A NH1 1 
ATOM   1798  N NH2 . ARG A 1 229 ? 30.594  29.836  58.202  1.00 32.55  ? 225 ARG A NH2 1 
ATOM   1799  N N   . ILE A 1 230 ? 30.844  21.976  60.945  1.00 28.24  ? 226 ILE A N   1 
ATOM   1800  C CA  . ILE A 1 230 ? 30.757  20.529  61.077  1.00 27.63  ? 226 ILE A CA  1 
ATOM   1801  C C   . ILE A 1 230 ? 29.861  19.973  59.976  1.00 28.16  ? 226 ILE A C   1 
ATOM   1802  O O   . ILE A 1 230 ? 28.697  20.342  59.876  1.00 24.94  ? 226 ILE A O   1 
ATOM   1803  C CB  . ILE A 1 230 ? 30.217  20.108  62.452  1.00 27.94  ? 226 ILE A CB  1 
ATOM   1804  C CG1 . ILE A 1 230 ? 31.209  20.502  63.554  1.00 29.75  ? 226 ILE A CG1 1 
ATOM   1805  C CG2 . ILE A 1 230 ? 29.956  18.609  62.481  1.00 27.49  ? 226 ILE A CG2 1 
ATOM   1806  C CD1 . ILE A 1 230 ? 30.669  20.328  64.957  1.00 28.19  ? 226 ILE A CD1 1 
ATOM   1807  N N   . ASP A 1 231 ? 30.418  19.092  59.152  1.00 29.30  ? 227 ASP A N   1 
ATOM   1808  C CA  . ASP A 1 231 ? 29.660  18.435  58.093  1.00 30.31  ? 227 ASP A CA  1 
ATOM   1809  C C   . ASP A 1 231 ? 29.227  17.055  58.569  1.00 28.80  ? 227 ASP A C   1 
ATOM   1810  O O   . ASP A 1 231 ? 30.022  16.326  59.166  1.00 29.07  ? 227 ASP A O   1 
ATOM   1811  C CB  . ASP A 1 231 ? 30.508  18.300  56.824  1.00 32.56  ? 227 ASP A CB  1 
ATOM   1812  C CG  . ASP A 1 231 ? 30.811  19.641  56.171  1.00 35.36  ? 227 ASP A CG  1 
ATOM   1813  O OD1 . ASP A 1 231 ? 30.246  20.669  56.598  1.00 39.01  ? 227 ASP A OD1 1 
ATOM   1814  O OD2 . ASP A 1 231 ? 31.614  19.665  55.220  1.00 38.10  ? 227 ASP A OD2 1 
ATOM   1815  N N   . PHE A 1 232 ? 27.974  16.699  58.295  1.00 25.28  ? 228 PHE A N   1 
ATOM   1816  C CA  . PHE A 1 232 ? 27.422  15.421  58.727  1.00 23.79  ? 228 PHE A CA  1 
ATOM   1817  C C   . PHE A 1 232 ? 27.150  14.508  57.549  1.00 22.79  ? 228 PHE A C   1 
ATOM   1818  O O   . PHE A 1 232 ? 26.796  14.962  56.459  1.00 21.86  ? 228 PHE A O   1 
ATOM   1819  C CB  . PHE A 1 232 ? 26.131  15.634  59.510  1.00 24.30  ? 228 PHE A CB  1 
ATOM   1820  C CG  . PHE A 1 232 ? 26.348  16.182  60.883  1.00 25.29  ? 228 PHE A CG  1 
ATOM   1821  C CD1 . PHE A 1 232 ? 26.166  17.531  61.145  1.00 26.42  ? 228 PHE A CD1 1 
ATOM   1822  C CD2 . PHE A 1 232 ? 26.742  15.347  61.918  1.00 27.18  ? 228 PHE A CD2 1 
ATOM   1823  C CE1 . PHE A 1 232 ? 26.367  18.036  62.418  1.00 28.61  ? 228 PHE A CE1 1 
ATOM   1824  C CE2 . PHE A 1 232 ? 26.946  15.846  63.195  1.00 29.24  ? 228 PHE A CE2 1 
ATOM   1825  C CZ  . PHE A 1 232 ? 26.759  17.193  63.445  1.00 28.98  ? 228 PHE A CZ  1 
ATOM   1826  N N   . PHE A 1 233 ? 27.311  13.210  57.790  1.00 22.84  ? 229 PHE A N   1 
ATOM   1827  C CA  . PHE A 1 233 ? 27.098  12.186  56.775  1.00 22.28  ? 229 PHE A CA  1 
ATOM   1828  C C   . PHE A 1 233 ? 26.240  11.075  57.362  1.00 21.30  ? 229 PHE A C   1 
ATOM   1829  O O   . PHE A 1 233 ? 26.037  11.024  58.573  1.00 21.07  ? 229 PHE A O   1 
ATOM   1830  C CB  . PHE A 1 233 ? 28.447  11.642  56.310  1.00 21.96  ? 229 PHE A CB  1 
ATOM   1831  C CG  . PHE A 1 233 ? 29.300  12.671  55.623  1.00 21.62  ? 229 PHE A CG  1 
ATOM   1832  C CD1 . PHE A 1 233 ? 30.025  13.597  56.361  1.00 21.51  ? 229 PHE A CD1 1 
ATOM   1833  C CD2 . PHE A 1 233 ? 29.368  12.724  54.239  1.00 22.82  ? 229 PHE A CD2 1 
ATOM   1834  C CE1 . PHE A 1 233 ? 30.801  14.557  55.732  1.00 21.78  ? 229 PHE A CE1 1 
ATOM   1835  C CE2 . PHE A 1 233 ? 30.150  13.678  53.600  1.00 22.10  ? 229 PHE A CE2 1 
ATOM   1836  C CZ  . PHE A 1 233 ? 30.870  14.595  54.349  1.00 21.55  ? 229 PHE A CZ  1 
ATOM   1837  N N   . TRP A 1 234 ? 25.737  10.193  56.507  1.00 21.88  ? 230 TRP A N   1 
ATOM   1838  C CA  . TRP A 1 234 ? 24.901  9.082   56.959  1.00 22.25  ? 230 TRP A CA  1 
ATOM   1839  C C   . TRP A 1 234 ? 24.968  7.891   56.042  1.00 23.87  ? 230 TRP A C   1 
ATOM   1840  O O   . TRP A 1 234 ? 25.376  8.009   54.884  1.00 23.70  ? 230 TRP A O   1 
ATOM   1841  C CB  . TRP A 1 234 ? 23.455  9.544   57.095  1.00 21.52  ? 230 TRP A CB  1 
ATOM   1842  C CG  . TRP A 1 234 ? 22.851  10.029  55.799  1.00 21.89  ? 230 TRP A CG  1 
ATOM   1843  C CD1 . TRP A 1 234 ? 22.994  11.284  55.218  1.00 23.19  ? 230 TRP A CD1 1 
ATOM   1844  C CD2 . TRP A 1 234 ? 21.991  9.278   54.871  1.00 22.21  ? 230 TRP A CD2 1 
ATOM   1845  N NE1 . TRP A 1 234 ? 22.302  11.360  54.037  1.00 24.40  ? 230 TRP A NE1 1 
ATOM   1846  C CE2 . TRP A 1 234 ? 21.680  10.193  53.771  1.00 22.78  ? 230 TRP A CE2 1 
ATOM   1847  C CE3 . TRP A 1 234 ? 21.469  7.990   54.842  1.00 21.85  ? 230 TRP A CE3 1 
ATOM   1848  C CZ2 . TRP A 1 234 ? 20.883  9.818   52.709  1.00 22.72  ? 230 TRP A CZ2 1 
ATOM   1849  C CZ3 . TRP A 1 234 ? 20.659  7.624   53.760  1.00 22.09  ? 230 TRP A CZ3 1 
ATOM   1850  C CH2 . TRP A 1 234 ? 20.378  8.519   52.721  1.00 22.29  ? 230 TRP A CH2 1 
ATOM   1851  N N   . THR A 1 235 ? 24.565  6.734   56.567  1.00 24.73  ? 231 THR A N   1 
ATOM   1852  C CA  . THR A 1 235 ? 24.300  5.534   55.753  1.00 26.06  ? 231 THR A CA  1 
ATOM   1853  C C   . THR A 1 235 ? 23.285  4.647   56.457  1.00 25.34  ? 231 THR A C   1 
ATOM   1854  O O   . THR A 1 235 ? 23.020  4.806   57.647  1.00 23.55  ? 231 THR A O   1 
ATOM   1855  C CB  . THR A 1 235 ? 25.539  4.651   55.451  1.00 27.16  ? 231 THR A CB  1 
ATOM   1856  O OG1 . THR A 1 235 ? 26.267  4.373   56.656  1.00 26.04  ? 231 THR A OG1 1 
ATOM   1857  C CG2 . THR A 1 235 ? 26.437  5.308   54.420  1.00 32.98  ? 231 THR A CG2 1 
ATOM   1858  N N   . ILE A 1 236 ? 22.734  3.709   55.701  1.00 26.56  ? 232 ILE A N   1 
ATOM   1859  C CA  . ILE A 1 236 ? 21.862  2.684   56.241  1.00 26.68  ? 232 ILE A CA  1 
ATOM   1860  C C   . ILE A 1 236 ? 22.675  1.397   56.364  1.00 26.32  ? 232 ILE A C   1 
ATOM   1861  O O   . ILE A 1 236 ? 23.130  0.842   55.363  1.00 25.90  ? 232 ILE A O   1 
ATOM   1862  C CB  . ILE A 1 236 ? 20.619  2.468   55.356  1.00 27.10  ? 232 ILE A CB  1 
ATOM   1863  C CG1 . ILE A 1 236 ? 19.494  3.417   55.770  1.00 28.69  ? 232 ILE A CG1 1 
ATOM   1864  C CG2 . ILE A 1 236 ? 20.096  1.048   55.508  1.00 29.15  ? 232 ILE A CG2 1 
ATOM   1865  C CD1 . ILE A 1 236 ? 19.881  4.876   55.844  1.00 29.36  ? 232 ILE A CD1 1 
ATOM   1866  N N   . LEU A 1 237 ? 22.870  0.944   57.599  1.00 26.55  ? 233 LEU A N   1 
ATOM   1867  C CA  . LEU A 1 237 ? 23.598  -0.290  57.867  1.00 25.50  ? 233 LEU A CA  1 
ATOM   1868  C C   . LEU A 1 237 ? 22.632  -1.475  57.783  1.00 26.90  ? 233 LEU A C   1 
ATOM   1869  O O   . LEU A 1 237 ? 21.624  -1.511  58.484  1.00 27.05  ? 233 LEU A O   1 
ATOM   1870  C CB  . LEU A 1 237 ? 24.261  -0.218  59.246  1.00 24.01  ? 233 LEU A CB  1 
ATOM   1871  C CG  . LEU A 1 237 ? 25.347  -1.247  59.581  1.00 23.95  ? 233 LEU A CG  1 
ATOM   1872  C CD1 . LEU A 1 237 ? 26.348  -1.390  58.447  1.00 24.18  ? 233 LEU A CD1 1 
ATOM   1873  C CD2 . LEU A 1 237 ? 26.066  -0.865  60.863  1.00 23.96  ? 233 LEU A CD2 1 
ATOM   1874  N N   . LYS A 1 238 ? 22.944  -2.429  56.908  1.00 30.25  ? 234 LYS A N   1 
ATOM   1875  C CA  . LYS A 1 238 ? 22.113  -3.618  56.696  1.00 30.60  ? 234 LYS A CA  1 
ATOM   1876  C C   . LYS A 1 238 ? 22.084  -4.519  57.933  1.00 32.43  ? 234 LYS A C   1 
ATOM   1877  O O   . LYS A 1 238 ? 22.965  -4.420  58.787  1.00 32.44  ? 234 LYS A O   1 
ATOM   1878  C CB  . LYS A 1 238 ? 22.624  -4.412  55.485  1.00 32.41  ? 234 LYS A CB  1 
ATOM   1879  C CG  . LYS A 1 238 ? 22.427  -3.723  54.140  1.00 33.66  ? 234 LYS A CG  1 
ATOM   1880  C CD  . LYS A 1 238 ? 20.956  -3.542  53.796  1.00 37.40  ? 234 LYS A CD  1 
ATOM   1881  C CE  . LYS A 1 238 ? 20.757  -2.711  52.536  1.00 39.91  ? 234 LYS A CE  1 
ATOM   1882  N NZ  . LYS A 1 238 ? 20.993  -3.494  51.291  1.00 40.57  ? 234 LYS A NZ  1 
ATOM   1883  N N   . PRO A 1 239 ? 21.073  -5.407  58.030  1.00 34.14  ? 235 PRO A N   1 
ATOM   1884  C CA  . PRO A 1 239 ? 20.925  -6.270  59.199  1.00 33.38  ? 235 PRO A CA  1 
ATOM   1885  C C   . PRO A 1 239 ? 22.204  -6.975  59.659  1.00 34.75  ? 235 PRO A C   1 
ATOM   1886  O O   . PRO A 1 239 ? 22.606  -6.792  60.801  1.00 37.36  ? 235 PRO A O   1 
ATOM   1887  C CB  . PRO A 1 239 ? 19.873  -7.281  58.747  1.00 34.04  ? 235 PRO A CB  1 
ATOM   1888  C CG  . PRO A 1 239 ? 19.015  -6.502  57.814  1.00 33.47  ? 235 PRO A CG  1 
ATOM   1889  C CD  . PRO A 1 239 ? 19.970  -5.613  57.071  1.00 33.95  ? 235 PRO A CD  1 
ATOM   1890  N N   . ASN A 1 240 ? 22.849  -7.751  58.793  1.00 35.24  ? 236 ASN A N   1 
ATOM   1891  C CA  . ASN A 1 240 ? 24.003  -8.559  59.222  1.00 37.10  ? 236 ASN A CA  1 
ATOM   1892  C C   . ASN A 1 240 ? 25.362  -7.885  58.980  1.00 34.67  ? 236 ASN A C   1 
ATOM   1893  O O   . ASN A 1 240 ? 26.408  -8.533  59.051  1.00 32.26  ? 236 ASN A O   1 
ATOM   1894  C CB  . ASN A 1 240 ? 23.959  -9.935  58.538  1.00 42.11  ? 236 ASN A CB  1 
ATOM   1895  C CG  . ASN A 1 240 ? 24.675  -11.012 59.334  1.00 46.33  ? 236 ASN A CG  1 
ATOM   1896  O OD1 . ASN A 1 240 ? 24.496  -11.132 60.547  1.00 49.44  ? 236 ASN A OD1 1 
ATOM   1897  N ND2 . ASN A 1 240 ? 25.488  -11.809 58.649  1.00 50.05  ? 236 ASN A ND2 1 
ATOM   1898  N N   . ASP A 1 241 ? 25.343  -6.578  58.723  1.00 35.81  ? 237 ASP A N   1 
ATOM   1899  C CA  . ASP A 1 241 ? 26.534  -5.833  58.309  1.00 31.34  ? 237 ASP A CA  1 
ATOM   1900  C C   . ASP A 1 241 ? 27.113  -5.035  59.477  1.00 30.41  ? 237 ASP A C   1 
ATOM   1901  O O   . ASP A 1 241 ? 26.450  -4.856  60.501  1.00 32.47  ? 237 ASP A O   1 
ATOM   1902  C CB  . ASP A 1 241 ? 26.163  -4.897  57.154  1.00 30.90  ? 237 ASP A CB  1 
ATOM   1903  C CG  . ASP A 1 241 ? 27.375  -4.321  56.442  1.00 31.39  ? 237 ASP A CG  1 
ATOM   1904  O OD1 . ASP A 1 241 ? 28.487  -4.866  56.588  1.00 31.78  ? 237 ASP A OD1 1 
ATOM   1905  O OD2 . ASP A 1 241 ? 27.216  -3.308  55.733  1.00 30.72  ? 237 ASP A OD2 1 
ATOM   1906  N N   . ALA A 1 242 ? 28.356  -4.580  59.325  1.00 28.64  ? 238 ALA A N   1 
ATOM   1907  C CA  . ALA A 1 242 ? 29.030  -3.769  60.339  1.00 26.92  ? 238 ALA A CA  1 
ATOM   1908  C C   . ALA A 1 242 ? 29.630  -2.495  59.741  1.00 26.28  ? 238 ALA A C   1 
ATOM   1909  O O   . ALA A 1 242 ? 29.944  -2.446  58.552  1.00 25.81  ? 238 ALA A O   1 
ATOM   1910  C CB  . ALA A 1 242 ? 30.110  -4.586  61.027  1.00 25.33  ? 238 ALA A CB  1 
ATOM   1911  N N   . ILE A 1 243 ? 29.776  -1.471  60.581  1.00 25.42  ? 239 ILE A N   1 
ATOM   1912  C CA  . ILE A 1 243 ? 30.360  -0.186  60.189  1.00 24.19  ? 239 ILE A CA  1 
ATOM   1913  C C   . ILE A 1 243 ? 31.665  0.018   60.952  1.00 25.34  ? 239 ILE A C   1 
ATOM   1914  O O   . ILE A 1 243 ? 31.733  -0.287  62.141  1.00 25.69  ? 239 ILE A O   1 
ATOM   1915  C CB  . ILE A 1 243 ? 29.391  0.991   60.463  1.00 23.70  ? 239 ILE A CB  1 
ATOM   1916  C CG1 . ILE A 1 243 ? 29.932  2.297   59.865  1.00 23.62  ? 239 ILE A CG1 1 
ATOM   1917  C CG2 . ILE A 1 243 ? 29.133  1.165   61.957  1.00 24.37  ? 239 ILE A CG2 1 
ATOM   1918  C CD1 . ILE A 1 243 ? 28.903  3.399   59.755  1.00 22.28  ? 239 ILE A CD1 1 
ATOM   1919  N N   . HIS A 1 244 ? 32.697  0.522   60.274  1.00 26.13  ? 240 HIS A N   1 
ATOM   1920  C CA  . HIS A 1 244 ? 34.026  0.662   60.880  1.00 27.88  ? 240 HIS A CA  1 
ATOM   1921  C C   . HIS A 1 244 ? 34.548  2.063   60.779  1.00 25.86  ? 240 HIS A C   1 
ATOM   1922  O O   . HIS A 1 244 ? 34.780  2.564   59.684  1.00 25.50  ? 240 HIS A O   1 
ATOM   1923  C CB  . HIS A 1 244 ? 35.013  -0.294  60.219  1.00 31.41  ? 240 HIS A CB  1 
ATOM   1924  C CG  . HIS A 1 244 ? 34.533  -1.723  60.172  1.00 35.69  ? 240 HIS A CG  1 
ATOM   1925  N ND1 . HIS A 1 244 ? 34.710  -2.581  61.194  1.00 35.83  ? 240 HIS A ND1 1 
ATOM   1926  C CD2 . HIS A 1 244 ? 33.848  -2.427  59.177  1.00 37.76  ? 240 HIS A CD2 1 
ATOM   1927  C CE1 . HIS A 1 244 ? 34.174  -3.774  60.872  1.00 37.64  ? 240 HIS A CE1 1 
ATOM   1928  N NE2 . HIS A 1 244 ? 33.647  -3.677  59.637  1.00 38.44  ? 240 HIS A NE2 1 
ATOM   1929  N N   . PHE A 1 245 ? 34.752  2.702   61.926  1.00 24.94  ? 241 PHE A N   1 
ATOM   1930  C CA  . PHE A 1 245 ? 35.334  4.038   61.975  1.00 25.80  ? 241 PHE A CA  1 
ATOM   1931  C C   . PHE A 1 245 ? 36.821  3.964   62.289  1.00 27.68  ? 241 PHE A C   1 
ATOM   1932  O O   . PHE A 1 245 ? 37.257  3.127   63.086  1.00 26.26  ? 241 PHE A O   1 
ATOM   1933  C CB  . PHE A 1 245 ? 34.646  4.892   63.038  1.00 26.75  ? 241 PHE A CB  1 
ATOM   1934  C CG  . PHE A 1 245 ? 33.194  5.142   62.766  1.00 26.82  ? 241 PHE A CG  1 
ATOM   1935  C CD1 . PHE A 1 245 ? 32.220  4.322   63.318  1.00 25.86  ? 241 PHE A CD1 1 
ATOM   1936  C CD2 . PHE A 1 245 ? 32.802  6.193   61.953  1.00 25.79  ? 241 PHE A CD2 1 
ATOM   1937  C CE1 . PHE A 1 245 ? 30.882  4.547   63.066  1.00 25.92  ? 241 PHE A CE1 1 
ATOM   1938  C CE2 . PHE A 1 245 ? 31.465  6.420   61.693  1.00 25.75  ? 241 PHE A CE2 1 
ATOM   1939  C CZ  . PHE A 1 245 ? 30.502  5.598   62.251  1.00 27.26  ? 241 PHE A CZ  1 
ATOM   1940  N N   . GLU A 1 246 ? 37.591  4.843   61.651  1.00 28.17  ? 242 GLU A N   1 
ATOM   1941  C CA  . GLU A 1 246 ? 38.995  5.028   61.980  1.00 29.96  ? 242 GLU A CA  1 
ATOM   1942  C C   . GLU A 1 246 ? 39.317  6.507   61.850  1.00 29.45  ? 242 GLU A C   1 
ATOM   1943  O O   . GLU A 1 246 ? 39.177  7.083   60.771  1.00 27.29  ? 242 GLU A O   1 
ATOM   1944  C CB  . GLU A 1 246 ? 39.884  4.189   61.062  1.00 33.81  ? 242 GLU A CB  1 
ATOM   1945  C CG  . GLU A 1 246 ? 41.353  4.167   61.464  1.00 40.44  ? 242 GLU A CG  1 
ATOM   1946  C CD  . GLU A 1 246 ? 42.177  3.136   60.703  1.00 44.94  ? 242 GLU A CD  1 
ATOM   1947  O OE1 . GLU A 1 246 ? 43.418  3.268   60.688  1.00 39.88  ? 242 GLU A OE1 1 
ATOM   1948  O OE2 . GLU A 1 246 ? 41.595  2.193   60.120  1.00 56.70  ? 242 GLU A OE2 1 
ATOM   1949  N N   . SER A 1 247 ? 39.714  7.128   62.956  1.00 30.43  ? 243 SER A N   1 
ATOM   1950  C CA  . SER A 1 247 ? 40.009  8.557   62.956  1.00 31.00  ? 243 SER A CA  1 
ATOM   1951  C C   . SER A 1 247 ? 41.168  8.913   63.864  1.00 28.59  ? 243 SER A C   1 
ATOM   1952  O O   . SER A 1 247 ? 41.373  8.301   64.910  1.00 27.10  ? 243 SER A O   1 
ATOM   1953  C CB  . SER A 1 247 ? 38.790  9.371   63.377  1.00 34.81  ? 243 SER A CB  1 
ATOM   1954  O OG  . SER A 1 247 ? 39.098  10.752  63.367  1.00 36.43  ? 243 SER A OG  1 
ATOM   1955  N N   . ASN A 1 248 ? 41.902  9.935   63.443  1.00 31.57  ? 244 ASN A N   1 
ATOM   1956  C CA  . ASN A 1 248 ? 43.087  10.407  64.136  1.00 33.27  ? 244 ASN A CA  1 
ATOM   1957  C C   . ASN A 1 248 ? 42.868  11.788  64.734  1.00 31.12  ? 244 ASN A C   1 
ATOM   1958  O O   . ASN A 1 248 ? 43.683  12.248  65.519  1.00 36.10  ? 244 ASN A O   1 
ATOM   1959  C CB  . ASN A 1 248 ? 44.291  10.387  63.184  1.00 34.52  ? 244 ASN A CB  1 
ATOM   1960  C CG  . ASN A 1 248 ? 44.325  11.528  62.226  1.00 38.42  ? 244 ASN A CG  1 
ATOM   1961  O OD1 . ASN A 1 248 ? 43.325  12.176  61.972  1.00 38.30  ? 244 ASN A OD1 1 
ATOM   1962  N ND2 . ASN A 1 248 ? 45.503  11.762  61.657  1.00 45.13  ? 244 ASN A ND2 1 
ATOM   1963  N N   . GLY A 1 249 ? 41.791  12.463  64.341  1.00 30.64  ? 245 GLY A N   1 
ATOM   1964  C CA  . GLY A 1 249 ? 41.465  13.754  64.934  1.00 33.22  ? 245 GLY A CA  1 
ATOM   1965  C C   . GLY A 1 249 ? 40.040  14.283  64.942  1.00 34.10  ? 245 GLY A C   1 
ATOM   1966  O O   . GLY A 1 249 ? 39.415  14.306  65.986  1.00 49.51  ? 245 GLY A O   1 
ATOM   1967  N N   . ASN A 1 250 ? 39.524  14.721  63.802  1.00 31.18  ? 246 ASN A N   1 
ATOM   1968  C CA  . ASN A 1 250 ? 38.359  15.651  63.772  1.00 30.39  ? 246 ASN A CA  1 
ATOM   1969  C C   . ASN A 1 250 ? 36.957  15.030  63.735  1.00 31.40  ? 246 ASN A C   1 
ATOM   1970  O O   . ASN A 1 250 ? 36.095  15.477  62.974  1.00 32.61  ? 246 ASN A O   1 
ATOM   1971  C CB  . ASN A 1 250 ? 38.507  16.571  62.556  1.00 30.08  ? 246 ASN A CB  1 
ATOM   1972  C CG  . ASN A 1 250 ? 39.595  17.602  62.745  1.00 28.62  ? 246 ASN A CG  1 
ATOM   1973  O OD1 . ASN A 1 250 ? 40.772  17.268  62.829  1.00 27.91  ? 246 ASN A OD1 1 
ATOM   1974  N ND2 . ASN A 1 250 ? 39.200  18.868  62.826  1.00 33.94  ? 246 ASN A ND2 1 
ATOM   1975  N N   . PHE A 1 251 ? 36.719  14.037  64.583  1.00 27.49  ? 247 PHE A N   1 
ATOM   1976  C CA  . PHE A 1 251 ? 35.587  13.124  64.426  1.00 25.25  ? 247 PHE A CA  1 
ATOM   1977  C C   . PHE A 1 251 ? 34.442  13.336  65.427  1.00 27.19  ? 247 PHE A C   1 
ATOM   1978  O O   . PHE A 1 251 ? 34.642  13.328  66.642  1.00 28.29  ? 247 PHE A O   1 
ATOM   1979  C CB  . PHE A 1 251 ? 36.175  11.700  64.427  1.00 24.62  ? 247 PHE A CB  1 
ATOM   1980  C CG  . PHE A 1 251 ? 35.170  10.582  64.484  1.00 22.01  ? 247 PHE A CG  1 
ATOM   1981  C CD1 . PHE A 1 251 ? 34.110  10.545  63.607  1.00 21.32  ? 247 PHE A CD1 1 
ATOM   1982  C CD2 . PHE A 1 251 ? 35.345  9.521   65.366  1.00 20.83  ? 247 PHE A CD2 1 
ATOM   1983  C CE1 . PHE A 1 251 ? 33.210  9.500   63.638  1.00 20.74  ? 247 PHE A CE1 1 
ATOM   1984  C CE2 . PHE A 1 251 ? 34.445  8.471   65.405  1.00 19.99  ? 247 PHE A CE2 1 
ATOM   1985  C CZ  . PHE A 1 251 ? 33.376  8.461   64.533  1.00 20.02  ? 247 PHE A CZ  1 
ATOM   1986  N N   . ILE A 1 252 ? 33.241  13.560  64.888  1.00 28.91  ? 248 ILE A N   1 
ATOM   1987  C CA  . ILE A 1 252 ? 32.026  13.677  65.680  1.00 27.92  ? 248 ILE A CA  1 
ATOM   1988  C C   . ILE A 1 252 ? 31.399  12.296  65.635  1.00 29.18  ? 248 ILE A C   1 
ATOM   1989  O O   . ILE A 1 252 ? 30.743  11.934  64.649  1.00 29.69  ? 248 ILE A O   1 
ATOM   1990  C CB  . ILE A 1 252 ? 31.044  14.729  65.117  1.00 28.19  ? 248 ILE A CB  1 
ATOM   1991  C CG1 . ILE A 1 252 ? 31.501  16.144  65.475  1.00 28.74  ? 248 ILE A CG1 1 
ATOM   1992  C CG2 . ILE A 1 252 ? 29.649  14.534  65.705  1.00 27.14  ? 248 ILE A CG2 1 
ATOM   1993  C CD1 . ILE A 1 252 ? 32.820  16.552  64.867  1.00 26.71  ? 248 ILE A CD1 1 
ATOM   1994  N N   . ALA A 1 253 ? 31.632  11.521  66.690  1.00 26.82  ? 249 ALA A N   1 
ATOM   1995  C CA  . ALA A 1 253 ? 31.225  10.122  66.710  1.00 26.53  ? 249 ALA A CA  1 
ATOM   1996  C C   . ALA A 1 253 ? 29.739  9.976   67.000  1.00 28.21  ? 249 ALA A C   1 
ATOM   1997  O O   . ALA A 1 253 ? 29.167  10.783  67.731  1.00 28.90  ? 249 ALA A O   1 
ATOM   1998  C CB  . ALA A 1 253 ? 32.030  9.346   67.738  1.00 24.39  ? 249 ALA A CB  1 
ATOM   1999  N N   . PRO A 1 254 ? 29.110  8.935   66.429  1.00 26.65  ? 250 PRO A N   1 
ATOM   2000  C CA  . PRO A 1 254 ? 27.748  8.613   66.817  1.00 25.74  ? 250 PRO A CA  1 
ATOM   2001  C C   . PRO A 1 254 ? 27.698  8.051   68.235  1.00 26.05  ? 250 PRO A C   1 
ATOM   2002  O O   . PRO A 1 254 ? 28.587  7.304   68.623  1.00 24.77  ? 250 PRO A O   1 
ATOM   2003  C CB  . PRO A 1 254 ? 27.349  7.524   65.821  1.00 24.58  ? 250 PRO A CB  1 
ATOM   2004  C CG  . PRO A 1 254 ? 28.626  6.880   65.431  1.00 25.11  ? 250 PRO A CG  1 
ATOM   2005  C CD  . PRO A 1 254 ? 29.652  7.969   65.456  1.00 25.86  ? 250 PRO A CD  1 
ATOM   2006  N N   . GLU A 1 255 ? 26.678  8.429   68.998  1.00 29.87  ? 251 GLU A N   1 
ATOM   2007  C CA  . GLU A 1 255 ? 26.312  7.710   70.222  1.00 31.13  ? 251 GLU A CA  1 
ATOM   2008  C C   . GLU A 1 255 ? 25.073  6.849   69.953  1.00 30.16  ? 251 GLU A C   1 
ATOM   2009  O O   . GLU A 1 255 ? 25.019  5.676   70.341  1.00 27.78  ? 251 GLU A O   1 
ATOM   2010  C CB  . GLU A 1 255 ? 26.040  8.684   71.368  1.00 34.05  ? 251 GLU A CB  1 
ATOM   2011  C CG  . GLU A 1 255 ? 25.898  8.007   72.728  1.00 37.09  ? 251 GLU A CG  1 
ATOM   2012  C CD  . GLU A 1 255 ? 25.625  8.977   73.865  1.00 40.92  ? 251 GLU A CD  1 
ATOM   2013  O OE1 . GLU A 1 255 ? 25.615  10.205  73.629  1.00 46.20  ? 251 GLU A OE1 1 
ATOM   2014  O OE2 . GLU A 1 255 ? 25.418  8.508   75.005  1.00 44.10  ? 251 GLU A OE2 1 
ATOM   2015  N N   . TYR A 1 256 ? 24.091  7.441   69.274  1.00 31.35  ? 252 TYR A N   1 
ATOM   2016  C CA  . TYR A 1 256 ? 22.839  6.766   68.953  1.00 33.80  ? 252 TYR A CA  1 
ATOM   2017  C C   . TYR A 1 256 ? 22.655  6.565   67.450  1.00 35.21  ? 252 TYR A C   1 
ATOM   2018  O O   . TYR A 1 256 ? 22.989  7.444   66.652  1.00 39.16  ? 252 TYR A O   1 
ATOM   2019  C CB  . TYR A 1 256 ? 21.661  7.578   69.487  1.00 33.36  ? 252 TYR A CB  1 
ATOM   2020  C CG  . TYR A 1 256 ? 21.660  7.718   70.987  1.00 37.31  ? 252 TYR A CG  1 
ATOM   2021  C CD1 . TYR A 1 256 ? 22.262  8.808   71.602  1.00 39.03  ? 252 TYR A CD1 1 
ATOM   2022  C CD2 . TYR A 1 256 ? 21.061  6.756   71.793  1.00 37.12  ? 252 TYR A CD2 1 
ATOM   2023  C CE1 . TYR A 1 256 ? 22.264  8.941   72.980  1.00 41.60  ? 252 TYR A CE1 1 
ATOM   2024  C CE2 . TYR A 1 256 ? 21.056  6.881   73.170  1.00 37.32  ? 252 TYR A CE2 1 
ATOM   2025  C CZ  . TYR A 1 256 ? 21.658  7.974   73.759  1.00 40.24  ? 252 TYR A CZ  1 
ATOM   2026  O OH  . TYR A 1 256 ? 21.662  8.099   75.130  1.00 45.79  ? 252 TYR A OH  1 
ATOM   2027  N N   . ALA A 1 257 ? 22.122  5.401   67.083  1.00 33.42  ? 253 ALA A N   1 
ATOM   2028  C CA  . ALA A 1 257 ? 21.669  5.118   65.720  1.00 30.88  ? 253 ALA A CA  1 
ATOM   2029  C C   . ALA A 1 257 ? 20.150  4.908   65.747  1.00 29.63  ? 253 ALA A C   1 
ATOM   2030  O O   . ALA A 1 257 ? 19.523  5.072   66.793  1.00 27.07  ? 253 ALA A O   1 
ATOM   2031  C CB  . ALA A 1 257 ? 22.376  3.887   65.176  1.00 29.52  ? 253 ALA A CB  1 
ATOM   2032  N N   . TYR A 1 258 ? 19.559  4.561   64.607  1.00 32.06  ? 254 TYR A N   1 
ATOM   2033  C CA  . TYR A 1 258 ? 18.104  4.456   64.503  1.00 34.74  ? 254 TYR A CA  1 
ATOM   2034  C C   . TYR A 1 258 ? 17.652  3.209   63.753  1.00 34.16  ? 254 TYR A C   1 
ATOM   2035  O O   . TYR A 1 258 ? 17.936  3.070   62.560  1.00 32.04  ? 254 TYR A O   1 
ATOM   2036  C CB  . TYR A 1 258 ? 17.546  5.674   63.775  1.00 37.88  ? 254 TYR A CB  1 
ATOM   2037  C CG  . TYR A 1 258 ? 17.677  6.979   64.515  1.00 40.72  ? 254 TYR A CG  1 
ATOM   2038  C CD1 . TYR A 1 258 ? 18.730  7.853   64.249  1.00 42.26  ? 254 TYR A CD1 1 
ATOM   2039  C CD2 . TYR A 1 258 ? 16.732  7.356   65.462  1.00 39.97  ? 254 TYR A CD2 1 
ATOM   2040  C CE1 . TYR A 1 258 ? 18.841  9.062   64.919  1.00 46.59  ? 254 TYR A CE1 1 
ATOM   2041  C CE2 . TYR A 1 258 ? 16.830  8.562   66.135  1.00 43.59  ? 254 TYR A CE2 1 
ATOM   2042  C CZ  . TYR A 1 258 ? 17.884  9.413   65.862  1.00 47.08  ? 254 TYR A CZ  1 
ATOM   2043  O OH  . TYR A 1 258 ? 17.981  10.616  66.527  1.00 48.43  ? 254 TYR A OH  1 
ATOM   2044  N N   . LYS A 1 259 ? 16.940  2.321   64.449  1.00 32.77  ? 255 LYS A N   1 
ATOM   2045  C CA  . LYS A 1 259 ? 16.263  1.194   63.805  1.00 32.47  ? 255 LYS A CA  1 
ATOM   2046  C C   . LYS A 1 259 ? 15.222  1.738   62.837  1.00 31.65  ? 255 LYS A C   1 
ATOM   2047  O O   . LYS A 1 259 ? 14.441  2.613   63.204  1.00 32.54  ? 255 LYS A O   1 
ATOM   2048  C CB  . LYS A 1 259 ? 15.573  0.294   64.836  1.00 34.60  ? 255 LYS A CB  1 
ATOM   2049  C CG  . LYS A 1 259 ? 16.502  -0.689  65.546  1.00 36.92  ? 255 LYS A CG  1 
ATOM   2050  C CD  . LYS A 1 259 ? 15.780  -1.881  66.187  1.00 39.24  ? 255 LYS A CD  1 
ATOM   2051  C CE  . LYS A 1 259 ? 15.540  -1.654  67.657  1.00 40.75  ? 255 LYS A CE  1 
ATOM   2052  N NZ  . LYS A 1 259 ? 15.009  -2.862  68.347  1.00 37.00  ? 255 LYS A NZ  1 
ATOM   2053  N N   . ILE A 1 260 ? 15.213  1.223   61.610  1.00 32.56  ? 256 ILE A N   1 
ATOM   2054  C CA  . ILE A 1 260 ? 14.315  1.712   60.564  1.00 34.36  ? 256 ILE A CA  1 
ATOM   2055  C C   . ILE A 1 260 ? 13.668  0.578   59.777  1.00 32.54  ? 256 ILE A C   1 
ATOM   2056  O O   . ILE A 1 260 ? 14.342  -0.362  59.358  1.00 33.63  ? 256 ILE A O   1 
ATOM   2057  C CB  . ILE A 1 260 ? 15.065  2.630   59.574  1.00 39.95  ? 256 ILE A CB  1 
ATOM   2058  C CG1 . ILE A 1 260 ? 15.062  4.073   60.078  1.00 42.73  ? 256 ILE A CG1 1 
ATOM   2059  C CG2 . ILE A 1 260 ? 14.437  2.573   58.185  1.00 39.41  ? 256 ILE A CG2 1 
ATOM   2060  C CD1 . ILE A 1 260 ? 15.684  5.054   59.106  1.00 46.76  ? 256 ILE A CD1 1 
ATOM   2061  N N   . VAL A 1 261 ? 12.355  0.676   59.588  1.00 31.38  ? 257 VAL A N   1 
ATOM   2062  C CA  . VAL A 1 261 ? 11.640  -0.157  58.628  1.00 29.13  ? 257 VAL A CA  1 
ATOM   2063  C C   . VAL A 1 261 ? 10.844  0.750   57.700  1.00 31.21  ? 257 VAL A C   1 
ATOM   2064  O O   . VAL A 1 261 ? 10.049  1.570   58.165  1.00 31.49  ? 257 VAL A O   1 
ATOM   2065  C CB  . VAL A 1 261 ? 10.677  -1.136  59.313  1.00 28.04  ? 257 VAL A CB  1 
ATOM   2066  C CG1 . VAL A 1 261 ? 10.042  -2.055  58.277  1.00 29.19  ? 257 VAL A CG1 1 
ATOM   2067  C CG2 . VAL A 1 261 ? 11.405  -1.949  60.367  1.00 25.56  ? 257 VAL A CG2 1 
ATOM   2068  N N   . LYS A 1 262 ? 11.067  0.601   56.396  1.00 31.27  ? 258 LYS A N   1 
ATOM   2069  C CA  . LYS A 1 262 ? 10.369  1.385   55.386  1.00 31.48  ? 258 LYS A CA  1 
ATOM   2070  C C   . LYS A 1 262 ? 9.523   0.473   54.507  1.00 32.58  ? 258 LYS A C   1 
ATOM   2071  O O   . LYS A 1 262 ? 10.011  -0.546  54.013  1.00 29.80  ? 258 LYS A O   1 
ATOM   2072  C CB  . LYS A 1 262 ? 11.366  2.159   54.521  1.00 34.95  ? 258 LYS A CB  1 
ATOM   2073  C CG  . LYS A 1 262 ? 10.708  3.111   53.531  1.00 37.30  ? 258 LYS A CG  1 
ATOM   2074  C CD  . LYS A 1 262 ? 11.642  4.239   53.127  1.00 39.97  ? 258 LYS A CD  1 
ATOM   2075  C CE  . LYS A 1 262 ? 11.031  5.110   52.038  1.00 39.97  ? 258 LYS A CE  1 
ATOM   2076  N NZ  . LYS A 1 262 ? 9.977   6.022   52.572  1.00 40.50  ? 258 LYS A NZ  1 
ATOM   2077  N N   . LYS A 1 263 ? 8.255   0.849   54.324  1.00 36.39  ? 259 LYS A N   1 
ATOM   2078  C CA  . LYS A 1 263 ? 7.296   0.071   53.533  1.00 38.63  ? 259 LYS A CA  1 
ATOM   2079  C C   . LYS A 1 263 ? 6.814   0.841   52.303  1.00 41.79  ? 259 LYS A C   1 
ATOM   2080  O O   . LYS A 1 263 ? 6.660   0.262   51.229  1.00 46.45  ? 259 LYS A O   1 
ATOM   2081  C CB  . LYS A 1 263 ? 6.093   -0.313  54.397  1.00 43.53  ? 259 LYS A CB  1 
ATOM   2082  C CG  . LYS A 1 263 ? 6.416   -1.224  55.576  1.00 49.58  ? 259 LYS A CG  1 
ATOM   2083  C CD  . LYS A 1 263 ? 6.360   -2.719  55.200  1.00 56.69  ? 259 LYS A CD  1 
ATOM   2084  C CE  . LYS A 1 263 ? 7.725   -3.260  54.784  1.00 63.35  ? 259 LYS A CE  1 
ATOM   2085  N NZ  . LYS A 1 263 ? 7.623   -4.572  54.084  1.00 65.68  ? 259 LYS A NZ  1 
ATOM   2086  N N   . GLY A 1 264 ? 6.561   2.139   52.470  1.00 41.20  ? 260 GLY A N   1 
ATOM   2087  C CA  . GLY A 1 264 ? 6.115   3.002   51.375  1.00 35.61  ? 260 GLY A CA  1 
ATOM   2088  C C   . GLY A 1 264 ? 6.732   4.390   51.417  1.00 34.94  ? 260 GLY A C   1 
ATOM   2089  O O   . GLY A 1 264 ? 7.597   4.673   52.245  1.00 28.78  ? 260 GLY A O   1 
ATOM   2090  N N   . ASP A 1 265 ? 6.273   5.259   50.517  1.00 37.15  ? 261 ASP A N   1 
ATOM   2091  C CA  . ASP A 1 265 ? 6.837   6.595   50.357  1.00 36.34  ? 261 ASP A CA  1 
ATOM   2092  C C   . ASP A 1 265 ? 5.817   7.710   50.547  1.00 30.69  ? 261 ASP A C   1 
ATOM   2093  O O   . ASP A 1 265 ? 4.610   7.487   50.513  1.00 33.04  ? 261 ASP A O   1 
ATOM   2094  C CB  . ASP A 1 265 ? 7.481   6.708   48.977  1.00 46.18  ? 261 ASP A CB  1 
ATOM   2095  C CG  . ASP A 1 265 ? 8.677   5.790   48.820  1.00 58.06  ? 261 ASP A CG  1 
ATOM   2096  O OD1 . ASP A 1 265 ? 9.771   6.151   49.309  1.00 64.35  ? 261 ASP A OD1 1 
ATOM   2097  O OD2 . ASP A 1 265 ? 8.525   4.713   48.203  1.00 68.89  ? 261 ASP A OD2 1 
ATOM   2098  N N   . SER A 1 266 ? 6.326   8.922   50.722  1.00 28.57  ? 262 SER A N   1 
ATOM   2099  C CA  . SER A 1 266 ? 5.493   10.097  50.961  1.00 29.58  ? 262 SER A CA  1 
ATOM   2100  C C   . SER A 1 266 ? 6.374   11.325  50.714  1.00 28.97  ? 262 SER A C   1 
ATOM   2101  O O   . SER A 1 266 ? 7.285   11.265  49.887  1.00 31.50  ? 262 SER A O   1 
ATOM   2102  C CB  . SER A 1 266 ? 4.888   10.047  52.378  1.00 29.51  ? 262 SER A CB  1 
ATOM   2103  O OG  . SER A 1 266 ? 5.280   11.136  53.193  1.00 34.98  ? 262 SER A OG  1 
ATOM   2104  N N   . THR A 1 267 ? 6.102   12.435  51.393  1.00 28.84  ? 263 THR A N   1 
ATOM   2105  C CA  . THR A 1 267 ? 6.937   13.629  51.261  1.00 30.41  ? 263 THR A CA  1 
ATOM   2106  C C   . THR A 1 267 ? 6.891   14.483  52.530  1.00 29.35  ? 263 THR A C   1 
ATOM   2107  O O   . THR A 1 267 ? 6.256   14.113  53.519  1.00 30.41  ? 263 THR A O   1 
ATOM   2108  C CB  . THR A 1 267 ? 6.518   14.467  50.030  1.00 32.71  ? 263 THR A CB  1 
ATOM   2109  O OG1 . THR A 1 267 ? 7.556   15.394  49.691  1.00 31.57  ? 263 THR A OG1 1 
ATOM   2110  C CG2 . THR A 1 267 ? 5.225   15.229  50.301  1.00 35.94  ? 263 THR A CG2 1 
ATOM   2111  N N   . ILE A 1 268 ? 7.593   15.612  52.497  1.00 29.51  ? 264 ILE A N   1 
ATOM   2112  C CA  . ILE A 1 268 ? 7.603   16.561  53.607  1.00 28.74  ? 264 ILE A CA  1 
ATOM   2113  C C   . ILE A 1 268 ? 6.646   17.692  53.267  1.00 30.00  ? 264 ILE A C   1 
ATOM   2114  O O   . ILE A 1 268 ? 6.760   18.303  52.199  1.00 33.92  ? 264 ILE A O   1 
ATOM   2115  C CB  . ILE A 1 268 ? 9.010   17.145  53.847  1.00 29.42  ? 264 ILE A CB  1 
ATOM   2116  C CG1 . ILE A 1 268 ? 9.966   16.053  54.327  1.00 31.97  ? 264 ILE A CG1 1 
ATOM   2117  C CG2 . ILE A 1 268 ? 8.970   18.272  54.869  1.00 28.79  ? 264 ILE A CG2 1 
ATOM   2118  C CD1 . ILE A 1 268 ? 10.450  15.151  53.212  1.00 35.30  ? 264 ILE A CD1 1 
ATOM   2119  N N   . MET A 1 269 ? 5.704   17.961  54.165  1.00 25.50  ? 265 MET A N   1 
ATOM   2120  C CA  . MET A 1 269 ? 4.750   19.033  53.966  1.00 24.39  ? 265 MET A CA  1 
ATOM   2121  C C   . MET A 1 269 ? 5.200   20.270  54.727  1.00 23.43  ? 265 MET A C   1 
ATOM   2122  O O   . MET A 1 269 ? 5.641   20.177  55.870  1.00 21.02  ? 265 MET A O   1 
ATOM   2123  C CB  . MET A 1 269 ? 3.359   18.607  54.429  1.00 25.27  ? 265 MET A CB  1 
ATOM   2124  C CG  . MET A 1 269 ? 2.258   19.538  53.959  1.00 27.82  ? 265 MET A CG  1 
ATOM   2125  S SD  . MET A 1 269 ? 0.629   18.791  54.065  1.00 35.12  ? 265 MET A SD  1 
ATOM   2126  C CE  . MET A 1 269 ? 0.397   18.844  55.838  1.00 32.97  ? 265 MET A CE  1 
ATOM   2127  N N   . LYS A 1 270 ? 5.084   21.425  54.079  1.00 25.37  ? 266 LYS A N   1 
ATOM   2128  C CA  . LYS A 1 270 ? 5.401   22.707  54.689  1.00 27.96  ? 266 LYS A CA  1 
ATOM   2129  C C   . LYS A 1 270 ? 4.105   23.393  55.116  1.00 28.68  ? 266 LYS A C   1 
ATOM   2130  O O   . LYS A 1 270 ? 3.333   23.828  54.269  1.00 27.99  ? 266 LYS A O   1 
ATOM   2131  C CB  . LYS A 1 270 ? 6.152   23.589  53.686  1.00 31.06  ? 266 LYS A CB  1 
ATOM   2132  C CG  . LYS A 1 270 ? 7.508   23.050  53.247  1.00 34.44  ? 266 LYS A CG  1 
ATOM   2133  C CD  . LYS A 1 270 ? 8.558   23.229  54.335  1.00 40.57  ? 266 LYS A CD  1 
ATOM   2134  C CE  . LYS A 1 270 ? 9.963   22.915  53.844  1.00 43.76  ? 266 LYS A CE  1 
ATOM   2135  N NZ  . LYS A 1 270 ? 10.979  23.293  54.874  1.00 44.08  ? 266 LYS A NZ  1 
ATOM   2136  N N   . SER A 1 271 ? 3.857   23.492  56.421  1.00 31.75  ? 267 SER A N   1 
ATOM   2137  C CA  . SER A 1 271 ? 2.650   24.183  56.905  1.00 33.02  ? 267 SER A CA  1 
ATOM   2138  C C   . SER A 1 271 ? 2.740   24.580  58.387  1.00 35.39  ? 267 SER A C   1 
ATOM   2139  O O   . SER A 1 271 ? 3.427   23.934  59.196  1.00 35.44  ? 267 SER A O   1 
ATOM   2140  C CB  . SER A 1 271 ? 1.363   23.371  56.599  1.00 33.95  ? 267 SER A CB  1 
ATOM   2141  O OG  . SER A 1 271 ? 0.935   22.577  57.690  1.00 36.65  ? 267 SER A OG  1 
ATOM   2142  N N   . GLU A 1 272 ? 2.060   25.678  58.710  1.00 39.21  ? 268 GLU A N   1 
ATOM   2143  C CA  . GLU A 1 272 ? 1.939   26.169  60.080  1.00 44.59  ? 268 GLU A CA  1 
ATOM   2144  C C   . GLU A 1 272 ? 0.598   25.755  60.692  1.00 40.22  ? 268 GLU A C   1 
ATOM   2145  O O   . GLU A 1 272 ? 0.356   25.998  61.876  1.00 37.64  ? 268 GLU A O   1 
ATOM   2146  C CB  . GLU A 1 272 ? 2.081   27.704  60.121  1.00 53.62  ? 268 GLU A CB  1 
ATOM   2147  C CG  . GLU A 1 272 ? 3.500   28.255  60.130  1.00 63.33  ? 268 GLU A CG  1 
ATOM   2148  C CD  . GLU A 1 272 ? 3.530   29.756  60.335  1.00 71.61  ? 268 GLU A CD  1 
ATOM   2149  O OE1 . GLU A 1 272 ? 2.462   30.385  60.524  1.00 75.80  ? 268 GLU A OE1 1 
ATOM   2150  O OE2 . GLU A 1 272 ? 4.641   30.306  60.320  1.00 72.02  ? 268 GLU A OE2 1 
ATOM   2151  N N   . VAL A 1 273 ? -0.267  25.133  59.889  1.00 36.68  ? 269 VAL A N   1 
ATOM   2152  C CA  . VAL A 1 273 ? -1.611  24.760  60.342  1.00 33.04  ? 269 VAL A CA  1 
ATOM   2153  C C   . VAL A 1 273 ? -1.548  23.712  61.452  1.00 31.07  ? 269 VAL A C   1 
ATOM   2154  O O   . VAL A 1 273 ? -0.708  22.818  61.429  1.00 31.41  ? 269 VAL A O   1 
ATOM   2155  C CB  . VAL A 1 273 ? -2.483  24.264  59.168  1.00 31.89  ? 269 VAL A CB  1 
ATOM   2156  C CG1 . VAL A 1 273 ? -3.709  23.522  59.672  1.00 30.85  ? 269 VAL A CG1 1 
ATOM   2157  C CG2 . VAL A 1 273 ? -2.895  25.441  58.297  1.00 29.94  ? 269 VAL A CG2 1 
ATOM   2158  N N   . GLU A 1 274 ? -2.454  23.834  62.415  1.00 34.52  ? 270 GLU A N   1 
ATOM   2159  C CA  . GLU A 1 274 ? -2.424  23.024  63.630  1.00 35.88  ? 270 GLU A CA  1 
ATOM   2160  C C   . GLU A 1 274 ? -2.969  21.631  63.328  1.00 33.34  ? 270 GLU A C   1 
ATOM   2161  O O   . GLU A 1 274 ? -3.677  21.436  62.349  1.00 32.62  ? 270 GLU A O   1 
ATOM   2162  C CB  . GLU A 1 274 ? -3.252  23.672  64.753  1.00 40.10  ? 270 GLU A CB  1 
ATOM   2163  C CG  . GLU A 1 274 ? -3.134  25.188  64.884  1.00 43.34  ? 270 GLU A CG  1 
ATOM   2164  C CD  . GLU A 1 274 ? -2.193  25.615  65.996  1.00 44.30  ? 270 GLU A CD  1 
ATOM   2165  O OE1 . GLU A 1 274 ? -2.634  26.344  66.914  1.00 46.19  ? 270 GLU A OE1 1 
ATOM   2166  O OE2 . GLU A 1 274 ? -1.012  25.214  65.950  1.00 43.59  ? 270 GLU A OE2 1 
ATOM   2167  N N   . TYR A 1 275 ? -2.640  20.672  64.182  1.00 32.82  ? 271 TYR A N   1 
ATOM   2168  C CA  . TYR A 1 275 ? -3.122  19.299  64.047  1.00 31.45  ? 271 TYR A CA  1 
ATOM   2169  C C   . TYR A 1 275 ? -4.456  19.116  64.769  1.00 32.31  ? 271 TYR A C   1 
ATOM   2170  O O   . TYR A 1 275 ? -4.558  19.356  65.969  1.00 30.22  ? 271 TYR A O   1 
ATOM   2171  C CB  . TYR A 1 275 ? -2.074  18.333  64.610  1.00 30.33  ? 271 TYR A CB  1 
ATOM   2172  C CG  . TYR A 1 275 ? -2.520  16.891  64.736  1.00 30.68  ? 271 TYR A CG  1 
ATOM   2173  C CD1 . TYR A 1 275 ? -2.552  16.051  63.630  1.00 30.78  ? 271 TYR A CD1 1 
ATOM   2174  C CD2 . TYR A 1 275 ? -2.891  16.364  65.969  1.00 32.31  ? 271 TYR A CD2 1 
ATOM   2175  C CE1 . TYR A 1 275 ? -2.951  14.728  63.745  1.00 31.63  ? 271 TYR A CE1 1 
ATOM   2176  C CE2 . TYR A 1 275 ? -3.296  15.045  66.094  1.00 32.46  ? 271 TYR A CE2 1 
ATOM   2177  C CZ  . TYR A 1 275 ? -3.325  14.230  64.980  1.00 32.41  ? 271 TYR A CZ  1 
ATOM   2178  O OH  . TYR A 1 275 ? -3.724  12.918  65.100  1.00 33.49  ? 271 TYR A OH  1 
ATOM   2179  N N   . GLY A 1 276 ? -5.476  18.703  64.024  1.00 37.43  ? 272 GLY A N   1 
ATOM   2180  C CA  . GLY A 1 276 ? -6.760  18.302  64.600  1.00 38.77  ? 272 GLY A CA  1 
ATOM   2181  C C   . GLY A 1 276 ? -6.798  16.787  64.671  1.00 41.61  ? 272 GLY A C   1 
ATOM   2182  O O   . GLY A 1 276 ? -6.130  16.106  63.887  1.00 54.84  ? 272 GLY A O   1 
ATOM   2183  N N   . ASN A 1 277 ? -7.571  16.247  65.603  1.00 40.97  ? 273 ASN A N   1 
ATOM   2184  C CA  . ASN A 1 277 ? -7.682  14.797  65.723  1.00 40.15  ? 273 ASN A CA  1 
ATOM   2185  C C   . ASN A 1 277 ? -8.670  14.214  64.721  1.00 35.46  ? 273 ASN A C   1 
ATOM   2186  O O   . ASN A 1 277 ? -9.796  13.861  65.068  1.00 33.46  ? 273 ASN A O   1 
ATOM   2187  C CB  . ASN A 1 277 ? -8.019  14.405  67.160  1.00 41.59  ? 273 ASN A CB  1 
ATOM   2188  C CG  . ASN A 1 277 ? -6.894  14.759  68.121  1.00 43.12  ? 273 ASN A CG  1 
ATOM   2189  O OD1 . ASN A 1 277 ? -6.433  15.899  68.151  1.00 39.57  ? 273 ASN A OD1 1 
ATOM   2190  N ND2 . ASN A 1 277 ? -6.426  13.777  68.884  1.00 47.27  ? 273 ASN A ND2 1 
ATOM   2191  N N   . CYS A 1 278 ? -8.208  14.104  63.479  1.00 33.09  ? 274 CYS A N   1 
ATOM   2192  C CA  . CYS A 1 278 ? -9.041  13.699  62.347  1.00 33.51  ? 274 CYS A CA  1 
ATOM   2193  C C   . CYS A 1 278 ? -8.318  12.667  61.491  1.00 31.98  ? 274 CYS A C   1 
ATOM   2194  O O   . CYS A 1 278 ? -7.114  12.495  61.633  1.00 29.84  ? 274 CYS A O   1 
ATOM   2195  C CB  . CYS A 1 278 ? -9.370  14.914  61.500  1.00 35.23  ? 274 CYS A CB  1 
ATOM   2196  S SG  . CYS A 1 278 ? -7.964  16.028  61.421  1.00 40.76  ? 274 CYS A SG  1 
ATOM   2197  N N   . ASN A 1 279 ? -9.049  11.992  60.605  1.00 31.42  ? 275 ASN A N   1 
ATOM   2198  C CA  . ASN A 1 279 ? -8.456  11.051  59.651  1.00 33.73  ? 275 ASN A CA  1 
ATOM   2199  C C   . ASN A 1 279 ? -8.933  11.352  58.230  1.00 33.24  ? 275 ASN A C   1 
ATOM   2200  O O   . ASN A 1 279 ? -10.120 11.600  58.014  1.00 34.45  ? 275 ASN A O   1 
ATOM   2201  C CB  . ASN A 1 279 ? -8.809  9.610   60.039  1.00 34.58  ? 275 ASN A CB  1 
ATOM   2202  C CG  . ASN A 1 279 ? -8.058  8.572   59.218  1.00 37.36  ? 275 ASN A CG  1 
ATOM   2203  O OD1 . ASN A 1 279 ? -6.938  8.807   58.756  1.00 38.76  ? 275 ASN A OD1 1 
ATOM   2204  N ND2 . ASN A 1 279 ? -8.672  7.409   59.042  1.00 38.58  ? 275 ASN A ND2 1 
ATOM   2205  N N   . THR A 1 280 ? -8.005  11.338  57.270  1.00 33.88  ? 276 THR A N   1 
ATOM   2206  C CA  . THR A 1 280 ? -8.320  11.623  55.866  1.00 34.56  ? 276 THR A CA  1 
ATOM   2207  C C   . THR A 1 280 ? -7.625  10.651  54.936  1.00 31.13  ? 276 THR A C   1 
ATOM   2208  O O   . THR A 1 280 ? -6.717  9.926   55.343  1.00 28.52  ? 276 THR A O   1 
ATOM   2209  C CB  . THR A 1 280 ? -7.835  13.031  55.422  1.00 37.64  ? 276 THR A CB  1 
ATOM   2210  O OG1 . THR A 1 280 ? -7.422  13.817  56.550  1.00 48.33  ? 276 THR A OG1 1 
ATOM   2211  C CG2 . THR A 1 280 ? -8.924  13.755  54.651  1.00 37.65  ? 276 THR A CG2 1 
ATOM   2212  N N   . ARG A 1 281 ? -8.062  10.657  53.681  1.00 33.36  ? 277 ARG A N   1 
ATOM   2213  C CA  . ARG A 1 281 ? -7.365  9.960   52.607  1.00 36.23  ? 277 ARG A CA  1 
ATOM   2214  C C   . ARG A 1 281 ? -6.550  10.954  51.783  1.00 31.33  ? 277 ARG A C   1 
ATOM   2215  O O   . ARG A 1 281 ? -5.785  10.546  50.912  1.00 30.87  ? 277 ARG A O   1 
ATOM   2216  C CB  . ARG A 1 281 ? -8.342  9.223   51.679  1.00 42.25  ? 277 ARG A CB  1 
ATOM   2217  C CG  . ARG A 1 281 ? -9.552  8.601   52.374  1.00 53.97  ? 277 ARG A CG  1 
ATOM   2218  C CD  . ARG A 1 281 ? -9.451  7.084   52.587  1.00 62.30  ? 277 ARG A CD  1 
ATOM   2219  N NE  . ARG A 1 281 ? -10.665 6.562   53.245  1.00 64.87  ? 277 ARG A NE  1 
ATOM   2220  C CZ  . ARG A 1 281 ? -10.953 6.678   54.542  1.00 66.57  ? 277 ARG A CZ  1 
ATOM   2221  N NH1 . ARG A 1 281 ? -10.119 7.298   55.369  1.00 64.94  ? 277 ARG A NH1 1 
ATOM   2222  N NH2 . ARG A 1 281 ? -12.089 6.166   55.018  1.00 66.84  ? 277 ARG A NH2 1 
ATOM   2223  N N   . CYS A 1 282 ? -6.728  12.249  52.051  1.00 27.49  ? 278 CYS A N   1 
ATOM   2224  C CA  . CYS A 1 282 ? -6.111  13.313  51.259  1.00 30.15  ? 278 CYS A CA  1 
ATOM   2225  C C   . CYS A 1 282 ? -5.844  14.564  52.096  1.00 27.38  ? 278 CYS A C   1 
ATOM   2226  O O   . CYS A 1 282 ? -6.775  15.220  52.557  1.00 28.39  ? 278 CYS A O   1 
ATOM   2227  C CB  . CYS A 1 282 ? -7.017  13.668  50.084  1.00 30.95  ? 278 CYS A CB  1 
ATOM   2228  S SG  . CYS A 1 282 ? -6.421  15.055  49.096  1.00 32.53  ? 278 CYS A SG  1 
ATOM   2229  N N   . GLN A 1 283 ? -4.565  14.879  52.284  1.00 27.78  ? 279 GLN A N   1 
ATOM   2230  C CA  . GLN A 1 283 ? -4.145  16.006  53.113  1.00 25.02  ? 279 GLN A CA  1 
ATOM   2231  C C   . GLN A 1 283 ? -3.540  17.132  52.280  1.00 25.36  ? 279 GLN A C   1 
ATOM   2232  O O   . GLN A 1 283 ? -2.781  16.895  51.341  1.00 23.33  ? 279 GLN A O   1 
ATOM   2233  C CB  . GLN A 1 283 ? -3.118  15.551  54.150  1.00 23.33  ? 279 GLN A CB  1 
ATOM   2234  C CG  . GLN A 1 283 ? -2.687  16.646  55.120  1.00 23.01  ? 279 GLN A CG  1 
ATOM   2235  C CD  . GLN A 1 283 ? -3.834  17.146  55.991  1.00 23.61  ? 279 GLN A CD  1 
ATOM   2236  O OE1 . GLN A 1 283 ? -4.491  16.359  56.668  1.00 22.90  ? 279 GLN A OE1 1 
ATOM   2237  N NE2 . GLN A 1 283 ? -4.083  18.454  55.968  1.00 22.26  ? 279 GLN A NE2 1 
ATOM   2238  N N   . THR A 1 284 ? -3.872  18.357  52.663  1.00 24.67  ? 280 THR A N   1 
ATOM   2239  C CA  . THR A 1 284 ? -3.372  19.557  52.016  1.00 23.80  ? 280 THR A CA  1 
ATOM   2240  C C   . THR A 1 284 ? -2.677  20.421  53.081  1.00 24.33  ? 280 THR A C   1 
ATOM   2241  O O   . THR A 1 284 ? -2.986  20.297  54.269  1.00 27.99  ? 280 THR A O   1 
ATOM   2242  C CB  . THR A 1 284 ? -4.547  20.292  51.329  1.00 23.68  ? 280 THR A CB  1 
ATOM   2243  O OG1 . THR A 1 284 ? -4.570  19.956  49.940  1.00 27.03  ? 280 THR A OG1 1 
ATOM   2244  C CG2 . THR A 1 284 ? -4.466  21.783  51.485  1.00 21.45  ? 280 THR A CG2 1 
ATOM   2245  N N   . PRO A 1 285 ? -1.732  21.288  52.672  1.00 23.51  ? 281 PRO A N   1 
ATOM   2246  C CA  . PRO A 1 285 ? -1.028  22.157  53.627  1.00 24.03  ? 281 PRO A CA  1 
ATOM   2247  C C   . PRO A 1 285 ? -1.919  23.165  54.366  1.00 24.04  ? 281 PRO A C   1 
ATOM   2248  O O   . PRO A 1 285 ? -1.509  23.698  55.398  1.00 28.36  ? 281 PRO A O   1 
ATOM   2249  C CB  . PRO A 1 285 ? -0.018  22.903  52.743  1.00 24.18  ? 281 PRO A CB  1 
ATOM   2250  C CG  . PRO A 1 285 ? 0.160   22.036  51.545  1.00 23.22  ? 281 PRO A CG  1 
ATOM   2251  C CD  . PRO A 1 285 ? -1.191  21.437  51.310  1.00 23.97  ? 281 PRO A CD  1 
ATOM   2252  N N   . ILE A 1 286 ? -3.108  23.428  53.831  1.00 24.10  ? 282 ILE A N   1 
ATOM   2253  C CA  . ILE A 1 286 ? -4.095  24.311  54.467  1.00 24.50  ? 282 ILE A CA  1 
ATOM   2254  C C   . ILE A 1 286 ? -5.309  23.572  55.061  1.00 23.34  ? 282 ILE A C   1 
ATOM   2255  O O   . ILE A 1 286 ? -6.154  24.198  55.692  1.00 23.92  ? 282 ILE A O   1 
ATOM   2256  C CB  . ILE A 1 286 ? -4.578  25.428  53.500  1.00 25.00  ? 282 ILE A CB  1 
ATOM   2257  C CG1 . ILE A 1 286 ? -5.302  24.861  52.272  1.00 24.81  ? 282 ILE A CG1 1 
ATOM   2258  C CG2 . ILE A 1 286 ? -3.396  26.265  53.026  1.00 25.86  ? 282 ILE A CG2 1 
ATOM   2259  C CD1 . ILE A 1 286 ? -6.015  25.913  51.446  1.00 23.91  ? 282 ILE A CD1 1 
ATOM   2260  N N   . GLY A 1 287 ? -5.390  22.254  54.876  1.00 23.12  ? 283 GLY A N   1 
ATOM   2261  C CA  . GLY A 1 287 ? -6.481  21.458  55.455  1.00 23.72  ? 283 GLY A CA  1 
ATOM   2262  C C   . GLY A 1 287 ? -6.719  20.133  54.747  1.00 24.50  ? 283 GLY A C   1 
ATOM   2263  O O   . GLY A 1 287 ? -6.265  19.934  53.625  1.00 23.43  ? 283 GLY A O   1 
ATOM   2264  N N   . ALA A 1 288 ? -7.439  19.226  55.403  1.00 25.01  ? 284 ALA A N   1 
ATOM   2265  C CA  . ALA A 1 288 ? -7.719  17.898  54.848  1.00 27.30  ? 284 ALA A CA  1 
ATOM   2266  C C   . ALA A 1 288 ? -8.977  17.901  53.976  1.00 29.61  ? 284 ALA A C   1 
ATOM   2267  O O   . ALA A 1 288 ? -9.826  18.783  54.111  1.00 29.62  ? 284 ALA A O   1 
ATOM   2268  C CB  . ALA A 1 288 ? -7.858  16.883  55.970  1.00 28.04  ? 284 ALA A CB  1 
ATOM   2269  N N   . ILE A 1 289 ? -9.091  16.904  53.094  1.00 31.47  ? 285 ILE A N   1 
ATOM   2270  C CA  . ILE A 1 289 ? -10.220 16.790  52.161  1.00 31.59  ? 285 ILE A CA  1 
ATOM   2271  C C   . ILE A 1 289 ? -10.927 15.443  52.304  1.00 34.66  ? 285 ILE A C   1 
ATOM   2272  O O   . ILE A 1 289 ? -10.295 14.393  52.212  1.00 34.59  ? 285 ILE A O   1 
ATOM   2273  C CB  . ILE A 1 289 ? -9.753  16.931  50.702  1.00 32.15  ? 285 ILE A CB  1 
ATOM   2274  C CG1 . ILE A 1 289 ? -9.164  18.314  50.455  1.00 32.97  ? 285 ILE A CG1 1 
ATOM   2275  C CG2 . ILE A 1 289 ? -10.915 16.706  49.749  1.00 32.79  ? 285 ILE A CG2 1 
ATOM   2276  C CD1 . ILE A 1 289 ? -8.555  18.454  49.077  1.00 34.33  ? 285 ILE A CD1 1 
ATOM   2277  N N   . ASN A 1 290 ? -12.243 15.482  52.500  1.00 43.07  ? 286 ASN A N   1 
ATOM   2278  C CA  . ASN A 1 290 ? -13.049 14.271  52.663  1.00 49.96  ? 286 ASN A CA  1 
ATOM   2279  C C   . ASN A 1 290 ? -13.673 14.071  51.298  1.00 51.45  ? 286 ASN A C   1 
ATOM   2280  O O   . ASN A 1 290 ? -14.686 14.686  50.971  1.00 40.87  ? 286 ASN A O   1 
ATOM   2281  C CB  . ASN A 1 290 ? -14.099 14.426  53.774  1.00 55.73  ? 286 ASN A CB  1 
ATOM   2282  C CG  . ASN A 1 290 ? -14.805 13.124  54.112  1.00 61.07  ? 286 ASN A CG  1 
ATOM   2283  O OD1 . ASN A 1 290 ? -14.357 12.031  53.751  1.00 57.55  ? 286 ASN A OD1 1 
ATOM   2284  N ND2 . ASN A 1 290 ? -15.926 13.248  54.823  1.00 74.79  ? 286 ASN A ND2 1 
ATOM   2285  N N   . SER A 1 291 ? -13.017 13.230  50.501  1.00 59.22  ? 287 SER A N   1 
ATOM   2286  C CA  . SER A 1 291 ? -13.051 13.335  49.042  1.00 59.91  ? 287 SER A CA  1 
ATOM   2287  C C   . SER A 1 291 ? -13.736 12.203  48.252  1.00 54.90  ? 287 SER A C   1 
ATOM   2288  O O   . SER A 1 291 ? -13.200 11.098  48.172  1.00 68.03  ? 287 SER A O   1 
ATOM   2289  C CB  . SER A 1 291 ? -11.599 13.526  48.546  1.00 64.60  ? 287 SER A CB  1 
ATOM   2290  O OG  . SER A 1 291 ? -10.716 12.564  49.113  1.00 57.30  ? 287 SER A OG  1 
ATOM   2291  N N   . SER A 1 292 ? -14.910 12.486  47.670  1.00 42.87  ? 288 SER A N   1 
ATOM   2292  C CA  . SER A 1 292 ? -15.516 11.617  46.637  1.00 39.97  ? 288 SER A CA  1 
ATOM   2293  C C   . SER A 1 292 ? -15.517 12.215  45.216  1.00 34.28  ? 288 SER A C   1 
ATOM   2294  O O   . SER A 1 292 ? -15.528 11.494  44.229  1.00 31.57  ? 288 SER A O   1 
ATOM   2295  C CB  . SER A 1 292 ? -16.967 11.305  46.977  1.00 41.56  ? 288 SER A CB  1 
ATOM   2296  O OG  . SER A 1 292 ? -17.672 12.498  47.267  1.00 49.85  ? 288 SER A OG  1 
ATOM   2297  N N   . MET A 1 293 ? -15.593 13.533  45.131  1.00 30.31  ? 289 MET A N   1 
ATOM   2298  C CA  . MET A 1 293 ? -15.639 14.258  43.855  1.00 31.68  ? 289 MET A CA  1 
ATOM   2299  C C   . MET A 1 293 ? -14.357 14.087  43.042  1.00 28.25  ? 289 MET A C   1 
ATOM   2300  O O   . MET A 1 293 ? -13.283 13.917  43.612  1.00 28.91  ? 289 MET A O   1 
ATOM   2301  C CB  . MET A 1 293 ? -15.863 15.749  44.116  1.00 35.42  ? 289 MET A CB  1 
ATOM   2302  C CG  . MET A 1 293 ? -17.204 16.116  44.737  1.00 38.82  ? 289 MET A CG  1 
ATOM   2303  S SD  . MET A 1 293 ? -18.634 15.595  43.772  1.00 45.49  ? 289 MET A SD  1 
ATOM   2304  C CE  . MET A 1 293 ? -19.044 14.053  44.589  1.00 47.22  ? 289 MET A CE  1 
ATOM   2305  N N   . PRO A 1 294 ? -14.462 14.146  41.704  1.00 24.71  ? 290 PRO A N   1 
ATOM   2306  C CA  . PRO A 1 294 ? -13.311 13.909  40.835  1.00 25.56  ? 290 PRO A CA  1 
ATOM   2307  C C   . PRO A 1 294 ? -12.312 15.066  40.755  1.00 25.88  ? 290 PRO A C   1 
ATOM   2308  O O   . PRO A 1 294 ? -11.144 14.819  40.452  1.00 27.81  ? 290 PRO A O   1 
ATOM   2309  C CB  . PRO A 1 294 ? -13.949 13.662  39.466  1.00 24.83  ? 290 PRO A CB  1 
ATOM   2310  C CG  . PRO A 1 294 ? -15.227 14.406  39.506  1.00 25.27  ? 290 PRO A CG  1 
ATOM   2311  C CD  . PRO A 1 294 ? -15.692 14.386  40.934  1.00 26.53  ? 290 PRO A CD  1 
ATOM   2312  N N   . PHE A 1 295 ? -12.749 16.296  41.035  1.00 23.65  ? 291 PHE A N   1 
ATOM   2313  C CA  . PHE A 1 295 ? -11.874 17.473  40.922  1.00 22.90  ? 291 PHE A CA  1 
ATOM   2314  C C   . PHE A 1 295 ? -11.871 18.367  42.167  1.00 23.26  ? 291 PHE A C   1 
ATOM   2315  O O   . PHE A 1 295 ? -12.842 18.393  42.919  1.00 23.67  ? 291 PHE A O   1 
ATOM   2316  C CB  . PHE A 1 295 ? -12.288 18.309  39.716  1.00 20.89  ? 291 PHE A CB  1 
ATOM   2317  C CG  . PHE A 1 295 ? -12.354 17.531  38.443  1.00 20.86  ? 291 PHE A CG  1 
ATOM   2318  C CD1 . PHE A 1 295 ? -13.577 17.207  37.876  1.00 21.55  ? 291 PHE A CD1 1 
ATOM   2319  C CD2 . PHE A 1 295 ? -11.196 17.119  37.813  1.00 20.75  ? 291 PHE A CD2 1 
ATOM   2320  C CE1 . PHE A 1 295 ? -13.640 16.486  36.702  1.00 21.37  ? 291 PHE A CE1 1 
ATOM   2321  C CE2 . PHE A 1 295 ? -11.247 16.405  36.633  1.00 20.93  ? 291 PHE A CE2 1 
ATOM   2322  C CZ  . PHE A 1 295 ? -12.471 16.085  36.078  1.00 22.61  ? 291 PHE A CZ  1 
ATOM   2323  N N   . HIS A 1 296 ? -10.778 19.105  42.363  1.00 22.40  ? 292 HIS A N   1 
ATOM   2324  C CA  . HIS A 1 296 ? -10.691 20.112  43.429  1.00 21.88  ? 292 HIS A CA  1 
ATOM   2325  C C   . HIS A 1 296 ? -9.880  21.320  43.017  1.00 22.63  ? 292 HIS A C   1 
ATOM   2326  O O   . HIS A 1 296 ? -9.113  21.259  42.053  1.00 21.80  ? 292 HIS A O   1 
ATOM   2327  C CB  . HIS A 1 296 ? -10.144 19.490  44.718  1.00 20.68  ? 292 HIS A CB  1 
ATOM   2328  C CG  . HIS A 1 296 ? -8.640  19.334  44.752  1.00 20.17  ? 292 HIS A CG  1 
ATOM   2329  N ND1 . HIS A 1 296 ? -8.017  18.225  44.317  1.00 19.29  ? 292 HIS A ND1 1 
ATOM   2330  C CD2 . HIS A 1 296 ? -7.642  20.181  45.231  1.00 20.82  ? 292 HIS A CD2 1 
ATOM   2331  C CE1 . HIS A 1 296 ? -6.689  18.364  44.491  1.00 21.34  ? 292 HIS A CE1 1 
ATOM   2332  N NE2 . HIS A 1 296 ? -6.463  19.560  45.051  1.00 21.47  ? 292 HIS A NE2 1 
ATOM   2333  N N   . ASN A 1 297 ? -10.065 22.429  43.735  1.00 23.14  ? 293 ASN A N   1 
ATOM   2334  C CA  . ASN A 1 297 ? -9.283  23.654  43.517  1.00 23.84  ? 293 ASN A CA  1 
ATOM   2335  C C   . ASN A 1 297 ? -8.636  24.209  44.797  1.00 25.18  ? 293 ASN A C   1 
ATOM   2336  O O   . ASN A 1 297 ? -8.232  25.372  44.843  1.00 27.69  ? 293 ASN A O   1 
ATOM   2337  C CB  . ASN A 1 297 ? -10.150 24.729  42.854  1.00 24.21  ? 293 ASN A CB  1 
ATOM   2338  C CG  . ASN A 1 297 ? -11.250 25.260  43.771  1.00 24.79  ? 293 ASN A CG  1 
ATOM   2339  O OD1 . ASN A 1 297 ? -11.570 24.663  44.793  1.00 25.65  ? 293 ASN A OD1 1 
ATOM   2340  N ND2 . ASN A 1 297 ? -11.854 26.374  43.382  1.00 22.03  ? 293 ASN A ND2 1 
ATOM   2341  N N   . ILE A 1 298 ? -8.527  23.363  45.819  1.00 25.30  ? 294 ILE A N   1 
ATOM   2342  C CA  . ILE A 1 298 ? -7.934  23.727  47.111  1.00 26.21  ? 294 ILE A CA  1 
ATOM   2343  C C   . ILE A 1 298 ? -6.449  24.107  47.029  1.00 28.95  ? 294 ILE A C   1 
ATOM   2344  O O   . ILE A 1 298 ? -6.081  25.241  47.332  1.00 31.83  ? 294 ILE A O   1 
ATOM   2345  C CB  . ILE A 1 298 ? -8.053  22.579  48.153  1.00 25.22  ? 294 ILE A CB  1 
ATOM   2346  C CG1 . ILE A 1 298 ? -9.474  21.987  48.208  1.00 25.32  ? 294 ILE A CG1 1 
ATOM   2347  C CG2 . ILE A 1 298 ? -7.608  23.062  49.524  1.00 23.82  ? 294 ILE A CG2 1 
ATOM   2348  C CD1 . ILE A 1 298 ? -10.596 22.997  48.200  1.00 23.55  ? 294 ILE A CD1 1 
ATOM   2349  N N   . HIS A 1 299 ? -5.602  23.154  46.649  1.00 28.87  ? 295 HIS A N   1 
ATOM   2350  C CA  . HIS A 1 299 ? -4.152  23.314  46.769  1.00 29.30  ? 295 HIS A CA  1 
ATOM   2351  C C   . HIS A 1 299 ? -3.418  22.246  45.996  1.00 29.53  ? 295 HIS A C   1 
ATOM   2352  O O   . HIS A 1 299 ? -3.833  21.086  46.010  1.00 31.10  ? 295 HIS A O   1 
ATOM   2353  C CB  . HIS A 1 299 ? -3.743  23.241  48.238  1.00 28.16  ? 295 HIS A CB  1 
ATOM   2354  C CG  . HIS A 1 299 ? -2.452  23.956  48.549  1.00 27.90  ? 295 HIS A CG  1 
ATOM   2355  N ND1 . HIS A 1 299 ? -1.255  23.358  48.457  1.00 29.60  ? 295 HIS A ND1 1 
ATOM   2356  C CD2 . HIS A 1 299 ? -2.208  25.264  48.957  1.00 26.90  ? 295 HIS A CD2 1 
ATOM   2357  C CE1 . HIS A 1 299 ? -0.292  24.233  48.794  1.00 29.70  ? 295 HIS A CE1 1 
ATOM   2358  N NE2 . HIS A 1 299 ? -0.878  25.399  49.100  1.00 27.86  ? 295 HIS A NE2 1 
ATOM   2359  N N   . PRO A 1 300 ? -2.312  22.612  45.319  1.00 29.24  ? 296 PRO A N   1 
ATOM   2360  C CA  . PRO A 1 300 ? -1.570  21.619  44.522  1.00 27.79  ? 296 PRO A CA  1 
ATOM   2361  C C   . PRO A 1 300 ? -0.735  20.620  45.330  1.00 26.81  ? 296 PRO A C   1 
ATOM   2362  O O   . PRO A 1 300 ? -0.578  19.480  44.901  1.00 27.34  ? 296 PRO A O   1 
ATOM   2363  C CB  . PRO A 1 300 ? -0.649  22.481  43.648  1.00 25.45  ? 296 PRO A CB  1 
ATOM   2364  C CG  . PRO A 1 300 ? -0.500  23.761  44.388  1.00 26.05  ? 296 PRO A CG  1 
ATOM   2365  C CD  . PRO A 1 300 ? -1.798  23.979  45.110  1.00 28.88  ? 296 PRO A CD  1 
ATOM   2366  N N   . LEU A 1 301 ? -0.213  21.034  46.483  1.00 26.78  ? 297 LEU A N   1 
ATOM   2367  C CA  . LEU A 1 301 ? 0.745   20.214  47.239  1.00 24.38  ? 297 LEU A CA  1 
ATOM   2368  C C   . LEU A 1 301 ? 0.048   19.212  48.150  1.00 23.03  ? 297 LEU A C   1 
ATOM   2369  O O   . LEU A 1 301 ? 0.147   19.287  49.366  1.00 24.01  ? 297 LEU A O   1 
ATOM   2370  C CB  . LEU A 1 301 ? 1.692   21.105  48.057  1.00 23.92  ? 297 LEU A CB  1 
ATOM   2371  C CG  . LEU A 1 301 ? 2.387   22.236  47.290  1.00 24.72  ? 297 LEU A CG  1 
ATOM   2372  C CD1 . LEU A 1 301 ? 3.364   22.978  48.192  1.00 23.51  ? 297 LEU A CD1 1 
ATOM   2373  C CD2 . LEU A 1 301 ? 3.099   21.711  46.053  1.00 24.01  ? 297 LEU A CD2 1 
ATOM   2374  N N   . THR A 1 302 ? -0.620  18.240  47.550  1.00 24.08  ? 298 THR A N   1 
ATOM   2375  C CA  . THR A 1 302 ? -1.432  17.293  48.298  1.00 24.39  ? 298 THR A CA  1 
ATOM   2376  C C   . THR A 1 302 ? -0.700  15.976  48.566  1.00 27.29  ? 298 THR A C   1 
ATOM   2377  O O   . THR A 1 302 ? 0.208   15.602  47.822  1.00 31.07  ? 298 THR A O   1 
ATOM   2378  C CB  . THR A 1 302 ? -2.723  17.007  47.532  1.00 22.60  ? 298 THR A CB  1 
ATOM   2379  O OG1 . THR A 1 302 ? -2.405  16.464  46.248  1.00 20.79  ? 298 THR A OG1 1 
ATOM   2380  C CG2 . THR A 1 302 ? -3.511  18.291  47.346  1.00 22.73  ? 298 THR A CG2 1 
ATOM   2381  N N   . ILE A 1 303 ? -1.098  15.288  49.636  1.00 28.04  ? 299 ILE A N   1 
ATOM   2382  C CA  . ILE A 1 303 ? -0.553  13.974  49.988  1.00 27.67  ? 299 ILE A CA  1 
ATOM   2383  C C   . ILE A 1 303 ? -1.716  13.033  50.275  1.00 30.52  ? 299 ILE A C   1 
ATOM   2384  O O   . ILE A 1 303 ? -2.508  13.297  51.174  1.00 35.55  ? 299 ILE A O   1 
ATOM   2385  C CB  . ILE A 1 303 ? 0.359   14.029  51.235  1.00 27.34  ? 299 ILE A CB  1 
ATOM   2386  C CG1 . ILE A 1 303 ? 1.428   15.114  51.087  1.00 27.62  ? 299 ILE A CG1 1 
ATOM   2387  C CG2 . ILE A 1 303 ? 1.033   12.684  51.481  1.00 25.23  ? 299 ILE A CG2 1 
ATOM   2388  C CD1 . ILE A 1 303 ? 2.375   15.187  52.267  1.00 26.23  ? 299 ILE A CD1 1 
ATOM   2389  N N   . GLY A 1 304 ? -1.821  11.945  49.515  1.00 29.09  ? 300 GLY A N   1 
ATOM   2390  C CA  . GLY A 1 304 ? -2.946  11.012  49.649  1.00 27.39  ? 300 GLY A CA  1 
ATOM   2391  C C   . GLY A 1 304 ? -3.572  10.627  48.321  1.00 26.32  ? 300 GLY A C   1 
ATOM   2392  O O   . GLY A 1 304 ? -3.036  10.933  47.259  1.00 25.46  ? 300 GLY A O   1 
ATOM   2393  N N   . GLU A 1 305 ? -4.710  9.944   48.389  1.00 30.82  ? 301 GLU A N   1 
ATOM   2394  C CA  . GLU A 1 305 ? -5.530  9.671   47.212  1.00 33.41  ? 301 GLU A CA  1 
ATOM   2395  C C   . GLU A 1 305 ? -6.463  10.859  47.026  1.00 32.45  ? 301 GLU A C   1 
ATOM   2396  O O   . GLU A 1 305 ? -7.492  10.950  47.688  1.00 31.76  ? 301 GLU A O   1 
ATOM   2397  C CB  . GLU A 1 305 ? -6.338  8.388   47.408  1.00 38.47  ? 301 GLU A CB  1 
ATOM   2398  C CG  . GLU A 1 305 ? -5.504  7.121   47.551  1.00 43.84  ? 301 GLU A CG  1 
ATOM   2399  C CD  . GLU A 1 305 ? -6.306  5.951   48.096  1.00 49.33  ? 301 GLU A CD  1 
ATOM   2400  O OE1 . GLU A 1 305 ? -6.722  5.069   47.307  1.00 53.21  ? 301 GLU A OE1 1 
ATOM   2401  O OE2 . GLU A 1 305 ? -6.533  5.924   49.322  1.00 47.45  ? 301 GLU A OE2 1 
ATOM   2402  N N   . CYS A 1 306 ? -6.097  11.780  46.137  1.00 30.87  ? 302 CYS A N   1 
ATOM   2403  C CA  . CYS A 1 306 ? -6.797  13.058  46.030  1.00 29.64  ? 302 CYS A CA  1 
ATOM   2404  C C   . CYS A 1 306 ? -7.514  13.232  44.702  1.00 27.16  ? 302 CYS A C   1 
ATOM   2405  O O   . CYS A 1 306 ? -7.169  12.580  43.720  1.00 29.84  ? 302 CYS A O   1 
ATOM   2406  C CB  . CYS A 1 306 ? -5.819  14.216  46.233  1.00 32.78  ? 302 CYS A CB  1 
ATOM   2407  S SG  . CYS A 1 306 ? -5.030  14.229  47.860  1.00 43.46  ? 302 CYS A SG  1 
ATOM   2408  N N   . PRO A 1 307 ? -8.526  14.117  44.667  1.00 23.81  ? 303 PRO A N   1 
ATOM   2409  C CA  . PRO A 1 307 ? -9.103  14.493  43.387  1.00 22.88  ? 303 PRO A CA  1 
ATOM   2410  C C   . PRO A 1 307 ? -8.082  15.238  42.536  1.00 21.60  ? 303 PRO A C   1 
ATOM   2411  O O   . PRO A 1 307 ? -7.054  15.669  43.044  1.00 20.19  ? 303 PRO A O   1 
ATOM   2412  C CB  . PRO A 1 307 ? -10.258 15.421  43.777  1.00 23.27  ? 303 PRO A CB  1 
ATOM   2413  C CG  . PRO A 1 307 ? -10.573 15.072  45.191  1.00 23.85  ? 303 PRO A CG  1 
ATOM   2414  C CD  . PRO A 1 307 ? -9.261  14.708  45.798  1.00 23.28  ? 303 PRO A CD  1 
ATOM   2415  N N   . LYS A 1 308 ? -8.364  15.388  41.251  1.00 21.46  ? 304 LYS A N   1 
ATOM   2416  C CA  . LYS A 1 308 ? -7.424  16.048  40.357  1.00 23.04  ? 304 LYS A CA  1 
ATOM   2417  C C   . LYS A 1 308 ? -7.496  17.564  40.519  1.00 21.83  ? 304 LYS A C   1 
ATOM   2418  O O   . LYS A 1 308 ? -8.570  18.152  40.424  1.00 23.79  ? 304 LYS A O   1 
ATOM   2419  C CB  . LYS A 1 308 ? -7.689  15.625  38.912  1.00 25.40  ? 304 LYS A CB  1 
ATOM   2420  C CG  . LYS A 1 308 ? -7.529  14.123  38.695  1.00 28.10  ? 304 LYS A CG  1 
ATOM   2421  C CD  . LYS A 1 308 ? -6.067  13.690  38.730  1.00 28.05  ? 304 LYS A CD  1 
ATOM   2422  C CE  . LYS A 1 308 ? -5.878  12.327  39.378  1.00 32.10  ? 304 LYS A CE  1 
ATOM   2423  N NZ  . LYS A 1 308 ? -6.760  11.277  38.794  1.00 38.76  ? 304 LYS A NZ  1 
ATOM   2424  N N   . TYR A 1 309 ? -6.349  18.185  40.781  1.00 20.87  ? 305 TYR A N   1 
ATOM   2425  C CA  . TYR A 1 309 ? -6.276  19.627  40.965  1.00 21.46  ? 305 TYR A CA  1 
ATOM   2426  C C   . TYR A 1 309 ? -6.586  20.323  39.655  1.00 22.23  ? 305 TYR A C   1 
ATOM   2427  O O   . TYR A 1 309 ? -6.060  19.956  38.607  1.00 23.51  ? 305 TYR A O   1 
ATOM   2428  C CB  . TYR A 1 309 ? -4.892  20.051  41.460  1.00 22.96  ? 305 TYR A CB  1 
ATOM   2429  C CG  . TYR A 1 309 ? -4.787  21.518  41.815  1.00 24.27  ? 305 TYR A CG  1 
ATOM   2430  C CD1 . TYR A 1 309 ? -5.640  22.086  42.754  1.00 24.90  ? 305 TYR A CD1 1 
ATOM   2431  C CD2 . TYR A 1 309 ? -3.826  22.336  41.224  1.00 26.44  ? 305 TYR A CD2 1 
ATOM   2432  C CE1 . TYR A 1 309 ? -5.548  23.426  43.092  1.00 25.78  ? 305 TYR A CE1 1 
ATOM   2433  C CE2 . TYR A 1 309 ? -3.723  23.680  41.561  1.00 27.94  ? 305 TYR A CE2 1 
ATOM   2434  C CZ  . TYR A 1 309 ? -4.589  24.219  42.497  1.00 27.38  ? 305 TYR A CZ  1 
ATOM   2435  O OH  . TYR A 1 309 ? -4.502  25.551  42.838  1.00 25.45  ? 305 TYR A OH  1 
ATOM   2436  N N   . VAL A 1 310 ? -7.423  21.347  39.730  1.00 22.93  ? 306 VAL A N   1 
ATOM   2437  C CA  . VAL A 1 310 ? -7.971  21.981  38.540  1.00 23.54  ? 306 VAL A CA  1 
ATOM   2438  C C   . VAL A 1 310 ? -8.130  23.472  38.804  1.00 23.76  ? 306 VAL A C   1 
ATOM   2439  O O   . VAL A 1 310 ? -8.244  23.893  39.955  1.00 26.30  ? 306 VAL A O   1 
ATOM   2440  C CB  . VAL A 1 310 ? -9.333  21.338  38.186  1.00 23.59  ? 306 VAL A CB  1 
ATOM   2441  C CG1 . VAL A 1 310 ? -10.495 22.263  38.527  1.00 22.07  ? 306 VAL A CG1 1 
ATOM   2442  C CG2 . VAL A 1 310 ? -9.369  20.904  36.735  1.00 22.25  ? 306 VAL A CG2 1 
ATOM   2443  N N   . LYS A 1 311 ? -8.121  24.267  37.742  1.00 25.99  ? 307 LYS A N   1 
ATOM   2444  C CA  . LYS A 1 311 ? -8.226  25.714  37.874  1.00 29.77  ? 307 LYS A CA  1 
ATOM   2445  C C   . LYS A 1 311 ? -9.610  26.169  37.455  1.00 31.66  ? 307 LYS A C   1 
ATOM   2446  O O   . LYS A 1 311 ? -9.833  26.590  36.317  1.00 34.62  ? 307 LYS A O   1 
ATOM   2447  C CB  . LYS A 1 311 ? -7.138  26.416  37.051  1.00 33.92  ? 307 LYS A CB  1 
ATOM   2448  C CG  . LYS A 1 311 ? -6.817  27.835  37.513  1.00 37.64  ? 307 LYS A CG  1 
ATOM   2449  C CD  . LYS A 1 311 ? -7.117  28.888  36.451  1.00 40.43  ? 307 LYS A CD  1 
ATOM   2450  C CE  . LYS A 1 311 ? -6.640  30.268  36.896  1.00 43.26  ? 307 LYS A CE  1 
ATOM   2451  N NZ  . LYS A 1 311 ? -5.155  30.351  37.029  1.00 43.55  ? 307 LYS A NZ  1 
ATOM   2452  N N   . SER A 1 312 ? -10.550 26.062  38.382  1.00 32.62  ? 308 SER A N   1 
ATOM   2453  C CA  . SER A 1 312 ? -11.860 26.639  38.170  1.00 37.37  ? 308 SER A CA  1 
ATOM   2454  C C   . SER A 1 312 ? -12.553 26.889  39.512  1.00 35.92  ? 308 SER A C   1 
ATOM   2455  O O   . SER A 1 312 ? -12.164 26.346  40.561  1.00 36.80  ? 308 SER A O   1 
ATOM   2456  C CB  . SER A 1 312 ? -12.703 25.767  37.225  1.00 39.99  ? 308 SER A CB  1 
ATOM   2457  O OG  . SER A 1 312 ? -13.587 24.915  37.923  1.00 43.96  ? 308 SER A OG  1 
ATOM   2458  N N   . ASN A 1 313 ? -13.550 27.760  39.461  1.00 35.26  ? 309 ASN A N   1 
ATOM   2459  C CA  . ASN A 1 313 ? -14.390 28.058  40.610  1.00 37.18  ? 309 ASN A CA  1 
ATOM   2460  C C   . ASN A 1 313 ? -15.638 27.186  40.648  1.00 34.48  ? 309 ASN A C   1 
ATOM   2461  O O   . ASN A 1 313 ? -16.212 26.982  41.712  1.00 34.84  ? 309 ASN A O   1 
ATOM   2462  C CB  . ASN A 1 313 ? -14.801 29.532  40.572  1.00 38.22  ? 309 ASN A CB  1 
ATOM   2463  C CG  . ASN A 1 313 ? -13.611 30.466  40.710  1.00 38.50  ? 309 ASN A CG  1 
ATOM   2464  O OD1 . ASN A 1 313 ? -12.724 30.241  41.536  1.00 35.45  ? 309 ASN A OD1 1 
ATOM   2465  N ND2 . ASN A 1 313 ? -13.583 31.515  39.894  1.00 39.49  ? 309 ASN A ND2 1 
ATOM   2466  N N   . LYS A 1 314 ? -16.047 26.680  39.482  1.00 36.18  ? 310 LYS A N   1 
ATOM   2467  C CA  . LYS A 1 314 ? -17.332 25.997  39.308  1.00 34.17  ? 310 LYS A CA  1 
ATOM   2468  C C   . LYS A 1 314 ? -17.257 24.852  38.295  1.00 30.13  ? 310 LYS A C   1 
ATOM   2469  O O   . LYS A 1 314 ? -16.731 25.038  37.198  1.00 32.21  ? 310 LYS A O   1 
ATOM   2470  C CB  . LYS A 1 314 ? -18.368 27.022  38.815  1.00 39.88  ? 310 LYS A CB  1 
ATOM   2471  C CG  . LYS A 1 314 ? -19.314 27.551  39.879  1.00 45.57  ? 310 LYS A CG  1 
ATOM   2472  C CD  . LYS A 1 314 ? -20.357 28.464  39.250  1.00 49.72  ? 310 LYS A CD  1 
ATOM   2473  C CE  . LYS A 1 314 ? -21.459 28.917  40.196  1.00 58.92  ? 310 LYS A CE  1 
ATOM   2474  N NZ  . LYS A 1 314 ? -22.483 29.725  39.474  1.00 65.24  ? 310 LYS A NZ  1 
ATOM   2475  N N   . LEU A 1 315 ? -17.772 23.675  38.658  1.00 24.81  ? 311 LEU A N   1 
ATOM   2476  C CA  . LEU A 1 315 ? -18.071 22.631  37.674  1.00 22.47  ? 311 LEU A CA  1 
ATOM   2477  C C   . LEU A 1 315 ? -19.464 22.078  37.950  1.00 23.15  ? 311 LEU A C   1 
ATOM   2478  O O   . LEU A 1 315 ? -19.619 21.054  38.613  1.00 26.42  ? 311 LEU A O   1 
ATOM   2479  C CB  . LEU A 1 315 ? -17.030 21.509  37.697  1.00 21.79  ? 311 LEU A CB  1 
ATOM   2480  C CG  . LEU A 1 315 ? -15.616 21.879  37.235  1.00 21.84  ? 311 LEU A CG  1 
ATOM   2481  C CD1 . LEU A 1 315 ? -14.653 20.732  37.494  1.00 21.47  ? 311 LEU A CD1 1 
ATOM   2482  C CD2 . LEU A 1 315 ? -15.602 22.282  35.766  1.00 19.46  ? 311 LEU A CD2 1 
ATOM   2483  N N   . VAL A 1 316 ? -20.477 22.759  37.429  1.00 20.80  ? 312 VAL A N   1 
ATOM   2484  C CA  . VAL A 1 316 ? -21.858 22.453  37.771  1.00 21.60  ? 312 VAL A CA  1 
ATOM   2485  C C   . VAL A 1 316 ? -22.574 21.647  36.689  1.00 23.90  ? 312 VAL A C   1 
ATOM   2486  O O   . VAL A 1 316 ? -22.744 22.110  35.560  1.00 24.09  ? 312 VAL A O   1 
ATOM   2487  C CB  . VAL A 1 316 ? -22.631 23.741  38.063  1.00 20.62  ? 312 VAL A CB  1 
ATOM   2488  C CG1 . VAL A 1 316 ? -24.030 23.411  38.554  1.00 20.38  ? 312 VAL A CG1 1 
ATOM   2489  C CG2 . VAL A 1 316 ? -21.872 24.551  39.106  1.00 18.62  ? 312 VAL A CG2 1 
ATOM   2490  N N   . LEU A 1 317 ? -22.998 20.440  37.063  1.00 25.35  ? 313 LEU A N   1 
ATOM   2491  C CA  . LEU A 1 317 ? -23.728 19.537  36.180  1.00 24.16  ? 313 LEU A CA  1 
ATOM   2492  C C   . LEU A 1 317 ? -25.219 19.769  36.323  1.00 24.99  ? 313 LEU A C   1 
ATOM   2493  O O   . LEU A 1 317 ? -25.762 19.744  37.433  1.00 25.64  ? 313 LEU A O   1 
ATOM   2494  C CB  . LEU A 1 317 ? -23.405 18.072  36.519  1.00 24.72  ? 313 LEU A CB  1 
ATOM   2495  C CG  . LEU A 1 317 ? -22.555 17.219  35.571  1.00 26.70  ? 313 LEU A CG  1 
ATOM   2496  C CD1 . LEU A 1 317 ? -21.527 18.021  34.786  1.00 27.91  ? 313 LEU A CD1 1 
ATOM   2497  C CD2 . LEU A 1 317 ? -21.866 16.122  36.364  1.00 27.48  ? 313 LEU A CD2 1 
ATOM   2498  N N   . ALA A 1 318 ? -25.883 20.005  35.198  1.00 26.42  ? 314 ALA A N   1 
ATOM   2499  C CA  . ALA A 1 318 ? -27.331 20.113  35.184  1.00 26.86  ? 314 ALA A CA  1 
ATOM   2500  C C   . ALA A 1 318 ? -27.902 18.740  35.465  1.00 27.74  ? 314 ALA A C   1 
ATOM   2501  O O   . ALA A 1 318 ? -27.597 17.773  34.766  1.00 29.84  ? 314 ALA A O   1 
ATOM   2502  C CB  . ALA A 1 318 ? -27.818 20.622  33.839  1.00 27.37  ? 314 ALA A CB  1 
ATOM   2503  N N   . THR A 1 319 ? -28.714 18.661  36.508  1.00 30.64  ? 315 THR A N   1 
ATOM   2504  C CA  . THR A 1 319 ? -29.402 17.427  36.855  1.00 35.57  ? 315 THR A CA  1 
ATOM   2505  C C   . THR A 1 319 ? -30.840 17.510  36.349  1.00 37.79  ? 315 THR A C   1 
ATOM   2506  O O   . THR A 1 319 ? -31.324 16.658  35.600  1.00 47.79  ? 315 THR A O   1 
ATOM   2507  C CB  . THR A 1 319 ? -29.417 17.177  38.369  1.00 39.47  ? 315 THR A CB  1 
ATOM   2508  O OG1 . THR A 1 319 ? -28.115 16.745  38.767  1.00 45.40  ? 315 THR A OG1 1 
ATOM   2509  C CG2 . THR A 1 319 ? -30.443 16.106  38.727  1.00 45.12  ? 315 THR A CG2 1 
ATOM   2510  N N   . GLY A 1 320 ? -31.512 18.581  36.740  1.00 32.71  ? 316 GLY A N   1 
ATOM   2511  C CA  . GLY A 1 320 ? -32.940 18.695  36.507  1.00 29.36  ? 316 GLY A CA  1 
ATOM   2512  C C   . GLY A 1 320 ? -33.283 19.351  35.184  1.00 28.93  ? 316 GLY A C   1 
ATOM   2513  O O   . GLY A 1 320 ? -32.567 19.193  34.199  1.00 30.17  ? 316 GLY A O   1 
ATOM   2514  N N   . LEU A 1 321 ? -34.390 20.089  35.169  1.00 29.04  ? 317 LEU A N   1 
ATOM   2515  C CA  . LEU A 1 321 ? -34.955 20.655  33.941  1.00 28.12  ? 317 LEU A CA  1 
ATOM   2516  C C   . LEU A 1 321 ? -34.671 22.148  33.846  1.00 29.53  ? 317 LEU A C   1 
ATOM   2517  O O   . LEU A 1 321 ? -34.271 22.763  34.830  1.00 35.18  ? 317 LEU A O   1 
ATOM   2518  C CB  . LEU A 1 321 ? -36.470 20.446  33.932  1.00 27.69  ? 317 LEU A CB  1 
ATOM   2519  C CG  . LEU A 1 321 ? -36.979 19.016  34.152  1.00 29.51  ? 317 LEU A CG  1 
ATOM   2520  C CD1 . LEU A 1 321 ? -38.318 19.041  34.870  1.00 31.64  ? 317 LEU A CD1 1 
ATOM   2521  C CD2 . LEU A 1 321 ? -37.102 18.252  32.844  1.00 27.99  ? 317 LEU A CD2 1 
ATOM   2522  N N   . ARG A 1 322 ? -34.883 22.724  32.664  1.00 26.71  ? 318 ARG A N   1 
ATOM   2523  C CA  . ARG A 1 322 ? -34.887 24.181  32.504  1.00 27.73  ? 318 ARG A CA  1 
ATOM   2524  C C   . ARG A 1 322 ? -35.981 24.796  33.376  1.00 26.74  ? 318 ARG A C   1 
ATOM   2525  O O   . ARG A 1 322 ? -37.083 24.266  33.435  1.00 23.57  ? 318 ARG A O   1 
ATOM   2526  C CB  . ARG A 1 322 ? -35.164 24.573  31.053  1.00 29.13  ? 318 ARG A CB  1 
ATOM   2527  C CG  . ARG A 1 322 ? -34.037 24.306  30.079  1.00 30.30  ? 318 ARG A CG  1 
ATOM   2528  C CD  . ARG A 1 322 ? -34.437 24.761  28.684  1.00 32.84  ? 318 ARG A CD  1 
ATOM   2529  N NE  . ARG A 1 322 ? -33.598 24.166  27.641  1.00 35.90  ? 318 ARG A NE  1 
ATOM   2530  C CZ  . ARG A 1 322 ? -32.522 24.735  27.097  1.00 38.18  ? 318 ARG A CZ  1 
ATOM   2531  N NH1 . ARG A 1 322 ? -32.112 25.943  27.481  1.00 39.81  ? 318 ARG A NH1 1 
ATOM   2532  N NH2 . ARG A 1 322 ? -31.841 24.086  26.156  1.00 38.14  ? 318 ARG A NH2 1 
ATOM   2533  N N   . ASN A 1 323 ? -35.670 25.913  34.031  1.00 30.10  ? 319 ASN A N   1 
ATOM   2534  C CA  . ASN A 1 323 ? -36.584 26.583  34.967  1.00 32.87  ? 319 ASN A CA  1 
ATOM   2535  C C   . ASN A 1 323 ? -36.753 28.098  34.701  1.00 42.48  ? 319 ASN A C   1 
ATOM   2536  O O   . ASN A 1 323 ? -37.077 28.858  35.622  1.00 47.39  ? 319 ASN A O   1 
ATOM   2537  C CB  . ASN A 1 323 ? -36.024 26.418  36.381  1.00 31.66  ? 319 ASN A CB  1 
ATOM   2538  C CG  . ASN A 1 323 ? -37.064 26.582  37.476  1.00 28.23  ? 319 ASN A CG  1 
ATOM   2539  O OD1 . ASN A 1 323 ? -36.746 27.070  38.564  1.00 29.04  ? 319 ASN A OD1 1 
ATOM   2540  N ND2 . ASN A 1 323 ? -38.292 26.159  37.213  1.00 25.16  ? 319 ASN A ND2 1 
ATOM   2541  N N   . SER A 1 324 ? -36.507 28.545  33.470  1.00 54.19  ? 320 SER A N   1 
ATOM   2542  C CA  . SER A 1 324 ? -36.523 29.980  33.156  1.00 65.02  ? 320 SER A CA  1 
ATOM   2543  C C   . SER A 1 324 ? -37.848 30.390  32.510  1.00 78.46  ? 320 SER A C   1 
ATOM   2544  O O   . SER A 1 324 ? -38.539 29.551  31.929  1.00 75.14  ? 320 SER A O   1 
ATOM   2545  C CB  . SER A 1 324 ? -35.344 30.351  32.244  1.00 68.23  ? 320 SER A CB  1 
ATOM   2546  O OG  . SER A 1 324 ? -35.382 29.634  31.024  1.00 75.15  ? 320 SER A OG  1 
ATOM   2547  N N   . PRO A 1 325 ? -38.211 31.685  32.617  1.00 99.37  ? 321 PRO A N   1 
ATOM   2548  C CA  . PRO A 1 325 ? -39.453 32.169  32.007  1.00 103.37 ? 321 PRO A CA  1 
ATOM   2549  C C   . PRO A 1 325 ? -39.356 32.281  30.484  1.00 95.62  ? 321 PRO A C   1 
ATOM   2550  O O   . PRO A 1 325 ? -39.954 31.475  29.766  1.00 85.89  ? 321 PRO A O   1 
ATOM   2551  C CB  . PRO A 1 325 ? -39.637 33.554  32.641  1.00 110.22 ? 321 PRO A CB  1 
ATOM   2552  C CG  . PRO A 1 325 ? -38.259 33.998  32.991  1.00 104.90 ? 321 PRO A CG  1 
ATOM   2553  C CD  . PRO A 1 325 ? -37.508 32.751  33.361  1.00 101.60 ? 321 PRO A CD  1 
ATOM   2554  N N   . GLY B 1 4   ? -57.120 -5.281  10.113  1.00 56.39  ? 0   GLY E N   1 
ATOM   2555  C CA  . GLY B 1 4   ? -56.637 -4.580  8.883   1.00 62.10  ? 0   GLY E CA  1 
ATOM   2556  C C   . GLY B 1 4   ? -55.187 -4.888  8.536   1.00 60.19  ? 0   GLY E C   1 
ATOM   2557  O O   . GLY B 1 4   ? -54.458 -5.475  9.336   1.00 64.48  ? 0   GLY E O   1 
ATOM   2558  N N   . ASP B 1 5   ? -54.767 -4.473  7.344   1.00 54.19  ? 1   ASP E N   1 
ATOM   2559  C CA  . ASP B 1 5   ? -53.393 -4.693  6.872   1.00 55.99  ? 1   ASP E CA  1 
ATOM   2560  C C   . ASP B 1 5   ? -52.422 -3.735  7.570   1.00 53.60  ? 1   ASP E C   1 
ATOM   2561  O O   . ASP B 1 5   ? -52.735 -2.556  7.747   1.00 60.51  ? 1   ASP E O   1 
ATOM   2562  C CB  . ASP B 1 5   ? -53.303 -4.497  5.351   1.00 59.13  ? 1   ASP E CB  1 
ATOM   2563  C CG  . ASP B 1 5   ? -54.004 -5.599  4.559   1.00 54.93  ? 1   ASP E CG  1 
ATOM   2564  O OD1 . ASP B 1 5   ? -54.042 -5.483  3.315   1.00 56.98  ? 1   ASP E OD1 1 
ATOM   2565  O OD2 . ASP B 1 5   ? -54.492 -6.582  5.158   1.00 53.92  ? 1   ASP E OD2 1 
ATOM   2566  N N   . HIS B 1 6   ? -51.250 -4.244  7.952   1.00 50.76  ? 2   HIS E N   1 
ATOM   2567  C CA  . HIS B 1 6   ? -50.248 -3.471  8.696   1.00 50.72  ? 2   HIS E CA  1 
ATOM   2568  C C   . HIS B 1 6   ? -48.932 -3.348  7.968   1.00 49.42  ? 2   HIS E C   1 
ATOM   2569  O O   . HIS B 1 6   ? -48.549 -4.232  7.206   1.00 49.82  ? 2   HIS E O   1 
ATOM   2570  C CB  . HIS B 1 6   ? -49.966 -4.126  10.046  1.00 52.17  ? 2   HIS E CB  1 
ATOM   2571  C CG  . HIS B 1 6   ? -51.178 -4.264  10.932  1.00 65.30  ? 2   HIS E CG  1 
ATOM   2572  N ND1 . HIS B 1 6   ? -51.448 -5.394  11.617  1.00 75.36  ? 2   HIS E ND1 1 
ATOM   2573  C CD2 . HIS B 1 6   ? -52.206 -3.372  11.222  1.00 70.22  ? 2   HIS E CD2 1 
ATOM   2574  C CE1 . HIS B 1 6   ? -52.587 -5.228  12.321  1.00 73.82  ? 2   HIS E CE1 1 
ATOM   2575  N NE2 . HIS B 1 6   ? -53.050 -3.991  12.077  1.00 70.96  ? 2   HIS E NE2 1 
ATOM   2576  N N   . ILE B 1 7   ? -48.229 -2.244  8.209   1.00 51.68  ? 3   ILE E N   1 
ATOM   2577  C CA  . ILE B 1 7   ? -46.791 -2.145  7.929   1.00 49.95  ? 3   ILE E CA  1 
ATOM   2578  C C   . ILE B 1 7   ? -46.124 -1.467  9.129   1.00 49.90  ? 3   ILE E C   1 
ATOM   2579  O O   . ILE B 1 7   ? -46.655 -0.498  9.664   1.00 49.97  ? 3   ILE E O   1 
ATOM   2580  C CB  . ILE B 1 7   ? -46.483 -1.384  6.618   1.00 48.58  ? 3   ILE E CB  1 
ATOM   2581  C CG1 . ILE B 1 7   ? -45.006 -1.529  6.247   1.00 51.25  ? 3   ILE E CG1 1 
ATOM   2582  C CG2 . ILE B 1 7   ? -46.829 0.093   6.737   1.00 45.48  ? 3   ILE E CG2 1 
ATOM   2583  C CD1 . ILE B 1 7   ? -44.680 -1.058  4.848   1.00 50.89  ? 3   ILE E CD1 1 
ATOM   2584  N N   . CYS B 1 8   ? -44.984 -2.001  9.565   1.00 53.79  ? 4   CYS E N   1 
ATOM   2585  C CA  . CYS B 1 8   ? -44.272 -1.490  10.743  1.00 53.47  ? 4   CYS E CA  1 
ATOM   2586  C C   . CYS B 1 8   ? -42.833 -1.148  10.398  1.00 45.21  ? 4   CYS E C   1 
ATOM   2587  O O   . CYS B 1 8   ? -42.252 -1.747  9.501   1.00 45.07  ? 4   CYS E O   1 
ATOM   2588  C CB  . CYS B 1 8   ? -44.278 -2.531  11.863  1.00 57.49  ? 4   CYS E CB  1 
ATOM   2589  S SG  . CYS B 1 8   ? -45.923 -3.002  12.439  1.00 74.68  ? 4   CYS E SG  1 
ATOM   2590  N N   . ILE B 1 9   ? -42.265 -0.180  11.112  1.00 43.39  ? 5   ILE E N   1 
ATOM   2591  C CA  . ILE B 1 9   ? -40.846 0.133   10.985  1.00 38.64  ? 5   ILE E CA  1 
ATOM   2592  C C   . ILE B 1 9   ? -40.148 -0.346  12.249  1.00 38.05  ? 5   ILE E C   1 
ATOM   2593  O O   . ILE B 1 9   ? -40.678 -0.215  13.350  1.00 40.87  ? 5   ILE E O   1 
ATOM   2594  C CB  . ILE B 1 9   ? -40.590 1.631   10.757  1.00 38.82  ? 5   ILE E CB  1 
ATOM   2595  C CG1 . ILE B 1 9   ? -41.088 2.060   9.376   1.00 40.28  ? 5   ILE E CG1 1 
ATOM   2596  C CG2 . ILE B 1 9   ? -39.104 1.931   10.840  1.00 45.79  ? 5   ILE E CG2 1 
ATOM   2597  C CD1 . ILE B 1 9   ? -42.592 2.158   9.265   1.00 38.10  ? 5   ILE E CD1 1 
ATOM   2598  N N   . GLY B 1 10  ? -38.965 -0.924  12.077  1.00 38.68  ? 6   GLY E N   1 
ATOM   2599  C CA  . GLY B 1 10  ? -38.246 -1.552  13.176  1.00 36.38  ? 6   GLY E CA  1 
ATOM   2600  C C   . GLY B 1 10  ? -36.798 -1.814  12.823  1.00 35.42  ? 6   GLY E C   1 
ATOM   2601  O O   . GLY B 1 10  ? -36.314 -1.357  11.786  1.00 37.78  ? 6   GLY E O   1 
ATOM   2602  N N   . TYR B 1 11  ? -36.111 -2.562  13.680  1.00 34.06  ? 7   TYR E N   1 
ATOM   2603  C CA  . TYR B 1 11  ? -34.681 -2.772  13.518  1.00 37.33  ? 7   TYR E CA  1 
ATOM   2604  C C   . TYR B 1 11  ? -34.229 -4.182  13.909  1.00 38.52  ? 7   TYR E C   1 
ATOM   2605  O O   . TYR B 1 11  ? -34.983 -4.951  14.501  1.00 33.07  ? 7   TYR E O   1 
ATOM   2606  C CB  . TYR B 1 11  ? -33.912 -1.714  14.317  1.00 44.03  ? 7   TYR E CB  1 
ATOM   2607  C CG  . TYR B 1 11  ? -34.251 -1.682  15.792  1.00 41.44  ? 7   TYR E CG  1 
ATOM   2608  C CD1 . TYR B 1 11  ? -33.536 -2.449  16.701  1.00 43.12  ? 7   TYR E CD1 1 
ATOM   2609  C CD2 . TYR B 1 11  ? -35.281 -0.888  16.273  1.00 43.99  ? 7   TYR E CD2 1 
ATOM   2610  C CE1 . TYR B 1 11  ? -33.833 -2.430  18.049  1.00 49.75  ? 7   TYR E CE1 1 
ATOM   2611  C CE2 . TYR B 1 11  ? -35.590 -0.859  17.623  1.00 46.84  ? 7   TYR E CE2 1 
ATOM   2612  C CZ  . TYR B 1 11  ? -34.861 -1.632  18.507  1.00 51.05  ? 7   TYR E CZ  1 
ATOM   2613  O OH  . TYR B 1 11  ? -35.153 -1.616  19.850  1.00 58.40  ? 7   TYR E OH  1 
ATOM   2614  N N   . HIS B 1 12  ? -32.985 -4.500  13.555  1.00 43.91  ? 8   HIS E N   1 
ATOM   2615  C CA  . HIS B 1 12  ? -32.434 -5.853  13.673  1.00 46.13  ? 8   HIS E CA  1 
ATOM   2616  C C   . HIS B 1 12  ? -32.239 -6.285  15.091  1.00 44.22  ? 8   HIS E C   1 
ATOM   2617  O O   . HIS B 1 12  ? -32.011 -5.465  15.975  1.00 48.17  ? 8   HIS E O   1 
ATOM   2618  C CB  . HIS B 1 12  ? -31.104 -5.919  12.922  1.00 55.76  ? 8   HIS E CB  1 
ATOM   2619  C CG  . HIS B 1 12  ? -30.391 -7.245  13.025  1.00 66.02  ? 8   HIS E CG  1 
ATOM   2620  N ND1 . HIS B 1 12  ? -30.618 -8.267  12.180  1.00 75.27  ? 8   HIS E ND1 1 
ATOM   2621  C CD2 . HIS B 1 12  ? -29.408 -7.673  13.904  1.00 68.98  ? 8   HIS E CD2 1 
ATOM   2622  C CE1 . HIS B 1 12  ? -29.828 -9.307  12.515  1.00 71.42  ? 8   HIS E CE1 1 
ATOM   2623  N NE2 . HIS B 1 12  ? -29.088 -8.942  13.570  1.00 67.88  ? 8   HIS E NE2 1 
ATOM   2624  N N   . ALA B 1 13  ? -32.343 -7.591  15.311  1.00 43.60  ? 9   ALA E N   1 
ATOM   2625  C CA  . ALA B 1 13  ? -32.001 -8.208  16.587  1.00 45.44  ? 9   ALA E CA  1 
ATOM   2626  C C   . ALA B 1 13  ? -31.355 -9.562  16.301  1.00 50.01  ? 9   ALA E C   1 
ATOM   2627  O O   . ALA B 1 13  ? -31.544 -10.128 15.225  1.00 51.01  ? 9   ALA E O   1 
ATOM   2628  C CB  . ALA B 1 13  ? -33.238 -8.364  17.453  1.00 39.54  ? 9   ALA E CB  1 
ATOM   2629  N N   . ASN B 1 14  ? -30.567 -10.061 17.247  1.00 51.94  ? 10  ASN E N   1 
ATOM   2630  C CA  . ASN B 1 14  ? -29.900 -11.353 17.088  1.00 53.78  ? 10  ASN E CA  1 
ATOM   2631  C C   . ASN B 1 14  ? -29.655 -12.042 18.437  1.00 57.76  ? 10  ASN E C   1 
ATOM   2632  O O   . ASN B 1 14  ? -30.185 -11.608 19.461  1.00 52.34  ? 10  ASN E O   1 
ATOM   2633  C CB  . ASN B 1 14  ? -28.601 -11.183 16.280  1.00 50.19  ? 10  ASN E CB  1 
ATOM   2634  C CG  . ASN B 1 14  ? -27.573 -10.307 16.981  1.00 50.62  ? 10  ASN E CG  1 
ATOM   2635  O OD1 . ASN B 1 14  ? -27.630 -10.098 18.197  1.00 55.71  ? 10  ASN E OD1 1 
ATOM   2636  N ND2 . ASN B 1 14  ? -26.626 -9.777  16.206  1.00 40.09  ? 10  ASN E ND2 1 
ATOM   2637  N N   . ASN B 1 15  ? -28.861 -13.111 18.427  1.00 61.77  ? 11  ASN E N   1 
ATOM   2638  C CA  . ASN B 1 15  ? -28.610 -13.925 19.622  1.00 70.32  ? 11  ASN E CA  1 
ATOM   2639  C C   . ASN B 1 15  ? -27.465 -13.407 20.511  1.00 77.70  ? 11  ASN E C   1 
ATOM   2640  O O   . ASN B 1 15  ? -27.052 -14.094 21.448  1.00 73.58  ? 11  ASN E O   1 
ATOM   2641  C CB  . ASN B 1 15  ? -28.356 -15.388 19.211  1.00 72.42  ? 11  ASN E CB  1 
ATOM   2642  C CG  . ASN B 1 15  ? -27.167 -15.546 18.278  1.00 82.10  ? 11  ASN E CG  1 
ATOM   2643  O OD1 . ASN B 1 15  ? -26.553 -14.565 17.859  1.00 81.05  ? 11  ASN E OD1 1 
ATOM   2644  N ND2 . ASN B 1 15  ? -26.848 -16.790 17.934  1.00 86.65  ? 11  ASN E ND2 1 
ATOM   2645  N N   . SER B 1 16  ? -26.974 -12.196 20.233  1.00 77.92  ? 12  SER E N   1 
ATOM   2646  C CA  . SER B 1 16  ? -25.820 -11.636 20.944  1.00 69.71  ? 12  SER E CA  1 
ATOM   2647  C C   . SER B 1 16  ? -26.126 -11.322 22.409  1.00 66.24  ? 12  SER E C   1 
ATOM   2648  O O   . SER B 1 16  ? -27.221 -10.871 22.744  1.00 60.65  ? 12  SER E O   1 
ATOM   2649  C CB  . SER B 1 16  ? -25.323 -10.367 20.242  1.00 67.43  ? 12  SER E CB  1 
ATOM   2650  O OG  . SER B 1 16  ? -24.164 -9.850  20.872  1.00 65.34  ? 12  SER E OG  1 
ATOM   2651  N N   . THR B 1 17  ? -25.143 -11.577 23.270  1.00 60.56  ? 13  THR E N   1 
ATOM   2652  C CA  . THR B 1 17  ? -25.226 -11.252 24.693  1.00 66.49  ? 13  THR E CA  1 
ATOM   2653  C C   . THR B 1 17  ? -24.184 -10.196 25.086  1.00 68.52  ? 13  THR E C   1 
ATOM   2654  O O   . THR B 1 17  ? -24.039 -9.874  26.271  1.00 55.44  ? 13  THR E O   1 
ATOM   2655  C CB  . THR B 1 17  ? -25.016 -12.509 25.561  1.00 69.92  ? 13  THR E CB  1 
ATOM   2656  O OG1 . THR B 1 17  ? -23.759 -13.116 25.231  1.00 70.06  ? 13  THR E OG1 1 
ATOM   2657  C CG2 . THR B 1 17  ? -26.153 -13.511 25.346  1.00 69.04  ? 13  THR E CG2 1 
ATOM   2658  N N   . GLU B 1 18  ? -23.471 -9.657  24.094  1.00 67.61  ? 14  GLU E N   1 
ATOM   2659  C CA  . GLU B 1 18  ? -22.452 -8.635  24.331  1.00 68.86  ? 14  GLU E CA  1 
ATOM   2660  C C   . GLU B 1 18  ? -23.077 -7.419  25.015  1.00 60.82  ? 14  GLU E C   1 
ATOM   2661  O O   . GLU B 1 18  ? -24.112 -6.919  24.576  1.00 59.04  ? 14  GLU E O   1 
ATOM   2662  C CB  . GLU B 1 18  ? -21.793 -8.207  23.015  1.00 77.22  ? 14  GLU E CB  1 
ATOM   2663  C CG  . GLU B 1 18  ? -21.016 -9.305  22.297  1.00 89.51  ? 14  GLU E CG  1 
ATOM   2664  C CD  . GLU B 1 18  ? -19.787 -9.770  23.062  1.00 101.59 ? 14  GLU E CD  1 
ATOM   2665  O OE1 . GLU B 1 18  ? -19.062 -8.914  23.615  1.00 103.27 ? 14  GLU E OE1 1 
ATOM   2666  O OE2 . GLU B 1 18  ? -19.537 -10.996 23.097  1.00 104.76 ? 14  GLU E OE2 1 
ATOM   2667  N N   . GLN B 1 19  ? -22.447 -6.966  26.096  1.00 58.10  ? 15  GLN E N   1 
ATOM   2668  C CA  . GLN B 1 19  ? -22.949 -5.846  26.888  1.00 53.34  ? 15  GLN E CA  1 
ATOM   2669  C C   . GLN B 1 19  ? -22.054 -4.624  26.733  1.00 49.32  ? 15  GLN E C   1 
ATOM   2670  O O   . GLN B 1 19  ? -20.835 -4.733  26.650  1.00 44.71  ? 15  GLN E O   1 
ATOM   2671  C CB  . GLN B 1 19  ? -23.050 -6.222  28.370  1.00 48.15  ? 15  GLN E CB  1 
ATOM   2672  C CG  . GLN B 1 19  ? -24.295 -7.015  28.724  1.00 52.53  ? 15  GLN E CG  1 
ATOM   2673  C CD  . GLN B 1 19  ? -24.457 -7.227  30.215  1.00 56.15  ? 15  GLN E CD  1 
ATOM   2674  O OE1 . GLN B 1 19  ? -23.563 -6.920  31.003  1.00 61.55  ? 15  GLN E OE1 1 
ATOM   2675  N NE2 . GLN B 1 19  ? -25.605 -7.763  30.609  1.00 62.61  ? 15  GLN E NE2 1 
ATOM   2676  N N   . VAL B 1 20  ? -22.688 -3.459  26.705  1.00 49.42  ? 16  VAL E N   1 
ATOM   2677  C CA  . VAL B 1 20  ? -22.001 -2.195  26.539  1.00 45.42  ? 16  VAL E CA  1 
ATOM   2678  C C   . VAL B 1 20  ? -22.512 -1.263  27.631  1.00 46.29  ? 16  VAL E C   1 
ATOM   2679  O O   . VAL B 1 20  ? -23.608 -1.463  28.160  1.00 46.66  ? 16  VAL E O   1 
ATOM   2680  C CB  . VAL B 1 20  ? -22.291 -1.609  25.141  1.00 44.62  ? 16  VAL E CB  1 
ATOM   2681  C CG1 . VAL B 1 20  ? -23.157 -0.362  25.240  1.00 43.59  ? 16  VAL E CG1 1 
ATOM   2682  C CG2 . VAL B 1 20  ? -20.993 -1.321  24.393  1.00 44.30  ? 16  VAL E CG2 1 
ATOM   2683  N N   . ASP B 1 21  ? -21.717 -0.259  27.978  1.00 43.16  ? 17  ASP E N   1 
ATOM   2684  C CA  . ASP B 1 21  ? -22.139 0.737   28.951  1.00 42.46  ? 17  ASP E CA  1 
ATOM   2685  C C   . ASP B 1 21  ? -22.310 2.099   28.274  1.00 39.34  ? 17  ASP E C   1 
ATOM   2686  O O   . ASP B 1 21  ? -21.563 2.466   27.367  1.00 35.60  ? 17  ASP E O   1 
ATOM   2687  C CB  . ASP B 1 21  ? -21.139 0.822   30.111  1.00 51.89  ? 17  ASP E CB  1 
ATOM   2688  C CG  . ASP B 1 21  ? -21.295 -0.327  31.135  1.00 60.60  ? 17  ASP E CG  1 
ATOM   2689  O OD1 . ASP B 1 21  ? -20.295 -0.752  31.772  1.00 70.28  ? 17  ASP E OD1 1 
ATOM   2690  O OD2 . ASP B 1 21  ? -22.419 -0.822  31.310  1.00 55.64  ? 17  ASP E OD2 1 
ATOM   2691  N N   . THR B 1 22  ? -23.322 2.828   28.722  1.00 40.62  ? 18  THR E N   1 
ATOM   2692  C CA  . THR B 1 22  ? -23.650 4.145   28.211  1.00 40.27  ? 18  THR E CA  1 
ATOM   2693  C C   . THR B 1 22  ? -23.433 5.129   29.356  1.00 37.37  ? 18  THR E C   1 
ATOM   2694  O O   . THR B 1 22  ? -23.371 4.731   30.517  1.00 40.41  ? 18  THR E O   1 
ATOM   2695  C CB  . THR B 1 22  ? -25.112 4.166   27.708  1.00 42.57  ? 18  THR E CB  1 
ATOM   2696  O OG1 . THR B 1 22  ? -25.198 3.432   26.480  1.00 47.58  ? 18  THR E OG1 1 
ATOM   2697  C CG2 . THR B 1 22  ? -25.613 5.575   27.463  1.00 42.41  ? 18  THR E CG2 1 
ATOM   2698  N N   . ILE B 1 23  ? -23.297 6.406   29.026  1.00 37.77  ? 19  ILE E N   1 
ATOM   2699  C CA  . ILE B 1 23  ? -23.132 7.457   30.030  1.00 37.02  ? 19  ILE E CA  1 
ATOM   2700  C C   . ILE B 1 23  ? -24.347 7.487   30.979  1.00 37.14  ? 19  ILE E C   1 
ATOM   2701  O O   . ILE B 1 23  ? -24.208 7.837   32.145  1.00 31.63  ? 19  ILE E O   1 
ATOM   2702  C CB  . ILE B 1 23  ? -22.861 8.841   29.353  1.00 38.89  ? 19  ILE E CB  1 
ATOM   2703  C CG1 . ILE B 1 23  ? -21.686 9.576   30.010  1.00 43.17  ? 19  ILE E CG1 1 
ATOM   2704  C CG2 . ILE B 1 23  ? -24.097 9.724   29.329  1.00 40.75  ? 19  ILE E CG2 1 
ATOM   2705  C CD1 . ILE B 1 23  ? -21.975 10.119  31.390  1.00 42.81  ? 19  ILE E CD1 1 
ATOM   2706  N N   . MET B 1 24  ? -25.522 7.101   30.476  1.00 39.19  ? 20  MET E N   1 
ATOM   2707  C CA  . MET B 1 24  ? -26.765 7.100   31.259  1.00 43.52  ? 20  MET E CA  1 
ATOM   2708  C C   . MET B 1 24  ? -27.315 5.711   31.619  1.00 49.15  ? 20  MET E C   1 
ATOM   2709  O O   . MET B 1 24  ? -28.182 5.607   32.485  1.00 48.77  ? 20  MET E O   1 
ATOM   2710  C CB  . MET B 1 24  ? -27.848 7.871   30.505  1.00 43.02  ? 20  MET E CB  1 
ATOM   2711  C CG  . MET B 1 24  ? -27.611 9.370   30.441  1.00 44.68  ? 20  MET E CG  1 
ATOM   2712  S SD  . MET B 1 24  ? -29.155 10.244  30.124  1.00 49.62  ? 20  MET E SD  1 
ATOM   2713  C CE  . MET B 1 24  ? -29.526 9.674   28.462  1.00 43.10  ? 20  MET E CE  1 
ATOM   2714  N N   . GLU B 1 25  ? -26.827 4.657   30.964  1.00 51.03  ? 21  GLU E N   1 
ATOM   2715  C CA  . GLU B 1 25  ? -27.319 3.295   31.198  1.00 48.59  ? 21  GLU E CA  1 
ATOM   2716  C C   . GLU B 1 25  ? -26.187 2.298   31.364  1.00 49.52  ? 21  GLU E C   1 
ATOM   2717  O O   . GLU B 1 25  ? -25.207 2.326   30.617  1.00 45.09  ? 21  GLU E O   1 
ATOM   2718  C CB  . GLU B 1 25  ? -28.187 2.831   30.032  1.00 52.20  ? 21  GLU E CB  1 
ATOM   2719  C CG  . GLU B 1 25  ? -29.521 3.538   29.912  1.00 56.99  ? 21  GLU E CG  1 
ATOM   2720  C CD  . GLU B 1 25  ? -30.263 3.135   28.656  1.00 60.75  ? 21  GLU E CD  1 
ATOM   2721  O OE1 . GLU B 1 25  ? -30.482 1.915   28.470  1.00 63.34  ? 21  GLU E OE1 1 
ATOM   2722  O OE2 . GLU B 1 25  ? -30.620 4.030   27.858  1.00 62.43  ? 21  GLU E OE2 1 
ATOM   2723  N N   . LYS B 1 26  ? -26.340 1.396   32.328  1.00 53.47  ? 22  LYS E N   1 
ATOM   2724  C CA  . LYS B 1 26  ? -25.376 0.324   32.523  1.00 51.59  ? 22  LYS E CA  1 
ATOM   2725  C C   . LYS B 1 26  ? -25.870 -0.972  31.881  1.00 49.40  ? 22  LYS E C   1 
ATOM   2726  O O   . LYS B 1 26  ? -27.074 -1.186  31.735  1.00 43.88  ? 22  LYS E O   1 
ATOM   2727  C CB  . LYS B 1 26  ? -25.073 0.109   34.005  1.00 56.58  ? 22  LYS E CB  1 
ATOM   2728  C CG  . LYS B 1 26  ? -24.096 1.107   34.605  1.00 59.40  ? 22  LYS E CG  1 
ATOM   2729  C CD  . LYS B 1 26  ? -23.179 0.431   35.614  1.00 64.78  ? 22  LYS E CD  1 
ATOM   2730  C CE  . LYS B 1 26  ? -22.185 1.386   36.228  1.00 65.13  ? 22  LYS E CE  1 
ATOM   2731  N NZ  . LYS B 1 26  ? -22.797 2.594   36.849  1.00 59.51  ? 22  LYS E NZ  1 
ATOM   2732  N N   . ASN B 1 27  ? -24.921 -1.822  31.494  1.00 49.64  ? 23  ASN E N   1 
ATOM   2733  C CA  . ASN B 1 27  ? -25.202 -3.175  31.010  1.00 52.40  ? 23  ASN E CA  1 
ATOM   2734  C C   . ASN B 1 27  ? -26.352 -3.232  30.008  1.00 50.39  ? 23  ASN E C   1 
ATOM   2735  O O   . ASN B 1 27  ? -27.380 -3.862  30.251  1.00 54.04  ? 23  ASN E O   1 
ATOM   2736  C CB  . ASN B 1 27  ? -25.425 -4.133  32.194  1.00 57.00  ? 23  ASN E CB  1 
ATOM   2737  C CG  . ASN B 1 27  ? -24.153 -4.368  32.996  1.00 65.10  ? 23  ASN E CG  1 
ATOM   2738  O OD1 . ASN B 1 27  ? -23.124 -3.737  32.732  1.00 71.89  ? 23  ASN E OD1 1 
ATOM   2739  N ND2 . ASN B 1 27  ? -24.213 -5.286  33.972  1.00 73.94  ? 23  ASN E ND2 1 
ATOM   2740  N N   . VAL B 1 28  ? -26.148 -2.562  28.876  1.00 48.02  ? 24  VAL E N   1 
ATOM   2741  C CA  . VAL B 1 28  ? -27.093 -2.580  27.766  1.00 43.79  ? 24  VAL E CA  1 
ATOM   2742  C C   . VAL B 1 28  ? -26.671 -3.650  26.773  1.00 46.52  ? 24  VAL E C   1 
ATOM   2743  O O   . VAL B 1 28  ? -25.572 -3.589  26.216  1.00 48.82  ? 24  VAL E O   1 
ATOM   2744  C CB  . VAL B 1 28  ? -27.139 -1.227  27.025  1.00 42.24  ? 24  VAL E CB  1 
ATOM   2745  C CG1 . VAL B 1 28  ? -28.005 -1.325  25.778  1.00 37.10  ? 24  VAL E CG1 1 
ATOM   2746  C CG2 . VAL B 1 28  ? -27.663 -0.134  27.939  1.00 40.24  ? 24  VAL E CG2 1 
ATOM   2747  N N   . THR B 1 29  ? -27.540 -4.629  26.548  1.00 49.17  ? 25  THR E N   1 
ATOM   2748  C CA  . THR B 1 29  ? -27.251 -5.695  25.597  1.00 46.89  ? 25  THR E CA  1 
ATOM   2749  C C   . THR B 1 29  ? -27.330 -5.128  24.190  1.00 41.98  ? 25  THR E C   1 
ATOM   2750  O O   . THR B 1 29  ? -28.189 -4.304  23.894  1.00 43.83  ? 25  THR E O   1 
ATOM   2751  C CB  . THR B 1 29  ? -28.217 -6.882  25.750  1.00 48.80  ? 25  THR E CB  1 
ATOM   2752  O OG1 . THR B 1 29  ? -28.273 -7.278  27.124  1.00 55.75  ? 25  THR E OG1 1 
ATOM   2753  C CG2 . THR B 1 29  ? -27.748 -8.059  24.915  1.00 45.75  ? 25  THR E CG2 1 
ATOM   2754  N N   . VAL B 1 30  ? -26.430 -5.581  23.326  1.00 42.65  ? 26  VAL E N   1 
ATOM   2755  C CA  . VAL B 1 30  ? -26.230 -4.956  22.027  1.00 42.33  ? 26  VAL E CA  1 
ATOM   2756  C C   . VAL B 1 30  ? -25.915 -5.995  20.948  1.00 44.17  ? 26  VAL E C   1 
ATOM   2757  O O   . VAL B 1 30  ? -25.385 -7.061  21.239  1.00 51.45  ? 26  VAL E O   1 
ATOM   2758  C CB  . VAL B 1 30  ? -25.089 -3.920  22.137  1.00 38.48  ? 26  VAL E CB  1 
ATOM   2759  C CG1 . VAL B 1 30  ? -23.838 -4.378  21.409  1.00 37.92  ? 26  VAL E CG1 1 
ATOM   2760  C CG2 . VAL B 1 30  ? -25.560 -2.566  21.642  1.00 38.27  ? 26  VAL E CG2 1 
ATOM   2761  N N   . THR B 1 31  ? -26.246 -5.678  19.703  1.00 43.40  ? 27  THR E N   1 
ATOM   2762  C CA  . THR B 1 31  ? -26.117 -6.623  18.598  1.00 46.00  ? 27  THR E CA  1 
ATOM   2763  C C   . THR B 1 31  ? -24.689 -6.888  18.144  1.00 48.66  ? 27  THR E C   1 
ATOM   2764  O O   . THR B 1 31  ? -24.323 -8.037  17.871  1.00 49.76  ? 27  THR E O   1 
ATOM   2765  C CB  . THR B 1 31  ? -26.915 -6.078  17.403  1.00 44.05  ? 27  THR E CB  1 
ATOM   2766  O OG1 . THR B 1 31  ? -28.295 -6.377  17.612  1.00 57.33  ? 27  THR E OG1 1 
ATOM   2767  C CG2 . THR B 1 31  ? -26.459 -6.671  16.100  1.00 48.46  ? 27  THR E CG2 1 
ATOM   2768  N N   . HIS B 1 32  ? -23.910 -5.817  18.029  1.00 52.77  ? 28  HIS E N   1 
ATOM   2769  C CA  . HIS B 1 32  ? -22.501 -5.898  17.649  1.00 56.23  ? 28  HIS E CA  1 
ATOM   2770  C C   . HIS B 1 32  ? -21.692 -4.978  18.510  1.00 54.22  ? 28  HIS E C   1 
ATOM   2771  O O   . HIS B 1 32  ? -22.143 -3.881  18.820  1.00 50.31  ? 28  HIS E O   1 
ATOM   2772  C CB  . HIS B 1 32  ? -22.306 -5.494  16.190  1.00 60.85  ? 28  HIS E CB  1 
ATOM   2773  C CG  . HIS B 1 32  ? -22.998 -6.401  15.195  1.00 72.63  ? 28  HIS E CG  1 
ATOM   2774  N ND1 . HIS B 1 32  ? -22.565 -7.649  14.933  1.00 83.05  ? 28  HIS E ND1 1 
ATOM   2775  C CD2 . HIS B 1 32  ? -24.113 -6.190  14.373  1.00 74.55  ? 28  HIS E CD2 1 
ATOM   2776  C CE1 . HIS B 1 32  ? -23.363 -8.215  14.005  1.00 79.97  ? 28  HIS E CE1 1 
ATOM   2777  N NE2 . HIS B 1 32  ? -24.310 -7.321  13.666  1.00 81.05  ? 28  HIS E NE2 1 
ATOM   2778  N N   . ALA B 1 33  ? -20.490 -5.403  18.900  1.00 53.24  ? 29  ALA E N   1 
ATOM   2779  C CA  . ALA B 1 33  ? -19.594 -4.559  19.687  1.00 49.04  ? 29  ALA E CA  1 
ATOM   2780  C C   . ALA B 1 33  ? -18.132 -4.808  19.321  1.00 53.59  ? 29  ALA E C   1 
ATOM   2781  O O   . ALA B 1 33  ? -17.764 -5.910  18.912  1.00 51.70  ? 29  ALA E O   1 
ATOM   2782  C CB  . ALA B 1 33  ? -19.812 -4.801  21.172  1.00 37.66  ? 29  ALA E CB  1 
ATOM   2783  N N   . GLN B 1 34  ? -17.308 -3.775  19.484  1.00 54.87  ? 30  GLN E N   1 
ATOM   2784  C CA  . GLN B 1 34  ? -15.876 -3.870  19.237  1.00 52.29  ? 30  GLN E CA  1 
ATOM   2785  C C   . GLN B 1 34  ? -15.102 -3.330  20.438  1.00 48.05  ? 30  GLN E C   1 
ATOM   2786  O O   . GLN B 1 34  ? -15.315 -2.191  20.857  1.00 42.06  ? 30  GLN E O   1 
ATOM   2787  C CB  . GLN B 1 34  ? -15.511 -3.089  17.973  1.00 58.86  ? 30  GLN E CB  1 
ATOM   2788  C CG  . GLN B 1 34  ? -14.144 -3.444  17.401  1.00 62.38  ? 30  GLN E CG  1 
ATOM   2789  C CD  . GLN B 1 34  ? -13.966 -3.006  15.958  1.00 70.65  ? 30  GLN E CD  1 
ATOM   2790  O OE1 . GLN B 1 34  ? -14.938 -2.843  15.218  1.00 75.48  ? 30  GLN E OE1 1 
ATOM   2791  N NE2 . GLN B 1 34  ? -12.717 -2.831  15.544  1.00 74.34  ? 30  GLN E NE2 1 
ATOM   2792  N N   . ASP B 1 35  ? -14.218 -4.154  20.998  1.00 50.83  ? 31  ASP E N   1 
ATOM   2793  C CA  . ASP B 1 35  ? -13.375 -3.735  22.118  1.00 47.99  ? 31  ASP E CA  1 
ATOM   2794  C C   . ASP B 1 35  ? -12.184 -2.960  21.567  1.00 47.00  ? 31  ASP E C   1 
ATOM   2795  O O   . ASP B 1 35  ? -11.569 -3.386  20.593  1.00 55.18  ? 31  ASP E O   1 
ATOM   2796  C CB  . ASP B 1 35  ? -12.901 -4.943  22.932  1.00 50.87  ? 31  ASP E CB  1 
ATOM   2797  C CG  . ASP B 1 35  ? -12.501 -4.577  24.364  1.00 61.21  ? 31  ASP E CG  1 
ATOM   2798  O OD1 . ASP B 1 35  ? -12.132 -3.410  24.622  1.00 59.31  ? 31  ASP E OD1 1 
ATOM   2799  O OD2 . ASP B 1 35  ? -12.555 -5.470  25.238  1.00 64.30  ? 31  ASP E OD2 1 
ATOM   2800  N N   . ILE B 1 36  ? -11.866 -1.827  22.190  1.00 44.11  ? 32  ILE E N   1 
ATOM   2801  C CA  . ILE B 1 36  ? -10.760 -0.981  21.723  1.00 40.52  ? 32  ILE E CA  1 
ATOM   2802  C C   . ILE B 1 36  ? -9.560  -1.035  22.673  1.00 44.79  ? 32  ILE E C   1 
ATOM   2803  O O   . ILE B 1 36  ? -8.667  -0.198  22.586  1.00 47.37  ? 32  ILE E O   1 
ATOM   2804  C CB  . ILE B 1 36  ? -11.163 0.487   21.466  1.00 38.66  ? 32  ILE E CB  1 
ATOM   2805  C CG1 . ILE B 1 36  ? -11.796 1.108   22.700  1.00 36.56  ? 32  ILE E CG1 1 
ATOM   2806  C CG2 . ILE B 1 36  ? -12.115 0.559   20.286  1.00 41.21  ? 32  ILE E CG2 1 
ATOM   2807  C CD1 . ILE B 1 36  ? -11.948 2.609   22.599  1.00 30.88  ? 32  ILE E CD1 1 
ATOM   2808  N N   . LEU B 1 37  ? -9.552  -2.024  23.568  1.00 47.85  ? 33  LEU E N   1 
ATOM   2809  C CA  . LEU B 1 37  ? -8.494  -2.195  24.563  1.00 48.59  ? 33  LEU E CA  1 
ATOM   2810  C C   . LEU B 1 37  ? -7.731  -3.486  24.292  1.00 52.80  ? 33  LEU E C   1 
ATOM   2811  O O   . LEU B 1 37  ? -8.308  -4.574  24.342  1.00 52.96  ? 33  LEU E O   1 
ATOM   2812  C CB  . LEU B 1 37  ? -9.102  -2.244  25.967  1.00 44.02  ? 33  LEU E CB  1 
ATOM   2813  C CG  . LEU B 1 37  ? -8.177  -2.507  27.153  1.00 43.84  ? 33  LEU E CG  1 
ATOM   2814  C CD1 . LEU B 1 37  ? -7.186  -1.372  27.334  1.00 46.98  ? 33  LEU E CD1 1 
ATOM   2815  C CD2 . LEU B 1 37  ? -8.993  -2.699  28.420  1.00 47.01  ? 33  LEU E CD2 1 
ATOM   2816  N N   . GLU B 1 38  ? -6.435  -3.366  24.011  1.00 55.34  ? 34  GLU E N   1 
ATOM   2817  C CA  . GLU B 1 38  ? -5.593  -4.533  23.759  1.00 58.48  ? 34  GLU E CA  1 
ATOM   2818  C C   . GLU B 1 38  ? -5.267  -5.247  25.071  1.00 57.88  ? 34  GLU E C   1 
ATOM   2819  O O   . GLU B 1 38  ? -4.793  -4.620  26.017  1.00 60.59  ? 34  GLU E O   1 
ATOM   2820  C CB  . GLU B 1 38  ? -4.299  -4.127  23.051  1.00 60.39  ? 34  GLU E CB  1 
ATOM   2821  C CG  . GLU B 1 38  ? -3.496  -5.302  22.513  1.00 64.28  ? 34  GLU E CG  1 
ATOM   2822  C CD  . GLU B 1 38  ? -4.317  -6.192  21.598  1.00 68.92  ? 34  GLU E CD  1 
ATOM   2823  O OE1 . GLU B 1 38  ? -4.731  -5.721  20.516  1.00 64.91  ? 34  GLU E OE1 1 
ATOM   2824  O OE2 . GLU B 1 38  ? -4.558  -7.361  21.969  1.00 68.38  ? 34  GLU E OE2 1 
ATOM   2825  N N   . LYS B 1 39  ? -5.526  -6.553  25.117  1.00 55.41  ? 35  LYS E N   1 
ATOM   2826  C CA  . LYS B 1 39  ? -5.316  -7.362  26.325  1.00 61.94  ? 35  LYS E CA  1 
ATOM   2827  C C   . LYS B 1 39  ? -4.383  -8.559  26.127  1.00 61.14  ? 35  LYS E C   1 
ATOM   2828  O O   . LYS B 1 39  ? -4.019  -9.214  27.101  1.00 63.77  ? 35  LYS E O   1 
ATOM   2829  C CB  . LYS B 1 39  ? -6.664  -7.863  26.834  1.00 67.09  ? 35  LYS E CB  1 
ATOM   2830  C CG  . LYS B 1 39  ? -7.471  -6.782  27.509  1.00 69.62  ? 35  LYS E CG  1 
ATOM   2831  C CD  . LYS B 1 39  ? -8.896  -7.217  27.771  1.00 73.90  ? 35  LYS E CD  1 
ATOM   2832  C CE  . LYS B 1 39  ? -9.854  -6.568  26.805  1.00 72.31  ? 35  LYS E CE  1 
ATOM   2833  N NZ  . LYS B 1 39  ? -11.224 -7.140  26.895  1.00 76.15  ? 35  LYS E NZ  1 
ATOM   2834  N N   . THR B 1 40  ? -3.989  -8.835  24.886  1.00 66.38  ? 36  THR E N   1 
ATOM   2835  C CA  . THR B 1 40  ? -3.225  -10.048 24.572  1.00 73.97  ? 36  THR E CA  1 
ATOM   2836  C C   . THR B 1 40  ? -1.775  -9.759  24.171  1.00 77.59  ? 36  THR E C   1 
ATOM   2837  O O   . THR B 1 40  ? -1.499  -8.853  23.375  1.00 73.74  ? 36  THR E O   1 
ATOM   2838  C CB  . THR B 1 40  ? -3.892  -10.872 23.449  1.00 69.34  ? 36  THR E CB  1 
ATOM   2839  O OG1 . THR B 1 40  ? -4.171  -10.026 22.326  1.00 68.68  ? 36  THR E OG1 1 
ATOM   2840  C CG2 . THR B 1 40  ? -5.184  -11.509 23.941  1.00 64.51  ? 36  THR E CG2 1 
ATOM   2841  N N   . HIS B 1 41  ? -0.859  -10.540 24.744  1.00 71.52  ? 37  HIS E N   1 
ATOM   2842  C CA  . HIS B 1 41  ? 0.554   -10.522 24.367  1.00 64.21  ? 37  HIS E CA  1 
ATOM   2843  C C   . HIS B 1 41  ? 0.989   -11.923 24.049  1.00 60.89  ? 37  HIS E C   1 
ATOM   2844  O O   . HIS B 1 41  ? 0.329   -12.886 24.447  1.00 60.80  ? 37  HIS E O   1 
ATOM   2845  C CB  . HIS B 1 41  ? 1.408   -9.944  25.492  1.00 58.83  ? 37  HIS E CB  1 
ATOM   2846  C CG  . HIS B 1 41  ? 1.291   -10.698 26.799  1.00 56.54  ? 37  HIS E CG  1 
ATOM   2847  N ND1 . HIS B 1 41  ? 2.084   -11.740 27.105  1.00 54.97  ? 37  HIS E ND1 1 
ATOM   2848  C CD2 . HIS B 1 41  ? 0.434   -10.525 27.886  1.00 57.30  ? 37  HIS E CD2 1 
ATOM   2849  C CE1 . HIS B 1 41  ? 1.759   -12.211 28.324  1.00 59.55  ? 37  HIS E CE1 1 
ATOM   2850  N NE2 . HIS B 1 41  ? 0.749   -11.465 28.804  1.00 54.74  ? 37  HIS E NE2 1 
ATOM   2851  N N   . ASN B 1 42  ? 2.104   -12.053 23.335  1.00 65.10  ? 38  ASN E N   1 
ATOM   2852  C CA  . ASN B 1 42  ? 2.573   -13.361 22.866  1.00 61.83  ? 38  ASN E CA  1 
ATOM   2853  C C   . ASN B 1 42  ? 3.449   -14.116 23.876  1.00 63.02  ? 38  ASN E C   1 
ATOM   2854  O O   . ASN B 1 42  ? 3.902   -15.224 23.598  1.00 65.58  ? 38  ASN E O   1 
ATOM   2855  C CB  . ASN B 1 42  ? 3.294   -13.222 21.516  1.00 56.66  ? 38  ASN E CB  1 
ATOM   2856  C CG  . ASN B 1 42  ? 4.649   -12.547 21.629  1.00 54.71  ? 38  ASN E CG  1 
ATOM   2857  O OD1 . ASN B 1 42  ? 5.168   -12.334 22.723  1.00 53.51  ? 38  ASN E OD1 1 
ATOM   2858  N ND2 . ASN B 1 42  ? 5.227   -12.197 20.484  1.00 56.21  ? 38  ASN E ND2 1 
ATOM   2859  N N   . GLY B 1 43  ? 3.690   -13.509 25.036  1.00 64.32  ? 39  GLY E N   1 
ATOM   2860  C CA  . GLY B 1 43  ? 4.383   -14.175 26.136  1.00 61.69  ? 39  GLY E CA  1 
ATOM   2861  C C   . GLY B 1 43  ? 5.877   -14.358 25.937  1.00 61.66  ? 39  GLY E C   1 
ATOM   2862  O O   . GLY B 1 43  ? 6.500   -15.150 26.646  1.00 56.05  ? 39  GLY E O   1 
ATOM   2863  N N   . LYS B 1 44  ? 6.458   -13.633 24.982  1.00 57.98  ? 40  LYS E N   1 
ATOM   2864  C CA  . LYS B 1 44  ? 7.869   -13.801 24.649  1.00 65.70  ? 40  LYS E CA  1 
ATOM   2865  C C   . LYS B 1 44  ? 8.563   -12.474 24.350  1.00 64.61  ? 40  LYS E C   1 
ATOM   2866  O O   . LYS B 1 44  ? 7.924   -11.509 23.938  1.00 70.67  ? 40  LYS E O   1 
ATOM   2867  C CB  . LYS B 1 44  ? 8.017   -14.746 23.449  1.00 72.07  ? 40  LYS E CB  1 
ATOM   2868  C CG  . LYS B 1 44  ? 7.663   -16.190 23.747  1.00 75.25  ? 40  LYS E CG  1 
ATOM   2869  C CD  . LYS B 1 44  ? 8.798   -16.873 24.486  1.00 79.47  ? 40  LYS E CD  1 
ATOM   2870  C CE  . LYS B 1 44  ? 8.365   -18.183 25.130  1.00 75.00  ? 40  LYS E CE  1 
ATOM   2871  N NZ  . LYS B 1 44  ? 8.493   -19.335 24.197  1.00 75.72  ? 40  LYS E NZ  1 
ATOM   2872  N N   . LEU B 1 45  ? 9.874   -12.441 24.581  1.00 59.86  ? 41  LEU E N   1 
ATOM   2873  C CA  . LEU B 1 45  ? 10.707  -11.302 24.204  1.00 57.42  ? 41  LEU E CA  1 
ATOM   2874  C C   . LEU B 1 45  ? 11.062  -11.429 22.727  1.00 57.84  ? 41  LEU E C   1 
ATOM   2875  O O   . LEU B 1 45  ? 11.290  -12.537 22.238  1.00 66.84  ? 41  LEU E O   1 
ATOM   2876  C CB  . LEU B 1 45  ? 11.979  -11.255 25.059  1.00 60.39  ? 41  LEU E CB  1 
ATOM   2877  C CG  . LEU B 1 45  ? 11.799  -11.273 26.586  1.00 62.66  ? 41  LEU E CG  1 
ATOM   2878  C CD1 . LEU B 1 45  ? 13.132  -11.045 27.281  1.00 67.79  ? 41  LEU E CD1 1 
ATOM   2879  C CD2 . LEU B 1 45  ? 10.784  -10.241 27.051  1.00 59.27  ? 41  LEU E CD2 1 
ATOM   2880  N N   . CYS B 1 46  ? 11.120  -10.298 22.029  1.00 56.84  ? 42  CYS E N   1 
ATOM   2881  C CA  . CYS B 1 46  ? 11.246  -10.281 20.572  1.00 61.31  ? 42  CYS E CA  1 
ATOM   2882  C C   . CYS B 1 46  ? 12.213  -9.217  20.084  1.00 63.60  ? 42  CYS E C   1 
ATOM   2883  O O   . CYS B 1 46  ? 12.689  -8.387  20.858  1.00 73.26  ? 42  CYS E O   1 
ATOM   2884  C CB  . CYS B 1 46  ? 9.886   -9.979  19.940  1.00 72.43  ? 42  CYS E CB  1 
ATOM   2885  S SG  . CYS B 1 46  ? 8.599   -11.218 20.192  1.00 93.56  ? 42  CYS E SG  1 
ATOM   2886  N N   . ASP B 1 47  ? 12.478  -9.243  18.781  1.00 64.47  ? 43  ASP E N   1 
ATOM   2887  C CA  . ASP B 1 47  ? 13.221  -8.183  18.107  1.00 67.23  ? 43  ASP E CA  1 
ATOM   2888  C C   . ASP B 1 47  ? 12.367  -6.922  18.067  1.00 64.82  ? 43  ASP E C   1 
ATOM   2889  O O   . ASP B 1 47  ? 11.137  -6.993  18.155  1.00 67.62  ? 43  ASP E O   1 
ATOM   2890  C CB  . ASP B 1 47  ? 13.588  -8.595  16.674  1.00 74.13  ? 43  ASP E CB  1 
ATOM   2891  C CG  . ASP B 1 47  ? 14.480  -9.833  16.621  1.00 79.61  ? 43  ASP E CG  1 
ATOM   2892  O OD1 . ASP B 1 47  ? 14.748  -10.434 17.685  1.00 77.01  ? 43  ASP E OD1 1 
ATOM   2893  O OD2 . ASP B 1 47  ? 14.912  -10.209 15.509  1.00 76.88  ? 43  ASP E OD2 1 
ATOM   2894  N N   . LEU B 1 48  ? 13.024  -5.775  17.931  1.00 58.63  ? 44  LEU E N   1 
ATOM   2895  C CA  . LEU B 1 48  ? 12.347  -4.488  17.898  1.00 61.59  ? 44  LEU E CA  1 
ATOM   2896  C C   . LEU B 1 48  ? 12.686  -3.787  16.587  1.00 62.81  ? 44  LEU E C   1 
ATOM   2897  O O   . LEU B 1 48  ? 13.798  -3.284  16.412  1.00 65.04  ? 44  LEU E O   1 
ATOM   2898  C CB  . LEU B 1 48  ? 12.764  -3.642  19.109  1.00 64.58  ? 44  LEU E CB  1 
ATOM   2899  C CG  . LEU B 1 48  ? 11.743  -2.628  19.623  1.00 64.00  ? 44  LEU E CG  1 
ATOM   2900  C CD1 . LEU B 1 48  ? 12.208  -2.054  20.951  1.00 76.78  ? 44  LEU E CD1 1 
ATOM   2901  C CD2 . LEU B 1 48  ? 11.508  -1.516  18.612  1.00 65.00  ? 44  LEU E CD2 1 
ATOM   2902  N N   . ASN B 1 49  ? 11.716  -3.758  15.674  1.00 69.87  ? 45  ASN E N   1 
ATOM   2903  C CA  . ASN B 1 49  ? 11.913  -3.234  14.318  1.00 70.53  ? 45  ASN E CA  1 
ATOM   2904  C C   . ASN B 1 49  ? 13.086  -3.907  13.597  1.00 66.74  ? 45  ASN E C   1 
ATOM   2905  O O   . ASN B 1 49  ? 13.937  -3.239  13.011  1.00 61.90  ? 45  ASN E O   1 
ATOM   2906  C CB  . ASN B 1 49  ? 12.083  -1.710  14.339  1.00 74.23  ? 45  ASN E CB  1 
ATOM   2907  C CG  . ASN B 1 49  ? 10.872  -0.997  14.914  1.00 82.62  ? 45  ASN E CG  1 
ATOM   2908  O OD1 . ASN B 1 49  ? 9.734   -1.293  14.547  1.00 85.28  ? 45  ASN E OD1 1 
ATOM   2909  N ND2 . ASN B 1 49  ? 11.111  -0.051  15.816  1.00 80.14  ? 45  ASN E ND2 1 
ATOM   2910  N N   . GLY B 1 50  ? 13.129  -5.237  13.674  1.00 67.76  ? 46  GLY E N   1 
ATOM   2911  C CA  . GLY B 1 50  ? 14.129  -6.039  12.969  1.00 73.85  ? 46  GLY E CA  1 
ATOM   2912  C C   . GLY B 1 50  ? 15.453  -6.272  13.684  1.00 71.42  ? 46  GLY E C   1 
ATOM   2913  O O   . GLY B 1 50  ? 16.298  -7.020  13.182  1.00 58.92  ? 46  GLY E O   1 
ATOM   2914  N N   . VAL B 1 51  ? 15.647  -5.641  14.843  1.00 68.30  ? 47  VAL E N   1 
ATOM   2915  C CA  . VAL B 1 51  ? 16.909  -5.755  15.579  1.00 55.68  ? 47  VAL E CA  1 
ATOM   2916  C C   . VAL B 1 51  ? 16.713  -6.514  16.887  1.00 53.98  ? 47  VAL E C   1 
ATOM   2917  O O   . VAL B 1 51  ? 15.781  -6.235  17.640  1.00 61.72  ? 47  VAL E O   1 
ATOM   2918  C CB  . VAL B 1 51  ? 17.517  -4.382  15.893  1.00 49.90  ? 47  VAL E CB  1 
ATOM   2919  C CG1 . VAL B 1 51  ? 18.878  -4.558  16.554  1.00 45.42  ? 47  VAL E CG1 1 
ATOM   2920  C CG2 . VAL B 1 51  ? 17.635  -3.551  14.624  1.00 44.45  ? 47  VAL E CG2 1 
ATOM   2921  N N   . LYS B 1 52  ? 17.625  -7.437  17.167  1.00 52.10  ? 48  LYS E N   1 
ATOM   2922  C CA  . LYS B 1 52  ? 17.507  -8.330  18.321  1.00 53.88  ? 48  LYS E CA  1 
ATOM   2923  C C   . LYS B 1 52  ? 17.911  -7.572  19.591  1.00 50.88  ? 48  LYS E C   1 
ATOM   2924  O O   . LYS B 1 52  ? 18.678  -6.615  19.523  1.00 46.58  ? 48  LYS E O   1 
ATOM   2925  C CB  . LYS B 1 52  ? 18.383  -9.595  18.163  1.00 64.24  ? 48  LYS E CB  1 
ATOM   2926  C CG  . LYS B 1 52  ? 18.754  -9.994  16.716  1.00 76.36  ? 48  LYS E CG  1 
ATOM   2927  C CD  . LYS B 1 52  ? 20.225  -9.689  16.422  1.00 87.16  ? 48  LYS E CD  1 
ATOM   2928  C CE  . LYS B 1 52  ? 20.862  -10.726 15.514  1.00 90.58  ? 48  LYS E CE  1 
ATOM   2929  N NZ  . LYS B 1 52  ? 20.097  -10.956 14.257  1.00 90.98  ? 48  LYS E NZ  1 
ATOM   2930  N N   . PRO B 1 53  ? 17.384  -7.987  20.754  1.00 52.25  ? 49  PRO E N   1 
ATOM   2931  C CA  . PRO B 1 53  ? 17.880  -7.426  22.009  1.00 54.28  ? 49  PRO E CA  1 
ATOM   2932  C C   . PRO B 1 53  ? 19.177  -8.077  22.469  1.00 59.42  ? 49  PRO E C   1 
ATOM   2933  O O   . PRO B 1 53  ? 19.464  -9.216  22.103  1.00 59.26  ? 49  PRO E O   1 
ATOM   2934  C CB  . PRO B 1 53  ? 16.769  -7.756  23.006  1.00 51.97  ? 49  PRO E CB  1 
ATOM   2935  C CG  . PRO B 1 53  ? 16.107  -8.966  22.453  1.00 47.83  ? 49  PRO E CG  1 
ATOM   2936  C CD  . PRO B 1 53  ? 16.199  -8.839  20.960  1.00 49.86  ? 49  PRO E CD  1 
ATOM   2937  N N   . LEU B 1 54  ? 19.944  -7.345  23.271  1.00 60.79  ? 50  LEU E N   1 
ATOM   2938  C CA  . LEU B 1 54  ? 21.098  -7.898  23.960  1.00 60.68  ? 50  LEU E CA  1 
ATOM   2939  C C   . LEU B 1 54  ? 20.610  -8.541  25.250  1.00 57.14  ? 50  LEU E C   1 
ATOM   2940  O O   . LEU B 1 54  ? 20.268  -7.840  26.204  1.00 61.09  ? 50  LEU E O   1 
ATOM   2941  C CB  . LEU B 1 54  ? 22.120  -6.795  24.258  1.00 67.28  ? 50  LEU E CB  1 
ATOM   2942  C CG  . LEU B 1 54  ? 23.401  -7.233  24.972  1.00 72.63  ? 50  LEU E CG  1 
ATOM   2943  C CD1 . LEU B 1 54  ? 24.136  -8.283  24.150  1.00 73.98  ? 50  LEU E CD1 1 
ATOM   2944  C CD2 . LEU B 1 54  ? 24.293  -6.029  25.248  1.00 63.59  ? 50  LEU E CD2 1 
ATOM   2945  N N   . ILE B 1 55  ? 20.576  -9.872  25.272  1.00 58.11  ? 51  ILE E N   1 
ATOM   2946  C CA  . ILE B 1 55  ? 20.103  -10.625 26.433  1.00 62.35  ? 51  ILE E CA  1 
ATOM   2947  C C   . ILE B 1 55  ? 21.287  -11.107 27.272  1.00 68.10  ? 51  ILE E C   1 
ATOM   2948  O O   . ILE B 1 55  ? 22.076  -11.941 26.830  1.00 72.23  ? 51  ILE E O   1 
ATOM   2949  C CB  . ILE B 1 55  ? 19.234  -11.828 26.006  1.00 62.50  ? 51  ILE E CB  1 
ATOM   2950  C CG1 . ILE B 1 55  ? 18.005  -11.335 25.241  1.00 66.28  ? 51  ILE E CG1 1 
ATOM   2951  C CG2 . ILE B 1 55  ? 18.785  -12.646 27.214  1.00 55.02  ? 51  ILE E CG2 1 
ATOM   2952  C CD1 . ILE B 1 55  ? 17.163  -12.445 24.654  1.00 69.34  ? 51  ILE E CD1 1 
ATOM   2953  N N   . LEU B 1 56  ? 21.399  -10.570 28.483  1.00 71.08  ? 52  LEU E N   1 
ATOM   2954  C CA  . LEU B 1 56  ? 22.465  -10.926 29.406  1.00 68.27  ? 52  LEU E CA  1 
ATOM   2955  C C   . LEU B 1 56  ? 21.887  -11.923 30.395  1.00 69.54  ? 52  LEU E C   1 
ATOM   2956  O O   . LEU B 1 56  ? 21.206  -11.536 31.338  1.00 80.48  ? 52  LEU E O   1 
ATOM   2957  C CB  . LEU B 1 56  ? 22.983  -9.681  30.133  1.00 66.27  ? 52  LEU E CB  1 
ATOM   2958  C CG  . LEU B 1 56  ? 23.422  -8.524  29.225  1.00 62.69  ? 52  LEU E CG  1 
ATOM   2959  C CD1 . LEU B 1 56  ? 23.781  -7.300  30.055  1.00 62.20  ? 52  LEU E CD1 1 
ATOM   2960  C CD2 . LEU B 1 56  ? 24.584  -8.925  28.329  1.00 57.90  ? 52  LEU E CD2 1 
ATOM   2961  N N   . LYS B 1 57  ? 22.136  -13.204 30.143  1.00 72.16  ? 53  LYS E N   1 
ATOM   2962  C CA  . LYS B 1 57  ? 21.620  -14.307 30.961  1.00 78.84  ? 53  LYS E CA  1 
ATOM   2963  C C   . LYS B 1 57  ? 21.427  -13.965 32.451  1.00 83.62  ? 53  LYS E C   1 
ATOM   2964  O O   . LYS B 1 57  ? 20.336  -13.553 32.852  1.00 87.58  ? 53  LYS E O   1 
ATOM   2965  C CB  . LYS B 1 57  ? 22.520  -15.542 30.799  1.00 88.84  ? 53  LYS E CB  1 
ATOM   2966  C CG  . LYS B 1 57  ? 22.630  -16.067 29.376  1.00 100.71 ? 53  LYS E CG  1 
ATOM   2967  C CD  . LYS B 1 57  ? 22.694  -17.579 29.348  1.00 106.95 ? 53  LYS E CD  1 
ATOM   2968  C CE  . LYS B 1 57  ? 22.655  -18.116 27.924  1.00 104.68 ? 53  LYS E CE  1 
ATOM   2969  N NZ  . LYS B 1 57  ? 23.833  -17.674 27.124  1.00 101.23 ? 53  LYS E NZ  1 
ATOM   2970  N N   . ASP B 1 58  ? 22.469  -14.136 33.265  1.00 81.31  ? 54  ASP E N   1 
ATOM   2971  C CA  . ASP B 1 58  ? 22.406  -13.803 34.691  1.00 77.65  ? 54  ASP E CA  1 
ATOM   2972  C C   . ASP B 1 58  ? 23.482  -12.767 35.046  1.00 67.34  ? 54  ASP E C   1 
ATOM   2973  O O   . ASP B 1 58  ? 23.846  -12.598 36.211  1.00 60.77  ? 54  ASP E O   1 
ATOM   2974  C CB  . ASP B 1 58  ? 22.571  -15.078 35.531  1.00 83.22  ? 54  ASP E CB  1 
ATOM   2975  C CG  . ASP B 1 58  ? 21.667  -15.100 36.757  1.00 82.04  ? 54  ASP E CG  1 
ATOM   2976  O OD1 . ASP B 1 58  ? 21.387  -14.027 37.332  1.00 78.62  ? 54  ASP E OD1 1 
ATOM   2977  O OD2 . ASP B 1 58  ? 21.238  -16.205 37.150  1.00 89.74  ? 54  ASP E OD2 1 
ATOM   2978  N N   . CYS B 1 59  ? 23.971  -12.070 34.023  1.00 64.76  ? 55  CYS E N   1 
ATOM   2979  C CA  . CYS B 1 59  ? 25.018  -11.072 34.177  1.00 66.90  ? 55  CYS E CA  1 
ATOM   2980  C C   . CYS B 1 59  ? 24.453  -9.668  34.091  1.00 62.73  ? 55  CYS E C   1 
ATOM   2981  O O   . CYS B 1 59  ? 23.508  -9.411  33.345  1.00 60.08  ? 55  CYS E O   1 
ATOM   2982  C CB  . CYS B 1 59  ? 26.083  -11.245 33.104  1.00 81.68  ? 55  CYS E CB  1 
ATOM   2983  S SG  . CYS B 1 59  ? 26.905  -12.858 33.180  1.00 104.07 ? 55  CYS E SG  1 
ATOM   2984  N N   . SER B 1 60  ? 25.053  -8.765  34.861  1.00 57.11  ? 56  SER E N   1 
ATOM   2985  C CA  . SER B 1 60  ? 24.742  -7.350  34.781  1.00 50.25  ? 56  SER E CA  1 
ATOM   2986  C C   . SER B 1 60  ? 25.543  -6.742  33.641  1.00 47.10  ? 56  SER E C   1 
ATOM   2987  O O   . SER B 1 60  ? 26.445  -7.380  33.101  1.00 47.77  ? 56  SER E O   1 
ATOM   2988  C CB  . SER B 1 60  ? 25.092  -6.655  36.092  1.00 47.84  ? 56  SER E CB  1 
ATOM   2989  O OG  . SER B 1 60  ? 26.488  -6.455  36.190  1.00 53.74  ? 56  SER E OG  1 
ATOM   2990  N N   . VAL B 1 61  ? 25.222  -5.503  33.286  1.00 49.07  ? 57  VAL E N   1 
ATOM   2991  C CA  . VAL B 1 61  ? 25.936  -4.807  32.218  1.00 47.57  ? 57  VAL E CA  1 
ATOM   2992  C C   . VAL B 1 61  ? 27.410  -4.623  32.588  1.00 50.54  ? 57  VAL E C   1 
ATOM   2993  O O   . VAL B 1 61  ? 28.294  -4.790  31.744  1.00 51.67  ? 57  VAL E O   1 
ATOM   2994  C CB  . VAL B 1 61  ? 25.298  -3.438  31.899  1.00 43.15  ? 57  VAL E CB  1 
ATOM   2995  C CG1 . VAL B 1 61  ? 26.065  -2.737  30.791  1.00 42.35  ? 57  VAL E CG1 1 
ATOM   2996  C CG2 . VAL B 1 61  ? 23.849  -3.620  31.475  1.00 44.03  ? 57  VAL E CG2 1 
ATOM   2997  N N   . ALA B 1 62  ? 27.669  -4.289  33.849  1.00 48.19  ? 58  ALA E N   1 
ATOM   2998  C CA  . ALA B 1 62  ? 29.037  -4.099  34.326  1.00 51.41  ? 58  ALA E CA  1 
ATOM   2999  C C   . ALA B 1 62  ? 29.848  -5.388  34.193  1.00 54.75  ? 58  ALA E C   1 
ATOM   3000  O O   . ALA B 1 62  ? 30.952  -5.379  33.649  1.00 51.66  ? 58  ALA E O   1 
ATOM   3001  C CB  . ALA B 1 62  ? 29.037  -3.623  35.769  1.00 51.73  ? 58  ALA E CB  1 
ATOM   3002  N N   . GLY B 1 63  ? 29.291  -6.487  34.697  1.00 53.99  ? 59  GLY E N   1 
ATOM   3003  C CA  . GLY B 1 63  ? 29.934  -7.795  34.615  1.00 52.58  ? 59  GLY E CA  1 
ATOM   3004  C C   . GLY B 1 63  ? 30.250  -8.182  33.181  1.00 55.64  ? 59  GLY E C   1 
ATOM   3005  O O   . GLY B 1 63  ? 31.334  -8.681  32.884  1.00 60.98  ? 59  GLY E O   1 
ATOM   3006  N N   . TRP B 1 64  ? 29.299  -7.939  32.291  1.00 53.77  ? 60  TRP E N   1 
ATOM   3007  C CA  . TRP B 1 64  ? 29.463  -8.254  30.879  1.00 50.32  ? 60  TRP E CA  1 
ATOM   3008  C C   . TRP B 1 64  ? 30.512  -7.396  30.217  1.00 49.86  ? 60  TRP E C   1 
ATOM   3009  O O   . TRP B 1 64  ? 31.309  -7.897  29.424  1.00 54.29  ? 60  TRP E O   1 
ATOM   3010  C CB  . TRP B 1 64  ? 28.116  -8.141  30.168  1.00 47.45  ? 60  TRP E CB  1 
ATOM   3011  C CG  . TRP B 1 64  ? 28.204  -8.007  28.676  1.00 46.34  ? 60  TRP E CG  1 
ATOM   3012  C CD1 . TRP B 1 64  ? 28.482  -9.001  27.745  1.00 51.49  ? 60  TRP E CD1 1 
ATOM   3013  C CD2 . TRP B 1 64  ? 27.999  -6.787  27.888  1.00 48.21  ? 60  TRP E CD2 1 
ATOM   3014  N NE1 . TRP B 1 64  ? 28.473  -8.488  26.470  1.00 54.61  ? 60  TRP E NE1 1 
ATOM   3015  C CE2 . TRP B 1 64  ? 28.190  -7.166  26.489  1.00 48.93  ? 60  TRP E CE2 1 
ATOM   3016  C CE3 . TRP B 1 64  ? 27.691  -5.468  28.192  1.00 50.59  ? 60  TRP E CE3 1 
ATOM   3017  C CZ2 . TRP B 1 64  ? 28.074  -6.249  25.460  1.00 49.33  ? 60  TRP E CZ2 1 
ATOM   3018  C CZ3 . TRP B 1 64  ? 27.576  -4.549  27.144  1.00 49.03  ? 60  TRP E CZ3 1 
ATOM   3019  C CH2 . TRP B 1 64  ? 27.764  -4.933  25.812  1.00 48.73  ? 60  TRP E CH2 1 
ATOM   3020  N N   . LEU B 1 65  ? 30.533  -6.104  30.535  1.00 53.64  ? 61  LEU E N   1 
ATOM   3021  C CA  . LEU B 1 65  ? 31.527  -5.184  29.965  1.00 51.90  ? 61  LEU E CA  1 
ATOM   3022  C C   . LEU B 1 65  ? 32.950  -5.503  30.415  1.00 50.09  ? 61  LEU E C   1 
ATOM   3023  O O   . LEU B 1 65  ? 33.885  -5.488  29.611  1.00 46.19  ? 61  LEU E O   1 
ATOM   3024  C CB  . LEU B 1 65  ? 31.220  -3.733  30.352  1.00 55.10  ? 61  LEU E CB  1 
ATOM   3025  C CG  . LEU B 1 65  ? 30.292  -2.921  29.457  1.00 54.24  ? 61  LEU E CG  1 
ATOM   3026  C CD1 . LEU B 1 65  ? 30.154  -1.516  30.027  1.00 52.41  ? 61  LEU E CD1 1 
ATOM   3027  C CD2 . LEU B 1 65  ? 30.826  -2.865  28.036  1.00 47.83  ? 61  LEU E CD2 1 
ATOM   3028  N N   . LEU B 1 66  ? 33.104  -5.772  31.707  1.00 51.88  ? 62  LEU E N   1 
ATOM   3029  C CA  . LEU B 1 66  ? 34.421  -5.974  32.310  1.00 59.71  ? 62  LEU E CA  1 
ATOM   3030  C C   . LEU B 1 66  ? 35.008  -7.367  32.067  1.00 56.01  ? 62  LEU E C   1 
ATOM   3031  O O   . LEU B 1 66  ? 36.222  -7.534  32.104  1.00 50.31  ? 62  LEU E O   1 
ATOM   3032  C CB  . LEU B 1 66  ? 34.358  -5.697  33.817  1.00 56.20  ? 62  LEU E CB  1 
ATOM   3033  C CG  . LEU B 1 66  ? 34.088  -4.233  34.175  1.00 53.81  ? 62  LEU E CG  1 
ATOM   3034  C CD1 . LEU B 1 66  ? 33.691  -4.090  35.639  1.00 48.69  ? 62  LEU E CD1 1 
ATOM   3035  C CD2 . LEU B 1 66  ? 35.302  -3.375  33.852  1.00 49.87  ? 62  LEU E CD2 1 
ATOM   3036  N N   . GLY B 1 67  ? 34.151  -8.359  31.834  1.00 53.70  ? 63  GLY E N   1 
ATOM   3037  C CA  . GLY B 1 67  ? 34.599  -9.725  31.565  1.00 52.89  ? 63  GLY E CA  1 
ATOM   3038  C C   . GLY B 1 67  ? 34.642  -10.628 32.786  1.00 50.52  ? 63  GLY E C   1 
ATOM   3039  O O   . GLY B 1 67  ? 35.508  -11.502 32.881  1.00 61.01  ? 63  GLY E O   1 
ATOM   3040  N N   . ASN B 1 68  ? 33.724  -10.410 33.724  1.00 47.78  ? 64  ASN E N   1 
ATOM   3041  C CA  . ASN B 1 68  ? 33.521  -11.321 34.854  1.00 55.31  ? 64  ASN E CA  1 
ATOM   3042  C C   . ASN B 1 68  ? 33.684  -12.793 34.409  1.00 70.09  ? 64  ASN E C   1 
ATOM   3043  O O   . ASN B 1 68  ? 33.039  -13.215 33.452  1.00 75.66  ? 64  ASN E O   1 
ATOM   3044  C CB  . ASN B 1 68  ? 32.129  -11.088 35.455  1.00 50.39  ? 64  ASN E CB  1 
ATOM   3045  C CG  . ASN B 1 68  ? 31.930  -11.786 36.795  1.00 52.00  ? 64  ASN E CG  1 
ATOM   3046  O OD1 . ASN B 1 68  ? 32.376  -12.916 36.998  1.00 53.04  ? 64  ASN E OD1 1 
ATOM   3047  N ND2 . ASN B 1 68  ? 31.229  -11.118 37.712  1.00 51.14  ? 64  ASN E ND2 1 
ATOM   3048  N N   . PRO B 1 69  ? 34.566  -13.567 35.083  1.00 84.10  ? 65  PRO E N   1 
ATOM   3049  C CA  . PRO B 1 69  ? 34.798  -14.982 34.737  1.00 85.01  ? 65  PRO E CA  1 
ATOM   3050  C C   . PRO B 1 69  ? 33.537  -15.855 34.698  1.00 83.61  ? 65  PRO E C   1 
ATOM   3051  O O   . PRO B 1 69  ? 33.435  -16.746 33.853  1.00 82.93  ? 65  PRO E O   1 
ATOM   3052  C CB  . PRO B 1 69  ? 35.733  -15.465 35.851  1.00 84.78  ? 65  PRO E CB  1 
ATOM   3053  C CG  . PRO B 1 69  ? 36.465  -14.244 36.269  1.00 89.07  ? 65  PRO E CG  1 
ATOM   3054  C CD  . PRO B 1 69  ? 35.473  -13.124 36.160  1.00 86.53  ? 65  PRO E CD  1 
ATOM   3055  N N   . MET B 1 70  ? 32.597  -15.594 35.604  1.00 84.80  ? 66  MET E N   1 
ATOM   3056  C CA  . MET B 1 70  ? 31.339  -16.349 35.685  1.00 88.36  ? 66  MET E CA  1 
ATOM   3057  C C   . MET B 1 70  ? 30.363  -16.037 34.543  1.00 89.23  ? 66  MET E C   1 
ATOM   3058  O O   . MET B 1 70  ? 29.366  -16.737 34.371  1.00 94.69  ? 66  MET E O   1 
ATOM   3059  C CB  . MET B 1 70  ? 30.667  -16.085 37.031  1.00 92.90  ? 66  MET E CB  1 
ATOM   3060  C CG  . MET B 1 70  ? 31.347  -16.775 38.187  1.00 102.48 ? 66  MET E CG  1 
ATOM   3061  S SD  . MET B 1 70  ? 30.822  -16.124 39.778  1.00 118.98 ? 66  MET E SD  1 
ATOM   3062  C CE  . MET B 1 70  ? 31.741  -14.586 39.837  1.00 95.67  ? 66  MET E CE  1 
ATOM   3063  N N   . CYS B 1 71  ? 30.651  -14.988 33.777  1.00 87.67  ? 67  CYS E N   1 
ATOM   3064  C CA  . CYS B 1 71  ? 29.895  -14.652 32.571  1.00 89.77  ? 67  CYS E CA  1 
ATOM   3065  C C   . CYS B 1 71  ? 30.588  -15.268 31.360  1.00 88.45  ? 67  CYS E C   1 
ATOM   3066  O O   . CYS B 1 71  ? 31.558  -16.013 31.519  1.00 91.67  ? 67  CYS E O   1 
ATOM   3067  C CB  . CYS B 1 71  ? 29.788  -13.128 32.442  1.00 91.67  ? 67  CYS E CB  1 
ATOM   3068  S SG  . CYS B 1 71  ? 28.800  -12.428 33.783  1.00 102.30 ? 67  CYS E SG  1 
ATOM   3069  N N   . ASP B 1 72  ? 30.085  -14.982 30.161  1.00 93.00  ? 68  ASP E N   1 
ATOM   3070  C CA  . ASP B 1 72  ? 30.717  -15.463 28.927  1.00 97.51  ? 68  ASP E CA  1 
ATOM   3071  C C   . ASP B 1 72  ? 30.886  -14.350 27.889  1.00 95.24  ? 68  ASP E C   1 
ATOM   3072  O O   . ASP B 1 72  ? 30.181  -13.338 27.924  1.00 86.25  ? 68  ASP E O   1 
ATOM   3073  C CB  . ASP B 1 72  ? 29.942  -16.647 28.321  1.00 95.42  ? 68  ASP E CB  1 
ATOM   3074  C CG  . ASP B 1 72  ? 28.461  -16.357 28.134  1.00 93.19  ? 68  ASP E CG  1 
ATOM   3075  O OD1 . ASP B 1 72  ? 27.741  -16.267 29.147  1.00 100.48 ? 68  ASP E OD1 1 
ATOM   3076  O OD2 . ASP B 1 72  ? 28.009  -16.242 26.976  1.00 80.07  ? 68  ASP E OD2 1 
ATOM   3077  N N   . GLU B 1 73  ? 31.834  -14.562 26.977  1.00 103.00 ? 69  GLU E N   1 
ATOM   3078  C CA  . GLU B 1 73  ? 32.116  -13.648 25.866  1.00 113.69 ? 69  GLU E CA  1 
ATOM   3079  C C   . GLU B 1 73  ? 31.476  -14.119 24.554  1.00 125.08 ? 69  GLU E C   1 
ATOM   3080  O O   . GLU B 1 73  ? 31.779  -13.575 23.490  1.00 118.70 ? 69  GLU E O   1 
ATOM   3081  C CB  . GLU B 1 73  ? 33.641  -13.471 25.679  1.00 119.38 ? 69  GLU E CB  1 
ATOM   3082  C CG  . GLU B 1 73  ? 34.398  -14.631 25.018  1.00 127.01 ? 69  GLU E CG  1 
ATOM   3083  C CD  . GLU B 1 73  ? 34.810  -15.737 25.987  1.00 125.07 ? 69  GLU E CD  1 
ATOM   3084  O OE1 . GLU B 1 73  ? 33.980  -16.635 26.252  1.00 116.33 ? 69  GLU E OE1 1 
ATOM   3085  O OE2 . GLU B 1 73  ? 35.974  -15.732 26.467  1.00 111.81 ? 69  GLU E OE2 1 
ATOM   3086  N N   . PHE B 1 74  ? 30.598  -15.123 24.628  1.00 141.87 ? 70  PHE E N   1 
ATOM   3087  C CA  . PHE B 1 74  ? 29.948  -15.700 23.434  1.00 155.10 ? 70  PHE E CA  1 
ATOM   3088  C C   . PHE B 1 74  ? 28.733  -14.895 22.938  1.00 143.52 ? 70  PHE E C   1 
ATOM   3089  O O   . PHE B 1 74  ? 27.680  -15.461 22.640  1.00 123.61 ? 70  PHE E O   1 
ATOM   3090  C CB  . PHE B 1 74  ? 29.583  -17.174 23.696  1.00 170.90 ? 70  PHE E CB  1 
ATOM   3091  C CG  . PHE B 1 74  ? 29.195  -17.943 22.459  1.00 185.18 ? 70  PHE E CG  1 
ATOM   3092  C CD1 . PHE B 1 74  ? 27.920  -18.486 22.334  1.00 186.62 ? 70  PHE E CD1 1 
ATOM   3093  C CD2 . PHE B 1 74  ? 30.103  -18.131 21.421  1.00 183.53 ? 70  PHE E CD2 1 
ATOM   3094  C CE1 . PHE B 1 74  ? 27.557  -19.196 21.201  1.00 179.42 ? 70  PHE E CE1 1 
ATOM   3095  C CE2 . PHE B 1 74  ? 29.744  -18.841 20.285  1.00 176.58 ? 70  PHE E CE2 1 
ATOM   3096  C CZ  . PHE B 1 74  ? 28.470  -19.374 20.175  1.00 176.76 ? 70  PHE E CZ  1 
ATOM   3097  N N   . ILE B 1 75  ? 28.895  -13.577 22.831  1.00 137.02 ? 71  ILE E N   1 
ATOM   3098  C CA  . ILE B 1 75  ? 27.917  -12.724 22.171  1.00 125.68 ? 71  ILE E CA  1 
ATOM   3099  C C   . ILE B 1 75  ? 28.516  -12.269 20.847  1.00 113.94 ? 71  ILE E C   1 
ATOM   3100  O O   . ILE B 1 75  ? 27.980  -12.571 19.787  1.00 108.69 ? 71  ILE E O   1 
ATOM   3101  C CB  . ILE B 1 75  ? 27.534  -11.492 23.009  1.00 115.37 ? 71  ILE E CB  1 
ATOM   3102  C CG1 . ILE B 1 75  ? 27.134  -11.905 24.436  1.00 101.29 ? 71  ILE E CG1 1 
ATOM   3103  C CG2 . ILE B 1 75  ? 26.387  -10.738 22.351  1.00 109.77 ? 71  ILE E CG2 1 
ATOM   3104  C CD1 . ILE B 1 75  ? 25.915  -12.799 24.512  1.00 93.15  ? 71  ILE E CD1 1 
ATOM   3105  N N   . ASN B 1 76  ? 29.626  -11.536 20.930  1.00 111.14 ? 72  ASN E N   1 
ATOM   3106  C CA  . ASN B 1 76  ? 30.330  -10.992 19.768  1.00 111.79 ? 72  ASN E CA  1 
ATOM   3107  C C   . ASN B 1 76  ? 29.451  -10.193 18.792  1.00 114.64 ? 72  ASN E C   1 
ATOM   3108  O O   . ASN B 1 76  ? 29.949  -9.733  17.767  1.00 105.72 ? 72  ASN E O   1 
ATOM   3109  C CB  . ASN B 1 76  ? 31.054  -12.132 19.031  1.00 112.39 ? 72  ASN E CB  1 
ATOM   3110  C CG  . ASN B 1 76  ? 32.380  -11.704 18.411  1.00 110.94 ? 72  ASN E CG  1 
ATOM   3111  O OD1 . ASN B 1 76  ? 32.805  -10.554 18.526  1.00 105.47 ? 72  ASN E OD1 1 
ATOM   3112  N ND2 . ASN B 1 76  ? 33.048  -12.648 17.758  1.00 107.97 ? 72  ASN E ND2 1 
ATOM   3113  N N   . VAL B 1 77  ? 28.173  -9.994  19.133  1.00 118.13 ? 73  VAL E N   1 
ATOM   3114  C CA  . VAL B 1 77  ? 27.197  -9.388  18.225  1.00 109.86 ? 73  VAL E CA  1 
ATOM   3115  C C   . VAL B 1 77  ? 27.252  -7.869  18.368  1.00 92.26  ? 73  VAL E C   1 
ATOM   3116  O O   . VAL B 1 77  ? 27.200  -7.362  19.488  1.00 88.21  ? 73  VAL E O   1 
ATOM   3117  C CB  . VAL B 1 77  ? 25.763  -9.877  18.514  1.00 117.95 ? 73  VAL E CB  1 
ATOM   3118  C CG1 . VAL B 1 77  ? 24.749  -9.076  17.708  1.00 125.36 ? 73  VAL E CG1 1 
ATOM   3119  C CG2 . VAL B 1 77  ? 25.636  -11.362 18.205  1.00 118.65 ? 73  VAL E CG2 1 
ATOM   3120  N N   . PRO B 1 78  ? 27.369  -7.141  17.240  1.00 86.54  ? 74  PRO E N   1 
ATOM   3121  C CA  . PRO B 1 78  ? 27.562  -5.691  17.266  1.00 92.06  ? 74  PRO E CA  1 
ATOM   3122  C C   . PRO B 1 78  ? 26.293  -4.812  17.137  1.00 100.33 ? 74  PRO E C   1 
ATOM   3123  O O   . PRO B 1 78  ? 26.411  -3.608  16.876  1.00 102.26 ? 74  PRO E O   1 
ATOM   3124  C CB  . PRO B 1 78  ? 28.515  -5.477  16.079  1.00 100.81 ? 74  PRO E CB  1 
ATOM   3125  C CG  . PRO B 1 78  ? 28.037  -6.479  15.080  1.00 103.58 ? 74  PRO E CG  1 
ATOM   3126  C CD  . PRO B 1 78  ? 27.650  -7.690  15.896  1.00 98.71  ? 74  PRO E CD  1 
ATOM   3127  N N   . GLU B 1 79  ? 25.100  -5.365  17.364  1.00 98.69  ? 75  GLU E N   1 
ATOM   3128  C CA  . GLU B 1 79  ? 23.870  -4.588  17.146  1.00 87.75  ? 75  GLU E CA  1 
ATOM   3129  C C   . GLU B 1 79  ? 22.760  -5.045  18.079  1.00 85.57  ? 75  GLU E C   1 
ATOM   3130  O O   . GLU B 1 79  ? 22.492  -6.243  18.169  1.00 87.37  ? 75  GLU E O   1 
ATOM   3131  C CB  . GLU B 1 79  ? 23.451  -4.742  15.679  1.00 87.35  ? 75  GLU E CB  1 
ATOM   3132  C CG  . GLU B 1 79  ? 22.310  -3.848  15.189  1.00 96.65  ? 75  GLU E CG  1 
ATOM   3133  C CD  . GLU B 1 79  ? 22.435  -3.454  13.721  1.00 101.39 ? 75  GLU E CD  1 
ATOM   3134  O OE1 . GLU B 1 79  ? 23.238  -4.079  12.991  1.00 100.45 ? 75  GLU E OE1 1 
ATOM   3135  O OE2 . GLU B 1 79  ? 21.727  -2.511  13.289  1.00 101.48 ? 75  GLU E OE2 1 
ATOM   3136  N N   . TRP B 1 80  ? 22.147  -4.102  18.801  1.00 71.78  ? 76  TRP E N   1 
ATOM   3137  C CA  . TRP B 1 80  ? 20.960  -4.410  19.598  1.00 69.26  ? 76  TRP E CA  1 
ATOM   3138  C C   . TRP B 1 80  ? 20.065  -3.208  19.776  1.00 59.58  ? 76  TRP E C   1 
ATOM   3139  O O   . TRP B 1 80  ? 20.496  -2.065  19.616  1.00 51.43  ? 76  TRP E O   1 
ATOM   3140  C CB  . TRP B 1 80  ? 21.345  -5.016  20.949  1.00 69.13  ? 76  TRP E CB  1 
ATOM   3141  C CG  . TRP B 1 80  ? 22.105  -4.074  21.851  1.00 80.89  ? 76  TRP E CG  1 
ATOM   3142  C CD1 . TRP B 1 80  ? 21.582  -3.107  22.703  1.00 81.63  ? 76  TRP E CD1 1 
ATOM   3143  C CD2 . TRP B 1 80  ? 23.556  -3.985  22.026  1.00 80.76  ? 76  TRP E CD2 1 
ATOM   3144  N NE1 . TRP B 1 80  ? 22.580  -2.443  23.366  1.00 79.65  ? 76  TRP E NE1 1 
ATOM   3145  C CE2 . TRP B 1 80  ? 23.785  -2.918  23.007  1.00 77.93  ? 76  TRP E CE2 1 
ATOM   3146  C CE3 . TRP B 1 80  ? 24.647  -4.649  21.488  1.00 74.29  ? 76  TRP E CE3 1 
ATOM   3147  C CZ2 . TRP B 1 80  ? 25.055  -2.556  23.412  1.00 72.46  ? 76  TRP E CZ2 1 
ATOM   3148  C CZ3 . TRP B 1 80  ? 25.921  -4.274  21.908  1.00 73.17  ? 76  TRP E CZ3 1 
ATOM   3149  C CH2 . TRP B 1 80  ? 26.117  -3.253  22.847  1.00 67.32  ? 76  TRP E CH2 1 
ATOM   3150  N N   . SER B 1 81  ? 18.802  -3.477  20.100  1.00 54.43  ? 77  SER E N   1 
ATOM   3151  C CA  . SER B 1 81  ? 17.770  -2.443  20.215  1.00 55.98  ? 77  SER E CA  1 
ATOM   3152  C C   . SER B 1 81  ? 17.417  -2.122  21.670  1.00 47.69  ? 77  SER E C   1 
ATOM   3153  O O   . SER B 1 81  ? 17.065  -0.993  21.984  1.00 49.20  ? 77  SER E O   1 
ATOM   3154  C CB  . SER B 1 81  ? 16.514  -2.887  19.470  1.00 57.24  ? 77  SER E CB  1 
ATOM   3155  O OG  . SER B 1 81  ? 16.114  -4.180  19.893  1.00 60.06  ? 77  SER E OG  1 
ATOM   3156  N N   . TYR B 1 82  ? 17.482  -3.125  22.538  1.00 45.71  ? 78  TYR E N   1 
ATOM   3157  C CA  . TYR B 1 82  ? 17.348  -2.922  23.978  1.00 46.21  ? 78  TYR E CA  1 
ATOM   3158  C C   . TYR B 1 82  ? 18.123  -4.006  24.723  1.00 46.82  ? 78  TYR E C   1 
ATOM   3159  O O   . TYR B 1 82  ? 18.604  -4.954  24.108  1.00 52.95  ? 78  TYR E O   1 
ATOM   3160  C CB  . TYR B 1 82  ? 15.873  -2.888  24.401  1.00 47.90  ? 78  TYR E CB  1 
ATOM   3161  C CG  . TYR B 1 82  ? 15.084  -4.156  24.145  1.00 43.23  ? 78  TYR E CG  1 
ATOM   3162  C CD1 . TYR B 1 82  ? 14.761  -5.018  25.187  1.00 44.90  ? 78  TYR E CD1 1 
ATOM   3163  C CD2 . TYR B 1 82  ? 14.638  -4.475  22.866  1.00 41.45  ? 78  TYR E CD2 1 
ATOM   3164  C CE1 . TYR B 1 82  ? 14.032  -6.173  24.963  1.00 41.53  ? 78  TYR E CE1 1 
ATOM   3165  C CE2 . TYR B 1 82  ? 13.908  -5.627  22.630  1.00 42.13  ? 78  TYR E CE2 1 
ATOM   3166  C CZ  . TYR B 1 82  ? 13.609  -6.473  23.682  1.00 44.03  ? 78  TYR E CZ  1 
ATOM   3167  O OH  . TYR B 1 82  ? 12.888  -7.621  23.453  1.00 52.31  ? 78  TYR E OH  1 
ATOM   3168  N N   . ILE B 1 83  ? 18.257  -3.849  26.036  1.00 42.68  ? 79  ILE E N   1 
ATOM   3169  C CA  . ILE B 1 83  ? 19.031  -4.777  26.853  1.00 39.22  ? 79  ILE E CA  1 
ATOM   3170  C C   . ILE B 1 83  ? 18.128  -5.462  27.864  1.00 43.45  ? 79  ILE E C   1 
ATOM   3171  O O   . ILE B 1 83  ? 17.291  -4.811  28.489  1.00 47.50  ? 79  ILE E O   1 
ATOM   3172  C CB  . ILE B 1 83  ? 20.151  -4.048  27.620  1.00 41.30  ? 79  ILE E CB  1 
ATOM   3173  C CG1 . ILE B 1 83  ? 21.219  -3.536  26.654  1.00 44.39  ? 79  ILE E CG1 1 
ATOM   3174  C CG2 . ILE B 1 83  ? 20.790  -4.973  28.648  1.00 37.05  ? 79  ILE E CG2 1 
ATOM   3175  C CD1 . ILE B 1 83  ? 22.332  -2.748  27.315  1.00 41.31  ? 79  ILE E CD1 1 
ATOM   3176  N N   . VAL B 1 84  ? 18.305  -6.771  28.030  1.00 45.60  ? 80  VAL E N   1 
ATOM   3177  C CA  . VAL B 1 84  ? 17.539  -7.532  29.006  1.00 47.62  ? 80  VAL E CA  1 
ATOM   3178  C C   . VAL B 1 84  ? 18.435  -8.067  30.121  1.00 54.27  ? 80  VAL E C   1 
ATOM   3179  O O   . VAL B 1 84  ? 19.319  -8.884  29.878  1.00 63.55  ? 80  VAL E O   1 
ATOM   3180  C CB  . VAL B 1 84  ? 16.805  -8.702  28.336  1.00 46.27  ? 80  VAL E CB  1 
ATOM   3181  C CG1 . VAL B 1 84  ? 15.821  -9.332  29.312  1.00 46.47  ? 80  VAL E CG1 1 
ATOM   3182  C CG2 . VAL B 1 84  ? 16.106  -8.223  27.073  1.00 47.16  ? 80  VAL E CG2 1 
ATOM   3183  N N   . GLU B 1 85  ? 18.208  -7.571  31.335  1.00 55.61  ? 81  GLU E N   1 
ATOM   3184  C CA  . GLU B 1 85  ? 18.831  -8.095  32.546  1.00 54.49  ? 81  GLU E CA  1 
ATOM   3185  C C   . GLU B 1 85  ? 17.759  -8.804  33.348  1.00 55.36  ? 81  GLU E C   1 
ATOM   3186  O O   . GLU B 1 85  ? 16.571  -8.574  33.131  1.00 59.89  ? 81  GLU E O   1 
ATOM   3187  C CB  . GLU B 1 85  ? 19.389  -6.962  33.413  1.00 59.51  ? 81  GLU E CB  1 
ATOM   3188  C CG  . GLU B 1 85  ? 20.669  -6.299  32.928  1.00 61.39  ? 81  GLU E CG  1 
ATOM   3189  C CD  . GLU B 1 85  ? 21.199  -5.279  33.929  1.00 68.15  ? 81  GLU E CD  1 
ATOM   3190  O OE1 . GLU B 1 85  ? 20.385  -4.631  34.619  1.00 75.26  ? 81  GLU E OE1 1 
ATOM   3191  O OE2 . GLU B 1 85  ? 22.430  -5.117  34.036  1.00 70.26  ? 81  GLU E OE2 1 
ATOM   3192  N N   . LYS B 1 86  ? 18.175  -9.646  34.286  1.00 56.39  ? 82  LYS E N   1 
ATOM   3193  C CA  . LYS B 1 86  ? 17.256  -10.174 35.285  1.00 62.74  ? 82  LYS E CA  1 
ATOM   3194  C C   . LYS B 1 86  ? 17.104  -9.122  36.379  1.00 60.53  ? 82  LYS E C   1 
ATOM   3195  O O   . LYS B 1 86  ? 17.870  -8.155  36.431  1.00 60.80  ? 82  LYS E O   1 
ATOM   3196  C CB  . LYS B 1 86  ? 17.772  -11.486 35.892  1.00 75.81  ? 82  LYS E CB  1 
ATOM   3197  C CG  . LYS B 1 86  ? 17.951  -12.643 34.925  1.00 83.31  ? 82  LYS E CG  1 
ATOM   3198  C CD  . LYS B 1 86  ? 17.728  -13.997 35.571  1.00 89.83  ? 82  LYS E CD  1 
ATOM   3199  C CE  . LYS B 1 86  ? 17.904  -15.110 34.553  1.00 90.64  ? 82  LYS E CE  1 
ATOM   3200  N NZ  . LYS B 1 86  ? 17.465  -16.433 35.081  1.00 93.75  ? 82  LYS E NZ  1 
ATOM   3201  N N   . ALA B 1 87  ? 16.121  -9.316  37.256  1.00 61.03  ? 83  ALA E N   1 
ATOM   3202  C CA  . ALA B 1 87  ? 15.862  -8.380  38.354  1.00 57.44  ? 83  ALA E CA  1 
ATOM   3203  C C   . ALA B 1 87  ? 17.099  -8.184  39.231  1.00 61.50  ? 83  ALA E C   1 
ATOM   3204  O O   . ALA B 1 87  ? 17.455  -7.054  39.559  1.00 63.33  ? 83  ALA E O   1 
ATOM   3205  C CB  . ALA B 1 87  ? 14.689  -8.858  39.199  1.00 47.88  ? 83  ALA E CB  1 
ATOM   3206  N N   . ASN B 1 88  ? 17.744  -9.288  39.601  1.00 66.74  ? 84  ASN E N   1 
ATOM   3207  C CA  . ASN B 1 88  ? 18.956  -9.255  40.421  1.00 68.01  ? 84  ASN E CA  1 
ATOM   3208  C C   . ASN B 1 88  ? 20.011  -10.208 39.869  1.00 65.70  ? 84  ASN E C   1 
ATOM   3209  O O   . ASN B 1 88  ? 20.086  -11.358 40.303  1.00 77.74  ? 84  ASN E O   1 
ATOM   3210  C CB  . ASN B 1 88  ? 18.626  -9.642  41.865  1.00 73.98  ? 84  ASN E CB  1 
ATOM   3211  C CG  . ASN B 1 88  ? 17.606  -8.721  42.495  1.00 75.44  ? 84  ASN E CG  1 
ATOM   3212  O OD1 . ASN B 1 88  ? 17.878  -7.543  42.730  1.00 84.95  ? 84  ASN E OD1 1 
ATOM   3213  N ND2 . ASN B 1 88  ? 16.424  -9.257  42.780  1.00 80.03  ? 84  ASN E ND2 1 
ATOM   3214  N N   . PRO B 1 89  ? 20.824  -9.746  38.900  1.00 62.62  ? 85  PRO E N   1 
ATOM   3215  C CA  . PRO B 1 89  ? 21.834  -10.623 38.300  1.00 62.77  ? 85  PRO E CA  1 
ATOM   3216  C C   . PRO B 1 89  ? 22.826  -11.136 39.338  1.00 71.00  ? 85  PRO E C   1 
ATOM   3217  O O   . PRO B 1 89  ? 23.254  -10.372 40.210  1.00 71.21  ? 85  PRO E O   1 
ATOM   3218  C CB  . PRO B 1 89  ? 22.542  -9.719  37.283  1.00 59.32  ? 85  PRO E CB  1 
ATOM   3219  C CG  . PRO B 1 89  ? 21.604  -8.592  37.036  1.00 58.87  ? 85  PRO E CG  1 
ATOM   3220  C CD  . PRO B 1 89  ? 20.858  -8.393  38.319  1.00 61.08  ? 85  PRO E CD  1 
ATOM   3221  N N   . ALA B 1 90  ? 23.166  -12.420 39.251  1.00 67.63  ? 86  ALA E N   1 
ATOM   3222  C CA  . ALA B 1 90  ? 24.073  -13.051 40.210  1.00 65.79  ? 86  ALA E CA  1 
ATOM   3223  C C   . ALA B 1 90  ? 25.524  -12.671 39.948  1.00 61.18  ? 86  ALA E C   1 
ATOM   3224  O O   . ALA B 1 90  ? 26.327  -12.616 40.876  1.00 58.89  ? 86  ALA E O   1 
ATOM   3225  C CB  . ALA B 1 90  ? 23.914  -14.564 40.171  1.00 68.78  ? 86  ALA E CB  1 
ATOM   3226  N N   . ASN B 1 91  ? 25.852  -12.424 38.682  1.00 64.88  ? 87  ASN E N   1 
ATOM   3227  C CA  . ASN B 1 91  ? 27.218  -12.108 38.276  1.00 64.93  ? 87  ASN E CA  1 
ATOM   3228  C C   . ASN B 1 91  ? 27.364  -10.634 37.912  1.00 66.10  ? 87  ASN E C   1 
ATOM   3229  O O   . ASN B 1 91  ? 27.231  -10.250 36.747  1.00 60.70  ? 87  ASN E O   1 
ATOM   3230  C CB  . ASN B 1 91  ? 27.638  -12.993 37.097  1.00 68.43  ? 87  ASN E CB  1 
ATOM   3231  C CG  . ASN B 1 91  ? 27.420  -14.473 37.368  1.00 72.55  ? 87  ASN E CG  1 
ATOM   3232  O OD1 . ASN B 1 91  ? 26.989  -15.214 36.486  1.00 81.60  ? 87  ASN E OD1 1 
ATOM   3233  N ND2 . ASN B 1 91  ? 27.712  -14.909 38.591  1.00 63.54  ? 87  ASN E ND2 1 
ATOM   3234  N N   . ASP B 1 92  ? 27.649  -9.815  38.922  1.00 67.22  ? 88  ASP E N   1 
ATOM   3235  C CA  . ASP B 1 92  ? 27.818  -8.377  38.741  1.00 68.88  ? 88  ASP E CA  1 
ATOM   3236  C C   . ASP B 1 92  ? 29.315  -8.034  38.830  1.00 65.33  ? 88  ASP E C   1 
ATOM   3237  O O   . ASP B 1 92  ? 30.057  -8.268  37.873  1.00 65.04  ? 88  ASP E O   1 
ATOM   3238  C CB  . ASP B 1 92  ? 26.951  -7.625  39.769  1.00 73.74  ? 88  ASP E CB  1 
ATOM   3239  C CG  . ASP B 1 92  ? 26.873  -6.124  39.508  1.00 77.89  ? 88  ASP E CG  1 
ATOM   3240  O OD1 . ASP B 1 92  ? 27.384  -5.645  38.473  1.00 81.69  ? 88  ASP E OD1 1 
ATOM   3241  O OD2 . ASP B 1 92  ? 26.286  -5.418  40.354  1.00 85.71  ? 88  ASP E OD2 1 
ATOM   3242  N N   . LEU B 1 93  ? 29.760  -7.498  39.966  1.00 64.14  ? 89  LEU E N   1 
ATOM   3243  C CA  . LEU B 1 93  ? 31.175  -7.239  40.203  1.00 60.73  ? 89  LEU E CA  1 
ATOM   3244  C C   . LEU B 1 93  ? 31.718  -8.331  41.125  1.00 56.82  ? 89  LEU E C   1 
ATOM   3245  O O   . LEU B 1 93  ? 31.503  -8.285  42.334  1.00 50.74  ? 89  LEU E O   1 
ATOM   3246  C CB  . LEU B 1 93  ? 31.362  -5.860  40.843  1.00 58.38  ? 89  LEU E CB  1 
ATOM   3247  C CG  . LEU B 1 93  ? 30.950  -4.643  40.007  1.00 52.18  ? 89  LEU E CG  1 
ATOM   3248  C CD1 . LEU B 1 93  ? 31.013  -3.371  40.839  1.00 47.48  ? 89  LEU E CD1 1 
ATOM   3249  C CD2 . LEU B 1 93  ? 31.823  -4.512  38.772  1.00 49.55  ? 89  LEU E CD2 1 
ATOM   3250  N N   . CYS B 1 94  ? 32.409  -9.316  40.551  1.00 59.32  ? 90  CYS E N   1 
ATOM   3251  C CA  . CYS B 1 94  ? 32.913  -10.451 41.330  1.00 60.29  ? 90  CYS E CA  1 
ATOM   3252  C C   . CYS B 1 94  ? 33.830  -9.969  42.449  1.00 51.86  ? 90  CYS E C   1 
ATOM   3253  O O   . CYS B 1 94  ? 33.668  -10.368 43.603  1.00 46.97  ? 90  CYS E O   1 
ATOM   3254  C CB  . CYS B 1 94  ? 33.627  -11.475 40.436  1.00 67.41  ? 90  CYS E CB  1 
ATOM   3255  S SG  . CYS B 1 94  ? 35.015  -10.840 39.471  1.00 84.07  ? 90  CYS E SG  1 
ATOM   3256  N N   . TYR B 1 95  ? 34.779  -9.101  42.104  1.00 50.95  ? 91  TYR E N   1 
ATOM   3257  C CA  . TYR B 1 95  ? 35.544  -8.371  43.107  1.00 51.32  ? 91  TYR E CA  1 
ATOM   3258  C C   . TYR B 1 95  ? 34.732  -7.136  43.485  1.00 46.73  ? 91  TYR E C   1 
ATOM   3259  O O   . TYR B 1 95  ? 34.372  -6.347  42.611  1.00 49.03  ? 91  TYR E O   1 
ATOM   3260  C CB  . TYR B 1 95  ? 36.924  -7.964  42.578  1.00 53.31  ? 91  TYR E CB  1 
ATOM   3261  C CG  . TYR B 1 95  ? 37.893  -7.587  43.679  1.00 52.75  ? 91  TYR E CG  1 
ATOM   3262  C CD1 . TYR B 1 95  ? 38.801  -8.512  44.180  1.00 51.87  ? 91  TYR E CD1 1 
ATOM   3263  C CD2 . TYR B 1 95  ? 37.884  -6.315  44.236  1.00 56.62  ? 91  TYR E CD2 1 
ATOM   3264  C CE1 . TYR B 1 95  ? 39.681  -8.177  45.198  1.00 53.41  ? 91  TYR E CE1 1 
ATOM   3265  C CE2 . TYR B 1 95  ? 38.761  -5.972  45.253  1.00 60.53  ? 91  TYR E CE2 1 
ATOM   3266  C CZ  . TYR B 1 95  ? 39.659  -6.906  45.727  1.00 55.30  ? 91  TYR E CZ  1 
ATOM   3267  O OH  . TYR B 1 95  ? 40.527  -6.566  46.736  1.00 57.68  ? 91  TYR E OH  1 
ATOM   3268  N N   . PRO B 1 96  ? 34.442  -6.960  44.785  1.00 40.32  ? 92  PRO E N   1 
ATOM   3269  C CA  . PRO B 1 96  ? 33.515  -5.909  45.212  1.00 38.59  ? 92  PRO E CA  1 
ATOM   3270  C C   . PRO B 1 96  ? 34.031  -4.494  44.947  1.00 41.62  ? 92  PRO E C   1 
ATOM   3271  O O   . PRO B 1 96  ? 35.243  -4.283  44.865  1.00 44.57  ? 92  PRO E O   1 
ATOM   3272  C CB  . PRO B 1 96  ? 33.372  -6.164  46.717  1.00 36.06  ? 92  PRO E CB  1 
ATOM   3273  C CG  . PRO B 1 96  ? 34.648  -6.815  47.107  1.00 37.37  ? 92  PRO E CG  1 
ATOM   3274  C CD  . PRO B 1 96  ? 35.040  -7.664  45.933  1.00 38.30  ? 92  PRO E CD  1 
ATOM   3275  N N   . GLY B 1 97  ? 33.109  -3.542  44.809  1.00 47.37  ? 93  GLY E N   1 
ATOM   3276  C CA  . GLY B 1 97  ? 33.463  -2.142  44.565  1.00 48.08  ? 93  GLY E CA  1 
ATOM   3277  C C   . GLY B 1 97  ? 32.359  -1.335  43.905  1.00 48.17  ? 93  GLY E C   1 
ATOM   3278  O O   . GLY B 1 97  ? 31.187  -1.699  43.972  1.00 47.96  ? 93  GLY E O   1 
ATOM   3279  N N   . ASN B 1 98  ? 32.747  -0.234  43.266  1.00 51.72  ? 94  ASN E N   1 
ATOM   3280  C CA  . ASN B 1 98  ? 31.807  0.678   42.624  1.00 48.17  ? 94  ASN E CA  1 
ATOM   3281  C C   . ASN B 1 98  ? 32.070  0.813   41.140  1.00 42.35  ? 94  ASN E C   1 
ATOM   3282  O O   . ASN B 1 98  ? 33.162  0.517   40.658  1.00 41.73  ? 94  ASN E O   1 
ATOM   3283  C CB  . ASN B 1 98  ? 31.890  2.067   43.262  1.00 57.59  ? 94  ASN E CB  1 
ATOM   3284  C CG  . ASN B 1 98  ? 31.220  2.134   44.623  1.00 63.91  ? 94  ASN E CG  1 
ATOM   3285  O OD1 . ASN B 1 98  ? 30.632  1.162   45.093  1.00 74.08  ? 94  ASN E OD1 1 
ATOM   3286  N ND2 . ASN B 1 98  ? 31.316  3.289   45.269  1.00 71.77  ? 94  ASN E ND2 1 
ATOM   3287  N N   . PHE B 1 99  ? 31.040  1.244   40.422  1.00 40.84  ? 95  PHE E N   1 
ATOM   3288  C CA  . PHE B 1 99  ? 31.148  1.586   39.013  1.00 38.44  ? 95  PHE E CA  1 
ATOM   3289  C C   . PHE B 1 99  ? 30.618  3.006   38.880  1.00 37.47  ? 95  PHE E C   1 
ATOM   3290  O O   . PHE B 1 99  ? 29.444  3.257   39.132  1.00 41.56  ? 95  PHE E O   1 
ATOM   3291  C CB  . PHE B 1 99  ? 30.331  0.604   38.167  1.00 35.77  ? 95  PHE E CB  1 
ATOM   3292  C CG  . PHE B 1 99  ? 30.780  0.508   36.739  1.00 34.21  ? 95  PHE E CG  1 
ATOM   3293  C CD1 . PHE B 1 99  ? 31.294  -0.681  36.239  1.00 38.87  ? 95  PHE E CD1 1 
ATOM   3294  C CD2 . PHE B 1 99  ? 30.704  1.602   35.894  1.00 37.82  ? 95  PHE E CD2 1 
ATOM   3295  C CE1 . PHE B 1 99  ? 31.719  -0.781  34.922  1.00 38.56  ? 95  PHE E CE1 1 
ATOM   3296  C CE2 . PHE B 1 99  ? 31.127  1.511   34.577  1.00 41.16  ? 95  PHE E CE2 1 
ATOM   3297  C CZ  . PHE B 1 99  ? 31.633  0.317   34.089  1.00 37.68  ? 95  PHE E CZ  1 
ATOM   3298  N N   . ASN B 1 100 ? 31.490  3.939   38.516  1.00 37.77  ? 96  ASN E N   1 
ATOM   3299  C CA  . ASN B 1 100 ? 31.125  5.350   38.471  1.00 37.42  ? 96  ASN E CA  1 
ATOM   3300  C C   . ASN B 1 100 ? 30.196  5.662   37.305  1.00 41.18  ? 96  ASN E C   1 
ATOM   3301  O O   . ASN B 1 100 ? 30.427  5.200   36.184  1.00 38.73  ? 96  ASN E O   1 
ATOM   3302  C CB  . ASN B 1 100 ? 32.369  6.229   38.371  1.00 36.47  ? 96  ASN E CB  1 
ATOM   3303  C CG  . ASN B 1 100 ? 32.064  7.685   38.641  1.00 37.51  ? 96  ASN E CG  1 
ATOM   3304  O OD1 . ASN B 1 100 ? 31.678  8.039   39.747  1.00 45.59  ? 96  ASN E OD1 1 
ATOM   3305  N ND2 . ASN B 1 100 ? 32.216  8.533   37.628  1.00 35.43  ? 96  ASN E ND2 1 
ATOM   3306  N N   . ASP B 1 101 ? 29.160  6.459   37.581  1.00 43.50  ? 97  ASP E N   1 
ATOM   3307  C CA  . ASP B 1 101 ? 28.154  6.838   36.585  1.00 39.97  ? 97  ASP E CA  1 
ATOM   3308  C C   . ASP B 1 101 ? 27.629  5.611   35.846  1.00 36.92  ? 97  ASP E C   1 
ATOM   3309  O O   . ASP B 1 101 ? 27.502  5.619   34.621  1.00 36.72  ? 97  ASP E O   1 
ATOM   3310  C CB  . ASP B 1 101 ? 28.726  7.868   35.597  1.00 46.79  ? 97  ASP E CB  1 
ATOM   3311  C CG  . ASP B 1 101 ? 28.968  9.231   36.235  1.00 56.07  ? 97  ASP E CG  1 
ATOM   3312  O OD1 . ASP B 1 101 ? 28.269  9.586   37.209  1.00 59.94  ? 97  ASP E OD1 1 
ATOM   3313  O OD2 . ASP B 1 101 ? 29.856  9.960   35.744  1.00 65.27  ? 97  ASP E OD2 1 
ATOM   3314  N N   . TYR B 1 102 ? 27.333  4.561   36.607  1.00 34.23  ? 98  TYR E N   1 
ATOM   3315  C CA  . TYR B 1 102 ? 26.910  3.280   36.050  1.00 36.24  ? 98  TYR E CA  1 
ATOM   3316  C C   . TYR B 1 102 ? 25.609  3.405   35.277  1.00 37.57  ? 98  TYR E C   1 
ATOM   3317  O O   . TYR B 1 102 ? 25.493  2.888   34.167  1.00 40.18  ? 98  TYR E O   1 
ATOM   3318  C CB  . TYR B 1 102 ? 26.747  2.248   37.171  1.00 37.35  ? 98  TYR E CB  1 
ATOM   3319  C CG  . TYR B 1 102 ? 26.398  0.839   36.727  1.00 39.89  ? 98  TYR E CG  1 
ATOM   3320  C CD1 . TYR B 1 102 ? 26.900  0.301   35.538  1.00 39.46  ? 98  TYR E CD1 1 
ATOM   3321  C CD2 . TYR B 1 102 ? 25.592  0.027   37.520  1.00 40.79  ? 98  TYR E CD2 1 
ATOM   3322  C CE1 . TYR B 1 102 ? 26.587  -0.992  35.147  1.00 40.10  ? 98  TYR E CE1 1 
ATOM   3323  C CE2 . TYR B 1 102 ? 25.277  -1.268  37.136  1.00 44.17  ? 98  TYR E CE2 1 
ATOM   3324  C CZ  . TYR B 1 102 ? 25.777  -1.772  35.951  1.00 44.71  ? 98  TYR E CZ  1 
ATOM   3325  O OH  . TYR B 1 102 ? 25.463  -3.056  35.573  1.00 53.44  ? 98  TYR E OH  1 
ATOM   3326  N N   . GLU B 1 103 ? 24.644  4.105   35.869  1.00 40.09  ? 99  GLU E N   1 
ATOM   3327  C CA  . GLU B 1 103 ? 23.300  4.219   35.302  1.00 37.97  ? 99  GLU E CA  1 
ATOM   3328  C C   . GLU B 1 103 ? 23.302  4.978   33.981  1.00 37.25  ? 99  GLU E C   1 
ATOM   3329  O O   . GLU B 1 103 ? 22.587  4.604   33.051  1.00 47.07  ? 99  GLU E O   1 
ATOM   3330  C CB  . GLU B 1 103 ? 22.343  4.888   36.291  1.00 39.43  ? 99  GLU E CB  1 
ATOM   3331  C CG  . GLU B 1 103 ? 22.026  4.051   37.529  1.00 44.53  ? 99  GLU E CG  1 
ATOM   3332  C CD  . GLU B 1 103 ? 23.126  4.054   38.582  1.00 50.76  ? 99  GLU E CD  1 
ATOM   3333  O OE1 . GLU B 1 103 ? 24.056  4.889   38.501  1.00 52.20  ? 99  GLU E OE1 1 
ATOM   3334  O OE2 . GLU B 1 103 ? 23.054  3.214   39.503  1.00 62.50  ? 99  GLU E OE2 1 
ATOM   3335  N N   . GLU B 1 104 ? 24.113  6.029   33.890  1.00 38.19  ? 100 GLU E N   1 
ATOM   3336  C CA  . GLU B 1 104 ? 24.268  6.766   32.634  1.00 44.69  ? 100 GLU E CA  1 
ATOM   3337  C C   . GLU B 1 104 ? 24.935  5.903   31.554  1.00 48.66  ? 100 GLU E C   1 
ATOM   3338  O O   . GLU B 1 104 ? 24.588  6.010   30.377  1.00 49.92  ? 100 GLU E O   1 
ATOM   3339  C CB  . GLU B 1 104 ? 25.055  8.068   32.848  1.00 45.77  ? 100 GLU E CB  1 
ATOM   3340  C CG  . GLU B 1 104 ? 24.232  9.197   33.462  1.00 50.49  ? 100 GLU E CG  1 
ATOM   3341  C CD  . GLU B 1 104 ? 23.146  9.731   32.533  1.00 56.65  ? 100 GLU E CD  1 
ATOM   3342  O OE1 . GLU B 1 104 ? 23.452  10.046  31.358  1.00 58.40  ? 100 GLU E OE1 1 
ATOM   3343  O OE2 . GLU B 1 104 ? 21.980  9.837   32.977  1.00 47.23  ? 100 GLU E OE2 1 
ATOM   3344  N N   . LEU B 1 105 ? 25.867  5.038   31.955  1.00 45.70  ? 101 LEU E N   1 
ATOM   3345  C CA  . LEU B 1 105 ? 26.506  4.123   31.010  1.00 48.20  ? 101 LEU E CA  1 
ATOM   3346  C C   . LEU B 1 105 ? 25.527  3.065   30.505  1.00 46.63  ? 101 LEU E C   1 
ATOM   3347  O O   . LEU B 1 105 ? 25.519  2.745   29.315  1.00 40.86  ? 101 LEU E O   1 
ATOM   3348  C CB  . LEU B 1 105 ? 27.732  3.444   31.626  1.00 47.69  ? 101 LEU E CB  1 
ATOM   3349  C CG  . LEU B 1 105 ? 28.515  2.531   30.675  1.00 48.18  ? 101 LEU E CG  1 
ATOM   3350  C CD1 . LEU B 1 105 ? 28.934  3.302   29.431  1.00 48.59  ? 101 LEU E CD1 1 
ATOM   3351  C CD2 . LEU B 1 105 ? 29.720  1.909   31.365  1.00 51.02  ? 101 LEU E CD2 1 
ATOM   3352  N N   . LYS B 1 106 ? 24.719  2.513   31.407  1.00 47.49  ? 102 LYS E N   1 
ATOM   3353  C CA  . LYS B 1 106 ? 23.683  1.556   31.013  1.00 46.32  ? 102 LYS E CA  1 
ATOM   3354  C C   . LYS B 1 106 ? 22.743  2.208   30.016  1.00 41.27  ? 102 LYS E C   1 
ATOM   3355  O O   . LYS B 1 106 ? 22.414  1.621   28.992  1.00 41.46  ? 102 LYS E O   1 
ATOM   3356  C CB  . LYS B 1 106 ? 22.884  1.065   32.219  1.00 46.74  ? 102 LYS E CB  1 
ATOM   3357  C CG  . LYS B 1 106 ? 23.646  0.126   33.134  1.00 50.05  ? 102 LYS E CG  1 
ATOM   3358  C CD  . LYS B 1 106 ? 22.913  -0.097  34.452  1.00 55.98  ? 102 LYS E CD  1 
ATOM   3359  C CE  . LYS B 1 106 ? 21.983  -1.294  34.402  1.00 58.99  ? 102 LYS E CE  1 
ATOM   3360  N NZ  . LYS B 1 106 ? 21.421  -1.565  35.755  1.00 62.49  ? 102 LYS E NZ  1 
ATOM   3361  N N   . HIS B 1 107 ? 22.326  3.433   30.312  1.00 39.34  ? 103 HIS E N   1 
ATOM   3362  C CA  . HIS B 1 107 ? 21.415  4.139   29.429  1.00 41.57  ? 103 HIS E CA  1 
ATOM   3363  C C   . HIS B 1 107 ? 22.030  4.325   28.074  1.00 43.31  ? 103 HIS E C   1 
ATOM   3364  O O   . HIS B 1 107 ? 21.389  4.064   27.056  1.00 42.11  ? 103 HIS E O   1 
ATOM   3365  C CB  . HIS B 1 107 ? 21.012  5.486   30.012  1.00 38.31  ? 103 HIS E CB  1 
ATOM   3366  C CG  . HIS B 1 107 ? 19.951  6.187   29.210  1.00 39.05  ? 103 HIS E CG  1 
ATOM   3367  N ND1 . HIS B 1 107 ? 18.675  5.758   29.172  1.00 38.18  ? 103 HIS E ND1 1 
ATOM   3368  C CD2 . HIS B 1 107 ? 20.020  7.304   28.378  1.00 39.62  ? 103 HIS E CD2 1 
ATOM   3369  C CE1 . HIS B 1 107 ? 17.960  6.567   28.366  1.00 41.95  ? 103 HIS E CE1 1 
ATOM   3370  N NE2 . HIS B 1 107 ? 18.784  7.512   27.882  1.00 42.63  ? 103 HIS E NE2 1 
ATOM   3371  N N   . LEU B 1 108 ? 23.281  4.771   28.050  1.00 46.83  ? 104 LEU E N   1 
ATOM   3372  C CA  . LEU B 1 108 ? 23.989  4.987   26.794  1.00 47.89  ? 104 LEU E CA  1 
ATOM   3373  C C   . LEU B 1 108 ? 24.103  3.697   25.982  1.00 47.24  ? 104 LEU E C   1 
ATOM   3374  O O   . LEU B 1 108 ? 23.956  3.717   24.765  1.00 54.18  ? 104 LEU E O   1 
ATOM   3375  C CB  . LEU B 1 108 ? 25.382  5.561   27.055  1.00 48.30  ? 104 LEU E CB  1 
ATOM   3376  C CG  . LEU B 1 108 ? 26.140  6.035   25.812  1.00 50.80  ? 104 LEU E CG  1 
ATOM   3377  C CD1 . LEU B 1 108 ? 25.794  7.482   25.483  1.00 53.17  ? 104 LEU E CD1 1 
ATOM   3378  C CD2 . LEU B 1 108 ? 27.636  5.877   26.025  1.00 50.96  ? 104 LEU E CD2 1 
ATOM   3379  N N   . LEU B 1 109 ? 24.348  2.582   26.661  1.00 45.49  ? 105 LEU E N   1 
ATOM   3380  C CA  . LEU B 1 109 ? 24.524  1.286   26.001  1.00 44.27  ? 105 LEU E CA  1 
ATOM   3381  C C   . LEU B 1 109 ? 23.208  0.543   25.743  1.00 48.60  ? 105 LEU E C   1 
ATOM   3382  O O   . LEU B 1 109 ? 23.226  -0.577  25.235  1.00 45.32  ? 105 LEU E O   1 
ATOM   3383  C CB  . LEU B 1 109 ? 25.437  0.388   26.843  1.00 42.89  ? 105 LEU E CB  1 
ATOM   3384  C CG  . LEU B 1 109 ? 26.910  0.786   26.932  1.00 38.53  ? 105 LEU E CG  1 
ATOM   3385  C CD1 . LEU B 1 109 ? 27.615  -0.045  27.995  1.00 37.41  ? 105 LEU E CD1 1 
ATOM   3386  C CD2 . LEU B 1 109 ? 27.584  0.623   25.578  1.00 40.11  ? 105 LEU E CD2 1 
ATOM   3387  N N   . SER B 1 110 ? 22.073  1.147   26.092  1.00 52.78  ? 106 SER E N   1 
ATOM   3388  C CA  . SER B 1 110 ? 20.773  0.484   25.934  1.00 51.41  ? 106 SER E CA  1 
ATOM   3389  C C   . SER B 1 110 ? 20.450  0.147   24.476  1.00 48.68  ? 106 SER E C   1 
ATOM   3390  O O   . SER B 1 110 ? 19.789  -0.845  24.208  1.00 54.71  ? 106 SER E O   1 
ATOM   3391  C CB  . SER B 1 110 ? 19.652  1.347   26.520  1.00 49.92  ? 106 SER E CB  1 
ATOM   3392  O OG  . SER B 1 110 ? 19.490  2.550   25.781  1.00 48.43  ? 106 SER E OG  1 
ATOM   3393  N N   . ARG B 1 111 ? 20.915  0.976   23.547  1.00 47.77  ? 107 ARG E N   1 
ATOM   3394  C CA  . ARG B 1 111 ? 20.730  0.731   22.121  1.00 53.21  ? 107 ARG E CA  1 
ATOM   3395  C C   . ARG B 1 111 ? 21.947  1.216   21.356  1.00 59.21  ? 107 ARG E C   1 
ATOM   3396  O O   . ARG B 1 111 ? 22.282  2.404   21.395  1.00 56.16  ? 107 ARG E O   1 
ATOM   3397  C CB  . ARG B 1 111 ? 19.487  1.456   21.611  1.00 60.03  ? 107 ARG E CB  1 
ATOM   3398  C CG  . ARG B 1 111 ? 19.189  1.242   20.136  1.00 57.25  ? 107 ARG E CG  1 
ATOM   3399  C CD  . ARG B 1 111 ? 17.698  1.448   19.839  1.00 62.58  ? 107 ARG E CD  1 
ATOM   3400  N NE  . ARG B 1 111 ? 17.388  2.726   19.209  1.00 68.07  ? 107 ARG E NE  1 
ATOM   3401  C CZ  . ARG B 1 111 ? 16.150  3.139   18.932  1.00 73.83  ? 107 ARG E CZ  1 
ATOM   3402  N NH1 . ARG B 1 111 ? 15.092  2.376   19.218  1.00 70.98  ? 107 ARG E NH1 1 
ATOM   3403  N NH2 . ARG B 1 111 ? 15.958  4.324   18.364  1.00 78.90  ? 107 ARG E NH2 1 
ATOM   3404  N N   . ILE B 1 112 ? 22.595  0.286   20.658  1.00 59.67  ? 108 ILE E N   1 
ATOM   3405  C CA  . ILE B 1 112 ? 23.834  0.565   19.953  1.00 57.38  ? 108 ILE E CA  1 
ATOM   3406  C C   . ILE B 1 112 ? 23.759  0.059   18.514  1.00 62.35  ? 108 ILE E C   1 
ATOM   3407  O O   . ILE B 1 112 ? 23.271  -1.050  18.251  1.00 61.68  ? 108 ILE E O   1 
ATOM   3408  C CB  . ILE B 1 112 ? 25.027  -0.086  20.680  1.00 53.23  ? 108 ILE E CB  1 
ATOM   3409  C CG1 . ILE B 1 112 ? 25.231  0.559   22.057  1.00 49.09  ? 108 ILE E CG1 1 
ATOM   3410  C CG2 . ILE B 1 112 ? 26.292  0.037   19.846  1.00 49.72  ? 108 ILE E CG2 1 
ATOM   3411  C CD1 . ILE B 1 112 ? 25.563  2.036   22.007  1.00 44.45  ? 108 ILE E CD1 1 
ATOM   3412  N N   . ASN B 1 113 ? 24.252  0.887   17.594  1.00 65.88  ? 109 ASN E N   1 
ATOM   3413  C CA  . ASN B 1 113 ? 24.249  0.575   16.174  1.00 69.34  ? 109 ASN E CA  1 
ATOM   3414  C C   . ASN B 1 113 ? 25.434  -0.308  15.784  1.00 78.88  ? 109 ASN E C   1 
ATOM   3415  O O   . ASN B 1 113 ? 25.284  -1.227  14.975  1.00 78.50  ? 109 ASN E O   1 
ATOM   3416  C CB  . ASN B 1 113 ? 24.265  1.859   15.342  1.00 75.21  ? 109 ASN E CB  1 
ATOM   3417  C CG  . ASN B 1 113 ? 24.080  1.587   13.857  1.00 78.47  ? 109 ASN E CG  1 
ATOM   3418  O OD1 . ASN B 1 113 ? 24.723  2.206   13.015  1.00 73.13  ? 109 ASN E OD1 1 
ATOM   3419  N ND2 . ASN B 1 113 ? 23.207  0.638   13.533  1.00 81.83  ? 109 ASN E ND2 1 
ATOM   3420  N N   . HIS B 1 114 ? 26.606  -0.018  16.351  1.00 79.74  ? 110 HIS E N   1 
ATOM   3421  C CA  . HIS B 1 114 ? 27.797  -0.849  16.155  1.00 76.00  ? 110 HIS E CA  1 
ATOM   3422  C C   . HIS B 1 114 ? 28.591  -0.983  17.428  1.00 71.38  ? 110 HIS E C   1 
ATOM   3423  O O   . HIS B 1 114 ? 28.827  0.004   18.126  1.00 71.93  ? 110 HIS E O   1 
ATOM   3424  C CB  . HIS B 1 114 ? 28.676  -0.280  15.052  1.00 82.43  ? 110 HIS E CB  1 
ATOM   3425  C CG  . HIS B 1 114 ? 29.842  -1.167  14.690  1.00 92.77  ? 110 HIS E CG  1 
ATOM   3426  N ND1 . HIS B 1 114 ? 31.121  -0.776  14.840  1.00 99.96  ? 110 HIS E ND1 1 
ATOM   3427  C CD2 . HIS B 1 114 ? 29.883  -2.468  14.188  1.00 93.65  ? 110 HIS E CD2 1 
ATOM   3428  C CE1 . HIS B 1 114 ? 31.942  -1.766  14.444  1.00 100.62 ? 110 HIS E CE1 1 
ATOM   3429  N NE2 . HIS B 1 114 ? 31.182  -2.803  14.047  1.00 100.32 ? 110 HIS E NE2 1 
ATOM   3430  N N   . PHE B 1 115 ? 29.020  -2.207  17.728  1.00 67.50  ? 111 PHE E N   1 
ATOM   3431  C CA  . PHE B 1 115 ? 29.749  -2.504  18.960  1.00 69.47  ? 111 PHE E CA  1 
ATOM   3432  C C   . PHE B 1 115 ? 30.831  -3.566  18.733  1.00 68.90  ? 111 PHE E C   1 
ATOM   3433  O O   . PHE B 1 115 ? 30.524  -4.732  18.497  1.00 67.84  ? 111 PHE E O   1 
ATOM   3434  C CB  . PHE B 1 115 ? 28.770  -2.982  20.028  1.00 62.14  ? 111 PHE E CB  1 
ATOM   3435  C CG  . PHE B 1 115 ? 29.336  -2.979  21.417  1.00 59.76  ? 111 PHE E CG  1 
ATOM   3436  C CD1 . PHE B 1 115 ? 29.486  -1.786  22.108  1.00 57.18  ? 111 PHE E CD1 1 
ATOM   3437  C CD2 . PHE B 1 115 ? 29.693  -4.167  22.045  1.00 56.51  ? 111 PHE E CD2 1 
ATOM   3438  C CE1 . PHE B 1 115 ? 29.992  -1.770  23.395  1.00 54.83  ? 111 PHE E CE1 1 
ATOM   3439  C CE2 . PHE B 1 115 ? 30.196  -4.158  23.333  1.00 55.51  ? 111 PHE E CE2 1 
ATOM   3440  C CZ  . PHE B 1 115 ? 30.345  -2.958  24.010  1.00 54.81  ? 111 PHE E CZ  1 
ATOM   3441  N N   . GLU B 1 116 ? 32.094  -3.161  18.816  1.00 67.87  ? 112 GLU E N   1 
ATOM   3442  C CA  . GLU B 1 116 ? 33.213  -4.073  18.579  1.00 68.31  ? 112 GLU E CA  1 
ATOM   3443  C C   . GLU B 1 116 ? 34.292  -3.925  19.651  1.00 59.88  ? 112 GLU E C   1 
ATOM   3444  O O   . GLU B 1 116 ? 34.843  -2.838  19.841  1.00 52.52  ? 112 GLU E O   1 
ATOM   3445  C CB  . GLU B 1 116 ? 33.812  -3.816  17.193  1.00 76.00  ? 112 GLU E CB  1 
ATOM   3446  C CG  . GLU B 1 116 ? 34.828  -4.857  16.738  1.00 79.47  ? 112 GLU E CG  1 
ATOM   3447  C CD  . GLU B 1 116 ? 35.524  -4.475  15.443  1.00 89.38  ? 112 GLU E CD  1 
ATOM   3448  O OE1 . GLU B 1 116 ? 34.919  -3.757  14.619  1.00 94.26  ? 112 GLU E OE1 1 
ATOM   3449  O OE2 . GLU B 1 116 ? 36.684  -4.895  15.248  1.00 103.11 ? 112 GLU E OE2 1 
ATOM   3450  N N   . LYS B 1 117 ? 34.585  -5.026  20.343  1.00 55.13  ? 113 LYS E N   1 
ATOM   3451  C CA  . LYS B 1 117 ? 35.688  -5.076  21.300  1.00 61.33  ? 113 LYS E CA  1 
ATOM   3452  C C   . LYS B 1 117 ? 37.021  -4.989  20.556  1.00 63.44  ? 113 LYS E C   1 
ATOM   3453  O O   . LYS B 1 117 ? 37.212  -5.655  19.540  1.00 70.05  ? 113 LYS E O   1 
ATOM   3454  C CB  . LYS B 1 117 ? 35.636  -6.367  22.125  1.00 60.57  ? 113 LYS E CB  1 
ATOM   3455  C CG  . LYS B 1 117 ? 36.627  -6.402  23.281  1.00 63.55  ? 113 LYS E CG  1 
ATOM   3456  C CD  . LYS B 1 117 ? 36.864  -7.811  23.811  1.00 64.28  ? 113 LYS E CD  1 
ATOM   3457  C CE  . LYS B 1 117 ? 35.749  -8.275  24.735  1.00 70.20  ? 113 LYS E CE  1 
ATOM   3458  N NZ  . LYS B 1 117 ? 36.145  -9.475  25.525  1.00 73.79  ? 113 LYS E NZ  1 
ATOM   3459  N N   . ILE B 1 118 ? 37.931  -4.165  21.071  1.00 62.64  ? 114 ILE E N   1 
ATOM   3460  C CA  . ILE B 1 118 ? 39.240  -3.932  20.458  1.00 65.06  ? 114 ILE E CA  1 
ATOM   3461  C C   . ILE B 1 118 ? 40.311  -4.003  21.536  1.00 71.57  ? 114 ILE E C   1 
ATOM   3462  O O   . ILE B 1 118 ? 40.126  -3.465  22.625  1.00 74.01  ? 114 ILE E O   1 
ATOM   3463  C CB  . ILE B 1 118 ? 39.314  -2.531  19.803  1.00 60.93  ? 114 ILE E CB  1 
ATOM   3464  C CG1 . ILE B 1 118 ? 38.354  -2.424  18.624  1.00 67.47  ? 114 ILE E CG1 1 
ATOM   3465  C CG2 . ILE B 1 118 ? 40.721  -2.220  19.320  1.00 59.90  ? 114 ILE E CG2 1 
ATOM   3466  C CD1 . ILE B 1 118 ? 38.626  -3.422  17.518  1.00 73.98  ? 114 ILE E CD1 1 
ATOM   3467  N N   . GLN B 1 119 ? 41.427  -4.665  21.235  1.00 72.19  ? 115 GLN E N   1 
ATOM   3468  C CA  . GLN B 1 119 ? 42.577  -4.666  22.136  1.00 69.88  ? 115 GLN E CA  1 
ATOM   3469  C C   . GLN B 1 119 ? 43.264  -3.308  22.034  1.00 67.95  ? 115 GLN E C   1 
ATOM   3470  O O   . GLN B 1 119 ? 43.776  -2.938  20.976  1.00 57.11  ? 115 GLN E O   1 
ATOM   3471  C CB  . GLN B 1 119 ? 43.550  -5.790  21.791  1.00 66.41  ? 115 GLN E CB  1 
ATOM   3472  C CG  . GLN B 1 119 ? 44.598  -6.040  22.862  1.00 69.65  ? 115 GLN E CG  1 
ATOM   3473  C CD  . GLN B 1 119 ? 45.679  -7.004  22.416  1.00 65.58  ? 115 GLN E CD  1 
ATOM   3474  O OE1 . GLN B 1 119 ? 46.362  -6.775  21.417  1.00 67.24  ? 115 GLN E OE1 1 
ATOM   3475  N NE2 . GLN B 1 119 ? 45.849  -8.085  23.166  1.00 54.24  ? 115 GLN E NE2 1 
ATOM   3476  N N   . ILE B 1 120 ? 43.255  -2.572  23.142  1.00 71.00  ? 116 ILE E N   1 
ATOM   3477  C CA  . ILE B 1 120 ? 43.711  -1.191  23.168  1.00 65.95  ? 116 ILE E CA  1 
ATOM   3478  C C   . ILE B 1 120 ? 45.184  -1.144  23.567  1.00 65.33  ? 116 ILE E C   1 
ATOM   3479  O O   . ILE B 1 120 ? 45.977  -0.447  22.937  1.00 69.13  ? 116 ILE E O   1 
ATOM   3480  C CB  . ILE B 1 120 ? 42.815  -0.337  24.107  1.00 63.89  ? 116 ILE E CB  1 
ATOM   3481  C CG1 . ILE B 1 120 ? 43.133  1.153   23.969  1.00 69.89  ? 116 ILE E CG1 1 
ATOM   3482  C CG2 . ILE B 1 120 ? 42.920  -0.777  25.561  1.00 59.71  ? 116 ILE E CG2 1 
ATOM   3483  C CD1 . ILE B 1 120 ? 42.294  2.025   24.882  1.00 61.75  ? 116 ILE E CD1 1 
ATOM   3484  N N   . ILE B 1 121 ? 45.547  -1.886  24.609  1.00 63.82  ? 117 ILE E N   1 
ATOM   3485  C CA  . ILE B 1 121 ? 46.945  -2.045  25.001  1.00 63.49  ? 117 ILE E CA  1 
ATOM   3486  C C   . ILE B 1 121 ? 47.172  -3.498  25.438  1.00 64.69  ? 117 ILE E C   1 
ATOM   3487  O O   . ILE B 1 121 ? 46.491  -3.996  26.336  1.00 63.17  ? 117 ILE E O   1 
ATOM   3488  C CB  . ILE B 1 121 ? 47.361  -1.037  26.077  1.00 63.95  ? 117 ILE E CB  1 
ATOM   3489  C CG1 . ILE B 1 121 ? 46.274  -0.931  27.142  1.00 69.06  ? 117 ILE E CG1 1 
ATOM   3490  C CG2 . ILE B 1 121 ? 47.539  0.345   25.468  1.00 70.51  ? 117 ILE E CG2 1 
ATOM   3491  C CD1 . ILE B 1 121 ? 46.761  -0.369  28.457  1.00 76.65  ? 117 ILE E CD1 1 
ATOM   3492  N N   . PRO B 1 122 ? 48.108  -4.200  24.775  1.00 62.55  ? 118 PRO E N   1 
ATOM   3493  C CA  . PRO B 1 122 ? 48.235  -5.643  25.008  1.00 58.98  ? 118 PRO E CA  1 
ATOM   3494  C C   . PRO B 1 122 ? 48.841  -6.012  26.362  1.00 54.50  ? 118 PRO E C   1 
ATOM   3495  O O   . PRO B 1 122 ? 49.725  -5.313  26.858  1.00 59.11  ? 118 PRO E O   1 
ATOM   3496  C CB  . PRO B 1 122 ? 49.129  -6.114  23.855  1.00 61.80  ? 118 PRO E CB  1 
ATOM   3497  C CG  . PRO B 1 122 ? 49.870  -4.907  23.400  1.00 65.19  ? 118 PRO E CG  1 
ATOM   3498  C CD  . PRO B 1 122 ? 49.042  -3.706  23.744  1.00 63.12  ? 118 PRO E CD  1 
ATOM   3499  N N   . LYS B 1 123 ? 48.364  -7.113  26.941  1.00 59.40  ? 119 LYS E N   1 
ATOM   3500  C CA  . LYS B 1 123 ? 48.805  -7.567  28.265  1.00 64.97  ? 119 LYS E CA  1 
ATOM   3501  C C   . LYS B 1 123 ? 50.312  -7.850  28.309  1.00 77.28  ? 119 LYS E C   1 
ATOM   3502  O O   . LYS B 1 123 ? 50.952  -7.670  29.345  1.00 87.78  ? 119 LYS E O   1 
ATOM   3503  C CB  . LYS B 1 123 ? 48.022  -8.817  28.697  1.00 65.85  ? 119 LYS E CB  1 
ATOM   3504  C CG  . LYS B 1 123 ? 48.116  -9.139  30.185  1.00 74.10  ? 119 LYS E CG  1 
ATOM   3505  C CD  . LYS B 1 123 ? 47.609  -10.537 30.520  1.00 73.60  ? 119 LYS E CD  1 
ATOM   3506  C CE  . LYS B 1 123 ? 46.176  -10.522 31.032  1.00 74.77  ? 119 LYS E CE  1 
ATOM   3507  N NZ  . LYS B 1 123 ? 45.750  -11.858 31.538  1.00 66.19  ? 119 LYS E NZ  1 
ATOM   3508  N N   . ASN B 1 124 ? 50.873  -8.285  27.183  1.00 85.77  ? 120 ASN E N   1 
ATOM   3509  C CA  . ASN B 1 124 ? 52.308  -8.572  27.084  1.00 80.97  ? 120 ASN E CA  1 
ATOM   3510  C C   . ASN B 1 124 ? 53.208  -7.327  27.042  1.00 81.24  ? 120 ASN E C   1 
ATOM   3511  O O   . ASN B 1 124 ? 54.426  -7.445  27.198  1.00 86.82  ? 120 ASN E O   1 
ATOM   3512  C CB  . ASN B 1 124 ? 52.595  -9.465  25.866  1.00 75.88  ? 120 ASN E CB  1 
ATOM   3513  C CG  . ASN B 1 124 ? 52.084  -8.867  24.561  1.00 77.54  ? 120 ASN E CG  1 
ATOM   3514  O OD1 . ASN B 1 124 ? 52.357  -7.708  24.243  1.00 76.79  ? 120 ASN E OD1 1 
ATOM   3515  N ND2 . ASN B 1 124 ? 51.335  -9.658  23.801  1.00 73.15  ? 120 ASN E ND2 1 
ATOM   3516  N N   . SER B 1 125 ? 52.620  -6.145  26.841  1.00 73.85  ? 121 SER E N   1 
ATOM   3517  C CA  . SER B 1 125 ? 53.409  -4.914  26.681  1.00 71.86  ? 121 SER E CA  1 
ATOM   3518  C C   . SER B 1 125 ? 53.888  -4.311  28.006  1.00 73.85  ? 121 SER E C   1 
ATOM   3519  O O   . SER B 1 125 ? 54.606  -3.313  27.992  1.00 71.91  ? 121 SER E O   1 
ATOM   3520  C CB  . SER B 1 125 ? 52.625  -3.852  25.908  1.00 68.39  ? 121 SER E CB  1 
ATOM   3521  O OG  . SER B 1 125 ? 51.628  -3.274  26.722  1.00 77.60  ? 121 SER E OG  1 
ATOM   3522  N N   . TRP B 1 126 ? 53.472  -4.888  29.135  1.00 69.25  ? 122 TRP E N   1 
ATOM   3523  C CA  . TRP B 1 126 ? 53.950  -4.451  30.448  1.00 72.05  ? 122 TRP E CA  1 
ATOM   3524  C C   . TRP B 1 126 ? 55.205  -5.197  30.807  1.00 69.97  ? 122 TRP E C   1 
ATOM   3525  O O   . TRP B 1 126 ? 55.149  -6.327  31.300  1.00 72.48  ? 122 TRP E O   1 
ATOM   3526  C CB  . TRP B 1 126 ? 52.884  -4.673  31.520  1.00 73.03  ? 122 TRP E CB  1 
ATOM   3527  C CG  . TRP B 1 126 ? 51.568  -3.979  31.239  1.00 65.54  ? 122 TRP E CG  1 
ATOM   3528  C CD1 . TRP B 1 126 ? 50.373  -4.561  30.837  1.00 64.07  ? 122 TRP E CD1 1 
ATOM   3529  C CD2 . TRP B 1 126 ? 51.274  -2.544  31.333  1.00 63.03  ? 122 TRP E CD2 1 
ATOM   3530  N NE1 . TRP B 1 126 ? 49.391  -3.618  30.684  1.00 66.94  ? 122 TRP E NE1 1 
ATOM   3531  C CE2 . TRP B 1 126 ? 49.864  -2.389  30.964  1.00 63.65  ? 122 TRP E CE2 1 
ATOM   3532  C CE3 . TRP B 1 126 ? 52.006  -1.421  31.673  1.00 61.37  ? 122 TRP E CE3 1 
ATOM   3533  C CZ2 . TRP B 1 126 ? 49.243  -1.153  30.941  1.00 60.96  ? 122 TRP E CZ2 1 
ATOM   3534  C CZ3 . TRP B 1 126 ? 51.368  -0.179  31.650  1.00 64.01  ? 122 TRP E CZ3 1 
ATOM   3535  C CH2 . TRP B 1 126 ? 50.019  -0.051  31.290  1.00 64.72  ? 122 TRP E CH2 1 
ATOM   3536  N N   . SER B 1 127 ? 56.353  -4.569  30.566  1.00 67.23  ? 123 SER E N   1 
ATOM   3537  C CA  . SER B 1 127 ? 57.649  -5.215  30.781  1.00 67.04  ? 123 SER E CA  1 
ATOM   3538  C C   . SER B 1 127 ? 58.211  -4.968  32.186  1.00 71.44  ? 123 SER E C   1 
ATOM   3539  O O   . SER B 1 127 ? 58.857  -5.851  32.755  1.00 67.63  ? 123 SER E O   1 
ATOM   3540  C CB  . SER B 1 127 ? 58.650  -4.760  29.716  1.00 66.96  ? 123 SER E CB  1 
ATOM   3541  O OG  . SER B 1 127 ? 58.686  -3.348  29.616  1.00 74.27  ? 123 SER E OG  1 
ATOM   3542  N N   . ASP B 1 128 ? 57.961  -3.779  32.740  1.00 72.22  ? 124 ASP E N   1 
ATOM   3543  C CA  . ASP B 1 128 ? 58.455  -3.410  34.075  1.00 68.43  ? 124 ASP E CA  1 
ATOM   3544  C C   . ASP B 1 128 ? 57.451  -3.690  35.199  1.00 62.79  ? 124 ASP E C   1 
ATOM   3545  O O   . ASP B 1 128 ? 57.709  -3.360  36.360  1.00 60.83  ? 124 ASP E O   1 
ATOM   3546  C CB  . ASP B 1 128 ? 58.850  -1.931  34.096  1.00 72.02  ? 124 ASP E CB  1 
ATOM   3547  C CG  . ASP B 1 128 ? 59.968  -1.616  33.119  1.00 74.51  ? 124 ASP E CG  1 
ATOM   3548  O OD1 . ASP B 1 128 ? 61.055  -2.212  33.261  1.00 72.19  ? 124 ASP E OD1 1 
ATOM   3549  O OD2 . ASP B 1 128 ? 59.763  -0.779  32.212  1.00 78.34  ? 124 ASP E OD2 1 
ATOM   3550  N N   . HIS B 1 129 ? 56.313  -4.291  34.853  1.00 56.28  ? 125 HIS E N   1 
ATOM   3551  C CA  . HIS B 1 129 ? 55.282  -4.649  35.831  1.00 52.47  ? 125 HIS E CA  1 
ATOM   3552  C C   . HIS B 1 129 ? 54.776  -6.035  35.557  1.00 52.25  ? 125 HIS E C   1 
ATOM   3553  O O   . HIS B 1 129 ? 54.876  -6.527  34.432  1.00 56.80  ? 125 HIS E O   1 
ATOM   3554  C CB  . HIS B 1 129 ? 54.122  -3.654  35.778  1.00 47.00  ? 125 HIS E CB  1 
ATOM   3555  C CG  . HIS B 1 129 ? 54.534  -2.218  36.005  1.00 42.88  ? 125 HIS E CG  1 
ATOM   3556  N ND1 . HIS B 1 129 ? 55.064  -1.455  35.029  1.00 42.34  ? 125 HIS E ND1 1 
ATOM   3557  C CD2 . HIS B 1 129 ? 54.477  -1.416  37.147  1.00 41.96  ? 125 HIS E CD2 1 
ATOM   3558  C CE1 . HIS B 1 129 ? 55.337  -0.229  35.517  1.00 44.26  ? 125 HIS E CE1 1 
ATOM   3559  N NE2 . HIS B 1 129 ? 54.977  -0.207  36.815  1.00 45.91  ? 125 HIS E NE2 1 
ATOM   3560  N N   . GLU B 1 130 ? 54.220  -6.672  36.583  1.00 51.79  ? 126 GLU E N   1 
ATOM   3561  C CA  . GLU B 1 130 ? 53.634  -8.005  36.449  1.00 57.58  ? 126 GLU E CA  1 
ATOM   3562  C C   . GLU B 1 130 ? 52.159  -7.885  36.072  1.00 63.52  ? 126 GLU E C   1 
ATOM   3563  O O   . GLU B 1 130 ? 51.363  -7.301  36.814  1.00 60.25  ? 126 GLU E O   1 
ATOM   3564  C CB  . GLU B 1 130 ? 53.785  -8.794  37.752  1.00 69.28  ? 126 GLU E CB  1 
ATOM   3565  C CG  . GLU B 1 130 ? 55.207  -9.282  38.024  1.00 77.30  ? 126 GLU E CG  1 
ATOM   3566  C CD  . GLU B 1 130 ? 55.535  -10.630 37.376  1.00 83.02  ? 126 GLU E CD  1 
ATOM   3567  O OE1 . GLU B 1 130 ? 54.733  -11.133 36.554  1.00 92.84  ? 126 GLU E OE1 1 
ATOM   3568  O OE2 . GLU B 1 130 ? 56.611  -11.191 37.679  1.00 93.21  ? 126 GLU E OE2 1 
ATOM   3569  N N   . ALA B 1 131 ? 51.807  -8.435  34.912  1.00 67.87  ? 127 ALA E N   1 
ATOM   3570  C CA  . ALA B 1 131 ? 50.439  -8.365  34.395  1.00 64.92  ? 127 ALA E CA  1 
ATOM   3571  C C   . ALA B 1 131 ? 49.641  -9.651  34.628  1.00 61.21  ? 127 ALA E C   1 
ATOM   3572  O O   . ALA B 1 131 ? 48.480  -9.725  34.231  1.00 71.88  ? 127 ALA E O   1 
ATOM   3573  C CB  . ALA B 1 131 ? 50.461  -8.022  32.911  1.00 58.44  ? 127 ALA E CB  1 
ATOM   3574  N N   . SER B 1 132 ? 50.252  -10.650 35.265  1.00 57.72  ? 128 SER E N   1 
ATOM   3575  C CA  . SER B 1 132 ? 49.628  -11.969 35.414  1.00 59.53  ? 128 SER E CA  1 
ATOM   3576  C C   . SER B 1 132 ? 49.418  -12.421 36.862  1.00 56.63  ? 128 SER E C   1 
ATOM   3577  O O   . SER B 1 132 ? 48.951  -13.532 37.093  1.00 53.64  ? 128 SER E O   1 
ATOM   3578  C CB  . SER B 1 132 ? 50.452  -13.019 34.658  1.00 64.92  ? 128 SER E CB  1 
ATOM   3579  O OG  . SER B 1 132 ? 50.410  -12.782 33.258  1.00 74.08  ? 128 SER E OG  1 
ATOM   3580  N N   . LEU B 1 133 ? 49.760  -11.576 37.829  1.00 63.10  ? 129 LEU E N   1 
ATOM   3581  C CA  . LEU B 1 133 ? 49.540  -11.896 39.245  1.00 66.15  ? 129 LEU E CA  1 
ATOM   3582  C C   . LEU B 1 133 ? 48.289  -11.220 39.811  1.00 62.93  ? 129 LEU E C   1 
ATOM   3583  O O   . LEU B 1 133 ? 47.914  -11.468 40.958  1.00 58.86  ? 129 LEU E O   1 
ATOM   3584  C CB  . LEU B 1 133 ? 50.770  -11.531 40.082  1.00 70.54  ? 129 LEU E CB  1 
ATOM   3585  C CG  . LEU B 1 133 ? 51.897  -12.581 40.051  1.00 72.43  ? 129 LEU E CG  1 
ATOM   3586  C CD1 . LEU B 1 133 ? 52.948  -12.206 39.018  1.00 67.81  ? 129 LEU E CD1 1 
ATOM   3587  C CD2 . LEU B 1 133 ? 52.536  -12.758 41.424  1.00 73.45  ? 129 LEU E CD2 1 
ATOM   3588  N N   . GLY B 1 134 ? 47.649  -10.374 39.005  1.00 60.46  ? 130 GLY E N   1 
ATOM   3589  C CA  . GLY B 1 134 ? 46.419  -9.698  39.406  1.00 53.77  ? 130 GLY E CA  1 
ATOM   3590  C C   . GLY B 1 134 ? 45.220  -10.621 39.350  1.00 50.15  ? 130 GLY E C   1 
ATOM   3591  O O   . GLY B 1 134 ? 44.532  -10.705 38.331  1.00 47.99  ? 130 GLY E O   1 
ATOM   3592  N N   . VAL B 1 135 ? 44.968  -11.301 40.461  1.00 46.79  ? 131 VAL E N   1 
ATOM   3593  C CA  . VAL B 1 135 ? 43.989  -12.373 40.514  1.00 47.03  ? 131 VAL E CA  1 
ATOM   3594  C C   . VAL B 1 135 ? 43.433  -12.498 41.933  1.00 49.78  ? 131 VAL E C   1 
ATOM   3595  O O   . VAL B 1 135 ? 44.107  -12.134 42.902  1.00 50.01  ? 131 VAL E O   1 
ATOM   3596  C CB  . VAL B 1 135 ? 44.642  -13.692 40.051  1.00 48.86  ? 131 VAL E CB  1 
ATOM   3597  C CG1 . VAL B 1 135 ? 44.040  -14.887 40.769  1.00 53.99  ? 131 VAL E CG1 1 
ATOM   3598  C CG2 . VAL B 1 135 ? 44.547  -13.825 38.535  1.00 41.00  ? 131 VAL E CG2 1 
ATOM   3599  N N   . SER B 1 136 ? 42.209  -13.008 42.051  1.00 49.24  ? 132 SER E N   1 
ATOM   3600  C CA  . SER B 1 136 ? 41.523  -13.071 43.344  1.00 52.13  ? 132 SER E CA  1 
ATOM   3601  C C   . SER B 1 136 ? 40.570  -14.259 43.466  1.00 55.74  ? 132 SER E C   1 
ATOM   3602  O O   . SER B 1 136 ? 39.986  -14.714 42.477  1.00 57.18  ? 132 SER E O   1 
ATOM   3603  C CB  . SER B 1 136 ? 40.739  -11.777 43.574  1.00 56.36  ? 132 SER E CB  1 
ATOM   3604  O OG  . SER B 1 136 ? 39.958  -11.844 44.760  1.00 55.42  ? 132 SER E OG  1 
ATOM   3605  N N   . ALA B 1 137 ? 40.398  -14.730 44.700  1.00 55.31  ? 133 ALA E N   1 
ATOM   3606  C CA  . ALA B 1 137 ? 39.490  -15.837 45.003  1.00 58.82  ? 133 ALA E CA  1 
ATOM   3607  C C   . ALA B 1 137 ? 38.012  -15.435 44.882  1.00 65.17  ? 133 ALA E C   1 
ATOM   3608  O O   . ALA B 1 137 ? 37.139  -16.298 44.763  1.00 67.29  ? 133 ALA E O   1 
ATOM   3609  C CB  . ALA B 1 137 ? 39.777  -16.384 46.394  1.00 50.42  ? 133 ALA E CB  1 
ATOM   3610  N N   . ALA B 1 138 ? 37.737  -14.131 44.913  1.00 66.05  ? 134 ALA E N   1 
ATOM   3611  C CA  . ALA B 1 138 ? 36.382  -13.618 44.705  1.00 68.91  ? 134 ALA E CA  1 
ATOM   3612  C C   . ALA B 1 138 ? 35.925  -13.743 43.245  1.00 68.22  ? 134 ALA E C   1 
ATOM   3613  O O   . ALA B 1 138 ? 34.724  -13.704 42.971  1.00 67.27  ? 134 ALA E O   1 
ATOM   3614  C CB  . ALA B 1 138 ? 36.286  -12.173 45.168  1.00 71.64  ? 134 ALA E CB  1 
ATOM   3615  N N   . CYS B 1 139 ? 36.877  -13.899 42.321  1.00 67.48  ? 135 CYS E N   1 
ATOM   3616  C CA  . CYS B 1 139 ? 36.575  -14.089 40.900  1.00 66.21  ? 135 CYS E CA  1 
ATOM   3617  C C   . CYS B 1 139 ? 37.141  -15.417 40.372  1.00 66.91  ? 135 CYS E C   1 
ATOM   3618  O O   . CYS B 1 139 ? 38.103  -15.414 39.600  1.00 63.08  ? 135 CYS E O   1 
ATOM   3619  C CB  . CYS B 1 139 ? 37.150  -12.932 40.075  1.00 64.72  ? 135 CYS E CB  1 
ATOM   3620  S SG  . CYS B 1 139 ? 36.653  -11.284 40.615  1.00 74.84  ? 135 CYS E SG  1 
ATOM   3621  N N   . PRO B 1 140 ? 36.541  -16.558 40.767  1.00 65.61  ? 136 PRO E N   1 
ATOM   3622  C CA  . PRO B 1 140 ? 37.024  -17.850 40.267  1.00 66.15  ? 136 PRO E CA  1 
ATOM   3623  C C   . PRO B 1 140 ? 36.586  -18.130 38.829  1.00 64.55  ? 136 PRO E C   1 
ATOM   3624  O O   . PRO B 1 140 ? 35.488  -17.732 38.434  1.00 62.62  ? 136 PRO E O   1 
ATOM   3625  C CB  . PRO B 1 140 ? 36.390  -18.868 41.226  1.00 62.75  ? 136 PRO E CB  1 
ATOM   3626  C CG  . PRO B 1 140 ? 35.285  -18.152 41.932  1.00 60.11  ? 136 PRO E CG  1 
ATOM   3627  C CD  . PRO B 1 140 ? 35.300  -16.702 41.545  1.00 63.74  ? 136 PRO E CD  1 
ATOM   3628  N N   . TYR B 1 141 ? 37.440  -18.812 38.065  1.00 71.41  ? 137 TYR E N   1 
ATOM   3629  C CA  . TYR B 1 141 ? 37.142  -19.160 36.674  1.00 80.22  ? 137 TYR E CA  1 
ATOM   3630  C C   . TYR B 1 141 ? 36.803  -20.650 36.554  1.00 88.18  ? 137 TYR E C   1 
ATOM   3631  O O   . TYR B 1 141 ? 35.624  -21.010 36.427  1.00 91.12  ? 137 TYR E O   1 
ATOM   3632  C CB  . TYR B 1 141 ? 38.305  -18.767 35.749  1.00 77.65  ? 137 TYR E CB  1 
ATOM   3633  C CG  . TYR B 1 141 ? 38.034  -19.018 34.284  1.00 87.90  ? 137 TYR E CG  1 
ATOM   3634  C CD1 . TYR B 1 141 ? 36.891  -18.507 33.680  1.00 96.46  ? 137 TYR E CD1 1 
ATOM   3635  C CD2 . TYR B 1 141 ? 38.923  -19.756 33.498  1.00 93.62  ? 137 TYR E CD2 1 
ATOM   3636  C CE1 . TYR B 1 141 ? 36.626  -18.735 32.342  1.00 101.35 ? 137 TYR E CE1 1 
ATOM   3637  C CE2 . TYR B 1 141 ? 38.664  -19.994 32.158  1.00 98.99  ? 137 TYR E CE2 1 
ATOM   3638  C CZ  . TYR B 1 141 ? 37.514  -19.479 31.584  1.00 103.24 ? 137 TYR E CZ  1 
ATOM   3639  O OH  . TYR B 1 141 ? 37.254  -19.700 30.252  1.00 106.91 ? 137 TYR E OH  1 
ATOM   3640  N N   . GLN B 1 142 ? 37.826  -21.507 36.590  1.00 79.44  ? 138 GLN E N   1 
ATOM   3641  C CA  . GLN B 1 142 ? 37.651  -22.946 36.557  1.00 76.44  ? 138 GLN E CA  1 
ATOM   3642  C C   . GLN B 1 142 ? 38.099  -23.543 37.893  1.00 76.07  ? 138 GLN E C   1 
ATOM   3643  O O   . GLN B 1 142 ? 38.825  -24.541 37.909  1.00 78.34  ? 138 GLN E O   1 
ATOM   3644  C CB  . GLN B 1 142 ? 38.518  -23.529 35.431  1.00 79.60  ? 138 GLN E CB  1 
ATOM   3645  C CG  . GLN B 1 142 ? 38.344  -22.815 34.085  1.00 86.47  ? 138 GLN E CG  1 
ATOM   3646  C CD  . GLN B 1 142 ? 37.505  -23.585 33.090  1.00 94.10  ? 138 GLN E CD  1 
ATOM   3647  O OE1 . GLN B 1 142 ? 36.727  -24.462 33.458  1.00 93.32  ? 138 GLN E OE1 1 
ATOM   3648  N NE2 . GLN B 1 142 ? 37.646  -23.245 31.815  1.00 101.58 ? 138 GLN E NE2 1 
ATOM   3649  N N   . GLY B 1 143 ? 37.687  -22.934 39.010  1.00 72.35  ? 139 GLY E N   1 
ATOM   3650  C CA  . GLY B 1 143 ? 38.209  -23.297 40.334  1.00 73.03  ? 139 GLY E CA  1 
ATOM   3651  C C   . GLY B 1 143 ? 39.440  -22.480 40.702  1.00 72.86  ? 139 GLY E C   1 
ATOM   3652  O O   . GLY B 1 143 ? 39.642  -22.146 41.867  1.00 77.44  ? 139 GLY E O   1 
ATOM   3653  N N   . LYS B 1 144 ? 40.271  -22.186 39.703  1.00 77.60  ? 140 LYS E N   1 
ATOM   3654  C CA  . LYS B 1 144 ? 41.425  -21.301 39.853  1.00 82.00  ? 140 LYS E CA  1 
ATOM   3655  C C   . LYS B 1 144 ? 40.952  -19.871 40.029  1.00 81.87  ? 140 LYS E C   1 
ATOM   3656  O O   . LYS B 1 144 ? 40.037  -19.437 39.337  1.00 103.17 ? 140 LYS E O   1 
ATOM   3657  C CB  . LYS B 1 144 ? 42.309  -21.396 38.598  1.00 93.10  ? 140 LYS E CB  1 
ATOM   3658  C CG  . LYS B 1 144 ? 43.617  -20.609 38.615  1.00 96.76  ? 140 LYS E CG  1 
ATOM   3659  C CD  . LYS B 1 144 ? 44.238  -20.479 37.229  1.00 106.26 ? 140 LYS E CD  1 
ATOM   3660  C CE  . LYS B 1 144 ? 45.427  -19.534 37.247  1.00 115.43 ? 140 LYS E CE  1 
ATOM   3661  N NZ  . LYS B 1 144 ? 46.025  -19.338 35.894  1.00 114.13 ? 140 LYS E NZ  1 
ATOM   3662  N N   . SER B 1 145 ? 41.584  -19.141 40.943  1.00 72.03  ? 141 SER E N   1 
ATOM   3663  C CA  . SER B 1 145 ? 41.256  -17.737 41.173  1.00 66.10  ? 141 SER E CA  1 
ATOM   3664  C C   . SER B 1 145 ? 41.678  -16.888 39.972  1.00 57.65  ? 141 SER E C   1 
ATOM   3665  O O   . SER B 1 145 ? 42.746  -17.102 39.399  1.00 51.45  ? 141 SER E O   1 
ATOM   3666  C CB  . SER B 1 145 ? 41.936  -17.238 42.446  1.00 69.39  ? 141 SER E CB  1 
ATOM   3667  O OG  . SER B 1 145 ? 43.325  -17.493 42.416  1.00 81.70  ? 141 SER E OG  1 
ATOM   3668  N N   . SER B 1 146 ? 40.829  -15.931 39.594  1.00 59.59  ? 142 SER E N   1 
ATOM   3669  C CA  . SER B 1 146 ? 41.030  -15.141 38.373  1.00 55.49  ? 142 SER E CA  1 
ATOM   3670  C C   . SER B 1 146 ? 40.575  -13.690 38.562  1.00 51.39  ? 142 SER E C   1 
ATOM   3671  O O   . SER B 1 146 ? 40.569  -13.176 39.684  1.00 48.95  ? 142 SER E O   1 
ATOM   3672  C CB  . SER B 1 146 ? 40.290  -15.797 37.196  1.00 55.74  ? 142 SER E CB  1 
ATOM   3673  O OG  . SER B 1 146 ? 40.657  -15.212 35.957  1.00 46.40  ? 142 SER E OG  1 
ATOM   3674  N N   . PHE B 1 147 ? 40.206  -13.035 37.462  1.00 52.73  ? 143 PHE E N   1 
ATOM   3675  C CA  . PHE B 1 147 ? 39.836  -11.626 37.480  1.00 52.92  ? 143 PHE E CA  1 
ATOM   3676  C C   . PHE B 1 147 ? 39.063  -11.261 36.210  1.00 58.59  ? 143 PHE E C   1 
ATOM   3677  O O   . PHE B 1 147 ? 38.989  -12.056 35.270  1.00 61.52  ? 143 PHE E O   1 
ATOM   3678  C CB  . PHE B 1 147 ? 41.107  -10.781 37.588  1.00 48.97  ? 143 PHE E CB  1 
ATOM   3679  C CG  . PHE B 1 147 ? 40.864  -9.350  37.972  1.00 46.97  ? 143 PHE E CG  1 
ATOM   3680  C CD1 . PHE B 1 147 ? 40.319  -9.031  39.212  1.00 45.49  ? 143 PHE E CD1 1 
ATOM   3681  C CD2 . PHE B 1 147 ? 41.196  -8.320  37.102  1.00 43.23  ? 143 PHE E CD2 1 
ATOM   3682  C CE1 . PHE B 1 147 ? 40.104  -7.713  39.573  1.00 41.27  ? 143 PHE E CE1 1 
ATOM   3683  C CE2 . PHE B 1 147 ? 40.982  -7.000  37.458  1.00 41.20  ? 143 PHE E CE2 1 
ATOM   3684  C CZ  . PHE B 1 147 ? 40.439  -6.696  38.696  1.00 39.63  ? 143 PHE E CZ  1 
ATOM   3685  N N   . PHE B 1 148 ? 38.480  -10.065 36.191  1.00 56.92  ? 144 PHE E N   1 
ATOM   3686  C CA  . PHE B 1 148 ? 37.839  -9.526  34.989  1.00 56.15  ? 144 PHE E CA  1 
ATOM   3687  C C   . PHE B 1 148 ? 38.793  -9.658  33.801  1.00 57.19  ? 144 PHE E C   1 
ATOM   3688  O O   . PHE B 1 148 ? 39.950  -9.258  33.885  1.00 63.26  ? 144 PHE E O   1 
ATOM   3689  C CB  . PHE B 1 148 ? 37.461  -8.048  35.178  1.00 56.58  ? 144 PHE E CB  1 
ATOM   3690  C CG  . PHE B 1 148 ? 36.536  -7.792  36.335  1.00 58.00  ? 144 PHE E CG  1 
ATOM   3691  C CD1 . PHE B 1 148 ? 37.033  -7.374  37.561  1.00 58.69  ? 144 PHE E CD1 1 
ATOM   3692  C CD2 . PHE B 1 148 ? 35.169  -7.959  36.196  1.00 57.09  ? 144 PHE E CD2 1 
ATOM   3693  C CE1 . PHE B 1 148 ? 36.187  -7.140  38.630  1.00 57.18  ? 144 PHE E CE1 1 
ATOM   3694  C CE2 . PHE B 1 148 ? 34.317  -7.722  37.260  1.00 54.81  ? 144 PHE E CE2 1 
ATOM   3695  C CZ  . PHE B 1 148 ? 34.825  -7.315  38.478  1.00 56.73  ? 144 PHE E CZ  1 
ATOM   3696  N N   . ARG B 1 149 ? 38.300  -10.218 32.701  1.00 60.61  ? 145 ARG E N   1 
ATOM   3697  C CA  . ARG B 1 149 ? 39.148  -10.582 31.562  1.00 63.96  ? 145 ARG E CA  1 
ATOM   3698  C C   . ARG B 1 149 ? 39.538  -9.413  30.659  1.00 56.99  ? 145 ARG E C   1 
ATOM   3699  O O   . ARG B 1 149 ? 40.557  -9.479  29.971  1.00 59.62  ? 145 ARG E O   1 
ATOM   3700  C CB  . ARG B 1 149 ? 38.462  -11.665 30.721  1.00 73.94  ? 145 ARG E CB  1 
ATOM   3701  C CG  . ARG B 1 149 ? 38.358  -13.004 31.434  1.00 84.23  ? 145 ARG E CG  1 
ATOM   3702  C CD  . ARG B 1 149 ? 37.801  -14.107 30.554  1.00 99.17  ? 145 ARG E CD  1 
ATOM   3703  N NE  . ARG B 1 149 ? 38.292  -15.418 30.988  1.00 110.32 ? 145 ARG E NE  1 
ATOM   3704  C CZ  . ARG B 1 149 ? 39.444  -15.966 30.596  1.00 110.13 ? 145 ARG E CZ  1 
ATOM   3705  N NH1 . ARG B 1 149 ? 40.245  -15.338 29.738  1.00 112.43 ? 145 ARG E NH1 1 
ATOM   3706  N NH2 . ARG B 1 149 ? 39.798  -17.156 31.063  1.00 106.54 ? 145 ARG E NH2 1 
ATOM   3707  N N   . ASN B 1 150 ? 38.740  -8.350  30.654  1.00 53.80  ? 146 ASN E N   1 
ATOM   3708  C CA  . ASN B 1 150 ? 38.979  -7.223  29.746  1.00 52.18  ? 146 ASN E CA  1 
ATOM   3709  C C   . ASN B 1 150 ? 39.859  -6.130  30.343  1.00 48.29  ? 146 ASN E C   1 
ATOM   3710  O O   . ASN B 1 150 ? 40.099  -5.103  29.707  1.00 44.84  ? 146 ASN E O   1 
ATOM   3711  C CB  . ASN B 1 150 ? 37.647  -6.625  29.287  1.00 55.43  ? 146 ASN E CB  1 
ATOM   3712  C CG  . ASN B 1 150 ? 36.755  -7.651  28.619  1.00 53.61  ? 146 ASN E CG  1 
ATOM   3713  O OD1 . ASN B 1 150 ? 37.236  -8.541  27.924  1.00 54.61  ? 146 ASN E OD1 1 
ATOM   3714  N ND2 . ASN B 1 150 ? 35.449  -7.537  28.834  1.00 60.73  ? 146 ASN E ND2 1 
ATOM   3715  N N   . VAL B 1 151 ? 40.362  -6.370  31.552  1.00 49.07  ? 147 VAL E N   1 
ATOM   3716  C CA  . VAL B 1 151 ? 41.058  -5.352  32.323  1.00 47.43  ? 147 VAL E CA  1 
ATOM   3717  C C   . VAL B 1 151 ? 42.203  -6.024  33.110  1.00 49.22  ? 147 VAL E C   1 
ATOM   3718  O O   . VAL B 1 151 ? 42.070  -7.166  33.552  1.00 49.92  ? 147 VAL E O   1 
ATOM   3719  C CB  . VAL B 1 151 ? 40.037  -4.619  33.233  1.00 45.21  ? 147 VAL E CB  1 
ATOM   3720  C CG1 . VAL B 1 151 ? 39.941  -5.273  34.604  1.00 43.57  ? 147 VAL E CG1 1 
ATOM   3721  C CG2 . VAL B 1 151 ? 40.358  -3.137  33.341  1.00 44.47  ? 147 VAL E CG2 1 
ATOM   3722  N N   . VAL B 1 152 ? 43.330  -5.327  33.257  1.00 48.27  ? 148 VAL E N   1 
ATOM   3723  C CA  . VAL B 1 152 ? 44.555  -5.919  33.819  1.00 44.87  ? 148 VAL E CA  1 
ATOM   3724  C C   . VAL B 1 152 ? 44.937  -5.283  35.152  1.00 43.51  ? 148 VAL E C   1 
ATOM   3725  O O   . VAL B 1 152 ? 45.190  -4.080  35.222  1.00 46.02  ? 148 VAL E O   1 
ATOM   3726  C CB  . VAL B 1 152 ? 45.744  -5.759  32.853  1.00 44.87  ? 148 VAL E CB  1 
ATOM   3727  C CG1 . VAL B 1 152 ? 47.004  -6.359  33.453  1.00 49.99  ? 148 VAL E CG1 1 
ATOM   3728  C CG2 . VAL B 1 152 ? 45.435  -6.404  31.509  1.00 52.13  ? 148 VAL E CG2 1 
ATOM   3729  N N   . TRP B 1 153 ? 44.989  -6.100  36.199  1.00 38.12  ? 149 TRP E N   1 
ATOM   3730  C CA  . TRP B 1 153 ? 45.347  -5.640  37.537  1.00 40.45  ? 149 TRP E CA  1 
ATOM   3731  C C   . TRP B 1 153 ? 46.842  -5.744  37.693  1.00 44.56  ? 149 TRP E C   1 
ATOM   3732  O O   . TRP B 1 153 ? 47.366  -6.784  38.081  1.00 50.49  ? 149 TRP E O   1 
ATOM   3733  C CB  . TRP B 1 153 ? 44.619  -6.489  38.569  1.00 38.28  ? 149 TRP E CB  1 
ATOM   3734  C CG  . TRP B 1 153 ? 44.824  -6.116  40.017  1.00 38.15  ? 149 TRP E CG  1 
ATOM   3735  C CD1 . TRP B 1 153 ? 45.742  -5.224  40.553  1.00 39.73  ? 149 TRP E CD1 1 
ATOM   3736  C CD2 . TRP B 1 153 ? 44.104  -6.660  41.180  1.00 37.50  ? 149 TRP E CD2 1 
ATOM   3737  N NE1 . TRP B 1 153 ? 45.624  -5.167  41.918  1.00 42.63  ? 149 TRP E NE1 1 
ATOM   3738  C CE2 . TRP B 1 153 ? 44.666  -6.004  42.355  1.00 39.75  ? 149 TRP E CE2 1 
ATOM   3739  C CE3 . TRP B 1 153 ? 43.085  -7.577  41.350  1.00 37.82  ? 149 TRP E CE3 1 
ATOM   3740  C CZ2 . TRP B 1 153 ? 44.211  -6.278  43.639  1.00 43.47  ? 149 TRP E CZ2 1 
ATOM   3741  C CZ3 . TRP B 1 153 ? 42.630  -7.845  42.647  1.00 40.19  ? 149 TRP E CZ3 1 
ATOM   3742  C CH2 . TRP B 1 153 ? 43.183  -7.210  43.765  1.00 42.13  ? 149 TRP E CH2 1 
ATOM   3743  N N   . LEU B 1 154 ? 47.545  -4.656  37.394  1.00 40.75  ? 150 LEU E N   1 
ATOM   3744  C CA  . LEU B 1 154 ? 49.005  -4.649  37.421  1.00 42.25  ? 150 LEU E CA  1 
ATOM   3745  C C   . LEU B 1 154 ? 49.560  -4.727  38.848  1.00 46.25  ? 150 LEU E C   1 
ATOM   3746  O O   . LEU B 1 154 ? 49.057  -4.069  39.753  1.00 51.56  ? 150 LEU E O   1 
ATOM   3747  C CB  . LEU B 1 154 ? 49.538  -3.400  36.718  1.00 41.71  ? 150 LEU E CB  1 
ATOM   3748  C CG  . LEU B 1 154 ? 49.197  -3.271  35.229  1.00 42.15  ? 150 LEU E CG  1 
ATOM   3749  C CD1 . LEU B 1 154 ? 49.493  -1.865  34.735  1.00 47.40  ? 150 LEU E CD1 1 
ATOM   3750  C CD2 . LEU B 1 154 ? 49.957  -4.296  34.401  1.00 39.81  ? 150 LEU E CD2 1 
ATOM   3751  N N   . ILE B 1 155 ? 50.592  -5.551  39.030  1.00 50.52  ? 151 ILE E N   1 
ATOM   3752  C CA  . ILE B 1 155 ? 51.279  -5.716  40.313  1.00 48.72  ? 151 ILE E CA  1 
ATOM   3753  C C   . ILE B 1 155 ? 52.780  -5.474  40.104  1.00 51.09  ? 151 ILE E C   1 
ATOM   3754  O O   . ILE B 1 155 ? 53.281  -5.549  38.980  1.00 52.23  ? 151 ILE E O   1 
ATOM   3755  C CB  . ILE B 1 155 ? 50.999  -7.112  40.923  1.00 52.85  ? 151 ILE E CB  1 
ATOM   3756  C CG1 . ILE B 1 155 ? 49.952  -7.013  42.034  1.00 58.71  ? 151 ILE E CG1 1 
ATOM   3757  C CG2 . ILE B 1 155 ? 52.248  -7.736  41.525  1.00 54.28  ? 151 ILE E CG2 1 
ATOM   3758  C CD1 . ILE B 1 155 ? 48.588  -6.579  41.549  1.00 55.80  ? 151 ILE E CD1 1 
ATOM   3759  N N   . LYS B 1 156 ? 53.484  -5.158  41.187  1.00 52.57  ? 152 LYS E N   1 
ATOM   3760  C CA  . LYS B 1 156 ? 54.919  -4.856  41.126  1.00 51.37  ? 152 LYS E CA  1 
ATOM   3761  C C   . LYS B 1 156 ? 55.748  -6.021  40.577  1.00 56.91  ? 152 LYS E C   1 
ATOM   3762  O O   . LYS B 1 156 ? 55.409  -7.187  40.782  1.00 53.76  ? 152 LYS E O   1 
ATOM   3763  C CB  . LYS B 1 156 ? 55.440  -4.478  42.514  1.00 42.18  ? 152 LYS E CB  1 
ATOM   3764  C CG  . LYS B 1 156 ? 55.510  -5.637  43.494  1.00 38.21  ? 152 LYS E CG  1 
ATOM   3765  C CD  . LYS B 1 156 ? 55.819  -5.152  44.899  1.00 39.15  ? 152 LYS E CD  1 
ATOM   3766  C CE  . LYS B 1 156 ? 56.268  -6.295  45.794  1.00 37.96  ? 152 LYS E CE  1 
ATOM   3767  N NZ  . LYS B 1 156 ? 56.239  -5.934  47.237  1.00 38.52  ? 152 LYS E NZ  1 
ATOM   3768  N N   . LYS B 1 157 ? 56.831  -5.687  39.880  1.00 63.53  ? 153 LYS E N   1 
ATOM   3769  C CA  . LYS B 1 157 ? 57.776  -6.676  39.372  1.00 68.46  ? 153 LYS E CA  1 
ATOM   3770  C C   . LYS B 1 157 ? 59.044  -6.615  40.214  1.00 65.74  ? 153 LYS E C   1 
ATOM   3771  O O   . LYS B 1 157 ? 59.544  -5.526  40.512  1.00 60.22  ? 153 LYS E O   1 
ATOM   3772  C CB  . LYS B 1 157 ? 58.097  -6.408  37.901  1.00 74.36  ? 153 LYS E CB  1 
ATOM   3773  C CG  . LYS B 1 157 ? 58.741  -7.586  37.188  1.00 78.49  ? 153 LYS E CG  1 
ATOM   3774  C CD  . LYS B 1 157 ? 58.887  -7.319  35.696  1.00 79.25  ? 153 LYS E CD  1 
ATOM   3775  C CE  . LYS B 1 157 ? 59.378  -8.554  34.954  1.00 77.61  ? 153 LYS E CE  1 
ATOM   3776  N NZ  . LYS B 1 157 ? 59.248  -8.428  33.477  1.00 77.87  ? 153 LYS E NZ  1 
ATOM   3777  N N   . ASP B 1 158 ? 59.558  -7.787  40.584  1.00 70.49  ? 154 ASP E N   1 
ATOM   3778  C CA  . ASP B 1 158 ? 60.642  -7.907  41.560  1.00 74.59  ? 154 ASP E CA  1 
ATOM   3779  C C   . ASP B 1 158 ? 60.165  -7.298  42.883  1.00 78.64  ? 154 ASP E C   1 
ATOM   3780  O O   . ASP B 1 158 ? 59.295  -7.872  43.543  1.00 89.91  ? 154 ASP E O   1 
ATOM   3781  C CB  . ASP B 1 158 ? 61.938  -7.269  41.035  1.00 70.35  ? 154 ASP E CB  1 
ATOM   3782  C CG  . ASP B 1 158 ? 62.391  -7.877  39.721  1.00 67.23  ? 154 ASP E CG  1 
ATOM   3783  O OD1 . ASP B 1 158 ? 62.447  -9.121  39.627  1.00 61.63  ? 154 ASP E OD1 1 
ATOM   3784  O OD2 . ASP B 1 158 ? 62.690  -7.110  38.781  1.00 67.44  ? 154 ASP E OD2 1 
ATOM   3785  N N   . ASN B 1 159 ? 60.715  -6.149  43.266  1.00 70.05  ? 155 ASN E N   1 
ATOM   3786  C CA  . ASN B 1 159 ? 60.172  -5.373  44.376  1.00 65.16  ? 155 ASN E CA  1 
ATOM   3787  C C   . ASN B 1 159 ? 60.194  -3.895  44.011  1.00 56.34  ? 155 ASN E C   1 
ATOM   3788  O O   . ASN B 1 159 ? 60.787  -3.072  44.706  1.00 54.17  ? 155 ASN E O   1 
ATOM   3789  C CB  . ASN B 1 159 ? 60.960  -5.647  45.661  1.00 63.16  ? 155 ASN E CB  1 
ATOM   3790  C CG  . ASN B 1 159 ? 60.544  -6.931  46.333  1.00 69.56  ? 155 ASN E CG  1 
ATOM   3791  O OD1 . ASN B 1 159 ? 59.523  -6.977  47.013  1.00 72.05  ? 155 ASN E OD1 1 
ATOM   3792  N ND2 . ASN B 1 159 ? 61.342  -7.979  46.159  1.00 77.58  ? 155 ASN E ND2 1 
ATOM   3793  N N   . ALA B 1 160 ? 59.541  -3.576  42.900  1.00 51.09  ? 156 ALA E N   1 
ATOM   3794  C CA  . ALA B 1 160 ? 59.530  -2.223  42.366  1.00 49.11  ? 156 ALA E CA  1 
ATOM   3795  C C   . ALA B 1 160 ? 58.292  -1.985  41.492  1.00 50.67  ? 156 ALA E C   1 
ATOM   3796  O O   . ALA B 1 160 ? 57.843  -2.885  40.779  1.00 44.93  ? 156 ALA E O   1 
ATOM   3797  C CB  . ALA B 1 160 ? 60.798  -1.980  41.563  1.00 41.58  ? 156 ALA E CB  1 
ATOM   3798  N N   . TYR B 1 161 ? 57.749  -0.771  41.561  1.00 49.47  ? 157 TYR E N   1 
ATOM   3799  C CA  . TYR B 1 161 ? 56.635  -0.353  40.712  1.00 44.05  ? 157 TYR E CA  1 
ATOM   3800  C C   . TYR B 1 161 ? 57.000  0.993   40.094  1.00 39.61  ? 157 TYR E C   1 
ATOM   3801  O O   . TYR B 1 161 ? 56.645  2.045   40.619  1.00 36.47  ? 157 TYR E O   1 
ATOM   3802  C CB  . TYR B 1 161 ? 55.338  -0.260  41.528  1.00 43.57  ? 157 TYR E CB  1 
ATOM   3803  C CG  . TYR B 1 161 ? 54.054  -0.178  40.710  1.00 40.63  ? 157 TYR E CG  1 
ATOM   3804  C CD1 . TYR B 1 161 ? 53.112  -1.203  40.759  1.00 42.22  ? 157 TYR E CD1 1 
ATOM   3805  C CD2 . TYR B 1 161 ? 53.768  0.931   39.908  1.00 36.75  ? 157 TYR E CD2 1 
ATOM   3806  C CE1 . TYR B 1 161 ? 51.936  -1.130  40.031  1.00 39.07  ? 157 TYR E CE1 1 
ATOM   3807  C CE2 . TYR B 1 161 ? 52.595  1.010   39.177  1.00 38.06  ? 157 TYR E CE2 1 
ATOM   3808  C CZ  . TYR B 1 161 ? 51.682  -0.021  39.241  1.00 39.68  ? 157 TYR E CZ  1 
ATOM   3809  O OH  . TYR B 1 161 ? 50.509  0.065   38.522  1.00 37.48  ? 157 TYR E OH  1 
ATOM   3810  N N   . PRO B 1 162 ? 57.738  0.963   38.979  1.00 45.47  ? 158 PRO E N   1 
ATOM   3811  C CA  . PRO B 1 162 ? 58.100  2.211   38.318  1.00 48.20  ? 158 PRO E CA  1 
ATOM   3812  C C   . PRO B 1 162 ? 56.861  2.932   37.808  1.00 50.96  ? 158 PRO E C   1 
ATOM   3813  O O   . PRO B 1 162 ? 55.874  2.285   37.457  1.00 54.77  ? 158 PRO E O   1 
ATOM   3814  C CB  . PRO B 1 162 ? 58.983  1.755   37.146  1.00 48.93  ? 158 PRO E CB  1 
ATOM   3815  C CG  . PRO B 1 162 ? 59.415  0.370   37.485  1.00 48.67  ? 158 PRO E CG  1 
ATOM   3816  C CD  . PRO B 1 162 ? 58.302  -0.212  38.294  1.00 47.29  ? 158 PRO E CD  1 
ATOM   3817  N N   . THR B 1 163 ? 56.923  4.258   37.764  1.00 47.61  ? 159 THR E N   1 
ATOM   3818  C CA  . THR B 1 163 ? 55.791  5.060   37.328  1.00 47.06  ? 159 THR E CA  1 
ATOM   3819  C C   . THR B 1 163 ? 55.426  4.737   35.877  1.00 50.32  ? 159 THR E C   1 
ATOM   3820  O O   . THR B 1 163 ? 56.274  4.789   34.984  1.00 57.12  ? 159 THR E O   1 
ATOM   3821  C CB  . THR B 1 163 ? 56.091  6.564   37.472  1.00 46.23  ? 159 THR E CB  1 
ATOM   3822  O OG1 . THR B 1 163 ? 56.397  6.851   38.843  1.00 48.32  ? 159 THR E OG1 1 
ATOM   3823  C CG2 . THR B 1 163 ? 54.892  7.408   37.037  1.00 44.20  ? 159 THR E CG2 1 
ATOM   3824  N N   . ILE B 1 164 ? 54.161  4.392   35.660  1.00 48.44  ? 160 ILE E N   1 
ATOM   3825  C CA  . ILE B 1 164 ? 53.642  4.105   34.328  1.00 45.40  ? 160 ILE E CA  1 
ATOM   3826  C C   . ILE B 1 164 ? 53.275  5.399   33.615  1.00 49.73  ? 160 ILE E C   1 
ATOM   3827  O O   . ILE B 1 164 ? 52.719  6.312   34.228  1.00 47.44  ? 160 ILE E O   1 
ATOM   3828  C CB  . ILE B 1 164 ? 52.381  3.230   34.401  1.00 43.89  ? 160 ILE E CB  1 
ATOM   3829  C CG1 . ILE B 1 164 ? 52.725  1.846   34.959  1.00 41.19  ? 160 ILE E CG1 1 
ATOM   3830  C CG2 . ILE B 1 164 ? 51.743  3.112   33.027  1.00 45.77  ? 160 ILE E CG2 1 
ATOM   3831  C CD1 . ILE B 1 164 ? 51.518  1.033   35.370  1.00 37.34  ? 160 ILE E CD1 1 
ATOM   3832  N N   . LYS B 1 165 ? 53.599  5.470   32.325  1.00 48.85  ? 161 LYS E N   1 
ATOM   3833  C CA  . LYS B 1 165 ? 53.184  6.576   31.468  1.00 55.37  ? 161 LYS E CA  1 
ATOM   3834  C C   . LYS B 1 165 ? 52.733  6.022   30.123  1.00 57.43  ? 161 LYS E C   1 
ATOM   3835  O O   . LYS B 1 165 ? 53.478  6.067   29.143  1.00 60.69  ? 161 LYS E O   1 
ATOM   3836  C CB  . LYS B 1 165 ? 54.336  7.559   31.265  1.00 59.13  ? 161 LYS E CB  1 
ATOM   3837  C CG  . LYS B 1 165 ? 54.606  8.462   32.448  1.00 64.04  ? 161 LYS E CG  1 
ATOM   3838  C CD  . LYS B 1 165 ? 55.963  9.145   32.320  1.00 61.60  ? 161 LYS E CD  1 
ATOM   3839  C CE  . LYS B 1 165 ? 56.217  10.157  33.427  1.00 61.14  ? 161 LYS E CE  1 
ATOM   3840  N NZ  . LYS B 1 165 ? 56.977  11.341  32.931  1.00 64.64  ? 161 LYS E NZ  1 
ATOM   3841  N N   . LYS B 1 166 ? 51.513  5.495   30.091  1.00 57.96  ? 162 LYS E N   1 
ATOM   3842  C CA  . LYS B 1 166 ? 50.971  4.863   28.894  1.00 62.16  ? 162 LYS E CA  1 
ATOM   3843  C C   . LYS B 1 166 ? 49.879  5.726   28.285  1.00 59.70  ? 162 LYS E C   1 
ATOM   3844  O O   . LYS B 1 166 ? 49.031  6.261   28.997  1.00 63.02  ? 162 LYS E O   1 
ATOM   3845  C CB  . LYS B 1 166 ? 50.408  3.481   29.231  1.00 65.88  ? 162 LYS E CB  1 
ATOM   3846  C CG  . LYS B 1 166 ? 50.183  2.590   28.018  1.00 67.05  ? 162 LYS E CG  1 
ATOM   3847  C CD  . LYS B 1 166 ? 51.476  1.934   27.541  1.00 68.21  ? 162 LYS E CD  1 
ATOM   3848  C CE  . LYS B 1 166 ? 51.279  1.105   26.270  1.00 72.81  ? 162 LYS E CE  1 
ATOM   3849  N NZ  . LYS B 1 166 ? 51.801  1.809   25.037  1.00 71.38  ? 162 LYS E NZ  1 
ATOM   3850  N N   . GLY B 1 167 ? 49.908  5.851   26.962  1.00 63.40  ? 163 GLY E N   1 
ATOM   3851  C CA  . GLY B 1 167 ? 48.903  6.615   26.230  1.00 65.99  ? 163 GLY E CA  1 
ATOM   3852  C C   . GLY B 1 167 ? 48.349  5.826   25.060  1.00 63.42  ? 163 GLY E C   1 
ATOM   3853  O O   . GLY B 1 167 ? 49.032  4.968   24.502  1.00 60.58  ? 163 GLY E O   1 
ATOM   3854  N N   . TYR B 1 168 ? 47.102  6.111   24.697  1.00 64.37  ? 164 TYR E N   1 
ATOM   3855  C CA  . TYR B 1 168 ? 46.483  5.495   23.531  1.00 59.11  ? 164 TYR E CA  1 
ATOM   3856  C C   . TYR B 1 168 ? 45.753  6.536   22.701  1.00 61.34  ? 164 TYR E C   1 
ATOM   3857  O O   . TYR B 1 168 ? 44.881  7.235   23.207  1.00 61.33  ? 164 TYR E O   1 
ATOM   3858  C CB  . TYR B 1 168 ? 45.511  4.388   23.932  1.00 59.67  ? 164 TYR E CB  1 
ATOM   3859  C CG  . TYR B 1 168 ? 44.836  3.767   22.735  1.00 73.65  ? 164 TYR E CG  1 
ATOM   3860  C CD1 . TYR B 1 168 ? 45.465  2.766   22.000  1.00 81.07  ? 164 TYR E CD1 1 
ATOM   3861  C CD2 . TYR B 1 168 ? 43.582  4.202   22.314  1.00 80.59  ? 164 TYR E CD2 1 
ATOM   3862  C CE1 . TYR B 1 168 ? 44.858  2.203   20.890  1.00 85.04  ? 164 TYR E CE1 1 
ATOM   3863  C CE2 . TYR B 1 168 ? 42.969  3.647   21.204  1.00 84.69  ? 164 TYR E CE2 1 
ATOM   3864  C CZ  . TYR B 1 168 ? 43.610  2.646   20.497  1.00 87.37  ? 164 TYR E CZ  1 
ATOM   3865  O OH  . TYR B 1 168 ? 43.007  2.093   19.392  1.00 91.79  ? 164 TYR E OH  1 
ATOM   3866  N N   . ASN B 1 169 ? 46.124  6.624   21.426  1.00 64.24  ? 165 ASN E N   1 
ATOM   3867  C CA  . ASN B 1 169 ? 45.458  7.494   20.469  1.00 71.71  ? 165 ASN E CA  1 
ATOM   3868  C C   . ASN B 1 169 ? 44.404  6.674   19.736  1.00 71.66  ? 165 ASN E C   1 
ATOM   3869  O O   . ASN B 1 169 ? 44.698  5.603   19.208  1.00 78.35  ? 165 ASN E O   1 
ATOM   3870  C CB  . ASN B 1 169 ? 46.485  8.075   19.485  1.00 71.64  ? 165 ASN E CB  1 
ATOM   3871  C CG  . ASN B 1 169 ? 45.901  9.135   18.557  1.00 74.48  ? 165 ASN E CG  1 
ATOM   3872  O OD1 . ASN B 1 169 ? 44.725  9.097   18.197  1.00 75.64  ? 165 ASN E OD1 1 
ATOM   3873  N ND2 . ASN B 1 169 ? 46.748  10.093  18.159  1.00 78.36  ? 165 ASN E ND2 1 
ATOM   3874  N N   . ASN B 1 170 ? 43.173  7.172   19.719  1.00 72.12  ? 166 ASN E N   1 
ATOM   3875  C CA  . ASN B 1 170 ? 42.094  6.517   18.994  1.00 68.44  ? 166 ASN E CA  1 
ATOM   3876  C C   . ASN B 1 170 ? 42.297  6.736   17.495  1.00 72.42  ? 166 ASN E C   1 
ATOM   3877  O O   . ASN B 1 170 ? 41.984  7.800   16.959  1.00 73.31  ? 166 ASN E O   1 
ATOM   3878  C CB  . ASN B 1 170 ? 40.739  7.055   19.455  1.00 65.10  ? 166 ASN E CB  1 
ATOM   3879  C CG  . ASN B 1 170 ? 39.567  6.296   18.862  1.00 68.08  ? 166 ASN E CG  1 
ATOM   3880  O OD1 . ASN B 1 170 ? 39.737  5.292   18.169  1.00 63.15  ? 166 ASN E OD1 1 
ATOM   3881  N ND2 . ASN B 1 170 ? 38.358  6.773   19.145  1.00 68.94  ? 166 ASN E ND2 1 
ATOM   3882  N N   . THR B 1 171 ? 42.856  5.724   16.837  1.00 78.08  ? 167 THR E N   1 
ATOM   3883  C CA  . THR B 1 171 ? 43.126  5.774   15.401  1.00 79.44  ? 167 THR E CA  1 
ATOM   3884  C C   . THR B 1 171 ? 41.898  5.351   14.587  1.00 78.58  ? 167 THR E C   1 
ATOM   3885  O O   . THR B 1 171 ? 41.858  5.536   13.371  1.00 87.56  ? 167 THR E O   1 
ATOM   3886  C CB  . THR B 1 171 ? 44.330  4.873   15.032  1.00 81.17  ? 167 THR E CB  1 
ATOM   3887  O OG1 . THR B 1 171 ? 44.578  4.953   13.623  1.00 99.25  ? 167 THR E OG1 1 
ATOM   3888  C CG2 . THR B 1 171 ? 44.074  3.413   15.426  1.00 76.99  ? 167 THR E CG2 1 
ATOM   3889  N N   . ASN B 1 172 ? 40.899  4.794   15.267  1.00 75.95  ? 168 ASN E N   1 
ATOM   3890  C CA  . ASN B 1 172 ? 39.669  4.335   14.626  1.00 67.59  ? 168 ASN E CA  1 
ATOM   3891  C C   . ASN B 1 172 ? 38.764  5.519   14.275  1.00 73.95  ? 168 ASN E C   1 
ATOM   3892  O O   . ASN B 1 172 ? 39.002  6.639   14.724  1.00 75.96  ? 168 ASN E O   1 
ATOM   3893  C CB  . ASN B 1 172 ? 38.933  3.359   15.546  1.00 62.14  ? 168 ASN E CB  1 
ATOM   3894  C CG  . ASN B 1 172 ? 39.855  2.317   16.154  1.00 64.50  ? 168 ASN E CG  1 
ATOM   3895  O OD1 . ASN B 1 172 ? 40.323  1.406   15.471  1.00 74.25  ? 168 ASN E OD1 1 
ATOM   3896  N ND2 . ASN B 1 172 ? 40.118  2.448   17.449  1.00 58.98  ? 168 ASN E ND2 1 
ATOM   3897  N N   . GLN B 1 173 ? 37.737  5.274   13.463  1.00 85.07  ? 169 GLN E N   1 
ATOM   3898  C CA  . GLN B 1 173 ? 36.791  6.328   13.065  1.00 93.51  ? 169 GLN E CA  1 
ATOM   3899  C C   . GLN B 1 173 ? 35.583  6.435   13.986  1.00 88.64  ? 169 GLN E C   1 
ATOM   3900  O O   . GLN B 1 173 ? 34.756  7.328   13.817  1.00 83.38  ? 169 GLN E O   1 
ATOM   3901  C CB  . GLN B 1 173 ? 36.295  6.113   11.634  1.00 104.31 ? 169 GLN E CB  1 
ATOM   3902  C CG  . GLN B 1 173 ? 37.278  6.565   10.583  1.00 111.64 ? 169 GLN E CG  1 
ATOM   3903  C CD  . GLN B 1 173 ? 38.393  5.556   10.355  1.00 119.48 ? 169 GLN E CD  1 
ATOM   3904  O OE1 . GLN B 1 173 ? 39.507  5.703   10.866  1.00 128.77 ? 169 GLN E OE1 1 
ATOM   3905  N NE2 . GLN B 1 173 ? 38.086  4.507   9.600   1.00 120.13 ? 169 GLN E NE2 1 
ATOM   3906  N N   . GLU B 1 174 ? 35.479  5.519   14.943  1.00 87.89  ? 170 GLU E N   1 
ATOM   3907  C CA  . GLU B 1 174 ? 34.354  5.494   15.873  1.00 86.11  ? 170 GLU E CA  1 
ATOM   3908  C C   . GLU B 1 174 ? 34.786  5.849   17.293  1.00 78.87  ? 170 GLU E C   1 
ATOM   3909  O O   . GLU B 1 174 ? 35.963  5.751   17.639  1.00 70.71  ? 170 GLU E O   1 
ATOM   3910  C CB  . GLU B 1 174 ? 33.693  4.116   15.863  1.00 88.31  ? 170 GLU E CB  1 
ATOM   3911  C CG  . GLU B 1 174 ? 32.901  3.818   14.596  1.00 99.82  ? 170 GLU E CG  1 
ATOM   3912  C CD  . GLU B 1 174 ? 33.676  3.025   13.555  1.00 111.57 ? 170 GLU E CD  1 
ATOM   3913  O OE1 . GLU B 1 174 ? 33.030  2.497   12.627  1.00 107.51 ? 170 GLU E OE1 1 
ATOM   3914  O OE2 . GLU B 1 174 ? 34.918  2.919   13.656  1.00 121.24 ? 170 GLU E OE2 1 
ATOM   3915  N N   . ASP B 1 175 ? 33.820  6.270   18.105  1.00 73.69  ? 171 ASP E N   1 
ATOM   3916  C CA  . ASP B 1 175 ? 34.055  6.544   19.520  1.00 66.72  ? 171 ASP E CA  1 
ATOM   3917  C C   . ASP B 1 175 ? 34.489  5.263   20.228  1.00 62.15  ? 171 ASP E C   1 
ATOM   3918  O O   . ASP B 1 175 ? 34.030  4.169   19.882  1.00 52.93  ? 171 ASP E O   1 
ATOM   3919  C CB  . ASP B 1 175 ? 32.783  7.083   20.191  1.00 70.91  ? 171 ASP E CB  1 
ATOM   3920  C CG  . ASP B 1 175 ? 32.429  8.496   19.752  1.00 65.87  ? 171 ASP E CG  1 
ATOM   3921  O OD1 . ASP B 1 175 ? 33.328  9.238   19.312  1.00 70.18  ? 171 ASP E OD1 1 
ATOM   3922  O OD2 . ASP B 1 175 ? 31.243  8.871   19.865  1.00 62.06  ? 171 ASP E OD2 1 
ATOM   3923  N N   . LEU B 1 176 ? 35.372  5.411   21.214  1.00 57.12  ? 172 LEU E N   1 
ATOM   3924  C CA  . LEU B 1 176 ? 35.841  4.282   22.015  1.00 52.80  ? 172 LEU E CA  1 
ATOM   3925  C C   . LEU B 1 176 ? 35.408  4.424   23.469  1.00 49.37  ? 172 LEU E C   1 
ATOM   3926  O O   . LEU B 1 176 ? 35.708  5.423   24.116  1.00 42.17  ? 172 LEU E O   1 
ATOM   3927  C CB  . LEU B 1 176 ? 37.366  4.177   21.958  1.00 58.54  ? 172 LEU E CB  1 
ATOM   3928  C CG  . LEU B 1 176 ? 37.974  3.326   20.850  1.00 61.36  ? 172 LEU E CG  1 
ATOM   3929  C CD1 . LEU B 1 176 ? 39.471  3.563   20.797  1.00 64.65  ? 172 LEU E CD1 1 
ATOM   3930  C CD2 . LEU B 1 176 ? 37.672  1.854   21.082  1.00 66.52  ? 172 LEU E CD2 1 
ATOM   3931  N N   . LEU B 1 177 ? 34.704  3.417   23.972  1.00 53.94  ? 173 LEU E N   1 
ATOM   3932  C CA  . LEU B 1 177 ? 34.387  3.329   25.390  1.00 50.16  ? 173 LEU E CA  1 
ATOM   3933  C C   . LEU B 1 177 ? 35.573  2.666   26.080  1.00 55.72  ? 173 LEU E C   1 
ATOM   3934  O O   . LEU B 1 177 ? 35.864  1.495   25.825  1.00 56.92  ? 173 LEU E O   1 
ATOM   3935  C CB  . LEU B 1 177 ? 33.107  2.512   25.612  1.00 43.87  ? 173 LEU E CB  1 
ATOM   3936  C CG  . LEU B 1 177 ? 32.745  2.185   27.066  1.00 44.09  ? 173 LEU E CG  1 
ATOM   3937  C CD1 . LEU B 1 177 ? 32.545  3.470   27.857  1.00 40.94  ? 173 LEU E CD1 1 
ATOM   3938  C CD2 . LEU B 1 177 ? 31.514  1.295   27.152  1.00 41.93  ? 173 LEU E CD2 1 
ATOM   3939  N N   . VAL B 1 178 ? 36.257  3.422   26.940  1.00 59.45  ? 174 VAL E N   1 
ATOM   3940  C CA  . VAL B 1 178 ? 37.420  2.916   27.675  1.00 55.20  ? 174 VAL E CA  1 
ATOM   3941  C C   . VAL B 1 178 ? 37.107  2.828   29.163  1.00 49.86  ? 174 VAL E C   1 
ATOM   3942  O O   . VAL B 1 178 ? 36.538  3.751   29.736  1.00 44.71  ? 174 VAL E O   1 
ATOM   3943  C CB  . VAL B 1 178 ? 38.656  3.814   27.493  1.00 51.20  ? 174 VAL E CB  1 
ATOM   3944  C CG1 . VAL B 1 178 ? 39.867  3.168   28.147  1.00 47.82  ? 174 VAL E CG1 1 
ATOM   3945  C CG2 . VAL B 1 178 ? 38.921  4.070   26.017  1.00 50.61  ? 174 VAL E CG2 1 
ATOM   3946  N N   . LEU B 1 179 ? 37.489  1.709   29.769  1.00 53.44  ? 175 LEU E N   1 
ATOM   3947  C CA  . LEU B 1 179 ? 37.248  1.450   31.183  1.00 51.11  ? 175 LEU E CA  1 
ATOM   3948  C C   . LEU B 1 179 ? 38.572  1.276   31.905  1.00 53.07  ? 175 LEU E C   1 
ATOM   3949  O O   . LEU B 1 179 ? 39.540  0.783   31.330  1.00 58.48  ? 175 LEU E O   1 
ATOM   3950  C CB  . LEU B 1 179 ? 36.428  0.175   31.353  1.00 54.29  ? 175 LEU E CB  1 
ATOM   3951  C CG  . LEU B 1 179 ? 35.076  0.110   30.639  1.00 59.45  ? 175 LEU E CG  1 
ATOM   3952  C CD1 . LEU B 1 179 ? 34.712  -1.340  30.366  1.00 57.90  ? 175 LEU E CD1 1 
ATOM   3953  C CD2 . LEU B 1 179 ? 33.994  0.790   31.461  1.00 53.69  ? 175 LEU E CD2 1 
ATOM   3954  N N   . TRP B 1 180 ? 38.611  1.684   33.166  1.00 49.03  ? 176 TRP E N   1 
ATOM   3955  C CA  . TRP B 1 180 ? 39.768  1.448   34.015  1.00 47.94  ? 176 TRP E CA  1 
ATOM   3956  C C   . TRP B 1 180 ? 39.320  1.537   35.435  1.00 47.28  ? 176 TRP E C   1 
ATOM   3957  O O   . TRP B 1 180 ? 38.198  1.964   35.698  1.00 53.41  ? 176 TRP E O   1 
ATOM   3958  C CB  . TRP B 1 180 ? 40.869  2.464   33.731  1.00 44.53  ? 176 TRP E CB  1 
ATOM   3959  C CG  . TRP B 1 180 ? 40.488  3.873   34.089  1.00 43.07  ? 176 TRP E CG  1 
ATOM   3960  C CD1 . TRP B 1 180 ? 40.753  4.546   35.273  1.00 42.90  ? 176 TRP E CD1 1 
ATOM   3961  C CD2 . TRP B 1 180 ? 39.747  4.833   33.265  1.00 46.37  ? 176 TRP E CD2 1 
ATOM   3962  N NE1 . TRP B 1 180 ? 40.245  5.818   35.237  1.00 45.36  ? 176 TRP E NE1 1 
ATOM   3963  C CE2 . TRP B 1 180 ? 39.630  6.053   34.064  1.00 43.57  ? 176 TRP E CE2 1 
ATOM   3964  C CE3 . TRP B 1 180 ? 39.190  4.806   31.993  1.00 48.26  ? 176 TRP E CE3 1 
ATOM   3965  C CZ2 . TRP B 1 180 ? 38.981  7.179   33.593  1.00 43.02  ? 176 TRP E CZ2 1 
ATOM   3966  C CZ3 . TRP B 1 180 ? 38.536  5.953   31.528  1.00 48.90  ? 176 TRP E CZ3 1 
ATOM   3967  C CH2 . TRP B 1 180 ? 38.435  7.110   32.312  1.00 45.73  ? 176 TRP E CH2 1 
ATOM   3968  N N   . GLY B 1 181 ? 40.183  1.140   36.365  1.00 47.95  ? 177 GLY E N   1 
ATOM   3969  C CA  . GLY B 1 181 ? 39.820  1.149   37.776  1.00 47.16  ? 177 GLY E CA  1 
ATOM   3970  C C   . GLY B 1 181 ? 40.963  1.412   38.730  1.00 49.89  ? 177 GLY E C   1 
ATOM   3971  O O   . GLY B 1 181 ? 42.129  1.472   38.332  1.00 53.57  ? 177 GLY E O   1 
ATOM   3972  N N   . ILE B 1 182 ? 40.605  1.582   39.999  1.00 45.60  ? 178 ILE E N   1 
ATOM   3973  C CA  . ILE B 1 182 ? 41.562  1.814   41.072  1.00 43.12  ? 178 ILE E CA  1 
ATOM   3974  C C   . ILE B 1 182 ? 41.273  0.821   42.191  1.00 41.22  ? 178 ILE E C   1 
ATOM   3975  O O   . ILE B 1 182 ? 40.108  0.506   42.462  1.00 47.59  ? 178 ILE E O   1 
ATOM   3976  C CB  . ILE B 1 182 ? 41.477  3.267   41.594  1.00 49.74  ? 178 ILE E CB  1 
ATOM   3977  C CG1 . ILE B 1 182 ? 42.549  3.544   42.655  1.00 50.01  ? 178 ILE E CG1 1 
ATOM   3978  C CG2 . ILE B 1 182 ? 40.091  3.566   42.157  1.00 50.34  ? 178 ILE E CG2 1 
ATOM   3979  C CD1 . ILE B 1 182 ? 42.791  5.015   42.902  1.00 48.96  ? 178 ILE E CD1 1 
ATOM   3980  N N   . HIS B 1 183 ? 42.334  0.320   42.820  1.00 40.41  ? 179 HIS E N   1 
ATOM   3981  C CA  . HIS B 1 183 ? 42.218  -0.651  43.904  1.00 40.60  ? 179 HIS E CA  1 
ATOM   3982  C C   . HIS B 1 183 ? 42.414  0.018   45.229  1.00 42.22  ? 179 HIS E C   1 
ATOM   3983  O O   . HIS B 1 183 ? 43.446  0.638   45.461  1.00 42.83  ? 179 HIS E O   1 
ATOM   3984  C CB  . HIS B 1 183 ? 43.242  -1.766  43.736  1.00 41.68  ? 179 HIS E CB  1 
ATOM   3985  C CG  . HIS B 1 183 ? 43.313  -2.710  44.914  1.00 44.99  ? 179 HIS E CG  1 
ATOM   3986  N ND1 . HIS B 1 183 ? 44.414  -2.838  45.677  1.00 47.17  ? 179 HIS E ND1 1 
ATOM   3987  C CD2 . HIS B 1 183 ? 42.358  -3.571  45.455  1.00 47.38  ? 179 HIS E CD2 1 
ATOM   3988  C CE1 . HIS B 1 183 ? 44.182  -3.745  46.650  1.00 43.78  ? 179 HIS E CE1 1 
ATOM   3989  N NE2 . HIS B 1 183 ? 42.926  -4.190  46.514  1.00 46.75  ? 179 HIS E NE2 1 
ATOM   3990  N N   . HIS B 1 184 ? 41.419  -0.096  46.104  1.00 40.63  ? 180 HIS E N   1 
ATOM   3991  C CA  . HIS B 1 184 ? 41.512  0.413   47.467  1.00 41.30  ? 180 HIS E CA  1 
ATOM   3992  C C   . HIS B 1 184 ? 41.846  -0.729  48.393  1.00 41.10  ? 180 HIS E C   1 
ATOM   3993  O O   . HIS B 1 184 ? 40.979  -1.556  48.688  1.00 39.64  ? 180 HIS E O   1 
ATOM   3994  C CB  . HIS B 1 184 ? 40.188  1.042   47.888  1.00 44.31  ? 180 HIS E CB  1 
ATOM   3995  C CG  . HIS B 1 184 ? 39.694  2.123   46.954  1.00 44.14  ? 180 HIS E CG  1 
ATOM   3996  N ND1 . HIS B 1 184 ? 40.326  3.300   46.813  1.00 45.68  ? 180 HIS E ND1 1 
ATOM   3997  C CD2 . HIS B 1 184 ? 38.575  2.175   46.128  1.00 41.54  ? 180 HIS E CD2 1 
ATOM   3998  C CE1 . HIS B 1 184 ? 39.657  4.068   45.938  1.00 42.95  ? 180 HIS E CE1 1 
ATOM   3999  N NE2 . HIS B 1 184 ? 38.584  3.377   45.515  1.00 39.37  ? 180 HIS E NE2 1 
ATOM   4000  N N   . PRO B 1 185 ? 43.102  -0.801  48.870  1.00 39.73  ? 181 PRO E N   1 
ATOM   4001  C CA  . PRO B 1 185 ? 43.492  -1.898  49.753  1.00 41.26  ? 181 PRO E CA  1 
ATOM   4002  C C   . PRO B 1 185 ? 42.984  -1.732  51.186  1.00 40.95  ? 181 PRO E C   1 
ATOM   4003  O O   . PRO B 1 185 ? 42.476  -0.672  51.549  1.00 39.81  ? 181 PRO E O   1 
ATOM   4004  C CB  . PRO B 1 185 ? 45.020  -1.849  49.713  1.00 44.31  ? 181 PRO E CB  1 
ATOM   4005  C CG  . PRO B 1 185 ? 45.335  -0.420  49.480  1.00 45.53  ? 181 PRO E CG  1 
ATOM   4006  C CD  . PRO B 1 185 ? 44.205  0.154   48.671  1.00 43.03  ? 181 PRO E CD  1 
ATOM   4007  N N   . ASN B 1 186 ? 43.138  -2.782  51.988  1.00 46.83  ? 182 ASN E N   1 
ATOM   4008  C CA  . ASN B 1 186 ? 42.610  -2.811  53.352  1.00 51.03  ? 182 ASN E CA  1 
ATOM   4009  C C   . ASN B 1 186 ? 43.515  -2.119  54.371  1.00 49.65  ? 182 ASN E C   1 
ATOM   4010  O O   . ASN B 1 186 ? 43.021  -1.559  55.353  1.00 52.57  ? 182 ASN E O   1 
ATOM   4011  C CB  . ASN B 1 186 ? 42.354  -4.257  53.786  1.00 58.80  ? 182 ASN E CB  1 
ATOM   4012  C CG  . ASN B 1 186 ? 41.400  -4.354  54.965  1.00 73.90  ? 182 ASN E CG  1 
ATOM   4013  O OD1 . ASN B 1 186 ? 40.314  -3.764  54.959  1.00 86.27  ? 182 ASN E OD1 1 
ATOM   4014  N ND2 . ASN B 1 186 ? 41.799  -5.105  55.985  1.00 75.58  ? 182 ASN E ND2 1 
ATOM   4015  N N   . ASP B 1 187 ? 44.830  -2.166  54.143  1.00 55.11  ? 183 ASP E N   1 
ATOM   4016  C CA  . ASP B 1 187 ? 45.808  -1.537  55.042  1.00 62.88  ? 183 ASP E CA  1 
ATOM   4017  C C   . ASP B 1 187 ? 47.133  -1.202  54.338  1.00 58.92  ? 183 ASP E C   1 
ATOM   4018  O O   . ASP B 1 187 ? 47.346  -1.565  53.182  1.00 54.58  ? 183 ASP E O   1 
ATOM   4019  C CB  . ASP B 1 187 ? 46.058  -2.426  56.270  1.00 67.18  ? 183 ASP E CB  1 
ATOM   4020  C CG  . ASP B 1 187 ? 46.444  -3.847  55.900  1.00 72.62  ? 183 ASP E CG  1 
ATOM   4021  O OD1 . ASP B 1 187 ? 45.792  -4.783  56.408  1.00 83.28  ? 183 ASP E OD1 1 
ATOM   4022  O OD2 . ASP B 1 187 ? 47.390  -4.031  55.105  1.00 73.84  ? 183 ASP E OD2 1 
ATOM   4023  N N   . GLU B 1 188 ? 48.018  -0.515  55.058  1.00 58.68  ? 184 GLU E N   1 
ATOM   4024  C CA  . GLU B 1 188 ? 49.295  -0.044  54.511  1.00 55.66  ? 184 GLU E CA  1 
ATOM   4025  C C   . GLU B 1 188 ? 50.242  -1.194  54.142  1.00 49.08  ? 184 GLU E C   1 
ATOM   4026  O O   . GLU B 1 188 ? 51.070  -1.056  53.241  1.00 42.01  ? 184 GLU E O   1 
ATOM   4027  C CB  . GLU B 1 188 ? 49.988  0.892   55.510  1.00 61.78  ? 184 GLU E CB  1 
ATOM   4028  C CG  . GLU B 1 188 ? 49.196  2.139   55.906  1.00 65.81  ? 184 GLU E CG  1 
ATOM   4029  C CD  . GLU B 1 188 ? 49.429  3.328   54.985  1.00 72.66  ? 184 GLU E CD  1 
ATOM   4030  O OE1 . GLU B 1 188 ? 49.393  4.474   55.483  1.00 76.68  ? 184 GLU E OE1 1 
ATOM   4031  O OE2 . GLU B 1 188 ? 49.650  3.124   53.771  1.00 74.69  ? 184 GLU E OE2 1 
ATOM   4032  N N   . ALA B 1 189 ? 50.125  -2.319  54.846  1.00 49.21  ? 185 ALA E N   1 
ATOM   4033  C CA  . ALA B 1 189 ? 50.940  -3.504  54.556  1.00 47.54  ? 185 ALA E CA  1 
ATOM   4034  C C   . ALA B 1 189 ? 50.583  -4.096  53.200  1.00 46.49  ? 185 ALA E C   1 
ATOM   4035  O O   . ALA B 1 189 ? 51.460  -4.430  52.409  1.00 47.96  ? 185 ALA E O   1 
ATOM   4036  C CB  . ALA B 1 189 ? 50.771  -4.547  55.647  1.00 46.08  ? 185 ALA E CB  1 
ATOM   4037  N N   . GLU B 1 190 ? 49.284  -4.225  52.951  1.00 51.45  ? 186 GLU E N   1 
ATOM   4038  C CA  . GLU B 1 190 ? 48.765  -4.686  51.664  1.00 48.32  ? 186 GLU E CA  1 
ATOM   4039  C C   . GLU B 1 190 ? 49.192  -3.744  50.536  1.00 41.15  ? 186 GLU E C   1 
ATOM   4040  O O   . GLU B 1 190 ? 49.598  -4.187  49.464  1.00 38.71  ? 186 GLU E O   1 
ATOM   4041  C CB  . GLU B 1 190 ? 47.238  -4.768  51.743  1.00 55.98  ? 186 GLU E CB  1 
ATOM   4042  C CG  . GLU B 1 190 ? 46.563  -5.465  50.571  1.00 59.96  ? 186 GLU E CG  1 
ATOM   4043  C CD  . GLU B 1 190 ? 45.070  -5.652  50.791  1.00 70.32  ? 186 GLU E CD  1 
ATOM   4044  O OE1 . GLU B 1 190 ? 44.291  -5.392  49.848  1.00 76.82  ? 186 GLU E OE1 1 
ATOM   4045  O OE2 . GLU B 1 190 ? 44.670  -6.049  51.910  1.00 76.43  ? 186 GLU E OE2 1 
ATOM   4046  N N   . GLN B 1 191 ? 49.096  -2.442  50.795  1.00 40.09  ? 187 GLN E N   1 
ATOM   4047  C CA  . GLN B 1 191 ? 49.491  -1.404  49.838  1.00 41.43  ? 187 GLN E CA  1 
ATOM   4048  C C   . GLN B 1 191 ? 50.866  -1.685  49.248  1.00 42.85  ? 187 GLN E C   1 
ATOM   4049  O O   . GLN B 1 191 ? 51.045  -1.717  48.025  1.00 42.82  ? 187 GLN E O   1 
ATOM   4050  C CB  . GLN B 1 191 ? 49.569  -0.053  50.555  1.00 44.36  ? 187 GLN E CB  1 
ATOM   4051  C CG  . GLN B 1 191 ? 48.832  1.086   49.888  1.00 47.87  ? 187 GLN E CG  1 
ATOM   4052  C CD  . GLN B 1 191 ? 49.019  1.131   48.388  1.00 44.20  ? 187 GLN E CD  1 
ATOM   4053  O OE1 . GLN B 1 191 ? 48.109  0.804   47.638  1.00 50.79  ? 187 GLN E OE1 1 
ATOM   4054  N NE2 . GLN B 1 191 ? 50.198  1.535   47.947  1.00 36.75  ? 187 GLN E NE2 1 
ATOM   4055  N N   . THR B 1 192 ? 51.827  -1.914  50.144  1.00 39.85  ? 188 THR E N   1 
ATOM   4056  C CA  . THR B 1 192 ? 53.234  -2.022  49.763  1.00 38.02  ? 188 THR E CA  1 
ATOM   4057  C C   . THR B 1 192 ? 53.575  -3.418  49.288  1.00 40.98  ? 188 THR E C   1 
ATOM   4058  O O   . THR B 1 192 ? 54.501  -3.574  48.511  1.00 39.85  ? 188 THR E O   1 
ATOM   4059  C CB  . THR B 1 192 ? 54.225  -1.718  50.908  1.00 37.20  ? 188 THR E CB  1 
ATOM   4060  O OG1 . THR B 1 192 ? 53.873  -2.495  52.048  1.00 39.83  ? 188 THR E OG1 1 
ATOM   4061  C CG2 . THR B 1 192 ? 54.222  -0.241  51.251  1.00 36.37  ? 188 THR E CG2 1 
ATOM   4062  N N   . ARG B 1 193 ? 52.884  -4.430  49.813  1.00 43.81  ? 189 ARG E N   1 
ATOM   4063  C CA  . ARG B 1 193 ? 53.008  -5.794  49.288  1.00 46.65  ? 189 ARG E CA  1 
ATOM   4064  C C   . ARG B 1 193 ? 52.746  -5.836  47.790  1.00 51.81  ? 189 ARG E C   1 
ATOM   4065  O O   . ARG B 1 193 ? 53.502  -6.447  47.034  1.00 52.15  ? 189 ARG E O   1 
ATOM   4066  C CB  . ARG B 1 193 ? 52.022  -6.768  49.948  1.00 49.96  ? 189 ARG E CB  1 
ATOM   4067  C CG  . ARG B 1 193 ? 52.679  -7.838  50.804  1.00 59.93  ? 189 ARG E CG  1 
ATOM   4068  C CD  . ARG B 1 193 ? 51.997  -9.201  50.707  1.00 61.25  ? 189 ARG E CD  1 
ATOM   4069  N NE  . ARG B 1 193 ? 50.561  -9.154  50.410  1.00 64.98  ? 189 ARG E NE  1 
ATOM   4070  C CZ  . ARG B 1 193 ? 49.608  -8.794  51.269  1.00 63.11  ? 189 ARG E CZ  1 
ATOM   4071  N NH1 . ARG B 1 193 ? 49.904  -8.409  52.513  1.00 58.92  ? 189 ARG E NH1 1 
ATOM   4072  N NH2 . ARG B 1 193 ? 48.342  -8.807  50.872  1.00 54.41  ? 189 ARG E NH2 1 
ATOM   4073  N N   . LEU B 1 194 ? 51.651  -5.202  47.377  1.00 49.66  ? 190 LEU E N   1 
ATOM   4074  C CA  . LEU B 1 194 ? 51.195  -5.276  45.994  1.00 50.24  ? 190 LEU E CA  1 
ATOM   4075  C C   . LEU B 1 194 ? 51.960  -4.343  45.059  1.00 48.07  ? 190 LEU E C   1 
ATOM   4076  O O   . LEU B 1 194 ? 52.333  -4.749  43.956  1.00 49.41  ? 190 LEU E O   1 
ATOM   4077  C CB  . LEU B 1 194 ? 49.694  -4.979  45.914  1.00 53.43  ? 190 LEU E CB  1 
ATOM   4078  C CG  . LEU B 1 194 ? 48.781  -5.973  46.641  1.00 53.69  ? 190 LEU E CG  1 
ATOM   4079  C CD1 . LEU B 1 194 ? 47.342  -5.484  46.665  1.00 49.85  ? 190 LEU E CD1 1 
ATOM   4080  C CD2 . LEU B 1 194 ? 48.874  -7.348  45.997  1.00 56.66  ? 190 LEU E CD2 1 
ATOM   4081  N N   . TYR B 1 195 ? 52.179  -3.098  45.487  1.00 46.39  ? 191 TYR E N   1 
ATOM   4082  C CA  . TYR B 1 195 ? 52.744  -2.071  44.600  1.00 51.25  ? 191 TYR E CA  1 
ATOM   4083  C C   . TYR B 1 195 ? 54.000  -1.359  45.123  1.00 54.88  ? 191 TYR E C   1 
ATOM   4084  O O   . TYR B 1 195 ? 54.420  -0.356  44.541  1.00 52.97  ? 191 TYR E O   1 
ATOM   4085  C CB  . TYR B 1 195 ? 51.677  -1.020  44.271  1.00 53.45  ? 191 TYR E CB  1 
ATOM   4086  C CG  . TYR B 1 195 ? 50.273  -1.565  44.159  1.00 53.47  ? 191 TYR E CG  1 
ATOM   4087  C CD1 . TYR B 1 195 ? 49.372  -1.432  45.209  1.00 53.89  ? 191 TYR E CD1 1 
ATOM   4088  C CD2 . TYR B 1 195 ? 49.846  -2.216  43.006  1.00 51.16  ? 191 TYR E CD2 1 
ATOM   4089  C CE1 . TYR B 1 195 ? 48.086  -1.931  45.116  1.00 51.16  ? 191 TYR E CE1 1 
ATOM   4090  C CE2 . TYR B 1 195 ? 48.560  -2.715  42.902  1.00 48.80  ? 191 TYR E CE2 1 
ATOM   4091  C CZ  . TYR B 1 195 ? 47.686  -2.572  43.961  1.00 49.09  ? 191 TYR E CZ  1 
ATOM   4092  O OH  . TYR B 1 195 ? 46.408  -3.062  43.867  1.00 48.56  ? 191 TYR E OH  1 
ATOM   4093  N N   . GLN B 1 196 ? 54.593  -1.862  46.207  1.00 56.49  ? 192 GLN E N   1 
ATOM   4094  C CA  . GLN B 1 196 ? 55.823  -1.291  46.798  1.00 54.37  ? 192 GLN E CA  1 
ATOM   4095  C C   . GLN B 1 196 ? 55.710  0.145   47.320  1.00 49.83  ? 192 GLN E C   1 
ATOM   4096  O O   . GLN B 1 196 ? 56.101  0.424   48.450  1.00 49.98  ? 192 GLN E O   1 
ATOM   4097  C CB  . GLN B 1 196 ? 57.006  -1.369  45.820  1.00 60.98  ? 192 GLN E CB  1 
ATOM   4098  C CG  . GLN B 1 196 ? 58.019  -2.465  46.131  1.00 64.63  ? 192 GLN E CG  1 
ATOM   4099  C CD  . GLN B 1 196 ? 58.869  -2.221  47.384  1.00 67.10  ? 192 GLN E CD  1 
ATOM   4100  O OE1 . GLN B 1 196 ? 58.958  -1.102  47.914  1.00 79.95  ? 192 GLN E OE1 1 
ATOM   4101  N NE2 . GLN B 1 196 ? 59.521  -3.282  47.850  1.00 72.14  ? 192 GLN E NE2 1 
ATOM   4102  N N   . ASN B 1 197 ? 55.208  1.053   46.488  1.00 45.14  ? 193 ASN E N   1 
ATOM   4103  C CA  . ASN B 1 197 ? 55.127  2.469   46.834  1.00 43.91  ? 193 ASN E CA  1 
ATOM   4104  C C   . ASN B 1 197 ? 53.971  2.723   47.806  1.00 51.38  ? 193 ASN E C   1 
ATOM   4105  O O   . ASN B 1 197 ? 52.844  2.313   47.538  1.00 50.06  ? 193 ASN E O   1 
ATOM   4106  C CB  . ASN B 1 197 ? 54.929  3.315   45.575  1.00 45.36  ? 193 ASN E CB  1 
ATOM   4107  C CG  . ASN B 1 197 ? 55.918  2.979   44.476  1.00 44.59  ? 193 ASN E CG  1 
ATOM   4108  O OD1 . ASN B 1 197 ? 55.545  2.881   43.311  1.00 44.54  ? 193 ASN E OD1 1 
ATOM   4109  N ND2 . ASN B 1 197 ? 57.179  2.792   44.842  1.00 43.73  ? 193 ASN E ND2 1 
ATOM   4110  N N   . PRO B 1 198 ? 54.242  3.404   48.936  1.00 55.01  ? 194 PRO E N   1 
ATOM   4111  C CA  . PRO B 1 198 ? 53.217  3.634   49.959  1.00 48.40  ? 194 PRO E CA  1 
ATOM   4112  C C   . PRO B 1 198 ? 52.196  4.723   49.608  1.00 48.75  ? 194 PRO E C   1 
ATOM   4113  O O   . PRO B 1 198 ? 51.022  4.580   49.945  1.00 50.34  ? 194 PRO E O   1 
ATOM   4114  C CB  . PRO B 1 198 ? 54.037  4.047   51.183  1.00 52.16  ? 194 PRO E CB  1 
ATOM   4115  C CG  . PRO B 1 198 ? 55.261  4.677   50.614  1.00 55.78  ? 194 PRO E CG  1 
ATOM   4116  C CD  . PRO B 1 198 ? 55.557  3.931   49.345  1.00 58.24  ? 194 PRO E CD  1 
ATOM   4117  N N   . THR B 1 199 ? 52.642  5.799   48.959  1.00 45.81  ? 195 THR E N   1 
ATOM   4118  C CA  . THR B 1 199 ? 51.766  6.906   48.568  1.00 44.27  ? 195 THR E CA  1 
ATOM   4119  C C   . THR B 1 199 ? 51.630  6.953   47.052  1.00 45.35  ? 195 THR E C   1 
ATOM   4120  O O   . THR B 1 199 ? 52.612  7.158   46.341  1.00 47.60  ? 195 THR E O   1 
ATOM   4121  C CB  . THR B 1 199 ? 52.321  8.258   49.044  1.00 44.52  ? 195 THR E CB  1 
ATOM   4122  O OG1 . THR B 1 199 ? 52.484  8.237   50.463  1.00 53.41  ? 195 THR E OG1 1 
ATOM   4123  C CG2 . THR B 1 199 ? 51.377  9.397   48.653  1.00 40.08  ? 195 THR E CG2 1 
ATOM   4124  N N   . THR B 1 200 ? 50.406  6.810   46.560  1.00 44.82  ? 196 THR E N   1 
ATOM   4125  C CA  . THR B 1 200 ? 50.191  6.538   45.148  1.00 45.49  ? 196 THR E CA  1 
ATOM   4126  C C   . THR B 1 200 ? 49.005  7.278   44.537  1.00 39.74  ? 196 THR E C   1 
ATOM   4127  O O   . THR B 1 200 ? 48.202  7.867   45.244  1.00 36.97  ? 196 THR E O   1 
ATOM   4128  C CB  . THR B 1 200 ? 49.995  5.043   44.904  1.00 50.58  ? 196 THR E CB  1 
ATOM   4129  O OG1 . THR B 1 200 ? 49.985  4.834   43.497  1.00 60.64  ? 196 THR E OG1 1 
ATOM   4130  C CG2 . THR B 1 200 ? 48.691  4.571   45.491  1.00 48.54  ? 196 THR E CG2 1 
ATOM   4131  N N   . TYR B 1 201 ? 48.902  7.214   43.212  1.00 42.23  ? 197 TYR E N   1 
ATOM   4132  C CA  . TYR B 1 201 ? 47.875  7.944   42.468  1.00 40.78  ? 197 TYR E CA  1 
ATOM   4133  C C   . TYR B 1 201 ? 47.659  7.372   41.064  1.00 39.23  ? 197 TYR E C   1 
ATOM   4134  O O   . TYR B 1 201 ? 48.469  6.599   40.569  1.00 36.88  ? 197 TYR E O   1 
ATOM   4135  C CB  . TYR B 1 201 ? 48.276  9.417   42.345  1.00 42.08  ? 197 TYR E CB  1 
ATOM   4136  C CG  . TYR B 1 201 ? 49.453  9.649   41.415  1.00 49.02  ? 197 TYR E CG  1 
ATOM   4137  C CD1 . TYR B 1 201 ? 49.253  9.921   40.066  1.00 51.18  ? 197 TYR E CD1 1 
ATOM   4138  C CD2 . TYR B 1 201 ? 50.768  9.590   41.884  1.00 50.32  ? 197 TYR E CD2 1 
ATOM   4139  C CE1 . TYR B 1 201 ? 50.323  10.133  39.209  1.00 51.88  ? 197 TYR E CE1 1 
ATOM   4140  C CE2 . TYR B 1 201 ? 51.846  9.799   41.034  1.00 51.19  ? 197 TYR E CE2 1 
ATOM   4141  C CZ  . TYR B 1 201 ? 51.617  10.070  39.698  1.00 51.26  ? 197 TYR E CZ  1 
ATOM   4142  O OH  . TYR B 1 201 ? 52.679  10.285  38.850  1.00 53.83  ? 197 TYR E OH  1 
ATOM   4143  N N   . ILE B 1 202 ? 46.556  7.763   40.435  1.00 37.96  ? 198 ILE E N   1 
ATOM   4144  C CA  . ILE B 1 202 ? 46.347  7.540   39.009  1.00 33.46  ? 198 ILE E CA  1 
ATOM   4145  C C   . ILE B 1 202 ? 45.778  8.812   38.410  1.00 36.85  ? 198 ILE E C   1 
ATOM   4146  O O   . ILE B 1 202 ? 44.766  9.315   38.888  1.00 34.92  ? 198 ILE E O   1 
ATOM   4147  C CB  . ILE B 1 202 ? 45.320  6.435   38.708  1.00 33.06  ? 198 ILE E CB  1 
ATOM   4148  C CG1 . ILE B 1 202 ? 45.569  5.178   39.534  1.00 31.22  ? 198 ILE E CG1 1 
ATOM   4149  C CG2 . ILE B 1 202 ? 45.368  6.089   37.224  1.00 30.20  ? 198 ILE E CG2 1 
ATOM   4150  C CD1 . ILE B 1 202 ? 44.424  4.196   39.441  1.00 29.05  ? 198 ILE E CD1 1 
ATOM   4151  N N   . SER B 1 203 ? 46.413  9.332   37.365  1.00 43.41  ? 199 SER E N   1 
ATOM   4152  C CA  . SER B 1 203 ? 45.829  10.442  36.621  1.00 43.37  ? 199 SER E CA  1 
ATOM   4153  C C   . SER B 1 203 ? 45.431  9.969   35.229  1.00 43.44  ? 199 SER E C   1 
ATOM   4154  O O   . SER B 1 203 ? 46.127  9.152   34.625  1.00 43.15  ? 199 SER E O   1 
ATOM   4155  C CB  . SER B 1 203 ? 46.782  11.636  36.549  1.00 44.51  ? 199 SER E CB  1 
ATOM   4156  O OG  . SER B 1 203 ? 48.030  11.275  35.997  1.00 51.21  ? 199 SER E OG  1 
ATOM   4157  N N   . ILE B 1 204 ? 44.295  10.472  34.744  1.00 41.66  ? 200 ILE E N   1 
ATOM   4158  C CA  . ILE B 1 204 ? 43.776  10.111  33.430  1.00 40.39  ? 200 ILE E CA  1 
ATOM   4159  C C   . ILE B 1 204 ? 43.444  11.382  32.673  1.00 39.64  ? 200 ILE E C   1 
ATOM   4160  O O   . ILE B 1 204 ? 42.738  12.250  33.190  1.00 39.15  ? 200 ILE E O   1 
ATOM   4161  C CB  . ILE B 1 204 ? 42.505  9.238   33.522  1.00 41.49  ? 200 ILE E CB  1 
ATOM   4162  C CG1 . ILE B 1 204 ? 42.687  8.120   34.548  1.00 40.43  ? 200 ILE E CG1 1 
ATOM   4163  C CG2 . ILE B 1 204 ? 42.164  8.646   32.162  1.00 38.84  ? 200 ILE E CG2 1 
ATOM   4164  C CD1 . ILE B 1 204 ? 42.330  8.533   35.956  1.00 42.54  ? 200 ILE E CD1 1 
ATOM   4165  N N   . GLY B 1 205 ? 43.955  11.479  31.448  1.00 44.87  ? 201 GLY E N   1 
ATOM   4166  C CA  . GLY B 1 205 ? 43.819  12.684  30.639  1.00 45.52  ? 201 GLY E CA  1 
ATOM   4167  C C   . GLY B 1 205 ? 43.211  12.433  29.276  1.00 46.00  ? 201 GLY E C   1 
ATOM   4168  O O   . GLY B 1 205 ? 43.295  11.339  28.724  1.00 44.19  ? 201 GLY E O   1 
ATOM   4169  N N   . THR B 1 206 ? 42.653  13.496  28.718  1.00 47.47  ? 202 THR E N   1 
ATOM   4170  C CA  . THR B 1 206 ? 41.855  13.423  27.489  1.00 49.60  ? 202 THR E CA  1 
ATOM   4171  C C   . THR B 1 206 ? 41.609  14.870  27.026  1.00 55.97  ? 202 THR E C   1 
ATOM   4172  O O   . THR B 1 206 ? 42.017  15.791  27.729  1.00 60.38  ? 202 THR E O   1 
ATOM   4173  C CB  . THR B 1 206 ? 40.540  12.620  27.734  1.00 51.71  ? 202 THR E CB  1 
ATOM   4174  O OG1 . THR B 1 206 ? 40.791  11.216  27.583  1.00 51.54  ? 202 THR E OG1 1 
ATOM   4175  C CG2 . THR B 1 206 ? 39.437  13.024  26.790  1.00 51.28  ? 202 THR E CG2 1 
ATOM   4176  N N   . SER B 1 207 ? 40.976  15.080  25.864  1.00 71.74  ? 203 SER E N   1 
ATOM   4177  C CA  . SER B 1 207 ? 40.618  16.429  25.380  1.00 75.85  ? 203 SER E CA  1 
ATOM   4178  C C   . SER B 1 207 ? 39.472  17.038  26.168  1.00 79.24  ? 203 SER E C   1 
ATOM   4179  O O   . SER B 1 207 ? 38.971  18.082  25.789  1.00 94.43  ? 203 SER E O   1 
ATOM   4180  C CB  . SER B 1 207 ? 40.263  16.434  23.870  1.00 77.40  ? 203 SER E CB  1 
ATOM   4181  O OG  . SER B 1 207 ? 41.307  15.871  23.103  1.00 94.35  ? 203 SER E OG  1 
ATOM   4182  N N   . THR B 1 208 ? 39.087  16.396  27.269  1.00 68.43  ? 204 THR E N   1 
ATOM   4183  C CA  . THR B 1 208 ? 37.887  16.759  28.035  1.00 71.36  ? 204 THR E CA  1 
ATOM   4184  C C   . THR B 1 208 ? 37.955  16.248  29.498  1.00 60.58  ? 204 THR E C   1 
ATOM   4185  O O   . THR B 1 208 ? 37.398  16.875  30.406  1.00 59.28  ? 204 THR E O   1 
ATOM   4186  C CB  . THR B 1 208 ? 36.597  16.230  27.334  1.00 73.80  ? 204 THR E CB  1 
ATOM   4187  O OG1 . THR B 1 208 ? 35.533  16.143  28.284  1.00 79.45  ? 204 THR E OG1 1 
ATOM   4188  C CG2 . THR B 1 208 ? 36.823  14.845  26.739  1.00 76.22  ? 204 THR E CG2 1 
ATOM   4189  N N   . LEU B 1 209 ? 38.635  15.122  29.716  1.00 53.16  ? 205 LEU E N   1 
ATOM   4190  C CA  . LEU B 1 209 ? 38.768  14.517  31.040  1.00 50.09  ? 205 LEU E CA  1 
ATOM   4191  C C   . LEU B 1 209 ? 40.077  14.926  31.704  1.00 52.53  ? 205 LEU E C   1 
ATOM   4192  O O   . LEU B 1 209 ? 41.134  14.931  31.072  1.00 54.35  ? 205 LEU E O   1 
ATOM   4193  C CB  . LEU B 1 209 ? 38.716  12.993  30.931  1.00 51.91  ? 205 LEU E CB  1 
ATOM   4194  C CG  . LEU B 1 209 ? 38.670  12.207  32.242  1.00 51.88  ? 205 LEU E CG  1 
ATOM   4195  C CD1 . LEU B 1 209 ? 37.387  12.490  33.005  1.00 44.61  ? 205 LEU E CD1 1 
ATOM   4196  C CD2 . LEU B 1 209 ? 38.793  10.720  31.951  1.00 55.09  ? 205 LEU E CD2 1 
ATOM   4197  N N   . ASN B 1 210 ? 39.990  15.256  32.989  1.00 52.30  ? 206 ASN E N   1 
ATOM   4198  C CA  . ASN B 1 210 ? 41.145  15.645  33.789  1.00 45.20  ? 206 ASN E CA  1 
ATOM   4199  C C   . ASN B 1 210 ? 40.939  15.164  35.219  1.00 46.26  ? 206 ASN E C   1 
ATOM   4200  O O   . ASN B 1 210 ? 40.435  15.907  36.067  1.00 48.20  ? 206 ASN E O   1 
ATOM   4201  C CB  . ASN B 1 210 ? 41.330  17.166  33.750  1.00 41.27  ? 206 ASN E CB  1 
ATOM   4202  C CG  . ASN B 1 210 ? 42.478  17.647  34.626  1.00 41.32  ? 206 ASN E CG  1 
ATOM   4203  O OD1 . ASN B 1 210 ? 43.445  16.923  34.873  1.00 42.90  ? 206 ASN E OD1 1 
ATOM   4204  N ND2 . ASN B 1 210 ? 42.382  18.888  35.083  1.00 40.99  ? 206 ASN E ND2 1 
ATOM   4205  N N   . GLN B 1 211 ? 41.324  13.922  35.497  1.00 45.45  ? 207 GLN E N   1 
ATOM   4206  C CA  . GLN B 1 211 ? 41.062  13.375  36.824  1.00 45.94  ? 207 GLN E CA  1 
ATOM   4207  C C   . GLN B 1 211 ? 42.289  12.738  37.482  1.00 40.30  ? 207 GLN E C   1 
ATOM   4208  O O   . GLN B 1 211 ? 43.208  12.241  36.818  1.00 38.40  ? 207 GLN E O   1 
ATOM   4209  C CB  . GLN B 1 211 ? 39.831  12.431  36.792  1.00 48.98  ? 207 GLN E CB  1 
ATOM   4210  C CG  . GLN B 1 211 ? 40.108  10.983  36.456  1.00 54.38  ? 207 GLN E CG  1 
ATOM   4211  C CD  . GLN B 1 211 ? 38.889  10.108  36.721  1.00 57.14  ? 207 GLN E CD  1 
ATOM   4212  O OE1 . GLN B 1 211 ? 38.133  9.767   35.807  1.00 61.44  ? 207 GLN E OE1 1 
ATOM   4213  N NE2 . GLN B 1 211 ? 38.676  9.767   37.983  1.00 61.07  ? 207 GLN E NE2 1 
ATOM   4214  N N   . ARG B 1 212 ? 42.299  12.807  38.810  1.00 40.81  ? 208 ARG E N   1 
ATOM   4215  C CA  . ARG B 1 212 ? 43.355  12.223  39.620  1.00 40.46  ? 208 ARG E CA  1 
ATOM   4216  C C   . ARG B 1 212 ? 42.716  11.412  40.740  1.00 40.67  ? 208 ARG E C   1 
ATOM   4217  O O   . ARG B 1 212 ? 41.947  11.942  41.536  1.00 44.05  ? 208 ARG E O   1 
ATOM   4218  C CB  . ARG B 1 212 ? 44.260  13.312  40.193  1.00 42.04  ? 208 ARG E CB  1 
ATOM   4219  C CG  . ARG B 1 212 ? 45.561  12.780  40.771  1.00 46.53  ? 208 ARG E CG  1 
ATOM   4220  C CD  . ARG B 1 212 ? 46.426  13.899  41.330  1.00 49.96  ? 208 ARG E CD  1 
ATOM   4221  N NE  . ARG B 1 212 ? 47.673  13.405  41.914  1.00 57.54  ? 208 ARG E NE  1 
ATOM   4222  C CZ  . ARG B 1 212 ? 48.827  13.250  41.259  1.00 67.00  ? 208 ARG E CZ  1 
ATOM   4223  N NH1 . ARG B 1 212 ? 48.940  13.552  39.965  1.00 67.22  ? 208 ARG E NH1 1 
ATOM   4224  N NH2 . ARG B 1 212 ? 49.888  12.786  41.910  1.00 66.80  ? 208 ARG E NH2 1 
ATOM   4225  N N   . LEU B 1 213 ? 43.038  10.124  40.783  1.00 42.90  ? 209 LEU E N   1 
ATOM   4226  C CA  . LEU B 1 213 ? 42.471  9.200   41.751  1.00 43.69  ? 209 LEU E CA  1 
ATOM   4227  C C   . LEU B 1 213 ? 43.544  8.796   42.749  1.00 48.17  ? 209 LEU E C   1 
ATOM   4228  O O   . LEU B 1 213 ? 44.677  8.512   42.362  1.00 51.11  ? 209 LEU E O   1 
ATOM   4229  C CB  . LEU B 1 213 ? 41.936  7.957   41.039  1.00 41.70  ? 209 LEU E CB  1 
ATOM   4230  C CG  . LEU B 1 213 ? 40.821  8.213   40.027  1.00 41.89  ? 209 LEU E CG  1 
ATOM   4231  C CD1 . LEU B 1 213 ? 40.568  6.975   39.182  1.00 43.72  ? 209 LEU E CD1 1 
ATOM   4232  C CD2 . LEU B 1 213 ? 39.549  8.644   40.736  1.00 40.03  ? 209 LEU E CD2 1 
ATOM   4233  N N   . VAL B 1 214 ? 43.175  8.773   44.028  1.00 45.95  ? 210 VAL E N   1 
ATOM   4234  C CA  . VAL B 1 214 ? 44.072  8.378   45.104  1.00 46.18  ? 210 VAL E CA  1 
ATOM   4235  C C   . VAL B 1 214 ? 43.384  7.262   45.887  1.00 46.59  ? 210 VAL E C   1 
ATOM   4236  O O   . VAL B 1 214 ? 42.202  7.381   46.212  1.00 48.88  ? 210 VAL E O   1 
ATOM   4237  C CB  . VAL B 1 214 ? 44.379  9.559   46.054  1.00 44.43  ? 210 VAL E CB  1 
ATOM   4238  C CG1 . VAL B 1 214 ? 45.159  9.089   47.278  1.00 43.90  ? 210 VAL E CG1 1 
ATOM   4239  C CG2 . VAL B 1 214 ? 45.142  10.651  45.318  1.00 40.95  ? 210 VAL E CG2 1 
ATOM   4240  N N   . PRO B 1 215 ? 44.109  6.173   46.189  1.00 42.21  ? 211 PRO E N   1 
ATOM   4241  C CA  . PRO B 1 215 ? 43.469  5.088   46.946  1.00 45.91  ? 211 PRO E CA  1 
ATOM   4242  C C   . PRO B 1 215 ? 43.095  5.474   48.371  1.00 44.42  ? 211 PRO E C   1 
ATOM   4243  O O   . PRO B 1 215 ? 43.777  6.288   48.996  1.00 44.25  ? 211 PRO E O   1 
ATOM   4244  C CB  . PRO B 1 215 ? 44.521  3.973   46.981  1.00 41.06  ? 211 PRO E CB  1 
ATOM   4245  C CG  . PRO B 1 215 ? 45.646  4.418   46.147  1.00 40.74  ? 211 PRO E CG  1 
ATOM   4246  C CD  . PRO B 1 215 ? 45.483  5.855   45.781  1.00 39.58  ? 211 PRO E CD  1 
ATOM   4247  N N   . LYS B 1 216 ? 42.016  4.875   48.864  1.00 46.99  ? 212 LYS E N   1 
ATOM   4248  C CA  . LYS B 1 216 ? 41.524  5.113   50.209  1.00 48.31  ? 212 LYS E CA  1 
ATOM   4249  C C   . LYS B 1 216 ? 41.707  3.842   51.021  1.00 53.19  ? 212 LYS E C   1 
ATOM   4250  O O   . LYS B 1 216 ? 41.014  2.849   50.794  1.00 53.11  ? 212 LYS E O   1 
ATOM   4251  C CB  . LYS B 1 216 ? 40.049  5.506   50.163  1.00 47.42  ? 212 LYS E CB  1 
ATOM   4252  C CG  . LYS B 1 216 ? 39.799  6.816   49.430  1.00 47.88  ? 212 LYS E CG  1 
ATOM   4253  C CD  . LYS B 1 216 ? 38.358  7.292   49.558  1.00 45.81  ? 212 LYS E CD  1 
ATOM   4254  C CE  . LYS B 1 216 ? 37.425  6.587   48.587  1.00 46.04  ? 212 LYS E CE  1 
ATOM   4255  N NZ  . LYS B 1 216 ? 37.621  7.040   47.185  1.00 50.67  ? 212 LYS E NZ  1 
ATOM   4256  N N   . ILE B 1 217 ? 42.658  3.871   51.950  1.00 63.38  ? 213 ILE E N   1 
ATOM   4257  C CA  . ILE B 1 217 ? 42.909  2.737   52.826  1.00 68.86  ? 213 ILE E CA  1 
ATOM   4258  C C   . ILE B 1 217 ? 41.958  2.832   54.013  1.00 74.47  ? 213 ILE E C   1 
ATOM   4259  O O   . ILE B 1 217 ? 41.976  3.816   54.752  1.00 74.20  ? 213 ILE E O   1 
ATOM   4260  C CB  . ILE B 1 217 ? 44.350  2.733   53.372  1.00 74.11  ? 213 ILE E CB  1 
ATOM   4261  C CG1 . ILE B 1 217 ? 45.370  2.531   52.249  1.00 77.15  ? 213 ILE E CG1 1 
ATOM   4262  C CG2 . ILE B 1 217 ? 44.517  1.653   54.430  1.00 78.55  ? 213 ILE E CG2 1 
ATOM   4263  C CD1 . ILE B 1 217 ? 45.694  3.777   51.451  1.00 91.37  ? 213 ILE E CD1 1 
ATOM   4264  N N   . ALA B 1 218 ? 41.134  1.807   54.192  1.00 86.12  ? 214 ALA E N   1 
ATOM   4265  C CA  . ALA B 1 218 ? 40.169  1.773   55.290  1.00 85.86  ? 214 ALA E CA  1 
ATOM   4266  C C   . ALA B 1 218 ? 39.809  0.342   55.668  1.00 83.07  ? 214 ALA E C   1 
ATOM   4267  O O   . ALA B 1 218 ? 40.039  -0.592  54.894  1.00 79.14  ? 214 ALA E O   1 
ATOM   4268  C CB  . ALA B 1 218 ? 38.912  2.546   54.918  1.00 81.08  ? 214 ALA E CB  1 
ATOM   4269  N N   . THR B 1 219 ? 39.254  0.185   56.869  1.00 81.89  ? 215 THR E N   1 
ATOM   4270  C CA  . THR B 1 219 ? 38.754  -1.104  57.340  1.00 76.87  ? 215 THR E CA  1 
ATOM   4271  C C   . THR B 1 219 ? 37.339  -1.291  56.811  1.00 70.98  ? 215 THR E C   1 
ATOM   4272  O O   . THR B 1 219 ? 36.493  -0.416  56.986  1.00 71.27  ? 215 THR E O   1 
ATOM   4273  C CB  . THR B 1 219 ? 38.717  -1.170  58.878  1.00 72.26  ? 215 THR E CB  1 
ATOM   4274  O OG1 . THR B 1 219 ? 39.985  -0.769  59.408  1.00 76.49  ? 215 THR E OG1 1 
ATOM   4275  C CG2 . THR B 1 219 ? 38.389  -2.579  59.350  1.00 69.83  ? 215 THR E CG2 1 
ATOM   4276  N N   . ARG B 1 220 ? 37.093  -2.425  56.161  1.00 60.82  ? 216 ARG E N   1 
ATOM   4277  C CA  . ARG B 1 220 ? 35.801  -2.698  55.541  1.00 55.78  ? 216 ARG E CA  1 
ATOM   4278  C C   . ARG B 1 220 ? 35.324  -4.111  55.828  1.00 54.36  ? 216 ARG E C   1 
ATOM   4279  O O   . ARG B 1 220 ? 36.125  -5.008  56.084  1.00 53.66  ? 216 ARG E O   1 
ATOM   4280  C CB  . ARG B 1 220 ? 35.894  -2.502  54.033  1.00 58.22  ? 216 ARG E CB  1 
ATOM   4281  C CG  . ARG B 1 220 ? 36.087  -1.056  53.622  1.00 56.90  ? 216 ARG E CG  1 
ATOM   4282  C CD  . ARG B 1 220 ? 36.344  -0.916  52.133  1.00 58.09  ? 216 ARG E CD  1 
ATOM   4283  N NE  . ARG B 1 220 ? 37.337  0.129   51.885  1.00 58.37  ? 216 ARG E NE  1 
ATOM   4284  C CZ  . ARG B 1 220 ? 38.618  -0.077  51.578  1.00 51.28  ? 216 ARG E CZ  1 
ATOM   4285  N NH1 . ARG B 1 220 ? 39.117  -1.304  51.447  1.00 43.35  ? 216 ARG E NH1 1 
ATOM   4286  N NH2 . ARG B 1 220 ? 39.411  0.971   51.390  1.00 57.14  ? 216 ARG E NH2 1 
ATOM   4287  N N   . SER B 1 221 ? 34.008  -4.291  55.786  1.00 55.22  ? 217 SER E N   1 
ATOM   4288  C CA  . SER B 1 221 ? 33.401  -5.606  55.933  1.00 51.34  ? 217 SER E CA  1 
ATOM   4289  C C   . SER B 1 221 ? 33.732  -6.440  54.704  1.00 53.25  ? 217 SER E C   1 
ATOM   4290  O O   . SER B 1 221 ? 33.780  -5.918  53.589  1.00 47.91  ? 217 SER E O   1 
ATOM   4291  C CB  . SER B 1 221 ? 31.885  -5.478  56.083  1.00 55.30  ? 217 SER E CB  1 
ATOM   4292  O OG  . SER B 1 221 ? 31.550  -4.623  57.166  1.00 61.66  ? 217 SER E OG  1 
ATOM   4293  N N   . LYS B 1 222 ? 33.977  -7.731  54.915  1.00 59.32  ? 218 LYS E N   1 
ATOM   4294  C CA  . LYS B 1 222 ? 34.296  -8.635  53.815  1.00 59.34  ? 218 LYS E CA  1 
ATOM   4295  C C   . LYS B 1 222 ? 33.071  -8.881  52.944  1.00 61.81  ? 218 LYS E C   1 
ATOM   4296  O O   . LYS B 1 222 ? 31.947  -8.929  53.437  1.00 65.57  ? 218 LYS E O   1 
ATOM   4297  C CB  . LYS B 1 222 ? 34.856  -9.963  54.334  1.00 64.02  ? 218 LYS E CB  1 
ATOM   4298  C CG  . LYS B 1 222 ? 36.369  -9.973  54.465  1.00 69.60  ? 218 LYS E CG  1 
ATOM   4299  C CD  . LYS B 1 222 ? 36.888  -11.247 55.113  1.00 74.38  ? 218 LYS E CD  1 
ATOM   4300  C CE  . LYS B 1 222 ? 38.408  -11.340 54.978  1.00 77.06  ? 218 LYS E CE  1 
ATOM   4301  N NZ  . LYS B 1 222 ? 38.985  -12.425 55.819  1.00 82.31  ? 218 LYS E NZ  1 
ATOM   4302  N N   . ILE B 1 223 ? 33.300  -9.008  51.642  1.00 65.41  ? 219 ILE E N   1 
ATOM   4303  C CA  . ILE B 1 223 ? 32.250  -9.370  50.693  1.00 67.24  ? 219 ILE E CA  1 
ATOM   4304  C C   . ILE B 1 223 ? 32.905  -10.176 49.576  1.00 64.38  ? 219 ILE E C   1 
ATOM   4305  O O   . ILE B 1 223 ? 33.841  -9.701  48.930  1.00 61.43  ? 219 ILE E O   1 
ATOM   4306  C CB  . ILE B 1 223 ? 31.502  -8.125  50.158  1.00 71.97  ? 219 ILE E CB  1 
ATOM   4307  C CG1 . ILE B 1 223 ? 30.713  -8.459  48.886  1.00 73.76  ? 219 ILE E CG1 1 
ATOM   4308  C CG2 . ILE B 1 223 ? 32.471  -6.984  49.894  1.00 74.54  ? 219 ILE E CG2 1 
ATOM   4309  C CD1 . ILE B 1 223 ? 29.730  -7.386  48.477  1.00 82.11  ? 219 ILE E CD1 1 
ATOM   4310  N N   . ASN B 1 224 ? 32.413  -11.399 49.372  1.00 61.06  ? 220 ASN E N   1 
ATOM   4311  C CA  . ASN B 1 224 ? 33.105  -12.422 48.578  1.00 58.38  ? 220 ASN E CA  1 
ATOM   4312  C C   . ASN B 1 224 ? 34.507  -12.696 49.138  1.00 55.83  ? 220 ASN E C   1 
ATOM   4313  O O   . ASN B 1 224 ? 35.452  -12.978 48.389  1.00 56.35  ? 220 ASN E O   1 
ATOM   4314  C CB  . ASN B 1 224 ? 33.184  -12.042 47.087  1.00 59.83  ? 220 ASN E CB  1 
ATOM   4315  C CG  . ASN B 1 224 ? 31.834  -12.011 46.396  1.00 63.51  ? 220 ASN E CG  1 
ATOM   4316  O OD1 . ASN B 1 224 ? 30.847  -12.534 46.900  1.00 60.46  ? 220 ASN E OD1 1 
ATOM   4317  N ND2 . ASN B 1 224 ? 31.798  -11.409 45.211  1.00 62.14  ? 220 ASN E ND2 1 
ATOM   4318  N N   . GLY B 1 225 ? 34.630  -12.612 50.463  1.00 55.12  ? 221 GLY E N   1 
ATOM   4319  C CA  . GLY B 1 225 ? 35.899  -12.844 51.155  1.00 56.56  ? 221 GLY E CA  1 
ATOM   4320  C C   . GLY B 1 225 ? 36.949  -11.758 50.982  1.00 57.49  ? 221 GLY E C   1 
ATOM   4321  O O   . GLY B 1 225 ? 38.123  -11.987 51.269  1.00 67.26  ? 221 GLY E O   1 
ATOM   4322  N N   . GLN B 1 226 ? 36.535  -10.578 50.520  1.00 55.14  ? 222 GLN E N   1 
ATOM   4323  C CA  . GLN B 1 226 ? 37.460  -9.476  50.257  1.00 49.46  ? 222 GLN E CA  1 
ATOM   4324  C C   . GLN B 1 226 ? 37.019  -8.205  50.967  1.00 47.53  ? 222 GLN E C   1 
ATOM   4325  O O   . GLN B 1 226 ? 35.865  -7.787  50.846  1.00 57.07  ? 222 GLN E O   1 
ATOM   4326  C CB  . GLN B 1 226 ? 37.555  -9.201  48.754  1.00 50.72  ? 222 GLN E CB  1 
ATOM   4327  C CG  . GLN B 1 226 ? 37.969  -10.398 47.913  1.00 57.46  ? 222 GLN E CG  1 
ATOM   4328  C CD  . GLN B 1 226 ? 39.351  -10.920 48.263  1.00 59.74  ? 222 GLN E CD  1 
ATOM   4329  O OE1 . GLN B 1 226 ? 40.267  -10.149 48.535  1.00 65.28  ? 222 GLN E OE1 1 
ATOM   4330  N NE2 . GLN B 1 226 ? 39.506  -12.239 48.252  1.00 60.77  ? 222 GLN E NE2 1 
ATOM   4331  N N   . SER B 1 227 ? 37.943  -7.597  51.706  1.00 46.08  ? 223 SER E N   1 
ATOM   4332  C CA  . SER B 1 227 ? 37.721  -6.283  52.304  1.00 49.49  ? 223 SER E CA  1 
ATOM   4333  C C   . SER B 1 227 ? 38.253  -5.173  51.403  1.00 48.35  ? 223 SER E C   1 
ATOM   4334  O O   . SER B 1 227 ? 37.921  -4.004  51.597  1.00 57.75  ? 223 SER E O   1 
ATOM   4335  C CB  . SER B 1 227 ? 38.358  -6.195  53.690  1.00 53.39  ? 223 SER E CB  1 
ATOM   4336  O OG  . SER B 1 227 ? 37.496  -6.748  54.668  1.00 61.49  ? 223 SER E OG  1 
ATOM   4337  N N   . GLY B 1 228 ? 39.083  -5.537  50.428  1.00 42.32  ? 224 GLY E N   1 
ATOM   4338  C CA  . GLY B 1 228 ? 39.528  -4.595  49.411  1.00 43.65  ? 224 GLY E CA  1 
ATOM   4339  C C   . GLY B 1 228 ? 38.392  -4.253  48.471  1.00 42.63  ? 224 GLY E C   1 
ATOM   4340  O O   . GLY B 1 228 ? 37.401  -4.973  48.408  1.00 48.98  ? 224 GLY E O   1 
ATOM   4341  N N   . ARG B 1 229 ? 38.534  -3.145  47.751  1.00 41.77  ? 225 ARG E N   1 
ATOM   4342  C CA  . ARG B 1 229 ? 37.531  -2.709  46.786  1.00 38.78  ? 225 ARG E CA  1 
ATOM   4343  C C   . ARG B 1 229 ? 38.207  -2.239  45.516  1.00 39.05  ? 225 ARG E C   1 
ATOM   4344  O O   . ARG B 1 229 ? 39.363  -1.821  45.543  1.00 46.26  ? 225 ARG E O   1 
ATOM   4345  C CB  . ARG B 1 229 ? 36.711  -1.557  47.356  1.00 41.71  ? 225 ARG E CB  1 
ATOM   4346  C CG  . ARG B 1 229 ? 35.905  -1.900  48.597  1.00 43.98  ? 225 ARG E CG  1 
ATOM   4347  C CD  . ARG B 1 229 ? 34.675  -2.724  48.265  1.00 49.27  ? 225 ARG E CD  1 
ATOM   4348  N NE  . ARG B 1 229 ? 33.877  -2.992  49.460  1.00 51.26  ? 225 ARG E NE  1 
ATOM   4349  C CZ  . ARG B 1 229 ? 34.095  -3.984  50.321  1.00 52.77  ? 225 ARG E CZ  1 
ATOM   4350  N NH1 . ARG B 1 229 ? 35.096  -4.844  50.143  1.00 55.70  ? 225 ARG E NH1 1 
ATOM   4351  N NH2 . ARG B 1 229 ? 33.304  -4.117  51.377  1.00 54.83  ? 225 ARG E NH2 1 
ATOM   4352  N N   . ILE B 1 230 ? 37.491  -2.320  44.402  1.00 39.20  ? 226 ILE E N   1 
ATOM   4353  C CA  . ILE B 1 230 ? 37.962  -1.743  43.148  1.00 40.98  ? 226 ILE E CA  1 
ATOM   4354  C C   . ILE B 1 230 ? 36.856  -0.900  42.530  1.00 41.97  ? 226 ILE E C   1 
ATOM   4355  O O   . ILE B 1 230 ? 35.771  -1.403  42.260  1.00 46.26  ? 226 ILE E O   1 
ATOM   4356  C CB  . ILE B 1 230 ? 38.411  -2.819  42.147  1.00 41.33  ? 226 ILE E CB  1 
ATOM   4357  C CG1 . ILE B 1 230 ? 39.645  -3.552  42.676  1.00 44.14  ? 226 ILE E CG1 1 
ATOM   4358  C CG2 . ILE B 1 230 ? 38.734  -2.184  40.801  1.00 35.56  ? 226 ILE E CG2 1 
ATOM   4359  C CD1 . ILE B 1 230 ? 40.035  -4.758  41.851  1.00 46.16  ? 226 ILE E CD1 1 
ATOM   4360  N N   . ASP B 1 231 ? 37.135  0.386   42.338  1.00 39.92  ? 227 ASP E N   1 
ATOM   4361  C CA  . ASP B 1 231 ? 36.187  1.305   41.721  1.00 40.86  ? 227 ASP E CA  1 
ATOM   4362  C C   . ASP B 1 231 ? 36.545  1.468   40.258  1.00 38.68  ? 227 ASP E C   1 
ATOM   4363  O O   . ASP B 1 231 ? 37.719  1.626   39.918  1.00 42.41  ? 227 ASP E O   1 
ATOM   4364  C CB  . ASP B 1 231 ? 36.215  2.674   42.412  1.00 44.24  ? 227 ASP E CB  1 
ATOM   4365  C CG  . ASP B 1 231 ? 35.675  2.631   43.831  1.00 45.77  ? 227 ASP E CG  1 
ATOM   4366  O OD1 . ASP B 1 231 ? 35.139  1.584   44.248  1.00 49.86  ? 227 ASP E OD1 1 
ATOM   4367  O OD2 . ASP B 1 231 ? 35.790  3.655   44.536  1.00 52.81  ? 227 ASP E OD2 1 
ATOM   4368  N N   . PHE B 1 232 ? 35.534  1.432   39.395  1.00 37.88  ? 228 PHE E N   1 
ATOM   4369  C CA  . PHE B 1 232 ? 35.743  1.534   37.958  1.00 35.99  ? 228 PHE E CA  1 
ATOM   4370  C C   . PHE B 1 232 ? 35.201  2.843   37.418  1.00 36.54  ? 228 PHE E C   1 
ATOM   4371  O O   . PHE B 1 232 ? 34.205  3.372   37.914  1.00 35.45  ? 228 PHE E O   1 
ATOM   4372  C CB  . PHE B 1 232 ? 35.077  0.367   37.238  1.00 37.13  ? 228 PHE E CB  1 
ATOM   4373  C CG  . PHE B 1 232 ? 35.798  -0.937  37.409  1.00 35.43  ? 228 PHE E CG  1 
ATOM   4374  C CD1 . PHE B 1 232 ? 35.353  -1.880  38.324  1.00 36.74  ? 228 PHE E CD1 1 
ATOM   4375  C CD2 . PHE B 1 232 ? 36.918  -1.221  36.651  1.00 35.13  ? 228 PHE E CD2 1 
ATOM   4376  C CE1 . PHE B 1 232 ? 36.022  -3.081  38.480  1.00 38.41  ? 228 PHE E CE1 1 
ATOM   4377  C CE2 . PHE B 1 232 ? 37.590  -2.421  36.796  1.00 36.22  ? 228 PHE E CE2 1 
ATOM   4378  C CZ  . PHE B 1 232 ? 37.141  -3.352  37.712  1.00 38.18  ? 228 PHE E CZ  1 
ATOM   4379  N N   . PHE B 1 233 ? 35.870  3.348   36.388  1.00 35.83  ? 229 PHE E N   1 
ATOM   4380  C CA  . PHE B 1 233 ? 35.498  4.591   35.739  1.00 35.60  ? 229 PHE E CA  1 
ATOM   4381  C C   . PHE B 1 233 ? 35.495  4.379   34.234  1.00 35.79  ? 229 PHE E C   1 
ATOM   4382  O O   . PHE B 1 233 ? 35.992  3.367   33.747  1.00 33.98  ? 229 PHE E O   1 
ATOM   4383  C CB  . PHE B 1 233 ? 36.486  5.687   36.127  1.00 37.45  ? 229 PHE E CB  1 
ATOM   4384  C CG  . PHE B 1 233 ? 36.459  6.020   37.589  1.00 39.85  ? 229 PHE E CG  1 
ATOM   4385  C CD1 . PHE B 1 233 ? 37.116  5.215   38.507  1.00 41.82  ? 229 PHE E CD1 1 
ATOM   4386  C CD2 . PHE B 1 233 ? 35.758  7.124   38.053  1.00 43.97  ? 229 PHE E CD2 1 
ATOM   4387  C CE1 . PHE B 1 233 ? 37.082  5.508   39.860  1.00 43.60  ? 229 PHE E CE1 1 
ATOM   4388  C CE2 . PHE B 1 233 ? 35.720  7.425   39.407  1.00 42.57  ? 229 PHE E CE2 1 
ATOM   4389  C CZ  . PHE B 1 233 ? 36.385  6.616   40.311  1.00 42.44  ? 229 PHE E CZ  1 
ATOM   4390  N N   . TRP B 1 234 ? 34.929  5.331   33.500  1.00 38.31  ? 230 TRP E N   1 
ATOM   4391  C CA  . TRP B 1 234 ? 34.868  5.226   32.051  1.00 40.18  ? 230 TRP E CA  1 
ATOM   4392  C C   . TRP B 1 234 ? 34.811  6.558   31.377  1.00 40.71  ? 230 TRP E C   1 
ATOM   4393  O O   . TRP B 1 234 ? 34.507  7.581   31.994  1.00 41.61  ? 230 TRP E O   1 
ATOM   4394  C CB  . TRP B 1 234 ? 33.651  4.397   31.639  1.00 43.29  ? 230 TRP E CB  1 
ATOM   4395  C CG  . TRP B 1 234 ? 32.333  4.988   32.081  1.00 43.39  ? 230 TRP E CG  1 
ATOM   4396  C CD1 . TRP B 1 234 ? 31.733  4.877   33.332  1.00 44.38  ? 230 TRP E CD1 1 
ATOM   4397  C CD2 . TRP B 1 234 ? 31.406  5.806   31.288  1.00 44.59  ? 230 TRP E CD2 1 
ATOM   4398  N NE1 . TRP B 1 234 ? 30.541  5.549   33.368  1.00 44.91  ? 230 TRP E NE1 1 
ATOM   4399  C CE2 . TRP B 1 234 ? 30.283  6.127   32.176  1.00 46.34  ? 230 TRP E CE2 1 
ATOM   4400  C CE3 . TRP B 1 234 ? 31.395  6.290   29.987  1.00 42.50  ? 230 TRP E CE3 1 
ATOM   4401  C CZ2 . TRP B 1 234 ? 29.210  6.893   31.756  1.00 46.85  ? 230 TRP E CZ2 1 
ATOM   4402  C CZ3 . TRP B 1 234 ? 30.302  7.062   29.574  1.00 46.43  ? 230 TRP E CZ3 1 
ATOM   4403  C CH2 . TRP B 1 234 ? 29.241  7.359   30.442  1.00 48.03  ? 230 TRP E CH2 1 
ATOM   4404  N N   . THR B 1 235 ? 35.117  6.550   30.088  1.00 42.82  ? 231 THR E N   1 
ATOM   4405  C CA  . THR B 1 235 ? 34.907  7.711   29.242  1.00 43.98  ? 231 THR E CA  1 
ATOM   4406  C C   . THR B 1 235 ? 34.770  7.272   27.786  1.00 42.86  ? 231 THR E C   1 
ATOM   4407  O O   . THR B 1 235 ? 35.122  6.146   27.433  1.00 44.51  ? 231 THR E O   1 
ATOM   4408  C CB  . THR B 1 235 ? 36.078  8.699   29.380  1.00 43.55  ? 231 THR E CB  1 
ATOM   4409  O OG1 . THR B 1 235 ? 35.730  9.952   28.785  1.00 44.31  ? 231 THR E OG1 1 
ATOM   4410  C CG2 . THR B 1 235 ? 37.346  8.138   28.721  1.00 43.27  ? 231 THR E CG2 1 
ATOM   4411  N N   . ILE B 1 236 ? 34.234  8.162   26.959  1.00 43.42  ? 232 ILE E N   1 
ATOM   4412  C CA  . ILE B 1 236 ? 34.149  7.937   25.524  1.00 45.41  ? 232 ILE E CA  1 
ATOM   4413  C C   . ILE B 1 236 ? 35.266  8.735   24.871  1.00 45.88  ? 232 ILE E C   1 
ATOM   4414  O O   . ILE B 1 236 ? 35.280  9.963   24.944  1.00 47.83  ? 232 ILE E O   1 
ATOM   4415  C CB  . ILE B 1 236 ? 32.768  8.347   24.953  1.00 44.55  ? 232 ILE E CB  1 
ATOM   4416  C CG1 . ILE B 1 236 ? 31.793  7.175   25.027  1.00 40.91  ? 232 ILE E CG1 1 
ATOM   4417  C CG2 . ILE B 1 236 ? 32.874  8.765   23.492  1.00 44.75  ? 232 ILE E CG2 1 
ATOM   4418  C CD1 . ILE B 1 236 ? 31.663  6.566   26.399  1.00 41.17  ? 232 ILE E CD1 1 
ATOM   4419  N N   . LEU B 1 237 ? 36.214  8.029   24.261  1.00 49.85  ? 233 LEU E N   1 
ATOM   4420  C CA  . LEU B 1 237 ? 37.335  8.666   23.581  1.00 53.53  ? 233 LEU E CA  1 
ATOM   4421  C C   . LEU B 1 237 ? 36.915  8.997   22.152  1.00 55.75  ? 233 LEU E C   1 
ATOM   4422  O O   . LEU B 1 237 ? 36.504  8.112   21.394  1.00 56.79  ? 233 LEU E O   1 
ATOM   4423  C CB  . LEU B 1 237 ? 38.557  7.742   23.597  1.00 53.38  ? 233 LEU E CB  1 
ATOM   4424  C CG  . LEU B 1 237 ? 39.929  8.328   23.237  1.00 55.88  ? 233 LEU E CG  1 
ATOM   4425  C CD1 . LEU B 1 237 ? 40.211  9.631   23.970  1.00 52.76  ? 233 LEU E CD1 1 
ATOM   4426  C CD2 . LEU B 1 237 ? 41.023  7.307   23.529  1.00 50.40  ? 233 LEU E CD2 1 
ATOM   4427  N N   . LYS B 1 238 ? 37.005  10.278  21.799  1.00 58.86  ? 234 LYS E N   1 
ATOM   4428  C CA  . LYS B 1 238 ? 36.623  10.756  20.468  1.00 67.83  ? 234 LYS E CA  1 
ATOM   4429  C C   . LYS B 1 238 ? 37.542  10.202  19.375  1.00 76.04  ? 234 LYS E C   1 
ATOM   4430  O O   . LYS B 1 238 ? 38.652  9.760   19.668  1.00 75.53  ? 234 LYS E O   1 
ATOM   4431  C CB  . LYS B 1 238 ? 36.642  12.293  20.429  1.00 70.24  ? 234 LYS E CB  1 
ATOM   4432  C CG  . LYS B 1 238 ? 35.560  12.965  21.262  1.00 68.02  ? 234 LYS E CG  1 
ATOM   4433  C CD  . LYS B 1 238 ? 34.160  12.649  20.750  1.00 73.30  ? 234 LYS E CD  1 
ATOM   4434  C CE  . LYS B 1 238 ? 33.078  13.178  21.680  1.00 75.72  ? 234 LYS E CE  1 
ATOM   4435  N NZ  . LYS B 1 238 ? 32.852  14.640  21.516  1.00 72.00  ? 234 LYS E NZ  1 
ATOM   4436  N N   . PRO B 1 239 ? 37.082  10.227  18.108  1.00 90.65  ? 235 PRO E N   1 
ATOM   4437  C CA  . PRO B 1 239 ? 37.856  9.658   17.003  1.00 88.72  ? 235 PRO E CA  1 
ATOM   4438  C C   . PRO B 1 239 ? 39.333  10.059  16.960  1.00 82.02  ? 235 PRO E C   1 
ATOM   4439  O O   . PRO B 1 239 ? 40.191  9.185   16.999  1.00 85.37  ? 235 PRO E O   1 
ATOM   4440  C CB  . PRO B 1 239 ? 37.112  10.167  15.767  1.00 96.75  ? 235 PRO E CB  1 
ATOM   4441  C CG  . PRO B 1 239 ? 35.697  10.248  16.218  1.00 96.56  ? 235 PRO E CG  1 
ATOM   4442  C CD  . PRO B 1 239 ? 35.772  10.724  17.641  1.00 91.82  ? 235 PRO E CD  1 
ATOM   4443  N N   . ASN B 1 240 ? 39.633  11.355  16.907  1.00 73.64  ? 236 ASN E N   1 
ATOM   4444  C CA  . ASN B 1 240 ? 41.023  11.794  16.729  1.00 78.83  ? 236 ASN E CA  1 
ATOM   4445  C C   . ASN B 1 240 ? 41.746  12.113  18.044  1.00 80.90  ? 236 ASN E C   1 
ATOM   4446  O O   . ASN B 1 240 ? 42.820  12.721  18.040  1.00 80.51  ? 236 ASN E O   1 
ATOM   4447  C CB  . ASN B 1 240 ? 41.071  13.007  15.792  1.00 87.16  ? 236 ASN E CB  1 
ATOM   4448  C CG  . ASN B 1 240 ? 42.403  13.139  15.073  1.00 95.24  ? 236 ASN E CG  1 
ATOM   4449  O OD1 . ASN B 1 240 ? 42.927  12.165  14.528  1.00 105.36 ? 236 ASN E OD1 1 
ATOM   4450  N ND2 . ASN B 1 240 ? 42.957  14.348  15.066  1.00 96.17  ? 236 ASN E ND2 1 
ATOM   4451  N N   . ASP B 1 241 ? 41.173  11.672  19.161  1.00 80.83  ? 237 ASP E N   1 
ATOM   4452  C CA  . ASP B 1 241 ? 41.656  12.041  20.488  1.00 71.72  ? 237 ASP E CA  1 
ATOM   4453  C C   . ASP B 1 241 ? 42.478  10.909  21.107  1.00 65.56  ? 237 ASP E C   1 
ATOM   4454  O O   . ASP B 1 241 ? 42.433  9.769   20.639  1.00 63.29  ? 237 ASP E O   1 
ATOM   4455  C CB  . ASP B 1 241 ? 40.459  12.382  21.382  1.00 74.54  ? 237 ASP E CB  1 
ATOM   4456  C CG  . ASP B 1 241 ? 40.856  13.093  22.665  1.00 70.67  ? 237 ASP E CG  1 
ATOM   4457  O OD1 . ASP B 1 241 ? 41.981  13.627  22.746  1.00 76.99  ? 237 ASP E OD1 1 
ATOM   4458  O OD2 . ASP B 1 241 ? 40.036  13.126  23.600  1.00 66.69  ? 237 ASP E OD2 1 
ATOM   4459  N N   . ALA B 1 242 ? 43.236  11.238  22.152  1.00 59.40  ? 238 ALA E N   1 
ATOM   4460  C CA  . ALA B 1 242 ? 44.030  10.253  22.883  1.00 59.96  ? 238 ALA E CA  1 
ATOM   4461  C C   . ALA B 1 242 ? 43.771  10.328  24.387  1.00 55.41  ? 238 ALA E C   1 
ATOM   4462  O O   . ALA B 1 242 ? 43.394  11.373  24.915  1.00 56.39  ? 238 ALA E O   1 
ATOM   4463  C CB  . ALA B 1 242 ? 45.511  10.444  22.591  1.00 60.02  ? 238 ALA E CB  1 
ATOM   4464  N N   . ILE B 1 243 ? 43.991  9.205   25.062  1.00 54.60  ? 239 ILE E N   1 
ATOM   4465  C CA  . ILE B 1 243 ? 43.844  9.100   26.509  1.00 47.74  ? 239 ILE E CA  1 
ATOM   4466  C C   . ILE B 1 243 ? 45.222  8.836   27.127  1.00 49.77  ? 239 ILE E C   1 
ATOM   4467  O O   . ILE B 1 243 ? 45.999  8.059   26.582  1.00 49.18  ? 239 ILE E O   1 
ATOM   4468  C CB  . ILE B 1 243 ? 42.845  7.979   26.872  1.00 43.71  ? 239 ILE E CB  1 
ATOM   4469  C CG1 . ILE B 1 243 ? 42.547  7.977   28.371  1.00 46.35  ? 239 ILE E CG1 1 
ATOM   4470  C CG2 . ILE B 1 243 ? 43.371  6.616   26.442  1.00 43.85  ? 239 ILE E CG2 1 
ATOM   4471  C CD1 . ILE B 1 243 ? 41.334  7.152   28.750  1.00 42.99  ? 239 ILE E CD1 1 
ATOM   4472  N N   . HIS B 1 244 ? 45.525  9.482   28.254  1.00 54.98  ? 240 HIS E N   1 
ATOM   4473  C CA  . HIS B 1 244 ? 46.850  9.362   28.893  1.00 53.82  ? 240 HIS E CA  1 
ATOM   4474  C C   . HIS B 1 244 ? 46.750  8.922   30.319  1.00 50.98  ? 240 HIS E C   1 
ATOM   4475  O O   . HIS B 1 244 ? 46.182  9.626   31.153  1.00 52.97  ? 240 HIS E O   1 
ATOM   4476  C CB  . HIS B 1 244 ? 47.604  10.680  28.845  1.00 57.19  ? 240 HIS E CB  1 
ATOM   4477  C CG  . HIS B 1 244 ? 47.833  11.198  27.451  1.00 71.28  ? 240 HIS E CG  1 
ATOM   4478  N ND1 . HIS B 1 244 ? 48.913  10.854  26.717  1.00 75.53  ? 240 HIS E ND1 1 
ATOM   4479  C CD2 . HIS B 1 244 ? 47.080  12.067  26.666  1.00 76.66  ? 240 HIS E CD2 1 
ATOM   4480  C CE1 . HIS B 1 244 ? 48.855  11.472  25.522  1.00 79.25  ? 240 HIS E CE1 1 
ATOM   4481  N NE2 . HIS B 1 244 ? 47.732  12.215  25.490  1.00 75.96  ? 240 HIS E NE2 1 
ATOM   4482  N N   . PHE B 1 245 ? 47.299  7.747   30.612  1.00 51.23  ? 241 PHE E N   1 
ATOM   4483  C CA  . PHE B 1 245 ? 47.346  7.237   31.973  1.00 54.46  ? 241 PHE E CA  1 
ATOM   4484  C C   . PHE B 1 245 ? 48.706  7.511   32.592  1.00 54.31  ? 241 PHE E C   1 
ATOM   4485  O O   . PHE B 1 245 ? 49.740  7.422   31.921  1.00 56.49  ? 241 PHE E O   1 
ATOM   4486  C CB  . PHE B 1 245 ? 47.089  5.731   32.001  1.00 58.01  ? 241 PHE E CB  1 
ATOM   4487  C CG  . PHE B 1 245 ? 45.723  5.342   31.527  1.00 62.31  ? 241 PHE E CG  1 
ATOM   4488  C CD1 . PHE B 1 245 ? 45.511  4.982   30.205  1.00 59.24  ? 241 PHE E CD1 1 
ATOM   4489  C CD2 . PHE B 1 245 ? 44.647  5.338   32.403  1.00 61.42  ? 241 PHE E CD2 1 
ATOM   4490  C CE1 . PHE B 1 245 ? 44.251  4.620   29.766  1.00 61.35  ? 241 PHE E CE1 1 
ATOM   4491  C CE2 . PHE B 1 245 ? 43.383  4.976   31.968  1.00 60.37  ? 241 PHE E CE2 1 
ATOM   4492  C CZ  . PHE B 1 245 ? 43.185  4.618   30.648  1.00 61.43  ? 241 PHE E CZ  1 
ATOM   4493  N N   . GLU B 1 246 ? 48.694  7.845   33.877  1.00 54.15  ? 242 GLU E N   1 
ATOM   4494  C CA  . GLU B 1 246 ? 49.916  7.961   34.653  1.00 57.73  ? 242 GLU E CA  1 
ATOM   4495  C C   . GLU B 1 246 ? 49.622  7.439   36.050  1.00 54.87  ? 242 GLU E C   1 
ATOM   4496  O O   . GLU B 1 246 ? 48.761  7.977   36.745  1.00 62.56  ? 242 GLU E O   1 
ATOM   4497  C CB  . GLU B 1 246 ? 50.396  9.412   34.688  1.00 61.36  ? 242 GLU E CB  1 
ATOM   4498  C CG  . GLU B 1 246 ? 51.772  9.598   35.312  1.00 72.54  ? 242 GLU E CG  1 
ATOM   4499  C CD  . GLU B 1 246 ? 52.343  10.996  35.111  1.00 84.48  ? 242 GLU E CD  1 
ATOM   4500  O OE1 . GLU B 1 246 ? 53.263  11.368  35.869  1.00 89.77  ? 242 GLU E OE1 1 
ATOM   4501  O OE2 . GLU B 1 246 ? 51.879  11.727  34.208  1.00 87.85  ? 242 GLU E OE2 1 
ATOM   4502  N N   . SER B 1 247 ? 50.309  6.372   36.446  1.00 47.05  ? 243 SER E N   1 
ATOM   4503  C CA  . SER B 1 247 ? 50.074  5.764   37.748  1.00 46.42  ? 243 SER E CA  1 
ATOM   4504  C C   . SER B 1 247 ? 51.328  5.219   38.388  1.00 48.79  ? 243 SER E C   1 
ATOM   4505  O O   . SER B 1 247 ? 52.263  4.783   37.721  1.00 51.88  ? 243 SER E O   1 
ATOM   4506  C CB  . SER B 1 247 ? 49.071  4.622   37.656  1.00 46.29  ? 243 SER E CB  1 
ATOM   4507  O OG  . SER B 1 247 ? 48.869  4.051   38.940  1.00 47.13  ? 243 SER E OG  1 
ATOM   4508  N N   . ASN B 1 248 ? 51.278  5.193   39.710  1.00 52.35  ? 244 ASN E N   1 
ATOM   4509  C CA  . ASN B 1 248 ? 52.422  4.920   40.558  1.00 56.44  ? 244 ASN E CA  1 
ATOM   4510  C C   . ASN B 1 248 ? 52.192  3.715   41.489  1.00 57.84  ? 244 ASN E C   1 
ATOM   4511  O O   . ASN B 1 248 ? 53.150  3.087   41.938  1.00 60.04  ? 244 ASN E O   1 
ATOM   4512  C CB  . ASN B 1 248 ? 52.729  6.194   41.355  1.00 63.66  ? 244 ASN E CB  1 
ATOM   4513  C CG  . ASN B 1 248 ? 53.865  6.019   42.323  1.00 69.71  ? 244 ASN E CG  1 
ATOM   4514  O OD1 . ASN B 1 248 ? 53.687  6.181   43.526  1.00 67.93  ? 244 ASN E OD1 1 
ATOM   4515  N ND2 . ASN B 1 248 ? 55.041  5.677   41.808  1.00 88.16  ? 244 ASN E ND2 1 
ATOM   4516  N N   . GLY B 1 249 ? 50.924  3.408   41.787  1.00 68.16  ? 245 GLY E N   1 
ATOM   4517  C CA  . GLY B 1 249 ? 50.559  2.257   42.623  1.00 75.03  ? 245 GLY E CA  1 
ATOM   4518  C C   . GLY B 1 249 ? 49.409  1.413   42.124  1.00 69.58  ? 245 GLY E C   1 
ATOM   4519  O O   . GLY B 1 249 ? 49.642  0.367   41.535  1.00 89.77  ? 245 GLY E O   1 
ATOM   4520  N N   . ASN B 1 250 ? 48.177  1.871   42.342  1.00 61.18  ? 246 ASN E N   1 
ATOM   4521  C CA  . ASN B 1 250 ? 46.990  0.994   42.364  1.00 56.15  ? 246 ASN E CA  1 
ATOM   4522  C C   . ASN B 1 250 ? 46.179  1.163   41.091  1.00 58.70  ? 246 ASN E C   1 
ATOM   4523  O O   . ASN B 1 250 ? 45.210  1.901   41.088  1.00 68.26  ? 246 ASN E O   1 
ATOM   4524  C CB  . ASN B 1 250 ? 46.085  1.341   43.559  1.00 46.64  ? 246 ASN E CB  1 
ATOM   4525  C CG  . ASN B 1 250 ? 46.798  1.261   44.881  1.00 42.45  ? 246 ASN E CG  1 
ATOM   4526  O OD1 . ASN B 1 250 ? 47.874  1.815   45.042  1.00 42.04  ? 246 ASN E OD1 1 
ATOM   4527  N ND2 . ASN B 1 250 ? 46.174  0.615   45.857  1.00 44.19  ? 246 ASN E ND2 1 
ATOM   4528  N N   . PHE B 1 251 ? 46.546  0.504   40.001  1.00 50.90  ? 247 PHE E N   1 
ATOM   4529  C CA  . PHE B 1 251 ? 45.905  0.825   38.736  1.00 46.86  ? 247 PHE E CA  1 
ATOM   4530  C C   . PHE B 1 251 ? 45.463  -0.441  38.018  1.00 48.84  ? 247 PHE E C   1 
ATOM   4531  O O   . PHE B 1 251 ? 46.265  -1.338  37.769  1.00 47.87  ? 247 PHE E O   1 
ATOM   4532  C CB  . PHE B 1 251 ? 46.834  1.735   37.920  1.00 44.92  ? 247 PHE E CB  1 
ATOM   4533  C CG  . PHE B 1 251 ? 46.444  1.910   36.479  1.00 45.36  ? 247 PHE E CG  1 
ATOM   4534  C CD1 . PHE B 1 251 ? 45.152  2.277   36.141  1.00 49.26  ? 247 PHE E CD1 1 
ATOM   4535  C CD2 . PHE B 1 251 ? 47.389  1.789   35.465  1.00 42.95  ? 247 PHE E CD2 1 
ATOM   4536  C CE1 . PHE B 1 251 ? 44.793  2.477   34.822  1.00 46.35  ? 247 PHE E CE1 1 
ATOM   4537  C CE2 . PHE B 1 251 ? 47.035  1.987   34.140  1.00 47.35  ? 247 PHE E CE2 1 
ATOM   4538  C CZ  . PHE B 1 251 ? 45.733  2.334   33.818  1.00 48.89  ? 247 PHE E CZ  1 
ATOM   4539  N N   . ILE B 1 252 ? 44.159  -0.522  37.753  1.00 47.63  ? 248 ILE E N   1 
ATOM   4540  C CA  . ILE B 1 252 ? 43.584  -1.618  36.995  1.00 43.99  ? 248 ILE E CA  1 
ATOM   4541  C C   . ILE B 1 252 ? 43.515  -1.102  35.571  1.00 42.40  ? 248 ILE E C   1 
ATOM   4542  O O   . ILE B 1 252 ? 42.601  -0.355  35.219  1.00 35.37  ? 248 ILE E O   1 
ATOM   4543  C CB  . ILE B 1 252 ? 42.186  -2.015  37.504  1.00 42.20  ? 248 ILE E CB  1 
ATOM   4544  C CG1 . ILE B 1 252 ? 42.284  -2.851  38.779  1.00 41.17  ? 248 ILE E CG1 1 
ATOM   4545  C CG2 . ILE B 1 252 ? 41.462  -2.869  36.479  1.00 44.83  ? 248 ILE E CG2 1 
ATOM   4546  C CD1 . ILE B 1 252 ? 42.870  -2.121  39.964  1.00 36.04  ? 248 ILE E CD1 1 
ATOM   4547  N N   . ALA B 1 253 ? 44.504  -1.485  34.767  1.00 43.35  ? 249 ALA E N   1 
ATOM   4548  C CA  . ALA B 1 253 ? 44.652  -0.949  33.420  1.00 43.09  ? 249 ALA E CA  1 
ATOM   4549  C C   . ALA B 1 253 ? 43.684  -1.608  32.451  1.00 39.67  ? 249 ALA E C   1 
ATOM   4550  O O   . ALA B 1 253 ? 43.351  -2.783  32.607  1.00 39.14  ? 249 ALA E O   1 
ATOM   4551  C CB  . ALA B 1 253 ? 46.083  -1.129  32.933  1.00 39.14  ? 249 ALA E CB  1 
ATOM   4552  N N   . PRO B 1 254 ? 43.229  -0.851  31.445  1.00 37.50  ? 250 PRO E N   1 
ATOM   4553  C CA  . PRO B 1 254 ? 42.459  -1.460  30.371  1.00 44.91  ? 250 PRO E CA  1 
ATOM   4554  C C   . PRO B 1 254 ? 43.345  -2.329  29.491  1.00 53.12  ? 250 PRO E C   1 
ATOM   4555  O O   . PRO B 1 254 ? 44.493  -1.972  29.249  1.00 53.63  ? 250 PRO E O   1 
ATOM   4556  C CB  . PRO B 1 254 ? 41.969  -0.258  29.564  1.00 41.88  ? 250 PRO E CB  1 
ATOM   4557  C CG  . PRO B 1 254 ? 42.972  0.805   29.816  1.00 40.65  ? 250 PRO E CG  1 
ATOM   4558  C CD  . PRO B 1 254 ? 43.447  0.589   31.224  1.00 39.21  ? 250 PRO E CD  1 
ATOM   4559  N N   . GLU B 1 255 ? 42.826  -3.472  29.054  1.00 63.42  ? 251 GLU E N   1 
ATOM   4560  C CA  . GLU B 1 255 ? 43.422  -4.218  27.946  1.00 65.83  ? 251 GLU E CA  1 
ATOM   4561  C C   . GLU B 1 255 ? 42.578  -4.000  26.689  1.00 70.49  ? 251 GLU E C   1 
ATOM   4562  O O   . GLU B 1 255 ? 43.111  -3.740  25.608  1.00 56.74  ? 251 GLU E O   1 
ATOM   4563  C CB  . GLU B 1 255 ? 43.516  -5.711  28.267  1.00 70.39  ? 251 GLU E CB  1 
ATOM   4564  C CG  . GLU B 1 255 ? 44.349  -6.499  27.261  1.00 82.10  ? 251 GLU E CG  1 
ATOM   4565  C CD  . GLU B 1 255 ? 44.440  -7.983  27.577  1.00 87.42  ? 251 GLU E CD  1 
ATOM   4566  O OE1 . GLU B 1 255 ? 43.919  -8.416  28.628  1.00 94.10  ? 251 GLU E OE1 1 
ATOM   4567  O OE2 . GLU B 1 255 ? 45.041  -8.719  26.764  1.00 83.09  ? 251 GLU E OE2 1 
ATOM   4568  N N   . TYR B 1 256 ? 41.258  -4.093  26.851  1.00 71.65  ? 252 TYR E N   1 
ATOM   4569  C CA  . TYR B 1 256 ? 40.317  -3.927  25.751  1.00 66.31  ? 252 TYR E CA  1 
ATOM   4570  C C   . TYR B 1 256 ? 39.439  -2.692  25.922  1.00 70.62  ? 252 TYR E C   1 
ATOM   4571  O O   . TYR B 1 256 ? 38.998  -2.381  27.030  1.00 82.01  ? 252 TYR E O   1 
ATOM   4572  C CB  . TYR B 1 256 ? 39.430  -5.161  25.641  1.00 62.08  ? 252 TYR E CB  1 
ATOM   4573  C CG  . TYR B 1 256 ? 40.193  -6.421  25.326  1.00 63.06  ? 252 TYR E CG  1 
ATOM   4574  C CD1 . TYR B 1 256 ? 40.648  -7.253  26.342  1.00 64.93  ? 252 TYR E CD1 1 
ATOM   4575  C CD2 . TYR B 1 256 ? 40.460  -6.785  24.010  1.00 70.33  ? 252 TYR E CD2 1 
ATOM   4576  C CE1 . TYR B 1 256 ? 41.346  -8.414  26.060  1.00 63.13  ? 252 TYR E CE1 1 
ATOM   4577  C CE2 . TYR B 1 256 ? 41.158  -7.943  23.715  1.00 70.45  ? 252 TYR E CE2 1 
ATOM   4578  C CZ  . TYR B 1 256 ? 41.599  -8.753  24.744  1.00 70.23  ? 252 TYR E CZ  1 
ATOM   4579  O OH  . TYR B 1 256 ? 42.293  -9.905  24.458  1.00 81.03  ? 252 TYR E OH  1 
ATOM   4580  N N   . ALA B 1 257 ? 39.198  -1.996  24.812  1.00 67.23  ? 253 ALA E N   1 
ATOM   4581  C CA  . ALA B 1 257 ? 38.208  -0.927  24.740  1.00 67.24  ? 253 ALA E CA  1 
ATOM   4582  C C   . ALA B 1 257 ? 37.101  -1.364  23.768  1.00 67.88  ? 253 ALA E C   1 
ATOM   4583  O O   . ALA B 1 257 ? 37.113  -2.496  23.280  1.00 67.41  ? 253 ALA E O   1 
ATOM   4584  C CB  . ALA B 1 257 ? 38.857  0.368   24.282  1.00 64.16  ? 253 ALA E CB  1 
ATOM   4585  N N   . TYR B 1 258 ? 36.143  -0.482  23.498  1.00 60.80  ? 254 TYR E N   1 
ATOM   4586  C CA  . TYR B 1 258 ? 34.981  -0.844  22.689  1.00 57.59  ? 254 TYR E CA  1 
ATOM   4587  C C   . TYR B 1 258 ? 34.623  0.219   21.662  1.00 59.95  ? 254 TYR E C   1 
ATOM   4588  O O   . TYR B 1 258 ? 34.264  1.340   22.027  1.00 56.68  ? 254 TYR E O   1 
ATOM   4589  C CB  . TYR B 1 258 ? 33.773  -1.052  23.588  1.00 55.56  ? 254 TYR E CB  1 
ATOM   4590  C CG  . TYR B 1 258 ? 33.853  -2.246  24.504  1.00 55.24  ? 254 TYR E CG  1 
ATOM   4591  C CD1 . TYR B 1 258 ? 34.252  -2.107  25.830  1.00 49.58  ? 254 TYR E CD1 1 
ATOM   4592  C CD2 . TYR B 1 258 ? 33.503  -3.515  24.050  1.00 53.51  ? 254 TYR E CD2 1 
ATOM   4593  C CE1 . TYR B 1 258 ? 34.307  -3.202  26.674  1.00 52.78  ? 254 TYR E CE1 1 
ATOM   4594  C CE2 . TYR B 1 258 ? 33.552  -4.615  24.886  1.00 50.98  ? 254 TYR E CE2 1 
ATOM   4595  C CZ  . TYR B 1 258 ? 33.954  -4.455  26.196  1.00 55.21  ? 254 TYR E CZ  1 
ATOM   4596  O OH  . TYR B 1 258 ? 34.007  -5.552  27.026  1.00 60.36  ? 254 TYR E OH  1 
ATOM   4597  N N   . LYS B 1 259 ? 34.718  -0.138  20.381  1.00 66.26  ? 255 LYS E N   1 
ATOM   4598  C CA  . LYS B 1 259 ? 34.206  0.707   19.298  1.00 67.76  ? 255 LYS E CA  1 
ATOM   4599  C C   . LYS B 1 259 ? 32.702  0.858   19.471  1.00 59.39  ? 255 LYS E C   1 
ATOM   4600  O O   . LYS B 1 259 ? 32.007  -0.134  19.673  1.00 51.96  ? 255 LYS E O   1 
ATOM   4601  C CB  . LYS B 1 259 ? 34.479  0.077   17.933  1.00 73.03  ? 255 LYS E CB  1 
ATOM   4602  C CG  . LYS B 1 259 ? 35.889  0.241   17.409  1.00 80.95  ? 255 LYS E CG  1 
ATOM   4603  C CD  . LYS B 1 259 ? 35.973  -0.379  16.021  1.00 89.76  ? 255 LYS E CD  1 
ATOM   4604  C CE  . LYS B 1 259 ? 37.325  -0.191  15.362  1.00 90.87  ? 255 LYS E CE  1 
ATOM   4605  N NZ  . LYS B 1 259 ? 37.245  -0.380  13.882  1.00 88.93  ? 255 LYS E NZ  1 
ATOM   4606  N N   . ILE B 1 260 ? 32.211  2.093   19.387  1.00 53.62  ? 256 ILE E N   1 
ATOM   4607  C CA  . ILE B 1 260 ? 30.797  2.390   19.612  1.00 53.23  ? 256 ILE E CA  1 
ATOM   4608  C C   . ILE B 1 260 ? 30.244  3.361   18.569  1.00 51.67  ? 256 ILE E C   1 
ATOM   4609  O O   . ILE B 1 260 ? 30.853  4.396   18.282  1.00 43.27  ? 256 ILE E O   1 
ATOM   4610  C CB  . ILE B 1 260 ? 30.570  2.980   21.025  1.00 53.05  ? 256 ILE E CB  1 
ATOM   4611  C CG1 . ILE B 1 260 ? 30.367  1.859   22.044  1.00 54.37  ? 256 ILE E CG1 1 
ATOM   4612  C CG2 . ILE B 1 260 ? 29.357  3.900   21.052  1.00 52.03  ? 256 ILE E CG2 1 
ATOM   4613  C CD1 . ILE B 1 260 ? 29.970  2.355   23.420  1.00 53.83  ? 256 ILE E CD1 1 
ATOM   4614  N N   . VAL B 1 261 ? 29.095  3.006   17.998  1.00 51.06  ? 257 VAL E N   1 
ATOM   4615  C CA  . VAL B 1 261 ? 28.305  3.928   17.189  1.00 58.80  ? 257 VAL E CA  1 
ATOM   4616  C C   . VAL B 1 261 ? 26.889  3.955   17.762  1.00 62.84  ? 257 VAL E C   1 
ATOM   4617  O O   . VAL B 1 261 ? 26.245  2.907   17.896  1.00 58.75  ? 257 VAL E O   1 
ATOM   4618  C CB  . VAL B 1 261 ? 28.248  3.510   15.705  1.00 64.24  ? 257 VAL E CB  1 
ATOM   4619  C CG1 . VAL B 1 261 ? 27.579  4.597   14.872  1.00 60.81  ? 257 VAL E CG1 1 
ATOM   4620  C CG2 . VAL B 1 261 ? 29.641  3.232   15.168  1.00 63.91  ? 257 VAL E CG2 1 
ATOM   4621  N N   . LYS B 1 262 ? 26.421  5.151   18.111  1.00 63.23  ? 258 LYS E N   1 
ATOM   4622  C CA  . LYS B 1 262 ? 25.097  5.331   18.690  1.00 65.35  ? 258 LYS E CA  1 
ATOM   4623  C C   . LYS B 1 262 ? 24.240  6.200   17.774  1.00 68.42  ? 258 LYS E C   1 
ATOM   4624  O O   . LYS B 1 262 ? 24.667  7.278   17.352  1.00 67.01  ? 258 LYS E O   1 
ATOM   4625  C CB  . LYS B 1 262 ? 25.205  5.972   20.075  1.00 64.24  ? 258 LYS E CB  1 
ATOM   4626  C CG  . LYS B 1 262 ? 23.880  6.045   20.822  1.00 68.34  ? 258 LYS E CG  1 
ATOM   4627  C CD  . LYS B 1 262 ? 24.098  5.970   22.329  1.00 70.67  ? 258 LYS E CD  1 
ATOM   4628  C CE  . LYS B 1 262 ? 22.795  6.172   23.086  1.00 66.32  ? 258 LYS E CE  1 
ATOM   4629  N NZ  . LYS B 1 262 ? 21.925  4.959   23.013  1.00 64.27  ? 258 LYS E NZ  1 
ATOM   4630  N N   . LYS B 1 263 ? 23.033  5.721   17.480  1.00 74.00  ? 259 LYS E N   1 
ATOM   4631  C CA  . LYS B 1 263 ? 22.100  6.412   16.587  1.00 78.81  ? 259 LYS E CA  1 
ATOM   4632  C C   . LYS B 1 263 ? 20.835  6.850   17.318  1.00 76.49  ? 259 LYS E C   1 
ATOM   4633  O O   . LYS B 1 263 ? 20.330  7.949   17.079  1.00 73.64  ? 259 LYS E O   1 
ATOM   4634  C CB  . LYS B 1 263 ? 21.730  5.502   15.416  1.00 83.81  ? 259 LYS E CB  1 
ATOM   4635  C CG  . LYS B 1 263 ? 22.900  5.131   14.509  1.00 91.42  ? 259 LYS E CG  1 
ATOM   4636  C CD  . LYS B 1 263 ? 23.114  6.156   13.378  1.00 100.86 ? 259 LYS E CD  1 
ATOM   4637  C CE  . LYS B 1 263 ? 24.122  7.233   13.755  1.00 101.05 ? 259 LYS E CE  1 
ATOM   4638  N NZ  . LYS B 1 263 ? 24.027  8.408   12.842  1.00 93.83  ? 259 LYS E NZ  1 
ATOM   4639  N N   . GLY B 1 264 ? 20.322  5.988   18.195  1.00 74.66  ? 260 GLY E N   1 
ATOM   4640  C CA  . GLY B 1 264 ? 19.121  6.291   18.970  1.00 71.84  ? 260 GLY E CA  1 
ATOM   4641  C C   . GLY B 1 264 ? 19.175  5.779   20.395  1.00 64.52  ? 260 GLY E C   1 
ATOM   4642  O O   . GLY B 1 264 ? 20.198  5.258   20.841  1.00 67.86  ? 260 GLY E O   1 
ATOM   4643  N N   . ASP B 1 265 ? 18.050  5.912   21.095  1.00 68.38  ? 261 ASP E N   1 
ATOM   4644  C CA  . ASP B 1 265 ? 17.964  5.619   22.523  1.00 61.87  ? 261 ASP E CA  1 
ATOM   4645  C C   . ASP B 1 265 ? 17.010  4.472   22.812  1.00 49.85  ? 261 ASP E C   1 
ATOM   4646  O O   . ASP B 1 265 ? 16.246  4.043   21.953  1.00 55.78  ? 261 ASP E O   1 
ATOM   4647  C CB  . ASP B 1 265 ? 17.504  6.856   23.290  1.00 70.57  ? 261 ASP E CB  1 
ATOM   4648  C CG  . ASP B 1 265 ? 18.507  7.990   23.215  1.00 83.02  ? 261 ASP E CG  1 
ATOM   4649  O OD1 . ASP B 1 265 ? 19.510  7.945   23.960  1.00 91.20  ? 261 ASP E OD1 1 
ATOM   4650  O OD2 . ASP B 1 265 ? 18.298  8.923   22.415  1.00 90.16  ? 261 ASP E OD2 1 
ATOM   4651  N N   . SER B 1 266 ? 17.074  3.970   24.036  1.00 45.46  ? 262 SER E N   1 
ATOM   4652  C CA  . SER B 1 266 ? 16.223  2.876   24.466  1.00 45.55  ? 262 SER E CA  1 
ATOM   4653  C C   . SER B 1 266 ? 16.321  2.770   25.992  1.00 39.90  ? 262 SER E C   1 
ATOM   4654  O O   . SER B 1 266 ? 16.580  3.770   26.644  1.00 46.01  ? 262 SER E O   1 
ATOM   4655  C CB  . SER B 1 266 ? 16.674  1.609   23.741  1.00 46.62  ? 262 SER E CB  1 
ATOM   4656  O OG  . SER B 1 266 ? 16.836  0.499   24.598  1.00 56.32  ? 262 SER E OG  1 
ATOM   4657  N N   . THR B 1 267 ? 16.111  1.587   26.563  1.00 38.62  ? 263 THR E N   1 
ATOM   4658  C CA  . THR B 1 267 ? 16.308  1.394   27.995  1.00 44.87  ? 263 THR E CA  1 
ATOM   4659  C C   . THR B 1 267 ? 16.688  -0.055  28.317  1.00 43.43  ? 263 THR E C   1 
ATOM   4660  O O   . THR B 1 267 ? 16.828  -0.886  27.420  1.00 42.80  ? 263 THR E O   1 
ATOM   4661  C CB  . THR B 1 267 ? 15.047  1.812   28.791  1.00 49.90  ? 263 THR E CB  1 
ATOM   4662  O OG1 . THR B 1 267 ? 15.373  1.975   30.177  1.00 55.53  ? 263 THR E OG1 1 
ATOM   4663  C CG2 . THR B 1 267 ? 13.936  0.774   28.646  1.00 49.44  ? 263 THR E CG2 1 
ATOM   4664  N N   . ILE B 1 268 ? 16.859  -0.341  29.603  1.00 42.75  ? 264 ILE E N   1 
ATOM   4665  C CA  . ILE B 1 268 ? 17.149  -1.688  30.071  1.00 49.04  ? 264 ILE E CA  1 
ATOM   4666  C C   . ILE B 1 268 ? 15.863  -2.307  30.596  1.00 56.06  ? 264 ILE E C   1 
ATOM   4667  O O   . ILE B 1 268 ? 15.201  -1.725  31.455  1.00 58.68  ? 264 ILE E O   1 
ATOM   4668  C CB  . ILE B 1 268 ? 18.196  -1.682  31.201  1.00 48.63  ? 264 ILE E CB  1 
ATOM   4669  C CG1 . ILE B 1 268 ? 19.555  -1.215  30.670  1.00 50.86  ? 264 ILE E CG1 1 
ATOM   4670  C CG2 . ILE B 1 268 ? 18.338  -3.068  31.813  1.00 45.52  ? 264 ILE E CG2 1 
ATOM   4671  C CD1 . ILE B 1 268 ? 19.662  0.279   30.445  1.00 53.05  ? 264 ILE E CD1 1 
ATOM   4672  N N   . MET B 1 269 ? 15.515  -3.483  30.077  1.00 57.43  ? 265 MET E N   1 
ATOM   4673  C CA  . MET B 1 269 ? 14.311  -4.181  30.499  1.00 53.46  ? 265 MET E CA  1 
ATOM   4674  C C   . MET B 1 269 ? 14.664  -5.252  31.516  1.00 52.20  ? 265 MET E C   1 
ATOM   4675  O O   . MET B 1 269 ? 15.646  -5.971  31.349  1.00 55.14  ? 265 MET E O   1 
ATOM   4676  C CB  . MET B 1 269 ? 13.607  -4.810  29.298  1.00 60.70  ? 265 MET E CB  1 
ATOM   4677  C CG  . MET B 1 269 ? 12.195  -5.277  29.602  1.00 67.15  ? 265 MET E CG  1 
ATOM   4678  S SD  . MET B 1 269 ? 11.207  -5.509  28.111  1.00 68.96  ? 265 MET E SD  1 
ATOM   4679  C CE  . MET B 1 269 ? 11.799  -7.098  27.545  1.00 86.50  ? 265 MET E CE  1 
ATOM   4680  N N   . LYS B 1 270 ? 13.863  -5.334  32.573  1.00 49.38  ? 266 LYS E N   1 
ATOM   4681  C CA  . LYS B 1 270 ? 14.026  -6.341  33.609  1.00 54.80  ? 266 LYS E CA  1 
ATOM   4682  C C   . LYS B 1 270 ? 13.011  -7.455  33.371  1.00 63.84  ? 266 LYS E C   1 
ATOM   4683  O O   . LYS B 1 270 ? 11.813  -7.248  33.553  1.00 66.89  ? 266 LYS E O   1 
ATOM   4684  C CB  . LYS B 1 270 ? 13.800  -5.720  34.990  1.00 61.17  ? 266 LYS E CB  1 
ATOM   4685  C CG  . LYS B 1 270 ? 14.811  -4.651  35.380  1.00 68.58  ? 266 LYS E CG  1 
ATOM   4686  C CD  . LYS B 1 270 ? 16.151  -5.260  35.766  1.00 77.52  ? 266 LYS E CD  1 
ATOM   4687  C CE  . LYS B 1 270 ? 17.095  -4.234  36.381  1.00 83.58  ? 266 LYS E CE  1 
ATOM   4688  N NZ  . LYS B 1 270 ? 18.323  -4.864  36.955  1.00 87.20  ? 266 LYS E NZ  1 
ATOM   4689  N N   . SER B 1 271 ? 13.485  -8.630  32.961  1.00 64.71  ? 267 SER E N   1 
ATOM   4690  C CA  . SER B 1 271 ? 12.597  -9.745  32.657  1.00 65.53  ? 267 SER E CA  1 
ATOM   4691  C C   . SER B 1 271 ? 13.295  -11.104 32.662  1.00 69.74  ? 267 SER E C   1 
ATOM   4692  O O   . SER B 1 271 ? 14.446  -11.214 32.253  1.00 66.32  ? 267 SER E O   1 
ATOM   4693  C CB  . SER B 1 271 ? 11.955  -9.509  31.292  1.00 63.60  ? 267 SER E CB  1 
ATOM   4694  O OG  . SER B 1 271 ? 11.332  -10.681 30.797  1.00 62.14  ? 267 SER E OG  1 
ATOM   4695  N N   . GLU B 1 272 ? 12.575  -12.131 33.113  1.00 76.28  ? 268 GLU E N   1 
ATOM   4696  C CA  . GLU B 1 272 ? 13.052  -13.518 33.051  1.00 80.94  ? 268 GLU E CA  1 
ATOM   4697  C C   . GLU B 1 272 ? 12.394  -14.305 31.906  1.00 72.03  ? 268 GLU E C   1 
ATOM   4698  O O   . GLU B 1 272 ? 12.741  -15.459 31.663  1.00 68.90  ? 268 GLU E O   1 
ATOM   4699  C CB  . GLU B 1 272 ? 12.885  -14.204 34.415  1.00 86.38  ? 268 GLU E CB  1 
ATOM   4700  C CG  . GLU B 1 272 ? 14.123  -13.993 35.274  1.00 95.69  ? 268 GLU E CG  1 
ATOM   4701  C CD  . GLU B 1 272 ? 13.881  -14.126 36.768  1.00 92.00  ? 268 GLU E CD  1 
ATOM   4702  O OE1 . GLU B 1 272 ? 14.260  -15.171 37.336  1.00 85.64  ? 268 GLU E OE1 1 
ATOM   4703  O OE2 . GLU B 1 272 ? 13.332  -13.182 37.380  1.00 93.84  ? 268 GLU E OE2 1 
ATOM   4704  N N   . VAL B 1 273 ? 11.484  -13.658 31.177  1.00 68.91  ? 269 VAL E N   1 
ATOM   4705  C CA  . VAL B 1 273 ? 10.792  -14.286 30.049  1.00 68.46  ? 269 VAL E CA  1 
ATOM   4706  C C   . VAL B 1 273 ? 11.776  -14.631 28.928  1.00 68.07  ? 269 VAL E C   1 
ATOM   4707  O O   . VAL B 1 273 ? 12.707  -13.877 28.651  1.00 64.45  ? 269 VAL E O   1 
ATOM   4708  C CB  . VAL B 1 273 ? 9.648   -13.390 29.513  1.00 62.87  ? 269 VAL E CB  1 
ATOM   4709  C CG1 . VAL B 1 273 ? 9.195   -13.833 28.127  1.00 60.61  ? 269 VAL E CG1 1 
ATOM   4710  C CG2 . VAL B 1 273 ? 8.480   -13.404 30.486  1.00 54.09  ? 269 VAL E CG2 1 
ATOM   4711  N N   . GLU B 1 274 ? 11.541  -15.772 28.288  1.00 72.14  ? 270 GLU E N   1 
ATOM   4712  C CA  . GLU B 1 274 ? 12.468  -16.338 27.307  1.00 75.13  ? 270 GLU E CA  1 
ATOM   4713  C C   . GLU B 1 274 ? 12.318  -15.598 25.978  1.00 64.52  ? 270 GLU E C   1 
ATOM   4714  O O   . GLU B 1 274 ? 11.302  -14.945 25.730  1.00 71.48  ? 270 GLU E O   1 
ATOM   4715  C CB  . GLU B 1 274 ? 12.195  -17.846 27.127  1.00 90.98  ? 270 GLU E CB  1 
ATOM   4716  C CG  . GLU B 1 274 ? 13.274  -18.641 26.396  1.00 103.02 ? 270 GLU E CG  1 
ATOM   4717  C CD  . GLU B 1 274 ? 12.850  -20.062 26.070  1.00 114.61 ? 270 GLU E CD  1 
ATOM   4718  O OE1 . GLU B 1 274 ? 11.669  -20.416 26.278  1.00 118.08 ? 270 GLU E OE1 1 
ATOM   4719  O OE2 . GLU B 1 274 ? 13.710  -20.826 25.592  1.00 119.85 ? 270 GLU E OE2 1 
ATOM   4720  N N   . TYR B 1 275 ? 13.343  -15.684 25.141  1.00 55.45  ? 271 TYR E N   1 
ATOM   4721  C CA  . TYR B 1 275 ? 13.330  -15.061 23.821  1.00 57.89  ? 271 TYR E CA  1 
ATOM   4722  C C   . TYR B 1 275 ? 12.718  -16.012 22.797  1.00 65.01  ? 271 TYR E C   1 
ATOM   4723  O O   . TYR B 1 275 ? 13.200  -17.132 22.625  1.00 79.21  ? 271 TYR E O   1 
ATOM   4724  C CB  . TYR B 1 275 ? 14.758  -14.687 23.415  1.00 53.38  ? 271 TYR E CB  1 
ATOM   4725  C CG  . TYR B 1 275 ? 14.924  -14.229 21.984  1.00 53.95  ? 271 TYR E CG  1 
ATOM   4726  C CD1 . TYR B 1 275 ? 14.598  -12.932 21.604  1.00 51.16  ? 271 TYR E CD1 1 
ATOM   4727  C CD2 . TYR B 1 275 ? 15.435  -15.085 21.013  1.00 55.34  ? 271 TYR E CD2 1 
ATOM   4728  C CE1 . TYR B 1 275 ? 14.763  -12.504 20.296  1.00 52.48  ? 271 TYR E CE1 1 
ATOM   4729  C CE2 . TYR B 1 275 ? 15.601  -14.666 19.703  1.00 54.24  ? 271 TYR E CE2 1 
ATOM   4730  C CZ  . TYR B 1 275 ? 15.262  -13.375 19.349  1.00 53.99  ? 271 TYR E CZ  1 
ATOM   4731  O OH  . TYR B 1 275 ? 15.418  -12.958 18.046  1.00 52.53  ? 271 TYR E OH  1 
ATOM   4732  N N   . GLY B 1 276 ? 11.652  -15.559 22.138  1.00 71.05  ? 272 GLY E N   1 
ATOM   4733  C CA  . GLY B 1 276 ? 11.033  -16.283 21.027  1.00 68.82  ? 272 GLY E CA  1 
ATOM   4734  C C   . GLY B 1 276 ? 11.251  -15.560 19.717  1.00 71.26  ? 272 GLY E C   1 
ATOM   4735  O O   . GLY B 1 276 ? 11.119  -14.344 19.661  1.00 86.84  ? 272 GLY E O   1 
ATOM   4736  N N   . ASN B 1 277 ? 11.543  -16.309 18.658  1.00 74.71  ? 273 ASN E N   1 
ATOM   4737  C CA  . ASN B 1 277 ? 11.977  -15.720 17.384  1.00 84.14  ? 273 ASN E CA  1 
ATOM   4738  C C   . ASN B 1 277 ? 10.845  -14.957 16.700  1.00 86.28  ? 273 ASN E C   1 
ATOM   4739  O O   . ASN B 1 277 ? 10.154  -15.491 15.837  1.00 93.35  ? 273 ASN E O   1 
ATOM   4740  C CB  . ASN B 1 277 ? 12.542  -16.802 16.453  1.00 89.28  ? 273 ASN E CB  1 
ATOM   4741  C CG  . ASN B 1 277 ? 13.840  -17.402 16.968  1.00 88.96  ? 273 ASN E CG  1 
ATOM   4742  O OD1 . ASN B 1 277 ? 13.948  -17.781 18.137  1.00 85.36  ? 273 ASN E OD1 1 
ATOM   4743  N ND2 . ASN B 1 277 ? 14.831  -17.501 16.089  1.00 90.16  ? 273 ASN E ND2 1 
ATOM   4744  N N   . CYS B 1 278 ? 10.666  -13.700 17.104  1.00 90.67  ? 274 CYS E N   1 
ATOM   4745  C CA  . CYS B 1 278 ? 9.568   -12.861 16.633  1.00 86.48  ? 274 CYS E CA  1 
ATOM   4746  C C   . CYS B 1 278 ? 10.040  -11.421 16.449  1.00 78.93  ? 274 CYS E C   1 
ATOM   4747  O O   . CYS B 1 278 ? 11.127  -11.058 16.896  1.00 73.56  ? 274 CYS E O   1 
ATOM   4748  C CB  . CYS B 1 278 ? 8.409   -12.934 17.647  1.00 99.22  ? 274 CYS E CB  1 
ATOM   4749  S SG  . CYS B 1 278 ? 7.778   -11.368 18.329  1.00 124.76 ? 274 CYS E SG  1 
ATOM   4750  N N   . ASN B 1 279 ? 9.220   -10.613 15.780  1.00 79.64  ? 275 ASN E N   1 
ATOM   4751  C CA  . ASN B 1 279 ? 9.494   -9.186  15.600  1.00 72.84  ? 275 ASN E CA  1 
ATOM   4752  C C   . ASN B 1 279 ? 8.274   -8.351  15.998  1.00 75.03  ? 275 ASN E C   1 
ATOM   4753  O O   . ASN B 1 279 ? 7.146   -8.697  15.644  1.00 80.81  ? 275 ASN E O   1 
ATOM   4754  C CB  . ASN B 1 279 ? 9.885   -8.901  14.146  1.00 66.34  ? 275 ASN E CB  1 
ATOM   4755  C CG  . ASN B 1 279 ? 10.391  -7.481  13.937  1.00 70.85  ? 275 ASN E CG  1 
ATOM   4756  O OD1 . ASN B 1 279 ? 10.941  -6.863  14.846  1.00 79.88  ? 275 ASN E OD1 1 
ATOM   4757  N ND2 . ASN B 1 279 ? 10.220  -6.964  12.726  1.00 66.82  ? 275 ASN E ND2 1 
ATOM   4758  N N   . THR B 1 280 ? 8.504   -7.267  16.743  1.00 71.89  ? 276 THR E N   1 
ATOM   4759  C CA  . THR B 1 280 ? 7.425   -6.388  17.204  1.00 66.12  ? 276 THR E CA  1 
ATOM   4760  C C   . THR B 1 280 ? 7.799   -4.926  17.055  1.00 59.93  ? 276 THR E C   1 
ATOM   4761  O O   . THR B 1 280 ? 8.963   -4.594  16.838  1.00 56.62  ? 276 THR E O   1 
ATOM   4762  C CB  . THR B 1 280 ? 7.109   -6.583  18.714  1.00 68.65  ? 276 THR E CB  1 
ATOM   4763  O OG1 . THR B 1 280 ? 7.774   -7.743  19.239  1.00 81.87  ? 276 THR E OG1 1 
ATOM   4764  C CG2 . THR B 1 280 ? 5.617   -6.689  18.941  1.00 69.90  ? 276 THR E CG2 1 
ATOM   4765  N N   . ARG B 1 281 ? 6.794   -4.062  17.187  1.00 59.40  ? 277 ARG E N   1 
ATOM   4766  C CA  . ARG B 1 281 ? 7.006   -2.620  17.311  1.00 59.06  ? 277 ARG E CA  1 
ATOM   4767  C C   . ARG B 1 281 ? 6.847   -2.179  18.766  1.00 51.74  ? 277 ARG E C   1 
ATOM   4768  O O   . ARG B 1 281 ? 7.092   -1.020  19.087  1.00 50.08  ? 277 ARG E O   1 
ATOM   4769  C CB  . ARG B 1 281 ? 6.008   -1.832  16.458  1.00 64.87  ? 277 ARG E CB  1 
ATOM   4770  C CG  . ARG B 1 281 ? 5.660   -2.434  15.105  1.00 72.65  ? 277 ARG E CG  1 
ATOM   4771  C CD  . ARG B 1 281 ? 5.296   -1.369  14.088  1.00 79.24  ? 277 ARG E CD  1 
ATOM   4772  N NE  . ARG B 1 281 ? 4.476   -0.294  14.634  1.00 90.24  ? 277 ARG E NE  1 
ATOM   4773  C CZ  . ARG B 1 281 ? 3.159   -0.348  14.829  1.00 86.90  ? 277 ARG E CZ  1 
ATOM   4774  N NH1 . ARG B 1 281 ? 2.455   -1.449  14.561  1.00 91.88  ? 277 ARG E NH1 1 
ATOM   4775  N NH2 . ARG B 1 281 ? 2.544   0.719   15.323  1.00 81.84  ? 277 ARG E NH2 1 
ATOM   4776  N N   . CYS B 1 282 ? 6.424   -3.100  19.631  1.00 46.81  ? 278 CYS E N   1 
ATOM   4777  C CA  . CYS B 1 282 ? 6.144   -2.790  21.027  1.00 47.98  ? 278 CYS E CA  1 
ATOM   4778  C C   . CYS B 1 282 ? 6.411   -4.000  21.918  1.00 44.04  ? 278 CYS E C   1 
ATOM   4779  O O   . CYS B 1 282 ? 5.704   -5.009  21.837  1.00 41.89  ? 278 CYS E O   1 
ATOM   4780  C CB  . CYS B 1 282 ? 4.690   -2.339  21.188  1.00 53.52  ? 278 CYS E CB  1 
ATOM   4781  S SG  . CYS B 1 282 ? 4.185   -2.048  22.908  1.00 54.93  ? 278 CYS E SG  1 
ATOM   4782  N N   . GLN B 1 283 ? 7.420   -3.879  22.778  1.00 41.76  ? 279 GLN E N   1 
ATOM   4783  C CA  . GLN B 1 283 ? 7.827   -4.963  23.668  1.00 45.79  ? 279 GLN E CA  1 
ATOM   4784  C C   . GLN B 1 283 ? 7.504   -4.650  25.126  1.00 43.80  ? 279 GLN E C   1 
ATOM   4785  O O   . GLN B 1 283 ? 7.688   -3.529  25.595  1.00 41.33  ? 279 GLN E O   1 
ATOM   4786  C CB  . GLN B 1 283 ? 9.330   -5.226  23.538  1.00 47.34  ? 279 GLN E CB  1 
ATOM   4787  C CG  . GLN B 1 283 ? 9.834   -6.401  24.368  1.00 45.40  ? 279 GLN E CG  1 
ATOM   4788  C CD  . GLN B 1 283 ? 9.234   -7.728  23.943  1.00 48.68  ? 279 GLN E CD  1 
ATOM   4789  O OE1 . GLN B 1 283 ? 9.315   -8.116  22.774  1.00 47.33  ? 279 GLN E OE1 1 
ATOM   4790  N NE2 . GLN B 1 283 ? 8.637   -8.439  24.895  1.00 50.78  ? 279 GLN E NE2 1 
ATOM   4791  N N   . THR B 1 284 ? 7.056   -5.677  25.834  1.00 43.92  ? 280 THR E N   1 
ATOM   4792  C CA  . THR B 1 284 ? 6.738   -5.591  27.245  1.00 49.06  ? 280 THR E CA  1 
ATOM   4793  C C   . THR B 1 284 ? 7.571   -6.645  27.996  1.00 55.33  ? 280 THR E C   1 
ATOM   4794  O O   . THR B 1 284 ? 7.987   -7.639  27.400  1.00 53.43  ? 280 THR E O   1 
ATOM   4795  C CB  . THR B 1 284 ? 5.217   -5.795  27.435  1.00 46.01  ? 280 THR E CB  1 
ATOM   4796  O OG1 . THR B 1 284 ? 4.583   -4.522  27.559  1.00 55.43  ? 280 THR E OG1 1 
ATOM   4797  C CG2 . THR B 1 284 ? 4.893   -6.627  28.649  1.00 45.29  ? 280 THR E CG2 1 
ATOM   4798  N N   . PRO B 1 285 ? 7.834   -6.427  29.298  1.00 56.30  ? 281 PRO E N   1 
ATOM   4799  C CA  . PRO B 1 285 ? 8.602   -7.396  30.092  1.00 59.69  ? 281 PRO E CA  1 
ATOM   4800  C C   . PRO B 1 285 ? 7.961   -8.782  30.227  1.00 63.75  ? 281 PRO E C   1 
ATOM   4801  O O   . PRO B 1 285 ? 8.645   -9.740  30.594  1.00 71.46  ? 281 PRO E O   1 
ATOM   4802  C CB  . PRO B 1 285 ? 8.687   -6.728  31.473  1.00 63.58  ? 281 PRO E CB  1 
ATOM   4803  C CG  . PRO B 1 285 ? 8.493   -5.276  31.207  1.00 61.07  ? 281 PRO E CG  1 
ATOM   4804  C CD  . PRO B 1 285 ? 7.504   -5.227  30.086  1.00 58.36  ? 281 PRO E CD  1 
ATOM   4805  N N   . ILE B 1 286 ? 6.659   -8.870  29.966  1.00 61.69  ? 282 ILE E N   1 
ATOM   4806  C CA  . ILE B 1 286 ? 5.908   -10.124 30.013  1.00 55.43  ? 282 ILE E CA  1 
ATOM   4807  C C   . ILE B 1 286 ? 5.521   -10.661 28.621  1.00 47.47  ? 282 ILE E C   1 
ATOM   4808  O O   . ILE B 1 286 ? 5.012   -11.776 28.510  1.00 53.06  ? 282 ILE E O   1 
ATOM   4809  C CB  . ILE B 1 286 ? 4.653   -9.919  30.902  1.00 61.17  ? 282 ILE E CB  1 
ATOM   4810  C CG1 . ILE B 1 286 ? 5.072   -9.841  32.374  1.00 58.91  ? 282 ILE E CG1 1 
ATOM   4811  C CG2 . ILE B 1 286 ? 3.630   -11.029 30.718  1.00 70.15  ? 282 ILE E CG2 1 
ATOM   4812  C CD1 . ILE B 1 286 ? 4.037   -9.200  33.273  1.00 59.03  ? 282 ILE E CD1 1 
ATOM   4813  N N   . GLY B 1 287 ? 5.781   -9.891  27.566  1.00 42.86  ? 283 GLY E N   1 
ATOM   4814  C CA  . GLY B 1 287 ? 5.487   -10.327 26.196  1.00 40.01  ? 283 GLY E CA  1 
ATOM   4815  C C   . GLY B 1 287 ? 5.348   -9.181  25.205  1.00 41.07  ? 283 GLY E C   1 
ATOM   4816  O O   . GLY B 1 287 ? 5.176   -8.033  25.598  1.00 44.28  ? 283 GLY E O   1 
ATOM   4817  N N   . ALA B 1 288 ? 5.410   -9.497  23.914  1.00 42.84  ? 284 ALA E N   1 
ATOM   4818  C CA  . ALA B 1 288 ? 5.316   -8.489  22.856  1.00 43.82  ? 284 ALA E CA  1 
ATOM   4819  C C   . ALA B 1 288 ? 3.860   -8.221  22.460  1.00 48.30  ? 284 ALA E C   1 
ATOM   4820  O O   . ALA B 1 288 ? 2.984   -9.048  22.710  1.00 55.19  ? 284 ALA E O   1 
ATOM   4821  C CB  . ALA B 1 288 ? 6.119   -8.928  21.644  1.00 36.29  ? 284 ALA E CB  1 
ATOM   4822  N N   . ILE B 1 289 ? 3.620   -7.062  21.844  1.00 50.57  ? 285 ILE E N   1 
ATOM   4823  C CA  . ILE B 1 289 ? 2.275   -6.633  21.445  1.00 49.76  ? 285 ILE E CA  1 
ATOM   4824  C C   . ILE B 1 289 ? 2.207   -6.283  19.955  1.00 51.17  ? 285 ILE E C   1 
ATOM   4825  O O   . ILE B 1 289 ? 3.021   -5.500  19.451  1.00 48.23  ? 285 ILE E O   1 
ATOM   4826  C CB  . ILE B 1 289 ? 1.829   -5.379  22.226  1.00 47.22  ? 285 ILE E CB  1 
ATOM   4827  C CG1 . ILE B 1 289 ? 1.719   -5.676  23.719  1.00 47.97  ? 285 ILE E CG1 1 
ATOM   4828  C CG2 . ILE B 1 289 ? 0.488   -4.875  21.716  1.00 51.46  ? 285 ILE E CG2 1 
ATOM   4829  C CD1 . ILE B 1 289 ? 1.434   -4.450  24.564  1.00 48.26  ? 285 ILE E CD1 1 
ATOM   4830  N N   . ASN B 1 290 ? 1.226   -6.865  19.269  1.00 52.14  ? 286 ASN E N   1 
ATOM   4831  C CA  . ASN B 1 290 ? 0.908   -6.515  17.889  1.00 63.29  ? 286 ASN E CA  1 
ATOM   4832  C C   . ASN B 1 290 ? -0.544  -6.047  17.787  1.00 60.35  ? 286 ASN E C   1 
ATOM   4833  O O   . ASN B 1 290 ? -1.471  -6.856  17.820  1.00 68.41  ? 286 ASN E O   1 
ATOM   4834  C CB  . ASN B 1 290 ? 1.150   -7.733  16.985  1.00 66.52  ? 286 ASN E CB  1 
ATOM   4835  C CG  . ASN B 1 290 ? 1.143   -7.391  15.503  1.00 59.80  ? 286 ASN E CG  1 
ATOM   4836  O OD1 . ASN B 1 290 ? 1.205   -6.224  15.114  1.00 54.30  ? 286 ASN E OD1 1 
ATOM   4837  N ND2 . ASN B 1 290 ? 1.081   -8.420  14.665  1.00 61.18  ? 286 ASN E ND2 1 
ATOM   4838  N N   . SER B 1 291 ? -0.736  -4.734  17.682  1.00 58.10  ? 287 SER E N   1 
ATOM   4839  C CA  . SER B 1 291 ? -2.071  -4.160  17.616  1.00 60.74  ? 287 SER E CA  1 
ATOM   4840  C C   . SER B 1 291 ? -2.067  -2.779  16.999  1.00 55.12  ? 287 SER E C   1 
ATOM   4841  O O   . SER B 1 291 ? -1.072  -2.060  17.038  1.00 48.52  ? 287 SER E O   1 
ATOM   4842  C CB  . SER B 1 291 ? -2.664  -4.044  19.018  1.00 67.30  ? 287 SER E CB  1 
ATOM   4843  O OG  . SER B 1 291 ? -2.042  -3.014  19.759  1.00 72.27  ? 287 SER E OG  1 
ATOM   4844  N N   . SER B 1 292 ? -3.216  -2.413  16.460  1.00 52.83  ? 288 SER E N   1 
ATOM   4845  C CA  . SER B 1 292 ? -3.461  -1.052  16.018  1.00 51.59  ? 288 SER E CA  1 
ATOM   4846  C C   . SER B 1 292 ? -4.334  -0.316  17.052  1.00 44.10  ? 288 SER E C   1 
ATOM   4847  O O   . SER B 1 292 ? -4.542  0.892   16.926  1.00 41.17  ? 288 SER E O   1 
ATOM   4848  C CB  . SER B 1 292 ? -4.084  -1.065  14.619  1.00 55.72  ? 288 SER E CB  1 
ATOM   4849  O OG  . SER B 1 292 ? -5.144  -2.005  14.530  1.00 63.90  ? 288 SER E OG  1 
ATOM   4850  N N   . MET B 1 293 ? -4.792  -1.030  18.092  1.00 39.53  ? 289 MET E N   1 
ATOM   4851  C CA  . MET B 1 293 ? -5.675  -0.452  19.109  1.00 42.64  ? 289 MET E CA  1 
ATOM   4852  C C   . MET B 1 293 ? -5.016  0.695   19.872  1.00 39.82  ? 289 MET E C   1 
ATOM   4853  O O   . MET B 1 293 ? -3.813  0.668   20.132  1.00 44.27  ? 289 MET E O   1 
ATOM   4854  C CB  . MET B 1 293 ? -6.141  -1.511  20.126  1.00 48.61  ? 289 MET E CB  1 
ATOM   4855  C CG  . MET B 1 293 ? -7.001  -2.636  19.568  1.00 49.71  ? 289 MET E CG  1 
ATOM   4856  S SD  . MET B 1 293 ? -8.504  -2.091  18.731  1.00 55.78  ? 289 MET E SD  1 
ATOM   4857  C CE  . MET B 1 293 ? -7.907  -1.968  17.042  1.00 54.42  ? 289 MET E CE  1 
ATOM   4858  N N   . PRO B 1 294 ? -5.815  1.697   20.260  1.00 42.89  ? 290 PRO E N   1 
ATOM   4859  C CA  . PRO B 1 294 ? -5.280  2.884   20.931  1.00 42.50  ? 290 PRO E CA  1 
ATOM   4860  C C   . PRO B 1 294 ? -4.878  2.691   22.394  1.00 36.91  ? 290 PRO E C   1 
ATOM   4861  O O   . PRO B 1 294 ? -4.036  3.442   22.878  1.00 40.62  ? 290 PRO E O   1 
ATOM   4862  C CB  . PRO B 1 294 ? -6.427  3.892   20.822  1.00 43.93  ? 290 PRO E CB  1 
ATOM   4863  C CG  . PRO B 1 294 ? -7.657  3.056   20.768  1.00 46.79  ? 290 PRO E CG  1 
ATOM   4864  C CD  . PRO B 1 294 ? -7.278  1.773   20.085  1.00 44.91  ? 290 PRO E CD  1 
ATOM   4865  N N   . PHE B 1 295 ? -5.452  1.701   23.085  1.00 35.74  ? 291 PHE E N   1 
ATOM   4866  C CA  . PHE B 1 295 ? -5.176  1.491   24.519  1.00 36.44  ? 291 PHE E CA  1 
ATOM   4867  C C   . PHE B 1 295 ? -4.802  0.052   24.874  1.00 38.27  ? 291 PHE E C   1 
ATOM   4868  O O   . PHE B 1 295 ? -5.180  -0.885  24.168  1.00 51.00  ? 291 PHE E O   1 
ATOM   4869  C CB  . PHE B 1 295 ? -6.390  1.897   25.351  1.00 33.55  ? 291 PHE E CB  1 
ATOM   4870  C CG  . PHE B 1 295 ? -6.874  3.285   25.074  1.00 30.61  ? 291 PHE E CG  1 
ATOM   4871  C CD1 . PHE B 1 295 ? -8.034  3.499   24.352  1.00 32.35  ? 291 PHE E CD1 1 
ATOM   4872  C CD2 . PHE B 1 295 ? -6.162  4.377   25.524  1.00 31.79  ? 291 PHE E CD2 1 
ATOM   4873  C CE1 . PHE B 1 295 ? -8.477  4.781   24.085  1.00 33.84  ? 291 PHE E CE1 1 
ATOM   4874  C CE2 . PHE B 1 295 ? -6.601  5.664   25.265  1.00 35.42  ? 291 PHE E CE2 1 
ATOM   4875  C CZ  . PHE B 1 295 ? -7.761  5.865   24.544  1.00 34.38  ? 291 PHE E CZ  1 
ATOM   4876  N N   . HIS B 1 296 ? -4.053  -0.111  25.966  1.00 34.10  ? 292 HIS E N   1 
ATOM   4877  C CA  . HIS B 1 296 ? -3.718  -1.438  26.497  1.00 37.03  ? 292 HIS E CA  1 
ATOM   4878  C C   . HIS B 1 296 ? -3.649  -1.448  28.005  1.00 39.07  ? 292 HIS E C   1 
ATOM   4879  O O   . HIS B 1 296 ? -3.528  -0.391  28.632  1.00 42.21  ? 292 HIS E O   1 
ATOM   4880  C CB  . HIS B 1 296 ? -2.416  -1.971  25.880  1.00 38.35  ? 292 HIS E CB  1 
ATOM   4881  C CG  . HIS B 1 296 ? -1.146  -1.419  26.506  1.00 40.77  ? 292 HIS E CG  1 
ATOM   4882  N ND1 . HIS B 1 296 ? -0.540  -0.304  26.059  1.00 43.83  ? 292 HIS E ND1 1 
ATOM   4883  C CD2 . HIS B 1 296 ? -0.362  -1.893  27.554  1.00 44.38  ? 292 HIS E CD2 1 
ATOM   4884  C CE1 . HIS B 1 296 ? 0.563   -0.068  26.796  1.00 42.04  ? 292 HIS E CE1 1 
ATOM   4885  N NE2 . HIS B 1 296 ? 0.669   -1.038  27.709  1.00 42.92  ? 292 HIS E NE2 1 
ATOM   4886  N N   . ASN B 1 297 ? -3.758  -2.641  28.595  1.00 35.81  ? 293 ASN E N   1 
ATOM   4887  C CA  . ASN B 1 297 ? -3.620  -2.817  30.050  1.00 37.04  ? 293 ASN E CA  1 
ATOM   4888  C C   . ASN B 1 297 ? -2.612  -3.907  30.443  1.00 38.23  ? 293 ASN E C   1 
ATOM   4889  O O   . ASN B 1 297 ? -2.628  -4.397  31.576  1.00 35.10  ? 293 ASN E O   1 
ATOM   4890  C CB  . ASN B 1 297 ? -4.979  -3.122  30.684  1.00 37.12  ? 293 ASN E CB  1 
ATOM   4891  C CG  . ASN B 1 297 ? -5.487  -4.516  30.348  1.00 38.23  ? 293 ASN E CG  1 
ATOM   4892  O OD1 . ASN B 1 297 ? -5.113  -5.104  29.329  1.00 45.32  ? 293 ASN E OD1 1 
ATOM   4893  N ND2 . ASN B 1 297 ? -6.331  -5.056  31.214  1.00 35.07  ? 293 ASN E ND2 1 
ATOM   4894  N N   . ILE B 1 298 ? -1.742  -4.266  29.502  1.00 36.28  ? 294 ILE E N   1 
ATOM   4895  C CA  . ILE B 1 298 ? -0.712  -5.283  29.713  1.00 40.09  ? 294 ILE E CA  1 
ATOM   4896  C C   . ILE B 1 298 ? 0.301   -4.916  30.802  1.00 41.61  ? 294 ILE E C   1 
ATOM   4897  O O   . ILE B 1 298 ? 0.398   -5.605  31.815  1.00 46.02  ? 294 ILE E O   1 
ATOM   4898  C CB  . ILE B 1 298 ? 0.093   -5.571  28.417  1.00 40.02  ? 294 ILE E CB  1 
ATOM   4899  C CG1 . ILE B 1 298 ? -0.823  -5.791  27.203  1.00 40.19  ? 294 ILE E CG1 1 
ATOM   4900  C CG2 . ILE B 1 298 ? 1.014   -6.762  28.623  1.00 38.42  ? 294 ILE E CG2 1 
ATOM   4901  C CD1 . ILE B 1 298 ? -2.019  -6.676  27.472  1.00 39.05  ? 294 ILE E CD1 1 
ATOM   4902  N N   . HIS B 1 299 ? 1.064   -3.845  30.582  1.00 45.29  ? 295 HIS E N   1 
ATOM   4903  C CA  . HIS B 1 299 ? 2.220   -3.531  31.426  1.00 46.93  ? 295 HIS E CA  1 
ATOM   4904  C C   . HIS B 1 299 ? 2.724   -2.132  31.164  1.00 45.63  ? 295 HIS E C   1 
ATOM   4905  O O   . HIS B 1 299 ? 2.768   -1.702  30.009  1.00 43.60  ? 295 HIS E O   1 
ATOM   4906  C CB  . HIS B 1 299 ? 3.343   -4.529  31.145  1.00 52.96  ? 295 HIS E CB  1 
ATOM   4907  C CG  . HIS B 1 299 ? 4.305   -4.705  32.292  1.00 54.70  ? 295 HIS E CG  1 
ATOM   4908  N ND1 . HIS B 1 299 ? 5.390   -3.932  32.451  1.00 53.37  ? 295 HIS E ND1 1 
ATOM   4909  C CD2 . HIS B 1 299 ? 4.309   -5.609  33.352  1.00 56.19  ? 295 HIS E CD2 1 
ATOM   4910  C CE1 . HIS B 1 299 ? 6.052   -4.314  33.556  1.00 53.42  ? 295 HIS E CE1 1 
ATOM   4911  N NE2 . HIS B 1 299 ? 5.392   -5.343  34.103  1.00 53.01  ? 295 HIS E NE2 1 
ATOM   4912  N N   . PRO B 1 300 ? 3.123   -1.401  32.223  1.00 39.47  ? 296 PRO E N   1 
ATOM   4913  C CA  . PRO B 1 300 ? 3.604   -0.026  32.029  1.00 38.80  ? 296 PRO E CA  1 
ATOM   4914  C C   . PRO B 1 300 ? 4.998   0.106   31.401  1.00 41.16  ? 296 PRO E C   1 
ATOM   4915  O O   . PRO B 1 300 ? 5.253   1.075   30.689  1.00 42.38  ? 296 PRO E O   1 
ATOM   4916  C CB  . PRO B 1 300 ? 3.606   0.555   33.453  1.00 35.48  ? 296 PRO E CB  1 
ATOM   4917  C CG  . PRO B 1 300 ? 3.710   -0.625  34.354  1.00 36.64  ? 296 PRO E CG  1 
ATOM   4918  C CD  . PRO B 1 300 ? 2.998   -1.746  33.652  1.00 39.90  ? 296 PRO E CD  1 
ATOM   4919  N N   . LEU B 1 301 ? 5.889   -0.844  31.668  1.00 43.85  ? 297 LEU E N   1 
ATOM   4920  C CA  . LEU B 1 301 ? 7.298   -0.716  31.273  1.00 44.35  ? 297 LEU E CA  1 
ATOM   4921  C C   . LEU B 1 301 ? 7.547   -1.172  29.845  1.00 44.58  ? 297 LEU E C   1 
ATOM   4922  O O   . LEU B 1 301 ? 8.230   -2.156  29.607  1.00 51.47  ? 297 LEU E O   1 
ATOM   4923  C CB  . LEU B 1 301 ? 8.195   -1.501  32.237  1.00 44.63  ? 297 LEU E CB  1 
ATOM   4924  C CG  . LEU B 1 301 ? 7.968   -1.172  33.709  1.00 44.18  ? 297 LEU E CG  1 
ATOM   4925  C CD1 . LEU B 1 301 ? 9.035   -1.810  34.589  1.00 36.39  ? 297 LEU E CD1 1 
ATOM   4926  C CD2 . LEU B 1 301 ? 7.944   0.342   33.858  1.00 45.56  ? 297 LEU E CD2 1 
ATOM   4927  N N   . THR B 1 302 ? 7.005   -0.430  28.891  1.00 47.27  ? 298 THR E N   1 
ATOM   4928  C CA  . THR B 1 302 ? 7.040   -0.836  27.498  1.00 42.37  ? 298 THR E CA  1 
ATOM   4929  C C   . THR B 1 302 ? 8.166   -0.155  26.732  1.00 41.57  ? 298 THR E C   1 
ATOM   4930  O O   . THR B 1 302 ? 8.612   0.928   27.106  1.00 39.80  ? 298 THR E O   1 
ATOM   4931  C CB  . THR B 1 302 ? 5.698   -0.513  26.832  1.00 40.92  ? 298 THR E CB  1 
ATOM   4932  O OG1 . THR B 1 302 ? 5.449   0.893   26.922  1.00 37.20  ? 298 THR E OG1 1 
ATOM   4933  C CG2 . THR B 1 302 ? 4.576   -1.262  27.531  1.00 36.83  ? 298 THR E CG2 1 
ATOM   4934  N N   . ILE B 1 303 ? 8.624   -0.805  25.662  1.00 45.48  ? 299 ILE E N   1 
ATOM   4935  C CA  . ILE B 1 303 ? 9.651   -0.246  24.779  1.00 45.45  ? 299 ILE E CA  1 
ATOM   4936  C C   . ILE B 1 303 ? 9.177   -0.395  23.343  1.00 40.12  ? 299 ILE E C   1 
ATOM   4937  O O   . ILE B 1 303 ? 8.956   -1.513  22.881  1.00 43.93  ? 299 ILE E O   1 
ATOM   4938  C CB  . ILE B 1 303 ? 11.015  -0.967  24.927  1.00 47.99  ? 299 ILE E CB  1 
ATOM   4939  C CG1 . ILE B 1 303 ? 11.442  -1.047  26.395  1.00 47.92  ? 299 ILE E CG1 1 
ATOM   4940  C CG2 . ILE B 1 303 ? 12.086  -0.244  24.118  1.00 41.24  ? 299 ILE E CG2 1 
ATOM   4941  C CD1 . ILE B 1 303 ? 12.781  -1.723  26.604  1.00 55.62  ? 299 ILE E CD1 1 
ATOM   4942  N N   . GLY B 1 304 ? 9.025   0.724   22.642  1.00 41.09  ? 300 GLY E N   1 
ATOM   4943  C CA  . GLY B 1 304 ? 8.501   0.714   21.276  1.00 45.54  ? 300 GLY E CA  1 
ATOM   4944  C C   . GLY B 1 304 ? 7.425   1.757   21.027  1.00 46.93  ? 300 GLY E C   1 
ATOM   4945  O O   . GLY B 1 304 ? 7.191   2.630   21.859  1.00 50.21  ? 300 GLY E O   1 
ATOM   4946  N N   . GLU B 1 305 ? 6.780   1.663   19.867  1.00 51.03  ? 301 GLU E N   1 
ATOM   4947  C CA  . GLU B 1 305 ? 5.591   2.453   19.562  1.00 54.46  ? 301 GLU E CA  1 
ATOM   4948  C C   . GLU B 1 305 ? 4.387   1.685   20.092  1.00 51.80  ? 301 GLU E C   1 
ATOM   4949  O O   . GLU B 1 305 ? 3.899   0.763   19.438  1.00 54.91  ? 301 GLU E O   1 
ATOM   4950  C CB  . GLU B 1 305 ? 5.462   2.664   18.053  1.00 63.36  ? 301 GLU E CB  1 
ATOM   4951  C CG  . GLU B 1 305 ? 6.582   3.484   17.428  1.00 74.55  ? 301 GLU E CG  1 
ATOM   4952  C CD  . GLU B 1 305 ? 6.609   3.377   15.912  1.00 81.08  ? 301 GLU E CD  1 
ATOM   4953  O OE1 . GLU B 1 305 ? 6.141   4.310   15.220  1.00 86.84  ? 301 GLU E OE1 1 
ATOM   4954  O OE2 . GLU B 1 305 ? 7.092   2.344   15.412  1.00 80.14  ? 301 GLU E OE2 1 
ATOM   4955  N N   . CYS B 1 306 ? 3.920   2.055   21.283  1.00 48.91  ? 302 CYS E N   1 
ATOM   4956  C CA  . CYS B 1 306 ? 2.903   1.279   21.989  1.00 51.25  ? 302 CYS E CA  1 
ATOM   4957  C C   . CYS B 1 306 ? 1.582   2.031   22.158  1.00 43.60  ? 302 CYS E C   1 
ATOM   4958  O O   . CYS B 1 306 ? 1.550   3.255   22.111  1.00 47.02  ? 302 CYS E O   1 
ATOM   4959  C CB  . CYS B 1 306 ? 3.424   0.863   23.367  1.00 55.16  ? 302 CYS E CB  1 
ATOM   4960  S SG  . CYS B 1 306 ? 4.898   -0.180  23.309  1.00 66.97  ? 302 CYS E SG  1 
ATOM   4961  N N   . PRO B 1 307 ? 0.484   1.292   22.371  1.00 40.42  ? 303 PRO E N   1 
ATOM   4962  C CA  . PRO B 1 307 ? -0.762  1.939   22.768  1.00 40.28  ? 303 PRO E CA  1 
ATOM   4963  C C   . PRO B 1 307 ? -0.622  2.587   24.140  1.00 40.52  ? 303 PRO E C   1 
ATOM   4964  O O   . PRO B 1 307 ? 0.329   2.302   24.862  1.00 34.95  ? 303 PRO E O   1 
ATOM   4965  C CB  . PRO B 1 307 ? -1.762  0.779   22.822  1.00 42.69  ? 303 PRO E CB  1 
ATOM   4966  C CG  . PRO B 1 307 ? -1.170  -0.283  21.957  1.00 46.68  ? 303 PRO E CG  1 
ATOM   4967  C CD  . PRO B 1 307 ? 0.306   -0.154  22.146  1.00 45.03  ? 303 PRO E CD  1 
ATOM   4968  N N   . LYS B 1 308 ? -1.567  3.447   24.499  1.00 40.04  ? 304 LYS E N   1 
ATOM   4969  C CA  . LYS B 1 308 ? -1.495  4.151   25.770  1.00 37.15  ? 304 LYS E CA  1 
ATOM   4970  C C   . LYS B 1 308 ? -1.931  3.243   26.918  1.00 32.96  ? 304 LYS E C   1 
ATOM   4971  O O   . LYS B 1 308 ? -3.010  2.655   26.882  1.00 30.95  ? 304 LYS E O   1 
ATOM   4972  C CB  . LYS B 1 308 ? -2.338  5.424   25.714  1.00 37.91  ? 304 LYS E CB  1 
ATOM   4973  C CG  . LYS B 1 308 ? -1.878  6.401   24.638  1.00 41.77  ? 304 LYS E CG  1 
ATOM   4974  C CD  . LYS B 1 308 ? -0.566  7.086   25.004  1.00 43.70  ? 304 LYS E CD  1 
ATOM   4975  C CE  . LYS B 1 308 ? 0.332   7.309   23.797  1.00 44.95  ? 304 LYS E CE  1 
ATOM   4976  N NZ  . LYS B 1 308 ? -0.352  7.999   22.676  1.00 50.65  ? 304 LYS E NZ  1 
ATOM   4977  N N   . TYR B 1 309 ? -1.068  3.114   27.924  1.00 33.22  ? 305 TYR E N   1 
ATOM   4978  C CA  . TYR B 1 309 ? -1.351  2.258   29.073  1.00 34.93  ? 305 TYR E CA  1 
ATOM   4979  C C   . TYR B 1 309 ? -2.499  2.840   29.874  1.00 34.24  ? 305 TYR E C   1 
ATOM   4980  O O   . TYR B 1 309 ? -2.531  4.035   30.143  1.00 33.07  ? 305 TYR E O   1 
ATOM   4981  C CB  . TYR B 1 309 ? -0.120  2.108   29.970  1.00 34.51  ? 305 TYR E CB  1 
ATOM   4982  C CG  . TYR B 1 309 ? -0.306  1.119   31.102  1.00 35.59  ? 305 TYR E CG  1 
ATOM   4983  C CD1 . TYR B 1 309 ? -0.657  -0.204  30.847  1.00 38.85  ? 305 TYR E CD1 1 
ATOM   4984  C CD2 . TYR B 1 309 ? -0.123  1.500   32.426  1.00 38.81  ? 305 TYR E CD2 1 
ATOM   4985  C CE1 . TYR B 1 309 ? -0.826  -1.113  31.878  1.00 39.11  ? 305 TYR E CE1 1 
ATOM   4986  C CE2 . TYR B 1 309 ? -0.293  0.595   33.466  1.00 38.27  ? 305 TYR E CE2 1 
ATOM   4987  C CZ  . TYR B 1 309 ? -0.640  -0.710  33.186  1.00 38.66  ? 305 TYR E CZ  1 
ATOM   4988  O OH  . TYR B 1 309 ? -0.810  -1.618  34.211  1.00 41.81  ? 305 TYR E OH  1 
ATOM   4989  N N   . VAL B 1 310 ? -3.427  1.977   30.265  1.00 38.18  ? 306 VAL E N   1 
ATOM   4990  C CA  . VAL B 1 310 ? -4.672  2.405   30.874  1.00 38.46  ? 306 VAL E CA  1 
ATOM   4991  C C   . VAL B 1 310 ? -5.070  1.393   31.940  1.00 42.22  ? 306 VAL E C   1 
ATOM   4992  O O   . VAL B 1 310 ? -4.675  0.234   31.868  1.00 49.08  ? 306 VAL E O   1 
ATOM   4993  C CB  . VAL B 1 310 ? -5.756  2.510   29.788  1.00 35.43  ? 306 VAL E CB  1 
ATOM   4994  C CG1 . VAL B 1 310 ? -6.697  1.319   29.835  1.00 34.28  ? 306 VAL E CG1 1 
ATOM   4995  C CG2 . VAL B 1 310 ? -6.514  3.811   29.928  1.00 38.61  ? 306 VAL E CG2 1 
ATOM   4996  N N   . LYS B 1 311 ? -5.848  1.827   32.923  1.00 45.46  ? 307 LYS E N   1 
ATOM   4997  C CA  . LYS B 1 311 ? -6.245  0.956   34.026  1.00 48.36  ? 307 LYS E CA  1 
ATOM   4998  C C   . LYS B 1 311 ? -7.709  0.561   33.867  1.00 48.51  ? 307 LYS E C   1 
ATOM   4999  O O   . LYS B 1 311 ? -8.590  1.117   34.518  1.00 56.76  ? 307 LYS E O   1 
ATOM   5000  C CB  . LYS B 1 311 ? -5.994  1.651   35.367  1.00 51.13  ? 307 LYS E CB  1 
ATOM   5001  C CG  . LYS B 1 311 ? -5.902  0.705   36.558  1.00 56.76  ? 307 LYS E CG  1 
ATOM   5002  C CD  . LYS B 1 311 ? -7.151  0.756   37.430  1.00 62.99  ? 307 LYS E CD  1 
ATOM   5003  C CE  . LYS B 1 311 ? -7.012  -0.115  38.667  1.00 59.75  ? 307 LYS E CE  1 
ATOM   5004  N NZ  . LYS B 1 311 ? -6.013  0.442   39.617  1.00 61.45  ? 307 LYS E NZ  1 
ATOM   5005  N N   . SER B 1 312 ? -7.953  -0.402  32.982  1.00 45.95  ? 308 SER E N   1 
ATOM   5006  C CA  . SER B 1 312 ? -9.307  -0.843  32.631  1.00 50.15  ? 308 SER E CA  1 
ATOM   5007  C C   . SER B 1 312 ? -9.264  -2.287  32.143  1.00 54.23  ? 308 SER E C   1 
ATOM   5008  O O   . SER B 1 312 ? -8.279  -2.699  31.544  1.00 56.81  ? 308 SER E O   1 
ATOM   5009  C CB  . SER B 1 312 ? -9.879  0.024   31.485  1.00 52.12  ? 308 SER E CB  1 
ATOM   5010  O OG  . SER B 1 312 ? -9.736  1.418   31.713  1.00 58.98  ? 308 SER E OG  1 
ATOM   5011  N N   . ASN B 1 313 ? -10.333 -3.046  32.376  1.00 55.40  ? 309 ASN E N   1 
ATOM   5012  C CA  . ASN B 1 313 ? -10.458 -4.403  31.826  1.00 63.19  ? 309 ASN E CA  1 
ATOM   5013  C C   . ASN B 1 313 ? -11.187 -4.436  30.480  1.00 60.44  ? 309 ASN E C   1 
ATOM   5014  O O   . ASN B 1 313 ? -10.941 -5.330  29.660  1.00 69.79  ? 309 ASN E O   1 
ATOM   5015  C CB  . ASN B 1 313 ? -11.176 -5.324  32.822  1.00 71.79  ? 309 ASN E CB  1 
ATOM   5016  C CG  . ASN B 1 313 ? -10.311 -5.678  34.021  1.00 73.05  ? 309 ASN E CG  1 
ATOM   5017  O OD1 . ASN B 1 313 ? -9.110  -5.917  33.891  1.00 82.05  ? 309 ASN E OD1 1 
ATOM   5018  N ND2 . ASN B 1 313 ? -10.924 -5.723  35.198  1.00 73.16  ? 309 ASN E ND2 1 
ATOM   5019  N N   . LYS B 1 314 ? -12.073 -3.462  30.265  1.00 59.22  ? 310 LYS E N   1 
ATOM   5020  C CA  . LYS B 1 314 ? -12.942 -3.402  29.091  1.00 59.74  ? 310 LYS E CA  1 
ATOM   5021  C C   . LYS B 1 314 ? -13.069 -1.975  28.553  1.00 51.19  ? 310 LYS E C   1 
ATOM   5022  O O   . LYS B 1 314 ? -13.283 -1.044  29.323  1.00 54.98  ? 310 LYS E O   1 
ATOM   5023  C CB  . LYS B 1 314 ? -14.342 -3.941  29.452  1.00 68.24  ? 310 LYS E CB  1 
ATOM   5024  C CG  . LYS B 1 314 ? -14.581 -5.395  29.077  1.00 82.19  ? 310 LYS E CG  1 
ATOM   5025  C CD  . LYS B 1 314 ? -16.037 -5.799  29.399  1.00 88.91  ? 310 LYS E CD  1 
ATOM   5026  C CE  . LYS B 1 314 ? -16.168 -6.495  30.745  1.00 93.52  ? 310 LYS E CE  1 
ATOM   5027  N NZ  . LYS B 1 314 ? -17.530 -7.072  30.933  1.00 85.97  ? 310 LYS E NZ  1 
ATOM   5028  N N   . LEU B 1 315 ? -12.926 -1.807  27.238  1.00 43.06  ? 311 LEU E N   1 
ATOM   5029  C CA  . LEU B 1 315 ? -13.359 -0.575  26.570  1.00 42.19  ? 311 LEU E CA  1 
ATOM   5030  C C   . LEU B 1 315 ? -14.167 -0.954  25.331  1.00 41.38  ? 311 LEU E C   1 
ATOM   5031  O O   . LEU B 1 315 ? -13.640 -1.005  24.220  1.00 41.24  ? 311 LEU E O   1 
ATOM   5032  C CB  . LEU B 1 315 ? -12.173 0.322   26.195  1.00 38.47  ? 311 LEU E CB  1 
ATOM   5033  C CG  . LEU B 1 315 ? -11.390 0.925   27.374  1.00 38.38  ? 311 LEU E CG  1 
ATOM   5034  C CD1 . LEU B 1 315 ? -10.133 1.630   26.893  1.00 44.81  ? 311 LEU E CD1 1 
ATOM   5035  C CD2 . LEU B 1 315 ? -12.231 1.868   28.222  1.00 35.92  ? 311 LEU E CD2 1 
ATOM   5036  N N   . VAL B 1 316 ? -15.454 -1.210  25.537  1.00 38.03  ? 312 VAL E N   1 
ATOM   5037  C CA  . VAL B 1 316 ? -16.299 -1.781  24.497  1.00 38.43  ? 312 VAL E CA  1 
ATOM   5038  C C   . VAL B 1 316 ? -17.185 -0.733  23.835  1.00 38.05  ? 312 VAL E C   1 
ATOM   5039  O O   . VAL B 1 316 ? -18.030 -0.113  24.481  1.00 33.33  ? 312 VAL E O   1 
ATOM   5040  C CB  . VAL B 1 316 ? -17.168 -2.905  25.070  1.00 39.65  ? 312 VAL E CB  1 
ATOM   5041  C CG1 . VAL B 1 316 ? -17.959 -3.581  23.962  1.00 41.80  ? 312 VAL E CG1 1 
ATOM   5042  C CG2 . VAL B 1 316 ? -16.295 -3.918  25.795  1.00 38.70  ? 312 VAL E CG2 1 
ATOM   5043  N N   . LEU B 1 317 ? -16.972 -0.547  22.533  1.00 43.57  ? 313 LEU E N   1 
ATOM   5044  C CA  . LEU B 1 317 ? -17.754 0.386   21.726  1.00 43.10  ? 313 LEU E CA  1 
ATOM   5045  C C   . LEU B 1 317 ? -18.962 -0.337  21.157  1.00 47.19  ? 313 LEU E C   1 
ATOM   5046  O O   . LEU B 1 317 ? -18.821 -1.392  20.531  1.00 41.96  ? 313 LEU E O   1 
ATOM   5047  C CB  . LEU B 1 317 ? -16.907 0.952   20.577  1.00 43.00  ? 313 LEU E CB  1 
ATOM   5048  C CG  . LEU B 1 317 ? -16.487 2.426   20.593  1.00 43.67  ? 313 LEU E CG  1 
ATOM   5049  C CD1 . LEU B 1 317 ? -16.345 3.000   21.994  1.00 47.90  ? 313 LEU E CD1 1 
ATOM   5050  C CD2 . LEU B 1 317 ? -15.186 2.578   19.824  1.00 46.41  ? 313 LEU E CD2 1 
ATOM   5051  N N   . ALA B 1 318 ? -20.147 0.222   21.393  1.00 50.57  ? 314 ALA E N   1 
ATOM   5052  C CA  . ALA B 1 318 ? -21.367 -0.296  20.791  1.00 47.59  ? 314 ALA E CA  1 
ATOM   5053  C C   . ALA B 1 318 ? -21.287 0.015   19.311  1.00 42.14  ? 314 ALA E C   1 
ATOM   5054  O O   . ALA B 1 318 ? -21.141 1.168   18.914  1.00 45.66  ? 314 ALA E O   1 
ATOM   5055  C CB  . ALA B 1 318 ? -22.600 0.341   21.409  1.00 43.08  ? 314 ALA E CB  1 
ATOM   5056  N N   . THR B 1 319 ? -21.339 -1.032  18.504  1.00 45.19  ? 315 THR E N   1 
ATOM   5057  C CA  . THR B 1 319 ? -21.219 -0.912  17.065  1.00 48.69  ? 315 THR E CA  1 
ATOM   5058  C C   . THR B 1 319 ? -22.467 -1.423  16.327  1.00 47.72  ? 315 THR E C   1 
ATOM   5059  O O   . THR B 1 319 ? -22.487 -1.431  15.098  1.00 56.98  ? 315 THR E O   1 
ATOM   5060  C CB  . THR B 1 319 ? -19.924 -1.631  16.620  1.00 49.48  ? 315 THR E CB  1 
ATOM   5061  O OG1 . THR B 1 319 ? -19.318 -0.926  15.529  1.00 52.73  ? 315 THR E OG1 1 
ATOM   5062  C CG2 . THR B 1 319 ? -20.180 -3.081  16.245  1.00 54.28  ? 315 THR E CG2 1 
ATOM   5063  N N   . GLY B 1 320 ? -23.500 -1.813  17.083  1.00 43.17  ? 316 GLY E N   1 
ATOM   5064  C CA  . GLY B 1 320 ? -24.811 -2.211  16.550  1.00 44.00  ? 316 GLY E CA  1 
ATOM   5065  C C   . GLY B 1 320 ? -25.971 -1.626  17.348  1.00 43.82  ? 316 GLY E C   1 
ATOM   5066  O O   . GLY B 1 320 ? -25.849 -0.549  17.929  1.00 42.13  ? 316 GLY E O   1 
ATOM   5067  N N   . LEU B 1 321 ? -27.087 -2.353  17.394  1.00 40.27  ? 317 LEU E N   1 
ATOM   5068  C CA  . LEU B 1 321 ? -28.327 -1.861  17.989  1.00 40.43  ? 317 LEU E CA  1 
ATOM   5069  C C   . LEU B 1 321 ? -28.574 -2.483  19.356  1.00 38.55  ? 317 LEU E C   1 
ATOM   5070  O O   . LEU B 1 321 ? -27.934 -3.470  19.719  1.00 39.09  ? 317 LEU E O   1 
ATOM   5071  C CB  . LEU B 1 321 ? -29.505 -2.220  17.081  1.00 42.41  ? 317 LEU E CB  1 
ATOM   5072  C CG  . LEU B 1 321 ? -29.399 -1.862  15.598  1.00 45.92  ? 317 LEU E CG  1 
ATOM   5073  C CD1 . LEU B 1 321 ? -29.977 -2.966  14.731  1.00 48.82  ? 317 LEU E CD1 1 
ATOM   5074  C CD2 . LEU B 1 321 ? -30.100 -0.540  15.324  1.00 45.11  ? 317 LEU E CD2 1 
ATOM   5075  N N   . ARG B 1 322 ? -29.509 -1.903  20.108  1.00 39.32  ? 318 ARG E N   1 
ATOM   5076  C CA  . ARG B 1 322 ? -30.017 -2.533  21.330  1.00 43.66  ? 318 ARG E CA  1 
ATOM   5077  C C   . ARG B 1 322 ? -30.618 -3.887  20.990  1.00 46.72  ? 318 ARG E C   1 
ATOM   5078  O O   . ARG B 1 322 ? -31.358 -4.015  20.013  1.00 43.44  ? 318 ARG E O   1 
ATOM   5079  C CB  . ARG B 1 322 ? -31.110 -1.688  21.986  1.00 42.41  ? 318 ARG E CB  1 
ATOM   5080  C CG  . ARG B 1 322 ? -30.639 -0.430  22.672  1.00 43.77  ? 318 ARG E CG  1 
ATOM   5081  C CD  . ARG B 1 322 ? -31.822 0.295   23.293  1.00 44.54  ? 318 ARG E CD  1 
ATOM   5082  N NE  . ARG B 1 322 ? -31.481 1.681   23.619  1.00 45.56  ? 318 ARG E NE  1 
ATOM   5083  C CZ  . ARG B 1 322 ? -31.074 2.115   24.811  1.00 45.48  ? 318 ARG E CZ  1 
ATOM   5084  N NH1 . ARG B 1 322 ? -30.953 1.286   25.844  1.00 55.33  ? 318 ARG E NH1 1 
ATOM   5085  N NH2 . ARG B 1 322 ? -30.790 3.403   24.974  1.00 47.84  ? 318 ARG E NH2 1 
ATOM   5086  N N   . ASN B 1 323 ? -30.328 -4.883  21.816  1.00 57.99  ? 319 ASN E N   1 
ATOM   5087  C CA  . ASN B 1 323 ? -30.755 -6.246  21.557  1.00 68.04  ? 319 ASN E CA  1 
ATOM   5088  C C   . ASN B 1 323 ? -31.139 -6.944  22.870  1.00 71.95  ? 319 ASN E C   1 
ATOM   5089  O O   . ASN B 1 323 ? -30.415 -7.812  23.354  1.00 79.75  ? 319 ASN E O   1 
ATOM   5090  C CB  . ASN B 1 323 ? -29.631 -7.017  20.854  1.00 67.83  ? 319 ASN E CB  1 
ATOM   5091  C CG  . ASN B 1 323 ? -30.014 -8.445  20.570  1.00 69.72  ? 319 ASN E CG  1 
ATOM   5092  O OD1 . ASN B 1 323 ? -29.257 -9.358  20.851  1.00 66.18  ? 319 ASN E OD1 1 
ATOM   5093  N ND2 . ASN B 1 323 ? -31.215 -8.643  20.037  1.00 88.41  ? 319 ASN E ND2 1 
ATOM   5094  N N   . SER B 1 324 ? -32.280 -6.561  23.439  1.00 73.38  ? 320 SER E N   1 
ATOM   5095  C CA  . SER B 1 324 ? -32.723 -7.103  24.732  1.00 86.00  ? 320 SER E CA  1 
ATOM   5096  C C   . SER B 1 324 ? -33.909 -8.034  24.519  1.00 89.63  ? 320 SER E C   1 
ATOM   5097  O O   . SER B 1 324 ? -34.021 -8.676  23.473  1.00 87.56  ? 320 SER E O   1 
ATOM   5098  C CB  . SER B 1 324 ? -33.075 -5.986  25.730  1.00 81.82  ? 320 SER E CB  1 
ATOM   5099  O OG  . SER B 1 324 ? -34.198 -5.234  25.309  1.00 82.23  ? 320 SER E OG  1 
ATOM   5100  N N   . ILE C 2 10  ? -43.850 24.231  23.829  1.00 63.68  ? 10  ILE B N   1 
ATOM   5101  C CA  . ILE C 2 10  ? -44.125 24.150  25.294  1.00 66.88  ? 10  ILE B CA  1 
ATOM   5102  C C   . ILE C 2 10  ? -43.397 25.298  25.986  1.00 74.00  ? 10  ILE B C   1 
ATOM   5103  O O   . ILE C 2 10  ? -42.185 25.394  25.898  1.00 82.10  ? 10  ILE B O   1 
ATOM   5104  C CB  . ILE C 2 10  ? -43.724 22.751  25.858  1.00 62.91  ? 10  ILE B CB  1 
ATOM   5105  C CG1 . ILE C 2 10  ? -43.943 22.633  27.373  1.00 59.01  ? 10  ILE B CG1 1 
ATOM   5106  C CG2 . ILE C 2 10  ? -42.280 22.429  25.501  1.00 67.66  ? 10  ILE B CG2 1 
ATOM   5107  C CD1 . ILE C 2 10  ? -45.325 23.037  27.845  1.00 57.88  ? 10  ILE B CD1 1 
ATOM   5108  N N   . GLU C 2 11  ? -44.146 26.157  26.678  1.00 75.77  ? 11  GLU B N   1 
ATOM   5109  C CA  . GLU C 2 11  ? -43.647 27.485  27.077  1.00 74.56  ? 11  GLU B CA  1 
ATOM   5110  C C   . GLU C 2 11  ? -42.653 27.440  28.233  1.00 75.42  ? 11  GLU B C   1 
ATOM   5111  O O   . GLU C 2 11  ? -41.672 28.188  28.263  1.00 80.33  ? 11  GLU B O   1 
ATOM   5112  C CB  . GLU C 2 11  ? -44.805 28.393  27.505  1.00 80.15  ? 11  GLU B CB  1 
ATOM   5113  C CG  . GLU C 2 11  ? -45.954 28.517  26.505  1.00 86.50  ? 11  GLU B CG  1 
ATOM   5114  C CD  . GLU C 2 11  ? -45.607 29.360  25.290  1.00 87.65  ? 11  GLU B CD  1 
ATOM   5115  O OE1 . GLU C 2 11  ? -46.137 30.487  25.157  1.00 85.52  ? 11  GLU B OE1 1 
ATOM   5116  O OE2 . GLU C 2 11  ? -44.800 28.892  24.463  1.00 90.55  ? 11  GLU B OE2 1 
ATOM   5117  N N   . GLY C 2 12  ? -42.932 26.563  29.187  1.00 70.21  ? 12  GLY B N   1 
ATOM   5118  C CA  . GLY C 2 12  ? -42.235 26.552  30.473  1.00 64.57  ? 12  GLY B CA  1 
ATOM   5119  C C   . GLY C 2 12  ? -42.736 25.365  31.269  1.00 60.66  ? 12  GLY B C   1 
ATOM   5120  O O   . GLY C 2 12  ? -43.425 24.506  30.719  1.00 57.23  ? 12  GLY B O   1 
ATOM   5121  N N   . GLY C 2 13  ? -42.440 25.347  32.566  1.00 55.00  ? 13  GLY B N   1 
ATOM   5122  C CA  . GLY C 2 13  ? -42.733 24.199  33.421  1.00 50.13  ? 13  GLY B CA  1 
ATOM   5123  C C   . GLY C 2 13  ? -43.863 24.428  34.407  1.00 43.01  ? 13  GLY B C   1 
ATOM   5124  O O   . GLY C 2 13  ? -44.191 25.564  34.730  1.00 42.46  ? 13  GLY B O   1 
ATOM   5125  N N   . TRP C 2 14  ? -44.447 23.332  34.889  1.00 42.03  ? 14  TRP B N   1 
ATOM   5126  C CA  . TRP C 2 14  ? -45.492 23.376  35.911  1.00 36.87  ? 14  TRP B CA  1 
ATOM   5127  C C   . TRP C 2 14  ? -44.884 23.431  37.280  1.00 34.52  ? 14  TRP B C   1 
ATOM   5128  O O   . TRP C 2 14  ? -44.335 22.438  37.755  1.00 33.64  ? 14  TRP B O   1 
ATOM   5129  C CB  . TRP C 2 14  ? -46.370 22.126  35.865  1.00 36.17  ? 14  TRP B CB  1 
ATOM   5130  C CG  . TRP C 2 14  ? -46.962 21.736  34.532  1.00 35.57  ? 14  TRP B CG  1 
ATOM   5131  C CD1 . TRP C 2 14  ? -47.264 20.448  34.095  1.00 36.00  ? 14  TRP B CD1 1 
ATOM   5132  C CD2 . TRP C 2 14  ? -47.364 22.612  33.426  1.00 34.52  ? 14  TRP B CD2 1 
ATOM   5133  N NE1 . TRP C 2 14  ? -47.806 20.469  32.841  1.00 36.25  ? 14  TRP B NE1 1 
ATOM   5134  C CE2 . TRP C 2 14  ? -47.893 21.728  32.378  1.00 36.82  ? 14  TRP B CE2 1 
ATOM   5135  C CE3 . TRP C 2 14  ? -47.337 23.978  33.202  1.00 35.04  ? 14  TRP B CE3 1 
ATOM   5136  C CZ2 . TRP C 2 14  ? -48.363 22.217  31.172  1.00 37.84  ? 14  TRP B CZ2 1 
ATOM   5137  C CZ3 . TRP C 2 14  ? -47.818 24.459  31.979  1.00 36.98  ? 14  TRP B CZ3 1 
ATOM   5138  C CH2 . TRP C 2 14  ? -48.319 23.600  30.989  1.00 38.44  ? 14  TRP B CH2 1 
ATOM   5139  N N   . GLN C 2 15  ? -44.982 24.571  37.952  1.00 36.96  ? 15  GLN B N   1 
ATOM   5140  C CA  . GLN C 2 15  ? -44.642 24.615  39.380  1.00 41.58  ? 15  GLN B CA  1 
ATOM   5141  C C   . GLN C 2 15  ? -45.688 23.838  40.189  1.00 39.86  ? 15  GLN B C   1 
ATOM   5142  O O   . GLN C 2 15  ? -45.391 23.325  41.268  1.00 42.45  ? 15  GLN B O   1 
ATOM   5143  C CB  . GLN C 2 15  ? -44.532 26.053  39.891  1.00 44.05  ? 15  GLN B CB  1 
ATOM   5144  C CG  . GLN C 2 15  ? -43.980 26.166  41.314  1.00 45.28  ? 15  GLN B CG  1 
ATOM   5145  C CD  . GLN C 2 15  ? -42.888 27.212  41.477  1.00 49.30  ? 15  GLN B CD  1 
ATOM   5146  O OE1 . GLN C 2 15  ? -42.466 27.853  40.513  1.00 56.51  ? 15  GLN B OE1 1 
ATOM   5147  N NE2 . GLN C 2 15  ? -42.416 27.380  42.706  1.00 50.00  ? 15  GLN B NE2 1 
ATOM   5148  N N   . GLY C 2 16  ? -46.903 23.752  39.651  1.00 39.54  ? 16  GLY B N   1 
ATOM   5149  C CA  . GLY C 2 16  ? -47.992 23.010  40.279  1.00 44.54  ? 16  GLY B CA  1 
ATOM   5150  C C   . GLY C 2 16  ? -47.855 21.497  40.221  1.00 47.97  ? 16  GLY B C   1 
ATOM   5151  O O   . GLY C 2 16  ? -48.483 20.795  41.010  1.00 49.30  ? 16  GLY B O   1 
ATOM   5152  N N   . MET C 2 17  ? -47.055 20.985  39.284  1.00 51.52  ? 17  MET B N   1 
ATOM   5153  C CA  . MET C 2 17  ? -46.790 19.546  39.210  1.00 50.88  ? 17  MET B CA  1 
ATOM   5154  C C   . MET C 2 17  ? -45.579 19.193  40.071  1.00 51.38  ? 17  MET B C   1 
ATOM   5155  O O   . MET C 2 17  ? -44.446 19.507  39.715  1.00 45.96  ? 17  MET B O   1 
ATOM   5156  C CB  . MET C 2 17  ? -46.558 19.096  37.764  1.00 48.58  ? 17  MET B CB  1 
ATOM   5157  C CG  . MET C 2 17  ? -46.618 17.585  37.590  1.00 47.14  ? 17  MET B CG  1 
ATOM   5158  S SD  . MET C 2 17  ? -46.266 17.027  35.914  1.00 46.72  ? 17  MET B SD  1 
ATOM   5159  C CE  . MET C 2 17  ? -44.614 17.679  35.676  1.00 51.09  ? 17  MET B CE  1 
ATOM   5160  N N   . VAL C 2 18  ? -45.836 18.525  41.193  1.00 57.65  ? 18  VAL B N   1 
ATOM   5161  C CA  . VAL C 2 18  ? -44.809 18.233  42.206  1.00 56.65  ? 18  VAL B CA  1 
ATOM   5162  C C   . VAL C 2 18  ? -44.275 16.798  42.090  1.00 53.56  ? 18  VAL B C   1 
ATOM   5163  O O   . VAL C 2 18  ? -43.068 16.549  42.181  1.00 55.66  ? 18  VAL B O   1 
ATOM   5164  C CB  . VAL C 2 18  ? -45.367 18.454  43.637  1.00 59.83  ? 18  VAL B CB  1 
ATOM   5165  C CG1 . VAL C 2 18  ? -44.271 18.291  44.683  1.00 59.25  ? 18  VAL B CG1 1 
ATOM   5166  C CG2 . VAL C 2 18  ? -46.017 19.826  43.750  1.00 57.08  ? 18  VAL B CG2 1 
ATOM   5167  N N   . ASP C 2 19  ? -45.195 15.869  41.861  1.00 52.02  ? 19  ASP B N   1 
ATOM   5168  C CA  . ASP C 2 19  ? -44.934 14.434  41.948  1.00 52.16  ? 19  ASP B CA  1 
ATOM   5169  C C   . ASP C 2 19  ? -44.006 13.846  40.880  1.00 47.63  ? 19  ASP B C   1 
ATOM   5170  O O   . ASP C 2 19  ? -43.548 12.724  41.058  1.00 48.81  ? 19  ASP B O   1 
ATOM   5171  C CB  . ASP C 2 19  ? -46.266 13.667  41.975  1.00 58.62  ? 19  ASP B CB  1 
ATOM   5172  C CG  . ASP C 2 19  ? -47.312 14.262  41.042  1.00 65.69  ? 19  ASP B CG  1 
ATOM   5173  O OD1 . ASP C 2 19  ? -47.714 15.395  41.338  1.00 69.22  ? 19  ASP B OD1 1 
ATOM   5174  O OD2 . ASP C 2 19  ? -47.740 13.625  40.045  1.00 66.21  ? 19  ASP B OD2 1 
ATOM   5175  N N   . GLY C 2 20  ? -43.720 14.573  39.797  1.00 39.67  ? 20  GLY B N   1 
ATOM   5176  C CA  . GLY C 2 20  ? -42.788 14.073  38.785  1.00 36.91  ? 20  GLY B CA  1 
ATOM   5177  C C   . GLY C 2 20  ? -42.039 15.118  37.978  1.00 34.63  ? 20  GLY B C   1 
ATOM   5178  O O   . GLY C 2 20  ? -41.984 16.285  38.350  1.00 38.80  ? 20  GLY B O   1 
ATOM   5179  N N   . TRP C 2 21  ? -41.451 14.674  36.868  1.00 32.09  ? 21  TRP B N   1 
ATOM   5180  C CA  . TRP C 2 21  ? -40.647 15.526  35.981  1.00 30.00  ? 21  TRP B CA  1 
ATOM   5181  C C   . TRP C 2 21  ? -41.386 15.895  34.733  1.00 27.59  ? 21  TRP B C   1 
ATOM   5182  O O   . TRP C 2 21  ? -41.394 17.062  34.346  1.00 27.39  ? 21  TRP B O   1 
ATOM   5183  C CB  . TRP C 2 21  ? -39.342 14.824  35.612  1.00 30.99  ? 21  TRP B CB  1 
ATOM   5184  C CG  . TRP C 2 21  ? -38.189 15.109  36.549  1.00 31.36  ? 21  TRP B CG  1 
ATOM   5185  C CD1 . TRP C 2 21  ? -38.221 15.761  37.787  1.00 31.97  ? 21  TRP B CD1 1 
ATOM   5186  C CD2 . TRP C 2 21  ? -36.786 14.736  36.358  1.00 31.67  ? 21  TRP B CD2 1 
ATOM   5187  N NE1 . TRP C 2 21  ? -36.969 15.828  38.340  1.00 31.96  ? 21  TRP B NE1 1 
ATOM   5188  C CE2 . TRP C 2 21  ? -36.063 15.229  37.540  1.00 30.83  ? 21  TRP B CE2 1 
ATOM   5189  C CE3 . TRP C 2 21  ? -36.079 14.071  35.364  1.00 31.59  ? 21  TRP B CE3 1 
ATOM   5190  C CZ2 . TRP C 2 21  ? -34.701 15.053  37.691  1.00 28.42  ? 21  TRP B CZ2 1 
ATOM   5191  C CZ3 . TRP C 2 21  ? -34.701 13.895  35.535  1.00 29.97  ? 21  TRP B CZ3 1 
ATOM   5192  C CH2 . TRP C 2 21  ? -34.033 14.378  36.670  1.00 28.95  ? 21  TRP B CH2 1 
ATOM   5193  N N   . TYR C 2 22  ? -42.000 14.908  34.085  1.00 26.49  ? 22  TYR B N   1 
ATOM   5194  C CA  . TYR C 2 22  ? -42.840 15.151  32.914  1.00 28.73  ? 22  TYR B CA  1 
ATOM   5195  C C   . TYR C 2 22  ? -44.247 14.656  33.214  1.00 30.07  ? 22  TYR B C   1 
ATOM   5196  O O   . TYR C 2 22  ? -44.423 13.695  33.960  1.00 34.56  ? 22  TYR B O   1 
ATOM   5197  C CB  . TYR C 2 22  ? -42.299 14.422  31.682  1.00 30.48  ? 22  TYR B CB  1 
ATOM   5198  C CG  . TYR C 2 22  ? -40.784 14.349  31.580  1.00 29.97  ? 22  TYR B CG  1 
ATOM   5199  C CD1 . TYR C 2 22  ? -40.128 13.123  31.593  1.00 28.77  ? 22  TYR B CD1 1 
ATOM   5200  C CD2 . TYR C 2 22  ? -40.014 15.501  31.459  1.00 30.69  ? 22  TYR B CD2 1 
ATOM   5201  C CE1 . TYR C 2 22  ? -38.749 13.046  31.488  1.00 30.51  ? 22  TYR B CE1 1 
ATOM   5202  C CE2 . TYR C 2 22  ? -38.629 15.433  31.355  1.00 33.23  ? 22  TYR B CE2 1 
ATOM   5203  C CZ  . TYR C 2 22  ? -38.004 14.201  31.368  1.00 32.85  ? 22  TYR B CZ  1 
ATOM   5204  O OH  . TYR C 2 22  ? -36.632 14.123  31.259  1.00 31.21  ? 22  TYR B OH  1 
ATOM   5205  N N   . GLY C 2 23  ? -45.253 15.305  32.638  1.00 28.36  ? 23  GLY B N   1 
ATOM   5206  C CA  . GLY C 2 23  ? -46.629 14.900  32.887  1.00 26.18  ? 23  GLY B CA  1 
ATOM   5207  C C   . GLY C 2 23  ? -47.681 15.693  32.145  1.00 25.73  ? 23  GLY B C   1 
ATOM   5208  O O   . GLY C 2 23  ? -47.396 16.347  31.142  1.00 28.45  ? 23  GLY B O   1 
ATOM   5209  N N   . TYR C 2 24  ? -48.909 15.621  32.649  1.00 26.25  ? 24  TYR B N   1 
ATOM   5210  C CA  . TYR C 2 24  ? -50.067 16.197  31.978  1.00 27.95  ? 24  TYR B CA  1 
ATOM   5211  C C   . TYR C 2 24  ? -50.823 17.169  32.873  1.00 28.47  ? 24  TYR B C   1 
ATOM   5212  O O   . TYR C 2 24  ? -50.771 17.063  34.100  1.00 28.22  ? 24  TYR B O   1 
ATOM   5213  C CB  . TYR C 2 24  ? -51.032 15.093  31.559  1.00 28.78  ? 24  TYR B CB  1 
ATOM   5214  C CG  . TYR C 2 24  ? -50.386 13.915  30.876  1.00 30.45  ? 24  TYR B CG  1 
ATOM   5215  C CD1 . TYR C 2 24  ? -49.951 12.817  31.609  1.00 30.94  ? 24  TYR B CD1 1 
ATOM   5216  C CD2 . TYR C 2 24  ? -50.225 13.888  29.496  1.00 33.07  ? 24  TYR B CD2 1 
ATOM   5217  C CE1 . TYR C 2 24  ? -49.370 11.727  30.989  1.00 31.99  ? 24  TYR B CE1 1 
ATOM   5218  C CE2 . TYR C 2 24  ? -49.644 12.801  28.864  1.00 32.92  ? 24  TYR B CE2 1 
ATOM   5219  C CZ  . TYR C 2 24  ? -49.219 11.725  29.615  1.00 32.46  ? 24  TYR B CZ  1 
ATOM   5220  O OH  . TYR C 2 24  ? -48.640 10.644  28.999  1.00 34.13  ? 24  TYR B OH  1 
ATOM   5221  N N   . HIS C 2 25  ? -51.513 18.117  32.241  1.00 28.14  ? 25  HIS B N   1 
ATOM   5222  C CA  . HIS C 2 25  ? -52.493 18.961  32.907  1.00 30.21  ? 25  HIS B CA  1 
ATOM   5223  C C   . HIS C 2 25  ? -53.745 18.967  32.087  1.00 29.89  ? 25  HIS B C   1 
ATOM   5224  O O   . HIS C 2 25  ? -53.690 19.167  30.877  1.00 28.27  ? 25  HIS B O   1 
ATOM   5225  C CB  . HIS C 2 25  ? -51.984 20.385  33.061  1.00 31.26  ? 25  HIS B CB  1 
ATOM   5226  C CG  . HIS C 2 25  ? -52.996 21.322  33.667  1.00 35.86  ? 25  HIS B CG  1 
ATOM   5227  N ND1 . HIS C 2 25  ? -53.186 21.414  34.993  1.00 40.54  ? 25  HIS B ND1 1 
ATOM   5228  C CD2 . HIS C 2 25  ? -53.898 22.207  33.077  1.00 37.85  ? 25  HIS B CD2 1 
ATOM   5229  C CE1 . HIS C 2 25  ? -54.149 22.317  35.247  1.00 40.35  ? 25  HIS B CE1 1 
ATOM   5230  N NE2 . HIS C 2 25  ? -54.584 22.803  34.074  1.00 40.27  ? 25  HIS B NE2 1 
ATOM   5231  N N   . HIS C 2 26  ? -54.883 18.755  32.736  1.00 31.85  ? 26  HIS B N   1 
ATOM   5232  C CA  . HIS C 2 26  ? -56.167 18.737  32.045  1.00 36.01  ? 26  HIS B CA  1 
ATOM   5233  C C   . HIS C 2 26  ? -57.140 19.687  32.674  1.00 36.52  ? 26  HIS B C   1 
ATOM   5234  O O   . HIS C 2 26  ? -57.011 20.041  33.848  1.00 38.84  ? 26  HIS B O   1 
ATOM   5235  C CB  . HIS C 2 26  ? -56.754 17.332  32.053  1.00 39.94  ? 26  HIS B CB  1 
ATOM   5236  C CG  . HIS C 2 26  ? -57.112 16.835  33.428  1.00 49.03  ? 26  HIS B CG  1 
ATOM   5237  N ND1 . HIS C 2 26  ? -58.298 17.100  34.003  1.00 51.74  ? 26  HIS B ND1 1 
ATOM   5238  C CD2 . HIS C 2 26  ? -56.387 16.085  34.349  1.00 53.08  ? 26  HIS B CD2 1 
ATOM   5239  C CE1 . HIS C 2 26  ? -58.335 16.546  35.224  1.00 50.29  ? 26  HIS B CE1 1 
ATOM   5240  N NE2 . HIS C 2 26  ? -57.166 15.923  35.436  1.00 50.74  ? 26  HIS B NE2 1 
ATOM   5241  N N   . SER C 2 27  ? -58.125 20.116  31.892  1.00 35.10  ? 27  SER B N   1 
ATOM   5242  C CA  . SER C 2 27  ? -59.250 20.874  32.419  1.00 36.78  ? 27  SER B CA  1 
ATOM   5243  C C   . SER C 2 27  ? -60.511 20.486  31.661  1.00 33.11  ? 27  SER B C   1 
ATOM   5244  O O   . SER C 2 27  ? -60.518 20.444  30.432  1.00 31.81  ? 27  SER B O   1 
ATOM   5245  C CB  . SER C 2 27  ? -58.995 22.380  32.323  1.00 42.02  ? 27  SER B CB  1 
ATOM   5246  O OG  . SER C 2 27  ? -58.884 22.798  30.974  1.00 51.97  ? 27  SER B OG  1 
ATOM   5247  N N   . ASN C 2 28  ? -61.561 20.173  32.410  1.00 32.42  ? 28  ASN B N   1 
ATOM   5248  C CA  . ASN C 2 28  ? -62.861 19.835  31.840  1.00 30.80  ? 28  ASN B CA  1 
ATOM   5249  C C   . ASN C 2 28  ? -63.972 20.339  32.758  1.00 30.94  ? 28  ASN B C   1 
ATOM   5250  O O   . ASN C 2 28  ? -63.696 21.096  33.685  1.00 29.94  ? 28  ASN B O   1 
ATOM   5251  C CB  . ASN C 2 28  ? -62.958 18.323  31.558  1.00 29.22  ? 28  ASN B CB  1 
ATOM   5252  C CG  . ASN C 2 28  ? -62.690 17.454  32.781  1.00 29.22  ? 28  ASN B CG  1 
ATOM   5253  O OD1 . ASN C 2 28  ? -62.469 16.245  32.647  1.00 31.45  ? 28  ASN B OD1 1 
ATOM   5254  N ND2 . ASN C 2 28  ? -62.708 18.051  33.972  1.00 25.82  ? 28  ASN B ND2 1 
ATOM   5255  N N   . GLU C 2 29  ? -65.216 19.937  32.506  1.00 36.16  ? 29  GLU B N   1 
ATOM   5256  C CA  . GLU C 2 29  ? -66.350 20.390  33.324  1.00 41.59  ? 29  GLU B CA  1 
ATOM   5257  C C   . GLU C 2 29  ? -66.250 19.946  34.792  1.00 36.50  ? 29  GLU B C   1 
ATOM   5258  O O   . GLU C 2 29  ? -66.675 20.671  35.689  1.00 32.49  ? 29  GLU B O   1 
ATOM   5259  C CB  . GLU C 2 29  ? -67.681 19.923  32.717  1.00 48.52  ? 29  GLU B CB  1 
ATOM   5260  C CG  . GLU C 2 29  ? -68.096 20.704  31.479  1.00 57.66  ? 29  GLU B CG  1 
ATOM   5261  C CD  . GLU C 2 29  ? -69.371 20.172  30.842  1.00 71.20  ? 29  GLU B CD  1 
ATOM   5262  O OE1 . GLU C 2 29  ? -69.325 19.752  29.662  1.00 70.71  ? 29  GLU B OE1 1 
ATOM   5263  O OE2 . GLU C 2 29  ? -70.424 20.173  31.520  1.00 79.78  ? 29  GLU B OE2 1 
ATOM   5264  N N   . GLN C 2 30  ? -65.685 18.762  35.021  1.00 34.63  ? 30  GLN B N   1 
ATOM   5265  C CA  . GLN C 2 30  ? -65.504 18.229  36.373  1.00 34.22  ? 30  GLN B CA  1 
ATOM   5266  C C   . GLN C 2 30  ? -64.434 18.973  37.180  1.00 33.80  ? 30  GLN B C   1 
ATOM   5267  O O   . GLN C 2 30  ? -64.435 18.906  38.407  1.00 37.29  ? 30  GLN B O   1 
ATOM   5268  C CB  . GLN C 2 30  ? -65.144 16.743  36.322  1.00 33.60  ? 30  GLN B CB  1 
ATOM   5269  C CG  . GLN C 2 30  ? -66.223 15.867  35.704  1.00 34.19  ? 30  GLN B CG  1 
ATOM   5270  C CD  . GLN C 2 30  ? -65.651 14.647  34.989  1.00 37.35  ? 30  GLN B CD  1 
ATOM   5271  O OE1 . GLN C 2 30  ? -65.732 13.509  35.456  1.00 36.96  ? 30  GLN B OE1 1 
ATOM   5272  N NE2 . GLN C 2 30  ? -65.055 14.898  33.832  1.00 39.87  ? 30  GLN B NE2 1 
ATOM   5273  N N   . GLY C 2 31  ? -63.526 19.671  36.500  1.00 30.97  ? 31  GLY B N   1 
ATOM   5274  C CA  . GLY C 2 31  ? -62.437 20.384  37.166  1.00 29.25  ? 31  GLY B CA  1 
ATOM   5275  C C   . GLY C 2 31  ? -61.130 20.292  36.402  1.00 29.34  ? 31  GLY B C   1 
ATOM   5276  O O   . GLY C 2 31  ? -61.121 20.051  35.193  1.00 26.44  ? 31  GLY B O   1 
ATOM   5277  N N   . SER C 2 32  ? -60.022 20.479  37.117  1.00 31.28  ? 32  SER B N   1 
ATOM   5278  C CA  . SER C 2 32  ? -58.689 20.490  36.508  1.00 32.03  ? 32  SER B CA  1 
ATOM   5279  C C   . SER C 2 32  ? -57.633 19.947  37.458  1.00 32.95  ? 32  SER B C   1 
ATOM   5280  O O   . SER C 2 32  ? -57.837 19.924  38.669  1.00 32.58  ? 32  SER B O   1 
ATOM   5281  C CB  . SER C 2 32  ? -58.310 21.915  36.100  1.00 31.75  ? 32  SER B CB  1 
ATOM   5282  O OG  . SER C 2 32  ? -58.119 22.741  37.235  1.00 29.89  ? 32  SER B OG  1 
ATOM   5283  N N   . GLY C 2 33  ? -56.501 19.518  36.906  1.00 32.86  ? 33  GLY B N   1 
ATOM   5284  C CA  . GLY C 2 33  ? -55.406 19.027  37.729  1.00 30.40  ? 33  GLY B CA  1 
ATOM   5285  C C   . GLY C 2 33  ? -54.211 18.501  36.956  1.00 29.01  ? 33  GLY B C   1 
ATOM   5286  O O   . GLY C 2 33  ? -54.278 18.282  35.746  1.00 29.54  ? 33  GLY B O   1 
ATOM   5287  N N   . TYR C 2 34  ? -53.111 18.306  37.676  1.00 28.28  ? 34  TYR B N   1 
ATOM   5288  C CA  . TYR C 2 34  ? -51.882 17.772  37.110  1.00 28.42  ? 34  TYR B CA  1 
ATOM   5289  C C   . TYR C 2 34  ? -51.764 16.276  37.375  1.00 26.77  ? 34  TYR B C   1 
ATOM   5290  O O   . TYR C 2 34  ? -52.284 15.770  38.366  1.00 27.53  ? 34  TYR B O   1 
ATOM   5291  C CB  . TYR C 2 34  ? -50.674 18.485  37.711  1.00 30.11  ? 34  TYR B CB  1 
ATOM   5292  C CG  . TYR C 2 34  ? -50.638 19.973  37.459  1.00 32.34  ? 34  TYR B CG  1 
ATOM   5293  C CD1 . TYR C 2 34  ? -51.132 20.868  38.401  1.00 31.81  ? 34  TYR B CD1 1 
ATOM   5294  C CD2 . TYR C 2 34  ? -50.095 20.490  36.281  1.00 32.51  ? 34  TYR B CD2 1 
ATOM   5295  C CE1 . TYR C 2 34  ? -51.092 22.233  38.180  1.00 33.32  ? 34  TYR B CE1 1 
ATOM   5296  C CE2 . TYR C 2 34  ? -50.055 21.856  36.049  1.00 33.66  ? 34  TYR B CE2 1 
ATOM   5297  C CZ  . TYR C 2 34  ? -50.555 22.722  37.004  1.00 34.01  ? 34  TYR B CZ  1 
ATOM   5298  O OH  . TYR C 2 34  ? -50.518 24.077  36.793  1.00 34.53  ? 34  TYR B OH  1 
ATOM   5299  N N   . ALA C 2 35  ? -51.076 15.576  36.481  1.00 27.61  ? 35  ALA B N   1 
ATOM   5300  C CA  . ALA C 2 35  ? -50.769 14.162  36.667  1.00 28.45  ? 35  ALA B CA  1 
ATOM   5301  C C   . ALA C 2 35  ? -49.423 13.859  36.027  1.00 32.25  ? 35  ALA B C   1 
ATOM   5302  O O   . ALA C 2 35  ? -49.238 14.094  34.833  1.00 37.21  ? 35  ALA B O   1 
ATOM   5303  C CB  . ALA C 2 35  ? -51.849 13.301  36.047  1.00 27.12  ? 35  ALA B CB  1 
ATOM   5304  N N   . ALA C 2 36  ? -48.490 13.336  36.818  1.00 33.34  ? 36  ALA B N   1 
ATOM   5305  C CA  . ALA C 2 36  ? -47.149 13.023  36.333  1.00 35.94  ? 36  ALA B CA  1 
ATOM   5306  C C   . ALA C 2 36  ? -47.132 11.678  35.613  1.00 36.57  ? 36  ALA B C   1 
ATOM   5307  O O   . ALA C 2 36  ? -47.803 10.735  36.044  1.00 37.73  ? 36  ALA B O   1 
ATOM   5308  C CB  . ALA C 2 36  ? -46.161 13.011  37.491  1.00 33.89  ? 36  ALA B CB  1 
ATOM   5309  N N   . ASP C 2 37  ? -46.372 11.597  34.519  1.00 34.22  ? 37  ASP B N   1 
ATOM   5310  C CA  . ASP C 2 37  ? -46.089 10.313  33.872  1.00 36.91  ? 37  ASP B CA  1 
ATOM   5311  C C   . ASP C 2 37  ? -44.923 9.652   34.602  1.00 39.56  ? 37  ASP B C   1 
ATOM   5312  O O   . ASP C 2 37  ? -43.777 10.085  34.470  1.00 37.75  ? 37  ASP B O   1 
ATOM   5313  C CB  . ASP C 2 37  ? -45.747 10.496  32.391  1.00 37.32  ? 37  ASP B CB  1 
ATOM   5314  C CG  . ASP C 2 37  ? -45.484 9.164   31.674  1.00 39.99  ? 37  ASP B CG  1 
ATOM   5315  O OD1 . ASP C 2 37  ? -46.075 8.126   32.043  1.00 48.85  ? 37  ASP B OD1 1 
ATOM   5316  O OD2 . ASP C 2 37  ? -44.662 9.140   30.737  1.00 44.49  ? 37  ASP B OD2 1 
ATOM   5317  N N   . LYS C 2 38  ? -45.223 8.602   35.363  1.00 40.44  ? 38  LYS B N   1 
ATOM   5318  C CA  . LYS C 2 38  ? -44.245 7.996   36.264  1.00 41.12  ? 38  LYS B CA  1 
ATOM   5319  C C   . LYS C 2 38  ? -43.172 7.189   35.535  1.00 38.28  ? 38  LYS B C   1 
ATOM   5320  O O   . LYS C 2 38  ? -42.033 7.118   35.996  1.00 36.23  ? 38  LYS B O   1 
ATOM   5321  C CB  . LYS C 2 38  ? -44.951 7.100   37.290  1.00 46.23  ? 38  LYS B CB  1 
ATOM   5322  C CG  . LYS C 2 38  ? -45.962 7.796   38.172  1.00 52.31  ? 38  LYS B CG  1 
ATOM   5323  C CD  . LYS C 2 38  ? -45.242 8.502   39.298  1.00 58.16  ? 38  LYS B CD  1 
ATOM   5324  C CE  . LYS C 2 38  ? -46.218 9.328   40.115  1.00 61.68  ? 38  LYS B CE  1 
ATOM   5325  N NZ  . LYS C 2 38  ? -45.541 10.135  41.169  1.00 61.40  ? 38  LYS B NZ  1 
ATOM   5326  N N   . GLU C 2 39  ? -43.537 6.583   34.409  1.00 37.54  ? 39  GLU B N   1 
ATOM   5327  C CA  . GLU C 2 39  ? -42.607 5.770   33.627  1.00 39.79  ? 39  GLU B CA  1 
ATOM   5328  C C   . GLU C 2 39  ? -41.438 6.599   33.100  1.00 35.33  ? 39  GLU B C   1 
ATOM   5329  O O   . GLU C 2 39  ? -40.275 6.339   33.434  1.00 33.98  ? 39  GLU B O   1 
ATOM   5330  C CB  . GLU C 2 39  ? -43.356 5.078   32.456  1.00 46.48  ? 39  GLU B CB  1 
ATOM   5331  C CG  . GLU C 2 39  ? -43.477 3.558   32.577  1.00 54.43  ? 39  GLU B CG  1 
ATOM   5332  C CD  . GLU C 2 39  ? -42.258 2.858   32.032  1.00 59.98  ? 39  GLU B CD  1 
ATOM   5333  O OE1 . GLU C 2 39  ? -41.156 3.447   32.132  1.00 64.75  ? 39  GLU B OE1 1 
ATOM   5334  O OE2 . GLU C 2 39  ? -42.408 1.733   31.507  1.00 59.18  ? 39  GLU B OE2 1 
ATOM   5335  N N   . SER C 2 40  ? -41.755 7.599   32.286  1.00 32.13  ? 40  SER B N   1 
ATOM   5336  C CA  . SER C 2 40  ? -40.728 8.422   31.658  1.00 32.06  ? 40  SER B CA  1 
ATOM   5337  C C   . SER C 2 40  ? -39.950 9.262   32.670  1.00 32.08  ? 40  SER B C   1 
ATOM   5338  O O   . SER C 2 40  ? -38.765 9.532   32.467  1.00 33.60  ? 40  SER B O   1 
ATOM   5339  C CB  . SER C 2 40  ? -41.337 9.309   30.568  1.00 31.45  ? 40  SER B CB  1 
ATOM   5340  O OG  . SER C 2 40  ? -42.236 10.252  31.111  1.00 33.85  ? 40  SER B OG  1 
ATOM   5341  N N   . THR C 2 41  ? -40.609 9.670   33.753  1.00 30.85  ? 41  THR B N   1 
ATOM   5342  C CA  . THR C 2 41  ? -39.938 10.393  34.832  1.00 30.86  ? 41  THR B CA  1 
ATOM   5343  C C   . THR C 2 41  ? -38.845 9.540   35.471  1.00 31.78  ? 41  THR B C   1 
ATOM   5344  O O   . THR C 2 41  ? -37.719 10.006  35.654  1.00 34.53  ? 41  THR B O   1 
ATOM   5345  C CB  . THR C 2 41  ? -40.930 10.841  35.932  1.00 30.59  ? 41  THR B CB  1 
ATOM   5346  O OG1 . THR C 2 41  ? -41.793 11.862  35.418  1.00 32.51  ? 41  THR B OG1 1 
ATOM   5347  C CG2 . THR C 2 41  ? -40.193 11.379  37.148  1.00 28.54  ? 41  THR B CG2 1 
ATOM   5348  N N   . GLN C 2 42  ? -39.184 8.303   35.818  1.00 31.33  ? 42  GLN B N   1 
ATOM   5349  C CA  . GLN C 2 42  ? -38.233 7.416   36.489  1.00 31.71  ? 42  GLN B CA  1 
ATOM   5350  C C   . GLN C 2 42  ? -37.047 7.069   35.608  1.00 31.17  ? 42  GLN B C   1 
ATOM   5351  O O   . GLN C 2 42  ? -35.925 6.981   36.098  1.00 33.66  ? 42  GLN B O   1 
ATOM   5352  C CB  . GLN C 2 42  ? -38.905 6.128   36.983  1.00 31.86  ? 42  GLN B CB  1 
ATOM   5353  C CG  . GLN C 2 42  ? -39.310 6.180   38.447  1.00 33.47  ? 42  GLN B CG  1 
ATOM   5354  C CD  . GLN C 2 42  ? -38.125 6.424   39.362  1.00 34.15  ? 42  GLN B CD  1 
ATOM   5355  O OE1 . GLN C 2 42  ? -37.049 5.861   39.166  1.00 35.29  ? 42  GLN B OE1 1 
ATOM   5356  N NE2 . GLN C 2 42  ? -38.313 7.280   40.361  1.00 35.65  ? 42  GLN B NE2 1 
ATOM   5357  N N   . LYS C 2 43  ? -37.293 6.869   34.318  1.00 30.70  ? 43  LYS B N   1 
ATOM   5358  C CA  . LYS C 2 43  ? -36.213 6.595   33.377  1.00 31.56  ? 43  LYS B CA  1 
ATOM   5359  C C   . LYS C 2 43  ? -35.263 7.784   33.306  1.00 27.43  ? 43  LYS B C   1 
ATOM   5360  O O   . LYS C 2 43  ? -34.044 7.610   33.288  1.00 24.93  ? 43  LYS B O   1 
ATOM   5361  C CB  . LYS C 2 43  ? -36.787 6.275   31.992  1.00 36.96  ? 43  LYS B CB  1 
ATOM   5362  C CG  . LYS C 2 43  ? -37.461 4.884   31.912  1.00 46.77  ? 43  LYS B CG  1 
ATOM   5363  C CD  . LYS C 2 43  ? -36.564 3.842   31.266  1.00 53.02  ? 43  LYS B CD  1 
ATOM   5364  C CE  . LYS C 2 43  ? -37.332 2.532   31.071  1.00 55.77  ? 43  LYS B CE  1 
ATOM   5365  N NZ  . LYS C 2 43  ? -38.070 2.523   29.778  1.00 58.95  ? 43  LYS B NZ  1 
ATOM   5366  N N   . ALA C 2 44  ? -35.829 8.988   33.299  1.00 25.27  ? 44  ALA B N   1 
ATOM   5367  C CA  . ALA C 2 44  ? -35.045 10.209  33.211  1.00 24.63  ? 44  ALA B CA  1 
ATOM   5368  C C   . ALA C 2 44  ? -34.214 10.450  34.471  1.00 24.98  ? 44  ALA B C   1 
ATOM   5369  O O   . ALA C 2 44  ? -33.046 10.836  34.381  1.00 26.22  ? 44  ALA B O   1 
ATOM   5370  C CB  . ALA C 2 44  ? -35.949 11.396  32.924  1.00 25.72  ? 44  ALA B CB  1 
ATOM   5371  N N   . ILE C 2 45  ? -34.813 10.219  35.637  1.00 24.87  ? 45  ILE B N   1 
ATOM   5372  C CA  . ILE C 2 45  ? -34.095 10.341  36.908  1.00 25.16  ? 45  ILE B CA  1 
ATOM   5373  C C   . ILE C 2 45  ? -32.965 9.316   37.001  1.00 25.97  ? 45  ILE B C   1 
ATOM   5374  O O   . ILE C 2 45  ? -31.860 9.643   37.440  1.00 24.58  ? 45  ILE B O   1 
ATOM   5375  C CB  . ILE C 2 45  ? -35.042 10.184  38.117  1.00 24.54  ? 45  ILE B CB  1 
ATOM   5376  C CG1 . ILE C 2 45  ? -35.957 11.404  38.226  1.00 26.21  ? 45  ILE B CG1 1 
ATOM   5377  C CG2 . ILE C 2 45  ? -34.256 10.038  39.413  1.00 20.55  ? 45  ILE B CG2 1 
ATOM   5378  C CD1 . ILE C 2 45  ? -37.024 11.265  39.294  1.00 25.50  ? 45  ILE B CD1 1 
ATOM   5379  N N   . ASP C 2 46  ? -33.248 8.084   36.583  1.00 26.51  ? 46  ASP B N   1 
ATOM   5380  C CA  . ASP C 2 46  ? -32.245 7.022   36.588  1.00 26.89  ? 46  ASP B CA  1 
ATOM   5381  C C   . ASP C 2 46  ? -31.086 7.325   35.641  1.00 25.71  ? 46  ASP B C   1 
ATOM   5382  O O   . ASP C 2 46  ? -29.932 7.111   35.991  1.00 25.36  ? 46  ASP B O   1 
ATOM   5383  C CB  . ASP C 2 46  ? -32.875 5.677   36.219  1.00 28.85  ? 46  ASP B CB  1 
ATOM   5384  C CG  . ASP C 2 46  ? -33.755 5.115   37.325  1.00 33.57  ? 46  ASP B CG  1 
ATOM   5385  O OD1 . ASP C 2 46  ? -33.771 5.687   38.438  1.00 35.60  ? 46  ASP B OD1 1 
ATOM   5386  O OD2 . ASP C 2 46  ? -34.437 4.092   37.078  1.00 35.45  ? 46  ASP B OD2 1 
ATOM   5387  N N   . GLY C 2 47  ? -31.396 7.826   34.449  1.00 24.37  ? 47  GLY B N   1 
ATOM   5388  C CA  . GLY C 2 47  ? -30.370 8.174   33.469  1.00 22.86  ? 47  GLY B CA  1 
ATOM   5389  C C   . GLY C 2 47  ? -29.474 9.301   33.937  1.00 21.06  ? 47  GLY B C   1 
ATOM   5390  O O   . GLY C 2 47  ? -28.252 9.207   33.867  1.00 19.94  ? 47  GLY B O   1 
ATOM   5391  N N   . VAL C 2 48  ? -30.089 10.371  34.423  1.00 21.62  ? 48  VAL B N   1 
ATOM   5392  C CA  . VAL C 2 48  ? -29.353 11.542  34.883  1.00 21.87  ? 48  VAL B CA  1 
ATOM   5393  C C   . VAL C 2 48  ? -28.483 11.219  36.100  1.00 20.05  ? 48  VAL B C   1 
ATOM   5394  O O   . VAL C 2 48  ? -27.348 11.679  36.188  1.00 20.43  ? 48  VAL B O   1 
ATOM   5395  C CB  . VAL C 2 48  ? -30.329 12.704  35.179  1.00 24.60  ? 48  VAL B CB  1 
ATOM   5396  C CG1 . VAL C 2 48  ? -29.657 13.794  36.007  1.00 27.12  ? 48  VAL B CG1 1 
ATOM   5397  C CG2 . VAL C 2 48  ? -30.862 13.264  33.870  1.00 23.68  ? 48  VAL B CG2 1 
ATOM   5398  N N   . THR C 2 49  ? -29.009 10.417  37.025  1.00 19.30  ? 49  THR B N   1 
ATOM   5399  C CA  . THR C 2 49  ? -28.236 9.972   38.183  1.00 18.37  ? 49  THR B CA  1 
ATOM   5400  C C   . THR C 2 49  ? -27.056 9.115   37.746  1.00 18.22  ? 49  THR B C   1 
ATOM   5401  O O   . THR C 2 49  ? -25.963 9.226   38.297  1.00 17.21  ? 49  THR B O   1 
ATOM   5402  C CB  . THR C 2 49  ? -29.109 9.177   39.176  1.00 18.29  ? 49  THR B CB  1 
ATOM   5403  O OG1 . THR C 2 49  ? -30.201 9.997   39.602  1.00 19.38  ? 49  THR B OG1 1 
ATOM   5404  C CG2 . THR C 2 49  ? -28.306 8.738   40.393  1.00 15.97  ? 49  THR B CG2 1 
ATOM   5405  N N   . ASN C 2 50  ? -27.287 8.263   36.753  1.00 19.96  ? 50  ASN B N   1 
ATOM   5406  C CA  . ASN C 2 50  ? -26.238 7.425   36.195  1.00 22.17  ? 50  ASN B CA  1 
ATOM   5407  C C   . ASN C 2 50  ? -25.149 8.269   35.531  1.00 20.73  ? 50  ASN B C   1 
ATOM   5408  O O   . ASN C 2 50  ? -23.968 7.966   35.655  1.00 19.85  ? 50  ASN B O   1 
ATOM   5409  C CB  . ASN C 2 50  ? -26.827 6.433   35.185  1.00 26.50  ? 50  ASN B CB  1 
ATOM   5410  C CG  . ASN C 2 50  ? -26.362 5.019   35.422  1.00 32.42  ? 50  ASN B CG  1 
ATOM   5411  O OD1 . ASN C 2 50  ? -25.540 4.492   34.677  1.00 41.69  ? 50  ASN B OD1 1 
ATOM   5412  N ND2 . ASN C 2 50  ? -26.886 4.395   36.474  1.00 32.38  ? 50  ASN B ND2 1 
ATOM   5413  N N   . LYS C 2 51  ? -25.555 9.331   34.836  1.00 21.07  ? 51  LYS B N   1 
ATOM   5414  C CA  . LYS C 2 51  ? -24.610 10.254  34.201  1.00 22.72  ? 51  LYS B CA  1 
ATOM   5415  C C   . LYS C 2 51  ? -23.687 10.886  35.228  1.00 20.66  ? 51  LYS B C   1 
ATOM   5416  O O   . LYS C 2 51  ? -22.474 10.864  35.070  1.00 20.14  ? 51  LYS B O   1 
ATOM   5417  C CB  . LYS C 2 51  ? -25.356 11.356  33.438  1.00 25.87  ? 51  LYS B CB  1 
ATOM   5418  C CG  . LYS C 2 51  ? -24.450 12.439  32.863  1.00 29.22  ? 51  LYS B CG  1 
ATOM   5419  C CD  . LYS C 2 51  ? -25.223 13.513  32.112  1.00 32.01  ? 51  LYS B CD  1 
ATOM   5420  C CE  . LYS C 2 51  ? -25.835 12.986  30.822  1.00 34.63  ? 51  LYS B CE  1 
ATOM   5421  N NZ  . LYS C 2 51  ? -26.144 14.046  29.821  1.00 35.33  ? 51  LYS B NZ  1 
ATOM   5422  N N   . VAL C 2 52  ? -24.272 11.450  36.278  1.00 19.92  ? 52  VAL B N   1 
ATOM   5423  C CA  . VAL C 2 52  ? -23.497 12.074  37.342  1.00 19.35  ? 52  VAL B CA  1 
ATOM   5424  C C   . VAL C 2 52  ? -22.572 11.063  38.011  1.00 19.30  ? 52  VAL B C   1 
ATOM   5425  O O   . VAL C 2 52  ? -21.416 11.374  38.297  1.00 19.59  ? 52  VAL B O   1 
ATOM   5426  C CB  . VAL C 2 52  ? -24.409 12.703  38.413  1.00 20.33  ? 52  VAL B CB  1 
ATOM   5427  C CG1 . VAL C 2 52  ? -23.578 13.269  39.562  1.00 18.48  ? 52  VAL B CG1 1 
ATOM   5428  C CG2 . VAL C 2 52  ? -25.288 13.773  37.786  1.00 20.71  ? 52  VAL B CG2 1 
ATOM   5429  N N   . ASN C 2 53  ? -23.080 9.855   38.255  1.00 18.40  ? 53  ASN B N   1 
ATOM   5430  C CA  . ASN C 2 53  ? -22.288 8.817   38.915  1.00 17.79  ? 53  ASN B CA  1 
ATOM   5431  C C   . ASN C 2 53  ? -21.120 8.324   38.079  1.00 16.46  ? 53  ASN B C   1 
ATOM   5432  O O   . ASN C 2 53  ? -20.032 8.138   38.605  1.00 17.63  ? 53  ASN B O   1 
ATOM   5433  C CB  . ASN C 2 53  ? -23.166 7.640   39.348  1.00 18.45  ? 53  ASN B CB  1 
ATOM   5434  C CG  . ASN C 2 53  ? -23.960 7.945   40.604  1.00 18.95  ? 53  ASN B CG  1 
ATOM   5435  O OD1 . ASN C 2 53  ? -23.531 8.737   41.442  1.00 19.31  ? 53  ASN B OD1 1 
ATOM   5436  N ND2 . ASN C 2 53  ? -25.124 7.322   40.737  1.00 18.56  ? 53  ASN B ND2 1 
ATOM   5437  N N   . SER C 2 54  ? -21.328 8.117   36.785  1.00 14.64  ? 54  SER B N   1 
ATOM   5438  C CA  . SER C 2 54  ? -20.241 7.670   35.935  1.00 14.73  ? 54  SER B CA  1 
ATOM   5439  C C   . SER C 2 54  ? -19.134 8.720   35.860  1.00 14.26  ? 54  SER B C   1 
ATOM   5440  O O   . SER C 2 54  ? -17.953 8.384   35.919  1.00 13.90  ? 54  SER B O   1 
ATOM   5441  C CB  . SER C 2 54  ? -20.747 7.331   34.538  1.00 15.39  ? 54  SER B CB  1 
ATOM   5442  O OG  . SER C 2 54  ? -22.108 6.959   34.543  1.00 15.95  ? 54  SER B OG  1 
ATOM   5443  N N   . ILE C 2 55  ? -19.521 9.989   35.756  1.00 14.47  ? 55  ILE B N   1 
ATOM   5444  C CA  . ILE C 2 55  ? -18.555 11.098  35.719  1.00 14.83  ? 55  ILE B CA  1 
ATOM   5445  C C   . ILE C 2 55  ? -17.711 11.177  36.996  1.00 14.15  ? 55  ILE B C   1 
ATOM   5446  O O   . ILE C 2 55  ? -16.567 11.622  36.959  1.00 14.26  ? 55  ILE B O   1 
ATOM   5447  C CB  . ILE C 2 55  ? -19.260 12.444  35.466  1.00 15.57  ? 55  ILE B CB  1 
ATOM   5448  C CG1 . ILE C 2 55  ? -19.782 12.508  34.031  1.00 16.21  ? 55  ILE B CG1 1 
ATOM   5449  C CG2 . ILE C 2 55  ? -18.306 13.606  35.692  1.00 16.48  ? 55  ILE B CG2 1 
ATOM   5450  C CD1 . ILE C 2 55  ? -20.694 13.684  33.768  1.00 17.02  ? 55  ILE B CD1 1 
ATOM   5451  N N   . ILE C 2 56  ? -18.280 10.738  38.116  1.00 14.75  ? 56  ILE B N   1 
ATOM   5452  C CA  . ILE C 2 56  ? -17.568 10.661  39.393  1.00 14.52  ? 56  ILE B CA  1 
ATOM   5453  C C   . ILE C 2 56  ? -16.795 9.352   39.510  1.00 15.56  ? 56  ILE B C   1 
ATOM   5454  O O   . ILE C 2 56  ? -15.607 9.358   39.842  1.00 17.49  ? 56  ILE B O   1 
ATOM   5455  C CB  . ILE C 2 56  ? -18.556 10.773  40.576  1.00 14.68  ? 56  ILE B CB  1 
ATOM   5456  C CG1 . ILE C 2 56  ? -19.179 12.170  40.612  1.00 14.95  ? 56  ILE B CG1 1 
ATOM   5457  C CG2 . ILE C 2 56  ? -17.889 10.456  41.905  1.00 13.52  ? 56  ILE B CG2 1 
ATOM   5458  C CD1 . ILE C 2 56  ? -20.338 12.293  41.581  1.00 14.33  ? 56  ILE B CD1 1 
ATOM   5459  N N   . ASP C 2 57  ? -17.463 8.235   39.224  1.00 17.03  ? 57  ASP B N   1 
ATOM   5460  C CA  . ASP C 2 57  ? -16.909 6.897   39.484  1.00 19.18  ? 57  ASP B CA  1 
ATOM   5461  C C   . ASP C 2 57  ? -15.746 6.497   38.570  1.00 18.96  ? 57  ASP B C   1 
ATOM   5462  O O   . ASP C 2 57  ? -14.869 5.753   38.992  1.00 17.79  ? 57  ASP B O   1 
ATOM   5463  C CB  . ASP C 2 57  ? -18.009 5.829   39.399  1.00 22.31  ? 57  ASP B CB  1 
ATOM   5464  C CG  . ASP C 2 57  ? -19.059 5.962   40.509  1.00 26.34  ? 57  ASP B CG  1 
ATOM   5465  O OD1 . ASP C 2 57  ? -18.870 6.777   41.437  1.00 29.48  ? 57  ASP B OD1 1 
ATOM   5466  O OD2 . ASP C 2 57  ? -20.083 5.248   40.449  1.00 26.75  ? 57  ASP B OD2 1 
ATOM   5467  N N   . LYS C 2 58  ? -15.734 6.985   37.331  1.00 19.35  ? 58  LYS B N   1 
ATOM   5468  C CA  . LYS C 2 58  ? -14.677 6.625   36.378  1.00 19.14  ? 58  LYS B CA  1 
ATOM   5469  C C   . LYS C 2 58  ? -13.320 7.255   36.687  1.00 20.39  ? 58  LYS B C   1 
ATOM   5470  O O   . LYS C 2 58  ? -12.306 6.846   36.114  1.00 20.06  ? 58  LYS B O   1 
ATOM   5471  C CB  . LYS C 2 58  ? -15.088 6.977   34.947  1.00 18.31  ? 58  LYS B CB  1 
ATOM   5472  C CG  . LYS C 2 58  ? -16.247 6.153   34.412  1.00 18.46  ? 58  LYS B CG  1 
ATOM   5473  C CD  . LYS C 2 58  ? -15.922 4.669   34.345  1.00 18.40  ? 58  LYS B CD  1 
ATOM   5474  C CE  . LYS C 2 58  ? -17.029 3.900   33.639  1.00 18.76  ? 58  LYS B CE  1 
ATOM   5475  N NZ  . LYS C 2 58  ? -16.738 2.447   33.473  1.00 18.45  ? 58  LYS B NZ  1 
ATOM   5476  N N   . MET C 2 59  ? -13.290 8.240   37.580  1.00 21.48  ? 59  MET B N   1 
ATOM   5477  C CA  . MET C 2 59  ? -12.020 8.814   38.009  1.00 23.49  ? 59  MET B CA  1 
ATOM   5478  C C   . MET C 2 59  ? -11.311 7.789   38.872  1.00 25.52  ? 59  MET B C   1 
ATOM   5479  O O   . MET C 2 59  ? -11.915 7.198   39.768  1.00 25.75  ? 59  MET B O   1 
ATOM   5480  C CB  . MET C 2 59  ? -12.231 10.109  38.798  1.00 22.84  ? 59  MET B CB  1 
ATOM   5481  C CG  . MET C 2 59  ? -10.947 10.816  39.218  1.00 20.54  ? 59  MET B CG  1 
ATOM   5482  S SD  . MET C 2 59  ? -9.898  11.349  37.845  1.00 19.03  ? 59  MET B SD  1 
ATOM   5483  C CE  . MET C 2 59  ? -10.906 12.630  37.108  1.00 19.27  ? 59  MET B CE  1 
ATOM   5484  N N   . ASN C 2 60  ? -10.031 7.577   38.587  1.00 31.19  ? 60  ASN B N   1 
ATOM   5485  C CA  . ASN C 2 60  ? -9.224  6.641   39.356  1.00 35.68  ? 60  ASN B CA  1 
ATOM   5486  C C   . ASN C 2 60  ? -8.009  7.394   39.861  1.00 37.76  ? 60  ASN B C   1 
ATOM   5487  O O   . ASN C 2 60  ? -7.138  7.779   39.083  1.00 43.71  ? 60  ASN B O   1 
ATOM   5488  C CB  . ASN C 2 60  ? -8.869  5.395   38.522  1.00 38.70  ? 60  ASN B CB  1 
ATOM   5489  C CG  . ASN C 2 60  ? -7.422  4.986   38.646  1.00 40.44  ? 60  ASN B CG  1 
ATOM   5490  O OD1 . ASN C 2 60  ? -7.048  4.291   39.581  1.00 40.73  ? 60  ASN B OD1 1 
ATOM   5491  N ND2 . ASN C 2 60  ? -6.599  5.410   37.691  1.00 40.82  ? 60  ASN B ND2 1 
ATOM   5492  N N   . THR C 2 61  ? -7.989  7.640   41.169  1.00 39.02  ? 61  THR B N   1 
ATOM   5493  C CA  . THR C 2 61  ? -6.938  8.426   41.794  1.00 43.13  ? 61  THR B CA  1 
ATOM   5494  C C   . THR C 2 61  ? -6.056  7.531   42.650  1.00 37.64  ? 61  THR B C   1 
ATOM   5495  O O   . THR C 2 61  ? -6.558  6.711   43.419  1.00 34.93  ? 61  THR B O   1 
ATOM   5496  C CB  . THR C 2 61  ? -7.537  9.528   42.681  1.00 46.02  ? 61  THR B CB  1 
ATOM   5497  O OG1 . THR C 2 61  ? -8.383  8.931   43.675  1.00 40.20  ? 61  THR B OG1 1 
ATOM   5498  C CG2 . THR C 2 61  ? -8.347  10.516  41.835  1.00 46.15  ? 61  THR B CG2 1 
ATOM   5499  N N   . GLN C 2 62  ? -4.746  7.693   42.498  1.00 36.67  ? 62  GLN B N   1 
ATOM   5500  C CA  . GLN C 2 62  ? -3.772  6.962   43.293  1.00 37.86  ? 62  GLN B CA  1 
ATOM   5501  C C   . GLN C 2 62  ? -3.173  7.842   44.378  1.00 33.57  ? 62  GLN B C   1 
ATOM   5502  O O   . GLN C 2 62  ? -3.397  9.053   44.412  1.00 30.78  ? 62  GLN B O   1 
ATOM   5503  C CB  . GLN C 2 62  ? -2.668  6.428   42.383  1.00 41.77  ? 62  GLN B CB  1 
ATOM   5504  C CG  . GLN C 2 62  ? -3.154  5.307   41.476  1.00 47.25  ? 62  GLN B CG  1 
ATOM   5505  C CD  . GLN C 2 62  ? -2.333  5.140   40.210  1.00 52.06  ? 62  GLN B CD  1 
ATOM   5506  O OE1 . GLN C 2 62  ? -1.752  6.096   39.697  1.00 47.95  ? 62  GLN B OE1 1 
ATOM   5507  N NE2 . GLN C 2 62  ? -2.303  3.915   39.687  1.00 59.52  ? 62  GLN B NE2 1 
ATOM   5508  N N   . PHE C 2 63  ? -2.417  7.214   45.271  1.00 31.17  ? 63  PHE B N   1 
ATOM   5509  C CA  . PHE C 2 63  ? -1.725  7.928   46.327  1.00 28.53  ? 63  PHE B CA  1 
ATOM   5510  C C   . PHE C 2 63  ? -0.572  8.712   45.716  1.00 27.51  ? 63  PHE B C   1 
ATOM   5511  O O   . PHE C 2 63  ? 0.063   8.236   44.783  1.00 25.85  ? 63  PHE B O   1 
ATOM   5512  C CB  . PHE C 2 63  ? -1.195  6.939   47.368  1.00 26.76  ? 63  PHE B CB  1 
ATOM   5513  C CG  . PHE C 2 63  ? -0.431  7.586   48.482  1.00 27.81  ? 63  PHE B CG  1 
ATOM   5514  C CD1 . PHE C 2 63  ? -1.086  8.029   49.620  1.00 29.42  ? 63  PHE B CD1 1 
ATOM   5515  C CD2 . PHE C 2 63  ? 0.944   7.760   48.391  1.00 27.67  ? 63  PHE B CD2 1 
ATOM   5516  C CE1 . PHE C 2 63  ? -0.385  8.632   50.649  1.00 31.66  ? 63  PHE B CE1 1 
ATOM   5517  C CE2 . PHE C 2 63  ? 1.651   8.361   49.416  1.00 29.45  ? 63  PHE B CE2 1 
ATOM   5518  C CZ  . PHE C 2 63  ? 0.986   8.800   50.546  1.00 30.79  ? 63  PHE B CZ  1 
ATOM   5519  N N   . GLU C 2 64  ? -0.304  9.903   46.244  1.00 28.78  ? 64  GLU B N   1 
ATOM   5520  C CA  . GLU C 2 64  ? 0.915   10.633  45.904  1.00 30.65  ? 64  GLU B CA  1 
ATOM   5521  C C   . GLU C 2 64  ? 1.255   11.722  46.889  1.00 30.22  ? 64  GLU B C   1 
ATOM   5522  O O   . GLU C 2 64  ? 0.390   12.237  47.592  1.00 33.87  ? 64  GLU B O   1 
ATOM   5523  C CB  . GLU C 2 64  ? 0.818   11.236  44.510  1.00 32.41  ? 64  GLU B CB  1 
ATOM   5524  C CG  . GLU C 2 64  ? 1.544   10.416  43.457  1.00 34.12  ? 64  GLU B CG  1 
ATOM   5525  C CD  . GLU C 2 64  ? 0.681   10.130  42.255  1.00 33.85  ? 64  GLU B CD  1 
ATOM   5526  O OE1 . GLU C 2 64  ? -0.070  11.033  41.827  1.00 43.64  ? 64  GLU B OE1 1 
ATOM   5527  O OE2 . GLU C 2 64  ? 0.761   8.998   41.740  1.00 27.83  ? 64  GLU B OE2 1 
ATOM   5528  N N   . ALA C 2 65  ? 2.533   12.072  46.910  1.00 29.66  ? 65  ALA B N   1 
ATOM   5529  C CA  . ALA C 2 65  ? 3.047   13.062  47.824  1.00 28.06  ? 65  ALA B CA  1 
ATOM   5530  C C   . ALA C 2 65  ? 3.609   14.209  47.005  1.00 24.96  ? 65  ALA B C   1 
ATOM   5531  O O   . ALA C 2 65  ? 4.809   14.274  46.755  1.00 27.26  ? 65  ALA B O   1 
ATOM   5532  C CB  . ALA C 2 65  ? 4.113   12.445  48.711  1.00 27.09  ? 65  ALA B CB  1 
ATOM   5533  N N   . VAL C 2 66  ? 2.727   15.102  46.569  1.00 24.62  ? 66  VAL B N   1 
ATOM   5534  C CA  . VAL C 2 66  ? 3.163   16.292  45.852  1.00 24.89  ? 66  VAL B CA  1 
ATOM   5535  C C   . VAL C 2 66  ? 3.734   17.269  46.869  1.00 27.60  ? 66  VAL B C   1 
ATOM   5536  O O   . VAL C 2 66  ? 2.998   17.940  47.589  1.00 30.41  ? 66  VAL B O   1 
ATOM   5537  C CB  . VAL C 2 66  ? 2.030   16.956  45.051  1.00 22.65  ? 66  VAL B CB  1 
ATOM   5538  C CG1 . VAL C 2 66  ? 2.544   18.204  44.349  1.00 21.40  ? 66  VAL B CG1 1 
ATOM   5539  C CG2 . VAL C 2 66  ? 1.461   15.976  44.043  1.00 19.84  ? 66  VAL B CG2 1 
ATOM   5540  N N   . GLY C 2 67  ? 5.058   17.296  46.949  1.00 31.28  ? 67  GLY B N   1 
ATOM   5541  C CA  . GLY C 2 67  ? 5.778   18.247  47.782  1.00 34.32  ? 67  GLY B CA  1 
ATOM   5542  C C   . GLY C 2 67  ? 7.124   18.540  47.147  1.00 39.66  ? 67  GLY B C   1 
ATOM   5543  O O   . GLY C 2 67  ? 7.798   17.633  46.666  1.00 56.53  ? 67  GLY B O   1 
ATOM   5544  N N   . ARG C 2 68  ? 7.513   19.809  47.135  1.00 37.57  ? 68  ARG B N   1 
ATOM   5545  C CA  . ARG C 2 68  ? 8.744   20.233  46.483  1.00 36.91  ? 68  ARG B CA  1 
ATOM   5546  C C   . ARG C 2 68  ? 9.977   20.027  47.357  1.00 31.36  ? 68  ARG B C   1 
ATOM   5547  O O   . ARG C 2 68  ? 10.148  20.711  48.359  1.00 32.44  ? 68  ARG B O   1 
ATOM   5548  C CB  . ARG C 2 68  ? 8.614   21.702  46.081  1.00 42.98  ? 68  ARG B CB  1 
ATOM   5549  C CG  . ARG C 2 68  ? 7.661   21.922  44.918  1.00 48.73  ? 68  ARG B CG  1 
ATOM   5550  C CD  . ARG C 2 68  ? 7.741   23.343  44.405  1.00 52.74  ? 68  ARG B CD  1 
ATOM   5551  N NE  . ARG C 2 68  ? 7.002   23.527  43.157  1.00 61.21  ? 68  ARG B NE  1 
ATOM   5552  C CZ  . ARG C 2 68  ? 5.676   23.550  43.047  1.00 57.28  ? 68  ARG B CZ  1 
ATOM   5553  N NH1 . ARG C 2 68  ? 4.902   23.388  44.106  1.00 60.82  ? 68  ARG B NH1 1 
ATOM   5554  N NH2 . ARG C 2 68  ? 5.118   23.734  41.857  1.00 64.78  ? 68  ARG B NH2 1 
ATOM   5555  N N   . GLU C 2 69  ? 10.844  19.101  46.952  1.00 29.15  ? 69  GLU B N   1 
ATOM   5556  C CA  . GLU C 2 69  ? 12.017  18.738  47.743  1.00 28.67  ? 69  GLU B CA  1 
ATOM   5557  C C   . GLU C 2 69  ? 13.323  18.775  46.932  1.00 26.78  ? 69  GLU B C   1 
ATOM   5558  O O   . GLU C 2 69  ? 14.199  17.928  47.093  1.00 26.53  ? 69  GLU B O   1 
ATOM   5559  C CB  . GLU C 2 69  ? 11.805  17.384  48.454  1.00 32.48  ? 69  GLU B CB  1 
ATOM   5560  C CG  . GLU C 2 69  ? 11.088  16.290  47.666  1.00 35.86  ? 69  GLU B CG  1 
ATOM   5561  C CD  . GLU C 2 69  ? 10.594  15.141  48.549  1.00 37.53  ? 69  GLU B CD  1 
ATOM   5562  O OE1 . GLU C 2 69  ? 9.655   14.432  48.125  1.00 38.62  ? 69  GLU B OE1 1 
ATOM   5563  O OE2 . GLU C 2 69  ? 11.133  14.939  49.664  1.00 34.36  ? 69  GLU B OE2 1 
ATOM   5564  N N   . PHE C 2 70  ? 13.458  19.795  46.088  1.00 24.80  ? 70  PHE B N   1 
ATOM   5565  C CA  . PHE C 2 70  ? 14.712  20.062  45.376  1.00 22.47  ? 70  PHE B CA  1 
ATOM   5566  C C   . PHE C 2 70  ? 15.391  21.335  45.883  1.00 21.95  ? 70  PHE B C   1 
ATOM   5567  O O   . PHE C 2 70  ? 14.725  22.329  46.176  1.00 22.31  ? 70  PHE B O   1 
ATOM   5568  C CB  . PHE C 2 70  ? 14.447  20.157  43.876  1.00 21.41  ? 70  PHE B CB  1 
ATOM   5569  C CG  . PHE C 2 70  ? 14.013  18.856  43.269  1.00 20.05  ? 70  PHE B CG  1 
ATOM   5570  C CD1 . PHE C 2 70  ? 12.723  18.688  42.790  1.00 18.55  ? 70  PHE B CD1 1 
ATOM   5571  C CD2 . PHE C 2 70  ? 14.891  17.782  43.218  1.00 18.75  ? 70  PHE B CD2 1 
ATOM   5572  C CE1 . PHE C 2 70  ? 12.323  17.478  42.250  1.00 17.42  ? 70  PHE B CE1 1 
ATOM   5573  C CE2 . PHE C 2 70  ? 14.497  16.569  42.685  1.00 18.15  ? 70  PHE B CE2 1 
ATOM   5574  C CZ  . PHE C 2 70  ? 13.209  16.417  42.201  1.00 17.74  ? 70  PHE B CZ  1 
ATOM   5575  N N   . ASN C 2 71  ? 16.719  21.296  45.976  1.00 21.30  ? 71  ASN B N   1 
ATOM   5576  C CA  . ASN C 2 71  ? 17.496  22.402  46.540  1.00 22.02  ? 71  ASN B CA  1 
ATOM   5577  C C   . ASN C 2 71  ? 17.824  23.462  45.491  1.00 23.89  ? 71  ASN B C   1 
ATOM   5578  O O   . ASN C 2 71  ? 17.456  23.321  44.316  1.00 23.58  ? 71  ASN B O   1 
ATOM   5579  C CB  . ASN C 2 71  ? 18.764  21.880  47.228  1.00 22.53  ? 71  ASN B CB  1 
ATOM   5580  C CG  . ASN C 2 71  ? 19.800  21.348  46.253  1.00 24.39  ? 71  ASN B CG  1 
ATOM   5581  O OD1 . ASN C 2 71  ? 20.156  22.005  45.274  1.00 28.08  ? 71  ASN B OD1 1 
ATOM   5582  N ND2 . ASN C 2 71  ? 20.312  20.160  46.536  1.00 23.91  ? 71  ASN B ND2 1 
ATOM   5583  N N   . ASN C 2 72  ? 18.519  24.518  45.919  1.00 26.35  ? 72  ASN B N   1 
ATOM   5584  C CA  . ASN C 2 72  ? 18.790  25.678  45.054  1.00 30.54  ? 72  ASN B CA  1 
ATOM   5585  C C   . ASN C 2 72  ? 19.755  25.405  43.892  1.00 27.93  ? 72  ASN B C   1 
ATOM   5586  O O   . ASN C 2 72  ? 19.862  26.225  42.989  1.00 27.35  ? 72  ASN B O   1 
ATOM   5587  C CB  . ASN C 2 72  ? 19.288  26.891  45.868  1.00 34.63  ? 72  ASN B CB  1 
ATOM   5588  C CG  . ASN C 2 72  ? 20.780  26.843  46.178  1.00 42.62  ? 72  ASN B CG  1 
ATOM   5589  O OD1 . ASN C 2 72  ? 21.431  25.792  46.116  1.00 51.46  ? 72  ASN B OD1 1 
ATOM   5590  N ND2 . ASN C 2 72  ? 21.335  28.005  46.508  1.00 45.49  ? 72  ASN B ND2 1 
ATOM   5591  N N   . LEU C 2 73  ? 20.476  24.285  43.934  1.00 26.19  ? 73  LEU B N   1 
ATOM   5592  C CA  . LEU C 2 73  ? 21.290  23.850  42.794  1.00 25.17  ? 73  LEU B CA  1 
ATOM   5593  C C   . LEU C 2 73  ? 20.620  22.702  42.021  1.00 24.21  ? 73  LEU B C   1 
ATOM   5594  O O   . LEU C 2 73  ? 21.291  21.947  41.321  1.00 26.12  ? 73  LEU B O   1 
ATOM   5595  C CB  . LEU C 2 73  ? 22.704  23.453  43.254  1.00 24.30  ? 73  LEU B CB  1 
ATOM   5596  C CG  . LEU C 2 73  ? 23.652  24.603  43.648  1.00 24.77  ? 73  LEU B CG  1 
ATOM   5597  C CD1 . LEU C 2 73  ? 24.923  24.068  44.289  1.00 22.56  ? 73  LEU B CD1 1 
ATOM   5598  C CD2 . LEU C 2 73  ? 24.010  25.492  42.464  1.00 24.31  ? 73  LEU B CD2 1 
ATOM   5599  N N   . GLU C 2 74  ? 19.300  22.589  42.140  1.00 23.06  ? 74  GLU B N   1 
ATOM   5600  C CA  . GLU C 2 74  ? 18.528  21.568  41.430  1.00 23.77  ? 74  GLU B CA  1 
ATOM   5601  C C   . GLU C 2 74  ? 17.287  22.195  40.781  1.00 23.13  ? 74  GLU B C   1 
ATOM   5602  O O   . GLU C 2 74  ? 16.238  21.561  40.679  1.00 21.87  ? 74  GLU B O   1 
ATOM   5603  C CB  . GLU C 2 74  ? 18.110  20.455  42.400  1.00 24.85  ? 74  GLU B CB  1 
ATOM   5604  C CG  . GLU C 2 74  ? 19.259  19.606  42.939  1.00 25.88  ? 74  GLU B CG  1 
ATOM   5605  C CD  . GLU C 2 74  ? 18.828  18.639  44.040  1.00 28.35  ? 74  GLU B CD  1 
ATOM   5606  O OE1 . GLU C 2 74  ? 17.971  19.004  44.873  1.00 27.02  ? 74  GLU B OE1 1 
ATOM   5607  O OE2 . GLU C 2 74  ? 19.353  17.506  44.086  1.00 31.79  ? 74  GLU B OE2 1 
ATOM   5608  N N   . ARG C 2 75  ? 17.424  23.431  40.310  1.00 23.76  ? 75  ARG B N   1 
ATOM   5609  C CA  . ARG C 2 75  ? 16.277  24.195  39.818  1.00 24.20  ? 75  ARG B CA  1 
ATOM   5610  C C   . ARG C 2 75  ? 15.811  23.743  38.440  1.00 21.11  ? 75  ARG B C   1 
ATOM   5611  O O   . ARG C 2 75  ? 14.647  23.926  38.087  1.00 21.63  ? 75  ARG B O   1 
ATOM   5612  C CB  . ARG C 2 75  ? 16.574  25.694  39.796  1.00 28.06  ? 75  ARG B CB  1 
ATOM   5613  C CG  . ARG C 2 75  ? 16.786  26.323  41.152  1.00 32.21  ? 75  ARG B CG  1 
ATOM   5614  C CD  . ARG C 2 75  ? 15.487  26.565  41.898  1.00 40.17  ? 75  ARG B CD  1 
ATOM   5615  N NE  . ARG C 2 75  ? 15.748  26.787  43.320  1.00 48.45  ? 75  ARG B NE  1 
ATOM   5616  C CZ  . ARG C 2 75  ? 14.969  26.396  44.329  1.00 53.20  ? 75  ARG B CZ  1 
ATOM   5617  N NH1 . ARG C 2 75  ? 13.846  25.717  44.111  1.00 54.43  ? 75  ARG B NH1 1 
ATOM   5618  N NH2 . ARG C 2 75  ? 15.332  26.675  45.580  1.00 52.90  ? 75  ARG B NH2 1 
ATOM   5619  N N   . ARG C 2 76  ? 16.709  23.159  37.658  1.00 19.74  ? 76  ARG B N   1 
ATOM   5620  C CA  . ARG C 2 76  ? 16.321  22.574  36.370  1.00 18.15  ? 76  ARG B CA  1 
ATOM   5621  C C   . ARG C 2 76  ? 15.367  21.398  36.553  1.00 16.61  ? 76  ARG B C   1 
ATOM   5622  O O   . ARG C 2 76  ? 14.444  21.230  35.768  1.00 15.22  ? 76  ARG B O   1 
ATOM   5623  C CB  . ARG C 2 76  ? 17.548  22.109  35.597  1.00 17.16  ? 76  ARG B CB  1 
ATOM   5624  C CG  . ARG C 2 76  ? 18.455  23.230  35.132  1.00 17.06  ? 76  ARG B CG  1 
ATOM   5625  C CD  . ARG C 2 76  ? 19.737  22.651  34.563  1.00 17.00  ? 76  ARG B CD  1 
ATOM   5626  N NE  . ARG C 2 76  ? 20.459  21.862  35.565  1.00 16.88  ? 76  ARG B NE  1 
ATOM   5627  C CZ  . ARG C 2 76  ? 21.299  20.865  35.297  1.00 16.14  ? 76  ARG B CZ  1 
ATOM   5628  N NH1 . ARG C 2 76  ? 21.535  20.493  34.045  1.00 16.92  ? 76  ARG B NH1 1 
ATOM   5629  N NH2 . ARG C 2 76  ? 21.899  20.227  36.293  1.00 15.09  ? 76  ARG B NH2 1 
ATOM   5630  N N   . ILE C 2 77  ? 15.592  20.599  37.598  1.00 17.98  ? 77  ILE B N   1 
ATOM   5631  C CA  . ILE C 2 77  ? 14.706  19.480  37.924  1.00 18.69  ? 77  ILE B CA  1 
ATOM   5632  C C   . ILE C 2 77  ? 13.396  20.005  38.501  1.00 18.38  ? 77  ILE B C   1 
ATOM   5633  O O   . ILE C 2 77  ? 12.325  19.508  38.172  1.00 18.04  ? 77  ILE B O   1 
ATOM   5634  C CB  . ILE C 2 77  ? 15.339  18.499  38.930  1.00 20.23  ? 77  ILE B CB  1 
ATOM   5635  C CG1 . ILE C 2 77  ? 16.647  17.936  38.388  1.00 21.15  ? 77  ILE B CG1 1 
ATOM   5636  C CG2 . ILE C 2 77  ? 14.404  17.326  39.201  1.00 19.35  ? 77  ILE B CG2 1 
ATOM   5637  C CD1 . ILE C 2 77  ? 17.340  17.003  39.358  1.00 20.54  ? 77  ILE B CD1 1 
ATOM   5638  N N   . GLU C 2 78  ? 13.483  21.015  39.358  1.00 20.75  ? 78  GLU B N   1 
ATOM   5639  C CA  . GLU C 2 78  ? 12.287  21.654  39.899  1.00 24.22  ? 78  GLU B CA  1 
ATOM   5640  C C   . GLU C 2 78  ? 11.431  22.270  38.788  1.00 22.93  ? 78  GLU B C   1 
ATOM   5641  O O   . GLU C 2 78  ? 10.204  22.203  38.835  1.00 24.04  ? 78  GLU B O   1 
ATOM   5642  C CB  . GLU C 2 78  ? 12.670  22.709  40.934  1.00 28.64  ? 78  GLU B CB  1 
ATOM   5643  C CG  . GLU C 2 78  ? 11.470  23.246  41.690  1.00 33.71  ? 78  GLU B CG  1 
ATOM   5644  C CD  . GLU C 2 78  ? 10.562  22.151  42.274  1.00 44.64  ? 78  GLU B CD  1 
ATOM   5645  O OE1 . GLU C 2 78  ? 10.817  21.589  43.375  1.00 51.42  ? 78  GLU B OE1 1 
ATOM   5646  O OE2 . GLU C 2 78  ? 9.548   21.855  41.614  1.00 43.54  ? 78  GLU B OE2 1 
ATOM   5647  N N   . ASN C 2 79  ? 12.075  22.855  37.783  1.00 22.28  ? 79  ASN B N   1 
ATOM   5648  C CA  . ASN C 2 79  ? 11.351  23.397  36.634  1.00 20.50  ? 79  ASN B CA  1 
ATOM   5649  C C   . ASN C 2 79  ? 10.682  22.291  35.824  1.00 19.64  ? 79  ASN B C   1 
ATOM   5650  O O   . ASN C 2 79  ? 9.568   22.461  35.321  1.00 20.11  ? 79  ASN B O   1 
ATOM   5651  C CB  . ASN C 2 79  ? 12.278  24.208  35.733  1.00 19.62  ? 79  ASN B CB  1 
ATOM   5652  C CG  . ASN C 2 79  ? 11.557  24.754  34.519  1.00 20.59  ? 79  ASN B CG  1 
ATOM   5653  O OD1 . ASN C 2 79  ? 10.516  25.394  34.643  1.00 22.15  ? 79  ASN B OD1 1 
ATOM   5654  N ND2 . ASN C 2 79  ? 12.084  24.473  33.338  1.00 22.43  ? 79  ASN B ND2 1 
ATOM   5655  N N   . LEU C 2 80  ? 11.369  21.163  35.689  1.00 19.69  ? 80  LEU B N   1 
ATOM   5656  C CA  . LEU C 2 80  ? 10.798  20.009  35.011  1.00 20.43  ? 80  LEU B CA  1 
ATOM   5657  C C   . LEU C 2 80  ? 9.525   19.544  35.725  1.00 19.44  ? 80  LEU B C   1 
ATOM   5658  O O   . LEU C 2 80  ? 8.519   19.240  35.084  1.00 17.92  ? 80  LEU B O   1 
ATOM   5659  C CB  . LEU C 2 80  ? 11.825  18.881  34.931  1.00 21.83  ? 80  LEU B CB  1 
ATOM   5660  C CG  . LEU C 2 80  ? 11.357  17.596  34.237  1.00 23.47  ? 80  LEU B CG  1 
ATOM   5661  C CD1 . LEU C 2 80  ? 10.675  17.911  32.913  1.00 23.65  ? 80  LEU B CD1 1 
ATOM   5662  C CD2 . LEU C 2 80  ? 12.534  16.648  34.020  1.00 22.52  ? 80  LEU B CD2 1 
ATOM   5663  N N   . ASN C 2 81  ? 9.565   19.519  37.054  1.00 18.19  ? 81  ASN B N   1 
ATOM   5664  C CA  . ASN C 2 81  ? 8.380   19.206  37.841  1.00 17.70  ? 81  ASN B CA  1 
ATOM   5665  C C   . ASN C 2 81  ? 7.275   20.240  37.686  1.00 17.50  ? 81  ASN B C   1 
ATOM   5666  O O   . ASN C 2 81  ? 6.099   19.889  37.617  1.00 20.14  ? 81  ASN B O   1 
ATOM   5667  C CB  . ASN C 2 81  ? 8.733   19.072  39.319  1.00 19.13  ? 81  ASN B CB  1 
ATOM   5668  C CG  . ASN C 2 81  ? 7.521   18.781  40.167  1.00 18.84  ? 81  ASN B CG  1 
ATOM   5669  O OD1 . ASN C 2 81  ? 7.090   19.614  40.963  1.00 21.08  ? 81  ASN B OD1 1 
ATOM   5670  N ND2 . ASN C 2 81  ? 6.932   17.617  39.964  1.00 19.26  ? 81  ASN B ND2 1 
ATOM   5671  N N   . LYS C 2 82  ? 7.648   21.515  37.634  1.00 17.92  ? 82  LYS B N   1 
ATOM   5672  C CA  . LYS C 2 82  ? 6.672   22.582  37.420  1.00 18.94  ? 82  LYS B CA  1 
ATOM   5673  C C   . LYS C 2 82  ? 5.951   22.424  36.073  1.00 18.94  ? 82  LYS B C   1 
ATOM   5674  O O   . LYS C 2 82  ? 4.726   22.530  36.009  1.00 19.26  ? 82  LYS B O   1 
ATOM   5675  C CB  . LYS C 2 82  ? 7.339   23.960  37.503  1.00 21.40  ? 82  LYS B CB  1 
ATOM   5676  C CG  . LYS C 2 82  ? 6.415   25.121  37.139  1.00 23.13  ? 82  LYS B CG  1 
ATOM   5677  C CD  . LYS C 2 82  ? 7.155   26.451  37.096  1.00 23.07  ? 82  LYS B CD  1 
ATOM   5678  C CE  . LYS C 2 82  ? 6.384   27.478  36.283  1.00 23.64  ? 82  LYS B CE  1 
ATOM   5679  N NZ  . LYS C 2 82  ? 4.964   27.581  36.727  1.00 24.17  ? 82  LYS B NZ  1 
ATOM   5680  N N   . LYS C 2 83  ? 6.709   22.182  35.004  1.00 19.08  ? 83  LYS B N   1 
ATOM   5681  C CA  . LYS C 2 83  ? 6.114   21.953  33.681  1.00 19.99  ? 83  LYS B CA  1 
ATOM   5682  C C   . LYS C 2 83  ? 5.107   20.808  33.717  1.00 20.12  ? 83  LYS B C   1 
ATOM   5683  O O   . LYS C 2 83  ? 4.024   20.909  33.142  1.00 20.69  ? 83  LYS B O   1 
ATOM   5684  C CB  . LYS C 2 83  ? 7.199   21.679  32.635  1.00 20.59  ? 83  LYS B CB  1 
ATOM   5685  C CG  . LYS C 2 83  ? 8.002   22.915  32.261  1.00 21.33  ? 83  LYS B CG  1 
ATOM   5686  C CD  . LYS C 2 83  ? 8.973   22.662  31.121  1.00 22.89  ? 83  LYS B CD  1 
ATOM   5687  C CE  . LYS C 2 83  ? 10.216  21.918  31.584  1.00 24.74  ? 83  LYS B CE  1 
ATOM   5688  N NZ  . LYS C 2 83  ? 11.196  21.695  30.476  1.00 27.26  ? 83  LYS B NZ  1 
ATOM   5689  N N   . MET C 2 84  ? 5.461   19.734  34.418  1.00 21.65  ? 84  MET B N   1 
ATOM   5690  C CA  . MET C 2 84  ? 4.579   18.581  34.571  1.00 21.63  ? 84  MET B CA  1 
ATOM   5691  C C   . MET C 2 84  ? 3.303   18.927  35.333  1.00 21.54  ? 84  MET B C   1 
ATOM   5692  O O   . MET C 2 84  ? 2.202   18.688  34.833  1.00 22.56  ? 84  MET B O   1 
ATOM   5693  C CB  . MET C 2 84  ? 5.312   17.452  35.287  1.00 24.12  ? 84  MET B CB  1 
ATOM   5694  C CG  . MET C 2 84  ? 4.601   16.109  35.215  1.00 26.35  ? 84  MET B CG  1 
ATOM   5695  S SD  . MET C 2 84  ? 5.032   15.053  36.606  1.00 30.05  ? 84  MET B SD  1 
ATOM   5696  C CE  . MET C 2 84  ? 4.283   15.947  37.968  1.00 27.46  ? 84  MET B CE  1 
ATOM   5697  N N   . GLU C 2 85  ? 3.443   19.480  36.538  1.00 22.18  ? 85  GLU B N   1 
ATOM   5698  C CA  . GLU C 2 85  ? 2.268   19.852  37.362  1.00 23.56  ? 85  GLU B CA  1 
ATOM   5699  C C   . GLU C 2 85  ? 1.333   20.805  36.620  1.00 22.32  ? 85  GLU B C   1 
ATOM   5700  O O   . GLU C 2 85  ? 0.119   20.620  36.611  1.00 22.58  ? 85  GLU B O   1 
ATOM   5701  C CB  . GLU C 2 85  ? 2.692   20.502  38.683  1.00 26.65  ? 85  GLU B CB  1 
ATOM   5702  C CG  . GLU C 2 85  ? 3.138   19.526  39.761  1.00 29.75  ? 85  GLU B CG  1 
ATOM   5703  C CD  . GLU C 2 85  ? 3.382   20.191  41.108  1.00 32.40  ? 85  GLU B CD  1 
ATOM   5704  O OE1 . GLU C 2 85  ? 2.646   21.141  41.462  1.00 32.49  ? 85  GLU B OE1 1 
ATOM   5705  O OE2 . GLU C 2 85  ? 4.305   19.748  41.827  1.00 32.97  ? 85  GLU B OE2 1 
ATOM   5706  N N   . ASP C 2 86  ? 1.915   21.830  36.003  1.00 22.77  ? 86  ASP B N   1 
ATOM   5707  C CA  . ASP C 2 86  ? 1.163   22.784  35.192  1.00 20.22  ? 86  ASP B CA  1 
ATOM   5708  C C   . ASP C 2 86  ? 0.501   22.101  33.995  1.00 19.38  ? 86  ASP B C   1 
ATOM   5709  O O   . ASP C 2 86  ? -0.645  22.408  33.652  1.00 19.37  ? 86  ASP B O   1 
ATOM   5710  C CB  . ASP C 2 86  ? 2.083   23.916  34.720  1.00 20.94  ? 86  ASP B CB  1 
ATOM   5711  C CG  . ASP C 2 86  ? 2.516   24.839  35.859  1.00 23.61  ? 86  ASP B CG  1 
ATOM   5712  O OD1 . ASP C 2 86  ? 2.080   24.626  37.018  1.00 25.79  ? 86  ASP B OD1 1 
ATOM   5713  O OD2 . ASP C 2 86  ? 3.297   25.781  35.600  1.00 22.75  ? 86  ASP B OD2 1 
ATOM   5714  N N   . GLY C 2 87  ? 1.218   21.169  33.373  1.00 18.39  ? 87  GLY B N   1 
ATOM   5715  C CA  . GLY C 2 87  ? 0.673   20.393  32.263  1.00 16.98  ? 87  GLY B CA  1 
ATOM   5716  C C   . GLY C 2 87  ? -0.599  19.655  32.647  1.00 16.39  ? 87  GLY B C   1 
ATOM   5717  O O   . GLY C 2 87  ? -1.616  19.768  31.968  1.00 15.99  ? 87  GLY B O   1 
ATOM   5718  N N   . PHE C 2 88  ? -0.555  18.905  33.746  1.00 15.92  ? 88  PHE B N   1 
ATOM   5719  C CA  . PHE C 2 88  ? -1.731  18.143  34.176  1.00 16.41  ? 88  PHE B CA  1 
ATOM   5720  C C   . PHE C 2 88  ? -2.873  19.048  34.618  1.00 16.08  ? 88  PHE B C   1 
ATOM   5721  O O   . PHE C 2 88  ? -4.031  18.764  34.327  1.00 17.37  ? 88  PHE B O   1 
ATOM   5722  C CB  . PHE C 2 88  ? -1.383  17.123  35.263  1.00 16.35  ? 88  PHE B CB  1 
ATOM   5723  C CG  . PHE C 2 88  ? -0.649  15.918  34.742  1.00 16.25  ? 88  PHE B CG  1 
ATOM   5724  C CD1 . PHE C 2 88  ? 0.620   15.613  35.194  1.00 17.74  ? 88  PHE B CD1 1 
ATOM   5725  C CD2 . PHE C 2 88  ? -1.223  15.103  33.776  1.00 16.96  ? 88  PHE B CD2 1 
ATOM   5726  C CE1 . PHE C 2 88  ? 1.306   14.510  34.703  1.00 18.67  ? 88  PHE B CE1 1 
ATOM   5727  C CE2 . PHE C 2 88  ? -0.548  14.000  33.280  1.00 18.66  ? 88  PHE B CE2 1 
ATOM   5728  C CZ  . PHE C 2 88  ? 0.722   13.702  33.745  1.00 19.14  ? 88  PHE B CZ  1 
ATOM   5729  N N   . LEU C 2 89  ? -2.553  20.155  35.275  1.00 17.11  ? 89  LEU B N   1 
ATOM   5730  C CA  . LEU C 2 89  ? -3.581  21.132  35.640  1.00 18.54  ? 89  LEU B CA  1 
ATOM   5731  C C   . LEU C 2 89  ? -4.312  21.658  34.404  1.00 19.15  ? 89  LEU B C   1 
ATOM   5732  O O   . LEU C 2 89  ? -5.532  21.835  34.430  1.00 19.64  ? 89  LEU B O   1 
ATOM   5733  C CB  . LEU C 2 89  ? -2.983  22.294  36.435  1.00 19.10  ? 89  LEU B CB  1 
ATOM   5734  C CG  . LEU C 2 89  ? -4.032  23.318  36.907  1.00 19.74  ? 89  LEU B CG  1 
ATOM   5735  C CD1 . LEU C 2 89  ? -3.763  23.815  38.318  1.00 21.13  ? 89  LEU B CD1 1 
ATOM   5736  C CD2 . LEU C 2 89  ? -4.124  24.483  35.936  1.00 20.25  ? 89  LEU B CD2 1 
ATOM   5737  N N   . ASP C 2 90  ? -3.566  21.902  33.329  1.00 19.33  ? 90  ASP B N   1 
ATOM   5738  C CA  . ASP C 2 90  ? -4.162  22.378  32.077  1.00 20.42  ? 90  ASP B CA  1 
ATOM   5739  C C   . ASP C 2 90  ? -5.017  21.306  31.409  1.00 17.93  ? 90  ASP B C   1 
ATOM   5740  O O   . ASP C 2 90  ? -6.111  21.594  30.926  1.00 16.20  ? 90  ASP B O   1 
ATOM   5741  C CB  . ASP C 2 90  ? -3.083  22.862  31.100  1.00 21.81  ? 90  ASP B CB  1 
ATOM   5742  C CG  . ASP C 2 90  ? -2.371  24.128  31.575  1.00 25.36  ? 90  ASP B CG  1 
ATOM   5743  O OD1 . ASP C 2 90  ? -2.856  24.791  32.523  1.00 27.66  ? 90  ASP B OD1 1 
ATOM   5744  O OD2 . ASP C 2 90  ? -1.314  24.462  30.990  1.00 30.22  ? 90  ASP B OD2 1 
ATOM   5745  N N   . VAL C 2 91  ? -4.526  20.070  31.392  1.00 16.82  ? 91  VAL B N   1 
ATOM   5746  C CA  . VAL C 2 91  ? -5.279  18.973  30.786  1.00 15.61  ? 91  VAL B CA  1 
ATOM   5747  C C   . VAL C 2 91  ? -6.597  18.744  31.515  1.00 14.69  ? 91  VAL B C   1 
ATOM   5748  O O   . VAL C 2 91  ? -7.656  18.732  30.892  1.00 14.83  ? 91  VAL B O   1 
ATOM   5749  C CB  . VAL C 2 91  ? -4.470  17.662  30.745  1.00 14.96  ? 91  VAL B CB  1 
ATOM   5750  C CG1 . VAL C 2 91  ? -5.397  16.469  30.572  1.00 14.16  ? 91  VAL B CG1 1 
ATOM   5751  C CG2 . VAL C 2 91  ? -3.439  17.718  29.625  1.00 14.95  ? 91  VAL B CG2 1 
ATOM   5752  N N   . TRP C 2 92  ? -6.535  18.584  32.831  1.00 14.04  ? 92  TRP B N   1 
ATOM   5753  C CA  . TRP C 2 92  ? -7.743  18.328  33.616  1.00 14.33  ? 92  TRP B CA  1 
ATOM   5754  C C   . TRP C 2 92  ? -8.717  19.466  33.601  1.00 15.37  ? 92  TRP B C   1 
ATOM   5755  O O   . TRP C 2 92  ? -9.924  19.249  33.548  1.00 15.17  ? 92  TRP B O   1 
ATOM   5756  C CB  . TRP C 2 92  ? -7.391  17.984  35.054  1.00 13.83  ? 92  TRP B CB  1 
ATOM   5757  C CG  . TRP C 2 92  ? -6.795  16.610  35.210  1.00 12.94  ? 92  TRP B CG  1 
ATOM   5758  C CD1 . TRP C 2 92  ? -5.533  16.281  35.688  1.00 12.60  ? 92  TRP B CD1 1 
ATOM   5759  C CD2 . TRP C 2 92  ? -7.428  15.329  34.893  1.00 11.94  ? 92  TRP B CD2 1 
ATOM   5760  N NE1 . TRP C 2 92  ? -5.350  14.925  35.687  1.00 12.73  ? 92  TRP B NE1 1 
ATOM   5761  C CE2 . TRP C 2 92  ? -6.450  14.297  35.223  1.00 12.38  ? 92  TRP B CE2 1 
ATOM   5762  C CE3 . TRP C 2 92  ? -8.655  14.952  34.391  1.00 12.49  ? 92  TRP B CE3 1 
ATOM   5763  C CZ2 . TRP C 2 92  ? -6.716  12.953  35.048  1.00 12.62  ? 92  TRP B CZ2 1 
ATOM   5764  C CZ3 . TRP C 2 92  ? -8.915  13.591  34.219  1.00 12.93  ? 92  TRP B CZ3 1 
ATOM   5765  C CH2 . TRP C 2 92  ? -7.967  12.617  34.542  1.00 12.75  ? 92  TRP B CH2 1 
ATOM   5766  N N   . THR C 2 93  ? -8.215  20.693  33.650  1.00 17.31  ? 93  THR B N   1 
ATOM   5767  C CA  . THR C 2 93  ? -9.088  21.861  33.623  1.00 18.63  ? 93  THR B CA  1 
ATOM   5768  C C   . THR C 2 93  ? -9.889  21.910  32.327  1.00 19.64  ? 93  THR B C   1 
ATOM   5769  O O   . THR C 2 93  ? -11.109 22.043  32.353  1.00 20.34  ? 93  THR B O   1 
ATOM   5770  C CB  . THR C 2 93  ? -8.286  23.161  33.803  1.00 20.70  ? 93  THR B CB  1 
ATOM   5771  O OG1 . THR C 2 93  ? -7.731  23.198  35.125  1.00 18.11  ? 93  THR B OG1 1 
ATOM   5772  C CG2 . THR C 2 93  ? -9.184  24.391  33.581  1.00 20.61  ? 93  THR B CG2 1 
ATOM   5773  N N   . TYR C 2 94  ? -9.208  21.778  31.195  1.00 19.92  ? 94  TYR B N   1 
ATOM   5774  C CA  . TYR C 2 94  ? -9.882  21.826  29.896  1.00 20.65  ? 94  TYR B CA  1 
ATOM   5775  C C   . TYR C 2 94  ? -10.889 20.694  29.732  1.00 21.39  ? 94  TYR B C   1 
ATOM   5776  O O   . TYR C 2 94  ? -12.026 20.921  29.308  1.00 20.17  ? 94  TYR B O   1 
ATOM   5777  C CB  . TYR C 2 94  ? -8.862  21.767  28.773  1.00 20.99  ? 94  TYR B CB  1 
ATOM   5778  C CG  . TYR C 2 94  ? -9.404  22.167  27.427  1.00 23.56  ? 94  TYR B CG  1 
ATOM   5779  C CD1 . TYR C 2 94  ? -9.699  23.494  27.143  1.00 25.01  ? 94  TYR B CD1 1 
ATOM   5780  C CD2 . TYR C 2 94  ? -9.601  21.223  26.424  1.00 25.08  ? 94  TYR B CD2 1 
ATOM   5781  C CE1 . TYR C 2 94  ? -10.180 23.870  25.901  1.00 25.04  ? 94  TYR B CE1 1 
ATOM   5782  C CE2 . TYR C 2 94  ? -10.078 21.590  25.180  1.00 24.83  ? 94  TYR B CE2 1 
ATOM   5783  C CZ  . TYR C 2 94  ? -10.365 22.913  24.923  1.00 24.55  ? 94  TYR B CZ  1 
ATOM   5784  O OH  . TYR C 2 94  ? -10.836 23.281  23.684  1.00 23.45  ? 94  TYR B OH  1 
ATOM   5785  N N   . ASN C 2 95  ? -10.469 19.476  30.063  1.00 23.53  ? 95  ASN B N   1 
ATOM   5786  C CA  . ASN C 2 95  ? -11.334 18.307  29.918  1.00 26.01  ? 95  ASN B CA  1 
ATOM   5787  C C   . ASN C 2 95  ? -12.548 18.376  30.841  1.00 26.43  ? 95  ASN B C   1 
ATOM   5788  O O   . ASN C 2 95  ? -13.659 18.071  30.420  1.00 28.03  ? 95  ASN B O   1 
ATOM   5789  C CB  . ASN C 2 95  ? -10.552 17.013  30.161  1.00 28.97  ? 95  ASN B CB  1 
ATOM   5790  C CG  . ASN C 2 95  ? -9.581  16.688  29.025  1.00 34.28  ? 95  ASN B CG  1 
ATOM   5791  O OD1 . ASN C 2 95  ? -9.438  17.447  28.068  1.00 35.04  ? 95  ASN B OD1 1 
ATOM   5792  N ND2 . ASN C 2 95  ? -8.913  15.546  29.130  1.00 40.36  ? 95  ASN B ND2 1 
ATOM   5793  N N   . ALA C 2 96  ? -12.334 18.791  32.088  1.00 24.54  ? 96  ALA B N   1 
ATOM   5794  C CA  . ALA C 2 96  ? -13.426 18.937  33.046  1.00 22.96  ? 96  ALA B CA  1 
ATOM   5795  C C   . ALA C 2 96  ? -14.424 19.985  32.576  1.00 24.45  ? 96  ALA B C   1 
ATOM   5796  O O   . ALA C 2 96  ? -15.632 19.747  32.592  1.00 25.30  ? 96  ALA B O   1 
ATOM   5797  C CB  . ALA C 2 96  ? -12.895 19.309  34.418  1.00 22.33  ? 96  ALA B CB  1 
ATOM   5798  N N   . GLU C 2 97  ? -13.918 21.144  32.159  1.00 24.43  ? 97  GLU B N   1 
ATOM   5799  C CA  . GLU C 2 97  ? -14.779 22.232  31.689  1.00 24.17  ? 97  GLU B CA  1 
ATOM   5800  C C   . GLU C 2 97  ? -15.593 21.821  30.468  1.00 22.11  ? 97  GLU B C   1 
ATOM   5801  O O   . GLU C 2 97  ? -16.811 22.001  30.442  1.00 21.94  ? 97  GLU B O   1 
ATOM   5802  C CB  . GLU C 2 97  ? -13.963 23.484  31.368  1.00 24.35  ? 97  GLU B CB  1 
ATOM   5803  C CG  . GLU C 2 97  ? -13.351 24.160  32.589  1.00 27.00  ? 97  GLU B CG  1 
ATOM   5804  C CD  . GLU C 2 97  ? -14.341 24.961  33.418  1.00 28.90  ? 97  GLU B CD  1 
ATOM   5805  O OE1 . GLU C 2 97  ? -15.541 25.026  33.066  1.00 29.15  ? 97  GLU B OE1 1 
ATOM   5806  O OE2 . GLU C 2 97  ? -13.904 25.539  34.434  1.00 29.28  ? 97  GLU B OE2 1 
ATOM   5807  N N   . LEU C 2 98  ? -14.928 21.248  29.472  1.00 20.99  ? 98  LEU B N   1 
ATOM   5808  C CA  . LEU C 2 98  ? -15.615 20.856  28.248  1.00 21.23  ? 98  LEU B CA  1 
ATOM   5809  C C   . LEU C 2 98  ? -16.554 19.678  28.452  1.00 21.76  ? 98  LEU B C   1 
ATOM   5810  O O   . LEU C 2 98  ? -17.602 19.609  27.809  1.00 23.05  ? 98  LEU B O   1 
ATOM   5811  C CB  . LEU C 2 98  ? -14.623 20.558  27.128  1.00 20.68  ? 98  LEU B CB  1 
ATOM   5812  C CG  . LEU C 2 98  ? -13.958 21.774  26.490  1.00 20.96  ? 98  LEU B CG  1 
ATOM   5813  C CD1 . LEU C 2 98  ? -13.231 21.333  25.235  1.00 21.83  ? 98  LEU B CD1 1 
ATOM   5814  C CD2 . LEU C 2 98  ? -14.981 22.841  26.150  1.00 21.85  ? 98  LEU B CD2 1 
ATOM   5815  N N   . LEU C 2 99  ? -16.189 18.756  29.337  1.00 23.30  ? 99  LEU B N   1 
ATOM   5816  C CA  . LEU C 2 99  ? -17.072 17.643  29.684  1.00 25.17  ? 99  LEU B CA  1 
ATOM   5817  C C   . LEU C 2 99  ? -18.378 18.151  30.275  1.00 24.14  ? 99  LEU B C   1 
ATOM   5818  O O   . LEU C 2 99  ? -19.449 17.675  29.917  1.00 24.72  ? 99  LEU B O   1 
ATOM   5819  C CB  . LEU C 2 99  ? -16.391 16.703  30.681  1.00 28.96  ? 99  LEU B CB  1 
ATOM   5820  C CG  . LEU C 2 99  ? -17.221 15.523  31.187  1.00 31.72  ? 99  LEU B CG  1 
ATOM   5821  C CD1 . LEU C 2 99  ? -17.582 14.593  30.037  1.00 32.51  ? 99  LEU B CD1 1 
ATOM   5822  C CD2 . LEU C 2 99  ? -16.462 14.782  32.278  1.00 33.50  ? 99  LEU B CD2 1 
ATOM   5823  N N   . VAL C 2 100 ? -18.278 19.116  31.183  1.00 24.05  ? 100 VAL B N   1 
ATOM   5824  C CA  . VAL C 2 100 ? -19.452 19.696  31.823  1.00 22.85  ? 100 VAL B CA  1 
ATOM   5825  C C   . VAL C 2 100 ? -20.337 20.428  30.809  1.00 23.80  ? 100 VAL B C   1 
ATOM   5826  O O   . VAL C 2 100 ? -21.542 20.185  30.749  1.00 23.29  ? 100 VAL B O   1 
ATOM   5827  C CB  . VAL C 2 100 ? -19.049 20.646  32.964  1.00 22.59  ? 100 VAL B CB  1 
ATOM   5828  C CG1 . VAL C 2 100 ? -20.249 21.456  33.442  1.00 22.07  ? 100 VAL B CG1 1 
ATOM   5829  C CG2 . VAL C 2 100 ? -18.462 19.846  34.110  1.00 22.45  ? 100 VAL B CG2 1 
ATOM   5830  N N   . LEU C 2 101 ? -19.741 21.312  30.009  1.00 23.35  ? 101 LEU B N   1 
ATOM   5831  C CA  . LEU C 2 101 ? -20.492 22.038  28.979  1.00 21.98  ? 101 LEU B CA  1 
ATOM   5832  C C   . LEU C 2 101 ? -21.177 21.082  27.999  1.00 21.65  ? 101 LEU B C   1 
ATOM   5833  O O   . LEU C 2 101 ? -22.333 21.296  27.621  1.00 20.06  ? 101 LEU B O   1 
ATOM   5834  C CB  . LEU C 2 101 ? -19.577 22.999  28.204  1.00 21.88  ? 101 LEU B CB  1 
ATOM   5835  C CG  . LEU C 2 101 ? -18.974 24.202  28.944  1.00 20.72  ? 101 LEU B CG  1 
ATOM   5836  C CD1 . LEU C 2 101 ? -18.113 25.037  28.003  1.00 19.07  ? 101 LEU B CD1 1 
ATOM   5837  C CD2 . LEU C 2 101 ? -20.058 25.056  29.582  1.00 19.79  ? 101 LEU B CD2 1 
ATOM   5838  N N   . MET C 2 102 ? -20.462 20.032  27.600  1.00 22.27  ? 102 MET B N   1 
ATOM   5839  C CA  . MET C 2 102 ? -20.976 19.076  26.625  1.00 24.35  ? 102 MET B CA  1 
ATOM   5840  C C   . MET C 2 102 ? -22.124 18.253  27.196  1.00 23.58  ? 102 MET B C   1 
ATOM   5841  O O   . MET C 2 102 ? -23.182 18.140  26.579  1.00 21.85  ? 102 MET B O   1 
ATOM   5842  C CB  . MET C 2 102 ? -19.855 18.157  26.131  1.00 28.86  ? 102 MET B CB  1 
ATOM   5843  C CG  . MET C 2 102 ? -18.948 18.811  25.100  1.00 33.45  ? 102 MET B CG  1 
ATOM   5844  S SD  . MET C 2 102 ? -17.404 17.921  24.795  1.00 40.36  ? 102 MET B SD  1 
ATOM   5845  C CE  . MET C 2 102 ? -18.032 16.498  23.906  1.00 42.01  ? 102 MET B CE  1 
ATOM   5846  N N   . GLU C 2 103 ? -21.925 17.691  28.381  1.00 24.80  ? 103 GLU B N   1 
ATOM   5847  C CA  . GLU C 2 103 ? -22.951 16.852  28.987  1.00 25.86  ? 103 GLU B CA  1 
ATOM   5848  C C   . GLU C 2 103 ? -24.180 17.630  29.452  1.00 23.91  ? 103 GLU B C   1 
ATOM   5849  O O   . GLU C 2 103 ? -25.288 17.091  29.459  1.00 25.57  ? 103 GLU B O   1 
ATOM   5850  C CB  . GLU C 2 103 ? -22.368 16.004  30.119  1.00 28.62  ? 103 GLU B CB  1 
ATOM   5851  C CG  . GLU C 2 103 ? -21.578 14.797  29.622  1.00 32.03  ? 103 GLU B CG  1 
ATOM   5852  C CD  . GLU C 2 103 ? -22.377 13.897  28.680  1.00 37.93  ? 103 GLU B CD  1 
ATOM   5853  O OE1 . GLU C 2 103 ? -23.602 13.724  28.892  1.00 40.93  ? 103 GLU B OE1 1 
ATOM   5854  O OE2 . GLU C 2 103 ? -21.782 13.357  27.723  1.00 36.53  ? 103 GLU B OE2 1 
ATOM   5855  N N   . ASN C 2 104 ? -23.997 18.895  29.810  1.00 23.99  ? 104 ASN B N   1 
ATOM   5856  C CA  . ASN C 2 104 ? -25.133 19.765  30.108  1.00 25.12  ? 104 ASN B CA  1 
ATOM   5857  C C   . ASN C 2 104 ? -26.020 19.984  28.878  1.00 25.97  ? 104 ASN B C   1 
ATOM   5858  O O   . ASN C 2 104 ? -27.241 19.922  28.984  1.00 26.73  ? 104 ASN B O   1 
ATOM   5859  C CB  . ASN C 2 104 ? -24.669 21.109  30.675  1.00 25.16  ? 104 ASN B CB  1 
ATOM   5860  C CG  . ASN C 2 104 ? -24.222 21.010  32.123  1.00 25.97  ? 104 ASN B CG  1 
ATOM   5861  O OD1 . ASN C 2 104 ? -24.457 20.005  32.793  1.00 27.68  ? 104 ASN B OD1 1 
ATOM   5862  N ND2 . ASN C 2 104 ? -23.572 22.061  32.614  1.00 24.77  ? 104 ASN B ND2 1 
ATOM   5863  N N   . GLU C 2 105 ? -25.410 20.238  27.722  1.00 25.07  ? 105 GLU B N   1 
ATOM   5864  C CA  . GLU C 2 105 ? -26.163 20.357  26.478  1.00 27.39  ? 105 GLU B CA  1 
ATOM   5865  C C   . GLU C 2 105 ? -26.977 19.080  26.251  1.00 26.87  ? 105 GLU B C   1 
ATOM   5866  O O   . GLU C 2 105 ? -28.162 19.130  25.944  1.00 22.89  ? 105 GLU B O   1 
ATOM   5867  C CB  . GLU C 2 105 ? -25.222 20.585  25.293  1.00 31.43  ? 105 GLU B CB  1 
ATOM   5868  C CG  . GLU C 2 105 ? -25.920 20.977  23.998  1.00 39.45  ? 105 GLU B CG  1 
ATOM   5869  C CD  . GLU C 2 105 ? -25.362 20.254  22.779  1.00 54.52  ? 105 GLU B CD  1 
ATOM   5870  O OE1 . GLU C 2 105 ? -24.712 20.909  21.930  1.00 65.34  ? 105 GLU B OE1 1 
ATOM   5871  O OE2 . GLU C 2 105 ? -25.562 19.024  22.670  1.00 60.04  ? 105 GLU B OE2 1 
ATOM   5872  N N   . ARG C 2 106 ? -26.318 17.938  26.410  1.00 30.48  ? 106 ARG B N   1 
ATOM   5873  C CA  . ARG C 2 106 ? -26.950 16.638  26.237  1.00 32.13  ? 106 ARG B CA  1 
ATOM   5874  C C   . ARG C 2 106 ? -28.110 16.423  27.195  1.00 28.50  ? 106 ARG B C   1 
ATOM   5875  O O   . ARG C 2 106 ? -29.181 15.965  26.785  1.00 27.29  ? 106 ARG B O   1 
ATOM   5876  C CB  . ARG C 2 106 ? -25.885 15.560  26.459  1.00 42.60  ? 106 ARG B CB  1 
ATOM   5877  C CG  . ARG C 2 106 ? -26.260 14.107  26.141  1.00 58.15  ? 106 ARG B CG  1 
ATOM   5878  C CD  . ARG C 2 106 ? -26.698 13.954  24.670  1.00 68.25  ? 106 ARG B CD  1 
ATOM   5879  N NE  . ARG C 2 106 ? -25.668 14.274  23.685  1.00 68.48  ? 106 ARG B NE  1 
ATOM   5880  C CZ  . ARG C 2 106 ? -25.803 14.048  22.377  1.00 79.28  ? 106 ARG B CZ  1 
ATOM   5881  N NH1 . ARG C 2 106 ? -26.912 13.502  21.882  1.00 74.76  ? 106 ARG B NH1 1 
ATOM   5882  N NH2 . ARG C 2 106 ? -24.818 14.372  21.552  1.00 89.39  ? 106 ARG B NH2 1 
ATOM   5883  N N   . THR C 2 107 ? -27.904 16.764  28.464  1.00 25.04  ? 107 THR B N   1 
ATOM   5884  C CA  . THR C 2 107 ? -28.948 16.601  29.475  1.00 24.78  ? 107 THR B CA  1 
ATOM   5885  C C   . THR C 2 107 ? -30.193 17.438  29.166  1.00 26.24  ? 107 THR B C   1 
ATOM   5886  O O   . THR C 2 107 ? -31.318 16.966  29.328  1.00 26.77  ? 107 THR B O   1 
ATOM   5887  C CB  . THR C 2 107 ? -28.425 16.949  30.885  1.00 23.78  ? 107 THR B CB  1 
ATOM   5888  O OG1 . THR C 2 107 ? -27.395 16.030  31.248  1.00 20.86  ? 107 THR B OG1 1 
ATOM   5889  C CG2 . THR C 2 107 ? -29.538 16.886  31.923  1.00 22.07  ? 107 THR B CG2 1 
ATOM   5890  N N   . LEU C 2 108 ? -30.004 18.672  28.710  1.00 27.37  ? 108 LEU B N   1 
ATOM   5891  C CA  . LEU C 2 108 ? -31.148 19.525  28.411  1.00 26.41  ? 108 LEU B CA  1 
ATOM   5892  C C   . LEU C 2 108 ? -31.895 19.021  27.182  1.00 25.30  ? 108 LEU B C   1 
ATOM   5893  O O   . LEU C 2 108 ? -33.123 19.047  27.158  1.00 26.49  ? 108 LEU B O   1 
ATOM   5894  C CB  . LEU C 2 108 ? -30.733 20.996  28.256  1.00 26.06  ? 108 LEU B CB  1 
ATOM   5895  C CG  . LEU C 2 108 ? -30.135 21.645  29.516  1.00 27.97  ? 108 LEU B CG  1 
ATOM   5896  C CD1 . LEU C 2 108 ? -29.960 23.142  29.305  1.00 26.70  ? 108 LEU B CD1 1 
ATOM   5897  C CD2 . LEU C 2 108 ? -30.984 21.376  30.759  1.00 24.83  ? 108 LEU B CD2 1 
ATOM   5898  N N   . ASP C 2 109 ? -31.161 18.553  26.175  1.00 26.10  ? 109 ASP B N   1 
ATOM   5899  C CA  . ASP C 2 109 ? -31.784 17.978  24.979  1.00 27.12  ? 109 ASP B CA  1 
ATOM   5900  C C   . ASP C 2 109 ? -32.509 16.673  25.288  1.00 24.07  ? 109 ASP B C   1 
ATOM   5901  O O   . ASP C 2 109 ? -33.537 16.370  24.686  1.00 20.97  ? 109 ASP B O   1 
ATOM   5902  C CB  . ASP C 2 109 ? -30.754 17.762  23.861  1.00 31.27  ? 109 ASP B CB  1 
ATOM   5903  C CG  . ASP C 2 109 ? -30.534 19.011  23.016  1.00 40.56  ? 109 ASP B CG  1 
ATOM   5904  O OD1 . ASP C 2 109 ? -29.383 19.253  22.586  1.00 46.94  ? 109 ASP B OD1 1 
ATOM   5905  O OD2 . ASP C 2 109 ? -31.514 19.753  22.772  1.00 48.87  ? 109 ASP B OD2 1 
ATOM   5906  N N   . PHE C 2 110 ? -31.969 15.911  26.231  1.00 24.12  ? 110 PHE B N   1 
ATOM   5907  C CA  . PHE C 2 110 ? -32.625 14.707  26.730  1.00 24.28  ? 110 PHE B CA  1 
ATOM   5908  C C   . PHE C 2 110 ? -34.041 15.022  27.247  1.00 24.64  ? 110 PHE B C   1 
ATOM   5909  O O   . PHE C 2 110 ? -35.013 14.379  26.835  1.00 25.86  ? 110 PHE B O   1 
ATOM   5910  C CB  . PHE C 2 110 ? -31.752 14.096  27.831  1.00 24.41  ? 110 PHE B CB  1 
ATOM   5911  C CG  . PHE C 2 110 ? -32.275 12.815  28.401  1.00 24.50  ? 110 PHE B CG  1 
ATOM   5912  C CD1 . PHE C 2 110 ? -32.561 11.736  27.580  1.00 25.39  ? 110 PHE B CD1 1 
ATOM   5913  C CD2 . PHE C 2 110 ? -32.438 12.673  29.773  1.00 25.56  ? 110 PHE B CD2 1 
ATOM   5914  C CE1 . PHE C 2 110 ? -33.026 10.545  28.108  1.00 25.84  ? 110 PHE B CE1 1 
ATOM   5915  C CE2 . PHE C 2 110 ? -32.897 11.483  30.306  1.00 27.86  ? 110 PHE B CE2 1 
ATOM   5916  C CZ  . PHE C 2 110 ? -33.194 10.418  29.473  1.00 27.11  ? 110 PHE B CZ  1 
ATOM   5917  N N   . HIS C 2 111 ? -34.153 16.019  28.126  1.00 23.05  ? 111 HIS B N   1 
ATOM   5918  C CA  . HIS C 2 111 ? -35.454 16.442  28.656  1.00 24.07  ? 111 HIS B CA  1 
ATOM   5919  C C   . HIS C 2 111 ? -36.371 16.918  27.568  1.00 25.18  ? 111 HIS B C   1 
ATOM   5920  O O   . HIS C 2 111 ? -37.548 16.546  27.537  1.00 30.42  ? 111 HIS B O   1 
ATOM   5921  C CB  . HIS C 2 111 ? -35.300 17.545  29.698  1.00 23.24  ? 111 HIS B CB  1 
ATOM   5922  C CG  . HIS C 2 111 ? -34.554 17.116  30.930  1.00 23.60  ? 111 HIS B CG  1 
ATOM   5923  N ND1 . HIS C 2 111 ? -34.848 15.984  31.588  1.00 24.72  ? 111 HIS B ND1 1 
ATOM   5924  C CD2 . HIS C 2 111 ? -33.511 17.718  31.626  1.00 22.82  ? 111 HIS B CD2 1 
ATOM   5925  C CE1 . HIS C 2 111 ? -34.034 15.858  32.648  1.00 24.39  ? 111 HIS B CE1 1 
ATOM   5926  N NE2 . HIS C 2 111 ? -33.212 16.918  32.669  1.00 24.35  ? 111 HIS B NE2 1 
ATOM   5927  N N   . ASP C 2 112 ? -35.855 17.747  26.666  1.00 24.46  ? 112 ASP B N   1 
ATOM   5928  C CA  . ASP C 2 112 ? -36.632 18.182  25.503  1.00 29.36  ? 112 ASP B CA  1 
ATOM   5929  C C   . ASP C 2 112 ? -37.182 16.983  24.735  1.00 28.40  ? 112 ASP B C   1 
ATOM   5930  O O   . ASP C 2 112 ? -38.369 16.929  24.420  1.00 32.02  ? 112 ASP B O   1 
ATOM   5931  C CB  . ASP C 2 112 ? -35.785 19.040  24.560  1.00 32.68  ? 112 ASP B CB  1 
ATOM   5932  C CG  . ASP C 2 112 ? -35.597 20.465  25.063  1.00 41.34  ? 112 ASP B CG  1 
ATOM   5933  O OD1 . ASP C 2 112 ? -36.179 20.828  26.114  1.00 47.58  ? 112 ASP B OD1 1 
ATOM   5934  O OD2 . ASP C 2 112 ? -34.859 21.226  24.396  1.00 43.99  ? 112 ASP B OD2 1 
ATOM   5935  N N   . SER C 2 113 ? -36.316 16.013  24.467  1.00 25.78  ? 113 SER B N   1 
ATOM   5936  C CA  . SER C 2 113 ? -36.692 14.820  23.719  1.00 25.68  ? 113 SER B CA  1 
ATOM   5937  C C   . SER C 2 113 ? -37.789 14.010  24.418  1.00 25.54  ? 113 SER B C   1 
ATOM   5938  O O   . SER C 2 113 ? -38.692 13.495  23.762  1.00 25.70  ? 113 SER B O   1 
ATOM   5939  C CB  . SER C 2 113 ? -35.460 13.937  23.484  1.00 26.65  ? 113 SER B CB  1 
ATOM   5940  O OG  . SER C 2 113 ? -35.702 13.000  22.459  1.00 29.36  ? 113 SER B OG  1 
ATOM   5941  N N   . ASN C 2 114 ? -37.708 13.902  25.741  1.00 24.54  ? 114 ASN B N   1 
ATOM   5942  C CA  . ASN C 2 114 ? -38.694 13.144  26.511  1.00 26.32  ? 114 ASN B CA  1 
ATOM   5943  C C   . ASN C 2 114 ? -40.084 13.786  26.497  1.00 26.52  ? 114 ASN B C   1 
ATOM   5944  O O   . ASN C 2 114 ? -41.094 13.091  26.411  1.00 26.09  ? 114 ASN B O   1 
ATOM   5945  C CB  . ASN C 2 114 ? -38.216 12.968  27.960  1.00 26.57  ? 114 ASN B CB  1 
ATOM   5946  C CG  . ASN C 2 114 ? -37.056 12.003  28.085  1.00 28.60  ? 114 ASN B CG  1 
ATOM   5947  O OD1 . ASN C 2 114 ? -36.884 11.102  27.259  1.00 33.41  ? 114 ASN B OD1 1 
ATOM   5948  N ND2 . ASN C 2 114 ? -36.252 12.181  29.126  1.00 26.61  ? 114 ASN B ND2 1 
ATOM   5949  N N   . VAL C 2 115 ? -40.128 15.110  26.583  1.00 28.15  ? 115 VAL B N   1 
ATOM   5950  C CA  . VAL C 2 115 ? -41.391 15.835  26.547  1.00 29.77  ? 115 VAL B CA  1 
ATOM   5951  C C   . VAL C 2 115 ? -42.047 15.668  25.184  1.00 29.86  ? 115 VAL B C   1 
ATOM   5952  O O   . VAL C 2 115 ? -43.247 15.432  25.090  1.00 29.72  ? 115 VAL B O   1 
ATOM   5953  C CB  . VAL C 2 115 ? -41.187 17.336  26.849  1.00 33.03  ? 115 VAL B CB  1 
ATOM   5954  C CG1 . VAL C 2 115 ? -42.396 18.151  26.413  1.00 35.86  ? 115 VAL B CG1 1 
ATOM   5955  C CG2 . VAL C 2 115 ? -40.910 17.541  28.330  1.00 32.48  ? 115 VAL B CG2 1 
ATOM   5956  N N   . ARG C 2 116 ? -41.249 15.791  24.130  1.00 29.21  ? 116 ARG B N   1 
ATOM   5957  C CA  . ARG C 2 116 ? -41.722 15.608  22.769  1.00 29.86  ? 116 ARG B CA  1 
ATOM   5958  C C   . ARG C 2 116 ? -42.340 14.250  22.541  1.00 28.94  ? 116 ARG B C   1 
ATOM   5959  O O   . ARG C 2 116 ? -43.346 14.153  21.850  1.00 28.71  ? 116 ARG B O   1 
ATOM   5960  C CB  . ARG C 2 116 ? -40.530 15.700  21.841  1.00 35.79  ? 116 ARG B CB  1 
ATOM   5961  C CG  . ARG C 2 116 ? -40.800 15.550  20.353  1.00 41.32  ? 116 ARG B CG  1 
ATOM   5962  C CD  . ARG C 2 116 ? -39.501 15.313  19.591  1.00 49.07  ? 116 ARG B CD  1 
ATOM   5963  N NE  . ARG C 2 116 ? -39.679 15.259  18.144  1.00 55.02  ? 116 ARG B NE  1 
ATOM   5964  C CZ  . ARG C 2 116 ? -38.669 15.283  17.279  1.00 55.22  ? 116 ARG B CZ  1 
ATOM   5965  N NH1 . ARG C 2 116 ? -37.412 15.367  17.709  1.00 55.49  ? 116 ARG B NH1 1 
ATOM   5966  N NH2 . ARG C 2 116 ? -38.918 15.222  15.978  1.00 56.32  ? 116 ARG B NH2 1 
ATOM   5967  N N   . ASN C 2 117 ? -41.700 13.202  23.059  1.00 29.81  ? 117 ASN B N   1 
ATOM   5968  C CA  . ASN C 2 117 ? -42.237 11.843  22.913  1.00 31.32  ? 117 ASN B CA  1 
ATOM   5969  C C   . ASN C 2 117 ? -43.581 11.714  23.600  1.00 31.28  ? 117 ASN B C   1 
ATOM   5970  O O   . ASN C 2 117 ? -44.495 11.074  23.080  1.00 32.57  ? 117 ASN B O   1 
ATOM   5971  C CB  . ASN C 2 117 ? -41.268 10.781  23.439  1.00 34.71  ? 117 ASN B CB  1 
ATOM   5972  C CG  . ASN C 2 117 ? -40.225 10.389  22.407  1.00 41.09  ? 117 ASN B CG  1 
ATOM   5973  O OD1 . ASN C 2 117 ? -39.028 10.350  22.705  1.00 44.59  ? 117 ASN B OD1 1 
ATOM   5974  N ND2 . ASN C 2 117 ? -40.684 10.077  21.183  1.00 43.43  ? 117 ASN B ND2 1 
ATOM   5975  N N   . LEU C 2 118 ? -43.696 12.351  24.761  1.00 30.46  ? 118 LEU B N   1 
ATOM   5976  C CA  . LEU C 2 118 ? -44.937 12.355  25.514  1.00 27.92  ? 118 LEU B CA  1 
ATOM   5977  C C   . LEU C 2 118 ? -46.031 13.090  24.729  1.00 27.71  ? 118 LEU B C   1 
ATOM   5978  O O   . LEU C 2 118 ? -47.185 12.663  24.703  1.00 28.41  ? 118 LEU B O   1 
ATOM   5979  C CB  . LEU C 2 118 ? -44.704 13.010  26.876  1.00 28.63  ? 118 LEU B CB  1 
ATOM   5980  C CG  . LEU C 2 118 ? -45.403 12.356  28.053  1.00 30.03  ? 118 LEU B CG  1 
ATOM   5981  C CD1 . LEU C 2 118 ? -44.950 10.910  28.194  1.00 29.21  ? 118 LEU B CD1 1 
ATOM   5982  C CD2 . LEU C 2 118 ? -45.057 13.142  29.307  1.00 30.29  ? 118 LEU B CD2 1 
ATOM   5983  N N   . TYR C 2 119 ? -45.653 14.186  24.077  1.00 26.19  ? 119 TYR B N   1 
ATOM   5984  C CA  . TYR C 2 119 ? -46.575 14.963  23.263  1.00 26.70  ? 119 TYR B CA  1 
ATOM   5985  C C   . TYR C 2 119 ? -47.047 14.200  22.028  1.00 29.47  ? 119 TYR B C   1 
ATOM   5986  O O   . TYR C 2 119 ? -48.212 14.302  21.639  1.00 30.18  ? 119 TYR B O   1 
ATOM   5987  C CB  . TYR C 2 119 ? -45.911 16.268  22.829  1.00 26.52  ? 119 TYR B CB  1 
ATOM   5988  C CG  . TYR C 2 119 ? -46.790 17.158  21.990  1.00 26.79  ? 119 TYR B CG  1 
ATOM   5989  C CD1 . TYR C 2 119 ? -47.722 18.009  22.581  1.00 27.33  ? 119 TYR B CD1 1 
ATOM   5990  C CD2 . TYR C 2 119 ? -46.693 17.152  20.603  1.00 28.35  ? 119 TYR B CD2 1 
ATOM   5991  C CE1 . TYR C 2 119 ? -48.533 18.830  21.816  1.00 27.91  ? 119 TYR B CE1 1 
ATOM   5992  C CE2 . TYR C 2 119 ? -47.506 17.966  19.832  1.00 29.17  ? 119 TYR B CE2 1 
ATOM   5993  C CZ  . TYR C 2 119 ? -48.420 18.803  20.444  1.00 27.85  ? 119 TYR B CZ  1 
ATOM   5994  O OH  . TYR C 2 119 ? -49.219 19.614  19.682  1.00 31.14  ? 119 TYR B OH  1 
ATOM   5995  N N   . ASP C 2 120 ? -46.144 13.449  21.407  1.00 31.02  ? 120 ASP B N   1 
ATOM   5996  C CA  . ASP C 2 120 ? -46.486 12.693  20.202  1.00 32.56  ? 120 ASP B CA  1 
ATOM   5997  C C   . ASP C 2 120 ? -47.385 11.491  20.510  1.00 31.89  ? 120 ASP B C   1 
ATOM   5998  O O   . ASP C 2 120 ? -48.285 11.177  19.728  1.00 29.62  ? 120 ASP B O   1 
ATOM   5999  C CB  . ASP C 2 120 ? -45.219 12.261  19.449  1.00 32.91  ? 120 ASP B CB  1 
ATOM   6000  C CG  . ASP C 2 120 ? -44.560 13.421  18.696  1.00 36.06  ? 120 ASP B CG  1 
ATOM   6001  O OD1 . ASP C 2 120 ? -45.281 14.192  18.017  1.00 35.87  ? 120 ASP B OD1 1 
ATOM   6002  O OD2 . ASP C 2 120 ? -43.317 13.559  18.778  1.00 37.92  ? 120 ASP B OD2 1 
ATOM   6003  N N   . LYS C 2 121 ? -47.146 10.829  21.643  1.00 34.02  ? 121 LYS B N   1 
ATOM   6004  C CA  . LYS C 2 121 ? -48.011 9.731   22.096  1.00 36.19  ? 121 LYS B CA  1 
ATOM   6005  C C   . LYS C 2 121 ? -49.468 10.187  22.253  1.00 33.39  ? 121 LYS B C   1 
ATOM   6006  O O   . LYS C 2 121 ? -50.403 9.439   21.944  1.00 33.82  ? 121 LYS B O   1 
ATOM   6007  C CB  . LYS C 2 121 ? -47.486 9.138   23.409  1.00 43.31  ? 121 LYS B CB  1 
ATOM   6008  C CG  . LYS C 2 121 ? -46.355 8.135   23.226  1.00 53.98  ? 121 LYS B CG  1 
ATOM   6009  C CD  . LYS C 2 121 ? -45.899 7.545   24.554  1.00 60.74  ? 121 LYS B CD  1 
ATOM   6010  C CE  . LYS C 2 121 ? -44.866 6.442   24.346  1.00 65.65  ? 121 LYS B CE  1 
ATOM   6011  N NZ  . LYS C 2 121 ? -45.390 5.282   23.571  1.00 67.35  ? 121 LYS B NZ  1 
ATOM   6012  N N   . VAL C 2 122 ? -49.650 11.422  22.708  1.00 27.98  ? 122 VAL B N   1 
ATOM   6013  C CA  . VAL C 2 122 ? -50.976 12.018  22.795  1.00 27.66  ? 122 VAL B CA  1 
ATOM   6014  C C   . VAL C 2 122 ? -51.520 12.382  21.407  1.00 28.55  ? 122 VAL B C   1 
ATOM   6015  O O   . VAL C 2 122 ? -52.637 12.002  21.058  1.00 28.56  ? 122 VAL B O   1 
ATOM   6016  C CB  . VAL C 2 122 ? -50.964 13.259  23.707  1.00 27.56  ? 122 VAL B CB  1 
ATOM   6017  C CG1 . VAL C 2 122 ? -52.235 14.077  23.532  1.00 24.65  ? 122 VAL B CG1 1 
ATOM   6018  C CG2 . VAL C 2 122 ? -50.795 12.831  25.160  1.00 26.72  ? 122 VAL B CG2 1 
ATOM   6019  N N   . ARG C 2 123 ? -50.720 13.093  20.620  1.00 28.29  ? 123 ARG B N   1 
ATOM   6020  C CA  . ARG C 2 123 ? -51.131 13.514  19.284  1.00 27.71  ? 123 ARG B CA  1 
ATOM   6021  C C   . ARG C 2 123 ? -51.642 12.359  18.420  1.00 26.76  ? 123 ARG B C   1 
ATOM   6022  O O   . ARG C 2 123 ? -52.697 12.464  17.795  1.00 23.91  ? 123 ARG B O   1 
ATOM   6023  C CB  . ARG C 2 123 ? -49.979 14.228  18.573  1.00 20.00  ? 123 ARG B CB  1 
ATOM   6024  C CG  . ARG C 2 123 ? -50.409 15.430  17.748  1.00 20.00  ? 123 ARG B CG  1 
ATOM   6025  C CD  . ARG C 2 123 ? -49.516 15.613  16.532  1.00 20.00  ? 123 ARG B CD  1 
ATOM   6026  N NE  . ARG C 2 123 ? -49.401 14.387  15.748  1.00 20.00  ? 123 ARG B NE  1 
ATOM   6027  C CZ  . ARG C 2 123 ? -48.248 13.848  15.368  1.00 20.00  ? 123 ARG B CZ  1 
ATOM   6028  N NH1 . ARG C 2 123 ? -47.102 14.428  15.699  1.00 20.00  ? 123 ARG B NH1 1 
ATOM   6029  N NH2 . ARG C 2 123 ? -48.239 12.730  14.656  1.00 20.00  ? 123 ARG B NH2 1 
ATOM   6030  N N   . LEU C 2 124 ? -50.888 11.264  18.382  1.00 27.34  ? 124 LEU B N   1 
ATOM   6031  C CA  . LEU C 2 124 ? -51.224 10.123  17.521  1.00 29.74  ? 124 LEU B CA  1 
ATOM   6032  C C   . LEU C 2 124 ? -52.502 9.396   17.958  1.00 30.28  ? 124 LEU B C   1 
ATOM   6033  O O   . LEU C 2 124 ? -53.076 8.626   17.179  1.00 33.00  ? 124 LEU B O   1 
ATOM   6034  C CB  . LEU C 2 124 ? -50.051 9.132   17.422  1.00 30.55  ? 124 LEU B CB  1 
ATOM   6035  C CG  . LEU C 2 124 ? -48.968 9.369   16.363  1.00 35.64  ? 124 LEU B CG  1 
ATOM   6036  C CD1 . LEU C 2 124 ? -48.238 10.689  16.562  1.00 39.60  ? 124 LEU B CD1 1 
ATOM   6037  C CD2 . LEU C 2 124 ? -47.979 8.214   16.369  1.00 38.69  ? 124 LEU B CD2 1 
ATOM   6038  N N   . GLN C 2 125 ? -52.940 9.625   19.193  1.00 29.31  ? 125 GLN B N   1 
ATOM   6039  C CA  . GLN C 2 125 ? -54.210 9.072   19.659  1.00 29.19  ? 125 GLN B CA  1 
ATOM   6040  C C   . GLN C 2 125 ? -55.378 9.964   19.234  1.00 29.05  ? 125 GLN B C   1 
ATOM   6041  O O   . GLN C 2 125 ? -56.351 9.511   18.612  1.00 27.27  ? 125 GLN B O   1 
ATOM   6042  C CB  . GLN C 2 125 ? -54.212 8.907   21.180  1.00 30.50  ? 125 GLN B CB  1 
ATOM   6043  C CG  . GLN C 2 125 ? -53.380 7.745   21.685  1.00 33.17  ? 125 GLN B CG  1 
ATOM   6044  C CD  . GLN C 2 125 ? -53.343 7.702   23.207  1.00 36.86  ? 125 GLN B CD  1 
ATOM   6045  O OE1 . GLN C 2 125 ? -54.000 6.869   23.835  1.00 42.64  ? 125 GLN B OE1 1 
ATOM   6046  N NE2 . GLN C 2 125 ? -52.604 8.630   23.807  1.00 34.10  ? 125 GLN B NE2 1 
ATOM   6047  N N   . LEU C 2 126 ? -55.275 11.240  19.574  1.00 26.07  ? 126 LEU B N   1 
ATOM   6048  C CA  . LEU C 2 126 ? -56.378 12.172  19.312  1.00 26.12  ? 126 LEU B CA  1 
ATOM   6049  C C   . LEU C 2 126 ? -56.664 12.497  17.848  1.00 24.73  ? 126 LEU B C   1 
ATOM   6050  O O   . LEU C 2 126 ? -57.785 12.863  17.523  1.00 24.47  ? 126 LEU B O   1 
ATOM   6051  C CB  . LEU C 2 126 ? -56.229 13.460  20.141  1.00 25.57  ? 126 LEU B CB  1 
ATOM   6052  C CG  . LEU C 2 126 ? -55.797 13.381  21.614  1.00 24.56  ? 126 LEU B CG  1 
ATOM   6053  C CD1 . LEU C 2 126 ? -55.647 14.758  22.237  1.00 23.65  ? 126 LEU B CD1 1 
ATOM   6054  C CD2 . LEU C 2 126 ? -56.810 12.550  22.387  1.00 23.05  ? 126 LEU B CD2 1 
ATOM   6055  N N   . LYS C 2 127 ? -55.721 12.316  16.962  1.00 26.19  ? 127 LYS B N   1 
ATOM   6056  C CA  . LYS C 2 127 ? -55.953 12.655  15.584  1.00 27.44  ? 127 LYS B CA  1 
ATOM   6057  C C   . LYS C 2 127 ? -56.775 13.901  15.427  1.00 27.41  ? 127 LYS B C   1 
ATOM   6058  O O   . LYS C 2 127 ? -56.433 14.909  15.951  1.00 26.77  ? 127 LYS B O   1 
ATOM   6059  C CB  . LYS C 2 127 ? -56.612 11.511  14.883  1.00 20.00  ? 127 LYS B CB  1 
ATOM   6060  C CG  . LYS C 2 127 ? -55.917 10.206  15.107  1.00 20.00  ? 127 LYS B CG  1 
ATOM   6061  C CD  . LYS C 2 127 ? -56.530 9.131   14.254  1.00 20.00  ? 127 LYS B CD  1 
ATOM   6062  C CE  . LYS C 2 127 ? -56.332 7.765   14.860  1.00 20.00  ? 127 LYS B CE  1 
ATOM   6063  N NZ  . LYS C 2 127 ? -57.298 6.802   14.292  1.00 20.00  ? 127 LYS B NZ  1 
ATOM   6064  N N   . ASP C 2 128 ? -57.856 13.837  14.664  1.00 30.41  ? 128 ASP B N   1 
ATOM   6065  C CA  . ASP C 2 128 ? -58.686 15.018  14.359  1.00 31.64  ? 128 ASP B CA  1 
ATOM   6066  C C   . ASP C 2 128 ? -59.804 15.219  15.402  1.00 30.37  ? 128 ASP B C   1 
ATOM   6067  O O   . ASP C 2 128 ? -60.675 16.071  15.228  1.00 30.16  ? 128 ASP B O   1 
ATOM   6068  C CB  . ASP C 2 128 ? -59.268 14.958  12.930  1.00 33.15  ? 128 ASP B CB  1 
ATOM   6069  C CG  . ASP C 2 128 ? -60.015 13.674  12.651  1.00 36.05  ? 128 ASP B CG  1 
ATOM   6070  O OD1 . ASP C 2 128 ? -60.387 12.981  13.624  1.00 38.76  ? 128 ASP B OD1 1 
ATOM   6071  O OD2 . ASP C 2 128 ? -60.231 13.366  11.459  1.00 41.06  ? 128 ASP B OD2 1 
ATOM   6072  N N   . ASN C 2 129 ? -59.789 14.430  16.473  1.00 29.41  ? 129 ASN B N   1 
ATOM   6073  C CA  . ASN C 2 129 ? -60.726 14.627  17.583  1.00 30.74  ? 129 ASN B CA  1 
ATOM   6074  C C   . ASN C 2 129 ? -60.308 15.770  18.506  1.00 30.17  ? 129 ASN B C   1 
ATOM   6075  O O   . ASN C 2 129 ? -61.077 16.167  19.375  1.00 29.62  ? 129 ASN B O   1 
ATOM   6076  C CB  . ASN C 2 129 ? -60.906 13.335  18.392  1.00 32.29  ? 129 ASN B CB  1 
ATOM   6077  C CG  . ASN C 2 129 ? -61.800 12.325  17.693  1.00 33.07  ? 129 ASN B CG  1 
ATOM   6078  O OD1 . ASN C 2 129 ? -62.186 12.508  16.540  1.00 32.26  ? 129 ASN B OD1 1 
ATOM   6079  N ND2 . ASN C 2 129 ? -62.131 11.247  18.393  1.00 34.41  ? 129 ASN B ND2 1 
ATOM   6080  N N   . ALA C 2 130 ? -59.094 16.293  18.328  1.00 31.42  ? 130 ALA B N   1 
ATOM   6081  C CA  . ALA C 2 130 ? -58.670 17.481  19.067  1.00 32.96  ? 130 ALA B CA  1 
ATOM   6082  C C   . ALA C 2 130 ? -57.751 18.387  18.245  1.00 33.35  ? 130 ALA B C   1 
ATOM   6083  O O   . ALA C 2 130 ? -57.050 17.937  17.339  1.00 32.15  ? 130 ALA B O   1 
ATOM   6084  C CB  . ALA C 2 130 ? -58.003 17.086  20.376  1.00 30.46  ? 130 ALA B CB  1 
ATOM   6085  N N   . LYS C 2 131 ? -57.771 19.669  18.594  1.00 36.73  ? 131 LYS B N   1 
ATOM   6086  C CA  . LYS C 2 131 ? -57.027 20.707  17.886  1.00 37.99  ? 131 LYS B CA  1 
ATOM   6087  C C   . LYS C 2 131 ? -55.702 20.989  18.581  1.00 39.56  ? 131 LYS B C   1 
ATOM   6088  O O   . LYS C 2 131 ? -55.703 21.434  19.727  1.00 38.58  ? 131 LYS B O   1 
ATOM   6089  C CB  . LYS C 2 131 ? -57.840 22.007  17.860  1.00 40.73  ? 131 LYS B CB  1 
ATOM   6090  C CG  . LYS C 2 131 ? -57.054 23.219  17.321  1.00 43.98  ? 131 LYS B CG  1 
ATOM   6091  C CD  . LYS C 2 131 ? -57.890 24.135  16.417  1.00 44.70  ? 131 LYS B CD  1 
ATOM   6092  C CE  . LYS C 2 131 ? -58.065 25.525  17.016  1.00 45.07  ? 131 LYS B CE  1 
ATOM   6093  N NZ  . LYS C 2 131 ? -58.657 26.480  16.039  1.00 46.53  ? 131 LYS B NZ  1 
ATOM   6094  N N   . GLU C 2 132 ? -54.589 20.745  17.886  1.00 40.03  ? 132 GLU B N   1 
ATOM   6095  C CA  . GLU C 2 132 ? -53.264 21.107  18.387  1.00 38.04  ? 132 GLU B CA  1 
ATOM   6096  C C   . GLU C 2 132 ? -53.141 22.619  18.515  1.00 39.22  ? 132 GLU B C   1 
ATOM   6097  O O   . GLU C 2 132 ? -53.052 23.342  17.527  1.00 40.14  ? 132 GLU B O   1 
ATOM   6098  C CB  . GLU C 2 132 ? -52.154 20.571  17.476  1.00 39.83  ? 132 GLU B CB  1 
ATOM   6099  C CG  . GLU C 2 132 ? -51.824 19.109  17.709  1.00 43.13  ? 132 GLU B CG  1 
ATOM   6100  C CD  . GLU C 2 132 ? -50.850 18.557  16.685  1.00 45.34  ? 132 GLU B CD  1 
ATOM   6101  O OE1 . GLU C 2 132 ? -49.657 18.382  17.020  1.00 42.67  ? 132 GLU B OE1 1 
ATOM   6102  O OE2 . GLU C 2 132 ? -51.283 18.298  15.540  1.00 46.66  ? 132 GLU B OE2 1 
ATOM   6103  N N   . LEU C 2 133 ? -53.141 23.102  19.746  1.00 43.36  ? 133 LEU B N   1 
ATOM   6104  C CA  . LEU C 2 133 ? -53.045 24.540  19.979  1.00 43.92  ? 133 LEU B CA  1 
ATOM   6105  C C   . LEU C 2 133 ? -51.657 25.118  19.710  1.00 41.66  ? 133 LEU B C   1 
ATOM   6106  O O   . LEU C 2 133 ? -51.524 26.326  19.638  1.00 45.43  ? 133 LEU B O   1 
ATOM   6107  C CB  . LEU C 2 133 ? -53.501 24.886  21.401  1.00 43.21  ? 133 LEU B CB  1 
ATOM   6108  C CG  . LEU C 2 133 ? -55.011 24.772  21.654  1.00 39.07  ? 133 LEU B CG  1 
ATOM   6109  C CD1 . LEU C 2 133 ? -55.345 25.166  23.083  1.00 37.84  ? 133 LEU B CD1 1 
ATOM   6110  C CD2 . LEU C 2 133 ? -55.803 25.615  20.667  1.00 40.44  ? 133 LEU B CD2 1 
ATOM   6111  N N   . GLY C 2 134 ? -50.641 24.274  19.542  1.00 40.16  ? 134 GLY B N   1 
ATOM   6112  C CA  . GLY C 2 134 ? -49.298 24.746  19.177  1.00 37.89  ? 134 GLY B CA  1 
ATOM   6113  C C   . GLY C 2 134 ? -48.416 25.154  20.350  1.00 38.38  ? 134 GLY B C   1 
ATOM   6114  O O   . GLY C 2 134 ? -47.310 25.650  20.148  1.00 38.36  ? 134 GLY B O   1 
ATOM   6115  N N   . ASN C 2 135 ? -48.904 24.947  21.571  1.00 38.09  ? 135 ASN B N   1 
ATOM   6116  C CA  . ASN C 2 135 ? -48.156 25.271  22.794  1.00 38.50  ? 135 ASN B CA  1 
ATOM   6117  C C   . ASN C 2 135 ? -47.989 24.074  23.738  1.00 37.94  ? 135 ASN B C   1 
ATOM   6118  O O   . ASN C 2 135 ? -47.727 24.244  24.929  1.00 38.78  ? 135 ASN B O   1 
ATOM   6119  C CB  . ASN C 2 135 ? -48.826 26.429  23.541  1.00 39.75  ? 135 ASN B CB  1 
ATOM   6120  C CG  . ASN C 2 135 ? -50.261 26.119  23.947  1.00 43.67  ? 135 ASN B CG  1 
ATOM   6121  O OD1 . ASN C 2 135 ? -50.962 25.374  23.273  1.00 44.05  ? 135 ASN B OD1 1 
ATOM   6122  N ND2 . ASN C 2 135 ? -50.694 26.683  25.069  1.00 47.31  ? 135 ASN B ND2 1 
ATOM   6123  N N   . GLY C 2 136 ? -48.132 22.870  23.195  1.00 35.89  ? 136 GLY B N   1 
ATOM   6124  C CA  . GLY C 2 136 ? -48.104 21.644  23.990  1.00 34.08  ? 136 GLY B CA  1 
ATOM   6125  C C   . GLY C 2 136 ? -49.473 21.169  24.467  1.00 34.62  ? 136 GLY B C   1 
ATOM   6126  O O   . GLY C 2 136 ? -49.576 20.119  25.099  1.00 32.07  ? 136 GLY B O   1 
ATOM   6127  N N   . CYS C 2 137 ? -50.521 21.936  24.160  1.00 36.25  ? 137 CYS B N   1 
ATOM   6128  C CA  . CYS C 2 137 ? -51.884 21.629  24.600  1.00 38.53  ? 137 CYS B CA  1 
ATOM   6129  C C   . CYS C 2 137 ? -52.789 21.211  23.447  1.00 38.31  ? 137 CYS B C   1 
ATOM   6130  O O   . CYS C 2 137 ? -52.633 21.675  22.318  1.00 38.18  ? 137 CYS B O   1 
ATOM   6131  C CB  . CYS C 2 137 ? -52.507 22.835  25.300  1.00 44.89  ? 137 CYS B CB  1 
ATOM   6132  S SG  . CYS C 2 137 ? -51.628 23.338  26.795  1.00 55.14  ? 137 CYS B SG  1 
ATOM   6133  N N   . PHE C 2 138 ? -53.733 20.326  23.748  1.00 34.61  ? 138 PHE B N   1 
ATOM   6134  C CA  . PHE C 2 138 ? -54.741 19.896  22.791  1.00 33.32  ? 138 PHE B CA  1 
ATOM   6135  C C   . PHE C 2 138 ? -56.103 20.363  23.274  1.00 32.28  ? 138 PHE B C   1 
ATOM   6136  O O   . PHE C 2 138 ? -56.463 20.112  24.423  1.00 29.25  ? 138 PHE B O   1 
ATOM   6137  C CB  . PHE C 2 138 ? -54.751 18.374  22.688  1.00 32.19  ? 138 PHE B CB  1 
ATOM   6138  C CG  . PHE C 2 138 ? -53.460 17.786  22.201  1.00 32.78  ? 138 PHE B CG  1 
ATOM   6139  C CD1 . PHE C 2 138 ? -52.421 17.532  23.085  1.00 32.54  ? 138 PHE B CD1 1 
ATOM   6140  C CD2 . PHE C 2 138 ? -53.287 17.466  20.860  1.00 31.70  ? 138 PHE B CD2 1 
ATOM   6141  C CE1 . PHE C 2 138 ? -51.232 16.980  22.639  1.00 33.74  ? 138 PHE B CE1 1 
ATOM   6142  C CE2 . PHE C 2 138 ? -52.101 16.913  20.409  1.00 30.76  ? 138 PHE B CE2 1 
ATOM   6143  C CZ  . PHE C 2 138 ? -51.072 16.668  21.300  1.00 32.52  ? 138 PHE B CZ  1 
ATOM   6144  N N   . GLU C 2 139 ? -56.850 21.048  22.411  1.00 33.40  ? 139 GLU B N   1 
ATOM   6145  C CA  . GLU C 2 139 ? -58.249 21.372  22.696  1.00 36.96  ? 139 GLU B CA  1 
ATOM   6146  C C   . GLU C 2 139 ? -59.133 20.297  22.091  1.00 32.38  ? 139 GLU B C   1 
ATOM   6147  O O   . GLU C 2 139 ? -59.101 20.077  20.885  1.00 33.12  ? 139 GLU B O   1 
ATOM   6148  C CB  . GLU C 2 139 ? -58.628 22.749  22.137  1.00 43.38  ? 139 GLU B CB  1 
ATOM   6149  C CG  . GLU C 2 139 ? -60.036 23.214  22.512  1.00 49.45  ? 139 GLU B CG  1 
ATOM   6150  C CD  . GLU C 2 139 ? -60.393 24.596  21.974  1.00 54.98  ? 139 GLU B CD  1 
ATOM   6151  O OE1 . GLU C 2 139 ? -59.583 25.197  21.229  1.00 59.40  ? 139 GLU B OE1 1 
ATOM   6152  O OE2 . GLU C 2 139 ? -61.501 25.085  22.297  1.00 57.14  ? 139 GLU B OE2 1 
ATOM   6153  N N   . PHE C 2 140 ? -59.914 19.626  22.932  1.00 31.65  ? 140 PHE B N   1 
ATOM   6154  C CA  . PHE C 2 140 ? -60.807 18.570  22.468  1.00 33.51  ? 140 PHE B CA  1 
ATOM   6155  C C   . PHE C 2 140 ? -62.025 19.134  21.742  1.00 35.02  ? 140 PHE B C   1 
ATOM   6156  O O   . PHE C 2 140 ? -62.562 20.168  22.135  1.00 33.10  ? 140 PHE B O   1 
ATOM   6157  C CB  . PHE C 2 140 ? -61.286 17.713  23.639  1.00 32.91  ? 140 PHE B CB  1 
ATOM   6158  C CG  . PHE C 2 140 ? -60.256 16.757  24.150  1.00 30.85  ? 140 PHE B CG  1 
ATOM   6159  C CD1 . PHE C 2 140 ? -59.413 17.116  25.188  1.00 32.30  ? 140 PHE B CD1 1 
ATOM   6160  C CD2 . PHE C 2 140 ? -60.138 15.494  23.601  1.00 29.17  ? 140 PHE B CD2 1 
ATOM   6161  C CE1 . PHE C 2 140 ? -58.464 16.231  25.664  1.00 31.94  ? 140 PHE B CE1 1 
ATOM   6162  C CE2 . PHE C 2 140 ? -59.193 14.605  24.069  1.00 30.42  ? 140 PHE B CE2 1 
ATOM   6163  C CZ  . PHE C 2 140 ? -58.351 14.974  25.101  1.00 31.27  ? 140 PHE B CZ  1 
ATOM   6164  N N   . TYR C 2 141 ? -62.456 18.433  20.693  1.00 36.85  ? 141 TYR B N   1 
ATOM   6165  C CA  . TYR C 2 141 ? -63.677 18.770  19.959  1.00 35.38  ? 141 TYR B CA  1 
ATOM   6166  C C   . TYR C 2 141 ? -64.902 18.077  20.555  1.00 36.82  ? 141 TYR B C   1 
ATOM   6167  O O   . TYR C 2 141 ? -66.017 18.277  20.082  1.00 41.54  ? 141 TYR B O   1 
ATOM   6168  C CB  . TYR C 2 141 ? -63.553 18.380  18.483  1.00 33.24  ? 141 TYR B CB  1 
ATOM   6169  C CG  . TYR C 2 141 ? -62.625 19.245  17.657  1.00 31.83  ? 141 TYR B CG  1 
ATOM   6170  C CD1 . TYR C 2 141 ? -62.747 20.632  17.649  1.00 32.94  ? 141 TYR B CD1 1 
ATOM   6171  C CD2 . TYR C 2 141 ? -61.656 18.670  16.844  1.00 32.28  ? 141 TYR B CD2 1 
ATOM   6172  C CE1 . TYR C 2 141 ? -61.911 21.422  16.876  1.00 33.44  ? 141 TYR B CE1 1 
ATOM   6173  C CE2 . TYR C 2 141 ? -60.812 19.445  16.068  1.00 33.54  ? 141 TYR B CE2 1 
ATOM   6174  C CZ  . TYR C 2 141 ? -60.946 20.820  16.085  1.00 34.60  ? 141 TYR B CZ  1 
ATOM   6175  O OH  . TYR C 2 141 ? -60.110 21.581  15.309  1.00 36.51  ? 141 TYR B OH  1 
ATOM   6176  N N   . HIS C 2 142 ? -64.698 17.259  21.582  1.00 37.64  ? 142 HIS B N   1 
ATOM   6177  C CA  . HIS C 2 142 ? -65.804 16.621  22.289  1.00 39.00  ? 142 HIS B CA  1 
ATOM   6178  C C   . HIS C 2 142 ? -65.618 16.739  23.773  1.00 39.43  ? 142 HIS B C   1 
ATOM   6179  O O   . HIS C 2 142 ? -64.584 17.202  24.244  1.00 42.65  ? 142 HIS B O   1 
ATOM   6180  C CB  . HIS C 2 142 ? -65.904 15.154  21.892  1.00 40.93  ? 142 HIS B CB  1 
ATOM   6181  C CG  . HIS C 2 142 ? -64.733 14.326  22.342  1.00 41.36  ? 142 HIS B CG  1 
ATOM   6182  N ND1 . HIS C 2 142 ? -63.593 14.249  21.640  1.00 42.90  ? 142 HIS B ND1 1 
ATOM   6183  C CD2 . HIS C 2 142 ? -64.550 13.545  23.478  1.00 42.06  ? 142 HIS B CD2 1 
ATOM   6184  C CE1 . HIS C 2 142 ? -62.725 13.453  22.287  1.00 43.11  ? 142 HIS B CE1 1 
ATOM   6185  N NE2 . HIS C 2 142 ? -63.313 13.020  23.410  1.00 43.72  ? 142 HIS B NE2 1 
ATOM   6186  N N   . LYS C 2 143 ? -66.636 16.329  24.519  1.00 41.49  ? 143 LYS B N   1 
ATOM   6187  C CA  . LYS C 2 143 ? -66.604 16.338  25.971  1.00 45.43  ? 143 LYS B CA  1 
ATOM   6188  C C   . LYS C 2 143 ? -65.754 15.172  26.488  1.00 43.14  ? 143 LYS B C   1 
ATOM   6189  O O   . LYS C 2 143 ? -66.123 14.010  26.342  1.00 42.17  ? 143 LYS B O   1 
ATOM   6190  C CB  . LYS C 2 143 ? -68.047 16.225  26.481  1.00 48.96  ? 143 LYS B CB  1 
ATOM   6191  C CG  . LYS C 2 143 ? -68.249 16.372  27.981  1.00 55.42  ? 143 LYS B CG  1 
ATOM   6192  C CD  . LYS C 2 143 ? -69.695 16.115  28.374  1.00 60.29  ? 143 LYS B CD  1 
ATOM   6193  C CE  . LYS C 2 143 ? -69.835 15.957  29.878  1.00 67.72  ? 143 LYS B CE  1 
ATOM   6194  N NZ  . LYS C 2 143 ? -71.246 15.696  30.283  1.00 73.17  ? 143 LYS B NZ  1 
ATOM   6195  N N   . CYS C 2 144 ? -64.612 15.496  27.087  1.00 42.02  ? 144 CYS B N   1 
ATOM   6196  C CA  . CYS C 2 144 ? -63.683 14.487  27.588  1.00 41.52  ? 144 CYS B CA  1 
ATOM   6197  C C   . CYS C 2 144 ? -63.667 14.520  29.111  1.00 39.34  ? 144 CYS B C   1 
ATOM   6198  O O   . CYS C 2 144 ? -63.090 15.426  29.714  1.00 39.15  ? 144 CYS B O   1 
ATOM   6199  C CB  . CYS C 2 144 ? -62.280 14.729  27.016  1.00 42.77  ? 144 CYS B CB  1 
ATOM   6200  S SG  . CYS C 2 144 ? -61.055 13.468  27.446  1.00 44.00  ? 144 CYS B SG  1 
ATOM   6201  N N   . ASP C 2 145 ? -64.318 13.533  29.724  1.00 41.08  ? 145 ASP B N   1 
ATOM   6202  C CA  . ASP C 2 145 ? -64.418 13.440  31.186  1.00 41.68  ? 145 ASP B CA  1 
ATOM   6203  C C   . ASP C 2 145 ? -63.160 12.814  31.802  1.00 39.29  ? 145 ASP B C   1 
ATOM   6204  O O   . ASP C 2 145 ? -62.219 12.476  31.092  1.00 40.40  ? 145 ASP B O   1 
ATOM   6205  C CB  . ASP C 2 145 ? -65.699 12.681  31.597  1.00 40.93  ? 145 ASP B CB  1 
ATOM   6206  C CG  . ASP C 2 145 ? -65.668 11.202  31.245  1.00 41.21  ? 145 ASP B CG  1 
ATOM   6207  O OD1 . ASP C 2 145 ? -66.674 10.505  31.515  1.00 45.34  ? 145 ASP B OD1 1 
ATOM   6208  O OD2 . ASP C 2 145 ? -64.651 10.730  30.710  1.00 39.42  ? 145 ASP B OD2 1 
ATOM   6209  N N   . ASN C 2 146 ? -63.162 12.645  33.120  1.00 38.31  ? 146 ASN B N   1 
ATOM   6210  C CA  . ASN C 2 146 ? -62.001 12.126  33.841  1.00 36.45  ? 146 ASN B CA  1 
ATOM   6211  C C   . ASN C 2 146 ? -61.595 10.717  33.432  1.00 36.61  ? 146 ASN B C   1 
ATOM   6212  O O   . ASN C 2 146 ? -60.421 10.365  33.524  1.00 42.20  ? 146 ASN B O   1 
ATOM   6213  C CB  . ASN C 2 146 ? -62.238 12.182  35.352  1.00 35.13  ? 146 ASN B CB  1 
ATOM   6214  C CG  . ASN C 2 146 ? -62.328 13.606  35.871  1.00 37.00  ? 146 ASN B CG  1 
ATOM   6215  O OD1 . ASN C 2 146 ? -61.958 14.555  35.181  1.00 34.61  ? 146 ASN B OD1 1 
ATOM   6216  N ND2 . ASN C 2 146 ? -62.845 13.763  37.085  1.00 41.41  ? 146 ASN B ND2 1 
ATOM   6217  N N   . GLU C 2 147 ? -62.554 9.917   32.979  1.00 38.77  ? 147 GLU B N   1 
ATOM   6218  C CA  . GLU C 2 147 ? -62.237 8.598   32.441  1.00 44.97  ? 147 GLU B CA  1 
ATOM   6219  C C   . GLU C 2 147 ? -61.593 8.747   31.069  1.00 41.37  ? 147 GLU B C   1 
ATOM   6220  O O   . GLU C 2 147 ? -60.620 8.067   30.763  1.00 42.73  ? 147 GLU B O   1 
ATOM   6221  C CB  . GLU C 2 147 ? -63.475 7.711   32.368  1.00 53.25  ? 147 GLU B CB  1 
ATOM   6222  C CG  . GLU C 2 147 ? -64.027 7.312   33.727  1.00 62.48  ? 147 GLU B CG  1 
ATOM   6223  C CD  . GLU C 2 147 ? -65.293 6.484   33.627  1.00 76.10  ? 147 GLU B CD  1 
ATOM   6224  O OE1 . GLU C 2 147 ? -65.531 5.850   32.573  1.00 88.65  ? 147 GLU B OE1 1 
ATOM   6225  O OE2 . GLU C 2 147 ? -66.060 6.476   34.609  1.00 78.54  ? 147 GLU B OE2 1 
ATOM   6226  N N   . CYS C 2 148 ? -62.139 9.647   30.255  1.00 40.27  ? 148 CYS B N   1 
ATOM   6227  C CA  . CYS C 2 148 ? -61.599 9.934   28.931  1.00 40.26  ? 148 CYS B CA  1 
ATOM   6228  C C   . CYS C 2 148 ? -60.161 10.463  29.017  1.00 42.00  ? 148 CYS B C   1 
ATOM   6229  O O   . CYS C 2 148 ? -59.310 10.088  28.211  1.00 41.60  ? 148 CYS B O   1 
ATOM   6230  C CB  . CYS C 2 148 ? -62.513 10.927  28.199  1.00 41.92  ? 148 CYS B CB  1 
ATOM   6231  S SG  . CYS C 2 148 ? -61.819 11.720  26.731  1.00 47.79  ? 148 CYS B SG  1 
ATOM   6232  N N   . MET C 2 149 ? -59.898 11.329  29.994  1.00 38.14  ? 149 MET B N   1 
ATOM   6233  C CA  . MET C 2 149 ? -58.562 11.889  30.191  1.00 36.52  ? 149 MET B CA  1 
ATOM   6234  C C   . MET C 2 149 ? -57.554 10.813  30.601  1.00 39.41  ? 149 MET B C   1 
ATOM   6235  O O   . MET C 2 149 ? -56.418 10.810  30.124  1.00 37.61  ? 149 MET B O   1 
ATOM   6236  C CB  . MET C 2 149 ? -58.594 12.998  31.249  1.00 38.57  ? 149 MET B CB  1 
ATOM   6237  C CG  . MET C 2 149 ? -59.356 14.251  30.840  1.00 39.50  ? 149 MET B CG  1 
ATOM   6238  S SD  . MET C 2 149 ? -58.529 15.220  29.559  1.00 41.34  ? 149 MET B SD  1 
ATOM   6239  C CE  . MET C 2 149 ? -59.690 16.563  29.328  1.00 35.74  ? 149 MET B CE  1 
ATOM   6240  N N   . GLU C 2 150 ? -57.969 9.915   31.494  1.00 42.94  ? 150 GLU B N   1 
ATOM   6241  C CA  . GLU C 2 150 ? -57.122 8.803   31.933  1.00 43.48  ? 150 GLU B CA  1 
ATOM   6242  C C   . GLU C 2 150 ? -56.696 7.935   30.757  1.00 38.52  ? 150 GLU B C   1 
ATOM   6243  O O   . GLU C 2 150 ? -55.530 7.561   30.654  1.00 36.61  ? 150 GLU B O   1 
ATOM   6244  C CB  . GLU C 2 150 ? -57.850 7.937   32.964  1.00 53.21  ? 150 GLU B CB  1 
ATOM   6245  C CG  . GLU C 2 150 ? -57.921 8.549   34.357  1.00 67.30  ? 150 GLU B CG  1 
ATOM   6246  C CD  . GLU C 2 150 ? -59.023 7.956   35.231  1.00 79.05  ? 150 GLU B CD  1 
ATOM   6247  O OE1 . GLU C 2 150 ? -59.667 6.963   34.821  1.00 81.17  ? 150 GLU B OE1 1 
ATOM   6248  O OE2 . GLU C 2 150 ? -59.244 8.487   36.342  1.00 83.29  ? 150 GLU B OE2 1 
ATOM   6249  N N   . SER C 2 151 ? -57.641 7.627   29.871  1.00 36.41  ? 151 SER B N   1 
ATOM   6250  C CA  . SER C 2 151 ? -57.367 6.769   28.716  1.00 36.62  ? 151 SER B CA  1 
ATOM   6251  C C   . SER C 2 151 ? -56.325 7.374   27.773  1.00 34.63  ? 151 SER B C   1 
ATOM   6252  O O   . SER C 2 151 ? -55.600 6.640   27.104  1.00 32.27  ? 151 SER B O   1 
ATOM   6253  C CB  . SER C 2 151 ? -58.656 6.469   27.942  1.00 36.00  ? 151 SER B CB  1 
ATOM   6254  O OG  . SER C 2 151 ? -59.205 7.645   27.374  1.00 37.09  ? 151 SER B OG  1 
ATOM   6255  N N   . VAL C 2 152 ? -56.265 8.704   27.723  1.00 32.43  ? 152 VAL B N   1 
ATOM   6256  C CA  . VAL C 2 152 ? -55.272 9.410   26.917  1.00 36.23  ? 152 VAL B CA  1 
ATOM   6257  C C   . VAL C 2 152 ? -53.869 9.238   27.515  1.00 38.03  ? 152 VAL B C   1 
ATOM   6258  O O   . VAL C 2 152 ? -52.887 9.141   26.779  1.00 37.69  ? 152 VAL B O   1 
ATOM   6259  C CB  . VAL C 2 152 ? -55.609 10.913  26.793  1.00 36.60  ? 152 VAL B CB  1 
ATOM   6260  C CG1 . VAL C 2 152 ? -54.584 11.628  25.921  1.00 32.75  ? 152 VAL B CG1 1 
ATOM   6261  C CG2 . VAL C 2 152 ? -57.012 11.102  26.232  1.00 34.27  ? 152 VAL B CG2 1 
ATOM   6262  N N   . ARG C 2 153 ? -53.791 9.178   28.844  1.00 39.88  ? 153 ARG B N   1 
ATOM   6263  C CA  . ARG C 2 153 ? -52.531 8.905   29.548  1.00 40.92  ? 153 ARG B CA  1 
ATOM   6264  C C   . ARG C 2 153 ? -52.168 7.420   29.473  1.00 40.24  ? 153 ARG B C   1 
ATOM   6265  O O   . ARG C 2 153 ? -51.005 7.077   29.280  1.00 40.49  ? 153 ARG B O   1 
ATOM   6266  C CB  . ARG C 2 153 ? -52.620 9.331   31.018  1.00 41.26  ? 153 ARG B CB  1 
ATOM   6267  C CG  . ARG C 2 153 ? -53.056 10.771  31.236  1.00 39.94  ? 153 ARG B CG  1 
ATOM   6268  C CD  . ARG C 2 153 ? -52.989 11.164  32.703  1.00 41.19  ? 153 ARG B CD  1 
ATOM   6269  N NE  . ARG C 2 153 ? -54.091 12.059  33.063  1.00 46.52  ? 153 ARG B NE  1 
ATOM   6270  C CZ  . ARG C 2 153 ? -55.114 11.753  33.865  1.00 43.25  ? 153 ARG B CZ  1 
ATOM   6271  N NH1 . ARG C 2 153 ? -55.211 10.562  34.452  1.00 41.99  ? 153 ARG B NH1 1 
ATOM   6272  N NH2 . ARG C 2 153 ? -56.052 12.663  34.092  1.00 41.60  ? 153 ARG B NH2 1 
ATOM   6273  N N   . ASN C 2 154 ? -53.168 6.550   29.638  1.00 43.44  ? 154 ASN B N   1 
ATOM   6274  C CA  . ASN C 2 154 ? -52.997 5.097   29.496  1.00 42.43  ? 154 ASN B CA  1 
ATOM   6275  C C   . ASN C 2 154 ? -52.373 4.711   28.166  1.00 38.24  ? 154 ASN B C   1 
ATOM   6276  O O   . ASN C 2 154 ? -51.508 3.842   28.107  1.00 41.46  ? 154 ASN B O   1 
ATOM   6277  C CB  . ASN C 2 154 ? -54.352 4.375   29.553  1.00 49.95  ? 154 ASN B CB  1 
ATOM   6278  C CG  . ASN C 2 154 ? -54.946 4.314   30.944  1.00 58.02  ? 154 ASN B CG  1 
ATOM   6279  O OD1 . ASN C 2 154 ? -54.380 4.806   31.916  1.00 57.92  ? 154 ASN B OD1 1 
ATOM   6280  N ND2 . ASN C 2 154 ? -56.116 3.691   31.035  1.00 69.25  ? 154 ASN B ND2 1 
ATOM   6281  N N   . GLY C 2 155 ? -52.840 5.357   27.100  1.00 36.10  ? 155 GLY B N   1 
ATOM   6282  C CA  . GLY C 2 155 ? -52.581 4.914   25.737  1.00 35.95  ? 155 GLY B CA  1 
ATOM   6283  C C   . GLY C 2 155 ? -53.730 4.072   25.192  1.00 36.09  ? 155 GLY B C   1 
ATOM   6284  O O   . GLY C 2 155 ? -53.551 3.353   24.209  1.00 41.95  ? 155 GLY B O   1 
ATOM   6285  N N   . THR C 2 156 ? -54.905 4.172   25.819  1.00 34.20  ? 156 THR B N   1 
ATOM   6286  C CA  . THR C 2 156 ? -56.072 3.340   25.482  1.00 35.04  ? 156 THR B CA  1 
ATOM   6287  C C   . THR C 2 156 ? -57.255 4.165   24.968  1.00 34.19  ? 156 THR B C   1 
ATOM   6288  O O   . THR C 2 156 ? -58.374 3.661   24.887  1.00 30.10  ? 156 THR B O   1 
ATOM   6289  C CB  . THR C 2 156 ? -56.572 2.533   26.707  1.00 36.38  ? 156 THR B CB  1 
ATOM   6290  O OG1 . THR C 2 156 ? -56.945 3.431   27.759  1.00 37.66  ? 156 THR B OG1 1 
ATOM   6291  C CG2 . THR C 2 156 ? -55.490 1.581   27.212  1.00 35.95  ? 156 THR B CG2 1 
ATOM   6292  N N   . TYR C 2 157 ? -57.002 5.426   24.621  1.00 35.46  ? 157 TYR B N   1 
ATOM   6293  C CA  . TYR C 2 157 ? -58.055 6.342   24.181  1.00 31.40  ? 157 TYR B CA  1 
ATOM   6294  C C   . TYR C 2 157 ? -58.780 5.803   22.946  1.00 33.54  ? 157 TYR B C   1 
ATOM   6295  O O   . TYR C 2 157 ? -58.160 5.561   21.910  1.00 36.08  ? 157 TYR B O   1 
ATOM   6296  C CB  . TYR C 2 157 ? -57.449 7.723   23.905  1.00 30.46  ? 157 TYR B CB  1 
ATOM   6297  C CG  . TYR C 2 157 ? -58.346 8.698   23.170  1.00 28.70  ? 157 TYR B CG  1 
ATOM   6298  C CD1 . TYR C 2 157 ? -59.282 9.470   23.852  1.00 27.68  ? 157 TYR B CD1 1 
ATOM   6299  C CD2 . TYR C 2 157 ? -58.235 8.867   21.795  1.00 28.00  ? 157 TYR B CD2 1 
ATOM   6300  C CE1 . TYR C 2 157 ? -60.097 10.368  23.179  1.00 26.15  ? 157 TYR B CE1 1 
ATOM   6301  C CE2 . TYR C 2 157 ? -59.040 9.763   21.116  1.00 27.44  ? 157 TYR B CE2 1 
ATOM   6302  C CZ  . TYR C 2 157 ? -59.970 10.510  21.809  1.00 27.73  ? 157 TYR B CZ  1 
ATOM   6303  O OH  . TYR C 2 157 ? -60.766 11.394  21.116  1.00 28.36  ? 157 TYR B OH  1 
ATOM   6304  N N   . ASP C 2 158 ? -60.091 5.605   23.077  1.00 35.81  ? 158 ASP B N   1 
ATOM   6305  C CA  . ASP C 2 158 ? -60.921 5.031   22.015  1.00 36.86  ? 158 ASP B CA  1 
ATOM   6306  C C   . ASP C 2 158 ? -61.363 6.126   21.040  1.00 34.07  ? 158 ASP B C   1 
ATOM   6307  O O   . ASP C 2 158 ? -62.333 6.840   21.287  1.00 29.14  ? 158 ASP B O   1 
ATOM   6308  C CB  . ASP C 2 158 ? -62.137 4.316   22.633  1.00 39.99  ? 158 ASP B CB  1 
ATOM   6309  C CG  . ASP C 2 158 ? -62.835 3.366   21.663  1.00 43.42  ? 158 ASP B CG  1 
ATOM   6310  O OD1 . ASP C 2 158 ? -63.937 2.888   22.007  1.00 41.60  ? 158 ASP B OD1 1 
ATOM   6311  O OD2 . ASP C 2 158 ? -62.288 3.078   20.575  1.00 48.59  ? 158 ASP B OD2 1 
ATOM   6312  N N   . TYR C 2 159 ? -60.636 6.251   19.933  1.00 36.73  ? 159 TYR B N   1 
ATOM   6313  C CA  . TYR C 2 159 ? -60.900 7.293   18.935  1.00 36.46  ? 159 TYR B CA  1 
ATOM   6314  C C   . TYR C 2 159 ? -62.273 7.180   18.249  1.00 37.56  ? 159 TYR B C   1 
ATOM   6315  O O   . TYR C 2 159 ? -63.014 8.163   18.208  1.00 35.12  ? 159 TYR B O   1 
ATOM   6316  C CB  . TYR C 2 159 ? -59.781 7.328   17.887  1.00 35.66  ? 159 TYR B CB  1 
ATOM   6317  C CG  . TYR C 2 159 ? -60.098 8.169   16.669  1.00 38.33  ? 159 TYR B CG  1 
ATOM   6318  C CD1 . TYR C 2 159 ? -59.943 9.550   16.696  1.00 38.95  ? 159 TYR B CD1 1 
ATOM   6319  C CD2 . TYR C 2 159 ? -60.545 7.581   15.484  1.00 38.69  ? 159 TYR B CD2 1 
ATOM   6320  C CE1 . TYR C 2 159 ? -60.223 10.324  15.584  1.00 38.57  ? 159 TYR B CE1 1 
ATOM   6321  C CE2 . TYR C 2 159 ? -60.828 8.350   14.368  1.00 38.48  ? 159 TYR B CE2 1 
ATOM   6322  C CZ  . TYR C 2 159 ? -60.667 9.720   14.425  1.00 38.33  ? 159 TYR B CZ  1 
ATOM   6323  O OH  . TYR C 2 159 ? -60.939 10.491  13.323  1.00 36.63  ? 159 TYR B OH  1 
ATOM   6324  N N   . PRO C 2 160 ? -62.615 5.993   17.703  1.00 39.32  ? 160 PRO B N   1 
ATOM   6325  C CA  . PRO C 2 160 ? -63.914 5.865   17.019  1.00 39.23  ? 160 PRO B CA  1 
ATOM   6326  C C   . PRO C 2 160 ? -65.126 6.234   17.880  1.00 39.94  ? 160 PRO B C   1 
ATOM   6327  O O   . PRO C 2 160 ? -66.137 6.689   17.350  1.00 37.94  ? 160 PRO B O   1 
ATOM   6328  C CB  . PRO C 2 160 ? -63.988 4.381   16.621  1.00 41.42  ? 160 PRO B CB  1 
ATOM   6329  C CG  . PRO C 2 160 ? -62.723 3.736   17.065  1.00 42.16  ? 160 PRO B CG  1 
ATOM   6330  C CD  . PRO C 2 160 ? -61.783 4.780   17.574  1.00 41.15  ? 160 PRO B CD  1 
ATOM   6331  N N   . GLN C 2 161 ? -65.014 6.038   19.191  1.00 42.78  ? 161 GLN B N   1 
ATOM   6332  C CA  . GLN C 2 161 ? -66.115 6.284   20.126  1.00 43.46  ? 161 GLN B CA  1 
ATOM   6333  C C   . GLN C 2 161 ? -66.567 7.746   20.169  1.00 40.83  ? 161 GLN B C   1 
ATOM   6334  O O   . GLN C 2 161 ? -67.754 8.025   20.343  1.00 42.64  ? 161 GLN B O   1 
ATOM   6335  C CB  . GLN C 2 161 ? -65.704 5.832   21.531  1.00 46.02  ? 161 GLN B CB  1 
ATOM   6336  C CG  . GLN C 2 161 ? -66.842 5.617   22.500  1.00 48.46  ? 161 GLN B CG  1 
ATOM   6337  C CD  . GLN C 2 161 ? -66.353 5.125   23.872  1.00 48.68  ? 161 GLN B CD  1 
ATOM   6338  O OE1 . GLN C 2 161 ? -66.613 5.739   24.922  1.00 45.07  ? 161 GLN B OE1 1 
ATOM   6339  N NE2 . GLN C 2 161 ? -65.616 4.018   23.862  1.00 50.57  ? 161 GLN B NE2 1 
ATOM   6340  N N   . TYR C 2 162 ? -65.622 8.670   20.018  1.00 40.17  ? 162 TYR B N   1 
ATOM   6341  C CA  . TYR C 2 162 ? -65.922 10.101  20.058  1.00 38.73  ? 162 TYR B CA  1 
ATOM   6342  C C   . TYR C 2 162 ? -65.846 10.765  18.680  1.00 34.68  ? 162 TYR B C   1 
ATOM   6343  O O   . TYR C 2 162 ? -66.154 11.946  18.551  1.00 32.02  ? 162 TYR B O   1 
ATOM   6344  C CB  . TYR C 2 162 ? -64.956 10.820  21.006  1.00 41.31  ? 162 TYR B CB  1 
ATOM   6345  C CG  . TYR C 2 162 ? -64.926 10.276  22.419  1.00 41.81  ? 162 TYR B CG  1 
ATOM   6346  C CD1 . TYR C 2 162 ? -63.905 9.428   22.835  1.00 41.94  ? 162 TYR B CD1 1 
ATOM   6347  C CD2 . TYR C 2 162 ? -65.910 10.623  23.347  1.00 43.68  ? 162 TYR B CD2 1 
ATOM   6348  C CE1 . TYR C 2 162 ? -63.863 8.933   24.128  1.00 44.18  ? 162 TYR B CE1 1 
ATOM   6349  C CE2 . TYR C 2 162 ? -65.877 10.133  24.646  1.00 44.17  ? 162 TYR B CE2 1 
ATOM   6350  C CZ  . TYR C 2 162 ? -64.850 9.288   25.031  1.00 46.18  ? 162 TYR B CZ  1 
ATOM   6351  O OH  . TYR C 2 162 ? -64.805 8.796   26.317  1.00 50.61  ? 162 TYR B OH  1 
ATOM   6352  N N   . SER C 2 163 ? -65.453 10.008  17.659  1.00 37.48  ? 163 SER B N   1 
ATOM   6353  C CA  . SER C 2 163 ? -65.169 10.571  16.334  1.00 40.51  ? 163 SER B CA  1 
ATOM   6354  C C   . SER C 2 163 ? -66.367 11.281  15.692  1.00 42.36  ? 163 SER B C   1 
ATOM   6355  O O   . SER C 2 163 ? -66.194 12.313  15.048  1.00 39.59  ? 163 SER B O   1 
ATOM   6356  C CB  . SER C 2 163 ? -64.645 9.484   15.389  1.00 42.89  ? 163 SER B CB  1 
ATOM   6357  O OG  . SER C 2 163 ? -65.615 8.474   15.176  1.00 45.14  ? 163 SER B OG  1 
ATOM   6358  N N   . GLU C 2 164 ? -67.567 10.722  15.869  1.00 48.65  ? 164 GLU B N   1 
ATOM   6359  C CA  . GLU C 2 164 ? -68.804 11.304  15.333  1.00 53.24  ? 164 GLU B CA  1 
ATOM   6360  C C   . GLU C 2 164 ? -69.075 12.673  15.953  1.00 49.64  ? 164 GLU B C   1 
ATOM   6361  O O   . GLU C 2 164 ? -69.235 13.667  15.240  1.00 52.67  ? 164 GLU B O   1 
ATOM   6362  C CB  . GLU C 2 164 ? -70.009 10.391  15.616  1.00 61.07  ? 164 GLU B CB  1 
ATOM   6363  C CG  . GLU C 2 164 ? -70.075 9.091   14.823  1.00 66.79  ? 164 GLU B CG  1 
ATOM   6364  C CD  . GLU C 2 164 ? -71.422 8.402   14.969  1.00 71.30  ? 164 GLU B CD  1 
ATOM   6365  O OE1 . GLU C 2 164 ? -72.173 8.272   13.963  1.00 73.31  ? 164 GLU B OE1 1 
ATOM   6366  O OE2 . GLU C 2 164 ? -71.730 8.003   16.109  1.00 69.31  ? 164 GLU B OE2 1 
ATOM   6367  N N   . GLU C 2 165 ? -69.126 12.711  17.283  1.00 40.94  ? 165 GLU B N   1 
ATOM   6368  C CA  . GLU C 2 165 ? -69.336 13.956  18.018  1.00 42.05  ? 165 GLU B CA  1 
ATOM   6369  C C   . GLU C 2 165 ? -68.304 15.010  17.622  1.00 43.36  ? 165 GLU B C   1 
ATOM   6370  O O   . GLU C 2 165 ? -68.642 16.179  17.439  1.00 43.40  ? 165 GLU B O   1 
ATOM   6371  C CB  . GLU C 2 165 ? -69.256 13.706  19.526  1.00 42.59  ? 165 GLU B CB  1 
ATOM   6372  C CG  . GLU C 2 165 ? -69.622 14.914  20.380  1.00 43.11  ? 165 GLU B CG  1 
ATOM   6373  C CD  . GLU C 2 165 ? -69.393 14.685  21.864  1.00 43.25  ? 165 GLU B CD  1 
ATOM   6374  O OE1 . GLU C 2 165 ? -69.218 13.514  22.277  1.00 47.33  ? 165 GLU B OE1 1 
ATOM   6375  O OE2 . GLU C 2 165 ? -69.384 15.680  22.619  1.00 39.15  ? 165 GLU B OE2 1 
ATOM   6376  N N   . ALA C 2 166 ? -67.053 14.573  17.479  1.00 42.72  ? 166 ALA B N   1 
ATOM   6377  C CA  . ALA C 2 166 ? -65.937 15.435  17.116  1.00 44.67  ? 166 ALA B CA  1 
ATOM   6378  C C   . ALA C 2 166 ? -66.137 16.048  15.739  1.00 49.24  ? 166 ALA B C   1 
ATOM   6379  O O   . ALA C 2 166 ? -65.803 17.210  15.535  1.00 52.89  ? 166 ALA B O   1 
ATOM   6380  C CB  . ALA C 2 166 ? -64.631 14.656  17.161  1.00 42.99  ? 166 ALA B CB  1 
ATOM   6381  N N   . ARG C 2 167 ? -66.708 15.270  14.817  1.00 50.87  ? 167 ARG B N   1 
ATOM   6382  C CA  . ARG C 2 167 ? -66.936 15.705  13.435  1.00 51.48  ? 167 ARG B CA  1 
ATOM   6383  C C   . ARG C 2 167 ? -68.039 16.756  13.332  1.00 52.59  ? 167 ARG B C   1 
ATOM   6384  O O   . ARG C 2 167 ? -68.060 17.570  12.399  1.00 60.26  ? 167 ARG B O   1 
ATOM   6385  C CB  . ARG C 2 167 ? -67.308 14.505  12.546  1.00 48.75  ? 167 ARG B CB  1 
ATOM   6386  C CG  . ARG C 2 167 ? -66.984 14.721  11.075  1.00 45.09  ? 167 ARG B CG  1 
ATOM   6387  C CD  . ARG C 2 167 ? -67.553 13.632  10.161  1.00 44.96  ? 167 ARG B CD  1 
ATOM   6388  N NE  . ARG C 2 167 ? -68.926 13.212  10.501  1.00 42.61  ? 167 ARG B NE  1 
ATOM   6389  C CZ  . ARG C 2 167 ? -70.030 13.878  10.164  1.00 41.69  ? 167 ARG B CZ  1 
ATOM   6390  N NH1 . ARG C 2 167 ? -69.945 15.011  9.481   1.00 42.33  ? 167 ARG B NH1 1 
ATOM   6391  N NH2 . ARG C 2 167 ? -71.229 13.415  10.513  1.00 42.49  ? 167 ARG B NH2 1 
ATOM   6392  N N   . LEU C 2 168 ? -68.960 16.736  14.287  1.00 49.58  ? 168 LEU B N   1 
ATOM   6393  C CA  . LEU C 2 168 ? -70.067 17.680  14.266  1.00 51.60  ? 168 LEU B CA  1 
ATOM   6394  C C   . LEU C 2 168 ? -69.545 19.048  14.660  1.00 53.25  ? 168 LEU B C   1 
ATOM   6395  O O   . LEU C 2 168 ? -69.784 20.019  13.948  1.00 57.66  ? 168 LEU B O   1 
ATOM   6396  C CB  . LEU C 2 168 ? -71.209 17.253  15.188  1.00 51.71  ? 168 LEU B CB  1 
ATOM   6397  C CG  . LEU C 2 168 ? -72.009 16.023  14.741  1.00 54.41  ? 168 LEU B CG  1 
ATOM   6398  C CD1 . LEU C 2 168 ? -73.007 15.601  15.813  1.00 52.37  ? 168 LEU B CD1 1 
ATOM   6399  C CD2 . LEU C 2 168 ? -72.722 16.269  13.417  1.00 50.34  ? 168 LEU B CD2 1 
ATOM   6400  N N   . LYS C 2 169 ? -68.795 19.111  15.760  1.00 50.08  ? 169 LYS B N   1 
ATOM   6401  C CA  . LYS C 2 169 ? -68.286 20.386  16.273  1.00 50.67  ? 169 LYS B CA  1 
ATOM   6402  C C   . LYS C 2 169 ? -67.160 20.969  15.413  1.00 48.36  ? 169 LYS B C   1 
ATOM   6403  O O   . LYS C 2 169 ? -66.904 22.178  15.453  1.00 45.93  ? 169 LYS B O   1 
ATOM   6404  C CB  . LYS C 2 169 ? -67.815 20.244  17.723  1.00 50.27  ? 169 LYS B CB  1 
ATOM   6405  C CG  . LYS C 2 169 ? -67.722 21.580  18.439  1.00 52.23  ? 169 LYS B CG  1 
ATOM   6406  C CD  . LYS C 2 169 ? -67.521 21.459  19.946  1.00 57.98  ? 169 LYS B CD  1 
ATOM   6407  C CE  . LYS C 2 169 ? -68.827 21.115  20.693  1.00 57.66  ? 169 LYS B CE  1 
ATOM   6408  N NZ  . LYS C 2 169 ? -69.255 22.238  21.583  1.00 51.37  ? 169 LYS B NZ  1 
ATOM   6409  N N   . ARG C 2 170 ? -66.493 20.111  14.645  1.00 52.48  ? 170 ARG B N   1 
ATOM   6410  C CA  . ARG C 2 170 ? -65.434 20.548  13.733  1.00 58.97  ? 170 ARG B CA  1 
ATOM   6411  C C   . ARG C 2 170 ? -65.963 21.378  12.574  1.00 64.34  ? 170 ARG B C   1 
ATOM   6412  O O   . ARG C 2 170 ? -65.307 22.320  12.137  1.00 67.47  ? 170 ARG B O   1 
ATOM   6413  C CB  . ARG C 2 170 ? -64.706 19.360  13.125  1.00 59.81  ? 170 ARG B CB  1 
ATOM   6414  C CG  . ARG C 2 170 ? -63.193 19.486  13.166  1.00 59.48  ? 170 ARG B CG  1 
ATOM   6415  C CD  . ARG C 2 170 ? -62.545 18.304  12.466  1.00 61.92  ? 170 ARG B CD  1 
ATOM   6416  N NE  . ARG C 2 170 ? -62.920 17.032  13.092  1.00 67.83  ? 170 ARG B NE  1 
ATOM   6417  C CZ  . ARG C 2 170 ? -62.911 15.842  12.487  1.00 70.53  ? 170 ARG B CZ  1 
ATOM   6418  N NH1 . ARG C 2 170 ? -62.546 15.722  11.212  1.00 72.41  ? 170 ARG B NH1 1 
ATOM   6419  N NH2 . ARG C 2 170 ? -63.274 14.756  13.162  1.00 69.26  ? 170 ARG B NH2 1 
ATOM   6420  N N   . GLU C 2 171 ? -67.117 20.979  12.043  1.00 69.05  ? 171 GLU B N   1 
ATOM   6421  C CA  . GLU C 2 171 ? -67.744 21.666  10.926  1.00 73.59  ? 171 GLU B CA  1 
ATOM   6422  C C   . GLU C 2 171 ? -68.899 22.542  11.425  1.00 75.12  ? 171 GLU B C   1 
ATOM   6423  O O   . GLU C 2 171 ? -69.662 23.096  10.628  1.00 78.53  ? 171 GLU B O   1 
ATOM   6424  C CB  . GLU C 2 171 ? -68.266 20.643  9.920   1.00 78.92  ? 171 GLU B CB  1 
ATOM   6425  C CG  . GLU C 2 171 ? -67.196 19.849  9.173   1.00 85.15  ? 171 GLU B CG  1 
ATOM   6426  C CD  . GLU C 2 171 ? -67.693 18.549  8.561   1.00 89.19  ? 171 GLU B CD  1 
ATOM   6427  O OE1 . GLU C 2 171 ? -68.637 18.610  7.748   1.00 91.75  ? 171 GLU B OE1 1 
ATOM   6428  O OE2 . GLU C 2 171 ? -67.118 17.470  8.866   1.00 90.33  ? 171 GLU B OE2 1 
ATOM   6429  N N   . GLU C 2 172 ? -69.031 22.662  12.745  1.00 76.07  ? 172 GLU B N   1 
ATOM   6430  C CA  . GLU C 2 172 ? -70.023 23.554  13.339  1.00 79.26  ? 172 GLU B CA  1 
ATOM   6431  C C   . GLU C 2 172 ? -69.575 25.002  13.182  1.00 84.12  ? 172 GLU B C   1 
ATOM   6432  O O   . GLU C 2 172 ? -70.413 25.894  13.116  1.00 93.52  ? 172 GLU B O   1 
ATOM   6433  C CB  . GLU C 2 172 ? -70.221 23.240  14.829  1.00 79.85  ? 172 GLU B CB  1 
ATOM   6434  C CG  . GLU C 2 172 ? -71.529 23.775  15.440  1.00 82.39  ? 172 GLU B CG  1 
ATOM   6435  C CD  . GLU C 2 172 ? -72.226 22.769  16.344  1.00 90.67  ? 172 GLU B CD  1 
ATOM   6436  O OE1 . GLU C 2 172 ? -71.541 22.092  17.143  1.00 95.03  ? 172 GLU B OE1 1 
ATOM   6437  O OE2 . GLU C 2 172 ? -73.469 22.658  16.261  1.00 93.22  ? 172 GLU B OE2 1 
ATOM   6438  N N   . ILE C 2 173 ? -68.259 25.226  13.133  1.00 81.90  ? 173 ILE B N   1 
ATOM   6439  C CA  . ILE C 2 173 ? -67.674 26.543  12.832  1.00 84.56  ? 173 ILE B CA  1 
ATOM   6440  C C   . ILE C 2 173 ? -68.280 27.205  11.585  1.00 91.24  ? 173 ILE B C   1 
ATOM   6441  O O   . ILE C 2 173 ? -68.418 28.429  11.541  1.00 90.98  ? 173 ILE B O   1 
ATOM   6442  C CB  . ILE C 2 173 ? -66.140 26.454  12.654  1.00 78.66  ? 173 ILE B CB  1 
ATOM   6443  C CG1 . ILE C 2 173 ? -65.791 25.578  11.442  1.00 77.70  ? 173 ILE B CG1 1 
ATOM   6444  C CG2 . ILE C 2 173 ? -65.484 25.939  13.930  1.00 74.56  ? 173 ILE B CG2 1 
ATOM   6445  C CD1 . ILE C 2 173 ? -64.340 25.166  11.356  1.00 79.04  ? 173 ILE B CD1 1 
ATOM   6446  N N   . SER C 2 174 ? -68.637 26.396  10.584  1.00 91.14  ? 174 SER B N   1 
ATOM   6447  C CA  . SER C 2 174 ? -69.210 26.897  9.329   1.00 86.12  ? 174 SER B CA  1 
ATOM   6448  C C   . SER C 2 174 ? -70.450 27.757  9.571   1.00 80.33  ? 174 SER B C   1 
ATOM   6449  O O   . SER C 2 174 ? -70.384 28.986  9.514   1.00 73.93  ? 174 SER B O   1 
ATOM   6450  C CB  . SER C 2 174 ? -69.568 25.733  8.396   1.00 86.13  ? 174 SER B CB  1 
ATOM   6451  O OG  . SER C 2 174 ? -70.656 24.976  8.901   1.00 82.95  ? 174 SER B OG  1 
ATOM   6452  N N   . GLY D 1 4   ? -51.402 24.637  -7.573  1.00 67.76  ? 0   GLY C N   1 
ATOM   6453  C CA  . GLY D 1 4   ? -51.819 25.199  -6.252  1.00 67.64  ? 0   GLY C CA  1 
ATOM   6454  C C   . GLY D 1 4   ? -50.728 26.044  -5.617  1.00 63.57  ? 0   GLY C C   1 
ATOM   6455  O O   . GLY D 1 4   ? -49.586 26.044  -6.079  1.00 68.38  ? 0   GLY C O   1 
ATOM   6456  N N   . ASP D 1 5   ? -51.087 26.768  -4.560  1.00 55.57  ? 1   ASP C N   1 
ATOM   6457  C CA  . ASP D 1 5   ? -50.137 27.608  -3.826  1.00 53.77  ? 1   ASP C CA  1 
ATOM   6458  C C   . ASP D 1 5   ? -49.210 26.736  -2.976  1.00 53.82  ? 1   ASP C C   1 
ATOM   6459  O O   . ASP D 1 5   ? -49.661 25.759  -2.374  1.00 55.63  ? 1   ASP C O   1 
ATOM   6460  C CB  . ASP D 1 5   ? -50.874 28.603  -2.920  1.00 56.61  ? 1   ASP C CB  1 
ATOM   6461  C CG  . ASP D 1 5   ? -51.592 29.709  -3.694  1.00 58.55  ? 1   ASP C CG  1 
ATOM   6462  O OD1 . ASP D 1 5   ? -52.260 30.535  -3.032  1.00 53.08  ? 1   ASP C OD1 1 
ATOM   6463  O OD2 . ASP D 1 5   ? -51.471 29.782  -4.940  1.00 63.12  ? 1   ASP C OD2 1 
ATOM   6464  N N   . HIS D 1 6   ? -47.924 27.090  -2.933  1.00 50.38  ? 2   HIS C N   1 
ATOM   6465  C CA  . HIS D 1 6   ? -46.921 26.331  -2.175  1.00 51.38  ? 2   HIS C CA  1 
ATOM   6466  C C   . HIS D 1 6   ? -46.275 27.149  -1.083  1.00 49.15  ? 2   HIS C C   1 
ATOM   6467  O O   . HIS D 1 6   ? -46.135 28.367  -1.200  1.00 49.47  ? 2   HIS C O   1 
ATOM   6468  C CB  . HIS D 1 6   ? -45.811 25.827  -3.093  1.00 51.98  ? 2   HIS C CB  1 
ATOM   6469  C CG  . HIS D 1 6   ? -46.237 24.739  -4.050  1.00 57.03  ? 2   HIS C CG  1 
ATOM   6470  N ND1 . HIS D 1 6   ? -45.358 24.117  -4.855  1.00 63.11  ? 2   HIS C ND1 1 
ATOM   6471  C CD2 . HIS D 1 6   ? -47.471 24.123  -4.269  1.00 61.75  ? 2   HIS C CD2 1 
ATOM   6472  C CE1 . HIS D 1 6   ? -45.995 23.175  -5.577  1.00 60.91  ? 2   HIS C CE1 1 
ATOM   6473  N NE2 . HIS D 1 6   ? -47.286 23.178  -5.217  1.00 62.26  ? 2   HIS C NE2 1 
ATOM   6474  N N   . ILE D 1 7   ? -45.883 26.471  -0.007  1.00 45.33  ? 3   ILE C N   1 
ATOM   6475  C CA  . ILE D 1 7   ? -44.919 27.003  0.959   1.00 41.66  ? 3   ILE C CA  1 
ATOM   6476  C C   . ILE D 1 7   ? -43.928 25.881  1.290   1.00 40.67  ? 3   ILE C C   1 
ATOM   6477  O O   . ILE D 1 7   ? -44.327 24.730  1.458   1.00 36.02  ? 3   ILE C O   1 
ATOM   6478  C CB  . ILE D 1 7   ? -45.595 27.550  2.236   1.00 36.64  ? 3   ILE C CB  1 
ATOM   6479  C CG1 . ILE D 1 7   ? -44.578 28.294  3.099   1.00 42.17  ? 3   ILE C CG1 1 
ATOM   6480  C CG2 . ILE D 1 7   ? -46.232 26.438  3.050   1.00 39.01  ? 3   ILE C CG2 1 
ATOM   6481  C CD1 . ILE D 1 7   ? -45.210 29.072  4.236   1.00 42.34  ? 3   ILE C CD1 1 
ATOM   6482  N N   . CYS D 1 8   ? -42.640 26.216  1.327   1.00 44.20  ? 4   CYS C N   1 
ATOM   6483  C CA  . CYS D 1 8   ? -41.572 25.239  1.558   1.00 47.01  ? 4   CYS C CA  1 
ATOM   6484  C C   . CYS D 1 8   ? -40.679 25.684  2.707   1.00 42.66  ? 4   CYS C C   1 
ATOM   6485  O O   . CYS D 1 8   ? -40.546 26.876  2.963   1.00 39.57  ? 4   CYS C O   1 
ATOM   6486  C CB  . CYS D 1 8   ? -40.707 25.073  0.307   1.00 54.02  ? 4   CYS C CB  1 
ATOM   6487  S SG  . CYS D 1 8   ? -41.585 24.510  -1.170  1.00 69.00  ? 4   CYS C SG  1 
ATOM   6488  N N   . ILE D 1 9   ? -40.079 24.720  3.398   1.00 37.62  ? 5   ILE C N   1 
ATOM   6489  C CA  . ILE D 1 9   ? -39.062 25.009  4.403   1.00 36.38  ? 5   ILE C CA  1 
ATOM   6490  C C   . ILE D 1 9   ? -37.725 24.517  3.873   1.00 34.19  ? 5   ILE C C   1 
ATOM   6491  O O   . ILE D 1 9   ? -37.647 23.460  3.244   1.00 33.03  ? 5   ILE C O   1 
ATOM   6492  C CB  . ILE D 1 9   ? -39.373 24.346  5.766   1.00 37.19  ? 5   ILE C CB  1 
ATOM   6493  C CG1 . ILE D 1 9   ? -40.590 25.011  6.417   1.00 35.88  ? 5   ILE C CG1 1 
ATOM   6494  C CG2 . ILE D 1 9   ? -38.189 24.488  6.712   1.00 35.39  ? 5   ILE C CG2 1 
ATOM   6495  C CD1 . ILE D 1 9   ? -41.903 24.736  5.721   1.00 34.58  ? 5   ILE C CD1 1 
ATOM   6496  N N   . GLY D 1 10  ? -36.677 25.290  4.126   1.00 35.04  ? 6   GLY C N   1 
ATOM   6497  C CA  . GLY D 1 10  ? -35.343 24.954  3.643   1.00 34.26  ? 6   GLY C CA  1 
ATOM   6498  C C   . GLY D 1 10  ? -34.267 25.729  4.370   1.00 35.48  ? 6   GLY C C   1 
ATOM   6499  O O   . GLY D 1 10  ? -34.539 26.411  5.365   1.00 34.16  ? 6   GLY C O   1 
ATOM   6500  N N   . TYR D 1 11  ? -33.045 25.638  3.860   1.00 38.41  ? 7   TYR C N   1 
ATOM   6501  C CA  . TYR D 1 11  ? -31.894 26.239  4.520   1.00 39.87  ? 7   TYR C CA  1 
ATOM   6502  C C   . TYR D 1 11  ? -30.876 26.817  3.533   1.00 41.33  ? 7   TYR C C   1 
ATOM   6503  O O   . TYR D 1 11  ? -30.942 26.567  2.329   1.00 36.05  ? 7   TYR C O   1 
ATOM   6504  C CB  . TYR D 1 11  ? -31.235 25.206  5.448   1.00 37.53  ? 7   TYR C CB  1 
ATOM   6505  C CG  . TYR D 1 11  ? -30.814 23.924  4.765   1.00 31.69  ? 7   TYR C CG  1 
ATOM   6506  C CD1 . TYR D 1 11  ? -29.537 23.782  4.242   1.00 29.74  ? 7   TYR C CD1 1 
ATOM   6507  C CD2 . TYR D 1 11  ? -31.686 22.850  4.656   1.00 31.79  ? 7   TYR C CD2 1 
ATOM   6508  C CE1 . TYR D 1 11  ? -29.141 22.611  3.622   1.00 29.83  ? 7   TYR C CE1 1 
ATOM   6509  C CE2 . TYR D 1 11  ? -31.300 21.672  4.031   1.00 30.53  ? 7   TYR C CE2 1 
ATOM   6510  C CZ  . TYR D 1 11  ? -30.025 21.559  3.516   1.00 30.90  ? 7   TYR C CZ  1 
ATOM   6511  O OH  . TYR D 1 11  ? -29.626 20.396  2.893   1.00 32.69  ? 7   TYR C OH  1 
ATOM   6512  N N   . HIS D 1 12  ? -29.926 27.578  4.071   1.00 44.17  ? 8   HIS C N   1 
ATOM   6513  C CA  . HIS D 1 12  ? -28.966 28.342  3.276   1.00 43.95  ? 8   HIS C CA  1 
ATOM   6514  C C   . HIS D 1 12  ? -27.988 27.488  2.526   1.00 40.86  ? 8   HIS C C   1 
ATOM   6515  O O   . HIS D 1 12  ? -27.659 26.380  2.946   1.00 43.29  ? 8   HIS C O   1 
ATOM   6516  C CB  . HIS D 1 12  ? -28.213 29.305  4.186   1.00 45.58  ? 8   HIS C CB  1 
ATOM   6517  C CG  . HIS D 1 12  ? -27.187 30.154  3.472   1.00 52.03  ? 8   HIS C CG  1 
ATOM   6518  N ND1 . HIS D 1 12  ? -27.534 31.115  2.605   1.00 55.40  ? 8   HIS C ND1 1 
ATOM   6519  C CD2 . HIS D 1 12  ? -25.792 30.168  3.537   1.00 58.61  ? 8   HIS C CD2 1 
ATOM   6520  C CE1 . HIS D 1 12  ? -26.430 31.717  2.131   1.00 58.53  ? 8   HIS C CE1 1 
ATOM   6521  N NE2 . HIS D 1 12  ? -25.361 31.136  2.702   1.00 61.85  ? 8   HIS C NE2 1 
ATOM   6522  N N   . ALA D 1 13  ? -27.533 28.005  1.390   1.00 42.91  ? 9   ALA C N   1 
ATOM   6523  C CA  . ALA D 1 13  ? -26.418 27.420  0.648   1.00 43.63  ? 9   ALA C CA  1 
ATOM   6524  C C   . ALA D 1 13  ? -25.605 28.549  0.028   1.00 42.75  ? 9   ALA C C   1 
ATOM   6525  O O   . ALA D 1 13  ? -26.120 29.652  -0.158  1.00 48.61  ? 9   ALA C O   1 
ATOM   6526  C CB  . ALA D 1 13  ? -26.920 26.463  -0.420  1.00 42.16  ? 9   ALA C CB  1 
ATOM   6527  N N   . ASN D 1 14  ? -24.335 28.285  -0.263  1.00 41.44  ? 10  ASN C N   1 
ATOM   6528  C CA  . ASN D 1 14  ? -23.457 29.304  -0.831  1.00 40.04  ? 10  ASN C CA  1 
ATOM   6529  C C   . ASN D 1 14  ? -22.352 28.700  -1.714  1.00 43.96  ? 10  ASN C C   1 
ATOM   6530  O O   . ASN D 1 14  ? -22.393 27.508  -2.037  1.00 37.48  ? 10  ASN C O   1 
ATOM   6531  C CB  . ASN D 1 14  ? -22.896 30.197  0.289   1.00 38.94  ? 10  ASN C CB  1 
ATOM   6532  C CG  . ASN D 1 14  ? -21.951 29.463  1.229   1.00 42.32  ? 10  ASN C CG  1 
ATOM   6533  O OD1 . ASN D 1 14  ? -21.505 28.352  0.948   1.00 40.73  ? 10  ASN C OD1 1 
ATOM   6534  N ND2 . ASN D 1 14  ? -21.634 30.095  2.357   1.00 36.81  ? 10  ASN C ND2 1 
ATOM   6535  N N   . ASN D 1 15  ? -21.376 29.527  -2.092  1.00 54.30  ? 11  ASN C N   1 
ATOM   6536  C CA  . ASN D 1 15  ? -20.308 29.128  -3.022  1.00 60.01  ? 11  ASN C CA  1 
ATOM   6537  C C   . ASN D 1 15  ? -19.170 28.335  -2.367  1.00 61.42  ? 11  ASN C C   1 
ATOM   6538  O O   . ASN D 1 15  ? -18.194 27.986  -3.034  1.00 64.92  ? 11  ASN C O   1 
ATOM   6539  C CB  . ASN D 1 15  ? -19.697 30.381  -3.686  1.00 60.87  ? 11  ASN C CB  1 
ATOM   6540  C CG  . ASN D 1 15  ? -19.081 31.336  -2.660  1.00 64.80  ? 11  ASN C CG  1 
ATOM   6541  O OD1 . ASN D 1 15  ? -19.223 31.108  -1.463  1.00 63.00  ? 11  ASN C OD1 1 
ATOM   6542  N ND2 . ASN D 1 15  ? -18.404 32.400  -3.095  1.00 76.99  ? 11  ASN C ND2 1 
ATOM   6543  N N   . SER D 1 16  ? -19.288 28.065  -1.069  1.00 55.68  ? 12  SER C N   1 
ATOM   6544  C CA  . SER D 1 16  ? -18.168 27.567  -0.271  1.00 50.69  ? 12  SER C CA  1 
ATOM   6545  C C   . SER D 1 16  ? -17.749 26.141  -0.615  1.00 43.74  ? 12  SER C C   1 
ATOM   6546  O O   . SER D 1 16  ? -18.590 25.283  -0.889  1.00 41.77  ? 12  SER C O   1 
ATOM   6547  C CB  . SER D 1 16  ? -18.507 27.651  1.219   1.00 52.46  ? 12  SER C CB  1 
ATOM   6548  O OG  . SER D 1 16  ? -17.397 27.274  2.016   1.00 54.29  ? 12  SER C OG  1 
ATOM   6549  N N   . THR D 1 17  ? -16.436 25.912  -0.604  1.00 44.47  ? 13  THR C N   1 
ATOM   6550  C CA  . THR D 1 17  ? -15.851 24.588  -0.822  1.00 45.84  ? 13  THR C CA  1 
ATOM   6551  C C   . THR D 1 17  ? -15.125 24.084  0.437   1.00 49.48  ? 13  THR C C   1 
ATOM   6552  O O   . THR D 1 17  ? -14.502 23.017  0.412   1.00 46.17  ? 13  THR C O   1 
ATOM   6553  C CB  . THR D 1 17  ? -14.848 24.611  -1.996  1.00 48.53  ? 13  THR C CB  1 
ATOM   6554  O OG1 . THR D 1 17  ? -13.828 25.587  -1.738  1.00 49.52  ? 13  THR C OG1 1 
ATOM   6555  C CG2 . THR D 1 17  ? -15.549 24.954  -3.311  1.00 42.36  ? 13  THR C CG2 1 
ATOM   6556  N N   . GLU D 1 18  ? -15.218 24.845  1.531   1.00 50.97  ? 14  GLU C N   1 
ATOM   6557  C CA  . GLU D 1 18  ? -14.586 24.479  2.799   1.00 54.97  ? 14  GLU C CA  1 
ATOM   6558  C C   . GLU D 1 18  ? -15.095 23.112  3.259   1.00 51.94  ? 14  GLU C C   1 
ATOM   6559  O O   . GLU D 1 18  ? -16.304 22.863  3.273   1.00 44.81  ? 14  GLU C O   1 
ATOM   6560  C CB  . GLU D 1 18  ? -14.878 25.526  3.883   1.00 66.19  ? 14  GLU C CB  1 
ATOM   6561  C CG  . GLU D 1 18  ? -14.313 26.917  3.613   1.00 76.94  ? 14  GLU C CG  1 
ATOM   6562  C CD  . GLU D 1 18  ? -12.795 26.962  3.629   1.00 88.25  ? 14  GLU C CD  1 
ATOM   6563  O OE1 . GLU D 1 18  ? -12.182 26.325  4.512   1.00 91.95  ? 14  GLU C OE1 1 
ATOM   6564  O OE2 . GLU D 1 18  ? -12.213 27.643  2.757   1.00 93.18  ? 14  GLU C OE2 1 
ATOM   6565  N N   . GLN D 1 19  ? -14.162 22.237  3.623   1.00 51.68  ? 15  GLN C N   1 
ATOM   6566  C CA  . GLN D 1 19  ? -14.479 20.881  4.053   1.00 49.50  ? 15  GLN C CA  1 
ATOM   6567  C C   . GLN D 1 19  ? -14.200 20.702  5.542   1.00 49.92  ? 15  GLN C C   1 
ATOM   6568  O O   . GLN D 1 19  ? -13.239 21.249  6.091   1.00 52.54  ? 15  GLN C O   1 
ATOM   6569  C CB  . GLN D 1 19  ? -13.675 19.854  3.253   1.00 49.52  ? 15  GLN C CB  1 
ATOM   6570  C CG  . GLN D 1 19  ? -14.251 19.534  1.883   1.00 58.68  ? 15  GLN C CG  1 
ATOM   6571  C CD  . GLN D 1 19  ? -13.526 18.380  1.201   1.00 67.43  ? 15  GLN C CD  1 
ATOM   6572  O OE1 . GLN D 1 19  ? -12.474 17.932  1.662   1.00 76.57  ? 15  GLN C OE1 1 
ATOM   6573  N NE2 . GLN D 1 19  ? -14.087 17.892  0.102   1.00 60.37  ? 15  GLN C NE2 1 
ATOM   6574  N N   . VAL D 1 20  ? -15.052 19.914  6.183   1.00 42.26  ? 16  VAL C N   1 
ATOM   6575  C CA  . VAL D 1 20  ? -14.947 19.633  7.603   1.00 36.89  ? 16  VAL C CA  1 
ATOM   6576  C C   . VAL D 1 20  ? -15.055 18.123  7.774   1.00 36.17  ? 16  VAL C C   1 
ATOM   6577  O O   . VAL D 1 20  ? -15.594 17.431  6.910   1.00 38.02  ? 16  VAL C O   1 
ATOM   6578  C CB  . VAL D 1 20  ? -16.052 20.387  8.387   1.00 33.91  ? 16  VAL C CB  1 
ATOM   6579  C CG1 . VAL D 1 20  ? -16.978 19.423  9.113   1.00 31.47  ? 16  VAL C CG1 1 
ATOM   6580  C CG2 . VAL D 1 20  ? -15.449 21.407  9.335   1.00 29.49  ? 16  VAL C CG2 1 
ATOM   6581  N N   . ASP D 1 21  ? -14.523 17.611  8.876   1.00 42.25  ? 17  ASP C N   1 
ATOM   6582  C CA  . ASP D 1 21  ? -14.660 16.196  9.189   1.00 45.32  ? 17  ASP C CA  1 
ATOM   6583  C C   . ASP D 1 21  ? -15.544 16.007  10.413  1.00 39.57  ? 17  ASP C C   1 
ATOM   6584  O O   . ASP D 1 21  ? -15.521 16.806  11.342  1.00 37.76  ? 17  ASP C O   1 
ATOM   6585  C CB  . ASP D 1 21  ? -13.293 15.551  9.398   1.00 53.05  ? 17  ASP C CB  1 
ATOM   6586  C CG  . ASP D 1 21  ? -12.624 15.187  8.090   1.00 60.54  ? 17  ASP C CG  1 
ATOM   6587  O OD1 . ASP D 1 21  ? -12.212 16.114  7.365   1.00 72.09  ? 17  ASP C OD1 1 
ATOM   6588  O OD2 . ASP D 1 21  ? -12.519 13.979  7.782   1.00 63.29  ? 17  ASP C OD2 1 
ATOM   6589  N N   . THR D 1 22  ? -16.332 14.942  10.377  1.00 38.60  ? 18  THR C N   1 
ATOM   6590  C CA  . THR D 1 22  ? -17.248 14.585  11.443  1.00 40.06  ? 18  THR C CA  1 
ATOM   6591  C C   . THR D 1 22  ? -16.782 13.247  12.007  1.00 39.23  ? 18  THR C C   1 
ATOM   6592  O O   . THR D 1 22  ? -16.016 12.532  11.363  1.00 37.30  ? 18  THR C O   1 
ATOM   6593  C CB  . THR D 1 22  ? -18.689 14.492  10.880  1.00 42.79  ? 18  THR C CB  1 
ATOM   6594  O OG1 . THR D 1 22  ? -19.183 15.813  10.618  1.00 45.38  ? 18  THR C OG1 1 
ATOM   6595  C CG2 . THR D 1 22  ? -19.637 13.800  11.831  1.00 38.00  ? 18  THR C CG2 1 
ATOM   6596  N N   . ILE D 1 23  ? -17.228 12.920  13.215  1.00 40.35  ? 19  ILE C N   1 
ATOM   6597  C CA  . ILE D 1 23  ? -16.909 11.636  13.843  1.00 40.84  ? 19  ILE C CA  1 
ATOM   6598  C C   . ILE D 1 23  ? -17.391 10.467  12.971  1.00 37.91  ? 19  ILE C C   1 
ATOM   6599  O O   . ILE D 1 23  ? -16.779 9.403   12.964  1.00 39.03  ? 19  ILE C O   1 
ATOM   6600  C CB  . ILE D 1 23  ? -17.490 11.563  15.293  1.00 45.39  ? 19  ILE C CB  1 
ATOM   6601  C CG1 . ILE D 1 23  ? -16.460 10.998  16.279  1.00 49.37  ? 19  ILE C CG1 1 
ATOM   6602  C CG2 . ILE D 1 23  ? -18.789 10.777  15.360  1.00 37.50  ? 19  ILE C CG2 1 
ATOM   6603  C CD1 . ILE D 1 23  ? -16.168 9.527   16.102  1.00 52.86  ? 19  ILE C CD1 1 
ATOM   6604  N N   . MET D 1 24  ? -18.474 10.681  12.226  1.00 42.12  ? 20  MET C N   1 
ATOM   6605  C CA  . MET D 1 24  ? -19.069 9.649   11.374  1.00 46.21  ? 20  MET C CA  1 
ATOM   6606  C C   . MET D 1 24  ? -18.911 9.872   9.863   1.00 49.99  ? 20  MET C C   1 
ATOM   6607  O O   . MET D 1 24  ? -19.130 8.943   9.087   1.00 50.11  ? 20  MET C O   1 
ATOM   6608  C CB  . MET D 1 24  ? -20.556 9.517   11.698  1.00 51.25  ? 20  MET C CB  1 
ATOM   6609  C CG  . MET D 1 24  ? -20.842 8.905   13.062  1.00 52.08  ? 20  MET C CG  1 
ATOM   6610  S SD  . MET D 1 24  ? -22.494 8.205   13.103  1.00 56.20  ? 20  MET C SD  1 
ATOM   6611  C CE  . MET D 1 24  ? -22.621 7.602   14.784  1.00 68.54  ? 20  MET C CE  1 
ATOM   6612  N N   . GLU D 1 25  ? -18.541 11.083  9.446   1.00 56.72  ? 21  GLU C N   1 
ATOM   6613  C CA  . GLU D 1 25  ? -18.408 11.411  8.018   1.00 54.76  ? 21  GLU C CA  1 
ATOM   6614  C C   . GLU D 1 25  ? -17.112 12.148  7.711   1.00 49.50  ? 21  GLU C C   1 
ATOM   6615  O O   . GLU D 1 25  ? -16.712 13.049  8.446   1.00 43.70  ? 21  GLU C O   1 
ATOM   6616  C CB  . GLU D 1 25  ? -19.567 12.296  7.564   1.00 58.72  ? 21  GLU C CB  1 
ATOM   6617  C CG  . GLU D 1 25  ? -20.912 11.601  7.512   1.00 65.46  ? 21  GLU C CG  1 
ATOM   6618  C CD  . GLU D 1 25  ? -22.036 12.568  7.209   1.00 66.13  ? 21  GLU C CD  1 
ATOM   6619  O OE1 . GLU D 1 25  ? -21.953 13.266  6.173   1.00 68.24  ? 21  GLU C OE1 1 
ATOM   6620  O OE2 . GLU D 1 25  ? -22.994 12.632  8.012   1.00 65.29  ? 21  GLU C OE2 1 
ATOM   6621  N N   . LYS D 1 26  ? -16.479 11.776  6.605   1.00 47.83  ? 22  LYS C N   1 
ATOM   6622  C CA  . LYS D 1 26  ? -15.277 12.458  6.147   1.00 54.20  ? 22  LYS C CA  1 
ATOM   6623  C C   . LYS D 1 26  ? -15.617 13.452  5.041   1.00 48.75  ? 22  LYS C C   1 
ATOM   6624  O O   . LYS D 1 26  ? -16.595 13.281  4.321   1.00 45.55  ? 22  LYS C O   1 
ATOM   6625  C CB  . LYS D 1 26  ? -14.234 11.454  5.659   1.00 57.45  ? 22  LYS C CB  1 
ATOM   6626  C CG  . LYS D 1 26  ? -13.517 10.738  6.793   1.00 61.81  ? 22  LYS C CG  1 
ATOM   6627  C CD  . LYS D 1 26  ? -12.099 10.329  6.419   1.00 65.14  ? 22  LYS C CD  1 
ATOM   6628  C CE  . LYS D 1 26  ? -11.423 9.594   7.578   1.00 65.49  ? 22  LYS C CE  1 
ATOM   6629  N NZ  . LYS D 1 26  ? -10.514 8.510   7.110   1.00 65.64  ? 22  LYS C NZ  1 
ATOM   6630  N N   . ASN D 1 27  ? -14.808 14.503  4.947   1.00 49.34  ? 23  ASN C N   1 
ATOM   6631  C CA  . ASN D 1 27  ? -14.876 15.479  3.857   1.00 51.29  ? 23  ASN C CA  1 
ATOM   6632  C C   . ASN D 1 27  ? -16.301 15.937  3.540   1.00 48.02  ? 23  ASN C C   1 
ATOM   6633  O O   . ASN D 1 27  ? -16.821 15.706  2.447   1.00 44.50  ? 23  ASN C O   1 
ATOM   6634  C CB  . ASN D 1 27  ? -14.128 14.932  2.623   1.00 56.19  ? 23  ASN C CB  1 
ATOM   6635  C CG  . ASN D 1 27  ? -12.627 14.765  2.892   1.00 67.52  ? 23  ASN C CG  1 
ATOM   6636  O OD1 . ASN D 1 27  ? -12.175 15.100  3.976   1.00 67.88  ? 23  ASN C OD1 1 
ATOM   6637  N ND2 . ASN D 1 27  ? -11.848 14.254  1.944   1.00 79.76  ? 23  ASN C ND2 1 
ATOM   6638  N N   . VAL D 1 28  ? -16.920 16.575  4.533   1.00 41.76  ? 24  VAL C N   1 
ATOM   6639  C CA  . VAL D 1 28  ? -18.256 17.134  4.409   1.00 38.69  ? 24  VAL C CA  1 
ATOM   6640  C C   . VAL D 1 28  ? -18.146 18.612  4.055   1.00 38.57  ? 24  VAL C C   1 
ATOM   6641  O O   . VAL D 1 28  ? -17.578 19.399  4.811   1.00 41.93  ? 24  VAL C O   1 
ATOM   6642  C CB  . VAL D 1 28  ? -19.051 16.983  5.725   1.00 37.64  ? 24  VAL C CB  1 
ATOM   6643  C CG1 . VAL D 1 28  ? -20.432 17.606  5.593   1.00 33.80  ? 24  VAL C CG1 1 
ATOM   6644  C CG2 . VAL D 1 28  ? -19.166 15.517  6.115   1.00 40.44  ? 24  VAL C CG2 1 
ATOM   6645  N N   . THR D 1 29  ? -18.695 18.987  2.905   1.00 39.19  ? 25  THR C N   1 
ATOM   6646  C CA  . THR D 1 29  ? -18.665 20.374  2.468   1.00 41.18  ? 25  THR C CA  1 
ATOM   6647  C C   . THR D 1 29  ? -19.616 21.192  3.333   1.00 38.92  ? 25  THR C C   1 
ATOM   6648  O O   . THR D 1 29  ? -20.694 20.729  3.692   1.00 43.85  ? 25  THR C O   1 
ATOM   6649  C CB  . THR D 1 29  ? -19.040 20.508  0.978   1.00 40.96  ? 25  THR C CB  1 
ATOM   6650  O OG1 . THR D 1 29  ? -18.239 19.600  0.207   1.00 42.01  ? 25  THR C OG1 1 
ATOM   6651  C CG2 . THR D 1 29  ? -18.780 21.929  0.486   1.00 37.11  ? 25  THR C CG2 1 
ATOM   6652  N N   . VAL D 1 30  ? -19.205 22.413  3.654   1.00 36.34  ? 26  VAL C N   1 
ATOM   6653  C CA  . VAL D 1 30  ? -19.885 23.220  4.657   1.00 36.23  ? 26  VAL C CA  1 
ATOM   6654  C C   . VAL D 1 30  ? -19.893 24.706  4.276   1.00 37.84  ? 26  VAL C C   1 
ATOM   6655  O O   . VAL D 1 30  ? -19.013 25.169  3.553   1.00 50.45  ? 26  VAL C O   1 
ATOM   6656  C CB  . VAL D 1 30  ? -19.235 22.968  6.039   1.00 36.35  ? 26  VAL C CB  1 
ATOM   6657  C CG1 . VAL D 1 30  ? -18.656 24.241  6.629   1.00 38.05  ? 26  VAL C CG1 1 
ATOM   6658  C CG2 . VAL D 1 30  ? -20.227 22.318  6.987   1.00 37.16  ? 26  VAL C CG2 1 
ATOM   6659  N N   . THR D 1 31  ? -20.887 25.447  4.761   1.00 37.24  ? 27  THR C N   1 
ATOM   6660  C CA  . THR D 1 31  ? -21.071 26.849  4.355   1.00 40.09  ? 27  THR C CA  1 
ATOM   6661  C C   . THR D 1 31  ? -20.053 27.800  4.980   1.00 39.68  ? 27  THR C C   1 
ATOM   6662  O O   . THR D 1 31  ? -19.589 28.722  4.320   1.00 43.78  ? 27  THR C O   1 
ATOM   6663  C CB  . THR D 1 31  ? -22.507 27.365  4.602   1.00 37.73  ? 27  THR C CB  1 
ATOM   6664  O OG1 . THR D 1 31  ? -22.809 27.374  6.004   1.00 42.85  ? 27  THR C OG1 1 
ATOM   6665  C CG2 . THR D 1 31  ? -23.504 26.490  3.864   1.00 36.90  ? 27  THR C CG2 1 
ATOM   6666  N N   . HIS D 1 32  ? -19.730 27.595  6.250   1.00 46.13  ? 28  HIS C N   1 
ATOM   6667  C CA  . HIS D 1 32  ? -18.686 28.384  6.907   1.00 56.05  ? 28  HIS C CA  1 
ATOM   6668  C C   . HIS D 1 32  ? -17.928 27.534  7.895   1.00 52.10  ? 28  HIS C C   1 
ATOM   6669  O O   . HIS D 1 32  ? -18.472 26.587  8.476   1.00 47.71  ? 28  HIS C O   1 
ATOM   6670  C CB  . HIS D 1 32  ? -19.295 29.626  7.569   1.00 60.02  ? 28  HIS C CB  1 
ATOM   6671  C CG  . HIS D 1 32  ? -18.333 30.796  7.702   1.00 75.85  ? 28  HIS C CG  1 
ATOM   6672  N ND1 . HIS D 1 32  ? -18.296 31.804  6.811   1.00 83.89  ? 28  HIS C ND1 1 
ATOM   6673  C CD2 . HIS D 1 32  ? -17.370 31.098  8.673   1.00 83.80  ? 28  HIS C CD2 1 
ATOM   6674  C CE1 . HIS D 1 32  ? -17.358 32.699  7.181   1.00 83.38  ? 28  HIS C CE1 1 
ATOM   6675  N NE2 . HIS D 1 32  ? -16.792 32.266  8.318   1.00 84.15  ? 28  HIS C NE2 1 
ATOM   6676  N N   . ALA D 1 33  ? -16.654 27.860  8.082   1.00 47.49  ? 29  ALA C N   1 
ATOM   6677  C CA  . ALA D 1 33  ? -15.780 27.072  8.954   1.00 44.72  ? 29  ALA C CA  1 
ATOM   6678  C C   . ALA D 1 33  ? -14.692 27.929  9.578   1.00 44.19  ? 29  ALA C C   1 
ATOM   6679  O O   . ALA D 1 33  ? -14.251 28.909  8.981   1.00 46.26  ? 29  ALA C O   1 
ATOM   6680  C CB  . ALA D 1 33  ? -15.159 25.926  8.181   1.00 37.85  ? 29  ALA C CB  1 
ATOM   6681  N N   . GLN D 1 34  ? -14.260 27.546  10.779  1.00 48.79  ? 30  GLN C N   1 
ATOM   6682  C CA  . GLN D 1 34  ? -13.207 28.257  11.499  1.00 46.57  ? 30  GLN C CA  1 
ATOM   6683  C C   . GLN D 1 34  ? -12.138 27.275  11.975  1.00 50.81  ? 30  GLN C C   1 
ATOM   6684  O O   . GLN D 1 34  ? -12.449 26.305  12.664  1.00 58.33  ? 30  GLN C O   1 
ATOM   6685  C CB  . GLN D 1 34  ? -13.809 29.006  12.685  1.00 46.87  ? 30  GLN C CB  1 
ATOM   6686  C CG  . GLN D 1 34  ? -12.912 30.088  13.263  1.00 49.24  ? 30  GLN C CG  1 
ATOM   6687  C CD  . GLN D 1 34  ? -13.665 31.035  14.178  1.00 51.85  ? 30  GLN C CD  1 
ATOM   6688  O OE1 . GLN D 1 34  ? -14.856 31.292  13.988  1.00 58.42  ? 30  GLN C OE1 1 
ATOM   6689  N NE2 . GLN D 1 34  ? -12.976 31.553  15.186  1.00 50.32  ? 30  GLN C NE2 1 
ATOM   6690  N N   . ASP D 1 35  ? -10.884 27.525  11.600  1.00 54.18  ? 31  ASP C N   1 
ATOM   6691  C CA  . ASP D 1 35  ? -9.758  26.700  12.047  1.00 49.99  ? 31  ASP C CA  1 
ATOM   6692  C C   . ASP D 1 35  ? -9.336  27.146  13.441  1.00 45.56  ? 31  ASP C C   1 
ATOM   6693  O O   . ASP D 1 35  ? -9.237  28.338  13.713  1.00 52.18  ? 31  ASP C O   1 
ATOM   6694  C CB  . ASP D 1 35  ? -8.574  26.804  11.077  1.00 50.04  ? 31  ASP C CB  1 
ATOM   6695  C CG  . ASP D 1 35  ? -7.627  25.605  11.164  1.00 56.52  ? 31  ASP C CG  1 
ATOM   6696  O OD1 . ASP D 1 35  ? -7.570  24.951  12.229  1.00 63.46  ? 31  ASP C OD1 1 
ATOM   6697  O OD2 . ASP D 1 35  ? -6.936  25.312  10.162  1.00 54.73  ? 31  ASP C OD2 1 
ATOM   6698  N N   . ILE D 1 36  ? -9.096  26.178  14.317  1.00 46.82  ? 32  ILE C N   1 
ATOM   6699  C CA  . ILE D 1 36  ? -8.788  26.433  15.719  1.00 47.15  ? 32  ILE C CA  1 
ATOM   6700  C C   . ILE D 1 36  ? -7.301  26.118  16.033  1.00 46.33  ? 32  ILE C C   1 
ATOM   6701  O O   . ILE D 1 36  ? -6.883  26.083  17.194  1.00 46.56  ? 32  ILE C O   1 
ATOM   6702  C CB  . ILE D 1 36  ? -9.794  25.609  16.583  1.00 48.26  ? 32  ILE C CB  1 
ATOM   6703  C CG1 . ILE D 1 36  ? -10.341 26.436  17.747  1.00 59.27  ? 32  ILE C CG1 1 
ATOM   6704  C CG2 . ILE D 1 36  ? -9.226  24.261  17.013  1.00 46.12  ? 32  ILE C CG2 1 
ATOM   6705  C CD1 . ILE D 1 36  ? -11.368 27.458  17.309  1.00 58.44  ? 32  ILE C CD1 1 
ATOM   6706  N N   . LEU D 1 37  ? -6.505  25.925  14.978  1.00 42.54  ? 33  LEU C N   1 
ATOM   6707  C CA  . LEU D 1 37  ? -5.085  25.572  15.088  1.00 42.09  ? 33  LEU C CA  1 
ATOM   6708  C C   . LEU D 1 37  ? -4.207  26.688  14.521  1.00 47.88  ? 33  LEU C C   1 
ATOM   6709  O O   . LEU D 1 37  ? -4.295  27.008  13.336  1.00 50.18  ? 33  LEU C O   1 
ATOM   6710  C CB  . LEU D 1 37  ? -4.815  24.277  14.321  1.00 40.29  ? 33  LEU C CB  1 
ATOM   6711  C CG  . LEU D 1 37  ? -3.359  23.790  14.260  1.00 42.84  ? 33  LEU C CG  1 
ATOM   6712  C CD1 . LEU D 1 37  ? -2.794  23.505  15.647  1.00 36.98  ? 33  LEU C CD1 1 
ATOM   6713  C CD2 . LEU D 1 37  ? -3.260  22.562  13.367  1.00 47.92  ? 33  LEU C CD2 1 
ATOM   6714  N N   . GLU D 1 38  ? -3.362  27.273  15.365  1.00 55.47  ? 34  GLU C N   1 
ATOM   6715  C CA  . GLU D 1 38  ? -2.457  28.338  14.936  1.00 56.03  ? 34  GLU C CA  1 
ATOM   6716  C C   . GLU D 1 38  ? -1.287  27.761  14.147  1.00 58.05  ? 34  GLU C C   1 
ATOM   6717  O O   . GLU D 1 38  ? -0.616  26.843  14.613  1.00 53.02  ? 34  GLU C O   1 
ATOM   6718  C CB  . GLU D 1 38  ? -1.937  29.126  16.143  1.00 56.95  ? 34  GLU C CB  1 
ATOM   6719  C CG  . GLU D 1 38  ? -1.218  30.417  15.786  1.00 56.53  ? 34  GLU C CG  1 
ATOM   6720  C CD  . GLU D 1 38  ? -2.055  31.325  14.906  1.00 62.83  ? 34  GLU C CD  1 
ATOM   6721  O OE1 . GLU D 1 38  ? -3.115  31.804  15.367  1.00 66.74  ? 34  GLU C OE1 1 
ATOM   6722  O OE2 . GLU D 1 38  ? -1.657  31.549  13.745  1.00 67.57  ? 34  GLU C OE2 1 
ATOM   6723  N N   . LYS D 1 39  ? -1.051  28.308  12.954  1.00 62.64  ? 35  LYS C N   1 
ATOM   6724  C CA  . LYS D 1 39  ? 0.001   27.818  12.056  1.00 56.02  ? 35  LYS C CA  1 
ATOM   6725  C C   . LYS D 1 39  ? 1.048   28.870  11.691  1.00 51.96  ? 35  LYS C C   1 
ATOM   6726  O O   . LYS D 1 39  ? 2.072   28.529  11.110  1.00 50.23  ? 35  LYS C O   1 
ATOM   6727  C CB  . LYS D 1 39  ? -0.625  27.274  10.771  1.00 57.49  ? 35  LYS C CB  1 
ATOM   6728  C CG  . LYS D 1 39  ? -1.312  25.931  10.958  1.00 61.17  ? 35  LYS C CG  1 
ATOM   6729  C CD  . LYS D 1 39  ? -2.061  25.477  9.708   1.00 58.00  ? 35  LYS C CD  1 
ATOM   6730  C CE  . LYS D 1 39  ? -3.553  25.231  9.946   1.00 57.94  ? 35  LYS C CE  1 
ATOM   6731  N NZ  . LYS D 1 39  ? -4.323  26.500  10.086  1.00 59.05  ? 35  LYS C NZ  1 
ATOM   6732  N N   . THR D 1 40  ? 0.806   30.132  12.037  1.00 52.73  ? 36  THR C N   1 
ATOM   6733  C CA  . THR D 1 40  ? 1.636   31.233  11.555  1.00 55.98  ? 36  THR C CA  1 
ATOM   6734  C C   . THR D 1 40  ? 2.489   31.876  12.655  1.00 60.65  ? 36  THR C C   1 
ATOM   6735  O O   . THR D 1 40  ? 2.007   32.141  13.764  1.00 58.07  ? 36  THR C O   1 
ATOM   6736  C CB  . THR D 1 40  ? 0.773   32.325  10.869  1.00 58.91  ? 36  THR C CB  1 
ATOM   6737  O OG1 . THR D 1 40  ? 1.626   33.288  10.240  1.00 59.55  ? 36  THR C OG1 1 
ATOM   6738  C CG2 . THR D 1 40  ? -0.127  33.048  11.868  1.00 55.88  ? 36  THR C CG2 1 
ATOM   6739  N N   . HIS D 1 41  ? 3.759   32.119  12.322  1.00 61.98  ? 37  HIS C N   1 
ATOM   6740  C CA  . HIS D 1 41  ? 4.685   32.880  13.164  1.00 61.67  ? 37  HIS C CA  1 
ATOM   6741  C C   . HIS D 1 41  ? 5.299   33.989  12.352  1.00 59.25  ? 37  HIS C C   1 
ATOM   6742  O O   . HIS D 1 41  ? 5.276   33.943  11.124  1.00 63.96  ? 37  HIS C O   1 
ATOM   6743  C CB  . HIS D 1 41  ? 5.775   31.972  13.737  1.00 60.80  ? 37  HIS C CB  1 
ATOM   6744  C CG  . HIS D 1 41  ? 6.604   31.269  12.687  1.00 58.39  ? 37  HIS C CG  1 
ATOM   6745  N ND1 . HIS D 1 41  ? 7.722   31.803  12.173  1.00 56.35  ? 37  HIS C ND1 1 
ATOM   6746  C CD2 . HIS D 1 41  ? 6.436   30.034  12.064  1.00 61.18  ? 37  HIS C CD2 1 
ATOM   6747  C CE1 . HIS D 1 41  ? 8.248   30.956  11.265  1.00 60.30  ? 37  HIS C CE1 1 
ATOM   6748  N NE2 . HIS D 1 41  ? 7.459   29.875  11.200  1.00 57.99  ? 37  HIS C NE2 1 
ATOM   6749  N N   . ASN D 1 42  ? 5.870   34.984  13.027  1.00 57.22  ? 38  ASN C N   1 
ATOM   6750  C CA  . ASN D 1 42  ? 6.424   36.162  12.351  1.00 57.70  ? 38  ASN C CA  1 
ATOM   6751  C C   . ASN D 1 42  ? 7.885   36.012  11.891  1.00 62.81  ? 38  ASN C C   1 
ATOM   6752  O O   . ASN D 1 42  ? 8.456   36.942  11.319  1.00 69.85  ? 38  ASN C O   1 
ATOM   6753  C CB  . ASN D 1 42  ? 6.255   37.415  13.228  1.00 54.36  ? 38  ASN C CB  1 
ATOM   6754  C CG  . ASN D 1 42  ? 7.201   37.450  14.418  1.00 50.49  ? 38  ASN C CG  1 
ATOM   6755  O OD1 . ASN D 1 42  ? 8.088   36.605  14.560  1.00 49.30  ? 38  ASN C OD1 1 
ATOM   6756  N ND2 . ASN D 1 42  ? 7.013   38.444  15.282  1.00 47.17  ? 38  ASN C ND2 1 
ATOM   6757  N N   . GLY D 1 43  ? 8.488   34.857  12.164  1.00 61.41  ? 39  GLY C N   1 
ATOM   6758  C CA  . GLY D 1 43  ? 9.824   34.537  11.666  1.00 53.67  ? 39  GLY C CA  1 
ATOM   6759  C C   . GLY D 1 43  ? 10.963  35.279  12.345  1.00 55.48  ? 39  GLY C C   1 
ATOM   6760  O O   . GLY D 1 43  ? 12.078  35.309  11.821  1.00 54.72  ? 39  GLY C O   1 
ATOM   6761  N N   . LYS D 1 44  ? 10.700  35.873  13.508  1.00 54.53  ? 40  LYS C N   1 
ATOM   6762  C CA  . LYS D 1 44  ? 11.706  36.680  14.203  1.00 56.11  ? 40  LYS C CA  1 
ATOM   6763  C C   . LYS D 1 44  ? 11.686  36.473  15.718  1.00 57.67  ? 40  LYS C C   1 
ATOM   6764  O O   . LYS D 1 44  ? 10.659  36.101  16.285  1.00 57.65  ? 40  LYS C O   1 
ATOM   6765  C CB  . LYS D 1 44  ? 11.493  38.160  13.879  1.00 64.07  ? 40  LYS C CB  1 
ATOM   6766  C CG  . LYS D 1 44  ? 11.825  38.535  12.448  1.00 77.60  ? 40  LYS C CG  1 
ATOM   6767  C CD  . LYS D 1 44  ? 13.326  38.659  12.265  1.00 85.91  ? 40  LYS C CD  1 
ATOM   6768  C CE  . LYS D 1 44  ? 13.733  38.666  10.797  1.00 89.08  ? 40  LYS C CE  1 
ATOM   6769  N NZ  . LYS D 1 44  ? 13.759  40.041  10.223  1.00 96.45  ? 40  LYS C NZ  1 
ATOM   6770  N N   . LEU D 1 45  ? 12.836  36.706  16.356  1.00 52.68  ? 41  LEU C N   1 
ATOM   6771  C CA  . LEU D 1 45  ? 12.941  36.716  17.816  1.00 51.39  ? 41  LEU C CA  1 
ATOM   6772  C C   . LEU D 1 45  ? 12.481  38.074  18.333  1.00 51.64  ? 41  LEU C C   1 
ATOM   6773  O O   . LEU D 1 45  ? 12.748  39.100  17.706  1.00 63.92  ? 41  LEU C O   1 
ATOM   6774  C CB  . LEU D 1 45  ? 14.381  36.451  18.266  1.00 50.21  ? 41  LEU C CB  1 
ATOM   6775  C CG  . LEU D 1 45  ? 15.065  35.192  17.735  1.00 49.99  ? 41  LEU C CG  1 
ATOM   6776  C CD1 . LEU D 1 45  ? 16.420  35.034  18.405  1.00 50.63  ? 41  LEU C CD1 1 
ATOM   6777  C CD2 . LEU D 1 45  ? 14.215  33.952  17.960  1.00 48.07  ? 41  LEU C CD2 1 
ATOM   6778  N N   . CYS D 1 46  ? 11.802  38.078  19.477  1.00 49.28  ? 42  CYS C N   1 
ATOM   6779  C CA  . CYS D 1 46  ? 11.126  39.276  19.976  1.00 52.62  ? 42  CYS C CA  1 
ATOM   6780  C C   . CYS D 1 46  ? 11.298  39.464  21.470  1.00 49.68  ? 42  CYS C C   1 
ATOM   6781  O O   . CYS D 1 46  ? 11.818  38.593  22.162  1.00 61.18  ? 42  CYS C O   1 
ATOM   6782  C CB  . CYS D 1 46  ? 9.625   39.178  19.693  1.00 60.07  ? 42  CYS C CB  1 
ATOM   6783  S SG  . CYS D 1 46  ? 9.133   39.163  17.955  1.00 71.64  ? 42  CYS C SG  1 
ATOM   6784  N N   . ASP D 1 47  ? 10.828  40.607  21.958  1.00 48.51  ? 43  ASP C N   1 
ATOM   6785  C CA  . ASP D 1 47  ? 10.727  40.863  23.389  1.00 51.32  ? 43  ASP C CA  1 
ATOM   6786  C C   . ASP D 1 47  ? 9.642   39.972  23.979  1.00 52.54  ? 43  ASP C C   1 
ATOM   6787  O O   . ASP D 1 47  ? 8.736   39.541  23.268  1.00 58.91  ? 43  ASP C O   1 
ATOM   6788  C CB  . ASP D 1 47  ? 10.383  42.336  23.660  1.00 55.78  ? 43  ASP C CB  1 
ATOM   6789  C CG  . ASP D 1 47  ? 11.443  43.300  23.139  1.00 61.00  ? 43  ASP C CG  1 
ATOM   6790  O OD1 . ASP D 1 47  ? 12.411  42.844  22.490  1.00 62.56  ? 43  ASP C OD1 1 
ATOM   6791  O OD2 . ASP D 1 47  ? 11.301  44.520  23.372  1.00 62.58  ? 43  ASP C OD2 1 
ATOM   6792  N N   . LEU D 1 48  ? 9.732   39.717  25.281  1.00 51.15  ? 44  LEU C N   1 
ATOM   6793  C CA  . LEU D 1 48  ? 8.767   38.881  25.979  1.00 51.63  ? 44  LEU C CA  1 
ATOM   6794  C C   . LEU D 1 48  ? 8.117   39.695  27.100  1.00 54.74  ? 44  LEU C C   1 
ATOM   6795  O O   . LEU D 1 48  ? 8.743   39.959  28.130  1.00 55.96  ? 44  LEU C O   1 
ATOM   6796  C CB  . LEU D 1 48  ? 9.461   37.637  26.532  1.00 57.47  ? 44  LEU C CB  1 
ATOM   6797  C CG  . LEU D 1 48  ? 8.576   36.392  26.677  1.00 63.73  ? 44  LEU C CG  1 
ATOM   6798  C CD1 . LEU D 1 48  ? 9.413   35.187  27.079  1.00 67.41  ? 44  LEU C CD1 1 
ATOM   6799  C CD2 . LEU D 1 48  ? 7.451   36.616  27.676  1.00 68.74  ? 44  LEU C CD2 1 
ATOM   6800  N N   . ASN D 1 49  ? 6.861   40.089  26.885  1.00 59.53  ? 45  ASN C N   1 
ATOM   6801  C CA  . ASN D 1 49  ? 6.137   40.980  27.802  1.00 60.95  ? 45  ASN C CA  1 
ATOM   6802  C C   . ASN D 1 49  ? 6.898   42.279  28.075  1.00 58.30  ? 45  ASN C C   1 
ATOM   6803  O O   . ASN D 1 49  ? 7.049   42.695  29.224  1.00 55.87  ? 45  ASN C O   1 
ATOM   6804  C CB  . ASN D 1 49  ? 5.796   40.262  29.115  1.00 59.44  ? 45  ASN C CB  1 
ATOM   6805  C CG  . ASN D 1 49  ? 4.898   39.059  28.905  1.00 64.06  ? 45  ASN C CG  1 
ATOM   6806  O OD1 . ASN D 1 49  ? 3.909   39.128  28.175  1.00 69.22  ? 45  ASN C OD1 1 
ATOM   6807  N ND2 . ASN D 1 49  ? 5.232   37.951  29.551  1.00 65.61  ? 45  ASN C ND2 1 
ATOM   6808  N N   . GLY D 1 50  ? 7.388   42.899  27.004  1.00 62.73  ? 46  GLY C N   1 
ATOM   6809  C CA  . GLY D 1 50  ? 8.054   44.199  27.081  1.00 64.21  ? 46  GLY C CA  1 
ATOM   6810  C C   . GLY D 1 50  ? 9.545   44.185  27.380  1.00 68.29  ? 46  GLY C C   1 
ATOM   6811  O O   . GLY D 1 50  ? 10.183  45.239  27.364  1.00 76.32  ? 46  GLY C O   1 
ATOM   6812  N N   . VAL D 1 51  ? 10.113  43.008  27.643  1.00 62.15  ? 47  VAL C N   1 
ATOM   6813  C CA  . VAL D 1 51  ? 11.533  42.903  27.992  1.00 54.94  ? 47  VAL C CA  1 
ATOM   6814  C C   . VAL D 1 51  ? 12.314  42.166  26.906  1.00 54.64  ? 47  VAL C C   1 
ATOM   6815  O O   . VAL D 1 51  ? 11.887  41.120  26.421  1.00 53.23  ? 47  VAL C O   1 
ATOM   6816  C CB  . VAL D 1 51  ? 11.724  42.178  29.330  1.00 46.69  ? 47  VAL C CB  1 
ATOM   6817  C CG1 . VAL D 1 51  ? 13.183  42.229  29.743  1.00 50.21  ? 47  VAL C CG1 1 
ATOM   6818  C CG2 . VAL D 1 51  ? 10.848  42.804  30.403  1.00 43.13  ? 47  VAL C CG2 1 
ATOM   6819  N N   . LYS D 1 52  ? 13.474  42.709  26.553  1.00 56.85  ? 48  LYS C N   1 
ATOM   6820  C CA  . LYS D 1 52  ? 14.268  42.198  25.433  1.00 57.02  ? 48  LYS C CA  1 
ATOM   6821  C C   . LYS D 1 52  ? 15.018  40.943  25.879  1.00 49.97  ? 48  LYS C C   1 
ATOM   6822  O O   . LYS D 1 52  ? 15.294  40.783  27.065  1.00 48.28  ? 48  LYS C O   1 
ATOM   6823  C CB  . LYS D 1 52  ? 15.288  43.240  24.921  1.00 64.30  ? 48  LYS C CB  1 
ATOM   6824  C CG  . LYS D 1 52  ? 14.994  44.706  25.204  1.00 77.79  ? 48  LYS C CG  1 
ATOM   6825  C CD  . LYS D 1 52  ? 16.139  45.618  24.788  1.00 90.58  ? 48  LYS C CD  1 
ATOM   6826  C CE  . LYS D 1 52  ? 15.653  47.042  24.521  1.00 95.41  ? 48  LYS C CE  1 
ATOM   6827  N NZ  . LYS D 1 52  ? 16.765  48.037  24.550  1.00 95.05  ? 48  LYS C NZ  1 
ATOM   6828  N N   . PRO D 1 53  ? 15.345  40.046  24.935  1.00 43.86  ? 49  PRO C N   1 
ATOM   6829  C CA  . PRO D 1 53  ? 16.225  38.930  25.274  1.00 44.81  ? 49  PRO C CA  1 
ATOM   6830  C C   . PRO D 1 53  ? 17.693  39.322  25.282  1.00 47.44  ? 49  PRO C C   1 
ATOM   6831  O O   . PRO D 1 53  ? 18.080  40.278  24.613  1.00 61.40  ? 49  PRO C O   1 
ATOM   6832  C CB  . PRO D 1 53  ? 15.972  37.925  24.148  1.00 45.00  ? 49  PRO C CB  1 
ATOM   6833  C CG  . PRO D 1 53  ? 15.534  38.751  22.992  1.00 44.27  ? 49  PRO C CG  1 
ATOM   6834  C CD  . PRO D 1 53  ? 14.783  39.914  23.578  1.00 43.86  ? 49  PRO C CD  1 
ATOM   6835  N N   . LEU D 1 54  ? 18.495  38.576  26.037  1.00 48.44  ? 50  LEU C N   1 
ATOM   6836  C CA  . LEU D 1 54  ? 19.943  38.690  25.984  1.00 47.59  ? 50  LEU C CA  1 
ATOM   6837  C C   . LEU D 1 54  ? 20.436  37.816  24.837  1.00 50.62  ? 50  LEU C C   1 
ATOM   6838  O O   . LEU D 1 54  ? 20.439  36.587  24.944  1.00 52.88  ? 50  LEU C O   1 
ATOM   6839  C CB  . LEU D 1 54  ? 20.563  38.239  27.309  1.00 51.96  ? 50  LEU C CB  1 
ATOM   6840  C CG  . LEU D 1 54  ? 22.089  38.272  27.429  1.00 52.60  ? 50  LEU C CG  1 
ATOM   6841  C CD1 . LEU D 1 54  ? 22.597  39.703  27.341  1.00 53.45  ? 50  LEU C CD1 1 
ATOM   6842  C CD2 . LEU D 1 54  ? 22.536  37.619  28.728  1.00 46.77  ? 50  LEU C CD2 1 
ATOM   6843  N N   . ILE D 1 55  ? 20.840  38.452  23.736  1.00 59.30  ? 51  ILE C N   1 
ATOM   6844  C CA  . ILE D 1 55  ? 21.307  37.741  22.541  1.00 56.19  ? 51  ILE C CA  1 
ATOM   6845  C C   . ILE D 1 55  ? 22.830  37.707  22.513  1.00 56.05  ? 51  ILE C C   1 
ATOM   6846  O O   . ILE D 1 55  ? 23.479  38.741  22.374  1.00 59.84  ? 51  ILE C O   1 
ATOM   6847  C CB  . ILE D 1 55  ? 20.775  38.395  21.249  1.00 53.28  ? 51  ILE C CB  1 
ATOM   6848  C CG1 . ILE D 1 55  ? 19.246  38.346  21.238  1.00 57.12  ? 51  ILE C CG1 1 
ATOM   6849  C CG2 . ILE D 1 55  ? 21.326  37.685  20.016  1.00 45.92  ? 51  ILE C CG2 1 
ATOM   6850  C CD1 . ILE D 1 55  ? 18.627  39.088  20.079  1.00 59.15  ? 51  ILE C CD1 1 
ATOM   6851  N N   . LEU D 1 56  ? 23.386  36.506  22.654  1.00 58.71  ? 52  LEU C N   1 
ATOM   6852  C CA  . LEU D 1 56  ? 24.824  36.302  22.642  1.00 62.02  ? 52  LEU C CA  1 
ATOM   6853  C C   . LEU D 1 56  ? 25.189  35.809  21.254  1.00 70.36  ? 52  LEU C C   1 
ATOM   6854  O O   . LEU D 1 56  ? 25.037  34.629  20.951  1.00 82.71  ? 52  LEU C O   1 
ATOM   6855  C CB  . LEU D 1 56  ? 25.231  35.278  23.706  1.00 56.52  ? 52  LEU C CB  1 
ATOM   6856  C CG  . LEU D 1 56  ? 24.735  35.559  25.127  1.00 58.51  ? 52  LEU C CG  1 
ATOM   6857  C CD1 . LEU D 1 56  ? 25.056  34.394  26.049  1.00 58.05  ? 52  LEU C CD1 1 
ATOM   6858  C CD2 . LEU D 1 56  ? 25.325  36.846  25.677  1.00 63.96  ? 52  LEU C CD2 1 
ATOM   6859  N N   . LYS D 1 57  ? 25.634  36.730  20.406  1.00 71.21  ? 53  LYS C N   1 
ATOM   6860  C CA  . LYS D 1 57  ? 25.970  36.430  19.007  1.00 76.75  ? 53  LYS C CA  1 
ATOM   6861  C C   . LYS D 1 57  ? 26.535  35.021  18.768  1.00 65.57  ? 53  LYS C C   1 
ATOM   6862  O O   . LYS D 1 57  ? 25.776  34.115  18.436  1.00 63.02  ? 53  LYS C O   1 
ATOM   6863  C CB  . LYS D 1 57  ? 26.912  37.503  18.452  1.00 89.94  ? 53  LYS C CB  1 
ATOM   6864  C CG  . LYS D 1 57  ? 26.251  38.887  18.415  1.00 91.13  ? 53  LYS C CG  1 
ATOM   6865  C CD  . LYS D 1 57  ? 25.956  39.397  16.989  1.00 96.76  ? 53  LYS C CD  1 
ATOM   6866  C CE  . LYS D 1 57  ? 24.552  39.002  16.533  1.00 93.52  ? 53  LYS C CE  1 
ATOM   6867  N NZ  . LYS D 1 57  ? 23.484  39.683  17.319  1.00 84.49  ? 53  LYS C NZ  1 
ATOM   6868  N N   . ASP D 1 58  ? 27.846  34.840  18.920  1.00 60.88  ? 54  ASP C N   1 
ATOM   6869  C CA  . ASP D 1 58  ? 28.467  33.524  18.748  1.00 58.92  ? 54  ASP C CA  1 
ATOM   6870  C C   . ASP D 1 58  ? 29.188  33.101  20.032  1.00 54.12  ? 54  ASP C C   1 
ATOM   6871  O O   . ASP D 1 58  ? 30.040  32.212  20.024  1.00 46.33  ? 54  ASP C O   1 
ATOM   6872  C CB  . ASP D 1 58  ? 29.441  33.553  17.561  1.00 66.71  ? 54  ASP C CB  1 
ATOM   6873  C CG  . ASP D 1 58  ? 29.394  32.279  16.724  1.00 73.78  ? 54  ASP C CG  1 
ATOM   6874  O OD1 . ASP D 1 58  ? 29.138  31.188  17.282  1.00 75.87  ? 54  ASP C OD1 1 
ATOM   6875  O OD2 . ASP D 1 58  ? 29.605  32.374  15.496  1.00 76.10  ? 54  ASP C OD2 1 
ATOM   6876  N N   . CYS D 1 59  ? 28.816  33.743  21.136  1.00 62.68  ? 55  CYS C N   1 
ATOM   6877  C CA  . CYS D 1 59  ? 29.434  33.541  22.435  1.00 66.12  ? 55  CYS C CA  1 
ATOM   6878  C C   . CYS D 1 59  ? 28.507  32.694  23.338  1.00 56.22  ? 55  CYS C C   1 
ATOM   6879  O O   . CYS D 1 59  ? 27.276  32.789  23.260  1.00 55.34  ? 55  CYS C O   1 
ATOM   6880  C CB  . CYS D 1 59  ? 29.752  34.950  22.994  1.00 74.81  ? 55  CYS C CB  1 
ATOM   6881  S SG  . CYS D 1 59  ? 30.982  35.067  24.297  1.00 100.89 ? 55  CYS C SG  1 
ATOM   6882  N N   . SER D 1 60  ? 29.105  31.806  24.133  1.00 49.67  ? 56  SER C N   1 
ATOM   6883  C CA  . SER D 1 60  ? 28.368  31.036  25.134  1.00 44.78  ? 56  SER C CA  1 
ATOM   6884  C C   . SER D 1 60  ? 28.209  31.896  26.379  1.00 41.60  ? 56  SER C C   1 
ATOM   6885  O O   . SER D 1 60  ? 28.837  32.946  26.494  1.00 45.58  ? 56  SER C O   1 
ATOM   6886  C CB  . SER D 1 60  ? 29.121  29.755  25.490  1.00 44.62  ? 56  SER C CB  1 
ATOM   6887  O OG  . SER D 1 60  ? 30.214  30.037  26.345  1.00 49.15  ? 56  SER C OG  1 
ATOM   6888  N N   . VAL D 1 61  ? 27.386  31.443  27.319  1.00 42.07  ? 57  VAL C N   1 
ATOM   6889  C CA  . VAL D 1 61  ? 27.172  32.179  28.569  1.00 40.49  ? 57  VAL C CA  1 
ATOM   6890  C C   . VAL D 1 61  ? 28.476  32.282  29.369  1.00 40.22  ? 57  VAL C C   1 
ATOM   6891  O O   . VAL D 1 61  ? 28.783  33.332  29.937  1.00 38.65  ? 57  VAL C O   1 
ATOM   6892  C CB  . VAL D 1 61  ? 26.075  31.528  29.440  1.00 38.52  ? 57  VAL C CB  1 
ATOM   6893  C CG1 . VAL D 1 61  ? 25.879  32.315  30.726  1.00 37.33  ? 57  VAL C CG1 1 
ATOM   6894  C CG2 . VAL D 1 61  ? 24.762  31.426  28.678  1.00 38.25  ? 57  VAL C CG2 1 
ATOM   6895  N N   . ALA D 1 62  ? 29.244  31.195  29.397  1.00 41.96  ? 58  ALA C N   1 
ATOM   6896  C CA  . ALA D 1 62  ? 30.523  31.169  30.113  1.00 44.13  ? 58  ALA C CA  1 
ATOM   6897  C C   . ALA D 1 62  ? 31.498  32.191  29.534  1.00 45.74  ? 58  ALA C C   1 
ATOM   6898  O O   . ALA D 1 62  ? 32.075  32.995  30.270  1.00 44.24  ? 58  ALA C O   1 
ATOM   6899  C CB  . ALA D 1 62  ? 31.130  29.772  30.068  1.00 41.93  ? 58  ALA C CB  1 
ATOM   6900  N N   . GLY D 1 63  ? 31.659  32.163  28.211  1.00 50.77  ? 59  GLY C N   1 
ATOM   6901  C CA  . GLY D 1 63  ? 32.526  33.109  27.512  1.00 47.30  ? 59  GLY C CA  1 
ATOM   6902  C C   . GLY D 1 63  ? 32.137  34.551  27.784  1.00 44.39  ? 59  GLY C C   1 
ATOM   6903  O O   . GLY D 1 63  ? 32.990  35.400  28.033  1.00 46.28  ? 59  GLY C O   1 
ATOM   6904  N N   . TRP D 1 64  ? 30.838  34.821  27.755  1.00 44.11  ? 60  TRP C N   1 
ATOM   6905  C CA  . TRP D 1 64  ? 30.318  36.161  28.005  1.00 47.37  ? 60  TRP C CA  1 
ATOM   6906  C C   . TRP D 1 64  ? 30.531  36.605  29.435  1.00 48.18  ? 60  TRP C C   1 
ATOM   6907  O O   . TRP D 1 64  ? 30.893  37.752  29.675  1.00 49.89  ? 60  TRP C O   1 
ATOM   6908  C CB  . TRP D 1 64  ? 28.843  36.220  27.614  1.00 53.04  ? 60  TRP C CB  1 
ATOM   6909  C CG  . TRP D 1 64  ? 28.079  37.373  28.211  1.00 54.79  ? 60  TRP C CG  1 
ATOM   6910  C CD1 . TRP D 1 64  ? 28.115  38.708  27.830  1.00 54.44  ? 60  TRP C CD1 1 
ATOM   6911  C CD2 . TRP D 1 64  ? 27.124  37.318  29.317  1.00 55.54  ? 60  TRP C CD2 1 
ATOM   6912  N NE1 . TRP D 1 64  ? 27.276  39.465  28.607  1.00 58.71  ? 60  TRP C NE1 1 
ATOM   6913  C CE2 . TRP D 1 64  ? 26.652  38.691  29.519  1.00 58.47  ? 60  TRP C CE2 1 
ATOM   6914  C CE3 . TRP D 1 64  ? 26.632  36.310  30.129  1.00 56.77  ? 60  TRP C CE3 1 
ATOM   6915  C CZ2 . TRP D 1 64  ? 25.731  39.012  30.497  1.00 57.22  ? 60  TRP C CZ2 1 
ATOM   6916  C CZ3 . TRP D 1 64  ? 25.701  36.646  31.114  1.00 60.58  ? 60  TRP C CZ3 1 
ATOM   6917  C CH2 . TRP D 1 64  ? 25.263  37.967  31.292  1.00 63.15  ? 60  TRP C CH2 1 
ATOM   6918  N N   . LEU D 1 65  ? 30.321  35.706  30.393  1.00 49.59  ? 61  LEU C N   1 
ATOM   6919  C CA  . LEU D 1 65  ? 30.521  36.028  31.813  1.00 51.53  ? 61  LEU C CA  1 
ATOM   6920  C C   . LEU D 1 65  ? 31.981  36.310  32.154  1.00 52.79  ? 61  LEU C C   1 
ATOM   6921  O O   . LEU D 1 65  ? 32.289  37.255  32.886  1.00 49.64  ? 61  LEU C O   1 
ATOM   6922  C CB  . LEU D 1 65  ? 30.029  34.884  32.710  1.00 50.67  ? 61  LEU C CB  1 
ATOM   6923  C CG  . LEU D 1 65  ? 28.564  34.891  33.141  1.00 46.02  ? 61  LEU C CG  1 
ATOM   6924  C CD1 . LEU D 1 65  ? 28.288  33.710  34.056  1.00 47.19  ? 61  LEU C CD1 1 
ATOM   6925  C CD2 . LEU D 1 65  ? 28.231  36.189  33.846  1.00 40.35  ? 61  LEU C CD2 1 
ATOM   6926  N N   . LEU D 1 66  ? 32.869  35.469  31.635  1.00 48.53  ? 62  LEU C N   1 
ATOM   6927  C CA  . LEU D 1 66  ? 34.289  35.528  31.975  1.00 50.47  ? 62  LEU C CA  1 
ATOM   6928  C C   . LEU D 1 66  ? 35.053  36.619  31.225  1.00 51.52  ? 62  LEU C C   1 
ATOM   6929  O O   . LEU D 1 66  ? 36.088  37.082  31.701  1.00 58.13  ? 62  LEU C O   1 
ATOM   6930  C CB  . LEU D 1 66  ? 34.948  34.169  31.714  1.00 48.89  ? 62  LEU C CB  1 
ATOM   6931  C CG  . LEU D 1 66  ? 34.462  33.011  32.582  1.00 40.88  ? 62  LEU C CG  1 
ATOM   6932  C CD1 . LEU D 1 66  ? 34.739  31.683  31.902  1.00 40.20  ? 62  LEU C CD1 1 
ATOM   6933  C CD2 . LEU D 1 66  ? 35.112  33.056  33.954  1.00 44.51  ? 62  LEU C CD2 1 
ATOM   6934  N N   . GLY D 1 67  ? 34.556  37.017  30.055  1.00 55.32  ? 63  GLY C N   1 
ATOM   6935  C CA  . GLY D 1 67  ? 35.191  38.072  29.261  1.00 53.85  ? 63  GLY C CA  1 
ATOM   6936  C C   . GLY D 1 67  ? 36.141  37.573  28.180  1.00 51.35  ? 63  GLY C C   1 
ATOM   6937  O O   . GLY D 1 67  ? 37.138  38.238  27.876  1.00 61.81  ? 63  GLY C O   1 
ATOM   6938  N N   . ASN D 1 68  ? 35.851  36.400  27.614  1.00 48.56  ? 64  ASN C N   1 
ATOM   6939  C CA  . ASN D 1 68  ? 36.565  35.886  26.439  1.00 54.57  ? 64  ASN C CA  1 
ATOM   6940  C C   . ASN D 1 68  ? 36.907  37.030  25.465  1.00 60.01  ? 64  ASN C C   1 
ATOM   6941  O O   . ASN D 1 68  ? 36.018  37.790  25.079  1.00 55.03  ? 64  ASN C O   1 
ATOM   6942  C CB  . ASN D 1 68  ? 35.705  34.824  25.734  1.00 56.28  ? 64  ASN C CB  1 
ATOM   6943  C CG  . ASN D 1 68  ? 36.462  34.041  24.662  1.00 58.67  ? 64  ASN C CG  1 
ATOM   6944  O OD1 . ASN D 1 68  ? 37.285  34.587  23.931  1.00 61.13  ? 64  ASN C OD1 1 
ATOM   6945  N ND2 . ASN D 1 68  ? 36.152  32.751  24.544  1.00 55.48  ? 64  ASN C ND2 1 
ATOM   6946  N N   . PRO D 1 69  ? 38.197  37.172  25.088  1.00 67.54  ? 65  PRO C N   1 
ATOM   6947  C CA  . PRO D 1 69  ? 38.638  38.237  24.173  1.00 74.55  ? 65  PRO C CA  1 
ATOM   6948  C C   . PRO D 1 69  ? 37.892  38.294  22.834  1.00 78.10  ? 65  PRO C C   1 
ATOM   6949  O O   . PRO D 1 69  ? 37.644  39.384  22.315  1.00 73.15  ? 65  PRO C O   1 
ATOM   6950  C CB  . PRO D 1 69  ? 40.107  37.892  23.930  1.00 77.48  ? 65  PRO C CB  1 
ATOM   6951  C CG  . PRO D 1 69  ? 40.535  37.199  25.166  1.00 78.46  ? 65  PRO C CG  1 
ATOM   6952  C CD  . PRO D 1 69  ? 39.344  36.394  25.600  1.00 75.54  ? 65  PRO C CD  1 
ATOM   6953  N N   . MET D 1 70  ? 37.545  37.127  22.293  1.00 79.05  ? 66  MET C N   1 
ATOM   6954  C CA  . MET D 1 70  ? 36.833  37.023  21.015  1.00 86.13  ? 66  MET C CA  1 
ATOM   6955  C C   . MET D 1 70  ? 35.353  37.460  21.111  1.00 86.43  ? 66  MET C C   1 
ATOM   6956  O O   . MET D 1 70  ? 34.683  37.629  20.090  1.00 85.81  ? 66  MET C O   1 
ATOM   6957  C CB  . MET D 1 70  ? 36.957  35.587  20.478  1.00 87.48  ? 66  MET C CB  1 
ATOM   6958  C CG  . MET D 1 70  ? 38.392  35.222  19.991  1.00 96.40  ? 66  MET C CG  1 
ATOM   6959  S SD  . MET D 1 70  ? 38.749  35.583  18.247  1.00 110.77 ? 66  MET C SD  1 
ATOM   6960  C CE  . MET D 1 70  ? 40.470  35.101  18.123  1.00 112.53 ? 66  MET C CE  1 
ATOM   6961  N N   . CYS D 1 71  ? 34.857  37.647  22.333  1.00 84.11  ? 67  CYS C N   1 
ATOM   6962  C CA  . CYS D 1 71  ? 33.519  38.198  22.577  1.00 90.03  ? 67  CYS C CA  1 
ATOM   6963  C C   . CYS D 1 71  ? 33.639  39.703  22.831  1.00 97.41  ? 67  CYS C C   1 
ATOM   6964  O O   . CYS D 1 71  ? 34.718  40.263  22.676  1.00 106.27 ? 67  CYS C O   1 
ATOM   6965  C CB  . CYS D 1 71  ? 32.879  37.461  23.763  1.00 94.11  ? 67  CYS C CB  1 
ATOM   6966  S SG  . CYS D 1 71  ? 32.654  35.715  23.366  1.00 90.67  ? 67  CYS C SG  1 
ATOM   6967  N N   . ASP D 1 72  ? 32.538  40.362  23.187  1.00 98.05  ? 68  ASP C N   1 
ATOM   6968  C CA  . ASP D 1 72  ? 32.570  41.788  23.567  1.00 99.08  ? 68  ASP C CA  1 
ATOM   6969  C C   . ASP D 1 72  ? 31.800  42.047  24.860  1.00 97.79  ? 68  ASP C C   1 
ATOM   6970  O O   . ASP D 1 72  ? 30.940  41.259  25.243  1.00 96.14  ? 68  ASP C O   1 
ATOM   6971  C CB  . ASP D 1 72  ? 32.034  42.690  22.441  1.00 98.28  ? 68  ASP C CB  1 
ATOM   6972  C CG  . ASP D 1 72  ? 30.679  42.246  21.916  1.00 97.44  ? 68  ASP C CG  1 
ATOM   6973  O OD1 . ASP D 1 72  ? 30.622  41.183  21.254  1.00 88.64  ? 68  ASP C OD1 1 
ATOM   6974  O OD2 . ASP D 1 72  ? 29.681  42.971  22.152  1.00 97.93  ? 68  ASP C OD2 1 
ATOM   6975  N N   . GLU D 1 73  ? 32.123  43.158  25.521  1.00 109.63 ? 69  GLU C N   1 
ATOM   6976  C CA  . GLU D 1 73  ? 31.437  43.584  26.747  1.00 120.98 ? 69  GLU C CA  1 
ATOM   6977  C C   . GLU D 1 73  ? 30.353  44.631  26.477  1.00 131.34 ? 69  GLU C C   1 
ATOM   6978  O O   . GLU D 1 73  ? 29.786  45.171  27.427  1.00 114.09 ? 69  GLU C O   1 
ATOM   6979  C CB  . GLU D 1 73  ? 32.438  44.135  27.783  1.00 119.79 ? 69  GLU C CB  1 
ATOM   6980  C CG  . GLU D 1 73  ? 32.963  45.548  27.522  1.00 123.75 ? 69  GLU C CG  1 
ATOM   6981  C CD  . GLU D 1 73  ? 34.123  45.588  26.541  1.00 120.92 ? 69  GLU C CD  1 
ATOM   6982  O OE1 . GLU D 1 73  ? 34.212  44.701  25.666  1.00 119.72 ? 69  GLU C OE1 1 
ATOM   6983  O OE2 . GLU D 1 73  ? 34.948  46.517  26.637  1.00 111.75 ? 69  GLU C OE2 1 
ATOM   6984  N N   . PHE D 1 74  ? 30.071  44.914  25.200  1.00 149.69 ? 70  PHE C N   1 
ATOM   6985  C CA  . PHE D 1 74  ? 28.992  45.843  24.824  1.00 155.24 ? 70  PHE C CA  1 
ATOM   6986  C C   . PHE D 1 74  ? 27.657  45.098  24.725  1.00 147.96 ? 70  PHE C C   1 
ATOM   6987  O O   . PHE D 1 74  ? 26.782  45.477  23.947  1.00 137.01 ? 70  PHE C O   1 
ATOM   6988  C CB  . PHE D 1 74  ? 29.281  46.551  23.492  1.00 163.90 ? 70  PHE C CB  1 
ATOM   6989  C CG  . PHE D 1 74  ? 28.260  47.611  23.132  1.00 171.01 ? 70  PHE C CG  1 
ATOM   6990  C CD1 . PHE D 1 74  ? 27.484  47.492  21.981  1.00 166.22 ? 70  PHE C CD1 1 
ATOM   6991  C CD2 . PHE D 1 74  ? 28.048  48.706  23.963  1.00 171.90 ? 70  PHE C CD2 1 
ATOM   6992  C CE1 . PHE D 1 74  ? 26.534  48.450  21.660  1.00 161.73 ? 70  PHE C CE1 1 
ATOM   6993  C CE2 . PHE D 1 74  ? 27.099  49.669  23.646  1.00 167.36 ? 70  PHE C CE2 1 
ATOM   6994  C CZ  . PHE D 1 74  ? 26.342  49.541  22.493  1.00 162.57 ? 70  PHE C CZ  1 
ATOM   6995  N N   . ILE D 1 75  ? 27.514  44.030  25.505  1.00 147.14 ? 71  ILE C N   1 
ATOM   6996  C CA  . ILE D 1 75  ? 26.247  43.342  25.658  1.00 142.73 ? 71  ILE C CA  1 
ATOM   6997  C C   . ILE D 1 75  ? 25.696  43.753  27.031  1.00 140.31 ? 71  ILE C C   1 
ATOM   6998  O O   . ILE D 1 75  ? 24.800  43.106  27.570  1.00 147.22 ? 71  ILE C O   1 
ATOM   6999  C CB  . ILE D 1 75  ? 26.400  41.803  25.564  1.00 130.54 ? 71  ILE C CB  1 
ATOM   7000  C CG1 . ILE D 1 75  ? 27.278  41.370  24.371  1.00 121.45 ? 71  ILE C CG1 1 
ATOM   7001  C CG2 . ILE D 1 75  ? 25.036  41.139  25.447  1.00 130.38 ? 71  ILE C CG2 1 
ATOM   7002  C CD1 . ILE D 1 75  ? 27.380  39.869  24.201  1.00 116.56 ? 71  ILE C CD1 1 
ATOM   7003  N N   . ASN D 1 76  ? 26.247  44.832  27.594  1.00 128.70 ? 72  ASN C N   1 
ATOM   7004  C CA  . ASN D 1 76  ? 25.812  45.334  28.912  1.00 117.59 ? 72  ASN C CA  1 
ATOM   7005  C C   . ASN D 1 76  ? 24.380  45.878  28.903  1.00 106.68 ? 72  ASN C C   1 
ATOM   7006  O O   . ASN D 1 76  ? 24.119  46.977  28.407  1.00 103.46 ? 72  ASN C O   1 
ATOM   7007  C CB  . ASN D 1 76  ? 26.779  46.399  29.452  1.00 113.27 ? 72  ASN C CB  1 
ATOM   7008  C CG  . ASN D 1 76  ? 28.022  45.792  30.084  1.00 120.52 ? 72  ASN C CG  1 
ATOM   7009  O OD1 . ASN D 1 76  ? 28.207  44.572  30.081  1.00 124.58 ? 72  ASN C OD1 1 
ATOM   7010  N ND2 . ASN D 1 76  ? 28.877  46.644  30.640  1.00 115.96 ? 72  ASN C ND2 1 
ATOM   7011  N N   . VAL D 1 77  ? 23.463  45.077  29.440  1.00 96.89  ? 73  VAL C N   1 
ATOM   7012  C CA  . VAL D 1 77  ? 22.066  45.458  29.631  1.00 91.71  ? 73  VAL C CA  1 
ATOM   7013  C C   . VAL D 1 77  ? 21.582  44.831  30.929  1.00 75.67  ? 73  VAL C C   1 
ATOM   7014  O O   . VAL D 1 77  ? 21.771  43.631  31.163  1.00 71.57  ? 73  VAL C O   1 
ATOM   7015  C CB  . VAL D 1 77  ? 21.171  44.992  28.466  1.00 97.38  ? 73  VAL C CB  1 
ATOM   7016  C CG1 . VAL D 1 77  ? 19.702  45.219  28.791  1.00 93.03  ? 73  VAL C CG1 1 
ATOM   7017  C CG2 . VAL D 1 77  ? 21.550  45.708  27.178  1.00 103.11 ? 73  VAL C CG2 1 
ATOM   7018  N N   . PRO D 1 78  ? 20.945  45.641  31.778  1.00 68.48  ? 74  PRO C N   1 
ATOM   7019  C CA  . PRO D 1 78  ? 20.618  45.161  33.107  1.00 70.22  ? 74  PRO C CA  1 
ATOM   7020  C C   . PRO D 1 78  ? 19.354  44.313  33.204  1.00 68.47  ? 74  PRO C C   1 
ATOM   7021  O O   . PRO D 1 78  ? 19.089  43.786  34.282  1.00 68.08  ? 74  PRO C O   1 
ATOM   7022  C CB  . PRO D 1 78  ? 20.409  46.457  33.880  1.00 72.04  ? 74  PRO C CB  1 
ATOM   7023  C CG  . PRO D 1 78  ? 19.814  47.373  32.862  1.00 71.98  ? 74  PRO C CG  1 
ATOM   7024  C CD  . PRO D 1 78  ? 20.510  47.036  31.572  1.00 65.80  ? 74  PRO C CD  1 
ATOM   7025  N N   . GLU D 1 79  ? 18.587  44.200  32.114  1.00 68.38  ? 75  GLU C N   1 
ATOM   7026  C CA  . GLU D 1 79  ? 17.346  43.414  32.094  1.00 64.80  ? 75  GLU C CA  1 
ATOM   7027  C C   . GLU D 1 79  ? 17.233  42.520  30.864  1.00 61.16  ? 75  GLU C C   1 
ATOM   7028  O O   . GLU D 1 79  ? 17.473  42.965  29.740  1.00 64.26  ? 75  GLU C O   1 
ATOM   7029  C CB  . GLU D 1 79  ? 16.081  44.315  32.161  1.00 61.73  ? 75  GLU C CB  1 
ATOM   7030  C CG  . GLU D 1 79  ? 15.201  44.067  33.394  1.00 75.45  ? 75  GLU C CG  1 
ATOM   7031  C CD  . GLU D 1 79  ? 13.704  44.107  33.131  1.00 89.79  ? 75  GLU C CD  1 
ATOM   7032  O OE1 . GLU D 1 79  ? 13.283  44.477  32.015  1.00 95.03  ? 75  GLU C OE1 1 
ATOM   7033  O OE2 . GLU D 1 79  ? 12.940  43.761  34.066  1.00 90.64  ? 75  GLU C OE2 1 
ATOM   7034  N N   . TRP D 1 80  ? 16.858  41.261  31.087  1.00 53.55  ? 76  TRP C N   1 
ATOM   7035  C CA  . TRP D 1 80  ? 16.452  40.382  29.990  1.00 52.13  ? 76  TRP C CA  1 
ATOM   7036  C C   . TRP D 1 80  ? 15.464  39.337  30.446  1.00 47.69  ? 76  TRP C C   1 
ATOM   7037  O O   . TRP D 1 80  ? 15.356  39.047  31.637  1.00 47.93  ? 76  TRP C O   1 
ATOM   7038  C CB  . TRP D 1 80  ? 17.659  39.746  29.309  1.00 46.45  ? 76  TRP C CB  1 
ATOM   7039  C CG  . TRP D 1 80  ? 18.437  38.812  30.198  1.00 52.08  ? 76  TRP C CG  1 
ATOM   7040  C CD1 . TRP D 1 80  ? 18.170  37.472  30.457  1.00 55.04  ? 76  TRP C CD1 1 
ATOM   7041  C CD2 . TRP D 1 80  ? 19.646  39.117  30.974  1.00 52.35  ? 76  TRP C CD2 1 
ATOM   7042  N NE1 . TRP D 1 80  ? 19.098  36.947  31.313  1.00 55.60  ? 76  TRP C NE1 1 
ATOM   7043  C CE2 . TRP D 1 80  ? 20.010  37.880  31.663  1.00 55.64  ? 76  TRP C CE2 1 
ATOM   7044  C CE3 . TRP D 1 80  ? 20.430  40.247  31.162  1.00 50.31  ? 76  TRP C CE3 1 
ATOM   7045  C CZ2 . TRP D 1 80  ? 21.115  37.801  32.495  1.00 51.34  ? 76  TRP C CZ2 1 
ATOM   7046  C CZ3 . TRP D 1 80  ? 21.540  40.153  32.010  1.00 55.28  ? 76  TRP C CZ3 1 
ATOM   7047  C CH2 . TRP D 1 80  ? 21.873  38.956  32.656  1.00 52.01  ? 76  TRP C CH2 1 
ATOM   7048  N N   . SER D 1 81  ? 14.719  38.790  29.488  1.00 42.57  ? 77  SER C N   1 
ATOM   7049  C CA  . SER D 1 81  ? 13.638  37.840  29.760  1.00 45.40  ? 77  SER C CA  1 
ATOM   7050  C C   . SER D 1 81  ? 14.023  36.401  29.419  1.00 43.22  ? 77  SER C C   1 
ATOM   7051  O O   . SER D 1 81  ? 13.552  35.468  30.054  1.00 43.64  ? 77  SER C O   1 
ATOM   7052  C CB  . SER D 1 81  ? 12.389  38.237  28.969  1.00 45.71  ? 77  SER C CB  1 
ATOM   7053  O OG  . SER D 1 81  ? 12.696  38.408  27.595  1.00 45.02  ? 77  SER C OG  1 
ATOM   7054  N N   . TYR D 1 82  ? 14.838  36.229  28.384  1.00 42.21  ? 78  TYR C N   1 
ATOM   7055  C CA  . TYR D 1 82  ? 15.423  34.933  28.059  1.00 43.09  ? 78  TYR C CA  1 
ATOM   7056  C C   . TYR D 1 82  ? 16.768  35.137  27.364  1.00 42.97  ? 78  TYR C C   1 
ATOM   7057  O O   . TYR D 1 82  ? 17.124  36.262  27.030  1.00 45.94  ? 78  TYR C O   1 
ATOM   7058  C CB  . TYR D 1 82  ? 14.471  34.084  27.212  1.00 43.56  ? 78  TYR C CB  1 
ATOM   7059  C CG  . TYR D 1 82  ? 14.110  34.654  25.855  1.00 46.55  ? 78  TYR C CG  1 
ATOM   7060  C CD1 . TYR D 1 82  ? 14.670  34.136  24.688  1.00 43.20  ? 78  TYR C CD1 1 
ATOM   7061  C CD2 . TYR D 1 82  ? 13.188  35.689  25.737  1.00 46.00  ? 78  TYR C CD2 1 
ATOM   7062  C CE1 . TYR D 1 82  ? 14.334  34.646  23.447  1.00 45.02  ? 78  TYR C CE1 1 
ATOM   7063  C CE2 . TYR D 1 82  ? 12.844  36.205  24.501  1.00 45.21  ? 78  TYR C CE2 1 
ATOM   7064  C CZ  . TYR D 1 82  ? 13.421  35.682  23.359  1.00 48.06  ? 78  TYR C CZ  1 
ATOM   7065  O OH  . TYR D 1 82  ? 13.087  36.194  22.129  1.00 51.03  ? 78  TYR C OH  1 
ATOM   7066  N N   . ILE D 1 83  ? 17.516  34.053  27.178  1.00 41.82  ? 79  ILE C N   1 
ATOM   7067  C CA  . ILE D 1 83  ? 18.850  34.115  26.586  1.00 41.12  ? 79  ILE C CA  1 
ATOM   7068  C C   . ILE D 1 83  ? 18.878  33.347  25.272  1.00 41.26  ? 79  ILE C C   1 
ATOM   7069  O O   . ILE D 1 83  ? 18.339  32.247  25.184  1.00 43.58  ? 79  ILE C O   1 
ATOM   7070  C CB  . ILE D 1 83  ? 19.912  33.513  27.530  1.00 43.40  ? 79  ILE C CB  1 
ATOM   7071  C CG1 . ILE D 1 83  ? 20.088  34.395  28.771  1.00 44.88  ? 79  ILE C CG1 1 
ATOM   7072  C CG2 . ILE D 1 83  ? 21.247  33.340  26.811  1.00 39.78  ? 79  ILE C CG2 1 
ATOM   7073  C CD1 . ILE D 1 83  ? 21.073  33.846  29.778  1.00 44.79  ? 79  ILE C CD1 1 
ATOM   7074  N N   . VAL D 1 84  ? 19.507  33.930  24.255  1.00 46.22  ? 80  VAL C N   1 
ATOM   7075  C CA  . VAL D 1 84  ? 19.661  33.264  22.965  1.00 46.71  ? 80  VAL C CA  1 
ATOM   7076  C C   . VAL D 1 84  ? 21.124  32.946  22.685  1.00 46.01  ? 80  VAL C C   1 
ATOM   7077  O O   . VAL D 1 84  ? 21.948  33.849  22.556  1.00 57.06  ? 80  VAL C O   1 
ATOM   7078  C CB  . VAL D 1 84  ? 19.112  34.116  21.813  1.00 50.27  ? 80  VAL C CB  1 
ATOM   7079  C CG1 . VAL D 1 84  ? 19.155  33.320  20.514  1.00 44.96  ? 80  VAL C CG1 1 
ATOM   7080  C CG2 . VAL D 1 84  ? 17.692  34.568  22.125  1.00 50.43  ? 80  VAL C CG2 1 
ATOM   7081  N N   . GLU D 1 85  ? 21.432  31.655  22.617  1.00 45.45  ? 81  GLU C N   1 
ATOM   7082  C CA  . GLU D 1 85  ? 22.728  31.164  22.161  1.00 49.62  ? 81  GLU C CA  1 
ATOM   7083  C C   . GLU D 1 85  ? 22.524  30.511  20.802  1.00 51.50  ? 81  GLU C C   1 
ATOM   7084  O O   . GLU D 1 85  ? 21.402  30.171  20.438  1.00 53.81  ? 81  GLU C O   1 
ATOM   7085  C CB  . GLU D 1 85  ? 23.275  30.093  23.110  1.00 52.93  ? 81  GLU C CB  1 
ATOM   7086  C CG  . GLU D 1 85  ? 23.830  30.581  24.439  1.00 53.97  ? 81  GLU C CG  1 
ATOM   7087  C CD  . GLU D 1 85  ? 24.471  29.449  25.237  1.00 56.09  ? 81  GLU C CD  1 
ATOM   7088  O OE1 . GLU D 1 85  ? 23.990  28.296  25.140  1.00 46.75  ? 81  GLU C OE1 1 
ATOM   7089  O OE2 . GLU D 1 85  ? 25.454  29.708  25.969  1.00 59.53  ? 81  GLU C OE2 1 
ATOM   7090  N N   . LYS D 1 86  ? 23.610  30.320  20.063  1.00 51.22  ? 82  LYS C N   1 
ATOM   7091  C CA  . LYS D 1 86  ? 23.576  29.475  18.882  1.00 51.82  ? 82  LYS C CA  1 
ATOM   7092  C C   . LYS D 1 86  ? 23.720  28.030  19.336  1.00 52.57  ? 82  LYS C C   1 
ATOM   7093  O O   . LYS D 1 86  ? 24.054  27.769  20.495  1.00 55.62  ? 82  LYS C O   1 
ATOM   7094  C CB  . LYS D 1 86  ? 24.699  29.834  17.914  1.00 59.46  ? 82  LYS C CB  1 
ATOM   7095  C CG  . LYS D 1 86  ? 24.601  31.245  17.366  1.00 65.72  ? 82  LYS C CG  1 
ATOM   7096  C CD  . LYS D 1 86  ? 24.951  31.260  15.863  1.00 73.92  ? 82  LYS C CD  1 
ATOM   7097  C CE  . LYS D 1 86  ? 26.222  32.042  15.570  1.00 79.82  ? 82  LYS C CE  1 
ATOM   7098  N NZ  . LYS D 1 86  ? 26.513  32.108  14.112  1.00 80.86  ? 82  LYS C NZ  1 
ATOM   7099  N N   . ALA D 1 87  ? 23.461  27.097  18.425  1.00 51.47  ? 83  ALA C N   1 
ATOM   7100  C CA  . ALA D 1 87  ? 23.544  25.671  18.731  1.00 53.26  ? 83  ALA C CA  1 
ATOM   7101  C C   . ALA D 1 87  ? 24.930  25.292  19.266  1.00 57.11  ? 83  ALA C C   1 
ATOM   7102  O O   . ALA D 1 87  ? 25.043  24.590  20.274  1.00 53.72  ? 83  ALA C O   1 
ATOM   7103  C CB  . ALA D 1 87  ? 23.192  24.844  17.501  1.00 49.88  ? 83  ALA C CB  1 
ATOM   7104  N N   . ASN D 1 88  ? 25.977  25.770  18.596  1.00 62.73  ? 84  ASN C N   1 
ATOM   7105  C CA  . ASN D 1 88  ? 27.359  25.518  19.021  1.00 65.36  ? 84  ASN C CA  1 
ATOM   7106  C C   . ASN D 1 88  ? 28.200  26.791  18.931  1.00 59.39  ? 84  ASN C C   1 
ATOM   7107  O O   . ASN D 1 88  ? 28.843  27.037  17.912  1.00 59.59  ? 84  ASN C O   1 
ATOM   7108  C CB  . ASN D 1 88  ? 27.984  24.404  18.177  1.00 68.41  ? 84  ASN C CB  1 
ATOM   7109  C CG  . ASN D 1 88  ? 27.282  23.064  18.363  1.00 76.09  ? 84  ASN C CG  1 
ATOM   7110  O OD1 . ASN D 1 88  ? 27.354  22.456  19.430  1.00 83.95  ? 84  ASN C OD1 1 
ATOM   7111  N ND2 . ASN D 1 88  ? 26.602  22.598  17.319  1.00 64.09  ? 84  ASN C ND2 1 
ATOM   7112  N N   . PRO D 1 89  ? 28.191  27.613  19.999  1.00 61.42  ? 85  PRO C N   1 
ATOM   7113  C CA  . PRO D 1 89  ? 28.944  28.870  19.976  1.00 64.03  ? 85  PRO C CA  1 
ATOM   7114  C C   . PRO D 1 89  ? 30.433  28.627  19.765  1.00 69.67  ? 85  PRO C C   1 
ATOM   7115  O O   . PRO D 1 89  ? 30.992  27.700  20.356  1.00 74.14  ? 85  PRO C O   1 
ATOM   7116  C CB  . PRO D 1 89  ? 28.689  29.473  21.367  1.00 61.60  ? 85  PRO C CB  1 
ATOM   7117  C CG  . PRO D 1 89  ? 27.466  28.790  21.871  1.00 59.57  ? 85  PRO C CG  1 
ATOM   7118  C CD  . PRO D 1 89  ? 27.494  27.414  21.282  1.00 56.12  ? 85  PRO C CD  1 
ATOM   7119  N N   . ALA D 1 90  ? 31.055  29.452  18.925  1.00 68.87  ? 86  ALA C N   1 
ATOM   7120  C CA  . ALA D 1 90  ? 32.477  29.315  18.601  1.00 65.13  ? 86  ALA C CA  1 
ATOM   7121  C C   . ALA D 1 90  ? 33.368  29.824  19.733  1.00 57.54  ? 86  ALA C C   1 
ATOM   7122  O O   . ALA D 1 90  ? 34.471  29.318  19.927  1.00 52.26  ? 86  ALA C O   1 
ATOM   7123  C CB  . ALA D 1 90  ? 32.799  30.057  17.309  1.00 62.30  ? 86  ALA C CB  1 
ATOM   7124  N N   . ASN D 1 91  ? 32.884  30.823  20.469  1.00 51.51  ? 87  ASN C N   1 
ATOM   7125  C CA  . ASN D 1 91  ? 33.649  31.440  21.544  1.00 53.79  ? 87  ASN C CA  1 
ATOM   7126  C C   . ASN D 1 91  ? 33.119  31.047  22.924  1.00 53.69  ? 87  ASN C C   1 
ATOM   7127  O O   . ASN D 1 91  ? 32.278  31.741  23.503  1.00 47.87  ? 87  ASN C O   1 
ATOM   7128  C CB  . ASN D 1 91  ? 33.634  32.962  21.387  1.00 61.11  ? 87  ASN C CB  1 
ATOM   7129  C CG  . ASN D 1 91  ? 34.051  33.413  19.997  1.00 62.33  ? 87  ASN C CG  1 
ATOM   7130  O OD1 . ASN D 1 91  ? 33.477  34.352  19.441  1.00 58.72  ? 87  ASN C OD1 1 
ATOM   7131  N ND2 . ASN D 1 91  ? 35.046  32.744  19.426  1.00 62.52  ? 87  ASN C ND2 1 
ATOM   7132  N N   . ASP D 1 92  ? 33.623  29.928  23.439  1.00 53.99  ? 88  ASP C N   1 
ATOM   7133  C CA  . ASP D 1 92  ? 33.213  29.406  24.736  1.00 55.05  ? 88  ASP C CA  1 
ATOM   7134  C C   . ASP D 1 92  ? 34.338  29.658  25.756  1.00 51.64  ? 88  ASP C C   1 
ATOM   7135  O O   . ASP D 1 92  ? 34.489  30.787  26.234  1.00 51.67  ? 88  ASP C O   1 
ATOM   7136  C CB  . ASP D 1 92  ? 32.833  27.919  24.597  1.00 65.64  ? 88  ASP C CB  1 
ATOM   7137  C CG  . ASP D 1 92  ? 32.163  27.346  25.846  1.00 76.17  ? 88  ASP C CG  1 
ATOM   7138  O OD1 . ASP D 1 92  ? 31.869  28.101  26.799  1.00 80.19  ? 88  ASP C OD1 1 
ATOM   7139  O OD2 . ASP D 1 92  ? 31.925  26.121  25.867  1.00 85.48  ? 88  ASP C OD2 1 
ATOM   7140  N N   . LEU D 1 93  ? 35.117  28.627  26.091  1.00 45.28  ? 89  LEU C N   1 
ATOM   7141  C CA  . LEU D 1 93  ? 36.276  28.777  26.969  1.00 51.36  ? 89  LEU C CA  1 
ATOM   7142  C C   . LEU D 1 93  ? 37.530  28.768  26.109  1.00 46.65  ? 89  LEU C C   1 
ATOM   7143  O O   . LEU D 1 93  ? 37.984  27.705  25.682  1.00 46.10  ? 89  LEU C O   1 
ATOM   7144  C CB  . LEU D 1 93  ? 36.334  27.633  27.990  1.00 51.19  ? 89  LEU C CB  1 
ATOM   7145  C CG  . LEU D 1 93  ? 35.185  27.544  28.997  1.00 49.35  ? 89  LEU C CG  1 
ATOM   7146  C CD1 . LEU D 1 93  ? 35.276  26.236  29.772  1.00 46.17  ? 89  LEU C CD1 1 
ATOM   7147  C CD2 . LEU D 1 93  ? 35.185  28.744  29.937  1.00 49.81  ? 89  LEU C CD2 1 
ATOM   7148  N N   . CYS D 1 94  ? 38.080  29.950  25.843  1.00 52.93  ? 90  CYS C N   1 
ATOM   7149  C CA  . CYS D 1 94  ? 39.239  30.067  24.953  1.00 54.28  ? 90  CYS C CA  1 
ATOM   7150  C C   . CYS D 1 94  ? 40.408  29.239  25.482  1.00 51.57  ? 90  CYS C C   1 
ATOM   7151  O O   . CYS D 1 94  ? 41.006  28.451  24.740  1.00 44.74  ? 90  CYS C O   1 
ATOM   7152  C CB  . CYS D 1 94  ? 39.642  31.530  24.749  1.00 52.37  ? 90  CYS C CB  1 
ATOM   7153  S SG  . CYS D 1 94  ? 40.030  32.452  26.253  1.00 63.22  ? 90  CYS C SG  1 
ATOM   7154  N N   . TYR D 1 95  ? 40.711  29.402  26.768  1.00 53.54  ? 91  TYR C N   1 
ATOM   7155  C CA  . TYR D 1 95  ? 41.625  28.494  27.454  1.00 51.53  ? 91  TYR C CA  1 
ATOM   7156  C C   . TYR D 1 95  ? 40.800  27.302  27.927  1.00 46.64  ? 91  TYR C C   1 
ATOM   7157  O O   . TYR D 1 95  ? 39.808  27.484  28.634  1.00 49.86  ? 91  TYR C O   1 
ATOM   7158  C CB  . TYR D 1 95  ? 42.313  29.177  28.640  1.00 55.48  ? 91  TYR C CB  1 
ATOM   7159  C CG  . TYR D 1 95  ? 43.549  28.439  29.114  1.00 55.67  ? 91  TYR C CG  1 
ATOM   7160  C CD1 . TYR D 1 95  ? 44.819  28.819  28.686  1.00 56.36  ? 91  TYR C CD1 1 
ATOM   7161  C CD2 . TYR D 1 95  ? 43.448  27.355  29.979  1.00 59.00  ? 91  TYR C CD2 1 
ATOM   7162  C CE1 . TYR D 1 95  ? 45.953  28.145  29.114  1.00 53.81  ? 91  TYR C CE1 1 
ATOM   7163  C CE2 . TYR D 1 95  ? 44.575  26.668  30.406  1.00 60.88  ? 91  TYR C CE2 1 
ATOM   7164  C CZ  . TYR D 1 95  ? 45.826  27.069  29.973  1.00 59.74  ? 91  TYR C CZ  1 
ATOM   7165  O OH  . TYR D 1 95  ? 46.945  26.388  30.397  1.00 51.69  ? 91  TYR C OH  1 
ATOM   7166  N N   . PRO D 1 96  ? 41.200  26.079  27.539  1.00 44.38  ? 92  PRO C N   1 
ATOM   7167  C CA  . PRO D 1 96  ? 40.370  24.900  27.795  1.00 45.61  ? 92  PRO C CA  1 
ATOM   7168  C C   . PRO D 1 96  ? 40.206  24.580  29.287  1.00 43.48  ? 92  PRO C C   1 
ATOM   7169  O O   . PRO D 1 96  ? 41.061  24.948  30.096  1.00 37.81  ? 92  PRO C O   1 
ATOM   7170  C CB  . PRO D 1 96  ? 41.132  23.777  27.080  1.00 44.36  ? 92  PRO C CB  1 
ATOM   7171  C CG  . PRO D 1 96  ? 42.552  24.224  27.091  1.00 45.81  ? 92  PRO C CG  1 
ATOM   7172  C CD  . PRO D 1 96  ? 42.500  25.716  26.942  1.00 46.02  ? 92  PRO C CD  1 
ATOM   7173  N N   . GLY D 1 97  ? 39.114  23.897  29.629  1.00 42.42  ? 93  GLY C N   1 
ATOM   7174  C CA  . GLY D 1 97  ? 38.837  23.507  31.014  1.00 46.12  ? 93  GLY C CA  1 
ATOM   7175  C C   . GLY D 1 97  ? 37.367  23.252  31.299  1.00 46.10  ? 93  GLY C C   1 
ATOM   7176  O O   . GLY D 1 97  ? 36.593  22.953  30.392  1.00 42.48  ? 93  GLY C O   1 
ATOM   7177  N N   . ASN D 1 98  ? 36.991  23.368  32.572  1.00 50.88  ? 94  ASN C N   1 
ATOM   7178  C CA  . ASN D 1 98  ? 35.624  23.116  33.021  1.00 48.85  ? 94  ASN C CA  1 
ATOM   7179  C C   . ASN D 1 98  ? 35.007  24.338  33.679  1.00 42.59  ? 94  ASN C C   1 
ATOM   7180  O O   . ASN D 1 98  ? 35.710  25.232  34.141  1.00 37.72  ? 94  ASN C O   1 
ATOM   7181  C CB  . ASN D 1 98  ? 35.585  21.954  34.021  1.00 52.46  ? 94  ASN C CB  1 
ATOM   7182  C CG  . ASN D 1 98  ? 35.658  20.594  33.356  1.00 61.56  ? 94  ASN C CG  1 
ATOM   7183  O OD1 . ASN D 1 98  ? 35.854  20.479  32.145  1.00 68.55  ? 94  ASN C OD1 1 
ATOM   7184  N ND2 . ASN D 1 98  ? 35.485  19.546  34.153  1.00 71.09  ? 94  ASN C ND2 1 
ATOM   7185  N N   . PHE D 1 99  ? 33.678  24.357  33.703  1.00 38.09  ? 95  PHE C N   1 
ATOM   7186  C CA  . PHE D 1 99  ? 32.916  25.344  34.443  1.00 34.67  ? 95  PHE C CA  1 
ATOM   7187  C C   . PHE D 1 99  ? 31.981  24.554  35.357  1.00 33.22  ? 95  PHE C C   1 
ATOM   7188  O O   . PHE D 1 99  ? 31.102  23.838  34.885  1.00 30.32  ? 95  PHE C O   1 
ATOM   7189  C CB  . PHE D 1 99  ? 32.134  26.237  33.480  1.00 33.90  ? 95  PHE C CB  1 
ATOM   7190  C CG  . PHE D 1 99  ? 31.762  27.576  34.053  1.00 34.82  ? 95  PHE C CG  1 
ATOM   7191  C CD1 . PHE D 1 99  ? 32.269  28.738  33.505  1.00 37.18  ? 95  PHE C CD1 1 
ATOM   7192  C CD2 . PHE D 1 99  ? 30.901  27.678  35.134  1.00 40.53  ? 95  PHE C CD2 1 
ATOM   7193  C CE1 . PHE D 1 99  ? 31.930  29.977  34.021  1.00 37.36  ? 95  PHE C CE1 1 
ATOM   7194  C CE2 . PHE D 1 99  ? 30.558  28.916  35.659  1.00 42.51  ? 95  PHE C CE2 1 
ATOM   7195  C CZ  . PHE D 1 99  ? 31.076  30.068  35.101  1.00 40.33  ? 95  PHE C CZ  1 
ATOM   7196  N N   . ASN D 1 100 ? 32.180  24.678  36.665  1.00 36.94  ? 96  ASN C N   1 
ATOM   7197  C CA  . ASN D 1 100 ? 31.419  23.893  37.627  1.00 36.12  ? 96  ASN C CA  1 
ATOM   7198  C C   . ASN D 1 100 ? 29.973  24.360  37.734  1.00 35.37  ? 96  ASN C C   1 
ATOM   7199  O O   . ASN D 1 100 ? 29.711  25.558  37.811  1.00 34.08  ? 96  ASN C O   1 
ATOM   7200  C CB  . ASN D 1 100 ? 32.070  23.946  39.005  1.00 37.02  ? 96  ASN C CB  1 
ATOM   7201  C CG  . ASN D 1 100 ? 31.496  22.904  39.944  1.00 40.74  ? 96  ASN C CG  1 
ATOM   7202  O OD1 . ASN D 1 100 ? 31.678  21.712  39.725  1.00 45.76  ? 96  ASN C OD1 1 
ATOM   7203  N ND2 . ASN D 1 100 ? 30.771  23.347  40.972  1.00 37.02  ? 96  ASN C ND2 1 
ATOM   7204  N N   . ASP D 1 101 ? 29.050  23.398  37.763  1.00 37.17  ? 97  ASP C N   1 
ATOM   7205  C CA  . ASP D 1 101 ? 27.613  23.670  37.845  1.00 39.27  ? 97  ASP C CA  1 
ATOM   7206  C C   . ASP D 1 101 ? 27.195  24.700  36.798  1.00 39.71  ? 97  ASP C C   1 
ATOM   7207  O O   . ASP D 1 101 ? 26.440  25.628  37.086  1.00 36.07  ? 97  ASP C O   1 
ATOM   7208  C CB  . ASP D 1 101 ? 27.217  24.141  39.257  1.00 47.03  ? 97  ASP C CB  1 
ATOM   7209  C CG  . ASP D 1 101 ? 27.317  23.040  40.305  1.00 51.76  ? 97  ASP C CG  1 
ATOM   7210  O OD1 . ASP D 1 101 ? 27.176  21.846  39.959  1.00 55.10  ? 97  ASP C OD1 1 
ATOM   7211  O OD2 . ASP D 1 101 ? 27.520  23.380  41.489  1.00 54.65  ? 97  ASP C OD2 1 
ATOM   7212  N N   . TYR D 1 102 ? 27.687  24.511  35.576  1.00 40.05  ? 98  TYR C N   1 
ATOM   7213  C CA  . TYR D 1 102 ? 27.459  25.448  34.484  1.00 36.49  ? 98  TYR C CA  1 
ATOM   7214  C C   . TYR D 1 102 ? 25.991  25.562  34.135  1.00 36.09  ? 98  TYR C C   1 
ATOM   7215  O O   . TYR D 1 102 ? 25.471  26.668  33.974  1.00 37.89  ? 98  TYR C O   1 
ATOM   7216  C CB  . TYR D 1 102 ? 28.243  25.005  33.247  1.00 39.11  ? 98  TYR C CB  1 
ATOM   7217  C CG  . TYR D 1 102 ? 28.163  25.938  32.051  1.00 38.62  ? 98  TYR C CG  1 
ATOM   7218  C CD1 . TYR D 1 102 ? 28.112  27.322  32.211  1.00 37.01  ? 98  TYR C CD1 1 
ATOM   7219  C CD2 . TYR D 1 102 ? 28.182  25.431  30.755  1.00 38.98  ? 98  TYR C CD2 1 
ATOM   7220  C CE1 . TYR D 1 102 ? 28.054  28.166  31.115  1.00 37.10  ? 98  TYR C CE1 1 
ATOM   7221  C CE2 . TYR D 1 102 ? 28.136  26.268  29.655  1.00 43.43  ? 98  TYR C CE2 1 
ATOM   7222  C CZ  . TYR D 1 102 ? 28.073  27.636  29.837  1.00 41.30  ? 98  TYR C CZ  1 
ATOM   7223  O OH  . TYR D 1 102 ? 28.023  28.470  28.738  1.00 41.26  ? 98  TYR C OH  1 
ATOM   7224  N N   . GLU D 1 103 ? 25.326  24.415  34.035  1.00 38.99  ? 99  GLU C N   1 
ATOM   7225  C CA  . GLU D 1 103 ? 23.929  24.360  33.597  1.00 40.74  ? 99  GLU C CA  1 
ATOM   7226  C C   . GLU D 1 103 ? 22.992  25.041  34.591  1.00 40.79  ? 99  GLU C C   1 
ATOM   7227  O O   . GLU D 1 103 ? 22.047  25.722  34.188  1.00 43.37  ? 99  GLU C O   1 
ATOM   7228  C CB  . GLU D 1 103 ? 23.485  22.914  33.357  1.00 45.64  ? 99  GLU C CB  1 
ATOM   7229  C CG  . GLU D 1 103 ? 24.160  22.230  32.170  1.00 48.19  ? 99  GLU C CG  1 
ATOM   7230  C CD  . GLU D 1 103 ? 25.576  21.744  32.457  1.00 57.77  ? 99  GLU C CD  1 
ATOM   7231  O OE1 . GLU D 1 103 ? 25.995  21.719  33.640  1.00 49.17  ? 99  GLU C OE1 1 
ATOM   7232  O OE2 . GLU D 1 103 ? 26.278  21.385  31.486  1.00 69.43  ? 99  GLU C OE2 1 
ATOM   7233  N N   . GLU D 1 104 ? 23.254  24.861  35.884  1.00 37.81  ? 100 GLU C N   1 
ATOM   7234  C CA  . GLU D 1 104 ? 22.477  25.545  36.916  1.00 35.62  ? 100 GLU C CA  1 
ATOM   7235  C C   . GLU D 1 104 ? 22.692  27.055  36.872  1.00 35.66  ? 100 GLU C C   1 
ATOM   7236  O O   . GLU D 1 104 ? 21.759  27.821  37.123  1.00 39.08  ? 100 GLU C O   1 
ATOM   7237  C CB  . GLU D 1 104 ? 22.799  24.991  38.312  1.00 36.35  ? 100 GLU C CB  1 
ATOM   7238  C CG  . GLU D 1 104 ? 22.111  23.664  38.612  1.00 37.61  ? 100 GLU C CG  1 
ATOM   7239  C CD  . GLU D 1 104 ? 20.592  23.784  38.730  1.00 39.13  ? 100 GLU C CD  1 
ATOM   7240  O OE1 . GLU D 1 104 ? 20.115  24.664  39.490  1.00 37.81  ? 100 GLU C OE1 1 
ATOM   7241  O OE2 . GLU D 1 104 ? 19.872  22.991  38.068  1.00 34.71  ? 100 GLU C OE2 1 
ATOM   7242  N N   . LEU D 1 105 ? 23.910  27.484  36.544  1.00 36.03  ? 101 LEU C N   1 
ATOM   7243  C CA  . LEU D 1 105 ? 24.196  28.912  36.410  1.00 36.25  ? 101 LEU C CA  1 
ATOM   7244  C C   . LEU D 1 105 ? 23.486  29.514  35.198  1.00 38.16  ? 101 LEU C C   1 
ATOM   7245  O O   . LEU D 1 105 ? 22.944  30.616  35.284  1.00 38.78  ? 101 LEU C O   1 
ATOM   7246  C CB  . LEU D 1 105 ? 25.699  29.180  36.316  1.00 35.53  ? 101 LEU C CB  1 
ATOM   7247  C CG  . LEU D 1 105 ? 26.070  30.669  36.288  1.00 33.35  ? 101 LEU C CG  1 
ATOM   7248  C CD1 . LEU D 1 105 ? 25.433  31.419  37.448  1.00 33.14  ? 101 LEU C CD1 1 
ATOM   7249  C CD2 . LEU D 1 105 ? 27.577  30.844  36.326  1.00 36.36  ? 101 LEU C CD2 1 
ATOM   7250  N N   . LYS D 1 106 ? 23.503  28.802  34.073  1.00 39.34  ? 102 LYS C N   1 
ATOM   7251  C CA  . LYS D 1 106 ? 22.771  29.240  32.887  1.00 39.41  ? 102 LYS C CA  1 
ATOM   7252  C C   . LYS D 1 106 ? 21.296  29.385  33.224  1.00 35.73  ? 102 LYS C C   1 
ATOM   7253  O O   . LYS D 1 106 ? 20.672  30.380  32.875  1.00 37.93  ? 102 LYS C O   1 
ATOM   7254  C CB  . LYS D 1 106 ? 22.933  28.252  31.727  1.00 42.25  ? 102 LYS C CB  1 
ATOM   7255  C CG  . LYS D 1 106 ? 24.314  28.240  31.093  1.00 42.21  ? 102 LYS C CG  1 
ATOM   7256  C CD  . LYS D 1 106 ? 24.498  27.051  30.158  1.00 43.81  ? 102 LYS C CD  1 
ATOM   7257  C CE  . LYS D 1 106 ? 24.102  27.374  28.727  1.00 49.72  ? 102 LYS C CE  1 
ATOM   7258  N NZ  . LYS D 1 106 ? 24.461  26.264  27.797  1.00 58.41  ? 102 LYS C NZ  1 
ATOM   7259  N N   . HIS D 1 107 ? 20.742  28.396  33.914  1.00 36.41  ? 103 HIS C N   1 
ATOM   7260  C CA  . HIS D 1 107 ? 19.328  28.432  34.273  1.00 34.68  ? 103 HIS C CA  1 
ATOM   7261  C C   . HIS D 1 107 ? 19.031  29.619  35.135  1.00 37.36  ? 103 HIS C C   1 
ATOM   7262  O O   . HIS D 1 107 ? 18.073  30.349  34.882  1.00 41.28  ? 103 HIS C O   1 
ATOM   7263  C CB  . HIS D 1 107 ? 18.903  27.154  34.980  1.00 33.93  ? 103 HIS C CB  1 
ATOM   7264  C CG  . HIS D 1 107 ? 17.418  27.076  35.234  1.00 37.05  ? 103 HIS C CG  1 
ATOM   7265  N ND1 . HIS D 1 107 ? 16.520  26.880  34.244  1.00 35.45  ? 103 HIS C ND1 1 
ATOM   7266  C CD2 . HIS D 1 107 ? 16.687  27.203  36.410  1.00 35.31  ? 103 HIS C CD2 1 
ATOM   7267  C CE1 . HIS D 1 107 ? 15.280  26.880  34.763  1.00 36.65  ? 103 HIS C CE1 1 
ATOM   7268  N NE2 . HIS D 1 107 ? 15.383  27.071  36.089  1.00 38.66  ? 103 HIS C NE2 1 
ATOM   7269  N N   . LEU D 1 108 ? 19.866  29.842  36.144  1.00 38.72  ? 104 LEU C N   1 
ATOM   7270  C CA  . LEU D 1 108 ? 19.686  30.977  37.043  1.00 42.44  ? 104 LEU C CA  1 
ATOM   7271  C C   . LEU D 1 108 ? 19.746  32.310  36.295  1.00 44.24  ? 104 LEU C C   1 
ATOM   7272  O O   . LEU D 1 108 ? 18.982  33.221  36.598  1.00 47.68  ? 104 LEU C O   1 
ATOM   7273  C CB  . LEU D 1 108 ? 20.744  30.957  38.151  1.00 46.71  ? 104 LEU C CB  1 
ATOM   7274  C CG  . LEU D 1 108 ? 20.591  32.034  39.239  1.00 51.14  ? 104 LEU C CG  1 
ATOM   7275  C CD1 . LEU D 1 108 ? 20.298  31.412  40.597  1.00 53.54  ? 104 LEU C CD1 1 
ATOM   7276  C CD2 . LEU D 1 108 ? 21.813  32.937  39.296  1.00 54.20  ? 104 LEU C CD2 1 
ATOM   7277  N N   . LEU D 1 109 ? 20.651  32.410  35.322  1.00 44.12  ? 105 LEU C N   1 
ATOM   7278  C CA  . LEU D 1 109 ? 20.849  33.642  34.552  1.00 45.52  ? 105 LEU C CA  1 
ATOM   7279  C C   . LEU D 1 109 ? 19.904  33.778  33.358  1.00 47.40  ? 105 LEU C C   1 
ATOM   7280  O O   . LEU D 1 109 ? 19.996  34.752  32.614  1.00 49.24  ? 105 LEU C O   1 
ATOM   7281  C CB  . LEU D 1 109 ? 22.299  33.727  34.044  1.00 43.07  ? 105 LEU C CB  1 
ATOM   7282  C CG  . LEU D 1 109 ? 23.401  33.951  35.081  1.00 39.21  ? 105 LEU C CG  1 
ATOM   7283  C CD1 . LEU D 1 109 ? 24.767  33.726  34.455  1.00 33.00  ? 105 LEU C CD1 1 
ATOM   7284  C CD2 . LEU D 1 109 ? 23.300  35.351  35.665  1.00 35.67  ? 105 LEU C CD2 1 
ATOM   7285  N N   . SER D 1 110 ? 19.010  32.811  33.159  1.00 47.76  ? 106 SER C N   1 
ATOM   7286  C CA  . SER D 1 110 ? 18.111  32.828  32.000  1.00 45.28  ? 106 SER C CA  1 
ATOM   7287  C C   . SER D 1 110 ? 17.189  34.051  31.986  1.00 43.63  ? 106 SER C C   1 
ATOM   7288  O O   . SER D 1 110 ? 16.832  34.537  30.920  1.00 44.49  ? 106 SER C O   1 
ATOM   7289  C CB  . SER D 1 110 ? 17.270  31.551  31.949  1.00 48.72  ? 106 SER C CB  1 
ATOM   7290  O OG  . SER D 1 110 ? 16.378  31.484  33.049  1.00 52.38  ? 106 SER C OG  1 
ATOM   7291  N N   . ARG D 1 111 ? 16.805  34.534  33.165  1.00 39.79  ? 107 ARG C N   1 
ATOM   7292  C CA  . ARG D 1 111 ? 15.982  35.732  33.288  1.00 42.63  ? 107 ARG C CA  1 
ATOM   7293  C C   . ARG D 1 111 ? 16.386  36.515  34.521  1.00 46.99  ? 107 ARG C C   1 
ATOM   7294  O O   . ARG D 1 111 ? 16.300  36.000  35.637  1.00 55.61  ? 107 ARG C O   1 
ATOM   7295  C CB  . ARG D 1 111 ? 14.505  35.360  33.377  1.00 47.06  ? 107 ARG C CB  1 
ATOM   7296  C CG  . ARG D 1 111 ? 13.556  36.543  33.477  1.00 48.85  ? 107 ARG C CG  1 
ATOM   7297  C CD  . ARG D 1 111 ? 12.156  36.179  32.958  1.00 55.76  ? 107 ARG C CD  1 
ATOM   7298  N NE  . ARG D 1 111 ? 11.177  35.921  34.008  1.00 60.18  ? 107 ARG C NE  1 
ATOM   7299  C CZ  . ARG D 1 111 ? 9.929   35.510  33.783  1.00 64.79  ? 107 ARG C CZ  1 
ATOM   7300  N NH1 . ARG D 1 111 ? 9.483   35.319  32.543  1.00 70.92  ? 107 ARG C NH1 1 
ATOM   7301  N NH2 . ARG D 1 111 ? 9.111   35.291  34.806  1.00 73.85  ? 107 ARG C NH2 1 
ATOM   7302  N N   . ILE D 1 112 ? 16.823  37.756  34.309  1.00 44.96  ? 108 ILE C N   1 
ATOM   7303  C CA  . ILE D 1 112 ? 17.347  38.597  35.377  1.00 47.05  ? 108 ILE C CA  1 
ATOM   7304  C C   . ILE D 1 112 ? 16.690  39.976  35.354  1.00 48.81  ? 108 ILE C C   1 
ATOM   7305  O O   . ILE D 1 112 ? 16.495  40.565  34.291  1.00 52.49  ? 108 ILE C O   1 
ATOM   7306  C CB  . ILE D 1 112 ? 18.884  38.737  35.259  1.00 51.41  ? 108 ILE C CB  1 
ATOM   7307  C CG1 . ILE D 1 112 ? 19.564  37.385  35.490  1.00 51.22  ? 108 ILE C CG1 1 
ATOM   7308  C CG2 . ILE D 1 112 ? 19.428  39.744  36.264  1.00 47.69  ? 108 ILE C CG2 1 
ATOM   7309  C CD1 . ILE D 1 112 ? 19.355  36.820  36.880  1.00 50.53  ? 108 ILE C CD1 1 
ATOM   7310  N N   . ASN D 1 113 ? 16.359  40.476  36.543  1.00 51.67  ? 109 ASN C N   1 
ATOM   7311  C CA  . ASN D 1 113 ? 15.716  41.775  36.710  1.00 48.56  ? 109 ASN C CA  1 
ATOM   7312  C C   . ASN D 1 113 ? 16.736  42.907  36.726  1.00 52.06  ? 109 ASN C C   1 
ATOM   7313  O O   . ASN D 1 113 ? 16.490  43.964  36.158  1.00 52.51  ? 109 ASN C O   1 
ATOM   7314  C CB  . ASN D 1 113 ? 14.901  41.785  38.003  1.00 51.61  ? 109 ASN C CB  1 
ATOM   7315  C CG  . ASN D 1 113 ? 14.153  43.088  38.222  1.00 58.32  ? 109 ASN C CG  1 
ATOM   7316  O OD1 . ASN D 1 113 ? 12.976  43.204  37.892  1.00 69.40  ? 109 ASN C OD1 1 
ATOM   7317  N ND2 . ASN D 1 113 ? 14.840  44.078  38.795  1.00 53.65  ? 109 ASN C ND2 1 
ATOM   7318  N N   . HIS D 1 114 ? 17.865  42.692  37.401  1.00 55.52  ? 110 HIS C N   1 
ATOM   7319  C CA  . HIS D 1 114 ? 18.961  43.664  37.417  1.00 53.72  ? 110 HIS C CA  1 
ATOM   7320  C C   . HIS D 1 114 ? 20.292  42.969  37.345  1.00 55.57  ? 110 HIS C C   1 
ATOM   7321  O O   . HIS D 1 114 ? 20.532  41.994  38.057  1.00 58.20  ? 110 HIS C O   1 
ATOM   7322  C CB  . HIS D 1 114 ? 18.888  44.537  38.666  1.00 58.41  ? 110 HIS C CB  1 
ATOM   7323  C CG  . HIS D 1 114 ? 19.904  45.655  38.691  1.00 66.88  ? 110 HIS C CG  1 
ATOM   7324  N ND1 . HIS D 1 114 ? 20.852  45.759  39.646  1.00 75.02  ? 110 HIS C ND1 1 
ATOM   7325  C CD2 . HIS D 1 114 ? 20.100  46.729  37.824  1.00 68.91  ? 110 HIS C CD2 1 
ATOM   7326  C CE1 . HIS D 1 114 ? 21.610  46.848  39.403  1.00 72.20  ? 110 HIS C CE1 1 
ATOM   7327  N NE2 . HIS D 1 114 ? 21.151  47.435  38.289  1.00 72.76  ? 110 HIS C NE2 1 
ATOM   7328  N N   . PHE D 1 115 ? 21.175  43.481  36.490  1.00 57.61  ? 111 PHE C N   1 
ATOM   7329  C CA  . PHE D 1 115 ? 22.489  42.884  36.269  1.00 57.88  ? 111 PHE C CA  1 
ATOM   7330  C C   . PHE D 1 115 ? 23.554  43.960  36.039  1.00 57.96  ? 111 PHE C C   1 
ATOM   7331  O O   . PHE D 1 115 ? 23.548  44.634  35.011  1.00 58.51  ? 111 PHE C O   1 
ATOM   7332  C CB  . PHE D 1 115 ? 22.424  41.946  35.067  1.00 57.89  ? 111 PHE C CB  1 
ATOM   7333  C CG  . PHE D 1 115 ? 23.592  41.015  34.960  1.00 59.23  ? 111 PHE C CG  1 
ATOM   7334  C CD1 . PHE D 1 115 ? 23.696  39.917  35.802  1.00 59.86  ? 111 PHE C CD1 1 
ATOM   7335  C CD2 . PHE D 1 115 ? 24.579  41.223  34.009  1.00 60.88  ? 111 PHE C CD2 1 
ATOM   7336  C CE1 . PHE D 1 115 ? 24.766  39.047  35.703  1.00 61.11  ? 111 PHE C CE1 1 
ATOM   7337  C CE2 . PHE D 1 115 ? 25.652  40.356  33.904  1.00 60.62  ? 111 PHE C CE2 1 
ATOM   7338  C CZ  . PHE D 1 115 ? 25.745  39.265  34.751  1.00 60.21  ? 111 PHE C CZ  1 
ATOM   7339  N N   . GLU D 1 116 ? 24.463  44.118  36.999  1.00 54.81  ? 112 GLU C N   1 
ATOM   7340  C CA  . GLU D 1 116 ? 25.505  45.136  36.914  1.00 58.10  ? 112 GLU C CA  1 
ATOM   7341  C C   . GLU D 1 116 ? 26.878  44.562  37.272  1.00 57.05  ? 112 GLU C C   1 
ATOM   7342  O O   . GLU D 1 116 ? 27.076  44.051  38.377  1.00 50.00  ? 112 GLU C O   1 
ATOM   7343  C CB  . GLU D 1 116 ? 25.171  46.314  37.838  1.00 66.25  ? 112 GLU C CB  1 
ATOM   7344  C CG  . GLU D 1 116 ? 26.061  47.538  37.653  1.00 76.55  ? 112 GLU C CG  1 
ATOM   7345  C CD  . GLU D 1 116 ? 25.816  48.612  38.701  1.00 84.35  ? 112 GLU C CD  1 
ATOM   7346  O OE1 . GLU D 1 116 ? 24.679  48.707  39.216  1.00 95.15  ? 112 GLU C OE1 1 
ATOM   7347  O OE2 . GLU D 1 116 ? 26.766  49.364  39.010  1.00 75.88  ? 112 GLU C OE2 1 
ATOM   7348  N N   . LYS D 1 117 ? 27.817  44.658  36.330  1.00 55.28  ? 113 LYS C N   1 
ATOM   7349  C CA  . LYS D 1 117 ? 29.208  44.285  36.573  1.00 54.44  ? 113 LYS C CA  1 
ATOM   7350  C C   . LYS D 1 117 ? 29.845  45.282  37.538  1.00 54.39  ? 113 LYS C C   1 
ATOM   7351  O O   . LYS D 1 117 ? 29.667  46.490  37.399  1.00 59.27  ? 113 LYS C O   1 
ATOM   7352  C CB  . LYS D 1 117 ? 30.001  44.252  35.263  1.00 53.96  ? 113 LYS C CB  1 
ATOM   7353  C CG  . LYS D 1 117 ? 31.405  43.680  35.405  1.00 59.11  ? 113 LYS C CG  1 
ATOM   7354  C CD  . LYS D 1 117 ? 32.312  44.040  34.230  1.00 65.74  ? 113 LYS C CD  1 
ATOM   7355  C CE  . LYS D 1 117 ? 32.054  43.158  33.009  1.00 67.00  ? 113 LYS C CE  1 
ATOM   7356  N NZ  . LYS D 1 117 ? 33.116  43.224  31.965  1.00 64.76  ? 113 LYS C NZ  1 
ATOM   7357  N N   . ILE D 1 118 ? 30.579  44.762  38.516  1.00 54.64  ? 114 ILE C N   1 
ATOM   7358  C CA  . ILE D 1 118 ? 31.204  45.573  39.554  1.00 57.19  ? 114 ILE C CA  1 
ATOM   7359  C C   . ILE D 1 118 ? 32.642  45.097  39.756  1.00 57.58  ? 114 ILE C C   1 
ATOM   7360  O O   . ILE D 1 118 ? 32.904  43.897  39.778  1.00 57.06  ? 114 ILE C O   1 
ATOM   7361  C CB  . ILE D 1 118 ? 30.407  45.474  40.877  1.00 59.75  ? 114 ILE C CB  1 
ATOM   7362  C CG1 . ILE D 1 118 ? 31.150  46.153  42.031  1.00 62.34  ? 114 ILE C CG1 1 
ATOM   7363  C CG2 . ILE D 1 118 ? 30.140  44.025  41.238  1.00 56.94  ? 114 ILE C CG2 1 
ATOM   7364  C CD1 . ILE D 1 118 ? 30.475  45.967  43.373  1.00 66.58  ? 114 ILE C CD1 1 
ATOM   7365  N N   . GLN D 1 119 ? 33.570  46.040  39.892  1.00 61.56  ? 115 GLN C N   1 
ATOM   7366  C CA  . GLN D 1 119 ? 34.951  45.707  40.220  1.00 63.51  ? 115 GLN C CA  1 
ATOM   7367  C C   . GLN D 1 119 ? 35.019  45.340  41.701  1.00 63.15  ? 115 GLN C C   1 
ATOM   7368  O O   . GLN D 1 119 ? 34.751  46.172  42.567  1.00 54.59  ? 115 GLN C O   1 
ATOM   7369  C CB  . GLN D 1 119 ? 35.885  46.875  39.909  1.00 67.85  ? 115 GLN C CB  1 
ATOM   7370  C CG  . GLN D 1 119 ? 37.359  46.507  39.926  1.00 72.85  ? 115 GLN C CG  1 
ATOM   7371  C CD  . GLN D 1 119 ? 38.254  47.725  39.794  1.00 75.52  ? 115 GLN C CD  1 
ATOM   7372  O OE1 . GLN D 1 119 ? 38.233  48.617  40.645  1.00 77.39  ? 115 GLN C OE1 1 
ATOM   7373  N NE2 . GLN D 1 119 ? 39.044  47.773  38.723  1.00 59.86  ? 115 GLN C NE2 1 
ATOM   7374  N N   . ILE D 1 120 ? 35.375  44.087  41.978  1.00 65.34  ? 116 ILE C N   1 
ATOM   7375  C CA  . ILE D 1 120 ? 35.320  43.536  43.328  1.00 64.96  ? 116 ILE C CA  1 
ATOM   7376  C C   . ILE D 1 120 ? 36.687  43.682  44.000  1.00 69.35  ? 116 ILE C C   1 
ATOM   7377  O O   . ILE D 1 120 ? 36.772  44.108  45.154  1.00 70.24  ? 116 ILE C O   1 
ATOM   7378  C CB  . ILE D 1 120 ? 34.827  42.063  43.300  1.00 69.82  ? 116 ILE C CB  1 
ATOM   7379  C CG1 . ILE D 1 120 ? 33.619  41.885  44.210  1.00 77.35  ? 116 ILE C CG1 1 
ATOM   7380  C CG2 . ILE D 1 120 ? 35.922  41.086  43.696  1.00 81.92  ? 116 ILE C CG2 1 
ATOM   7381  C CD1 . ILE D 1 120 ? 32.432  42.744  43.836  1.00 87.73  ? 116 ILE C CD1 1 
ATOM   7382  N N   . ILE D 1 121 ? 37.751  43.335  43.277  1.00 64.33  ? 117 ILE C N   1 
ATOM   7383  C CA  . ILE D 1 121 ? 39.119  43.562  43.739  1.00 66.35  ? 117 ILE C CA  1 
ATOM   7384  C C   . ILE D 1 121 ? 39.967  44.042  42.560  1.00 63.69  ? 117 ILE C C   1 
ATOM   7385  O O   . ILE D 1 121 ? 40.054  43.351  41.545  1.00 69.40  ? 117 ILE C O   1 
ATOM   7386  C CB  . ILE D 1 121 ? 39.738  42.301  44.380  1.00 74.82  ? 117 ILE C CB  1 
ATOM   7387  C CG1 . ILE D 1 121 ? 39.911  41.176  43.373  1.00 77.91  ? 117 ILE C CG1 1 
ATOM   7388  C CG2 . ILE D 1 121 ? 38.898  41.827  45.559  1.00 76.24  ? 117 ILE C CG2 1 
ATOM   7389  C CD1 . ILE D 1 121 ? 41.278  41.134  42.719  1.00 73.68  ? 117 ILE C CD1 1 
ATOM   7390  N N   . PRO D 1 122 ? 40.577  45.236  42.676  1.00 59.63  ? 118 PRO C N   1 
ATOM   7391  C CA  . PRO D 1 122 ? 41.249  45.815  41.506  1.00 59.20  ? 118 PRO C CA  1 
ATOM   7392  C C   . PRO D 1 122 ? 42.558  45.116  41.134  1.00 56.89  ? 118 PRO C C   1 
ATOM   7393  O O   . PRO D 1 122 ? 43.294  44.664  42.012  1.00 59.80  ? 118 PRO C O   1 
ATOM   7394  C CB  . PRO D 1 122 ? 41.497  47.269  41.917  1.00 60.01  ? 118 PRO C CB  1 
ATOM   7395  C CG  . PRO D 1 122 ? 41.463  47.278  43.403  1.00 62.05  ? 118 PRO C CG  1 
ATOM   7396  C CD  . PRO D 1 122 ? 40.612  46.128  43.849  1.00 60.16  ? 118 PRO C CD  1 
ATOM   7397  N N   . LYS D 1 123 ? 42.831  45.040  39.832  1.00 54.53  ? 119 LYS C N   1 
ATOM   7398  C CA  . LYS D 1 123 ? 44.013  44.353  39.316  1.00 61.06  ? 119 LYS C CA  1 
ATOM   7399  C C   . LYS D 1 123 ? 45.318  44.956  39.853  1.00 67.36  ? 119 LYS C C   1 
ATOM   7400  O O   . LYS D 1 123 ? 46.309  44.246  40.032  1.00 71.81  ? 119 LYS C O   1 
ATOM   7401  C CB  . LYS D 1 123 ? 44.015  44.376  37.779  1.00 62.86  ? 119 LYS C CB  1 
ATOM   7402  C CG  . LYS D 1 123 ? 44.976  43.380  37.138  1.00 63.18  ? 119 LYS C CG  1 
ATOM   7403  C CD  . LYS D 1 123 ? 45.198  43.653  35.657  1.00 61.39  ? 119 LYS C CD  1 
ATOM   7404  C CE  . LYS D 1 123 ? 44.334  42.769  34.773  1.00 65.81  ? 119 LYS C CE  1 
ATOM   7405  N NZ  . LYS D 1 123 ? 44.676  42.938  33.332  1.00 65.85  ? 119 LYS C NZ  1 
ATOM   7406  N N   . ASN D 1 124 ? 45.312  46.262  40.108  1.00 75.52  ? 120 ASN C N   1 
ATOM   7407  C CA  . ASN D 1 124 ? 46.490  46.960  40.641  1.00 76.98  ? 120 ASN C CA  1 
ATOM   7408  C C   . ASN D 1 124 ? 46.788  46.678  42.121  1.00 68.88  ? 120 ASN C C   1 
ATOM   7409  O O   . ASN D 1 124 ? 47.868  47.020  42.606  1.00 65.90  ? 120 ASN C O   1 
ATOM   7410  C CB  . ASN D 1 124 ? 46.368  48.477  40.413  1.00 85.05  ? 120 ASN C CB  1 
ATOM   7411  C CG  . ASN D 1 124 ? 45.096  49.067  41.010  1.00 99.30  ? 120 ASN C CG  1 
ATOM   7412  O OD1 . ASN D 1 124 ? 44.761  48.825  42.173  1.00 111.93 ? 120 ASN C OD1 1 
ATOM   7413  N ND2 . ASN D 1 124 ? 44.381  49.851  40.210  1.00 103.82 ? 120 ASN C ND2 1 
ATOM   7414  N N   . SER D 1 125 ? 45.846  46.054  42.831  1.00 64.21  ? 121 SER C N   1 
ATOM   7415  C CA  . SER D 1 125 ? 45.995  45.834  44.277  1.00 60.86  ? 121 SER C CA  1 
ATOM   7416  C C   . SER D 1 125 ? 46.873  44.632  44.638  1.00 55.52  ? 121 SER C C   1 
ATOM   7417  O O   . SER D 1 125 ? 47.109  44.385  45.818  1.00 54.70  ? 121 SER C O   1 
ATOM   7418  C CB  . SER D 1 125 ? 44.628  45.671  44.951  1.00 61.69  ? 121 SER C CB  1 
ATOM   7419  O OG  . SER D 1 125 ? 44.082  44.400  44.666  1.00 61.48  ? 121 SER C OG  1 
ATOM   7420  N N   . TRP D 1 126 ? 47.318  43.868  43.639  1.00 58.51  ? 122 TRP C N   1 
ATOM   7421  C CA  . TRP D 1 126 ? 48.238  42.745  43.870  1.00 59.51  ? 122 TRP C CA  1 
ATOM   7422  C C   . TRP D 1 126 ? 49.656  43.237  43.836  1.00 62.85  ? 122 TRP C C   1 
ATOM   7423  O O   . TRP D 1 126 ? 50.238  43.402  42.760  1.00 68.20  ? 122 TRP C O   1 
ATOM   7424  C CB  . TRP D 1 126 ? 48.038  41.653  42.822  1.00 56.37  ? 122 TRP C CB  1 
ATOM   7425  C CG  . TRP D 1 126 ? 46.635  41.091  42.783  1.00 52.53  ? 122 TRP C CG  1 
ATOM   7426  C CD1 . TRP D 1 126 ? 45.658  41.315  41.817  1.00 51.25  ? 122 TRP C CD1 1 
ATOM   7427  C CD2 . TRP D 1 126 ? 46.006  40.186  43.754  1.00 47.29  ? 122 TRP C CD2 1 
ATOM   7428  N NE1 . TRP D 1 126 ? 44.506  40.631  42.113  1.00 51.09  ? 122 TRP C NE1 1 
ATOM   7429  C CE2 . TRP D 1 126 ? 44.648  39.936  43.263  1.00 48.76  ? 122 TRP C CE2 1 
ATOM   7430  C CE3 . TRP D 1 126 ? 46.414  39.584  44.931  1.00 47.71  ? 122 TRP C CE3 1 
ATOM   7431  C CZ2 . TRP D 1 126 ? 43.760  39.117  43.945  1.00 48.57  ? 122 TRP C CZ2 1 
ATOM   7432  C CZ3 . TRP D 1 126 ? 45.507  38.758  45.608  1.00 50.25  ? 122 TRP C CZ3 1 
ATOM   7433  C CH2 . TRP D 1 126 ? 44.214  38.531  45.126  1.00 45.72  ? 122 TRP C CH2 1 
ATOM   7434  N N   . SER D 1 127 ? 50.226  43.482  45.015  1.00 64.65  ? 123 SER C N   1 
ATOM   7435  C CA  . SER D 1 127 ? 51.569  44.064  45.122  1.00 67.17  ? 123 SER C CA  1 
ATOM   7436  C C   . SER D 1 127 ? 52.675  43.008  45.196  1.00 67.21  ? 123 SER C C   1 
ATOM   7437  O O   . SER D 1 127 ? 53.761  43.215  44.656  1.00 61.40  ? 123 SER C O   1 
ATOM   7438  C CB  . SER D 1 127 ? 51.650  44.998  46.333  1.00 64.54  ? 123 SER C CB  1 
ATOM   7439  O OG  . SER D 1 127 ? 51.178  44.360  47.506  1.00 66.87  ? 123 SER C OG  1 
ATOM   7440  N N   . ASP D 1 128 ? 52.392  41.880  45.849  1.00 72.14  ? 124 ASP C N   1 
ATOM   7441  C CA  . ASP D 1 128 ? 53.378  40.797  46.002  1.00 63.09  ? 124 ASP C CA  1 
ATOM   7442  C C   . ASP D 1 128 ? 53.263  39.712  44.926  1.00 56.26  ? 124 ASP C C   1 
ATOM   7443  O O   . ASP D 1 128 ? 53.973  38.707  44.986  1.00 55.64  ? 124 ASP C O   1 
ATOM   7444  C CB  . ASP D 1 128 ? 53.253  40.171  47.389  1.00 59.60  ? 124 ASP C CB  1 
ATOM   7445  C CG  . ASP D 1 128 ? 53.585  41.146  48.491  1.00 67.90  ? 124 ASP C CG  1 
ATOM   7446  O OD1 . ASP D 1 128 ? 54.794  41.395  48.746  1.00 76.03  ? 124 ASP C OD1 1 
ATOM   7447  O OD2 . ASP D 1 128 ? 52.627  41.674  49.101  1.00 69.86  ? 124 ASP C OD2 1 
ATOM   7448  N N   . HIS D 1 129 ? 52.368  39.915  43.957  1.00 53.64  ? 125 HIS C N   1 
ATOM   7449  C CA  . HIS D 1 129 ? 52.185  38.982  42.841  1.00 51.61  ? 125 HIS C CA  1 
ATOM   7450  C C   . HIS D 1 129 ? 52.077  39.735  41.549  1.00 47.85  ? 125 HIS C C   1 
ATOM   7451  O O   . HIS D 1 129 ? 51.729  40.914  41.539  1.00 41.69  ? 125 HIS C O   1 
ATOM   7452  C CB  . HIS D 1 129 ? 50.934  38.140  43.051  1.00 50.64  ? 125 HIS C CB  1 
ATOM   7453  C CG  . HIS D 1 129 ? 50.927  37.377  44.358  1.00 48.15  ? 125 HIS C CG  1 
ATOM   7454  N ND1 . HIS D 1 129 ? 50.593  37.949  45.533  1.00 44.65  ? 125 HIS C ND1 1 
ATOM   7455  C CD2 . HIS D 1 129 ? 51.236  36.049  44.641  1.00 45.74  ? 125 HIS C CD2 1 
ATOM   7456  C CE1 . HIS D 1 129 ? 50.683  37.034  46.517  1.00 44.82  ? 125 HIS C CE1 1 
ATOM   7457  N NE2 . HIS D 1 129 ? 51.075  35.871  45.969  1.00 46.51  ? 125 HIS C NE2 1 
ATOM   7458  N N   . GLU D 1 130 ? 52.382  39.057  40.446  1.00 52.48  ? 126 GLU C N   1 
ATOM   7459  C CA  . GLU D 1 130 ? 52.269  39.646  39.114  1.00 55.21  ? 126 GLU C CA  1 
ATOM   7460  C C   . GLU D 1 130 ? 50.872  39.397  38.556  1.00 59.69  ? 126 GLU C C   1 
ATOM   7461  O O   . GLU D 1 130 ? 50.467  38.246  38.378  1.00 55.56  ? 126 GLU C O   1 
ATOM   7462  C CB  . GLU D 1 130 ? 53.328  39.064  38.170  1.00 58.25  ? 126 GLU C CB  1 
ATOM   7463  C CG  . GLU D 1 130 ? 54.731  39.592  38.442  1.00 64.29  ? 126 GLU C CG  1 
ATOM   7464  C CD  . GLU D 1 130 ? 55.011  40.937  37.780  1.00 67.75  ? 126 GLU C CD  1 
ATOM   7465  O OE1 . GLU D 1 130 ? 54.070  41.570  37.251  1.00 65.75  ? 126 GLU C OE1 1 
ATOM   7466  O OE2 . GLU D 1 130 ? 56.185  41.367  37.792  1.00 69.32  ? 126 GLU C OE2 1 
ATOM   7467  N N   . ALA D 1 131 ? 50.151  40.484  38.280  1.00 56.47  ? 127 ALA C N   1 
ATOM   7468  C CA  . ALA D 1 131 ? 48.783  40.418  37.769  1.00 58.50  ? 127 ALA C CA  1 
ATOM   7469  C C   . ALA D 1 131 ? 48.689  40.629  36.251  1.00 58.16  ? 127 ALA C C   1 
ATOM   7470  O O   . ALA D 1 131 ? 47.590  40.594  35.694  1.00 62.10  ? 127 ALA C O   1 
ATOM   7471  C CB  . ALA D 1 131 ? 47.918  41.447  38.488  1.00 52.88  ? 127 ALA C CB  1 
ATOM   7472  N N   . SER D 1 132 ? 49.826  40.832  35.587  1.00 56.74  ? 128 SER C N   1 
ATOM   7473  C CA  . SER D 1 132 ? 49.840  41.197  34.165  1.00 60.74  ? 128 SER C CA  1 
ATOM   7474  C C   . SER D 1 132 ? 50.585  40.215  33.257  1.00 57.68  ? 128 SER C C   1 
ATOM   7475  O O   . SER D 1 132 ? 50.691  40.457  32.057  1.00 58.75  ? 128 SER C O   1 
ATOM   7476  C CB  . SER D 1 132 ? 50.427  42.602  34.001  1.00 62.94  ? 128 SER C CB  1 
ATOM   7477  O OG  . SER D 1 132 ? 49.578  43.572  34.597  1.00 67.55  ? 128 SER C OG  1 
ATOM   7478  N N   . LEU D 1 133 ? 51.080  39.110  33.811  1.00 64.07  ? 129 LEU C N   1 
ATOM   7479  C CA  . LEU D 1 133 ? 51.750  38.081  33.003  1.00 66.68  ? 129 LEU C CA  1 
ATOM   7480  C C   . LEU D 1 133 ? 50.835  36.895  32.684  1.00 68.43  ? 129 LEU C C   1 
ATOM   7481  O O   . LEU D 1 133 ? 51.217  36.007  31.922  1.00 65.01  ? 129 LEU C O   1 
ATOM   7482  C CB  . LEU D 1 133 ? 53.025  37.592  33.701  1.00 73.04  ? 129 LEU C CB  1 
ATOM   7483  C CG  . LEU D 1 133 ? 54.307  38.374  33.404  1.00 75.75  ? 129 LEU C CG  1 
ATOM   7484  C CD1 . LEU D 1 133 ? 55.003  38.821  34.686  1.00 70.95  ? 129 LEU C CD1 1 
ATOM   7485  C CD2 . LEU D 1 133 ? 55.238  37.546  32.525  1.00 74.61  ? 129 LEU C CD2 1 
ATOM   7486  N N   . GLY D 1 134 ? 49.634  36.883  33.260  1.00 71.14  ? 130 GLY C N   1 
ATOM   7487  C CA  . GLY D 1 134 ? 48.673  35.802  33.031  1.00 67.54  ? 130 GLY C CA  1 
ATOM   7488  C C   . GLY D 1 134 ? 47.981  35.904  31.683  1.00 63.74  ? 130 GLY C C   1 
ATOM   7489  O O   . GLY D 1 134 ? 46.919  36.514  31.567  1.00 66.72  ? 130 GLY C O   1 
ATOM   7490  N N   . VAL D 1 135 ? 48.586  35.291  30.669  1.00 60.81  ? 131 VAL C N   1 
ATOM   7491  C CA  . VAL D 1 135 ? 48.167  35.454  29.271  1.00 57.19  ? 131 VAL C CA  1 
ATOM   7492  C C   . VAL D 1 135 ? 48.511  34.200  28.465  1.00 54.19  ? 131 VAL C C   1 
ATOM   7493  O O   . VAL D 1 135 ? 49.447  33.479  28.818  1.00 47.61  ? 131 VAL C O   1 
ATOM   7494  C CB  . VAL D 1 135 ? 48.846  36.698  28.661  1.00 60.13  ? 131 VAL C CB  1 
ATOM   7495  C CG1 . VAL D 1 135 ? 49.165  36.494  27.188  1.00 63.38  ? 131 VAL C CG1 1 
ATOM   7496  C CG2 . VAL D 1 135 ? 47.971  37.929  28.864  1.00 58.65  ? 131 VAL C CG2 1 
ATOM   7497  N N   . SER D 1 136 ? 47.756  33.941  27.394  1.00 57.75  ? 132 SER C N   1 
ATOM   7498  C CA  . SER D 1 136 ? 47.909  32.702  26.614  1.00 61.11  ? 132 SER C CA  1 
ATOM   7499  C C   . SER D 1 136 ? 47.575  32.860  25.128  1.00 64.43  ? 132 SER C C   1 
ATOM   7500  O O   . SER D 1 136 ? 46.733  33.677  24.747  1.00 60.63  ? 132 SER C O   1 
ATOM   7501  C CB  . SER D 1 136 ? 47.022  31.603  27.205  1.00 62.66  ? 132 SER C CB  1 
ATOM   7502  O OG  . SER D 1 136 ? 47.051  30.428  26.414  1.00 60.60  ? 132 SER C OG  1 
ATOM   7503  N N   . ALA D 1 137 ? 48.235  32.050  24.302  1.00 74.12  ? 133 ALA C N   1 
ATOM   7504  C CA  . ALA D 1 137 ? 48.012  32.041  22.853  1.00 77.48  ? 133 ALA C CA  1 
ATOM   7505  C C   . ALA D 1 137 ? 46.658  31.434  22.473  1.00 77.53  ? 133 ALA C C   1 
ATOM   7506  O O   . ALA D 1 137 ? 46.164  31.654  21.365  1.00 80.69  ? 133 ALA C O   1 
ATOM   7507  C CB  . ALA D 1 137 ? 49.138  31.289  22.156  1.00 76.21  ? 133 ALA C CB  1 
ATOM   7508  N N   . ALA D 1 138 ? 46.066  30.669  23.388  1.00 73.53  ? 134 ALA C N   1 
ATOM   7509  C CA  . ALA D 1 138 ? 44.727  30.115  23.186  1.00 64.75  ? 134 ALA C CA  1 
ATOM   7510  C C   . ALA D 1 138 ? 43.635  31.184  23.269  1.00 60.23  ? 134 ALA C C   1 
ATOM   7511  O O   . ALA D 1 138 ? 42.528  30.963  22.777  1.00 63.38  ? 134 ALA C O   1 
ATOM   7512  C CB  . ALA D 1 138 ? 44.455  29.009  24.193  1.00 67.53  ? 134 ALA C CB  1 
ATOM   7513  N N   . CYS D 1 139 ? 43.943  32.327  23.887  1.00 55.56  ? 135 CYS C N   1 
ATOM   7514  C CA  . CYS D 1 139 ? 43.006  33.451  23.995  1.00 59.94  ? 135 CYS C CA  1 
ATOM   7515  C C   . CYS D 1 139 ? 43.563  34.720  23.349  1.00 68.55  ? 135 CYS C C   1 
ATOM   7516  O O   . CYS D 1 139 ? 43.927  35.664  24.055  1.00 67.39  ? 135 CYS C O   1 
ATOM   7517  C CB  . CYS D 1 139 ? 42.680  33.736  25.468  1.00 63.24  ? 135 CYS C CB  1 
ATOM   7518  S SG  . CYS D 1 139 ? 42.067  32.314  26.401  1.00 70.52  ? 135 CYS C SG  1 
ATOM   7519  N N   . PRO D 1 140 ? 43.617  34.761  22.002  1.00 79.47  ? 136 PRO C N   1 
ATOM   7520  C CA  . PRO D 1 140 ? 44.121  35.955  21.326  1.00 85.29  ? 136 PRO C CA  1 
ATOM   7521  C C   . PRO D 1 140 ? 43.086  37.074  21.289  1.00 84.63  ? 136 PRO C C   1 
ATOM   7522  O O   . PRO D 1 140 ? 41.892  36.798  21.206  1.00 79.76  ? 136 PRO C O   1 
ATOM   7523  C CB  . PRO D 1 140 ? 44.428  35.464  19.904  1.00 94.67  ? 136 PRO C CB  1 
ATOM   7524  C CG  . PRO D 1 140 ? 43.718  34.161  19.738  1.00 93.60  ? 136 PRO C CG  1 
ATOM   7525  C CD  . PRO D 1 140 ? 43.097  33.768  21.046  1.00 87.06  ? 136 PRO C CD  1 
ATOM   7526  N N   . TYR D 1 141 ? 43.548  38.321  21.350  1.00 90.17  ? 137 TYR C N   1 
ATOM   7527  C CA  . TYR D 1 141 ? 42.658  39.479  21.269  1.00 93.97  ? 137 TYR C CA  1 
ATOM   7528  C C   . TYR D 1 141 ? 42.712  40.121  19.869  1.00 108.13 ? 137 TYR C C   1 
ATOM   7529  O O   . TYR D 1 141 ? 41.819  39.892  19.051  1.00 111.69 ? 137 TYR C O   1 
ATOM   7530  C CB  . TYR D 1 141 ? 42.970  40.486  22.378  1.00 91.22  ? 137 TYR C CB  1 
ATOM   7531  C CG  . TYR D 1 141 ? 42.011  41.670  22.350  1.00 107.55 ? 137 TYR C CG  1 
ATOM   7532  C CD1 . TYR D 1 141 ? 40.687  41.547  22.781  1.00 119.53 ? 137 TYR C CD1 1 
ATOM   7533  C CD2 . TYR D 1 141 ? 42.419  42.902  21.858  1.00 115.26 ? 137 TYR C CD2 1 
ATOM   7534  C CE1 . TYR D 1 141 ? 39.810  42.622  22.742  1.00 124.30 ? 137 TYR C CE1 1 
ATOM   7535  C CE2 . TYR D 1 141 ? 41.551  43.986  21.815  1.00 118.58 ? 137 TYR C CE2 1 
ATOM   7536  C CZ  . TYR D 1 141 ? 40.248  43.840  22.256  1.00 120.71 ? 137 TYR C CZ  1 
ATOM   7537  O OH  . TYR D 1 141 ? 39.385  44.911  22.217  1.00 108.95 ? 137 TYR C OH  1 
ATOM   7538  N N   . GLN D 1 142 ? 43.750  40.907  19.587  1.00 106.07 ? 138 GLN C N   1 
ATOM   7539  C CA  . GLN D 1 142 ? 43.961  41.436  18.239  1.00 99.33  ? 138 GLN C CA  1 
ATOM   7540  C C   . GLN D 1 142 ? 45.300  40.912  17.736  1.00 92.66  ? 138 GLN C C   1 
ATOM   7541  O O   . GLN D 1 142 ? 46.190  41.685  17.385  1.00 94.74  ? 138 GLN C O   1 
ATOM   7542  C CB  . GLN D 1 142 ? 43.961  42.964  18.224  1.00 103.17 ? 138 GLN C CB  1 
ATOM   7543  C CG  . GLN D 1 142 ? 42.639  43.681  18.441  1.00 108.98 ? 138 GLN C CG  1 
ATOM   7544  C CD  . GLN D 1 142 ? 42.753  45.189  18.270  1.00 114.00 ? 138 GLN C CD  1 
ATOM   7545  O OE1 . GLN D 1 142 ? 43.591  45.680  17.508  1.00 119.29 ? 138 GLN C OE1 1 
ATOM   7546  N NE2 . GLN D 1 142 ? 41.894  45.930  18.964  1.00 102.93 ? 138 GLN C NE2 1 
ATOM   7547  N N   . GLY D 1 143 ? 45.436  39.589  17.732  1.00 93.36  ? 139 GLY C N   1 
ATOM   7548  C CA  . GLY D 1 143 ? 46.680  38.926  17.346  1.00 91.17  ? 139 GLY C CA  1 
ATOM   7549  C C   . GLY D 1 143 ? 47.601  38.668  18.525  1.00 94.66  ? 139 GLY C C   1 
ATOM   7550  O O   . GLY D 1 143 ? 48.280  37.643  18.578  1.00 80.38  ? 139 GLY C O   1 
ATOM   7551  N N   . LYS D 1 144 ? 47.644  39.611  19.462  1.00 101.94 ? 140 LYS C N   1 
ATOM   7552  C CA  . LYS D 1 144 ? 48.406  39.449  20.696  1.00 103.01 ? 140 LYS C CA  1 
ATOM   7553  C C   . LYS D 1 144 ? 47.702  38.475  21.633  1.00 93.96  ? 140 LYS C C   1 
ATOM   7554  O O   . LYS D 1 144 ? 46.481  38.526  21.765  1.00 102.36 ? 140 LYS C O   1 
ATOM   7555  C CB  . LYS D 1 144 ? 48.558  40.805  21.389  1.00 105.69 ? 140 LYS C CB  1 
ATOM   7556  C CG  . LYS D 1 144 ? 49.471  40.780  22.610  1.00 107.65 ? 140 LYS C CG  1 
ATOM   7557  C CD  . LYS D 1 144 ? 49.206  41.911  23.588  1.00 104.42 ? 140 LYS C CD  1 
ATOM   7558  C CE  . LYS D 1 144 ? 49.912  41.652  24.908  1.00 99.07  ? 140 LYS C CE  1 
ATOM   7559  N NZ  . LYS D 1 144 ? 49.676  42.731  25.905  1.00 102.93 ? 140 LYS C NZ  1 
ATOM   7560  N N   . SER D 1 145 ? 48.477  37.611  22.293  1.00 76.68  ? 141 SER C N   1 
ATOM   7561  C CA  . SER D 1 145 ? 47.932  36.644  23.245  1.00 73.55  ? 141 SER C CA  1 
ATOM   7562  C C   . SER D 1 145 ? 47.386  37.344  24.494  1.00 75.78  ? 141 SER C C   1 
ATOM   7563  O O   . SER D 1 145 ? 47.997  38.290  24.995  1.00 75.50  ? 141 SER C O   1 
ATOM   7564  C CB  . SER D 1 145 ? 49.001  35.623  23.642  1.00 67.92  ? 141 SER C CB  1 
ATOM   7565  O OG  . SER D 1 145 ? 50.164  36.260  24.122  1.00 67.33  ? 141 SER C OG  1 
ATOM   7566  N N   . SER D 1 146 ? 46.239  36.870  24.984  1.00 67.21  ? 142 SER C N   1 
ATOM   7567  C CA  . SER D 1 146 ? 45.526  37.518  26.091  1.00 59.45  ? 142 SER C CA  1 
ATOM   7568  C C   . SER D 1 146 ? 44.829  36.490  27.004  1.00 58.09  ? 142 SER C C   1 
ATOM   7569  O O   . SER D 1 146 ? 45.262  35.340  27.103  1.00 55.47  ? 142 SER C O   1 
ATOM   7570  C CB  . SER D 1 146 ? 44.517  38.530  25.528  1.00 55.05  ? 142 SER C CB  1 
ATOM   7571  O OG  . SER D 1 146 ? 43.982  39.355  26.550  1.00 54.04  ? 142 SER C OG  1 
ATOM   7572  N N   . PHE D 1 147 ? 43.759  36.915  27.674  1.00 51.17  ? 143 PHE C N   1 
ATOM   7573  C CA  . PHE D 1 147 ? 43.048  36.074  28.638  1.00 53.73  ? 143 PHE C CA  1 
ATOM   7574  C C   . PHE D 1 147 ? 41.655  36.646  28.918  1.00 51.95  ? 143 PHE C C   1 
ATOM   7575  O O   . PHE D 1 147 ? 41.343  37.764  28.507  1.00 50.26  ? 143 PHE C O   1 
ATOM   7576  C CB  . PHE D 1 147 ? 43.856  35.997  29.942  1.00 51.40  ? 143 PHE C CB  1 
ATOM   7577  C CG  . PHE D 1 147 ? 43.431  34.891  30.867  1.00 49.64  ? 143 PHE C CG  1 
ATOM   7578  C CD1 . PHE D 1 147 ? 43.553  33.563  30.485  1.00 47.99  ? 143 PHE C CD1 1 
ATOM   7579  C CD2 . PHE D 1 147 ? 42.920  35.179  32.131  1.00 54.64  ? 143 PHE C CD2 1 
ATOM   7580  C CE1 . PHE D 1 147 ? 43.166  32.539  31.336  1.00 50.30  ? 143 PHE C CE1 1 
ATOM   7581  C CE2 . PHE D 1 147 ? 42.535  34.160  32.988  1.00 47.61  ? 143 PHE C CE2 1 
ATOM   7582  C CZ  . PHE D 1 147 ? 42.658  32.840  32.591  1.00 51.48  ? 143 PHE C CZ  1 
ATOM   7583  N N   . PHE D 1 148 ? 40.820  35.867  29.604  1.00 53.14  ? 144 PHE C N   1 
ATOM   7584  C CA  . PHE D 1 148 ? 39.509  36.336  30.068  1.00 51.42  ? 144 PHE C CA  1 
ATOM   7585  C C   . PHE D 1 148 ? 39.680  37.671  30.797  1.00 50.67  ? 144 PHE C C   1 
ATOM   7586  O O   . PHE D 1 148 ? 40.520  37.792  31.686  1.00 49.63  ? 144 PHE C O   1 
ATOM   7587  C CB  . PHE D 1 148 ? 38.856  35.313  31.013  1.00 46.49  ? 144 PHE C CB  1 
ATOM   7588  C CG  . PHE D 1 148 ? 38.653  33.951  30.405  1.00 41.34  ? 144 PHE C CG  1 
ATOM   7589  C CD1 . PHE D 1 148 ? 39.566  32.932  30.638  1.00 43.75  ? 144 PHE C CD1 1 
ATOM   7590  C CD2 . PHE D 1 148 ? 37.547  33.682  29.614  1.00 39.57  ? 144 PHE C CD2 1 
ATOM   7591  C CE1 . PHE D 1 148 ? 39.386  31.676  30.083  1.00 42.57  ? 144 PHE C CE1 1 
ATOM   7592  C CE2 . PHE D 1 148 ? 37.358  32.427  29.059  1.00 38.58  ? 144 PHE C CE2 1 
ATOM   7593  C CZ  . PHE D 1 148 ? 38.279  31.424  29.291  1.00 42.01  ? 144 PHE C CZ  1 
ATOM   7594  N N   . ARG D 1 149 ? 38.878  38.660  30.419  1.00 54.03  ? 145 ARG C N   1 
ATOM   7595  C CA  . ARG D 1 149 ? 39.059  40.033  30.891  1.00 64.79  ? 145 ARG C CA  1 
ATOM   7596  C C   . ARG D 1 149 ? 38.533  40.296  32.307  1.00 62.54  ? 145 ARG C C   1 
ATOM   7597  O O   . ARG D 1 149 ? 38.994  41.223  32.977  1.00 52.13  ? 145 ARG C O   1 
ATOM   7598  C CB  . ARG D 1 149 ? 38.402  41.013  29.910  1.00 75.36  ? 145 ARG C CB  1 
ATOM   7599  C CG  . ARG D 1 149 ? 39.096  41.078  28.555  1.00 87.27  ? 145 ARG C CG  1 
ATOM   7600  C CD  . ARG D 1 149 ? 38.507  42.131  27.637  1.00 100.02 ? 145 ARG C CD  1 
ATOM   7601  N NE  . ARG D 1 149 ? 39.485  42.607  26.655  1.00 116.53 ? 145 ARG C NE  1 
ATOM   7602  C CZ  . ARG D 1 149 ? 40.360  43.590  26.868  1.00 126.58 ? 145 ARG C CZ  1 
ATOM   7603  N NH1 . ARG D 1 149 ? 40.398  44.230  28.035  1.00 130.45 ? 145 ARG C NH1 1 
ATOM   7604  N NH2 . ARG D 1 149 ? 41.206  43.940  25.906  1.00 123.15 ? 145 ARG C NH2 1 
ATOM   7605  N N   . ASN D 1 150 ? 37.576  39.491  32.763  1.00 63.72  ? 146 ASN C N   1 
ATOM   7606  C CA  . ASN D 1 150 ? 36.936  39.720  34.065  1.00 62.47  ? 146 ASN C CA  1 
ATOM   7607  C C   . ASN D 1 150 ? 37.609  38.992  35.223  1.00 54.77  ? 146 ASN C C   1 
ATOM   7608  O O   . ASN D 1 150 ? 37.148  39.069  36.363  1.00 48.74  ? 146 ASN C O   1 
ATOM   7609  C CB  . ASN D 1 150 ? 35.458  39.341  33.994  1.00 59.64  ? 146 ASN C CB  1 
ATOM   7610  C CG  . ASN D 1 150 ? 34.732  40.082  32.889  1.00 58.77  ? 146 ASN C CG  1 
ATOM   7611  O OD1 . ASN D 1 150 ? 34.999  41.257  32.644  1.00 59.69  ? 146 ASN C OD1 1 
ATOM   7612  N ND2 . ASN D 1 150 ? 33.831  39.393  32.199  1.00 60.89  ? 146 ASN C ND2 1 
ATOM   7613  N N   . VAL D 1 151 ? 38.723  38.329  34.931  1.00 52.57  ? 147 VAL C N   1 
ATOM   7614  C CA  . VAL D 1 151 ? 39.370  37.446  35.888  1.00 56.25  ? 147 VAL C CA  1 
ATOM   7615  C C   . VAL D 1 151 ? 40.897  37.536  35.704  1.00 53.98  ? 147 VAL C C   1 
ATOM   7616  O O   . VAL D 1 151 ? 41.379  37.708  34.581  1.00 57.19  ? 147 VAL C O   1 
ATOM   7617  C CB  . VAL D 1 151 ? 38.824  36.011  35.690  1.00 54.35  ? 147 VAL C CB  1 
ATOM   7618  C CG1 . VAL D 1 151 ? 39.674  35.225  34.703  1.00 47.18  ? 147 VAL C CG1 1 
ATOM   7619  C CG2 . VAL D 1 151 ? 38.705  35.291  37.023  1.00 56.95  ? 147 VAL C CG2 1 
ATOM   7620  N N   . VAL D 1 152 ? 41.648  37.442  36.803  1.00 55.04  ? 148 VAL C N   1 
ATOM   7621  C CA  . VAL D 1 152 ? 43.099  37.690  36.787  1.00 50.13  ? 148 VAL C CA  1 
ATOM   7622  C C   . VAL D 1 152 ? 43.908  36.440  37.112  1.00 45.86  ? 148 VAL C C   1 
ATOM   7623  O O   . VAL D 1 152 ? 43.771  35.871  38.195  1.00 46.84  ? 148 VAL C O   1 
ATOM   7624  C CB  . VAL D 1 152 ? 43.494  38.775  37.805  1.00 55.57  ? 148 VAL C CB  1 
ATOM   7625  C CG1 . VAL D 1 152 ? 45.001  38.991  37.787  1.00 57.61  ? 148 VAL C CG1 1 
ATOM   7626  C CG2 . VAL D 1 152 ? 42.765  40.076  37.506  1.00 58.43  ? 148 VAL C CG2 1 
ATOM   7627  N N   . TRP D 1 153 ? 44.758  36.035  36.175  1.00 40.79  ? 149 TRP C N   1 
ATOM   7628  C CA  . TRP D 1 153 ? 45.605  34.856  36.329  1.00 40.89  ? 149 TRP C CA  1 
ATOM   7629  C C   . TRP D 1 153 ? 46.898  35.270  36.972  1.00 43.85  ? 149 TRP C C   1 
ATOM   7630  O O   . TRP D 1 153 ? 47.849  35.657  36.287  1.00 48.94  ? 149 TRP C O   1 
ATOM   7631  C CB  . TRP D 1 153 ? 45.837  34.223  34.957  1.00 41.53  ? 149 TRP C CB  1 
ATOM   7632  C CG  . TRP D 1 153 ? 46.650  32.950  34.934  1.00 38.83  ? 149 TRP C CG  1 
ATOM   7633  C CD1 . TRP D 1 153 ? 47.385  32.377  35.968  1.00 40.86  ? 149 TRP C CD1 1 
ATOM   7634  C CD2 . TRP D 1 153 ? 46.860  32.060  33.783  1.00 37.13  ? 149 TRP C CD2 1 
ATOM   7635  N NE1 . TRP D 1 153 ? 47.996  31.220  35.554  1.00 40.49  ? 149 TRP C NE1 1 
ATOM   7636  C CE2 . TRP D 1 153 ? 47.727  30.978  34.253  1.00 38.65  ? 149 TRP C CE2 1 
ATOM   7637  C CE3 . TRP D 1 153 ? 46.425  32.050  32.465  1.00 38.60  ? 149 TRP C CE3 1 
ATOM   7638  C CZ2 . TRP D 1 153 ? 48.127  29.943  33.421  1.00 38.92  ? 149 TRP C CZ2 1 
ATOM   7639  C CZ3 . TRP D 1 153 ? 46.832  31.001  31.633  1.00 37.45  ? 149 TRP C CZ3 1 
ATOM   7640  C CH2 . TRP D 1 153 ? 47.661  29.972  32.104  1.00 39.90  ? 149 TRP C CH2 1 
ATOM   7641  N N   . LEU D 1 154 ? 46.946  35.189  38.301  1.00 42.23  ? 150 LEU C N   1 
ATOM   7642  C CA  . LEU D 1 154 ? 48.104  35.645  39.071  1.00 42.44  ? 150 LEU C CA  1 
ATOM   7643  C C   . LEU D 1 154 ? 49.319  34.732  38.887  1.00 40.95  ? 150 LEU C C   1 
ATOM   7644  O O   . LEU D 1 154 ? 49.193  33.510  38.891  1.00 46.17  ? 150 LEU C O   1 
ATOM   7645  C CB  . LEU D 1 154 ? 47.753  35.752  40.558  1.00 45.42  ? 150 LEU C CB  1 
ATOM   7646  C CG  . LEU D 1 154 ? 46.664  36.771  40.915  1.00 44.00  ? 150 LEU C CG  1 
ATOM   7647  C CD1 . LEU D 1 154 ? 46.192  36.566  42.347  1.00 39.52  ? 150 LEU C CD1 1 
ATOM   7648  C CD2 . LEU D 1 154 ? 47.144  38.201  40.709  1.00 43.04  ? 150 LEU C CD2 1 
ATOM   7649  N N   . ILE D 1 155 ? 50.489  35.346  38.722  1.00 45.24  ? 151 ILE C N   1 
ATOM   7650  C CA  . ILE D 1 155 ? 51.767  34.632  38.580  1.00 43.02  ? 151 ILE C CA  1 
ATOM   7651  C C   . ILE D 1 155 ? 52.750  35.167  39.625  1.00 40.45  ? 151 ILE C C   1 
ATOM   7652  O O   . ILE D 1 155 ? 52.570  36.270  40.150  1.00 45.72  ? 151 ILE C O   1 
ATOM   7653  C CB  . ILE D 1 155 ? 52.322  34.766  37.132  1.00 43.95  ? 151 ILE C CB  1 
ATOM   7654  C CG1 . ILE D 1 155 ? 52.086  33.486  36.335  1.00 42.41  ? 151 ILE C CG1 1 
ATOM   7655  C CG2 . ILE D 1 155 ? 53.815  35.047  37.103  1.00 45.04  ? 151 ILE C CG2 1 
ATOM   7656  C CD1 . ILE D 1 155 ? 50.639  33.209  36.016  1.00 37.85  ? 151 ILE C CD1 1 
ATOM   7657  N N   . LYS D 1 156 ? 53.775  34.377  39.935  1.00 43.63  ? 152 LYS C N   1 
ATOM   7658  C CA  . LYS D 1 156 ? 54.776  34.750  40.943  1.00 49.16  ? 152 LYS C CA  1 
ATOM   7659  C C   . LYS D 1 156 ? 55.506  36.049  40.597  1.00 48.11  ? 152 LYS C C   1 
ATOM   7660  O O   . LYS D 1 156 ? 55.714  36.363  39.425  1.00 44.63  ? 152 LYS C O   1 
ATOM   7661  C CB  . LYS D 1 156 ? 55.804  33.626  41.119  1.00 50.73  ? 152 LYS C CB  1 
ATOM   7662  C CG  . LYS D 1 156 ? 56.751  33.453  39.943  1.00 48.54  ? 152 LYS C CG  1 
ATOM   7663  C CD  . LYS D 1 156 ? 57.581  32.193  40.086  1.00 47.79  ? 152 LYS C CD  1 
ATOM   7664  C CE  . LYS D 1 156 ? 58.778  32.200  39.149  1.00 43.39  ? 152 LYS C CE  1 
ATOM   7665  N NZ  . LYS D 1 156 ? 59.394  30.846  39.051  1.00 38.09  ? 152 LYS C NZ  1 
ATOM   7666  N N   . LYS D 1 157 ? 55.883  36.797  41.632  1.00 57.74  ? 153 LYS C N   1 
ATOM   7667  C CA  . LYS D 1 157 ? 56.670  38.016  41.477  1.00 57.75  ? 153 LYS C CA  1 
ATOM   7668  C C   . LYS D 1 157 ? 58.089  37.733  41.945  1.00 61.99  ? 153 LYS C C   1 
ATOM   7669  O O   . LYS D 1 157 ? 58.291  37.112  42.994  1.00 61.52  ? 153 LYS C O   1 
ATOM   7670  C CB  . LYS D 1 157 ? 56.058  39.156  42.287  1.00 59.71  ? 153 LYS C CB  1 
ATOM   7671  C CG  . LYS D 1 157 ? 56.559  40.533  41.887  1.00 61.57  ? 153 LYS C CG  1 
ATOM   7672  C CD  . LYS D 1 157 ? 55.797  41.630  42.611  1.00 62.59  ? 153 LYS C CD  1 
ATOM   7673  C CE  . LYS D 1 157 ? 56.163  43.006  42.083  1.00 64.63  ? 153 LYS C CE  1 
ATOM   7674  N NZ  . LYS D 1 157 ? 55.160  44.020  42.514  1.00 58.45  ? 153 LYS C NZ  1 
ATOM   7675  N N   . ASP D 1 158 ? 59.066  38.202  41.171  1.00 68.28  ? 154 ASP C N   1 
ATOM   7676  C CA  . ASP D 1 158 ? 60.474  37.845  41.366  1.00 72.68  ? 154 ASP C CA  1 
ATOM   7677  C C   . ASP D 1 158 ? 60.608  36.325  41.221  1.00 69.76  ? 154 ASP C C   1 
ATOM   7678  O O   . ASP D 1 158 ? 60.456  35.801  40.112  1.00 68.56  ? 154 ASP C O   1 
ATOM   7679  C CB  . ASP D 1 158 ? 61.007  38.370  42.710  1.00 73.39  ? 154 ASP C CB  1 
ATOM   7680  C CG  . ASP D 1 158 ? 60.857  39.874  42.846  1.00 86.13  ? 154 ASP C CG  1 
ATOM   7681  O OD1 . ASP D 1 158 ? 61.250  40.601  41.908  1.00 95.50  ? 154 ASP C OD1 1 
ATOM   7682  O OD2 . ASP D 1 158 ? 60.344  40.330  43.889  1.00 91.83  ? 154 ASP C OD2 1 
ATOM   7683  N N   . ASN D 1 159 ? 60.887  35.621  42.315  1.00 59.26  ? 155 ASN C N   1 
ATOM   7684  C CA  . ASN D 1 159 ? 60.796  34.164  42.336  1.00 59.45  ? 155 ASN C CA  1 
ATOM   7685  C C   . ASN D 1 159 ? 60.152  33.732  43.648  1.00 54.35  ? 155 ASN C C   1 
ATOM   7686  O O   . ASN D 1 159 ? 60.719  32.957  44.415  1.00 56.53  ? 155 ASN C O   1 
ATOM   7687  C CB  . ASN D 1 159 ? 62.172  33.517  42.131  1.00 66.94  ? 155 ASN C CB  1 
ATOM   7688  C CG  . ASN D 1 159 ? 62.544  33.392  40.651  1.00 69.93  ? 155 ASN C CG  1 
ATOM   7689  O OD1 . ASN D 1 159 ? 62.581  32.290  40.082  1.00 74.02  ? 155 ASN C OD1 1 
ATOM   7690  N ND2 . ASN D 1 159 ? 62.794  34.529  40.014  1.00 68.42  ? 155 ASN C ND2 1 
ATOM   7691  N N   . ALA D 1 160 ? 58.950  34.247  43.887  1.00 48.01  ? 156 ALA C N   1 
ATOM   7692  C CA  . ALA D 1 160 ? 58.222  33.988  45.120  1.00 45.44  ? 156 ALA C CA  1 
ATOM   7693  C C   . ALA D 1 160 ? 56.713  34.138  44.907  1.00 45.89  ? 156 ALA C C   1 
ATOM   7694  O O   . ALA D 1 160 ? 56.267  35.003  44.149  1.00 45.02  ? 156 ALA C O   1 
ATOM   7695  C CB  . ALA D 1 160 ? 58.701  34.935  46.213  1.00 36.77  ? 156 ALA C CB  1 
ATOM   7696  N N   . TYR D 1 161 ? 55.938  33.279  45.568  1.00 46.50  ? 157 TYR C N   1 
ATOM   7697  C CA  . TYR D 1 161 ? 54.479  33.373  45.571  1.00 42.94  ? 157 TYR C CA  1 
ATOM   7698  C C   . TYR D 1 161 ? 54.025  33.303  47.029  1.00 38.77  ? 157 TYR C C   1 
ATOM   7699  O O   . TYR D 1 161 ? 53.685  32.232  47.535  1.00 34.78  ? 157 TYR C O   1 
ATOM   7700  C CB  . TYR D 1 161 ? 53.860  32.247  44.732  1.00 41.92  ? 157 TYR C CB  1 
ATOM   7701  C CG  . TYR D 1 161 ? 52.391  32.434  44.369  1.00 40.64  ? 157 TYR C CG  1 
ATOM   7702  C CD1 . TYR D 1 161 ? 52.001  32.609  43.041  1.00 42.66  ? 157 TYR C CD1 1 
ATOM   7703  C CD2 . TYR D 1 161 ? 51.392  32.419  45.346  1.00 38.93  ? 157 TYR C CD2 1 
ATOM   7704  C CE1 . TYR D 1 161 ? 50.668  32.773  42.700  1.00 42.26  ? 157 TYR C CE1 1 
ATOM   7705  C CE2 . TYR D 1 161 ? 50.057  32.580  45.017  1.00 40.48  ? 157 TYR C CE2 1 
ATOM   7706  C CZ  . TYR D 1 161 ? 49.696  32.759  43.697  1.00 42.94  ? 157 TYR C CZ  1 
ATOM   7707  O OH  . TYR D 1 161 ? 48.364  32.918  43.369  1.00 46.43  ? 157 TYR C OH  1 
ATOM   7708  N N   . PRO D 1 162 ? 54.048  34.448  47.724  1.00 40.38  ? 158 PRO C N   1 
ATOM   7709  C CA  . PRO D 1 162 ? 53.583  34.472  49.105  1.00 45.86  ? 158 PRO C CA  1 
ATOM   7710  C C   . PRO D 1 162 ? 52.105  34.114  49.199  1.00 46.40  ? 158 PRO C C   1 
ATOM   7711  O O   . PRO D 1 162 ? 51.345  34.385  48.262  1.00 45.56  ? 158 PRO C O   1 
ATOM   7712  C CB  . PRO D 1 162 ? 53.805  35.928  49.535  1.00 49.35  ? 158 PRO C CB  1 
ATOM   7713  C CG  . PRO D 1 162 ? 54.757  36.499  48.543  1.00 48.45  ? 158 PRO C CG  1 
ATOM   7714  C CD  . PRO D 1 162 ? 54.483  35.777  47.265  1.00 45.61  ? 158 PRO C CD  1 
ATOM   7715  N N   . THR D 1 163 ? 51.712  33.501  50.312  1.00 42.52  ? 159 THR C N   1 
ATOM   7716  C CA  . THR D 1 163 ? 50.337  33.059  50.493  1.00 43.00  ? 159 THR C CA  1 
ATOM   7717  C C   . THR D 1 163 ? 49.386  34.252  50.474  1.00 50.01  ? 159 THR C C   1 
ATOM   7718  O O   . THR D 1 163 ? 49.570  35.219  51.213  1.00 57.79  ? 159 THR C O   1 
ATOM   7719  C CB  . THR D 1 163 ? 50.166  32.290  51.814  1.00 45.13  ? 159 THR C CB  1 
ATOM   7720  O OG1 . THR D 1 163 ? 51.027  31.144  51.813  1.00 46.07  ? 159 THR C OG1 1 
ATOM   7721  C CG2 . THR D 1 163 ? 48.728  31.838  51.990  1.00 44.77  ? 159 THR C CG2 1 
ATOM   7722  N N   . ILE D 1 164 ? 48.385  34.181  49.603  1.00 48.13  ? 160 ILE C N   1 
ATOM   7723  C CA  . ILE D 1 164 ? 47.363  35.217  49.499  1.00 43.80  ? 160 ILE C CA  1 
ATOM   7724  C C   . ILE D 1 164 ? 46.296  35.001  50.561  1.00 42.47  ? 160 ILE C C   1 
ATOM   7725  O O   . ILE D 1 164 ? 45.890  33.871  50.801  1.00 42.17  ? 160 ILE C O   1 
ATOM   7726  C CB  . ILE D 1 164 ? 46.679  35.182  48.120  1.00 43.73  ? 160 ILE C CB  1 
ATOM   7727  C CG1 . ILE D 1 164 ? 47.675  35.551  47.017  1.00 43.45  ? 160 ILE C CG1 1 
ATOM   7728  C CG2 . ILE D 1 164 ? 45.479  36.115  48.093  1.00 39.47  ? 160 ILE C CG2 1 
ATOM   7729  C CD1 . ILE D 1 164 ? 47.178  35.225  45.625  1.00 38.54  ? 160 ILE C CD1 1 
ATOM   7730  N N   . LYS D 1 165 ? 45.852  36.089  51.186  1.00 44.47  ? 161 LYS C N   1 
ATOM   7731  C CA  . LYS D 1 165 ? 44.712  36.074  52.108  1.00 44.22  ? 161 LYS C CA  1 
ATOM   7732  C C   . LYS D 1 165 ? 43.842  37.292  51.811  1.00 46.10  ? 161 LYS C C   1 
ATOM   7733  O O   . LYS D 1 165 ? 43.909  38.303  52.511  1.00 48.84  ? 161 LYS C O   1 
ATOM   7734  C CB  . LYS D 1 165 ? 45.179  36.097  53.567  1.00 44.74  ? 161 LYS C CB  1 
ATOM   7735  C CG  . LYS D 1 165 ? 45.674  34.753  54.113  1.00 47.32  ? 161 LYS C CG  1 
ATOM   7736  C CD  . LYS D 1 165 ? 47.053  34.921  54.737  1.00 50.88  ? 161 LYS C CD  1 
ATOM   7737  C CE  . LYS D 1 165 ? 47.488  33.652  55.458  1.00 48.87  ? 161 LYS C CE  1 
ATOM   7738  N NZ  . LYS D 1 165 ? 47.480  33.852  56.931  1.00 49.83  ? 161 LYS C NZ  1 
ATOM   7739  N N   . LYS D 1 166 ? 43.041  37.195  50.755  1.00 49.31  ? 162 LYS C N   1 
ATOM   7740  C CA  . LYS D 1 166 ? 42.200  38.302  50.306  1.00 54.59  ? 162 LYS C CA  1 
ATOM   7741  C C   . LYS D 1 166 ? 40.741  37.999  50.624  1.00 53.40  ? 162 LYS C C   1 
ATOM   7742  O O   . LYS D 1 166 ? 40.269  36.882  50.404  1.00 51.08  ? 162 LYS C O   1 
ATOM   7743  C CB  . LYS D 1 166 ? 42.370  38.530  48.796  1.00 61.44  ? 162 LYS C CB  1 
ATOM   7744  C CG  . LYS D 1 166 ? 41.862  39.878  48.291  1.00 64.86  ? 162 LYS C CG  1 
ATOM   7745  C CD  . LYS D 1 166 ? 42.910  40.974  48.443  1.00 70.23  ? 162 LYS C CD  1 
ATOM   7746  C CE  . LYS D 1 166 ? 42.370  42.341  48.044  1.00 70.32  ? 162 LYS C CE  1 
ATOM   7747  N NZ  . LYS D 1 166 ? 41.910  43.133  49.221  1.00 67.87  ? 162 LYS C NZ  1 
ATOM   7748  N N   . GLY D 1 167 ? 40.031  39.005  51.125  1.00 56.03  ? 163 GLY C N   1 
ATOM   7749  C CA  . GLY D 1 167 ? 38.605  38.883  51.423  1.00 58.76  ? 163 GLY C CA  1 
ATOM   7750  C C   . GLY D 1 167 ? 37.805  40.034  50.839  1.00 56.22  ? 163 GLY C C   1 
ATOM   7751  O O   . GLY D 1 167 ? 38.331  41.132  50.660  1.00 54.97  ? 163 GLY C O   1 
ATOM   7752  N N   . TYR D 1 168 ? 36.537  39.776  50.524  1.00 53.34  ? 164 TYR C N   1 
ATOM   7753  C CA  . TYR D 1 168 ? 35.629  40.816  50.051  1.00 50.71  ? 164 TYR C CA  1 
ATOM   7754  C C   . TYR D 1 168 ? 34.282  40.716  50.750  1.00 50.50  ? 164 TYR C C   1 
ATOM   7755  O O   . TYR D 1 168 ? 33.637  39.670  50.714  1.00 46.16  ? 164 TYR C O   1 
ATOM   7756  C CB  . TYR D 1 168 ? 35.418  40.733  48.539  1.00 48.38  ? 164 TYR C CB  1 
ATOM   7757  C CG  . TYR D 1 168 ? 34.442  41.778  48.042  1.00 51.77  ? 164 TYR C CG  1 
ATOM   7758  C CD1 . TYR D 1 168 ? 34.864  43.078  47.775  1.00 56.87  ? 164 TYR C CD1 1 
ATOM   7759  C CD2 . TYR D 1 168 ? 33.093  41.478  47.869  1.00 46.21  ? 164 TYR C CD2 1 
ATOM   7760  C CE1 . TYR D 1 168 ? 33.974  44.043  47.338  1.00 55.93  ? 164 TYR C CE1 1 
ATOM   7761  C CE2 . TYR D 1 168 ? 32.196  42.436  47.432  1.00 49.90  ? 164 TYR C CE2 1 
ATOM   7762  C CZ  . TYR D 1 168 ? 32.639  43.717  47.170  1.00 54.41  ? 164 TYR C CZ  1 
ATOM   7763  O OH  . TYR D 1 168 ? 31.756  44.677  46.734  1.00 56.28  ? 164 TYR C OH  1 
ATOM   7764  N N   . ASN D 1 169 ? 33.873  41.814  51.382  1.00 50.46  ? 165 ASN C N   1 
ATOM   7765  C CA  . ASN D 1 169 ? 32.568  41.913  52.016  1.00 55.78  ? 165 ASN C CA  1 
ATOM   7766  C C   . ASN D 1 169 ? 31.604  42.559  51.033  1.00 51.86  ? 165 ASN C C   1 
ATOM   7767  O O   . ASN D 1 169 ? 31.893  43.620  50.481  1.00 51.36  ? 165 ASN C O   1 
ATOM   7768  C CB  . ASN D 1 169 ? 32.670  42.739  53.305  1.00 60.12  ? 165 ASN C CB  1 
ATOM   7769  C CG  . ASN D 1 169 ? 31.390  42.718  54.132  1.00 62.98  ? 165 ASN C CG  1 
ATOM   7770  O OD1 . ASN D 1 169 ? 30.281  42.676  53.598  1.00 62.73  ? 165 ASN C OD1 1 
ATOM   7771  N ND2 . ASN D 1 169 ? 31.554  42.753  55.461  1.00 66.11  ? 165 ASN C ND2 1 
ATOM   7772  N N   . ASN D 1 170 ? 30.465  41.913  50.809  1.00 49.14  ? 166 ASN C N   1 
ATOM   7773  C CA  . ASN D 1 170 ? 29.436  42.463  49.938  1.00 52.85  ? 166 ASN C CA  1 
ATOM   7774  C C   . ASN D 1 170 ? 28.738  43.617  50.655  1.00 59.36  ? 166 ASN C C   1 
ATOM   7775  O O   . ASN D 1 170 ? 27.873  43.406  51.501  1.00 57.86  ? 166 ASN C O   1 
ATOM   7776  C CB  . ASN D 1 170 ? 28.435  41.374  49.532  1.00 50.21  ? 166 ASN C CB  1 
ATOM   7777  C CG  . ASN D 1 170 ? 27.424  41.849  48.499  1.00 48.19  ? 166 ASN C CG  1 
ATOM   7778  O OD1 . ASN D 1 170 ? 27.524  42.954  47.962  1.00 47.08  ? 166 ASN C OD1 1 
ATOM   7779  N ND2 . ASN D 1 170 ? 26.445  41.000  48.208  1.00 46.55  ? 166 ASN C ND2 1 
ATOM   7780  N N   . THR D 1 171 ? 29.145  44.837  50.321  1.00 66.67  ? 167 THR C N   1 
ATOM   7781  C CA  . THR D 1 171 ? 28.575  46.043  50.919  1.00 65.19  ? 167 THR C CA  1 
ATOM   7782  C C   . THR D 1 171 ? 27.331  46.513  50.165  1.00 65.16  ? 167 THR C C   1 
ATOM   7783  O O   . THR D 1 171 ? 26.615  47.389  50.638  1.00 67.15  ? 167 THR C O   1 
ATOM   7784  C CB  . THR D 1 171 ? 29.607  47.182  50.949  1.00 64.99  ? 167 THR C CB  1 
ATOM   7785  O OG1 . THR D 1 171 ? 30.162  47.365  49.638  1.00 61.03  ? 167 THR C OG1 1 
ATOM   7786  C CG2 . THR D 1 171 ? 30.722  46.857  51.932  1.00 61.36  ? 167 THR C CG2 1 
ATOM   7787  N N   . ASN D 1 172 ? 27.078  45.918  49.002  1.00 61.70  ? 168 ASN C N   1 
ATOM   7788  C CA  . ASN D 1 172 ? 25.914  46.252  48.184  1.00 56.23  ? 168 ASN C CA  1 
ATOM   7789  C C   . ASN D 1 172 ? 24.642  45.640  48.779  1.00 61.87  ? 168 ASN C C   1 
ATOM   7790  O O   . ASN D 1 172 ? 24.720  44.792  49.670  1.00 63.76  ? 168 ASN C O   1 
ATOM   7791  C CB  . ASN D 1 172 ? 26.137  45.762  46.750  1.00 53.85  ? 168 ASN C CB  1 
ATOM   7792  C CG  . ASN D 1 172 ? 27.525  46.114  46.226  1.00 56.12  ? 168 ASN C CG  1 
ATOM   7793  O OD1 . ASN D 1 172 ? 27.802  47.271  45.922  1.00 68.23  ? 168 ASN C OD1 1 
ATOM   7794  N ND2 . ASN D 1 172 ? 28.405  45.120  46.134  1.00 47.47  ? 168 ASN C ND2 1 
ATOM   7795  N N   . GLN D 1 173 ? 23.477  46.076  48.299  1.00 64.29  ? 169 GLN C N   1 
ATOM   7796  C CA  . GLN D 1 173 ? 22.189  45.549  48.788  1.00 68.15  ? 169 GLN C CA  1 
ATOM   7797  C C   . GLN D 1 173 ? 21.683  44.368  47.962  1.00 63.61  ? 169 GLN C C   1 
ATOM   7798  O O   . GLN D 1 173 ? 20.664  43.773  48.306  1.00 64.67  ? 169 GLN C O   1 
ATOM   7799  C CB  . GLN D 1 173 ? 21.100  46.637  48.873  1.00 79.65  ? 169 GLN C CB  1 
ATOM   7800  C CG  . GLN D 1 173 ? 20.981  47.304  50.236  1.00 87.13  ? 169 GLN C CG  1 
ATOM   7801  C CD  . GLN D 1 173 ? 22.078  48.288  50.560  1.00 89.54  ? 169 GLN C CD  1 
ATOM   7802  O OE1 . GLN D 1 173 ? 23.245  47.923  50.620  1.00 78.60  ? 169 GLN C OE1 1 
ATOM   7803  N NE2 . GLN D 1 173 ? 21.701  49.537  50.816  1.00 93.04  ? 169 GLN C NE2 1 
ATOM   7804  N N   . GLU D 1 174 ? 22.395  44.023  46.891  1.00 64.48  ? 170 GLU C N   1 
ATOM   7805  C CA  . GLU D 1 174 ? 22.000  42.916  46.020  1.00 70.09  ? 170 GLU C CA  1 
ATOM   7806  C C   . GLU D 1 174 ? 22.971  41.738  46.116  1.00 62.73  ? 170 GLU C C   1 
ATOM   7807  O O   . GLU D 1 174 ? 24.115  41.897  46.541  1.00 50.68  ? 170 GLU C O   1 
ATOM   7808  C CB  . GLU D 1 174 ? 21.907  43.393  44.567  1.00 83.80  ? 170 GLU C CB  1 
ATOM   7809  C CG  . GLU D 1 174 ? 20.721  44.316  44.287  1.00 101.17 ? 170 GLU C CG  1 
ATOM   7810  C CD  . GLU D 1 174 ? 21.096  45.796  44.106  1.00 116.24 ? 170 GLU C CD  1 
ATOM   7811  O OE1 . GLU D 1 174 ? 20.257  46.532  43.533  1.00 113.68 ? 170 GLU C OE1 1 
ATOM   7812  O OE2 . GLU D 1 174 ? 22.206  46.235  44.534  1.00 126.94 ? 170 GLU C OE2 1 
ATOM   7813  N N   . ASP D 1 175 ? 22.499  40.559  45.717  1.00 62.08  ? 171 ASP C N   1 
ATOM   7814  C CA  . ASP D 1 175 ? 23.341  39.367  45.645  1.00 58.40  ? 171 ASP C CA  1 
ATOM   7815  C C   . ASP D 1 175 ? 24.456  39.578  44.627  1.00 58.95  ? 171 ASP C C   1 
ATOM   7816  O O   . ASP D 1 175 ? 24.254  40.248  43.608  1.00 56.28  ? 171 ASP C O   1 
ATOM   7817  C CB  . ASP D 1 175 ? 22.518  38.137  45.235  1.00 60.24  ? 171 ASP C CB  1 
ATOM   7818  C CG  . ASP D 1 175 ? 21.568  37.663  46.324  1.00 61.73  ? 171 ASP C CG  1 
ATOM   7819  O OD1 . ASP D 1 175 ? 21.816  37.944  47.510  1.00 63.23  ? 171 ASP C OD1 1 
ATOM   7820  O OD2 . ASP D 1 175 ? 20.567  36.994  45.988  1.00 70.82  ? 171 ASP C OD2 1 
ATOM   7821  N N   . LEU D 1 176 ? 25.627  39.007  44.912  1.00 54.92  ? 172 LEU C N   1 
ATOM   7822  C CA  . LEU D 1 176 ? 26.774  39.090  44.012  1.00 52.61  ? 172 LEU C CA  1 
ATOM   7823  C C   . LEU D 1 176 ? 27.153  37.717  43.481  1.00 50.60  ? 172 LEU C C   1 
ATOM   7824  O O   . LEU D 1 176 ? 27.426  36.804  44.257  1.00 50.13  ? 172 LEU C O   1 
ATOM   7825  C CB  . LEU D 1 176 ? 27.983  39.696  44.725  1.00 60.18  ? 172 LEU C CB  1 
ATOM   7826  C CG  . LEU D 1 176 ? 28.132  41.212  44.627  1.00 67.53  ? 172 LEU C CG  1 
ATOM   7827  C CD1 . LEU D 1 176 ? 29.296  41.665  45.493  1.00 70.36  ? 172 LEU C CD1 1 
ATOM   7828  C CD2 . LEU D 1 176 ? 28.343  41.645  43.183  1.00 67.81  ? 172 LEU C CD2 1 
ATOM   7829  N N   . LEU D 1 177 ? 27.175  37.584  42.157  1.00 43.31  ? 173 LEU C N   1 
ATOM   7830  C CA  . LEU D 1 177 ? 27.704  36.391  41.508  1.00 41.20  ? 173 LEU C CA  1 
ATOM   7831  C C   . LEU D 1 177 ? 29.212  36.568  41.378  1.00 44.08  ? 173 LEU C C   1 
ATOM   7832  O O   . LEU D 1 177 ? 29.671  37.456  40.662  1.00 47.75  ? 173 LEU C O   1 
ATOM   7833  C CB  . LEU D 1 177 ? 27.063  36.193  40.128  1.00 37.00  ? 173 LEU C CB  1 
ATOM   7834  C CG  . LEU D 1 177 ? 27.643  35.094  39.234  1.00 35.80  ? 173 LEU C CG  1 
ATOM   7835  C CD1 . LEU D 1 177 ? 27.469  33.725  39.871  1.00 40.23  ? 173 LEU C CD1 1 
ATOM   7836  C CD2 . LEU D 1 177 ? 27.004  35.132  37.858  1.00 36.34  ? 173 LEU C CD2 1 
ATOM   7837  N N   . VAL D 1 178 ? 29.972  35.737  42.089  1.00 48.52  ? 174 VAL C N   1 
ATOM   7838  C CA  . VAL D 1 178 ? 31.433  35.803  42.082  1.00 44.23  ? 174 VAL C CA  1 
ATOM   7839  C C   . VAL D 1 178 ? 32.010  34.564  41.415  1.00 42.46  ? 174 VAL C C   1 
ATOM   7840  O O   . VAL D 1 178 ? 31.582  33.446  41.700  1.00 49.28  ? 174 VAL C O   1 
ATOM   7841  C CB  . VAL D 1 178 ? 31.997  35.911  43.511  1.00 42.69  ? 174 VAL C CB  1 
ATOM   7842  C CG1 . VAL D 1 178 ? 33.483  36.223  43.467  1.00 40.52  ? 174 VAL C CG1 1 
ATOM   7843  C CG2 . VAL D 1 178 ? 31.246  36.971  44.303  1.00 40.26  ? 174 VAL C CG2 1 
ATOM   7844  N N   . LEU D 1 179 ? 32.984  34.775  40.535  1.00 40.45  ? 175 LEU C N   1 
ATOM   7845  C CA  . LEU D 1 179 ? 33.626  33.701  39.784  1.00 39.66  ? 175 LEU C CA  1 
ATOM   7846  C C   . LEU D 1 179 ? 35.115  33.649  40.108  1.00 38.40  ? 175 LEU C C   1 
ATOM   7847  O O   . LEU D 1 179 ? 35.731  34.668  40.385  1.00 40.19  ? 175 LEU C O   1 
ATOM   7848  C CB  . LEU D 1 179 ? 33.463  33.937  38.286  1.00 42.32  ? 175 LEU C CB  1 
ATOM   7849  C CG  . LEU D 1 179 ? 32.035  34.099  37.751  1.00 44.41  ? 175 LEU C CG  1 
ATOM   7850  C CD1 . LEU D 1 179 ? 32.004  34.982  36.510  1.00 51.90  ? 175 LEU C CD1 1 
ATOM   7851  C CD2 . LEU D 1 179 ? 31.414  32.746  37.464  1.00 39.85  ? 175 LEU C CD2 1 
ATOM   7852  N N   . TRP D 1 180 ? 35.683  32.451  40.081  1.00 36.07  ? 176 TRP C N   1 
ATOM   7853  C CA  . TRP D 1 180 ? 37.119  32.276  40.234  1.00 35.77  ? 176 TRP C CA  1 
ATOM   7854  C C   . TRP D 1 180 ? 37.484  30.953  39.648  1.00 32.52  ? 176 TRP C C   1 
ATOM   7855  O O   . TRP D 1 180 ? 36.601  30.159  39.340  1.00 33.16  ? 176 TRP C O   1 
ATOM   7856  C CB  . TRP D 1 180 ? 37.527  32.347  41.705  1.00 37.98  ? 176 TRP C CB  1 
ATOM   7857  C CG  . TRP D 1 180 ? 36.971  31.223  42.539  1.00 38.77  ? 176 TRP C CG  1 
ATOM   7858  C CD1 . TRP D 1 180 ? 37.594  30.022  42.864  1.00 39.47  ? 176 TRP C CD1 1 
ATOM   7859  C CD2 . TRP D 1 180 ? 35.650  31.152  43.174  1.00 38.01  ? 176 TRP C CD2 1 
ATOM   7860  N NE1 . TRP D 1 180 ? 36.776  29.238  43.636  1.00 38.74  ? 176 TRP C NE1 1 
ATOM   7861  C CE2 . TRP D 1 180 ? 35.596  29.854  43.858  1.00 38.50  ? 176 TRP C CE2 1 
ATOM   7862  C CE3 . TRP D 1 180 ? 34.549  31.997  43.244  1.00 38.49  ? 176 TRP C CE3 1 
ATOM   7863  C CZ2 . TRP D 1 180 ? 34.482  29.447  44.572  1.00 35.69  ? 176 TRP C CZ2 1 
ATOM   7864  C CZ3 . TRP D 1 180 ? 33.430  31.573  43.970  1.00 40.75  ? 176 TRP C CZ3 1 
ATOM   7865  C CH2 . TRP D 1 180 ? 33.400  30.327  44.617  1.00 38.47  ? 176 TRP C CH2 1 
ATOM   7866  N N   . GLY D 1 181 ? 38.780  30.693  39.500  1.00 30.59  ? 177 GLY C N   1 
ATOM   7867  C CA  . GLY D 1 181 ? 39.234  29.439  38.904  1.00 32.35  ? 177 GLY C CA  1 
ATOM   7868  C C   . GLY D 1 181 ? 40.558  28.913  39.423  1.00 32.59  ? 177 GLY C C   1 
ATOM   7869  O O   . GLY D 1 181 ? 41.242  29.586  40.185  1.00 34.07  ? 177 GLY C O   1 
ATOM   7870  N N   . ILE D 1 182 ? 40.898  27.698  38.994  1.00 33.03  ? 178 ILE C N   1 
ATOM   7871  C CA  . ILE D 1 182 ? 42.157  27.023  39.338  1.00 39.44  ? 178 ILE C CA  1 
ATOM   7872  C C   . ILE D 1 182 ? 42.830  26.592  38.053  1.00 42.04  ? 178 ILE C C   1 
ATOM   7873  O O   . ILE D 1 182 ? 42.151  26.130  37.136  1.00 42.46  ? 178 ILE C O   1 
ATOM   7874  C CB  . ILE D 1 182 ? 41.950  25.699  40.123  1.00 44.17  ? 178 ILE C CB  1 
ATOM   7875  C CG1 . ILE D 1 182 ? 40.561  25.680  40.746  1.00 51.50  ? 178 ILE C CG1 1 
ATOM   7876  C CG2 . ILE D 1 182 ? 43.052  25.477  41.154  1.00 37.12  ? 178 ILE C CG2 1 
ATOM   7877  C CD1 . ILE D 1 182 ? 40.299  26.854  41.668  1.00 59.48  ? 178 ILE C CD1 1 
ATOM   7878  N N   . HIS D 1 183 ? 44.156  26.685  38.018  1.00 41.64  ? 179 HIS C N   1 
ATOM   7879  C CA  . HIS D 1 183 ? 44.942  26.245  36.872  1.00 39.35  ? 179 HIS C CA  1 
ATOM   7880  C C   . HIS D 1 183 ? 45.579  24.914  37.148  1.00 40.76  ? 179 HIS C C   1 
ATOM   7881  O O   . HIS D 1 183 ? 46.318  24.758  38.121  1.00 39.49  ? 179 HIS C O   1 
ATOM   7882  C CB  . HIS D 1 183 ? 46.012  27.274  36.537  1.00 41.73  ? 179 HIS C CB  1 
ATOM   7883  C CG  . HIS D 1 183 ? 46.982  26.827  35.464  1.00 47.38  ? 179 HIS C CG  1 
ATOM   7884  N ND1 . HIS D 1 183 ? 48.293  26.654  35.703  1.00 53.49  ? 179 HIS C ND1 1 
ATOM   7885  C CD2 . HIS D 1 183 ? 46.784  26.515  34.119  1.00 47.31  ? 179 HIS C CD2 1 
ATOM   7886  C CE1 . HIS D 1 183 ? 48.906  26.252  34.575  1.00 52.18  ? 179 HIS C CE1 1 
ATOM   7887  N NE2 . HIS D 1 183 ? 47.982  26.166  33.606  1.00 49.59  ? 179 HIS C NE2 1 
ATOM   7888  N N   . HIS D 1 184 ? 45.296  23.942  36.285  1.00 43.22  ? 180 HIS C N   1 
ATOM   7889  C CA  . HIS D 1 184 ? 45.933  22.630  36.342  1.00 43.79  ? 180 HIS C CA  1 
ATOM   7890  C C   . HIS D 1 184 ? 47.046  22.572  35.327  1.00 46.22  ? 180 HIS C C   1 
ATOM   7891  O O   . HIS D 1 184 ? 46.781  22.474  34.125  1.00 41.80  ? 180 HIS C O   1 
ATOM   7892  C CB  . HIS D 1 184 ? 44.913  21.542  36.042  1.00 44.24  ? 180 HIS C CB  1 
ATOM   7893  C CG  . HIS D 1 184 ? 43.692  21.587  36.925  1.00 39.53  ? 180 HIS C CG  1 
ATOM   7894  N ND1 . HIS D 1 184 ? 43.743  21.346  38.239  1.00 37.71  ? 180 HIS C ND1 1 
ATOM   7895  C CD2 . HIS D 1 184 ? 42.363  21.849  36.627  1.00 41.87  ? 180 HIS C CD2 1 
ATOM   7896  C CE1 . HIS D 1 184 ? 42.510  21.445  38.759  1.00 41.86  ? 180 HIS C CE1 1 
ATOM   7897  N NE2 . HIS D 1 184 ? 41.667  21.754  37.771  1.00 42.99  ? 180 HIS C NE2 1 
ATOM   7898  N N   . PRO D 1 185 ? 48.311  22.638  35.783  1.00 46.45  ? 181 PRO C N   1 
ATOM   7899  C CA  . PRO D 1 185 ? 49.431  22.622  34.841  1.00 44.81  ? 181 PRO C CA  1 
ATOM   7900  C C   . PRO D 1 185 ? 49.736  21.232  34.299  1.00 44.20  ? 181 PRO C C   1 
ATOM   7901  O O   . PRO D 1 185 ? 49.189  20.238  34.784  1.00 47.04  ? 181 PRO C O   1 
ATOM   7902  C CB  . PRO D 1 185 ? 50.597  23.132  35.682  1.00 48.92  ? 181 PRO C CB  1 
ATOM   7903  C CG  . PRO D 1 185 ? 50.273  22.693  37.061  1.00 48.40  ? 181 PRO C CG  1 
ATOM   7904  C CD  . PRO D 1 185 ? 48.775  22.681  37.181  1.00 46.28  ? 181 PRO C CD  1 
ATOM   7905  N N   . ASN D 1 186 ? 50.612  21.174  33.299  1.00 53.91  ? 182 ASN C N   1 
ATOM   7906  C CA  . ASN D 1 186 ? 50.925  19.926  32.606  1.00 53.48  ? 182 ASN C CA  1 
ATOM   7907  C C   . ASN D 1 186 ? 51.958  19.063  33.337  1.00 49.16  ? 182 ASN C C   1 
ATOM   7908  O O   . ASN D 1 186 ? 51.912  17.835  33.245  1.00 51.47  ? 182 ASN C O   1 
ATOM   7909  C CB  . ASN D 1 186 ? 51.410  20.219  31.180  1.00 62.89  ? 182 ASN C CB  1 
ATOM   7910  C CG  . ASN D 1 186 ? 51.318  19.000  30.273  1.00 84.80  ? 182 ASN C CG  1 
ATOM   7911  O OD1 . ASN D 1 186 ? 50.265  18.367  30.174  1.00 105.08 ? 182 ASN C OD1 1 
ATOM   7912  N ND2 . ASN D 1 186 ? 52.422  18.662  29.611  1.00 77.97  ? 182 ASN C ND2 1 
ATOM   7913  N N   . ASP D 1 187 ? 52.889  19.702  34.046  1.00 46.64  ? 183 ASP C N   1 
ATOM   7914  C CA  . ASP D 1 187 ? 53.935  18.988  34.798  1.00 49.18  ? 183 ASP C CA  1 
ATOM   7915  C C   . ASP D 1 187 ? 54.502  19.822  35.960  1.00 48.18  ? 183 ASP C C   1 
ATOM   7916  O O   . ASP D 1 187 ? 54.174  21.001  36.114  1.00 43.92  ? 183 ASP C O   1 
ATOM   7917  C CB  . ASP D 1 187 ? 55.064  18.536  33.857  1.00 46.92  ? 183 ASP C CB  1 
ATOM   7918  C CG  . ASP D 1 187 ? 55.624  19.673  33.020  1.00 55.69  ? 183 ASP C CG  1 
ATOM   7919  O OD1 . ASP D 1 187 ? 55.672  19.524  31.782  1.00 67.73  ? 183 ASP C OD1 1 
ATOM   7920  O OD2 . ASP D 1 187 ? 56.008  20.717  33.592  1.00 58.70  ? 183 ASP C OD2 1 
ATOM   7921  N N   . GLU D 1 188 ? 55.361  19.197  36.761  1.00 49.88  ? 184 GLU C N   1 
ATOM   7922  C CA  . GLU D 1 188 ? 55.930  19.831  37.956  1.00 56.39  ? 184 GLU C CA  1 
ATOM   7923  C C   . GLU D 1 188 ? 56.854  21.007  37.626  1.00 51.54  ? 184 GLU C C   1 
ATOM   7924  O O   . GLU D 1 188 ? 56.995  21.929  38.428  1.00 49.13  ? 184 GLU C O   1 
ATOM   7925  C CB  . GLU D 1 188 ? 56.697  18.796  38.789  1.00 62.30  ? 184 GLU C CB  1 
ATOM   7926  C CG  . GLU D 1 188 ? 55.858  17.620  39.286  1.00 68.71  ? 184 GLU C CG  1 
ATOM   7927  C CD  . GLU D 1 188 ? 55.162  17.892  40.610  1.00 77.41  ? 184 GLU C CD  1 
ATOM   7928  O OE1 . GLU D 1 188 ? 54.995  16.930  41.393  1.00 89.66  ? 184 GLU C OE1 1 
ATOM   7929  O OE2 . GLU D 1 188 ? 54.784  19.055  40.876  1.00 75.33  ? 184 GLU C OE2 1 
ATOM   7930  N N   . ALA D 1 189 ? 57.487  20.969  36.455  1.00 53.46  ? 185 ALA C N   1 
ATOM   7931  C CA  . ALA D 1 189 ? 58.349  22.069  36.005  1.00 51.93  ? 185 ALA C CA  1 
ATOM   7932  C C   . ALA D 1 189 ? 57.531  23.328  35.749  1.00 48.85  ? 185 ALA C C   1 
ATOM   7933  O O   . ALA D 1 189 ? 57.909  24.420  36.172  1.00 43.42  ? 185 ALA C O   1 
ATOM   7934  C CB  . ALA D 1 189 ? 59.130  21.677  34.758  1.00 51.00  ? 185 ALA C CB  1 
ATOM   7935  N N   . GLU D 1 190 ? 56.414  23.158  35.050  1.00 50.03  ? 186 GLU C N   1 
ATOM   7936  C CA  . GLU D 1 190 ? 55.469  24.244  34.791  1.00 50.21  ? 186 GLU C CA  1 
ATOM   7937  C C   . GLU D 1 190 ? 54.902  24.809  36.101  1.00 43.96  ? 186 GLU C C   1 
ATOM   7938  O O   . GLU D 1 190 ? 54.802  26.024  36.267  1.00 39.59  ? 186 GLU C O   1 
ATOM   7939  C CB  . GLU D 1 190 ? 54.342  23.722  33.899  1.00 55.39  ? 186 GLU C CB  1 
ATOM   7940  C CG  . GLU D 1 190 ? 53.409  24.785  33.333  1.00 62.79  ? 186 GLU C CG  1 
ATOM   7941  C CD  . GLU D 1 190 ? 52.411  24.209  32.340  1.00 74.99  ? 186 GLU C CD  1 
ATOM   7942  O OE1 . GLU D 1 190 ? 51.216  24.567  32.415  1.00 89.32  ? 186 GLU C OE1 1 
ATOM   7943  O OE2 . GLU D 1 190 ? 52.815  23.386  31.487  1.00 86.03  ? 186 GLU C OE2 1 
ATOM   7944  N N   . GLN D 1 191 ? 54.550  23.911  37.019  1.00 41.79  ? 187 GLN C N   1 
ATOM   7945  C CA  . GLN D 1 191 ? 54.006  24.266  38.336  1.00 43.23  ? 187 GLN C CA  1 
ATOM   7946  C C   . GLN D 1 191 ? 54.870  25.332  39.003  1.00 46.76  ? 187 GLN C C   1 
ATOM   7947  O O   . GLN D 1 191 ? 54.388  26.383  39.433  1.00 44.52  ? 187 GLN C O   1 
ATOM   7948  C CB  . GLN D 1 191 ? 53.933  23.006  39.224  1.00 44.51  ? 187 GLN C CB  1 
ATOM   7949  C CG  . GLN D 1 191 ? 53.400  23.154  40.661  1.00 48.71  ? 187 GLN C CG  1 
ATOM   7950  C CD  . GLN D 1 191 ? 52.270  24.139  40.842  1.00 46.20  ? 187 GLN C CD  1 
ATOM   7951  O OE1 . GLN D 1 191 ? 51.298  24.101  40.119  1.00 50.98  ? 187 GLN C OE1 1 
ATOM   7952  N NE2 . GLN D 1 191 ? 52.374  24.993  41.853  1.00 40.10  ? 187 GLN C NE2 1 
ATOM   7953  N N   . THR D 1 192 ? 56.166  25.059  39.030  1.00 49.58  ? 188 THR C N   1 
ATOM   7954  C CA  . THR D 1 192 ? 57.114  25.811  39.817  1.00 49.09  ? 188 THR C CA  1 
ATOM   7955  C C   . THR D 1 192 ? 57.625  27.039  39.038  1.00 47.83  ? 188 THR C C   1 
ATOM   7956  O O   . THR D 1 192 ? 57.956  28.066  39.630  1.00 52.12  ? 188 THR C O   1 
ATOM   7957  C CB  . THR D 1 192 ? 58.231  24.840  40.253  1.00 47.94  ? 188 THR C CB  1 
ATOM   7958  O OG1 . THR D 1 192 ? 58.496  24.974  41.651  1.00 58.35  ? 188 THR C OG1 1 
ATOM   7959  C CG2 . THR D 1 192 ? 59.473  25.044  39.449  1.00 46.38  ? 188 THR C CG2 1 
ATOM   7960  N N   . ARG D 1 193 ? 57.668  26.938  37.710  1.00 55.39  ? 189 ARG C N   1 
ATOM   7961  C CA  . ARG D 1 193 ? 57.945  28.091  36.843  1.00 53.28  ? 189 ARG C CA  1 
ATOM   7962  C C   . ARG D 1 193 ? 56.929  29.213  37.063  1.00 49.91  ? 189 ARG C C   1 
ATOM   7963  O O   . ARG D 1 193 ? 57.310  30.370  37.212  1.00 52.96  ? 189 ARG C O   1 
ATOM   7964  C CB  . ARG D 1 193 ? 57.983  27.650  35.368  1.00 55.76  ? 189 ARG C CB  1 
ATOM   7965  C CG  . ARG D 1 193 ? 58.647  28.587  34.355  1.00 59.39  ? 189 ARG C CG  1 
ATOM   7966  C CD  . ARG D 1 193 ? 58.061  28.471  32.944  1.00 61.54  ? 189 ARG C CD  1 
ATOM   7967  N NE  . ARG D 1 193 ? 57.503  27.154  32.619  1.00 66.35  ? 189 ARG C NE  1 
ATOM   7968  C CZ  . ARG D 1 193 ? 58.212  26.053  32.365  1.00 68.15  ? 189 ARG C CZ  1 
ATOM   7969  N NH1 . ARG D 1 193 ? 59.542  26.066  32.399  1.00 77.17  ? 189 ARG C NH1 1 
ATOM   7970  N NH2 . ARG D 1 193 ? 57.578  24.919  32.084  1.00 69.44  ? 189 ARG C NH2 1 
ATOM   7971  N N   . LEU D 1 194 ? 55.646  28.861  37.133  1.00 47.87  ? 190 LEU C N   1 
ATOM   7972  C CA  . LEU D 1 194 ? 54.578  29.854  37.245  1.00 49.91  ? 190 LEU C CA  1 
ATOM   7973  C C   . LEU D 1 194 ? 54.373  30.376  38.668  1.00 47.84  ? 190 LEU C C   1 
ATOM   7974  O O   . LEU D 1 194 ? 54.218  31.588  38.864  1.00 45.21  ? 190 LEU C O   1 
ATOM   7975  C CB  . LEU D 1 194 ? 53.260  29.280  36.720  1.00 54.20  ? 190 LEU C CB  1 
ATOM   7976  C CG  . LEU D 1 194 ? 53.231  28.890  35.240  1.00 59.23  ? 190 LEU C CG  1 
ATOM   7977  C CD1 . LEU D 1 194 ? 51.970  28.106  34.922  1.00 57.08  ? 190 LEU C CD1 1 
ATOM   7978  C CD2 . LEU D 1 194 ? 53.330  30.123  34.351  1.00 54.93  ? 190 LEU C CD2 1 
ATOM   7979  N N   . TYR D 1 195 ? 54.370  29.476  39.655  1.00 45.52  ? 191 TYR C N   1 
ATOM   7980  C CA  . TYR D 1 195 ? 54.021  29.855  41.033  1.00 46.09  ? 191 TYR C CA  1 
ATOM   7981  C C   . TYR D 1 195 ? 55.063  29.495  42.109  1.00 45.29  ? 191 TYR C C   1 
ATOM   7982  O O   . TYR D 1 195 ? 54.764  29.594  43.301  1.00 43.04  ? 191 TYR C O   1 
ATOM   7983  C CB  . TYR D 1 195 ? 52.669  29.241  41.409  1.00 42.46  ? 191 TYR C CB  1 
ATOM   7984  C CG  . TYR D 1 195 ? 51.693  29.145  40.257  1.00 37.29  ? 191 TYR C CG  1 
ATOM   7985  C CD1 . TYR D 1 195 ? 51.501  27.947  39.584  1.00 36.23  ? 191 TYR C CD1 1 
ATOM   7986  C CD2 . TYR D 1 195 ? 50.964  30.253  39.840  1.00 37.99  ? 191 TYR C CD2 1 
ATOM   7987  C CE1 . TYR D 1 195 ? 50.604  27.850  38.534  1.00 34.53  ? 191 TYR C CE1 1 
ATOM   7988  C CE2 . TYR D 1 195 ? 50.059  30.162  38.791  1.00 36.37  ? 191 TYR C CE2 1 
ATOM   7989  C CZ  . TYR D 1 195 ? 49.886  28.959  38.142  1.00 34.82  ? 191 TYR C CZ  1 
ATOM   7990  O OH  . TYR D 1 195 ? 48.991  28.869  37.098  1.00 36.90  ? 191 TYR C OH  1 
ATOM   7991  N N   . GLN D 1 196 ? 56.266  29.082  41.699  1.00 42.84  ? 192 GLN C N   1 
ATOM   7992  C CA  . GLN D 1 196 ? 57.368  28.741  42.624  1.00 47.65  ? 192 GLN C CA  1 
ATOM   7993  C C   . GLN D 1 196 ? 57.106  27.566  43.559  1.00 49.66  ? 192 GLN C C   1 
ATOM   7994  O O   . GLN D 1 196 ? 57.929  26.653  43.657  1.00 49.87  ? 192 GLN C O   1 
ATOM   7995  C CB  . GLN D 1 196 ? 57.788  29.953  43.469  1.00 52.55  ? 192 GLN C CB  1 
ATOM   7996  C CG  . GLN D 1 196 ? 59.091  30.594  43.031  1.00 54.93  ? 192 GLN C CG  1 
ATOM   7997  C CD  . GLN D 1 196 ? 60.296  29.718  43.282  1.00 58.45  ? 192 GLN C CD  1 
ATOM   7998  O OE1 . GLN D 1 196 ? 61.043  29.420  42.361  1.00 64.86  ? 192 GLN C OE1 1 
ATOM   7999  N NE2 . GLN D 1 196 ? 60.489  29.298  44.528  1.00 66.60  ? 192 GLN C NE2 1 
ATOM   8000  N N   . ASN D 1 197 ? 55.980  27.605  44.265  1.00 47.69  ? 193 ASN C N   1 
ATOM   8001  C CA  . ASN D 1 197 ? 55.657  26.594  45.265  1.00 42.76  ? 193 ASN C CA  1 
ATOM   8002  C C   . ASN D 1 197 ? 55.180  25.308  44.587  1.00 41.75  ? 193 ASN C C   1 
ATOM   8003  O O   . ASN D 1 197 ? 54.281  25.353  43.753  1.00 43.73  ? 193 ASN C O   1 
ATOM   8004  C CB  . ASN D 1 197 ? 54.580  27.130  46.212  1.00 45.42  ? 193 ASN C CB  1 
ATOM   8005  C CG  . ASN D 1 197 ? 54.893  28.541  46.717  1.00 43.16  ? 193 ASN C CG  1 
ATOM   8006  O OD1 . ASN D 1 197 ? 56.056  28.918  46.861  1.00 44.78  ? 193 ASN C OD1 1 
ATOM   8007  N ND2 . ASN D 1 197 ? 53.855  29.329  46.960  1.00 38.46  ? 193 ASN C ND2 1 
ATOM   8008  N N   . PRO D 1 198 ? 55.784  24.159  44.933  1.00 44.20  ? 194 PRO C N   1 
ATOM   8009  C CA  . PRO D 1 198 ? 55.423  22.885  44.302  1.00 40.87  ? 194 PRO C CA  1 
ATOM   8010  C C   . PRO D 1 198 ? 54.083  22.285  44.766  1.00 44.23  ? 194 PRO C C   1 
ATOM   8011  O O   . PRO D 1 198 ? 53.371  21.700  43.952  1.00 49.61  ? 194 PRO C O   1 
ATOM   8012  C CB  . PRO D 1 198 ? 56.581  21.966  44.697  1.00 40.67  ? 194 PRO C CB  1 
ATOM   8013  C CG  . PRO D 1 198 ? 57.058  22.509  45.997  1.00 44.74  ? 194 PRO C CG  1 
ATOM   8014  C CD  . PRO D 1 198 ? 56.866  23.996  45.922  1.00 47.37  ? 194 PRO C CD  1 
ATOM   8015  N N   . THR D 1 199 ? 53.763  22.403  46.054  1.00 41.06  ? 195 THR C N   1 
ATOM   8016  C CA  . THR D 1 199 ? 52.517  21.855  46.613  1.00 42.35  ? 195 THR C CA  1 
ATOM   8017  C C   . THR D 1 199 ? 51.570  22.985  46.995  1.00 42.28  ? 195 THR C C   1 
ATOM   8018  O O   . THR D 1 199 ? 51.909  23.830  47.826  1.00 39.05  ? 195 THR C O   1 
ATOM   8019  C CB  . THR D 1 199 ? 52.795  21.008  47.865  1.00 43.52  ? 195 THR C CB  1 
ATOM   8020  O OG1 . THR D 1 199 ? 53.677  19.936  47.516  1.00 52.20  ? 195 THR C OG1 1 
ATOM   8021  C CG2 . THR D 1 199 ? 51.501  20.441  48.444  1.00 37.76  ? 195 THR C CG2 1 
ATOM   8022  N N   . THR D 1 200 ? 50.377  22.984  46.408  1.00 39.58  ? 196 THR C N   1 
ATOM   8023  C CA  . THR D 1 200 ? 49.556  24.181  46.404  1.00 36.92  ? 196 THR C CA  1 
ATOM   8024  C C   . THR D 1 200 ? 48.062  23.922  46.578  1.00 35.30  ? 196 THR C C   1 
ATOM   8025  O O   . THR D 1 200 ? 47.601  22.793  46.441  1.00 38.26  ? 196 THR C O   1 
ATOM   8026  C CB  . THR D 1 200 ? 49.813  24.943  45.091  1.00 37.66  ? 196 THR C CB  1 
ATOM   8027  O OG1 . THR D 1 200 ? 49.738  26.342  45.329  1.00 53.32  ? 196 THR C OG1 1 
ATOM   8028  C CG2 . THR D 1 200 ? 48.805  24.580  44.027  1.00 34.82  ? 196 THR C CG2 1 
ATOM   8029  N N   . TYR D 1 201 ? 47.317  24.986  46.875  1.00 35.05  ? 197 TYR C N   1 
ATOM   8030  C CA  . TYR D 1 201 ? 45.881  24.885  47.156  1.00 34.91  ? 197 TYR C CA  1 
ATOM   8031  C C   . TYR D 1 201 ? 45.163  26.233  47.013  1.00 32.83  ? 197 TYR C C   1 
ATOM   8032  O O   . TYR D 1 201 ? 45.802  27.281  46.974  1.00 30.71  ? 197 TYR C O   1 
ATOM   8033  C CB  . TYR D 1 201 ? 45.653  24.355  48.581  1.00 34.51  ? 197 TYR C CB  1 
ATOM   8034  C CG  . TYR D 1 201 ? 46.022  25.350  49.656  1.00 36.05  ? 197 TYR C CG  1 
ATOM   8035  C CD1 . TYR D 1 201 ? 45.073  26.228  50.172  1.00 40.32  ? 197 TYR C CD1 1 
ATOM   8036  C CD2 . TYR D 1 201 ? 47.328  25.431  50.145  1.00 38.10  ? 197 TYR C CD2 1 
ATOM   8037  C CE1 . TYR D 1 201 ? 45.411  27.157  51.143  1.00 45.09  ? 197 TYR C CE1 1 
ATOM   8038  C CE2 . TYR D 1 201 ? 47.676  26.354  51.116  1.00 39.06  ? 197 TYR C CE2 1 
ATOM   8039  C CZ  . TYR D 1 201 ? 46.716  27.215  51.612  1.00 45.55  ? 197 TYR C CZ  1 
ATOM   8040  O OH  . TYR D 1 201 ? 47.050  28.132  52.584  1.00 48.97  ? 197 TYR C OH  1 
ATOM   8041  N N   . ILE D 1 202 ? 43.833  26.185  46.925  1.00 32.07  ? 198 ILE C N   1 
ATOM   8042  C CA  . ILE D 1 202 ? 42.990  27.373  47.060  1.00 32.23  ? 198 ILE C CA  1 
ATOM   8043  C C   . ILE D 1 202 ? 41.816  27.034  47.962  1.00 33.58  ? 198 ILE C C   1 
ATOM   8044  O O   . ILE D 1 202 ? 41.108  26.068  47.698  1.00 35.00  ? 198 ILE C O   1 
ATOM   8045  C CB  . ILE D 1 202 ? 42.383  27.841  45.726  1.00 30.73  ? 198 ILE C CB  1 
ATOM   8046  C CG1 . ILE D 1 202 ? 43.426  27.884  44.612  1.00 32.13  ? 198 ILE C CG1 1 
ATOM   8047  C CG2 . ILE D 1 202 ? 41.761  29.218  45.899  1.00 28.61  ? 198 ILE C CG2 1 
ATOM   8048  C CD1 . ILE D 1 202 ? 42.820  28.018  43.232  1.00 30.01  ? 198 ILE C CD1 1 
ATOM   8049  N N   . SER D 1 203 ? 41.607  27.809  49.023  1.00 37.42  ? 199 SER C N   1 
ATOM   8050  C CA  . SER D 1 203 ? 40.403  27.653  49.840  1.00 39.15  ? 199 SER C CA  1 
ATOM   8051  C C   . SER D 1 203 ? 39.517  28.876  49.681  1.00 38.31  ? 199 SER C C   1 
ATOM   8052  O O   . SER D 1 203 ? 40.010  29.992  49.571  1.00 39.88  ? 199 SER C O   1 
ATOM   8053  C CB  . SER D 1 203 ? 40.740  27.397  51.313  1.00 38.28  ? 199 SER C CB  1 
ATOM   8054  O OG  . SER D 1 203 ? 41.559  28.414  51.844  1.00 42.36  ? 199 SER C OG  1 
ATOM   8055  N N   . ILE D 1 204 ? 38.207  28.647  49.635  1.00 40.16  ? 200 ILE C N   1 
ATOM   8056  C CA  . ILE D 1 204 ? 37.222  29.714  49.458  1.00 36.12  ? 200 ILE C CA  1 
ATOM   8057  C C   . ILE D 1 204 ? 36.140  29.562  50.519  1.00 35.53  ? 200 ILE C C   1 
ATOM   8058  O O   . ILE D 1 204 ? 35.588  28.480  50.694  1.00 38.16  ? 200 ILE C O   1 
ATOM   8059  C CB  . ILE D 1 204 ? 36.563  29.673  48.064  1.00 35.82  ? 200 ILE C CB  1 
ATOM   8060  C CG1 . ILE D 1 204 ? 37.610  29.450  46.969  1.00 36.02  ? 200 ILE C CG1 1 
ATOM   8061  C CG2 . ILE D 1 204 ? 35.802  30.964  47.795  1.00 33.50  ? 200 ILE C CG2 1 
ATOM   8062  C CD1 . ILE D 1 204 ? 37.962  27.998  46.739  1.00 36.59  ? 200 ILE C CD1 1 
ATOM   8063  N N   . GLY D 1 205 ? 35.855  30.648  51.227  1.00 37.80  ? 201 GLY C N   1 
ATOM   8064  C CA  . GLY D 1 205 ? 34.915  30.633  52.344  1.00 39.10  ? 201 GLY C CA  1 
ATOM   8065  C C   . GLY D 1 205 ? 33.781  31.628  52.169  1.00 39.68  ? 201 GLY C C   1 
ATOM   8066  O O   . GLY D 1 205 ? 33.966  32.678  51.565  1.00 44.00  ? 201 GLY C O   1 
ATOM   8067  N N   . THR D 1 206 ? 32.606  31.280  52.692  1.00 42.33  ? 202 THR C N   1 
ATOM   8068  C CA  . THR D 1 206 ? 31.444  32.175  52.781  1.00 47.78  ? 202 THR C CA  1 
ATOM   8069  C C   . THR D 1 206 ? 30.649  31.699  53.988  1.00 49.15  ? 202 THR C C   1 
ATOM   8070  O O   . THR D 1 206 ? 31.084  30.801  54.713  1.00 53.02  ? 202 THR C O   1 
ATOM   8071  C CB  . THR D 1 206 ? 30.514  32.183  51.532  1.00 45.64  ? 202 THR C CB  1 
ATOM   8072  O OG1 . THR D 1 206 ? 29.698  31.004  51.496  1.00 49.00  ? 202 THR C OG1 1 
ATOM   8073  C CG2 . THR D 1 206 ? 31.301  32.318  50.232  1.00 40.19  ? 202 THR C CG2 1 
ATOM   8074  N N   . SER D 1 207 ? 29.474  32.274  54.193  1.00 51.75  ? 203 SER C N   1 
ATOM   8075  C CA  . SER D 1 207 ? 28.585  31.784  55.246  1.00 48.80  ? 203 SER C CA  1 
ATOM   8076  C C   . SER D 1 207 ? 28.139  30.332  54.989  1.00 48.79  ? 203 SER C C   1 
ATOM   8077  O O   . SER D 1 207 ? 27.826  29.584  55.924  1.00 55.86  ? 203 SER C O   1 
ATOM   8078  C CB  . SER D 1 207 ? 27.366  32.695  55.376  1.00 48.21  ? 203 SER C CB  1 
ATOM   8079  O OG  . SER D 1 207 ? 26.540  32.635  54.229  1.00 45.82  ? 203 SER C OG  1 
ATOM   8080  N N   . THR D 1 208 ? 28.161  29.932  53.719  1.00 48.96  ? 204 THR C N   1 
ATOM   8081  C CA  . THR D 1 208 ? 27.619  28.645  53.274  1.00 50.80  ? 204 THR C CA  1 
ATOM   8082  C C   . THR D 1 208 ? 28.618  27.801  52.461  1.00 49.23  ? 204 THR C C   1 
ATOM   8083  O O   . THR D 1 208 ? 28.454  26.589  52.385  1.00 58.60  ? 204 THR C O   1 
ATOM   8084  C CB  . THR D 1 208 ? 26.314  28.822  52.456  1.00 48.91  ? 204 THR C CB  1 
ATOM   8085  O OG1 . THR D 1 208 ? 26.572  29.586  51.268  1.00 43.07  ? 204 THR C OG1 1 
ATOM   8086  C CG2 . THR D 1 208 ? 25.242  29.515  53.290  1.00 46.30  ? 204 THR C CG2 1 
ATOM   8087  N N   . LEU D 1 209 ? 29.634  28.428  51.858  1.00 43.27  ? 205 LEU C N   1 
ATOM   8088  C CA  . LEU D 1 209 ? 30.632  27.714  51.043  1.00 40.23  ? 205 LEU C CA  1 
ATOM   8089  C C   . LEU D 1 209 ? 31.877  27.390  51.860  1.00 39.58  ? 205 LEU C C   1 
ATOM   8090  O O   . LEU D 1 209 ? 32.359  28.226  52.620  1.00 42.29  ? 205 LEU C O   1 
ATOM   8091  C CB  . LEU D 1 209 ? 31.027  28.554  49.823  1.00 37.85  ? 205 LEU C CB  1 
ATOM   8092  C CG  . LEU D 1 209 ? 31.965  27.939  48.770  1.00 38.26  ? 205 LEU C CG  1 
ATOM   8093  C CD1 . LEU D 1 209 ? 31.313  26.814  47.971  1.00 28.64  ? 205 LEU C CD1 1 
ATOM   8094  C CD2 . LEU D 1 209 ? 32.482  29.024  47.828  1.00 32.24  ? 205 LEU C CD2 1 
ATOM   8095  N N   . ASN D 1 210 ? 32.386  26.172  51.694  1.00 40.09  ? 206 ASN C N   1 
ATOM   8096  C CA  . ASN D 1 210 ? 33.600  25.717  52.374  1.00 38.16  ? 206 ASN C CA  1 
ATOM   8097  C C   . ASN D 1 210 ? 34.371  24.784  51.442  1.00 38.21  ? 206 ASN C C   1 
ATOM   8098  O O   . ASN D 1 210 ? 34.234  23.566  51.511  1.00 37.15  ? 206 ASN C O   1 
ATOM   8099  C CB  . ASN D 1 210 ? 33.242  25.007  53.683  1.00 36.93  ? 206 ASN C CB  1 
ATOM   8100  C CG  . ASN D 1 210 ? 34.459  24.455  54.412  1.00 40.11  ? 206 ASN C CG  1 
ATOM   8101  O OD1 . ASN D 1 210 ? 35.565  24.989  54.303  1.00 40.76  ? 206 ASN C OD1 1 
ATOM   8102  N ND2 . ASN D 1 210 ? 34.255  23.384  55.169  1.00 39.22  ? 206 ASN C ND2 1 
ATOM   8103  N N   . GLN D 1 211 ? 35.180  25.370  50.568  1.00 35.94  ? 207 GLN C N   1 
ATOM   8104  C CA  . GLN D 1 211 ? 35.794  24.638  49.471  1.00 35.95  ? 207 GLN C CA  1 
ATOM   8105  C C   . GLN D 1 211 ? 37.313  24.707  49.528  1.00 35.78  ? 207 GLN C C   1 
ATOM   8106  O O   . GLN D 1 211 ? 37.867  25.746  49.845  1.00 38.30  ? 207 GLN C O   1 
ATOM   8107  C CB  . GLN D 1 211 ? 35.276  25.214  48.155  1.00 36.52  ? 207 GLN C CB  1 
ATOM   8108  C CG  . GLN D 1 211 ? 35.801  24.558  46.893  1.00 39.06  ? 207 GLN C CG  1 
ATOM   8109  C CD  . GLN D 1 211 ? 34.970  24.900  45.670  1.00 44.94  ? 207 GLN C CD  1 
ATOM   8110  O OE1 . GLN D 1 211 ? 34.590  26.047  45.474  1.00 44.88  ? 207 GLN C OE1 1 
ATOM   8111  N NE2 . GLN D 1 211 ? 34.691  23.901  44.836  1.00 48.60  ? 207 GLN C NE2 1 
ATOM   8112  N N   . ARG D 1 212 ? 37.975  23.594  49.225  1.00 39.21  ? 208 ARG C N   1 
ATOM   8113  C CA  . ARG D 1 212 ? 39.426  23.565  49.070  1.00 36.35  ? 208 ARG C CA  1 
ATOM   8114  C C   . ARG D 1 212 ? 39.766  22.878  47.750  1.00 36.08  ? 208 ARG C C   1 
ATOM   8115  O O   . ARG D 1 212 ? 39.400  21.727  47.530  1.00 35.39  ? 208 ARG C O   1 
ATOM   8116  C CB  . ARG D 1 212 ? 40.091  22.839  50.231  1.00 37.69  ? 208 ARG C CB  1 
ATOM   8117  C CG  . ARG D 1 212 ? 41.595  23.059  50.306  1.00 39.63  ? 208 ARG C CG  1 
ATOM   8118  C CD  . ARG D 1 212 ? 42.213  22.317  51.478  1.00 45.18  ? 208 ARG C CD  1 
ATOM   8119  N NE  . ARG D 1 212 ? 43.664  22.500  51.555  1.00 46.68  ? 208 ARG C NE  1 
ATOM   8120  C CZ  . ARG D 1 212 ? 44.287  23.464  52.238  1.00 53.00  ? 208 ARG C CZ  1 
ATOM   8121  N NH1 . ARG D 1 212 ? 43.609  24.377  52.932  1.00 49.21  ? 208 ARG C NH1 1 
ATOM   8122  N NH2 . ARG D 1 212 ? 45.617  23.514  52.230  1.00 58.51  ? 208 ARG C NH2 1 
ATOM   8123  N N   . LEU D 1 213 ? 40.460  23.601  46.876  1.00 38.78  ? 209 LEU C N   1 
ATOM   8124  C CA  . LEU D 1 213 ? 40.816  23.114  45.548  1.00 39.92  ? 209 LEU C CA  1 
ATOM   8125  C C   . LEU D 1 213 ? 42.317  22.866  45.472  1.00 35.73  ? 209 LEU C C   1 
ATOM   8126  O O   . LEU D 1 213 ? 43.105  23.668  45.964  1.00 36.17  ? 209 LEU C O   1 
ATOM   8127  C CB  . LEU D 1 213 ? 40.416  24.144  44.492  1.00 40.93  ? 209 LEU C CB  1 
ATOM   8128  C CG  . LEU D 1 213 ? 38.926  24.462  44.421  1.00 38.21  ? 209 LEU C CG  1 
ATOM   8129  C CD1 . LEU D 1 213 ? 38.697  25.688  43.565  1.00 35.95  ? 209 LEU C CD1 1 
ATOM   8130  C CD2 . LEU D 1 213 ? 38.137  23.275  43.888  1.00 35.33  ? 209 LEU C CD2 1 
ATOM   8131  N N   . VAL D 1 214 ? 42.698  21.747  44.864  1.00 32.99  ? 210 VAL C N   1 
ATOM   8132  C CA  . VAL D 1 214 ? 44.099  21.371  44.709  1.00 33.37  ? 210 VAL C CA  1 
ATOM   8133  C C   . VAL D 1 214 ? 44.344  21.050  43.242  1.00 32.27  ? 210 VAL C C   1 
ATOM   8134  O O   . VAL D 1 214 ? 43.545  20.350  42.633  1.00 34.29  ? 210 VAL C O   1 
ATOM   8135  C CB  . VAL D 1 214 ? 44.443  20.142  45.576  1.00 36.53  ? 210 VAL C CB  1 
ATOM   8136  C CG1 . VAL D 1 214 ? 45.854  19.645  45.284  1.00 38.94  ? 210 VAL C CG1 1 
ATOM   8137  C CG2 . VAL D 1 214 ? 44.299  20.495  47.049  1.00 32.31  ? 210 VAL C CG2 1 
ATOM   8138  N N   . PRO D 1 215 ? 45.440  21.565  42.666  1.00 34.34  ? 211 PRO C N   1 
ATOM   8139  C CA  . PRO D 1 215 ? 45.681  21.299  41.245  1.00 37.87  ? 211 PRO C CA  1 
ATOM   8140  C C   . PRO D 1 215 ? 45.982  19.838  40.939  1.00 40.24  ? 211 PRO C C   1 
ATOM   8141  O O   . PRO D 1 215 ? 46.572  19.132  41.757  1.00 44.77  ? 211 PRO C O   1 
ATOM   8142  C CB  . PRO D 1 215 ? 46.902  22.157  40.897  1.00 40.03  ? 211 PRO C CB  1 
ATOM   8143  C CG  . PRO D 1 215 ? 47.236  22.951  42.094  1.00 41.15  ? 211 PRO C CG  1 
ATOM   8144  C CD  . PRO D 1 215 ? 46.419  22.492  43.258  1.00 40.84  ? 211 PRO C CD  1 
ATOM   8145  N N   . LYS D 1 216 ? 45.579  19.408  39.750  1.00 40.36  ? 212 LYS C N   1 
ATOM   8146  C CA  . LYS D 1 216 ? 45.789  18.050  39.284  1.00 45.53  ? 212 LYS C CA  1 
ATOM   8147  C C   . LYS D 1 216 ? 46.795  18.100  38.141  1.00 50.20  ? 212 LYS C C   1 
ATOM   8148  O O   . LYS D 1 216 ? 46.480  18.575  37.060  1.00 52.61  ? 212 LYS C O   1 
ATOM   8149  C CB  . LYS D 1 216 ? 44.460  17.450  38.826  1.00 47.09  ? 212 LYS C CB  1 
ATOM   8150  C CG  . LYS D 1 216 ? 43.443  17.317  39.953  1.00 52.14  ? 212 LYS C CG  1 
ATOM   8151  C CD  . LYS D 1 216 ? 42.189  16.564  39.531  1.00 53.85  ? 212 LYS C CD  1 
ATOM   8152  C CE  . LYS D 1 216 ? 41.220  17.449  38.761  1.00 55.17  ? 212 LYS C CE  1 
ATOM   8153  N NZ  . LYS D 1 216 ? 40.592  18.497  39.606  1.00 63.49  ? 212 LYS C NZ  1 
ATOM   8154  N N   . ILE D 1 217 ? 48.013  17.630  38.400  1.00 60.42  ? 213 ILE C N   1 
ATOM   8155  C CA  . ILE D 1 217 ? 49.110  17.702  37.434  1.00 63.40  ? 213 ILE C CA  1 
ATOM   8156  C C   . ILE D 1 217 ? 49.191  16.396  36.643  1.00 67.47  ? 213 ILE C C   1 
ATOM   8157  O O   . ILE D 1 217 ? 49.520  15.348  37.199  1.00 71.23  ? 213 ILE C O   1 
ATOM   8158  C CB  . ILE D 1 217 ? 50.450  17.974  38.150  1.00 63.27  ? 213 ILE C CB  1 
ATOM   8159  C CG1 . ILE D 1 217 ? 50.414  19.325  38.874  1.00 65.03  ? 213 ILE C CG1 1 
ATOM   8160  C CG2 . ILE D 1 217 ? 51.600  17.968  37.157  1.00 64.61  ? 213 ILE C CG2 1 
ATOM   8161  C CD1 . ILE D 1 217 ? 51.246  19.365  40.138  1.00 69.34  ? 213 ILE C CD1 1 
ATOM   8162  N N   . ALA D 1 218 ? 48.882  16.462  35.350  1.00 71.61  ? 214 ALA C N   1 
ATOM   8163  C CA  . ALA D 1 218 ? 48.824  15.264  34.512  1.00 74.11  ? 214 ALA C CA  1 
ATOM   8164  C C   . ALA D 1 218 ? 49.062  15.575  33.038  1.00 82.16  ? 214 ALA C C   1 
ATOM   8165  O O   . ALA D 1 218 ? 49.028  16.734  32.617  1.00 71.61  ? 214 ALA C O   1 
ATOM   8166  C CB  . ALA D 1 218 ? 47.481  14.574  34.689  1.00 61.50  ? 214 ALA C CB  1 
ATOM   8167  N N   . THR D 1 219 ? 49.300  14.518  32.264  1.00 95.98  ? 215 THR C N   1 
ATOM   8168  C CA  . THR D 1 219 ? 49.508  14.626  30.823  1.00 89.51  ? 215 THR C CA  1 
ATOM   8169  C C   . THR D 1 219 ? 48.159  14.646  30.118  1.00 78.48  ? 215 THR C C   1 
ATOM   8170  O O   . THR D 1 219 ? 47.319  13.776  30.353  1.00 73.57  ? 215 THR C O   1 
ATOM   8171  C CB  . THR D 1 219 ? 50.333  13.445  30.280  1.00 92.73  ? 215 THR C CB  1 
ATOM   8172  O OG1 . THR D 1 219 ? 51.514  13.277  31.074  1.00 105.17 ? 215 THR C OG1 1 
ATOM   8173  C CG2 . THR D 1 219 ? 50.731  13.691  28.828  1.00 89.99  ? 215 THR C CG2 1 
ATOM   8174  N N   . ARG D 1 220 ? 47.957  15.645  29.260  1.00 74.02  ? 216 ARG C N   1 
ATOM   8175  C CA  . ARG D 1 220 ? 46.688  15.828  28.559  1.00 71.91  ? 216 ARG C CA  1 
ATOM   8176  C C   . ARG D 1 220 ? 46.898  16.142  27.090  1.00 68.51  ? 216 ARG C C   1 
ATOM   8177  O O   . ARG D 1 220 ? 47.939  16.667  26.697  1.00 67.49  ? 216 ARG C O   1 
ATOM   8178  C CB  . ARG D 1 220 ? 45.896  16.964  29.200  1.00 72.21  ? 216 ARG C CB  1 
ATOM   8179  C CG  . ARG D 1 220 ? 45.385  16.633  30.586  1.00 68.71  ? 216 ARG C CG  1 
ATOM   8180  C CD  . ARG D 1 220 ? 44.751  17.834  31.257  1.00 66.43  ? 216 ARG C CD  1 
ATOM   8181  N NE  . ARG D 1 220 ? 45.076  17.842  32.677  1.00 65.46  ? 216 ARG C NE  1 
ATOM   8182  C CZ  . ARG D 1 220 ? 45.983  18.628  33.256  1.00 62.59  ? 216 ARG C CZ  1 
ATOM   8183  N NH1 . ARG D 1 220 ? 46.691  19.516  32.562  1.00 56.84  ? 216 ARG C NH1 1 
ATOM   8184  N NH2 . ARG D 1 220 ? 46.176  18.521  34.561  1.00 66.01  ? 216 ARG C NH2 1 
ATOM   8185  N N   . SER D 1 221 ? 45.890  15.819  26.286  1.00 68.51  ? 217 SER C N   1 
ATOM   8186  C CA  . SER D 1 221 ? 45.892  16.153  24.871  1.00 67.83  ? 217 SER C CA  1 
ATOM   8187  C C   . SER D 1 221 ? 45.758  17.662  24.724  1.00 69.20  ? 217 SER C C   1 
ATOM   8188  O O   . SER D 1 221 ? 45.041  18.307  25.493  1.00 66.05  ? 217 SER C O   1 
ATOM   8189  C CB  . SER D 1 221 ? 44.735  15.453  24.157  1.00 73.86  ? 217 SER C CB  1 
ATOM   8190  O OG  . SER D 1 221 ? 44.782  14.049  24.361  1.00 77.74  ? 217 SER C OG  1 
ATOM   8191  N N   . LYS D 1 222 ? 46.459  18.224  23.744  1.00 66.66  ? 218 LYS C N   1 
ATOM   8192  C CA  . LYS D 1 222 ? 46.402  19.663  23.497  1.00 63.74  ? 218 LYS C CA  1 
ATOM   8193  C C   . LYS D 1 222 ? 45.046  20.057  22.927  1.00 62.53  ? 218 LYS C C   1 
ATOM   8194  O O   . LYS D 1 222 ? 44.438  19.305  22.168  1.00 69.56  ? 218 LYS C O   1 
ATOM   8195  C CB  . LYS D 1 222 ? 47.528  20.111  22.555  1.00 65.93  ? 218 LYS C CB  1 
ATOM   8196  C CG  . LYS D 1 222 ? 48.795  20.525  23.282  1.00 61.24  ? 218 LYS C CG  1 
ATOM   8197  C CD  . LYS D 1 222 ? 49.939  20.799  22.323  1.00 63.55  ? 218 LYS C CD  1 
ATOM   8198  C CE  . LYS D 1 222 ? 51.148  21.388  23.021  1.00 65.34  ? 218 LYS C CE  1 
ATOM   8199  N NZ  . LYS D 1 222 ? 51.500  20.682  24.290  1.00 55.27  ? 218 LYS C NZ  1 
ATOM   8200  N N   . ILE D 1 223 ? 44.573  21.235  23.318  1.00 59.96  ? 219 ILE C N   1 
ATOM   8201  C CA  . ILE D 1 223 ? 43.349  21.811  22.766  1.00 57.92  ? 219 ILE C CA  1 
ATOM   8202  C C   . ILE D 1 223 ? 43.523  23.326  22.765  1.00 58.62  ? 219 ILE C C   1 
ATOM   8203  O O   . ILE D 1 223 ? 43.768  23.928  23.812  1.00 53.21  ? 219 ILE C O   1 
ATOM   8204  C CB  . ILE D 1 223 ? 42.090  21.357  23.550  1.00 63.43  ? 219 ILE C CB  1 
ATOM   8205  C CG1 . ILE D 1 223 ? 40.891  22.262  23.244  1.00 66.66  ? 219 ILE C CG1 1 
ATOM   8206  C CG2 . ILE D 1 223 ? 42.354  21.333  25.049  1.00 56.85  ? 219 ILE C CG2 1 
ATOM   8207  C CD1 . ILE D 1 223 ? 39.568  21.707  23.730  1.00 69.10  ? 219 ILE C CD1 1 
ATOM   8208  N N   . ASN D 1 224 ? 43.404  23.926  21.579  1.00 61.65  ? 220 ASN C N   1 
ATOM   8209  C CA  . ASN D 1 224 ? 43.844  25.304  21.330  1.00 60.64  ? 220 ASN C CA  1 
ATOM   8210  C C   . ASN D 1 224 ? 45.330  25.485  21.661  1.00 59.95  ? 220 ASN C C   1 
ATOM   8211  O O   . ASN D 1 224 ? 45.756  26.544  22.128  1.00 62.70  ? 220 ASN C O   1 
ATOM   8212  C CB  . ASN D 1 224 ? 42.970  26.319  22.081  1.00 67.43  ? 220 ASN C CB  1 
ATOM   8213  C CG  . ASN D 1 224 ? 41.548  26.375  21.529  1.00 68.55  ? 220 ASN C CG  1 
ATOM   8214  O OD1 . ASN D 1 224 ? 41.081  27.425  21.071  1.00 70.56  ? 220 ASN C OD1 1 
ATOM   8215  N ND2 . ASN D 1 224 ? 40.867  25.236  21.535  1.00 65.59  ? 220 ASN C ND2 1 
ATOM   8216  N N   . GLY D 1 225 ? 46.107  24.434  21.409  1.00 60.62  ? 221 GLY C N   1 
ATOM   8217  C CA  . GLY D 1 225 ? 47.544  24.438  21.667  1.00 66.86  ? 221 GLY C CA  1 
ATOM   8218  C C   . GLY D 1 225 ? 47.941  24.395  23.133  1.00 71.66  ? 221 GLY C C   1 
ATOM   8219  O O   . GLY D 1 225 ? 49.093  24.680  23.464  1.00 84.80  ? 221 GLY C O   1 
ATOM   8220  N N   . GLN D 1 226 ? 47.005  24.029  24.011  1.00 63.10  ? 222 GLN C N   1 
ATOM   8221  C CA  . GLN D 1 226 ? 47.260  24.002  25.453  1.00 57.60  ? 222 GLN C CA  1 
ATOM   8222  C C   . GLN D 1 226 ? 46.902  22.649  26.055  1.00 60.07  ? 222 GLN C C   1 
ATOM   8223  O O   . GLN D 1 226 ? 45.800  22.141  25.839  1.00 57.93  ? 222 GLN C O   1 
ATOM   8224  C CB  . GLN D 1 226 ? 46.454  25.092  26.160  1.00 63.51  ? 222 GLN C CB  1 
ATOM   8225  C CG  . GLN D 1 226 ? 46.700  26.500  25.639  1.00 70.23  ? 222 GLN C CG  1 
ATOM   8226  C CD  . GLN D 1 226 ? 48.142  26.943  25.804  1.00 72.83  ? 222 GLN C CD  1 
ATOM   8227  O OE1 . GLN D 1 226 ? 48.774  26.673  26.827  1.00 73.91  ? 222 GLN C OE1 1 
ATOM   8228  N NE2 . GLN D 1 226 ? 48.670  27.627  24.795  1.00 73.68  ? 222 GLN C NE2 1 
ATOM   8229  N N   . SER D 1 227 ? 47.841  22.073  26.804  1.00 62.43  ? 223 SER C N   1 
ATOM   8230  C CA  . SER D 1 227 ? 47.586  20.860  27.581  1.00 63.88  ? 223 SER C CA  1 
ATOM   8231  C C   . SER D 1 227 ? 47.193  21.199  29.016  1.00 65.98  ? 223 SER C C   1 
ATOM   8232  O O   . SER D 1 227 ? 46.667  20.347  29.732  1.00 71.54  ? 223 SER C O   1 
ATOM   8233  C CB  . SER D 1 227 ? 48.801  19.933  27.573  1.00 65.06  ? 223 SER C CB  1 
ATOM   8234  O OG  . SER D 1 227 ? 48.806  19.137  26.402  1.00 70.06  ? 223 SER C OG  1 
ATOM   8235  N N   . GLY D 1 228 ? 47.449  22.439  29.430  1.00 57.54  ? 224 GLY C N   1 
ATOM   8236  C CA  . GLY D 1 228 ? 46.969  22.932  30.713  1.00 55.52  ? 224 GLY C CA  1 
ATOM   8237  C C   . GLY D 1 228 ? 45.464  23.127  30.677  1.00 51.40  ? 224 GLY C C   1 
ATOM   8238  O O   . GLY D 1 228 ? 44.867  23.196  29.604  1.00 45.03  ? 224 GLY C O   1 
ATOM   8239  N N   . ARG D 1 229 ? 44.850  23.193  31.857  1.00 46.89  ? 225 ARG C N   1 
ATOM   8240  C CA  . ARG D 1 229 ? 43.409  23.402  31.978  1.00 43.46  ? 225 ARG C CA  1 
ATOM   8241  C C   . ARG D 1 229 ? 43.127  24.410  33.074  1.00 42.36  ? 225 ARG C C   1 
ATOM   8242  O O   . ARG D 1 229 ? 43.925  24.571  33.991  1.00 42.03  ? 225 ARG C O   1 
ATOM   8243  C CB  . ARG D 1 229 ? 42.703  22.095  32.322  1.00 40.72  ? 225 ARG C CB  1 
ATOM   8244  C CG  . ARG D 1 229 ? 42.831  21.004  31.272  1.00 40.02  ? 225 ARG C CG  1 
ATOM   8245  C CD  . ARG D 1 229 ? 41.934  21.266  30.077  1.00 44.18  ? 225 ARG C CD  1 
ATOM   8246  N NE  . ARG D 1 229 ? 42.021  20.177  29.110  1.00 45.93  ? 225 ARG C NE  1 
ATOM   8247  C CZ  . ARG D 1 229 ? 42.957  20.060  28.169  1.00 44.48  ? 225 ARG C CZ  1 
ATOM   8248  N NH1 . ARG D 1 229 ? 43.916  20.974  28.033  1.00 43.80  ? 225 ARG C NH1 1 
ATOM   8249  N NH2 . ARG D 1 229 ? 42.933  19.015  27.350  1.00 48.24  ? 225 ARG C NH2 1 
ATOM   8250  N N   . ILE D 1 230 ? 41.994  25.095  32.968  1.00 42.36  ? 226 ILE C N   1 
ATOM   8251  C CA  . ILE D 1 230 ? 41.528  25.965  34.036  1.00 44.46  ? 226 ILE C CA  1 
ATOM   8252  C C   . ILE D 1 230 ? 40.065  25.664  34.331  1.00 46.63  ? 226 ILE C C   1 
ATOM   8253  O O   . ILE D 1 230 ? 39.215  25.770  33.447  1.00 41.74  ? 226 ILE C O   1 
ATOM   8254  C CB  . ILE D 1 230 ? 41.692  27.451  33.686  1.00 46.29  ? 226 ILE C CB  1 
ATOM   8255  C CG1 . ILE D 1 230 ? 43.175  27.809  33.567  1.00 48.64  ? 226 ILE C CG1 1 
ATOM   8256  C CG2 . ILE D 1 230 ? 41.053  28.314  34.761  1.00 46.22  ? 226 ILE C CG2 1 
ATOM   8257  C CD1 . ILE D 1 230 ? 43.438  29.195  33.023  1.00 56.44  ? 226 ILE C CD1 1 
ATOM   8258  N N   . ASP D 1 231 ? 39.786  25.272  35.573  1.00 46.74  ? 227 ASP C N   1 
ATOM   8259  C CA  . ASP D 1 231 ? 38.420  24.997  36.018  1.00 42.34  ? 227 ASP C CA  1 
ATOM   8260  C C   . ASP D 1 231 ? 37.874  26.211  36.753  1.00 37.37  ? 227 ASP C C   1 
ATOM   8261  O O   . ASP D 1 231 ? 38.570  26.802  37.570  1.00 37.37  ? 227 ASP C O   1 
ATOM   8262  C CB  . ASP D 1 231 ? 38.385  23.777  36.940  1.00 45.43  ? 227 ASP C CB  1 
ATOM   8263  C CG  . ASP D 1 231 ? 38.723  22.479  36.219  1.00 49.40  ? 227 ASP C CG  1 
ATOM   8264  O OD1 . ASP D 1 231 ? 38.835  22.483  34.976  1.00 50.64  ? 227 ASP C OD1 1 
ATOM   8265  O OD2 . ASP D 1 231 ? 38.872  21.445  36.907  1.00 55.18  ? 227 ASP C OD2 1 
ATOM   8266  N N   . PHE D 1 232 ? 36.629  26.578  36.461  1.00 36.41  ? 228 PHE C N   1 
ATOM   8267  C CA  . PHE D 1 232 ? 36.000  27.743  37.075  1.00 33.80  ? 228 PHE C CA  1 
ATOM   8268  C C   . PHE D 1 232 ? 34.877  27.337  38.011  1.00 34.82  ? 228 PHE C C   1 
ATOM   8269  O O   . PHE D 1 232 ? 34.187  26.342  37.780  1.00 37.15  ? 228 PHE C O   1 
ATOM   8270  C CB  . PHE D 1 232 ? 35.454  28.679  36.005  1.00 35.81  ? 228 PHE C CB  1 
ATOM   8271  C CG  . PHE D 1 232 ? 36.517  29.437  35.272  1.00 40.81  ? 228 PHE C CG  1 
ATOM   8272  C CD1 . PHE D 1 232 ? 36.950  29.023  34.017  1.00 44.66  ? 228 PHE C CD1 1 
ATOM   8273  C CD2 . PHE D 1 232 ? 37.090  30.560  35.836  1.00 43.24  ? 228 PHE C CD2 1 
ATOM   8274  C CE1 . PHE D 1 232 ? 37.932  29.722  33.339  1.00 48.50  ? 228 PHE C CE1 1 
ATOM   8275  C CE2 . PHE D 1 232 ? 38.069  31.264  35.163  1.00 44.12  ? 228 PHE C CE2 1 
ATOM   8276  C CZ  . PHE D 1 232 ? 38.493  30.847  33.914  1.00 46.45  ? 228 PHE C CZ  1 
ATOM   8277  N N   . PHE D 1 233 ? 34.700  28.131  39.061  1.00 31.31  ? 229 PHE C N   1 
ATOM   8278  C CA  . PHE D 1 233 ? 33.678  27.901  40.065  1.00 30.35  ? 229 PHE C CA  1 
ATOM   8279  C C   . PHE D 1 233 ? 32.951  29.204  40.341  1.00 31.05  ? 229 PHE C C   1 
ATOM   8280  O O   . PHE D 1 233 ? 33.400  30.269  39.922  1.00 32.67  ? 229 PHE C O   1 
ATOM   8281  C CB  . PHE D 1 233 ? 34.322  27.370  41.342  1.00 31.83  ? 229 PHE C CB  1 
ATOM   8282  C CG  . PHE D 1 233 ? 34.974  26.030  41.168  1.00 32.54  ? 229 PHE C CG  1 
ATOM   8283  C CD1 . PHE D 1 233 ? 36.234  25.926  40.585  1.00 34.24  ? 229 PHE C CD1 1 
ATOM   8284  C CD2 . PHE D 1 233 ? 34.321  24.872  41.559  1.00 33.94  ? 229 PHE C CD2 1 
ATOM   8285  C CE1 . PHE D 1 233 ? 36.831  24.691  40.402  1.00 34.01  ? 229 PHE C CE1 1 
ATOM   8286  C CE2 . PHE D 1 233 ? 34.913  23.632  41.381  1.00 36.76  ? 229 PHE C CE2 1 
ATOM   8287  C CZ  . PHE D 1 233 ? 36.170  23.541  40.803  1.00 36.10  ? 229 PHE C CZ  1 
ATOM   8288  N N   . TRP D 1 234 ? 31.819  29.119  41.030  1.00 29.30  ? 230 TRP C N   1 
ATOM   8289  C CA  . TRP D 1 234 ? 31.033  30.305  41.337  1.00 31.07  ? 230 TRP C CA  1 
ATOM   8290  C C   . TRP D 1 234 ? 30.212  30.150  42.582  1.00 29.89  ? 230 TRP C C   1 
ATOM   8291  O O   . TRP D 1 234 ? 29.983  29.043  43.061  1.00 27.35  ? 230 TRP C O   1 
ATOM   8292  C CB  . TRP D 1 234 ? 30.115  30.644  40.163  1.00 29.55  ? 230 TRP C CB  1 
ATOM   8293  C CG  . TRP D 1 234 ? 29.121  29.562  39.826  1.00 29.94  ? 230 TRP C CG  1 
ATOM   8294  C CD1 . TRP D 1 234 ? 29.338  28.427  39.058  1.00 31.75  ? 230 TRP C CD1 1 
ATOM   8295  C CD2 . TRP D 1 234 ? 27.710  29.478  40.233  1.00 32.33  ? 230 TRP C CD2 1 
ATOM   8296  N NE1 . TRP D 1 234 ? 28.195  27.675  38.960  1.00 32.16  ? 230 TRP C NE1 1 
ATOM   8297  C CE2 . TRP D 1 234 ? 27.185  28.248  39.640  1.00 29.88  ? 230 TRP C CE2 1 
ATOM   8298  C CE3 . TRP D 1 234 ? 26.860  30.270  40.998  1.00 36.56  ? 230 TRP C CE3 1 
ATOM   8299  C CZ2 . TRP D 1 234 ? 25.874  27.844  39.823  1.00 31.07  ? 230 TRP C CZ2 1 
ATOM   8300  C CZ3 . TRP D 1 234 ? 25.532  29.853  41.167  1.00 34.41  ? 230 TRP C CZ3 1 
ATOM   8301  C CH2 . TRP D 1 234 ? 25.056  28.667  40.597  1.00 32.72  ? 230 TRP C CH2 1 
ATOM   8302  N N   . THR D 1 235 ? 29.770  31.280  43.113  1.00 32.28  ? 231 THR C N   1 
ATOM   8303  C CA  . THR D 1 235 ? 28.782  31.296  44.181  1.00 37.07  ? 231 THR C CA  1 
ATOM   8304  C C   . THR D 1 235 ? 28.047  32.631  44.191  1.00 38.80  ? 231 THR C C   1 
ATOM   8305  O O   . THR D 1 235 ? 28.498  33.598  43.576  1.00 45.32  ? 231 THR C O   1 
ATOM   8306  C CB  . THR D 1 235 ? 29.436  31.055  45.555  1.00 36.64  ? 231 THR C CB  1 
ATOM   8307  O OG1 . THR D 1 235 ? 28.423  30.741  46.514  1.00 36.35  ? 231 THR C OG1 1 
ATOM   8308  C CG2 . THR D 1 235 ? 30.213  32.280  46.028  1.00 32.22  ? 231 THR C CG2 1 
ATOM   8309  N N   . ILE D 1 236 ? 26.908  32.663  44.872  1.00 34.99  ? 232 ILE C N   1 
ATOM   8310  C CA  . ILE D 1 236 ? 26.155  33.889  45.072  1.00 37.04  ? 232 ILE C CA  1 
ATOM   8311  C C   . ILE D 1 236 ? 26.444  34.381  46.483  1.00 36.15  ? 232 ILE C C   1 
ATOM   8312  O O   . ILE D 1 236 ? 26.107  33.710  47.458  1.00 33.42  ? 232 ILE C O   1 
ATOM   8313  C CB  . ILE D 1 236 ? 24.636  33.673  44.859  1.00 41.92  ? 232 ILE C CB  1 
ATOM   8314  C CG1 . ILE D 1 236 ? 24.269  33.896  43.389  1.00 45.19  ? 232 ILE C CG1 1 
ATOM   8315  C CG2 . ILE D 1 236 ? 23.813  34.643  45.695  1.00 40.36  ? 232 ILE C CG2 1 
ATOM   8316  C CD1 . ILE D 1 236 ? 25.086  33.088  42.411  1.00 42.57  ? 232 ILE C CD1 1 
ATOM   8317  N N   . LEU D 1 237 ? 27.091  35.540  46.580  1.00 38.42  ? 233 LEU C N   1 
ATOM   8318  C CA  . LEU D 1 237 ? 27.413  36.146  47.867  1.00 40.83  ? 233 LEU C CA  1 
ATOM   8319  C C   . LEU D 1 237 ? 26.222  36.989  48.334  1.00 46.36  ? 233 LEU C C   1 
ATOM   8320  O O   . LEU D 1 237 ? 25.776  37.900  47.628  1.00 43.79  ? 233 LEU C O   1 
ATOM   8321  C CB  . LEU D 1 237 ? 28.679  37.005  47.746  1.00 39.07  ? 233 LEU C CB  1 
ATOM   8322  C CG  . LEU D 1 237 ? 29.398  37.463  49.021  1.00 39.50  ? 233 LEU C CG  1 
ATOM   8323  C CD1 . LEU D 1 237 ? 29.638  36.322  49.999  1.00 39.42  ? 233 LEU C CD1 1 
ATOM   8324  C CD2 . LEU D 1 237 ? 30.718  38.130  48.666  1.00 34.85  ? 233 LEU C CD2 1 
ATOM   8325  N N   . LYS D 1 238 ? 25.704  36.661  49.516  1.00 54.37  ? 234 LYS C N   1 
ATOM   8326  C CA  . LYS D 1 238 ? 24.548  37.355  50.093  1.00 61.65  ? 234 LYS C CA  1 
ATOM   8327  C C   . LYS D 1 238 ? 24.876  38.808  50.437  1.00 60.51  ? 234 LYS C C   1 
ATOM   8328  O O   . LYS D 1 238 ? 26.048  39.161  50.569  1.00 60.75  ? 234 LYS C O   1 
ATOM   8329  C CB  . LYS D 1 238 ? 24.058  36.621  51.351  1.00 68.69  ? 234 LYS C CB  1 
ATOM   8330  C CG  . LYS D 1 238 ? 23.423  35.260  51.089  1.00 76.67  ? 234 LYS C CG  1 
ATOM   8331  C CD  . LYS D 1 238 ? 22.143  35.369  50.268  1.00 78.10  ? 234 LYS C CD  1 
ATOM   8332  C CE  . LYS D 1 238 ? 21.599  34.006  49.866  1.00 82.88  ? 234 LYS C CE  1 
ATOM   8333  N NZ  . LYS D 1 238 ? 20.856  33.343  50.973  1.00 79.73  ? 234 LYS C NZ  1 
ATOM   8334  N N   . PRO D 1 239 ? 23.839  39.656  50.582  1.00 64.86  ? 235 PRO C N   1 
ATOM   8335  C CA  . PRO D 1 239 ? 24.054  41.075  50.853  1.00 69.66  ? 235 PRO C CA  1 
ATOM   8336  C C   . PRO D 1 239 ? 25.077  41.392  51.955  1.00 70.69  ? 235 PRO C C   1 
ATOM   8337  O O   . PRO D 1 239 ? 26.051  42.088  51.683  1.00 68.57  ? 235 PRO C O   1 
ATOM   8338  C CB  . PRO D 1 239 ? 22.657  41.563  51.241  1.00 71.23  ? 235 PRO C CB  1 
ATOM   8339  C CG  . PRO D 1 239 ? 21.747  40.699  50.441  1.00 68.20  ? 235 PRO C CG  1 
ATOM   8340  C CD  . PRO D 1 239 ? 22.402  39.348  50.448  1.00 66.78  ? 235 PRO C CD  1 
ATOM   8341  N N   . ASN D 1 240 ? 24.881  40.884  53.169  1.00 65.74  ? 236 ASN C N   1 
ATOM   8342  C CA  . ASN D 1 240 ? 25.751  41.266  54.293  1.00 77.39  ? 236 ASN C CA  1 
ATOM   8343  C C   . ASN D 1 240 ? 26.915  40.293  54.534  1.00 71.00  ? 236 ASN C C   1 
ATOM   8344  O O   . ASN D 1 240 ? 27.568  40.339  55.579  1.00 59.81  ? 236 ASN C O   1 
ATOM   8345  C CB  . ASN D 1 240 ? 24.914  41.420  55.573  1.00 89.38  ? 236 ASN C CB  1 
ATOM   8346  C CG  . ASN D 1 240 ? 25.549  42.368  56.583  1.00 94.33  ? 236 ASN C CG  1 
ATOM   8347  O OD1 . ASN D 1 240 ? 25.999  43.459  56.229  1.00 86.09  ? 236 ASN C OD1 1 
ATOM   8348  N ND2 . ASN D 1 240 ? 25.577  41.957  57.851  1.00 87.86  ? 236 ASN C ND2 1 
ATOM   8349  N N   . ASP D 1 241 ? 27.184  39.434  53.554  1.00 67.78  ? 237 ASP C N   1 
ATOM   8350  C CA  . ASP D 1 241 ? 28.141  38.344  53.710  1.00 67.93  ? 237 ASP C CA  1 
ATOM   8351  C C   . ASP D 1 241 ? 29.472  38.689  53.043  1.00 67.68  ? 237 ASP C C   1 
ATOM   8352  O O   . ASP D 1 241 ? 29.550  39.625  52.239  1.00 63.73  ? 237 ASP C O   1 
ATOM   8353  C CB  . ASP D 1 241 ? 27.554  37.065  53.103  1.00 74.13  ? 237 ASP C CB  1 
ATOM   8354  C CG  . ASP D 1 241 ? 28.319  35.812  53.494  1.00 69.00  ? 237 ASP C CG  1 
ATOM   8355  O OD1 . ASP D 1 241 ? 29.076  35.842  54.487  1.00 66.22  ? 237 ASP C OD1 1 
ATOM   8356  O OD2 . ASP D 1 241 ? 28.158  34.789  52.802  1.00 73.73  ? 237 ASP C OD2 1 
ATOM   8357  N N   . ALA D 1 242 ? 30.514  37.938  53.396  1.00 61.15  ? 238 ALA C N   1 
ATOM   8358  C CA  . ALA D 1 242 ? 31.842  38.118  52.818  1.00 56.08  ? 238 ALA C CA  1 
ATOM   8359  C C   . ALA D 1 242 ? 32.412  36.797  52.301  1.00 47.75  ? 238 ALA C C   1 
ATOM   8360  O O   . ALA D 1 242 ? 32.067  35.722  52.792  1.00 42.55  ? 238 ALA C O   1 
ATOM   8361  C CB  . ALA D 1 242 ? 32.784  38.729  53.848  1.00 50.25  ? 238 ALA C CB  1 
ATOM   8362  N N   . ILE D 1 243 ? 33.288  36.903  51.307  1.00 45.44  ? 239 ILE C N   1 
ATOM   8363  C CA  . ILE D 1 243 ? 33.960  35.757  50.708  1.00 41.05  ? 239 ILE C CA  1 
ATOM   8364  C C   . ILE D 1 243 ? 35.453  35.845  51.023  1.00 41.39  ? 239 ILE C C   1 
ATOM   8365  O O   . ILE D 1 243 ? 36.034  36.925  50.965  1.00 44.70  ? 239 ILE C O   1 
ATOM   8366  C CB  . ILE D 1 243 ? 33.727  35.711  49.182  1.00 37.53  ? 239 ILE C CB  1 
ATOM   8367  C CG1 . ILE D 1 243 ? 34.272  34.409  48.585  1.00 38.10  ? 239 ILE C CG1 1 
ATOM   8368  C CG2 . ILE D 1 243 ? 34.366  36.910  48.497  1.00 34.15  ? 239 ILE C CG2 1 
ATOM   8369  C CD1 . ILE D 1 243 ? 33.745  34.112  47.200  1.00 37.37  ? 239 ILE C CD1 1 
ATOM   8370  N N   . HIS D 1 244 ? 36.069  34.716  51.360  1.00 47.76  ? 240 HIS C N   1 
ATOM   8371  C CA  . HIS D 1 244 ? 37.472  34.699  51.785  1.00 49.56  ? 240 HIS C CA  1 
ATOM   8372  C C   . HIS D 1 244 ? 38.293  33.749  50.960  1.00 44.71  ? 240 HIS C C   1 
ATOM   8373  O O   . HIS D 1 244 ? 38.064  32.544  50.987  1.00 53.36  ? 240 HIS C O   1 
ATOM   8374  C CB  . HIS D 1 244 ? 37.569  34.307  53.255  1.00 47.99  ? 240 HIS C CB  1 
ATOM   8375  C CG  . HIS D 1 244 ? 36.648  35.092  54.165  1.00 59.43  ? 240 HIS C CG  1 
ATOM   8376  N ND1 . HIS D 1 244 ? 36.987  36.283  54.687  1.00 66.35  ? 240 HIS C ND1 1 
ATOM   8377  C CD2 . HIS D 1 244 ? 35.368  34.803  54.646  1.00 60.49  ? 240 HIS C CD2 1 
ATOM   8378  C CE1 . HIS D 1 244 ? 35.978  36.733  55.460  1.00 70.50  ? 240 HIS C CE1 1 
ATOM   8379  N NE2 . HIS D 1 244 ? 34.989  35.826  55.429  1.00 67.68  ? 240 HIS C NE2 1 
ATOM   8380  N N   . PHE D 1 245 ? 39.263  34.283  50.224  1.00 40.51  ? 241 PHE C N   1 
ATOM   8381  C CA  . PHE D 1 245 ? 40.186  33.462  49.442  1.00 42.69  ? 241 PHE C CA  1 
ATOM   8382  C C   . PHE D 1 245 ? 41.489  33.263  50.198  1.00 41.10  ? 241 PHE C C   1 
ATOM   8383  O O   . PHE D 1 245 ? 41.979  34.176  50.864  1.00 40.31  ? 241 PHE C O   1 
ATOM   8384  C CB  . PHE D 1 245 ? 40.488  34.110  48.086  1.00 42.77  ? 241 PHE C CB  1 
ATOM   8385  C CG  . PHE D 1 245 ? 39.290  34.240  47.197  1.00 41.60  ? 241 PHE C CG  1 
ATOM   8386  C CD1 . PHE D 1 245 ? 38.544  35.408  47.184  1.00 42.41  ? 241 PHE C CD1 1 
ATOM   8387  C CD2 . PHE D 1 245 ? 38.910  33.195  46.371  1.00 44.71  ? 241 PHE C CD2 1 
ATOM   8388  C CE1 . PHE D 1 245 ? 37.437  35.530  46.363  1.00 45.00  ? 241 PHE C CE1 1 
ATOM   8389  C CE2 . PHE D 1 245 ? 37.802  33.309  45.546  1.00 45.18  ? 241 PHE C CE2 1 
ATOM   8390  C CZ  . PHE D 1 245 ? 37.066  34.479  45.541  1.00 44.53  ? 241 PHE C CZ  1 
ATOM   8391  N N   . GLU D 1 246 ? 42.047  32.063  50.083  1.00 42.02  ? 242 GLU C N   1 
ATOM   8392  C CA  . GLU D 1 246 ? 43.389  31.775  50.574  1.00 40.75  ? 242 GLU C CA  1 
ATOM   8393  C C   . GLU D 1 246 ? 44.057  30.830  49.585  1.00 36.17  ? 242 GLU C C   1 
ATOM   8394  O O   . GLU D 1 246 ? 43.571  29.725  49.358  1.00 40.86  ? 242 GLU C O   1 
ATOM   8395  C CB  . GLU D 1 246 ? 43.340  31.166  51.974  1.00 39.34  ? 242 GLU C CB  1 
ATOM   8396  C CG  . GLU D 1 246 ? 44.704  31.022  52.633  1.00 47.45  ? 242 GLU C CG  1 
ATOM   8397  C CD  . GLU D 1 246 ? 44.629  30.680  54.113  1.00 56.69  ? 242 GLU C CD  1 
ATOM   8398  O OE1 . GLU D 1 246 ? 45.629  30.157  54.651  1.00 56.07  ? 242 GLU C OE1 1 
ATOM   8399  O OE2 . GLU D 1 246 ? 43.583  30.940  54.745  1.00 67.59  ? 242 GLU C OE2 1 
ATOM   8400  N N   . SER D 1 247 ? 45.143  31.281  48.969  1.00 33.69  ? 243 SER C N   1 
ATOM   8401  C CA  . SER D 1 247 ? 45.838  30.477  47.971  1.00 37.61  ? 243 SER C CA  1 
ATOM   8402  C C   . SER D 1 247 ? 47.340  30.657  47.996  1.00 42.21  ? 243 SER C C   1 
ATOM   8403  O O   . SER D 1 247 ? 47.866  31.718  48.323  1.00 50.80  ? 243 SER C O   1 
ATOM   8404  C CB  . SER D 1 247 ? 45.360  30.799  46.561  1.00 36.28  ? 243 SER C CB  1 
ATOM   8405  O OG  . SER D 1 247 ? 46.074  29.999  45.624  1.00 30.53  ? 243 SER C OG  1 
ATOM   8406  N N   . ASN D 1 248 ? 48.006  29.600  47.574  1.00 46.90  ? 244 ASN C N   1 
ATOM   8407  C CA  . ASN D 1 248 ? 49.448  29.461  47.677  1.00 50.50  ? 244 ASN C CA  1 
ATOM   8408  C C   . ASN D 1 248 ? 50.090  29.336  46.296  1.00 47.84  ? 244 ASN C C   1 
ATOM   8409  O O   . ASN D 1 248 ? 51.294  29.500  46.146  1.00 49.37  ? 244 ASN C O   1 
ATOM   8410  C CB  . ASN D 1 248 ? 49.732  28.241  48.557  1.00 53.83  ? 244 ASN C CB  1 
ATOM   8411  C CG  . ASN D 1 248 ? 51.198  28.034  48.832  1.00 59.05  ? 244 ASN C CG  1 
ATOM   8412  O OD1 . ASN D 1 248 ? 51.733  26.952  48.595  1.00 55.60  ? 244 ASN C OD1 1 
ATOM   8413  N ND2 . ASN D 1 248 ? 51.859  29.064  49.346  1.00 81.30  ? 244 ASN C ND2 1 
ATOM   8414  N N   . GLY D 1 249 ? 49.275  29.036  45.290  1.00 45.07  ? 245 GLY C N   1 
ATOM   8415  C CA  . GLY D 1 249 ? 49.714  29.024  43.912  1.00 47.54  ? 245 GLY C CA  1 
ATOM   8416  C C   . GLY D 1 249 ? 48.484  28.882  43.015  1.00 48.31  ? 245 GLY C C   1 
ATOM   8417  O O   . GLY D 1 249 ? 47.339  28.859  43.480  1.00 43.36  ? 245 GLY C O   1 
ATOM   8418  N N   . ASN D 1 250 ? 48.730  28.747  41.725  1.00 47.31  ? 246 ASN C N   1 
ATOM   8419  C CA  . ASN D 1 250 ? 47.751  28.235  40.773  1.00 49.79  ? 246 ASN C CA  1 
ATOM   8420  C C   . ASN D 1 250 ? 46.317  28.773  40.728  1.00 49.39  ? 246 ASN C C   1 
ATOM   8421  O O   . ASN D 1 250 ? 45.379  27.999  40.479  1.00 49.69  ? 246 ASN C O   1 
ATOM   8422  C CB  . ASN D 1 250 ? 47.625  26.728  40.968  1.00 51.76  ? 246 ASN C CB  1 
ATOM   8423  C CG  . ASN D 1 250 ? 48.837  25.975  40.462  1.00 59.46  ? 246 ASN C CG  1 
ATOM   8424  O OD1 . ASN D 1 250 ? 49.902  26.014  41.081  1.00 69.64  ? 246 ASN C OD1 1 
ATOM   8425  N ND2 . ASN D 1 250 ? 48.685  25.282  39.327  1.00 68.27  ? 246 ASN C ND2 1 
ATOM   8426  N N   . PHE D 1 251 ? 46.114  30.068  40.920  1.00 46.17  ? 247 PHE C N   1 
ATOM   8427  C CA  . PHE D 1 251 ? 44.749  30.542  41.046  1.00 43.03  ? 247 PHE C CA  1 
ATOM   8428  C C   . PHE D 1 251 ? 44.356  31.796  40.275  1.00 45.43  ? 247 PHE C C   1 
ATOM   8429  O O   . PHE D 1 251 ? 45.093  32.782  40.192  1.00 45.20  ? 247 PHE C O   1 
ATOM   8430  C CB  . PHE D 1 251 ? 44.462  30.643  42.546  1.00 45.41  ? 247 PHE C CB  1 
ATOM   8431  C CG  . PHE D 1 251 ? 43.516  31.738  42.973  1.00 42.59  ? 247 PHE C CG  1 
ATOM   8432  C CD1 . PHE D 1 251 ? 42.131  31.590  42.882  1.00 41.98  ? 247 PHE C CD1 1 
ATOM   8433  C CD2 . PHE D 1 251 ? 44.013  32.856  43.604  1.00 40.04  ? 247 PHE C CD2 1 
ATOM   8434  C CE1 . PHE D 1 251 ? 41.270  32.583  43.342  1.00 40.50  ? 247 PHE C CE1 1 
ATOM   8435  C CE2 . PHE D 1 251 ? 43.164  33.847  44.071  1.00 38.72  ? 247 PHE C CE2 1 
ATOM   8436  C CZ  . PHE D 1 251 ? 41.792  33.712  43.945  1.00 39.31  ? 247 PHE C CZ  1 
ATOM   8437  N N   . ILE D 1 252 ? 43.159  31.706  39.709  1.00 39.29  ? 248 ILE C N   1 
ATOM   8438  C CA  . ILE D 1 252 ? 42.638  32.707  38.807  1.00 38.43  ? 248 ILE C CA  1 
ATOM   8439  C C   . ILE D 1 252 ? 41.689  33.550  39.628  1.00 37.63  ? 248 ILE C C   1 
ATOM   8440  O O   . ILE D 1 252 ? 40.557  33.149  39.886  1.00 39.38  ? 248 ILE C O   1 
ATOM   8441  C CB  . ILE D 1 252 ? 41.916  32.059  37.609  1.00 36.93  ? 248 ILE C CB  1 
ATOM   8442  C CG1 . ILE D 1 252 ? 42.937  31.488  36.621  1.00 37.31  ? 248 ILE C CG1 1 
ATOM   8443  C CG2 . ILE D 1 252 ? 41.059  33.074  36.875  1.00 36.36  ? 248 ILE C CG2 1 
ATOM   8444  C CD1 . ILE D 1 252 ? 43.861  30.439  37.185  1.00 35.04  ? 248 ILE C CD1 1 
ATOM   8445  N N   . ALA D 1 253 ? 42.176  34.704  40.070  1.00 37.66  ? 249 ALA C N   1 
ATOM   8446  C CA  . ALA D 1 253 ? 41.428  35.549  40.989  1.00 35.07  ? 249 ALA C CA  1 
ATOM   8447  C C   . ALA D 1 253 ? 40.355  36.343  40.245  1.00 39.80  ? 249 ALA C C   1 
ATOM   8448  O O   . ALA D 1 253 ? 40.534  36.695  39.071  1.00 44.67  ? 249 ALA C O   1 
ATOM   8449  C CB  . ALA D 1 253 ? 42.365  36.487  41.736  1.00 27.49  ? 249 ALA C CB  1 
ATOM   8450  N N   . PRO D 1 254 ? 39.231  36.617  40.921  1.00 38.01  ? 250 PRO C N   1 
ATOM   8451  C CA  . PRO D 1 254 ? 38.240  37.512  40.342  1.00 46.27  ? 250 PRO C CA  1 
ATOM   8452  C C   . PRO D 1 254 ? 38.744  38.944  40.343  1.00 53.60  ? 250 PRO C C   1 
ATOM   8453  O O   . PRO D 1 254 ? 39.420  39.343  41.289  1.00 59.54  ? 250 PRO C O   1 
ATOM   8454  C CB  . PRO D 1 254 ? 37.057  37.396  41.303  1.00 46.23  ? 250 PRO C CB  1 
ATOM   8455  C CG  . PRO D 1 254 ? 37.660  36.995  42.605  1.00 41.02  ? 250 PRO C CG  1 
ATOM   8456  C CD  . PRO D 1 254 ? 38.837  36.140  42.259  1.00 36.66  ? 250 PRO C CD  1 
ATOM   8457  N N   . GLU D 1 255 ? 38.447  39.690  39.281  1.00 53.70  ? 251 GLU C N   1 
ATOM   8458  C CA  . GLU D 1 255 ? 38.554  41.145  39.313  1.00 52.79  ? 251 GLU C CA  1 
ATOM   8459  C C   . GLU D 1 255 ? 37.152  41.744  39.426  1.00 54.00  ? 251 GLU C C   1 
ATOM   8460  O O   . GLU D 1 255 ? 36.917  42.654  40.228  1.00 49.59  ? 251 GLU C O   1 
ATOM   8461  C CB  . GLU D 1 255 ? 39.261  41.673  38.064  1.00 59.91  ? 251 GLU C CB  1 
ATOM   8462  C CG  . GLU D 1 255 ? 39.632  43.150  38.152  1.00 68.34  ? 251 GLU C CG  1 
ATOM   8463  C CD  . GLU D 1 255 ? 40.334  43.674  36.909  1.00 79.05  ? 251 GLU C CD  1 
ATOM   8464  O OE1 . GLU D 1 255 ? 40.615  42.877  35.980  1.00 79.98  ? 251 GLU C OE1 1 
ATOM   8465  O OE2 . GLU D 1 255 ? 40.612  44.894  36.867  1.00 83.82  ? 251 GLU C OE2 1 
ATOM   8466  N N   . TYR D 1 256 ? 36.229  41.223  38.617  1.00 57.27  ? 252 TYR C N   1 
ATOM   8467  C CA  . TYR D 1 256 ? 34.852  41.703  38.582  1.00 57.30  ? 252 TYR C CA  1 
ATOM   8468  C C   . TYR D 1 256 ? 33.866  40.651  39.072  1.00 56.94  ? 252 TYR C C   1 
ATOM   8469  O O   . TYR D 1 256 ? 34.018  39.465  38.782  1.00 62.63  ? 252 TYR C O   1 
ATOM   8470  C CB  . TYR D 1 256 ? 34.477  42.111  37.159  1.00 57.29  ? 252 TYR C CB  1 
ATOM   8471  C CG  . TYR D 1 256 ? 35.301  43.251  36.626  1.00 66.45  ? 252 TYR C CG  1 
ATOM   8472  C CD1 . TYR D 1 256 ? 36.461  43.012  35.898  1.00 69.61  ? 252 TYR C CD1 1 
ATOM   8473  C CD2 . TYR D 1 256 ? 34.929  44.573  36.857  1.00 74.26  ? 252 TYR C CD2 1 
ATOM   8474  C CE1 . TYR D 1 256 ? 37.225  44.058  35.408  1.00 74.53  ? 252 TYR C CE1 1 
ATOM   8475  C CE2 . TYR D 1 256 ? 35.687  45.626  36.374  1.00 76.95  ? 252 TYR C CE2 1 
ATOM   8476  C CZ  . TYR D 1 256 ? 36.835  45.364  35.649  1.00 77.20  ? 252 TYR C CZ  1 
ATOM   8477  O OH  . TYR D 1 256 ? 37.593  46.405  35.166  1.00 79.46  ? 252 TYR C OH  1 
ATOM   8478  N N   . ALA D 1 257 ? 32.865  41.103  39.826  1.00 54.48  ? 253 ALA C N   1 
ATOM   8479  C CA  . ALA D 1 257 ? 31.711  40.288  40.190  1.00 51.83  ? 253 ALA C CA  1 
ATOM   8480  C C   . ALA D 1 257 ? 30.464  40.914  39.557  1.00 58.32  ? 253 ALA C C   1 
ATOM   8481  O O   . ALA D 1 257 ? 30.571  41.883  38.803  1.00 61.99  ? 253 ALA C O   1 
ATOM   8482  C CB  . ALA D 1 257 ? 31.574  40.205  41.699  1.00 47.29  ? 253 ALA C CB  1 
ATOM   8483  N N   . TYR D 1 258 ? 29.286  40.376  39.865  1.00 55.90  ? 254 TYR C N   1 
ATOM   8484  C CA  . TYR D 1 258 ? 28.054  40.821  39.223  1.00 48.26  ? 254 TYR C CA  1 
ATOM   8485  C C   . TYR D 1 258 ? 26.903  40.996  40.209  1.00 47.80  ? 254 TYR C C   1 
ATOM   8486  O O   . TYR D 1 258 ? 26.455  40.028  40.821  1.00 41.07  ? 254 TYR C O   1 
ATOM   8487  C CB  . TYR D 1 258 ? 27.630  39.806  38.174  1.00 48.45  ? 254 TYR C CB  1 
ATOM   8488  C CG  . TYR D 1 258 ? 28.546  39.697  36.988  1.00 50.84  ? 254 TYR C CG  1 
ATOM   8489  C CD1 . TYR D 1 258 ? 29.511  38.697  36.916  1.00 53.36  ? 254 TYR C CD1 1 
ATOM   8490  C CD2 . TYR D 1 258 ? 28.433  40.577  35.922  1.00 56.60  ? 254 TYR C CD2 1 
ATOM   8491  C CE1 . TYR D 1 258 ? 30.347  38.583  35.815  1.00 57.75  ? 254 TYR C CE1 1 
ATOM   8492  C CE2 . TYR D 1 258 ? 29.259  40.473  34.814  1.00 58.34  ? 254 TYR C CE2 1 
ATOM   8493  C CZ  . TYR D 1 258 ? 30.214  39.475  34.764  1.00 59.76  ? 254 TYR C CZ  1 
ATOM   8494  O OH  . TYR D 1 258 ? 31.039  39.381  33.665  1.00 59.80  ? 254 TYR C OH  1 
ATOM   8495  N N   . LYS D 1 259 ? 26.419  42.231  40.344  1.00 50.46  ? 255 LYS C N   1 
ATOM   8496  C CA  . LYS D 1 259 ? 25.183  42.504  41.075  1.00 51.52  ? 255 LYS C CA  1 
ATOM   8497  C C   . LYS D 1 259 ? 24.030  41.793  40.372  1.00 51.29  ? 255 LYS C C   1 
ATOM   8498  O O   . LYS D 1 259 ? 23.895  41.897  39.154  1.00 50.24  ? 255 LYS C O   1 
ATOM   8499  C CB  . LYS D 1 259 ? 24.887  44.002  41.111  1.00 55.41  ? 255 LYS C CB  1 
ATOM   8500  C CG  . LYS D 1 259 ? 25.681  44.807  42.123  1.00 59.57  ? 255 LYS C CG  1 
ATOM   8501  C CD  . LYS D 1 259 ? 25.207  46.260  42.085  1.00 63.56  ? 255 LYS C CD  1 
ATOM   8502  C CE  . LYS D 1 259 ? 25.799  47.148  43.180  1.00 63.95  ? 255 LYS C CE  1 
ATOM   8503  N NZ  . LYS D 1 259 ? 24.757  48.073  43.746  1.00 58.27  ? 255 LYS C NZ  1 
ATOM   8504  N N   . ILE D 1 260 ? 23.207  41.082  41.140  1.00 51.94  ? 256 ILE C N   1 
ATOM   8505  C CA  . ILE D 1 260 ? 22.117  40.285  40.579  1.00 50.53  ? 256 ILE C CA  1 
ATOM   8506  C C   . ILE D 1 260 ? 20.824  40.436  41.376  1.00 47.91  ? 256 ILE C C   1 
ATOM   8507  O O   . ILE D 1 260 ? 20.830  40.352  42.609  1.00 40.30  ? 256 ILE C O   1 
ATOM   8508  C CB  . ILE D 1 260 ? 22.491  38.790  40.534  1.00 56.30  ? 256 ILE C CB  1 
ATOM   8509  C CG1 . ILE D 1 260 ? 23.215  38.462  39.230  1.00 59.80  ? 256 ILE C CG1 1 
ATOM   8510  C CG2 . ILE D 1 260 ? 21.251  37.916  40.636  1.00 62.61  ? 256 ILE C CG2 1 
ATOM   8511  C CD1 . ILE D 1 260 ? 23.484  36.985  39.048  1.00 63.75  ? 256 ILE C CD1 1 
ATOM   8512  N N   . VAL D 1 261 ? 19.728  40.671  40.654  1.00 45.73  ? 257 VAL C N   1 
ATOM   8513  C CA  . VAL D 1 261 ? 18.385  40.575  41.210  1.00 46.80  ? 257 VAL C CA  1 
ATOM   8514  C C   . VAL D 1 261 ? 17.565  39.644  40.324  1.00 43.72  ? 257 VAL C C   1 
ATOM   8515  O O   . VAL D 1 261 ? 17.463  39.854  39.111  1.00 41.97  ? 257 VAL C O   1 
ATOM   8516  C CB  . VAL D 1 261 ? 17.683  41.946  41.284  1.00 51.92  ? 257 VAL C CB  1 
ATOM   8517  C CG1 . VAL D 1 261 ? 16.355  41.823  42.019  1.00 50.57  ? 257 VAL C CG1 1 
ATOM   8518  C CG2 . VAL D 1 261 ? 18.569  42.967  41.977  1.00 44.53  ? 257 VAL C CG2 1 
ATOM   8519  N N   . LYS D 1 262 ? 16.993  38.608  40.933  1.00 45.23  ? 258 LYS C N   1 
ATOM   8520  C CA  . LYS D 1 262 ? 16.177  37.632  40.215  1.00 48.61  ? 258 LYS C CA  1 
ATOM   8521  C C   . LYS D 1 262 ? 14.742  37.679  40.725  1.00 50.87  ? 258 LYS C C   1 
ATOM   8522  O O   . LYS D 1 262 ? 14.509  37.648  41.932  1.00 47.83  ? 258 LYS C O   1 
ATOM   8523  C CB  . LYS D 1 262 ? 16.756  36.222  40.388  1.00 47.40  ? 258 LYS C CB  1 
ATOM   8524  C CG  . LYS D 1 262 ? 16.048  35.159  39.559  1.00 47.10  ? 258 LYS C CG  1 
ATOM   8525  C CD  . LYS D 1 262 ? 16.950  33.970  39.280  1.00 44.84  ? 258 LYS C CD  1 
ATOM   8526  C CE  . LYS D 1 262 ? 16.205  32.848  38.583  1.00 45.64  ? 258 LYS C CE  1 
ATOM   8527  N NZ  . LYS D 1 262 ? 15.998  33.148  37.137  1.00 47.22  ? 258 LYS C NZ  1 
ATOM   8528  N N   . LYS D 1 263 ? 13.792  37.755  39.794  1.00 61.71  ? 259 LYS C N   1 
ATOM   8529  C CA  . LYS D 1 263 ? 12.365  37.828  40.121  1.00 64.18  ? 259 LYS C CA  1 
ATOM   8530  C C   . LYS D 1 263 ? 11.617  36.586  39.641  1.00 66.87  ? 259 LYS C C   1 
ATOM   8531  O O   . LYS D 1 263 ? 10.751  36.072  40.350  1.00 80.88  ? 259 LYS C O   1 
ATOM   8532  C CB  . LYS D 1 263 ? 11.738  39.076  39.494  1.00 63.87  ? 259 LYS C CB  1 
ATOM   8533  C CG  . LYS D 1 263 ? 12.328  40.390  39.979  1.00 68.82  ? 259 LYS C CG  1 
ATOM   8534  C CD  . LYS D 1 263 ? 11.699  40.941  41.217  1.00 72.96  ? 259 LYS C CD  1 
ATOM   8535  C CE  . LYS D 1 263 ? 12.319  42.283  41.593  1.00 71.41  ? 259 LYS C CE  1 
ATOM   8536  N NZ  . LYS D 1 263 ? 11.730  42.870  42.826  1.00 72.13  ? 259 LYS C NZ  1 
ATOM   8537  N N   . GLY D 1 264 ? 11.942  36.121  38.435  1.00 59.76  ? 260 GLY C N   1 
ATOM   8538  C CA  . GLY D 1 264 ? 11.309  34.936  37.854  1.00 55.68  ? 260 GLY C CA  1 
ATOM   8539  C C   . GLY D 1 264 ? 12.268  34.078  37.046  1.00 50.05  ? 260 GLY C C   1 
ATOM   8540  O O   . GLY D 1 264 ? 13.469  34.326  37.026  1.00 52.22  ? 260 GLY C O   1 
ATOM   8541  N N   . ASP D 1 265 ? 11.725  33.067  36.376  1.00 49.05  ? 261 ASP C N   1 
ATOM   8542  C CA  . ASP D 1 265 ? 12.526  32.083  35.655  1.00 49.03  ? 261 ASP C CA  1 
ATOM   8543  C C   . ASP D 1 265 ? 12.190  32.005  34.173  1.00 41.66  ? 261 ASP C C   1 
ATOM   8544  O O   . ASP D 1 265 ? 11.159  32.499  33.726  1.00 43.03  ? 261 ASP C O   1 
ATOM   8545  C CB  . ASP D 1 265 ? 12.351  30.709  36.302  1.00 58.63  ? 261 ASP C CB  1 
ATOM   8546  C CG  . ASP D 1 265 ? 12.919  30.656  37.708  1.00 75.71  ? 261 ASP C CG  1 
ATOM   8547  O OD1 . ASP D 1 265 ? 14.156  30.522  37.848  1.00 83.95  ? 261 ASP C OD1 1 
ATOM   8548  O OD2 . ASP D 1 265 ? 12.124  30.750  38.671  1.00 83.04  ? 261 ASP C OD2 1 
ATOM   8549  N N   . SER D 1 266 ? 13.082  31.367  33.424  1.00 37.65  ? 262 SER C N   1 
ATOM   8550  C CA  . SER D 1 266 ? 12.941  31.234  31.984  1.00 38.95  ? 262 SER C CA  1 
ATOM   8551  C C   . SER D 1 266 ? 13.907  30.134  31.543  1.00 38.58  ? 262 SER C C   1 
ATOM   8552  O O   . SER D 1 266 ? 14.169  29.206  32.309  1.00 46.77  ? 262 SER C O   1 
ATOM   8553  C CB  . SER D 1 266 ? 13.195  32.587  31.289  1.00 39.36  ? 262 SER C CB  1 
ATOM   8554  O OG  . SER D 1 266 ? 14.287  32.560  30.392  1.00 48.98  ? 262 SER C OG  1 
ATOM   8555  N N   . THR D 1 267 ? 14.411  30.203  30.317  1.00 39.08  ? 263 THR C N   1 
ATOM   8556  C CA  . THR D 1 267 ? 15.384  29.222  29.845  1.00 42.73  ? 263 THR C CA  1 
ATOM   8557  C C   . THR D 1 267 ? 16.298  29.815  28.771  1.00 40.92  ? 263 THR C C   1 
ATOM   8558  O O   . THR D 1 267 ? 16.195  30.996  28.440  1.00 40.82  ? 263 THR C O   1 
ATOM   8559  C CB  . THR D 1 267 ? 14.673  27.953  29.312  1.00 43.42  ? 263 THR C CB  1 
ATOM   8560  O OG1 . THR D 1 267 ? 15.611  26.877  29.206  1.00 42.86  ? 263 THR C OG1 1 
ATOM   8561  C CG2 . THR D 1 267 ? 14.030  28.208  27.949  1.00 42.81  ? 263 THR C CG2 1 
ATOM   8562  N N   . ILE D 1 268 ? 17.199  28.990  28.250  1.00 43.24  ? 264 ILE C N   1 
ATOM   8563  C CA  . ILE D 1 268 ? 18.097  29.387  27.175  1.00 49.24  ? 264 ILE C CA  1 
ATOM   8564  C C   . ILE D 1 268 ? 17.548  28.844  25.868  1.00 51.26  ? 264 ILE C C   1 
ATOM   8565  O O   . ILE D 1 268 ? 17.301  27.644  25.751  1.00 58.23  ? 264 ILE C O   1 
ATOM   8566  C CB  . ILE D 1 268 ? 19.519  28.825  27.386  1.00 53.53  ? 264 ILE C CB  1 
ATOM   8567  C CG1 . ILE D 1 268 ? 20.172  29.472  28.613  1.00 52.63  ? 264 ILE C CG1 1 
ATOM   8568  C CG2 . ILE D 1 268 ? 20.368  29.038  26.140  1.00 55.35  ? 264 ILE C CG2 1 
ATOM   8569  C CD1 . ILE D 1 268 ? 19.672  28.915  29.929  1.00 57.31  ? 264 ILE C CD1 1 
ATOM   8570  N N   . MET D 1 269 ? 17.353  29.726  24.890  1.00 50.71  ? 265 MET C N   1 
ATOM   8571  C CA  . MET D 1 269 ? 16.843  29.324  23.584  1.00 51.20  ? 265 MET C CA  1 
ATOM   8572  C C   . MET D 1 269 ? 17.994  29.165  22.605  1.00 47.72  ? 265 MET C C   1 
ATOM   8573  O O   . MET D 1 269 ? 18.908  29.985  22.578  1.00 49.23  ? 265 MET C O   1 
ATOM   8574  C CB  . MET D 1 269 ? 15.845  30.352  23.053  1.00 61.33  ? 265 MET C CB  1 
ATOM   8575  C CG  . MET D 1 269 ? 15.026  29.856  21.869  1.00 64.71  ? 265 MET C CG  1 
ATOM   8576  S SD  . MET D 1 269 ? 13.545  30.844  21.587  1.00 66.02  ? 265 MET C SD  1 
ATOM   8577  C CE  . MET D 1 269 ? 14.277  32.239  20.741  1.00 77.31  ? 265 MET C CE  1 
ATOM   8578  N N   . LYS D 1 270 ? 17.948  28.089  21.825  1.00 50.48  ? 266 LYS C N   1 
ATOM   8579  C CA  . LYS D 1 270 ? 18.941  27.817  20.793  1.00 57.38  ? 266 LYS C CA  1 
ATOM   8580  C C   . LYS D 1 270 ? 18.358  28.215  19.444  1.00 56.05  ? 266 LYS C C   1 
ATOM   8581  O O   . LYS D 1 270 ? 17.434  27.568  18.948  1.00 56.69  ? 266 LYS C O   1 
ATOM   8582  C CB  . LYS D 1 270 ? 19.303  26.330  20.784  1.00 63.61  ? 266 LYS C CB  1 
ATOM   8583  C CG  . LYS D 1 270 ? 19.975  25.830  22.057  1.00 73.10  ? 266 LYS C CG  1 
ATOM   8584  C CD  . LYS D 1 270 ? 21.427  26.279  22.140  1.00 81.88  ? 266 LYS C CD  1 
ATOM   8585  C CE  . LYS D 1 270 ? 22.178  25.597  23.275  1.00 86.59  ? 266 LYS C CE  1 
ATOM   8586  N NZ  . LYS D 1 270 ? 23.640  25.887  23.211  1.00 90.24  ? 266 LYS C NZ  1 
ATOM   8587  N N   . SER D 1 271 ? 18.881  29.291  18.861  1.00 60.45  ? 267 SER C N   1 
ATOM   8588  C CA  . SER D 1 271 ? 18.358  29.801  17.595  1.00 62.08  ? 267 SER C CA  1 
ATOM   8589  C C   . SER D 1 271 ? 19.335  30.708  16.854  1.00 63.17  ? 267 SER C C   1 
ATOM   8590  O O   . SER D 1 271 ? 20.074  31.469  17.475  1.00 52.14  ? 267 SER C O   1 
ATOM   8591  C CB  . SER D 1 271 ? 17.061  30.560  17.859  1.00 58.09  ? 267 SER C CB  1 
ATOM   8592  O OG  . SER D 1 271 ? 16.685  31.351  16.746  1.00 54.40  ? 267 SER C OG  1 
ATOM   8593  N N   . GLU D 1 272 ? 19.314  30.624  15.523  1.00 75.68  ? 268 GLU C N   1 
ATOM   8594  C CA  . GLU D 1 272 ? 20.100  31.509  14.658  1.00 77.10  ? 268 GLU C CA  1 
ATOM   8595  C C   . GLU D 1 272 ? 19.254  32.642  14.081  1.00 71.26  ? 268 GLU C C   1 
ATOM   8596  O O   . GLU D 1 272 ? 19.778  33.518  13.398  1.00 80.11  ? 268 GLU C O   1 
ATOM   8597  C CB  . GLU D 1 272 ? 20.684  30.715  13.483  1.00 82.30  ? 268 GLU C CB  1 
ATOM   8598  C CG  . GLU D 1 272 ? 22.168  30.960  13.239  1.00 98.94  ? 268 GLU C CG  1 
ATOM   8599  C CD  . GLU D 1 272 ? 22.847  29.866  12.423  1.00 108.62 ? 268 GLU C CD  1 
ATOM   8600  O OE1 . GLU D 1 272 ? 23.105  30.095  11.220  1.00 111.16 ? 268 GLU C OE1 1 
ATOM   8601  O OE2 . GLU D 1 272 ? 23.140  28.780  12.982  1.00 111.43 ? 268 GLU C OE2 1 
ATOM   8602  N N   . VAL D 1 273 ? 17.949  32.604  14.334  1.00 68.05  ? 269 VAL C N   1 
ATOM   8603  C CA  . VAL D 1 273 ? 17.012  33.596  13.800  1.00 65.08  ? 269 VAL C CA  1 
ATOM   8604  C C   . VAL D 1 273 ? 17.315  34.987  14.344  1.00 63.99  ? 269 VAL C C   1 
ATOM   8605  O O   . VAL D 1 273 ? 17.678  35.144  15.506  1.00 66.63  ? 269 VAL C O   1 
ATOM   8606  C CB  . VAL D 1 273 ? 15.540  33.219  14.112  1.00 58.98  ? 269 VAL C CB  1 
ATOM   8607  C CG1 . VAL D 1 273 ? 14.619  34.426  14.012  1.00 55.53  ? 269 VAL C CG1 1 
ATOM   8608  C CG2 . VAL D 1 273 ? 15.068  32.106  13.188  1.00 52.52  ? 269 VAL C CG2 1 
ATOM   8609  N N   . GLU D 1 274 ? 17.139  35.986  13.485  1.00 69.47  ? 270 GLU C N   1 
ATOM   8610  C CA  . GLU D 1 274 ? 17.521  37.363  13.776  1.00 66.93  ? 270 GLU C CA  1 
ATOM   8611  C C   . GLU D 1 274 ? 16.481  37.998  14.689  1.00 60.78  ? 270 GLU C C   1 
ATOM   8612  O O   . GLU D 1 274 ? 15.347  37.530  14.766  1.00 70.09  ? 270 GLU C O   1 
ATOM   8613  C CB  . GLU D 1 274 ? 17.624  38.175  12.470  1.00 75.94  ? 270 GLU C CB  1 
ATOM   8614  C CG  . GLU D 1 274 ? 17.985  37.356  11.214  1.00 88.03  ? 270 GLU C CG  1 
ATOM   8615  C CD  . GLU D 1 274 ? 18.967  38.037  10.269  1.00 91.11  ? 270 GLU C CD  1 
ATOM   8616  O OE1 . GLU D 1 274 ? 18.580  38.317  9.115   1.00 91.66  ? 270 GLU C OE1 1 
ATOM   8617  O OE2 . GLU D 1 274 ? 20.136  38.265  10.663  1.00 90.03  ? 270 GLU C OE2 1 
ATOM   8618  N N   . TYR D 1 275 ? 16.868  39.076  15.360  1.00 58.89  ? 271 TYR C N   1 
ATOM   8619  C CA  . TYR D 1 275 ? 15.965  39.814  16.243  1.00 59.18  ? 271 TYR C CA  1 
ATOM   8620  C C   . TYR D 1 275 ? 15.222  40.909  15.482  1.00 69.62  ? 271 TYR C C   1 
ATOM   8621  O O   . TYR D 1 275 ? 15.839  41.785  14.882  1.00 80.73  ? 271 TYR C O   1 
ATOM   8622  C CB  . TYR D 1 275 ? 16.766  40.427  17.392  1.00 54.94  ? 271 TYR C CB  1 
ATOM   8623  C CG  . TYR D 1 275 ? 16.004  41.390  18.274  1.00 50.41  ? 271 TYR C CG  1 
ATOM   8624  C CD1 . TYR D 1 275 ? 15.142  40.929  19.263  1.00 51.44  ? 271 TYR C CD1 1 
ATOM   8625  C CD2 . TYR D 1 275 ? 16.170  42.767  18.141  1.00 54.05  ? 271 TYR C CD2 1 
ATOM   8626  C CE1 . TYR D 1 275 ? 14.453  41.811  20.083  1.00 51.48  ? 271 TYR C CE1 1 
ATOM   8627  C CE2 . TYR D 1 275 ? 15.488  43.657  18.956  1.00 53.14  ? 271 TYR C CE2 1 
ATOM   8628  C CZ  . TYR D 1 275 ? 14.630  43.175  19.924  1.00 52.86  ? 271 TYR C CZ  1 
ATOM   8629  O OH  . TYR D 1 275 ? 13.955  44.056  20.734  1.00 55.34  ? 271 TYR C OH  1 
ATOM   8630  N N   . GLY D 1 276 ? 13.893  40.843  15.503  1.00 82.01  ? 272 GLY C N   1 
ATOM   8631  C CA  . GLY D 1 276 ? 13.036  41.916  14.986  1.00 80.01  ? 272 GLY C CA  1 
ATOM   8632  C C   . GLY D 1 276 ? 12.528  42.736  16.164  1.00 85.18  ? 272 GLY C C   1 
ATOM   8633  O O   . GLY D 1 276 ? 12.462  42.228  17.284  1.00 102.50 ? 272 GLY C O   1 
ATOM   8634  N N   . ASN D 1 277 ? 12.184  44.003  15.934  1.00 83.28  ? 273 ASN C N   1 
ATOM   8635  C CA  . ASN D 1 277 ? 11.700  44.870  17.015  1.00 83.02  ? 273 ASN C CA  1 
ATOM   8636  C C   . ASN D 1 277 ? 10.205  44.701  17.278  1.00 86.00  ? 273 ASN C C   1 
ATOM   8637  O O   . ASN D 1 277 ? 9.388   45.594  16.980  1.00 95.81  ? 273 ASN C O   1 
ATOM   8638  C CB  . ASN D 1 277 ? 12.040  46.333  16.727  1.00 87.30  ? 273 ASN C CB  1 
ATOM   8639  C CG  . ASN D 1 277 ? 13.532  46.587  16.723  1.00 83.91  ? 273 ASN C CG  1 
ATOM   8640  O OD1 . ASN D 1 277 ? 14.292  45.883  16.053  1.00 72.89  ? 273 ASN C OD1 1 
ATOM   8641  N ND2 . ASN D 1 277 ? 13.963  47.590  17.480  1.00 84.55  ? 273 ASN C ND2 1 
ATOM   8642  N N   . CYS D 1 278 ? 9.881   43.542  17.859  1.00 90.58  ? 274 CYS C N   1 
ATOM   8643  C CA  . CYS D 1 278 ? 8.507   43.128  18.122  1.00 86.86  ? 274 CYS C CA  1 
ATOM   8644  C C   . CYS D 1 278 ? 8.351   42.728  19.591  1.00 75.07  ? 274 CYS C C   1 
ATOM   8645  O O   . CYS D 1 278 ? 9.338   42.566  20.315  1.00 71.98  ? 274 CYS C O   1 
ATOM   8646  C CB  . CYS D 1 278 ? 8.132   41.961  17.182  1.00 94.79  ? 274 CYS C CB  1 
ATOM   8647  S SG  . CYS D 1 278 ? 7.531   40.425  17.951  1.00 122.89 ? 274 CYS C SG  1 
ATOM   8648  N N   . ASN D 1 279 ? 7.102   42.588  20.024  1.00 73.28  ? 275 ASN C N   1 
ATOM   8649  C CA  . ASN D 1 279 ? 6.783   42.117  21.370  1.00 68.08  ? 275 ASN C CA  1 
ATOM   8650  C C   . ASN D 1 279 ? 5.762   40.981  21.300  1.00 68.29  ? 275 ASN C C   1 
ATOM   8651  O O   . ASN D 1 279 ? 4.786   41.067  20.550  1.00 74.16  ? 275 ASN C O   1 
ATOM   8652  C CB  . ASN D 1 279 ? 6.238   43.268  22.221  1.00 63.15  ? 275 ASN C CB  1 
ATOM   8653  C CG  . ASN D 1 279 ? 6.059   42.887  23.679  1.00 68.38  ? 275 ASN C CG  1 
ATOM   8654  O OD1 . ASN D 1 279 ? 6.786   42.046  24.214  1.00 79.45  ? 275 ASN C OD1 1 
ATOM   8655  N ND2 . ASN D 1 279 ? 5.087   43.509  24.333  1.00 62.18  ? 275 ASN C ND2 1 
ATOM   8656  N N   . THR D 1 280 ? 5.982   39.919  22.074  1.00 66.41  ? 276 THR C N   1 
ATOM   8657  C CA  . THR D 1 280 ? 5.034   38.796  22.116  1.00 60.07  ? 276 THR C CA  1 
ATOM   8658  C C   . THR D 1 280 ? 4.851   38.265  23.531  1.00 53.43  ? 276 THR C C   1 
ATOM   8659  O O   . THR D 1 280 ? 5.565   38.659  24.460  1.00 42.61  ? 276 THR C O   1 
ATOM   8660  C CB  . THR D 1 280 ? 5.415   37.649  21.167  1.00 59.06  ? 276 THR C CB  1 
ATOM   8661  O OG1 . THR D 1 280 ? 6.743   37.234  21.447  1.00 55.61  ? 276 THR C OG1 1 
ATOM   8662  C CG2 . THR D 1 280 ? 5.304   38.085  19.711  1.00 65.40  ? 276 THR C CG2 1 
ATOM   8663  N N   . ARG D 1 281 ? 3.848   37.406  23.680  1.00 56.79  ? 277 ARG C N   1 
ATOM   8664  C CA  . ARG D 1 281 ? 3.625   36.659  24.912  1.00 56.39  ? 277 ARG C CA  1 
ATOM   8665  C C   . ARG D 1 281 ? 4.116   35.223  24.756  1.00 49.65  ? 277 ARG C C   1 
ATOM   8666  O O   . ARG D 1 281 ? 4.092   34.458  25.720  1.00 49.89  ? 277 ARG C O   1 
ATOM   8667  C CB  . ARG D 1 281 ? 2.139   36.619  25.275  1.00 65.93  ? 277 ARG C CB  1 
ATOM   8668  C CG  . ARG D 1 281 ? 1.339   37.890  25.027  1.00 76.83  ? 277 ARG C CG  1 
ATOM   8669  C CD  . ARG D 1 281 ? 0.174   38.002  25.999  1.00 85.18  ? 277 ARG C CD  1 
ATOM   8670  N NE  . ARG D 1 281 ? -0.546  36.736  26.184  1.00 91.64  ? 277 ARG C NE  1 
ATOM   8671  C CZ  . ARG D 1 281 ? -1.711  36.610  26.817  1.00 95.50  ? 277 ARG C CZ  1 
ATOM   8672  N NH1 . ARG D 1 281 ? -2.323  37.666  27.350  1.00 97.25  ? 277 ARG C NH1 1 
ATOM   8673  N NH2 . ARG D 1 281 ? -2.268  35.408  26.920  1.00 87.05  ? 277 ARG C NH2 1 
ATOM   8674  N N   . CYS D 1 282 ? 4.538   34.863  23.544  1.00 40.16  ? 278 CYS C N   1 
ATOM   8675  C CA  . CYS D 1 282 ? 4.941   33.502  23.232  1.00 42.06  ? 278 CYS C CA  1 
ATOM   8676  C C   . CYS D 1 282 ? 6.009   33.483  22.134  1.00 45.27  ? 278 CYS C C   1 
ATOM   8677  O O   . CYS D 1 282 ? 5.731   33.819  20.982  1.00 43.57  ? 278 CYS C O   1 
ATOM   8678  C CB  . CYS D 1 282 ? 3.720   32.686  22.794  1.00 43.20  ? 278 CYS C CB  1 
ATOM   8679  S SG  . CYS D 1 282 ? 4.099   31.005  22.259  1.00 49.15  ? 278 CYS C SG  1 
ATOM   8680  N N   . GLN D 1 283 ? 7.218   33.062  22.498  1.00 42.54  ? 279 GLN C N   1 
ATOM   8681  C CA  . GLN D 1 283 ? 8.349   33.022  21.577  1.00 39.30  ? 279 GLN C CA  1 
ATOM   8682  C C   . GLN D 1 283 ? 8.755   31.596  21.228  1.00 41.26  ? 279 GLN C C   1 
ATOM   8683  O O   . GLN D 1 283 ? 8.782   30.713  22.082  1.00 37.89  ? 279 GLN C O   1 
ATOM   8684  C CB  . GLN D 1 283 ? 9.552   33.743  22.183  1.00 39.96  ? 279 GLN C CB  1 
ATOM   8685  C CG  . GLN D 1 283 ? 10.761  33.832  21.259  1.00 39.70  ? 279 GLN C CG  1 
ATOM   8686  C CD  . GLN D 1 283 ? 10.467  34.631  20.001  1.00 38.80  ? 279 GLN C CD  1 
ATOM   8687  O OE1 . GLN D 1 283 ? 10.075  35.796  20.074  1.00 34.48  ? 279 GLN C OE1 1 
ATOM   8688  N NE2 . GLN D 1 283 ? 10.647  34.006  18.841  1.00 36.95  ? 279 GLN C NE2 1 
ATOM   8689  N N   . THR D 1 284 ? 9.100   31.400  19.963  1.00 47.57  ? 280 THR C N   1 
ATOM   8690  C CA  . THR D 1 284 ? 9.557   30.119  19.450  1.00 52.33  ? 280 THR C CA  1 
ATOM   8691  C C   . THR D 1 284 ? 10.948  30.318  18.817  1.00 50.93  ? 280 THR C C   1 
ATOM   8692  O O   . THR D 1 284 ? 11.283  31.431  18.413  1.00 49.64  ? 280 THR C O   1 
ATOM   8693  C CB  . THR D 1 284 ? 8.525   29.571  18.439  1.00 54.36  ? 280 THR C CB  1 
ATOM   8694  O OG1 . THR D 1 284 ? 7.662   28.634  19.092  1.00 63.47  ? 280 THR C OG1 1 
ATOM   8695  C CG2 . THR D 1 284 ? 9.190   28.900  17.254  1.00 48.59  ? 280 THR C CG2 1 
ATOM   8696  N N   . PRO D 1 285 ? 11.769  29.251  18.749  1.00 50.23  ? 281 PRO C N   1 
ATOM   8697  C CA  . PRO D 1 285 ? 13.108  29.352  18.149  1.00 52.72  ? 281 PRO C CA  1 
ATOM   8698  C C   . PRO D 1 285 ? 13.124  29.728  16.660  1.00 53.66  ? 281 PRO C C   1 
ATOM   8699  O O   . PRO D 1 285 ? 14.161  30.154  16.153  1.00 55.67  ? 281 PRO C O   1 
ATOM   8700  C CB  . PRO D 1 285 ? 13.685  27.939  18.336  1.00 55.56  ? 281 PRO C CB  1 
ATOM   8701  C CG  . PRO D 1 285 ? 12.916  27.359  19.470  1.00 51.48  ? 281 PRO C CG  1 
ATOM   8702  C CD  . PRO D 1 285 ? 11.532  27.907  19.304  1.00 52.13  ? 281 PRO C CD  1 
ATOM   8703  N N   . ILE D 1 286 ? 11.996  29.549  15.973  1.00 53.72  ? 282 ILE C N   1 
ATOM   8704  C CA  . ILE D 1 286 ? 11.853  29.940  14.563  1.00 48.79  ? 282 ILE C CA  1 
ATOM   8705  C C   . ILE D 1 286 ? 10.935  31.166  14.344  1.00 51.70  ? 282 ILE C C   1 
ATOM   8706  O O   . ILE D 1 286 ? 10.796  31.632  13.213  1.00 63.47  ? 282 ILE C O   1 
ATOM   8707  C CB  . ILE D 1 286 ? 11.419  28.748  13.671  1.00 46.54  ? 282 ILE C CB  1 
ATOM   8708  C CG1 . ILE D 1 286 ? 10.097  28.128  14.141  1.00 47.16  ? 282 ILE C CG1 1 
ATOM   8709  C CG2 . ILE D 1 286 ? 12.513  27.689  13.661  1.00 44.28  ? 282 ILE C CG2 1 
ATOM   8710  C CD1 . ILE D 1 286 ? 9.423   27.266  13.086  1.00 43.71  ? 282 ILE C CD1 1 
ATOM   8711  N N   . GLY D 1 287 ? 10.336  31.700  15.410  1.00 47.55  ? 283 GLY C N   1 
ATOM   8712  C CA  . GLY D 1 287 ? 9.513   32.915  15.305  1.00 46.97  ? 283 GLY C CA  1 
ATOM   8713  C C   . GLY D 1 287 ? 8.523   33.093  16.448  1.00 49.33  ? 283 GLY C C   1 
ATOM   8714  O O   . GLY D 1 287 ? 8.231   32.148  17.167  1.00 50.94  ? 283 GLY C O   1 
ATOM   8715  N N   . ALA D 1 288 ? 8.001   34.306  16.609  1.00 44.79  ? 284 ALA C N   1 
ATOM   8716  C CA  . ALA D 1 288 ? 7.058   34.612  17.688  1.00 44.32  ? 284 ALA C CA  1 
ATOM   8717  C C   . ALA D 1 288 ? 5.608   34.326  17.271  1.00 52.60  ? 284 ALA C C   1 
ATOM   8718  O O   . ALA D 1 288 ? 5.302   34.261  16.081  1.00 52.37  ? 284 ALA C O   1 
ATOM   8719  C CB  . ALA D 1 288 ? 7.211   36.058  18.126  1.00 39.63  ? 284 ALA C CB  1 
ATOM   8720  N N   . ILE D 1 289 ? 4.729   34.167  18.262  1.00 53.57  ? 285 ILE C N   1 
ATOM   8721  C CA  . ILE D 1 289 ? 3.315   33.843  18.033  1.00 50.21  ? 285 ILE C CA  1 
ATOM   8722  C C   . ILE D 1 289 ? 2.379   34.838  18.720  1.00 50.52  ? 285 ILE C C   1 
ATOM   8723  O O   . ILE D 1 289 ? 2.525   35.121  19.908  1.00 51.90  ? 285 ILE C O   1 
ATOM   8724  C CB  . ILE D 1 289 ? 2.966   32.448  18.581  1.00 53.76  ? 285 ILE C CB  1 
ATOM   8725  C CG1 . ILE D 1 289 ? 3.757   31.358  17.859  1.00 53.37  ? 285 ILE C CG1 1 
ATOM   8726  C CG2 . ILE D 1 289 ? 1.472   32.180  18.466  1.00 54.05  ? 285 ILE C CG2 1 
ATOM   8727  C CD1 . ILE D 1 289 ? 3.576   29.989  18.482  1.00 52.78  ? 285 ILE C CD1 1 
ATOM   8728  N N   . ASN D 1 290 ? 1.424   35.366  17.958  1.00 53.23  ? 286 ASN C N   1 
ATOM   8729  C CA  . ASN D 1 290 ? 0.333   36.178  18.495  1.00 56.62  ? 286 ASN C CA  1 
ATOM   8730  C C   . ASN D 1 290 ? -1.005  35.528  18.153  1.00 58.98  ? 286 ASN C C   1 
ATOM   8731  O O   . ASN D 1 290 ? -1.471  35.612  17.014  1.00 61.01  ? 286 ASN C O   1 
ATOM   8732  C CB  . ASN D 1 290 ? 0.404   37.596  17.916  1.00 59.70  ? 286 ASN C CB  1 
ATOM   8733  C CG  . ASN D 1 290 ? -0.554  38.566  18.593  1.00 61.49  ? 286 ASN C CG  1 
ATOM   8734  O OD1 . ASN D 1 290 ? -1.018  38.335  19.709  1.00 59.58  ? 286 ASN C OD1 1 
ATOM   8735  N ND2 . ASN D 1 290 ? -0.853  39.666  17.911  1.00 74.97  ? 286 ASN C ND2 1 
ATOM   8736  N N   . SER D 1 291 ? -1.620  34.880  19.140  1.00 60.94  ? 287 SER C N   1 
ATOM   8737  C CA  . SER D 1 291 ? -2.887  34.179  18.918  1.00 57.56  ? 287 SER C CA  1 
ATOM   8738  C C   . SER D 1 291 ? -3.688  34.006  20.194  1.00 49.10  ? 287 SER C C   1 
ATOM   8739  O O   . SER D 1 291 ? -3.144  33.982  21.291  1.00 51.79  ? 287 SER C O   1 
ATOM   8740  C CB  . SER D 1 291 ? -2.656  32.794  18.304  1.00 56.51  ? 287 SER C CB  1 
ATOM   8741  O OG  . SER D 1 291 ? -3.882  32.221  17.888  1.00 55.65  ? 287 SER C OG  1 
ATOM   8742  N N   . SER D 1 292 ? -4.994  33.874  20.023  1.00 48.74  ? 288 SER C N   1 
ATOM   8743  C CA  . SER D 1 292 ? -5.880  33.475  21.106  1.00 48.56  ? 288 SER C CA  1 
ATOM   8744  C C   . SER D 1 292 ? -6.275  31.994  20.949  1.00 40.79  ? 288 SER C C   1 
ATOM   8745  O O   . SER D 1 292 ? -6.901  31.431  21.850  1.00 41.27  ? 288 SER C O   1 
ATOM   8746  C CB  . SER D 1 292 ? -7.099  34.408  21.164  1.00 50.65  ? 288 SER C CB  1 
ATOM   8747  O OG  . SER D 1 292 ? -7.674  34.604  19.882  1.00 58.72  ? 288 SER C OG  1 
ATOM   8748  N N   . MET D 1 293 ? -5.873  31.364  19.834  1.00 36.63  ? 289 MET C N   1 
ATOM   8749  C CA  . MET D 1 293 ? -6.233  29.972  19.544  1.00 38.77  ? 289 MET C CA  1 
ATOM   8750  C C   . MET D 1 293 ? -5.658  29.000  20.572  1.00 39.34  ? 289 MET C C   1 
ATOM   8751  O O   . MET D 1 293 ? -4.565  29.219  21.096  1.00 38.87  ? 289 MET C O   1 
ATOM   8752  C CB  . MET D 1 293 ? -5.753  29.537  18.152  1.00 46.68  ? 289 MET C CB  1 
ATOM   8753  C CG  . MET D 1 293 ? -6.381  30.264  16.972  1.00 53.97  ? 289 MET C CG  1 
ATOM   8754  S SD  . MET D 1 293 ? -8.182  30.158  16.898  1.00 61.45  ? 289 MET C SD  1 
ATOM   8755  C CE  . MET D 1 293 ? -8.656  31.620  17.821  1.00 57.72  ? 289 MET C CE  1 
ATOM   8756  N N   . PRO D 1 294 ? -6.396  27.915  20.856  1.00 37.72  ? 290 PRO C N   1 
ATOM   8757  C CA  . PRO D 1 294 ? -6.004  26.985  21.908  1.00 34.67  ? 290 PRO C CA  1 
ATOM   8758  C C   . PRO D 1 294 ? -4.857  26.050  21.533  1.00 33.68  ? 290 PRO C C   1 
ATOM   8759  O O   . PRO D 1 294 ? -4.171  25.570  22.427  1.00 33.61  ? 290 PRO C O   1 
ATOM   8760  C CB  . PRO D 1 294 ? -7.288  26.191  22.170  1.00 36.89  ? 290 PRO C CB  1 
ATOM   8761  C CG  . PRO D 1 294 ? -8.035  26.242  20.885  1.00 39.15  ? 290 PRO C CG  1 
ATOM   8762  C CD  . PRO D 1 294 ? -7.688  27.550  20.241  1.00 40.50  ? 290 PRO C CD  1 
ATOM   8763  N N   . PHE D 1 295 ? -4.647  25.798  20.239  1.00 35.25  ? 291 PHE C N   1 
ATOM   8764  C CA  . PHE D 1 295 ? -3.615  24.853  19.789  1.00 35.09  ? 291 PHE C CA  1 
ATOM   8765  C C   . PHE D 1 295 ? -2.684  25.419  18.716  1.00 35.58  ? 291 PHE C C   1 
ATOM   8766  O O   . PHE D 1 295 ? -3.063  26.323  17.973  1.00 35.10  ? 291 PHE C O   1 
ATOM   8767  C CB  . PHE D 1 295 ? -4.272  23.587  19.247  1.00 36.86  ? 291 PHE C CB  1 
ATOM   8768  C CG  . PHE D 1 295 ? -5.236  22.954  20.203  1.00 40.31  ? 291 PHE C CG  1 
ATOM   8769  C CD1 . PHE D 1 295 ? -6.605  23.034  19.989  1.00 44.44  ? 291 PHE C CD1 1 
ATOM   8770  C CD2 . PHE D 1 295 ? -4.777  22.286  21.324  1.00 42.72  ? 291 PHE C CD2 1 
ATOM   8771  C CE1 . PHE D 1 295 ? -7.497  22.455  20.875  1.00 45.28  ? 291 PHE C CE1 1 
ATOM   8772  C CE2 . PHE D 1 295 ? -5.662  21.699  22.213  1.00 42.66  ? 291 PHE C CE2 1 
ATOM   8773  C CZ  . PHE D 1 295 ? -7.024  21.785  21.989  1.00 45.11  ? 291 PHE C CZ  1 
ATOM   8774  N N   . HIS D 1 296 ? -1.465  24.877  18.648  1.00 36.29  ? 292 HIS C N   1 
ATOM   8775  C CA  . HIS D 1 296 ? -0.511  25.224  17.591  1.00 36.93  ? 292 HIS C CA  1 
ATOM   8776  C C   . HIS D 1 296 ? 0.333   24.049  17.175  1.00 40.49  ? 292 HIS C C   1 
ATOM   8777  O O   . HIS D 1 296 ? 0.433   23.060  17.907  1.00 40.93  ? 292 HIS C O   1 
ATOM   8778  C CB  . HIS D 1 296 ? 0.366   26.412  18.010  1.00 39.87  ? 292 HIS C CB  1 
ATOM   8779  C CG  . HIS D 1 296 ? 1.527   26.053  18.920  1.00 43.18  ? 292 HIS C CG  1 
ATOM   8780  N ND1 . HIS D 1 296 ? 1.424   26.055  20.258  1.00 45.19  ? 292 HIS C ND1 1 
ATOM   8781  C CD2 . HIS D 1 296 ? 2.852   25.720  18.631  1.00 44.26  ? 292 HIS C CD2 1 
ATOM   8782  C CE1 . HIS D 1 296 ? 2.616   25.720  20.798  1.00 47.83  ? 292 HIS C CE1 1 
ATOM   8783  N NE2 . HIS D 1 296 ? 3.484   25.516  19.799  1.00 44.26  ? 292 HIS C NE2 1 
ATOM   8784  N N   . ASN D 1 297 ? 0.929   24.140  15.981  1.00 39.90  ? 293 ASN C N   1 
ATOM   8785  C CA  . ASN D 1 297 ? 1.858   23.113  15.482  1.00 38.08  ? 293 ASN C CA  1 
ATOM   8786  C C   . ASN D 1 297 ? 3.208   23.675  15.008  1.00 40.31  ? 293 ASN C C   1 
ATOM   8787  O O   . ASN D 1 297 ? 3.940   23.014  14.271  1.00 42.57  ? 293 ASN C O   1 
ATOM   8788  C CB  . ASN D 1 297 ? 1.200   22.303  14.367  1.00 37.38  ? 293 ASN C CB  1 
ATOM   8789  C CG  . ASN D 1 297 ? 1.001   23.101  13.092  1.00 40.26  ? 293 ASN C CG  1 
ATOM   8790  O OD1 . ASN D 1 297 ? 1.014   24.339  13.091  1.00 44.14  ? 293 ASN C OD1 1 
ATOM   8791  N ND2 . ASN D 1 297 ? 0.797   22.386  11.991  1.00 35.68  ? 293 ASN C ND2 1 
ATOM   8792  N N   . ILE D 1 298 ? 3.525   24.889  15.446  1.00 39.58  ? 294 ILE C N   1 
ATOM   8793  C CA  . ILE D 1 298 ? 4.775   25.571  15.096  1.00 42.42  ? 294 ILE C CA  1 
ATOM   8794  C C   . ILE D 1 298 ? 6.041   24.853  15.588  1.00 46.59  ? 294 ILE C C   1 
ATOM   8795  O O   . ILE D 1 298 ? 6.863   24.423  14.783  1.00 50.94  ? 294 ILE C O   1 
ATOM   8796  C CB  . ILE D 1 298 ? 4.823   27.021  15.659  1.00 42.88  ? 294 ILE C CB  1 
ATOM   8797  C CG1 . ILE D 1 298 ? 3.522   27.798  15.382  1.00 40.66  ? 294 ILE C CG1 1 
ATOM   8798  C CG2 . ILE D 1 298 ? 6.020   27.766  15.092  1.00 43.11  ? 294 ILE C CG2 1 
ATOM   8799  C CD1 . ILE D 1 298 ? 2.925   27.574  14.013  1.00 34.62  ? 294 ILE C CD1 1 
ATOM   8800  N N   . HIS D 1 299 ? 6.200   24.745  16.907  1.00 48.34  ? 295 HIS C N   1 
ATOM   8801  C CA  . HIS D 1 299 ? 7.460   24.286  17.508  1.00 48.95  ? 295 HIS C CA  1 
ATOM   8802  C C   . HIS D 1 299 ? 7.282   23.961  18.971  1.00 51.56  ? 295 HIS C C   1 
ATOM   8803  O O   . HIS D 1 299 ? 6.578   24.683  19.679  1.00 52.39  ? 295 HIS C O   1 
ATOM   8804  C CB  . HIS D 1 299 ? 8.527   25.372  17.368  1.00 52.36  ? 295 HIS C CB  1 
ATOM   8805  C CG  . HIS D 1 299 ? 9.943   24.846  17.393  1.00 51.74  ? 295 HIS C CG  1 
ATOM   8806  N ND1 . HIS D 1 299 ? 10.638  24.682  18.534  1.00 49.78  ? 295 HIS C ND1 1 
ATOM   8807  C CD2 . HIS D 1 299 ? 10.785  24.447  16.357  1.00 52.65  ? 295 HIS C CD2 1 
ATOM   8808  C CE1 . HIS D 1 299 ? 11.859  24.196  18.249  1.00 52.72  ? 295 HIS C CE1 1 
ATOM   8809  N NE2 . HIS D 1 299 ? 11.950  24.055  16.914  1.00 53.62  ? 295 HIS C NE2 1 
ATOM   8810  N N   . PRO D 1 300 ? 7.914   22.874  19.453  1.00 48.69  ? 296 PRO C N   1 
ATOM   8811  C CA  . PRO D 1 300 ? 7.755   22.493  20.862  1.00 44.46  ? 296 PRO C CA  1 
ATOM   8812  C C   . PRO D 1 300 ? 8.494   23.369  21.880  1.00 42.52  ? 296 PRO C C   1 
ATOM   8813  O O   . PRO D 1 300 ? 8.015   23.537  23.000  1.00 42.12  ? 296 PRO C O   1 
ATOM   8814  C CB  . PRO D 1 300 ? 8.308   21.062  20.904  1.00 47.55  ? 296 PRO C CB  1 
ATOM   8815  C CG  . PRO D 1 300 ? 9.237   20.968  19.746  1.00 48.53  ? 296 PRO C CG  1 
ATOM   8816  C CD  . PRO D 1 300 ? 8.665   21.861  18.687  1.00 50.19  ? 296 PRO C CD  1 
ATOM   8817  N N   . LEU D 1 301 ? 9.642   23.923  21.501  1.00 41.92  ? 297 LEU C N   1 
ATOM   8818  C CA  . LEU D 1 301 ? 10.511  24.623  22.458  1.00 40.78  ? 297 LEU C CA  1 
ATOM   8819  C C   . LEU D 1 301 ? 10.109  26.080  22.637  1.00 39.22  ? 297 LEU C C   1 
ATOM   8820  O O   . LEU D 1 301 ? 10.851  26.985  22.286  1.00 37.68  ? 297 LEU C O   1 
ATOM   8821  C CB  . LEU D 1 301 ? 11.981  24.526  22.022  1.00 37.34  ? 297 LEU C CB  1 
ATOM   8822  C CG  . LEU D 1 301 ? 12.478  23.111  21.712  1.00 40.39  ? 297 LEU C CG  1 
ATOM   8823  C CD1 . LEU D 1 301 ? 13.970  23.133  21.417  1.00 35.28  ? 297 LEU C CD1 1 
ATOM   8824  C CD2 . LEU D 1 301 ? 12.150  22.134  22.837  1.00 36.40  ? 297 LEU C CD2 1 
ATOM   8825  N N   . THR D 1 302 ? 8.942   26.297  23.225  1.00 42.29  ? 298 THR C N   1 
ATOM   8826  C CA  . THR D 1 302 ? 8.376   27.636  23.336  1.00 41.11  ? 298 THR C CA  1 
ATOM   8827  C C   . THR D 1 302 ? 8.645   28.268  24.701  1.00 39.61  ? 298 THR C C   1 
ATOM   8828  O O   . THR D 1 302 ? 8.843   27.563  25.689  1.00 46.45  ? 298 THR C O   1 
ATOM   8829  C CB  . THR D 1 302 ? 6.865   27.584  23.094  1.00 41.76  ? 298 THR C CB  1 
ATOM   8830  O OG1 . THR D 1 302 ? 6.262   26.712  24.059  1.00 40.75  ? 298 THR C OG1 1 
ATOM   8831  C CG2 . THR D 1 302 ? 6.579   27.062  21.696  1.00 38.09  ? 298 THR C CG2 1 
ATOM   8832  N N   . ILE D 1 303 ? 8.667   29.597  24.737  1.00 39.11  ? 299 ILE C N   1 
ATOM   8833  C CA  . ILE D 1 303 ? 8.846   30.353  25.977  1.00 42.29  ? 299 ILE C CA  1 
ATOM   8834  C C   . ILE D 1 303 ? 7.770   31.426  26.040  1.00 46.36  ? 299 ILE C C   1 
ATOM   8835  O O   . ILE D 1 303 ? 7.712   32.287  25.164  1.00 54.54  ? 299 ILE C O   1 
ATOM   8836  C CB  . ILE D 1 303 ? 10.234  31.031  26.067  1.00 41.80  ? 299 ILE C CB  1 
ATOM   8837  C CG1 . ILE D 1 303 ? 11.356  30.027  25.800  1.00 42.46  ? 299 ILE C CG1 1 
ATOM   8838  C CG2 . ILE D 1 303 ? 10.438  31.666  27.439  1.00 34.83  ? 299 ILE C CG2 1 
ATOM   8839  C CD1 . ILE D 1 303 ? 12.744  30.621  25.937  1.00 47.63  ? 299 ILE C CD1 1 
ATOM   8840  N N   . GLY D 1 304 ? 6.920   31.371  27.066  1.00 51.62  ? 300 GLY C N   1 
ATOM   8841  C CA  . GLY D 1 304 ? 5.792   32.298  27.191  1.00 50.31  ? 300 GLY C CA  1 
ATOM   8842  C C   . GLY D 1 304 ? 4.473   31.621  27.534  1.00 51.99  ? 300 GLY C C   1 
ATOM   8843  O O   . GLY D 1 304 ? 4.444   30.436  27.873  1.00 44.32  ? 300 GLY C O   1 
ATOM   8844  N N   . GLU D 1 305 ? 3.384   32.387  27.465  1.00 52.51  ? 301 GLU C N   1 
ATOM   8845  C CA  . GLU D 1 305 ? 2.029   31.841  27.561  1.00 51.50  ? 301 GLU C CA  1 
ATOM   8846  C C   . GLU D 1 305 ? 1.612   31.420  26.166  1.00 48.35  ? 301 GLU C C   1 
ATOM   8847  O O   . GLU D 1 305 ? 1.181   32.252  25.369  1.00 51.52  ? 301 GLU C O   1 
ATOM   8848  C CB  . GLU D 1 305 ? 1.035   32.872  28.094  1.00 58.78  ? 301 GLU C CB  1 
ATOM   8849  C CG  . GLU D 1 305 ? 1.170   33.152  29.577  1.00 66.78  ? 301 GLU C CG  1 
ATOM   8850  C CD  . GLU D 1 305 ? 0.055   34.045  30.094  1.00 76.50  ? 301 GLU C CD  1 
ATOM   8851  O OE1 . GLU D 1 305 ? -1.046  33.504  30.323  1.00 66.20  ? 301 GLU C OE1 1 
ATOM   8852  O OE2 . GLU D 1 305 ? 0.273   35.271  30.271  1.00 94.35  ? 301 GLU C OE2 1 
ATOM   8853  N N   . CYS D 1 306 ? 1.739   30.130  25.873  1.00 45.62  ? 302 CYS C N   1 
ATOM   8854  C CA  . CYS D 1 306 ? 1.549   29.635  24.516  1.00 48.73  ? 302 CYS C CA  1 
ATOM   8855  C C   . CYS D 1 306 ? 0.347   28.698  24.393  1.00 45.68  ? 302 CYS C C   1 
ATOM   8856  O O   . CYS D 1 306 ? -0.100  28.124  25.378  1.00 48.34  ? 302 CYS C O   1 
ATOM   8857  C CB  . CYS D 1 306 ? 2.812   28.912  24.047  1.00 52.19  ? 302 CYS C CB  1 
ATOM   8858  S SG  . CYS D 1 306 ? 4.284   29.961  24.001  1.00 66.61  ? 302 CYS C SG  1 
ATOM   8859  N N   . PRO D 1 307 ? -0.184  28.543  23.170  1.00 44.05  ? 303 PRO C N   1 
ATOM   8860  C CA  . PRO D 1 307 ? -1.169  27.493  22.934  1.00 44.90  ? 303 PRO C CA  1 
ATOM   8861  C C   . PRO D 1 307 ? -0.543  26.116  23.127  1.00 39.72  ? 303 PRO C C   1 
ATOM   8862  O O   . PRO D 1 307 ? 0.676   25.997  23.174  1.00 37.73  ? 303 PRO C O   1 
ATOM   8863  C CB  . PRO D 1 307 ? -1.568  27.701  21.465  1.00 47.35  ? 303 PRO C CB  1 
ATOM   8864  C CG  . PRO D 1 307 ? -1.214  29.118  21.172  1.00 48.00  ? 303 PRO C CG  1 
ATOM   8865  C CD  . PRO D 1 307 ? 0.016   29.386  21.979  1.00 45.87  ? 303 PRO C CD  1 
ATOM   8866  N N   . LYS D 1 308 ? -1.370  25.086  23.227  1.00 35.50  ? 304 LYS C N   1 
ATOM   8867  C CA  . LYS D 1 308 ? -0.867  23.744  23.458  1.00 33.98  ? 304 LYS C CA  1 
ATOM   8868  C C   . LYS D 1 308 ? -0.327  23.143  22.158  1.00 32.55  ? 304 LYS C C   1 
ATOM   8869  O O   . LYS D 1 308 ? -1.026  23.102  21.145  1.00 29.77  ? 304 LYS C O   1 
ATOM   8870  C CB  . LYS D 1 308 ? -1.963  22.869  24.067  1.00 34.99  ? 304 LYS C CB  1 
ATOM   8871  C CG  . LYS D 1 308 ? -2.469  23.392  25.406  1.00 35.37  ? 304 LYS C CG  1 
ATOM   8872  C CD  . LYS D 1 308 ? -1.451  23.188  26.522  1.00 37.62  ? 304 LYS C CD  1 
ATOM   8873  C CE  . LYS D 1 308 ? -1.446  24.339  27.518  1.00 40.11  ? 304 LYS C CE  1 
ATOM   8874  N NZ  . LYS D 1 308 ? -2.811  24.671  28.008  1.00 44.10  ? 304 LYS C NZ  1 
ATOM   8875  N N   . TYR D 1 309 ? 0.926   22.695  22.195  1.00 33.48  ? 305 TYR C N   1 
ATOM   8876  C CA  . TYR D 1 309 ? 1.571   22.110  21.028  1.00 33.22  ? 305 TYR C CA  1 
ATOM   8877  C C   . TYR D 1 309 ? 0.901   20.798  20.680  1.00 33.86  ? 305 TYR C C   1 
ATOM   8878  O O   . TYR D 1 309 ? 0.639   19.973  21.553  1.00 43.61  ? 305 TYR C O   1 
ATOM   8879  C CB  . TYR D 1 309 ? 3.062   21.875  21.275  1.00 35.84  ? 305 TYR C CB  1 
ATOM   8880  C CG  . TYR D 1 309 ? 3.818   21.404  20.044  1.00 40.14  ? 305 TYR C CG  1 
ATOM   8881  C CD1 . TYR D 1 309 ? 3.820   22.158  18.872  1.00 37.81  ? 305 TYR C CD1 1 
ATOM   8882  C CD2 . TYR D 1 309 ? 4.529   20.203  20.051  1.00 42.79  ? 305 TYR C CD2 1 
ATOM   8883  C CE1 . TYR D 1 309 ? 4.501   21.729  17.744  1.00 40.05  ? 305 TYR C CE1 1 
ATOM   8884  C CE2 . TYR D 1 309 ? 5.216   19.768  18.926  1.00 44.43  ? 305 TYR C CE2 1 
ATOM   8885  C CZ  . TYR D 1 309 ? 5.198   20.537  17.775  1.00 44.37  ? 305 TYR C CZ  1 
ATOM   8886  O OH  . TYR D 1 309 ? 5.880   20.118  16.655  1.00 45.04  ? 305 TYR C OH  1 
ATOM   8887  N N   . VAL D 1 310 ? 0.638   20.607  19.397  1.00 37.25  ? 306 VAL C N   1 
ATOM   8888  C CA  . VAL D 1 310 ? -0.157  19.480  18.939  1.00 41.02  ? 306 VAL C CA  1 
ATOM   8889  C C   . VAL D 1 310 ? 0.414   19.005  17.604  1.00 40.57  ? 306 VAL C C   1 
ATOM   8890  O O   . VAL D 1 310 ? 1.040   19.782  16.889  1.00 46.68  ? 306 VAL C O   1 
ATOM   8891  C CB  . VAL D 1 310 ? -1.641  19.900  18.844  1.00 43.74  ? 306 VAL C CB  1 
ATOM   8892  C CG1 . VAL D 1 310 ? -2.104  19.992  17.398  1.00 40.62  ? 306 VAL C CG1 1 
ATOM   8893  C CG2 . VAL D 1 310 ? -2.509  18.935  19.635  1.00 45.16  ? 306 VAL C CG2 1 
ATOM   8894  N N   . LYS D 1 311 ? 0.242   17.727  17.290  1.00 43.23  ? 307 LYS C N   1 
ATOM   8895  C CA  . LYS D 1 311 ? 0.809   17.158  16.070  1.00 48.11  ? 307 LYS C CA  1 
ATOM   8896  C C   . LYS D 1 311 ? -0.306  16.951  15.062  1.00 46.96  ? 307 LYS C C   1 
ATOM   8897  O O   . LYS D 1 311 ? -0.816  15.849  14.890  1.00 54.76  ? 307 LYS C O   1 
ATOM   8898  C CB  . LYS D 1 311 ? 1.539   15.848  16.373  1.00 58.28  ? 307 LYS C CB  1 
ATOM   8899  C CG  . LYS D 1 311 ? 2.532   15.423  15.295  1.00 67.28  ? 307 LYS C CG  1 
ATOM   8900  C CD  . LYS D 1 311 ? 2.007   14.269  14.450  1.00 75.86  ? 307 LYS C CD  1 
ATOM   8901  C CE  . LYS D 1 311 ? 3.045   13.780  13.449  1.00 74.87  ? 307 LYS C CE  1 
ATOM   8902  N NZ  . LYS D 1 311 ? 4.190   13.090  14.107  1.00 65.75  ? 307 LYS C NZ  1 
ATOM   8903  N N   . SER D 1 312 ? -0.684  18.042  14.409  1.00 47.14  ? 308 SER C N   1 
ATOM   8904  C CA  . SER D 1 312 ? -1.830  18.073  13.525  1.00 48.60  ? 308 SER C CA  1 
ATOM   8905  C C   . SER D 1 312 ? -1.648  19.163  12.473  1.00 52.65  ? 308 SER C C   1 
ATOM   8906  O O   . SER D 1 312 ? -1.032  20.187  12.749  1.00 55.32  ? 308 SER C O   1 
ATOM   8907  C CB  . SER D 1 312 ? -3.072  18.328  14.367  1.00 49.45  ? 308 SER C CB  1 
ATOM   8908  O OG  . SER D 1 312 ? -4.063  19.031  13.664  1.00 50.12  ? 308 SER C OG  1 
ATOM   8909  N N   . ASN D 1 313 ? -2.188  18.941  11.277  1.00 49.20  ? 309 ASN C N   1 
ATOM   8910  C CA  . ASN D 1 313 ? -2.104  19.921  10.192  1.00 53.78  ? 309 ASN C CA  1 
ATOM   8911  C C   . ASN D 1 313 ? -3.302  20.873  10.163  1.00 55.90  ? 309 ASN C C   1 
ATOM   8912  O O   . ASN D 1 313 ? -3.200  22.006  9.673   1.00 54.26  ? 309 ASN C O   1 
ATOM   8913  C CB  . ASN D 1 313 ? -1.946  19.216  8.838   1.00 58.73  ? 309 ASN C CB  1 
ATOM   8914  C CG  . ASN D 1 313 ? -0.561  18.615  8.643   1.00 60.83  ? 309 ASN C CG  1 
ATOM   8915  O OD1 . ASN D 1 313 ? 0.444   19.182  9.077   1.00 60.19  ? 309 ASN C OD1 1 
ATOM   8916  N ND2 . ASN D 1 313 ? -0.502  17.468  7.975   1.00 60.31  ? 309 ASN C ND2 1 
ATOM   8917  N N   . LYS D 1 314 ? -4.437  20.417  10.683  1.00 57.73  ? 310 LYS C N   1 
ATOM   8918  C CA  . LYS D 1 314 ? -5.599  21.287  10.815  1.00 53.12  ? 310 LYS C CA  1 
ATOM   8919  C C   . LYS D 1 314 ? -6.624  20.833  11.852  1.00 48.25  ? 310 LYS C C   1 
ATOM   8920  O O   . LYS D 1 314 ? -6.791  19.648  12.125  1.00 46.97  ? 310 LYS C O   1 
ATOM   8921  C CB  . LYS D 1 314 ? -6.324  21.437  9.487   1.00 53.43  ? 310 LYS C CB  1 
ATOM   8922  C CG  . LYS D 1 314 ? -6.683  20.156  8.757   1.00 56.03  ? 310 LYS C CG  1 
ATOM   8923  C CD  . LYS D 1 314 ? -7.364  20.470  7.443   1.00 62.74  ? 310 LYS C CD  1 
ATOM   8924  C CE  . LYS D 1 314 ? -7.624  19.181  6.676   1.00 63.27  ? 310 LYS C CE  1 
ATOM   8925  N NZ  . LYS D 1 314 ? -8.769  18.437  7.271   1.00 67.76  ? 310 LYS C NZ  1 
ATOM   8926  N N   . LEU D 1 315 ? -7.335  21.810  12.390  1.00 43.67  ? 311 LEU C N   1 
ATOM   8927  C CA  . LEU D 1 315 ? -8.444  21.573  13.314  1.00 39.89  ? 311 LEU C CA  1 
ATOM   8928  C C   . LEU D 1 315 ? -9.611  22.485  12.955  1.00 39.03  ? 311 LEU C C   1 
ATOM   8929  O O   . LEU D 1 315 ? -9.743  23.578  13.504  1.00 40.86  ? 311 LEU C O   1 
ATOM   8930  C CB  . LEU D 1 315 ? -7.992  21.821  14.750  1.00 37.93  ? 311 LEU C CB  1 
ATOM   8931  C CG  . LEU D 1 315 ? -6.980  20.804  15.282  1.00 38.96  ? 311 LEU C CG  1 
ATOM   8932  C CD1 . LEU D 1 315 ? -6.575  21.227  16.683  1.00 41.08  ? 311 LEU C CD1 1 
ATOM   8933  C CD2 . LEU D 1 315 ? -7.535  19.386  15.285  1.00 34.99  ? 311 LEU C CD2 1 
ATOM   8934  N N   . VAL D 1 316 ? -10.452 22.020  12.032  1.00 31.60  ? 312 VAL C N   1 
ATOM   8935  C CA  . VAL D 1 316 ? -11.493 22.854  11.441  1.00 31.79  ? 312 VAL C CA  1 
ATOM   8936  C C   . VAL D 1 316 ? -12.867 22.575  12.043  1.00 32.23  ? 312 VAL C C   1 
ATOM   8937  O O   . VAL D 1 316 ? -13.392 21.464  11.942  1.00 29.11  ? 312 VAL C O   1 
ATOM   8938  C CB  . VAL D 1 316 ? -11.586 22.647  9.910   1.00 30.50  ? 312 VAL C CB  1 
ATOM   8939  C CG1 . VAL D 1 316 ? -12.665 23.539  9.312   1.00 26.61  ? 312 VAL C CG1 1 
ATOM   8940  C CG2 . VAL D 1 316 ? -10.239 22.903  9.259   1.00 29.55  ? 312 VAL C CG2 1 
ATOM   8941  N N   . LEU D 1 317 ? -13.434 23.604  12.664  1.00 33.89  ? 313 LEU C N   1 
ATOM   8942  C CA  . LEU D 1 317 ? -14.763 23.537  13.259  1.00 34.28  ? 313 LEU C CA  1 
ATOM   8943  C C   . LEU D 1 317 ? -15.804 23.965  12.238  1.00 39.27  ? 313 LEU C C   1 
ATOM   8944  O O   . LEU D 1 317 ? -15.690 25.045  11.652  1.00 40.43  ? 313 LEU C O   1 
ATOM   8945  C CB  . LEU D 1 317 ? -14.845 24.450  14.491  1.00 33.95  ? 313 LEU C CB  1 
ATOM   8946  C CG  . LEU D 1 317 ? -14.983 23.809  15.881  1.00 33.99  ? 313 LEU C CG  1 
ATOM   8947  C CD1 . LEU D 1 317 ? -14.456 22.386  15.946  1.00 31.10  ? 313 LEU C CD1 1 
ATOM   8948  C CD2 . LEU D 1 317 ? -14.313 24.681  16.935  1.00 33.67  ? 313 LEU C CD2 1 
ATOM   8949  N N   . ALA D 1 318 ? -16.809 23.117  12.026  1.00 38.43  ? 314 ALA C N   1 
ATOM   8950  C CA  . ALA D 1 318 ? -17.950 23.478  11.191  1.00 38.15  ? 314 ALA C CA  1 
ATOM   8951  C C   . ALA D 1 318 ? -18.733 24.546  11.932  1.00 40.23  ? 314 ALA C C   1 
ATOM   8952  O O   . ALA D 1 318 ? -19.162 24.336  13.062  1.00 41.84  ? 314 ALA C O   1 
ATOM   8953  C CB  . ALA D 1 318 ? -18.829 22.271  10.901  1.00 34.38  ? 314 ALA C CB  1 
ATOM   8954  N N   . THR D 1 319 ? -18.863 25.708  11.309  1.00 42.94  ? 315 THR C N   1 
ATOM   8955  C CA  . THR D 1 319 ? -19.522 26.853  11.920  1.00 48.74  ? 315 THR C CA  1 
ATOM   8956  C C   . THR D 1 319 ? -20.741 27.331  11.117  1.00 47.94  ? 315 THR C C   1 
ATOM   8957  O O   . THR D 1 319 ? -21.359 28.332  11.476  1.00 52.08  ? 315 THR C O   1 
ATOM   8958  C CB  . THR D 1 319 ? -18.481 27.979  12.109  1.00 57.73  ? 315 THR C CB  1 
ATOM   8959  O OG1 . THR D 1 319 ? -18.732 28.691  13.327  1.00 66.54  ? 315 THR C OG1 1 
ATOM   8960  C CG2 . THR D 1 319 ? -18.467 28.938  10.931  1.00 58.21  ? 315 THR C CG2 1 
ATOM   8961  N N   . GLY D 1 320 ? -21.080 26.594  10.054  1.00 42.42  ? 316 GLY C N   1 
ATOM   8962  C CA  . GLY D 1 320 ? -22.275 26.825  9.241   1.00 36.32  ? 316 GLY C CA  1 
ATOM   8963  C C   . GLY D 1 320 ? -22.991 25.516  8.947   1.00 37.41  ? 316 GLY C C   1 
ATOM   8964  O O   . GLY D 1 320 ? -22.931 24.582  9.740   1.00 39.90  ? 316 GLY C O   1 
ATOM   8965  N N   . LEU D 1 321 ? -23.648 25.441  7.793   1.00 38.27  ? 317 LEU C N   1 
ATOM   8966  C CA  . LEU D 1 321 ? -24.496 24.301  7.443   1.00 39.72  ? 317 LEU C CA  1 
ATOM   8967  C C   . LEU D 1 321 ? -23.825 23.398  6.413   1.00 38.31  ? 317 LEU C C   1 
ATOM   8968  O O   . LEU D 1 321 ? -22.840 23.787  5.796   1.00 41.01  ? 317 LEU C O   1 
ATOM   8969  C CB  . LEU D 1 321 ? -25.812 24.815  6.862   1.00 45.23  ? 317 LEU C CB  1 
ATOM   8970  C CG  . LEU D 1 321 ? -26.578 25.862  7.687   1.00 47.96  ? 317 LEU C CG  1 
ATOM   8971  C CD1 . LEU D 1 321 ? -27.358 26.805  6.789   1.00 54.29  ? 317 LEU C CD1 1 
ATOM   8972  C CD2 . LEU D 1 321 ? -27.508 25.215  8.688   1.00 52.71  ? 317 LEU C CD2 1 
ATOM   8973  N N   . ARG D 1 322 ? -24.368 22.195  6.220   1.00 41.33  ? 318 ARG C N   1 
ATOM   8974  C CA  . ARG D 1 322 ? -23.993 21.357  5.075   1.00 40.92  ? 318 ARG C CA  1 
ATOM   8975  C C   . ARG D 1 322 ? -24.283 22.105  3.781   1.00 41.31  ? 318 ARG C C   1 
ATOM   8976  O O   . ARG D 1 322 ? -25.343 22.717  3.637   1.00 39.90  ? 318 ARG C O   1 
ATOM   8977  C CB  . ARG D 1 322 ? -24.793 20.055  5.037   1.00 38.75  ? 318 ARG C CB  1 
ATOM   8978  C CG  . ARG D 1 322 ? -24.409 19.019  6.068   1.00 43.49  ? 318 ARG C CG  1 
ATOM   8979  C CD  . ARG D 1 322 ? -25.259 17.772  5.885   1.00 46.58  ? 318 ARG C CD  1 
ATOM   8980  N NE  . ARG D 1 322 ? -25.233 16.901  7.061   1.00 49.61  ? 318 ARG C NE  1 
ATOM   8981  C CZ  . ARG D 1 322 ? -24.431 15.847  7.226   1.00 50.14  ? 318 ARG C CZ  1 
ATOM   8982  N NH1 . ARG D 1 322 ? -23.556 15.495  6.289   1.00 51.75  ? 318 ARG C NH1 1 
ATOM   8983  N NH2 . ARG D 1 322 ? -24.510 15.137  8.346   1.00 50.52  ? 318 ARG C NH2 1 
ATOM   8984  N N   . ASN D 1 323 ? -23.360 22.021  2.830   1.00 47.51  ? 319 ASN C N   1 
ATOM   8985  C CA  . ASN D 1 323 ? -23.499 22.740  1.569   1.00 53.52  ? 319 ASN C CA  1 
ATOM   8986  C C   . ASN D 1 323 ? -23.632 21.787  0.398   1.00 60.30  ? 319 ASN C C   1 
ATOM   8987  O O   . ASN D 1 323 ? -22.652 21.441  -0.254  1.00 71.26  ? 319 ASN C O   1 
ATOM   8988  C CB  . ASN D 1 323 ? -22.343 23.734  1.416   1.00 55.22  ? 319 ASN C CB  1 
ATOM   8989  C CG  . ASN D 1 323 ? -22.610 24.795  0.366   1.00 53.10  ? 319 ASN C CG  1 
ATOM   8990  O OD1 . ASN D 1 323 ? -21.676 25.405  -0.168  1.00 56.16  ? 319 ASN C OD1 1 
ATOM   8991  N ND2 . ASN D 1 323 ? -23.885 25.023  0.060   1.00 48.43  ? 319 ASN C ND2 1 
ATOM   8992  N N   . SER D 1 324 ? -24.868 21.338  0.175   1.00 71.98  ? 320 SER C N   1 
ATOM   8993  C CA  . SER D 1 324 ? -25.204 20.464  -0.944  1.00 88.23  ? 320 SER C CA  1 
ATOM   8994  C C   . SER D 1 324 ? -26.424 20.971  -1.724  1.00 87.12  ? 320 SER C C   1 
ATOM   8995  O O   . SER D 1 324 ? -26.603 22.174  -1.930  1.00 82.11  ? 320 SER C O   1 
ATOM   8996  C CB  . SER D 1 324 ? -25.480 19.054  -0.421  1.00 86.88  ? 320 SER C CB  1 
ATOM   8997  O OG  . SER D 1 324 ? -26.657 19.018  0.368   1.00 92.63  ? 320 SER C OG  1 
ATOM   8998  N N   . ILE E 2 10  ? -42.210 2.703   19.104  1.00 78.85  ? 10  ILE F N   1 
ATOM   8999  C CA  . ILE E 2 10  ? -41.373 1.731   18.337  1.00 86.70  ? 10  ILE F CA  1 
ATOM   9000  C C   . ILE E 2 10  ? -40.523 0.921   19.312  1.00 95.23  ? 10  ILE F C   1 
ATOM   9001  O O   . ILE E 2 10  ? -39.325 1.167   19.470  1.00 79.42  ? 10  ILE F O   1 
ATOM   9002  C CB  . ILE E 2 10  ? -40.473 2.434   17.286  1.00 82.01  ? 10  ILE F CB  1 
ATOM   9003  C CG1 . ILE E 2 10  ? -41.188 3.627   16.627  1.00 82.14  ? 10  ILE F CG1 1 
ATOM   9004  C CG2 . ILE E 2 10  ? -40.008 1.430   16.238  1.00 72.07  ? 10  ILE F CG2 1 
ATOM   9005  C CD1 . ILE E 2 10  ? -40.272 4.511   15.803  1.00 74.02  ? 10  ILE F CD1 1 
ATOM   9006  N N   . GLU E 2 11  ? -41.178 -0.047  19.951  1.00 109.46 ? 11  GLU F N   1 
ATOM   9007  C CA  . GLU E 2 11  ? -40.606 -0.851  21.034  1.00 110.91 ? 11  GLU F CA  1 
ATOM   9008  C C   . GLU E 2 11  ? -40.205 -2.268  20.622  1.00 98.90  ? 11  GLU F C   1 
ATOM   9009  O O   . GLU E 2 11  ? -41.067 -3.108  20.377  1.00 99.85  ? 11  GLU F O   1 
ATOM   9010  C CB  . GLU E 2 11  ? -41.593 -0.926  22.204  1.00 114.64 ? 11  GLU F CB  1 
ATOM   9011  C CG  . GLU E 2 11  ? -41.950 0.424   22.803  1.00 113.25 ? 11  GLU F CG  1 
ATOM   9012  C CD  . GLU E 2 11  ? -42.739 0.308   24.096  1.00 108.18 ? 11  GLU F CD  1 
ATOM   9013  O OE1 . GLU E 2 11  ? -43.242 -0.795  24.394  1.00 107.63 ? 11  GLU F OE1 1 
ATOM   9014  O OE2 . GLU E 2 11  ? -42.858 1.322   24.818  1.00 100.55 ? 11  GLU F OE2 1 
ATOM   9015  N N   . GLY E 2 12  ? -38.896 -2.519  20.562  1.00 89.11  ? 12  GLY F N   1 
ATOM   9016  C CA  . GLY E 2 12  ? -38.341 -3.855  20.341  1.00 89.30  ? 12  GLY F CA  1 
ATOM   9017  C C   . GLY E 2 12  ? -37.749 -4.058  18.951  1.00 88.42  ? 12  GLY F C   1 
ATOM   9018  O O   . GLY E 2 12  ? -38.144 -3.385  17.997  1.00 79.56  ? 12  GLY F O   1 
ATOM   9019  N N   . GLY E 2 13  ? -36.771 -4.963  18.850  1.00 86.02  ? 13  GLY F N   1 
ATOM   9020  C CA  . GLY E 2 13  ? -36.097 -5.266  17.585  1.00 80.44  ? 13  GLY F CA  1 
ATOM   9021  C C   . GLY E 2 13  ? -36.540 -6.600  17.012  1.00 70.16  ? 13  GLY F C   1 
ATOM   9022  O O   . GLY E 2 13  ? -36.981 -7.482  17.745  1.00 66.33  ? 13  GLY F O   1 
ATOM   9023  N N   . TRP E 2 14  ? -36.407 -6.741  15.697  1.00 66.48  ? 14  TRP F N   1 
ATOM   9024  C CA  . TRP E 2 14  ? -36.808 -7.958  14.994  1.00 58.68  ? 14  TRP F CA  1 
ATOM   9025  C C   . TRP E 2 14  ? -35.702 -8.969  15.008  1.00 65.17  ? 14  TRP F C   1 
ATOM   9026  O O   . TRP E 2 14  ? -34.679 -8.781  14.341  1.00 72.82  ? 14  TRP F O   1 
ATOM   9027  C CB  . TRP E 2 14  ? -37.137 -7.665  13.534  1.00 54.32  ? 14  TRP F CB  1 
ATOM   9028  C CG  . TRP E 2 14  ? -38.110 -6.541  13.247  1.00 46.15  ? 14  TRP F CG  1 
ATOM   9029  C CD1 . TRP E 2 14  ? -38.133 -5.717  12.120  1.00 47.19  ? 14  TRP F CD1 1 
ATOM   9030  C CD2 . TRP E 2 14  ? -39.226 -6.081  14.068  1.00 44.70  ? 14  TRP F CD2 1 
ATOM   9031  N NE1 . TRP E 2 14  ? -39.156 -4.811  12.179  1.00 40.94  ? 14  TRP F NE1 1 
ATOM   9032  C CE2 . TRP E 2 14  ? -39.853 -4.973  13.323  1.00 42.37  ? 14  TRP F CE2 1 
ATOM   9033  C CE3 . TRP E 2 14  ? -39.759 -6.458  15.288  1.00 45.67  ? 14  TRP F CE3 1 
ATOM   9034  C CZ2 . TRP E 2 14  ? -40.945 -4.295  13.810  1.00 46.20  ? 14  TRP F CZ2 1 
ATOM   9035  C CZ3 . TRP E 2 14  ? -40.864 -5.757  15.769  1.00 52.16  ? 14  TRP F CZ3 1 
ATOM   9036  C CH2 . TRP E 2 14  ? -41.442 -4.701  15.047  1.00 54.83  ? 14  TRP F CH2 1 
ATOM   9037  N N   . GLN E 2 15  ? -35.877 -10.053 15.760  1.00 62.39  ? 15  GLN F N   1 
ATOM   9038  C CA  . GLN E 2 15  ? -34.943 -11.172 15.670  1.00 69.07  ? 15  GLN F CA  1 
ATOM   9039  C C   . GLN E 2 15  ? -35.104 -11.859 14.315  1.00 69.80  ? 15  GLN F C   1 
ATOM   9040  O O   . GLN E 2 15  ? -34.163 -12.471 13.808  1.00 65.61  ? 15  GLN F O   1 
ATOM   9041  C CB  . GLN E 2 15  ? -35.156 -12.167 16.814  1.00 77.27  ? 15  GLN F CB  1 
ATOM   9042  C CG  . GLN E 2 15  ? -34.072 -13.240 16.917  1.00 85.14  ? 15  GLN F CG  1 
ATOM   9043  C CD  . GLN E 2 15  ? -33.597 -13.494 18.343  1.00 89.65  ? 15  GLN F CD  1 
ATOM   9044  O OE1 . GLN E 2 15  ? -33.952 -12.772 19.276  1.00 92.65  ? 15  GLN F OE1 1 
ATOM   9045  N NE2 . GLN E 2 15  ? -32.788 -14.535 18.515  1.00 86.07  ? 15  GLN F NE2 1 
ATOM   9046  N N   . GLY E 2 16  ? -36.299 -11.743 13.738  1.00 77.51  ? 16  GLY F N   1 
ATOM   9047  C CA  . GLY E 2 16  ? -36.594 -12.307 12.426  1.00 73.17  ? 16  GLY F CA  1 
ATOM   9048  C C   . GLY E 2 16  ? -35.973 -11.569 11.250  1.00 72.52  ? 16  GLY F C   1 
ATOM   9049  O O   . GLY E 2 16  ? -35.822 -12.145 10.175  1.00 76.40  ? 16  GLY F O   1 
ATOM   9050  N N   . MET E 2 17  ? -35.631 -10.295 11.434  1.00 73.69  ? 17  MET F N   1 
ATOM   9051  C CA  . MET E 2 17  ? -34.990 -9.525  10.363  1.00 73.26  ? 17  MET F CA  1 
ATOM   9052  C C   . MET E 2 17  ? -33.472 -9.671  10.419  1.00 81.31  ? 17  MET F C   1 
ATOM   9053  O O   . MET E 2 17  ? -32.842 -9.161  11.343  1.00 88.86  ? 17  MET F O   1 
ATOM   9054  C CB  . MET E 2 17  ? -35.370 -8.045  10.447  1.00 65.96  ? 17  MET F CB  1 
ATOM   9055  C CG  . MET E 2 17  ? -35.024 -7.278  9.181   1.00 64.24  ? 17  MET F CG  1 
ATOM   9056  S SD  . MET E 2 17  ? -35.368 -5.517  9.266   1.00 68.92  ? 17  MET F SD  1 
ATOM   9057  C CE  . MET E 2 17  ? -34.142 -4.969  10.451  1.00 62.32  ? 17  MET F CE  1 
ATOM   9058  N N   . VAL E 2 18  ? -32.900 -10.354 9.423   1.00 89.26  ? 18  VAL F N   1 
ATOM   9059  C CA  . VAL E 2 18  ? -31.460 -10.657 9.370   1.00 87.30  ? 18  VAL F CA  1 
ATOM   9060  C C   . VAL E 2 18  ? -30.673 -9.822  8.346   1.00 86.42  ? 18  VAL F C   1 
ATOM   9061  O O   . VAL E 2 18  ? -29.535 -9.419  8.610   1.00 96.46  ? 18  VAL F O   1 
ATOM   9062  C CB  . VAL E 2 18  ? -31.232 -12.156 9.078   1.00 86.43  ? 18  VAL F CB  1 
ATOM   9063  C CG1 . VAL E 2 18  ? -31.777 -12.998 10.224  1.00 83.26  ? 18  VAL F CG1 1 
ATOM   9064  C CG2 . VAL E 2 18  ? -31.875 -12.557 7.757   1.00 81.85  ? 18  VAL F CG2 1 
ATOM   9065  N N   . ASP E 2 19  ? -31.288 -9.557  7.193   1.00 87.23  ? 19  ASP F N   1 
ATOM   9066  C CA  . ASP E 2 19  ? -30.596 -8.948  6.034   1.00 91.18  ? 19  ASP F CA  1 
ATOM   9067  C C   . ASP E 2 19  ? -30.115 -7.508  6.242   1.00 83.79  ? 19  ASP F C   1 
ATOM   9068  O O   . ASP E 2 19  ? -29.306 -7.035  5.446   1.00 78.81  ? 19  ASP F O   1 
ATOM   9069  C CB  . ASP E 2 19  ? -31.439 -8.994  4.733   1.00 99.22  ? 19  ASP F CB  1 
ATOM   9070  C CG  . ASP E 2 19  ? -32.597 -9.982  4.797   1.00 109.94 ? 19  ASP F CG  1 
ATOM   9071  O OD1 . ASP E 2 19  ? -32.590 -11.043 4.116   1.00 108.85 ? 19  ASP F OD1 1 
ATOM   9072  O OD2 . ASP E 2 19  ? -33.535 -9.668  5.548   1.00 112.81 ? 19  ASP F OD2 1 
ATOM   9073  N N   . GLY E 2 20  ? -30.620 -6.799  7.255   1.00 76.82  ? 20  GLY F N   1 
ATOM   9074  C CA  . GLY E 2 20  ? -30.169 -5.426  7.505   1.00 68.16  ? 20  GLY F CA  1 
ATOM   9075  C C   . GLY E 2 20  ? -30.265 -4.955  8.943   1.00 58.48  ? 20  GLY F C   1 
ATOM   9076  O O   . GLY E 2 20  ? -30.395 -5.755  9.863   1.00 54.02  ? 20  GLY F O   1 
ATOM   9077  N N   . TRP E 2 21  ? -30.197 -3.638  9.120   1.00 55.66  ? 21  TRP F N   1 
ATOM   9078  C CA  . TRP E 2 21  ? -30.248 -3.005  10.441  1.00 50.71  ? 21  TRP F CA  1 
ATOM   9079  C C   . TRP E 2 21  ? -31.586 -2.390  10.723  1.00 47.03  ? 21  TRP F C   1 
ATOM   9080  O O   . TRP E 2 21  ? -32.143 -2.590  11.800  1.00 43.25  ? 21  TRP F O   1 
ATOM   9081  C CB  . TRP E 2 21  ? -29.158 -1.943  10.555  1.00 50.65  ? 21  TRP F CB  1 
ATOM   9082  C CG  . TRP E 2 21  ? -27.839 -2.450  11.088  1.00 56.15  ? 21  TRP F CG  1 
ATOM   9083  C CD1 . TRP E 2 21  ? -27.442 -3.774  11.299  1.00 55.14  ? 21  TRP F CD1 1 
ATOM   9084  C CD2 . TRP E 2 21  ? -26.680 -1.640  11.474  1.00 54.02  ? 21  TRP F CD2 1 
ATOM   9085  N NE1 . TRP E 2 21  ? -26.169 -3.828  11.795  1.00 58.05  ? 21  TRP F NE1 1 
ATOM   9086  C CE2 . TRP E 2 21  ? -25.652 -2.584  11.920  1.00 56.99  ? 21  TRP F CE2 1 
ATOM   9087  C CE3 . TRP E 2 21  ? -26.407 -0.279  11.508  1.00 49.85  ? 21  TRP F CE3 1 
ATOM   9088  C CZ2 . TRP E 2 21  ? -24.413 -2.160  12.368  1.00 53.60  ? 21  TRP F CZ2 1 
ATOM   9089  C CZ3 . TRP E 2 21  ? -25.152 0.135   11.956  1.00 55.06  ? 21  TRP F CZ3 1 
ATOM   9090  C CH2 . TRP E 2 21  ? -24.180 -0.786  12.377  1.00 55.19  ? 21  TRP F CH2 1 
ATOM   9091  N N   . TYR E 2 22  ? -32.101 -1.612  9.775   1.00 43.11  ? 22  TYR F N   1 
ATOM   9092  C CA  . TYR E 2 22  ? -33.436 -1.035  9.891   1.00 47.32  ? 22  TYR F CA  1 
ATOM   9093  C C   . TYR E 2 22  ? -34.276 -1.565  8.750   1.00 54.09  ? 22  TYR F C   1 
ATOM   9094  O O   . TYR E 2 22  ? -33.753 -1.847  7.673   1.00 59.71  ? 22  TYR F O   1 
ATOM   9095  C CB  . TYR E 2 22  ? -33.396 0.491   9.824   1.00 47.85  ? 22  TYR F CB  1 
ATOM   9096  C CG  . TYR E 2 22  ? -32.202 1.126   10.493  1.00 45.94  ? 22  TYR F CG  1 
ATOM   9097  C CD1 . TYR E 2 22  ? -31.292 1.887   9.763   1.00 45.27  ? 22  TYR F CD1 1 
ATOM   9098  C CD2 . TYR E 2 22  ? -31.979 0.968   11.854  1.00 43.09  ? 22  TYR F CD2 1 
ATOM   9099  C CE1 . TYR E 2 22  ? -30.197 2.473   10.369  1.00 46.10  ? 22  TYR F CE1 1 
ATOM   9100  C CE2 . TYR E 2 22  ? -30.887 1.552   12.465  1.00 43.28  ? 22  TYR F CE2 1 
ATOM   9101  C CZ  . TYR E 2 22  ? -29.997 2.303   11.727  1.00 45.79  ? 22  TYR F CZ  1 
ATOM   9102  O OH  . TYR E 2 22  ? -28.906 2.874   12.355  1.00 46.74  ? 22  TYR F OH  1 
ATOM   9103  N N   . GLY E 2 23  ? -35.577 -1.700  8.974   1.00 56.79  ? 23  GLY F N   1 
ATOM   9104  C CA  . GLY E 2 23  ? -36.439 -2.224  7.933   1.00 56.11  ? 23  GLY F CA  1 
ATOM   9105  C C   . GLY E 2 23  ? -37.910 -2.251  8.265   1.00 55.18  ? 23  GLY F C   1 
ATOM   9106  O O   . GLY E 2 23  ? -38.375 -1.546  9.166   1.00 48.65  ? 23  GLY F O   1 
ATOM   9107  N N   . TYR E 2 24  ? -38.634 -3.082  7.522   1.00 54.70  ? 24  TYR F N   1 
ATOM   9108  C CA  . TYR E 2 24  ? -40.079 -3.118  7.585   1.00 47.37  ? 24  TYR F CA  1 
ATOM   9109  C C   . TYR E 2 24  ? -40.578 -4.510  7.916   1.00 46.24  ? 24  TYR F C   1 
ATOM   9110  O O   . TYR E 2 24  ? -39.925 -5.511  7.604   1.00 55.10  ? 24  TYR F O   1 
ATOM   9111  C CB  . TYR E 2 24  ? -40.672 -2.693  6.248   1.00 47.74  ? 24  TYR F CB  1 
ATOM   9112  C CG  . TYR E 2 24  ? -40.000 -1.497  5.613   1.00 50.97  ? 24  TYR F CG  1 
ATOM   9113  C CD1 . TYR E 2 24  ? -38.934 -1.663  4.730   1.00 55.35  ? 24  TYR F CD1 1 
ATOM   9114  C CD2 . TYR E 2 24  ? -40.433 -0.206  5.880   1.00 55.84  ? 24  TYR F CD2 1 
ATOM   9115  C CE1 . TYR E 2 24  ? -38.316 -0.585  4.130   1.00 58.54  ? 24  TYR F CE1 1 
ATOM   9116  C CE2 . TYR E 2 24  ? -39.821 0.887   5.285   1.00 59.86  ? 24  TYR F CE2 1 
ATOM   9117  C CZ  . TYR E 2 24  ? -38.762 0.689   4.411   1.00 60.40  ? 24  TYR F CZ  1 
ATOM   9118  O OH  . TYR E 2 24  ? -38.144 1.760   3.810   1.00 65.70  ? 24  TYR F OH  1 
ATOM   9119  N N   . HIS E 2 25  ? -41.732 -4.555  8.569   1.00 43.08  ? 25  HIS F N   1 
ATOM   9120  C CA  . HIS E 2 25  ? -42.504 -5.782  8.719   1.00 45.85  ? 25  HIS F CA  1 
ATOM   9121  C C   . HIS E 2 25  ? -43.911 -5.489  8.308   1.00 46.30  ? 25  HIS F C   1 
ATOM   9122  O O   . HIS E 2 25  ? -44.480 -4.479  8.719   1.00 42.03  ? 25  HIS F O   1 
ATOM   9123  C CB  . HIS E 2 25  ? -42.479 -6.279  10.153  1.00 46.04  ? 25  HIS F CB  1 
ATOM   9124  C CG  . HIS E 2 25  ? -43.351 -7.489  10.403  1.00 48.80  ? 25  HIS F CG  1 
ATOM   9125  N ND1 . HIS E 2 25  ? -42.916 -8.744  10.208  1.00 52.80  ? 25  HIS F ND1 1 
ATOM   9126  C CD2 . HIS E 2 25  ? -44.664 -7.595  10.867  1.00 49.50  ? 25  HIS F CD2 1 
ATOM   9127  C CE1 . HIS E 2 25  ? -43.897 -9.613  10.518  1.00 55.78  ? 25  HIS F CE1 1 
ATOM   9128  N NE2 . HIS E 2 25  ? -44.966 -8.908  10.922  1.00 52.53  ? 25  HIS F NE2 1 
ATOM   9129  N N   . HIS E 2 26  ? -44.480 -6.361  7.483   1.00 47.91  ? 26  HIS F N   1 
ATOM   9130  C CA  . HIS E 2 26  ? -45.843 -6.177  6.989   1.00 46.84  ? 26  HIS F CA  1 
ATOM   9131  C C   . HIS E 2 26  ? -46.680 -7.374  7.295   1.00 43.65  ? 26  HIS F C   1 
ATOM   9132  O O   . HIS E 2 26  ? -46.164 -8.474  7.496   1.00 39.41  ? 26  HIS F O   1 
ATOM   9133  C CB  . HIS E 2 26  ? -45.845 -5.929  5.488   1.00 44.17  ? 26  HIS F CB  1 
ATOM   9134  C CG  . HIS E 2 26  ? -45.356 -7.108  4.682   1.00 54.74  ? 26  HIS F CG  1 
ATOM   9135  N ND1 . HIS E 2 26  ? -46.163 -8.116  4.305   1.00 56.07  ? 26  HIS F ND1 1 
ATOM   9136  C CD2 . HIS E 2 26  ? -44.087 -7.422  4.207   1.00 61.13  ? 26  HIS F CD2 1 
ATOM   9137  C CE1 . HIS E 2 26  ? -45.444 -9.024  3.615   1.00 60.45  ? 26  HIS F CE1 1 
ATOM   9138  N NE2 . HIS E 2 26  ? -44.178 -8.595  3.558   1.00 63.45  ? 26  HIS F NE2 1 
ATOM   9139  N N   . SER E 2 27  ? -47.987 -7.160  7.349   1.00 44.37  ? 27  SER F N   1 
ATOM   9140  C CA  . SER E 2 27  ? -48.934 -8.260  7.411   1.00 47.42  ? 27  SER F CA  1 
ATOM   9141  C C   . SER E 2 27  ? -50.162 -7.880  6.589   1.00 42.84  ? 27  SER F C   1 
ATOM   9142  O O   . SER E 2 27  ? -50.696 -6.787  6.728   1.00 38.80  ? 27  SER F O   1 
ATOM   9143  C CB  . SER E 2 27  ? -49.306 -8.594  8.858   1.00 46.98  ? 27  SER F CB  1 
ATOM   9144  O OG  . SER E 2 27  ? -50.002 -7.524  9.468   1.00 66.92  ? 27  SER F OG  1 
ATOM   9145  N N   . ASN E 2 28  ? -50.570 -8.784  5.706   1.00 42.71  ? 28  ASN F N   1 
ATOM   9146  C CA  . ASN E 2 28  ? -51.779 -8.616  4.906   1.00 39.27  ? 28  ASN F CA  1 
ATOM   9147  C C   . ASN E 2 28  ? -52.452 -9.973  4.714   1.00 41.28  ? 28  ASN F C   1 
ATOM   9148  O O   . ASN E 2 28  ? -52.078 -10.935 5.383   1.00 37.91  ? 28  ASN F O   1 
ATOM   9149  C CB  . ASN E 2 28  ? -51.471 -7.902  3.582   1.00 38.30  ? 28  ASN F CB  1 
ATOM   9150  C CG  . ASN E 2 28  ? -50.396 -8.591  2.755   1.00 35.21  ? 28  ASN F CG  1 
ATOM   9151  O OD1 . ASN E 2 28  ? -49.892 -8.005  1.797   1.00 35.12  ? 28  ASN F OD1 1 
ATOM   9152  N ND2 . ASN E 2 28  ? -50.050 -9.824  3.102   1.00 29.44  ? 28  ASN F ND2 1 
ATOM   9153  N N   . GLU E 2 29  ? -53.456 -10.051 3.842   1.00 53.81  ? 29  GLU F N   1 
ATOM   9154  C CA  . GLU E 2 29  ? -54.184 -11.310 3.625   1.00 63.41  ? 29  GLU F CA  1 
ATOM   9155  C C   . GLU E 2 29  ? -53.295 -12.424 3.074   1.00 55.90  ? 29  GLU F C   1 
ATOM   9156  O O   . GLU E 2 29  ? -53.489 -13.597 3.404   1.00 50.74  ? 29  GLU F O   1 
ATOM   9157  C CB  . GLU E 2 29  ? -55.382 -11.100 2.696   1.00 72.41  ? 29  GLU F CB  1 
ATOM   9158  C CG  . GLU E 2 29  ? -56.563 -10.426 3.367   1.00 83.75  ? 29  GLU F CG  1 
ATOM   9159  C CD  . GLU E 2 29  ? -57.738 -10.280 2.428   1.00 95.67  ? 29  GLU F CD  1 
ATOM   9160  O OE1 . GLU E 2 29  ? -57.996 -9.133  1.989   1.00 108.52 ? 29  GLU F OE1 1 
ATOM   9161  O OE2 . GLU E 2 29  ? -58.391 -11.312 2.116   1.00 89.92  ? 29  GLU F OE2 1 
ATOM   9162  N N   . GLN E 2 30  ? -52.322 -12.046 2.247   1.00 52.08  ? 30  GLN F N   1 
ATOM   9163  C CA  . GLN E 2 30  ? -51.386 -13.005 1.661   1.00 57.54  ? 30  GLN F CA  1 
ATOM   9164  C C   . GLN E 2 30  ? -50.395 -13.592 2.670   1.00 60.16  ? 30  GLN F C   1 
ATOM   9165  O O   . GLN E 2 30  ? -49.827 -14.655 2.424   1.00 74.08  ? 30  GLN F O   1 
ATOM   9166  C CB  . GLN E 2 30  ? -50.602 -12.356 0.518   1.00 55.97  ? 30  GLN F CB  1 
ATOM   9167  C CG  . GLN E 2 30  ? -51.451 -11.931 -0.666  1.00 57.23  ? 30  GLN F CG  1 
ATOM   9168  C CD  . GLN E 2 30  ? -50.625 -11.291 -1.761  1.00 66.29  ? 30  GLN F CD  1 
ATOM   9169  O OE1 . GLN E 2 30  ? -50.453 -10.078 -1.804  1.00 75.61  ? 30  GLN F OE1 1 
ATOM   9170  N NE2 . GLN E 2 30  ? -50.094 -12.119 -2.653  1.00 74.52  ? 30  GLN F NE2 1 
ATOM   9171  N N   . GLY E 2 31  ? -50.184 -12.909 3.793   1.00 62.02  ? 31  GLY F N   1 
ATOM   9172  C CA  . GLY E 2 31  ? -49.235 -13.364 4.811   1.00 61.04  ? 31  GLY F CA  1 
ATOM   9173  C C   . GLY E 2 31  ? -48.469 -12.217 5.442   1.00 58.04  ? 31  GLY F C   1 
ATOM   9174  O O   . GLY E 2 31  ? -48.927 -11.073 5.421   1.00 60.83  ? 31  GLY F O   1 
ATOM   9175  N N   . SER E 2 32  ? -47.302 -12.528 6.002   1.00 50.06  ? 32  SER F N   1 
ATOM   9176  C CA  . SER E 2 32  ? -46.489 -11.541 6.712   1.00 44.58  ? 32  SER F CA  1 
ATOM   9177  C C   . SER E 2 32  ? -45.004 -11.830 6.564   1.00 42.01  ? 32  SER F C   1 
ATOM   9178  O O   . SER E 2 32  ? -44.614 -12.959 6.292   1.00 42.15  ? 32  SER F O   1 
ATOM   9179  C CB  . SER E 2 32  ? -46.866 -11.520 8.195   1.00 47.08  ? 32  SER F CB  1 
ATOM   9180  O OG  . SER E 2 32  ? -46.511 -12.736 8.828   1.00 49.92  ? 32  SER F OG  1 
ATOM   9181  N N   . GLY E 2 33  ? -44.175 -10.808 6.758   1.00 48.22  ? 33  GLY F N   1 
ATOM   9182  C CA  . GLY E 2 33  ? -42.728 -10.970 6.626   1.00 48.05  ? 33  GLY F CA  1 
ATOM   9183  C C   . GLY E 2 33  ? -41.909 -9.701  6.796   1.00 48.50  ? 33  GLY F C   1 
ATOM   9184  O O   . GLY E 2 33  ? -42.453 -8.605  6.830   1.00 49.75  ? 33  GLY F O   1 
ATOM   9185  N N   . TYR E 2 34  ? -40.590 -9.864  6.897   1.00 47.73  ? 34  TYR F N   1 
ATOM   9186  C CA  . TYR E 2 34  ? -39.656 -8.750  7.083   1.00 47.64  ? 34  TYR F CA  1 
ATOM   9187  C C   . TYR E 2 34  ? -38.958 -8.356  5.785   1.00 49.51  ? 34  TYR F C   1 
ATOM   9188  O O   . TYR E 2 34  ? -38.806 -9.175  4.884   1.00 52.82  ? 34  TYR F O   1 
ATOM   9189  C CB  . TYR E 2 34  ? -38.589 -9.133  8.109   1.00 44.77  ? 34  TYR F CB  1 
ATOM   9190  C CG  . TYR E 2 34  ? -39.160 -9.491  9.460   1.00 43.86  ? 34  TYR F CG  1 
ATOM   9191  C CD1 . TYR E 2 34  ? -39.408 -10.812 9.802   1.00 48.30  ? 34  TYR F CD1 1 
ATOM   9192  C CD2 . TYR E 2 34  ? -39.470 -8.505  10.390  1.00 48.12  ? 34  TYR F CD2 1 
ATOM   9193  C CE1 . TYR E 2 34  ? -39.945 -11.150 11.036  1.00 51.16  ? 34  TYR F CE1 1 
ATOM   9194  C CE2 . TYR E 2 34  ? -40.007 -8.831  11.624  1.00 50.49  ? 34  TYR F CE2 1 
ATOM   9195  C CZ  . TYR E 2 34  ? -40.243 -10.155 11.945  1.00 55.27  ? 34  TYR F CZ  1 
ATOM   9196  O OH  . TYR E 2 34  ? -40.773 -10.494 13.169  1.00 55.35  ? 34  TYR F OH  1 
ATOM   9197  N N   . ALA E 2 35  ? -38.548 -7.093  5.695   1.00 49.13  ? 35  ALA F N   1 
ATOM   9198  C CA  . ALA E 2 35  ? -37.714 -6.616  4.595   1.00 49.01  ? 35  ALA F CA  1 
ATOM   9199  C C   . ALA E 2 35  ? -36.845 -5.445  5.063   1.00 53.29  ? 35  ALA F C   1 
ATOM   9200  O O   . ALA E 2 35  ? -37.351 -4.467  5.610   1.00 54.03  ? 35  ALA F O   1 
ATOM   9201  C CB  . ALA E 2 35  ? -38.578 -6.193  3.421   1.00 46.77  ? 35  ALA F CB  1 
ATOM   9202  N N   . ALA E 2 36  ? -35.539 -5.547  4.844   1.00 53.56  ? 36  ALA F N   1 
ATOM   9203  C CA  . ALA E 2 36  ? -34.590 -4.526  5.304   1.00 52.95  ? 36  ALA F CA  1 
ATOM   9204  C C   . ALA E 2 36  ? -34.508 -3.353  4.327   1.00 54.14  ? 36  ALA F C   1 
ATOM   9205  O O   . ALA E 2 36  ? -34.555 -3.552  3.111   1.00 60.44  ? 36  ALA F O   1 
ATOM   9206  C CB  . ALA E 2 36  ? -33.211 -5.138  5.508   1.00 48.32  ? 36  ALA F CB  1 
ATOM   9207  N N   . ASP E 2 37  ? -34.400 -2.136  4.862   1.00 51.90  ? 37  ASP F N   1 
ATOM   9208  C CA  . ASP E 2 37  ? -34.108 -0.951  4.052   1.00 59.00  ? 37  ASP F CA  1 
ATOM   9209  C C   . ASP E 2 37  ? -32.599 -0.831  3.859   1.00 60.23  ? 37  ASP F C   1 
ATOM   9210  O O   . ASP E 2 37  ? -31.872 -0.485  4.786   1.00 62.69  ? 37  ASP F O   1 
ATOM   9211  C CB  . ASP E 2 37  ? -34.646 0.317   4.713   1.00 62.11  ? 37  ASP F CB  1 
ATOM   9212  C CG  . ASP E 2 37  ? -34.507 1.529   3.828   1.00 63.29  ? 37  ASP F CG  1 
ATOM   9213  O OD1 . ASP E 2 37  ? -35.291 1.624   2.858   1.00 63.17  ? 37  ASP F OD1 1 
ATOM   9214  O OD2 . ASP E 2 37  ? -33.632 2.381   4.107   1.00 69.47  ? 37  ASP F OD2 1 
ATOM   9215  N N   . LYS E 2 38  ? -32.134 -1.110  2.647   1.00 68.10  ? 38  LYS F N   1 
ATOM   9216  C CA  . LYS E 2 38  ? -30.697 -1.224  2.375   1.00 72.78  ? 38  LYS F CA  1 
ATOM   9217  C C   . LYS E 2 38  ? -29.968 0.118   2.326   1.00 66.37  ? 38  LYS F C   1 
ATOM   9218  O O   . LYS E 2 38  ? -28.795 0.199   2.685   1.00 65.86  ? 38  LYS F O   1 
ATOM   9219  C CB  . LYS E 2 38  ? -30.475 -2.024  1.093   1.00 82.70  ? 38  LYS F CB  1 
ATOM   9220  C CG  . LYS E 2 38  ? -31.045 -3.442  1.222   1.00 91.26  ? 38  LYS F CG  1 
ATOM   9221  C CD  . LYS E 2 38  ? -30.352 -4.512  0.390   1.00 98.90  ? 38  LYS F CD  1 
ATOM   9222  C CE  . LYS E 2 38  ? -30.967 -5.881  0.666   1.00 98.79  ? 38  LYS F CE  1 
ATOM   9223  N NZ  . LYS E 2 38  ? -30.247 -6.984  -0.029  1.00 102.62 ? 38  LYS F NZ  1 
ATOM   9224  N N   . GLU E 2 39  ? -30.665 1.167   1.905   1.00 64.57  ? 39  GLU F N   1 
ATOM   9225  C CA  . GLU E 2 39  ? -30.066 2.503   1.831   1.00 64.68  ? 39  GLU F CA  1 
ATOM   9226  C C   . GLU E 2 39  ? -29.676 3.033   3.215   1.00 60.14  ? 39  GLU F C   1 
ATOM   9227  O O   . GLU E 2 39  ? -28.505 3.320   3.462   1.00 58.91  ? 39  GLU F O   1 
ATOM   9228  C CB  . GLU E 2 39  ? -31.004 3.483   1.129   1.00 72.57  ? 39  GLU F CB  1 
ATOM   9229  C CG  . GLU E 2 39  ? -30.283 4.464   0.217   1.00 83.96  ? 39  GLU F CG  1 
ATOM   9230  C CD  . GLU E 2 39  ? -31.128 5.678   -0.167  1.00 93.97  ? 39  GLU F CD  1 
ATOM   9231  O OE1 . GLU E 2 39  ? -31.327 6.575   0.684   1.00 90.57  ? 39  GLU F OE1 1 
ATOM   9232  O OE2 . GLU E 2 39  ? -31.571 5.752   -1.337  1.00 94.67  ? 39  GLU F OE2 1 
ATOM   9233  N N   . SER E 2 40  ? -30.645 3.144   4.120   1.00 53.08  ? 40  SER F N   1 
ATOM   9234  C CA  . SER E 2 40  ? -30.382 3.677   5.459   1.00 54.14  ? 40  SER F CA  1 
ATOM   9235  C C   . SER E 2 40  ? -29.478 2.760   6.299   1.00 52.49  ? 40  SER F C   1 
ATOM   9236  O O   . SER E 2 40  ? -28.706 3.241   7.131   1.00 48.53  ? 40  SER F O   1 
ATOM   9237  C CB  . SER E 2 40  ? -31.689 3.959   6.206   1.00 54.47  ? 40  SER F CB  1 
ATOM   9238  O OG  . SER E 2 40  ? -32.404 2.769   6.460   1.00 54.56  ? 40  SER F OG  1 
ATOM   9239  N N   . THR E 2 41  ? -29.570 1.449   6.073   1.00 47.53  ? 41  THR F N   1 
ATOM   9240  C CA  . THR E 2 41  ? -28.686 0.489   6.732   1.00 48.28  ? 41  THR F CA  1 
ATOM   9241  C C   . THR E 2 41  ? -27.223 0.742   6.359   1.00 51.46  ? 41  THR F C   1 
ATOM   9242  O O   . THR E 2 41  ? -26.363 0.790   7.239   1.00 54.34  ? 41  THR F O   1 
ATOM   9243  C CB  . THR E 2 41  ? -29.055 -0.971  6.390   1.00 47.24  ? 41  THR F CB  1 
ATOM   9244  O OG1 . THR E 2 41  ? -30.324 -1.307  6.980   1.00 47.01  ? 41  THR F OG1 1 
ATOM   9245  C CG2 . THR E 2 41  ? -27.993 -1.932  6.927   1.00 42.34  ? 41  THR F CG2 1 
ATOM   9246  N N   . GLN E 2 42  ? -26.946 0.908   5.065   1.00 50.91  ? 42  GLN F N   1 
ATOM   9247  C CA  . GLN E 2 42  ? -25.567 1.133   4.599   1.00 55.77  ? 42  GLN F CA  1 
ATOM   9248  C C   . GLN E 2 42  ? -24.967 2.436   5.112   1.00 51.44  ? 42  GLN F C   1 
ATOM   9249  O O   . GLN E 2 42  ? -23.789 2.480   5.456   1.00 52.26  ? 42  GLN F O   1 
ATOM   9250  C CB  . GLN E 2 42  ? -25.463 1.092   3.066   1.00 59.29  ? 42  GLN F CB  1 
ATOM   9251  C CG  . GLN E 2 42  ? -25.028 -0.255  2.508   1.00 62.58  ? 42  GLN F CG  1 
ATOM   9252  C CD  . GLN E 2 42  ? -23.651 -0.678  2.983   1.00 60.27  ? 42  GLN F CD  1 
ATOM   9253  O OE1 . GLN E 2 42  ? -22.754 0.146   3.133   1.00 53.63  ? 42  GLN F OE1 1 
ATOM   9254  N NE2 . GLN E 2 42  ? -23.481 -1.973  3.230   1.00 63.27  ? 42  GLN F NE2 1 
ATOM   9255  N N   . LYS E 2 43  ? -25.771 3.491   5.164   1.00 51.38  ? 43  LYS F N   1 
ATOM   9256  C CA  . LYS E 2 43  ? -25.310 4.762   5.730   1.00 56.92  ? 43  LYS F CA  1 
ATOM   9257  C C   . LYS E 2 43  ? -24.938 4.596   7.205   1.00 51.14  ? 43  LYS F C   1 
ATOM   9258  O O   . LYS E 2 43  ? -23.928 5.129   7.662   1.00 53.89  ? 43  LYS F O   1 
ATOM   9259  C CB  . LYS E 2 43  ? -26.386 5.842   5.586   1.00 62.84  ? 43  LYS F CB  1 
ATOM   9260  C CG  . LYS E 2 43  ? -26.461 6.488   4.233   1.00 78.13  ? 43  LYS F CG  1 
ATOM   9261  C CD  . LYS E 2 43  ? -27.605 7.484   4.103   1.00 87.87  ? 43  LYS F CD  1 
ATOM   9262  C CE  . LYS E 2 43  ? -28.027 7.665   2.654   1.00 95.83  ? 43  LYS F CE  1 
ATOM   9263  N NZ  . LYS E 2 43  ? -29.015 8.768   2.470   1.00 96.28  ? 43  LYS F NZ  1 
ATOM   9264  N N   . ALA E 2 44  ? -25.754 3.843   7.932   1.00 43.43  ? 44  ALA F N   1 
ATOM   9265  C CA  . ALA E 2 44  ? -25.535 3.622   9.354   1.00 42.87  ? 44  ALA F CA  1 
ATOM   9266  C C   . ALA E 2 44  ? -24.286 2.772   9.608   1.00 43.06  ? 44  ALA F C   1 
ATOM   9267  O O   . ALA E 2 44  ? -23.509 3.065   10.517  1.00 38.52  ? 44  ALA F O   1 
ATOM   9268  C CB  . ALA E 2 44  ? -26.760 2.970   9.973   1.00 38.32  ? 44  ALA F CB  1 
ATOM   9269  N N   . ILE E 2 45  ? -24.100 1.721   8.811   1.00 44.82  ? 45  ILE F N   1 
ATOM   9270  C CA  . ILE E 2 45  ? -22.904 0.880   8.908   1.00 45.72  ? 45  ILE F CA  1 
ATOM   9271  C C   . ILE E 2 45  ? -21.640 1.679   8.574   1.00 44.79  ? 45  ILE F C   1 
ATOM   9272  O O   . ILE E 2 45  ? -20.620 1.551   9.250   1.00 49.31  ? 45  ILE F O   1 
ATOM   9273  C CB  . ILE E 2 45  ? -23.001 -0.356  7.991   1.00 49.42  ? 45  ILE F CB  1 
ATOM   9274  C CG1 . ILE E 2 45  ? -24.036 -1.337  8.546   1.00 56.25  ? 45  ILE F CG1 1 
ATOM   9275  C CG2 . ILE E 2 45  ? -21.658 -1.059  7.880   1.00 49.27  ? 45  ILE F CG2 1 
ATOM   9276  C CD1 . ILE E 2 45  ? -24.309 -2.521  7.640   1.00 57.52  ? 45  ILE F CD1 1 
ATOM   9277  N N   . ASP E 2 46  ? -21.715 2.507   7.538   1.00 42.69  ? 46  ASP F N   1 
ATOM   9278  C CA  . ASP E 2 46  ? -20.587 3.358   7.147   1.00 44.85  ? 46  ASP F CA  1 
ATOM   9279  C C   . ASP E 2 46  ? -20.230 4.375   8.223   1.00 40.20  ? 46  ASP F C   1 
ATOM   9280  O O   . ASP E 2 46  ? -19.054 4.599   8.504   1.00 45.33  ? 46  ASP F O   1 
ATOM   9281  C CB  . ASP E 2 46  ? -20.887 4.076   5.823   1.00 50.78  ? 46  ASP F CB  1 
ATOM   9282  C CG  . ASP E 2 46  ? -20.855 3.136   4.622   1.00 57.38  ? 46  ASP F CG  1 
ATOM   9283  O OD1 . ASP E 2 46  ? -20.461 1.955   4.785   1.00 53.17  ? 46  ASP F OD1 1 
ATOM   9284  O OD2 . ASP E 2 46  ? -21.230 3.582   3.512   1.00 61.86  ? 46  ASP F OD2 1 
ATOM   9285  N N   . GLY E 2 47  ? -21.241 4.994   8.821   1.00 40.28  ? 47  GLY F N   1 
ATOM   9286  C CA  . GLY E 2 47  ? -21.017 5.964   9.891   1.00 39.34  ? 47  GLY F CA  1 
ATOM   9287  C C   . GLY E 2 47  ? -20.397 5.339   11.131  1.00 39.18  ? 47  GLY F C   1 
ATOM   9288  O O   . GLY E 2 47  ? -19.426 5.854   11.680  1.00 37.79  ? 47  GLY F O   1 
ATOM   9289  N N   . VAL E 2 48  ? -20.959 4.221   11.567  1.00 37.02  ? 48  VAL F N   1 
ATOM   9290  C CA  . VAL E 2 48  ? -20.475 3.533   12.758  1.00 37.56  ? 48  VAL F CA  1 
ATOM   9291  C C   . VAL E 2 48  ? -19.057 3.004   12.564  1.00 40.15  ? 48  VAL F C   1 
ATOM   9292  O O   . VAL E 2 48  ? -18.236 3.086   13.474  1.00 44.33  ? 48  VAL F O   1 
ATOM   9293  C CB  . VAL E 2 48  ? -21.427 2.391   13.156  1.00 37.88  ? 48  VAL F CB  1 
ATOM   9294  C CG1 . VAL E 2 48  ? -20.723 1.355   14.019  1.00 42.77  ? 48  VAL F CG1 1 
ATOM   9295  C CG2 . VAL E 2 48  ? -22.642 2.968   13.868  1.00 33.17  ? 48  VAL F CG2 1 
ATOM   9296  N N   . THR E 2 49  ? -18.768 2.472   11.380  1.00 41.94  ? 49  THR F N   1 
ATOM   9297  C CA  . THR E 2 49  ? -17.417 2.018   11.054  1.00 42.24  ? 49  THR F CA  1 
ATOM   9298  C C   . THR E 2 49  ? -16.434 3.194   11.054  1.00 42.61  ? 49  THR F C   1 
ATOM   9299  O O   . THR E 2 49  ? -15.301 3.061   11.527  1.00 42.12  ? 49  THR F O   1 
ATOM   9300  C CB  . THR E 2 49  ? -17.370 1.303   9.692   1.00 43.40  ? 49  THR F CB  1 
ATOM   9301  O OG1 . THR E 2 49  ? -18.268 0.188   9.711   1.00 51.24  ? 49  THR F OG1 1 
ATOM   9302  C CG2 . THR E 2 49  ? -15.965 0.788   9.399   1.00 40.96  ? 49  THR F CG2 1 
ATOM   9303  N N   . ASN E 2 50  ? -16.880 4.339   10.538  1.00 38.85  ? 50  ASN F N   1 
ATOM   9304  C CA  . ASN E 2 50  ? -16.071 5.555   10.543  1.00 38.06  ? 50  ASN F CA  1 
ATOM   9305  C C   . ASN E 2 50  ? -15.802 6.036   11.972  1.00 41.48  ? 50  ASN F C   1 
ATOM   9306  O O   . ASN E 2 50  ? -14.703 6.481   12.271  1.00 38.78  ? 50  ASN F O   1 
ATOM   9307  C CB  . ASN E 2 50  ? -16.754 6.666   9.738   1.00 44.92  ? 50  ASN F CB  1 
ATOM   9308  C CG  . ASN E 2 50  ? -15.763 7.519   8.951   1.00 56.61  ? 50  ASN F CG  1 
ATOM   9309  O OD1 . ASN E 2 50  ? -15.714 7.486   7.714   1.00 66.03  ? 50  ASN F OD1 1 
ATOM   9310  N ND2 . ASN E 2 50  ? -14.970 8.303   9.677   1.00 62.80  ? 50  ASN F ND2 1 
ATOM   9311  N N   . LYS E 2 51  ? -16.807 5.932   12.847  1.00 42.65  ? 51  LYS F N   1 
ATOM   9312  C CA  . LYS E 2 51  ? -16.661 6.302   14.261  1.00 37.42  ? 51  LYS F CA  1 
ATOM   9313  C C   . LYS E 2 51  ? -15.572 5.471   14.917  1.00 36.82  ? 51  LYS F C   1 
ATOM   9314  O O   . LYS E 2 51  ? -14.676 6.018   15.556  1.00 35.40  ? 51  LYS F O   1 
ATOM   9315  C CB  . LYS E 2 51  ? -17.978 6.115   15.020  1.00 39.81  ? 51  LYS F CB  1 
ATOM   9316  C CG  . LYS E 2 51  ? -17.869 6.322   16.528  1.00 45.15  ? 51  LYS F CG  1 
ATOM   9317  C CD  . LYS E 2 51  ? -19.194 6.121   17.251  1.00 47.16  ? 51  LYS F CD  1 
ATOM   9318  C CE  . LYS E 2 51  ? -20.192 7.214   16.921  1.00 46.01  ? 51  LYS F CE  1 
ATOM   9319  N NZ  . LYS E 2 51  ? -21.220 7.348   17.986  1.00 42.31  ? 51  LYS F NZ  1 
ATOM   9320  N N   . VAL E 2 52  ? -15.657 4.152   14.761  1.00 33.68  ? 52  VAL F N   1 
ATOM   9321  C CA  . VAL E 2 52  ? -14.665 3.249   15.346  1.00 39.85  ? 52  VAL F CA  1 
ATOM   9322  C C   . VAL E 2 52  ? -13.272 3.537   14.789  1.00 40.30  ? 52  VAL F C   1 
ATOM   9323  O O   . VAL E 2 52  ? -12.292 3.546   15.535  1.00 41.11  ? 52  VAL F O   1 
ATOM   9324  C CB  . VAL E 2 52  ? -15.020 1.768   15.097  1.00 39.33  ? 52  VAL F CB  1 
ATOM   9325  C CG1 . VAL E 2 52  ? -13.903 0.852   15.579  1.00 39.06  ? 52  VAL F CG1 1 
ATOM   9326  C CG2 . VAL E 2 52  ? -16.334 1.413   15.779  1.00 37.66  ? 52  VAL F CG2 1 
ATOM   9327  N N   . ASN E 2 53  ? -13.192 3.779   13.482  1.00 39.70  ? 53  ASN F N   1 
ATOM   9328  C CA  . ASN E 2 53  ? -11.907 4.038   12.831  1.00 39.05  ? 53  ASN F CA  1 
ATOM   9329  C C   . ASN E 2 53  ? -11.269 5.359   13.257  1.00 39.47  ? 53  ASN F C   1 
ATOM   9330  O O   . ASN E 2 53  ? -10.069 5.400   13.494  1.00 39.69  ? 53  ASN F O   1 
ATOM   9331  C CB  . ASN E 2 53  ? -12.029 3.968   11.304  1.00 36.08  ? 53  ASN F CB  1 
ATOM   9332  C CG  . ASN E 2 53  ? -12.067 2.539   10.785  1.00 36.64  ? 53  ASN F CG  1 
ATOM   9333  O OD1 . ASN E 2 53  ? -11.552 1.624   11.423  1.00 35.90  ? 53  ASN F OD1 1 
ATOM   9334  N ND2 . ASN E 2 53  ? -12.678 2.342   9.620   1.00 35.55  ? 53  ASN F ND2 1 
ATOM   9335  N N   . SER E 2 54  ? -12.054 6.427   13.370  1.00 40.11  ? 54  SER F N   1 
ATOM   9336  C CA  . SER E 2 54  ? -11.494 7.711   13.812  1.00 43.27  ? 54  SER F CA  1 
ATOM   9337  C C   . SER E 2 54  ? -10.961 7.609   15.244  1.00 45.81  ? 54  SER F C   1 
ATOM   9338  O O   . SER E 2 54  ? -9.880  8.120   15.535  1.00 48.78  ? 54  SER F O   1 
ATOM   9339  C CB  . SER E 2 54  ? -12.484 8.885   13.673  1.00 44.74  ? 54  SER F CB  1 
ATOM   9340  O OG  . SER E 2 54  ? -13.757 8.461   13.233  1.00 51.43  ? 54  SER F OG  1 
ATOM   9341  N N   . ILE E 2 55  ? -11.703 6.925   16.116  1.00 42.63  ? 55  ILE F N   1 
ATOM   9342  C CA  . ILE E 2 55  ? -11.285 6.727   17.511  1.00 38.72  ? 55  ILE F CA  1 
ATOM   9343  C C   . ILE E 2 55  ? -9.966  5.957   17.607  1.00 41.75  ? 55  ILE F C   1 
ATOM   9344  O O   . ILE E 2 55  ? -9.202  6.150   18.548  1.00 41.33  ? 55  ILE F O   1 
ATOM   9345  C CB  . ILE E 2 55  ? -12.376 5.999   18.332  1.00 37.40  ? 55  ILE F CB  1 
ATOM   9346  C CG1 . ILE E 2 55  ? -13.561 6.930   18.563  1.00 38.52  ? 55  ILE F CG1 1 
ATOM   9347  C CG2 . ILE E 2 55  ? -11.850 5.544   19.689  1.00 32.81  ? 55  ILE F CG2 1 
ATOM   9348  C CD1 . ILE E 2 55  ? -14.766 6.244   19.173  1.00 39.94  ? 55  ILE F CD1 1 
ATOM   9349  N N   . ILE E 2 56  ? -9.705  5.091   16.631  1.00 43.49  ? 56  ILE F N   1 
ATOM   9350  C CA  . ILE E 2 56  ? -8.440  4.362   16.545  1.00 43.71  ? 56  ILE F CA  1 
ATOM   9351  C C   . ILE E 2 56  ? -7.365  5.182   15.827  1.00 43.38  ? 56  ILE F C   1 
ATOM   9352  O O   . ILE E 2 56  ? -6.244  5.307   16.324  1.00 41.26  ? 56  ILE F O   1 
ATOM   9353  C CB  . ILE E 2 56  ? -8.624  3.027   15.794  1.00 42.66  ? 56  ILE F CB  1 
ATOM   9354  C CG1 . ILE E 2 56  ? -9.511  2.078   16.606  1.00 41.51  ? 56  ILE F CG1 1 
ATOM   9355  C CG2 . ILE E 2 56  ? -7.274  2.379   15.515  1.00 41.92  ? 56  ILE F CG2 1 
ATOM   9356  C CD1 . ILE E 2 56  ? -9.942  0.842   15.844  1.00 40.47  ? 56  ILE F CD1 1 
ATOM   9357  N N   . ASP E 2 57  ? -7.714  5.733   14.666  1.00 43.18  ? 57  ASP F N   1 
ATOM   9358  C CA  . ASP E 2 57  ? -6.740  6.371   13.770  1.00 45.68  ? 57  ASP F CA  1 
ATOM   9359  C C   . ASP E 2 57  ? -6.163  7.687   14.293  1.00 47.17  ? 57  ASP F C   1 
ATOM   9360  O O   . ASP E 2 57  ? -5.015  8.014   13.996  1.00 53.76  ? 57  ASP F O   1 
ATOM   9361  C CB  . ASP E 2 57  ? -7.353  6.606   12.379  1.00 49.54  ? 57  ASP F CB  1 
ATOM   9362  C CG  . ASP E 2 57  ? -7.654  5.306   11.631  1.00 51.79  ? 57  ASP F CG  1 
ATOM   9363  O OD1 . ASP E 2 57  ? -7.259  4.220   12.109  1.00 57.70  ? 57  ASP F OD1 1 
ATOM   9364  O OD2 . ASP E 2 57  ? -8.295  5.372   10.560  1.00 55.00  ? 57  ASP F OD2 1 
ATOM   9365  N N   . LYS E 2 58  ? -6.942  8.441   15.064  1.00 47.52  ? 58  LYS F N   1 
ATOM   9366  C CA  . LYS E 2 58  ? -6.481  9.736   15.572  1.00 44.75  ? 58  LYS F CA  1 
ATOM   9367  C C   . LYS E 2 58  ? -5.397  9.637   16.656  1.00 46.06  ? 58  LYS F C   1 
ATOM   9368  O O   . LYS E 2 58  ? -4.775  10.644  17.000  1.00 50.11  ? 58  LYS F O   1 
ATOM   9369  C CB  . LYS E 2 58  ? -7.661  10.558  16.097  1.00 46.38  ? 58  LYS F CB  1 
ATOM   9370  C CG  . LYS E 2 58  ? -8.635  11.006  15.020  1.00 49.52  ? 58  LYS F CG  1 
ATOM   9371  C CD  . LYS E 2 58  ? -7.979  11.913  13.988  1.00 49.94  ? 58  LYS F CD  1 
ATOM   9372  C CE  . LYS E 2 58  ? -9.010  12.497  13.037  1.00 50.68  ? 58  LYS F CE  1 
ATOM   9373  N NZ  . LYS E 2 58  ? -8.426  13.474  12.076  1.00 51.77  ? 58  LYS F NZ  1 
ATOM   9374  N N   . MET E 2 59  ? -5.172  8.438   17.189  1.00 45.37  ? 59  MET F N   1 
ATOM   9375  C CA  . MET E 2 59  ? -4.104  8.211   18.163  1.00 48.84  ? 59  MET F CA  1 
ATOM   9376  C C   . MET E 2 59  ? -2.746  8.130   17.476  1.00 58.07  ? 59  MET F C   1 
ATOM   9377  O O   . MET E 2 59  ? -2.587  7.444   16.468  1.00 63.51  ? 59  MET F O   1 
ATOM   9378  C CB  . MET E 2 59  ? -4.361  6.917   18.940  1.00 42.62  ? 59  MET F CB  1 
ATOM   9379  C CG  . MET E 2 59  ? -3.403  6.653   20.087  1.00 39.72  ? 59  MET F CG  1 
ATOM   9380  S SD  . MET E 2 59  ? -3.404  7.917   21.371  1.00 40.91  ? 59  MET F SD  1 
ATOM   9381  C CE  . MET E 2 59  ? -4.846  7.437   22.322  1.00 41.05  ? 59  MET F CE  1 
ATOM   9382  N N   . ASN E 2 60  ? -1.768  8.830   18.037  1.00 67.42  ? 60  ASN F N   1 
ATOM   9383  C CA  . ASN E 2 60  ? -0.408  8.794   17.540  1.00 81.97  ? 60  ASN F CA  1 
ATOM   9384  C C   . ASN E 2 60  ? 0.505   8.395   18.705  1.00 83.76  ? 60  ASN F C   1 
ATOM   9385  O O   . ASN E 2 60  ? 0.629   9.119   19.697  1.00 89.95  ? 60  ASN F O   1 
ATOM   9386  C CB  . ASN E 2 60  ? -0.086  10.145  16.866  1.00 85.82  ? 60  ASN F CB  1 
ATOM   9387  C CG  . ASN E 2 60  ? 0.686   11.111  17.761  1.00 85.01  ? 60  ASN F CG  1 
ATOM   9388  O OD1 . ASN E 2 60  ? 1.811   11.532  17.439  1.00 68.57  ? 60  ASN F OD1 1 
ATOM   9389  N ND2 . ASN E 2 60  ? 0.074   11.488  18.879  1.00 98.58  ? 60  ASN F ND2 1 
ATOM   9390  N N   . THR E 2 61  ? 1.065   7.191   18.615  1.00 86.56  ? 61  THR F N   1 
ATOM   9391  C CA  . THR E 2 61  ? 1.945   6.679   19.651  1.00 95.55  ? 61  THR F CA  1 
ATOM   9392  C C   . THR E 2 61  ? 3.362   6.729   19.110  1.00 85.89  ? 61  THR F C   1 
ATOM   9393  O O   . THR E 2 61  ? 3.667   6.099   18.096  1.00 100.49 ? 61  THR F O   1 
ATOM   9394  C CB  . THR E 2 61  ? 1.550   5.252   20.072  1.00 101.36 ? 61  THR F CB  1 
ATOM   9395  O OG1 . THR E 2 61  ? 1.501   4.394   18.924  1.00 93.22  ? 61  THR F OG1 1 
ATOM   9396  C CG2 . THR E 2 61  ? 0.179   5.269   20.746  1.00 104.52 ? 61  THR F CG2 1 
ATOM   9397  N N   . GLN E 2 62  ? 4.213   7.517   19.765  1.00 77.24  ? 62  GLN F N   1 
ATOM   9398  C CA  . GLN E 2 62  ? 5.610   7.615   19.369  1.00 65.41  ? 62  GLN F CA  1 
ATOM   9399  C C   . GLN E 2 62  ? 6.377   6.538   20.109  1.00 59.33  ? 62  GLN F C   1 
ATOM   9400  O O   . GLN E 2 62  ? 5.842   5.882   21.003  1.00 55.76  ? 62  GLN F O   1 
ATOM   9401  C CB  . GLN E 2 62  ? 6.186   8.994   19.690  1.00 66.13  ? 62  GLN F CB  1 
ATOM   9402  C CG  . GLN E 2 62  ? 5.703   10.085  18.749  1.00 79.26  ? 62  GLN F CG  1 
ATOM   9403  C CD  . GLN E 2 62  ? 5.841   11.480  19.333  1.00 84.02  ? 62  GLN F CD  1 
ATOM   9404  O OE1 . GLN E 2 62  ? 5.659   11.684  20.534  1.00 70.91  ? 62  GLN F OE1 1 
ATOM   9405  N NE2 . GLN E 2 62  ? 6.156   12.452  18.479  1.00 95.65  ? 62  GLN F NE2 1 
ATOM   9406  N N   . PHE E 2 63  ? 7.631   6.359   19.723  1.00 54.99  ? 63  PHE F N   1 
ATOM   9407  C CA  . PHE E 2 63  ? 8.513   5.412   20.383  1.00 51.40  ? 63  PHE F CA  1 
ATOM   9408  C C   . PHE E 2 63  ? 8.896   5.954   21.759  1.00 42.47  ? 63  PHE F C   1 
ATOM   9409  O O   . PHE E 2 63  ? 9.063   7.156   21.913  1.00 40.29  ? 63  PHE F O   1 
ATOM   9410  C CB  . PHE E 2 63  ? 9.770   5.202   19.530  1.00 50.94  ? 63  PHE F CB  1 
ATOM   9411  C CG  . PHE E 2 63  ? 10.770  4.266   20.142  1.00 54.52  ? 63  PHE F CG  1 
ATOM   9412  C CD1 . PHE E 2 63  ? 10.697  2.904   19.901  1.00 63.37  ? 63  PHE F CD1 1 
ATOM   9413  C CD2 . PHE E 2 63  ? 11.778  4.747   20.965  1.00 49.55  ? 63  PHE F CD2 1 
ATOM   9414  C CE1 . PHE E 2 63  ? 11.613  2.035   20.468  1.00 62.73  ? 63  PHE F CE1 1 
ATOM   9415  C CE2 . PHE E 2 63  ? 12.692  3.884   21.536  1.00 53.26  ? 63  PHE F CE2 1 
ATOM   9416  C CZ  . PHE E 2 63  ? 12.609  2.527   21.291  1.00 56.28  ? 63  PHE F CZ  1 
ATOM   9417  N N   . GLU E 2 64  ? 9.030   5.068   22.743  1.00 40.34  ? 64  GLU F N   1 
ATOM   9418  C CA  . GLU E 2 64  ? 9.613   5.436   24.032  1.00 48.96  ? 64  GLU F CA  1 
ATOM   9419  C C   . GLU E 2 64  ? 10.072  4.252   24.848  1.00 44.57  ? 64  GLU F C   1 
ATOM   9420  O O   . GLU E 2 64  ? 9.619   3.136   24.639  1.00 47.11  ? 64  GLU F O   1 
ATOM   9421  C CB  . GLU E 2 64  ? 8.627   6.256   24.852  1.00 55.42  ? 64  GLU F CB  1 
ATOM   9422  C CG  . GLU E 2 64  ? 8.908   7.750   24.799  1.00 62.07  ? 64  GLU F CG  1 
ATOM   9423  C CD  . GLU E 2 64  ? 7.679   8.558   24.464  1.00 64.19  ? 64  GLU F CD  1 
ATOM   9424  O OE1 . GLU E 2 64  ? 6.588   8.232   24.976  1.00 89.06  ? 64  GLU F OE1 1 
ATOM   9425  O OE2 . GLU E 2 64  ? 7.805   9.517   23.683  1.00 52.74  ? 64  GLU F OE2 1 
ATOM   9426  N N   . ALA E 2 65  ? 10.969  4.523   25.790  1.00 52.05  ? 65  ALA F N   1 
ATOM   9427  C CA  . ALA E 2 65  ? 11.544  3.499   26.641  1.00 54.95  ? 65  ALA F CA  1 
ATOM   9428  C C   . ALA E 2 65  ? 11.149  3.765   28.084  1.00 51.18  ? 65  ALA F C   1 
ATOM   9429  O O   . ALA E 2 65  ? 11.883  4.406   28.835  1.00 53.46  ? 65  ALA F O   1 
ATOM   9430  C CB  . ALA E 2 65  ? 13.056  3.481   26.483  1.00 57.24  ? 65  ALA F CB  1 
ATOM   9431  N N   . VAL E 2 66  ? 9.957   3.304   28.450  1.00 56.07  ? 66  VAL F N   1 
ATOM   9432  C CA  . VAL E 2 66  ? 9.544   3.315   29.843  1.00 56.61  ? 66  VAL F CA  1 
ATOM   9433  C C   . VAL E 2 66  ? 10.322  2.211   30.548  1.00 51.24  ? 66  VAL F C   1 
ATOM   9434  O O   . VAL E 2 66  ? 10.006  1.035   30.421  1.00 53.27  ? 66  VAL F O   1 
ATOM   9435  C CB  . VAL E 2 66  ? 8.028   3.111   30.014  1.00 53.92  ? 66  VAL F CB  1 
ATOM   9436  C CG1 . VAL E 2 66  ? 7.664   3.122   31.491  1.00 53.16  ? 66  VAL F CG1 1 
ATOM   9437  C CG2 . VAL E 2 66  ? 7.256   4.184   29.259  1.00 52.04  ? 66  VAL F CG2 1 
ATOM   9438  N N   . GLY E 2 67  ? 11.378  2.614   31.246  1.00 52.73  ? 67  GLY F N   1 
ATOM   9439  C CA  . GLY E 2 67  ? 12.166  1.719   32.082  1.00 54.16  ? 67  GLY F CA  1 
ATOM   9440  C C   . GLY E 2 67  ? 12.770  2.488   33.244  1.00 58.12  ? 67  GLY F C   1 
ATOM   9441  O O   . GLY E 2 67  ? 13.229  3.619   33.072  1.00 84.97  ? 67  GLY F O   1 
ATOM   9442  N N   . ARG E 2 68  ? 12.785  1.873   34.423  1.00 54.56  ? 68  ARG F N   1 
ATOM   9443  C CA  . ARG E 2 68  ? 13.302  2.527   35.633  1.00 59.43  ? 68  ARG F CA  1 
ATOM   9444  C C   . ARG E 2 68  ? 14.811  2.369   35.830  1.00 54.20  ? 68  ARG F C   1 
ATOM   9445  O O   . ARG E 2 68  ? 15.288  1.287   36.158  1.00 58.93  ? 68  ARG F O   1 
ATOM   9446  C CB  . ARG E 2 68  ? 12.547  2.071   36.890  1.00 65.77  ? 68  ARG F CB  1 
ATOM   9447  C CG  . ARG E 2 68  ? 11.477  3.086   37.280  1.00 73.32  ? 68  ARG F CG  1 
ATOM   9448  C CD  . ARG E 2 68  ? 10.422  2.577   38.261  1.00 74.56  ? 68  ARG F CD  1 
ATOM   9449  N NE  . ARG E 2 68  ? 9.475   1.621   37.696  1.00 73.11  ? 68  ARG F NE  1 
ATOM   9450  C CZ  . ARG E 2 68  ? 8.477   1.924   36.865  1.00 74.21  ? 68  ARG F CZ  1 
ATOM   9451  N NH1 . ARG E 2 68  ? 8.286   3.163   36.427  1.00 62.63  ? 68  ARG F NH1 1 
ATOM   9452  N NH2 . ARG E 2 68  ? 7.660   0.964   36.450  1.00 85.43  ? 68  ARG F NH2 1 
ATOM   9453  N N   . GLU E 2 69  ? 15.546  3.469   35.658  1.00 53.62  ? 69  GLU F N   1 
ATOM   9454  C CA  . GLU E 2 69  ? 17.005  3.451   35.729  1.00 53.42  ? 69  GLU F CA  1 
ATOM   9455  C C   . GLU E 2 69  ? 17.575  4.520   36.676  1.00 49.38  ? 69  GLU F C   1 
ATOM   9456  O O   . GLU E 2 69  ? 18.597  5.140   36.391  1.00 43.21  ? 69  GLU F O   1 
ATOM   9457  C CB  . GLU E 2 69  ? 17.626  3.527   34.316  1.00 63.39  ? 69  GLU F CB  1 
ATOM   9458  C CG  . GLU E 2 69  ? 16.952  4.462   33.315  1.00 69.42  ? 69  GLU F CG  1 
ATOM   9459  C CD  . GLU E 2 69  ? 17.407  4.219   31.873  1.00 76.58  ? 69  GLU F CD  1 
ATOM   9460  O OE1 . GLU E 2 69  ? 16.657  4.592   30.946  1.00 76.36  ? 69  GLU F OE1 1 
ATOM   9461  O OE2 . GLU E 2 69  ? 18.504  3.653   31.655  1.00 77.36  ? 69  GLU F OE2 1 
ATOM   9462  N N   . PHE E 2 70  ? 16.929  4.694   37.827  1.00 52.66  ? 70  PHE F N   1 
ATOM   9463  C CA  . PHE E 2 70  ? 17.446  5.559   38.892  1.00 53.07  ? 70  PHE F CA  1 
ATOM   9464  C C   . PHE E 2 70  ? 17.883  4.756   40.114  1.00 51.06  ? 70  PHE F C   1 
ATOM   9465  O O   . PHE E 2 70  ? 17.220  3.793   40.505  1.00 50.94  ? 70  PHE F O   1 
ATOM   9466  C CB  . PHE E 2 70  ? 16.401  6.598   39.288  1.00 50.46  ? 70  PHE F CB  1 
ATOM   9467  C CG  . PHE E 2 70  ? 16.087  7.559   38.189  1.00 49.35  ? 70  PHE F CG  1 
ATOM   9468  C CD1 . PHE E 2 70  ? 14.855  7.544   37.553  1.00 50.63  ? 70  PHE F CD1 1 
ATOM   9469  C CD2 . PHE E 2 70  ? 17.052  8.459   37.759  1.00 52.43  ? 70  PHE F CD2 1 
ATOM   9470  C CE1 . PHE E 2 70  ? 14.580  8.427   36.523  1.00 51.76  ? 70  PHE F CE1 1 
ATOM   9471  C CE2 . PHE E 2 70  ? 16.783  9.342   36.727  1.00 50.32  ? 70  PHE F CE2 1 
ATOM   9472  C CZ  . PHE E 2 70  ? 15.546  9.325   36.108  1.00 51.80  ? 70  PHE F CZ  1 
ATOM   9473  N N   . ASN E 2 71  ? 18.997  5.169   40.716  1.00 47.87  ? 71  ASN F N   1 
ATOM   9474  C CA  . ASN E 2 71  ? 19.593  4.436   41.832  1.00 49.05  ? 71  ASN F CA  1 
ATOM   9475  C C   . ASN E 2 71  ? 18.978  4.838   43.171  1.00 48.91  ? 71  ASN F C   1 
ATOM   9476  O O   . ASN E 2 71  ? 18.111  5.707   43.228  1.00 43.74  ? 71  ASN F O   1 
ATOM   9477  C CB  . ASN E 2 71  ? 21.124  4.599   41.839  1.00 48.54  ? 71  ASN F CB  1 
ATOM   9478  C CG  . ASN E 2 71  ? 21.573  6.001   42.216  1.00 51.65  ? 71  ASN F CG  1 
ATOM   9479  O OD1 . ASN E 2 71  ? 21.156  6.549   43.231  1.00 48.57  ? 71  ASN F OD1 1 
ATOM   9480  N ND2 . ASN E 2 71  ? 22.443  6.582   41.398  1.00 60.13  ? 71  ASN F ND2 1 
ATOM   9481  N N   . ASN E 2 72  ? 19.447  4.204   44.243  1.00 49.16  ? 72  ASN F N   1 
ATOM   9482  C CA  . ASN E 2 72  ? 18.876  4.370   45.578  1.00 47.22  ? 72  ASN F CA  1 
ATOM   9483  C C   . ASN E 2 72  ? 19.111  5.759   46.215  1.00 48.92  ? 72  ASN F C   1 
ATOM   9484  O O   . ASN E 2 72  ? 18.449  6.117   47.192  1.00 49.73  ? 72  ASN F O   1 
ATOM   9485  C CB  . ASN E 2 72  ? 19.395  3.227   46.464  1.00 53.88  ? 72  ASN F CB  1 
ATOM   9486  C CG  . ASN E 2 72  ? 18.787  3.223   47.864  1.00 57.66  ? 72  ASN F CG  1 
ATOM   9487  O OD1 . ASN E 2 72  ? 19.500  3.295   48.880  1.00 60.67  ? 72  ASN F OD1 1 
ATOM   9488  N ND2 . ASN E 2 72  ? 17.464  3.138   47.926  1.00 57.65  ? 72  ASN F ND2 1 
ATOM   9489  N N   . LEU E 2 73  ? 20.028  6.548   45.653  1.00 47.02  ? 73  LEU F N   1 
ATOM   9490  C CA  . LEU E 2 73  ? 20.187  7.956   46.050  1.00 46.46  ? 73  LEU F CA  1 
ATOM   9491  C C   . LEU E 2 73  ? 19.587  8.920   45.013  1.00 41.54  ? 73  LEU F C   1 
ATOM   9492  O O   . LEU E 2 73  ? 19.970  10.089  44.948  1.00 38.14  ? 73  LEU F O   1 
ATOM   9493  C CB  . LEU E 2 73  ? 21.667  8.285   46.298  1.00 51.20  ? 73  LEU F CB  1 
ATOM   9494  C CG  . LEU E 2 73  ? 22.289  7.727   47.586  1.00 53.14  ? 73  LEU F CG  1 
ATOM   9495  C CD1 . LEU E 2 73  ? 23.797  7.927   47.568  1.00 53.14  ? 73  LEU F CD1 1 
ATOM   9496  C CD2 . LEU E 2 73  ? 21.683  8.376   48.826  1.00 48.38  ? 73  LEU F CD2 1 
ATOM   9497  N N   . GLU E 2 74  ? 18.638  8.428   44.219  1.00 38.17  ? 74  GLU F N   1 
ATOM   9498  C CA  . GLU E 2 74  ? 17.956  9.244   43.221  1.00 41.01  ? 74  GLU F CA  1 
ATOM   9499  C C   . GLU E 2 74  ? 16.441  9.029   43.304  1.00 40.88  ? 74  GLU F C   1 
ATOM   9500  O O   . GLU E 2 74  ? 15.746  9.074   42.288  1.00 42.92  ? 74  GLU F O   1 
ATOM   9501  C CB  . GLU E 2 74  ? 18.460  8.893   41.812  1.00 42.50  ? 74  GLU F CB  1 
ATOM   9502  C CG  . GLU E 2 74  ? 19.905  9.289   41.529  1.00 43.08  ? 74  GLU F CG  1 
ATOM   9503  C CD  . GLU E 2 74  ? 20.407  8.771   40.184  1.00 45.93  ? 74  GLU F CD  1 
ATOM   9504  O OE1 . GLU E 2 74  ? 20.066  7.631   39.806  1.00 41.87  ? 74  GLU F OE1 1 
ATOM   9505  O OE2 . GLU E 2 74  ? 21.156  9.500   39.496  1.00 47.29  ? 74  GLU F OE2 1 
ATOM   9506  N N   . ARG E 2 75  ? 15.931  8.825   44.515  1.00 37.60  ? 75  ARG F N   1 
ATOM   9507  C CA  . ARG E 2 75  ? 14.534  8.442   44.709  1.00 41.96  ? 75  ARG F CA  1 
ATOM   9508  C C   . ARG E 2 75  ? 13.565  9.613   44.518  1.00 38.81  ? 75  ARG F C   1 
ATOM   9509  O O   . ARG E 2 75  ? 12.400  9.413   44.167  1.00 40.50  ? 75  ARG F O   1 
ATOM   9510  C CB  . ARG E 2 75  ? 14.341  7.794   46.085  1.00 49.45  ? 75  ARG F CB  1 
ATOM   9511  C CG  . ARG E 2 75  ? 15.358  6.692   46.396  1.00 60.33  ? 75  ARG F CG  1 
ATOM   9512  C CD  . ARG E 2 75  ? 14.754  5.541   47.184  1.00 74.84  ? 75  ARG F CD  1 
ATOM   9513  N NE  . ARG E 2 75  ? 14.055  4.574   46.343  1.00 88.52  ? 75  ARG F NE  1 
ATOM   9514  C CZ  . ARG E 2 75  ? 13.216  3.659   46.820  1.00 101.03 ? 75  ARG F CZ  1 
ATOM   9515  N NH1 . ARG E 2 75  ? 12.967  3.577   48.129  1.00 113.47 ? 75  ARG F NH1 1 
ATOM   9516  N NH2 . ARG E 2 75  ? 12.622  2.820   45.985  1.00 100.82 ? 75  ARG F NH2 1 
ATOM   9517  N N   . ARG E 2 76  ? 14.042  10.831  44.736  1.00 33.84  ? 76  ARG F N   1 
ATOM   9518  C CA  . ARG E 2 76  ? 13.237  12.011  44.445  1.00 33.02  ? 76  ARG F CA  1 
ATOM   9519  C C   . ARG E 2 76  ? 12.944  12.139  42.948  1.00 36.98  ? 76  ARG F C   1 
ATOM   9520  O O   . ARG E 2 76  ? 11.857  12.558  42.565  1.00 41.81  ? 76  ARG F O   1 
ATOM   9521  C CB  . ARG E 2 76  ? 13.931  13.267  44.942  1.00 31.81  ? 76  ARG F CB  1 
ATOM   9522  C CG  . ARG E 2 76  ? 14.035  13.363  46.456  1.00 30.30  ? 76  ARG F CG  1 
ATOM   9523  C CD  . ARG E 2 76  ? 14.899  14.546  46.832  1.00 31.08  ? 76  ARG F CD  1 
ATOM   9524  N NE  . ARG E 2 76  ? 16.245  14.423  46.275  1.00 29.11  ? 76  ARG F NE  1 
ATOM   9525  C CZ  . ARG E 2 76  ? 17.058  15.441  46.010  1.00 28.20  ? 76  ARG F CZ  1 
ATOM   9526  N NH1 . ARG E 2 76  ? 16.676  16.693  46.226  1.00 31.52  ? 76  ARG F NH1 1 
ATOM   9527  N NH2 . ARG E 2 76  ? 18.265  15.207  45.513  1.00 27.85  ? 76  ARG F NH2 1 
ATOM   9528  N N   . ILE E 2 77  ? 13.919  11.781  42.111  1.00 39.34  ? 77  ILE F N   1 
ATOM   9529  C CA  . ILE E 2 77  ? 13.741  11.799  40.657  1.00 37.99  ? 77  ILE F CA  1 
ATOM   9530  C C   . ILE E 2 77  ? 12.858  10.638  40.227  1.00 38.06  ? 77  ILE F C   1 
ATOM   9531  O O   . ILE E 2 77  ? 11.995  10.801  39.372  1.00 41.93  ? 77  ILE F O   1 
ATOM   9532  C CB  . ILE E 2 77  ? 15.081  11.720  39.897  1.00 39.31  ? 77  ILE F CB  1 
ATOM   9533  C CG1 . ILE E 2 77  ? 15.990  12.892  40.291  1.00 43.60  ? 77  ILE F CG1 1 
ATOM   9534  C CG2 . ILE E 2 77  ? 14.843  11.722  38.395  1.00 32.84  ? 77  ILE F CG2 1 
ATOM   9535  C CD1 . ILE E 2 77  ? 17.360  12.862  39.650  1.00 43.56  ? 77  ILE F CD1 1 
ATOM   9536  N N   . GLU E 2 78  ? 13.059  9.473   40.836  1.00 39.95  ? 78  GLU F N   1 
ATOM   9537  C CA  . GLU E 2 78  ? 12.192  8.315   40.590  1.00 43.46  ? 78  GLU F CA  1 
ATOM   9538  C C   . GLU E 2 78  ? 10.740  8.626   40.964  1.00 41.96  ? 78  GLU F C   1 
ATOM   9539  O O   . GLU E 2 78  ? 9.820   8.219   40.260  1.00 45.62  ? 78  GLU F O   1 
ATOM   9540  C CB  . GLU E 2 78  ? 12.699  7.085   41.364  1.00 44.69  ? 78  GLU F CB  1 
ATOM   9541  C CG  . GLU E 2 78  ? 11.957  5.764   41.132  1.00 50.02  ? 78  GLU F CG  1 
ATOM   9542  C CD  . GLU E 2 78  ? 12.250  4.726   42.211  1.00 62.26  ? 78  GLU F CD  1 
ATOM   9543  O OE1 . GLU E 2 78  ? 12.258  5.097   43.406  1.00 62.18  ? 78  GLU F OE1 1 
ATOM   9544  O OE2 . GLU E 2 78  ? 12.461  3.534   41.874  1.00 69.01  ? 78  GLU F OE2 1 
ATOM   9545  N N   . ASN E 2 79  ? 10.537  9.352   42.062  1.00 37.07  ? 79  ASN F N   1 
ATOM   9546  C CA  . ASN E 2 79  ? 9.195   9.755   42.460  1.00 34.96  ? 79  ASN F CA  1 
ATOM   9547  C C   . ASN E 2 79  ? 8.584   10.737  41.465  1.00 34.57  ? 79  ASN F C   1 
ATOM   9548  O O   . ASN E 2 79  ? 7.388   10.687  41.177  1.00 33.50  ? 79  ASN F O   1 
ATOM   9549  C CB  . ASN E 2 79  ? 9.203   10.372  43.858  1.00 38.31  ? 79  ASN F CB  1 
ATOM   9550  C CG  . ASN E 2 79  ? 7.831   10.839  44.284  1.00 37.10  ? 79  ASN F CG  1 
ATOM   9551  O OD1 . ASN E 2 79  ? 6.864   10.084  44.229  1.00 42.11  ? 79  ASN F OD1 1 
ATOM   9552  N ND2 . ASN E 2 79  ? 7.732   12.097  44.673  1.00 40.89  ? 79  ASN F ND2 1 
ATOM   9553  N N   . LEU E 2 80  ? 9.408   11.638  40.947  1.00 33.51  ? 80  LEU F N   1 
ATOM   9554  C CA  . LEU E 2 80  ? 8.963   12.570  39.915  1.00 34.49  ? 80  LEU F CA  1 
ATOM   9555  C C   . LEU E 2 80  ? 8.480   11.803  38.681  1.00 33.17  ? 80  LEU F C   1 
ATOM   9556  O O   . LEU E 2 80  ? 7.449   12.139  38.101  1.00 33.67  ? 80  LEU F O   1 
ATOM   9557  C CB  . LEU E 2 80  ? 10.093  13.536  39.557  1.00 37.45  ? 80  LEU F CB  1 
ATOM   9558  C CG  . LEU E 2 80  ? 9.854   14.578  38.475  1.00 40.67  ? 80  LEU F CG  1 
ATOM   9559  C CD1 . LEU E 2 80  ? 8.656   15.441  38.820  1.00 37.36  ? 80  LEU F CD1 1 
ATOM   9560  C CD2 . LEU E 2 80  ? 11.105  15.430  38.319  1.00 45.82  ? 80  LEU F CD2 1 
ATOM   9561  N N   . ASN E 2 81  ? 9.216   10.765  38.295  1.00 31.23  ? 81  ASN F N   1 
ATOM   9562  C CA  . ASN E 2 81  ? 8.800   9.904   37.196  1.00 29.74  ? 81  ASN F CA  1 
ATOM   9563  C C   . ASN E 2 81  ? 7.518   9.150   37.519  1.00 30.12  ? 81  ASN F C   1 
ATOM   9564  O O   . ASN E 2 81  ? 6.666   8.977   36.655  1.00 30.99  ? 81  ASN F O   1 
ATOM   9565  C CB  . ASN E 2 81  ? 9.906   8.915   36.831  1.00 31.48  ? 81  ASN F CB  1 
ATOM   9566  C CG  . ASN E 2 81  ? 9.502   7.971   35.705  1.00 33.00  ? 81  ASN F CG  1 
ATOM   9567  O OD1 . ASN E 2 81  ? 9.292   6.785   35.932  1.00 32.81  ? 81  ASN F OD1 1 
ATOM   9568  N ND2 . ASN E 2 81  ? 9.377   8.495   34.497  1.00 34.84  ? 81  ASN F ND2 1 
ATOM   9569  N N   . LYS E 2 82  ? 7.385   8.690   38.760  1.00 34.62  ? 82  LYS F N   1 
ATOM   9570  C CA  . LYS E 2 82  ? 6.171   7.989   39.190  1.00 35.61  ? 82  LYS F CA  1 
ATOM   9571  C C   . LYS E 2 82  ? 4.945   8.897   39.084  1.00 34.70  ? 82  LYS F C   1 
ATOM   9572  O O   . LYS E 2 82  ? 3.917   8.485   38.558  1.00 35.72  ? 82  LYS F O   1 
ATOM   9573  C CB  . LYS E 2 82  ? 6.313   7.457   40.619  1.00 35.69  ? 82  LYS F CB  1 
ATOM   9574  C CG  . LYS E 2 82  ? 5.031   6.859   41.194  1.00 38.33  ? 82  LYS F CG  1 
ATOM   9575  C CD  . LYS E 2 82  ? 5.183   6.462   42.659  1.00 39.49  ? 82  LYS F CD  1 
ATOM   9576  C CE  . LYS E 2 82  ? 3.831   6.331   43.340  1.00 40.80  ? 82  LYS F CE  1 
ATOM   9577  N NZ  . LYS E 2 82  ? 2.910   5.434   42.581  1.00 45.16  ? 82  LYS F NZ  1 
ATOM   9578  N N   . LYS E 2 83  ? 5.056   10.126  39.584  1.00 36.93  ? 83  LYS F N   1 
ATOM   9579  C CA  . LYS E 2 83  ? 3.966   11.102  39.473  1.00 35.20  ? 83  LYS F CA  1 
ATOM   9580  C C   . LYS E 2 83  ? 3.553   11.313  38.011  1.00 37.47  ? 83  LYS F C   1 
ATOM   9581  O O   . LYS E 2 83  ? 2.367   11.354  37.702  1.00 39.15  ? 83  LYS F O   1 
ATOM   9582  C CB  . LYS E 2 83  ? 4.357   12.434  40.110  1.00 33.72  ? 83  LYS F CB  1 
ATOM   9583  C CG  . LYS E 2 83  ? 4.398   12.383  41.627  1.00 37.88  ? 83  LYS F CG  1 
ATOM   9584  C CD  . LYS E 2 83  ? 4.638   13.748  42.252  1.00 39.57  ? 83  LYS F CD  1 
ATOM   9585  C CE  . LYS E 2 83  ? 6.091   14.171  42.155  1.00 47.44  ? 83  LYS F CE  1 
ATOM   9586  N NZ  . LYS E 2 83  ? 6.285   15.520  42.764  1.00 46.53  ? 83  LYS F NZ  1 
ATOM   9587  N N   . MET E 2 84  ? 4.535   11.405  37.119  1.00 36.05  ? 84  MET F N   1 
ATOM   9588  C CA  . MET E 2 84  ? 4.280   11.553  35.690  1.00 34.69  ? 84  MET F CA  1 
ATOM   9589  C C   . MET E 2 84  ? 3.567   10.337  35.099  1.00 36.57  ? 84  MET F C   1 
ATOM   9590  O O   . MET E 2 84  ? 2.509   10.485  34.487  1.00 35.19  ? 84  MET F O   1 
ATOM   9591  C CB  . MET E 2 84  ? 5.591   11.784  34.943  1.00 39.66  ? 84  MET F CB  1 
ATOM   9592  C CG  . MET E 2 84  ? 5.415   12.263  33.512  1.00 45.90  ? 84  MET F CG  1 
ATOM   9593  S SD  . MET E 2 84  ? 6.799   11.770  32.474  1.00 56.03  ? 84  MET F SD  1 
ATOM   9594  C CE  . MET E 2 84  ? 6.423   10.039  32.207  1.00 51.38  ? 84  MET F CE  1 
ATOM   9595  N N   . GLU E 2 85  ? 4.141   9.144   35.273  1.00 37.23  ? 85  GLU F N   1 
ATOM   9596  C CA  . GLU E 2 85  ? 3.532   7.908   34.745  1.00 39.10  ? 85  GLU F CA  1 
ATOM   9597  C C   . GLU E 2 85  ? 2.107   7.710   35.256  1.00 36.64  ? 85  GLU F C   1 
ATOM   9598  O O   . GLU E 2 85  ? 1.198   7.405   34.482  1.00 33.95  ? 85  GLU F O   1 
ATOM   9599  C CB  . GLU E 2 85  ? 4.358   6.672   35.103  1.00 42.74  ? 85  GLU F CB  1 
ATOM   9600  C CG  . GLU E 2 85  ? 5.570   6.445   34.214  1.00 50.66  ? 85  GLU F CG  1 
ATOM   9601  C CD  . GLU E 2 85  ? 6.270   5.122   34.483  1.00 55.80  ? 85  GLU F CD  1 
ATOM   9602  O OE1 . GLU E 2 85  ? 5.594   4.121   34.807  1.00 58.91  ? 85  GLU F OE1 1 
ATOM   9603  O OE2 . GLU E 2 85  ? 7.512   5.077   34.371  1.00 64.81  ? 85  GLU F OE2 1 
ATOM   9604  N N   . ASP E 2 86  ? 1.927   7.885   36.563  1.00 36.08  ? 86  ASP F N   1 
ATOM   9605  C CA  . ASP E 2 86  ? 0.606   7.816   37.186  1.00 33.92  ? 86  ASP F CA  1 
ATOM   9606  C C   . ASP E 2 86  ? -0.331  8.898   36.640  1.00 35.24  ? 86  ASP F C   1 
ATOM   9607  O O   . ASP E 2 86  ? -1.515  8.636   36.404  1.00 38.08  ? 86  ASP F O   1 
ATOM   9608  C CB  . ASP E 2 86  ? 0.725   7.936   38.706  1.00 33.52  ? 86  ASP F CB  1 
ATOM   9609  C CG  . ASP E 2 86  ? 1.372   6.711   39.340  1.00 39.76  ? 86  ASP F CG  1 
ATOM   9610  O OD1 . ASP E 2 86  ? 1.703   5.750   38.607  1.00 43.08  ? 86  ASP F OD1 1 
ATOM   9611  O OD2 . ASP E 2 86  ? 1.560   6.707   40.575  1.00 44.16  ? 86  ASP F OD2 1 
ATOM   9612  N N   . GLY E 2 87  ? 0.201   10.102  36.425  1.00 29.84  ? 87  GLY F N   1 
ATOM   9613  C CA  . GLY E 2 87  ? -0.572  11.198  35.844  1.00 29.02  ? 87  GLY F CA  1 
ATOM   9614  C C   . GLY E 2 87  ? -1.155  10.837  34.488  1.00 30.76  ? 87  GLY F C   1 
ATOM   9615  O O   . GLY E 2 87  ? -2.358  10.975  34.269  1.00 34.12  ? 87  GLY F O   1 
ATOM   9616  N N   . PHE E 2 88  ? -0.316  10.342  33.582  1.00 27.79  ? 88  PHE F N   1 
ATOM   9617  C CA  . PHE E 2 88  ? -0.791  9.975   32.249  1.00 28.80  ? 88  PHE F CA  1 
ATOM   9618  C C   . PHE E 2 88  ? -1.743  8.788   32.283  1.00 26.46  ? 88  PHE F C   1 
ATOM   9619  O O   . PHE E 2 88  ? -2.725  8.767   31.547  1.00 25.75  ? 88  PHE F O   1 
ATOM   9620  C CB  . PHE E 2 88  ? 0.374   9.725   31.281  1.00 30.65  ? 88  PHE F CB  1 
ATOM   9621  C CG  . PHE E 2 88  ? 1.061   10.982  30.833  1.00 31.41  ? 88  PHE F CG  1 
ATOM   9622  C CD1 . PHE E 2 88  ? 2.408   11.191  31.097  1.00 33.66  ? 88  PHE F CD1 1 
ATOM   9623  C CD2 . PHE E 2 88  ? 0.355   11.967  30.159  1.00 35.03  ? 88  PHE F CD2 1 
ATOM   9624  C CE1 . PHE E 2 88  ? 3.041   12.355  30.689  1.00 36.36  ? 88  PHE F CE1 1 
ATOM   9625  C CE2 . PHE E 2 88  ? 0.980   13.135  29.749  1.00 40.08  ? 88  PHE F CE2 1 
ATOM   9626  C CZ  . PHE E 2 88  ? 2.325   13.332  30.016  1.00 39.89  ? 88  PHE F CZ  1 
ATOM   9627  N N   . LEU E 2 89  ? -1.478  7.815   33.147  1.00 30.40  ? 89  LEU F N   1 
ATOM   9628  C CA  . LEU E 2 89  ? -2.401  6.688   33.322  1.00 37.57  ? 89  LEU F CA  1 
ATOM   9629  C C   . LEU E 2 89  ? -3.792  7.172   33.746  1.00 40.30  ? 89  LEU F C   1 
ATOM   9630  O O   . LEU E 2 89  ? -4.801  6.656   33.266  1.00 43.70  ? 89  LEU F O   1 
ATOM   9631  C CB  . LEU E 2 89  ? -1.867  5.681   34.345  1.00 40.72  ? 89  LEU F CB  1 
ATOM   9632  C CG  . LEU E 2 89  ? -2.674  4.394   34.559  1.00 46.26  ? 89  LEU F CG  1 
ATOM   9633  C CD1 . LEU E 2 89  ? -2.589  3.507   33.327  1.00 50.25  ? 89  LEU F CD1 1 
ATOM   9634  C CD2 . LEU E 2 89  ? -2.168  3.650   35.784  1.00 45.67  ? 89  LEU F CD2 1 
ATOM   9635  N N   . ASP E 2 90  ? -3.840  8.162   34.632  1.00 37.39  ? 90  ASP F N   1 
ATOM   9636  C CA  . ASP E 2 90  ? -5.112  8.723   35.082  1.00 39.24  ? 90  ASP F CA  1 
ATOM   9637  C C   . ASP E 2 90  ? -5.814  9.502   33.966  1.00 35.46  ? 90  ASP F C   1 
ATOM   9638  O O   . ASP E 2 90  ? -7.025  9.383   33.794  1.00 33.98  ? 90  ASP F O   1 
ATOM   9639  C CB  . ASP E 2 90  ? -4.911  9.623   36.306  1.00 44.54  ? 90  ASP F CB  1 
ATOM   9640  C CG  . ASP E 2 90  ? -4.483  8.848   37.551  1.00 49.09  ? 90  ASP F CG  1 
ATOM   9641  O OD1 . ASP E 2 90  ? -4.586  7.601   37.563  1.00 49.28  ? 90  ASP F OD1 1 
ATOM   9642  O OD2 . ASP E 2 90  ? -4.047  9.496   38.530  1.00 54.36  ? 90  ASP F OD2 1 
ATOM   9643  N N   . VAL E 2 91  ? -5.056  10.292  33.210  1.00 33.39  ? 91  VAL F N   1 
ATOM   9644  C CA  . VAL E 2 91  ? -5.637  11.074  32.117  1.00 31.59  ? 91  VAL F CA  1 
ATOM   9645  C C   . VAL E 2 91  ? -6.232  10.152  31.059  1.00 29.93  ? 91  VAL F C   1 
ATOM   9646  O O   . VAL E 2 91  ? -7.397  10.298  30.701  1.00 29.05  ? 91  VAL F O   1 
ATOM   9647  C CB  . VAL E 2 91  ? -4.612  12.047  31.488  1.00 31.64  ? 91  VAL F CB  1 
ATOM   9648  C CG1 . VAL E 2 91  ? -5.069  12.523  30.118  1.00 28.85  ? 91  VAL F CG1 1 
ATOM   9649  C CG2 . VAL E 2 91  ? -4.401  13.240  32.409  1.00 30.16  ? 91  VAL F CG2 1 
ATOM   9650  N N   . TRP E 2 92  ? -5.444  9.192   30.582  1.00 28.39  ? 92  TRP F N   1 
ATOM   9651  C CA  . TRP E 2 92  ? -5.907  8.280   29.536  1.00 27.37  ? 92  TRP F CA  1 
ATOM   9652  C C   . TRP E 2 92  ? -7.037  7.404   29.977  1.00 27.26  ? 92  TRP F C   1 
ATOM   9653  O O   . TRP E 2 92  ? -7.956  7.145   29.206  1.00 32.69  ? 92  TRP F O   1 
ATOM   9654  C CB  . TRP E 2 92  ? -4.760  7.421   29.011  1.00 28.58  ? 92  TRP F CB  1 
ATOM   9655  C CG  . TRP E 2 92  ? -3.788  8.188   28.153  1.00 26.84  ? 92  TRP F CG  1 
ATOM   9656  C CD1 . TRP E 2 92  ? -2.438  8.403   28.384  1.00 26.35  ? 92  TRP F CD1 1 
ATOM   9657  C CD2 . TRP E 2 92  ? -4.070  8.881   26.897  1.00 28.02  ? 92  TRP F CD2 1 
ATOM   9658  N NE1 . TRP E 2 92  ? -1.885  9.147   27.385  1.00 26.59  ? 92  TRP F NE1 1 
ATOM   9659  C CE2 . TRP E 2 92  ? -2.809  9.469   26.464  1.00 27.26  ? 92  TRP F CE2 1 
ATOM   9660  C CE3 . TRP E 2 92  ? -5.198  9.062   26.118  1.00 29.00  ? 92  TRP F CE3 1 
ATOM   9661  C CZ2 . TRP E 2 92  ? -2.709  10.208  25.304  1.00 28.90  ? 92  TRP F CZ2 1 
ATOM   9662  C CZ3 . TRP E 2 92  ? -5.086  9.803   24.944  1.00 27.08  ? 92  TRP F CZ3 1 
ATOM   9663  C CH2 . TRP E 2 92  ? -3.873  10.362  24.549  1.00 28.46  ? 92  TRP F CH2 1 
ATOM   9664  N N   . THR E 2 93  ? -6.990  6.931   31.216  1.00 29.23  ? 93  THR F N   1 
ATOM   9665  C CA  . THR E 2 93  ? -8.053  6.075   31.745  1.00 31.89  ? 93  THR F CA  1 
ATOM   9666  C C   . THR E 2 93  ? -9.391  6.811   31.763  1.00 32.20  ? 93  THR F C   1 
ATOM   9667  O O   . THR E 2 93  ? -10.380 6.316   31.232  1.00 34.51  ? 93  THR F O   1 
ATOM   9668  C CB  . THR E 2 93  ? -7.711  5.560   33.156  1.00 35.08  ? 93  THR F CB  1 
ATOM   9669  O OG1 . THR E 2 93  ? -6.588  4.669   33.078  1.00 35.25  ? 93  THR F OG1 1 
ATOM   9670  C CG2 . THR E 2 93  ? -8.900  4.836   33.785  1.00 35.15  ? 93  THR F CG2 1 
ATOM   9671  N N   . TYR E 2 94  ? -9.404  8.011   32.327  1.00 30.70  ? 94  TYR F N   1 
ATOM   9672  C CA  . TYR E 2 94  ? -10.630 8.804   32.394  1.00 32.92  ? 94  TYR F CA  1 
ATOM   9673  C C   . TYR E 2 94  ? -11.170 9.160   31.007  1.00 35.98  ? 94  TYR F C   1 
ATOM   9674  O O   . TYR E 2 94  ? -12.360 8.996   30.740  1.00 37.50  ? 94  TYR F O   1 
ATOM   9675  C CB  . TYR E 2 94  ? -10.391 10.082  33.185  1.00 32.34  ? 94  TYR F CB  1 
ATOM   9676  C CG  . TYR E 2 94  ? -11.658 10.765  33.628  1.00 35.24  ? 94  TYR F CG  1 
ATOM   9677  C CD1 . TYR E 2 94  ? -12.441 10.224  34.646  1.00 33.16  ? 94  TYR F CD1 1 
ATOM   9678  C CD2 . TYR E 2 94  ? -12.073 11.956  33.041  1.00 36.71  ? 94  TYR F CD2 1 
ATOM   9679  C CE1 . TYR E 2 94  ? -13.601 10.848  35.066  1.00 32.18  ? 94  TYR F CE1 1 
ATOM   9680  C CE2 . TYR E 2 94  ? -13.230 12.589  33.458  1.00 36.93  ? 94  TYR F CE2 1 
ATOM   9681  C CZ  . TYR E 2 94  ? -13.990 12.028  34.472  1.00 35.45  ? 94  TYR F CZ  1 
ATOM   9682  O OH  . TYR E 2 94  ? -15.142 12.656  34.885  1.00 36.99  ? 94  TYR F OH  1 
ATOM   9683  N N   . ASN E 2 95  ? -10.291 9.641   30.130  1.00 36.79  ? 95  ASN F N   1 
ATOM   9684  C CA  . ASN E 2 95  ? -10.693 10.046  28.787  1.00 40.39  ? 95  ASN F CA  1 
ATOM   9685  C C   . ASN E 2 95  ? -11.194 8.872   27.958  1.00 38.64  ? 95  ASN F C   1 
ATOM   9686  O O   . ASN E 2 95  ? -12.206 8.987   27.273  1.00 36.11  ? 95  ASN F O   1 
ATOM   9687  C CB  . ASN E 2 95  ? -9.543  10.752  28.060  1.00 46.55  ? 95  ASN F CB  1 
ATOM   9688  C CG  . ASN E 2 95  ? -9.225  12.120  28.646  1.00 52.48  ? 95  ASN F CG  1 
ATOM   9689  O OD1 . ASN E 2 95  ? -9.889  12.592  29.579  1.00 57.39  ? 95  ASN F OD1 1 
ATOM   9690  N ND2 . ASN E 2 95  ? -8.193  12.762  28.106  1.00 56.44  ? 95  ASN F ND2 1 
ATOM   9691  N N   . ALA E 2 96  ? -10.499 7.741   28.040  1.00 38.36  ? 96  ALA F N   1 
ATOM   9692  C CA  . ALA E 2 96  ? -10.913 6.536   27.330  1.00 38.16  ? 96  ALA F CA  1 
ATOM   9693  C C   . ALA E 2 96  ? -12.277 6.051   27.817  1.00 37.63  ? 96  ALA F C   1 
ATOM   9694  O O   . ALA E 2 96  ? -13.161 5.756   27.007  1.00 38.97  ? 96  ALA F O   1 
ATOM   9695  C CB  . ALA E 2 96  ? -9.875  5.437   27.492  1.00 40.79  ? 96  ALA F CB  1 
ATOM   9696  N N   . GLU E 2 97  ? -12.444 5.973   29.135  1.00 33.78  ? 97  GLU F N   1 
ATOM   9697  C CA  . GLU E 2 97  ? -13.706 5.519   29.720  1.00 36.69  ? 97  GLU F CA  1 
ATOM   9698  C C   . GLU E 2 97  ? -14.862 6.433   29.335  1.00 36.11  ? 97  GLU F C   1 
ATOM   9699  O O   . GLU E 2 97  ? -15.908 5.965   28.880  1.00 38.71  ? 97  GLU F O   1 
ATOM   9700  C CB  . GLU E 2 97  ? -13.605 5.428   31.241  1.00 39.74  ? 97  GLU F CB  1 
ATOM   9701  C CG  . GLU E 2 97  ? -12.685 4.322   31.743  1.00 44.07  ? 97  GLU F CG  1 
ATOM   9702  C CD  . GLU E 2 97  ? -13.295 2.934   31.674  1.00 51.55  ? 97  GLU F CD  1 
ATOM   9703  O OE1 . GLU E 2 97  ? -14.457 2.785   31.230  1.00 58.28  ? 97  GLU F OE1 1 
ATOM   9704  O OE2 . GLU E 2 97  ? -12.596 1.978   32.069  1.00 58.74  ? 97  GLU F OE2 1 
ATOM   9705  N N   . LEU E 2 98  ? -14.670 7.737   29.495  1.00 33.42  ? 98  LEU F N   1 
ATOM   9706  C CA  . LEU E 2 98  ? -15.737 8.684   29.196  1.00 34.18  ? 98  LEU F CA  1 
ATOM   9707  C C   . LEU E 2 98  ? -16.020 8.813   27.707  1.00 31.72  ? 98  LEU F C   1 
ATOM   9708  O O   . LEU E 2 98  ? -17.167 9.016   27.322  1.00 29.85  ? 98  LEU F O   1 
ATOM   9709  C CB  . LEU E 2 98  ? -15.449 10.052  29.804  1.00 36.68  ? 98  LEU F CB  1 
ATOM   9710  C CG  . LEU E 2 98  ? -15.670 10.119  31.318  1.00 37.05  ? 98  LEU F CG  1 
ATOM   9711  C CD1 . LEU E 2 98  ? -15.744 11.568  31.760  1.00 47.83  ? 98  LEU F CD1 1 
ATOM   9712  C CD2 . LEU E 2 98  ? -16.938 9.403   31.749  1.00 35.75  ? 98  LEU F CD2 1 
ATOM   9713  N N   . LEU E 2 99  ? -14.988 8.685   26.875  1.00 33.14  ? 99  LEU F N   1 
ATOM   9714  C CA  . LEU E 2 99  ? -15.174 8.666   25.425  1.00 33.38  ? 99  LEU F CA  1 
ATOM   9715  C C   . LEU E 2 99  ? -16.076 7.504   25.012  1.00 33.21  ? 99  LEU F C   1 
ATOM   9716  O O   . LEU E 2 99  ? -16.972 7.676   24.194  1.00 37.29  ? 99  LEU F O   1 
ATOM   9717  C CB  . LEU E 2 99  ? -13.831 8.547   24.709  1.00 38.89  ? 99  LEU F CB  1 
ATOM   9718  C CG  . LEU E 2 99  ? -13.861 8.438   23.179  1.00 45.02  ? 99  LEU F CG  1 
ATOM   9719  C CD1 . LEU E 2 99  ? -14.410 9.721   22.577  1.00 45.52  ? 99  LEU F CD1 1 
ATOM   9720  C CD2 . LEU E 2 99  ? -12.480 8.128   22.619  1.00 47.68  ? 99  LEU F CD2 1 
ATOM   9721  N N   . VAL E 2 100 ? -15.834 6.330   25.583  1.00 29.94  ? 100 VAL F N   1 
ATOM   9722  C CA  . VAL E 2 100 ? -16.630 5.148   25.279  1.00 31.65  ? 100 VAL F CA  1 
ATOM   9723  C C   . VAL E 2 100 ? -18.081 5.315   25.727  1.00 33.59  ? 100 VAL F C   1 
ATOM   9724  O O   . VAL E 2 100 ? -19.003 5.089   24.939  1.00 34.65  ? 100 VAL F O   1 
ATOM   9725  C CB  . VAL E 2 100 ? -16.019 3.884   25.926  1.00 34.94  ? 100 VAL F CB  1 
ATOM   9726  C CG1 . VAL E 2 100 ? -17.010 2.727   25.947  1.00 32.46  ? 100 VAL F CG1 1 
ATOM   9727  C CG2 . VAL E 2 100 ? -14.738 3.495   25.196  1.00 34.93  ? 100 VAL F CG2 1 
ATOM   9728  N N   . LEU E 2 101 ? -18.283 5.707   26.983  1.00 30.57  ? 101 LEU F N   1 
ATOM   9729  C CA  . LEU E 2 101 ? -19.631 5.930   27.504  1.00 29.00  ? 101 LEU F CA  1 
ATOM   9730  C C   . LEU E 2 101 ? -20.387 6.976   26.683  1.00 32.87  ? 101 LEU F C   1 
ATOM   9731  O O   . LEU E 2 101 ? -21.578 6.803   26.388  1.00 31.70  ? 101 LEU F O   1 
ATOM   9732  C CB  . LEU E 2 101 ? -19.591 6.371   28.968  1.00 28.95  ? 101 LEU F CB  1 
ATOM   9733  C CG  . LEU E 2 101 ? -19.112 5.368   30.016  1.00 26.79  ? 101 LEU F CG  1 
ATOM   9734  C CD1 . LEU E 2 101 ? -19.188 5.977   31.407  1.00 26.03  ? 101 LEU F CD1 1 
ATOM   9735  C CD2 . LEU E 2 101 ? -19.941 4.100   29.951  1.00 27.95  ? 101 LEU F CD2 1 
ATOM   9736  N N   . MET E 2 102 ? -19.691 8.047   26.303  1.00 32.80  ? 102 MET F N   1 
ATOM   9737  C CA  . MET E 2 102 ? -20.310 9.143   25.559  1.00 34.51  ? 102 MET F CA  1 
ATOM   9738  C C   . MET E 2 102 ? -20.691 8.723   24.147  1.00 33.48  ? 102 MET F C   1 
ATOM   9739  O O   . MET E 2 102 ? -21.821 8.942   23.713  1.00 34.55  ? 102 MET F O   1 
ATOM   9740  C CB  . MET E 2 102 ? -19.384 10.360  25.523  1.00 39.37  ? 102 MET F CB  1 
ATOM   9741  C CG  . MET E 2 102 ? -19.394 11.155  26.822  1.00 48.09  ? 102 MET F CG  1 
ATOM   9742  S SD  . MET E 2 102 ? -18.052 12.348  26.984  1.00 55.04  ? 102 MET F SD  1 
ATOM   9743  C CE  . MET E 2 102 ? -18.550 13.570  25.767  1.00 57.35  ? 102 MET F CE  1 
ATOM   9744  N N   . GLU E 2 103 ? -19.754 8.112   23.433  1.00 34.25  ? 103 GLU F N   1 
ATOM   9745  C CA  . GLU E 2 103 ? -20.011 7.717   22.054  1.00 36.69  ? 103 GLU F CA  1 
ATOM   9746  C C   . GLU E 2 103 ? -21.009 6.573   21.938  1.00 34.36  ? 103 GLU F C   1 
ATOM   9747  O O   . GLU E 2 103 ? -21.720 6.480   20.940  1.00 35.38  ? 103 GLU F O   1 
ATOM   9748  C CB  . GLU E 2 103 ? -18.707 7.405   21.313  1.00 40.48  ? 103 GLU F CB  1 
ATOM   9749  C CG  . GLU E 2 103 ? -17.951 8.657   20.879  1.00 48.38  ? 103 GLU F CG  1 
ATOM   9750  C CD  . GLU E 2 103 ? -18.789 9.606   20.024  1.00 57.35  ? 103 GLU F CD  1 
ATOM   9751  O OE1 . GLU E 2 103 ? -19.609 9.130   19.207  1.00 50.75  ? 103 GLU F OE1 1 
ATOM   9752  O OE2 . GLU E 2 103 ? -18.631 10.836  20.170  1.00 64.57  ? 103 GLU F OE2 1 
ATOM   9753  N N   . ASN E 2 104 ? -21.075 5.711   22.950  1.00 35.08  ? 104 ASN F N   1 
ATOM   9754  C CA  . ASN E 2 104 ? -22.109 4.673   22.999  1.00 33.56  ? 104 ASN F CA  1 
ATOM   9755  C C   . ASN E 2 104 ? -23.512 5.275   23.103  1.00 33.36  ? 104 ASN F C   1 
ATOM   9756  O O   . ASN E 2 104 ? -24.422 4.841   22.408  1.00 37.31  ? 104 ASN F O   1 
ATOM   9757  C CB  . ASN E 2 104 ? -21.869 3.692   24.152  1.00 34.19  ? 104 ASN F CB  1 
ATOM   9758  C CG  . ASN E 2 104 ? -20.773 2.679   23.854  1.00 36.99  ? 104 ASN F CG  1 
ATOM   9759  O OD1 . ASN E 2 104 ? -20.275 2.589   22.730  1.00 36.37  ? 104 ASN F OD1 1 
ATOM   9760  N ND2 . ASN E 2 104 ? -20.401 1.898   24.867  1.00 33.25  ? 104 ASN F ND2 1 
ATOM   9761  N N   . GLU E 2 105 ? -23.684 6.273   23.963  1.00 36.31  ? 105 GLU F N   1 
ATOM   9762  C CA  . GLU E 2 105 ? -24.956 6.986   24.057  1.00 38.84  ? 105 GLU F CA  1 
ATOM   9763  C C   . GLU E 2 105 ? -25.318 7.561   22.690  1.00 37.62  ? 105 GLU F C   1 
ATOM   9764  O O   . GLU E 2 105 ? -26.444 7.422   22.215  1.00 36.55  ? 105 GLU F O   1 
ATOM   9765  C CB  . GLU E 2 105 ? -24.868 8.121   25.080  1.00 45.14  ? 105 GLU F CB  1 
ATOM   9766  C CG  . GLU E 2 105 ? -26.206 8.761   25.437  1.00 50.78  ? 105 GLU F CG  1 
ATOM   9767  C CD  . GLU E 2 105 ? -26.128 10.280  25.516  1.00 72.16  ? 105 GLU F CD  1 
ATOM   9768  O OE1 . GLU E 2 105 ? -26.245 10.833  26.636  1.00 85.81  ? 105 GLU F OE1 1 
ATOM   9769  O OE2 . GLU E 2 105 ? -25.939 10.924  24.456  1.00 80.73  ? 105 GLU F OE2 1 
ATOM   9770  N N   . ARG E 2 106 ? -24.347 8.206   22.058  1.00 38.84  ? 106 ARG F N   1 
ATOM   9771  C CA  . ARG E 2 106 ? -24.554 8.786   20.738  1.00 41.96  ? 106 ARG F CA  1 
ATOM   9772  C C   . ARG E 2 106 ? -24.914 7.749   19.677  1.00 36.39  ? 106 ARG F C   1 
ATOM   9773  O O   . ARG E 2 106 ? -25.818 7.971   18.883  1.00 34.75  ? 106 ARG F O   1 
ATOM   9774  C CB  . ARG E 2 106 ? -23.342 9.597   20.312  1.00 49.02  ? 106 ARG F CB  1 
ATOM   9775  C CG  . ARG E 2 106 ? -23.355 10.980  20.928  1.00 60.88  ? 106 ARG F CG  1 
ATOM   9776  C CD  . ARG E 2 106 ? -23.134 12.024  19.862  1.00 80.82  ? 106 ARG F CD  1 
ATOM   9777  N NE  . ARG E 2 106 ? -22.262 13.095  20.351  1.00 92.22  ? 106 ARG F NE  1 
ATOM   9778  C CZ  . ARG E 2 106 ? -21.035 13.379  19.899  1.00 86.25  ? 106 ARG F CZ  1 
ATOM   9779  N NH1 . ARG E 2 106 ? -20.457 12.696  18.906  1.00 79.15  ? 106 ARG F NH1 1 
ATOM   9780  N NH2 . ARG E 2 106 ? -20.369 14.381  20.461  1.00 84.58  ? 106 ARG F NH2 1 
ATOM   9781  N N   . THR E 2 107 ? -24.218 6.617   19.678  1.00 33.77  ? 107 THR F N   1 
ATOM   9782  C CA  . THR E 2 107 ? -24.495 5.550   18.721  1.00 34.37  ? 107 THR F CA  1 
ATOM   9783  C C   . THR E 2 107 ? -25.927 5.013   18.862  1.00 34.96  ? 107 THR F C   1 
ATOM   9784  O O   . THR E 2 107 ? -26.592 4.751   17.860  1.00 38.68  ? 107 THR F O   1 
ATOM   9785  C CB  . THR E 2 107 ? -23.472 4.405   18.840  1.00 33.49  ? 107 THR F CB  1 
ATOM   9786  O OG1 . THR E 2 107 ? -22.165 4.890   18.501  1.00 34.44  ? 107 THR F OG1 1 
ATOM   9787  C CG2 . THR E 2 107 ? -23.826 3.256   17.897  1.00 29.29  ? 107 THR F CG2 1 
ATOM   9788  N N   . LEU E 2 108 ? -26.407 4.848   20.090  1.00 33.22  ? 108 LEU F N   1 
ATOM   9789  C CA  . LEU E 2 108 ? -27.761 4.327   20.291  1.00 33.53  ? 108 LEU F CA  1 
ATOM   9790  C C   . LEU E 2 108 ? -28.818 5.350   19.873  1.00 33.52  ? 108 LEU F C   1 
ATOM   9791  O O   . LEU E 2 108 ? -29.824 4.995   19.265  1.00 38.96  ? 108 LEU F O   1 
ATOM   9792  C CB  . LEU E 2 108 ? -27.967 3.851   21.731  1.00 31.80  ? 108 LEU F CB  1 
ATOM   9793  C CG  . LEU E 2 108 ? -27.055 2.694   22.157  1.00 34.07  ? 108 LEU F CG  1 
ATOM   9794  C CD1 . LEU E 2 108 ? -27.513 2.141   23.496  1.00 39.70  ? 108 LEU F CD1 1 
ATOM   9795  C CD2 . LEU E 2 108 ? -27.008 1.594   21.107  1.00 29.42  ? 108 LEU F CD2 1 
ATOM   9796  N N   . ASP E 2 109 ? -28.569 6.622   20.155  1.00 36.31  ? 109 ASP F N   1 
ATOM   9797  C CA  . ASP E 2 109 ? -29.455 7.692   19.695  1.00 37.06  ? 109 ASP F CA  1 
ATOM   9798  C C   . ASP E 2 109 ? -29.428 7.854   18.164  1.00 37.27  ? 109 ASP F C   1 
ATOM   9799  O O   . ASP E 2 109 ? -30.433 8.216   17.552  1.00 38.01  ? 109 ASP F O   1 
ATOM   9800  C CB  . ASP E 2 109 ? -29.111 9.012   20.391  1.00 42.02  ? 109 ASP F CB  1 
ATOM   9801  C CG  . ASP E 2 109 ? -29.728 9.121   21.789  1.00 57.08  ? 109 ASP F CG  1 
ATOM   9802  O OD1 . ASP E 2 109 ? -29.111 9.753   22.673  1.00 61.25  ? 109 ASP F OD1 1 
ATOM   9803  O OD2 . ASP E 2 109 ? -30.839 8.582   22.010  1.00 72.10  ? 109 ASP F OD2 1 
ATOM   9804  N N   . PHE E 2 110 ? -28.272 7.600   17.561  1.00 34.68  ? 110 PHE F N   1 
ATOM   9805  C CA  . PHE E 2 110 ? -28.129 7.591   16.113  1.00 36.83  ? 110 PHE F CA  1 
ATOM   9806  C C   . PHE E 2 110 ? -29.110 6.593   15.487  1.00 42.43  ? 110 PHE F C   1 
ATOM   9807  O O   . PHE E 2 110 ? -29.859 6.950   14.572  1.00 39.43  ? 110 PHE F O   1 
ATOM   9808  C CB  . PHE E 2 110 ? -26.692 7.242   15.746  1.00 37.10  ? 110 PHE F CB  1 
ATOM   9809  C CG  . PHE E 2 110 ? -26.416 7.245   14.274  1.00 33.96  ? 110 PHE F CG  1 
ATOM   9810  C CD1 . PHE E 2 110 ? -26.659 8.372   13.505  1.00 35.77  ? 110 PHE F CD1 1 
ATOM   9811  C CD2 . PHE E 2 110 ? -25.878 6.127   13.664  1.00 37.45  ? 110 PHE F CD2 1 
ATOM   9812  C CE1 . PHE E 2 110 ? -26.392 8.376   12.147  1.00 37.93  ? 110 PHE F CE1 1 
ATOM   9813  C CE2 . PHE E 2 110 ? -25.607 6.123   12.305  1.00 37.94  ? 110 PHE F CE2 1 
ATOM   9814  C CZ  . PHE E 2 110 ? -25.862 7.248   11.547  1.00 37.56  ? 110 PHE F CZ  1 
ATOM   9815  N N   . HIS E 2 111 ? -29.125 5.362   16.003  1.00 38.85  ? 111 HIS F N   1 
ATOM   9816  C CA  . HIS E 2 111 ? -30.055 4.331   15.522  1.00 40.43  ? 111 HIS F CA  1 
ATOM   9817  C C   . HIS E 2 111 ? -31.487 4.738   15.715  1.00 42.08  ? 111 HIS F C   1 
ATOM   9818  O O   . HIS E 2 111 ? -32.303 4.587   14.817  1.00 46.37  ? 111 HIS F O   1 
ATOM   9819  C CB  . HIS E 2 111 ? -29.807 2.989   16.207  1.00 36.73  ? 111 HIS F CB  1 
ATOM   9820  C CG  . HIS E 2 111 ? -28.460 2.387   15.891  1.00 38.63  ? 111 HIS F CG  1 
ATOM   9821  N ND1 . HIS E 2 111 ? -27.974 2.305   14.635  1.00 38.47  ? 111 HIS F ND1 1 
ATOM   9822  C CD2 . HIS E 2 111 ? -27.495 1.828   16.721  1.00 41.29  ? 111 HIS F CD2 1 
ATOM   9823  C CE1 . HIS E 2 111 ? -26.756 1.729   14.668  1.00 40.65  ? 111 HIS F CE1 1 
ATOM   9824  N NE2 . HIS E 2 111 ? -26.467 1.435   15.941  1.00 40.71  ? 111 HIS F NE2 1 
ATOM   9825  N N   . ASP E 2 112 ? -31.809 5.252   16.895  1.00 42.59  ? 112 ASP F N   1 
ATOM   9826  C CA  . ASP E 2 112 ? -33.148 5.781   17.148  1.00 47.53  ? 112 ASP F CA  1 
ATOM   9827  C C   . ASP E 2 112 ? -33.524 6.825   16.096  1.00 42.98  ? 112 ASP F C   1 
ATOM   9828  O O   . ASP E 2 112 ? -34.608 6.788   15.516  1.00 46.38  ? 112 ASP F O   1 
ATOM   9829  C CB  . ASP E 2 112 ? -33.232 6.394   18.552  1.00 52.52  ? 112 ASP F CB  1 
ATOM   9830  C CG  . ASP E 2 112 ? -33.338 5.341   19.655  1.00 55.49  ? 112 ASP F CG  1 
ATOM   9831  O OD1 . ASP E 2 112 ? -33.413 4.131   19.351  1.00 52.26  ? 112 ASP F OD1 1 
ATOM   9832  O OD2 . ASP E 2 112 ? -33.351 5.729   20.841  1.00 60.77  ? 112 ASP F OD2 1 
ATOM   9833  N N   . SER E 2 113 ? -32.613 7.751   15.846  1.00 42.13  ? 113 SER F N   1 
ATOM   9834  C CA  . SER E 2 113 ? -32.851 8.819   14.879  1.00 44.04  ? 113 SER F CA  1 
ATOM   9835  C C   . SER E 2 113 ? -33.073 8.289   13.451  1.00 40.72  ? 113 SER F C   1 
ATOM   9836  O O   . SER E 2 113 ? -33.910 8.806   12.708  1.00 41.34  ? 113 SER F O   1 
ATOM   9837  C CB  . SER E 2 113 ? -31.686 9.806   14.896  1.00 42.40  ? 113 SER F CB  1 
ATOM   9838  O OG  . SER E 2 113 ? -32.058 11.034  14.300  1.00 47.20  ? 113 SER F OG  1 
ATOM   9839  N N   . ASN E 2 114 ? -32.325 7.257   13.076  1.00 37.02  ? 114 ASN F N   1 
ATOM   9840  C CA  . ASN E 2 114 ? -32.453 6.662   11.749  1.00 38.61  ? 114 ASN F CA  1 
ATOM   9841  C C   . ASN E 2 114 ? -33.782 5.954   11.537  1.00 36.64  ? 114 ASN F C   1 
ATOM   9842  O O   . ASN E 2 114 ? -34.351 6.010   10.451  1.00 38.08  ? 114 ASN F O   1 
ATOM   9843  C CB  . ASN E 2 114 ? -31.300 5.697   11.474  1.00 40.37  ? 114 ASN F CB  1 
ATOM   9844  C CG  . ASN E 2 114 ? -29.984 6.420   11.265  1.00 40.54  ? 114 ASN F CG  1 
ATOM   9845  O OD1 . ASN E 2 114 ? -29.964 7.567   10.824  1.00 38.19  ? 114 ASN F OD1 1 
ATOM   9846  N ND2 . ASN E 2 114 ? -28.878 5.758   11.589  1.00 42.76  ? 114 ASN F ND2 1 
ATOM   9847  N N   . VAL E 2 115 ? -34.261 5.276   12.571  1.00 40.17  ? 115 VAL F N   1 
ATOM   9848  C CA  . VAL E 2 115 ? -35.551 4.603   12.509  1.00 49.04  ? 115 VAL F CA  1 
ATOM   9849  C C   . VAL E 2 115 ? -36.666 5.627   12.322  1.00 48.83  ? 115 VAL F C   1 
ATOM   9850  O O   . VAL E 2 115 ? -37.549 5.426   11.498  1.00 48.87  ? 115 VAL F O   1 
ATOM   9851  C CB  . VAL E 2 115 ? -35.822 3.751   13.767  1.00 52.13  ? 115 VAL F CB  1 
ATOM   9852  C CG1 . VAL E 2 115 ? -37.304 3.412   13.886  1.00 55.45  ? 115 VAL F CG1 1 
ATOM   9853  C CG2 . VAL E 2 115 ? -34.975 2.488   13.727  1.00 45.11  ? 115 VAL F CG2 1 
ATOM   9854  N N   . ARG E 2 116 ? -36.606 6.713   13.093  1.00 52.73  ? 116 ARG F N   1 
ATOM   9855  C CA  . ARG E 2 116 ? -37.574 7.814   12.999  1.00 51.40  ? 116 ARG F CA  1 
ATOM   9856  C C   . ARG E 2 116 ? -37.605 8.437   11.592  1.00 48.64  ? 116 ARG F C   1 
ATOM   9857  O O   . ARG E 2 116 ? -38.672 8.701   11.054  1.00 45.81  ? 116 ARG F O   1 
ATOM   9858  C CB  . ARG E 2 116 ? -37.336 8.847   14.119  1.00 59.12  ? 116 ARG F CB  1 
ATOM   9859  C CG  . ARG E 2 116 ? -37.935 8.392   15.441  1.00 69.98  ? 116 ARG F CG  1 
ATOM   9860  C CD  . ARG E 2 116 ? -37.829 9.446   16.530  1.00 81.18  ? 116 ARG F CD  1 
ATOM   9861  N NE  . ARG E 2 116 ? -38.258 8.905   17.827  1.00 88.21  ? 116 ARG F NE  1 
ATOM   9862  C CZ  . ARG E 2 116 ? -37.449 8.476   18.805  1.00 93.39  ? 116 ARG F CZ  1 
ATOM   9863  N NH1 . ARG E 2 116 ? -36.120 8.487   18.687  1.00 86.25  ? 116 ARG F NH1 1 
ATOM   9864  N NH2 . ARG E 2 116 ? -37.990 8.014   19.932  1.00 86.58  ? 116 ARG F NH2 1 
ATOM   9865  N N   . ASN E 2 117 ? -36.446 8.612   10.969  1.00 53.34  ? 117 ASN F N   1 
ATOM   9866  C CA  . ASN E 2 117 ? -36.388 9.095   9.581   1.00 55.55  ? 117 ASN F CA  1 
ATOM   9867  C C   . ASN E 2 117 ? -37.048 8.120   8.599   1.00 54.54  ? 117 ASN F C   1 
ATOM   9868  O O   . ASN E 2 117 ? -37.736 8.531   7.669   1.00 49.21  ? 117 ASN F O   1 
ATOM   9869  C CB  . ASN E 2 117 ? -34.938 9.335   9.154   1.00 61.13  ? 117 ASN F CB  1 
ATOM   9870  C CG  . ASN E 2 117 ? -34.268 10.471  9.920   1.00 68.16  ? 117 ASN F CG  1 
ATOM   9871  O OD1 . ASN E 2 117 ? -33.039 10.522  10.021  1.00 63.01  ? 117 ASN F OD1 1 
ATOM   9872  N ND2 . ASN E 2 117 ? -35.069 11.379  10.475  1.00 64.32  ? 117 ASN F ND2 1 
ATOM   9873  N N   . LEU E 2 118 ? -36.833 6.827   8.818   1.00 56.50  ? 118 LEU F N   1 
ATOM   9874  C CA  . LEU E 2 118 ? -37.444 5.778   8.000   1.00 52.18  ? 118 LEU F CA  1 
ATOM   9875  C C   . LEU E 2 118 ? -38.966 5.792   8.182   1.00 53.34  ? 118 LEU F C   1 
ATOM   9876  O O   . LEU E 2 118 ? -39.717 5.613   7.227   1.00 62.80  ? 118 LEU F O   1 
ATOM   9877  C CB  . LEU E 2 118 ? -36.874 4.404   8.376   1.00 47.34  ? 118 LEU F CB  1 
ATOM   9878  C CG  . LEU E 2 118 ? -36.728 3.375   7.242   1.00 49.72  ? 118 LEU F CG  1 
ATOM   9879  C CD1 . LEU E 2 118 ? -35.720 3.825   6.193   1.00 51.55  ? 118 LEU F CD1 1 
ATOM   9880  C CD2 . LEU E 2 118 ? -36.353 2.012   7.801   1.00 43.59  ? 118 LEU F CD2 1 
ATOM   9881  N N   . TYR E 2 119 ? -39.411 6.022   9.413   1.00 45.94  ? 119 TYR F N   1 
ATOM   9882  C CA  . TYR E 2 119 ? -40.831 6.104   9.727   1.00 49.08  ? 119 TYR F CA  1 
ATOM   9883  C C   . TYR E 2 119 ? -41.493 7.305   9.067   1.00 55.06  ? 119 TYR F C   1 
ATOM   9884  O O   . TYR E 2 119 ? -42.633 7.212   8.618   1.00 59.63  ? 119 TYR F O   1 
ATOM   9885  C CB  . TYR E 2 119 ? -41.026 6.193   11.237  1.00 47.95  ? 119 TYR F CB  1 
ATOM   9886  C CG  . TYR E 2 119 ? -42.454 6.301   11.678  1.00 50.63  ? 119 TYR F CG  1 
ATOM   9887  C CD1 . TYR E 2 119 ? -43.223 5.169   11.850  1.00 52.58  ? 119 TYR F CD1 1 
ATOM   9888  C CD2 . TYR E 2 119 ? -43.032 7.539   11.956  1.00 53.50  ? 119 TYR F CD2 1 
ATOM   9889  C CE1 . TYR E 2 119 ? -44.528 5.265   12.273  1.00 55.36  ? 119 TYR F CE1 1 
ATOM   9890  C CE2 . TYR E 2 119 ? -44.338 7.645   12.380  1.00 54.23  ? 119 TYR F CE2 1 
ATOM   9891  C CZ  . TYR E 2 119 ? -45.083 6.503   12.537  1.00 51.76  ? 119 TYR F CZ  1 
ATOM   9892  O OH  . TYR E 2 119 ? -46.382 6.602   12.948  1.00 54.46  ? 119 TYR F OH  1 
ATOM   9893  N N   . ASP E 2 120 ? -40.789 8.436   9.036   1.00 63.99  ? 120 ASP F N   1 
ATOM   9894  C CA  . ASP E 2 120 ? -41.333 9.659   8.445   1.00 64.31  ? 120 ASP F CA  1 
ATOM   9895  C C   . ASP E 2 120 ? -41.400 9.561   6.919   1.00 64.81  ? 120 ASP F C   1 
ATOM   9896  O O   . ASP E 2 120 ? -42.353 10.045  6.316   1.00 70.15  ? 120 ASP F O   1 
ATOM   9897  C CB  . ASP E 2 120 ? -40.538 10.896  8.897   1.00 69.76  ? 120 ASP F CB  1 
ATOM   9898  C CG  . ASP E 2 120 ? -40.859 11.308  10.338  1.00 82.73  ? 120 ASP F CG  1 
ATOM   9899  O OD1 . ASP E 2 120 ? -42.057 11.367  10.695  1.00 87.42  ? 120 ASP F OD1 1 
ATOM   9900  O OD2 . ASP E 2 120 ? -39.915 11.580  11.117  1.00 78.53  ? 120 ASP F OD2 1 
ATOM   9901  N N   . LYS E 2 121 ? -40.403 8.929   6.303   1.00 61.87  ? 121 LYS F N   1 
ATOM   9902  C CA  . LYS E 2 121 ? -40.431 8.671   4.860   1.00 64.42  ? 121 LYS F CA  1 
ATOM   9903  C C   . LYS E 2 121 ? -41.679 7.886   4.455   1.00 64.13  ? 121 LYS F C   1 
ATOM   9904  O O   . LYS E 2 121 ? -42.227 8.101   3.382   1.00 66.77  ? 121 LYS F O   1 
ATOM   9905  C CB  . LYS E 2 121 ? -39.202 7.889   4.383   1.00 72.29  ? 121 LYS F CB  1 
ATOM   9906  C CG  . LYS E 2 121 ? -38.613 8.431   3.093   1.00 80.98  ? 121 LYS F CG  1 
ATOM   9907  C CD  . LYS E 2 121 ? -37.587 7.482   2.499   1.00 91.54  ? 121 LYS F CD  1 
ATOM   9908  C CE  . LYS E 2 121 ? -37.197 7.921   1.097   1.00 94.74  ? 121 LYS F CE  1 
ATOM   9909  N NZ  . LYS E 2 121 ? -36.195 7.014   0.474   1.00 89.57  ? 121 LYS F NZ  1 
ATOM   9910  N N   . VAL E 2 122 ? -42.095 6.952   5.303   1.00 60.17  ? 122 VAL F N   1 
ATOM   9911  C CA  . VAL E 2 122 ? -43.315 6.184   5.077   1.00 59.25  ? 122 VAL F CA  1 
ATOM   9912  C C   . VAL E 2 122 ? -44.547 7.057   5.322   1.00 61.18  ? 122 VAL F C   1 
ATOM   9913  O O   . VAL E 2 122 ? -45.431 7.129   4.478   1.00 74.83  ? 122 VAL F O   1 
ATOM   9914  C CB  . VAL E 2 122 ? -43.357 4.922   5.974   1.00 51.09  ? 122 VAL F CB  1 
ATOM   9915  C CG1 . VAL E 2 122 ? -44.747 4.309   6.005   1.00 50.83  ? 122 VAL F CG1 1 
ATOM   9916  C CG2 . VAL E 2 122 ? -42.336 3.903   5.494   1.00 48.65  ? 122 VAL F CG2 1 
ATOM   9917  N N   . ARG E 2 123 ? -44.588 7.723   6.470   1.00 64.00  ? 123 ARG F N   1 
ATOM   9918  C CA  . ARG E 2 123 ? -45.725 8.567   6.828   1.00 65.79  ? 123 ARG F CA  1 
ATOM   9919  C C   . ARG E 2 123 ? -46.072 9.588   5.744   1.00 75.15  ? 123 ARG F C   1 
ATOM   9920  O O   . ARG E 2 123 ? -47.236 9.739   5.373   1.00 78.26  ? 123 ARG F O   1 
ATOM   9921  C CB  . ARG E 2 123 ? -45.461 9.283   8.155   1.00 20.00  ? 123 ARG F CB  1 
ATOM   9922  C CG  . ARG E 2 123 ? -46.488 10.349  8.500   1.00 20.00  ? 123 ARG F CG  1 
ATOM   9923  C CD  . ARG E 2 123 ? -45.845 11.522  9.222   1.00 20.00  ? 123 ARG F CD  1 
ATOM   9924  N NE  . ARG E 2 123 ? -46.229 12.802  8.636   1.00 20.00  ? 123 ARG F NE  1 
ATOM   9925  C CZ  . ARG E 2 123 ? -45.370 13.674  8.117   1.00 20.00  ? 123 ARG F CZ  1 
ATOM   9926  N NH1 . ARG E 2 123 ? -44.072 13.404  8.110   1.00 20.00  ? 123 ARG F NH1 1 
ATOM   9927  N NH2 . ARG E 2 123 ? -45.809 14.815  7.605   1.00 20.00  ? 123 ARG F NH2 1 
ATOM   9928  N N   . LEU E 2 124 ? -45.059 10.289  5.244   1.00 83.45  ? 124 LEU F N   1 
ATOM   9929  C CA  . LEU E 2 124 ? -45.265 11.354  4.249   1.00 92.79  ? 124 LEU F CA  1 
ATOM   9930  C C   . LEU E 2 124 ? -45.687 10.810  2.879   1.00 97.56  ? 124 LEU F C   1 
ATOM   9931  O O   . LEU E 2 124 ? -46.201 11.558  2.045   1.00 107.85 ? 124 LEU F O   1 
ATOM   9932  C CB  . LEU E 2 124 ? -44.005 12.226  4.089   1.00 95.56  ? 124 LEU F CB  1 
ATOM   9933  C CG  . LEU E 2 124 ? -43.788 13.401  5.045   1.00 104.04 ? 124 LEU F CG  1 
ATOM   9934  C CD1 . LEU E 2 124 ? -43.715 12.950  6.495   1.00 104.60 ? 124 LEU F CD1 1 
ATOM   9935  C CD2 . LEU E 2 124 ? -42.522 14.153  4.660   1.00 103.61 ? 124 LEU F CD2 1 
ATOM   9936  N N   . GLN E 2 125 ? -45.472 9.516   2.655   1.00 86.01  ? 125 GLN F N   1 
ATOM   9937  C CA  . GLN E 2 125 ? -45.814 8.870   1.399   1.00 78.87  ? 125 GLN F CA  1 
ATOM   9938  C C   . GLN E 2 125 ? -47.263 8.396   1.360   1.00 82.78  ? 125 GLN F C   1 
ATOM   9939  O O   . GLN E 2 125 ? -47.770 8.205   0.266   1.00 85.14  ? 125 GLN F O   1 
ATOM   9940  C CB  . GLN E 2 125 ? -44.872 7.688   1.124   1.00 76.10  ? 125 GLN F CB  1 
ATOM   9941  C CG  . GLN E 2 125 ? -44.744 7.338   -0.357  1.00 83.78  ? 125 GLN F CG  1 
ATOM   9942  C CD  . GLN E 2 125 ? -43.380 6.823   -0.747  1.00 83.72  ? 125 GLN F CD  1 
ATOM   9943  O OE1 . GLN E 2 125 ? -43.066 5.658   -0.530  1.00 70.67  ? 125 GLN F OE1 1 
ATOM   9944  N NE2 . GLN E 2 125 ? -42.577 7.684   -1.367  1.00 81.09  ? 125 GLN F NE2 1 
ATOM   9945  N N   . LEU E 2 126 ? -47.903 8.192   2.525   1.00 77.98  ? 126 LEU F N   1 
ATOM   9946  C CA  . LEU E 2 126 ? -49.304 7.750   2.632   1.00 77.28  ? 126 LEU F CA  1 
ATOM   9947  C C   . LEU E 2 126 ? -50.071 8.527   3.716   1.00 78.26  ? 126 LEU F C   1 
ATOM   9948  O O   . LEU E 2 126 ? -50.293 8.016   4.816   1.00 91.40  ? 126 LEU F O   1 
ATOM   9949  C CB  . LEU E 2 126 ? -49.353 6.233   2.939   1.00 85.41  ? 126 LEU F CB  1 
ATOM   9950  C CG  . LEU E 2 126 ? -48.118 5.611   3.601   1.00 76.61  ? 126 LEU F CG  1 
ATOM   9951  C CD1 . LEU E 2 126 ? -48.099 5.933   5.085   1.00 75.91  ? 126 LEU F CD1 1 
ATOM   9952  C CD2 . LEU E 2 126 ? -48.107 4.105   3.398   1.00 74.84  ? 126 LEU F CD2 1 
ATOM   9953  N N   . LYS E 2 127 ? -50.497 9.743   3.375   1.00 79.89  ? 127 LYS F N   1 
ATOM   9954  C CA  . LYS E 2 127 ? -51.086 10.714  4.333   1.00 82.48  ? 127 LYS F CA  1 
ATOM   9955  C C   . LYS E 2 127 ? -52.371 10.216  5.042   1.00 81.33  ? 127 LYS F C   1 
ATOM   9956  O O   . LYS E 2 127 ? -52.339 9.663   6.151   1.00 69.18  ? 127 LYS F O   1 
ATOM   9957  C CB  . LYS E 2 127 ? -51.387 12.028  3.611   1.00 20.00  ? 127 LYS F CB  1 
ATOM   9958  C CG  . LYS E 2 127 ? -50.151 12.761  3.112   1.00 20.00  ? 127 LYS F CG  1 
ATOM   9959  C CD  . LYS E 2 127 ? -50.523 14.042  2.386   1.00 20.00  ? 127 LYS F CD  1 
ATOM   9960  C CE  . LYS E 2 127 ? -49.288 14.786  1.908   1.00 20.00  ? 127 LYS F CE  1 
ATOM   9961  N NZ  . LYS E 2 127 ? -49.639 16.032  1.173   1.00 20.00  ? 127 LYS F NZ  1 
ATOM   9962  N N   . ASP E 2 128 ? -53.503 10.437  4.385   1.00 90.82  ? 128 ASP F N   1 
ATOM   9963  C CA  . ASP E 2 128 ? -54.824 10.072  4.874   1.00 95.32  ? 128 ASP F CA  1 
ATOM   9964  C C   . ASP E 2 128 ? -55.136 8.617   4.505   1.00 92.54  ? 128 ASP F C   1 
ATOM   9965  O O   . ASP E 2 128 ? -56.199 8.091   4.842   1.00 94.80  ? 128 ASP F O   1 
ATOM   9966  C CB  . ASP E 2 128 ? -55.832 11.025  4.199   1.00 105.85 ? 128 ASP F CB  1 
ATOM   9967  C CG  . ASP E 2 128 ? -57.176 11.148  4.915   1.00 110.49 ? 128 ASP F CG  1 
ATOM   9968  O OD1 . ASP E 2 128 ? -57.280 10.987  6.145   1.00 112.03 ? 128 ASP F OD1 1 
ATOM   9969  O OD2 . ASP E 2 128 ? -58.159 11.475  4.216   1.00 99.79  ? 128 ASP F OD2 1 
ATOM   9970  N N   . ASN E 2 129 ? -54.214 7.970   3.796   1.00 89.77  ? 129 ASN F N   1 
ATOM   9971  C CA  . ASN E 2 129 ? -54.401 6.575   3.404   1.00 84.19  ? 129 ASN F CA  1 
ATOM   9972  C C   . ASN E 2 129 ? -54.055 5.570   4.510   1.00 77.78  ? 129 ASN F C   1 
ATOM   9973  O O   . ASN E 2 129 ? -54.379 4.385   4.381   1.00 79.90  ? 129 ASN F O   1 
ATOM   9974  C CB  . ASN E 2 129 ? -53.588 6.263   2.143   1.00 84.14  ? 129 ASN F CB  1 
ATOM   9975  C CG  . ASN E 2 129 ? -54.189 6.875   0.887   1.00 83.92  ? 129 ASN F CG  1 
ATOM   9976  O OD1 . ASN E 2 129 ? -55.162 7.633   0.947   1.00 75.63  ? 129 ASN F OD1 1 
ATOM   9977  N ND2 . ASN E 2 129 ? -53.609 6.546   -0.265  1.00 83.43  ? 129 ASN F ND2 1 
ATOM   9978  N N   . ALA E 2 130 ? -53.406 6.035   5.582   1.00 73.17  ? 130 ALA F N   1 
ATOM   9979  C CA  . ALA E 2 130 ? -52.992 5.168   6.692   1.00 68.36  ? 130 ALA F CA  1 
ATOM   9980  C C   . ALA E 2 130 ? -53.398 5.757   8.040   1.00 64.78  ? 130 ALA F C   1 
ATOM   9981  O O   . ALA E 2 130 ? -53.526 6.974   8.173   1.00 66.12  ? 130 ALA F O   1 
ATOM   9982  C CB  . ALA E 2 130 ? -51.486 4.950   6.649   1.00 69.33  ? 130 ALA F CB  1 
ATOM   9983  N N   . LYS E 2 131 ? -53.609 4.870   9.015   1.00 62.09  ? 131 LYS F N   1 
ATOM   9984  C CA  . LYS E 2 131 ? -53.905 5.216   10.395  1.00 62.69  ? 131 LYS F CA  1 
ATOM   9985  C C   . LYS E 2 131 ? -52.652 4.946   11.233  1.00 73.58  ? 131 LYS F C   1 
ATOM   9986  O O   . LYS E 2 131 ? -52.309 3.796   11.549  1.00 83.31  ? 131 LYS F O   1 
ATOM   9987  C CB  . LYS E 2 131 ? -55.075 4.367   10.888  1.00 60.95  ? 131 LYS F CB  1 
ATOM   9988  C CG  . LYS E 2 131 ? -55.412 4.516   12.356  1.00 65.33  ? 131 LYS F CG  1 
ATOM   9989  C CD  . LYS E 2 131 ? -56.617 3.675   12.752  1.00 70.06  ? 131 LYS F CD  1 
ATOM   9990  C CE  . LYS E 2 131 ? -56.359 2.865   14.018  1.00 75.35  ? 131 LYS F CE  1 
ATOM   9991  N NZ  . LYS E 2 131 ? -57.614 2.377   14.653  1.00 84.85  ? 131 LYS F NZ  1 
ATOM   9992  N N   . GLU E 2 132 ? -51.948 6.012   11.581  1.00 71.23  ? 132 GLU F N   1 
ATOM   9993  C CA  . GLU E 2 132 ? -50.784 5.878   12.456  1.00 71.04  ? 132 GLU F CA  1 
ATOM   9994  C C   . GLU E 2 132 ? -51.186 5.279   13.803  1.00 64.44  ? 132 GLU F C   1 
ATOM   9995  O O   . GLU E 2 132 ? -52.004 5.863   14.513  1.00 71.07  ? 132 GLU F O   1 
ATOM   9996  C CB  . GLU E 2 132 ? -50.115 7.233   12.673  1.00 66.04  ? 132 GLU F CB  1 
ATOM   9997  C CG  . GLU E 2 132 ? -49.191 7.650   11.541  1.00 64.86  ? 132 GLU F CG  1 
ATOM   9998  C CD  . GLU E 2 132 ? -48.686 9.068   11.702  1.00 67.19  ? 132 GLU F CD  1 
ATOM   9999  O OE1 . GLU E 2 132 ? -47.512 9.238   12.095  1.00 62.28  ? 132 GLU F OE1 1 
ATOM   10000 O OE2 . GLU E 2 132 ? -49.467 10.010  11.449  1.00 66.77  ? 132 GLU F OE2 1 
ATOM   10001 N N   . LEU E 2 133 ? -50.648 4.093   14.103  1.00 67.70  ? 133 LEU F N   1 
ATOM   10002 C CA  . LEU E 2 133 ? -50.656 3.520   15.440  1.00 70.63  ? 133 LEU F CA  1 
ATOM   10003 C C   . LEU E 2 133 ? -49.376 4.020   16.154  1.00 75.54  ? 133 LEU F C   1 
ATOM   10004 O O   . LEU E 2 133 ? -48.501 4.663   15.539  1.00 88.12  ? 133 LEU F O   1 
ATOM   10005 C CB  . LEU E 2 133 ? -50.726 1.977   15.373  1.00 76.80  ? 133 LEU F CB  1 
ATOM   10006 C CG  . LEU E 2 133 ? -52.008 1.348   14.812  1.00 82.75  ? 133 LEU F CG  1 
ATOM   10007 C CD1 . LEU E 2 133 ? -51.863 -0.162  14.736  1.00 78.03  ? 133 LEU F CD1 1 
ATOM   10008 C CD2 . LEU E 2 133 ? -53.193 1.721   15.692  1.00 91.84  ? 133 LEU F CD2 1 
ATOM   10009 N N   . GLY E 2 134 ? -49.245 3.726   17.442  1.00 74.74  ? 134 GLY F N   1 
ATOM   10010 C CA  . GLY E 2 134 ? -48.159 4.304   18.231  1.00 84.41  ? 134 GLY F CA  1 
ATOM   10011 C C   . GLY E 2 134 ? -46.860 3.516   18.263  1.00 87.50  ? 134 GLY F C   1 
ATOM   10012 O O   . GLY E 2 134 ? -45.873 3.970   18.852  1.00 96.53  ? 134 GLY F O   1 
ATOM   10013 N N   . ASN E 2 135 ? -46.846 2.341   17.639  1.00 74.59  ? 135 ASN F N   1 
ATOM   10014 C CA  . ASN E 2 135 ? -45.732 1.414   17.794  1.00 71.32  ? 135 ASN F CA  1 
ATOM   10015 C C   . ASN E 2 135 ? -44.803 1.392   16.589  1.00 60.27  ? 135 ASN F C   1 
ATOM   10016 O O   . ASN E 2 135 ? -44.101 0.412   16.384  1.00 54.27  ? 135 ASN F O   1 
ATOM   10017 C CB  . ASN E 2 135 ? -46.274 -0.010  18.025  1.00 73.75  ? 135 ASN F CB  1 
ATOM   10018 C CG  . ASN E 2 135 ? -47.676 -0.023  18.581  1.00 82.42  ? 135 ASN F CG  1 
ATOM   10019 O OD1 . ASN E 2 135 ? -48.619 0.358   17.895  1.00 91.02  ? 135 ASN F OD1 1 
ATOM   10020 N ND2 . ASN E 2 135 ? -47.825 -0.471  19.822  1.00 98.39  ? 135 ASN F ND2 1 
ATOM   10021 N N   . GLY E 2 136 ? -44.791 2.459   15.795  1.00 57.95  ? 136 GLY F N   1 
ATOM   10022 C CA  . GLY E 2 136 ? -44.064 2.454   14.532  1.00 55.67  ? 136 GLY F CA  1 
ATOM   10023 C C   . GLY E 2 136 ? -44.838 1.797   13.410  1.00 53.23  ? 136 GLY F C   1 
ATOM   10024 O O   . GLY E 2 136 ? -44.289 1.604   12.334  1.00 53.28  ? 136 GLY F O   1 
ATOM   10025 N N   . CYS E 2 137 ? -46.110 1.467   13.645  1.00 56.07  ? 137 CYS F N   1 
ATOM   10026 C CA  . CYS E 2 137 ? -46.912 0.740   12.663  1.00 60.46  ? 137 CYS F CA  1 
ATOM   10027 C C   . CYS E 2 137 ? -48.019 1.596   12.052  1.00 54.38  ? 137 CYS F C   1 
ATOM   10028 O O   . CYS E 2 137 ? -48.596 2.461   12.709  1.00 60.24  ? 137 CYS F O   1 
ATOM   10029 C CB  . CYS E 2 137 ? -47.520 -0.513  13.293  1.00 65.38  ? 137 CYS F CB  1 
ATOM   10030 S SG  . CYS E 2 137 ? -46.307 -1.683  13.947  1.00 80.97  ? 137 CYS F SG  1 
ATOM   10031 N N   . PHE E 2 138 ? -48.303 1.334   10.782  1.00 53.38  ? 138 PHE F N   1 
ATOM   10032 C CA  . PHE E 2 138 ? -49.400 1.965   10.067  1.00 53.02  ? 138 PHE F CA  1 
ATOM   10033 C C   . PHE E 2 138 ? -50.450 0.907   9.760   1.00 58.44  ? 138 PHE F C   1 
ATOM   10034 O O   . PHE E 2 138 ? -50.121 -0.142  9.200   1.00 56.71  ? 138 PHE F O   1 
ATOM   10035 C CB  . PHE E 2 138 ? -48.905 2.563   8.749   1.00 51.91  ? 138 PHE F CB  1 
ATOM   10036 C CG  . PHE E 2 138 ? -47.874 3.638   8.918   1.00 58.87  ? 138 PHE F CG  1 
ATOM   10037 C CD1 . PHE E 2 138 ? -46.532 3.316   9.060   1.00 60.00  ? 138 PHE F CD1 1 
ATOM   10038 C CD2 . PHE E 2 138 ? -48.246 4.975   8.933   1.00 65.14  ? 138 PHE F CD2 1 
ATOM   10039 C CE1 . PHE E 2 138 ? -45.579 4.311   9.216   1.00 61.27  ? 138 PHE F CE1 1 
ATOM   10040 C CE2 . PHE E 2 138 ? -47.300 5.977   9.090   1.00 67.18  ? 138 PHE F CE2 1 
ATOM   10041 C CZ  . PHE E 2 138 ? -45.965 5.643   9.231   1.00 69.54  ? 138 PHE F CZ  1 
ATOM   10042 N N   . GLU E 2 139 ? -51.702 1.172   10.132  1.00 61.17  ? 139 GLU F N   1 
ATOM   10043 C CA  . GLU E 2 139 ? -52.824 0.347   9.692   1.00 62.93  ? 139 GLU F CA  1 
ATOM   10044 C C   . GLU E 2 139 ? -53.420 0.991   8.448   1.00 67.13  ? 139 GLU F C   1 
ATOM   10045 O O   . GLU E 2 139 ? -53.855 2.142   8.482   1.00 67.41  ? 139 GLU F O   1 
ATOM   10046 C CB  . GLU E 2 139 ? -53.881 0.202   10.790  1.00 68.56  ? 139 GLU F CB  1 
ATOM   10047 C CG  . GLU E 2 139 ? -55.015 -0.753  10.438  1.00 77.80  ? 139 GLU F CG  1 
ATOM   10048 C CD  . GLU E 2 139 ? -56.004 -0.934  11.575  1.00 85.47  ? 139 GLU F CD  1 
ATOM   10049 O OE1 . GLU E 2 139 ? -56.210 -2.087  12.014  1.00 80.77  ? 139 GLU F OE1 1 
ATOM   10050 O OE2 . GLU E 2 139 ? -56.573 0.078   12.033  1.00 89.98  ? 139 GLU F OE2 1 
ATOM   10051 N N   . PHE E 2 140 ? -53.416 0.253   7.342   1.00 67.03  ? 140 PHE F N   1 
ATOM   10052 C CA  . PHE E 2 140 ? -53.944 0.758   6.075   1.00 63.52  ? 140 PHE F CA  1 
ATOM   10053 C C   . PHE E 2 140 ? -55.467 0.816   6.093   1.00 63.78  ? 140 PHE F C   1 
ATOM   10054 O O   . PHE E 2 140 ? -56.127 -0.055  6.670   1.00 58.32  ? 140 PHE F O   1 
ATOM   10055 C CB  . PHE E 2 140 ? -53.500 -0.134  4.921   1.00 63.08  ? 140 PHE F CB  1 
ATOM   10056 C CG  . PHE E 2 140 ? -52.076 0.069   4.510   1.00 56.21  ? 140 PHE F CG  1 
ATOM   10057 C CD1 . PHE E 2 140 ? -51.063 -0.695  5.067   1.00 54.89  ? 140 PHE F CD1 1 
ATOM   10058 C CD2 . PHE E 2 140 ? -51.750 1.023   3.555   1.00 50.65  ? 140 PHE F CD2 1 
ATOM   10059 C CE1 . PHE E 2 140 ? -49.747 -0.510  4.683   1.00 57.23  ? 140 PHE F CE1 1 
ATOM   10060 C CE2 . PHE E 2 140 ? -50.435 1.214   3.163   1.00 54.67  ? 140 PHE F CE2 1 
ATOM   10061 C CZ  . PHE E 2 140 ? -49.432 0.446   3.729   1.00 58.18  ? 140 PHE F CZ  1 
ATOM   10062 N N   . TYR E 2 141 ? -56.010 1.848   5.451   1.00 71.45  ? 141 TYR F N   1 
ATOM   10063 C CA  . TYR E 2 141 ? -57.455 1.988   5.285   1.00 71.63  ? 141 TYR F CA  1 
ATOM   10064 C C   . TYR E 2 141 ? -57.950 1.274   4.027   1.00 73.27  ? 141 TYR F C   1 
ATOM   10065 O O   . TYR E 2 141 ? -59.155 1.219   3.787   1.00 79.00  ? 141 TYR F O   1 
ATOM   10066 C CB  . TYR E 2 141 ? -57.862 3.464   5.193   1.00 69.97  ? 141 TYR F CB  1 
ATOM   10067 C CG  . TYR E 2 141 ? -57.741 4.253   6.476   1.00 72.62  ? 141 TYR F CG  1 
ATOM   10068 C CD1 . TYR E 2 141 ? -58.314 3.797   7.667   1.00 72.72  ? 141 TYR F CD1 1 
ATOM   10069 C CD2 . TYR E 2 141 ? -57.073 5.476   6.491   1.00 67.13  ? 141 TYR F CD2 1 
ATOM   10070 C CE1 . TYR E 2 141 ? -58.202 4.534   8.839   1.00 74.06  ? 141 TYR F CE1 1 
ATOM   10071 C CE2 . TYR E 2 141 ? -56.960 6.217   7.650   1.00 64.38  ? 141 TYR F CE2 1 
ATOM   10072 C CZ  . TYR E 2 141 ? -57.525 5.753   8.822   1.00 75.15  ? 141 TYR F CZ  1 
ATOM   10073 O OH  . TYR E 2 141 ? -57.386 6.508   9.974   1.00 85.42  ? 141 TYR F OH  1 
ATOM   10074 N N   . HIS E 2 142 ? -57.023 0.763   3.216   1.00 70.63  ? 142 HIS F N   1 
ATOM   10075 C CA  . HIS E 2 142 ? -57.363 0.026   2.002   1.00 69.37  ? 142 HIS F CA  1 
ATOM   10076 C C   . HIS E 2 142 ? -56.624 -1.275  1.978   1.00 71.60  ? 142 HIS F C   1 
ATOM   10077 O O   . HIS E 2 142 ? -55.748 -1.517  2.807   1.00 75.14  ? 142 HIS F O   1 
ATOM   10078 C CB  . HIS E 2 142 ? -57.037 0.846   0.755   1.00 70.76  ? 142 HIS F CB  1 
ATOM   10079 C CG  . HIS E 2 142 ? -55.562 1.092   0.544   1.00 74.20  ? 142 HIS F CG  1 
ATOM   10080 N ND1 . HIS E 2 142 ? -54.913 2.125   1.110   1.00 75.58  ? 142 HIS F ND1 1 
ATOM   10081 C CD2 . HIS E 2 142 ? -54.620 0.403   -0.217  1.00 72.15  ? 142 HIS F CD2 1 
ATOM   10082 C CE1 . HIS E 2 142 ? -53.619 2.099   0.741   1.00 69.29  ? 142 HIS F CE1 1 
ATOM   10083 N NE2 . HIS E 2 142 ? -53.440 1.045   -0.074  1.00 67.58  ? 142 HIS F NE2 1 
ATOM   10084 N N   . LYS E 2 143 ? -56.971 -2.131  1.024   1.00 81.17  ? 143 LYS F N   1 
ATOM   10085 C CA  . LYS E 2 143 ? -56.286 -3.418  0.873   1.00 79.64  ? 143 LYS F CA  1 
ATOM   10086 C C   . LYS E 2 143 ? -54.936 -3.226  0.199   1.00 70.55  ? 143 LYS F C   1 
ATOM   10087 O O   . LYS E 2 143 ? -54.868 -2.834  -0.970  1.00 73.97  ? 143 LYS F O   1 
ATOM   10088 C CB  . LYS E 2 143 ? -57.141 -4.421  0.103   1.00 88.06  ? 143 LYS F CB  1 
ATOM   10089 C CG  . LYS E 2 143 ? -58.234 -5.002  0.981   1.00 98.33  ? 143 LYS F CG  1 
ATOM   10090 C CD  . LYS E 2 143 ? -59.063 -6.031  0.243   1.00 104.87 ? 143 LYS F CD  1 
ATOM   10091 C CE  . LYS E 2 143 ? -59.951 -6.802  1.202   1.00 102.06 ? 143 LYS F CE  1 
ATOM   10092 N NZ  . LYS E 2 143 ? -60.776 -7.835  0.517   1.00 101.06 ? 143 LYS F NZ  1 
ATOM   10093 N N   . CYS E 2 144 ? -53.868 -3.500  0.946   1.00 66.83  ? 144 CYS F N   1 
ATOM   10094 C CA  . CYS E 2 144 ? -52.507 -3.335  0.444   1.00 69.36  ? 144 CYS F CA  1 
ATOM   10095 C C   . CYS E 2 144 ? -51.840 -4.701  0.268   1.00 66.98  ? 144 CYS F C   1 
ATOM   10096 O O   . CYS E 2 144 ? -51.433 -5.345  1.239   1.00 65.63  ? 144 CYS F O   1 
ATOM   10097 C CB  . CYS E 2 144 ? -51.694 -2.450  1.392   1.00 66.80  ? 144 CYS F CB  1 
ATOM   10098 S SG  . CYS E 2 144 ? -50.040 -2.014  0.809   1.00 70.28  ? 144 CYS F SG  1 
ATOM   10099 N N   . ASP E 2 145 ? -51.748 -5.133  -0.986  1.00 67.60  ? 145 ASP F N   1 
ATOM   10100 C CA  . ASP E 2 145 ? -51.165 -6.428  -1.338  1.00 68.06  ? 145 ASP F CA  1 
ATOM   10101 C C   . ASP E 2 145 ? -49.632 -6.356  -1.390  1.00 64.35  ? 145 ASP F C   1 
ATOM   10102 O O   . ASP E 2 145 ? -49.044 -5.301  -1.140  1.00 58.33  ? 145 ASP F O   1 
ATOM   10103 C CB  . ASP E 2 145 ? -51.751 -6.914  -2.677  1.00 71.41  ? 145 ASP F CB  1 
ATOM   10104 C CG  . ASP E 2 145 ? -51.405 -5.991  -3.848  1.00 81.57  ? 145 ASP F CG  1 
ATOM   10105 O OD1 . ASP E 2 145 ? -51.708 -4.782  -3.765  1.00 94.55  ? 145 ASP F OD1 1 
ATOM   10106 O OD2 . ASP E 2 145 ? -50.839 -6.476  -4.856  1.00 92.98  ? 145 ASP F OD2 1 
ATOM   10107 N N   . ASN E 2 146 ? -48.990 -7.477  -1.720  1.00 60.22  ? 146 ASN F N   1 
ATOM   10108 C CA  . ASN E 2 146 ? -47.526 -7.555  -1.747  1.00 58.70  ? 146 ASN F CA  1 
ATOM   10109 C C   . ASN E 2 146 ? -46.876 -6.586  -2.734  1.00 64.77  ? 146 ASN F C   1 
ATOM   10110 O O   . ASN E 2 146 ? -45.741 -6.171  -2.529  1.00 75.71  ? 146 ASN F O   1 
ATOM   10111 C CB  . ASN E 2 146 ? -47.060 -8.987  -2.038  1.00 52.37  ? 146 ASN F CB  1 
ATOM   10112 C CG  . ASN E 2 146 ? -47.310 -9.933  -0.881  1.00 54.58  ? 146 ASN F CG  1 
ATOM   10113 O OD1 . ASN E 2 146 ? -47.735 -9.522  0.202   1.00 54.29  ? 146 ASN F OD1 1 
ATOM   10114 N ND2 . ASN E 2 146 ? -47.044 -11.213 -1.104  1.00 51.99  ? 146 ASN F ND2 1 
ATOM   10115 N N   . GLU E 2 147 ? -47.587 -6.240  -3.803  1.00 65.04  ? 147 GLU F N   1 
ATOM   10116 C CA  . GLU E 2 147 ? -47.122 -5.237  -4.753  1.00 68.03  ? 147 GLU F CA  1 
ATOM   10117 C C   . GLU E 2 147 ? -47.204 -3.858  -4.104  1.00 64.02  ? 147 GLU F C   1 
ATOM   10118 O O   . GLU E 2 147 ? -46.291 -3.042  -4.220  1.00 66.10  ? 147 GLU F O   1 
ATOM   10119 C CB  . GLU E 2 147 ? -48.032 -5.231  -6.001  1.00 77.21  ? 147 GLU F CB  1 
ATOM   10120 C CG  . GLU E 2 147 ? -47.417 -4.549  -7.219  1.00 88.23  ? 147 GLU F CG  1 
ATOM   10121 C CD  . GLU E 2 147 ? -48.435 -3.856  -8.131  1.00 98.78  ? 147 GLU F CD  1 
ATOM   10122 O OE1 . GLU E 2 147 ? -48.324 -4.037  -9.361  1.00 88.59  ? 147 GLU F OE1 1 
ATOM   10123 O OE2 . GLU E 2 147 ? -49.328 -3.112  -7.646  1.00 106.34 ? 147 GLU F OE2 1 
ATOM   10124 N N   . CYS E 2 148 ? -48.330 -3.602  -3.448  1.00 65.54  ? 148 CYS F N   1 
ATOM   10125 C CA  . CYS E 2 148 ? -48.560 -2.340  -2.752  1.00 59.59  ? 148 CYS F CA  1 
ATOM   10126 C C   . CYS E 2 148 ? -47.532 -2.122  -1.641  1.00 60.57  ? 148 CYS F C   1 
ATOM   10127 O O   . CYS E 2 148 ? -47.042 -1.008  -1.459  1.00 67.54  ? 148 CYS F O   1 
ATOM   10128 C CB  . CYS E 2 148 ? -49.988 -2.314  -2.197  1.00 63.24  ? 148 CYS F CB  1 
ATOM   10129 S SG  . CYS E 2 148 ? -50.342 -1.041  -0.963  1.00 70.19  ? 148 CYS F SG  1 
ATOM   10130 N N   . MET E 2 149 ? -47.201 -3.186  -0.911  1.00 60.56  ? 149 MET F N   1 
ATOM   10131 C CA  . MET E 2 149 ? -46.211 -3.106  0.164   1.00 61.01  ? 149 MET F CA  1 
ATOM   10132 C C   . MET E 2 149 ? -44.815 -2.791  -0.382  1.00 64.94  ? 149 MET F C   1 
ATOM   10133 O O   . MET E 2 149 ? -44.085 -1.994  0.200   1.00 63.47  ? 149 MET F O   1 
ATOM   10134 C CB  . MET E 2 149 ? -46.173 -4.413  0.961   1.00 63.52  ? 149 MET F CB  1 
ATOM   10135 C CG  . MET E 2 149 ? -47.432 -4.711  1.767   1.00 64.13  ? 149 MET F CG  1 
ATOM   10136 S SD  . MET E 2 149 ? -47.662 -3.626  3.188   1.00 60.55  ? 149 MET F SD  1 
ATOM   10137 C CE  . MET E 2 149 ? -49.012 -4.439  4.045   1.00 52.18  ? 149 MET F CE  1 
ATOM   10138 N N   . GLU E 2 150 ? -44.450 -3.423  -1.496  1.00 70.33  ? 150 GLU F N   1 
ATOM   10139 C CA  . GLU E 2 150 ? -43.161 -3.169  -2.151  1.00 73.43  ? 150 GLU F CA  1 
ATOM   10140 C C   . GLU E 2 150 ? -43.006 -1.702  -2.539  1.00 74.21  ? 150 GLU F C   1 
ATOM   10141 O O   . GLU E 2 150 ? -41.951 -1.110  -2.328  1.00 82.13  ? 150 GLU F O   1 
ATOM   10142 C CB  . GLU E 2 150 ? -43.002 -4.047  -3.399  1.00 82.59  ? 150 GLU F CB  1 
ATOM   10143 C CG  . GLU E 2 150 ? -42.669 -5.505  -3.106  1.00 93.76  ? 150 GLU F CG  1 
ATOM   10144 C CD  . GLU E 2 150 ? -42.984 -6.448  -4.262  1.00 102.50 ? 150 GLU F CD  1 
ATOM   10145 O OE1 . GLU E 2 150 ? -43.348 -5.977  -5.363  1.00 118.27 ? 150 GLU F OE1 1 
ATOM   10146 O OE2 . GLU E 2 150 ? -42.868 -7.676  -4.069  1.00 95.89  ? 150 GLU F OE2 1 
ATOM   10147 N N   . SER E 2 151 ? -44.058 -1.120  -3.105  1.00 77.20  ? 151 SER F N   1 
ATOM   10148 C CA  . SER E 2 151 ? -44.022 0.279   -3.548  1.00 81.61  ? 151 SER F CA  1 
ATOM   10149 C C   . SER E 2 151 ? -43.786 1.252   -2.389  1.00 81.23  ? 151 SER F C   1 
ATOM   10150 O O   . SER E 2 151 ? -43.200 2.325   -2.582  1.00 89.04  ? 151 SER F O   1 
ATOM   10151 C CB  . SER E 2 151 ? -45.312 0.642   -4.283  1.00 85.03  ? 151 SER F CB  1 
ATOM   10152 O OG  . SER E 2 151 ? -46.432 0.581   -3.421  1.00 89.82  ? 151 SER F OG  1 
ATOM   10153 N N   . VAL E 2 152 ? -44.238 0.872   -1.194  1.00 76.00  ? 152 VAL F N   1 
ATOM   10154 C CA  . VAL E 2 152 ? -44.014 1.672   0.013   1.00 74.65  ? 152 VAL F CA  1 
ATOM   10155 C C   . VAL E 2 152 ? -42.534 1.648   0.410   1.00 78.49  ? 152 VAL F C   1 
ATOM   10156 O O   . VAL E 2 152 ? -42.003 2.635   0.916   1.00 69.53  ? 152 VAL F O   1 
ATOM   10157 C CB  . VAL E 2 152 ? -44.895 1.195   1.185   1.00 70.55  ? 152 VAL F CB  1 
ATOM   10158 C CG1 . VAL E 2 152 ? -44.677 2.070   2.411   1.00 69.89  ? 152 VAL F CG1 1 
ATOM   10159 C CG2 . VAL E 2 152 ? -46.362 1.215   0.785   1.00 62.73  ? 152 VAL F CG2 1 
ATOM   10160 N N   . ARG E 2 153 ? -41.872 0.520   0.162   1.00 82.67  ? 153 ARG F N   1 
ATOM   10161 C CA  . ARG E 2 153 ? -40.431 0.396   0.392   1.00 84.84  ? 153 ARG F CA  1 
ATOM   10162 C C   . ARG E 2 153 ? -39.630 1.068   -0.724  1.00 85.53  ? 153 ARG F C   1 
ATOM   10163 O O   . ARG E 2 153 ? -38.622 1.719   -0.452  1.00 93.60  ? 153 ARG F O   1 
ATOM   10164 C CB  . ARG E 2 153 ? -40.025 -1.075  0.497   1.00 77.29  ? 153 ARG F CB  1 
ATOM   10165 C CG  . ARG E 2 153 ? -40.816 -1.863  1.529   1.00 68.79  ? 153 ARG F CG  1 
ATOM   10166 C CD  . ARG E 2 153 ? -40.262 -3.264  1.713   1.00 71.41  ? 153 ARG F CD  1 
ATOM   10167 N NE  . ARG E 2 153 ? -41.337 -4.234  1.937   1.00 77.28  ? 153 ARG F NE  1 
ATOM   10168 C CZ  . ARG E 2 153 ? -41.719 -5.184  1.079   1.00 73.63  ? 153 ARG F CZ  1 
ATOM   10169 N NH1 . ARG E 2 153 ? -41.115 -5.352  -0.097  1.00 76.21  ? 153 ARG F NH1 1 
ATOM   10170 N NH2 . ARG E 2 153 ? -42.719 -5.991  1.406   1.00 70.99  ? 153 ARG F NH2 1 
ATOM   10171 N N   . ASN E 2 154 ? -40.077 0.889   -1.970  1.00 89.71  ? 154 ASN F N   1 
ATOM   10172 C CA  . ASN E 2 154 ? -39.473 1.550   -3.136  1.00 84.06  ? 154 ASN F CA  1 
ATOM   10173 C C   . ASN E 2 154 ? -39.346 3.052   -2.939  1.00 87.87  ? 154 ASN F C   1 
ATOM   10174 O O   . ASN E 2 154 ? -38.330 3.655   -3.298  1.00 97.32  ? 154 ASN F O   1 
ATOM   10175 C CB  . ASN E 2 154 ? -40.327 1.345   -4.395  1.00 79.52  ? 154 ASN F CB  1 
ATOM   10176 C CG  . ASN E 2 154 ? -40.170 -0.027  -5.019  1.00 83.99  ? 154 ASN F CG  1 
ATOM   10177 O OD1 . ASN E 2 154 ? -39.525 -0.925  -4.458  1.00 78.86  ? 154 ASN F OD1 1 
ATOM   10178 N ND2 . ASN E 2 154 ? -40.766 -0.183  -6.218  1.00 93.60  ? 154 ASN F ND2 1 
ATOM   10179 N N   . GLY E 2 155 ? -40.398 3.647   -2.382  1.00 83.42  ? 155 GLY F N   1 
ATOM   10180 C CA  . GLY E 2 155 ? -40.531 5.094   -2.334  1.00 94.14  ? 155 GLY F CA  1 
ATOM   10181 C C   . GLY E 2 155 ? -41.363 5.631   -3.484  1.00 105.75 ? 155 GLY F C   1 
ATOM   10182 O O   . GLY E 2 155 ? -41.284 6.815   -3.808  1.00 123.22 ? 155 GLY F O   1 
ATOM   10183 N N   . THR E 2 156 ? -42.169 4.769   -4.102  1.00 103.16 ? 156 THR F N   1 
ATOM   10184 C CA  . THR E 2 156 ? -43.014 5.177   -5.228  1.00 105.99 ? 156 THR F CA  1 
ATOM   10185 C C   . THR E 2 156 ? -44.450 4.669   -5.079  1.00 94.88  ? 156 THR F C   1 
ATOM   10186 O O   . THR E 2 156 ? -45.151 4.406   -6.063  1.00 97.16  ? 156 THR F O   1 
ATOM   10187 C CB  . THR E 2 156 ? -42.398 4.699   -6.549  1.00 118.82 ? 156 THR F CB  1 
ATOM   10188 O OG1 . THR E 2 156 ? -42.139 3.291   -6.474  1.00 119.40 ? 156 THR F OG1 1 
ATOM   10189 C CG2 . THR E 2 156 ? -41.109 5.462   -6.853  1.00 117.28 ? 156 THR F CG2 1 
ATOM   10190 N N   . TYR E 2 157 ? -44.887 4.558   -3.830  1.00 87.65  ? 157 TYR F N   1 
ATOM   10191 C CA  . TYR E 2 157 ? -46.274 4.238   -3.506  1.00 85.66  ? 157 TYR F CA  1 
ATOM   10192 C C   . TYR E 2 157 ? -47.194 5.264   -4.155  1.00 81.92  ? 157 TYR F C   1 
ATOM   10193 O O   . TYR E 2 157 ? -47.058 6.465   -3.917  1.00 68.24  ? 157 TYR F O   1 
ATOM   10194 C CB  . TYR E 2 157 ? -46.445 4.210   -1.987  1.00 79.27  ? 157 TYR F CB  1 
ATOM   10195 C CG  . TYR E 2 157 ? -47.860 4.250   -1.475  1.00 71.66  ? 157 TYR F CG  1 
ATOM   10196 C CD1 . TYR E 2 157 ? -48.620 3.087   -1.344  1.00 70.75  ? 157 TYR F CD1 1 
ATOM   10197 C CD2 . TYR E 2 157 ? -48.423 5.450   -1.073  1.00 68.35  ? 157 TYR F CD2 1 
ATOM   10198 C CE1 . TYR E 2 157 ? -49.914 3.131   -0.849  1.00 68.46  ? 157 TYR F CE1 1 
ATOM   10199 C CE2 . TYR E 2 157 ? -49.710 5.505   -0.584  1.00 70.08  ? 157 TYR F CE2 1 
ATOM   10200 C CZ  . TYR E 2 157 ? -50.448 4.348   -0.473  1.00 71.25  ? 157 TYR F CZ  1 
ATOM   10201 O OH  . TYR E 2 157 ? -51.721 4.431   0.020   1.00 74.83  ? 157 TYR F OH  1 
ATOM   10202 N N   . ASP E 2 158 ? -48.113 4.775   -4.987  1.00 97.61  ? 158 ASP F N   1 
ATOM   10203 C CA  . ASP E 2 158 ? -49.031 5.627   -5.734  1.00 102.86 ? 158 ASP F CA  1 
ATOM   10204 C C   . ASP E 2 158 ? -50.227 5.994   -4.851  1.00 95.65  ? 158 ASP F C   1 
ATOM   10205 O O   . ASP E 2 158 ? -51.183 5.223   -4.722  1.00 82.33  ? 158 ASP F O   1 
ATOM   10206 C CB  . ASP E 2 158 ? -49.486 4.911   -7.017  1.00 107.90 ? 158 ASP F CB  1 
ATOM   10207 C CG  . ASP E 2 158 ? -50.113 5.856   -8.037  1.00 113.04 ? 158 ASP F CG  1 
ATOM   10208 O OD1 . ASP E 2 158 ? -50.689 5.352   -9.022  1.00 117.55 ? 158 ASP F OD1 1 
ATOM   10209 O OD2 . ASP E 2 158 ? -50.032 7.092   -7.869  1.00 119.98 ? 158 ASP F OD2 1 
ATOM   10210 N N   . TYR E 2 159 ? -50.156 7.174   -4.237  1.00 95.57  ? 159 TYR F N   1 
ATOM   10211 C CA  . TYR E 2 159 ? -51.189 7.648   -3.310  1.00 100.53 ? 159 TYR F CA  1 
ATOM   10212 C C   . TYR E 2 159 ? -52.565 7.850   -3.961  1.00 106.22 ? 159 TYR F C   1 
ATOM   10213 O O   . TYR E 2 159 ? -53.558 7.326   -3.448  1.00 99.94  ? 159 TYR F O   1 
ATOM   10214 C CB  . TYR E 2 159 ? -50.731 8.935   -2.604  1.00 97.92  ? 159 TYR F CB  1 
ATOM   10215 C CG  . TYR E 2 159 ? -51.828 9.661   -1.853  1.00 101.21 ? 159 TYR F CG  1 
ATOM   10216 C CD1 . TYR E 2 159 ? -52.215 9.256   -0.577  1.00 98.56  ? 159 TYR F CD1 1 
ATOM   10217 C CD2 . TYR E 2 159 ? -52.481 10.757  -2.418  1.00 106.12 ? 159 TYR F CD2 1 
ATOM   10218 C CE1 . TYR E 2 159 ? -53.223 9.919   0.111   1.00 94.54  ? 159 TYR F CE1 1 
ATOM   10219 C CE2 . TYR E 2 159 ? -53.487 11.424  -1.738  1.00 107.44 ? 159 TYR F CE2 1 
ATOM   10220 C CZ  . TYR E 2 159 ? -53.855 11.001  -0.475  1.00 99.34  ? 159 TYR F CZ  1 
ATOM   10221 O OH  . TYR E 2 159 ? -54.856 11.663  0.199   1.00 96.65  ? 159 TYR F OH  1 
ATOM   10222 N N   . PRO E 2 160 ? -52.635 8.604   -5.082  1.00 117.84 ? 160 PRO F N   1 
ATOM   10223 C CA  . PRO E 2 160 ? -53.953 8.836   -5.705  1.00 111.98 ? 160 PRO F CA  1 
ATOM   10224 C C   . PRO E 2 160 ? -54.718 7.559   -6.074  1.00 106.27 ? 160 PRO F C   1 
ATOM   10225 O O   . PRO E 2 160 ? -55.953 7.559   -6.063  1.00 107.44 ? 160 PRO F O   1 
ATOM   10226 C CB  . PRO E 2 160 ? -53.633 9.643   -6.976  1.00 113.65 ? 160 PRO F CB  1 
ATOM   10227 C CG  . PRO E 2 160 ? -52.163 9.855   -7.011  1.00 112.40 ? 160 PRO F CG  1 
ATOM   10228 C CD  . PRO E 2 160 ? -51.557 9.374   -5.732  1.00 112.62 ? 160 PRO F CD  1 
ATOM   10229 N N   . GLN E 2 161 ? -53.985 6.492   -6.387  1.00 95.83  ? 161 GLN F N   1 
ATOM   10230 C CA  . GLN E 2 161 ? -54.578 5.230   -6.834  1.00 91.27  ? 161 GLN F CA  1 
ATOM   10231 C C   . GLN E 2 161 ? -55.475 4.567   -5.778  1.00 88.20  ? 161 GLN F C   1 
ATOM   10232 O O   . GLN E 2 161 ? -56.475 3.938   -6.124  1.00 86.90  ? 161 GLN F O   1 
ATOM   10233 C CB  . GLN E 2 161 ? -53.476 4.259   -7.279  1.00 93.72  ? 161 GLN F CB  1 
ATOM   10234 C CG  . GLN E 2 161 ? -53.970 3.131   -8.213  1.00 92.41  ? 161 GLN F CG  1 
ATOM   10235 C CD  . GLN E 2 161 ? -53.846 1.783   -7.566  1.00 90.26  ? 161 GLN F CD  1 
ATOM   10236 O OE1 . GLN E 2 161 ? -54.470 1.537   -6.548  1.00 93.48  ? 161 GLN F OE1 1 
ATOM   10237 N NE2 . GLN E 2 161 ? -53.041 0.903   -8.151  1.00 85.13  ? 161 GLN F NE2 1 
ATOM   10238 N N   . TYR E 2 162 ? -55.118 4.706   -4.502  1.00 87.45  ? 162 TYR F N   1 
ATOM   10239 C CA  . TYR E 2 162 ? -55.893 4.113   -3.402  1.00 79.19  ? 162 TYR F CA  1 
ATOM   10240 C C   . TYR E 2 162 ? -56.669 5.151   -2.588  1.00 77.26  ? 162 TYR F C   1 
ATOM   10241 O O   . TYR E 2 162 ? -57.422 4.786   -1.677  1.00 74.37  ? 162 TYR F O   1 
ATOM   10242 C CB  . TYR E 2 162 ? -54.971 3.345   -2.450  1.00 76.89  ? 162 TYR F CB  1 
ATOM   10243 C CG  . TYR E 2 162 ? -54.137 2.271   -3.108  1.00 76.01  ? 162 TYR F CG  1 
ATOM   10244 C CD1 . TYR E 2 162 ? -52.803 2.503   -3.439  1.00 79.19  ? 162 TYR F CD1 1 
ATOM   10245 C CD2 . TYR E 2 162 ? -54.677 1.019   -3.390  1.00 76.51  ? 162 TYR F CD2 1 
ATOM   10246 C CE1 . TYR E 2 162 ? -52.034 1.518   -4.037  1.00 80.53  ? 162 TYR F CE1 1 
ATOM   10247 C CE2 . TYR E 2 162 ? -53.920 0.026   -3.983  1.00 80.01  ? 162 TYR F CE2 1 
ATOM   10248 C CZ  . TYR E 2 162 ? -52.600 0.281   -4.306  1.00 82.47  ? 162 TYR F CZ  1 
ATOM   10249 O OH  . TYR E 2 162 ? -51.848 -0.698  -4.899  1.00 81.85  ? 162 TYR F OH  1 
ATOM   10250 N N   . SER E 2 163 ? -56.490 6.432   -2.912  1.00 75.34  ? 163 SER F N   1 
ATOM   10251 C CA  . SER E 2 163 ? -57.006 7.522   -2.076  1.00 81.76  ? 163 SER F CA  1 
ATOM   10252 C C   . SER E 2 163 ? -58.521 7.500   -1.885  1.00 83.13  ? 163 SER F C   1 
ATOM   10253 O O   . SER E 2 163 ? -59.017 7.779   -0.789  1.00 80.28  ? 163 SER F O   1 
ATOM   10254 C CB  . SER E 2 163 ? -56.580 8.881   -2.641  1.00 79.97  ? 163 SER F CB  1 
ATOM   10255 O OG  . SER E 2 163 ? -57.113 9.091   -3.935  1.00 73.17  ? 163 SER F OG  1 
ATOM   10256 N N   . GLU E 2 164 ? -59.253 7.165   -2.942  1.00 90.06  ? 164 GLU F N   1 
ATOM   10257 C CA  . GLU E 2 164 ? -60.713 7.114   -2.855  1.00 97.89  ? 164 GLU F CA  1 
ATOM   10258 C C   . GLU E 2 164 ? -61.189 5.986   -1.955  1.00 88.30  ? 164 GLU F C   1 
ATOM   10259 O O   . GLU E 2 164 ? -61.988 6.215   -1.043  1.00 85.00  ? 164 GLU F O   1 
ATOM   10260 C CB  . GLU E 2 164 ? -61.347 6.991   -4.240  1.00 108.99 ? 164 GLU F CB  1 
ATOM   10261 C CG  . GLU E 2 164 ? -61.400 8.308   -4.985  1.00 114.27 ? 164 GLU F CG  1 
ATOM   10262 C CD  . GLU E 2 164 ? -62.510 9.215   -4.481  1.00 115.69 ? 164 GLU F CD  1 
ATOM   10263 O OE1 . GLU E 2 164 ? -62.259 9.876   -3.469  1.00 114.18 ? 164 GLU F OE1 1 
ATOM   10264 O OE2 . GLU E 2 164 ? -63.614 9.283   -5.078  1.00 111.64 ? 164 GLU F OE2 1 
ATOM   10265 N N   . GLU E 2 165 ? -60.696 4.775   -2.206  1.00 83.09  ? 165 GLU F N   1 
ATOM   10266 C CA  . GLU E 2 165 ? -61.037 3.623   -1.375  1.00 83.92  ? 165 GLU F CA  1 
ATOM   10267 C C   . GLU E 2 165 ? -60.794 3.941   0.099   1.00 88.54  ? 165 GLU F C   1 
ATOM   10268 O O   . GLU E 2 165 ? -61.584 3.551   0.959   1.00 81.12  ? 165 GLU F O   1 
ATOM   10269 C CB  . GLU E 2 165 ? -60.226 2.391   -1.789  1.00 82.55  ? 165 GLU F CB  1 
ATOM   10270 C CG  . GLU E 2 165 ? -60.629 1.108   -1.068  1.00 83.02  ? 165 GLU F CG  1 
ATOM   10271 C CD  . GLU E 2 165 ? -59.711 -0.063  -1.373  1.00 82.93  ? 165 GLU F CD  1 
ATOM   10272 O OE1 . GLU E 2 165 ? -58.933 0.015   -2.348  1.00 73.26  ? 165 GLU F OE1 1 
ATOM   10273 O OE2 . GLU E 2 165 ? -59.758 -1.064  -0.624  1.00 79.43  ? 165 GLU F OE2 1 
ATOM   10274 N N   . ALA E 2 166 ? -59.698 4.643   0.381   1.00 89.01  ? 166 ALA F N   1 
ATOM   10275 C CA  . ALA E 2 166 ? -59.364 5.032   1.765   1.00 95.60  ? 166 ALA F CA  1 
ATOM   10276 C C   . ALA E 2 166 ? -60.454 5.809   2.536   1.00 109.58 ? 166 ALA F C   1 
ATOM   10277 O O   . ALA E 2 166 ? -60.706 5.538   3.715   1.00 129.43 ? 166 ALA F O   1 
ATOM   10278 C CB  . ALA E 2 166 ? -58.064 5.827   1.775   1.00 94.80  ? 166 ALA F CB  1 
ATOM   10279 N N   . ARG E 2 167 ? -61.107 6.767   1.888   1.00 114.82 ? 167 ARG F N   1 
ATOM   10280 C CA  . ARG E 2 167 ? -62.091 7.616   2.590   1.00 117.49 ? 167 ARG F CA  1 
ATOM   10281 C C   . ARG E 2 167 ? -63.361 6.862   3.038   1.00 112.52 ? 167 ARG F C   1 
ATOM   10282 O O   . ARG E 2 167 ? -64.197 7.468   3.683   1.00 111.29 ? 167 ARG F O   1 
ATOM   10283 C CB  . ARG E 2 167 ? -62.480 8.838   1.736   1.00 114.19 ? 167 ARG F CB  1 
ATOM   10284 C CG  . ARG E 2 167 ? -61.297 9.634   1.193   1.00 115.99 ? 167 ARG F CG  1 
ATOM   10285 C CD  . ARG E 2 167 ? -61.746 10.836  0.376   1.00 117.54 ? 167 ARG F CD  1 
ATOM   10286 N NE  . ARG E 2 167 ? -62.831 10.493  -0.539  1.00 126.34 ? 167 ARG F NE  1 
ATOM   10287 C CZ  . ARG E 2 167 ? -63.760 11.342  -0.981  1.00 133.96 ? 167 ARG F CZ  1 
ATOM   10288 N NH1 . ARG E 2 167 ? -63.766 12.625  -0.615  1.00 138.12 ? 167 ARG F NH1 1 
ATOM   10289 N NH2 . ARG E 2 167 ? -64.700 10.899  -1.807  1.00 133.34 ? 167 ARG F NH2 1 
ATOM   10290 N N   . LEU E 2 168 ? -63.478 5.559   2.738   1.00 116.41 ? 168 LEU F N   1 
ATOM   10291 C CA  . LEU E 2 168 ? -64.696 4.763   2.966   1.00 122.59 ? 168 LEU F CA  1 
ATOM   10292 C C   . LEU E 2 168 ? -64.653 3.904   4.242   1.00 130.42 ? 168 LEU F C   1 
ATOM   10293 O O   . LEU E 2 168 ? -65.660 3.781   4.962   1.00 133.25 ? 168 LEU F O   1 
ATOM   10294 C CB  . LEU E 2 168 ? -64.915 3.845   1.749   1.00 120.74 ? 168 LEU F CB  1 
ATOM   10295 C CG  . LEU E 2 168 ? -65.018 4.498   0.360   1.00 120.84 ? 168 LEU F CG  1 
ATOM   10296 C CD1 . LEU E 2 168 ? -65.330 3.441   -0.688  1.00 112.00 ? 168 LEU F CD1 1 
ATOM   10297 C CD2 . LEU E 2 168 ? -66.077 5.589   0.343   1.00 119.92 ? 168 LEU F CD2 1 
ATOM   10298 N N   . LYS E 2 169 ? -63.495 3.297   4.501   1.00 135.49 ? 169 LYS F N   1 
ATOM   10299 C CA  . LYS E 2 169 ? -63.309 2.392   5.643   1.00 137.44 ? 169 LYS F CA  1 
ATOM   10300 C C   . LYS E 2 169 ? -63.339 3.127   6.988   1.00 135.81 ? 169 LYS F C   1 
ATOM   10301 O O   . LYS E 2 169 ? -63.604 2.517   8.024   1.00 114.19 ? 169 LYS F O   1 
ATOM   10302 C CB  . LYS E 2 169 ? -61.993 1.607   5.498   1.00 134.11 ? 169 LYS F CB  1 
ATOM   10303 C CG  . LYS E 2 169 ? -61.950 0.303   6.292   1.00 135.09 ? 169 LYS F CG  1 
ATOM   10304 C CD  . LYS E 2 169 ? -62.145 -0.916  5.401   1.00 138.59 ? 169 LYS F CD  1 
ATOM   10305 C CE  . LYS E 2 169 ? -63.568 -1.029  4.897   1.00 139.26 ? 169 LYS F CE  1 
ATOM   10306 N NZ  . LYS E 2 169 ? -63.820 -2.318  4.194   1.00 138.09 ? 169 LYS F NZ  1 
ATOM   10307 N N   . ARG E 2 170 ? -63.063 4.429   6.957   1.00 141.04 ? 170 ARG F N   1 
ATOM   10308 C CA  . ARG E 2 170 ? -63.091 5.277   8.160   1.00 140.92 ? 170 ARG F CA  1 
ATOM   10309 C C   . ARG E 2 170 ? -64.490 5.492   8.739   1.00 137.13 ? 170 ARG F C   1 
ATOM   10310 O O   . ARG E 2 170 ? -64.667 5.513   9.957   1.00 120.43 ? 170 ARG F O   1 
ATOM   10311 C CB  . ARG E 2 170 ? -62.436 6.637   7.873   1.00 128.79 ? 170 ARG F CB  1 
ATOM   10312 C CG  . ARG E 2 170 ? -61.073 6.784   8.519   1.00 110.56 ? 170 ARG F CG  1 
ATOM   10313 C CD  . ARG E 2 170 ? -60.381 8.057   8.069   1.00 103.58 ? 170 ARG F CD  1 
ATOM   10314 N NE  . ARG E 2 170 ? -60.061 8.048   6.637   1.00 102.65 ? 170 ARG F NE  1 
ATOM   10315 C CZ  . ARG E 2 170 ? -59.840 9.130   5.888   1.00 109.37 ? 170 ARG F CZ  1 
ATOM   10316 N NH1 . ARG E 2 170 ? -59.922 10.351  6.413   1.00 122.16 ? 170 ARG F NH1 1 
ATOM   10317 N NH2 . ARG E 2 170 ? -59.545 8.999   4.594   1.00 99.00  ? 170 ARG F NH2 1 
ATOM   10318 N N   . GLU E 2 171 ? -65.476 5.659   7.864   1.00 129.99 ? 171 GLU F N   1 
ATOM   10319 C CA  . GLU E 2 171 ? -66.842 5.892   8.291   1.00 115.73 ? 171 GLU F CA  1 
ATOM   10320 C C   . GLU E 2 171 ? -67.640 4.582   8.299   1.00 117.77 ? 171 GLU F C   1 
ATOM   10321 O O   . GLU E 2 171 ? -68.866 4.597   8.406   1.00 119.76 ? 171 GLU F O   1 
ATOM   10322 C CB  . GLU E 2 171 ? -67.491 6.929   7.381   1.00 108.86 ? 171 GLU F CB  1 
ATOM   10323 C CG  . GLU E 2 171 ? -66.945 8.345   7.556   1.00 108.87 ? 171 GLU F CG  1 
ATOM   10324 C CD  . GLU E 2 171 ? -65.831 8.659   6.586   1.00 109.71 ? 171 GLU F CD  1 
ATOM   10325 O OE1 . GLU E 2 171 ? -66.106 8.807   5.377   1.00 115.43 ? 171 GLU F OE1 1 
ATOM   10326 O OE2 . GLU E 2 171 ? -64.682 8.769   7.043   1.00 100.81 ? 171 GLU F OE2 1 
ATOM   10327 N N   . GLU E 2 172 ? -66.935 3.456   8.175   1.00 120.00 ? 172 GLU F N   1 
ATOM   10328 C CA  . GLU E 2 172 ? -67.524 2.126   8.322   1.00 124.52 ? 172 GLU F CA  1 
ATOM   10329 C C   . GLU E 2 172 ? -67.280 1.606   9.737   1.00 112.34 ? 172 GLU F C   1 
ATOM   10330 O O   . GLU E 2 172 ? -67.464 2.329   10.720  1.00 100.49 ? 172 GLU F O   1 
ATOM   10331 C CB  . GLU E 2 172 ? -66.910 1.162   7.299   1.00 134.44 ? 172 GLU F CB  1 
ATOM   10332 C CG  . GLU E 2 172 ? -67.474 -0.257  7.322   1.00 145.96 ? 172 GLU F CG  1 
ATOM   10333 C CD  . GLU E 2 172 ? -68.905 -0.345  6.821   1.00 158.52 ? 172 GLU F CD  1 
ATOM   10334 O OE1 . GLU E 2 172 ? -69.693 -1.116  7.409   1.00 161.91 ? 172 GLU F OE1 1 
ATOM   10335 O OE2 . GLU E 2 172 ? -69.245 0.348   5.838   1.00 161.92 ? 172 GLU F OE2 1 
ATOM   10336 N N   . ILE F 2 6   ? -39.376 23.990  -7.483  1.00 70.81  ? 6   ILE D N   1 
ATOM   10337 C CA  . ILE F 2 6   ? -38.631 24.408  -6.255  1.00 76.98  ? 6   ILE D CA  1 
ATOM   10338 C C   . ILE F 2 6   ? -38.774 23.326  -5.184  1.00 75.45  ? 6   ILE D C   1 
ATOM   10339 O O   . ILE F 2 6   ? -39.887 23.006  -4.768  1.00 68.25  ? 6   ILE D O   1 
ATOM   10340 C CB  . ILE F 2 6   ? -39.152 25.750  -5.700  1.00 82.17  ? 6   ILE D CB  1 
ATOM   10341 C CG1 . ILE F 2 6   ? -39.340 26.774  -6.834  1.00 93.78  ? 6   ILE D CG1 1 
ATOM   10342 C CG2 . ILE F 2 6   ? -38.196 26.286  -4.640  1.00 73.20  ? 6   ILE D CG2 1 
ATOM   10343 C CD1 . ILE F 2 6   ? -40.595 27.616  -6.711  1.00 93.30  ? 6   ILE D CD1 1 
ATOM   10344 N N   . ALA F 2 7   ? -37.644 22.777  -4.738  1.00 84.90  ? 7   ALA D N   1 
ATOM   10345 C CA  . ALA F 2 7   ? -37.618 21.637  -3.810  1.00 77.74  ? 7   ALA D CA  1 
ATOM   10346 C C   . ALA F 2 7   ? -37.987 22.049  -2.378  1.00 74.00  ? 7   ALA D C   1 
ATOM   10347 O O   . ALA F 2 7   ? -38.629 23.076  -2.180  1.00 80.26  ? 7   ALA D O   1 
ATOM   10348 C CB  . ALA F 2 7   ? -36.240 20.994  -3.841  1.00 83.15  ? 7   ALA D CB  1 
ATOM   10349 N N   . GLY F 2 8   ? -37.599 21.242  -1.389  1.00 76.09  ? 8   GLY D N   1 
ATOM   10350 C CA  . GLY F 2 8   ? -37.699 21.614  0.036   1.00 69.22  ? 8   GLY D CA  1 
ATOM   10351 C C   . GLY F 2 8   ? -36.402 21.278  0.751   1.00 60.68  ? 8   GLY D C   1 
ATOM   10352 O O   . GLY F 2 8   ? -35.368 21.122  0.106   1.00 67.10  ? 8   GLY D O   1 
ATOM   10353 N N   . PHE F 2 9   ? -36.445 21.155  2.076   1.00 59.29  ? 9   PHE D N   1 
ATOM   10354 C CA  . PHE F 2 9   ? -35.216 20.908  2.843   1.00 56.32  ? 9   PHE D CA  1 
ATOM   10355 C C   . PHE F 2 9   ? -34.586 19.562  2.505   1.00 58.63  ? 9   PHE D C   1 
ATOM   10356 O O   . PHE F 2 9   ? -33.387 19.501  2.236   1.00 57.87  ? 9   PHE D O   1 
ATOM   10357 C CB  . PHE F 2 9   ? -35.417 21.069  4.362   1.00 51.13  ? 9   PHE D CB  1 
ATOM   10358 C CG  . PHE F 2 9   ? -36.296 20.024  4.998   1.00 48.64  ? 9   PHE D CG  1 
ATOM   10359 C CD1 . PHE F 2 9   ? -37.678 20.161  4.997   1.00 53.10  ? 9   PHE D CD1 1 
ATOM   10360 C CD2 . PHE F 2 9   ? -35.743 18.934  5.645   1.00 48.72  ? 9   PHE D CD2 1 
ATOM   10361 C CE1 . PHE F 2 9   ? -38.489 19.218  5.602   1.00 52.01  ? 9   PHE D CE1 1 
ATOM   10362 C CE2 . PHE F 2 9   ? -36.553 17.987  6.255   1.00 55.19  ? 9   PHE D CE2 1 
ATOM   10363 C CZ  . PHE F 2 9   ? -37.928 18.125  6.227   1.00 52.14  ? 9   PHE D CZ  1 
ATOM   10364 N N   . ILE F 2 10  ? -35.388 18.498  2.468   1.00 63.54  ? 10  ILE D N   1 
ATOM   10365 C CA  . ILE F 2 10  ? -34.837 17.151  2.241   1.00 71.36  ? 10  ILE D CA  1 
ATOM   10366 C C   . ILE F 2 10  ? -34.512 16.836  0.757   1.00 72.94  ? 10  ILE D C   1 
ATOM   10367 O O   . ILE F 2 10  ? -34.775 15.732  0.252   1.00 74.88  ? 10  ILE D O   1 
ATOM   10368 C CB  . ILE F 2 10  ? -35.713 16.022  2.832   1.00 81.63  ? 10  ILE D CB  1 
ATOM   10369 C CG1 . ILE F 2 10  ? -37.165 16.159  2.364   1.00 73.95  ? 10  ILE D CG1 1 
ATOM   10370 C CG2 . ILE F 2 10  ? -35.622 16.007  4.349   1.00 88.62  ? 10  ILE D CG2 1 
ATOM   10371 C CD1 . ILE F 2 10  ? -37.603 15.010  1.487   1.00 75.62  ? 10  ILE D CD1 1 
ATOM   10372 N N   . GLU F 2 11  ? -33.975 17.827  0.052   1.00 72.11  ? 11  GLU D N   1 
ATOM   10373 C CA  . GLU F 2 11  ? -33.196 17.581  -1.160  1.00 74.48  ? 11  GLU D CA  1 
ATOM   10374 C C   . GLU F 2 11  ? -32.392 18.854  -1.453  1.00 70.94  ? 11  GLU D C   1 
ATOM   10375 O O   . GLU F 2 11  ? -32.550 19.498  -2.494  1.00 79.83  ? 11  GLU D O   1 
ATOM   10376 C CB  . GLU F 2 11  ? -34.061 17.131  -2.361  1.00 82.21  ? 11  GLU D CB  1 
ATOM   10377 C CG  . GLU F 2 11  ? -35.236 18.021  -2.745  1.00 85.38  ? 11  GLU D CG  1 
ATOM   10378 C CD  . GLU F 2 11  ? -36.114 17.412  -3.834  1.00 91.78  ? 11  GLU D CD  1 
ATOM   10379 O OE1 . GLU F 2 11  ? -35.693 16.422  -4.468  1.00 94.53  ? 11  GLU D OE1 1 
ATOM   10380 O OE2 . GLU F 2 11  ? -37.237 17.919  -4.060  1.00 88.73  ? 11  GLU D OE2 1 
ATOM   10381 N N   . GLY F 2 12  ? -31.553 19.224  -0.489  1.00 60.00  ? 12  GLY D N   1 
ATOM   10382 C CA  . GLY F 2 12  ? -30.612 20.325  -0.646  1.00 60.70  ? 12  GLY D CA  1 
ATOM   10383 C C   . GLY F 2 12  ? -31.041 21.646  -0.050  1.00 57.77  ? 12  GLY D C   1 
ATOM   10384 O O   . GLY F 2 12  ? -32.135 21.785  0.495   1.00 59.46  ? 12  GLY D O   1 
ATOM   10385 N N   . GLY F 2 13  ? -30.158 22.628  -0.188  1.00 52.15  ? 13  GLY D N   1 
ATOM   10386 C CA  . GLY F 2 13  ? -30.358 23.958  0.375   1.00 50.31  ? 13  GLY D CA  1 
ATOM   10387 C C   . GLY F 2 13  ? -30.722 24.992  -0.672  1.00 50.34  ? 13  GLY D C   1 
ATOM   10388 O O   . GLY F 2 13  ? -30.565 24.745  -1.862  1.00 43.03  ? 13  GLY D O   1 
ATOM   10389 N N   . TRP F 2 14  ? -31.224 26.145  -0.220  1.00 51.99  ? 14  TRP D N   1 
ATOM   10390 C CA  . TRP F 2 14  ? -31.507 27.277  -1.093  1.00 47.34  ? 14  TRP D CA  1 
ATOM   10391 C C   . TRP F 2 14  ? -30.275 28.102  -1.301  1.00 49.98  ? 14  TRP D C   1 
ATOM   10392 O O   . TRP F 2 14  ? -29.849 28.826  -0.397  1.00 52.25  ? 14  TRP D O   1 
ATOM   10393 C CB  . TRP F 2 14  ? -32.566 28.210  -0.492  1.00 47.38  ? 14  TRP D CB  1 
ATOM   10394 C CG  . TRP F 2 14  ? -33.865 27.606  -0.045  1.00 44.77  ? 14  TRP D CG  1 
ATOM   10395 C CD1 . TRP F 2 14  ? -34.692 28.053  0.995   1.00 44.19  ? 14  TRP D CD1 1 
ATOM   10396 C CD2 . TRP F 2 14  ? -34.564 26.464  -0.623  1.00 40.72  ? 14  TRP D CD2 1 
ATOM   10397 N NE1 . TRP F 2 14  ? -35.809 27.276  1.093   1.00 43.21  ? 14  TRP D NE1 1 
ATOM   10398 C CE2 . TRP F 2 14  ? -35.794 26.305  0.157   1.00 45.76  ? 14  TRP D CE2 1 
ATOM   10399 C CE3 . TRP F 2 14  ? -34.304 25.581  -1.659  1.00 43.15  ? 14  TRP D CE3 1 
ATOM   10400 C CZ2 . TRP F 2 14  ? -36.694 25.306  -0.109  1.00 51.54  ? 14  TRP D CZ2 1 
ATOM   10401 C CZ3 . TRP F 2 14  ? -35.221 24.578  -1.921  1.00 49.72  ? 14  TRP D CZ3 1 
ATOM   10402 C CH2 . TRP F 2 14  ? -36.383 24.448  -1.163  1.00 58.54  ? 14  TRP D CH2 1 
ATOM   10403 N N   . GLN F 2 15  ? -29.710 28.052  -2.501  1.00 55.02  ? 15  GLN D N   1 
ATOM   10404 C CA  . GLN F 2 15  ? -28.668 29.005  -2.868  1.00 60.49  ? 15  GLN D CA  1 
ATOM   10405 C C   . GLN F 2 15  ? -29.279 30.409  -3.023  1.00 66.16  ? 15  GLN D C   1 
ATOM   10406 O O   . GLN F 2 15  ? -28.592 31.414  -2.835  1.00 61.38  ? 15  GLN D O   1 
ATOM   10407 C CB  . GLN F 2 15  ? -27.958 28.569  -4.147  1.00 60.39  ? 15  GLN D CB  1 
ATOM   10408 C CG  . GLN F 2 15  ? -26.648 29.309  -4.408  1.00 69.79  ? 15  GLN D CG  1 
ATOM   10409 C CD  . GLN F 2 15  ? -25.405 28.424  -4.350  1.00 71.57  ? 15  GLN D CD  1 
ATOM   10410 O OE1 . GLN F 2 15  ? -25.486 27.196  -4.268  1.00 71.80  ? 15  GLN D OE1 1 
ATOM   10411 N NE2 . GLN F 2 15  ? -24.239 29.061  -4.389  1.00 68.01  ? 15  GLN D NE2 1 
ATOM   10412 N N   . GLY F 2 16  ? -30.573 30.465  -3.350  1.00 65.39  ? 16  GLY D N   1 
ATOM   10413 C CA  . GLY F 2 16  ? -31.306 31.726  -3.483  1.00 63.44  ? 16  GLY D CA  1 
ATOM   10414 C C   . GLY F 2 16  ? -31.626 32.426  -2.174  1.00 66.62  ? 16  GLY D C   1 
ATOM   10415 O O   . GLY F 2 16  ? -31.863 33.636  -2.159  1.00 65.48  ? 16  GLY D O   1 
ATOM   10416 N N   . MET F 2 17  ? -31.651 31.685  -1.069  1.00 65.86  ? 17  MET D N   1 
ATOM   10417 C CA  . MET F 2 17  ? -31.877 32.301  0.229   1.00 61.26  ? 17  MET D CA  1 
ATOM   10418 C C   . MET F 2 17  ? -30.514 32.771  0.703   1.00 61.86  ? 17  MET D C   1 
ATOM   10419 O O   . MET F 2 17  ? -29.698 31.990  1.195   1.00 61.74  ? 17  MET D O   1 
ATOM   10420 C CB  . MET F 2 17  ? -32.525 31.338  1.225   1.00 59.06  ? 17  MET D CB  1 
ATOM   10421 C CG  . MET F 2 17  ? -33.046 32.015  2.488   1.00 61.05  ? 17  MET D CG  1 
ATOM   10422 S SD  . MET F 2 17  ? -33.799 30.877  3.685   1.00 53.82  ? 17  MET D SD  1 
ATOM   10423 C CE  . MET F 2 17  ? -32.380 29.887  4.149   1.00 55.86  ? 17  MET D CE  1 
ATOM   10424 N N   . VAL F 2 18  ? -30.270 34.058  0.488   1.00 66.43  ? 18  VAL D N   1 
ATOM   10425 C CA  . VAL F 2 18  ? -29.077 34.739  0.977   1.00 64.99  ? 18  VAL D CA  1 
ATOM   10426 C C   . VAL F 2 18  ? -29.396 35.368  2.329   1.00 68.28  ? 18  VAL D C   1 
ATOM   10427 O O   . VAL F 2 18  ? -28.502 35.833  3.018   1.00 69.73  ? 18  VAL D O   1 
ATOM   10428 C CB  . VAL F 2 18  ? -28.647 35.871  0.015   1.00 61.15  ? 18  VAL D CB  1 
ATOM   10429 C CG1 . VAL F 2 18  ? -27.233 36.345  0.333   1.00 58.26  ? 18  VAL D CG1 1 
ATOM   10430 C CG2 . VAL F 2 18  ? -28.746 35.428  -1.442  1.00 47.52  ? 18  VAL D CG2 1 
ATOM   10431 N N   . ASP F 2 19  ? -30.675 35.370  2.699   1.00 79.65  ? 19  ASP D N   1 
ATOM   10432 C CA  . ASP F 2 19  ? -31.159 36.078  3.886   1.00 86.84  ? 19  ASP D CA  1 
ATOM   10433 C C   . ASP F 2 19  ? -30.560 35.566  5.209   1.00 82.75  ? 19  ASP D C   1 
ATOM   10434 O O   . ASP F 2 19  ? -29.890 36.303  5.954   1.00 86.64  ? 19  ASP D O   1 
ATOM   10435 C CB  . ASP F 2 19  ? -32.698 35.953  3.923   1.00 101.18 ? 19  ASP D CB  1 
ATOM   10436 C CG  . ASP F 2 19  ? -33.381 37.093  4.672   1.00 98.43  ? 19  ASP D CG  1 
ATOM   10437 O OD1 . ASP F 2 19  ? -32.712 37.829  5.435   1.00 100.91 ? 19  ASP D OD1 1 
ATOM   10438 O OD2 . ASP F 2 19  ? -34.611 37.236  4.496   1.00 76.81  ? 19  ASP D OD2 1 
ATOM   10439 N N   . GLY F 2 20  ? -30.800 34.289  5.478   1.00 74.20  ? 20  GLY D N   1 
ATOM   10440 C CA  . GLY F 2 20  ? -30.560 33.698  6.802   1.00 65.36  ? 20  GLY D CA  1 
ATOM   10441 C C   . GLY F 2 20  ? -30.028 32.285  6.710   1.00 55.74  ? 20  GLY D C   1 
ATOM   10442 O O   . GLY F 2 20  ? -29.413 31.926  5.711   1.00 54.16  ? 20  GLY D O   1 
ATOM   10443 N N   . TRP F 2 21  ? -30.268 31.492  7.753   1.00 50.75  ? 21  TRP D N   1 
ATOM   10444 C CA  . TRP F 2 21  ? -29.813 30.095  7.802   1.00 47.01  ? 21  TRP D CA  1 
ATOM   10445 C C   . TRP F 2 21  ? -30.942 29.141  7.530   1.00 42.35  ? 21  TRP D C   1 
ATOM   10446 O O   . TRP F 2 21  ? -30.791 28.221  6.733   1.00 43.39  ? 21  TRP D O   1 
ATOM   10447 C CB  . TRP F 2 21  ? -29.172 29.790  9.157   1.00 49.12  ? 21  TRP D CB  1 
ATOM   10448 C CG  . TRP F 2 21  ? -27.677 30.044  9.232   1.00 49.49  ? 21  TRP D CG  1 
ATOM   10449 C CD1 . TRP F 2 21  ? -26.867 30.691  8.298   1.00 48.38  ? 21  TRP D CD1 1 
ATOM   10450 C CD2 . TRP F 2 21  ? -26.767 29.695  10.337  1.00 48.53  ? 21  TRP D CD2 1 
ATOM   10451 N NE1 . TRP F 2 21  ? -25.568 30.744  8.728   1.00 47.85  ? 21  TRP D NE1 1 
ATOM   10452 C CE2 . TRP F 2 21  ? -25.438 30.168  9.940   1.00 48.95  ? 21  TRP D CE2 1 
ATOM   10453 C CE3 . TRP F 2 21  ? -26.915 29.059  11.560  1.00 47.56  ? 21  TRP D CE3 1 
ATOM   10454 C CZ2 . TRP F 2 21  ? -24.324 29.998  10.751  1.00 47.96  ? 21  TRP D CZ2 1 
ATOM   10455 C CZ3 . TRP F 2 21  ? -25.783 28.899  12.372  1.00 48.57  ? 21  TRP D CZ3 1 
ATOM   10456 C CH2 . TRP F 2 21  ? -24.519 29.351  11.973  1.00 47.33  ? 21  TRP D CH2 1 
ATOM   10457 N N   . TYR F 2 22  ? -32.074 29.341  8.202   1.00 35.86  ? 22  TYR D N   1 
ATOM   10458 C CA  . TYR F 2 22  ? -33.273 28.548  7.962   1.00 36.65  ? 22  TYR D CA  1 
ATOM   10459 C C   . TYR F 2 22  ? -34.401 29.479  7.551   1.00 40.05  ? 22  TYR D C   1 
ATOM   10460 O O   . TYR F 2 22  ? -34.462 30.623  8.004   1.00 48.55  ? 22  TYR D O   1 
ATOM   10461 C CB  . TYR F 2 22  ? -33.688 27.782  9.224   1.00 39.65  ? 22  TYR D CB  1 
ATOM   10462 C CG  . TYR F 2 22  ? -32.544 27.279  10.086  1.00 37.81  ? 22  TYR D CG  1 
ATOM   10463 C CD1 . TYR F 2 22  ? -32.389 27.722  11.397  1.00 38.51  ? 22  TYR D CD1 1 
ATOM   10464 C CD2 . TYR F 2 22  ? -31.627 26.353  9.597   1.00 38.74  ? 22  TYR D CD2 1 
ATOM   10465 C CE1 . TYR F 2 22  ? -31.354 27.261  12.194  1.00 38.53  ? 22  TYR D CE1 1 
ATOM   10466 C CE2 . TYR F 2 22  ? -30.584 25.888  10.384  1.00 38.10  ? 22  TYR D CE2 1 
ATOM   10467 C CZ  . TYR F 2 22  ? -30.456 26.347  11.682  1.00 38.33  ? 22  TYR D CZ  1 
ATOM   10468 O OH  . TYR F 2 22  ? -29.433 25.894  12.472  1.00 37.81  ? 22  TYR D OH  1 
ATOM   10469 N N   . GLY F 2 23  ? -35.310 29.000  6.709   1.00 40.53  ? 23  GLY D N   1 
ATOM   10470 C CA  . GLY F 2 23  ? -36.421 29.847  6.266   1.00 41.91  ? 23  GLY D CA  1 
ATOM   10471 C C   . GLY F 2 23  ? -37.416 29.203  5.323   1.00 39.64  ? 23  GLY D C   1 
ATOM   10472 O O   . GLY F 2 23  ? -37.453 27.982  5.178   1.00 39.67  ? 23  GLY D O   1 
ATOM   10473 N N   . TYR F 2 24  ? -38.209 30.047  4.668   1.00 40.82  ? 24  TYR D N   1 
ATOM   10474 C CA  . TYR F 2 24  ? -39.318 29.601  3.839   1.00 42.11  ? 24  TYR D CA  1 
ATOM   10475 C C   . TYR F 2 24  ? -39.166 30.077  2.405   1.00 41.98  ? 24  TYR D C   1 
ATOM   10476 O O   . TYR F 2 24  ? -38.497 31.065  2.139   1.00 35.61  ? 24  TYR D O   1 
ATOM   10477 C CB  . TYR F 2 24  ? -40.644 30.134  4.390   1.00 42.95  ? 24  TYR D CB  1 
ATOM   10478 C CG  . TYR F 2 24  ? -40.819 29.917  5.871   1.00 48.52  ? 24  TYR D CG  1 
ATOM   10479 C CD1 . TYR F 2 24  ? -40.402 30.879  6.783   1.00 49.07  ? 24  TYR D CD1 1 
ATOM   10480 C CD2 . TYR F 2 24  ? -41.395 28.747  6.364   1.00 53.90  ? 24  TYR D CD2 1 
ATOM   10481 C CE1 . TYR F 2 24  ? -40.558 30.684  8.145   1.00 46.31  ? 24  TYR D CE1 1 
ATOM   10482 C CE2 . TYR F 2 24  ? -41.557 28.545  7.725   1.00 55.94  ? 24  TYR D CE2 1 
ATOM   10483 C CZ  . TYR F 2 24  ? -41.134 29.519  8.610   1.00 52.98  ? 24  TYR D CZ  1 
ATOM   10484 O OH  . TYR F 2 24  ? -41.274 29.334  9.965   1.00 62.99  ? 24  TYR D OH  1 
ATOM   10485 N N   . HIS F 2 25  ? -39.781 29.337  1.489   1.00 45.62  ? 25  HIS D N   1 
ATOM   10486 C CA  . HIS F 2 25  ? -40.005 29.802  0.131   1.00 48.62  ? 25  HIS D CA  1 
ATOM   10487 C C   . HIS F 2 25  ? -41.454 29.590  -0.179  1.00 50.00  ? 25  HIS D C   1 
ATOM   10488 O O   . HIS F 2 25  ? -41.989 28.510  0.060   1.00 45.53  ? 25  HIS D O   1 
ATOM   10489 C CB  . HIS F 2 25  ? -39.137 29.051  -0.869  1.00 48.10  ? 25  HIS D CB  1 
ATOM   10490 C CG  . HIS F 2 25  ? -39.376 29.472  -2.300  1.00 49.94  ? 25  HIS D CG  1 
ATOM   10491 N ND1 . HIS F 2 25  ? -38.782 30.551  -2.853  1.00 51.81  ? 25  HIS D ND1 1 
ATOM   10492 C CD2 . HIS F 2 25  ? -40.207 28.936  -3.279  1.00 53.51  ? 25  HIS D CD2 1 
ATOM   10493 C CE1 . HIS F 2 25  ? -39.200 30.684  -4.128  1.00 49.42  ? 25  HIS D CE1 1 
ATOM   10494 N NE2 . HIS F 2 25  ? -40.069 29.695  -4.386  1.00 49.07  ? 25  HIS D NE2 1 
ATOM   10495 N N   . HIS F 2 26  ? -42.110 30.619  -0.707  1.00 55.76  ? 26  HIS D N   1 
ATOM   10496 C CA  . HIS F 2 26  ? -43.522 30.518  -1.071  1.00 57.13  ? 26  HIS D CA  1 
ATOM   10497 C C   . HIS F 2 26  ? -43.727 30.870  -2.508  1.00 56.19  ? 26  HIS D C   1 
ATOM   10498 O O   . HIS F 2 26  ? -42.923 31.588  -3.106  1.00 50.95  ? 26  HIS D O   1 
ATOM   10499 C CB  . HIS F 2 26  ? -44.378 31.427  -0.201  1.00 52.22  ? 26  HIS D CB  1 
ATOM   10500 C CG  . HIS F 2 26  ? -44.085 32.893  -0.389  1.00 58.57  ? 26  HIS D CG  1 
ATOM   10501 N ND1 . HIS F 2 26  ? -44.674 33.628  -1.352  1.00 60.62  ? 26  HIS D ND1 1 
ATOM   10502 C CD2 . HIS F 2 26  ? -43.223 33.750  0.292   1.00 68.67  ? 26  HIS D CD2 1 
ATOM   10503 C CE1 . HIS F 2 26  ? -44.221 34.892  -1.293  1.00 59.99  ? 26  HIS D CE1 1 
ATOM   10504 N NE2 . HIS F 2 26  ? -43.333 34.970  -0.284  1.00 65.40  ? 26  HIS D NE2 1 
ATOM   10505 N N   . SER F 2 27  ? -44.807 30.352  -3.081  1.00 53.47  ? 27  SER D N   1 
ATOM   10506 C CA  . SER F 2 27  ? -45.248 30.780  -4.399  1.00 56.92  ? 27  SER D CA  1 
ATOM   10507 C C   . SER F 2 27  ? -46.770 30.791  -4.425  1.00 56.91  ? 27  SER D C   1 
ATOM   10508 O O   . SER F 2 27  ? -47.413 29.823  -4.018  1.00 59.50  ? 27  SER D O   1 
ATOM   10509 C CB  . SER F 2 27  ? -44.687 29.873  -5.495  1.00 58.14  ? 27  SER D CB  1 
ATOM   10510 O OG  . SER F 2 27  ? -45.161 28.546  -5.365  1.00 71.70  ? 27  SER D OG  1 
ATOM   10511 N N   . ASN F 2 28  ? -47.331 31.910  -4.873  1.00 58.35  ? 28  ASN D N   1 
ATOM   10512 C CA  . ASN F 2 28  ? -48.773 32.052  -5.039  1.00 55.04  ? 28  ASN D CA  1 
ATOM   10513 C C   . ASN F 2 28  ? -49.065 32.932  -6.256  1.00 60.13  ? 28  ASN D C   1 
ATOM   10514 O O   . ASN F 2 28  ? -48.158 33.209  -7.038  1.00 61.20  ? 28  ASN D O   1 
ATOM   10515 C CB  . ASN F 2 28  ? -49.430 32.573  -3.748  1.00 50.38  ? 28  ASN D CB  1 
ATOM   10516 C CG  . ASN F 2 28  ? -48.854 33.889  -3.260  1.00 48.43  ? 28  ASN D CG  1 
ATOM   10517 O OD1 . ASN F 2 28  ? -49.095 34.286  -2.120  1.00 50.00  ? 28  ASN D OD1 1 
ATOM   10518 N ND2 . ASN F 2 28  ? -48.101 34.572  -4.109  1.00 43.67  ? 28  ASN D ND2 1 
ATOM   10519 N N   . GLU F 2 29  ? -50.318 33.344  -6.436  1.00 71.66  ? 29  GLU D N   1 
ATOM   10520 C CA  . GLU F 2 29  ? -50.704 34.164  -7.592  1.00 76.00  ? 29  GLU D CA  1 
ATOM   10521 C C   . GLU F 2 29  ? -50.005 35.525  -7.611  1.00 69.76  ? 29  GLU D C   1 
ATOM   10522 O O   . GLU F 2 29  ? -49.683 36.044  -8.683  1.00 64.10  ? 29  GLU D O   1 
ATOM   10523 C CB  . GLU F 2 29  ? -52.226 34.347  -7.642  1.00 81.89  ? 29  GLU D CB  1 
ATOM   10524 C CG  . GLU F 2 29  ? -52.967 33.105  -8.115  1.00 85.46  ? 29  GLU D CG  1 
ATOM   10525 C CD  . GLU F 2 29  ? -54.479 33.250  -8.050  1.00 88.43  ? 29  GLU D CD  1 
ATOM   10526 O OE1 . GLU F 2 29  ? -55.124 32.459  -7.326  1.00 81.44  ? 29  GLU D OE1 1 
ATOM   10527 O OE2 . GLU F 2 29  ? -55.023 34.157  -8.717  1.00 87.40  ? 29  GLU D OE2 1 
ATOM   10528 N N   . GLN F 2 30  ? -49.757 36.084  -6.429  1.00 59.62  ? 30  GLN D N   1 
ATOM   10529 C CA  . GLN F 2 30  ? -49.058 37.367  -6.304  1.00 63.24  ? 30  GLN D CA  1 
ATOM   10530 C C   . GLN F 2 30  ? -47.564 37.302  -6.653  1.00 62.62  ? 30  GLN D C   1 
ATOM   10531 O O   . GLN F 2 30  ? -46.961 38.327  -6.949  1.00 64.50  ? 30  GLN D O   1 
ATOM   10532 C CB  . GLN F 2 30  ? -49.214 37.919  -4.889  1.00 61.88  ? 30  GLN D CB  1 
ATOM   10533 C CG  . GLN F 2 30  ? -50.644 38.230  -4.493  1.00 62.31  ? 30  GLN D CG  1 
ATOM   10534 C CD  . GLN F 2 30  ? -50.744 38.624  -3.044  1.00 65.54  ? 30  GLN D CD  1 
ATOM   10535 O OE1 . GLN F 2 30  ? -50.172 39.623  -2.625  1.00 66.91  ? 30  GLN D OE1 1 
ATOM   10536 N NE2 . GLN F 2 30  ? -51.475 37.844  -2.271  1.00 66.39  ? 30  GLN D NE2 1 
ATOM   10537 N N   . GLY F 2 31  ? -46.975 36.108  -6.616  1.00 61.18  ? 31  GLY D N   1 
ATOM   10538 C CA  . GLY F 2 31  ? -45.551 35.934  -6.916  1.00 62.75  ? 31  GLY D CA  1 
ATOM   10539 C C   . GLY F 2 31  ? -44.889 34.906  -6.019  1.00 62.02  ? 31  GLY D C   1 
ATOM   10540 O O   . GLY F 2 31  ? -45.565 34.043  -5.455  1.00 62.42  ? 31  GLY D O   1 
ATOM   10541 N N   . SER F 2 32  ? -43.564 35.003  -5.892  1.00 58.34  ? 32  SER D N   1 
ATOM   10542 C CA  . SER F 2 32  ? -42.779 34.052  -5.101  1.00 54.30  ? 32  SER D CA  1 
ATOM   10543 C C   . SER F 2 32  ? -41.553 34.705  -4.472  1.00 55.00  ? 32  SER D C   1 
ATOM   10544 O O   . SER F 2 32  ? -41.088 35.742  -4.929  1.00 56.73  ? 32  SER D O   1 
ATOM   10545 C CB  . SER F 2 32  ? -42.320 32.888  -5.977  1.00 50.61  ? 32  SER D CB  1 
ATOM   10546 O OG  . SER F 2 32  ? -41.379 33.313  -6.940  1.00 46.27  ? 32  SER D OG  1 
ATOM   10547 N N   . GLY F 2 33  ? -41.025 34.085  -3.424  1.00 65.84  ? 33  GLY D N   1 
ATOM   10548 C CA  . GLY F 2 33  ? -39.804 34.574  -2.788  1.00 62.30  ? 33  GLY D CA  1 
ATOM   10549 C C   . GLY F 2 33  ? -39.389 33.810  -1.546  1.00 59.17  ? 33  GLY D C   1 
ATOM   10550 O O   . GLY F 2 33  ? -40.169 33.026  -0.988  1.00 55.23  ? 33  GLY D O   1 
ATOM   10551 N N   . TYR F 2 34  ? -38.151 34.059  -1.116  1.00 54.26  ? 34  TYR D N   1 
ATOM   10552 C CA  . TYR F 2 34  ? -37.595 33.459  0.085   1.00 43.87  ? 34  TYR D CA  1 
ATOM   10553 C C   . TYR F 2 34  ? -37.788 34.399  1.267   1.00 47.97  ? 34  TYR D C   1 
ATOM   10554 O O   . TYR F 2 34  ? -37.774 35.621  1.115   1.00 55.85  ? 34  TYR D O   1 
ATOM   10555 C CB  . TYR F 2 34  ? -36.105 33.145  -0.099  1.00 39.85  ? 34  TYR D CB  1 
ATOM   10556 C CG  . TYR F 2 34  ? -35.801 32.178  -1.223  1.00 36.32  ? 34  TYR D CG  1 
ATOM   10557 C CD1 . TYR F 2 34  ? -35.445 32.636  -2.485  1.00 36.51  ? 34  TYR D CD1 1 
ATOM   10558 C CD2 . TYR F 2 34  ? -35.857 30.804  -1.019  1.00 35.39  ? 34  TYR D CD2 1 
ATOM   10559 C CE1 . TYR F 2 34  ? -35.161 31.752  -3.516  1.00 38.64  ? 34  TYR D CE1 1 
ATOM   10560 C CE2 . TYR F 2 34  ? -35.574 29.908  -2.043  1.00 38.39  ? 34  TYR D CE2 1 
ATOM   10561 C CZ  . TYR F 2 34  ? -35.225 30.393  -3.291  1.00 39.40  ? 34  TYR D CZ  1 
ATOM   10562 O OH  . TYR F 2 34  ? -34.954 29.519  -4.318  1.00 40.37  ? 34  TYR D OH  1 
ATOM   10563 N N   . ALA F 2 35  ? -37.956 33.816  2.445   1.00 49.73  ? 35  ALA D N   1 
ATOM   10564 C CA  . ALA F 2 35  ? -38.100 34.577  3.681   1.00 57.71  ? 35  ALA D CA  1 
ATOM   10565 C C   . ALA F 2 35  ? -37.419 33.794  4.787   1.00 62.21  ? 35  ALA D C   1 
ATOM   10566 O O   . ALA F 2 35  ? -37.814 32.661  5.069   1.00 73.11  ? 35  ALA D O   1 
ATOM   10567 C CB  . ALA F 2 35  ? -39.567 34.793  4.006   1.00 62.67  ? 35  ALA D CB  1 
ATOM   10568 N N   . ALA F 2 36  ? -36.392 34.388  5.397   1.00 58.43  ? 36  ALA D N   1 
ATOM   10569 C CA  . ALA F 2 36  ? -35.650 33.720  6.457   1.00 61.70  ? 36  ALA D CA  1 
ATOM   10570 C C   . ALA F 2 36  ? -36.425 33.820  7.762   1.00 60.36  ? 36  ALA D C   1 
ATOM   10571 O O   . ALA F 2 36  ? -37.037 34.853  8.044   1.00 57.93  ? 36  ALA D O   1 
ATOM   10572 C CB  . ALA F 2 36  ? -34.273 34.348  6.620   1.00 63.00  ? 36  ALA D CB  1 
ATOM   10573 N N   . ASP F 2 37  ? -36.406 32.743  8.545   1.00 59.04  ? 37  ASP D N   1 
ATOM   10574 C CA  . ASP F 2 37  ? -36.916 32.793  9.907   1.00 66.23  ? 37  ASP D CA  1 
ATOM   10575 C C   . ASP F 2 37  ? -35.812 33.379  10.778  1.00 64.17  ? 37  ASP D C   1 
ATOM   10576 O O   . ASP F 2 37  ? -34.807 32.714  11.043  1.00 61.12  ? 37  ASP D O   1 
ATOM   10577 C CB  . ASP F 2 37  ? -37.308 31.408  10.414  1.00 70.15  ? 37  ASP D CB  1 
ATOM   10578 C CG  . ASP F 2 37  ? -37.968 31.464  11.767  1.00 73.86  ? 37  ASP D CG  1 
ATOM   10579 O OD1 . ASP F 2 37  ? -39.140 31.889  11.830  1.00 85.92  ? 37  ASP D OD1 1 
ATOM   10580 O OD2 . ASP F 2 37  ? -37.320 31.106  12.766  1.00 72.99  ? 37  ASP D OD2 1 
ATOM   10581 N N   . LYS F 2 38  ? -35.998 34.623  11.212  1.00 69.81  ? 38  LYS D N   1 
ATOM   10582 C CA  . LYS F 2 38  ? -34.931 35.370  11.879  1.00 72.48  ? 38  LYS D CA  1 
ATOM   10583 C C   . LYS F 2 38  ? -34.680 34.890  13.301  1.00 68.67  ? 38  LYS D C   1 
ATOM   10584 O O   . LYS F 2 38  ? -33.548 34.945  13.774  1.00 70.77  ? 38  LYS D O   1 
ATOM   10585 C CB  . LYS F 2 38  ? -35.240 36.871  11.883  1.00 76.61  ? 38  LYS D CB  1 
ATOM   10586 C CG  . LYS F 2 38  ? -35.328 37.472  10.481  1.00 86.02  ? 38  LYS D CG  1 
ATOM   10587 C CD  . LYS F 2 38  ? -35.104 38.981  10.429  1.00 89.44  ? 38  LYS D CD  1 
ATOM   10588 C CE  . LYS F 2 38  ? -35.196 39.484  8.995   1.00 94.35  ? 38  LYS D CE  1 
ATOM   10589 N NZ  . LYS F 2 38  ? -34.917 40.945  8.888   1.00 95.76  ? 38  LYS D NZ  1 
ATOM   10590 N N   . GLU F 2 39  ? -35.726 34.420  13.977  1.00 74.47  ? 39  GLU D N   1 
ATOM   10591 C CA  . GLU F 2 39  ? -35.590 33.963  15.360  1.00 76.94  ? 39  GLU D CA  1 
ATOM   10592 C C   . GLU F 2 39  ? -34.690 32.734  15.456  1.00 69.60  ? 39  GLU D C   1 
ATOM   10593 O O   . GLU F 2 39  ? -33.670 32.775  16.135  1.00 67.38  ? 39  GLU D O   1 
ATOM   10594 C CB  . GLU F 2 39  ? -36.948 33.690  16.007  1.00 81.64  ? 39  GLU D CB  1 
ATOM   10595 C CG  . GLU F 2 39  ? -37.022 34.178  17.448  1.00 91.38  ? 39  GLU D CG  1 
ATOM   10596 C CD  . GLU F 2 39  ? -38.190 33.596  18.232  1.00 103.41 ? 39  GLU D CD  1 
ATOM   10597 O OE1 . GLU F 2 39  ? -38.138 32.399  18.601  1.00 108.45 ? 39  GLU D OE1 1 
ATOM   10598 O OE2 . GLU F 2 39  ? -39.160 34.342  18.499  1.00 110.04 ? 39  GLU D OE2 1 
ATOM   10599 N N   . SER F 2 40  ? -35.055 31.656  14.764  1.00 61.40  ? 40  SER D N   1 
ATOM   10600 C CA  . SER F 2 40  ? -34.288 30.411  14.824  1.00 58.97  ? 40  SER D CA  1 
ATOM   10601 C C   . SER F 2 40  ? -32.886 30.551  14.211  1.00 52.84  ? 40  SER D C   1 
ATOM   10602 O O   . SER F 2 40  ? -31.954 29.888  14.662  1.00 52.20  ? 40  SER D O   1 
ATOM   10603 C CB  . SER F 2 40  ? -35.051 29.254  14.162  1.00 53.02  ? 40  SER D CB  1 
ATOM   10604 O OG  . SER F 2 40  ? -35.202 29.464  12.775  1.00 52.37  ? 40  SER D OG  1 
ATOM   10605 N N   . THR F 2 41  ? -32.744 31.406  13.199  1.00 45.29  ? 41  THR D N   1 
ATOM   10606 C CA  . THR F 2 41  ? -31.433 31.695  12.608  1.00 47.42  ? 41  THR D CA  1 
ATOM   10607 C C   . THR F 2 41  ? -30.499 32.337  13.633  1.00 49.18  ? 41  THR D C   1 
ATOM   10608 O O   . THR F 2 41  ? -29.362 31.902  13.795  1.00 54.82  ? 41  THR D O   1 
ATOM   10609 C CB  . THR F 2 41  ? -31.531 32.630  11.378  1.00 46.31  ? 41  THR D CB  1 
ATOM   10610 O OG1 . THR F 2 41  ? -32.169 31.947  10.297  1.00 43.40  ? 41  THR D OG1 1 
ATOM   10611 C CG2 . THR F 2 41  ? -30.147 33.073  10.918  1.00 43.89  ? 41  THR D CG2 1 
ATOM   10612 N N   . GLN F 2 42  ? -30.986 33.361  14.330  1.00 54.94  ? 42  GLN D N   1 
ATOM   10613 C CA  . GLN F 2 42  ? -30.175 34.070  15.328  1.00 56.62  ? 42  GLN D CA  1 
ATOM   10614 C C   . GLN F 2 42  ? -29.809 33.181  16.505  1.00 52.24  ? 42  GLN D C   1 
ATOM   10615 O O   . GLN F 2 42  ? -28.703 33.274  17.017  1.00 54.53  ? 42  GLN D O   1 
ATOM   10616 C CB  . GLN F 2 42  ? -30.870 35.342  15.841  1.00 57.74  ? 42  GLN D CB  1 
ATOM   10617 C CG  . GLN F 2 42  ? -30.441 36.620  15.131  1.00 62.01  ? 42  GLN D CG  1 
ATOM   10618 C CD  . GLN F 2 42  ? -28.968 36.940  15.311  1.00 61.28  ? 42  GLN D CD  1 
ATOM   10619 O OE1 . GLN F 2 42  ? -28.384 36.667  16.359  1.00 64.25  ? 42  GLN D OE1 1 
ATOM   10620 N NE2 . GLN F 2 42  ? -28.362 37.527  14.287  1.00 67.46  ? 42  GLN D NE2 1 
ATOM   10621 N N   . LYS F 2 43  ? -30.734 32.327  16.931  1.00 54.33  ? 43  LYS D N   1 
ATOM   10622 C CA  . LYS F 2 43  ? -30.454 31.389  18.014  1.00 56.38  ? 43  LYS D CA  1 
ATOM   10623 C C   . LYS F 2 43  ? -29.352 30.421  17.591  1.00 51.04  ? 43  LYS D C   1 
ATOM   10624 O O   . LYS F 2 43  ? -28.466 30.110  18.381  1.00 54.10  ? 43  LYS D O   1 
ATOM   10625 C CB  . LYS F 2 43  ? -31.700 30.617  18.475  1.00 64.62  ? 43  LYS D CB  1 
ATOM   10626 C CG  . LYS F 2 43  ? -31.955 30.769  19.973  1.00 79.54  ? 43  LYS D CG  1 
ATOM   10627 C CD  . LYS F 2 43  ? -33.445 30.927  20.284  1.00 89.27  ? 43  LYS D CD  1 
ATOM   10628 C CE  . LYS F 2 43  ? -33.824 32.381  20.510  1.00 90.49  ? 43  LYS D CE  1 
ATOM   10629 N NZ  . LYS F 2 43  ? -35.298 32.590  20.521  1.00 92.30  ? 43  LYS D NZ  1 
ATOM   10630 N N   . ALA F 2 44  ? -29.403 29.964  16.341  1.00 43.91  ? 44  ALA D N   1 
ATOM   10631 C CA  . ALA F 2 44  ? -28.415 29.021  15.821  1.00 42.44  ? 44  ALA D CA  1 
ATOM   10632 C C   . ALA F 2 44  ? -27.036 29.665  15.681  1.00 43.19  ? 44  ALA D C   1 
ATOM   10633 O O   . ALA F 2 44  ? -26.030 29.051  16.028  1.00 44.78  ? 44  ALA D O   1 
ATOM   10634 C CB  . ALA F 2 44  ? -28.871 28.455  14.489  1.00 39.55  ? 44  ALA D CB  1 
ATOM   10635 N N   . ILE F 2 45  ? -26.996 30.899  15.181  1.00 44.60  ? 45  ILE D N   1 
ATOM   10636 C CA  . ILE F 2 45  ? -25.745 31.653  15.081  1.00 49.77  ? 45  ILE D CA  1 
ATOM   10637 C C   . ILE F 2 45  ? -25.150 31.928  16.467  1.00 46.21  ? 45  ILE D C   1 
ATOM   10638 O O   . ILE F 2 45  ? -23.944 31.793  16.667  1.00 46.87  ? 45  ILE D O   1 
ATOM   10639 C CB  . ILE F 2 45  ? -25.941 32.986  14.320  1.00 50.76  ? 45  ILE D CB  1 
ATOM   10640 C CG1 . ILE F 2 45  ? -26.207 32.710  12.839  1.00 55.47  ? 45  ILE D CG1 1 
ATOM   10641 C CG2 . ILE F 2 45  ? -24.720 33.884  14.455  1.00 41.58  ? 45  ILE D CG2 1 
ATOM   10642 C CD1 . ILE F 2 45  ? -26.600 33.941  12.054  1.00 59.22  ? 45  ILE D CD1 1 
ATOM   10643 N N   . ASP F 2 46  ? -25.999 32.301  17.420  1.00 48.33  ? 46  ASP D N   1 
ATOM   10644 C CA  . ASP F 2 46  ? -25.563 32.543  18.801  1.00 51.31  ? 46  ASP D CA  1 
ATOM   10645 C C   . ASP F 2 46  ? -25.026 31.282  19.477  1.00 44.61  ? 46  ASP D C   1 
ATOM   10646 O O   . ASP F 2 46  ? -24.006 31.333  20.150  1.00 43.18  ? 46  ASP D O   1 
ATOM   10647 C CB  . ASP F 2 46  ? -26.705 33.127  19.638  1.00 57.00  ? 46  ASP D CB  1 
ATOM   10648 C CG  . ASP F 2 46  ? -27.016 34.572  19.277  1.00 66.30  ? 46  ASP D CG  1 
ATOM   10649 O OD1 . ASP F 2 46  ? -26.263 35.174  18.477  1.00 64.21  ? 46  ASP D OD1 1 
ATOM   10650 O OD2 . ASP F 2 46  ? -28.017 35.107  19.800  1.00 74.51  ? 46  ASP D OD2 1 
ATOM   10651 N N   . GLY F 2 47  ? -25.703 30.156  19.279  1.00 39.60  ? 47  GLY D N   1 
ATOM   10652 C CA  . GLY F 2 47  ? -25.257 28.884  19.830  1.00 38.49  ? 47  GLY D CA  1 
ATOM   10653 C C   . GLY F 2 47  ? -23.923 28.434  19.256  1.00 42.07  ? 47  GLY D C   1 
ATOM   10654 O O   . GLY F 2 47  ? -23.015 28.065  20.000  1.00 37.22  ? 47  GLY D O   1 
ATOM   10655 N N   . VAL F 2 48  ? -23.804 28.471  17.929  1.00 40.40  ? 48  VAL D N   1 
ATOM   10656 C CA  . VAL F 2 48  ? -22.582 28.054  17.247  1.00 37.64  ? 48  VAL D CA  1 
ATOM   10657 C C   . VAL F 2 48  ? -21.399 28.948  17.612  1.00 39.90  ? 48  VAL D C   1 
ATOM   10658 O O   . VAL F 2 48  ? -20.294 28.457  17.817  1.00 40.98  ? 48  VAL D O   1 
ATOM   10659 C CB  . VAL F 2 48  ? -22.759 28.019  15.711  1.00 38.92  ? 48  VAL D CB  1 
ATOM   10660 C CG1 . VAL F 2 48  ? -21.418 28.129  15.000  1.00 38.04  ? 48  VAL D CG1 1 
ATOM   10661 C CG2 . VAL F 2 48  ? -23.473 26.746  15.290  1.00 39.79  ? 48  VAL D CG2 1 
ATOM   10662 N N   . THR F 2 49  ? -21.633 30.252  17.695  1.00 38.16  ? 49  THR D N   1 
ATOM   10663 C CA  . THR F 2 49  ? -20.593 31.189  18.117  1.00 42.08  ? 49  THR D CA  1 
ATOM   10664 C C   . THR F 2 49  ? -20.164 30.910  19.558  1.00 42.83  ? 49  THR D C   1 
ATOM   10665 O O   . THR F 2 49  ? -18.980 30.986  19.885  1.00 44.71  ? 49  THR D O   1 
ATOM   10666 C CB  . THR F 2 49  ? -21.062 32.653  17.987  1.00 42.83  ? 49  THR D CB  1 
ATOM   10667 O OG1 . THR F 2 49  ? -21.425 32.912  16.624  1.00 49.91  ? 49  THR D OG1 1 
ATOM   10668 C CG2 . THR F 2 49  ? -19.965 33.628  18.411  1.00 37.36  ? 49  THR D CG2 1 
ATOM   10669 N N   . ASN F 2 50  ? -21.135 30.589  20.409  1.00 42.13  ? 50  ASN D N   1 
ATOM   10670 C CA  . ASN F 2 50  ? -20.863 30.242  21.799  1.00 40.33  ? 50  ASN D CA  1 
ATOM   10671 C C   . ASN F 2 50  ? -20.043 28.951  21.896  1.00 39.75  ? 50  ASN D C   1 
ATOM   10672 O O   . ASN F 2 50  ? -19.134 28.857  22.716  1.00 36.44  ? 50  ASN D O   1 
ATOM   10673 C CB  . ASN F 2 50  ? -22.169 30.092  22.576  1.00 44.78  ? 50  ASN D CB  1 
ATOM   10674 C CG  . ASN F 2 50  ? -22.157 30.852  23.874  1.00 52.55  ? 50  ASN D CG  1 
ATOM   10675 O OD1 . ASN F 2 50  ? -22.045 30.270  24.946  1.00 55.45  ? 50  ASN D OD1 1 
ATOM   10676 N ND2 . ASN F 2 50  ? -22.268 32.171  23.780  1.00 54.86  ? 50  ASN D ND2 1 
ATOM   10677 N N   . LYS F 2 51  ? -20.352 27.977  21.039  1.00 36.70  ? 51  LYS D N   1 
ATOM   10678 C CA  . LYS F 2 51  ? -19.598 26.724  20.975  1.00 35.78  ? 51  LYS D CA  1 
ATOM   10679 C C   . LYS F 2 51  ? -18.136 26.982  20.651  1.00 36.85  ? 51  LYS D C   1 
ATOM   10680 O O   . LYS F 2 51  ? -17.256 26.502  21.349  1.00 40.89  ? 51  LYS D O   1 
ATOM   10681 C CB  . LYS F 2 51  ? -20.195 25.785  19.922  1.00 38.34  ? 51  LYS D CB  1 
ATOM   10682 C CG  . LYS F 2 51  ? -19.390 24.514  19.684  1.00 41.06  ? 51  LYS D CG  1 
ATOM   10683 C CD  . LYS F 2 51  ? -20.022 23.606  18.635  1.00 41.35  ? 51  LYS D CD  1 
ATOM   10684 C CE  . LYS F 2 51  ? -21.323 22.991  19.123  1.00 44.56  ? 51  LYS D CE  1 
ATOM   10685 N NZ  . LYS F 2 51  ? -21.632 21.729  18.395  1.00 43.71  ? 51  LYS D NZ  1 
ATOM   10686 N N   . VAL F 2 52  ? -17.887 27.740  19.588  1.00 35.14  ? 52  VAL D N   1 
ATOM   10687 C CA  . VAL F 2 52  ? -16.526 28.072  19.178  1.00 35.77  ? 52  VAL D CA  1 
ATOM   10688 C C   . VAL F 2 52  ? -15.792 28.847  20.276  1.00 38.16  ? 52  VAL D C   1 
ATOM   10689 O O   . VAL F 2 52  ? -14.625 28.580  20.553  1.00 42.65  ? 52  VAL D O   1 
ATOM   10690 C CB  . VAL F 2 52  ? -16.512 28.894  17.871  1.00 33.64  ? 52  VAL D CB  1 
ATOM   10691 C CG1 . VAL F 2 52  ? -15.090 29.278  17.490  1.00 31.05  ? 52  VAL D CG1 1 
ATOM   10692 C CG2 . VAL F 2 52  ? -17.168 28.112  16.745  1.00 30.43  ? 52  VAL D CG2 1 
ATOM   10693 N N   . ASN F 2 53  ? -16.483 29.787  20.912  1.00 40.53  ? 53  ASN D N   1 
ATOM   10694 C CA  . ASN F 2 53  ? -15.880 30.592  21.972  1.00 39.44  ? 53  ASN D CA  1 
ATOM   10695 C C   . ASN F 2 53  ? -15.536 29.793  23.226  1.00 40.93  ? 53  ASN D C   1 
ATOM   10696 O O   . ASN F 2 53  ? -14.468 29.989  23.794  1.00 44.22  ? 53  ASN D O   1 
ATOM   10697 C CB  . ASN F 2 53  ? -16.770 31.790  22.332  1.00 41.18  ? 53  ASN D CB  1 
ATOM   10698 C CG  . ASN F 2 53  ? -16.689 32.908  21.304  1.00 46.56  ? 53  ASN D CG  1 
ATOM   10699 O OD1 . ASN F 2 53  ? -15.661 33.087  20.650  1.00 45.98  ? 53  ASN D OD1 1 
ATOM   10700 N ND2 . ASN F 2 53  ? -17.770 33.670  21.163  1.00 44.95  ? 53  ASN D ND2 1 
ATOM   10701 N N   . SER F 2 54  ? -16.422 28.900  23.665  1.00 43.11  ? 54  SER D N   1 
ATOM   10702 C CA  . SER F 2 54  ? -16.126 28.085  24.853  1.00 41.52  ? 54  SER D CA  1 
ATOM   10703 C C   . SER F 2 54  ? -14.921 27.182  24.595  1.00 38.32  ? 54  SER D C   1 
ATOM   10704 O O   . SER F 2 54  ? -14.059 27.044  25.459  1.00 36.54  ? 54  SER D O   1 
ATOM   10705 C CB  . SER F 2 54  ? -17.340 27.270  25.348  1.00 43.96  ? 54  SER D CB  1 
ATOM   10706 O OG  . SER F 2 54  ? -18.464 27.418  24.501  1.00 50.89  ? 54  SER D OG  1 
ATOM   10707 N N   . ILE F 2 55  ? -14.850 26.601  23.397  1.00 36.70  ? 55  ILE D N   1 
ATOM   10708 C CA  . ILE F 2 55  ? -13.726 25.738  23.013  1.00 34.71  ? 55  ILE D CA  1 
ATOM   10709 C C   . ILE F 2 55  ? -12.390 26.487  23.026  1.00 34.32  ? 55  ILE D C   1 
ATOM   10710 O O   . ILE F 2 55  ? -11.346 25.894  23.276  1.00 33.54  ? 55  ILE D O   1 
ATOM   10711 C CB  . ILE F 2 55  ? -13.953 25.093  21.628  1.00 33.42  ? 55  ILE D CB  1 
ATOM   10712 C CG1 . ILE F 2 55  ? -15.061 24.034  21.717  1.00 34.90  ? 55  ILE D CG1 1 
ATOM   10713 C CG2 . ILE F 2 55  ? -12.672 24.462  21.093  1.00 31.51  ? 55  ILE D CG2 1 
ATOM   10714 C CD1 . ILE F 2 55  ? -15.513 23.486  20.375  1.00 33.57  ? 55  ILE D CD1 1 
ATOM   10715 N N   . ILE F 2 56  ? -12.434 27.788  22.759  1.00 40.61  ? 56  ILE D N   1 
ATOM   10716 C CA  . ILE F 2 56  ? -11.251 28.648  22.824  1.00 38.90  ? 56  ILE D CA  1 
ATOM   10717 C C   . ILE F 2 56  ? -11.017 29.158  24.247  1.00 40.49  ? 56  ILE D C   1 
ATOM   10718 O O   . ILE F 2 56  ? -9.903  29.071  24.761  1.00 44.78  ? 56  ILE D O   1 
ATOM   10719 C CB  . ILE F 2 56  ? -11.398 29.858  21.874  1.00 40.03  ? 56  ILE D CB  1 
ATOM   10720 C CG1 . ILE F 2 56  ? -11.410 29.397  20.418  1.00 41.59  ? 56  ILE D CG1 1 
ATOM   10721 C CG2 . ILE F 2 56  ? -10.259 30.853  22.060  1.00 36.58  ? 56  ILE D CG2 1 
ATOM   10722 C CD1 . ILE F 2 56  ? -11.783 30.492  19.437  1.00 39.21  ? 56  ILE D CD1 1 
ATOM   10723 N N   . ASP F 2 57  ? -12.071 29.672  24.880  1.00 39.70  ? 57  ASP D N   1 
ATOM   10724 C CA  . ASP F 2 57  ? -11.954 30.366  26.167  1.00 47.62  ? 57  ASP D CA  1 
ATOM   10725 C C   . ASP F 2 57  ? -11.611 29.464  27.354  1.00 47.11  ? 57  ASP D C   1 
ATOM   10726 O O   . ASP F 2 57  ? -10.948 29.909  28.286  1.00 50.62  ? 57  ASP D O   1 
ATOM   10727 C CB  . ASP F 2 57  ? -13.240 31.152  26.482  1.00 62.13  ? 57  ASP D CB  1 
ATOM   10728 C CG  . ASP F 2 57  ? -13.486 32.313  25.512  1.00 73.75  ? 57  ASP D CG  1 
ATOM   10729 O OD1 . ASP F 2 57  ? -12.597 32.619  24.684  1.00 80.12  ? 57  ASP D OD1 1 
ATOM   10730 O OD2 . ASP F 2 57  ? -14.580 32.918  25.575  1.00 80.48  ? 57  ASP D OD2 1 
ATOM   10731 N N   . LYS F 2 58  ? -12.057 28.210  27.329  1.00 46.75  ? 58  LYS D N   1 
ATOM   10732 C CA  . LYS F 2 58  ? -11.809 27.292  28.448  1.00 45.06  ? 58  LYS D CA  1 
ATOM   10733 C C   . LYS F 2 58  ? -10.356 26.831  28.562  1.00 44.83  ? 58  LYS D C   1 
ATOM   10734 O O   . LYS F 2 58  ? -9.972  26.247  29.580  1.00 42.97  ? 58  LYS D O   1 
ATOM   10735 C CB  . LYS F 2 58  ? -12.729 26.072  28.365  1.00 47.11  ? 58  LYS D CB  1 
ATOM   10736 C CG  . LYS F 2 58  ? -14.200 26.389  28.575  1.00 50.50  ? 58  LYS D CG  1 
ATOM   10737 C CD  . LYS F 2 58  ? -14.470 26.967  29.955  1.00 51.53  ? 58  LYS D CD  1 
ATOM   10738 C CE  . LYS F 2 58  ? -15.960 27.108  30.203  1.00 52.00  ? 58  LYS D CE  1 
ATOM   10739 N NZ  . LYS F 2 58  ? -16.230 27.640  31.565  1.00 45.86  ? 58  LYS D NZ  1 
ATOM   10740 N N   . MET F 2 59  ? -9.554  27.071  27.527  1.00 42.55  ? 59  MET D N   1 
ATOM   10741 C CA  . MET F 2 59  ? -8.137  26.744  27.595  1.00 45.56  ? 59  MET D CA  1 
ATOM   10742 C C   . MET F 2 59  ? -7.480  27.718  28.551  1.00 46.42  ? 59  MET D C   1 
ATOM   10743 O O   . MET F 2 59  ? -7.719  28.925  28.477  1.00 52.14  ? 59  MET D O   1 
ATOM   10744 C CB  . MET F 2 59  ? -7.480  26.837  26.215  1.00 45.24  ? 59  MET D CB  1 
ATOM   10745 C CG  . MET F 2 59  ? -6.009  26.443  26.184  1.00 40.56  ? 59  MET D CG  1 
ATOM   10746 S SD  . MET F 2 59  ? -5.679  24.725  26.662  1.00 42.94  ? 59  MET D SD  1 
ATOM   10747 C CE  . MET F 2 59  ? -6.360  23.833  25.267  1.00 40.41  ? 59  MET D CE  1 
ATOM   10748 N N   . ASN F 2 60  ? -6.664  27.189  29.454  1.00 51.75  ? 60  ASN D N   1 
ATOM   10749 C CA  . ASN F 2 60  ? -5.944  28.016  30.410  1.00 57.16  ? 60  ASN D CA  1 
ATOM   10750 C C   . ASN F 2 60  ? -4.463  27.714  30.267  1.00 57.98  ? 60  ASN D C   1 
ATOM   10751 O O   . ASN F 2 60  ? -4.016  26.615  30.581  1.00 70.43  ? 60  ASN D O   1 
ATOM   10752 C CB  . ASN F 2 60  ? -6.473  27.800  31.842  1.00 60.47  ? 60  ASN D CB  1 
ATOM   10753 C CG  . ASN F 2 60  ? -5.371  27.640  32.865  1.00 62.34  ? 60  ASN D CG  1 
ATOM   10754 O OD1 . ASN F 2 60  ? -4.841  28.619  33.366  1.00 57.71  ? 60  ASN D OD1 1 
ATOM   10755 N ND2 . ASN F 2 60  ? -5.026  26.398  33.184  1.00 66.07  ? 60  ASN D ND2 1 
ATOM   10756 N N   . THR F 2 61  ? -3.721  28.685  29.742  1.00 59.53  ? 61  THR D N   1 
ATOM   10757 C CA  . THR F 2 61  ? -2.296  28.526  29.487  1.00 65.19  ? 61  THR D CA  1 
ATOM   10758 C C   . THR F 2 61  ? -1.468  29.401  30.426  1.00 56.00  ? 61  THR D C   1 
ATOM   10759 O O   . THR F 2 61  ? -1.771  30.575  30.610  1.00 54.50  ? 61  THR D O   1 
ATOM   10760 C CB  . THR F 2 61  ? -1.964  28.916  28.035  1.00 68.25  ? 61  THR D CB  1 
ATOM   10761 O OG1 . THR F 2 61  ? -2.354  30.274  27.808  1.00 64.40  ? 61  THR D OG1 1 
ATOM   10762 C CG2 . THR F 2 61  ? -2.717  28.028  27.043  1.00 63.83  ? 61  THR D CG2 1 
ATOM   10763 N N   . GLN F 2 62  ? -0.432  28.814  31.020  1.00 57.14  ? 62  GLN D N   1 
ATOM   10764 C CA  . GLN F 2 62  ? 0.527   29.544  31.853  1.00 57.69  ? 62  GLN D CA  1 
ATOM   10765 C C   . GLN F 2 62  ? 1.858   29.751  31.140  1.00 50.49  ? 62  GLN D C   1 
ATOM   10766 O O   . GLN F 2 62  ? 2.085   29.220  30.047  1.00 55.13  ? 62  GLN D O   1 
ATOM   10767 C CB  . GLN F 2 62  ? 0.752   28.796  33.171  1.00 69.22  ? 62  GLN D CB  1 
ATOM   10768 C CG  . GLN F 2 62  ? -0.393  28.937  34.168  1.00 83.75  ? 62  GLN D CG  1 
ATOM   10769 C CD  . GLN F 2 62  ? -0.386  27.846  35.222  1.00 80.25  ? 62  GLN D CD  1 
ATOM   10770 O OE1 . GLN F 2 62  ? -0.102  26.681  34.924  1.00 58.35  ? 62  GLN D OE1 1 
ATOM   10771 N NE2 . GLN F 2 62  ? -0.706  28.213  36.459  1.00 86.28  ? 62  GLN D NE2 1 
ATOM   10772 N N   . PHE F 2 63  ? 2.733   30.533  31.772  1.00 50.66  ? 63  PHE D N   1 
ATOM   10773 C CA  . PHE F 2 63  ? 4.063   30.802  31.246  1.00 50.66  ? 63  PHE D CA  1 
ATOM   10774 C C   . PHE F 2 63  ? 4.944   29.576  31.410  1.00 49.36  ? 63  PHE D C   1 
ATOM   10775 O O   . PHE F 2 63  ? 4.821   28.866  32.399  1.00 52.87  ? 63  PHE D O   1 
ATOM   10776 C CB  . PHE F 2 63  ? 4.691   31.993  31.983  1.00 53.75  ? 63  PHE D CB  1 
ATOM   10777 C CG  . PHE F 2 63  ? 6.068   32.346  31.504  1.00 59.17  ? 63  PHE D CG  1 
ATOM   10778 C CD1 . PHE F 2 63  ? 6.241   33.234  30.452  1.00 65.89  ? 63  PHE D CD1 1 
ATOM   10779 C CD2 . PHE F 2 63  ? 7.190   31.788  32.099  1.00 58.73  ? 63  PHE D CD2 1 
ATOM   10780 C CE1 . PHE F 2 63  ? 7.509   33.559  29.999  1.00 73.63  ? 63  PHE D CE1 1 
ATOM   10781 C CE2 . PHE F 2 63  ? 8.460   32.108  31.650  1.00 68.18  ? 63  PHE D CE2 1 
ATOM   10782 C CZ  . PHE F 2 63  ? 8.620   32.993  30.597  1.00 72.36  ? 63  PHE D CZ  1 
ATOM   10783 N N   . GLU F 2 64  ? 5.815   29.326  30.434  1.00 57.57  ? 64  GLU D N   1 
ATOM   10784 C CA  . GLU F 2 64  ? 6.875   28.328  30.586  1.00 57.11  ? 64  GLU D CA  1 
ATOM   10785 C C   . GLU F 2 64  ? 7.996   28.482  29.588  1.00 54.86  ? 64  GLU D C   1 
ATOM   10786 O O   . GLU F 2 64  ? 7.814   29.046  28.515  1.00 51.83  ? 64  GLU D O   1 
ATOM   10787 C CB  . GLU F 2 64  ? 6.313   26.916  30.491  1.00 64.10  ? 64  GLU D CB  1 
ATOM   10788 C CG  . GLU F 2 64  ? 6.114   26.264  31.851  1.00 74.32  ? 64  GLU D CG  1 
ATOM   10789 C CD  . GLU F 2 64  ? 4.740   25.658  32.007  1.00 69.15  ? 64  GLU D CD  1 
ATOM   10790 O OE1 . GLU F 2 64  ? 4.241   25.053  31.035  1.00 83.20  ? 64  GLU D OE1 1 
ATOM   10791 O OE2 . GLU F 2 64  ? 4.161   25.801  33.102  1.00 49.78  ? 64  GLU D OE2 1 
ATOM   10792 N N   . ALA F 2 65  ? 9.152   27.948  29.965  1.00 55.76  ? 65  ALA D N   1 
ATOM   10793 C CA  . ALA F 2 65  ? 10.348  28.039  29.168  1.00 59.91  ? 65  ALA D CA  1 
ATOM   10794 C C   . ALA F 2 65  ? 10.766  26.633  28.790  1.00 55.71  ? 65  ALA D C   1 
ATOM   10795 O O   . ALA F 2 65  ? 11.627  26.035  29.437  1.00 71.27  ? 65  ALA D O   1 
ATOM   10796 C CB  . ALA F 2 65  ? 11.441  28.735  29.961  1.00 65.30  ? 65  ALA D CB  1 
ATOM   10797 N N   . VAL F 2 66  ? 10.139  26.100  27.748  1.00 51.98  ? 66  VAL D N   1 
ATOM   10798 C CA  . VAL F 2 66  ? 10.508  24.790  27.240  1.00 49.05  ? 66  VAL D CA  1 
ATOM   10799 C C   . VAL F 2 66  ? 11.812  24.927  26.464  1.00 48.77  ? 66  VAL D C   1 
ATOM   10800 O O   . VAL F 2 66  ? 11.832  25.396  25.329  1.00 52.21  ? 66  VAL D O   1 
ATOM   10801 C CB  . VAL F 2 66  ? 9.415   24.174  26.347  1.00 45.85  ? 66  VAL D CB  1 
ATOM   10802 C CG1 . VAL F 2 66  ? 9.851   22.804  25.860  1.00 44.71  ? 66  VAL D CG1 1 
ATOM   10803 C CG2 . VAL F 2 66  ? 8.101   24.074  27.106  1.00 43.61  ? 66  VAL D CG2 1 
ATOM   10804 N N   . GLY F 2 67  ? 12.902  24.547  27.119  1.00 52.71  ? 67  GLY D N   1 
ATOM   10805 C CA  . GLY F 2 67  ? 14.217  24.478  26.496  1.00 59.06  ? 67  GLY D CA  1 
ATOM   10806 C C   . GLY F 2 67  ? 15.047  23.393  27.162  1.00 60.30  ? 67  GLY D C   1 
ATOM   10807 O O   . GLY F 2 67  ? 15.020  23.248  28.382  1.00 82.98  ? 67  GLY D O   1 
ATOM   10808 N N   . ARG F 2 68  ? 15.774  22.626  26.359  1.00 57.55  ? 68  ARG D N   1 
ATOM   10809 C CA  . ARG F 2 68  ? 16.568  21.507  26.855  1.00 64.17  ? 68  ARG D CA  1 
ATOM   10810 C C   . ARG F 2 68  ? 17.914  21.954  27.424  1.00 57.28  ? 68  ARG D C   1 
ATOM   10811 O O   . ARG F 2 68  ? 18.786  22.396  26.687  1.00 59.68  ? 68  ARG D O   1 
ATOM   10812 C CB  . ARG F 2 68  ? 16.779  20.496  25.724  1.00 68.71  ? 68  ARG D CB  1 
ATOM   10813 C CG  . ARG F 2 68  ? 15.521  19.722  25.369  1.00 80.83  ? 68  ARG D CG  1 
ATOM   10814 C CD  . ARG F 2 68  ? 15.827  18.578  24.424  1.00 88.89  ? 68  ARG D CD  1 
ATOM   10815 N NE  . ARG F 2 68  ? 14.680  17.690  24.233  1.00 103.68 ? 68  ARG D NE  1 
ATOM   10816 C CZ  . ARG F 2 68  ? 13.585  17.990  23.536  1.00 102.32 ? 68  ARG D CZ  1 
ATOM   10817 N NH1 . ARG F 2 68  ? 13.449  19.172  22.954  1.00 101.15 ? 68  ARG D NH1 1 
ATOM   10818 N NH2 . ARG F 2 68  ? 12.608  17.098  23.428  1.00 109.28 ? 68  ARG D NH2 1 
ATOM   10819 N N   . GLU F 2 69  ? 18.077  21.815  28.738  1.00 57.41  ? 69  GLU D N   1 
ATOM   10820 C CA  . GLU F 2 69  ? 19.278  22.286  29.428  1.00 53.71  ? 69  GLU D CA  1 
ATOM   10821 C C   . GLU F 2 69  ? 19.931  21.207  30.311  1.00 44.88  ? 69  GLU D C   1 
ATOM   10822 O O   . GLU F 2 69  ? 20.425  21.489  31.396  1.00 44.28  ? 69  GLU D O   1 
ATOM   10823 C CB  . GLU F 2 69  ? 18.990  23.589  30.211  1.00 61.73  ? 69  GLU D CB  1 
ATOM   10824 C CG  . GLU F 2 69  ? 17.654  23.672  30.945  1.00 69.70  ? 69  GLU D CG  1 
ATOM   10825 C CD  . GLU F 2 69  ? 17.303  25.092  31.393  1.00 80.11  ? 69  GLU D CD  1 
ATOM   10826 O OE1 . GLU F 2 69  ? 16.099  25.367  31.591  1.00 93.91  ? 69  GLU D OE1 1 
ATOM   10827 O OE2 . GLU F 2 69  ? 18.217  25.939  31.542  1.00 69.64  ? 69  GLU D OE2 1 
ATOM   10828 N N   . PHE F 2 70  ? 19.957  19.976  29.812  1.00 43.26  ? 70  PHE D N   1 
ATOM   10829 C CA  . PHE F 2 70  ? 20.671  18.882  30.465  1.00 44.32  ? 70  PHE D CA  1 
ATOM   10830 C C   . PHE F 2 70  ? 21.888  18.439  29.652  1.00 49.33  ? 70  PHE D C   1 
ATOM   10831 O O   . PHE F 2 70  ? 21.840  18.380  28.422  1.00 50.43  ? 70  PHE D O   1 
ATOM   10832 C CB  . PHE F 2 70  ? 19.732  17.705  30.694  1.00 41.62  ? 70  PHE D CB  1 
ATOM   10833 C CG  . PHE F 2 70  ? 18.647  18.001  31.683  1.00 41.29  ? 70  PHE D CG  1 
ATOM   10834 C CD1 . PHE F 2 70  ? 17.322  18.083  31.282  1.00 41.20  ? 70  PHE D CD1 1 
ATOM   10835 C CD2 . PHE F 2 70  ? 18.956  18.240  33.016  1.00 39.05  ? 70  PHE D CD2 1 
ATOM   10836 C CE1 . PHE F 2 70  ? 16.325  18.375  32.199  1.00 41.10  ? 70  PHE D CE1 1 
ATOM   10837 C CE2 . PHE F 2 70  ? 17.964  18.526  33.941  1.00 37.42  ? 70  PHE D CE2 1 
ATOM   10838 C CZ  . PHE F 2 70  ? 16.646  18.597  33.530  1.00 39.92  ? 70  PHE D CZ  1 
ATOM   10839 N N   . ASN F 2 71  ? 22.974  18.122  30.356  1.00 49.53  ? 71  ASN D N   1 
ATOM   10840 C CA  . ASN F 2 71  ? 24.246  17.791  29.716  1.00 48.57  ? 71  ASN D CA  1 
ATOM   10841 C C   . ASN F 2 71  ? 24.332  16.312  29.345  1.00 46.84  ? 71  ASN D C   1 
ATOM   10842 O O   . ASN F 2 71  ? 23.407  15.547  29.618  1.00 45.94  ? 71  ASN D O   1 
ATOM   10843 C CB  . ASN F 2 71  ? 25.425  18.222  30.603  1.00 48.63  ? 71  ASN D CB  1 
ATOM   10844 C CG  . ASN F 2 71  ? 25.559  17.387  31.863  1.00 46.80  ? 71  ASN D CG  1 
ATOM   10845 O OD1 . ASN F 2 71  ? 25.598  16.157  31.811  1.00 43.97  ? 71  ASN D OD1 1 
ATOM   10846 N ND2 . ASN F 2 71  ? 25.650  18.058  33.005  1.00 48.87  ? 71  ASN D ND2 1 
ATOM   10847 N N   . ASN F 2 72  ? 25.451  15.920  28.741  1.00 47.00  ? 72  ASN D N   1 
ATOM   10848 C CA  . ASN F 2 72  ? 25.619  14.565  28.213  1.00 53.05  ? 72  ASN D CA  1 
ATOM   10849 C C   . ASN F 2 72  ? 25.728  13.460  29.281  1.00 49.04  ? 72  ASN D C   1 
ATOM   10850 O O   . ASN F 2 72  ? 25.618  12.279  28.955  1.00 47.09  ? 72  ASN D O   1 
ATOM   10851 C CB  . ASN F 2 72  ? 26.807  14.511  27.246  1.00 59.13  ? 72  ASN D CB  1 
ATOM   10852 C CG  . ASN F 2 72  ? 28.117  14.679  27.942  1.00 70.29  ? 72  ASN D CG  1 
ATOM   10853 O OD1 . ASN F 2 72  ? 28.368  15.729  28.501  1.00 82.01  ? 72  ASN D OD1 1 
ATOM   10854 N ND2 . ASN F 2 72  ? 28.955  13.653  27.921  1.00 80.61  ? 72  ASN D ND2 1 
ATOM   10855 N N   . LEU F 2 73  ? 25.941  13.835  30.543  1.00 47.16  ? 73  LEU D N   1 
ATOM   10856 C CA  . LEU F 2 73  ? 25.857  12.878  31.657  1.00 47.67  ? 73  LEU D CA  1 
ATOM   10857 C C   . LEU F 2 73  ? 24.544  13.026  32.450  1.00 47.68  ? 73  LEU D C   1 
ATOM   10858 O O   . LEU F 2 73  ? 24.467  12.629  33.611  1.00 45.19  ? 73  LEU D O   1 
ATOM   10859 C CB  . LEU F 2 73  ? 27.071  13.019  32.587  1.00 48.99  ? 73  LEU D CB  1 
ATOM   10860 C CG  . LEU F 2 73  ? 28.410  12.485  32.064  1.00 55.62  ? 73  LEU D CG  1 
ATOM   10861 C CD1 . LEU F 2 73  ? 29.538  12.925  32.984  1.00 54.72  ? 73  LEU D CD1 1 
ATOM   10862 C CD2 . LEU F 2 73  ? 28.389  10.967  31.927  1.00 51.80  ? 73  LEU D CD2 1 
ATOM   10863 N N   . GLU F 2 74  ? 23.518  13.590  31.812  1.00 44.75  ? 74  GLU D N   1 
ATOM   10864 C CA  . GLU F 2 74  ? 22.200  13.761  32.429  1.00 43.95  ? 74  GLU D CA  1 
ATOM   10865 C C   . GLU F 2 74  ? 21.092  13.292  31.469  1.00 41.75  ? 74  GLU D C   1 
ATOM   10866 O O   . GLU F 2 74  ? 20.003  13.859  31.441  1.00 37.86  ? 74  GLU D O   1 
ATOM   10867 C CB  . GLU F 2 74  ? 21.990  15.231  32.811  1.00 42.87  ? 74  GLU D CB  1 
ATOM   10868 C CG  . GLU F 2 74  ? 22.891  15.738  33.933  1.00 40.67  ? 74  GLU D CG  1 
ATOM   10869 C CD  . GLU F 2 74  ? 22.779  17.245  34.157  1.00 43.30  ? 74  GLU D CD  1 
ATOM   10870 O OE1 . GLU F 2 74  ? 22.644  17.999  33.172  1.00 40.65  ? 74  GLU D OE1 1 
ATOM   10871 O OE2 . GLU F 2 74  ? 22.836  17.690  35.323  1.00 49.02  ? 74  GLU D OE2 1 
ATOM   10872 N N   . ARG F 2 75  ? 21.378  12.251  30.692  1.00 41.11  ? 75  ARG D N   1 
ATOM   10873 C CA  . ARG F 2 75  ? 20.490  11.827  29.613  1.00 41.44  ? 75  ARG D CA  1 
ATOM   10874 C C   . ARG F 2 75  ? 19.258  11.088  30.123  1.00 36.97  ? 75  ARG D C   1 
ATOM   10875 O O   . ARG F 2 75  ? 18.216  11.074  29.462  1.00 33.76  ? 75  ARG D O   1 
ATOM   10876 C CB  . ARG F 2 75  ? 21.251  10.964  28.596  1.00 50.60  ? 75  ARG D CB  1 
ATOM   10877 C CG  . ARG F 2 75  ? 22.559  11.596  28.108  1.00 60.81  ? 75  ARG D CG  1 
ATOM   10878 C CD  . ARG F 2 75  ? 22.834  11.330  26.627  1.00 70.93  ? 75  ARG D CD  1 
ATOM   10879 N NE  . ARG F 2 75  ? 22.176  12.282  25.715  1.00 79.08  ? 75  ARG D NE  1 
ATOM   10880 C CZ  . ARG F 2 75  ? 21.505  11.977  24.596  1.00 83.78  ? 75  ARG D CZ  1 
ATOM   10881 N NH1 . ARG F 2 75  ? 21.358  10.717  24.180  1.00 77.15  ? 75  ARG D NH1 1 
ATOM   10882 N NH2 . ARG F 2 75  ? 20.969  12.959  23.870  1.00 88.36  ? 75  ARG D NH2 1 
ATOM   10883 N N   . ARG F 2 76  ? 19.368  10.470  31.291  1.00 36.29  ? 76  ARG D N   1 
ATOM   10884 C CA  . ARG F 2 76  ? 18.203  9.847   31.919  1.00 36.61  ? 76  ARG D CA  1 
ATOM   10885 C C   . ARG F 2 76  ? 17.152  10.889  32.292  1.00 37.51  ? 76  ARG D C   1 
ATOM   10886 O O   . ARG F 2 76  ? 15.953  10.626  32.179  1.00 38.93  ? 76  ARG D O   1 
ATOM   10887 C CB  . ARG F 2 76  ? 18.605  9.069   33.164  1.00 35.00  ? 76  ARG D CB  1 
ATOM   10888 C CG  . ARG F 2 76  ? 19.449  7.837   32.887  1.00 32.59  ? 76  ARG D CG  1 
ATOM   10889 C CD  . ARG F 2 76  ? 19.955  7.253   34.193  1.00 31.30  ? 76  ARG D CD  1 
ATOM   10890 N NE  . ARG F 2 76  ? 20.760  8.228   34.934  1.00 29.60  ? 76  ARG D NE  1 
ATOM   10891 C CZ  . ARG F 2 76  ? 20.938  8.229   36.251  1.00 29.58  ? 76  ARG D CZ  1 
ATOM   10892 N NH1 . ARG F 2 76  ? 20.368  7.306   37.018  1.00 33.62  ? 76  ARG D NH1 1 
ATOM   10893 N NH2 . ARG F 2 76  ? 21.683  9.171   36.812  1.00 30.26  ? 76  ARG D NH2 1 
ATOM   10894 N N   . ILE F 2 77  ? 17.604  12.064  32.735  1.00 38.43  ? 77  ILE D N   1 
ATOM   10895 C CA  . ILE F 2 77  ? 16.694  13.161  33.062  1.00 41.19  ? 77  ILE D CA  1 
ATOM   10896 C C   . ILE F 2 77  ? 16.127  13.773  31.783  1.00 39.73  ? 77  ILE D C   1 
ATOM   10897 O O   . ILE F 2 77  ? 14.948  14.100  31.718  1.00 39.73  ? 77  ILE D O   1 
ATOM   10898 C CB  . ILE F 2 77  ? 17.373  14.261  33.899  1.00 41.43  ? 77  ILE D CB  1 
ATOM   10899 C CG1 . ILE F 2 77  ? 17.928  13.689  35.207  1.00 45.80  ? 77  ILE D CG1 1 
ATOM   10900 C CG2 . ILE F 2 77  ? 16.374  15.364  34.211  1.00 44.34  ? 77  ILE D CG2 1 
ATOM   10901 C CD1 . ILE F 2 77  ? 18.659  14.708  36.055  1.00 42.71  ? 77  ILE D CD1 1 
ATOM   10902 N N   . GLU F 2 78  ? 16.972  13.924  30.770  1.00 42.25  ? 78  GLU D N   1 
ATOM   10903 C CA  . GLU F 2 78  ? 16.523  14.411  29.462  1.00 46.14  ? 78  GLU D CA  1 
ATOM   10904 C C   . GLU F 2 78  ? 15.474  13.465  28.860  1.00 43.40  ? 78  GLU D C   1 
ATOM   10905 O O   . GLU F 2 78  ? 14.509  13.920  28.256  1.00 44.56  ? 78  GLU D O   1 
ATOM   10906 C CB  . GLU F 2 78  ? 17.721  14.574  28.518  1.00 51.94  ? 78  GLU D CB  1 
ATOM   10907 C CG  . GLU F 2 78  ? 17.421  15.148  27.129  1.00 64.46  ? 78  GLU D CG  1 
ATOM   10908 C CD  . GLU F 2 78  ? 18.517  14.848  26.114  1.00 82.40  ? 78  GLU D CD  1 
ATOM   10909 O OE1 . GLU F 2 78  ? 19.012  13.699  26.098  1.00 77.66  ? 78  GLU D OE1 1 
ATOM   10910 O OE2 . GLU F 2 78  ? 18.873  15.763  25.328  1.00 98.03  ? 78  GLU D OE2 1 
ATOM   10911 N N   . ASN F 2 79  ? 15.657  12.156  29.040  1.00 37.92  ? 79  ASN D N   1 
ATOM   10912 C CA  . ASN F 2 79  ? 14.679  11.177  28.569  1.00 33.75  ? 79  ASN D CA  1 
ATOM   10913 C C   . ASN F 2 79  ? 13.367  11.288  29.343  1.00 35.32  ? 79  ASN D C   1 
ATOM   10914 O O   . ASN F 2 79  ? 12.285  11.159  28.769  1.00 40.55  ? 79  ASN D O   1 
ATOM   10915 C CB  . ASN F 2 79  ? 15.245  9.762   28.678  1.00 34.61  ? 79  ASN D CB  1 
ATOM   10916 C CG  . ASN F 2 79  ? 14.282  8.695   28.192  1.00 36.67  ? 79  ASN D CG  1 
ATOM   10917 O OD1 . ASN F 2 79  ? 13.656  8.840   27.149  1.00 38.97  ? 79  ASN D OD1 1 
ATOM   10918 N ND2 . ASN F 2 79  ? 14.179  7.604   28.939  1.00 39.36  ? 79  ASN D ND2 1 
ATOM   10919 N N   . LEU F 2 80  ? 13.462  11.547  30.642  1.00 33.68  ? 80  LEU D N   1 
ATOM   10920 C CA  . LEU F 2 80  ? 12.276  11.780  31.462  1.00 33.70  ? 80  LEU D CA  1 
ATOM   10921 C C   . LEU F 2 80  ? 11.484  12.987  30.942  1.00 31.77  ? 80  LEU D C   1 
ATOM   10922 O O   . LEU F 2 80  ? 10.262  12.941  30.846  1.00 29.35  ? 80  LEU D O   1 
ATOM   10923 C CB  . LEU F 2 80  ? 12.679  11.981  32.925  1.00 40.46  ? 80  LEU D CB  1 
ATOM   10924 C CG  . LEU F 2 80  ? 11.577  12.274  33.950  1.00 43.85  ? 80  LEU D CG  1 
ATOM   10925 C CD1 . LEU F 2 80  ? 10.504  11.205  33.917  1.00 39.64  ? 80  LEU D CD1 1 
ATOM   10926 C CD2 . LEU F 2 80  ? 12.175  12.396  35.344  1.00 41.15  ? 80  LEU D CD2 1 
ATOM   10927 N N   . ASN F 2 81  ? 12.189  14.051  30.577  1.00 30.74  ? 81  ASN D N   1 
ATOM   10928 C CA  . ASN F 2 81  ? 11.555  15.209  29.963  1.00 33.06  ? 81  ASN D CA  1 
ATOM   10929 C C   . ASN F 2 81  ? 10.938  14.888  28.608  1.00 34.17  ? 81  ASN D C   1 
ATOM   10930 O O   . ASN F 2 81  ? 9.859   15.382  28.287  1.00 39.44  ? 81  ASN D O   1 
ATOM   10931 C CB  . ASN F 2 81  ? 12.554  16.357  29.814  1.00 35.72  ? 81  ASN D CB  1 
ATOM   10932 C CG  . ASN F 2 81  ? 11.937  17.592  29.177  1.00 38.16  ? 81  ASN D CG  1 
ATOM   10933 O OD1 . ASN F 2 81  ? 11.132  18.283  29.795  1.00 42.64  ? 81  ASN D OD1 1 
ATOM   10934 N ND2 . ASN F 2 81  ? 12.323  17.879  27.943  1.00 42.23  ? 81  ASN D ND2 1 
ATOM   10935 N N   . LYS F 2 82  ? 11.627  14.075  27.812  1.00 34.65  ? 82  LYS D N   1 
ATOM   10936 C CA  . LYS F 2 82  ? 11.109  13.667  26.507  1.00 37.04  ? 82  LYS D CA  1 
ATOM   10937 C C   . LYS F 2 82  ? 9.797   12.890  26.650  1.00 34.00  ? 82  LYS D C   1 
ATOM   10938 O O   . LYS F 2 82  ? 8.832   13.170  25.945  1.00 30.65  ? 82  LYS D O   1 
ATOM   10939 C CB  . LYS F 2 82  ? 12.138  12.828  25.742  1.00 40.29  ? 82  LYS D CB  1 
ATOM   10940 C CG  . LYS F 2 82  ? 11.605  12.228  24.444  1.00 43.13  ? 82  LYS D CG  1 
ATOM   10941 C CD  . LYS F 2 82  ? 12.602  11.282  23.787  1.00 46.16  ? 82  LYS D CD  1 
ATOM   10942 C CE  . LYS F 2 82  ? 11.914  10.328  22.817  1.00 47.23  ? 82  LYS D CE  1 
ATOM   10943 N NZ  . LYS F 2 82  ? 11.045  11.013  21.814  1.00 48.95  ? 82  LYS D NZ  1 
ATOM   10944 N N   . LYS F 2 83  ? 9.769   11.921  27.561  1.00 35.08  ? 83  LYS D N   1 
ATOM   10945 C CA  . LYS F 2 83  ? 8.545   11.160  27.830  1.00 36.81  ? 83  LYS D CA  1 
ATOM   10946 C C   . LYS F 2 83  ? 7.383   12.082  28.201  1.00 37.30  ? 83  LYS D C   1 
ATOM   10947 O O   . LYS F 2 83  ? 6.266   11.901  27.719  1.00 36.30  ? 83  LYS D O   1 
ATOM   10948 C CB  . LYS F 2 83  ? 8.775   10.131  28.941  1.00 38.10  ? 83  LYS D CB  1 
ATOM   10949 C CG  . LYS F 2 83  ? 9.624   8.949   28.499  1.00 41.56  ? 83  LYS D CG  1 
ATOM   10950 C CD  . LYS F 2 83  ? 9.719   7.864   29.562  1.00 43.21  ? 83  LYS D CD  1 
ATOM   10951 C CE  . LYS F 2 83  ? 10.685  8.238   30.674  1.00 43.40  ? 83  LYS D CE  1 
ATOM   10952 N NZ  . LYS F 2 83  ? 10.761  7.208   31.744  1.00 45.74  ? 83  LYS D NZ  1 
ATOM   10953 N N   . MET F 2 84  ? 7.664   13.082  29.034  1.00 36.12  ? 84  MET D N   1 
ATOM   10954 C CA  . MET F 2 84  ? 6.660   14.059  29.438  1.00 35.84  ? 84  MET D CA  1 
ATOM   10955 C C   . MET F 2 84  ? 6.154   14.891  28.260  1.00 35.98  ? 84  MET D C   1 
ATOM   10956 O O   . MET F 2 84  ? 4.950   14.950  28.021  1.00 36.17  ? 84  MET D O   1 
ATOM   10957 C CB  . MET F 2 84  ? 7.227   14.984  30.515  1.00 38.71  ? 84  MET D CB  1 
ATOM   10958 C CG  . MET F 2 84  ? 6.179   15.812  31.239  1.00 39.43  ? 84  MET D CG  1 
ATOM   10959 S SD  . MET F 2 84  ? 6.875   17.317  31.939  1.00 48.40  ? 84  MET D SD  1 
ATOM   10960 C CE  . MET F 2 84  ? 6.748   18.442  30.546  1.00 47.22  ? 84  MET D CE  1 
ATOM   10961 N N   . GLU F 2 85  ? 7.066   15.541  27.537  1.00 39.67  ? 85  GLU D N   1 
ATOM   10962 C CA  . GLU F 2 85  ? 6.684   16.375  26.381  1.00 41.36  ? 85  GLU D CA  1 
ATOM   10963 C C   . GLU F 2 85  ? 5.883   15.581  25.357  1.00 38.38  ? 85  GLU D C   1 
ATOM   10964 O O   . GLU F 2 85  ? 4.859   16.049  24.863  1.00 34.80  ? 85  GLU D O   1 
ATOM   10965 C CB  . GLU F 2 85  ? 7.913   16.973  25.685  1.00 49.12  ? 85  GLU D CB  1 
ATOM   10966 C CG  . GLU F 2 85  ? 8.492   18.205  26.362  1.00 56.58  ? 85  GLU D CG  1 
ATOM   10967 C CD  . GLU F 2 85  ? 9.609   18.857  25.556  1.00 57.87  ? 85  GLU D CD  1 
ATOM   10968 O OE1 . GLU F 2 85  ? 9.542   18.857  24.306  1.00 58.58  ? 85  GLU D OE1 1 
ATOM   10969 O OE2 . GLU F 2 85  ? 10.554  19.385  26.179  1.00 61.35  ? 85  GLU D OE2 1 
ATOM   10970 N N   . ASP F 2 86  ? 6.377   14.392  25.028  1.00 39.92  ? 86  ASP D N   1 
ATOM   10971 C CA  . ASP F 2 86  ? 5.687   13.499  24.106  1.00 40.66  ? 86  ASP D CA  1 
ATOM   10972 C C   . ASP F 2 86  ? 4.321   13.088  24.653  1.00 39.96  ? 86  ASP D C   1 
ATOM   10973 O O   . ASP F 2 86  ? 3.346   13.003  23.902  1.00 39.32  ? 86  ASP D O   1 
ATOM   10974 C CB  . ASP F 2 86  ? 6.548   12.258  23.826  1.00 44.32  ? 86  ASP D CB  1 
ATOM   10975 C CG  . ASP F 2 86  ? 7.785   12.574  22.984  1.00 49.26  ? 86  ASP D CG  1 
ATOM   10976 O OD1 . ASP F 2 86  ? 7.963   13.744  22.583  1.00 53.72  ? 86  ASP D OD1 1 
ATOM   10977 O OD2 . ASP F 2 86  ? 8.581   11.649  22.719  1.00 45.84  ? 86  ASP D OD2 1 
ATOM   10978 N N   . GLY F 2 87  ? 4.256   12.831  25.961  1.00 37.27  ? 87  GLY D N   1 
ATOM   10979 C CA  . GLY F 2 87  ? 3.001   12.484  26.621  1.00 32.52  ? 87  GLY D CA  1 
ATOM   10980 C C   . GLY F 2 87  ? 1.941   13.554  26.425  1.00 31.07  ? 87  GLY D C   1 
ATOM   10981 O O   . GLY F 2 87  ? 0.827   13.260  25.994  1.00 32.29  ? 87  GLY D O   1 
ATOM   10982 N N   . PHE F 2 88  ? 2.286   14.803  26.714  1.00 29.61  ? 88  PHE D N   1 
ATOM   10983 C CA  . PHE F 2 88  ? 1.320   15.892  26.571  1.00 33.20  ? 88  PHE D CA  1 
ATOM   10984 C C   . PHE F 2 88  ? 0.940   16.141  25.116  1.00 31.35  ? 88  PHE D C   1 
ATOM   10985 O O   . PHE F 2 88  ? -0.219  16.413  24.820  1.00 30.85  ? 88  PHE D O   1 
ATOM   10986 C CB  . PHE F 2 88  ? 1.814   17.177  27.250  1.00 31.44  ? 88  PHE D CB  1 
ATOM   10987 C CG  . PHE F 2 88  ? 1.733   17.130  28.754  1.00 33.32  ? 88  PHE D CG  1 
ATOM   10988 C CD1 . PHE F 2 88  ? 2.868   17.273  29.533  1.00 34.82  ? 88  PHE D CD1 1 
ATOM   10989 C CD2 . PHE F 2 88  ? 0.514   16.924  29.389  1.00 35.42  ? 88  PHE D CD2 1 
ATOM   10990 C CE1 . PHE F 2 88  ? 2.793   17.222  30.912  1.00 35.65  ? 88  PHE D CE1 1 
ATOM   10991 C CE2 . PHE F 2 88  ? 0.430   16.877  30.769  1.00 38.21  ? 88  PHE D CE2 1 
ATOM   10992 C CZ  . PHE F 2 88  ? 1.573   17.023  31.534  1.00 38.51  ? 88  PHE D CZ  1 
ATOM   10993 N N   . LEU F 2 89  ? 1.903   16.026  24.211  1.00 33.33  ? 89  LEU D N   1 
ATOM   10994 C CA  . LEU F 2 89  ? 1.612   16.149  22.782  1.00 34.63  ? 89  LEU D CA  1 
ATOM   10995 C C   . LEU F 2 89  ? 0.589   15.111  22.340  1.00 34.83  ? 89  LEU D C   1 
ATOM   10996 O O   . LEU F 2 89  ? -0.305  15.418  21.546  1.00 36.44  ? 89  LEU D O   1 
ATOM   10997 C CB  . LEU F 2 89  ? 2.886   16.016  21.943  1.00 33.79  ? 89  LEU D CB  1 
ATOM   10998 C CG  . LEU F 2 89  ? 2.668   16.155  20.434  1.00 34.00  ? 89  LEU D CG  1 
ATOM   10999 C CD1 . LEU F 2 89  ? 3.803   16.920  19.774  1.00 36.75  ? 89  LEU D CD1 1 
ATOM   11000 C CD2 . LEU F 2 89  ? 2.512   14.781  19.798  1.00 36.18  ? 89  LEU D CD2 1 
ATOM   11001 N N   . ASP F 2 90  ? 0.714   13.891  22.858  1.00 32.36  ? 90  ASP D N   1 
ATOM   11002 C CA  . ASP F 2 90  ? -0.236  12.830  22.533  1.00 35.10  ? 90  ASP D CA  1 
ATOM   11003 C C   . ASP F 2 90  ? -1.619  13.100  23.127  1.00 31.19  ? 90  ASP D C   1 
ATOM   11004 O O   . ASP F 2 90  ? -2.632  12.887  22.465  1.00 32.52  ? 90  ASP D O   1 
ATOM   11005 C CB  . ASP F 2 90  ? 0.284   11.466  23.006  1.00 42.20  ? 90  ASP D CB  1 
ATOM   11006 C CG  . ASP F 2 90  ? 1.518   10.995  22.230  1.00 49.26  ? 90  ASP D CG  1 
ATOM   11007 O OD1 . ASP F 2 90  ? 1.836   11.574  21.164  1.00 51.12  ? 90  ASP D OD1 1 
ATOM   11008 O OD2 . ASP F 2 90  ? 2.166   10.029  22.689  1.00 55.66  ? 90  ASP D OD2 1 
ATOM   11009 N N   . VAL F 2 91  ? -1.661  13.565  24.371  1.00 28.83  ? 91  VAL D N   1 
ATOM   11010 C CA  . VAL F 2 91  ? -2.934  13.838  25.029  1.00 26.10  ? 91  VAL D CA  1 
ATOM   11011 C C   . VAL F 2 91  ? -3.688  14.945  24.308  1.00 24.31  ? 91  VAL D C   1 
ATOM   11012 O O   . VAL F 2 91  ? -4.845  14.765  23.932  1.00 22.34  ? 91  VAL D O   1 
ATOM   11013 C CB  . VAL F 2 91  ? -2.755  14.193  26.522  1.00 24.20  ? 91  VAL D CB  1 
ATOM   11014 C CG1 . VAL F 2 91  ? -4.011  14.861  27.065  1.00 20.64  ? 91  VAL D CG1 1 
ATOM   11015 C CG2 . VAL F 2 91  ? -2.425  12.945  27.326  1.00 23.01  ? 91  VAL D CG2 1 
ATOM   11016 N N   . TRP F 2 92  ? -3.021  16.070  24.082  1.00 26.92  ? 92  TRP D N   1 
ATOM   11017 C CA  . TRP F 2 92  ? -3.660  17.209  23.408  1.00 28.11  ? 92  TRP D CA  1 
ATOM   11018 C C   . TRP F 2 92  ? -4.056  16.914  21.986  1.00 28.46  ? 92  TRP D C   1 
ATOM   11019 O O   . TRP F 2 92  ? -5.107  17.352  21.537  1.00 31.86  ? 92  TRP D O   1 
ATOM   11020 C CB  . TRP F 2 92  ? -2.762  18.434  23.446  1.00 27.12  ? 92  TRP D CB  1 
ATOM   11021 C CG  . TRP F 2 92  ? -2.677  19.052  24.815  1.00 30.08  ? 92  TRP D CG  1 
ATOM   11022 C CD1 . TRP F 2 92  ? -1.550  19.201  25.616  1.00 30.77  ? 92  TRP D CD1 1 
ATOM   11023 C CD2 . TRP F 2 92  ? -3.779  19.622  25.603  1.00 30.54  ? 92  TRP D CD2 1 
ATOM   11024 N NE1 . TRP F 2 92  ? -1.870  19.813  26.798  1.00 32.04  ? 92  TRP D NE1 1 
ATOM   11025 C CE2 . TRP F 2 92  ? -3.190  20.085  26.854  1.00 28.29  ? 92  TRP D CE2 1 
ATOM   11026 C CE3 . TRP F 2 92  ? -5.136  19.783  25.401  1.00 31.95  ? 92  TRP D CE3 1 
ATOM   11027 C CZ2 . TRP F 2 92  ? -3.944  20.685  27.838  1.00 30.34  ? 92  TRP D CZ2 1 
ATOM   11028 C CZ3 . TRP F 2 92  ? -5.890  20.385  26.404  1.00 31.23  ? 92  TRP D CZ3 1 
ATOM   11029 C CH2 . TRP F 2 92  ? -5.308  20.829  27.590  1.00 31.09  ? 92  TRP D CH2 1 
ATOM   11030 N N   . THR F 2 93  ? -3.224  16.176  21.263  1.00 27.67  ? 93  THR D N   1 
ATOM   11031 C CA  . THR F 2 93  ? -3.523  15.841  19.875  1.00 30.29  ? 93  THR D CA  1 
ATOM   11032 C C   . THR F 2 93  ? -4.801  15.028  19.786  1.00 31.16  ? 93  THR D C   1 
ATOM   11033 O O   . THR F 2 93  ? -5.708  15.369  19.025  1.00 32.02  ? 93  THR D O   1 
ATOM   11034 C CB  . THR F 2 93  ? -2.351  15.080  19.221  1.00 32.00  ? 93  THR D CB  1 
ATOM   11035 O OG1 . THR F 2 93  ? -1.234  15.969  19.093  1.00 32.82  ? 93  THR D OG1 1 
ATOM   11036 C CG2 . THR F 2 93  ? -2.734  14.520  17.853  1.00 30.52  ? 93  THR D CG2 1 
ATOM   11037 N N   . TYR F 2 94  ? -4.880  13.966  20.577  1.00 30.73  ? 94  TYR D N   1 
ATOM   11038 C CA  . TYR F 2 94  ? -6.056  13.099  20.560  1.00 33.35  ? 94  TYR D CA  1 
ATOM   11039 C C   . TYR F 2 94  ? -7.322  13.836  20.984  1.00 35.59  ? 94  TYR D C   1 
ATOM   11040 O O   . TYR F 2 94  ? -8.351  13.737  20.316  1.00 39.09  ? 94  TYR D O   1 
ATOM   11041 C CB  . TYR F 2 94  ? -5.839  11.907  21.477  1.00 35.28  ? 94  TYR D CB  1 
ATOM   11042 C CG  . TYR F 2 94  ? -6.810  10.777  21.264  1.00 36.07  ? 94  TYR D CG  1 
ATOM   11043 C CD1 . TYR F 2 94  ? -6.730  9.975   20.135  1.00 34.75  ? 94  TYR D CD1 1 
ATOM   11044 C CD2 . TYR F 2 94  ? -7.796  10.495  22.205  1.00 35.29  ? 94  TYR D CD2 1 
ATOM   11045 C CE1 . TYR F 2 94  ? -7.610  8.924   19.941  1.00 38.28  ? 94  TYR D CE1 1 
ATOM   11046 C CE2 . TYR F 2 94  ? -8.678  9.448   22.022  1.00 35.85  ? 94  TYR D CE2 1 
ATOM   11047 C CZ  . TYR F 2 94  ? -8.581  8.662   20.889  1.00 37.45  ? 94  TYR D CZ  1 
ATOM   11048 O OH  . TYR F 2 94  ? -9.460  7.621   20.699  1.00 38.48  ? 94  TYR D OH  1 
ATOM   11049 N N   . ASN F 2 95  ? -7.238  14.577  22.086  1.00 33.91  ? 95  ASN D N   1 
ATOM   11050 C CA  . ASN F 2 95  ? -8.392  15.301  22.602  1.00 35.93  ? 95  ASN D CA  1 
ATOM   11051 C C   . ASN F 2 95  ? -8.861  16.380  21.639  1.00 38.19  ? 95  ASN D C   1 
ATOM   11052 O O   . ASN F 2 95  ? -10.059 16.534  21.424  1.00 42.22  ? 95  ASN D O   1 
ATOM   11053 C CB  . ASN F 2 95  ? -8.089  15.919  23.973  1.00 43.28  ? 95  ASN D CB  1 
ATOM   11054 C CG  . ASN F 2 95  ? -7.988  14.879  25.078  1.00 48.79  ? 95  ASN D CG  1 
ATOM   11055 O OD1 . ASN F 2 95  ? -8.115  13.668  24.841  1.00 44.59  ? 95  ASN D OD1 1 
ATOM   11056 N ND2 . ASN F 2 95  ? -7.755  15.351  26.299  1.00 51.94  ? 95  ASN D ND2 1 
ATOM   11057 N N   . ALA F 2 96  ? -7.919  17.125  21.064  1.00 38.01  ? 96  ALA D N   1 
ATOM   11058 C CA  . ALA F 2 96  ? -8.251  18.181  20.112  1.00 35.77  ? 96  ALA D CA  1 
ATOM   11059 C C   . ALA F 2 96  ? -8.923  17.607  18.864  1.00 38.49  ? 96  ALA D C   1 
ATOM   11060 O O   . ALA F 2 96  ? -9.968  18.098  18.432  1.00 40.68  ? 96  ALA D O   1 
ATOM   11061 C CB  . ALA F 2 96  ? -7.004  18.956  19.733  1.00 35.85  ? 96  ALA D CB  1 
ATOM   11062 N N   . GLU F 2 97  ? -8.337  16.550  18.310  1.00 38.03  ? 97  GLU D N   1 
ATOM   11063 C CA  . GLU F 2 97  ? -8.898  15.901  17.129  1.00 39.29  ? 97  GLU D CA  1 
ATOM   11064 C C   . GLU F 2 97  ? -10.300 15.357  17.397  1.00 40.88  ? 97  GLU D C   1 
ATOM   11065 O O   . GLU F 2 97  ? -11.225 15.606  16.621  1.00 43.10  ? 97  GLU D O   1 
ATOM   11066 C CB  . GLU F 2 97  ? -7.993  14.765  16.649  1.00 42.02  ? 97  GLU D CB  1 
ATOM   11067 C CG  . GLU F 2 97  ? -6.665  15.233  16.073  1.00 48.58  ? 97  GLU D CG  1 
ATOM   11068 C CD  . GLU F 2 97  ? -6.769  15.790  14.664  1.00 57.17  ? 97  GLU D CD  1 
ATOM   11069 O OE1 . GLU F 2 97  ? -7.879  15.834  14.092  1.00 62.62  ? 97  GLU D OE1 1 
ATOM   11070 O OE2 . GLU F 2 97  ? -5.718  16.191  14.124  1.00 63.82  ? 97  GLU D OE2 1 
ATOM   11071 N N   . LEU F 2 98  ? -10.458 14.614  18.488  1.00 38.33  ? 98  LEU D N   1 
ATOM   11072 C CA  . LEU F 2 98  ? -11.747 14.003  18.789  1.00 37.96  ? 98  LEU D CA  1 
ATOM   11073 C C   . LEU F 2 98  ? -12.796 15.028  19.199  1.00 34.31  ? 98  LEU D C   1 
ATOM   11074 O O   . LEU F 2 98  ? -13.972 14.851  18.900  1.00 39.64  ? 98  LEU D O   1 
ATOM   11075 C CB  . LEU F 2 98  ? -11.611 12.916  19.857  1.00 40.25  ? 98  LEU D CB  1 
ATOM   11076 C CG  . LEU F 2 98  ? -10.993 11.595  19.391  1.00 40.20  ? 98  LEU D CG  1 
ATOM   11077 C CD1 . LEU F 2 98  ? -11.169 10.535  20.463  1.00 45.00  ? 98  LEU D CD1 1 
ATOM   11078 C CD2 . LEU F 2 98  ? -11.616 11.121  18.092  1.00 39.80  ? 98  LEU D CD2 1 
ATOM   11079 N N   . LEU F 2 99  ? -12.378 16.091  19.872  1.00 29.81  ? 99  LEU D N   1 
ATOM   11080 C CA  . LEU F 2 99  ? -13.291 17.176  20.212  1.00 32.50  ? 99  LEU D CA  1 
ATOM   11081 C C   . LEU F 2 99  ? -13.873 17.809  18.956  1.00 34.71  ? 99  LEU D C   1 
ATOM   11082 O O   . LEU F 2 99  ? -15.069 18.072  18.892  1.00 38.68  ? 99  LEU D O   1 
ATOM   11083 C CB  . LEU F 2 99  ? -12.569 18.245  21.028  1.00 35.28  ? 99  LEU D CB  1 
ATOM   11084 C CG  . LEU F 2 99  ? -13.387 19.472  21.408  1.00 34.13  ? 99  LEU D CG  1 
ATOM   11085 C CD1 . LEU F 2 99  ? -14.556 19.069  22.292  1.00 33.74  ? 99  LEU D CD1 1 
ATOM   11086 C CD2 . LEU F 2 99  ? -12.470 20.463  22.112  1.00 32.75  ? 99  LEU D CD2 1 
ATOM   11087 N N   . VAL F 2 100 ? -13.017 18.058  17.965  1.00 34.45  ? 100 VAL D N   1 
ATOM   11088 C CA  . VAL F 2 100 ? -13.445 18.654  16.700  1.00 33.61  ? 100 VAL D CA  1 
ATOM   11089 C C   . VAL F 2 100 ? -14.412 17.731  15.949  1.00 37.07  ? 100 VAL D C   1 
ATOM   11090 O O   . VAL F 2 100 ? -15.494 18.162  15.546  1.00 39.41  ? 100 VAL D O   1 
ATOM   11091 C CB  . VAL F 2 100 ? -12.235 18.995  15.799  1.00 33.76  ? 100 VAL D CB  1 
ATOM   11092 C CG1 . VAL F 2 100 ? -12.670 19.266  14.358  1.00 27.69  ? 100 VAL D CG1 1 
ATOM   11093 C CG2 . VAL F 2 100 ? -11.477 20.188  16.366  1.00 31.59  ? 100 VAL D CG2 1 
ATOM   11094 N N   . LEU F 2 101 ? -14.031 16.467  15.779  1.00 30.91  ? 101 LEU D N   1 
ATOM   11095 C CA  . LEU F 2 101 ? -14.896 15.498  15.112  1.00 35.18  ? 101 LEU D CA  1 
ATOM   11096 C C   . LEU F 2 101 ? -16.250 15.361  15.817  1.00 40.53  ? 101 LEU D C   1 
ATOM   11097 O O   . LEU F 2 101 ? -17.294 15.280  15.160  1.00 44.83  ? 101 LEU D O   1 
ATOM   11098 C CB  . LEU F 2 101 ? -14.225 14.124  15.029  1.00 33.30  ? 101 LEU D CB  1 
ATOM   11099 C CG  . LEU F 2 101 ? -12.989 13.996  14.137  1.00 32.65  ? 101 LEU D CG  1 
ATOM   11100 C CD1 . LEU F 2 101 ? -12.536 12.541  14.109  1.00 33.09  ? 101 LEU D CD1 1 
ATOM   11101 C CD2 . LEU F 2 101 ? -13.248 14.513  12.732  1.00 27.97  ? 101 LEU D CD2 1 
ATOM   11102 N N   . MET F 2 102 ? -16.225 15.335  17.148  1.00 37.87  ? 102 MET D N   1 
ATOM   11103 C CA  . MET F 2 102 ? -17.440 15.139  17.943  1.00 40.28  ? 102 MET D CA  1 
ATOM   11104 C C   . MET F 2 102 ? -18.370 16.342  17.856  1.00 35.51  ? 102 MET D C   1 
ATOM   11105 O O   . MET F 2 102 ? -19.560 16.201  17.582  1.00 32.54  ? 102 MET D O   1 
ATOM   11106 C CB  . MET F 2 102 ? -17.084 14.845  19.403  1.00 40.65  ? 102 MET D CB  1 
ATOM   11107 C CG  . MET F 2 102 ? -16.650 13.411  19.644  1.00 43.35  ? 102 MET D CG  1 
ATOM   11108 S SD  . MET F 2 102 ? -15.847 13.121  21.241  1.00 54.62  ? 102 MET D SD  1 
ATOM   11109 C CE  . MET F 2 102 ? -16.372 14.526  22.218  1.00 62.48  ? 102 MET D CE  1 
ATOM   11110 N N   . GLU F 2 103 ? -17.822 17.528  18.064  1.00 38.80  ? 103 GLU D N   1 
ATOM   11111 C CA  . GLU F 2 103 ? -18.638 18.733  18.035  1.00 41.60  ? 103 GLU D CA  1 
ATOM   11112 C C   . GLU F 2 103 ? -19.144 19.087  16.633  1.00 39.06  ? 103 GLU D C   1 
ATOM   11113 O O   . GLU F 2 103 ? -20.208 19.689  16.498  1.00 39.95  ? 103 GLU D O   1 
ATOM   11114 C CB  . GLU F 2 103 ? -17.894 19.906  18.677  1.00 41.88  ? 103 GLU D CB  1 
ATOM   11115 C CG  . GLU F 2 103 ? -17.902 19.858  20.203  1.00 52.64  ? 103 GLU D CG  1 
ATOM   11116 C CD  . GLU F 2 103 ? -19.304 19.768  20.799  1.00 59.89  ? 103 GLU D CD  1 
ATOM   11117 O OE1 . GLU F 2 103 ? -20.246 20.381  20.244  1.00 51.59  ? 103 GLU D OE1 1 
ATOM   11118 O OE2 . GLU F 2 103 ? -19.468 19.073  21.825  1.00 64.75  ? 103 GLU D OE2 1 
ATOM   11119 N N   . ASN F 2 104 ? -18.394 18.715  15.600  1.00 38.94  ? 104 ASN D N   1 
ATOM   11120 C CA  . ASN F 2 104 ? -18.869 18.874  14.224  1.00 36.91  ? 104 ASN D CA  1 
ATOM   11121 C C   . ASN F 2 104 ? -20.096 18.013  13.951  1.00 34.25  ? 104 ASN D C   1 
ATOM   11122 O O   . ASN F 2 104 ? -21.050 18.482  13.345  1.00 35.42  ? 104 ASN D O   1 
ATOM   11123 C CB  . ASN F 2 104 ? -17.765 18.550  13.211  1.00 37.18  ? 104 ASN D CB  1 
ATOM   11124 C CG  . ASN F 2 104 ? -16.739 19.660  13.085  1.00 37.77  ? 104 ASN D CG  1 
ATOM   11125 O OD1 . ASN F 2 104 ? -16.933 20.775  13.583  1.00 37.07  ? 104 ASN D OD1 1 
ATOM   11126 N ND2 . ASN F 2 104 ? -15.632 19.356  12.416  1.00 34.66  ? 104 ASN D ND2 1 
ATOM   11127 N N   . GLU F 2 105 ? -20.077 16.762  14.403  1.00 36.59  ? 105 GLU D N   1 
ATOM   11128 C CA  . GLU F 2 105 ? -21.248 15.893  14.289  1.00 40.62  ? 105 GLU D CA  1 
ATOM   11129 C C   . GLU F 2 105 ? -22.451 16.553  14.973  1.00 41.86  ? 105 GLU D C   1 
ATOM   11130 O O   . GLU F 2 105 ? -23.543 16.622  14.403  1.00 39.59  ? 105 GLU D O   1 
ATOM   11131 C CB  . GLU F 2 105 ? -20.982 14.532  14.932  1.00 44.39  ? 105 GLU D CB  1 
ATOM   11132 C CG  . GLU F 2 105 ? -22.034 13.469  14.634  1.00 52.29  ? 105 GLU D CG  1 
ATOM   11133 C CD  . GLU F 2 105 ? -22.409 12.651  15.864  1.00 73.88  ? 105 GLU D CD  1 
ATOM   11134 O OE1 . GLU F 2 105 ? -22.062 11.449  15.920  1.00 79.60  ? 105 GLU D OE1 1 
ATOM   11135 O OE2 . GLU F 2 105 ? -23.048 13.218  16.782  1.00 97.15  ? 105 GLU D OE2 1 
ATOM   11136 N N   . ARG F 2 106 ? -22.232 17.046  16.190  1.00 39.45  ? 106 ARG D N   1 
ATOM   11137 C CA  . ARG F 2 106 ? -23.282 17.715  16.960  1.00 42.29  ? 106 ARG D CA  1 
ATOM   11138 C C   . ARG F 2 106 ? -23.824 18.955  16.245  1.00 36.42  ? 106 ARG D C   1 
ATOM   11139 O O   . ARG F 2 106 ? -25.042 19.152  16.169  1.00 34.48  ? 106 ARG D O   1 
ATOM   11140 C CB  . ARG F 2 106 ? -22.787 18.084  18.368  1.00 46.02  ? 106 ARG D CB  1 
ATOM   11141 C CG  . ARG F 2 106 ? -22.881 16.978  19.392  1.00 56.92  ? 106 ARG D CG  1 
ATOM   11142 C CD  . ARG F 2 106 ? -23.137 17.468  20.808  1.00 79.19  ? 106 ARG D CD  1 
ATOM   11143 N NE  . ARG F 2 106 ? -22.487 16.612  21.795  1.00 94.01  ? 106 ARG D NE  1 
ATOM   11144 C CZ  . ARG F 2 106 ? -22.352 16.920  23.079  1.00 80.28  ? 106 ARG D CZ  1 
ATOM   11145 N NH1 . ARG F 2 106 ? -22.811 18.075  23.542  1.00 77.84  ? 106 ARG D NH1 1 
ATOM   11146 N NH2 . ARG F 2 106 ? -21.754 16.068  23.900  1.00 74.89  ? 106 ARG D NH2 1 
ATOM   11147 N N   . THR F 2 107 ? -22.924 19.774  15.706  1.00 35.23  ? 107 THR D N   1 
ATOM   11148 C CA  . THR F 2 107 ? -23.326 20.988  14.997  1.00 32.90  ? 107 THR D CA  1 
ATOM   11149 C C   . THR F 2 107 ? -24.190 20.689  13.765  1.00 32.82  ? 107 THR D C   1 
ATOM   11150 O O   . THR F 2 107 ? -25.176 21.381  13.514  1.00 32.47  ? 107 THR D O   1 
ATOM   11151 C CB  . THR F 2 107 ? -22.102 21.829  14.585  1.00 34.61  ? 107 THR D CB  1 
ATOM   11152 O OG1 . THR F 2 107 ? -21.407 22.278  15.759  1.00 35.33  ? 107 THR D OG1 1 
ATOM   11153 C CG2 . THR F 2 107 ? -22.522 23.042  13.744  1.00 35.05  ? 107 THR D CG2 1 
ATOM   11154 N N   . LEU F 2 108 ? -23.838 19.658  13.005  1.00 31.11  ? 108 LEU D N   1 
ATOM   11155 C CA  . LEU F 2 108 ? -24.613 19.329  11.815  1.00 32.84  ? 108 LEU D CA  1 
ATOM   11156 C C   . LEU F 2 108 ? -25.984 18.776  12.191  1.00 32.77  ? 108 LEU D C   1 
ATOM   11157 O O   . LEU F 2 108 ? -26.975 19.103  11.546  1.00 35.92  ? 108 LEU D O   1 
ATOM   11158 C CB  . LEU F 2 108 ? -23.849 18.373  10.889  1.00 34.12  ? 108 LEU D CB  1 
ATOM   11159 C CG  . LEU F 2 108 ? -22.532 18.930  10.312  1.00 40.99  ? 108 LEU D CG  1 
ATOM   11160 C CD1 . LEU F 2 108 ? -21.965 18.008  9.240   1.00 42.51  ? 108 LEU D CD1 1 
ATOM   11161 C CD2 . LEU F 2 108 ? -22.670 20.343  9.757   1.00 39.15  ? 108 LEU D CD2 1 
ATOM   11162 N N   . ASP F 2 109 ? -26.045 17.959  13.240  1.00 37.75  ? 109 ASP D N   1 
ATOM   11163 C CA  . ASP F 2 109 ? -27.329 17.439  13.735  1.00 41.93  ? 109 ASP D CA  1 
ATOM   11164 C C   . ASP F 2 109 ? -28.211 18.542  14.317  1.00 36.68  ? 109 ASP D C   1 
ATOM   11165 O O   . ASP F 2 109 ? -29.430 18.490  14.195  1.00 39.32  ? 109 ASP D O   1 
ATOM   11166 C CB  . ASP F 2 109 ? -27.118 16.324  14.774  1.00 47.76  ? 109 ASP D CB  1 
ATOM   11167 C CG  . ASP F 2 109 ? -26.921 14.953  14.136  1.00 65.89  ? 109 ASP D CG  1 
ATOM   11168 O OD1 . ASP F 2 109 ? -26.111 14.154  14.664  1.00 79.40  ? 109 ASP D OD1 1 
ATOM   11169 O OD2 . ASP F 2 109 ? -27.577 14.675  13.102  1.00 88.68  ? 109 ASP D OD2 1 
ATOM   11170 N N   . PHE F 2 110 ? -27.583 19.537  14.934  1.00 34.38  ? 110 PHE D N   1 
ATOM   11171 C CA  . PHE F 2 110 ? -28.281 20.727  15.416  1.00 36.41  ? 110 PHE D CA  1 
ATOM   11172 C C   . PHE F 2 110 ? -29.056 21.404  14.274  1.00 38.15  ? 110 PHE D C   1 
ATOM   11173 O O   . PHE F 2 110 ? -30.257 21.652  14.400  1.00 40.71  ? 110 PHE D O   1 
ATOM   11174 C CB  . PHE F 2 110 ? -27.246 21.677  16.030  1.00 38.29  ? 110 PHE D CB  1 
ATOM   11175 C CG  . PHE F 2 110 ? -27.809 22.940  16.621  1.00 41.55  ? 110 PHE D CG  1 
ATOM   11176 C CD1 . PHE F 2 110 ? -28.813 22.898  17.574  1.00 41.18  ? 110 PHE D CD1 1 
ATOM   11177 C CD2 . PHE F 2 110 ? -27.266 24.180  16.279  1.00 41.32  ? 110 PHE D CD2 1 
ATOM   11178 C CE1 . PHE F 2 110 ? -29.293 24.072  18.141  1.00 42.63  ? 110 PHE D CE1 1 
ATOM   11179 C CE2 . PHE F 2 110 ? -27.740 25.355  16.842  1.00 39.42  ? 110 PHE D CE2 1 
ATOM   11180 C CZ  . PHE F 2 110 ? -28.756 25.302  17.775  1.00 41.85  ? 110 PHE D CZ  1 
ATOM   11181 N N   . HIS F 2 111 ? -28.375 21.671  13.158  1.00 34.70  ? 111 HIS D N   1 
ATOM   11182 C CA  . HIS F 2 111 ? -29.015 22.283  11.988  1.00 31.98  ? 111 HIS D CA  1 
ATOM   11183 C C   . HIS F 2 111 ? -30.118 21.428  11.445  1.00 32.42  ? 111 HIS D C   1 
ATOM   11184 O O   . HIS F 2 111 ? -31.204 21.926  11.149  1.00 34.76  ? 111 HIS D O   1 
ATOM   11185 C CB  . HIS F 2 111 ? -28.002 22.552  10.876  1.00 31.62  ? 111 HIS D CB  1 
ATOM   11186 C CG  . HIS F 2 111 ? -26.934 23.548  11.248  1.00 30.62  ? 111 HIS D CG  1 
ATOM   11187 N ND1 . HIS F 2 111 ? -27.218 24.723  11.833  1.00 31.47  ? 111 HIS D ND1 1 
ATOM   11188 C CD2 . HIS F 2 111 ? -25.553 23.514  11.084  1.00 31.08  ? 111 HIS D CD2 1 
ATOM   11189 C CE1 . HIS F 2 111 ? -26.079 25.404  12.042  1.00 32.28  ? 111 HIS D CE1 1 
ATOM   11190 N NE2 . HIS F 2 111 ? -25.058 24.667  11.585  1.00 30.36  ? 111 HIS D NE2 1 
ATOM   11191 N N   . ASP F 2 112 ? -29.855 20.134  11.302  1.00 34.35  ? 112 ASP D N   1 
ATOM   11192 C CA  . ASP F 2 112 ? -30.889 19.201  10.875  1.00 42.11  ? 112 ASP D CA  1 
ATOM   11193 C C   . ASP F 2 112 ? -32.117 19.326  11.768  1.00 45.75  ? 112 ASP D C   1 
ATOM   11194 O O   . ASP F 2 112 ? -33.245 19.437  11.277  1.00 49.97  ? 112 ASP D O   1 
ATOM   11195 C CB  . ASP F 2 112 ? -30.375 17.755  10.907  1.00 47.77  ? 112 ASP D CB  1 
ATOM   11196 C CG  . ASP F 2 112 ? -29.485 17.416  9.723   1.00 63.62  ? 112 ASP D CG  1 
ATOM   11197 O OD1 . ASP F 2 112 ? -29.314 18.272  8.821   1.00 73.25  ? 112 ASP D OD1 1 
ATOM   11198 O OD2 . ASP F 2 112 ? -28.957 16.278  9.695   1.00 76.29  ? 112 ASP D OD2 1 
ATOM   11199 N N   . SER F 2 113 ? -31.886 19.322  13.078  1.00 44.41  ? 113 SER D N   1 
ATOM   11200 C CA  . SER F 2 113 ? -32.970 19.375  14.050  1.00 47.70  ? 113 SER D CA  1 
ATOM   11201 C C   . SER F 2 113 ? -33.784 20.663  13.935  1.00 42.75  ? 113 SER D C   1 
ATOM   11202 O O   . SER F 2 113 ? -35.001 20.629  14.049  1.00 39.75  ? 113 SER D O   1 
ATOM   11203 C CB  . SER F 2 113 ? -32.416 19.228  15.473  1.00 48.38  ? 113 SER D CB  1 
ATOM   11204 O OG  . SER F 2 113 ? -33.453 18.868  16.368  1.00 45.89  ? 113 SER D OG  1 
ATOM   11205 N N   . ASN F 2 114 ? -33.108 21.786  13.703  1.00 45.11  ? 114 ASN D N   1 
ATOM   11206 C CA  . ASN F 2 114 ? -33.774 23.083  13.589  1.00 47.26  ? 114 ASN D CA  1 
ATOM   11207 C C   . ASN F 2 114 ? -34.672 23.188  12.355  1.00 50.07  ? 114 ASN D C   1 
ATOM   11208 O O   . ASN F 2 114 ? -35.757 23.752  12.424  1.00 53.78  ? 114 ASN D O   1 
ATOM   11209 C CB  . ASN F 2 114 ? -32.742 24.221  13.592  1.00 50.39  ? 114 ASN D CB  1 
ATOM   11210 C CG  . ASN F 2 114 ? -32.092 24.411  14.948  1.00 50.37  ? 114 ASN D CG  1 
ATOM   11211 O OD1 . ASN F 2 114 ? -32.683 24.110  15.980  1.00 57.72  ? 114 ASN D OD1 1 
ATOM   11212 N ND2 . ASN F 2 114 ? -30.871 24.931  14.950  1.00 50.94  ? 114 ASN D ND2 1 
ATOM   11213 N N   . VAL F 2 115 ? -34.223 22.636  11.236  1.00 47.17  ? 115 VAL D N   1 
ATOM   11214 C CA  . VAL F 2 115 ? -35.017 22.623  10.009  1.00 47.20  ? 115 VAL D CA  1 
ATOM   11215 C C   . VAL F 2 115 ? -36.285 21.774  10.194  1.00 47.11  ? 115 VAL D C   1 
ATOM   11216 O O   . VAL F 2 115 ? -37.389 22.184  9.808   1.00 47.28  ? 115 VAL D O   1 
ATOM   11217 C CB  . VAL F 2 115 ? -34.163 22.108  8.822   1.00 47.26  ? 115 VAL D CB  1 
ATOM   11218 C CG1 . VAL F 2 115 ? -35.025 21.809  7.605   1.00 44.79  ? 115 VAL D CG1 1 
ATOM   11219 C CG2 . VAL F 2 115 ? -33.088 23.121  8.469   1.00 44.52  ? 115 VAL D CG2 1 
ATOM   11220 N N   . ARG F 2 116 ? -36.119 20.600  10.794  1.00 48.47  ? 116 ARG D N   1 
ATOM   11221 C CA  . ARG F 2 116 ? -37.244 19.692  11.084  1.00 51.62  ? 116 ARG D CA  1 
ATOM   11222 C C   . ARG F 2 116 ? -38.291 20.336  12.000  1.00 50.31  ? 116 ARG D C   1 
ATOM   11223 O O   . ARG F 2 116 ? -39.498 20.193  11.759  1.00 55.00  ? 116 ARG D O   1 
ATOM   11224 C CB  . ARG F 2 116 ? -36.718 18.349  11.629  1.00 55.94  ? 116 ARG D CB  1 
ATOM   11225 C CG  . ARG F 2 116 ? -36.246 17.450  10.503  1.00 65.92  ? 116 ARG D CG  1 
ATOM   11226 C CD  . ARG F 2 116 ? -35.819 16.072  10.972  1.00 76.15  ? 116 ARG D CD  1 
ATOM   11227 N NE  . ARG F 2 116 ? -35.193 15.360  9.851   1.00 86.05  ? 116 ARG D NE  1 
ATOM   11228 C CZ  . ARG F 2 116 ? -34.226 14.448  9.951   1.00 108.00 ? 116 ARG D CZ  1 
ATOM   11229 N NH1 . ARG F 2 116 ? -33.743 14.076  11.133  1.00 121.69 ? 116 ARG D NH1 1 
ATOM   11230 N NH2 . ARG F 2 116 ? -33.738 13.890  8.844   1.00 113.69 ? 116 ARG D NH2 1 
ATOM   11231 N N   . ASN F 2 117 ? -37.839 21.087  13.003  1.00 43.74  ? 117 ASN D N   1 
ATOM   11232 C CA  . ASN F 2 117 ? -38.753 21.802  13.882  1.00 49.11  ? 117 ASN D CA  1 
ATOM   11233 C C   . ASN F 2 117 ? -39.555 22.851  13.127  1.00 49.60  ? 117 ASN D C   1 
ATOM   11234 O O   . ASN F 2 117 ? -40.746 23.047  13.388  1.00 47.29  ? 117 ASN D O   1 
ATOM   11235 C CB  . ASN F 2 117 ? -37.991 22.489  15.024  1.00 56.28  ? 117 ASN D CB  1 
ATOM   11236 C CG  . ASN F 2 117 ? -37.339 21.502  15.985  1.00 61.19  ? 117 ASN D CG  1 
ATOM   11237 O OD1 . ASN F 2 117 ? -36.414 21.860  16.716  1.00 60.22  ? 117 ASN D OD1 1 
ATOM   11238 N ND2 . ASN F 2 117 ? -37.798 20.251  15.972  1.00 61.97  ? 117 ASN D ND2 1 
ATOM   11239 N N   . LEU F 2 118 ? -38.884 23.534  12.206  1.00 50.32  ? 118 LEU D N   1 
ATOM   11240 C CA  . LEU F 2 118 ? -39.516 24.557  11.380  1.00 46.67  ? 118 LEU D CA  1 
ATOM   11241 C C   . LEU F 2 118 ? -40.586 23.915  10.486  1.00 44.57  ? 118 LEU D C   1 
ATOM   11242 O O   . LEU F 2 118 ? -41.668 24.467  10.304  1.00 43.92  ? 118 LEU D O   1 
ATOM   11243 C CB  . LEU F 2 118 ? -38.454 25.275  10.536  1.00 48.26  ? 118 LEU D CB  1 
ATOM   11244 C CG  . LEU F 2 118 ? -38.611 26.767  10.272  1.00 54.05  ? 118 LEU D CG  1 
ATOM   11245 C CD1 . LEU F 2 118 ? -38.418 27.561  11.556  1.00 50.39  ? 118 LEU D CD1 1 
ATOM   11246 C CD2 . LEU F 2 118 ? -37.619 27.214  9.206   1.00 54.46  ? 118 LEU D CD2 1 
ATOM   11247 N N   . TYR F 2 119 ? -40.280 22.734  9.958   1.00 44.28  ? 119 TYR D N   1 
ATOM   11248 C CA  . TYR F 2 119 ? -41.215 21.993  9.120   1.00 46.80  ? 119 TYR D CA  1 
ATOM   11249 C C   . TYR F 2 119 ? -42.436 21.510  9.902   1.00 53.31  ? 119 TYR D C   1 
ATOM   11250 O O   . TYR F 2 119 ? -43.554 21.521  9.387   1.00 61.22  ? 119 TYR D O   1 
ATOM   11251 C CB  . TYR F 2 119 ? -40.512 20.796  8.482   1.00 45.65  ? 119 TYR D CB  1 
ATOM   11252 C CG  . TYR F 2 119 ? -41.417 19.965  7.578   1.00 49.93  ? 119 TYR D CG  1 
ATOM   11253 C CD1 . TYR F 2 119 ? -41.653 20.338  6.251   1.00 52.33  ? 119 TYR D CD1 1 
ATOM   11254 C CD2 . TYR F 2 119 ? -42.037 18.812  8.050   1.00 52.12  ? 119 TYR D CD2 1 
ATOM   11255 C CE1 . TYR F 2 119 ? -42.473 19.581  5.416   1.00 53.55  ? 119 TYR D CE1 1 
ATOM   11256 C CE2 . TYR F 2 119 ? -42.864 18.051  7.222   1.00 55.17  ? 119 TYR D CE2 1 
ATOM   11257 C CZ  . TYR F 2 119 ? -43.079 18.439  5.908   1.00 56.55  ? 119 TYR D CZ  1 
ATOM   11258 O OH  . TYR F 2 119 ? -43.898 17.693  5.076   1.00 50.76  ? 119 TYR D OH  1 
ATOM   11259 N N   . ASP F 2 120 ? -42.222 21.077  11.140  1.00 61.51  ? 120 ASP D N   1 
ATOM   11260 C CA  . ASP F 2 120 ? -43.316 20.566  11.971  1.00 61.75  ? 120 ASP D CA  1 
ATOM   11261 C C   . ASP F 2 120 ? -44.245 21.681  12.462  1.00 54.25  ? 120 ASP D C   1 
ATOM   11262 O O   . ASP F 2 120 ? -45.459 21.486  12.523  1.00 51.49  ? 120 ASP D O   1 
ATOM   11263 C CB  . ASP F 2 120 ? -42.774 19.746  13.150  1.00 63.79  ? 120 ASP D CB  1 
ATOM   11264 C CG  . ASP F 2 120 ? -42.269 18.364  12.723  1.00 69.80  ? 120 ASP D CG  1 
ATOM   11265 O OD1 . ASP F 2 120 ? -42.964 17.675  11.945  1.00 64.81  ? 120 ASP D OD1 1 
ATOM   11266 O OD2 . ASP F 2 120 ? -41.179 17.958  13.177  1.00 74.67  ? 120 ASP D OD2 1 
ATOM   11267 N N   . LYS F 2 121 ? -43.681 22.844  12.788  1.00 49.26  ? 121 LYS D N   1 
ATOM   11268 C CA  . LYS F 2 121 ? -44.483 24.016  13.159  1.00 51.94  ? 121 LYS D CA  1 
ATOM   11269 C C   . LYS F 2 121 ? -45.471 24.388  12.051  1.00 55.61  ? 121 LYS D C   1 
ATOM   11270 O O   . LYS F 2 121 ? -46.599 24.802  12.327  1.00 57.91  ? 121 LYS D O   1 
ATOM   11271 C CB  . LYS F 2 121 ? -43.578 25.210  13.485  1.00 53.84  ? 121 LYS D CB  1 
ATOM   11272 C CG  . LYS F 2 121 ? -43.037 25.199  14.906  1.00 63.91  ? 121 LYS D CG  1 
ATOM   11273 C CD  . LYS F 2 121 ? -42.188 26.433  15.196  1.00 74.32  ? 121 LYS D CD  1 
ATOM   11274 C CE  . LYS F 2 121 ? -41.806 26.558  16.671  1.00 80.04  ? 121 LYS D CE  1 
ATOM   11275 N NZ  . LYS F 2 121 ? -41.009 25.400  17.164  1.00 89.02  ? 121 LYS D NZ  1 
ATOM   11276 N N   . VAL F 2 122 ? -45.043 24.229  10.801  1.00 55.96  ? 122 VAL D N   1 
ATOM   11277 C CA  . VAL F 2 122 ? -45.919 24.450  9.663   1.00 50.18  ? 122 VAL D CA  1 
ATOM   11278 C C   . VAL F 2 122 ? -46.948 23.329  9.531   1.00 48.98  ? 122 VAL D C   1 
ATOM   11279 O O   . VAL F 2 122 ? -48.141 23.594  9.418   1.00 51.16  ? 122 VAL D O   1 
ATOM   11280 C CB  . VAL F 2 122 ? -45.119 24.575  8.351   1.00 47.48  ? 122 VAL D CB  1 
ATOM   11281 C CG1 . VAL F 2 122 ? -46.027 24.387  7.143   1.00 43.76  ? 122 VAL D CG1 1 
ATOM   11282 C CG2 . VAL F 2 122 ? -44.415 25.922  8.305   1.00 44.34  ? 122 VAL D CG2 1 
ATOM   11283 N N   . ARG F 2 123 ? -46.478 22.086  9.548   1.00 51.37  ? 123 ARG D N   1 
ATOM   11284 C CA  . ARG F 2 123 ? -47.350 20.929  9.376   1.00 53.87  ? 123 ARG D CA  1 
ATOM   11285 C C   . ARG F 2 123 ? -48.521 20.912  10.357  1.00 56.40  ? 123 ARG D C   1 
ATOM   11286 O O   . ARG F 2 123 ? -49.659 20.645  9.971   1.00 58.09  ? 123 ARG D O   1 
ATOM   11287 C CB  . ARG F 2 123 ? -46.545 19.633  9.501   1.00 20.00  ? 123 ARG D CB  1 
ATOM   11288 C CG  . ARG F 2 123 ? -47.352 18.448  10.008  1.00 20.00  ? 123 ARG D CG  1 
ATOM   11289 C CD  . ARG F 2 123 ? -46.883 17.149  9.375   1.00 20.00  ? 123 ARG D CD  1 
ATOM   11290 N NE  . ARG F 2 123 ? -46.132 16.321  10.315  1.00 20.00  ? 123 ARG D NE  1 
ATOM   11291 C CZ  . ARG F 2 123 ? -46.637 15.271  10.953  1.00 20.00  ? 123 ARG D CZ  1 
ATOM   11292 N NH1 . ARG F 2 123 ? -47.899 14.914  10.754  1.00 20.00  ? 123 ARG D NH1 1 
ATOM   11293 N NH2 . ARG F 2 123 ? -45.881 14.575  11.792  1.00 20.00  ? 123 ARG D NH2 1 
ATOM   11294 N N   . LEU F 2 124 ? -48.237 21.192  11.625  1.00 60.26  ? 124 LEU D N   1 
ATOM   11295 C CA  . LEU F 2 124 ? -49.261 21.132  12.672  1.00 64.71  ? 124 LEU D CA  1 
ATOM   11296 C C   . LEU F 2 124 ? -50.291 22.264  12.581  1.00 63.65  ? 124 LEU D C   1 
ATOM   11297 O O   . LEU F 2 124 ? -51.353 22.184  13.197  1.00 58.41  ? 124 LEU D O   1 
ATOM   11298 C CB  . LEU F 2 124 ? -48.598 21.094  14.051  1.00 68.51  ? 124 LEU D CB  1 
ATOM   11299 C CG  . LEU F 2 124 ? -48.091 19.683  14.439  1.00 77.42  ? 124 LEU D CG  1 
ATOM   11300 C CD1 . LEU F 2 124 ? -47.530 18.882  13.264  1.00 72.94  ? 124 LEU D CD1 1 
ATOM   11301 C CD2 . LEU F 2 124 ? -47.044 19.771  15.547  1.00 74.82  ? 124 LEU D CD2 1 
ATOM   11302 N N   . GLN F 2 125 ? -49.981 23.306  11.812  1.00 59.78  ? 125 GLN D N   1 
ATOM   11303 C CA  . GLN F 2 125 ? -50.950 24.367  11.538  1.00 58.25  ? 125 GLN D CA  1 
ATOM   11304 C C   . GLN F 2 125 ? -51.863 23.994  10.368  1.00 63.12  ? 125 GLN D C   1 
ATOM   11305 O O   . GLN F 2 125 ? -53.101 23.993  10.486  1.00 62.00  ? 125 GLN D O   1 
ATOM   11306 C CB  . GLN F 2 125 ? -50.241 25.686  11.235  1.00 54.70  ? 125 GLN D CB  1 
ATOM   11307 C CG  . GLN F 2 125 ? -49.637 26.364  12.449  1.00 51.93  ? 125 GLN D CG  1 
ATOM   11308 C CD  . GLN F 2 125 ? -48.837 27.606  12.081  1.00 52.25  ? 125 GLN D CD  1 
ATOM   11309 O OE1 . GLN F 2 125 ? -49.307 28.729  12.233  1.00 54.28  ? 125 GLN D OE1 1 
ATOM   11310 N NE2 . GLN F 2 125 ? -47.631 27.403  11.567  1.00 55.93  ? 125 GLN D NE2 1 
ATOM   11311 N N   . LEU F 2 126 ? -51.236 23.666  9.241   1.00 67.08  ? 126 LEU D N   1 
ATOM   11312 C CA  . LEU F 2 126 ? -51.965 23.324  8.031   1.00 69.98  ? 126 LEU D CA  1 
ATOM   11313 C C   . LEU F 2 126 ? -52.189 21.816  8.118   1.00 78.50  ? 126 LEU D C   1 
ATOM   11314 O O   . LEU F 2 126 ? -51.352 21.043  7.656   1.00 99.33  ? 126 LEU D O   1 
ATOM   11315 C CB  . LEU F 2 126 ? -51.186 23.652  6.740   1.00 65.07  ? 126 LEU D CB  1 
ATOM   11316 C CG  . LEU F 2 126 ? -50.089 24.718  6.719   1.00 57.97  ? 126 LEU D CG  1 
ATOM   11317 C CD1 . LEU F 2 126 ? -49.431 24.752  5.348   1.00 51.48  ? 126 LEU D CD1 1 
ATOM   11318 C CD2 . LEU F 2 126 ? -50.618 26.091  7.097   1.00 53.84  ? 126 LEU D CD2 1 
ATOM   11319 N N   . LYS F 2 127 ? -53.309 21.422  8.667   1.00 75.79  ? 127 LYS D N   1 
ATOM   11320 C CA  . LYS F 2 127 ? -53.550 20.025  8.781   1.00 74.65  ? 127 LYS D CA  1 
ATOM   11321 C C   . LYS F 2 127 ? -53.941 19.543  7.414   1.00 70.91  ? 127 LYS D C   1 
ATOM   11322 O O   . LYS F 2 127 ? -53.119 19.473  6.539   1.00 67.58  ? 127 LYS D O   1 
ATOM   11323 C CB  . LYS F 2 127 ? -54.606 19.787  9.836   1.00 20.00  ? 127 LYS D CB  1 
ATOM   11324 C CG  . LYS F 2 127 ? -54.276 20.485  11.137  1.00 20.00  ? 127 LYS D CG  1 
ATOM   11325 C CD  . LYS F 2 127 ? -55.509 20.973  11.866  1.00 20.00  ? 127 LYS D CD  1 
ATOM   11326 C CE  . LYS F 2 127 ? -55.281 22.255  12.654  1.00 20.00  ? 127 LYS D CE  1 
ATOM   11327 N NZ  . LYS F 2 127 ? -54.665 22.082  13.992  1.00 20.00  ? 127 LYS D NZ  1 
ATOM   11328 N N   . ASP F 2 128 ? -55.204 19.237  7.220   1.00 71.20  ? 128 ASP D N   1 
ATOM   11329 C CA  . ASP F 2 128 ? -55.673 18.703  5.937   1.00 68.73  ? 128 ASP D CA  1 
ATOM   11330 C C   . ASP F 2 128 ? -55.990 19.838  4.947   1.00 67.61  ? 128 ASP D C   1 
ATOM   11331 O O   . ASP F 2 128 ? -56.532 19.592  3.877   1.00 69.16  ? 128 ASP D O   1 
ATOM   11332 C CB  . ASP F 2 128 ? -56.885 17.767  6.121   1.00 71.08  ? 128 ASP D CB  1 
ATOM   11333 C CG  . ASP F 2 128 ? -58.006 18.399  6.920   1.00 69.46  ? 128 ASP D CG  1 
ATOM   11334 O OD1 . ASP F 2 128 ? -58.019 19.642  7.052   1.00 67.25  ? 128 ASP D OD1 1 
ATOM   11335 O OD2 . ASP F 2 128 ? -58.870 17.645  7.413   1.00 70.50  ? 128 ASP D OD2 1 
ATOM   11336 N N   . ASN F 2 129 ? -55.668 21.078  5.315   1.00 62.56  ? 129 ASN D N   1 
ATOM   11337 C CA  . ASN F 2 129 ? -55.808 22.218  4.407   1.00 55.65  ? 129 ASN D CA  1 
ATOM   11338 C C   . ASN F 2 129 ? -54.682 22.295  3.387   1.00 57.67  ? 129 ASN D C   1 
ATOM   11339 O O   . ASN F 2 129 ? -54.765 23.079  2.439   1.00 60.58  ? 129 ASN D O   1 
ATOM   11340 C CB  . ASN F 2 129 ? -55.895 23.537  5.185   1.00 56.14  ? 129 ASN D CB  1 
ATOM   11341 C CG  . ASN F 2 129 ? -57.240 23.728  5.852   1.00 57.62  ? 129 ASN D CG  1 
ATOM   11342 O OD1 . ASN F 2 129 ? -58.096 22.843  5.819   1.00 65.63  ? 129 ASN D OD1 1 
ATOM   11343 N ND2 . ASN F 2 129 ? -57.432 24.885  6.469   1.00 57.92  ? 129 ASN D ND2 1 
ATOM   11344 N N   . ALA F 2 130 ? -53.629 21.499  3.578   1.00 58.60  ? 130 ALA D N   1 
ATOM   11345 C CA  . ALA F 2 130 ? -52.570 21.400  2.583   1.00 55.18  ? 130 ALA D CA  1 
ATOM   11346 C C   . ALA F 2 130 ? -51.987 19.994  2.503   1.00 52.55  ? 130 ALA D C   1 
ATOM   11347 O O   . ALA F 2 130 ? -52.001 19.236  3.467   1.00 54.51  ? 130 ALA D O   1 
ATOM   11348 C CB  . ALA F 2 130 ? -51.472 22.416  2.866   1.00 49.59  ? 130 ALA D CB  1 
ATOM   11349 N N   . LYS F 2 131 ? -51.463 19.672  1.331   1.00 54.87  ? 131 LYS D N   1 
ATOM   11350 C CA  . LYS F 2 131 ? -50.918 18.354  1.039   1.00 58.74  ? 131 LYS D CA  1 
ATOM   11351 C C   . LYS F 2 131 ? -49.402 18.342  1.233   1.00 60.18  ? 131 LYS D C   1 
ATOM   11352 O O   . LYS F 2 131 ? -48.696 19.073  0.539   1.00 59.42  ? 131 LYS D O   1 
ATOM   11353 C CB  . LYS F 2 131 ? -51.249 17.995  -0.409  1.00 59.79  ? 131 LYS D CB  1 
ATOM   11354 C CG  . LYS F 2 131 ? -50.744 16.649  -0.871  1.00 62.95  ? 131 LYS D CG  1 
ATOM   11355 C CD  . LYS F 2 131 ? -51.210 16.311  -2.279  1.00 65.73  ? 131 LYS D CD  1 
ATOM   11356 C CE  . LYS F 2 131 ? -50.068 15.782  -3.139  1.00 66.57  ? 131 LYS D CE  1 
ATOM   11357 N NZ  . LYS F 2 131 ? -50.557 14.979  -4.291  1.00 66.37  ? 131 LYS D NZ  1 
ATOM   11358 N N   . GLU F 2 132 ? -48.909 17.526  2.170   1.00 57.65  ? 132 GLU D N   1 
ATOM   11359 C CA  . GLU F 2 132 ? -47.467 17.313  2.331   1.00 56.60  ? 132 GLU D CA  1 
ATOM   11360 C C   . GLU F 2 132 ? -46.895 16.649  1.084   1.00 61.51  ? 132 GLU D C   1 
ATOM   11361 O O   . GLU F 2 132 ? -47.135 15.472  0.824   1.00 77.47  ? 132 GLU D O   1 
ATOM   11362 C CB  . GLU F 2 132 ? -47.164 16.456  3.565   1.00 56.48  ? 132 GLU D CB  1 
ATOM   11363 C CG  . GLU F 2 132 ? -47.170 17.231  4.872   1.00 66.19  ? 132 GLU D CG  1 
ATOM   11364 C CD  . GLU F 2 132 ? -47.033 16.332  6.085   1.00 66.60  ? 132 GLU D CD  1 
ATOM   11365 O OE1 . GLU F 2 132 ? -45.930 16.278  6.672   1.00 77.27  ? 132 GLU D OE1 1 
ATOM   11366 O OE2 . GLU F 2 132 ? -48.029 15.671  6.442   1.00 62.05  ? 132 GLU D OE2 1 
ATOM   11367 N N   . LEU F 2 133 ? -46.142 17.405  0.300   1.00 60.34  ? 133 LEU D N   1 
ATOM   11368 C CA  . LEU F 2 133 ? -45.564 16.849  -0.931  1.00 65.02  ? 133 LEU D CA  1 
ATOM   11369 C C   . LEU F 2 133 ? -44.464 15.822  -0.697  1.00 68.54  ? 133 LEU D C   1 
ATOM   11370 O O   . LEU F 2 133 ? -44.101 15.100  -1.618  1.00 66.31  ? 133 LEU D O   1 
ATOM   11371 C CB  . LEU F 2 133 ? -45.039 17.953  -1.853  1.00 66.52  ? 133 LEU D CB  1 
ATOM   11372 C CG  . LEU F 2 133 ? -46.153 18.593  -2.675  1.00 64.67  ? 133 LEU D CG  1 
ATOM   11373 C CD1 . LEU F 2 133 ? -45.729 19.960  -3.193  1.00 61.11  ? 133 LEU D CD1 1 
ATOM   11374 C CD2 . LEU F 2 133 ? -46.594 17.685  -3.823  1.00 74.75  ? 133 LEU D CD2 1 
ATOM   11375 N N   . GLY F 2 134 ? -43.927 15.770  0.518   1.00 70.13  ? 134 GLY D N   1 
ATOM   11376 C CA  . GLY F 2 134 ? -42.894 14.790  0.857   1.00 69.43  ? 134 GLY D CA  1 
ATOM   11377 C C   . GLY F 2 134 ? -41.465 15.229  0.574   1.00 68.32  ? 134 GLY D C   1 
ATOM   11378 O O   . GLY F 2 134 ? -40.531 14.452  0.783   1.00 64.79  ? 134 GLY D O   1 
ATOM   11379 N N   . ASN F 2 135 ? -41.289 16.466  0.107   1.00 60.26  ? 135 ASN D N   1 
ATOM   11380 C CA  . ASN F 2 135 ? -39.952 17.035  -0.106  1.00 59.40  ? 135 ASN D CA  1 
ATOM   11381 C C   . ASN F 2 135 ? -39.691 18.335  0.682   1.00 53.26  ? 135 ASN D C   1 
ATOM   11382 O O   . ASN F 2 135 ? -38.826 19.120  0.308   1.00 58.10  ? 135 ASN D O   1 
ATOM   11383 C CB  . ASN F 2 135 ? -39.689 17.235  -1.609  1.00 63.84  ? 135 ASN D CB  1 
ATOM   11384 C CG  . ASN F 2 135 ? -40.796 18.021  -2.308  1.00 64.23  ? 135 ASN D CG  1 
ATOM   11385 O OD1 . ASN F 2 135 ? -41.771 18.483  -1.684  1.00 62.36  ? 135 ASN D OD1 1 
ATOM   11386 N ND2 . ASN F 2 135 ? -40.657 18.164  -3.621  1.00 60.96  ? 135 ASN D ND2 1 
ATOM   11387 N N   . GLY F 2 136 ? -40.413 18.540  1.785   1.00 48.26  ? 136 GLY D N   1 
ATOM   11388 C CA  . GLY F 2 136 ? -40.296 19.763  2.590   1.00 44.62  ? 136 GLY D CA  1 
ATOM   11389 C C   . GLY F 2 136 ? -41.290 20.857  2.221   1.00 47.92  ? 136 GLY D C   1 
ATOM   11390 O O   . GLY F 2 136 ? -41.324 21.917  2.865   1.00 47.41  ? 136 GLY D O   1 
ATOM   11391 N N   . CYS F 2 137 ? -42.099 20.606  1.192   1.00 47.84  ? 137 CYS D N   1 
ATOM   11392 C CA  . CYS F 2 137 ? -43.066 21.591  0.699   1.00 52.05  ? 137 CYS D CA  1 
ATOM   11393 C C   . CYS F 2 137 ? -44.500 21.174  0.975   1.00 47.22  ? 137 CYS D C   1 
ATOM   11394 O O   . CYS F 2 137 ? -44.822 19.989  0.979   1.00 46.98  ? 137 CYS D O   1 
ATOM   11395 C CB  . CYS F 2 137 ? -42.890 21.806  -0.808  1.00 56.62  ? 137 CYS D CB  1 
ATOM   11396 S SG  . CYS F 2 137 ? -41.277 22.490  -1.251  1.00 67.43  ? 137 CYS D SG  1 
ATOM   11397 N N   . PHE F 2 138 ? -45.354 22.168  1.187   1.00 48.91  ? 138 PHE D N   1 
ATOM   11398 C CA  . PHE F 2 138 ? -46.782 21.958  1.359   1.00 51.04  ? 138 PHE D CA  1 
ATOM   11399 C C   . PHE F 2 138 ? -47.519 22.595  0.189   1.00 52.13  ? 138 PHE D C   1 
ATOM   11400 O O   . PHE F 2 138 ? -47.304 23.767  -0.105  1.00 55.55  ? 138 PHE D O   1 
ATOM   11401 C CB  . PHE F 2 138 ? -47.256 22.614  2.656   1.00 52.04  ? 138 PHE D CB  1 
ATOM   11402 C CG  . PHE F 2 138 ? -46.604 22.064  3.892   1.00 53.16  ? 138 PHE D CG  1 
ATOM   11403 C CD1 . PHE F 2 138 ? -45.377 22.546  4.317   1.00 52.94  ? 138 PHE D CD1 1 
ATOM   11404 C CD2 . PHE F 2 138 ? -47.225 21.073  4.636   1.00 53.58  ? 138 PHE D CD2 1 
ATOM   11405 C CE1 . PHE F 2 138 ? -44.779 22.046  5.459   1.00 57.06  ? 138 PHE D CE1 1 
ATOM   11406 C CE2 . PHE F 2 138 ? -46.632 20.572  5.781   1.00 54.83  ? 138 PHE D CE2 1 
ATOM   11407 C CZ  . PHE F 2 138 ? -45.408 21.060  6.195   1.00 54.24  ? 138 PHE D CZ  1 
ATOM   11408 N N   . GLU F 2 139 ? -48.376 21.825  -0.479  1.00 58.28  ? 139 GLU D N   1 
ATOM   11409 C CA  . GLU F 2 139 ? -49.276 22.370  -1.497  1.00 57.14  ? 139 GLU D CA  1 
ATOM   11410 C C   . GLU F 2 139 ? -50.613 22.684  -0.846  1.00 54.74  ? 139 GLU D C   1 
ATOM   11411 O O   . GLU F 2 139 ? -51.264 21.794  -0.306  1.00 59.53  ? 139 GLU D O   1 
ATOM   11412 C CB  . GLU F 2 139 ? -49.468 21.381  -2.655  1.00 65.44  ? 139 GLU D CB  1 
ATOM   11413 C CG  . GLU F 2 139 ? -50.290 21.932  -3.820  1.00 69.50  ? 139 GLU D CG  1 
ATOM   11414 C CD  . GLU F 2 139 ? -50.431 20.963  -4.987  1.00 80.15  ? 139 GLU D CD  1 
ATOM   11415 O OE1 . GLU F 2 139 ? -49.978 19.801  -4.882  1.00 93.79  ? 139 GLU D OE1 1 
ATOM   11416 O OE2 . GLU F 2 139 ? -51.006 21.366  -6.023  1.00 78.45  ? 139 GLU D OE2 1 
ATOM   11417 N N   . PHE F 2 140 ? -51.018 23.948  -0.898  1.00 54.31  ? 140 PHE D N   1 
ATOM   11418 C CA  . PHE F 2 140 ? -52.286 24.373  -0.312  1.00 54.26  ? 140 PHE D CA  1 
ATOM   11419 C C   . PHE F 2 140 ? -53.478 23.932  -1.154  1.00 56.41  ? 140 PHE D C   1 
ATOM   11420 O O   . PHE F 2 140 ? -53.414 23.939  -2.384  1.00 58.14  ? 140 PHE D O   1 
ATOM   11421 C CB  . PHE F 2 140 ? -52.326 25.888  -0.164  1.00 54.56  ? 140 PHE D CB  1 
ATOM   11422 C CG  . PHE F 2 140 ? -51.494 26.405  0.964   1.00 53.09  ? 140 PHE D CG  1 
ATOM   11423 C CD1 . PHE F 2 140 ? -50.178 26.795  0.756   1.00 51.40  ? 140 PHE D CD1 1 
ATOM   11424 C CD2 . PHE F 2 140 ? -52.033 26.517  2.233   1.00 51.86  ? 140 PHE D CD2 1 
ATOM   11425 C CE1 . PHE F 2 140 ? -49.412 27.286  1.797   1.00 52.21  ? 140 PHE D CE1 1 
ATOM   11426 C CE2 . PHE F 2 140 ? -51.274 27.008  3.279   1.00 49.27  ? 140 PHE D CE2 1 
ATOM   11427 C CZ  . PHE F 2 140 ? -49.961 27.389  3.064   1.00 50.62  ? 140 PHE D CZ  1 
ATOM   11428 N N   . TYR F 2 141 ? -54.563 23.559  -0.478  1.00 56.45  ? 141 TYR D N   1 
ATOM   11429 C CA  . TYR F 2 141 ? -55.826 23.209  -1.135  1.00 56.62  ? 141 TYR D CA  1 
ATOM   11430 C C   . TYR F 2 141 ? -56.730 24.430  -1.301  1.00 64.13  ? 141 TYR D C   1 
ATOM   11431 O O   . TYR F 2 141 ? -57.828 24.321  -1.845  1.00 74.34  ? 141 TYR D O   1 
ATOM   11432 C CB  . TYR F 2 141 ? -56.570 22.141  -0.329  1.00 55.49  ? 141 TYR D CB  1 
ATOM   11433 C CG  . TYR F 2 141 ? -55.973 20.748  -0.380  1.00 53.33  ? 141 TYR D CG  1 
ATOM   11434 C CD1 . TYR F 2 141 ? -55.666 20.133  -1.596  1.00 53.34  ? 141 TYR D CD1 1 
ATOM   11435 C CD2 . TYR F 2 141 ? -55.766 20.026  0.791   1.00 53.45  ? 141 TYR D CD2 1 
ATOM   11436 C CE1 . TYR F 2 141 ? -55.146 18.849  -1.641  1.00 56.51  ? 141 TYR D CE1 1 
ATOM   11437 C CE2 . TYR F 2 141 ? -55.246 18.746  0.762   1.00 56.17  ? 141 TYR D CE2 1 
ATOM   11438 C CZ  . TYR F 2 141 ? -54.942 18.159  -0.453  1.00 58.87  ? 141 TYR D CZ  1 
ATOM   11439 O OH  . TYR F 2 141 ? -54.438 16.883  -0.465  1.00 60.48  ? 141 TYR D OH  1 
ATOM   11440 N N   . HIS F 2 142 ? -56.280 25.583  -0.814  1.00 62.90  ? 142 HIS D N   1 
ATOM   11441 C CA  . HIS F 2 142 ? -57.008 26.836  -0.993  1.00 59.22  ? 142 HIS D CA  1 
ATOM   11442 C C   . HIS F 2 142 ? -56.077 27.929  -1.439  1.00 60.66  ? 142 HIS D C   1 
ATOM   11443 O O   . HIS F 2 142 ? -54.860 27.740  -1.476  1.00 63.05  ? 142 HIS D O   1 
ATOM   11444 C CB  . HIS F 2 142 ? -57.698 27.229  0.306   1.00 56.15  ? 142 HIS D CB  1 
ATOM   11445 C CG  . HIS F 2 142 ? -56.744 27.587  1.413   1.00 52.31  ? 142 HIS D CG  1 
ATOM   11446 N ND1 . HIS F 2 142 ? -56.192 26.663  2.216   1.00 57.17  ? 142 HIS D ND1 1 
ATOM   11447 C CD2 . HIS F 2 142 ? -56.241 28.816  1.822   1.00 50.92  ? 142 HIS D CD2 1 
ATOM   11448 C CE1 . HIS F 2 142 ? -55.382 27.273  3.100   1.00 57.03  ? 142 HIS D CE1 1 
ATOM   11449 N NE2 . HIS F 2 142 ? -55.416 28.589  2.858   1.00 51.87  ? 142 HIS D NE2 1 
ATOM   11450 N N   . LYS F 2 143 ? -56.649 29.078  -1.787  1.00 67.27  ? 143 LYS D N   1 
ATOM   11451 C CA  . LYS F 2 143 ? -55.867 30.243  -2.193  1.00 76.16  ? 143 LYS D CA  1 
ATOM   11452 C C   . LYS F 2 143 ? -55.238 30.912  -0.968  1.00 70.35  ? 143 LYS D C   1 
ATOM   11453 O O   . LYS F 2 143 ? -55.941 31.465  -0.123  1.00 59.47  ? 143 LYS D O   1 
ATOM   11454 C CB  . LYS F 2 143 ? -56.740 31.252  -2.962  1.00 83.05  ? 143 LYS D CB  1 
ATOM   11455 C CG  . LYS F 2 143 ? -57.215 30.784  -4.339  1.00 86.22  ? 143 LYS D CG  1 
ATOM   11456 C CD  . LYS F 2 143 ? -58.500 31.501  -4.785  1.00 94.94  ? 143 LYS D CD  1 
ATOM   11457 C CE  . LYS F 2 143 ? -58.243 32.893  -5.354  1.00 101.99 ? 143 LYS D CE  1 
ATOM   11458 N NZ  . LYS F 2 143 ? -57.421 32.852  -6.594  1.00 107.98 ? 143 LYS D NZ  1 
ATOM   11459 N N   . CYS F 2 144 ? -53.912 30.857  -0.883  1.00 69.28  ? 144 CYS D N   1 
ATOM   11460 C CA  . CYS F 2 144 ? -53.178 31.430  0.239   1.00 66.71  ? 144 CYS D CA  1 
ATOM   11461 C C   . CYS F 2 144 ? -52.381 32.645  -0.234  1.00 65.55  ? 144 CYS D C   1 
ATOM   11462 O O   . CYS F 2 144 ? -51.345 32.508  -0.890  1.00 62.27  ? 144 CYS D O   1 
ATOM   11463 C CB  . CYS F 2 144 ? -52.252 30.377  0.861   1.00 71.53  ? 144 CYS D CB  1 
ATOM   11464 S SG  . CYS F 2 144 ? -51.388 30.910  2.359   1.00 79.21  ? 144 CYS D SG  1 
ATOM   11465 N N   . ASP F 2 145 ? -52.879 33.832  0.105   1.00 72.88  ? 145 ASP D N   1 
ATOM   11466 C CA  . ASP F 2 145 ? -52.248 35.094  -0.294  1.00 71.43  ? 145 ASP D CA  1 
ATOM   11467 C C   . ASP F 2 145 ? -51.097 35.475  0.647   1.00 67.76  ? 145 ASP D C   1 
ATOM   11468 O O   . ASP F 2 145 ? -50.779 34.736  1.578   1.00 60.77  ? 145 ASP D O   1 
ATOM   11469 C CB  . ASP F 2 145 ? -53.299 36.214  -0.373  1.00 70.56  ? 145 ASP D CB  1 
ATOM   11470 C CG  . ASP F 2 145 ? -53.871 36.593  0.983   1.00 76.95  ? 145 ASP D CG  1 
ATOM   11471 O OD1 . ASP F 2 145 ? -54.318 35.679  1.711   1.00 89.31  ? 145 ASP D OD1 1 
ATOM   11472 O OD2 . ASP F 2 145 ? -53.899 37.803  1.309   1.00 90.78  ? 145 ASP D OD2 1 
ATOM   11473 N N   . ASN F 2 146 ? -50.470 36.622  0.389   1.00 66.03  ? 146 ASN D N   1 
ATOM   11474 C CA  . ASN F 2 146 ? -49.306 37.065  1.157   1.00 61.42  ? 146 ASN D CA  1 
ATOM   11475 C C   . ASN F 2 146 ? -49.592 37.274  2.638   1.00 67.21  ? 146 ASN D C   1 
ATOM   11476 O O   . ASN F 2 146 ? -48.688 37.129  3.461   1.00 85.10  ? 146 ASN D O   1 
ATOM   11477 C CB  . ASN F 2 146 ? -48.705 38.342  0.560   1.00 55.03  ? 146 ASN D CB  1 
ATOM   11478 C CG  . ASN F 2 146 ? -47.964 38.093  -0.746  1.00 58.78  ? 146 ASN D CG  1 
ATOM   11479 O OD1 . ASN F 2 146 ? -47.825 36.952  -1.204  1.00 66.21  ? 146 ASN D OD1 1 
ATOM   11480 N ND2 . ASN F 2 146 ? -47.466 39.166  -1.344  1.00 53.41  ? 146 ASN D ND2 1 
ATOM   11481 N N   . GLU F 2 147 ? -50.837 37.591  2.985   1.00 72.00  ? 147 GLU D N   1 
ATOM   11482 C CA  . GLU F 2 147 ? -51.223 37.675  4.398   1.00 78.33  ? 147 GLU D CA  1 
ATOM   11483 C C   . GLU F 2 147 ? -51.342 36.273  4.986   1.00 73.15  ? 147 GLU D C   1 
ATOM   11484 O O   . GLU F 2 147 ? -50.892 36.022  6.100   1.00 65.82  ? 147 GLU D O   1 
ATOM   11485 C CB  . GLU F 2 147 ? -52.532 38.430  4.571   1.00 91.43  ? 147 GLU D CB  1 
ATOM   11486 C CG  . GLU F 2 147 ? -52.453 39.899  4.197   1.00 101.34 ? 147 GLU D CG  1 
ATOM   11487 C CD  . GLU F 2 147 ? -53.802 40.585  4.269   1.00 110.02 ? 147 GLU D CD  1 
ATOM   11488 O OE1 . GLU F 2 147 ? -54.688 40.123  5.023   1.00 114.20 ? 147 GLU D OE1 1 
ATOM   11489 O OE2 . GLU F 2 147 ? -53.975 41.594  3.563   1.00 110.94 ? 147 GLU D OE2 1 
ATOM   11490 N N   . CYS F 2 148 ? -51.945 35.367  4.220   1.00 72.55  ? 148 CYS D N   1 
ATOM   11491 C CA  . CYS F 2 148 ? -52.090 33.968  4.620   1.00 71.62  ? 148 CYS D CA  1 
ATOM   11492 C C   . CYS F 2 148 ? -50.725 33.299  4.824   1.00 65.81  ? 148 CYS D C   1 
ATOM   11493 O O   . CYS F 2 148 ? -50.542 32.540  5.775   1.00 63.87  ? 148 CYS D O   1 
ATOM   11494 C CB  . CYS F 2 148 ? -52.924 33.210  3.578   1.00 76.72  ? 148 CYS D CB  1 
ATOM   11495 S SG  . CYS F 2 148 ? -52.869 31.404  3.673   1.00 79.48  ? 148 CYS D SG  1 
ATOM   11496 N N   . MET F 2 149 ? -49.771 33.599  3.942   1.00 65.93  ? 149 MET D N   1 
ATOM   11497 C CA  . MET F 2 149 ? -48.415 33.050  4.043   1.00 60.50  ? 149 MET D CA  1 
ATOM   11498 C C   . MET F 2 149 ? -47.690 33.556  5.288   1.00 62.56  ? 149 MET D C   1 
ATOM   11499 O O   . MET F 2 149 ? -47.016 32.782  5.968   1.00 57.67  ? 149 MET D O   1 
ATOM   11500 C CB  . MET F 2 149 ? -47.590 33.398  2.802   1.00 54.40  ? 149 MET D CB  1 
ATOM   11501 C CG  . MET F 2 149 ? -48.062 32.724  1.522   1.00 59.35  ? 149 MET D CG  1 
ATOM   11502 S SD  . MET F 2 149 ? -47.746 30.950  1.456   1.00 55.58  ? 149 MET D SD  1 
ATOM   11503 C CE  . MET F 2 149 ? -48.262 30.565  -0.216  1.00 49.75  ? 149 MET D CE  1 
ATOM   11504 N N   . GLU F 2 150 ? -47.832 34.848  5.578   1.00 59.28  ? 150 GLU D N   1 
ATOM   11505 C CA  . GLU F 2 150 ? -47.239 35.443  6.778   1.00 60.39  ? 150 GLU D CA  1 
ATOM   11506 C C   . GLU F 2 150 ? -47.731 34.754  8.047   1.00 59.23  ? 150 GLU D C   1 
ATOM   11507 O O   . GLU F 2 150 ? -46.935 34.453  8.933   1.00 60.31  ? 150 GLU D O   1 
ATOM   11508 C CB  . GLU F 2 150 ? -47.558 36.938  6.860   1.00 75.42  ? 150 GLU D CB  1 
ATOM   11509 C CG  . GLU F 2 150 ? -46.742 37.808  5.912   1.00 91.84  ? 150 GLU D CG  1 
ATOM   11510 C CD  . GLU F 2 150 ? -47.368 39.175  5.646   1.00 107.20 ? 150 GLU D CD  1 
ATOM   11511 O OE1 . GLU F 2 150 ? -48.389 39.523  6.284   1.00 116.13 ? 150 GLU D OE1 1 
ATOM   11512 O OE2 . GLU F 2 150 ? -46.837 39.909  4.784   1.00 117.53 ? 150 GLU D OE2 1 
ATOM   11513 N N   . SER F 2 151 ? -49.038 34.499  8.123   1.00 57.58  ? 151 SER D N   1 
ATOM   11514 C CA  . SER F 2 151 ? -49.638 33.872  9.305   1.00 57.91  ? 151 SER D CA  1 
ATOM   11515 C C   . SER F 2 151 ? -49.090 32.467  9.563   1.00 56.43  ? 151 SER D C   1 
ATOM   11516 O O   . SER F 2 151 ? -49.039 32.024  10.708  1.00 58.77  ? 151 SER D O   1 
ATOM   11517 C CB  . SER F 2 151 ? -51.168 33.817  9.181   1.00 55.40  ? 151 SER D CB  1 
ATOM   11518 O OG  . SER F 2 151 ? -51.571 32.984  8.110   1.00 54.42  ? 151 SER D OG  1 
ATOM   11519 N N   . VAL F 2 152 ? -48.693 31.772  8.497   1.00 52.55  ? 152 VAL D N   1 
ATOM   11520 C CA  . VAL F 2 152 ? -48.080 30.444  8.617   1.00 50.39  ? 152 VAL D CA  1 
ATOM   11521 C C   . VAL F 2 152 ? -46.684 30.547  9.241   1.00 52.37  ? 152 VAL D C   1 
ATOM   11522 O O   . VAL F 2 152 ? -46.276 29.661  9.987   1.00 53.47  ? 152 VAL D O   1 
ATOM   11523 C CB  . VAL F 2 152 ? -47.977 29.731  7.251   1.00 47.48  ? 152 VAL D CB  1 
ATOM   11524 C CG1 . VAL F 2 152 ? -47.278 28.385  7.384   1.00 47.90  ? 152 VAL D CG1 1 
ATOM   11525 C CG2 . VAL F 2 152 ? -49.360 29.551  6.645   1.00 46.03  ? 152 VAL D CG2 1 
ATOM   11526 N N   . ARG F 2 153 ? -45.968 31.631  8.933   1.00 53.37  ? 153 ARG D N   1 
ATOM   11527 C CA  . ARG F 2 153 ? -44.662 31.910  9.532   1.00 55.62  ? 153 ARG D CA  1 
ATOM   11528 C C   . ARG F 2 153 ? -44.824 32.429  10.962  1.00 66.20  ? 153 ARG D C   1 
ATOM   11529 O O   . ARG F 2 153 ? -44.061 32.048  11.845  1.00 82.61  ? 153 ARG D O   1 
ATOM   11530 C CB  . ARG F 2 153 ? -43.876 32.928  8.694   1.00 59.35  ? 153 ARG D CB  1 
ATOM   11531 C CG  . ARG F 2 153 ? -43.723 32.564  7.222   1.00 63.61  ? 153 ARG D CG  1 
ATOM   11532 C CD  . ARG F 2 153 ? -42.821 33.546  6.489   1.00 70.66  ? 153 ARG D CD  1 
ATOM   11533 N NE  . ARG F 2 153 ? -43.284 33.790  5.122   1.00 77.47  ? 153 ARG D NE  1 
ATOM   11534 C CZ  . ARG F 2 153 ? -43.793 34.938  4.669   1.00 80.86  ? 153 ARG D CZ  1 
ATOM   11535 N NH1 . ARG F 2 153 ? -43.915 36.007  5.453   1.00 85.58  ? 153 ARG D NH1 1 
ATOM   11536 N NH2 . ARG F 2 153 ? -44.180 35.019  3.403   1.00 84.86  ? 153 ARG D NH2 1 
ATOM   11537 N N   . ASN F 2 154 ? -45.808 33.308  11.174  1.00 69.30  ? 154 ASN D N   1 
ATOM   11538 C CA  . ASN F 2 154 ? -46.150 33.828  12.509  1.00 66.25  ? 154 ASN D CA  1 
ATOM   11539 C C   . ASN F 2 154 ? -46.409 32.717  13.514  1.00 67.51  ? 154 ASN D C   1 
ATOM   11540 O O   . ASN F 2 154 ? -45.969 32.793  14.660  1.00 69.34  ? 154 ASN D O   1 
ATOM   11541 C CB  . ASN F 2 154 ? -47.434 34.673  12.460  1.00 72.24  ? 154 ASN D CB  1 
ATOM   11542 C CG  . ASN F 2 154 ? -47.241 36.032  11.807  1.00 78.39  ? 154 ASN D CG  1 
ATOM   11543 O OD1 . ASN F 2 154 ? -46.142 36.397  11.398  1.00 91.99  ? 154 ASN D OD1 1 
ATOM   11544 N ND2 . ASN F 2 154 ? -48.329 36.790  11.705  1.00 74.80  ? 154 ASN D ND2 1 
ATOM   11545 N N   . GLY F 2 155 ? -47.144 31.701  13.071  1.00 66.35  ? 155 GLY D N   1 
ATOM   11546 C CA  . GLY F 2 155 ? -47.743 30.716  13.963  1.00 69.68  ? 155 GLY D CA  1 
ATOM   11547 C C   . GLY F 2 155 ? -49.194 31.054  14.288  1.00 72.24  ? 155 GLY D C   1 
ATOM   11548 O O   . GLY F 2 155 ? -49.743 30.532  15.258  1.00 84.82  ? 155 GLY D O   1 
ATOM   11549 N N   . THR F 2 156 ? -49.811 31.917  13.476  1.00 71.80  ? 156 THR D N   1 
ATOM   11550 C CA  . THR F 2 156 ? -51.171 32.424  13.722  1.00 75.41  ? 156 THR D CA  1 
ATOM   11551 C C   . THR F 2 156 ? -52.165 32.004  12.635  1.00 79.77  ? 156 THR D C   1 
ATOM   11552 O O   . THR F 2 156 ? -53.265 32.550  12.555  1.00 71.84  ? 156 THR D O   1 
ATOM   11553 C CB  . THR F 2 156 ? -51.199 33.967  13.800  1.00 69.94  ? 156 THR D CB  1 
ATOM   11554 O OG1 . THR F 2 156 ? -50.717 34.520  12.568  1.00 72.14  ? 156 THR D OG1 1 
ATOM   11555 C CG2 . THR F 2 156 ? -50.339 34.464  14.950  1.00 77.65  ? 156 THR D CG2 1 
ATOM   11556 N N   . TYR F 2 157 ? -51.776 31.041  11.802  1.00 76.47  ? 157 TYR D N   1 
ATOM   11557 C CA  . TYR F 2 157 ? -52.601 30.606  10.675  1.00 71.29  ? 157 TYR D CA  1 
ATOM   11558 C C   . TYR F 2 157 ? -53.967 30.095  11.147  1.00 68.18  ? 157 TYR D C   1 
ATOM   11559 O O   . TYR F 2 157 ? -54.043 29.150  11.927  1.00 63.78  ? 157 TYR D O   1 
ATOM   11560 C CB  . TYR F 2 157 ? -51.857 29.525  9.880   1.00 67.33  ? 157 TYR D CB  1 
ATOM   11561 C CG  . TYR F 2 157 ? -52.689 28.765  8.864   1.00 61.19  ? 157 TYR D CG  1 
ATOM   11562 C CD1 . TYR F 2 157 ? -52.901 29.273  7.588   1.00 59.04  ? 157 TYR D CD1 1 
ATOM   11563 C CD2 . TYR F 2 157 ? -53.238 27.520  9.174   1.00 60.85  ? 157 TYR D CD2 1 
ATOM   11564 C CE1 . TYR F 2 157 ? -53.649 28.568  6.655   1.00 55.42  ? 157 TYR D CE1 1 
ATOM   11565 C CE2 . TYR F 2 157 ? -53.984 26.807  8.251   1.00 58.68  ? 157 TYR D CE2 1 
ATOM   11566 C CZ  . TYR F 2 157 ? -54.187 27.336  6.994   1.00 58.91  ? 157 TYR D CZ  1 
ATOM   11567 O OH  . TYR F 2 157 ? -54.936 26.620  6.090   1.00 71.51  ? 157 TYR D OH  1 
ATOM   11568 N N   . ASP F 2 158 ? -55.033 30.737  10.668  1.00 69.31  ? 158 ASP D N   1 
ATOM   11569 C CA  . ASP F 2 158 ? -56.404 30.418  11.068  1.00 66.92  ? 158 ASP D CA  1 
ATOM   11570 C C   . ASP F 2 158 ? -56.949 29.258  10.226  1.00 68.25  ? 158 ASP D C   1 
ATOM   11571 O O   . ASP F 2 158 ? -57.419 29.454  9.104   1.00 62.91  ? 158 ASP D O   1 
ATOM   11572 C CB  . ASP F 2 158 ? -57.291 31.666  10.925  1.00 75.59  ? 158 ASP D CB  1 
ATOM   11573 C CG  . ASP F 2 158 ? -58.610 31.556  11.683  1.00 84.39  ? 158 ASP D CG  1 
ATOM   11574 O OD1 . ASP F 2 158 ? -59.479 32.430  11.472  1.00 90.88  ? 158 ASP D OD1 1 
ATOM   11575 O OD2 . ASP F 2 158 ? -58.788 30.616  12.487  1.00 90.11  ? 158 ASP D OD2 1 
ATOM   11576 N N   . TYR F 2 159 ? -56.872 28.048  10.777  1.00 71.03  ? 159 TYR D N   1 
ATOM   11577 C CA  . TYR F 2 159 ? -57.298 26.831  10.073  1.00 68.61  ? 159 TYR D CA  1 
ATOM   11578 C C   . TYR F 2 159 ? -58.797 26.792  9.727   1.00 75.53  ? 159 TYR D C   1 
ATOM   11579 O O   . TYR F 2 159 ? -59.145 26.543  8.572   1.00 80.67  ? 159 TYR D O   1 
ATOM   11580 C CB  . TYR F 2 159 ? -56.900 25.580  10.872  1.00 66.02  ? 159 TYR D CB  1 
ATOM   11581 C CG  . TYR F 2 159 ? -57.536 24.293  10.379  1.00 65.12  ? 159 TYR D CG  1 
ATOM   11582 C CD1 . TYR F 2 159 ? -57.004 23.603  9.297   1.00 60.50  ? 159 TYR D CD1 1 
ATOM   11583 C CD2 . TYR F 2 159 ? -58.663 23.760  11.005  1.00 69.52  ? 159 TYR D CD2 1 
ATOM   11584 C CE1 . TYR F 2 159 ? -57.573 22.425  8.848   1.00 62.74  ? 159 TYR D CE1 1 
ATOM   11585 C CE2 . TYR F 2 159 ? -59.241 22.579  10.559  1.00 64.51  ? 159 TYR D CE2 1 
ATOM   11586 C CZ  . TYR F 2 159 ? -58.693 21.917  9.480   1.00 65.38  ? 159 TYR D CZ  1 
ATOM   11587 O OH  . TYR F 2 159 ? -59.261 20.750  9.027   1.00 68.40  ? 159 TYR D OH  1 
ATOM   11588 N N   . PRO F 2 160 ? -59.689 27.020  10.720  1.00 76.28  ? 160 PRO D N   1 
ATOM   11589 C CA  . PRO F 2 160 ? -61.132 26.959  10.420  1.00 72.91  ? 160 PRO D CA  1 
ATOM   11590 C C   . PRO F 2 160 ? -61.587 27.896  9.295   1.00 72.07  ? 160 PRO D C   1 
ATOM   11591 O O   . PRO F 2 160 ? -62.546 27.588  8.588   1.00 62.89  ? 160 PRO D O   1 
ATOM   11592 C CB  . PRO F 2 160 ? -61.808 27.360  11.740  1.00 70.67  ? 160 PRO D CB  1 
ATOM   11593 C CG  . PRO F 2 160 ? -60.733 27.602  12.737  1.00 72.65  ? 160 PRO D CG  1 
ATOM   11594 C CD  . PRO F 2 160 ? -59.416 27.209  12.158  1.00 74.92  ? 160 PRO D CD  1 
ATOM   11595 N N   . GLN F 2 161 ? -60.891 29.019  9.135   1.00 76.62  ? 161 GLN D N   1 
ATOM   11596 C CA  . GLN F 2 161 ? -61.253 30.038  8.150   1.00 73.14  ? 161 GLN D CA  1 
ATOM   11597 C C   . GLN F 2 161 ? -61.179 29.550  6.699   1.00 67.09  ? 161 GLN D C   1 
ATOM   11598 O O   . GLN F 2 161 ? -61.978 29.971  5.861   1.00 76.48  ? 161 GLN D O   1 
ATOM   11599 C CB  . GLN F 2 161 ? -60.357 31.264  8.329   1.00 77.21  ? 161 GLN D CB  1 
ATOM   11600 C CG  . GLN F 2 161 ? -60.942 32.534  7.766   1.00 83.95  ? 161 GLN D CG  1 
ATOM   11601 C CD  . GLN F 2 161 ? -60.167 33.772  8.148   1.00 93.83  ? 161 GLN D CD  1 
ATOM   11602 O OE1 . GLN F 2 161 ? -59.101 34.034  7.599   1.00 95.45  ? 161 GLN D OE1 1 
ATOM   11603 N NE2 . GLN F 2 161 ? -60.712 34.555  9.078   1.00 94.72  ? 161 GLN D NE2 1 
ATOM   11604 N N   . TYR F 2 162 ? -60.226 28.670  6.406   1.00 63.53  ? 162 TYR D N   1 
ATOM   11605 C CA  . TYR F 2 162 ? -60.054 28.127  5.054   1.00 64.04  ? 162 TYR D CA  1 
ATOM   11606 C C   . TYR F 2 162 ? -60.501 26.666  4.935   1.00 67.92  ? 162 TYR D C   1 
ATOM   11607 O O   . TYR F 2 162 ? -60.484 26.103  3.840   1.00 78.08  ? 162 TYR D O   1 
ATOM   11608 C CB  . TYR F 2 162 ? -58.585 28.233  4.625   1.00 64.31  ? 162 TYR D CB  1 
ATOM   11609 C CG  . TYR F 2 162 ? -57.995 29.629  4.686   1.00 61.18  ? 162 TYR D CG  1 
ATOM   11610 C CD1 . TYR F 2 162 ? -57.200 30.023  5.757   1.00 61.86  ? 162 TYR D CD1 1 
ATOM   11611 C CD2 . TYR F 2 162 ? -58.224 30.552  3.667   1.00 62.25  ? 162 TYR D CD2 1 
ATOM   11612 C CE1 . TYR F 2 162 ? -56.655 31.298  5.819   1.00 68.07  ? 162 TYR D CE1 1 
ATOM   11613 C CE2 . TYR F 2 162 ? -57.680 31.829  3.720   1.00 63.28  ? 162 TYR D CE2 1 
ATOM   11614 C CZ  . TYR F 2 162 ? -56.896 32.198  4.798   1.00 67.48  ? 162 TYR D CZ  1 
ATOM   11615 O OH  . TYR F 2 162 ? -56.350 33.465  4.864   1.00 69.67  ? 162 TYR D OH  1 
ATOM   11616 N N   . SER F 2 163 ? -60.905 26.057  6.049   1.00 74.44  ? 163 SER D N   1 
ATOM   11617 C CA  . SER F 2 163 ? -61.166 24.610  6.098   1.00 84.68  ? 163 SER D CA  1 
ATOM   11618 C C   . SER F 2 163 ? -62.249 24.139  5.129   1.00 88.38  ? 163 SER D C   1 
ATOM   11619 O O   . SER F 2 163 ? -62.122 23.070  4.528   1.00 87.98  ? 163 SER D O   1 
ATOM   11620 C CB  . SER F 2 163 ? -61.524 24.174  7.524   1.00 86.44  ? 163 SER D CB  1 
ATOM   11621 O OG  . SER F 2 163 ? -62.713 24.805  7.968   1.00 81.44  ? 163 SER D OG  1 
ATOM   11622 N N   . GLU F 2 164 ? -63.308 24.930  4.981   1.00 92.71  ? 164 GLU D N   1 
ATOM   11623 C CA  . GLU F 2 164 ? -64.402 24.564  4.081   1.00 96.94  ? 164 GLU D CA  1 
ATOM   11624 C C   . GLU F 2 164 ? -63.958 24.575  2.622   1.00 91.71  ? 164 GLU D C   1 
ATOM   11625 O O   . GLU F 2 164 ? -64.158 23.593  1.910   1.00 88.35  ? 164 GLU D O   1 
ATOM   11626 C CB  . GLU F 2 164 ? -65.621 25.467  4.288   1.00 113.72 ? 164 GLU D CB  1 
ATOM   11627 C CG  . GLU F 2 164 ? -66.426 25.109  5.539   1.00 126.77 ? 164 GLU D CG  1 
ATOM   11628 C CD  . GLU F 2 164 ? -67.891 25.496  5.443   1.00 130.77 ? 164 GLU D CD  1 
ATOM   11629 O OE1 . GLU F 2 164 ? -68.762 24.597  5.346   1.00 137.26 ? 164 GLU D OE1 1 
ATOM   11630 O OE2 . GLU F 2 164 ? -68.173 26.709  5.471   1.00 136.40 ? 164 GLU D OE2 1 
ATOM   11631 N N   . GLU F 2 165 ? -63.344 25.674  2.189   1.00 88.27  ? 165 GLU D N   1 
ATOM   11632 C CA  . GLU F 2 165 ? -62.796 25.771  0.832   1.00 86.36  ? 165 GLU D CA  1 
ATOM   11633 C C   . GLU F 2 165 ? -61.854 24.603  0.536   1.00 85.49  ? 165 GLU D C   1 
ATOM   11634 O O   . GLU F 2 165 ? -61.892 24.023  -0.551  1.00 77.93  ? 165 GLU D O   1 
ATOM   11635 C CB  . GLU F 2 165 ? -62.046 27.094  0.648   1.00 90.61  ? 165 GLU D CB  1 
ATOM   11636 C CG  . GLU F 2 165 ? -61.575 27.355  -0.778  1.00 93.00  ? 165 GLU D CG  1 
ATOM   11637 C CD  . GLU F 2 165 ? -60.711 28.598  -0.900  1.00 94.87  ? 165 GLU D CD  1 
ATOM   11638 O OE1 . GLU F 2 165 ? -60.688 29.419  0.047   1.00 88.76  ? 165 GLU D OE1 1 
ATOM   11639 O OE2 . GLU F 2 165 ? -60.044 28.752  -1.948  1.00 93.27  ? 165 GLU D OE2 1 
ATOM   11640 N N   . ALA F 2 166 ? -61.026 24.263  1.522   1.00 84.81  ? 166 ALA D N   1 
ATOM   11641 C CA  . ALA F 2 166 ? -60.061 23.178  1.413   1.00 81.04  ? 166 ALA D CA  1 
ATOM   11642 C C   . ALA F 2 166 ? -60.744 21.834  1.180   1.00 79.86  ? 166 ALA D C   1 
ATOM   11643 O O   . ALA F 2 166 ? -60.235 21.016  0.415   1.00 70.37  ? 166 ALA D O   1 
ATOM   11644 C CB  . ALA F 2 166 ? -59.198 23.118  2.663   1.00 83.69  ? 166 ALA D CB  1 
ATOM   11645 N N   . ARG F 2 167 ? -61.891 21.622  1.831   1.00 90.37  ? 167 ARG D N   1 
ATOM   11646 C CA  . ARG F 2 167 ? -62.635 20.352  1.725   1.00 98.00  ? 167 ARG D CA  1 
ATOM   11647 C C   . ARG F 2 167 ? -63.287 20.166  0.368   1.00 90.27  ? 167 ARG D C   1 
ATOM   11648 O O   . ARG F 2 167 ? -63.553 19.035  -0.058  1.00 88.52  ? 167 ARG D O   1 
ATOM   11649 C CB  . ARG F 2 167 ? -63.746 20.237  2.775   1.00 107.88 ? 167 ARG D CB  1 
ATOM   11650 C CG  . ARG F 2 167 ? -63.321 19.865  4.192   1.00 116.68 ? 167 ARG D CG  1 
ATOM   11651 C CD  . ARG F 2 167 ? -64.525 19.590  5.087   1.00 115.69 ? 167 ARG D CD  1 
ATOM   11652 N NE  . ARG F 2 167 ? -65.573 20.602  4.944   1.00 117.45 ? 167 ARG D NE  1 
ATOM   11653 C CZ  . ARG F 2 167 ? -66.687 20.476  4.216   1.00 105.09 ? 167 ARG D CZ  1 
ATOM   11654 N NH1 . ARG F 2 167 ? -66.952 19.377  3.507   1.00 103.32 ? 167 ARG D NH1 1 
ATOM   11655 N NH2 . ARG F 2 167 ? -67.551 21.485  4.186   1.00 93.91  ? 167 ARG D NH2 1 
ATOM   11656 N N   . LEU F 2 168 ? -63.571 21.276  -0.299  1.00 85.84  ? 168 LEU D N   1 
ATOM   11657 C CA  . LEU F 2 168 ? -64.244 21.202  -1.582  1.00 97.98  ? 168 LEU D CA  1 
ATOM   11658 C C   . LEU F 2 168 ? -63.242 20.715  -2.614  1.00 107.87 ? 168 LEU D C   1 
ATOM   11659 O O   . LEU F 2 168 ? -63.540 19.802  -3.370  1.00 111.58 ? 168 LEU D O   1 
ATOM   11660 C CB  . LEU F 2 168 ? -64.837 22.550  -1.993  1.00 100.74 ? 168 LEU D CB  1 
ATOM   11661 C CG  . LEU F 2 168 ? -66.042 23.035  -1.178  1.00 102.42 ? 168 LEU D CG  1 
ATOM   11662 C CD1 . LEU F 2 168 ? -66.402 24.464  -1.560  1.00 95.95  ? 168 LEU D CD1 1 
ATOM   11663 C CD2 . LEU F 2 168 ? -67.241 22.109  -1.353  1.00 87.35  ? 168 LEU D CD2 1 
ATOM   11664 N N   . LYS F 2 169 ? -62.043 21.297  -2.605  1.00 109.65 ? 169 LYS D N   1 
ATOM   11665 C CA  . LYS F 2 169 ? -61.003 20.961  -3.588  1.00 104.48 ? 169 LYS D CA  1 
ATOM   11666 C C   . LYS F 2 169 ? -60.358 19.588  -3.341  1.00 97.99  ? 169 LYS D C   1 
ATOM   11667 O O   . LYS F 2 169 ? -59.801 18.982  -4.253  1.00 91.97  ? 169 LYS D O   1 
ATOM   11668 C CB  . LYS F 2 169 ? -59.918 22.047  -3.609  1.00 105.00 ? 169 LYS D CB  1 
ATOM   11669 C CG  . LYS F 2 169 ? -59.141 22.136  -4.920  1.00 101.92 ? 169 LYS D CG  1 
ATOM   11670 C CD  . LYS F 2 169 ? -59.584 23.328  -5.757  1.00 107.28 ? 169 LYS D CD  1 
ATOM   11671 C CE  . LYS F 2 169 ? -60.966 23.126  -6.346  1.00 110.70 ? 169 LYS D CE  1 
ATOM   11672 N NZ  . LYS F 2 169 ? -61.337 24.189  -7.321  1.00 109.36 ? 169 LYS D NZ  1 
ATOM   11673 N N   . ARG F 2 170 ? -60.445 19.095  -2.111  1.00 99.91  ? 170 ARG D N   1 
ATOM   11674 C CA  . ARG F 2 170 ? -59.839 17.813  -1.740  1.00 100.47 ? 170 ARG D CA  1 
ATOM   11675 C C   . ARG F 2 170 ? -60.437 16.599  -2.493  1.00 104.19 ? 170 ARG D C   1 
ATOM   11676 O O   . ARG F 2 170 ? -59.797 15.547  -2.561  1.00 107.04 ? 170 ARG D O   1 
ATOM   11677 C CB  . ARG F 2 170 ? -59.908 17.623  -0.213  1.00 96.40  ? 170 ARG D CB  1 
ATOM   11678 C CG  . ARG F 2 170 ? -58.601 17.150  0.410   1.00 88.87  ? 170 ARG D CG  1 
ATOM   11679 C CD  . ARG F 2 170 ? -58.768 16.912  1.903   1.00 85.22  ? 170 ARG D CD  1 
ATOM   11680 N NE  . ARG F 2 170 ? -59.133 18.141  2.610   1.00 86.31  ? 170 ARG D NE  1 
ATOM   11681 C CZ  . ARG F 2 170 ? -59.780 18.195  3.775   1.00 88.81  ? 170 ARG D CZ  1 
ATOM   11682 N NH1 . ARG F 2 170 ? -60.161 17.088  4.406   1.00 90.69  ? 170 ARG D NH1 1 
ATOM   11683 N NH2 . ARG F 2 170 ? -60.057 19.376  4.320   1.00 93.42  ? 170 ARG D NH2 1 
ATOM   11684 N N   . GLU F 2 171 ? -61.614 16.770  -3.104  1.00 109.59 ? 171 GLU D N   1 
ATOM   11685 C CA  . GLU F 2 171 ? -62.363 15.649  -3.743  1.00 113.63 ? 171 GLU D CA  1 
ATOM   11686 C C   . GLU F 2 171 ? -62.488 15.741  -5.278  1.00 118.13 ? 171 GLU D C   1 
ATOM   11687 O O   . GLU F 2 171 ? -63.452 15.228  -5.852  1.00 125.22 ? 171 GLU D O   1 
ATOM   11688 C CB  . GLU F 2 171 ? -63.766 15.467  -3.073  1.00 116.12 ? 171 GLU D CB  1 
ATOM   11689 C CG  . GLU F 2 171 ? -64.336 16.772  -2.552  1.00 117.93 ? 171 GLU D CG  1 
ATOM   11690 C CD  . GLU F 2 171 ? -65.756 16.657  -2.037  1.00 119.98 ? 171 GLU D CD  1 
ATOM   11691 O OE1 . GLU F 2 171 ? -66.697 16.925  -2.818  1.00 122.44 ? 171 GLU D OE1 1 
ATOM   11692 O OE2 . GLU F 2 171 ? -65.928 16.307  -0.850  1.00 113.65 ? 171 GLU D OE2 1 
ATOM   11693 N N   . GLU F 2 172 ? -61.480 16.323  -5.935  1.00 121.66 ? 172 GLU D N   1 
ATOM   11694 C CA  . GLU F 2 172 ? -61.540 16.640  -7.377  1.00 132.22 ? 172 GLU D CA  1 
ATOM   11695 C C   . GLU F 2 172 ? -60.991 15.558  -8.309  1.00 151.42 ? 172 GLU D C   1 
ATOM   11696 O O   . GLU F 2 172 ? -61.682 15.102  -9.230  1.00 161.05 ? 172 GLU D O   1 
ATOM   11697 C CB  . GLU F 2 172 ? -60.824 17.964  -7.669  1.00 121.89 ? 172 GLU D CB  1 
ATOM   11698 C CG  . GLU F 2 172 ? -61.769 19.137  -7.804  1.00 118.68 ? 172 GLU D CG  1 
ATOM   11699 C CD  . GLU F 2 172 ? -62.767 19.259  -6.666  1.00 113.97 ? 172 GLU D CD  1 
ATOM   11700 O OE1 . GLU F 2 172 ? -63.816 19.900  -6.878  1.00 112.08 ? 172 GLU D OE1 1 
ATOM   11701 O OE2 . GLU F 2 172 ? -62.516 18.714  -5.572  1.00 106.07 ? 172 GLU D OE2 1 
ATOM   11702 N N   . ILE F 2 173 ? -59.740 15.169  -8.076  1.00 160.08 ? 173 ILE D N   1 
ATOM   11703 C CA  . ILE F 2 173 ? -59.028 14.231  -8.962  1.00 164.16 ? 173 ILE D CA  1 
ATOM   11704 C C   . ILE F 2 173 ? -59.910 13.039  -9.354  1.00 154.74 ? 173 ILE D C   1 
ATOM   11705 O O   . ILE F 2 173 ? -59.900 12.589  -10.505 1.00 125.53 ? 173 ILE D O   1 
ATOM   11706 C CB  . ILE F 2 173 ? -57.718 13.706  -8.311  1.00 169.32 ? 173 ILE D CB  1 
ATOM   11707 C CG1 . ILE F 2 173 ? -56.674 14.824  -8.164  1.00 170.20 ? 173 ILE D CG1 1 
ATOM   11708 C CG2 . ILE F 2 173 ? -57.124 12.561  -9.123  1.00 162.82 ? 173 ILE D CG2 1 
ATOM   11709 C CD1 . ILE F 2 173 ? -56.048 15.266  -9.471  1.00 163.37 ? 173 ILE D CD1 1 
ATOM   11710 N N   . SER F 2 174 ? -60.670 12.544  -8.382  1.00 156.78 ? 174 SER D N   1 
ATOM   11711 C CA  . SER F 2 174 ? -61.629 11.469  -8.601  1.00 143.90 ? 174 SER D CA  1 
ATOM   11712 C C   . SER F 2 174 ? -62.745 11.921  -9.538  1.00 135.25 ? 174 SER D C   1 
ATOM   11713 O O   . SER F 2 174 ? -62.997 11.290  -10.566 1.00 132.00 ? 174 SER D O   1 
ATOM   11714 C CB  . SER F 2 174 ? -62.222 11.029  -7.261  1.00 137.09 ? 174 SER D CB  1 
ATOM   11715 O OG  . SER F 2 174 ? -61.299 11.248  -6.205  1.00 123.48 ? 174 SER D OG  1 
ATOM   11716 N N   . SER F 2 175 ? -63.404 13.019  -9.175  1.00 127.63 ? 175 SER D N   1 
ATOM   11717 C CA  . SER F 2 175 ? -64.495 13.569  -9.976  1.00 117.48 ? 175 SER D CA  1 
ATOM   11718 C C   . SER F 2 175 ? -65.045 14.856  -9.371  1.00 100.08 ? 175 SER D C   1 
ATOM   11719 O O   . SER F 2 175 ? -64.513 15.938  -9.609  1.00 99.08  ? 175 SER D O   1 
HETATM 11720 C C1  . NAG G 3 .   ? -16.817 12.212  55.286  1.00 103.53 ? 401 NAG A C1  1 
HETATM 11721 C C2  . NAG G 3 .   ? -16.641 11.140  56.367  1.00 117.19 ? 401 NAG A C2  1 
HETATM 11722 C C3  . NAG G 3 .   ? -17.872 10.234  56.519  1.00 124.31 ? 401 NAG A C3  1 
HETATM 11723 C C4  . NAG G 3 .   ? -19.216 10.945  56.342  1.00 123.76 ? 401 NAG A C4  1 
HETATM 11724 C C5  . NAG G 3 .   ? -19.169 12.039  55.282  1.00 118.40 ? 401 NAG A C5  1 
HETATM 11725 C C6  . NAG G 3 .   ? -20.407 12.925  55.342  1.00 118.68 ? 401 NAG A C6  1 
HETATM 11726 C C7  . NAG G 3 .   ? -14.830 9.618   57.004  1.00 126.55 ? 401 NAG A C7  1 
HETATM 11727 C C8  . NAG G 3 .   ? -13.637 8.830   56.544  1.00 121.81 ? 401 NAG A C8  1 
HETATM 11728 N N2  . NAG G 3 .   ? -15.468 10.329  56.073  1.00 122.72 ? 401 NAG A N2  1 
HETATM 11729 O O3  . NAG G 3 .   ? -17.865 9.645   57.802  1.00 117.89 ? 401 NAG A O3  1 
HETATM 11730 O O4  . NAG G 3 .   ? -20.202 9.995   55.997  1.00 123.72 ? 401 NAG A O4  1 
HETATM 11731 O O5  . NAG G 3 .   ? -18.049 12.852  55.530  1.00 112.00 ? 401 NAG A O5  1 
HETATM 11732 O O6  . NAG G 3 .   ? -20.552 13.615  54.122  1.00 118.31 ? 401 NAG A O6  1 
HETATM 11733 O O7  . NAG G 3 .   ? -15.171 9.583   58.186  1.00 129.35 ? 401 NAG A O7  1 
HETATM 11734 C C1  . NAG H 3 .   ? 28.321  -9.522  62.320  1.00 66.83  ? 402 NAG A C1  1 
HETATM 11735 C C2  . NAG H 3 .   ? 29.137  -9.955  61.096  1.00 72.38  ? 402 NAG A C2  1 
HETATM 11736 C C3  . NAG H 3 .   ? 28.525  -11.205 60.464  1.00 71.81  ? 402 NAG A C3  1 
HETATM 11737 C C4  . NAG H 3 .   ? 28.274  -12.290 61.507  1.00 81.76  ? 402 NAG A C4  1 
HETATM 11738 C C5  . NAG H 3 .   ? 27.516  -11.725 62.705  1.00 77.04  ? 402 NAG A C5  1 
HETATM 11739 C C6  . NAG H 3 .   ? 27.376  -12.754 63.824  1.00 78.16  ? 402 NAG A C6  1 
HETATM 11740 C C7  . NAG H 3 .   ? 30.162  -8.729  59.219  1.00 74.16  ? 402 NAG A C7  1 
HETATM 11741 C C8  . NAG H 3 .   ? 30.043  -7.559  58.291  1.00 70.20  ? 402 NAG A C8  1 
HETATM 11742 N N2  . NAG H 3 .   ? 29.184  -8.876  60.120  1.00 77.33  ? 402 NAG A N2  1 
HETATM 11743 O O3  . NAG H 3 .   ? 29.357  -11.711 59.444  1.00 63.77  ? 402 NAG A O3  1 
HETATM 11744 O O4  . NAG H 3 .   ? 27.541  -13.344 60.910  1.00 107.15 ? 402 NAG A O4  1 
HETATM 11745 O O5  . NAG H 3 .   ? 28.219  -10.614 63.209  1.00 69.84  ? 402 NAG A O5  1 
HETATM 11746 O O6  . NAG H 3 .   ? 27.194  -12.114 65.070  1.00 68.26  ? 402 NAG A O6  1 
HETATM 11747 O O7  . NAG H 3 .   ? 31.126  -9.483  59.109  1.00 74.00  ? 402 NAG A O7  1 
HETATM 11748 C C1  . NAG I 3 .   ? 28.184  -14.626 61.069  1.00 129.00 ? 403 NAG A C1  1 
HETATM 11749 C C2  . NAG I 3 .   ? 27.360  -15.685 60.327  1.00 134.15 ? 403 NAG A C2  1 
HETATM 11750 C C3  . NAG I 3 .   ? 28.029  -16.129 59.023  1.00 134.63 ? 403 NAG A C3  1 
HETATM 11751 C C4  . NAG I 3 .   ? 29.471  -16.585 59.255  1.00 149.39 ? 403 NAG A C4  1 
HETATM 11752 C C5  . NAG I 3 .   ? 30.082  -15.901 60.478  1.00 147.28 ? 403 NAG A C5  1 
HETATM 11753 C C6  . NAG I 3 .   ? 31.603  -15.804 60.378  1.00 138.51 ? 403 NAG A C6  1 
HETATM 11754 C C7  . NAG I 3 .   ? 26.114  -16.881 62.076  1.00 118.97 ? 403 NAG A C7  1 
HETATM 11755 C C8  . NAG I 3 .   ? 25.983  -18.154 62.863  1.00 112.55 ? 403 NAG A C8  1 
HETATM 11756 N N2  . NAG I 3 .   ? 27.098  -16.843 61.174  1.00 130.29 ? 403 NAG A N2  1 
HETATM 11757 O O3  . NAG I 3 .   ? 28.003  -15.064 58.098  1.00 111.77 ? 403 NAG A O3  1 
HETATM 11758 O O4  . NAG I 3 .   ? 29.499  -17.985 59.437  1.00 154.53 ? 403 NAG A O4  1 
HETATM 11759 O O5  . NAG I 3 .   ? 29.520  -14.612 60.605  1.00 139.99 ? 403 NAG A O5  1 
HETATM 11760 O O6  . NAG I 3 .   ? 31.981  -14.671 59.627  1.00 121.24 ? 403 NAG A O6  1 
HETATM 11761 O O7  . NAG I 3 .   ? 25.340  -15.947 62.282  1.00 106.08 ? 403 NAG A O7  1 
HETATM 11762 C C1  . NAG J 3 .   ? -23.797 34.822  34.011  1.00 68.75  ? 404 NAG A C1  1 
HETATM 11763 C C2  . NAG J 3 .   ? -22.928 35.900  33.384  1.00 89.28  ? 404 NAG A C2  1 
HETATM 11764 C C3  . NAG J 3 .   ? -21.826 36.341  34.352  1.00 95.15  ? 404 NAG A C3  1 
HETATM 11765 C C4  . NAG J 3 .   ? -22.278 36.468  35.813  1.00 101.76 ? 404 NAG A C4  1 
HETATM 11766 C C5  . NAG J 3 .   ? -23.374 35.493  36.230  1.00 100.22 ? 404 NAG A C5  1 
HETATM 11767 C C6  . NAG J 3 .   ? -24.130 35.973  37.469  1.00 106.39 ? 404 NAG A C6  1 
HETATM 11768 C C7  . NAG J 3 .   ? -21.883 36.178  31.190  1.00 117.55 ? 404 NAG A C7  1 
HETATM 11769 C C8  . NAG J 3 .   ? -21.333 35.487  29.976  1.00 113.55 ? 404 NAG A C8  1 
HETATM 11770 N N2  . NAG J 3 .   ? -22.362 35.387  32.149  1.00 104.03 ? 404 NAG A N2  1 
HETATM 11771 O O3  . NAG J 3 .   ? -21.326 37.596  33.940  1.00 98.96  ? 404 NAG A O3  1 
HETATM 11772 O O4  . NAG J 3 .   ? -21.179 36.253  36.678  1.00 118.30 ? 404 NAG A O4  1 
HETATM 11773 O O5  . NAG J 3 .   ? -24.306 35.390  35.190  1.00 88.07  ? 404 NAG A O5  1 
HETATM 11774 O O6  . NAG J 3 .   ? -24.297 34.920  38.392  1.00 109.41 ? 404 NAG A O6  1 
HETATM 11775 O O7  . NAG J 3 .   ? -21.873 37.407  31.268  1.00 130.53 ? 404 NAG A O7  1 
HETATM 11776 C C1  . NAG K 3 .   ? -20.506 37.472  37.041  1.00 133.64 ? 405 NAG A C1  1 
HETATM 11777 C C2  . NAG K 3 .   ? -20.235 37.438  38.542  1.00 139.99 ? 405 NAG A C2  1 
HETATM 11778 C C3  . NAG K 3 .   ? -19.370 38.616  38.975  1.00 145.70 ? 405 NAG A C3  1 
HETATM 11779 C C4  . NAG K 3 .   ? -18.162 38.771  38.057  1.00 151.38 ? 405 NAG A C4  1 
HETATM 11780 C C5  . NAG K 3 .   ? -18.626 38.819  36.604  1.00 141.05 ? 405 NAG A C5  1 
HETATM 11781 C C6  . NAG K 3 .   ? -17.470 38.987  35.625  1.00 133.86 ? 405 NAG A C6  1 
HETATM 11782 C C7  . NAG K 3 .   ? -21.855 36.621  40.205  1.00 167.00 ? 405 NAG A C7  1 
HETATM 11783 C C8  . NAG K 3 .   ? -23.200 36.844  40.835  1.00 160.15 ? 405 NAG A C8  1 
HETATM 11784 N N2  . NAG K 3 .   ? -21.497 37.495  39.261  1.00 155.35 ? 405 NAG A N2  1 
HETATM 11785 O O3  . NAG K 3 .   ? -18.947 38.428  40.307  1.00 139.08 ? 405 NAG A O3  1 
HETATM 11786 O O4  . NAG K 3 .   ? -17.467 39.951  38.394  1.00 164.63 ? 405 NAG A O4  1 
HETATM 11787 O O5  . NAG K 3 .   ? -19.304 37.615  36.315  1.00 133.09 ? 405 NAG A O5  1 
HETATM 11788 O O6  . NAG K 3 .   ? -16.620 37.865  35.692  1.00 124.11 ? 405 NAG A O6  1 
HETATM 11789 O O7  . NAG K 3 .   ? -21.158 35.675  40.569  1.00 175.44 ? 405 NAG A O7  1 
HETATM 11790 C C1  . NAG L 3 .   ? -38.014 27.301  47.883  1.00 99.51  ? 406 NAG A C1  1 
HETATM 11791 C C2  . NAG L 3 .   ? -38.877 26.503  48.880  1.00 114.56 ? 406 NAG A C2  1 
HETATM 11792 C C3  . NAG L 3 .   ? -39.188 27.169  50.240  1.00 116.79 ? 406 NAG A C3  1 
HETATM 11793 C C4  . NAG L 3 .   ? -38.342 28.391  50.597  1.00 118.86 ? 406 NAG A C4  1 
HETATM 11794 C C5  . NAG L 3 .   ? -37.956 29.131  49.330  1.00 114.09 ? 406 NAG A C5  1 
HETATM 11795 C C6  . NAG L 3 .   ? -37.121 30.377  49.595  1.00 112.20 ? 406 NAG A C6  1 
HETATM 11796 C C7  . NAG L 3 .   ? -40.762 24.967  48.476  1.00 121.91 ? 406 NAG A C7  1 
HETATM 11797 C C8  . NAG L 3 .   ? -42.062 24.750  47.758  1.00 104.44 ? 406 NAG A C8  1 
HETATM 11798 N N2  . NAG L 3 .   ? -40.143 26.133  48.254  1.00 125.64 ? 406 NAG A N2  1 
HETATM 11799 O O3  . NAG L 3 .   ? -39.043 26.217  51.276  1.00 108.04 ? 406 NAG A O3  1 
HETATM 11800 O O4  . NAG L 3 .   ? -39.066 29.235  51.465  1.00 120.16 ? 406 NAG A O4  1 
HETATM 11801 O O5  . NAG L 3 .   ? -37.196 28.209  48.589  1.00 111.15 ? 406 NAG A O5  1 
HETATM 11802 O O6  . NAG L 3 .   ? -37.105 31.149  48.415  1.00 100.27 ? 406 NAG A O6  1 
HETATM 11803 O O7  . NAG L 3 .   ? -40.326 24.086  49.216  1.00 125.25 ? 406 NAG A O7  1 
HETATM 11804 C C1  . NAG M 3 .   ? 46.434  11.190  17.266  1.00 88.55  ? 401 NAG E C1  1 
HETATM 11805 C C2  . NAG M 3 .   ? 46.651  12.658  17.660  1.00 92.72  ? 401 NAG E C2  1 
HETATM 11806 C C3  . NAG M 3 .   ? 46.503  13.663  16.518  1.00 93.53  ? 401 NAG E C3  1 
HETATM 11807 C C4  . NAG M 3 .   ? 47.205  13.169  15.264  1.00 95.94  ? 401 NAG E C4  1 
HETATM 11808 C C5  . NAG M 3 .   ? 46.629  11.804  14.921  1.00 97.70  ? 401 NAG E C5  1 
HETATM 11809 C C6  . NAG M 3 .   ? 47.210  11.280  13.611  1.00 94.30  ? 401 NAG E C6  1 
HETATM 11810 C C7  . NAG M 3 .   ? 46.132  13.570  19.876  1.00 90.34  ? 401 NAG E C7  1 
HETATM 11811 C C8  . NAG M 3 .   ? 45.054  13.901  20.864  1.00 91.67  ? 401 NAG E C8  1 
HETATM 11812 N N2  . NAG M 3 .   ? 45.732  13.030  18.723  1.00 89.91  ? 401 NAG E N2  1 
HETATM 11813 O O3  . NAG M 3 .   ? 47.044  14.904  16.911  1.00 90.14  ? 401 NAG E O3  1 
HETATM 11814 O O4  . NAG M 3 .   ? 47.003  14.075  14.200  1.00 96.33  ? 401 NAG E O4  1 
HETATM 11815 O O5  . NAG M 3 .   ? 46.931  10.901  15.967  1.00 98.12  ? 401 NAG E O5  1 
HETATM 11816 O O6  . NAG M 3 .   ? 46.876  9.920   13.442  1.00 86.60  ? 401 NAG E O6  1 
HETATM 11817 O O7  . NAG M 3 .   ? 47.308  13.796  20.158  1.00 88.67  ? 401 NAG E O7  1 
HETATM 11818 C C1  . NAG N 3 .   ? -23.103 -5.629  34.846  1.00 77.31  ? 402 NAG E C1  1 
HETATM 11819 C C2  . NAG N 3 .   ? -22.443 -6.901  35.411  1.00 78.30  ? 402 NAG E C2  1 
HETATM 11820 C C3  . NAG N 3 .   ? -22.558 -7.120  36.938  1.00 78.03  ? 402 NAG E C3  1 
HETATM 11821 C C4  . NAG N 3 .   ? -23.092 -5.948  37.770  1.00 81.72  ? 402 NAG E C4  1 
HETATM 11822 C C5  . NAG N 3 .   ? -23.910 -4.989  36.922  1.00 80.94  ? 402 NAG E C5  1 
HETATM 11823 C C6  . NAG N 3 .   ? -24.316 -3.732  37.687  1.00 80.90  ? 402 NAG E C6  1 
HETATM 11824 C C7  . NAG N 3 .   ? -22.241 -9.212  34.559  1.00 83.31  ? 402 NAG E C7  1 
HETATM 11825 C C8  . NAG N 3 .   ? -22.885 -10.332 33.789  1.00 68.65  ? 402 NAG E C8  1 
HETATM 11826 N N2  . NAG N 3 .   ? -22.939 -8.076  34.693  1.00 85.91  ? 402 NAG E N2  1 
HETATM 11827 O O3  . NAG N 3 .   ? -21.287 -7.461  37.458  1.00 68.46  ? 402 NAG E O3  1 
HETATM 11828 O O4  . NAG N 3 .   ? -23.864 -6.422  38.853  1.00 86.32  ? 402 NAG E O4  1 
HETATM 11829 O O5  . NAG N 3 .   ? -23.077 -4.639  35.845  1.00 84.14  ? 402 NAG E O5  1 
HETATM 11830 O O6  . NAG N 3 .   ? -25.679 -3.454  37.452  1.00 75.19  ? 402 NAG E O6  1 
HETATM 11831 O O7  . NAG N 3 .   ? -21.118 -9.379  35.028  1.00 89.42  ? 402 NAG E O7  1 
HETATM 11832 C C1  . NAG O 3 .   ? -56.985 3.441   32.163  1.00 99.20  ? 201 NAG B C1  1 
HETATM 11833 C C2  . NAG O 3 .   ? -57.331 2.286   33.113  1.00 117.95 ? 201 NAG B C2  1 
HETATM 11834 C C3  . NAG O 3 .   ? -58.654 1.616   32.713  1.00 121.74 ? 201 NAG B C3  1 
HETATM 11835 C C4  . NAG O 3 .   ? -59.757 2.630   32.392  1.00 125.74 ? 201 NAG B C4  1 
HETATM 11836 C C5  . NAG O 3 .   ? -59.207 3.718   31.473  1.00 126.37 ? 201 NAG B C5  1 
HETATM 11837 C C6  . NAG O 3 .   ? -60.221 4.809   31.150  1.00 137.30 ? 201 NAG B C6  1 
HETATM 11838 C C7  . NAG O 3 .   ? -56.076 0.375   34.029  1.00 114.54 ? 201 NAG B C7  1 
HETATM 11839 C C8  . NAG O 3 .   ? -54.884 -0.520  33.861  1.00 113.73 ? 201 NAG B C8  1 
HETATM 11840 N N2  . NAG O 3 .   ? -56.233 1.328   33.106  1.00 119.70 ? 201 NAG B N2  1 
HETATM 11841 O O3  . NAG O 3 .   ? -59.106 0.761   33.740  1.00 120.53 ? 201 NAG B O3  1 
HETATM 11842 O O4  . NAG O 3 .   ? -60.870 1.969   31.805  1.00 126.39 ? 201 NAG B O4  1 
HETATM 11843 O O5  . NAG O 3 .   ? -58.103 4.311   32.126  1.00 109.81 ? 201 NAG B O5  1 
HETATM 11844 O O6  . NAG O 3 .   ? -61.124 4.341   30.172  1.00 160.94 ? 201 NAG B O6  1 
HETATM 11845 O O7  . NAG O 3 .   ? -56.842 0.200   34.977  1.00 99.23  ? 201 NAG B O7  1 
HETATM 11846 C C1  . NAG P 3 .   ? -62.122 2.342   32.427  1.00 122.93 ? 202 NAG B C1  1 
HETATM 11847 C C2  . NAG P 3 .   ? -63.297 1.792   31.600  1.00 131.06 ? 202 NAG B C2  1 
HETATM 11848 C C3  . NAG P 3 .   ? -64.334 0.962   32.376  1.00 128.59 ? 202 NAG B C3  1 
HETATM 11849 C C4  . NAG P 3 .   ? -64.472 1.283   33.872  1.00 124.11 ? 202 NAG B C4  1 
HETATM 11850 C C5  . NAG P 3 .   ? -63.421 2.269   34.368  1.00 118.65 ? 202 NAG B C5  1 
HETATM 11851 C C6  . NAG P 3 .   ? -63.313 2.279   35.896  1.00 107.76 ? 202 NAG B C6  1 
HETATM 11852 C C7  . NAG P 3 .   ? -64.424 2.806   29.654  1.00 151.13 ? 202 NAG B C7  1 
HETATM 11853 C C8  . NAG P 3 .   ? -65.138 4.018   29.127  1.00 136.29 ? 202 NAG B C8  1 
HETATM 11854 N N2  . NAG P 3 .   ? -64.000 2.876   30.921  1.00 147.58 ? 202 NAG B N2  1 
HETATM 11855 O O3  . NAG P 3 .   ? -64.051 -0.414  32.222  1.00 136.12 ? 202 NAG B O3  1 
HETATM 11856 O O4  . NAG P 3 .   ? -65.757 1.803   34.141  1.00 128.75 ? 202 NAG B O4  1 
HETATM 11857 O O5  . NAG P 3 .   ? -62.194 1.912   33.769  1.00 121.84 ? 202 NAG B O5  1 
HETATM 11858 O O6  . NAG P 3 .   ? -62.058 1.802   36.334  1.00 88.28  ? 202 NAG B O6  1 
HETATM 11859 O O7  . NAG P 3 .   ? -64.260 1.829   28.922  1.00 160.25 ? 202 NAG B O7  1 
HETATM 11860 C C1  . NAG Q 3 .   ? 30.505  42.762  56.456  1.00 63.61  ? 401 NAG C C1  1 
HETATM 11861 C C2  . NAG Q 3 .   ? 30.381  41.754  57.607  1.00 66.38  ? 401 NAG C C2  1 
HETATM 11862 C C3  . NAG Q 3 .   ? 29.288  42.071  58.633  1.00 69.75  ? 401 NAG C C3  1 
HETATM 11863 C C4  . NAG Q 3 .   ? 29.292  43.545  59.004  1.00 65.64  ? 401 NAG C C4  1 
HETATM 11864 C C5  . NAG Q 3 .   ? 29.184  44.345  57.711  1.00 67.57  ? 401 NAG C C5  1 
HETATM 11865 C C6  . NAG Q 3 .   ? 29.057  45.849  57.959  1.00 68.62  ? 401 NAG C C6  1 
HETATM 11866 C C7  . NAG Q 3 .   ? 30.984  39.408  57.247  1.00 66.87  ? 401 NAG C C7  1 
HETATM 11867 C C8  . NAG Q 3 .   ? 30.574  38.093  56.657  1.00 64.37  ? 401 NAG C C8  1 
HETATM 11868 N N2  . NAG Q 3 .   ? 30.133  40.421  57.085  1.00 68.14  ? 401 NAG C N2  1 
HETATM 11869 O O3  . NAG Q 3 .   ? 29.460  41.275  59.788  1.00 68.56  ? 401 NAG C O3  1 
HETATM 11870 O O4  . NAG Q 3 .   ? 28.210  43.815  59.867  1.00 67.40  ? 401 NAG C O4  1 
HETATM 11871 O O5  . NAG Q 3 .   ? 30.323  44.091  56.911  1.00 63.12  ? 401 NAG C O5  1 
HETATM 11872 O O6  . NAG Q 3 .   ? 30.327  46.467  57.970  1.00 61.40  ? 401 NAG C O6  1 
HETATM 11873 O O7  . NAG Q 3 .   ? 32.058  39.506  57.835  1.00 64.37  ? 401 NAG C O7  1 
HETATM 11874 C C1  . NAG R 3 .   ? -12.124 13.808  0.602   1.00 96.09  ? 402 NAG C C1  1 
HETATM 11875 C C2  . NAG R 3 .   ? -10.784 14.290  -0.001  1.00 105.62 ? 402 NAG C C2  1 
HETATM 11876 C C3  . NAG R 3 .   ? -9.728  13.194  -0.151  1.00 102.75 ? 402 NAG C C3  1 
HETATM 11877 C C4  . NAG R 3 .   ? -9.869  12.098  0.897   1.00 101.88 ? 402 NAG C C4  1 
HETATM 11878 C C5  . NAG R 3 .   ? -11.287 11.522  0.944   1.00 101.00 ? 402 NAG C C5  1 
HETATM 11879 C C6  . NAG R 3 .   ? -11.621 10.996  2.341   1.00 98.48  ? 402 NAG C C6  1 
HETATM 11880 C C7  . NAG R 3 .   ? -10.130 15.920  -1.699  1.00 113.38 ? 402 NAG C C7  1 
HETATM 11881 C C8  . NAG R 3 .   ? -10.409 16.513  -3.052  1.00 97.53  ? 402 NAG C C8  1 
HETATM 11882 N N2  . NAG R 3 .   ? -10.953 14.947  -1.290  1.00 115.04 ? 402 NAG C N2  1 
HETATM 11883 O O3  . NAG R 3 .   ? -8.439  13.764  -0.046  1.00 86.42  ? 402 NAG C O3  1 
HETATM 11884 O O4  . NAG R 3 .   ? -8.969  11.059  0.582   1.00 100.66 ? 402 NAG C O4  1 
HETATM 11885 O O5  . NAG R 3 .   ? -12.309 12.405  0.483   1.00 98.33  ? 402 NAG C O5  1 
HETATM 11886 O O6  . NAG R 3 .   ? -12.265 9.747   2.230   1.00 94.69  ? 402 NAG C O6  1 
HETATM 11887 O O7  . NAG R 3 .   ? -9.184  16.339  -1.028  1.00 106.62 ? 402 NAG C O7  1 
HETATM 11888 C C1  . NAG S 3 .   ? -18.109 32.861  -4.428  1.00 88.51  ? 403 NAG C C1  1 
HETATM 11889 C C2  . NAG S 3 .   ? -18.480 34.330  -4.093  1.00 94.66  ? 403 NAG C C2  1 
HETATM 11890 C C3  . NAG S 3 .   ? -17.436 35.378  -4.482  1.00 96.89  ? 403 NAG C C3  1 
HETATM 11891 C C4  . NAG S 3 .   ? -16.032 34.850  -4.251  1.00 95.87  ? 403 NAG C C4  1 
HETATM 11892 C C5  . NAG S 3 .   ? -15.836 33.594  -5.089  1.00 100.00 ? 403 NAG C C5  1 
HETATM 11893 C C6  . NAG S 3 .   ? -14.418 33.048  -4.918  1.00 107.20 ? 403 NAG C C6  1 
HETATM 11894 C C7  . NAG S 3 .   ? -20.674 35.468  -4.010  1.00 115.86 ? 403 NAG C C7  1 
HETATM 11895 C C8  . NAG S 3 .   ? -21.973 35.723  -4.725  1.00 98.96  ? 403 NAG C C8  1 
HETATM 11896 N N2  . NAG S 3 .   ? -19.791 34.680  -4.640  1.00 110.93 ? 403 NAG C N2  1 
HETATM 11897 O O3  . NAG S 3 .   ? -17.618 36.555  -3.720  1.00 93.10  ? 403 NAG C O3  1 
HETATM 11898 O O4  . NAG S 3 .   ? -15.085 35.839  -4.604  1.00 85.83  ? 403 NAG C O4  1 
HETATM 11899 O O5  . NAG S 3 .   ? -16.742 32.574  -4.709  1.00 90.82  ? 403 NAG C O5  1 
HETATM 11900 O O6  . NAG S 3 .   ? -13.536 33.633  -5.851  1.00 104.49 ? 403 NAG C O6  1 
HETATM 11901 O O7  . NAG S 3 .   ? -20.478 35.980  -2.906  1.00 117.66 ? 403 NAG C O7  1 
HETATM 11902 C C1  . NAG T 3 .   ? -40.807 -1.337  -7.097  1.00 105.07 ? 201 NAG F C1  1 
HETATM 11903 C C2  . NAG T 3 .   ? -40.548 -1.281  -8.616  1.00 111.64 ? 201 NAG F C2  1 
HETATM 11904 C C3  . NAG T 3 .   ? -41.772 -1.457  -9.525  1.00 111.52 ? 201 NAG F C3  1 
HETATM 11905 C C4  . NAG T 3 .   ? -42.816 -2.400  -8.960  1.00 108.18 ? 201 NAG F C4  1 
HETATM 11906 C C5  . NAG T 3 .   ? -43.061 -2.041  -7.503  1.00 104.10 ? 201 NAG F C5  1 
HETATM 11907 C C6  . NAG T 3 .   ? -44.135 -2.928  -6.888  1.00 97.43  ? 201 NAG F C6  1 
HETATM 11908 C C7  . NAG T 3 .   ? -39.084 0.091   -10.022 1.00 122.02 ? 201 NAG F C7  1 
HETATM 11909 C C8  . NAG T 3 .   ? -38.525 1.460   -10.281 1.00 118.21 ? 201 NAG F C8  1 
HETATM 11910 N N2  . NAG T 3 .   ? -39.918 -0.020  -8.985  1.00 114.81 ? 201 NAG F N2  1 
HETATM 11911 O O3  . NAG T 3 .   ? -41.369 -1.958  -10.781 1.00 112.11 ? 201 NAG F O3  1 
HETATM 11912 O O4  . NAG T 3 .   ? -43.996 -2.278  -9.727  1.00 100.77 ? 201 NAG F O4  1 
HETATM 11913 O O5  . NAG T 3 .   ? -41.865 -2.222  -6.774  1.00 105.91 ? 201 NAG F O5  1 
HETATM 11914 O O6  . NAG T 3 .   ? -45.116 -2.101  -6.311  1.00 112.41 ? 201 NAG F O6  1 
HETATM 11915 O O7  . NAG T 3 .   ? -38.763 -0.852  -10.748 1.00 123.51 ? 201 NAG F O7  1 
HETATM 11916 O O   . HOH U 4 .   ? 39.067  5.813   73.414  1.00 49.47  ? 501 HOH A O   1 
HETATM 11917 O O   . HOH U 4 .   ? 37.357  13.938  67.498  1.00 41.07  ? 502 HOH A O   1 
HETATM 11918 O O   . HOH U 4 .   ? -14.557 15.654  47.454  1.00 44.33  ? 503 HOH A O   1 
HETATM 11919 O O   . HOH U 4 .   ? -11.577 27.087  34.346  1.00 33.21  ? 504 HOH A O   1 
HETATM 11920 O O   . HOH U 4 .   ? -14.639 28.548  36.662  1.00 36.89  ? 505 HOH A O   1 
HETATM 11921 O O   . HOH U 4 .   ? 26.394  11.019  53.608  1.00 43.23  ? 506 HOH A O   1 
HETATM 11922 O O   . HOH U 4 .   ? 35.875  10.418  78.352  1.00 50.09  ? 507 HOH A O   1 
HETATM 11923 O O   . HOH U 4 .   ? -3.883  18.253  38.054  1.00 31.87  ? 508 HOH A O   1 
HETATM 11924 O O   . HOH U 4 .   ? 37.839  3.198   73.610  1.00 54.09  ? 509 HOH A O   1 
HETATM 11925 O O   . HOH U 4 .   ? 1.556   7.775   53.476  1.00 36.29  ? 510 HOH A O   1 
HETATM 11926 O O   . HOH U 4 .   ? 31.052  27.856  55.316  1.00 50.54  ? 511 HOH A O   1 
HETATM 11927 O O   . HOH U 4 .   ? -23.651 31.378  36.371  1.00 44.18  ? 512 HOH A O   1 
HETATM 11928 O O   . HOH U 4 .   ? 41.238  18.422  76.482  1.00 40.56  ? 513 HOH A O   1 
HETATM 11929 O O   . HOH U 4 .   ? 15.814  23.462  56.846  1.00 44.68  ? 514 HOH A O   1 
HETATM 11930 O O   . HOH U 4 .   ? 9.634   22.928  61.488  1.00 42.63  ? 515 HOH A O   1 
HETATM 11931 O O   . HOH U 4 .   ? 10.489  23.739  68.007  1.00 37.89  ? 516 HOH A O   1 
HETATM 11932 O O   . HOH U 4 .   ? 13.633  15.958  50.498  1.00 36.74  ? 517 HOH A O   1 
HETATM 11933 O O   . HOH U 4 .   ? -19.538 25.066  35.793  1.00 33.31  ? 518 HOH A O   1 
HETATM 11934 O O   . HOH U 4 .   ? 34.529  15.980  74.138  1.00 37.00  ? 519 HOH A O   1 
HETATM 11935 O O   . HOH U 4 .   ? 15.832  8.749   49.446  1.00 42.99  ? 520 HOH A O   1 
HETATM 11936 O O   . HOH U 4 .   ? 24.438  7.445   64.138  1.00 49.61  ? 521 HOH A O   1 
HETATM 11937 O O   . HOH U 4 .   ? 26.699  21.286  61.437  1.00 42.41  ? 522 HOH A O   1 
HETATM 11938 O O   . HOH U 4 .   ? 20.542  21.293  56.979  1.00 36.09  ? 523 HOH A O   1 
HETATM 11939 O O   . HOH V 4 .   ? 55.829  -1.612  32.091  1.00 48.26  ? 501 HOH E O   1 
HETATM 11940 O O   . HOH V 4 .   ? 33.497  7.654   35.403  1.00 40.20  ? 502 HOH E O   1 
HETATM 11941 O O   . HOH V 4 .   ? 0.953   5.342   27.853  1.00 31.65  ? 503 HOH E O   1 
HETATM 11942 O O   . HOH V 4 .   ? 39.841  14.211  39.655  1.00 33.46  ? 504 HOH E O   1 
HETATM 11943 O O   . HOH V 4 .   ? -17.902 0.604   31.556  1.00 40.25  ? 505 HOH E O   1 
HETATM 11944 O O   . HOH V 4 .   ? 48.691  -1.511  39.546  1.00 36.41  ? 506 HOH E O   1 
HETATM 11945 O O   . HOH V 4 .   ? 46.873  -4.347  28.910  1.00 35.79  ? 507 HOH E O   1 
HETATM 11946 O O   . HOH V 4 .   ? -42.414 -1.489  15.135  1.00 39.80  ? 508 HOH E O   1 
HETATM 11947 O O   . HOH V 4 .   ? 23.201  -5.102  38.731  1.00 42.54  ? 509 HOH E O   1 
HETATM 11948 O O   . HOH V 4 .   ? 37.161  11.337  26.824  1.00 43.41  ? 510 HOH E O   1 
HETATM 11949 O O   . HOH V 4 .   ? 41.120  17.334  30.038  1.00 39.56  ? 511 HOH E O   1 
HETATM 11950 O O   . HOH V 4 .   ? 54.984  6.432   47.538  1.00 47.11  ? 512 HOH E O   1 
HETATM 11951 O O   . HOH V 4 .   ? 23.060  -3.763  36.540  1.00 42.21  ? 513 HOH E O   1 
HETATM 11952 O O   . HOH W 4 .   ? 14.169  21.132  49.200  1.00 37.51  ? 301 HOH B O   1 
HETATM 11953 O O   . HOH W 4 .   ? -25.746 17.440  32.542  1.00 26.35  ? 302 HOH B O   1 
HETATM 11954 O O   . HOH W 4 .   ? -47.800 7.502   35.140  1.00 45.76  ? 303 HOH B O   1 
HETATM 11955 O O   . HOH W 4 .   ? -29.249 13.582  24.846  1.00 29.34  ? 304 HOH B O   1 
HETATM 11956 O O   . HOH W 4 .   ? -61.572 17.110  36.291  1.00 50.76  ? 305 HOH B O   1 
HETATM 11957 O O   . HOH W 4 .   ? -35.644 18.225  39.094  1.00 47.93  ? 306 HOH B O   1 
HETATM 11958 O O   . HOH W 4 .   ? -45.009 22.946  31.209  1.00 50.85  ? 307 HOH B O   1 
HETATM 11959 O O   . HOH X 4 .   ? 24.492  32.140  48.548  1.00 40.67  ? 501 HOH C O   1 
HETATM 11960 O O   . HOH X 4 .   ? 24.783  22.494  36.354  1.00 35.95  ? 502 HOH C O   1 
HETATM 11961 O O   . HOH X 4 .   ? 19.633  40.527  44.943  1.00 36.18  ? 503 HOH C O   1 
HETATM 11962 O O   . HOH X 4 .   ? 1.626   19.414  23.880  1.00 37.44  ? 504 HOH C O   1 
HETATM 11963 O O   . HOH X 4 .   ? 50.593  22.264  43.264  1.00 38.65  ? 505 HOH C O   1 
HETATM 11964 O O   . HOH X 4 .   ? 53.495  15.128  34.688  1.00 49.37  ? 506 HOH C O   1 
HETATM 11965 O O   . HOH X 4 .   ? 15.875  27.806  14.680  1.00 52.64  ? 507 HOH C O   1 
HETATM 11966 O O   . HOH X 4 .   ? -10.159 14.147  5.570   1.00 46.57  ? 508 HOH C O   1 
HETATM 11967 O O   . HOH X 4 .   ? 5.840   27.950  26.470  1.00 32.04  ? 509 HOH C O   1 
HETATM 11968 O O   . HOH X 4 .   ? -14.858 27.775  0.083   1.00 38.13  ? 510 HOH C O   1 
HETATM 11969 O O   . HOH X 4 .   ? 16.151  25.182  19.529  1.00 39.05  ? 511 HOH C O   1 
HETATM 11970 O O   . HOH X 4 .   ? 31.402  25.699  29.425  1.00 39.21  ? 512 HOH C O   1 
HETATM 11971 O O   . HOH X 4 .   ? 56.060  30.534  31.811  1.00 54.94  ? 513 HOH C O   1 
HETATM 11972 O O   . HOH X 4 .   ? -33.289 24.242  1.413   1.00 41.18  ? 514 HOH C O   1 
HETATM 11973 O O   . HOH X 4 .   ? 49.493  40.515  46.563  1.00 41.23  ? 515 HOH C O   1 
HETATM 11974 O O   . HOH X 4 .   ? -27.011 21.510  7.723   1.00 40.65  ? 516 HOH C O   1 
HETATM 11975 O O   . HOH X 4 .   ? 34.251  37.114  39.798  1.00 57.77  ? 517 HOH C O   1 
HETATM 11976 O O   . HOH Y 4 .   ? 1.806   6.196   31.951  1.00 27.04  ? 301 HOH F O   1 
HETATM 11977 O O   . HOH Y 4 .   ? -33.562 1.082   0.479   1.00 50.59  ? 302 HOH F O   1 
HETATM 11978 O O   . HOH Y 4 .   ? -40.523 10.869  16.803  1.00 46.14  ? 303 HOH F O   1 
HETATM 11979 O O   . HOH Y 4 .   ? -38.488 -10.897 14.771  1.00 53.17  ? 304 HOH F O   1 
HETATM 11980 O O   . HOH Y 4 .   ? -40.085 -3.257  10.798  1.00 58.51  ? 305 HOH F O   1 
HETATM 11981 O O   . HOH Y 4 .   ? 14.201  3.938   38.851  1.00 37.37  ? 306 HOH F O   1 
HETATM 11982 O O   . HOH Z 4 .   ? -32.248 28.681  -4.518  1.00 41.71  ? 201 HOH D O   1 
HETATM 11983 O O   . HOH Z 4 .   ? -43.220 17.445  2.312   1.00 37.66  ? 202 HOH D O   1 
HETATM 11984 O O   . HOH Z 4 .   ? -49.404 23.351  15.741  1.00 46.91  ? 203 HOH D O   1 
HETATM 11985 O O   . HOH Z 4 .   ? -37.711 27.429  1.967   1.00 60.79  ? 204 HOH D O   1 
HETATM 11986 O O   . HOH Z 4 .   ? -18.881 22.627  15.130  1.00 37.92  ? 205 HOH D O   1 
HETATM 11987 O O   . HOH Z 4 .   ? -22.994 9.135   16.885  1.00 59.54  ? 206 HOH D O   1 
# 
_database_PDB_caveat.id     1 
_database_PDB_caveat.text   'Chirality error at NAG406A, NAG402E, NAG201B, and NAG201F.' 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   -3  ?   ?   ?   A . n 
A 1 2   ASP 2   -2  ?   ?   ?   A . n 
A 1 3   PRO 3   -1  ?   ?   ?   A . n 
A 1 4   GLY 4   0   0   GLY GLY A . n 
A 1 5   ASP 5   1   1   ASP ASP A . n 
A 1 6   HIS 6   2   2   HIS HIS A . n 
A 1 7   ILE 7   3   3   ILE ILE A . n 
A 1 8   CYS 8   4   4   CYS CYS A . n 
A 1 9   ILE 9   5   5   ILE ILE A . n 
A 1 10  GLY 10  6   6   GLY GLY A . n 
A 1 11  TYR 11  7   7   TYR TYR A . n 
A 1 12  HIS 12  8   8   HIS HIS A . n 
A 1 13  ALA 13  9   9   ALA ALA A . n 
A 1 14  ASN 14  10  10  ASN ASN A . n 
A 1 15  ASN 15  11  11  ASN ASN A . n 
A 1 16  SER 16  12  12  SER SER A . n 
A 1 17  THR 17  13  13  THR THR A . n 
A 1 18  GLU 18  14  14  GLU GLU A . n 
A 1 19  GLN 19  15  15  GLN GLN A . n 
A 1 20  VAL 20  16  16  VAL VAL A . n 
A 1 21  ASP 21  17  17  ASP ASP A . n 
A 1 22  THR 22  18  18  THR THR A . n 
A 1 23  ILE 23  19  19  ILE ILE A . n 
A 1 24  MET 24  20  20  MET MET A . n 
A 1 25  GLU 25  21  21  GLU GLU A . n 
A 1 26  LYS 26  22  22  LYS LYS A . n 
A 1 27  ASN 27  23  23  ASN ASN A . n 
A 1 28  VAL 28  24  24  VAL VAL A . n 
A 1 29  THR 29  25  25  THR THR A . n 
A 1 30  VAL 30  26  26  VAL VAL A . n 
A 1 31  THR 31  27  27  THR THR A . n 
A 1 32  HIS 32  28  28  HIS HIS A . n 
A 1 33  ALA 33  29  29  ALA ALA A . n 
A 1 34  GLN 34  30  30  GLN GLN A . n 
A 1 35  ASP 35  31  31  ASP ASP A . n 
A 1 36  ILE 36  32  32  ILE ILE A . n 
A 1 37  LEU 37  33  33  LEU LEU A . n 
A 1 38  GLU 38  34  34  GLU GLU A . n 
A 1 39  LYS 39  35  35  LYS LYS A . n 
A 1 40  THR 40  36  36  THR THR A . n 
A 1 41  HIS 41  37  37  HIS HIS A . n 
A 1 42  ASN 42  38  38  ASN ASN A . n 
A 1 43  GLY 43  39  39  GLY GLY A . n 
A 1 44  LYS 44  40  40  LYS LYS A . n 
A 1 45  LEU 45  41  41  LEU LEU A . n 
A 1 46  CYS 46  42  42  CYS CYS A . n 
A 1 47  ASP 47  43  43  ASP ASP A . n 
A 1 48  LEU 48  44  44  LEU LEU A . n 
A 1 49  ASN 49  45  45  ASN ASN A . n 
A 1 50  GLY 50  46  46  GLY GLY A . n 
A 1 51  VAL 51  47  47  VAL VAL A . n 
A 1 52  LYS 52  48  48  LYS LYS A . n 
A 1 53  PRO 53  49  49  PRO PRO A . n 
A 1 54  LEU 54  50  50  LEU LEU A . n 
A 1 55  ILE 55  51  51  ILE ILE A . n 
A 1 56  LEU 56  52  52  LEU LEU A . n 
A 1 57  LYS 57  53  53  LYS LYS A . n 
A 1 58  ASP 58  54  54  ASP ASP A . n 
A 1 59  CYS 59  55  55  CYS CYS A . n 
A 1 60  SER 60  56  56  SER SER A . n 
A 1 61  VAL 61  57  57  VAL VAL A . n 
A 1 62  ALA 62  58  58  ALA ALA A . n 
A 1 63  GLY 63  59  59  GLY GLY A . n 
A 1 64  TRP 64  60  60  TRP TRP A . n 
A 1 65  LEU 65  61  61  LEU LEU A . n 
A 1 66  LEU 66  62  62  LEU LEU A . n 
A 1 67  GLY 67  63  63  GLY GLY A . n 
A 1 68  ASN 68  64  64  ASN ASN A . n 
A 1 69  PRO 69  65  65  PRO PRO A . n 
A 1 70  MET 70  66  66  MET MET A . n 
A 1 71  CYS 71  67  67  CYS CYS A . n 
A 1 72  ASP 72  68  68  ASP ASP A . n 
A 1 73  GLU 73  69  69  GLU GLU A . n 
A 1 74  PHE 74  70  70  PHE PHE A . n 
A 1 75  ILE 75  71  71  ILE ILE A . n 
A 1 76  ASN 76  72  72  ASN ASN A . n 
A 1 77  VAL 77  73  73  VAL VAL A . n 
A 1 78  PRO 78  74  74  PRO PRO A . n 
A 1 79  GLU 79  75  75  GLU GLU A . n 
A 1 80  TRP 80  76  76  TRP TRP A . n 
A 1 81  SER 81  77  77  SER SER A . n 
A 1 82  TYR 82  78  78  TYR TYR A . n 
A 1 83  ILE 83  79  79  ILE ILE A . n 
A 1 84  VAL 84  80  80  VAL VAL A . n 
A 1 85  GLU 85  81  81  GLU GLU A . n 
A 1 86  LYS 86  82  82  LYS LYS A . n 
A 1 87  ALA 87  83  83  ALA ALA A . n 
A 1 88  ASN 88  84  84  ASN ASN A . n 
A 1 89  PRO 89  85  85  PRO PRO A . n 
A 1 90  ALA 90  86  86  ALA ALA A . n 
A 1 91  ASN 91  87  87  ASN ASN A . n 
A 1 92  ASP 92  88  88  ASP ASP A . n 
A 1 93  LEU 93  89  89  LEU LEU A . n 
A 1 94  CYS 94  90  90  CYS CYS A . n 
A 1 95  TYR 95  91  91  TYR TYR A . n 
A 1 96  PRO 96  92  92  PRO PRO A . n 
A 1 97  GLY 97  93  93  GLY GLY A . n 
A 1 98  ASN 98  94  94  ASN ASN A . n 
A 1 99  PHE 99  95  95  PHE PHE A . n 
A 1 100 ASN 100 96  96  ASN ASN A . n 
A 1 101 ASP 101 97  97  ASP ASP A . n 
A 1 102 TYR 102 98  98  TYR TYR A . n 
A 1 103 GLU 103 99  99  GLU GLU A . n 
A 1 104 GLU 104 100 100 GLU GLU A . n 
A 1 105 LEU 105 101 101 LEU LEU A . n 
A 1 106 LYS 106 102 102 LYS LYS A . n 
A 1 107 HIS 107 103 103 HIS HIS A . n 
A 1 108 LEU 108 104 104 LEU LEU A . n 
A 1 109 LEU 109 105 105 LEU LEU A . n 
A 1 110 SER 110 106 106 SER SER A . n 
A 1 111 ARG 111 107 107 ARG ARG A . n 
A 1 112 ILE 112 108 108 ILE ILE A . n 
A 1 113 ASN 113 109 109 ASN ASN A . n 
A 1 114 HIS 114 110 110 HIS HIS A . n 
A 1 115 PHE 115 111 111 PHE PHE A . n 
A 1 116 GLU 116 112 112 GLU GLU A . n 
A 1 117 LYS 117 113 113 LYS LYS A . n 
A 1 118 ILE 118 114 114 ILE ILE A . n 
A 1 119 GLN 119 115 115 GLN GLN A . n 
A 1 120 ILE 120 116 116 ILE ILE A . n 
A 1 121 ILE 121 117 117 ILE ILE A . n 
A 1 122 PRO 122 118 118 PRO PRO A . n 
A 1 123 LYS 123 119 119 LYS LYS A . n 
A 1 124 ASN 124 120 120 ASN ASN A . n 
A 1 125 SER 125 121 121 SER SER A . n 
A 1 126 TRP 126 122 122 TRP TRP A . n 
A 1 127 SER 127 123 123 SER SER A . n 
A 1 128 ASP 128 124 124 ASP ASP A . n 
A 1 129 HIS 129 125 125 HIS HIS A . n 
A 1 130 GLU 130 126 126 GLU GLU A . n 
A 1 131 ALA 131 127 127 ALA ALA A . n 
A 1 132 SER 132 128 128 SER SER A . n 
A 1 133 LEU 133 129 129 LEU LEU A . n 
A 1 134 GLY 134 130 130 GLY GLY A . n 
A 1 135 VAL 135 131 131 VAL VAL A . n 
A 1 136 SER 136 132 132 SER SER A . n 
A 1 137 ALA 137 133 133 ALA ALA A . n 
A 1 138 ALA 138 134 134 ALA ALA A . n 
A 1 139 CYS 139 135 135 CYS CYS A . n 
A 1 140 PRO 140 136 136 PRO PRO A . n 
A 1 141 TYR 141 137 137 TYR TYR A . n 
A 1 142 GLN 142 138 138 GLN GLN A . n 
A 1 143 GLY 143 139 139 GLY GLY A . n 
A 1 144 LYS 144 140 140 LYS LYS A . n 
A 1 145 SER 145 141 141 SER SER A . n 
A 1 146 SER 146 142 142 SER SER A . n 
A 1 147 PHE 147 143 143 PHE PHE A . n 
A 1 148 PHE 148 144 144 PHE PHE A . n 
A 1 149 ARG 149 145 145 ARG ARG A . n 
A 1 150 ASN 150 146 146 ASN ASN A . n 
A 1 151 VAL 151 147 147 VAL VAL A . n 
A 1 152 VAL 152 148 148 VAL VAL A . n 
A 1 153 TRP 153 149 149 TRP TRP A . n 
A 1 154 LEU 154 150 150 LEU LEU A . n 
A 1 155 ILE 155 151 151 ILE ILE A . n 
A 1 156 LYS 156 152 152 LYS LYS A . n 
A 1 157 LYS 157 153 153 LYS LYS A . n 
A 1 158 ASP 158 154 154 ASP ASP A . n 
A 1 159 ASN 159 155 155 ASN ASN A . n 
A 1 160 ALA 160 156 156 ALA ALA A . n 
A 1 161 TYR 161 157 157 TYR TYR A . n 
A 1 162 PRO 162 158 158 PRO PRO A . n 
A 1 163 THR 163 159 159 THR THR A . n 
A 1 164 ILE 164 160 160 ILE ILE A . n 
A 1 165 LYS 165 161 161 LYS LYS A . n 
A 1 166 LYS 166 162 162 LYS LYS A . n 
A 1 167 GLY 167 163 163 GLY GLY A . n 
A 1 168 TYR 168 164 164 TYR TYR A . n 
A 1 169 ASN 169 165 165 ASN ASN A . n 
A 1 170 ASN 170 166 166 ASN ASN A . n 
A 1 171 THR 171 167 167 THR THR A . n 
A 1 172 ASN 172 168 168 ASN ASN A . n 
A 1 173 GLN 173 169 169 GLN GLN A . n 
A 1 174 GLU 174 170 170 GLU GLU A . n 
A 1 175 ASP 175 171 171 ASP ASP A . n 
A 1 176 LEU 176 172 172 LEU LEU A . n 
A 1 177 LEU 177 173 173 LEU LEU A . n 
A 1 178 VAL 178 174 174 VAL VAL A . n 
A 1 179 LEU 179 175 175 LEU LEU A . n 
A 1 180 TRP 180 176 176 TRP TRP A . n 
A 1 181 GLY 181 177 177 GLY GLY A . n 
A 1 182 ILE 182 178 178 ILE ILE A . n 
A 1 183 HIS 183 179 179 HIS HIS A . n 
A 1 184 HIS 184 180 180 HIS HIS A . n 
A 1 185 PRO 185 181 181 PRO PRO A . n 
A 1 186 ASN 186 182 182 ASN ASN A . n 
A 1 187 ASP 187 183 183 ASP ASP A . n 
A 1 188 GLU 188 184 184 GLU GLU A . n 
A 1 189 ALA 189 185 185 ALA ALA A . n 
A 1 190 GLU 190 186 186 GLU GLU A . n 
A 1 191 GLN 191 187 187 GLN GLN A . n 
A 1 192 THR 192 188 188 THR THR A . n 
A 1 193 ARG 193 189 189 ARG ARG A . n 
A 1 194 LEU 194 190 190 LEU LEU A . n 
A 1 195 TYR 195 191 191 TYR TYR A . n 
A 1 196 GLN 196 192 192 GLN GLN A . n 
A 1 197 ASN 197 193 193 ASN ASN A . n 
A 1 198 PRO 198 194 194 PRO PRO A . n 
A 1 199 THR 199 195 195 THR THR A . n 
A 1 200 THR 200 196 196 THR THR A . n 
A 1 201 TYR 201 197 197 TYR TYR A . n 
A 1 202 ILE 202 198 198 ILE ILE A . n 
A 1 203 SER 203 199 199 SER SER A . n 
A 1 204 ILE 204 200 200 ILE ILE A . n 
A 1 205 GLY 205 201 201 GLY GLY A . n 
A 1 206 THR 206 202 202 THR THR A . n 
A 1 207 SER 207 203 203 SER SER A . n 
A 1 208 THR 208 204 204 THR THR A . n 
A 1 209 LEU 209 205 205 LEU LEU A . n 
A 1 210 ASN 210 206 206 ASN ASN A . n 
A 1 211 GLN 211 207 207 GLN GLN A . n 
A 1 212 ARG 212 208 208 ARG ARG A . n 
A 1 213 LEU 213 209 209 LEU LEU A . n 
A 1 214 VAL 214 210 210 VAL VAL A . n 
A 1 215 PRO 215 211 211 PRO PRO A . n 
A 1 216 LYS 216 212 212 LYS LYS A . n 
A 1 217 ILE 217 213 213 ILE ILE A . n 
A 1 218 ALA 218 214 214 ALA ALA A . n 
A 1 219 THR 219 215 215 THR THR A . n 
A 1 220 ARG 220 216 216 ARG ARG A . n 
A 1 221 SER 221 217 217 SER SER A . n 
A 1 222 LYS 222 218 218 LYS LYS A . n 
A 1 223 ILE 223 219 219 ILE ILE A . n 
A 1 224 ASN 224 220 220 ASN ASN A . n 
A 1 225 GLY 225 221 221 GLY GLY A . n 
A 1 226 GLN 226 222 222 GLN GLN A . n 
A 1 227 SER 227 223 223 SER SER A . n 
A 1 228 GLY 228 224 224 GLY GLY A . n 
A 1 229 ARG 229 225 225 ARG ARG A . n 
A 1 230 ILE 230 226 226 ILE ILE A . n 
A 1 231 ASP 231 227 227 ASP ASP A . n 
A 1 232 PHE 232 228 228 PHE PHE A . n 
A 1 233 PHE 233 229 229 PHE PHE A . n 
A 1 234 TRP 234 230 230 TRP TRP A . n 
A 1 235 THR 235 231 231 THR THR A . n 
A 1 236 ILE 236 232 232 ILE ILE A . n 
A 1 237 LEU 237 233 233 LEU LEU A . n 
A 1 238 LYS 238 234 234 LYS LYS A . n 
A 1 239 PRO 239 235 235 PRO PRO A . n 
A 1 240 ASN 240 236 236 ASN ASN A . n 
A 1 241 ASP 241 237 237 ASP ASP A . n 
A 1 242 ALA 242 238 238 ALA ALA A . n 
A 1 243 ILE 243 239 239 ILE ILE A . n 
A 1 244 HIS 244 240 240 HIS HIS A . n 
A 1 245 PHE 245 241 241 PHE PHE A . n 
A 1 246 GLU 246 242 242 GLU GLU A . n 
A 1 247 SER 247 243 243 SER SER A . n 
A 1 248 ASN 248 244 244 ASN ASN A . n 
A 1 249 GLY 249 245 245 GLY GLY A . n 
A 1 250 ASN 250 246 246 ASN ASN A . n 
A 1 251 PHE 251 247 247 PHE PHE A . n 
A 1 252 ILE 252 248 248 ILE ILE A . n 
A 1 253 ALA 253 249 249 ALA ALA A . n 
A 1 254 PRO 254 250 250 PRO PRO A . n 
A 1 255 GLU 255 251 251 GLU GLU A . n 
A 1 256 TYR 256 252 252 TYR TYR A . n 
A 1 257 ALA 257 253 253 ALA ALA A . n 
A 1 258 TYR 258 254 254 TYR TYR A . n 
A 1 259 LYS 259 255 255 LYS LYS A . n 
A 1 260 ILE 260 256 256 ILE ILE A . n 
A 1 261 VAL 261 257 257 VAL VAL A . n 
A 1 262 LYS 262 258 258 LYS LYS A . n 
A 1 263 LYS 263 259 259 LYS LYS A . n 
A 1 264 GLY 264 260 260 GLY GLY A . n 
A 1 265 ASP 265 261 261 ASP ASP A . n 
A 1 266 SER 266 262 262 SER SER A . n 
A 1 267 THR 267 263 263 THR THR A . n 
A 1 268 ILE 268 264 264 ILE ILE A . n 
A 1 269 MET 269 265 265 MET MET A . n 
A 1 270 LYS 270 266 266 LYS LYS A . n 
A 1 271 SER 271 267 267 SER SER A . n 
A 1 272 GLU 272 268 268 GLU GLU A . n 
A 1 273 VAL 273 269 269 VAL VAL A . n 
A 1 274 GLU 274 270 270 GLU GLU A . n 
A 1 275 TYR 275 271 271 TYR TYR A . n 
A 1 276 GLY 276 272 272 GLY GLY A . n 
A 1 277 ASN 277 273 273 ASN ASN A . n 
A 1 278 CYS 278 274 274 CYS CYS A . n 
A 1 279 ASN 279 275 275 ASN ASN A . n 
A 1 280 THR 280 276 276 THR THR A . n 
A 1 281 ARG 281 277 277 ARG ARG A . n 
A 1 282 CYS 282 278 278 CYS CYS A . n 
A 1 283 GLN 283 279 279 GLN GLN A . n 
A 1 284 THR 284 280 280 THR THR A . n 
A 1 285 PRO 285 281 281 PRO PRO A . n 
A 1 286 ILE 286 282 282 ILE ILE A . n 
A 1 287 GLY 287 283 283 GLY GLY A . n 
A 1 288 ALA 288 284 284 ALA ALA A . n 
A 1 289 ILE 289 285 285 ILE ILE A . n 
A 1 290 ASN 290 286 286 ASN ASN A . n 
A 1 291 SER 291 287 287 SER SER A . n 
A 1 292 SER 292 288 288 SER SER A . n 
A 1 293 MET 293 289 289 MET MET A . n 
A 1 294 PRO 294 290 290 PRO PRO A . n 
A 1 295 PHE 295 291 291 PHE PHE A . n 
A 1 296 HIS 296 292 292 HIS HIS A . n 
A 1 297 ASN 297 293 293 ASN ASN A . n 
A 1 298 ILE 298 294 294 ILE ILE A . n 
A 1 299 HIS 299 295 295 HIS HIS A . n 
A 1 300 PRO 300 296 296 PRO PRO A . n 
A 1 301 LEU 301 297 297 LEU LEU A . n 
A 1 302 THR 302 298 298 THR THR A . n 
A 1 303 ILE 303 299 299 ILE ILE A . n 
A 1 304 GLY 304 300 300 GLY GLY A . n 
A 1 305 GLU 305 301 301 GLU GLU A . n 
A 1 306 CYS 306 302 302 CYS CYS A . n 
A 1 307 PRO 307 303 303 PRO PRO A . n 
A 1 308 LYS 308 304 304 LYS LYS A . n 
A 1 309 TYR 309 305 305 TYR TYR A . n 
A 1 310 VAL 310 306 306 VAL VAL A . n 
A 1 311 LYS 311 307 307 LYS LYS A . n 
A 1 312 SER 312 308 308 SER SER A . n 
A 1 313 ASN 313 309 309 ASN ASN A . n 
A 1 314 LYS 314 310 310 LYS LYS A . n 
A 1 315 LEU 315 311 311 LEU LEU A . n 
A 1 316 VAL 316 312 312 VAL VAL A . n 
A 1 317 LEU 317 313 313 LEU LEU A . n 
A 1 318 ALA 318 314 314 ALA ALA A . n 
A 1 319 THR 319 315 315 THR THR A . n 
A 1 320 GLY 320 316 316 GLY GLY A . n 
A 1 321 LEU 321 317 317 LEU LEU A . n 
A 1 322 ARG 322 318 318 ARG ARG A . n 
A 1 323 ASN 323 319 319 ASN ASN A . n 
A 1 324 SER 324 320 320 SER SER A . n 
A 1 325 PRO 325 321 321 PRO PRO A . n 
A 1 326 GLN 326 322 ?   ?   ?   A . n 
A 1 327 ARG 327 323 ?   ?   ?   A . n 
A 1 328 GLU 328 324 ?   ?   ?   A . n 
A 1 329 THR 329 325 ?   ?   ?   A . n 
A 1 330 ARG 330 326 ?   ?   ?   A . n 
B 1 1   ALA 1   -3  ?   ?   ?   E . n 
B 1 2   ASP 2   -2  ?   ?   ?   E . n 
B 1 3   PRO 3   -1  ?   ?   ?   E . n 
B 1 4   GLY 4   0   0   GLY GLY E . n 
B 1 5   ASP 5   1   1   ASP ASP E . n 
B 1 6   HIS 6   2   2   HIS HIS E . n 
B 1 7   ILE 7   3   3   ILE ILE E . n 
B 1 8   CYS 8   4   4   CYS CYS E . n 
B 1 9   ILE 9   5   5   ILE ILE E . n 
B 1 10  GLY 10  6   6   GLY GLY E . n 
B 1 11  TYR 11  7   7   TYR TYR E . n 
B 1 12  HIS 12  8   8   HIS HIS E . n 
B 1 13  ALA 13  9   9   ALA ALA E . n 
B 1 14  ASN 14  10  10  ASN ASN E . n 
B 1 15  ASN 15  11  11  ASN ASN E . n 
B 1 16  SER 16  12  12  SER SER E . n 
B 1 17  THR 17  13  13  THR THR E . n 
B 1 18  GLU 18  14  14  GLU GLU E . n 
B 1 19  GLN 19  15  15  GLN GLN E . n 
B 1 20  VAL 20  16  16  VAL VAL E . n 
B 1 21  ASP 21  17  17  ASP ASP E . n 
B 1 22  THR 22  18  18  THR THR E . n 
B 1 23  ILE 23  19  19  ILE ILE E . n 
B 1 24  MET 24  20  20  MET MET E . n 
B 1 25  GLU 25  21  21  GLU GLU E . n 
B 1 26  LYS 26  22  22  LYS LYS E . n 
B 1 27  ASN 27  23  23  ASN ASN E . n 
B 1 28  VAL 28  24  24  VAL VAL E . n 
B 1 29  THR 29  25  25  THR THR E . n 
B 1 30  VAL 30  26  26  VAL VAL E . n 
B 1 31  THR 31  27  27  THR THR E . n 
B 1 32  HIS 32  28  28  HIS HIS E . n 
B 1 33  ALA 33  29  29  ALA ALA E . n 
B 1 34  GLN 34  30  30  GLN GLN E . n 
B 1 35  ASP 35  31  31  ASP ASP E . n 
B 1 36  ILE 36  32  32  ILE ILE E . n 
B 1 37  LEU 37  33  33  LEU LEU E . n 
B 1 38  GLU 38  34  34  GLU GLU E . n 
B 1 39  LYS 39  35  35  LYS LYS E . n 
B 1 40  THR 40  36  36  THR THR E . n 
B 1 41  HIS 41  37  37  HIS HIS E . n 
B 1 42  ASN 42  38  38  ASN ASN E . n 
B 1 43  GLY 43  39  39  GLY GLY E . n 
B 1 44  LYS 44  40  40  LYS LYS E . n 
B 1 45  LEU 45  41  41  LEU LEU E . n 
B 1 46  CYS 46  42  42  CYS CYS E . n 
B 1 47  ASP 47  43  43  ASP ASP E . n 
B 1 48  LEU 48  44  44  LEU LEU E . n 
B 1 49  ASN 49  45  45  ASN ASN E . n 
B 1 50  GLY 50  46  46  GLY GLY E . n 
B 1 51  VAL 51  47  47  VAL VAL E . n 
B 1 52  LYS 52  48  48  LYS LYS E . n 
B 1 53  PRO 53  49  49  PRO PRO E . n 
B 1 54  LEU 54  50  50  LEU LEU E . n 
B 1 55  ILE 55  51  51  ILE ILE E . n 
B 1 56  LEU 56  52  52  LEU LEU E . n 
B 1 57  LYS 57  53  53  LYS LYS E . n 
B 1 58  ASP 58  54  54  ASP ASP E . n 
B 1 59  CYS 59  55  55  CYS CYS E . n 
B 1 60  SER 60  56  56  SER SER E . n 
B 1 61  VAL 61  57  57  VAL VAL E . n 
B 1 62  ALA 62  58  58  ALA ALA E . n 
B 1 63  GLY 63  59  59  GLY GLY E . n 
B 1 64  TRP 64  60  60  TRP TRP E . n 
B 1 65  LEU 65  61  61  LEU LEU E . n 
B 1 66  LEU 66  62  62  LEU LEU E . n 
B 1 67  GLY 67  63  63  GLY GLY E . n 
B 1 68  ASN 68  64  64  ASN ASN E . n 
B 1 69  PRO 69  65  65  PRO PRO E . n 
B 1 70  MET 70  66  66  MET MET E . n 
B 1 71  CYS 71  67  67  CYS CYS E . n 
B 1 72  ASP 72  68  68  ASP ASP E . n 
B 1 73  GLU 73  69  69  GLU GLU E . n 
B 1 74  PHE 74  70  70  PHE PHE E . n 
B 1 75  ILE 75  71  71  ILE ILE E . n 
B 1 76  ASN 76  72  72  ASN ASN E . n 
B 1 77  VAL 77  73  73  VAL VAL E . n 
B 1 78  PRO 78  74  74  PRO PRO E . n 
B 1 79  GLU 79  75  75  GLU GLU E . n 
B 1 80  TRP 80  76  76  TRP TRP E . n 
B 1 81  SER 81  77  77  SER SER E . n 
B 1 82  TYR 82  78  78  TYR TYR E . n 
B 1 83  ILE 83  79  79  ILE ILE E . n 
B 1 84  VAL 84  80  80  VAL VAL E . n 
B 1 85  GLU 85  81  81  GLU GLU E . n 
B 1 86  LYS 86  82  82  LYS LYS E . n 
B 1 87  ALA 87  83  83  ALA ALA E . n 
B 1 88  ASN 88  84  84  ASN ASN E . n 
B 1 89  PRO 89  85  85  PRO PRO E . n 
B 1 90  ALA 90  86  86  ALA ALA E . n 
B 1 91  ASN 91  87  87  ASN ASN E . n 
B 1 92  ASP 92  88  88  ASP ASP E . n 
B 1 93  LEU 93  89  89  LEU LEU E . n 
B 1 94  CYS 94  90  90  CYS CYS E . n 
B 1 95  TYR 95  91  91  TYR TYR E . n 
B 1 96  PRO 96  92  92  PRO PRO E . n 
B 1 97  GLY 97  93  93  GLY GLY E . n 
B 1 98  ASN 98  94  94  ASN ASN E . n 
B 1 99  PHE 99  95  95  PHE PHE E . n 
B 1 100 ASN 100 96  96  ASN ASN E . n 
B 1 101 ASP 101 97  97  ASP ASP E . n 
B 1 102 TYR 102 98  98  TYR TYR E . n 
B 1 103 GLU 103 99  99  GLU GLU E . n 
B 1 104 GLU 104 100 100 GLU GLU E . n 
B 1 105 LEU 105 101 101 LEU LEU E . n 
B 1 106 LYS 106 102 102 LYS LYS E . n 
B 1 107 HIS 107 103 103 HIS HIS E . n 
B 1 108 LEU 108 104 104 LEU LEU E . n 
B 1 109 LEU 109 105 105 LEU LEU E . n 
B 1 110 SER 110 106 106 SER SER E . n 
B 1 111 ARG 111 107 107 ARG ARG E . n 
B 1 112 ILE 112 108 108 ILE ILE E . n 
B 1 113 ASN 113 109 109 ASN ASN E . n 
B 1 114 HIS 114 110 110 HIS HIS E . n 
B 1 115 PHE 115 111 111 PHE PHE E . n 
B 1 116 GLU 116 112 112 GLU GLU E . n 
B 1 117 LYS 117 113 113 LYS LYS E . n 
B 1 118 ILE 118 114 114 ILE ILE E . n 
B 1 119 GLN 119 115 115 GLN GLN E . n 
B 1 120 ILE 120 116 116 ILE ILE E . n 
B 1 121 ILE 121 117 117 ILE ILE E . n 
B 1 122 PRO 122 118 118 PRO PRO E . n 
B 1 123 LYS 123 119 119 LYS LYS E . n 
B 1 124 ASN 124 120 120 ASN ASN E . n 
B 1 125 SER 125 121 121 SER SER E . n 
B 1 126 TRP 126 122 122 TRP TRP E . n 
B 1 127 SER 127 123 123 SER SER E . n 
B 1 128 ASP 128 124 124 ASP ASP E . n 
B 1 129 HIS 129 125 125 HIS HIS E . n 
B 1 130 GLU 130 126 126 GLU GLU E . n 
B 1 131 ALA 131 127 127 ALA ALA E . n 
B 1 132 SER 132 128 128 SER SER E . n 
B 1 133 LEU 133 129 129 LEU LEU E . n 
B 1 134 GLY 134 130 130 GLY GLY E . n 
B 1 135 VAL 135 131 131 VAL VAL E . n 
B 1 136 SER 136 132 132 SER SER E . n 
B 1 137 ALA 137 133 133 ALA ALA E . n 
B 1 138 ALA 138 134 134 ALA ALA E . n 
B 1 139 CYS 139 135 135 CYS CYS E . n 
B 1 140 PRO 140 136 136 PRO PRO E . n 
B 1 141 TYR 141 137 137 TYR TYR E . n 
B 1 142 GLN 142 138 138 GLN GLN E . n 
B 1 143 GLY 143 139 139 GLY GLY E . n 
B 1 144 LYS 144 140 140 LYS LYS E . n 
B 1 145 SER 145 141 141 SER SER E . n 
B 1 146 SER 146 142 142 SER SER E . n 
B 1 147 PHE 147 143 143 PHE PHE E . n 
B 1 148 PHE 148 144 144 PHE PHE E . n 
B 1 149 ARG 149 145 145 ARG ARG E . n 
B 1 150 ASN 150 146 146 ASN ASN E . n 
B 1 151 VAL 151 147 147 VAL VAL E . n 
B 1 152 VAL 152 148 148 VAL VAL E . n 
B 1 153 TRP 153 149 149 TRP TRP E . n 
B 1 154 LEU 154 150 150 LEU LEU E . n 
B 1 155 ILE 155 151 151 ILE ILE E . n 
B 1 156 LYS 156 152 152 LYS LYS E . n 
B 1 157 LYS 157 153 153 LYS LYS E . n 
B 1 158 ASP 158 154 154 ASP ASP E . n 
B 1 159 ASN 159 155 155 ASN ASN E . n 
B 1 160 ALA 160 156 156 ALA ALA E . n 
B 1 161 TYR 161 157 157 TYR TYR E . n 
B 1 162 PRO 162 158 158 PRO PRO E . n 
B 1 163 THR 163 159 159 THR THR E . n 
B 1 164 ILE 164 160 160 ILE ILE E . n 
B 1 165 LYS 165 161 161 LYS LYS E . n 
B 1 166 LYS 166 162 162 LYS LYS E . n 
B 1 167 GLY 167 163 163 GLY GLY E . n 
B 1 168 TYR 168 164 164 TYR TYR E . n 
B 1 169 ASN 169 165 165 ASN ASN E . n 
B 1 170 ASN 170 166 166 ASN ASN E . n 
B 1 171 THR 171 167 167 THR THR E . n 
B 1 172 ASN 172 168 168 ASN ASN E . n 
B 1 173 GLN 173 169 169 GLN GLN E . n 
B 1 174 GLU 174 170 170 GLU GLU E . n 
B 1 175 ASP 175 171 171 ASP ASP E . n 
B 1 176 LEU 176 172 172 LEU LEU E . n 
B 1 177 LEU 177 173 173 LEU LEU E . n 
B 1 178 VAL 178 174 174 VAL VAL E . n 
B 1 179 LEU 179 175 175 LEU LEU E . n 
B 1 180 TRP 180 176 176 TRP TRP E . n 
B 1 181 GLY 181 177 177 GLY GLY E . n 
B 1 182 ILE 182 178 178 ILE ILE E . n 
B 1 183 HIS 183 179 179 HIS HIS E . n 
B 1 184 HIS 184 180 180 HIS HIS E . n 
B 1 185 PRO 185 181 181 PRO PRO E . n 
B 1 186 ASN 186 182 182 ASN ASN E . n 
B 1 187 ASP 187 183 183 ASP ASP E . n 
B 1 188 GLU 188 184 184 GLU GLU E . n 
B 1 189 ALA 189 185 185 ALA ALA E . n 
B 1 190 GLU 190 186 186 GLU GLU E . n 
B 1 191 GLN 191 187 187 GLN GLN E . n 
B 1 192 THR 192 188 188 THR THR E . n 
B 1 193 ARG 193 189 189 ARG ARG E . n 
B 1 194 LEU 194 190 190 LEU LEU E . n 
B 1 195 TYR 195 191 191 TYR TYR E . n 
B 1 196 GLN 196 192 192 GLN GLN E . n 
B 1 197 ASN 197 193 193 ASN ASN E . n 
B 1 198 PRO 198 194 194 PRO PRO E . n 
B 1 199 THR 199 195 195 THR THR E . n 
B 1 200 THR 200 196 196 THR THR E . n 
B 1 201 TYR 201 197 197 TYR TYR E . n 
B 1 202 ILE 202 198 198 ILE ILE E . n 
B 1 203 SER 203 199 199 SER SER E . n 
B 1 204 ILE 204 200 200 ILE ILE E . n 
B 1 205 GLY 205 201 201 GLY GLY E . n 
B 1 206 THR 206 202 202 THR THR E . n 
B 1 207 SER 207 203 203 SER SER E . n 
B 1 208 THR 208 204 204 THR THR E . n 
B 1 209 LEU 209 205 205 LEU LEU E . n 
B 1 210 ASN 210 206 206 ASN ASN E . n 
B 1 211 GLN 211 207 207 GLN GLN E . n 
B 1 212 ARG 212 208 208 ARG ARG E . n 
B 1 213 LEU 213 209 209 LEU LEU E . n 
B 1 214 VAL 214 210 210 VAL VAL E . n 
B 1 215 PRO 215 211 211 PRO PRO E . n 
B 1 216 LYS 216 212 212 LYS LYS E . n 
B 1 217 ILE 217 213 213 ILE ILE E . n 
B 1 218 ALA 218 214 214 ALA ALA E . n 
B 1 219 THR 219 215 215 THR THR E . n 
B 1 220 ARG 220 216 216 ARG ARG E . n 
B 1 221 SER 221 217 217 SER SER E . n 
B 1 222 LYS 222 218 218 LYS LYS E . n 
B 1 223 ILE 223 219 219 ILE ILE E . n 
B 1 224 ASN 224 220 220 ASN ASN E . n 
B 1 225 GLY 225 221 221 GLY GLY E . n 
B 1 226 GLN 226 222 222 GLN GLN E . n 
B 1 227 SER 227 223 223 SER SER E . n 
B 1 228 GLY 228 224 224 GLY GLY E . n 
B 1 229 ARG 229 225 225 ARG ARG E . n 
B 1 230 ILE 230 226 226 ILE ILE E . n 
B 1 231 ASP 231 227 227 ASP ASP E . n 
B 1 232 PHE 232 228 228 PHE PHE E . n 
B 1 233 PHE 233 229 229 PHE PHE E . n 
B 1 234 TRP 234 230 230 TRP TRP E . n 
B 1 235 THR 235 231 231 THR THR E . n 
B 1 236 ILE 236 232 232 ILE ILE E . n 
B 1 237 LEU 237 233 233 LEU LEU E . n 
B 1 238 LYS 238 234 234 LYS LYS E . n 
B 1 239 PRO 239 235 235 PRO PRO E . n 
B 1 240 ASN 240 236 236 ASN ASN E . n 
B 1 241 ASP 241 237 237 ASP ASP E . n 
B 1 242 ALA 242 238 238 ALA ALA E . n 
B 1 243 ILE 243 239 239 ILE ILE E . n 
B 1 244 HIS 244 240 240 HIS HIS E . n 
B 1 245 PHE 245 241 241 PHE PHE E . n 
B 1 246 GLU 246 242 242 GLU GLU E . n 
B 1 247 SER 247 243 243 SER SER E . n 
B 1 248 ASN 248 244 244 ASN ASN E . n 
B 1 249 GLY 249 245 245 GLY GLY E . n 
B 1 250 ASN 250 246 246 ASN ASN E . n 
B 1 251 PHE 251 247 247 PHE PHE E . n 
B 1 252 ILE 252 248 248 ILE ILE E . n 
B 1 253 ALA 253 249 249 ALA ALA E . n 
B 1 254 PRO 254 250 250 PRO PRO E . n 
B 1 255 GLU 255 251 251 GLU GLU E . n 
B 1 256 TYR 256 252 252 TYR TYR E . n 
B 1 257 ALA 257 253 253 ALA ALA E . n 
B 1 258 TYR 258 254 254 TYR TYR E . n 
B 1 259 LYS 259 255 255 LYS LYS E . n 
B 1 260 ILE 260 256 256 ILE ILE E . n 
B 1 261 VAL 261 257 257 VAL VAL E . n 
B 1 262 LYS 262 258 258 LYS LYS E . n 
B 1 263 LYS 263 259 259 LYS LYS E . n 
B 1 264 GLY 264 260 260 GLY GLY E . n 
B 1 265 ASP 265 261 261 ASP ASP E . n 
B 1 266 SER 266 262 262 SER SER E . n 
B 1 267 THR 267 263 263 THR THR E . n 
B 1 268 ILE 268 264 264 ILE ILE E . n 
B 1 269 MET 269 265 265 MET MET E . n 
B 1 270 LYS 270 266 266 LYS LYS E . n 
B 1 271 SER 271 267 267 SER SER E . n 
B 1 272 GLU 272 268 268 GLU GLU E . n 
B 1 273 VAL 273 269 269 VAL VAL E . n 
B 1 274 GLU 274 270 270 GLU GLU E . n 
B 1 275 TYR 275 271 271 TYR TYR E . n 
B 1 276 GLY 276 272 272 GLY GLY E . n 
B 1 277 ASN 277 273 273 ASN ASN E . n 
B 1 278 CYS 278 274 274 CYS CYS E . n 
B 1 279 ASN 279 275 275 ASN ASN E . n 
B 1 280 THR 280 276 276 THR THR E . n 
B 1 281 ARG 281 277 277 ARG ARG E . n 
B 1 282 CYS 282 278 278 CYS CYS E . n 
B 1 283 GLN 283 279 279 GLN GLN E . n 
B 1 284 THR 284 280 280 THR THR E . n 
B 1 285 PRO 285 281 281 PRO PRO E . n 
B 1 286 ILE 286 282 282 ILE ILE E . n 
B 1 287 GLY 287 283 283 GLY GLY E . n 
B 1 288 ALA 288 284 284 ALA ALA E . n 
B 1 289 ILE 289 285 285 ILE ILE E . n 
B 1 290 ASN 290 286 286 ASN ASN E . n 
B 1 291 SER 291 287 287 SER SER E . n 
B 1 292 SER 292 288 288 SER SER E . n 
B 1 293 MET 293 289 289 MET MET E . n 
B 1 294 PRO 294 290 290 PRO PRO E . n 
B 1 295 PHE 295 291 291 PHE PHE E . n 
B 1 296 HIS 296 292 292 HIS HIS E . n 
B 1 297 ASN 297 293 293 ASN ASN E . n 
B 1 298 ILE 298 294 294 ILE ILE E . n 
B 1 299 HIS 299 295 295 HIS HIS E . n 
B 1 300 PRO 300 296 296 PRO PRO E . n 
B 1 301 LEU 301 297 297 LEU LEU E . n 
B 1 302 THR 302 298 298 THR THR E . n 
B 1 303 ILE 303 299 299 ILE ILE E . n 
B 1 304 GLY 304 300 300 GLY GLY E . n 
B 1 305 GLU 305 301 301 GLU GLU E . n 
B 1 306 CYS 306 302 302 CYS CYS E . n 
B 1 307 PRO 307 303 303 PRO PRO E . n 
B 1 308 LYS 308 304 304 LYS LYS E . n 
B 1 309 TYR 309 305 305 TYR TYR E . n 
B 1 310 VAL 310 306 306 VAL VAL E . n 
B 1 311 LYS 311 307 307 LYS LYS E . n 
B 1 312 SER 312 308 308 SER SER E . n 
B 1 313 ASN 313 309 309 ASN ASN E . n 
B 1 314 LYS 314 310 310 LYS LYS E . n 
B 1 315 LEU 315 311 311 LEU LEU E . n 
B 1 316 VAL 316 312 312 VAL VAL E . n 
B 1 317 LEU 317 313 313 LEU LEU E . n 
B 1 318 ALA 318 314 314 ALA ALA E . n 
B 1 319 THR 319 315 315 THR THR E . n 
B 1 320 GLY 320 316 316 GLY GLY E . n 
B 1 321 LEU 321 317 317 LEU LEU E . n 
B 1 322 ARG 322 318 318 ARG ARG E . n 
B 1 323 ASN 323 319 319 ASN ASN E . n 
B 1 324 SER 324 320 320 SER SER E . n 
B 1 325 PRO 325 321 ?   ?   ?   E . n 
B 1 326 GLN 326 322 ?   ?   ?   E . n 
B 1 327 ARG 327 323 ?   ?   ?   E . n 
B 1 328 GLU 328 324 ?   ?   ?   E . n 
B 1 329 THR 329 325 ?   ?   ?   E . n 
B 1 330 ARG 330 326 ?   ?   ?   E . n 
C 2 1   GLY 1   1   ?   ?   ?   B . n 
C 2 2   LEU 2   2   ?   ?   ?   B . n 
C 2 3   PHE 3   3   ?   ?   ?   B . n 
C 2 4   GLY 4   4   ?   ?   ?   B . n 
C 2 5   ALA 5   5   ?   ?   ?   B . n 
C 2 6   ILE 6   6   ?   ?   ?   B . n 
C 2 7   ALA 7   7   ?   ?   ?   B . n 
C 2 8   GLY 8   8   ?   ?   ?   B . n 
C 2 9   PHE 9   9   ?   ?   ?   B . n 
C 2 10  ILE 10  10  10  ILE ILE B . n 
C 2 11  GLU 11  11  11  GLU GLU B . n 
C 2 12  GLY 12  12  12  GLY GLY B . n 
C 2 13  GLY 13  13  13  GLY GLY B . n 
C 2 14  TRP 14  14  14  TRP TRP B . n 
C 2 15  GLN 15  15  15  GLN GLN B . n 
C 2 16  GLY 16  16  16  GLY GLY B . n 
C 2 17  MET 17  17  17  MET MET B . n 
C 2 18  VAL 18  18  18  VAL VAL B . n 
C 2 19  ASP 19  19  19  ASP ASP B . n 
C 2 20  GLY 20  20  20  GLY GLY B . n 
C 2 21  TRP 21  21  21  TRP TRP B . n 
C 2 22  TYR 22  22  22  TYR TYR B . n 
C 2 23  GLY 23  23  23  GLY GLY B . n 
C 2 24  TYR 24  24  24  TYR TYR B . n 
C 2 25  HIS 25  25  25  HIS HIS B . n 
C 2 26  HIS 26  26  26  HIS HIS B . n 
C 2 27  SER 27  27  27  SER SER B . n 
C 2 28  ASN 28  28  28  ASN ASN B . n 
C 2 29  GLU 29  29  29  GLU GLU B . n 
C 2 30  GLN 30  30  30  GLN GLN B . n 
C 2 31  GLY 31  31  31  GLY GLY B . n 
C 2 32  SER 32  32  32  SER SER B . n 
C 2 33  GLY 33  33  33  GLY GLY B . n 
C 2 34  TYR 34  34  34  TYR TYR B . n 
C 2 35  ALA 35  35  35  ALA ALA B . n 
C 2 36  ALA 36  36  36  ALA ALA B . n 
C 2 37  ASP 37  37  37  ASP ASP B . n 
C 2 38  LYS 38  38  38  LYS LYS B . n 
C 2 39  GLU 39  39  39  GLU GLU B . n 
C 2 40  SER 40  40  40  SER SER B . n 
C 2 41  THR 41  41  41  THR THR B . n 
C 2 42  GLN 42  42  42  GLN GLN B . n 
C 2 43  LYS 43  43  43  LYS LYS B . n 
C 2 44  ALA 44  44  44  ALA ALA B . n 
C 2 45  ILE 45  45  45  ILE ILE B . n 
C 2 46  ASP 46  46  46  ASP ASP B . n 
C 2 47  GLY 47  47  47  GLY GLY B . n 
C 2 48  VAL 48  48  48  VAL VAL B . n 
C 2 49  THR 49  49  49  THR THR B . n 
C 2 50  ASN 50  50  50  ASN ASN B . n 
C 2 51  LYS 51  51  51  LYS LYS B . n 
C 2 52  VAL 52  52  52  VAL VAL B . n 
C 2 53  ASN 53  53  53  ASN ASN B . n 
C 2 54  SER 54  54  54  SER SER B . n 
C 2 55  ILE 55  55  55  ILE ILE B . n 
C 2 56  ILE 56  56  56  ILE ILE B . n 
C 2 57  ASP 57  57  57  ASP ASP B . n 
C 2 58  LYS 58  58  58  LYS LYS B . n 
C 2 59  MET 59  59  59  MET MET B . n 
C 2 60  ASN 60  60  60  ASN ASN B . n 
C 2 61  THR 61  61  61  THR THR B . n 
C 2 62  GLN 62  62  62  GLN GLN B . n 
C 2 63  PHE 63  63  63  PHE PHE B . n 
C 2 64  GLU 64  64  64  GLU GLU B . n 
C 2 65  ALA 65  65  65  ALA ALA B . n 
C 2 66  VAL 66  66  66  VAL VAL B . n 
C 2 67  GLY 67  67  67  GLY GLY B . n 
C 2 68  ARG 68  68  68  ARG ARG B . n 
C 2 69  GLU 69  69  69  GLU GLU B . n 
C 2 70  PHE 70  70  70  PHE PHE B . n 
C 2 71  ASN 71  71  71  ASN ASN B . n 
C 2 72  ASN 72  72  72  ASN ASN B . n 
C 2 73  LEU 73  73  73  LEU LEU B . n 
C 2 74  GLU 74  74  74  GLU GLU B . n 
C 2 75  ARG 75  75  75  ARG ARG B . n 
C 2 76  ARG 76  76  76  ARG ARG B . n 
C 2 77  ILE 77  77  77  ILE ILE B . n 
C 2 78  GLU 78  78  78  GLU GLU B . n 
C 2 79  ASN 79  79  79  ASN ASN B . n 
C 2 80  LEU 80  80  80  LEU LEU B . n 
C 2 81  ASN 81  81  81  ASN ASN B . n 
C 2 82  LYS 82  82  82  LYS LYS B . n 
C 2 83  LYS 83  83  83  LYS LYS B . n 
C 2 84  MET 84  84  84  MET MET B . n 
C 2 85  GLU 85  85  85  GLU GLU B . n 
C 2 86  ASP 86  86  86  ASP ASP B . n 
C 2 87  GLY 87  87  87  GLY GLY B . n 
C 2 88  PHE 88  88  88  PHE PHE B . n 
C 2 89  LEU 89  89  89  LEU LEU B . n 
C 2 90  ASP 90  90  90  ASP ASP B . n 
C 2 91  VAL 91  91  91  VAL VAL B . n 
C 2 92  TRP 92  92  92  TRP TRP B . n 
C 2 93  THR 93  93  93  THR THR B . n 
C 2 94  TYR 94  94  94  TYR TYR B . n 
C 2 95  ASN 95  95  95  ASN ASN B . n 
C 2 96  ALA 96  96  96  ALA ALA B . n 
C 2 97  GLU 97  97  97  GLU GLU B . n 
C 2 98  LEU 98  98  98  LEU LEU B . n 
C 2 99  LEU 99  99  99  LEU LEU B . n 
C 2 100 VAL 100 100 100 VAL VAL B . n 
C 2 101 LEU 101 101 101 LEU LEU B . n 
C 2 102 MET 102 102 102 MET MET B . n 
C 2 103 GLU 103 103 103 GLU GLU B . n 
C 2 104 ASN 104 104 104 ASN ASN B . n 
C 2 105 GLU 105 105 105 GLU GLU B . n 
C 2 106 ARG 106 106 106 ARG ARG B . n 
C 2 107 THR 107 107 107 THR THR B . n 
C 2 108 LEU 108 108 108 LEU LEU B . n 
C 2 109 ASP 109 109 109 ASP ASP B . n 
C 2 110 PHE 110 110 110 PHE PHE B . n 
C 2 111 HIS 111 111 111 HIS HIS B . n 
C 2 112 ASP 112 112 112 ASP ASP B . n 
C 2 113 SER 113 113 113 SER SER B . n 
C 2 114 ASN 114 114 114 ASN ASN B . n 
C 2 115 VAL 115 115 115 VAL VAL B . n 
C 2 116 ARG 116 116 116 ARG ARG B . n 
C 2 117 ASN 117 117 117 ASN ASN B . n 
C 2 118 LEU 118 118 118 LEU LEU B . n 
C 2 119 TYR 119 119 119 TYR TYR B . n 
C 2 120 ASP 120 120 120 ASP ASP B . n 
C 2 121 LYS 121 121 121 LYS LYS B . n 
C 2 122 VAL 122 122 122 VAL VAL B . n 
C 2 123 ARG 123 123 123 ARG ARG B . n 
C 2 124 LEU 124 124 124 LEU LEU B . n 
C 2 125 GLN 125 125 125 GLN GLN B . n 
C 2 126 LEU 126 126 126 LEU LEU B . n 
C 2 127 LYS 127 127 127 LYS LYS B . n 
C 2 128 ASP 128 128 128 ASP ASP B . n 
C 2 129 ASN 129 129 129 ASN ASN B . n 
C 2 130 ALA 130 130 130 ALA ALA B . n 
C 2 131 LYS 131 131 131 LYS LYS B . n 
C 2 132 GLU 132 132 132 GLU GLU B . n 
C 2 133 LEU 133 133 133 LEU LEU B . n 
C 2 134 GLY 134 134 134 GLY GLY B . n 
C 2 135 ASN 135 135 135 ASN ASN B . n 
C 2 136 GLY 136 136 136 GLY GLY B . n 
C 2 137 CYS 137 137 137 CYS CYS B . n 
C 2 138 PHE 138 138 138 PHE PHE B . n 
C 2 139 GLU 139 139 139 GLU GLU B . n 
C 2 140 PHE 140 140 140 PHE PHE B . n 
C 2 141 TYR 141 141 141 TYR TYR B . n 
C 2 142 HIS 142 142 142 HIS HIS B . n 
C 2 143 LYS 143 143 143 LYS LYS B . n 
C 2 144 CYS 144 144 144 CYS CYS B . n 
C 2 145 ASP 145 145 145 ASP ASP B . n 
C 2 146 ASN 146 146 146 ASN ASN B . n 
C 2 147 GLU 147 147 147 GLU GLU B . n 
C 2 148 CYS 148 148 148 CYS CYS B . n 
C 2 149 MET 149 149 149 MET MET B . n 
C 2 150 GLU 150 150 150 GLU GLU B . n 
C 2 151 SER 151 151 151 SER SER B . n 
C 2 152 VAL 152 152 152 VAL VAL B . n 
C 2 153 ARG 153 153 153 ARG ARG B . n 
C 2 154 ASN 154 154 154 ASN ASN B . n 
C 2 155 GLY 155 155 155 GLY GLY B . n 
C 2 156 THR 156 156 156 THR THR B . n 
C 2 157 TYR 157 157 157 TYR TYR B . n 
C 2 158 ASP 158 158 158 ASP ASP B . n 
C 2 159 TYR 159 159 159 TYR TYR B . n 
C 2 160 PRO 160 160 160 PRO PRO B . n 
C 2 161 GLN 161 161 161 GLN GLN B . n 
C 2 162 TYR 162 162 162 TYR TYR B . n 
C 2 163 SER 163 163 163 SER SER B . n 
C 2 164 GLU 164 164 164 GLU GLU B . n 
C 2 165 GLU 165 165 165 GLU GLU B . n 
C 2 166 ALA 166 166 166 ALA ALA B . n 
C 2 167 ARG 167 167 167 ARG ARG B . n 
C 2 168 LEU 168 168 168 LEU LEU B . n 
C 2 169 LYS 169 169 169 LYS LYS B . n 
C 2 170 ARG 170 170 170 ARG ARG B . n 
C 2 171 GLU 171 171 171 GLU GLU B . n 
C 2 172 GLU 172 172 172 GLU GLU B . n 
C 2 173 ILE 173 173 173 ILE ILE B . n 
C 2 174 SER 174 174 174 SER SER B . n 
C 2 175 SER 175 175 ?   ?   ?   B . n 
C 2 176 GLY 176 176 ?   ?   ?   B . n 
C 2 177 ARG 177 177 ?   ?   ?   B . n 
C 2 178 LEU 178 178 ?   ?   ?   B . n 
C 2 179 VAL 179 179 ?   ?   ?   B . n 
C 2 180 PRO 180 180 ?   ?   ?   B . n 
C 2 181 ARG 181 181 ?   ?   ?   B . n 
D 1 1   ALA 1   -3  ?   ?   ?   C . n 
D 1 2   ASP 2   -2  ?   ?   ?   C . n 
D 1 3   PRO 3   -1  ?   ?   ?   C . n 
D 1 4   GLY 4   0   0   GLY GLY C . n 
D 1 5   ASP 5   1   1   ASP ASP C . n 
D 1 6   HIS 6   2   2   HIS HIS C . n 
D 1 7   ILE 7   3   3   ILE ILE C . n 
D 1 8   CYS 8   4   4   CYS CYS C . n 
D 1 9   ILE 9   5   5   ILE ILE C . n 
D 1 10  GLY 10  6   6   GLY GLY C . n 
D 1 11  TYR 11  7   7   TYR TYR C . n 
D 1 12  HIS 12  8   8   HIS HIS C . n 
D 1 13  ALA 13  9   9   ALA ALA C . n 
D 1 14  ASN 14  10  10  ASN ASN C . n 
D 1 15  ASN 15  11  11  ASN ASN C . n 
D 1 16  SER 16  12  12  SER SER C . n 
D 1 17  THR 17  13  13  THR THR C . n 
D 1 18  GLU 18  14  14  GLU GLU C . n 
D 1 19  GLN 19  15  15  GLN GLN C . n 
D 1 20  VAL 20  16  16  VAL VAL C . n 
D 1 21  ASP 21  17  17  ASP ASP C . n 
D 1 22  THR 22  18  18  THR THR C . n 
D 1 23  ILE 23  19  19  ILE ILE C . n 
D 1 24  MET 24  20  20  MET MET C . n 
D 1 25  GLU 25  21  21  GLU GLU C . n 
D 1 26  LYS 26  22  22  LYS LYS C . n 
D 1 27  ASN 27  23  23  ASN ASN C . n 
D 1 28  VAL 28  24  24  VAL VAL C . n 
D 1 29  THR 29  25  25  THR THR C . n 
D 1 30  VAL 30  26  26  VAL VAL C . n 
D 1 31  THR 31  27  27  THR THR C . n 
D 1 32  HIS 32  28  28  HIS HIS C . n 
D 1 33  ALA 33  29  29  ALA ALA C . n 
D 1 34  GLN 34  30  30  GLN GLN C . n 
D 1 35  ASP 35  31  31  ASP ASP C . n 
D 1 36  ILE 36  32  32  ILE ILE C . n 
D 1 37  LEU 37  33  33  LEU LEU C . n 
D 1 38  GLU 38  34  34  GLU GLU C . n 
D 1 39  LYS 39  35  35  LYS LYS C . n 
D 1 40  THR 40  36  36  THR THR C . n 
D 1 41  HIS 41  37  37  HIS HIS C . n 
D 1 42  ASN 42  38  38  ASN ASN C . n 
D 1 43  GLY 43  39  39  GLY GLY C . n 
D 1 44  LYS 44  40  40  LYS LYS C . n 
D 1 45  LEU 45  41  41  LEU LEU C . n 
D 1 46  CYS 46  42  42  CYS CYS C . n 
D 1 47  ASP 47  43  43  ASP ASP C . n 
D 1 48  LEU 48  44  44  LEU LEU C . n 
D 1 49  ASN 49  45  45  ASN ASN C . n 
D 1 50  GLY 50  46  46  GLY GLY C . n 
D 1 51  VAL 51  47  47  VAL VAL C . n 
D 1 52  LYS 52  48  48  LYS LYS C . n 
D 1 53  PRO 53  49  49  PRO PRO C . n 
D 1 54  LEU 54  50  50  LEU LEU C . n 
D 1 55  ILE 55  51  51  ILE ILE C . n 
D 1 56  LEU 56  52  52  LEU LEU C . n 
D 1 57  LYS 57  53  53  LYS LYS C . n 
D 1 58  ASP 58  54  54  ASP ASP C . n 
D 1 59  CYS 59  55  55  CYS CYS C . n 
D 1 60  SER 60  56  56  SER SER C . n 
D 1 61  VAL 61  57  57  VAL VAL C . n 
D 1 62  ALA 62  58  58  ALA ALA C . n 
D 1 63  GLY 63  59  59  GLY GLY C . n 
D 1 64  TRP 64  60  60  TRP TRP C . n 
D 1 65  LEU 65  61  61  LEU LEU C . n 
D 1 66  LEU 66  62  62  LEU LEU C . n 
D 1 67  GLY 67  63  63  GLY GLY C . n 
D 1 68  ASN 68  64  64  ASN ASN C . n 
D 1 69  PRO 69  65  65  PRO PRO C . n 
D 1 70  MET 70  66  66  MET MET C . n 
D 1 71  CYS 71  67  67  CYS CYS C . n 
D 1 72  ASP 72  68  68  ASP ASP C . n 
D 1 73  GLU 73  69  69  GLU GLU C . n 
D 1 74  PHE 74  70  70  PHE PHE C . n 
D 1 75  ILE 75  71  71  ILE ILE C . n 
D 1 76  ASN 76  72  72  ASN ASN C . n 
D 1 77  VAL 77  73  73  VAL VAL C . n 
D 1 78  PRO 78  74  74  PRO PRO C . n 
D 1 79  GLU 79  75  75  GLU GLU C . n 
D 1 80  TRP 80  76  76  TRP TRP C . n 
D 1 81  SER 81  77  77  SER SER C . n 
D 1 82  TYR 82  78  78  TYR TYR C . n 
D 1 83  ILE 83  79  79  ILE ILE C . n 
D 1 84  VAL 84  80  80  VAL VAL C . n 
D 1 85  GLU 85  81  81  GLU GLU C . n 
D 1 86  LYS 86  82  82  LYS LYS C . n 
D 1 87  ALA 87  83  83  ALA ALA C . n 
D 1 88  ASN 88  84  84  ASN ASN C . n 
D 1 89  PRO 89  85  85  PRO PRO C . n 
D 1 90  ALA 90  86  86  ALA ALA C . n 
D 1 91  ASN 91  87  87  ASN ASN C . n 
D 1 92  ASP 92  88  88  ASP ASP C . n 
D 1 93  LEU 93  89  89  LEU LEU C . n 
D 1 94  CYS 94  90  90  CYS CYS C . n 
D 1 95  TYR 95  91  91  TYR TYR C . n 
D 1 96  PRO 96  92  92  PRO PRO C . n 
D 1 97  GLY 97  93  93  GLY GLY C . n 
D 1 98  ASN 98  94  94  ASN ASN C . n 
D 1 99  PHE 99  95  95  PHE PHE C . n 
D 1 100 ASN 100 96  96  ASN ASN C . n 
D 1 101 ASP 101 97  97  ASP ASP C . n 
D 1 102 TYR 102 98  98  TYR TYR C . n 
D 1 103 GLU 103 99  99  GLU GLU C . n 
D 1 104 GLU 104 100 100 GLU GLU C . n 
D 1 105 LEU 105 101 101 LEU LEU C . n 
D 1 106 LYS 106 102 102 LYS LYS C . n 
D 1 107 HIS 107 103 103 HIS HIS C . n 
D 1 108 LEU 108 104 104 LEU LEU C . n 
D 1 109 LEU 109 105 105 LEU LEU C . n 
D 1 110 SER 110 106 106 SER SER C . n 
D 1 111 ARG 111 107 107 ARG ARG C . n 
D 1 112 ILE 112 108 108 ILE ILE C . n 
D 1 113 ASN 113 109 109 ASN ASN C . n 
D 1 114 HIS 114 110 110 HIS HIS C . n 
D 1 115 PHE 115 111 111 PHE PHE C . n 
D 1 116 GLU 116 112 112 GLU GLU C . n 
D 1 117 LYS 117 113 113 LYS LYS C . n 
D 1 118 ILE 118 114 114 ILE ILE C . n 
D 1 119 GLN 119 115 115 GLN GLN C . n 
D 1 120 ILE 120 116 116 ILE ILE C . n 
D 1 121 ILE 121 117 117 ILE ILE C . n 
D 1 122 PRO 122 118 118 PRO PRO C . n 
D 1 123 LYS 123 119 119 LYS LYS C . n 
D 1 124 ASN 124 120 120 ASN ASN C . n 
D 1 125 SER 125 121 121 SER SER C . n 
D 1 126 TRP 126 122 122 TRP TRP C . n 
D 1 127 SER 127 123 123 SER SER C . n 
D 1 128 ASP 128 124 124 ASP ASP C . n 
D 1 129 HIS 129 125 125 HIS HIS C . n 
D 1 130 GLU 130 126 126 GLU GLU C . n 
D 1 131 ALA 131 127 127 ALA ALA C . n 
D 1 132 SER 132 128 128 SER SER C . n 
D 1 133 LEU 133 129 129 LEU LEU C . n 
D 1 134 GLY 134 130 130 GLY GLY C . n 
D 1 135 VAL 135 131 131 VAL VAL C . n 
D 1 136 SER 136 132 132 SER SER C . n 
D 1 137 ALA 137 133 133 ALA ALA C . n 
D 1 138 ALA 138 134 134 ALA ALA C . n 
D 1 139 CYS 139 135 135 CYS CYS C . n 
D 1 140 PRO 140 136 136 PRO PRO C . n 
D 1 141 TYR 141 137 137 TYR TYR C . n 
D 1 142 GLN 142 138 138 GLN GLN C . n 
D 1 143 GLY 143 139 139 GLY GLY C . n 
D 1 144 LYS 144 140 140 LYS LYS C . n 
D 1 145 SER 145 141 141 SER SER C . n 
D 1 146 SER 146 142 142 SER SER C . n 
D 1 147 PHE 147 143 143 PHE PHE C . n 
D 1 148 PHE 148 144 144 PHE PHE C . n 
D 1 149 ARG 149 145 145 ARG ARG C . n 
D 1 150 ASN 150 146 146 ASN ASN C . n 
D 1 151 VAL 151 147 147 VAL VAL C . n 
D 1 152 VAL 152 148 148 VAL VAL C . n 
D 1 153 TRP 153 149 149 TRP TRP C . n 
D 1 154 LEU 154 150 150 LEU LEU C . n 
D 1 155 ILE 155 151 151 ILE ILE C . n 
D 1 156 LYS 156 152 152 LYS LYS C . n 
D 1 157 LYS 157 153 153 LYS LYS C . n 
D 1 158 ASP 158 154 154 ASP ASP C . n 
D 1 159 ASN 159 155 155 ASN ASN C . n 
D 1 160 ALA 160 156 156 ALA ALA C . n 
D 1 161 TYR 161 157 157 TYR TYR C . n 
D 1 162 PRO 162 158 158 PRO PRO C . n 
D 1 163 THR 163 159 159 THR THR C . n 
D 1 164 ILE 164 160 160 ILE ILE C . n 
D 1 165 LYS 165 161 161 LYS LYS C . n 
D 1 166 LYS 166 162 162 LYS LYS C . n 
D 1 167 GLY 167 163 163 GLY GLY C . n 
D 1 168 TYR 168 164 164 TYR TYR C . n 
D 1 169 ASN 169 165 165 ASN ASN C . n 
D 1 170 ASN 170 166 166 ASN ASN C . n 
D 1 171 THR 171 167 167 THR THR C . n 
D 1 172 ASN 172 168 168 ASN ASN C . n 
D 1 173 GLN 173 169 169 GLN GLN C . n 
D 1 174 GLU 174 170 170 GLU GLU C . n 
D 1 175 ASP 175 171 171 ASP ASP C . n 
D 1 176 LEU 176 172 172 LEU LEU C . n 
D 1 177 LEU 177 173 173 LEU LEU C . n 
D 1 178 VAL 178 174 174 VAL VAL C . n 
D 1 179 LEU 179 175 175 LEU LEU C . n 
D 1 180 TRP 180 176 176 TRP TRP C . n 
D 1 181 GLY 181 177 177 GLY GLY C . n 
D 1 182 ILE 182 178 178 ILE ILE C . n 
D 1 183 HIS 183 179 179 HIS HIS C . n 
D 1 184 HIS 184 180 180 HIS HIS C . n 
D 1 185 PRO 185 181 181 PRO PRO C . n 
D 1 186 ASN 186 182 182 ASN ASN C . n 
D 1 187 ASP 187 183 183 ASP ASP C . n 
D 1 188 GLU 188 184 184 GLU GLU C . n 
D 1 189 ALA 189 185 185 ALA ALA C . n 
D 1 190 GLU 190 186 186 GLU GLU C . n 
D 1 191 GLN 191 187 187 GLN GLN C . n 
D 1 192 THR 192 188 188 THR THR C . n 
D 1 193 ARG 193 189 189 ARG ARG C . n 
D 1 194 LEU 194 190 190 LEU LEU C . n 
D 1 195 TYR 195 191 191 TYR TYR C . n 
D 1 196 GLN 196 192 192 GLN GLN C . n 
D 1 197 ASN 197 193 193 ASN ASN C . n 
D 1 198 PRO 198 194 194 PRO PRO C . n 
D 1 199 THR 199 195 195 THR THR C . n 
D 1 200 THR 200 196 196 THR THR C . n 
D 1 201 TYR 201 197 197 TYR TYR C . n 
D 1 202 ILE 202 198 198 ILE ILE C . n 
D 1 203 SER 203 199 199 SER SER C . n 
D 1 204 ILE 204 200 200 ILE ILE C . n 
D 1 205 GLY 205 201 201 GLY GLY C . n 
D 1 206 THR 206 202 202 THR THR C . n 
D 1 207 SER 207 203 203 SER SER C . n 
D 1 208 THR 208 204 204 THR THR C . n 
D 1 209 LEU 209 205 205 LEU LEU C . n 
D 1 210 ASN 210 206 206 ASN ASN C . n 
D 1 211 GLN 211 207 207 GLN GLN C . n 
D 1 212 ARG 212 208 208 ARG ARG C . n 
D 1 213 LEU 213 209 209 LEU LEU C . n 
D 1 214 VAL 214 210 210 VAL VAL C . n 
D 1 215 PRO 215 211 211 PRO PRO C . n 
D 1 216 LYS 216 212 212 LYS LYS C . n 
D 1 217 ILE 217 213 213 ILE ILE C . n 
D 1 218 ALA 218 214 214 ALA ALA C . n 
D 1 219 THR 219 215 215 THR THR C . n 
D 1 220 ARG 220 216 216 ARG ARG C . n 
D 1 221 SER 221 217 217 SER SER C . n 
D 1 222 LYS 222 218 218 LYS LYS C . n 
D 1 223 ILE 223 219 219 ILE ILE C . n 
D 1 224 ASN 224 220 220 ASN ASN C . n 
D 1 225 GLY 225 221 221 GLY GLY C . n 
D 1 226 GLN 226 222 222 GLN GLN C . n 
D 1 227 SER 227 223 223 SER SER C . n 
D 1 228 GLY 228 224 224 GLY GLY C . n 
D 1 229 ARG 229 225 225 ARG ARG C . n 
D 1 230 ILE 230 226 226 ILE ILE C . n 
D 1 231 ASP 231 227 227 ASP ASP C . n 
D 1 232 PHE 232 228 228 PHE PHE C . n 
D 1 233 PHE 233 229 229 PHE PHE C . n 
D 1 234 TRP 234 230 230 TRP TRP C . n 
D 1 235 THR 235 231 231 THR THR C . n 
D 1 236 ILE 236 232 232 ILE ILE C . n 
D 1 237 LEU 237 233 233 LEU LEU C . n 
D 1 238 LYS 238 234 234 LYS LYS C . n 
D 1 239 PRO 239 235 235 PRO PRO C . n 
D 1 240 ASN 240 236 236 ASN ASN C . n 
D 1 241 ASP 241 237 237 ASP ASP C . n 
D 1 242 ALA 242 238 238 ALA ALA C . n 
D 1 243 ILE 243 239 239 ILE ILE C . n 
D 1 244 HIS 244 240 240 HIS HIS C . n 
D 1 245 PHE 245 241 241 PHE PHE C . n 
D 1 246 GLU 246 242 242 GLU GLU C . n 
D 1 247 SER 247 243 243 SER SER C . n 
D 1 248 ASN 248 244 244 ASN ASN C . n 
D 1 249 GLY 249 245 245 GLY GLY C . n 
D 1 250 ASN 250 246 246 ASN ASN C . n 
D 1 251 PHE 251 247 247 PHE PHE C . n 
D 1 252 ILE 252 248 248 ILE ILE C . n 
D 1 253 ALA 253 249 249 ALA ALA C . n 
D 1 254 PRO 254 250 250 PRO PRO C . n 
D 1 255 GLU 255 251 251 GLU GLU C . n 
D 1 256 TYR 256 252 252 TYR TYR C . n 
D 1 257 ALA 257 253 253 ALA ALA C . n 
D 1 258 TYR 258 254 254 TYR TYR C . n 
D 1 259 LYS 259 255 255 LYS LYS C . n 
D 1 260 ILE 260 256 256 ILE ILE C . n 
D 1 261 VAL 261 257 257 VAL VAL C . n 
D 1 262 LYS 262 258 258 LYS LYS C . n 
D 1 263 LYS 263 259 259 LYS LYS C . n 
D 1 264 GLY 264 260 260 GLY GLY C . n 
D 1 265 ASP 265 261 261 ASP ASP C . n 
D 1 266 SER 266 262 262 SER SER C . n 
D 1 267 THR 267 263 263 THR THR C . n 
D 1 268 ILE 268 264 264 ILE ILE C . n 
D 1 269 MET 269 265 265 MET MET C . n 
D 1 270 LYS 270 266 266 LYS LYS C . n 
D 1 271 SER 271 267 267 SER SER C . n 
D 1 272 GLU 272 268 268 GLU GLU C . n 
D 1 273 VAL 273 269 269 VAL VAL C . n 
D 1 274 GLU 274 270 270 GLU GLU C . n 
D 1 275 TYR 275 271 271 TYR TYR C . n 
D 1 276 GLY 276 272 272 GLY GLY C . n 
D 1 277 ASN 277 273 273 ASN ASN C . n 
D 1 278 CYS 278 274 274 CYS CYS C . n 
D 1 279 ASN 279 275 275 ASN ASN C . n 
D 1 280 THR 280 276 276 THR THR C . n 
D 1 281 ARG 281 277 277 ARG ARG C . n 
D 1 282 CYS 282 278 278 CYS CYS C . n 
D 1 283 GLN 283 279 279 GLN GLN C . n 
D 1 284 THR 284 280 280 THR THR C . n 
D 1 285 PRO 285 281 281 PRO PRO C . n 
D 1 286 ILE 286 282 282 ILE ILE C . n 
D 1 287 GLY 287 283 283 GLY GLY C . n 
D 1 288 ALA 288 284 284 ALA ALA C . n 
D 1 289 ILE 289 285 285 ILE ILE C . n 
D 1 290 ASN 290 286 286 ASN ASN C . n 
D 1 291 SER 291 287 287 SER SER C . n 
D 1 292 SER 292 288 288 SER SER C . n 
D 1 293 MET 293 289 289 MET MET C . n 
D 1 294 PRO 294 290 290 PRO PRO C . n 
D 1 295 PHE 295 291 291 PHE PHE C . n 
D 1 296 HIS 296 292 292 HIS HIS C . n 
D 1 297 ASN 297 293 293 ASN ASN C . n 
D 1 298 ILE 298 294 294 ILE ILE C . n 
D 1 299 HIS 299 295 295 HIS HIS C . n 
D 1 300 PRO 300 296 296 PRO PRO C . n 
D 1 301 LEU 301 297 297 LEU LEU C . n 
D 1 302 THR 302 298 298 THR THR C . n 
D 1 303 ILE 303 299 299 ILE ILE C . n 
D 1 304 GLY 304 300 300 GLY GLY C . n 
D 1 305 GLU 305 301 301 GLU GLU C . n 
D 1 306 CYS 306 302 302 CYS CYS C . n 
D 1 307 PRO 307 303 303 PRO PRO C . n 
D 1 308 LYS 308 304 304 LYS LYS C . n 
D 1 309 TYR 309 305 305 TYR TYR C . n 
D 1 310 VAL 310 306 306 VAL VAL C . n 
D 1 311 LYS 311 307 307 LYS LYS C . n 
D 1 312 SER 312 308 308 SER SER C . n 
D 1 313 ASN 313 309 309 ASN ASN C . n 
D 1 314 LYS 314 310 310 LYS LYS C . n 
D 1 315 LEU 315 311 311 LEU LEU C . n 
D 1 316 VAL 316 312 312 VAL VAL C . n 
D 1 317 LEU 317 313 313 LEU LEU C . n 
D 1 318 ALA 318 314 314 ALA ALA C . n 
D 1 319 THR 319 315 315 THR THR C . n 
D 1 320 GLY 320 316 316 GLY GLY C . n 
D 1 321 LEU 321 317 317 LEU LEU C . n 
D 1 322 ARG 322 318 318 ARG ARG C . n 
D 1 323 ASN 323 319 319 ASN ASN C . n 
D 1 324 SER 324 320 320 SER SER C . n 
D 1 325 PRO 325 321 ?   ?   ?   C . n 
D 1 326 GLN 326 322 ?   ?   ?   C . n 
D 1 327 ARG 327 323 ?   ?   ?   C . n 
D 1 328 GLU 328 324 ?   ?   ?   C . n 
D 1 329 THR 329 325 ?   ?   ?   C . n 
D 1 330 ARG 330 326 ?   ?   ?   C . n 
E 2 1   GLY 1   1   ?   ?   ?   F . n 
E 2 2   LEU 2   2   ?   ?   ?   F . n 
E 2 3   PHE 3   3   ?   ?   ?   F . n 
E 2 4   GLY 4   4   ?   ?   ?   F . n 
E 2 5   ALA 5   5   ?   ?   ?   F . n 
E 2 6   ILE 6   6   ?   ?   ?   F . n 
E 2 7   ALA 7   7   ?   ?   ?   F . n 
E 2 8   GLY 8   8   ?   ?   ?   F . n 
E 2 9   PHE 9   9   ?   ?   ?   F . n 
E 2 10  ILE 10  10  10  ILE ILE F . n 
E 2 11  GLU 11  11  11  GLU GLU F . n 
E 2 12  GLY 12  12  12  GLY GLY F . n 
E 2 13  GLY 13  13  13  GLY GLY F . n 
E 2 14  TRP 14  14  14  TRP TRP F . n 
E 2 15  GLN 15  15  15  GLN GLN F . n 
E 2 16  GLY 16  16  16  GLY GLY F . n 
E 2 17  MET 17  17  17  MET MET F . n 
E 2 18  VAL 18  18  18  VAL VAL F . n 
E 2 19  ASP 19  19  19  ASP ASP F . n 
E 2 20  GLY 20  20  20  GLY GLY F . n 
E 2 21  TRP 21  21  21  TRP TRP F . n 
E 2 22  TYR 22  22  22  TYR TYR F . n 
E 2 23  GLY 23  23  23  GLY GLY F . n 
E 2 24  TYR 24  24  24  TYR TYR F . n 
E 2 25  HIS 25  25  25  HIS HIS F . n 
E 2 26  HIS 26  26  26  HIS HIS F . n 
E 2 27  SER 27  27  27  SER SER F . n 
E 2 28  ASN 28  28  28  ASN ASN F . n 
E 2 29  GLU 29  29  29  GLU GLU F . n 
E 2 30  GLN 30  30  30  GLN GLN F . n 
E 2 31  GLY 31  31  31  GLY GLY F . n 
E 2 32  SER 32  32  32  SER SER F . n 
E 2 33  GLY 33  33  33  GLY GLY F . n 
E 2 34  TYR 34  34  34  TYR TYR F . n 
E 2 35  ALA 35  35  35  ALA ALA F . n 
E 2 36  ALA 36  36  36  ALA ALA F . n 
E 2 37  ASP 37  37  37  ASP ASP F . n 
E 2 38  LYS 38  38  38  LYS LYS F . n 
E 2 39  GLU 39  39  39  GLU GLU F . n 
E 2 40  SER 40  40  40  SER SER F . n 
E 2 41  THR 41  41  41  THR THR F . n 
E 2 42  GLN 42  42  42  GLN GLN F . n 
E 2 43  LYS 43  43  43  LYS LYS F . n 
E 2 44  ALA 44  44  44  ALA ALA F . n 
E 2 45  ILE 45  45  45  ILE ILE F . n 
E 2 46  ASP 46  46  46  ASP ASP F . n 
E 2 47  GLY 47  47  47  GLY GLY F . n 
E 2 48  VAL 48  48  48  VAL VAL F . n 
E 2 49  THR 49  49  49  THR THR F . n 
E 2 50  ASN 50  50  50  ASN ASN F . n 
E 2 51  LYS 51  51  51  LYS LYS F . n 
E 2 52  VAL 52  52  52  VAL VAL F . n 
E 2 53  ASN 53  53  53  ASN ASN F . n 
E 2 54  SER 54  54  54  SER SER F . n 
E 2 55  ILE 55  55  55  ILE ILE F . n 
E 2 56  ILE 56  56  56  ILE ILE F . n 
E 2 57  ASP 57  57  57  ASP ASP F . n 
E 2 58  LYS 58  58  58  LYS LYS F . n 
E 2 59  MET 59  59  59  MET MET F . n 
E 2 60  ASN 60  60  60  ASN ASN F . n 
E 2 61  THR 61  61  61  THR THR F . n 
E 2 62  GLN 62  62  62  GLN GLN F . n 
E 2 63  PHE 63  63  63  PHE PHE F . n 
E 2 64  GLU 64  64  64  GLU GLU F . n 
E 2 65  ALA 65  65  65  ALA ALA F . n 
E 2 66  VAL 66  66  66  VAL VAL F . n 
E 2 67  GLY 67  67  67  GLY GLY F . n 
E 2 68  ARG 68  68  68  ARG ARG F . n 
E 2 69  GLU 69  69  69  GLU GLU F . n 
E 2 70  PHE 70  70  70  PHE PHE F . n 
E 2 71  ASN 71  71  71  ASN ASN F . n 
E 2 72  ASN 72  72  72  ASN ASN F . n 
E 2 73  LEU 73  73  73  LEU LEU F . n 
E 2 74  GLU 74  74  74  GLU GLU F . n 
E 2 75  ARG 75  75  75  ARG ARG F . n 
E 2 76  ARG 76  76  76  ARG ARG F . n 
E 2 77  ILE 77  77  77  ILE ILE F . n 
E 2 78  GLU 78  78  78  GLU GLU F . n 
E 2 79  ASN 79  79  79  ASN ASN F . n 
E 2 80  LEU 80  80  80  LEU LEU F . n 
E 2 81  ASN 81  81  81  ASN ASN F . n 
E 2 82  LYS 82  82  82  LYS LYS F . n 
E 2 83  LYS 83  83  83  LYS LYS F . n 
E 2 84  MET 84  84  84  MET MET F . n 
E 2 85  GLU 85  85  85  GLU GLU F . n 
E 2 86  ASP 86  86  86  ASP ASP F . n 
E 2 87  GLY 87  87  87  GLY GLY F . n 
E 2 88  PHE 88  88  88  PHE PHE F . n 
E 2 89  LEU 89  89  89  LEU LEU F . n 
E 2 90  ASP 90  90  90  ASP ASP F . n 
E 2 91  VAL 91  91  91  VAL VAL F . n 
E 2 92  TRP 92  92  92  TRP TRP F . n 
E 2 93  THR 93  93  93  THR THR F . n 
E 2 94  TYR 94  94  94  TYR TYR F . n 
E 2 95  ASN 95  95  95  ASN ASN F . n 
E 2 96  ALA 96  96  96  ALA ALA F . n 
E 2 97  GLU 97  97  97  GLU GLU F . n 
E 2 98  LEU 98  98  98  LEU LEU F . n 
E 2 99  LEU 99  99  99  LEU LEU F . n 
E 2 100 VAL 100 100 100 VAL VAL F . n 
E 2 101 LEU 101 101 101 LEU LEU F . n 
E 2 102 MET 102 102 102 MET MET F . n 
E 2 103 GLU 103 103 103 GLU GLU F . n 
E 2 104 ASN 104 104 104 ASN ASN F . n 
E 2 105 GLU 105 105 105 GLU GLU F . n 
E 2 106 ARG 106 106 106 ARG ARG F . n 
E 2 107 THR 107 107 107 THR THR F . n 
E 2 108 LEU 108 108 108 LEU LEU F . n 
E 2 109 ASP 109 109 109 ASP ASP F . n 
E 2 110 PHE 110 110 110 PHE PHE F . n 
E 2 111 HIS 111 111 111 HIS HIS F . n 
E 2 112 ASP 112 112 112 ASP ASP F . n 
E 2 113 SER 113 113 113 SER SER F . n 
E 2 114 ASN 114 114 114 ASN ASN F . n 
E 2 115 VAL 115 115 115 VAL VAL F . n 
E 2 116 ARG 116 116 116 ARG ARG F . n 
E 2 117 ASN 117 117 117 ASN ASN F . n 
E 2 118 LEU 118 118 118 LEU LEU F . n 
E 2 119 TYR 119 119 119 TYR TYR F . n 
E 2 120 ASP 120 120 120 ASP ASP F . n 
E 2 121 LYS 121 121 121 LYS LYS F . n 
E 2 122 VAL 122 122 122 VAL VAL F . n 
E 2 123 ARG 123 123 123 ARG ARG F . n 
E 2 124 LEU 124 124 124 LEU LEU F . n 
E 2 125 GLN 125 125 125 GLN GLN F . n 
E 2 126 LEU 126 126 126 LEU LEU F . n 
E 2 127 LYS 127 127 127 LYS LYS F . n 
E 2 128 ASP 128 128 128 ASP ASP F . n 
E 2 129 ASN 129 129 129 ASN ASN F . n 
E 2 130 ALA 130 130 130 ALA ALA F . n 
E 2 131 LYS 131 131 131 LYS LYS F . n 
E 2 132 GLU 132 132 132 GLU GLU F . n 
E 2 133 LEU 133 133 133 LEU LEU F . n 
E 2 134 GLY 134 134 134 GLY GLY F . n 
E 2 135 ASN 135 135 135 ASN ASN F . n 
E 2 136 GLY 136 136 136 GLY GLY F . n 
E 2 137 CYS 137 137 137 CYS CYS F . n 
E 2 138 PHE 138 138 138 PHE PHE F . n 
E 2 139 GLU 139 139 139 GLU GLU F . n 
E 2 140 PHE 140 140 140 PHE PHE F . n 
E 2 141 TYR 141 141 141 TYR TYR F . n 
E 2 142 HIS 142 142 142 HIS HIS F . n 
E 2 143 LYS 143 143 143 LYS LYS F . n 
E 2 144 CYS 144 144 144 CYS CYS F . n 
E 2 145 ASP 145 145 145 ASP ASP F . n 
E 2 146 ASN 146 146 146 ASN ASN F . n 
E 2 147 GLU 147 147 147 GLU GLU F . n 
E 2 148 CYS 148 148 148 CYS CYS F . n 
E 2 149 MET 149 149 149 MET MET F . n 
E 2 150 GLU 150 150 150 GLU GLU F . n 
E 2 151 SER 151 151 151 SER SER F . n 
E 2 152 VAL 152 152 152 VAL VAL F . n 
E 2 153 ARG 153 153 153 ARG ARG F . n 
E 2 154 ASN 154 154 154 ASN ASN F . n 
E 2 155 GLY 155 155 155 GLY GLY F . n 
E 2 156 THR 156 156 156 THR THR F . n 
E 2 157 TYR 157 157 157 TYR TYR F . n 
E 2 158 ASP 158 158 158 ASP ASP F . n 
E 2 159 TYR 159 159 159 TYR TYR F . n 
E 2 160 PRO 160 160 160 PRO PRO F . n 
E 2 161 GLN 161 161 161 GLN GLN F . n 
E 2 162 TYR 162 162 162 TYR TYR F . n 
E 2 163 SER 163 163 163 SER SER F . n 
E 2 164 GLU 164 164 164 GLU GLU F . n 
E 2 165 GLU 165 165 165 GLU GLU F . n 
E 2 166 ALA 166 166 166 ALA ALA F . n 
E 2 167 ARG 167 167 167 ARG ARG F . n 
E 2 168 LEU 168 168 168 LEU LEU F . n 
E 2 169 LYS 169 169 169 LYS LYS F . n 
E 2 170 ARG 170 170 170 ARG ARG F . n 
E 2 171 GLU 171 171 171 GLU GLU F . n 
E 2 172 GLU 172 172 172 GLU GLU F . n 
E 2 173 ILE 173 173 ?   ?   ?   F . n 
E 2 174 SER 174 174 ?   ?   ?   F . n 
E 2 175 SER 175 175 ?   ?   ?   F . n 
E 2 176 GLY 176 176 ?   ?   ?   F . n 
E 2 177 ARG 177 177 ?   ?   ?   F . n 
E 2 178 LEU 178 178 ?   ?   ?   F . n 
E 2 179 VAL 179 179 ?   ?   ?   F . n 
E 2 180 PRO 180 180 ?   ?   ?   F . n 
E 2 181 ARG 181 181 ?   ?   ?   F . n 
F 2 1   GLY 1   1   ?   ?   ?   D . n 
F 2 2   LEU 2   2   ?   ?   ?   D . n 
F 2 3   PHE 3   3   ?   ?   ?   D . n 
F 2 4   GLY 4   4   ?   ?   ?   D . n 
F 2 5   ALA 5   5   ?   ?   ?   D . n 
F 2 6   ILE 6   6   6   ILE ILE D . n 
F 2 7   ALA 7   7   7   ALA ALA D . n 
F 2 8   GLY 8   8   8   GLY GLY D . n 
F 2 9   PHE 9   9   9   PHE PHE D . n 
F 2 10  ILE 10  10  10  ILE ILE D . n 
F 2 11  GLU 11  11  11  GLU GLU D . n 
F 2 12  GLY 12  12  12  GLY GLY D . n 
F 2 13  GLY 13  13  13  GLY GLY D . n 
F 2 14  TRP 14  14  14  TRP TRP D . n 
F 2 15  GLN 15  15  15  GLN GLN D . n 
F 2 16  GLY 16  16  16  GLY GLY D . n 
F 2 17  MET 17  17  17  MET MET D . n 
F 2 18  VAL 18  18  18  VAL VAL D . n 
F 2 19  ASP 19  19  19  ASP ASP D . n 
F 2 20  GLY 20  20  20  GLY GLY D . n 
F 2 21  TRP 21  21  21  TRP TRP D . n 
F 2 22  TYR 22  22  22  TYR TYR D . n 
F 2 23  GLY 23  23  23  GLY GLY D . n 
F 2 24  TYR 24  24  24  TYR TYR D . n 
F 2 25  HIS 25  25  25  HIS HIS D . n 
F 2 26  HIS 26  26  26  HIS HIS D . n 
F 2 27  SER 27  27  27  SER SER D . n 
F 2 28  ASN 28  28  28  ASN ASN D . n 
F 2 29  GLU 29  29  29  GLU GLU D . n 
F 2 30  GLN 30  30  30  GLN GLN D . n 
F 2 31  GLY 31  31  31  GLY GLY D . n 
F 2 32  SER 32  32  32  SER SER D . n 
F 2 33  GLY 33  33  33  GLY GLY D . n 
F 2 34  TYR 34  34  34  TYR TYR D . n 
F 2 35  ALA 35  35  35  ALA ALA D . n 
F 2 36  ALA 36  36  36  ALA ALA D . n 
F 2 37  ASP 37  37  37  ASP ASP D . n 
F 2 38  LYS 38  38  38  LYS LYS D . n 
F 2 39  GLU 39  39  39  GLU GLU D . n 
F 2 40  SER 40  40  40  SER SER D . n 
F 2 41  THR 41  41  41  THR THR D . n 
F 2 42  GLN 42  42  42  GLN GLN D . n 
F 2 43  LYS 43  43  43  LYS LYS D . n 
F 2 44  ALA 44  44  44  ALA ALA D . n 
F 2 45  ILE 45  45  45  ILE ILE D . n 
F 2 46  ASP 46  46  46  ASP ASP D . n 
F 2 47  GLY 47  47  47  GLY GLY D . n 
F 2 48  VAL 48  48  48  VAL VAL D . n 
F 2 49  THR 49  49  49  THR THR D . n 
F 2 50  ASN 50  50  50  ASN ASN D . n 
F 2 51  LYS 51  51  51  LYS LYS D . n 
F 2 52  VAL 52  52  52  VAL VAL D . n 
F 2 53  ASN 53  53  53  ASN ASN D . n 
F 2 54  SER 54  54  54  SER SER D . n 
F 2 55  ILE 55  55  55  ILE ILE D . n 
F 2 56  ILE 56  56  56  ILE ILE D . n 
F 2 57  ASP 57  57  57  ASP ASP D . n 
F 2 58  LYS 58  58  58  LYS LYS D . n 
F 2 59  MET 59  59  59  MET MET D . n 
F 2 60  ASN 60  60  60  ASN ASN D . n 
F 2 61  THR 61  61  61  THR THR D . n 
F 2 62  GLN 62  62  62  GLN GLN D . n 
F 2 63  PHE 63  63  63  PHE PHE D . n 
F 2 64  GLU 64  64  64  GLU GLU D . n 
F 2 65  ALA 65  65  65  ALA ALA D . n 
F 2 66  VAL 66  66  66  VAL VAL D . n 
F 2 67  GLY 67  67  67  GLY GLY D . n 
F 2 68  ARG 68  68  68  ARG ARG D . n 
F 2 69  GLU 69  69  69  GLU GLU D . n 
F 2 70  PHE 70  70  70  PHE PHE D . n 
F 2 71  ASN 71  71  71  ASN ASN D . n 
F 2 72  ASN 72  72  72  ASN ASN D . n 
F 2 73  LEU 73  73  73  LEU LEU D . n 
F 2 74  GLU 74  74  74  GLU GLU D . n 
F 2 75  ARG 75  75  75  ARG ARG D . n 
F 2 76  ARG 76  76  76  ARG ARG D . n 
F 2 77  ILE 77  77  77  ILE ILE D . n 
F 2 78  GLU 78  78  78  GLU GLU D . n 
F 2 79  ASN 79  79  79  ASN ASN D . n 
F 2 80  LEU 80  80  80  LEU LEU D . n 
F 2 81  ASN 81  81  81  ASN ASN D . n 
F 2 82  LYS 82  82  82  LYS LYS D . n 
F 2 83  LYS 83  83  83  LYS LYS D . n 
F 2 84  MET 84  84  84  MET MET D . n 
F 2 85  GLU 85  85  85  GLU GLU D . n 
F 2 86  ASP 86  86  86  ASP ASP D . n 
F 2 87  GLY 87  87  87  GLY GLY D . n 
F 2 88  PHE 88  88  88  PHE PHE D . n 
F 2 89  LEU 89  89  89  LEU LEU D . n 
F 2 90  ASP 90  90  90  ASP ASP D . n 
F 2 91  VAL 91  91  91  VAL VAL D . n 
F 2 92  TRP 92  92  92  TRP TRP D . n 
F 2 93  THR 93  93  93  THR THR D . n 
F 2 94  TYR 94  94  94  TYR TYR D . n 
F 2 95  ASN 95  95  95  ASN ASN D . n 
F 2 96  ALA 96  96  96  ALA ALA D . n 
F 2 97  GLU 97  97  97  GLU GLU D . n 
F 2 98  LEU 98  98  98  LEU LEU D . n 
F 2 99  LEU 99  99  99  LEU LEU D . n 
F 2 100 VAL 100 100 100 VAL VAL D . n 
F 2 101 LEU 101 101 101 LEU LEU D . n 
F 2 102 MET 102 102 102 MET MET D . n 
F 2 103 GLU 103 103 103 GLU GLU D . n 
F 2 104 ASN 104 104 104 ASN ASN D . n 
F 2 105 GLU 105 105 105 GLU GLU D . n 
F 2 106 ARG 106 106 106 ARG ARG D . n 
F 2 107 THR 107 107 107 THR THR D . n 
F 2 108 LEU 108 108 108 LEU LEU D . n 
F 2 109 ASP 109 109 109 ASP ASP D . n 
F 2 110 PHE 110 110 110 PHE PHE D . n 
F 2 111 HIS 111 111 111 HIS HIS D . n 
F 2 112 ASP 112 112 112 ASP ASP D . n 
F 2 113 SER 113 113 113 SER SER D . n 
F 2 114 ASN 114 114 114 ASN ASN D . n 
F 2 115 VAL 115 115 115 VAL VAL D . n 
F 2 116 ARG 116 116 116 ARG ARG D . n 
F 2 117 ASN 117 117 117 ASN ASN D . n 
F 2 118 LEU 118 118 118 LEU LEU D . n 
F 2 119 TYR 119 119 119 TYR TYR D . n 
F 2 120 ASP 120 120 120 ASP ASP D . n 
F 2 121 LYS 121 121 121 LYS LYS D . n 
F 2 122 VAL 122 122 122 VAL VAL D . n 
F 2 123 ARG 123 123 123 ARG ARG D . n 
F 2 124 LEU 124 124 124 LEU LEU D . n 
F 2 125 GLN 125 125 125 GLN GLN D . n 
F 2 126 LEU 126 126 126 LEU LEU D . n 
F 2 127 LYS 127 127 127 LYS LYS D . n 
F 2 128 ASP 128 128 128 ASP ASP D . n 
F 2 129 ASN 129 129 129 ASN ASN D . n 
F 2 130 ALA 130 130 130 ALA ALA D . n 
F 2 131 LYS 131 131 131 LYS LYS D . n 
F 2 132 GLU 132 132 132 GLU GLU D . n 
F 2 133 LEU 133 133 133 LEU LEU D . n 
F 2 134 GLY 134 134 134 GLY GLY D . n 
F 2 135 ASN 135 135 135 ASN ASN D . n 
F 2 136 GLY 136 136 136 GLY GLY D . n 
F 2 137 CYS 137 137 137 CYS CYS D . n 
F 2 138 PHE 138 138 138 PHE PHE D . n 
F 2 139 GLU 139 139 139 GLU GLU D . n 
F 2 140 PHE 140 140 140 PHE PHE D . n 
F 2 141 TYR 141 141 141 TYR TYR D . n 
F 2 142 HIS 142 142 142 HIS HIS D . n 
F 2 143 LYS 143 143 143 LYS LYS D . n 
F 2 144 CYS 144 144 144 CYS CYS D . n 
F 2 145 ASP 145 145 145 ASP ASP D . n 
F 2 146 ASN 146 146 146 ASN ASN D . n 
F 2 147 GLU 147 147 147 GLU GLU D . n 
F 2 148 CYS 148 148 148 CYS CYS D . n 
F 2 149 MET 149 149 149 MET MET D . n 
F 2 150 GLU 150 150 150 GLU GLU D . n 
F 2 151 SER 151 151 151 SER SER D . n 
F 2 152 VAL 152 152 152 VAL VAL D . n 
F 2 153 ARG 153 153 153 ARG ARG D . n 
F 2 154 ASN 154 154 154 ASN ASN D . n 
F 2 155 GLY 155 155 155 GLY GLY D . n 
F 2 156 THR 156 156 156 THR THR D . n 
F 2 157 TYR 157 157 157 TYR TYR D . n 
F 2 158 ASP 158 158 158 ASP ASP D . n 
F 2 159 TYR 159 159 159 TYR TYR D . n 
F 2 160 PRO 160 160 160 PRO PRO D . n 
F 2 161 GLN 161 161 161 GLN GLN D . n 
F 2 162 TYR 162 162 162 TYR TYR D . n 
F 2 163 SER 163 163 163 SER SER D . n 
F 2 164 GLU 164 164 164 GLU GLU D . n 
F 2 165 GLU 165 165 165 GLU GLU D . n 
F 2 166 ALA 166 166 166 ALA ALA D . n 
F 2 167 ARG 167 167 167 ARG ARG D . n 
F 2 168 LEU 168 168 168 LEU LEU D . n 
F 2 169 LYS 169 169 169 LYS LYS D . n 
F 2 170 ARG 170 170 170 ARG ARG D . n 
F 2 171 GLU 171 171 171 GLU GLU D . n 
F 2 172 GLU 172 172 172 GLU GLU D . n 
F 2 173 ILE 173 173 173 ILE ILE D . n 
F 2 174 SER 174 174 174 SER SER D . n 
F 2 175 SER 175 175 175 SER SER D . n 
F 2 176 GLY 176 176 ?   ?   ?   D . n 
F 2 177 ARG 177 177 ?   ?   ?   D . n 
F 2 178 LEU 178 178 ?   ?   ?   D . n 
F 2 179 VAL 179 179 ?   ?   ?   D . n 
F 2 180 PRO 180 180 ?   ?   ?   D . n 
F 2 181 ARG 181 181 ?   ?   ?   D . n 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1  A ASN 27  A ASN 23  ? ASN 'GLYCOSYLATION SITE' 
2  D ASN 27  C ASN 23  ? ASN 'GLYCOSYLATION SITE' 
3  D ASN 15  C ASN 11  ? ASN 'GLYCOSYLATION SITE' 
4  A ASN 290 A ASN 286 ? ASN 'GLYCOSYLATION SITE' 
5  A ASN 169 A ASN 165 ? ASN 'GLYCOSYLATION SITE' 
6  C ASN 154 B ASN 154 ? ASN 'GLYCOSYLATION SITE' 
7  D ASN 169 C ASN 165 ? ASN 'GLYCOSYLATION SITE' 
8  A ASN 15  A ASN 11  ? ASN 'GLYCOSYLATION SITE' 
9  B ASN 169 E ASN 165 ? ASN 'GLYCOSYLATION SITE' 
10 E ASN 154 F ASN 154 ? ASN 'GLYCOSYLATION SITE' 
11 B ASN 27  E ASN 23  ? ASN 'GLYCOSYLATION SITE' 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA trimeric  3 
2 author_defined_assembly              ?    trimeric  3 
3 software_defined_assembly            PISA hexameric 6 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 C,E,F,O,P,T,W,Y,Z                                   
2 1 A,B,D,G,H,I,J,K,L,M,N,Q,R,S,U,V,X                   
3 1 A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 9330  ? 
1 MORE         -26   ? 
1 'SSA (A^2)'  30840 ? 
3 'ABSA (A^2)' 33900 ? 
3 MORE         -117  ? 
3 'SSA (A^2)'  62690 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2013-11-27 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined 12.0970  15.3220 57.6500 0.0362 0.5767 0.0437 0.0489  0.0375  0.0982  4.1131  0.1284 0.5765 0.1580 
1.4454 0.1434  0.0276  -0.9925 -0.0672 -0.0054 -0.0229 -0.0005 0.0179  -0.3217 -0.0047 
'X-RAY DIFFRACTION' 2 ? refined -35.4070 15.7240 29.9900 0.0698 0.3093 0.0337 0.0089  0.0398  -0.0129 11.8847 0.3510 0.4760 1.0045 
1.9702 0.3024  0.0403  -0.1709 -0.1783 0.0310  -0.0671 0.0227  0.0521  -0.0245 0.0268  
'X-RAY DIFFRACTION' 3 ? refined 23.2840  31.6930 29.3400 0.1976 0.5363 0.3149 -0.0653 0.0012  0.1605  2.7042  0.0623 0.7678 0.1309 
1.1884 0.1490  -0.2409 0.5108  0.5125  -0.0325 0.1100  0.0118  -0.1623 0.2381  0.1309  
'X-RAY DIFFRACTION' 4 ? refined -28.6080 23.9200 12.4980 0.2240 0.6094 0.2849 -0.0014 0.0231  0.1232  7.9564  1.2747 2.2757 
-2.6011 4.1643 -1.3280 -0.1094 0.0070  0.2580  -0.0339 0.0406  0.0452  -0.0930 0.0333  0.0688  
'X-RAY DIFFRACTION' 5 ? refined 23.1980  -2.7370 30.4430 0.1936 0.5051 0.4633 0.0760  -0.0758 -0.2069 3.4400  0.0194 0.5139 0.1596 
1.0536 0.0361  0.2546  0.5857  -0.8781 0.0233  0.0447  -0.0176 0.0522  0.2611  -0.2993 
'X-RAY DIFFRACTION' 6 ? refined -28.9910 3.6360  14.6430 0.2105 0.4554 0.2192 0.0357  -0.0084 -0.0179 8.5493  1.0925 3.4972 2.5339 
5.1858 1.6785  -0.1682 0.3911  0.2161  -0.1266 -0.0490 0.0773  -0.1206 0.2072  0.2173  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 A 0  ? ? A 321 ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B 10 ? ? B 174 ? ? ? ? 
'X-RAY DIFFRACTION' 3 3 E 0  ? ? E 320 ? ? ? ? 
'X-RAY DIFFRACTION' 4 4 F 10 ? ? F 172 ? ? ? ? 
'X-RAY DIFFRACTION' 5 5 C 0  ? ? C 320 ? ? ? ? 
'X-RAY DIFFRACTION' 6 6 D 6  ? ? D 175 ? ? ? ? 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
HKL-2000 'data collection' .        ? 1 
PHASER   phasing           .        ? 2 
REFMAC   refinement        5.6.0117 ? 3 
HKL-2000 'data reduction'  .        ? 4 
HKL-2000 'data scaling'    .        ? 5 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 NH1 F ARG 123 ? ? CD1 F LEU 124 ? ? 1.72 
2 1 NH2 F ARG 123 ? ? OE1 D GLU 132 ? ? 1.74 
3 1 NZ  F LYS 127 ? ? N   D GLU 132 ? ? 1.94 
4 1 NE1 D TRP 14  ? ? O   D HOH 204 ? ? 2.10 
5 1 OG1 A THR 196 ? ? OD1 A ASN 244 ? ? 2.16 
6 1 ND2 C ASN 11  ? ? C2  C NAG 403 ? ? 2.17 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LYS A 53  ? ? -14.49  -90.13  
2  1 ASN A 64  ? ? -38.18  126.11  
3  1 ASN A 72  ? ? -131.07 -68.37  
4  1 VAL A 73  ? ? 45.88   80.84   
5  1 ASP A 88  ? ? -106.08 -102.65 
6  1 TYR A 137 ? ? -104.06 -80.03  
7  1 SER A 142 ? ? -144.59 -153.91 
8  1 ASP A 154 ? ? 59.89   -109.57 
9  1 GLN A 192 ? ? 62.53   -51.47  
10 1 ASN A 246 ? ? -89.92  46.17   
11 1 SER A 262 ? ? -164.19 -150.58 
12 1 LYS E 53  ? ? -30.75  -87.78  
13 1 ASN E 64  ? ? -37.86  125.77  
14 1 PHE E 70  ? ? -81.85  47.24   
15 1 ILE E 71  ? ? -108.12 -62.23  
16 1 ASN E 72  ? ? 51.96   4.43    
17 1 ASP E 88  ? ? -105.62 -102.30 
18 1 TYR E 137 ? ? -105.61 -77.03  
19 1 SER E 142 ? ? -144.16 -154.21 
20 1 ASP E 154 ? ? 59.93   -109.62 
21 1 GLN E 192 ? ? 62.36   -51.51  
22 1 THR E 204 ? ? -158.36 -30.67  
23 1 SER E 262 ? ? -166.96 -152.72 
24 1 ASN E 273 ? ? -68.92  84.15   
25 1 LYS E 307 ? ? -106.27 78.68   
26 1 LYS B 127 ? ? 37.76   -127.13 
27 1 LYS C 53  ? ? -32.85  -86.26  
28 1 ASN C 64  ? ? -37.40  125.95  
29 1 ASP C 88  ? ? -106.04 -102.71 
30 1 TYR C 137 ? ? -102.48 -78.68  
31 1 GLN C 138 ? ? -118.86 56.40   
32 1 SER C 142 ? ? -145.26 -153.69 
33 1 ASP C 154 ? ? 59.96   -110.48 
34 1 GLN C 192 ? ? 62.87   -51.61  
35 1 SER C 262 ? ? -164.26 -150.78 
36 1 LYS C 307 ? ? -105.46 79.46   
37 1 LYS F 127 ? ? -60.15  -86.59  
38 1 ALA D 7   ? ? -74.50  -159.18 
39 1 ILE D 10  ? ? -79.20  39.64   
40 1 GLU D 11  ? ? -162.87 59.61   
41 1 LYS D 127 ? ? -76.39  -106.95 
# 
loop_
_pdbx_validate_chiral.id 
_pdbx_validate_chiral.PDB_model_num 
_pdbx_validate_chiral.auth_atom_id 
_pdbx_validate_chiral.label_alt_id 
_pdbx_validate_chiral.auth_asym_id 
_pdbx_validate_chiral.auth_comp_id 
_pdbx_validate_chiral.auth_seq_id 
_pdbx_validate_chiral.PDB_ins_code 
_pdbx_validate_chiral.details 
_pdbx_validate_chiral.omega 
1 1 C1 ? A NAG 406 ? 'WRONG HAND' . 
2 1 C1 ? E NAG 402 ? 'WRONG HAND' . 
3 1 C1 ? B NAG 201 ? 'WRONG HAND' . 
4 1 C1 ? F NAG 201 ? 'WRONG HAND' . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 D SER 175 ? CB ? F SER 175 CB 
2 1 Y 1 D SER 175 ? OG ? F SER 175 OG 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ALA -3  ? A ALA 1   
2  1 Y 1 A ASP -2  ? A ASP 2   
3  1 Y 1 A PRO -1  ? A PRO 3   
4  1 Y 1 A GLN 322 ? A GLN 326 
5  1 Y 1 A ARG 323 ? A ARG 327 
6  1 Y 1 A GLU 324 ? A GLU 328 
7  1 Y 1 A THR 325 ? A THR 329 
8  1 Y 1 A ARG 326 ? A ARG 330 
9  1 Y 1 E ALA -3  ? B ALA 1   
10 1 Y 1 E ASP -2  ? B ASP 2   
11 1 Y 1 E PRO -1  ? B PRO 3   
12 1 Y 1 E PRO 321 ? B PRO 325 
13 1 Y 1 E GLN 322 ? B GLN 326 
14 1 Y 1 E ARG 323 ? B ARG 327 
15 1 Y 1 E GLU 324 ? B GLU 328 
16 1 Y 1 E THR 325 ? B THR 329 
17 1 Y 1 E ARG 326 ? B ARG 330 
18 1 Y 1 B GLY 1   ? C GLY 1   
19 1 Y 1 B LEU 2   ? C LEU 2   
20 1 Y 1 B PHE 3   ? C PHE 3   
21 1 Y 1 B GLY 4   ? C GLY 4   
22 1 Y 1 B ALA 5   ? C ALA 5   
23 1 Y 1 B ILE 6   ? C ILE 6   
24 1 Y 1 B ALA 7   ? C ALA 7   
25 1 Y 1 B GLY 8   ? C GLY 8   
26 1 Y 1 B PHE 9   ? C PHE 9   
27 1 Y 1 B SER 175 ? C SER 175 
28 1 Y 1 B GLY 176 ? C GLY 176 
29 1 Y 1 B ARG 177 ? C ARG 177 
30 1 Y 1 B LEU 178 ? C LEU 178 
31 1 Y 1 B VAL 179 ? C VAL 179 
32 1 Y 1 B PRO 180 ? C PRO 180 
33 1 Y 1 B ARG 181 ? C ARG 181 
34 1 Y 1 C ALA -3  ? D ALA 1   
35 1 Y 1 C ASP -2  ? D ASP 2   
36 1 Y 1 C PRO -1  ? D PRO 3   
37 1 Y 1 C PRO 321 ? D PRO 325 
38 1 Y 1 C GLN 322 ? D GLN 326 
39 1 Y 1 C ARG 323 ? D ARG 327 
40 1 Y 1 C GLU 324 ? D GLU 328 
41 1 Y 1 C THR 325 ? D THR 329 
42 1 Y 1 C ARG 326 ? D ARG 330 
43 1 Y 1 F GLY 1   ? E GLY 1   
44 1 Y 1 F LEU 2   ? E LEU 2   
45 1 Y 1 F PHE 3   ? E PHE 3   
46 1 Y 1 F GLY 4   ? E GLY 4   
47 1 Y 1 F ALA 5   ? E ALA 5   
48 1 Y 1 F ILE 6   ? E ILE 6   
49 1 Y 1 F ALA 7   ? E ALA 7   
50 1 Y 1 F GLY 8   ? E GLY 8   
51 1 Y 1 F PHE 9   ? E PHE 9   
52 1 Y 1 F ILE 173 ? E ILE 173 
53 1 Y 1 F SER 174 ? E SER 174 
54 1 Y 1 F SER 175 ? E SER 175 
55 1 Y 1 F GLY 176 ? E GLY 176 
56 1 Y 1 F ARG 177 ? E ARG 177 
57 1 Y 1 F LEU 178 ? E LEU 178 
58 1 Y 1 F VAL 179 ? E VAL 179 
59 1 Y 1 F PRO 180 ? E PRO 180 
60 1 Y 1 F ARG 181 ? E ARG 181 
61 1 Y 1 D GLY 1   ? F GLY 1   
62 1 Y 1 D LEU 2   ? F LEU 2   
63 1 Y 1 D PHE 3   ? F PHE 3   
64 1 Y 1 D GLY 4   ? F GLY 4   
65 1 Y 1 D ALA 5   ? F ALA 5   
66 1 Y 1 D GLY 176 ? F GLY 176 
67 1 Y 1 D ARG 177 ? F ARG 177 
68 1 Y 1 D LEU 178 ? F LEU 178 
69 1 Y 1 D VAL 179 ? F VAL 179 
70 1 Y 1 D PRO 180 ? F PRO 180 
71 1 Y 1 D ARG 181 ? F ARG 181 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 N-ACETYL-D-GLUCOSAMINE NAG 
4 water                  HOH 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
G 3 NAG 1  401 322 NAG NAG A . 
H 3 NAG 1  402 323 NAG NAG A . 
I 3 NAG 2  403 324 NAG NAG A . 
J 3 NAG 1  404 328 NAG NAG A . 
K 3 NAG 2  405 329 NAG NAG A . 
L 3 NAG 1  406 330 NAG NAG A . 
M 3 NAG 1  401 323 NAG NAG E . 
N 3 NAG 1  402 324 NAG NAG E . 
O 3 NAG 1  201 176 NAG NAG B . 
P 3 NAG 2  202 177 NAG NAG B . 
Q 3 NAG 1  401 326 NAG NAG C . 
R 3 NAG 1  402 327 NAG NAG C . 
S 3 NAG 1  403 328 NAG NAG C . 
T 3 NAG 1  201 176 NAG NAG F . 
U 4 HOH 1  501 3   HOH HOH A . 
U 4 HOH 2  502 5   HOH HOH A . 
U 4 HOH 3  503 7   HOH HOH A . 
U 4 HOH 4  504 8   HOH HOH A . 
U 4 HOH 5  505 13  HOH HOH A . 
U 4 HOH 6  506 23  HOH HOH A . 
U 4 HOH 7  507 26  HOH HOH A . 
U 4 HOH 8  508 28  HOH HOH A . 
U 4 HOH 9  509 33  HOH HOH A . 
U 4 HOH 10 510 143 HOH HOH A . 
U 4 HOH 11 511 148 HOH HOH A . 
U 4 HOH 12 512 149 HOH HOH A . 
U 4 HOH 13 513 154 HOH HOH A . 
U 4 HOH 14 514 160 HOH HOH A . 
U 4 HOH 15 515 181 HOH HOH A . 
U 4 HOH 16 516 182 HOH HOH A . 
U 4 HOH 17 517 183 HOH HOH A . 
U 4 HOH 18 518 185 HOH HOH A . 
U 4 HOH 19 519 186 HOH HOH A . 
U 4 HOH 20 520 212 HOH HOH A . 
U 4 HOH 21 521 213 HOH HOH A . 
U 4 HOH 22 522 214 HOH HOH A . 
U 4 HOH 23 523 216 HOH HOH A . 
V 4 HOH 1  501 9   HOH HOH E . 
V 4 HOH 2  502 19  HOH HOH E . 
V 4 HOH 3  503 20  HOH HOH E . 
V 4 HOH 4  504 34  HOH HOH E . 
V 4 HOH 5  505 155 HOH HOH E . 
V 4 HOH 6  506 165 HOH HOH E . 
V 4 HOH 7  507 167 HOH HOH E . 
V 4 HOH 8  508 170 HOH HOH E . 
V 4 HOH 9  509 171 HOH HOH E . 
V 4 HOH 10 510 203 HOH HOH E . 
V 4 HOH 11 511 204 HOH HOH E . 
V 4 HOH 12 512 205 HOH HOH E . 
V 4 HOH 13 513 206 HOH HOH E . 
W 4 HOH 1  301 4   HOH HOH B . 
W 4 HOH 2  302 24  HOH HOH B . 
W 4 HOH 3  303 35  HOH HOH B . 
W 4 HOH 4  304 144 HOH HOH B . 
W 4 HOH 5  305 168 HOH HOH B . 
W 4 HOH 6  306 207 HOH HOH B . 
W 4 HOH 7  307 217 HOH HOH B . 
X 4 HOH 1  501 10  HOH HOH C . 
X 4 HOH 2  502 15  HOH HOH C . 
X 4 HOH 3  503 18  HOH HOH C . 
X 4 HOH 4  504 21  HOH HOH C . 
X 4 HOH 5  505 22  HOH HOH C . 
X 4 HOH 6  506 31  HOH HOH C . 
X 4 HOH 7  507 32  HOH HOH C . 
X 4 HOH 8  508 37  HOH HOH C . 
X 4 HOH 9  509 38  HOH HOH C . 
X 4 HOH 10 510 39  HOH HOH C . 
X 4 HOH 11 511 153 HOH HOH C . 
X 4 HOH 12 512 175 HOH HOH C . 
X 4 HOH 13 513 188 HOH HOH C . 
X 4 HOH 14 514 189 HOH HOH C . 
X 4 HOH 15 515 208 HOH HOH C . 
X 4 HOH 16 516 209 HOH HOH C . 
X 4 HOH 17 517 215 HOH HOH C . 
Y 4 HOH 1  301 14  HOH HOH F . 
Y 4 HOH 2  302 36  HOH HOH F . 
Y 4 HOH 3  303 190 HOH HOH F . 
Y 4 HOH 4  304 191 HOH HOH F . 
Y 4 HOH 5  305 192 HOH HOH F . 
Y 4 HOH 6  306 211 HOH HOH F . 
Z 4 HOH 1  201 27  HOH HOH D . 
Z 4 HOH 2  202 164 HOH HOH D . 
Z 4 HOH 3  203 179 HOH HOH D . 
Z 4 HOH 4  204 199 HOH HOH D . 
Z 4 HOH 5  205 218 HOH HOH D . 
Z 4 HOH 6  206 219 HOH HOH D . 
# 
